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ID        	=	 210208151045105432
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0

REMARK Date 2020-04-04 Time 14:04:58 BST +0100 (1586005498.47 s)                
REMARK PHENIX refinement                                                        
REMARK                                                                          
REMARK ****************** INPUT FILES AND LABELS ****************************** 
REMARK Reflections:                                                             
REMARK   file name      : /Users/stephenmarshall/Documents/Crystals/Vdc/25-6-201
REMARK   labels         : ['IMEAN,SIGIMEAN']                                    
REMARK R-free flags:                                                            
REMARK   file name      : /Users/stephenmarshall/Documents/Crystals/Vdc/25-6-201
REMARK   label          : FreeR_flag                                            
REMARK   test_flag_value: 0                                                     
REMARK Model file name(s):                                                      
REMARK   /Users/stephenmarshall/Documents/Crystals/Vdc/25-6-2018/ShdCD-73-28-029
REMARK                                                                          
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* 
REMARK Start: r_work = 0.2082 r_free = 0.2447 bonds = 0.004 angles = 0.729      
REMARK Final: r_work = 0.2132 r_free = 0.2498 bonds = 0.003 angles = 0.663      
REMARK ************************************************************************ 
REMARK                                                                          
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ****************** 
REMARK leading digit, like 1_, means number of macro-cycle                      
REMARK   0  : statistics at the very beginning when nothing is done yet         
REMARK   1 s: bulk solvent correction and/or (anisotropic) scaling              
REMARK   1 z: refinement of coordinates                                         
REMARK   1 p: refinement of ADPs (Atomic Displacement Parameters)               
REMARK   1 c: refinement of occupancies                                         
REMARK ------------------------------------------------------------------------ 
REMARK  stage r-work r-free bonds angles b_min b_max b_ave n_water shift        
REMARK       0    : 0.3886 0.3358 0.004  0.729  23.4 159.4  59.3 822      0.000 
REMARK       1_bss: 0.2082 0.2447 0.004  0.729  23.4 159.5  59.3 822      0.000 
REMARK   1 ttarget: 0.2082 0.2447 0.004  0.729  23.4 159.5  59.3 822      0.000 
REMARK    1_weight: 0.2082 0.2447 0.004  0.729  23.4 159.5  59.3 822      0.000 
REMARK    1_xyzrec: 0.2048 0.2445 0.005  0.791  23.4 159.5  59.3 822      0.035 
REMARK       1_adp: 0.2121 0.2492 0.005  0.791  26.9 139.1  58.4 822      0.035 
REMARK       1_occ: 0.2121 0.2492 0.005  0.791  26.9 139.1  58.4 822      0.035 
REMARK       2_bss: 0.2121 0.2489 0.005  0.791  26.9 139.1  58.4 822      0.035 
REMARK   2 ttarget: 0.2121 0.2489 0.005  0.791  26.9 139.1  58.4 822      0.035 
REMARK   2 datecdl: 0.2121 0.2489 0.005  0.801  26.9 139.1  58.4 822      0.035 
REMARK   2 realsrl: 0.2138 0.2507 0.005  0.866  26.9 139.1  58.4 822      0.062 
REMARK    2_weight: 0.2138 0.2507 0.005  0.866  26.9 139.1  58.4 822      0.062 
REMARK    2_xyzrec: 0.2149 0.2502 0.004  0.693  26.9 139.1  58.4 822      0.062 
REMARK   2 ealsrl2: 0.2150 0.2502 0.004  0.693  26.9 139.1  58.4 822      0.062 
REMARK       2_adp: 0.2116 0.2481 0.004  0.693  25.7 153.0  59.1 822      0.062 
REMARK       2_occ: 0.2116 0.2481 0.004  0.693  25.7 153.0  59.1 822      0.062 
REMARK       3_bss: 0.2115 0.2482 0.004  0.693  25.7 153.0  59.1 822      0.062 
REMARK   3 ttarget: 0.2115 0.2482 0.004  0.693  25.7 153.0  59.1 822      0.062 
REMARK   3 datecdl: 0.2115 0.2482 0.004  0.700  25.7 153.0  59.1 822      0.062 
REMARK     3_setrh: 0.2115 0.2482 0.004  0.700  25.7 153.0  59.1 822      0.062 
REMARK   3 realsrl: 0.2126 0.2496 0.004  0.745  25.7 153.0  59.1 822      0.062 
REMARK    3_weight: 0.2126 0.2496 0.004  0.745  25.7 153.0  59.1 822      0.062 
REMARK    3_xyzrec: 0.2135 0.2498 0.003  0.663  25.7 153.0  59.1 822      0.069 
REMARK   3 ealsrl2: 0.2136 0.2499 0.003  0.663  25.7 153.0  59.1 822      0.069 
REMARK       3_adp: 0.2133 0.2499 0.003  0.663  25.5 154.3  59.2 822      0.069 
REMARK       3_occ: 0.2133 0.2499 0.003  0.663  25.5 154.3  59.2 822      0.069 
REMARK         end: 0.2132 0.2498 0.003  0.663  25.5 154.3  59.2 822      0.069 
REMARK ------------------------------------------------------------------------ 
REMARK MODEL CONTENT.                                                           
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM                        
REMARK       Zn                        6            6.00                        
REMARK        C                    16214        16197.00                        
REMARK        O                     5556         5551.00                        
REMARK        N                     4274         4265.00                        
REMARK        S                      143          143.00                        
REMARK       Rb                       12           12.00                        
REMARK    TOTAL                    26205        26174.00                        
REMARK -----------------------------------------------------------------------  
REMARK r_free_flags.md5.hexdigest 5b317b1260da3a74fd8b7ad9249cae52              
REMARK                                                                          
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.        
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.17.1_3660: ???)                            
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,       
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,   
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty, 
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini, 
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart    
REMARK   3                                                                      
REMARK   3  X-RAY DATA.                                                         
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ML                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.96                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.03                          
REMARK   3   NUMBER OF REFLECTIONS             : 197037                         
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 197037                     
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2151                          
REMARK   3   R VALUE            (WORKING SET) : 0.2132                          
REMARK   3   FREE R VALUE                     : 0.2498                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.98                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 9805                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWOR 
REMARK   3     1   70.14 -    6.80    0.99     6364   318  0.1745 0.1932   0.91 
REMARK   3     2    6.80 -    5.40    0.98     6295   335  0.1858 0.2202   0.89 
REMARK   3     3    5.40 -    4.72    0.99     6307   369  0.1763 0.2025   0.90 
REMARK   3     4    4.72 -    4.29    0.98     6371   282  0.1631 0.2070   0.91 
REMARK   3     5    4.29 -    3.98    0.97     6227   359  0.1707 0.2022   0.91 
REMARK   3     6    3.98 -    3.74    0.97     6276   303  0.1859 0.2393   0.90 
REMARK   3     7    3.74 -    3.56    0.98     6298   341  0.1950 0.2420   0.89 
REMARK   3     8    3.56 -    3.40    0.98     6241   327  0.2064 0.2417   0.87 
REMARK   3     9    3.40 -    3.27    0.98     6301   311  0.2290 0.2683   0.85 
REMARK   3    10    3.27 -    3.16    0.98     6298   301  0.2353 0.2734   0.84 
REMARK   3    11    3.16 -    3.06    0.97     6302   334  0.2309 0.2791   0.84 
REMARK   3    12    3.06 -    2.97    0.97     6231   338  0.2345 0.2863   0.85 
REMARK   3    13    2.97 -    2.89    0.97     6190   326  0.2373 0.2908   0.84 
REMARK   3    14    2.89 -    2.82    0.98     6278   340  0.2478 0.2759   0.82 
REMARK   3    15    2.82 -    2.76    0.98     6289   340  0.2544 0.2989   0.82 
REMARK   3    16    2.76 -    2.70    0.97     6187   333  0.2496 0.2646   0.83 
REMARK   3    17    2.70 -    2.65    0.96     6151   352  0.2690 0.3193   0.79 
REMARK   3    18    2.65 -    2.60    0.97     6270   341  0.2634 0.3165   0.80 
REMARK   3    19    2.60 -    2.55    0.97     6297   344  0.2630 0.3019   0.80 
REMARK   3    20    2.55 -    2.51    0.97     6241   293  0.2681 0.2993   0.79 
REMARK   3    21    2.51 -    2.47    0.97     6227   331  0.2654 0.3076   0.78 
REMARK   3    22    2.47 -    2.43    0.97     6264   318  0.2779 0.3130   0.76 
REMARK   3    23    2.43 -    2.39    0.96     6196   285  0.2803 0.3214   0.75 
REMARK   3    24    2.39 -    2.36    0.96     6176   320  0.2900 0.3078   0.75 
REMARK   3    25    2.36 -    2.33    0.96     6201   319  0.2912 0.3146   0.74 
REMARK   3    26    2.33 -    2.30    0.95     6188   315  0.2959 0.3509   0.73 
REMARK   3    27    2.30 -    2.27    0.96     6165   323  0.3073 0.3367   0.69 
REMARK   3    28    2.27 -    2.24    0.95     6064   340  0.3281 0.3486   0.63 
REMARK   3    29    2.24 -    2.21    0.96     6147   328  0.3241 0.3461   0.63 
REMARK   3    30    2.21 -    2.19    0.97     6190   339  0.3103 0.3244   0.66 
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   GRID STEP FACTOR   : 4.00                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.31             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.25            
REMARK   3                                                                      
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT                       
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2    
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3    BOND      :  0.003   0.060  25986                                 
REMARK   3    ANGLE     :  0.663  11.298  35382                                 
REMARK   3    CHIRALITY :  0.049   0.204   3935                                 
REMARK   3    PLANARITY :  0.005   0.054   4630                                 
REMARK   3    DIHEDRAL  :  7.767 179.984   3475                                 
REMARK   3    MIN NONBONDED DISTANCE : 2.199                                    
REMARK   3                                                                      
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3    ALL-ATOM CLASHSCORE : 6.44                                        
REMARK   3    RAMACHANDRAN PLOT:                                                
REMARK   3      OUTLIERS :  0.09 %                                              
REMARK   3      ALLOWED  :  3.63 %                                              
REMARK   3      FAVORED  : 96.27 %                                              
REMARK   3    ROTAMER OUTLIERS :  0.07 %                                        
REMARK   3    CBETA DEVIATIONS :  0.00 %                                        
REMARK   3    PEPTIDE PLANE:                                                    
REMARK   3      CIS-PROLINE     : 13.85 %                                       
REMARK   3      CIS-GENERAL     : 0.20 %                                        
REMARK   3      TWISTED PROLINE : 0.00 %                                        
REMARK   3      TWISTED GENERAL : 0.00 %                                        
REMARK   3                                                                      
REMARK   3                  min    max   mean    iso aniso                
REMARK   3     Overall:   25.49 154.34  59.24   3.38 26187 25383                
REMARK   3     Protein:   25.49 154.34  59.51   3.38 25365 25365                
REMARK   3     Water:     26.92  79.09  51.13    N/A   822     0                
REMARK   3     Other:     40.79  97.14  52.73    N/A     0    18                
REMARK   3     Chain  A:  28.50 149.86  62.94    N/A  4213  4213                
REMARK   3     Chain  C:  26.37 146.28  50.88    N/A  4246  4246                
REMARK   3     Chain  B:  28.27 128.92  59.02    N/A  4197  4197                
REMARK   3     Chain  E:  26.90 134.34  59.47    N/A  4230  4230                
REMARK   3     Chain  D:  25.49 154.10  59.36    N/A  4292  4292                
REMARK   3     Chain  G:  40.79  97.14  63.15    N/A     0     5                
REMARK   3     Chain  F:  26.32 154.34  65.50    N/A  4187  4187                
REMARK   3     Chain  I:  41.90  65.70  49.18    N/A     0    12                
REMARK   3     Chain  H:  43.21  43.21  43.21    N/A     0     1                
REMARK   3     Chain  S:  26.92  79.09  51.13    N/A   822     0                
REMARK   3     Histogram:                                                       
REMARK   3         Values      Number of atoms                                  
REMARK   3      25.49 - 38.37      3389                                         
REMARK   3      38.37 - 51.26      7922                                         
REMARK   3      51.26 - 64.14      6116                                         
REMARK   3      64.14 - 77.03      4065                                         
REMARK   3      77.03 - 89.91      2377                                         
REMARK   3      89.91 - 102.80     1140                                         
REMARK   3     102.80 - 115.68      676                                         
REMARK   3     115.68 - 128.57      351                                         
REMARK   3     128.57 - 141.45      117                                         
REMARK   3     141.45 - 154.34       52                                         
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 27                                           
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'B' and (resid    3  through  241 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  52.6489   6.6391   6.3145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6331 T22:   0.4270                                     
REMARK   3      T33:   0.3241 T12:   0.0924                                     
REMARK   3      T13:   0.1047 T23:  -0.0829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6269 L22:   1.2678                                     
REMARK   3      L33:   1.4777 L12:   0.5137                                     
REMARK   3      L13:   0.1897 L23:   0.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0511 S12:   0.3597 S13:  -0.3290                       
REMARK   3      S21:  -0.2382 S22:  -0.0026 S23:  -0.2441                       
REMARK   3      S31:   0.3891 S32:   0.2117 S33:  -0.0604                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'B' and (resid  242  through  667 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  45.7127  13.7299  18.2024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5075 T22:   0.2952                                     
REMARK   3      T33:   0.2631 T12:   0.0013                                     
REMARK   3      T13:   0.0462 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2554 L22:   0.9450                                     
REMARK   3      L33:   1.1103 L12:  -0.1164                                     
REMARK   3      L13:   0.1398 L23:  -0.0362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0143 S12:   0.1757 S13:  -0.1777                       
REMARK   3      S21:  -0.0965 S22:   0.0185 S23:  -0.1605                       
REMARK   3      S31:   0.2886 S32:   0.0894 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'C' and (resid    2  through  142 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9725  61.8766  71.2247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2992 T22:   0.4120                                     
REMARK   3      T33:   0.4829 T12:   0.0036                                     
REMARK   3      T13:   0.0382 T23:  -0.1729                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0781 L22:   1.3703                                     
REMARK   3      L33:   2.0539 L12:  -0.8141                                     
REMARK   3      L13:   0.4777 L23:   0.0885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0608 S12:  -0.4916 S13:   0.5413                       
REMARK   3      S21:   0.1673 S22:   0.0473 S23:   0.0193                       
REMARK   3      S31:  -0.2973 S32:  -0.2253 S33:  -0.0207                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'C' and (resid  143  through  315 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5678  50.2122  71.4744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3074 T22:   0.4841                                     
REMARK   3      T33:   0.4414 T12:  -0.0039                                     
REMARK   3      T13:   0.0524 T23:  -0.1050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1369 L22:   0.7149                                     
REMARK   3      L33:   1.3958 L12:  -0.1711                                     
REMARK   3      L13:   0.3855 L23:   0.0443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0489 S12:  -0.4817 S13:  -0.0210                       
REMARK   3      S21:   0.1765 S22:  -0.0835 S23:   0.2339                       
REMARK   3      S31:   0.0888 S32:  -0.3711 S33:   0.0348                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'C' and (resid  316  through  476 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1599  40.6948  61.9985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2759 T22:   0.3245                                     
REMARK   3      T33:   0.3080 T12:  -0.0201                                     
REMARK   3      T13:  -0.0080 T23:  -0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6260 L22:   1.4187                                     
REMARK   3      L33:   1.4827 L12:  -0.1017                                     
REMARK   3      L13:  -0.4762 L23:   0.0897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:  -0.3776 S13:   0.1700                       
REMARK   3      S21:   0.0143 S22:   0.0230 S23:  -0.1031                       
REMARK   3      S31:   0.0267 S32:   0.0758 S33:  -0.0104                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'C' and (resid  477  through  667 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4758  57.4198  52.9918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3187 T22:   0.4586                                     
REMARK   3      T33:   0.5456 T12:   0.0767                                     
REMARK   3      T13:  -0.0375 T23:  -0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3663 L22:   1.6735                                     
REMARK   3      L33:   2.2985 L12:   0.6275                                     
REMARK   3      L13:   0.6702 L23:   1.0018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1099 S12:   0.1186 S13:   0.3004                       
REMARK   3      S21:  -0.1329 S22:   0.0532 S23:   0.1576                       
REMARK   3      S31:   0.0193 S32:  -0.3632 S33:   0.1029                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'D' and (resid    3  through  124 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3760  71.2181  57.0782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3507 T22:   0.3770                                     
REMARK   3      T33:   1.1062 T12:  -0.0388                                     
REMARK   3      T13:  -0.0143 T23:  -0.2199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3834 L22:   1.7249                                     
REMARK   3      L33:   1.2058 L12:   0.0666                                     
REMARK   3      L13:   0.7108 L23:   0.3036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1850 S12:  -0.3237 S13:   1.2532                       
REMARK   3      S21:   0.1338 S22:   0.0242 S23:  -0.1637                       
REMARK   3      S31:  -0.3093 S32:   0.0110 S33:   0.1388                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'D' and (resid  125  through  156 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  58.4625  62.7085  54.5331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2744 T22:   0.4285                                     
REMARK   3      T33:   0.8639 T12:  -0.0685                                     
REMARK   3      T13:  -0.0132 T23:  -0.1041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4461 L22:   2.1625                                     
REMARK   3      L33:   1.7775 L12:  -0.2095                                     
REMARK   3      L13:   0.2890 L23:   0.0416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0407 S12:  -0.0175 S13:   0.7143                       
REMARK   3      S21:  -0.0335 S22:  -0.0038 S23:  -0.1860                       
REMARK   3      S31:  -0.2883 S32:   0.2717 S33:   0.0357                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'D' and (resid  157  through  207 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  61.9266  61.3506  43.8730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4046 T22:   0.5321                                     
REMARK   3      T33:   0.8781 T12:  -0.0513                                     
REMARK   3      T13:   0.0298 T23:   0.0790                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6131 L22:   3.8585                                     
REMARK   3      L33:   1.9061 L12:  -0.6676                                     
REMARK   3      L13:  -0.5757 L23:  -0.5367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0411 S12:   0.4168 S13:   0.6635                       
REMARK   3      S21:  -0.6719 S22:  -0.0223 S23:  -0.1327                       
REMARK   3      S31:   0.2362 S32:   0.2764 S33:   0.0675                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'D' and (resid  208  through  407 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4507  59.3844  45.8373              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2528 T22:   0.2392                                     
REMARK   3      T33:   0.6698 T12:  -0.0181                                     
REMARK   3      T13:   0.0341 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3193 L22:   0.3561                                     
REMARK   3      L33:   0.7287 L12:  -0.1900                                     
REMARK   3      L13:   0.3766 L23:   0.0664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0505 S12:   0.1561 S13:   0.9461                       
REMARK   3      S21:  -0.0148 S22:   0.0065 S23:  -0.2075                       
REMARK   3      S31:  -0.1487 S32:   0.1589 S33:   0.0450                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'D' and (resid  408  through  476 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5944  49.1603  46.1861              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3170 T22:   0.2630                                     
REMARK   3      T33:   0.3878 T12:  -0.0111                                     
REMARK   3      T13:   0.0273 T23:   0.0306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2381 L22:   1.1367                                     
REMARK   3      L33:   1.2619 L12:  -0.1726                                     
REMARK   3      L13:  -0.3553 L23:   0.5355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0834 S12:   0.1377 S13:   0.4394                       
REMARK   3      S21:  -0.0240 S22:  -0.0503 S23:   0.0297                       
REMARK   3      S31:  -0.1129 S32:  -0.1243 S33:  -0.0371                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'D' and (resid  477  through  667 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  65.8301  51.8347  62.9009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3211 T22:   0.5419                                     
REMARK   3      T33:   0.6537 T12:   0.0022                                     
REMARK   3      T13:  -0.0568 T23:  -0.1377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8513 L22:   1.4203                                     
REMARK   3      L33:   1.0315 L12:  -0.1180                                     
REMARK   3      L13:   0.0181 L23:  -0.1808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0021 S12:  -0.5695 S13:   0.5006                       
REMARK   3      S21:   0.2550 S22:   0.0081 S23:  -0.1718                       
REMARK   3      S31:  -0.0062 S32:   0.2017 S33:  -0.0784                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'E' and (resid    2  through   53 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4169 -13.2914  73.8579              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7295 T22:   0.3428                                     
REMARK   3      T33:   0.4939 T12:   0.0642                                     
REMARK   3      T13:   0.0423 T23:   0.1423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9337 L22:   2.3879                                     
REMARK   3      L33:   2.4199 L12:  -0.0329                                     
REMARK   3      L13:  -1.7214 L23:   0.5694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2213 S12:  -0.2844 S13:  -0.6507                       
REMARK   3      S21:   0.2131 S22:  -0.0894 S23:  -0.0562                       
REMARK   3      S31:   0.5656 S32:   0.3323 S33:   0.3262                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'E' and (resid   54  through  142 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9894  -4.3565  80.2543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5608 T22:   0.3916                                     
REMARK   3      T33:   0.3547 T12:   0.0362                                     
REMARK   3      T13:   0.0066 T23:   0.1212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3209 L22:   1.5180                                     
REMARK   3      L33:   2.3979 L12:  -0.3526                                     
REMARK   3      L13:  -0.6338 L23:  -0.8718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1750 S12:  -0.4965 S13:  -0.3081                       
REMARK   3      S21:   0.1582 S22:   0.0096 S23:  -0.1562                       
REMARK   3      S31:   0.3948 S32:   0.3729 S33:   0.0860                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'E' and (resid  143  through  241 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0749   7.0978  83.7356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6624 T22:   0.5488                                     
REMARK   3      T33:   0.3960 T12:  -0.0503                                     
REMARK   3      T13:  -0.0430 T23:   0.1410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7757 L22:   1.1646                                     
REMARK   3      L33:   1.8855 L12:  -0.2306                                     
REMARK   3      L13:  -0.9030 L23:   0.4808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2672 S12:  -0.4949 S13:   0.3071                       
REMARK   3      S21:   0.2557 S22:  -0.1707 S23:  -0.2437                       
REMARK   3      S31:  -0.3045 S32:   0.4690 S33:  -0.0931                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'E' and (resid  242  through  351 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  37.1442   4.5055  76.9352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4545 T22:   0.4751                                     
REMARK   3      T33:   0.3457 T12:  -0.0079                                     
REMARK   3      T13:  -0.0356 T23:   0.1114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0702 L22:   0.9008                                     
REMARK   3      L33:   1.7389 L12:  -0.1802                                     
REMARK   3      L13:   0.1055 L23:  -0.6506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0007 S12:  -0.3909 S13:  -0.0449                       
REMARK   3      S21:   0.1670 S22:  -0.1292 S23:  -0.3027                       
REMARK   3      S31:   0.1094 S32:   0.3842 S33:   0.1667                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'E' and (resid  352  through  442 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9814  17.2483  57.4931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3843 T22:   0.2459                                     
REMARK   3      T33:   0.2473 T12:  -0.0532                                     
REMARK   3      T13:   0.0087 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9607 L22:   2.2320                                     
REMARK   3      L33:   1.7184 L12:   0.1423                                     
REMARK   3      L13:  -0.0566 L23:  -0.0671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0558 S12:  -0.0865 S13:   0.0507                       
REMARK   3      S21:   0.0390 S22:   0.0159 S23:   0.0436                       
REMARK   3      S31:   0.1760 S32:  -0.0567 S33:   0.0308                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain 'E' and (resid  443  through  610 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6841   2.0458  60.9064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6569 T22:   0.5142                                     
REMARK   3      T33:   0.3548 T12:  -0.0202                                     
REMARK   3      T13:   0.0775 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5417 L22:   0.7320                                     
REMARK   3      L33:   0.7281 L12:   0.4976                                     
REMARK   3      L13:  -0.0786 L23:  -0.3797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2393 S12:  -0.3460 S13:  -0.2219                       
REMARK   3      S21:   0.0961 S22:   0.1641 S23:   0.0545                       
REMARK   3      S31:   0.2296 S32:  -0.0103 S33:   0.0892                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: chain 'E' and (resid  611  through  667 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  58.0838  -2.4407  70.3715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6277 T22:   0.8706                                     
REMARK   3      T33:   0.7711 T12:   0.1682                                     
REMARK   3      T13:   0.0666 T23:   0.2731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2450 L22:   0.9126                                     
REMARK   3      L33:   3.7425 L12:   0.6522                                     
REMARK   3      L13:  -0.7496 L23:   0.0673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0630 S12:  -0.1020 S13:  -0.1149                       
REMARK   3      S21:   0.0052 S22:  -0.0972 S23:  -0.5986                       
REMARK   3      S31:  -0.0777 S32:   1.0823 S33:   0.0936                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: chain 'F' and (resid    2  through  241 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9137  43.8661  -2.2803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5784 T22:   0.7486                                     
REMARK   3      T33:   0.3285 T12:   0.0442                                     
REMARK   3      T13:  -0.0075 T23:   0.1869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0532 L22:   1.5194                                     
REMARK   3      L33:   2.1202 L12:   0.4025                                     
REMARK   3      L13:  -0.1392 L23:  -0.6582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0415 S12:   0.4686 S13:   0.2871                       
REMARK   3      S21:  -0.3052 S22:   0.1880 S23:   0.2773                       
REMARK   3      S31:  -0.1039 S32:  -0.6754 S33:  -0.1768                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: chain 'F' and (resid  242  through  407 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1282  41.7023  11.3267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3669 T22:   0.4519                                     
REMARK   3      T33:   0.2849 T12:   0.0507                                     
REMARK   3      T13:   0.0115 T23:   0.1358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2328 L22:   0.9791                                     
REMARK   3      L33:   2.7995 L12:  -0.0763                                     
REMARK   3      L13:  -0.1780 L23:  -0.8350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0024 S12:   0.4276 S13:   0.2991                       
REMARK   3      S21:  -0.2447 S22:   0.1581 S23:   0.1349                       
REMARK   3      S31:  -0.1419 S32:  -0.5235 S33:  -0.0511                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: chain 'F' and (resid  408  through  476 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0222  31.2817  22.4640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4228 T22:   0.3090                                     
REMARK   3      T33:   0.2884 T12:  -0.0194                                     
REMARK   3      T13:   0.0648 T23:   0.0389                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7287 L22:   1.0652                                     
REMARK   3      L33:   1.1620 L12:  -0.3423                                     
REMARK   3      L13:  -0.0795 L23:   0.1414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0629 S12:   0.1159 S13:   0.2225                       
REMARK   3      S21:  -0.1766 S22:   0.0834 S23:  -0.1674                       
REMARK   3      S31:   0.1643 S32:   0.0322 S33:  -0.0312                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: chain 'F' and (resid  477  through  667 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7376  35.0778   2.6206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6485 T22:   1.5198                                     
REMARK   3      T33:   0.6410 T12:  -0.0892                                     
REMARK   3      T13:  -0.1842 T23:   0.3850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3973 L22:   1.5667                                     
REMARK   3      L33:   1.4858 L12:  -0.3627                                     
REMARK   3      L13:  -0.6871 L23:  -0.1460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:   0.4607 S13:   0.1278                       
REMARK   3      S21:  -0.1189 S22:   0.1767 S23:   0.8405                       
REMARK   3      S31:  -0.2687 S32:  -0.9759 S33:  -0.2582                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: chain 'A' and (resid    3  through   53 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3417 -15.1619  57.7510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8141 T22:   0.5419                                     
REMARK   3      T33:   0.5377 T12:  -0.2539                                     
REMARK   3      T13:   0.0328 T23:   0.1505                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0727 L22:   3.5232                                     
REMARK   3      L33:   2.3049 L12:  -1.8469                                     
REMARK   3      L13:   0.1688 L23:   0.6062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1614 S12:  -0.3708 S13:  -0.8276                       
REMARK   3      S21:   0.0747 S22:   0.1739 S23:   0.5335                       
REMARK   3      S31:   0.8038 S32:  -0.2820 S33:  -0.0452                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: chain 'A' and (resid   54  through  241 )              
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4095 -13.9501  40.4708              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7921 T22:   0.4365                                     
REMARK   3      T33:   0.4978 T12:  -0.2059                                     
REMARK   3      T13:  -0.0360 T23:  -0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8020 L22:   1.6907                                     
REMARK   3      L33:   1.1499 L12:  -0.3195                                     
REMARK   3      L13:  -0.0161 L23:   0.0414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0552 S12:   0.3320 S13:  -0.5500                       
REMARK   3      S21:  -0.2904 S22:  -0.0374 S23:   0.2912                       
REMARK   3      S31:   0.4276 S32:  -0.3187 S33:  -0.0217                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: chain 'A' and (resid  242  through  476 )              
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4236  -1.4729  43.4420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5869 T22:   0.2988                                     
REMARK   3      T33:   0.3147 T12:  -0.0729                                     
REMARK   3      T13:   0.0212 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0265 L22:   0.6083                                     
REMARK   3      L33:   0.6929 L12:  -0.2231                                     
REMARK   3      L13:  -0.0162 L23:  -0.2196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0012 S12:   0.1662 S13:  -0.2450                       
REMARK   3      S21:  -0.2164 S22:   0.0031 S23:   0.0584                       
REMARK   3      S31:   0.3458 S32:  -0.1200 S33:  -0.0050                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: chain 'A' and (resid  477  through  667 )              
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3104   2.2887  45.6395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4958 T22:   0.6984                                     
REMARK   3      T33:   0.5313 T12:  -0.1630                                     
REMARK   3      T13:   0.0234 T23:  -0.0527                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7044 L22:   3.5705                                     
REMARK   3      L33:   2.0470 L12:  -1.5852                                     
REMARK   3      L13:   1.5696 L23:  -0.9837                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0351 S12:  -0.0646 S13:  -0.0384                       
REMARK   3      S21:  -0.2240 S22:  -0.0837 S23:   0.6496                       
REMARK   3      S31:   0.2504 S32:  -0.6001 S33:   0.0119                       
REMARK   3                                                                      
HELIX    1   1 LEU B    8  GLN B   17  1                                  10    
HELIX    2   2 ASP B   33  LEU B   44  1                                  12    
HELIX    3   3 TRP B   71  MET B   77  1                                   7    
HELIX    4   4 THR B   86  TRP B   97  1                                  12    
HELIX    5   5 ARG B  109  ALA B  111  5                                   3    
HELIX    6   6 PRO B  113  LYS B  115  5                                   3    
HELIX    7   7 LEU B  125  GLU B  127  5                                   3    
HELIX    8   8 HIS B  185  ALA B  196  5                                  12    
HELIX    9   9 PRO B  211  ALA B  217  1                                   7    
HELIX   10  10 GLU B  227  LEU B  234  1                                   8    
HELIX   11  11 GLU B  316  TYR B  319  1                                   4    
HELIX   12  12 LEU B  323  THR B  336  1                                  14    
HELIX   13  13 TYR B  364  SER B  374  1                                  11    
HELIX   14  14 PRO B  376  TYR B  381  1                                   6    
HELIX   15  15 LEU B  397  ARG B  407  1                                  11    
HELIX   16  16 THR B  464  LEU B  475  1                                  12    
HELIX   17  17 GLU B  645  PHE B  647  5                                   3    
HELIX   18  18 ASP B  651  ALA B  655  1                                   5    
HELIX   19  19 LEU C    8  GLN C   17  1                                  10    
HELIX   20  20 ASP C   33  LEU C   44  1                                  12    
HELIX   21  21 TRP C   71  MET C   77  1                                   7    
HELIX   22  22 THR C   86  ARG C   96  1                                  11    
HELIX   23  23 ARG C  109  ALA C  111  5                                   3    
HELIX   24  24 PRO C  113  GLU C  116  5                                   4    
HELIX   25  25 LEU C  125  GLU C  127  5                                   3    
HELIX   26  26 ALA C  188  ALA C  196  1                                   9    
HELIX   27  27 PRO C  211  ALA C  217  1                                   7    
HELIX   28  28 GLU C  227  LEU C  234  1                                   8    
HELIX   29  29 GLU C  316  MET C  321  1                                   6    
HELIX   30  30 LEU C  323  THR C  336  1                                  14    
HELIX   31  31 TYR C  364  SER C  374  1                                  11    
HELIX   32  32 PRO C  376  TYR C  381  1                                   6    
HELIX   33  33 LEU C  397  ARG C  407  1                                  11    
HELIX   34  34 THR C  464  LYS C  476  1                                  13    
HELIX   35  35 GLU C  645  PHE C  647  5                                   3    
HELIX   36  36 ASP C  651  ALA C  655  1                                   5    
HELIX   37  37 LEU D    8  GLN D   17  1                                  10    
HELIX   38  38 ASP D   33  LEU D   44  1                                  12    
HELIX   39  39 TRP D   71  MET D   77  1                                   7    
HELIX   40  40 THR D   86  ARG D   96  1                                  11    
HELIX   41  41 PRO D  113  LYS D  115  5                                   3    
HELIX   42  42 LEU D  125  GLU D  127  5                                   3    
HELIX   43  43 ASP D  157  PHE D  159  5                                   3    
HELIX   44  44 ALA D  188  ALA D  196  1                                   9    
HELIX   45  45 PRO D  211  ALA D  217  1                                   7    
HELIX   46  46 GLU D  227  LEU D  234  1                                   8    
HELIX   47  47 GLU D  316  MET D  321  1                                   6    
HELIX   48  48 LEU D  323  THR D  336  1                                  14    
HELIX   49  49 TYR D  364  SER D  374  1                                  11    
HELIX   50  50 PRO D  376  TYR D  381  1                                   6    
HELIX   51  51 LEU D  397  ARG D  407  1                                  11    
HELIX   52  52 THR D  464  LYS D  476  1                                  13    
HELIX   53  53 GLU D  645  PHE D  647  5                                   3    
HELIX   54  54 ASP D  651  ALA D  655  1                                   5    
HELIX   55  55 LEU E    8  GLN E   17  1                                  10    
HELIX   56  56 ASP E   33  LEU E   44  1                                  12    
HELIX   57  57 TRP E   71  LEU E   78  1                                   8    
HELIX   58  58 THR E   86  ARG E   96  1                                  11    
HELIX   59  59 ARG E  109  ALA E  111  5                                   3    
HELIX   60  60 PRO E  113  LYS E  115  5                                   3    
HELIX   61  61 LEU E  125  GLU E  127  5                                   3    
HELIX   62  62 HIS E  185  ALA E  196  5                                  12    
HELIX   63  63 PRO E  211  ALA E  217  1                                   7    
HELIX   64  64 GLU E  227  LEU E  234  1                                   8    
HELIX   65  65 GLU E  316  LEU E  320  1                                   5    
HELIX   66  66 LEU E  323  THR E  336  1                                  14    
HELIX   67  67 TYR E  364  SER E  374  1                                  11    
HELIX   68  68 GLY E  378  TYR E  381  1                                   4    
HELIX   69  69 LEU E  397  ARG E  407  1                                  11    
HELIX   70  70 THR E  464  LYS E  476  1                                  13    
HELIX   71  71 GLU E  645  PHE E  647  5                                   3    
HELIX   72  72 ASP E  651  ALA E  655  1                                   5    
HELIX   73  73 LEU F    8  GLN F   17  1                                  10    
HELIX   74  74 PRO F   30  LEU F   44  1                                  15    
HELIX   75  75 TRP F   71  MET F   77  1                                   7    
HELIX   76  76 THR F   86  ARG F   96  1                                  11    
HELIX   77  77 ARG F  109  ALA F  111  5                                   3    
HELIX   78  78 PRO F  113  LYS F  115  5                                   3    
HELIX   79  79 LEU F  125  GLU F  127  5                                   3    
HELIX   80  80 HIS F  185  ALA F  196  5                                  12    
HELIX   81  81 PRO F  211  ALA F  217  1                                   7    
HELIX   82  82 GLU F  227  LEU F  234  1                                   8    
HELIX   83  83 GLU F  316  LEU F  320  1                                   5    
HELIX   84  84 LEU F  323  THR F  336  1                                  14    
HELIX   85  85 TYR F  364  SER F  374  1                                  11    
HELIX   86  86 PRO F  376  TYR F  381  1                                   6    
HELIX   87  87 LEU F  397  ARG F  407  1                                  11    
HELIX   88  88 THR F  464  LYS F  476  1                                  13    
HELIX   89  89 GLU F  645  PHE F  647  5                                   3    
HELIX   90  90 LEU A    8  GLN A   17  1                                  10    
HELIX   91  91 ASP A   33  LEU A   44  1                                  12    
HELIX   92  92 TRP A   71  MET A   77  1                                   7    
HELIX   93  93 THR A   86  ARG A   96  1                                  11    
HELIX   94  94 ARG A  109  ALA A  111  5                                   3    
HELIX   95  95 PRO A  113  LYS A  115  5                                   3    
HELIX   96  96 LEU A  125  GLU A  127  5                                   3    
HELIX   97  97 HIS A  185  ALA A  196  5                                  12    
HELIX   98  98 PRO A  211  ALA A  217  1                                   7    
HELIX   99  99 GLU A  227  LEU A  234  1                                   8    
HELIX  100 100 GLU A  316  TYR A  319  1                                   4    
HELIX  101 101 LEU A  323  THR A  336  1                                  14    
HELIX  102 102 TYR A  364  SER A  374  1                                  11    
HELIX  103 103 GLY A  378  TYR A  381  1                                   4    
HELIX  104 104 LEU A  397  ARG A  407  1                                  11    
HELIX  105 105 THR A  464  LYS A  476  1                                  13    
HELIX  106 106 GLU A  645  PHE A  647  5                                   3    
HELIX  107 107 ASP A  651  ALA A  655  1                                   5    
SHEET    1   A 4 LEU B  21  VAL B  24  0                                        
SHEET    2   A 4 ALA B  50  PHE B  53  1  N  ALA B  50   O  ILE B  22           
SHEET    3   A 4 SER B  62  THR B  65 -1  N  THR B  65   O  VAL B  51           
SHEET    4   A 4 ILE B 304  ASN B 307  1  N  PHE B 305   O  SER B  62           
SHEET    1   B 6 ASN B 117  ILE B 119  0                                        
SHEET    2   B 6 VAL B 292  HIS B 299 -1  N  HIS B 299   O  ASN B 117           
SHEET    3   B 6 VAL B 259  ILE B 265 -1  N  HIS B 264   O  LYS B 293           
SHEET    4   B 6 LEU B 201  ILE B 207 -1  N  ILE B 207   O  VAL B 259           
SHEET    5   B 6 SER B 147  THR B 150 -1  N  VAL B 149   O  ALA B 204           
SHEET    6   B 6 ASN B 163  THR B 166 -1  N  GLY B 165   O  VAL B 148           
SHEET    1   C 3 CYS B 290  LYS B 293  0                                        
SHEET    2   C 3 ARG B 176  ILE B 179 -1  N  ILE B 179   O  CYS B 290           
SHEET    3   C 3 ILE B 169  ASP B 173 -1  N  ASP B 173   O  ARG B 176           
SHEET    1   D 2 ILE B 242  LYS B 244  0                                        
SHEET    2   D 2 TYR B 252  PRO B 254 -1  N  VAL B 253   O  VAL B 243           
SHEET    1   E 2 THR B 271  GLU B 273  0                                        
SHEET    2   E 2 ARG B 287  GLN B 289 -1  N  GLN B 289   O  THR B 271           
SHEET    1   F 5 VAL B 414  ILE B 417  0                                        
SHEET    2   F 5 LYS B 437  ALA B 442 -1  N  ILE B 439   O  SER B 415           
SHEET    3   F 5 ILE B 384  VAL B 388  1  N  VAL B 385   O  MET B 438           
SHEET    4   F 5 GLY B 352  THR B 357  1  N  VAL B 353   O  ILE B 384           
SHEET    5   F 5 VAL B 340  ASN B 344 -1  N  ASN B 344   O  ILE B 354           
SHEET    1   G 3 SER B 634  ARG B 636  0                                        
SHEET    2   G 3 GLU B 624  CYS B 628 -1  N  TYR B 626   O  TRP B 635           
SHEET    3   G 3 VAL B 611  ASP B 616 -1  N  VAL B 615   O  VAL B 625           
SHEET    1   H 4 LEU C  21  VAL C  24  0                                        
SHEET    2   H 4 ALA C  50  PHE C  53  1  N  ALA C  50   O  ILE C  22           
SHEET    3   H 4 SER C  62  THR C  65 -1  N  THR C  65   O  VAL C  51           
SHEET    4   H 4 ILE C 304  GLU C 306  1  N  PHE C 305   O  SER C  62           
SHEET    1   I 6 ASN C 117  ILE C 119  0                                        
SHEET    2   I 6 VAL C 292  HIS C 299 -1  N  HIS C 299   O  ASN C 117           
SHEET    3   I 6 VAL C 259  ILE C 265 -1  N  HIS C 264   O  LYS C 293           
SHEET    4   I 6 LEU C 201  ILE C 207 -1  N  ILE C 207   O  VAL C 259           
SHEET    5   I 6 SER C 147  THR C 150 -1  N  VAL C 149   O  ALA C 204           
SHEET    6   I 6 ASN C 163  GLY C 165 -1  N  GLY C 165   O  VAL C 148           
SHEET    1   J 4 ARG C 270  GLU C 273  0                                        
SHEET    2   J 4 ARG C 287  LYS C 293 -1  N  GLN C 289   O  THR C 271           
SHEET    3   J 4 ARG C 176  ILE C 179 -1  N  ILE C 179   O  CYS C 290           
SHEET    4   J 4 ILE C 169  ASP C 173 -1  N  ASP C 173   O  ARG C 176           
SHEET    1   K 2 ILE C 242  LYS C 244  0                                        
SHEET    2   K 2 TYR C 252  PRO C 254 -1  N  VAL C 253   O  VAL C 243           
SHEET    1   L 5 VAL C 414  ILE C 417  0                                        
SHEET    2   L 5 LYS C 437  ALA C 442 -1  N  ILE C 439   O  SER C 415           
SHEET    3   L 5 ILE C 384  VAL C 388  1  N  VAL C 385   O  MET C 438           
SHEET    4   L 5 GLY C 352  THR C 357  1  N  VAL C 353   O  ILE C 384           
SHEET    5   L 5 VAL C 340  ASN C 344 -1  N  ASN C 344   O  ILE C 354           
SHEET    1   M 3 SER C 634  ARG C 636  0                                        
SHEET    2   M 3 GLU C 624  CYS C 628 -1  N  TYR C 626   O  TRP C 635           
SHEET    3   M 3 VAL C 611  ASP C 616 -1  N  VAL C 615   O  VAL C 625           
SHEET    1   N 4 LEU D  21  VAL D  24  0                                        
SHEET    2   N 4 ALA D  50  PHE D  53  1  N  ALA D  50   O  ILE D  22           
SHEET    3   N 4 SER D  62  THR D  65 -1  N  THR D  65   O  VAL D  51           
SHEET    4   N 4 ILE D 304  GLU D 306  1  N  PHE D 305   O  SER D  62           
SHEET    1   O 6 ASN D 117  ILE D 119  0                                        
SHEET    2   O 6 VAL D 292  HIS D 299 -1  N  HIS D 299   O  ASN D 117           
SHEET    3   O 6 VAL D 259  ILE D 265 -1  N  HIS D 264   O  LYS D 293           
SHEET    4   O 6 LEU D 201  ILE D 207 -1  N  ILE D 207   O  VAL D 259           
SHEET    5   O 6 SER D 147  THR D 150 -1  N  VAL D 149   O  ALA D 204           
SHEET    6   O 6 ASN D 163  THR D 166 -1  N  GLY D 165   O  VAL D 148           
SHEET    1   P 3 CYS D 290  LYS D 293  0                                        
SHEET    2   P 3 ARG D 176  ILE D 179 -1  N  ILE D 179   O  CYS D 290           
SHEET    3   P 3 GLN D 170  ASP D 173 -1  N  ASP D 173   O  ARG D 176           
SHEET    1   Q 2 ILE D 242  LYS D 244  0                                        
SHEET    2   Q 2 TYR D 252  PRO D 254 -1  N  VAL D 253   O  VAL D 243           
SHEET    1   R 2 THR D 271  GLU D 273  0                                        
SHEET    2   R 2 ARG D 287  GLN D 289 -1  N  GLN D 289   O  THR D 271           
SHEET    1   S 5 VAL D 414  ILE D 417  0                                        
SHEET    2   S 5 LYS D 437  ALA D 442 -1  N  ILE D 439   O  SER D 415           
SHEET    3   S 5 ILE D 384  VAL D 388  1  N  VAL D 385   O  MET D 438           
SHEET    4   S 5 GLY D 352  THR D 357  1  N  VAL D 353   O  ILE D 384           
SHEET    5   S 5 VAL D 340  ASN D 344 -1  N  ASN D 344   O  ILE D 354           
SHEET    1   T 3 SER D 634  ARG D 636  0                                        
SHEET    2   T 3 GLU D 624  CYS D 628 -1  N  TYR D 626   O  TRP D 635           
SHEET    3   T 3 VAL D 611  ASP D 616 -1  N  VAL D 615   O  VAL D 625           
SHEET    1   U 4 LEU E  21  VAL E  24  0                                        
SHEET    2   U 4 ALA E  50  PHE E  53  1  N  ALA E  50   O  ILE E  22           
SHEET    3   U 4 SER E  62  THR E  65 -1  N  THR E  65   O  VAL E  51           
SHEET    4   U 4 ILE E 304  GLU E 306  1  N  PHE E 305   O  SER E  62           
SHEET    1   V 6 ASN E 117  ILE E 119  0                                        
SHEET    2   V 6 VAL E 292  HIS E 299 -1  N  HIS E 299   O  ASN E 117           
SHEET    3   V 6 VAL E 259  ILE E 265 -1  N  HIS E 264   O  LYS E 293           
SHEET    4   V 6 LEU E 201  ILE E 207 -1  N  ILE E 207   O  VAL E 259           
SHEET    5   V 6 SER E 147  THR E 150 -1  N  VAL E 149   O  ALA E 204           
SHEET    6   V 6 ASN E 163  GLY E 165 -1  N  GLY E 165   O  VAL E 148           
SHEET    1   W 3 ILE E 169  VAL E 171  0                                        
SHEET    2   W 3 ARG E 176  ILE E 179 -1  N  GLY E 178   O  GLN E 170           
SHEET    3   W 3 CYS E 290  LYS E 293 -1  N  VAL E 292   O  VAL E 177           
SHEET    1   X 2 ILE E 242  LYS E 244  0                                        
SHEET    2   X 2 TYR E 252  PRO E 254 -1  N  VAL E 253   O  VAL E 243           
SHEET    1   Y 2 THR E 271  GLU E 273  0                                        
SHEET    2   Y 2 ARG E 287  GLN E 289 -1  N  GLN E 289   O  THR E 271           
SHEET    1   Z 5 VAL E 414  ILE E 417  0                                        
SHEET    2   Z 5 LYS E 437  ALA E 442 -1  N  ILE E 439   O  SER E 415           
SHEET    3   Z 5 ILE E 384  VAL E 388  1  N  VAL E 385   O  MET E 438           
SHEET    4   Z 5 GLY E 352  THR E 357  1  N  VAL E 353   O  ILE E 384           
SHEET    5   Z 5 VAL E 340  ASN E 344 -1  N  ASN E 344   O  ILE E 354           
SHEET    1  AA 3 SER E 634  ARG E 636  0                                        
SHEET    2  AA 3 GLU E 624  CYS E 628 -1  N  TYR E 626   O  TRP E 635           
SHEET    3  AA 3 VAL E 611  ASP E 616 -1  N  VAL E 615   O  VAL E 625           
SHEET    1  AB 4 LEU F  21  VAL F  24  0                                        
SHEET    2  AB 4 ALA F  50  PHE F  53  1  N  ALA F  50   O  ILE F  22           
SHEET    3  AB 4 SER F  62  THR F  65 -1  N  THR F  65   O  VAL F  51           
SHEET    4  AB 4 ILE F 304  ASN F 307  1  N  PHE F 305   O  SER F  62           
SHEET    1  AC 6 ASN F 117  ILE F 119  0                                        
SHEET    2  AC 6 VAL F 292  HIS F 299 -1  N  HIS F 299   O  ASN F 117           
SHEET    3  AC 6 VAL F 259  ILE F 265 -1  N  HIS F 264   O  LYS F 293           
SHEET    4  AC 6 LEU F 201  ILE F 207 -1  N  ILE F 207   O  VAL F 259           
SHEET    5  AC 6 SER F 147  THR F 150 -1  N  VAL F 149   O  ALA F 204           
SHEET    6  AC 6 ASN F 163  GLY F 165 -1  N  GLY F 165   O  VAL F 148           
SHEET    1  AD 2 ARG F 176  ILE F 179  0                                        
SHEET    2  AD 2 CYS F 290  LYS F 293 -1  N  VAL F 292   O  VAL F 177           
SHEET    1  AE 2 ILE F 242  LYS F 244  0                                        
SHEET    2  AE 2 TYR F 252  PRO F 254 -1  N  VAL F 253   O  VAL F 243           
SHEET    1  AF 2 THR F 271  GLU F 273  0                                        
SHEET    2  AF 2 ARG F 287  GLN F 289 -1  N  GLN F 289   O  THR F 271           
SHEET    1  AG 5 VAL F 414  ILE F 417  0                                        
SHEET    2  AG 5 LYS F 437  ALA F 442 -1  N  ILE F 439   O  SER F 415           
SHEET    3  AG 5 ILE F 384  ASP F 389  1  N  VAL F 385   O  MET F 438           
SHEET    4  AG 5 GLY F 352  THR F 357  1  N  VAL F 353   O  ILE F 384           
SHEET    5  AG 5 VAL F 340  ASN F 344 -1  N  ASN F 344   O  ILE F 354           
SHEET    1  AH 3 SER F 634  ARG F 636  0                                        
SHEET    2  AH 3 GLU F 624  CYS F 628 -1  N  TYR F 626   O  TRP F 635           
SHEET    3  AH 3 VAL F 611  ASP F 616 -1  N  VAL F 615   O  VAL F 625           
SHEET    1  AI 4 LEU A  21  VAL A  24  0                                        
SHEET    2  AI 4 ALA A  50  PHE A  53  1  N  ALA A  50   O  ILE A  22           
SHEET    3  AI 4 SER A  62  THR A  65 -1  N  THR A  65   O  VAL A  51           
SHEET    4  AI 4 ILE A 304  GLU A 306  1  N  PHE A 305   O  SER A  62           
SHEET    1  AJ 6 ASN A 117  ILE A 119  0                                        
SHEET    2  AJ 6 VAL A 292  HIS A 299 -1  N  HIS A 299   O  ASN A 117           
SHEET    3  AJ 6 VAL A 259  ILE A 265 -1  N  HIS A 264   O  LYS A 293           
SHEET    4  AJ 6 LEU A 201  ILE A 207 -1  N  ILE A 207   O  VAL A 259           
SHEET    5  AJ 6 SER A 147  THR A 150 -1  N  VAL A 149   O  ALA A 204           
SHEET    6  AJ 6 ASN A 163  GLY A 165 -1  N  GLY A 165   O  VAL A 148           
SHEET    1  AK 3 CYS A 290  LYS A 293  0                                        
SHEET    2  AK 3 ARG A 176  ILE A 179 -1  N  ILE A 179   O  CYS A 290           
SHEET    3  AK 3 GLN A 170  ASP A 173 -1  N  ASP A 173   O  ARG A 176           
SHEET    1  AL 2 ILE A 242  LYS A 244  0                                        
SHEET    2  AL 2 TYR A 252  PRO A 254 -1  N  VAL A 253   O  VAL A 243           
SHEET    1  AM 2 THR A 271  GLU A 273  0                                        
SHEET    2  AM 2 ARG A 287  GLN A 289 -1  N  GLN A 289   O  THR A 271           
SHEET    1  AN 5 VAL A 414  ILE A 417  0                                        
SHEET    2  AN 5 LYS A 437  ALA A 442 -1  N  ILE A 439   O  SER A 415           
SHEET    3  AN 5 ILE A 384  VAL A 388  1  N  VAL A 385   O  MET A 438           
SHEET    4  AN 5 GLY A 352  THR A 357  1  N  VAL A 353   O  ILE A 384           
SHEET    5  AN 5 VAL A 340  ASN A 344 -1  N  ASN A 344   O  ILE A 354           
SHEET    1  AO 3 SER A 634  ARG A 636  0                                        
SHEET    2  AO 3 GLU A 624  CYS A 628 -1  N  TYR A 626   O  TRP A 635           
SHEET    3  AO 3 VAL A 611  ASP A 616 -1  N  VAL A 615   O  VAL A 625           
LINK        ZN    ZN G   1                 SG  CYS B 603                        
LINK        ZN    ZN G   1                 SG  CYS B 606                        
LINK        ZN    ZN G   1                 SG  CYS B 628                        
LINK        ZN    ZN G   1                 SG  CYS B 631                        
LINK        ZN    ZN G   2                 SG  CYS C 606                        
LINK        ZN    ZN G   2                 SG  CYS C 628                        
LINK        ZN    ZN G   2                 SG  CYS C 603                        
LINK        ZN    ZN G   2                 SG  CYS C 631                        
LINK        ZN    ZN G   3                 SG  CYS A 603                        
LINK        ZN    ZN G   3                 SG  CYS A 606                        
LINK        ZN    ZN G   3                 SG  CYS A 631                        
LINK        ZN    ZN G   3                 SG  CYS A 628                        
LINK        ZN    ZN G   4                 CB  CYS F 606                        
LINK        ZN    ZN G   4                 SG  CYS F 603                        
LINK        ZN    ZN G   4                 SG  CYS F 606                        
LINK        ZN    ZN G   4                 SG  CYS F 631                        
LINK        ZN    ZN G   4                 SG  CYS F 628                        
LINK        ZN    ZN G   5                 SG  CYS E 603                        
LINK        ZN    ZN G   5                 SG  CYS E 606                        
LINK        ZN    ZN G   5                 SG  CYS E 628                        
LINK        ZN    ZN G   5                 SG  CYS E 631                        
LINK        ZN    ZN H   1                 SG  CYS D 603                        
LINK        ZN    ZN H   1                 SG  CYS D 606                        
LINK        ZN    ZN H   1                 SG  CYS D 631                        
LINK        ZN    ZN H   1                 SG  CYS D 628                        
LINK        RB    RB I   1                 O   HOH S   3                        
LINK        RB    RB I   1                 O   HOH S 722                        
LINK        RB    RB I   1                 O   ASP E 441                        
LINK        RB    RB I   1                 O   THR E 443                        
LINK        RB    RB I   1                 O   ARG E 407                        
LINK        RB    RB I   1                 OD2 ASP E 413                        
LINK        RB    RB I   2                 O   HOH S   2                        
LINK        RB    RB I   2                 O  AARG D 407                        
LINK        RB    RB I   2                 O   ASP D 441                        
LINK        RB    RB I   2                 OD2 ASP D 413                        
LINK        RB    RB I   2                 O   THR D 443                        
LINK        RB    RB I   2                 OD1 ASP D 413                        
LINK        RB    RB I   3                 O   HOH S 820                        
LINK        RB    RB I   3                 O   HOH S 709                        
LINK        RB    RB I   3                 O   HOH S 628                        
LINK        RB    RB I   3                 O   ARG C 407                        
LINK        RB    RB I   3                 O   THR C 443                        
LINK        RB    RB I   3                 OD2 ASP C 413                        
LINK        RB    RB I   3                 OD1 ASP C 413                        
LINK        RB    RB I   3                 O   ASP C 441                        
LINK        RB    RB I   4                 O   HOH S   1                        
LINK        RB    RB I   4                 OD2 ASP B 413                        
LINK        RB    RB I   4                 O   ARG B 407                        
LINK        RB    RB I   4                 O   THR B 443                        
LINK        RB    RB I   4                 O   ASP B 441                        
LINK        RB    RB I   5                 O   HOH S 720                        
LINK        RB    RB I   5                 O   HOH S 711                        
LINK        RB    RB I   5                 O   ASP A 441                        
LINK        RB    RB I   5                 O   THR A 443                        
LINK        RB    RB I   5                 OD2 ASP A 413                        
LINK        RB    RB I   5                 O   ARG A 407                        
LINK        RB    RB I   5                 OD1 ASP A 413                        
LINK        RB    RB I   6                 O   HOH S 466                        
LINK        RB    RB I   6                 O   HOH S 723                        
LINK        RB    RB I   6                 O   ASP F 441                        
LINK        RB    RB I   6                 O   THR F 443                        
LINK        RB    RB I   6                 O   ARG F 407                        
LINK        RB    RB I   6                 OD2 ASP F 413                        
LINK        RB    RB I   7                 OE2 GLU C 227                        
LINK        RB    RB I   7                 O   VAL C 164                        
LINK        RB    RB I   7                 OH  TYR C 223                        
LINK        RB    RB I   7                 O   THR C 219                        
LINK        RB    RB I   7                 O   MET C 216                        
LINK        RB    RB I   8                 O   HOH S 755                        
LINK        RB    RB I   8                 OH  TYR D 223                        
LINK        RB    RB I   8                 OE2 GLU D 227                        
LINK        RB    RB I   8                 O   THR D 219                        
LINK        RB    RB I   8                 O   MET D 216                        
LINK        RB    RB I   8                 O   VAL D 164                        
LINK        RB    RB I   9                 O   HOH S 728                        
LINK        RB    RB I   9                 OH  TYR E 223                        
LINK        RB    RB I   9                 O   VAL E 164                        
LINK        RB    RB I   9                 OE2 GLU E 227                        
LINK        RB    RB I   9                 O   THR E 219                        
LINK        RB    RB I   9                 O   MET E 216                        
LINK        RB    RB I  10                 OH  TYR F 223                        
LINK        RB    RB I  10                 O   VAL F 164                        
LINK        RB    RB I  10                 OE2 GLU F 227                        
LINK        RB    RB I  10                 O   MET F 216                        
LINK        RB    RB I  10                 O   THR F 219                        
LINK        RB    RB I  11                 OH  TYR A 223                        
LINK        RB    RB I  11                 O   VAL A 164                        
LINK        RB    RB I  11                 OE1 GLU A 227                        
LINK        RB    RB I  11                 O   THR A 219                        
LINK        RB    RB I  11                 O   MET A 216                        
LINK        RB    RB I  12                 O   VAL B 164                        
LINK        RB    RB I  12                 O   HOH S 717                        
LINK        RB    RB I  12                 OH  TYR B 223                        
LINK        RB    RB I  12                 OE2 GLU B 227                        
LINK        RB    RB I  12                 O   THR B 219                        
LINK        RB    RB I  12                 O   MET B 216                        
LINK         O  BARG D 407                RB    RB I   2                        
CRYST1   98.230  108.300  111.420 117.72 101.32  91.80 P 1                      
SCALE1      0.010180  0.000320  0.002500        0.00000                         
SCALE2      0.000000  0.009238  0.005067        0.00000                         
SCALE3      0.000000  0.000000  0.010440        0.00000                         
ATOM      1  N   LYS B   3      37.413   3.544  -4.704  1.00 82.31           N  
ANISOU    1  N   LYS B   3    12719  10891   7664   -273    229  -1521       N  
ATOM      2  CA  LYS B   3      38.772   3.521  -5.232  1.00 80.81           C  
ANISOU    2  CA  LYS B   3    12567  10738   7398   -175    340  -1593       C  
ATOM      3  C   LYS B   3      39.765   3.156  -4.133  1.00 78.15           C  
ANISOU    3  C   LYS B   3    12251  10198   7244    -74    426  -1602       C  
ATOM      4  O   LYS B   3      39.695   3.683  -3.024  1.00 77.47           O  
ANISOU    4  O   LYS B   3    12109  10024   7300    -50    426  -1460       O  
ATOM      5  CB  LYS B   3      39.135   4.874  -5.848  1.00 80.82           C  
ANISOU    5  CB  LYS B   3    12493  10941   7275   -138    370  -1434       C  
ATOM      6  CG  LYS B   3      38.050   5.471  -6.734  1.00 83.75           C  
ANISOU    6  CG  LYS B   3    12818  11511   7492   -233    263  -1353       C  
ATOM      7  CD  LYS B   3      38.016   4.762  -8.075  1.00 86.10           C  
ANISOU    7  CD  LYS B   3    13185  11961   7567   -294    246  -1531       C  
ATOM      8  CE  LYS B   3      37.367   5.594  -9.165  1.00 87.49           C  
ANISOU    8  CE  LYS B   3    13307  12397   7537   -364    164  -1415       C  
ATOM      9  NZ  LYS B   3      37.411   7.047  -8.847  1.00 86.85           N  
ANISOU    9  NZ  LYS B   3    13123  12364   7512   -315    164  -1149       N  
ATOM     10  N   VAL B   4      40.696   2.258  -4.454  1.00 79.22           N  
ANISOU   10  N   VAL B   4    12460  10267   7374    -13    499  -1775       N  
ATOM     11  CA  VAL B   4      41.688   1.769  -3.506  1.00 75.63           C  
ANISOU   11  CA  VAL B   4    12025   9620   7092     90    571  -1797       C  
ATOM     12  C   VAL B   4      43.073   1.939  -4.116  1.00 75.12           C  
ANISOU   12  C   VAL B   4    11952   9637   6953    202    690  -1858       C  
ATOM     13  O   VAL B   4      43.253   1.841  -5.333  1.00 78.72           O  
ANISOU   13  O   VAL B   4    12431  10249   7230    191    721  -1976       O  
ATOM     14  CB  VAL B   4      41.416   0.295  -3.115  1.00 76.70           C  
ANISOU   14  CB  VAL B   4    12254   9536   7354     60    534  -1953       C  
ATOM     15  CG1 VAL B   4      41.170  -0.541  -4.345  1.00 77.81           C  
ANISOU   15  CG1 VAL B   4    12471   9732   7362      7    518  -2176       C  
ATOM     16  CG2 VAL B   4      42.563  -0.285  -2.317  1.00 77.05           C  
ANISOU   16  CG2 VAL B   4    12320   9391   7564    181    605  -1982       C  
ATOM     17  N   TYR B   5      44.054   2.213  -3.258  1.00 69.48           N  
ANISOU   17  N   TYR B   5    11197   8836   6368    305    758  -1778       N  
ATOM     18  CA  TYR B   5      45.424   2.484  -3.672  1.00 69.30           C  
ANISOU   18  CA  TYR B   5    11139   8892   6301    414    876  -1808       C  
ATOM     19  C   TYR B   5      46.340   1.380  -3.167  1.00 69.63           C  
ANISOU   19  C   TYR B   5    11220   8740   6495    518    928  -1940       C  
ATOM     20  O   TYR B   5      46.246   0.974  -2.003  1.00 69.71           O  
ANISOU   20  O   TYR B   5    11242   8558   6688    533    886  -1885       O  
ATOM     21  CB  TYR B   5      45.880   3.845  -3.145  1.00 67.56           C  
ANISOU   21  CB  TYR B   5    10817   8746   6105    447    909  -1595       C  
ATOM     22  CG  TYR B   5      44.813   4.900  -3.286  1.00 68.25           C  
ANISOU   22  CG  TYR B   5    10862   8951   6119    351    834  -1436       C  
ATOM     23  CD1 TYR B   5      43.967   5.204  -2.227  1.00 68.56           C  
ANISOU   23  CD1 TYR B   5    10877   8889   6285    305    756  -1317       C  
ATOM     24  CD2 TYR B   5      44.637   5.578  -4.483  1.00 68.69           C  
ANISOU   24  CD2 TYR B   5    10896   9224   5979    308    838  -1404       C  
ATOM     25  CE1 TYR B   5      42.981   6.160  -2.355  1.00 68.81           C  
ANISOU   25  CE1 TYR B   5    10857   9019   6270    232    688  -1181       C  
ATOM     26  CE2 TYR B   5      43.655   6.537  -4.621  1.00 68.48           C  
ANISOU   26  CE2 TYR B   5    10822   9292   5903    230    759  -1248       C  
ATOM     27  CZ  TYR B   5      42.830   6.825  -3.554  1.00 67.47           C  
ANISOU   27  CZ  TYR B   5    10665   9047   5924    199    685  -1142       C  
ATOM     28  OH  TYR B   5      41.851   7.781  -3.691  1.00 66.80           O  
ANISOU   28  OH  TYR B   5    10521   9050   5810    136    608   -994       O  
ATOM     29  N   LYS B   6      47.217   0.889  -4.047  1.00 79.21           N  
ANISOU   29  N   LYS B   6    12451  10012   7635    591   1020  -2113       N  
ATOM     30  CA  LYS B   6      48.182  -0.136  -3.663  1.00 78.66           C  
ANISOU   30  CA  LYS B   6    12404   9762   7722    712   1076  -2246       C  
ATOM     31  C   LYS B   6      49.416   0.445  -2.990  1.00 77.09           C  
ANISOU   31  C   LYS B   6    12109   9562   7619    829   1153  -2129       C  
ATOM     32  O   LYS B   6      50.161  -0.309  -2.356  1.00 76.86           O  
ANISOU   32  O   LYS B   6    12081   9359   7763    933   1175  -2182       O  
ATOM     33  CB  LYS B   6      48.626  -0.973  -4.876  1.00 80.48           C  
ANISOU   33  CB  LYS B   6    12648  10057   7874    745   1138  -2495       C  
ATOM     34  CG  LYS B   6      47.638  -2.044  -5.329  1.00 83.04           C  
ANISOU   34  CG  LYS B   6    13060  10293   8198    655   1053  -2668       C  
ATOM     35  CD  LYS B   6      46.427  -1.396  -5.985  1.00 84.75           C  
ANISOU   35  CD  LYS B   6    13292  10696   8211    505    978  -2608       C  
ATOM     36  CE  LYS B   6      45.507  -2.402  -6.640  1.00 86.79           C  
ANISOU   36  CE  LYS B   6    13618  10919   8439    408    897  -2797       C  
ATOM     37  NZ  LYS B   6      46.246  -3.177  -7.664  1.00 90.19           N  
ANISOU   37  NZ  LYS B   6    14013  11417   8837    473    962  -3037       N  
ATOM     38  N   ASP B   7      49.642   1.753  -3.093  1.00 67.25           N  
ANISOU   38  N   ASP B   7    10777   8497   6278    811   1187  -1967       N  
ATOM     39  CA  ASP B   7      50.843   2.365  -2.541  1.00 65.69           C  
ANISOU   39  CA  ASP B   7    10479   8319   6160    907   1261  -1865       C  
ATOM     40  C   ASP B   7      50.628   3.869  -2.433  1.00 64.42           C  
ANISOU   40  C   ASP B   7    10243   8309   5926    840   1252  -1652       C  
ATOM     41  O   ASP B   7      49.550   4.390  -2.731  1.00 64.33           O  
ANISOU   41  O   ASP B   7    10254   8370   5818    734   1185  -1580       O  
ATOM     42  CB  ASP B   7      52.070   2.036  -3.396  1.00 67.55           C  
ANISOU   42  CB  ASP B   7    10677   8652   6338   1012   1392  -2019       C  
ATOM     43  CG  ASP B   7      51.855   2.332  -4.873  1.00 70.70           C  
ANISOU   43  CG  ASP B   7    11072   9290   6499    944   1438  -2098       C  
ATOM     44  OD1 ASP B   7      51.004   3.184  -5.209  1.00 71.00           O  
ANISOU   44  OD1 ASP B   7    11128   9456   6395    837   1390  -1979       O  
ATOM     45  OD2 ASP B   7      52.543   1.704  -5.704  1.00 72.55           O  
ANISOU   45  OD2 ASP B   7    11262   9599   6706    989   1512  -2273       O  
ATOM     46  N   LEU B   8      51.685   4.564  -2.011  1.00 53.00           N  
ANISOU   46  N   LEU B   8     8699   6901   4537    906   1319  -1554       N  
ATOM     47  CA  LEU B   8      51.623   6.013  -1.861  1.00 51.37           C  
ANISOU   47  CA  LEU B   8     8415   6810   4291    850   1317  -1357       C  
ATOM     48  C   LEU B   8      51.500   6.709  -3.210  1.00 54.41           C  
ANISOU   48  C   LEU B   8     8786   7423   4463    791   1362  -1340       C  
ATOM     49  O   LEU B   8      50.799   7.721  -3.329  1.00 55.29           O  
ANISOU   49  O   LEU B   8     8880   7612   4517    706   1313  -1190       O  
ATOM     50  CB  LEU B   8      52.864   6.506  -1.118  1.00 50.62           C  
ANISOU   50  CB  LEU B   8     8218   6701   4313    927   1378  -1276       C  
ATOM     51  CG  LEU B   8      53.115   8.015  -1.051  1.00 50.88           C  
ANISOU   51  CG  LEU B   8     8159   6852   4321    880   1400  -1093       C  
ATOM     52  CD1 LEU B   8      51.970   8.732  -0.356  1.00 49.59           C  
ANISOU   52  CD1 LEU B   8     8011   6628   4202    792   1297   -957       C  
ATOM     53  CD2 LEU B   8      54.439   8.308  -0.361  1.00 53.03           C  
ANISOU   53  CD2 LEU B   8     8328   7109   4711    957   1461  -1050       C  
ATOM     54  N   ARG B   9      52.174   6.184  -4.237  1.00 62.04           N  
ANISOU   54  N   ARG B   9     9758   8503   5312    835   1456  -1490       N  
ATOM     55  CA  ARG B   9      52.243   6.886  -5.514  1.00 63.21           C  
ANISOU   55  CA  ARG B   9     9881   8899   5239    778   1515  -1459       C  
ATOM     56  C   ARG B   9      50.878   6.971  -6.181  1.00 64.52           C  
ANISOU   56  C   ARG B   9    10120   9137   5258    665   1419  -1444       C  
ATOM     57  O   ARG B   9      50.560   7.978  -6.821  1.00 65.63           O  
ANISOU   57  O   ARG B   9    10228   9445   5261    589   1408  -1301       O  
ATOM     58  CB  ARG B   9      53.249   6.202  -6.438  1.00 64.76           C  
ANISOU   58  CB  ARG B   9    10058   9211   5335    847   1642  -1649       C  
ATOM     59  CG  ARG B   9      54.568   5.883  -5.766  1.00 65.34           C  
ANISOU   59  CG  ARG B   9    10055   9196   5575    976   1729  -1695       C  
ATOM     60  CD  ARG B   9      55.732   6.007  -6.729  1.00 67.16           C  
ANISOU   60  CD  ARG B   9    10173   9633   5712    998   1863  -1760       C  
ATOM     61  NE  ARG B   9      56.946   5.410  -6.181  1.00 69.54           N  
ANISOU   61  NE  ARG B   9    10399   9839   6183   1134   1939  -1854       N  
ATOM     62  CZ  ARG B   9      58.176   5.850  -6.429  1.00 72.50           C  
ANISOU   62  CZ  ARG B   9    10648  10349   6552   1177   2060  -1832       C  
ATOM     63  NH1 ARG B   9      58.362   6.895  -7.224  1.00 74.17           N  
ANISOU   63  NH1 ARG B   9    10800  10790   6593   1085   2122  -1713       N  
ATOM     64  NH2 ARG B   9      59.221   5.241  -5.885  1.00 72.77           N  
ANISOU   64  NH2 ARG B   9    10610  10287   6753   1310   2117  -1920       N  
ATOM     65  N   GLU B  10      50.057   5.929  -6.047  1.00 57.67           N  
ANISOU   65  N   GLU B  10     9344   8143   4423    648   1343  -1582       N  
ATOM     66  CA  GLU B  10      48.716   5.990  -6.618  1.00 57.65           C  
ANISOU   66  CA  GLU B  10     9400   8210   4293    535   1239  -1568       C  
ATOM     67  C   GLU B  10      47.863   7.034  -5.900  1.00 58.03           C  
ANISOU   67  C   GLU B  10     9409   8218   4422    472   1141  -1339       C  
ATOM     68  O   GLU B  10      47.086   7.768  -6.534  1.00 59.16           O  
ANISOU   68  O   GLU B  10     9541   8501   4438    388   1083  -1228       O  
ATOM     69  CB  GLU B  10      48.066   4.604  -6.580  1.00 57.58           C  
ANISOU   69  CB  GLU B  10     9494   8061   4324    523   1181  -1773       C  
ATOM     70  CG  GLU B  10      48.703   3.601  -7.551  1.00 59.30           C  
ANISOU   70  CG  GLU B  10     9718   8349   4463    560   1254  -2015       C  
ATOM     71  CD  GLU B  10      47.822   2.388  -7.815  1.00 65.09           C  
ANISOU   71  CD  GLU B  10    10536   8989   5207    508   1170  -2207       C  
ATOM     72  OE1 GLU B  10      46.930   2.117  -6.984  1.00 63.35           O  
ANISOU   72  OE1 GLU B  10    10391   8587   5093    467   1077  -2169       O  
ATOM     73  OE2 GLU B  10      48.020   1.705  -8.846  1.00 66.31           O  
ANISOU   73  OE2 GLU B  10    10677   9253   5264    506   1197  -2399       O  
ATOM     74  N   PHE B  11      48.034   7.163  -4.585  1.00 52.70           N  
ANISOU   74  N   PHE B  11     8703   7363   3957    516   1125  -1263       N  
ATOM     75  CA  PHE B  11      47.301   8.210  -3.890  1.00 51.73           C  
ANISOU   75  CA  PHE B  11     8533   7208   3915    465   1049  -1066       C  
ATOM     76  C   PHE B  11      47.784   9.593  -4.311  1.00 51.25           C  
ANISOU   76  C   PHE B  11     8388   7293   3792    455   1094   -892       C  
ATOM     77  O   PHE B  11      46.974  10.512  -4.479  1.00 50.79           O  
ANISOU   77  O   PHE B  11     8300   7291   3705    390   1027   -743       O  
ATOM     78  CB  PHE B  11      47.416   8.034  -2.385  1.00 50.96           C  
ANISOU   78  CB  PHE B  11     8422   6907   4035    507   1028  -1036       C  
ATOM     79  CG  PHE B  11      46.551   8.970  -1.625  1.00 50.59           C  
ANISOU   79  CG  PHE B  11     8330   6819   4072    454    952   -875       C  
ATOM     80  CD1 PHE B  11      45.189   9.020  -1.868  1.00 49.47           C  
ANISOU   80  CD1 PHE B  11     8211   6700   3886    371    857   -850       C  
ATOM     81  CD2 PHE B  11      47.097   9.824  -0.694  1.00 48.14           C  
ANISOU   81  CD2 PHE B  11     7948   6457   3888    485    978   -758       C  
ATOM     82  CE1 PHE B  11      44.387   9.896  -1.177  1.00 49.33           C  
ANISOU   82  CE1 PHE B  11     8139   6647   3958    333    795   -713       C  
ATOM     83  CE2 PHE B  11      46.306  10.698   0.000  1.00 48.25           C  
ANISOU   83  CE2 PHE B  11     7917   6431   3985    442    918   -634       C  
ATOM     84  CZ  PHE B  11      44.948  10.738  -0.238  1.00 50.23           C  
ANISOU   84  CZ  PHE B  11     8185   6699   4200    371    830   -612       C  
ATOM     85  N   LEU B  12      49.096   9.752  -4.506  1.00 47.69           N  
ANISOU   85  N   LEU B  12     7891   6901   3328    517   1207   -904       N  
ATOM     86  CA  LEU B  12      49.621  11.029  -4.974  1.00 48.48           C  
ANISOU   86  CA  LEU B  12     7911   7142   3367    494   1257   -735       C  
ATOM     87  C   LEU B  12      49.119  11.340  -6.379  1.00 51.29           C  
ANISOU   87  C   LEU B  12     8286   7711   3492    418   1243   -697       C  
ATOM     88  O   LEU B  12      48.849  12.500  -6.706  1.00 53.49           O  
ANISOU   88  O   LEU B  12     8517   8076   3732    363   1214   -504       O  
ATOM     89  CB  LEU B  12      51.152  11.019  -4.945  1.00 47.72           C  
ANISOU   89  CB  LEU B  12     7753   7081   3296    569   1387   -772       C  
ATOM     90  CG  LEU B  12      51.857  10.882  -3.589  1.00 47.61           C  
ANISOU   90  CG  LEU B  12     7698   6892   3502    644   1403   -779       C  
ATOM     91  CD1 LEU B  12      53.323  11.284  -3.701  1.00 46.61           C  
ANISOU   91  CD1 LEU B  12     7477   6847   3387    694   1523   -755       C  
ATOM     92  CD2 LEU B  12      51.160  11.684  -2.498  1.00 45.46           C  
ANISOU   92  CD2 LEU B  12     7403   6491   3379    606   1313   -635       C  
ATOM     93  N   GLU B  13      48.986  10.317  -7.227  1.00 72.04           N  
ANISOU   93  N   GLU B  13    10983  10425   5964    412   1257   -878       N  
ATOM     94  CA  GLU B  13      48.430  10.540  -8.562  1.00 74.75           C  
ANISOU   94  CA  GLU B  13    11349  10991   6062    328   1230   -852       C  
ATOM     95  C   GLU B  13      47.007  11.073  -8.471  1.00 73.94           C  
ANISOU   95  C   GLU B  13    11255  10867   5971    250   1082   -715       C  
ATOM     96  O   GLU B  13      46.660  12.052  -9.155  1.00 75.74           O  
ANISOU   96  O   GLU B  13    11446  11244   6088    187   1044   -534       O  
ATOM     97  CB  GLU B  13      48.505   9.245  -9.400  1.00 77.45           C  
ANISOU   97  CB  GLU B  13    11769  11415   6243    333   1269  -1112       C  
ATOM     98  CG  GLU B  13      47.308   8.290  -9.277  1.00 81.65           C  
ANISOU   98  CG  GLU B  13    12389  11845   6790    292   1154  -1247       C  
ATOM     99  CD  GLU B  13      47.602   6.866  -9.744  1.00 86.65           C  
ANISOU   99  CD  GLU B  13    13098  12467   7359    324   1205  -1541       C  
ATOM    100  OE1 GLU B  13      48.733   6.586 -10.188  1.00 88.56           O  
ANISOU  100  OE1 GLU B  13    13277  12793   7579    383   1317  -1642       O  
ATOM    101  OE2 GLU B  13      46.713   6.000  -9.572  1.00 88.09           O  
ANISOU  101  OE2 GLU B  13    13351  12538   7583    289   1115  -1665       O  
ATOM    102  N   VAL B  14      46.197  10.494  -7.575  1.00 58.35           N  
ANISOU  102  N   VAL B  14     9317   8706   4147    254    998   -780       N  
ATOM    103  CA  VAL B  14      44.816  10.950  -7.458  1.00 60.05           C  
ANISOU  103  CA  VAL B  14     9524   8906   4386    184    862   -663       C  
ATOM    104  C   VAL B  14      44.756  12.360  -6.871  1.00 59.95           C  
ANISOU  104  C   VAL B  14     9424   8846   4508    190    840   -425       C  
ATOM    105  O   VAL B  14      43.940  13.193  -7.287  1.00 60.30           O  
ANISOU  105  O   VAL B  14     9431   8968   4510    136    755   -265       O  
ATOM    106  CB  VAL B  14      43.993   9.953  -6.628  1.00 59.63           C  
ANISOU  106  CB  VAL B  14     9524   8673   4460    179    789   -795       C  
ATOM    107  CG1 VAL B  14      42.780  10.625  -5.984  1.00 60.26           C  
ANISOU  107  CG1 VAL B  14     9558   8682   4657    136    674   -648       C  
ATOM    108  CG2 VAL B  14      43.557   8.796  -7.512  1.00 61.19           C  
ANISOU  108  CG2 VAL B  14     9806   8949   4495    130    760   -992       C  
ATOM    109  N   LEU B  15      45.638  12.655  -5.913  1.00 50.27           N  
ANISOU  109  N   LEU B  15     8159   7492   3450    255    913   -400       N  
ATOM    110  CA  LEU B  15      45.700  13.996  -5.333  1.00 51.16           C  
ANISOU  110  CA  LEU B  15     8190   7547   3703    259    903   -199       C  
ATOM    111  C   LEU B  15      46.072  15.043  -6.378  1.00 53.44           C  
ANISOU  111  C   LEU B  15     8433   8009   3865    222    929    -26       C  
ATOM    112  O   LEU B  15      45.456  16.115  -6.444  1.00 55.56           O  
ANISOU  112  O   LEU B  15     8651   8279   4181    189    859    161       O  
ATOM    113  CB  LEU B  15      46.706  14.024  -4.177  1.00 48.25           C  
ANISOU  113  CB  LEU B  15     7790   7032   3513    327    980   -229       C  
ATOM    114  CG  LEU B  15      46.315  13.320  -2.880  1.00 48.97           C  
ANISOU  114  CG  LEU B  15     7905   6934   3767    357    943   -329       C  
ATOM    115  CD1 LEU B  15      47.372  13.571  -1.814  1.00 47.80           C  
ANISOU  115  CD1 LEU B  15     7711   6677   3774    415   1012   -322       C  
ATOM    116  CD2 LEU B  15      44.946  13.782  -2.405  1.00 47.49           C  
ANISOU  116  CD2 LEU B  15     7699   6682   3662    312    835   -249       C  
ATOM    117  N   GLU B  16      47.077  14.749  -7.205  1.00 62.08           N  
ANISOU  117  N   GLU B  16     9537   9249   4801    228   1030    -83       N  
ATOM    118  CA  GLU B  16      47.492  15.707  -8.224  1.00 64.07           C  
ANISOU  118  CA  GLU B  16     9745   9685   4913    180   1065     91       C  
ATOM    119  C   GLU B  16      46.399  15.915  -9.262  1.00 64.26           C  
ANISOU  119  C   GLU B  16     9792   9865   4760    102    959    183       C  
ATOM    120  O   GLU B  16      46.119  17.055  -9.652  1.00 66.41           O  
ANISOU  120  O   GLU B  16    10013  10195   5025     58    909    414       O  
ATOM    121  CB  GLU B  16      48.784  15.246  -8.896  1.00 64.88           C  
ANISOU  121  CB  GLU B  16     9849   9936   4869    199   1208    -11       C  
ATOM    122  CG  GLU B  16      49.248  16.163 -10.023  1.00 68.44           C  
ANISOU  122  CG  GLU B  16    10254  10608   5143    133   1255    171       C  
ATOM    123  CD  GLU B  16      50.753  16.351 -10.049  1.00 70.76           C  
ANISOU  123  CD  GLU B  16    10487  10958   5441    162   1410    166       C  
ATOM    124  OE1 GLU B  16      51.217  17.495  -9.859  1.00 71.80           O  
ANISOU  124  OE1 GLU B  16    10544  11067   5668    137   1432    367       O  
ATOM    125  OE2 GLU B  16      51.472  15.352 -10.262  1.00 71.47           O  
ANISOU  125  OE2 GLU B  16    10597  11110   5448    211   1510    -44       O  
ATOM    126  N   GLN B  17      45.762  14.832  -9.718  1.00 59.38           N  
ANISOU  126  N   GLN B  17     9246   9312   4006     82    914     10       N  
ATOM    127  CA  GLN B  17      44.705  14.984 -10.713  1.00 62.41           C  
ANISOU  127  CA  GLN B  17     9644   9862   4207      1    800     90       C  
ATOM    128  C   GLN B  17      43.546  15.826 -10.190  1.00 62.68           C  
ANISOU  128  C   GLN B  17     9628   9784   4403    -14    663    271       C  
ATOM    129  O   GLN B  17      42.904  16.545 -10.964  1.00 63.24           O  
ANISOU  129  O   GLN B  17     9668   9987   4373    -71    573    454       O  
ATOM    130  CB  GLN B  17      44.205  13.612 -11.157  1.00 63.44           C  
ANISOU  130  CB  GLN B  17     9860  10055   4191    -24    771   -157       C  
ATOM    131  CG  GLN B  17      42.925  13.642 -11.965  1.00 67.89           C  
ANISOU  131  CG  GLN B  17    10436  10761   4600   -111    626   -100       C  
ATOM    132  CD  GLN B  17      42.267  12.289 -12.004  1.00 72.28           C  
ANISOU  132  CD  GLN B  17    11069  11293   5102   -136    578   -353       C  
ATOM    133  OE1 GLN B  17      42.941  11.278 -12.167  1.00 73.28           O  
ANISOU  133  OE1 GLN B  17    11258  11425   5160   -112    671   -582       O  
ATOM    134  NE2 GLN B  17      40.949  12.256 -11.845  1.00 74.95           N  
ANISOU  134  NE2 GLN B  17    11396  11595   5485   -184    432   -317       N  
ATOM    135  N   GLU B  18      43.271  15.765  -8.889  1.00 61.18           N  
ANISOU  135  N   GLU B  18     9423   9362   4463     38    645    228       N  
ATOM    136  CA  GLU B  18      42.157  16.492  -8.296  1.00 61.81           C  
ANISOU  136  CA  GLU B  18     9445   9328   4713     35    529    364       C  
ATOM    137  C   GLU B  18      42.545  17.880  -7.801  1.00 61.20           C  
ANISOU  137  C   GLU B  18     9287   9150   4815     65    549    572       C  
ATOM    138  O   GLU B  18      41.752  18.517  -7.100  1.00 62.44           O  
ANISOU  138  O   GLU B  18     9389   9175   5162     82    474    660       O  
ATOM    139  CB  GLU B  18      41.554  15.682  -7.144  1.00 62.32           C  
ANISOU  139  CB  GLU B  18     9531   9209   4938     63    500    202       C  
ATOM    140  CG  GLU B  18      40.896  14.382  -7.578  1.00 64.47           C  
ANISOU  140  CG  GLU B  18     9877   9548   5073     18    449     14       C  
ATOM    141  CD  GLU B  18      39.702  14.606  -8.488  1.00 68.53           C  
ANISOU  141  CD  GLU B  18    10370  10213   5456    -54    314    106       C  
ATOM    142  OE1 GLU B  18      39.004  15.628  -8.318  1.00 70.35           O  
ANISOU  142  OE1 GLU B  18    10519  10418   5793    -53    233    295       O  
ATOM    143  OE2 GLU B  18      39.463  13.759  -9.375  1.00 70.53           O  
ANISOU  143  OE2 GLU B  18    10683  10611   5503   -111    286    -17       O  
ATOM    144  N   GLY B  19      43.735  18.363  -8.150  1.00 51.34           N  
ANISOU  144  N   GLY B  19     8025   7962   3520     68    651    645       N  
ATOM    145  CA  GLY B  19      44.167  19.666  -7.687  1.00 51.44           C  
ANISOU  145  CA  GLY B  19     7963   7867   3714     85    673    833       C  
ATOM    146  C   GLY B  19      44.504  19.733  -6.217  1.00 53.55           C  
ANISOU  146  C   GLY B  19     8207   7907   4234    146    717    748       C  
ATOM    147  O   GLY B  19      44.501  20.824  -5.639  1.00 50.35           O  
ANISOU  147  O   GLY B  19     7736   7374   4021    159    704    881       O  
ATOM    148  N   GLN B  20      44.796  18.592  -5.590  1.00 45.93           N  
ANISOU  148  N   GLN B  20     7291   6887   3273    181    767    530       N  
ATOM    149  CA  GLN B  20      45.103  18.528  -4.167  1.00 44.51           C  
ANISOU  149  CA  GLN B  20     7094   6514   3306    232    802    444       C  
ATOM    150  C   GLN B  20      46.575  18.234  -3.901  1.00 44.35           C  
ANISOU  150  C   GLN B  20     7075   6490   3287    265    927    364       C  
ATOM    151  O   GLN B  20      46.921  17.753  -2.817  1.00 41.86           O  
ANISOU  151  O   GLN B  20     6763   6049   3092    308    957    247       O  
ATOM    152  CB  GLN B  20      44.223  17.482  -3.481  1.00 42.52           C  
ANISOU  152  CB  GLN B  20     6886   6180   3089    244    747    282       C  
ATOM    153  CG  GLN B  20      42.776  17.904  -3.322  1.00 44.01           C  
ANISOU  153  CG  GLN B  20     7042   6329   3352    222    630    355       C  
ATOM    154  CD  GLN B  20      42.633  19.198  -2.545  1.00 47.04           C  
ANISOU  154  CD  GLN B  20     7341   6582   3951    243    616    485       C  
ATOM    155  OE1 GLN B  20      41.909  20.105  -2.956  1.00 47.82           O  
ANISOU  155  OE1 GLN B  20     7387   6694   4090    230    542    639       O  
ATOM    156  NE2 GLN B  20      43.329  19.291  -1.416  1.00 42.94           N  
ANISOU  156  NE2 GLN B  20     6806   5935   3576    278    682    422       N  
ATOM    157  N   LEU B  21      47.450  18.508  -4.866  1.00 53.42           N  
ANISOU  157  N   LEU B  21     8211   7786   4301    244    998    432       N  
ATOM    158  CA  LEU B  21      48.882  18.317  -4.685  1.00 53.61           C  
ANISOU  158  CA  LEU B  21     8213   7825   4331    275   1121    370       C  
ATOM    159  C   LEU B  21      49.630  19.424  -5.408  1.00 54.78           C  
ANISOU  159  C   LEU B  21     8299   8077   4437    229   1176    557       C  
ATOM    160  O   LEU B  21      49.311  19.747  -6.556  1.00 53.93           O  
ANISOU  160  O   LEU B  21     8199   8125   4165    175   1154    673       O  
ATOM    161  CB  LEU B  21      49.337  16.945  -5.198  1.00 51.93           C  
ANISOU  161  CB  LEU B  21     8062   7716   3954    305   1183    172       C  
ATOM    162  CG  LEU B  21      50.802  16.591  -4.924  1.00 50.43           C  
ANISOU  162  CG  LEU B  21     7837   7533   3790    357   1309     82       C  
ATOM    163  CD1 LEU B  21      50.929  15.156  -4.435  1.00 48.99           C  
ANISOU  163  CD1 LEU B  21     7713   7278   3623    426   1324   -145       C  
ATOM    164  CD2 LEU B  21      51.661  16.812  -6.164  1.00 50.58           C  
ANISOU  164  CD2 LEU B  21     7827   7769   3621    326   1407    130       C  
ATOM    165  N   ILE B  22      50.623  19.997  -4.733  1.00 61.88           N  
ANISOU  165  N   ILE B  22     9133   8895   5481    242   1244    591       N  
ATOM    166  CA  ILE B  22      51.472  21.045  -5.284  1.00 62.57           C  
ANISOU  166  CA  ILE B  22     9152   9061   5560    190   1307    767       C  
ATOM    167  C   ILE B  22      52.869  20.475  -5.487  1.00 62.18           C  
ANISOU  167  C   ILE B  22     9074   9122   5429    212   1443    664       C  
ATOM    168  O   ILE B  22      53.391  19.765  -4.620  1.00 61.23           O  
ANISOU  168  O   ILE B  22     8949   8916   5397    278   1478    502       O  
ATOM    169  CB  ILE B  22      51.517  22.278  -4.360  1.00 64.40           C  
ANISOU  169  CB  ILE B  22     9319   9108   6044    174   1276    893       C  
ATOM    170  CG1 ILE B  22      50.139  22.927  -4.254  1.00 65.99           C  
ANISOU  170  CG1 ILE B  22     9532   9207   6335    161   1149   1002       C  
ATOM    171  CG2 ILE B  22      52.537  23.291  -4.858  1.00 67.02           C  
ANISOU  171  CG2 ILE B  22     9577   9504   6386    112   1351   1065       C  
ATOM    172  CD1 ILE B  22      50.151  24.214  -3.456  1.00 67.58           C  
ANISOU  172  CD1 ILE B  22     9667   9223   6789    146   1122   1120       C  
ATOM    173  N   ARG B  23      53.475  20.788  -6.631  1.00 74.59           N  
ANISOU  173  N   ARG B  23    10618  10891   6832    158   1517    765       N  
ATOM    174  CA  ARG B  23      54.829  20.355  -6.946  1.00 72.85           C  
ANISOU  174  CA  ARG B  23    10348  10803   6527    174   1659    680       C  
ATOM    175  C   ARG B  23      55.787  21.529  -6.785  1.00 73.06           C  
ANISOU  175  C   ARG B  23    10271  10817   6670    118   1720    852       C  
ATOM    176  O   ARG B  23      55.585  22.588  -7.387  1.00 74.11           O  
ANISOU  176  O   ARG B  23    10382  10995   6782     31   1696   1075       O  
ATOM    177  CB  ARG B  23      54.907  19.780  -8.360  1.00 73.74           C  
ANISOU  177  CB  ARG B  23    10494  11177   6346    147   1721    643       C  
ATOM    178  CG  ARG B  23      54.303  18.394  -8.476  1.00 73.95           C  
ANISOU  178  CG  ARG B  23    10615  11219   6265    210   1692    410       C  
ATOM    179  CD  ARG B  23      54.647  17.732  -9.800  1.00 75.07           C  
ANISOU  179  CD  ARG B  23    10778  11625   6119    191   1783    319       C  
ATOM    180  NE  ARG B  23      54.355  16.301  -9.770  1.00 75.27           N  
ANISOU  180  NE  ARG B  23    10883  11633   6085    264   1780     50       N  
ATOM    181  CZ  ARG B  23      55.255  15.360  -9.506  1.00 76.94           C  
ANISOU  181  CZ  ARG B  23    11077  11832   6327    353   1880   -158       C  
ATOM    182  NH1 ARG B  23      56.513  15.695  -9.254  1.00 76.53           N  
ANISOU  182  NH1 ARG B  23    10923  11804   6352    378   1992   -131       N  
ATOM    183  NH2 ARG B  23      54.899  14.082  -9.495  1.00 78.96           N  
ANISOU  183  NH2 ARG B  23    11411  12043   6546    415   1864   -392       N  
ATOM    184  N   VAL B  24      56.816  21.341  -5.965  1.00 64.59           N  
ANISOU  184  N   VAL B  24     9133   9680   5729    162   1789    755       N  
ATOM    185  CA  VAL B  24      57.885  22.322  -5.796  1.00 64.65           C  
ANISOU  185  CA  VAL B  24     9030   9690   5845    104   1859    886       C  
ATOM    186  C   VAL B  24      59.086  21.736  -6.531  1.00 65.41           C  
ANISOU  186  C   VAL B  24     9065  10007   5782    115   2009    807       C  
ATOM    187  O   VAL B  24      59.869  20.964  -5.983  1.00 66.70           O  
ANISOU  187  O   VAL B  24     9187  10160   5996    195   2070    636       O  
ATOM    188  CB  VAL B  24      58.182  22.609  -4.326  1.00 62.46           C  
ANISOU  188  CB  VAL B  24     8706   9196   5830    135   1823    836       C  
ATOM    189  CG1 VAL B  24      59.258  23.680  -4.205  1.00 62.30           C  
ANISOU  189  CG1 VAL B  24     8568   9179   5924     57   1888    974       C  
ATOM    190  CG2 VAL B  24      56.919  23.037  -3.596  1.00 62.32           C  
ANISOU  190  CG2 VAL B  24     8751   8975   5952    138   1686    871       C  
ATOM    191  N   LYS B  25      59.220  22.099  -7.808  1.00 73.52           N  
ANISOU  191  N   LYS B  25    10079  11247   6607     34   2070    938       N  
ATOM    192  CA  LYS B  25      60.338  21.608  -8.604  1.00 75.22           C  
ANISOU  192  CA  LYS B  25    10226  11703   6650     36   2228    865       C  
ATOM    193  C   LYS B  25      61.623  22.378  -8.335  1.00 75.21           C  
ANISOU  193  C   LYS B  25    10083  11724   6769    -18   2323    965       C  
ATOM    194  O   LYS B  25      62.708  21.866  -8.629  1.00 74.35           O  
ANISOU  194  O   LYS B  25     9889  11776   6586     12   2459    861       O  
ATOM    195  CB  LYS B  25      59.988  21.671 -10.094  1.00 76.88           C  
ANISOU  195  CB  LYS B  25    10476  12166   6568    -42   2262    962       C  
ATOM    196  CG  LYS B  25      58.601  21.138 -10.420  1.00 75.80           C  
ANISOU  196  CG  LYS B  25    10474  12012   6317    -19   2144    907       C  
ATOM    197  CD  LYS B  25      58.385  21.031 -11.922  1.00 76.26           C  
ANISOU  197  CD  LYS B  25    10565  12361   6050    -93   2187    965       C  
ATOM    198  CE  LYS B  25      58.819  19.671 -12.450  1.00 76.75           C  
ANISOU  198  CE  LYS B  25    10650  12569   5943    -23   2285    677       C  
ATOM    199  NZ  LYS B  25      59.257  19.737 -13.871  1.00 78.87           N  
ANISOU  199  NZ  LYS B  25    10909  13042   6014   -113   2353    703       N  
ATOM    200  N   GLU B  26      61.525  23.584  -7.782  1.00 80.45           N  
ANISOU  200  N   GLU B  26    10713  12229   7626    -95   2256   1155       N  
ATOM    201  CA  GLU B  26      62.710  24.345  -7.416  1.00 82.37           C  
ANISOU  201  CA  GLU B  26    10820  12466   8012   -158   2332   1244       C  
ATOM    202  C   GLU B  26      63.359  23.747  -6.172  1.00 83.03           C  
ANISOU  202  C   GLU B  26    10848  12423   8276    -58   2337   1046       C  
ATOM    203  O   GLU B  26      62.675  23.240  -5.278  1.00 82.86           O  
ANISOU  203  O   GLU B  26    10902  12224   8357     28   2237    920       O  
ATOM    204  CB  GLU B  26      62.333  25.809  -7.175  1.00 84.29           C  
ANISOU  204  CB  GLU B  26    11054  12548   8425   -272   2247   1493       C  
ATOM    205  CG  GLU B  26      63.422  26.677  -6.567  1.00 86.78           C  
ANISOU  205  CG  GLU B  26    11237  12794   8942   -347   2295   1574       C  
ATOM    206  CD  GLU B  26      62.869  27.959  -5.973  1.00 87.75           C  
ANISOU  206  CD  GLU B  26    11372  12669   9299   -425   2181   1746       C  
ATOM    207  OE1 GLU B  26      61.804  27.902  -5.321  1.00 85.44           O  
ANISOU  207  OE1 GLU B  26    11171  12185   9106   -364   2058   1689       O  
ATOM    208  OE2 GLU B  26      63.496  29.024  -6.161  1.00 89.46           O  
ANISOU  208  OE2 GLU B  26    11503  12879   9608   -550   2218   1934       O  
ATOM    209  N   GLU B  27      64.688  23.793  -6.125  1.00 82.16           N  
ANISOU  209  N   GLU B  27    10599  12420   8199    -73   2453   1027       N  
ATOM    210  CA  GLU B  27      65.418  23.266  -4.979  1.00 81.28           C  
ANISOU  210  CA  GLU B  27    10415  12213   8257     17   2454    861       C  
ATOM    211  C   GLU B  27      65.150  24.108  -3.737  1.00 79.97           C  
ANISOU  211  C   GLU B  27    10246  11795   8344    -23   2336    923       C  
ATOM    212  O   GLU B  27      65.136  25.341  -3.792  1.00 80.27           O  
ANISOU  212  O   GLU B  27    10253  11773   8474   -147   2314   1112       O  
ATOM    213  CB  GLU B  27      66.916  23.231  -5.278  1.00 82.82           C  
ANISOU  213  CB  GLU B  27    10439  12596   8432     -1   2604    846       C  
ATOM    214  CG  GLU B  27      67.791  22.889  -4.082  1.00 84.25           C  
ANISOU  214  CG  GLU B  27    10515  12688   8808     72   2596    717       C  
ATOM    215  CD  GLU B  27      69.238  23.297  -4.288  1.00 87.19           C  
ANISOU  215  CD  GLU B  27    10693  13222   9213     10   2724    768       C  
ATOM    216  OE1 GLU B  27      69.556  24.490  -4.091  1.00 88.97           O  
ANISOU  216  OE1 GLU B  27    10847  13399   9558   -128   2712    940       O  
ATOM    217  OE2 GLU B  27      70.057  22.427  -4.651  1.00 87.74           O  
ANISOU  217  OE2 GLU B  27    10674  13463   9199     97   2838    634       O  
ATOM    218  N   VAL B  28      64.931  23.434  -2.609  1.00 59.29           N  
ANISOU  218  N   VAL B  28     7660   9027   5839     80   2258    759       N  
ATOM    219  CA  VAL B  28      64.695  24.101  -1.337  1.00 58.61           C  
ANISOU  219  CA  VAL B  28     7572   8722   5977     51   2151    776       C  
ATOM    220  C   VAL B  28      65.732  23.622  -0.331  1.00 59.11           C  
ANISOU  220  C   VAL B  28     7528   8774   6157    111   2165    643       C  
ATOM    221  O   VAL B  28      66.339  22.558  -0.479  1.00 57.12           O  
ANISOU  221  O   VAL B  28     7237   8636   5829    212   2229    513       O  
ATOM    222  CB  VAL B  28      63.270  23.854  -0.799  1.00 58.99           C  
ANISOU  222  CB  VAL B  28     7765   8596   6051    102   2022    724       C  
ATOM    223  CG1 VAL B  28      62.231  24.315  -1.809  1.00 59.69           C  
ANISOU  223  CG1 VAL B  28     7947   8704   6027     48   1996    861       C  
ATOM    224  CG2 VAL B  28      63.079  22.383  -0.457  1.00 53.49           C  
ANISOU  224  CG2 VAL B  28     7129   7906   5288    240   2008    523       C  
ATOM    225  N   ASN B  29      65.936  24.434   0.702  1.00 62.33           N  
ANISOU  225  N   ASN B  29     7884   9042   6758     49   2100    676       N  
ATOM    226  CA  ASN B  29      66.773  24.009   1.809  1.00 63.28           C  
ANISOU  226  CA  ASN B  29     7912   9140   6993    101   2080    555       C  
ATOM    227  C   ASN B  29      65.991  23.058   2.711  1.00 62.25           C  
ANISOU  227  C   ASN B  29     7889   8892   6874    216   1981    410       C  
ATOM    228  O   ASN B  29      64.770  23.178   2.836  1.00 60.96           O  
ANISOU  228  O   ASN B  29     7853   8608   6702    213   1904    420       O  
ATOM    229  CB  ASN B  29      67.248  25.212   2.617  1.00 65.71           C  
ANISOU  229  CB  ASN B  29     8127   9348   7490    -19   2040    626       C  
ATOM    230  CG  ASN B  29      68.119  26.150   1.809  1.00 68.26           C  
ANISOU  230  CG  ASN B  29     8331   9779   7824   -146   2137    778       C  
ATOM    231  OD1 ASN B  29      68.899  25.716   0.962  1.00 68.93           O  
ANISOU  231  OD1 ASN B  29     8335  10060   7795   -128   2252    787       O  
ATOM    232  ND2 ASN B  29      67.991  27.447   2.066  1.00 69.69           N  
ANISOU  232  ND2 ASN B  29     8496   9833   8149   -280   2095    897       N  
ATOM    233  N   PRO B  30      66.669  22.090   3.335  1.00 57.31           N  
ANISOU  233  N   PRO B  30     7206   8300   6268    317   1980    283       N  
ATOM    234  CA  PRO B  30      65.952  21.192   4.261  1.00 55.43           C  
ANISOU  234  CA  PRO B  30     7068   7945   6048    413   1879    166       C  
ATOM    235  C   PRO B  30      65.242  21.941   5.376  1.00 56.44           C  
ANISOU  235  C   PRO B  30     7243   7907   6294    345   1767    182       C  
ATOM    236  O   PRO B  30      64.072  21.659   5.666  1.00 56.91           O  
ANISOU  236  O   PRO B  30     7430   7863   6329    372   1696    149       O  
ATOM    237  CB  PRO B  30      67.066  20.273   4.789  1.00 55.19           C  
ANISOU  237  CB  PRO B  30     6930   7984   6056    513   1896     66       C  
ATOM    238  CG  PRO B  30      68.354  20.974   4.457  1.00 57.25           C  
ANISOU  238  CG  PRO B  30     7016   8374   6363    444   1984    132       C  
ATOM    239  CD  PRO B  30      68.090  21.730   3.201  1.00 57.23           C  
ANISOU  239  CD  PRO B  30     7037   8440   6269    352   2068    248       C  
ATOM    240  N   GLU B  31      65.917  22.903   6.002  1.00 52.54           N  
ANISOU  240  N   GLU B  31     6644   7392   5929    253   1753    224       N  
ATOM    241  CA  GLU B  31      65.317  23.737   7.027  1.00 55.29           C  
ANISOU  241  CA  GLU B  31     7023   7589   6394    177   1659    223       C  
ATOM    242  C   GLU B  31      65.521  25.203   6.674  1.00 58.37           C  
ANISOU  242  C   GLU B  31     7356   7942   6880     37   1686    343       C  
ATOM    243  O   GLU B  31      66.594  25.580   6.186  1.00 61.81           O  
ANISOU  243  O   GLU B  31     7670   8479   7334    -18   1761    407       O  
ATOM    244  CB  GLU B  31      65.922  23.449   8.408  1.00 57.67           C  
ANISOU  244  CB  GLU B  31     7255   7878   6779    194   1589    128       C  
ATOM    245  CG  GLU B  31      65.958  21.980   8.769  1.00 56.88           C  
ANISOU  245  CG  GLU B  31     7189   7817   6606    332   1562     33       C  
ATOM    246  CD  GLU B  31      67.307  21.345   8.508  1.00 58.28           C  
ANISOU  246  CD  GLU B  31     7232   8136   6777    397   1623     16       C  
ATOM    247  OE1 GLU B  31      68.315  22.081   8.433  1.00 60.69           O  
ANISOU  247  OE1 GLU B  31     7396   8512   7150    321   1665     63       O  
ATOM    248  OE2 GLU B  31      67.359  20.106   8.380  1.00 57.10           O  
ANISOU  248  OE2 GLU B  31     7112   8020   6564    524   1629    -47       O  
ATOM    249  N   PRO B  32      64.516  26.057   6.915  1.00 54.72           N  
ANISOU  249  N   PRO B  32     6971   7329   6491    -24   1628    378       N  
ATOM    250  CA  PRO B  32      63.223  25.686   7.492  1.00 53.55           C  
ANISOU  250  CA  PRO B  32     6950   7070   6326     32   1548    304       C  
ATOM    251  C   PRO B  32      62.139  25.498   6.436  1.00 51.98           C  
ANISOU  251  C   PRO B  32     6864   6864   6021     66   1560    371       C  
ATOM    252  O   PRO B  32      60.956  25.535   6.768  1.00 51.23           O  
ANISOU  252  O   PRO B  32     6863   6663   5939     84   1496    344       O  
ATOM    253  CB  PRO B  32      62.906  26.886   8.377  1.00 54.95           C  
ANISOU  253  CB  PRO B  32     7113   7095   6669    -64   1487    296       C  
ATOM    254  CG  PRO B  32      63.446  28.046   7.576  1.00 56.63           C  
ANISOU  254  CG  PRO B  32     7254   7299   6964   -172   1542    438       C  
ATOM    255  CD  PRO B  32      64.642  27.520   6.789  1.00 57.22           C  
ANISOU  255  CD  PRO B  32     7238   7559   6945   -159   1633    485       C  
ATOM    256  N   ASP B  33      62.548  25.273   5.186  1.00 50.86           N  
ANISOU  256  N   ASP B  33     6706   6851   5768     74   1643    453       N  
ATOM    257  CA  ASP B  33      61.624  25.397   4.062  1.00 49.23           C  
ANISOU  257  CA  ASP B  33     6587   6654   5463     71   1653    550       C  
ATOM    258  C   ASP B  33      60.556  24.309   4.076  1.00 45.06           C  
ANISOU  258  C   ASP B  33     6180   6114   4825    169   1606    457       C  
ATOM    259  O   ASP B  33      59.372  24.592   3.867  1.00 44.06           O  
ANISOU  259  O   ASP B  33     6138   5911   4694    162   1553    499       O  
ATOM    260  CB  ASP B  33      62.398  25.373   2.744  1.00 49.52           C  
ANISOU  260  CB  ASP B  33     6571   6865   5380     46   1759    649       C  
ATOM    261  CG  ASP B  33      63.403  26.501   2.640  1.00 53.81           C  
ANISOU  261  CG  ASP B  33     6991   7422   6033    -70   1809    765       C  
ATOM    262  OD1 ASP B  33      63.234  27.515   3.350  1.00 55.29           O  
ANISOU  262  OD1 ASP B  33     7159   7455   6393   -145   1752    799       O  
ATOM    263  OD2 ASP B  33      64.359  26.377   1.845  1.00 55.14           O  
ANISOU  263  OD2 ASP B  33     7078   7757   6118    -92   1909    815       O  
ATOM    264  N   ILE B  34      60.952  23.056   4.303  1.00 45.81           N  
ANISOU  264  N   ILE B  34     6281   6281   4842    261   1622    335       N  
ATOM    265  CA  ILE B  34      59.991  21.957   4.225  1.00 43.87           C  
ANISOU  265  CA  ILE B  34     6152   6023   4494    344   1582    250       C  
ATOM    266  C   ILE B  34      58.947  22.075   5.333  1.00 41.76           C  
ANISOU  266  C   ILE B  34     5947   5606   4314    343   1482    200       C  
ATOM    267  O   ILE B  34      57.740  21.913   5.097  1.00 43.47           O  
ANISOU  267  O   ILE B  34     6256   5776   4486    354   1437    203       O  
ATOM    268  CB  ILE B  34      60.731  20.608   4.268  1.00 44.75           C  
ANISOU  268  CB  ILE B  34     6249   6220   4535    444   1621    133       C  
ATOM    269  CG1 ILE B  34      61.647  20.472   3.048  1.00 44.08           C  
ANISOU  269  CG1 ILE B  34     6100   6301   4346    451   1734    166       C  
ATOM    270  CG2 ILE B  34      59.744  19.451   4.331  1.00 44.09           C  
ANISOU  270  CG2 ILE B  34     6286   6093   4373    521   1570     38       C  
ATOM    271  CD1 ILE B  34      62.416  19.173   2.996  1.00 42.22           C  
ANISOU  271  CD1 ILE B  34     5838   6146   4059    562   1783     40       C  
ATOM    272  N   ALA B  35      59.389  22.386   6.552  1.00 39.87           N  
ANISOU  272  N   ALA B  35     5650   5303   4196    322   1448    152       N  
ATOM    273  CA  ALA B  35      58.450  22.563   7.655  1.00 39.14           C  
ANISOU  273  CA  ALA B  35     5605   5088   4177    311   1366     95       C  
ATOM    274  C   ALA B  35      57.593  23.807   7.461  1.00 42.64           C  
ANISOU  274  C   ALA B  35     6063   5434   4706    242   1341    175       C  
ATOM    275  O   ALA B  35      56.402  23.805   7.798  1.00 42.62           O  
ANISOU  275  O   ALA B  35     6126   5351   4716    252   1287    146       O  
ATOM    276  CB  ALA B  35      59.207  22.638   8.976  1.00 39.69           C  
ANISOU  276  CB  ALA B  35     5604   5139   4337    295   1337     22       C  
ATOM    277  N   ALA B  36      58.182  24.885   6.936  1.00 43.63           N  
ANISOU  277  N   ALA B  36     6119   5556   4901    171   1381    280       N  
ATOM    278  CA  ALA B  36      57.400  26.085   6.658  1.00 45.19           C  
ANISOU  278  CA  ALA B  36     6327   5642   5200    113   1354    376       C  
ATOM    279  C   ALA B  36      56.333  25.817   5.610  1.00 43.62           C  
ANISOU  279  C   ALA B  36     6211   5467   4895    146   1340    450       C  
ATOM    280  O   ALA B  36      55.225  26.353   5.701  1.00 44.68           O  
ANISOU  280  O   ALA B  36     6380   5497   5098    140   1286    476       O  
ATOM    281  CB  ALA B  36      58.314  27.225   6.210  1.00 47.47           C  
ANISOU  281  CB  ALA B  36     6528   5924   5586     23   1400    495       C  
ATOM    282  N   ALA B  37      56.633  24.968   4.627  1.00 47.12           N  
ANISOU  282  N   ALA B  37     6681   6053   5171    182   1387    472       N  
ATOM    283  CA  ALA B  37      55.631  24.617   3.628  1.00 47.23           C  
ANISOU  283  CA  ALA B  37     6774   6112   5060    207   1367    526       C  
ATOM    284  C   ALA B  37      54.543  23.734   4.224  1.00 45.18           C  
ANISOU  284  C   ALA B  37     6594   5806   4768    267   1302    407       C  
ATOM    285  O   ALA B  37      53.368  23.874   3.871  1.00 44.83           O  
ANISOU  285  O   ALA B  37     6599   5726   4707    269   1249    448       O  
ATOM    286  CB  ALA B  37      56.291  23.933   2.435  1.00 46.42           C  
ANISOU  286  CB  ALA B  37     6675   6187   4776    223   1441    556       C  
ATOM    287  N   GLY B  38      54.907  22.819   5.124  1.00 42.36           N  
ANISOU  287  N   GLY B  38     6243   5449   4401    313   1302    271       N  
ATOM    288  CA  GLY B  38      53.881  22.070   5.839  1.00 39.20           C  
ANISOU  288  CA  GLY B  38     5911   4993   3989    352   1240    171       C  
ATOM    289  C   GLY B  38      52.943  22.980   6.614  1.00 41.23           C  
ANISOU  289  C   GLY B  38     6159   5125   4381    318   1183    175       C  
ATOM    290  O   GLY B  38      51.714  22.882   6.503  1.00 42.38           O  
ANISOU  290  O   GLY B  38     6353   5237   4514    329   1135    175       O  
ATOM    291  N   ARG B  39      53.520  23.897   7.396  1.00 37.18           N  
ANISOU  291  N   ARG B  39     5576   4544   4006    277   1190    170       N  
ATOM    292  CA  ARG B  39      52.716  24.836   8.173  1.00 37.87           C  
ANISOU  292  CA  ARG B  39     5644   4506   4239    247   1147    150       C  
ATOM    293  C   ARG B  39      51.849  25.703   7.269  1.00 39.20           C  
ANISOU  293  C   ARG B  39     5817   4618   4458    234   1125    273       C  
ATOM    294  O   ARG B  39      50.686  25.970   7.586  1.00 40.47           O  
ANISOU  294  O   ARG B  39     5992   4703   4682    247   1078    251       O  
ATOM    295  CB  ARG B  39      53.629  25.706   9.040  1.00 39.10           C  
ANISOU  295  CB  ARG B  39     5721   4604   4532    195   1164    116       C  
ATOM    296  CG  ARG B  39      52.916  26.783   9.848  1.00 40.94           C  
ANISOU  296  CG  ARG B  39     5926   4698   4933    162   1130     71       C  
ATOM    297  CD  ARG B  39      52.136  26.212  11.020  1.00 40.07           C  
ANISOU  297  CD  ARG B  39     5844   4578   4803    186   1097    -72       C  
ATOM    298  NE  ARG B  39      50.755  25.899  10.669  1.00 40.05           N  
ANISOU  298  NE  ARG B  39     5893   4561   4764    226   1065    -60       N  
ATOM    299  CZ  ARG B  39      49.876  25.357  11.507  1.00 37.07           C  
ANISOU  299  CZ  ARG B  39     5542   4187   4358    243   1040   -164       C  
ATOM    300  NH1 ARG B  39      50.232  25.070  12.753  1.00 34.47           N  
ANISOU  300  NH1 ARG B  39     5199   3880   4020    222   1041   -283       N  
ATOM    301  NH2 ARG B  39      48.640  25.107  11.099  1.00 34.95           N  
ANISOU  301  NH2 ARG B  39     5306   3911   4062    273   1011   -143       N  
ATOM    302  N   ALA B  40      52.391  26.141   6.129  1.00 37.25           N  
ANISOU  302  N   ALA B  40     5554   4419   4182    208   1157    413       N  
ATOM    303  CA  ALA B  40      51.639  27.004   5.223  1.00 37.32           C  
ANISOU  303  CA  ALA B  40     5562   4380   4238    191   1126    563       C  
ATOM    304  C   ALA B  40      50.487  26.252   4.569  1.00 36.75           C  
ANISOU  304  C   ALA B  40     5558   4372   4035    235   1081    575       C  
ATOM    305  O   ALA B  40      49.361  26.765   4.485  1.00 37.25           O  
ANISOU  305  O   ALA B  40     5621   4359   4174    246   1021    621       O  
ATOM    306  CB  ALA B  40      52.578  27.578   4.163  1.00 40.98           C  
ANISOU  306  CB  ALA B  40     5991   4904   4675    139   1174    722       C  
ATOM    307  N   ALA B  41      50.758  25.040   4.075  1.00 45.95           N  
ANISOU  307  N   ALA B  41     6774   5674   5010    262   1106    529       N  
ATOM    308  CA  ALA B  41      49.700  24.210   3.516  1.00 45.15           C  
ANISOU  308  CA  ALA B  41     6740   5637   4779    293   1060    513       C  
ATOM    309  C   ALA B  41      48.587  23.995   4.530  1.00 45.56           C  
ANISOU  309  C   ALA B  41     6804   5598   4909    318   1003    409       C  
ATOM    310  O   ALA B  41      47.404  24.054   4.181  1.00 47.00           O  
ANISOU  310  O   ALA B  41     7001   5771   5087    327    944    445       O  
ATOM    311  CB  ALA B  41      50.275  22.873   3.048  1.00 42.47           C  
ANISOU  311  CB  ALA B  41     6452   5432   4251    320   1103    436       C  
ATOM    312  N   ALA B  42      48.946  23.766   5.797  1.00 39.61           N  
ANISOU  312  N   ALA B  42     6037   4790   4225    325   1020    283       N  
ATOM    313  CA  ALA B  42      47.920  23.678   6.833  1.00 40.40           C  
ANISOU  313  CA  ALA B  42     6136   4815   4397    336    978    187       C  
ATOM    314  C   ALA B  42      47.188  25.008   7.004  1.00 44.83           C  
ANISOU  314  C   ALA B  42     6638   5262   5135    326    947    242       C  
ATOM    315  O   ALA B  42      45.969  25.033   7.207  1.00 43.17           O  
ANISOU  315  O   ALA B  42     6423   5018   4963    344    901    218       O  
ATOM    316  CB  ALA B  42      48.542  23.230   8.155  1.00 37.10           C  
ANISOU  316  CB  ALA B  42     5711   4382   4002    334   1002     55       C  
ATOM    317  N   ASN B  43      47.915  26.125   6.908  1.00 41.40           N  
ANISOU  317  N   ASN B  43     6151   4758   4819    298    971    316       N  
ATOM    318  CA  ASN B  43      47.344  27.446   7.138  1.00 46.50           C  
ANISOU  318  CA  ASN B  43     6738   5262   5669    293    944    359       C  
ATOM    319  C   ASN B  43      46.423  27.907   6.018  1.00 49.05           C  
ANISOU  319  C   ASN B  43     7058   5574   6006    310    889    515       C  
ATOM    320  O   ASN B  43      45.671  28.866   6.220  1.00 50.89           O  
ANISOU  320  O   ASN B  43     7239   5680   6416    327    853    544       O  
ATOM    321  CB  ASN B  43      48.459  28.473   7.333  1.00 48.66           C  
ANISOU  321  CB  ASN B  43     6960   5455   6075    246    982    396       C  
ATOM    322  CG  ASN B  43      49.061  28.417   8.717  1.00 48.81           C  
ANISOU  322  CG  ASN B  43     6954   5442   6149    226   1013    227       C  
ATOM    323  OD1 ASN B  43      48.670  27.590   9.543  1.00 47.57           O  
ANISOU  323  OD1 ASN B  43     6822   5332   5922    247   1008     94       O  
ATOM    324  ND2 ASN B  43      50.018  29.299   8.983  1.00 45.97           N  
ANISOU  324  ND2 ASN B  43     6543   5012   5911    175   1041    238       N  
ATOM    325  N   LEU B  44      46.460  27.263   4.849  1.00 56.10           N  
ANISOU  325  N   LEU B  44     7998   6598   6718    309    880    613       N  
ATOM    326  CA  LEU B  44      45.473  27.585   3.823  1.00 59.58           C  
ANISOU  326  CA  LEU B  44     8436   7056   7146    323    811    758       C  
ATOM    327  C   LEU B  44      44.039  27.327   4.286  1.00 62.75           C  
ANISOU  327  C   LEU B  44     8825   7426   7591    365    751    681       C  
ATOM    328  O   LEU B  44      43.101  27.770   3.613  1.00 63.05           O  
ANISOU  328  O   LEU B  44     8836   7453   7667    384    681    798       O  
ATOM    329  CB  LEU B  44      45.759  26.800   2.544  1.00 58.00           C  
ANISOU  329  CB  LEU B  44     8295   7033   6711    306    814    843       C  
ATOM    330  CG  LEU B  44      47.116  27.131   1.922  1.00 58.03           C  
ANISOU  330  CG  LEU B  44     8295   7091   6664    261    880    942       C  
ATOM    331  CD1 LEU B  44      47.457  26.160   0.808  1.00 58.27           C  
ANISOU  331  CD1 LEU B  44     8384   7319   6438    249    904    968       C  
ATOM    332  CD2 LEU B  44      47.140  28.567   1.419  1.00 59.71           C  
ANISOU  332  CD2 LEU B  44     8452   7207   7028    230    855   1141       C  
ATOM    333  N   GLY B  45      43.847  26.633   5.406  1.00 79.44           N  
ANISOU  333  N   GLY B  45    10949   9535   9699    377    773    499       N  
ATOM    334  CA  GLY B  45      42.533  26.455   6.030  1.00 80.71           C  
ANISOU  334  CA  GLY B  45    11081   9667   9918    406    732    412       C  
ATOM    335  C   GLY B  45      41.571  25.476   5.389  1.00 79.75           C  
ANISOU  335  C   GLY B  45    10996   9660   9646    412    677    422       C  
ATOM    336  O   GLY B  45      40.960  24.661   6.087  1.00 79.17           O  
ANISOU  336  O   GLY B  45    10934   9617   9531    412    675    296       O  
ATOM    337  N   LYS B  46      41.400  25.551   4.070  1.00 65.70           N  
ANISOU  337  N   LYS B  46     9232   7953   7779    408    629    573       N  
ATOM    338  CA  LYS B  46      40.469  24.683   3.364  1.00 63.15           C  
ANISOU  338  CA  LYS B  46     8937   7747   7308    403    565    584       C  
ATOM    339  C   LYS B  46      41.093  24.251   2.049  1.00 60.95           C  
ANISOU  339  C   LYS B  46     8725   7604   6831    374    563    683       C  
ATOM    340  O   LYS B  46      41.894  24.982   1.459  1.00 62.92           O  
ANISOU  340  O   LYS B  46     8967   7850   7090    362    586    808       O  
ATOM    341  CB  LYS B  46      39.130  25.382   3.096  1.00 65.51           C  
ANISOU  341  CB  LYS B  46     9155   8009   7725    434    477    672       C  
ATOM    342  CG  LYS B  46      38.459  25.955   4.327  1.00 69.97           C  
ANISOU  342  CG  LYS B  46     9637   8445   8503    471    488    573       C  
ATOM    343  CD  LYS B  46      37.801  27.299   4.040  1.00 73.57           C  
ANISOU  343  CD  LYS B  46     9995   8791   9168    520    429    704       C  
ATOM    344  CE  LYS B  46      36.535  27.193   3.172  1.00 75.11           C  
ANISOU  344  CE  LYS B  46    10145   9065   9330    539    321    810       C  
ATOM    345  NZ  LYS B  46      36.752  26.834   1.732  1.00 76.30           N  
ANISOU  345  NZ  LYS B  46    10355   9358   9278    501    264    968       N  
ATOM    346  N   ASN B  47      40.707  23.059   1.592  1.00 55.85           N  
ANISOU  346  N   ASN B  47     8139   7079   6003    354    538    619       N  
ATOM    347  CA  ASN B  47      41.256  22.453   0.377  1.00 56.21           C  
ANISOU  347  CA  ASN B  47     8252   7272   5831    324    545    665       C  
ATOM    348  C   ASN B  47      42.776  22.340   0.444  1.00 54.21           C  
ANISOU  348  C   ASN B  47     8035   7028   5534    320    646    635       C  
ATOM    349  O   ASN B  47      43.455  22.394  -0.583  1.00 53.60           O  
ANISOU  349  O   ASN B  47     7982   7057   5327    298    671    721       O  
ATOM    350  CB  ASN B  47      40.847  23.228  -0.882  1.00 58.68           C  
ANISOU  350  CB  ASN B  47     8535   7661   6100    310    473    866       C  
ATOM    351  CG  ASN B  47      39.368  23.554  -0.918  1.00 64.05           C  
ANISOU  351  CG  ASN B  47     9152   8322   6864    325    365    920       C  
ATOM    352  OD1 ASN B  47      38.551  22.745  -1.359  1.00 67.76           O  
ANISOU  352  OD1 ASN B  47     9643   8895   7207    304    302    878       O  
ATOM    353  ND2 ASN B  47      39.016  24.748  -0.458  1.00 64.92           N  
ANISOU  353  ND2 ASN B  47     9175   8294   7198    363    341   1008       N  
ATOM    354  N   GLN B  48      43.314  22.183   1.649  1.00 48.56           N  
ANISOU  354  N   GLN B  48     7316   6216   4918    337    703    517       N  
ATOM    355  CA  GLN B  48      44.756  22.194   1.855  1.00 47.84           C  
ANISOU  355  CA  GLN B  48     7235   6123   4820    337    792    493       C  
ATOM    356  C   GLN B  48      45.419  21.053   1.093  1.00 46.17           C  
ANISOU  356  C   GLN B  48     7094   6045   4404    333    833    434       C  
ATOM    357  O   GLN B  48      45.126  19.880   1.368  1.00 45.21           O  
ANISOU  357  O   GLN B  48     7027   5941   4210    343    825    302       O  
ATOM    358  CB  GLN B  48      45.077  22.089   3.341  1.00 45.66           C  
ANISOU  358  CB  GLN B  48     6940   5737   4670    353    828    365       C  
ATOM    359  CG  GLN B  48      44.432  23.172   4.186  1.00 48.18           C  
ANISOU  359  CG  GLN B  48     7188   5927   5192    359    800    382       C  
ATOM    360  CD  GLN B  48      43.270  22.651   4.999  1.00 47.62           C  
ANISOU  360  CD  GLN B  48     7115   5826   5152    369    760    275       C  
ATOM    361  OE1 GLN B  48      42.287  22.156   4.450  1.00 47.48           O  
ANISOU  361  OE1 GLN B  48     7115   5865   5059    366    703    288       O  
ATOM    362  NE2 GLN B  48      43.379  22.755   6.318  1.00 46.56           N  
ANISOU  362  NE2 GLN B  48     6955   5615   5122    371    789    169       N  
ATOM    363  N   PRO B  49      46.310  21.339   0.152  1.00 41.24           N  
ANISOU  363  N   PRO B  49     6468   5514   3687    316    882    522       N  
ATOM    364  CA  PRO B  49      46.899  20.284  -0.671  1.00 40.67           C  
ANISOU  364  CA  PRO B  49     6455   5582   3414    317    929    452       C  
ATOM    365  C   PRO B  49      48.117  19.652  -0.007  1.00 40.94           C  
ANISOU  365  C   PRO B  49     6495   5594   3466    351   1015    330       C  
ATOM    366  O   PRO B  49      48.669  20.163   0.970  1.00 41.30           O  
ANISOU  366  O   PRO B  49     6492   5540   3660    360   1042    325       O  
ATOM    367  CB  PRO B  49      47.306  21.044  -1.938  1.00 43.22           C  
ANISOU  367  CB  PRO B  49     6756   6028   3637    278    949    619       C  
ATOM    368  CG  PRO B  49      47.720  22.385  -1.408  1.00 44.19           C  
ANISOU  368  CG  PRO B  49     6802   6036   3951    266    962    743       C  
ATOM    369  CD  PRO B  49      46.808  22.673  -0.228  1.00 42.84           C  
ANISOU  369  CD  PRO B  49     6609   5698   3970    291    899    693       C  
ATOM    370  N   ALA B  50      48.519  18.510  -0.555  1.00 49.35           N  
ANISOU  370  N   ALA B  50     7616   6756   4380    369   1054    223       N  
ATOM    371  CA  ALA B  50      49.828  17.960  -0.256  1.00 47.92           C  
ANISOU  371  CA  ALA B  50     7425   6586   4196    409   1143    132       C  
ATOM    372  C   ALA B  50      50.890  18.749  -1.008  1.00 48.95           C  
ANISOU  372  C   ALA B  50     7496   6818   4283    387   1222    242       C  
ATOM    373  O   ALA B  50      50.639  19.298  -2.086  1.00 48.93           O  
ANISOU  373  O   ALA B  50     7490   6923   4177    341   1216    362       O  
ATOM    374  CB  ALA B  50      49.898  16.483  -0.643  1.00 45.79           C  
ANISOU  374  CB  ALA B  50     7230   6371   3797    446   1162    -26       C  
ATOM    375  N   VAL B  51      52.084  18.818  -0.428  1.00 49.85           N  
ANISOU  375  N   VAL B  51     7555   6908   4476    411   1293    212       N  
ATOM    376  CA  VAL B  51      53.197  19.539  -1.035  1.00 51.47           C  
ANISOU  376  CA  VAL B  51     7690   7211   4656    382   1378    311       C  
ATOM    377  C   VAL B  51      54.308  18.541  -1.322  1.00 50.46           C  
ANISOU  377  C   VAL B  51     7553   7183   4436    436   1473    185       C  
ATOM    378  O   VAL B  51      54.760  17.825  -0.417  1.00 48.40           O  
ANISOU  378  O   VAL B  51     7287   6846   4256    496   1480     64       O  
ATOM    379  CB  VAL B  51      53.696  20.689  -0.147  1.00 51.97           C  
ANISOU  379  CB  VAL B  51     7671   7164   4913    352   1380    398       C  
ATOM    380  CG1 VAL B  51      54.931  21.324  -0.763  1.00 53.05           C  
ANISOU  380  CG1 VAL B  51     7727   7405   5024    313   1474    494       C  
ATOM    381  CG2 VAL B  51      52.598  21.729   0.027  1.00 49.69           C  
ANISOU  381  CG2 VAL B  51     7384   6770   4727    309   1293    517       C  
ATOM    382  N   PHE B  52      54.739  18.497  -2.581  1.00 54.99           N  
ANISOU  382  N   PHE B  52     8120   7933   4839    415   1544    217       N  
ATOM    383  CA  PHE B  52      55.749  17.565  -3.064  1.00 54.57           C  
ANISOU  383  CA  PHE B  52     8052   8002   4681    469   1648     87       C  
ATOM    384  C   PHE B  52      56.997  18.348  -3.453  1.00 56.23           C  
ANISOU  384  C   PHE B  52     8152   8325   4887    433   1753    188       C  
ATOM    385  O   PHE B  52      56.964  19.147  -4.396  1.00 58.65           O  
ANISOU  385  O   PHE B  52     8439   8753   5091    355   1779    337       O  
ATOM    386  CB  PHE B  52      55.215  16.765  -4.256  1.00 53.79           C  
ANISOU  386  CB  PHE B  52     8032   8043   4362    469   1658      8       C  
ATOM    387  CG  PHE B  52      56.128  15.658  -4.713  1.00 54.88           C  
ANISOU  387  CG  PHE B  52     8164   8285   4403    541   1764   -170       C  
ATOM    388  CD1 PHE B  52      57.136  15.903  -5.633  1.00 55.09           C  
ANISOU  388  CD1 PHE B  52     8118   8507   4305    523   1888   -144       C  
ATOM    389  CD2 PHE B  52      55.964  14.368  -4.236  1.00 54.96           C  
ANISOU  389  CD2 PHE B  52     8235   8196   4451    625   1741   -364       C  
ATOM    390  CE1 PHE B  52      57.971  14.884  -6.059  1.00 56.59           C  
ANISOU  390  CE1 PHE B  52     8292   8797   4415    600   1994   -326       C  
ATOM    391  CE2 PHE B  52      56.794  13.346  -4.658  1.00 55.29           C  
ANISOU  391  CE2 PHE B  52     8267   8312   4428    704   1838   -538       C  
ATOM    392  CZ  PHE B  52      57.799  13.604  -5.570  1.00 56.30           C  
ANISOU  392  CZ  PHE B  52     8317   8640   4435    696   1967   -529       C  
ATOM    393  N   PHE B  53      58.082  18.126  -2.716  1.00 50.65           N  
ANISOU  393  N   PHE B  53     7368   7582   4293    484   1809    119       N  
ATOM    394  CA  PHE B  53      59.390  18.688  -3.021  1.00 51.45           C  
ANISOU  394  CA  PHE B  53     7349   7800   4399    456   1918    185       C  
ATOM    395  C   PHE B  53      60.168  17.698  -3.874  1.00 57.53           C  
ANISOU  395  C   PHE B  53     8098   8745   5015    518   2035     49       C  
ATOM    396  O   PHE B  53      60.482  16.590  -3.415  1.00 56.08           O  
ANISOU  396  O   PHE B  53     7923   8513   4872    623   2046   -126       O  
ATOM    397  CB  PHE B  53      60.162  18.983  -1.741  1.00 51.43           C  
ANISOU  397  CB  PHE B  53     7259   7675   4606    476   1908    177       C  
ATOM    398  CG  PHE B  53      59.449  19.898  -0.811  1.00 54.89           C  
ANISOU  398  CG  PHE B  53     7714   7939   5202    422   1802    271       C  
ATOM    399  CD1 PHE B  53      58.629  19.395   0.182  1.00 52.65           C  
ANISOU  399  CD1 PHE B  53     7502   7500   5001    468   1704    184       C  
ATOM    400  CD2 PHE B  53      59.596  21.267  -0.930  1.00 56.81           C  
ANISOU  400  CD2 PHE B  53     7898   8170   5515    322   1805    445       C  
ATOM    401  CE1 PHE B  53      57.970  20.241   1.039  1.00 53.90           C  
ANISOU  401  CE1 PHE B  53     7668   7511   5299    421   1619    251       C  
ATOM    402  CE2 PHE B  53      58.941  22.117  -0.076  1.00 56.89           C  
ANISOU  402  CE2 PHE B  53     7921   8010   5686    279   1713    510       C  
ATOM    403  CZ  PHE B  53      58.128  21.603   0.909  1.00 55.10           C  
ANISOU  403  CZ  PHE B  53     7760   7645   5529    332   1624    404       C  
ATOM    404  N   GLU B  54      60.496  18.119  -5.100  1.00 79.93           N  
ANISOU  404  N   GLU B  54    10901  11786   7681    453   2125    133       N  
ATOM    405  CA  GLU B  54      61.196  17.275  -6.061  1.00 81.93           C  
ANISOU  405  CA  GLU B  54    11130  12241   7760    501   2252     -1       C  
ATOM    406  C   GLU B  54      62.683  17.169  -5.745  1.00 82.90           C  
ANISOU  406  C   GLU B  54    11107  12421   7970    551   2367    -55       C  
ATOM    407  O   GLU B  54      63.281  16.101  -5.919  1.00 83.32           O  
ANISOU  407  O   GLU B  54    11136  12536   7986    655   2445   -244       O  
ATOM    408  CB  GLU B  54      60.994  17.827  -7.476  1.00 82.11           C  
ANISOU  408  CB  GLU B  54    11163  12489   7548    398   2307    122       C  
ATOM    409  CG  GLU B  54      59.537  17.877  -7.927  1.00 82.53           C  
ANISOU  409  CG  GLU B  54    11348  12519   7491    350   2191    175       C  
ATOM    410  CD  GLU B  54      59.381  17.846  -9.437  1.00 85.08           C  
ANISOU  410  CD  GLU B  54    11697  13107   7521    283   2254    206       C  
ATOM    411  OE1 GLU B  54      60.407  17.864 -10.149  1.00 86.69           O  
ANISOU  411  OE1 GLU B  54    11816  13519   7602    265   2398    196       O  
ATOM    412  OE2 GLU B  54      58.226  17.797  -9.913  1.00 85.10           O  
ANISOU  412  OE2 GLU B  54    11800  13124   7409    244   2159    238       O  
ATOM    413  N   LYS B  55      63.301  18.258  -5.290  1.00 72.73           N  
ANISOU  413  N   LYS B  55     9714  11110   6809    479   2376    104       N  
ATOM    414  CA  LYS B  55      64.726  18.257  -4.987  1.00 75.20           C  
ANISOU  414  CA  LYS B  55     9870  11490   7212    511   2478     70       C  
ATOM    415  C   LYS B  55      65.005  19.140  -3.781  1.00 74.24           C  
ANISOU  415  C   LYS B  55     9681  11205   7322    466   2404    178       C  
ATOM    416  O   LYS B  55      64.611  20.309  -3.756  1.00 75.66           O  
ANISOU  416  O   LYS B  55     9869  11333   7546    349   2355    360       O  
ATOM    417  CB  LYS B  55      65.550  18.733  -6.190  1.00 78.32           C  
ANISOU  417  CB  LYS B  55    10164  12149   7445    433   2630    154       C  
ATOM    418  N   ILE B  56      65.685  18.572  -2.788  1.00 59.93           N  
ANISOU  418  N   ILE B  56     7801   9311   5659    559   2392     64       N  
ATOM    419  CA  ILE B  56      66.143  19.292  -1.606  1.00 59.70           C  
ANISOU  419  CA  ILE B  56     7687   9157   5837    521   2331    133       C  
ATOM    420  C   ILE B  56      67.663  19.335  -1.651  1.00 59.66           C  
ANISOU  420  C   ILE B  56     7496   9294   5879    531   2444    119       C  
ATOM    421  O   ILE B  56      68.307  18.336  -1.991  1.00 59.01           O  
ANISOU  421  O   ILE B  56     7361   9318   5743    642   2529    -21       O  
ATOM    422  CB  ILE B  56      65.643  18.627  -0.307  1.00 56.86           C  
ANISOU  422  CB  ILE B  56     7397   8596   5610    609   2205     27       C  
ATOM    423  CG1 ILE B  56      64.128  18.413  -0.363  1.00 55.18           C  
ANISOU  423  CG1 ILE B  56     7360   8270   5336    606   2108     20       C  
ATOM    424  CG2 ILE B  56      66.018  19.464   0.908  1.00 56.06           C  
ANISOU  424  CG2 ILE B  56     7218   8383   5701    550   2134     97       C  
ATOM    425  CD1 ILE B  56      63.717  17.006  -0.749  1.00 53.85           C  
ANISOU  425  CD1 ILE B  56     7286   8112   5064    721   2115   -145       C  
ATOM    426  N   LYS B  57      68.235  20.492  -1.317  1.00 69.72           N  
ANISOU  426  N   LYS B  57     8663  10564   7263    416   2447    258       N  
ATOM    427  CA  LYS B  57      69.671  20.686  -1.480  1.00 71.80           C  
ANISOU  427  CA  LYS B  57     8733  10986   7563    397   2561    271       C  
ATOM    428  C   LYS B  57      70.455  19.708  -0.614  1.00 71.22           C  
ANISOU  428  C   LYS B  57     8569  10889   7600    538   2549    112       C  
ATOM    429  O   LYS B  57      70.219  19.595   0.592  1.00 68.56           O  
ANISOU  429  O   LYS B  57     8261  10384   7403    572   2425     78       O  
ATOM    430  CB  LYS B  57      70.066  22.120  -1.133  1.00 72.73           C  
ANISOU  430  CB  LYS B  57     8760  11067   7808    235   2543    446       C  
ATOM    431  CG  LYS B  57      71.530  22.419  -1.430  1.00 76.02           C  
ANISOU  431  CG  LYS B  57     8965  11668   8251    188   2670    481       C  
ATOM    432  CD  LYS B  57      71.897  23.851  -1.092  1.00 79.26           C  
ANISOU  432  CD  LYS B  57     9290  12025   8800     12   2647    655       C  
ATOM    433  CE  LYS B  57      71.622  24.158   0.369  1.00 80.37           C  
ANISOU  433  CE  LYS B  57     9456  11940   9139      7   2494    621       C  
ATOM    434  NZ  LYS B  57      71.753  25.614   0.656  1.00 81.73           N  
ANISOU  434  NZ  LYS B  57     9579  12023   9452   -172   2459    778       N  
ATOM    435  N   GLY B  58      71.398  19.005  -1.242  1.00 68.26           N  
ANISOU  435  N   GLY B  58     8079  10694   7161    622   2679     18       N  
ATOM    436  CA  GLY B  58      72.194  18.003  -0.574  1.00 68.45           C  
ANISOU  436  CA  GLY B  58     8005  10711   7292    775   2676   -130       C  
ATOM    437  C   GLY B  58      71.651  16.593  -0.658  1.00 67.16           C  
ANISOU  437  C   GLY B  58     7959  10481   7076    942   2655   -305       C  
ATOM    438  O   GLY B  58      72.383  15.648  -0.341  1.00 68.35           O  
ANISOU  438  O   GLY B  58     8020  10644   7306   1087   2676   -433       O  
ATOM    439  N   TYR B  59      70.404  16.418  -1.082  1.00 66.51           N  
ANISOU  439  N   TYR B  59     8069  10326   6877    927   2611   -314       N  
ATOM    440  CA  TYR B  59      69.760  15.115  -1.108  1.00 64.79           C  
ANISOU  440  CA  TYR B  59     7980  10016   6622   1065   2574   -476       C  
ATOM    441  C   TYR B  59      69.464  14.682  -2.538  1.00 64.98           C  
ANISOU  441  C   TYR B  59     8066  10191   6432   1077   2691   -557       C  
ATOM    442  O   TYR B  59      69.359  15.501  -3.455  1.00 66.99           O  
ANISOU  442  O   TYR B  59     8318  10594   6543    954   2763   -449       O  
ATOM    443  CB  TYR B  59      68.465  15.131  -0.289  1.00 62.15           C  
ANISOU  443  CB  TYR B  59     7819   9461   6334   1039   2409   -443       C  
ATOM    444  CG  TYR B  59      68.688  15.233   1.202  1.00 62.03           C  
ANISOU  444  CG  TYR B  59     7761   9296   6511   1056   2288   -413       C  
ATOM    445  CD1 TYR B  59      69.283  14.193   1.906  1.00 63.14           C  
ANISOU  445  CD1 TYR B  59     7847   9380   6765   1199   2257   -521       C  
ATOM    446  CD2 TYR B  59      68.303  16.366   1.907  1.00 62.63           C  
ANISOU  446  CD2 TYR B  59     7850   9290   6656    927   2201   -278       C  
ATOM    447  CE1 TYR B  59      69.486  14.278   3.271  1.00 63.24           C  
ANISOU  447  CE1 TYR B  59     7819   9279   6930   1206   2139   -484       C  
ATOM    448  CE2 TYR B  59      68.502  16.460   3.272  1.00 62.92           C  
ANISOU  448  CE2 TYR B  59     7849   9212   6847    933   2092   -265       C  
ATOM    449  CZ  TYR B  59      69.094  15.413   3.949  1.00 63.39           C  
ANISOU  449  CZ  TYR B  59     7854   9238   6992   1068   2059   -362       C  
ATOM    450  OH  TYR B  59      69.295  15.504   5.307  1.00 64.34           O  
ANISOU  450  OH  TYR B  59     7934   9267   7244   1065   1943   -338       O  
ATOM    451  N   LYS B  60      69.323  13.368  -2.711  1.00 75.97           N  
ANISOU  451  N   LYS B  60     9518  11543   7804   1222   2703   -748       N  
ATOM    452  CA  LYS B  60      69.067  12.768  -4.015  1.00 75.89           C  
ANISOU  452  CA  LYS B  60     9570  11673   7592   1250   2811   -874       C  
ATOM    453  C   LYS B  60      67.583  12.713  -4.351  1.00 76.35           C  
ANISOU  453  C   LYS B  60     9838  11648   7526   1187   2721   -862       C  
ATOM    454  O   LYS B  60      67.197  12.970  -5.496  1.00 76.59           O  
ANISOU  454  O   LYS B  60     9917  11838   7346   1110   2789   -847       O  
ATOM    455  CB  LYS B  60      69.634  11.342  -4.077  1.00 76.00           C  
ANISOU  455  CB  LYS B  60     9547  11669   7662   1441   2871  -1110       C  
ATOM    456  CG  LYS B  60      71.157  11.207  -4.069  1.00 78.66           C  
ANISOU  456  CG  LYS B  60     9657  12139   8090   1530   2995  -1165       C  
ATOM    457  CD  LYS B  60      71.707  11.394  -2.671  1.00 78.31           C  
ANISOU  457  CD  LYS B  60     9515  11953   8287   1565   2887  -1079       C  
ATOM    458  CE  LYS B  60      71.007  10.483  -1.695  1.00 77.36           C  
ANISOU  458  CE  LYS B  60     9526  11568   8298   1666   2730  -1143       C  
ATOM    459  NZ  LYS B  60      70.996  11.121  -0.353  1.00 76.58           N  
ANISOU  459  NZ  LYS B  60     9403  11338   8356   1608   2587   -988       N  
ATOM    460  N   TYR B  61      66.747  12.367  -3.377  1.00 70.24           N  
ANISOU  460  N   TYR B  61     9178  10640   6869   1216   2568   -865       N  
ATOM    461  CA  TYR B  61      65.357  12.016  -3.613  1.00 68.82           C  
ANISOU  461  CA  TYR B  61     9187  10366   6596   1187   2479   -897       C  
ATOM    462  C   TYR B  61      64.428  13.093  -3.046  1.00 68.39           C  
ANISOU  462  C   TYR B  61     9201  10210   6575   1057   2355   -703       C  
ATOM    463  O   TYR B  61      64.861  14.182  -2.661  1.00 69.37           O  
ANISOU  463  O   TYR B  61     9233  10353   6769    977   2354   -548       O  
ATOM    464  CB  TYR B  61      65.091  10.626  -3.033  1.00 67.33           C  
ANISOU  464  CB  TYR B  61     9077   9994   6513   1326   2414  -1073       C  
ATOM    465  CG  TYR B  61      65.997   9.569  -3.633  1.00 68.25           C  
ANISOU  465  CG  TYR B  61     9123  10193   6617   1466   2539  -1278       C  
ATOM    466  CD1 TYR B  61      66.742   8.720  -2.825  1.00 69.02           C  
ANISOU  466  CD1 TYR B  61     9148  10167   6909   1614   2523  -1372       C  
ATOM    467  CD2 TYR B  61      66.118   9.434  -5.011  1.00 69.72           C  
ANISOU  467  CD2 TYR B  61     9307  10589   6596   1451   2673  -1379       C  
ATOM    468  CE1 TYR B  61      67.574   7.759  -3.373  1.00 70.87           C  
ANISOU  468  CE1 TYR B  61     9306  10463   7156   1756   2640  -1568       C  
ATOM    469  CE2 TYR B  61      66.947   8.475  -5.567  1.00 71.36           C  
ANISOU  469  CE2 TYR B  61     9439  10856   6818   1559   2782  -1583       C  
ATOM    470  CZ  TYR B  61      67.672   7.641  -4.743  1.00 71.97           C  
ANISOU  470  CZ  TYR B  61     9443  10799   7103   1730   2775  -1684       C  
ATOM    471  OH  TYR B  61      68.498   6.686  -5.288  1.00 74.79           O  
ANISOU  471  OH  TYR B  61     9718  11179   7521   1825   2868  -1882       O  
ATOM    472  N   SER B  62      63.139  12.775  -2.993  1.00 69.52           N  
ANISOU  472  N   SER B  62     9499  10237   6677   1037   2253   -723       N  
ATOM    473  CA  SER B  62      62.082  13.764  -2.838  1.00 70.13           C  
ANISOU  473  CA  SER B  62     9650  10259   6738    914   2156   -559       C  
ATOM    474  C   SER B  62      61.333  13.579  -1.523  1.00 67.00           C  
ANISOU  474  C   SER B  62     9324   9634   6500    931   2013   -551       C  
ATOM    475  O   SER B  62      61.384  12.519  -0.889  1.00 63.64           O  
ANISOU  475  O   SER B  62     8929   9092   6161   1030   1976   -675       O  
ATOM    476  CB  SER B  62      61.096  13.676  -4.010  1.00 71.65           C  
ANISOU  476  CB  SER B  62     9954  10548   6721    857   2155   -570       C  
ATOM    477  OG  SER B  62      60.408  12.435  -4.029  1.00 72.46           O  
ANISOU  477  OG  SER B  62    10171  10563   6798    928   2108   -742       O  
ATOM    478  N   VAL B  63      60.606  14.626  -1.132  1.00 59.75           N  
ANISOU  478  N   VAL B  63     8431   8652   5620    831   1933   -400       N  
ATOM    479  CA  VAL B  63      59.843  14.635   0.115  1.00 57.81           C  
ANISOU  479  CA  VAL B  63     8241   8215   5510    827   1807   -381       C  
ATOM    480  C   VAL B  63      58.405  15.014  -0.210  1.00 55.97           C  
ANISOU  480  C   VAL B  63     8115   7945   5205    751   1729   -318       C  
ATOM    481  O   VAL B  63      58.163  15.838  -1.094  1.00 56.72           O  
ANISOU  481  O   VAL B  63     8205   8143   5203    674   1754   -211       O  
ATOM    482  CB  VAL B  63      60.452  15.611   1.148  1.00 57.79           C  
ANISOU  482  CB  VAL B  63     8137   8158   5664    786   1785   -278       C  
ATOM    483  CG1 VAL B  63      59.501  15.845   2.324  1.00 55.74           C  
ANISOU  483  CG1 VAL B  63     7939   7730   5512    756   1661   -248       C  
ATOM    484  CG2 VAL B  63      61.775  15.082   1.658  1.00 59.39           C  
ANISOU  484  CG2 VAL B  63     8231   8380   5953    871   1834   -348       C  
ATOM    485  N   VAL B  64      57.446  14.395   0.467  1.00 45.65           N  
ANISOU  485  N   VAL B  64     6899   6500   3944    770   1633   -376       N  
ATOM    486  CA  VAL B  64      56.053  14.804   0.342  1.00 45.70           C  
ANISOU  486  CA  VAL B  64     6987   6461   3914    700   1548   -312       C  
ATOM    487  C   VAL B  64      55.464  14.970   1.736  1.00 46.56           C  
ANISOU  487  C   VAL B  64     7111   6407   4172    690   1454   -293       C  
ATOM    488  O   VAL B  64      55.729  14.167   2.640  1.00 46.70           O  
ANISOU  488  O   VAL B  64     7137   6337   4271    748   1430   -375       O  
ATOM    489  CB  VAL B  64      55.222  13.820  -0.515  1.00 43.31           C  
ANISOU  489  CB  VAL B  64     6791   6195   3470    713   1531   -416       C  
ATOM    490  CG1 VAL B  64      54.992  12.502   0.202  1.00 42.60           C  
ANISOU  490  CG1 VAL B  64     6767   5975   3445    782   1486   -559       C  
ATOM    491  CG2 VAL B  64      53.898  14.460  -0.920  1.00 44.78           C  
ANISOU  491  CG2 VAL B  64     7030   6388   3595    629   1454   -319       C  
ATOM    492  N   THR B  65      54.670  16.026   1.909  1.00 47.18           N  
ANISOU  492  N   THR B  65     7188   6449   4290    616   1400   -181       N  
ATOM    493  CA  THR B  65      54.130  16.363   3.216  1.00 46.68           C  
ANISOU  493  CA  THR B  65     7123   6252   4362    597   1325   -166       C  
ATOM    494  C   THR B  65      52.689  16.839   3.080  1.00 46.55           C  
ANISOU  494  C   THR B  65     7156   6195   4336    543   1252   -111       C  
ATOM    495  O   THR B  65      52.226  17.193   1.991  1.00 46.31           O  
ANISOU  495  O   THR B  65     7144   6241   4210    510   1254    -46       O  
ATOM    496  CB  THR B  65      54.979  17.433   3.916  1.00 46.99           C  
ANISOU  496  CB  THR B  65     7061   6269   4524    569   1347    -95       C  
ATOM    497  OG1 THR B  65      54.584  17.534   5.290  1.00 47.96           O  
ANISOU  497  OG1 THR B  65     7183   6277   4761    559   1282   -121       O  
ATOM    498  CG2 THR B  65      54.807  18.785   3.237  1.00 45.49           C  
ANISOU  498  CG2 THR B  65     6831   6113   4339    496   1361     43       C  
ATOM    499  N   ASN B  66      51.991  16.840   4.220  1.00 41.55           N  
ANISOU  499  N   ASN B  66     6536   5450   3799    533   1187   -134       N  
ATOM    500  CA  ASN B  66      50.576  17.210   4.308  1.00 39.55           C  
ANISOU  500  CA  ASN B  66     6315   5149   3563    492   1115   -101       C  
ATOM    501  C   ASN B  66      49.716  16.330   3.405  1.00 38.86           C  
ANISOU  501  C   ASN B  66     6308   5111   3347    493   1085   -142       C  
ATOM    502  O   ASN B  66      48.750  16.791   2.793  1.00 40.80           O  
ANISOU  502  O   ASN B  66     6564   5382   3556    455   1042    -78       O  
ATOM    503  CB  ASN B  66      50.361  18.692   3.990  1.00 41.17           C  
ANISOU  503  CB  ASN B  66     6462   5352   3830    445   1111     29       C  
ATOM    504  CG  ASN B  66      49.103  19.248   4.637  1.00 44.21           C  
ANISOU  504  CG  ASN B  66     6841   5647   4308    418   1041     47       C  
ATOM    505  OD1 ASN B  66      48.890  19.096   5.840  1.00 44.25           O  
ANISOU  505  OD1 ASN B  66     6840   5577   4395    420   1020    -21       O  
ATOM    506  ND2 ASN B  66      48.261  19.891   3.837  1.00 46.17           N  
ANISOU  506  ND2 ASN B  66     7086   5914   4541    393   1004    142       N  
ATOM    507  N   VAL B  67      50.063  15.044   3.337  1.00 39.19           N  
ANISOU  507  N   VAL B  67     6404   5159   3328    535   1102   -252       N  
ATOM    508  CA  VAL B  67      49.347  14.122   2.461  1.00 39.78           C  
ANISOU  508  CA  VAL B  67     6558   5275   3280    531   1076   -318       C  
ATOM    509  C   VAL B  67      47.909  13.935   2.934  1.00 40.33           C  
ANISOU  509  C   VAL B  67     6666   5278   3380    488    988   -325       C  
ATOM    510  O   VAL B  67      46.982  13.842   2.121  1.00 39.89           O  
ANISOU  510  O   VAL B  67     6644   5276   3238    451    945   -318       O  
ATOM    511  CB  VAL B  67      50.107  12.786   2.376  1.00 39.37           C  
ANISOU  511  CB  VAL B  67     6551   5215   3191    593   1117   -449       C  
ATOM    512  CG1 VAL B  67      49.234  11.704   1.766  1.00 39.79           C  
ANISOU  512  CG1 VAL B  67     6697   5268   3152    580   1075   -547       C  
ATOM    513  CG2 VAL B  67      51.384  12.962   1.566  1.00 40.17           C  
ANISOU  513  CG2 VAL B  67     6608   5426   3231    632   1213   -450       C  
ATOM    514  N   HIS B  68      47.696  13.894   4.249  1.00 45.86           N  
ANISOU  514  N   HIS B  68     7352   5877   4195    485    961   -338       N  
ATOM    515  CA  HIS B  68      46.368  13.732   4.827  1.00 46.14           C  
ANISOU  515  CA  HIS B  68     7407   5857   4266    440    890   -346       C  
ATOM    516  C   HIS B  68      45.753  15.049   5.286  1.00 46.25           C  
ANISOU  516  C   HIS B  68     7348   5855   4370    409    867   -259       C  
ATOM    517  O   HIS B  68      44.702  15.034   5.933  1.00 48.25           O  
ANISOU  517  O   HIS B  68     7595   6067   4671    376    820   -270       O  
ATOM    518  CB  HIS B  68      46.421  12.768   6.016  1.00 44.88           C  
ANISOU  518  CB  HIS B  68     7280   5608   4164    448    874   -417       C  
ATOM    519  CG  HIS B  68      46.701  11.345   5.646  1.00 45.62           C  
ANISOU  519  CG  HIS B  68     7455   5679   4201    476    876   -510       C  
ATOM    520  ND1 HIS B  68      47.972  10.879   5.390  1.00 45.19           N  
ANISOU  520  ND1 HIS B  68     7405   5630   4135    544    932   -552       N  
ATOM    521  CD2 HIS B  68      45.876  10.280   5.513  1.00 45.29           C  
ANISOU  521  CD2 HIS B  68     7486   5596   4127    445    829   -576       C  
ATOM    522  CE1 HIS B  68      47.917   9.590   5.105  1.00 45.96           C  
ANISOU  522  CE1 HIS B  68     7579   5681   4202    563    920   -646       C  
ATOM    523  NE2 HIS B  68      46.656   9.202   5.174  1.00 45.63           N  
ANISOU  523  NE2 HIS B  68     7584   5606   4147    498    855   -661       N  
ATOM    524  N   GLY B  69      46.370  16.184   4.961  1.00 36.93           N  
ANISOU  524  N   GLY B  69     6108   4702   3222    417    902   -176       N  
ATOM    525  CA  GLY B  69      46.075  17.425   5.655  1.00 36.48           C  
ANISOU  525  CA  GLY B  69     5977   4591   3293    400    892   -115       C  
ATOM    526  C   GLY B  69      44.880  18.240   5.201  1.00 38.48           C  
ANISOU  526  C   GLY B  69     6197   4846   3577    375    840    -39       C  
ATOM    527  O   GLY B  69      44.938  19.473   5.226  1.00 42.12           O  
ANISOU  527  O   GLY B  69     6593   5273   4136    372    844     43       O  
ATOM    528  N   SER B  70      43.790  17.586   4.811  1.00 36.97           N  
ANISOU  528  N   SER B  70     6043   4685   3320    356    784    -62       N  
ATOM    529  CA  SER B  70      42.573  18.297   4.434  1.00 39.18           C  
ANISOU  529  CA  SER B  70     6277   4972   3638    337    722     11       C  
ATOM    530  C   SER B  70      41.435  17.297   4.338  1.00 38.73           C  
ANISOU  530  C   SER B  70     6258   4944   3513    307    663    -52       C  
ATOM    531  O   SER B  70      41.656  16.090   4.209  1.00 39.11           O  
ANISOU  531  O   SER B  70     6381   5014   3465    298    669   -135       O  
ATOM    532  CB  SER B  70      42.729  19.042   3.104  1.00 41.26           C  
ANISOU  532  CB  SER B  70     6524   5306   3845    337    710    140       C  
ATOM    533  OG  SER B  70      42.633  18.149   2.007  1.00 40.09           O  
ANISOU  533  OG  SER B  70     6443   5268   3522    321    691    122       O  
ATOM    534  N   TRP B  71      40.208  17.819   4.392  1.00 37.13           N  
ANISOU  534  N   TRP B  71     5996   4737   3376    292    605    -12       N  
ATOM    535  CA  TRP B  71      39.047  16.962   4.205  1.00 37.27           C  
ANISOU  535  CA  TRP B  71     6033   4796   3334    252    541    -59       C  
ATOM    536  C   TRP B  71      38.890  16.534   2.755  1.00 38.74           C  
ANISOU  536  C   TRP B  71     6266   5089   3365    231    495    -26       C  
ATOM    537  O   TRP B  71      38.266  15.502   2.492  1.00 40.48           O  
ANISOU  537  O   TRP B  71     6532   5348   3500    188    453    -97       O  
ATOM    538  CB  TRP B  71      37.787  17.663   4.709  1.00 38.89           C  
ANISOU  538  CB  TRP B  71     6139   4975   3661    246    496    -30       C  
ATOM    539  CG  TRP B  71      37.762  17.754   6.199  1.00 38.86           C  
ANISOU  539  CG  TRP B  71     6100   4893   3771    247    543   -105       C  
ATOM    540  CD1 TRP B  71      37.747  18.890   6.952  1.00 39.10           C  
ANISOU  540  CD1 TRP B  71     6047   4859   3950    279    572    -91       C  
ATOM    541  CD2 TRP B  71      37.785  16.658   7.122  1.00 35.28           C  
ANISOU  541  CD2 TRP B  71     5696   4423   3285    210    567   -208       C  
ATOM    542  NE1 TRP B  71      37.744  18.570   8.289  1.00 38.27           N  
ANISOU  542  NE1 TRP B  71     5934   4719   3887    260    615   -189       N  
ATOM    543  CE2 TRP B  71      37.768  17.206   8.419  1.00 36.49           C  
ANISOU  543  CE2 TRP B  71     5790   4524   3550    216    610   -247       C  
ATOM    544  CE3 TRP B  71      37.811  15.267   6.978  1.00 34.20           C  
ANISOU  544  CE3 TRP B  71     5649   4304   3041    170    553   -270       C  
ATOM    545  CZ2 TRP B  71      37.777  16.413   9.564  1.00 35.36           C  
ANISOU  545  CZ2 TRP B  71     5673   4369   3395    178    638   -328       C  
ATOM    546  CZ3 TRP B  71      37.821  14.481   8.116  1.00 33.70           C  
ANISOU  546  CZ3 TRP B  71     5612   4202   2989    136    577   -341       C  
ATOM    547  CH2 TRP B  71      37.803  15.055   9.392  1.00 33.46           C  
ANISOU  547  CH2 TRP B  71     5520   4140   3052    138    618   -360       C  
ATOM    548  N   GLN B  72      39.460  17.287   1.814  1.00 40.42           N  
ANISOU  548  N   GLN B  72     6468   5356   3532    251    503     79       N  
ATOM    549  CA  GLN B  72      39.517  16.824   0.432  1.00 38.47           C  
ANISOU  549  CA  GLN B  72     6275   5238   3103    226    474     98       C  
ATOM    550  C   GLN B  72      40.454  15.629   0.303  1.00 39.19           C  
ANISOU  550  C   GLN B  72     6463   5346   3082    227    536    -31       C  
ATOM    551  O   GLN B  72      40.092  14.600  -0.283  1.00 37.93           O  
ANISOU  551  O   GLN B  72     6366   5246   2799    192    503   -118       O  
ATOM    552  CB  GLN B  72      39.961  17.964  -0.486  1.00 39.83           C  
ANISOU  552  CB  GLN B  72     6410   5475   3250    239    475    258       C  
ATOM    553  CG  GLN B  72      38.863  18.959  -0.838  1.00 42.09           C  
ANISOU  553  CG  GLN B  72     6611   5775   3606    235    383    402       C  
ATOM    554  CD  GLN B  72      38.364  19.743   0.362  1.00 47.21           C  
ANISOU  554  CD  GLN B  72     7174   6281   4482    269    381    412       C  
ATOM    555  OE1 GLN B  72      39.120  20.029   1.293  1.00 46.86           O  
ANISOU  555  OE1 GLN B  72     7123   6135   4546    296    456    368       O  
ATOM    556  NE2 GLN B  72      37.084  20.097   0.345  1.00 48.80           N  
ANISOU  556  NE2 GLN B  72     7302   6485   4757    268    295    461       N  
ATOM    557  N   ASN B  73      41.670  15.751   0.846  1.00 44.81           N  
ANISOU  557  N   ASN B  73     7182   6001   3845    269    622    -50       N  
ATOM    558  CA  ASN B  73      42.603  14.629   0.842  1.00 43.62           C  
ANISOU  558  CA  ASN B  73     7106   5846   3620    288    682   -174       C  
ATOM    559  C   ASN B  73      42.035  13.443   1.610  1.00 44.00           C  
ANISOU  559  C   ASN B  73     7205   5815   3699    269    653   -297       C  
ATOM    560  O   ASN B  73      42.192  12.289   1.194  1.00 43.62           O  
ANISOU  560  O   ASN B  73     7234   5779   3563    262    657   -406       O  
ATOM    561  CB  ASN B  73      43.944  15.057   1.440  1.00 41.71           C  
ANISOU  561  CB  ASN B  73     6838   5554   3455    337    768   -160       C  
ATOM    562  CG  ASN B  73      44.676  16.068   0.577  1.00 44.26           C  
ANISOU  562  CG  ASN B  73     7120   5961   3734    344    809    -43       C  
ATOM    563  OD1 ASN B  73      44.084  16.700  -0.299  1.00 44.95           O  
ANISOU  563  OD1 ASN B  73     7187   6128   3765    314    764     61       O  
ATOM    564  ND2 ASN B  73      45.972  16.228   0.823  1.00 42.75           N  
ANISOU  564  ND2 ASN B  73     6910   5759   3572    379    891    -48       N  
ATOM    565  N   HIS B  74      41.367  13.711   2.734  1.00 40.95           N  
ANISOU  565  N   HIS B  74     6775   5346   3440    255    627   -283       N  
ATOM    566  CA  HIS B  74      40.752  12.638   3.506  1.00 38.90           C  
ANISOU  566  CA  HIS B  74     6555   5017   3208    220    598   -375       C  
ATOM    567  C   HIS B  74      39.656  11.941   2.709  1.00 41.15           C  
ANISOU  567  C   HIS B  74     6874   5358   3403    159    524   -416       C  
ATOM    568  O   HIS B  74      39.573  10.707   2.700  1.00 41.46           O  
ANISOU  568  O   HIS B  74     6988   5361   3403    131    512   -519       O  
ATOM    569  CB  HIS B  74      40.195  13.199   4.815  1.00 38.65           C  
ANISOU  569  CB  HIS B  74     6454   4919   3312    209    593   -346       C  
ATOM    570  CG  HIS B  74      39.929  12.158   5.857  1.00 41.18           C  
ANISOU  570  CG  HIS B  74     6813   5166   3667    175    588   -421       C  
ATOM    571  ND1 HIS B  74      38.807  11.358   5.838  1.00 43.07           N  
ANISOU  571  ND1 HIS B  74     7073   5406   3885    106    530   -462       N  
ATOM    572  CD2 HIS B  74      40.632  11.796   6.956  1.00 41.13           C  
ANISOU  572  CD2 HIS B  74     6823   5089   3714    191    628   -449       C  
ATOM    573  CE1 HIS B  74      38.833  10.543   6.878  1.00 42.22           C  
ANISOU  573  CE1 HIS B  74     6999   5224   3819     79    540   -505       C  
ATOM    574  NE2 HIS B  74      39.930  10.789   7.572  1.00 39.86           N  
ANISOU  574  NE2 HIS B  74     6699   4884   3561    133    595   -495       N  
ATOM    575  N   ALA B  75      38.807  12.716   2.029  1.00 38.76           N  
ANISOU  575  N   ALA B  75     6513   5140   3076    135    467   -334       N  
ATOM    576  CA  ALA B  75      37.738  12.125   1.231  1.00 40.67           C  
ANISOU  576  CA  ALA B  75     6773   5455   3224     69    383   -367       C  
ATOM    577  C   ALA B  75      38.300  11.297   0.084  1.00 42.41           C  
ANISOU  577  C   ALA B  75     7085   5746   3282     61    392   -450       C  
ATOM    578  O   ALA B  75      37.767  10.230  -0.241  1.00 43.48           O  
ANISOU  578  O   ALA B  75     7279   5888   3353      3    348   -555       O  
ATOM    579  CB  ALA B  75      36.814  13.220   0.700  1.00 41.36           C  
ANISOU  579  CB  ALA B  75     6766   5627   3322     58    314   -241       C  
ATOM    580  N   LEU B  76      39.378  11.774  -0.543  1.00 44.09           N  
ANISOU  580  N   LEU B  76     7308   6017   3428    112    453   -413       N  
ATOM    581  CA  LEU B  76      40.004  10.996  -1.606  1.00 44.14           C  
ANISOU  581  CA  LEU B  76     7394   6104   3273    110    481   -511       C  
ATOM    582  C   LEU B  76      40.670   9.740  -1.060  1.00 42.35           C  
ANISOU  582  C   LEU B  76     7248   5760   3082    135    533   -665       C  
ATOM    583  O   LEU B  76      40.753   8.728  -1.765  1.00 41.78           O  
ANISOU  583  O   LEU B  76     7252   5715   2908    116    532   -798       O  
ATOM    584  CB  LEU B  76      41.015  11.856  -2.363  1.00 43.54           C  
ANISOU  584  CB  LEU B  76     7294   6131   3117    153    546   -424       C  
ATOM    585  CG  LEU B  76      40.402  12.973  -3.210  1.00 44.84           C  
ANISOU  585  CG  LEU B  76     7396   6428   3214    122    484   -263       C  
ATOM    586  CD1 LEU B  76      41.474  13.935  -3.699  1.00 44.38           C  
ANISOU  586  CD1 LEU B  76     7306   6440   3118    159    557   -146       C  
ATOM    587  CD2 LEU B  76      39.618  12.390  -4.379  1.00 44.94           C  
ANISOU  587  CD2 LEU B  76     7449   6585   3042     52    405   -314       C  
ATOM    588  N   MET B  77      41.147   9.785   0.186  1.00 45.84           N  
ANISOU  588  N   MET B  77     7672   6073   3672    178    575   -650       N  
ATOM    589  CA  MET B  77      41.697   8.589   0.816  1.00 45.06           C  
ANISOU  589  CA  MET B  77     7643   5849   3630    203    607   -769       C  
ATOM    590  C   MET B  77      40.648   7.487   0.908  1.00 46.51           C  
ANISOU  590  C   MET B  77     7883   5971   3817    127    534   -861       C  
ATOM    591  O   MET B  77      40.953   6.307   0.693  1.00 45.11           O  
ANISOU  591  O   MET B  77     7789   5728   3623    130    543   -991       O  
ATOM    592  CB  MET B  77      42.242   8.938   2.201  1.00 45.66           C  
ANISOU  592  CB  MET B  77     7677   5818   3853    247    645   -711       C  
ATOM    593  CG  MET B  77      42.663   7.744   3.043  1.00 44.86           C  
ANISOU  593  CG  MET B  77     7638   5578   3831    267    657   -796       C  
ATOM    594  SD  MET B  77      42.991   8.206   4.755  1.00 45.14           S  
ANISOU  594  SD  MET B  77     7616   5522   4013    288    675   -710       S  
ATOM    595  CE  MET B  77      41.332   8.545   5.343  1.00 44.58           C  
ANISOU  595  CE  MET B  77     7503   5457   3979    189    603   -657       C  
ATOM    596  N   LEU B  78      39.406   7.854   1.216  1.00 48.12           N  
ANISOU  596  N   LEU B  78     8038   6192   4054     57    463   -797       N  
ATOM    597  CA  LEU B  78      38.297   6.911   1.278  1.00 49.07           C  
ANISOU  597  CA  LEU B  78     8194   6271   4178    -35    388   -868       C  
ATOM    598  C   LEU B  78      37.698   6.611  -0.091  1.00 52.94           C  
ANISOU  598  C   LEU B  78     8714   6881   4520    -95    328   -934       C  
ATOM    599  O   LEU B  78      36.684   5.907  -0.166  1.00 53.98           O  
ANISOU  599  O   LEU B  78     8864   6998   4648   -186    254   -993       O  
ATOM    600  CB  LEU B  78      37.208   7.445   2.212  1.00 49.45           C  
ANISOU  600  CB  LEU B  78     8158   6306   4325    -87    343   -776       C  
ATOM    601  CG  LEU B  78      37.626   7.729   3.656  1.00 48.37           C  
ANISOU  601  CG  LEU B  78     7988   6071   4319    -50    394   -721       C  
ATOM    602  CD1 LEU B  78      36.499   8.417   4.409  1.00 47.78           C  
ANISOU  602  CD1 LEU B  78     7814   6021   4321    -99    361   -644       C  
ATOM    603  CD2 LEU B  78      38.042   6.446   4.360  1.00 50.54           C  
ANISOU  603  CD2 LEU B  78     8348   6208   4648    -61    410   -797       C  
ATOM    604  N   GLY B  79      38.290   7.128  -1.166  1.00 56.52           N  
ANISOU  604  N   GLY B  79     9168   7464   4845    -55    356   -923       N  
ATOM    605  CA  GLY B  79      37.776   6.880  -2.498  1.00 55.90           C  
ANISOU  605  CA  GLY B  79     9116   7528   4597   -117    298   -985       C  
ATOM    606  C   GLY B  79      36.509   7.627  -2.839  1.00 56.71           C  
ANISOU  606  C   GLY B  79     9135   7748   4665   -185    197   -874       C  
ATOM    607  O   GLY B  79      35.772   7.200  -3.731  1.00 59.08           O  
ANISOU  607  O   GLY B  79     9454   8151   4843   -265    119   -936       O  
ATOM    608  N   LEU B  80      36.237   8.736  -2.162  1.00 48.91           N  
ANISOU  608  N   LEU B  80     8049   6749   3785   -154    194   -718       N  
ATOM    609  CA  LEU B  80      35.020   9.507  -2.358  1.00 50.72           C  
ANISOU  609  CA  LEU B  80     8180   7070   4023   -200     98   -602       C  
ATOM    610  C   LEU B  80      35.324  10.792  -3.118  1.00 52.79           C  
ANISOU  610  C   LEU B  80     8383   7457   4219   -153     97   -449       C  
ATOM    611  O   LEU B  80      36.482  11.178  -3.304  1.00 52.78           O  
ANISOU  611  O   LEU B  80     8407   7461   4187    -89    181   -421       O  
ATOM    612  CB  LEU B  80      34.364   9.830  -1.010  1.00 50.80           C  
ANISOU  612  CB  LEU B  80     8111   6968   4222   -200     93   -546       C  
ATOM    613  CG  LEU B  80      34.158   8.638  -0.075  1.00 50.36           C  
ANISOU  613  CG  LEU B  80     8110   6778   4247   -249    106   -663       C  
ATOM    614  CD1 LEU B  80      33.738   9.100   1.312  1.00 49.40           C  
ANISOU  614  CD1 LEU B  80     7906   6571   4291   -240    127   -597       C  
ATOM    615  CD2 LEU B  80      33.132   7.678  -0.658  1.00 51.01           C  
ANISOU  615  CD2 LEU B  80     8218   6905   4258   -361     12   -756       C  
ATOM    616  N   ASP B  81      34.255  11.447  -3.570  1.00 54.60           N  
ANISOU  616  N   ASP B  81     8525   7789   4432   -189     -5   -340       N  
ATOM    617  CA  ASP B  81      34.381  12.779  -4.144  1.00 56.69           C  
ANISOU  617  CA  ASP B  81     8716   8146   4676   -146    -23   -156       C  
ATOM    618  C   ASP B  81      35.042  13.706  -3.132  1.00 56.97           C  
ANISOU  618  C   ASP B  81     8705   8049   4892    -60     62    -70       C  
ATOM    619  O   ASP B  81      34.690  13.701  -1.948  1.00 55.35           O  
ANISOU  619  O   ASP B  81     8460   7718   4852    -46     79    -96       O  
ATOM    620  CB  ASP B  81      33.005  13.310  -4.549  1.00 60.50           C  
ANISOU  620  CB  ASP B  81     9095   8726   5166   -188   -157    -46       C  
ATOM    621  CG  ASP B  81      33.079  14.644  -5.269  1.00 65.40           C  
ANISOU  621  CG  ASP B  81     9644   9442   5764   -147   -195    164       C  
ATOM    622  OD1 ASP B  81      33.192  15.685  -4.588  1.00 67.11           O  
ANISOU  622  OD1 ASP B  81     9784   9556   6157    -77   -165    281       O  
ATOM    623  OD2 ASP B  81      33.019  14.651  -6.518  1.00 67.93           O  
ANISOU  623  OD2 ASP B  81     9984   9938   5888   -190   -257    213       O  
ATOM    624  N   LYS B  82      36.016  14.492  -3.601  1.00 47.41           N  
ANISOU  624  N   LYS B  82     7496   6875   3640    -11    117     28       N  
ATOM    625  CA  LYS B  82      36.858  15.263  -2.690  1.00 47.51           C  
ANISOU  625  CA  LYS B  82     7480   6762   3811     61    208     82       C  
ATOM    626  C   LYS B  82      36.044  16.202  -1.808  1.00 49.08           C  
ANISOU  626  C   LYS B  82     7568   6868   4213     88    170    174       C  
ATOM    627  O   LYS B  82      36.431  16.466  -0.664  1.00 48.06           O  
ANISOU  627  O   LYS B  82     7419   6608   4235    128    237    146       O  
ATOM    628  CB  LYS B  82      37.902  16.054  -3.480  1.00 47.47           C  
ANISOU  628  CB  LYS B  82     7479   6830   3727     90    259    197       C  
ATOM    629  CG  LYS B  82      37.316  17.031  -4.484  1.00 50.96           C  
ANISOU  629  CG  LYS B  82     7858   7393   4112     73    170    387       C  
ATOM    630  CD  LYS B  82      38.402  17.685  -5.328  1.00 53.69           C  
ANISOU  630  CD  LYS B  82     8218   7828   4353     82    227    504       C  
ATOM    631  CE  LYS B  82      38.964  18.922  -4.643  1.00 57.56           C  
ANISOU  631  CE  LYS B  82     8642   8186   5042    137    278    634       C  
ATOM    632  NZ  LYS B  82      39.555  19.882  -5.617  1.00 60.00           N  
ANISOU  632  NZ  LYS B  82     8931   8593   5275    126    286    828       N  
ATOM    633  N   ASN B  83      34.919  16.706  -2.308  1.00 49.29           N  
ANISOU  633  N   ASN B  83     7515   6965   4247     68     64    275       N  
ATOM    634  CA  ASN B  83      34.099  17.653  -1.566  1.00 49.78           C  
ANISOU  634  CA  ASN B  83     7457   6944   4512    106     28    357       C  
ATOM    635  C   ASN B  83      33.057  16.972  -0.688  1.00 50.56           C  
ANISOU  635  C   ASN B  83     7519   7000   4693     72      2    244       C  
ATOM    636  O   ASN B  83      32.142  17.646  -0.202  1.00 52.48           O  
ANISOU  636  O   ASN B  83     7647   7208   5087     96    -39    297       O  
ATOM    637  CB  ASN B  83      33.418  18.625  -2.532  1.00 51.85           C  
ANISOU  637  CB  ASN B  83     7635   7298   4769    115    -78    544       C  
ATOM    638  CG  ASN B  83      34.414  19.481  -3.291  1.00 52.39           C  
ANISOU  638  CG  ASN B  83     7724   7397   4785    142    -48    691       C  
ATOM    639  OD1 ASN B  83      35.406  19.945  -2.730  1.00 53.02           O  
ANISOU  639  OD1 ASN B  83     7819   7371   4953    184     49    694       O  
ATOM    640  ND2 ASN B  83      34.157  19.688  -4.574  1.00 53.27           N  
ANISOU  640  ND2 ASN B  83     7832   7665   4744    110   -134    820       N  
ATOM    641  N   THR B  84      33.172  15.661  -0.480  1.00 44.76           N  
ANISOU  641  N   THR B  84     6874   6265   3869     17     26     92       N  
ATOM    642  CA  THR B  84      32.271  14.962   0.428  1.00 44.04           C  
ANISOU  642  CA  THR B  84     6753   6127   3854    -29     12     -7       C  
ATOM    643  C   THR B  84      32.357  15.573   1.821  1.00 43.14           C  
ANISOU  643  C   THR B  84     6575   5890   3928     21     85    -12       C  
ATOM    644  O   THR B  84      33.449  15.744   2.370  1.00 42.17           O  
ANISOU  644  O   THR B  84     6500   5686   3837     64    175    -32       O  
ATOM    645  CB  THR B  84      32.618  13.473   0.479  1.00 41.35           C  
ANISOU  645  CB  THR B  84     6535   5770   3405    -92     38   -159       C  
ATOM    646  OG1 THR B  84      32.386  12.881  -0.806  1.00 42.48           O  
ANISOU  646  OG1 THR B  84     6731   6037   3374   -149    -35   -183       O  
ATOM    647  CG2 THR B  84      31.769  12.757   1.517  1.00 40.53           C  
ANISOU  647  CG2 THR B  84     6404   5607   3389   -152     33   -243       C  
ATOM    648  N   SER B  85      31.200  15.916   2.383  1.00 43.40           N  
ANISOU  648  N   SER B  85     6490   5920   4080     13     48      0       N  
ATOM    649  CA  SER B  85      31.161  16.562   3.686  1.00 43.52           C  
ANISOU  649  CA  SER B  85     6430   5839   4267     57    118    -19       C  
ATOM    650  C   SER B  85      31.748  15.648   4.758  1.00 40.96           C  
ANISOU  650  C   SER B  85     6189   5446   3929     22    203   -139       C  
ATOM    651  O   SER B  85      31.787  14.422   4.620  1.00 40.37           O  
ANISOU  651  O   SER B  85     6203   5387   3748    -45    192   -211       O  
ATOM    652  CB  SER B  85      29.728  16.948   4.053  1.00 49.05           C  
ANISOU  652  CB  SER B  85     6981   6570   5087     51     67     -6       C  
ATOM    653  OG  SER B  85      28.963  15.808   4.404  1.00 49.05           O  
ANISOU  653  OG  SER B  85     6987   6611   5038    -43     48    -98       O  
ATOM    654  N   THR B  86      32.216  16.270   5.843  1.00 38.09           N  
ANISOU  654  N   THR B  86     5793   5002   3677     68    283   -158       N  
ATOM    655  CA  THR B  86      32.845  15.513   6.920  1.00 36.94           C  
ANISOU  655  CA  THR B  86     5718   4800   3516     39    358   -249       C  
ATOM    656  C   THR B  86      31.867  14.524   7.545  1.00 37.51           C  
ANISOU  656  C   THR B  86     5777   4899   3577    -50    342   -317       C  
ATOM    657  O   THR B  86      32.250  13.404   7.902  1.00 35.91           O  
ANISOU  657  O   THR B  86     5670   4669   3306   -103    361   -374       O  
ATOM    658  CB  THR B  86      33.397  16.472   7.976  1.00 38.08           C  
ANISOU  658  CB  THR B  86     5813   4877   3780     94    436   -259       C  
ATOM    659  OG1 THR B  86      34.291  17.405   7.354  1.00 36.36           O  
ANISOU  659  OG1 THR B  86     5604   4627   3584    164    447   -186       O  
ATOM    660  CG2 THR B  86      34.149  15.706   9.054  1.00 34.46           C  
ANISOU  660  CG2 THR B  86     5429   4377   3287     64    503   -335       C  
ATOM    661  N   LYS B  87      30.598  14.916   7.676  1.00 39.63           N  
ANISOU  661  N   LYS B  87     5919   5218   3919    -68    307   -306       N  
ATOM    662  CA  LYS B  87      29.591  14.007   8.218  1.00 40.65           C  
ANISOU  662  CA  LYS B  87     6018   5389   4038   -166    292   -361       C  
ATOM    663  C   LYS B  87      29.436  12.768   7.342  1.00 40.83           C  
ANISOU  663  C   LYS B  87     6138   5439   3938   -247    222   -379       C  
ATOM    664  O   LYS B  87      29.341  11.641   7.848  1.00 39.45           O  
ANISOU  664  O   LYS B  87     6025   5241   3724   -333    233   -435       O  
ATOM    665  CB  LYS B  87      28.257  14.742   8.358  1.00 43.94           C  
ANISOU  665  CB  LYS B  87     6262   5870   4564   -159    263   -343       C  
ATOM    666  CG  LYS B  87      27.168  13.954   9.064  1.00 45.95           C  
ANISOU  666  CG  LYS B  87     6453   6181   4824   -265    265   -398       C  
ATOM    667  CD  LYS B  87      25.806  14.604   8.860  1.00 51.40           C  
ANISOU  667  CD  LYS B  87     6961   6955   5613   -254    216   -373       C  
ATOM    668  CE  LYS B  87      25.488  14.774   7.379  1.00 54.97           C  
ANISOU  668  CE  LYS B  87     7403   7456   6026   -234     97   -295       C  
ATOM    669  NZ  LYS B  87      24.046  15.072   7.147  1.00 58.78           N  
ANISOU  669  NZ  LYS B  87     7708   8036   6588   -250     26   -270       N  
ATOM    670  N   ASP B  88      29.423  12.953   6.021  1.00 47.13           N  
ANISOU  670  N   ASP B  88     6951   6285   4672   -225    148   -332       N  
ATOM    671  CA  ASP B  88      29.270  11.811   5.127  1.00 45.69           C  
ANISOU  671  CA  ASP B  88     6859   6137   4365   -305     81   -372       C  
ATOM    672  C   ASP B  88      30.514  10.929   5.125  1.00 45.15           C  
ANISOU  672  C   ASP B  88     6952   5987   4216   -304    130   -432       C  
ATOM    673  O   ASP B  88      30.400   9.700   5.027  1.00 46.28           O  
ANISOU  673  O   ASP B  88     7178   6103   4301   -386    106   -504       O  
ATOM    674  CB  ASP B  88      28.932  12.296   3.718  1.00 50.51           C  
ANISOU  674  CB  ASP B  88     7438   6847   4907   -286    -12   -307       C  
ATOM    675  CG  ASP B  88      27.480  12.724   3.584  1.00 57.17           C  
ANISOU  675  CG  ASP B  88     8124   7782   5817   -315    -93   -261       C  
ATOM    676  OD1 ASP B  88      26.657  12.305   4.426  1.00 59.20           O  
ANISOU  676  OD1 ASP B  88     8315   8038   6141   -381    -82   -308       O  
ATOM    677  OD2 ASP B  88      27.160  13.482   2.644  1.00 60.62           O  
ANISOU  677  OD2 ASP B  88     8496   8297   6239   -275   -168   -171       O  
ATOM    678  N   GLN B  89      31.704  11.525   5.251  1.00 40.45           N  
ANISOU  678  N   GLN B  89     6396   5343   3630   -213    196   -406       N  
ATOM    679  CA  GLN B  89      32.913  10.723   5.413  1.00 38.82           C  
ANISOU  679  CA  GLN B  89     6322   5056   3372   -199    250   -463       C  
ATOM    680  C   GLN B  89      32.860   9.908   6.700  1.00 39.00           C  
ANISOU  680  C   GLN B  89     6371   4999   3447   -253    288   -510       C  
ATOM    681  O   GLN B  89      33.278   8.743   6.727  1.00 36.25           O  
ANISOU  681  O   GLN B  89     6129   4584   3059   -290    289   -568       O  
ATOM    682  CB  GLN B  89      34.151  11.620   5.404  1.00 36.19           C  
ANISOU  682  CB  GLN B  89     5998   4698   3054    -97    315   -417       C  
ATOM    683  CG  GLN B  89      34.362  12.400   4.116  1.00 37.54           C  
ANISOU  683  CG  GLN B  89     6154   4946   3162    -50    284   -350       C  
ATOM    684  CD  GLN B  89      35.713  13.091   4.075  1.00 37.57           C  
ANISOU  684  CD  GLN B  89     6181   4920   3173     33    355   -310       C  
ATOM    685  OE1 GLN B  89      36.741  12.489   4.388  1.00 35.71           O  
ANISOU  685  OE1 GLN B  89     6024   4628   2915     53    412   -365       O  
ATOM    686  NE2 GLN B  89      35.716  14.363   3.695  1.00 38.16           N  
ANISOU  686  NE2 GLN B  89     6181   5028   3291     80    349   -208       N  
ATOM    687  N   PHE B  90      32.360  10.514   7.779  1.00 38.01           N  
ANISOU  687  N   PHE B  90     6149   4881   3413   -258    322   -484       N  
ATOM    688  CA  PHE B  90      32.170   9.797   9.036  1.00 37.03           C  
ANISOU  688  CA  PHE B  90     6035   4712   3321   -326    356   -511       C  
ATOM    689  C   PHE B  90      31.248   8.599   8.843  1.00 38.95           C  
ANISOU  689  C   PHE B  90     6307   4957   3534   -445    297   -546       C  
ATOM    690  O   PHE B  90      31.537   7.490   9.312  1.00 37.67           O  
ANISOU  690  O   PHE B  90     6236   4717   3360   -502    304   -572       O  
ATOM    691  CB  PHE B  90      31.614  10.763  10.087  1.00 37.74           C  
ANISOU  691  CB  PHE B  90     5995   4846   3498   -317    403   -492       C  
ATOM    692  CG  PHE B  90      30.936  10.094  11.252  1.00 38.70           C  
ANISOU  692  CG  PHE B  90     6089   4978   3636   -417    426   -511       C  
ATOM    693  CD1 PHE B  90      31.670   9.682  12.351  1.00 37.58           C  
ANISOU  693  CD1 PHE B  90     6005   4788   3485   -431    482   -513       C  
ATOM    694  CD2 PHE B  90      29.561   9.907  11.261  1.00 40.28           C  
ANISOU  694  CD2 PHE B  90     6197   5249   3858   -503    392   -516       C  
ATOM    695  CE1 PHE B  90      31.048   9.076  13.431  1.00 38.15           C  
ANISOU  695  CE1 PHE B  90     6052   4885   3557   -535    504   -512       C  
ATOM    696  CE2 PHE B  90      28.935   9.301  12.336  1.00 40.00           C  
ANISOU  696  CE2 PHE B  90     6130   5238   3831   -607    422   -524       C  
ATOM    697  CZ  PHE B  90      29.679   8.885  13.422  1.00 39.87           C  
ANISOU  697  CZ  PHE B  90     6180   5176   3794   -626    480   -518       C  
ATOM    698  N   TYR B  91      30.132   8.809   8.142  1.00 45.02           N  
ANISOU  698  N   TYR B  91     6995   5810   4299   -486    232   -541       N  
ATOM    699  CA  TYR B  91      29.193   7.715   7.903  1.00 47.35           C  
ANISOU  699  CA  TYR B  91     7306   6115   4570   -614    168   -579       C  
ATOM    700  C   TYR B  91      29.828   6.605   7.074  1.00 48.10           C  
ANISOU  700  C   TYR B  91     7553   6136   4588   -637    132   -641       C  
ATOM    701  O   TYR B  91      29.623   5.417   7.354  1.00 49.70           O  
ANISOU  701  O   TYR B  91     7825   6265   4795   -734    114   -682       O  
ATOM    702  CB  TYR B  91      27.933   8.244   7.222  1.00 47.85           C  
ANISOU  702  CB  TYR B  91     7240   6299   4642   -645     95   -559       C  
ATOM    703  CG  TYR B  91      26.974   8.906   8.181  1.00 52.39           C  
ANISOU  703  CG  TYR B  91     7654   6939   5312   -663    127   -528       C  
ATOM    704  CD1 TYR B  91      26.714   8.347   9.425  1.00 51.67           C  
ANISOU  704  CD1 TYR B  91     7553   6823   5257   -744    183   -542       C  
ATOM    705  CD2 TYR B  91      26.334  10.091   7.846  1.00 54.54           C  
ANISOU  705  CD2 TYR B  91     7781   7300   5640   -598    103   -484       C  
ATOM    706  CE1 TYR B  91      25.840   8.947  10.306  1.00 55.90           C  
ANISOU  706  CE1 TYR B  91     7935   7438   5868   -763    226   -530       C  
ATOM    707  CE2 TYR B  91      25.458  10.698   8.722  1.00 56.11           C  
ANISOU  707  CE2 TYR B  91     7824   7557   5939   -603    141   -476       C  
ATOM    708  CZ  TYR B  91      25.216  10.122   9.949  1.00 59.12           C  
ANISOU  708  CZ  TYR B  91     8195   7929   6340   -687    208   -508       C  
ATOM    709  OH  TYR B  91      24.344  10.726  10.821  1.00 63.75           O  
ANISOU  709  OH  TYR B  91     8617   8592   7013   -694    259   -515       O  
ATOM    710  N   GLU B  92      30.610   6.969   6.055  1.00 46.85           N  
ANISOU  710  N   GLU B  92     7446   5992   4363   -550    125   -650       N  
ATOM    711  CA  GLU B  92      31.266   5.957   5.228  1.00 45.50           C  
ANISOU  711  CA  GLU B  92     7414   5760   4115   -560    103   -732       C  
ATOM    712  C   GLU B  92      32.285   5.153   6.031  1.00 45.48           C  
ANISOU  712  C   GLU B  92     7517   5612   4152   -538    164   -760       C  
ATOM    713  O   GLU B  92      32.343   3.918   5.921  1.00 46.49           O  
ANISOU  713  O   GLU B  92     7743   5642   4278   -599    139   -831       O  
ATOM    714  CB  GLU B  92      31.931   6.622   4.022  1.00 45.80           C  
ANISOU  714  CB  GLU B  92     7470   5872   4060   -470     99   -729       C  
ATOM    715  CG  GLU B  92      32.446   5.648   2.978  1.00 48.44           C  
ANISOU  715  CG  GLU B  92     7929   6183   4293   -485     76   -838       C  
ATOM    716  CD  GLU B  92      31.350   4.767   2.415  1.00 52.01           C  
ANISOU  716  CD  GLU B  92     8393   6663   4706   -615    -16   -914       C  
ATOM    717  OE1 GLU B  92      30.194   5.231   2.322  1.00 54.36           O  
ANISOU  717  OE1 GLU B  92     8581   7062   5010   -674    -79   -862       O  
ATOM    718  OE2 GLU B  92      31.646   3.607   2.064  1.00 53.06           O  
ANISOU  718  OE2 GLU B  92     8640   6711   4810   -657    -27  -1030       O  
ATOM    719  N   LEU B  93      33.099   5.838   6.841  1.00 50.06           N  
ANISOU  719  N   LEU B  93     8076   6170   4775   -451    236   -703       N  
ATOM    720  CA  LEU B  93      34.050   5.141   7.699  1.00 49.31           C  
ANISOU  720  CA  LEU B  93     8064   5951   4722   -427    284   -709       C  
ATOM    721  C   LEU B  93      33.336   4.191   8.649  1.00 51.09           C  
ANISOU  721  C   LEU B  93     8302   6108   5001   -545    264   -698       C  
ATOM    722  O   LEU B  93      33.773   3.049   8.840  1.00 51.81           O  
ANISOU  722  O   LEU B  93     8496   6073   5117   -570    256   -728       O  
ATOM    723  CB  LEU B  93      34.889   6.147   8.486  1.00 48.11           C  
ANISOU  723  CB  LEU B  93     7863   5814   4604   -332    354   -645       C  
ATOM    724  CG  LEU B  93      36.324   6.368   8.009  1.00 48.54           C  
ANISOU  724  CG  LEU B  93     7972   5840   4631   -216    397   -660       C  
ATOM    725  CD1 LEU B  93      37.063   7.294   8.957  1.00 48.08           C  
ANISOU  725  CD1 LEU B  93     7858   5790   4618   -148    459   -600       C  
ATOM    726  CD2 LEU B  93      37.047   5.046   7.884  1.00 47.79           C  
ANISOU  726  CD2 LEU B  93     7997   5623   4537   -209    393   -722       C  
ATOM    727  N   ASN B  94      32.236   4.644   9.255  1.00 41.03           N  
ANISOU  727  N   ASN B  94     6919   4917   3755   -618    259   -653       N  
ATOM    728  CA  ASN B  94      31.487   3.782  10.164  1.00 40.59           C  
ANISOU  728  CA  ASN B  94     6861   4819   3740   -747    247   -630       C  
ATOM    729  C   ASN B  94      30.927   2.567   9.436  1.00 43.45           C  
ANISOU  729  C   ASN B  94     7298   5114   4097   -852    174   -693       C  
ATOM    730  O   ASN B  94      30.928   1.455   9.977  1.00 44.85           O  
ANISOU  730  O   ASN B  94     7550   5174   4316   -934    161   -686       O  
ATOM    731  CB  ASN B  94      30.363   4.572  10.831  1.00 42.02           C  
ANISOU  731  CB  ASN B  94     6892   5128   3945   -802    264   -586       C  
ATOM    732  CG  ASN B  94      29.440   3.692  11.646  1.00 44.87           C  
ANISOU  732  CG  ASN B  94     7236   5479   4336   -957    253   -560       C  
ATOM    733  OD1 ASN B  94      29.856   3.082  12.630  1.00 45.43           O  
ANISOU  733  OD1 ASN B  94     7361   5477   4422   -995    283   -515       O  
ATOM    734  ND2 ASN B  94      28.179   3.616  11.236  1.00 46.56           N  
ANISOU  734  ND2 ASN B  94     7366   5770   4556  -1054    205   -578       N  
ATOM    735  N   ARG B  95      30.445   2.759   8.205  1.00 53.50           N  
ANISOU  735  N   ARG B  95     8552   6458   5319   -857    119   -752       N  
ATOM    736  CA  ARG B  95      29.917   1.636   7.438  1.00 54.37           C  
ANISOU  736  CA  ARG B  95     8731   6511   5415   -963     44   -835       C  
ATOM    737  C   ARG B  95      31.003   0.610   7.139  1.00 54.50           C  
ANISOU  737  C   ARG B  95     8907   6361   5441   -923     49   -908       C  
ATOM    738  O   ARG B  95      30.758  -0.600   7.200  1.00 57.48           O  
ANISOU  738  O   ARG B  95     9364   6611   5866  -1022     10   -953       O  
ATOM    739  CB  ARG B  95      29.281   2.136   6.141  1.00 55.60           C  
ANISOU  739  CB  ARG B  95     8831   6802   5492   -968    -20   -883       C  
ATOM    740  CG  ARG B  95      28.632   1.042   5.307  1.00 57.60           C  
ANISOU  740  CG  ARG B  95     9144   7022   5719  -1094   -107   -986       C  
ATOM    741  CD  ARG B  95      28.137   1.579   3.971  1.00 60.22           C  
ANISOU  741  CD  ARG B  95     9425   7511   5946  -1091   -176  -1029       C  
ATOM    742  NE  ARG B  95      29.237   1.940   3.081  1.00 60.41           N  
ANISOU  742  NE  ARG B  95     9521   7553   5878   -964   -150  -1072       N  
ATOM    743  CZ  ARG B  95      29.915   1.069   2.339  1.00 60.11           C  
ANISOU  743  CZ  ARG B  95     9615   7434   5788   -958   -156  -1197       C  
ATOM    744  NH1 ARG B  95      29.608  -0.222   2.378  1.00 60.12           N  
ANISOU  744  NH1 ARG B  95     9699   7309   5836  -1069   -195  -1294       N  
ATOM    745  NH2 ARG B  95      30.901   1.487   1.557  1.00 58.23           N  
ANISOU  745  NH2 ARG B  95     9424   7242   5460   -842   -119  -1230       N  
ATOM    746  N   ARG B  96      32.214   1.073   6.821  1.00 48.25           N  
ANISOU  746  N   ARG B  96     8156   5561   4614   -777     98   -921       N  
ATOM    747  CA  ARG B  96      33.289   0.141   6.491  1.00 48.30           C  
ANISOU  747  CA  ARG B  96     8298   5417   4638   -720    110  -1002       C  
ATOM    748  C   ARG B  96      33.968  -0.465   7.715  1.00 48.49           C  
ANISOU  748  C   ARG B  96     8374   5290   4761   -702    145   -936       C  
ATOM    749  O   ARG B  96      34.628  -1.502   7.581  1.00 48.72           O  
ANISOU  749  O   ARG B  96     8513   5157   4843   -680    138   -997       O  
ATOM    750  CB  ARG B  96      34.352   0.831   5.634  1.00 45.85           C  
ANISOU  750  CB  ARG B  96     8000   5170   4250   -574    154  -1043       C  
ATOM    751  CG  ARG B  96      33.831   1.443   4.350  1.00 45.92           C  
ANISOU  751  CG  ARG B  96     7967   5339   4143   -583    117  -1091       C  
ATOM    752  CD  ARG B  96      34.941   2.172   3.618  1.00 45.19           C  
ANISOU  752  CD  ARG B  96     7882   5317   3971   -448    172  -1104       C  
ATOM    753  NE  ARG B  96      34.450   2.864   2.431  1.00 46.66           N  
ANISOU  753  NE  ARG B  96     8020   5674   4034   -459    133  -1116       N  
ATOM    754  CZ  ARG B  96      35.219   3.557   1.597  1.00 44.68           C  
ANISOU  754  CZ  ARG B  96     7767   5522   3688   -369    170  -1116       C  
ATOM    755  NH1 ARG B  96      36.524   3.650   1.813  1.00 42.09           N  
ANISOU  755  NH1 ARG B  96     7474   5137   3380   -258    252  -1117       N  
ATOM    756  NH2 ARG B  96      34.681   4.156   0.545  1.00 44.83           N  
ANISOU  756  NH2 ARG B  96     7740   5703   3589   -394    121  -1105       N  
ATOM    757  N   TRP B  97      33.797   0.139   8.895  1.00 44.17           N  
ANISOU  757  N   TRP B  97     7748   4795   4241   -713    179   -816       N  
ATOM    758  CA  TRP B  97      34.676  -0.123  10.035  1.00 46.36           C  
ANISOU  758  CA  TRP B  97     8059   4976   4579   -666    218   -735       C  
ATOM    759  C   TRP B  97      34.764  -1.606  10.398  1.00 47.33           C  
ANISOU  759  C   TRP B  97     8292   4902   4791   -735    178   -735       C  
ATOM    760  O   TRP B  97      35.858  -2.133  10.626  1.00 47.26           O  
ANISOU  760  O   TRP B  97     8358   4763   4836   -648    191   -728       O  
ATOM    761  CB  TRP B  97      34.201   0.695  11.239  1.00 44.29           C  
ANISOU  761  CB  TRP B  97     7690   4826   4313   -706    253   -622       C  
ATOM    762  CG  TRP B  97      35.224   0.871  12.323  1.00 46.04           C  
ANISOU  762  CG  TRP B  97     7919   5018   4556   -634    299   -541       C  
ATOM    763  CD1 TRP B  97      35.375   0.098  13.439  1.00 48.54           C  
ANISOU  763  CD1 TRP B  97     8275   5248   4919   -691    291   -452       C  
ATOM    764  CD2 TRP B  97      36.226   1.893  12.405  1.00 44.49           C  
ANISOU  764  CD2 TRP B  97     7684   4887   4334   -501    351   -531       C  
ATOM    765  NE1 TRP B  97      36.412   0.571  14.206  1.00 47.61           N  
ANISOU  765  NE1 TRP B  97     8144   5149   4796   -600    330   -392       N  
ATOM    766  CE2 TRP B  97      36.951   1.673  13.594  1.00 44.28           C  
ANISOU  766  CE2 TRP B  97     7672   4816   4334   -484    369   -446       C  
ATOM    767  CE3 TRP B  97      36.582   2.971  11.588  1.00 43.36           C  
ANISOU  767  CE3 TRP B  97     7493   4836   4147   -403    380   -576       C  
ATOM    768  CZ2 TRP B  97      38.011   2.490  13.986  1.00 42.35           C  
ANISOU  768  CZ2 TRP B  97     7394   4621   4077   -375    414   -422       C  
ATOM    769  CZ3 TRP B  97      37.636   3.782  11.979  1.00 41.53           C  
ANISOU  769  CZ3 TRP B  97     7230   4639   3912   -297    431   -546       C  
ATOM    770  CH2 TRP B  97      38.338   3.536  13.168  1.00 41.42           C  
ANISOU  770  CH2 TRP B  97     7228   4582   3927   -285    446   -477       C  
ATOM    771  N   ASP B  98      33.626  -2.296  10.462  1.00 48.62           N  
ANISOU  771  N   ASP B  98     8458   5033   4982   -892    127   -735       N  
ATOM    772  CA  ASP B  98      33.577  -3.643  11.020  1.00 53.95           C  
ANISOU  772  CA  ASP B  98     9225   5513   5759   -983     88   -698       C  
ATOM    773  C   ASP B  98      33.580  -4.746   9.965  1.00 54.29           C  
ANISOU  773  C   ASP B  98     9378   5394   5854  -1008     33   -839       C  
ATOM    774  O   ASP B  98      33.322  -5.906  10.305  1.00 52.75           O  
ANISOU  774  O   ASP B  98     9258   5022   5762  -1109    -12   -820       O  
ATOM    775  CB  ASP B  98      32.347  -3.797  11.917  1.00 57.13           C  
ANISOU  775  CB  ASP B  98     9562   5970   6176  -1161     71   -595       C  
ATOM    776  CG  ASP B  98      32.504  -3.090  13.249  1.00 58.51           C  
ANISOU  776  CG  ASP B  98     9658   6252   6321  -1149    127   -453       C  
ATOM    777  OD1 ASP B  98      33.655  -2.938  13.711  1.00 58.23           O  
ANISOU  777  OD1 ASP B  98     9657   6175   6294  -1029    157   -408       O  
ATOM    778  OD2 ASP B  98      31.477  -2.691  13.837  1.00 59.48           O  
ANISOU  778  OD2 ASP B  98     9680   6509   6412  -1261    142   -395       O  
ATOM    779  N   LYS B  99      33.872  -4.424   8.706  1.00 58.13           N  
ANISOU  779  N   LYS B  99     9878   5936   6272   -925     37   -981       N  
ATOM    780  CA  LYS B  99      33.844  -5.438   7.658  1.00 59.30           C  
ANISOU  780  CA  LYS B  99    10128   5952   6453   -955    -10  -1144       C  
ATOM    781  C   LYS B  99      34.914  -6.497   7.904  1.00 60.04           C  
ANISOU  781  C   LYS B  99    10340   5798   6674   -875     -6  -1169       C  
ATOM    782  O   LYS B  99      36.081  -6.178   8.146  1.00 59.82           O  
ANISOU  782  O   LYS B  99    10316   5756   6655   -720     46  -1138       O  
ATOM    783  CB  LYS B  99      34.031  -4.789   6.287  1.00 58.98           C  
ANISOU  783  CB  LYS B  99    10072   6055   6283   -876      2  -1284       C  
ATOM    784  CG  LYS B  99      32.907  -3.835   5.911  1.00 60.42           C  
ANISOU  784  CG  LYS B  99    10138   6464   6354   -955    -23  -1261       C  
ATOM    785  CD  LYS B  99      32.929  -3.489   4.431  1.00 60.87           C  
ANISOU  785  CD  LYS B  99    10199   6646   6283   -917    -38  -1401       C  
ATOM    786  CE  LYS B  99      32.572  -4.692   3.573  1.00 62.20           C  
ANISOU  786  CE  LYS B  99    10466   6703   6466  -1012   -102  -1575       C  
ATOM    787  NZ  LYS B  99      32.116  -4.283   2.215  1.00 62.68           N  
ANISOU  787  NZ  LYS B  99    10500   6946   6371  -1037   -142  -1690       N  
ATOM    788  N   PHE B 100      34.502  -7.767   7.839  1.00 63.13           N  
ANISOU  788  N   PHE B 100    10820   5986   7179   -984    -66  -1223       N  
ATOM    789  CA  PHE B 100      35.341  -8.903   8.198  1.00 64.32           C  
ANISOU  789  CA  PHE B 100    11082   5864   7494   -929    -78  -1225       C  
ATOM    790  C   PHE B 100      34.752 -10.137   7.539  1.00 66.18           C  
ANISOU  790  C   PHE B 100    11415   5906   7826  -1049   -146  -1371       C  
ATOM    791  O   PHE B 100      33.521 -10.245   7.461  1.00 66.84           O  
ANISOU  791  O   PHE B 100    11467   6045   7883  -1230   -196  -1370       O  
ATOM    792  CB  PHE B 100      35.400  -9.077   9.724  1.00 65.85           C  
ANISOU  792  CB  PHE B 100    11260   5987   7773   -969    -84   -994       C  
ATOM    793  CG  PHE B 100      36.142 -10.308  10.181  1.00 68.64           C  
ANISOU  793  CG  PHE B 100    11722   6043   8314   -929   -116   -958       C  
ATOM    794  CD1 PHE B 100      37.509 -10.264  10.414  1.00 68.95           C  
ANISOU  794  CD1 PHE B 100    11780   6015   8403   -738    -81   -933       C  
ATOM    795  CD2 PHE B 100      35.471 -11.503  10.394  1.00 70.96           C  
ANISOU  795  CD2 PHE B 100    12094   6120   8749  -1084   -187   -939       C  
ATOM    796  CE1 PHE B 100      38.192 -11.391  10.838  1.00 71.02           C  
ANISOU  796  CE1 PHE B 100    12132   5996   8856   -688   -119   -888       C  
ATOM    797  CE2 PHE B 100      36.148 -12.633  10.818  1.00 72.24           C  
ANISOU  797  CE2 PHE B 100    12355   5986   9105  -1042   -224   -891       C  
ATOM    798  CZ  PHE B 100      37.510 -12.577  11.041  1.00 72.66           C  
ANISOU  798  CZ  PHE B 100    12423   5974   9211   -837   -192   -864       C  
ATOM    799  N   PRO B 101      35.576 -11.077   7.048  1.00 76.01           N  
ANISOU  799  N   PRO B 101    12768   6923   9188   -958   -150  -1509       N  
ATOM    800  CA  PRO B 101      37.039 -11.004   7.025  1.00 75.96           C  
ANISOU  800  CA  PRO B 101    12786   6855   9221   -739    -91  -1533       C  
ATOM    801  C   PRO B 101      37.600 -10.478   5.707  1.00 74.24           C  
ANISOU  801  C   PRO B 101    12559   6778   8870   -614    -34  -1742       C  
ATOM    802  O   PRO B 101      37.087 -10.802   4.636  1.00 75.12           O  
ANISOU  802  O   PRO B 101    12710   6904   8929   -682    -58  -1937       O  
ATOM    803  CB  PRO B 101      37.449 -12.459   7.241  1.00 78.22           C  
ANISOU  803  CB  PRO B 101    13191   6790   9739   -730   -136  -1570       C  
ATOM    804  CG  PRO B 101      36.369 -13.234   6.552  1.00 78.81           C  
ANISOU  804  CG  PRO B 101    13327   6773   9846   -909   -201  -1719       C  
ATOM    805  CD  PRO B 101      35.096 -12.417   6.664  1.00 78.07           C  
ANISOU  805  CD  PRO B 101    13136   6934   9593  -1077   -220  -1634       C  
ATOM    806  N   VAL B 102      38.642  -9.658   5.796  1.00 63.95           N  
ANISOU  806  N   VAL B 102    11200   5593   7504   -443     39  -1698       N  
ATOM    807  CA  VAL B 102      39.390  -9.221   4.620  1.00 62.53           C  
ANISOU  807  CA  VAL B 102    11013   5535   7211   -310    106  -1878       C  
ATOM    808  C   VAL B 102      40.860  -9.547   4.856  1.00 61.30           C  
ANISOU  808  C   VAL B 102    10877   5244   7171   -114    160  -1889       C  
ATOM    809  O   VAL B 102      41.664  -8.636   5.101  1.00 59.98           O  
ANISOU  809  O   VAL B 102    10633   5221   6938      7    222  -1803       O  
ATOM    810  CB  VAL B 102      39.188  -7.724   4.336  1.00 61.24           C  
ANISOU  810  CB  VAL B 102    10740   5690   6840   -301    147  -1814       C  
ATOM    811  CG1 VAL B 102      39.667  -7.385   2.931  1.00 61.21           C  
ANISOU  811  CG1 VAL B 102    10738   5828   6693   -217    201  -2009       C  
ATOM    812  CG2 VAL B 102      37.728  -7.333   4.513  1.00 60.58           C  
ANISOU  812  CG2 VAL B 102    10607   5729   6682   -485     87  -1733       C  
ATOM    813  N   PRO B 103      41.255 -10.816   4.799  1.00 60.75           N  
ANISOU  813  N   PRO B 103    10901   4894   7285    -74    136  -1993       N  
ATOM    814  CA  PRO B 103      42.641 -11.178   5.103  1.00 61.07           C  
ANISOU  814  CA  PRO B 103    10946   4792   7464    122    179  -1990       C  
ATOM    815  C   PRO B 103      43.583 -10.668   4.029  1.00 59.86           C  
ANISOU  815  C   PRO B 103    10756   4792   7196    278    278  -2169       C  
ATOM    816  O   PRO B 103      43.269 -10.737   2.831  1.00 58.67           O  
ANISOU  816  O   PRO B 103    10637   4722   6935    244    300  -2386       O  
ATOM    817  CB  PRO B 103      42.605 -12.712   5.134  1.00 62.89           C  
ANISOU  817  CB  PRO B 103    11293   4673   7931    104    120  -2085       C  
ATOM    818  CG  PRO B 103      41.489 -13.067   4.214  1.00 62.57           C  
ANISOU  818  CG  PRO B 103    11312   4644   7819    -59     83  -2267       C  
ATOM    819  CD  PRO B 103      40.456 -11.983   4.384  1.00 61.39           C  
ANISOU  819  CD  PRO B 103    11084   4772   7469   -205     67  -2134       C  
ATOM    820  N   PRO B 104      44.743 -10.143   4.415  1.00 64.55           N  
ANISOU  820  N   PRO B 104    11277   5445   7803    441    339  -2085       N  
ATOM    821  CA  PRO B 104      45.683  -9.619   3.420  1.00 64.33           C  
ANISOU  821  CA  PRO B 104    11199   5580   7662    583    443  -2241       C  
ATOM    822  C   PRO B 104      46.236 -10.724   2.535  1.00 66.13           C  
ANISOU  822  C   PRO B 104    11501   5629   7998    680    476  -2509       C  
ATOM    823  O   PRO B 104      46.248 -11.905   2.891  1.00 67.16           O  
ANISOU  823  O   PRO B 104    11708   5462   8346    691    422  -2545       O  
ATOM    824  CB  PRO B 104      46.787  -8.985   4.273  1.00 63.18           C  
ANISOU  824  CB  PRO B 104    10959   5490   7558    722    483  -2065       C  
ATOM    825  CG  PRO B 104      46.715  -9.714   5.575  1.00 63.97           C  
ANISOU  825  CG  PRO B 104    11093   5355   7859    701    396  -1885       C  
ATOM    826  CD  PRO B 104      45.258 -10.012   5.788  1.00 64.29           C  
ANISOU  826  CD  PRO B 104    11199   5346   7881    493    313  -1840       C  
ATOM    827  N   ASN B 105      46.697 -10.318   1.355  1.00 80.39           N  
ANISOU  827  N   ASN B 105    13277   7619   9647    749    569  -2700       N  
ATOM    828  CA  ASN B 105      47.276 -11.230   0.378  1.00 82.46           C  
ANISOU  828  CA  ASN B 105    13593   7764   9973    849    626  -2993       C  
ATOM    829  C   ASN B 105      48.794 -11.125   0.442  1.00 81.47           C  
ANISOU  829  C   ASN B 105    13387   7643   9926   1072    723  -3011       C  
ATOM    830  O   ASN B 105      49.359 -10.061   0.168  1.00 78.08           O  
ANISOU  830  O   ASN B 105    12859   7477   9331   1128    804  -2963       O  
ATOM    831  CB  ASN B 105      46.770 -10.914  -1.029  1.00 83.96           C  
ANISOU  831  CB  ASN B 105    13764   8205   9932    762    662  -3192       C  
ATOM    832  CG  ASN B 105      45.638 -11.826  -1.457  1.00 86.73           C  
ANISOU  832  CG  ASN B 105    14194   8435  10323    601    572  -3332       C  
ATOM    833  OD1 ASN B 105      45.735 -13.048  -1.348  1.00 90.37           O  
ANISOU  833  OD1 ASN B 105    14699   8625  11015    623    535  -3443       O  
ATOM    834  ND2 ASN B 105      44.553 -11.234  -1.943  1.00 85.09           N  
ANISOU  834  ND2 ASN B 105    13999   8428   9902    436    531  -3325       N  
ATOM    835  N   VAL B 106      49.447 -12.225   0.804  1.00 72.62           N  
ANISOU  835  N   VAL B 106    12277   6244   9073   1189    707  -3063       N  
ATOM    836  CA  VAL B 106      50.900 -12.250   0.932  1.00 72.65           C  
ANISOU  836  CA  VAL B 106    12174   6235   9192   1403    786  -3072       C  
ATOM    837  C   VAL B 106      51.508 -12.501  -0.442  1.00 73.77           C  
ANISOU  837  C   VAL B 106    12217   6524   9290   1468    892  -3357       C  
ATOM    838  O   VAL B 106      51.280 -13.551  -1.052  1.00 75.54           O  
ANISOU  838  O   VAL B 106    12464   6606   9632   1444    879  -3571       O  
ATOM    839  CB  VAL B 106      51.351 -13.319   1.937  1.00 73.18           C  
ANISOU  839  CB  VAL B 106    12280   5942   9584   1506    714  -2985       C  
ATOM    840  CG1 VAL B 106      52.869 -13.359   2.023  1.00 73.26           C  
ANISOU  840  CG1 VAL B 106    12161   5951   9722   1734    792  -3001       C  
ATOM    841  CG2 VAL B 106      50.744 -13.054   3.305  1.00 71.11           C  
ANISOU  841  CG2 VAL B 106    12053   5607   9358   1402    601  -2667       C  
ATOM    842  N   VAL B 107      52.282 -11.539  -0.931  1.00 69.08           N  
ANISOU  842  N   VAL B 107    11507   6215   8526   1542   1001  -3363       N  
ATOM    843  CA  VAL B 107      52.968 -11.669  -2.209  1.00 70.23           C  
ANISOU  843  CA  VAL B 107    11544   6534   8606   1602   1119  -3618       C  
ATOM    844  C   VAL B 107      54.402 -12.105  -1.954  1.00 71.69           C  
ANISOU  844  C   VAL B 107    11623   6610   9007   1810   1197  -3657       C  
ATOM    845  O   VAL B 107      54.967 -11.870  -0.878  1.00 70.52           O  
ANISOU  845  O   VAL B 107    11456   6365   8974   1915   1169  -3449       O  
ATOM    846  CB  VAL B 107      52.921 -10.352  -3.013  1.00 68.69           C  
ANISOU  846  CB  VAL B 107    11279   6737   8085   1534   1195  -3599       C  
ATOM    847  CG1 VAL B 107      51.490  -9.854  -3.135  1.00 67.14           C  
ANISOU  847  CG1 VAL B 107    11178   6638   7692   1335   1107  -3521       C  
ATOM    848  CG2 VAL B 107      53.803  -9.298  -2.360  1.00 66.87           C  
ANISOU  848  CG2 VAL B 107    10963   6632   7814   1634   1250  -3387       C  
ATOM    849  N   LYS B 108      54.995 -12.757  -2.949  1.00 88.90           N  
ANISOU  849  N   LYS B 108    13730   8804  11243   1866   1306  -3926       N  
ATOM    850  CA  LYS B 108      56.388 -13.160  -2.852  1.00 91.57           C  
ANISOU  850  CA  LYS B 108    13963   9051  11776   2054   1421  -3975       C  
ATOM    851  C   LYS B 108      57.295 -11.945  -3.054  1.00 90.97           C  
ANISOU  851  C   LYS B 108    13751   9296  11517   2121   1527  -3892       C  
ATOM    852  O   LYS B 108      56.866 -10.889  -3.529  1.00 87.59           O  
ANISOU  852  O   LYS B 108    13311   9165  10806   2010   1539  -3845       O  
ATOM    853  CB  LYS B 108      56.697 -14.266  -3.868  1.00 95.27           C  
ANISOU  853  CB  LYS B 108    14501   9396  12302   2066   1568  -4205       C  
ATOM    854  CG  LYS B 108      58.012 -15.017  -3.643  1.00 99.36           C  
ANISOU  854  CG  LYS B 108    15025   9705  13024   2306   1662  -4201       C  
ATOM    855  CD  LYS B 108      58.301 -15.264  -2.165  1.00 98.79           C  
ANISOU  855  CD  LYS B 108    14877   9381  13279   2409   1536  -4019       C  
ATOM    856  CE  LYS B 108      59.733 -15.746  -1.967  1.00101.26           C  
ANISOU  856  CE  LYS B 108    15126   9574  13773   2659   1627  -4002       C  
ATOM    857  NZ  LYS B 108      60.674 -15.097  -2.931  1.00101.74           N  
ANISOU  857  NZ  LYS B 108    15097   9944  13617   2740   1801  -4099       N  
ATOM    858  N   ARG B 109      58.566 -12.113  -2.679  1.00 88.49           N  
ANISOU  858  N   ARG B 109    13333   8912  11377   2303   1603  -3860       N  
ATOM    859  CA  ARG B 109      59.482 -10.983  -2.545  1.00 85.82           C  
ANISOU  859  CA  ARG B 109    12856   8831  10919   2380   1673  -3733       C  
ATOM    860  C   ARG B 109      59.609 -10.192  -3.843  1.00 84.29           C  
ANISOU  860  C   ARG B 109    12606   8988  10431   2285   1826  -3850       C  
ATOM    861  O   ARG B 109      59.518  -8.959  -3.841  1.00 81.28           O  
ANISOU  861  O   ARG B 109    12177   8874   9834   2222   1820  -3708       O  
ATOM    862  CB  ARG B 109      60.850 -11.485  -2.087  1.00 87.63           C  
ANISOU  862  CB  ARG B 109    12973   8919  11404   2595   1737  -3721       C  
ATOM    863  CG  ARG B 109      61.768 -10.391  -1.597  1.00 85.09           C  
ANISOU  863  CG  ARG B 109    12504   8809  11016   2684   1763  -3546       C  
ATOM    864  CD  ARG B 109      63.124 -10.943  -1.212  1.00 85.61           C  
ANISOU  864  CD  ARG B 109    12440   8747  11341   2900   1821  -3548       C  
ATOM    865  NE  ARG B 109      63.997  -9.891  -0.706  1.00 85.53           N  
ANISOU  865  NE  ARG B 109    12280   8946  11274   2978   1839  -3380       N  
ATOM    866  CZ  ARG B 109      64.634  -9.017  -1.477  1.00 85.58           C  
ANISOU  866  CZ  ARG B 109    12164   9263  11089   2957   1987  -3424       C  
ATOM    867  NH1 ARG B 109      64.502  -9.069  -2.796  1.00 87.62           N  
ANISOU  867  NH1 ARG B 109    12451   9663  11177   2867   2132  -3614       N  
ATOM    868  NH2 ARG B 109      65.405  -8.091  -0.929  1.00 83.11           N  
ANISOU  868  NH2 ARG B 109    11717   9116  10743   3022   1994  -3259       N  
ATOM    869  N   GLU B 110      59.822 -10.882  -4.965  1.00 87.40           N  
ANISOU  869  N   GLU B 110    13068   9367  10775   2279   1972  -4045       N  
ATOM    870  CA  GLU B 110      60.070 -10.195  -6.229  1.00 89.74           C  
ANISOU  870  CA  GLU B 110    13376   9975  10748   2226   2117  -4093       C  
ATOM    871  C   GLU B 110      58.865  -9.412  -6.735  1.00 89.92           C  
ANISOU  871  C   GLU B 110    13446  10216  10502   1997   2057  -4063       C  
ATOM    872  O   GLU B 110      59.024  -8.592  -7.646  1.00 90.93           O  
ANISOU  872  O   GLU B 110    13579  10624  10345   1947   2150  -4035       O  
ATOM    873  CB  GLU B 110      60.511 -11.196  -7.298  1.00 93.81           C  
ANISOU  873  CB  GLU B 110    14020  10424  11202   2357   2210  -4291       C  
ATOM    874  CG  GLU B 110      59.467 -12.246  -7.634  1.00 97.05           C  
ANISOU  874  CG  GLU B 110    14631  10629  11615   2299   2109  -4429       C  
ATOM    875  CD  GLU B 110      59.629 -13.506  -6.810  1.00100.53           C  
ANISOU  875  CD  GLU B 110    15115  10675  12408   2420   2043  -4468       C  
ATOM    876  OE1 GLU B 110      59.536 -14.612  -7.385  1.00103.11           O  
ANISOU  876  OE1 GLU B 110    15564  10836  12779   2484   2039  -4664       O  
ATOM    877  OE2 GLU B 110      59.859 -13.389  -5.588  1.00100.68           O  
ANISOU  877  OE2 GLU B 110    15031  10551  12672   2451   1991  -4309       O  
ATOM    878  N   ALA B 111      57.678  -9.634  -6.176  1.00 95.18           N  
ANISOU  878  N   ALA B 111    14146  10774  11244   1889   1878  -4060       N  
ATOM    879  CA  ALA B 111      56.475  -8.931  -6.599  1.00 93.98           C  
ANISOU  879  CA  ALA B 111    14025  10839  10845   1709   1780  -4032       C  
ATOM    880  C   ALA B 111      56.193  -7.680  -5.777  1.00 90.20           C  
ANISOU  880  C   ALA B 111    13525  10486  10260   1697   1691  -3765       C  
ATOM    881  O   ALA B 111      55.242  -6.954  -6.088  1.00 89.94           O  
ANISOU  881  O   ALA B 111    13541  10625  10009   1558   1631  -3682       O  
ATOM    882  CB  ALA B 111      55.265  -9.869  -6.535  1.00 94.82           C  
ANISOU  882  CB  ALA B 111    14251  10746  11033   1625   1633  -4136       C  
ATOM    883  N   ALA B 112      56.990  -7.408  -4.743  1.00 69.72           N  
ANISOU  883  N   ALA B 112    10880   7797   7814   1828   1691  -3594       N  
ATOM    884  CA  ALA B 112      56.775  -6.249  -3.890  1.00 64.96           C  
ANISOU  884  CA  ALA B 112    10286   7272   7124   1799   1635  -3309       C  
ATOM    885  C   ALA B 112      57.703  -5.124  -4.310  1.00 64.42           C  
ANISOU  885  C   ALA B 112    10076   7494   6906   1824   1757  -3239       C  
ATOM    886  O   ALA B 112      58.930  -5.311  -4.295  1.00 65.85           O  
ANISOU  886  O   ALA B 112    10141   7677   7202   1959   1853  -3292       O  
ATOM    887  CB  ALA B 112      57.014  -6.608  -2.429  1.00 64.93           C  
ANISOU  887  CB  ALA B 112    10321   6990   7361   1909   1552  -3151       C  
ATOM    888  N   PRO B 113      57.181  -3.954  -4.690  1.00 70.31           N  
ANISOU  888  N   PRO B 113    10822   8482   7410   1695   1759  -3113       N  
ATOM    889  CA  PRO B 113      58.070  -2.834  -5.042  1.00 70.42           C  
ANISOU  889  CA  PRO B 113    10703   8759   7293   1707   1871  -3020       C  
ATOM    890  C   PRO B 113      58.966  -2.387  -3.902  1.00 70.15           C  
ANISOU  890  C   PRO B 113    10594   8657   7403   1830   1878  -2845       C  
ATOM    891  O   PRO B 113      60.028  -1.807  -4.160  1.00 71.31           O  
ANISOU  891  O   PRO B 113    10604   8973   7517   1884   1989  -2822       O  
ATOM    892  CB  PRO B 113      57.091  -1.725  -5.454  1.00 69.58           C  
ANISOU  892  CB  PRO B 113    10641   8856   6940   1539   1830  -2880       C  
ATOM    893  CG  PRO B 113      55.838  -2.444  -5.835  1.00 70.11           C  
ANISOU  893  CG  PRO B 113    10834   8839   6966   1439   1735  -2996       C  
ATOM    894  CD  PRO B 113      55.764  -3.630  -4.921  1.00 70.03           C  
ANISOU  894  CD  PRO B 113    10898   8495   7213   1529   1662  -3058       C  
ATOM    895  N   CYS B 114      58.578  -2.639  -2.649  1.00 64.09           N  
ANISOU  895  N   CYS B 114     9911   7653   6789   1870   1767  -2721       N  
ATOM    896  CA  CYS B 114      59.421  -2.291  -1.514  1.00 63.08           C  
ANISOU  896  CA  CYS B 114     9715   7456   6798   1990   1766  -2564       C  
ATOM    897  C   CYS B 114      60.748  -3.043  -1.517  1.00 65.35           C  
ANISOU  897  C   CYS B 114     9880   7678   7271   2170   1839  -2684       C  
ATOM    898  O   CYS B 114      61.656  -2.663  -0.770  1.00 65.56           O  
ANISOU  898  O   CYS B 114     9808   7712   7392   2279   1858  -2568       O  
ATOM    899  CB  CYS B 114      58.671  -2.555  -0.204  1.00 61.05           C  
ANISOU  899  CB  CYS B 114     9548   6965   6683   1950   1610  -2402       C  
ATOM    900  SG  CYS B 114      58.654  -4.276   0.321  1.00 66.25           S  
ANISOU  900  SG  CYS B 114    10293   7266   7613   2067   1533  -2525       S  
ATOM    901  N   LYS B 115      60.882  -4.093  -2.329  1.00 66.85           N  
ANISOU  901  N   LYS B 115    10067   7808   7526   2203   1881  -2919       N  
ATOM    902  CA  LYS B 115      62.092  -4.903  -2.388  1.00 71.63           C  
ANISOU  902  CA  LYS B 115    10555   8329   8333   2375   1957  -3054       C  
ATOM    903  C   LYS B 115      62.942  -4.606  -3.620  1.00 75.05           C  
ANISOU  903  C   LYS B 115    10854   9017   8644   2367   2135  -3197       C  
ATOM    904  O   LYS B 115      63.792  -5.423  -3.989  1.00 78.31           O  
ANISOU  904  O   LYS B 115    11195   9358   9201   2480   2232  -3360       O  
ATOM    905  CB  LYS B 115      61.730  -6.389  -2.354  1.00 73.45           C  
ANISOU  905  CB  LYS B 115    10878   8262   8767   2425   1898  -3221       C  
ATOM    906  CG  LYS B 115      60.796  -6.778  -1.225  1.00 72.08           C  
ANISOU  906  CG  LYS B 115    10857   7823   8706   2405   1727  -3081       C  
ATOM    907  CD  LYS B 115      61.558  -6.980   0.070  1.00 72.39           C  
ANISOU  907  CD  LYS B 115    10850   7683   8973   2569   1666  -2923       C  
ATOM    908  CE  LYS B 115      60.623  -7.354   1.208  1.00 71.25           C  
ANISOU  908  CE  LYS B 115    10869   7278   8925   2531   1506  -2765       C  
ATOM    909  NZ  LYS B 115      61.380  -7.702   2.442  1.00 71.24           N  
ANISOU  909  NZ  LYS B 115    10789   7109   9170   2655   1422  -2593       N  
ATOM    910  N   GLU B 116      62.734  -3.455  -4.264  1.00 85.90           N  
ANISOU  910  N   GLU B 116    12205  10674   9759   2232   2191  -3122       N  
ATOM    911  CA  GLU B 116      63.449  -3.170  -5.505  1.00 88.02           C  
ANISOU  911  CA  GLU B 116    12382  11181   9883   2196   2371  -3235       C  
ATOM    912  C   GLU B 116      64.935  -2.936  -5.255  1.00 89.59           C  
ANISOU  912  C   GLU B 116    12398  11449  10193   2339   2477  -3199       C  
ATOM    913  O   GLU B 116      65.781  -3.427  -6.012  1.00 92.38           O  
ANISOU  913  O   GLU B 116    12693  11837  10571   2409   2626  -3343       O  
ATOM    914  CB  GLU B 116      62.819  -1.969  -6.211  1.00 86.57           C  
ANISOU  914  CB  GLU B 116    12224  11268   9399   2010   2388  -3128       C  
ATOM    915  CG  GLU B 116      61.885  -2.350  -7.353  1.00 88.48           C  
ANISOU  915  CG  GLU B 116    12604  11554   9462   1871   2410  -3270       C  
ATOM    916  CD  GLU B 116      60.733  -1.378  -7.523  1.00 87.74           C  
ANISOU  916  CD  GLU B 116    12575  11614   9149   1697   2315  -3126       C  
ATOM    917  OE1 GLU B 116      60.969  -0.154  -7.457  1.00 86.80           O  
ANISOU  917  OE1 GLU B 116    12384  11683   8914   1650   2334  -2936       O  
ATOM    918  OE2 GLU B 116      59.590  -1.840  -7.730  1.00 88.22           O  
ANISOU  918  OE2 GLU B 116    12758  11601   9161   1609   2222  -3197       O  
ATOM    919  N   ASN B 117      65.276  -2.197  -4.202  1.00 80.90           N  
ANISOU  919  N   ASN B 117    11221  10363   9155   2390   2409  -2996       N  
ATOM    920  CA  ASN B 117      66.664  -1.908  -3.867  1.00 80.58           C  
ANISOU  920  CA  ASN B 117    10990  10402   9225   2518   2492  -2946       C  
ATOM    921  C   ASN B 117      66.946  -2.313  -2.430  1.00 79.39           C  
ANISOU  921  C   ASN B 117    10820  10023   9324   2675   2368  -2840       C  
ATOM    922  O   ASN B 117      66.103  -2.129  -1.546  1.00 77.71           O  
ANISOU  922  O   ASN B 117    10730   9683   9114   2639   2231  -2695       O  
ATOM    923  CB  ASN B 117      66.995  -0.426  -4.056  1.00 79.51           C  
ANISOU  923  CB  ASN B 117    10758  10554   8899   2417   2556  -2776       C  
ATOM    924  CG  ASN B 117      66.647   0.074  -5.439  1.00 79.52           C  
ANISOU  924  CG  ASN B 117    10796  10782   8636   2251   2663  -2831       C  
ATOM    925  OD1 ASN B 117      67.486   0.080  -6.339  1.00 80.56           O  
ANISOU  925  OD1 ASN B 117    10837  11063   8708   2261   2820  -2917       O  
ATOM    926  ND2 ASN B 117      65.403   0.502  -5.616  1.00 77.56           N  
ANISOU  926  ND2 ASN B 117    10690  10558   8223   2101   2577  -2764       N  
ATOM    927  N   VAL B 118      68.151  -2.837  -2.206  1.00 80.10           N  
ANISOU  927  N   VAL B 118    10755  10064   9614   2845   2423  -2898       N  
ATOM    928  CA  VAL B 118      68.575  -3.366  -0.915  1.00 79.43           C  
ANISOU  928  CA  VAL B 118    10633   9760   9788   3016   2309  -2805       C  
ATOM    929  C   VAL B 118      69.898  -2.720  -0.531  1.00 79.38           C  
ANISOU  929  C   VAL B 118    10401   9917   9844   3115   2371  -2706       C  
ATOM    930  O   VAL B 118      70.831  -2.675  -1.341  1.00 81.01           O  
ANISOU  930  O   VAL B 118    10454  10285  10041   3142   2521  -2816       O  
ATOM    931  CB  VAL B 118      68.716  -4.900  -0.953  1.00 81.66           C  
ANISOU  931  CB  VAL B 118    10945   9763  10318   3150   2288  -2979       C  
ATOM    932  CG1 VAL B 118      69.593  -5.389   0.190  1.00 82.95           C  
ANISOU  932  CG1 VAL B 118    10995   9757  10765   3354   2205  -2884       C  
ATOM    933  CG2 VAL B 118      67.352  -5.553  -0.897  1.00 80.53           C  
ANISOU  933  CG2 VAL B 118    11027   9405  10164   3063   2175  -3021       C  
ATOM    934  N   ILE B 119      69.976  -2.220   0.700  1.00 85.05           N  
ANISOU  934  N   ILE B 119    11097  10594  10625   3149   2258  -2490       N  
ATOM    935  CA  ILE B 119      71.201  -1.690   1.282  1.00 86.46           C  
ANISOU  935  CA  ILE B 119    11050  10893  10907   3217   2271  -2366       C  
ATOM    936  C   ILE B 119      71.456  -2.476   2.560  1.00 88.88           C  
ANISOU  936  C   ILE B 119    11338  10946  11487   3341   2105  -2257       C  
ATOM    937  O   ILE B 119      70.684  -2.378   3.526  1.00 87.60           O  
ANISOU  937  O   ILE B 119    11294  10649  11341   3242   1942  -2079       O  
ATOM    938  CB  ILE B 119      71.112  -0.184   1.560  1.00 83.56           C  
ANISOU  938  CB  ILE B 119    10639  10738  10371   3023   2259  -2154       C  
ATOM    939  CG1 ILE B 119      70.419   0.524   0.394  1.00 82.14           C  
ANISOU  939  CG1 ILE B 119    10552  10746   9912   2866   2371  -2218       C  
ATOM    940  CG2 ILE B 119      72.499   0.395   1.805  1.00 83.93           C  
ANISOU  940  CG2 ILE B 119    10430  10966  10494   3086   2320  -2082       C  
ATOM    941  CD1 ILE B 119      70.625   2.017   0.367  1.00 82.45           C  
ANISOU  941  CD1 ILE B 119    10503  11024   9800   2704   2409  -2045       C  
ATOM    942  N   ASP B 120      72.540  -3.258   2.560  1.00100.29           N  
ANISOU  942  N   ASP B 120    12626  12335  13145   3560   2148  -2360       N  
ATOM    943  CA  ASP B 120      72.851  -4.207   3.618  1.00102.99           C  
ANISOU  943  CA  ASP B 120    12944  12418  13770   3713   1997  -2279       C  
ATOM    944  C   ASP B 120      74.044  -3.809   4.475  1.00103.20           C  
ANISOU  944  C   ASP B 120    12735  12543  13933   3792   1948  -2114       C  
ATOM    945  O   ASP B 120      74.139  -4.265   5.618  1.00104.74           O  
ANISOU  945  O   ASP B 120    12924  12563  14310   3851   1777  -1953       O  
ATOM    946  CB  ASP B 120      73.124  -5.593   3.015  1.00107.29           C  
ANISOU  946  CB  ASP B 120    13494  12763  14509   3912   2056  -2523       C  
ATOM    947  CG  ASP B 120      74.010  -5.525   1.779  1.00111.44           C  
ANISOU  947  CG  ASP B 120    13857  13489  14997   3915   2268  -2713       C  
ATOM    948  OD1 ASP B 120      74.144  -6.552   1.079  1.00114.54           O  
ANISOU  948  OD1 ASP B 120    14272  13740  15507   3978   2347  -2899       O  
ATOM    949  OD2 ASP B 120      74.570  -4.441   1.508  1.00111.40           O  
ANISOU  949  OD2 ASP B 120    13711  13779  14838   3849   2365  -2663       O  
ATOM    950  N   LYS B 121      74.955  -2.990   3.953  1.00 92.98           N  
ANISOU  950  N   LYS B 121    11244  11530  12554   3787   2089  -2145       N  
ATOM    951  CA  LYS B 121      76.128  -2.560   4.699  1.00 93.38           C  
ANISOU  951  CA  LYS B 121    11052  11700  12727   3850   2049  -2000       C  
ATOM    952  C   LYS B 121      76.438  -1.113   4.346  1.00 91.82           C  
ANISOU  952  C   LYS B 121    10747  11822  12317   3677   2152  -1931       C  
ATOM    953  O   LYS B 121      76.041  -0.611   3.290  1.00 90.20           O  
ANISOU  953  O   LYS B 121    10607  11765  11900   3570   2296  -2038       O  
ATOM    954  CB  LYS B 121      77.337  -3.461   4.419  1.00 95.30           C  
ANISOU  954  CB  LYS B 121    11087  11912  13209   4119   2126  -2150       C  
ATOM    955  CG  LYS B 121      77.682  -3.613   2.947  1.00 96.91           C  
ANISOU  955  CG  LYS B 121    11237  12250  13336   4141   2357  -2411       C  
ATOM    956  CD  LYS B 121      78.670  -4.752   2.723  1.00100.75           C  
ANISOU  956  CD  LYS B 121    11575  12602  14103   4334   2407  -2535       C  
ATOM    957  CE  LYS B 121      79.731  -4.811   3.817  1.00100.89           C  
ANISOU  957  CE  LYS B 121    11361  12617  14357   4501   2291  -2379       C  
ATOM    958  NZ  LYS B 121      80.507  -3.543   3.939  1.00 98.62           N  
ANISOU  958  NZ  LYS B 121    10858  12664  13950   4431   2347  -2272       N  
ATOM    959  N   ASP B 122      77.167  -0.450   5.245  1.00 86.34           N  
ANISOU  959  N   ASP B 122     9887  11234  11685   3646   2069  -1744       N  
ATOM    960  CA  ASP B 122      77.377   0.996   5.183  1.00 86.08           C  
ANISOU  960  CA  ASP B 122     9767  11461  11477   3452   2122  -1632       C  
ATOM    961  C   ASP B 122      76.036   1.722   5.118  1.00 82.35           C  
ANISOU  961  C   ASP B 122     9532  10973  10784   3224   2086  -1560       C  
ATOM    962  O   ASP B 122      75.814   2.609   4.292  1.00 81.89           O  
ANISOU  962  O   ASP B 122     9492  11095  10529   3083   2208  -1585       O  
ATOM    963  CB  ASP B 122      78.272   1.381   4.004  1.00 88.29           C  
ANISOU  963  CB  ASP B 122     9862  12000  11686   3484   2348  -1776       C  
ATOM    964  CG  ASP B 122      79.707   0.943   4.197  1.00 92.17           C  
ANISOU  964  CG  ASP B 122    10068  12557  12394   3685   2381  -1812       C  
ATOM    965  OD1 ASP B 122      80.543   1.796   4.563  1.00 93.24           O  
ANISOU  965  OD1 ASP B 122    10002  12884  12540   3621   2383  -1692       O  
ATOM    966  OD2 ASP B 122      79.998  -0.252   3.983  1.00 94.25           O  
ANISOU  966  OD2 ASP B 122    10304  12676  12830   3906   2404  -1964       O  
ATOM    967  N   ILE B 123      75.128   1.321   6.008  1.00 73.57           N  
ANISOU  967  N   ILE B 123     8599   9645   9711   3189   1912  -1462       N  
ATOM    968  CA  ILE B 123      73.777   1.865   6.004  1.00 71.26           C  
ANISOU  968  CA  ILE B 123     8531   9310   9234   2993   1868  -1404       C  
ATOM    969  C   ILE B 123      73.816   3.337   6.384  1.00 69.60           C  
ANISOU  969  C   ILE B 123     8264   9281   8901   2797   1853  -1245       C  
ATOM    970  O   ILE B 123      74.369   3.717   7.424  1.00 70.14           O  
ANISOU  970  O   ILE B 123     8217   9379   9055   2779   1747  -1103       O  
ATOM    971  CB  ILE B 123      72.875   1.065   6.953  1.00 72.50           C  
ANISOU  971  CB  ILE B 123     8866   9204   9476   3003   1688  -1327       C  
ATOM    972  CG1 ILE B 123      72.534  -0.284   6.327  1.00 74.04           C  
ANISOU  972  CG1 ILE B 123     9172   9203   9758   3150   1721  -1507       C  
ATOM    973  CG2 ILE B 123      71.609   1.847   7.276  1.00 70.01           C  
ANISOU  973  CG2 ILE B 123     8733   8878   8987   2785   1618  -1220       C  
ATOM    974  CD1 ILE B 123      71.441  -1.003   7.038  1.00 74.00           C  
ANISOU  974  CD1 ILE B 123     9372   8944   9799   3118   1567  -1441       C  
ATOM    975  N   ASN B 124      73.224   4.173   5.536  1.00 64.51           N  
ANISOU  975  N   ASN B 124     7699   8755   8058   2648   1953  -1270       N  
ATOM    976  CA  ASN B 124      73.184   5.616   5.745  1.00 64.63           C  
ANISOU  976  CA  ASN B 124     7673   8923   7961   2456   1952  -1132       C  
ATOM    977  C   ASN B 124      71.776   6.087   5.410  1.00 63.35           C  
ANISOU  977  C   ASN B 124     7730   8714   7626   2298   1938  -1112       C  
ATOM    978  O   ASN B 124      71.386   6.093   4.238  1.00 63.03           O  
ANISOU  978  O   ASN B 124     7759   8738   7453   2276   2056  -1214       O  
ATOM    979  CB  ASN B 124      74.227   6.326   4.880  1.00 66.07           C  
ANISOU  979  CB  ASN B 124     7659   9351   8094   2441   2119  -1167       C  
ATOM    980  CG  ASN B 124      74.402   7.788   5.248  1.00 66.39           C  
ANISOU  980  CG  ASN B 124     7625   9528   8073   2254   2103  -1012       C  
ATOM    981  OD1 ASN B 124      73.526   8.402   5.858  1.00 64.81           O  
ANISOU  981  OD1 ASN B 124     7553   9253   7819   2114   1999   -906       O  
ATOM    982  ND2 ASN B 124      75.545   8.353   4.876  1.00 63.80           N  
ANISOU  982  ND2 ASN B 124     7081   9398   7762   2247   2212  -1005       N  
ATOM    983  N   LEU B 125      71.015   6.474   6.437  1.00 64.32           N  
ANISOU  983  N   LEU B 125     7954   8738   7748   2190   1793   -983       N  
ATOM    984  CA  LEU B 125      69.646   6.925   6.214  1.00 62.06           C  
ANISOU  984  CA  LEU B 125     7862   8401   7318   2047   1769   -957       C  
ATOM    985  C   LEU B 125      69.599   8.173   5.344  1.00 61.08           C  
ANISOU  985  C   LEU B 125     7708   8454   7046   1908   1879   -928       C  
ATOM    986  O   LEU B 125      68.620   8.389   4.620  1.00 60.80           O  
ANISOU  986  O   LEU B 125     7810   8416   6874   1827   1912   -951       O  
ATOM    987  CB  LEU B 125      68.956   7.192   7.553  1.00 62.23           C  
ANISOU  987  CB  LEU B 125     7964   8309   7372   1957   1604   -827       C  
ATOM    988  CG  LEU B 125      68.589   5.973   8.400  1.00 61.99           C  
ANISOU  988  CG  LEU B 125     8023   8082   7450   2052   1478   -826       C  
ATOM    989  CD1 LEU B 125      68.249   6.390   9.821  1.00 62.05           C  
ANISOU  989  CD1 LEU B 125     8052   8044   7482   1958   1329   -682       C  
ATOM    990  CD2 LEU B 125      67.430   5.223   7.772  1.00 60.32           C  
ANISOU  990  CD2 LEU B 125     8005   7740   7174   2057   1486   -918       C  
ATOM    991  N   PHE B 126      70.644   9.000   5.394  1.00 66.03           N  
ANISOU  991  N   PHE B 126     8151   9235   7702   1873   1933   -867       N  
ATOM    992  CA  PHE B 126      70.637  10.249   4.641  1.00 67.67           C  
ANISOU  992  CA  PHE B 126     8326   9600   7787   1727   2029   -809       C  
ATOM    993  C   PHE B 126      70.764  10.005   3.145  1.00 69.41           C  
ANISOU  993  C   PHE B 126     8545   9947   7882   1762   2193   -919       C  
ATOM    994  O   PHE B 126      70.277  10.812   2.344  1.00 68.39           O  
ANISOU  994  O   PHE B 126     8468   9911   7607   1638   2257   -876       O  
ATOM    995  CB  PHE B 126      71.758  11.161   5.133  1.00 69.09           C  
ANISOU  995  CB  PHE B 126     8305   9903   8045   1671   2038   -715       C  
ATOM    996  CG  PHE B 126      71.522  11.712   6.506  1.00 69.73           C  
ANISOU  996  CG  PHE B 126     8397   9895   8204   1586   1885   -603       C  
ATOM    997  CD1 PHE B 126      71.701  10.915   7.622  1.00 70.67           C  
ANISOU  997  CD1 PHE B 126     8504   9906   8440   1682   1760   -603       C  
ATOM    998  CD2 PHE B 126      71.116  13.023   6.683  1.00 69.99           C  
ANISOU  998  CD2 PHE B 126     8452   9951   8191   1409   1865   -501       C  
ATOM    999  CE1 PHE B 126      71.479  11.412   8.883  1.00 69.58           C  
ANISOU  999  CE1 PHE B 126     8377   9712   8348   1595   1623   -509       C  
ATOM   1000  CE2 PHE B 126      70.895  13.529   7.950  1.00 69.82           C  
ANISOU 1000  CE2 PHE B 126     8440   9855   8233   1330   1732   -425       C  
ATOM   1001  CZ  PHE B 126      71.078  12.721   9.052  1.00 69.59           C  
ANISOU 1001  CZ  PHE B 126     8399   9745   8296   1419   1613   -433       C  
ATOM   1002  N   GLU B 127      71.401   8.904   2.747  1.00 83.20           N  
ANISOU 1002  N   GLU B 127    10229  11702   9681   1930   2261  -1063       N  
ATOM   1003  CA  GLU B 127      71.493   8.570   1.331  1.00 83.61           C  
ANISOU 1003  CA  GLU B 127    10285  11883   9601   1969   2422  -1200       C  
ATOM   1004  C   GLU B 127      70.166   8.112   0.741  1.00 82.02           C  
ANISOU 1004  C   GLU B 127    10307  11589   9268   1940   2401  -1274       C  
ATOM   1005  O   GLU B 127      70.133   7.721  -0.431  1.00 82.93           O  
ANISOU 1005  O   GLU B 127    10446  11805   9257   1972   2523  -1409       O  
ATOM   1006  CB  GLU B 127      72.557   7.495   1.106  1.00 85.58           C  
ANISOU 1006  CB  GLU B 127    10397  12157   9963   2170   2504  -1357       C  
ATOM   1007  CG  GLU B 127      73.979   7.971   1.348  1.00 88.35           C  
ANISOU 1007  CG  GLU B 127    10492  12663  10413   2198   2566  -1305       C  
ATOM   1008  CD  GLU B 127      74.981   6.836   1.312  1.00 91.68           C  
ANISOU 1008  CD  GLU B 127    10771  13077  10988   2419   2621  -1455       C  
ATOM   1009  OE1 GLU B 127      76.199   7.108   1.371  1.00 93.53           O  
ANISOU 1009  OE1 GLU B 127    10774  13458  11303   2461   2690  -1438       O  
ATOM   1010  OE2 GLU B 127      74.546   5.669   1.214  1.00 91.57           O  
ANISOU 1010  OE2 GLU B 127    10869  12902  11022   2551   2595  -1593       O  
ATOM   1011  N   ILE B 128      69.080   8.152   1.511  1.00 70.39           N  
ANISOU 1011  N   ILE B 128     8988   9942   7814   1875   2253  -1197       N  
ATOM   1012  CA  ILE B 128      67.773   7.718   1.035  1.00 68.23           C  
ANISOU 1012  CA  ILE B 128     8918   9576   7429   1839   2218  -1259       C  
ATOM   1013  C   ILE B 128      66.732   8.772   1.380  1.00 66.50           C  
ANISOU 1013  C   ILE B 128     8799   9331   7137   1667   2129  -1102       C  
ATOM   1014  O   ILE B 128      66.014   9.266   0.504  1.00 64.67           O  
ANISOU 1014  O   ILE B 128     8648   9180   6742   1568   2168  -1087       O  
ATOM   1015  CB  ILE B 128      67.388   6.359   1.641  1.00 67.27           C  
ANISOU 1015  CB  ILE B 128     8895   9230   7434   1963   2121  -1357       C  
ATOM   1016  CG1 ILE B 128      68.326   5.264   1.141  1.00 69.49           C  
ANISOU 1016  CG1 ILE B 128     9088   9520   7795   2146   2218  -1538       C  
ATOM   1017  CG2 ILE B 128      65.942   6.021   1.320  1.00 64.88           C  
ANISOU 1017  CG2 ILE B 128     8801   8824   7029   1895   2062  -1397       C  
ATOM   1018  CD1 ILE B 128      68.394   4.098   2.072  1.00 71.32           C  
ANISOU 1018  CD1 ILE B 128     9347   9523   8228   2284   2108  -1576       C  
ATOM   1019  N   LEU B 129      66.645   9.120   2.663  1.00 58.37           N  
ANISOU 1019  N   LEU B 129     7758   8191   6227   1634   2007   -986       N  
ATOM   1020  CA  LEU B 129      65.622  10.032   3.143  1.00 55.08           C  
ANISOU 1020  CA  LEU B 129     7435   7723   5771   1489   1916   -858       C  
ATOM   1021  C   LEU B 129      66.185  11.438   3.231  1.00 55.47           C  
ANISOU 1021  C   LEU B 129     7364   7894   5819   1378   1950   -726       C  
ATOM   1022  O   LEU B 129      67.209  11.642   3.904  1.00 57.52           O  
ANISOU 1022  O   LEU B 129     7481   8183   6191   1406   1945   -690       O  
ATOM   1023  CB  LEU B 129      65.113   9.590   4.507  1.00 54.30           C  
ANISOU 1023  CB  LEU B 129     7404   7440   5790   1504   1767   -821       C  
ATOM   1024  CG  LEU B 129      64.607   8.155   4.609  1.00 53.65           C  
ANISOU 1024  CG  LEU B 129     7435   7205   5746   1608   1716   -931       C  
ATOM   1025  CD1 LEU B 129      64.203   7.849   6.041  1.00 54.87           C  
ANISOU 1025  CD1 LEU B 129     7636   7203   6010   1603   1571   -858       C  
ATOM   1026  CD2 LEU B 129      63.443   7.936   3.658  1.00 51.59           C  
ANISOU 1026  CD2 LEU B 129     7326   6930   5346   1558   1736   -998       C  
ATOM   1027  N   PRO B 130      65.577  12.424   2.580  1.00 57.64           N  
ANISOU 1027  N   PRO B 130     7684   8237   5980   1252   1978   -646       N  
ATOM   1028  CA  PRO B 130      65.966  13.815   2.835  1.00 58.04           C  
ANISOU 1028  CA  PRO B 130     7638   8352   6062   1132   1985   -505       C  
ATOM   1029  C   PRO B 130      65.511  14.271   4.212  1.00 57.28           C  
ANISOU 1029  C   PRO B 130     7569   8116   6078   1077   1851   -433       C  
ATOM   1030  O   PRO B 130      64.500  14.969   4.345  1.00 56.73           O  
ANISOU 1030  O   PRO B 130     7591   7983   5982    979   1794   -365       O  
ATOM   1031  CB  PRO B 130      65.265  14.593   1.713  1.00 57.07           C  
ANISOU 1031  CB  PRO B 130     7582   8314   5790   1023   2037   -437       C  
ATOM   1032  CG  PRO B 130      64.905  13.558   0.682  1.00 56.69           C  
ANISOU 1032  CG  PRO B 130     7618   8312   5608   1098   2096   -566       C  
ATOM   1033  CD  PRO B 130      64.633  12.312   1.458  1.00 55.31           C  
ANISOU 1033  CD  PRO B 130     7513   7980   5522   1214   2014   -681       C  
ATOM   1034  N   LEU B 131      66.249  13.869   5.242  1.00 56.07           N  
ANISOU 1034  N   LEU B 131     7332   7922   6049   1141   1799   -453       N  
ATOM   1035  CA  LEU B 131      65.889  14.210   6.610  1.00 57.42           C  
ANISOU 1035  CA  LEU B 131     7524   7984   6309   1091   1673   -399       C  
ATOM   1036  C   LEU B 131      66.049  15.707   6.852  1.00 58.25           C  
ANISOU 1036  C   LEU B 131     7559   8128   6445    950   1672   -297       C  
ATOM   1037  O   LEU B 131      66.872  16.378   6.225  1.00 58.64           O  
ANISOU 1037  O   LEU B 131     7494   8296   6492    907   1762   -255       O  
ATOM   1038  CB  LEU B 131      66.749  13.423   7.599  1.00 57.96           C  
ANISOU 1038  CB  LEU B 131     7505   8027   6489   1191   1614   -432       C  
ATOM   1039  CG  LEU B 131      66.607  11.900   7.552  1.00 58.95           C  
ANISOU 1039  CG  LEU B 131     7700   8071   6626   1337   1594   -525       C  
ATOM   1040  CD1 LEU B 131      67.789  11.232   8.235  1.00 60.41           C  
ANISOU 1040  CD1 LEU B 131     7750   8269   6934   1451   1564   -540       C  
ATOM   1041  CD2 LEU B 131      65.296  11.460   8.188  1.00 59.78           C  
ANISOU 1041  CD2 LEU B 131     7974   8026   6714   1313   1486   -523       C  
ATOM   1042  N   TYR B 132      65.247  16.226   7.778  1.00 53.80           N  
ANISOU 1042  N   TYR B 132     7062   7461   5917    873   1574   -260       N  
ATOM   1043  CA  TYR B 132      65.231  17.652   8.070  1.00 53.47           C  
ANISOU 1043  CA  TYR B 132     6974   7418   5924    738   1563   -180       C  
ATOM   1044  C   TYR B 132      64.691  17.854   9.478  1.00 53.56           C  
ANISOU 1044  C   TYR B 132     7024   7327   5999    695   1445   -188       C  
ATOM   1045  O   TYR B 132      64.197  16.922  10.117  1.00 51.49           O  
ANISOU 1045  O   TYR B 132     6839   7001   5724    759   1376   -235       O  
ATOM   1046  CB  TYR B 132      64.391  18.421   7.045  1.00 51.87           C  
ANISOU 1046  CB  TYR B 132     6848   7212   5649    661   1611   -119       C  
ATOM   1047  CG  TYR B 132      62.932  18.024   7.036  1.00 50.35           C  
ANISOU 1047  CG  TYR B 132     6817   6918   5396    672   1552   -143       C  
ATOM   1048  CD1 TYR B 132      62.502  16.899   6.344  1.00 51.17           C  
ANISOU 1048  CD1 TYR B 132     7009   7031   5403    759   1573   -207       C  
ATOM   1049  CD2 TYR B 132      61.984  18.773   7.720  1.00 48.06           C  
ANISOU 1049  CD2 TYR B 132     6585   6525   5152    594   1478   -113       C  
ATOM   1050  CE1 TYR B 132      61.169  16.532   6.335  1.00 49.92           C  
ANISOU 1050  CE1 TYR B 132     6989   6786   5193    758   1516   -229       C  
ATOM   1051  CE2 TYR B 132      60.651  18.413   7.717  1.00 47.11           C  
ANISOU 1051  CE2 TYR B 132     6595   6324   4981    602   1428   -134       C  
ATOM   1052  CZ  TYR B 132      60.249  17.293   7.024  1.00 47.45           C  
ANISOU 1052  CZ  TYR B 132     6721   6383   4926    679   1444   -186       C  
ATOM   1053  OH  TYR B 132      58.921  16.935   7.020  1.00 45.33           O  
ANISOU 1053  OH  TYR B 132     6572   6040   4611    676   1390   -207       O  
ATOM   1054  N   ARG B 133      64.793  19.092   9.953  1.00 52.19           N  
ANISOU 1054  N   ARG B 133     6796   7140   5894    580   1426   -144       N  
ATOM   1055  CA  ARG B 133      64.291  19.465  11.269  1.00 51.26           C  
ANISOU 1055  CA  ARG B 133     6705   6943   5827    521   1326   -167       C  
ATOM   1056  C   ARG B 133      62.863  19.980  11.130  1.00 49.75           C  
ANISOU 1056  C   ARG B 133     6640   6651   5613    468   1308   -157       C  
ATOM   1057  O   ARG B 133      62.620  20.971  10.432  1.00 49.49           O  
ANISOU 1057  O   ARG B 133     6605   6600   5600    398   1352   -100       O  
ATOM   1058  CB  ARG B 133      65.193  20.518  11.912  1.00 51.98           C  
ANISOU 1058  CB  ARG B 133     6663   7069   6017    424   1313   -150       C  
ATOM   1059  CG  ARG B 133      64.643  21.111  13.196  1.00 52.79           C  
ANISOU 1059  CG  ARG B 133     6792   7100   6166    343   1222   -191       C  
ATOM   1060  CD  ARG B 133      65.736  21.805  13.996  1.00 55.96           C  
ANISOU 1060  CD  ARG B 133     7050   7558   6653    264   1191   -203       C  
ATOM   1061  NE  ARG B 133      66.364  20.904  14.957  1.00 57.27           N  
ANISOU 1061  NE  ARG B 133     7164   7794   6802    323   1117   -238       N  
ATOM   1062  CZ  ARG B 133      67.666  20.637  14.995  1.00 59.38           C  
ANISOU 1062  CZ  ARG B 133     7288   8168   7105    354   1121   -222       C  
ATOM   1063  NH1 ARG B 133      68.489  21.206  14.125  1.00 60.71           N  
ANISOU 1063  NH1 ARG B 133     7351   8395   7323    322   1207   -180       N  
ATOM   1064  NH2 ARG B 133      68.147  19.805  15.909  1.00 59.32           N  
ANISOU 1064  NH2 ARG B 133     7236   8216   7085    413   1037   -240       N  
ATOM   1065  N   ILE B 134      61.925  19.310  11.799  1.00 50.76           N  
ANISOU 1065  N   ILE B 134     6869   6715   5704    499   1240   -203       N  
ATOM   1066  CA  ILE B 134      60.513  19.649  11.659  1.00 48.32           C  
ANISOU 1066  CA  ILE B 134     6670   6319   5370    463   1222   -201       C  
ATOM   1067  C   ILE B 134      60.180  20.924  12.425  1.00 51.32           C  
ANISOU 1067  C   ILE B 134     7023   6640   5837    359   1190   -207       C  
ATOM   1068  O   ILE B 134      59.625  21.873  11.865  1.00 52.87           O  
ANISOU 1068  O   ILE B 134     7235   6783   6072    306   1215   -165       O  
ATOM   1069  CB  ILE B 134      59.638  18.470  12.118  1.00 45.38           C  
ANISOU 1069  CB  ILE B 134     6405   5906   4933    523   1167   -248       C  
ATOM   1070  CG1 ILE B 134      59.980  17.215  11.315  1.00 44.80           C  
ANISOU 1070  CG1 ILE B 134     6360   5867   4794    627   1200   -258       C  
ATOM   1071  CG2 ILE B 134      58.164  18.815  11.974  1.00 45.72           C  
ANISOU 1071  CG2 ILE B 134     6544   5873   4955    484   1149   -248       C  
ATOM   1072  CD1 ILE B 134      59.298  15.967  11.819  1.00 42.18           C  
ANISOU 1072  CD1 ILE B 134     6125   5480   4420    683   1140   -299       C  
ATOM   1073  N   ASN B 135      60.493  20.966  13.716  1.00 48.08           N  
ANISOU 1073  N   ASN B 135     6571   6238   5462    329   1131   -261       N  
ATOM   1074  CA  ASN B 135      60.281  22.161  14.517  1.00 47.59           C  
ANISOU 1074  CA  ASN B 135     6473   6125   5483    228   1104   -298       C  
ATOM   1075  C   ASN B 135      61.603  22.588  15.142  1.00 50.63           C  
ANISOU 1075  C   ASN B 135     6731   6575   5930    178   1090   -314       C  
ATOM   1076  O   ASN B 135      62.455  21.753  15.457  1.00 49.98           O  
ANISOU 1076  O   ASN B 135     6599   6579   5811    229   1068   -315       O  
ATOM   1077  CB  ASN B 135      59.215  21.933  15.593  1.00 44.91           C  
ANISOU 1077  CB  ASN B 135     6206   5746   5111    214   1043   -371       C  
ATOM   1078  CG  ASN B 135      57.806  22.140  15.064  1.00 43.46           C  
ANISOU 1078  CG  ASN B 135     6116   5478   4921    219   1058   -364       C  
ATOM   1079  OD1 ASN B 135      57.390  23.269  14.800  1.00 46.85           O  
ANISOU 1079  OD1 ASN B 135     6532   5832   5435    167   1078   -357       O  
ATOM   1080  ND2 ASN B 135      57.067  21.049  14.902  1.00 40.34           N  
ANISOU 1080  ND2 ASN B 135     5809   5086   4434    281   1043   -361       N  
ATOM   1081  N   GLU B 136      61.761  23.903  15.321  1.00 49.61           N  
ANISOU 1081  N   GLU B 136     6545   6399   5906     77   1098   -327       N  
ATOM   1082  CA  GLU B 136      63.087  24.465  15.563  1.00 52.24           C  
ANISOU 1082  CA  GLU B 136     6744   6791   6312     13   1101   -325       C  
ATOM   1083  C   GLU B 136      63.703  23.974  16.869  1.00 51.85           C  
ANISOU 1083  C   GLU B 136     6638   6830   6231      6   1023   -396       C  
ATOM   1084  O   GLU B 136      64.932  23.922  16.986  1.00 53.41           O  
ANISOU 1084  O   GLU B 136     6719   7121   6455     -5   1016   -380       O  
ATOM   1085  CB  GLU B 136      63.022  25.994  15.543  1.00 56.66           C  
ANISOU 1085  CB  GLU B 136     7265   7254   7008   -105   1118   -332       C  
ATOM   1086  CG  GLU B 136      62.422  26.622  16.787  1.00 61.14           C  
ANISOU 1086  CG  GLU B 136     7851   7757   7622   -177   1059   -454       C  
ATOM   1087  CD  GLU B 136      63.054  27.960  17.122  1.00 65.49           C  
ANISOU 1087  CD  GLU B 136     8307   8255   8321   -305   1056   -494       C  
ATOM   1088  OE1 GLU B 136      63.354  28.729  16.182  1.00 66.34           O  
ANISOU 1088  OE1 GLU B 136     8380   8299   8527   -347   1110   -405       O  
ATOM   1089  OE2 GLU B 136      63.250  28.241  18.324  1.00 66.08           O  
ANISOU 1089  OE2 GLU B 136     8343   8354   8411   -371    999   -614       O  
ATOM   1090  N   GLN B 137      62.885  23.601  17.852  1.00 52.33           N  
ANISOU 1090  N   GLN B 137     6772   6879   6230     10    962   -466       N  
ATOM   1091  CA  GLN B 137      63.396  23.131  19.133  1.00 52.46           C  
ANISOU 1091  CA  GLN B 137     6742   6995   6196     -6    878   -519       C  
ATOM   1092  C   GLN B 137      63.417  21.610  19.241  1.00 52.28           C  
ANISOU 1092  C   GLN B 137     6763   7033   6069    108    842   -472       C  
ATOM   1093  O   GLN B 137      63.600  21.083  20.343  1.00 55.22           O  
ANISOU 1093  O   GLN B 137     7121   7481   6379    102    761   -496       O  
ATOM   1094  CB  GLN B 137      62.582  23.729  20.282  1.00 52.92           C  
ANISOU 1094  CB  GLN B 137     6839   7025   6242    -93    833   -630       C  
ATOM   1095  CG  GLN B 137      62.705  25.239  20.406  1.00 55.11           C  
ANISOU 1095  CG  GLN B 137     7059   7235   6646   -211    853   -702       C  
ATOM   1096  CD  GLN B 137      64.128  25.686  20.681  1.00 58.65           C  
ANISOU 1096  CD  GLN B 137     7366   7763   7154   -281    828   -707       C  
ATOM   1097  OE1 GLN B 137      64.782  25.190  21.599  1.00 59.44           O  
ANISOU 1097  OE1 GLN B 137     7408   7990   7187   -293    755   -735       O  
ATOM   1098  NE2 GLN B 137      64.616  26.630  19.884  1.00 61.07           N  
ANISOU 1098  NE2 GLN B 137     7611   8003   7589   -335    884   -671       N  
ATOM   1099  N   ASP B 138      63.241  20.898  18.129  1.00 45.03           N  
ANISOU 1099  N   ASP B 138     5897   6083   5130    207    897   -407       N  
ATOM   1100  CA  ASP B 138      63.331  19.446  18.151  1.00 44.75           C  
ANISOU 1100  CA  ASP B 138     5900   6080   5023    320    865   -369       C  
ATOM   1101  C   ASP B 138      64.743  19.007  18.516  1.00 49.58           C  
ANISOU 1101  C   ASP B 138     6382   6797   5659    357    825   -341       C  
ATOM   1102  O   ASP B 138      65.722  19.720  18.281  1.00 51.76           O  
ANISOU 1102  O   ASP B 138     6536   7126   6005    316    852   -337       O  
ATOM   1103  CB  ASP B 138      62.947  18.860  16.792  1.00 42.28           C  
ANISOU 1103  CB  ASP B 138     5659   5713   4692    411    940   -327       C  
ATOM   1104  CG  ASP B 138      61.460  18.943  16.517  1.00 41.40           C  
ANISOU 1104  CG  ASP B 138     5681   5509   4541    395    956   -344       C  
ATOM   1105  OD1 ASP B 138      60.693  19.277  17.444  1.00 40.97           O  
ANISOU 1105  OD1 ASP B 138     5666   5430   4469    330    910   -389       O  
ATOM   1106  OD2 ASP B 138      61.060  18.669  15.366  1.00 41.32           O  
ANISOU 1106  OD2 ASP B 138     5729   5461   4511    446   1014   -316       O  
ATOM   1107  N   GLY B 139      64.844  17.812  19.100  1.00 45.42           N  
ANISOU 1107  N   GLY B 139     5876   6300   5081    436    754   -314       N  
ATOM   1108  CA  GLY B 139      66.152  17.284  19.446  1.00 46.39           C  
ANISOU 1108  CA  GLY B 139     5871   6520   5236    491    704   -276       C  
ATOM   1109  C   GLY B 139      66.978  16.910  18.232  1.00 46.86           C  
ANISOU 1109  C   GLY B 139     5859   6590   5353    595    786   -245       C  
ATOM   1110  O   GLY B 139      68.210  16.870  18.302  1.00 49.83           O  
ANISOU 1110  O   GLY B 139     6087   7059   5787    623    774   -224       O  
ATOM   1111  N   GLY B 140      66.323  16.636  17.113  1.00 52.90           N  
ANISOU 1111  N   GLY B 140     6720   7277   6100    649    872   -248       N  
ATOM   1112  CA  GLY B 140      67.040  16.289  15.907  1.00 52.42           C  
ANISOU 1112  CA  GLY B 140     6599   7243   6074    742    964   -235       C  
ATOM   1113  C   GLY B 140      66.117  16.173  14.715  1.00 50.74           C  
ANISOU 1113  C   GLY B 140     6510   6954   5813    767   1052   -248       C  
ATOM   1114  O   GLY B 140      65.019  16.733  14.699  1.00 48.52           O  
ANISOU 1114  O   GLY B 140     6333   6606   5494    691   1054   -258       O  
ATOM   1115  N   PHE B 141      66.587  15.445  13.706  1.00 61.20           N  
ANISOU 1115  N   PHE B 141     7814   8300   7140    877   1125   -255       N  
ATOM   1116  CA  PHE B 141      65.780  15.176  12.526  1.00 61.85           C  
ANISOU 1116  CA  PHE B 141     8011   8331   7158    909   1204   -276       C  
ATOM   1117  C   PHE B 141      64.885  13.976  12.800  1.00 60.20           C  
ANISOU 1117  C   PHE B 141     7941   8021   6912    982   1145   -301       C  
ATOM   1118  O   PHE B 141      65.347  12.953  13.315  1.00 60.53           O  
ANISOU 1118  O   PHE B 141     7961   8047   6991   1077   1090   -303       O  
ATOM   1119  CB  PHE B 141      66.667  14.919  11.308  1.00 64.21           C  
ANISOU 1119  CB  PHE B 141     8225   8712   7459    987   1317   -292       C  
ATOM   1120  CG  PHE B 141      67.690  15.993  11.065  1.00 66.11           C  
ANISOU 1120  CG  PHE B 141     8309   9065   7746    914   1377   -256       C  
ATOM   1121  CD1 PHE B 141      67.420  17.315  11.384  1.00 66.97           C  
ANISOU 1121  CD1 PHE B 141     8408   9164   7873    768   1362   -214       C  
ATOM   1122  CD2 PHE B 141      68.923  15.679  10.519  1.00 67.00           C  
ANISOU 1122  CD2 PHE B 141     8276   9286   7893    989   1451   -267       C  
ATOM   1123  CE1 PHE B 141      68.362  18.302  11.164  1.00 69.11           C  
ANISOU 1123  CE1 PHE B 141     8535   9523   8199    687   1414   -176       C  
ATOM   1124  CE2 PHE B 141      69.868  16.662  10.296  1.00 69.37           C  
ANISOU 1124  CE2 PHE B 141     8423   9697   8238    908   1509   -226       C  
ATOM   1125  CZ  PHE B 141      69.587  17.975  10.619  1.00 70.33           C  
ANISOU 1125  CZ  PHE B 141     8544   9798   8379    751   1488   -176       C  
ATOM   1126  N   TYR B 142      63.607  14.098  12.456  1.00 48.11           N  
ANISOU 1126  N   TYR B 142     6546   6417   5316    936   1151   -312       N  
ATOM   1127  CA  TYR B 142      62.605  13.134  12.879  1.00 46.78           C  
ANISOU 1127  CA  TYR B 142     6511   6150   5114    966   1085   -327       C  
ATOM   1128  C   TYR B 142      61.901  12.502  11.688  1.00 45.60           C  
ANISOU 1128  C   TYR B 142     6468   5952   4906   1015   1142   -371       C  
ATOM   1129  O   TYR B 142      61.561  13.184  10.715  1.00 44.36           O  
ANISOU 1129  O   TYR B 142     6327   5827   4700    971   1213   -373       O  
ATOM   1130  CB  TYR B 142      61.567  13.791  13.790  1.00 42.51           C  
ANISOU 1130  CB  TYR B 142     6033   5569   4547    853   1021   -310       C  
ATOM   1131  CG  TYR B 142      61.879  13.655  15.260  1.00 45.99           C  
ANISOU 1131  CG  TYR B 142     6433   6028   5013    829    923   -286       C  
ATOM   1132  CD1 TYR B 142      62.716  14.561  15.898  1.00 47.39           C  
ANISOU 1132  CD1 TYR B 142     6490   6287   5230    768    906   -274       C  
ATOM   1133  CD2 TYR B 142      61.338  12.621  16.012  1.00 47.51           C  
ANISOU 1133  CD2 TYR B 142     6708   6162   5183    856    844   -270       C  
ATOM   1134  CE1 TYR B 142      63.003  14.442  17.245  1.00 48.50           C  
ANISOU 1134  CE1 TYR B 142     6590   6465   5371    737    809   -255       C  
ATOM   1135  CE2 TYR B 142      61.618  12.493  17.357  1.00 48.84           C  
ANISOU 1135  CE2 TYR B 142     6839   6368   5352    825    750   -232       C  
ATOM   1136  CZ  TYR B 142      62.450  13.408  17.969  1.00 49.12           C  
ANISOU 1136  CZ  TYR B 142     6753   6500   5411    767    732   -229       C  
ATOM   1137  OH  TYR B 142      62.735  13.282  19.309  1.00 50.99           O  
ANISOU 1137  OH  TYR B 142     6950   6795   5628    728    632   -195       O  
ATOM   1138  N   ILE B 143      61.692  11.192  11.780  1.00 53.50           N  
ANISOU 1138  N   ILE B 143     7538   6874   5914   1102   1105   -401       N  
ATOM   1139  CA  ILE B 143      60.759  10.477  10.918  1.00 51.52           C  
ANISOU 1139  CA  ILE B 143     7415   6554   5606   1127   1130   -455       C  
ATOM   1140  C   ILE B 143      59.421  10.463  11.649  1.00 50.80           C  
ANISOU 1140  C   ILE B 143     7435   6385   5484   1044   1052   -429       C  
ATOM   1141  O   ILE B 143      59.246   9.728  12.625  1.00 51.90           O  
ANISOU 1141  O   ILE B 143     7609   6457   5655   1057    970   -405       O  
ATOM   1142  CB  ILE B 143      61.251   9.058  10.611  1.00 51.80           C  
ANISOU 1142  CB  ILE B 143     7466   6528   5687   1263   1134   -514       C  
ATOM   1143  CG1 ILE B 143      62.576   9.111   9.849  1.00 51.39           C  
ANISOU 1143  CG1 ILE B 143     7288   6573   5667   1349   1227   -553       C  
ATOM   1144  CG2 ILE B 143      60.207   8.291   9.814  1.00 50.58           C  
ANISOU 1144  CG2 ILE B 143     7452   6290   5476   1272   1146   -583       C  
ATOM   1145  CD1 ILE B 143      63.333   7.805   9.858  1.00 53.88           C  
ANISOU 1145  CD1 ILE B 143     7574   6826   6071   1501   1220   -606       C  
ATOM   1146  N   SER B 144      58.477  11.283  11.187  1.00 49.74           N  
ANISOU 1146  N   SER B 144     7348   6263   5288    957   1076   -426       N  
ATOM   1147  CA  SER B 144      57.273  11.587  11.949  1.00 48.96           C  
ANISOU 1147  CA  SER B 144     7316   6118   5168    866   1014   -401       C  
ATOM   1148  C   SER B 144      56.010  10.922  11.415  1.00 48.96           C  
ANISOU 1148  C   SER B 144     7440   6050   5114    854   1001   -434       C  
ATOM   1149  O   SER B 144      54.924  11.192  11.938  1.00 48.35           O  
ANISOU 1149  O   SER B 144     7411   5945   5017    776    959   -417       O  
ATOM   1150  CB  SER B 144      57.055  13.105  11.996  1.00 46.38           C  
ANISOU 1150  CB  SER B 144     6937   5844   4839    774   1037   -371       C  
ATOM   1151  OG  SER B 144      56.954  13.639  10.687  1.00 48.35           O  
ANISOU 1151  OG  SER B 144     7188   6131   5051    769   1108   -371       O  
ATOM   1152  N   LYS B 145      56.110  10.060  10.398  1.00 51.25           N  
ANISOU 1152  N   LYS B 145     7776   6317   5379    923   1037   -491       N  
ATOM   1153  CA  LYS B 145      54.904   9.482   9.816  1.00 49.98           C  
ANISOU 1153  CA  LYS B 145     7728   6099   5162    897   1021   -531       C  
ATOM   1154  C   LYS B 145      55.085   8.018   9.427  1.00 51.37           C  
ANISOU 1154  C   LYS B 145     7969   6193   5356    982   1016   -604       C  
ATOM   1155  O   LYS B 145      54.324   7.506   8.596  1.00 52.28           O  
ANISOU 1155  O   LYS B 145     8168   6278   5418    971   1022   -666       O  
ATOM   1156  CB  LYS B 145      54.462  10.288   8.590  1.00 47.44           C  
ANISOU 1156  CB  LYS B 145     7411   5854   4760    858   1078   -540       C  
ATOM   1157  CG  LYS B 145      52.963  10.294   8.351  1.00 47.36           C  
ANISOU 1157  CG  LYS B 145     7486   5815   4696    784   1038   -543       C  
ATOM   1158  CD  LYS B 145      52.638  10.884   6.995  1.00 47.99           C  
ANISOU 1158  CD  LYS B 145     7571   5977   4687    761   1085   -547       C  
ATOM   1159  CE  LYS B 145      51.145  10.900   6.755  1.00 47.41           C  
ANISOU 1159  CE  LYS B 145     7566   5884   4565    690   1034   -544       C  
ATOM   1160  NZ  LYS B 145      50.837  11.366   5.380  1.00 46.40           N  
ANISOU 1160  NZ  LYS B 145     7445   5848   4336    670   1067   -539       N  
ATOM   1161  N   ALA B 146      56.065   7.331   9.999  1.00 45.48           N  
ANISOU 1161  N   ALA B 146     7183   5404   4692   1066    999   -601       N  
ATOM   1162  CA  ALA B 146      56.298   5.941   9.651  1.00 47.86           C  
ANISOU 1162  CA  ALA B 146     7540   5602   5042   1159    993   -675       C  
ATOM   1163  C   ALA B 146      55.274   5.037  10.321  1.00 48.70           C  
ANISOU 1163  C   ALA B 146     7756   5574   5175   1114    905   -655       C  
ATOM   1164  O   ALA B 146      54.747   5.341  11.395  1.00 49.21           O  
ANISOU 1164  O   ALA B 146     7824   5633   5240   1035    842   -568       O  
ATOM   1165  CB  ALA B 146      57.708   5.517  10.056  1.00 50.26           C  
ANISOU 1165  CB  ALA B 146     7751   5898   5446   1275    997   -666       C  
ATOM   1166  N   SER B 147      54.982   3.922   9.663  1.00 48.50           N  
ANISOU 1166  N   SER B 147     7815   5444   5169   1157    905   -745       N  
ATOM   1167  CA  SER B 147      54.208   2.840  10.254  1.00 50.24           C  
ANISOU 1167  CA  SER B 147     8136   5509   5444   1127    822   -728       C  
ATOM   1168  C   SER B 147      55.186   1.781  10.750  1.00 52.68           C  
ANISOU 1168  C   SER B 147     8428   5696   5890   1247    788   -717       C  
ATOM   1169  O   SER B 147      55.943   1.205   9.961  1.00 53.33           O  
ANISOU 1169  O   SER B 147     8496   5742   6025   1363    839   -820       O  
ATOM   1170  CB  SER B 147      53.214   2.259   9.247  1.00 49.17           C  
ANISOU 1170  CB  SER B 147     8106   5316   5259   1087    831   -836       C  
ATOM   1171  OG  SER B 147      52.320   3.260   8.789  1.00 46.34           O  
ANISOU 1171  OG  SER B 147     7751   5076   4780    984    852   -830       O  
ATOM   1172  N   VAL B 148      55.194   1.561  12.059  1.00 48.89           N  
ANISOU 1172  N   VAL B 148     7942   5167   5467   1220    702   -590       N  
ATOM   1173  CA  VAL B 148      56.105   0.648  12.728  1.00 49.18           C  
ANISOU 1173  CA  VAL B 148     7952   5095   5640   1327    646   -535       C  
ATOM   1174  C   VAL B 148      55.388  -0.678  12.921  1.00 51.49           C  
ANISOU 1174  C   VAL B 148     8366   5184   6014   1313    575   -528       C  
ATOM   1175  O   VAL B 148      54.235  -0.712  13.379  1.00 52.34           O  
ANISOU 1175  O   VAL B 148     8550   5267   6069   1182    528   -471       O  
ATOM   1176  CB  VAL B 148      56.576   1.222  14.075  1.00 50.63           C  
ANISOU 1176  CB  VAL B 148     8051   5365   5822   1296    584   -383       C  
ATOM   1177  CG1 VAL B 148      57.634   0.325  14.703  1.00 52.98           C  
ANISOU 1177  CG1 VAL B 148     8301   5568   6261   1419    519   -313       C  
ATOM   1178  CG2 VAL B 148      57.100   2.639  13.893  1.00 49.58           C  
ANISOU 1178  CG2 VAL B 148     7807   5424   5608   1276    652   -396       C  
ATOM   1179  N   VAL B 149      56.078  -1.762  12.575  1.00 52.84           N  
ANISOU 1179  N   VAL B 149     8548   5204   6324   1447    570   -587       N  
ATOM   1180  CA  VAL B 149      55.557  -3.121  12.586  1.00 52.32           C  
ANISOU 1180  CA  VAL B 149     8598   4908   6373   1454    509   -603       C  
ATOM   1181  C   VAL B 149      56.312  -3.898  13.653  1.00 55.50           C  
ANISOU 1181  C   VAL B 149     8970   5187   6932   1538    414   -460       C  
ATOM   1182  O   VAL B 149      57.554  -3.968  13.622  1.00 57.06           O  
ANISOU 1182  O   VAL B 149     9066   5395   7220   1687    429   -469       O  
ATOM   1183  CB  VAL B 149      55.716  -3.796  11.214  1.00 52.45           C  
ANISOU 1183  CB  VAL B 149     8658   4831   6441   1549    583   -814       C  
ATOM   1184  CG1 VAL B 149      55.200  -5.227  11.256  1.00 52.05           C  
ANISOU 1184  CG1 VAL B 149     8728   4514   6534   1554    514   -839       C  
ATOM   1185  CG2 VAL B 149      55.013  -2.991  10.137  1.00 48.79           C  
ANISOU 1185  CG2 VAL B 149     8217   4517   5804   1463    668   -938       C  
ATOM   1186  N   THR B 150      55.555  -4.475  14.589  1.00 61.20           N  
ANISOU 1186  N   THR B 150     9771   5798   7682   1440    313   -320       N  
ATOM   1187  CA  THR B 150      56.070  -5.359  15.623  1.00 63.40           C  
ANISOU 1187  CA  THR B 150    10046   5935   8109   1497    202   -156       C  
ATOM   1188  C   THR B 150      55.257  -6.647  15.620  1.00 63.70           C  
ANISOU 1188  C   THR B 150    10223   5717   8264   1454    138   -143       C  
ATOM   1189  O   THR B 150      54.131  -6.690  15.119  1.00 63.49           O  
ANISOU 1189  O   THR B 150    10290   5666   8168   1334    165   -224       O  
ATOM   1190  CB  THR B 150      56.001  -4.709  17.012  1.00 64.79           C  
ANISOU 1190  CB  THR B 150    10171   6261   8185   1393    130     51       C  
ATOM   1191  OG1 THR B 150      54.690  -4.169  17.221  1.00 65.45           O  
ANISOU 1191  OG1 THR B 150    10319   6434   8114   1205    141     67       O  
ATOM   1192  CG2 THR B 150      57.025  -3.596  17.130  1.00 63.47           C  
ANISOU 1192  CG2 THR B 150     9857   6310   7949   1453    173     48       C  
ATOM   1193  N   ALA B 151      55.838  -7.698  16.192  1.00 67.47           N  
ANISOU 1193  N   ALA B 151    10707   5998   8929   1549     47    -32       N  
ATOM   1194  CA  ALA B 151      55.153  -8.983  16.302  1.00 69.44           C  
ANISOU 1194  CA  ALA B 151    11087   5973   9323   1508    -29      9       C  
ATOM   1195  C   ALA B 151      55.803  -9.857  17.368  1.00 70.42           C  
ANISOU 1195  C   ALA B 151    11195   5937   9623   1582   -158    228       C  
ATOM   1196  O   ALA B 151      56.303  -9.355  18.374  1.00 70.78           O  
ANISOU 1196  O   ALA B 151    11155   6133   9605   1575   -214    408       O  
ATOM   1197  CB  ALA B 151      55.144  -9.703  14.960  1.00 70.76           C  
ANISOU 1197  CB  ALA B 151    11317   5959   9609   1601     39   -238       C  
ATOM   1198  N   ASP B 157      55.648 -15.717  14.397  1.00120.01           N  
ANISOU 1198  N   ASP B 157    17895  10703  17000   1973   -228   -348       N  
ATOM   1199  CA  ASP B 157      55.159 -16.901  15.093  1.00121.28           C  
ANISOU 1199  CA  ASP B 157    18167  10541  17371   1908   -362   -169       C  
ATOM   1200  C   ASP B 157      53.634 -16.982  15.032  1.00119.92           C  
ANISOU 1200  C   ASP B 157    18129  10352  17082   1649   -372   -172       C  
ATOM   1201  O   ASP B 157      53.050 -18.059  15.169  1.00120.32           O  
ANISOU 1201  O   ASP B 157    18297  10103  17316   1576   -451   -125       O  
ATOM   1202  CB  ASP B 157      55.650 -16.899  16.543  1.00122.75           C  
ANISOU 1202  CB  ASP B 157    18289  10754  17594   1917   -490    190       C  
ATOM   1203  CG  ASP B 157      55.387 -15.583  17.252  1.00122.00           C  
ANISOU 1203  CG  ASP B 157    18123  11045  17188   1775   -474    338       C  
ATOM   1204  OD1 ASP B 157      55.815 -14.523  16.744  1.00120.09           O  
ANISOU 1204  OD1 ASP B 157    17783  11072  16774   1827   -367    195       O  
ATOM   1205  OD2 ASP B 157      54.781 -15.623  18.343  1.00122.80           O  
ANISOU 1205  OD2 ASP B 157    18263  11174  17220   1611   -569    602       O  
ATOM   1206  N   ASP B 158      53.001 -15.838  14.797  1.00122.21           N  
ANISOU 1206  N   ASP B 158    18395  10961  17078   1511   -293   -230       N  
ATOM   1207  CA  ASP B 158      51.549 -15.737  14.686  1.00122.35           C  
ANISOU 1207  CA  ASP B 158    18510  11019  16957   1269   -291   -246       C  
ATOM   1208  C   ASP B 158      51.207 -14.342  14.189  1.00120.38           C  
ANISOU 1208  C   ASP B 158    18195  11136  16406   1198   -182   -361       C  
ATOM   1209  O   ASP B 158      51.982 -13.399  14.377  1.00119.47           O  
ANISOU 1209  O   ASP B 158    17964  11253  16176   1288   -137   -327       O  
ATOM   1210  CB  ASP B 158      50.861 -16.015  16.024  1.00123.74           C  
ANISOU 1210  CB  ASP B 158    18730  11154  17130   1091   -408     77       C  
ATOM   1211  CG  ASP B 158      49.342 -15.920  15.955  1.00123.52           C  
ANISOU 1211  CG  ASP B 158    18786  11180  16967    835   -404     68       C  
ATOM   1212  OD1 ASP B 158      48.730 -15.922  17.040  1.00123.66           O  
ANISOU 1212  OD1 ASP B 158    18818  11242  16924    672   -474    323       O  
ATOM   1213  OD2 ASP B 158      48.761 -15.840  14.849  1.00122.72           O  
ANISOU 1213  OD2 ASP B 158    18728  11090  16810    792   -332   -186       O  
ATOM   1214  N   PHE B 159      50.045 -14.223  13.544  1.00100.59           N  
ANISOU 1214  N   PHE B 159    15761   8671  13786   1036   -146   -494       N  
ATOM   1215  CA  PHE B 159      49.658 -12.988  12.872  1.00 96.71           C  
ANISOU 1215  CA  PHE B 159    15217   8494  13035    978    -45   -628       C  
ATOM   1216  C   PHE B 159      48.724 -12.105  13.685  1.00 93.67           C  
ANISOU 1216  C   PHE B 159    14807   8338  12447    784    -62   -449       C  
ATOM   1217  O   PHE B 159      48.699 -10.886  13.468  1.00 89.86           O  
ANISOU 1217  O   PHE B 159    14245   8136  11763    771     10   -489       O  
ATOM   1218  CB  PHE B 159      48.998 -13.311  11.529  1.00 95.56           C  
ANISOU 1218  CB  PHE B 159    15150   8287  12872    933      8   -909       C  
ATOM   1219  CG  PHE B 159      49.375 -12.367  10.436  1.00 94.62           C  
ANISOU 1219  CG  PHE B 159    14963   8409  12581   1013    127  -1118       C  
ATOM   1220  CD1 PHE B 159      50.704 -12.180  10.095  1.00 94.67           C  
ANISOU 1220  CD1 PHE B 159    14886   8452  12631   1223    191  -1199       C  
ATOM   1221  CD2 PHE B 159      48.404 -11.663   9.750  1.00 93.92           C  
ANISOU 1221  CD2 PHE B 159    14885   8515  12286    875    172  -1222       C  
ATOM   1222  CE1 PHE B 159      51.056 -11.308   9.086  1.00 93.66           C  
ANISOU 1222  CE1 PHE B 159    14693   8555  12337   1283    304  -1376       C  
ATOM   1223  CE2 PHE B 159      48.748 -10.790   8.741  1.00 92.90           C  
ANISOU 1223  CE2 PHE B 159    14695   8610  11994    940    274  -1390       C  
ATOM   1224  CZ  PHE B 159      50.076 -10.611   8.410  1.00 92.90           C  
ANISOU 1224  CZ  PHE B 159    14618   8648  12032   1139    344  -1465       C  
ATOM   1225  N   ASN B 160      47.943 -12.682  14.601  1.00 82.68           N  
ANISOU 1225  N   ASN B 160    13475   6833  11105    630   -152   -256       N  
ATOM   1226  CA  ASN B 160      47.121 -11.862  15.484  1.00 81.17           C  
ANISOU 1226  CA  ASN B 160    13245   6871  10724    455   -161    -83       C  
ATOM   1227  C   ASN B 160      47.981 -11.024  16.412  1.00 80.27           C  
ANISOU 1227  C   ASN B 160    13024   6954  10523    530   -160     80       C  
ATOM   1228  O   ASN B 160      47.512  -9.994  16.922  1.00 78.97           O  
ANISOU 1228  O   ASN B 160    12797   7043  10165    427   -132    152       O  
ATOM   1229  CB  ASN B 160      46.168 -12.757  16.289  1.00 81.42           C  
ANISOU 1229  CB  ASN B 160    13361   6739  10837    272   -253     96       C  
ATOM   1230  CG  ASN B 160      45.527 -13.850  15.436  1.00 82.23           C  
ANISOU 1230  CG  ASN B 160    13579   6573  11092    215   -276    -58       C  
ATOM   1231  OD1 ASN B 160      45.348 -13.691  14.231  1.00 81.65           O  
ANISOU 1231  OD1 ASN B 160    13521   6523  10981    245   -212   -310       O  
ATOM   1232  ND2 ASN B 160      45.201 -14.978  16.067  1.00 83.75           N  
ANISOU 1232  ND2 ASN B 160    13853   6508  11458    129   -371     98       N  
ATOM   1233  N   LYS B 161      49.230 -11.421  16.632  1.00 97.84           N  
ANISOU 1233  N   LYS B 161    15215   9070  12889    709   -192    128       N  
ATOM   1234  CA  LYS B 161      50.122 -10.697  17.519  1.00 98.59           C  
ANISOU 1234  CA  LYS B 161    15201   9345  12912    781   -204    281       C  
ATOM   1235  C   LYS B 161      50.884  -9.591  16.810  1.00 97.74           C  
ANISOU 1235  C   LYS B 161    14991   9449  12696    905   -103    119       C  
ATOM   1236  O   LYS B 161      51.704  -8.910  17.439  1.00 98.75           O  
ANISOU 1236  O   LYS B 161    15018   9738  12766    970   -106    217       O  
ATOM   1237  CB  LYS B 161      51.100 -11.683  18.175  1.00 99.73           C  
ANISOU 1237  CB  LYS B 161    15346   9274  13271    911   -304    440       C  
ATOM   1238  CG  LYS B 161      50.457 -12.522  19.292  1.00101.87           C  
ANISOU 1238  CG  LYS B 161    15693   9407  13607    764   -421    700       C  
ATOM   1239  CD  LYS B 161      50.608 -14.007  19.003  1.00104.83           C  
ANISOU 1239  CD  LYS B 161    16165   9397  14268    836   -493    699       C  
ATOM   1240  CE  LYS B 161      52.096 -14.404  18.906  1.00106.20           C  
ANISOU 1240  CE  LYS B 161    16274   9443  14636   1092   -522    693       C  
ATOM   1241  NZ  LYS B 161      52.284 -15.885  18.834  1.00107.72           N  
ANISOU 1241  NZ  LYS B 161    16554   9236  15137   1169   -610    733       N  
ATOM   1242  N   LEU B 162      50.649  -9.406  15.512  1.00 70.72           N  
ANISOU 1242  N   LEU B 162    11591   6038   9243    932    -15   -122       N  
ATOM   1243  CA  LEU B 162      51.315  -8.350  14.767  1.00 67.65           C  
ANISOU 1243  CA  LEU B 162    11108   5854   8743   1033     86   -266       C  
ATOM   1244  C   LEU B 162      50.576  -7.025  14.935  1.00 65.71           C  
ANISOU 1244  C   LEU B 162    10816   5883   8270    895    133   -245       C  
ATOM   1245  O   LEU B 162      49.348  -6.965  14.848  1.00 66.82           O  
ANISOU 1245  O   LEU B 162    11014   6045   8331    739    130   -256       O  
ATOM   1246  CB  LEU B 162      51.421  -8.723  13.287  1.00 67.25           C  
ANISOU 1246  CB  LEU B 162    11097   5715   8742   1120    161   -529       C  
ATOM   1247  CG  LEU B 162      52.276  -7.844  12.374  1.00 66.85           C  
ANISOU 1247  CG  LEU B 162    10952   5847   8603   1244    272   -686       C  
ATOM   1248  CD1 LEU B 162      53.001  -8.705  11.349  1.00 66.79           C  
ANISOU 1248  CD1 LEU B 162    10964   5671   8741   1408    316   -888       C  
ATOM   1249  CD2 LEU B 162      51.413  -6.804  11.687  1.00 67.37           C  
ANISOU 1249  CD2 LEU B 162    11014   6126   8456   1124    341   -778       C  
ATOM   1250  N   ASN B 163      51.334  -5.953  15.175  1.00 47.20           N  
ANISOU 1250  N   ASN B 163     8359   3743   5832    955    175   -216       N  
ATOM   1251  CA  ASN B 163      50.750  -4.647  15.438  1.00 47.25           C  
ANISOU 1251  CA  ASN B 163     8311   3993   5649    840    215   -189       C  
ATOM   1252  C   ASN B 163      51.481  -3.583  14.636  1.00 45.44           C  
ANISOU 1252  C   ASN B 163     7991   3932   5342    933    310   -311       C  
ATOM   1253  O   ASN B 163      52.702  -3.659  14.439  1.00 45.66           O  
ANISOU 1253  O   ASN B 163     7955   3947   5445   1083    330   -340       O  
ATOM   1254  CB  ASN B 163      50.790  -4.309  16.936  1.00 49.45           C  
ANISOU 1254  CB  ASN B 163     8543   4369   5878    767    152     20       C  
ATOM   1255  N   VAL B 164      50.715  -2.597  14.169  1.00 49.55           N  
ANISOU 1255  N   VAL B 164     8499   4610   5719    841    367   -376       N  
ATOM   1256  CA  VAL B 164      51.226  -1.480  13.385  1.00 47.54           C  
ANISOU 1256  CA  VAL B 164     8163   4523   5377    897    456   -471       C  
ATOM   1257  C   VAL B 164      50.784  -0.182  14.048  1.00 47.03           C  
ANISOU 1257  C   VAL B 164     8033   4648   5188    795    468   -392       C  
ATOM   1258  O   VAL B 164      49.587   0.022  14.302  1.00 46.66           O  
ANISOU 1258  O   VAL B 164     8022   4632   5074    663    451   -365       O  
ATOM   1259  CB  VAL B 164      50.742  -1.528  11.923  1.00 46.96           C  
ANISOU 1259  CB  VAL B 164     8139   4447   5257    898    518   -646       C  
ATOM   1260  CG1 VAL B 164      51.410  -0.429  11.116  1.00 47.20           C  
ANISOU 1260  CG1 VAL B 164     8082   4649   5201    961    609   -720       C  
ATOM   1261  CG2 VAL B 164      51.024  -2.888  11.307  1.00 47.90           C  
ANISOU 1261  CG2 VAL B 164     8335   4362   5503    982    506   -751       C  
ATOM   1262  N   GLY B 165      51.754   0.692  14.317  1.00 50.04           N  
ANISOU 1262  N   GLY B 165     8312   5153   5547    856    498   -363       N  
ATOM   1263  CA  GLY B 165      51.467   1.967  14.943  1.00 49.52           C  
ANISOU 1263  CA  GLY B 165     8178   5255   5382    771    512   -308       C  
ATOM   1264  C   GLY B 165      52.416   3.041  14.449  1.00 48.49           C  
ANISOU 1264  C   GLY B 165     7948   5252   5225    840    582   -354       C  
ATOM   1265  O   GLY B 165      53.474   2.751  13.902  1.00 49.21           O  
ANISOU 1265  O   GLY B 165     8004   5319   5376    960    611   -400       O  
ATOM   1266  N   THR B 166      52.022   4.294  14.646  1.00 55.79           N  
ANISOU 1266  N   THR B 166     8820   6310   6068    763    611   -344       N  
ATOM   1267  CA  THR B 166      52.875   5.425  14.295  1.00 56.52           C  
ANISOU 1267  CA  THR B 166     8814   6520   6141    805    672   -369       C  
ATOM   1268  C   THR B 166      53.582   5.920  15.551  1.00 56.06           C  
ANISOU 1268  C   THR B 166     8672   6535   6092    793    635   -285       C  
ATOM   1269  O   THR B 166      52.929   6.304  16.526  1.00 56.23           O  
ANISOU 1269  O   THR B 166     8693   6602   6068    695    601   -234       O  
ATOM   1270  CB  THR B 166      52.080   6.558  13.644  1.00 56.55           C  
ANISOU 1270  CB  THR B 166     8807   6611   6070    735    724   -411       C  
ATOM   1271  OG1 THR B 166      51.185   6.021  12.662  1.00 57.29           O  
ANISOU 1271  OG1 THR B 166     8985   6647   6136    718    734   -474       O  
ATOM   1272  CG2 THR B 166      53.024   7.552  12.969  1.00 56.52           C  
ANISOU 1272  CG2 THR B 166     8714   6699   6060    786    794   -437       C  
ATOM   1273  N   TYR B 167      54.912   5.895  15.527  1.00 45.32           N  
ANISOU 1273  N   TYR B 167     7235   5197   4787    890    644   -278       N  
ATOM   1274  CA  TYR B 167      55.729   6.387  16.626  1.00 46.28           C  
ANISOU 1274  CA  TYR B 167     7264   5405   4917    882    604   -208       C  
ATOM   1275  C   TYR B 167      56.805   7.304  16.068  1.00 45.96           C  
ANISOU 1275  C   TYR B 167     7112   5457   4893    933    669   -248       C  
ATOM   1276  O   TYR B 167      57.422   6.996  15.043  1.00 46.52           O  
ANISOU 1276  O   TYR B 167     7166   5505   5005   1029    723   -303       O  
ATOM   1277  CB  TYR B 167      56.370   5.235  17.411  1.00 50.26           C  
ANISOU 1277  CB  TYR B 167     7769   5836   5490    947    519   -124       C  
ATOM   1278  N   ARG B 168      57.017   8.435  16.736  1.00 50.40           N  
ANISOU 1278  N   ARG B 168     7597   6129   5425    863    667   -227       N  
ATOM   1279  CA  ARG B 168      58.041   9.369  16.293  1.00 50.13           C  
ANISOU 1279  CA  ARG B 168     7450   6183   5415    890    724   -254       C  
ATOM   1280  C   ARG B 168      59.418   8.731  16.415  1.00 51.34           C  
ANISOU 1280  C   ARG B 168     7519   6344   5644   1002    701   -226       C  
ATOM   1281  O   ARG B 168      59.691   7.969  17.347  1.00 55.12           O  
ANISOU 1281  O   ARG B 168     7995   6797   6149   1027    614   -160       O  
ATOM   1282  CB  ARG B 168      57.972  10.665  17.102  1.00 49.86           C  
ANISOU 1282  CB  ARG B 168     7352   6244   5348    783    715   -245       C  
ATOM   1283  CG  ARG B 168      58.395  10.526  18.550  1.00 50.91           C  
ANISOU 1283  CG  ARG B 168     7440   6433   5472    750    626   -187       C  
ATOM   1284  CD  ARG B 168      58.083  11.785  19.330  1.00 51.63           C  
ANISOU 1284  CD  ARG B 168     7488   6610   5518    630    624   -212       C  
ATOM   1285  NE  ARG B 168      58.876  11.876  20.551  1.00 54.23           N  
ANISOU 1285  NE  ARG B 168     7737   7033   5834    601    549   -172       N  
ATOM   1286  CZ  ARG B 168      58.447  12.432  21.678  1.00 55.13           C  
ANISOU 1286  CZ  ARG B 168     7844   7223   5880    492    510   -183       C  
ATOM   1287  NH1 ARG B 168      57.227  12.948  21.740  1.00 53.23           N  
ANISOU 1287  NH1 ARG B 168     7665   6966   5594    412    546   -236       N  
ATOM   1288  NH2 ARG B 168      59.235  12.470  22.743  1.00 57.91           N  
ANISOU 1288  NH2 ARG B 168     8120   7678   6206    464    435   -148       N  
ATOM   1289  N   ILE B 169      60.287   9.039  15.458  1.00 47.55           N  
ANISOU 1289  N   ILE B 169     6962   5906   5199   1069    778   -271       N  
ATOM   1290  CA  ILE B 169      61.570   8.367  15.312  1.00 50.21           C  
ANISOU 1290  CA  ILE B 169     7208   6247   5620   1196    777   -266       C  
ATOM   1291  C   ILE B 169      62.637   9.435  15.107  1.00 52.02           C  
ANISOU 1291  C   ILE B 169     7291   6607   5869   1186    831   -273       C  
ATOM   1292  O   ILE B 169      62.703  10.058  14.039  1.00 52.26           O  
ANISOU 1292  O   ILE B 169     7301   6680   5876   1176    930   -323       O  
ATOM   1293  CB  ILE B 169      61.553   7.362  14.152  1.00 50.55           C  
ANISOU 1293  CB  ILE B 169     7310   6200   5696   1308    835   -339       C  
ATOM   1294  CG1 ILE B 169      60.737   6.127  14.541  1.00 52.47           C  
ANISOU 1294  CG1 ILE B 169     7682   6296   5959   1326    760   -319       C  
ATOM   1295  CG2 ILE B 169      62.950   6.957  13.760  1.00 50.22           C  
ANISOU 1295  CG2 ILE B 169     7145   6191   5745   1443    871   -363       C  
ATOM   1296  CD1 ILE B 169      60.039   5.466  13.378  1.00 52.89           C  
ANISOU 1296  CD1 ILE B 169     7844   6255   5996   1360    817   -414       C  
ATOM   1297  N   GLN B 170      63.463   9.657  16.129  1.00 46.62           N  
ANISOU 1297  N   GLN B 170     6500   5994   5221   1176    762   -216       N  
ATOM   1298  CA  GLN B 170      64.547  10.627  16.053  1.00 47.58           C  
ANISOU 1298  CA  GLN B 170     6467   6239   5372   1156    800   -219       C  
ATOM   1299  C   GLN B 170      65.788   9.971  15.468  1.00 49.66           C  
ANISOU 1299  C   GLN B 170     6617   6527   5724   1299    838   -233       C  
ATOM   1300  O   GLN B 170      66.228   8.924  15.950  1.00 48.69           O  
ANISOU 1300  O   GLN B 170     6474   6358   5666   1401    767   -197       O  
ATOM   1301  CB  GLN B 170      64.874  11.201  17.432  1.00 48.94           C  
ANISOU 1301  CB  GLN B 170     6567   6492   5538   1069    704   -165       C  
ATOM   1302  CG  GLN B 170      66.042  12.180  17.413  1.00 51.37           C  
ANISOU 1302  CG  GLN B 170     6705   6925   5889   1036    732   -171       C  
ATOM   1303  CD  GLN B 170      66.364  12.745  18.782  1.00 54.32           C  
ANISOU 1303  CD  GLN B 170     7006   7386   6247    940    630   -136       C  
ATOM   1304  OE1 GLN B 170      65.630  12.525  19.744  1.00 54.37           O  
ANISOU 1304  OE1 GLN B 170     7095   7373   6190    885    548   -110       O  
ATOM   1305  NE2 GLN B 170      67.469  13.476  18.876  1.00 56.23           N  
ANISOU 1305  NE2 GLN B 170     7089   7738   6538    910    636   -138       N  
ATOM   1306  N   VAL B 171      66.355  10.596  14.442  1.00 55.26           N  
ANISOU 1306  N   VAL B 171     7247   7312   6440   1305    951   -278       N  
ATOM   1307  CA  VAL B 171      67.583  10.100  13.831  1.00 55.61           C  
ANISOU 1307  CA  VAL B 171     7158   7407   6562   1436   1008   -306       C  
ATOM   1308  C   VAL B 171      68.753  10.451  14.743  1.00 57.18           C  
ANISOU 1308  C   VAL B 171     7183   7712   6832   1431    942   -248       C  
ATOM   1309  O   VAL B 171      69.021  11.628  15.003  1.00 56.34           O  
ANISOU 1309  O   VAL B 171     6999   7701   6708   1312    949   -229       O  
ATOM   1310  CB  VAL B 171      67.776  10.685  12.424  1.00 54.10           C  
ANISOU 1310  CB  VAL B 171     6935   7287   6333   1426   1159   -367       C  
ATOM   1311  CG1 VAL B 171      69.061  10.171  11.809  1.00 55.27           C  
ANISOU 1311  CG1 VAL B 171     6933   7508   6558   1561   1232   -408       C  
ATOM   1312  CG2 VAL B 171      66.590  10.335  11.542  1.00 52.46           C  
ANISOU 1312  CG2 VAL B 171     6900   6991   6042   1423   1209   -422       C  
ATOM   1313  N   LYS B 172      69.441   9.425  15.242  1.00 59.22           N  
ANISOU 1313  N   LYS B 172     7375   7946   7179   1559    869   -218       N  
ATOM   1314  CA  LYS B 172      70.586   9.592  16.129  1.00 63.08           C  
ANISOU 1314  CA  LYS B 172     7687   8541   7740   1572    787   -155       C  
ATOM   1315  C   LYS B 172      71.916   9.402  15.416  1.00 65.72           C  
ANISOU 1315  C   LYS B 172     7833   8962   8174   1693    866   -189       C  
ATOM   1316  O   LYS B 172      72.857  10.164  15.653  1.00 67.61           O  
ANISOU 1316  O   LYS B 172     7901   9342   8445   1644    867   -167       O  
ATOM   1317  CB  LYS B 172      70.500   8.606  17.299  1.00 63.20           C  
ANISOU 1317  CB  LYS B 172     7736   8486   7791   1630    630    -69       C  
ATOM   1318  CG  LYS B 172      69.215   8.694  18.102  1.00 62.61           C  
ANISOU 1318  CG  LYS B 172     7834   8342   7611   1509    551    -29       C  
ATOM   1319  CD  LYS B 172      69.072  10.047  18.774  1.00 63.36           C  
ANISOU 1319  CD  LYS B 172     7898   8554   7624   1330    528    -23       C  
ATOM   1320  CE  LYS B 172      68.076   9.984  19.919  1.00 63.79           C  
ANISOU 1320  CE  LYS B 172     8075   8577   7584   1228    421     29       C  
ATOM   1321  NZ  LYS B 172      68.601   9.193  21.066  1.00 67.23           N  
ANISOU 1321  NZ  LYS B 172     8457   9041   8045   1276    273    137       N  
ATOM   1322  N   ASP B 173      72.015   8.393  14.556  1.00 75.63           N  
ANISOU 1322  N   ASP B 173     9110  10140   9483   1849    936   -253       N  
ATOM   1323  CA  ASP B 173      73.208   8.144  13.764  1.00 76.09           C  
ANISOU 1323  CA  ASP B 173     8992  10284   9634   1978   1035   -310       C  
ATOM   1324  C   ASP B 173      72.773   7.675  12.384  1.00 73.20           C  
ANISOU 1324  C   ASP B 173     8721   9859   9232   2050   1180   -430       C  
ATOM   1325  O   ASP B 173      71.606   7.339  12.162  1.00 71.89           O  
ANISOU 1325  O   ASP B 173     8752   9568   8995   2022   1176   -459       O  
ATOM   1326  CB  ASP B 173      74.126   7.114  14.427  1.00 78.75           C  
ANISOU 1326  CB  ASP B 173     9203  10595  10124   2145    935   -265       C  
ATOM   1327  CG  ASP B 173      75.591   7.366  14.131  1.00 80.43           C  
ANISOU 1327  CG  ASP B 173     9156  10970  10433   2218    996   -282       C  
ATOM   1328  OD1 ASP B 173      75.892   8.280  13.333  1.00 79.87           O  
ANISOU 1328  OD1 ASP B 173     9012  11029  10307   2137   1129   -333       O  
ATOM   1329  OD2 ASP B 173      76.441   6.650  14.698  1.00 82.40           O  
ANISOU 1329  OD2 ASP B 173     9270  11221  10818   2353    908   -235       O  
ATOM   1330  N   ARG B 174      73.732   7.643  11.452  1.00 68.86           N  
ANISOU 1330  N   ARG B 174     8021   9416   8727   2139   1311   -507       N  
ATOM   1331  CA  ARG B 174      73.432   7.274  10.072  1.00 66.02           C  
ANISOU 1331  CA  ARG B 174     7731   9043   8311   2198   1464   -636       C  
ATOM   1332  C   ARG B 174      72.690   5.947   9.965  1.00 67.13           C  
ANISOU 1332  C   ARG B 174     8036   8983   8487   2318   1425   -703       C  
ATOM   1333  O   ARG B 174      72.001   5.713   8.966  1.00 66.70           O  
ANISOU 1333  O   ARG B 174     8108   8890   8346   2317   1519   -806       O  
ATOM   1334  CB  ARG B 174      74.725   7.223   9.247  1.00 67.09           C  
ANISOU 1334  CB  ARG B 174     7652   9330   8509   2305   1602   -714       C  
ATOM   1335  CG  ARG B 174      75.694   6.115   9.632  1.00 70.43           C  
ANISOU 1335  CG  ARG B 174     7933   9709   9119   2515   1556   -738       C  
ATOM   1336  CD  ARG B 174      77.105   6.426   9.142  1.00 72.40           C  
ANISOU 1336  CD  ARG B 174     7916  10158   9435   2578   1671   -776       C  
ATOM   1337  NE  ARG B 174      77.184   6.501   7.685  1.00 73.28           N  
ANISOU 1337  NE  ARG B 174     8017  10370   9456   2595   1875   -913       N  
ATOM   1338  CZ  ARG B 174      77.807   5.607   6.922  1.00 76.09           C  
ANISOU 1338  CZ  ARG B 174     8281  10740   9891   2781   1987  -1057       C  
ATOM   1339  NH1 ARG B 174      78.409   4.563   7.476  1.00 78.19           N  
ANISOU 1339  NH1 ARG B 174     8454  10903  10351   2977   1909  -1075       N  
ATOM   1340  NH2 ARG B 174      77.830   5.756   5.604  1.00 75.73           N  
ANISOU 1340  NH2 ARG B 174     8232  10815   9729   2773   2177  -1183       N  
ATOM   1341  N   ASP B 175      72.800   5.078  10.973  1.00 69.21           N  
ANISOU 1341  N   ASP B 175     8302   9118   8875   2412   1283   -641       N  
ATOM   1342  CA  ASP B 175      72.075   3.812  10.993  1.00 69.46           C  
ANISOU 1342  CA  ASP B 175     8495   8935   8962   2511   1228   -683       C  
ATOM   1343  C   ASP B 175      71.428   3.557  12.350  1.00 70.38           C  
ANISOU 1343  C   ASP B 175     8715   8930   9097   2451   1043   -539       C  
ATOM   1344  O   ASP B 175      71.177   2.406  12.714  1.00 69.41           O  
ANISOU 1344  O   ASP B 175     8670   8627   9077   2554    959   -524       O  
ATOM   1345  CB  ASP B 175      72.992   2.651  10.614  1.00 71.14           C  
ANISOU 1345  CB  ASP B 175     8597   9081   9350   2741   1265   -775       C  
ATOM   1346  CG  ASP B 175      74.340   2.716  11.310  1.00 73.59           C  
ANISOU 1346  CG  ASP B 175     8669   9492   9800   2830   1208   -693       C  
ATOM   1347  OD1 ASP B 175      74.443   3.404  12.348  1.00 75.62           O  
ANISOU 1347  OD1 ASP B 175     8879   9822  10031   2718   1094   -547       O  
ATOM   1348  OD2 ASP B 175      75.295   2.079  10.819  1.00 74.69           O  
ANISOU 1348  OD2 ASP B 175     8660   9642  10076   3011   1277   -782       O  
ATOM   1349  N   ARG B 176      71.149   4.612  13.112  1.00 68.07           N  
ANISOU 1349  N   ARG B 176     8423   8733   8707   2282    981   -434       N  
ATOM   1350  CA  ARG B 176      70.563   4.453  14.436  1.00 67.95           C  
ANISOU 1350  CA  ARG B 176     8493   8642   8682   2210    814   -301       C  
ATOM   1351  C   ARG B 176      69.498   5.511  14.666  1.00 66.34           C  
ANISOU 1351  C   ARG B 176     8408   8482   8315   2005    812   -275       C  
ATOM   1352  O   ARG B 176      69.695   6.680  14.325  1.00 65.18           O  
ANISOU 1352  O   ARG B 176     8195   8474   8096   1904    888   -296       O  
ATOM   1353  CB  ARG B 176      71.623   4.558  15.536  1.00 71.11           C  
ANISOU 1353  CB  ARG B 176     8717   9134   9166   2240    697   -183       C  
ATOM   1354  CG  ARG B 176      72.120   3.227  16.061  1.00 74.13           C  
ANISOU 1354  CG  ARG B 176     9062   9390   9715   2415    589   -121       C  
ATOM   1355  CD  ARG B 176      72.942   3.430  17.326  1.00 76.76           C  
ANISOU 1355  CD  ARG B 176     9244   9829  10092   2404    440     27       C  
ATOM   1356  NE  ARG B 176      74.001   4.418  17.141  1.00 77.75           N  
ANISOU 1356  NE  ARG B 176     9161  10164  10217   2375    500      2       N  
ATOM   1357  CZ  ARG B 176      74.004   5.626  17.699  1.00 77.82           C  
ANISOU 1357  CZ  ARG B 176     9127  10326  10113   2197    474     43       C  
ATOM   1358  NH1 ARG B 176      72.999   5.999  18.479  1.00 77.08           N  
ANISOU 1358  NH1 ARG B 176     9183  10211   9895   2042    395    102       N  
ATOM   1359  NH2 ARG B 176      75.009   6.460  17.475  1.00 78.85           N  
ANISOU 1359  NH2 ARG B 176     9063  10633  10264   2171    530     18       N  
ATOM   1360  N   VAL B 177      68.384   5.106  15.278  1.00 57.10           N  
ANISOU 1360  N   VAL B 177     7405   7191   7098   1943    724   -224       N  
ATOM   1361  CA  VAL B 177      67.280   6.019  15.543  1.00 55.17           C  
ANISOU 1361  CA  VAL B 177     7274   6976   6712   1761    720   -207       C  
ATOM   1362  C   VAL B 177      66.806   5.859  16.984  1.00 56.44           C  
ANISOU 1362  C   VAL B 177     7489   7111   6846   1683    570    -85       C  
ATOM   1363  O   VAL B 177      67.164   4.913  17.681  1.00 58.25           O  
ANISOU 1363  O   VAL B 177     7700   7273   7158   1769    466     -4       O  
ATOM   1364  CB  VAL B 177      66.107   5.810  14.566  1.00 52.29           C  
ANISOU 1364  CB  VAL B 177     7077   6513   6276   1733    800   -296       C  
ATOM   1365  CG1 VAL B 177      66.501   6.233  13.160  1.00 50.36           C  
ANISOU 1365  CG1 VAL B 177     6780   6344   6009   1768    953   -408       C  
ATOM   1366  CG2 VAL B 177      65.640   4.359  14.590  1.00 53.97           C  
ANISOU 1366  CG2 VAL B 177     7406   6539   6560   1830    746   -302       C  
ATOM   1367  N   GLY B 178      65.984   6.809  17.425  1.00 54.99           N  
ANISOU 1367  N   GLY B 178     7367   6983   6543   1519    561    -72       N  
ATOM   1368  CA  GLY B 178      65.368   6.733  18.737  1.00 56.27           C  
ANISOU 1368  CA  GLY B 178     7592   7141   6646   1424    439     24       C  
ATOM   1369  C   GLY B 178      63.892   6.411  18.627  1.00 54.04           C  
ANISOU 1369  C   GLY B 178     7494   6746   6291   1355    446      9       C  
ATOM   1370  O   GLY B 178      63.282   6.677  17.590  1.00 52.67           O  
ANISOU 1370  O   GLY B 178     7389   6537   6087   1340    546    -82       O  
ATOM   1371  N   ILE B 179      63.302   5.837  19.674  1.00 53.47           N  
ANISOU 1371  N   ILE B 179     7498   6631   6188   1307    339    104       N  
ATOM   1372  CA  ILE B 179      61.902   5.430  19.615  1.00 52.08           C  
ANISOU 1372  CA  ILE B 179     7486   6348   5952   1239    342     98       C  
ATOM   1373  C   ILE B 179      61.333   5.377  21.028  1.00 54.42           C  
ANISOU 1373  C   ILE B 179     7823   6688   6164   1124    235    208       C  
ATOM   1374  O   ILE B 179      62.058   5.133  22.008  1.00 55.15           O  
ANISOU 1374  O   ILE B 179     7843   6842   6270   1139    134    313       O  
ATOM   1375  CB  ILE B 179      61.746   4.078  18.866  1.00 51.84           C  
ANISOU 1375  CB  ILE B 179     7540   6133   6021   1360    350     79       C  
ATOM   1376  CG1 ILE B 179      60.315   3.913  18.338  1.00 51.80           C  
ANISOU 1376  CG1 ILE B 179     7690   6036   5954   1283    394     22       C  
ATOM   1377  CG2 ILE B 179      62.147   2.913  19.753  1.00 53.64           C  
ANISOU 1377  CG2 ILE B 179     7769   6275   6336   1431    224    211       C  
ATOM   1378  CD1 ILE B 179      60.174   2.815  17.296  1.00 51.96           C  
ANISOU 1378  CD1 ILE B 179     7788   5889   6065   1391    431    -51       C  
ATOM   1379  N   GLN B 180      60.023   5.632  21.124  1.00 69.68           N  
ANISOU 1379  N   GLN B 180     9865   8605   8003   1006    259    184       N  
ATOM   1380  CA  GLN B 180      59.255   5.651  22.368  1.00 70.48           C  
ANISOU 1380  CA  GLN B 180    10017   8764   8000    877    185    266       C  
ATOM   1381  C   GLN B 180      58.706   4.250  22.603  1.00 73.41           C  
ANISOU 1381  C   GLN B 180    10495   8989   8407    900    117    365       C  
ATOM   1382  O   GLN B 180      57.586   3.923  22.207  1.00 72.09           O  
ANISOU 1382  O   GLN B 180    10440   8730   8220    852    152    334       O  
ATOM   1383  CB  GLN B 180      58.122   6.669  22.284  1.00 67.68           C  
ANISOU 1383  CB  GLN B 180     9707   8466   7542    747    257    179       C  
ATOM   1384  CG  GLN B 180      58.556   8.110  22.121  1.00 64.96           C  
ANISOU 1384  CG  GLN B 180     9265   8244   7174    707    319     88       C  
ATOM   1385  CD  GLN B 180      57.625   9.080  22.826  1.00 62.18           C  
ANISOU 1385  CD  GLN B 180     8928   7985   6713    560    335     45       C  
ATOM   1386  OE1 GLN B 180      58.053   9.866  23.668  1.00 62.22           O  
ANISOU 1386  OE1 GLN B 180     8854   8119   6668    493    308     35       O  
ATOM   1387  NE2 GLN B 180      56.343   9.035  22.474  1.00 60.83           N  
ANISOU 1387  NE2 GLN B 180     8852   7753   6509    510    380      8       N  
ATOM   1388  N   ALA B 181      59.503   3.412  23.270  1.00 95.88           N  
ANISOU 1388  N   ALA B 181    13305  11811  11316    970     12    493       N  
ATOM   1389  CA  ALA B 181      59.095   2.030  23.496  1.00 99.18           C  
ANISOU 1389  CA  ALA B 181    13821  12064  11797    999    -62    606       C  
ATOM   1390  C   ALA B 181      57.906   1.934  24.443  1.00 98.71           C  
ANISOU 1390  C   ALA B 181    13852  12043  11608    834   -104    691       C  
ATOM   1391  O   ALA B 181      57.140   0.967  24.370  1.00 99.79           O  
ANISOU 1391  O   ALA B 181    14100  12032  11782    816   -127    747       O  
ATOM   1392  CB  ALA B 181      60.271   1.220  24.039  1.00101.99           C  
ANISOU 1392  CB  ALA B 181    14103  12387  12262   1117   -176    743       C  
ATOM   1393  N   LEU B 182      57.738   2.911  25.338  1.00 88.60           N  
ANISOU 1393  N   LEU B 182    12523  10962  10178    709   -110    696       N  
ATOM   1394  CA  LEU B 182      56.587   2.891  26.236  1.00 85.84           C  
ANISOU 1394  CA  LEU B 182    12247  10679   9691    547   -132    760       C  
ATOM   1395  C   LEU B 182      55.288   3.140  25.482  1.00 83.76           C  
ANISOU 1395  C   LEU B 182    12070  10351   9402    481    -29    641       C  
ATOM   1396  O   LEU B 182      54.243   2.594  25.854  1.00 82.63           O  
ANISOU 1396  O   LEU B 182    12014  10172   9210    385    -43    704       O  
ATOM   1397  CB  LEU B 182      56.768   3.924  27.347  1.00 83.85           C  
ANISOU 1397  CB  LEU B 182    11912  10666   9280    433   -154    761       C  
ATOM   1398  CG  LEU B 182      55.630   4.079  28.359  1.00 80.98           C  
ANISOU 1398  CG  LEU B 182    11601  10421   8746    257   -159    802       C  
ATOM   1399  CD1 LEU B 182      55.540   2.857  29.262  1.00 82.39           C  
ANISOU 1399  CD1 LEU B 182    11833  10572   8898    221   -277   1020       C  
ATOM   1400  CD2 LEU B 182      55.814   5.345  29.181  1.00 78.81           C  
ANISOU 1400  CD2 LEU B 182    11236  10380   8327    157   -145    725       C  
ATOM   1401  N   ALA B 183      55.330   3.953  24.425  1.00 93.31           N  
ANISOU 1401  N   ALA B 183    13252  11556  10647    527     72    482       N  
ATOM   1402  CA  ALA B 183      54.166   4.129  23.566  1.00 93.27           C  
ANISOU 1402  CA  ALA B 183    13322  11482  10635    485    159    377       C  
ATOM   1403  C   ALA B 183      53.847   2.880  22.756  1.00 96.64           C  
ANISOU 1403  C   ALA B 183    13847  11703  11170    552    150    392       C  
ATOM   1404  O   ALA B 183      52.749   2.788  22.195  1.00 95.94           O  
ANISOU 1404  O   ALA B 183    13831  11554  11067    496    197    332       O  
ATOM   1405  CB  ALA B 183      54.383   5.316  22.625  1.00 90.69           C  
ANISOU 1405  CB  ALA B 183    12935  11204  10318    520    257    226       C  
ATOM   1406  N   MET B 184      54.773   1.925  22.687  1.00104.15           N  
ANISOU 1406  N   MET B 184    14794  12542  12236    670     87    464       N  
ATOM   1407  CA  MET B 184      54.575   0.678  21.951  1.00105.18           C  
ANISOU 1407  CA  MET B 184    15016  12455  12492    744     74    465       C  
ATOM   1408  C   MET B 184      54.091  -0.405  22.914  1.00106.26           C  
ANISOU 1408  C   MET B 184    15228  12507  12638    674    -27    638       C  
ATOM   1409  O   MET B 184      54.785  -1.376  23.218  1.00107.08           O  
ANISOU 1409  O   MET B 184    15337  12495  12854    759   -113    752       O  
ATOM   1410  CB  MET B 184      55.869   0.272  21.255  1.00105.82           C  
ANISOU 1410  CB  MET B 184    15042  12450  12716    927     75    428       C  
ATOM   1411  CG  MET B 184      55.685  -0.484  19.957  1.00105.88           C  
ANISOU 1411  CG  MET B 184    15122  12271  12835   1016    126    313       C  
ATOM   1412  SD  MET B 184      57.254  -0.610  19.082  1.00106.66           S  
ANISOU 1412  SD  MET B 184    15120  12335  13069   1227    165    225       S  
ATOM   1413  CE  MET B 184      57.958   0.997  19.442  1.00105.45           C  
ANISOU 1413  CE  MET B 184    14821  12442  12802   1193    206    212       C  
ATOM   1414  N   HIS B 185      52.854  -0.218  23.382  1.00120.23           N  
ANISOU 1414  N   HIS B 185    17052  14337  14295    514    -15    660       N  
ATOM   1415  CA  HIS B 185      52.306  -1.047  24.451  1.00122.28           C  
ANISOU 1415  CA  HIS B 185    17371  14569  14522    407   -102    840       C  
ATOM   1416  C   HIS B 185      52.301  -2.535  24.115  1.00125.54           C  
ANISOU 1416  C   HIS B 185    17877  14723  15100    468   -166    919       C  
ATOM   1417  O   HIS B 185      52.198  -3.361  25.028  1.00126.53           O  
ANISOU 1417  O   HIS B 185    18041  14799  15237    411   -261   1108       O  
ATOM   1418  CB  HIS B 185      50.883  -0.589  24.780  1.00120.32           C  
ANISOU 1418  CB  HIS B 185    17158  14425  14135    229    -52    816       C  
ATOM   1419  N   ASP B 186      52.433  -2.898  22.838  1.00125.04           N  
ANISOU 1419  N   ASP B 186    17849  14495  15167    579   -117    779       N  
ATOM   1420  CA  ASP B 186      52.200  -4.279  22.428  1.00127.04           C  
ANISOU 1420  CA  ASP B 186    18204  14484  15580    615   -164    814       C  
ATOM   1421  C   ASP B 186      53.375  -5.203  22.732  1.00126.63           C  
ANISOU 1421  C   ASP B 186    18133  14287  15694    762   -260    934       C  
ATOM   1422  O   ASP B 186      53.168  -6.405  22.930  1.00128.92           O  
ANISOU 1422  O   ASP B 186    18505  14366  16111    759   -337   1046       O  
ATOM   1423  CB  ASP B 186      51.873  -4.330  20.934  1.00128.76           C  
ANISOU 1423  CB  ASP B 186    18468  14592  15863    674    -76    598       C  
ATOM   1424  N   ILE B 187      54.603  -4.683  22.771  1.00 89.92           N  
ANISOU 1424  N   ILE B 187    13371   9736  11059    889   -260    918       N  
ATOM   1425  CA  ILE B 187      55.787  -5.521  22.909  1.00 85.26           C  
ANISOU 1425  CA  ILE B 187    12740   9007  10647   1056   -344   1009       C  
ATOM   1426  C   ILE B 187      56.520  -5.280  24.223  1.00 81.13           C  
ANISOU 1426  C   ILE B 187    12126   8641  10059   1043   -447   1210       C  
ATOM   1427  O   ILE B 187      57.655  -5.735  24.384  1.00 80.99           O  
ANISOU 1427  O   ILE B 187    12037   8561  10174   1192   -519   1286       O  
ATOM   1428  CB  ILE B 187      56.742  -5.336  21.713  1.00 83.52           C  
ANISOU 1428  CB  ILE B 187    12451   8745  10537   1244   -263    816       C  
ATOM   1429  N   ALA B 188      55.882  -4.590  25.175  1.00 84.00           N  
ANISOU 1429  N   ALA B 188    12486   9213  10219    867   -458   1292       N  
ATOM   1430  CA  ALA B 188      56.531  -4.262  26.443  1.00 84.00           C  
ANISOU 1430  CA  ALA B 188    12397   9401  10117    833   -553   1465       C  
ATOM   1431  C   ALA B 188      57.183  -5.487  27.076  1.00 84.81           C  
ANISOU 1431  C   ALA B 188    12506   9350  10368    914   -703   1695       C  
ATOM   1432  O   ALA B 188      58.393  -5.497  27.334  1.00 85.24           O  
ANISOU 1432  O   ALA B 188    12453   9442  10492   1042   -773   1759       O  
ATOM   1433  CB  ALA B 188      55.515  -3.636  27.401  1.00 82.48           C  
ANISOU 1433  CB  ALA B 188    12231   9417   9692    613   -545   1525       C  
ATOM   1434  N   VAL B 189      56.400  -6.541  27.309  1.00 76.92           N  
ANISOU 1434  N   VAL B 189    11627   8168   9432    843   -759   1828       N  
ATOM   1435  CA  VAL B 189      56.936  -7.741  27.942  1.00 78.16           C  
ANISOU 1435  CA  VAL B 189    11800   8155   9743    911   -912   2074       C  
ATOM   1436  C   VAL B 189      57.898  -8.496  27.024  1.00 80.17           C  
ANISOU 1436  C   VAL B 189    12029   8153  10280   1153   -924   2000       C  
ATOM   1437  O   VAL B 189      58.808  -9.176  27.519  1.00 81.82           O  
ANISOU 1437  O   VAL B 189    12184   8274  10629   1271  -1051   2177       O  
ATOM   1438  CB  VAL B 189      55.765  -8.618  28.419  1.00 77.62           C  
ANISOU 1438  CB  VAL B 189    11870   7957   9666    748   -960   2236       C  
ATOM   1439  CG1 VAL B 189      56.225 -10.029  28.791  1.00 77.87           C  
ANISOU 1439  CG1 VAL B 189    11944   7721   9922    834  -1110   2476       C  
ATOM   1440  CG2 VAL B 189      55.067  -7.950  29.596  1.00 76.79           C  
ANISOU 1440  CG2 VAL B 189    11759   8142   9277    524   -971   2358       C  
ATOM   1441  N   GLN B 190      57.760  -8.370  25.698  1.00 85.15           N  
ANISOU 1441  N   GLN B 190    12685   8674  10995   1235   -797   1739       N  
ATOM   1442  CA  GLN B 190      58.813  -8.883  24.828  1.00 87.04           C  
ANISOU 1442  CA  GLN B 190    12868   8732  11473   1473   -787   1632       C  
ATOM   1443  C   GLN B 190      60.082  -8.052  24.957  1.00 86.68           C  
ANISOU 1443  C   GLN B 190    12648   8896  11392   1588   -784   1604       C  
ATOM   1444  O   GLN B 190      61.188  -8.583  24.806  1.00 86.97           O  
ANISOU 1444  O   GLN B 190    12598   8824  11624   1783   -837   1632       O  
ATOM   1445  CB  GLN B 190      58.349  -8.911  23.371  1.00 87.94           C  
ANISOU 1445  CB  GLN B 190    13049   8713  11653   1518   -645   1351       C  
ATOM   1446  N   LEU B 191      59.945  -6.755  25.239  1.00 77.86           N  
ANISOU 1446  N   LEU B 191    11470   8072  10042   1472   -724   1545       N  
ATOM   1447  CA  LEU B 191      61.120  -5.904  25.384  1.00 78.85           C  
ANISOU 1447  CA  LEU B 191    11427   8404  10129   1558   -723   1515       C  
ATOM   1448  C   LEU B 191      61.866  -6.221  26.673  1.00 81.73           C  
ANISOU 1448  C   LEU B 191    11710   8847  10497   1571   -893   1778       C  
ATOM   1449  O   LEU B 191      63.066  -6.521  26.646  1.00 81.63           O  
ANISOU 1449  O   LEU B 191    11577   8802  10638   1746   -954   1820       O  
ATOM   1450  CB  LEU B 191      60.710  -4.430  25.343  1.00 76.21           C  
ANISOU 1450  CB  LEU B 191    11059   8338   9559   1418   -616   1377       C  
ATOM   1451  N   GLU B 192      61.167  -6.162  27.811  1.00117.31           N  
ANISOU 1451  N   GLU B 192    16273  13471  14828   1385   -972   1958       N  
ATOM   1452  CA  GLU B 192      61.756  -6.528  29.097  1.00120.96           C  
ANISOU 1452  CA  GLU B 192    16673  14022  15265   1373  -1147   2234       C  
ATOM   1453  C   GLU B 192      62.547  -7.827  28.992  1.00121.96           C  
ANISOU 1453  C   GLU B 192    16781  13881  15678   1572  -1263   2378       C  
ATOM   1454  O   GLU B 192      63.767  -7.841  29.195  1.00124.62           O  
ANISOU 1454  O   GLU B 192    16972  14269  16110   1718  -1342   2441       O  
ATOM   1455  CB  GLU B 192      60.655  -6.642  30.159  1.00122.33           C  
ANISOU 1455  CB  GLU B 192    16954  14285  15241   1144  -1204   2413       C  
ATOM   1456  N   LYS B 193      61.864  -8.925  28.644  1.00115.37           N  
ANISOU 1456  N   LYS B 193    16086  12750  14998   1583  -1273   2421       N  
ATOM   1457  CA  LYS B 193      62.536 -10.195  28.381  1.00114.61           C  
ANISOU 1457  CA  LYS B 193    15984  12346  15215   1787  -1365   2518       C  
ATOM   1458  C   LYS B 193      63.779  -9.995  27.519  1.00112.22           C  
ANISOU 1458  C   LYS B 193    15532  12023  15083   2025  -1309   2338       C  
ATOM   1459  O   LYS B 193      64.895 -10.352  27.919  1.00114.39           O  
ANISOU 1459  O   LYS B 193    15679  12288  15498   2179  -1426   2475       O  
ATOM   1460  CB  LYS B 193      61.567 -11.169  27.708  1.00112.54           C  
ANISOU 1460  CB  LYS B 193    15896  11759  15105   1769  -1322   2464       C  
ATOM   1461  N   ALA B 194      63.605  -9.385  26.341  1.00 86.75           N  
ANISOU 1461  N   ALA B 194    12312   8814  11836   2053  -1130   2035       N  
ATOM   1462  CA  ALA B 194      64.740  -9.182  25.445  1.00 86.24           C  
ANISOU 1462  CA  ALA B 194    12104   8744  11918   2268  -1055   1850       C  
ATOM   1463  C   ALA B 194      65.850  -8.397  26.131  1.00 88.49           C  
ANISOU 1463  C   ALA B 194    12195   9306  12121   2301  -1121   1935       C  
ATOM   1464  O   ALA B 194      67.030  -8.747  26.014  1.00 89.66           O  
ANISOU 1464  O   ALA B 194    12198   9408  12459   2503  -1171   1959       O  
ATOM   1465  CB  ALA B 194      64.289  -8.471  24.170  1.00 82.83           C  
ANISOU 1465  CB  ALA B 194    11710   8351  11411   2246   -852   1535       C  
ATOM   1466  N   GLU B 195      65.491  -7.346  26.871  1.00 98.89           N  
ANISOU 1466  N   GLU B 195    13500  10912  13162   2106  -1124   1978       N  
ATOM   1467  CA  GLU B 195      66.510  -6.581  27.580  1.00 99.94           C  
ANISOU 1467  CA  GLU B 195    13452  11317  13205   2114  -1195   2053       C  
ATOM   1468  C   GLU B 195      67.076  -7.380  28.745  1.00101.97           C  
ANISOU 1468  C   GLU B 195    13655  11554  13536   2158  -1412   2366       C  
ATOM   1469  O   GLU B 195      68.272  -7.286  29.048  1.00103.83           O  
ANISOU 1469  O   GLU B 195    13711  11892  13846   2280  -1497   2436       O  
ATOM   1470  CB  GLU B 195      65.930  -5.251  28.060  1.00 99.03           C  
ANISOU 1470  CB  GLU B 195    13346  11501  12781   1888  -1139   1994       C  
ATOM   1471  CG  GLU B 195      66.018  -4.138  27.028  1.00 98.24           C  
ANISOU 1471  CG  GLU B 195    13195  11509  12624   1889   -956   1710       C  
ATOM   1472  CD  GLU B 195      65.595  -2.795  27.583  1.00 97.76           C  
ANISOU 1472  CD  GLU B 195    13121  11734  12291   1683   -916   1660       C  
ATOM   1473  OE1 GLU B 195      64.452  -2.687  28.069  1.00 97.03           O  
ANISOU 1473  OE1 GLU B 195    13158  11670  12039   1508   -913   1700       O  
ATOM   1474  OE2 GLU B 195      66.402  -1.845  27.534  1.00 98.16           O  
ANISOU 1474  OE2 GLU B 195    13026  11976  12296   1694   -885   1574       O  
ATOM   1475  N   ALA B 196      66.233  -8.184  29.399  1.00109.86           N  
ANISOU 1475  N   ALA B 196    14800  12423  14518   2058  -1507   2567       N  
ATOM   1476  CA  ALA B 196      66.717  -9.040  30.476  1.00111.79           C  
ANISOU 1476  CA  ALA B 196    15007  12625  14843   2098  -1722   2894       C  
ATOM   1477  C   ALA B 196      67.735 -10.042  29.950  1.00112.97           C  
ANISOU 1477  C   ALA B 196    15066  12510  15347   2380  -1782   2924       C  
ATOM   1478  O   ALA B 196      68.828 -10.190  30.509  1.00113.80           O  
ANISOU 1478  O   ALA B 196    15010  12693  15537   2499  -1921   3083       O  
ATOM   1479  CB  ALA B 196      65.542  -9.757  31.144  1.00111.52           C  
ANISOU 1479  CB  ALA B 196    15159  12476  14738   1929  -1792   3098       C  
ATOM   1480  N   GLU B 197      67.400 -10.725  28.857  1.00106.17           N  
ANISOU 1480  N   GLU B 197    14300  11342  14699   2493  -1678   2758       N  
ATOM   1481  CA  GLU B 197      68.303 -11.674  28.218  1.00106.99           C  
ANISOU 1481  CA  GLU B 197    14323  11172  15155   2772  -1704   2730       C  
ATOM   1482  C   GLU B 197      69.277 -11.005  27.254  1.00106.04           C  
ANISOU 1482  C   GLU B 197    14032  11158  15100   2936  -1568   2460       C  
ATOM   1483  O   GLU B 197      69.971 -11.715  26.519  1.00106.75           O  
ANISOU 1483  O   GLU B 197    14053  11028  15478   3173  -1545   2367       O  
ATOM   1484  CB  GLU B 197      67.501 -12.752  27.483  1.00106.99           C  
ANISOU 1484  CB  GLU B 197    14505  10787  15359   2814  -1653   2657       C  
ATOM   1485  N   ASN B 198      69.336  -9.672  27.243  1.00101.76           N  
ANISOU 1485  N   ASN B 198    13419  10941  14304   2812  -1476   2331       N  
ATOM   1486  CA  ASN B 198      70.250  -8.913  26.386  1.00101.14           C  
ANISOU 1486  CA  ASN B 198    13171  11001  14257   2933  -1344   2094       C  
ATOM   1487  C   ASN B 198      70.165  -9.383  24.934  1.00101.42           C  
ANISOU 1487  C   ASN B 198    13256  10796  14483   3085  -1176   1824       C  
ATOM   1488  O   ASN B 198      71.163  -9.734  24.301  1.00102.31           O  
ANISOU 1488  O   ASN B 198    13227  10827  14818   3311  -1141   1724       O  
ATOM   1489  CB  ASN B 198      71.685  -8.992  26.913  1.00101.85           C  
ANISOU 1489  CB  ASN B 198    13025  11197  14478   3097  -1476   2232       C  
ATOM   1490  CG  ASN B 198      72.603  -7.968  26.268  1.00102.17           C  
ANISOU 1490  CG  ASN B 198    12872  11465  14484   3159  -1350   2020       C  
ATOM   1491  OD1 ASN B 198      73.303  -8.265  25.299  1.00103.15           O  
ANISOU 1491  OD1 ASN B 198    12895  11479  14817   3364  -1253   1853       O  
ATOM   1492  ND2 ASN B 198      72.599  -6.752  26.801  1.00101.73           N  
ANISOU 1492  ND2 ASN B 198    12762  11727  14165   2976  -1345   2021       N  
ATOM   1493  N   LYS B 199      68.943  -9.401  24.408  1.00 96.37           N  
ANISOU 1493  N   LYS B 199    12814  10052  13750   2955  -1071   1701       N  
ATOM   1494  CA  LYS B 199      68.700  -9.828  23.042  1.00 94.61           C  
ANISOU 1494  CA  LYS B 199    12662   9618  13666   3063   -914   1437       C  
ATOM   1495  C   LYS B 199      67.968  -8.734  22.272  1.00 91.81           C  
ANISOU 1495  C   LYS B 199    12375   9437  13074   2907   -732   1205       C  
ATOM   1496  O   LYS B 199      67.159  -8.000  22.847  1.00 89.72           O  
ANISOU 1496  O   LYS B 199    12187   9337  12565   2688   -741   1271       O  
ATOM   1497  CB  LYS B 199      67.877 -11.122  23.004  1.00 94.24           C  
ANISOU 1497  CB  LYS B 199    12802   9219  13785   3072   -972   1502       C  
ATOM   1498  N   PRO B 200      68.242  -8.591  20.977  1.00 90.98           N  
ANISOU 1498  N   PRO B 200    12235   9304  13029   3016   -565    935       N  
ATOM   1499  CA  PRO B 200      67.573  -7.551  20.187  1.00 89.42           C  
ANISOU 1499  CA  PRO B 200    12096   9268  12611   2873   -398    730       C  
ATOM   1500  C   PRO B 200      66.077  -7.804  20.087  1.00 87.77           C  
ANISOU 1500  C   PRO B 200    12112   8934  12302   2705   -382    714       C  
ATOM   1501  O   PRO B 200      65.598  -8.928  20.256  1.00 88.69           O  
ANISOU 1501  O   PRO B 200    12347   8789  12561   2729   -460    791       O  
ATOM   1502  CB  PRO B 200      68.239  -7.668  18.811  1.00 89.37           C  
ANISOU 1502  CB  PRO B 200    12010   9215  12731   3054   -241    468       C  
ATOM   1503  CG  PRO B 200      69.535  -8.379  19.066  1.00 91.06           C  
ANISOU 1503  CG  PRO B 200    12054   9345  13198   3286   -321    543       C  
ATOM   1504  CD  PRO B 200      69.245  -9.325  20.187  1.00 92.08           C  
ANISOU 1504  CD  PRO B 200    12262   9286  13439   3278   -519    807       C  
ATOM   1505  N   LEU B 201      65.328  -6.742  19.799  1.00 76.12           N  
ANISOU 1505  N   LEU B 201    10689   7642  10590   2531   -282    614       N  
ATOM   1506  CA  LEU B 201      63.903  -6.913  19.490  1.00 73.37           C  
ANISOU 1506  CA  LEU B 201    10536   7191  10149   2380   -243    557       C  
ATOM   1507  C   LEU B 201      63.625  -6.450  18.067  1.00 71.72           C  
ANISOU 1507  C   LEU B 201    10355   7017   9879   2387    -65    284       C  
ATOM   1508  O   LEU B 201      63.662  -5.235  17.801  1.00 70.97           O  
ANISOU 1508  O   LEU B 201    10198   7157   9609   2308     23    209       O  
ATOM   1509  CB  LEU B 201      63.015  -6.159  20.482  1.00 71.15           C  
ANISOU 1509  CB  LEU B 201    10314   7080   9639   2149   -296    700       C  
ATOM   1510  CG  LEU B 201      61.511  -6.464  20.405  1.00 70.76           C  
ANISOU 1510  CG  LEU B 201    10453   6921   9510   1985   -285    691       C  
ATOM   1511  CD1 LEU B 201      60.881  -6.415  21.787  1.00 72.18           C  
ANISOU 1511  CD1 LEU B 201    10682   7174   9569   1815   -405    926       C  
ATOM   1512  CD2 LEU B 201      60.785  -5.507  19.472  1.00 69.13           C  
ANISOU 1512  CD2 LEU B 201    10288   6841   9138   1885   -137    487       C  
ATOM   1513  N   PRO B 202      63.330  -7.346  17.125  1.00 73.93           N  
ANISOU 1513  N   PRO B 202    10726   7074  10288   2469    -11    131       N  
ATOM   1514  CA  PRO B 202      63.197  -6.920  15.725  1.00 72.52           C  
ANISOU 1514  CA  PRO B 202    10558   6956  10039   2486    157   -132       C  
ATOM   1515  C   PRO B 202      61.945  -6.086  15.487  1.00 71.20           C  
ANISOU 1515  C   PRO B 202    10500   6914   9640   2274    214   -178       C  
ATOM   1516  O   PRO B 202      60.857  -6.410  15.970  1.00 72.74           O  
ANISOU 1516  O   PRO B 202    10828   7017   9793   2138    146    -90       O  
ATOM   1517  CB  PRO B 202      63.132  -8.246  14.953  1.00 72.80           C  
ANISOU 1517  CB  PRO B 202    10678   6701  10283   2618    174   -273       C  
ATOM   1518  CG  PRO B 202      63.602  -9.298  15.921  1.00 74.19           C  
ANISOU 1518  CG  PRO B 202    10839   6667  10684   2721     20    -79       C  
ATOM   1519  CD  PRO B 202      63.191  -8.803  17.269  1.00 74.47           C  
ANISOU 1519  CD  PRO B 202    10885   6825  10584   2557   -101    185       C  
ATOM   1520  N   ILE B 203      62.114  -4.999  14.727  1.00 65.17           N  
ANISOU 1520  N   ILE B 203     9671   6362   8731   2248    339   -310       N  
ATOM   1521  CA  ILE B 203      61.013  -4.152  14.281  1.00 62.95           C  
ANISOU 1521  CA  ILE B 203     9474   6200   8245   2074    407   -377       C  
ATOM   1522  C   ILE B 203      61.246  -3.749  12.830  1.00 60.21           C  
ANISOU 1522  C   ILE B 203     9098   5940   7840   2128    560   -600       C  
ATOM   1523  O   ILE B 203      62.361  -3.838  12.299  1.00 60.69           O  
ANISOU 1523  O   ILE B 203     9043   6032   7985   2281    626   -689       O  
ATOM   1524  CB  ILE B 203      60.829  -2.880  15.145  1.00 63.88           C  
ANISOU 1524  CB  ILE B 203     9536   6541   8193   1929    381   -245       C  
ATOM   1525  CG1 ILE B 203      61.993  -1.909  14.940  1.00 63.87           C  
ANISOU 1525  CG1 ILE B 203     9364   6742   8161   1995    449   -277       C  
ATOM   1526  CG2 ILE B 203      60.659  -3.228  16.616  1.00 66.34           C  
ANISOU 1526  CG2 ILE B 203     9866   6810   8531   1868    234    -25       C  
ATOM   1527  CD1 ILE B 203      61.726  -0.528  15.499  1.00 63.49           C  
ANISOU 1527  CD1 ILE B 203     9272   6908   7942   1843    452   -206       C  
ATOM   1528  N   ALA B 204      60.166  -3.300  12.186  1.00 55.52           N  
ANISOU 1528  N   ALA B 204     8602   5397   7095   1996    616   -684       N  
ATOM   1529  CA  ALA B 204      60.248  -2.798  10.817  1.00 55.01           C  
ANISOU 1529  CA  ALA B 204     8520   5449   6933   2014    755   -873       C  
ATOM   1530  C   ALA B 204      59.596  -1.426  10.730  1.00 53.84           C  
ANISOU 1530  C   ALA B 204     8369   5507   6582   1854    794   -838       C  
ATOM   1531  O   ALA B 204      58.434  -1.265  11.105  1.00 55.06           O  
ANISOU 1531  O   ALA B 204     8621   5642   6658   1712    742   -777       O  
ATOM   1532  CB  ALA B 204      59.585  -3.762   9.828  1.00 53.21           C  
ANISOU 1532  CB  ALA B 204     8420   5061   6737   2031    789  -1048       C  
ATOM   1533  N   ILE B 205      60.333  -0.445  10.222  1.00 54.35           N  
ANISOU 1533  N   ILE B 205     8317   5762   6572   1877    887   -875       N  
ATOM   1534  CA  ILE B 205      59.863   0.931  10.109  1.00 52.68           C  
ANISOU 1534  CA  ILE B 205     8086   5736   6194   1740    926   -836       C  
ATOM   1535  C   ILE B 205      59.565   1.196   8.638  1.00 52.45           C  
ANISOU 1535  C   ILE B 205     8090   5787   6053   1727   1041   -989       C  
ATOM   1536  O   ILE B 205      60.480   1.211   7.809  1.00 53.27           O  
ANISOU 1536  O   ILE B 205     8111   5967   6163   1826   1138  -1089       O  
ATOM   1537  CB  ILE B 205      60.901   1.922  10.655  1.00 53.28           C  
ANISOU 1537  CB  ILE B 205     8005   5970   6269   1752    939   -746       C  
ATOM   1538  CG1 ILE B 205      61.126   1.692  12.152  1.00 54.67           C  
ANISOU 1538  CG1 ILE B 205     8151   6093   6527   1747    813   -589       C  
ATOM   1539  CG2 ILE B 205      60.478   3.350  10.379  1.00 51.08           C  
ANISOU 1539  CG2 ILE B 205     7704   5861   5841   1622    991   -724       C  
ATOM   1540  CD1 ILE B 205      62.444   2.239  12.670  1.00 54.65           C  
ANISOU 1540  CD1 ILE B 205     7977   6211   6574   1808    810   -524       C  
ATOM   1541  N   THR B 206      58.298   1.412   8.294  1.00 52.75           N  
ANISOU 1541  N   THR B 206     8238   5824   5980   1603   1031  -1006       N  
ATOM   1542  CA  THR B 206      57.896   1.608   6.908  1.00 50.27           C  
ANISOU 1542  CA  THR B 206     7966   5591   5543   1577   1120  -1140       C  
ATOM   1543  C   THR B 206      57.535   3.069   6.680  1.00 49.55           C  
ANISOU 1543  C   THR B 206     7836   5684   5309   1462   1155  -1069       C  
ATOM   1544  O   THR B 206      56.818   3.669   7.485  1.00 48.43           O  
ANISOU 1544  O   THR B 206     7713   5545   5144   1357   1089   -954       O  
ATOM   1545  CB  THR B 206      56.718   0.700   6.554  1.00 49.93           C  
ANISOU 1545  CB  THR B 206     8073   5410   5488   1525   1076  -1222       C  
ATOM   1546  OG1 THR B 206      55.549   1.136   7.257  1.00 49.63           O  
ANISOU 1546  OG1 THR B 206     8095   5363   5400   1383    995  -1107       O  
ATOM   1547  CG2 THR B 206      57.030  -0.735   6.946  1.00 50.05           C  
ANISOU 1547  CG2 THR B 206     8133   5207   5678   1630   1024  -1268       C  
ATOM   1548  N   ILE B 207      58.034   3.636   5.584  1.00 57.00           N  
ANISOU 1548  N   ILE B 207     8721   6778   6159   1481   1262  -1136       N  
ATOM   1549  CA  ILE B 207      57.867   5.049   5.265  1.00 56.25           C  
ANISOU 1549  CA  ILE B 207     8576   6851   5946   1383   1303  -1058       C  
ATOM   1550  C   ILE B 207      57.320   5.161   3.849  1.00 54.09           C  
ANISOU 1550  C   ILE B 207     8359   6673   5521   1342   1369  -1152       C  
ATOM   1551  O   ILE B 207      57.813   4.490   2.935  1.00 56.45           O  
ANISOU 1551  O   ILE B 207     8658   6997   5792   1422   1444  -1292       O  
ATOM   1552  CB  ILE B 207      59.195   5.819   5.395  1.00 58.09           C  
ANISOU 1552  CB  ILE B 207     8655   7205   6210   1431   1368  -1005       C  
ATOM   1553  CG1 ILE B 207      59.864   5.495   6.731  1.00 60.42           C  
ANISOU 1553  CG1 ILE B 207     8888   7413   6655   1489   1296   -932       C  
ATOM   1554  CG2 ILE B 207      58.962   7.315   5.258  1.00 57.44           C  
ANISOU 1554  CG2 ILE B 207     8527   7258   6039   1316   1390   -901       C  
ATOM   1555  CD1 ILE B 207      61.156   6.229   6.961  1.00 62.33           C  
ANISOU 1555  CD1 ILE B 207     8969   7774   6939   1526   1344   -878       C  
ATOM   1556  N   GLY B 208      56.312   6.013   3.667  1.00 49.49           N  
ANISOU 1556  N   GLY B 208     7816   6151   4838   1221   1340  -1080       N  
ATOM   1557  CA  GLY B 208      55.680   6.180   2.371  1.00 49.22           C  
ANISOU 1557  CA  GLY B 208     7835   6221   4646   1166   1381  -1143       C  
ATOM   1558  C   GLY B 208      54.724   5.051   2.051  1.00 51.40           C  
ANISOU 1558  C   GLY B 208     8237   6388   4902   1154   1330  -1260       C  
ATOM   1559  O   GLY B 208      55.126   4.044   1.461  1.00 53.80           O  
ANISOU 1559  O   GLY B 208     8573   6657   5213   1233   1373  -1414       O  
ATOM   1560  N   ASN B 209      53.454   5.204   2.422  1.00 48.84           N  
ANISOU 1560  N   ASN B 209     7983   6012   4563   1053   1241  -1199       N  
ATOM   1561  CA  ASN B 209      52.524   4.086   2.413  1.00 49.24           C  
ANISOU 1561  CA  ASN B 209     8147   5929   4632   1027   1173  -1291       C  
ATOM   1562  C   ASN B 209      51.183   4.496   1.825  1.00 47.87           C  
ANISOU 1562  C   ASN B 209     8030   5825   4334    906   1127  -1275       C  
ATOM   1563  O   ASN B 209      50.878   5.682   1.669  1.00 45.46           O  
ANISOU 1563  O   ASN B 209     7676   5641   3956    844   1129  -1164       O  
ATOM   1564  CB  ASN B 209      52.305   3.537   3.830  1.00 48.74           C  
ANISOU 1564  CB  ASN B 209     8108   5687   4724   1028   1087  -1224       C  
ATOM   1565  CG  ASN B 209      53.507   2.787   4.354  1.00 49.03           C  
ANISOU 1565  CG  ASN B 209     8107   5624   4897   1156   1108  -1255       C  
ATOM   1566  OD1 ASN B 209      53.875   1.736   3.827  1.00 49.85           O  
ANISOU 1566  OD1 ASN B 209     8251   5648   5041   1236   1135  -1395       O  
ATOM   1567  ND2 ASN B 209      54.131   3.323   5.397  1.00 47.54           N  
ANISOU 1567  ND2 ASN B 209     7837   5439   4787   1178   1093  -1131       N  
ATOM   1568  N   ASN B 210      50.391   3.474   1.487  1.00 53.80           N  
ANISOU 1568  N   ASN B 210     8880   6489   5073    873   1079  -1388       N  
ATOM   1569  CA  ASN B 210      48.956   3.561   1.255  1.00 53.27           C  
ANISOU 1569  CA  ASN B 210     8871   6437   4933    752   1002  -1372       C  
ATOM   1570  C   ASN B 210      48.361   4.455   2.336  1.00 52.41           C  
ANISOU 1570  C   ASN B 210     8716   6317   4881    689    945  -1198       C  
ATOM   1571  O   ASN B 210      48.604   4.223   3.527  1.00 52.40           O  
ANISOU 1571  O   ASN B 210     8703   6199   5009    712    919  -1140       O  
ATOM   1572  CB  ASN B 210      48.348   2.152   1.278  1.00 55.06           C  
ANISOU 1572  CB  ASN B 210     9202   6501   5217    732    945  -1502       C  
ATOM   1573  CG  ASN B 210      46.838   2.132   1.054  1.00 58.51           C  
ANISOU 1573  CG  ASN B 210     9691   6952   5587    598    859  -1495       C  
ATOM   1574  OD1 ASN B 210      46.104   3.013   1.498  1.00 58.64           O  
ANISOU 1574  OD1 ASN B 210     9665   7026   5589    526    815  -1358       O  
ATOM   1575  ND2 ASN B 210      46.370   1.094   0.372  1.00 61.92           N  
ANISOU 1575  ND2 ASN B 210    10210   7327   5990    566    833  -1654       N  
ATOM   1576  N   PRO B 211      47.597   5.489   1.969  1.00 51.97           N  
ANISOU 1576  N   PRO B 211     8627   6383   4734    612    924  -1113       N  
ATOM   1577  CA  PRO B 211      47.068   6.405   2.995  1.00 50.87           C  
ANISOU 1577  CA  PRO B 211     8434   6234   4661    562    882   -967       C  
ATOM   1578  C   PRO B 211      46.255   5.703   4.068  1.00 52.30           C  
ANISOU 1578  C   PRO B 211     8657   6276   4938    512    808   -957       C  
ATOM   1579  O   PRO B 211      46.278   6.127   5.232  1.00 51.27           O  
ANISOU 1579  O   PRO B 211     8482   6105   4892    504    793   -865       O  
ATOM   1580  CB  PRO B 211      46.210   7.389   2.183  1.00 49.49           C  
ANISOU 1580  CB  PRO B 211     8232   6196   4377    491    860   -905       C  
ATOM   1581  CG  PRO B 211      45.953   6.702   0.871  1.00 51.74           C  
ANISOU 1581  CG  PRO B 211     8581   6547   4530    474    860  -1025       C  
ATOM   1582  CD  PRO B 211      47.154   5.851   0.612  1.00 52.67           C  
ANISOU 1582  CD  PRO B 211     8728   6627   4659    566    933  -1147       C  
ATOM   1583  N   LEU B 212      45.557   4.621   3.718  1.00 45.08           N  
ANISOU 1583  N   LEU B 212     7826   5292   4012    469    762  -1054       N  
ATOM   1584  CA  LEU B 212      44.794   3.880   4.714  1.00 44.49           C  
ANISOU 1584  CA  LEU B 212     7792   5083   4029    409    695  -1036       C  
ATOM   1585  C   LEU B 212      45.692   3.058   5.633  1.00 45.67           C  
ANISOU 1585  C   LEU B 212     7963   5087   4301    479    703  -1036       C  
ATOM   1586  O   LEU B 212      45.319   2.804   6.783  1.00 46.27           O  
ANISOU 1586  O   LEU B 212     8043   5080   4457    435    658   -960       O  
ATOM   1587  CB  LEU B 212      43.764   2.988   4.020  1.00 44.40           C  
ANISOU 1587  CB  LEU B 212     7858   5036   3974    328    639  -1137       C  
ATOM   1588  CG  LEU B 212      42.594   3.775   3.418  1.00 43.67           C  
ANISOU 1588  CG  LEU B 212     7732   5081   3781    236    598  -1101       C  
ATOM   1589  CD1 LEU B 212      41.763   2.898   2.505  1.00 44.60           C  
ANISOU 1589  CD1 LEU B 212     7921   5192   3832    161    546  -1223       C  
ATOM   1590  CD2 LEU B 212      41.729   4.387   4.516  1.00 42.78           C  
ANISOU 1590  CD2 LEU B 212     7558   4965   3730    169    558   -976       C  
ATOM   1591  N   VAL B 213      46.875   2.655   5.166  1.00 48.04           N  
ANISOU 1591  N   VAL B 213     8270   5367   4617    587    759  -1113       N  
ATOM   1592  CA  VAL B 213      47.832   1.995   6.051  1.00 48.39           C  
ANISOU 1592  CA  VAL B 213     8313   5283   4789    671    762  -1093       C  
ATOM   1593  C   VAL B 213      48.299   2.959   7.136  1.00 48.98           C  
ANISOU 1593  C   VAL B 213     8299   5413   4897    682    768   -951       C  
ATOM   1594  O   VAL B 213      48.333   2.616   8.324  1.00 50.36           O  
ANISOU 1594  O   VAL B 213     8476   5501   5159    671    723   -871       O  
ATOM   1595  CB  VAL B 213      49.015   1.432   5.243  1.00 48.04           C  
ANISOU 1595  CB  VAL B 213     8274   5220   4759    796    829  -1216       C  
ATOM   1596  CG1 VAL B 213      50.190   1.114   6.161  1.00 47.21           C  
ANISOU 1596  CG1 VAL B 213     8125   5028   4785    902    837  -1164       C  
ATOM   1597  CG2 VAL B 213      48.586   0.193   4.472  1.00 49.40           C  
ANISOU 1597  CG2 VAL B 213     8548   5282   4938    787    810  -1376       C  
ATOM   1598  N   THR B 214      48.667   4.183   6.742  1.00 44.26           N  
ANISOU 1598  N   THR B 214     7624   4963   4229    695    822   -916       N  
ATOM   1599  CA  THR B 214      48.994   5.210   7.726  1.00 42.81           C  
ANISOU 1599  CA  THR B 214     7355   4834   4075    687    825   -798       C  
ATOM   1600  C   THR B 214      47.805   5.488   8.638  1.00 43.02           C  
ANISOU 1600  C   THR B 214     7388   4849   4111    580    765   -723       C  
ATOM   1601  O   THR B 214      47.973   5.710   9.843  1.00 41.47           O  
ANISOU 1601  O   THR B 214     7154   4637   3965    566    744   -645       O  
ATOM   1602  CB  THR B 214      49.437   6.492   7.018  1.00 41.52           C  
ANISOU 1602  CB  THR B 214     7115   4818   3844    702    889   -775       C  
ATOM   1603  OG1 THR B 214      50.538   6.204   6.146  1.00 42.16           O  
ANISOU 1603  OG1 THR B 214     7182   4932   3904    794    957   -849       O  
ATOM   1604  CG2 THR B 214      49.863   7.548   8.032  1.00 38.78           C  
ANISOU 1604  CG2 THR B 214     6679   4512   3543    693    894   -673       C  
ATOM   1605  N   PHE B 215      46.593   5.471   8.079  1.00 47.60           N  
ANISOU 1605  N   PHE B 215     8006   5448   4634    501    737   -750       N  
ATOM   1606  CA  PHE B 215      45.396   5.710   8.880  1.00 46.27           C  
ANISOU 1606  CA  PHE B 215     7828   5278   4474    399    687   -689       C  
ATOM   1607  C   PHE B 215      45.225   4.643   9.960  1.00 47.13           C  
ANISOU 1607  C   PHE B 215     7987   5267   4654    367    639   -662       C  
ATOM   1608  O   PHE B 215      44.888   4.959  11.107  1.00 45.10           O  
ANISOU 1608  O   PHE B 215     7693   5023   4418    314    620   -585       O  
ATOM   1609  CB  PHE B 215      44.175   5.762   7.963  1.00 46.18           C  
ANISOU 1609  CB  PHE B 215     7841   5311   4394    327    660   -729       C  
ATOM   1610  CG  PHE B 215      42.958   6.355   8.602  1.00 46.21           C  
ANISOU 1610  CG  PHE B 215     7799   5356   4402    233    626   -668       C  
ATOM   1611  CD1 PHE B 215      42.921   7.696   8.941  1.00 44.82           C  
ANISOU 1611  CD1 PHE B 215     7533   5265   4230    236    651   -604       C  
ATOM   1612  CD2 PHE B 215      41.842   5.574   8.848  1.00 47.44           C  
ANISOU 1612  CD2 PHE B 215     7995   5462   4567    142    572   -681       C  
ATOM   1613  CE1 PHE B 215      41.796   8.245   9.525  1.00 45.25           C  
ANISOU 1613  CE1 PHE B 215     7536   5357   4301    162    627   -565       C  
ATOM   1614  CE2 PHE B 215      40.715   6.116   9.430  1.00 47.80           C  
ANISOU 1614  CE2 PHE B 215     7984   5560   4619     59    550   -632       C  
ATOM   1615  CZ  PHE B 215      40.691   7.455   9.769  1.00 46.78           C  
ANISOU 1615  CZ  PHE B 215     7760   5518   4495     75    580   -579       C  
ATOM   1616  N   MET B 216      45.455   3.375   9.610  1.00 42.17           N  
ANISOU 1616  N   MET B 216     7439   4520   4063    396    619   -726       N  
ATOM   1617  CA  MET B 216      45.347   2.285  10.579  1.00 46.27           C  
ANISOU 1617  CA  MET B 216     8012   4904   4665    366    566   -682       C  
ATOM   1618  C   MET B 216      46.503   2.299  11.576  1.00 47.01           C  
ANISOU 1618  C   MET B 216     8067   4975   4820    440    570   -603       C  
ATOM   1619  O   MET B 216      46.346   1.861  12.729  1.00 48.96           O  
ANISOU 1619  O   MET B 216     8325   5169   5110    394    524   -512       O  
ATOM   1620  CB  MET B 216      45.289   0.945   9.839  1.00 46.01           C  
ANISOU 1620  CB  MET B 216     8077   4728   4677    381    542   -782       C  
ATOM   1621  CG  MET B 216      45.391  -0.300  10.715  1.00 48.58           C  
ANISOU 1621  CG  MET B 216     8465   4875   5116    371    485   -732       C  
ATOM   1622  SD  MET B 216      47.088  -0.800  11.091  1.00 51.30           S  
ANISOU 1622  SD  MET B 216     8797   5126   5569    533    498   -711       S  
ATOM   1623  CE  MET B 216      47.809  -0.942   9.458  1.00 51.25           C  
ANISOU 1623  CE  MET B 216     8804   5127   5542    651    569   -898       C  
ATOM   1624  N   ALA B 217      47.675   2.768  11.146  1.00 46.07           N  
ANISOU 1624  N   ALA B 217     7897   4905   4701    549    622   -632       N  
ATOM   1625  CA  ALA B 217      48.809   2.856  12.056  1.00 46.82           C  
ANISOU 1625  CA  ALA B 217     7938   4999   4852    619    620   -559       C  
ATOM   1626  C   ALA B 217      48.588   3.926  13.115  1.00 45.73           C  
ANISOU 1626  C   ALA B 217     7727   4973   4676    551    615   -466       C  
ATOM   1627  O   ALA B 217      49.103   3.807  14.231  1.00 47.73           O  
ANISOU 1627  O   ALA B 217     7953   5221   4962    557    582   -383       O  
ATOM   1628  CB  ALA B 217      50.091   3.132  11.272  1.00 46.42           C  
ANISOU 1628  CB  ALA B 217     7837   4990   4812    744    683   -620       C  
ATOM   1629  N   SER B 218      47.824   4.966  12.792  1.00 47.80           N  
ANISOU 1629  N   SER B 218     7956   5337   4870    489    643   -482       N  
ATOM   1630  CA  SER B 218      47.490   6.012  13.748  1.00 46.67           C  
ANISOU 1630  CA  SER B 218     7742   5290   4698    423    645   -422       C  
ATOM   1631  C   SER B 218      46.247   5.686  14.564  1.00 46.55           C  
ANISOU 1631  C   SER B 218     7756   5265   4666    308    604   -381       C  
ATOM   1632  O   SER B 218      45.856   6.488  15.419  1.00 46.67           O  
ANISOU 1632  O   SER B 218     7714   5366   4654    247    610   -347       O  
ATOM   1633  CB  SER B 218      47.301   7.349  13.025  1.00 48.11           C  
ANISOU 1633  CB  SER B 218     7864   5574   4842    420    696   -453       C  
ATOM   1634  OG  SER B 218      48.504   7.760  12.399  1.00 49.26           O  
ANISOU 1634  OG  SER B 218     7969   5750   4998    510    742   -473       O  
ATOM   1635  N   THR B 219      45.622   4.533  14.327  1.00 36.17           N  
ANISOU 1635  N   THR B 219     6524   3850   3369    272    565   -390       N  
ATOM   1636  CA  THR B 219      44.503   4.096  15.145  1.00 40.45           C  
ANISOU 1636  CA  THR B 219     7089   4381   3898    152    527   -339       C  
ATOM   1637  C   THR B 219      45.017   3.116  16.188  1.00 42.60           C  
ANISOU 1637  C   THR B 219     7400   4573   4213    148    477   -247       C  
ATOM   1638  O   THR B 219      45.471   2.013  15.825  1.00 45.07           O  
ANISOU 1638  O   THR B 219     7783   4747   4594    201    446   -253       O  
ATOM   1639  CB  THR B 219      43.414   3.453  14.292  1.00 40.80           C  
ANISOU 1639  CB  THR B 219     7196   4367   3942     92    507   -394       C  
ATOM   1640  OG1 THR B 219      43.066   4.337  13.221  1.00 38.94           O  
ANISOU 1640  OG1 THR B 219     6922   4210   3661    109    542   -466       O  
ATOM   1641  CG2 THR B 219      42.176   3.197  15.135  1.00 40.90           C  
ANISOU 1641  CG2 THR B 219     7206   4397   3936    -46    479   -338       C  
ATOM   1642  N   PRO B 220      44.998   3.474  17.475  1.00 57.77           N  
ANISOU 1642  N   PRO B 220     9276   6577   6098     91    467   -164       N  
ATOM   1643  CA  PRO B 220      45.533   2.578  18.508  1.00 58.51           C  
ANISOU 1643  CA  PRO B 220     9401   6612   6220     83    409    -51       C  
ATOM   1644  C   PRO B 220      44.535   1.521  18.958  1.00 58.27           C  
ANISOU 1644  C   PRO B 220     9440   6504   6198    -33    362     21       C  
ATOM   1645  O   PRO B 220      44.917   0.369  19.183  1.00 62.84           O  
ANISOU 1645  O   PRO B 220    10084   6943   6848    -16    304     95       O  
ATOM   1646  CB  PRO B 220      45.888   3.536  19.658  1.00 57.58           C  
ANISOU 1646  CB  PRO B 220     9197   6651   6031     56    422     -2       C  
ATOM   1647  CG  PRO B 220      45.693   4.938  19.112  1.00 57.32           C  
ANISOU 1647  CG  PRO B 220     9090   6726   5963     71    491   -105       C  
ATOM   1648  CD  PRO B 220      44.694   4.807  18.013  1.00 57.36           C  
ANISOU 1648  CD  PRO B 220     9133   6682   5980     48    510   -176       C  
ATOM   1649  N   VAL B 221      43.262   1.897  19.105  1.00 51.70           N  
ANISOU 1649  N   VAL B 221     8585   5753   5305   -152    386      4       N  
ATOM   1650  CA  VAL B 221      42.201   0.985  19.526  1.00 54.54           C  
ANISOU 1650  CA  VAL B 221     8996   6061   5667   -285    350     72       C  
ATOM   1651  C   VAL B 221      40.917   1.354  18.790  1.00 53.31           C  
ANISOU 1651  C   VAL B 221     8819   5949   5488   -358    383    -19       C  
ATOM   1652  O   VAL B 221      40.813   2.412  18.166  1.00 52.55           O  
ANISOU 1652  O   VAL B 221     8662   5941   5363   -311    430   -111       O  
ATOM   1653  CB  VAL B 221      41.955   1.018  21.053  1.00 56.37           C  
ANISOU 1653  CB  VAL B 221     9192   6403   5821   -394    338    199       C  
ATOM   1654  CG1 VAL B 221      43.169   0.502  21.821  1.00 59.73           C  
ANISOU 1654  CG1 VAL B 221     9641   6785   6269   -334    283    315       C  
ATOM   1655  CG2 VAL B 221      41.581   2.424  21.505  1.00 53.68           C  
ANISOU 1655  CG2 VAL B 221     8746   6269   5383   -425    406    141       C  
ATOM   1656  N   GLY B 222      39.923   0.475  18.883  1.00 45.52           N  
ANISOU 1656  N   GLY B 222     7877   4899   4519   -478    351     20       N  
ATOM   1657  CA  GLY B 222      38.625   0.706  18.271  1.00 46.52           C  
ANISOU 1657  CA  GLY B 222     7974   5074   4627   -564    369    -53       C  
ATOM   1658  C   GLY B 222      38.228  -0.293  17.202  1.00 48.23           C  
ANISOU 1658  C   GLY B 222     8275   5134   4914   -583    325   -111       C  
ATOM   1659  O   GLY B 222      37.095  -0.216  16.707  1.00 49.22           O  
ANISOU 1659  O   GLY B 222     8375   5301   5026   -670    326   -164       O  
ATOM   1660  N   TYR B 223      39.093  -1.228  16.810  1.00 54.59           N  
ANISOU 1660  N   TYR B 223     9175   5765   5802   -507    286   -115       N  
ATOM   1661  CA  TYR B 223      38.751  -2.231  15.813  1.00 56.12           C  
ANISOU 1661  CA  TYR B 223     9456   5799   6070   -528    245   -194       C  
ATOM   1662  C   TYR B 223      39.180  -3.611  16.292  1.00 58.34           C  
ANISOU 1662  C   TYR B 223     9835   5870   6460   -544    184   -107       C  
ATOM   1663  O   TYR B 223      40.161  -3.756  17.027  1.00 58.72           O  
ANISOU 1663  O   TYR B 223     9891   5882   6537   -471    173    -13       O  
ATOM   1664  CB  TYR B 223      39.387  -1.922  14.442  1.00 53.86           C  
ANISOU 1664  CB  TYR B 223     9186   5495   5785   -393    267   -343       C  
ATOM   1665  CG  TYR B 223      40.886  -1.687  14.448  1.00 52.65           C  
ANISOU 1665  CG  TYR B 223     9032   5319   5654   -229    292   -344       C  
ATOM   1666  CD1 TYR B 223      41.412  -0.432  14.728  1.00 50.93           C  
ANISOU 1666  CD1 TYR B 223     8724   5259   5367   -161    343   -328       C  
ATOM   1667  CD2 TYR B 223      41.774  -2.714  14.145  1.00 53.58           C  
ANISOU 1667  CD2 TYR B 223     9232   5252   5875   -140    264   -370       C  
ATOM   1668  CE1 TYR B 223      42.781  -0.208  14.722  1.00 50.07           C  
ANISOU 1668  CE1 TYR B 223     8603   5140   5282    -22    364   -329       C  
ATOM   1669  CE2 TYR B 223      43.147  -2.497  14.136  1.00 53.74           C  
ANISOU 1669  CE2 TYR B 223     9232   5263   5922     14    288   -373       C  
ATOM   1670  CZ  TYR B 223      43.646  -1.240  14.426  1.00 52.51           C  
ANISOU 1670  CZ  TYR B 223     8983   5282   5687     67    337   -349       C  
ATOM   1671  OH  TYR B 223      45.009  -1.000  14.425  1.00 54.10           O  
ANISOU 1671  OH  TYR B 223     9152   5487   5916    209    360   -350       O  
ATOM   1672  N   ASN B 224      38.427  -4.625  15.863  1.00 70.69           N  
ANISOU 1672  N   ASN B 224    11471   7293   8095   -644    138   -137       N  
ATOM   1673  CA  ASN B 224      38.674  -6.002  16.269  1.00 73.64           C  
ANISOU 1673  CA  ASN B 224    11944   7438   8600   -677     73    -51       C  
ATOM   1674  C   ASN B 224      39.540  -6.774  15.284  1.00 73.26           C  
ANISOU 1674  C   ASN B 224    11984   7180   8670   -544     51   -174       C  
ATOM   1675  O   ASN B 224      40.168  -7.763  15.677  1.00 74.22           O  
ANISOU 1675  O   ASN B 224    12178   7102   8923   -506      2    -99       O  
ATOM   1676  CB  ASN B 224      37.347  -6.744  16.454  1.00 77.16           C  
ANISOU 1676  CB  ASN B 224    12417   7825   9074   -880     33     -7       C  
ATOM   1677  CG  ASN B 224      36.604  -6.308  17.699  1.00 79.70           C  
ANISOU 1677  CG  ASN B 224    12660   8318   9303  -1020     51    149       C  
ATOM   1678  OD1 ASN B 224      37.212  -5.881  18.681  1.00 80.12           O  
ANISOU 1678  OD1 ASN B 224    12675   8463   9303   -980     68    266       O  
ATOM   1679  ND2 ASN B 224      35.280  -6.411  17.664  1.00 80.88           N  
ANISOU 1679  ND2 ASN B 224    12778   8527   9427  -1191     49    145       N  
ATOM   1680  N   GLN B 225      39.583  -6.355  14.023  1.00 60.10           N  
ANISOU 1680  N   GLN B 225    10312   5561   6963   -473     87   -359       N  
ATOM   1681  CA  GLN B 225      40.393  -7.044  13.033  1.00 58.43           C  
ANISOU 1681  CA  GLN B 225    10176   5177   6846   -346     82   -503       C  
ATOM   1682  C   GLN B 225      41.878  -6.848  13.323  1.00 57.65           C  
ANISOU 1682  C   GLN B 225    10057   5061   6786   -162    107   -467       C  
ATOM   1683  O   GLN B 225      42.287  -5.919  14.025  1.00 56.58           O  
ANISOU 1683  O   GLN B 225     9840   5088   6571   -124    137   -369       O  
ATOM   1684  CB  GLN B 225      40.072  -6.537  11.625  1.00 56.11           C  
ANISOU 1684  CB  GLN B 225     9871   4987   6463   -325    120   -702       C  
ATOM   1685  CG  GLN B 225      38.589  -6.495  11.291  1.00 56.41           C  
ANISOU 1685  CG  GLN B 225     9897   5097   6439   -501     93   -739       C  
ATOM   1686  CD  GLN B 225      37.948  -5.163  11.634  1.00 56.40           C  
ANISOU 1686  CD  GLN B 225     9779   5353   6299   -551    130   -671       C  
ATOM   1687  OE1 GLN B 225      38.245  -4.564  12.669  1.00 56.46           O  
ANISOU 1687  OE1 GLN B 225     9725   5447   6278   -532    155   -536       O  
ATOM   1688  NE2 GLN B 225      37.062  -4.693  10.764  1.00 56.34           N  
ANISOU 1688  NE2 GLN B 225     9733   5469   6205   -614    130   -768       N  
ATOM   1689  N   ASN B 226      42.688  -7.747  12.773  1.00 64.41           N  
ANISOU 1689  N   ASN B 226    10983   5716   7774    -47     93   -558       N  
ATOM   1690  CA  ASN B 226      44.125  -7.531  12.771  1.00 65.05           C  
ANISOU 1690  CA  ASN B 226    11029   5795   7893    145    126   -565       C  
ATOM   1691  C   ASN B 226      44.460  -6.351  11.860  1.00 62.34           C  
ANISOU 1691  C   ASN B 226    10612   5666   7409    226    211   -695       C  
ATOM   1692  O   ASN B 226      43.649  -5.928  11.031  1.00 61.81           O  
ANISOU 1692  O   ASN B 226    10544   5703   7239    154    235   -804       O  
ATOM   1693  CB  ASN B 226      44.853  -8.803  12.333  1.00 67.70           C  
ANISOU 1693  CB  ASN B 226    11446   5857   8418    255     98   -652       C  
ATOM   1694  CG  ASN B 226      44.591  -9.975  13.270  1.00 70.46           C  
ANISOU 1694  CG  ASN B 226    11869   5971   8929    179      5   -495       C  
ATOM   1695  OD1 ASN B 226      44.303  -9.785  14.453  1.00 72.52           O  
ANISOU 1695  OD1 ASN B 226    12101   6295   9156     88    -33   -285       O  
ATOM   1696  ND2 ASN B 226      44.685 -11.190  12.742  1.00 69.92           N  
ANISOU 1696  ND2 ASN B 226    11896   5633   9038    210    -31   -598       N  
ATOM   1697  N   GLU B 227      45.673  -5.815  12.028  1.00 56.23           N  
ANISOU 1697  N   GLU B 227     9772   4961   6632    373    251   -671       N  
ATOM   1698  CA  GLU B 227      46.026  -4.519  11.447  1.00 53.79           C  
ANISOU 1698  CA  GLU B 227     9376   4875   6185    431    330   -735       C  
ATOM   1699  C   GLU B 227      45.770  -4.474   9.938  1.00 53.85           C  
ANISOU 1699  C   GLU B 227     9413   4919   6129    445    376   -937       C  
ATOM   1700  O   GLU B 227      44.980  -3.657   9.444  1.00 51.83           O  
ANISOU 1700  O   GLU B 227     9129   4824   5742    364    398   -970       O  
ATOM   1701  CB  GLU B 227      47.493  -4.200  11.759  1.00 53.01           C  
ANISOU 1701  CB  GLU B 227     9208   4807   6127    591    361   -696       C  
ATOM   1702  CG  GLU B 227      47.867  -4.191  13.251  1.00 54.62           C  
ANISOU 1702  CG  GLU B 227     9375   5005   6375    582    308   -494       C  
ATOM   1703  CD  GLU B 227      47.099  -3.159  14.071  1.00 56.35           C  
ANISOU 1703  CD  GLU B 227     9538   5409   6464    453    308   -383       C  
ATOM   1704  OE1 GLU B 227      45.980  -3.480  14.522  1.00 58.51           O  
ANISOU 1704  OE1 GLU B 227     9853   5655   6721    310    267   -323       O  
ATOM   1705  OE2 GLU B 227      47.608  -2.029  14.271  1.00 57.07           O  
ANISOU 1705  OE2 GLU B 227     9538   5671   6476    491    352   -362       O  
ATOM   1706  N   TYR B 228      46.438  -5.354   9.189  1.00 51.49           N  
ANISOU 1706  N   TYR B 228     9167   4476   5922    550    391  -1077       N  
ATOM   1707  CA  TYR B 228      46.283  -5.355   7.737  1.00 51.06           C  
ANISOU 1707  CA  TYR B 228     9140   4472   5787    564    439  -1284       C  
ATOM   1708  C   TYR B 228      44.869  -5.755   7.324  1.00 51.52           C  
ANISOU 1708  C   TYR B 228     9269   4501   5806    401    388  -1345       C  
ATOM   1709  O   TYR B 228      44.349  -5.255   6.316  1.00 49.55           O  
ANISOU 1709  O   TYR B 228     9013   4396   5419    355    415  -1453       O  
ATOM   1710  CB  TYR B 228      47.328  -6.281   7.115  1.00 52.03           C  
ANISOU 1710  CB  TYR B 228     9300   4440   6028    716    472  -1437       C  
ATOM   1711  CG  TYR B 228      48.754  -5.860   7.417  1.00 51.39           C  
ANISOU 1711  CG  TYR B 228     9130   4411   5985    882    526  -1388       C  
ATOM   1712  CD1 TYR B 228      49.118  -4.519   7.415  1.00 50.57           C  
ANISOU 1712  CD1 TYR B 228     8923   4544   5746    900    584  -1324       C  
ATOM   1713  CD2 TYR B 228      49.733  -6.802   7.709  1.00 52.84           C  
ANISOU 1713  CD2 TYR B 228     9323   4399   6353   1019    515  -1404       C  
ATOM   1714  CE1 TYR B 228      50.418  -4.127   7.689  1.00 51.03           C  
ANISOU 1714  CE1 TYR B 228     8891   4656   5841   1038    630  -1281       C  
ATOM   1715  CE2 TYR B 228      51.037  -6.419   7.984  1.00 53.37           C  
ANISOU 1715  CE2 TYR B 228     9292   4525   6459   1169    560  -1358       C  
ATOM   1716  CZ  TYR B 228      51.372  -5.081   7.974  1.00 51.88           C  
ANISOU 1716  CZ  TYR B 228     9001   4586   6124   1172    618  -1299       C  
ATOM   1717  OH  TYR B 228      52.665  -4.696   8.247  1.00 51.65           O  
ANISOU 1717  OH  TYR B 228     8867   4621   6136   1308    659  -1255       O  
ATOM   1718  N   GLU B 229      44.226  -6.635   8.096  1.00 58.92           N  
ANISOU 1718  N   GLU B 229    10268   5262   6858    303    311  -1264       N  
ATOM   1719  CA  GLU B 229      42.820  -6.943   7.854  1.00 59.33           C  
ANISOU 1719  CA  GLU B 229    10367   5300   6874    127    258  -1296       C  
ATOM   1720  C   GLU B 229      41.953  -5.701   8.018  1.00 56.35           C  
ANISOU 1720  C   GLU B 229     9906   5168   6337     26    267  -1207       C  
ATOM   1721  O   GLU B 229      40.992  -5.497   7.266  1.00 55.79           O  
ANISOU 1721  O   GLU B 229     9837   5190   6172    -73    253  -1289       O  
ATOM   1722  CB  GLU B 229      42.361  -8.048   8.804  1.00 63.18           C  
ANISOU 1722  CB  GLU B 229    10923   5560   7521     33    177  -1188       C  
ATOM   1723  CG  GLU B 229      41.223  -8.901   8.276  1.00 67.38           C  
ANISOU 1723  CG  GLU B 229    11537   5978   8088   -120    120  -1292       C  
ATOM   1724  CD  GLU B 229      41.045 -10.181   9.069  1.00 71.32           C  
ANISOU 1724  CD  GLU B 229    12118   6197   8784   -186     45  -1203       C  
ATOM   1725  OE1 GLU B 229      41.141 -10.127  10.314  1.00 72.81           O  
ANISOU 1725  OE1 GLU B 229    12279   6368   9017   -209     20   -986       O  
ATOM   1726  OE2 GLU B 229      40.808 -11.241   8.450  1.00 71.90           O  
ANISOU 1726  OE2 GLU B 229    12285   6068   8967   -222     10  -1349       O  
ATOM   1727  N   PHE B 230      42.280  -4.852   8.995  1.00 44.86           N  
ANISOU 1727  N   PHE B 230     8371   3819   4855     53    287  -1044       N  
ATOM   1728  CA  PHE B 230      41.526  -3.616   9.170  1.00 44.02           C  
ANISOU 1728  CA  PHE B 230     8176   3932   4617    -23    302   -972       C  
ATOM   1729  C   PHE B 230      41.761  -2.663   8.006  1.00 43.53           C  
ANISOU 1729  C   PHE B 230     8068   4044   4428     42    358  -1075       C  
ATOM   1730  O   PHE B 230      40.846  -1.937   7.600  1.00 43.59           O  
ANISOU 1730  O   PHE B 230     8030   4198   4334    -38    353  -1079       O  
ATOM   1731  CB  PHE B 230      41.890  -2.948  10.494  1.00 42.86           C  
ANISOU 1731  CB  PHE B 230     7958   3852   4475     -7    314   -797       C  
ATOM   1732  CG  PHE B 230      41.078  -1.720  10.796  1.00 41.56           C  
ANISOU 1732  CG  PHE B 230     7701   3889   4203    -85    332   -732       C  
ATOM   1733  CD1 PHE B 230      39.698  -1.795  10.899  1.00 42.06           C  
ANISOU 1733  CD1 PHE B 230     7755   3986   4238   -235    296   -715       C  
ATOM   1734  CD2 PHE B 230      41.694  -0.493  10.982  1.00 42.59           C  
ANISOU 1734  CD2 PHE B 230     7744   4166   4271     -6    386   -692       C  
ATOM   1735  CE1 PHE B 230      38.946  -0.667  11.177  1.00 42.17           C  
ANISOU 1735  CE1 PHE B 230     7672   4179   4172   -292    315   -664       C  
ATOM   1736  CE2 PHE B 230      40.948   0.640  11.262  1.00 39.05           C  
ANISOU 1736  CE2 PHE B 230     7209   3880   3747    -68    403   -643       C  
ATOM   1737  CZ  PHE B 230      39.571   0.551  11.360  1.00 40.34           C  
ANISOU 1737  CZ  PHE B 230     7361   4076   3891   -204    369   -632       C  
ATOM   1738  N   VAL B 231      42.979  -2.646   7.457  1.00 50.46           N  
ANISOU 1738  N   VAL B 231     8948   4914   5311    187    412  -1151       N  
ATOM   1739  CA  VAL B 231      43.201  -1.898   6.218  1.00 50.30           C  
ANISOU 1739  CA  VAL B 231     8896   5054   5161    236    467  -1255       C  
ATOM   1740  C   VAL B 231      42.277  -2.411   5.122  1.00 49.96           C  
ANISOU 1740  C   VAL B 231     8914   5015   5054    147    432  -1398       C  
ATOM   1741  O   VAL B 231      41.613  -1.633   4.426  1.00 50.36           O  
ANISOU 1741  O   VAL B 231     8925   5236   4975     91    430  -1411       O  
ATOM   1742  CB  VAL B 231      44.673  -1.974   5.780  1.00 50.84           C  
ANISOU 1742  CB  VAL B 231     8957   5108   5252    398    537  -1328       C  
ATOM   1743  CG1 VAL B 231      44.841  -1.286   4.434  1.00 49.46           C  
ANISOU 1743  CG1 VAL B 231     8756   5111   4926    429    596  -1434       C  
ATOM   1744  CG2 VAL B 231      45.559  -1.326   6.812  1.00 49.32           C  
ANISOU 1744  CG2 VAL B 231     8688   4946   5107    475    564  -1186       C  
ATOM   1745  N   GLY B 232      42.223  -3.735   4.956  1.00 48.96           N  
ANISOU 1745  N   GLY B 232     8882   4696   5024    130    398  -1505       N  
ATOM   1746  CA  GLY B 232      41.316  -4.314   3.976  1.00 50.59           C  
ANISOU 1746  CA  GLY B 232     9150   4894   5177     29    355  -1654       C  
ATOM   1747  C   GLY B 232      39.871  -3.905   4.201  1.00 51.91           C  
ANISOU 1747  C   GLY B 232     9281   5156   5287   -135    291  -1571       C  
ATOM   1748  O   GLY B 232      39.118  -3.693   3.247  1.00 51.81           O  
ANISOU 1748  O   GLY B 232     9264   5265   5157   -210    265  -1657       O  
ATOM   1749  N   ALA B 233      39.467  -3.789   5.467  1.00 47.34           N  
ANISOU 1749  N   ALA B 233     8667   4535   4784   -193    264  -1404       N  
ATOM   1750  CA  ALA B 233      38.115  -3.331   5.776  1.00 47.23           C  
ANISOU 1750  CA  ALA B 233     8597   4626   4724   -339    215  -1320       C  
ATOM   1751  C   ALA B 233      37.923  -1.868   5.388  1.00 44.70           C  
ANISOU 1751  C   ALA B 233     8172   4545   4267   -314    246  -1272       C  
ATOM   1752  O   ALA B 233      36.854  -1.486   4.897  1.00 44.67           O  
ANISOU 1752  O   ALA B 233     8125   4662   4186   -409    205  -1282       O  
ATOM   1753  CB  ALA B 233      37.814  -3.536   7.260  1.00 46.86           C  
ANISOU 1753  CB  ALA B 233     8531   4495   4778   -403    195  -1157       C  
ATOM   1754  N   LEU B 234      38.945  -1.035   5.606  1.00 44.10           N  
ANISOU 1754  N   LEU B 234     8049   4534   4172   -188    313  -1213       N  
ATOM   1755  CA  LEU B 234      38.854   0.376   5.236  1.00 44.68           C  
ANISOU 1755  CA  LEU B 234     8028   4810   4139   -158    342  -1158       C  
ATOM   1756  C   LEU B 234      38.757   0.562   3.727  1.00 45.37           C  
ANISOU 1756  C   LEU B 234     8128   5014   4097   -152    340  -1272       C  
ATOM   1757  O   LEU B 234      38.195   1.559   3.262  1.00 45.22           O  
ANISOU 1757  O   LEU B 234     8036   5159   3986   -177    328  -1224       O  
ATOM   1758  CB  LEU B 234      40.059   1.144   5.777  1.00 41.59           C  
ANISOU 1758  CB  LEU B 234     7590   4446   3768    -33    413  -1080       C  
ATOM   1759  CG  LEU B 234      40.148   1.305   7.293  1.00 42.89           C  
ANISOU 1759  CG  LEU B 234     7716   4558   4021    -42    416   -949       C  
ATOM   1760  CD1 LEU B 234      41.432   2.022   7.677  1.00 42.12           C  
ANISOU 1760  CD1 LEU B 234     7574   4494   3935     80    480   -897       C  
ATOM   1761  CD2 LEU B 234      38.935   2.049   7.815  1.00 41.14           C  
ANISOU 1761  CD2 LEU B 234     7415   4438   3779   -143    390   -865       C  
ATOM   1762  N   GLN B 235      39.303  -0.373   2.953  1.00 52.39           N  
ANISOU 1762  N   GLN B 235     9105   5824   4976   -117    350  -1423       N  
ATOM   1763  CA  GLN B 235      39.209  -0.344   1.502  1.00 53.95           C  
ANISOU 1763  CA  GLN B 235     9325   6143   5030   -124    348  -1553       C  
ATOM   1764  C   GLN B 235      37.905  -0.952   0.991  1.00 58.23           C  
ANISOU 1764  C   GLN B 235     9900   6691   5535   -271    257  -1633       C  
ATOM   1765  O   GLN B 235      37.818  -1.307  -0.190  1.00 60.46           O  
ANISOU 1765  O   GLN B 235    10227   7038   5706   -294    243  -1781       O  
ATOM   1766  CB  GLN B 235      40.417  -1.056   0.891  1.00 52.21           C  
ANISOU 1766  CB  GLN B 235     9176   5850   4810    -16    412  -1704       C  
ATOM   1767  CG  GLN B 235      41.741  -0.547   1.445  1.00 51.37           C  
ANISOU 1767  CG  GLN B 235     9028   5733   4758    125    497  -1626       C  
ATOM   1768  CD  GLN B 235      42.949  -1.184   0.790  1.00 53.64           C  
ANISOU 1768  CD  GLN B 235     9363   5971   5047    242    569  -1780       C  
ATOM   1769  OE1 GLN B 235      43.964  -0.523   0.561  1.00 53.68           O  
ANISOU 1769  OE1 GLN B 235     9316   6073   5007    345    649  -1757       O  
ATOM   1770  NE2 GLN B 235      42.846  -2.469   0.478  1.00 54.45           N  
ANISOU 1770  NE2 GLN B 235     9559   5919   5209    226    545  -1944       N  
ATOM   1771  N   ASP B 236      36.902  -1.081   1.865  1.00 62.63           N  
ANISOU 1771  N   ASP B 236    10428   7193   6175   -376    198  -1543       N  
ATOM   1772  CA  ASP B 236      35.572  -1.586   1.516  1.00 64.87           C  
ANISOU 1772  CA  ASP B 236    10719   7492   6438   -531    107  -1596       C  
ATOM   1773  C   ASP B 236      35.617  -3.049   1.076  1.00 66.32           C  
ANISOU 1773  C   ASP B 236    11023   7505   6671   -581     77  -1778       C  
ATOM   1774  O   ASP B 236      34.892  -3.460   0.170  1.00 68.05           O  
ANISOU 1774  O   ASP B 236    11268   7777   6813   -680     15  -1902       O  
ATOM   1775  CB  ASP B 236      34.903  -0.717   0.447  1.00 65.66           C  
ANISOU 1775  CB  ASP B 236    10750   7825   6372   -569     67  -1598       C  
ATOM   1776  CG  ASP B 236      33.397  -0.660   0.603  1.00 69.52           C  
ANISOU 1776  CG  ASP B 236    11172   8377   6867   -718    -25  -1548       C  
ATOM   1777  OD1 ASP B 236      32.888  -1.150   1.633  1.00 71.31           O  
ANISOU 1777  OD1 ASP B 236    11392   8481   7221   -791    -43  -1494       O  
ATOM   1778  OD2 ASP B 236      32.723  -0.124  -0.301  1.00 71.34           O  
ANISOU 1778  OD2 ASP B 236    11347   8787   6972   -765    -81  -1555       O  
ATOM   1779  N   GLY B 237      36.465  -3.839   1.727  1.00 66.96           N  
ANISOU 1779  N   GLY B 237    11174   7376   6890   -512    115  -1796       N  
ATOM   1780  CA  GLY B 237      36.532  -5.263   1.481  1.00 67.78           C  
ANISOU 1780  CA  GLY B 237    11394   7271   7090   -551     86  -1957       C  
ATOM   1781  C   GLY B 237      37.616  -5.722   0.534  1.00 68.09           C  
ANISOU 1781  C   GLY B 237    11506   7270   7094   -432    144  -2149       C  
ATOM   1782  O   GLY B 237      37.631  -6.903   0.169  1.00 70.97           O  
ANISOU 1782  O   GLY B 237    11968   7461   7537   -463    120  -2320       O  
ATOM   1783  N   VAL B 238      38.521  -4.840   0.130  1.00 56.33           N  
ANISOU 1783  N   VAL B 238     9970   5933   5501   -301    224  -2133       N  
ATOM   1784  CA  VAL B 238      39.591  -5.174  -0.807  1.00 56.81           C  
ANISOU 1784  CA  VAL B 238    10080   5996   5508   -183    296  -2317       C  
ATOM   1785  C   VAL B 238      40.841  -5.502   0.001  1.00 55.85           C  
ANISOU 1785  C   VAL B 238     9971   5701   5549    -32    363  -2276       C  
ATOM   1786  O   VAL B 238      41.318  -4.639   0.754  1.00 54.59           O  
ANISOU 1786  O   VAL B 238     9734   5602   5404     37    400  -2098       O  
ATOM   1787  CB  VAL B 238      39.861  -4.025  -1.788  1.00 55.57           C  
ANISOU 1787  CB  VAL B 238     9856   6125   5132   -140    347  -2315       C  
ATOM   1788  CG1 VAL B 238      40.890  -4.447  -2.826  1.00 55.23           C  
ANISOU 1788  CG1 VAL B 238     9862   6108   5014    -37    429  -2526       C  
ATOM   1789  CG2 VAL B 238      38.573  -3.589  -2.448  1.00 56.41           C  
ANISOU 1789  CG2 VAL B 238     9933   6413   5088   -286    263  -2306       C  
ATOM   1790  N   PRO B 239      41.398  -6.705  -0.120  1.00 57.45           N  
ANISOU 1790  N   PRO B 239    10260   5687   5882     23    376  -2436       N  
ATOM   1791  CA  PRO B 239      42.626  -7.022   0.616  1.00 58.56           C  
ANISOU 1791  CA  PRO B 239    10399   5666   6184    180    431  -2390       C  
ATOM   1792  C   PRO B 239      43.792  -6.170   0.140  1.00 58.91           C  
ANISOU 1792  C   PRO B 239    10372   5890   6123    330    539  -2400       C  
ATOM   1793  O   PRO B 239      43.848  -5.740  -1.015  1.00 60.23           O  
ANISOU 1793  O   PRO B 239    10525   6253   6106    331    584  -2520       O  
ATOM   1794  CB  PRO B 239      42.858  -8.507   0.306  1.00 59.58           C  
ANISOU 1794  CB  PRO B 239    10637   5533   6468    204    418  -2599       C  
ATOM   1795  CG  PRO B 239      41.550  -9.014  -0.224  1.00 60.41           C  
ANISOU 1795  CG  PRO B 239    10805   5623   6525     21    333  -2706       C  
ATOM   1796  CD  PRO B 239      40.913  -7.849  -0.909  1.00 58.90           C  
ANISOU 1796  CD  PRO B 239    10543   5750   6085    -55    333  -2669       C  
ATOM   1797  N   MET B 240      44.725  -5.922   1.050  1.00 65.64           N  
ANISOU 1797  N   MET B 240    11173   6684   7085    447    576  -2264       N  
ATOM   1798  CA  MET B 240      45.967  -5.240   0.729  1.00 66.29           C  
ANISOU 1798  CA  MET B 240    11179   6902   7106    594    680  -2270       C  
ATOM   1799  C   MET B 240      47.095  -6.256   0.591  1.00 67.60           C  
ANISOU 1799  C   MET B 240    11376   6888   7420    746    733  -2423       C  
ATOM   1800  O   MET B 240      47.034  -7.364   1.129  1.00 68.67           O  
ANISOU 1800  O   MET B 240    11581   6762   7748    755    680  -2452       O  
ATOM   1801  CB  MET B 240      46.318  -4.203   1.800  1.00 65.55           C  
ANISOU 1801  CB  MET B 240    10989   6883   7032    625    687  -2026       C  
ATOM   1802  CG  MET B 240      46.630  -4.798   3.164  1.00 66.35           C  
ANISOU 1802  CG  MET B 240    11100   6769   7340    663    641  -1900       C  
ATOM   1803  SD  MET B 240      47.507  -3.645   4.238  1.00 66.71           S  
ANISOU 1803  SD  MET B 240    11025   6924   7399    742    675  -1677       S  
ATOM   1804  CE  MET B 240      48.938  -3.264   3.230  1.00 66.26           C  
ANISOU 1804  CE  MET B 240    10901   6999   7277    904    799  -1804       C  
ATOM   1805  N   ASP B 241      48.129  -5.865  -0.146  1.00 71.62           N  
ANISOU 1805  N   ASP B 241    11828   7539   7845    867    841  -2518       N  
ATOM   1806  CA  ASP B 241      49.270  -6.734  -0.395  1.00 71.38           C  
ANISOU 1806  CA  ASP B 241    11804   7371   7946   1030    910  -2684       C  
ATOM   1807  C   ASP B 241      50.338  -6.511   0.668  1.00 70.69           C  
ANISOU 1807  C   ASP B 241    11631   7218   8009   1162    929  -2517       C  
ATOM   1808  O   ASP B 241      50.724  -5.370   0.941  1.00 70.79           O  
ANISOU 1808  O   ASP B 241    11547   7418   7932   1175    965  -2363       O  
ATOM   1809  CB  ASP B 241      49.850  -6.480  -1.787  1.00 70.82           C  
ANISOU 1809  CB  ASP B 241    11691   7516   7703   1084   1023  -2883       C  
ATOM   1810  CG  ASP B 241      48.900  -6.883  -2.896  1.00 75.08           C  
ANISOU 1810  CG  ASP B 241    12268   8139   8120    950    986  -3058       C  
ATOM   1811  OD1 ASP B 241      47.966  -7.666  -2.627  1.00 76.93           O  
ANISOU 1811  OD1 ASP B 241    12604   8183   8441    854    891  -3095       O  
ATOM   1812  OD2 ASP B 241      49.090  -6.417  -4.040  1.00 76.79           O  
ANISOU 1812  OD2 ASP B 241    12409   8617   8150    935   1049  -3154       O  
ATOM   1813  N   ILE B 242      50.808  -7.604   1.267  1.00 59.55           N  
ANISOU 1813  N   ILE B 242    10571   5743   6313   1137    998  -2744       N  
ATOM   1814  CA  ILE B 242      51.883  -7.570   2.247  1.00 60.56           C  
ANISOU 1814  CA  ILE B 242    10617   5826   6566   1255   1035  -2640       C  
ATOM   1815  C   ILE B 242      52.980  -8.524   1.791  1.00 63.16           C  
ANISOU 1815  C   ILE B 242    10961   6092   6944   1433   1098  -2777       C  
ATOM   1816  O   ILE B 242      52.793  -9.339   0.888  1.00 65.73           O  
ANISOU 1816  O   ILE B 242    11333   6393   7249   1436   1086  -2927       O  
ATOM   1817  CB  ILE B 242      51.402  -7.934   3.667  1.00 58.96           C  
ANISOU 1817  CB  ILE B 242    10441   5438   6523   1189    944  -2512       C  
ATOM   1818  CG1 ILE B 242      50.829  -9.350   3.687  1.00 61.05           C  
ANISOU 1818  CG1 ILE B 242    10868   5456   6874   1172    877  -2631       C  
ATOM   1819  CG2 ILE B 242      50.373  -6.926   4.159  1.00 57.51           C  
ANISOU 1819  CG2 ILE B 242    10206   5344   6302   1015    885  -2363       C  
ATOM   1820  CD1 ILE B 242      50.460  -9.832   5.065  1.00 60.39           C  
ANISOU 1820  CD1 ILE B 242    10817   5178   6950   1122    798  -2506       C  
ATOM   1821  N   VAL B 243      54.142  -8.408   2.434  1.00 59.29           N  
ANISOU 1821  N   VAL B 243    10397   5596   6533   1575   1156  -2712       N  
ATOM   1822  CA  VAL B 243      55.298  -9.221   2.078  1.00 61.23           C  
ANISOU 1822  CA  VAL B 243    10607   5812   6844   1748   1216  -2814       C  
ATOM   1823  C   VAL B 243      56.174  -9.385   3.311  1.00 60.89           C  
ANISOU 1823  C   VAL B 243    10522   5661   6954   1867   1217  -2708       C  
ATOM   1824  O   VAL B 243      56.289  -8.479   4.141  1.00 59.14           O  
ANISOU 1824  O   VAL B 243    10203   5515   6753   1825   1207  -2539       O  
ATOM   1825  CB  VAL B 243      56.084  -8.600   0.895  1.00 61.90           C  
ANISOU 1825  CB  VAL B 243    10594   6140   6787   1825   1335  -2885       C  
ATOM   1826  CG1 VAL B 243      56.631  -7.228   1.266  1.00 60.19           C  
ANISOU 1826  CG1 VAL B 243    10256   6099   6514   1840   1402  -2738       C  
ATOM   1827  CG2 VAL B 243      57.201  -9.529   0.435  1.00 64.17           C  
ANISOU 1827  CG2 VAL B 243    10844   6397   7140   1996   1398  -3009       C  
ATOM   1828  N   LYS B 244      56.782 -10.562   3.435  1.00 77.45           N  
ANISOU 1828  N   LYS B 244    12638   7608   9180   1984   1208  -2781       N  
ATOM   1829  CA  LYS B 244      57.686 -10.823   4.544  1.00 77.96           C  
ANISOU 1829  CA  LYS B 244    12656   7571   9393   2113   1204  -2687       C  
ATOM   1830  C   LYS B 244      58.906  -9.914   4.463  1.00 78.84           C  
ANISOU 1830  C   LYS B 244    12618   7879   9460   2240   1311  -2641       C  
ATOM   1831  O   LYS B 244      59.403  -9.609   3.374  1.00 79.55           O  
ANISOU 1831  O   LYS B 244    12638   8143   9444   2288   1404  -2732       O  
ATOM   1832  CB  LYS B 244      58.124 -12.287   4.537  1.00 79.50           C  
ANISOU 1832  CB  LYS B 244    12898   7580   9731   2219   1180  -2786       C  
ATOM   1833  CG  LYS B 244      58.589 -12.808   5.886  1.00 80.71           C  
ANISOU 1833  CG  LYS B 244    13052   7556  10059   2301   1124  -2669       C  
ATOM   1834  CD  LYS B 244      59.130 -14.224   5.770  1.00 85.50           C  
ANISOU 1834  CD  LYS B 244    13693   7992  10803   2419   1112  -2772       C  
ATOM   1835  CE  LYS B 244      58.017 -15.225   5.504  1.00 88.24           C  
ANISOU 1835  CE  LYS B 244    14183   8158  11187   2298   1032  -2856       C  
ATOM   1836  NZ  LYS B 244      57.190 -15.474   6.720  1.00 88.05           N  
ANISOU 1836  NZ  LYS B 244    14242   7953  11259   2189    925  -2714       N  
ATOM   1837  N   SER B 245      59.382  -9.472   5.623  1.00 75.06           N  
ANISOU 1837  N   SER B 245    12044   7401   9076   2263   1283  -2476       N  
ATOM   1838  CA  SER B 245      60.615  -8.704   5.669  1.00 75.26           C  
ANISOU 1838  CA  SER B 245    11887   7610   9098   2368   1364  -2413       C  
ATOM   1839  C   SER B 245      61.801  -9.595   5.311  1.00 76.96           C  
ANISOU 1839  C   SER B 245    12086   7774   9381   2592   1436  -2537       C  
ATOM   1840  O   SER B 245      61.723 -10.826   5.349  1.00 79.28           O  
ANISOU 1840  O   SER B 245    12474   7877   9771   2643   1390  -2621       O  
ATOM   1841  CB  SER B 245      60.811  -8.082   7.052  1.00 74.86           C  
ANISOU 1841  CB  SER B 245    11737   7565   9140   2329   1300  -2211       C  
ATOM   1842  OG  SER B 245      61.132  -9.067   8.018  1.00 75.23           O  
ANISOU 1842  OG  SER B 245    11835   7405   9344   2428   1235  -2183       O  
ATOM   1843  N   ASP B 246      62.914  -8.953   4.954  1.00 81.02           N  
ANISOU 1843  N   ASP B 246    12436   8485   9862   2692   1537  -2527       N  
ATOM   1844  CA  ASP B 246      64.074  -9.700   4.477  1.00 83.61           C  
ANISOU 1844  CA  ASP B 246    12706   8814  10247   2887   1613  -2642       C  
ATOM   1845  C   ASP B 246      64.711 -10.518   5.595  1.00 84.01           C  
ANISOU 1845  C   ASP B 246    12745   8686  10490   3013   1548  -2585       C  
ATOM   1846  O   ASP B 246      65.032 -11.697   5.408  1.00 85.57           O  
ANISOU 1846  O   ASP B 246    12979   8749  10783   3102   1535  -2682       O  
ATOM   1847  CB  ASP B 246      65.097  -8.743   3.863  1.00 83.95           C  
ANISOU 1847  CB  ASP B 246    12572   9120  10205   2962   1745  -2635       C  
ATOM   1848  CG  ASP B 246      64.913  -8.575   2.368  1.00 84.72           C  
ANISOU 1848  CG  ASP B 246    12672   9375  10142   2913   1835  -2764       C  
ATOM   1849  OD1 ASP B 246      63.854  -8.983   1.846  1.00 84.93           O  
ANISOU 1849  OD1 ASP B 246    12838   9327  10105   2799   1785  -2844       O  
ATOM   1850  OD2 ASP B 246      65.831  -8.037   1.713  1.00 85.11           O  
ANISOU 1850  OD2 ASP B 246    12579   9630  10130   2985   1953  -2780       O  
ATOM   1851  N   LEU B 247      64.893  -9.913   6.767  1.00 84.38           N  
ANISOU 1851  N   LEU B 247    12723   8737  10602   3001   1495  -2415       N  
ATOM   1852  CA  LEU B 247      65.664 -10.533   7.838  1.00 85.21           C  
ANISOU 1852  CA  LEU B 247    12791   8710  10875   3142   1440  -2346       C  
ATOM   1853  C   LEU B 247      64.816 -11.252   8.876  1.00 84.54           C  
ANISOU 1853  C   LEU B 247    12856   8376  10888   3075   1307  -2273       C  
ATOM   1854  O   LEU B 247      65.298 -12.208   9.491  1.00 86.42           O  
ANISOU 1854  O   LEU B 247    13115   8452  11268   3193   1256  -2262       O  
ATOM   1855  CB  LEU B 247      66.522  -9.480   8.548  1.00 84.21           C  
ANISOU 1855  CB  LEU B 247    12456   8763  10778   3152   1447  -2188       C  
ATOM   1856  CG  LEU B 247      67.379  -8.593   7.645  1.00 84.13           C  
ANISOU 1856  CG  LEU B 247    12271   9018  10677   3192   1578  -2223       C  
ATOM   1857  CD1 LEU B 247      68.035  -7.483   8.449  1.00 82.24           C  
ANISOU 1857  CD1 LEU B 247    11838   8937  10473   3159   1563  -2053       C  
ATOM   1858  CD2 LEU B 247      68.424  -9.428   6.927  1.00 86.59           C  
ANISOU 1858  CD2 LEU B 247    12549   9324  11026   3416   1676  -2376       C  
ATOM   1859  N   TYR B 248      63.574 -10.828   9.091  1.00 89.99           N  
ANISOU 1859  N   TYR B 248    13630   9049  11515   2869   1242  -2207       N  
ATOM   1860  CA  TYR B 248      62.767 -11.321  10.200  1.00 90.61           C  
ANISOU 1860  CA  TYR B 248    13824   8925  11680   2785   1120  -2103       C  
ATOM   1861  C   TYR B 248      61.522 -12.008   9.658  1.00 92.59           C  
ANISOU 1861  C   TYR B 248    14268   9022  11891   2672   1087  -2207       C  
ATOM   1862  O   TYR B 248      60.735 -11.396   8.927  1.00 93.00           O  
ANISOU 1862  O   TYR B 248    14338   9186  11813   2530   1111  -2246       O  
ATOM   1863  CB  TYR B 248      62.422 -10.176  11.151  1.00 89.98           C  
ANISOU 1863  CB  TYR B 248    13653   8960  11575   2640   1064  -1911       C  
ATOM   1864  CG  TYR B 248      63.669  -9.471  11.633  1.00 92.05           C  
ANISOU 1864  CG  TYR B 248    13720   9379  11876   2743   1092  -1820       C  
ATOM   1865  CD1 TYR B 248      64.620 -10.150  12.383  1.00 93.73           C  
ANISOU 1865  CD1 TYR B 248    13896   9493  12224   2914   1060  -1784       C  
ATOM   1866  CD2 TYR B 248      63.917  -8.143  11.308  1.00 92.40           C  
ANISOU 1866  CD2 TYR B 248    13615   9668  11825   2673   1149  -1773       C  
ATOM   1867  CE1 TYR B 248      65.771  -9.524  12.817  1.00 94.74           C  
ANISOU 1867  CE1 TYR B 248    13837   9770  12391   3008   1080  -1705       C  
ATOM   1868  CE2 TYR B 248      65.069  -7.506  11.737  1.00 93.22           C  
ANISOU 1868  CE2 TYR B 248    13536   9913  11972   2759   1172  -1694       C  
ATOM   1869  CZ  TYR B 248      65.992  -8.203  12.492  1.00 94.77           C  
ANISOU 1869  CZ  TYR B 248    13692  10016  12302   2925   1136  -1663       C  
ATOM   1870  OH  TYR B 248      67.140  -7.579  12.924  1.00 95.86           O  
ANISOU 1870  OH  TYR B 248    13639  10298  12486   3008   1151  -1587       O  
ATOM   1871  N   ASP B 249      61.349 -13.279  10.030  1.00 94.42           N  
ANISOU 1871  N   ASP B 249    14605   9024  12248   2703   1019  -2230       N  
ATOM   1872  CA  ASP B 249      60.330 -14.121   9.414  1.00 95.81           C  
ANISOU 1872  CA  ASP B 249    14917   9070  12418   2588    982  -2337       C  
ATOM   1873  C   ASP B 249      58.925 -13.774   9.892  1.00 93.18           C  
ANISOU 1873  C   ASP B 249    14687   8678  12038   2383    907  -2251       C  
ATOM   1874  O   ASP B 249      57.950 -14.026   9.174  1.00 94.53           O  
ANISOU 1874  O   ASP B 249    14945   8822  12151   2253    892  -2342       O  
ATOM   1875  CB  ASP B 249      60.638 -15.590   9.704  1.00 99.55           C  
ANISOU 1875  CB  ASP B 249    15449   9320  13057   2677    934  -2375       C  
ATOM   1876  CG  ASP B 249      60.218 -16.510   8.578  1.00103.11           C  
ANISOU 1876  CG  ASP B 249    15982   9697  13500   2646    948  -2560       C  
ATOM   1877  OD1 ASP B 249      59.007 -16.577   8.283  1.00103.30           O  
ANISOU 1877  OD1 ASP B 249    16107   9673  13470   2476    905  -2591       O  
ATOM   1878  OD2 ASP B 249      61.100 -17.168   7.989  1.00106.24           O  
ANISOU 1878  OD2 ASP B 249    16337  10084  13947   2790   1003  -2676       O  
ATOM   1879  N   HIS B 250      58.797 -13.205  11.087  1.00 75.67           N  
ANISOU 1879  N   HIS B 250    12459   6445   9847   2350    858  -2079       N  
ATOM   1880  CA  HIS B 250      57.497 -12.934  11.685  1.00 72.75           C  
ANISOU 1880  CA  HIS B 250    12159   6030   9454   2145    782  -1973       C  
ATOM   1881  C   HIS B 250      57.001 -11.516  11.430  1.00 71.55           C  
ANISOU 1881  C   HIS B 250    11902   6121   9162   1998    806  -1914       C  
ATOM   1882  O   HIS B 250      55.890 -11.179  11.851  1.00 70.68           O  
ANISOU 1882  O   HIS B 250    11831   6002   9021   1824    749  -1831       O  
ATOM   1883  CB  HIS B 250      57.546 -13.200  13.194  1.00 72.54           C  
ANISOU 1883  CB  HIS B 250    12141   5878   9545   2151    698  -1794       C  
ATOM   1884  CG  HIS B 250      58.576 -12.389  13.919  1.00 75.31           C  
ANISOU 1884  CG  HIS B 250    12324   6382   9908   2240    710  -1669       C  
ATOM   1885  ND1 HIS B 250      59.927 -12.507  13.672  1.00 76.87           N  
ANISOU 1885  ND1 HIS B 250    12427   6632  10147   2438    766  -1720       N  
ATOM   1886  CD2 HIS B 250      58.451 -11.447  14.884  1.00 75.24           C  
ANISOU 1886  CD2 HIS B 250    12224   6487   9878   2157    672  -1500       C  
ATOM   1887  CE1 HIS B 250      60.590 -11.673  14.453  1.00 76.69           C  
ANISOU 1887  CE1 HIS B 250    12258   6750  10131   2467    756  -1586       C  
ATOM   1888  NE2 HIS B 250      59.717 -11.017  15.198  1.00 75.50           N  
ANISOU 1888  NE2 HIS B 250    12112   6636   9941   2299    698  -1454       N  
ATOM   1889  N   LEU B 251      57.787 -10.684  10.753  1.00 63.00           N  
ANISOU 1889  N   LEU B 251    10687   5253   7998   2063    891  -1951       N  
ATOM   1890  CA  LEU B 251      57.424  -9.301  10.475  1.00 62.13           C  
ANISOU 1890  CA  LEU B 251    10473   5373   7761   1937    918  -1891       C  
ATOM   1891  C   LEU B 251      57.046  -9.154   9.008  1.00 61.79           C  
ANISOU 1891  C   LEU B 251    10463   5428   7586   1896    982  -2047       C  
ATOM   1892  O   LEU B 251      57.824  -9.520   8.121  1.00 62.28           O  
ANISOU 1892  O   LEU B 251    10515   5522   7627   2029   1059  -2181       O  
ATOM   1893  CB  LEU B 251      58.576  -8.352  10.816  1.00 62.52           C  
ANISOU 1893  CB  LEU B 251    10339   5604   7810   2023    964  -1801       C  
ATOM   1894  CG  LEU B 251      58.920  -8.208  12.300  1.00 63.03           C  
ANISOU 1894  CG  LEU B 251    10349   5624   7978   2042    894  -1631       C  
ATOM   1895  CD1 LEU B 251      59.992  -7.151  12.496  1.00 62.26           C  
ANISOU 1895  CD1 LEU B 251    10063   5728   7867   2105    939  -1556       C  
ATOM   1896  CD2 LEU B 251      57.680  -7.873  13.116  1.00 62.17           C  
ANISOU 1896  CD2 LEU B 251    10298   5470   7853   1860    810  -1511       C  
ATOM   1897  N   TYR B 252      55.857  -8.612   8.758  1.00 62.37           N  
ANISOU 1897  N   TYR B 252    10574   5557   7568   1717    951  -2027       N  
ATOM   1898  CA  TYR B 252      55.357  -8.395   7.408  1.00 62.57           C  
ANISOU 1898  CA  TYR B 252    10634   5686   7455   1658    996  -2159       C  
ATOM   1899  C   TYR B 252      55.131  -6.908   7.186  1.00 62.37           C  
ANISOU 1899  C   TYR B 252    10490   5898   7310   1555   1024  -2068       C  
ATOM   1900  O   TYR B 252      54.562  -6.226   8.045  1.00 62.28           O  
ANISOU 1900  O   TYR B 252    10440   5911   7312   1442    968  -1923       O  
ATOM   1901  CB  TYR B 252      54.064  -9.175   7.166  1.00 62.43           C  
ANISOU 1901  CB  TYR B 252    10777   5511   7433   1535    926  -2236       C  
ATOM   1902  CG  TYR B 252      54.291 -10.646   6.918  1.00 63.57           C  
ANISOU 1902  CG  TYR B 252    11053   5436   7665   1640    917  -2381       C  
ATOM   1903  CD1 TYR B 252      54.523 -11.519   7.972  1.00 64.42           C  
ANISOU 1903  CD1 TYR B 252    11214   5331   7931   1701    863  -2319       C  
ATOM   1904  CD2 TYR B 252      54.283 -11.162   5.629  1.00 65.66           C  
ANISOU 1904  CD2 TYR B 252    11367   5719   7860   1671    956  -2568       C  
ATOM   1905  CE1 TYR B 252      54.735 -12.865   7.750  1.00 66.71           C  
ANISOU 1905  CE1 TYR B 252    11577   5444   8325   1775    841  -2426       C  
ATOM   1906  CE2 TYR B 252      54.495 -12.507   5.397  1.00 67.99           C  
ANISOU 1906  CE2 TYR B 252    11717   5853   8262   1737    931  -2677       C  
ATOM   1907  CZ  TYR B 252      54.721 -13.354   6.462  1.00 68.05           C  
ANISOU 1907  CZ  TYR B 252    11763   5653   8439   1788    875  -2604       C  
ATOM   1908  OH  TYR B 252      54.932 -14.695   6.240  1.00 70.68           O  
ANISOU 1908  OH  TYR B 252    12151   5817   8886   1853    852  -2709       O  
ATOM   1909  N   VAL B 253      55.576  -6.416   6.035  1.00 69.58           N  
ANISOU 1909  N   VAL B 253    11348   6983   8105   1596   1112  -2154       N  
ATOM   1910  CA  VAL B 253      55.467  -5.002   5.689  1.00 69.61           C  
ANISOU 1910  CA  VAL B 253    11240   7215   7993   1511   1149  -2072       C  
ATOM   1911  C   VAL B 253      54.496  -4.852   4.524  1.00 69.04           C  
ANISOU 1911  C   VAL B 253    11242   7215   7774   1406   1153  -2170       C  
ATOM   1912  O   VAL B 253      54.238  -5.828   3.802  1.00 69.60           O  
ANISOU 1912  O   VAL B 253    11430   7191   7822   1435   1153  -2327       O  
ATOM   1913  CB  VAL B 253      56.841  -4.409   5.340  1.00 69.56           C  
ANISOU 1913  CB  VAL B 253    11089   7374   7964   1639   1254  -2064       C  
ATOM   1914  CG1 VAL B 253      57.774  -4.495   6.536  1.00 69.99           C  
ANISOU 1914  CG1 VAL B 253    11060   7370   8164   1735   1237  -1960       C  
ATOM   1915  CG2 VAL B 253      57.439  -5.126   4.138  1.00 68.91           C  
ANISOU 1915  CG2 VAL B 253    11047   7311   7825   1766   1341  -2246       C  
ATOM   1916  N   PRO B 254      53.920  -3.669   4.314  1.00 58.02           N  
ANISOU 1916  N   PRO B 254     9786   5980   6278   1285   1150  -2085       N  
ATOM   1917  CA  PRO B 254      53.158  -3.440   3.083  1.00 57.24           C  
ANISOU 1917  CA  PRO B 254     9741   5984   6024   1205   1162  -2177       C  
ATOM   1918  C   PRO B 254      54.066  -3.551   1.868  1.00 59.07           C  
ANISOU 1918  C   PRO B 254     9952   6333   6157   1327   1273  -2305       C  
ATOM   1919  O   PRO B 254      55.185  -3.034   1.856  1.00 59.97           O  
ANISOU 1919  O   PRO B 254     9948   6560   6276   1423   1356  -2260       O  
ATOM   1920  CB  PRO B 254      52.612  -2.019   3.258  1.00 56.00           C  
ANISOU 1920  CB  PRO B 254     9495   5983   5799   1078   1145  -2029       C  
ATOM   1921  CG  PRO B 254      52.634  -1.780   4.734  1.00 53.00           C  
ANISOU 1921  CG  PRO B 254     9065   5520   5554   1053   1087  -1878       C  
ATOM   1922  CD  PRO B 254      53.830  -2.527   5.240  1.00 56.91           C  
ANISOU 1922  CD  PRO B 254     9538   5920   6166   1208   1121  -1901       C  
ATOM   1923  N   ALA B 255      53.573  -4.244   0.839  1.00 63.52           N  
ANISOU 1923  N   ALA B 255    10632   6872   6632   1322   1273  -2470       N  
ATOM   1924  CA  ALA B 255      54.398  -4.504  -0.335  1.00 64.87           C  
ANISOU 1924  CA  ALA B 255    10801   7143   6702   1447   1380  -2614       C  
ATOM   1925  C   ALA B 255      54.748  -3.223  -1.082  1.00 65.44           C  
ANISOU 1925  C   ALA B 255    10760   7476   6627   1430   1465  -2549       C  
ATOM   1926  O   ALA B 255      55.799  -3.156  -1.731  1.00 67.63           O  
ANISOU 1926  O   ALA B 255    10975   7869   6851   1552   1577  -2604       O  
ATOM   1927  CB  ALA B 255      53.689  -5.488  -1.265  1.00 65.11           C  
ANISOU 1927  CB  ALA B 255    10980   7097   6663   1427   1346  -2804       C  
ATOM   1928  N   GLY B 256      53.900  -2.204  -1.002  1.00 71.15           N  
ANISOU 1928  N   GLY B 256    11452   8293   7287   1283   1417  -2430       N  
ATOM   1929  CA  GLY B 256      54.108  -0.976  -1.737  1.00 73.18           C  
ANISOU 1929  CA  GLY B 256    11616   8785   7403   1252   1488  -2360       C  
ATOM   1930  C   GLY B 256      54.795   0.140  -0.981  1.00 73.50           C  
ANISOU 1930  C   GLY B 256    11501   8915   7508   1250   1521  -2177       C  
ATOM   1931  O   GLY B 256      54.846   1.265  -1.489  1.00 74.04           O  
ANISOU 1931  O   GLY B 256    11494   9166   7473   1201   1567  -2094       O  
ATOM   1932  N   SER B 257      55.323  -0.132   0.212  1.00 63.12           N  
ANISOU 1932  N   SER B 257    10141   7479   6362   1300   1495  -2111       N  
ATOM   1933  CA  SER B 257      55.978   0.905   0.999  1.00 62.37           C  
ANISOU 1933  CA  SER B 257     9899   7461   6336   1295   1514  -1944       C  
ATOM   1934  C   SER B 257      57.161   1.495   0.241  1.00 63.11           C  
ANISOU 1934  C   SER B 257     9876   7742   6362   1382   1646  -1941       C  
ATOM   1935  O   SER B 257      57.875   0.790  -0.479  1.00 64.39           O  
ANISOU 1935  O   SER B 257    10052   7925   6489   1504   1728  -2070       O  
ATOM   1936  CB  SER B 257      56.440   0.341   2.344  1.00 62.32           C  
ANISOU 1936  CB  SER B 257     9873   7292   6515   1355   1465  -1896       C  
ATOM   1937  OG  SER B 257      55.346  -0.136   3.110  1.00 60.88           O  
ANISOU 1937  OG  SER B 257     9790   6944   6396   1265   1349  -1878       O  
ATOM   1938  N   GLU B 258      57.361   2.804   0.402  1.00 54.57           N  
ANISOU 1938  N   GLU B 258     8676   6796   5260   1316   1668  -1794       N  
ATOM   1939  CA  GLU B 258      58.455   3.475  -0.293  1.00 54.81           C  
ANISOU 1939  CA  GLU B 258     8584   7012   5228   1378   1794  -1769       C  
ATOM   1940  C   GLU B 258      59.806   3.047   0.267  1.00 55.80           C  
ANISOU 1940  C   GLU B 258     8610   7109   5485   1519   1849  -1776       C  
ATOM   1941  O   GLU B 258      60.734   2.743  -0.490  1.00 56.86           O  
ANISOU 1941  O   GLU B 258     8698   7332   5575   1634   1961  -1858       O  
ATOM   1942  CB  GLU B 258      58.290   4.991  -0.195  1.00 52.26           C  
ANISOU 1942  CB  GLU B 258     8165   6821   4869   1263   1794  -1601       C  
ATOM   1943  CG  GLU B 258      57.153   5.549  -1.031  1.00 51.83           C  
ANISOU 1943  CG  GLU B 258     8187   6847   4660   1145   1768  -1593       C  
ATOM   1944  CD  GLU B 258      57.455   5.518  -2.513  1.00 54.40           C  
ANISOU 1944  CD  GLU B 258     8528   7330   4812   1191   1877  -1682       C  
ATOM   1945  OE1 GLU B 258      58.633   5.704  -2.886  1.00 55.75           O  
ANISOU 1945  OE1 GLU B 258     8596   7612   4973   1278   1993  -1679       O  
ATOM   1946  OE2 GLU B 258      56.515   5.306  -3.306  1.00 55.34           O  
ANISOU 1946  OE2 GLU B 258     8758   7468   4800   1139   1846  -1755       O  
ATOM   1947  N   VAL B 259      59.935   3.022   1.591  1.00 54.48           N  
ANISOU 1947  N   VAL B 259     8403   6823   5473   1515   1771  -1690       N  
ATOM   1948  CA  VAL B 259      61.186   2.677   2.257  1.00 56.21           C  
ANISOU 1948  CA  VAL B 259     8518   7013   5827   1644   1804  -1679       C  
ATOM   1949  C   VAL B 259      60.873   1.754   3.426  1.00 56.25           C  
ANISOU 1949  C   VAL B 259     8600   6802   5972   1670   1694  -1686       C  
ATOM   1950  O   VAL B 259      59.921   1.990   4.176  1.00 55.51           O  
ANISOU 1950  O   VAL B 259     8562   6623   5908   1557   1590  -1610       O  
ATOM   1951  CB  VAL B 259      61.939   3.937   2.741  1.00 56.96           C  
ANISOU 1951  CB  VAL B 259     8439   7235   5970   1608   1831  -1524       C  
ATOM   1952  CG1 VAL B 259      63.132   3.555   3.595  1.00 56.62           C  
ANISOU 1952  CG1 VAL B 259     8287   7148   6079   1731   1838  -1505       C  
ATOM   1953  CG2 VAL B 259      62.385   4.783   1.561  1.00 58.64           C  
ANISOU 1953  CG2 VAL B 259     8569   7659   6052   1593   1953  -1511       C  
ATOM   1954  N   VAL B 260      61.668   0.699   3.579  1.00 60.15           N  
ANISOU 1954  N   VAL B 260     9096   7208   6552   1822   1718  -1774       N  
ATOM   1955  CA  VAL B 260      61.550  -0.216   4.709  1.00 60.11           C  
ANISOU 1955  CA  VAL B 260     9154   6996   6689   1866   1622  -1770       C  
ATOM   1956  C   VAL B 260      62.887  -0.243   5.436  1.00 60.23           C  
ANISOU 1956  C   VAL B 260     9027   7024   6831   1992   1645  -1717       C  
ATOM   1957  O   VAL B 260      63.918  -0.580   4.840  1.00 62.23           O  
ANISOU 1957  O   VAL B 260     9211   7346   7087   2129   1743  -1796       O  
ATOM   1958  CB  VAL B 260      61.136  -1.630   4.271  1.00 61.25           C  
ANISOU 1958  CB  VAL B 260     9459   6981   6831   1934   1608  -1932       C  
ATOM   1959  CG1 VAL B 260      60.938  -2.523   5.489  1.00 61.07           C  
ANISOU 1959  CG1 VAL B 260     9508   6737   6958   1964   1502  -1905       C  
ATOM   1960  CG2 VAL B 260      59.870  -1.579   3.430  1.00 60.70           C  
ANISOU 1960  CG2 VAL B 260     9517   6921   6625   1810   1588  -1995       C  
ATOM   1961  N   LEU B 261      62.869   0.119   6.715  1.00 55.11           N  
ANISOU 1961  N   LEU B 261     8334   6319   6286   1948   1556  -1588       N  
ATOM   1962  CA  LEU B 261      64.029   0.035   7.591  1.00 57.03           C  
ANISOU 1962  CA  LEU B 261     8452   6554   6661   2060   1548  -1529       C  
ATOM   1963  C   LEU B 261      63.829  -1.174   8.494  1.00 57.07           C  
ANISOU 1963  C   LEU B 261     8564   6339   6780   2130   1456  -1551       C  
ATOM   1964  O   LEU B 261      63.015  -1.134   9.420  1.00 57.73           O  
ANISOU 1964  O   LEU B 261     8718   6319   6899   2035   1351  -1469       O  
ATOM   1965  CB  LEU B 261      64.182   1.305   8.423  1.00 56.40           C  
ANISOU 1965  CB  LEU B 261     8248   6569   6614   1962   1506  -1369       C  
ATOM   1966  CG  LEU B 261      64.002   2.649   7.717  1.00 56.54           C  
ANISOU 1966  CG  LEU B 261     8191   6769   6521   1842   1565  -1314       C  
ATOM   1967  CD1 LEU B 261      64.173   3.797   8.699  1.00 53.24           C  
ANISOU 1967  CD1 LEU B 261     7661   6408   6160   1755   1507  -1163       C  
ATOM   1968  CD2 LEU B 261      64.986   2.773   6.569  1.00 57.63           C  
ANISOU 1968  CD2 LEU B 261     8228   7065   6603   1929   1705  -1381       C  
ATOM   1969  N   GLU B 262      64.546  -2.253   8.216  1.00 69.04           N  
ANISOU 1969  N   GLU B 262    10098   7783   8352   2295   1497  -1658       N  
ATOM   1970  CA  GLU B 262      64.487  -3.441   9.052  1.00 70.67           C  
ANISOU 1970  CA  GLU B 262    10401   7772   8677   2379   1414  -1674       C  
ATOM   1971  C   GLU B 262      65.570  -3.330  10.114  1.00 71.07           C  
ANISOU 1971  C   GLU B 262    10315   7833   8855   2478   1380  -1575       C  
ATOM   1972  O   GLU B 262      66.732  -3.074   9.787  1.00 73.40           O  
ANISOU 1972  O   GLU B 262    10460   8258   9171   2585   1460  -1590       O  
ATOM   1973  CB  GLU B 262      64.676  -4.697   8.205  1.00 72.18           C  
ANISOU 1973  CB  GLU B 262    10692   7864   8870   2514   1469  -1848       C  
ATOM   1974  CG  GLU B 262      63.674  -4.799   7.064  1.00 73.49           C  
ANISOU 1974  CG  GLU B 262    10987   8037   8899   2422   1503  -1960       C  
ATOM   1975  CD  GLU B 262      63.640  -6.175   6.436  1.00 74.85           C  
ANISOU 1975  CD  GLU B 262    11296   8058   9087   2538   1524  -2135       C  
ATOM   1976  OE1 GLU B 262      63.309  -6.275   5.235  1.00 74.63           O  
ANISOU 1976  OE1 GLU B 262    11330   8089   8938   2522   1591  -2263       O  
ATOM   1977  OE2 GLU B 262      63.952  -7.157   7.141  1.00 75.56           O  
ANISOU 1977  OE2 GLU B 262    11433   7967   9307   2646   1471  -2144       O  
ATOM   1978  N   GLY B 263      65.199  -3.485  11.375  1.00 62.34           N  
ANISOU 1978  N   GLY B 263     9252   6605   7830   2439   1264  -1471       N  
ATOM   1979  CA  GLY B 263      66.187  -3.344  12.417  1.00 64.07           C  
ANISOU 1979  CA  GLY B 263     9343   6841   8160   2526   1220  -1373       C  
ATOM   1980  C   GLY B 263      65.719  -3.930  13.717  1.00 64.92           C  
ANISOU 1980  C   GLY B 263     9546   6769   8353   2516   1092  -1288       C  
ATOM   1981  O   GLY B 263      64.808  -4.757  13.756  1.00 66.14           O  
ANISOU 1981  O   GLY B 263     9871   6754   8507   2483   1050  -1326       O  
ATOM   1982  N   HIS B 264      66.345  -3.480  14.800  1.00 63.26           N  
ANISOU 1982  N   HIS B 264     9223   6600   8213   2538   1030  -1169       N  
ATOM   1983  CA  HIS B 264      65.991  -4.006  16.109  1.00 63.49           C  
ANISOU 1983  CA  HIS B 264     9334   6474   8317   2537    909  -1075       C  
ATOM   1984  C   HIS B 264      66.217  -2.967  17.195  1.00 63.99           C  
ANISOU 1984  C   HIS B 264     9283   6639   8392   2468    838   -932       C  
ATOM   1985  O   HIS B 264      67.170  -2.187  17.137  1.00 65.44           O  
ANISOU 1985  O   HIS B 264     9293   6982   8588   2501    871   -908       O  
ATOM   1986  CB  HIS B 264      66.792  -5.273  16.437  1.00 64.68           C  
ANISOU 1986  CB  HIS B 264     9505   6483   8586   2735    886  -1109       C  
ATOM   1987  CG  HIS B 264      68.264  -5.040  16.581  1.00 66.70           C  
ANISOU 1987  CG  HIS B 264     9570   6859   8913   2882    912  -1094       C  
ATOM   1988  ND1 HIS B 264      69.156  -5.249  15.550  1.00 67.87           N  
ANISOU 1988  ND1 HIS B 264     9629   7088   9069   3010   1022  -1207       N  
ATOM   1989  CD2 HIS B 264      69.002  -4.617  17.635  1.00 67.03           C  
ANISOU 1989  CD2 HIS B 264     9486   6962   9021   2920    841   -981       C  
ATOM   1990  CE1 HIS B 264      70.378  -4.968  15.965  1.00 68.30           C  
ANISOU 1990  CE1 HIS B 264     9505   7247   9199   3119   1019  -1161       C  
ATOM   1991  NE2 HIS B 264      70.312  -4.582  17.226  1.00 67.93           N  
ANISOU 1991  NE2 HIS B 264     9432   7188   9189   3066    906  -1025       N  
ATOM   1992  N   ILE B 265      65.325  -2.973  18.186  1.00 63.48           N  
ANISOU 1992  N   ILE B 265     9317   6481   8323   2369    741   -839       N  
ATOM   1993  CA  ILE B 265      65.595  -2.288  19.439  1.00 63.33           C  
ANISOU 1993  CA  ILE B 265     9214   6517   8331   2338    653   -708       C  
ATOM   1994  C   ILE B 265      66.811  -2.924  20.092  1.00 64.90           C  
ANISOU 1994  C   ILE B 265     9334   6683   8643   2518    611   -681       C  
ATOM   1995  O   ILE B 265      66.863  -4.149  20.297  1.00 63.20           O  
ANISOU 1995  O   ILE B 265     9218   6302   8494   2629    583   -702       O  
ATOM   1996  CB  ILE B 265      64.373  -2.339  20.366  1.00 62.73           C  
ANISOU 1996  CB  ILE B 265     9273   6336   8224   2212    564   -621       C  
ATOM   1997  CG1 ILE B 265      63.146  -1.749  19.669  1.00 62.60           C  
ANISOU 1997  CG1 ILE B 265     9330   6353   8101   2042    604   -653       C  
ATOM   1998  CG2 ILE B 265      64.662  -1.593  21.666  1.00 62.26           C  
ANISOU 1998  CG2 ILE B 265     9130   6346   8180   2182    473   -493       C  
ATOM   1999  CD1 ILE B 265      61.949  -1.583  20.578  1.00 61.78           C  
ANISOU 1999  CD1 ILE B 265     9330   6184   7961   1906    526   -562       C  
ATOM   2000  N   ILE B 266      67.797  -2.082  20.403  1.00 67.75           N  
ANISOU 2000  N   ILE B 266     9514   7200   9030   2547    605   -634       N  
ATOM   2001  CA  ILE B 266      69.059  -2.441  21.045  1.00 68.53           C  
ANISOU 2001  CA  ILE B 266     9494   7312   9232   2710    560   -600       C  
ATOM   2002  C   ILE B 266      68.810  -2.601  22.538  1.00 67.73           C  
ANISOU 2002  C   ILE B 266     9447   7130   9159   2697    424   -475       C  
ATOM   2003  O   ILE B 266      68.377  -1.646  23.202  1.00 65.73           O  
ANISOU 2003  O   ILE B 266     9171   6950   8852   2565    370   -395       O  
ATOM   2004  CB  ILE B 266      70.140  -1.380  20.779  1.00 68.57           C  
ANISOU 2004  CB  ILE B 266     9276   7529   9249   2721    604   -596       C  
ATOM   2005  CG1 ILE B 266      70.086  -0.902  19.324  1.00 69.28           C  
ANISOU 2005  CG1 ILE B 266     9326   7725   9271   2672    743   -695       C  
ATOM   2006  CG2 ILE B 266      71.525  -1.916  21.122  1.00 68.84           C  
ANISOU 2006  CG2 ILE B 266     9177   7581   9397   2915    582   -593       C  
ATOM   2007  CD1 ILE B 266      71.209   0.047  18.945  1.00 70.80           C  
ANISOU 2007  CD1 ILE B 266     9296   8121   9484   2688    803   -693       C  
ATOM   2008  N   PRO B 267      69.074  -3.773  23.107  1.00 70.66           N  
ANISOU 2008  N   PRO B 267     9890   7350   9609   2833    364   -454       N  
ATOM   2009  CA  PRO B 267      68.710  -4.009  24.509  1.00 71.11           C  
ANISOU 2009  CA  PRO B 267    10023   7320   9676   2814    237   -329       C  
ATOM   2010  C   PRO B 267      69.571  -3.203  25.470  1.00 72.80           C  
ANISOU 2010  C   PRO B 267    10075   7675   9912   2834    157   -239       C  
ATOM   2011  O   PRO B 267      70.784  -3.069  25.290  1.00 73.93           O  
ANISOU 2011  O   PRO B 267    10053   7918  10120   2950    173   -263       O  
ATOM   2012  CB  PRO B 267      68.934  -5.515  24.683  1.00 71.34           C  
ANISOU 2012  CB  PRO B 267    10158   7152   9795   2976    208   -339       C  
ATOM   2013  CG  PRO B 267      69.941  -5.867  23.636  1.00 72.24           C  
ANISOU 2013  CG  PRO B 267    10171   7305   9971   3126    300   -456       C  
ATOM   2014  CD  PRO B 267      69.661  -4.965  22.472  1.00 71.55           C  
ANISOU 2014  CD  PRO B 267    10029   7357   9800   3010    414   -545       C  
ATOM   2015  N   ARG B 268      68.911  -2.652  26.493  1.00 87.97           N  
ANISOU 2015  N   ARG B 268    12043   9608  11775   2715     72   -139       N  
ATOM   2016  CA  ARG B 268      69.554  -2.013  27.641  1.00 88.41           C  
ANISOU 2016  CA  ARG B 268    11984   9767  11841   2726    -32    -44       C  
ATOM   2017  C   ARG B 268      70.249  -0.705  27.275  1.00 89.09           C  
ANISOU 2017  C   ARG B 268    11873  10059  11917   2672      3    -72       C  
ATOM   2018  O   ARG B 268      71.211  -0.302  27.933  1.00 90.94           O  
ANISOU 2018  O   ARG B 268    11963  10395  12195   2730    -66    -27       O  
ATOM   2019  CB  ARG B 268      70.533  -2.970  28.332  1.00 88.86           C  
ANISOU 2019  CB  ARG B 268    12009   9758  11995   2920   -111      2       C  
ATOM   2020  CG  ARG B 268      69.943  -4.348  28.598  1.00 89.91           C  
ANISOU 2020  CG  ARG B 268    12336   9670  12155   2987   -138     29       C  
ATOM   2021  CD  ARG B 268      70.894  -5.231  29.388  1.00 92.19           C  
ANISOU 2021  CD  ARG B 268    12596   9893  12538   3179   -229     92       C  
ATOM   2022  NE  ARG B 268      70.905  -4.890  30.807  1.00 92.54           N  
ANISOU 2022  NE  ARG B 268    12634   9978  12548   3152   -360    224       N  
ATOM   2023  CZ  ARG B 268      69.925  -5.180  31.657  1.00 92.36           C  
ANISOU 2023  CZ  ARG B 268    12775   9853  12465   3073   -423    318       C  
ATOM   2024  NH1 ARG B 268      68.842  -5.822  31.238  1.00 91.30           N  
ANISOU 2024  NH1 ARG B 268    12818   9563  12308   3005   -369    296       N  
ATOM   2025  NH2 ARG B 268      70.027  -4.828  32.931  1.00 93.18           N  
ANISOU 2025  NH2 ARG B 268    12861  10015  12527   3058   -539    432       N  
ATOM   2026  N   VAL B 269      69.759  -0.018  26.247  1.00 81.15           N  
ANISOU 2026  N   VAL B 269    10860   9117  10854   2557    105   -141       N  
ATOM   2027  CA  VAL B 269      70.292   1.274  25.830  1.00 80.01           C  
ANISOU 2027  CA  VAL B 269    10546   9158  10698   2484    146   -161       C  
ATOM   2028  C   VAL B 269      69.198   2.319  25.990  1.00 80.77           C  
ANISOU 2028  C   VAL B 269    10702   9293  10695   2288    139   -131       C  
ATOM   2029  O   VAL B 269      68.079   2.135  25.499  1.00 81.02           O  
ANISOU 2029  O   VAL B 269    10874   9246  10662   2204    187   -158       O  
ATOM   2030  CB  VAL B 269      70.805   1.238  24.379  1.00 78.43           C  
ANISOU 2030  CB  VAL B 269    10265   9018  10518   2530    283   -266       C  
ATOM   2031  CG1 VAL B 269      71.260   2.622  23.945  1.00 78.11           C  
ANISOU 2031  CG1 VAL B 269    10056   9163  10458   2434    330   -272       C  
ATOM   2032  CG2 VAL B 269      71.937   0.232  24.240  1.00 78.54           C  
ANISOU 2032  CG2 VAL B 269    10206   9001  10634   2736    293   -301       C  
ATOM   2033  N   ARG B 270      69.524   3.412  26.679  1.00 69.26           N  
ANISOU 2033  N   ARG B 270     9134   7953   9228   2218     76    -78       N  
ATOM   2034  CA  ARG B 270      68.603   4.528  26.865  1.00 67.43           C  
ANISOU 2034  CA  ARG B 270     8939   7769   8912   2042     66    -52       C  
ATOM   2035  C   ARG B 270      69.367   5.818  26.625  1.00 67.60           C  
ANISOU 2035  C   ARG B 270     8777   7955   8953   1983     83    -60       C  
ATOM   2036  O   ARG B 270      70.350   6.092  27.321  1.00 67.66           O  
ANISOU 2036  O   ARG B 270     8654   8036   9018   2036      9    -26       O  
ATOM   2037  CB  ARG B 270      67.996   4.523  28.269  1.00 66.12           C  
ANISOU 2037  CB  ARG B 270     8867   7551   8705   2002    -54     33       C  
ATOM   2038  CG  ARG B 270      67.121   3.325  28.559  1.00 65.04           C  
ANISOU 2038  CG  ARG B 270     8918   7249   8544   2034    -70     56       C  
ATOM   2039  CD  ARG B 270      65.810   3.390  27.800  1.00 64.21           C  
ANISOU 2039  CD  ARG B 270     8943   7089   8367   1913      7     17       C  
ATOM   2040  NE  ARG B 270      64.855   2.402  28.294  1.00 64.41           N  
ANISOU 2040  NE  ARG B 270     9145   6961   8365   1911    -24     56       N  
ATOM   2041  CZ  ARG B 270      64.917   1.101  28.025  1.00 65.35           C  
ANISOU 2041  CZ  ARG B 270     9349   6947   8533   2014     -7     35       C  
ATOM   2042  NH1 ARG B 270      65.891   0.623  27.261  1.00 66.13           N  
ANISOU 2042  NH1 ARG B 270     9371   7051   8706   2138     43    -30       N  
ATOM   2043  NH2 ARG B 270      64.004   0.276  28.519  1.00 65.43           N  
ANISOU 2043  NH2 ARG B 270     9520   6817   8521   1993    -39     80       N  
ATOM   2044  N   THR B 271      68.924   6.608  25.649  1.00 70.26           N  
ANISOU 2044  N   THR B 271     9104   8349   9244   1873    175   -100       N  
ATOM   2045  CA  THR B 271      69.621   7.838  25.298  1.00 70.72           C  
ANISOU 2045  CA  THR B 271     8992   8554   9324   1807    204   -103       C  
ATOM   2046  C   THR B 271      68.630   8.988  25.190  1.00 70.33           C  
ANISOU 2046  C   THR B 271     8994   8532   9197   1634    214    -89       C  
ATOM   2047  O   THR B 271      67.419   8.783  25.092  1.00 71.76           O  
ANISOU 2047  O   THR B 271     9330   8631   9304   1572    227    -91       O  
ATOM   2048  CB  THR B 271      70.399   7.701  23.983  1.00 71.89           C  
ANISOU 2048  CB  THR B 271     9034   8769   9511   1868    329   -168       C  
ATOM   2049  OG1 THR B 271      69.503   7.308  22.938  1.00 71.52           O  
ANISOU 2049  OG1 THR B 271     9115   8663   9396   1837    428   -222       O  
ATOM   2050  CG2 THR B 271      71.510   6.668  24.118  1.00 72.98           C  
ANISOU 2050  CG2 THR B 271     9094   8895   9739   2050    318   -185       C  
ATOM   2051  N   VAL B 272      69.169  10.208  25.207  1.00 54.60           N  
ANISOU 2051  N   VAL B 272     6863   6654   7228   1557    207    -73       N  
ATOM   2052  CA  VAL B 272      68.326  11.398  25.187  1.00 54.35           C  
ANISOU 2052  CA  VAL B 272     6867   6647   7135   1399    206    -55       C  
ATOM   2053  C   VAL B 272      67.579  11.469  23.863  1.00 55.51           C  
ANISOU 2053  C   VAL B 272     7084   6786   7223   1341    328    -95       C  
ATOM   2054  O   VAL B 272      68.187  11.511  22.786  1.00 56.21           O  
ANISOU 2054  O   VAL B 272     7085   6939   7332   1366    427   -129       O  
ATOM   2055  CB  VAL B 272      69.161  12.659  25.429  1.00 54.13           C  
ANISOU 2055  CB  VAL B 272     6671   6734   7160   1333    174    -33       C  
ATOM   2056  CG1 VAL B 272      68.251  13.874  25.554  1.00 52.09           C  
ANISOU 2056  CG1 VAL B 272     6464   6483   6845   1178    158    -13       C  
ATOM   2057  CG2 VAL B 272      70.016  12.497  26.676  1.00 53.75           C  
ANISOU 2057  CG2 VAL B 272     6543   6707   7174   1404     50     -3       C  
ATOM   2058  N   GLU B 273      66.253  11.481  23.945  1.00 51.71           N  
ANISOU 2058  N   GLU B 273     6755   6231   6660   1265    319    -89       N  
ATOM   2059  CA  GLU B 273      65.355  11.598  22.810  1.00 47.67           C  
ANISOU 2059  CA  GLU B 273     6326   5708   6079   1197    413   -121       C  
ATOM   2060  C   GLU B 273      64.422  12.770  23.069  1.00 47.73           C  
ANISOU 2060  C   GLU B 273     6374   5730   6033   1055    384    -87       C  
ATOM   2061  O   GLU B 273      63.986  12.991  24.207  1.00 46.22           O  
ANISOU 2061  O   GLU B 273     6228   5503   5831   1023    290    -51       O  
ATOM   2062  CB  GLU B 273      64.553  10.305  22.601  1.00 46.79           C  
ANISOU 2062  CB  GLU B 273     6371   5481   5927   1250    431   -154       C  
ATOM   2063  CG  GLU B 273      63.774  10.238  21.298  1.00 48.80           C  
ANISOU 2063  CG  GLU B 273     6701   5730   6113   1200    531   -203       C  
ATOM   2064  CD  GLU B 273      62.378  10.820  21.412  1.00 49.58           C  
ANISOU 2064  CD  GLU B 273     6906   5798   6133   1074    509   -180       C  
ATOM   2065  OE1 GLU B 273      61.916  11.052  22.550  1.00 49.50           O  
ANISOU 2065  OE1 GLU B 273     6937   5753   6120   1036    421   -132       O  
ATOM   2066  OE2 GLU B 273      61.742  11.045  20.360  1.00 49.71           O  
ANISOU 2066  OE2 GLU B 273     6966   5833   6089   1015    581   -210       O  
ATOM   2067  N   GLY B 274      64.128  13.522  22.015  1.00 44.42           N  
ANISOU 2067  N   GLY B 274     5937   5363   5577    975    465    -98       N  
ATOM   2068  CA  GLY B 274      63.325  14.711  22.136  1.00 42.06           C  
ANISOU 2068  CA  GLY B 274     5664   5080   5237    848    444    -66       C  
ATOM   2069  C   GLY B 274      64.175  15.933  22.411  1.00 44.11           C  
ANISOU 2069  C   GLY B 274     5780   5424   5557    796    418    -34       C  
ATOM   2070  O   GLY B 274      65.406  15.852  22.491  1.00 45.49           O  
ANISOU 2070  O   GLY B 274     5826   5652   5805    856    417    -35       O  
ATOM   2071  N   PRO B 275      63.534  17.100  22.576  1.00 51.22           N  
ANISOU 2071  N   PRO B 275     6696   6332   6432    684    393     -6       N  
ATOM   2072  CA  PRO B 275      62.080  17.302  22.539  1.00 51.64           C  
ANISOU 2072  CA  PRO B 275     6887   6331   6405    614    389     -2       C  
ATOM   2073  C   PRO B 275      61.488  17.164  21.139  1.00 51.11           C  
ANISOU 2073  C   PRO B 275     6870   6272   6275    589    492    -21       C  
ATOM   2074  O   PRO B 275      62.223  17.203  20.153  1.00 51.55           O  
ANISOU 2074  O   PRO B 275     6847   6391   6347    608    573    -32       O  
ATOM   2075  CB  PRO B 275      61.907  18.741  23.051  1.00 53.02           C  
ANISOU 2075  CB  PRO B 275     7022   6527   6594    513    336     32       C  
ATOM   2076  CG  PRO B 275      63.233  19.122  23.645  1.00 53.61           C  
ANISOU 2076  CG  PRO B 275     6958   6654   6759    535    288     42       C  
ATOM   2077  CD  PRO B 275      64.246  18.352  22.875  1.00 52.65           C  
ANISOU 2077  CD  PRO B 275     6753   6576   6675    618    360     23       C  
ATOM   2078  N   PHE B 276      60.171  16.991  21.065  1.00 46.07           N  
ANISOU 2078  N   PHE B 276     6361   5580   5564    549    488    -26       N  
ATOM   2079  CA  PHE B 276      59.480  16.912  19.788  1.00 44.85           C  
ANISOU 2079  CA  PHE B 276     6264   5436   5341    518    570    -46       C  
ATOM   2080  C   PHE B 276      58.033  17.333  19.989  1.00 43.03           C  
ANISOU 2080  C   PHE B 276     6137   5164   5047    438    537    -30       C  
ATOM   2081  O   PHE B 276      57.493  17.257  21.095  1.00 41.72           O  
ANISOU 2081  O   PHE B 276     6024   4947   4882    430    462    -18       O  
ATOM   2082  CB  PHE B 276      59.554  15.503  19.185  1.00 44.92           C  
ANISOU 2082  CB  PHE B 276     6328   5414   5328    604    621   -101       C  
ATOM   2083  CG  PHE B 276      59.040  15.419  17.776  1.00 43.86           C  
ANISOU 2083  CG  PHE B 276     6237   5308   5119    579    709   -131       C  
ATOM   2084  CD1 PHE B 276      59.766  15.960  16.729  1.00 44.04           C  
ANISOU 2084  CD1 PHE B 276     6171   5423   5138    573    792   -129       C  
ATOM   2085  CD2 PHE B 276      57.831  14.803  17.499  1.00 42.82           C  
ANISOU 2085  CD2 PHE B 276     6235   5118   4919    559    707   -160       C  
ATOM   2086  CE1 PHE B 276      59.297  15.888  15.431  1.00 43.48           C  
ANISOU 2086  CE1 PHE B 276     6146   5389   4986    552    870   -155       C  
ATOM   2087  CE2 PHE B 276      57.356  14.727  16.202  1.00 42.48           C  
ANISOU 2087  CE2 PHE B 276     6233   5108   4801    536    779   -193       C  
ATOM   2088  CZ  PHE B 276      58.091  15.270  15.167  1.00 42.98           C  
ANISOU 2088  CZ  PHE B 276     6214   5267   4851    536    860   -190       C  
ATOM   2089  N   GLY B 277      57.412  17.782  18.903  1.00 46.10           N  
ANISOU 2089  N   GLY B 277     6554   5585   5379    383    596    -30       N  
ATOM   2090  CA  GLY B 277      56.041  18.238  18.983  1.00 45.09           C  
ANISOU 2090  CA  GLY B 277     6512   5428   5194    310    568    -14       C  
ATOM   2091  C   GLY B 277      55.067  17.100  19.226  1.00 45.31           C  
ANISOU 2091  C   GLY B 277     6656   5385   5176    331    548    -46       C  
ATOM   2092  O   GLY B 277      55.286  15.957  18.823  1.00 46.16           O  
ANISOU 2092  O   GLY B 277     6797   5467   5276    391    580    -89       O  
ATOM   2093  N   GLU B 278      53.971  17.429  19.901  1.00 53.67           N  
ANISOU 2093  N   GLU B 278     7775   6409   6208    279    495    -26       N  
ATOM   2094  CA  GLU B 278      52.889  16.492  20.156  1.00 55.39           C  
ANISOU 2094  CA  GLU B 278     8099   6563   6383    277    476    -45       C  
ATOM   2095  C   GLU B 278      51.580  17.120  19.693  1.00 53.50           C  
ANISOU 2095  C   GLU B 278     7906   6337   6083    198    479    -34       C  
ATOM   2096  O   GLU B 278      51.501  18.325  19.438  1.00 52.32           O  
ANISOU 2096  O   GLU B 278     7713   6235   5932    152    483     -4       O  
ATOM   2097  CB  GLU B 278      52.834  16.096  21.639  1.00 57.81           C  
ANISOU 2097  CB  GLU B 278     8431   6814   6718    302    404    -27       C  
ATOM   2098  CG  GLU B 278      54.028  15.249  22.077  1.00 61.77           C  
ANISOU 2098  CG  GLU B 278     8900   7294   7276    391    394    -38       C  
ATOM   2099  CD  GLU B 278      54.086  15.023  23.575  1.00 64.85           C  
ANISOU 2099  CD  GLU B 278     9307   7645   7688    417    317     -8       C  
ATOM   2100  OE1 GLU B 278      53.840  15.983  24.336  1.00 65.77           O  
ANISOU 2100  OE1 GLU B 278     9403   7787   7802    374    271     21       O  
ATOM   2101  OE2 GLU B 278      54.384  13.883  23.993  1.00 65.75           O  
ANISOU 2101  OE2 GLU B 278     9458   7703   7821    482    301    -13       O  
ATOM   2102  N   PHE B 279      50.544  16.290  19.575  1.00 44.52           N  
ANISOU 2102  N   PHE B 279     6858   5157   4902    183    476    -57       N  
ATOM   2103  CA  PHE B 279      49.287  16.744  18.986  1.00 42.15           C  
ANISOU 2103  CA  PHE B 279     6596   4876   4541    115    481    -52       C  
ATOM   2104  C   PHE B 279      48.543  17.804  19.808  1.00 40.97           C  
ANISOU 2104  C   PHE B 279     6437   4736   4393     65    434     -8       C  
ATOM   2105  O   PHE B 279      47.740  18.547  19.227  1.00 39.63           O  
ANISOU 2105  O   PHE B 279     6270   4600   4185     15    440      6       O  
ATOM   2106  CB  PHE B 279      48.369  15.546  18.694  1.00 41.90           C  
ANISOU 2106  CB  PHE B 279     6655   4795   4471    105    484    -91       C  
ATOM   2107  CG  PHE B 279      47.823  14.861  19.916  1.00 43.36           C  
ANISOU 2107  CG  PHE B 279     6892   4911   4674    104    436    -78       C  
ATOM   2108  CD1 PHE B 279      46.615  15.258  20.469  1.00 42.39           C  
ANISOU 2108  CD1 PHE B 279     6794   4787   4525     46    403    -50       C  
ATOM   2109  CD2 PHE B 279      48.499  13.798  20.494  1.00 45.64           C  
ANISOU 2109  CD2 PHE B 279     7203   5135   5002    166    426    -90       C  
ATOM   2110  CE1 PHE B 279      46.105  14.625  21.588  1.00 42.07           C  
ANISOU 2110  CE1 PHE B 279     6800   4692   4494     42    367    -32       C  
ATOM   2111  CE2 PHE B 279      47.992  13.159  21.611  1.00 45.21           C  
ANISOU 2111  CE2 PHE B 279     7202   5019   4959    163    384    -67       C  
ATOM   2112  CZ  PHE B 279      46.793  13.574  22.158  1.00 43.85           C  
ANISOU 2112  CZ  PHE B 279     7052   4853   4754     97    358    -36       C  
ATOM   2113  N   PRO B 280      48.750  17.935  21.127  1.00 38.11           N  
ANISOU 2113  N   PRO B 280     6064   4347   4067     81    385     13       N  
ATOM   2114  CA  PRO B 280      48.176  19.096  21.827  1.00 36.28           C  
ANISOU 2114  CA  PRO B 280     5816   4133   3837     41    346     45       C  
ATOM   2115  C   PRO B 280      48.800  20.432  21.448  1.00 37.85           C  
ANISOU 2115  C   PRO B 280     5941   4376   4065     24    354     66       C  
ATOM   2116  O   PRO B 280      48.363  21.463  21.972  1.00 35.18           O  
ANISOU 2116  O   PRO B 280     5590   4044   3734     -6    321     87       O  
ATOM   2117  CB  PRO B 280      48.429  18.773  23.305  1.00 35.00           C  
ANISOU 2117  CB  PRO B 280     5663   3937   3699     72    295     55       C  
ATOM   2118  CG  PRO B 280      48.464  17.302  23.347  1.00 36.98           C  
ANISOU 2118  CG  PRO B 280     5968   4139   3943    107    304     37       C  
ATOM   2119  CD  PRO B 280      49.205  16.925  22.102  1.00 36.83           C  
ANISOU 2119  CD  PRO B 280     5926   4133   3934    132    357      8       C  
ATOM   2120  N   GLY B 281      49.805  20.453  20.576  1.00 41.17           N  
ANISOU 2120  N   GLY B 281     6313   4826   4506     42    397     62       N  
ATOM   2121  CA  GLY B 281      50.333  21.689  20.037  1.00 41.63           C  
ANISOU 2121  CA  GLY B 281     6303   4925   4590     14    414     91       C  
ATOM   2122  C   GLY B 281      51.559  22.253  20.719  1.00 43.12           C  
ANISOU 2122  C   GLY B 281     6412   5118   4853     30    389    103       C  
ATOM   2123  O   GLY B 281      51.909  23.410  20.456  1.00 42.58           O  
ANISOU 2123  O   GLY B 281     6289   5073   4818     -7    392    133       O  
ATOM   2124  N   SER B 282      52.225  21.484  21.575  1.00 42.71           N  
ANISOU 2124  N   SER B 282     6351   5045   4831     81    360     84       N  
ATOM   2125  CA  SER B 282      53.408  21.962  22.273  1.00 45.74           C  
ANISOU 2125  CA  SER B 282     6653   5439   5286     97    325     92       C  
ATOM   2126  C   SER B 282      54.483  20.885  22.232  1.00 45.67           C  
ANISOU 2126  C   SER B 282     6610   5436   5306    168    344     71       C  
ATOM   2127  O   SER B 282      54.242  19.748  21.819  1.00 45.28           O  
ANISOU 2127  O   SER B 282     6615   5368   5223    206    376     48       O  
ATOM   2128  CB  SER B 282      53.083  22.356  23.721  1.00 47.23           C  
ANISOU 2128  CB  SER B 282     6860   5599   5485     92    244     92       C  
ATOM   2129  OG  SER B 282      52.551  21.259  24.441  1.00 45.60           O  
ANISOU 2129  OG  SER B 282     6726   5359   5241    130    220     79       O  
ATOM   2130  N   TYR B 283      55.684  21.261  22.665  1.00 39.52           N  
ANISOU 2130  N   TYR B 283     5740   4681   4596    185    319     78       N  
ATOM   2131  CA  TYR B 283      56.817  20.349  22.661  1.00 42.84           C  
ANISOU 2131  CA  TYR B 283     6109   5114   5056    260    333     61       C  
ATOM   2132  C   TYR B 283      56.714  19.335  23.791  1.00 43.20           C  
ANISOU 2132  C   TYR B 283     6208   5111   5095    320    273     49       C  
ATOM   2133  O   TYR B 283      56.220  19.630  24.883  1.00 42.99           O  
ANISOU 2133  O   TYR B 283     6218   5061   5056    303    204     59       O  
ATOM   2134  CB  TYR B 283      58.135  21.111  22.805  1.00 46.55           C  
ANISOU 2134  CB  TYR B 283     6449   5631   5607    255    320     75       C  
ATOM   2135  CG  TYR B 283      58.600  21.811  21.553  1.00 47.31           C  
ANISOU 2135  CG  TYR B 283     6473   5782   5720    213    398     94       C  
ATOM   2136  CD1 TYR B 283      59.302  21.126  20.568  1.00 47.47           C  
ANISOU 2136  CD1 TYR B 283     6451   5845   5742    261    479     80       C  
ATOM   2137  CD2 TYR B 283      58.348  23.162  21.360  1.00 47.05           C  
ANISOU 2137  CD2 TYR B 283     6418   5759   5701    129    394    127       C  
ATOM   2138  CE1 TYR B 283      59.732  21.767  19.421  1.00 47.57           C  
ANISOU 2138  CE1 TYR B 283     6397   5918   5759    222    558    104       C  
ATOM   2139  CE2 TYR B 283      58.773  23.812  20.219  1.00 47.46           C  
ANISOU 2139  CE2 TYR B 283     6406   5860   5765     87    467    157       C  
ATOM   2140  CZ  TYR B 283      59.462  23.110  19.251  1.00 47.41           C  
ANISOU 2140  CZ  TYR B 283     6356   5906   5750    132    551    148       C  
ATOM   2141  OH  TYR B 283      59.887  23.762  18.116  1.00 47.62           O  
ANISOU 2141  OH  TYR B 283     6321   5993   5780     88    631    185       O  
ATOM   2142  N   SER B 284      57.208  18.131  23.519  1.00 53.88           N  
ANISOU 2142  N   SER B 284     7567   6450   6455    396    301     29       N  
ATOM   2143  CA  SER B 284      57.432  17.155  24.569  1.00 54.52           C  
ANISOU 2143  CA  SER B 284     7680   6486   6548    466    243     28       C  
ATOM   2144  C   SER B 284      58.601  17.600  25.443  1.00 56.46           C  
ANISOU 2144  C   SER B 284     7824   6768   6859    494    179     41       C  
ATOM   2145  O   SER B 284      59.193  18.667  25.256  1.00 58.84           O  
ANISOU 2145  O   SER B 284     8032   7122   7202    452    179     48       O  
ATOM   2146  CB  SER B 284      57.713  15.780  23.969  1.00 54.24           C  
ANISOU 2146  CB  SER B 284     7677   6417   6514    544    291      0       C  
ATOM   2147  OG  SER B 284      59.058  15.696  23.522  1.00 55.98           O  
ANISOU 2147  OG  SER B 284     7788   6685   6796    602    322    -13       O  
ATOM   2148  N   GLY B 285      58.936  16.767  26.416  1.00 58.28           N  
ANISOU 2148  N   GLY B 285     8074   6968   7101    565    120     47       N  
ATOM   2149  CA  GLY B 285      60.161  16.917  27.170  1.00 59.88           C  
ANISOU 2149  CA  GLY B 285     8176   7208   7368    613     56     55       C  
ATOM   2150  C   GLY B 285      61.165  15.880  26.705  1.00 59.28           C  
ANISOU 2150  C   GLY B 285     8049   7134   7341    713     90     42       C  
ATOM   2151  O   GLY B 285      60.795  14.823  26.201  1.00 59.81           O  
ANISOU 2151  O   GLY B 285     8191   7148   7385    758    138     27       O  
ATOM   2152  N   ALA B 286      62.444  16.202  26.858  1.00 46.83           N  
ANISOU 2152  N   ALA B 286     6340   5617   5838    746     66     43       N  
ATOM   2153  CA  ALA B 286      63.484  15.233  26.548  1.00 45.50           C  
ANISOU 2153  CA  ALA B 286     6107   5456   5724    855     90     29       C  
ATOM   2154  C   ALA B 286      63.488  14.128  27.597  1.00 45.82           C  
ANISOU 2154  C   ALA B 286     6216   5436   5759    946     15     47       C  
ATOM   2155  O   ALA B 286      63.349  14.390  28.795  1.00 46.29           O  
ANISOU 2155  O   ALA B 286     6296   5492   5802    934    -80     74       O  
ATOM   2156  CB  ALA B 286      64.850  15.913  26.488  1.00 46.28           C  
ANISOU 2156  CB  ALA B 286     6031   5644   5908    863     79     30       C  
ATOM   2157  N   ARG B 287      63.624  12.884  27.143  1.00 56.71           N  
ANISOU 2157  N   ARG B 287     7636   6762   7149   1038     58     31       N  
ATOM   2158  CA  ARG B 287      63.650  11.746  28.054  1.00 56.68           C  
ANISOU 2158  CA  ARG B 287     7702   6687   7146   1130     -8     55       C  
ATOM   2159  C   ARG B 287      64.679  10.739  27.568  1.00 58.56           C  
ANISOU 2159  C   ARG B 287     7882   6914   7453   1260     26     32       C  
ATOM   2160  O   ARG B 287      65.077  10.745  26.405  1.00 59.89           O  
ANISOU 2160  O   ARG B 287     7991   7116   7647   1273    118    -11       O  
ATOM   2161  CB  ARG B 287      62.281  11.058  28.165  1.00 56.05           C  
ANISOU 2161  CB  ARG B 287     7795   6508   6994   1101      3     65       C  
ATOM   2162  CG  ARG B 287      61.142  11.951  28.623  1.00 54.96           C  
ANISOU 2162  CG  ARG B 287     7722   6377   6783    983    -21     85       C  
ATOM   2163  CD  ARG B 287      61.223  12.261  30.106  1.00 58.81           C  
ANISOU 2163  CD  ARG B 287     8211   6882   7254    985   -131    130       C  
ATOM   2164  NE  ARG B 287      59.996  12.889  30.587  1.00 59.19           N  
ANISOU 2164  NE  ARG B 287     8343   6923   7224    887   -147    145       N  
ATOM   2165  CZ  ARG B 287      59.813  14.202  30.672  1.00 58.92           C  
ANISOU 2165  CZ  ARG B 287     8262   6949   7175    803   -159    135       C  
ATOM   2166  NH1 ARG B 287      60.781  15.032  30.308  1.00 61.59           N  
ANISOU 2166  NH1 ARG B 287     8471   7357   7573    793   -159    113       N  
ATOM   2167  NH2 ARG B 287      58.663  14.685  31.120  1.00 56.65           N  
ANISOU 2167  NH2 ARG B 287     8055   6651   6817    728   -171    145       N  
ATOM   2168  N   LEU B 288      65.102   9.853  28.464  1.00 48.44           N  
ANISOU 2168  N   LEU B 288     6619   5586   6198   1361    -48     63       N  
ATOM   2169  CA  LEU B 288      65.937   8.728  28.057  1.00 50.08           C  
ANISOU 2169  CA  LEU B 288     6796   5759   6472   1499    -20     41       C  
ATOM   2170  C   LEU B 288      65.026   7.650  27.477  1.00 50.74           C  
ANISOU 2170  C   LEU B 288     7035   5723   6522   1517     40     17       C  
ATOM   2171  O   LEU B 288      64.233   7.042  28.202  1.00 50.69           O  
ANISOU 2171  O   LEU B 288     7159   5624   6477   1513     -9     56       O  
ATOM   2172  CB  LEU B 288      66.759   8.207  29.232  1.00 48.70           C  
ANISOU 2172  CB  LEU B 288     6581   5579   6343   1607   -129     88       C  
ATOM   2173  CG  LEU B 288      67.872   9.139  29.720  1.00 49.90           C  
ANISOU 2173  CG  LEU B 288     6559   5855   6547   1607   -193    100       C  
ATOM   2174  CD1 LEU B 288      68.495   8.616  31.002  1.00 50.47           C  
ANISOU 2174  CD1 LEU B 288     6612   5919   6644   1705   -318    154       C  
ATOM   2175  CD2 LEU B 288      68.932   9.321  28.647  1.00 52.04           C  
ANISOU 2175  CD2 LEU B 288     6673   6206   6895   1649   -110     52       C  
ATOM   2176  N   GLN B 289      65.122   7.431  26.166  1.00 61.21           N  
ANISOU 2176  N   GLN B 289     8346   7053   7857   1532    147    -47       N  
ATOM   2177  CA  GLN B 289      64.240   6.532  25.433  1.00 60.66           C  
ANISOU 2177  CA  GLN B 289     8417   6879   7753   1532    210    -88       C  
ATOM   2178  C   GLN B 289      65.073   5.516  24.664  1.00 61.89           C  
ANISOU 2178  C   GLN B 289     8543   7001   7971   1669    269   -147       C  
ATOM   2179  O   GLN B 289      66.310   5.506  24.740  1.00 62.66           O  
ANISOU 2179  O   GLN B 289     8507   7161   8139   1766    262   -149       O  
ATOM   2180  CB  GLN B 289      63.319   7.307  24.484  1.00 59.27           C  
ANISOU 2180  CB  GLN B 289     8274   6740   7505   1403    285   -122       C  
ATOM   2181  CG  GLN B 289      62.579   8.441  25.151  1.00 59.89           C  
ANISOU 2181  CG  GLN B 289     8362   6862   7530   1275    235    -72       C  
ATOM   2182  CD  GLN B 289      61.084   8.356  24.949  1.00 61.01           C  
ANISOU 2182  CD  GLN B 289     8646   6939   7594   1178    253    -74       C  
ATOM   2183  OE1 GLN B 289      60.483   7.293  25.110  1.00 62.53           O  
ANISOU 2183  OE1 GLN B 289     8958   7022   7777   1205    244    -75       O  
ATOM   2184  NE2 GLN B 289      60.471   9.481  24.601  1.00 59.53           N  
ANISOU 2184  NE2 GLN B 289     8445   6817   7357   1064    276    -73       N  
ATOM   2185  N   CYS B 290      64.385   4.658  23.907  1.00 74.08           N  
ANISOU 2185  N   CYS B 290    10209   8449   9490   1678    328   -200       N  
ATOM   2186  CA  CYS B 290      65.086   3.503  23.367  1.00 75.54           C  
ANISOU 2186  CA  CYS B 290    10396   8571   9736   1824    370   -257       C  
ATOM   2187  C   CYS B 290      65.725   3.833  22.026  1.00 75.11           C  
ANISOU 2187  C   CYS B 290    10238   8616   9683   1847    483   -338       C  
ATOM   2188  O   CYS B 290      65.348   4.786  21.346  1.00 74.02           O  
ANISOU 2188  O   CYS B 290    10070   8568   9485   1738    538   -352       O  
ATOM   2189  CB  CYS B 290      64.143   2.308  23.223  1.00 78.08           C  
ANISOU 2189  CB  CYS B 290    10899   8726  10041   1834    374   -284       C  
ATOM   2190  SG  CYS B 290      63.713   1.490  24.779  1.00 80.30           S  
ANISOU 2190  SG  CYS B 290    11297   8868  10346   1861    251   -186       S  
ATOM   2191  N   GLU B 291      66.708   3.023  21.649  1.00 69.32           N  
ANISOU 2191  N   GLU B 291     9451   7870   9019   1998    519   -387       N  
ATOM   2192  CA  GLU B 291      67.390   3.178  20.376  1.00 69.94           C  
ANISOU 2192  CA  GLU B 291     9432   8044   9098   2042    635   -468       C  
ATOM   2193  C   GLU B 291      67.229   1.918  19.536  1.00 70.24           C  
ANISOU 2193  C   GLU B 291     9577   7973   9139   2138    700   -564       C  
ATOM   2194  O   GLU B 291      67.153   0.801  20.058  1.00 70.05           O  
ANISOU 2194  O   GLU B 291     9649   7805   9164   2229    648   -565       O  
ATOM   2195  CB  GLU B 291      68.877   3.498  20.565  1.00 71.69           C  
ANISOU 2195  CB  GLU B 291     9454   8382   9404   2140    637   -452       C  
ATOM   2196  CG  GLU B 291      69.150   4.972  20.818  1.00 73.44           C  
ANISOU 2196  CG  GLU B 291     9539   8750   9613   2025    621   -392       C  
ATOM   2197  CD  GLU B 291      70.564   5.383  20.450  1.00 75.94           C  
ANISOU 2197  CD  GLU B 291     9646   9210   9998   2097    672   -404       C  
ATOM   2198  OE1 GLU B 291      70.864   6.595  20.510  1.00 76.17           O  
ANISOU 2198  OE1 GLU B 291     9555   9361  10027   1999    671   -362       O  
ATOM   2199  OE2 GLU B 291      71.373   4.498  20.098  1.00 76.29           O  
ANISOU 2199  OE2 GLU B 291     9643   9242  10102   2250    714   -455       O  
ATOM   2200  N   VAL B 292      67.175   2.123  18.224  1.00 72.60           N  
ANISOU 2200  N   VAL B 292     9863   8341   9382   2117    813   -646       N  
ATOM   2201  CA  VAL B 292      66.949   1.066  17.250  1.00 72.29           C  
ANISOU 2201  CA  VAL B 292     9927   8216   9324   2192    884   -757       C  
ATOM   2202  C   VAL B 292      68.083   1.106  16.236  1.00 73.26           C  
ANISOU 2202  C   VAL B 292     9913   8460   9462   2297    998   -832       C  
ATOM   2203  O   VAL B 292      68.343   2.154  15.625  1.00 73.93           O  
ANISOU 2203  O   VAL B 292     9887   8703   9498   2226   1065   -824       O  
ATOM   2204  CB  VAL B 292      65.588   1.210  16.549  1.00 71.82           C  
ANISOU 2204  CB  VAL B 292    10010   8123   9157   2055    913   -795       C  
ATOM   2205  CG1 VAL B 292      65.473   0.221  15.393  1.00 72.15           C  
ANISOU 2205  CG1 VAL B 292    10141   8101   9171   2130    996   -927       C  
ATOM   2206  CG2 VAL B 292      64.459   1.010  17.544  1.00 71.38           C  
ANISOU 2206  CG2 VAL B 292    10090   7938   9092   1963    809   -726       C  
ATOM   2207  N   LYS B 293      68.759  -0.028  16.076  1.00 64.39           N  
ANISOU 2207  N   LYS B 293     8796   7261   8408   2468   1019   -901       N  
ATOM   2208  CA  LYS B 293      69.765  -0.204  15.042  1.00 64.23           C  
ANISOU 2208  CA  LYS B 293     8665   7340   8398   2587   1138   -992       C  
ATOM   2209  C   LYS B 293      69.094  -0.624  13.743  1.00 64.21           C  
ANISOU 2209  C   LYS B 293     8785   7314   8300   2569   1233  -1113       C  
ATOM   2210  O   LYS B 293      68.184  -1.461  13.739  1.00 63.44           O  
ANISOU 2210  O   LYS B 293     8866   7053   8184   2557   1197  -1158       O  
ATOM   2211  CB  LYS B 293      70.783  -1.261  15.473  1.00 65.99           C  
ANISOU 2211  CB  LYS B 293     8842   7488   8742   2792   1116  -1018       C  
ATOM   2212  CG  LYS B 293      71.950  -1.456  14.521  1.00 68.06           C  
ANISOU 2212  CG  LYS B 293     8966   7864   9030   2937   1238  -1108       C  
ATOM   2213  CD  LYS B 293      73.000  -0.381  14.713  1.00 68.85           C  
ANISOU 2213  CD  LYS B 293     8832   8162   9166   2925   1259  -1036       C  
ATOM   2214  CE  LYS B 293      74.329  -0.803  14.115  1.00 70.61           C  
ANISOU 2214  CE  LYS B 293     8899   8476   9453   3108   1356  -1109       C  
ATOM   2215  NZ  LYS B 293      74.735   0.091  12.996  1.00 71.65           N  
ANISOU 2215  NZ  LYS B 293     8901   8811   9512   3053   1495  -1139       N  
ATOM   2216  N   ILE B 294      69.547  -0.038  12.640  1.00 68.34           N  
ANISOU 2216  N   ILE B 294     9207   7999   8758   2564   1354  -1163       N  
ATOM   2217  CA  ILE B 294      69.002  -0.307  11.315  1.00 68.82           C  
ANISOU 2217  CA  ILE B 294     9365   8073   8710   2546   1452  -1280       C  
ATOM   2218  C   ILE B 294      69.916  -1.322  10.640  1.00 70.75           C  
ANISOU 2218  C   ILE B 294     9582   8306   8995   2744   1539  -1404       C  
ATOM   2219  O   ILE B 294      71.024  -0.983  10.209  1.00 71.90           O  
ANISOU 2219  O   ILE B 294     9556   8603   9158   2826   1628  -1416       O  
ATOM   2220  CB  ILE B 294      68.878   0.978  10.485  1.00 67.39           C  
ANISOU 2220  CB  ILE B 294     9103   8083   8418   2416   1534  -1253       C  
ATOM   2221  CG1 ILE B 294      68.113   2.052  11.261  1.00 66.13           C  
ANISOU 2221  CG1 ILE B 294     8950   7937   8238   2237   1444  -1124       C  
ATOM   2222  CG2 ILE B 294      68.191   0.691   9.158  1.00 66.59           C  
ANISOU 2222  CG2 ILE B 294     9121   7994   8187   2389   1621  -1368       C  
ATOM   2223  CD1 ILE B 294      66.838   1.557  11.920  1.00 65.03           C  
ANISOU 2223  CD1 ILE B 294     8997   7622   8091   2161   1336  -1108       C  
ATOM   2224  N   ASP B 295      69.455  -2.570  10.548  1.00 86.04           N  
ANISOU 2224  N   ASP B 295    11682  10059  10949   2822   1514  -1498       N  
ATOM   2225  CA  ASP B 295      70.250  -3.662  10.007  1.00 87.64           C  
ANISOU 2225  CA  ASP B 295    11882  10216  11203   3023   1583  -1625       C  
ATOM   2226  C   ASP B 295      70.177  -3.758   8.488  1.00 89.34           C  
ANISOU 2226  C   ASP B 295    12129  10520  11297   3041   1718  -1767       C  
ATOM   2227  O   ASP B 295      71.159  -4.167   7.858  1.00 91.80           O  
ANISOU 2227  O   ASP B 295    12353  10898  11627   3200   1818  -1859       O  
ATOM   2228  CB  ASP B 295      69.797  -4.986  10.626  1.00 88.59           C  
ANISOU 2228  CB  ASP B 295    12172  10080  11407   3100   1489  -1661       C  
ATOM   2229  CG  ASP B 295      69.902  -4.986  12.139  1.00 89.56           C  
ANISOU 2229  CG  ASP B 295    12272  10115  11642   3097   1355  -1519       C  
ATOM   2230  OD1 ASP B 295      70.968  -4.596  12.659  1.00 90.65           O  
ANISOU 2230  OD1 ASP B 295    12234  10353  11855   3174   1350  -1451       O  
ATOM   2231  OD2 ASP B 295      68.915  -5.359  12.807  1.00 89.50           O  
ANISOU 2231  OD2 ASP B 295    12418   9945  11644   3014   1255  -1474       O  
ATOM   2232  N   ARG B 296      69.048  -3.397   7.877  1.00 83.46           N  
ANISOU 2232  N   ARG B 296    11503   9784  10423   2887   1725  -1790       N  
ATOM   2233  CA  ARG B 296      68.960  -3.389   6.422  1.00 83.13           C  
ANISOU 2233  CA  ARG B 296    11489   9849  10247   2894   1850  -1917       C  
ATOM   2234  C   ARG B 296      67.865  -2.431   5.981  1.00 81.01           C  
ANISOU 2234  C   ARG B 296    11279   9661   9839   2688   1844  -1871       C  
ATOM   2235  O   ARG B 296      66.860  -2.256   6.676  1.00 79.06           O  
ANISOU 2235  O   ARG B 296    11127   9313   9599   2557   1734  -1795       O  
ATOM   2236  CB  ARG B 296      68.693  -4.784   5.852  1.00 85.23           C  
ANISOU 2236  CB  ARG B 296    11920   9953  10512   3010   1865  -2090       C  
ATOM   2237  CG  ARG B 296      69.031  -4.877   4.376  1.00 87.74           C  
ANISOU 2237  CG  ARG B 296    12226  10405  10706   3078   2013  -2237       C  
ATOM   2238  CD  ARG B 296      67.974  -5.615   3.583  1.00 87.97           C  
ANISOU 2238  CD  ARG B 296    12467  10321  10638   3040   2006  -2381       C  
ATOM   2239  NE  ARG B 296      68.008  -7.051   3.832  1.00 88.23           N  
ANISOU 2239  NE  ARG B 296    12626  10124  10775   3180   1961  -2493       N  
ATOM   2240  CZ  ARG B 296      68.983  -7.859   3.427  1.00 89.39           C  
ANISOU 2240  CZ  ARG B 296    12722  10261  10980   3364   2030  -2606       C  
ATOM   2241  NH1 ARG B 296      70.017  -7.378   2.751  1.00 90.70           N  
ANISOU 2241  NH1 ARG B 296    12715  10642  11104   3438   2158  -2625       N  
ATOM   2242  NH2 ARG B 296      68.923  -9.154   3.697  1.00 89.65           N  
ANISOU 2242  NH2 ARG B 296    12854  10077  11132   3431   1960  -2680       N  
ATOM   2243  N   ILE B 297      68.064  -1.822   4.814  1.00 69.91           N  
ANISOU 2243  N   ILE B 297     9814   8442   8306   2665   1964  -1915       N  
ATOM   2244  CA  ILE B 297      67.069  -0.942   4.213  1.00 68.81           C  
ANISOU 2244  CA  ILE B 297     9731   8391   8022   2486   1970  -1881       C  
ATOM   2245  C   ILE B 297      66.643  -1.531   2.876  1.00 70.06           C  
ANISOU 2245  C   ILE B 297    10011   8565   8042   2516   2048  -2046       C  
ATOM   2246  O   ILE B 297      67.490  -1.910   2.061  1.00 70.30           O  
ANISOU 2246  O   ILE B 297     9988   8682   8041   2651   2165  -2151       O  
ATOM   2247  CB  ILE B 297      67.602   0.490   4.029  1.00 68.78           C  
ANISOU 2247  CB  ILE B 297     9550   8609   7974   2406   2035  -1761       C  
ATOM   2248  CG1 ILE B 297      67.987   1.093   5.381  1.00 67.91           C  
ANISOU 2248  CG1 ILE B 297     9326   8480   7999   2369   1947  -1608       C  
ATOM   2249  CG2 ILE B 297      66.561   1.353   3.333  1.00 68.70           C  
ANISOU 2249  CG2 ILE B 297     9608   8684   7811   2234   2042  -1730       C  
ATOM   2250  CD1 ILE B 297      68.614   2.465   5.283  1.00 66.59           C  
ANISOU 2250  CD1 ILE B 297     8975   8511   7813   2294   2004  -1491       C  
ATOM   2251  N   THR B 298      65.336  -1.624   2.655  1.00 76.32           N  
ANISOU 2251  N   THR B 298    10965   9278   8753   2391   1982  -2072       N  
ATOM   2252  CA  THR B 298      64.787  -1.987   1.356  1.00 76.29           C  
ANISOU 2252  CA  THR B 298    11079   9312   8596   2385   2042  -2217       C  
ATOM   2253  C   THR B 298      63.870  -0.865   0.897  1.00 74.30           C  
ANISOU 2253  C   THR B 298    10842   9183   8205   2200   2032  -2138       C  
ATOM   2254  O   THR B 298      63.014  -0.409   1.660  1.00 72.95           O  
ANISOU 2254  O   THR B 298    10708   8945   8066   2065   1925  -2030       O  
ATOM   2255  CB  THR B 298      64.023  -3.315   1.408  1.00 77.81           C  
ANISOU 2255  CB  THR B 298    11466   9278   8820   2416   1966  -2349       C  
ATOM   2256  OG1 THR B 298      62.701  -3.093   1.912  1.00 76.60           O  
ANISOU 2256  OG1 THR B 298    11420   9027   8656   2245   1845  -2279       O  
ATOM   2257  CG2 THR B 298      64.741  -4.318   2.301  1.00 79.74           C  
ANISOU 2257  CG2 THR B 298    11703   9352   9243   2568   1929  -2369       C  
ATOM   2258  N   HIS B 299      64.052  -0.418  -0.343  1.00 72.70           N  
ANISOU 2258  N   HIS B 299    10611   9165   7847   2199   2145  -2189       N  
ATOM   2259  CA  HIS B 299      63.301   0.734  -0.818  1.00 71.79           C  
ANISOU 2259  CA  HIS B 299    10495   9184   7599   2036   2143  -2099       C  
ATOM   2260  C   HIS B 299      63.046   0.629  -2.313  1.00 73.37           C  
ANISOU 2260  C   HIS B 299    10766   9508   7603   2043   2232  -2223       C  
ATOM   2261  O   HIS B 299      63.828   0.028  -3.055  1.00 74.82           O  
ANISOU 2261  O   HIS B 299    10935   9750   7745   2183   2340  -2349       O  
ATOM   2262  CB  HIS B 299      64.033   2.046  -0.506  1.00 71.25           C  
ANISOU 2262  CB  HIS B 299    10239   9275   7557   1989   2190  -1931       C  
ATOM   2263  CG  HIS B 299      65.311   2.222  -1.265  1.00 72.33           C  
ANISOU 2263  CG  HIS B 299    10238   9590   7655   2102   2346  -1960       C  
ATOM   2264  ND1 HIS B 299      65.363   2.815  -2.508  1.00 72.48           N  
ANISOU 2264  ND1 HIS B 299    10236   9804   7500   2072   2457  -1975       N  
ATOM   2265  CD2 HIS B 299      66.586   1.886  -0.955  1.00 73.40           C  
ANISOU 2265  CD2 HIS B 299    10244   9745   7900   2246   2410  -1974       C  
ATOM   2266  CE1 HIS B 299      66.614   2.836  -2.932  1.00 73.45           C  
ANISOU 2266  CE1 HIS B 299    10221  10061   7626   2189   2590  -1996       C  
ATOM   2267  NE2 HIS B 299      67.376   2.278  -2.009  1.00 73.97           N  
ANISOU 2267  NE2 HIS B 299    10215  10025   7867   2297   2564  -1999       N  
ATOM   2268  N   ARG B 300      61.936   1.225  -2.744  1.00 71.82           N  
ANISOU 2268  N   ARG B 300    10647   9356   7284   1895   2186  -2187       N  
ATOM   2269  CA  ARG B 300      61.666   1.376  -4.164  1.00 71.56           C  
ANISOU 2269  CA  ARG B 300    10668   9476   7045   1882   2265  -2273       C  
ATOM   2270  C   ARG B 300      62.652   2.363  -4.776  1.00 72.14           C  
ANISOU 2270  C   ARG B 300    10583   9785   7043   1904   2406  -2190       C  
ATOM   2271  O   ARG B 300      63.186   3.243  -4.095  1.00 70.90           O  
ANISOU 2271  O   ARG B 300    10284   9677   6977   1867   2412  -2034       O  
ATOM   2272  CB  ARG B 300      60.235   1.865  -4.392  1.00 69.46           C  
ANISOU 2272  CB  ARG B 300    10509   9208   6676   1714   2169  -2232       C  
ATOM   2273  CG  ARG B 300      59.195   1.214  -3.492  1.00 69.12           C  
ANISOU 2273  CG  ARG B 300    10584   8939   6738   1648   2017  -2247       C  
ATOM   2274  CD  ARG B 300      57.833   1.877  -3.644  1.00 69.23           C  
ANISOU 2274  CD  ARG B 300    10669   8975   6661   1477   1926  -2181       C  
ATOM   2275  NE  ARG B 300      57.368   1.877  -5.028  1.00 70.34           N  
ANISOU 2275  NE  ARG B 300    10888   9241   6596   1457   1968  -2282       N  
ATOM   2276  CZ  ARG B 300      56.089   1.947  -5.384  1.00 69.25           C  
ANISOU 2276  CZ  ARG B 300    10857   9090   6365   1340   1879  -2301       C  
ATOM   2277  NH1 ARG B 300      55.145   2.021  -4.457  1.00 68.58           N  
ANISOU 2277  NH1 ARG B 300    10807   8871   6377   1233   1752  -2226       N  
ATOM   2278  NH2 ARG B 300      55.754   1.941  -6.666  1.00 68.99           N  
ANISOU 2278  NH2 ARG B 300    10891   9185   6139   1331   1917  -2395       N  
ATOM   2279  N   THR B 301      62.898   2.210  -6.074  1.00 73.60           N  
ANISOU 2279  N   THR B 301    10792  10116   7057   1962   2519  -2298       N  
ATOM   2280  CA  THR B 301      63.770   3.143  -6.771  1.00 73.34           C  
ANISOU 2280  CA  THR B 301    10612  10317   6935   1969   2659  -2216       C  
ATOM   2281  C   THR B 301      63.111   4.515  -6.842  1.00 72.79           C  
ANISOU 2281  C   THR B 301    10518  10351   6787   1800   2627  -2042       C  
ATOM   2282  O   THR B 301      61.899   4.629  -7.046  1.00 72.15           O  
ANISOU 2282  O   THR B 301    10562  10231   6622   1692   2534  -2045       O  
ATOM   2283  CB  THR B 301      64.094   2.633  -8.173  1.00 74.23           C  
ANISOU 2283  CB  THR B 301    10727  10549   6926   2000   2740  -2350       C  
ATOM   2284  OG1 THR B 301      64.212   1.206  -8.143  1.00 74.11           O  
ANISOU 2284  OG1 THR B 301    10787  10381   6992   2104   2708  -2530       O  
ATOM   2285  CG2 THR B 301      65.406   3.229  -8.658  1.00 76.38           C  
ANISOU 2285  CG2 THR B 301    10819  11021   7181   2052   2897  -2287       C  
ATOM   2286  N   ASN B 302      63.922   5.555  -6.674  1.00 72.11           N  
ANISOU 2286  N   ASN B 302    10265  10395   6739   1774   2700  -1889       N  
ATOM   2287  CA  ASN B 302      63.440   6.916  -6.468  1.00 70.10           C  
ANISOU 2287  CA  ASN B 302     9963  10205   6468   1614   2657  -1700       C  
ATOM   2288  C   ASN B 302      62.440   6.965  -5.309  1.00 68.14           C  
ANISOU 2288  C   ASN B 302     9784   9765   6342   1516   2483  -1640       C  
ATOM   2289  O   ASN B 302      61.284   7.354  -5.497  1.00 66.89           O  
ANISOU 2289  O   ASN B 302     9722   9592   6100   1400   2402  -1606       O  
ATOM   2290  CB  ASN B 302      62.821   7.481  -7.739  1.00 70.24           C  
ANISOU 2290  CB  ASN B 302    10048  10382   6257   1541   2704  -1691       C  
ATOM   2291  CG  ASN B 302      63.794   7.517  -8.896  1.00 73.07           C  
ANISOU 2291  CG  ASN B 302    10328  10943   6491   1618   2873  -1732       C  
ATOM   2292  OD1 ASN B 302      63.441   7.187 -10.028  1.00 75.81           O  
ANISOU 2292  OD1 ASN B 302    10747  11359   6699   1592   2884  -1825       O  
ATOM   2293  ND2 ASN B 302      65.029   7.919  -8.619  1.00 73.25           N  
ANISOU 2293  ND2 ASN B 302    10181  11051   6600   1677   2981  -1656       N  
ATOM   2294  N   PRO B 303      62.855   6.581  -4.102  1.00 56.16           N  
ANISOU 2294  N   PRO B 303     8216   8106   5018   1561   2425  -1624       N  
ATOM   2295  CA  PRO B 303      61.907   6.527  -2.987  1.00 55.76           C  
ANISOU 2295  CA  PRO B 303     8237   7874   5076   1476   2266  -1576       C  
ATOM   2296  C   PRO B 303      61.474   7.919  -2.558  1.00 54.54           C  
ANISOU 2296  C   PRO B 303     8022   7765   4935   1328   2215  -1392       C  
ATOM   2297  O   PRO B 303      62.218   8.895  -2.677  1.00 54.79           O  
ANISOU 2297  O   PRO B 303     7920   7928   4971   1305   2289  -1280       O  
ATOM   2298  CB  PRO B 303      62.701   5.822  -1.884  1.00 54.69           C  
ANISOU 2298  CB  PRO B 303     8040   7607   5132   1579   2239  -1595       C  
ATOM   2299  CG  PRO B 303      64.111   6.203  -2.162  1.00 56.04           C  
ANISOU 2299  CG  PRO B 303     8041   7927   5324   1662   2371  -1561       C  
ATOM   2300  CD  PRO B 303      64.232   6.287  -3.664  1.00 56.86           C  
ANISOU 2300  CD  PRO B 303     8164   8206   5234   1686   2500  -1630       C  
ATOM   2301  N   ILE B 304      60.246   7.999  -2.056  1.00 57.60           N  
ANISOU 2301  N   ILE B 304     8511   8040   5333   1227   2086  -1364       N  
ATOM   2302  CA  ILE B 304      59.622   9.261  -1.678  1.00 55.41           C  
ANISOU 2302  CA  ILE B 304     8204   7790   5060   1088   2024  -1206       C  
ATOM   2303  C   ILE B 304      59.471   9.280  -0.164  1.00 56.42           C  
ANISOU 2303  C   ILE B 304     8309   7763   5366   1059   1913  -1140       C  
ATOM   2304  O   ILE B 304      58.821   8.399   0.414  1.00 57.23           O  
ANISOU 2304  O   ILE B 304     8511   7713   5522   1069   1824  -1209       O  
ATOM   2305  CB  ILE B 304      58.267   9.450  -2.376  1.00 54.59           C  
ANISOU 2305  CB  ILE B 304     8227   7705   4812    992   1968  -1221       C  
ATOM   2306  CG1 ILE B 304      58.462   9.510  -3.894  1.00 57.62           C  
ANISOU 2306  CG1 ILE B 304     8629   8260   5003   1020   2080  -1278       C  
ATOM   2307  CG2 ILE B 304      57.575  10.705  -1.868  1.00 52.25           C  
ANISOU 2307  CG2 ILE B 304     7901   7413   4539    858   1894  -1060       C  
ATOM   2308  CD1 ILE B 304      57.171   9.565  -4.683  1.00 57.14           C  
ANISOU 2308  CD1 ILE B 304     8698   8228   4786    940   2023  -1311       C  
ATOM   2309  N   PHE B 305      60.072  10.280   0.480  1.00 50.86           N  
ANISOU 2309  N   PHE B 305     7474   7099   4750   1021   1918  -1005       N  
ATOM   2310  CA  PHE B 305      60.009  10.427   1.931  1.00 49.77           C  
ANISOU 2310  CA  PHE B 305     7305   6835   4771    993   1816   -934       C  
ATOM   2311  C   PHE B 305      58.686  11.097   2.282  1.00 48.85           C  
ANISOU 2311  C   PHE B 305     7261   6669   4630    862   1712   -860       C  
ATOM   2312  O   PHE B 305      58.534  12.312   2.139  1.00 49.70           O  
ANISOU 2312  O   PHE B 305     7317   6858   4708    774   1717   -747       O  
ATOM   2313  CB  PHE B 305      61.204  11.235   2.425  1.00 47.68           C  
ANISOU 2313  CB  PHE B 305     6870   6640   4606   1004   1861   -832       C  
ATOM   2314  CG  PHE B 305      61.262  11.407   3.918  1.00 50.86           C  
ANISOU 2314  CG  PHE B 305     7231   6927   5165    983   1758   -764       C  
ATOM   2315  CD1 PHE B 305      60.592  10.542   4.768  1.00 46.86           C  
ANISOU 2315  CD1 PHE B 305     6825   6262   4717    999   1656   -813       C  
ATOM   2316  CD2 PHE B 305      62.005  12.437   4.470  1.00 51.62           C  
ANISOU 2316  CD2 PHE B 305     7187   7078   5346    945   1763   -649       C  
ATOM   2317  CE1 PHE B 305      60.655  10.708   6.138  1.00 51.11           C  
ANISOU 2317  CE1 PHE B 305     7327   6706   5385    983   1564   -747       C  
ATOM   2318  CE2 PHE B 305      62.074  12.607   5.838  1.00 52.31           C  
ANISOU 2318  CE2 PHE B 305     7240   7070   5567    928   1665   -593       C  
ATOM   2319  CZ  PHE B 305      61.399  11.741   6.673  1.00 51.15           C  
ANISOU 2319  CZ  PHE B 305     7196   6773   5465    950   1567   -641       C  
ATOM   2320  N   GLU B 306      57.715  10.306   2.729  1.00 54.87           N  
ANISOU 2320  N   GLU B 306     8143   7297   5407    849   1619   -922       N  
ATOM   2321  CA  GLU B 306      56.422  10.832   3.155  1.00 53.28           C  
ANISOU 2321  CA  GLU B 306     8008   7043   5195    732   1518   -859       C  
ATOM   2322  C   GLU B 306      56.521  11.211   4.626  1.00 52.83           C  
ANISOU 2322  C   GLU B 306     7895   6896   5283    707   1440   -769       C  
ATOM   2323  O   GLU B 306      56.522  10.337   5.499  1.00 54.74           O  
ANISOU 2323  O   GLU B 306     8172   7012   5616    752   1385   -810       O  
ATOM   2324  CB  GLU B 306      55.312   9.809   2.927  1.00 53.77           C  
ANISOU 2324  CB  GLU B 306     8216   7012   5204    721   1457   -966       C  
ATOM   2325  CG  GLU B 306      53.937  10.288   3.372  1.00 52.53           C  
ANISOU 2325  CG  GLU B 306     8118   6804   5037    604   1354   -905       C  
ATOM   2326  CD  GLU B 306      52.943   9.153   3.542  1.00 53.90           C  
ANISOU 2326  CD  GLU B 306     8418   6849   5211    592   1279  -1002       C  
ATOM   2327  OE1 GLU B 306      53.306   7.992   3.266  1.00 55.59           O  
ANISOU 2327  OE1 GLU B 306     8686   7006   5430    674   1306  -1120       O  
ATOM   2328  OE2 GLU B 306      51.795   9.422   3.954  1.00 52.76           O  
ANISOU 2328  OE2 GLU B 306     8319   6660   5067    501   1194   -960       O  
ATOM   2329  N   ASN B 307      56.608  12.508   4.906  1.00 49.76           N  
ANISOU 2329  N   ASN B 307     7424   6568   4915    635   1433   -647       N  
ATOM   2330  CA  ASN B 307      56.762  12.975   6.275  1.00 49.82           C  
ANISOU 2330  CA  ASN B 307     7374   6505   5052    610   1361   -565       C  
ATOM   2331  C   ASN B 307      55.642  13.943   6.632  1.00 48.90           C  
ANISOU 2331  C   ASN B 307     7288   6374   4919    495   1285   -480       C  
ATOM   2332  O   ASN B 307      54.905  14.431   5.771  1.00 48.55           O  
ANISOU 2332  O   ASN B 307     7286   6393   4770    435   1295   -465       O  
ATOM   2333  CB  ASN B 307      58.131  13.632   6.486  1.00 52.10           C  
ANISOU 2333  CB  ASN B 307     7514   6867   5415    642   1419   -503       C  
ATOM   2334  CG  ASN B 307      58.717  13.327   7.850  1.00 52.50           C  
ANISOU 2334  CG  ASN B 307     7514   6828   5608    687   1359   -488       C  
ATOM   2335  OD1 ASN B 307      58.629  12.200   8.340  1.00 51.46           O  
ANISOU 2335  OD1 ASN B 307     7443   6594   5514    752   1321   -557       O  
ATOM   2336  ND2 ASN B 307      59.322  14.331   8.472  1.00 52.94           N  
ANISOU 2336  ND2 ASN B 307     7458   6917   5739    651   1345   -395       N  
ATOM   2337  N   LEU B 308      55.524  14.216   7.929  1.00 50.77           N  
ANISOU 2337  N   LEU B 308     7503   6530   5259    471   1206   -426       N  
ATOM   2338  CA  LEU B 308      54.410  14.976   8.474  1.00 49.59           C  
ANISOU 2338  CA  LEU B 308     7388   6345   5108    376   1125   -359       C  
ATOM   2339  C   LEU B 308      54.924  16.164   9.272  1.00 49.35           C  
ANISOU 2339  C   LEU B 308     7259   6332   5162    340   1103   -258       C  
ATOM   2340  O   LEU B 308      55.893  16.043  10.027  1.00 51.35           O  
ANISOU 2340  O   LEU B 308     7439   6563   5508    388   1100   -250       O  
ATOM   2341  CB  LEU B 308      53.531  14.083   9.365  1.00 49.49           C  
ANISOU 2341  CB  LEU B 308     7466   6206   5130    375   1041   -401       C  
ATOM   2342  CG  LEU B 308      52.386  14.712  10.162  1.00 49.08           C  
ANISOU 2342  CG  LEU B 308     7446   6108   5092    291    954   -339       C  
ATOM   2343  CD1 LEU B 308      51.203  13.767  10.185  1.00 46.96           C  
ANISOU 2343  CD1 LEU B 308     7290   5764   4787    269    906   -400       C  
ATOM   2344  CD2 LEU B 308      52.815  15.047  11.585  1.00 51.44           C  
ANISOU 2344  CD2 LEU B 308     7691   6353   5502    297    902   -284       C  
ATOM   2345  N   TYR B 309      54.271  17.310   9.102  1.00 41.08           N  
ANISOU 2345  N   TYR B 309     6208   5320   4082    256   1082   -184       N  
ATOM   2346  CA  TYR B 309      54.472  18.451   9.980  1.00 41.48           C  
ANISOU 2346  CA  TYR B 309     6189   5359   4215    208   1039    -96       C  
ATOM   2347  C   TYR B 309      53.351  18.501  11.010  1.00 42.46           C  
ANISOU 2347  C   TYR B 309     6375   5393   4364    168    941    -85       C  
ATOM   2348  O   TYR B 309      52.186  18.250  10.689  1.00 42.04           O  
ANISOU 2348  O   TYR B 309     6407   5324   4243    137    914   -107       O  
ATOM   2349  CB  TYR B 309      54.508  19.774   9.210  1.00 38.12           C  
ANISOU 2349  CB  TYR B 309     5716   5018   3751    144   1077    -12       C  
ATOM   2350  CG  TYR B 309      54.506  20.974  10.135  1.00 38.63           C  
ANISOU 2350  CG  TYR B 309     5727   5050   3901     87   1019     71       C  
ATOM   2351  CD1 TYR B 309      55.681  21.414  10.731  1.00 39.56           C  
ANISOU 2351  CD1 TYR B 309     5739   5173   4118     96   1027    103       C  
ATOM   2352  CD2 TYR B 309      53.326  21.647  10.439  1.00 38.07           C  
ANISOU 2352  CD2 TYR B 309     5710   4941   3815     26    953    109       C  
ATOM   2353  CE1 TYR B 309      55.685  22.496  11.590  1.00 40.59           C  
ANISOU 2353  CE1 TYR B 309     5828   5268   4328     43    968    167       C  
ATOM   2354  CE2 TYR B 309      53.321  22.730  11.300  1.00 38.58           C  
ANISOU 2354  CE2 TYR B 309     5732   4969   3958    -20    899    173       C  
ATOM   2355  CZ  TYR B 309      54.504  23.149  11.872  1.00 41.22           C  
ANISOU 2355  CZ  TYR B 309     5970   5305   4388    -13    906    199       C  
ATOM   2356  OH  TYR B 309      54.511  24.228  12.729  1.00 43.86           O  
ANISOU 2356  OH  TYR B 309     6266   5597   4800    -60    847    251       O  
ATOM   2357  N   LEU B 310      53.708  18.834  12.245  1.00 44.67           N  
ANISOU 2357  N   LEU B 310     6610   5623   4739    168    887    -53       N  
ATOM   2358  CA  LEU B 310      52.730  19.082  13.291  1.00 44.65           C  
ANISOU 2358  CA  LEU B 310     6653   5551   4761    128    801    -33       C  
ATOM   2359  C   LEU B 310      53.107  20.357  14.028  1.00 43.98           C  
ANISOU 2359  C   LEU B 310     6494   5469   4747     90    767     37       C  
ATOM   2360  O   LEU B 310      54.290  20.630  14.257  1.00 45.70           O  
ANISOU 2360  O   LEU B 310     6624   5710   5031    112    785     54       O  
ATOM   2361  CB  LEU B 310      52.626  17.899  14.271  1.00 44.03           C  
ANISOU 2361  CB  LEU B 310     6623   5388   4720    177    755    -82       C  
ATOM   2362  CG  LEU B 310      53.658  17.731  15.387  1.00 45.17           C  
ANISOU 2362  CG  LEU B 310     6706   5500   4958    227    726    -75       C  
ATOM   2363  CD1 LEU B 310      53.173  16.681  16.374  1.00 45.07           C  
ANISOU 2363  CD1 LEU B 310     6764   5396   4962    258    669   -105       C  
ATOM   2364  CD2 LEU B 310      55.021  17.351  14.829  1.00 45.62           C  
ANISOU 2364  CD2 LEU B 310     6689   5603   5042    294    793    -99       C  
ATOM   2365  N   GLY B 311      52.097  21.144  14.370  1.00 38.88           N  
ANISOU 2365  N   GLY B 311     5880   4801   4090     32    716     75       N  
ATOM   2366  CA  GLY B 311      52.294  22.379  15.118  1.00 38.79           C  
ANISOU 2366  CA  GLY B 311     5814   4778   4146     -7    674    131       C  
ATOM   2367  C   GLY B 311      51.052  22.713  15.885  1.00 37.78           C  
ANISOU 2367  C   GLY B 311     5744   4600   4010    -40    605    139       C  
ATOM   2368  O   GLY B 311      50.369  21.813  16.392  1.00 38.00           O  
ANISOU 2368  O   GLY B 311     5835   4587   4015    -21    575    100       O  
ATOM   2369  N   ILE B 312      50.744  24.002  15.983  1.00 40.99           N  
ANISOU 2369  N   ILE B 312     6130   5008   4438    -89    581    192       N  
ATOM   2370  CA  ILE B 312      49.477  24.401  16.601  1.00 39.32           C  
ANISOU 2370  CA  ILE B 312     5970   4758   4212   -115    522    198       C  
ATOM   2371  C   ILE B 312      48.326  23.877  15.750  1.00 38.89           C  
ANISOU 2371  C   ILE B 312     5984   4723   4068   -126    538    184       C  
ATOM   2372  O   ILE B 312      48.300  24.121  14.527  1.00 41.27           O  
ANISOU 2372  O   ILE B 312     6284   5077   4319   -142    582    205       O  
ATOM   2373  CB  ILE B 312      49.407  25.931  16.743  1.00 42.76           C  
ANISOU 2373  CB  ILE B 312     6370   5185   4691   -159    497    254       C  
ATOM   2374  CG1 ILE B 312      50.499  26.423  17.696  1.00 44.26           C  
ANISOU 2374  CG1 ILE B 312     6495   5349   4974   -155    469    258       C  
ATOM   2375  CG2 ILE B 312      48.031  26.363  17.231  1.00 41.37           C  
ANISOU 2375  CG2 ILE B 312     6246   4978   4495   -177    446    258       C  
ATOM   2376  CD1 ILE B 312      50.678  27.923  17.687  1.00 45.95           C  
ANISOU 2376  CD1 ILE B 312     6667   5549   5244   -203    452    311       C  
ATOM   2377  N   PRO B 313      47.375  23.136  16.323  1.00 36.86           N  
ANISOU 2377  N   PRO B 313     5785   4433   3786   -120    502    149       N  
ATOM   2378  CA  PRO B 313      46.263  22.610  15.522  1.00 36.99           C  
ANISOU 2378  CA  PRO B 313     5860   4470   3724   -138    510    130       C  
ATOM   2379  C   PRO B 313      45.485  23.725  14.833  1.00 34.21           C  
ANISOU 2379  C   PRO B 313     5505   4154   3339   -177    503    180       C  
ATOM   2380  O   PRO B 313      45.413  24.854  15.322  1.00 33.54           O  
ANISOU 2380  O   PRO B 313     5390   4053   3298   -192    475    223       O  
ATOM   2381  CB  PRO B 313      45.401  21.881  16.560  1.00 35.49           C  
ANISOU 2381  CB  PRO B 313     5716   4230   3537   -136    464    100       C  
ATOM   2382  CG  PRO B 313      46.384  21.474  17.617  1.00 35.45           C  
ANISOU 2382  CG  PRO B 313     5690   4184   3595    -97    453     86       C  
ATOM   2383  CD  PRO B 313      47.337  22.636  17.708  1.00 35.82           C  
ANISOU 2383  CD  PRO B 313     5667   4247   3695    -98    456    124       C  
ATOM   2384  N   TRP B 314      44.904  23.402  13.679  1.00 33.99           N  
ANISOU 2384  N   TRP B 314     5511   4173   3231   -190    524    172       N  
ATOM   2385  CA  TRP B 314      44.971  22.069  13.083  1.00 36.08           C  
ANISOU 2385  CA  TRP B 314     5817   4450   3444   -173    554    109       C  
ATOM   2386  C   TRP B 314      46.137  21.928  12.108  1.00 36.55           C  
ANISOU 2386  C   TRP B 314     5851   4557   3479   -149    622    104       C  
ATOM   2387  O   TRP B 314      46.435  22.848  11.347  1.00 38.16           O  
ANISOU 2387  O   TRP B 314     6023   4813   3662   -164    651    157       O  
ATOM   2388  CB  TRP B 314      43.665  21.746  12.349  1.00 37.48           C  
ANISOU 2388  CB  TRP B 314     6044   4656   3539   -203    534     90       C  
ATOM   2389  CG  TRP B 314      42.610  21.091  13.193  1.00 35.82           C  
ANISOU 2389  CG  TRP B 314     5871   4399   3340   -219    485     59       C  
ATOM   2390  CD1 TRP B 314      42.237  21.438  14.458  1.00 34.79           C  
ANISOU 2390  CD1 TRP B 314     5727   4224   3268   -222    445     79       C  
ATOM   2391  CD2 TRP B 314      41.782  19.981  12.821  1.00 36.26           C  
ANISOU 2391  CD2 TRP B 314     5981   4450   3345   -237    473      2       C  
ATOM   2392  NE1 TRP B 314      41.234  20.610  14.900  1.00 33.39           N  
ANISOU 2392  NE1 TRP B 314     5588   4020   3078   -243    416     47       N  
ATOM   2393  CE2 TRP B 314      40.936  19.707  13.914  1.00 33.94           C  
ANISOU 2393  CE2 TRP B 314     5699   4109   3088   -256    429      0       C  
ATOM   2394  CE3 TRP B 314      41.678  19.190  11.673  1.00 37.30           C  
ANISOU 2394  CE3 TRP B 314     6153   4614   3404   -242    494    -50       C  
ATOM   2395  CZ2 TRP B 314      39.998  18.676  13.893  1.00 34.97           C  
ANISOU 2395  CZ2 TRP B 314     5875   4219   3192   -287    407    -46       C  
ATOM   2396  CZ3 TRP B 314      40.746  18.166  11.654  1.00 38.38           C  
ANISOU 2396  CZ3 TRP B 314     6340   4726   3516   -271    465   -105       C  
ATOM   2397  CH2 TRP B 314      39.919  17.919  12.756  1.00 37.07           C  
ANISOU 2397  CH2 TRP B 314     6180   4509   3397   -296    422    -99       C  
ATOM   2398  N   THR B 315      46.795  20.769  12.143  1.00 38.27           N  
ANISOU 2398  N   THR B 315     6083   4756   3703   -108    650     42       N  
ATOM   2399  CA  THR B 315      47.734  20.380  11.096  1.00 40.22           C  
ANISOU 2399  CA  THR B 315     6317   5057   3909    -76    721     17       C  
ATOM   2400  C   THR B 315      47.361  18.990  10.596  1.00 40.98           C  
ANISOU 2400  C   THR B 315     6482   5140   3946    -55    731    -70       C  
ATOM   2401  O   THR B 315      46.283  18.485  10.924  1.00 40.28           O  
ANISOU 2401  O   THR B 315     6450   5010   3844    -79    682    -98       O  
ATOM   2402  CB  THR B 315      49.181  20.408  11.595  1.00 41.62           C  
ANISOU 2402  CB  THR B 315     6425   5225   4165    -34    754     24       C  
ATOM   2403  OG1 THR B 315      49.330  19.512  12.703  1.00 41.42           O  
ANISOU 2403  OG1 THR B 315     6416   5123   4200      2    719    -19       O  
ATOM   2404  CG2 THR B 315      49.573  21.814  12.024  1.00 41.86           C  
ANISOU 2404  CG2 THR B 315     6385   5264   4257    -65    741    105       C  
ATOM   2405  N   GLU B 316      48.241  18.360   9.812  1.00 41.89           N  
ANISOU 2405  N   GLU B 316     6595   5291   4031     -9    796   -117       N  
ATOM   2406  CA  GLU B 316      47.907  17.063   9.230  1.00 42.77           C  
ANISOU 2406  CA  GLU B 316     6779   5386   4084     13    806   -210       C  
ATOM   2407  C   GLU B 316      47.601  16.026  10.305  1.00 44.04           C  
ANISOU 2407  C   GLU B 316     6985   5440   4310     28    758   -256       C  
ATOM   2408  O   GLU B 316      46.719  15.177  10.123  1.00 44.04           O  
ANISOU 2408  O   GLU B 316     7058   5402   4273      8    730   -312       O  
ATOM   2409  CB  GLU B 316      49.040  16.566   8.333  1.00 43.82           C  
ANISOU 2409  CB  GLU B 316     6896   5571   4183     74    890   -259       C  
ATOM   2410  CG  GLU B 316      48.745  15.208   7.701  1.00 45.41           C  
ANISOU 2410  CG  GLU B 316     7180   5749   4326    103    901   -369       C  
ATOM   2411  CD  GLU B 316      49.868  14.694   6.824  1.00 47.70           C  
ANISOU 2411  CD  GLU B 316     7453   6092   4579    174    989   -428       C  
ATOM   2412  OE1 GLU B 316      50.996  15.223   6.920  1.00 48.03           O  
ANISOU 2412  OE1 GLU B 316     7410   6175   4664    209   1040   -384       O  
ATOM   2413  OE2 GLU B 316      49.622  13.753   6.038  1.00 49.24           O  
ANISOU 2413  OE2 GLU B 316     7718   6287   4702    197   1006   -523       O  
ATOM   2414  N   ILE B 317      48.310  16.083  11.437  1.00 41.03           N  
ANISOU 2414  N   ILE B 317     6560   5008   4023     59    745   -228       N  
ATOM   2415  CA  ILE B 317      48.164  15.046  12.457  1.00 40.63           C  
ANISOU 2415  CA  ILE B 317     6552   4855   4029     82    704   -262       C  
ATOM   2416  C   ILE B 317      46.749  15.021  13.019  1.00 39.04           C  
ANISOU 2416  C   ILE B 317     6402   4613   3820     18    640   -248       C  
ATOM   2417  O   ILE B 317      46.269  13.971  13.463  1.00 40.43           O  
ANISOU 2417  O   ILE B 317     6638   4712   4011     17    612   -287       O  
ATOM   2418  CB  ILE B 317      49.211  15.236  13.574  1.00 41.67           C  
ANISOU 2418  CB  ILE B 317     6621   4955   4255    127    696   -226       C  
ATOM   2419  CG1 ILE B 317      49.260  13.995  14.471  1.00 43.41           C  
ANISOU 2419  CG1 ILE B 317     6891   5075   4527    168    664   -262       C  
ATOM   2420  CG2 ILE B 317      48.912  16.483  14.395  1.00 39.40           C  
ANISOU 2420  CG2 ILE B 317     6288   4682   4001     81    653   -148       C  
ATOM   2421  CD1 ILE B 317      50.313  14.056  15.551  1.00 44.79           C  
ANISOU 2421  CD1 ILE B 317     7009   5223   4788    222    649   -231       C  
ATOM   2422  N   ASP B 318      46.054  16.161  13.001  1.00 40.51           N  
ANISOU 2422  N   ASP B 318     6561   4847   3983    -36    616   -189       N  
ATOM   2423  CA  ASP B 318      44.672  16.179  13.466  1.00 39.01           C  
ANISOU 2423  CA  ASP B 318     6407   4632   3782    -94    561   -177       C  
ATOM   2424  C   ASP B 318      43.760  15.376  12.547  1.00 39.40           C  
ANISOU 2424  C   ASP B 318     6522   4686   3761   -127    556   -237       C  
ATOM   2425  O   ASP B 318      42.781  14.782  13.013  1.00 41.04           O  
ANISOU 2425  O   ASP B 318     6772   4846   3976   -165    514   -253       O  
ATOM   2426  CB  ASP B 318      44.176  17.619  13.585  1.00 38.94           C  
ANISOU 2426  CB  ASP B 318     6352   4675   3768   -133    539   -105       C  
ATOM   2427  CG  ASP B 318      44.919  18.406  14.648  1.00 40.29           C  
ANISOU 2427  CG  ASP B 318     6466   4829   4015   -111    529    -53       C  
ATOM   2428  OD1 ASP B 318      44.494  18.368  15.821  1.00 38.53           O  
ANISOU 2428  OD1 ASP B 318     6249   4558   3832   -119    487    -38       O  
ATOM   2429  OD2 ASP B 318      45.929  19.059  14.311  1.00 40.57           O  
ANISOU 2429  OD2 ASP B 318     6449   4900   4066    -89    563    -29       O  
ATOM   2430  N   TYR B 319      44.064  15.339  11.247  1.00 34.74           N  
ANISOU 2430  N   TYR B 319     5940   4159   3102   -115    597   -273       N  
ATOM   2431  CA  TYR B 319      43.250  14.557  10.321  1.00 34.39           C  
ANISOU 2431  CA  TYR B 319     5960   4122   2983   -146    586   -342       C  
ATOM   2432  C   TYR B 319      43.508  13.064  10.469  1.00 35.93           C  
ANISOU 2432  C   TYR B 319     6218   4228   3206   -116    592   -427       C  
ATOM   2433  O   TYR B 319      42.632  12.252  10.152  1.00 37.96           O  
ANISOU 2433  O   TYR B 319     6536   4452   3433   -156    561   -485       O  
ATOM   2434  CB  TYR B 319      43.512  15.004   8.882  1.00 35.45           C  
ANISOU 2434  CB  TYR B 319     6088   4360   3021   -139    629   -354       C  
ATOM   2435  CG  TYR B 319      42.921  16.356   8.556  1.00 35.01           C  
ANISOU 2435  CG  TYR B 319     5991   4385   2925   -180    610   -273       C  
ATOM   2436  CD1 TYR B 319      41.602  16.476   8.142  1.00 34.29           C  
ANISOU 2436  CD1 TYR B 319     5926   4327   2777   -237    559   -274       C  
ATOM   2437  CD2 TYR B 319      43.679  17.514   8.676  1.00 35.59           C  
ANISOU 2437  CD2 TYR B 319     5999   4499   3026   -163    640   -194       C  
ATOM   2438  CE1 TYR B 319      41.055  17.713   7.850  1.00 34.39           C  
ANISOU 2438  CE1 TYR B 319     5901   4408   2758   -266    538   -196       C  
ATOM   2439  CE2 TYR B 319      43.140  18.754   8.388  1.00 33.37           C  
ANISOU 2439  CE2 TYR B 319     5686   4277   2716   -198    620   -116       C  
ATOM   2440  CZ  TYR B 319      41.827  18.847   7.977  1.00 33.80           C  
ANISOU 2440  CZ  TYR B 319     5769   4361   2712   -244    569   -116       C  
ATOM   2441  OH  TYR B 319      41.286  20.077   7.688  1.00 33.96           O  
ANISOU 2441  OH  TYR B 319     5758   4436   2708   -269    547    -36       O  
ATOM   2442  N   LEU B 320      44.694  12.682  10.942  1.00 40.62           N  
ANISOU 2442  N   LEU B 320     6796   4777   3860    -47    626   -435       N  
ATOM   2443  CA  LEU B 320      44.985  11.277  11.189  1.00 41.67           C  
ANISOU 2443  CA  LEU B 320     6990   4810   4034     -8    627   -507       C  
ATOM   2444  C   LEU B 320      44.403  10.776  12.506  1.00 43.24           C  
ANISOU 2444  C   LEU B 320     7215   4908   4306    -35    573   -478       C  
ATOM   2445  O   LEU B 320      44.497   9.577  12.788  1.00 45.03           O  
ANISOU 2445  O   LEU B 320     7501   5035   4572    -13    566   -527       O  
ATOM   2446  CB  LEU B 320      46.497  11.041  11.167  1.00 41.32           C  
ANISOU 2446  CB  LEU B 320     6912   4761   4027     87    684   -526       C  
ATOM   2447  CG  LEU B 320      47.136  11.056   9.777  1.00 44.14           C  
ANISOU 2447  CG  LEU B 320     7263   5202   4308    127    751   -583       C  
ATOM   2448  CD1 LEU B 320      48.630  11.301   9.872  1.00 44.52           C  
ANISOU 2448  CD1 LEU B 320     7236   5280   4398    210    810   -566       C  
ATOM   2449  CD2 LEU B 320      46.849   9.757   9.038  1.00 44.65           C  
ANISOU 2449  CD2 LEU B 320     7418   5214   4332    141    756   -699       C  
ATOM   2450  N   MET B 321      43.806  11.657  13.310  1.00 49.24           N  
ANISOU 2450  N   MET B 321     7935   5689   5083    -81    538   -398       N  
ATOM   2451  CA  MET B 321      43.201  11.269  14.575  1.00 50.69           C  
ANISOU 2451  CA  MET B 321     8141   5795   5324   -110    493   -363       C  
ATOM   2452  C   MET B 321      41.740  11.686  14.693  1.00 49.48           C  
ANISOU 2452  C   MET B 321     7990   5671   5141   -197    452   -334       C  
ATOM   2453  O   MET B 321      41.138  11.473  15.750  1.00 50.06           O  
ANISOU 2453  O   MET B 321     8072   5695   5253   -228    420   -296       O  
ATOM   2454  CB  MET B 321      43.987  11.867  15.753  1.00 50.37           C  
ANISOU 2454  CB  MET B 321     8045   5748   5344    -67    489   -294       C  
ATOM   2455  CG  MET B 321      45.459  11.490  15.780  1.00 52.56           C  
ANISOU 2455  CG  MET B 321     8305   6002   5663     23    524   -314       C  
ATOM   2456  SD  MET B 321      46.395  12.419  17.013  1.00 54.71           S  
ANISOU 2456  SD  MET B 321     8497   6293   5997     65    511   -236       S  
ATOM   2457  CE  MET B 321      45.630  11.854  18.527  1.00 53.53           C  
ANISOU 2457  CE  MET B 321     8394   6059   5886     39    454   -195       C  
ATOM   2458  N   ALA B 322      41.152  12.254  13.640  1.00 43.19           N  
ANISOU 2458  N   ALA B 322     7181   4956   4275   -235    452   -347       N  
ATOM   2459  CA  ALA B 322      39.819  12.849  13.742  1.00 43.10           C  
ANISOU 2459  CA  ALA B 322     7151   4988   4238   -308    411   -311       C  
ATOM   2460  C   ALA B 322      38.718  11.791  13.767  1.00 43.98           C  
ANISOU 2460  C   ALA B 322     7317   5045   4350   -374    377   -353       C  
ATOM   2461  O   ALA B 322      38.086  11.559  14.801  1.00 44.09           O  
ANISOU 2461  O   ALA B 322     7332   5014   4408   -409    352   -316       O  
ATOM   2462  CB  ALA B 322      39.603  13.835  12.588  1.00 40.45           C  
ANISOU 2462  CB  ALA B 322     6782   4760   3826   -320    418   -303       C  
ATOM   2463  N   LEU B 323      38.472  11.142  12.627  1.00 38.12           N  
ANISOU 2463  N   LEU B 323     6618   4309   3555   -394    375   -430       N  
ATOM   2464  CA  LEU B 323      37.301  10.281  12.508  1.00 40.31           C  
ANISOU 2464  CA  LEU B 323     6938   4547   3829   -473    333   -472       C  
ATOM   2465  C   LEU B 323      37.544   8.881  13.061  1.00 41.55           C  
ANISOU 2465  C   LEU B 323     7165   4570   4051   -471    333   -512       C  
ATOM   2466  O   LEU B 323      36.587   8.204  13.459  1.00 41.92           O  
ANISOU 2466  O   LEU B 323     7238   4561   4127   -544    299   -516       O  
ATOM   2467  CB  LEU B 323      36.853  10.209  11.047  1.00 40.94           C  
ANISOU 2467  CB  LEU B 323     7039   4694   3821   -503    319   -542       C  
ATOM   2468  CG  LEU B 323      36.339  11.523  10.454  1.00 40.12           C  
ANISOU 2468  CG  LEU B 323     6872   4720   3650   -519    306   -494       C  
ATOM   2469  CD1 LEU B 323      35.695  11.297   9.095  1.00 37.34           C  
ANISOU 2469  CD1 LEU B 323     6548   4434   3207   -560    277   -563       C  
ATOM   2470  CD2 LEU B 323      35.358  12.186  11.410  1.00 39.45           C  
ANISOU 2470  CD2 LEU B 323     6732   4654   3605   -565    272   -414       C  
ATOM   2471  N   ASN B 324      38.799   8.428  13.095  1.00 48.86           N  
ANISOU 2471  N   ASN B 324     8119   5442   5005   -389    371   -539       N  
ATOM   2472  CA  ASN B 324      39.091   7.131  13.694  1.00 49.74           C  
ANISOU 2472  CA  ASN B 324     8298   5416   5187   -375    369   -567       C  
ATOM   2473  C   ASN B 324      38.944   7.149  15.210  1.00 50.76           C  
ANISOU 2473  C   ASN B 324     8410   5491   5384   -384    355   -477       C  
ATOM   2474  O   ASN B 324      38.919   6.078  15.826  1.00 52.57           O  
ANISOU 2474  O   ASN B 324     8698   5603   5672   -392    344   -480       O  
ATOM   2475  CB  ASN B 324      40.496   6.665  13.305  1.00 51.31           C  
ANISOU 2475  CB  ASN B 324     8523   5577   5398   -272    413   -621       C  
ATOM   2476  CG  ASN B 324      41.540   7.740  13.493  1.00 51.73           C  
ANISOU 2476  CG  ASN B 324     8500   5709   5445   -198    450   -566       C  
ATOM   2477  OD1 ASN B 324      41.214   8.912  13.675  1.00 52.39           O  
ANISOU 2477  OD1 ASN B 324     8519   5882   5504   -224    443   -500       O  
ATOM   2478  ND2 ASN B 324      42.807   7.346  13.454  1.00 50.06           N  
ANISOU 2478  ND2 ASN B 324     8294   5461   5264   -105    488   -594       N  
ATOM   2479  N   THR B 325      38.855   8.331  15.817  1.00 45.66           N  
ANISOU 2479  N   THR B 325     7693   4926   4730   -382    355   -397       N  
ATOM   2480  CA  THR B 325      38.433   8.455  17.204  1.00 45.02           C  
ANISOU 2480  CA  THR B 325     7594   4818   4692   -406    338   -315       C  
ATOM   2481  C   THR B 325      36.918   8.510  17.337  1.00 44.73           C  
ANISOU 2481  C   THR B 325     7545   4808   4641   -508    307   -294       C  
ATOM   2482  O   THR B 325      36.367   7.988  18.314  1.00 46.03           O  
ANISOU 2482  O   THR B 325     7728   4917   4846   -550    295   -251       O  
ATOM   2483  CB  THR B 325      39.038   9.717  17.830  1.00 45.08           C  
ANISOU 2483  CB  THR B 325     7531   4899   4698   -353    350   -249       C  
ATOM   2484  OG1 THR B 325      40.448   9.752  17.579  1.00 43.33           O  
ANISOU 2484  OG1 THR B 325     7303   4669   4489   -264    379   -270       O  
ATOM   2485  CG2 THR B 325      38.792   9.743  19.332  1.00 45.32           C  
ANISOU 2485  CG2 THR B 325     7554   4899   4768   -361    335   -173       C  
ATOM   2486  N   SER B 326      36.238   9.111  16.357  1.00 41.99           N  
ANISOU 2486  N   SER B 326     7167   4551   4238   -548    295   -322       N  
ATOM   2487  CA  SER B 326      34.804   9.357  16.458  1.00 41.36           C  
ANISOU 2487  CA  SER B 326     7053   4519   4144   -638    264   -298       C  
ATOM   2488  C   SER B 326      33.983   8.107  16.165  1.00 42.45           C  
ANISOU 2488  C   SER B 326     7245   4585   4300   -722    238   -349       C  
ATOM   2489  O   SER B 326      32.940   7.892  16.792  1.00 43.32           O  
ANISOU 2489  O   SER B 326     7338   4688   4434   -798    219   -311       O  
ATOM   2490  CB  SER B 326      34.406  10.484  15.504  1.00 40.10           C  
ANISOU 2490  CB  SER B 326     6835   4482   3917   -643    254   -303       C  
ATOM   2491  OG  SER B 326      35.049  11.695  15.857  1.00 40.13           O  
ANISOU 2491  OG  SER B 326     6788   4545   3916   -578    274   -249       O  
ATOM   2492  N   VAL B 327      34.422   7.279  15.214  1.00 34.71           N  
ANISOU 2492  N   VAL B 327     6328   3551   3308   -711    237   -437       N  
ATOM   2493  CA  VAL B 327      33.633   6.103  14.833  1.00 34.55           C  
ANISOU 2493  CA  VAL B 327     6365   3456   3308   -797    205   -498       C  
ATOM   2494  C   VAL B 327      33.493   5.103  15.979  1.00 37.62           C  
ANISOU 2494  C   VAL B 327     6798   3716   3779   -831    205   -457       C  
ATOM   2495  O   VAL B 327      32.365   4.653  16.244  1.00 39.74           O  
ANISOU 2495  O   VAL B 327     7062   3963   4073   -933    178   -443       O  
ATOM   2496  CB  VAL B 327      34.206   5.469  13.559  1.00 35.56           C  
ANISOU 2496  CB  VAL B 327     6557   3554   3400   -768    206   -613       C  
ATOM   2497  CG1 VAL B 327      33.682   4.049  13.392  1.00 35.67           C  
ANISOU 2497  CG1 VAL B 327     6651   3444   3460   -842    175   -682       C  
ATOM   2498  CG2 VAL B 327      33.857   6.313  12.344  1.00 34.63           C  
ANISOU 2498  CG2 VAL B 327     6398   3572   3188   -777    191   -650       C  
ATOM   2499  N   PRO B 328      34.566   4.703  16.680  1.00 45.45           N  
ANISOU 2499  N   PRO B 328     7830   4621   4816   -752    233   -432       N  
ATOM   2500  CA  PRO B 328      34.375   3.758  17.798  1.00 45.63           C  
ANISOU 2500  CA  PRO B 328     7900   4523   4914   -786    231   -379       C  
ATOM   2501  C   PRO B 328      33.480   4.302  18.899  1.00 44.49           C  
ANISOU 2501  C   PRO B 328     7694   4434   4775   -844    229   -276       C  
ATOM   2502  O   PRO B 328      32.644   3.563  19.440  1.00 43.96           O  
ANISOU 2502  O   PRO B 328     7648   4305   4750   -932    218   -243       O  
ATOM   2503  CB  PRO B 328      35.809   3.517  18.296  1.00 45.95           C  
ANISOU 2503  CB  PRO B 328     7978   4494   4987   -669    258   -364       C  
ATOM   2504  CG  PRO B 328      36.675   3.838  17.126  1.00 45.48           C  
ANISOU 2504  CG  PRO B 328     7916   4480   4883   -593    274   -449       C  
ATOM   2505  CD  PRO B 328      35.995   4.983  16.452  1.00 44.36           C  
ANISOU 2505  CD  PRO B 328     7701   4487   4668   -632    267   -453       C  
ATOM   2506  N   LEU B 329      33.644   5.579  19.252  1.00 46.55           N  
ANISOU 2506  N   LEU B 329     7880   4811   4996   -797    244   -225       N  
ATOM   2507  CA  LEU B 329      32.751   6.203  20.222  1.00 46.10           C  
ANISOU 2507  CA  LEU B 329     7759   4823   4935   -843    246   -140       C  
ATOM   2508  C   LEU B 329      31.308   6.160  19.739  1.00 46.60           C  
ANISOU 2508  C   LEU B 329     7783   4936   4986   -956    221   -156       C  
ATOM   2509  O   LEU B 329      30.388   5.878  20.519  1.00 47.01           O  
ANISOU 2509  O   LEU B 329     7815   4984   5064  -1032    222    -99       O  
ATOM   2510  CB  LEU B 329      33.185   7.646  20.478  1.00 45.39           C  
ANISOU 2510  CB  LEU B 329     7598   4846   4804   -769    261   -104       C  
ATOM   2511  CG  LEU B 329      34.478   7.844  21.269  1.00 46.06           C  
ANISOU 2511  CG  LEU B 329     7699   4899   4904   -668    281    -68       C  
ATOM   2512  CD1 LEU B 329      34.775   9.322  21.442  1.00 44.60           C  
ANISOU 2512  CD1 LEU B 329     7440   4823   4681   -612    288    -41       C  
ATOM   2513  CD2 LEU B 329      34.376   7.158  22.620  1.00 45.62           C  
ANISOU 2513  CD2 LEU B 329     7677   4772   4885   -682    287      5       C  
ATOM   2514  N   TYR B 330      31.095   6.445  18.451  1.00 38.67           N  
ANISOU 2514  N   TYR B 330     6763   3989   3940   -969    199   -231       N  
ATOM   2515  CA  TYR B 330      29.750   6.393  17.893  1.00 38.54           C  
ANISOU 2515  CA  TYR B 330     6705   4028   3912  -1074    164   -254       C  
ATOM   2516  C   TYR B 330      29.148   5.004  18.043  1.00 40.11           C  
ANISOU 2516  C   TYR B 330     6958   4111   4169  -1175    146   -272       C  
ATOM   2517  O   TYR B 330      27.982   4.868  18.424  1.00 41.87           O  
ANISOU 2517  O   TYR B 330     7134   4360   4412  -1273    134   -235       O  
ATOM   2518  CB  TYR B 330      29.767   6.811  16.423  1.00 38.51           C  
ANISOU 2518  CB  TYR B 330     6690   4096   3844  -1063    137   -337       C  
ATOM   2519  CG  TYR B 330      28.481   6.498  15.689  1.00 38.88           C  
ANISOU 2519  CG  TYR B 330     6710   4182   3880  -1173     88   -381       C  
ATOM   2520  CD1 TYR B 330      27.356   7.299  15.845  1.00 38.34           C  
ANISOU 2520  CD1 TYR B 330     6543   4229   3794  -1221     70   -334       C  
ATOM   2521  CD2 TYR B 330      28.390   5.401  14.841  1.00 38.30           C  
ANISOU 2521  CD2 TYR B 330     6706   4031   3814  -1228     56   -475       C  
ATOM   2522  CE1 TYR B 330      26.177   7.014  15.180  1.00 39.37           C  
ANISOU 2522  CE1 TYR B 330     6638   4404   3918  -1322     19   -373       C  
ATOM   2523  CE2 TYR B 330      27.216   5.109  14.170  1.00 40.42           C  
ANISOU 2523  CE2 TYR B 330     6947   4339   4073  -1335      2   -520       C  
ATOM   2524  CZ  TYR B 330      26.114   5.920  14.343  1.00 41.67           C  
ANISOU 2524  CZ  TYR B 330     6999   4619   4216  -1383    -17   -466       C  
ATOM   2525  OH  TYR B 330      24.944   5.634  13.677  1.00 43.91           O  
ANISOU 2525  OH  TYR B 330     7242   4949   4491  -1489    -77   -511       O  
ATOM   2526  N   LYS B 331      29.927   3.960  17.752  1.00 43.90           N  
ANISOU 2526  N   LYS B 331     7536   4461   4681  -1153    146   -328       N  
ATOM   2527  CA  LYS B 331      29.399   2.602  17.869  1.00 45.60           C  
ANISOU 2527  CA  LYS B 331     7815   4547   4964  -1250    127   -347       C  
ATOM   2528  C   LYS B 331      29.064   2.262  19.320  1.00 46.61           C  
ANISOU 2528  C   LYS B 331     7939   4623   5147  -1289    152   -234       C  
ATOM   2529  O   LYS B 331      27.998   1.689  19.608  1.00 47.35           O  
ANISOU 2529  O   LYS B 331     8020   4690   5281  -1409    138   -207       O  
ATOM   2530  CB  LYS B 331      30.406   1.603  17.298  1.00 46.22           C  
ANISOU 2530  CB  LYS B 331     8005   4489   5070  -1199    124   -432       C  
ATOM   2531  CG  LYS B 331      30.639   1.743  15.797  1.00 47.55           C  
ANISOU 2531  CG  LYS B 331     8188   4703   5176  -1174    101   -554       C  
ATOM   2532  CD  LYS B 331      31.419   0.558  15.249  1.00 48.45           C  
ANISOU 2532  CD  LYS B 331     8416   4669   5326  -1140     97   -650       C  
ATOM   2533  CE  LYS B 331      31.529   0.608  13.732  1.00 47.76           C  
ANISOU 2533  CE  LYS B 331     8347   4633   5167  -1127     74   -781       C  
ATOM   2534  NZ  LYS B 331      30.193   0.582  13.071  1.00 46.51           N  
ANISOU 2534  NZ  LYS B 331     8154   4535   4982  -1254     18   -824       N  
ATOM   2535  N   GLN B 332      29.965   2.607  20.244  1.00 46.47           N  
ANISOU 2535  N   GLN B 332     7931   4596   5129  -1192    188   -166       N  
ATOM   2536  CA  GLN B 332      29.718   2.346  21.659  1.00 47.18           C  
ANISOU 2536  CA  GLN B 332     8022   4651   5254  -1218    214    -53       C  
ATOM   2537  C   GLN B 332      28.430   3.013  22.120  1.00 46.37           C  
ANISOU 2537  C   GLN B 332     7817   4670   5129  -1300    221      7       C  
ATOM   2538  O   GLN B 332      27.607   2.392  22.802  1.00 47.55           O  
ANISOU 2538  O   GLN B 332     7965   4784   5319  -1396    229     69       O  
ATOM   2539  CB  GLN B 332      30.908   2.820  22.496  1.00 47.13           C  
ANISOU 2539  CB  GLN B 332     8029   4646   5233  -1091    243      1       C  
ATOM   2540  CG  GLN B 332      32.006   1.778  22.645  1.00 49.14           C  
ANISOU 2540  CG  GLN B 332     8389   4745   5539  -1029    243    -10       C  
ATOM   2541  CD  GLN B 332      33.343   2.384  23.022  1.00 49.77           C  
ANISOU 2541  CD  GLN B 332     8467   4849   5595   -889    259      7       C  
ATOM   2542  OE1 GLN B 332      33.452   3.589  23.250  1.00 49.79           O  
ANISOU 2542  OE1 GLN B 332     8395   4976   5546   -844    271     31       O  
ATOM   2543  NE2 GLN B 332      34.373   1.548  23.085  1.00 50.99           N  
ANISOU 2543  NE2 GLN B 332     8702   4878   5793   -818    258     -8       N  
ATOM   2544  N   LEU B 333      28.231   4.279  21.746  1.00 44.92           N  
ANISOU 2544  N   LEU B 333     7548   4633   4886  -1262    219     -7       N  
ATOM   2545  CA  LEU B 333      26.989   4.960  22.105  1.00 46.80           C  
ANISOU 2545  CA  LEU B 333     7683   4993   5105  -1328    224     41       C  
ATOM   2546  C   LEU B 333      25.786   4.307  21.434  1.00 48.40           C  
ANISOU 2546  C   LEU B 333     7861   5192   5337  -1463    190      3       C  
ATOM   2547  O   LEU B 333      24.742   4.108  22.068  1.00 49.13           O  
ANISOU 2547  O   LEU B 333     7901   5312   5454  -1555    202     63       O  
ATOM   2548  CB  LEU B 333      27.067   6.438  21.724  1.00 45.62           C  
ANISOU 2548  CB  LEU B 333     7454   4986   4892  -1252    223     27       C  
ATOM   2549  CG  LEU B 333      27.283   7.439  22.859  1.00 46.45           C  
ANISOU 2549  CG  LEU B 333     7512   5166   4970  -1178    260    103       C  
ATOM   2550  CD1 LEU B 333      28.406   6.981  23.774  1.00 45.20           C  
ANISOU 2550  CD1 LEU B 333     7432   4913   4829  -1111    285    145       C  
ATOM   2551  CD2 LEU B 333      27.572   8.823  22.298  1.00 46.16           C  
ANISOU 2551  CD2 LEU B 333     7419   5237   4884  -1097    251     75       C  
ATOM   2552  N   LYS B 334      25.922   3.953  20.155  1.00 50.73           N  
ANISOU 2552  N   LYS B 334     8193   5455   5627  -1477    147    -99       N  
ATOM   2553  CA  LYS B 334      24.790   3.482  19.368  1.00 52.14           C  
ANISOU 2553  CA  LYS B 334     8339   5648   5823  -1602    101   -152       C  
ATOM   2554  C   LYS B 334      24.265   2.145  19.865  1.00 51.37           C  
ANISOU 2554  C   LYS B 334     8289   5422   5806  -1721    100   -126       C  
ATOM   2555  O   LYS B 334      23.084   1.838  19.665  1.00 54.88           O  
ANISOU 2555  O   LYS B 334     8677   5897   6279  -1846     72   -131       O  
ATOM   2556  CB  LYS B 334      25.199   3.376  17.898  1.00 52.96           C  
ANISOU 2556  CB  LYS B 334     8488   5744   5891  -1578     55   -273       C  
ATOM   2557  CG  LYS B 334      24.055   3.138  16.933  1.00 54.65           C  
ANISOU 2557  CG  LYS B 334     8656   6007   6100  -1693     -5   -341       C  
ATOM   2558  CD  LYS B 334      23.311   4.425  16.635  1.00 55.15           C  
ANISOU 2558  CD  LYS B 334     8596   6253   6105  -1681    -21   -320       C  
ATOM   2559  CE  LYS B 334      22.376   4.248  15.450  1.00 55.86           C  
ANISOU 2559  CE  LYS B 334     8648   6402   6174  -1772    -94   -402       C  
ATOM   2560  NZ  LYS B 334      21.434   5.392  15.318  1.00 55.76           N  
ANISOU 2560  NZ  LYS B 334     8503   6563   6120  -1776   -113   -365       N  
ATOM   2561  N   GLU B 335      25.122   1.335  20.495  1.00 64.54           N  
ANISOU 2561  N   GLU B 335    10058   6946   7519  -1686    125    -97       N  
ATOM   2562  CA  GLU B 335      24.678   0.023  20.969  1.00 67.74           C  
ANISOU 2562  CA  GLU B 335    10520   7209   8008  -1799    124    -64       C  
ATOM   2563  C   GLU B 335      23.428   0.118  21.846  1.00 67.43           C  
ANISOU 2563  C   GLU B 335    10388   7242   7990  -1910    148     36       C  
ATOM   2564  O   GLU B 335      22.469  -0.640  21.658  1.00 66.03           O  
ANISOU 2564  O   GLU B 335    10196   7024   7870  -2052    123     28       O  
ATOM   2565  CB  GLU B 335      25.809  -0.678  21.721  1.00 69.66           C  
ANISOU 2565  CB  GLU B 335    10876   7303   8288  -1724    153    -20       C  
ATOM   2566  CG  GLU B 335      26.942  -1.140  20.822  1.00 72.53           C  
ANISOU 2566  CG  GLU B 335    11340   7561   8656  -1639    129   -127       C  
ATOM   2567  CD  GLU B 335      26.784  -2.582  20.369  1.00 77.19           C  
ANISOU 2567  CD  GLU B 335    12030   7971   9329  -1727     95   -188       C  
ATOM   2568  OE1 GLU B 335      25.646  -2.997  20.054  1.00 78.98           O  
ANISOU 2568  OE1 GLU B 335    12224   8195   9588  -1870     63   -207       O  
ATOM   2569  OE2 GLU B 335      27.802  -3.304  20.329  1.00 78.34           O  
ANISOU 2569  OE2 GLU B 335    12282   7973   9509  -1653     96   -219       O  
ATOM   2570  N   THR B 336      23.413   1.047  22.804  1.00 58.87           N  
ANISOU 2570  N   THR B 336     9236   6270   6862  -1849    196    127       N  
ATOM   2571  CA  THR B 336      22.286   1.176  23.724  1.00 60.06           C  
ANISOU 2571  CA  THR B 336     9295   6501   7024  -1939    232    225       C  
ATOM   2572  C   THR B 336      21.378   2.360  23.418  1.00 61.16           C  
ANISOU 2572  C   THR B 336     9293   6833   7114  -1943    227    214       C  
ATOM   2573  O   THR B 336      20.264   2.418  23.950  1.00 61.63           O  
ANISOU 2573  O   THR B 336     9259   6971   7189  -2033    250    276       O  
ATOM   2574  CB  THR B 336      22.780   1.298  25.173  1.00 58.33           C  
ANISOU 2574  CB  THR B 336     9100   6273   6788  -1875    296    343       C  
ATOM   2575  OG1 THR B 336      23.749   2.351  25.266  1.00 58.06           O  
ANISOU 2575  OG1 THR B 336     9067   6307   6687  -1720    307    329       O  
ATOM   2576  CG2 THR B 336      23.403  -0.008  25.641  1.00 56.14           C  
ANISOU 2576  CG2 THR B 336     8952   5805   6574  -1896    302    383       C  
ATOM   2577  N   MET B 337      21.819   3.302  22.589  1.00 54.52           N  
ANISOU 2577  N   MET B 337     8430   6070   6215  -1847    199    142       N  
ATOM   2578  CA  MET B 337      21.074   4.529  22.316  1.00 53.58           C  
ANISOU 2578  CA  MET B 337     8183   6128   6046  -1827    192    137       C  
ATOM   2579  C   MET B 337      20.954   4.711  20.809  1.00 52.61           C  
ANISOU 2579  C   MET B 337     8049   6037   5901  -1834    123     28       C  
ATOM   2580  O   MET B 337      21.684   5.509  20.205  1.00 51.05           O  
ANISOU 2580  O   MET B 337     7866   5882   5649  -1726    109    -17       O  
ATOM   2581  CB  MET B 337      21.745   5.730  22.983  1.00 51.07           C  
ANISOU 2581  CB  MET B 337     7845   5889   5669  -1686    233    179       C  
ATOM   2582  CG  MET B 337      21.860   5.573  24.491  1.00 52.64           C  
ANISOU 2582  CG  MET B 337     8057   6069   5875  -1675    299    284       C  
ATOM   2583  SD  MET B 337      22.856   6.837  25.295  1.00 51.56           S  
ANISOU 2583  SD  MET B 337     7922   5997   5672  -1508    337    318       S  
ATOM   2584  CE  MET B 337      22.055   6.911  26.896  1.00 47.95           C  
ANISOU 2584  CE  MET B 337     7404   5611   5205  -1544    408    434       C  
ATOM   2585  N   PRO B 338      20.027   3.992  20.168  1.00 46.73           N  
ANISOU 2585  N   PRO B 338     7279   5280   5196  -1965     76    -16       N  
ATOM   2586  CA  PRO B 338      19.879   4.109  18.708  1.00 46.14           C  
ANISOU 2586  CA  PRO B 338     7199   5242   5090  -1977      2   -125       C  
ATOM   2587  C   PRO B 338      19.449   5.491  18.246  1.00 47.17           C  
ANISOU 2587  C   PRO B 338     7219   5549   5154  -1913    -16   -128       C  
ATOM   2588  O   PRO B 338      19.500   5.760  17.040  1.00 45.61           O  
ANISOU 2588  O   PRO B 338     7025   5394   4912  -1895    -74   -208       O  
ATOM   2589  CB  PRO B 338      18.814   3.054  18.375  1.00 46.55           C  
ANISOU 2589  CB  PRO B 338     7229   5252   5207  -2146    -43   -155       C  
ATOM   2590  CG  PRO B 338      18.039   2.893  19.643  1.00 48.45           C  
ANISOU 2590  CG  PRO B 338     7399   5512   5500  -2220     12    -42       C  
ATOM   2591  CD  PRO B 338      19.037   3.072  20.755  1.00 46.11           C  
ANISOU 2591  CD  PRO B 338     7168   5161   5190  -2113     86     35       C  
ATOM   2592  N   GLU B 339      19.033   6.371  19.162  1.00 55.14           N  
ANISOU 2592  N   GLU B 339     8135   6660   6155  -1875     30    -42       N  
ATOM   2593  CA  GLU B 339      18.672   7.732  18.788  1.00 55.29           C  
ANISOU 2593  CA  GLU B 339     8056   6834   6120  -1801     14    -40       C  
ATOM   2594  C   GLU B 339      19.878   8.561  18.373  1.00 54.68           C  
ANISOU 2594  C   GLU B 339     8039   6755   5981  -1658     18    -66       C  
ATOM   2595  O   GLU B 339      19.709   9.569  17.678  1.00 56.06           O  
ANISOU 2595  O   GLU B 339     8158   7035   6107  -1602    -13    -84       O  
ATOM   2596  CB  GLU B 339      17.955   8.427  19.947  1.00 55.92           C  
ANISOU 2596  CB  GLU B 339     8027   7011   6209  -1788     69     51       C  
ATOM   2597  CG  GLU B 339      16.568   7.890  20.238  1.00 59.84           C  
ANISOU 2597  CG  GLU B 339     8421   7558   6758  -1925     66     82       C  
ATOM   2598  CD  GLU B 339      16.591   6.682  21.154  1.00 60.70           C  
ANISOU 2598  CD  GLU B 339     8587   7550   6926  -2018    112    132       C  
ATOM   2599  OE1 GLU B 339      17.680   6.337  21.659  1.00 59.20           O  
ANISOU 2599  OE1 GLU B 339     8513   7247   6733  -1961    148    148       O  
ATOM   2600  OE2 GLU B 339      15.519   6.079  21.369  1.00 62.04           O  
ANISOU 2600  OE2 GLU B 339     8684   7741   7149  -2148    112    158       O  
ATOM   2601  N   VAL B 340      21.085   8.169  18.792  1.00 46.23           N  
ANISOU 2601  N   VAL B 340     7078   5570   4915  -1601     55    -62       N  
ATOM   2602  CA  VAL B 340      22.276   8.940  18.458  1.00 44.58           C  
ANISOU 2602  CA  VAL B 340     6920   5361   4656  -1471     64    -81       C  
ATOM   2603  C   VAL B 340      22.467   8.952  16.951  1.00 43.67           C  
ANISOU 2603  C   VAL B 340     6832   5262   4497  -1467      6   -170       C  
ATOM   2604  O   VAL B 340      22.463   7.902  16.295  1.00 42.64           O  
ANISOU 2604  O   VAL B 340     6763   5056   4381  -1536    -27   -237       O  
ATOM   2605  CB  VAL B 340      23.507   8.366  19.175  1.00 43.24           C  
ANISOU 2605  CB  VAL B 340     6856   5064   4508  -1419    109    -64       C  
ATOM   2606  CG1 VAL B 340      24.782   8.981  18.611  1.00 42.35           C  
ANISOU 2606  CG1 VAL B 340     6796   4943   4351  -1301    111    -99       C  
ATOM   2607  CG2 VAL B 340      23.408   8.614  20.670  1.00 41.42           C  
ANISOU 2607  CG2 VAL B 340     6597   4843   4298  -1400    165     29       C  
ATOM   2608  N   VAL B 341      22.628  10.147  16.394  1.00 46.09           N  
ANISOU 2608  N   VAL B 341     7097   5667   4747  -1385     -7   -170       N  
ATOM   2609  CA  VAL B 341      22.808  10.299  14.957  1.00 45.68           C  
ANISOU 2609  CA  VAL B 341     7067   5652   4636  -1372    -58   -243       C  
ATOM   2610  C   VAL B 341      24.282  10.333  14.584  1.00 45.75           C  
ANISOU 2610  C   VAL B 341     7174   5597   4613  -1279    -32   -275       C  
ATOM   2611  O   VAL B 341      24.706   9.662  13.639  1.00 46.52           O  
ANISOU 2611  O   VAL B 341     7342   5650   4684  -1292    -56   -353       O  
ATOM   2612  CB  VAL B 341      22.065  11.559  14.466  1.00 47.37           C  
ANISOU 2612  CB  VAL B 341     7178   6013   4806  -1341    -93   -218       C  
ATOM   2613  CG1 VAL B 341      22.489  11.913  13.055  1.00 49.69           C  
ANISOU 2613  CG1 VAL B 341     7506   6351   5022  -1301   -135   -274       C  
ATOM   2614  CG2 VAL B 341      20.566  11.338  14.532  1.00 48.78           C  
ANISOU 2614  CG2 VAL B 341     7259   6262   5014  -1443   -132   -209       C  
ATOM   2615  N   ALA B 342      25.095  11.094  15.317  1.00 43.51           N  
ANISOU 2615  N   ALA B 342     6891   5308   4332  -1185     17   -219       N  
ATOM   2616  CA  ALA B 342      26.511  11.161  14.968  1.00 42.23           C  
ANISOU 2616  CA  ALA B 342     6806   5094   4145  -1099     44   -246       C  
ATOM   2617  C   ALA B 342      27.336  11.637  16.156  1.00 43.25           C  
ANISOU 2617  C   ALA B 342     6940   5187   4305  -1023     98   -181       C  
ATOM   2618  O   ALA B 342      26.833  12.310  17.058  1.00 45.48           O  
ANISOU 2618  O   ALA B 342     7159   5516   4605  -1015    112   -118       O  
ATOM   2619  CB  ALA B 342      26.748  12.076  13.759  1.00 39.27           C  
ANISOU 2619  CB  ALA B 342     6416   4809   3696  -1048     20   -269       C  
ATOM   2620  N   VAL B 343      28.622  11.282  16.132  1.00 37.73           N  
ANISOU 2620  N   VAL B 343     6316   4410   3609   -964    126   -204       N  
ATOM   2621  CA  VAL B 343      29.589  11.700  17.143  1.00 36.36           C  
ANISOU 2621  CA  VAL B 343     6153   4202   3460   -885    168   -153       C  
ATOM   2622  C   VAL B 343      30.788  12.321  16.437  1.00 35.89           C  
ANISOU 2622  C   VAL B 343     6113   4157   3366   -799    183   -175       C  
ATOM   2623  O   VAL B 343      31.391  11.694  15.556  1.00 34.99           O  
ANISOU 2623  O   VAL B 343     6056   4006   3233   -790    183   -237       O  
ATOM   2624  CB  VAL B 343      30.042  10.532  18.037  1.00 37.84           C  
ANISOU 2624  CB  VAL B 343     6406   4270   3701   -897    191   -146       C  
ATOM   2625  CG1 VAL B 343      31.187  10.972  18.936  1.00 37.37           C  
ANISOU 2625  CG1 VAL B 343     6359   4182   3657   -807    226   -103       C  
ATOM   2626  CG2 VAL B 343      28.881  10.016  18.871  1.00 36.60           C  
ANISOU 2626  CG2 VAL B 343     6223   4104   3580   -984    187   -106       C  
ATOM   2627  N   ASN B 344      31.136  13.544  16.829  1.00 35.28           N  
ANISOU 2627  N   ASN B 344     5989   4133   3283   -737    197   -124       N  
ATOM   2628  CA  ASN B 344      32.293  14.281  16.333  1.00 34.69           C  
ANISOU 2628  CA  ASN B 344     5920   4075   3186   -660    216   -127       C  
ATOM   2629  C   ASN B 344      33.242  14.422  17.519  1.00 36.45           C  
ANISOU 2629  C   ASN B 344     6152   4245   3453   -602    246    -89       C  
ATOM   2630  O   ASN B 344      33.034  15.270  18.390  1.00 37.09           O  
ANISOU 2630  O   ASN B 344     6188   4357   3549   -583    248    -38       O  
ATOM   2631  CB  ASN B 344      31.857  15.636  15.772  1.00 35.17           C  
ANISOU 2631  CB  ASN B 344     5918   4236   3208   -643    200    -97       C  
ATOM   2632  CG  ASN B 344      33.018  16.603  15.545  1.00 35.28           C  
ANISOU 2632  CG  ASN B 344     5925   4265   3214   -568    224    -75       C  
ATOM   2633  OD1 ASN B 344      34.190  16.243  15.649  1.00 35.57           O  
ANISOU 2633  OD1 ASN B 344     5998   4249   3267   -527    253    -91       O  
ATOM   2634  ND2 ASN B 344      32.681  17.849  15.231  1.00 34.95           N  
ANISOU 2634  ND2 ASN B 344     5832   4294   3152   -550    210    -36       N  
ATOM   2635  N   ALA B 345      34.273  13.587  17.557  1.00 36.71           N  
ANISOU 2635  N   ALA B 345     6241   4201   3506   -571    266   -117       N  
ATOM   2636  CA  ALA B 345      35.269  13.609  18.621  1.00 36.23           C  
ANISOU 2636  CA  ALA B 345     6190   4090   3485   -513    287    -86       C  
ATOM   2637  C   ALA B 345      36.644  13.946  18.061  1.00 36.25           C  
ANISOU 2637  C   ALA B 345     6197   4093   3484   -442    310   -104       C  
ATOM   2638  O   ALA B 345      37.657  13.359  18.446  1.00 38.62           O  
ANISOU 2638  O   ALA B 345     6528   4330   3815   -396    326   -113       O  
ATOM   2639  CB  ALA B 345      35.296  12.276  19.366  1.00 39.47           C  
ANISOU 2639  CB  ALA B 345     6659   4403   3934   -533    290    -89       C  
ATOM   2640  N   MET B 346      36.692  14.913  17.149  1.00 39.55           N  
ANISOU 2640  N   MET B 346     6579   4586   3864   -431    311   -105       N  
ATOM   2641  CA  MET B 346      37.881  15.191  16.355  1.00 39.27           C  
ANISOU 2641  CA  MET B 346     6542   4564   3813   -378    339   -125       C  
ATOM   2642  C   MET B 346      38.864  16.141  17.027  1.00 39.60           C  
ANISOU 2642  C   MET B 346     6542   4614   3890   -322    353    -80       C  
ATOM   2643  O   MET B 346      39.944  16.373  16.475  1.00 38.84           O  
ANISOU 2643  O   MET B 346     6435   4530   3792   -280    380    -89       O  
ATOM   2644  CB  MET B 346      37.475  15.782  15.001  1.00 39.61           C  
ANISOU 2644  CB  MET B 346     6569   4688   3792   -398    336   -138       C  
ATOM   2645  CG  MET B 346      36.557  14.900  14.177  1.00 39.84           C  
ANISOU 2645  CG  MET B 346     6638   4721   3779   -454    315   -194       C  
ATOM   2646  SD  MET B 346      36.237  15.597  12.545  1.00 40.24           S  
ANISOU 2646  SD  MET B 346     6673   4877   3737   -465    308   -207       S  
ATOM   2647  CE  MET B 346      35.918  17.311  12.959  1.00 39.25           C  
ANISOU 2647  CE  MET B 346     6473   4817   3624   -452    295   -115       C  
ATOM   2648  N   TYR B 347      38.536  16.692  18.192  1.00 35.99           N  
ANISOU 2648  N   TYR B 347     6058   4154   3463   -323    335    -35       N  
ATOM   2649  CA  TYR B 347      39.247  17.848  18.728  1.00 34.52           C  
ANISOU 2649  CA  TYR B 347     5825   3987   3303   -283    336      4       C  
ATOM   2650  C   TYR B 347      40.181  17.422  19.856  1.00 35.14           C  
ANISOU 2650  C   TYR B 347     5913   4010   3428   -240    337     10       C  
ATOM   2651  O   TYR B 347      39.730  17.092  20.958  1.00 35.87           O  
ANISOU 2651  O   TYR B 347     6020   4074   3533   -249    320     28       O  
ATOM   2652  CB  TYR B 347      38.242  18.903  19.179  1.00 34.81           C  
ANISOU 2652  CB  TYR B 347     5824   4066   3336   -305    312     41       C  
ATOM   2653  CG  TYR B 347      37.289  19.251  18.059  1.00 36.61           C  
ANISOU 2653  CG  TYR B 347     6040   4350   3518   -342    304     38       C  
ATOM   2654  CD1 TYR B 347      37.754  19.846  16.895  1.00 37.20           C  
ANISOU 2654  CD1 TYR B 347     6102   4465   3566   -331    316     41       C  
ATOM   2655  CD2 TYR B 347      35.937  18.944  18.143  1.00 38.17           C  
ANISOU 2655  CD2 TYR B 347     6238   4567   3697   -389    282     36       C  
ATOM   2656  CE1 TYR B 347      36.898  20.152  15.855  1.00 37.72           C  
ANISOU 2656  CE1 TYR B 347     6162   4589   3582   -360    303     43       C  
ATOM   2657  CE2 TYR B 347      35.070  19.248  17.106  1.00 36.99           C  
ANISOU 2657  CE2 TYR B 347     6073   4476   3505   -421    266     33       C  
ATOM   2658  CZ  TYR B 347      35.558  19.851  15.965  1.00 37.84           C  
ANISOU 2658  CZ  TYR B 347     6175   4623   3581   -404    273     37       C  
ATOM   2659  OH  TYR B 347      34.705  20.157  14.930  1.00 39.23           O  
ANISOU 2659  OH  TYR B 347     6337   4862   3705   -431    251     40       O  
ATOM   2660  N   THR B 348      41.486  17.442  19.569  1.00 36.61           N  
ANISOU 2660  N   THR B 348     6087   4187   3635   -194    357      0       N  
ATOM   2661  CA  THR B 348      42.542  17.088  20.519  1.00 37.34           C  
ANISOU 2661  CA  THR B 348     6178   4235   3774   -144    353      6       C  
ATOM   2662  C   THR B 348      42.324  15.680  21.080  1.00 38.34           C  
ANISOU 2662  C   THR B 348     6365   4294   3909   -143    346     -8       C  
ATOM   2663  O   THR B 348      42.223  15.466  22.289  1.00 38.00           O  
ANISOU 2663  O   THR B 348     6334   4221   3882   -136    324     20       O  
ATOM   2664  CB  THR B 348      42.647  18.129  21.640  1.00 37.37           C  
ANISOU 2664  CB  THR B 348     6143   4255   3802   -133    325     44       C  
ATOM   2665  OG1 THR B 348      42.376  19.431  21.107  1.00 37.19           O  
ANISOU 2665  OG1 THR B 348     6078   4284   3770   -152    325     61       O  
ATOM   2666  CG2 THR B 348      44.046  18.125  22.239  1.00 38.25           C  
ANISOU 2666  CG2 THR B 348     6229   4346   3958    -78    319     48       C  
ATOM   2667  N   HIS B 349      42.257  14.718  20.159  1.00 35.99           N  
ANISOU 2667  N   HIS B 349     6109   3969   3596   -151    366    -51       N  
ATOM   2668  CA  HIS B 349      42.023  13.308  20.481  1.00 35.80           C  
ANISOU 2668  CA  HIS B 349     6151   3865   3587   -157    361    -69       C  
ATOM   2669  C   HIS B 349      40.773  13.128  21.337  1.00 36.14           C  
ANISOU 2669  C   HIS B 349     6215   3894   3621   -215    337    -36       C  
ATOM   2670  O   HIS B 349      40.739  12.319  22.268  1.00 36.37           O  
ANISOU 2670  O   HIS B 349     6284   3862   3674   -211    326    -13       O  
ATOM   2671  CB  HIS B 349      43.239  12.680  21.162  1.00 37.50           C  
ANISOU 2671  CB  HIS B 349     6377   4021   3849    -85    361    -65       C  
ATOM   2672  CG  HIS B 349      43.346  11.201  20.950  1.00 42.19           C  
ANISOU 2672  CG  HIS B 349     7042   4526   4463    -71    368   -101       C  
ATOM   2673  ND1 HIS B 349      44.317  10.429  21.552  1.00 44.02           N  
ANISOU 2673  ND1 HIS B 349     7295   4689   4741     -3    363    -96       N  
ATOM   2674  CD2 HIS B 349      42.607  10.355  20.194  1.00 42.97           C  
ANISOU 2674  CD2 HIS B 349     7196   4585   4544   -116    374   -147       C  
ATOM   2675  CE1 HIS B 349      44.167   9.170  21.180  1.00 45.04           C  
ANISOU 2675  CE1 HIS B 349     7494   4733   4885     -3    369   -135       C  
ATOM   2676  NE2 HIS B 349      43.137   9.098  20.356  1.00 44.72           N  
ANISOU 2676  NE2 HIS B 349     7476   4707   4807    -75    376   -170       N  
ATOM   2677  N   GLY B 350      39.733  13.891  21.021  1.00 35.14           N  
ANISOU 2677  N   GLY B 350     6060   3831   3461   -267    331    -27       N  
ATOM   2678  CA  GLY B 350      38.455  13.691  21.668  1.00 35.51           C  
ANISOU 2678  CA  GLY B 350     6116   3878   3498   -326    315      0       C  
ATOM   2679  C   GLY B 350      38.279  14.377  23.002  1.00 35.70           C  
ANISOU 2679  C   GLY B 350     6111   3925   3526   -315    303     52       C  
ATOM   2680  O   GLY B 350      37.352  14.028  23.739  1.00 34.32           O  
ANISOU 2680  O   GLY B 350     5949   3746   3346   -356    299     80       O  
ATOM   2681  N   ILE B 351      39.138  15.339  23.348  1.00 37.19           N  
ANISOU 2681  N   ILE B 351     6262   4143   3725   -262    299     65       N  
ATOM   2682  CA  ILE B 351      38.877  16.133  24.544  1.00 36.14           C  
ANISOU 2682  CA  ILE B 351     6101   4041   3587   -252    284    102       C  
ATOM   2683  C   ILE B 351      37.615  16.964  24.354  1.00 34.27           C  
ANISOU 2683  C   ILE B 351     5829   3869   3325   -294    282    109       C  
ATOM   2684  O   ILE B 351      36.868  17.207  25.310  1.00 35.14           O  
ANISOU 2684  O   ILE B 351     5929   4003   3421   -307    278    135       O  
ATOM   2685  CB  ILE B 351      40.097  17.008  24.897  1.00 35.54           C  
ANISOU 2685  CB  ILE B 351     5991   3977   3533   -191    272    105       C  
ATOM   2686  CG1 ILE B 351      41.315  16.133  25.189  1.00 36.33           C  
ANISOU 2686  CG1 ILE B 351     6119   4022   3664   -143    269    102       C  
ATOM   2687  CG2 ILE B 351      39.802  17.876  26.109  1.00 34.23           C  
ANISOU 2687  CG2 ILE B 351     5802   3845   3357   -180    252    130       C  
ATOM   2688  CD1 ILE B 351      42.583  16.920  25.432  1.00 35.92           C  
ANISOU 2688  CD1 ILE B 351     6022   3985   3640    -89    255    101       C  
ATOM   2689  N   GLY B 352      37.347  17.395  23.125  1.00 30.00           N  
ANISOU 2689  N   GLY B 352     5267   3360   2773   -313    287     88       N  
ATOM   2690  CA  GLY B 352      36.093  18.037  22.771  1.00 28.92           C  
ANISOU 2690  CA  GLY B 352     5094   3281   2612   -352    281     94       C  
ATOM   2691  C   GLY B 352      35.263  17.106  21.902  1.00 31.45           C  
ANISOU 2691  C   GLY B 352     5436   3598   2914   -411    282     72       C  
ATOM   2692  O   GLY B 352      35.763  16.548  20.922  1.00 31.54           O  
ANISOU 2692  O   GLY B 352     5476   3587   2921   -413    288     39       O  
ATOM   2693  N   VAL B 353      33.998  16.938  22.282  1.00 31.48           N  
ANISOU 2693  N   VAL B 353     5424   3628   2907   -460    278     87       N  
ATOM   2694  CA  VAL B 353      33.087  16.017  21.613  1.00 33.63           C  
ANISOU 2694  CA  VAL B 353     5711   3897   3169   -530    272     66       C  
ATOM   2695  C   VAL B 353      31.757  16.720  21.386  1.00 35.12           C  
ANISOU 2695  C   VAL B 353     5839   4166   3339   -565    258     78       C  
ATOM   2696  O   VAL B 353      31.259  17.428  22.269  1.00 34.84           O  
ANISOU 2696  O   VAL B 353     5761   4169   3306   -550    262    110       O  
ATOM   2697  CB  VAL B 353      32.881  14.722  22.429  1.00 33.81           C  
ANISOU 2697  CB  VAL B 353     5781   3855   3211   -568    281     78       C  
ATOM   2698  CG1 VAL B 353      31.936  13.772  21.702  1.00 33.81           C  
ANISOU 2698  CG1 VAL B 353     5794   3843   3208   -650    271     51       C  
ATOM   2699  CG2 VAL B 353      34.213  14.039  22.701  1.00 33.59           C  
ANISOU 2699  CG2 VAL B 353     5812   3746   3206   -520    291     70       C  
ATOM   2700  N   ILE B 354      31.189  16.527  20.198  1.00 31.66           N  
ANISOU 2700  N   ILE B 354     5393   3757   2879   -607    239     50       N  
ATOM   2701  CA  ILE B 354      29.874  17.046  19.839  1.00 32.49           C  
ANISOU 2701  CA  ILE B 354     5435   3941   2968   -644    217     59       C  
ATOM   2702  C   ILE B 354      29.044  15.885  19.311  1.00 36.31           C  
ANISOU 2702  C   ILE B 354     5933   4416   3448   -729    201     29       C  
ATOM   2703  O   ILE B 354      29.405  15.264  18.306  1.00 35.05           O  
ANISOU 2703  O   ILE B 354     5817   4229   3271   -747    188    -17       O  
ATOM   2704  CB  ILE B 354      29.957  18.171  18.796  1.00 31.13           C  
ANISOU 2704  CB  ILE B 354     5232   3828   2769   -608    198     57       C  
ATOM   2705  CG1 ILE B 354      30.883  19.283  19.289  1.00 31.12           C  
ANISOU 2705  CG1 ILE B 354     5223   3819   2783   -531    212     84       C  
ATOM   2706  CG2 ILE B 354      28.572  18.722  18.499  1.00 30.89           C  
ANISOU 2706  CG2 ILE B 354     5131   3881   2725   -636    169     72       C  
ATOM   2707  CD1 ILE B 354      31.287  20.256  18.212  1.00 32.86           C  
ANISOU 2707  CD1 ILE B 354     5430   4073   2982   -497    200     90       C  
ATOM   2708  N   ILE B 355      27.937  15.595  19.981  1.00 36.31           N  
ANISOU 2708  N   ILE B 355     5893   4440   3463   -783    202     52       N  
ATOM   2709  CA  ILE B 355      27.062  14.483  19.640  1.00 36.16           C  
ANISOU 2709  CA  ILE B 355     5879   4408   3452   -879    184     29       C  
ATOM   2710  C   ILE B 355      25.752  15.055  19.130  1.00 37.15           C  
ANISOU 2710  C   ILE B 355     5917   4637   3563   -916    153     33       C  
ATOM   2711  O   ILE B 355      25.197  15.970  19.742  1.00 38.78           O  
ANISOU 2711  O   ILE B 355     6054   4908   3772   -886    162     72       O  
ATOM   2712  CB  ILE B 355      26.821  13.575  20.858  1.00 37.90           C  
ANISOU 2712  CB  ILE B 355     6119   4573   3709   -923    214     62       C  
ATOM   2713  CG1 ILE B 355      28.152  13.078  21.421  1.00 36.74           C  
ANISOU 2713  CG1 ILE B 355     6055   4328   3576   -873    239     66       C  
ATOM   2714  CG2 ILE B 355      25.903  12.421  20.491  1.00 37.95           C  
ANISOU 2714  CG2 ILE B 355     6128   4556   3734  -1034    195     41       C  
ATOM   2715  CD1 ILE B 355      28.076  12.671  22.872  1.00 36.18           C  
ANISOU 2715  CD1 ILE B 355     5994   4225   3526   -881    272    122       C  
ATOM   2716  N   SER B 356      25.259  14.527  18.016  1.00 38.43           N  
ANISOU 2716  N   SER B 356     6081   4814   3708   -976    112    -12       N  
ATOM   2717  CA  SER B 356      23.929  14.854  17.522  1.00 38.80           C  
ANISOU 2717  CA  SER B 356     6040   4957   3744  -1025     72    -11       C  
ATOM   2718  C   SER B 356      23.031  13.643  17.713  1.00 40.38           C  
ANISOU 2718  C   SER B 356     6230   5134   3977  -1139     62    -25       C  
ATOM   2719  O   SER B 356      23.400  12.525  17.326  1.00 40.53           O  
ANISOU 2719  O   SER B 356     6324   5070   4004  -1190     53    -71       O  
ATOM   2720  CB  SER B 356      23.959  15.264  16.049  1.00 38.69           C  
ANISOU 2720  CB  SER B 356     6027   4996   3678  -1011     22    -50       C  
ATOM   2721  OG  SER B 356      24.168  14.140  15.217  1.00 39.82           O  
ANISOU 2721  OG  SER B 356     6237   5088   3805  -1071     -2   -116       O  
ATOM   2722  N   THR B 357      21.855  13.874  18.298  1.00 37.54           N  
ANISOU 2722  N   THR B 357     5777   4847   3640  -1179     64     14       N  
ATOM   2723  CA  THR B 357      20.960  12.786  18.670  1.00 38.57           C  
ANISOU 2723  CA  THR B 357     5884   4959   3812  -1295     64     17       C  
ATOM   2724  C   THR B 357      19.518  13.270  18.659  1.00 40.17           C  
ANISOU 2724  C   THR B 357     5955   5285   4023  -1336     42     39       C  
ATOM   2725  O   THR B 357      19.245  14.458  18.851  1.00 40.28           O  
ANISOU 2725  O   THR B 357     5897   5385   4021  -1261     48     70       O  
ATOM   2726  CB  THR B 357      21.307  12.233  20.062  1.00 38.54           C  
ANISOU 2726  CB  THR B 357     5919   4881   3844  -1301    128     66       C  
ATOM   2727  OG1 THR B 357      20.375  11.208  20.429  1.00 39.08           O  
ANISOU 2727  OG1 THR B 357     5959   4933   3956  -1422    132     81       O  
ATOM   2728  CG2 THR B 357      21.254  13.342  21.103  1.00 36.86           C  
ANISOU 2728  CG2 THR B 357     5649   4735   3622  -1218    173    124       C  
ATOM   2729  N   LYS B 358      18.595  12.338  18.428  1.00 44.41           N  
ANISOU 2729  N   LYS B 358     6457   5826   4591  -1457     14     22       N  
ATOM   2730  CA  LYS B 358      17.191  12.594  18.714  1.00 46.76           C  
ANISOU 2730  CA  LYS B 358     6618   6235   4913  -1511      7     55       C  
ATOM   2731  C   LYS B 358      16.948  12.414  20.206  1.00 46.74           C  
ANISOU 2731  C   LYS B 358     6588   6224   4946  -1526     86    123       C  
ATOM   2732  O   LYS B 358      17.488  11.497  20.830  1.00 45.48           O  
ANISOU 2732  O   LYS B 358     6512   5959   4810  -1564    123    138       O  
ATOM   2733  CB  LYS B 358      16.278  11.660  17.915  1.00 48.62           C  
ANISOU 2733  CB  LYS B 358     6817   6483   5173  -1646    -55     10       C  
ATOM   2734  CG  LYS B 358      14.790  11.954  18.107  1.00 50.35           C  
ANISOU 2734  CG  LYS B 358     6877   6833   5421  -1704    -69     42       C  
ATOM   2735  CD  LYS B 358      13.899  10.896  17.471  1.00 52.49           C  
ANISOU 2735  CD  LYS B 358     7110   7104   5728  -1856   -129      0       C  
ATOM   2736  CE  LYS B 358      14.000   9.563  18.197  1.00 54.80           C  
ANISOU 2736  CE  LYS B 358     7466   7276   6080  -1967    -87     14       C  
ATOM   2737  NZ  LYS B 358      13.401   9.610  19.561  1.00 55.94           N  
ANISOU 2737  NZ  LYS B 358     7531   7460   6265  -1990     -7    102       N  
ATOM   2738  N   VAL B 359      16.144  13.302  20.779  1.00 46.60           N  
ANISOU 2738  N   VAL B 359     6454   6322   4931  -1488    111    167       N  
ATOM   2739  CA  VAL B 359      15.894  13.313  22.215  1.00 44.29           C  
ANISOU 2739  CA  VAL B 359     6128   6045   4654  -1484    192    232       C  
ATOM   2740  C   VAL B 359      14.658  12.461  22.486  1.00 47.12           C  
ANISOU 2740  C   VAL B 359     6397   6446   5061  -1622    201    258       C  
ATOM   2741  O   VAL B 359      13.538  12.846  22.141  1.00 50.15           O  
ANISOU 2741  O   VAL B 359     6650   6946   5458  -1650    174    257       O  
ATOM   2742  CB  VAL B 359      15.723  14.743  22.740  1.00 46.35           C  
ANISOU 2742  CB  VAL B 359     6315   6405   4890  -1361    221    257       C  
ATOM   2743  CG1 VAL B 359      15.560  14.741  24.243  1.00 46.24           C  
ANISOU 2743  CG1 VAL B 359     6280   6410   4878  -1349    308    316       C  
ATOM   2744  CG2 VAL B 359      16.918  15.594  22.339  1.00 43.26           C  
ANISOU 2744  CG2 VAL B 359     6007   5967   4460  -1239    202    231       C  
ATOM   2745  N   ARG B 360      14.868  11.293  23.103  1.00 58.46           N  
ANISOU 2745  N   ARG B 360     7900   7785   6526  -1709    238    285       N  
ATOM   2746  CA  ARG B 360      13.773  10.354  23.337  1.00 60.62           C  
ANISOU 2746  CA  ARG B 360     8100   8077   6854  -1859    248    315       C  
ATOM   2747  C   ARG B 360      12.726  10.943  24.273  1.00 58.53           C  
ANISOU 2747  C   ARG B 360     7692   7953   6594  -1853    310    378       C  
ATOM   2748  O   ARG B 360      11.519  10.801  24.041  1.00 59.37           O  
ANISOU 2748  O   ARG B 360     7668   8152   6737  -1942    294    384       O  
ATOM   2749  CB  ARG B 360      14.327   9.045  23.901  1.00 63.61           C  
ANISOU 2749  CB  ARG B 360     8595   8309   7265  -1940    281    344       C  
ATOM   2750  CG  ARG B 360      13.267   8.052  24.358  1.00 65.59           C  
ANISOU 2750  CG  ARG B 360     8778   8565   7578  -2100    306    394       C  
ATOM   2751  CD  ARG B 360      13.675   6.614  24.066  1.00 66.17           C  
ANISOU 2751  CD  ARG B 360     8970   8469   7701  -2212    280    377       C  
ATOM   2752  NE  ARG B 360      15.090   6.370  24.337  1.00 67.14           N  
ANISOU 2752  NE  ARG B 360     9253   8457   7800  -2127    296    374       N  
ATOM   2753  CZ  ARG B 360      15.656   5.167  24.330  1.00 68.17           C  
ANISOU 2753  CZ  ARG B 360     9506   8424   7972  -2192    288    372       C  
ATOM   2754  NH1 ARG B 360      14.925   4.091  24.069  1.00 69.77           N  
ANISOU 2754  NH1 ARG B 360     9696   8569   8245  -2350    264    369       N  
ATOM   2755  NH2 ARG B 360      16.952   5.037  24.584  1.00 66.52           N  
ANISOU 2755  NH2 ARG B 360     9430   8105   7739  -2098    302    370       N  
ATOM   2756  N   TYR B 361      13.171  11.594  25.342  1.00 44.41           N  
ANISOU 2756  N   TYR B 361     5920   6184   4767  -1750    382    422       N  
ATOM   2757  CA  TYR B 361      12.284  12.274  26.274  1.00 44.38           C  
ANISOU 2757  CA  TYR B 361     5789   6318   4754  -1719    450    473       C  
ATOM   2758  C   TYR B 361      13.087  13.370  26.956  1.00 43.74           C  
ANISOU 2758  C   TYR B 361     5754   6250   4615  -1557    490    475       C  
ATOM   2759  O   TYR B 361      14.298  13.487  26.759  1.00 43.75           O  
ANISOU 2759  O   TYR B 361     5881   6152   4591  -1488    467    448       O  
ATOM   2760  CB  TYR B 361      11.680  11.300  27.293  1.00 46.54           C  
ANISOU 2760  CB  TYR B 361     6033   6595   5056  -1837    525    549       C  
ATOM   2761  CG  TYR B 361      12.668  10.297  27.853  1.00 45.88           C  
ANISOU 2761  CG  TYR B 361     6105   6358   4969  -1872    553    583       C  
ATOM   2762  CD1 TYR B 361      13.782  10.713  28.572  1.00 44.10           C  
ANISOU 2762  CD1 TYR B 361     5986   6083   4689  -1754    589    596       C  
ATOM   2763  CD2 TYR B 361      12.484   8.932  27.667  1.00 48.12           C  
ANISOU 2763  CD2 TYR B 361     6430   6544   5311  -2024    540    603       C  
ATOM   2764  CE1 TYR B 361      14.687   9.802  29.085  1.00 46.66           C  
ANISOU 2764  CE1 TYR B 361     6446   6270   5011  -1777    609    631       C  
ATOM   2765  CE2 TYR B 361      13.385   8.011  28.180  1.00 49.68           C  
ANISOU 2765  CE2 TYR B 361     6773   6594   5512  -2048    562    639       C  
ATOM   2766  CZ  TYR B 361      14.485   8.454  28.890  1.00 47.72           C  
ANISOU 2766  CZ  TYR B 361     6622   6305   5204  -1921    597    655       C  
ATOM   2767  OH  TYR B 361      15.391   7.554  29.406  1.00 46.38           O  
ANISOU 2767  OH  TYR B 361     6592   5994   5037  -1935    614    694       O  
ATOM   2768  N   GLY B 362      12.397  14.173  27.764  1.00 43.46           N  
ANISOU 2768  N   GLY B 362     5612   6339   4561  -1498    549    505       N  
ATOM   2769  CA  GLY B 362      13.025  15.293  28.442  1.00 39.21           C  
ANISOU 2769  CA  GLY B 362     5106   5823   3971  -1346    584    498       C  
ATOM   2770  C   GLY B 362      14.303  14.934  29.174  1.00 39.95           C  
ANISOU 2770  C   GLY B 362     5351   5801   4027  -1311    614    516       C  
ATOM   2771  O   GLY B 362      14.320  14.002  29.982  1.00 38.52           O  
ANISOU 2771  O   GLY B 362     5208   5585   3843  -1385    667    572       O  
ATOM   2772  N   GLY B 363      15.385  15.655  28.884  1.00 41.02           N  
ANISOU 2772  N   GLY B 363     5572   5878   4138  -1201    579    473       N  
ATOM   2773  CA  GLY B 363      16.659  15.431  29.537  1.00 39.17           C  
ANISOU 2773  CA  GLY B 363     5472   5543   3869  -1155    597    484       C  
ATOM   2774  C   GLY B 363      17.537  14.365  28.916  1.00 40.47           C  
ANISOU 2774  C   GLY B 363     5753   5566   4057  -1218    555    474       C  
ATOM   2775  O   GLY B 363      18.659  14.160  29.395  1.00 36.58           O  
ANISOU 2775  O   GLY B 363     5370   4986   3541  -1173    563    482       O  
ATOM   2776  N   TYR B 364      17.076  13.698  27.855  1.00 46.61           N  
ANISOU 2776  N   TYR B 364     6511   6321   4879  -1314    505    452       N  
ATOM   2777  CA  TYR B 364      17.798  12.559  27.289  1.00 46.99           C  
ANISOU 2777  CA  TYR B 364     6669   6232   4953  -1381    469    437       C  
ATOM   2778  C   TYR B 364      19.191  12.940  26.790  1.00 47.27           C  
ANISOU 2778  C   TYR B 364     6810   6184   4967  -1284    432    390       C  
ATOM   2779  O   TYR B 364      20.100  12.097  26.778  1.00 46.81           O  
ANISOU 2779  O   TYR B 364     6861   6006   4918  -1300    425    389       O  
ATOM   2780  CB  TYR B 364      16.962  11.957  26.160  1.00 49.41           C  
ANISOU 2780  CB  TYR B 364     6923   6547   5305  -1493    415    404       C  
ATOM   2781  CG  TYR B 364      17.525  10.714  25.521  1.00 52.17           C  
ANISOU 2781  CG  TYR B 364     7378   6757   5687  -1573    376    377       C  
ATOM   2782  CD1 TYR B 364      17.377   9.472  26.122  1.00 53.68           C  
ANISOU 2782  CD1 TYR B 364     7613   6869   5915  -1678    407    426       C  
ATOM   2783  CD2 TYR B 364      18.175  10.778  24.296  1.00 52.19           C  
ANISOU 2783  CD2 TYR B 364     7439   6708   5685  -1544    309    304       C  
ATOM   2784  CE1 TYR B 364      17.881   8.330  25.530  1.00 54.68           C  
ANISOU 2784  CE1 TYR B 364     7840   6856   6078  -1747    370    395       C  
ATOM   2785  CE2 TYR B 364      18.680   9.644  23.696  1.00 51.38           C  
ANISOU 2785  CE2 TYR B 364     7435   6479   5610  -1610    276    268       C  
ATOM   2786  CZ  TYR B 364      18.532   8.423  24.317  1.00 54.73           C  
ANISOU 2786  CZ  TYR B 364     7902   6815   6077  -1709    304    310       C  
ATOM   2787  OH  TYR B 364      19.037   7.290  23.722  1.00 56.06           O  
ANISOU 2787  OH  TYR B 364     8174   6845   6280  -1768    269    269       O  
ATOM   2788  N   ALA B 365      19.377  14.196  26.373  1.00 43.09           N  
ANISOU 2788  N   ALA B 365     6246   5712   4414  -1184    408    355       N  
ATOM   2789  CA  ALA B 365      20.679  14.627  25.869  1.00 40.35           C  
ANISOU 2789  CA  ALA B 365     5986   5294   4050  -1097    376    316       C  
ATOM   2790  C   ALA B 365      21.758  14.490  26.937  1.00 39.27           C  
ANISOU 2790  C   ALA B 365     5937   5089   3893  -1041    414    343       C  
ATOM   2791  O   ALA B 365      22.887  14.063  26.648  1.00 39.45           O  
ANISOU 2791  O   ALA B 365     6057   5014   3919  -1020    395    324       O  
ATOM   2792  CB  ALA B 365      20.590  16.069  25.374  1.00 40.60           C  
ANISOU 2792  CB  ALA B 365     5959   5403   4065  -1004    351    288       C  
ATOM   2793  N   LYS B 366      21.426  14.843  28.181  1.00 41.00           N  
ANISOU 2793  N   LYS B 366     6124   5367   4088  -1013    468    387       N  
ATOM   2794  CA  LYS B 366      22.369  14.651  29.275  1.00 41.09           C  
ANISOU 2794  CA  LYS B 366     6217   5325   4072   -965    499    417       C  
ATOM   2795  C   LYS B 366      22.683  13.174  29.483  1.00 39.68           C  
ANISOU 2795  C   LYS B 366     6119   5045   3914  -1046    508    454       C  
ATOM   2796  O   LYS B 366      23.812  12.827  29.841  1.00 39.16           O  
ANISOU 2796  O   LYS B 366     6146   4893   3840  -1005    504    462       O  
ATOM   2797  CB  LYS B 366      21.817  15.274  30.559  1.00 42.30           C  
ANISOU 2797  CB  LYS B 366     6315   5574   4183   -925    557    454       C  
ATOM   2798  CG  LYS B 366      21.440  16.742  30.416  1.00 42.91           C  
ANISOU 2798  CG  LYS B 366     6312   5744   4246   -838    550    415       C  
ATOM   2799  CD  LYS B 366      22.504  17.654  31.001  1.00 42.87           C  
ANISOU 2799  CD  LYS B 366     6361   5721   4209   -724    546    393       C  
ATOM   2800  CE  LYS B 366      22.073  19.111  30.930  1.00 44.99           C  
ANISOU 2800  CE  LYS B 366     6554   6069   4472   -639    541    355       C  
ATOM   2801  NZ  LYS B 366      22.729  19.941  31.978  1.00 45.60           N  
ANISOU 2801  NZ  LYS B 366     6664   6154   4508   -541    558    341       N  
ATOM   2802  N   GLY B 367      21.708  12.291  29.252  1.00 37.13           N  
ANISOU 2802  N   GLY B 367     5761   4724   3624  -1162    515    476       N  
ATOM   2803  CA  GLY B 367      21.985  10.865  29.339  1.00 37.59           C  
ANISOU 2803  CA  GLY B 367     5901   4667   3714  -1244    516    508       C  
ATOM   2804  C   GLY B 367      22.956  10.396  28.272  1.00 38.96           C  
ANISOU 2804  C   GLY B 367     6161   4726   3917  -1233    461    449       C  
ATOM   2805  O   GLY B 367      23.841   9.575  28.538  1.00 39.23           O  
ANISOU 2805  O   GLY B 367     6295   4647   3964  -1228    460    465       O  
ATOM   2806  N   VAL B 368      22.802  10.907  27.047  1.00 36.97           N  
ANISOU 2806  N   VAL B 368     5870   4503   3672  -1226    415    381       N  
ATOM   2807  CA  VAL B 368      23.763  10.600  25.988  1.00 36.49           C  
ANISOU 2807  CA  VAL B 368     5887   4352   3625  -1202    369    318       C  
ATOM   2808  C   VAL B 368      25.162  11.059  26.388  1.00 34.89           C  
ANISOU 2808  C   VAL B 368     5752   4108   3399  -1087    374    316       C  
ATOM   2809  O   VAL B 368      26.156  10.339  26.196  1.00 34.50           O  
ANISOU 2809  O   VAL B 368     5793   3951   3366  -1070    362    301       O  
ATOM   2810  CB  VAL B 368      23.315  11.241  24.661  1.00 38.09           C  
ANISOU 2810  CB  VAL B 368     6030   4620   3822  -1204    322    254       C  
ATOM   2811  CG1 VAL B 368      24.394  11.081  23.597  1.00 38.22           C  
ANISOU 2811  CG1 VAL B 368     6124   4561   3835  -1163    283    190       C  
ATOM   2812  CG2 VAL B 368      22.002  10.631  24.195  1.00 40.00           C  
ANISOU 2812  CG2 VAL B 368     6210   4896   4094  -1327    304    249       C  
ATOM   2813  N   ALA B 369      25.261  12.265  26.952  1.00 40.13           N  
ANISOU 2813  N   ALA B 369     6369   4853   4026  -1004    390    328       N  
ATOM   2814  CA  ALA B 369      26.563  12.762  27.391  1.00 37.97           C  
ANISOU 2814  CA  ALA B 369     6149   4545   3732   -901    391    326       C  
ATOM   2815  C   ALA B 369      27.142  11.899  28.510  1.00 38.59           C  
ANISOU 2815  C   ALA B 369     6302   4552   3810   -899    416    379       C  
ATOM   2816  O   ALA B 369      28.352  11.644  28.543  1.00 38.64           O  
ANISOU 2816  O   ALA B 369     6379   4481   3822   -844    402    370       O  
ATOM   2817  CB  ALA B 369      26.450  14.220  27.836  1.00 36.61           C  
ANISOU 2817  CB  ALA B 369     5913   4470   3526   -823    400    324       C  
ATOM   2818  N   PHE B 370      26.292  11.447  29.440  1.00 37.84           N  
ANISOU 2818  N   PHE B 370     6186   4485   3706   -957    454    441       N  
ATOM   2819  CA  PHE B 370      26.739  10.529  30.487  1.00 38.28           C  
ANISOU 2819  CA  PHE B 370     6316   4471   3757   -966    478    506       C  
ATOM   2820  C   PHE B 370      27.311   9.253  29.883  1.00 38.73           C  
ANISOU 2820  C   PHE B 370     6460   4390   3866  -1006    452    496       C  
ATOM   2821  O   PHE B 370      28.359   8.753  30.324  1.00 37.90           O  
ANISOU 2821  O   PHE B 370     6436   4201   3765   -957    446    517       O  
ATOM   2822  CB  PHE B 370      25.578  10.180  31.424  1.00 38.40           C  
ANISOU 2822  CB  PHE B 370     6289   4545   3755  -1041    528    580       C  
ATOM   2823  CG  PHE B 370      25.099  11.326  32.276  1.00 40.40           C  
ANISOU 2823  CG  PHE B 370     6470   4931   3950   -987    564    594       C  
ATOM   2824  CD1 PHE B 370      25.939  12.382  32.588  1.00 40.62           C  
ANISOU 2824  CD1 PHE B 370     6506   4990   3940   -873    550    562       C  
ATOM   2825  CD2 PHE B 370      23.800  11.342  32.767  1.00 39.91           C  
ANISOU 2825  CD2 PHE B 370     6328   4963   3874  -1052    612    636       C  
ATOM   2826  CE1 PHE B 370      25.492  13.433  33.374  1.00 41.19           C  
ANISOU 2826  CE1 PHE B 370     6516   5175   3959   -821    581    565       C  
ATOM   2827  CE2 PHE B 370      23.348  12.389  33.553  1.00 40.71           C  
ANISOU 2827  CE2 PHE B 370     6362   5187   3918   -994    649    642       C  
ATOM   2828  CZ  PHE B 370      24.195  13.434  33.858  1.00 41.56           C  
ANISOU 2828  CZ  PHE B 370     6489   5316   3988   -876    632    602       C  
ATOM   2829  N   ARG B 371      26.625   8.706  28.876  1.00 38.50           N  
ANISOU 2829  N   ARG B 371     6415   4334   3878  -1093    435    461       N  
ATOM   2830  CA  ARG B 371      27.113   7.498  28.219  1.00 39.69           C  
ANISOU 2830  CA  ARG B 371     6650   4348   4081  -1132    408    435       C  
ATOM   2831  C   ARG B 371      28.485   7.730  27.604  1.00 38.69           C  
ANISOU 2831  C   ARG B 371     6577   4168   3954  -1032    379    375       C  
ATOM   2832  O   ARG B 371      29.395   6.909  27.767  1.00 38.59           O  
ANISOU 2832  O   ARG B 371     6651   4044   3968  -1003    372    383       O  
ATOM   2833  CB  ARG B 371      26.124   7.027  27.154  1.00 41.06           C  
ANISOU 2833  CB  ARG B 371     6791   4518   4292  -1240    386    389       C  
ATOM   2834  CG  ARG B 371      26.489   5.672  26.568  1.00 44.19           C  
ANISOU 2834  CG  ARG B 371     7282   4764   4746  -1292    360    360       C  
ATOM   2835  CD  ARG B 371      26.416   4.590  27.634  1.00 46.18           C  
ANISOU 2835  CD  ARG B 371     7594   4922   5029  -1344    388    449       C  
ATOM   2836  NE  ARG B 371      27.088   3.353  27.240  1.00 50.78           N  
ANISOU 2836  NE  ARG B 371     8287   5337   5671  -1358    364    424       N  
ATOM   2837  CZ  ARG B 371      28.347   3.051  27.548  1.00 53.82           C  
ANISOU 2837  CZ  ARG B 371     8755   5633   6060  -1263    360    432       C  
ATOM   2838  NH1 ARG B 371      29.083   3.899  28.254  1.00 52.65           N  
ANISOU 2838  NH1 ARG B 371     8593   5550   5860  -1155    375    463       N  
ATOM   2839  NH2 ARG B 371      28.871   1.897  27.151  1.00 55.84           N  
ANISOU 2839  NH2 ARG B 371     9108   5733   6376  -1274    338    406       N  
ATOM   2840  N   LEU B 372      28.657   8.849  26.896  1.00 39.33           N  
ANISOU 2840  N   LEU B 372     6606   4329   4009   -977    362    320       N  
ATOM   2841  CA  LEU B 372      29.974   9.144  26.336  1.00 40.10           C  
ANISOU 2841  CA  LEU B 372     6744   4389   4105   -884    342    270       C  
ATOM   2842  C   LEU B 372      31.023   9.234  27.438  1.00 40.14           C  
ANISOU 2842  C   LEU B 372     6789   4365   4099   -800    353    315       C  
ATOM   2843  O   LEU B 372      32.120   8.676  27.317  1.00 40.86           O  
ANISOU 2843  O   LEU B 372     6944   4368   4212   -750    341    301       O  
ATOM   2844  CB  LEU B 372      29.954  10.436  25.524  1.00 39.77           C  
ANISOU 2844  CB  LEU B 372     6635   4443   4034   -842    328    221       C  
ATOM   2845  CG  LEU B 372      31.348  10.714  24.949  1.00 40.85           C  
ANISOU 2845  CG  LEU B 372     6808   4543   4171   -753    314    177       C  
ATOM   2846  CD1 LEU B 372      31.439  10.268  23.496  1.00 41.28           C  
ANISOU 2846  CD1 LEU B 372     6885   4564   4236   -779    293    105       C  
ATOM   2847  CD2 LEU B 372      31.746  12.171  25.099  1.00 39.74           C  
ANISOU 2847  CD2 LEU B 372     6612   4486   4001   -678    314    177       C  
ATOM   2848  N   LEU B 373      30.691   9.920  28.532  1.00 40.70           N  
ANISOU 2848  N   LEU B 373     6819   4513   4132   -781    375    367       N  
ATOM   2849  CA  LEU B 373      31.626  10.080  29.637  1.00 39.72           C  
ANISOU 2849  CA  LEU B 373     6728   4377   3985   -702    378    409       C  
ATOM   2850  C   LEU B 373      31.829   8.803  30.443  1.00 40.68           C  
ANISOU 2850  C   LEU B 373     6927   4405   4123   -725    387    474       C  
ATOM   2851  O   LEU B 373      32.608   8.827  31.401  1.00 40.87           O  
ANISOU 2851  O   LEU B 373     6984   4419   4124   -659    384    516       O  
ATOM   2852  CB  LEU B 373      31.161  11.210  30.558  1.00 38.81           C  
ANISOU 2852  CB  LEU B 373     6552   4378   3817   -673    397    435       C  
ATOM   2853  CG  LEU B 373      31.221  12.607  29.937  1.00 38.95           C  
ANISOU 2853  CG  LEU B 373     6504   4474   3822   -626    383    377       C  
ATOM   2854  CD1 LEU B 373      30.477  13.612  30.798  1.00 39.53           C  
ANISOU 2854  CD1 LEU B 373     6515   4655   3850   -610    406    397       C  
ATOM   2855  CD2 LEU B 373      32.663  13.040  29.731  1.00 37.85           C  
ANISOU 2855  CD2 LEU B 373     6390   4301   3692   -538    355    344       C  
ATOM   2856  N   SER B 374      31.153   7.702  30.105  1.00 33.56           N  
ANISOU 2856  N   SER B 374     6057   3434   3261   -816    393    488       N  
ATOM   2857  CA  SER B 374      31.464   6.411  30.711  1.00 33.64           C  
ANISOU 2857  CA  SER B 374     6154   3328   3301   -836    396    550       C  
ATOM   2858  C   SER B 374      32.017   5.395  29.709  1.00 34.94           C  
ANISOU 2858  C   SER B 374     6386   3357   3531   -844    369    497       C  
ATOM   2859  O   SER B 374      31.995   4.192  29.985  1.00 35.71           O  
ANISOU 2859  O   SER B 374     6556   3340   3671   -885    370    540       O  
ATOM   2860  CB  SER B 374      30.237   5.840  31.420  1.00 36.40           C  
ANISOU 2860  CB  SER B 374     6494   3689   3646   -941    431    629       C  
ATOM   2861  OG  SER B 374      29.078   5.980  30.626  1.00 37.03           O  
ANISOU 2861  OG  SER B 374     6509   3818   3743  -1033    437    590       O  
ATOM   2862  N   THR B 375      32.530   5.853  28.548  1.00 36.10           N  
ANISOU 2862  N   THR B 375     6515   3514   3687   -802    348    405       N  
ATOM   2863  CA  THR B 375      33.200   4.955  27.613  1.00 36.77           C  
ANISOU 2863  CA  THR B 375     6666   3480   3825   -789    327    343       C  
ATOM   2864  C   THR B 375      34.687   4.865  27.940  1.00 37.55           C  
ANISOU 2864  C   THR B 375     6810   3526   3933   -670    315    347       C  
ATOM   2865  O   THR B 375      35.237   5.748  28.604  1.00 36.52           O  
ANISOU 2865  O   THR B 375     6643   3470   3764   -599    315    373       O  
ATOM   2866  CB  THR B 375      33.014   5.447  26.175  1.00 36.17           C  
ANISOU 2866  CB  THR B 375     6550   3450   3743   -802    313    244       C  
ATOM   2867  OG1 THR B 375      33.556   6.766  26.041  1.00 35.66           O  
ANISOU 2867  OG1 THR B 375     6424   3490   3635   -723    314    222       O  
ATOM   2868  CG2 THR B 375      31.543   5.460  25.788  1.00 37.08           C  
ANISOU 2868  CG2 THR B 375     6618   3617   3855   -919    315    237       C  
ATOM   2869  N   PRO B 376      35.375   3.804  27.493  1.00 44.91           N  
ANISOU 2869  N   PRO B 376     7817   4326   4919   -645    301    316       N  
ATOM   2870  CA  PRO B 376      36.814   3.694  27.804  1.00 44.71           C  
ANISOU 2870  CA  PRO B 376     7824   4255   4908   -525    288    320       C  
ATOM   2871  C   PRO B 376      37.634   4.897  27.366  1.00 44.35           C  
ANISOU 2871  C   PRO B 376     7711   4309   4830   -442    286    268       C  
ATOM   2872  O   PRO B 376      38.579   5.281  28.067  1.00 45.89           O  
ANISOU 2872  O   PRO B 376     7895   4527   5016   -355    276    300       O  
ATOM   2873  CB  PRO B 376      37.234   2.421  27.057  1.00 45.86           C  
ANISOU 2873  CB  PRO B 376     8052   4250   5121   -518    278    269       C  
ATOM   2874  CG  PRO B 376      35.992   1.617  26.963  1.00 45.26           C  
ANISOU 2874  CG  PRO B 376     8011   4114   5071   -645    282    285       C  
ATOM   2875  CD  PRO B 376      34.872   2.604  26.798  1.00 44.89           C  
ANISOU 2875  CD  PRO B 376     7877   4206   4971   -723    294    281       C  
ATOM   2876  N   HIS B 377      37.304   5.504  26.227  1.00 39.62           N  
ANISOU 2876  N   HIS B 377     7066   3773   4215   -468    291    193       N  
ATOM   2877  CA  HIS B 377      38.015   6.696  25.781  1.00 39.03           C  
ANISOU 2877  CA  HIS B 377     6926   3793   4111   -401    292    153       C  
ATOM   2878  C   HIS B 377      37.373   7.980  26.292  1.00 37.67           C  
ANISOU 2878  C   HIS B 377     6679   3746   3889   -423    296    187       C  
ATOM   2879  O   HIS B 377      38.081   8.889  26.738  1.00 36.94           O  
ANISOU 2879  O   HIS B 377     6546   3712   3778   -357    291    199       O  
ATOM   2880  CB  HIS B 377      38.087   6.732  24.251  1.00 42.50           C  
ANISOU 2880  CB  HIS B 377     7358   4239   4550   -408    298     60       C  
ATOM   2881  CG  HIS B 377      38.874   7.888  23.712  1.00 42.37           C  
ANISOU 2881  CG  HIS B 377     7278   4311   4508   -343    304     27       C  
ATOM   2882  ND1 HIS B 377      40.231   7.822  23.483  1.00 43.07           N  
ANISOU 2882  ND1 HIS B 377     7369   4375   4619   -251    308      0       N  
ATOM   2883  CD2 HIS B 377      38.495   9.141  23.367  1.00 42.46           C  
ANISOU 2883  CD2 HIS B 377     7220   4434   4479   -358    307     21       C  
ATOM   2884  CE1 HIS B 377      40.653   8.983  23.013  1.00 43.05           C  
ANISOU 2884  CE1 HIS B 377     7300   4466   4590   -221    316    -18       C  
ATOM   2885  NE2 HIS B 377      39.619   9.801  22.935  1.00 41.70           N  
ANISOU 2885  NE2 HIS B 377     7089   4372   4382   -284    314     -4       N  
ATOM   2886  N   GLY B 378      36.044   8.073  26.234  1.00 36.74           N  
ANISOU 2886  N   GLY B 378     6540   3668   3752   -513    304    198       N  
ATOM   2887  CA  GLY B 378      35.381   9.301  26.635  1.00 35.11           C  
ANISOU 2887  CA  GLY B 378     6260   3579   3501   -526    310    221       C  
ATOM   2888  C   GLY B 378      35.539   9.620  28.107  1.00 35.59           C  
ANISOU 2888  C   GLY B 378     6316   3668   3538   -492    313    292       C  
ATOM   2889  O   GLY B 378      35.609  10.792  28.486  1.00 35.29           O  
ANISOU 2889  O   GLY B 378     6225   3717   3468   -456    312    295       O  
ATOM   2890  N   MET B 379      35.611   8.591  28.953  1.00 43.39           N  
ANISOU 2890  N   MET B 379     7365   4581   4540   -501    315    349       N  
ATOM   2891  CA  MET B 379      35.689   8.818  30.395  1.00 44.14           C  
ANISOU 2891  CA  MET B 379     7463   4711   4598   -472    318    421       C  
ATOM   2892  C   MET B 379      36.920   9.620  30.799  1.00 43.50           C  
ANISOU 2892  C   MET B 379     7363   4663   4502   -370    294    410       C  
ATOM   2893  O   MET B 379      36.764  10.613  31.531  1.00 42.93           O  
ANISOU 2893  O   MET B 379     7248   4679   4383   -349    294    425       O  
ATOM   2894  CB  MET B 379      35.607   7.472  31.128  1.00 43.41           C  
ANISOU 2894  CB  MET B 379     7448   4522   4524   -499    322    492       C  
ATOM   2895  CG  MET B 379      35.720   7.548  32.637  1.00 44.95           C  
ANISOU 2895  CG  MET B 379     7659   4750   4671   -469    324    577       C  
ATOM   2896  SD  MET B 379      35.095   6.047  33.424  1.00 46.49           S  
ANISOU 2896  SD  MET B 379     7935   4850   4879   -541    343    680       S  
ATOM   2897  CE  MET B 379      35.710   4.788  32.304  1.00 47.44           C  
ANISOU 2897  CE  MET B 379     8126   4804   5093   -541    321    634       C  
ATOM   2898  N   PRO B 380      38.152   9.280  30.372  1.00 38.53           N  
ANISOU 2898  N   PRO B 380     6758   3970   3910   -303    274    381       N  
ATOM   2899  CA  PRO B 380      39.294  10.122  30.755  1.00 38.14           C  
ANISOU 2899  CA  PRO B 380     6675   3964   3852   -215    249    370       C  
ATOM   2900  C   PRO B 380      39.566  11.277  29.798  1.00 39.73           C  
ANISOU 2900  C   PRO B 380     6810   4229   4058   -200    249    303       C  
ATOM   2901  O   PRO B 380      40.108  12.303  30.219  1.00 39.69           O  
ANISOU 2901  O   PRO B 380     6760   4282   4036   -154    232    297       O  
ATOM   2902  CB  PRO B 380      40.460   9.128  30.777  1.00 39.40           C  
ANISOU 2902  CB  PRO B 380     6885   4027   4056   -151    228    377       C  
ATOM   2903  CG  PRO B 380      40.102   8.124  29.753  1.00 39.44           C  
ANISOU 2903  CG  PRO B 380     6934   3947   4104   -196    247    345       C  
ATOM   2904  CD  PRO B 380      38.598   8.028  29.729  1.00 39.02           C  
ANISOU 2904  CD  PRO B 380     6882   3915   4028   -300    270    364       C  
ATOM   2905  N   TYR B 381      39.196  11.150  28.524  1.00 39.96           N  
ANISOU 2905  N   TYR B 381     6831   4244   4106   -239    266    254       N  
ATOM   2906  CA  TYR B 381      39.593  12.162  27.546  1.00 39.11           C  
ANISOU 2906  CA  TYR B 381     6668   4190   4003   -219    268    200       C  
ATOM   2907  C   TYR B 381      38.592  13.311  27.430  1.00 38.63           C  
ANISOU 2907  C   TYR B 381     6552   4217   3907   -261    275    196       C  
ATOM   2908  O   TYR B 381      38.979  14.482  27.510  1.00 36.40           O  
ANISOU 2908  O   TYR B 381     6221   3991   3619   -227    265    186       O  
ATOM   2909  CB  TYR B 381      39.801  11.519  26.170  1.00 40.02           C  
ANISOU 2909  CB  TYR B 381     6804   4259   4145   -229    282    146       C  
ATOM   2910  CG  TYR B 381      41.184  10.937  25.967  1.00 42.88           C  
ANISOU 2910  CG  TYR B 381     7187   4561   4546   -154    277    126       C  
ATOM   2911  CD1 TYR B 381      41.463   9.623  26.317  1.00 44.02           C  
ANISOU 2911  CD1 TYR B 381     7398   4607   4720   -137    272    141       C  
ATOM   2912  CD2 TYR B 381      42.209  11.703  25.421  1.00 43.83           C  
ANISOU 2912  CD2 TYR B 381     7256   4721   4676   -100    280     94       C  
ATOM   2913  CE1 TYR B 381      42.723   9.087  26.132  1.00 45.34           C  
ANISOU 2913  CE1 TYR B 381     7580   4721   4928    -58    268    121       C  
ATOM   2914  CE2 TYR B 381      43.473  11.174  25.233  1.00 43.25           C  
ANISOU 2914  CE2 TYR B 381     7189   4603   4640    -28    280     75       C  
ATOM   2915  CZ  TYR B 381      43.723   9.866  25.590  1.00 44.63           C  
ANISOU 2915  CZ  TYR B 381     7429   4683   4845     -2    274     86       C  
ATOM   2916  OH  TYR B 381      44.976   9.331  25.406  1.00 46.99           O  
ANISOU 2916  OH  TYR B 381     7730   4938   5187     80    274     65       O  
ATOM   2917  N   SER B 382      37.312  12.998  27.239  1.00 36.03           N  
ANISOU 2917  N   SER B 382     6228   3899   3563   -334    289    203       N  
ATOM   2918  CA  SER B 382      36.327  14.009  26.870  1.00 35.60           C  
ANISOU 2918  CA  SER B 382     6116   3926   3484   -369    294    192       C  
ATOM   2919  C   SER B 382      36.056  14.962  28.032  1.00 37.78           C  
ANISOU 2919  C   SER B 382     6357   4265   3731   -347    292    223       C  
ATOM   2920  O   SER B 382      35.532  14.551  29.072  1.00 39.16           O  
ANISOU 2920  O   SER B 382     6550   4444   3884   -364    301    265       O  
ATOM   2921  CB  SER B 382      35.038  13.331  26.420  1.00 36.80           C  
ANISOU 2921  CB  SER B 382     6275   4075   3631   -454    306    192       C  
ATOM   2922  OG  SER B 382      35.279  12.486  25.308  1.00 38.49           O  
ANISOU 2922  OG  SER B 382     6526   4231   3868   -474    304    151       O  
ATOM   2923  N   LYS B 383      36.395  16.237  27.843  1.00 35.02           N  
ANISOU 2923  N   LYS B 383     5961   3965   3380   -308    281    201       N  
ATOM   2924  CA  LYS B 383      36.161  17.279  28.838  1.00 35.00           C  
ANISOU 2924  CA  LYS B 383     5926   4019   3353   -281    274    213       C  
ATOM   2925  C   LYS B 383      34.963  18.160  28.505  1.00 35.86           C  
ANISOU 2925  C   LYS B 383     5983   4195   3447   -309    284    205       C  
ATOM   2926  O   LYS B 383      34.180  18.493  29.400  1.00 37.10           O  
ANISOU 2926  O   LYS B 383     6122   4399   3575   -311    295    222       O  
ATOM   2927  CB  LYS B 383      37.409  18.156  28.989  1.00 33.89           C  
ANISOU 2927  CB  LYS B 383     5769   3877   3230   -217    249    194       C  
ATOM   2928  CG  LYS B 383      37.242  19.323  29.957  1.00 33.50           C  
ANISOU 2928  CG  LYS B 383     5691   3879   3159   -186    235    191       C  
ATOM   2929  CD  LYS B 383      38.552  20.072  30.158  1.00 34.19           C  
ANISOU 2929  CD  LYS B 383     5765   3955   3273   -132    203    170       C  
ATOM   2930  CE  LYS B 383      39.076  20.641  28.843  1.00 33.39           C  
ANISOU 2930  CE  LYS B 383     5631   3841   3214   -134    202    147       C  
ATOM   2931  NZ  LYS B 383      40.402  21.305  29.006  1.00 34.95           N  
ANISOU 2931  NZ  LYS B 383     5807   4025   3447    -93    173    131       N  
ATOM   2932  N   ILE B 384      34.800  18.543  27.242  1.00 38.98           N  
ANISOU 2932  N   ILE B 384     6352   4599   3858   -324    281    180       N  
ATOM   2933  CA  ILE B 384      33.702  19.397  26.801  1.00 38.50           C  
ANISOU 2933  CA  ILE B 384     6239   4600   3788   -343    283    175       C  
ATOM   2934  C   ILE B 384      32.816  18.570  25.881  1.00 39.01           C  
ANISOU 2934  C   ILE B 384     6303   4668   3850   -410    290    172       C  
ATOM   2935  O   ILE B 384      33.226  18.217  24.768  1.00 38.82           O  
ANISOU 2935  O   ILE B 384     6297   4617   3835   -422    283    150       O  
ATOM   2936  CB  ILE B 384      34.210  20.657  26.088  1.00 39.79           C  
ANISOU 2936  CB  ILE B 384     6371   4777   3970   -305    265    156       C  
ATOM   2937  CG1 ILE B 384      35.189  21.420  26.981  1.00 41.09           C  
ANISOU 2937  CG1 ILE B 384     6537   4928   4147   -247    251    152       C  
ATOM   2938  CG2 ILE B 384      33.044  21.541  25.677  1.00 41.00           C  
ANISOU 2938  CG2 ILE B 384     6472   4990   4117   -315    262    157       C  
ATOM   2939  CD1 ILE B 384      35.728  22.683  26.349  1.00 41.19           C  
ANISOU 2939  CD1 ILE B 384     6520   4943   4189   -217    234    139       C  
ATOM   2940  N   VAL B 385      31.595  18.278  26.328  1.00 34.64           N  
ANISOU 2940  N   VAL B 385     5727   4153   3281   -454    304    191       N  
ATOM   2941  CA  VAL B 385      30.668  17.437  25.578  1.00 34.77           C  
ANISOU 2941  CA  VAL B 385     5738   4174   3299   -529    306    188       C  
ATOM   2942  C   VAL B 385      29.425  18.259  25.265  1.00 35.41           C  
ANISOU 2942  C   VAL B 385     5744   4339   3370   -544    301    188       C  
ATOM   2943  O   VAL B 385      28.634  18.571  26.164  1.00 36.96           O  
ANISOU 2943  O   VAL B 385     5900   4586   3555   -544    320    210       O  
ATOM   2944  CB  VAL B 385      30.307  16.159  26.344  1.00 35.20           C  
ANISOU 2944  CB  VAL B 385     5829   4192   3354   -582    326    217       C  
ATOM   2945  CG1 VAL B 385      29.346  15.305  25.532  1.00 35.79           C  
ANISOU 2945  CG1 VAL B 385     5895   4265   3439   -670    321    207       C  
ATOM   2946  CG2 VAL B 385      31.569  15.380  26.678  1.00 35.05           C  
ANISOU 2946  CG2 VAL B 385     5884   4085   3347   -553    325    220       C  
ATOM   2947  N   ILE B 386      29.246  18.597  23.990  1.00 35.50           N  
ANISOU 2947  N   ILE B 386     5734   4371   3382   -554    277    165       N  
ATOM   2948  CA  ILE B 386      28.080  19.329  23.504  1.00 34.42           C  
ANISOU 2948  CA  ILE B 386     5524   4313   3239   -566    263    168       C  
ATOM   2949  C   ILE B 386      27.126  18.338  22.857  1.00 36.10           C  
ANISOU 2949  C   ILE B 386     5724   4542   3450   -653    252    159       C  
ATOM   2950  O   ILE B 386      27.558  17.445  22.121  1.00 38.32           O  
ANISOU 2950  O   ILE B 386     6057   4773   3731   -690    241    134       O  
ATOM   2951  CB  ILE B 386      28.498  20.426  22.505  1.00 35.31           C  
ANISOU 2951  CB  ILE B 386     5623   4442   3350   -517    236    156       C  
ATOM   2952  CG1 ILE B 386      29.553  21.344  23.128  1.00 35.57           C  
ANISOU 2952  CG1 ILE B 386     5674   4446   3396   -442    243    161       C  
ATOM   2953  CG2 ILE B 386      27.285  21.219  22.034  1.00 36.94           C  
ANISOU 2953  CG2 ILE B 386     5753   4730   3551   -518    216    165       C  
ATOM   2954  CD1 ILE B 386      30.181  22.305  22.145  1.00 34.76           C  
ANISOU 2954  CD1 ILE B 386     5567   4341   3298   -404    223    159       C  
ATOM   2955  N   VAL B 387      25.831  18.477  23.135  1.00 32.93           N  
ANISOU 2955  N   VAL B 387     5251   4211   3048   -686    255    176       N  
ATOM   2956  CA  VAL B 387      24.803  17.615  22.556  1.00 34.89           C  
ANISOU 2956  CA  VAL B 387     5471   4486   3302   -778    240    168       C  
ATOM   2957  C   VAL B 387      23.812  18.481  21.790  1.00 36.32           C  
ANISOU 2957  C   VAL B 387     5565   4759   3475   -772    206    165       C  
ATOM   2958  O   VAL B 387      23.255  19.433  22.347  1.00 36.40           O  
ANISOU 2958  O   VAL B 387     5510   4832   3489   -724    217    186       O  
ATOM   2959  CB  VAL B 387      24.076  16.784  23.629  1.00 36.16           C  
ANISOU 2959  CB  VAL B 387     5615   4650   3476   -840    276    199       C  
ATOM   2960  CG1 VAL B 387      23.200  15.739  22.967  1.00 37.76           C  
ANISOU 2960  CG1 VAL B 387     5800   4856   3694   -948    254    186       C  
ATOM   2961  CG2 VAL B 387      25.074  16.128  24.569  1.00 34.17           C  
ANISOU 2961  CG2 VAL B 387     5446   4312   3226   -825    308    217       C  
ATOM   2962  N   VAL B 388      23.569  18.129  20.527  1.00 31.36           N  
ANISOU 2962  N   VAL B 388     4939   4143   2835   -817    163    136       N  
ATOM   2963  CA  VAL B 388      22.730  18.903  19.625  1.00 30.21           C  
ANISOU 2963  CA  VAL B 388     4719   4084   2675   -808    119    135       C  
ATOM   2964  C   VAL B 388      21.674  17.992  19.001  1.00 33.32           C  
ANISOU 2964  C   VAL B 388     5073   4516   3070   -910     85    114       C  
ATOM   2965  O   VAL B 388      21.738  16.760  19.083  1.00 34.25           O  
ANISOU 2965  O   VAL B 388     5237   4577   3200   -988     92     95       O  
ATOM   2966  CB  VAL B 388      23.554  19.607  18.525  1.00 29.44           C  
ANISOU 2966  CB  VAL B 388     4660   3978   2548   -751     89    122       C  
ATOM   2967  CG1 VAL B 388      24.553  20.581  19.143  1.00 28.27           C  
ANISOU 2967  CG1 VAL B 388     4539   3791   2409   -659    118    143       C  
ATOM   2968  CG2 VAL B 388      24.269  18.584  17.656  1.00 29.47           C  
ANISOU 2968  CG2 VAL B 388     4745   3923   2529   -797     76     79       C  
ATOM   2969  N   ASP B 389      20.698  18.634  18.360  1.00 45.43           N  
ANISOU 2969  N   ASP B 389     6522   6145   4596   -907     42    119       N  
ATOM   2970  CA  ASP B 389      19.553  17.954  17.775  1.00 47.62           C  
ANISOU 2970  CA  ASP B 389     6738   6480   4876  -1002     -1    101       C  
ATOM   2971  C   ASP B 389      19.977  17.077  16.599  1.00 47.87           C  
ANISOU 2971  C   ASP B 389     6843   6468   4876  -1060    -45     47       C  
ATOM   2972  O   ASP B 389      21.078  17.202  16.054  1.00 46.61           O  
ANISOU 2972  O   ASP B 389     6767   6257   4685  -1013    -44     27       O  
ATOM   2973  CB  ASP B 389      18.509  18.972  17.315  1.00 49.07           C  
ANISOU 2973  CB  ASP B 389     6810   6781   5054   -967    -44    121       C  
ATOM   2974  CG  ASP B 389      17.747  19.595  18.470  1.00 52.23           C  
ANISOU 2974  CG  ASP B 389     7116   7238   5490   -930     -2    162       C  
ATOM   2975  OD1 ASP B 389      17.346  18.850  19.390  1.00 54.50           O  
ANISOU 2975  OD1 ASP B 389     7383   7519   5807   -991     42    172       O  
ATOM   2976  OD2 ASP B 389      17.549  20.829  18.460  1.00 50.40           O  
ANISOU 2976  OD2 ASP B 389     6834   7057   5258   -837    -11    185       O  
ATOM   2977  N   GLU B 390      19.065  16.187  16.197  1.00 48.32           N  
ANISOU 2977  N   GLU B 390     6864   6553   4944  -1165    -82     19       N  
ATOM   2978  CA  GLU B 390      19.383  15.210  15.161  1.00 48.61           C  
ANISOU 2978  CA  GLU B 390     6974   6541   4953  -1230   -124    -46       C  
ATOM   2979  C   GLU B 390      19.607  15.868  13.805  1.00 46.02           C  
ANISOU 2979  C   GLU B 390     6659   6270   4557  -1182   -181    -71       C  
ATOM   2980  O   GLU B 390      20.375  15.349  12.988  1.00 46.82           O  
ANISOU 2980  O   GLU B 390     6851   6322   4618  -1189   -195   -123       O  
ATOM   2981  CB  GLU B 390      18.273  14.160  15.069  1.00 50.11           C  
ANISOU 2981  CB  GLU B 390     7116   6748   5176  -1361   -159    -73       C  
ATOM   2982  CG  GLU B 390      16.932  14.688  14.569  1.00 53.64           C  
ANISOU 2982  CG  GLU B 390     7432   7330   5618  -1388   -220    -64       C  
ATOM   2983  CD  GLU B 390      16.031  15.182  15.689  1.00 58.41           C  
ANISOU 2983  CD  GLU B 390     7919   8001   6272  -1381   -180      0       C  
ATOM   2984  OE1 GLU B 390      16.542  15.446  16.800  1.00 59.71           O  
ANISOU 2984  OE1 GLU B 390     8108   8122   6459  -1327   -106     42       O  
ATOM   2985  OE2 GLU B 390      14.809  15.306  15.456  1.00 58.68           O  
ANISOU 2985  OE2 GLU B 390     7835   8139   6323  -1428   -223      6       O  
ATOM   2986  N   PHE B 391      18.959  17.004  13.548  1.00 44.87           N  
ANISOU 2986  N   PHE B 391     6425   6227   4395  -1129   -212    -33       N  
ATOM   2987  CA  PHE B 391      19.095  17.700  12.275  1.00 44.63           C  
ANISOU 2987  CA  PHE B 391     6403   6259   4296  -1082   -268    -40       C  
ATOM   2988  C   PHE B 391      20.298  18.632  12.227  1.00 44.07           C  
ANISOU 2988  C   PHE B 391     6394   6150   4199   -973   -231     -8       C  
ATOM   2989  O   PHE B 391      20.579  19.198  11.165  1.00 42.45           O  
ANISOU 2989  O   PHE B 391     6210   5987   3932   -933   -267     -6       O  
ATOM   2990  CB  PHE B 391      17.823  18.498  11.969  1.00 45.22           C  
ANISOU 2990  CB  PHE B 391     6353   6461   4370  -1071   -326     -6       C  
ATOM   2991  CG  PHE B 391      17.484  19.523  13.013  1.00 46.00           C  
ANISOU 2991  CG  PHE B 391     6374   6585   4519   -996   -286     60       C  
ATOM   2992  CD1 PHE B 391      18.022  20.799  12.953  1.00 46.48           C  
ANISOU 2992  CD1 PHE B 391     6445   6649   4565   -883   -275    105       C  
ATOM   2993  CD2 PHE B 391      16.625  19.212  14.052  1.00 47.78           C  
ANISOU 2993  CD2 PHE B 391     6517   6831   4806  -1039   -256     74       C  
ATOM   2994  CE1 PHE B 391      17.713  21.742  13.913  1.00 47.48           C  
ANISOU 2994  CE1 PHE B 391     6507   6792   4740   -810   -240    153       C  
ATOM   2995  CE2 PHE B 391      16.308  20.152  15.012  1.00 49.02           C  
ANISOU 2995  CE2 PHE B 391     6604   7017   5002   -964   -215    124       C  
ATOM   2996  CZ  PHE B 391      16.856  21.417  14.944  1.00 48.67           C  
ANISOU 2996  CZ  PHE B 391     6578   6970   4945   -846   -209    159       C  
ATOM   2997  N   VAL B 392      20.999  18.818  13.338  1.00 43.41           N  
ANISOU 2997  N   VAL B 392     6339   5994   4160   -930   -161     19       N  
ATOM   2998  CA  VAL B 392      22.210  19.629  13.364  1.00 41.83           C  
ANISOU 2998  CA  VAL B 392     6197   5750   3947   -838   -125     44       C  
ATOM   2999  C   VAL B 392      23.393  18.741  13.015  1.00 41.24           C  
ANISOU 2999  C   VAL B 392     6230   5590   3848   -856   -100     -3       C  
ATOM   3000  O   VAL B 392      23.578  17.674  13.613  1.00 42.07           O  
ANISOU 3000  O   VAL B 392     6374   5625   3986   -906    -72    -34       O  
ATOM   3001  CB  VAL B 392      22.405  20.293  14.737  1.00 39.61           C  
ANISOU 3001  CB  VAL B 392     5891   5436   3723   -781    -71     89       C  
ATOM   3002  CG1 VAL B 392      23.783  20.934  14.822  1.00 36.36           C  
ANISOU 3002  CG1 VAL B 392     5547   4962   3307   -704    -35    105       C  
ATOM   3003  CG2 VAL B 392      21.316  21.325  14.990  1.00 40.62           C  
ANISOU 3003  CG2 VAL B 392     5913   5648   3871   -742    -93    132       C  
ATOM   3004  N   ASP B 393      24.181  19.168  12.041  1.00 43.31           N  
ANISOU 3004  N   ASP B 393     6540   5861   4055   -812   -107     -7       N  
ATOM   3005  CA  ASP B 393      25.411  18.476  11.682  1.00 41.82           C  
ANISOU 3005  CA  ASP B 393     6447   5601   3842   -808    -75    -51       C  
ATOM   3006  C   ASP B 393      26.459  18.739  12.754  1.00 41.17           C  
ANISOU 3006  C   ASP B 393     6394   5439   3812   -753    -11    -22       C  
ATOM   3007  O   ASP B 393      26.961  19.868  12.842  1.00 41.62           O  
ANISOU 3007  O   ASP B 393     6438   5506   3871   -684      5     26       O  
ATOM   3008  CB  ASP B 393      25.900  18.954  10.311  1.00 40.98           C  
ANISOU 3008  CB  ASP B 393     6373   5545   3653   -775    -95    -55       C  
ATOM   3009  CG  ASP B 393      27.112  18.180   9.806  1.00 43.86           C  
ANISOU 3009  CG  ASP B 393     6830   5851   3984   -770    -59   -110       C  
ATOM   3010  OD1 ASP B 393      27.693  17.380  10.572  1.00 44.23           O  
ANISOU 3010  OD1 ASP B 393     6918   5808   4080   -780    -18   -138       O  
ATOM   3011  OD2 ASP B 393      27.483  18.376   8.627  1.00 44.41           O  
ANISOU 3011  OD2 ASP B 393     6930   5969   3974   -752    -71   -124       O  
ATOM   3012  N   PRO B 394      26.826  17.751  13.577  1.00 39.91           N  
ANISOU 3012  N   PRO B 394     6274   5196   3694   -781     23    -49       N  
ATOM   3013  CA  PRO B 394      27.817  18.003  14.635  1.00 37.76           C  
ANISOU 3013  CA  PRO B 394     6026   4855   3466   -726     75    -21       C  
ATOM   3014  C   PRO B 394      29.205  18.306  14.105  1.00 38.29           C  
ANISOU 3014  C   PRO B 394     6145   4894   3511   -668    102    -26       C  
ATOM   3015  O   PRO B 394      30.045  18.800  14.870  1.00 36.79           O  
ANISOU 3015  O   PRO B 394     5960   4663   3355   -615    136      3       O  
ATOM   3016  CB  PRO B 394      27.804  16.698  15.439  1.00 40.24           C  
ANISOU 3016  CB  PRO B 394     6377   5091   3820   -778     95    -48       C  
ATOM   3017  CG  PRO B 394      27.415  15.665  14.436  1.00 38.68           C  
ANISOU 3017  CG  PRO B 394     6212   4893   3592   -847     63   -110       C  
ATOM   3018  CD  PRO B 394      26.425  16.334  13.526  1.00 38.05           C  
ANISOU 3018  CD  PRO B 394     6071   4919   3467   -864     11   -105       C  
ATOM   3019  N   PHE B 395      29.473  18.025  12.833  1.00 35.67           N  
ANISOU 3019  N   PHE B 395     5848   4586   3119   -676     88    -64       N  
ATOM   3020  CA  PHE B 395      30.734  18.372  12.196  1.00 36.10           C  
ANISOU 3020  CA  PHE B 395     5940   4632   3142   -623    119    -65       C  
ATOM   3021  C   PHE B 395      30.706  19.759  11.567  1.00 36.84           C  
ANISOU 3021  C   PHE B 395     5996   4799   3203   -582    107     -8       C  
ATOM   3022  O   PHE B 395      31.736  20.218  11.063  1.00 36.83           O  
ANISOU 3022  O   PHE B 395     6016   4799   3179   -540    137      7       O  
ATOM   3023  CB  PHE B 395      31.090  17.328  11.132  1.00 37.05           C  
ANISOU 3023  CB  PHE B 395     6124   4747   3207   -647    119   -140       C  
ATOM   3024  CG  PHE B 395      31.304  15.947  11.684  1.00 37.25           C  
ANISOU 3024  CG  PHE B 395     6201   4680   3273   -679    134   -196       C  
ATOM   3025  CD1 PHE B 395      32.532  15.579  12.209  1.00 36.17           C  
ANISOU 3025  CD1 PHE B 395     6104   4466   3174   -633    183   -204       C  
ATOM   3026  CD2 PHE B 395      30.277  15.016  11.679  1.00 36.89           C  
ANISOU 3026  CD2 PHE B 395     6161   4622   3234   -755     97   -238       C  
ATOM   3027  CE1 PHE B 395      32.733  14.308  12.715  1.00 35.83           C  
ANISOU 3027  CE1 PHE B 395     6111   4330   3171   -655    193   -249       C  
ATOM   3028  CE2 PHE B 395      30.472  13.746  12.186  1.00 37.40           C  
ANISOU 3028  CE2 PHE B 395     6278   4589   3342   -786    110   -283       C  
ATOM   3029  CZ  PHE B 395      31.701  13.392  12.705  1.00 37.32           C  
ANISOU 3029  CZ  PHE B 395     6314   4498   3368   -732    158   -287       C  
ATOM   3030  N   ASN B 396      29.556  20.427  11.584  1.00 40.09           N  
ANISOU 3030  N   ASN B 396     6349   5270   3614   -593     64     28       N  
ATOM   3031  CA  ASN B 396      29.403  21.781  11.056  1.00 39.97           C  
ANISOU 3031  CA  ASN B 396     6296   5315   3576   -551     45     92       C  
ATOM   3032  C   ASN B 396      29.416  22.732  12.247  1.00 39.96           C  
ANISOU 3032  C   ASN B 396     6253   5279   3650   -508     60    143       C  
ATOM   3033  O   ASN B 396      28.405  22.897  12.935  1.00 41.06           O  
ANISOU 3033  O   ASN B 396     6342   5436   3823   -517     38    154       O  
ATOM   3034  CB  ASN B 396      28.114  21.896  10.249  1.00 40.60           C  
ANISOU 3034  CB  ASN B 396     6337   5483   3606   -581    -18     95       C  
ATOM   3035  CG  ASN B 396      27.994  23.219   9.525  1.00 43.36           C  
ANISOU 3035  CG  ASN B 396     6659   5894   3923   -534    -43    165       C  
ATOM   3036  OD1 ASN B 396      28.478  24.244   9.996  1.00 43.77           O  
ANISOU 3036  OD1 ASN B 396     6697   5914   4018   -482    -20    221       O  
ATOM   3037  ND2 ASN B 396      27.344  23.201   8.369  1.00 45.34           N  
ANISOU 3037  ND2 ASN B 396     6903   6228   4094   -554    -94    163       N  
ATOM   3038  N   LEU B 397      30.562  23.374  12.481  1.00 35.07           N  
ANISOU 3038  N   LEU B 397     5652   4617   3056   -461     97    171       N  
ATOM   3039  CA  LEU B 397      30.740  24.117  13.724  1.00 36.52           C  
ANISOU 3039  CA  LEU B 397     5810   4754   3313   -423    112    201       C  
ATOM   3040  C   LEU B 397      29.915  25.400  13.755  1.00 37.47           C  
ANISOU 3040  C   LEU B 397     5875   4911   3450   -390     79    255       C  
ATOM   3041  O   LEU B 397      29.545  25.862  14.839  1.00 38.77           O  
ANISOU 3041  O   LEU B 397     6008   5055   3669   -366     80    263       O  
ATOM   3042  CB  LEU B 397      32.224  24.403  13.954  1.00 32.08           C  
ANISOU 3042  CB  LEU B 397     5278   4134   2777   -390    154    210       C  
ATOM   3043  CG  LEU B 397      32.999  23.182  14.462  1.00 34.33           C  
ANISOU 3043  CG  LEU B 397     5605   4365   3075   -406    187    159       C  
ATOM   3044  CD1 LEU B 397      34.470  23.487  14.689  1.00 36.47           C  
ANISOU 3044  CD1 LEU B 397     5892   4589   3377   -370    224    169       C  
ATOM   3045  CD2 LEU B 397      32.367  22.656  15.736  1.00 32.71           C  
ANISOU 3045  CD2 LEU B 397     5389   4131   2910   -421    183    141       C  
ATOM   3046  N  AGLU B 398      29.608  25.988  12.595  0.57 38.85           N  
ANISOU 3046  N  AGLU B 398     6042   5143   3578   -382     49    291       N  
ATOM   3047  CA AGLU B 398      28.716  27.145  12.601  0.57 40.09           C  
ANISOU 3047  CA AGLU B 398     6146   5331   3755   -345     10    343       C  
ATOM   3048  C  AGLU B 398      27.292  26.740  12.977  0.57 41.31           C  
ANISOU 3048  C  AGLU B 398     6246   5537   3915   -368    -23    321       C  
ATOM   3049  O  AGLU B 398      26.601  27.481  13.690  0.57 42.00           O  
ANISOU 3049  O  AGLU B 398     6281   5626   4049   -330    -35    342       O  
ATOM   3050  CB AGLU B 398      28.769  27.869  11.245  0.57 40.43           C  
ANISOU 3050  CB AGLU B 398     6196   5423   3743   -329    -16    399       C  
ATOM   3051  CG AGLU B 398      27.973  27.244  10.104  0.57 43.92           C  
ANISOU 3051  CG AGLU B 398     6635   5954   4099   -367    -60    383       C  
ATOM   3052  CD AGLU B 398      28.383  27.772   8.732  0.57 45.52           C  
ANISOU 3052  CD AGLU B 398     6868   6203   4227   -354    -72    435       C  
ATOM   3053  OE1AGLU B 398      29.042  28.832   8.667  0.57 45.44           O  
ANISOU 3053  OE1AGLU B 398     6865   6157   4242   -313    -54    501       O  
ATOM   3054  OE2AGLU B 398      28.046  27.125   7.716  0.57 45.73           O  
ANISOU 3054  OE2AGLU B 398     6909   6300   4165   -387    -99    410       O  
ATOM   3055  N  BGLU B 398      29.626  25.986  12.591  0.43 38.82           N  
ANISOU 3055  N  BGLU B 398     6038   5138   3574   -382     49    291       N  
ATOM   3056  CA BGLU B 398      28.714  27.126  12.547  0.43 40.06           C  
ANISOU 3056  CA BGLU B 398     6143   5330   3748   -346      9    343       C  
ATOM   3057  C  BGLU B 398      27.316  26.719  13.001  0.43 41.12           C  
ANISOU 3057  C  BGLU B 398     6223   5510   3891   -368    -22    320       C  
ATOM   3058  O  BGLU B 398      26.654  27.449  13.751  0.43 41.93           O  
ANISOU 3058  O  BGLU B 398     6275   5613   4043   -331    -32    340       O  
ATOM   3059  CB BGLU B 398      28.675  27.708  11.133  0.43 40.82           C  
ANISOU 3059  CB BGLU B 398     6246   5482   3781   -336    -20    392       C  
ATOM   3060  CG BGLU B 398      29.879  28.568  10.760  0.43 42.64           C  
ANISOU 3060  CG BGLU B 398     6510   5672   4019   -305     10    445       C  
ATOM   3061  CD BGLU B 398      31.145  27.759  10.531  0.43 43.44           C  
ANISOU 3061  CD BGLU B 398     6664   5747   4095   -330     62    408       C  
ATOM   3062  OE1BGLU B 398      32.247  28.283  10.806  0.43 43.34           O  
ANISOU 3062  OE1BGLU B 398     6665   5679   4123   -310    100    433       O  
ATOM   3063  OE2BGLU B 398      31.040  26.600  10.076  0.43 43.68           O  
ANISOU 3063  OE2BGLU B 398     6718   5809   4068   -369     64    351       O  
ATOM   3064  N   GLN B 399      26.860  25.543  12.570  1.00 39.51           N  
ANISOU 3064  N   GLN B 399     6026   5344   3643   -429    -35    273       N  
ATOM   3065  CA  GLN B 399      25.560  25.042  13.004  1.00 40.87           C  
ANISOU 3065  CA  GLN B 399     6139   5560   3828   -465    -62    251       C  
ATOM   3066  C   GLN B 399      25.565  24.710  14.494  1.00 39.93           C  
ANISOU 3066  C   GLN B 399     6011   5390   3772   -467    -20    231       C  
ATOM   3067  O   GLN B 399      24.564  24.931  15.190  1.00 40.64           O  
ANISOU 3067  O   GLN B 399     6035   5513   3894   -462    -28    238       O  
ATOM   3068  CB  GLN B 399      25.186  23.815  12.178  1.00 42.11           C  
ANISOU 3068  CB  GLN B 399     6316   5757   3928   -540    -88    200       C  
ATOM   3069  CG  GLN B 399      23.728  23.736  11.793  1.00 43.17           C  
ANISOU 3069  CG  GLN B 399     6375   5980   4046   -572   -148    200       C  
ATOM   3070  CD  GLN B 399      23.497  22.774  10.650  1.00 45.10           C  
ANISOU 3070  CD  GLN B 399     6648   6269   4219   -639   -188    151       C  
ATOM   3071  OE1 GLN B 399      23.476  21.559  10.844  1.00 43.91           O  
ANISOU 3071  OE1 GLN B 399     6524   6088   4073   -706   -178     92       O  
ATOM   3072  NE2 GLN B 399      23.324  23.311   9.447  1.00 46.72           N  
ANISOU 3072  NE2 GLN B 399     6851   6544   4357   -619   -237    176       N  
ATOM   3073  N   VAL B 400      26.681  24.176  15.001  1.00 35.93           N  
ANISOU 3073  N   VAL B 400     5564   4809   3278   -472     25    208       N  
ATOM   3074  CA  VAL B 400      26.800  23.926  16.435  1.00 36.93           C  
ANISOU 3074  CA  VAL B 400     5690   4889   3455   -467     62    197       C  
ATOM   3075  C   VAL B 400      26.734  25.237  17.207  1.00 38.02           C  
ANISOU 3075  C   VAL B 400     5791   5020   3636   -397     67    231       C  
ATOM   3076  O   VAL B 400      26.128  25.313  18.283  1.00 37.92           O  
ANISOU 3076  O   VAL B 400     5741   5016   3653   -386     82    228       O  
ATOM   3077  CB  VAL B 400      28.098  23.153  16.740  1.00 35.57           C  
ANISOU 3077  CB  VAL B 400     5590   4639   3286   -477    101    170       C  
ATOM   3078  CG1 VAL B 400      28.260  22.948  18.240  1.00 34.99           C  
ANISOU 3078  CG1 VAL B 400     5519   4522   3255   -466    134    167       C  
ATOM   3079  CG2 VAL B 400      28.099  21.818  16.015  1.00 35.62           C  
ANISOU 3079  CG2 VAL B 400     5636   4642   3255   -542     96    127       C  
ATOM   3080  N   MET B 401      27.353  26.291  16.668  1.00 47.21           N  
ANISOU 3080  N   MET B 401     6968   6168   4803   -347     58    263       N  
ATOM   3081  CA  MET B 401      27.244  27.610  17.282  1.00 46.18           C  
ANISOU 3081  CA  MET B 401     6806   6021   4719   -280     54    291       C  
ATOM   3082  C   MET B 401      25.801  28.091  17.293  1.00 48.04           C  
ANISOU 3082  C   MET B 401     6966   6325   4961   -260     23    306       C  
ATOM   3083  O   MET B 401      25.343  28.682  18.278  1.00 48.16           O  
ANISOU 3083  O   MET B 401     6944   6337   5016   -216     33    304       O  
ATOM   3084  CB  MET B 401      28.130  28.612  16.540  1.00 46.45           C  
ANISOU 3084  CB  MET B 401     6869   6021   4759   -243     45    331       C  
ATOM   3085  CG  MET B 401      29.589  28.598  16.959  1.00 47.61           C  
ANISOU 3085  CG  MET B 401     7068   6093   4929   -237     80    321       C  
ATOM   3086  SD  MET B 401      29.828  28.953  18.713  1.00 50.49           S  
ANISOU 3086  SD  MET B 401     7427   6402   5354   -200    102    293       S  
ATOM   3087  CE  MET B 401      28.819  30.420  18.918  1.00 47.47           C  
ANISOU 3087  CE  MET B 401     6992   6034   5012   -134     71    321       C  
ATOM   3088  N   TRP B 402      25.079  27.873  16.191  1.00 33.70           N  
ANISOU 3088  N   TRP B 402     5124   4575   3105   -287    -16    319       N  
ATOM   3089  CA  TRP B 402      23.657  28.215  16.174  1.00 34.81           C  
ANISOU 3089  CA  TRP B 402     5181   4792   3254   -271    -51    332       C  
ATOM   3090  C   TRP B 402      22.908  27.498  17.294  1.00 35.88           C  
ANISOU 3090  C   TRP B 402     5272   4952   3410   -301    -22    298       C  
ATOM   3091  O   TRP B 402      22.094  28.103  18.008  1.00 37.89           O  
ANISOU 3091  O   TRP B 402     5460   5237   3699   -256    -18    304       O  
ATOM   3092  CB  TRP B 402      23.031  27.869  14.825  1.00 35.33           C  
ANISOU 3092  CB  TRP B 402     5227   4933   3264   -310   -104    344       C  
ATOM   3093  CG  TRP B 402      21.538  27.968  14.872  1.00 38.79           C  
ANISOU 3093  CG  TRP B 402     5567   5459   3714   -307   -140    349       C  
ATOM   3094  CD1 TRP B 402      20.793  29.111  14.846  1.00 38.98           C  
ANISOU 3094  CD1 TRP B 402     5526   5518   3767   -233   -172    389       C  
ATOM   3095  CD2 TRP B 402      20.606  26.885  14.990  1.00 40.72           C  
ANISOU 3095  CD2 TRP B 402     5761   5765   3947   -382   -148    315       C  
ATOM   3096  NE1 TRP B 402      19.455  28.808  14.921  1.00 39.79           N  
ANISOU 3096  NE1 TRP B 402     5533   5710   3874   -252   -198    380       N  
ATOM   3097  CE2 TRP B 402      19.313  27.448  15.012  1.00 41.63           C  
ANISOU 3097  CE2 TRP B 402     5772   5963   4085   -349   -185    336       C  
ATOM   3098  CE3 TRP B 402      20.738  25.495  15.072  1.00 41.72           C  
ANISOU 3098  CE3 TRP B 402     5919   5880   4054   -474   -130    269       C  
ATOM   3099  CZ2 TRP B 402      18.161  26.671  15.112  1.00 45.65           C  
ANISOU 3099  CZ2 TRP B 402     6199   6551   4595   -412   -201    315       C  
ATOM   3100  CZ3 TRP B 402      19.591  24.724  15.171  1.00 44.54           C  
ANISOU 3100  CZ3 TRP B 402     6205   6305   4415   -540   -148    249       C  
ATOM   3101  CH2 TRP B 402      18.320  25.314  15.191  1.00 46.14           C  
ANISOU 3101  CH2 TRP B 402     6295   6597   4638   -513   -183    272       C  
ATOM   3102  N   ALA B 403      23.159  26.195  17.444  1.00 37.30           N  
ANISOU 3102  N   ALA B 403     5486   5118   3569   -377      0    264       N  
ATOM   3103  CA  ALA B 403      22.510  25.433  18.507  1.00 37.78           C  
ANISOU 3103  CA  ALA B 403     5512   5198   3647   -416     33    243       C  
ATOM   3104  C   ALA B 403      22.871  25.989  19.878  1.00 38.81           C  
ANISOU 3104  C   ALA B 403     5647   5286   3811   -359     79    241       C  
ATOM   3105  O   ALA B 403      22.016  26.077  20.764  1.00 40.46           O  
ANISOU 3105  O   ALA B 403     5796   5540   4038   -347    100    240       O  
ATOM   3106  CB  ALA B 403      22.888  23.955  18.409  1.00 36.21           C  
ANISOU 3106  CB  ALA B 403     5366   4967   3426   -505     48    212       C  
ATOM   3107  N   LEU B 404      24.134  26.376  20.066  1.00 39.77           N  
ANISOU 3107  N   LEU B 404     5839   5331   3940   -322     93    240       N  
ATOM   3108  CA  LEU B 404      24.549  26.960  21.337  1.00 38.60           C  
ANISOU 3108  CA  LEU B 404     5702   5144   3820   -266    127    232       C  
ATOM   3109  C   LEU B 404      23.803  28.257  21.618  1.00 40.40           C  
ANISOU 3109  C   LEU B 404     5868   5403   4078   -188    115    242       C  
ATOM   3110  O   LEU B 404      23.371  28.504  22.750  1.00 41.40           O  
ANISOU 3110  O   LEU B 404     5964   5547   4218   -154    144    226       O  
ATOM   3111  CB  LEU B 404      26.058  27.210  21.337  1.00 36.27           C  
ANISOU 3111  CB  LEU B 404     5484   4763   3533   -245    134    228       C  
ATOM   3112  CG  LEU B 404      27.007  26.011  21.320  1.00 36.17           C  
ANISOU 3112  CG  LEU B 404     5538   4705   3500   -300    153    212       C  
ATOM   3113  CD1 LEU B 404      28.451  26.489  21.327  1.00 34.89           C  
ANISOU 3113  CD1 LEU B 404     5431   4471   3355   -267    157    212       C  
ATOM   3114  CD2 LEU B 404      26.743  25.082  22.495  1.00 34.61           C  
ANISOU 3114  CD2 LEU B 404     5343   4510   3297   -331    188    197       C  
ATOM   3115  N   THR B 405      23.639  29.097  20.597  1.00 33.20           N  
ANISOU 3115  N   THR B 405     4939   4500   3175   -155     72    270       N  
ATOM   3116  CA  THR B 405      23.051  30.413  20.805  1.00 34.84           C  
ANISOU 3116  CA  THR B 405     5099   4719   3422    -68     56    282       C  
ATOM   3117  C   THR B 405      21.533  30.382  20.928  1.00 37.26           C  
ANISOU 3117  C   THR B 405     5305   5122   3731    -59     49    284       C  
ATOM   3118  O   THR B 405      20.957  31.326  21.479  1.00 39.32           O  
ANISOU 3118  O   THR B 405     5518   5396   4026     21     51    279       O  
ATOM   3119  CB  THR B 405      23.443  31.364  19.670  1.00 35.39           C  
ANISOU 3119  CB  THR B 405     5188   4755   3503    -32     11    324       C  
ATOM   3120  OG1 THR B 405      22.998  30.828  18.417  1.00 37.62           O  
ANISOU 3120  OG1 THR B 405     5453   5097   3743    -81    -26    350       O  
ATOM   3121  CG2 THR B 405      24.952  31.565  19.633  1.00 33.97           C  
ANISOU 3121  CG2 THR B 405     5094   4483   3332    -36     23    326       C  
ATOM   3122  N   THR B 406      20.863  29.338  20.429  1.00 37.76           N  
ANISOU 3122  N   THR B 406     5332   5253   3763   -135     40    286       N  
ATOM   3123  CA  THR B 406      19.406  29.318  20.505  1.00 37.61           C  
ANISOU 3123  CA  THR B 406     5204   5334   3753   -132     30    289       C  
ATOM   3124  C   THR B 406      18.813  28.239  21.407  1.00 39.17           C  
ANISOU 3124  C   THR B 406     5363   5581   3940   -197     79    267       C  
ATOM   3125  O   THR B 406      17.649  28.371  21.798  1.00 40.96           O  
ANISOU 3125  O   THR B 406     5490   5891   4183   -181     89    268       O  
ATOM   3126  CB  THR B 406      18.795  29.178  19.102  1.00 39.91           C  
ANISOU 3126  CB  THR B 406     5456   5685   4022   -164    -35    316       C  
ATOM   3127  OG1 THR B 406      19.163  27.916  18.533  1.00 39.45           O  
ANISOU 3127  OG1 THR B 406     5444   5622   3922   -267    -40    303       O  
ATOM   3128  CG2 THR B 406      19.277  30.301  18.199  1.00 39.87           C  
ANISOU 3128  CG2 THR B 406     5486   5641   4024    -96    -81    353       C  
ATOM   3129  N   ARG B 407      19.570  27.195  21.766  1.00 45.33           N  
ANISOU 3129  N   ARG B 407     6214   6312   4697   -268    111    252       N  
ATOM   3130  CA  ARG B 407      19.041  26.077  22.544  1.00 45.78           C  
ANISOU 3130  CA  ARG B 407     6244   6407   4745   -342    155    243       C  
ATOM   3131  C   ARG B 407      19.655  25.935  23.930  1.00 44.58           C  
ANISOU 3131  C   ARG B 407     6141   6211   4587   -324    218    230       C  
ATOM   3132  O   ARG B 407      19.207  25.071  24.701  1.00 45.01           O  
ANISOU 3132  O   ARG B 407     6174   6298   4631   -380    262    233       O  
ATOM   3133  CB  ARG B 407      19.254  24.751  21.797  1.00 44.67           C  
ANISOU 3133  CB  ARG B 407     6144   6247   4581   -453    136    239       C  
ATOM   3134  CG  ARG B 407      18.849  24.753  20.340  1.00 48.13           C  
ANISOU 3134  CG  ARG B 407     6557   6724   5008   -481     68    244       C  
ATOM   3135  CD  ARG B 407      17.354  24.898  20.182  1.00 51.66           C  
ANISOU 3135  CD  ARG B 407     6875   7282   5470   -491     45    255       C  
ATOM   3136  NE  ARG B 407      17.024  25.941  19.220  1.00 53.41           N  
ANISOU 3136  NE  ARG B 407     7058   7543   5694   -423    -16    274       N  
ATOM   3137  CZ  ARG B 407      15.869  26.015  18.570  1.00 55.35           C  
ANISOU 3137  CZ  ARG B 407     7203   7886   5943   -437    -66    285       C  
ATOM   3138  NH1 ARG B 407      14.929  25.103  18.778  1.00 58.02           N  
ANISOU 3138  NH1 ARG B 407     7464   8291   6289   -523    -60    275       N  
ATOM   3139  NH2 ARG B 407      15.655  27.001  17.712  1.00 54.87           N  
ANISOU 3139  NH2 ARG B 407     7116   7853   5881   -366   -125    310       N  
ATOM   3140  N   VAL B 408      20.674  26.723  24.259  1.00 37.45           N  
ANISOU 3140  N   VAL B 408     5303   5236   3689   -253    220    219       N  
ATOM   3141  CA  VAL B 408      21.396  26.592  25.518  1.00 34.51           C  
ANISOU 3141  CA  VAL B 408     4988   4820   3304   -234    268    203       C  
ATOM   3142  C   VAL B 408      20.934  27.697  26.457  1.00 35.11           C  
ANISOU 3142  C   VAL B 408     5018   4930   3391   -140    292    184       C  
ATOM   3143  O   VAL B 408      21.172  28.882  26.205  1.00 37.62           O  
ANISOU 3143  O   VAL B 408     5339   5217   3736    -60    263    174       O  
ATOM   3144  CB  VAL B 408      22.915  26.655  25.317  1.00 33.92           C  
ANISOU 3144  CB  VAL B 408     5015   4644   3228   -225    252    195       C  
ATOM   3145  CG1 VAL B 408      23.622  26.699  26.666  1.00 32.44           C  
ANISOU 3145  CG1 VAL B 408     4877   4421   3028   -192    289    176       C  
ATOM   3146  CG2 VAL B 408      23.393  25.472  24.521  1.00 32.91           C  
ANISOU 3146  CG2 VAL B 408     4935   4483   3085   -311    238    204       C  
ATOM   3147  N   HIS B 409      20.278  27.305  27.545  1.00 34.80           N  
ANISOU 3147  N   HIS B 409     4940   4953   3330   -148    347    180       N  
ATOM   3148  CA  HIS B 409      20.080  28.177  28.690  1.00 34.35           C  
ANISOU 3148  CA  HIS B 409     4864   4921   3267    -58    383    150       C  
ATOM   3149  C   HIS B 409      21.172  27.828  29.692  1.00 35.40           C  
ANISOU 3149  C   HIS B 409     5090   4997   3364    -61    410    135       C  
ATOM   3150  O   HIS B 409      21.090  26.778  30.348  1.00 34.54           O  
ANISOU 3150  O   HIS B 409     4994   4914   3217   -122    452    154       O  
ATOM   3151  CB  HIS B 409      18.689  27.980  29.302  1.00 37.61           C  
ANISOU 3151  CB  HIS B 409     5171   5453   3667    -61    434    156       C  
ATOM   3152  CG  HIS B 409      18.359  28.953  30.391  1.00 40.90           C  
ANISOU 3152  CG  HIS B 409     5558   5908   4073     44    474    117       C  
ATOM   3153  ND1 HIS B 409      19.147  29.118  31.510  1.00 41.02           N  
ANISOU 3153  ND1 HIS B 409     5648   5887   4051     82    504     86       N  
ATOM   3154  CD2 HIS B 409      17.318  29.807  30.536  1.00 43.12           C  
ANISOU 3154  CD2 HIS B 409     5744   6264   4376    123    488     98       C  
ATOM   3155  CE1 HIS B 409      18.609  30.035  32.294  1.00 41.66           C  
ANISOU 3155  CE1 HIS B 409     5686   6018   4126    179    535     44       C  
ATOM   3156  NE2 HIS B 409      17.498  30.468  31.726  1.00 42.97           N  
ANISOU 3156  NE2 HIS B 409     5748   6249   4330    208    529     51       N  
ATOM   3157  N   PRO B 410      22.219  28.645  29.832  1.00 37.08           N  
ANISOU 3157  N   PRO B 410     5369   5130   3588      0    383    106       N  
ATOM   3158  CA  PRO B 410      23.366  28.235  30.661  1.00 37.07           C  
ANISOU 3158  CA  PRO B 410     5457   5074   3555     -9    395     94       C  
ATOM   3159  C   PRO B 410      23.028  28.006  32.124  1.00 38.38           C  
ANISOU 3159  C   PRO B 410     5619   5300   3665     11    452     80       C  
ATOM   3160  O   PRO B 410      23.821  27.370  32.829  1.00 37.51           O  
ANISOU 3160  O   PRO B 410     5576   5162   3516    -13    464     85       O  
ATOM   3161  CB  PRO B 410      24.353  29.398  30.488  1.00 35.53           C  
ANISOU 3161  CB  PRO B 410     5310   4795   3396     59    350     61       C  
ATOM   3162  CG  PRO B 410      23.976  30.007  29.169  1.00 38.66           C  
ANISOU 3162  CG  PRO B 410     5666   5180   3844     68    309     78       C  
ATOM   3163  CD  PRO B 410      22.478  29.909  29.125  1.00 39.22           C  
ANISOU 3163  CD  PRO B 410     5641   5351   3910     69    334     90       C  
ATOM   3164  N   GLY B 411      21.883  28.493  32.604  1.00 37.60           N  
ANISOU 3164  N   GLY B 411     5442   5289   3556     56    490     65       N  
ATOM   3165  CA  GLY B 411      21.503  28.255  33.985  1.00 38.33           C  
ANISOU 3165  CA  GLY B 411     5526   5453   3583     74    554     54       C  
ATOM   3166  C   GLY B 411      21.050  26.837  34.264  1.00 39.95           C  
ANISOU 3166  C   GLY B 411     5718   5712   3748    -24    602    112       C  
ATOM   3167  O   GLY B 411      21.082  26.405  35.422  1.00 41.17           O  
ANISOU 3167  O   GLY B 411     5897   5907   3837    -26    652    120       O  
ATOM   3168  N   LYS B 412      20.629  26.105  33.233  1.00 40.76           N  
ANISOU 3168  N   LYS B 412     5785   5813   3888   -107    585    154       N  
ATOM   3169  CA  LYS B 412      20.172  24.731  33.394  1.00 39.54           C  
ANISOU 3169  CA  LYS B 412     5618   5694   3711   -212    624    210       C  
ATOM   3170  C   LYS B 412      20.790  23.749  32.411  1.00 38.97           C  
ANISOU 3170  C   LYS B 412     5601   5538   3669   -302    580    240       C  
ATOM   3171  O   LYS B 412      20.786  22.546  32.697  1.00 38.28           O  
ANISOU 3171  O   LYS B 412     5539   5442   3562   -385    606    283       O  
ATOM   3172  CB  LYS B 412      18.642  24.653  33.260  1.00 42.39           C  
ANISOU 3172  CB  LYS B 412     5853   6169   4086   -239    662    229       C  
ATOM   3173  CG  LYS B 412      18.147  24.711  31.822  1.00 44.70           C  
ANISOU 3173  CG  LYS B 412     6087   6457   4441   -274    606    234       C  
ATOM   3174  CD  LYS B 412      16.638  24.549  31.736  1.00 46.78           C  
ANISOU 3174  CD  LYS B 412     6216   6840   4720   -308    640    255       C  
ATOM   3175  CE  LYS B 412      16.126  24.928  30.354  1.00 49.55           C  
ANISOU 3175  CE  LYS B 412     6501   7199   5127   -312    573    250       C  
ATOM   3176  NZ  LYS B 412      16.661  24.045  29.275  1.00 48.70           N  
ANISOU 3176  NZ  LYS B 412     6452   7014   5038   -407    517    267       N  
ATOM   3177  N   ASP B 413      21.327  24.207  31.279  1.00 37.61           N  
ANISOU 3177  N   ASP B 413     5449   5301   3541   -286    517    219       N  
ATOM   3178  CA  ASP B 413      21.826  23.317  30.239  1.00 36.46           C  
ANISOU 3178  CA  ASP B 413     5347   5087   3419   -364    478    238       C  
ATOM   3179  C   ASP B 413      23.334  23.105  30.284  1.00 37.26           C  
ANISOU 3179  C   ASP B 413     5557   5085   3515   -352    454    229       C  
ATOM   3180  O   ASP B 413      23.849  22.284  29.516  1.00 35.78           O  
ANISOU 3180  O   ASP B 413     5414   4837   3343   -411    429    240       O  
ATOM   3181  CB  ASP B 413      21.429  23.850  28.854  1.00 39.90           C  
ANISOU 3181  CB  ASP B 413     5733   5529   3897   -362    427    227       C  
ATOM   3182  CG  ASP B 413      19.961  23.626  28.540  1.00 44.49           C  
ANISOU 3182  CG  ASP B 413     6207   6207   4492   -407    438    244       C  
ATOM   3183  OD1 ASP B 413      19.343  22.754  29.186  1.00 43.36           O  
ANISOU 3183  OD1 ASP B 413     6034   6108   4331   -472    484    271       O  
ATOM   3184  OD2 ASP B 413      19.430  24.311  27.636  1.00 43.41           O  
ANISOU 3184  OD2 ASP B 413     6009   6102   4382   -380    398    235       O  
ATOM   3185  N   VAL B 414      24.051  23.817  31.148  1.00 40.19           N  
ANISOU 3185  N   VAL B 414     5967   5437   3865   -277    458    205       N  
ATOM   3186  CA  VAL B 414      25.492  23.652  31.320  1.00 38.52           C  
ANISOU 3186  CA  VAL B 414     5847   5139   3650   -261    434    197       C  
ATOM   3187  C   VAL B 414      25.736  23.061  32.701  1.00 38.74           C  
ANISOU 3187  C   VAL B 414     5916   5179   3622   -262    472    215       C  
ATOM   3188  O   VAL B 414      25.412  23.687  33.721  1.00 39.48           O  
ANISOU 3188  O   VAL B 414     5993   5330   3679   -207    500    197       O  
ATOM   3189  CB  VAL B 414      26.241  24.984  31.154  1.00 38.27           C  
ANISOU 3189  CB  VAL B 414     5830   5069   3643   -179    396    154       C  
ATOM   3190  CG1 VAL B 414      27.716  24.805  31.465  1.00 38.34           C  
ANISOU 3190  CG1 VAL B 414     5919   5000   3648   -165    373    146       C  
ATOM   3191  CG2 VAL B 414      26.040  25.552  29.749  1.00 35.63           C  
ANISOU 3191  CG2 VAL B 414     5460   4720   3357   -179    358    150       C  
ATOM   3192  N   SER B 415      26.308  21.862  32.735  1.00 38.39           N  
ANISOU 3192  N   SER B 415     5932   5084   3572   -318    473    249       N  
ATOM   3193  CA  SER B 415      26.602  21.158  33.979  1.00 39.82           C  
ANISOU 3193  CA  SER B 415     6162   5269   3699   -324    504    281       C  
ATOM   3194  C   SER B 415      28.105  20.963  34.128  1.00 37.96           C  
ANISOU 3194  C   SER B 415     6009   4949   3464   -295    465    274       C  
ATOM   3195  O   SER B 415      28.761  20.411  33.235  1.00 37.90           O  
ANISOU 3195  O   SER B 415     6034   4869   3499   -325    435    278       O  
ATOM   3196  CB  SER B 415      25.849  19.817  34.040  1.00 40.24           C  
ANISOU 3196  CB  SER B 415     6209   5334   3744   -418    542    341       C  
ATOM   3197  OG  SER B 415      24.491  19.987  33.674  1.00 42.82           O  
ANISOU 3197  OG  SER B 415     6446   5738   4085   -454    569    345       O  
ATOM   3198  N   ILE B 416      28.635  21.429  35.258  1.00 38.80           N  
ANISOU 3198  N   ILE B 416     6145   5073   3523   -234    464    260       N  
ATOM   3199  CA  ILE B 416      30.059  21.402  35.576  1.00 38.40           C  
ANISOU 3199  CA  ILE B 416     6161   4959   3470   -196    422    248       C  
ATOM   3200  C   ILE B 416      30.263  20.355  36.663  1.00 38.41           C  
ANISOU 3200  C   ILE B 416     6217   4965   3411   -213    443    303       C  
ATOM   3201  O   ILE B 416      29.666  20.457  37.741  1.00 38.78           O  
ANISOU 3201  O   ILE B 416     6258   5088   3390   -198    481    317       O  
ATOM   3202  CB  ILE B 416      30.543  22.784  36.037  1.00 39.03           C  
ANISOU 3202  CB  ILE B 416     6234   5053   3542   -115    393    186       C  
ATOM   3203  CG1 ILE B 416      30.145  23.862  35.021  1.00 38.41           C  
ANISOU 3203  CG1 ILE B 416     6100   4971   3521    -98    378    144       C  
ATOM   3204  CG2 ILE B 416      32.040  22.794  36.274  1.00 38.98           C  
ANISOU 3204  CG2 ILE B 416     6284   4985   3543    -82    341    171       C  
ATOM   3205  CD1 ILE B 416      31.005  23.895  33.789  1.00 37.33           C  
ANISOU 3205  CD1 ILE B 416     5974   4757   3452   -113    336    139       C  
ATOM   3206  N   ILE B 417      31.089  19.348  36.391  1.00 39.32           N  
ANISOU 3206  N   ILE B 417     6387   5004   3550   -239    421    336       N  
ATOM   3207  CA  ILE B 417      31.255  18.206  37.293  1.00 38.31           C  
ANISOU 3207  CA  ILE B 417     6316   4865   3375   -261    439    403       C  
ATOM   3208  C   ILE B 417      32.725  18.104  37.691  1.00 38.50           C  
ANISOU 3208  C   ILE B 417     6399   4834   3395   -207    386    398       C  
ATOM   3209  O   ILE B 417      33.588  17.828  36.847  1.00 38.14           O  
ANISOU 3209  O   ILE B 417     6369   4710   3410   -206    350    385       O  
ATOM   3210  CB  ILE B 417      30.760  16.900  36.656  1.00 38.36           C  
ANISOU 3210  CB  ILE B 417     6336   4821   3419   -348    462    457       C  
ATOM   3211  CG1 ILE B 417      29.329  17.070  36.144  1.00 40.60           C  
ANISOU 3211  CG1 ILE B 417     6546   5164   3717   -405    504    455       C  
ATOM   3212  CG2 ILE B 417      30.825  15.758  37.661  1.00 36.15           C  
ANISOU 3212  CG2 ILE B 417     6117   4527   3092   -372    484    538       C  
ATOM   3213  CD1 ILE B 417      28.932  16.075  35.078  1.00 42.00           C  
ANISOU 3213  CD1 ILE B 417     6722   5281   3954   -490    506    475       C  
ATOM   3214  N   GLU B 418      33.007  18.301  38.977  1.00 45.69           N  
ANISOU 3214  N   GLU B 418     7339   5793   4230   -161    382    408       N  
ATOM   3215  CA  GLU B 418      34.373  18.282  39.481  1.00 45.22           C  
ANISOU 3215  CA  GLU B 418     7326   5697   4158   -105    324    401       C  
ATOM   3216  C   GLU B 418      34.859  16.855  39.729  1.00 47.31           C  
ANISOU 3216  C   GLU B 418     7655   5900   4420   -126    319    480       C  
ATOM   3217  O   GLU B 418      34.074  15.914  39.877  1.00 47.77           O  
ANISOU 3217  O   GLU B 418     7731   5956   4461   -183    365    547       O  
ATOM   3218  CB  GLU B 418      34.484  19.069  40.788  1.00 44.57           C  
ANISOU 3218  CB  GLU B 418     7254   5696   3986    -44    313    376       C  
ATOM   3219  CG  GLU B 418      33.870  20.451  40.773  1.00 52.21           C  
ANISOU 3219  CG  GLU B 418     8166   6724   4946    -15    324    299       C  
ATOM   3220  CD  GLU B 418      34.729  21.460  40.033  1.00 57.16           C  
ANISOU 3220  CD  GLU B 418     8768   7301   5648     18    266    224       C  
ATOM   3221  OE1 GLU B 418      34.160  22.426  39.480  1.00 58.45           O  
ANISOU 3221  OE1 GLU B 418     8883   7479   5847     23    277    173       O  
ATOM   3222  OE2 GLU B 418      35.967  21.284  39.992  1.00 59.45           O  
ANISOU 3222  OE2 GLU B 418     9086   7538   5965     40    211    221       O  
ATOM   3223  N   ASN B 419      36.169  16.741  39.858  1.00 42.30           N  
ANISOU 3223  N   ASN B 419     7052   5213   3807    -79    260    473       N  
ATOM   3224  CA  ASN B 419      36.858  15.500  40.278  1.00 43.49           C  
ANISOU 3224  CA  ASN B 419     7268   5311   3945    -71    241    545       C  
ATOM   3225  C   ASN B 419      36.482  14.274  39.455  1.00 42.68           C  
ANISOU 3225  C   ASN B 419     7190   5125   3903   -136    272    596       C  
ATOM   3226  O   ASN B 419      36.241  13.261  40.021  1.00 41.58           O  
ANISOU 3226  O   ASN B 419     7102   4961   3736   -165    293    678       O  
ATOM   3227  CB  ASN B 419      36.584  15.227  41.747  1.00 44.80           C  
ANISOU 3227  CB  ASN B 419     7475   5548   3998    -53    254    603       C  
ATOM   3228  CG  ASN B 419      37.753  14.607  42.461  1.00 47.66           C  
ANISOU 3228  CG  ASN B 419     7897   5877   4334     -2    199    652       C  
ATOM   3229  OD1 ASN B 419      37.619  13.538  43.021  1.00 49.14           O  
ANISOU 3229  OD1 ASN B 419     8142   6046   4484    -19    216    745       O  
ATOM   3230  ND2 ASN B 419      38.881  15.274  42.445  1.00 48.03           N  
ANISOU 3230  ND2 ASN B 419     7929   5915   4404     61    130    594       N  
ATOM   3231  N   CYS B 420      36.474  14.410  38.152  1.00 37.61           N  
ANISOU 3231  N   CYS B 420     6513   4436   3342   -160    273    546       N  
ATOM   3232  CA  CYS B 420      36.214  13.346  37.194  1.00 40.15           C  
ANISOU 3232  CA  CYS B 420     6855   4672   3729   -219    292    568       C  
ATOM   3233  C   CYS B 420      37.516  12.921  36.527  1.00 41.02           C  
ANISOU 3233  C   CYS B 420     6987   4693   3904   -176    249    546       C  
ATOM   3234  O   CYS B 420      38.529  13.619  36.619  1.00 39.73           O  
ANISOU 3234  O   CYS B 420     6804   4544   3747   -111    207    507       O  
ATOM   3235  CB  CYS B 420      35.200  13.831  36.153  1.00 38.04           C  
ANISOU 3235  CB  CYS B 420     6529   4430   3494   -276    325    523       C  
ATOM   3236  SG  CYS B 420      33.470  13.650  36.674  1.00 41.30           S  
ANISOU 3236  SG  CYS B 420     6918   4916   3858   -355    390    571       S  
ATOM   3237  N   PRO B 421      37.537  11.770  35.843  1.00 38.26           N  
ANISOU 3237  N   PRO B 421     6676   4250   3610   -210    258    567       N  
ATOM   3238  CA  PRO B 421      38.780  11.333  35.190  1.00 37.55           C  
ANISOU 3238  CA  PRO B 421     6605   4079   3583   -160    223    540       C  
ATOM   3239  C   PRO B 421      39.229  12.313  34.118  1.00 36.67           C  
ANISOU 3239  C   PRO B 421     6432   3992   3510   -140    213    457       C  
ATOM   3240  O   PRO B 421      38.415  12.942  33.441  1.00 35.06           O  
ANISOU 3240  O   PRO B 421     6186   3829   3308   -185    237    421       O  
ATOM   3241  CB  PRO B 421      38.406   9.982  34.573  1.00 36.60           C  
ANISOU 3241  CB  PRO B 421     6537   3857   3511   -214    244    566       C  
ATOM   3242  CG  PRO B 421      37.269   9.501  35.390  1.00 39.24           C  
ANISOU 3242  CG  PRO B 421     6898   4210   3800   -279    278    639       C  
ATOM   3243  CD  PRO B 421      36.488  10.740  35.737  1.00 39.26           C  
ANISOU 3243  CD  PRO B 421     6835   4336   3745   -294    298    617       C  
ATOM   3244  N   GLY B 422      40.547  12.428  33.967  1.00 36.83           N  
ANISOU 3244  N   GLY B 422     6444   3986   3563    -71    176    432       N  
ATOM   3245  CA  GLY B 422      41.129  13.286  32.954  1.00 38.67           C  
ANISOU 3245  CA  GLY B 422     6620   4236   3836    -52    169    364       C  
ATOM   3246  C   GLY B 422      42.356  12.671  32.309  1.00 40.59           C  
ANISOU 3246  C   GLY B 422     6871   4412   4139     -2    153    345       C  
ATOM   3247  O   GLY B 422      42.645  11.488  32.516  1.00 39.56           O  
ANISOU 3247  O   GLY B 422     6796   4208   4027     16    148    379       O  
ATOM   3248  N   MET B 423      43.078  13.457  31.516  1.00 50.17           N  
ANISOU 3248  N   MET B 423     8028   5648   5385     23    147    292       N  
ATOM   3249  CA  MET B 423      44.342  13.029  30.941  1.00 50.09           C  
ANISOU 3249  CA  MET B 423     8008   5594   5431     80    137    269       C  
ATOM   3250  C   MET B 423      45.381  14.119  31.159  1.00 47.82           C  
ANISOU 3250  C   MET B 423     7652   5361   5157    127    103    247       C  
ATOM   3251  O   MET B 423      45.071  15.309  31.022  1.00 47.93           O  
ANISOU 3251  O   MET B 423     7621   5433   5158    100    105    223       O  
ATOM   3252  CB  MET B 423      44.209  12.724  29.440  1.00 50.33           C  
ANISOU 3252  CB  MET B 423     8036   5594   5494     54    176    223       C  
ATOM   3253  CG  MET B 423      43.439  11.445  29.122  1.00 51.38           C  
ANISOU 3253  CG  MET B 423     8239   5652   5630     13    199    234       C  
ATOM   3254  SD  MET B 423      44.103   9.966  29.919  1.00 53.50           S  
ANISOU 3254  SD  MET B 423     8580   5820   5927     69    177    282       S  
ATOM   3255  CE  MET B 423      45.614   9.716  28.991  1.00 54.75           C  
ANISOU 3255  CE  MET B 423     8708   5945   6149    154    177    227       C  
ATOM   3256  N   PRO B 424      46.617  13.750  31.508  1.00 40.10           N  
ANISOU 3256  N   PRO B 424     6663   4362   4212    196     70    254       N  
ATOM   3257  CA  PRO B 424      47.634  14.783  31.767  1.00 42.07           C  
ANISOU 3257  CA  PRO B 424     6840   4665   4481    232     32    232       C  
ATOM   3258  C   PRO B 424      48.008  15.580  30.528  1.00 41.78           C  
ANISOU 3258  C   PRO B 424     6737   4652   4486    216     61    184       C  
ATOM   3259  O   PRO B 424      48.454  16.727  30.658  1.00 40.39           O  
ANISOU 3259  O   PRO B 424     6501   4525   4322    215     38    166       O  
ATOM   3260  CB  PRO B 424      48.829  13.981  32.308  1.00 41.81           C  
ANISOU 3260  CB  PRO B 424     6808   4600   4479    311     -9    255       C  
ATOM   3261  CG  PRO B 424      48.304  12.593  32.580  1.00 41.90           C  
ANISOU 3261  CG  PRO B 424     6908   4539   4476    316      3    299       C  
ATOM   3262  CD  PRO B 424      47.160  12.391  31.645  1.00 40.68           C  
ANISOU 3262  CD  PRO B 424     6785   4359   4312    244     62    281       C  
ATOM   3263  N   LEU B 425      47.822  15.018  29.329  1.00 45.98           N  
ANISOU 3263  N   LEU B 425     7283   5150   5037    201    110    164       N  
ATOM   3264  CA  LEU B 425      48.116  15.747  28.103  1.00 49.84           C  
ANISOU 3264  CA  LEU B 425     7715   5670   5553    183    144    127       C  
ATOM   3265  C   LEU B 425      47.246  16.986  27.937  1.00 48.48           C  
ANISOU 3265  C   LEU B 425     7521   5547   5352    123    150    121       C  
ATOM   3266  O   LEU B 425      47.502  17.783  27.028  1.00 46.50           O  
ANISOU 3266  O   LEU B 425     7221   5326   5121    107    172    101       O  
ATOM   3267  CB  LEU B 425      47.965  14.825  26.887  1.00 52.54           C  
ANISOU 3267  CB  LEU B 425     8088   5971   5903    179    194    102       C  
ATOM   3268  CG  LEU B 425      46.711  13.956  26.756  1.00 53.93           C  
ANISOU 3268  CG  LEU B 425     8343   6102   6044    133    214    107       C  
ATOM   3269  CD1 LEU B 425      45.540  14.737  26.182  1.00 52.20           C  
ANISOU 3269  CD1 LEU B 425     8119   5927   5788     61    235     98       C  
ATOM   3270  CD2 LEU B 425      47.011  12.737  25.895  1.00 56.86           C  
ANISOU 3270  CD2 LEU B 425     8754   6410   6439    159    244     78       C  
ATOM   3271  N   ASP B 426      46.224  17.155  28.773  1.00 47.14           N  
ANISOU 3271  N   ASP B 426     7387   5386   5138     94    135    141       N  
ATOM   3272  CA  ASP B 426      45.484  18.403  28.876  1.00 45.40           C  
ANISOU 3272  CA  ASP B 426     7142   5212   4896     55    131    134       C  
ATOM   3273  C   ASP B 426      46.238  19.308  29.844  1.00 44.97           C  
ANISOU 3273  C   ASP B 426     7048   5186   4854     84     81    130       C  
ATOM   3274  O   ASP B 426      46.207  19.084  31.062  1.00 45.39           O  
ANISOU 3274  O   ASP B 426     7128   5243   4876    106     46    146       O  
ATOM   3275  CB  ASP B 426      44.048  18.146  29.345  1.00 44.48           C  
ANISOU 3275  CB  ASP B 426     7074   5101   4726     16    143    153       C  
ATOM   3276  CG  ASP B 426      43.204  19.413  29.403  1.00 45.13           C  
ANISOU 3276  CG  ASP B 426     7128   5230   4788    -15    142    142       C  
ATOM   3277  OD1 ASP B 426      43.750  20.519  29.210  1.00 44.77           O  
ANISOU 3277  OD1 ASP B 426     7035   5203   4771     -7    126    123       O  
ATOM   3278  OD2 ASP B 426      41.985  19.302  29.655  1.00 45.61           O  
ANISOU 3278  OD2 ASP B 426     7213   5307   4809    -48    158    154       O  
ATOM   3279  N   PRO B 427      46.929  20.337  29.341  1.00 39.03           N  
ANISOU 3279  N   PRO B 427     6233   4452   4144     81     74    110       N  
ATOM   3280  CA  PRO B 427      47.770  21.164  30.221  1.00 38.42           C  
ANISOU 3280  CA  PRO B 427     6114   4395   4090    104     19     99       C  
ATOM   3281  C   PRO B 427      46.983  22.031  31.186  1.00 36.54           C  
ANISOU 3281  C   PRO B 427     5893   4180   3812     90    -11     88       C  
ATOM   3282  O   PRO B 427      47.578  22.557  32.137  1.00 38.91           O  
ANISOU 3282  O   PRO B 427     6173   4495   4115    111    -66     73       O  
ATOM   3283  CB  PRO B 427      48.570  22.019  29.231  1.00 40.12           C  
ANISOU 3283  CB  PRO B 427     6259   4618   4368     89     32     85       C  
ATOM   3284  CG  PRO B 427      47.672  22.131  28.046  1.00 39.18           C  
ANISOU 3284  CG  PRO B 427     6155   4498   4234     48     88     89       C  
ATOM   3285  CD  PRO B 427      46.953  20.810  27.947  1.00 38.34           C  
ANISOU 3285  CD  PRO B 427     6113   4372   4085     52    116    100       C  
ATOM   3286  N   SER B 428      45.677  22.196  30.987  1.00 34.02           N  
ANISOU 3286  N   SER B 428     5605   3868   3454     57     21     92       N  
ATOM   3287  CA  SER B 428      44.867  23.019  31.874  1.00 34.03           C  
ANISOU 3287  CA  SER B 428     5618   3896   3416     52      1     77       C  
ATOM   3288  C   SER B 428      44.319  22.244  33.066  1.00 34.36           C  
ANISOU 3288  C   SER B 428     5714   3954   3387     69     -8     96       C  
ATOM   3289  O   SER B 428      43.678  22.848  33.932  1.00 34.98           O  
ANISOU 3289  O   SER B 428     5804   4064   3421     73    -21     80       O  
ATOM   3290  CB  SER B 428      43.702  23.651  31.105  1.00 33.31           C  
ANISOU 3290  CB  SER B 428     5525   3813   3320     14     39     73       C  
ATOM   3291  OG  SER B 428      43.076  22.707  30.257  1.00 34.62           O  
ANISOU 3291  OG  SER B 428     5713   3970   3471    -10     86     97       O  
ATOM   3292  N   THR B 429      44.546  20.931  33.132  1.00 34.05           N  
ANISOU 3292  N   THR B 429     5709   3893   3337     82      2    130       N  
ATOM   3293  CA  THR B 429      44.048  20.146  34.255  1.00 35.85           C  
ANISOU 3293  CA  THR B 429     5992   4133   3498     95     -3    162       C  
ATOM   3294  C   THR B 429      44.705  20.593  35.554  1.00 35.47           C  
ANISOU 3294  C   THR B 429     5942   4116   3418    137    -64    150       C  
ATOM   3295  O   THR B 429      45.927  20.751  35.627  1.00 34.90           O  
ANISOU 3295  O   THR B 429     5837   4037   3386    168   -110    136       O  
ATOM   3296  CB  THR B 429      44.300  18.654  34.033  1.00 30.65           C  
ANISOU 3296  CB  THR B 429     5372   3427   2846    103     13    204       C  
ATOM   3297  OG1 THR B 429      45.692  18.427  33.792  1.00 35.98           O  
ANISOU 3297  OG1 THR B 429     6019   4077   3575    145    -18    197       O  
ATOM   3298  CG2 THR B 429      43.488  18.141  32.856  1.00 30.31           C  
ANISOU 3298  CG2 THR B 429     5341   3355   2821     56     70    209       C  
ATOM   3299  N   ASN B 430      43.879  20.811  36.572  1.00 39.16           N  
ANISOU 3299  N   ASN B 430     6441   4627   3810    138    -65    153       N  
ATOM   3300  CA  ASN B 430      44.331  21.095  37.926  1.00 38.81           C  
ANISOU 3300  CA  ASN B 430     6412   4625   3711    178   -122    143       C  
ATOM   3301  C   ASN B 430      43.331  20.479  38.898  1.00 39.00           C  
ANISOU 3301  C   ASN B 430     6495   4686   3637    177    -95    185       C  
ATOM   3302  O   ASN B 430      42.186  20.942  38.978  1.00 36.65           O  
ANISOU 3302  O   ASN B 430     6200   4422   3303    153    -54    173       O  
ATOM   3303  CB  ASN B 430      44.470  22.599  38.164  1.00 37.56           C  
ANISOU 3303  CB  ASN B 430     6215   4493   3563    183   -157     73       C  
ATOM   3304  CG  ASN B 430      45.224  22.917  39.440  1.00 39.44           C  
ANISOU 3304  CG  ASN B 430     6462   4769   3755    226   -232     47       C  
ATOM   3305  OD1 ASN B 430      45.649  22.016  40.167  1.00 40.39           O  
ANISOU 3305  OD1 ASN B 430     6615   4902   3829    257   -259     89       O  
ATOM   3306  ND2 ASN B 430      45.396  24.204  39.720  1.00 38.75           N  
ANISOU 3306  ND2 ASN B 430     6347   4698   3680    229   -271    -22       N  
ATOM   3307  N   PRO B 431      43.705  19.416  39.632  1.00 42.48           N  
ANISOU 3307  N   PRO B 431     6981   5123   4035    204   -114    241       N  
ATOM   3308  CA  PRO B 431      44.998  18.716  39.617  1.00 42.82           C  
ANISOU 3308  CA  PRO B 431     7022   5128   4119    243   -163    265       C  
ATOM   3309  C   PRO B 431      45.304  18.049  38.278  1.00 42.49           C  
ANISOU 3309  C   PRO B 431     6964   5014   4168    226   -130    277       C  
ATOM   3310  O   PRO B 431      44.372  17.636  37.588  1.00 42.94           O  
ANISOU 3310  O   PRO B 431     7037   5045   4232    181    -68    293       O  
ATOM   3311  CB  PRO B 431      44.839  17.653  40.714  1.00 41.28           C  
ANISOU 3311  CB  PRO B 431     6897   4946   3843    268   -171    339       C  
ATOM   3312  CG  PRO B 431      43.691  18.120  41.550  1.00 41.69           C  
ANISOU 3312  CG  PRO B 431     6976   5068   3797    248   -141    338       C  
ATOM   3313  CD  PRO B 431      42.776  18.824  40.608  1.00 43.05           C  
ANISOU 3313  CD  PRO B 431     7111   5237   4010    198    -84    294       C  
ATOM   3314  N   PRO B 432      46.584  17.965  37.915  1.00 40.50           N  
ANISOU 3314  N   PRO B 432     6672   4734   3981    262   -170    264       N  
ATOM   3315  CA  PRO B 432      46.947  17.346  36.634  1.00 39.31           C  
ANISOU 3315  CA  PRO B 432     6503   4521   3910    255   -135    266       C  
ATOM   3316  C   PRO B 432      46.425  15.920  36.543  1.00 39.44           C  
ANISOU 3316  C   PRO B 432     6587   4483   3913    249    -98    325       C  
ATOM   3317  O   PRO B 432      46.491  15.151  37.504  1.00 37.68           O  
ANISOU 3317  O   PRO B 432     6416   4256   3646    279   -122    379       O  
ATOM   3318  CB  PRO B 432      48.479  17.387  36.640  1.00 41.37           C  
ANISOU 3318  CB  PRO B 432     6713   4778   4228    310   -192    252       C  
ATOM   3319  CG  PRO B 432      48.825  18.495  37.581  1.00 43.26           C  
ANISOU 3319  CG  PRO B 432     6921   5078   4436    322   -254    217       C  
ATOM   3320  CD  PRO B 432      47.762  18.467  38.643  1.00 40.57           C  
ANISOU 3320  CD  PRO B 432     6645   4775   3993    311   -250    240       C  
ATOM   3321  N   GLY B 433      45.895  15.575  35.371  1.00 42.08           N  
ANISOU 3321  N   GLY B 433     6925   4776   4287    208    -41    316       N  
ATOM   3322  CA  GLY B 433      45.323  14.265  35.153  1.00 42.96           C  
ANISOU 3322  CA  GLY B 433     7101   4826   4398    189     -5    361       C  
ATOM   3323  C   GLY B 433      43.888  14.105  35.604  1.00 43.21           C  
ANISOU 3323  C   GLY B 433     7177   4876   4367    131     32    394       C  
ATOM   3324  O   GLY B 433      43.279  13.067  35.314  1.00 41.02           O  
ANISOU 3324  O   GLY B 433     6947   4542   4096     97     66    429       O  
ATOM   3325  N   MET B 434      43.330  15.081  36.314  1.00 43.19           N  
ANISOU 3325  N   MET B 434     7156   4948   4306    118     27    383       N  
ATOM   3326  CA  MET B 434      41.923  15.089  36.680  1.00 41.56           C  
ANISOU 3326  CA  MET B 434     6973   4777   4042     63     71    407       C  
ATOM   3327  C   MET B 434      41.183  16.115  35.834  1.00 40.81           C  
ANISOU 3327  C   MET B 434     6826   4717   3964     22    101    353       C  
ATOM   3328  O   MET B 434      41.757  17.118  35.402  1.00 41.79           O  
ANISOU 3328  O   MET B 434     6900   4858   4121     42     79    300       O  
ATOM   3329  CB  MET B 434      41.735  15.408  38.166  1.00 41.67           C  
ANISOU 3329  CB  MET B 434     7007   4858   3965     88     49    435       C  
ATOM   3330  CG  MET B 434      42.453  14.453  39.104  1.00 41.83           C  
ANISOU 3330  CG  MET B 434     7083   4855   3957    134     11    499       C  
ATOM   3331  SD  MET B 434      41.803  12.774  39.004  1.00 44.26           S  
ANISOU 3331  SD  MET B 434     7465   5080   4272     91     56    589       S  
ATOM   3332  CE  MET B 434      40.194  12.987  39.766  1.00 45.48           C  
ANISOU 3332  CE  MET B 434     7634   5313   4335     27    114    626       C  
ATOM   3333  N   HIS B 435      39.901  15.858  35.598  1.00 38.54           N  
ANISOU 3333  N   HIS B 435     6547   4439   3657    -37    150    370       N  
ATOM   3334  CA  HIS B 435      39.075  16.734  34.786  1.00 38.13           C  
ANISOU 3334  CA  HIS B 435     6447   4422   3620    -75    178    327       C  
ATOM   3335  C   HIS B 435      37.918  17.288  35.599  1.00 37.09           C  
ANISOU 3335  C   HIS B 435     6304   4366   3423    -93    203    335       C  
ATOM   3336  O   HIS B 435      37.406  16.639  36.517  1.00 38.17           O  
ANISOU 3336  O   HIS B 435     6477   4521   3505   -106    222    387       O  
ATOM   3337  CB  HIS B 435      38.505  16.006  33.565  1.00 37.99           C  
ANISOU 3337  CB  HIS B 435     6433   4357   3644   -132    212    329       C  
ATOM   3338  CG  HIS B 435      39.275  16.235  32.303  1.00 39.39           C  
ANISOU 3338  CG  HIS B 435     6585   4500   3883   -120    202    284       C  
ATOM   3339  ND1 HIS B 435      39.138  15.429  31.194  1.00 40.02           N  
ANISOU 3339  ND1 HIS B 435     6680   4527   3998   -154    222    277       N  
ATOM   3340  CD2 HIS B 435      40.187  17.180  31.971  1.00 40.08           C  
ANISOU 3340  CD2 HIS B 435     6631   4599   3998    -80    176    245       C  
ATOM   3341  CE1 HIS B 435      39.932  15.866  30.233  1.00 40.43           C  
ANISOU 3341  CE1 HIS B 435     6703   4569   4090   -131    214    236       C  
ATOM   3342  NE2 HIS B 435      40.579  16.928  30.679  1.00 40.32           N  
ANISOU 3342  NE2 HIS B 435     6652   4593   4076    -90    188    221       N  
ATOM   3343  N   THR B 436      37.520  18.499  35.249  1.00 33.75           N  
ANISOU 3343  N   THR B 436     5830   3986   3007    -91    206    286       N  
ATOM   3344  CA  THR B 436      36.208  19.032  35.584  1.00 34.86           C  
ANISOU 3344  CA  THR B 436     5945   4195   3106   -114    242    284       C  
ATOM   3345  C   THR B 436      35.424  19.013  34.275  1.00 35.91           C  
ANISOU 3345  C   THR B 436     6043   4317   3285   -166    269    273       C  
ATOM   3346  O   THR B 436      35.658  19.838  33.389  1.00 36.85           O  
ANISOU 3346  O   THR B 436     6126   4428   3446   -156    254    232       O  
ATOM   3347  CB  THR B 436      36.305  20.430  36.183  1.00 36.03           C  
ANISOU 3347  CB  THR B 436     6064   4396   3231    -65    220    232       C  
ATOM   3348  OG1 THR B 436      36.984  20.366  37.445  1.00 37.62           O  
ANISOU 3348  OG1 THR B 436     6301   4615   3376    -20    190    239       O  
ATOM   3349  CG2 THR B 436      34.929  20.992  36.407  1.00 37.44           C  
ANISOU 3349  CG2 THR B 436     6208   4643   3374    -79    262    223       C  
ATOM   3350  N   LYS B 437      34.528  18.040  34.140  1.00 38.59           N  
ANISOU 3350  N   LYS B 437     6395   4653   3615   -225    306    314       N  
ATOM   3351  CA  LYS B 437      33.766  17.877  32.911  1.00 37.52           C  
ANISOU 3351  CA  LYS B 437     6229   4509   3519   -280    324    304       C  
ATOM   3352  C   LYS B 437      32.751  19.001  32.743  1.00 36.86           C  
ANISOU 3352  C   LYS B 437     6080   4499   3426   -280    338    277       C  
ATOM   3353  O   LYS B 437      32.218  19.538  33.717  1.00 36.98           O  
ANISOU 3353  O   LYS B 437     6078   4578   3396   -257    355    279       O  
ATOM   3354  CB  LYS B 437      33.038  16.534  32.909  1.00 34.71           C  
ANISOU 3354  CB  LYS B 437     5901   4128   3159   -350    354    353       C  
ATOM   3355  CG  LYS B 437      33.909  15.342  33.241  1.00 34.48           C  
ANISOU 3355  CG  LYS B 437     5943   4020   3139   -346    343    390       C  
ATOM   3356  CD  LYS B 437      34.962  15.118  32.179  1.00 34.94           C  
ANISOU 3356  CD  LYS B 437     6018   4005   3252   -326    313    354       C  
ATOM   3357  CE  LYS B 437      35.568  13.730  32.295  1.00 34.69           C  
ANISOU 3357  CE  LYS B 437     6055   3883   3242   -331    308    389       C  
ATOM   3358  NZ  LYS B 437      36.565  13.476  31.217  1.00 35.09           N  
ANISOU 3358  NZ  LYS B 437     6118   3868   3345   -306    287    347       N  
ATOM   3359  N   MET B 438      32.471  19.341  31.486  1.00 39.15           N  
ANISOU 3359  N   MET B 438     6336   4784   3756   -301    332    251       N  
ATOM   3360  CA  MET B 438      31.429  20.302  31.148  1.00 38.01           C  
ANISOU 3360  CA  MET B 438     6127   4703   3612   -302    341    232       C  
ATOM   3361  C   MET B 438      30.511  19.686  30.104  1.00 40.34           C  
ANISOU 3361  C   MET B 438     6396   5004   3925   -371    353    242       C  
ATOM   3362  O   MET B 438      30.947  19.397  28.982  1.00 42.05           O  
ANISOU 3362  O   MET B 438     6627   5177   4173   -390    333    227       O  
ATOM   3363  CB  MET B 438      32.017  21.616  30.629  1.00 39.70           C  
ANISOU 3363  CB  MET B 438     6318   4911   3855   -248    310    191       C  
ATOM   3364  CG  MET B 438      30.960  22.609  30.171  1.00 40.40           C  
ANISOU 3364  CG  MET B 438     6343   5054   3951   -242    314    176       C  
ATOM   3365  SD  MET B 438      31.626  24.244  29.820  1.00 44.38           S  
ANISOU 3365  SD  MET B 438     6828   5541   4493   -176    278    138       S  
ATOM   3366  CE  MET B 438      32.922  23.832  28.659  1.00 44.79           C  
ANISOU 3366  CE  MET B 438     6914   5522   4582   -194    254    141       C  
ATOM   3367  N   ILE B 439      29.246  19.498  30.474  1.00 35.91           N  
ANISOU 3367  N   ILE B 439     5796   4504   3344   -409    384    263       N  
ATOM   3368  CA  ILE B 439      28.216  19.004  29.567  1.00 36.31           C  
ANISOU 3368  CA  ILE B 439     5808   4575   3413   -480    389    269       C  
ATOM   3369  C   ILE B 439      27.329  20.174  29.166  1.00 36.34           C  
ANISOU 3369  C   ILE B 439     5732   4653   3422   -455    384    248       C  
ATOM   3370  O   ILE B 439      26.872  20.937  30.027  1.00 36.78           O  
ANISOU 3370  O   ILE B 439     5751   4767   3456   -411    405    247       O  
ATOM   3371  CB  ILE B 439      27.385  17.887  30.222  1.00 35.92           C  
ANISOU 3371  CB  ILE B 439     5760   4541   3348   -552    427    314       C  
ATOM   3372  CG1 ILE B 439      28.269  16.688  30.567  1.00 36.36           C  
ANISOU 3372  CG1 ILE B 439     5901   4509   3405   -573    426    341       C  
ATOM   3373  CG2 ILE B 439      26.232  17.478  29.316  1.00 35.81           C  
ANISOU 3373  CG2 ILE B 439     5691   4558   3357   -631    426    315       C  
ATOM   3374  CD1 ILE B 439      27.631  15.739  31.566  1.00 35.48           C  
ANISOU 3374  CD1 ILE B 439     5802   4408   3270   -629    468    401       C  
ATOM   3375  N   ILE B 440      27.084  20.318  27.863  1.00 31.70           N  
ANISOU 3375  N   ILE B 440     5119   4065   2860   -478    357    232       N  
ATOM   3376  CA  ILE B 440      26.275  21.403  27.314  1.00 32.51           C  
ANISOU 3376  CA  ILE B 440     5148   4231   2972   -451    342    218       C  
ATOM   3377  C   ILE B 440      25.147  20.786  26.495  1.00 35.27           C  
ANISOU 3377  C   ILE B 440     5448   4624   3330   -527    336    226       C  
ATOM   3378  O   ILE B 440      25.393  20.187  25.439  1.00 34.74           O  
ANISOU 3378  O   ILE B 440     5408   4520   3272   -572    309    216       O  
ATOM   3379  CB  ILE B 440      27.108  22.364  26.456  1.00 34.28           C  
ANISOU 3379  CB  ILE B 440     5387   4422   3216   -397    305    196       C  
ATOM   3380  CG1 ILE B 440      28.219  23.007  27.288  1.00 33.67           C  
ANISOU 3380  CG1 ILE B 440     5351   4304   3140   -330    305    184       C  
ATOM   3381  CG2 ILE B 440      26.219  23.430  25.836  1.00 33.83           C  
ANISOU 3381  CG2 ILE B 440     5258   4425   3171   -369    286    192       C  
ATOM   3382  CD1 ILE B 440      29.136  23.907  26.480  1.00 33.50           C  
ANISOU 3382  CD1 ILE B 440     5344   4241   3145   -288    273    169       C  
ATOM   3383  N   ASP B 441      23.910  20.967  26.957  1.00 37.80           N  
ANISOU 3383  N   ASP B 441     5692   5026   3646   -539    359    240       N  
ATOM   3384  CA  ASP B 441      22.718  20.420  26.303  1.00 38.59           C  
ANISOU 3384  CA  ASP B 441     5726   5181   3757   -616    351    249       C  
ATOM   3385  C   ASP B 441      22.127  21.490  25.387  1.00 40.13           C  
ANISOU 3385  C   ASP B 441     5851   5433   3965   -575    312    234       C  
ATOM   3386  O   ASP B 441      21.203  22.220  25.762  1.00 40.76           O  
ANISOU 3386  O   ASP B 441     5848   5591   4049   -539    325    240       O  
ATOM   3387  CB  ASP B 441      21.710  19.947  27.347  1.00 40.09           C  
ANISOU 3387  CB  ASP B 441     5861   5434   3937   -658    402    280       C  
ATOM   3388  CG  ASP B 441      20.417  19.435  26.731  1.00 44.95           C  
ANISOU 3388  CG  ASP B 441     6392   6114   4573   -743    393    289       C  
ATOM   3389  OD1 ASP B 441      20.373  19.237  25.499  1.00 46.81           O  
ANISOU 3389  OD1 ASP B 441     6628   6335   4824   -779    342    269       O  
ATOM   3390  OD2 ASP B 441      19.441  19.227  27.483  1.00 46.46           O  
ANISOU 3390  OD2 ASP B 441     6513   6377   4761   -776    437    316       O  
ATOM   3391  N   ALA B 442      22.663  21.574  24.163  1.00 36.14           N  
ANISOU 3391  N   ALA B 442     5379   4890   3463   -577    266    218       N  
ATOM   3392  CA  ALA B 442      22.158  22.464  23.125  1.00 38.26           C  
ANISOU 3392  CA  ALA B 442     5592   5207   3737   -546    221    214       C  
ATOM   3393  C   ALA B 442      21.033  21.840  22.308  1.00 38.69           C  
ANISOU 3393  C   ALA B 442     5583   5325   3793   -625    191    214       C  
ATOM   3394  O   ALA B 442      20.944  22.093  21.099  1.00 36.96           O  
ANISOU 3394  O   ALA B 442     5355   5123   3565   -627    140    206       O  
ATOM   3395  CB  ALA B 442      23.301  22.887  22.201  1.00 34.18           C  
ANISOU 3395  CB  ALA B 442     5142   4630   3215   -511    188    203       C  
ATOM   3396  N   THR B 443      20.181  21.024  22.919  1.00 34.04           N  
ANISOU 3396  N   THR B 443     4949   4774   3211   -694    219    225       N  
ATOM   3397  CA  THR B 443      19.033  20.472  22.217  1.00 35.37           C  
ANISOU 3397  CA  THR B 443     5042   5008   3388   -776    187    223       C  
ATOM   3398  C   THR B 443      17.761  21.214  22.605  1.00 38.52           C  
ANISOU 3398  C   THR B 443     5313   5519   3803   -745    196    241       C  
ATOM   3399  O   THR B 443      17.701  21.924  23.619  1.00 42.71           O  
ANISOU 3399  O   THR B 443     5820   6072   4337   -673    242    253       O  
ATOM   3400  CB  THR B 443      18.858  18.975  22.500  1.00 35.35           C  
ANISOU 3400  CB  THR B 443     5066   4971   3395   -892    208    225       C  
ATOM   3401  OG1 THR B 443      18.589  18.774  23.894  1.00 37.28           O  
ANISOU 3401  OG1 THR B 443     5290   5228   3645   -896    275    256       O  
ATOM   3402  CG2 THR B 443      20.102  18.197  22.099  1.00 33.83           C  
ANISOU 3402  CG2 THR B 443     4998   4664   3191   -914    199    201       C  
ATOM   3403  N   THR B 444      16.739  21.031  21.768  1.00 40.22           N  
ANISOU 3403  N   THR B 444     5446   5808   4029   -798    150    239       N  
ATOM   3404  CA  THR B 444      15.417  21.607  21.978  1.00 40.56           C  
ANISOU 3404  CA  THR B 444     5350   5969   4093   -777    151    255       C  
ATOM   3405  C   THR B 444      14.657  20.790  23.016  1.00 41.61           C  
ANISOU 3405  C   THR B 444     5423   6144   4243   -853    213    275       C  
ATOM   3406  O   THR B 444      14.602  19.561  22.907  1.00 43.10           O  
ANISOU 3406  O   THR B 444     5638   6299   4438   -969    213    274       O  
ATOM   3407  CB  THR B 444      14.636  21.633  20.665  1.00 42.15           C  
ANISOU 3407  CB  THR B 444     5482   6238   4297   -812     70    246       C  
ATOM   3408  OG1 THR B 444      15.430  22.252  19.644  1.00 41.96           O  
ANISOU 3408  OG1 THR B 444     5528   6171   4246   -754     15    236       O  
ATOM   3409  CG2 THR B 444      13.327  22.397  20.826  1.00 42.84           C  
ANISOU 3409  CG2 THR B 444     5417   6451   4411   -768     63    265       C  
ATOM   3410  N   PRO B 445      14.066  21.427  24.025  1.00 37.64           N  
ANISOU 3410  N   PRO B 445     4842   5711   3748   -793    268    292       N  
ATOM   3411  CA  PRO B 445      13.340  20.670  25.051  1.00 38.30           C  
ANISOU 3411  CA  PRO B 445     4866   5846   3840   -866    338    320       C  
ATOM   3412  C   PRO B 445      12.193  19.860  24.462  1.00 40.04           C  
ANISOU 3412  C   PRO B 445     4983   6138   4092   -987    308    329       C  
ATOM   3413  O   PRO B 445      11.523  20.286  23.519  1.00 40.63           O  
ANISOU 3413  O   PRO B 445     4974   6279   4183   -978    243    316       O  
ATOM   3414  CB  PRO B 445      12.827  21.761  25.997  1.00 38.31           C  
ANISOU 3414  CB  PRO B 445     4786   5931   3838   -755    393    326       C  
ATOM   3415  CG  PRO B 445      13.786  22.893  25.817  1.00 36.97           C  
ANISOU 3415  CG  PRO B 445     4695   5698   3655   -628    366    301       C  
ATOM   3416  CD  PRO B 445      14.184  22.856  24.366  1.00 36.83           C  
ANISOU 3416  CD  PRO B 445     4720   5630   3642   -651    278    287       C  
ATOM   3417  N   VAL B 446      11.984  18.673  25.023  1.00 40.41           N  
ANISOU 3417  N   VAL B 446     5037   6168   4150  -1104    352    354       N  
ATOM   3418  CA  VAL B 446      10.846  17.825  24.675  1.00 43.05           C  
ANISOU 3418  CA  VAL B 446     5266   6568   4523  -1236    335    366       C  
ATOM   3419  C   VAL B 446      10.168  17.402  25.972  1.00 42.40           C  
ANISOU 3419  C   VAL B 446     5112   6548   4451  -1285    433    417       C  
ATOM   3420  O   VAL B 446      10.771  17.486  27.054  1.00 40.88           O  
ANISOU 3420  O   VAL B 446     4988   6320   4225  -1235    506    439       O  
ATOM   3421  CB  VAL B 446      11.280  16.597  23.837  1.00 41.88           C  
ANISOU 3421  CB  VAL B 446     5208   6317   4387  -1361    279    345       C  
ATOM   3422  CG1 VAL B 446      12.092  17.029  22.624  1.00 41.67           C  
ANISOU 3422  CG1 VAL B 446     5266   6231   4335  -1302    196    296       C  
ATOM   3423  CG2 VAL B 446      12.063  15.620  24.687  1.00 39.29           C  
ANISOU 3423  CG2 VAL B 446     4999   5876   4053  -1415    339    371       C  
ATOM   3424  N   PRO B 447       8.905  16.977  25.905  1.00 42.11           N  
ANISOU 3424  N   PRO B 447     4933   6613   4455  -1381    436    438       N  
ATOM   3425  CA  PRO B 447       8.183  16.573  27.125  1.00 43.88           C  
ANISOU 3425  CA  PRO B 447     5076   6912   4687  -1434    538    494       C  
ATOM   3426  C   PRO B 447       8.971  15.556  27.931  1.00 43.49           C  
ANISOU 3426  C   PRO B 447     5158   6748   4617  -1503    596    532       C  
ATOM   3427  O   PRO B 447       9.640  14.681  27.362  1.00 40.70           O  
ANISOU 3427  O   PRO B 447     4919   6269   4277  -1581    547    519       O  
ATOM   3428  CB  PRO B 447       6.887  15.963  26.576  1.00 43.42           C  
ANISOU 3428  CB  PRO B 447     4866   6945   4689  -1568    506    505       C  
ATOM   3429  CG  PRO B 447       6.653  16.711  25.309  1.00 43.75           C  
ANISOU 3429  CG  PRO B 447     4855   7026   4740  -1509    400    453       C  
ATOM   3430  CD  PRO B 447       8.017  16.986  24.726  1.00 42.75           C  
ANISOU 3430  CD  PRO B 447     4904   6767   4574  -1433    348    412       C  
ATOM   3431  N   PRO B 448       8.913  15.633  29.270  1.00 48.57           N  
ANISOU 3431  N   PRO B 448     5794   7434   5227  -1473    700    581       N  
ATOM   3432  CA  PRO B 448       8.094  16.615  29.987  1.00 50.18           C  
ANISOU 3432  CA  PRO B 448     5863   7790   5413  -1380    766    590       C  
ATOM   3433  C   PRO B 448       8.821  17.914  30.344  1.00 49.70           C  
ANISOU 3433  C   PRO B 448     5860   7724   5300  -1196    774    550       C  
ATOM   3434  O   PRO B 448       8.318  18.670  31.176  1.00 50.35           O  
ANISOU 3434  O   PRO B 448     5861   7914   5356  -1108    844    554       O  
ATOM   3435  CB  PRO B 448       7.702  15.860  31.255  1.00 48.88           C  
ANISOU 3435  CB  PRO B 448     5675   7668   5231  -1459    878    665       C  
ATOM   3436  CG  PRO B 448       8.885  14.982  31.527  1.00 47.42           C  
ANISOU 3436  CG  PRO B 448     5674   7323   5021  -1505    877    688       C  
ATOM   3437  CD  PRO B 448       9.525  14.658  30.192  1.00 45.74           C  
ANISOU 3437  CD  PRO B 448     5548   6986   4846  -1539    763    635       C  
ATOM   3438  N   GLU B 449       9.974  18.172  29.737  1.00 49.80           N  
ANISOU 3438  N   GLU B 449     6007   7615   5299  -1139    707    509       N  
ATOM   3439  CA  GLU B 449      10.683  19.415  30.022  1.00 49.58           C  
ANISOU 3439  CA  GLU B 449     6032   7572   5232   -975    707    470       C  
ATOM   3440  C   GLU B 449       9.880  20.599  29.494  1.00 50.99           C  
ANISOU 3440  C   GLU B 449     6085   7854   5437   -879    674    436       C  
ATOM   3441  O   GLU B 449       9.507  20.612  28.315  1.00 50.01           O  
ANISOU 3441  O   GLU B 449     5911   7738   5353   -911    593    420       O  
ATOM   3442  CB  GLU B 449      12.077  19.420  29.402  1.00 47.52           C  
ANISOU 3442  CB  GLU B 449     5931   7164   4960   -946    641    438       C  
ATOM   3443  CG  GLU B 449      12.852  20.691  29.723  1.00 48.23           C  
ANISOU 3443  CG  GLU B 449     6078   7230   5018   -788    639    400       C  
ATOM   3444  CD  GLU B 449      14.247  20.713  29.131  1.00 48.58           C  
ANISOU 3444  CD  GLU B 449     6268   7136   5054   -763    580    373       C  
ATOM   3445  OE1 GLU B 449      14.661  19.699  28.533  1.00 49.54           O  
ANISOU 3445  OE1 GLU B 449     6455   7180   5189   -859    546    382       O  
ATOM   3446  OE2 GLU B 449      14.930  21.751  29.266  1.00 49.63           O  
ANISOU 3446  OE2 GLU B 449     6448   7239   5171   -646    568    342       O  
ATOM   3447  N   PRO B 450       9.588  21.597  30.324  1.00 52.15           N  
ANISOU 3447  N   PRO B 450     6177   8078   5560   -758    732    424       N  
ATOM   3448  CA  PRO B 450       8.858  22.769  29.834  1.00 52.74           C  
ANISOU 3448  CA  PRO B 450     6135   8238   5665   -651    698    392       C  
ATOM   3449  C   PRO B 450       9.676  23.549  28.820  1.00 50.50           C  
ANISOU 3449  C   PRO B 450     5936   7859   5393   -571    603    353       C  
ATOM   3450  O   PRO B 450      10.906  23.612  28.888  1.00 48.26           O  
ANISOU 3450  O   PRO B 450     5798   7457   5081   -544    588    337       O  
ATOM   3451  CB  PRO B 450       8.619  23.597  31.104  1.00 50.15           C  
ANISOU 3451  CB  PRO B 450     5769   7987   5300   -532    790    378       C  
ATOM   3452  CG  PRO B 450       8.759  22.623  32.230  1.00 50.70           C  
ANISOU 3452  CG  PRO B 450     5880   8063   5321   -615    881    422       C  
ATOM   3453  CD  PRO B 450       9.809  21.655  31.776  1.00 51.35           C  
ANISOU 3453  CD  PRO B 450     6109   8001   5399   -714    832    439       C  
ATOM   3454  N   ASN B 451       8.968  24.144  27.863  1.00 58.46           N  
ANISOU 3454  N   ASN B 451     6845   8925   6443   -536    536    342       N  
ATOM   3455  CA  ASN B 451       9.580  24.997  26.855  1.00 58.67           C  
ANISOU 3455  CA  ASN B 451     6933   8880   6480   -454    447    316       C  
ATOM   3456  C   ASN B 451       9.174  26.436  27.122  1.00 61.17           C  
ANISOU 3456  C   ASN B 451     7181   9248   6813   -292    455    293       C  
ATOM   3457  O   ASN B 451       7.973  26.744  27.095  1.00 62.66           O  
ANISOU 3457  O   ASN B 451     7216   9559   7034   -265    461    299       O  
ATOM   3458  CB  ASN B 451       9.150  24.570  25.452  1.00 57.92           C  
ANISOU 3458  CB  ASN B 451     6793   8802   6414   -535    353    324       C  
ATOM   3459  CG  ASN B 451      10.034  25.153  24.365  1.00 57.34           C  
ANISOU 3459  CG  ASN B 451     6819   8634   6333   -481    266    308       C  
ATOM   3460  OD1 ASN B 451      10.417  26.322  24.416  1.00 56.67           O  
ANISOU 3460  OD1 ASN B 451     6763   8518   6250   -352    256    295       O  
ATOM   3461  ND2 ASN B 451      10.364  24.336  23.373  1.00 57.12           N  
ANISOU 3461  ND2 ASN B 451     6846   8559   6297   -583    203    309       N  
ATOM   3462  N   PRO B 452      10.118  27.343  27.387  1.00 70.42           N  
ANISOU 3462  N   PRO B 452     8457  10329   7970   -182    452    264       N  
ATOM   3463  CA  PRO B 452       9.727  28.736  27.663  1.00 70.62           C  
ANISOU 3463  CA  PRO B 452     8424  10389   8018    -24    458    237       C  
ATOM   3464  C   PRO B 452       9.037  29.412  26.495  1.00 69.68           C  
ANISOU 3464  C   PRO B 452     8215  10310   7948     27    372    247       C  
ATOM   3465  O   PRO B 452       8.238  30.334  26.707  1.00 71.69           O  
ANISOU 3465  O   PRO B 452     8367  10637   8236    140    382    234       O  
ATOM   3466  CB  PRO B 452      11.063  29.409  28.014  1.00 69.83           C  
ANISOU 3466  CB  PRO B 452     8477  10157   7897     54    455    206       C  
ATOM   3467  CG  PRO B 452      12.099  28.560  27.360  1.00 69.56           C  
ANISOU 3467  CG  PRO B 452     8564  10021   7844    -52    412    224       C  
ATOM   3468  CD  PRO B 452      11.578  27.155  27.434  1.00 70.42           C  
ANISOU 3468  CD  PRO B 452     8628  10190   7938   -196    442    254       C  
ATOM   3469  N   ARG B 453       9.317  28.986  25.265  1.00 54.57           N  
ANISOU 3469  N   ARG B 453     6339   8357   6039    -48    288    270       N  
ATOM   3470  CA  ARG B 453       8.615  29.506  24.093  1.00 54.59           C  
ANISOU 3470  CA  ARG B 453     6254   8410   6076    -13    199    288       C  
ATOM   3471  C   ARG B 453       8.910  28.571  22.929  1.00 53.98           C  
ANISOU 3471  C   ARG B 453     6224   8306   5980   -141    126    308       C  
ATOM   3472  O   ARG B 453      10.024  28.579  22.398  1.00 50.87           O  
ANISOU 3472  O   ARG B 453     5965   7800   5561   -151     91    306       O  
ATOM   3473  CB  ARG B 453       9.045  30.935  23.778  1.00 52.90           C  
ANISOU 3473  CB  ARG B 453     6087   8127   5885    137    156    281       C  
ATOM   3474  CG  ARG B 453       8.172  31.613  22.730  1.00 54.30           C  
ANISOU 3474  CG  ARG B 453     6159   8371   6101    200     70    308       C  
ATOM   3475  CD  ARG B 453       8.585  33.057  22.510  1.00 52.46           C  
ANISOU 3475  CD  ARG B 453     5977   8057   5898    352     33    308       C  
ATOM   3476  NE  ARG B 453       9.976  33.166  22.081  1.00 52.65           N  
ANISOU 3476  NE  ARG B 453     6169   7938   5896    333      5    314       N  
ATOM   3477  CZ  ARG B 453      10.359  33.454  20.841  1.00 51.80           C  
ANISOU 3477  CZ  ARG B 453     6112   7785   5783    333    -81    352       C  
ATOM   3478  NH1 ARG B 453       9.454  33.668  19.895  1.00 51.08           N  
ANISOU 3478  NH1 ARG B 453     5923   7779   5707    352   -156    387       N  
ATOM   3479  NH2 ARG B 453      11.650  33.533  20.546  1.00 50.96           N  
ANISOU 3479  NH2 ARG B 453     6152   7557   5654    313    -92    356       N  
ATOM   3480  N   GLU B 454       7.921  27.766  22.547  1.00 71.68           N  
ANISOU 3480  N   GLU B 454     8352  10651   8234   -240    105    321       N  
ATOM   3481  CA  GLU B 454       8.076  26.848  21.430  1.00 72.74           C  
ANISOU 3481  CA  GLU B 454     8521  10768   8349   -364     30    329       C  
ATOM   3482  C   GLU B 454       7.976  27.604  20.111  1.00 70.90           C  
ANISOU 3482  C   GLU B 454     8277  10545   8116   -302    -78    342       C  
ATOM   3483  O   GLU B 454       6.993  28.309  19.864  1.00 70.27           O  
ANISOU 3483  O   GLU B 454     8067  10562   8069   -228   -114    357       O  
ATOM   3484  CB  GLU B 454       7.012  25.751  21.484  1.00 76.03           C  
ANISOU 3484  CB  GLU B 454     8815  11290   8784   -497     38    335       C  
ATOM   3485  CG  GLU B 454       6.716  25.241  22.883  1.00 79.39           C  
ANISOU 3485  CG  GLU B 454     9200  11749   9216   -535    153    338       C  
ATOM   3486  CD  GLU B 454       5.708  24.108  22.893  1.00 80.13           C  
ANISOU 3486  CD  GLU B 454     9174  11936   9334   -684    161    352       C  
ATOM   3487  OE1 GLU B 454       5.377  23.619  23.994  1.00 79.36           O  
ANISOU 3487  OE1 GLU B 454     9034  11878   9242   -729    257    366       O  
ATOM   3488  OE2 GLU B 454       5.244  23.708  21.803  1.00 80.19           O  
ANISOU 3488  OE2 GLU B 454     9133  11982   9355   -759     71    351       O  
ATOM   3489  N   THR B 455       8.989  27.450  19.263  1.00 58.85           N  
ANISOU 3489  N   THR B 455     6886   8924   6552   -330   -128    341       N  
ATOM   3490  CA  THR B 455       9.004  28.062  17.943  1.00 57.24           C  
ANISOU 3490  CA  THR B 455     6690   8727   6332   -285   -230    362       C  
ATOM   3491  C   THR B 455       9.005  26.982  16.871  1.00 57.05           C  
ANISOU 3491  C   THR B 455     6690   8720   6267   -418   -298    352       C  
ATOM   3492  O   THR B 455       9.552  25.890  17.063  1.00 57.67           O  
ANISOU 3492  O   THR B 455     6846   8742   6325   -528   -265    326       O  
ATOM   3493  CB  THR B 455      10.227  28.970  17.744  1.00 54.10           C  
ANISOU 3493  CB  THR B 455     6430   8208   5916   -191   -233    373       C  
ATOM   3494  OG1 THR B 455      11.430  28.212  17.934  1.00 51.83           O  
ANISOU 3494  OG1 THR B 455     6283   7815   5594   -265   -193    351       O  
ATOM   3495  CG2 THR B 455      10.198  30.140  18.718  1.00 52.96           C  
ANISOU 3495  CG2 THR B 455     6264   8040   5816    -52   -180    375       C  
ATOM   3496  N   GLN B 456       8.382  27.298  15.740  1.00 53.91           N  
ANISOU 3496  N   GLN B 456     6227   8398   5856   -403   -397    371       N  
ATOM   3497  CA  GLN B 456       8.395  26.421  14.577  1.00 52.62           C  
ANISOU 3497  CA  GLN B 456     6094   8257   5644   -514   -477    354       C  
ATOM   3498  C   GLN B 456       9.659  26.693  13.772  1.00 51.37           C  
ANISOU 3498  C   GLN B 456     6095   7998   5424   -485   -503    360       C  
ATOM   3499  O   GLN B 456       9.845  27.798  13.253  1.00 48.93           O  
ANISOU 3499  O   GLN B 456     5803   7683   5104   -376   -543    400       O  
ATOM   3500  CB  GLN B 456       7.152  26.638  13.715  1.00 53.24           C  
ANISOU 3500  CB  GLN B 456     6028   8475   5727   -510   -578    371       C  
ATOM   3501  CG  GLN B 456       7.106  25.766  12.472  1.00 54.27           C  
ANISOU 3501  CG  GLN B 456     6186   8637   5796   -623   -672    346       C  
ATOM   3502  CD  GLN B 456       7.250  24.290  12.794  1.00 56.07           C  
ANISOU 3502  CD  GLN B 456     6450   8828   6025   -784   -634    293       C  
ATOM   3503  OE1 GLN B 456       6.463  23.731  13.559  1.00 57.13           O  
ANISOU 3503  OE1 GLN B 456     6479   9014   6215   -852   -594    284       O  
ATOM   3504  NE2 GLN B 456       8.257  23.651  12.208  1.00 55.37           N  
ANISOU 3504  NE2 GLN B 456     6510   8651   5877   -844   -645    261       N  
ATOM   3505  N   LEU B 457      10.530  25.694  13.685  1.00 49.00           N  
ANISOU 3505  N   LEU B 457     5912   7619   5088   -582   -478    324       N  
ATOM   3506  CA  LEU B 457      11.757  25.845  12.921  1.00 49.27           C  
ANISOU 3506  CA  LEU B 457     6092   7566   5062   -563   -494    325       C  
ATOM   3507  C   LEU B 457      11.452  25.946  11.432  1.00 47.37           C  
ANISOU 3507  C   LEU B 457     5843   7397   4758   -572   -603    335       C  
ATOM   3508  O   LEU B 457      10.443  25.432  10.943  1.00 48.49           O  
ANISOU 3508  O   LEU B 457     5890   7640   4893   -638   -669    319       O  
ATOM   3509  CB  LEU B 457      12.699  24.674  13.187  1.00 48.58           C  
ANISOU 3509  CB  LEU B 457     6120   7383   4954   -661   -441    278       C  
ATOM   3510  CG  LEU B 457      13.287  24.658  14.597  1.00 47.98           C  
ANISOU 3510  CG  LEU B 457     6084   7223   4924   -638   -337    276       C  
ATOM   3511  CD1 LEU B 457      13.957  23.331  14.886  1.00 47.84           C  
ANISOU 3511  CD1 LEU B 457     6156   7127   4895   -746   -294    233       C  
ATOM   3512  CD2 LEU B 457      14.269  25.807  14.767  1.00 46.24           C  
ANISOU 3512  CD2 LEU B 457     5940   6926   4702   -520   -309    306       C  
ATOM   3513  N   LEU B 458      12.338  26.630  10.710  1.00 47.90           N  
ANISOU 3513  N   LEU B 458     6009   7416   4775   -505   -622    366       N  
ATOM   3514  CA  LEU B 458      12.202  26.802   9.266  1.00 47.63           C  
ANISOU 3514  CA  LEU B 458     5987   7447   4663   -503   -720    384       C  
ATOM   3515  C   LEU B 458      12.671  25.519   8.587  1.00 48.63           C  
ANISOU 3515  C   LEU B 458     6197   7559   4720   -624   -737    319       C  
ATOM   3516  O   LEU B 458      13.819  25.385   8.155  1.00 49.77           O  
ANISOU 3516  O   LEU B 458     6469   7631   4810   -626   -712    310       O  
ATOM   3517  CB  LEU B 458      12.990  28.016   8.795  1.00 46.79           C  
ANISOU 3517  CB  LEU B 458     5956   7293   4530   -391   -725    450       C  
ATOM   3518  CG  LEU B 458      12.492  29.365   9.321  1.00 50.21           C  
ANISOU 3518  CG  LEU B 458     6313   7733   5033   -263   -723    512       C  
ATOM   3519  CD1 LEU B 458      13.487  30.475   9.023  1.00 49.18           C  
ANISOU 3519  CD1 LEU B 458     6280   7517   4891   -168   -710    574       C  
ATOM   3520  CD2 LEU B 458      11.138  29.688   8.724  1.00 49.76           C  
ANISOU 3520  CD2 LEU B 458     6121   7809   4975   -235   -820    541       C  
ATOM   3521  N   ASP B 459      11.758  24.554   8.504  1.00 59.72           N  
ANISOU 3521  N   ASP B 459     7525   9035   6132   -727   -777    271       N  
ATOM   3522  CA  ASP B 459      12.079  23.273   7.897  1.00 60.77           C  
ANISOU 3522  CA  ASP B 459     7731   9149   6209   -846   -799    197       C  
ATOM   3523  C   ASP B 459      12.453  23.461   6.426  1.00 61.44           C  
ANISOU 3523  C   ASP B 459     7887   9275   6181   -830   -877    198       C  
ATOM   3524  O   ASP B 459      11.896  24.325   5.741  1.00 62.50           O  
ANISOU 3524  O   ASP B 459     7963   9500   6283   -763   -952    251       O  
ATOM   3525  CB  ASP B 459      10.898  22.313   8.028  1.00 61.82           C  
ANISOU 3525  CB  ASP B 459     7755   9356   6380   -962   -842    150       C  
ATOM   3526  CG  ASP B 459      10.617  21.927   9.470  1.00 65.29           C  
ANISOU 3526  CG  ASP B 459     8138   9752   6918   -997   -753    148       C  
ATOM   3527  OD1 ASP B 459      11.572  21.909  10.277  1.00 66.27           O  
ANISOU 3527  OD1 ASP B 459     8352   9765   7064   -971   -659    152       O  
ATOM   3528  OD2 ASP B 459       9.445  21.641   9.797  1.00 65.80           O  
ANISOU 3528  OD2 ASP B 459     8067   9900   7035  -1052   -776    144       O  
ATOM   3529  N   PRO B 460      13.400  22.667   5.918  1.00 59.84           N  
ANISOU 3529  N   PRO B 460     7812   9010   5915   -885   -860    142       N  
ATOM   3530  CA  PRO B 460      13.872  22.879   4.550  1.00 58.30           C  
ANISOU 3530  CA  PRO B 460     7695   8856   5601   -862   -919    144       C  
ATOM   3531  C   PRO B 460      12.765  22.619   3.544  1.00 57.45           C  
ANISOU 3531  C   PRO B 460     7511   8884   5433   -912  -1043    120       C  
ATOM   3532  O   PRO B 460      11.907  21.744   3.753  1.00 56.97           O  
ANISOU 3532  O   PRO B 460     7376   8859   5411  -1011  -1079     62       O  
ATOM   3533  CB  PRO B 460      15.013  21.857   4.406  1.00 58.24           C  
ANISOU 3533  CB  PRO B 460     7824   8751   5552   -923   -863     69       C  
ATOM   3534  CG  PRO B 460      14.746  20.831   5.462  1.00 59.27           C  
ANISOU 3534  CG  PRO B 460     7929   8816   5774  -1012   -816     13       C  
ATOM   3535  CD  PRO B 460      14.118  21.574   6.596  1.00 60.18           C  
ANISOU 3535  CD  PRO B 460     7935   8940   5990   -961   -781     78       C  
ATOM   3536  N   PRO B 461      12.741  23.359   2.437  1.00 59.39           N  
ANISOU 3536  N   PRO B 461     7771   9213   5583   -849  -1116    168       N  
ATOM   3537  CA  PRO B 461      11.665  23.188   1.454  1.00 61.04           C  
ANISOU 3537  CA  PRO B 461     7902   9564   5727   -888  -1247    150       C  
ATOM   3538  C   PRO B 461      11.688  21.811   0.805  1.00 61.82           C  
ANISOU 3538  C   PRO B 461     8057   9674   5759  -1015  -1289     31       C  
ATOM   3539  O   PRO B 461      12.684  21.084   0.847  1.00 60.17           O  
ANISOU 3539  O   PRO B 461     7968   9366   5526  -1055  -1222    -30       O  
ATOM   3540  CB  PRO B 461      11.948  24.289   0.421  1.00 58.86           C  
ANISOU 3540  CB  PRO B 461     7665   9351   5348   -783  -1297    235       C  
ATOM   3541  CG  PRO B 461      12.767  25.301   1.155  1.00 59.97           C  
ANISOU 3541  CG  PRO B 461     7847   9390   5550   -679  -1197    319       C  
ATOM   3542  CD  PRO B 461      13.605  24.507   2.117  1.00 58.75           C  
ANISOU 3542  CD  PRO B 461     7761   9102   5459   -734  -1084    255       C  
ATOM   3543  N   ASP B 462      10.553  21.462   0.200  1.00 85.32           N  
ANISOU 3543  N   ASP B 462    10940  12772   8708  -1077  -1408     -4       N  
ATOM   3544  CA  ASP B 462      10.434  20.224  -0.560  1.00 87.41           C  
ANISOU 3544  CA  ASP B 462    11251  13062   8901  -1198  -1473   -122       C  
ATOM   3545  C   ASP B 462      11.506  20.153  -1.639  1.00 85.48           C  
ANISOU 3545  C   ASP B 462    11163  12808   8508  -1171  -1471   -151       C  
ATOM   3546  O   ASP B 462      11.746  21.125  -2.359  1.00 85.35           O  
ANISOU 3546  O   ASP B 462    11172  12857   8401  -1074  -1499    -73       O  
ATOM   3547  CB  ASP B 462       9.045  20.139  -1.199  1.00 91.15           C  
ANISOU 3547  CB  ASP B 462    11591  13691   9352  -1249  -1619   -139       C  
ATOM   3548  CG  ASP B 462       8.089  19.261  -0.418  1.00 94.26           C  
ANISOU 3548  CG  ASP B 462    11868  14080   9868  -1370  -1630   -196       C  
ATOM   3549  OD1 ASP B 462       8.123  19.298   0.830  1.00 94.70           O  
ANISOU 3549  OD1 ASP B 462    11883  14051  10047  -1365  -1530   -164       O  
ATOM   3550  OD2 ASP B 462       7.292  18.539  -1.057  1.00 95.84           O  
ANISOU 3550  OD2 ASP B 462    12015  14364  10036  -1473  -1741   -272       O  
ATOM   3551  N   GLY B 463      12.156  18.996  -1.742  1.00 63.24           N  
ANISOU 3551  N   GLY B 463     8454   9909   5667  -1254  -1435   -261       N  
ATOM   3552  CA  GLY B 463      13.111  18.769  -2.807  1.00 61.31           C  
ANISOU 3552  CA  GLY B 463     8353   9667   5276  -1237  -1434   -309       C  
ATOM   3553  C   GLY B 463      14.476  19.386  -2.610  1.00 60.35           C  
ANISOU 3553  C   GLY B 463     8337   9457   5137  -1139  -1315   -247       C  
ATOM   3554  O   GLY B 463      15.188  19.607  -3.594  1.00 59.08           O  
ANISOU 3554  O   GLY B 463     8272   9335   4841  -1094  -1317   -245       O  
ATOM   3555  N   THR B 464      14.870  19.672  -1.368  1.00 63.93           N  
ANISOU 3555  N   THR B 464     8774   9799   5719  -1106  -1211   -195       N  
ATOM   3556  CA  THR B 464      16.190  20.248  -1.132  1.00 63.71           C  
ANISOU 3556  CA  THR B 464     8839   9684   5684  -1020  -1100   -139       C  
ATOM   3557  C   THR B 464      17.294  19.231  -1.398  1.00 62.56           C  
ANISOU 3557  C   THR B 464     8827   9454   5488  -1059  -1038   -240       C  
ATOM   3558  O   THR B 464      18.345  19.576  -1.953  1.00 61.27           O  
ANISOU 3558  O   THR B 464     8757   9283   5240   -999   -987   -218       O  
ATOM   3559  CB  THR B 464      16.285  20.779   0.298  1.00 63.22           C  
ANISOU 3559  CB  THR B 464     8722   9528   5771   -979  -1015    -70       C  
ATOM   3560  OG1 THR B 464      15.305  21.805   0.499  1.00 65.39           O  
ANISOU 3560  OG1 THR B 464     8875   9881   6089   -925  -1068     22       O  
ATOM   3561  CG2 THR B 464      17.669  21.344   0.562  1.00 60.65           C  
ANISOU 3561  CG2 THR B 464     8489   9111   5445   -899   -907    -19       C  
ATOM   3562  N   GLU B 465      17.071  17.973  -1.011  1.00 80.51           N  
ANISOU 3562  N   GLU B 465    11111  11663   7817  -1160  -1039   -347       N  
ATOM   3563  CA  GLU B 465      18.083  16.940  -1.208  1.00 81.49           C  
ANISOU 3563  CA  GLU B 465    11361  11695   7907  -1193   -981   -450       C  
ATOM   3564  C   GLU B 465      18.311  16.668  -2.690  1.00 81.50           C  
ANISOU 3564  C   GLU B 465    11443  11786   7738  -1195  -1040   -519       C  
ATOM   3565  O   GLU B 465      19.440  16.386  -3.110  1.00 81.79           O  
ANISOU 3565  O   GLU B 465    11592  11781   7705  -1163   -975   -562       O  
ATOM   3566  CB  GLU B 465      17.681  15.661  -0.469  1.00 85.37           C  
ANISOU 3566  CB  GLU B 465    11843  12092   8503  -1303   -980   -543       C  
ATOM   3567  CG  GLU B 465      16.196  15.304  -0.559  1.00 89.09           C  
ANISOU 3567  CG  GLU B 465    12204  12642   9004  -1398  -1092   -574       C  
ATOM   3568  CD  GLU B 465      15.346  16.020   0.479  1.00 90.57           C  
ANISOU 3568  CD  GLU B 465    12252  12850   9310  -1384  -1086   -473       C  
ATOM   3569  OE1 GLU B 465      15.032  17.209   0.264  1.00 91.25           O  
ANISOU 3569  OE1 GLU B 465    12274  13031   9367  -1302  -1114   -377       O  
ATOM   3570  OE2 GLU B 465      14.990  15.397   1.504  1.00 90.63           O  
ANISOU 3570  OE2 GLU B 465    12217  12780   9438  -1453  -1053   -489       O  
ATOM   3571  N   GLU B 466      17.252  16.752  -3.501  1.00 73.93           N  
ANISOU 3571  N   GLU B 466    10425  10960   6705  -1231  -1164   -533       N  
ATOM   3572  CA  GLU B 466      17.409  16.610  -4.947  1.00 75.91           C  
ANISOU 3572  CA  GLU B 466    10749  11317   6774  -1226  -1228   -592       C  
ATOM   3573  C   GLU B 466      18.153  17.804  -5.538  1.00 73.95           C  
ANISOU 3573  C   GLU B 466    10541  11133   6423  -1109  -1188   -479       C  
ATOM   3574  O   GLU B 466      18.982  17.651  -6.451  1.00 72.73           O  
ANISOU 3574  O   GLU B 466    10493  11011   6133  -1080  -1162   -519       O  
ATOM   3575  CB  GLU B 466      16.039  16.452  -5.613  1.00 78.44           C  
ANISOU 3575  CB  GLU B 466    10987  11771   7045  -1292  -1381   -628       C  
ATOM   3576  CG  GLU B 466      15.308  15.141  -5.309  1.00 80.86           C  
ANISOU 3576  CG  GLU B 466    11267  12027   7429  -1427  -1436   -759       C  
ATOM   3577  CD  GLU B 466      14.638  15.131  -3.946  1.00 81.31           C  
ANISOU 3577  CD  GLU B 466    11208  12011   7674  -1469  -1410   -709       C  
ATOM   3578  OE1 GLU B 466      14.775  16.130  -3.211  1.00 79.82           O  
ANISOU 3578  OE1 GLU B 466    10965  11807   7555  -1387  -1346   -583       O  
ATOM   3579  OE2 GLU B 466      13.969  14.127  -3.614  1.00 82.53           O  
ANISOU 3579  OE2 GLU B 466    11326  12124   7907  -1586  -1451   -796       O  
ATOM   3580  N   TRP B 467      17.869  19.003  -5.028  1.00 64.34           N  
ANISOU 3580  N   TRP B 467     9241   9936   5271  -1041  -1180   -337       N  
ATOM   3581  CA  TRP B 467      18.488  20.198  -5.582  1.00 64.49           C  
ANISOU 3581  CA  TRP B 467     9291  10010   5203   -937  -1149   -216       C  
ATOM   3582  C   TRP B 467      19.957  20.296  -5.206  1.00 63.84           C  
ANISOU 3582  C   TRP B 467     9298   9816   5141   -887  -1008   -198       C  
ATOM   3583  O   TRP B 467      20.745  20.857  -5.971  1.00 64.69           O  
ANISOU 3583  O   TRP B 467     9473   9969   5137   -826   -972   -145       O  
ATOM   3584  CB  TRP B 467      17.727  21.444  -5.135  1.00 63.58           C  
ANISOU 3584  CB  TRP B 467     9063   9934   5162   -877  -1187    -75       C  
ATOM   3585  CG  TRP B 467      16.660  21.831  -6.107  1.00 64.83           C  
ANISOU 3585  CG  TRP B 467     9162  10253   5218   -873  -1326    -45       C  
ATOM   3586  CD1 TRP B 467      15.339  21.491  -6.053  1.00 65.11           C  
ANISOU 3586  CD1 TRP B 467     9090  10358   5290   -933  -1437    -84       C  
ATOM   3587  CD2 TRP B 467      16.825  22.613  -7.294  1.00 65.14           C  
ANISOU 3587  CD2 TRP B 467     9242  10409   5097   -806  -1371     33       C  
ATOM   3588  NE1 TRP B 467      14.670  22.024  -7.128  1.00 66.80           N  
ANISOU 3588  NE1 TRP B 467     9274  10727   5379   -904  -1556    -37       N  
ATOM   3589  CE2 TRP B 467      15.560  22.716  -7.906  1.00 65.97           C  
ANISOU 3589  CE2 TRP B 467     9264  10654   5148   -825  -1518     38       C  
ATOM   3590  CE3 TRP B 467      17.919  23.241  -7.897  1.00 64.30           C  
ANISOU 3590  CE3 TRP B 467     9233  10309   4890   -735  -1301    107       C  
ATOM   3591  CZ2 TRP B 467      15.358  23.423  -9.089  1.00 66.85           C  
ANISOU 3591  CZ2 TRP B 467     9392  10907   5101   -769  -1600    115       C  
ATOM   3592  CZ3 TRP B 467      17.717  23.942  -9.073  1.00 68.35           C  
ANISOU 3592  CZ3 TRP B 467     9764  10961   5246   -685  -1375    187       C  
ATOM   3593  CH2 TRP B 467      16.447  24.027  -9.656  1.00 67.89           C  
ANISOU 3593  CH2 TRP B 467     9627  11038   5131   -700  -1526    191       C  
ATOM   3594  N   GLU B 468      20.352  19.755  -4.053  1.00 65.56           N  
ANISOU 3594  N   GLU B 468     9518   9895   5499   -913   -928   -237       N  
ATOM   3595  CA  GLU B 468      21.778  19.638  -3.766  1.00 65.74           C  
ANISOU 3595  CA  GLU B 468     9628   9816   5534   -875   -803   -243       C  
ATOM   3596  C   GLU B 468      22.487  18.879  -4.884  1.00 65.98           C  
ANISOU 3596  C   GLU B 468     9768   9885   5416   -886   -791   -343       C  
ATOM   3597  O   GLU B 468      23.464  19.369  -5.460  1.00 65.20           O  
ANISOU 3597  O   GLU B 468     9731   9812   5229   -824   -727   -298       O  
ATOM   3598  CB  GLU B 468      21.989  18.955  -2.412  1.00 65.10           C  
ANISOU 3598  CB  GLU B 468     9535   9587   5613   -912   -737   -288       C  
ATOM   3599  CG  GLU B 468      21.595  19.823  -1.217  1.00 67.22           C  
ANISOU 3599  CG  GLU B 468     9709   9809   6022   -880   -717   -182       C  
ATOM   3600  CD  GLU B 468      21.912  19.174   0.116  1.00 67.50           C  
ANISOU 3600  CD  GLU B 468     9743   9705   6198   -910   -644   -219       C  
ATOM   3601  OE1 GLU B 468      22.965  18.510   0.225  1.00 67.22           O  
ANISOU 3601  OE1 GLU B 468     9791   9585   6163   -910   -570   -277       O  
ATOM   3602  OE2 GLU B 468      21.103  19.326   1.054  1.00 68.13           O  
ANISOU 3602  OE2 GLU B 468     9736   9765   6386   -930   -661   -188       O  
ATOM   3603  N   GLU B 469      21.980  17.687  -5.215  1.00 84.30           N  
ANISOU 3603  N   GLU B 469    12112  12212   7706   -967   -852   -482       N  
ATOM   3604  CA  GLU B 469      22.466  16.885  -6.339  1.00 85.29           C  
ANISOU 3604  CA  GLU B 469    12341  12383   7681   -983   -858   -600       C  
ATOM   3605  C   GLU B 469      22.591  17.715  -7.610  1.00 87.54           C  
ANISOU 3605  C   GLU B 469    12654  12823   7784   -924   -889   -536       C  
ATOM   3606  O   GLU B 469      23.656  17.767  -8.255  1.00 87.59           O  
ANISOU 3606  O   GLU B 469    12746  12851   7683   -874   -814   -543       O  
ATOM   3607  CB  GLU B 469      21.497  15.725  -6.589  1.00 87.91           C  
ANISOU 3607  CB  GLU B 469    12669  12726   8006  -1086   -962   -742       C  
ATOM   3608  CG  GLU B 469      21.362  14.708  -5.473  1.00 89.53           C  
ANISOU 3608  CG  GLU B 469    12863  12779   8376  -1159   -936   -819       C  
ATOM   3609  CD  GLU B 469      22.613  14.559  -4.645  1.00 90.39           C  
ANISOU 3609  CD  GLU B 469    13025  12746   8573  -1111   -799   -806       C  
ATOM   3610  OE1 GLU B 469      22.563  14.874  -3.436  1.00 87.79           O  
ANISOU 3610  OE1 GLU B 469    12634  12331   8390  -1105   -754   -730       O  
ATOM   3611  OE2 GLU B 469      23.638  14.111  -5.202  1.00 92.85           O  
ANISOU 3611  OE2 GLU B 469    13438  13038   8805  -1077   -738   -876       O  
ATOM   3612  N   LYS B 470      21.467  18.305  -8.023  1.00 83.78           N  
ANISOU 3612  N   LYS B 470    12105  12463   7265   -933  -1004   -476       N  
ATOM   3613  CA  LYS B 470      21.431  18.975  -9.316  1.00 84.10           C  
ANISOU 3613  CA  LYS B 470    12176  12663   7117   -886  -1055   -421       C  
ATOM   3614  C   LYS B 470      22.380  20.167  -9.351  1.00 82.50           C  
ANISOU 3614  C   LYS B 470    11992  12460   6893   -790   -959   -269       C  
ATOM   3615  O   LYS B 470      23.068  20.380 -10.354  1.00 83.43           O  
ANISOU 3615  O   LYS B 470    12187  12662   6852   -749   -927   -253       O  
ATOM   3616  CB  LYS B 470      20.001  19.388  -9.654  1.00 84.98           C  
ANISOU 3616  CB  LYS B 470    12192  12892   7203   -909  -1204   -379       C  
ATOM   3617  CG  LYS B 470      19.703  19.423 -11.151  1.00 86.73           C  
ANISOU 3617  CG  LYS B 470    12460  13289   7203   -904  -1300   -403       C  
ATOM   3618  CD  LYS B 470      20.274  18.213 -11.900  1.00 87.67           C  
ANISOU 3618  CD  LYS B 470    12694  13414   7202   -943  -1282   -578       C  
ATOM   3619  CE  LYS B 470      19.705  16.883 -11.411  1.00 88.34           C  
ANISOU 3619  CE  LYS B 470    12769  13417   7380  -1053  -1331   -745       C  
ATOM   3620  NZ  LYS B 470      20.717  15.790 -11.507  1.00 88.66           N  
ANISOU 3620  NZ  LYS B 470    12924  13362   7401  -1067  -1241   -891       N  
ATOM   3621  N   LEU B 471      22.461  20.933  -8.259  1.00 67.10           N  
ANISOU 3621  N   LEU B 471     9976  10417   5103   -757   -908   -159       N  
ATOM   3622  CA  LEU B 471      23.380  22.065  -8.216  1.00 63.78           C  
ANISOU 3622  CA  LEU B 471     9572   9979   4682   -676   -818    -17       C  
ATOM   3623  C   LEU B 471      24.830  21.607  -8.286  1.00 64.62           C  
ANISOU 3623  C   LEU B 471     9769  10023   4759   -659   -688    -68       C  
ATOM   3624  O   LEU B 471      25.646  22.223  -8.981  1.00 65.26           O  
ANISOU 3624  O   LEU B 471     9900  10160   4738   -607   -630      8       O  
ATOM   3625  CB  LEU B 471      23.143  22.893  -6.953  1.00 64.55           C  
ANISOU 3625  CB  LEU B 471     9583   9977   4966   -648   -795     88       C  
ATOM   3626  CG  LEU B 471      21.896  23.780  -6.894  1.00 65.26           C  
ANISOU 3626  CG  LEU B 471     9575  10133   5089   -628   -901    187       C  
ATOM   3627  CD1 LEU B 471      21.857  24.535  -5.575  1.00 64.03           C  
ANISOU 3627  CD1 LEU B 471     9347   9862   5119   -594   -856    272       C  
ATOM   3628  CD2 LEU B 471      21.842  24.745  -8.067  1.00 64.26           C  
ANISOU 3628  CD2 LEU B 471     9468  10134   4812   -571   -949    302       C  
ATOM   3629  N   LYS B 472      25.184  20.534  -7.573  1.00 76.19           N  
ANISOU 3629  N   LYS B 472    11257  11375   6317   -700   -639   -190       N  
ATOM   3630  CA  LYS B 472      26.598  20.168  -7.566  1.00 78.18           C  
ANISOU 3630  CA  LYS B 472    11583  11564   6556   -672   -512   -229       C  
ATOM   3631  C   LYS B 472      27.028  19.556  -8.892  1.00 80.87           C  
ANISOU 3631  C   LYS B 472    12017  12009   6702   -669   -507   -322       C  
ATOM   3632  O   LYS B 472      28.209  19.643  -9.248  1.00 81.90           O  
ANISOU 3632  O   LYS B 472    12202  12143   6771   -624   -403   -311       O  
ATOM   3633  CB  LYS B 472      26.932  19.219  -6.414  1.00 77.75           C  
ANISOU 3633  CB  LYS B 472    11530  11354   6658   -705   -459   -323       C  
ATOM   3634  CG  LYS B 472      26.006  18.041  -6.244  1.00 79.43           C  
ANISOU 3634  CG  LYS B 472    11739  11539   6903   -786   -540   -460       C  
ATOM   3635  CD  LYS B 472      26.522  17.098  -5.172  1.00 79.32           C  
ANISOU 3635  CD  LYS B 472    11743  11365   7030   -811   -473   -541       C  
ATOM   3636  CE  LYS B 472      26.159  17.621  -3.790  1.00 78.92           C  
ANISOU 3636  CE  LYS B 472    11606  11224   7156   -814   -464   -451       C  
ATOM   3637  NZ  LYS B 472      25.807  16.535  -2.835  1.00 79.20           N  
ANISOU 3637  NZ  LYS B 472    11633  11141   7317   -880   -470   -541       N  
ATOM   3638  N   GLU B 473      26.108  18.943  -9.641  1.00100.80           N  
ANISOU 3638  N   GLU B 473    14555  14622   9122   -717   -617   -416       N  
ATOM   3639  CA  GLU B 473      26.533  18.503 -10.971  1.00102.79           C  
ANISOU 3639  CA  GLU B 473    14899  14990   9166   -705   -613   -497       C  
ATOM   3640  C   GLU B 473      26.461  19.633 -11.997  1.00104.37           C  
ANISOU 3640  C   GLU B 473    15089  15330   9238   -638   -635   -360       C  
ATOM   3641  O   GLU B 473      27.253  19.649 -12.948  1.00106.39           O  
ANISOU 3641  O   GLU B 473    15399  15643   9383   -574   -570   -365       O  
ATOM   3642  CB  GLU B 473      25.722  17.301 -11.461  1.00104.79           C  
ANISOU 3642  CB  GLU B 473    15178  15268   9368   -770   -715   -671       C  
ATOM   3643  CG  GLU B 473      26.360  16.615 -12.677  1.00107.34           C  
ANISOU 3643  CG  GLU B 473    15582  15644   9558   -718   -681   -785       C  
ATOM   3644  CD  GLU B 473      25.698  17.003 -13.986  1.00110.13           C  
ANISOU 3644  CD  GLU B 473    15934  16152   9761   -684   -775   -759       C  
ATOM   3645  OE1 GLU B 473      26.112  16.492 -15.051  1.00111.46           O  
ANISOU 3645  OE1 GLU B 473    16170  16375   9803   -639   -760   -848       O  
ATOM   3646  OE2 GLU B 473      24.748  17.813 -13.946  1.00110.30           O  
ANISOU 3646  OE2 GLU B 473    15886  16236   9787   -697   -869   -650       O  
ATOM   3647  N   LEU B 474      25.534  20.582 -11.826  1.00 84.28           N  
ANISOU 3647  N   LEU B 474    12472  12835   6716   -642   -722   -233       N  
ATOM   3648  CA  LEU B 474      25.541  21.788 -12.648  1.00 83.29           C  
ANISOU 3648  CA  LEU B 474    12335  12808   6503   -567   -732    -76       C  
ATOM   3649  C   LEU B 474      26.831  22.571 -12.459  1.00 82.99           C  
ANISOU 3649  C   LEU B 474    12320  12725   6488   -510   -591     42       C  
ATOM   3650  O   LEU B 474      27.284  23.261 -13.381  1.00 83.71           O  
ANISOU 3650  O   LEU B 474    12438  12886   6480   -445   -556    136       O  
ATOM   3651  CB  LEU B 474      24.338  22.665 -12.297  1.00 81.29           C  
ANISOU 3651  CB  LEU B 474    11992  12593   6300   -578   -847     41       C  
ATOM   3652  CG  LEU B 474      23.104  22.607 -13.195  1.00 82.54           C  
ANISOU 3652  CG  LEU B 474    12122  12872   6368   -582   -996     19       C  
ATOM   3653  CD1 LEU B 474      21.989  23.463 -12.614  1.00 79.02           C  
ANISOU 3653  CD1 LEU B 474    11572  12449   6003   -589  -1097    135       C  
ATOM   3654  CD2 LEU B 474      23.463  23.067 -14.595  1.00 84.63           C  
ANISOU 3654  CD2 LEU B 474    12446  13235   6474   -506   -987     75       C  
ATOM   3655  N   LEU B 475      27.418  22.488 -11.263  1.00 83.91           N  
ANISOU 3655  N   LEU B 475    12423  12717   6741   -534   -511     41       N  
ATOM   3656  CA  LEU B 475      28.743  23.043 -11.014  1.00 83.16           C  
ANISOU 3656  CA  LEU B 475    12347  12565   6685   -488   -372    125       C  
ATOM   3657  C   LEU B 475      29.751  22.502 -12.021  1.00 84.18           C  
ANISOU 3657  C   LEU B 475    12549  12750   6686   -450   -284     54       C  
ATOM   3658  O   LEU B 475      30.429  23.262 -12.721  1.00 82.94           O  
ANISOU 3658  O   LEU B 475    12406  12647   6460   -392   -220    162       O  
ATOM   3659  CB  LEU B 475      29.169  22.708  -9.582  1.00 82.08           C  
ANISOU 3659  CB  LEU B 475    12172  12251   6763   -501   -307     87       C  
ATOM   3660  CG  LEU B 475      29.862  23.762  -8.717  1.00 82.22           C  
ANISOU 3660  CG  LEU B 475    12145  12172   6922   -464   -226    226       C  
ATOM   3661  CD1 LEU B 475      29.047  25.041  -8.658  1.00 82.46           C  
ANISOU 3661  CD1 LEU B 475    12117  12230   6984   -443   -301    383       C  
ATOM   3662  CD2 LEU B 475      30.096  23.209  -7.316  1.00 80.72           C  
ANISOU 3662  CD2 LEU B 475    11923  11823   6926   -484   -186    158       C  
ATOM   3663  N   LYS B 476      29.850  21.179 -12.112  1.00 95.24           N  
ANISOU 3663  N   LYS B 476    13993  14129   8066   -476   -281   -128       N  
ATOM   3664  CA  LYS B 476      30.707  20.535 -13.096  1.00 97.08           C  
ANISOU 3664  CA  LYS B 476    14291  14414   8182   -428   -207   -220       C  
ATOM   3665  C   LYS B 476      30.101  20.658 -14.491  1.00 98.81           C  
ANISOU 3665  C   LYS B 476    14538  14769   8236   -395   -286   -218       C  
ATOM   3666  O   LYS B 476      30.752  21.126 -15.424  1.00100.20           O  
ANISOU 3666  O   LYS B 476    14751  15019   8301   -333   -224   -152       O  
ATOM   3667  CB  LYS B 476      30.922  19.062 -12.741  1.00 96.79           C  
ANISOU 3667  CB  LYS B 476    14296  14297   8184   -463   -190   -421       C  
ATOM   3668  CG  LYS B 476      31.066  18.794 -11.252  1.00 95.56           C  
ANISOU 3668  CG  LYS B 476    14119  13989   8200   -516   -160   -439       C  
ATOM   3669  CD  LYS B 476      31.983  17.607 -10.995  1.00 95.85           C  
ANISOU 3669  CD  LYS B 476    14211  13937   8272   -509    -73   -592       C  
ATOM   3670  CE  LYS B 476      31.239  16.466 -10.320  1.00 95.52           C  
ANISOU 3670  CE  LYS B 476    14181  13788   8324   -579   -147   -736       C  
ATOM   3671  NZ  LYS B 476      32.104  15.266 -10.141  1.00 95.05           N  
ANISOU 3671  NZ  LYS B 476    14183  13632   8297   -565    -69   -887       N  
ATOM   3672  N   ALA C   2      21.256  55.825  85.671  1.00 66.50           N  
ANISOU 3672  N   ALA C   2     7463  10529   7274    327   -538  -2739       N  
ATOM   3673  CA  ALA C   2      20.724  56.356  84.422  1.00 66.02           C  
ANISOU 3673  CA  ALA C   2     7381  10247   7457    218   -459  -2679       C  
ATOM   3674  C   ALA C   2      19.728  57.479  84.679  1.00 63.41           C  
ANISOU 3674  C   ALA C   2     7045   9870   7177    236   -414  -2822       C  
ATOM   3675  O   ALA C   2      19.014  57.475  85.682  1.00 65.11           O  
ANISOU 3675  O   ALA C   2     7295  10242   7201    336   -384  -2878       O  
ATOM   3676  CB  ALA C   2      20.068  55.247  83.611  1.00 64.55           C  
ANISOU 3676  CB  ALA C   2     7256  10014   7255    185   -351  -2409       C  
ATOM   3677  N   LYS C   3      19.692  58.444  83.766  1.00 72.11           N  
ANISOU 3677  N   LYS C   3     8105  10761   8533    149   -408  -2875       N  
ATOM   3678  CA  LYS C   3      18.688  59.496  83.816  1.00 68.57           C  
ANISOU 3678  CA  LYS C   3     7659  10234   8162    170   -362  -2990       C  
ATOM   3679  C   LYS C   3      17.375  58.968  83.255  1.00 66.84           C  
ANISOU 3679  C   LYS C   3     7481   9998   7916    171   -219  -2794       C  
ATOM   3680  O   LYS C   3      17.343  58.405  82.158  1.00 64.43           O  
ANISOU 3680  O   LYS C   3     7184   9587   7711     92   -170  -2604       O  
ATOM   3681  CB  LYS C   3      19.157  60.712  83.025  1.00 65.84           C  
ANISOU 3681  CB  LYS C   3     7262   9650   8105     75   -412  -3102       C  
ATOM   3682  CG  LYS C   3      18.210  61.882  83.092  1.00 66.55           C  
ANISOU 3682  CG  LYS C   3     7363   9635   8289    111   -384  -3240       C  
ATOM   3683  CD  LYS C   3      18.573  62.909  82.047  1.00 67.86           C  
ANISOU 3683  CD  LYS C   3     7496   9530   8759      0   -410  -3272       C  
ATOM   3684  CE  LYS C   3      18.227  64.301  82.517  1.00 70.29           C  
ANISOU 3684  CE  LYS C   3     7808   9731   9169     44   -464  -3516       C  
ATOM   3685  NZ  LYS C   3      18.150  64.400  84.007  1.00 72.48           N  
ANISOU 3685  NZ  LYS C   3     8098  10210   9232    175   -530  -3726       N  
ATOM   3686  N   VAL C   4      16.294  59.145  84.010  1.00 74.97           N  
ANISOU 3686  N   VAL C   4     8530  11146   8808    264   -157  -2846       N  
ATOM   3687  CA  VAL C   4      15.005  58.573  83.653  1.00 75.33           C  
ANISOU 3687  CA  VAL C   4     8596  11219   8805    268    -24  -2665       C  
ATOM   3688  C   VAL C   4      13.975  59.691  83.537  1.00 74.03           C  
ANISOU 3688  C   VAL C   4     8410  10980   8740    310     24  -2781       C  
ATOM   3689  O   VAL C   4      14.172  60.807  84.025  1.00 74.59           O  
ANISOU 3689  O   VAL C   4     8466  11016   8860    363    -43  -3013       O  
ATOM   3690  CB  VAL C   4      14.559  57.503  84.670  1.00 77.44           C  
ANISOU 3690  CB  VAL C   4     8899  11738   8788    343     32  -2563       C  
ATOM   3691  CG1 VAL C   4      15.535  56.347  84.666  1.00 78.40           C  
ANISOU 3691  CG1 VAL C   4     9056  11906   8826    309    -18  -2426       C  
ATOM   3692  CG2 VAL C   4      14.514  58.086  86.048  1.00 78.18           C  
ANISOU 3692  CG2 VAL C   4     8988  12013   8703    472     -3  -2775       C  
ATOM   3693  N   TYR C   5      12.862  59.376  82.875  1.00 60.77           N  
ANISOU 3693  N   TYR C   5     6726   9270   7094    290    133  -2624       N  
ATOM   3694  CA  TYR C   5      11.860  60.366  82.497  1.00 60.43           C  
ANISOU 3694  CA  TYR C   5     6656   9130   7175    327    180  -2700       C  
ATOM   3695  C   TYR C   5      10.480  59.913  82.946  1.00 60.85           C  
ANISOU 3695  C   TYR C   5     6686   9362   7072    396    301  -2618       C  
ATOM   3696  O   TYR C   5      10.062  58.790  82.645  1.00 61.17           O  
ANISOU 3696  O   TYR C   5     6729   9467   7047    341    372  -2402       O  
ATOM   3697  CB  TYR C   5      11.872  60.603  80.983  1.00 59.21           C  
ANISOU 3697  CB  TYR C   5     6499   8731   7267    227    186  -2591       C  
ATOM   3698  CG  TYR C   5      13.250  60.885  80.436  1.00 58.97           C  
ANISOU 3698  CG  TYR C   5     6478   8541   7389    140     89  -2623       C  
ATOM   3699  CD1 TYR C   5      14.039  59.864  79.922  1.00 58.13           C  
ANISOU 3699  CD1 TYR C   5     6383   8433   7269     59     74  -2461       C  
ATOM   3700  CD2 TYR C   5      13.771  62.172  80.449  1.00 58.88           C  
ANISOU 3700  CD2 TYR C   5     6455   8380   7535    140     10  -2816       C  
ATOM   3701  CE1 TYR C   5      15.304  60.119  79.427  1.00 57.90           C  
ANISOU 3701  CE1 TYR C   5     6342   8284   7373    -16     -5  -2487       C  
ATOM   3702  CE2 TYR C   5      15.032  62.436  79.957  1.00 58.13           C  
ANISOU 3702  CE2 TYR C   5     6349   8150   7588     45    -71  -2835       C  
ATOM   3703  CZ  TYR C   5      15.795  61.407  79.448  1.00 57.31           C  
ANISOU 3703  CZ  TYR C   5     6243   8074   7460    -31    -73  -2668       C  
ATOM   3704  OH  TYR C   5      17.053  61.669  78.958  1.00 54.85           O  
ANISOU 3704  OH  TYR C   5     5899   7650   7290   -120   -144  -2684       O  
ATOM   3705  N   LYS C   6       9.773  60.797  83.656  1.00 63.89           N  
ANISOU 3705  N   LYS C   6     7046   9826   7405    517    323  -2795       N  
ATOM   3706  CA  LYS C   6       8.418  60.491  84.101  1.00 64.09           C  
ANISOU 3706  CA  LYS C   6     7025  10041   7286    592    448  -2731       C  
ATOM   3707  C   LYS C   6       7.442  60.417  82.936  1.00 64.97           C  
ANISOU 3707  C   LYS C   6     7096  10037   7552    536    521  -2582       C  
ATOM   3708  O   LYS C   6       6.474  59.649  82.987  1.00 64.13           O  
ANISOU 3708  O   LYS C   6     6945  10072   7350    528    626  -2426       O  
ATOM   3709  CB  LYS C   6       7.936  61.546  85.095  1.00 63.41           C  
ANISOU 3709  CB  LYS C   6     6916  10066   7111    757    447  -2980       C  
ATOM   3710  CG  LYS C   6       8.473  61.402  86.505  1.00 64.76           C  
ANISOU 3710  CG  LYS C   6     7112  10458   7035    852    410  -3108       C  
ATOM   3711  CD  LYS C   6       8.295  62.704  87.267  1.00 67.11           C  
ANISOU 3711  CD  LYS C   6     7410  10764   7325   1001    352  -3378       C  
ATOM   3712  CE  LYS C   6       6.867  63.218  87.133  1.00 69.12           C  
ANISOU 3712  CE  LYS C   6     7608  11046   7608   1087    451  -3372       C  
ATOM   3713  NZ  LYS C   6       6.804  64.706  87.090  1.00 71.37           N  
ANISOU 3713  NZ  LYS C   6     7914  11138   8067   1165    356  -3575       N  
ATOM   3714  N   ASP C   7       7.664  61.206  81.892  1.00 60.14           N  
ANISOU 3714  N   ASP C   7     6497   9176   7179    497    466  -2623       N  
ATOM   3715  CA  ASP C   7       6.689  61.345  80.820  1.00 58.22           C  
ANISOU 3715  CA  ASP C   7     6216   8827   7080    476    522  -2519       C  
ATOM   3716  C   ASP C   7       7.409  61.820  79.564  1.00 56.56           C  
ANISOU 3716  C   ASP C   7     6047   8335   7107    391    448  -2494       C  
ATOM   3717  O   ASP C   7       8.642  61.902  79.525  1.00 55.49           O  
ANISOU 3717  O   ASP C   7     5957   8105   7022    332    366  -2534       O  
ATOM   3718  CB  ASP C   7       5.568  62.306  81.234  1.00 57.58           C  
ANISOU 3718  CB  ASP C   7     6080   8810   6989    621    569  -2667       C  
ATOM   3719  CG  ASP C   7       6.096  63.622  81.787  1.00 59.67           C  
ANISOU 3719  CG  ASP C   7     6382   8984   7307    720    481  -2939       C  
ATOM   3720  OD1 ASP C   7       7.249  63.992  81.478  1.00 60.44           O  
ANISOU 3720  OD1 ASP C   7     6537   8899   7528    650    380  -2996       O  
ATOM   3721  OD2 ASP C   7       5.355  64.292  82.537  1.00 61.75           O  
ANISOU 3721  OD2 ASP C   7     6612   9360   7491    869    511  -3100       O  
ATOM   3722  N   LEU C   8       6.626  62.148  78.534  1.00 46.43           N  
ANISOU 3722  N   LEU C   8     4742   6931   5968    390    478  -2424       N  
ATOM   3723  CA  LEU C   8       7.197  62.664  77.297  1.00 44.56           C  
ANISOU 3723  CA  LEU C   8     4545   6436   5949    323    421  -2385       C  
ATOM   3724  C   LEU C   8       7.797  64.053  77.484  1.00 43.81           C  
ANISOU 3724  C   LEU C   8     4485   6175   5986    368    344  -2590       C  
ATOM   3725  O   LEU C   8       8.794  64.381  76.834  1.00 42.72           O  
ANISOU 3725  O   LEU C   8     4386   5852   5993    285    282  -2576       O  
ATOM   3726  CB  LEU C   8       6.128  62.692  76.203  1.00 44.72           C  
ANISOU 3726  CB  LEU C   8     4535   6387   6069    332    469  -2264       C  
ATOM   3727  CG  LEU C   8       6.484  63.410  74.898  1.00 43.15           C  
ANISOU 3727  CG  LEU C   8     4379   5929   6087    298    423  -2224       C  
ATOM   3728  CD1 LEU C   8       7.623  62.696  74.190  1.00 40.25           C  
ANISOU 3728  CD1 LEU C   8     4056   5482   5756    169    389  -2090       C  
ATOM   3729  CD2 LEU C   8       5.267  63.526  73.992  1.00 43.06           C  
ANISOU 3729  CD2 LEU C   8     4332   5885   6145    345    464  -2134       C  
ATOM   3730  N   ARG C   9       7.220  64.874  78.366  1.00 46.56           N  
ANISOU 3730  N   ARG C   9     4817   6587   6288    498    345  -2782       N  
ATOM   3731  CA  ARG C   9       7.633  66.272  78.454  1.00 49.15           C  
ANISOU 3731  CA  ARG C   9     5185   6719   6771    548    262  -2984       C  
ATOM   3732  C   ARG C   9       9.025  66.415  79.062  1.00 50.36           C  
ANISOU 3732  C   ARG C   9     5371   6839   6923    484    167  -3104       C  
ATOM   3733  O   ARG C   9       9.810  67.269  78.629  1.00 50.35           O  
ANISOU 3733  O   ARG C   9     5406   6608   7116    428     88  -3175       O  
ATOM   3734  CB  ARG C   9       6.602  67.067  79.253  1.00 49.62           C  
ANISOU 3734  CB  ARG C   9     5221   6864   6769    725    283  -3172       C  
ATOM   3735  CG  ARG C   9       5.239  67.102  78.582  1.00 51.39           C  
ANISOU 3735  CG  ARG C   9     5397   7104   7026    797    364  -3072       C  
ATOM   3736  CD  ARG C   9       4.189  67.777  79.439  1.00 51.95           C  
ANISOU 3736  CD  ARG C   9     5426   7303   7008    989    396  -3255       C  
ATOM   3737  NE  ARG C   9       2.854  67.607  78.873  1.00 52.79           N  
ANISOU 3737  NE  ARG C   9     5459   7483   7118   1053    482  -3143       N  
ATOM   3738  CZ  ARG C   9       1.812  68.373  79.174  1.00 53.64           C  
ANISOU 3738  CZ  ARG C   9     5522   7641   7217   1230    508  -3275       C  
ATOM   3739  NH1 ARG C   9       1.948  69.370  80.037  1.00 54.45           N  
ANISOU 3739  NH1 ARG C   9     5672   7712   7304   1349    445  -3492       N  
ATOM   3740  NH2 ARG C   9       0.634  68.143  78.608  1.00 53.37           N  
ANISOU 3740  NH2 ARG C   9     5403   7685   7189   1278    582  -3161       N  
ATOM   3741  N   GLU C  10       9.351  65.598  80.066  1.00 56.15           N  
ANISOU 3741  N   GLU C  10     6089   7800   7444    491    172  -3123       N  
ATOM   3742  CA  GLU C  10      10.708  65.611  80.607  1.00 56.92           C  
ANISOU 3742  CA  GLU C  10     6207   7889   7531    430     74  -3224       C  
ATOM   3743  C   GLU C  10      11.724  65.212  79.538  1.00 55.62           C  
ANISOU 3743  C   GLU C  10     6051   7571   7510    272     45  -3061       C  
ATOM   3744  O   GLU C  10      12.782  65.846  79.398  1.00 57.54           O  
ANISOU 3744  O   GLU C  10     6303   7660   7900    201    -45  -3151       O  
ATOM   3745  CB  GLU C  10      10.789  64.683  81.823  1.00 57.63           C  
ANISOU 3745  CB  GLU C  10     6284   8271   7342    481     91  -3240       C  
ATOM   3746  CG  GLU C  10      10.003  65.184  83.041  1.00 59.80           C  
ANISOU 3746  CG  GLU C  10     6548   8721   7453    651    108  -3439       C  
ATOM   3747  CD  GLU C  10      10.305  64.401  84.311  1.00 63.12           C  
ANISOU 3747  CD  GLU C  10     6965   9423   7594    706    108  -3473       C  
ATOM   3748  OE1 GLU C  10      10.737  63.234  84.204  1.00 62.95           O  
ANISOU 3748  OE1 GLU C  10     6947   9491   7481    621    132  -3285       O  
ATOM   3749  OE2 GLU C  10      10.107  64.954  85.416  1.00 66.31           O  
ANISOU 3749  OE2 GLU C  10     7373   9952   7870    838     78  -3665       O  
ATOM   3750  N   PHE C  11      11.402  64.185  78.749  1.00 41.40           N  
ANISOU 3750  N   PHE C  11     4243   5810   5676    214    121  -2823       N  
ATOM   3751  CA  PHE C  11      12.285  63.793  77.656  1.00 40.68           C  
ANISOU 3751  CA  PHE C  11     4160   5587   5709     86    103  -2666       C  
ATOM   3752  C   PHE C  11      12.419  64.907  76.624  1.00 40.24           C  
ANISOU 3752  C   PHE C  11     4120   5263   5907     45     80  -2674       C  
ATOM   3753  O   PHE C  11      13.515  65.155  76.111  1.00 40.22           O  
ANISOU 3753  O   PHE C  11     4116   5128   6038    -54     31  -2654       O  
ATOM   3754  CB  PHE C  11      11.774  62.515  76.996  1.00 38.89           C  
ANISOU 3754  CB  PHE C  11     3932   5447   5397     52    181  -2429       C  
ATOM   3755  CG  PHE C  11      12.712  61.962  75.968  1.00 39.01           C  
ANISOU 3755  CG  PHE C  11     3958   5366   5496    -57    164  -2276       C  
ATOM   3756  CD1 PHE C  11      14.045  61.754  76.280  1.00 38.12           C  
ANISOU 3756  CD1 PHE C  11     3839   5271   5373   -113     96  -2315       C  
ATOM   3757  CD2 PHE C  11      12.272  61.668  74.689  1.00 37.22           C  
ANISOU 3757  CD2 PHE C  11     3744   5045   5354    -91    210  -2102       C  
ATOM   3758  CE1 PHE C  11      14.921  61.253  75.341  1.00 37.22           C  
ANISOU 3758  CE1 PHE C  11     3724   5089   5329   -198     86  -2179       C  
ATOM   3759  CE2 PHE C  11      13.144  61.165  73.743  1.00 38.88           C  
ANISOU 3759  CE2 PHE C  11     3964   5183   5625   -173    197  -1969       C  
ATOM   3760  CZ  PHE C  11      14.471  60.958  74.069  1.00 37.61           C  
ANISOU 3760  CZ  PHE C  11     3791   5047   5452   -225    140  -2006       C  
ATOM   3761  N   LEU C  12      11.316  65.592  76.311  1.00 43.67           N  
ANISOU 3761  N   LEU C  12     4564   5620   6410    123    119  -2694       N  
ATOM   3762  CA  LEU C  12      11.357  66.664  75.322  1.00 42.05           C  
ANISOU 3762  CA  LEU C  12     4387   5151   6440     99     99  -2684       C  
ATOM   3763  C   LEU C  12      12.218  67.824  75.800  1.00 42.66           C  
ANISOU 3763  C   LEU C  12     4480   5070   6659     75      3  -2885       C  
ATOM   3764  O   LEU C  12      12.970  68.416  75.014  1.00 42.60           O  
ANISOU 3764  O   LEU C  12     4486   4850   6849    -22    -30  -2840       O  
ATOM   3765  CB  LEU C  12       9.941  67.152  75.011  1.00 42.22           C  
ANISOU 3765  CB  LEU C  12     4415   5139   6488    215    150  -2681       C  
ATOM   3766  CG  LEU C  12       9.007  66.243  74.211  1.00 42.74           C  
ANISOU 3766  CG  LEU C  12     4459   5296   6485    224    233  -2475       C  
ATOM   3767  CD1 LEU C  12       7.795  67.028  73.728  1.00 43.48           C  
ANISOU 3767  CD1 LEU C  12     4555   5302   6664    335    260  -2488       C  
ATOM   3768  CD2 LEU C  12       9.730  65.596  73.039  1.00 41.44           C  
ANISOU 3768  CD2 LEU C  12     4309   5053   6382    103    240  -2271       C  
ATOM   3769  N   GLU C  13      12.118  68.175  77.084  1.00 52.33           N  
ANISOU 3769  N   GLU C  13     5701   6396   7785    161    -45  -3107       N  
ATOM   3770  CA  GLU C  13      12.938  69.273  77.586  1.00 54.37           C  
ANISOU 3770  CA  GLU C  13     5976   6499   8184    137   -156  -3323       C  
ATOM   3771  C   GLU C  13      14.413  68.885  77.612  1.00 53.79           C  
ANISOU 3771  C   GLU C  13     5867   6430   8140     -7   -218  -3302       C  
ATOM   3772  O   GLU C  13      15.283  69.722  77.334  1.00 54.34           O  
ANISOU 3772  O   GLU C  13     5936   6293   8419   -104   -292  -3367       O  
ATOM   3773  CB  GLU C  13      12.450  69.729  78.966  1.00 58.87           C  
ANISOU 3773  CB  GLU C  13     6554   7193   8623    285   -200  -3585       C  
ATOM   3774  CG  GLU C  13      12.623  68.736  80.096  1.00 63.50           C  
ANISOU 3774  CG  GLU C  13     7107   8085   8935    327   -196  -3630       C  
ATOM   3775  CD  GLU C  13      12.125  69.271  81.426  1.00 69.89           C  
ANISOU 3775  CD  GLU C  13     7926   9026   9602    486   -236  -3854       C  
ATOM   3776  OE1 GLU C  13      11.925  68.462  82.357  1.00 71.49           O  
ANISOU 3776  OE1 GLU C  13     8107   9507   9548    557   -203  -3865       O  
ATOM   3777  OE2 GLU C  13      11.937  70.501  81.541  1.00 72.97           O  
ANISOU 3777  OE2 GLU C  13     8352   9248  10126    539   -298  -3962       O  
ATOM   3778  N   VAL C  14      14.719  67.615  77.901  1.00 52.09           N  
ANISOU 3778  N   VAL C  14     5620   6442   7730    -26   -188  -3202       N  
ATOM   3779  CA  VAL C  14      16.109  67.173  77.785  1.00 52.41           C  
ANISOU 3779  CA  VAL C  14     5619   6495   7801   -152   -240  -3158       C  
ATOM   3780  C   VAL C  14      16.574  67.250  76.334  1.00 50.07           C  
ANISOU 3780  C   VAL C  14     5313   6011   7698   -275   -203  -2958       C  
ATOM   3781  O   VAL C  14      17.705  67.667  76.052  1.00 49.72           O  
ANISOU 3781  O   VAL C  14     5231   5852   7810   -391   -260  -2976       O  
ATOM   3782  CB  VAL C  14      16.285  65.759  78.367  1.00 54.10           C  
ANISOU 3782  CB  VAL C  14     5813   6984   7760   -127   -217  -3080       C  
ATOM   3783  CG1 VAL C  14      17.688  65.237  78.074  1.00 53.81           C  
ANISOU 3783  CG1 VAL C  14     5728   6959   7759   -243   -265  -3010       C  
ATOM   3784  CG2 VAL C  14      16.038  65.782  79.863  1.00 55.49           C  
ANISOU 3784  CG2 VAL C  14     5994   7349   7741    -10   -263  -3285       C  
ATOM   3785  N   LEU C  15      15.709  66.860  75.392  1.00 46.76           N  
ANISOU 3785  N   LEU C  15     4923   5572   7271   -250   -106  -2767       N  
ATOM   3786  CA  LEU C  15      16.065  66.934  73.977  1.00 46.91           C  
ANISOU 3786  CA  LEU C  15     4943   5430   7450   -344    -64  -2572       C  
ATOM   3787  C   LEU C  15      16.369  68.367  73.561  1.00 47.04           C  
ANISOU 3787  C   LEU C  15     4974   5173   7724   -400   -106  -2640       C  
ATOM   3788  O   LEU C  15      17.333  68.618  72.828  1.00 48.29           O  
ANISOU 3788  O   LEU C  15     5103   5209   8035   -523   -112  -2551       O  
ATOM   3789  CB  LEU C  15      14.939  66.361  73.113  1.00 45.28           C  
ANISOU 3789  CB  LEU C  15     4770   5251   7181   -284     30  -2387       C  
ATOM   3790  CG  LEU C  15      14.822  64.840  72.984  1.00 45.45           C  
ANISOU 3790  CG  LEU C  15     4782   5476   7010   -278     79  -2235       C  
ATOM   3791  CD1 LEU C  15      13.739  64.466  71.983  1.00 44.97           C  
ANISOU 3791  CD1 LEU C  15     4751   5399   6938   -235    154  -2067       C  
ATOM   3792  CD2 LEU C  15      16.152  64.225  72.584  1.00 44.36           C  
ANISOU 3792  CD2 LEU C  15     4610   5363   6882   -378     60  -2145       C  
ATOM   3793  N   GLU C  16      15.559  69.321  74.021  1.00 52.95           N  
ANISOU 3793  N   GLU C  16     5767   5823   8527   -310   -132  -2794       N  
ATOM   3794  CA  GLU C  16      15.794  70.713  73.652  1.00 55.35           C  
ANISOU 3794  CA  GLU C  16     6103   5837   9090   -358   -180  -2861       C  
ATOM   3795  C   GLU C  16      17.067  71.253  74.294  1.00 57.10           C  
ANISOU 3795  C   GLU C  16     6280   5990   9427   -470   -288  -3026       C  
ATOM   3796  O   GLU C  16      17.818  71.999  73.654  1.00 59.36           O  
ANISOU 3796  O   GLU C  16     6556   6056   9942   -597   -312  -2981       O  
ATOM   3797  CB  GLU C  16      14.596  71.582  74.030  1.00 56.95           C  
ANISOU 3797  CB  GLU C  16     6370   5950   9316   -211   -193  -3002       C  
ATOM   3798  CG  GLU C  16      14.683  72.984  73.446  1.00 62.05           C  
ANISOU 3798  CG  GLU C  16     7073   6263  10241   -247   -233  -3028       C  
ATOM   3799  CD  GLU C  16      13.353  73.709  73.432  1.00 66.04           C  
ANISOU 3799  CD  GLU C  16     7650   6672  10771    -81   -222  -3094       C  
ATOM   3800  OE1 GLU C  16      12.426  73.279  74.150  1.00 66.42           O  
ANISOU 3800  OE1 GLU C  16     7688   6924  10623     64   -199  -3184       O  
ATOM   3801  OE2 GLU C  16      13.238  74.717  72.701  1.00 67.38           O  
ANISOU 3801  OE2 GLU C  16     7882   6565  11156    -92   -235  -3049       O  
ATOM   3802  N   GLN C  17      17.333  70.888  75.553  1.00 66.42           N  
ANISOU 3802  N   GLN C  17     7428   7359  10451   -427   -355  -3214       N  
ATOM   3803  CA  GLN C  17      18.549  71.376  76.198  1.00 69.19           C  
ANISOU 3803  CA  GLN C  17     7728   7675  10886   -521   -468  -3354       C  
ATOM   3804  C   GLN C  17      19.804  70.806  75.547  1.00 68.11           C  
ANISOU 3804  C   GLN C  17     7504   7558  10817   -685   -459  -3214       C  
ATOM   3805  O   GLN C  17      20.872  71.424  75.621  1.00 70.59           O  
ANISOU 3805  O   GLN C  17     7770   7783  11267   -791   -525  -3230       O  
ATOM   3806  CB  GLN C  17      18.536  71.048  77.690  1.00 71.43           C  
ANISOU 3806  CB  GLN C  17     8001   8196  10942   -411   -537  -3542       C  
ATOM   3807  CG  GLN C  17      19.230  72.092  78.554  1.00 77.87           C  
ANISOU 3807  CG  GLN C  17     8812   8936  11838   -422   -662  -3706       C  
ATOM   3808  CD  GLN C  17      20.727  71.864  78.672  1.00 81.55           C  
ANISOU 3808  CD  GLN C  17     9188   9447  12350   -558   -728  -3693       C  
ATOM   3809  OE1 GLN C  17      21.176  70.760  78.981  1.00 82.04           O  
ANISOU 3809  OE1 GLN C  17     9194   9734  12243   -558   -723  -3670       O  
ATOM   3810  NE2 GLN C  17      21.507  72.913  78.426  1.00 83.32           N  
ANISOU 3810  NE2 GLN C  17     9396   9459  12803   -673   -792  -3704       N  
ATOM   3811  N   GLU C  18      19.702  69.640  74.910  1.00 59.82           N  
ANISOU 3811  N   GLU C  18     6438   6658   9632   -680   -363  -3005       N  
ATOM   3812  CA  GLU C  18      20.832  69.009  74.243  1.00 59.25           C  
ANISOU 3812  CA  GLU C  18     6285   6638   9590   -803   -341  -2845       C  
ATOM   3813  C   GLU C  18      20.885  69.319  72.753  1.00 58.02           C  
ANISOU 3813  C   GLU C  18     6137   6301   9606   -886   -252  -2614       C  
ATOM   3814  O   GLU C  18      21.652  68.681  72.024  1.00 57.93           O  
ANISOU 3814  O   GLU C  18     6066   6356   9590   -961   -204  -2445       O  
ATOM   3815  CB  GLU C  18      20.793  67.495  74.460  1.00 59.82           C  
ANISOU 3815  CB  GLU C  18     6343   6989   9396   -734   -299  -2749       C  
ATOM   3816  CG  GLU C  18      21.003  67.070  75.903  1.00 62.99           C  
ANISOU 3816  CG  GLU C  18     6725   7595   9612   -665   -386  -2945       C  
ATOM   3817  CD  GLU C  18      22.352  67.502  76.448  1.00 66.68           C  
ANISOU 3817  CD  GLU C  18     7098   8055  10181   -765   -504  -3100       C  
ATOM   3818  OE1 GLU C  18      23.328  67.551  75.669  1.00 67.86           O  
ANISOU 3818  OE1 GLU C  18     7170   8137  10478   -895   -496  -2991       O  
ATOM   3819  OE2 GLU C  18      22.435  67.797  77.660  1.00 68.96           O  
ANISOU 3819  OE2 GLU C  18     7387   8420  10395   -707   -602  -3320       O  
ATOM   3820  N   GLY C  19      20.093  70.281  72.285  1.00 47.59           N  
ANISOU 3820  N   GLY C  19     4892   4762   8426   -860   -228  -2601       N  
ATOM   3821  CA  GLY C  19      20.090  70.624  70.878  1.00 47.70           C  
ANISOU 3821  CA  GLY C  19     4927   4606   8590   -923   -144  -2373       C  
ATOM   3822  C   GLY C  19      19.462  69.590  69.976  1.00 48.30           C  
ANISOU 3822  C   GLY C  19     5033   4810   8507   -849    -37  -2150       C  
ATOM   3823  O   GLY C  19      19.761  69.563  68.780  1.00 49.11           O  
ANISOU 3823  O   GLY C  19     5131   4844   8685   -906     35  -1942       O  
ATOM   3824  N   GLN C  20      18.592  68.734  70.512  1.00 46.31           N  
ANISOU 3824  N   GLN C  20     4814   4747   8036   -722    -25  -2187       N  
ATOM   3825  CA  GLN C  20      17.972  67.660  69.747  1.00 45.53           C  
ANISOU 3825  CA  GLN C  20     4742   4775   7784   -656     60  -1996       C  
ATOM   3826  C   GLN C  20      16.468  67.861  69.587  1.00 47.47           C  
ANISOU 3826  C   GLN C  20     5062   4985   7988   -530     95  -1986       C  
ATOM   3827  O   GLN C  20      15.725  66.893  69.409  1.00 46.53           O  
ANISOU 3827  O   GLN C  20     4960   5014   7705   -455    140  -1900       O  
ATOM   3828  CB  GLN C  20      18.261  66.308  70.395  1.00 45.58           C  
ANISOU 3828  CB  GLN C  20     4710   5039   7568   -630     50  -2009       C  
ATOM   3829  CG  GLN C  20      19.707  65.855  70.269  1.00 45.93           C  
ANISOU 3829  CG  GLN C  20     4672   5152   7627   -733     30  -1966       C  
ATOM   3830  CD  GLN C  20      20.173  65.790  68.827  1.00 46.31           C  
ANISOU 3830  CD  GLN C  20     4706   5125   7765   -794    103  -1748       C  
ATOM   3831  OE1 GLN C  20      21.156  66.430  68.450  1.00 46.41           O  
ANISOU 3831  OE1 GLN C  20     4657   5036   7942   -906     99  -1724       O  
ATOM   3832  NE2 GLN C  20      19.467  65.017  68.010  1.00 46.01           N  
ANISOU 3832  NE2 GLN C  20     4719   5143   7617   -722    169  -1590       N  
ATOM   3833  N   LEU C  21      16.006  69.109  69.650  1.00 49.28           N  
ANISOU 3833  N   LEU C  21     5336   5017   8373   -503     69  -2077       N  
ATOM   3834  CA  LEU C  21      14.602  69.416  69.411  1.00 50.30           C  
ANISOU 3834  CA  LEU C  21     5527   5100   8483   -373     99  -2066       C  
ATOM   3835  C   LEU C  21      14.495  70.771  68.729  1.00 50.99           C  
ANISOU 3835  C   LEU C  21     5671   4901   8802   -384     91  -2040       C  
ATOM   3836  O   LEU C  21      15.074  71.754  69.200  1.00 50.32           O  
ANISOU 3836  O   LEU C  21     5590   4651   8878   -444     26  -2176       O  
ATOM   3837  CB  LEU C  21      13.793  69.413  70.715  1.00 51.42           C  
ANISOU 3837  CB  LEU C  21     5670   5365   8501   -259     64  -2275       C  
ATOM   3838  CG  LEU C  21      12.268  69.423  70.550  1.00 50.35           C  
ANISOU 3838  CG  LEU C  21     5568   5265   8296   -112    107  -2256       C  
ATOM   3839  CD1 LEU C  21      11.603  68.547  71.602  1.00 49.58           C  
ANISOU 3839  CD1 LEU C  21     5435   5430   7973    -30    120  -2346       C  
ATOM   3840  CD2 LEU C  21      11.707  70.839  70.608  1.00 51.18           C  
ANISOU 3840  CD2 LEU C  21     5728   5153   8566    -34     70  -2376       C  
ATOM   3841  N   ILE C  22      13.751  70.813  67.626  1.00 56.85           N  
ANISOU 3841  N   ILE C  22     6461   5580   9561   -323    149  -1868       N  
ATOM   3842  CA  ILE C  22      13.465  72.046  66.902  1.00 59.41           C  
ANISOU 3842  CA  ILE C  22     6856   5635  10084   -304    148  -1815       C  
ATOM   3843  C   ILE C  22      12.037  72.465  67.216  1.00 58.43           C  
ANISOU 3843  C   ILE C  22     6779   5496   9925   -129    134  -1915       C  
ATOM   3844  O   ILE C  22      11.117  71.639  67.168  1.00 56.92           O  
ANISOU 3844  O   ILE C  22     6569   5494   9564    -32    171  -1877       O  
ATOM   3845  CB  ILE C  22      13.655  71.862  65.387  1.00 61.55           C  
ANISOU 3845  CB  ILE C  22     7148   5849  10389   -340    220  -1542       C  
ATOM   3846  CG1 ILE C  22      15.127  71.660  65.041  1.00 62.70           C  
ANISOU 3846  CG1 ILE C  22     7237   5988  10597   -510    240  -1445       C  
ATOM   3847  CG2 ILE C  22      13.098  73.055  64.621  1.00 63.33           C  
ANISOU 3847  CG2 ILE C  22     7463   5816  10785   -282    223  -1466       C  
ATOM   3848  CD1 ILE C  22      15.357  71.462  63.563  1.00 63.22           C  
ANISOU 3848  CD1 ILE C  22     7322   6026  10675   -534    320  -1177       C  
ATOM   3849  N   ARG C  23      11.848  73.742  67.535  1.00 61.96           N  
ANISOU 3849  N   ARG C  23     7283   5719  10542    -89     78  -2045       N  
ATOM   3850  CA  ARG C  23      10.520  74.313  67.719  1.00 62.37           C  
ANISOU 3850  CA  ARG C  23     7384   5726  10589     93     63  -2137       C  
ATOM   3851  C   ARG C  23      10.113  75.044  66.447  1.00 62.49           C  
ANISOU 3851  C   ARG C  23     7478   5520  10745    139     86  -1956       C  
ATOM   3852  O   ARG C  23      10.791  75.987  66.025  1.00 63.55           O  
ANISOU 3852  O   ARG C  23     7670   5389  11087     54     63  -1908       O  
ATOM   3853  CB  ARG C  23      10.483  75.268  68.910  1.00 63.01           C  
ANISOU 3853  CB  ARG C  23     7489   5698  10753    145    -24  -2416       C  
ATOM   3854  CG  ARG C  23      10.912  74.664  70.231  1.00 63.07           C  
ANISOU 3854  CG  ARG C  23     7427   5920  10616    116    -57  -2609       C  
ATOM   3855  CD  ARG C  23      10.582  75.606  71.376  1.00 65.26           C  
ANISOU 3855  CD  ARG C  23     7739   6118  10941    223   -143  -2900       C  
ATOM   3856  NE  ARG C  23       9.199  75.470  71.819  1.00 67.77           N  
ANISOU 3856  NE  ARG C  23     8049   6594  11108    427   -116  -2987       N  
ATOM   3857  CZ  ARG C  23       8.810  74.673  72.808  1.00 68.14           C  
ANISOU 3857  CZ  ARG C  23     8028   6935  10927    495    -94  -3097       C  
ATOM   3858  NH1 ARG C  23       9.705  73.940  73.457  1.00 67.82           N  
ANISOU 3858  NH1 ARG C  23     7937   7052  10781    385   -107  -3135       N  
ATOM   3859  NH2 ARG C  23       7.531  74.609  73.149  1.00 67.97           N  
ANISOU 3859  NH2 ARG C  23     7986   7057  10782    676    -59  -3162       N  
ATOM   3860  N   VAL C  24       9.012  74.609  65.840  1.00 48.87           N  
ANISOU 3860  N   VAL C  24     5755   3905   8909    269    129  -1851       N  
ATOM   3861  CA  VAL C  24       8.406  75.325  64.722  1.00 48.91           C  
ANISOU 3861  CA  VAL C  24     5840   3724   9019    360    140  -1702       C  
ATOM   3862  C   VAL C  24       7.332  76.226  65.321  1.00 52.46           C  
ANISOU 3862  C   VAL C  24     6330   4084   9519    544     87  -1885       C  
ATOM   3863  O   VAL C  24       6.201  75.799  65.556  1.00 52.97           O  
ANISOU 3863  O   VAL C  24     6349   4334   9444    691     99  -1939       O  
ATOM   3864  CB  VAL C  24       7.837  74.371  63.670  1.00 48.17           C  
ANISOU 3864  CB  VAL C  24     5721   3801   8779    407    201  -1493       C  
ATOM   3865  CG1 VAL C  24       7.348  75.151  62.460  1.00 49.57           C  
ANISOU 3865  CG1 VAL C  24     5988   3783   9062    500    205  -1325       C  
ATOM   3866  CG2 VAL C  24       8.891  73.355  63.258  1.00 47.61           C  
ANISOU 3866  CG2 VAL C  24     5604   3857   8630    246    248  -1354       C  
ATOM   3867  N   LYS C  25       7.697  77.484  65.579  1.00 71.03           N  
ANISOU 3867  N   LYS C  25     8763   6147  12078    536     25  -1985       N  
ATOM   3868  CA  LYS C  25       6.808  78.402  66.283  1.00 72.63           C  
ANISOU 3868  CA  LYS C  25     9011   6248  12337    717    -39  -2198       C  
ATOM   3869  C   LYS C  25       5.589  78.790  65.459  1.00 73.45           C  
ANISOU 3869  C   LYS C  25     9164   6297  12448    913    -30  -2098       C  
ATOM   3870  O   LYS C  25       4.604  79.275  66.025  1.00 74.30           O  
ANISOU 3870  O   LYS C  25     9277   6412  12540   1104    -68  -2269       O  
ATOM   3871  CB  LYS C  25       7.572  79.667  66.682  1.00 74.45           C  
ANISOU 3871  CB  LYS C  25     9331   6177  12779    643   -121  -2305       C  
ATOM   3872  CG  LYS C  25       8.360  79.550  67.977  1.00 75.72           C  
ANISOU 3872  CG  LYS C  25     9440   6443  12888    538   -172  -2514       C  
ATOM   3873  CD  LYS C  25       9.492  80.565  68.018  1.00 79.07           C  
ANISOU 3873  CD  LYS C  25     9932   6614  13498    375   -238  -2503       C  
ATOM   3874  CE  LYS C  25      10.850  79.886  67.951  1.00 79.44           C  
ANISOU 3874  CE  LYS C  25     9899   6712  13574    143   -213  -2435       C  
ATOM   3875  NZ  LYS C  25      11.255  79.332  69.274  1.00 79.60           N  
ANISOU 3875  NZ  LYS C  25     9833   6956  13454    112   -256  -2657       N  
ATOM   3876  N   GLU C  26       5.629  78.587  64.149  1.00 60.29           N  
ANISOU 3876  N   GLU C  26     7527   4587  10793    883     17  -1831       N  
ATOM   3877  CA  GLU C  26       4.616  79.114  63.249  1.00 60.17           C  
ANISOU 3877  CA  GLU C  26     7576   4473  10812   1065     11  -1718       C  
ATOM   3878  C   GLU C  26       3.537  78.080  62.952  1.00 57.64           C  
ANISOU 3878  C   GLU C  26     7158   4466  10275   1182     51  -1663       C  
ATOM   3879  O   GLU C  26       3.748  76.869  63.053  1.00 55.91           O  
ANISOU 3879  O   GLU C  26     6843   4505   9895   1084     99  -1625       O  
ATOM   3880  CB  GLU C  26       5.257  79.583  61.941  1.00 62.42           C  
ANISOU 3880  CB  GLU C  26     7960   4522  11233    980     33  -1449       C  
ATOM   3881  N   GLU C  27       2.364  78.589  62.581  1.00 65.36           N  
ANISOU 3881  N   GLU C  27     8161   5409  11262   1396     24  -1663       N  
ATOM   3882  CA  GLU C  27       1.276  77.735  62.129  1.00 65.63           C  
ANISOU 3882  CA  GLU C  27     8101   5711  11122   1512     50  -1595       C  
ATOM   3883  C   GLU C  27       1.655  77.044  60.826  1.00 65.53           C  
ANISOU 3883  C   GLU C  27     8102   5744  11053   1420     91  -1325       C  
ATOM   3884  O   GLU C  27       2.044  77.694  59.852  1.00 68.68           O  
ANISOU 3884  O   GLU C  27     8612   5918  11564   1415     87  -1151       O  
ATOM   3885  CB  GLU C  27       0.006  78.567  61.942  1.00 67.18           C  
ANISOU 3885  CB  GLU C  27     8325   5838  11363   1771      1  -1650       C  
ATOM   3886  CG  GLU C  27      -1.133  77.846  61.231  1.00 68.93           C  
ANISOU 3886  CG  GLU C  27     8455   6298  11438   1898     13  -1550       C  
ATOM   3887  CD  GLU C  27      -2.281  78.780  60.885  1.00 73.47           C  
ANISOU 3887  CD  GLU C  27     9066   6774  12076   2161    -44  -1579       C  
ATOM   3888  OE1 GLU C  27      -2.373  79.203  59.712  1.00 75.23           O  
ANISOU 3888  OE1 GLU C  27     9382   6845  12356   2229    -67  -1389       O  
ATOM   3889  OE2 GLU C  27      -3.083  79.099  61.788  1.00 74.67           O  
ANISOU 3889  OE2 GLU C  27     9153   7005  12211   2313    -66  -1789       O  
ATOM   3890  N   VAL C  28       1.553  75.720  60.816  1.00 56.33           N  
ANISOU 3890  N   VAL C  28     6827   4865   9710   1350    130  -1289       N  
ATOM   3891  CA  VAL C  28       1.774  74.925  59.618  1.00 57.46           C  
ANISOU 3891  CA  VAL C  28     6971   5093   9767   1291    160  -1063       C  
ATOM   3892  C   VAL C  28       0.440  74.303  59.210  1.00 58.06           C  
ANISOU 3892  C   VAL C  28     6961   5389   9710   1440    143  -1046       C  
ATOM   3893  O   VAL C  28      -0.523  74.289  59.976  1.00 58.75           O  
ANISOU 3893  O   VAL C  28     6962   5604   9757   1549    126  -1207       O  
ATOM   3894  CB  VAL C  28       2.854  73.844  59.829  1.00 55.37           C  
ANISOU 3894  CB  VAL C  28     6659   4962   9416   1080    208  -1026       C  
ATOM   3895  CG1 VAL C  28       4.163  74.475  60.291  1.00 55.42           C  
ANISOU 3895  CG1 VAL C  28     6726   4769   9562    931    217  -1059       C  
ATOM   3896  CG2 VAL C  28       2.376  72.805  60.832  1.00 54.22           C  
ANISOU 3896  CG2 VAL C  28     6385   5094   9122   1061    217  -1174       C  
ATOM   3897  N   ASN C  29       0.380  73.797  57.974  1.00 71.20           N  
ANISOU 3897  N   ASN C  29     8643   7104  11305   1448    145   -852       N  
ATOM   3898  CA  ASN C  29      -0.819  73.058  57.612  1.00 70.45           C  
ANISOU 3898  CA  ASN C  29     8448   7237  11081   1560    117   -847       C  
ATOM   3899  C   ASN C  29      -0.643  71.590  58.009  1.00 67.87           C  
ANISOU 3899  C   ASN C  29     8013   7165  10611   1416    146   -874       C  
ATOM   3900  O   ASN C  29       0.474  71.074  57.986  1.00 68.93           O  
ANISOU 3900  O   ASN C  29     8178   7289  10724   1253    183   -814       O  
ATOM   3901  CB  ASN C  29      -1.092  73.195  56.113  1.00 72.38           C  
ANISOU 3901  CB  ASN C  29     8763   7433  11306   1663     87   -647       C  
ATOM   3902  CG  ASN C  29      -2.399  72.559  55.691  1.00 74.22           C  
ANISOU 3902  CG  ASN C  29     8889   7887  11424   1795     37   -656       C  
ATOM   3903  OD1 ASN C  29      -2.492  71.345  55.564  1.00 74.71           O  
ANISOU 3903  OD1 ASN C  29     8866   8158  11363   1713     38   -641       O  
ATOM   3904  ND2 ASN C  29      -3.432  73.379  55.514  1.00 75.67           N  
ANISOU 3904  ND2 ASN C  29     9071   8024  11657   2002    -15   -690       N  
ATOM   3905  N   PRO C  30      -1.718  70.912  58.436  1.00 50.29           N  
ANISOU 3905  N   PRO C  30     5653   5164   8291   1472    131   -967       N  
ATOM   3906  CA  PRO C  30      -1.602  69.466  58.719  1.00 48.78           C  
ANISOU 3906  CA  PRO C  30     5368   5197   7969   1332    153   -968       C  
ATOM   3907  C   PRO C  30      -0.910  68.664  57.628  1.00 49.35           C  
ANISOU 3907  C   PRO C  30     5495   5281   7976   1241    149   -798       C  
ATOM   3908  O   PRO C  30      -0.088  67.795  57.944  1.00 47.62           O  
ANISOU 3908  O   PRO C  30     5269   5127   7698   1087    180   -789       O  
ATOM   3909  CB  PRO C  30      -3.061  69.023  58.904  1.00 48.44           C  
ANISOU 3909  CB  PRO C  30     5180   5366   7860   1436    125  -1040       C  
ATOM   3910  CG  PRO C  30      -3.915  70.210  58.505  1.00 49.85           C  
ANISOU 3910  CG  PRO C  30     5380   5440   8122   1648     82  -1058       C  
ATOM   3911  CD  PRO C  30      -3.063  71.414  58.758  1.00 50.44           C  
ANISOU 3911  CD  PRO C  30     5592   5250   8324   1657     98  -1078       C  
ATOM   3912  N   GLU C  31      -1.238  68.905  56.359  1.00 54.90           N  
ANISOU 3912  N   GLU C  31     6251   5934   8675   1348    108   -668       N  
ATOM   3913  CA  GLU C  31      -0.576  68.231  55.254  1.00 55.93           C  
ANISOU 3913  CA  GLU C  31     6443   6078   8731   1290    104   -509       C  
ATOM   3914  C   GLU C  31      -0.156  69.249  54.203  1.00 57.28           C  
ANISOU 3914  C   GLU C  31     6747   6050   8966   1375    105   -359       C  
ATOM   3915  O   GLU C  31      -0.887  70.207  53.934  1.00 59.38           O  
ANISOU 3915  O   GLU C  31     7041   6222   9298   1532     71   -354       O  
ATOM   3916  CB  GLU C  31      -1.479  67.171  54.601  1.00 55.57           C  
ANISOU 3916  CB  GLU C  31     6317   6232   8566   1334     41   -486       C  
ATOM   3917  CG  GLU C  31      -2.130  66.209  55.569  1.00 54.93           C  
ANISOU 3917  CG  GLU C  31     6093   6346   8432   1261     37   -616       C  
ATOM   3918  CD  GLU C  31      -3.514  66.658  55.982  1.00 55.38           C  
ANISOU 3918  CD  GLU C  31     6039   6483   8521   1394      6   -719       C  
ATOM   3919  OE1 GLU C  31      -4.003  67.664  55.423  1.00 56.14           O  
ANISOU 3919  OE1 GLU C  31     6175   6482   8674   1558    -27   -691       O  
ATOM   3920  OE2 GLU C  31      -4.113  66.006  56.861  1.00 54.37           O  
ANISOU 3920  OE2 GLU C  31     5780   6519   8360   1339     17   -822       O  
ATOM   3921  N   PRO C  32       1.007  69.058  53.573  1.00 55.41           N  
ANISOU 3921  N   PRO C  32     6593   5752   8709   1281    145   -224       N  
ATOM   3922  CA  PRO C  32       1.931  67.956  53.841  1.00 52.54           C  
ANISOU 3922  CA  PRO C  32     6202   5493   8268   1115    181   -227       C  
ATOM   3923  C   PRO C  32       3.031  68.347  54.824  1.00 53.03           C  
ANISOU 3923  C   PRO C  32     6278   5445   8424    972    242   -287       C  
ATOM   3924  O   PRO C  32       4.040  67.650  54.907  1.00 53.65           O  
ANISOU 3924  O   PRO C  32     6356   5572   8456    842    278   -259       O  
ATOM   3925  CB  PRO C  32       2.509  67.667  52.459  1.00 49.69           C  
ANISOU 3925  CB  PRO C  32     5921   5133   7826   1134    187    -41       C  
ATOM   3926  CG  PRO C  32       2.564  69.026  51.816  1.00 52.77           C  
ANISOU 3926  CG  PRO C  32     6413   5322   8316   1234    203     78       C  
ATOM   3927  CD  PRO C  32       1.409  69.828  52.382  1.00 55.13           C  
ANISOU 3927  CD  PRO C  32     6680   5565   8702   1356    156    -38       C  
ATOM   3928  N   ASP C  33       2.815  69.431  55.574  1.00 45.28           N  
ANISOU 3928  N   ASP C  33     5307   4324   7572   1007    245   -383       N  
ATOM   3929  CA  ASP C  33       3.904  70.059  56.319  1.00 46.91           C  
ANISOU 3929  CA  ASP C  33     5548   4381   7896    886    287   -430       C  
ATOM   3930  C   ASP C  33       4.475  69.132  57.385  1.00 45.35           C  
ANISOU 3930  C   ASP C  33     5273   4322   7636    743    307   -548       C  
ATOM   3931  O   ASP C  33       5.694  68.955  57.476  1.00 42.48           O  
ANISOU 3931  O   ASP C  33     4926   3926   7289    610    344   -510       O  
ATOM   3932  CB  ASP C  33       3.424  71.365  56.954  1.00 48.21           C  
ANISOU 3932  CB  ASP C  33     5741   4370   8206    972    266   -540       C  
ATOM   3933  CG  ASP C  33       3.175  72.455  55.932  1.00 50.24           C  
ANISOU 3933  CG  ASP C  33     6104   4428   8557   1094    252   -401       C  
ATOM   3934  OD1 ASP C  33       3.596  72.288  54.766  1.00 50.34           O  
ANISOU 3934  OD1 ASP C  33     6174   4427   8528   1089    274   -206       O  
ATOM   3935  OD2 ASP C  33       2.559  73.479  56.296  1.00 51.79           O  
ANISOU 3935  OD2 ASP C  33     6332   4485   8863   1207    219   -485       O  
ATOM   3936  N   ILE C  34       3.613  68.549  58.219  1.00 46.74           N  
ANISOU 3936  N   ILE C  34     5360   4660   7740    770    285   -685       N  
ATOM   3937  CA  ILE C  34       4.103  67.770  59.354  1.00 46.35           C  
ANISOU 3937  CA  ILE C  34     5247   4733   7631    647    304   -798       C  
ATOM   3938  C   ILE C  34       4.846  66.527  58.874  1.00 45.89           C  
ANISOU 3938  C   ILE C  34     5184   4789   7463    544    317   -698       C  
ATOM   3939  O   ILE C  34       5.931  66.195  59.375  1.00 45.91           O  
ANISOU 3939  O   ILE C  34     5186   4799   7458    424    342   -717       O  
ATOM   3940  CB  ILE C  34       2.934  67.422  60.294  1.00 44.44           C  
ANISOU 3940  CB  ILE C  34     4908   4651   7328    707    288   -942       C  
ATOM   3941  CG1 ILE C  34       2.303  68.706  60.840  1.00 44.65           C  
ANISOU 3941  CG1 ILE C  34     4940   4562   7461    825    276  -1062       C  
ATOM   3942  CG2 ILE C  34       3.411  66.549  61.438  1.00 43.83           C  
ANISOU 3942  CG2 ILE C  34     4773   4712   7168    588    311  -1036       C  
ATOM   3943  CD1 ILE C  34       0.980  68.497  61.550  1.00 45.88           C  
ANISOU 3943  CD1 ILE C  34     4990   4888   7555    924    268  -1184       C  
ATOM   3944  N   ALA C  35       4.291  65.837  57.877  1.00 41.00           N  
ANISOU 3944  N   ALA C  35     4563   4258   6755    601    292   -598       N  
ATOM   3945  CA  ALA C  35       4.960  64.666  57.321  1.00 38.50           C  
ANISOU 3945  CA  ALA C  35     4256   4040   6332    527    295   -509       C  
ATOM   3946  C   ALA C  35       6.246  65.047  56.599  1.00 39.37           C  
ANISOU 3946  C   ALA C  35     4440   4038   6481    479    336   -386       C  
ATOM   3947  O   ALA C  35       7.253  64.334  56.695  1.00 37.93           O  
ANISOU 3947  O   ALA C  35     4254   3910   6247    382    358   -365       O  
ATOM   3948  CB  ALA C  35       4.018  63.935  56.372  1.00 37.38           C  
ANISOU 3948  CB  ALA C  35     4101   4005   6096    611    243   -447       C  
ATOM   3949  N   ALA C  36       6.225  66.155  55.852  1.00 43.58           N  
ANISOU 3949  N   ALA C  36     5036   4418   7103    549    348   -295       N  
ATOM   3950  CA  ALA C  36       7.437  66.609  55.181  1.00 44.44           C  
ANISOU 3950  CA  ALA C  36     5205   4419   7261    493    401   -160       C  
ATOM   3951  C   ALA C  36       8.526  66.951  56.184  1.00 46.59           C  
ANISOU 3951  C   ALA C  36     5453   4620   7629    353    437   -238       C  
ATOM   3952  O   ALA C  36       9.708  66.708  55.925  1.00 46.95           O  
ANISOU 3952  O   ALA C  36     5499   4673   7669    261    480   -163       O  
ATOM   3953  CB  ALA C  36       7.135  67.814  54.292  1.00 45.11           C  
ANISOU 3953  CB  ALA C  36     5368   4336   7436    593    410    -39       C  
ATOM   3954  N   ALA C  37       8.149  67.494  57.343  1.00 46.68           N  
ANISOU 3954  N   ALA C  37     5436   4579   7722    344    415   -399       N  
ATOM   3955  CA  ALA C  37       9.137  67.800  58.368  1.00 45.20           C  
ANISOU 3955  CA  ALA C  37     5221   4336   7618    218    430   -500       C  
ATOM   3956  C   ALA C  37       9.683  66.529  59.000  1.00 44.44           C  
ANISOU 3956  C   ALA C  37     5063   4425   7398    132    430   -560       C  
ATOM   3957  O   ALA C  37      10.881  66.442  59.287  1.00 45.01           O  
ANISOU 3957  O   ALA C  37     5115   4491   7497     21    451   -561       O  
ATOM   3958  CB  ALA C  37       8.532  68.713  59.429  1.00 44.04           C  
ANISOU 3958  CB  ALA C  37     5069   4093   7573    255    398   -672       C  
ATOM   3959  N   GLY C  38       8.824  65.533  59.230  1.00 41.75           N  
ANISOU 3959  N   GLY C  38     4687   4248   6926    180    402   -607       N  
ATOM   3960  CA  GLY C  38       9.329  64.243  59.680  1.00 41.44           C  
ANISOU 3960  CA  GLY C  38     4608   4372   6765    108    399   -633       C  
ATOM   3961  C   GLY C  38      10.340  63.655  58.712  1.00 43.52           C  
ANISOU 3961  C   GLY C  38     4895   4663   6978     69    423   -494       C  
ATOM   3962  O   GLY C  38      11.429  63.219  59.108  1.00 46.02           O  
ANISOU 3962  O   GLY C  38     5187   5026   7274    -19    437   -509       O  
ATOM   3963  N   ARG C  39      10.002  63.666  57.419  1.00 38.67           N  
ANISOU 3963  N   ARG C  39     4326   4031   6335    147    428   -360       N  
ATOM   3964  CA  ARG C  39      10.895  63.117  56.402  1.00 38.36           C  
ANISOU 3964  CA  ARG C  39     4312   4037   6227    137    456   -225       C  
ATOM   3965  C   ARG C  39      12.198  63.905  56.313  1.00 42.03           C  
ANISOU 3965  C   ARG C  39     4772   4401   6797     52    516   -163       C  
ATOM   3966  O   ARG C  39      13.274  63.314  56.183  1.00 42.01           O  
ANISOU 3966  O   ARG C  39     4743   4473   6744     -6    544   -124       O  
ATOM   3967  CB  ARG C  39      10.189  63.093  55.045  1.00 37.94           C  
ANISOU 3967  CB  ARG C  39     4313   3989   6115    258    444   -101       C  
ATOM   3968  CG  ARG C  39      11.068  62.644  53.881  1.00 39.52           C  
ANISOU 3968  CG  ARG C  39     4546   4242   6230    276    480     44       C  
ATOM   3969  CD  ARG C  39      11.294  61.135  53.873  1.00 38.24           C  
ANISOU 3969  CD  ARG C  39     4371   4240   5920    273    443     10       C  
ATOM   3970  NE  ARG C  39      12.521  60.749  54.563  1.00 38.42           N  
ANISOU 3970  NE  ARG C  39     4350   4302   5946    169    474    -28       N  
ATOM   3971  CZ  ARG C  39      12.924  59.492  54.731  1.00 37.96           C  
ANISOU 3971  CZ  ARG C  39     4283   4365   5777    158    445    -65       C  
ATOM   3972  NH1 ARG C  39      12.198  58.486  54.257  1.00 35.55           N  
ANISOU 3972  NH1 ARG C  39     4012   4139   5356    232    382    -71       N  
ATOM   3973  NH2 ARG C  39      14.056  59.242  55.373  1.00 35.24           N  
ANISOU 3973  NH2 ARG C  39     3894   4056   5441     76    470    -99       N  
ATOM   3974  N   ALA C  40      12.126  65.237  56.379  1.00 44.87           N  
ANISOU 3974  N   ALA C  40     5151   4588   7308     43    536   -154       N  
ATOM   3975  CA  ALA C  40      13.331  66.058  56.304  1.00 45.77           C  
ANISOU 3975  CA  ALA C  40     5253   4587   7551    -59    590    -91       C  
ATOM   3976  C   ALA C  40      14.226  65.836  57.517  1.00 45.62           C  
ANISOU 3976  C   ALA C  40     5160   4606   7567   -182    578   -228       C  
ATOM   3977  O   ALA C  40      15.451  65.686  57.384  1.00 45.19           O  
ANISOU 3977  O   ALA C  40     5060   4583   7528   -271    617   -175       O  
ATOM   3978  CB  ALA C  40      12.947  67.532  56.179  1.00 47.32           C  
ANISOU 3978  CB  ALA C  40     5499   4561   7918    -42    597    -63       C  
ATOM   3979  N   ALA C  41      13.632  65.835  58.715  1.00 44.22           N  
ANISOU 3979  N   ALA C  41     4964   4440   7397   -181    525   -406       N  
ATOM   3980  CA  ALA C  41      14.378  65.526  59.926  1.00 42.89           C  
ANISOU 3980  CA  ALA C  41     4732   4335   7230   -275    501   -548       C  
ATOM   3981  C   ALA C  41      15.098  64.194  59.789  1.00 43.03           C  
ANISOU 3981  C   ALA C  41     4714   4535   7102   -298    508   -509       C  
ATOM   3982  O   ALA C  41      16.284  64.083  60.115  1.00 40.28           O  
ANISOU 3982  O   ALA C  41     4308   4219   6777   -387    517   -525       O  
ATOM   3983  CB  ALA C  41      13.436  65.515  61.132  1.00 41.34           C  
ANISOU 3983  CB  ALA C  41     4528   4171   7008   -235    449   -729       C  
ATOM   3984  N   ALA C  42      14.401  63.173  59.281  1.00 38.79           N  
ANISOU 3984  N   ALA C  42     4207   4114   6419   -213    496   -460       N  
ATOM   3985  CA  ALA C  42      15.069  61.901  59.020  1.00 37.83           C  
ANISOU 3985  CA  ALA C  42     4068   4142   6162   -217    496   -416       C  
ATOM   3986  C   ALA C  42      16.206  62.065  58.012  1.00 41.50           C  
ANISOU 3986  C   ALA C  42     4519   4600   6649   -243    555   -275       C  
ATOM   3987  O   ALA C  42      17.296  61.509  58.197  1.00 41.62           O  
ANISOU 3987  O   ALA C  42     4482   4705   6626   -291    565   -279       O  
ATOM   3988  CB  ALA C  42      14.057  60.867  58.527  1.00 35.79           C  
ANISOU 3988  CB  ALA C  42     3856   3978   5766   -123    462   -387       C  
ATOM   3989  N   ASN C  43      15.976  62.841  56.950  1.00 41.79           N  
ANISOU 3989  N   ASN C  43     4597   4539   6744   -204    600   -145       N  
ATOM   3990  CA  ASN C  43      16.949  63.015  55.877  1.00 41.70           C  
ANISOU 3990  CA  ASN C  43     4572   4534   6737   -217    673     16       C  
ATOM   3991  C   ASN C  43      18.184  63.793  56.301  1.00 42.19           C  
ANISOU 3991  C   ASN C  43     4555   4529   6946   -353    716     16       C  
ATOM   3992  O   ASN C  43      19.163  63.815  55.548  1.00 41.99           O  
ANISOU 3992  O   ASN C  43     4489   4546   6920   -382    785    146       O  
ATOM   3993  CB  ASN C  43      16.300  63.721  54.686  1.00 43.91           C  
ANISOU 3993  CB  ASN C  43     4925   4722   7037   -135    709    165       C  
ATOM   3994  CG  ASN C  43      15.366  62.819  53.916  1.00 45.42           C  
ANISOU 3994  CG  ASN C  43     5179   5015   7061      4    671    198       C  
ATOM   3995  OD1 ASN C  43      15.207  61.644  54.247  1.00 42.91           O  
ANISOU 3995  OD1 ASN C  43     4855   4824   6624     29    619    116       O  
ATOM   3996  ND2 ASN C  43      14.738  63.364  52.880  1.00 46.95           N  
ANISOU 3996  ND2 ASN C  43     5439   5149   7251     96    689    320       N  
ATOM   3997  N   LEU C  44      18.162  64.444  57.465  1.00 52.89           N  
ANISOU 3997  N   LEU C  44     5880   5789   8426   -434    675   -127       N  
ATOM   3998  CA  LEU C  44      19.382  65.090  57.941  1.00 52.80           C  
ANISOU 3998  CA  LEU C  44     5781   5724   8558   -575    696   -152       C  
ATOM   3999  C   LEU C  44      20.500  64.099  58.262  1.00 51.13           C  
ANISOU 3999  C   LEU C  44     5478   5694   8254   -614    693   -185       C  
ATOM   4000  O   LEU C  44      21.627  64.532  58.522  1.00 51.76           O  
ANISOU 4000  O   LEU C  44     5462   5760   8443   -730    713   -190       O  
ATOM   4001  CB  LEU C  44      19.083  65.959  59.163  1.00 52.61           C  
ANISOU 4001  CB  LEU C  44     5752   5563   8675   -638    634   -328       C  
ATOM   4002  CG  LEU C  44      18.169  67.153  58.880  1.00 53.51           C  
ANISOU 4002  CG  LEU C  44     5948   5465   8918   -606    635   -300       C  
ATOM   4003  CD1 LEU C  44      17.907  67.954  60.147  1.00 51.97           C  
ANISOU 4003  CD1 LEU C  44     5749   5146   8850   -650    565   -501       C  
ATOM   4004  CD2 LEU C  44      18.761  68.038  57.789  1.00 54.67           C  
ANISOU 4004  CD2 LEU C  44     6100   5477   9195   -662    715   -102       C  
ATOM   4005  N   GLY C  45      20.224  62.800  58.252  1.00 62.79           N  
ANISOU 4005  N   GLY C  45     6980   7333   9545   -522    664   -208       N  
ATOM   4006  CA  GLY C  45      21.275  61.779  58.352  1.00 63.59           C  
ANISOU 4006  CA  GLY C  45     7010   7608   9542   -526    663   -215       C  
ATOM   4007  C   GLY C  45      21.901  61.502  59.701  1.00 64.46           C  
ANISOU 4007  C   GLY C  45     7046   7782   9663   -594    599   -379       C  
ATOM   4008  O   GLY C  45      21.908  60.354  60.156  1.00 66.64           O  
ANISOU 4008  O   GLY C  45     7332   8192   9796   -536    551   -442       O  
ATOM   4009  N   LYS C  46      22.451  62.527  60.347  1.00 57.32           N  
ANISOU 4009  N   LYS C  46     6072   6781   8927   -713    591   -449       N  
ATOM   4010  CA  LYS C  46      23.063  62.388  61.660  1.00 55.20           C  
ANISOU 4010  CA  LYS C  46     5729   6572   8671   -775    519   -619       C  
ATOM   4011  C   LYS C  46      22.589  63.527  62.549  1.00 54.29           C  
ANISOU 4011  C   LYS C  46     5627   6296   8703   -840    472   -754       C  
ATOM   4012  O   LYS C  46      22.279  64.620  62.067  1.00 55.41           O  
ANISOU 4012  O   LYS C  46     5798   6261   8993   -880    507   -697       O  
ATOM   4013  CB  LYS C  46      24.600  62.390  61.589  1.00 56.07           C  
ANISOU 4013  CB  LYS C  46     5699   6767   8837   -862    540   -594       C  
ATOM   4014  CG  LYS C  46      25.199  61.310  60.702  1.00 57.14           C  
ANISOU 4014  CG  LYS C  46     5809   7074   8828   -783    590   -470       C  
ATOM   4015  CD  LYS C  46      25.494  61.839  59.308  1.00 59.31           C  
ANISOU 4015  CD  LYS C  46     6066   7306   9164   -799    701   -271       C  
ATOM   4016  CE  LYS C  46      25.347  60.746  58.264  1.00 60.61           C  
ANISOU 4016  CE  LYS C  46     6287   7605   9137   -654    742   -154       C  
ATOM   4017  NZ  LYS C  46      24.853  61.286  56.967  1.00 62.72           N  
ANISOU 4017  NZ  LYS C  46     6618   7790   9420   -618    829     22       N  
ATOM   4018  N   ASN C  47      22.535  63.257  63.854  1.00 47.87           N  
ANISOU 4018  N   ASN C  47     4801   5545   7841   -839    390   -934       N  
ATOM   4019  CA  ASN C  47      22.092  64.232  64.853  1.00 48.80           C  
ANISOU 4019  CA  ASN C  47     4933   5539   8068   -877    331  -1099       C  
ATOM   4020  C   ASN C  47      20.679  64.732  64.569  1.00 47.15           C  
ANISOU 4020  C   ASN C  47     4834   5204   7878   -804    350  -1080       C  
ATOM   4021  O   ASN C  47      20.330  65.861  64.923  1.00 47.25           O  
ANISOU 4021  O   ASN C  47     4868   5052   8033   -834    326  -1165       O  
ATOM   4022  CB  ASN C  47      23.059  65.417  64.946  1.00 52.39           C  
ANISOU 4022  CB  ASN C  47     5302   5860   8745  -1020    321  -1136       C  
ATOM   4023  CG  ASN C  47      24.482  64.988  65.224  1.00 53.78           C  
ANISOU 4023  CG  ASN C  47     5343   6172   8918  -1097    299  -1161       C  
ATOM   4024  OD1 ASN C  47      24.836  64.670  66.359  1.00 54.30           O  
ANISOU 4024  OD1 ASN C  47     5365   6340   8927  -1099    215  -1326       O  
ATOM   4025  ND2 ASN C  47      25.311  64.978  64.185  1.00 53.98           N  
ANISOU 4025  ND2 ASN C  47     5297   6214   8997  -1152    376   -993       N  
ATOM   4026  N   GLN C  48      19.862  63.898  63.933  1.00 41.04           N  
ANISOU 4026  N   GLN C  48     4127   4503   6963   -702    383   -978       N  
ATOM   4027  CA  GLN C  48      18.526  64.317  63.539  1.00 42.65           C  
ANISOU 4027  CA  GLN C  48     4419   4607   7179   -624    400   -947       C  
ATOM   4028  C   GLN C  48      17.709  64.686  64.772  1.00 43.26           C  
ANISOU 4028  C   GLN C  48     4518   4666   7255   -591    343  -1133       C  
ATOM   4029  O   GLN C  48      17.666  63.911  65.738  1.00 41.76           O  
ANISOU 4029  O   GLN C  48     4311   4620   6935   -570    303  -1236       O  
ATOM   4030  CB  GLN C  48      17.825  63.211  62.754  1.00 40.74           C  
ANISOU 4030  CB  GLN C  48     4230   4474   6774   -526    426   -829       C  
ATOM   4031  CG  GLN C  48      18.618  62.711  61.559  1.00 41.85           C  
ANISOU 4031  CG  GLN C  48     4355   4667   6879   -529    479   -661       C  
ATOM   4032  CD  GLN C  48      19.271  61.373  61.817  1.00 41.00           C  
ANISOU 4032  CD  GLN C  48     4215   4741   6620   -514    457   -672       C  
ATOM   4033  OE1 GLN C  48      20.131  61.246  62.689  1.00 40.08           O  
ANISOU 4033  OE1 GLN C  48     4032   4687   6510   -572    424   -767       O  
ATOM   4034  NE2 GLN C  48      18.863  60.363  61.059  1.00 38.99           N  
ANISOU 4034  NE2 GLN C  48     4012   4571   6231   -428    466   -581       N  
ATOM   4035  N   PRO C  49      17.067  65.848  64.790  1.00 41.11           N  
ANISOU 4035  N   PRO C  49     4285   4222   7114   -577    338  -1178       N  
ATOM   4036  CA  PRO C  49      16.314  66.269  65.971  1.00 40.61           C  
ANISOU 4036  CA  PRO C  49     4237   4148   7045   -529    286  -1369       C  
ATOM   4037  C   PRO C  49      14.847  65.873  65.895  1.00 41.08           C  
ANISOU 4037  C   PRO C  49     4346   4268   6993   -406    301  -1355       C  
ATOM   4038  O   PRO C  49      14.315  65.519  64.842  1.00 41.44           O  
ANISOU 4038  O   PRO C  49     4426   4317   7004   -358    342  -1205       O  
ATOM   4039  CB  PRO C  49      16.461  67.794  65.928  1.00 40.61           C  
ANISOU 4039  CB  PRO C  49     4254   3908   7266   -574    268  -1422       C  
ATOM   4040  CG  PRO C  49      16.433  68.087  64.453  1.00 41.40           C  
ANISOU 4040  CG  PRO C  49     4391   3893   7445   -578    333  -1206       C  
ATOM   4041  CD  PRO C  49      17.112  66.909  63.768  1.00 40.85           C  
ANISOU 4041  CD  PRO C  49     4283   3988   7249   -604    378  -1059       C  
ATOM   4042  N   ALA C  50      14.200  65.932  67.054  1.00 42.67           N  
ANISOU 4042  N   ALA C  50     4544   4534   7135   -353    267  -1521       N  
ATOM   4043  CA  ALA C  50      12.749  65.932  67.081  1.00 42.31           C  
ANISOU 4043  CA  ALA C  50     4528   4516   7032   -239    282  -1536       C  
ATOM   4044  C   ALA C  50      12.237  67.296  66.637  1.00 42.14           C  
ANISOU 4044  C   ALA C  50     4551   4281   7181   -192    279  -1551       C  
ATOM   4045  O   ALA C  50      12.920  68.314  66.776  1.00 43.55           O  
ANISOU 4045  O   ALA C  50     4739   4292   7517   -249    250  -1614       O  
ATOM   4046  CB  ALA C  50      12.235  65.596  68.480  1.00 43.50           C  
ANISOU 4046  CB  ALA C  50     4652   4820   7056   -189    258  -1702       C  
ATOM   4047  N   VAL C  51      11.031  67.311  66.079  1.00 44.84           N  
ANISOU 4047  N   VAL C  51     4918   4621   7496    -89    301  -1489       N  
ATOM   4048  CA  VAL C  51      10.423  68.529  65.555  1.00 44.74           C  
ANISOU 4048  CA  VAL C  51     4957   4411   7631    -17    297  -1483       C  
ATOM   4049  C   VAL C  51       9.105  68.754  66.281  1.00 46.92           C  
ANISOU 4049  C   VAL C  51     5222   4751   7853    115    284  -1618       C  
ATOM   4050  O   VAL C  51       8.231  67.877  66.280  1.00 46.86           O  
ANISOU 4050  O   VAL C  51     5178   4919   7706    173    307  -1584       O  
ATOM   4051  CB  VAL C  51      10.212  68.459  64.034  1.00 44.76           C  
ANISOU 4051  CB  VAL C  51     4999   4348   7658      6    332  -1267       C  
ATOM   4052  CG1 VAL C  51       9.663  69.776  63.521  1.00 44.08           C  
ANISOU 4052  CG1 VAL C  51     4978   4042   7729     85    322  -1252       C  
ATOM   4053  CG2 VAL C  51      11.519  68.119  63.334  1.00 45.51           C  
ANISOU 4053  CG2 VAL C  51     5092   4424   7777   -115    359  -1129       C  
ATOM   4054  N   PHE C  52       8.965  69.928  66.890  1.00 45.09           N  
ANISOU 4054  N   PHE C  52     5017   4376   7738    164    246  -1773       N  
ATOM   4055  CA  PHE C  52       7.807  70.286  67.700  1.00 44.91           C  
ANISOU 4055  CA  PHE C  52     4979   4415   7670    306    234  -1932       C  
ATOM   4056  C   PHE C  52       7.063  71.429  67.020  1.00 46.73           C  
ANISOU 4056  C   PHE C  52     5269   4442   8044    420    219  -1914       C  
ATOM   4057  O   PHE C  52       7.605  72.531  66.878  1.00 46.81           O  
ANISOU 4057  O   PHE C  52     5346   4207   8233    397    182  -1946       O  
ATOM   4058  CB  PHE C  52       8.244  70.681  69.113  1.00 46.40           C  
ANISOU 4058  CB  PHE C  52     5154   4625   7852    297    189  -2163       C  
ATOM   4059  CG  PHE C  52       7.108  70.852  70.084  1.00 47.07           C  
ANISOU 4059  CG  PHE C  52     5206   4837   7840    450    189  -2335       C  
ATOM   4060  CD1 PHE C  52       6.546  72.100  70.300  1.00 48.33           C  
ANISOU 4060  CD1 PHE C  52     5409   4836   8116    575    150  -2475       C  
ATOM   4061  CD2 PHE C  52       6.614  69.769  70.794  1.00 45.50           C  
ANISOU 4061  CD2 PHE C  52     4934   4920   7435    472    230  -2353       C  
ATOM   4062  CE1 PHE C  52       5.506  72.262  71.198  1.00 47.85           C  
ANISOU 4062  CE1 PHE C  52     5310   4914   7957    732    156  -2640       C  
ATOM   4063  CE2 PHE C  52       5.576  69.926  71.693  1.00 45.34           C  
ANISOU 4063  CE2 PHE C  52     4870   5041   7316    612    245  -2500       C  
ATOM   4064  CZ  PHE C  52       5.021  71.174  71.895  1.00 46.40           C  
ANISOU 4064  CZ  PHE C  52     5039   5034   7557    749    209  -2649       C  
ATOM   4065  N   PHE C  53       5.833  71.154  66.587  1.00 50.63           N  
ANISOU 4065  N   PHE C  53     5739   5032   8466    542    243  -1856       N  
ATOM   4066  CA  PHE C  53       4.941  72.144  65.996  1.00 51.24           C  
ANISOU 4066  CA  PHE C  53     5864   4955   8650    687    225  -1845       C  
ATOM   4067  C   PHE C  53       4.038  72.689  67.093  1.00 51.19           C  
ANISOU 4067  C   PHE C  53     5825   5004   8619    835    204  -2066       C  
ATOM   4068  O   PHE C  53       3.207  71.952  67.645  1.00 51.31           O  
ANISOU 4068  O   PHE C  53     5750   5268   8478    896    236  -2117       O  
ATOM   4069  CB  PHE C  53       4.102  71.532  64.879  1.00 51.46           C  
ANISOU 4069  CB  PHE C  53     5869   5075   8609    748    252  -1666       C  
ATOM   4070  CG  PHE C  53       4.907  70.963  63.762  1.00 51.84           C  
ANISOU 4070  CG  PHE C  53     5950   5091   8656    632    273  -1456       C  
ATOM   4071  CD1 PHE C  53       5.339  69.650  63.804  1.00 51.83           C  
ANISOU 4071  CD1 PHE C  53     5895   5280   8517    525    301  -1394       C  
ATOM   4072  CD2 PHE C  53       5.230  71.740  62.663  1.00 53.60           C  
ANISOU 4072  CD2 PHE C  53     6261   5095   9010    639    268  -1315       C  
ATOM   4073  CE1 PHE C  53       6.079  69.123  62.773  1.00 53.11           C  
ANISOU 4073  CE1 PHE C  53     6088   5424   8668    438    320  -1214       C  
ATOM   4074  CE2 PHE C  53       5.968  71.218  61.629  1.00 53.66           C  
ANISOU 4074  CE2 PHE C  53     6293   5097   8998    547    297  -1120       C  
ATOM   4075  CZ  PHE C  53       6.392  69.909  61.684  1.00 53.01           C  
ANISOU 4075  CZ  PHE C  53     6154   5216   8774    452    322  -1078       C  
ATOM   4076  N   GLU C  54       4.205  73.983  67.389  1.00 57.27           N  
ANISOU 4076  N   GLU C  54     6671   5542   9547    894    151  -2195       N  
ATOM   4077  CA  GLU C  54       3.397  74.685  68.377  1.00 57.91           C  
ANISOU 4077  CA  GLU C  54     6741   5642   9622   1061    121  -2424       C  
ATOM   4078  C   GLU C  54       2.012  75.035  67.846  1.00 60.09           C  
ANISOU 4078  C   GLU C  54     7001   5932   9897   1259    127  -2395       C  
ATOM   4079  O   GLU C  54       1.057  75.114  68.628  1.00 61.73           O  
ANISOU 4079  O   GLU C  54     7143   6294  10018   1411    134  -2551       O  
ATOM   4080  CB  GLU C  54       4.111  75.966  68.819  1.00 59.57           C  
ANISOU 4080  CB  GLU C  54     7050   5566  10019   1053     45  -2579       C  
ATOM   4081  CG  GLU C  54       5.513  75.754  69.383  1.00 60.77           C  
ANISOU 4081  CG  GLU C  54     7206   5692  10192    861     22  -2631       C  
ATOM   4082  CD  GLU C  54       6.078  76.997  70.053  1.00 64.83           C  
ANISOU 4082  CD  GLU C  54     7799   5954  10881    865    -69  -2840       C  
ATOM   4083  OE1 GLU C  54       5.342  78.001  70.180  1.00 67.31           O  
ANISOU 4083  OE1 GLU C  54     8175   6152  11249   1017   -113  -2921       O  
ATOM   4084  OE2 GLU C  54       7.261  76.970  70.453  1.00 66.12           O  
ANISOU 4084  OE2 GLU C  54     7963   6065  11093    704   -104  -2890       O  
ATOM   4085  N   LYS C  55       1.880  75.257  66.539  1.00 56.96           N  
ANISOU 4085  N   LYS C  55     6661   5392   9591   1271    124  -2201       N  
ATOM   4086  CA  LYS C  55       0.615  75.690  65.958  1.00 57.97           C  
ANISOU 4086  CA  LYS C  55     6781   5511   9733   1471    113  -2171       C  
ATOM   4087  C   LYS C  55       0.358  74.940  64.660  1.00 57.36           C  
ANISOU 4087  C   LYS C  55     6684   5508   9604   1439    141  -1926       C  
ATOM   4088  O   LYS C  55       1.200  74.947  63.758  1.00 57.52           O  
ANISOU 4088  O   LYS C  55     6782   5380   9694   1324    143  -1753       O  
ATOM   4089  CB  LYS C  55       0.614  77.203  65.705  1.00 58.98           C  
ANISOU 4089  CB  LYS C  55     7041   5304  10067   1586     47  -2223       C  
ATOM   4090  N   ILE C  56      -0.802  74.293  64.575  1.00 50.63           N  
ANISOU 4090  N   ILE C  56     5719   4894   8624   1541    162  -1915       N  
ATOM   4091  CA  ILE C  56      -1.263  73.624  63.364  1.00 50.05           C  
ANISOU 4091  CA  ILE C  56     5616   4905   8496   1546    169  -1716       C  
ATOM   4092  C   ILE C  56      -2.621  74.211  63.004  1.00 52.10           C  
ANISOU 4092  C   ILE C  56     5841   5180   8775   1777    135  -1742       C  
ATOM   4093  O   ILE C  56      -3.484  74.366  63.876  1.00 53.50           O  
ANISOU 4093  O   ILE C  56     5925   5494   8907   1901    140  -1910       O  
ATOM   4094  CB  ILE C  56      -1.344  72.096  63.547  1.00 48.57           C  
ANISOU 4094  CB  ILE C  56     5310   5008   8138   1424    214  -1668       C  
ATOM   4095  CG1 ILE C  56       0.019  71.535  63.961  1.00 47.09           C  
ANISOU 4095  CG1 ILE C  56     5158   4807   7927   1217    241  -1652       C  
ATOM   4096  CG2 ILE C  56      -1.816  71.422  62.264  1.00 45.72           C  
ANISOU 4096  CG2 ILE C  56     4925   4719   7726   1433    202  -1481       C  
ATOM   4097  CD1 ILE C  56       0.128  71.206  65.434  1.00 47.06           C  
ANISOU 4097  CD1 ILE C  56     5084   4957   7839   1176    268  -1829       C  
ATOM   4098  N   LYS C  57      -2.801  74.545  61.726  1.00 62.53           N  
ANISOU 4098  N   LYS C  57     7232   6372  10154   1844    101  -1577       N  
ATOM   4099  CA  LYS C  57      -3.987  75.271  61.286  1.00 63.34           C  
ANISOU 4099  CA  LYS C  57     7325   6446  10295   2082     54  -1592       C  
ATOM   4100  C   LYS C  57      -5.258  74.490  61.598  1.00 62.54           C  
ANISOU 4100  C   LYS C  57     7035   6669  10060   2169     65  -1660       C  
ATOM   4101  O   LYS C  57      -5.417  73.344  61.165  1.00 62.11           O  
ANISOU 4101  O   LYS C  57     6893   6809   9897   2072     81  -1559       O  
ATOM   4102  CB  LYS C  57      -3.895  75.561  59.789  1.00 66.31           C  
ANISOU 4102  CB  LYS C  57     7806   6665  10723   2124     18  -1373       C  
ATOM   4103  CG  LYS C  57      -5.092  76.312  59.230  1.00 69.69           C  
ANISOU 4103  CG  LYS C  57     8234   7059  11188   2382    -43  -1370       C  
ATOM   4104  CD  LYS C  57      -4.718  77.119  57.997  1.00 72.41           C  
ANISOU 4104  CD  LYS C  57     8749   7131  11634   2440    -81  -1177       C  
ATOM   4105  CE  LYS C  57      -4.640  76.241  56.759  1.00 72.43           C  
ANISOU 4105  CE  LYS C  57     8743   7248  11529   2382    -80   -964       C  
ATOM   4106  NZ  LYS C  57      -5.991  75.859  56.260  1.00 72.45           N  
ANISOU 4106  NZ  LYS C  57     8627   7466  11435   2557   -133   -962       N  
ATOM   4107  N   GLY C  58      -6.161  75.116  62.350  1.00 62.31           N  
ANISOU 4107  N   GLY C  58     6938   6694  10043   2352     55  -1836       N  
ATOM   4108  CA  GLY C  58      -7.432  74.519  62.697  1.00 62.60           C  
ANISOU 4108  CA  GLY C  58     6777   7041   9968   2449     73  -1908       C  
ATOM   4109  C   GLY C  58      -7.438  73.702  63.969  1.00 61.36           C  
ANISOU 4109  C   GLY C  58     6489   7134   9693   2340    147  -2030       C  
ATOM   4110  O   GLY C  58      -8.507  73.225  64.372  1.00 60.80           O  
ANISOU 4110  O   GLY C  58     6238   7333   9531   2412    176  -2091       O  
ATOM   4111  N   TYR C  59      -6.293  73.531  64.621  1.00 51.05           N  
ANISOU 4111  N   TYR C  59     5260   5755   8383   2172    180  -2064       N  
ATOM   4112  CA  TYR C  59      -6.185  72.692  65.803  1.00 51.06           C  
ANISOU 4112  CA  TYR C  59     5155   5991   8257   2060    250  -2157       C  
ATOM   4113  C   TYR C  59      -5.799  73.526  67.015  1.00 51.27           C  
ANISOU 4113  C   TYR C  59     5233   5940   8307   2121    258  -2367       C  
ATOM   4114  O   TYR C  59      -5.187  74.591  66.892  1.00 51.55           O  
ANISOU 4114  O   TYR C  59     5419   5690   8478   2166    205  -2415       O  
ATOM   4115  CB  TYR C  59      -5.159  71.575  65.595  1.00 50.53           C  
ANISOU 4115  CB  TYR C  59     5118   5949   8132   1809    276  -2021       C  
ATOM   4116  CG  TYR C  59      -5.628  70.489  64.658  1.00 50.31           C  
ANISOU 4116  CG  TYR C  59     5009   6065   8041   1738    273  -1851       C  
ATOM   4117  CD1 TYR C  59      -6.730  69.703  64.971  1.00 49.61           C  
ANISOU 4117  CD1 TYR C  59     4737   6261   7852   1759    306  -1867       C  
ATOM   4118  CD2 TYR C  59      -4.973  70.251  63.457  1.00 49.66           C  
ANISOU 4118  CD2 TYR C  59     5028   5839   8000   1651    235  -1677       C  
ATOM   4119  CE1 TYR C  59      -7.163  68.707  64.119  1.00 48.62           C  
ANISOU 4119  CE1 TYR C  59     4536   6253   7682   1686    287  -1726       C  
ATOM   4120  CE2 TYR C  59      -5.397  69.256  62.599  1.00 50.93           C  
ANISOU 4120  CE2 TYR C  59     5124   6129   8099   1598    218  -1543       C  
ATOM   4121  CZ  TYR C  59      -6.493  68.488  62.934  1.00 50.69           C  
ANISOU 4121  CZ  TYR C  59     4915   6362   7983   1612    237  -1573       C  
ATOM   4122  OH  TYR C  59      -6.920  67.497  62.081  1.00 52.03           O  
ANISOU 4122  OH  TYR C  59     5018   6646   8105   1550    203  -1453       O  
ATOM   4123  N   LYS C  60      -6.169  73.023  68.194  1.00 58.43           N  
ANISOU 4123  N   LYS C  60     6015   7106   9079   2122    322  -2491       N  
ATOM   4124  CA  LYS C  60      -5.869  73.721  69.438  1.00 60.06           C  
ANISOU 4124  CA  LYS C  60     6269   7291   9261   2179    325  -2691       C  
ATOM   4125  C   LYS C  60      -4.460  73.421  69.932  1.00 58.49           C  
ANISOU 4125  C   LYS C  60     6157   7001   9066   1996    328  -2720       C  
ATOM   4126  O   LYS C  60      -3.787  74.310  70.466  1.00 60.13           O  
ANISOU 4126  O   LYS C  60     6482   7024   9340   2013    281  -2849       O  
ATOM   4127  CB  LYS C  60      -6.885  73.334  70.514  1.00 62.85           C  
ANISOU 4127  CB  LYS C  60     6469   7983   9429   2245    395  -2768       C  
ATOM   4128  CG  LYS C  60      -7.838  74.443  70.920  1.00 67.76           C  
ANISOU 4128  CG  LYS C  60     7100   8608  10037   2453    369  -2871       C  
ATOM   4129  CD  LYS C  60      -8.576  74.077  72.201  1.00 71.12           C  
ANISOU 4129  CD  LYS C  60     7391   9360  10271   2496    448  -2961       C  
ATOM   4130  CE  LYS C  60      -9.405  72.813  72.022  1.00 71.54           C  
ANISOU 4130  CE  LYS C  60     7242   9720  10220   2429    530  -2836       C  
ATOM   4131  NZ  LYS C  60      -9.973  72.323  73.311  1.00 72.69           N  
ANISOU 4131  NZ  LYS C  60     7261  10184  10174   2432    622  -2893       N  
ATOM   4132  N   TYR C  61      -3.995  72.188  69.760  1.00 52.79           N  
ANISOU 4132  N   TYR C  61     5396   6406   8254   1795    369  -2571       N  
ATOM   4133  CA  TYR C  61      -2.822  71.704  70.466  1.00 53.26           C  
ANISOU 4133  CA  TYR C  61     5505   6475   8258   1625    382  -2595       C  
ATOM   4134  C   TYR C  61      -1.669  71.428  69.502  1.00 54.26           C  
ANISOU 4134  C   TYR C  61     5741   6402   8474   1444    348  -2425       C  
ATOM   4135  O   TYR C  61      -1.721  71.768  68.314  1.00 55.38           O  
ANISOU 4135  O   TYR C  61     5941   6372   8729   1460    312  -2298       O  
ATOM   4136  CB  TYR C  61      -3.207  70.477  71.293  1.00 52.55           C  
ANISOU 4136  CB  TYR C  61     5277   6722   7969   1558    465  -2582       C  
ATOM   4137  CG  TYR C  61      -4.276  70.802  72.308  1.00 54.10           C  
ANISOU 4137  CG  TYR C  61     5358   7133   8065   1740    513  -2752       C  
ATOM   4138  CD1 TYR C  61      -4.023  71.697  73.339  1.00 53.00           C  
ANISOU 4138  CD1 TYR C  61     5275   6953   7912   1848    492  -2967       C  
ATOM   4139  CD2 TYR C  61      -5.543  70.241  72.222  1.00 55.55           C  
ANISOU 4139  CD2 TYR C  61     5376   7563   8166   1804    575  -2694       C  
ATOM   4140  CE1 TYR C  61      -4.996  72.013  74.265  1.00 56.61           C  
ANISOU 4140  CE1 TYR C  61     5664   7611   8236   1984    524  -3055       C  
ATOM   4141  CE2 TYR C  61      -6.525  70.552  73.146  1.00 56.69           C  
ANISOU 4141  CE2 TYR C  61     5425   7916   8198   1949    620  -2804       C  
ATOM   4142  CZ  TYR C  61      -6.244  71.438  74.165  1.00 57.54           C  
ANISOU 4142  CZ  TYR C  61     5621   7978   8262   2035    594  -2969       C  
ATOM   4143  OH  TYR C  61      -7.213  71.753  75.089  1.00 59.61           O  
ANISOU 4143  OH  TYR C  61     5808   8446   8394   2168    635  -3048       O  
ATOM   4144  N   SER C  62      -0.618  70.804  70.027  1.00 52.24           N  
ANISOU 4144  N   SER C  62     5510   6182   8157   1281    360  -2420       N  
ATOM   4145  CA  SER C  62       0.680  70.746  69.377  1.00 52.45           C  
ANISOU 4145  CA  SER C  62     5640   6013   8274   1121    326  -2310       C  
ATOM   4146  C   SER C  62       1.033  69.317  68.988  1.00 52.07           C  
ANISOU 4146  C   SER C  62     5552   6112   8119    962    362  -2136       C  
ATOM   4147  O   SER C  62       0.476  68.347  69.513  1.00 51.39           O  
ANISOU 4147  O   SER C  62     5367   6272   7885    945    411  -2125       O  
ATOM   4148  CB  SER C  62       1.768  71.307  70.298  1.00 54.45           C  
ANISOU 4148  CB  SER C  62     5962   6160   8567   1069    290  -2468       C  
ATOM   4149  OG  SER C  62       1.994  70.432  71.389  1.00 56.18           O  
ANISOU 4149  OG  SER C  62     6116   6615   8615   1008    326  -2533       O  
ATOM   4150  N   VAL C  63       1.998  69.199  68.076  1.00 53.48           N  
ANISOU 4150  N   VAL C  63     5809   6134   8377    845    340  -1998       N  
ATOM   4151  CA  VAL C  63       2.444  67.898  67.584  1.00 52.94           C  
ANISOU 4151  CA  VAL C  63     5722   6171   8220    706    362  -1836       C  
ATOM   4152  C   VAL C  63       3.955  67.809  67.741  1.00 53.66           C  
ANISOU 4152  C   VAL C  63     5878   6168   8342    565    346  -1828       C  
ATOM   4153  O   VAL C  63       4.657  68.815  67.615  1.00 55.72           O  
ANISOU 4153  O   VAL C  63     6211   6219   8740    556    312  -1871       O  
ATOM   4154  CB  VAL C  63       2.026  67.674  66.112  1.00 54.44           C  
ANISOU 4154  CB  VAL C  63     5928   6306   8451    722    351  -1655       C  
ATOM   4155  CG1 VAL C  63       2.628  66.391  65.553  1.00 52.70           C  
ANISOU 4155  CG1 VAL C  63     5708   6165   8150    586    361  -1504       C  
ATOM   4156  CG2 VAL C  63       0.515  67.631  65.994  1.00 55.84           C  
ANISOU 4156  CG2 VAL C  63     6015   6611   8590    854    359  -1668       C  
ATOM   4157  N   VAL C  64       4.463  66.619  68.047  1.00 35.07           N  
ANISOU 4157  N   VAL C  64     3495   3965   5866    455    366  -1774       N  
ATOM   4158  CA  VAL C  64       5.902  66.387  68.034  1.00 34.40           C  
ANISOU 4158  CA  VAL C  64     3457   3813   5801    325    349  -1742       C  
ATOM   4159  C   VAL C  64       6.185  65.109  67.256  1.00 34.16           C  
ANISOU 4159  C   VAL C  64     3421   3866   5690    240    364  -1566       C  
ATOM   4160  O   VAL C  64       5.438  64.128  67.350  1.00 32.78           O  
ANISOU 4160  O   VAL C  64     3196   3859   5400    246    385  -1520       O  
ATOM   4161  CB  VAL C  64       6.505  66.332  69.458  1.00 35.48           C  
ANISOU 4161  CB  VAL C  64     3575   4041   5866    292    339  -1902       C  
ATOM   4162  CG1 VAL C  64       6.043  65.098  70.217  1.00 34.16           C  
ANISOU 4162  CG1 VAL C  64     3344   4129   5507    281    376  -1893       C  
ATOM   4163  CG2 VAL C  64       8.030  66.403  69.395  1.00 34.63           C  
ANISOU 4163  CG2 VAL C  64     3507   3829   5821    171    307  -1891       C  
ATOM   4164  N   THR C  65       7.250  65.136  66.460  1.00 39.92           N  
ANISOU 4164  N   THR C  65     4202   4477   6488    161    353  -1468       N  
ATOM   4165  CA  THR C  65       7.597  64.019  65.596  1.00 39.02           C  
ANISOU 4165  CA  THR C  65     4096   4423   6306    100    360  -1308       C  
ATOM   4166  C   THR C  65       9.104  63.805  65.629  1.00 38.74           C  
ANISOU 4166  C   THR C  65     4083   4354   6284     -6    353  -1285       C  
ATOM   4167  O   THR C  65       9.866  64.666  66.077  1.00 39.51           O  
ANISOU 4167  O   THR C  65     4189   4347   6475    -40    340  -1371       O  
ATOM   4168  CB  THR C  65       7.108  64.251  64.159  1.00 40.37           C  
ANISOU 4168  CB  THR C  65     4302   4502   6535    155    360  -1172       C  
ATOM   4169  OG1 THR C  65       7.331  63.071  63.378  1.00 40.81           O  
ANISOU 4169  OG1 THR C  65     4365   4638   6502    114    359  -1040       O  
ATOM   4170  CG2 THR C  65       7.840  65.424  63.522  1.00 39.91           C  
ANISOU 4170  CG2 THR C  65     4302   4232   6628    148    359  -1135       C  
ATOM   4171  N   ASN C  66       9.523  62.634  65.145  1.00 41.77           N  
ANISOU 4171  N   ASN C  66     4469   4825   6575    -54    357  -1175       N  
ATOM   4172  CA  ASN C  66      10.934  62.234  65.118  1.00 41.43           C  
ANISOU 4172  CA  ASN C  66     4433   4786   6522   -141    351  -1142       C  
ATOM   4173  C   ASN C  66      11.549  62.266  66.516  1.00 41.63           C  
ANISOU 4173  C   ASN C  66     4427   4876   6515   -184    332  -1286       C  
ATOM   4174  O   ASN C  66      12.708  62.646  66.696  1.00 43.75           O  
ANISOU 4174  O   ASN C  66     4686   5091   6846   -247    317  -1320       O  
ATOM   4175  CB  ASN C  66      11.742  63.099  64.149  1.00 43.13           C  
ANISOU 4175  CB  ASN C  66     4675   4839   6873   -169    364  -1063       C  
ATOM   4176  CG  ASN C  66      12.948  62.372  63.589  1.00 46.22           C  
ANISOU 4176  CG  ASN C  66     5063   5272   7225   -233    373   -964       C  
ATOM   4177  OD1 ASN C  66      12.867  61.195  63.234  1.00 45.32           O  
ANISOU 4177  OD1 ASN C  66     4959   5270   6992   -219    369   -893       O  
ATOM   4178  ND2 ASN C  66      14.078  63.067  63.513  1.00 47.17           N  
ANISOU 4178  ND2 ASN C  66     5166   5303   7453   -303    382   -963       N  
ATOM   4179  N   VAL C  67      10.767  61.854  67.515  1.00 32.98           N  
ANISOU 4179  N   VAL C  67     3308   3907   5316   -148    331  -1370       N  
ATOM   4180  CA  VAL C  67      11.244  61.878  68.895  1.00 34.80           C  
ANISOU 4180  CA  VAL C  67     3514   4222   5487   -166    310  -1512       C  
ATOM   4181  C   VAL C  67      12.374  60.873  69.090  1.00 34.67           C  
ANISOU 4181  C   VAL C  67     3496   4294   5384   -232    291  -1469       C  
ATOM   4182  O   VAL C  67      13.351  61.147  69.797  1.00 33.98           O  
ANISOU 4182  O   VAL C  67     3390   4215   5306   -269    257  -1564       O  
ATOM   4183  CB  VAL C  67      10.072  61.623  69.862  1.00 36.29           C  
ANISOU 4183  CB  VAL C  67     3675   4550   5564   -101    330  -1587       C  
ATOM   4184  CG1 VAL C  67      10.568  61.484  71.295  1.00 34.04           C  
ANISOU 4184  CG1 VAL C  67     3372   4386   5177   -106    310  -1720       C  
ATOM   4185  CG2 VAL C  67       9.040  62.739  69.753  1.00 33.24           C  
ANISOU 4185  CG2 VAL C  67     3281   4080   5270    -16    343  -1657       C  
ATOM   4186  N   HIS C  68      12.268  59.703  68.461  1.00 43.16           N  
ANISOU 4186  N   HIS C  68     4590   5433   6377   -241    301  -1333       N  
ATOM   4187  CA  HIS C  68      13.279  58.660  68.562  1.00 42.09           C  
ANISOU 4187  CA  HIS C  68     4461   5377   6153   -283    278  -1284       C  
ATOM   4188  C   HIS C  68      14.235  58.646  67.374  1.00 43.83           C  
ANISOU 4188  C   HIS C  68     4692   5516   6446   -313    277  -1183       C  
ATOM   4189  O   HIS C  68      15.060  57.735  67.270  1.00 45.31           O  
ANISOU 4189  O   HIS C  68     4885   5769   6562   -330    259  -1132       O  
ATOM   4190  CB  HIS C  68      12.611  57.287  68.686  1.00 42.08           C  
ANISOU 4190  CB  HIS C  68     4483   5493   6012   -270    281  -1204       C  
ATOM   4191  CG  HIS C  68      11.976  57.029  70.018  1.00 44.06           C  
ANISOU 4191  CG  HIS C  68     4716   5870   6154   -253    290  -1280       C  
ATOM   4192  ND1 HIS C  68      10.759  57.565  70.379  1.00 44.49           N  
ANISOU 4192  ND1 HIS C  68     4743   5946   6216   -212    324  -1332       N  
ATOM   4193  CD2 HIS C  68      12.380  56.275  71.067  1.00 44.65           C  
ANISOU 4193  CD2 HIS C  68     4797   6070   6098   -260    274  -1304       C  
ATOM   4194  CE1 HIS C  68      10.445  57.159  71.597  1.00 45.54           C  
ANISOU 4194  CE1 HIS C  68     4859   6220   6224   -200    337  -1383       C  
ATOM   4195  NE2 HIS C  68      11.412  56.375  72.037  1.00 45.15           N  
ANISOU 4195  NE2 HIS C  68     4836   6232   6087   -229    306  -1363       N  
ATOM   4196  N   GLY C  69      14.154  59.635  66.487  1.00 38.90           N  
ANISOU 4196  N   GLY C  69     4069   4755   5954   -312    300  -1150       N  
ATOM   4197  CA  GLY C  69      14.724  59.498  65.159  1.00 38.89           C  
ANISOU 4197  CA  GLY C  69     4084   4698   5993   -320    318  -1016       C  
ATOM   4198  C   GLY C  69      16.189  59.831  64.954  1.00 37.59           C  
ANISOU 4198  C   GLY C  69     3882   4504   5897   -381    320  -1005       C  
ATOM   4199  O   GLY C  69      16.546  60.408  63.923  1.00 39.63           O  
ANISOU 4199  O   GLY C  69     4140   4669   6249   -394    354   -914       O  
ATOM   4200  N   SER C  70      17.045  59.465  65.905  1.00 37.63           N  
ANISOU 4200  N   SER C  70     3848   4598   5854   -417    286  -1088       N  
ATOM   4201  CA  SER C  70      18.489  59.599  65.739  1.00 38.07           C  
ANISOU 4201  CA  SER C  70     3844   4660   5961   -475    282  -1077       C  
ATOM   4202  C   SER C  70      19.178  58.888  66.891  1.00 38.26           C  
ANISOU 4202  C   SER C  70     3835   4820   5883   -483    228  -1173       C  
ATOM   4203  O   SER C  70      18.580  58.657  67.945  1.00 38.78           O  
ANISOU 4203  O   SER C  70     3921   4948   5867   -456    198  -1265       O  
ATOM   4204  CB  SER C  70      18.933  61.064  65.682  1.00 39.72           C  
ANISOU 4204  CB  SER C  70     4009   4725   6358   -547    293  -1123       C  
ATOM   4205  OG  SER C  70      18.774  61.700  66.939  1.00 39.61           O  
ANISOU 4205  OG  SER C  70     3978   4694   6379   -566    245  -1296       O  
ATOM   4206  N   TRP C  71      20.453  58.556  66.681  1.00 38.97           N  
ANISOU 4206  N   TRP C  71     3868   4968   5971   -510    218  -1145       N  
ATOM   4207  CA  TRP C  71      21.217  57.905  67.734  1.00 37.02           C  
ANISOU 4207  CA  TRP C  71     3584   4854   5626   -506    157  -1233       C  
ATOM   4208  C   TRP C  71      21.493  58.837  68.905  1.00 39.12           C  
ANISOU 4208  C   TRP C  71     3797   5107   5961   -556    108  -1404       C  
ATOM   4209  O   TRP C  71      21.686  58.358  70.026  1.00 41.49           O  
ANISOU 4209  O   TRP C  71     4091   5523   6149   -529     50  -1501       O  
ATOM   4210  CB  TRP C  71      22.516  57.337  67.161  1.00 36.33           C  
ANISOU 4210  CB  TRP C  71     3436   4843   5524   -509    156  -1164       C  
ATOM   4211  CG  TRP C  71      22.246  56.145  66.301  1.00 38.66           C  
ANISOU 4211  CG  TRP C  71     3801   5185   5702   -429    177  -1034       C  
ATOM   4212  CD1 TRP C  71      22.534  56.005  64.976  1.00 37.91           C  
ANISOU 4212  CD1 TRP C  71     3705   5070   5629   -407    228   -908       C  
ATOM   4213  CD2 TRP C  71      21.581  54.940  66.699  1.00 38.01           C  
ANISOU 4213  CD2 TRP C  71     3806   5170   5465   -358    143  -1019       C  
ATOM   4214  NE1 TRP C  71      22.109  54.778  64.528  1.00 37.46           N  
ANISOU 4214  NE1 TRP C  71     3733   5061   5440   -320    216   -836       N  
ATOM   4215  CE2 TRP C  71      21.520  54.105  65.567  1.00 38.77           C  
ANISOU 4215  CE2 TRP C  71     3955   5270   5508   -298    163   -898       C  
ATOM   4216  CE3 TRP C  71      21.042  54.480  67.906  1.00 38.28           C  
ANISOU 4216  CE3 TRP C  71     3881   5263   5399   -339    100  -1092       C  
ATOM   4217  CZ2 TRP C  71      20.941  52.839  65.605  1.00 39.12           C  
ANISOU 4217  CZ2 TRP C  71     4091   5350   5422   -232    130   -855       C  
ATOM   4218  CZ3 TRP C  71      20.466  53.223  67.941  1.00 37.19           C  
ANISOU 4218  CZ3 TRP C  71     3831   5170   5130   -281     81  -1027       C  
ATOM   4219  CH2 TRP C  71      20.421  52.417  66.798  1.00 37.52           C  
ANISOU 4219  CH2 TRP C  71     3924   5189   5141   -234     91   -913       C  
ATOM   4220  N   GLN C  72      21.488  60.152  68.678  1.00 37.44           N  
ANISOU 4220  N   GLN C  72     3553   4750   5923   -622    123  -1445       N  
ATOM   4221  CA  GLN C  72      21.563  61.093  69.790  1.00 38.19           C  
ANISOU 4221  CA  GLN C  72     3615   4807   6088   -659     65  -1630       C  
ATOM   4222  C   GLN C  72      20.307  61.015  70.651  1.00 39.32           C  
ANISOU 4222  C   GLN C  72     3831   4983   6127   -582     55  -1715       C  
ATOM   4223  O   GLN C  72      20.388  60.935  71.884  1.00 39.72           O  
ANISOU 4223  O   GLN C  72     3871   5131   6090   -557     -3  -1858       O  
ATOM   4224  CB  GLN C  72      21.770  62.513  69.261  1.00 38.73           C  
ANISOU 4224  CB  GLN C  72     3650   4680   6385   -746     82  -1642       C  
ATOM   4225  CG  GLN C  72      23.212  62.861  68.912  1.00 40.22           C  
ANISOU 4225  CG  GLN C  72     3727   4852   6701   -853     72  -1623       C  
ATOM   4226  CD  GLN C  72      23.756  62.052  67.742  1.00 41.88           C  
ANISOU 4226  CD  GLN C  72     3913   5132   6866   -844    139  -1430       C  
ATOM   4227  OE1 GLN C  72      23.002  61.582  66.888  1.00 41.79           O  
ANISOU 4227  OE1 GLN C  72     3981   5110   6788   -778    200  -1296       O  
ATOM   4228  NE2 GLN C  72      25.074  61.890  67.700  1.00 43.92           N  
ANISOU 4228  NE2 GLN C  72     4057   5472   7157   -904    122  -1426       N  
ATOM   4229  N   ASN C  73      19.133  61.043  70.014  1.00 36.95           N  
ANISOU 4229  N   ASN C  73     3597   4615   5827   -539    113  -1628       N  
ATOM   4230  CA  ASN C  73      17.882  60.914  70.755  1.00 34.62           C  
ANISOU 4230  CA  ASN C  73     3352   4371   5430   -465    118  -1692       C  
ATOM   4231  C   ASN C  73      17.783  59.552  71.430  1.00 34.81           C  
ANISOU 4231  C   ASN C  73     3397   4581   5247   -418    105  -1667       C  
ATOM   4232  O   ASN C  73      17.322  59.448  72.573  1.00 36.31           O  
ANISOU 4232  O   ASN C  73     3597   4870   5329   -374     86  -1770       O  
ATOM   4233  CB  ASN C  73      16.695  61.136  69.819  1.00 37.00           C  
ANISOU 4233  CB  ASN C  73     3703   4576   5779   -428    178  -1590       C  
ATOM   4234  CG  ASN C  73      16.656  62.541  69.252  1.00 39.86           C  
ANISOU 4234  CG  ASN C  73     4063   4742   6340   -458    189  -1611       C  
ATOM   4235  OD1 ASN C  73      17.605  63.311  69.401  1.00 39.66           O  
ANISOU 4235  OD1 ASN C  73     3996   4636   6438   -528    157  -1681       O  
ATOM   4236  ND2 ASN C  73      15.552  62.883  68.596  1.00 37.88           N  
ANISOU 4236  ND2 ASN C  73     3854   4409   6128   -407    229  -1549       N  
ATOM   4237  N   HIS C  74      18.210  58.496  70.732  1.00 35.12           N  
ANISOU 4237  N   HIS C  74     3450   4668   5226   -419    116  -1529       N  
ATOM   4238  CA  HIS C  74      18.233  57.162  71.323  1.00 36.87           C  
ANISOU 4238  CA  HIS C  74     3703   5041   5265   -377     95  -1492       C  
ATOM   4239  C   HIS C  74      19.130  57.120  72.554  1.00 37.85           C  
ANISOU 4239  C   HIS C  74     3788   5278   5315   -373     29  -1619       C  
ATOM   4240  O   HIS C  74      18.773  56.516  73.573  1.00 38.62           O  
ANISOU 4240  O   HIS C  74     3916   5499   5259   -326     12  -1653       O  
ATOM   4241  CB  HIS C  74      18.704  56.148  70.279  1.00 34.97           C  
ANISOU 4241  CB  HIS C  74     3486   4807   4996   -372    104  -1340       C  
ATOM   4242  CG  HIS C  74      18.386  54.724  70.618  1.00 35.95           C  
ANISOU 4242  CG  HIS C  74     3672   5035   4953   -325     90  -1268       C  
ATOM   4243  ND1 HIS C  74      19.143  53.980  71.497  1.00 36.09           N  
ANISOU 4243  ND1 HIS C  74     3690   5171   4850   -299     37  -1298       N  
ATOM   4244  CD2 HIS C  74      17.405  53.901  70.177  1.00 36.25           C  
ANISOU 4244  CD2 HIS C  74     3775   5065   4934   -304    114  -1163       C  
ATOM   4245  CE1 HIS C  74      18.637  52.763  71.590  1.00 36.10           C  
ANISOU 4245  CE1 HIS C  74     3766   5222   4730   -264     35  -1205       C  
ATOM   4246  NE2 HIS C  74      17.582  52.689  70.799  1.00 35.66           N  
ANISOU 4246  NE2 HIS C  74     3745   5087   4715   -274     80  -1125       N  
ATOM   4247  N   ALA C  75      20.298  57.763  72.481  1.00 39.87           N  
ANISOU 4247  N   ALA C  75     3972   5500   5677   -424    -10  -1687       N  
ATOM   4248  CA  ALA C  75      21.204  57.789  73.624  1.00 40.56           C  
ANISOU 4248  CA  ALA C  75     4009   5698   5704   -419    -90  -1825       C  
ATOM   4249  C   ALA C  75      20.598  58.557  74.790  1.00 42.24           C  
ANISOU 4249  C   ALA C  75     4229   5931   5889   -393   -117  -1996       C  
ATOM   4250  O   ALA C  75      20.715  58.134  75.947  1.00 44.32           O  
ANISOU 4250  O   ALA C  75     4501   6342   5998   -339   -166  -2079       O  
ATOM   4251  CB  ALA C  75      22.543  58.403  73.218  1.00 39.66           C  
ANISOU 4251  CB  ALA C  75     3795   5536   5737   -494   -127  -1864       C  
ATOM   4252  N   LEU C  76      19.951  59.689  74.508  1.00 38.83           N  
ANISOU 4252  N   LEU C  76     3799   5357   5599   -419    -89  -2050       N  
ATOM   4253  CA  LEU C  76      19.324  60.456  75.579  1.00 40.25           C  
ANISOU 4253  CA  LEU C  76     3990   5553   5751   -374   -115  -2227       C  
ATOM   4254  C   LEU C  76      18.150  59.704  76.195  1.00 39.55           C  
ANISOU 4254  C   LEU C  76     3962   5597   5469   -286    -67  -2189       C  
ATOM   4255  O   LEU C  76      17.873  59.861  77.390  1.00 39.38           O  
ANISOU 4255  O   LEU C  76     3946   5688   5330   -223    -95  -2325       O  
ATOM   4256  CB  LEU C  76      18.877  61.820  75.056  1.00 40.00           C  
ANISOU 4256  CB  LEU C  76     3956   5320   5923   -408    -97  -2285       C  
ATOM   4257  CG  LEU C  76      20.027  62.756  74.680  1.00 39.84           C  
ANISOU 4257  CG  LEU C  76     3869   5159   6109   -510   -149  -2348       C  
ATOM   4258  CD1 LEU C  76      19.530  63.932  73.857  1.00 38.87           C  
ANISOU 4258  CD1 LEU C  76     3765   4808   6196   -548   -113  -2333       C  
ATOM   4259  CD2 LEU C  76      20.751  63.237  75.930  1.00 39.86           C  
ANISOU 4259  CD2 LEU C  76     3824   5225   6095   -513   -258  -2573       C  
ATOM   4260  N   MET C  77      17.455  58.885  75.403  1.00 40.03           N  
ANISOU 4260  N   MET C  77     4064   5652   5494   -281      3  -2007       N  
ATOM   4261  CA  MET C  77      16.382  58.057  75.944  1.00 41.77           C  
ANISOU 4261  CA  MET C  77     4329   6001   5543   -221     51  -1946       C  
ATOM   4262  C   MET C  77      16.911  57.099  77.004  1.00 43.48           C  
ANISOU 4262  C   MET C  77     4559   6399   5561   -183     11  -1954       C  
ATOM   4263  O   MET C  77      16.221  56.805  77.988  1.00 43.99           O  
ANISOU 4263  O   MET C  77     4646   6600   5470   -123     33  -1981       O  
ATOM   4264  CB  MET C  77      15.697  57.292  74.811  1.00 40.38           C  
ANISOU 4264  CB  MET C  77     4188   5770   5386   -240    113  -1752       C  
ATOM   4265  CG  MET C  77      14.798  56.155  75.264  1.00 42.20           C  
ANISOU 4265  CG  MET C  77     4458   6129   5448   -208    155  -1651       C  
ATOM   4266  SD  MET C  77      14.305  55.083  73.898  1.00 42.82           S  
ANISOU 4266  SD  MET C  77     4579   6135   5556   -244    190  -1436       S  
ATOM   4267  CE  MET C  77      15.706  53.969  73.804  1.00 40.88           C  
ANISOU 4267  CE  MET C  77     4367   5928   5240   -252    127  -1365       C  
ATOM   4268  N   LEU C  78      18.136  56.613  76.826  1.00 41.56           N  
ANISOU 4268  N   LEU C  78     4302   6171   5317   -207    -47  -1926       N  
ATOM   4269  CA  LEU C  78      18.787  55.738  77.789  1.00 41.57           C  
ANISOU 4269  CA  LEU C  78     4319   6337   5137   -160   -101  -1935       C  
ATOM   4270  C   LEU C  78      19.512  56.507  78.886  1.00 41.98           C  
ANISOU 4270  C   LEU C  78     4323   6468   5161   -132   -185  -2145       C  
ATOM   4271  O   LEU C  78      20.261  55.901  79.659  1.00 43.05           O  
ANISOU 4271  O   LEU C  78     4458   6741   5156    -87   -250  -2171       O  
ATOM   4272  CB  LEU C  78      19.772  54.811  77.074  1.00 39.32           C  
ANISOU 4272  CB  LEU C  78     4038   6043   4859   -179   -132  -1813       C  
ATOM   4273  CG  LEU C  78      19.195  53.941  75.957  1.00 38.82           C  
ANISOU 4273  CG  LEU C  78     4031   5903   4815   -196    -71  -1618       C  
ATOM   4274  CD1 LEU C  78      20.315  53.316  75.135  1.00 39.00           C  
ANISOU 4274  CD1 LEU C  78     4043   5901   4875   -204   -108  -1539       C  
ATOM   4275  CD2 LEU C  78      18.288  52.868  76.531  1.00 39.29           C  
ANISOU 4275  CD2 LEU C  78     4169   6055   4705   -157    -37  -1515       C  
ATOM   4276  N   GLY C  79      19.313  57.820  78.970  1.00 45.98           N  
ANISOU 4276  N   GLY C  79     4791   6884   5797   -151   -196  -2300       N  
ATOM   4277  CA  GLY C  79      20.018  58.608  79.961  1.00 46.24           C  
ANISOU 4277  CA  GLY C  79     4777   6971   5823   -130   -292  -2521       C  
ATOM   4278  C   GLY C  79      21.510  58.699  79.748  1.00 46.70           C  
ANISOU 4278  C   GLY C  79     4760   7009   5973   -189   -384  -2568       C  
ATOM   4279  O   GLY C  79      22.248  58.951  80.703  1.00 48.20           O  
ANISOU 4279  O   GLY C  79     4910   7299   6103   -160   -485  -2733       O  
ATOM   4280  N   LEU C  80      21.978  58.500  78.522  1.00 46.17           N  
ANISOU 4280  N   LEU C  80     4666   6830   6045   -266   -353  -2430       N  
ATOM   4281  CA  LEU C  80      23.395  58.563  78.200  1.00 47.59           C  
ANISOU 4281  CA  LEU C  80     4755   7003   6324   -327   -423  -2453       C  
ATOM   4282  C   LEU C  80      23.731  59.881  77.513  1.00 47.76           C  
ANISOU 4282  C   LEU C  80     4705   6832   6608   -438   -428  -2523       C  
ATOM   4283  O   LEU C  80      22.854  60.596  77.020  1.00 48.27           O  
ANISOU 4283  O   LEU C  80     4808   6748   6784   -462   -365  -2508       O  
ATOM   4284  CB  LEU C  80      23.799  57.393  77.299  1.00 48.02           C  
ANISOU 4284  CB  LEU C  80     4821   7084   6341   -325   -384  -2248       C  
ATOM   4285  CG  LEU C  80      23.497  55.980  77.801  1.00 48.59           C  
ANISOU 4285  CG  LEU C  80     4977   7307   6177   -226   -378  -2141       C  
ATOM   4286  CD1 LEU C  80      23.740  54.962  76.697  1.00 46.94           C  
ANISOU 4286  CD1 LEU C  80     4795   7070   5973   -226   -336  -1945       C  
ATOM   4287  CD2 LEU C  80      24.339  55.655  79.029  1.00 49.33           C  
ANISOU 4287  CD2 LEU C  80     5043   7581   6121   -158   -485  -2258       C  
ATOM   4288  N   ASP C  81      25.026  60.194  77.492  1.00 48.58           N  
ANISOU 4288  N   ASP C  81     4700   6941   6816   -506   -505  -2595       N  
ATOM   4289  CA  ASP C  81      25.519  61.322  76.712  1.00 49.69           C  
ANISOU 4289  CA  ASP C  81     4761   6896   7222   -635   -502  -2619       C  
ATOM   4290  C   ASP C  81      25.083  61.173  75.259  1.00 49.50           C  
ANISOU 4290  C   ASP C  81     4772   6745   7291   -673   -380  -2400       C  
ATOM   4291  O   ASP C  81      25.085  60.070  74.707  1.00 48.89           O  
ANISOU 4291  O   ASP C  81     4723   6748   7103   -627   -329  -2235       O  
ATOM   4292  CB  ASP C  81      27.045  61.401  76.817  1.00 52.18           C  
ANISOU 4292  CB  ASP C  81     4933   7274   7617   -707   -591  -2687       C  
ATOM   4293  CG  ASP C  81      27.625  62.583  76.064  1.00 57.20           C  
ANISOU 4293  CG  ASP C  81     5473   7720   8541   -862   -587  -2704       C  
ATOM   4294  OD1 ASP C  81      27.798  62.480  74.831  1.00 57.45           O  
ANISOU 4294  OD1 ASP C  81     5482   7675   8674   -921   -494  -2517       O  
ATOM   4295  OD2 ASP C  81      27.913  63.616  76.709  1.00 60.16           O  
ANISOU 4295  OD2 ASP C  81     5798   8019   9041   -926   -679  -2902       O  
ATOM   4296  N   LYS C  82      24.703  62.297  74.642  1.00 51.99           N  
ANISOU 4296  N   LYS C  82     5091   6856   7807   -748   -341  -2402       N  
ATOM   4297  CA  LYS C  82      24.013  62.240  73.355  1.00 51.84           C  
ANISOU 4297  CA  LYS C  82     5128   6718   7849   -756   -227  -2206       C  
ATOM   4298  C   LYS C  82      24.877  61.626  72.261  1.00 52.09           C  
ANISOU 4298  C   LYS C  82     5101   6782   7910   -798   -179  -2029       C  
ATOM   4299  O   LYS C  82      24.348  61.008  71.331  1.00 51.61           O  
ANISOU 4299  O   LYS C  82     5101   6711   7796   -756    -96  -1857       O  
ATOM   4300  CB  LYS C  82      23.554  63.638  72.937  1.00 51.65           C  
ANISOU 4300  CB  LYS C  82     5119   6463   8041   -823   -206  -2244       C  
ATOM   4301  CG  LYS C  82      24.685  64.604  72.640  1.00 54.22           C  
ANISOU 4301  CG  LYS C  82     5337   6667   8598   -965   -243  -2287       C  
ATOM   4302  CD  LYS C  82      24.163  65.996  72.328  1.00 56.95           C  
ANISOU 4302  CD  LYS C  82     5720   6760   9159  -1024   -233  -2328       C  
ATOM   4303  CE  LYS C  82      23.950  66.185  70.834  1.00 58.88           C  
ANISOU 4303  CE  LYS C  82     5989   6868   9515  -1065   -120  -2098       C  
ATOM   4304  NZ  LYS C  82      24.149  67.604  70.425  1.00 61.15           N  
ANISOU 4304  NZ  LYS C  82     6261   6901  10074  -1181   -125  -2114       N  
ATOM   4305  N   ASN C  83      26.196  61.773  72.348  1.00 51.33           N  
ANISOU 4305  N   ASN C  83     4879   6732   7891   -872   -231  -2075       N  
ATOM   4306  CA  ASN C  83      27.088  61.295  71.301  1.00 52.21           C  
ANISOU 4306  CA  ASN C  83     4913   6887   8038   -907   -178  -1916       C  
ATOM   4307  C   ASN C  83      27.613  59.890  71.567  1.00 51.41           C  
ANISOU 4307  C   ASN C  83     4801   6998   7733   -809   -207  -1879       C  
ATOM   4308  O   ASN C  83      28.569  59.465  70.911  1.00 51.38           O  
ANISOU 4308  O   ASN C  83     4708   7068   7744   -823   -186  -1789       O  
ATOM   4309  CB  ASN C  83      28.252  62.271  71.119  1.00 52.59           C  
ANISOU 4309  CB  ASN C  83     4809   6868   8306  -1053   -205  -1965       C  
ATOM   4310  CG  ASN C  83      27.819  63.572  70.468  1.00 54.26           C  
ANISOU 4310  CG  ASN C  83     5039   6836   8740  -1156   -151  -1931       C  
ATOM   4311  OD1 ASN C  83      26.950  63.582  69.596  1.00 55.74           O  
ANISOU 4311  OD1 ASN C  83     5325   6928   8926  -1120    -59  -1788       O  
ATOM   4312  ND2 ASN C  83      28.419  64.677  70.894  1.00 54.95           N  
ANISOU 4312  ND2 ASN C  83     5037   6816   9024  -1282   -218  -2065       N  
ATOM   4313  N   THR C  84      27.008  59.165  72.505  1.00 46.99           N  
ANISOU 4313  N   THR C  84     4331   6540   6983   -705   -252  -1940       N  
ATOM   4314  CA  THR C  84      27.392  57.782  72.751  1.00 46.84           C  
ANISOU 4314  CA  THR C  84     4330   6699   6767   -601   -281  -1887       C  
ATOM   4315  C   THR C  84      27.185  56.945  71.494  1.00 45.10           C  
ANISOU 4315  C   THR C  84     4163   6465   6507   -557   -193  -1686       C  
ATOM   4316  O   THR C  84      26.120  56.989  70.871  1.00 44.67           O  
ANISOU 4316  O   THR C  84     4205   6304   6462   -548   -122  -1595       O  
ATOM   4317  CB  THR C  84      26.581  57.207  73.912  1.00 46.45           C  
ANISOU 4317  CB  THR C  84     4389   6736   6525   -505   -324  -1956       C  
ATOM   4318  OG1 THR C  84      26.717  58.054  75.061  1.00 46.97           O  
ANISOU 4318  OG1 THR C  84     4412   6818   6617   -531   -407  -2158       O  
ATOM   4319  CG2 THR C  84      27.066  55.812  74.263  1.00 44.96           C  
ANISOU 4319  CG2 THR C  84     4225   6717   6141   -399   -368  -1902       C  
ATOM   4320  N   SER C  85      28.214  56.190  71.118  1.00 37.79           N  
ANISOU 4320  N   SER C  85     3170   5652   5535   -519   -206  -1626       N  
ATOM   4321  CA  SER C  85      28.163  55.382  69.910  1.00 38.94           C  
ANISOU 4321  CA  SER C  85     3360   5798   5637   -462   -135  -1455       C  
ATOM   4322  C   SER C  85      27.047  54.345  69.999  1.00 38.05           C  
ANISOU 4322  C   SER C  85     3413   5682   5361   -363   -128  -1386       C  
ATOM   4323  O   SER C  85      26.557  54.006  71.080  1.00 38.37           O  
ANISOU 4323  O   SER C  85     3519   5768   5291   -324   -180  -1455       O  
ATOM   4324  CB  SER C  85      29.503  54.684  69.679  1.00 38.48           C  
ANISOU 4324  CB  SER C  85     3198   5889   5535   -411   -164  -1430       C  
ATOM   4325  OG  SER C  85      29.701  53.649  70.627  1.00 39.48           O  
ANISOU 4325  OG  SER C  85     3369   6146   5484   -303   -252  -1480       O  
ATOM   4326  N   THR C  86      26.648  53.833  68.833  1.00 38.98           N  
ANISOU 4326  N   THR C  86     3596   5750   5464   -324    -63  -1246       N  
ATOM   4327  CA  THR C  86      25.587  52.832  68.795  1.00 38.79           C  
ANISOU 4327  CA  THR C  86     3722   5707   5310   -247    -61  -1175       C  
ATOM   4328  C   THR C  86      26.017  51.546  69.489  1.00 38.40           C  
ANISOU 4328  C   THR C  86     3717   5778   5094   -148   -136  -1179       C  
ATOM   4329  O   THR C  86      25.207  50.893  70.155  1.00 38.65           O  
ANISOU 4329  O   THR C  86     3856   5814   5016   -111   -161  -1171       O  
ATOM   4330  CB  THR C  86      25.180  52.551  67.349  1.00 37.63           C  
ANISOU 4330  CB  THR C  86     3627   5486   5184   -221      7  -1040       C  
ATOM   4331  OG1 THR C  86      24.886  53.788  66.687  1.00 38.65           O  
ANISOU 4331  OG1 THR C  86     3713   5505   5467   -305     75  -1024       O  
ATOM   4332  CG2 THR C  86      23.952  51.655  67.309  1.00 35.08           C  
ANISOU 4332  CG2 THR C  86     3450   5120   4759   -167      1   -980       C  
ATOM   4333  N   LYS C  87      27.290  51.168  69.347  1.00 36.32           N  
ANISOU 4333  N   LYS C  87     3369   5618   4810   -100   -170  -1185       N  
ATOM   4334  CA  LYS C  87      27.788  49.963  70.004  1.00 38.52           C  
ANISOU 4334  CA  LYS C  87     3692   6010   4932     12   -251  -1189       C  
ATOM   4335  C   LYS C  87      27.685  50.075  71.523  1.00 39.44           C  
ANISOU 4335  C   LYS C  87     3816   6194   4974      7   -321  -1296       C  
ATOM   4336  O   LYS C  87      27.280  49.121  72.203  1.00 39.61           O  
ANISOU 4336  O   LYS C  87     3951   6250   4851     81   -364  -1267       O  
ATOM   4337  CB  LYS C  87      29.234  49.705  69.574  1.00 38.33           C  
ANISOU 4337  CB  LYS C  87     3547   6100   4915     69   -275  -1192       C  
ATOM   4338  CG  LYS C  87      29.852  48.435  70.135  1.00 41.10           C  
ANISOU 4338  CG  LYS C  87     3943   6566   5107    210   -365  -1192       C  
ATOM   4339  CD  LYS C  87      31.149  48.092  69.410  1.00 43.82           C  
ANISOU 4339  CD  LYS C  87     4173   7019   5458    289   -371  -1175       C  
ATOM   4340  CE  LYS C  87      32.360  48.223  70.323  1.00 44.25           C  
ANISOU 4340  CE  LYS C  87     4083   7236   5494    314   -456  -1284       C  
ATOM   4341  NZ  LYS C  87      33.618  47.776  69.652  1.00 42.77           N  
ANISOU 4341  NZ  LYS C  87     3775   7177   5299    411   -462  -1265       N  
ATOM   4342  N   ASP C  88      28.034  51.239  72.074  1.00 41.94           N  
ANISOU 4342  N   ASP C  88     4020   6527   5388    -79   -334  -1418       N  
ATOM   4343  CA  ASP C  88      27.959  51.416  73.521  1.00 40.84           C  
ANISOU 4343  CA  ASP C  88     3885   6466   5166    -70   -406  -1539       C  
ATOM   4344  C   ASP C  88      26.513  51.480  73.998  1.00 39.87           C  
ANISOU 4344  C   ASP C  88     3885   6274   4990    -85   -367  -1526       C  
ATOM   4345  O   ASP C  88      26.190  50.983  75.084  1.00 40.55           O  
ANISOU 4345  O   ASP C  88     4039   6441   4926    -28   -411  -1552       O  
ATOM   4346  CB  ASP C  88      28.729  52.668  73.935  1.00 41.86           C  
ANISOU 4346  CB  ASP C  88     3859   6621   5426   -159   -443  -1693       C  
ATOM   4347  CG  ASP C  88      30.228  52.446  73.956  1.00 45.36           C  
ANISOU 4347  CG  ASP C  88     4163   7197   5876   -127   -512  -1735       C  
ATOM   4348  OD1 ASP C  88      30.660  51.293  73.749  1.00 47.37           O  
ANISOU 4348  OD1 ASP C  88     4453   7533   6013    -15   -535  -1654       O  
ATOM   4349  OD2 ASP C  88      30.974  53.422  74.179  1.00 45.95           O  
ANISOU 4349  OD2 ASP C  88     4089   7291   6079   -214   -548  -1854       O  
ATOM   4350  N   GLN C  89      25.627  52.087  73.204  1.00 40.55           N  
ANISOU 4350  N   GLN C  89     3996   6223   5190   -155   -284  -1479       N  
ATOM   4351  CA  GLN C  89      24.202  52.032  73.518  1.00 40.13           C  
ANISOU 4351  CA  GLN C  89     4049   6115   5085   -160   -240  -1449       C  
ATOM   4352  C   GLN C  89      23.706  50.592  73.531  1.00 39.75           C  
ANISOU 4352  C   GLN C  89     4125   6092   4886    -84   -243  -1321       C  
ATOM   4353  O   GLN C  89      22.889  50.212  74.378  1.00 38.06           O  
ANISOU 4353  O   GLN C  89     3986   5914   4560    -64   -242  -1310       O  
ATOM   4354  CB  GLN C  89      23.403  52.860  72.509  1.00 39.38           C  
ANISOU 4354  CB  GLN C  89     3953   5870   5141   -232   -157  -1410       C  
ATOM   4355  CG  GLN C  89      23.746  54.343  72.486  1.00 39.80           C  
ANISOU 4355  CG  GLN C  89     3903   5857   5361   -316   -151  -1523       C  
ATOM   4356  CD  GLN C  89      22.791  55.145  71.623  1.00 39.46           C  
ANISOU 4356  CD  GLN C  89     3884   5662   5448   -368    -73  -1478       C  
ATOM   4357  OE1 GLN C  89      21.574  55.013  71.740  1.00 39.80           O  
ANISOU 4357  OE1 GLN C  89     4003   5674   5444   -348    -38  -1449       O  
ATOM   4358  NE2 GLN C  89      23.340  55.978  70.744  1.00 38.06           N  
ANISOU 4358  NE2 GLN C  89     3634   5395   5433   -432    -43  -1463       N  
ATOM   4359  N   PHE C  90      24.196  49.779  72.594  1.00 36.41           N  
ANISOU 4359  N   PHE C  90     3724   5648   4461    -41   -248  -1222       N  
ATOM   4360  CA  PHE C  90      23.842  48.365  72.554  1.00 34.93           C  
ANISOU 4360  CA  PHE C  90     3662   5462   4149     32   -268  -1107       C  
ATOM   4361  C   PHE C  90      24.300  47.654  73.818  1.00 37.00           C  
ANISOU 4361  C   PHE C  90     3960   5847   4252    106   -344  -1131       C  
ATOM   4362  O   PHE C  90      23.551  46.863  74.402  1.00 37.22           O  
ANISOU 4362  O   PHE C  90     4097   5878   4167    130   -347  -1059       O  
ATOM   4363  CB  PHE C  90      24.457  47.728  71.305  1.00 35.39           C  
ANISOU 4363  CB  PHE C  90     3729   5481   4237     84   -272  -1028       C  
ATOM   4364  CG  PHE C  90      24.551  46.229  71.355  1.00 35.04           C  
ANISOU 4364  CG  PHE C  90     3803   5446   4065    184   -329   -940       C  
ATOM   4365  CD1 PHE C  90      23.480  45.443  70.966  1.00 35.09           C  
ANISOU 4365  CD1 PHE C  90     3936   5350   4046    180   -314   -838       C  
ATOM   4366  CD2 PHE C  90      25.723  45.606  71.758  1.00 35.27           C  
ANISOU 4366  CD2 PHE C  90     3813   5578   4010    283   -404   -961       C  
ATOM   4367  CE1 PHE C  90      23.566  44.063  70.999  1.00 34.91           C  
ANISOU 4367  CE1 PHE C  90     4034   5307   3925    265   -375   -757       C  
ATOM   4368  CE2 PHE C  90      25.816  44.227  71.795  1.00 36.18           C  
ANISOU 4368  CE2 PHE C  90     4051   5681   4015    386   -464   -879       C  
ATOM   4369  CZ  PHE C  90      24.736  43.454  71.414  1.00 35.33           C  
ANISOU 4369  CZ  PHE C  90     4083   5450   3891    374   -449   -775       C  
ATOM   4370  N   TYR C  91      25.528  47.932  74.259  1.00 40.28           N  
ANISOU 4370  N   TYR C  91     4277   6369   4657    141   -406  -1226       N  
ATOM   4371  CA  TYR C  91      26.029  47.302  75.478  1.00 42.09           C  
ANISOU 4371  CA  TYR C  91     4536   6731   4724    228   -489  -1255       C  
ATOM   4372  C   TYR C  91      25.233  47.743  76.702  1.00 42.83           C  
ANISOU 4372  C   TYR C  91     4658   6878   4737    202   -479  -1315       C  
ATOM   4373  O   TYR C  91      24.952  46.933  77.591  1.00 43.22           O  
ANISOU 4373  O   TYR C  91     4803   6995   4622    266   -507  -1261       O  
ATOM   4374  CB  TYR C  91      27.513  47.608  75.659  1.00 42.09           C  
ANISOU 4374  CB  TYR C  91     4402   6848   4743    269   -565  -1361       C  
ATOM   4375  CG  TYR C  91      28.398  46.763  74.777  1.00 43.73           C  
ANISOU 4375  CG  TYR C  91     4601   7062   4952    353   -592  -1289       C  
ATOM   4376  CD1 TYR C  91      28.129  45.413  74.583  1.00 43.91           C  
ANISOU 4376  CD1 TYR C  91     4771   7047   4868    448   -611  -1162       C  
ATOM   4377  CD2 TYR C  91      29.497  47.313  74.131  1.00 44.87           C  
ANISOU 4377  CD2 TYR C  91     4589   7250   5208    339   -597  -1348       C  
ATOM   4378  CE1 TYR C  91      28.932  44.635  73.777  1.00 44.41           C  
ANISOU 4378  CE1 TYR C  91     4834   7116   4925    546   -642  -1112       C  
ATOM   4379  CE2 TYR C  91      30.305  46.543  73.322  1.00 45.45           C  
ANISOU 4379  CE2 TYR C  91     4646   7352   5270    433   -614  -1288       C  
ATOM   4380  CZ  TYR C  91      30.017  45.206  73.148  1.00 45.68           C  
ANISOU 4380  CZ  TYR C  91     4831   7343   5181    546   -640  -1178       C  
ATOM   4381  OH  TYR C  91      30.821  44.439  72.343  1.00 46.60           O  
ANISOU 4381  OH  TYR C  91     4938   7487   5281    660   -663  -1133       O  
ATOM   4382  N   GLU C  92      24.849  49.020  76.760  1.00 45.82           N  
ANISOU 4382  N   GLU C  92     4960   7225   5224    115   -438  -1421       N  
ATOM   4383  CA  GLU C  92      24.047  49.507  77.881  1.00 47.54           C  
ANISOU 4383  CA  GLU C  92     5201   7501   5362    104   -423  -1494       C  
ATOM   4384  C   GLU C  92      22.678  48.828  77.914  1.00 47.57           C  
ANISOU 4384  C   GLU C  92     5324   7458   5290     97   -349  -1356       C  
ATOM   4385  O   GLU C  92      22.230  48.341  78.965  1.00 47.65           O  
ANISOU 4385  O   GLU C  92     5401   7566   5136    144   -352  -1329       O  
ATOM   4386  CB  GLU C  92      23.901  51.027  77.784  1.00 47.89           C  
ANISOU 4386  CB  GLU C  92     5145   7490   5560     19   -398  -1640       C  
ATOM   4387  CG  GLU C  92      23.206  51.680  78.965  1.00 50.32           C  
ANISOU 4387  CG  GLU C  92     5461   7870   5788     28   -394  -1756       C  
ATOM   4388  CD  GLU C  92      23.946  51.472  80.271  1.00 52.67           C  
ANISOU 4388  CD  GLU C  92     5747   8347   5918    114   -491  -1858       C  
ATOM   4389  OE1 GLU C  92      25.190  51.354  80.244  1.00 53.24           O  
ANISOU 4389  OE1 GLU C  92     5751   8473   6006    138   -577  -1907       O  
ATOM   4390  OE2 GLU C  92      23.283  51.428  81.327  1.00 54.58           O  
ANISOU 4390  OE2 GLU C  92     6042   8690   6006    164   -481  -1888       O  
ATOM   4391  N   LEU C  93      22.000  48.789  76.762  1.00 42.02           N  
ANISOU 4391  N   LEU C  93     4645   6616   4706     38   -282  -1265       N  
ATOM   4392  CA  LEU C  93      20.716  48.102  76.671  1.00 43.45           C  
ANISOU 4392  CA  LEU C  93     4923   6746   4841     17   -220  -1133       C  
ATOM   4393  C   LEU C  93      20.843  46.640  77.076  1.00 44.56           C  
ANISOU 4393  C   LEU C  93     5174   6925   4831     82   -260  -1002       C  
ATOM   4394  O   LEU C  93      19.999  46.117  77.814  1.00 45.53           O  
ANISOU 4394  O   LEU C  93     5367   7089   4841     81   -228   -924       O  
ATOM   4395  CB  LEU C  93      20.159  48.216  75.251  1.00 43.18           C  
ANISOU 4395  CB  LEU C  93     4890   6558   4957    -42   -168  -1064       C  
ATOM   4396  CG  LEU C  93      19.005  49.195  75.027  1.00 44.11           C  
ANISOU 4396  CG  LEU C  93     4972   6617   5172   -111    -90  -1100       C  
ATOM   4397  CD1 LEU C  93      18.496  49.098  73.601  1.00 41.29           C  
ANISOU 4397  CD1 LEU C  93     4630   6120   4937   -150    -54  -1014       C  
ATOM   4398  CD2 LEU C  93      17.880  48.936  76.018  1.00 43.46           C  
ANISOU 4398  CD2 LEU C  93     4930   6609   4975   -115    -46  -1068       C  
ATOM   4399  N   ASN C  94      21.893  45.964  76.604  1.00 42.37           N  
ANISOU 4399  N   ASN C  94     4914   6635   4550    143   -328   -972       N  
ATOM   4400  CA  ASN C  94      22.104  44.570  76.978  1.00 42.88           C  
ANISOU 4400  CA  ASN C  94     5096   6717   4479    220   -381   -851       C  
ATOM   4401  C   ASN C  94      22.326  44.430  78.478  1.00 43.77           C  
ANISOU 4401  C   ASN C  94     5229   6987   4413    283   -417   -878       C  
ATOM   4402  O   ASN C  94      21.863  43.463  79.095  1.00 45.27           O  
ANISOU 4402  O   ASN C  94     5532   7193   4473    312   -417   -752       O  
ATOM   4403  CB  ASN C  94      23.292  43.996  76.207  1.00 42.13           C  
ANISOU 4403  CB  ASN C  94     5000   6595   4413    299   -453   -842       C  
ATOM   4404  CG  ASN C  94      23.614  42.575  76.612  1.00 43.80           C  
ANISOU 4404  CG  ASN C  94     5341   6813   4488    400   -523   -729       C  
ATOM   4405  OD1 ASN C  94      22.812  41.662  76.410  1.00 44.12           O  
ANISOU 4405  OD1 ASN C  94     5504   6749   4510    381   -508   -595       O  
ATOM   4406  ND2 ASN C  94      24.788  42.380  77.201  1.00 42.81           N  
ANISOU 4406  ND2 ASN C  94     5188   6807   4273    507   -608   -784       N  
ATOM   4407  N   ARG C  95      23.031  45.388  79.081  1.00 45.94           N  
ANISOU 4407  N   ARG C  95     5398   7379   4678    305   -452  -1041       N  
ATOM   4408  CA  ARG C  95      23.287  45.326  80.515  1.00 45.83           C  
ANISOU 4408  CA  ARG C  95     5399   7535   4480    381   -499  -1088       C  
ATOM   4409  C   ARG C  95      21.996  45.454  81.313  1.00 48.52           C  
ANISOU 4409  C   ARG C  95     5787   7921   4727    343   -415  -1045       C  
ATOM   4410  O   ARG C  95      21.815  44.768  82.326  1.00 50.20           O  
ANISOU 4410  O   ARG C  95     6083   8238   4751    407   -423   -966       O  
ATOM   4411  CB  ARG C  95      24.280  46.417  80.919  1.00 44.34           C  
ANISOU 4411  CB  ARG C  95     5074   7452   4323    400   -565  -1296       C  
ATOM   4412  CG  ARG C  95      24.786  46.298  82.347  1.00 48.01           C  
ANISOU 4412  CG  ARG C  95     5548   8110   4585    505   -644  -1366       C  
ATOM   4413  CD  ARG C  95      25.640  47.496  82.734  1.00 49.28           C  
ANISOU 4413  CD  ARG C  95     5564   8361   4801    503   -716  -1596       C  
ATOM   4414  NE  ARG C  95      24.870  48.736  82.745  1.00 49.85           N  
ANISOU 4414  NE  ARG C  95     5577   8388   4976    411   -650  -1714       N  
ATOM   4415  CZ  ARG C  95      24.100  49.131  83.755  1.00 51.14           C  
ANISOU 4415  CZ  ARG C  95     5768   8645   5017    432   -621  -1773       C  
ATOM   4416  NH1 ARG C  95      23.994  48.383  84.845  1.00 51.34           N  
ANISOU 4416  NH1 ARG C  95     5880   8823   4804    535   -643  -1713       N  
ATOM   4417  NH2 ARG C  95      23.434  50.277  83.675  1.00 49.89           N  
ANISOU 4417  NH2 ARG C  95     5556   8432   4968    361   -566  -1889       N  
ATOM   4418  N   ARG C  96      21.080  46.320  80.872  1.00 42.86           N  
ANISOU 4418  N   ARG C  96     5018   7134   4132    249   -329  -1089       N  
ATOM   4419  CA  ARG C  96      19.844  46.509  81.630  1.00 44.52           C  
ANISOU 4419  CA  ARG C  96     5250   7410   4254    223   -242  -1061       C  
ATOM   4420  C   ARG C  96      18.761  45.484  81.311  1.00 44.55           C  
ANISOU 4420  C   ARG C  96     5349   7333   4243    170   -169   -850       C  
ATOM   4421  O   ARG C  96      17.783  45.397  82.062  1.00 45.08           O  
ANISOU 4421  O   ARG C  96     5438   7483   4206    155    -94   -791       O  
ATOM   4422  CB  ARG C  96      19.272  47.904  81.384  1.00 44.33           C  
ANISOU 4422  CB  ARG C  96     5127   7356   4362    160   -186  -1206       C  
ATOM   4423  CG  ARG C  96      20.216  49.037  81.695  1.00 43.80           C  
ANISOU 4423  CG  ARG C  96     4962   7342   4340    188   -258  -1424       C  
ATOM   4424  CD  ARG C  96      19.552  50.358  81.376  1.00 44.11           C  
ANISOU 4424  CD  ARG C  96     4924   7312   4524    126   -202  -1549       C  
ATOM   4425  NE  ARG C  96      20.515  51.447  81.288  1.00 44.79           N  
ANISOU 4425  NE  ARG C  96     4914   7376   4727    116   -275  -1740       N  
ATOM   4426  CZ  ARG C  96      20.190  52.704  81.011  1.00 43.82           C  
ANISOU 4426  CZ  ARG C  96     4725   7170   4753     67   -252  -1870       C  
ATOM   4427  NH1 ARG C  96      18.922  53.028  80.795  1.00 44.08           N  
ANISOU 4427  NH1 ARG C  96     4774   7150   4823     39   -158  -1835       N  
ATOM   4428  NH2 ARG C  96      21.131  53.635  80.944  1.00 42.05           N  
ANISOU 4428  NH2 ARG C  96     4417   6913   4648     44   -326  -2032       N  
ATOM   4429  N   TRP C  97      18.928  44.693  80.249  1.00 36.14           N  
ANISOU 4429  N   TRP C  97     4338   6118   3276    143   -193   -741       N  
ATOM   4430  CA  TRP C  97      17.797  44.002  79.631  1.00 38.19           C  
ANISOU 4430  CA  TRP C  97     4659   6257   3596     60   -129   -582       C  
ATOM   4431  C   TRP C  97      17.099  43.040  80.590  1.00 40.01           C  
ANISOU 4431  C   TRP C  97     4981   6554   3666     58    -90   -419       C  
ATOM   4432  O   TRP C  97      15.867  42.933  80.579  1.00 42.78           O  
ANISOU 4432  O   TRP C  97     5330   6885   4038    -27     -2   -329       O  
ATOM   4433  CB  TRP C  97      18.278  43.262  78.382  1.00 38.00           C  
ANISOU 4433  CB  TRP C  97     4687   6067   3683     58   -187   -516       C  
ATOM   4434  CG  TRP C  97      17.192  42.845  77.435  1.00 37.96           C  
ANISOU 4434  CG  TRP C  97     4715   5915   3793    -37   -140   -409       C  
ATOM   4435  CD1 TRP C  97      16.554  41.640  77.399  1.00 39.89           C  
ANISOU 4435  CD1 TRP C  97     5066   6078   4011    -75   -139   -239       C  
ATOM   4436  CD2 TRP C  97      16.634  43.625  76.369  1.00 35.69           C  
ANISOU 4436  CD2 TRP C  97     4352   5538   3669   -104    -97   -466       C  
ATOM   4437  NE1 TRP C  97      15.629  41.622  76.384  1.00 38.60           N  
ANISOU 4437  NE1 TRP C  97     4890   5788   3987   -165   -106   -201       N  
ATOM   4438  CE2 TRP C  97      15.657  42.829  75.737  1.00 36.87           C  
ANISOU 4438  CE2 TRP C  97     4562   5570   3878   -176    -79   -337       C  
ATOM   4439  CE3 TRP C  97      16.862  44.919  75.891  1.00 32.95           C  
ANISOU 4439  CE3 TRP C  97     3898   5194   3428   -111    -78   -609       C  
ATOM   4440  CZ2 TRP C  97      14.911  43.285  74.652  1.00 35.60           C  
ANISOU 4440  CZ2 TRP C  97     4352   5313   3862   -240    -47   -354       C  
ATOM   4441  CZ3 TRP C  97      16.118  45.370  74.816  1.00 33.27           C  
ANISOU 4441  CZ3 TRP C  97     3901   5129   3612   -173    -37   -610       C  
ATOM   4442  CH2 TRP C  97      15.155  44.554  74.208  1.00 34.16           C  
ANISOU 4442  CH2 TRP C  97     4070   5143   3765   -230    -24   -487       C  
ATOM   4443  N   ASP C  98      17.858  42.329  81.421  1.00 48.10           N  
ANISOU 4443  N   ASP C  98     6084   7662   4530    151   -153   -369       N  
ATOM   4444  CA  ASP C  98      17.303  41.252  82.233  1.00 52.43           C  
ANISOU 4444  CA  ASP C  98     6744   8248   4931    151   -122   -175       C  
ATOM   4445  C   ASP C  98      17.033  41.652  83.680  1.00 52.94           C  
ANISOU 4445  C   ASP C  98     6786   8536   4793    201    -69   -197       C  
ATOM   4446  O   ASP C  98      16.666  40.789  84.484  1.00 55.22           O  
ANISOU 4446  O   ASP C  98     7167   8885   4930    213    -38    -26       O  
ATOM   4447  CB  ASP C  98      18.233  40.038  82.206  1.00 54.48           C  
ANISOU 4447  CB  ASP C  98     7132   8440   5129    235   -227    -68       C  
ATOM   4448  CG  ASP C  98      18.086  39.218  80.941  1.00 56.32           C  
ANISOU 4448  CG  ASP C  98     7433   8444   5520    178   -260     27       C  
ATOM   4449  OD1 ASP C  98      17.011  39.282  80.309  1.00 56.36           O  
ANISOU 4449  OD1 ASP C  98     7415   8352   5648     56   -190     75       O  
ATOM   4450  OD2 ASP C  98      19.045  38.504  80.581  1.00 56.85           O  
ANISOU 4450  OD2 ASP C  98     7576   8437   5587    265   -361     46       O  
ATOM   4451  N   LYS C  99      17.197  42.928  84.028  1.00 54.38           N  
ANISOU 4451  N   LYS C  99     6855   8839   4968    233    -59   -401       N  
ATOM   4452  CA  LYS C  99      17.024  43.353  85.412  1.00 57.21           C  
ANISOU 4452  CA  LYS C  99     7194   9424   5118    306    -23   -454       C  
ATOM   4453  C   LYS C  99      15.623  43.017  85.912  1.00 58.32           C  
ANISOU 4453  C   LYS C  99     7352   9628   5179    240    114   -294       C  
ATOM   4454  O   LYS C  99      14.625  43.302  85.244  1.00 57.68           O  
ANISOU 4454  O   LYS C  99     7212   9463   5241    132    197   -273       O  
ATOM   4455  CB  LYS C  99      17.292  44.853  85.544  1.00 58.52           C  
ANISOU 4455  CB  LYS C  99     7234   9670   5332    336    -38   -718       C  
ATOM   4456  CG  LYS C  99      18.764  45.227  85.436  1.00 59.48           C  
ANISOU 4456  CG  LYS C  99     7322   9795   5484    412   -174   -882       C  
ATOM   4457  CD  LYS C  99      19.031  46.618  85.989  1.00 60.45           C  
ANISOU 4457  CD  LYS C  99     7337  10033   5598    454   -200  -1137       C  
ATOM   4458  CE  LYS C  99      20.477  46.760  86.442  1.00 61.17           C  
ANISOU 4458  CE  LYS C  99     7405  10212   5624    554   -343  -1276       C  
ATOM   4459  NZ  LYS C  99      20.609  47.695  87.595  1.00 61.77           N  
ANISOU 4459  NZ  LYS C  99     7428  10479   5565    636   -377  -1480       N  
ATOM   4460  N   PHE C 100      15.559  42.397  87.096  1.00 56.10           N  
ANISOU 4460  N   PHE C 100     7145   9507   4662    308    139   -173       N  
ATOM   4461  CA  PHE C 100      14.315  41.916  87.680  1.00 59.57           C  
ANISOU 4461  CA  PHE C 100     7604  10030   4999    246    276     17       C  
ATOM   4462  C   PHE C 100      14.552  41.692  89.162  1.00 62.87           C  
ANISOU 4462  C   PHE C 100     8079  10692   5119    373    289     64       C  
ATOM   4463  O   PHE C 100      15.634  41.214  89.532  1.00 64.12           O  
ANISOU 4463  O   PHE C 100     8323  10873   5168    481    177     70       O  
ATOM   4464  CB  PHE C 100      13.856  40.617  87.000  1.00 60.31           C  
ANISOU 4464  CB  PHE C 100     7793   9926   5196    129    292    272       C  
ATOM   4465  CG  PHE C 100      12.636  39.991  87.625  1.00 62.04           C  
ANISOU 4465  CG  PHE C 100     8031  10224   5318     47    431    500       C  
ATOM   4466  CD1 PHE C 100      11.366  40.327  87.184  1.00 62.64           C  
ANISOU 4466  CD1 PHE C 100     8002  10279   5520    -83    548    526       C  
ATOM   4467  CD2 PHE C 100      12.760  39.057  88.642  1.00 62.96           C  
ANISOU 4467  CD2 PHE C 100     8264  10439   5220     99    447    700       C  
ATOM   4468  CE1 PHE C 100      10.243  39.752  87.752  1.00 64.60           C  
ANISOU 4468  CE1 PHE C 100     8244  10614   5688   -170    683    742       C  
ATOM   4469  CE2 PHE C 100      11.641  38.480  89.215  1.00 65.49           C  
ANISOU 4469  CE2 PHE C 100     8592  10835   5454     10    588    930       C  
ATOM   4470  CZ  PHE C 100      10.381  38.828  88.769  1.00 66.32           C  
ANISOU 4470  CZ  PHE C 100     8575  10928   5694   -130    708    950       C  
ATOM   4471  N   PRO C 101      13.585  42.013  90.038  1.00 76.55           N  
ANISOU 4471  N   PRO C 101     9762  12624   6700    379    421     98       N  
ATOM   4472  CA  PRO C 101      12.290  42.605  89.693  1.00 76.75           C  
ANISOU 4472  CA  PRO C 101     9670  12655   6836    273    555     84       C  
ATOM   4473  C   PRO C 101      12.259  44.127  89.801  1.00 74.73           C  
ANISOU 4473  C   PRO C 101     9287  12502   6603    340    556   -212       C  
ATOM   4474  O   PRO C 101      12.855  44.699  90.715  1.00 75.19           O  
ANISOU 4474  O   PRO C 101     9342  12741   6485    480    509   -370       O  
ATOM   4475  CB  PRO C 101      11.352  41.975  90.721  1.00 78.25           C  
ANISOU 4475  CB  PRO C 101     9885  13033   6814    263    700    309       C  
ATOM   4476  CG  PRO C 101      12.212  41.825  91.939  1.00 78.25           C  
ANISOU 4476  CG  PRO C 101     9969  13233   6528    434    644    293       C  
ATOM   4477  CD  PRO C 101      13.634  41.606  91.455  1.00 77.24           C  
ANISOU 4477  CD  PRO C 101     9919  12954   6475    494    458    202       C  
ATOM   4478  N   VAL C 102      11.579  44.772  88.859  1.00 64.94           N  
ANISOU 4478  N   VAL C 102     7949  11139   5585    245    598   -290       N  
ATOM   4479  CA  VAL C 102      11.287  46.201  88.951  1.00 62.25           C  
ANISOU 4479  CA  VAL C 102     7492  10881   5281    298    621   -543       C  
ATOM   4480  C   VAL C 102       9.785  46.386  88.769  1.00 62.09           C  
ANISOU 4480  C   VAL C 102     7375  10898   5317    216    774   -468       C  
ATOM   4481  O   VAL C 102       9.346  46.855  87.709  1.00 61.38           O  
ANISOU 4481  O   VAL C 102     7216  10648   5457    134    778   -524       O  
ATOM   4482  CB  VAL C 102      12.073  47.018  87.914  1.00 60.24           C  
ANISOU 4482  CB  VAL C 102     7201  10430   5259    284    503   -748       C  
ATOM   4483  CG1 VAL C 102      12.171  48.471  88.358  1.00 57.96           C  
ANISOU 4483  CG1 VAL C 102     6828  10242   4953    380    484  -1033       C  
ATOM   4484  CG2 VAL C 102      13.459  46.431  87.695  1.00 60.57           C  
ANISOU 4484  CG2 VAL C 102     7331  10376   5308    312    361   -737       C  
ATOM   4485  N   PRO C 103       8.967  46.036  89.757  1.00 56.86           N  
ANISOU 4485  N   PRO C 103     6699  10456   4450    239    903   -337       N  
ATOM   4486  CA  PRO C 103       7.514  46.152  89.596  1.00 56.42           C  
ANISOU 4486  CA  PRO C 103     6531  10458   4449    158   1055   -252       C  
ATOM   4487  C   PRO C 103       7.095  47.605  89.482  1.00 55.78           C  
ANISOU 4487  C   PRO C 103     6328  10429   4438    230   1074   -517       C  
ATOM   4488  O   PRO C 103       7.681  48.484  90.134  1.00 55.14           O  
ANISOU 4488  O   PRO C 103     6247  10458   4245    374   1019   -742       O  
ATOM   4489  CB  PRO C 103       6.964  45.509  90.879  1.00 56.55           C  
ANISOU 4489  CB  PRO C 103     6562  10741   4185    197   1185    -66       C  
ATOM   4490  CG  PRO C 103       8.060  45.666  91.873  1.00 55.97           C  
ANISOU 4490  CG  PRO C 103     6578  10809   3880    364   1099   -177       C  
ATOM   4491  CD  PRO C 103       9.337  45.536  91.094  1.00 56.62           C  
ANISOU 4491  CD  PRO C 103     6745  10650   4116    351    918   -257       C  
ATOM   4492  N   PRO C 104       6.093  47.902  88.659  1.00 56.76           N  
ANISOU 4492  N   PRO C 104     6349  10469   4750    139   1141   -505       N  
ATOM   4493  CA  PRO C 104       5.643  49.289  88.515  1.00 55.53           C  
ANISOU 4493  CA  PRO C 104     6084  10346   4669    219   1157   -749       C  
ATOM   4494  C   PRO C 104       4.908  49.768  89.757  1.00 56.43           C  
ANISOU 4494  C   PRO C 104     6122  10773   4546    346   1281   -810       C  
ATOM   4495  O   PRO C 104       4.433  48.983  90.580  1.00 57.28           O  
ANISOU 4495  O   PRO C 104     6231  11078   4456    340   1393   -617       O  
ATOM   4496  CB  PRO C 104       4.708  49.234  87.303  1.00 54.08           C  
ANISOU 4496  CB  PRO C 104     5815  10000   4731     85   1197   -670       C  
ATOM   4497  CG  PRO C 104       4.207  47.829  87.286  1.00 56.29           C  
ANISOU 4497  CG  PRO C 104     6118  10284   4984    -54   1267   -367       C  
ATOM   4498  CD  PRO C 104       5.343  46.978  87.791  1.00 58.02           C  
ANISOU 4498  CD  PRO C 104     6489  10486   5069    -36   1189   -274       C  
ATOM   4499  N   ASN C 105       4.821  51.090  89.880  1.00 65.17           N  
ANISOU 4499  N   ASN C 105     7166  11921   5674    469   1261  -1081       N  
ATOM   4500  CA  ASN C 105       4.149  51.737  91.001  1.00 66.15           C  
ANISOU 4500  CA  ASN C 105     7215  12339   5579    624   1365  -1195       C  
ATOM   4501  C   ASN C 105       2.743  52.134  90.564  1.00 63.75           C  
ANISOU 4501  C   ASN C 105     6760  12077   5385    597   1491  -1179       C  
ATOM   4502  O   ASN C 105       2.576  52.989  89.688  1.00 62.09           O  
ANISOU 4502  O   ASN C 105     6503  11693   5395    595   1438  -1331       O  
ATOM   4503  CB  ASN C 105       4.937  52.954  91.480  1.00 67.94           C  
ANISOU 4503  CB  ASN C 105     7472  12584   5756    794   1251  -1526       C  
ATOM   4504  CG  ASN C 105       6.041  52.589  92.454  1.00 70.93           C  
ANISOU 4504  CG  ASN C 105     7964  13074   5911    878   1168  -1549       C  
ATOM   4505  OD1 ASN C 105       5.926  51.619  93.204  1.00 73.77           O  
ANISOU 4505  OD1 ASN C 105     8366  13588   6075    873   1235  -1333       O  
ATOM   4506  ND2 ASN C 105       7.118  53.368  92.449  1.00 70.28           N  
ANISOU 4506  ND2 ASN C 105     7935  12878   5891    947   1004  -1793       N  
ATOM   4507  N   VAL C 106       1.738  51.509  91.170  1.00 63.42           N  
ANISOU 4507  N   VAL C 106     6639  12270   5189    576   1658   -986       N  
ATOM   4508  CA  VAL C 106       0.347  51.863  90.914  1.00 64.39           C  
ANISOU 4508  CA  VAL C 106     6608  12443   5414    559   1768   -958       C  
ATOM   4509  C   VAL C 106       0.006  53.090  91.750  1.00 65.52           C  
ANISOU 4509  C   VAL C 106     6723  12687   5486    761   1754  -1187       C  
ATOM   4510  O   VAL C 106       0.038  53.041  92.983  1.00 67.99           O  
ANISOU 4510  O   VAL C 106     7073  13178   5581    867   1779  -1177       O  
ATOM   4511  CB  VAL C 106      -0.592  50.691  91.237  1.00 67.37           C  
ANISOU 4511  CB  VAL C 106     6923  12954   5720    432   1918   -635       C  
ATOM   4512  CG1 VAL C 106      -2.033  51.063  90.926  1.00 64.67           C  
ANISOU 4512  CG1 VAL C 106     6410  12658   5504    410   2017   -614       C  
ATOM   4513  CG2 VAL C 106      -0.181  49.445  90.461  1.00 68.21           C  
ANISOU 4513  CG2 VAL C 106     7092  12904   5920    227   1896   -399       C  
ATOM   4514  N   VAL C 107      -0.316  54.193  91.084  1.00 56.46           N  
ANISOU 4514  N   VAL C 107     5513  11421   4518    818   1707  -1392       N  
ATOM   4515  CA  VAL C 107      -0.617  55.448  91.761  1.00 58.16           C  
ANISOU 4515  CA  VAL C 107     5711  11696   4692   1010   1674  -1627       C  
ATOM   4516  C   VAL C 107      -2.121  55.670  91.765  1.00 59.68           C  
ANISOU 4516  C   VAL C 107     5754  12002   4921   1030   1798  -1564       C  
ATOM   4517  O   VAL C 107      -2.854  55.144  90.917  1.00 58.82           O  
ANISOU 4517  O   VAL C 107     5547  11853   4948    894   1871  -1404       O  
ATOM   4518  CB  VAL C 107       0.118  56.632  91.099  1.00 56.60           C  
ANISOU 4518  CB  VAL C 107     5565  11267   4673   1077   1520  -1910       C  
ATOM   4519  CG1 VAL C 107       1.601  56.334  90.984  1.00 55.07           C  
ANISOU 4519  CG1 VAL C 107     5501  10956   4467   1033   1398  -1958       C  
ATOM   4520  CG2 VAL C 107      -0.476  56.932  89.732  1.00 54.84           C  
ANISOU 4520  CG2 VAL C 107     5257  10873   4708    998   1531  -1914       C  
ATOM   4521  N   LYS C 108      -2.587  56.448  92.741  1.00 68.62           N  
ANISOU 4521  N   LYS C 108     6863  13281   5928   1204   1815  -1695       N  
ATOM   4522  CA  LYS C 108      -3.992  56.816  92.803  1.00 69.35           C  
ANISOU 4522  CA  LYS C 108     6812  13492   6047   1255   1921  -1673       C  
ATOM   4523  C   LYS C 108      -4.369  57.664  91.592  1.00 67.28           C  
ANISOU 4523  C   LYS C 108     6491  13027   6044   1257   1863  -1808       C  
ATOM   4524  O   LYS C 108      -3.516  58.256  90.924  1.00 65.33           O  
ANISOU 4524  O   LYS C 108     6327  12561   5936   1265   1733  -1972       O  
ATOM   4525  CB  LYS C 108      -4.290  57.574  94.097  1.00 72.50           C  
ANISOU 4525  CB  LYS C 108     7211  14083   6253   1463   1932  -1818       C  
ATOM   4526  CG  LYS C 108      -4.106  56.743  95.359  1.00 76.49           C  
ANISOU 4526  CG  LYS C 108     7758  14819   6487   1478   2006  -1668       C  
ATOM   4527  CD  LYS C 108      -3.521  57.575  96.491  1.00 78.92           C  
ANISOU 4527  CD  LYS C 108     8153  15213   6620   1685   1916  -1895       C  
ATOM   4528  CE  LYS C 108      -2.864  56.699  97.548  1.00 80.30           C  
ANISOU 4528  CE  LYS C 108     8416  15546   6548   1687   1936  -1762       C  
ATOM   4529  NZ  LYS C 108      -1.949  57.474  98.435  1.00 80.44           N  
ANISOU 4529  NZ  LYS C 108     8542  15584   6438   1863   1797  -2006       N  
ATOM   4530  N   ARG C 109      -5.674  57.726  91.315  1.00 67.08           N  
ANISOU 4530  N   ARG C 109     6319  13081   6088   1250   1961  -1732       N  
ATOM   4531  CA  ARG C 109      -6.131  58.343  90.073  1.00 65.41           C  
ANISOU 4531  CA  ARG C 109     6042  12686   6126   1235   1916  -1810       C  
ATOM   4532  C   ARG C 109      -5.788  59.828  90.018  1.00 65.63           C  
ANISOU 4532  C   ARG C 109     6138  12571   6226   1416   1789  -2111       C  
ATOM   4533  O   ARG C 109      -5.348  60.328  88.976  1.00 64.46           O  
ANISOU 4533  O   ARG C 109     6032  12180   6281   1391   1690  -2212       O  
ATOM   4534  CB  ARG C 109      -7.635  58.139  89.896  1.00 65.34           C  
ANISOU 4534  CB  ARG C 109     5854  12811   6161   1208   2038  -1676       C  
ATOM   4535  CG  ARG C 109      -8.141  58.652  88.561  1.00 63.83           C  
ANISOU 4535  CG  ARG C 109     5590  12437   6225   1186   1988  -1730       C  
ATOM   4536  CD  ARG C 109      -9.652  58.612  88.462  1.00 65.98           C  
ANISOU 4536  CD  ARG C 109     5679  12854   6537   1190   2092  -1635       C  
ATOM   4537  NE  ARG C 109     -10.097  58.980  87.123  1.00 65.94           N  
ANISOU 4537  NE  ARG C 109     5608  12673   6775   1159   2033  -1664       N  
ATOM   4538  CZ  ARG C 109     -10.284  60.231  86.716  1.00 66.91           C  
ANISOU 4538  CZ  ARG C 109     5741  12680   7003   1320   1952  -1872       C  
ATOM   4539  NH1 ARG C 109     -10.071  61.243  87.546  1.00 68.76           N  
ANISOU 4539  NH1 ARG C 109     6049  12948   7130   1517   1915  -2076       N  
ATOM   4540  NH2 ARG C 109     -10.687  60.469  85.477  1.00 65.60           N  
ANISOU 4540  NH2 ARG C 109     5518  12359   7050   1287   1900  -1873       N  
ATOM   4541  N   GLU C 110      -5.975  60.551  91.124  1.00 68.42           N  
ANISOU 4541  N   GLU C 110     6507  13064   6424   1597   1788  -2255       N  
ATOM   4542  CA  GLU C 110      -5.724  61.988  91.091  1.00 69.56           C  
ANISOU 4542  CA  GLU C 110     6716  13061   6651   1765   1663  -2539       C  
ATOM   4543  C   GLU C 110      -4.240  62.330  91.075  1.00 68.05           C  
ANISOU 4543  C   GLU C 110     6686  12676   6493   1762   1511  -2693       C  
ATOM   4544  O   GLU C 110      -3.895  63.504  90.901  1.00 69.65           O  
ANISOU 4544  O   GLU C 110     6955  12702   6808   1868   1390  -2921       O  
ATOM   4545  CB  GLU C 110      -6.405  62.685  92.273  1.00 74.17           C  
ANISOU 4545  CB  GLU C 110     7265  13853   7063   1966   1699  -2657       C  
ATOM   4546  CG  GLU C 110      -6.653  64.173  92.032  1.00 78.02           C  
ANISOU 4546  CG  GLU C 110     7772  14194   7678   2137   1598  -2912       C  
ATOM   4547  CD  GLU C 110      -7.456  64.836  93.134  1.00 84.76           C  
ANISOU 4547  CD  GLU C 110     8575  15266   8364   2340   1642  -3024       C  
ATOM   4548  OE1 GLU C 110      -6.840  65.336  94.099  1.00 87.12           O  
ANISOU 4548  OE1 GLU C 110     8967  15607   8528   2462   1568  -3187       O  
ATOM   4549  OE2 GLU C 110      -8.700  64.872  93.027  1.00 87.18           O  
ANISOU 4549  OE2 GLU C 110     8743  15704   8675   2383   1744  -2955       O  
ATOM   4550  N   ALA C 111      -3.357  61.349  91.242  1.00 72.74           N  
ANISOU 4550  N   ALA C 111     7344  13292   7001   1641   1511  -2572       N  
ATOM   4551  CA  ALA C 111      -1.927  61.595  91.130  1.00 71.52           C  
ANISOU 4551  CA  ALA C 111     7327  12952   6894   1619   1365  -2706       C  
ATOM   4552  C   ALA C 111      -1.406  61.430  89.708  1.00 69.89           C  
ANISOU 4552  C   ALA C 111     7141  12488   6925   1474   1310  -2674       C  
ATOM   4553  O   ALA C 111      -0.248  61.771  89.447  1.00 69.68           O  
ANISOU 4553  O   ALA C 111     7218  12275   6983   1452   1182  -2800       O  
ATOM   4554  CB  ALA C 111      -1.152  60.664  92.068  1.00 72.24           C  
ANISOU 4554  CB  ALA C 111     7485  13199   6763   1583   1376  -2607       C  
ATOM   4555  N   ALA C 112      -2.229  60.928  88.788  1.00 58.42           N  
ANISOU 4555  N   ALA C 112     5587  11022   5586   1374   1398  -2511       N  
ATOM   4556  CA  ALA C 112      -1.787  60.664  87.425  1.00 57.09           C  
ANISOU 4556  CA  ALA C 112     5429  10631   5631   1236   1355  -2461       C  
ATOM   4557  C   ALA C 112      -2.102  61.859  86.536  1.00 56.22           C  
ANISOU 4557  C   ALA C 112     5308  10303   5748   1309   1283  -2618       C  
ATOM   4558  O   ALA C 112      -3.278  62.226  86.408  1.00 55.48           O  
ANISOU 4558  O   ALA C 112     5116  10274   5690   1378   1342  -2604       O  
ATOM   4559  CB  ALA C 112      -2.457  59.417  86.875  1.00 56.43           C  
ANISOU 4559  CB  ALA C 112     5244  10641   5558   1077   1474  -2192       C  
ATOM   4560  N   PRO C 113      -1.104  62.487  85.911  1.00 55.89           N  
ANISOU 4560  N   PRO C 113     5365  10004   5867   1296   1157  -2760       N  
ATOM   4561  CA  PRO C 113      -1.394  63.648  85.053  1.00 55.72           C  
ANISOU 4561  CA  PRO C 113     5348   9755   6069   1367   1086  -2892       C  
ATOM   4562  C   PRO C 113      -2.291  63.321  83.874  1.00 56.61           C  
ANISOU 4562  C   PRO C 113     5356   9825   6329   1301   1149  -2749       C  
ATOM   4563  O   PRO C 113      -3.071  64.183  83.448  1.00 55.38           O  
ANISOU 4563  O   PRO C 113     5162   9592   6289   1401   1134  -2816       O  
ATOM   4564  CB  PRO C 113      -0.000  64.099  84.594  1.00 53.39           C  
ANISOU 4564  CB  PRO C 113     5177   9195   5912   1316    951  -3019       C  
ATOM   4565  CG  PRO C 113       0.938  63.547  85.621  1.00 54.22           C  
ANISOU 4565  CG  PRO C 113     5348   9427   5828   1290    928  -3032       C  
ATOM   4566  CD  PRO C 113       0.341  62.240  86.040  1.00 54.68           C  
ANISOU 4566  CD  PRO C 113     5326   9755   5695   1227   1067  -2812       C  
ATOM   4567  N   CYS C 114      -2.211  62.101  83.334  1.00 59.12           N  
ANISOU 4567  N   CYS C 114     5626  10189   6646   1139   1211  -2552       N  
ATOM   4568  CA  CYS C 114      -3.056  61.751  82.196  1.00 56.93           C  
ANISOU 4568  CA  CYS C 114     5245   9868   6517   1066   1251  -2411       C  
ATOM   4569  C   CYS C 114      -4.532  61.904  82.534  1.00 58.59           C  
ANISOU 4569  C   CYS C 114     5322  10267   6671   1153   1338  -2367       C  
ATOM   4570  O   CYS C 114      -5.338  62.215  81.652  1.00 58.34           O  
ANISOU 4570  O   CYS C 114     5213  10167   6787   1173   1334  -2343       O  
ATOM   4571  CB  CYS C 114      -2.743  60.330  81.717  1.00 56.70           C  
ANISOU 4571  CB  CYS C 114     5235   9815   6494    845   1261  -2149       C  
ATOM   4572  SG  CYS C 114      -3.411  58.980  82.713  1.00 59.13           S  
ANISOU 4572  SG  CYS C 114     5435  10466   6568    767   1416  -1950       S  
ATOM   4573  N   LYS C 115      -4.895  61.746  83.808  1.00 55.72           N  
ANISOU 4573  N   LYS C 115     4934  10138   6098   1215   1409  -2359       N  
ATOM   4574  CA  LYS C 115      -6.267  61.890  84.276  1.00 57.77           C  
ANISOU 4574  CA  LYS C 115     5066  10598   6288   1301   1499  -2318       C  
ATOM   4575  C   LYS C 115      -6.680  63.343  84.516  1.00 60.82           C  
ANISOU 4575  C   LYS C 115     5473  10926   6710   1512   1442  -2533       C  
ATOM   4576  O   LYS C 115      -7.697  63.569  85.184  1.00 60.89           O  
ANISOU 4576  O   LYS C 115     5391  11127   6617   1617   1514  -2536       O  
ATOM   4577  CB  LYS C 115      -6.466  61.089  85.566  1.00 58.59           C  
ANISOU 4577  CB  LYS C 115     5137  10980   6145   1282   1607  -2208       C  
ATOM   4578  CG  LYS C 115      -5.970  59.658  85.504  1.00 58.08           C  
ANISOU 4578  CG  LYS C 115     5078  10969   6022   1082   1658  -1993       C  
ATOM   4579  CD  LYS C 115      -7.020  58.741  84.909  1.00 57.83           C  
ANISOU 4579  CD  LYS C 115     4895  11019   6059    940   1750  -1766       C  
ATOM   4580  CE  LYS C 115      -6.569  57.293  84.955  1.00 57.23           C  
ANISOU 4580  CE  LYS C 115     4832  10994   5917    739   1800  -1542       C  
ATOM   4581  NZ  LYS C 115      -7.584  56.387  84.354  1.00 58.02           N  
ANISOU 4581  NZ  LYS C 115     4788  11147   6109    580   1871  -1322       N  
ATOM   4582  N   GLU C 116      -5.935  64.327  84.003  1.00 65.13           N  
ANISOU 4582  N   GLU C 116     6136  11211   7401   1575   1316  -2707       N  
ATOM   4583  CA  GLU C 116      -6.264  65.722  84.294  1.00 66.09           C  
ANISOU 4583  CA  GLU C 116     6296  11258   7558   1772   1251  -2911       C  
ATOM   4584  C   GLU C 116      -7.610  66.121  83.699  1.00 66.13           C  
ANISOU 4584  C   GLU C 116     6180  11291   7655   1854   1288  -2879       C  
ATOM   4585  O   GLU C 116      -8.414  66.787  84.362  1.00 66.80           O  
ANISOU 4585  O   GLU C 116     6221  11497   7663   2014   1313  -2968       O  
ATOM   4586  CB  GLU C 116      -5.157  66.642  83.781  1.00 64.67           C  
ANISOU 4586  CB  GLU C 116     6269  10760   7543   1792   1105  -3077       C  
ATOM   4587  CG  GLU C 116      -4.036  66.874  84.780  1.00 66.12           C  
ANISOU 4587  CG  GLU C 116     6575  10932   7616   1811   1037  -3215       C  
ATOM   4588  CD  GLU C 116      -2.759  67.351  84.118  1.00 67.77           C  
ANISOU 4588  CD  GLU C 116     6916  10831   8004   1744    907  -3311       C  
ATOM   4589  OE1 GLU C 116      -2.833  67.863  82.981  1.00 67.44           O  
ANISOU 4589  OE1 GLU C 116     6891  10558   8177   1735    859  -3314       O  
ATOM   4590  OE2 GLU C 116      -1.681  67.212  84.734  1.00 69.04           O  
ANISOU 4590  OE2 GLU C 116     7161  10980   8091   1700    851  -3377       O  
ATOM   4591  N   ASN C 117      -7.874  65.728  82.455  1.00 60.14           N  
ANISOU 4591  N   ASN C 117     5364  10428   7058   1755   1286  -2756       N  
ATOM   4592  CA  ASN C 117      -9.112  66.047  81.757  1.00 61.65           C  
ANISOU 4592  CA  ASN C 117     5436  10637   7351   1824   1305  -2715       C  
ATOM   4593  C   ASN C 117      -9.787  64.764  81.295  1.00 61.87           C  
ANISOU 4593  C   ASN C 117     5311  10820   7375   1661   1397  -2484       C  
ATOM   4594  O   ASN C 117      -9.117  63.818  80.862  1.00 60.67           O  
ANISOU 4594  O   ASN C 117     5180  10621   7249   1485   1399  -2364       O  
ATOM   4595  CB  ASN C 117      -8.863  66.948  80.542  1.00 58.54           C  
ANISOU 4595  CB  ASN C 117     5122   9936   7186   1876   1188  -2795       C  
ATOM   4596  CG  ASN C 117      -8.025  68.165  80.873  1.00 59.64           C  
ANISOU 4596  CG  ASN C 117     5430   9863   7369   1995   1081  -3007       C  
ATOM   4597  OD1 ASN C 117      -8.555  69.245  81.132  1.00 61.12           O  
ANISOU 4597  OD1 ASN C 117     5635  10016   7572   2171   1045  -3141       O  
ATOM   4598  ND2 ASN C 117      -6.707  68.001  80.853  1.00 57.55           N  
ANISOU 4598  ND2 ASN C 117     5287   9448   7131   1894   1024  -3040       N  
ATOM   4599  N   VAL C 118     -11.118  64.752  81.365  1.00 64.68           N  
ANISOU 4599  N   VAL C 118     5513  11352   7709   1718   1466  -2426       N  
ATOM   4600  CA  VAL C 118     -11.933  63.600  80.999  1.00 65.53           C  
ANISOU 4600  CA  VAL C 118     5457  11617   7825   1565   1550  -2212       C  
ATOM   4601  C   VAL C 118     -12.988  64.041  79.995  1.00 65.53           C  
ANISOU 4601  C   VAL C 118     5346  11572   7979   1631   1515  -2203       C  
ATOM   4602  O   VAL C 118     -13.753  64.976  80.260  1.00 65.31           O  
ANISOU 4602  O   VAL C 118     5280  11596   7941   1815   1513  -2314       O  
ATOM   4603  CB  VAL C 118     -12.603  62.961  82.230  1.00 68.64           C  
ANISOU 4603  CB  VAL C 118     5742  12319   8020   1544   1686  -2120       C  
ATOM   4604  CG1 VAL C 118     -13.416  61.739  81.825  1.00 68.00           C  
ANISOU 4604  CG1 VAL C 118     5494  12370   7974   1359   1765  -1888       C  
ATOM   4605  CG2 VAL C 118     -11.561  62.593  83.267  1.00 68.62           C  
ANISOU 4605  CG2 VAL C 118     5858  12366   7847   1506   1711  -2135       C  
ATOM   4606  N   ILE C 119     -13.029  63.368  78.849  1.00 64.16           N  
ANISOU 4606  N   ILE C 119     5125  11309   7944   1488   1479  -2074       N  
ATOM   4607  CA  ILE C 119     -14.061  63.546  77.837  1.00 64.44           C  
ANISOU 4607  CA  ILE C 119     5038  11329   8119   1522   1442  -2033       C  
ATOM   4608  C   ILE C 119     -14.877  62.261  77.816  1.00 65.09           C  
ANISOU 4608  C   ILE C 119     4941  11609   8182   1339   1525  -1830       C  
ATOM   4609  O   ILE C 119     -14.382  61.207  77.392  1.00 63.21           O  
ANISOU 4609  O   ILE C 119     4710  11326   7979   1138   1518  -1695       O  
ATOM   4610  CB  ILE C 119     -13.464  63.852  76.457  1.00 62.03           C  
ANISOU 4610  CB  ILE C 119     4825  10747   7997   1512   1316  -2055       C  
ATOM   4611  CG1 ILE C 119     -12.457  65.002  76.547  1.00 63.60           C  
ANISOU 4611  CG1 ILE C 119     5220  10720   8224   1650   1238  -2236       C  
ATOM   4612  CG2 ILE C 119     -14.566  64.178  75.458  1.00 60.91           C  
ANISOU 4612  CG2 ILE C 119     4566  10596   7982   1586   1265  -2030       C  
ATOM   4613  CD1 ILE C 119     -13.031  66.274  77.133  1.00 67.64           C  
ANISOU 4613  CD1 ILE C 119     5748  11252   8700   1882   1231  -2398       C  
ATOM   4614  N   ASP C 120     -16.122  62.345  78.288  1.00 63.21           N  
ANISOU 4614  N   ASP C 120     4541  11582   7893   1405   1600  -1809       N  
ATOM   4615  CA  ASP C 120     -16.999  61.189  78.403  1.00 65.69           C  
ANISOU 4615  CA  ASP C 120     4673  12092   8194   1233   1688  -1620       C  
ATOM   4616  C   ASP C 120     -18.182  61.222  77.446  1.00 66.79           C  
ANISOU 4616  C   ASP C 120     4644  12257   8475   1242   1646  -1577       C  
ATOM   4617  O   ASP C 120     -18.868  60.204  77.306  1.00 68.69           O  
ANISOU 4617  O   ASP C 120     4732  12615   8751   1070   1691  -1416       O  
ATOM   4618  CB  ASP C 120     -17.519  61.061  79.845  1.00 69.41           C  
ANISOU 4618  CB  ASP C 120     5069  12826   8478   1271   1830  -1601       C  
ATOM   4619  CG  ASP C 120     -18.224  62.317  80.328  1.00 73.31           C  
ANISOU 4619  CG  ASP C 120     5527  13407   8919   1529   1841  -1771       C  
ATOM   4620  OD1 ASP C 120     -17.826  63.425  79.910  1.00 73.42           O  
ANISOU 4620  OD1 ASP C 120     5661  13240   8994   1696   1739  -1939       O  
ATOM   4621  OD2 ASP C 120     -19.174  62.196  81.131  1.00 77.04           O  
ANISOU 4621  OD2 ASP C 120     5855  14124   9291   1564   1951  -1734       O  
ATOM   4622  N   LYS C 121     -18.441  62.351  76.789  1.00 69.75           N  
ANISOU 4622  N   LYS C 121     5044  12521   8937   1435   1555  -1714       N  
ATOM   4623  CA  LYS C 121     -19.536  62.460  75.837  1.00 70.91           C  
ANISOU 4623  CA  LYS C 121     5039  12689   9213   1468   1500  -1685       C  
ATOM   4624  C   LYS C 121     -19.095  63.314  74.657  1.00 69.77           C  
ANISOU 4624  C   LYS C 121     5017  12290   9201   1589   1353  -1784       C  
ATOM   4625  O   LYS C 121     -18.154  64.107  74.756  1.00 69.15           O  
ANISOU 4625  O   LYS C 121     5125  12039   9110   1698   1309  -1905       O  
ATOM   4626  CB  LYS C 121     -20.795  63.061  76.476  1.00 74.59           C  
ANISOU 4626  CB  LYS C 121     5351  13371   9617   1630   1572  -1743       C  
ATOM   4627  CG  LYS C 121     -21.588  62.088  77.333  1.00 78.00           C  
ANISOU 4627  CG  LYS C 121     5598  14074   9963   1490   1713  -1605       C  
ATOM   4628  CD  LYS C 121     -21.340  62.329  78.811  1.00 79.74           C  
ANISOU 4628  CD  LYS C 121     5870  14441   9986   1569   1831  -1661       C  
ATOM   4629  CE  LYS C 121     -22.174  61.400  79.678  1.00 81.80           C  
ANISOU 4629  CE  LYS C 121     5945  14978  10157   1441   1982  -1513       C  
ATOM   4630  NZ  LYS C 121     -21.952  59.968  79.340  1.00 81.20           N  
ANISOU 4630  NZ  LYS C 121     5830  14877  10145   1149   1998  -1306       N  
ATOM   4631  N   ASP C 122     -19.799  63.142  73.535  1.00 66.98           N  
ANISOU 4631  N   ASP C 122     4557  11914   8978   1567   1273  -1727       N  
ATOM   4632  CA  ASP C 122     -19.497  63.855  72.292  1.00 65.31           C  
ANISOU 4632  CA  ASP C 122     4447  11472   8894   1678   1130  -1791       C  
ATOM   4633  C   ASP C 122     -18.019  63.731  71.939  1.00 63.61           C  
ANISOU 4633  C   ASP C 122     4437  11026   8706   1601   1075  -1798       C  
ATOM   4634  O   ASP C 122     -17.357  64.707  71.580  1.00 63.58           O  
ANISOU 4634  O   ASP C 122     4595  10814   8747   1745   1003  -1906       O  
ATOM   4635  CB  ASP C 122     -19.918  65.322  72.382  1.00 66.26           C  
ANISOU 4635  CB  ASP C 122     4611  11548   9015   1958   1099  -1947       C  
ATOM   4636  CG  ASP C 122     -21.421  65.493  72.452  1.00 69.71           C  
ANISOU 4636  CG  ASP C 122     4837  12197   9451   2050   1128  -1943       C  
ATOM   4637  OD1 ASP C 122     -22.125  64.924  71.591  1.00 70.54           O  
ANISOU 4637  OD1 ASP C 122     4802  12353   9645   1969   1077  -1850       O  
ATOM   4638  OD2 ASP C 122     -21.899  66.193  73.369  1.00 71.14           O  
ANISOU 4638  OD2 ASP C 122     4990  12499   9543   2204   1196  -2039       O  
ATOM   4639  N   ILE C 123     -17.499  62.508  72.052  1.00 59.44           N  
ANISOU 4639  N   ILE C 123     3900  10529   8157   1369   1111  -1678       N  
ATOM   4640  CA  ILE C 123     -16.071  62.275  71.887  1.00 57.63           C  
ANISOU 4640  CA  ILE C 123     3850  10114   7935   1282   1078  -1682       C  
ATOM   4641  C   ILE C 123     -15.649  62.671  70.481  1.00 57.19           C  
ANISOU 4641  C   ILE C 123     3884   9825   8019   1335    939  -1705       C  
ATOM   4642  O   ILE C 123     -16.176  62.158  69.487  1.00 56.35           O  
ANISOU 4642  O   ILE C 123     3687   9722   8002   1269    866  -1623       O  
ATOM   4643  CB  ILE C 123     -15.730  60.815  72.185  1.00 56.72           C  
ANISOU 4643  CB  ILE C 123     3694  10081   7775   1020   1133  -1533       C  
ATOM   4644  CG1 ILE C 123     -15.804  60.565  73.689  1.00 60.25           C  
ANISOU 4644  CG1 ILE C 123     4113  10718   8060    992   1274  -1518       C  
ATOM   4645  CG2 ILE C 123     -14.351  60.467  71.649  1.00 54.80           C  
ANISOU 4645  CG2 ILE C 123     3613   9634   7574    920   1071  -1523       C  
ATOM   4646  CD1 ILE C 123     -15.419  59.178  74.076  1.00 61.15           C  
ANISOU 4646  CD1 ILE C 123     4211  10899   8122    747   1333  -1362       C  
ATOM   4647  N   ASN C 124     -14.696  63.596  70.395  1.00 52.41           N  
ANISOU 4647  N   ASN C 124     3462   9012   7438   1455    897  -1815       N  
ATOM   4648  CA  ASN C 124     -14.136  64.054  69.128  1.00 50.31           C  
ANISOU 4648  CA  ASN C 124     3312   8502   7302   1515    776  -1831       C  
ATOM   4649  C   ASN C 124     -12.619  64.005  69.249  1.00 49.10           C  
ANISOU 4649  C   ASN C 124     3345   8160   7151   1440    771  -1856       C  
ATOM   4650  O   ASN C 124     -12.028  64.802  69.985  1.00 48.37           O  
ANISOU 4650  O   ASN C 124     3362   7994   7024   1536    800  -1974       O  
ATOM   4651  CB  ASN C 124     -14.619  65.467  68.790  1.00 51.47           C  
ANISOU 4651  CB  ASN C 124     3509   8541   7505   1765    716  -1934       C  
ATOM   4652  CG  ASN C 124     -14.228  65.904  67.387  1.00 51.13           C  
ANISOU 4652  CG  ASN C 124     3573   8259   7595   1835    591  -1916       C  
ATOM   4653  OD1 ASN C 124     -13.350  65.313  66.758  1.00 49.49           O  
ANISOU 4653  OD1 ASN C 124     3452   7923   7430   1705    548  -1844       O  
ATOM   4654  ND2 ASN C 124     -14.880  66.950  66.893  1.00 52.37           N  
ANISOU 4654  ND2 ASN C 124     3748   8344   7805   2038    528  -1962       N  
ATOM   4655  N   LEU C 125     -11.994  63.069  68.529  1.00 55.01           N  
ANISOU 4655  N   LEU C 125     4181   8794   7926   1245    715  -1714       N  
ATOM   4656  CA  LEU C 125     -10.538  62.957  68.558  1.00 54.81           C  
ANISOU 4656  CA  LEU C 125     4380   8557   7890   1141    693  -1686       C  
ATOM   4657  C   LEU C 125      -9.866  64.214  68.025  1.00 56.23           C  
ANISOU 4657  C   LEU C 125     4738   8473   8156   1284    623  -1762       C  
ATOM   4658  O   LEU C 125      -8.733  64.524  68.413  1.00 56.36           O  
ANISOU 4658  O   LEU C 125     4913   8340   8161   1252    626  -1801       O  
ATOM   4659  CB  LEU C 125     -10.081  61.752  67.737  1.00 53.53           C  
ANISOU 4659  CB  LEU C 125     4272   8321   7745    936    636  -1525       C  
ATOM   4660  CG  LEU C 125     -10.367  60.335  68.224  1.00 55.20           C  
ANISOU 4660  CG  LEU C 125     4372   8714   7886    738    690  -1420       C  
ATOM   4661  CD1 LEU C 125     -10.143  59.369  67.074  1.00 55.04           C  
ANISOU 4661  CD1 LEU C 125     4404   8586   7921    593    593  -1289       C  
ATOM   4662  CD2 LEU C 125      -9.478  59.984  69.400  1.00 54.82           C  
ANISOU 4662  CD2 LEU C 125     4405   8695   7728    648    772  -1426       C  
ATOM   4663  N   PHE C 126     -10.539  64.942  67.133  1.00 54.67           N  
ANISOU 4663  N   PHE C 126     4513   8210   8048   1439    555  -1779       N  
ATOM   4664  CA  PHE C 126      -9.904  66.076  66.473  1.00 54.77           C  
ANISOU 4664  CA  PHE C 126     4707   7947   8157   1559    482  -1814       C  
ATOM   4665  C   PHE C 126      -9.740  67.263  67.413  1.00 55.61           C  
ANISOU 4665  C   PHE C 126     4863   7999   8268   1716    517  -1987       C  
ATOM   4666  O   PHE C 126      -8.824  68.072  67.228  1.00 55.34           O  
ANISOU 4666  O   PHE C 126     5009   7714   8305   1749    476  -2021       O  
ATOM   4667  CB  PHE C 126     -10.708  66.474  65.237  1.00 53.69           C  
ANISOU 4667  CB  PHE C 126     4533   7763   8105   1690    395  -1769       C  
ATOM   4668  CG  PHE C 126     -10.598  65.492  64.108  1.00 52.39           C  
ANISOU 4668  CG  PHE C 126     4381   7576   7949   1551    328  -1612       C  
ATOM   4669  CD1 PHE C 126     -11.338  64.321  64.114  1.00 52.82           C  
ANISOU 4669  CD1 PHE C 126     4265   7849   7958   1432    339  -1552       C  
ATOM   4670  CD2 PHE C 126      -9.747  65.735  63.043  1.00 50.98           C  
ANISOU 4670  CD2 PHE C 126     4386   7158   7825   1540    255  -1526       C  
ATOM   4671  CE1 PHE C 126     -11.234  63.414  63.077  1.00 51.76           C  
ANISOU 4671  CE1 PHE C 126     4150   7682   7833   1313    262  -1429       C  
ATOM   4672  CE2 PHE C 126      -9.639  64.832  62.004  1.00 51.23           C  
ANISOU 4672  CE2 PHE C 126     4435   7180   7849   1433    190  -1397       C  
ATOM   4673  CZ  PHE C 126     -10.383  63.671  62.022  1.00 51.47           C  
ANISOU 4673  CZ  PHE C 126     4304   7418   7836   1323    186  -1358       C  
ATOM   4674  N   GLU C 127     -10.602  67.386  68.420  1.00 57.24           N  
ANISOU 4674  N   GLU C 127     4912   8437   8401   1815    592  -2100       N  
ATOM   4675  CA  GLU C 127     -10.457  68.443  69.413  1.00 57.49           C  
ANISOU 4675  CA  GLU C 127     4995   8435   8412   1968    622  -2280       C  
ATOM   4676  C   GLU C 127      -9.342  68.164  70.413  1.00 57.42           C  
ANISOU 4676  C   GLU C 127     5080   8412   8325   1846    670  -2331       C  
ATOM   4677  O   GLU C 127      -9.084  69.006  71.280  1.00 59.19           O  
ANISOU 4677  O   GLU C 127     5378   8590   8521   1946    678  -2478       O  
ATOM   4678  CB  GLU C 127     -11.778  68.658  70.155  1.00 60.04           C  
ANISOU 4678  CB  GLU C 127     5178   9000   8636   2077    674  -2321       C  
ATOM   4679  CG  GLU C 127     -12.786  69.493  69.384  1.00 64.00           C  
ANISOU 4679  CG  GLU C 127     5652   9452   9214   2260    607  -2322       C  
ATOM   4680  CD  GLU C 127     -14.192  69.357  69.930  1.00 69.80           C  
ANISOU 4680  CD  GLU C 127     6195  10469   9856   2327    666  -2325       C  
ATOM   4681  OE1 GLU C 127     -14.358  68.702  70.981  1.00 70.30           O  
ANISOU 4681  OE1 GLU C 127     6162  10756   9792   2238    765  -2327       O  
ATOM   4682  OE2 GLU C 127     -15.129  69.903  69.309  1.00 72.99           O  
ANISOU 4682  OE2 GLU C 127     6546  10875  10313   2469    615  -2318       O  
ATOM   4683  N   ILE C 128      -8.678  67.013  70.312  1.00 49.58           N  
ANISOU 4683  N   ILE C 128     4114   7440   7283   1619    685  -2192       N  
ATOM   4684  CA  ILE C 128      -7.562  66.655  71.178  1.00 50.43           C  
ANISOU 4684  CA  ILE C 128     4318   7532   7311   1493    718  -2216       C  
ATOM   4685  C   ILE C 128      -6.271  66.492  70.383  1.00 49.69           C  
ANISOU 4685  C   ILE C 128     4404   7179   7297   1351    646  -2117       C  
ATOM   4686  O   ILE C 128      -5.245  67.096  70.711  1.00 48.59           O  
ANISOU 4686  O   ILE C 128     4401   6871   7188   1348    618  -2197       O  
ATOM   4687  CB  ILE C 128      -7.867  65.375  71.989  1.00 51.05           C  
ANISOU 4687  CB  ILE C 128     4266   7895   7236   1359    813  -2143       C  
ATOM   4688  CG1 ILE C 128      -9.116  65.572  72.852  1.00 52.01           C  
ANISOU 4688  CG1 ILE C 128     4196   8300   7267   1502    903  -2238       C  
ATOM   4689  CG2 ILE C 128      -6.673  64.986  72.846  1.00 50.23           C  
ANISOU 4689  CG2 ILE C 128     4273   7773   7040   1241    835  -2159       C  
ATOM   4690  CD1 ILE C 128      -8.971  66.658  73.900  1.00 51.89           C  
ANISOU 4690  CD1 ILE C 128     4254   8272   7190   1661    913  -2422       C  
ATOM   4691  N   LEU C 129      -6.307  65.676  69.314  1.00 45.63           N  
ANISOU 4691  N   LEU C 129     3885   6636   6818   1236    612  -1945       N  
ATOM   4692  CA  LEU C 129      -5.127  65.380  68.508  1.00 43.92           C  
ANISOU 4692  CA  LEU C 129     3820   6212   6656   1104    555  -1836       C  
ATOM   4693  C   LEU C 129      -5.169  66.153  67.201  1.00 45.41           C  
ANISOU 4693  C   LEU C 129     4087   6188   6979   1191    477  -1788       C  
ATOM   4694  O   LEU C 129      -6.171  66.073  66.475  1.00 45.62           O  
ANISOU 4694  O   LEU C 129     4026   6277   7030   1262    452  -1737       O  
ATOM   4695  CB  LEU C 129      -5.044  63.885  68.207  1.00 43.35           C  
ANISOU 4695  CB  LEU C 129     3707   6246   6516    922    564  -1682       C  
ATOM   4696  CG  LEU C 129      -5.121  62.888  69.364  1.00 42.81           C  
ANISOU 4696  CG  LEU C 129     3556   6400   6311    816    643  -1676       C  
ATOM   4697  CD1 LEU C 129      -5.409  61.495  68.826  1.00 40.79           C  
ANISOU 4697  CD1 LEU C 129     3242   6230   6026    663    634  -1517       C  
ATOM   4698  CD2 LEU C 129      -3.832  62.894  70.169  1.00 41.01           C  
ANISOU 4698  CD2 LEU C 129     3446   6108   6027    748    656  -1726       C  
ATOM   4699  N   PRO C 130      -4.125  66.908  66.864  1.00 45.87           N  
ANISOU 4699  N   PRO C 130     4304   6000   7125   1190    436  -1797       N  
ATOM   4700  CA  PRO C 130      -4.039  67.478  65.512  1.00 45.82           C  
ANISOU 4700  CA  PRO C 130     4386   5791   7232   1246    370  -1703       C  
ATOM   4701  C   PRO C 130      -3.703  66.416  64.475  1.00 44.64           C  
ANISOU 4701  C   PRO C 130     4258   5646   7056   1114    344  -1527       C  
ATOM   4702  O   PRO C 130      -2.543  66.271  64.076  1.00 45.45           O  
ANISOU 4702  O   PRO C 130     4477   5612   7180   1010    331  -1453       O  
ATOM   4703  CB  PRO C 130      -2.921  68.523  65.637  1.00 46.29           C  
ANISOU 4703  CB  PRO C 130     4599   5598   7391   1250    349  -1760       C  
ATOM   4704  CG  PRO C 130      -2.772  68.765  67.113  1.00 45.75           C  
ANISOU 4704  CG  PRO C 130     4502   5613   7271   1263    389  -1937       C  
ATOM   4705  CD  PRO C 130      -3.092  67.455  67.756  1.00 45.16           C  
ANISOU 4705  CD  PRO C 130     4307   5809   7043   1162    447  -1910       C  
ATOM   4706  N   LEU C 131      -4.712  65.671  64.034  1.00 40.90           N  
ANISOU 4706  N   LEU C 131     3668   5335   6538   1122    332  -1467       N  
ATOM   4707  CA  LEU C 131      -4.495  64.562  63.117  1.00 42.25           C  
ANISOU 4707  CA  LEU C 131     3852   5528   6673   1004    296  -1323       C  
ATOM   4708  C   LEU C 131      -4.225  65.065  61.703  1.00 42.89           C  
ANISOU 4708  C   LEU C 131     4043   5430   6824   1070    230  -1223       C  
ATOM   4709  O   LEU C 131      -4.721  66.116  61.286  1.00 43.67           O  
ANISOU 4709  O   LEU C 131     4158   5438   6994   1228    201  -1246       O  
ATOM   4710  CB  LEU C 131      -5.703  63.624  63.120  1.00 42.28           C  
ANISOU 4710  CB  LEU C 131     3689   5756   6621    983    293  -1303       C  
ATOM   4711  CG  LEU C 131      -6.018  62.963  64.464  1.00 43.26           C  
ANISOU 4711  CG  LEU C 131     3694   6081   6660    901    371  -1364       C  
ATOM   4712  CD1 LEU C 131      -7.504  62.683  64.593  1.00 43.28           C  
ANISOU 4712  CD1 LEU C 131     3498   6297   6647    953    382  -1383       C  
ATOM   4713  CD2 LEU C 131      -5.212  61.686  64.633  1.00 44.68           C  
ANISOU 4713  CD2 LEU C 131     3919   6286   6771    706    382  -1278       C  
ATOM   4714  N   TYR C 132      -3.435  64.290  60.963  1.00 38.77           N  
ANISOU 4714  N   TYR C 132     3598   4862   6271    958    206  -1108       N  
ATOM   4715  CA  TYR C 132      -2.998  64.667  59.626  1.00 38.03           C  
ANISOU 4715  CA  TYR C 132     3619   4614   6217   1009    157   -995       C  
ATOM   4716  C   TYR C 132      -2.721  63.400  58.829  1.00 35.86           C  
ANISOU 4716  C   TYR C 132     3358   4402   5866    908    118   -889       C  
ATOM   4717  O   TYR C 132      -2.699  62.294  59.374  1.00 37.87           O  
ANISOU 4717  O   TYR C 132     3554   4780   6055    786    131   -901       O  
ATOM   4718  CB  TYR C 132      -1.754  65.561  59.682  1.00 36.13           C  
ANISOU 4718  CB  TYR C 132     3516   4165   6046    991    187   -984       C  
ATOM   4719  CG  TYR C 132      -0.580  64.902  60.370  1.00 35.40           C  
ANISOU 4719  CG  TYR C 132     3457   4081   5911    825    230   -992       C  
ATOM   4720  CD1 TYR C 132      -0.465  64.912  61.755  1.00 35.26           C  
ANISOU 4720  CD1 TYR C 132     3391   4130   5878    777    274  -1117       C  
ATOM   4721  CD2 TYR C 132       0.409  64.260  59.636  1.00 34.93           C  
ANISOU 4721  CD2 TYR C 132     3475   3981   5817    733    222   -878       C  
ATOM   4722  CE1 TYR C 132       0.603  64.303  62.390  1.00 35.83           C  
ANISOU 4722  CE1 TYR C 132     3493   4219   5903    639    304  -1125       C  
ATOM   4723  CE2 TYR C 132       1.480  63.650  60.261  1.00 35.85           C  
ANISOU 4723  CE2 TYR C 132     3615   4114   5894    597    255   -888       C  
ATOM   4724  CZ  TYR C 132       1.572  63.672  61.638  1.00 36.33           C  
ANISOU 4724  CZ  TYR C 132     3628   4235   5943    549    292  -1010       C  
ATOM   4725  OH  TYR C 132       2.639  63.066  62.261  1.00 36.78           O  
ANISOU 4725  OH  TYR C 132     3708   4315   5952    427    315  -1020       O  
ATOM   4726  N   ARG C 133      -2.507  63.570  57.526  1.00 37.80           N  
ANISOU 4726  N   ARG C 133     3688   4558   6115    969     69   -782       N  
ATOM   4727  CA  ARG C 133      -2.148  62.459  56.655  1.00 39.48           C  
ANISOU 4727  CA  ARG C 133     3937   4814   6250    900     24   -690       C  
ATOM   4728  C   ARG C 133      -0.629  62.347  56.593  1.00 39.53           C  
ANISOU 4728  C   ARG C 133     4062   4714   6242    805     68   -630       C  
ATOM   4729  O   ARG C 133       0.056  63.314  56.242  1.00 39.68           O  
ANISOU 4729  O   ARG C 133     4173   4585   6317    849     96   -581       O  
ATOM   4730  CB  ARG C 133      -2.731  62.634  55.253  1.00 39.78           C  
ANISOU 4730  CB  ARG C 133     4000   4843   6273   1032    -56   -611       C  
ATOM   4731  CG  ARG C 133      -2.690  61.352  54.433  1.00 40.55           C  
ANISOU 4731  CG  ARG C 133     4104   5025   6278    977   -124   -557       C  
ATOM   4732  CD  ARG C 133      -3.195  61.554  53.017  1.00 42.08           C  
ANISOU 4732  CD  ARG C 133     4332   5217   6438   1122   -212   -485       C  
ATOM   4733  NE  ARG C 133      -4.492  62.219  52.989  1.00 42.32           N  
ANISOU 4733  NE  ARG C 133     4265   5297   6516   1256   -255   -534       N  
ATOM   4734  CZ  ARG C 133      -5.656  61.589  53.093  1.00 41.33           C  
ANISOU 4734  CZ  ARG C 133     3995   5326   6383   1255   -321   -601       C  
ATOM   4735  NH1 ARG C 133      -5.697  60.272  53.235  1.00 41.46           N  
ANISOU 4735  NH1 ARG C 133     3958   5441   6354   1117   -355   -622       N  
ATOM   4736  NH2 ARG C 133      -6.782  62.279  53.056  1.00 42.04           N  
ANISOU 4736  NH2 ARG C 133     3989   5468   6518   1392   -356   -645       N  
ATOM   4737  N   ILE C 134      -0.111  61.166  56.927  1.00 41.83           N  
ANISOU 4737  N   ILE C 134     4347   5082   6466    675     72   -629       N  
ATOM   4738  CA  ILE C 134       1.332  60.982  57.038  1.00 41.59           C  
ANISOU 4738  CA  ILE C 134     4404   4979   6418    584    115   -589       C  
ATOM   4739  C   ILE C 134       1.956  60.748  55.667  1.00 44.05           C  
ANISOU 4739  C   ILE C 134     4810   5244   6684    619     86   -469       C  
ATOM   4740  O   ILE C 134       2.933  61.402  55.292  1.00 44.54           O  
ANISOU 4740  O   ILE C 134     4951   5196   6774    626    128   -403       O  
ATOM   4741  CB  ILE C 134       1.645  59.833  58.013  1.00 39.56           C  
ANISOU 4741  CB  ILE C 134     4107   4822   6102    449    130   -638       C  
ATOM   4742  CG1 ILE C 134       1.046  60.131  59.390  1.00 40.45           C  
ANISOU 4742  CG1 ILE C 134     4129   4999   6242    428    172   -749       C  
ATOM   4743  CG2 ILE C 134       3.145  59.618  58.122  1.00 40.26           C  
ANISOU 4743  CG2 ILE C 134     4276   4851   6170    368    166   -603       C  
ATOM   4744  CD1 ILE C 134       1.064  58.951  60.333  1.00 39.35           C  
ANISOU 4744  CD1 ILE C 134     3939   4980   6031    309    185   -780       C  
ATOM   4745  N   ASN C 135       1.417  59.811  54.898  1.00 43.98           N  
ANISOU 4745  N   ASN C 135     4788   5322   6599    641     12   -441       N  
ATOM   4746  CA  ASN C 135       1.875  59.592  53.536  1.00 43.37           C  
ANISOU 4746  CA  ASN C 135     4799   5224   6456    706    -24   -338       C  
ATOM   4747  C   ASN C 135       0.709  59.797  52.579  1.00 44.32           C  
ANISOU 4747  C   ASN C 135     4897   5381   6560    840   -105   -319       C  
ATOM   4748  O   ASN C 135      -0.454  59.598  52.943  1.00 42.74           O  
ANISOU 4748  O   ASN C 135     4596   5261   6383    850   -153   -393       O  
ATOM   4749  CB  ASN C 135       2.495  58.202  53.372  1.00 42.16           C  
ANISOU 4749  CB  ASN C 135     4675   5136   6210    625    -56   -331       C  
ATOM   4750  CG  ASN C 135       3.950  58.161  53.819  1.00 42.88           C  
ANISOU 4750  CG  ASN C 135     4818   5177   6295    541     20   -307       C  
ATOM   4751  OD1 ASN C 135       4.780  58.935  53.339  1.00 43.91           O  
ANISOU 4751  OD1 ASN C 135     5009   5230   6444    575     74   -231       O  
ATOM   4752  ND2 ASN C 135       4.261  57.265  54.749  1.00 40.60           N  
ANISOU 4752  ND2 ASN C 135     4503   4938   5986    430     25   -366       N  
ATOM   4753  N   GLU C 136       1.034  60.204  51.349  1.00 52.48           N  
ANISOU 4753  N   GLU C 136     6021   6370   7550    948   -120   -215       N  
ATOM   4754  CA  GLU C 136       0.018  60.762  50.460  1.00 54.93           C  
ANISOU 4754  CA  GLU C 136     6324   6693   7853   1105   -187   -184       C  
ATOM   4755  C   GLU C 136      -1.049  59.741  50.082  1.00 53.15           C  
ANISOU 4755  C   GLU C 136     6024   6603   7568   1127   -308   -247       C  
ATOM   4756  O   GLU C 136      -2.202  60.117  49.843  1.00 51.88           O  
ANISOU 4756  O   GLU C 136     5795   6487   7432   1227   -371   -277       O  
ATOM   4757  CB  GLU C 136       0.677  61.340  49.204  1.00 58.27           C  
ANISOU 4757  CB  GLU C 136     6869   7050   8219   1217   -171    -41       C  
ATOM   4758  CG  GLU C 136       1.082  60.310  48.164  1.00 61.09           C  
ANISOU 4758  CG  GLU C 136     7286   7493   8434   1244   -228      5       C  
ATOM   4759  CD  GLU C 136       1.389  60.934  46.817  1.00 63.79           C  
ANISOU 4759  CD  GLU C 136     7733   7808   8696   1396   -223    150       C  
ATOM   4760  OE1 GLU C 136       1.394  62.181  46.724  1.00 64.28           O  
ANISOU 4760  OE1 GLU C 136     7831   7763   8830   1461   -167    232       O  
ATOM   4761  OE2 GLU C 136       1.624  60.178  45.851  1.00 64.07           O  
ANISOU 4761  OE2 GLU C 136     7821   7929   8595   1455   -277    185       O  
ATOM   4762  N   GLN C 137      -0.701  58.456  50.031  1.00 41.52           N  
ANISOU 4762  N   GLN C 137     4557   5193   6025   1035   -348   -273       N  
ATOM   4763  CA  GLN C 137      -1.646  57.421  49.634  1.00 42.10           C  
ANISOU 4763  CA  GLN C 137     4566   5376   6055   1037   -475   -336       C  
ATOM   4764  C   GLN C 137      -2.289  56.722  50.823  1.00 42.36           C  
ANISOU 4764  C   GLN C 137     4472   5470   6154    892   -479   -435       C  
ATOM   4765  O   GLN C 137      -2.968  55.707  50.637  1.00 43.81           O  
ANISOU 4765  O   GLN C 137     4595   5731   6319    847   -580   -486       O  
ATOM   4766  CB  GLN C 137      -0.964  56.392  48.731  1.00 42.73           C  
ANISOU 4766  CB  GLN C 137     4740   5477   6017   1042   -537   -310       C  
ATOM   4767  CG  GLN C 137      -0.462  56.962  47.415  1.00 43.56           C  
ANISOU 4767  CG  GLN C 137     4961   5562   6028   1202   -540   -205       C  
ATOM   4768  CD  GLN C 137      -1.584  57.500  46.549  1.00 43.92           C  
ANISOU 4768  CD  GLN C 137     4978   5655   6054   1363   -634   -198       C  
ATOM   4769  OE1 GLN C 137      -2.541  56.789  46.242  1.00 44.67           O  
ANISOU 4769  OE1 GLN C 137     5005   5839   6130   1379   -764   -278       O  
ATOM   4770  NE2 GLN C 137      -1.473  58.762  46.151  1.00 42.44           N  
ANISOU 4770  NE2 GLN C 137     4843   5404   5879   1483   -575   -100       N  
ATOM   4771  N   ASP C 138      -2.093  57.238  52.034  1.00 36.96           N  
ANISOU 4771  N   ASP C 138     3746   4754   5543    817   -374   -460       N  
ATOM   4772  CA  ASP C 138      -2.749  56.668  53.201  1.00 34.87           C  
ANISOU 4772  CA  ASP C 138     3356   4565   5327    693   -362   -539       C  
ATOM   4773  C   ASP C 138      -4.264  56.766  53.060  1.00 36.46           C  
ANISOU 4773  C   ASP C 138     3415   4868   5570    749   -435   -590       C  
ATOM   4774  O   ASP C 138      -4.797  57.728  52.502  1.00 37.90           O  
ANISOU 4774  O   ASP C 138     3585   5043   5771    898   -456   -580       O  
ATOM   4775  CB  ASP C 138      -2.291  57.386  54.473  1.00 36.73           C  
ANISOU 4775  CB  ASP C 138     3577   4761   5618    639   -238   -564       C  
ATOM   4776  CG  ASP C 138      -0.864  57.035  54.863  1.00 37.55           C  
ANISOU 4776  CG  ASP C 138     3783   4798   5688    546   -175   -534       C  
ATOM   4777  OD1 ASP C 138      -0.304  56.077  54.289  1.00 35.08           O  
ANISOU 4777  OD1 ASP C 138     3538   4483   5308    510   -223   -500       O  
ATOM   4778  OD2 ASP C 138      -0.301  57.720  55.744  1.00 36.43           O  
ANISOU 4778  OD2 ASP C 138     3650   4607   5585    517    -85   -554       O  
ATOM   4779  N   GLY C 139      -4.960  55.747  53.570  1.00 40.20           N  
ANISOU 4779  N   GLY C 139     3776   5436   6061    629   -475   -639       N  
ATOM   4780  CA  GLY C 139      -6.413  55.729  53.528  1.00 40.88           C  
ANISOU 4780  CA  GLY C 139     3696   5641   6196    657   -541   -691       C  
ATOM   4781  C   GLY C 139      -7.074  56.798  54.370  1.00 42.24           C  
ANISOU 4781  C   GLY C 139     3755   5862   6432    718   -457   -732       C  
ATOM   4782  O   GLY C 139      -8.200  57.204  54.067  1.00 44.85           O  
ANISOU 4782  O   GLY C 139     3965   6278   6797    817   -511   -767       O  
ATOM   4783  N   GLY C 140      -6.406  57.259  55.415  1.00 39.79           N  
ANISOU 4783  N   GLY C 140     3480   5506   6134    674   -335   -739       N  
ATOM   4784  CA  GLY C 140      -6.929  58.318  56.243  1.00 39.53           C  
ANISOU 4784  CA  GLY C 140     3360   5506   6152    749   -255   -794       C  
ATOM   4785  C   GLY C 140      -5.831  58.916  57.091  1.00 39.43           C  
ANISOU 4785  C   GLY C 140     3449   5392   6139    722   -144   -798       C  
ATOM   4786  O   GLY C 140      -4.643  58.744  56.814  1.00 38.81           O  
ANISOU 4786  O   GLY C 140     3513   5204   6028    678   -132   -746       O  
ATOM   4787  N   PHE C 141      -6.238  59.633  58.135  1.00 44.16           N  
ANISOU 4787  N   PHE C 141     3966   6039   6774    757    -66   -871       N  
ATOM   4788  CA  PHE C 141      -5.285  60.147  59.109  1.00 43.57           C  
ANISOU 4788  CA  PHE C 141     3968   5888   6700    722     30   -902       C  
ATOM   4789  C   PHE C 141      -4.976  59.062  60.131  1.00 43.34           C  
ANISOU 4789  C   PHE C 141     3902   5948   6619    549     80   -909       C  
ATOM   4790  O   PHE C 141      -5.873  58.350  60.591  1.00 44.11           O  
ANISOU 4790  O   PHE C 141     3861   6197   6703    484     84   -923       O  
ATOM   4791  CB  PHE C 141      -5.833  61.393  59.804  1.00 44.35           C  
ANISOU 4791  CB  PHE C 141     4007   5995   6850    850     83   -994       C  
ATOM   4792  CG  PHE C 141      -6.395  62.420  58.860  1.00 44.79           C  
ANISOU 4792  CG  PHE C 141     4079   5979   6962   1036     25   -987       C  
ATOM   4793  CD1 PHE C 141      -5.812  62.646  57.621  1.00 43.64           C  
ANISOU 4793  CD1 PHE C 141     4068   5693   6820   1086    -32   -893       C  
ATOM   4794  CD2 PHE C 141      -7.508  63.163  59.214  1.00 45.81           C  
ANISOU 4794  CD2 PHE C 141     4086   6190   7130   1173     31  -1070       C  
ATOM   4795  CE1 PHE C 141      -6.331  63.590  56.755  1.00 46.20           C  
ANISOU 4795  CE1 PHE C 141     4417   5952   7187   1265    -85   -871       C  
ATOM   4796  CE2 PHE C 141      -8.030  64.109  58.354  1.00 46.86           C  
ANISOU 4796  CE2 PHE C 141     4240   6251   7312   1360    -28  -1060       C  
ATOM   4797  CZ  PHE C 141      -7.442  64.323  57.122  1.00 46.53           C  
ANISOU 4797  CZ  PHE C 141     4344   6061   7274   1404    -88   -955       C  
ATOM   4798  N   TYR C 142      -3.700  58.930  60.479  1.00 38.15           N  
ANISOU 4798  N   TYR C 142     3365   5200   5932    474    119   -890       N  
ATOM   4799  CA  TYR C 142      -3.229  57.799  61.263  1.00 37.12           C  
ANISOU 4799  CA  TYR C 142     3234   5130   5740    319    150   -873       C  
ATOM   4800  C   TYR C 142      -2.587  58.256  62.565  1.00 38.17           C  
ANISOU 4800  C   TYR C 142     3385   5267   5850    295    240   -937       C  
ATOM   4801  O   TYR C 142      -1.884  59.271  62.606  1.00 37.39           O  
ANISOU 4801  O   TYR C 142     3366   5054   5786    362    261   -974       O  
ATOM   4802  CB  TYR C 142      -2.223  56.966  60.463  1.00 36.56           C  
ANISOU 4802  CB  TYR C 142     3289   4969   5634    250     97   -792       C  
ATOM   4803  CG  TYR C 142      -2.834  55.808  59.709  1.00 36.44           C  
ANISOU 4803  CG  TYR C 142     3238   5004   5603    195      9   -743       C  
ATOM   4804  CD1 TYR C 142      -3.402  55.990  58.455  1.00 38.71           C  
ANISOU 4804  CD1 TYR C 142     3522   5272   5915    288    -78   -723       C  
ATOM   4805  CD2 TYR C 142      -2.834  54.528  60.248  1.00 37.44           C  
ANISOU 4805  CD2 TYR C 142     3343   5191   5693     52      4   -718       C  
ATOM   4806  CE1 TYR C 142      -3.956  54.930  57.759  1.00 37.34           C  
ANISOU 4806  CE1 TYR C 142     3316   5141   5730    239   -175   -698       C  
ATOM   4807  CE2 TYR C 142      -3.385  53.464  59.561  1.00 38.42           C  
ANISOU 4807  CE2 TYR C 142     3439   5338   5820     -7    -90   -683       C  
ATOM   4808  CZ  TYR C 142      -3.943  53.671  58.317  1.00 37.21           C  
ANISOU 4808  CZ  TYR C 142     3277   5168   5693     85   -183   -683       C  
ATOM   4809  OH  TYR C 142      -4.494  52.614  57.634  1.00 37.40           O  
ANISOU 4809  OH  TYR C 142     3273   5213   5724     27   -293   -667       O  
ATOM   4810  N   ILE C 143      -2.851  57.499  63.626  1.00 41.22           N  
ANISOU 4810  N   ILE C 143     4153   5367   6141    584    193  -1328       N  
ATOM   4811  CA  ILE C 143      -2.074  57.538  64.858  1.00 40.71           C  
ANISOU 4811  CA  ILE C 143     4129   5311   6027    546    227  -1358       C  
ATOM   4812  C   ILE C 143      -1.054  56.410  64.755  1.00 39.54           C  
ANISOU 4812  C   ILE C 143     4050   5152   5820    474    219  -1277       C  
ATOM   4813  O   ILE C 143      -1.416  55.229  64.813  1.00 40.15           O  
ANISOU 4813  O   ILE C 143     4119   5282   5854    416    235  -1244       O  
ATOM   4814  CB  ILE C 143      -2.967  57.383  66.096  1.00 41.07           C  
ANISOU 4814  CB  ILE C 143     4110   5471   6025    526    289  -1434       C  
ATOM   4815  CG1 ILE C 143      -3.988  58.520  66.163  1.00 39.46           C  
ANISOU 4815  CG1 ILE C 143     3829   5280   5884    614    296  -1528       C  
ATOM   4816  CG2 ILE C 143      -2.127  57.344  67.365  1.00 40.37           C  
ANISOU 4816  CG2 ILE C 143     4064   5411   5864    485    321  -1460       C  
ATOM   4817  CD1 ILE C 143      -5.206  58.199  67.002  1.00 39.87           C  
ANISOU 4817  CD1 ILE C 143     3785   5473   5889    600    358  -1591       C  
ATOM   4818  N   SER C 144       0.221  56.760  64.589  1.00 39.27           N  
ANISOU 4818  N   SER C 144     4082   5047   5792    479    191  -1244       N  
ATOM   4819  CA  SER C 144       1.239  55.787  64.216  1.00 38.73           C  
ANISOU 4819  CA  SER C 144     4074   4959   5681    435    172  -1166       C  
ATOM   4820  C   SER C 144       2.272  55.518  65.302  1.00 38.86           C  
ANISOU 4820  C   SER C 144     4137   4990   5637    390    189  -1163       C  
ATOM   4821  O   SER C 144       3.227  54.776  65.050  1.00 38.22           O  
ANISOU 4821  O   SER C 144     4105   4891   5526    364    170  -1101       O  
ATOM   4822  CB  SER C 144       1.956  56.246  62.939  1.00 39.09           C  
ANISOU 4822  CB  SER C 144     4150   4933   5772    475    123  -1111       C  
ATOM   4823  OG  SER C 144       2.791  57.361  63.201  1.00 40.83           O  
ANISOU 4823  OG  SER C 144     4393   5095   6027    495    112  -1122       O  
ATOM   4824  N   LYS C 145       2.113  56.085  66.501  1.00 42.68           N  
ANISOU 4824  N   LYS C 145     4603   5516   6099    387    221  -1234       N  
ATOM   4825  CA  LYS C 145       3.083  55.863  67.569  1.00 44.27           C  
ANISOU 4825  CA  LYS C 145     4842   5748   6231    348    231  -1234       C  
ATOM   4826  C   LYS C 145       2.392  55.582  68.899  1.00 46.40           C  
ANISOU 4826  C   LYS C 145     5076   6130   6426    317    284  -1284       C  
ATOM   4827  O   LYS C 145       2.950  55.861  69.966  1.00 47.78           O  
ANISOU 4827  O   LYS C 145     5262   6349   6542    305    296  -1324       O  
ATOM   4828  CB  LYS C 145       4.025  57.061  67.709  1.00 43.57           C  
ANISOU 4828  CB  LYS C 145     4775   5597   6181    375    203  -1276       C  
ATOM   4829  CG  LYS C 145       5.420  56.707  68.187  1.00 42.43           C  
ANISOU 4829  CG  LYS C 145     4680   5458   5983    338    186  -1238       C  
ATOM   4830  CD  LYS C 145       6.176  57.953  68.593  1.00 44.45           C  
ANISOU 4830  CD  LYS C 145     4942   5669   6277    351    162  -1304       C  
ATOM   4831  CE  LYS C 145       7.593  57.625  69.020  1.00 44.14           C  
ANISOU 4831  CE  LYS C 145     4940   5644   6186    313    139  -1267       C  
ATOM   4832  NZ  LYS C 145       8.297  58.849  69.484  1.00 44.34           N  
ANISOU 4832  NZ  LYS C 145     4965   5628   6255    315    111  -1342       N  
ATOM   4833  N   ALA C 146       1.186  55.029  68.854  1.00 41.55           N  
ANISOU 4833  N   ALA C 146     4411   5573   5804    302    317  -1280       N  
ATOM   4834  CA  ALA C 146       0.437  54.746  70.066  1.00 41.36           C  
ANISOU 4834  CA  ALA C 146     4338   5674   5701    269    376  -1316       C  
ATOM   4835  C   ALA C 146       0.932  53.466  70.727  1.00 43.44           C  
ANISOU 4835  C   ALA C 146     4639   5989   5877    192    390  -1225       C  
ATOM   4836  O   ALA C 146       1.394  52.532  70.065  1.00 44.88           O  
ANISOU 4836  O   ALA C 146     4868   6108   6077    162    359  -1136       O  
ATOM   4837  CB  ALA C 146      -1.053  54.627  69.756  1.00 40.52           C  
ANISOU 4837  CB  ALA C 146     4151   5620   5626    274    406  -1338       C  
ATOM   4838  N   SER C 147       0.841  53.440  72.054  1.00 38.15           N  
ANISOU 4838  N   SER C 147     3948   5438   5111    165    435  -1251       N  
ATOM   4839  CA  SER C 147       1.086  52.242  72.846  1.00 41.13           C  
ANISOU 4839  CA  SER C 147     4346   5886   5395     91    457  -1154       C  
ATOM   4840  C   SER C 147      -0.270  51.712  73.302  1.00 42.07           C  
ANISOU 4840  C   SER C 147     4388   6117   5478     42    519  -1139       C  
ATOM   4841  O   SER C 147      -0.968  52.359  74.089  1.00 42.43           O  
ANISOU 4841  O   SER C 147     4366   6284   5472     60    570  -1223       O  
ATOM   4842  CB  SER C 147       2.007  52.542  74.027  1.00 42.51           C  
ANISOU 4842  CB  SER C 147     4548   6135   5469     90    460  -1177       C  
ATOM   4843  OG  SER C 147       3.339  52.760  73.589  1.00 41.68           O  
ANISOU 4843  OG  SER C 147     4510   5929   5396    115    399  -1163       O  
ATOM   4844  N   VAL C 148      -0.660  50.556  72.774  1.00 36.98           N  
ANISOU 4844  N   VAL C 148     3749   5435   4867    -18    514  -1039       N  
ATOM   4845  CA  VAL C 148      -1.976  49.980  72.999  1.00 38.88           C  
ANISOU 4845  CA  VAL C 148     3910   5765   5098    -79    566  -1011       C  
ATOM   4846  C   VAL C 148      -1.855  48.887  74.050  1.00 39.55           C  
ANISOU 4846  C   VAL C 148     4007   5933   5087   -170    600   -894       C  
ATOM   4847  O   VAL C 148      -0.962  48.027  73.975  1.00 40.72           O  
ANISOU 4847  O   VAL C 148     4235   6000   5236   -201    559   -795       O  
ATOM   4848  CB  VAL C 148      -2.573  49.440  71.689  1.00 39.47           C  
ANISOU 4848  CB  VAL C 148     3974   5738   5284    -94    531   -983       C  
ATOM   4849  CG1 VAL C 148      -3.976  48.879  71.925  1.00 38.38           C  
ANISOU 4849  CG1 VAL C 148     3739   5699   5145   -167    583   -959       C  
ATOM   4850  CG2 VAL C 148      -2.607  50.544  70.638  1.00 35.85           C  
ANISOU 4850  CG2 VAL C 148     3508   5203   4909      1    492  -1080       C  
ATOM   4851  N   VAL C 149      -2.761  48.937  75.023  1.00 37.79           N  
ANISOU 4851  N   VAL C 149     3699   5878   4782   -207    674   -903       N  
ATOM   4852  CA  VAL C 149      -2.782  48.093  76.209  1.00 40.99           C  
ANISOU 4852  CA  VAL C 149     4096   6408   5071   -291    721   -792       C  
ATOM   4853  C   VAL C 149      -3.976  47.158  76.106  1.00 41.74           C  
ANISOU 4853  C   VAL C 149     4120   6542   5197   -390    760   -705       C  
ATOM   4854  O   VAL C 149      -5.112  47.611  75.883  1.00 42.07           O  
ANISOU 4854  O   VAL C 149     4062   6654   5267   -382    799   -780       O  
ATOM   4855  CB  VAL C 149      -2.881  48.940  77.490  1.00 40.29           C  
ANISOU 4855  CB  VAL C 149     3953   6515   4841   -257    783   -876       C  
ATOM   4856  CG1 VAL C 149      -2.837  48.055  78.729  1.00 42.75           C  
ANISOU 4856  CG1 VAL C 149     4256   6973   5013   -344    830   -744       C  
ATOM   4857  CG2 VAL C 149      -1.793  49.997  77.523  1.00 39.42           C  
ANISOU 4857  CG2 VAL C 149     3901   6355   4722   -162    737   -988       C  
ATOM   4858  N   THR C 150      -3.712  45.861  76.280  1.00 44.07           N  
ANISOU 4858  N   THR C 150     4463   6788   5493   -484    746   -545       N  
ATOM   4859  CA  THR C 150      -4.730  44.821  76.341  1.00 48.29           C  
ANISOU 4859  CA  THR C 150     4938   7353   6057   -604    780   -434       C  
ATOM   4860  C   THR C 150      -4.429  43.908  77.522  1.00 50.03           C  
ANISOU 4860  C   THR C 150     5180   7658   6170   -693    812   -269       C  
ATOM   4861  O   THR C 150      -3.292  43.831  77.990  1.00 49.11           O  
ANISOU 4861  O   THR C 150     5150   7520   5991   -661    781   -226       O  
ATOM   4862  CB  THR C 150      -4.770  43.990  75.053  1.00 48.62           C  
ANISOU 4862  CB  THR C 150     5026   7191   6257   -638    708   -394       C  
ATOM   4863  OG1 THR C 150      -3.458  43.480  74.780  1.00 48.54           O  
ANISOU 4863  OG1 THR C 150     5142   7027   6273   -612    635   -337       O  
ATOM   4864  CG2 THR C 150      -5.232  44.837  73.881  1.00 45.14           C  
ANISOU 4864  CG2 THR C 150     4547   6694   5909   -558    680   -541       C  
ATOM   4865  N   ALA C 151      -5.456  43.208  78.001  1.00 54.64           N  
ANISOU 4865  N   ALA C 151     5682   8344   6735   -808    872   -167       N  
ATOM   4866  CA  ALA C 151      -5.278  42.240  79.085  1.00 58.62           C  
ANISOU 4866  CA  ALA C 151     6201   8927   7144   -909    903     23       C  
ATOM   4867  C   ALA C 151      -6.467  41.289  79.182  1.00 62.44           C  
ANISOU 4867  C   ALA C 151     6599   9451   7673  -1058    949    151       C  
ATOM   4868  O   ALA C 151      -7.350  41.294  78.326  1.00 63.52           O  
ANISOU 4868  O   ALA C 151     6673   9537   7926  -1082    945     88       O  
ATOM   4869  CB  ALA C 151      -5.066  42.956  80.415  1.00 57.35           C  
ANISOU 4869  CB  ALA C 151     6003   9005   6784   -869    971     -4       C  
ATOM   4870  N   ASP C 158      -5.588  39.690  85.695  1.00103.34           N  
ANISOU 4870  N   ASP C 158    11710  15562  11994  -1307   1217    857       N  
ATOM   4871  CA  ASP C 158      -4.255  39.594  86.280  1.00104.84           C  
ANISOU 4871  CA  ASP C 158    12010  15742  12084  -1245   1161    919       C  
ATOM   4872  C   ASP C 158      -3.229  40.340  85.423  1.00103.55           C  
ANISOU 4872  C   ASP C 158    11943  15391  12011  -1100   1068    726       C  
ATOM   4873  O   ASP C 158      -3.472  40.625  84.249  1.00101.75           O  
ANISOU 4873  O   ASP C 158    11723  14985  11953  -1066   1032    598       O  
ATOM   4874  CB  ASP C 158      -3.853  38.126  86.453  1.00107.11           C  
ANISOU 4874  CB  ASP C 158    12380  15889  12428  -1352   1112   1201       C  
ATOM   4875  CG  ASP C 158      -2.483  37.964  87.088  1.00107.57           C  
ANISOU 4875  CG  ASP C 158    12543  15947  12380  -1285   1049   1282       C  
ATOM   4876  OD1 ASP C 158      -1.668  37.181  86.556  1.00107.82           O  
ANISOU 4876  OD1 ASP C 158    12692  15728  12546  -1278    952   1378       O  
ATOM   4877  OD2 ASP C 158      -2.214  38.636  88.107  1.00107.16           O  
ANISOU 4877  OD2 ASP C 158    12454  16152  12111  -1231   1093   1237       O  
ATOM   4878  N   PHE C 159      -2.075  40.640  86.021  1.00103.02           N  
ANISOU 4878  N   PHE C 159    11943  15374  11825  -1020   1028    716       N  
ATOM   4879  CA  PHE C 159      -1.078  41.506  85.409  1.00101.01           C  
ANISOU 4879  CA  PHE C 159    11760  14996  11621   -885    953    527       C  
ATOM   4880  C   PHE C 159      -0.104  40.781  84.492  1.00100.48           C  
ANISOU 4880  C   PHE C 159    11819  14635  11721   -865    843    596       C  
ATOM   4881  O   PHE C 159       0.479  41.421  83.608  1.00 97.59           O  
ANISOU 4881  O   PHE C 159    11501  14126  11454   -771    785    439       O  
ATOM   4882  CB  PHE C 159      -0.287  42.233  86.498  1.00100.20           C  
ANISOU 4882  CB  PHE C 159    11659  15101  11311   -809    958    463       C  
ATOM   4883  CG  PHE C 159      -0.051  43.677  86.201  1.00 97.51           C  
ANISOU 4883  CG  PHE C 159    11300  14780  10968   -689    949    193       C  
ATOM   4884  CD1 PHE C 159      -1.115  44.554  86.092  1.00 96.41           C  
ANISOU 4884  CD1 PHE C 159    11059  14747  10827   -669   1020     27       C  
ATOM   4885  CD2 PHE C 159       1.233  44.157  86.023  1.00 95.61           C  
ANISOU 4885  CD2 PHE C 159    11142  14448  10738   -596    865    107       C  
ATOM   4886  CE1 PHE C 159      -0.902  45.885  85.815  1.00 94.60           C  
ANISOU 4886  CE1 PHE C 159    10818  14514  10613   -557   1005   -216       C  
ATOM   4887  CE2 PHE C 159       1.453  45.487  85.746  1.00 93.72           C  
ANISOU 4887  CE2 PHE C 159    10887  14211  10512   -497    853   -133       C  
ATOM   4888  CZ  PHE C 159       0.383  46.351  85.640  1.00 93.56           C  
ANISOU 4888  CZ  PHE C 159    10773  14277  10497   -476    920   -293       C  
ATOM   4889  N   ASN C 160       0.105  39.477  84.683  1.00 98.86           N  
ANISOU 4889  N   ASN C 160    11670  14340  11552   -947    812    826       N  
ATOM   4890  CA  ASN C 160       0.999  38.745  83.791  1.00 97.74           C  
ANISOU 4890  CA  ASN C 160    11644  13917  11577   -918    707    880       C  
ATOM   4891  C   ASN C 160       0.453  38.703  82.370  1.00 97.05           C  
ANISOU 4891  C   ASN C 160    11559  13617  11699   -923    681    777       C  
ATOM   4892  O   ASN C 160       1.225  38.580  81.411  1.00 96.86           O  
ANISOU 4892  O   ASN C 160    11616  13384  11804   -855    598    722       O  
ATOM   4893  CB  ASN C 160       1.223  37.327  84.318  1.00 98.56           C  
ANISOU 4893  CB  ASN C 160    11803  13958  11688  -1006    678   1151       C  
ATOM   4894  CG  ASN C 160       2.683  36.913  84.274  1.00 98.71           C  
ANISOU 4894  CG  ASN C 160    11934  13844  11726   -923    577   1211       C  
ATOM   4895  OD1 ASN C 160       3.570  37.675  84.660  1.00 98.56           O  
ANISOU 4895  OD1 ASN C 160    11929  13928  11593   -826    557   1118       O  
ATOM   4896  ND2 ASN C 160       2.939  35.696  83.806  1.00 99.18           N  
ANISOU 4896  ND2 ASN C 160    12072  13673  11938   -961    509   1361       N  
ATOM   4897  N   LYS C 161      -0.865  38.811  82.214  1.00 84.84           N  
ANISOU 4897  N   LYS C 161     9916  12137  10181   -998    751    747       N  
ATOM   4898  CA  LYS C 161      -1.511  38.745  80.912  1.00 83.74           C  
ANISOU 4898  CA  LYS C 161     9765  11824  10229  -1011    727    656       C  
ATOM   4899  C   LYS C 161      -1.585  40.092  80.207  1.00 78.13           C  
ANISOU 4899  C   LYS C 161     9020  11131   9535   -902    731    412       C  
ATOM   4900  O   LYS C 161      -1.995  40.141  79.043  1.00 77.27           O  
ANISOU 4900  O   LYS C 161     8906  10881   9573   -892    701    324       O  
ATOM   4901  CB  LYS C 161      -2.925  38.178  81.064  1.00 86.00           C  
ANISOU 4901  CB  LYS C 161     9953  12175  10547  -1152    795    748       C  
ATOM   4902  CG  LYS C 161      -2.986  36.676  81.296  1.00 87.61           C  
ANISOU 4902  CG  LYS C 161    10202  12263  10825  -1280    768    990       C  
ATOM   4903  CD  LYS C 161      -4.400  36.254  81.641  1.00 88.90           C  
ANISOU 4903  CD  LYS C 161    10247  12541  10990  -1431    850   1086       C  
ATOM   4904  CE  LYS C 161      -4.545  34.746  81.664  1.00 88.20           C  
ANISOU 4904  CE  LYS C 161    10203  12286  11022  -1571    812   1319       C  
ATOM   4905  NZ  LYS C 161      -5.955  34.312  81.464  1.00 88.08           N  
ANISOU 4905  NZ  LYS C 161    10076  12297  11093  -1720    864   1367       N  
ATOM   4906  N   LEU C 162      -1.230  41.181  80.885  1.00 60.45           N  
ANISOU 4906  N   LEU C 162     6754   9063   7151   -821    764    304       N  
ATOM   4907  CA  LEU C 162      -1.288  42.496  80.263  1.00 57.37           C  
ANISOU 4907  CA  LEU C 162     6334   8676   6787   -718    764     81       C  
ATOM   4908  C   LEU C 162      -0.161  42.658  79.250  1.00 55.15           C  
ANISOU 4908  C   LEU C 162     6153   8187   6614   -628    669     14       C  
ATOM   4909  O   LEU C 162       0.988  42.286  79.503  1.00 57.19           O  
ANISOU 4909  O   LEU C 162     6494   8392   6844   -600    616     84       O  
ATOM   4910  CB  LEU C 162      -1.212  43.599  81.321  1.00 56.44           C  
ANISOU 4910  CB  LEU C 162     6161   8790   6492   -660    820    -24       C  
ATOM   4911  CG  LEU C 162      -1.509  45.024  80.842  1.00 54.02           C  
ANISOU 4911  CG  LEU C 162     5806   8507   6213   -562    833   -253       C  
ATOM   4912  CD1 LEU C 162      -2.353  45.767  81.868  1.00 53.22           C  
ANISOU 4912  CD1 LEU C 162     5590   8666   5964   -557    927   -335       C  
ATOM   4913  CD2 LEU C 162      -0.224  45.790  80.552  1.00 50.78           C  
ANISOU 4913  CD2 LEU C 162     5474   8004   5814   -456    762   -359       C  
ATOM   4914  N   ASN C 163      -0.498  43.227  78.097  1.00 50.61           N  
ANISOU 4914  N   ASN C 163     5563   7507   6158   -581    649   -119       N  
ATOM   4915  CA  ASN C 163       0.446  43.397  77.006  1.00 52.04           C  
ANISOU 4915  CA  ASN C 163     5825   7505   6444   -500    566   -183       C  
ATOM   4916  C   ASN C 163       0.314  44.791  76.415  1.00 47.94           C  
ANISOU 4916  C   ASN C 163     5269   6997   5949   -410    570   -369       C  
ATOM   4917  O   ASN C 163      -0.790  45.347  76.325  1.00 46.55           O  
ANISOU 4917  O   ASN C 163     5007   6898   5782   -416    620   -448       O  
ATOM   4918  CB  ASN C 163       0.233  42.337  75.922  1.00 53.99           C  
ANISOU 4918  CB  ASN C 163     6110   7560   6842   -544    515   -119       C  
ATOM   4919  CG  ASN C 163       0.799  40.989  76.319  1.00 60.97           C  
ANISOU 4919  CG  ASN C 163     7065   8364   7735   -602    479     57       C  
ATOM   4920  OD1 ASN C 163       1.978  40.871  76.657  1.00 63.20           O  
ANISOU 4920  OD1 ASN C 163     7417   8623   7972   -553    438     98       O  
ATOM   4921  ND2 ASN C 163      -0.045  39.968  76.310  1.00 64.62           N  
ANISOU 4921  ND2 ASN C 163     7507   8785   8260   -710    491    166       N  
ATOM   4922  N   VAL C 164       1.460  45.347  76.028  1.00 47.09           N  
ANISOU 4922  N   VAL C 164     5224   6813   5857   -327    515   -432       N  
ATOM   4923  CA  VAL C 164       1.552  46.667  75.422  1.00 44.05           C  
ANISOU 4923  CA  VAL C 164     4820   6409   5509   -240    505   -589       C  
ATOM   4924  C   VAL C 164       2.312  46.531  74.111  1.00 41.65           C  
ANISOU 4924  C   VAL C 164     4582   5925   5320   -193    431   -598       C  
ATOM   4925  O   VAL C 164       3.448  46.026  74.089  1.00 41.24           O  
ANISOU 4925  O   VAL C 164     4600   5805   5263   -178    383   -536       O  
ATOM   4926  CB  VAL C 164       2.246  47.685  76.342  1.00 43.10           C  
ANISOU 4926  CB  VAL C 164     4697   6397   5282   -188    515   -670       C  
ATOM   4927  CG1 VAL C 164       2.186  49.071  75.725  1.00 40.48           C  
ANISOU 4927  CG1 VAL C 164     4341   6030   5010   -108    505   -829       C  
ATOM   4928  CG2 VAL C 164       1.607  47.682  77.723  1.00 43.57           C  
ANISOU 4928  CG2 VAL C 164     4695   6659   5201   -233    587   -654       C  
ATOM   4929  N   GLY C 165       1.685  46.976  73.025  1.00 42.74           N  
ANISOU 4929  N   GLY C 165     4690   5997   5553   -164    423   -674       N  
ATOM   4930  CA  GLY C 165       2.324  46.957  71.725  1.00 40.97           C  
ANISOU 4930  CA  GLY C 165     4516   5629   5423   -113    359   -692       C  
ATOM   4931  C   GLY C 165       1.937  48.185  70.929  1.00 40.17           C  
ANISOU 4931  C   GLY C 165     4374   5513   5376    -48    357   -808       C  
ATOM   4932  O   GLY C 165       0.947  48.849  71.224  1.00 40.93           O  
ANISOU 4932  O   GLY C 165     4400   5689   5462    -47    401   -873       O  
ATOM   4933  N   THR C 166       2.734  48.487  69.912  1.00 51.30           N  
ANISOU 4933  N   THR C 166     5826   6824   6843      9    305   -829       N  
ATOM   4934  CA  THR C 166       2.438  49.619  69.046  1.00 52.13           C  
ANISOU 4934  CA  THR C 166     5899   6900   7006     72    294   -916       C  
ATOM   4935  C   THR C 166       1.820  49.118  67.745  1.00 50.69           C  
ANISOU 4935  C   THR C 166     5706   6650   6903     74    266   -907       C  
ATOM   4936  O   THR C 166       2.369  48.230  67.084  1.00 51.69           O  
ANISOU 4936  O   THR C 166     5881   6703   7054     69    225   -858       O  
ATOM   4937  CB  THR C 166       3.686  50.470  68.782  1.00 52.04           C  
ANISOU 4937  CB  THR C 166     5929   6844   7002    130    260   -943       C  
ATOM   4938  OG1 THR C 166       3.338  51.584  67.950  1.00 53.91           O  
ANISOU 4938  OG1 THR C 166     6135   7046   7303    186    249  -1009       O  
ATOM   4939  CG2 THR C 166       4.798  49.661  68.125  1.00 50.36           C  
ANISOU 4939  CG2 THR C 166     5779   6554   6802    139    211   -875       C  
ATOM   4940  N   TYR C 167       0.657  49.666  67.404  1.00 43.93           N  
ANISOU 4940  N   TYR C 167     4782   5827   6083     86    284   -963       N  
ATOM   4941  CA  TYR C 167      -0.084  49.263  66.220  1.00 43.27           C  
ANISOU 4941  CA  TYR C 167     4673   5703   6066     88    255   -967       C  
ATOM   4942  C   TYR C 167      -0.595  50.507  65.515  1.00 42.28           C  
ANISOU 4942  C   TYR C 167     4498   5581   5983    160    247  -1038       C  
ATOM   4943  O   TYR C 167      -0.966  51.487  66.168  1.00 43.34           O  
ANISOU 4943  O   TYR C 167     4592   5770   6107    188    282  -1093       O  
ATOM   4944  CB  TYR C 167      -1.257  48.344  66.581  1.00 43.72           C  
ANISOU 4944  CB  TYR C 167     4677   5809   6127      6    284   -943       C  
ATOM   4945  CG  TYR C 167      -0.875  47.183  67.468  1.00 48.34           C  
ANISOU 4945  CG  TYR C 167     5304   6393   6671    -73    298   -857       C  
ATOM   4946  CD1 TYR C 167      -0.232  46.067  66.947  1.00 48.96           C  
ANISOU 4946  CD1 TYR C 167     5449   6372   6781    -94    249   -799       C  
ATOM   4947  CD2 TYR C 167      -1.151  47.205  68.830  1.00 49.18           C  
ANISOU 4947  CD2 TYR C 167     5381   6601   6705   -120    358   -833       C  
ATOM   4948  CE1 TYR C 167       0.121  45.004  67.753  1.00 51.11           C  
ANISOU 4948  CE1 TYR C 167     5763   6628   7028   -161    255   -708       C  
ATOM   4949  CE2 TYR C 167      -0.802  46.146  69.646  1.00 52.86           C  
ANISOU 4949  CE2 TYR C 167     5886   7070   7130   -192    368   -734       C  
ATOM   4950  CZ  TYR C 167      -0.165  45.048  69.102  1.00 54.78           C  
ANISOU 4950  CZ  TYR C 167     6200   7196   7419   -212    314   -667       C  
ATOM   4951  OH  TYR C 167       0.186  43.989  69.908  1.00 59.12           O  
ANISOU 4951  OH  TYR C 167     6791   7733   7939   -278    317   -558       O  
ATOM   4952  N   ARG C 168      -0.609  50.470  64.186  1.00 34.25           N  
ANISOU 4952  N   ARG C 168     3487   4511   5015    198    199  -1038       N  
ATOM   4953  CA  ARG C 168      -1.122  51.603  63.433  1.00 33.60           C  
ANISOU 4953  CA  ARG C 168     3359   4431   4977    269    184  -1085       C  
ATOM   4954  C   ARG C 168      -2.624  51.735  63.654  1.00 36.60           C  
ANISOU 4954  C   ARG C 168     3645   4884   5377    257    213  -1130       C  
ATOM   4955  O   ARG C 168      -3.347  50.739  63.761  1.00 35.47           O  
ANISOU 4955  O   ARG C 168     3470   4776   5232    190    223  -1116       O  
ATOM   4956  CB  ARG C 168      -0.792  51.456  61.948  1.00 33.17           C  
ANISOU 4956  CB  ARG C 168     3327   4324   4950    311    125  -1065       C  
ATOM   4957  CG  ARG C 168      -1.697  50.523  61.169  1.00 34.02           C  
ANISOU 4957  CG  ARG C 168     3399   4448   5080    282     99  -1070       C  
ATOM   4958  CD  ARG C 168      -1.075  50.210  59.826  1.00 33.70           C  
ANISOU 4958  CD  ARG C 168     3396   4367   5041    321     41  -1053       C  
ATOM   4959  NE  ARG C 168      -2.031  49.642  58.888  1.00 34.64           N  
ANISOU 4959  NE  ARG C 168     3468   4510   5184    314      3  -1081       N  
ATOM   4960  CZ  ARG C 168      -1.727  48.696  58.008  1.00 42.23           C  
ANISOU 4960  CZ  ARG C 168     4459   5446   6140    309    -44  -1083       C  
ATOM   4961  NH1 ARG C 168      -0.491  48.216  57.957  1.00 38.06           N  
ANISOU 4961  NH1 ARG C 168     4006   4868   5586    317    -55  -1055       N  
ATOM   4962  NH2 ARG C 168      -2.655  48.230  57.183  1.00 45.61           N  
ANISOU 4962  NH2 ARG C 168     4837   5904   6590    300    -83  -1122       N  
ATOM   4963  N   ILE C 169      -3.085  52.978  63.750  1.00 41.07           N  
ANISOU 4963  N   ILE C 169     4164   5472   5968    323    225  -1186       N  
ATOM   4964  CA  ILE C 169      -4.438  53.297  64.186  1.00 40.92           C  
ANISOU 4964  CA  ILE C 169     4046   5541   5962    328    262  -1242       C  
ATOM   4965  C   ILE C 169      -4.993  54.312  63.194  1.00 43.70           C  
ANISOU 4965  C   ILE C 169     4352   5872   6379    421    224  -1277       C  
ATOM   4966  O   ILE C 169      -4.653  55.499  63.255  1.00 43.08           O  
ANISOU 4966  O   ILE C 169     4286   5752   6331    494    217  -1307       O  
ATOM   4967  CB  ILE C 169      -4.468  53.844  65.618  1.00 43.09           C  
ANISOU 4967  CB  ILE C 169     4301   5879   6193    326    323  -1292       C  
ATOM   4968  CG1 ILE C 169      -3.995  52.779  66.614  1.00 45.68           C  
ANISOU 4968  CG1 ILE C 169     4667   6244   6445    231    359  -1240       C  
ATOM   4969  CG2 ILE C 169      -5.853  54.328  65.982  1.00 41.69           C  
ANISOU 4969  CG2 ILE C 169     4009   5800   6029    352    362  -1363       C  
ATOM   4970  CD1 ILE C 169      -5.000  51.678  66.857  1.00 48.12           C  
ANISOU 4970  CD1 ILE C 169     4915   6631   6739    144    390  -1207       C  
ATOM   4971  N   GLN C 170      -5.840  53.853  62.274  1.00 39.50           N  
ANISOU 4971  N   GLN C 170     3766   5366   5874    418    193  -1270       N  
ATOM   4972  CA  GLN C 170      -6.459  54.733  61.292  1.00 40.33           C  
ANISOU 4972  CA  GLN C 170     3821   5468   6036    509    151  -1291       C  
ATOM   4973  C   GLN C 170      -7.715  55.356  61.879  1.00 40.40           C  
ANISOU 4973  C   GLN C 170     3720   5561   6069    545    187  -1363       C  
ATOM   4974  O   GLN C 170      -8.606  54.643  62.348  1.00 41.91           O  
ANISOU 4974  O   GLN C 170     3838   5844   6242    482    223  -1382       O  
ATOM   4975  CB  GLN C 170      -6.814  53.981  60.011  1.00 41.12           C  
ANISOU 4975  CB  GLN C 170     3904   5576   6144    496     94  -1262       C  
ATOM   4976  CG  GLN C 170      -7.431  54.880  58.945  1.00 41.27           C  
ANISOU 4976  CG  GLN C 170     3868   5604   6207    595     43  -1269       C  
ATOM   4977  CD  GLN C 170      -7.846  54.126  57.698  1.00 43.15           C  
ANISOU 4977  CD  GLN C 170     4080   5875   6439    584    -17  -1253       C  
ATOM   4978  OE1 GLN C 170      -7.495  52.961  57.519  1.00 41.80           O  
ANISOU 4978  OE1 GLN C 170     3949   5696   6238    508    -27  -1239       O  
ATOM   4979  NE2 GLN C 170      -8.598  54.791  56.827  1.00 40.87           N  
ANISOU 4979  NE2 GLN C 170     3725   5624   6180    665    -62  -1260       N  
ATOM   4980  N   VAL C 171      -7.789  56.684  61.841  1.00 38.59           N  
ANISOU 4980  N   VAL C 171     3476   5299   5889    647    177  -1401       N  
ATOM   4981  CA  VAL C 171      -8.990  57.377  62.293  1.00 37.90           C  
ANISOU 4981  CA  VAL C 171     3278   5287   5834    708    204  -1480       C  
ATOM   4982  C   VAL C 171     -10.088  57.175  61.257  1.00 38.55           C  
ANISOU 4982  C   VAL C 171     3271   5427   5951    735    162  -1474       C  
ATOM   4983  O   VAL C 171      -9.955  57.589  60.100  1.00 42.97           O  
ANISOU 4983  O   VAL C 171     3848   5930   6548    799     95  -1433       O  
ATOM   4984  CB  VAL C 171      -8.711  58.866  62.529  1.00 39.71           C  
ANISOU 4984  CB  VAL C 171     3524   5441   6122    817    195  -1529       C  
ATOM   4985  CG1 VAL C 171      -9.983  59.580  62.960  1.00 38.37           C  
ANISOU 4985  CG1 VAL C 171     3235   5351   5993    897    220  -1624       C  
ATOM   4986  CG2 VAL C 171      -7.619  59.042  63.576  1.00 38.31           C  
ANISOU 4986  CG2 VAL C 171     3429   5218   5908    782    231  -1548       C  
ATOM   4987  N   LYS C 172     -11.174  56.523  61.669  1.00 41.21           N  
ANISOU 4987  N   LYS C 172     3504   5885   6269    682    199  -1509       N  
ATOM   4988  CA  LYS C 172     -12.331  56.309  60.808  1.00 41.42           C  
ANISOU 4988  CA  LYS C 172     3423   5986   6326    701    160  -1516       C  
ATOM   4989  C   LYS C 172     -13.436  57.326  61.033  1.00 44.23           C  
ANISOU 4989  C   LYS C 172     3659   6415   6732    808    172  -1593       C  
ATOM   4990  O   LYS C 172     -14.198  57.616  60.105  1.00 43.96           O  
ANISOU 4990  O   LYS C 172     3550   6411   6740    875    117  -1594       O  
ATOM   4991  CB  LYS C 172     -12.902  54.904  61.027  1.00 42.12           C  
ANISOU 4991  CB  LYS C 172     3459   6164   6379    566    186  -1504       C  
ATOM   4992  CG  LYS C 172     -11.916  53.783  60.767  1.00 43.70           C  
ANISOU 4992  CG  LYS C 172     3771   6288   6543    465    166  -1436       C  
ATOM   4993  CD  LYS C 172     -11.428  53.804  59.331  1.00 43.40           C  
ANISOU 4993  CD  LYS C 172     3791   6176   6522    512     79  -1399       C  
ATOM   4994  CE  LYS C 172     -11.035  52.412  58.877  1.00 43.97           C  
ANISOU 4994  CE  LYS C 172     3916   6220   6570    407     50  -1362       C  
ATOM   4995  NZ  LYS C 172     -12.225  51.548  58.651  1.00 45.04           N  
ANISOU 4995  NZ  LYS C 172     3945   6444   6726    331     37  -1389       N  
ATOM   4996  N   ASP C 173     -13.545  57.864  62.243  1.00 53.99           N  
ANISOU 4996  N   ASP C 173     4869   7687   7957    832    241  -1661       N  
ATOM   4997  CA  ASP C 173     -14.602  58.808  62.580  1.00 53.99           C  
ANISOU 4997  CA  ASP C 173     4747   7765   8003    942    259  -1752       C  
ATOM   4998  C   ASP C 173     -14.119  59.653  63.751  1.00 52.29           C  
ANISOU 4998  C   ASP C 173     4568   7520   7780    993    313  -1828       C  
ATOM   4999  O   ASP C 173     -12.999  59.487  64.242  1.00 52.86           O  
ANISOU 4999  O   ASP C 173     4755   7519   7811    937    330  -1802       O  
ATOM   5000  CB  ASP C 173     -15.913  58.083  62.899  1.00 56.28           C  
ANISOU 5000  CB  ASP C 173     4882   8234   8267    883    304  -1786       C  
ATOM   5001  CG  ASP C 173     -17.139  58.917  62.578  1.00 58.37           C  
ANISOU 5001  CG  ASP C 173     5004   8579   8596   1011    284  -1856       C  
ATOM   5002  OD1 ASP C 173     -16.997  60.141  62.372  1.00 59.64           O  
ANISOU 5002  OD1 ASP C 173     5186   8653   8822   1154    248  -1892       O  
ATOM   5003  OD2 ASP C 173     -18.249  58.347  62.531  1.00 60.15           O  
ANISOU 5003  OD2 ASP C 173     5090   8950   8813    969    300  -1872       O  
ATOM   5004  N   ARG C 174     -14.979  60.572  64.196  1.00 59.39           N  
ANISOU 5004  N   ARG C 174     5364   8481   8720   1105    334  -1931       N  
ATOM   5005  CA  ARG C 174     -14.651  61.388  65.359  1.00 61.70           C  
ANISOU 5005  CA  ARG C 174     5676   8763   9003   1162    384  -2033       C  
ATOM   5006  C   ARG C 174     -14.439  60.544  66.609  1.00 61.95           C  
ANISOU 5006  C   ARG C 174     5708   8913   8916   1041    476  -2047       C  
ATOM   5007  O   ARG C 174     -13.762  60.996  67.539  1.00 62.67           O  
ANISOU 5007  O   ARG C 174     5857   8980   8974   1054    509  -2107       O  
ATOM   5008  CB  ARG C 174     -15.753  62.420  65.604  1.00 63.05           C  
ANISOU 5008  CB  ARG C 174     5718   9001   9239   1311    393  -2156       C  
ATOM   5009  CG  ARG C 174     -17.147  61.823  65.711  1.00 65.85           C  
ANISOU 5009  CG  ARG C 174     5899   9560   9560   1290    438  -2183       C  
ATOM   5010  CD  ARG C 174     -18.199  62.763  65.141  1.00 68.65           C  
ANISOU 5010  CD  ARG C 174     6160   9921  10002   1439    388  -2229       C  
ATOM   5011  NE  ARG C 174     -18.307  63.999  65.911  1.00 70.02           N  
ANISOU 5011  NE  ARG C 174     6365  10046  10195   1548    397  -2322       N  
ATOM   5012  CZ  ARG C 174     -18.999  64.119  67.039  1.00 72.79           C  
ANISOU 5012  CZ  ARG C 174     6643  10541  10474   1552    471  -2412       C  
ATOM   5013  NH1 ARG C 174     -19.648  63.074  67.536  1.00 74.45           N  
ANISOU 5013  NH1 ARG C 174     6742  10955  10589   1446    548  -2406       N  
ATOM   5014  NH2 ARG C 174     -19.042  65.283  67.673  1.00 73.37           N  
ANISOU 5014  NH2 ARG C 174     6749  10555  10571   1659    467  -2506       N  
ATOM   5015  N   ASP C 175     -14.993  59.326  66.648  1.00 46.86           N  
ANISOU 5015  N   ASP C 175     3732   7129   6943    920    512  -1989       N  
ATOM   5016  CA  ASP C 175     -14.837  58.447  67.801  1.00 46.22           C  
ANISOU 5016  CA  ASP C 175     3647   7164   6749    796    597  -1974       C  
ATOM   5017  C   ASP C 175     -14.581  56.998  67.394  1.00 49.34           C  
ANISOU 5017  C   ASP C 175     4086   7553   7109    638    587  -1843       C  
ATOM   5018  O   ASP C 175     -14.842  56.086  68.189  1.00 49.98           O  
ANISOU 5018  O   ASP C 175     4124   7755   7111    522    655  -1809       O  
ATOM   5019  CB  ASP C 175     -16.075  58.512  68.703  1.00 47.50           C  
ANISOU 5019  CB  ASP C 175     3641   7542   6864    812    682  -2062       C  
ATOM   5020  CG  ASP C 175     -17.357  58.145  67.968  1.00 49.88           C  
ANISOU 5020  CG  ASP C 175     3798   7940   7212    806    668  -2048       C  
ATOM   5021  OD1 ASP C 175     -17.308  57.936  66.736  1.00 49.70           O  
ANISOU 5021  OD1 ASP C 175     3811   7815   7259    804    586  -1982       O  
ATOM   5022  OD2 ASP C 175     -18.418  58.066  68.626  1.00 49.27           O  
ANISOU 5022  OD2 ASP C 175     3567   8057   7096    803    740  -2105       O  
ATOM   5023  N  AARG C 176     -14.090  56.755  66.183  0.64 47.33           N  
ANISOU 5023  N  AARG C 176     3911   7161   6910    631    504  -1770       N  
ATOM   5024  CA AARG C 176     -13.870  55.395  65.718  0.64 47.28           C  
ANISOU 5024  CA AARG C 176     3945   7136   6883    494    485  -1665       C  
ATOM   5025  C  AARG C 176     -12.539  55.316  64.990  0.64 46.87           C  
ANISOU 5025  C  AARG C 176     4050   6910   6847    495    418  -1600       C  
ATOM   5026  O  AARG C 176     -12.223  56.174  64.163  0.64 45.92           O  
ANISOU 5026  O  AARG C 176     3970   6693   6785    597    358  -1610       O  
ATOM   5027  CB AARG C 176     -15.003  54.927  64.800  0.64 48.71           C  
ANISOU 5027  CB AARG C 176     4015   7381   7114    474    448  -1655       C  
ATOM   5028  CG AARG C 176     -16.092  54.147  65.515  0.64 50.18           C  
ANISOU 5028  CG AARG C 176     4063   7740   7262    372    519  -1658       C  
ATOM   5029  CD AARG C 176     -17.202  53.744  64.559  0.64 51.52           C  
ANISOU 5029  CD AARG C 176     4115   7971   7490    352    472  -1657       C  
ATOM   5030  NE AARG C 176     -16.732  53.644  63.180  0.64 51.37           N  
ANISOU 5030  NE AARG C 176     4178   7820   7522    380    369  -1621       N  
ATOM   5031  CZ AARG C 176     -17.121  54.450  62.197  0.64 50.35           C  
ANISOU 5031  CZ AARG C 176     4009   7673   7448    503    301  -1655       C  
ATOM   5032  NH1AARG C 176     -17.989  55.422  62.438  0.64 51.87           N  
ANISOU 5032  NH1AARG C 176     4083   7957   7668    616    322  -1731       N  
ATOM   5033  NH2AARG C 176     -16.640  54.286  60.972  0.64 47.88           N  
ANISOU 5033  NH2AARG C 176     3771   7259   7161    520    212  -1613       N  
ATOM   5034  N  BARG C 176     -14.064  56.770  66.186  0.36 47.35           N  
ANISOU 5034  N  BARG C 176     3917   7161   6913    632    504  -1770       N  
ATOM   5035  CA BARG C 176     -13.885  55.436  65.625  0.36 47.38           C  
ANISOU 5035  CA BARG C 176     3958   7143   6902    501    479  -1666       C  
ATOM   5036  C  BARG C 176     -12.509  55.342  64.989  0.36 46.78           C  
ANISOU 5036  C  BARG C 176     4042   6895   6836    497    418  -1600       C  
ATOM   5037  O  BARG C 176     -12.138  56.215  64.198  0.36 45.83           O  
ANISOU 5037  O  BARG C 176     3966   6674   6772    599    358  -1610       O  
ATOM   5038  CB BARG C 176     -14.948  55.143  64.565  0.36 48.63           C  
ANISOU 5038  CB BARG C 176     4013   7346   7118    504    431  -1660       C  
ATOM   5039  CG BARG C 176     -15.825  53.949  64.833  0.36 50.13           C  
ANISOU 5039  CG BARG C 176     4103   7661   7283    367    469  -1628       C  
ATOM   5040  CD BARG C 176     -17.177  54.157  64.167  0.36 51.18           C  
ANISOU 5040  CD BARG C 176     4078   7896   7471    412    442  -1674       C  
ATOM   5041  NE BARG C 176     -18.115  53.071  64.434  0.36 52.27           N  
ANISOU 5041  NE BARG C 176     4099   8164   7595    274    479  -1647       N  
ATOM   5042  CZ BARG C 176     -18.656  52.822  65.622  0.36 54.00           C  
ANISOU 5042  CZ BARG C 176     4227   8530   7759    207    577  -1656       C  
ATOM   5043  NH1BARG C 176     -19.502  51.812  65.765  0.36 55.84           N  
ANISOU 5043  NH1BARG C 176     4351   8873   7992     68    604  -1616       N  
ATOM   5044  NH2BARG C 176     -18.355  53.578  66.669  0.36 54.12           N  
ANISOU 5044  NH2BARG C 176     4255   8589   7718    274    645  -1706       N  
ATOM   5045  N   VAL C 177     -11.772  54.273  65.300  1.00 39.79           N  
ANISOU 5045  N   VAL C 177     3238   5981   5900    381    431  -1525       N  
ATOM   5046  CA  VAL C 177     -10.458  54.056  64.713  1.00 41.03           C  
ANISOU 5046  CA  VAL C 177     3537   5993   6060    373    377  -1463       C  
ATOM   5047  C   VAL C 177     -10.370  52.632  64.180  1.00 42.29           C  
ANISOU 5047  C   VAL C 177     3726   6128   6215    260    349  -1386       C  
ATOM   5048  O   VAL C 177     -11.127  51.748  64.574  1.00 44.71           O  
ANISOU 5048  O   VAL C 177     3962   6517   6508    163    382  -1368       O  
ATOM   5049  CB  VAL C 177      -9.322  54.326  65.722  1.00 40.60           C  
ANISOU 5049  CB  VAL C 177     3577   5901   5950    368    412  -1461       C  
ATOM   5050  CG1 VAL C 177      -9.217  55.815  66.016  1.00 38.75           C  
ANISOU 5050  CG1 VAL C 177     3334   5645   5742    490    415  -1547       C  
ATOM   5051  CG2 VAL C 177      -9.543  53.539  67.006  1.00 40.92           C  
ANISOU 5051  CG2 VAL C 177     3586   6053   5909    267    489  -1443       C  
ATOM   5052  N   GLY C 178      -9.444  52.419  63.250  1.00 39.14           N  
ANISOU 5052  N   GLY C 178     3426   5612   5833    273    284  -1343       N  
ATOM   5053  CA  GLY C 178      -9.166  51.078  62.783  1.00 40.18           C  
ANISOU 5053  CA  GLY C 178     3604   5700   5963    178    252  -1284       C  
ATOM   5054  C   GLY C 178      -7.980  50.467  63.506  1.00 41.76           C  
ANISOU 5054  C   GLY C 178     3914   5838   6116    120    273  -1227       C  
ATOM   5055  O   GLY C 178      -7.130  51.176  64.037  1.00 41.63           O  
ANISOU 5055  O   GLY C 178     3955   5793   6069    168    292  -1231       O  
ATOM   5056  N   ILE C 179      -7.921  49.136  63.537  1.00 42.62           N  
ANISOU 5056  N   ILE C 179     4047   5921   6224     15    265  -1174       N  
ATOM   5057  CA  ILE C 179      -6.807  48.462  64.197  1.00 40.43           C  
ANISOU 5057  CA  ILE C 179     3872   5582   5907    -35    277  -1109       C  
ATOM   5058  C   ILE C 179      -6.581  47.101  63.554  1.00 42.06           C  
ANISOU 5058  C   ILE C 179     4127   5705   6150   -107    225  -1064       C  
ATOM   5059  O   ILE C 179      -7.518  46.442  63.095  1.00 43.15           O  
ANISOU 5059  O   ILE C 179     4202   5860   6334   -167    204  -1074       O  
ATOM   5060  CB  ILE C 179      -7.040  48.338  65.723  1.00 41.42           C  
ANISOU 5060  CB  ILE C 179     3967   5798   5973    -99    358  -1082       C  
ATOM   5061  CG1 ILE C 179      -5.717  48.068  66.447  1.00 41.28           C  
ANISOU 5061  CG1 ILE C 179     4057   5728   5900   -112    366  -1025       C  
ATOM   5062  CG2 ILE C 179      -8.064  47.256  66.037  1.00 44.38           C  
ANISOU 5062  CG2 ILE C 179     4268   6229   6364   -221    383  -1040       C  
ATOM   5063  CD1 ILE C 179      -5.815  48.179  67.954  1.00 42.17           C  
ANISOU 5063  CD1 ILE C 179     4143   5948   5931   -152    443  -1005       C  
ATOM   5064  N   GLN C 180      -5.314  46.690  63.513  1.00 51.40           N  
ANISOU 5064  N   GLN C 180     5420   6795   7315    -98    200  -1023       N  
ATOM   5065  CA  GLN C 180      -4.925  45.383  62.986  1.00 54.96           C  
ANISOU 5065  CA  GLN C 180     5930   7149   7803   -153    148   -988       C  
ATOM   5066  C   GLN C 180      -4.978  44.388  64.137  1.00 57.75           C  
ANISOU 5066  C   GLN C 180     6298   7498   8147   -263    186   -908       C  
ATOM   5067  O   GLN C 180      -3.984  44.142  64.821  1.00 57.88           O  
ANISOU 5067  O   GLN C 180     6391   7477   8124   -266    198   -851       O  
ATOM   5068  CB  GLN C 180      -3.540  45.449  62.357  1.00 54.53           C  
ANISOU 5068  CB  GLN C 180     5976   7008   7733    -76    102   -985       C  
ATOM   5069  CG  GLN C 180      -3.481  46.259  61.074  1.00 54.53           C  
ANISOU 5069  CG  GLN C 180     5963   7012   7742     21     58  -1043       C  
ATOM   5070  CD  GLN C 180      -2.107  46.233  60.437  1.00 55.53           C  
ANISOU 5070  CD  GLN C 180     6179   7072   7848     87     19  -1032       C  
ATOM   5071  OE1 GLN C 180      -1.109  46.579  61.071  1.00 54.41           O  
ANISOU 5071  OE1 GLN C 180     6090   6914   7669    110     43   -997       O  
ATOM   5072  NE2 GLN C 180      -2.046  45.814  59.178  1.00 56.99           N  
ANISOU 5072  NE2 GLN C 180     6373   7230   8052    119    -42  -1066       N  
ATOM   5073  N   ALA C 181      -6.159  43.802  64.348  1.00 53.98           N  
ANISOU 5073  N   ALA C 181     5738   7065   7706   -360    203   -896       N  
ATOM   5074  CA  ALA C 181      -6.371  42.969  65.529  1.00 57.00           C  
ANISOU 5074  CA  ALA C 181     6116   7468   8075   -475    251   -803       C  
ATOM   5075  C   ALA C 181      -5.544  41.691  65.476  1.00 57.31           C  
ANISOU 5075  C   ALA C 181     6258   7364   8154   -526    203   -730       C  
ATOM   5076  O   ALA C 181      -5.057  41.221  66.511  1.00 56.68           O  
ANISOU 5076  O   ALA C 181     6223   7277   8037   -574    234   -635       O  
ATOM   5077  CB  ALA C 181      -7.854  42.642  65.677  1.00 58.63           C  
ANISOU 5077  CB  ALA C 181     6199   7759   8319   -575    280   -802       C  
ATOM   5078  N   LEU C 182      -5.383  41.105  64.287  1.00 69.81           N  
ANISOU 5078  N   LEU C 182     7877   8835   9810   -509    123   -776       N  
ATOM   5079  CA  LEU C 182      -4.557  39.909  64.167  1.00 70.78           C  
ANISOU 5079  CA  LEU C 182     8101   8811   9983   -538     69   -725       C  
ATOM   5080  C   LEU C 182      -3.082  40.217  64.390  1.00 69.29           C  
ANISOU 5080  C   LEU C 182     8010   8584   9734   -443     65   -703       C  
ATOM   5081  O   LEU C 182      -2.328  39.325  64.793  1.00 69.00           O  
ANISOU 5081  O   LEU C 182     8052   8451   9714   -467     43   -630       O  
ATOM   5082  CB  LEU C 182      -4.776  39.256  62.798  1.00 70.54           C  
ANISOU 5082  CB  LEU C 182     8077   8683  10041   -532    -18   -807       C  
ATOM   5083  CG  LEU C 182      -3.999  37.985  62.438  1.00 70.66           C  
ANISOU 5083  CG  LEU C 182     8191   8528  10128   -545    -90   -790       C  
ATOM   5084  CD1 LEU C 182      -4.055  36.961  63.565  1.00 73.96           C  
ANISOU 5084  CD1 LEU C 182     8638   8878  10587   -665    -70   -661       C  
ATOM   5085  CD2 LEU C 182      -4.540  37.385  61.149  1.00 67.41           C  
ANISOU 5085  CD2 LEU C 182     7759   8051   9803   -556   -172   -893       C  
ATOM   5086  N   ALA C 183      -2.657  41.462  64.156  1.00 60.76           N  
ANISOU 5086  N   ALA C 183     6924   7574   8590   -339     82   -759       N  
ATOM   5087  CA  ALA C 183      -1.298  41.859  64.504  1.00 60.48           C  
ANISOU 5087  CA  ALA C 183     6964   7523   8493   -262     85   -734       C  
ATOM   5088  C   ALA C 183      -1.077  41.880  66.011  1.00 63.90           C  
ANISOU 5088  C   ALA C 183     7406   8014   8859   -309    145   -645       C  
ATOM   5089  O   ALA C 183       0.073  41.830  66.458  1.00 64.33           O  
ANISOU 5089  O   ALA C 183     7529   8042   8872   -271    139   -603       O  
ATOM   5090  CB  ALA C 183      -0.975  43.229  63.907  1.00 57.95           C  
ANISOU 5090  CB  ALA C 183     6627   7259   8132   -155     89   -809       C  
ATOM   5091  N   MET C 184      -2.147  41.963  66.798  1.00 74.09           N  
ANISOU 5091  N   MET C 184     8620   9400  10132   -388    204   -619       N  
ATOM   5092  CA  MET C 184      -2.070  41.788  68.242  1.00 77.01           C  
ANISOU 5092  CA  MET C 184     8989   9842  10430   -448    261   -524       C  
ATOM   5093  C   MET C 184      -2.312  40.313  68.542  1.00 82.05           C  
ANISOU 5093  C   MET C 184     9652  10397  11126   -560    243   -414       C  
ATOM   5094  O   MET C 184      -3.319  39.745  68.107  1.00 84.90           O  
ANISOU 5094  O   MET C 184     9961  10732  11564   -637    232   -419       O  
ATOM   5095  CB  MET C 184      -3.095  42.675  68.947  1.00 75.89           C  
ANISOU 5095  CB  MET C 184     8742   9864  10227   -468    340   -556       C  
ATOM   5096  CG  MET C 184      -3.403  43.973  68.211  1.00 73.87           C  
ANISOU 5096  CG  MET C 184     8438   9655   9977   -373    340   -682       C  
ATOM   5097  SD  MET C 184      -4.942  44.745  68.753  1.00 74.12           S  
ANISOU 5097  SD  MET C 184     8325   9858   9979   -400    418   -735       S  
ATOM   5098  CE  MET C 184      -4.470  45.341  70.373  1.00 72.73           C  
ANISOU 5098  CE  MET C 184     8152   9813   9670   -391    492   -709       C  
ATOM   5099  N   HIS C 185      -1.386  39.687  69.265  1.00101.61           N  
ANISOU 5099  N   HIS C 185    12207  12827  13573   -569    233   -313       N  
ATOM   5100  CA  HIS C 185      -1.377  38.232  69.365  1.00106.57           C  
ANISOU 5100  CA  HIS C 185    12883  13327  14281   -656    194   -206       C  
ATOM   5101  C   HIS C 185      -1.999  37.692  70.645  1.00111.74           C  
ANISOU 5101  C   HIS C 185    13500  14059  14898   -780    252    -64       C  
ATOM   5102  O   HIS C 185      -2.603  36.615  70.611  1.00113.84           O  
ANISOU 5102  O   HIS C 185    13761  14239  15254   -889    233     14       O  
ATOM   5103  CB  HIS C 185       0.057  37.706  69.232  1.00105.60           C  
ANISOU 5103  CB  HIS C 185    12872  13080  14170   -583    131   -171       C  
ATOM   5104  CG  HIS C 185       0.566  37.708  67.824  1.00103.00           C  
ANISOU 5104  CG  HIS C 185    12582  12640  13912   -491     60   -286       C  
ATOM   5105  ND1 HIS C 185       1.793  38.228  67.474  1.00101.21           N  
ANISOU 5105  ND1 HIS C 185    12407  12404  13643   -371     34   -334       N  
ATOM   5106  CD2 HIS C 185       0.005  37.262  66.675  1.00102.24           C  
ANISOU 5106  CD2 HIS C 185    12473  12455  13918   -502     10   -364       C  
ATOM   5107  CE1 HIS C 185       1.969  38.096  66.171  1.00 99.16           C  
ANISOU 5107  CE1 HIS C 185    12165  12062  13449   -311    -23   -430       C  
ATOM   5108  NE2 HIS C 185       0.898  37.513  65.663  1.00 99.93           N  
ANISOU 5108  NE2 HIS C 185    12227  12111  13632   -385    -41   -455       N  
ATOM   5109  N   ASP C 186      -1.881  38.398  71.767  1.00109.98           N  
ANISOU 5109  N   ASP C 186    13248  13999  14541   -770    322    -28       N  
ATOM   5110  CA  ASP C 186      -2.482  37.941  73.016  1.00114.87           C  
ANISOU 5110  CA  ASP C 186    13821  14725  15097   -885    387    111       C  
ATOM   5111  C   ASP C 186      -3.981  38.189  73.074  1.00113.86           C  
ANISOU 5111  C   ASP C 186    13567  14719  14977   -971    451     84       C  
ATOM   5112  O   ASP C 186      -4.580  38.077  74.150  1.00116.60           O  
ANISOU 5112  O   ASP C 186    13848  15211  15243  -1057    524    181       O  
ATOM   5113  CB  ASP C 186      -1.805  38.618  74.206  1.00117.75           C  
ANISOU 5113  CB  ASP C 186    14194  15244  15300   -837    436    145       C  
ATOM   5114  N   ILE C 187      -4.592  38.513  71.940  1.00 97.96           N  
ANISOU 5114  N   ILE C 187    11509  12663  13050   -946    424    -43       N  
ATOM   5115  CA  ILE C 187      -6.001  38.879  71.883  1.00 95.05           C  
ANISOU 5115  CA  ILE C 187    11007  12418  12689  -1007    478    -91       C  
ATOM   5116  C   ILE C 187      -6.809  37.936  71.003  1.00 93.49           C  
ANISOU 5116  C   ILE C 187    10781  12101  12641  -1104    428    -87       C  
ATOM   5117  O   ILE C 187      -8.045  37.909  71.122  1.00 92.39           O  
ANISOU 5117  O   ILE C 187    10522  12061  12518  -1194    473    -84       O  
ATOM   5118  CB  ILE C 187      -6.159  40.338  71.400  1.00 92.91           C  
ANISOU 5118  CB  ILE C 187    10685  12243  12374   -883    497   -259       C  
ATOM   5119  CG1 ILE C 187      -7.615  40.779  71.329  1.00 92.58           C  
ANISOU 5119  CG1 ILE C 187    10497  12339  12341   -926    550   -318       C  
ATOM   5120  CG2 ILE C 187      -5.540  40.504  70.042  1.00 90.95           C  
ANISOU 5120  CG2 ILE C 187    10506  11844  12208   -786    410   -360       C  
ATOM   5121  CD1 ILE C 187      -7.769  42.138  70.735  1.00 91.02           C  
ANISOU 5121  CD1 ILE C 187    10256  12201  12126   -797    552   -476       C  
ATOM   5122  N   ALA C 188      -6.149  37.120  70.173  1.00 83.14           N  
ANISOU 5122  N   ALA C 188     9570  10583  11438  -1091    335    -88       N  
ATOM   5123  CA  ALA C 188      -6.835  36.298  69.177  1.00 81.79           C  
ANISOU 5123  CA  ALA C 188     9378  10284  11414  -1164    270   -122       C  
ATOM   5124  C   ALA C 188      -7.962  35.468  69.784  1.00 83.37           C  
ANISOU 5124  C   ALA C 188     9492  10518  11665  -1345    307     -5       C  
ATOM   5125  O   ALA C 188      -9.108  35.529  69.324  1.00 83.21           O  
ANISOU 5125  O   ALA C 188     9362  10553  11700  -1409    314    -64       O  
ATOM   5126  CB  ALA C 188      -5.824  35.390  68.473  1.00 80.49           C  
ANISOU 5126  CB  ALA C 188     9344   9892  11346  -1128    169   -121       C  
ATOM   5127  N   VAL C 189      -7.655  34.679  70.816  1.00 92.67           N  
ANISOU 5127  N   VAL C 189    10714  11670  12828  -1432    330    170       N  
ATOM   5128  CA  VAL C 189      -8.677  33.823  71.413  1.00 92.86           C  
ANISOU 5128  CA  VAL C 189    10659  11719  12906  -1619    366    308       C  
ATOM   5129  C   VAL C 189      -9.753  34.664  72.093  1.00 92.28           C  
ANISOU 5129  C   VAL C 189    10429  11912  12721  -1659    478    301       C  
ATOM   5130  O   VAL C 189     -10.956  34.399  71.944  1.00 92.05           O  
ANISOU 5130  O   VAL C 189    10281  11939  12756  -1778    499    305       O  
ATOM   5131  CB  VAL C 189      -8.030  32.814  72.383  1.00 93.19           C  
ANISOU 5131  CB  VAL C 189    10788  11671  12948  -1695    363    517       C  
ATOM   5132  CG1 VAL C 189      -7.136  33.521  73.399  1.00 90.53           C  
ANISOU 5132  CG1 VAL C 189    10494  11473  12431  -1597    421    567       C  
ATOM   5133  CG2 VAL C 189      -9.096  31.979  73.081  1.00 94.59           C  
ANISOU 5133  CG2 VAL C 189    10876  11891  13173  -1899    409    685       C  
ATOM   5134  N   GLN C 190      -9.342  35.696  72.837  1.00 82.18           N  
ANISOU 5134  N   GLN C 190     9142  10805  11276  -1558    549    279       N  
ATOM   5135  CA  GLN C 190     -10.302  36.602  73.458  1.00 80.72           C  
ANISOU 5135  CA  GLN C 190     8810  10881  10980  -1566    654    242       C  
ATOM   5136  C   GLN C 190     -11.199  37.249  72.413  1.00 78.90           C  
ANISOU 5136  C   GLN C 190     8480  10685  10813  -1525    638     70       C  
ATOM   5137  O   GLN C 190     -12.406  37.396  72.627  1.00 77.72           O  
ANISOU 5137  O   GLN C 190     8182  10691  10658  -1603    699     66       O  
ATOM   5138  CB  GLN C 190      -9.566  37.673  74.264  1.00 79.61           C  
ANISOU 5138  CB  GLN C 190     8695  10887  10664  -1437    711    205       C  
ATOM   5139  CG  GLN C 190      -9.603  37.468  75.770  1.00 81.71           C  
ANISOU 5139  CG  GLN C 190     8929  11326  10790  -1513    800    363       C  
ATOM   5140  CD  GLN C 190      -9.225  38.722  76.535  1.00 81.38           C  
ANISOU 5140  CD  GLN C 190     8867  11481  10570  -1388    866    277       C  
ATOM   5141  OE1 GLN C 190      -8.046  39.050  76.667  1.00 81.37           O  
ANISOU 5141  OE1 GLN C 190     8976  11426  10515  -1285    831    255       O  
ATOM   5142  NE2 GLN C 190     -10.227  39.431  77.042  1.00 81.22           N  
ANISOU 5142  NE2 GLN C 190     8703  11695  10463  -1396    959    221       N  
ATOM   5143  N   LEU C 191     -10.629  37.617  71.263  1.00 71.77           N  
ANISOU 5143  N   LEU C 191     7651   9648   9970  -1404    555    -65       N  
ATOM   5144  CA  LEU C 191     -11.408  38.287  70.227  1.00 69.13           C  
ANISOU 5144  CA  LEU C 191     7229   9351   9687  -1348    532   -223       C  
ATOM   5145  C   LEU C 191     -12.389  37.335  69.555  1.00 69.17           C  
ANISOU 5145  C   LEU C 191     7164   9283   9835  -1486    485   -212       C  
ATOM   5146  O   LEU C 191     -13.535  37.711  69.282  1.00 68.75           O  
ANISOU 5146  O   LEU C 191     6969   9355   9798  -1513    510   -279       O  
ATOM   5147  CB  LEU C 191     -10.474  38.911  69.194  1.00 67.21           C  
ANISOU 5147  CB  LEU C 191     7085   8993   9457  -1186    456   -352       C  
ATOM   5148  CG  LEU C 191     -11.150  39.809  68.161  1.00 66.81           C  
ANISOU 5148  CG  LEU C 191     6952   8998   9434  -1099    433   -508       C  
ATOM   5149  CD1 LEU C 191     -11.990  40.873  68.847  1.00 65.97           C  
ANISOU 5149  CD1 LEU C 191     6713   9117   9237  -1068    527   -550       C  
ATOM   5150  CD2 LEU C 191     -10.106  40.440  67.267  1.00 66.05           C  
ANISOU 5150  CD2 LEU C 191     6960   8802   9333   -943    368   -604       C  
ATOM   5151  N   GLU C 192     -11.957  36.106  69.262  1.00 64.52           N  
ANISOU 5151  N   GLU C 192     6669   8489   9355  -1569    411   -136       N  
ATOM   5152  CA  GLU C 192     -12.881  35.124  68.703  1.00 65.86           C  
ANISOU 5152  CA  GLU C 192     6775   8577   9673  -1717    361   -123       C  
ATOM   5153  C   GLU C 192     -14.030  34.851  69.666  1.00 64.63           C  
ANISOU 5153  C   GLU C 192     6473   8584   9499  -1882    452     -4       C  
ATOM   5154  O   GLU C 192     -15.196  34.787  69.253  1.00 62.21           O  
ANISOU 5154  O   GLU C 192     6030   8350   9259  -1965    452    -52       O  
ATOM   5155  CB  GLU C 192     -12.140  33.830  68.364  1.00 68.97           C  
ANISOU 5155  CB  GLU C 192     7306   8708  10193  -1775    266    -57       C  
ATOM   5156  N   LYS C 193     -13.725  34.716  70.960  1.00 66.19           N  
ANISOU 5156  N   LYS C 193     6688   8863   9598  -1929    533    153       N  
ATOM   5157  CA  LYS C 193     -14.781  34.482  71.941  1.00 67.43           C  
ANISOU 5157  CA  LYS C 193     6699   9205   9716  -2084    632    279       C  
ATOM   5158  C   LYS C 193     -15.711  35.685  72.058  1.00 66.63           C  
ANISOU 5158  C   LYS C 193     6432   9368   9514  -2020    716    163       C  
ATOM   5159  O   LYS C 193     -16.927  35.522  72.210  1.00 66.63           O  
ANISOU 5159  O   LYS C 193     6270   9504   9542  -2141    764    188       O  
ATOM   5160  CB  LYS C 193     -14.170  34.142  73.300  1.00 68.14           C  
ANISOU 5160  CB  LYS C 193     6848   9345   9698  -2131    700    472       C  
ATOM   5161  N   ALA C 194     -15.161  36.901  71.983  1.00 69.09           N  
ANISOU 5161  N   ALA C 194     6778   9754   9718  -1830    732     35       N  
ATOM   5162  CA  ALA C 194     -15.983  38.098  72.133  1.00 65.08           C  
ANISOU 5162  CA  ALA C 194     6123   9484   9120  -1748    807    -82       C  
ATOM   5163  C   ALA C 194     -16.895  38.301  70.931  1.00 63.97           C  
ANISOU 5163  C   ALA C 194     5882   9332   9090  -1737    750   -219       C  
ATOM   5164  O   ALA C 194     -18.064  38.673  71.088  1.00 63.67           O  
ANISOU 5164  O   ALA C 194     5668   9487   9035  -1772    810   -255       O  
ATOM   5165  CB  ALA C 194     -15.093  39.322  72.343  1.00 60.97           C  
ANISOU 5165  CB  ALA C 194     5678   9012   8477  -1551    826   -183       C  
ATOM   5166  N   GLU C 195     -16.382  38.067  69.722  1.00 71.10           N  
ANISOU 5166  N   GLU C 195     6887  10027  10098  -1683    634   -300       N  
ATOM   5167  CA  GLU C 195     -17.200  38.246  68.530  1.00 71.86           C  
ANISOU 5167  CA  GLU C 195     6894  10119  10289  -1666    568   -431       C  
ATOM   5168  C   GLU C 195     -18.194  37.107  68.345  1.00 73.87           C  
ANISOU 5168  C   GLU C 195     7049  10347  10670  -1869    543   -366       C  
ATOM   5169  O   GLU C 195     -19.258  37.312  67.750  1.00 73.42           O  
ANISOU 5169  O   GLU C 195     6847  10384  10664  -1891    527   -453       O  
ATOM   5170  CB  GLU C 195     -16.305  38.393  67.297  1.00 72.13           C  
ANISOU 5170  CB  GLU C 195     7066   9964  10376  -1537    455   -541       C  
ATOM   5171  CG  GLU C 195     -15.488  39.680  67.300  1.00 72.42           C  
ANISOU 5171  CG  GLU C 195     7171  10040  10304  -1336    473   -623       C  
ATOM   5172  CD  GLU C 195     -14.786  39.943  65.982  1.00 72.07           C  
ANISOU 5172  CD  GLU C 195     7229   9850  10305  -1209    368   -733       C  
ATOM   5173  OE1 GLU C 195     -14.017  39.069  65.529  1.00 72.30           O  
ANISOU 5173  OE1 GLU C 195     7380   9692  10397  -1238    295   -705       O  
ATOM   5174  OE2 GLU C 195     -15.000  41.029  65.401  1.00 70.48           O  
ANISOU 5174  OE2 GLU C 195     6982   9724  10074  -1077    359   -845       O  
ATOM   5175  N   ALA C 196     -17.879  35.910  68.852  1.00 86.58           N  
ANISOU 5175  N   ALA C 196     8729  11830  12338  -2020    536   -212       N  
ATOM   5176  CA  ALA C 196     -18.862  34.832  68.829  1.00 88.79           C  
ANISOU 5176  CA  ALA C 196     8905  12088  12744  -2235    521   -131       C  
ATOM   5177  C   ALA C 196     -20.032  35.124  69.761  1.00 88.97           C  
ANISOU 5177  C   ALA C 196     8727  12385  12695  -2332    644    -63       C  
ATOM   5178  O   ALA C 196     -21.170  34.746  69.462  1.00 88.85           O  
ANISOU 5178  O   ALA C 196     8558  12433  12768  -2463    637    -71       O  
ATOM   5179  CB  ALA C 196     -18.202  33.506  69.202  1.00 90.57           C  
ANISOU 5179  CB  ALA C 196     9261  12096  13056  -2370    482     32       C  
ATOM   5180  N   GLU C 197     -19.775  35.792  70.884  1.00 80.20           N  
ANISOU 5180  N   GLU C 197     7605  11446  11420  -2270    757     -3       N  
ATOM   5181  CA  GLU C 197     -20.814  36.174  71.830  1.00 80.57           C  
ANISOU 5181  CA  GLU C 197     7459  11785  11370  -2335    886     48       C  
ATOM   5182  C   GLU C 197     -21.293  37.606  71.637  1.00 78.65           C  
ANISOU 5182  C   GLU C 197     7104  11746  11033  -2156    929   -130       C  
ATOM   5183  O   GLU C 197     -22.103  38.085  72.438  1.00 76.51           O  
ANISOU 5183  O   GLU C 197     6670  11737  10664  -2173   1042   -117       O  
ATOM   5184  CB  GLU C 197     -20.317  35.984  73.267  1.00 82.65           C  
ANISOU 5184  CB  GLU C 197     7764  12141  11498  -2384    988    224       C  
ATOM   5185  CG  GLU C 197     -20.403  34.550  73.763  1.00 86.30           C  
ANISOU 5185  CG  GLU C 197     8245  12500  12046  -2616    985    448       C  
ATOM   5186  CD  GLU C 197     -19.398  34.245  74.857  1.00 88.91           C  
ANISOU 5186  CD  GLU C 197     8707  12809  12268  -2620   1030    617       C  
ATOM   5187  OE1 GLU C 197     -18.851  35.199  75.449  1.00 88.44           O  
ANISOU 5187  OE1 GLU C 197     8678  12887  12038  -2466   1091    565       O  
ATOM   5188  OE2 GLU C 197     -19.156  33.048  75.123  1.00 91.06           O  
ANISOU 5188  OE2 GLU C 197     9049  12922  12627  -2778    998    801       O  
ATOM   5189  N   ASN C 198     -20.807  38.297  70.602  1.00 70.73           N  
ANISOU 5189  N   ASN C 198     6185  10632  10059  -1983    843   -293       N  
ATOM   5190  CA  ASN C 198     -21.244  39.655  70.269  1.00 68.53           C  
ANISOU 5190  CA  ASN C 198     5811  10508   9718  -1804    864   -462       C  
ATOM   5191  C   ASN C 198     -20.970  40.627  71.415  1.00 68.11           C  
ANISOU 5191  C   ASN C 198     5745  10640   9493  -1693    978   -466       C  
ATOM   5192  O   ASN C 198     -21.799  41.479  71.744  1.00 68.20           O  
ANISOU 5192  O   ASN C 198     5599  10875   9438  -1627   1052   -546       O  
ATOM   5193  CB  ASN C 198     -22.724  39.675  69.875  1.00 69.72           C  
ANISOU 5193  CB  ASN C 198     5741  10818   9932  -1875    873   -517       C  
ATOM   5194  CG  ASN C 198     -23.043  40.747  68.852  1.00 68.99           C  
ANISOU 5194  CG  ASN C 198     5599  10758   9858  -1693    815   -704       C  
ATOM   5195  OD1 ASN C 198     -22.159  41.236  68.148  1.00 67.88           O  
ANISOU 5195  OD1 ASN C 198     5604  10469   9721  -1546    741   -785       O  
ATOM   5196  ND2 ASN C 198     -24.317  41.114  68.762  1.00 70.23           N  
ANISOU 5196  ND2 ASN C 198     5544  11117  10025  -1704    849   -766       N  
ATOM   5197  N   LYS C 199     -19.791  40.502  72.026  1.00 64.10           N  
ANISOU 5197  N   LYS C 199     5400  10039   8914  -1666    989   -390       N  
ATOM   5198  CA  LYS C 199     -19.394  41.342  73.144  1.00 64.09           C  
ANISOU 5198  CA  LYS C 199     5406  10199   8747  -1568   1085   -397       C  
ATOM   5199  C   LYS C 199     -18.227  42.246  72.754  1.00 64.26           C  
ANISOU 5199  C   LYS C 199     5584  10094   8737  -1372   1030   -508       C  
ATOM   5200  O   LYS C 199     -17.398  41.874  71.917  1.00 62.92           O  
ANISOU 5200  O   LYS C 199     5562   9694   8652  -1350    930   -510       O  
ATOM   5201  CB  LYS C 199     -18.992  40.490  74.355  1.00 64.46           C  
ANISOU 5201  CB  LYS C 199     5498  10283   8713  -1704   1152   -202       C  
ATOM   5202  CG  LYS C 199     -20.160  40.077  75.239  1.00 66.37           C  
ANISOU 5202  CG  LYS C 199     5548  10767   8903  -1860   1262    -96       C  
ATOM   5203  CD  LYS C 199     -19.722  39.089  76.308  1.00 68.48           C  
ANISOU 5203  CD  LYS C 199     5874  11040   9107  -2011   1311    127       C  
ATOM   5204  CE  LYS C 199     -20.920  38.475  77.015  1.00 71.10           C  
ANISOU 5204  CE  LYS C 199     6013  11585   9417  -2202   1409    263       C  
ATOM   5205  NZ  LYS C 199     -21.523  39.410  78.007  1.00 72.24           N  
ANISOU 5205  NZ  LYS C 199     5999  12071   9376  -2132   1545    208       N  
ATOM   5206  N   PRO C 200     -18.139  43.442  73.333  1.00 73.16           N  
ANISOU 5206  N   PRO C 200     6681  11369   9748  -1227   1093   -607       N  
ATOM   5207  CA  PRO C 200     -17.001  44.323  73.043  1.00 71.47           C  
ANISOU 5207  CA  PRO C 200     6613  11034   9508  -1055   1043   -703       C  
ATOM   5208  C   PRO C 200     -15.707  43.751  73.604  1.00 71.18           C  
ANISOU 5208  C   PRO C 200     6746  10880   9420  -1089   1030   -589       C  
ATOM   5209  O   PRO C 200     -15.712  42.887  74.484  1.00 72.75           O  
ANISOU 5209  O   PRO C 200     6939  11136   9566  -1223   1081   -440       O  
ATOM   5210  CB  PRO C 200     -17.373  45.630  73.753  1.00 72.06           C  
ANISOU 5210  CB  PRO C 200     6590  11318   9472   -921   1125   -826       C  
ATOM   5211  CG  PRO C 200     -18.858  45.539  73.994  1.00 73.55           C  
ANISOU 5211  CG  PRO C 200     6564  11722   9658   -992   1197   -832       C  
ATOM   5212  CD  PRO C 200     -19.120  44.085  74.221  1.00 74.36           C  
ANISOU 5212  CD  PRO C 200     6652  11807   9796  -1209   1208   -650       C  
ATOM   5213  N   LEU C 201     -14.581  44.249  73.097  1.00 60.74           N  
ANISOU 5213  N   LEU C 201     5569   9398   8110   -966    961   -652       N  
ATOM   5214  CA  LEU C 201     -13.290  43.879  73.689  1.00 60.04           C  
ANISOU 5214  CA  LEU C 201     5633   9221   7960   -973    950   -562       C  
ATOM   5215  C   LEU C 201     -12.522  45.116  74.132  1.00 58.17           C  
ANISOU 5215  C   LEU C 201     5448   9030   7625   -817    968   -669       C  
ATOM   5216  O   LEU C 201     -11.999  45.853  73.279  1.00 55.94           O  
ANISOU 5216  O   LEU C 201     5232   8627   7398   -694    902   -775       O  
ATOM   5217  CB  LEU C 201     -12.453  43.049  72.718  1.00 59.35           C  
ANISOU 5217  CB  LEU C 201     5688   8877   7986   -998    842   -512       C  
ATOM   5218  CG  LEU C 201     -11.409  42.127  73.365  1.00 62.92           C  
ANISOU 5218  CG  LEU C 201     6268   9237   8403  -1066    831   -364       C  
ATOM   5219  CD1 LEU C 201     -10.909  41.180  72.311  1.00 62.73           C  
ANISOU 5219  CD1 LEU C 201     6348   8972   8515  -1103    726   -327       C  
ATOM   5220  CD2 LEU C 201     -10.218  42.850  74.010  1.00 63.88           C  
ANISOU 5220  CD2 LEU C 201     6487   9374   8411   -954    841   -389       C  
ATOM   5221  N   PRO C 202     -12.389  45.367  75.433  1.00 56.62           N  
ANISOU 5221  N   PRO C 202     5226   9002   7283   -819   1050   -642       N  
ATOM   5222  CA  PRO C 202     -11.784  46.628  75.884  1.00 55.31           C  
ANISOU 5222  CA  PRO C 202     5092   8893   7030   -670   1065   -771       C  
ATOM   5223  C   PRO C 202     -10.298  46.715  75.564  1.00 53.76           C  
ANISOU 5223  C   PRO C 202     5067   8508   6850   -607    986   -767       C  
ATOM   5224  O   PRO C 202      -9.545  45.753  75.736  1.00 53.46           O  
ANISOU 5224  O   PRO C 202     5126   8379   6807   -684    958   -634       O  
ATOM   5225  CB  PRO C 202     -12.021  46.613  77.400  1.00 57.69           C  
ANISOU 5225  CB  PRO C 202     5322   9436   7161   -715   1171   -724       C  
ATOM   5226  CG  PRO C 202     -13.069  45.561  77.635  1.00 59.77           C  
ANISOU 5226  CG  PRO C 202     5475   9801   7433   -876   1225   -590       C  
ATOM   5227  CD  PRO C 202     -12.857  44.547  76.560  1.00 58.94           C  
ANISOU 5227  CD  PRO C 202     5451   9458   7484   -958   1134   -498       C  
ATOM   5228  N   ILE C 203      -9.883  47.897  75.098  1.00 50.89           N  
ANISOU 5228  N   ILE C 203     4736   8087   6511   -465    950   -912       N  
ATOM   5229  CA  ILE C 203      -8.482  48.230  74.878  1.00 50.02           C  
ANISOU 5229  CA  ILE C 203     4769   7831   6405   -392    885   -929       C  
ATOM   5230  C   ILE C 203      -8.247  49.670  75.321  1.00 49.02           C  
ANISOU 5230  C   ILE C 203     4627   7774   6223   -262    904  -1083       C  
ATOM   5231  O   ILE C 203      -9.182  50.467  75.465  1.00 48.13           O  
ANISOU 5231  O   ILE C 203     4404   7778   6104   -204    948  -1194       O  
ATOM   5232  CB  ILE C 203      -8.038  48.062  73.403  1.00 49.13           C  
ANISOU 5232  CB  ILE C 203     4736   7498   6432   -362    787   -932       C  
ATOM   5233  CG1 ILE C 203      -8.712  49.108  72.512  1.00 46.78           C  
ANISOU 5233  CG1 ILE C 203     4373   7187   6214   -260    767  -1066       C  
ATOM   5234  CG2 ILE C 203      -8.319  46.655  72.894  1.00 50.03           C  
ANISOU 5234  CG2 ILE C 203     4863   7530   6617   -485    759   -807       C  
ATOM   5235  CD1 ILE C 203      -8.078  49.229  71.145  1.00 46.09           C  
ANISOU 5235  CD1 ILE C 203     4371   6908   6232   -203    674  -1083       C  
ATOM   5236  N   ALA C 204      -6.973  49.998  75.543  1.00 46.92           N  
ANISOU 5236  N   ALA C 204     4471   7432   5923   -214    865  -1094       N  
ATOM   5237  CA  ALA C 204      -6.584  51.367  75.865  1.00 46.12           C  
ANISOU 5237  CA  ALA C 204     4375   7356   5793    -95    864  -1245       C  
ATOM   5238  C   ALA C 204      -5.475  51.806  74.920  1.00 45.48           C  
ANISOU 5238  C   ALA C 204     4407   7068   5805    -30    774  -1268       C  
ATOM   5239  O   ALA C 204      -4.533  51.052  74.679  1.00 44.91           O  
ANISOU 5239  O   ALA C 204     4430   6893   5740    -75    729  -1166       O  
ATOM   5240  CB  ALA C 204      -6.130  51.490  77.323  1.00 44.05           C  
ANISOU 5240  CB  ALA C 204     4115   7253   5370   -104    915  -1254       C  
ATOM   5241  N   ILE C 205      -5.582  53.014  74.382  1.00 44.19           N  
ANISOU 5241  N   ILE C 205     4228   6847   5714     77    747  -1397       N  
ATOM   5242  CA  ILE C 205      -4.642  53.529  73.392  1.00 42.15           C  
ANISOU 5242  CA  ILE C 205     4061   6402   5551    137    666  -1412       C  
ATOM   5243  C   ILE C 205      -3.980  54.759  73.993  1.00 41.82           C  
ANISOU 5243  C   ILE C 205     4044   6362   5485    219    658  -1533       C  
ATOM   5244  O   ILE C 205      -4.638  55.786  74.184  1.00 41.47           O  
ANISOU 5244  O   ILE C 205     3932   6364   5462    297    679  -1661       O  
ATOM   5245  CB  ILE C 205      -5.344  53.872  72.070  1.00 41.00           C  
ANISOU 5245  CB  ILE C 205     3880   6166   5533    187    629  -1439       C  
ATOM   5246  CG1 ILE C 205      -6.006  52.628  71.469  1.00 42.07           C  
ANISOU 5246  CG1 ILE C 205     3987   6300   5696     99    628  -1335       C  
ATOM   5247  CG2 ILE C 205      -4.371  54.500  71.089  1.00 39.12           C  
ANISOU 5247  CG2 ILE C 205     3728   5754   5380    251    551  -1448       C  
ATOM   5248  CD1 ILE C 205      -6.826  52.914  70.227  1.00 41.70           C  
ANISOU 5248  CD1 ILE C 205     3888   6197   5757    145    591  -1366       C  
ATOM   5249  N   THR C 206      -2.688  54.676  74.294  1.00 44.46           N  
ANISOU 5249  N   THR C 206     4468   6644   5781    204    625  -1500       N  
ATOM   5250  CA  THR C 206      -1.975  55.789  74.901  1.00 44.33           C  
ANISOU 5250  CA  THR C 206     4476   6625   5743    267    609  -1616       C  
ATOM   5251  C   THR C 206      -1.099  56.478  73.863  1.00 44.04           C  
ANISOU 5251  C   THR C 206     4509   6398   5826    316    532  -1626       C  
ATOM   5252  O   THR C 206      -0.484  55.822  73.015  1.00 43.34           O  
ANISOU 5252  O   THR C 206     4482   6207   5780    283    490  -1518       O  
ATOM   5253  CB  THR C 206      -1.125  55.320  76.083  1.00 43.97           C  
ANISOU 5253  CB  THR C 206     4469   6679   5560    216    624  -1581       C  
ATOM   5254  OG1 THR C 206      -0.133  54.395  75.625  1.00 45.05           O  
ANISOU 5254  OG1 THR C 206     4691   6721   5706    161    579  -1443       O  
ATOM   5255  CG2 THR C 206      -2.003  54.645  77.130  1.00 45.62           C  
ANISOU 5255  CG2 THR C 206     4603   7092   5638    162    706  -1552       C  
ATOM   5256  N   ILE C 207      -1.060  57.806  73.932  1.00 46.51           N  
ANISOU 5256  N   ILE C 207     4811   6667   6196    396    513  -1759       N  
ATOM   5257  CA  ILE C 207      -0.320  58.639  72.993  1.00 46.96           C  
ANISOU 5257  CA  ILE C 207     4922   6546   6374    443    443  -1770       C  
ATOM   5258  C   ILE C 207       0.502  59.638  73.794  1.00 46.69           C  
ANISOU 5258  C   ILE C 207     4913   6497   6329    472    420  -1884       C  
ATOM   5259  O   ILE C 207      -0.005  60.243  74.746  1.00 44.96           O  
ANISOU 5259  O   ILE C 207     4643   6374   6064    511    454  -2017       O  
ATOM   5260  CB  ILE C 207      -1.262  59.369  72.016  1.00 48.77           C  
ANISOU 5260  CB  ILE C 207     5106   6697   6729    517    428  -1810       C  
ATOM   5261  CG1 ILE C 207      -2.086  58.363  71.210  1.00 48.57           C  
ANISOU 5261  CG1 ILE C 207     5047   6695   6711    483    443  -1707       C  
ATOM   5262  CG2 ILE C 207      -0.475  60.278  71.082  1.00 47.84           C  
ANISOU 5262  CG2 ILE C 207     5044   6399   6734    560    357  -1804       C  
ATOM   5263  CD1 ILE C 207      -3.347  58.948  70.617  1.00 48.08           C  
ANISOU 5263  CD1 ILE C 207     4906   6631   6733    555    447  -1763       C  
ATOM   5264  N   GLY C 208       1.766  59.812  73.408  1.00 43.17           N  
ANISOU 5264  N   GLY C 208     4540   5938   5923    453    363  -1839       N  
ATOM   5265  CA  GLY C 208       2.660  60.708  74.119  1.00 44.19           C  
ANISOU 5265  CA  GLY C 208     4694   6044   6051    465    331  -1942       C  
ATOM   5266  C   GLY C 208       3.159  60.099  75.412  1.00 45.12           C  
ANISOU 5266  C   GLY C 208     4817   6317   6009    415    357  -1952       C  
ATOM   5267  O   GLY C 208       2.540  60.274  76.465  1.00 46.47           O  
ANISOU 5267  O   GLY C 208     4937   6628   6089    433    402  -2056       O  
ATOM   5268  N   ASN C 209       4.282  59.388  75.353  1.00 39.93           N  
ANISOU 5268  N   ASN C 209     4215   5647   5309    358    328  -1844       N  
ATOM   5269  CA  ASN C 209       4.726  58.560  76.464  1.00 42.23           C  
ANISOU 5269  CA  ASN C 209     4514   6090   5443    307    349  -1809       C  
ATOM   5270  C   ASN C 209       6.203  58.782  76.750  1.00 41.93           C  
ANISOU 5270  C   ASN C 209     4523   6020   5388    284    290  -1811       C  
ATOM   5271  O   ASN C 209       6.943  59.345  75.937  1.00 41.60           O  
ANISOU 5271  O   ASN C 209     4512   5833   5461    291    236  -1803       O  
ATOM   5272  CB  ASN C 209       4.488  57.073  76.173  1.00 41.82           C  
ANISOU 5272  CB  ASN C 209     4474   6078   5337    254    378  -1641       C  
ATOM   5273  CG  ASN C 209       3.042  56.665  76.356  1.00 42.79           C  
ANISOU 5273  CG  ASN C 209     4534   6299   5425    252    447  -1640       C  
ATOM   5274  OD1 ASN C 209       2.458  56.889  77.415  1.00 45.30           O  
ANISOU 5274  OD1 ASN C 209     4799   6767   5646    260    495  -1724       O  
ATOM   5275  ND2 ASN C 209       2.456  56.061  75.328  1.00 39.90           N  
ANISOU 5275  ND2 ASN C 209     4165   5861   5133    240    451  -1550       N  
ATOM   5276  N   ASN C 210       6.613  58.337  77.932  1.00 45.89           N  
ANISOU 5276  N   ASN C 210     5023   6674   5742    254    301  -1816       N  
ATOM   5277  CA  ASN C 210       8.021  58.114  78.228  1.00 45.99           C  
ANISOU 5277  CA  ASN C 210     5074   6690   5709    221    248  -1773       C  
ATOM   5278  C   ASN C 210       8.647  57.345  77.068  1.00 43.98           C  
ANISOU 5278  C   ASN C 210     4866   6315   5530    199    219  -1613       C  
ATOM   5279  O   ASN C 210       8.086  56.331  76.635  1.00 42.79           O  
ANISOU 5279  O   ASN C 210     4722   6167   5370    184    251  -1499       O  
ATOM   5280  CB  ASN C 210       8.118  57.337  79.550  1.00 48.14           C  
ANISOU 5280  CB  ASN C 210     5335   7164   5790    191    275  -1745       C  
ATOM   5281  CG  ASN C 210       9.496  56.737  79.838  1.00 50.20           C  
ANISOU 5281  CG  ASN C 210     5635   7451   5987    157    223  -1654       C  
ATOM   5282  OD1 ASN C 210      10.435  56.795  79.048  1.00 49.36           O  
ANISOU 5282  OD1 ASN C 210     5561   7220   5973    152    170  -1606       O  
ATOM   5283  ND2 ASN C 210       9.610  56.153  81.025  1.00 53.92           N  
ANISOU 5283  ND2 ASN C 210     6094   8104   6287    136    239  -1628       N  
ATOM   5284  N   PRO C 211       9.775  57.808  76.521  1.00 41.68           N  
ANISOU 5284  N   PRO C 211     4601   5920   5317    196    158  -1608       N  
ATOM   5285  CA  PRO C 211      10.352  57.132  75.345  1.00 40.50           C  
ANISOU 5285  CA  PRO C 211     4486   5667   5236    186    134  -1469       C  
ATOM   5286  C   PRO C 211      10.613  55.651  75.552  1.00 41.92           C  
ANISOU 5286  C   PRO C 211     4690   5917   5321    160    145  -1332       C  
ATOM   5287  O   PRO C 211      10.509  54.873  74.594  1.00 40.56           O  
ANISOU 5287  O   PRO C 211     4539   5674   5198    162    147  -1228       O  
ATOM   5288  CB  PRO C 211      11.656  57.909  75.097  1.00 40.58           C  
ANISOU 5288  CB  PRO C 211     4504   5604   5309    177     72  -1498       C  
ATOM   5289  CG  PRO C 211      11.951  58.610  76.398  1.00 40.94           C  
ANISOU 5289  CG  PRO C 211     4528   5744   5282    169     55  -1630       C  
ATOM   5290  CD  PRO C 211      10.603  58.944  76.962  1.00 41.08           C  
ANISOU 5290  CD  PRO C 211     4518   5821   5269    197    108  -1730       C  
ATOM   5291  N   LEU C 212      10.932  55.228  76.775  1.00 39.66           N  
ANISOU 5291  N   LEU C 212     4400   5768   4901    140    147  -1329       N  
ATOM   5292  CA  LEU C 212      11.164  53.811  77.017  1.00 40.08           C  
ANISOU 5292  CA  LEU C 212     4479   5876   4872    118    152  -1186       C  
ATOM   5293  C   LEU C 212       9.863  53.016  77.046  1.00 40.67           C  
ANISOU 5293  C   LEU C 212     4547   5984   4923    102    212  -1127       C  
ATOM   5294  O   LEU C 212       9.868  51.820  76.734  1.00 41.00           O  
ANISOU 5294  O   LEU C 212     4618   5999   4962     84    213   -996       O  
ATOM   5295  CB  LEU C 212      11.952  53.626  78.314  1.00 40.39           C  
ANISOU 5295  CB  LEU C 212     4515   6059   4771    103    129  -1187       C  
ATOM   5296  CG  LEU C 212      13.413  54.073  78.203  1.00 40.39           C  
ANISOU 5296  CG  LEU C 212     4521   6028   4796    109     59  -1208       C  
ATOM   5297  CD1 LEU C 212      14.054  54.203  79.575  1.00 40.72           C  
ANISOU 5297  CD1 LEU C 212     4545   6230   4697     98     33  -1253       C  
ATOM   5298  CD2 LEU C 212      14.206  53.116  77.326  1.00 40.42           C  
ANISOU 5298  CD2 LEU C 212     4558   5949   4850    118     28  -1069       C  
ATOM   5299  N   VAL C 213       8.742  53.656  77.385  1.00 45.17           N  
ANISOU 5299  N   VAL C 213     5073   6605   5483    108    261  -1224       N  
ATOM   5300  CA  VAL C 213       7.445  52.993  77.258  1.00 45.94           C  
ANISOU 5300  CA  VAL C 213     5149   6728   5578     88    319  -1172       C  
ATOM   5301  C   VAL C 213       7.170  52.652  75.799  1.00 45.81           C  
ANISOU 5301  C   VAL C 213     5153   6558   5696     97    306  -1114       C  
ATOM   5302  O   VAL C 213       6.812  51.516  75.463  1.00 48.33           O  
ANISOU 5302  O   VAL C 213     5487   6853   6021     66    317  -1002       O  
ATOM   5303  CB  VAL C 213       6.329  53.871  77.853  1.00 45.86           C  
ANISOU 5303  CB  VAL C 213     5076   6812   5538    106    373  -1305       C  
ATOM   5304  CG1 VAL C 213       4.962  53.321  77.473  1.00 46.59           C  
ANISOU 5304  CG1 VAL C 213     5131   6913   5657     88    429  -1259       C  
ATOM   5305  CG2 VAL C 213       6.475  53.960  79.360  1.00 46.13           C  
ANISOU 5305  CG2 VAL C 213     5085   7035   5407     94    394  -1350       C  
ATOM   5306  N   THR C 214       7.339  53.636  74.909  1.00 37.39           N  
ANISOU 5306  N   THR C 214     4085   5382   4738    137    278  -1189       N  
ATOM   5307  CA  THR C 214       7.175  53.389  73.479  1.00 36.53           C  
ANISOU 5307  CA  THR C 214     3993   5144   4744    152    260  -1137       C  
ATOM   5308  C   THR C 214       8.179  52.356  72.982  1.00 36.09           C  
ANISOU 5308  C   THR C 214     3988   5034   4691    141    221  -1021       C  
ATOM   5309  O   THR C 214       7.857  51.531  72.117  1.00 35.19           O  
ANISOU 5309  O   THR C 214     3890   4857   4625    137    217   -951       O  
ATOM   5310  CB  THR C 214       7.323  54.699  72.701  1.00 33.97           C  
ANISOU 5310  CB  THR C 214     3659   4724   4525    197    234  -1222       C  
ATOM   5311  OG1 THR C 214       6.486  55.703  73.288  1.00 36.04           O  
ANISOU 5311  OG1 THR C 214     3874   5031   4787    219    263  -1344       O  
ATOM   5312  CG2 THR C 214       6.929  54.509  71.244  1.00 33.14           C  
ANISOU 5312  CG2 THR C 214     3559   4514   4520    217    222  -1173       C  
ATOM   5313  N   PHE C 215       9.399  52.381  73.525  1.00 36.12           N  
ANISOU 5313  N   PHE C 215     4013   5067   4643    140    187  -1009       N  
ATOM   5314  CA  PHE C 215      10.413  51.402  73.144  1.00 35.58           C  
ANISOU 5314  CA  PHE C 215     3987   4959   4573    142    148   -905       C  
ATOM   5315  C   PHE C 215       9.972  49.984  73.500  1.00 37.46           C  
ANISOU 5315  C   PHE C 215     4247   5224   4763    111    165   -800       C  
ATOM   5316  O   PHE C 215      10.104  49.057  72.692  1.00 37.02           O  
ANISOU 5316  O   PHE C 215     4221   5088   4758    118    144   -725       O  
ATOM   5317  CB  PHE C 215      11.738  51.755  73.824  1.00 37.13           C  
ANISOU 5317  CB  PHE C 215     4187   5205   4714    146    108   -919       C  
ATOM   5318  CG  PHE C 215      12.934  51.056  73.244  1.00 38.31           C  
ANISOU 5318  CG  PHE C 215     4365   5307   4883    166     62   -836       C  
ATOM   5319  CD1 PHE C 215      13.409  51.388  71.986  1.00 39.33           C  
ANISOU 5319  CD1 PHE C 215     4494   5344   5104    195     39   -838       C  
ATOM   5320  CD2 PHE C 215      13.600  50.085  73.970  1.00 41.92           C  
ANISOU 5320  CD2 PHE C 215     4844   5822   5261    163     40   -753       C  
ATOM   5321  CE1 PHE C 215      14.517  50.750  71.458  1.00 40.45           C  
ANISOU 5321  CE1 PHE C 215     4651   5460   5256    222      0   -771       C  
ATOM   5322  CE2 PHE C 215      14.708  49.444  73.447  1.00 43.68           C  
ANISOU 5322  CE2 PHE C 215     5087   6005   5505    195     -5   -686       C  
ATOM   5323  CZ  PHE C 215      15.168  49.778  72.191  1.00 41.60           C  
ANISOU 5323  CZ  PHE C 215     4817   5659   5331    225    -23   -701       C  
ATOM   5324  N   MET C 216       9.440  49.801  74.712  1.00 32.49           N  
ANISOU 5324  N   MET C 216     3599   4709   4036     76    201   -793       N  
ATOM   5325  CA  MET C 216       8.950  48.489  75.137  1.00 35.18           C  
ANISOU 5325  CA  MET C 216     3957   5077   4334     33    220   -676       C  
ATOM   5326  C   MET C 216       7.731  48.065  74.324  1.00 35.10           C  
ANISOU 5326  C   MET C 216     3933   4999   4405     11    249   -662       C  
ATOM   5327  O   MET C 216       7.523  46.868  74.067  1.00 40.70           O  
ANISOU 5327  O   MET C 216     4670   5653   5142    -19    241   -562       O  
ATOM   5328  CB  MET C 216       8.619  48.523  76.632  1.00 35.91           C  
ANISOU 5328  CB  MET C 216     4021   5333   4289     -3    259   -671       C  
ATOM   5329  CG  MET C 216       7.874  47.303  77.173  1.00 38.06           C  
ANISOU 5329  CG  MET C 216     4296   5652   4513    -63    293   -543       C  
ATOM   5330  SD  MET C 216       6.081  47.328  76.913  1.00 40.84           S  
ANISOU 5330  SD  MET C 216     4589   6022   4907   -108    365   -571       S  
ATOM   5331  CE  MET C 216       5.592  48.785  77.837  1.00 39.33           C  
ANISOU 5331  CE  MET C 216     4327   5996   4622    -85    417   -729       C  
ATOM   5332  N   ALA C 217       6.891  49.029  73.949  1.00 34.97           N  
ANISOU 5332  N   ALA C 217     3871   4985   4430     24    278   -765       N  
ATOM   5333  CA  ALA C 217       5.735  48.707  73.125  1.00 36.39           C  
ANISOU 5333  CA  ALA C 217     4028   5111   4689      7    299   -761       C  
ATOM   5334  C   ALA C 217       6.157  48.293  71.722  1.00 36.00           C  
ANISOU 5334  C   ALA C 217     4016   4922   4739     37    250   -736       C  
ATOM   5335  O   ALA C 217       5.490  47.466  71.091  1.00 37.21           O  
ANISOU 5335  O   ALA C 217     4170   5020   4947     12    248   -694       O  
ATOM   5336  CB  ALA C 217       4.779  49.898  73.072  1.00 33.40           C  
ANISOU 5336  CB  ALA C 217     3586   4774   4330     30    337   -879       C  
ATOM   5337  N   SER C 218       7.262  48.847  71.228  1.00 46.45           N  
ANISOU 5337  N   SER C 218     5365   6199   6086     88    209   -763       N  
ATOM   5338  CA  SER C 218       7.820  48.444  69.946  1.00 46.96           C  
ANISOU 5338  CA  SER C 218     5460   6158   6223    123    165   -738       C  
ATOM   5339  C   SER C 218       8.631  47.161  70.040  1.00 48.35           C  
ANISOU 5339  C   SER C 218     5688   6298   6385    119    130   -645       C  
ATOM   5340  O   SER C 218       9.119  46.678  69.012  1.00 49.47           O  
ANISOU 5340  O   SER C 218     5855   6360   6581    155     93   -629       O  
ATOM   5341  CB  SER C 218       8.688  49.566  69.376  1.00 45.34           C  
ANISOU 5341  CB  SER C 218     5252   5929   6047    173    140   -793       C  
ATOM   5342  OG  SER C 218       7.888  50.558  68.759  1.00 44.58           O  
ANISOU 5342  OG  SER C 218     5118   5815   6006    191    155   -863       O  
ATOM   5343  N   THR C 219       8.792  46.604  71.242  1.00 34.72           N  
ANISOU 5343  N   THR C 219     3975   4634   4584     83    140   -583       N  
ATOM   5344  CA  THR C 219       9.463  45.326  71.411  1.00 35.92           C  
ANISOU 5344  CA  THR C 219     4176   4743   4731     82    104   -481       C  
ATOM   5345  C   THR C 219       8.406  44.245  71.571  1.00 40.30           C  
ANISOU 5345  C   THR C 219     4737   5266   5309     20    123   -412       C  
ATOM   5346  O   THR C 219       7.689  44.232  72.590  1.00 44.32           O  
ANISOU 5346  O   THR C 219     5221   5864   5754    -38    167   -380       O  
ATOM   5347  CB  THR C 219      10.395  45.349  72.619  1.00 36.98           C  
ANISOU 5347  CB  THR C 219     4321   4963   4766     84     94   -438       C  
ATOM   5348  OG1 THR C 219      11.241  46.503  72.545  1.00 34.82           O  
ANISOU 5348  OG1 THR C 219     4028   4726   4476    126     80   -517       O  
ATOM   5349  CG2 THR C 219      11.267  44.104  72.639  1.00 36.70           C  
ANISOU 5349  CG2 THR C 219     4337   4868   4740    106     44   -334       C  
ATOM   5350  N   PRO C 220       8.246  43.348  70.594  1.00 45.90           N  
ANISOU 5350  N   PRO C 220     5474   5858   6107     26     90   -390       N  
ATOM   5351  CA  PRO C 220       7.190  42.332  70.681  1.00 47.34           C  
ANISOU 5351  CA  PRO C 220     5659   5996   6332    -47    102   -329       C  
ATOM   5352  C   PRO C 220       7.638  41.054  71.374  1.00 52.04           C  
ANISOU 5352  C   PRO C 220     6307   6546   6922    -74     74   -199       C  
ATOM   5353  O   PRO C 220       6.813  40.340  71.952  1.00 56.87           O  
ANISOU 5353  O   PRO C 220     6913   7159   7538   -155     96   -117       O  
ATOM   5354  CB  PRO C 220       6.839  42.077  69.210  1.00 46.21           C  
ANISOU 5354  CB  PRO C 220     5519   5746   6294    -21     71   -391       C  
ATOM   5355  CG  PRO C 220       8.113  42.348  68.475  1.00 44.91           C  
ANISOU 5355  CG  PRO C 220     5382   5545   6136     71     27   -430       C  
ATOM   5356  CD  PRO C 220       8.868  43.397  69.258  1.00 43.80           C  
ANISOU 5356  CD  PRO C 220     5225   5507   5909     96     47   -444       C  
ATOM   5357  N   VAL C 221       8.934  40.750  71.322  1.00 51.35           N  
ANISOU 5357  N   VAL C 221     6265   6419   6828     -6     23   -172       N  
ATOM   5358  CA  VAL C 221       9.493  39.539  71.913  1.00 54.76           C  
ANISOU 5358  CA  VAL C 221     6750   6792   7264    -11    -16    -45       C  
ATOM   5359  C   VAL C 221      10.881  39.863  72.452  1.00 55.13           C  
ANISOU 5359  C   VAL C 221     6811   6903   7233     58    -44    -28       C  
ATOM   5360  O   VAL C 221      11.472  40.895  72.128  1.00 53.28           O  
ANISOU 5360  O   VAL C 221     6549   6726   6968    110    -41   -120       O  
ATOM   5361  CB  VAL C 221       9.581  38.375  70.897  1.00 56.77           C  
ANISOU 5361  CB  VAL C 221     7054   6870   7646     14    -75    -36       C  
ATOM   5362  CG1 VAL C 221       8.210  37.767  70.643  1.00 58.19           C  
ANISOU 5362  CG1 VAL C 221     7224   6982   7905    -78    -58    -20       C  
ATOM   5363  CG2 VAL C 221      10.208  38.856  69.596  1.00 54.72           C  
ANISOU 5363  CG2 VAL C 221     6791   6573   7428    107   -104   -157       C  
ATOM   5364  N   GLY C 222      11.408  38.971  73.287  1.00 40.75           N  
ANISOU 5364  N   GLY C 222     5029   5072   5384     57    -74     99       N  
ATOM   5365  CA  GLY C 222      12.796  39.030  73.698  1.00 40.83           C  
ANISOU 5365  CA  GLY C 222     5052   5125   5335    132   -117    126       C  
ATOM   5366  C   GLY C 222      13.039  39.316  75.164  1.00 43.19           C  
ANISOU 5366  C   GLY C 222     5335   5580   5497    102   -100    201       C  
ATOM   5367  O   GLY C 222      14.197  39.246  75.597  1.00 43.02           O  
ANISOU 5367  O   GLY C 222     5323   5600   5423    162   -144    237       O  
ATOM   5368  N   TYR C 223      12.009  39.641  75.944  1.00 47.44           N  
ANISOU 5368  N   TYR C 223     5842   6218   5964     18    -38    220       N  
ATOM   5369  CA  TYR C 223      12.180  39.897  77.367  1.00 47.85           C  
ANISOU 5369  CA  TYR C 223     5874   6441   5867    -10    -18    285       C  
ATOM   5370  C   TYR C 223      11.213  39.039  78.172  1.00 51.69           C  
ANISOU 5370  C   TYR C 223     6367   6950   6322   -101     16    431       C  
ATOM   5371  O   TYR C 223      10.133  38.677  77.699  1.00 53.72           O  
ANISOU 5371  O   TYR C 223     6620   7130   6662   -164     48    437       O  
ATOM   5372  CB  TYR C 223      11.987  41.386  77.713  1.00 45.48           C  
ANISOU 5372  CB  TYR C 223     5512   6295   5474    -15     31    147       C  
ATOM   5373  CG  TYR C 223      10.702  42.013  77.210  1.00 45.31           C  
ANISOU 5373  CG  TYR C 223     5450   6269   5497    -62     94     49       C  
ATOM   5374  CD1 TYR C 223       9.564  42.055  78.007  1.00 45.48           C  
ANISOU 5374  CD1 TYR C 223     5433   6399   5448   -139    161     80       C  
ATOM   5375  CD2 TYR C 223      10.633  42.584  75.946  1.00 43.17           C  
ANISOU 5375  CD2 TYR C 223     5171   5901   5331    -25     89    -71       C  
ATOM   5376  CE1 TYR C 223       8.389  42.637  77.551  1.00 44.77           C  
ANISOU 5376  CE1 TYR C 223     5296   6314   5400   -173    216    -14       C  
ATOM   5377  CE2 TYR C 223       9.465  43.165  75.483  1.00 41.56           C  
ANISOU 5377  CE2 TYR C 223     4927   5697   5167    -60    140   -155       C  
ATOM   5378  CZ  TYR C 223       8.344  43.192  76.286  1.00 43.66           C  
ANISOU 5378  CZ  TYR C 223     5153   6066   5371   -131    202   -131       C  
ATOM   5379  OH  TYR C 223       7.183  43.779  75.810  1.00 44.36           O  
ANISOU 5379  OH  TYR C 223     5191   6160   5503   -155    250   -219       O  
ATOM   5380  N   ASN C 224      11.619  38.716  79.401  1.00 65.63           N  
ANISOU 5380  N   ASN C 224     8138   8833   7965   -113      8    554       N  
ATOM   5381  CA  ASN C 224      10.850  37.833  80.267  1.00 68.54           C  
ANISOU 5381  CA  ASN C 224     8513   9238   8291   -202     37    728       C  
ATOM   5382  C   ASN C 224       9.974  38.572  81.268  1.00 67.40           C  
ANISOU 5382  C   ASN C 224     8301   9315   7995   -272    122    709       C  
ATOM   5383  O   ASN C 224       9.032  37.973  81.799  1.00 67.69           O  
ANISOU 5383  O   ASN C 224     8323   9389   8007   -364    168    831       O  
ATOM   5384  CB  ASN C 224      11.790  36.893  81.031  1.00 71.48           C  
ANISOU 5384  CB  ASN C 224     8935   9608   8615   -170    -28    906       C  
ATOM   5385  CG  ASN C 224      12.504  35.919  80.118  1.00 74.33           C  
ANISOU 5385  CG  ASN C 224     9364   9738   9138   -104   -111    947       C  
ATOM   5386  OD1 ASN C 224      13.735  35.874  80.078  1.00 75.91           O  
ANISOU 5386  OD1 ASN C 224     9585   9927   9330     -7   -176    943       O  
ATOM   5387  ND2 ASN C 224      11.734  35.132  79.375  1.00 74.20           N  
ANISOU 5387  ND2 ASN C 224     9378   9542   9272   -152   -111    978       N  
ATOM   5388  N   GLN C 225      10.256  39.842  81.540  1.00 55.01           N  
ANISOU 5388  N   GLN C 225     6684   7891   6326   -232    143    557       N  
ATOM   5389  CA  GLN C 225       9.478  40.589  82.514  1.00 53.52           C  
ANISOU 5389  CA  GLN C 225     6427   7921   5986   -281    221    515       C  
ATOM   5390  C   GLN C 225       8.112  40.960  81.940  1.00 52.59           C  
ANISOU 5390  C   GLN C 225     6261   7780   5940   -336    293    427       C  
ATOM   5391  O   GLN C 225       7.857  40.852  80.738  1.00 50.75           O  
ANISOU 5391  O   GLN C 225     6047   7371   5866   -327    277    371       O  
ATOM   5392  CB  GLN C 225      10.228  41.852  82.942  1.00 52.44           C  
ANISOU 5392  CB  GLN C 225     6258   7928   5740   -217    211    359       C  
ATOM   5393  CG  GLN C 225      11.660  41.612  83.399  1.00 53.82           C  
ANISOU 5393  CG  GLN C 225     6468   8132   5851   -154    132    418       C  
ATOM   5394  CD  GLN C 225      12.679  41.867  82.301  1.00 52.43           C  
ANISOU 5394  CD  GLN C 225     6322   7796   5804    -75     65    327       C  
ATOM   5395  OE1 GLN C 225      12.389  41.708  81.114  1.00 50.45           O  
ANISOU 5395  OE1 GLN C 225     6091   7369   5708    -68     63    288       O  
ATOM   5396  NE2 GLN C 225      13.884  42.266  82.695  1.00 50.85           N  
ANISOU 5396  NE2 GLN C 225     6116   7672   5531    -16      9    293       N  
ATOM   5397  N   ASN C 226       7.223  41.400  82.827  1.00 54.95           N  
ANISOU 5397  N   ASN C 226     6492   8275   6111   -389    372    414       N  
ATOM   5398  CA  ASN C 226       5.989  42.029  82.390  1.00 54.98           C  
ANISOU 5398  CA  ASN C 226     6431   8298   6160   -421    441    295       C  
ATOM   5399  C   ASN C 226       6.314  43.358  81.701  1.00 52.29           C  
ANISOU 5399  C   ASN C 226     6075   7926   5866   -338    426     74       C  
ATOM   5400  O   ASN C 226       7.427  43.881  81.804  1.00 50.60           O  
ANISOU 5400  O   ASN C 226     5888   7721   5618   -271    376     10       O  
ATOM   5401  CB  ASN C 226       5.044  42.229  83.576  1.00 55.84           C  
ANISOU 5401  CB  ASN C 226     6461   8651   6107   -484    531    324       C  
ATOM   5402  CG  ASN C 226       4.629  40.912  84.223  1.00 57.92           C  
ANISOU 5402  CG  ASN C 226     6732   8946   6331   -582    551    566       C  
ATOM   5403  OD1 ASN C 226       4.389  40.847  85.429  1.00 58.96           O  
ANISOU 5403  OD1 ASN C 226     6820   9296   6287   -622    601    649       O  
ATOM   5404  ND2 ASN C 226       4.542  39.857  83.418  1.00 58.23           N  
ANISOU 5404  ND2 ASN C 226     6824   8766   6535   -622    511    679       N  
ATOM   5405  N   GLU C 227       5.327  43.903  80.982  1.00 54.12           N  
ANISOU 5405  N   GLU C 227     6262   8119   6183   -347    468    -37       N  
ATOM   5406  CA  GLU C 227       5.572  45.074  80.139  1.00 51.84           C  
ANISOU 5406  CA  GLU C 227     5967   7760   5972   -272    447   -223       C  
ATOM   5407  C   GLU C 227       6.129  46.241  80.955  1.00 49.87           C  
ANISOU 5407  C   GLU C 227     5690   7657   5600   -220    450   -351       C  
ATOM   5408  O   GLU C 227       7.239  46.734  80.699  1.00 49.02           O  
ANISOU 5408  O   GLU C 227     5618   7495   5514   -162    391   -413       O  
ATOM   5409  CB  GLU C 227       4.281  45.482  79.418  1.00 50.03           C  
ANISOU 5409  CB  GLU C 227     5680   7499   5831   -289    496   -310       C  
ATOM   5410  CG  GLU C 227       3.667  44.426  78.477  1.00 53.32           C  
ANISOU 5410  CG  GLU C 227     6114   7763   6382   -342    486   -216       C  
ATOM   5411  CD  GLU C 227       4.617  43.946  77.381  1.00 54.97           C  
ANISOU 5411  CD  GLU C 227     6403   7769   6713   -298    403   -194       C  
ATOM   5412  OE1 GLU C 227       5.399  43.013  77.654  1.00 56.77           O  
ANISOU 5412  OE1 GLU C 227     6691   7948   6930   -307    361    -70       O  
ATOM   5413  OE2 GLU C 227       4.582  44.491  76.249  1.00 55.45           O  
ANISOU 5413  OE2 GLU C 227     6465   7727   6878   -251    381   -299       O  
ATOM   5414  N   TYR C 228       5.371  46.695  81.954  1.00 46.69           N  
ANISOU 5414  N   TYR C 228     5219   7451   5069   -242    519   -397       N  
ATOM   5415  CA  TYR C 228       5.817  47.827  82.759  1.00 45.43           C  
ANISOU 5415  CA  TYR C 228     5030   7436   4794   -192    519   -542       C  
ATOM   5416  C   TYR C 228       7.029  47.465  83.613  1.00 46.53           C  
ANISOU 5416  C   TYR C 228     5209   7656   4813   -183    469   -464       C  
ATOM   5417  O   TYR C 228       7.889  48.319  83.868  1.00 44.38           O  
ANISOU 5417  O   TYR C 228     4940   7419   4503   -132    426   -582       O  
ATOM   5418  CB  TYR C 228       4.654  48.332  83.613  1.00 44.99           C  
ANISOU 5418  CB  TYR C 228     4885   7584   4623   -210    608   -619       C  
ATOM   5419  CG  TYR C 228       3.481  48.818  82.780  1.00 44.33           C  
ANISOU 5419  CG  TYR C 228     4751   7433   4661   -204    652   -714       C  
ATOM   5420  CD1 TYR C 228       3.684  49.622  81.663  1.00 42.89           C  
ANISOU 5420  CD1 TYR C 228     4589   7076   4631   -145    610   -838       C  
ATOM   5421  CD2 TYR C 228       2.175  48.466  83.101  1.00 44.84           C  
ANISOU 5421  CD2 TYR C 228     4741   7612   4684   -258    734   -672       C  
ATOM   5422  CE1 TYR C 228       2.622  50.069  80.896  1.00 42.63           C  
ANISOU 5422  CE1 TYR C 228     4508   6986   4704   -131    643   -918       C  
ATOM   5423  CE2 TYR C 228       1.105  48.910  82.337  1.00 44.51           C  
ANISOU 5423  CE2 TYR C 228     4644   7516   4751   -247    769   -761       C  
ATOM   5424  CZ  TYR C 228       1.336  49.711  81.237  1.00 43.90           C  
ANISOU 5424  CZ  TYR C 228     4593   7264   4824   -179    720   -884       C  
ATOM   5425  OH  TYR C 228       0.278  50.154  80.476  1.00 43.52           O  
ANISOU 5425  OH  TYR C 228     4487   7168   4880   -161    748   -965       O  
ATOM   5426  N   GLU C 229       7.129  46.204  84.039  1.00 52.50           N  
ANISOU 5426  N   GLU C 229     5995   8436   5518   -234    465   -261       N  
ATOM   5427  CA  GLU C 229       8.344  45.741  84.702  1.00 53.81           C  
ANISOU 5427  CA  GLU C 229     6204   8653   5589   -217    403   -164       C  
ATOM   5428  C   GLU C 229       9.546  45.841  83.770  1.00 53.30           C  
ANISOU 5428  C   GLU C 229     6197   8403   5651   -158    316   -197       C  
ATOM   5429  O   GLU C 229      10.653  46.190  84.199  1.00 52.83           O  
ANISOU 5429  O   GLU C 229     6148   8400   5525   -116    261   -233       O  
ATOM   5430  CB  GLU C 229       8.156  44.303  85.184  1.00 57.62           C  
ANISOU 5430  CB  GLU C 229     6713   9156   6025   -280    411     79       C  
ATOM   5431  CG  GLU C 229       8.999  43.927  86.384  1.00 62.62           C  
ANISOU 5431  CG  GLU C 229     7357   9954   6481   -273    378    188       C  
ATOM   5432  CD  GLU C 229       8.472  42.693  87.091  1.00 67.44           C  
ANISOU 5432  CD  GLU C 229     7973  10638   7015   -350    411    428       C  
ATOM   5433  OE1 GLU C 229       8.102  41.721  86.397  1.00 68.98           O  
ANISOU 5433  OE1 GLU C 229     8206  10652   7352   -395    406    559       O  
ATOM   5434  OE2 GLU C 229       8.426  42.695  88.339  1.00 68.41           O  
ANISOU 5434  OE2 GLU C 229     8058  11001   6934   -369    440    486       O  
ATOM   5435  N   PHE C 230       9.345  45.548  82.483  1.00 43.36           N  
ANISOU 5435  N   PHE C 230     4969   6935   4571   -154    303   -190       N  
ATOM   5436  CA  PHE C 230      10.435  45.682  81.524  1.00 41.67           C  
ANISOU 5436  CA  PHE C 230     4799   6562   4473    -96    230   -228       C  
ATOM   5437  C   PHE C 230      10.831  47.141  81.344  1.00 38.57           C  
ANISOU 5437  C   PHE C 230     4376   6190   4090    -50    218   -423       C  
ATOM   5438  O   PHE C 230      12.020  47.452  81.196  1.00 36.95           O  
ANISOU 5438  O   PHE C 230     4186   5956   3897     -8    156   -457       O  
ATOM   5439  CB  PHE C 230      10.046  45.060  80.184  1.00 40.90           C  
ANISOU 5439  CB  PHE C 230     4734   6257   4547   -101    223   -188       C  
ATOM   5440  CG  PHE C 230      11.144  45.100  79.160  1.00 40.41           C  
ANISOU 5440  CG  PHE C 230     4712   6049   4594    -38    154   -216       C  
ATOM   5441  CD1 PHE C 230      12.356  44.473  79.402  1.00 40.43           C  
ANISOU 5441  CD1 PHE C 230     4751   6041   4570     -3     90   -127       C  
ATOM   5442  CD2 PHE C 230      10.967  45.763  77.959  1.00 39.61           C  
ANISOU 5442  CD2 PHE C 230     4602   5832   4614    -11    154   -326       C  
ATOM   5443  CE1 PHE C 230      13.370  44.509  78.465  1.00 40.98           C  
ANISOU 5443  CE1 PHE C 230     4844   5996   4732     57     32   -156       C  
ATOM   5444  CE2 PHE C 230      11.977  45.801  77.014  1.00 39.90           C  
ANISOU 5444  CE2 PHE C 230     4667   5757   4738     44     97   -346       C  
ATOM   5445  CZ  PHE C 230      13.181  45.172  77.268  1.00 40.90           C  
ANISOU 5445  CZ  PHE C 230     4823   5881   4835     78     39   -264       C  
ATOM   5446  N   VAL C 231       9.852  48.051  81.349  1.00 43.24           N  
ANISOU 5446  N   VAL C 231     4918   6826   4685    -58    274   -553       N  
ATOM   5447  CA  VAL C 231      10.195  49.473  81.341  1.00 42.83           C  
ANISOU 5447  CA  VAL C 231     4838   6794   4643    -18    260   -740       C  
ATOM   5448  C   VAL C 231      11.038  49.819  82.562  1.00 42.77           C  
ANISOU 5448  C   VAL C 231     4816   6953   4482     -8    230   -777       C  
ATOM   5449  O   VAL C 231      12.033  50.548  82.464  1.00 43.76           O  
ANISOU 5449  O   VAL C 231     4943   7054   4630     23    173   -867       O  
ATOM   5450  CB  VAL C 231       8.930  50.346  81.266  1.00 41.87           C  
ANISOU 5450  CB  VAL C 231     4663   6701   4545    -18    325   -872       C  
ATOM   5451  CG1 VAL C 231       9.303  51.818  81.407  1.00 38.84           C  
ANISOU 5451  CG1 VAL C 231     4252   6333   4171     24    303  -1066       C  
ATOM   5452  CG2 VAL C 231       8.207  50.109  79.956  1.00 39.94           C  
ANISOU 5452  CG2 VAL C 231     4427   6289   4458    -21    340   -847       C  
ATOM   5453  N   GLY C 232      10.656  49.298  83.729  1.00 46.64           N  
ANISOU 5453  N   GLY C 232     5287   7625   4811    -38    265   -705       N  
ATOM   5454  CA  GLY C 232      11.470  49.501  84.918  1.00 48.19           C  
ANISOU 5454  CA  GLY C 232     5468   8000   4841    -27    231   -726       C  
ATOM   5455  C   GLY C 232      12.884  48.976  84.752  1.00 49.38           C  
ANISOU 5455  C   GLY C 232     5662   8090   5009     -5    145   -633       C  
ATOM   5456  O   GLY C 232      13.841  49.560  85.268  1.00 48.35           O  
ANISOU 5456  O   GLY C 232     5517   8042   4812     19     90   -715       O  
ATOM   5457  N   ALA C 233      13.033  47.863  84.032  1.00 45.84           N  
ANISOU 5457  N   ALA C 233     5263   7501   4653    -10    128   -471       N  
ATOM   5458  CA  ALA C 233      14.365  47.330  83.757  1.00 45.59           C  
ANISOU 5458  CA  ALA C 233     5268   7400   4655     26     46   -388       C  
ATOM   5459  C   ALA C 233      15.160  48.266  82.853  1.00 42.50           C  
ANISOU 5459  C   ALA C 233     4870   6893   4385     62      1   -523       C  
ATOM   5460  O   ALA C 233      16.354  48.495  83.081  1.00 43.42           O  
ANISOU 5460  O   ALA C 233     4977   7049   4471     89    -65   -544       O  
ATOM   5461  CB  ALA C 233      14.263  45.941  83.129  1.00 46.23           C  
ANISOU 5461  CB  ALA C 233     5403   7340   4824     20     39   -202       C  
ATOM   5462  N   LEU C 234      14.515  48.816  81.821  1.00 52.90           N  
ANISOU 5462  N   LEU C 234     6185   8076   5839     60     34   -608       N  
ATOM   5463  CA  LEU C 234      15.198  49.737  80.917  1.00 52.80           C  
ANISOU 5463  CA  LEU C 234     6164   7953   5944     87     -3   -720       C  
ATOM   5464  C   LEU C 234      15.622  51.022  81.614  1.00 52.58           C  
ANISOU 5464  C   LEU C 234     6092   8027   5858     86    -25   -883       C  
ATOM   5465  O   LEU C 234      16.545  51.696  81.143  1.00 51.99           O  
ANISOU 5465  O   LEU C 234     6006   7892   5856    100    -75   -951       O  
ATOM   5466  CB  LEU C 234      14.301  50.064  79.723  1.00 51.37           C  
ANISOU 5466  CB  LEU C 234     5988   7622   5908     86     38   -765       C  
ATOM   5467  CG  LEU C 234      13.918  48.866  78.854  1.00 51.38           C  
ANISOU 5467  CG  LEU C 234     6031   7502   5990     86     50   -631       C  
ATOM   5468  CD1 LEU C 234      13.054  49.300  77.682  1.00 50.79           C  
ANISOU 5468  CD1 LEU C 234     5952   7300   6046     88     83   -692       C  
ATOM   5469  CD2 LEU C 234      15.164  48.145  78.372  1.00 51.30           C  
ANISOU 5469  CD2 LEU C 234     6050   7425   6017    123    -14   -542       C  
ATOM   5470  N   GLN C 235      14.970  51.376  82.720  1.00 47.88           N  
ANISOU 5470  N   GLN C 235     5469   7588   5134     69     11   -951       N  
ATOM   5471  CA  GLN C 235      15.325  52.547  83.507  1.00 47.95           C  
ANISOU 5471  CA  GLN C 235     5436   7707   5075     71    -14  -1122       C  
ATOM   5472  C   GLN C 235      16.362  52.233  84.579  1.00 51.52           C  
ANISOU 5472  C   GLN C 235     5876   8325   5374     74    -72  -1087       C  
ATOM   5473  O   GLN C 235      16.517  53.013  85.526  1.00 54.99           O  
ANISOU 5473  O   GLN C 235     6278   8908   5708     72    -90  -1223       O  
ATOM   5474  CB  GLN C 235      14.068  53.153  84.134  1.00 45.47           C  
ANISOU 5474  CB  GLN C 235     5090   7492   4696     64     54  -1240       C  
ATOM   5475  CG  GLN C 235      12.996  53.505  83.114  1.00 46.88           C  
ANISOU 5475  CG  GLN C 235     5271   7520   5022     69    108  -1280       C  
ATOM   5476  CD  GLN C 235      11.878  54.348  83.694  1.00 48.03           C  
ANISOU 5476  CD  GLN C 235     5371   7758   5121     77    166  -1434       C  
ATOM   5477  OE1 GLN C 235      11.447  55.327  83.085  1.00 48.87           O  
ANISOU 5477  OE1 GLN C 235     5464   7753   5350     98    173  -1562       O  
ATOM   5478  NE2 GLN C 235      11.398  53.970  84.873  1.00 47.06           N  
ANISOU 5478  NE2 GLN C 235     5219   7843   4817     66    207  -1419       N  
ATOM   5479  N   ASP C 236      17.061  51.102  84.451  1.00 56.71           N  
ANISOU 5479  N   ASP C 236     6563   8967   6018     84   -108   -912       N  
ATOM   5480  CA  ASP C 236      18.152  50.721  85.351  1.00 58.56           C  
ANISOU 5480  CA  ASP C 236     6784   9347   6119     97   -175   -856       C  
ATOM   5481  C   ASP C 236      17.658  50.516  86.783  1.00 58.29           C  
ANISOU 5481  C   ASP C 236     6730   9545   5871     84   -149   -842       C  
ATOM   5482  O   ASP C 236      18.331  50.878  87.750  1.00 57.79           O  
ANISOU 5482  O   ASP C 236     6632   9654   5672     89   -198   -906       O  
ATOM   5483  CB  ASP C 236      19.288  51.747  85.307  1.00 60.55           C  
ANISOU 5483  CB  ASP C 236     6998   9600   6407    102   -248   -999       C  
ATOM   5484  CG  ASP C 236      20.647  51.125  85.553  1.00 64.67           C  
ANISOU 5484  CG  ASP C 236     7511  10181   6880    127   -330   -898       C  
ATOM   5485  OD1 ASP C 236      20.767  49.886  85.449  1.00 66.08           O  
ANISOU 5485  OD1 ASP C 236     7724  10340   7042    151   -334   -713       O  
ATOM   5486  OD2 ASP C 236      21.595  51.879  85.863  1.00 66.65           O  
ANISOU 5486  OD2 ASP C 236     7717  10496   7113    123   -396  -1008       O  
ATOM   5487  N   GLY C 237      16.478  49.921  86.918  1.00 52.70           N  
ANISOU 5487  N   GLY C 237     6037   8857   5128     63    -72   -756       N  
ATOM   5488  CA  GLY C 237      15.919  49.610  88.215  1.00 54.00           C  
ANISOU 5488  CA  GLY C 237     6180   9253   5086     45    -34   -712       C  
ATOM   5489  C   GLY C 237      14.940  50.620  88.768  1.00 55.38           C  
ANISOU 5489  C   GLY C 237     6305   9549   5186     34     30   -897       C  
ATOM   5490  O   GLY C 237      14.521  50.477  89.922  1.00 58.73           O  
ANISOU 5490  O   GLY C 237     6699  10203   5415     23     63   -883       O  
ATOM   5491  N   VAL C 238      14.561  51.629  87.992  1.00 54.41           N  
ANISOU 5491  N   VAL C 238     6174   9288   5212     41     47  -1066       N  
ATOM   5492  CA  VAL C 238      13.616  52.648  88.434  1.00 53.32           C  
ANISOU 5492  CA  VAL C 238     5988   9242   5029     46    103  -1260       C  
ATOM   5493  C   VAL C 238      12.217  52.204  88.015  1.00 51.24           C  
ANISOU 5493  C   VAL C 238     5724   8932   4814     26    199  -1189       C  
ATOM   5494  O   VAL C 238      11.973  52.035  86.811  1.00 51.02           O  
ANISOU 5494  O   VAL C 238     5727   8689   4970     23    206  -1143       O  
ATOM   5495  CB  VAL C 238      13.949  54.021  87.840  1.00 52.84           C  
ANISOU 5495  CB  VAL C 238     5916   9046   5116     67     63  -1479       C  
ATOM   5496  CG1 VAL C 238      13.000  55.080  88.386  1.00 53.39           C  
ANISOU 5496  CG1 VAL C 238     5936   9212   5139     86    113  -1693       C  
ATOM   5497  CG2 VAL C 238      15.395  54.388  88.113  1.00 53.21           C  
ANISOU 5497  CG2 VAL C 238     5959   9115   5142     73    -37  -1533       C  
ATOM   5498  N   PRO C 239      11.289  52.012  88.947  1.00 48.86           N  
ANISOU 5498  N   PRO C 239     5380   8835   4351     11    271  -1179       N  
ATOM   5499  CA  PRO C 239       9.920  51.666  88.556  1.00 50.13           C  
ANISOU 5499  CA  PRO C 239     5524   8962   4561    -13    363  -1125       C  
ATOM   5500  C   PRO C 239       9.258  52.817  87.820  1.00 48.51           C  
ANISOU 5500  C   PRO C 239     5294   8632   4505     20    387  -1326       C  
ATOM   5501  O   PRO C 239       9.595  53.988  88.014  1.00 47.33           O  
ANISOU 5501  O   PRO C 239     5125   8494   4366     60    353  -1534       O  
ATOM   5502  CB  PRO C 239       9.221  51.393  89.895  1.00 50.52           C  
ANISOU 5502  CB  PRO C 239     5515   9305   4374    -33    432  -1096       C  
ATOM   5503  CG  PRO C 239      10.324  51.260  90.904  1.00 50.42           C  
ANISOU 5503  CG  PRO C 239     5508   9462   4185    -23    367  -1071       C  
ATOM   5504  CD  PRO C 239      11.426  52.131  90.405  1.00 48.84           C  
ANISOU 5504  CD  PRO C 239     5333   9121   4102     16    274  -1223       C  
ATOM   5505  N   MET C 240       8.310  52.472  86.961  1.00 55.87           N  
ANISOU 5505  N   MET C 240     6228   9440   5561      2    439  -1262       N  
ATOM   5506  CA  MET C 240       7.486  53.469  86.300  1.00 56.55           C  
ANISOU 5506  CA  MET C 240     6282   9427   5778     37    470  -1429       C  
ATOM   5507  C   MET C 240       6.127  53.550  86.983  1.00 56.21           C  
ANISOU 5507  C   MET C 240     6161   9571   5625     35    568  -1478       C  
ATOM   5508  O   MET C 240       5.670  52.604  87.630  1.00 57.12           O  
ANISOU 5508  O   MET C 240     6254   9842   5606    -14    622  -1329       O  
ATOM   5509  CB  MET C 240       7.320  53.150  84.811  1.00 56.89           C  
ANISOU 5509  CB  MET C 240     6367   9216   6034     29    458  -1347       C  
ATOM   5510  CG  MET C 240       6.397  51.987  84.509  1.00 59.82           C  
ANISOU 5510  CG  MET C 240     6733   9579   6415    -23    517  -1170       C  
ATOM   5511  SD  MET C 240       5.869  52.007  82.786  1.00 58.88           S  
ANISOU 5511  SD  MET C 240     6637   9196   6539    -14    510  -1159       S  
ATOM   5512  CE  MET C 240       5.041  53.594  82.712  1.00 57.14           C  
ANISOU 5512  CE  MET C 240     6351   8988   6372     51    541  -1406       C  
ATOM   5513  N   ASP C 241       5.492  54.709  86.849  1.00 57.28           N  
ANISOU 5513  N   ASP C 241     6250   9692   5820     89    590  -1686       N  
ATOM   5514  CA  ASP C 241       4.187  54.946  87.447  1.00 57.94           C  
ANISOU 5514  CA  ASP C 241     6246   9957   5811    104    684  -1767       C  
ATOM   5515  C   ASP C 241       3.093  54.532  86.473  1.00 55.71           C  
ANISOU 5515  C   ASP C 241     5943   9558   5665     83    736  -1683       C  
ATOM   5516  O   ASP C 241       3.117  54.921  85.301  1.00 53.30           O  
ANISOU 5516  O   ASP C 241     5670   9024   5556    107    698  -1716       O  
ATOM   5517  CB  ASP C 241       4.025  56.417  87.828  1.00 60.62           C  
ANISOU 5517  CB  ASP C 241     6540  10341   6150    186    677  -2050       C  
ATOM   5518  CG  ASP C 241       4.924  56.824  88.977  1.00 63.57           C  
ANISOU 5518  CG  ASP C 241     6914  10884   6358    204    634  -2158       C  
ATOM   5519  OD1 ASP C 241       5.504  55.927  89.626  1.00 65.56           O  
ANISOU 5519  OD1 ASP C 241     7185  11267   6458    154    626  -2004       O  
ATOM   5520  OD2 ASP C 241       5.052  58.041  89.229  1.00 63.21           O  
ANISOU 5520  OD2 ASP C 241     6848  10834   6336    268    603  -2399       O  
ATOM   5521  N   ILE C 242       2.140  53.740  86.960  1.00 45.42           N  
ANISOU 5521  N   ILE C 242     4582   8423   4254     33    821  -1570       N  
ATOM   5522  CA  ILE C 242       0.985  53.328  86.177  1.00 45.33           C  
ANISOU 5522  CA  ILE C 242     4532   8340   4352      5    875  -1499       C  
ATOM   5523  C   ILE C 242      -0.272  53.644  86.976  1.00 46.77           C  
ANISOU 5523  C   ILE C 242     4593   8765   4410     20    977  -1591       C  
ATOM   5524  O   ILE C 242      -0.222  53.919  88.175  1.00 47.78           O  
ANISOU 5524  O   ILE C 242     4677   9132   4346     38   1010  -1666       O  
ATOM   5525  CB  ILE C 242       1.032  51.835  85.797  1.00 45.23           C  
ANISOU 5525  CB  ILE C 242     4562   8258   4365    -93    875  -1233       C  
ATOM   5526  CG1 ILE C 242       1.053  50.970  87.056  1.00 46.92           C  
ANISOU 5526  CG1 ILE C 242     4753   8710   4363   -158    921  -1087       C  
ATOM   5527  CG2 ILE C 242       2.240  51.543  84.921  1.00 44.61           C  
ANISOU 5527  CG2 ILE C 242     4593   7939   4416    -92    777  -1159       C  
ATOM   5528  CD1 ILE C 242       0.793  49.518  86.787  1.00 48.04           C  
ANISOU 5528  CD1 ILE C 242     4919   8799   4535   -259    937   -828       C  
ATOM   5529  N   VAL C 243      -1.412  53.604  86.288  1.00 52.61           N  
ANISOU 5529  N   VAL C 243     5275   9457   5258     15   1025  -1589       N  
ATOM   5530  CA  VAL C 243      -2.688  53.969  86.890  1.00 53.56           C  
ANISOU 5530  CA  VAL C 243     5267   9798   5286     40   1124  -1688       C  
ATOM   5531  C   VAL C 243      -3.795  53.196  86.188  1.00 52.93           C  
ANISOU 5531  C   VAL C 243     5133   9680   5298    -27   1176  -1553       C  
ATOM   5532  O   VAL C 243      -3.720  52.914  84.989  1.00 52.76           O  
ANISOU 5532  O   VAL C 243     5167   9419   5461    -45   1124  -1485       O  
ATOM   5533  CB  VAL C 243      -2.925  55.499  86.819  1.00 52.00           C  
ANISOU 5533  CB  VAL C 243     5030   9579   5150    169   1111  -1973       C  
ATOM   5534  CG1 VAL C 243      -3.022  55.965  85.372  1.00 48.41           C  
ANISOU 5534  CG1 VAL C 243     4615   8833   4946    210   1053  -2012       C  
ATOM   5535  CG2 VAL C 243      -4.164  55.896  87.611  1.00 50.71           C  
ANISOU 5535  CG2 VAL C 243     4724   9681   4862    210   1215  -2096       C  
ATOM   5536  N   LYS C 244      -4.827  52.846  86.951  1.00 51.21           N  
ANISOU 5536  N   LYS C 244     4800   9713   4943    -68   1278  -1516       N  
ATOM   5537  CA  LYS C 244      -5.940  52.087  86.402  1.00 54.74           C  
ANISOU 5537  CA  LYS C 244     5177  10154   5466   -146   1332  -1387       C  
ATOM   5538  C   LYS C 244      -6.730  52.924  85.405  1.00 53.62           C  
ANISOU 5538  C   LYS C 244     4984   9888   5501    -64   1324  -1544       C  
ATOM   5539  O   LYS C 244      -6.992  54.109  85.630  1.00 53.14           O  
ANISOU 5539  O   LYS C 244     4871   9889   5430     52   1336  -1766       O  
ATOM   5540  CB  LYS C 244      -6.863  51.608  87.523  1.00 55.88           C  
ANISOU 5540  CB  LYS C 244     5194  10624   5413   -209   1451  -1316       C  
ATOM   5541  CG  LYS C 244      -7.928  50.621  87.066  1.00 55.78           C  
ANISOU 5541  CG  LYS C 244     5108  10616   5468   -324   1505  -1142       C  
ATOM   5542  CD  LYS C 244      -8.859  50.243  88.208  1.00 57.20           C  
ANISOU 5542  CD  LYS C 244     5146  11141   5446   -388   1630  -1075       C  
ATOM   5543  CE  LYS C 244      -9.872  51.343  88.487  1.00 57.14           C  
ANISOU 5543  CE  LYS C 244     4992  11325   5393   -280   1705  -1311       C  
ATOM   5544  NZ  LYS C 244     -10.848  51.500  87.370  1.00 57.32           N  
ANISOU 5544  NZ  LYS C 244     4950  11217   5614   -268   1704  -1357       N  
ATOM   5545  N   SER C 245      -7.103  52.292  84.292  1.00 64.21           N  
ANISOU 5545  N   SER C 245     6340  11050   7005   -122   1299  -1428       N  
ATOM   5546  CA  SER C 245      -8.012  52.878  83.315  1.00 64.43           C  
ANISOU 5546  CA  SER C 245     6304  10984   7191    -61   1296  -1536       C  
ATOM   5547  C   SER C 245      -9.302  53.323  83.994  1.00 65.58           C  
ANISOU 5547  C   SER C 245     6282  11391   7243    -26   1400  -1645       C  
ATOM   5548  O   SER C 245      -9.664  52.796  85.050  1.00 67.50           O  
ANISOU 5548  O   SER C 245     6452  11885   7310    -93   1485  -1570       O  
ATOM   5549  CB  SER C 245      -8.306  51.866  82.203  1.00 64.74           C  
ANISOU 5549  CB  SER C 245     6370  10851   7379   -156   1263  -1367       C  
ATOM   5550  OG  SER C 245      -9.098  52.425  81.176  1.00 65.07           O  
ANISOU 5550  OG  SER C 245     6356  10794   7574    -94   1246  -1464       O  
ATOM   5551  N   ASP C 246     -10.002  54.295  83.405  1.00 68.03           N  
ANISOU 5551  N   ASP C 246     6527  11657   7665     83   1395  -1816       N  
ATOM   5552  CA  ASP C 246     -11.226  54.788  84.028  1.00 68.73           C  
ANISOU 5552  CA  ASP C 246     6446  11998   7670    136   1492  -1941       C  
ATOM   5553  C   ASP C 246     -12.359  53.775  83.914  1.00 69.59           C  
ANISOU 5553  C   ASP C 246     6438  12231   7772     17   1565  -1785       C  
ATOM   5554  O   ASP C 246     -13.098  53.553  84.880  1.00 70.34           O  
ANISOU 5554  O   ASP C 246     6405  12614   7709    -19   1670  -1773       O  
ATOM   5555  CB  ASP C 246     -11.638  56.121  83.405  1.00 67.92           C  
ANISOU 5555  CB  ASP C 246     6307  11795   7704    298   1456  -2166       C  
ATOM   5556  CG  ASP C 246     -11.120  57.314  84.183  1.00 67.64           C  
ANISOU 5556  CG  ASP C 246     6290  11815   7596    428   1446  -2389       C  
ATOM   5557  OD1 ASP C 246     -10.264  57.122  85.073  1.00 67.81           O  
ANISOU 5557  OD1 ASP C 246     6373  11921   7472    394   1449  -2367       O  
ATOM   5558  OD2 ASP C 246     -11.575  58.445  83.908  1.00 66.25           O  
ANISOU 5558  OD2 ASP C 246     6066  11594   7513    568   1430  -2587       O  
ATOM   5559  N   LEU C 247     -12.508  53.148  82.747  1.00 68.07           N  
ANISOU 5559  N   LEU C 247     6282  11835   7745    -49   1511  -1665       N  
ATOM   5560  CA  LEU C 247     -13.640  52.268  82.489  1.00 67.55           C  
ANISOU 5560  CA  LEU C 247     6099  11859   7708   -162   1566  -1538       C  
ATOM   5561  C   LEU C 247     -13.341  50.794  82.717  1.00 68.85           C  
ANISOU 5561  C   LEU C 247     6313  12018   7828   -344   1576  -1282       C  
ATOM   5562  O   LEU C 247     -14.281  50.012  82.898  1.00 67.96           O  
ANISOU 5562  O   LEU C 247     6086  12044   7690   -460   1644  -1164       O  
ATOM   5563  CB  LEU C 247     -14.132  52.451  81.047  1.00 63.97           C  
ANISOU 5563  CB  LEU C 247     5637  11202   7466   -127   1497  -1572       C  
ATOM   5564  CG  LEU C 247     -14.350  53.893  80.590  1.00 64.01           C  
ANISOU 5564  CG  LEU C 247     5615  11147   7558     59   1463  -1801       C  
ATOM   5565  CD1 LEU C 247     -14.905  53.928  79.175  1.00 63.86           C  
ANISOU 5565  CD1 LEU C 247     5577  10955   7732     79   1397  -1799       C  
ATOM   5566  CD2 LEU C 247     -15.266  54.633  81.552  1.00 63.77           C  
ANISOU 5566  CD2 LEU C 247     5422  11400   7410    144   1563  -1957       C  
ATOM   5567  N   TYR C 248     -12.072  50.392  82.718  1.00 68.92           N  
ANISOU 5567  N   TYR C 248     6484  11869   7832   -373   1508  -1191       N  
ATOM   5568  CA  TYR C 248     -11.702  48.982  82.712  1.00 71.18           C  
ANISOU 5568  CA  TYR C 248     6840  12082   8122   -532   1492   -948       C  
ATOM   5569  C   TYR C 248     -10.692  48.719  83.818  1.00 71.14           C  
ANISOU 5569  C   TYR C 248     6916  12166   7948   -554   1502   -869       C  
ATOM   5570  O   TYR C 248      -9.574  49.242  83.780  1.00 70.98           O  
ANISOU 5570  O   TYR C 248     7012  12028   7927   -471   1434   -943       O  
ATOM   5571  CB  TYR C 248     -11.152  48.584  81.340  1.00 70.86           C  
ANISOU 5571  CB  TYR C 248     6922  11720   8281   -545   1379   -899       C  
ATOM   5572  CG  TYR C 248     -12.096  48.960  80.219  1.00 69.69           C  
ANISOU 5572  CG  TYR C 248     6696  11494   8290   -505   1359   -992       C  
ATOM   5573  CD1 TYR C 248     -13.352  48.374  80.124  1.00 69.13           C  
ANISOU 5573  CD1 TYR C 248     6486  11534   8245   -602   1415   -926       C  
ATOM   5574  CD2 TYR C 248     -11.747  49.919  79.275  1.00 68.08           C  
ANISOU 5574  CD2 TYR C 248     6548  11115   8204   -373   1282  -1142       C  
ATOM   5575  CE1 TYR C 248     -14.228  48.718  79.113  1.00 69.86           C  
ANISOU 5575  CE1 TYR C 248     6498  11571   8473   -562   1391  -1014       C  
ATOM   5576  CE2 TYR C 248     -12.618  50.270  78.257  1.00 67.58           C  
ANISOU 5576  CE2 TYR C 248     6410  10993   8274   -330   1259  -1218       C  
ATOM   5577  CZ  TYR C 248     -13.857  49.665  78.182  1.00 69.16           C  
ANISOU 5577  CZ  TYR C 248     6472  11312   8494   -422   1312  -1159       C  
ATOM   5578  OH  TYR C 248     -14.731  50.007  77.175  1.00 68.62           O  
ANISOU 5578  OH  TYR C 248     6322  11198   8553   -377   1283  -1236       O  
ATOM   5579  N   ASP C 249     -11.087  47.899  84.797  1.00 72.23           N  
ANISOU 5579  N   ASP C 249     6986  12517   7942   -672   1584   -709       N  
ATOM   5580  CA  ASP C 249     -10.275  47.693  85.991  1.00 72.81           C  
ANISOU 5580  CA  ASP C 249     7109  12735   7820   -688   1606   -633       C  
ATOM   5581  C   ASP C 249      -9.042  46.837  85.731  1.00 71.34           C  
ANISOU 5581  C   ASP C 249     7093  12327   7687   -743   1513   -466       C  
ATOM   5582  O   ASP C 249      -8.091  46.893  86.518  1.00 72.31           O  
ANISOU 5582  O   ASP C 249     7286  12514   7676   -717   1497   -444       O  
ATOM   5583  CB  ASP C 249     -11.121  47.057  87.095  1.00 74.39           C  
ANISOU 5583  CB  ASP C 249     7177  13245   7844   -800   1726   -491       C  
ATOM   5584  CG  ASP C 249     -12.338  47.889  87.449  1.00 75.25           C  
ANISOU 5584  CG  ASP C 249     7102  13610   7879   -738   1828   -661       C  
ATOM   5585  OD1 ASP C 249     -12.296  49.120  87.245  1.00 73.66           O  
ANISOU 5585  OD1 ASP C 249     6890  13395   7701   -581   1808   -909       O  
ATOM   5586  OD2 ASP C 249     -13.338  47.311  87.927  1.00 77.20           O  
ANISOU 5586  OD2 ASP C 249     7211  14070   8050   -846   1926   -544       O  
ATOM   5587  N   HIS C 250      -9.032  46.049  84.660  1.00 58.43           N  
ANISOU 5587  N   HIS C 250     5519  10442   6241   -813   1449   -357       N  
ATOM   5588  CA  HIS C 250      -7.900  45.187  84.352  1.00 60.54           C  
ANISOU 5588  CA  HIS C 250     5940  10490   6572   -858   1359   -205       C  
ATOM   5589  C   HIS C 250      -6.887  45.843  83.423  1.00 59.43           C  
ANISOU 5589  C   HIS C 250     5920  10108   6552   -739   1254   -341       C  
ATOM   5590  O   HIS C 250      -5.836  45.249  83.157  1.00 57.62           O  
ANISOU 5590  O   HIS C 250     5817   9705   6370   -752   1176   -242       O  
ATOM   5591  CB  HIS C 250      -8.389  43.873  83.732  1.00 63.45           C  
ANISOU 5591  CB  HIS C 250     6314  10716   7079  -1003   1342    -10       C  
ATOM   5592  CG  HIS C 250      -9.121  44.050  82.438  1.00 64.56           C  
ANISOU 5592  CG  HIS C 250     6416  10702   7411   -991   1311   -108       C  
ATOM   5593  ND1 HIS C 250     -10.384  44.597  82.365  1.00 64.76           N  
ANISOU 5593  ND1 HIS C 250     6289  10878   7439   -984   1382   -213       N  
ATOM   5594  CD2 HIS C 250      -8.766  43.753  81.166  1.00 64.40           C  
ANISOU 5594  CD2 HIS C 250     6485  10404   7580   -980   1215   -118       C  
ATOM   5595  CE1 HIS C 250     -10.776  44.628  81.104  1.00 63.94           C  
ANISOU 5595  CE1 HIS C 250     6184  10594   7517   -971   1326   -278       C  
ATOM   5596  NE2 HIS C 250      -9.813  44.122  80.356  1.00 63.52           N  
ANISOU 5596  NE2 HIS C 250     6276  10283   7574   -970   1226   -224       N  
ATOM   5597  N   LEU C 251      -7.171  47.044  82.927  1.00 54.62           N  
ANISOU 5597  N   LEU C 251     5271   9486   5995   -624   1250   -558       N  
ATOM   5598  CA  LEU C 251      -6.281  47.760  82.024  1.00 51.35           C  
ANISOU 5598  CA  LEU C 251     4958   8854   5697   -516   1156   -684       C  
ATOM   5599  C   LEU C 251      -5.608  48.899  82.775  1.00 50.96           C  
ANISOU 5599  C   LEU C 251     4923   8909   5530   -405   1157   -843       C  
ATOM   5600  O   LEU C 251      -6.286  49.728  83.391  1.00 47.40           O  
ANISOU 5600  O   LEU C 251     4371   8650   4991   -350   1224   -981       O  
ATOM   5601  CB  LEU C 251      -7.047  48.301  80.815  1.00 48.50           C  
ANISOU 5601  CB  LEU C 251     4550   8375   5501   -466   1136   -802       C  
ATOM   5602  CG  LEU C 251      -7.594  47.254  79.843  1.00 50.10           C  
ANISOU 5602  CG  LEU C 251     4751   8435   5847   -564   1110   -677       C  
ATOM   5603  CD1 LEU C 251      -8.379  47.917  78.721  1.00 49.93           C  
ANISOU 5603  CD1 LEU C 251     4670   8334   5965   -500   1089   -809       C  
ATOM   5604  CD2 LEU C 251      -6.461  46.409  79.282  1.00 50.76           C  
ANISOU 5604  CD2 LEU C 251     4981   8297   6009   -596   1020   -557       C  
ATOM   5605  N   TYR C 252      -4.280  48.933  82.728  1.00 50.19           N  
ANISOU 5605  N   TYR C 252     4945   8689   5434   -371   1081   -830       N  
ATOM   5606  CA  TYR C 252      -3.497  49.972  83.376  1.00 50.27           C  
ANISOU 5606  CA  TYR C 252     4979   8770   5350   -276   1064   -981       C  
ATOM   5607  C   TYR C 252      -2.665  50.705  82.334  1.00 49.52           C  
ANISOU 5607  C   TYR C 252     4971   8437   5407   -192    971  -1088       C  
ATOM   5608  O   TYR C 252      -2.092  50.084  81.431  1.00 49.05           O  
ANISOU 5608  O   TYR C 252     4995   8177   5465   -219    906   -987       O  
ATOM   5609  CB  TYR C 252      -2.595  49.388  84.469  1.00 50.34           C  
ANISOU 5609  CB  TYR C 252     5039   8895   5192   -318   1059   -863       C  
ATOM   5610  CG  TYR C 252      -3.326  49.091  85.762  1.00 52.82           C  
ANISOU 5610  CG  TYR C 252     5254   9510   5306   -371   1159   -808       C  
ATOM   5611  CD1 TYR C 252      -4.164  47.988  85.873  1.00 54.90           C  
ANISOU 5611  CD1 TYR C 252     5465   9838   5557   -488   1217   -619       C  
ATOM   5612  CD2 TYR C 252      -3.178  49.914  86.872  1.00 51.74           C  
ANISOU 5612  CD2 TYR C 252     5072   9598   4990   -307   1194   -946       C  
ATOM   5613  CE1 TYR C 252      -4.835  47.713  87.052  1.00 56.44           C  
ANISOU 5613  CE1 TYR C 252     5562  10324   5561   -544   1314   -552       C  
ATOM   5614  CE2 TYR C 252      -3.846  49.647  88.055  1.00 53.81           C  
ANISOU 5614  CE2 TYR C 252     5236  10161   5049   -352   1290   -895       C  
ATOM   5615  CZ  TYR C 252      -4.672  48.546  88.139  1.00 56.26           C  
ANISOU 5615  CZ  TYR C 252     5491  10539   5344   -472   1353   -689       C  
ATOM   5616  OH  TYR C 252      -5.337  48.277  89.313  1.00 58.19           O  
ANISOU 5616  OH  TYR C 252     5630  11098   5380   -524   1455   -623       O  
ATOM   5617  N   VAL C 253      -2.607  52.023  82.462  1.00 48.74           N  
ANISOU 5617  N   VAL C 253     4849   8363   5308    -90    965  -1292       N  
ATOM   5618  CA  VAL C 253      -1.934  52.877  81.488  1.00 45.67           C  
ANISOU 5618  CA  VAL C 253     4526   7759   5068    -11    884  -1399       C  
ATOM   5619  C   VAL C 253      -0.829  53.628  82.214  1.00 45.19           C  
ANISOU 5619  C   VAL C 253     4511   7732   4926     41    845  -1504       C  
ATOM   5620  O   VAL C 253      -0.878  53.801  83.445  1.00 46.32           O  
ANISOU 5620  O   VAL C 253     4611   8088   4902     45    889  -1556       O  
ATOM   5621  CB  VAL C 253      -2.921  53.847  80.798  1.00 43.96           C  
ANISOU 5621  CB  VAL C 253     4239   7496   4968     66    899  -1549       C  
ATOM   5622  CG1 VAL C 253      -3.950  53.072  79.994  1.00 44.70           C  
ANISOU 5622  CG1 VAL C 253     4285   7550   5148      9    925  -1445       C  
ATOM   5623  CG2 VAL C 253      -3.601  54.735  81.831  1.00 44.29           C  
ANISOU 5623  CG2 VAL C 253     4182   7747   4899    128    964  -1718       C  
ATOM   5624  N   PRO C 254       0.194  54.085  81.489  1.00 48.77           N  
ANISOU 5624  N   PRO C 254     5047   7992   5490     79    761  -1537       N  
ATOM   5625  CA  PRO C 254       1.212  54.931  82.122  1.00 48.75           C  
ANISOU 5625  CA  PRO C 254     5078   8013   5432    127    717  -1659       C  
ATOM   5626  C   PRO C 254       0.576  56.183  82.706  1.00 49.21           C  
ANISOU 5626  C   PRO C 254     5062   8176   5460    206    750  -1880       C  
ATOM   5627  O   PRO C 254      -0.293  56.806  82.093  1.00 49.30           O  
ANISOU 5627  O   PRO C 254     5027   8123   5582    258    766  -1970       O  
ATOM   5628  CB  PRO C 254       2.170  55.262  80.972  1.00 48.37           C  
ANISOU 5628  CB  PRO C 254     5111   7718   5547    150    629  -1653       C  
ATOM   5629  CG  PRO C 254       1.959  54.168  79.975  1.00 47.12           C  
ANISOU 5629  CG  PRO C 254     4984   7445   5475     97    624  -1479       C  
ATOM   5630  CD  PRO C 254       0.508  53.806  80.077  1.00 48.06           C  
ANISOU 5630  CD  PRO C 254     5020   7669   5573     74    702  -1460       C  
ATOM   5631  N   ALA C 255       1.016  56.542  83.914  1.00 47.29           N  
ANISOU 5631  N   ALA C 255     4805   8101   5063    222    755  -1974       N  
ATOM   5632  CA  ALA C 255       0.362  57.621  84.646  1.00 47.62           C  
ANISOU 5632  CA  ALA C 255     4768   8280   5047    300    794  -2195       C  
ATOM   5633  C   ALA C 255       0.504  58.964  83.941  1.00 46.73           C  
ANISOU 5633  C   ALA C 255     4673   7969   5114    387    734  -2377       C  
ATOM   5634  O   ALA C 255      -0.387  59.814  84.049  1.00 48.78           O  
ANISOU 5634  O   ALA C 255     4863   8266   5406    465    766  -2542       O  
ATOM   5635  CB  ALA C 255       0.925  57.704  86.065  1.00 48.52           C  
ANISOU 5635  CB  ALA C 255     4869   8616   4949    298    801  -2263       C  
ATOM   5636  N   GLY C 256       1.595  59.172  83.208  1.00 45.61           N  
ANISOU 5636  N   GLY C 256     4618   7616   5094    378    647  -2343       N  
ATOM   5637  CA  GLY C 256       1.868  60.478  82.639  1.00 45.88           C  
ANISOU 5637  CA  GLY C 256     4674   7465   5295    449    584  -2502       C  
ATOM   5638  C   GLY C 256       1.706  60.588  81.137  1.00 45.53           C  
ANISOU 5638  C   GLY C 256     4662   7181   5456    459    550  -2423       C  
ATOM   5639  O   GLY C 256       2.234  61.522  80.525  1.00 44.13           O  
ANISOU 5639  O   GLY C 256     4523   6817   5426    497    483  -2497       O  
ATOM   5640  N   SER C 257       0.983  59.651  80.528  1.00 52.02           N  
ANISOU 5640  N   SER C 257     5467   8009   6291    423    593  -2272       N  
ATOM   5641  CA  SER C 257       0.756  59.716  79.090  1.00 50.33           C  
ANISOU 5641  CA  SER C 257     5276   7593   6255    436    562  -2201       C  
ATOM   5642  C   SER C 257      -0.036  60.965  78.726  1.00 48.14           C  
ANISOU 5642  C   SER C 257     4951   7238   6103    535    556  -2361       C  
ATOM   5643  O   SER C 257      -0.893  61.427  79.483  1.00 48.10           O  
ANISOU 5643  O   SER C 257     4869   7368   6039    589    606  -2499       O  
ATOM   5644  CB  SER C 257       0.019  58.469  78.602  1.00 51.09           C  
ANISOU 5644  CB  SER C 257     5350   7729   6332    378    608  -2033       C  
ATOM   5645  OG  SER C 257       0.515  57.301  79.225  1.00 52.36           O  
ANISOU 5645  OG  SER C 257     5539   7998   6359    295    627  -1900       O  
ATOM   5646  N   GLU C 258       0.263  61.513  77.548  1.00 45.85           N  
ANISOU 5646  N   GLU C 258     4704   6731   5984    563    494  -2339       N  
ATOM   5647  CA  GLU C 258      -0.409  62.735  77.116  1.00 45.65           C  
ANISOU 5647  CA  GLU C 258     4644   6602   6099    661    475  -2473       C  
ATOM   5648  C   GLU C 258      -1.898  62.496  76.897  1.00 47.37           C  
ANISOU 5648  C   GLU C 258     4772   6908   6319    701    537  -2475       C  
ATOM   5649  O   GLU C 258      -2.737  63.278  77.361  1.00 48.89           O  
ANISOU 5649  O   GLU C 258     4893   7162   6522    786    564  -2633       O  
ATOM   5650  CB  GLU C 258       0.242  63.280  75.844  1.00 43.89           C  
ANISOU 5650  CB  GLU C 258     4487   6137   6053    672    397  -2411       C  
ATOM   5651  CG  GLU C 258       1.672  63.768  76.024  1.00 45.57           C  
ANISOU 5651  CG  GLU C 258     4771   6250   6291    641    331  -2432       C  
ATOM   5652  CD  GLU C 258       1.776  64.980  76.936  1.00 47.36           C  
ANISOU 5652  CD  GLU C 258     4982   6474   6538    699    309  -2647       C  
ATOM   5653  OE1 GLU C 258       0.843  65.811  76.939  1.00 46.40           O  
ANISOU 5653  OE1 GLU C 258     4811   6326   6494    790    318  -2775       O  
ATOM   5654  OE2 GLU C 258       2.796  65.100  77.648  1.00 48.42           O  
ANISOU 5654  OE2 GLU C 258     5150   6634   6613    658    279  -2694       O  
ATOM   5655  N   VAL C 259      -2.249  61.422  76.189  1.00 40.98           N  
ANISOU 5655  N   VAL C 259     3960   6109   5503    642    557  -2309       N  
ATOM   5656  CA  VAL C 259      -3.637  61.142  75.835  1.00 42.27           C  
ANISOU 5656  CA  VAL C 259     4033   6346   5683    666    606  -2297       C  
ATOM   5657  C   VAL C 259      -3.920  59.661  76.057  1.00 43.64           C  
ANISOU 5657  C   VAL C 259     4187   6656   5737    561    661  -2149       C  
ATOM   5658  O   VAL C 259      -3.112  58.805  75.686  1.00 43.52           O  
ANISOU 5658  O   VAL C 259     4247   6579   5710    483    633  -2008       O  
ATOM   5659  CB  VAL C 259      -3.941  61.538  74.373  1.00 41.80           C  
ANISOU 5659  CB  VAL C 259     3983   6105   5793    715    552  -2250       C  
ATOM   5660  CG1 VAL C 259      -5.333  61.085  73.975  1.00 40.97           C  
ANISOU 5660  CG1 VAL C 259     3780   6090   5696    727    597  -2222       C  
ATOM   5661  CG2 VAL C 259      -3.802  63.041  74.183  1.00 40.79           C  
ANISOU 5661  CG2 VAL C 259     3866   5835   5796    822    499  -2387       C  
ATOM   5662  N   VAL C 260      -5.067  59.361  76.663  1.00 47.96           N  
ANISOU 5662  N   VAL C 260     4630   7388   6205    560    738  -2182       N  
ATOM   5663  CA  VAL C 260      -5.538  57.993  76.856  1.00 48.54           C  
ANISOU 5663  CA  VAL C 260     4668   7589   6184    455    794  -2038       C  
ATOM   5664  C   VAL C 260      -6.902  57.866  76.190  1.00 48.22           C  
ANISOU 5664  C   VAL C 260     4528   7582   6213    473    822  -2031       C  
ATOM   5665  O   VAL C 260      -7.854  58.552  76.578  1.00 47.82           O  
ANISOU 5665  O   VAL C 260     4374   7639   6156    549    865  -2160       O  
ATOM   5666  CB  VAL C 260      -5.622  57.612  78.343  1.00 48.61           C  
ANISOU 5666  CB  VAL C 260     4633   7831   6006    412    869  -2058       C  
ATOM   5667  CG1 VAL C 260      -6.218  56.222  78.498  1.00 50.12           C  
ANISOU 5667  CG1 VAL C 260     4781   8144   6120    296    927  -1894       C  
ATOM   5668  CG2 VAL C 260      -4.249  57.677  78.994  1.00 49.17           C  
ANISOU 5668  CG2 VAL C 260     4799   7882   6001    392    833  -2059       C  
ATOM   5669  N   LEU C 261      -6.992  57.004  75.180  1.00 45.73           N  
ANISOU 5669  N   LEU C 261     4237   7175   5963    409    793  -1892       N  
ATOM   5670  CA  LEU C 261      -8.250  56.663  74.528  1.00 46.03           C  
ANISOU 5670  CA  LEU C 261     4178   7253   6058    402    814  -1865       C  
ATOM   5671  C   LEU C 261      -8.699  55.318  75.079  1.00 48.10           C  
ANISOU 5671  C   LEU C 261     4395   7662   6220    272    877  -1742       C  
ATOM   5672  O   LEU C 261      -8.113  54.283  74.754  1.00 48.20           O  
ANISOU 5672  O   LEU C 261     4484   7598   6232    178    849  -1602       O  
ATOM   5673  CB  LEU C 261      -8.082  56.588  73.013  1.00 44.02           C  
ANISOU 5673  CB  LEU C 261     3975   6808   5941    414    734  -1799       C  
ATOM   5674  CG  LEU C 261      -7.235  57.653  72.320  1.00 43.44           C  
ANISOU 5674  CG  LEU C 261     3986   6550   5968    506    657  -1851       C  
ATOM   5675  CD1 LEU C 261      -7.091  57.329  70.840  1.00 41.78           C  
ANISOU 5675  CD1 LEU C 261     3821   6193   5861    498    588  -1756       C  
ATOM   5676  CD2 LEU C 261      -7.870  59.014  72.507  1.00 42.60           C  
ANISOU 5676  CD2 LEU C 261     3811   6458   5917    634    662  -2010       C  
ATOM   5677  N   GLU C 262      -9.720  55.326  75.921  1.00 49.13           N  
ANISOU 5677  N   GLU C 262     4401   8000   6267    267    961  -1792       N  
ATOM   5678  CA  GLU C 262     -10.292  54.084  76.415  1.00 50.66           C  
ANISOU 5678  CA  GLU C 262     4534   8339   6377    135   1025  -1664       C  
ATOM   5679  C   GLU C 262     -11.416  53.675  75.477  1.00 49.47           C  
ANISOU 5679  C   GLU C 262     4292   8178   6325    106   1021  -1627       C  
ATOM   5680  O   GLU C 262     -12.300  54.482  75.178  1.00 48.14           O  
ANISOU 5680  O   GLU C 262     4025   8054   6211    199   1029  -1742       O  
ATOM   5681  CB  GLU C 262     -10.797  54.260  77.845  1.00 51.56           C  
ANISOU 5681  CB  GLU C 262     4548   8710   6332    134   1125  -1725       C  
ATOM   5682  CG  GLU C 262      -9.694  54.680  78.802  1.00 52.36           C  
ANISOU 5682  CG  GLU C 262     4733   8838   6324    165   1123  -1776       C  
ATOM   5683  CD  GLU C 262     -10.184  54.899  80.217  1.00 54.42           C  
ANISOU 5683  CD  GLU C 262     4893   9375   6411    175   1220  -1851       C  
ATOM   5684  OE1 GLU C 262     -11.243  54.348  80.576  1.00 57.25           O  
ANISOU 5684  OE1 GLU C 262     5126   9917   6707    113   1301  -1799       O  
ATOM   5685  OE2 GLU C 262      -9.499  55.611  80.979  1.00 55.55           O  
ANISOU 5685  OE2 GLU C 262     5074   9560   6471    241   1217  -1962       O  
ATOM   5686  N   GLY C 263     -11.369  52.449  74.982  1.00 49.90           N  
ANISOU 5686  N   GLY C 263     4381   8167   6411    -17    999  -1475       N  
ATOM   5687  CA  GLY C 263     -12.390  52.030  74.055  1.00 49.89           C  
ANISOU 5687  CA  GLY C 263     4296   8153   6508    -52    983  -1447       C  
ATOM   5688  C   GLY C 263     -12.499  50.537  73.975  1.00 52.46           C  
ANISOU 5688  C   GLY C 263     4631   8466   6834   -215    986  -1282       C  
ATOM   5689  O   GLY C 263     -12.011  49.810  74.840  1.00 54.45           O  
ANISOU 5689  O   GLY C 263     4927   8766   6995   -306   1022  -1181       O  
ATOM   5690  N   HIS C 264     -13.139  50.073  72.908  1.00 48.23           N  
ANISOU 5690  N   HIS C 264     4056   7860   6408   -253    941  -1255       N  
ATOM   5691  CA  HIS C 264     -13.299  48.641  72.723  1.00 50.03           C  
ANISOU 5691  CA  HIS C 264     4293   8051   6665   -411    931  -1110       C  
ATOM   5692  C   HIS C 264     -13.361  48.306  71.242  1.00 48.99           C  
ANISOU 5692  C   HIS C 264     4194   7750   6668   -411    835  -1109       C  
ATOM   5693  O   HIS C 264     -13.862  49.085  70.427  1.00 49.09           O  
ANISOU 5693  O   HIS C 264     4153   7752   6746   -314    800  -1208       O  
ATOM   5694  CB  HIS C 264     -14.557  48.120  73.427  1.00 51.47           C  
ANISOU 5694  CB  HIS C 264     4314   8441   6803   -518   1019  -1065       C  
ATOM   5695  CG  HIS C 264     -15.830  48.694  72.890  1.00 53.70           C  
ANISOU 5695  CG  HIS C 264     4440   8820   7145   -466   1029  -1167       C  
ATOM   5696  ND1 HIS C 264     -16.431  49.809  73.433  1.00 53.89           N  
ANISOU 5696  ND1 HIS C 264     4354   9010   7112   -352   1090  -1294       N  
ATOM   5697  CD2 HIS C 264     -16.613  48.310  71.854  1.00 53.85           C  
ANISOU 5697  CD2 HIS C 264     4391   8796   7275   -504    979  -1166       C  
ATOM   5698  CE1 HIS C 264     -17.533  50.084  72.759  1.00 53.75           C  
ANISOU 5698  CE1 HIS C 264     4204   9047   7170   -319   1080  -1360       C  
ATOM   5699  NE2 HIS C 264     -17.668  49.189  71.797  1.00 53.83           N  
ANISOU 5699  NE2 HIS C 264     4235   8938   7279   -414   1012  -1282       N  
ATOM   5700  N   ILE C 265     -12.837  47.130  70.912  1.00 43.73           N  
ANISOU 5700  N   ILE C 265     3617   6955   6041   -517    790   -996       N  
ATOM   5701  CA  ILE C 265     -13.071  46.534  69.606  1.00 43.22           C  
ANISOU 5701  CA  ILE C 265     3565   6762   6096   -549    705   -988       C  
ATOM   5702  C   ILE C 265     -14.545  46.177  69.499  1.00 44.43           C  
ANISOU 5702  C   ILE C 265     3552   7039   6289   -632    734   -991       C  
ATOM   5703  O   ILE C 265     -15.089  45.452  70.348  1.00 45.28           O  
ANISOU 5703  O   ILE C 265     3589   7255   6362   -760    800   -905       O  
ATOM   5704  CB  ILE C 265     -12.178  45.310  69.388  1.00 46.12           C  
ANISOU 5704  CB  ILE C 265     4062   6965   6498   -641    652   -877       C  
ATOM   5705  CG1 ILE C 265     -10.720  45.751  69.324  1.00 46.24           C  
ANISOU 5705  CG1 ILE C 265     4227   6863   6480   -543    615   -888       C  
ATOM   5706  CG2 ILE C 265     -12.572  44.582  68.108  1.00 46.13           C  
ANISOU 5706  CG2 ILE C 265     4057   6853   6616   -688    568   -883       C  
ATOM   5707  CD1 ILE C 265      -9.757  44.677  69.648  1.00 48.13           C  
ANISOU 5707  CD1 ILE C 265     4584   6993   6712   -621    593   -772       C  
ATOM   5708  N   ILE C 266     -15.190  46.715  68.468  1.00 44.94           N  
ANISOU 5708  N   ILE C 266     3549   7101   6426   -557    685  -1085       N  
ATOM   5709  CA  ILE C 266     -16.596  46.509  68.143  1.00 45.54           C  
ANISOU 5709  CA  ILE C 266     3457   7292   6553   -614    694  -1110       C  
ATOM   5710  C   ILE C 266     -16.737  45.117  67.543  1.00 47.94           C  
ANISOU 5710  C   ILE C 266     3781   7492   6942   -766    635  -1030       C  
ATOM   5711  O   ILE C 266     -16.104  44.813  66.521  1.00 49.81           O  
ANISOU 5711  O   ILE C 266     4124   7561   7242   -742    541  -1041       O  
ATOM   5712  CB  ILE C 266     -17.103  47.590  67.175  1.00 43.78           C  
ANISOU 5712  CB  ILE C 266     3171   7087   6379   -466    645  -1234       C  
ATOM   5713  CG1 ILE C 266     -16.767  48.987  67.706  1.00 45.13           C  
ANISOU 5713  CG1 ILE C 266     3352   7308   6486   -306    686  -1318       C  
ATOM   5714  CG2 ILE C 266     -18.599  47.447  66.947  1.00 48.51           C  
ANISOU 5714  CG2 ILE C 266     3576   7834   7021   -516    659  -1266       C  
ATOM   5715  CD1 ILE C 266     -16.812  50.074  66.649  1.00 44.89           C  
ANISOU 5715  CD1 ILE C 266     3323   7219   6513   -144    616  -1415       C  
ATOM   5716  N   PRO C 267     -17.545  44.246  68.138  1.00 55.23           N  
ANISOU 5716  N   PRO C 267     4603   8509   7874   -925    686   -950       N  
ATOM   5717  CA  PRO C 267     -17.602  42.859  67.669  1.00 56.40           C  
ANISOU 5717  CA  PRO C 267     4782   8531   8116  -1083    626   -868       C  
ATOM   5718  C   PRO C 267     -18.256  42.748  66.301  1.00 54.91           C  
ANISOU 5718  C   PRO C 267     4534   8297   8033  -1074    531   -954       C  
ATOM   5719  O   PRO C 267     -19.244  43.424  66.005  1.00 54.09           O  
ANISOU 5719  O   PRO C 267     4284   8331   7935  -1021    541  -1037       O  
ATOM   5720  CB  PRO C 267     -18.435  42.154  68.746  1.00 58.20           C  
ANISOU 5720  CB  PRO C 267     4889   8903   8320  -1252    717   -759       C  
ATOM   5721  CG  PRO C 267     -19.246  43.247  69.370  1.00 57.82           C  
ANISOU 5721  CG  PRO C 267     4689   9094   8186  -1170    809   -830       C  
ATOM   5722  CD  PRO C 267     -18.383  44.472  69.327  1.00 55.92           C  
ANISOU 5722  CD  PRO C 267     4545   8822   7880   -971    803   -926       C  
ATOM   5723  N   ARG C 268     -17.679  41.881  65.466  1.00 54.87           N  
ANISOU 5723  N   ARG C 268     4640   8099   8107  -1120    435   -939       N  
ATOM   5724  CA  ARG C 268     -18.253  41.475  64.183  1.00 56.26           C  
ANISOU 5724  CA  ARG C 268     4770   8221   8385  -1145    335  -1012       C  
ATOM   5725  C   ARG C 268     -18.344  42.627  63.186  1.00 56.96           C  
ANISOU 5725  C   ARG C 268     4834   8348   8458   -965    284  -1138       C  
ATOM   5726  O   ARG C 268     -19.246  42.654  62.347  1.00 58.37           O  
ANISOU 5726  O   ARG C 268     4902   8585   8691   -968    229  -1209       O  
ATOM   5727  CB  ARG C 268     -19.633  40.835  64.366  1.00 55.65           C  
ANISOU 5727  CB  ARG C 268     4514   8260   8371  -1306    356   -988       C  
ATOM   5728  CG  ARG C 268     -19.762  39.941  65.587  1.00 54.19           C  
ANISOU 5728  CG  ARG C 268     4311   8097   8181  -1483    436   -841       C  
ATOM   5729  CD  ARG C 268     -21.095  39.223  65.581  1.00 58.90           C  
ANISOU 5729  CD  ARG C 268     4731   8787   8861  -1659    441   -815       C  
ATOM   5730  NE  ARG C 268     -21.302  38.498  64.332  1.00 58.42           N  
ANISOU 5730  NE  ARG C 268     4681   8589   8928  -1714    314   -881       N  
ATOM   5731  CZ  ARG C 268     -20.724  37.338  64.038  1.00 59.87           C  
ANISOU 5731  CZ  ARG C 268     4986   8559   9203  -1817    241   -832       C  
ATOM   5732  NH1 ARG C 268     -19.897  36.766  64.905  1.00 60.97           N  
ANISOU 5732  NH1 ARG C 268     5247   8594   9324  -1876    282   -702       N  
ATOM   5733  NH2 ARG C 268     -20.969  36.749  62.876  1.00 59.52           N  
ANISOU 5733  NH2 ARG C 268     4940   8406   9269  -1856    122   -919       N  
ATOM   5734  N   VAL C 269     -17.419  43.580  63.250  1.00 56.25           N  
ANISOU 5734  N   VAL C 269     4847   8228   8299   -812    297  -1161       N  
ATOM   5735  CA  VAL C 269     -17.376  44.696  62.314  1.00 52.92           C  
ANISOU 5735  CA  VAL C 269     4421   7821   7866   -640    246  -1258       C  
ATOM   5736  C   VAL C 269     -16.045  44.660  61.581  1.00 52.34           C  
ANISOU 5736  C   VAL C 269     4523   7577   7787   -564    177  -1261       C  
ATOM   5737  O   VAL C 269     -14.984  44.576  62.211  1.00 51.66           O  
ANISOU 5737  O   VAL C 269     4559   7409   7658   -559    209  -1204       O  
ATOM   5738  CB  VAL C 269     -17.574  46.049  63.022  1.00 51.99           C  
ANISOU 5738  CB  VAL C 269     4244   7831   7680   -516    325  -1292       C  
ATOM   5739  CG1 VAL C 269     -17.279  47.194  62.065  1.00 52.03           C  
ANISOU 5739  CG1 VAL C 269     4281   7805   7684   -336    265  -1368       C  
ATOM   5740  CG2 VAL C 269     -18.989  46.155  63.558  1.00 50.52           C  
ANISOU 5740  CG2 VAL C 269     3860   7837   7499   -569    387  -1311       C  
ATOM   5741  N   ARG C 270     -16.104  44.716  60.253  1.00 55.81           N  
ANISOU 5741  N   ARG C 270     4967   7978   8261   -504     81  -1326       N  
ATOM   5742  CA  ARG C 270     -14.915  44.762  59.411  1.00 56.05           C  
ANISOU 5742  CA  ARG C 270     5144   7877   8277   -418     14  -1337       C  
ATOM   5743  C   ARG C 270     -15.112  45.849  58.368  1.00 55.53           C  
ANISOU 5743  C   ARG C 270     5041   7863   8194   -267    -38  -1404       C  
ATOM   5744  O   ARG C 270     -16.075  45.803  57.595  1.00 55.95           O  
ANISOU 5744  O   ARG C 270     4986   7991   8280   -269    -92  -1459       O  
ATOM   5745  CB  ARG C 270     -14.659  43.411  58.742  1.00 55.57           C  
ANISOU 5745  CB  ARG C 270     5143   7698   8273   -516    -64  -1341       C  
ATOM   5746  CG  ARG C 270     -14.406  42.281  59.720  1.00 56.14           C  
ANISOU 5746  CG  ARG C 270     5263   7691   8375   -664    -23  -1258       C  
ATOM   5747  CD  ARG C 270     -13.115  42.481  60.492  1.00 56.75           C  
ANISOU 5747  CD  ARG C 270     5476   7692   8393   -618     26  -1190       C  
ATOM   5748  NE  ARG C 270     -12.709  41.260  61.181  1.00 58.99           N  
ANISOU 5748  NE  ARG C 270     5830   7871   8714   -747     37  -1105       N  
ATOM   5749  CZ  ARG C 270     -13.184  40.874  62.360  1.00 61.08           C  
ANISOU 5749  CZ  ARG C 270     6042   8188   8978   -863    112  -1020       C  
ATOM   5750  NH1 ARG C 270     -14.085  41.615  62.990  1.00 57.60           N  
ANISOU 5750  NH1 ARG C 270     5474   7915   8496   -863    187  -1023       N  
ATOM   5751  NH2 ARG C 270     -12.758  39.746  62.912  1.00 64.49           N  
ANISOU 5751  NH2 ARG C 270     6547   8510   9448   -976    112   -929       N  
ATOM   5752  N   THR C 271     -14.210  46.828  58.350  1.00 49.58           N  
ANISOU 5752  N   THR C 271     4374   7073   7392   -141    -25  -1394       N  
ATOM   5753  CA  THR C 271     -14.292  47.933  57.406  1.00 47.36           C  
ANISOU 5753  CA  THR C 271     4070   6827   7097      6    -73  -1433       C  
ATOM   5754  C   THR C 271     -12.923  48.172  56.785  1.00 44.66           C  
ANISOU 5754  C   THR C 271     3873   6377   6718     86   -110  -1410       C  
ATOM   5755  O   THR C 271     -11.900  47.720  57.300  1.00 44.71           O  
ANISOU 5755  O   THR C 271     3990   6291   6706     47    -84  -1368       O  
ATOM   5756  CB  THR C 271     -14.801  49.222  58.071  1.00 45.09           C  
ANISOU 5756  CB  THR C 271     3705   6627   6799     96    -12  -1446       C  
ATOM   5757  OG1 THR C 271     -13.990  49.527  59.210  1.00 45.57           O  
ANISOU 5757  OG1 THR C 271     3846   6642   6826     96     65  -1409       O  
ATOM   5758  CG2 THR C 271     -16.251  49.062  58.514  1.00 44.80           C  
ANISOU 5758  CG2 THR C 271     3500   6729   6794     35     20  -1479       C  
ATOM   5759  N   VAL C 272     -12.918  48.888  55.663  1.00 40.84           N  
ANISOU 5759  N   VAL C 272     3381   5916   6222    198   -173  -1430       N  
ATOM   5760  CA  VAL C 272     -11.697  49.068  54.885  1.00 41.13           C  
ANISOU 5760  CA  VAL C 272     3537   5874   6218    270   -214  -1404       C  
ATOM   5761  C   VAL C 272     -10.696  49.890  55.688  1.00 41.43           C  
ANISOU 5761  C   VAL C 272     3659   5848   6234    320   -152  -1354       C  
ATOM   5762  O   VAL C 272     -10.955  51.049  56.032  1.00 40.17           O  
ANISOU 5762  O   VAL C 272     3462   5718   6083    398   -123  -1351       O  
ATOM   5763  CB  VAL C 272     -11.999  49.730  53.536  1.00 43.57           C  
ANISOU 5763  CB  VAL C 272     3803   6242   6508    379   -291  -1420       C  
ATOM   5764  CG1 VAL C 272     -10.764  49.693  52.645  1.00 42.79           C  
ANISOU 5764  CG1 VAL C 272     3817   6085   6357    434   -334  -1392       C  
ATOM   5765  CG2 VAL C 272     -13.176  49.041  52.862  1.00 43.53           C  
ANISOU 5765  CG2 VAL C 272     3688   6325   6526    330   -353  -1484       C  
ATOM   5766  N   GLU C 273      -9.547  49.287  55.986  1.00 37.94           N  
ANISOU 5766  N   GLU C 273     3330   5315   5769    279   -138  -1321       N  
ATOM   5767  CA  GLU C 273      -8.424  49.939  56.636  1.00 38.20           C  
ANISOU 5767  CA  GLU C 273     3452   5285   5776    319    -93  -1276       C  
ATOM   5768  C   GLU C 273      -7.237  49.926  55.685  1.00 37.73           C  
ANISOU 5768  C   GLU C 273     3487   5168   5682    374   -140  -1249       C  
ATOM   5769  O   GLU C 273      -7.041  48.964  54.930  1.00 38.56           O  
ANISOU 5769  O   GLU C 273     3618   5259   5775    346   -189  -1267       O  
ATOM   5770  CB  GLU C 273      -8.050  49.236  57.951  1.00 38.91           C  
ANISOU 5770  CB  GLU C 273     3585   5337   5862    223    -30  -1253       C  
ATOM   5771  CG  GLU C 273      -7.096  50.021  58.850  1.00 38.59           C  
ANISOU 5771  CG  GLU C 273     3611   5258   5794    260     22  -1221       C  
ATOM   5772  CD  GLU C 273      -5.637  49.634  58.662  1.00 41.83           C  
ANISOU 5772  CD  GLU C 273     4139   5580   6173    264      5  -1179       C  
ATOM   5773  OE1 GLU C 273      -5.364  48.655  57.934  1.00 42.89           O  
ANISOU 5773  OE1 GLU C 273     4308   5680   6308    236    -42  -1179       O  
ATOM   5774  OE2 GLU C 273      -4.760  50.307  59.247  1.00 41.18           O  
ANISOU 5774  OE2 GLU C 273     4111   5467   6070    296     35  -1155       O  
ATOM   5775  N   GLY C 274      -6.449  50.996  55.728  1.00 35.60           N  
ANISOU 5775  N   GLY C 274     3262   4867   5396    451   -125  -1210       N  
ATOM   5776  CA  GLY C 274      -5.317  51.142  54.850  1.00 33.62           C  
ANISOU 5776  CA  GLY C 274     3086   4581   5107    505   -160  -1173       C  
ATOM   5777  C   GLY C 274      -5.669  51.923  53.601  1.00 35.61           C  
ANISOU 5777  C   GLY C 274     3295   4886   5348    597   -215  -1160       C  
ATOM   5778  O   GLY C 274      -6.814  52.346  53.409  1.00 37.35           O  
ANISOU 5778  O   GLY C 274     3428   5167   5597    624   -231  -1185       O  
ATOM   5779  N   PRO C 275      -4.683  52.131  52.714  1.00 36.67           N  
ANISOU 5779  N   PRO C 275     3485   5012   5437    649   -244  -1115       N  
ATOM   5780  CA  PRO C 275      -3.301  51.662  52.862  1.00 36.58           C  
ANISOU 5780  CA  PRO C 275     3565   4944   5390    628   -228  -1088       C  
ATOM   5781  C   PRO C 275      -2.510  52.477  53.879  1.00 34.65           C  
ANISOU 5781  C   PRO C 275     3367   4633   5167    629   -173  -1043       C  
ATOM   5782  O   PRO C 275      -2.945  53.559  54.270  1.00 34.77           O  
ANISOU 5782  O   PRO C 275     3348   4639   5223    662   -156  -1032       O  
ATOM   5783  CB  PRO C 275      -2.709  51.842  51.454  1.00 37.70           C  
ANISOU 5783  CB  PRO C 275     3722   5134   5470    698   -277  -1052       C  
ATOM   5784  CG  PRO C 275      -3.871  52.194  50.561  1.00 37.49           C  
ANISOU 5784  CG  PRO C 275     3612   5191   5440    746   -327  -1068       C  
ATOM   5785  CD  PRO C 275      -4.873  52.847  51.444  1.00 35.27           C  
ANISOU 5785  CD  PRO C 275     3274   4895   5232    737   -298  -1081       C  
ATOM   5786  N   PHE C 276      -1.369  51.946  54.307  1.00 35.75           N  
ANISOU 5786  N   PHE C 276     3578   4724   5281    595   -152  -1027       N  
ATOM   5787  CA  PHE C 276      -0.490  52.658  55.221  1.00 35.96           C  
ANISOU 5787  CA  PHE C 276     3648   4696   5320    592   -109   -990       C  
ATOM   5788  C   PHE C 276       0.921  52.120  55.052  1.00 35.93           C  
ANISOU 5788  C   PHE C 276     3713   4668   5271    585   -111   -959       C  
ATOM   5789  O   PHE C 276       1.117  50.956  54.692  1.00 36.07           O  
ANISOU 5789  O   PHE C 276     3751   4693   5259    566   -132   -983       O  
ATOM   5790  CB  PHE C 276      -0.940  52.517  56.679  1.00 37.02           C  
ANISOU 5790  CB  PHE C 276     3774   4809   5483    532    -60  -1026       C  
ATOM   5791  CG  PHE C 276      -0.177  53.393  57.633  1.00 35.82           C  
ANISOU 5791  CG  PHE C 276     3654   4613   5342    535    -22  -1007       C  
ATOM   5792  CD1 PHE C 276      -0.337  54.767  57.610  1.00 35.05           C  
ANISOU 5792  CD1 PHE C 276     3533   4497   5286    589    -22   -999       C  
ATOM   5793  CD2 PHE C 276       0.709  52.843  58.545  1.00 35.93           C  
ANISOU 5793  CD2 PHE C 276     3722   4600   5329    485      5   -999       C  
ATOM   5794  CE1 PHE C 276       0.365  55.578  58.484  1.00 35.57           C  
ANISOU 5794  CE1 PHE C 276     3629   4515   5372    588      5   -997       C  
ATOM   5795  CE2 PHE C 276       1.414  53.647  59.423  1.00 35.73           C  
ANISOU 5795  CE2 PHE C 276     3723   4544   5310    486     32   -992       C  
ATOM   5796  CZ  PHE C 276       1.242  55.016  59.392  1.00 34.73           C  
ANISOU 5796  CZ  PHE C 276     3572   4396   5229    534     31   -998       C  
ATOM   5797  N   GLY C 277       1.896  52.983  55.319  1.00 40.38           N  
ANISOU 5797  N   GLY C 277     4306   5200   5836    604    -93   -909       N  
ATOM   5798  CA  GLY C 277       3.280  52.577  55.184  1.00 40.97           C  
ANISOU 5798  CA  GLY C 277     4433   5264   5868    602    -92   -876       C  
ATOM   5799  C   GLY C 277       3.659  51.506  56.187  1.00 41.81           C  
ANISOU 5799  C   GLY C 277     4579   5339   5966    546    -72   -904       C  
ATOM   5800  O   GLY C 277       3.097  51.410  57.279  1.00 43.02           O  
ANISOU 5800  O   GLY C 277     4728   5473   6145    499    -44   -930       O  
ATOM   5801  N   GLU C 278       4.621  50.679  55.795  1.00 48.29           N  
ANISOU 5801  N   GLU C 278     5437   6164   6747    555    -87   -895       N  
ATOM   5802  CA  GLU C 278       5.202  49.679  56.672  1.00 50.23           C  
ANISOU 5802  CA  GLU C 278     5728   6371   6986    514    -75   -904       C  
ATOM   5803  C   GLU C 278       6.712  49.862  56.677  1.00 49.21           C  
ANISOU 5803  C   GLU C 278     5629   6244   6824    539    -71   -861       C  
ATOM   5804  O   GLU C 278       7.281  50.493  55.782  1.00 47.93           O  
ANISOU 5804  O   GLU C 278     5452   6121   6639    585    -80   -829       O  
ATOM   5805  CB  GLU C 278       4.823  48.256  56.236  1.00 54.12           C  
ANISOU 5805  CB  GLU C 278     6233   6853   7478    503   -107   -949       C  
ATOM   5806  CG  GLU C 278       3.318  48.025  56.143  1.00 57.56           C  
ANISOU 5806  CG  GLU C 278     6627   7296   7949    469   -117   -992       C  
ATOM   5807  CD  GLU C 278       2.949  46.556  56.049  1.00 60.63           C  
ANISOU 5807  CD  GLU C 278     7032   7646   8358    430   -147  -1036       C  
ATOM   5808  OE1 GLU C 278       3.393  45.888  55.090  1.00 61.06           O  
ANISOU 5808  OE1 GLU C 278     7104   7702   8392    471   -189  -1069       O  
ATOM   5809  OE2 GLU C 278       2.208  46.070  56.931  1.00 61.91           O  
ANISOU 5809  OE2 GLU C 278     7187   7777   8559    358   -130  -1039       O  
ATOM   5810  N   PHE C 279       7.360  49.302  57.698  1.00 38.69           N  
ANISOU 5810  N   PHE C 279     4333   4880   5487    507    -57   -853       N  
ATOM   5811  CA  PHE C 279       8.793  49.521  57.858  1.00 39.86           C  
ANISOU 5811  CA  PHE C 279     4500   5039   5608    527    -53   -815       C  
ATOM   5812  C   PHE C 279       9.647  49.065  56.672  1.00 40.20           C  
ANISOU 5812  C   PHE C 279     4542   5121   5611    587    -78   -809       C  
ATOM   5813  O   PHE C 279      10.731  49.648  56.492  1.00 39.93           O  
ANISOU 5813  O   PHE C 279     4498   5122   5554    608    -70   -767       O  
ATOM   5814  CB  PHE C 279       9.280  48.877  59.171  1.00 39.88           C  
ANISOU 5814  CB  PHE C 279     4538   5009   5605    488    -42   -807       C  
ATOM   5815  CG  PHE C 279       9.252  47.374  59.176  1.00 42.31           C  
ANISOU 5815  CG  PHE C 279     4880   5283   5913    487    -65   -822       C  
ATOM   5816  CD1 PHE C 279      10.372  46.644  58.813  1.00 41.53           C  
ANISOU 5816  CD1 PHE C 279     4804   5184   5792    533    -88   -815       C  
ATOM   5817  CD2 PHE C 279       8.112  46.690  59.566  1.00 42.20           C  
ANISOU 5817  CD2 PHE C 279     4871   5233   5930    439    -64   -843       C  
ATOM   5818  CE1 PHE C 279      10.349  45.262  58.822  1.00 41.86           C  
ANISOU 5818  CE1 PHE C 279     4881   5173   5850    539   -117   -834       C  
ATOM   5819  CE2 PHE C 279       8.084  45.309  59.578  1.00 41.27           C  
ANISOU 5819  CE2 PHE C 279     4789   5063   5830    430    -91   -852       C  
ATOM   5820  CZ  PHE C 279       9.204  44.594  59.207  1.00 41.32           C  
ANISOU 5820  CZ  PHE C 279     4825   5051   5822    484   -121   -849       C  
ATOM   5821  N   PRO C 280       9.257  48.085  55.842  1.00 39.05           N  
ANISOU 5821  N   PRO C 280     4401   4982   5454    616   -107   -853       N  
ATOM   5822  CA  PRO C 280      10.051  47.809  54.630  1.00 38.68           C  
ANISOU 5822  CA  PRO C 280     4343   4997   5355    685   -127   -859       C  
ATOM   5823  C   PRO C 280      10.113  48.966  53.645  1.00 37.91           C  
ANISOU 5823  C   PRO C 280     4200   4977   5225    717   -120   -816       C  
ATOM   5824  O   PRO C 280      10.881  48.881  52.679  1.00 39.46           O  
ANISOU 5824  O   PRO C 280     4378   5251   5363    773   -128   -806       O  
ATOM   5825  CB  PRO C 280       9.342  46.599  54.013  1.00 40.25           C  
ANISOU 5825  CB  PRO C 280     4554   5180   5559    703   -166   -937       C  
ATOM   5826  CG  PRO C 280       8.750  45.909  55.168  1.00 41.85           C  
ANISOU 5826  CG  PRO C 280     4791   5291   5820    637   -164   -950       C  
ATOM   5827  CD  PRO C 280       8.266  47.013  56.060  1.00 40.90           C  
ANISOU 5827  CD  PRO C 280     4653   5165   5721    584   -125   -904       C  
ATOM   5828  N   GLY C 281       9.334  50.025  53.844  1.00 39.22           N  
ANISOU 5828  N   GLY C 281     4346   5129   5426    687   -108   -787       N  
ATOM   5829  CA  GLY C 281       9.408  51.203  53.006  1.00 40.28           C  
ANISOU 5829  CA  GLY C 281     4442   5318   5545    713   -104   -725       C  
ATOM   5830  C   GLY C 281       8.370  51.301  51.911  1.00 41.09           C  
ANISOU 5830  C   GLY C 281     4513   5470   5628    748   -131   -740       C  
ATOM   5831  O   GLY C 281       8.537  52.120  51.000  1.00 39.60           O  
ANISOU 5831  O   GLY C 281     4292   5346   5408    781   -135   -675       O  
ATOM   5832  N   SER C 282       7.306  50.505  51.970  1.00 39.23           N  
ANISOU 5832  N   SER C 282     4282   5214   5411    737   -153   -815       N  
ATOM   5833  CA  SER C 282       6.285  50.505  50.935  1.00 40.25           C  
ANISOU 5833  CA  SER C 282     4375   5401   5518    769   -187   -841       C  
ATOM   5834  C   SER C 282       4.908  50.495  51.582  1.00 40.11           C  
ANISOU 5834  C   SER C 282     4343   5330   5566    725   -190   -883       C  
ATOM   5835  O   SER C 282       4.757  50.219  52.775  1.00 38.26           O  
ANISOU 5835  O   SER C 282     4133   5023   5383    670   -166   -903       O  
ATOM   5836  CB  SER C 282       6.444  49.305  49.994  1.00 41.76           C  
ANISOU 5836  CB  SER C 282     4569   5652   5646    810   -223   -913       C  
ATOM   5837  OG  SER C 282       6.195  48.092  50.681  1.00 43.35           O  
ANISOU 5837  OG  SER C 282     4806   5776   5890    771   -234   -991       O  
ATOM   5838  N   TYR C 283       3.896  50.804  50.776  1.00 35.09           N  
ANISOU 5838  N   TYR C 283     3662   4747   4923    752   -220   -894       N  
ATOM   5839  CA  TYR C 283       2.523  50.780  51.257  1.00 35.29           C  
ANISOU 5839  CA  TYR C 283     3656   4745   5007    717   -226   -938       C  
ATOM   5840  C   TYR C 283       2.043  49.347  51.440  1.00 34.47           C  
ANISOU 5840  C   TYR C 283     3563   4619   4915    673   -247  -1028       C  
ATOM   5841  O   TYR C 283       2.301  48.476  50.605  1.00 35.98           O  
ANISOU 5841  O   TYR C 283     3764   4846   5062    698   -284  -1076       O  
ATOM   5842  CB  TYR C 283       1.593  51.498  50.279  1.00 34.63           C  
ANISOU 5842  CB  TYR C 283     3513   4734   4911    766   -261   -922       C  
ATOM   5843  CG  TYR C 283       1.715  53.003  50.271  1.00 33.06           C  
ANISOU 5843  CG  TYR C 283     3298   4527   4736    799   -245   -830       C  
ATOM   5844  CD1 TYR C 283       1.147  53.773  51.278  1.00 33.85           C  
ANISOU 5844  CD1 TYR C 283     3386   4559   4916    777   -218   -826       C  
ATOM   5845  CD2 TYR C 283       2.384  53.655  49.243  1.00 33.29           C  
ANISOU 5845  CD2 TYR C 283     3321   4617   4709    854   -259   -746       C  
ATOM   5846  CE1 TYR C 283       1.250  55.155  51.267  1.00 34.20           C  
ANISOU 5846  CE1 TYR C 283     3420   4574   5001    812   -212   -750       C  
ATOM   5847  CE2 TYR C 283       2.494  55.034  49.224  1.00 33.31           C  
ANISOU 5847  CE2 TYR C 283     3312   4593   4751    879   -251   -650       C  
ATOM   5848  CZ  TYR C 283       1.930  55.777  50.239  1.00 33.76           C  
ANISOU 5848  CZ  TYR C 283     3364   4559   4904    858   -231   -657       C  
ATOM   5849  OH  TYR C 283       2.037  57.147  50.215  1.00 35.03           O  
ANISOU 5849  OH  TYR C 283     3518   4672   5120    886   -230   -571       O  
ATOM   5850  N   SER C 284       1.339  49.108  52.541  1.00 38.07           N  
ANISOU 5850  N   SER C 284     4015   5016   5433    607   -224  -1050       N  
ATOM   5851  CA  SER C 284       0.584  47.878  52.681  1.00 42.83           C  
ANISOU 5851  CA  SER C 284     4611   5595   6066    551   -247  -1122       C  
ATOM   5852  C   SER C 284      -0.724  47.990  51.906  1.00 45.57           C  
ANISOU 5852  C   SER C 284     4885   6008   6420    561   -287  -1166       C  
ATOM   5853  O   SER C 284      -1.104  49.060  51.423  1.00 47.65           O  
ANISOU 5853  O   SER C 284     5105   6331   6671    612   -292  -1134       O  
ATOM   5854  CB  SER C 284       0.306  47.578  54.152  1.00 45.78           C  
ANISOU 5854  CB  SER C 284     5000   5902   6495    470   -202  -1114       C  
ATOM   5855  OG  SER C 284      -0.915  48.168  54.565  1.00 47.06           O  
ANISOU 5855  OG  SER C 284     5097   6092   6694    445   -185  -1121       O  
ATOM   5856  N   GLY C 285      -1.423  46.870  51.790  1.00 47.41           N  
ANISOU 5856  N   GLY C 285     5103   6228   6682    509   -322  -1238       N  
ATOM   5857  CA  GLY C 285      -2.688  46.878  51.094  1.00 48.84           C  
ANISOU 5857  CA  GLY C 285     5207   6479   6873    509   -366  -1290       C  
ATOM   5858  C   GLY C 285      -3.841  47.282  51.990  1.00 47.69           C  
ANISOU 5858  C   GLY C 285     4998   6335   6789    454   -333  -1281       C  
ATOM   5859  O   GLY C 285      -3.754  47.273  53.218  1.00 48.75           O  
ANISOU 5859  O   GLY C 285     5151   6412   6958    398   -277  -1251       O  
ATOM   5860  N   ALA C 286      -4.944  47.659  51.351  1.00 41.80           N  
ANISOU 5860  N   ALA C 286     4166   5670   6045    475   -368  -1311       N  
ATOM   5861  CA  ALA C 286      -6.188  47.899  52.066  1.00 41.55           C  
ANISOU 5861  CA  ALA C 286     4053   5661   6071    426   -344  -1322       C  
ATOM   5862  C   ALA C 286      -6.875  46.566  52.330  1.00 43.43           C  
ANISOU 5862  C   ALA C 286     4267   5874   6359    317   -363  -1384       C  
ATOM   5863  O   ALA C 286      -7.021  45.744  51.420  1.00 44.31           O  
ANISOU 5863  O   ALA C 286     4374   5999   6465    308   -430  -1448       O  
ATOM   5864  CB  ALA C 286      -7.100  48.821  51.261  1.00 39.86           C  
ANISOU 5864  CB  ALA C 286     3750   5549   5846    499   -380  -1326       C  
ATOM   5865  N   ARG C 287      -7.282  46.344  53.577  1.00 46.87           N  
ANISOU 5865  N   ARG C 287     4687   6277   6846    233   -306  -1363       N  
ATOM   5866  CA  ARG C 287      -7.960  45.111  53.949  1.00 47.39           C  
ANISOU 5866  CA  ARG C 287     4725   6311   6971    112   -317  -1399       C  
ATOM   5867  C   ARG C 287      -9.171  45.436  54.810  1.00 46.93           C  
ANISOU 5867  C   ARG C 287     4564   6317   6953     53   -268  -1390       C  
ATOM   5868  O   ARG C 287      -9.275  46.519  55.384  1.00 46.49           O  
ANISOU 5868  O   ARG C 287     4481   6305   6879    103   -214  -1356       O  
ATOM   5869  CB  ARG C 287      -7.030  44.151  54.706  1.00 49.41           C  
ANISOU 5869  CB  ARG C 287     5080   6449   7244     47   -293  -1365       C  
ATOM   5870  CG  ARG C 287      -5.794  43.712  53.935  1.00 51.40           C  
ANISOU 5870  CG  ARG C 287     5429   6639   7460    107   -338  -1382       C  
ATOM   5871  CD  ARG C 287      -6.075  42.506  53.050  1.00 53.62           C  
ANISOU 5871  CD  ARG C 287     5709   6886   7777     70   -420  -1469       C  
ATOM   5872  NE  ARG C 287      -4.844  41.922  52.520  1.00 54.37           N  
ANISOU 5872  NE  ARG C 287     5900   6913   7844    124   -454  -1493       N  
ATOM   5873  CZ  ARG C 287      -4.170  42.408  51.481  1.00 54.55           C  
ANISOU 5873  CZ  ARG C 287     5943   6996   7789    235   -483  -1518       C  
ATOM   5874  NH1 ARG C 287      -4.607  43.491  50.852  1.00 53.73           N  
ANISOU 5874  NH1 ARG C 287     5776   7008   7630    302   -487  -1511       N  
ATOM   5875  NH2 ARG C 287      -3.059  41.811  51.071  1.00 54.15           N  
ANISOU 5875  NH2 ARG C 287     5969   6893   7712    282   -508  -1545       N  
ATOM   5876  N   LEU C 288     -10.090  44.481  54.907  1.00 45.12           N  
ANISOU 5876  N   LEU C 288     4271   6093   6781    -56   -288  -1424       N  
ATOM   5877  CA  LEU C 288     -11.235  44.631  55.800  1.00 44.17           C  
ANISOU 5877  CA  LEU C 288     4041   6044   6696   -130   -234  -1410       C  
ATOM   5878  C   LEU C 288     -10.787  44.269  57.212  1.00 47.24           C  
ANISOU 5878  C   LEU C 288     4483   6377   7090   -209   -154  -1336       C  
ATOM   5879  O   LEU C 288     -10.600  43.091  57.532  1.00 50.60           O  
ANISOU 5879  O   LEU C 288     4952   6718   7556   -313   -163  -1314       O  
ATOM   5880  CB  LEU C 288     -12.400  43.763  55.333  1.00 46.02           C  
ANISOU 5880  CB  LEU C 288     4176   6316   6992   -227   -288  -1468       C  
ATOM   5881  CG  LEU C 288     -13.195  44.348  54.160  1.00 45.42           C  
ANISOU 5881  CG  LEU C 288     4005   6350   6904   -149   -355  -1538       C  
ATOM   5882  CD1 LEU C 288     -14.261  43.383  53.668  1.00 45.89           C  
ANISOU 5882  CD1 LEU C 288     3968   6441   7027   -255   -420  -1607       C  
ATOM   5883  CD2 LEU C 288     -13.824  45.674  54.545  1.00 45.10           C  
ANISOU 5883  CD2 LEU C 288     3874   6421   6841    -69   -304  -1519       C  
ATOM   5884  N   GLN C 289     -10.604  45.280  58.054  1.00 46.31           N  
ANISOU 5884  N   GLN C 289     4362   6303   6931   -156    -81  -1299       N  
ATOM   5885  CA  GLN C 289      -9.994  45.122  59.366  1.00 49.10           C  
ANISOU 5885  CA  GLN C 289     4774   6620   7262   -204     -7  -1230       C  
ATOM   5886  C   GLN C 289     -10.946  45.581  60.466  1.00 48.14           C  
ANISOU 5886  C   GLN C 289     4547   6613   7132   -244     74  -1217       C  
ATOM   5887  O   GLN C 289     -12.037  46.108  60.209  1.00 46.50           O  
ANISOU 5887  O   GLN C 289     4220   6507   6940   -222     75  -1264       O  
ATOM   5888  CB  GLN C 289      -8.674  45.893  59.442  1.00 50.06           C  
ANISOU 5888  CB  GLN C 289     5000   6691   7328   -102      5  -1207       C  
ATOM   5889  CG  GLN C 289      -7.706  45.567  58.321  1.00 51.08           C  
ANISOU 5889  CG  GLN C 289     5220   6735   7451    -46    -67  -1222       C  
ATOM   5890  CD  GLN C 289      -6.485  44.817  58.809  1.00 52.35           C  
ANISOU 5890  CD  GLN C 289     5497   6793   7600    -76    -60  -1171       C  
ATOM   5891  OE1 GLN C 289      -6.566  44.018  59.742  1.00 52.49           O  
ANISOU 5891  OE1 GLN C 289     5527   6780   7637   -173    -29  -1125       O  
ATOM   5892  NE2 GLN C 289      -5.343  45.073  58.183  1.00 53.23           N  
ANISOU 5892  NE2 GLN C 289     5690   6858   7679      8    -91  -1172       N  
ATOM   5893  N   CYS C 290     -10.496  45.387  61.704  1.00 54.51           N  
ANISOU 5893  N   CYS C 290     5396   7412   7905   -296    142  -1154       N  
ATOM   5894  CA  CYS C 290     -11.299  45.673  62.881  1.00 55.63           C  
ANISOU 5894  CA  CYS C 290     5442   7675   8021   -344    229  -1136       C  
ATOM   5895  C   CYS C 290     -11.409  47.168  63.136  1.00 53.63           C  
ANISOU 5895  C   CYS C 290     5147   7505   7725   -219    268  -1189       C  
ATOM   5896  O   CYS C 290     -10.495  47.950  62.847  1.00 53.28           O  
ANISOU 5896  O   CYS C 290     5184   7401   7659   -115    248  -1205       O  
ATOM   5897  CB  CYS C 290     -10.697  45.006  64.115  1.00 57.25           C  
ANISOU 5897  CB  CYS C 290     5711   7856   8187   -431    285  -1046       C  
ATOM   5898  SG  CYS C 290     -10.983  43.247  64.209  1.00 60.23           S  
ANISOU 5898  SG  CYS C 290     6096   8157   8630   -607    261   -966       S  
ATOM   5899  N   GLU C 291     -12.542  47.552  63.713  1.00 59.24           N  
ANISOU 5899  N   GLU C 291     5726   8353   8430   -234    324  -1217       N  
ATOM   5900  CA  GLU C 291     -12.778  48.898  64.199  1.00 59.42           C  
ANISOU 5900  CA  GLU C 291     5695   8463   8419   -123    372  -1276       C  
ATOM   5901  C   GLU C 291     -12.883  48.898  65.718  1.00 59.59           C  
ANISOU 5901  C   GLU C 291     5685   8586   8371   -175    470  -1252       C  
ATOM   5902  O   GLU C 291     -13.219  47.894  66.350  1.00 61.69           O  
ANISOU 5902  O   GLU C 291     5920   8897   8621   -306    509  -1185       O  
ATOM   5903  CB  GLU C 291     -14.045  49.500  63.579  1.00 59.44           C  
ANISOU 5903  CB  GLU C 291     5556   8563   8465    -64    354  -1347       C  
ATOM   5904  CG  GLU C 291     -13.801  50.163  62.236  1.00 62.59           C  
ANISOU 5904  CG  GLU C 291     5989   8889   8905     54    267  -1384       C  
ATOM   5905  CD  GLU C 291     -14.905  51.133  61.843  1.00 66.89           C  
ANISOU 5905  CD  GLU C 291     6401   9532   9480    154    257  -1455       C  
ATOM   5906  OE1 GLU C 291     -15.745  51.465  62.705  1.00 68.33           O  
ANISOU 5906  OE1 GLU C 291     6471   9840   9651    153    325  -1490       O  
ATOM   5907  OE2 GLU C 291     -14.931  51.563  60.669  1.00 67.79           O  
ANISOU 5907  OE2 GLU C 291     6519   9609   9628    239    180  -1473       O  
ATOM   5908  N   VAL C 292     -12.581  50.058  66.289  1.00 40.79           N  
ANISOU 5908  N   VAL C 292     3311   6239   5947    -69    507  -1306       N  
ATOM   5909  CA  VAL C 292     -12.549  50.285  67.722  1.00 38.47           C  
ANISOU 5909  CA  VAL C 292     2995   6054   5568    -87    597  -1307       C  
ATOM   5910  C   VAL C 292     -13.333  51.557  67.981  1.00 39.91           C  
ANISOU 5910  C   VAL C 292     3069   6348   5748     29    633  -1419       C  
ATOM   5911  O   VAL C 292     -13.030  52.605  67.394  1.00 41.72           O  
ANISOU 5911  O   VAL C 292     3330   6502   6019    157    588  -1484       O  
ATOM   5912  CB  VAL C 292     -11.112  50.427  68.253  1.00 39.32           C  
ANISOU 5912  CB  VAL C 292     3245   6073   5621    -67    597  -1278       C  
ATOM   5913  CG1 VAL C 292     -11.115  51.026  69.654  1.00 38.36           C  
ANISOU 5913  CG1 VAL C 292     3090   6081   5405    -45    680  -1318       C  
ATOM   5914  CG2 VAL C 292     -10.397  49.093  68.230  1.00 40.67           C  
ANISOU 5914  CG2 VAL C 292     3511   6155   5788   -182    573  -1164       C  
ATOM   5915  N   LYS C 293     -14.344  51.467  68.838  1.00 51.01           N  
ANISOU 5915  N   LYS C 293     4341   7931   7109    -13    713  -1438       N  
ATOM   5916  CA  LYS C 293     -15.054  52.650  69.291  1.00 51.89           C  
ANISOU 5916  CA  LYS C 293     4345   8166   7207    105    758  -1556       C  
ATOM   5917  C   LYS C 293     -14.367  53.199  70.531  1.00 51.17           C  
ANISOU 5917  C   LYS C 293     4302   8121   7018    142    819  -1595       C  
ATOM   5918  O   LYS C 293     -13.857  52.442  71.363  1.00 51.47           O  
ANISOU 5918  O   LYS C 293     4389   8194   6973     40    861  -1516       O  
ATOM   5919  CB  LYS C 293     -16.522  52.349  69.595  1.00 55.38           C  
ANISOU 5919  CB  LYS C 293     4600   8802   7641     54    818  -1573       C  
ATOM   5920  CG  LYS C 293     -17.348  53.616  69.794  1.00 57.40           C  
ANISOU 5920  CG  LYS C 293     4732   9172   7905    203    848  -1711       C  
ATOM   5921  CD  LYS C 293     -18.657  53.360  70.517  1.00 60.46           C  
ANISOU 5921  CD  LYS C 293     4927   9799   8245    152    938  -1732       C  
ATOM   5922  CE  LYS C 293     -19.516  54.618  70.534  1.00 61.60           C  
ANISOU 5922  CE  LYS C 293     4943  10046   8418    320    953  -1881       C  
ATOM   5923  NZ  LYS C 293     -19.746  55.151  69.159  1.00 61.17           N  
ANISOU 5923  NZ  LYS C 293     4889   9866   8486    423    850  -1913       N  
ATOM   5924  N   ILE C 294     -14.346  54.521  70.637  1.00 48.25           N  
ANISOU 5924  N   ILE C 294     3921   7748   6665    290    815  -1718       N  
ATOM   5925  CA  ILE C 294     -13.712  55.222  71.744  1.00 46.80           C  
ANISOU 5925  CA  ILE C 294     3779   7603   6401    345    860  -1789       C  
ATOM   5926  C   ILE C 294     -14.813  55.653  72.702  1.00 46.84           C  
ANISOU 5926  C   ILE C 294     3624   7832   6339    385    951  -1889       C  
ATOM   5927  O   ILE C 294     -15.657  56.487  72.357  1.00 47.63           O  
ANISOU 5927  O   ILE C 294     3625   7969   6504    499    944  -1994       O  
ATOM   5928  CB  ILE C 294     -12.892  56.419  71.247  1.00 45.98           C  
ANISOU 5928  CB  ILE C 294     3773   7329   6369    479    790  -1867       C  
ATOM   5929  CG1 ILE C 294     -11.844  55.943  70.243  1.00 44.91           C  
ANISOU 5929  CG1 ILE C 294     3779   6998   6289    437    707  -1761       C  
ATOM   5930  CG2 ILE C 294     -12.235  57.137  72.412  1.00 46.02           C  
ANISOU 5930  CG2 ILE C 294     3818   7372   6296    529    829  -1957       C  
ATOM   5931  CD1 ILE C 294     -11.575  56.926  69.146  1.00 44.76           C  
ANISOU 5931  CD1 ILE C 294     3804   6822   6382    554    625  -1800       C  
ATOM   5932  N   ASP C 295     -14.817  55.073  73.904  1.00 53.49           N  
ANISOU 5932  N   ASP C 295     4437   8837   7051    296   1036  -1854       N  
ATOM   5933  CA  ASP C 295     -15.840  55.348  74.901  1.00 54.72           C  
ANISOU 5933  CA  ASP C 295     4432   9242   7118    319   1135  -1937       C  
ATOM   5934  C   ASP C 295     -15.438  56.424  75.900  1.00 54.99           C  
ANISOU 5934  C   ASP C 295     4478   9343   7073    436   1170  -2087       C  
ATOM   5935  O   ASP C 295     -16.319  57.014  76.534  1.00 56.48           O  
ANISOU 5935  O   ASP C 295     4529   9719   7214    513   1238  -2210       O  
ATOM   5936  CB  ASP C 295     -16.190  54.064  75.661  1.00 58.12           C  
ANISOU 5936  CB  ASP C 295     4804   9841   7439    146   1216  -1801       C  
ATOM   5937  CG  ASP C 295     -16.508  52.910  74.732  1.00 60.54           C  
ANISOU 5937  CG  ASP C 295     5109  10063   7830     14   1174  -1656       C  
ATOM   5938  OD1 ASP C 295     -17.484  53.019  73.959  1.00 61.99           O  
ANISOU 5938  OD1 ASP C 295     5185  10265   8104     38   1154  -1689       O  
ATOM   5939  OD2 ASP C 295     -15.775  51.898  74.766  1.00 60.17           O  
ANISOU 5939  OD2 ASP C 295     5168   9929   7765   -110   1155  -1515       O  
ATOM   5940  N   ARG C 296     -14.143  56.702  76.053  1.00 57.77           N  
ANISOU 5940  N   ARG C 296     4984   9554   7412    454   1124  -2089       N  
ATOM   5941  CA  ARG C 296     -13.698  57.756  76.955  1.00 58.13           C  
ANISOU 5941  CA  ARG C 296     5048   9644   7395    563   1143  -2246       C  
ATOM   5942  C   ARG C 296     -12.309  58.222  76.544  1.00 57.40           C  
ANISOU 5942  C   ARG C 296     5128   9315   7366    598   1052  -2248       C  
ATOM   5943  O   ARG C 296     -11.445  57.401  76.223  1.00 58.23           O  
ANISOU 5943  O   ARG C 296     5344   9312   7469    497   1014  -2106       O  
ATOM   5944  CB  ARG C 296     -13.680  57.280  78.412  1.00 58.98           C  
ANISOU 5944  CB  ARG C 296     5111   9991   7306    492   1240  -2236       C  
ATOM   5945  CG  ARG C 296     -13.101  58.300  79.382  1.00 59.86           C  
ANISOU 5945  CG  ARG C 296     5251  10154   7338    597   1251  -2406       C  
ATOM   5946  CD  ARG C 296     -13.374  57.918  80.823  1.00 60.97           C  
ANISOU 5946  CD  ARG C 296     5309  10590   7269    547   1359  -2416       C  
ATOM   5947  NE  ARG C 296     -14.801  57.897  81.121  1.00 62.19           N  
ANISOU 5947  NE  ARG C 296     5285  10963   7380    562   1442  -2454       N  
ATOM   5948  CZ  ARG C 296     -15.323  58.244  82.292  1.00 62.41           C  
ANISOU 5948  CZ  ARG C 296     5256  11191   7264    591   1492  -2521       C  
ATOM   5949  NH1 ARG C 296     -14.534  58.646  83.280  1.00 60.55           N  
ANISOU 5949  NH1 ARG C 296     5089  11008   6908    621   1491  -2596       N  
ATOM   5950  NH2 ARG C 296     -16.635  58.193  82.476  1.00 65.37           N  
ANISOU 5950  NH2 ARG C 296     5501  11721   7617    593   1541  -2517       N  
ATOM   5951  N   ILE C 297     -12.099  59.537  76.562  1.00 51.73           N  
ANISOU 5951  N   ILE C 297     4427   8516   6711    740   1016  -2412       N  
ATOM   5952  CA  ILE C 297     -10.783  60.127  76.345  1.00 51.08           C  
ANISOU 5952  CA  ILE C 297     4494   8231   6685    773    936  -2433       C  
ATOM   5953  C   ILE C 297     -10.298  60.698  77.670  1.00 51.53           C  
ANISOU 5953  C   ILE C 297     4559   8396   6625    811    972  -2569       C  
ATOM   5954  O   ILE C 297     -11.053  61.371  78.378  1.00 51.88           O  
ANISOU 5954  O   ILE C 297     4498   8587   6626    903   1024  -2730       O  
ATOM   5955  CB  ILE C 297     -10.811  61.206  75.249  1.00 49.60           C  
ANISOU 5955  CB  ILE C 297     4333   7832   6681    895    852  -2500       C  
ATOM   5956  CG1 ILE C 297     -11.170  60.580  73.900  1.00 49.02           C  
ANISOU 5956  CG1 ILE C 297     4261   7661   6704    852    808  -2357       C  
ATOM   5957  CG2 ILE C 297      -9.465  61.917  75.163  1.00 48.75           C  
ANISOU 5957  CG2 ILE C 297     4364   7531   6628    924    778  -2532       C  
ATOM   5958  CD1 ILE C 297     -10.908  61.483  72.714  1.00 47.87           C  
ANISOU 5958  CD1 ILE C 297     4172   7291   6724    948    713  -2370       C  
ATOM   5959  N   THR C 298      -9.046  60.414  78.013  1.00 52.04           N  
ANISOU 5959  N   THR C 298     4742   8400   6632    746    942  -2513       N  
ATOM   5960  CA  THR C 298      -8.443  60.872  79.258  1.00 54.16           C  
ANISOU 5960  CA  THR C 298     5029   8773   6778    770    964  -2633       C  
ATOM   5961  C   THR C 298      -7.096  61.486  78.908  1.00 53.79           C  
ANISOU 5961  C   THR C 298     5119   8502   6818    789    869  -2654       C  
ATOM   5962  O   THR C 298      -6.231  60.800  78.354  1.00 55.08           O  
ANISOU 5962  O   THR C 298     5379   8546   7003    703    824  -2499       O  
ATOM   5963  CB  THR C 298      -8.307  59.703  80.246  1.00 56.41           C  
ANISOU 5963  CB  THR C 298     5299   9270   6866    647   1036  -2518       C  
ATOM   5964  OG1 THR C 298      -9.560  59.484  80.908  1.00 58.17           O  
ANISOU 5964  OG1 THR C 298     5373   9745   6985    651   1136  -2557       O  
ATOM   5965  CG2 THR C 298      -7.249  59.967  81.283  1.00 56.65           C  
ANISOU 5965  CG2 THR C 298     5395   9355   6775    644   1025  -2586       C  
ATOM   5966  N   HIS C 299      -6.924  62.779  79.191  1.00 47.22           N  
ANISOU 5966  N   HIS C 299     4291   7606   6046    902    835  -2848       N  
ATOM   5967  CA  HIS C 299      -5.761  63.470  78.646  1.00 46.39           C  
ANISOU 5967  CA  HIS C 299     4303   7258   6065    920    737  -2862       C  
ATOM   5968  C   HIS C 299      -5.264  64.563  79.582  1.00 47.16           C  
ANISOU 5968  C   HIS C 299     4413   7361   6143    994    714  -3075       C  
ATOM   5969  O   HIS C 299      -6.037  65.166  80.328  1.00 49.89           O  
ANISOU 5969  O   HIS C 299     4684   7828   6444   1069    745  -3222       O  
ATOM   5970  CB  HIS C 299      -6.070  64.073  77.268  1.00 47.09           C  
ANISOU 5970  CB  HIS C 299     4406   7124   6362    986    673  -2837       C  
ATOM   5971  CG  HIS C 299      -6.937  65.294  77.316  1.00 44.36           C  
ANISOU 5971  CG  HIS C 299     3985   6754   6115   1133    669  -3027       C  
ATOM   5972  ND1 HIS C 299      -6.423  66.567  77.443  1.00 46.38           N  
ANISOU 5972  ND1 HIS C 299     4303   6845   6473   1200    590  -3141       N  
ATOM   5973  CD2 HIS C 299      -8.281  65.438  77.235  1.00 46.27           C  
ANISOU 5973  CD2 HIS C 299     4127   7085   6369   1192    701  -3049       C  
ATOM   5974  CE1 HIS C 299      -7.413  67.441  77.447  1.00 48.16           C  
ANISOU 5974  CE1 HIS C 299     4478   7055   6767   1295    573  -321