CNRS Nantes University UFIP UFIP
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***  2HAD  ***

elNémo ID: 21080315133538722

Job options:

ID        	=	 21080315133538722
JOBID     	=	 2HAD
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 2HAD

REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.18.2_3874: ???)                            
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) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.00                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.56                          
REMARK   3   NUMBER OF REFLECTIONS             : 35189                          
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 35189                      
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2254                          
REMARK   3   R VALUE            (WORKING SET) : 0.2233                          
REMARK   3   FREE R VALUE                     : 0.2652                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.95                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1741                            
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   21.51 -    4.96    0.99     3529   186  0.1937 0.2233   0.92 
REMARK   3     2    4.96 -    3.95    0.98     3443   182  0.1685 0.2123   0.93 
REMARK   3     3    3.95 -    3.45    0.82     2888   151  0.2055 0.2546   0.89 
REMARK   3     4    3.45 -    3.14    0.97     3403   174  0.2408 0.2811   0.87 
REMARK   3     5    3.14 -    2.91    0.96     3345   169  0.2531 0.2948   0.85 
REMARK   3     6    2.91 -    2.74    0.93     3252   174  0.2483 0.3047   0.86 
REMARK   3     7    2.74 -    2.60    0.89     3135   156  0.2667 0.3323   0.84 
REMARK   3     8    2.60 -    2.49    0.85     2975   150  0.2698 0.2764   0.84 
REMARK   3     9    2.49 -    2.39    0.82     2835   148  0.2750 0.3198   0.81 
REMARK   3    10    2.39 -    2.31    0.75     2659   134  0.3009 0.3478   0.77 
REMARK   3    11    2.31 -    2.24    0.33     1139    66  0.4842 0.5391   0.50 
REMARK   3    12    2.24 -    2.18    0.25      845    51  0.4130 0.4467   0.53 
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)     : 0.33             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.44            
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      :  0.007   0.146   5238                                 
REMARK   3    ANGLE     :  0.995  19.358   7135                                 
REMARK   3    CHIRALITY :  0.043   0.183    787                                 
REMARK   3    PLANARITY :  0.008   0.094    937                                 
REMARK   3    DIHEDRAL  :  5.401  26.644    750                                 
REMARK   3    MIN NONBONDED DISTANCE : 1.376                                    
REMARK   3                                                                      
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3    ALL-ATOM CLASHSCORE : 4.74                                        
REMARK   3    RAMACHANDRAN PLOT:                                                
REMARK   3      OUTLIERS :  0.00 %                                              
REMARK   3      ALLOWED  :  2.07 %                                              
REMARK   3      FAVORED  : 97.93 %                                              
REMARK   3    ROTAMER OUTLIERS :  0.00 %                                        
REMARK   3    CBETA DEVIATIONS :  0.00 %                                        
REMARK   3    PEPTIDE PLANE:                                                    
REMARK   3      CIS-PROLINE     : 6.67 %                                        
REMARK   3      CIS-GENERAL     : 0.00 %                                        
REMARK   3      TWISTED PROLINE : 0.00 %                                        
REMARK   3      TWISTED GENERAL : 0.00 %                                        
REMARK   3                                                                      
REMARK   3  RAMA-Z (RAMACHANDRAN PLOT Z-SCORE):                                 
REMARK   3  INTERPRETATION: BAD |RAMA-Z| > 3; SUSPICIOUS 2 < |RAMA-Z| < 3; GOOD 
REMARK   3  SCORES FOR WHOLE/HELIX/SHEET/LOOP ARE SCALED INDEPENDENTLY;         
REMARK   3  THEREFORE, THE VALUES ARE NOT RELATED IN A SIMPLE MANNER.           
REMARK   3    WHOLE: -1.38 (0.29), RESIDUES: 675                                
REMARK   3    HELIX: -1.22 (0.22), RESIDUES: 372                                
REMARK   3    SHEET:  0.29 (0.57), RESIDUES: 90                                 
REMARK   3    LOOP : -0.46 (0.39), RESIDUES: 213                                
REMARK   3                                                                      
REMARK   3                  min    max   mean    iso aniso                
REMARK   3     Overall:   26.95 135.28  58.49   6.78  5293  5110                
REMARK   3     Protein:   26.95 135.28  58.67   6.78  5110  5110                
REMARK   3     Water:     32.97  76.91  53.35    N/A   183     0                
REMARK   3     Chain  A:  26.95 135.28  56.31    N/A  1705  1705                
REMARK   3     Chain  C:  30.90 111.64  60.77    N/A  1707  1707                
REMARK   3     Chain  B:  28.63 116.35  58.93    N/A  1698  1698                
REMARK   3     Chain  S:  32.97  76.91  53.35    N/A   183     0                
REMARK   3     Histogram:                                                       
REMARK   3         Values      Number of atoms                                  
REMARK   3      26.95 - 37.78       232                                         
REMARK   3      37.78 - 48.61      1164                                         
REMARK   3      48.61 - 59.45      1605                                         
REMARK   3      59.45 - 70.28      1279                                         
REMARK   3      70.28 - 81.12       674                                         
REMARK   3      81.12 - 91.95       225                                         
REMARK   3      91.95 - 102.78       96                                         
REMARK   3     102.78 - 113.62       16                                         
REMARK   3     113.62 - 124.45        1                                         
REMARK   3     124.45 - 135.28        1                                         
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 19                                           
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'C' and (resid 86 through 99 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  47.9987 -11.9454   3.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6160 T22:   0.2276                                     
REMARK   3      T33:   0.5470 T12:   0.0162                                     
REMARK   3      T13:  -0.0119 T23:  -0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1952 L22:   3.3858                                     
REMARK   3      L33:   4.4570 L12:   0.2643                                     
REMARK   3      L13:   1.4188 L23:   0.6471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3984 S12:   0.8977 S13:  -0.2031                       
REMARK   3      S21:  -1.0309 S22:   0.0165 S23:   0.4735                       
REMARK   3      S31:   0.2396 S32:   0.2156 S33:   0.2593                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'C' and (resid 100 through 189 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  68.5509  -8.9344  20.8787              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4089 T22:   0.4389                                     
REMARK   3      T33:   1.1674 T12:  -0.1508                                     
REMARK   3      T13:  -0.0603 T23:   0.1025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8970 L22:   4.0880                                     
REMARK   3      L33:   4.0827 L12:   0.1703                                     
REMARK   3      L13:   0.6286 L23:   0.3577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0976 S12:   0.0237 S13:   0.2953                       
REMARK   3      S21:   0.1016 S22:  -0.3787 S23:  -1.0301                       
REMARK   3      S31:  -0.4102 S32:   0.5426 S33:   0.3196                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'C' and (resid 190 through 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  61.6124 -12.0366  33.5739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5868 T22:   0.4493                                     
REMARK   3      T33:   0.9654 T12:  -0.1458                                     
REMARK   3      T13:  -0.2933 T23:  -0.0704                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7775 L22:   2.2335                                     
REMARK   3      L33:   1.7654 L12:   0.8833                                     
REMARK   3      L13:  -0.9685 L23:  -0.2997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1419 S12:  -0.4719 S13:   0.5187                       
REMARK   3      S21:   0.7167 S22:  -0.1522 S23:  -0.3087                       
REMARK   3      S31:  -0.5485 S32:   0.2162 S33:   0.2409                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 10 through 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2240  18.0456  17.3778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3603 T22:   0.3248                                     
REMARK   3      T33:   0.5818 T12:   0.0851                                     
REMARK   3      T13:  -0.1510 T23:  -0.0356                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4991 L22:   8.5709                                     
REMARK   3      L33:   2.2165 L12:   2.1622                                     
REMARK   3      L13:  -1.5329 L23:  -1.5402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2853 S12:   0.0065 S13:  -0.1721                       
REMARK   3      S21:   0.5660 S22:  -0.3026 S23:  -0.2455                       
REMARK   3      S31:   0.1873 S32:   0.2905 S33:   0.2249                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 39 through 60 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5307  26.8080  16.6546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3891 T22:   0.2861                                     
REMARK   3      T33:   0.4002 T12:   0.1154                                     
REMARK   3      T13:  -0.0281 T23:   0.0362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6911 L22:   7.5989                                     
REMARK   3      L33:   2.1876 L12:   2.5087                                     
REMARK   3      L13:  -2.2830 L23:  -0.0813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0634 S12:  -0.5391 S13:   0.0954                       
REMARK   3      S21:   0.2801 S22:  -0.1113 S23:   0.3169                       
REMARK   3      S31:  -0.0108 S32:   0.0650 S33:  -0.1667                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 61 through 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2432  24.4352   7.9716              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4708 T22:   0.2831                                     
REMARK   3      T33:   0.4179 T12:   0.0575                                     
REMARK   3      T13:  -0.1782 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0262 L22:   9.3327                                     
REMARK   3      L33:   3.1002 L12:   1.8548                                     
REMARK   3      L13:  -1.6936 L23:  -0.4771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1291 S12:   0.5079 S13:  -0.2073                       
REMARK   3      S21:  -0.9890 S22:   0.0876 S23:   0.5841                       
REMARK   3      S31:   0.2940 S32:  -0.3798 S33:  -0.0540                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 103 through 133 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.1198   3.5183  23.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7196 T22:   0.3440                                     
REMARK   3      T33:   0.9111 T12:   0.0549                                     
REMARK   3      T13:  -0.1549 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2225 L22:   4.9770                                     
REMARK   3      L33:   2.9894 L12:  -1.3073                                     
REMARK   3      L13:   0.7534 L23:  -1.3007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2666 S12:   0.2167 S13:  -0.0829                       
REMARK   3      S21:   0.5637 S22:  -0.3258 S23:  -0.6041                       
REMARK   3      S31:   0.6530 S32:   0.4671 S33:   0.2466                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 134 through 165 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9144   7.7010  15.1521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4761 T22:   0.2182                                     
REMARK   3      T33:   0.7417 T12:   0.0006                                     
REMARK   3      T13:  -0.1728 T23:  -0.0680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0535 L22:   6.5152                                     
REMARK   3      L33:   2.2768 L12:   0.0382                                     
REMARK   3      L13:  -0.8937 L23:  -1.6471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0725 S12:   0.3790 S13:  -0.1576                       
REMARK   3      S21:  -0.1331 S22:  -0.1784 S23:  -0.1189                       
REMARK   3      S31:   0.3201 S32:  -0.0356 S33:   0.1713                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'A' and (resid 166 through 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7712  11.9689  31.6688              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0468 T22:   0.0941                                     
REMARK   3      T33:   0.6751 T12:   0.0475                                     
REMARK   3      T13:  -0.0465 T23:   0.0762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5108 L22:   4.4136                                     
REMARK   3      L33:   4.6484 L12:  -0.8097                                     
REMARK   3      L13:  -0.6091 L23:   0.7298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1103 S12:  -0.1672 S13:  -0.2189                       
REMARK   3      S21:   1.3441 S22:   0.0339 S23:  -0.2950                       
REMARK   3      S31:   0.3811 S32:   0.1080 S33:   0.0714                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid 10 through 23 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  65.2535  25.1959  23.3796              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4131 T22:   0.5996                                     
REMARK   3      T33:   0.7605 T12:   0.1002                                     
REMARK   3      T13:  -0.0857 T23:   0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0374 L22:   5.8001                                     
REMARK   3      L33:   4.7572 L12:  -5.6743                                     
REMARK   3      L13:  -4.0384 L23:   4.8583                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0882 S12:  -2.2144 S13:   0.9801                       
REMARK   3      S21:   0.9899 S22:   1.5022 S23:  -1.1593                       
REMARK   3      S31:   0.6142 S32:   0.7888 S33:   0.0308                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resid 24 through 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3507   5.5027  11.6265              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5504 T22:   0.4315                                     
REMARK   3      T33:   1.1712 T12:  -0.0547                                     
REMARK   3      T13:  -0.0794 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3401 L22:   5.7708                                     
REMARK   3      L33:   2.5739 L12:  -1.0471                                     
REMARK   3      L13:  -0.0593 L23:   1.4856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4712 S12:   0.3434 S13:  -1.4353                       
REMARK   3      S21:   0.7717 S22:  -0.0998 S23:   1.8137                       
REMARK   3      S31:   0.7428 S32:  -0.3632 S33:   0.1348                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resid 39 through 60 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  82.7784  19.4171  16.4400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2159 T22:   0.4090                                     
REMARK   3      T33:   0.4310 T12:  -0.0533                                     
REMARK   3      T13:   0.0493 T23:   0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9765 L22:   3.2000                                     
REMARK   3      L33:   4.1870 L12:   0.3549                                     
REMARK   3      L13:   1.0529 L23:   3.2940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1652 S12:   0.0847 S13:  -0.1318                       
REMARK   3      S21:   1.0386 S22:   0.2938 S23:   0.5535                       
REMARK   3      S31:   0.4084 S32:   0.0791 S33:  -0.0140                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'B' and (resid 61 through 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  80.7817  19.2915   7.7469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2219 T22:   0.4855                                     
REMARK   3      T33:   0.3774 T12:  -0.0826                                     
REMARK   3      T13:   0.0081 T23:   0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3323 L22:   8.0118                                     
REMARK   3      L33:   3.3541 L12:  -3.4273                                     
REMARK   3      L13:   0.2129 L23:   1.3923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1362 S12:   0.7825 S13:  -0.0182                       
REMARK   3      S21:  -0.6177 S22:   0.1234 S23:  -0.0334                       
REMARK   3      S31:  -0.3321 S32:   0.1543 S33:   0.0362                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'B' and (resid 103 through 133 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  58.8732  24.1174  22.6458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3514 T22:   0.8811                                     
REMARK   3      T33:   0.6598 T12:   0.2055                                     
REMARK   3      T13:  -0.0107 T23:   0.0476                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9694 L22:   1.8762                                     
REMARK   3      L33:   2.9472 L12:   2.9692                                     
REMARK   3      L13:  -1.4854 L23:  -1.4080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3491 S12:  -0.6586 S13:  -0.4858                       
REMARK   3      S21:   0.0051 S22:   0.1367 S23:   0.3450                       
REMARK   3      S31:  -0.2345 S32:  -0.9564 S33:   0.3054                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'B' and (resid 134 through 155 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  62.0597  26.8294  13.7163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2936 T22:   0.5939                                     
REMARK   3      T33:   0.6387 T12:   0.1100                                     
REMARK   3      T13:  -0.0433 T23:   0.0442                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7844 L22:   5.6542                                     
REMARK   3      L33:   3.5431 L12:  -1.7027                                     
REMARK   3      L13:  -2.1561 L23:   2.0694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1126 S12:   0.9463 S13:  -0.3337                       
REMARK   3      S21:  -0.2346 S22:  -0.2190 S23:   0.0894                       
REMARK   3      S31:  -0.2434 S32:  -0.7038 S33:   0.0548                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'B' and (resid 156 through 176 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  73.8383  35.4613  20.0977              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3920 T22:   0.3923                                     
REMARK   3      T33:   0.5855 T12:   0.1014                                     
REMARK   3      T13:  -0.1539 T23:  -0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8579 L22:   3.5523                                     
REMARK   3      L33:   1.8290 L12:  -2.4184                                     
REMARK   3      L13:  -0.5030 L23:  -0.0806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5549 S12:  -0.5321 S13:   0.8263                       
REMARK   3      S21:   0.2538 S22:   0.1041 S23:   0.2632                       
REMARK   3      S31:  -1.0821 S32:  -0.3129 S33:   0.3068                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'B' and (resid 177 through 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  70.0606  25.3985  32.5754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3158 T22:   0.9214                                     
REMARK   3      T33:   0.6199 T12:   0.1482                                     
REMARK   3      T13:   0.0260 T23:   0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3131 L22:   1.3246                                     
REMARK   3      L33:   2.5429 L12:   0.4270                                     
REMARK   3      L13:   1.3484 L23:  -0.3273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3056 S12:  -1.2139 S13:   0.0299                       
REMARK   3      S21:   0.1088 S22:   0.1986 S23:   0.0677                       
REMARK   3      S31:   0.0290 S32:  -0.5193 S33:   0.0409                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain 'C' and (resid 10 through 60 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9880 -13.2015  17.3171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3647 T22:   0.2155                                     
REMARK   3      T33:   0.4093 T12:   0.0122                                     
REMARK   3      T13:   0.0864 T23:  -0.0614                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3673 L22:   4.1880                                     
REMARK   3      L33:   4.5148 L12:   1.0187                                     
REMARK   3      L13:   2.8450 L23:  -1.9129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1575 S12:  -0.8797 S13:   0.3400                       
REMARK   3      S21:   0.0598 S22:  -0.1637 S23:  -0.4459                       
REMARK   3      S31:   0.0035 S32:  -0.4087 S33:   0.2941                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: chain 'C' and (resid 61 through 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  54.5865 -21.9500   9.8154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5990 T22:   0.2164                                     
REMARK   3      T33:   0.7926 T12:  -0.0459                                     
REMARK   3      T13:   0.1102 T23:  -0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3652 L22:   7.3134                                     
REMARK   3      L33:   5.7662 L12:  -4.1964                                     
REMARK   3      L13:   0.1646 L23:  -2.0078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5560 S12:   0.4245 S13:  -1.4772                       
REMARK   3      S21:  -1.2421 S22:  -0.4208 S23:  -1.0370                       
REMARK   3      S31:   0.9061 S32:   0.3914 S33:  -0.0658                       
REMARK   3                                                                      
CRYST1  181.539  105.501   45.759  90.00 101.52  90.00 C 1 2 1                  
SCALE1      0.005508  0.000000  0.001123        0.00000                         
SCALE2      0.000000  0.009479  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022303        0.00000                         
ATOM      1  N   PRO A  10      33.269  -2.350  34.174  1.00101.28           N  
ANISOU    1  N   PRO A  10    18296   7406  12781   -934    834    548       N  
ATOM      2  CA  PRO A  10      32.028  -1.591  33.964  1.00 95.54           C  
ANISOU    2  CA  PRO A  10    17304   6749  12250  -1023   1312    283       C  
ATOM      3  C   PRO A  10      31.235  -2.081  32.756  1.00 88.42           C  
ANISOU    3  C   PRO A  10    15781   5900  11916   -883   1445     96       C  
ATOM      4  O   PRO A  10      31.771  -2.826  31.933  1.00 70.42           O  
ANISOU    4  O   PRO A  10    13275   3631   9851   -707   1164    125       O  
ATOM      5  CB  PRO A  10      32.522  -0.151  33.743  1.00 86.27           C  
ANISOU    5  CB  PRO A  10    16079   5750  10950  -1039   1151    238       C  
ATOM      6  CG  PRO A  10      33.929  -0.122  34.295  1.00 97.68           C  
ANISOU    6  CG  PRO A  10    17958   7183  11973  -1059    631    501       C  
ATOM      7  CD  PRO A  10      34.470  -1.503  34.064  1.00 96.41           C  
ANISOU    7  CD  PRO A  10    17750   6922  11959   -892    355    680       C  
ATOM      8  HA  PRO A  10      31.468  -1.624  34.755  1.00114.97           H  
ATOM      9  HB2 PRO A  10      32.517   0.056  32.795  1.00103.85           H  
ATOM     10  HB3 PRO A  10      31.950   0.469  34.221  1.00103.85           H  
ATOM     11  HG2 PRO A  10      34.456   0.540  33.820  1.00117.53           H  
ATOM     12  HG3 PRO A  10      33.908   0.088  35.242  1.00117.53           H  
ATOM     13  HD2 PRO A  10      34.867  -1.577  33.182  1.00116.01           H  
ATOM     14  HD3 PRO A  10      35.123  -1.737  34.742  1.00116.01           H  
ATOM     15  N   ASP A  11      29.968  -1.666  32.657  1.00 88.11           N  
ANISOU   15  N   ASP A  11    15479   5885  12112   -968   1859    -84       N  
ATOM     16  CA  ASP A  11      29.162  -2.029  31.496  1.00 87.64           C  
ANISOU   16  CA  ASP A  11    14843   5890  12564   -882   1909   -244       C  
ATOM     17  C   ASP A  11      29.849  -1.616  30.203  1.00 78.53           C  
ANISOU   17  C   ASP A  11    13319   4920  11598   -709   1522   -305       C  
ATOM     18  O   ASP A  11      29.792  -2.336  29.200  1.00 70.73           O  
ANISOU   18  O   ASP A  11    12029   3955  10889   -608   1372   -380       O  
ATOM     19  CB  ASP A  11      27.777  -1.387  31.594  1.00 75.30           C  
ANISOU   19  CB  ASP A  11    13032   4338  11241   -996   2355   -374       C  
ATOM     20  H   ASP A  11      29.562  -1.181  33.239  1.00106.05           H  
ATOM     21  HA  ASP A  11      29.043  -2.992  31.484  1.00105.48           H  
ATOM     22  N   ALA A  12      30.509  -0.462  30.210  1.00 63.30           N  
ANISOU   22  N   ALA A  12    11444   3114   9492   -687   1374   -285       N  
ATOM     23  CA  ALA A  12      31.264  -0.029  29.044  1.00 60.09           C  
ANISOU   23  CA  ALA A  12    10740   2870   9219   -517   1026   -333       C  
ATOM     24  C   ALA A  12      32.057   1.222  29.388  1.00 64.25           C  
ANISOU   24  C   ALA A  12    11460   3495   9457   -531    882   -271       C  
ATOM     25  O   ALA A  12      31.776   1.911  30.372  1.00 60.93           O  
ANISOU   25  O   ALA A  12    11318   3039   8793   -695   1108   -245       O  
ATOM     26  CB  ALA A  12      30.343   0.235  27.846  1.00 58.46           C  
ANISOU   26  CB  ALA A  12     9981   2788   9441   -487   1093   -521       C  
ATOM     27  H   ALA A  12      30.534   0.084  30.874  1.00 74.37           H  
ATOM     28  HA  ALA A  12      31.898  -0.724  28.807  1.00 70.51           H  
ATOM     29  HB1 ALA A  12      30.879   0.544  27.098  1.00 69.43           H  
ATOM     30  HB2 ALA A  12      29.889  -0.588  27.609  1.00 69.43           H  
ATOM     31  HB3 ALA A  12      29.694   0.913  28.090  1.00 69.43           H  
ATOM     32  N   ILE A  13      33.057   1.499  28.557  1.00 56.73           N  
ANISOU   32  N   ILE A  13    10269   2779   8507   -352    480   -248       N  
ATOM     33  CA  ILE A  13      33.849   2.720  28.625  1.00 55.44           C  
ANISOU   33  CA  ILE A  13    10098   2843   8125   -336    258   -200       C  
ATOM     34  C   ILE A  13      33.701   3.421  27.282  1.00 59.18           C  
ANISOU   34  C   ILE A  13    10010   3586   8889   -203    176   -350       C  
ATOM     35  O   ILE A  13      34.078   2.867  26.241  1.00 58.82           O  
ANISOU   35  O   ILE A  13     9657   3672   9021    -34    -41   -383       O  
ATOM     36  CB  ILE A  13      35.326   2.436  28.937  1.00 56.04           C  
ANISOU   36  CB  ILE A  13    10348   3006   7938   -244   -200     22       C  
ATOM     37  CG1 ILE A  13      35.434   1.439  30.091  1.00 68.90           C  
ANISOU   37  CG1 ILE A  13    12504   4347   9330   -354   -186    208       C  
ATOM     38  CG2 ILE A  13      36.053   3.722  29.297  1.00 57.78           C  
ANISOU   38  CG2 ILE A  13    10663   3400   7891   -311   -399     84       C  
ATOM     39  CD1 ILE A  13      36.850   1.033  30.435  1.00 66.56           C  
ANISOU   39  CD1 ILE A  13    12342   4093   8855   -262   -683    488       C  
ATOM     40  H   ILE A  13      33.303   0.974  27.922  1.00 67.02           H  
ATOM     41  HA  ILE A  13      33.503   3.297  29.324  1.00 64.94           H  
ATOM     42  HB  ILE A  13      35.737   2.056  28.145  1.00 65.66           H  
ATOM     43 HG12 ILE A  13      35.043   1.839  30.883  1.00 83.00           H  
ATOM     44 HG13 ILE A  13      34.948   0.634  29.851  1.00 83.00           H  
ATOM     45 HG21 ILE A  13      37.008   3.551  29.314  1.00 69.66           H  
ATOM     46 HG22 ILE A  13      35.851   4.397  28.630  1.00 69.66           H  
ATOM     47 HG23 ILE A  13      35.755   4.020  30.170  1.00 69.66           H  
ATOM     48 HD11 ILE A  13      36.823   0.313  31.084  1.00 80.19           H  
ATOM     49 HD12 ILE A  13      37.297   0.734  29.628  1.00 80.19           H  
ATOM     50 HD13 ILE A  13      37.316   1.798  30.807  1.00 80.19           H  
ATOM     51  N   LEU A  14      33.001   4.559  27.261  1.00 55.66           N  
ANISOU   51  N   LEU A  14     9466   3192   8490   -287    374   -436       N  
ATOM     52  CA  LEU A  14      32.779   5.354  26.032  1.00 53.96           C  
ANISOU   52  CA  LEU A  14     8752   3210   8541   -184    301   -547       C  
ATOM     53  C   LEU A  14      33.833   6.457  26.029  1.00 49.61           C  
ANISOU   53  C   LEU A  14     8189   2886   7774   -138     77   -497       C  
ATOM     54  O   LEU A  14      34.183   6.879  27.102  1.00 49.14           O  
ANISOU   54  O   LEU A  14     8467   2747   7458   -277    190   -449       O  
ATOM     55  CB  LEU A  14      31.349   5.899  26.019  1.00 50.14           C  
ANISOU   55  CB  LEU A  14     8075   2589   8386   -296    697   -654       C  
ATOM     56  CG  LEU A  14      30.244   4.946  25.571  1.00 55.03           C  
ANISOU   56  CG  LEU A  14     8461   3055   9391   -330    852   -731       C  
ATOM     57  CD1 LEU A  14      28.878   5.549  25.852  1.00 52.93           C  
ANISOU   57  CD1 LEU A  14     8049   2668   9396   -458   1270   -755       C  
ATOM     58  CD2 LEU A  14      30.363   4.605  24.093  1.00 64.36           C  
ANISOU   58  CD2 LEU A  14     9209   4469  10776   -205    519   -796       C  
ATOM     59  H   LEU A  14      32.638   4.937  28.004  1.00 67.11           H  
ATOM     60  HA  LEU A  14      32.918   4.782  25.252  1.00 65.07           H  
ATOM     61  HB2 LEU A  14      31.135   6.215  26.919  1.00 58.57           H  
ATOM     62  HB3 LEU A  14      31.333   6.681  25.432  1.00 58.57           H  
ATOM     63  HG  LEU A  14      30.326   4.108  26.091  1.00 66.35           H  
ATOM     64 HD11 LEU A  14      28.192   4.871  25.730  1.00 61.93           H  
ATOM     65 HD12 LEU A  14      28.845   5.880  26.766  1.00 61.93           H  
ATOM     66 HD13 LEU A  14      28.717   6.287  25.239  1.00 61.93           H  
ATOM     67 HD21 LEU A  14      29.556   4.147  23.801  1.00 77.55           H  
ATOM     68 HD22 LEU A  14      30.474   5.422  23.576  1.00 77.55           H  
ATOM     69 HD23 LEU A  14      31.132   4.026  23.951  1.00 77.55           H  
ATOM     70  N   PHE A  15      34.371   6.816  24.874  1.00 48.61           N  
ANISOU   70  N   PHE A  15     7712   3018   7739     33   -217   -515       N  
ATOM     71  CA  PHE A  15      35.431   7.838  24.743  1.00 50.96           C  
ANISOU   71  CA  PHE A  15     7942   3537   7884     91   -439   -467       C  
ATOM     72  C   PHE A  15      35.029   8.876  23.704  1.00 54.84           C  
ANISOU   72  C   PHE A  15     8049   4192   8594    140   -384   -570       C  
ATOM     73  O   PHE A  15      34.606   8.490  22.610  1.00 42.05           O  
ANISOU   73  O   PHE A  15     6126   2651   7201    227   -446   -642       O  
ATOM     74  CB  PHE A  15      36.771   7.227  24.325  1.00 49.86           C  
ANISOU   74  CB  PHE A  15     7724   3536   7686    260   -804   -370       C  
ATOM     75  CG  PHE A  15      37.442   6.376  25.368  1.00 51.91           C  
ANISOU   75  CG  PHE A  15     8331   3642   7750    226   -943   -200       C  
ATOM     76  CD1 PHE A  15      38.280   6.952  26.303  1.00 60.80           C  
ANISOU   76  CD1 PHE A  15     9627   4825   8650    190  -1213    -33       C  
ATOM     77  CD2 PHE A  15      37.249   5.006  25.408  1.00 51.94           C  
ANISOU   77  CD2 PHE A  15     8492   3433   7812    216   -834   -185       C  
ATOM     78  CE1 PHE A  15      38.896   6.177  27.267  1.00 62.55           C  
ANISOU   78  CE1 PHE A  15    10164   4899   8703    144  -1409    169       C  
ATOM     79  CE2 PHE A  15      37.874   4.231  26.369  1.00 59.75           C  
ANISOU   79  CE2 PHE A  15     9813   4265   8627    189   -985      9       C  
ATOM     80  CZ  PHE A  15      38.698   4.818  27.297  1.00 65.50           C  
ANISOU   80  CZ  PHE A  15    10702   5056   9127    154  -1295    200       C  
ATOM     81  H   PHE A  15      34.136   6.458  24.067  1.00 58.65           H  
ATOM     82  HA  PHE A  15      35.550   8.292  25.612  1.00 61.47           H  
ATOM     83  HB2 PHE A  15      36.623   6.682  23.523  1.00 60.15           H  
ATOM     84  HB3 PHE A  15      37.376   7.957  24.077  1.00 60.15           H  
ATOM     85  HD1 PHE A  15      38.419   7.885  26.293  1.00 73.28           H  
ATOM     86  HD2 PHE A  15      36.684   4.597  24.773  1.00 62.65           H  
ATOM     87  HE1 PHE A  15      39.452   6.585  27.905  1.00 75.38           H  
ATOM     88  HE2 PHE A  15      37.731   3.298  26.388  1.00 72.02           H  
ATOM     89  HZ  PHE A  15      39.121   4.291  27.956  1.00 78.91           H  
ATOM     90  N   ASP A  16      35.149  10.157  24.037  1.00 49.14           N  
ANISOU   90  N   ASP A  16     7376   3501   7793     64   -276   -567       N  
ATOM     91  CA  ASP A  16      34.955  11.241  23.054  1.00 41.01           C  
ANISOU   91  CA  ASP A  16     5998   2665   6920    145   -324   -610       C  
ATOM     92  C   ASP A  16      36.148  11.105  22.121  1.00 47.12           C  
ANISOU   92  C   ASP A  16     6599   3680   7623    309   -679   -578       C  
ATOM     93  O   ASP A  16      37.189  10.681  22.613  1.00 47.53           O  
ANISOU   93  O   ASP A  16     6815   3752   7493    342   -876   -492       O  
ATOM     94  CB  ASP A  16      34.834  12.584  23.768  1.00 42.27           C  
ANISOU   94  CB  ASP A  16     6298   2786   6977     34   -136   -604       C  
ATOM     95  CG  ASP A  16      34.679  13.785  22.853  1.00 64.67           C  
ANISOU   95  CG  ASP A  16     8766   5769  10035    114   -123   -632       C  
ATOM     96  OD2 ASP A  16      34.966  14.906  23.312  1.00 79.82           O  
ANISOU   96  OD2 ASP A  16    10773   7639  11918     35     66   -635       O  
ATOM     97  OD1 ASP A  16      34.237  13.598  21.709  1.00 56.27           O  
ANISOU   97  OD1 ASP A  16     7367   4846   9167    236   -290   -647       O  
ATOM     98  H   ASP A  16      35.389  10.439  24.868  1.00 59.28           H  
ATOM     99  HA  ASP A  16      34.128  11.069  22.551  1.00 49.36           H  
ATOM    100  HB2 ASP A  16      34.052  12.554  24.356  1.00 51.04           H  
ATOM    101  HB3 ASP A  16      35.622  12.719  24.327  1.00 51.04           H  
ATOM    102  N   ALA A  17      36.007  11.402  20.840  1.00 40.36           N  
ANISOU  102  N   ALA A  17     5414   2986   6934    406   -756   -628       N  
ATOM    103  CA  ALA A  17      37.075  11.195  19.850  1.00 40.82           C  
ANISOU  103  CA  ALA A  17     5336   3228   6946    557  -1007   -619       C  
ATOM    104  C   ALA A  17      37.920  12.445  19.620  1.00 45.54           C  
ANISOU  104  C   ALA A  17     5846   3997   7459    599  -1097   -576       C  
ATOM    105  O   ALA A  17      39.090  12.426  20.008  1.00 36.44           O  
ANISOU  105  O   ALA A  17     4783   2887   6174    626  -1239   -496       O  
ATOM    106  CB  ALA A  17      36.453  10.758  18.568  1.00 41.35           C  
ANISOU  106  CB  ALA A  17     5187   3348   7175    607  -1055   -706       C  
ATOM    107  H   ALA A  17      35.266  11.800  20.489  1.00 48.75           H  
ATOM    108  HA  ALA A  17      37.668  10.475  20.169  1.00 49.30           H  
ATOM    109  HB1 ALA A  17      37.141  10.644  17.896  1.00 49.93           H  
ATOM    110  HB2 ALA A  17      35.992   9.916  18.703  1.00 49.93           H  
ATOM    111  HB3 ALA A  17      35.820  11.426  18.263  1.00 49.93           H  
ATOM    112  N   PHE A  18      37.348  13.499  19.050  1.00 42.66           N  
ANISOU  112  N   PHE A  18     5287   3719   7202    599  -1035   -608       N  
ATOM    113  CA  PHE A  18      38.109  14.712  18.676  1.00 41.46           C  
ANISOU  113  CA  PHE A  18     5034   3725   6993    646  -1104   -573       C  
ATOM    114  C   PHE A  18      38.261  15.557  19.935  1.00 45.48           C  
ANISOU  114  C   PHE A  18     5730   4161   7388    520   -991   -536       C  
ATOM    115  O   PHE A  18      37.253  15.993  20.482  1.00 45.90           O  
ANISOU  115  O   PHE A  18     5820   4092   7527    424   -754   -559       O  
ATOM    116  CB  PHE A  18      37.460  15.390  17.472  1.00 38.81           C  
ANISOU  116  CB  PHE A  18     4454   3484   6807    685  -1093   -595       C  
ATOM    117  CG  PHE A  18      37.470  14.569  16.209  1.00 48.67           C  
ANISOU  117  CG  PHE A  18     5608   4809   8076    762  -1237   -640       C  
ATOM    118  CD1 PHE A  18      38.608  14.499  15.426  1.00 38.05           C  
ANISOU  118  CD1 PHE A  18     4251   3585   6620    868  -1342   -645       C  
ATOM    119  CD2 PHE A  18      36.345  13.870  15.800  1.00 41.54           C  
ANISOU  119  CD2 PHE A  18     4651   3826   7307    706  -1246   -682       C  
ATOM    120  CE1 PHE A  18      38.624  13.746  14.264  1.00 49.35           C  
ANISOU  120  CE1 PHE A  18     5683   5044   8024    910  -1413   -710       C  
ATOM    121  CE2 PHE A  18      36.364  13.118  14.638  1.00 41.64           C  
ANISOU  121  CE2 PHE A  18     4655   3886   7280    727  -1387   -741       C  
ATOM    122  CZ  PHE A  18      37.502  13.058  13.873  1.00 39.68           C  
ANISOU  122  CZ  PHE A  18     4462   3745   6870    826  -1450   -765       C  
ATOM    123  H   PHE A  18      36.457  13.584  18.918  1.00 51.51           H  
ATOM    124  HA  PHE A  18      39.013  14.422  18.395  1.00 50.07           H  
ATOM    125  HB2 PHE A  18      36.534  15.612  17.700  1.00 46.89           H  
ATOM    126  HB3 PHE A  18      37.933  16.231  17.303  1.00 46.89           H  
ATOM    127  HD1 PHE A  18      39.382  14.969  15.690  1.00 45.98           H  
ATOM    128  HD2 PHE A  18      35.559  13.906  16.321  1.00 50.17           H  
ATOM    129  HE1 PHE A  18      39.408  13.706  13.741  1.00 59.54           H  
ATOM    130  HE2 PHE A  18      35.591  12.645  14.371  1.00 50.29           H  
ATOM    131  HZ  PHE A  18      37.513  12.544  13.080  1.00 47.93           H  
ATOM    132  N   GLY A  19      39.498  15.766  20.372  1.00 45.53           N  
ANISOU  132  N   GLY A  19     5860   4216   7223    506  -1153   -471       N  
ATOM    133  CA  GLY A  19      39.810  16.493  21.605  1.00 36.33           C  
ANISOU  133  CA  GLY A  19     4959   2973   5873    334  -1114   -435       C  
ATOM    134  C   GLY A  19      40.351  15.575  22.673  1.00 52.19           C  
ANISOU  134  C   GLY A  19     7292   4857   7682    224  -1240   -359       C  
ATOM    135  O   GLY A  19      41.346  16.004  23.248  1.00 49.28           O  
ANISOU  135  O   GLY A  19     7176   4451   7097     60  -1345   -297       O  
ATOM    136  H   GLY A  19      40.229  15.465  19.929  1.00 54.96           H  
ATOM    137  HA2 GLY A  19      40.483  17.191  21.402  1.00 43.27           H  
ATOM    138  HA3 GLY A  19      38.997  16.944  21.941  1.00 43.27           H  
ATOM    139  N   THR A  20      39.905  14.311  22.771  1.00 45.62           N  
ANISOU  139  N   THR A  20     6484   3944   6904    286  -1254   -352       N  
ATOM    140  CA  THR A  20      40.315  13.344  23.832  1.00 47.21           C  
ANISOU  140  CA  THR A  20     6998   4009   6932    198  -1389   -248       C  
ATOM    141  C   THR A  20      41.251  12.256  23.307  1.00 49.83           C  
ANISOU  141  C   THR A  20     7153   4397   7383    378  -1653   -148       C  
ATOM    142  O   THR A  20      42.267  12.046  23.958  1.00 62.16           O  
ANISOU  142  O   THR A  20     8802   5952   8865    354  -1936     17       O  
ATOM    143  CB  THR A  20      39.107  12.691  24.499  1.00 50.26           C  
ANISOU  143  CB  THR A  20     7630   4172   7294     93  -1101   -312       C  
ATOM    144  OG1 THR A  20      38.044  13.639  24.504  1.00 54.76           O  
ANISOU  144  OG1 THR A  20     8302   4648   7856    -45   -765   -409       O  
ATOM    145  CG2 THR A  20      39.404  12.185  25.894  1.00 50.02           C  
ANISOU  145  CG2 THR A  20     8024   3972   7011    -45  -1222   -187       C  
ATOM    146  H   THR A  20      39.331  13.944  22.168  1.00 55.06           H  
ATOM    147  HA  THR A  20      40.803  13.833  24.513  1.00 56.97           H  
ATOM    148  HB  THR A  20      38.840  11.927  23.950  1.00 60.63           H  
ATOM    149  HG1 THR A  20      37.651  13.645  23.755  1.00 66.03           H  
ATOM    150 HG21 THR A  20      38.596  11.802  26.280  1.00 60.35           H  
ATOM    151 HG22 THR A  20      40.094  11.500  25.852  1.00 60.35           H  
ATOM    152 HG23 THR A  20      39.713  12.919  26.453  1.00 60.35           H  
ATOM    153  N   LEU A  21      40.914  11.576  22.216  1.00 42.44           N  
ANISOU  153  N   LEU A  21     5977   3494   6656    545  -1567   -233       N  
ATOM    154  CA  LEU A  21      41.763  10.534  21.595  1.00 46.73           C  
ANISOU  154  CA  LEU A  21     6353   4053   7351    729  -1722   -167       C  
ATOM    155  C   LEU A  21      42.593  11.165  20.484  1.00 46.17           C  
ANISOU  155  C   LEU A  21     5969   4159   7415    874  -1782   -180       C  
ATOM    156  O   LEU A  21      43.782  10.857  20.413  1.00 40.58           O  
ANISOU  156  O   LEU A  21     5129   3460   6830    988  -1942    -57       O  
ATOM    157  CB  LEU A  21      40.886   9.403  21.048  1.00 50.62           C  
ANISOU  157  CB  LEU A  21     6837   4440   7958    794  -1566   -272       C  
ATOM    158  CG  LEU A  21      40.010   8.650  22.048  1.00 47.50           C  
ANISOU  158  CG  LEU A  21     6734   3828   7484    684  -1486   -242       C  
ATOM    159  CD1 LEU A  21      39.105   7.671  21.320  1.00 51.87           C  
ANISOU  159  CD1 LEU A  21     7227   4289   8191    735  -1331   -369       C  
ATOM    160  CD2 LEU A  21      40.833   7.918  23.092  1.00 60.06           C  
ANISOU  160  CD2 LEU A  21     8494   5317   9009    698  -1715    -31       C  
ATOM    161  H   LEU A  21      40.129  11.719  21.777  1.00 51.25           H  
ATOM    162  HA  LEU A  21      42.376  10.176  22.274  1.00 56.40           H  
ATOM    163  HB2 LEU A  21      40.303   9.781  20.359  1.00 61.07           H  
ATOM    164  HB3 LEU A  21      41.471   8.759  20.606  1.00 61.07           H  
ATOM    165  HG  LEU A  21      39.439   9.307  22.515  1.00 57.31           H  
ATOM    166 HD11 LEU A  21      38.612   7.138  21.967  1.00 62.56           H  
ATOM    167 HD12 LEU A  21      38.477   8.162  20.761  1.00 62.56           H  
ATOM    168 HD13 LEU A  21      39.643   7.084  20.762  1.00 62.56           H  
ATOM    169 HD21 LEU A  21      40.237   7.489  23.730  1.00 72.39           H  
ATOM    170 HD22 LEU A  21      41.377   7.240  22.657  1.00 72.39           H  
ATOM    171 HD23 LEU A  21      41.407   8.545  23.562  1.00 72.39           H  
ATOM    172  N   PHE A  22      41.989  12.015  19.662  1.00 42.20           N  
ANISOU  172  N   PHE A  22     5337   3773   6926    872  -1643   -309       N  
ATOM    173  CA  PHE A  22      42.674  12.700  18.548  1.00 49.71           C  
ANISOU  173  CA  PHE A  22     6047   4881   7959    980  -1660   -326       C  
ATOM    174  C   PHE A  22      42.894  14.143  18.998  1.00 43.91           C  
ANISOU  174  C   PHE A  22     5309   4240   7135    872  -1682   -297       C  
ATOM    175  O   PHE A  22      41.961  14.698  19.562  1.00 50.70           O  
ANISOU  175  O   PHE A  22     6284   5070   7910    745  -1557   -353       O  
ATOM    176  CB  PHE A  22      41.875  12.512  17.261  1.00 43.28           C  
ANISOU  176  CB  PHE A  22     5131   4117   7196   1042  -1524   -469       C  
ATOM    177  CG  PHE A  22      41.410  11.105  16.990  1.00 45.35           C  
ANISOU  177  CG  PHE A  22     5472   4253   7505   1075  -1473   -537       C  
ATOM    178  CD1 PHE A  22      42.291  10.149  16.517  1.00 49.53           C  
ANISOU  178  CD1 PHE A  22     5978   4711   8130   1209  -1470   -523       C  
ATOM    179  CD2 PHE A  22      40.088  10.743  17.184  1.00 48.19           C  
ANISOU  179  CD2 PHE A  22     5917   4536   7858    966  -1397   -613       C  
ATOM    180  CE1 PHE A  22      41.863   8.858  16.267  1.00 49.34           C  
ANISOU  180  CE1 PHE A  22     6060   4542   8145   1224  -1395   -601       C  
ATOM    181  CE2 PHE A  22      39.664   9.449  16.931  1.00 54.10           C  
ANISOU  181  CE2 PHE A  22     6743   5156   8657    969  -1355   -684       C  
ATOM    182  CZ  PHE A  22      40.551   8.511  16.472  1.00 49.25           C  
ANISOU  182  CZ  PHE A  22     6150   4473   8089   1093  -1356   -686       C  
ATOM    183  H   PHE A  22      41.116  12.258  19.737  1.00 50.96           H  
ATOM    184  HA  PHE A  22      43.560  12.281  18.417  1.00 59.97           H  
ATOM    185  HB2 PHE A  22      41.093  13.102  17.297  1.00 52.25           H  
ATOM    186  HB3 PHE A  22      42.431  12.807  16.511  1.00 52.25           H  
ATOM    187  HD1 PHE A  22      43.196  10.377  16.379  1.00 59.75           H  
ATOM    188  HD2 PHE A  22      39.473  11.383  17.498  1.00 58.15           H  
ATOM    189  HE1 PHE A  22      42.474   8.214  15.954  1.00 59.53           H  
ATOM    190  HE2 PHE A  22      38.762   9.213  17.071  1.00 65.24           H  
ATOM    191  HZ  PHE A  22      40.264   7.631  16.300  1.00 59.41           H  
ATOM    192  N   ASP A  23      44.094  14.696  18.822  1.00 47.76           N  
ANISOU  192  N   ASP A  23     5655   4812   7681    917  -1811   -207       N  
ATOM    193  CA  ASP A  23      44.456  16.059  19.290  1.00 42.72           C  
ANISOU  193  CA  ASP A  23     5032   4242   6958    790  -1861   -170       C  
ATOM    194  C   ASP A  23      44.190  17.048  18.164  1.00 42.73           C  
ANISOU  194  C   ASP A  23     4860   4366   7009    849  -1703   -259       C  
ATOM    195  O   ASP A  23      44.950  17.055  17.201  1.00 43.09           O  
ANISOU  195  O   ASP A  23     4703   4491   7178    982  -1696   -249       O  
ATOM    196  CB  ASP A  23      45.902  16.135  19.784  1.00 48.94           C  
ANISOU  196  CB  ASP A  23     5726   5041   7827    781  -2122     -2       C  
ATOM    197  CG  ASP A  23      46.247  17.381  20.580  1.00 47.82           C  
ANISOU  197  CG  ASP A  23     5690   4931   7547    574  -2228     40       C  
ATOM    198  OD1 ASP A  23      45.404  18.285  20.663  1.00 45.32           O  
ANISOU  198  OD1 ASP A  23     5472   4635   7113    486  -2031    -77       O  
ATOM    199  OD2 ASP A  23      47.354  17.419  21.132  1.00 48.66           O  
ANISOU  199  OD2 ASP A  23     5780   5022   7685    489  -2518    201       O  
ATOM    200  H   ASP A  23      44.756  14.289  18.353  1.00 57.64           H  
ATOM    201  HA  ASP A  23      43.872  16.282  20.051  1.00 51.58           H  
ATOM    202  HB2 ASP A  23      46.074  15.358  20.355  1.00 59.04           H  
ATOM    203  HB3 ASP A  23      46.508  16.085  19.018  1.00 59.04           H  
ATOM    204  N   VAL A  24      43.161  17.867  18.319  1.00 42.48           N  
ANISOU  204  N   VAL A  24     4918   4321   6901    751  -1549   -332       N  
ATOM    205  CA  VAL A  24      42.755  18.904  17.327  1.00 44.61           C  
ANISOU  205  CA  VAL A  24     5031   4687   7231    805  -1425   -378       C  
ATOM    206  C   VAL A  24      43.839  19.991  17.238  1.00 50.84           C  
ANISOU  206  C   VAL A  24     5730   5559   8026    781  -1464   -326       C  
ATOM    207  O   VAL A  24      43.986  20.557  16.155  1.00 38.65           O  
ANISOU  207  O   VAL A  24     4033   4107   6544    864  -1394   -335       O  
ATOM    208  CB  VAL A  24      41.356  19.458  17.685  1.00 42.19           C  
ANISOU  208  CB  VAL A  24     4788   4302   6938    722  -1242   -429       C  
ATOM    209  CG1 VAL A  24      40.279  18.384  17.614  1.00 42.77           C  
ANISOU  209  CG1 VAL A  24     4898   4287   7065    737  -1207   -474       C  
ATOM    210  CG2 VAL A  24      41.329  20.155  19.039  1.00 42.28           C  
ANISOU  210  CG2 VAL A  24     5014   4202   6849    541  -1151   -423       C  
ATOM    211  H   VAL A  24      42.638  17.845  19.059  1.00 51.29           H  
ATOM    212  HA  VAL A  24      42.693  18.474  16.456  1.00 53.85           H  
ATOM    213  HB  VAL A  24      41.134  20.139  17.002  1.00 50.94           H  
ATOM    214 HG11 VAL A  24      39.405  18.790  17.748  1.00 51.64           H  
ATOM    215 HG12 VAL A  24      40.304  17.955  16.740  1.00 51.64           H  
ATOM    216 HG13 VAL A  24      40.431  17.715  18.304  1.00 51.64           H  
ATOM    217 HG21 VAL A  24      40.624  19.773  19.585  1.00 51.05           H  
ATOM    218 HG22 VAL A  24      42.180  20.039  19.492  1.00 51.05           H  
ATOM    219 HG23 VAL A  24      41.165  21.102  18.912  1.00 51.05           H  
ATOM    220  N   ARG A  25      44.605  20.228  18.303  1.00 40.72           N  
ANISOU  220  N   ARG A  25     4565   4237   6671    642  -1591   -264       N  
ATOM    221  CA  ARG A  25      45.634  21.299  18.364  1.00 53.54           C  
ANISOU  221  CA  ARG A  25     6094   5925   8325    583  -1656   -212       C  
ATOM    222  C   ARG A  25      46.712  21.020  17.320  1.00 47.81           C  
ANISOU  222  C   ARG A  25     5084   5289   7791    751  -1718   -153       C  
ATOM    223  O   ARG A  25      47.372  21.971  16.930  1.00 48.72           O  
ANISOU  223  O   ARG A  25     5058   5464   7991    738  -1705   -121       O  
ATOM    224  CB  ARG A  25      46.197  21.440  19.779  1.00 42.99           C  
ANISOU  224  CB  ARG A  25     4968   4512   6852    357  -1860   -141       C  
ATOM    225  CG  ARG A  25      45.148  21.747  20.838  1.00 61.27           C  
ANISOU  225  CG  ARG A  25     7634   6696   8949    148  -1698   -222       C  
ATOM    226  CD  ARG A  25      45.748  22.163  22.162  1.00 63.03           C  
ANISOU  226  CD  ARG A  25     8174   6825   8949   -134  -1914   -160       C  
ATOM    227  NE  ARG A  25      46.566  21.118  22.763  1.00 71.41           N  
ANISOU  227  NE  ARG A  25     9199   7899  10036   -123  -2279     -8       N  
ATOM    228  CZ  ARG A  25      46.139  20.098  23.504  1.00 71.99           C  
ANISOU  228  CZ  ARG A  25     9553   7856   9943   -210  -2388     40       C  
ATOM    229  NH1 ARG A  25      44.853  19.916  23.767  1.00 81.94           N  
ANISOU  229  NH1 ARG A  25    11160   8975  10999   -321  -2120    -73       N  
ATOM    230  NH2 ARG A  25      47.022  19.238  23.984  1.00 71.92           N  
ANISOU  230  NH2 ARG A  25     9469   7848  10011   -180  -2743    219       N  
ATOM    231  H   ARG A  25      44.580  19.702  19.044  1.00 49.19           H  
ATOM    232  HA  ARG A  25      45.195  22.148  18.125  1.00 64.57           H  
ATOM    233  HB2 ARG A  25      46.657  20.608  20.017  1.00 51.90           H  
ATOM    234  HB3 ARG A  25      46.862  22.158  19.777  1.00 51.90           H  
ATOM    235  HG2 ARG A  25      44.566  22.467  20.514  1.00 73.84           H  
ATOM    236  HG3 ARG A  25      44.590  20.955  20.982  1.00 73.84           H  
ATOM    237  HD2 ARG A  25      46.308  22.956  22.019  1.00 75.95           H  
ATOM    238  HD3 ARG A  25      45.031  22.418  22.779  1.00 75.95           H  
ATOM    239  HE  ARG A  25      47.417  21.178  22.641  1.00 86.02           H  
ATOM    240 HH11 ARG A  25      44.246  20.464  23.462  1.00 98.65           H  
ATOM    241 HH12 ARG A  25      44.603  19.229  24.255  1.00 98.65           H  
ATOM    242 HH21 ARG A  25      47.881  19.344  23.819  1.00 86.63           H  
ATOM    243 HH22 ARG A  25      46.753  18.557  24.472  1.00 86.63           H  
ATOM    244  N   ALA A  26      46.834  19.787  16.839  1.00 48.92           N  
ANISOU  244  N   ALA A  26     5152   5412   8025    905  -1733   -146       N  
ATOM    245  CA  ALA A  26      47.852  19.365  15.851  1.00 59.42           C  
ANISOU  245  CA  ALA A  26     6240   6768   9569   1069  -1699   -101       C  
ATOM    246  C   ALA A  26      47.669  20.070  14.509  1.00 47.65           C  
ANISOU  246  C   ALA A  26     4677   5353   8075   1154  -1471   -180       C  
ATOM    247  O   ALA A  26      48.607  20.017  13.712  1.00 49.70           O  
ANISOU  247  O   ALA A  26     4769   5615   8501   1264  -1368   -151       O  
ATOM    248  CB  ALA A  26      47.814  17.872  15.692  1.00 43.99           C  
ANISOU  248  CB  ALA A  26     4284   4725   7705   1204  -1700    -97       C  
ATOM    249  H   ALA A  26      46.319  19.093  17.115  1.00 59.03           H  
ATOM    250  HA  ALA A  26      48.733  19.613  16.201  1.00 71.62           H  
ATOM    251  HB1 ALA A  26      48.543  17.586  15.117  1.00 53.10           H  
ATOM    252  HB2 ALA A  26      47.907  17.450  16.562  1.00 53.10           H  
ATOM    253  HB3 ALA A  26      46.967  17.607  15.295  1.00 53.10           H  
ATOM    254  N   VAL A  27      46.515  20.678  14.252  1.00 44.90           N  
ANISOU  254  N   VAL A  27     4453   5043   7565   1105  -1380   -258       N  
ATOM    255  CA  VAL A  27      46.238  21.449  13.005  1.00 41.01           C  
ANISOU  255  CA  VAL A  27     3926   4616   7041   1161  -1219   -291       C  
ATOM    256  C   VAL A  27      47.090  22.734  12.962  1.00 42.87           C  
ANISOU  256  C   VAL A  27     4047   4894   7348   1117  -1168   -235       C  
ATOM    257  O   VAL A  27      47.262  23.247  11.858  1.00 38.09           O  
ANISOU  257  O   VAL A  27     3408   4329   6735   1173  -1020   -238       O  
ATOM    258  CB  VAL A  27      44.726  21.726  12.877  1.00 46.12           C  
ANISOU  258  CB  VAL A  27     4687   5267   7569   1115  -1191   -336       C  
ATOM    259  CG1 VAL A  27      44.292  22.982  13.615  1.00 43.26           C  
ANISOU  259  CG1 VAL A  27     4361   4874   7203    985  -1179   -312       C  
ATOM    260  CG2 VAL A  27      44.293  21.771  11.425  1.00 53.38           C  
ANISOU  260  CG2 VAL A  27     5612   6243   8427   1174  -1100   -339       C  
ATOM    261  H   VAL A  27      45.819  20.669  14.835  1.00 54.20           H  
ATOM    262  HA  VAL A  27      46.508  20.893  12.253  1.00 49.54           H  
ATOM    263  HB  VAL A  27      44.252  20.964  13.292  1.00 55.66           H  
ATOM    264 HG11 VAL A  27      43.323  22.992  13.693  1.00 52.24           H  
ATOM    265 HG12 VAL A  27      44.687  22.989  14.505  1.00 52.24           H  
ATOM    266 HG13 VAL A  27      44.583  23.771  13.126  1.00 52.24           H  
ATOM    267 HG21 VAL A  27      43.327  21.690  11.375  1.00 64.38           H  
ATOM    268 HG22 VAL A  27      44.573  22.611  11.027  1.00 64.38           H  
ATOM    269 HG23 VAL A  27      44.698  21.034  10.938  1.00 64.38           H  
ATOM    270  N   LEU A  28      47.658  23.188  14.086  1.00 41.82           N  
ANISOU  270  N   LEU A  28     3887   4740   7263    993  -1296   -182       N  
ATOM    271  CA  LEU A  28      48.431  24.464  14.203  1.00 44.71           C  
ANISOU  271  CA  LEU A  28     4161   5130   7697    906  -1265   -138       C  
ATOM    272  C   LEU A  28      49.576  24.532  13.212  1.00 45.94           C  
ANISOU  272  C   LEU A  28     4103   5308   8043   1022  -1145    -95       C  
ATOM    273  O   LEU A  28      49.717  25.570  12.593  1.00 42.42           O  
ANISOU  273  O   LEU A  28     3620   4890   7606   1024   -980    -94       O  
ATOM    274  CB  LEU A  28      49.023  24.549  15.611  1.00 45.35           C  
ANISOU  274  CB  LEU A  28     4281   5165   7783    713  -1489    -82       C  
ATOM    275  CG  LEU A  28      50.130  25.579  15.856  1.00 49.50           C  
ANISOU  275  CG  LEU A  28     4656   5701   8451    598  -1546    -12       C  
ATOM    276  CD1 LEU A  28      49.643  26.992  15.592  1.00 36.73           C  
ANISOU  276  CD1 LEU A  28     3121   4088   6746    529  -1337    -72       C  
ATOM    277  CD2 LEU A  28      50.650  25.472  17.278  1.00 46.73           C  
ANISOU  277  CD2 LEU A  28     4369   5298   8089    375  -1873     71       C  
ATOM    278  H   LEU A  28      47.549  22.764  14.881  1.00 50.50           H  
ATOM    279  HA  LEU A  28      47.820  25.222  14.047  1.00 53.97           H  
ATOM    280  HB2 LEU A  28      48.292  24.735  16.233  1.00 54.73           H  
ATOM    281  HB3 LEU A  28      49.382  23.669  15.840  1.00 54.73           H  
ATOM    282  HG  LEU A  28      50.885  25.392  15.247  1.00 59.72           H  
ATOM    283 HD11 LEU A  28      50.338  27.627  15.833  1.00 42.48           H  
ATOM    284 HD12 LEU A  28      49.424  27.098  14.652  1.00 42.48           H  
ATOM    285 HD13 LEU A  28      48.854  27.159  16.128  1.00 42.48           H  
ATOM    286 HD21 LEU A  28      51.362  26.121  17.414  1.00 56.40           H  
ATOM    287 HD22 LEU A  28      49.926  25.651  17.904  1.00 56.40           H  
ATOM    288 HD23 LEU A  28      50.995  24.576  17.431  1.00 56.40           H  
ATOM    289  N   ALA A  29      50.339  23.461  13.047  1.00 46.46           N  
ANISOU  289  N   ALA A  29     4026   5330   8295   1121  -1189    -48       N  
ATOM    290  CA  ALA A  29      51.539  23.474  12.196  1.00 51.28           C  
ANISOU  290  CA  ALA A  29     4403   5908   9174   1224  -1019      6       C  
ATOM    291  C   ALA A  29      51.172  23.752  10.747  1.00 45.12           C  
ANISOU  291  C   ALA A  29     3735   5143   8265   1323   -705    -75       C  
ATOM    292  O   ALA A  29      51.816  24.614  10.151  1.00 40.07           O  
ANISOU  292  O   ALA A  29     3006   4502   7718   1325   -517    -50       O  
ATOM    293  CB  ALA A  29      52.292  22.177  12.342  1.00 46.73           C  
ANISOU  293  CB  ALA A  29     3707   5247   8800   1316  -1037     74       C  
ATOM    294  H   ALA A  29      50.170  22.648  13.421  1.00 56.07           H  
ATOM    295  HA  ALA A  29      52.120  24.206  12.507  1.00 61.86           H  
ATOM    296  HB1 ALA A  29      53.088  22.200  11.785  1.00 56.39           H  
ATOM    297  HB2 ALA A  29      52.553  22.054  13.271  1.00 56.39           H  
ATOM    298  HB3 ALA A  29      51.726  21.437  12.065  1.00 56.39           H  
ATOM    299  N   ALA A  30      50.153  23.091  10.219  1.00 40.22           N  
ANISOU  299  N   ALA A  30     3334   4526   7423   1385   -658   -165       N  
ATOM    300  CA  ALA A  30      49.689  23.328   8.838  1.00 47.03           C  
ANISOU  300  CA  ALA A  30     4383   5405   8082   1424   -445   -224       C  
ATOM    301  C   ALA A  30      49.165  24.757   8.731  1.00 41.69           C  
ANISOU  301  C   ALA A  30     3739   4800   7302   1336   -446   -186       C  
ATOM    302  O   ALA A  30      49.534  25.435   7.780  1.00 52.58           O  
ANISOU  302  O   ALA A  30     5096   6170   8713   1347   -247   -155       O  
ATOM    303  CB  ALA A  30      48.641  22.316   8.481  1.00 49.55           C  
ANISOU  303  CB  ALA A  30     4940   5721   8164   1439   -510   -310       C  
ATOM    304  H   ALA A  30      49.651  22.477  10.668  1.00 48.59           H  
ATOM    305  HA  ALA A  30      50.454  23.226   8.225  1.00 56.76           H  
ATOM    306  HB1 ALA A  30      48.378  22.433   7.554  1.00 59.77           H  
ATOM    307  HB2 ALA A  30      48.998  21.421   8.602  1.00 59.77           H  
ATOM    308  HB3 ALA A  30      47.864  22.435   9.053  1.00 59.77           H  
ATOM    309  N   ALA A  31      48.406  25.212   9.720  1.00 44.30           N  
ANISOU  309  N   ALA A  31     4118   5171   7544   1248   -629   -182       N  
ATOM    310  CA  ALA A  31      47.807  26.564   9.734  1.00 46.12           C  
ANISOU  310  CA  ALA A  31     4384   5426   7713   1178   -594   -140       C  
ATOM    311  C   ALA A  31      48.915  27.613   9.751  1.00 45.21           C  
ANISOU  311  C   ALA A  31     4131   5299   7747   1132   -474    -90       C  
ATOM    312  O   ALA A  31      48.812  28.563   8.976  1.00 49.17           O  
ANISOU  312  O   ALA A  31     4675   5802   8207   1131   -329    -48       O  
ATOM    313  CB  ALA A  31      46.888  26.698  10.911  1.00 38.95           C  
ANISOU  313  CB  ALA A  31     3519   4500   6781   1082   -734   -149       C  
ATOM    314  H   ALA A  31      48.212  24.732  10.468  1.00 53.48           H  
ATOM    315  HA  ALA A  31      47.282  26.682   8.908  1.00 55.66           H  
ATOM    316  HB1 ALA A  31      46.452  27.566  10.885  1.00 47.06           H  
ATOM    317  HB2 ALA A  31      46.214  25.998  10.881  1.00 47.06           H  
ATOM    318  HB3 ALA A  31      47.397  26.620  11.736  1.00 47.06           H  
ATOM    319  N   GLU A  32      49.961  27.410  10.551  1.00 49.12           N  
ANISOU  319  N   GLU A  32     4455   5773   8436   1080   -557    -74       N  
ATOM    320  CA  GLU A  32      51.094  28.357  10.640  1.00 47.69           C  
ANISOU  320  CA  GLU A  32     4104   5569   8446   1004   -480    -19       C  
ATOM    321  C   GLU A  32      51.818  28.403   9.299  1.00 49.21           C  
ANISOU  321  C   GLU A  32     4219   5731   8746   1116   -196      4       C  
ATOM    322  O   GLU A  32      52.145  29.497   8.866  1.00 44.64           O  
ANISOU  322  O   GLU A  32     3582   5131   8249   1068    -36     43       O  
ATOM    323  CB  GLU A  32      52.024  27.983  11.790  1.00 50.40           C  
ANISOU  323  CB  GLU A  32     4270   5888   8993    898   -718     26       C  
ATOM    324  CG  GLU A  32      53.167  28.948  12.003  1.00 46.87           C  
ANISOU  324  CG  GLU A  32     3573   5404   8831    798   -712    105       C  
ATOM    325  CD  GLU A  32      52.793  30.348  12.441  1.00 55.97           C  
ANISOU  325  CD  GLU A  32     4793   6550   9924    689   -558     91       C  
ATOM    326  OE1 GLU A  32      53.629  31.246  12.269  1.00 65.14           O  
ANISOU  326  OE1 GLU A  32     5779   7677  11294    706   -362    138       O  
ATOM    327  OE2 GLU A  32      51.683  30.539  12.966  1.00 58.55           O  
ANISOU  327  OE2 GLU A  32     5340   6877  10029    591   -592     40       O  
ATOM    328  H   GLU A  32      50.060  26.660  11.048  1.00 59.26           H  
ATOM    329  HA  GLU A  32      50.723  29.251  10.818  1.00 57.54           H  
ATOM    330  HB2 GLU A  32      51.496  27.928  12.615  1.00 60.80           H  
ATOM    331  HB3 GLU A  32      52.394  27.092  11.614  1.00 60.80           H  
ATOM    332  HG2 GLU A  32      53.749  28.577  12.678  1.00 56.56           H  
ATOM    333  HG3 GLU A  32      53.689  29.013  11.176  1.00 56.56           H  
ATOM    334  N   GLN A  33      52.046  27.269   8.655  1.00 41.37           N  
ANISOU  334  N   GLN A  33     3269   4709   7740   1251    -87    -29       N  
ATOM    335  CA  GLN A  33      52.824  27.224   7.388  1.00 44.87           C  
ANISOU  335  CA  GLN A  33     3687   5072   8291   1343    259    -22       C  
ATOM    336  C   GLN A  33      52.035  27.891   6.272  1.00 43.63           C  
ANISOU  336  C   GLN A  33     3825   4924   7827   1352    460    -36       C  
ATOM    337  O   GLN A  33      52.663  28.535   5.429  1.00 48.20           O  
ANISOU  337  O   GLN A  33     4416   5431   8467   1370    768    -10       O  
ATOM    338  CB  GLN A  33      53.223  25.790   7.031  1.00 57.31           C  
ANISOU  338  CB  GLN A  33     5245   6558   9975   1469    367    -63       C  
ATOM    339  CG  GLN A  33      54.270  25.191   7.964  1.00 57.71           C  
ANISOU  339  CG  GLN A  33     4920   6536  10472   1494    262     18       C  
ATOM    340  CD  GLN A  33      54.347  23.688   7.858  1.00 52.98           C  
ANISOU  340  CD  GLN A  33     4331   5838   9960   1625    307    -15       C  
ATOM    341  OE1 GLN A  33      54.141  22.967   8.828  1.00 55.40           O  
ANISOU  341  OE1 GLN A  33     4513   6152  10385   1608     23     42       O  
ATOM    342  NE2 GLN A  33      54.639  23.197   6.666  1.00 64.39           N  
ANISOU  342  NE2 GLN A  33     6000   7180  11285   1722    674   -107       N  
ATOM    343  H   GLN A  33      51.717  26.466   8.931  1.00 49.96           H  
ATOM    344  HA  GLN A  33      53.650  27.742   7.526  1.00 54.16           H  
ATOM    345  HB2 GLN A  33      52.420  25.228   7.047  1.00 69.10           H  
ATOM    346  HB3 GLN A  33      53.571  25.786   6.116  1.00 69.10           H  
ATOM    347  HG2 GLN A  33      55.148  25.571   7.749  1.00 69.58           H  
ATOM    348  HG3 GLN A  33      54.059  25.435   8.890  1.00 69.58           H  
ATOM    349 HE21 GLN A  33      55.020  23.710   6.056  1.00 77.58           H  
ATOM    350 HE22 GLN A  33      54.465  22.350   6.483  1.00 77.58           H  
ATOM    351  N   MET A  34      50.733  27.654   6.210  1.00 45.60           N  
ANISOU  351  N   MET A  34     4308   5243   7773   1332    289    -54       N  
ATOM    352  CA  MET A  34      49.836  28.291   5.215  1.00 64.78           C  
ANISOU  352  CA  MET A  34     7005   7684   9924   1318    372    -11       C  
ATOM    353  C   MET A  34      49.639  29.790   5.510  1.00 41.98           C  
ANISOU  353  C   MET A  34     4055   4824   7072   1247    315     78       C  
ATOM    354  O   MET A  34      49.593  30.550   4.543  1.00 59.37           O  
ANISOU  354  O   MET A  34     6402   7000   9154   1238    454    157       O  
ATOM    355  CB  MET A  34      48.501  27.544   5.155  1.00 60.67           C  
ANISOU  355  CB  MET A  34     6712   7204   9135   1322    162    -45       C  
ATOM    356  CG  MET A  34      48.554  26.389   4.190  1.00 69.78           C  
ANISOU  356  CG  MET A  34     8008   8303  10203   1371    247   -147       C  
ATOM    357  SD  MET A  34      47.093  25.360   4.251  1.00 75.57           S  
ANISOU  357  SD  MET A  34     8888   9105  10722   1324   -119   -164       S  
ATOM    358  CE  MET A  34      47.443  24.374   5.702  1.00 68.16           C  
ANISOU  358  CE  MET A  34     7632   8180  10086   1351   -263   -210       C  
ATOM    359  H   MET A  34      50.313  27.110   6.805  1.00 55.03           H  
ATOM    360  HA  MET A  34      50.272  28.217   4.336  1.00 78.05           H  
ATOM    361  HB2 MET A  34      48.264  27.220   6.045  1.00 73.12           H  
ATOM    362  HB3 MET A  34      47.804  28.168   4.869  1.00 73.12           H  
ATOM    363  HG2 MET A  34      48.656  26.737   3.279  1.00 84.06           H  
ATOM    364  HG3 MET A  34      49.340  25.838   4.392  1.00 84.06           H  
ATOM    365  HE1 MET A  34      46.851  23.613   5.723  1.00 82.11           H  
ATOM    366  HE2 MET A  34      48.357  24.069   5.670  1.00 82.11           H  
ATOM    367  HE3 MET A  34      47.309  24.910   6.490  1.00 82.11           H  
ATOM    368  N   PHE A  35      49.543  30.199   6.771  1.00 45.53           N  
ANISOU  368  N   PHE A  35     4327   5297   7675   1183    138     69       N  
ATOM    369  CA  PHE A  35      49.283  31.597   7.192  1.00 42.32           C  
ANISOU  369  CA  PHE A  35     3878   4870   7332   1097    138    127       C  
ATOM    370  C   PHE A  35      50.301  31.990   8.256  1.00 44.55           C  
ANISOU  370  C   PHE A  35     3946   5127   7855    989    123     98       C  
ATOM    371  O   PHE A  35      49.994  31.938   9.447  1.00 40.14           O  
ANISOU  371  O   PHE A  35     3359   4565   7328    890    -56     60       O  
ATOM    372  CB  PHE A  35      47.851  31.735   7.705  1.00 41.50           C  
ANISOU  372  CB  PHE A  35     3847   4770   7148   1078    -41    142       C  
ATOM    373  CG  PHE A  35      46.780  31.307   6.736  1.00 49.61           C  
ANISOU  373  CG  PHE A  35     5042   5823   7985   1154   -122    201       C  
ATOM    374  CD1 PHE A  35      46.474  32.088   5.635  1.00 51.75           C  
ANISOU  374  CD1 PHE A  35     5440   6071   8151   1179    -42    326       C  
ATOM    375  CD2 PHE A  35      46.071  30.134   6.931  1.00 41.27           C  
ANISOU  375  CD2 PHE A  35     4029   4802   6852   1178   -309    147       C  
ATOM    376  CE1 PHE A  35      45.489  31.699   4.745  1.00 49.63           C  
ANISOU  376  CE1 PHE A  35     5345   5821   7690   1207   -199    411       C  
ATOM    377  CE2 PHE A  35      45.085  29.749   6.041  1.00 37.75           C  
ANISOU  377  CE2 PHE A  35     3733   4372   6238   1205   -438    209       C  
ATOM    378  CZ  PHE A  35      44.797  30.531   4.949  1.00 43.97           C  
ANISOU  378  CZ  PHE A  35     4653   5144   6910   1210   -410    348       C  
ATOM    379  H   PHE A  35      49.619  29.635   7.479  1.00 54.95           H  
ATOM    380  HA  PHE A  35      49.393  32.195   6.415  1.00 51.10           H  
ATOM    381  HB2 PHE A  35      47.760  31.202   8.522  1.00 50.11           H  
ATOM    382  HB3 PHE A  35      47.699  32.673   7.945  1.00 50.11           H  
ATOM    383  HD1 PHE A  35      46.946  32.892   5.489  1.00 62.41           H  
ATOM    384  HD2 PHE A  35      46.265  29.589   7.677  1.00 49.85           H  
ATOM    385  HE1 PHE A  35      45.291  32.240   3.999  1.00 59.87           H  
ATOM    386  HE2 PHE A  35      44.611  28.945   6.183  1.00 45.62           H  
ATOM    387  HZ  PHE A  35      44.124  30.268   4.343  1.00 53.08           H  
ATOM    388  N   PRO A  36      51.547  32.330   7.878  1.00 46.21           N  
ANISOU  388  N   PRO A  36     4017   5299   8241    982    304    121       N  
ATOM    389  CA  PRO A  36      52.552  32.619   8.888  1.00 41.08           C  
ANISOU  389  CA  PRO A  36     3128   4619   7862    846    223    122       C  
ATOM    390  C   PRO A  36      52.154  33.750   9.843  1.00 45.12           C  
ANISOU  390  C   PRO A  36     3704   5098   8340    672    139    113       C  
ATOM    391  O   PRO A  36      51.785  34.788   9.366  1.00 46.89           O  
ANISOU  391  O   PRO A  36     4037   5276   8502    661    314    145       O  
ATOM    392  CB  PRO A  36      53.772  32.945   8.030  1.00 46.88           C  
ANISOU  392  CB  PRO A  36     3708   5288   8816    873    512    171       C  
ATOM    393  CG  PRO A  36      53.567  32.178   6.760  1.00 45.90           C  
ANISOU  393  CG  PRO A  36     3755   5158   8529   1047    727    161       C  
ATOM    394  CD  PRO A  36      52.083  32.292   6.518  1.00 47.61           C  
ANISOU  394  CD  PRO A  36     4262   5437   8390   1078    596    152       C  
ATOM    395  HA  PRO A  36      52.739  31.799   9.406  1.00 47.71           H  
ATOM    396  HB2 PRO A  36      53.827  33.907   7.848  1.00 56.57           H  
ATOM    397  HB3 PRO A  36      54.598  32.662   8.477  1.00 56.57           H  
ATOM    398  HG2 PRO A  36      54.074  32.574   6.023  1.00 55.40           H  
ATOM    399  HG3 PRO A  36      53.833  31.242   6.868  1.00 55.40           H  
ATOM    400  HD2 PRO A  36      51.864  33.102   6.024  1.00 57.45           H  
ATOM    401  HD3 PRO A  36      51.756  31.518   6.026  1.00 57.45           H  
ATOM    402  N   GLY A  37      52.238  33.517  11.149  1.00 40.40           N  
ANISOU  402  N   GLY A  37     3080   4499   7770    527   -116     74       N  
ATOM    403  CA  GLY A  37      51.887  34.486  12.198  1.00 40.90           C  
ANISOU  403  CA  GLY A  37     3275   4491   7773    318   -167     35       C  
ATOM    404  C   GLY A  37      50.457  34.381  12.696  1.00 50.17           C  
ANISOU  404  C   GLY A  37     4690   5636   8736    324   -186    -17       C  
ATOM    405  O   GLY A  37      50.170  35.035  13.713  1.00 49.56           O  
ANISOU  405  O   GLY A  37     4773   5456   8602    138   -179    -70       O  
ATOM    406  H   GLY A  37      52.496  32.721  11.474  1.00 47.40           H  
ATOM    407  HA2 GLY A  37      52.501  34.353  12.963  1.00 49.40           H  
ATOM    408  HA3 GLY A  37      52.041  35.400  11.853  1.00 49.40           H  
ATOM    409  N   HIS A  38      49.591  33.607  12.044  1.00 40.32           N  
ANISOU  409  N   HIS A  38     3484   4449   7389    515   -189     -6       N  
ATOM    410  CA  HIS A  38      48.152  33.506  12.395  1.00 38.85           C  
ANISOU  410  CA  HIS A  38     3462   4213   7086    533   -184    -32       C  
ATOM    411  C   HIS A  38      47.704  32.079  12.719  1.00 35.34           C  
ANISOU  411  C   HIS A  38     3046   3826   6557    597   -370    -70       C  
ATOM    412  O   HIS A  38      46.525  31.915  12.990  1.00 34.60           O  
ANISOU  412  O   HIS A  38     3057   3682   6409    620   -354    -85       O  
ATOM    413  CB  HIS A  38      47.345  34.066  11.232  1.00 36.05           C  
ANISOU  413  CB  HIS A  38     3133   3840   6726    683    -17     56       C  
ATOM    414  CG  HIS A  38      47.738  35.438  10.815  1.00 47.69           C  
ANISOU  414  CG  HIS A  38     4598   5238   8285    646    193    117       C  
ATOM    415  ND1 HIS A  38      48.391  35.684   9.630  1.00 61.31           N  
ANISOU  415  ND1 HIS A  38     6257   7010  10027    722    294    185       N  
ATOM    416  CD2 HIS A  38      47.558  36.635  11.408  1.00 54.50           C  
ANISOU  416  CD2 HIS A  38     5536   5949   9223    537    364    119       C  
ATOM    417  CE1 HIS A  38      48.602  36.975   9.510  1.00 56.16           C  
ANISOU  417  CE1 HIS A  38     5624   6255   9459    662    489    236       C  
ATOM    418  NE2 HIS A  38      48.104  37.579  10.588  1.00 60.28           N  
ANISOU  418  NE2 HIS A  38     6226   6653  10024    553    533    195       N  
ATOM    419  H   HIS A  38      49.811  33.111  11.313  1.00 48.71           H  
ATOM    420  HA  HIS A  38      47.980  34.063  13.187  1.00 46.94           H  
ATOM    421  HB2 HIS A  38      47.441  33.463  10.461  1.00 42.51           H  
ATOM    422  HB3 HIS A  38      46.395  34.078  11.482  1.00 42.51           H  
ATOM    423  HD2 HIS A  38      47.139  36.793  12.233  1.00 65.72           H  
ATOM    424  HE1 HIS A  38      49.037  37.397   8.789  1.00 67.71           H  
ATOM    425  HE2 HIS A  38      48.124  38.441  10.743  1.00 72.65           H  
ATOM    426  N   GLY A  39      48.589  31.089  12.727  1.00 38.48           N  
ANISOU  426  N   GLY A  39     3992   3474   7153    785    134    -53       N  
ATOM    427  CA  GLY A  39      48.200  29.676  12.877  1.00 37.74           C  
ANISOU  427  CA  GLY A  39     3911   3440   6989    911     46    123       C  
ATOM    428  C   GLY A  39      47.495  29.380  14.176  1.00 37.17           C  
ANISOU  428  C   GLY A  39     3843   3654   6628    937   -306    206       C  
ATOM    429  O   GLY A  39      46.430  28.764  14.125  1.00 42.93           O  
ANISOU  429  O   GLY A  39     4778   4430   7103   1002   -326    284       O  
ATOM    430  H   GLY A  39      49.486  31.227  12.660  1.00 44.58           H  
ATOM    431  HA2 GLY A  39      47.608  29.429  12.124  1.00 43.70           H  
ATOM    432  HA3 GLY A  39      49.013  29.115  12.817  1.00 43.70           H  
ATOM    433  N   GLU A  40      48.018  29.864  15.288  1.00 39.15           N  
ANISOU  433  N   GLU A  40     3873   4107   6897    857   -580    178       N  
ATOM    434  CA  GLU A  40      47.417  29.587  16.607  1.00 39.48           C  
ANISOU  434  CA  GLU A  40     3948   4447   6606    839   -895    259       C  
ATOM    435  C   GLU A  40      46.032  30.232  16.685  1.00 38.60           C  
ANISOU  435  C   GLU A  40     4156   4385   6125    797   -826    120       C  
ATOM    436  O   GLU A  40      45.123  29.575  17.182  1.00 40.11           O  
ANISOU  436  O   GLU A  40     4479   4715   6045    834   -920    217       O  
ATOM    437  CB  GLU A  40      48.319  30.015  17.756  1.00 42.80           C  
ANISOU  437  CB  GLU A  40     4107   5109   7046    695  -1215    213       C  
ATOM    438  CG  GLU A  40      47.840  29.485  19.088  1.00 45.11           C  
ANISOU  438  CG  GLU A  40     4425   5744   6972    655  -1566    370       C  
ATOM    439  CD  GLU A  40      48.855  29.607  20.203  1.00 58.32           C  
ANISOU  439  CD  GLU A  40     5789   7683   8687    514  -1964    419       C  
ATOM    440  OE1 GLU A  40      49.059  28.619  20.930  1.00 64.13           O  
ANISOU  440  OE1 GLU A  40     6451   8661   9254    529  -2292    708       O  
ATOM    441  OE2 GLU A  40      49.417  30.693  20.345  1.00 57.02           O  
ANISOU  441  OE2 GLU A  40     5448   7487   8728    373  -1963    186       O  
ATOM    442  H   GLU A  40      48.748  30.409  15.303  1.00 45.39           H  
ATOM    443  HA  GLU A  40      47.292  28.621  16.674  1.00 45.79           H  
ATOM    444  HB2 GLU A  40      49.227  29.687  17.586  1.00 49.77           H  
ATOM    445  HB3 GLU A  40      48.347  30.994  17.789  1.00 49.77           H  
ATOM    446  HG2 GLU A  40      47.031  29.972  19.352  1.00 54.45           H  
ATOM    447  HG3 GLU A  40      47.598  28.539  18.991  1.00 54.45           H  
ATOM    448  N   ARG A  41      45.882  31.461  16.209  1.00 36.62           N  
ANISOU  448  N   ARG A  41     4010   3994   5911    722   -639    -90       N  
ATOM    449  CA  ARG A  41      44.587  32.186  16.262  1.00 40.90           C  
ANISOU  449  CA  ARG A  41     4790   4532   6217    700   -562   -203       C  
ATOM    450  C   ARG A  41      43.560  31.519  15.340  1.00 32.82           C  
ANISOU  450  C   ARG A  41     3968   3377   5127    835   -433    -64       C  
ATOM    451  O   ARG A  41      42.441  31.358  15.786  1.00 35.16           O  
ANISOU  451  O   ARG A  41     4389   3743   5227    864   -464    -50       O  
ATOM    452  CB  ARG A  41      44.792  33.677  15.996  1.00 38.48           C  
ANISOU  452  CB  ARG A  41     4502   4070   6048    591   -399   -427       C  
ATOM    453  CG  ARG A  41      45.539  34.400  17.106  1.00 56.70           C  
ANISOU  453  CG  ARG A  41     6637   6537   8372    399   -534   -651       C  
ATOM    454  CD  ARG A  41      44.822  35.666  17.517  1.00 55.18           C  
ANISOU  454  CD  ARG A  41     6564   6308   8093    277   -417   -913       C  
ATOM    455  NE  ARG A  41      44.833  36.637  16.432  1.00 74.49           N  
ANISOU  455  NE  ARG A  41     9067   8420  10816    292   -137   -980       N  
ATOM    456  CZ  ARG A  41      44.052  37.713  16.330  1.00 63.72           C  
ANISOU  456  CZ  ARG A  41     7833   6880   9497    296     47  -1078       C  
ATOM    457  NH1 ARG A  41      43.136  37.993  17.245  1.00 59.62           N  
ANISOU  457  NH1 ARG A  41     7394   6480   8778    273     22  -1176       N  
ATOM    458  NH2 ARG A  41      44.186  38.507  15.282  1.00 58.51           N  
ANISOU  458  NH2 ARG A  41     7214   5901   9117    321    278  -1059       N  
ATOM    459  H   ARG A  41      46.553  31.913  15.792  1.00 42.35           H  
ATOM    460  HA  ARG A  41      44.249  32.095  17.180  1.00 49.40           H  
ATOM    461  HB2 ARG A  41      45.289  33.782  15.157  1.00 46.49           H  
ATOM    462  HB3 ARG A  41      43.913  34.093  15.875  1.00 46.49           H  
ATOM    463  HG2 ARG A  41      45.622  33.812  17.886  1.00 68.36           H  
ATOM    464  HG3 ARG A  41      46.443  34.625  16.798  1.00 68.36           H  
ATOM    465  HD2 ARG A  41      43.898  35.446  17.760  1.00 66.53           H  
ATOM    466  HD3 ARG A  41      45.263  36.050  18.305  1.00 66.53           H  
ATOM    467  HE  ARG A  41      45.415  36.511  15.796  1.00 89.71           H  
ATOM    468 HH11 ARG A  41      43.028  37.487  17.949  1.00 71.86           H  
ATOM    469 HH12 ARG A  41      42.633  38.707  17.151  1.00 71.86           H  
ATOM    470 HH21 ARG A  41      44.787  38.329  14.664  1.00 70.54           H  
ATOM    471 HH22 ARG A  41      43.676  39.215  15.200  1.00 70.54           H  
ATOM    472  N   LEU A  42      43.949  31.109  14.136  1.00 32.32           N  
ANISOU  472  N   LEU A  42     3932   3124   5222    892   -275     18       N  
ATOM    473  CA  LEU A  42      43.029  30.460  13.177  1.00 37.81           C  
ANISOU  473  CA  LEU A  42     4825   3726   5813    971   -184    122       C  
ATOM    474  C   LEU A  42      42.539  29.140  13.757  1.00 39.63           C  
ANISOU  474  C   LEU A  42     5032   4078   5947   1045   -301    249       C  
ATOM    475  O   LEU A  42      41.335  28.934  13.741  1.00 31.89           O  
ANISOU  475  O   LEU A  42     4179   3129   4808   1076   -329    279       O  
ATOM    476  CB  LEU A  42      43.719  30.248  11.830  1.00 37.76           C  
ANISOU  476  CB  LEU A  42     4882   3522   5945    960     39    146       C  
ATOM    477  CG  LEU A  42      42.903  29.512  10.765  1.00 49.79           C  
ANISOU  477  CG  LEU A  42     6626   4972   7320    981    128    216       C  
ATOM    478  CD1 LEU A  42      41.621  30.262  10.435  1.00 38.89           C  
ANISOU  478  CD1 LEU A  42     5435   3597   5744    973     55    238       C  
ATOM    479  CD2 LEU A  42      43.723  29.283   9.506  1.00 34.23           C  
ANISOU  479  CD2 LEU A  42     4743   2820   5441    916    402    189       C  
ATOM    480  H   LEU A  42      44.806  31.187  13.843  1.00 39.10           H  
ATOM    481  HA  LEU A  42      42.254  31.046  13.055  1.00 45.69           H  
ATOM    482  HB2 LEU A  42      43.971  31.124  11.476  1.00 45.64           H  
ATOM    483  HB3 LEU A  42      44.544  29.746  11.985  1.00 45.64           H  
ATOM    484  HG  LEU A  42      42.653  28.625  11.124  1.00 60.07           H  
ATOM    485 HD11 LEU A  42      41.208  29.873   9.645  1.00 46.99           H  
ATOM    486 HD12 LEU A  42      41.007  30.196  11.183  1.00 46.99           H  
ATOM    487 HD13 LEU A  42      41.823  31.198  10.264  1.00 46.99           H  
ATOM    488 HD21 LEU A  42      43.202  28.769   8.865  1.00 41.39           H  
ATOM    489 HD22 LEU A  42      43.962  30.141   9.114  1.00 41.39           H  
ATOM    490 HD23 LEU A  42      44.533  28.793   9.729  1.00 41.39           H  
ATOM    491  N   SER A  43      43.438  28.328  14.312  1.00 38.26           N  
ANISOU  491  N   SER A  43     4667   3948   5921   1077   -365    347       N  
ATOM    492  CA  SER A  43      43.096  26.991  14.843  1.00 38.51           C  
ANISOU  492  CA  SER A  43     4671   4043   5917   1157   -444    519       C  
ATOM    493  C   SER A  43      42.144  27.139  16.023  1.00 37.01           C  
ANISOU  493  C   SER A  43     4549   4067   5447   1134   -608    538       C  
ATOM    494  O   SER A  43      41.141  26.428  16.056  1.00 39.26           O  
ANISOU  494  O   SER A  43     4937   4352   5629   1177   -581    612       O  
ATOM    495  CB  SER A  43      44.333  26.224  15.215  1.00 37.84           C  
ANISOU  495  CB  SER A  43     4316   3948   6111   1210   -514    677       C  
ATOM    496  OG  SER A  43      44.953  26.778  16.356  1.00 54.06           O  
ANISOU  496  OG  SER A  43     6200   6218   8122   1147   -768    694       O  
ATOM    497  H   SER A  43      44.314  28.544  14.424  1.00 46.22           H  
ATOM    498  HA  SER A  43      42.623  26.489  14.126  1.00 46.53           H  
ATOM    499  HB2 SER A  43      44.091  25.289  15.397  1.00 45.72           H  
ATOM    500  HB3 SER A  43      44.965  26.233  14.460  1.00 45.72           H  
ATOM    501  HG  SER A  43      45.452  27.406  16.109  1.00 65.19           H  
ATOM    502  N   GLN A  44      42.427  28.058  16.929  1.00 36.95           N  
ANISOU  502  N   GLN A  44     4489   4234   5317   1037   -744    440       N  
ATOM    503  CA  GLN A  44      41.598  28.242  18.142  1.00 43.65           C  
ANISOU  503  CA  GLN A  44     5427   5294   5865    970   -843    421       C  
ATOM    504  C   GLN A  44      40.203  28.775  17.792  1.00 38.84           C  
ANISOU  504  C   GLN A  44     4992   4593   5173    969   -681    279       C  
ATOM    505  O   GLN A  44      39.254  28.280  18.381  1.00 41.34           O  
ANISOU  505  O   GLN A  44     5394   4973   5341    976   -656    325       O  
ATOM    506  CB  GLN A  44      42.348  29.079  19.173  1.00 37.71           C  
ANISOU  506  CB  GLN A  44     4595   4758   4974    811  -1008    291       C  
ATOM    507  CG  GLN A  44      43.499  28.314  19.812  1.00 46.74           C  
ANISOU  507  CG  GLN A  44     5538   6078   6142    801  -1276    508       C  
ATOM    508  CD  GLN A  44      44.300  29.124  20.798  1.00 41.64           C  
ANISOU  508  CD  GLN A  44     4791   5668   5364    600  -1488    349       C  
ATOM    509  OE1 GLN A  44      43.874  30.171  21.267  1.00 49.48           O  
ANISOU  509  OE1 GLN A  44     5907   6713   6179    445  -1402     50       O  
ATOM    510  NE2 GLN A  44      45.474  28.624  21.141  1.00 59.88           N  
ANISOU  510  NE2 GLN A  44     6850   8104   7799    591  -1766    542       N  
ATOM    511  H   GLN A  44      43.114  28.649  16.838  1.00 44.66           H  
ATOM    512  HA  GLN A  44      41.470  27.348  18.535  1.00 52.70           H  
ATOM    513  HB2 GLN A  44      42.693  29.887  18.738  1.00 45.57           H  
ATOM    514  HB3 GLN A  44      41.716  29.355  19.869  1.00 45.57           H  
ATOM    515  HG2 GLN A  44      43.138  27.527  20.273  1.00 56.40           H  
ATOM    516  HG3 GLN A  44      44.098  27.992  19.106  1.00 56.40           H  
ATOM    517 HE21 GLN A  44      45.725  27.832  20.839  1.00 72.18           H  
ATOM    518 HE22 GLN A  44      46.010  29.082  21.674  1.00 72.18           H  
ATOM    519  N   LEU A  45      40.093  29.741  16.886  1.00 39.68           N  
ANISOU  519  N   LEU A  45     5132   4533   5409    960   -565    133       N  
ATOM    520  CA  LEU A  45      38.787  30.312  16.469  1.00 46.98           C  
ANISOU  520  CA  LEU A  45     6167   5338   6345    987   -450     67       C  
ATOM    521  C   LEU A  45      38.021  29.210  15.734  1.00 42.00           C  
ANISOU  521  C   LEU A  45     5596   4621   5740   1082   -432    218       C  
ATOM    522  O   LEU A  45      36.817  29.113  15.936  1.00 35.58           O  
ANISOU  522  O   LEU A  45     4821   3786   4911   1102   -400    215       O  
ATOM    523  CB  LEU A  45      38.984  31.581  15.628  1.00 29.63           C  
ANISOU  523  CB  LEU A  45     3986   2960   4314    969   -354    -39       C  
ATOM    524  CG  LEU A  45      37.716  32.303  15.173  1.00 40.08           C  
ANISOU  524  CG  LEU A  45     5369   4124   5736   1014   -273    -51       C  
ATOM    525  CD1 LEU A  45      36.792  32.626  16.337  1.00 38.57           C  
ANISOU  525  CD1 LEU A  45     5151   3987   5517    969   -203   -199       C  
ATOM    526  CD2 LEU A  45      38.078  33.573  14.428  1.00 39.63           C  
ANISOU  526  CD2 LEU A  45     5329   3866   5863   1005   -189    -73       C  
ATOM    527  H   LEU A  45      40.812  30.089  16.448  1.00 47.93           H  
ATOM    528  HA  LEU A  45      38.289  30.541  17.286  1.00 56.69           H  
ATOM    529  HB2 LEU A  45      39.524  32.209  16.147  1.00 33.97           H  
ATOM    530  HB3 LEU A  45      39.500  31.341  14.833  1.00 33.97           H  
ATOM    531  HG  LEU A  45      37.229  31.711  14.549  1.00 48.42           H  
ATOM    532 HD11 LEU A  45      36.079  33.211  16.028  1.00 46.60           H  
ATOM    533 HD12 LEU A  45      36.404  31.807  16.687  1.00 46.60           H  
ATOM    534 HD13 LEU A  45      37.295  33.075  17.038  1.00 46.60           H  
ATOM    535 HD21 LEU A  45      37.280  33.943  14.012  1.00 47.88           H  
ATOM    536 HD22 LEU A  45      38.449  34.221  15.050  1.00 47.88           H  
ATOM    537 HD23 LEU A  45      38.736  33.372  13.740  1.00 47.88           H  
ATOM    538  N   TRP A  46      38.724  28.400  14.949  1.00 40.65           N  
ANISOU  538  N   TRP A  46     5416   4384   5645   1120   -426    320       N  
ATOM    539  CA  TRP A  46      38.119  27.288  14.175  1.00 45.35           C  
ANISOU  539  CA  TRP A  46     6078   4894   6259   1163   -386    407       C  
ATOM    540  C   TRP A  46      37.509  26.256  15.123  1.00 42.13           C  
ANISOU  540  C   TRP A  46     5638   4573   5796   1191   -412    501       C  
ATOM    541  O   TRP A  46      36.350  25.907  14.900  1.00 32.98           O  
ANISOU  541  O   TRP A  46     4525   3373   4634   1197   -386    506       O  
ATOM    542  CB  TRP A  46      39.164  26.711  13.227  1.00 39.41           C  
ANISOU  542  CB  TRP A  46     5324   4026   5623   1164   -296    439       C  
ATOM    543  CG  TRP A  46      38.784  25.516  12.412  1.00 49.35           C  
ANISOU  543  CG  TRP A  46     6657   5182   6911   1163   -207    470       C  
ATOM    544  CD1 TRP A  46      37.548  24.989  12.188  1.00 44.89           C  
ANISOU  544  CD1 TRP A  46     6166   4614   6275   1148   -235    469       C  
ATOM    545  CD2 TRP A  46      39.701  24.698  11.671  1.00 44.84           C  
ANISOU  545  CD2 TRP A  46     6075   4470   6491   1151    -41    467       C  
ATOM    546  NE1 TRP A  46      37.639  23.899  11.374  1.00 38.23           N  
ANISOU  546  NE1 TRP A  46     5379   3655   5492   1107   -114    447       N  
ATOM    547  CE2 TRP A  46      38.946  23.694  11.038  1.00 39.57           C  
ANISOU  547  CE2 TRP A  46     5509   3725   5800   1109     34    436       C  
ATOM    548  CE3 TRP A  46      41.086  24.715  11.491  1.00 45.36           C  
ANISOU  548  CE3 TRP A  46     6032   4445   6758   1159     80    464       C  
ATOM    549  CZ2 TRP A  46      39.528  22.718  10.237  1.00 36.82           C  
ANISOU  549  CZ2 TRP A  46     5188   3203   5599   1062    259    374       C  
ATOM    550  CZ3 TRP A  46      41.659  23.759  10.691  1.00 40.27           C  
ANISOU  550  CZ3 TRP A  46     5389   3611   6300   1137    315    426       C  
ATOM    551  CH2 TRP A  46      40.890  22.771  10.079  1.00 44.65           C  
ANISOU  551  CH2 TRP A  46     6076   4082   6805   1083    419    369       C  
ATOM    552  H   TRP A  46      39.624  28.472  14.846  1.00 49.10           H  
ATOM    553  HA  TRP A  46      37.396  27.670  13.624  1.00 54.74           H  
ATOM    554  HB2 TRP A  46      39.429  27.425  12.611  1.00 47.61           H  
ATOM    555  HB3 TRP A  46      39.951  26.478  13.754  1.00 47.61           H  
ATOM    556  HD1 TRP A  46      36.745  25.315  12.542  1.00 54.18           H  
ATOM    557  HE1 TRP A  46      36.975  23.411  11.121  1.00 46.19           H  
ATOM    558  HE3 TRP A  46      41.614  25.384  11.897  1.00 54.75           H  
ATOM    559  HZ2 TRP A  46      39.008  22.053   9.821  1.00 44.50           H  
ATOM    560  HZ3 TRP A  46      42.589  23.768  10.558  1.00 48.64           H  
ATOM    561  HH2 TRP A  46      41.311  22.129   9.545  1.00 53.89           H  
ATOM    562  N   ARG A  47      38.200  25.875  16.194  1.00 32.64           N  
ANISOU  562  N   ARG A  47     4350   3493   4559   1197   -477    598       N  
ATOM    563  CA  ARG A  47      37.628  24.926  17.173  1.00 41.81           C  
ANISOU  563  CA  ARG A  47     5513   4741   5632   1210   -488    732       C  
ATOM    564  C   ARG A  47      36.439  25.563  17.882  1.00 37.82           C  
ANISOU  564  C   ARG A  47     5081   4324   4967   1150   -449    621       C  
ATOM    565  O   ARG A  47      35.422  24.900  17.979  1.00 34.03           O  
ANISOU  565  O   ARG A  47     4631   3802   4497   1158   -363    655       O  
ATOM    566  CB  ARG A  47      38.639  24.414  18.204  1.00 34.38           C  
ANISOU  566  CB  ARG A  47     4473   3939   4649   1218   -617    927       C  
ATOM    567  CG  ARG A  47      38.134  23.239  19.034  1.00 47.78           C  
ANISOU  567  CG  ARG A  47     6201   5706   6246   1231   -614   1146       C  
ATOM    568  CD  ARG A  47      38.129  21.923  18.270  1.00 61.70           C  
ANISOU  568  CD  ARG A  47     7904   7246   8291   1332   -504   1314       C  
ATOM    569  NE  ARG A  47      37.155  20.926  18.709  1.00 67.63           N  
ANISOU  569  NE  ARG A  47     8721   7956   9019   1334   -391   1434       N  
ATOM    570  CZ  ARG A  47      37.227  20.182  19.817  1.00 68.71           C  
ANISOU  570  CZ  ARG A  47     8861   8190   9054   1340   -435   1716       C  
ATOM    571  NH1 ARG A  47      38.215  20.332  20.685  1.00 66.39           N  
ANISOU  571  NH1 ARG A  47     8501   8079   8645   1340   -653   1924       N  
ATOM    572  NH2 ARG A  47      36.279  19.296  20.075  1.00 64.30           N  
ANISOU  572  NH2 ARG A  47     8368   7551   8514   1331   -274   1809       N  
ATOM    573  H   ARG A  47      39.027  26.194  16.400  1.00 39.49           H  
ATOM    574  HA  ARG A  47      37.291  24.155  16.666  1.00 50.49           H  
ATOM    575  HB2 ARG A  47      39.454  24.140  17.733  1.00 41.57           H  
ATOM    576  HB3 ARG A  47      38.873  25.150  18.806  1.00 41.57           H  
ATOM    577  HG2 ARG A  47      38.705  23.142  19.824  1.00 57.65           H  
ATOM    578  HG3 ARG A  47      37.224  23.424  19.348  1.00 57.65           H  
ATOM    579  HD2 ARG A  47      37.964  22.112  17.325  1.00 74.35           H  
ATOM    580  HD3 ARG A  47      39.021  21.530  18.325  1.00 74.35           H  
ATOM    581  HE  ARG A  47      36.484  20.773  18.173  1.00 81.47           H  
ATOM    582 HH11 ARG A  47      38.855  20.907  20.546  1.00 79.99           H  
ATOM    583 HH12 ARG A  47      38.236  19.838  21.402  1.00 79.99           H  
ATOM    584 HH21 ARG A  47      35.614  19.180  19.511  1.00 77.48           H  
ATOM    585 HH22 ARG A  47      36.316  18.812  20.810  1.00 77.48           H  
ATOM    586  N   ARG A  48      36.561  26.806  18.326  1.00 42.13           N  
ANISOU  586  N   ARG A  48     5638   4962   5408   1075   -468    462       N  
ATOM    587  CA  ARG A  48      35.476  27.448  19.097  1.00 39.16           C  
ANISOU  587  CA  ARG A  48     5316   4621   4942   1010   -350    323       C  
ATOM    588  C   ARG A  48      34.238  27.513  18.211  1.00 37.99           C  
ANISOU  588  C   ARG A  48     5148   4280   5006   1072   -255    281       C  
ATOM    589  O   ARG A  48      33.162  27.162  18.688  1.00 34.50           O  
ANISOU  589  O   ARG A  48     4702   3821   4583   1059   -140    270       O  
ATOM    590  CB  ARG A  48      35.852  28.858  19.548  1.00 47.56           C  
ANISOU  590  CB  ARG A  48     6394   5754   5923    898   -315     93       C  
ATOM    591  CG  ARG A  48      36.721  28.934  20.794  1.00 59.79           C  
ANISOU  591  CG  ARG A  48     7987   7563   7166    760   -400     79       C  
ATOM    592  CD  ARG A  48      36.470  30.149  21.670  1.00 76.73           C  
ANISOU  592  CD  ARG A  48    10174   9745   9236    604   -279   -234       C  
ATOM    593  NE  ARG A  48      37.089  31.365  21.148  1.00 71.03           N  
ANISOU  593  NE  ARG A  48     9388   8929   8670    560   -277   -434       N  
ATOM    594  CZ  ARG A  48      36.523  32.291  20.368  1.00 76.09           C  
ANISOU  594  CZ  ARG A  48     9996   9322   9593    594    -93   -603       C  
ATOM    595  NH1 ARG A  48      35.265  32.205  19.959  1.00 77.96           N  
ANISOU  595  NH1 ARG A  48    10217   9373  10030    704     49   -562       N  
ATOM    596  NH2 ARG A  48      37.243  33.334  19.993  1.00 70.65           N  
ANISOU  596  NH2 ARG A  48     9259   8544   9041    523    -59   -789       N  
ATOM    597  H   ARG A  48      37.299  27.320  18.185  1.00 50.88           H  
ATOM    598  HA  ARG A  48      35.277  26.894  19.885  1.00 47.31           H  
ATOM    599  HB2 ARG A  48      36.318  29.310  18.813  1.00 57.39           H  
ATOM    600  HB3 ARG A  48      35.023  29.347  19.714  1.00 57.39           H  
ATOM    601  HG2 ARG A  48      36.584  28.126  21.332  1.00 72.06           H  
ATOM    602  HG3 ARG A  48      37.659  28.949  20.517  1.00 72.06           H  
ATOM    603  HD2 ARG A  48      35.506  30.282  21.780  1.00 92.40           H  
ATOM    604  HD3 ARG A  48      36.840  29.970  22.560  1.00 92.40           H  
ATOM    605  HE  ARG A  48      37.921  31.498  21.371  1.00 85.55           H  
ATOM    606 HH11 ARG A  48      34.758  31.538  20.187  1.00 93.87           H  
ATOM    607 HH12 ARG A  48      34.933  32.837  19.447  1.00 93.87           H  
ATOM    608 HH21 ARG A  48      38.082  33.413  20.250  1.00 85.10           H  
ATOM    609 HH22 ARG A  48      36.888  33.951  19.480  1.00 85.10           H  
ATOM    610  N   LYS A  49      34.407  27.896  16.954  1.00 33.25           N  
ANISOU  610  N   LYS A  49     4529   3538   4565   1124   -308    271       N  
ATOM    611  CA  LYS A  49      33.270  28.048  16.023  1.00 38.72           C  
ANISOU  611  CA  LYS A  49     5188   4084   5440   1163   -300    266       C  
ATOM    612  C   LYS A  49      32.653  26.686  15.715  1.00 35.48           C  
ANISOU  612  C   LYS A  49     4773   3646   5060   1178   -316    369       C  
ATOM    613  O   LYS A  49      31.433  26.625  15.621  1.00 33.05           O  
ANISOU  613  O   LYS A  49     4393   3273   4892   1180   -294    356       O  
ATOM    614  CB  LYS A  49      33.677  28.856  14.790  1.00 37.40           C  
ANISOU  614  CB  LYS A  49     5045   3802   5362   1186   -379    275       C  
ATOM    615  CG  LYS A  49      33.653  30.367  14.975  1.00 39.60           C  
ANISOU  615  CG  LYS A  49     5285   4007   5755   1179   -316    166       C  
ATOM    616  CD  LYS A  49      32.331  30.886  15.508  1.00 48.38           C  
ANISOU  616  CD  LYS A  49     6285   5032   7067   1197   -218     97       C  
ATOM    617  CE  LYS A  49      32.003  32.297  15.088  1.00 48.58           C  
ANISOU  617  CE  LYS A  49     6233   4854   7371   1239   -189     83       C  
ATOM    618  NZ  LYS A  49      30.783  32.800  15.757  1.00 53.86           N  
ANISOU  618  NZ  LYS A  49     6743   5393   8328   1258    -19    -23       N  
ATOM    619  H   LYS A  49      35.224  28.047  16.589  1.00 40.22           H  
ATOM    620  HA  LYS A  49      32.586  28.554  16.504  1.00 46.78           H  
ATOM    621  HB2 LYS A  49      34.577  28.586  14.515  1.00 45.19           H  
ATOM    622  HB3 LYS A  49      33.066  28.625  14.059  1.00 45.19           H  
ATOM    623  HG2 LYS A  49      34.369  30.621  15.594  1.00 47.84           H  
ATOM    624  HG3 LYS A  49      33.839  30.790  14.112  1.00 47.84           H  
ATOM    625  HD2 LYS A  49      31.610  30.294  15.204  1.00 58.38           H  
ATOM    626  HD3 LYS A  49      32.354  30.852  16.487  1.00 58.38           H  
ATOM    627  HE2 LYS A  49      32.748  32.882  15.312  1.00 58.61           H  
ATOM    628  HE3 LYS A  49      31.866  32.326  14.124  1.00 58.61           H  
ATOM    629  HZ1 LYS A  49      30.086  32.248  15.583  1.00 64.95           H  
ATOM    630  HZ2 LYS A  49      30.917  32.837  16.653  1.00 64.95           H  
ATOM    631  HZ3 LYS A  49      30.589  33.632  15.452  1.00 64.95           H  
ATOM    632  N   GLN A  50      33.462  25.643  15.586  1.00 42.19           N  
ANISOU  632  N   GLN A  50     5668   4519   5845   1183   -335    459       N  
ATOM    633  CA  GLN A  50      32.983  24.276  15.276  1.00 37.81           C  
ANISOU  633  CA  GLN A  50     5105   3904   5355   1179   -294    529       C  
ATOM    634  C   GLN A  50      32.039  23.847  16.387  1.00 34.79           C  
ANISOU  634  C   GLN A  50     4676   3556   4987   1165   -188    555       C  
ATOM    635  O   GLN A  50      30.938  23.405  16.064  1.00 29.47           O  
ANISOU  635  O   GLN A  50     3942   2798   4456   1142   -149    528       O  
ATOM    636  CB  GLN A  50      34.189  23.355  15.125  1.00 38.65           C  
ANISOU  636  CB  GLN A  50     5232   3991   5464   1201   -265    630       C  
ATOM    637  CG  GLN A  50      33.871  21.902  14.810  1.00 39.40           C  
ANISOU  637  CG  GLN A  50     5318   3959   5694   1187   -168    677       C  
ATOM    638  CD  GLN A  50      35.105  21.038  14.927  1.00 48.31           C  
ANISOU  638  CD  GLN A  50     6410   5018   6927   1237    -94    813       C  
ATOM    639  OE1 GLN A  50      35.865  21.127  15.885  1.00 48.21           O  
ANISOU  639  OE1 GLN A  50     6345   5108   6866   1291   -147    965       O  
ATOM    640  NE2 GLN A  50      35.309  20.169  13.957  1.00 48.35           N  
ANISOU  640  NE2 GLN A  50     6430   4844   7095   1205     26    756       N  
ATOM    641  H   GLN A  50      34.364  25.710  15.681  1.00 50.95           H  
ATOM    642  HA  GLN A  50      32.487  24.300  14.425  1.00 45.69           H  
ATOM    643  HB2 GLN A  50      34.758  23.710  14.411  1.00 46.70           H  
ATOM    644  HB3 GLN A  50      34.703  23.390  15.956  1.00 46.70           H  
ATOM    645  HG2 GLN A  50      33.188  21.571  15.429  1.00 47.60           H  
ATOM    646  HG3 GLN A  50      33.511  21.839  13.899  1.00 47.60           H  
ATOM    647 HE21 GLN A  50      34.626  19.820  13.528  1.00 58.33           H  
ATOM    648 HE22 GLN A  50      36.127  19.924  13.747  1.00 58.33           H  
ATOM    649  N   ILE A  51      32.431  24.058  17.635  1.00 30.04           N  
ANISOU  649  N   ILE A  51     4104   3086   4223   1153   -138    600       N  
ATOM    650  CA  ILE A  51      31.595  23.664  18.796  1.00 34.82           C  
ANISOU  650  CA  ILE A  51     4717   3737   4777   1107     15    631       C  
ATOM    651  C   ILE A  51      30.338  24.540  18.817  1.00 33.87           C  
ANISOU  651  C   ILE A  51     4520   3544   4807   1080    121    455       C  
ATOM    652  O   ILE A  51      29.263  23.972  18.985  1.00 34.79           O  
ANISOU  652  O   ILE A  51     4559   3567   5093   1061    245    449       O  
ATOM    653  CB  ILE A  51      32.369  23.720  20.128  1.00 32.50           C  
ANISOU  653  CB  ILE A  51     4519   3650   4180   1052     16    710       C  
ATOM    654  CG1 ILE A  51      33.667  22.904  20.113  1.00 47.38           C  
ANISOU  654  CG1 ILE A  51     6402   5586   6016   1105   -141    924       C  
ATOM    655  CG2 ILE A  51      31.474  23.316  21.291  1.00 38.74           C  
ANISOU  655  CG2 ILE A  51     5376   4496   4850    974    215    774       C  
ATOM    656  CD1 ILE A  51      33.567  21.553  19.457  1.00 50.07           C  
ANISOU  656  CD1 ILE A  51     6697   5762   6564   1173    -87   1108       C  
ATOM    657  H   ILE A  51      33.199  24.495  17.850  1.00 36.36           H  
ATOM    658  HA  ILE A  51      31.308  22.747  18.657  1.00 42.11           H  
ATOM    659  HB  ILE A  51      32.625  24.664  20.273  1.00 38.19           H  
ATOM    660 HG12 ILE A  51      34.356  23.421  19.655  1.00 57.18           H  
ATOM    661 HG13 ILE A  51      33.966  22.775  21.038  1.00 57.18           H  
ATOM    662 HG21 ILE A  51      32.006  23.228  22.101  1.00 46.81           H  
ATOM    663 HG22 ILE A  51      30.792  23.994  21.432  1.00 46.81           H  
ATOM    664 HG23 ILE A  51      31.047  22.464  21.095  1.00 46.81           H  
ATOM    665 HD11 ILE A  51      34.337  21.023  19.704  1.00 60.40           H  
ATOM    666 HD12 ILE A  51      32.758  21.101  19.755  1.00 60.40           H  
ATOM    667 HD13 ILE A  51      33.543  21.656  18.490  1.00 60.40           H  
ATOM    668  N   GLU A  52      30.459  25.852  18.604  1.00 31.24           N  
ANISOU  668  N   GLU A  52     4172   3217   4480   1077     96    313       N  
ATOM    669  CA  GLU A  52      29.306  26.785  18.709  1.00 38.35           C  
ANISOU  669  CA  GLU A  52     4954   4001   5615   1069    231    161       C  
ATOM    670  C   GLU A  52      28.274  26.436  17.644  1.00 32.44           C  
ANISOU  670  C   GLU A  52     4045   3093   5189   1121    139    201       C  
ATOM    671  O   GLU A  52      27.113  26.336  17.991  1.00 33.65           O  
ANISOU  671  O   GLU A  52     4050   3145   5592   1107    281    148       O  
ATOM    672  CB  GLU A  52      29.764  28.230  18.549  1.00 34.22           C  
ANISOU  672  CB  GLU A  52     4425   3450   5128   1073    218     23       C  
ATOM    673  CG  GLU A  52      28.703  29.258  18.896  1.00 46.87           C  
ANISOU  673  CG  GLU A  52     5882   4887   7039   1067    427   -144       C  
ATOM    674  CD  GLU A  52      28.971  30.671  18.403  1.00 60.78           C  
ANISOU  674  CD  GLU A  52     7579   6510   9004   1117    377   -213       C  
ATOM    675  OE1 GLU A  52      28.134  31.552  18.670  1.00 65.03           O  
ANISOU  675  OE1 GLU A  52     7958   6853   9898   1137    558   -331       O  
ATOM    676  OE2 GLU A  52      30.005  30.891  17.754  1.00 45.93           O  
ANISOU  676  OE2 GLU A  52     5789   4681   6979   1138    190   -140       O  
ATOM    677  H   GLU A  52      31.244  26.244  18.359  1.00 37.80           H  
ATOM    678  HA  GLU A  52      28.895  26.676  19.597  1.00 46.34           H  
ATOM    679  HB2 GLU A  52      30.545  28.376  19.122  1.00 41.39           H  
ATOM    680  HB3 GLU A  52      30.045  28.361  17.619  1.00 41.39           H  
ATOM    681  HG2 GLU A  52      27.847  28.966  18.529  1.00 56.56           H  
ATOM    682  HG3 GLU A  52      28.605  29.289  19.871  1.00 56.56           H  
ATOM    683  N   TYR A  53      28.711  26.192  16.421  1.00 30.86           N  
ANISOU  683  N   TYR A  53     3867   2872   4985   1157    -92    283       N  
ATOM    684  CA  TYR A  53      27.811  25.897  15.288  1.00 31.36           C  
ANISOU  684  CA  TYR A  53     3803   2835   5278   1160   -247    317       C  
ATOM    685  C   TYR A  53      27.065  24.585  15.521  1.00 38.81           C  
ANISOU  685  C   TYR A  53     4679   3748   6318   1104   -158    326       C  
ATOM    686  O   TYR A  53      25.864  24.560  15.258  1.00 36.25           O  
ANISOU  686  O   TYR A  53     4155   3331   6288   1085   -170    295       O  
ATOM    687  CB  TYR A  53      28.595  25.918  13.979  1.00 31.63           C  
ANISOU  687  CB  TYR A  53     3956   2891   5173   1151   -473    382       C  
ATOM    688  CG  TYR A  53      29.016  27.266  13.439  1.00 33.13           C  
ANISOU  688  CG  TYR A  53     4167   3050   5371   1196   -587    409       C  
ATOM    689  CD1 TYR A  53      28.833  28.453  14.135  1.00 34.38           C  
ANISOU  689  CD1 TYR A  53     4230   3141   5692   1250   -476    355       C  
ATOM    690  CD2 TYR A  53      29.622  27.343  12.197  1.00 31.19           C  
ANISOU  690  CD2 TYR A  53     4055   2818   4978   1165   -760    480       C  
ATOM    691  CE1 TYR A  53      29.233  29.668  13.609  1.00 33.57           C  
ANISOU  691  CE1 TYR A  53     4138   2961   5658   1293   -546    395       C  
ATOM    692  CE2 TYR A  53      30.033  28.549  11.660  1.00 32.61           C  
ANISOU  692  CE2 TYR A  53     4272   2948   5172   1201   -837    544       C  
ATOM    693  CZ  TYR A  53      29.834  29.718  12.367  1.00 34.85           C  
ANISOU  693  CZ  TYR A  53     4433   3139   5669   1275   -737    515       C  
ATOM    694  OH  TYR A  53      30.231  30.912  11.849  1.00 46.37           O  
ANISOU  694  OH  TYR A  53     5917   4499   7202   1313   -784    594       O  
ATOM    695  H   TYR A  53      29.590  26.151  16.201  1.00 36.63           H  
ATOM    696  HA  TYR A  53      27.128  26.612  15.247  1.00 36.71           H  
ATOM    697  HB2 TYR A  53      29.399  25.371  14.098  1.00 38.28           H  
ATOM    698  HB3 TYR A  53      28.046  25.476  13.299  1.00 38.28           H  
ATOM    699  HD1 TYR A  53      28.428  28.442  14.983  1.00 41.57           H  
ATOM    700  HD2 TYR A  53      29.763  26.551  11.704  1.00 37.75           H  
ATOM    701  HE1 TYR A  53      29.099  30.462  14.099  1.00 40.61           H  
ATOM    702  HE2 TYR A  53      30.442  28.574  10.810  1.00 39.46           H  
ATOM    703  HH  TYR A  53      29.863  31.042  11.086  1.00 55.96           H  
ATOM    704  N   SER A  54      27.738  23.555  16.028  1.00 33.50           N  
ANISOU  704  N   SER A  54     4140   3129   5458   1080    -67    383       N  
ATOM    705  CA  SER A  54      27.112  22.249  16.314  1.00 36.79           C  
ANISOU  705  CA  SER A  54     4501   3477   6001   1024     70    406       C  
ATOM    706  C   SER A  54      26.023  22.463  17.357  1.00 37.06           C  
ANISOU  706  C   SER A  54     4416   3470   6196   1002    307    361       C  
ATOM    707  O   SER A  54      24.926  21.968  17.153  1.00 36.07           O  
ANISOU  707  O   SER A  54     4121   3230   6353    950    381    321       O  
ATOM    708  CB  SER A  54      28.136  21.243  16.777  1.00 35.36           C  
ANISOU  708  CB  SER A  54     4469   3323   5642   1029    161    533       C  
ATOM    709  OG  SER A  54      28.442  21.408  18.146  1.00 35.53           O  
ANISOU  709  OG  SER A  54     4577   3452   5469   1046    304    624       O  
ATOM    710  H   SER A  54      28.618  23.590  16.262  1.00 40.52           H  
ATOM    711  HA  SER A  54      26.688  21.913  15.479  1.00 44.47           H  
ATOM    712  HB2 SER A  54      27.786  20.337  16.631  1.00 42.75           H  
ATOM    713  HB3 SER A  54      28.956  21.338  16.242  1.00 42.75           H  
ATOM    714  HG  SER A  54      29.152  21.857  18.208  1.00 42.95           H  
ATOM    715  N   GLN A  55      26.320  23.220  18.402  1.00 34.57           N  
ANISOU  715  N   GLN A  55     4180   3239   5715   1013    454    336       N  
ATOM    716  CA  GLN A  55      25.369  23.465  19.511  1.00 37.08           C  
ANISOU  716  CA  GLN A  55     4428   3511   6148    956    767    254       C  
ATOM    717  C   GLN A  55      24.200  24.344  19.049  1.00 40.91           C  
ANISOU  717  C   GLN A  55     4644   3840   7058    980    788    112       C  
ATOM    718  O   GLN A  55      23.086  24.067  19.478  1.00 44.46           O  
ANISOU  718  O   GLN A  55     4928   4169   7796    932   1044     38       O  
ATOM    719  CB  GLN A  55      26.124  24.013  20.718  1.00 38.09           C  
ANISOU  719  CB  GLN A  55     4763   3800   5908    905    933    229       C  
ATOM    720  CG  GLN A  55      27.058  22.994  21.356  1.00 49.28           C  
ANISOU  720  CG  GLN A  55     6404   5381   6942    880    895    435       C  
ATOM    721  CD  GLN A  55      27.895  23.574  22.468  1.00 58.44           C  
ANISOU  721  CD  GLN A  55     7769   6751   7686    780   1006    412       C  
ATOM    722  OE1 GLN A  55      27.842  24.766  22.756  1.00 52.06           O  
ANISOU  722  OE1 GLN A  55     6958   5959   6864    724   1119    186       O  
ATOM    723  NE2 GLN A  55      28.685  22.725  23.104  1.00 49.02           N  
ANISOU  723  NE2 GLN A  55     6749   5714   6164    742    967    651       N  
ATOM    724  H   GLN A  55      27.110  23.666  18.475  1.00 39.89           H  
ATOM    725  HA  GLN A  55      24.994  22.592  19.769  1.00 44.81           H  
ATOM    726  HB2 GLN A  55      26.640  24.796  20.434  1.00 46.02           H  
ATOM    727  HB3 GLN A  55      25.469  24.309  21.383  1.00 46.02           H  
ATOM    728  HG2 GLN A  55      26.525  22.253  21.713  1.00 59.46           H  
ATOM    729  HG3 GLN A  55      27.653  22.627  20.670  1.00 59.46           H  
ATOM    730 HE21 GLN A  55      28.772  21.895  22.813  1.00 59.15           H  
ATOM    731 HE22 GLN A  55      29.137  22.990  23.817  1.00 59.15           H  
ATOM    732  N   LEU A  56      24.447  25.359  18.231  1.00 37.10           N  
ANISOU  732  N   LEU A  56     4094   3335   6666   1057    540     95       N  
ATOM    733  CA  LEU A  56      23.402  26.301  17.773  1.00 45.01           C  
ANISOU  733  CA  LEU A  56     4798   4159   8143   1106    525     29       C  
ATOM    734  C   LEU A  56      22.423  25.577  16.857  1.00 48.71           C  
ANISOU  734  C   LEU A  56     5018   4537   8951   1093    323     91       C  
ATOM    735  O   LEU A  56      21.226  25.780  17.019  1.00 47.57           O  
ANISOU  735  O   LEU A  56     4560   4230   9286   1097    426     39       O  
ATOM    736  CB  LEU A  56      24.022  27.508  17.069  1.00 39.41           C  
ANISOU  736  CB  LEU A  56     4099   3433   7441   1193    310     57       C  
ATOM    737  CG  LEU A  56      24.690  28.558  17.955  1.00 53.33           C  
ANISOU  737  CG  LEU A  56     5995   5211   9058   1187    541    -78       C  
ATOM    738  CD1 LEU A  56      25.476  29.538  17.099  1.00 45.55           C  
ANISOU  738  CD1 LEU A  56     5064   4214   8028   1261    292     -8       C  
ATOM    739  CD2 LEU A  56      23.679  29.296  18.819  1.00 58.98           C  
ANISOU  739  CD2 LEU A  56     6504   5732  10173   1175    909   -259       C  
ATOM    740  H   LEU A  56      25.271  25.513  17.881  1.00 44.36           H  
ATOM    741  HA  LEU A  56      22.906  26.608  18.564  1.00 54.33           H  
ATOM    742  HB2 LEU A  56      24.684  27.180  16.428  1.00 47.61           H  
ATOM    743  HB3 LEU A  56      23.318  27.948  16.554  1.00 47.61           H  
ATOM    744  HG  LEU A  56      25.324  28.097  18.556  1.00 64.32           H  
ATOM    745 HD11 LEU A  56      25.861  30.229  17.664  1.00 54.98           H  
ATOM    746 HD12 LEU A  56      26.190  29.065  16.635  1.00 54.98           H  
ATOM    747 HD13 LEU A  56      24.882  29.948  16.447  1.00 54.98           H  
ATOM    748 HD21 LEU A  56      24.118  30.036  19.273  1.00 71.09           H  
ATOM    749 HD22 LEU A  56      22.963  29.640  18.259  1.00 71.09           H  
ATOM    750 HD23 LEU A  56      23.309  28.688  19.481  1.00 71.09           H  
ATOM    751  N   ARG A  57      22.922  24.745  15.954  1.00 49.26           N  
ANISOU  751  N   ARG A  57     5207   4703   8808   1056     50    178       N  
ATOM    752  CA  ARG A  57      22.064  23.996  15.002  1.00 49.07           C  
ANISOU  752  CA  ARG A  57     4970   4625   9049    987   -172    193       C  
ATOM    753  C   ARG A  57      21.189  23.021  15.798  1.00 51.28           C  
ANISOU  753  C   ARG A  57     5108   4806   9571    903    123    117       C  
ATOM    754  O   ARG A  57      19.988  22.932  15.497  1.00 53.08           O  
ANISOU  754  O   ARG A  57     5011   4922  10235    855     51     79       O  
ATOM    755  CB  ARG A  57      22.912  23.356  13.907  1.00 38.67           C  
ANISOU  755  CB  ARG A  57     3869   3426   7398    919   -450    237       C  
ATOM    756  CG  ARG A  57      23.481  24.340  12.897  1.00 40.32           C  
ANISOU  756  CG  ARG A  57     4189   3713   7417    969   -759    327       C  
ATOM    757  CD  ARG A  57      24.442  23.662  11.947  1.00 36.81           C  
ANISOU  757  CD  ARG A  57     4007   3375   6602    872   -921    327       C  
ATOM    758  NE  ARG A  57      24.786  24.477  10.793  1.00 37.06           N  
ANISOU  758  NE  ARG A  57     4141   3477   6464    872  -1225    425       N  
ATOM    759  CZ  ARG A  57      24.032  24.670   9.710  1.00 54.02           C  
ANISOU  759  CZ  ARG A  57     6168   5658   8700    797  -1583    502       C  
ATOM    760  NH1 ARG A  57      22.831  24.124   9.596  1.00 47.67           N  
ANISOU  760  NH1 ARG A  57     5092   4819   8202    716  -1698    461       N  
ATOM    761  NH2 ARG A  57      24.489  25.434   8.733  1.00 41.55           N  
ANISOU  761  NH2 ARG A  57     4734   4149   6906    790  -1839    640       N  
ATOM    762  H   ARG A  57      23.811  24.562  15.890  1.00 59.44           H  
ATOM    763  HA  ARG A  57      21.465  24.648  14.571  1.00 59.20           H  
ATOM    764  HB2 ARG A  57      23.652  22.868  14.326  1.00 44.83           H  
ATOM    765  HB3 ARG A  57      22.358  22.703  13.432  1.00 44.83           H  
ATOM    766  HG2 ARG A  57      22.748  24.741  12.385  1.00 48.70           H  
ATOM    767  HG3 ARG A  57      23.951  25.060  13.369  1.00 48.70           H  
ATOM    768  HD2 ARG A  57      25.264  23.455  12.436  1.00 42.57           H  
ATOM    769  HD3 ARG A  57      24.059  22.811  11.645  1.00 42.57           H  
ATOM    770  HE  ARG A  57      25.569  24.861  10.804  1.00 43.84           H  
ATOM    771 HH11 ARG A  57      22.503  23.613  10.224  1.00 57.52           H  
ATOM    772 HH12 ARG A  57      22.355  24.270   8.873  1.00 57.52           H  
ATOM    773 HH21 ARG A  57      25.285  25.805   8.795  1.00 50.18           H  
ATOM    774 HH22 ARG A  57      23.998  25.572   8.015  1.00 50.18           H  
ATOM    775  N   THR A  58      21.739  22.364  16.805  1.00 40.97           N  
ANISOU  775  N   THR A  58     4025   3536   8007    878    449    118       N  
ATOM    776  CA  THR A  58      20.992  21.392  17.635  1.00 55.68           C  
ANISOU  776  CA  THR A  58     5795   5288  10073    789    783     83       C  
ATOM    777  C   THR A  58      19.944  22.139  18.458  1.00 60.41           C  
ANISOU  777  C   THR A  58     6179   5760  11013    792   1117    -17       C  
ATOM    778  O   THR A  58      18.815  21.647  18.536  1.00 62.00           O  
ANISOU  778  O   THR A  58     6125   5804  11628    718   1320    -83       O  
ATOM    779  CB  THR A  58      21.934  20.491  18.445  1.00 41.82           C  
ANISOU  779  CB  THR A  58     4362   3609   7919    764   1006    191       C  
ATOM    780  OG1 THR A  58      22.817  19.856  17.526  1.00 43.04           O  
ANISOU  780  OG1 THR A  58     4673   3826   7853    771    748    264       O  
ATOM    781  CG2 THR A  58      21.208  19.434  19.245  1.00 54.60           C  
ANISOU  781  CG2 THR A  58     5910   5088   9748    662   1370    203       C  
ATOM    782  H   THR A  58      22.591  22.503  17.094  1.00 49.49           H  
ATOM    783  HA  THR A  58      20.504  20.807  17.011  1.00 67.13           H  
ATOM    784  HB  THR A  58      22.459  21.057  19.061  1.00 48.59           H  
ATOM    785  HG1 THR A  58      23.464  20.370  17.348  1.00 51.96           H  
ATOM    786 HG21 THR A  58      21.857  18.831  19.647  1.00 65.84           H  
ATOM    787 HG22 THR A  58      20.681  19.855  19.947  1.00 65.84           H  
ATOM    788 HG23 THR A  58      20.619  18.927  18.657  1.00 65.84           H  
ATOM    789  N   LEU A  59      20.283  23.292  19.023  1.00 54.94           N  
ANISOU  789  N   LEU A  59     5575   5108  10193    859   1222    -62       N  
ATOM    790  CA  LEU A  59      19.361  24.064  19.895  1.00 57.54           C  
ANISOU  790  CA  LEU A  59     5706   5279  10876    844   1614   -211       C  
ATOM    791  C   LEU A  59      18.156  24.559  19.081  1.00 54.64           C  
ANISOU  791  C   LEU A  59     4859   4706  11197    907   1448   -248       C  
ATOM    792  O   LEU A  59      17.065  24.563  19.639  1.00 54.15           O  
ANISOU  792  O   LEU A  59     4501   4438  11637    876   1793   -367       O  
ATOM    793  CB  LEU A  59      20.157  25.188  20.566  1.00 47.91           C  
ANISOU  793  CB  LEU A  59     4712   4142   9351    868   1772   -297       C  
ATOM    794  CG  LEU A  59      19.504  25.927  21.733  1.00 67.42           C  
ANISOU  794  CG  LEU A  59     7131   6482  12002    792   2324   -514       C  
ATOM    795  CD1 LEU A  59      18.815  24.986  22.709  1.00 66.73           C  
ANISOU  795  CD1 LEU A  59     7080   6349  11926    647   2766   -546       C  
ATOM    796  CD2 LEU A  59      20.546  26.758  22.461  1.00 63.42           C  
ANISOU  796  CD2 LEU A  59     6980   6151  10964    745   2427   -607       C  
ATOM    797  H   LEU A  59      21.085  23.694  18.873  1.00 66.25           H  
ATOM    798  HA  LEU A  59      19.029  23.447  20.582  1.00 69.36           H  
ATOM    799  HB2 LEU A  59      20.997  24.808  20.890  1.00 57.82           H  
ATOM    800  HB3 LEU A  59      20.384  25.846  19.880  1.00 57.82           H  
ATOM    801  HG  LEU A  59      18.822  26.541  21.365  1.00 81.22           H  
ATOM    802 HD11 LEU A  59      18.619  25.462  23.534  1.00 80.40           H  
ATOM    803 HD12 LEU A  59      17.984  24.661  22.322  1.00 80.40           H  
ATOM    804 HD13 LEU A  59      19.401  24.233  22.904  1.00 80.40           H  
ATOM    805 HD21 LEU A  59      20.108  27.328  23.116  1.00 76.42           H  
ATOM    806 HD22 LEU A  59      21.175  26.170  22.913  1.00 76.42           H  
ATOM    807 HD23 LEU A  59      21.024  27.313  21.820  1.00 76.42           H  
ATOM    808  N   ALA A  60      18.339  24.940  17.818  1.00 50.81           N  
ANISOU  808  N   ALA A  60     4280   4271  10756    983    924   -130       N  
ATOM    809  CA  ALA A  60      17.261  25.439  16.943  1.00 60.19           C  
ANISOU  809  CA  ALA A  60     4997   5292  12579   1045    663    -88       C  
ATOM    810  C   ALA A  60      16.178  24.372  16.834  1.00 74.22           C  
ANISOU  810  C   ALA A  60     6456   6982  14762    936    629   -116       C  
ATOM    811  O   ALA A  60      15.048  24.694  17.232  1.00 65.96           O  
ANISOU  811  O   ALA A  60     5011   5749  14303    910    717   -157       O  
ATOM    812  CB  ALA A  60      17.804  25.825  15.602  1.00 67.65           C  
ANISOU  812  CB  ALA A  60     5993   6357  13354   1119     87     91       C  
ATOM    813  H   ALA A  60      19.149  24.920  17.395  1.00 61.30           H  
ATOM    814  HA  ALA A  60      16.867  26.238  17.363  1.00 72.54           H  
ATOM    815  HB1 ALA A  60      17.072  26.086  15.019  1.00 81.50           H  
ATOM    816  HB2 ALA A  60      18.418  26.572  15.702  1.00 81.50           H  
ATOM    817  HB3 ALA A  60      18.276  25.073  15.206  1.00 81.50           H  
ATOM    818  N   ASP A  61      16.460  23.210  16.240  1.00 71.05           N  
ANISOU  818  N   ASP A  61     4287   6315  16394   -395    204   -114       N  
ATOM    819  CA  ASP A  61      15.519  22.059  16.236  1.00 74.04           C  
ANISOU  819  CA  ASP A  61     4441   6565  17126   -597    205   -163       C  
ATOM    820  C   ASP A  61      16.254  20.827  16.766  1.00 72.98           C  
ANISOU  820  C   ASP A  61     4644   6438  16648   -841    417   -238       C  
ATOM    821  O   ASP A  61      17.094  20.297  16.035  1.00 68.19           O  
ANISOU  821  O   ASP A  61     4314   5979  15618   -917    -35   -256       O  
ATOM    822  CB  ASP A  61      14.922  21.751  14.865  1.00 82.22           C  
ANISOU  822  CB  ASP A  61     5264   7689  18287   -615   -578   -120       C  
ATOM    823  CG  ASP A  61      13.955  20.578  14.903  1.00 81.62           C  
ANISOU  823  CG  ASP A  61     4934   7483  18593   -840   -581   -194       C  
ATOM    824  OD1 ASP A  61      13.385  20.319  15.979  1.00 84.32           O  
ANISOU  824  OD1 ASP A  61     5123   7609  19306   -905     52   -239       O  
ATOM    825  OD2 ASP A  61      13.806  19.911  13.872  1.00 91.46           O  
ANISOU  825  OD2 ASP A  61     6173   8840  19737   -964  -1187   -218       O  
ATOM    826  H   ASP A  61      17.244  23.048  15.805  1.00 85.58           H  
ATOM    827  HA  ASP A  61      14.777  22.271  16.835  1.00 88.47           H  
ATOM    828  HB2 ASP A  61      14.443  22.539  14.539  1.00 98.98           H  
ATOM    829  HB3 ASP A  61      15.641  21.547  14.234  1.00 98.98           H  
ATOM    830  N   PRO A  62      15.937  20.301  17.964  1.00 79.09           N  
ANISOU  830  N   PRO A  62     5480   7022  17547   -970   1116   -272       N  
ATOM    831  CA  PRO A  62      16.566  19.066  18.427  1.00 71.93           C  
ANISOU  831  CA  PRO A  62     4965   6070  16296  -1207   1305   -289       C  
ATOM    832  C   PRO A  62      16.220  17.876  17.517  1.00 79.37           C  
ANISOU  832  C   PRO A  62     5793   7003  17363  -1371    832   -351       C  
ATOM    833  O   PRO A  62      16.959  16.927  17.527  1.00 76.90           O  
ANISOU  833  O   PRO A  62     5850   6661  16707  -1530    808   -366       O  
ATOM    834  CB  PRO A  62      16.050  18.913  19.855  1.00 86.29           C  
ANISOU  834  CB  PRO A  62     6877   7680  18230  -1280   2161   -285       C  
ATOM    835  CG  PRO A  62      15.671  20.310  20.264  1.00 89.96           C  
ANISOU  835  CG  PRO A  62     7161   8113  18907  -1070   2484   -298       C  
ATOM    836  CD  PRO A  62      15.109  20.916  19.001  1.00 77.34           C  
ANISOU  836  CD  PRO A  62     5092   6594  17701   -898   1808   -288       C  
ATOM    837  HA  PRO A  62      17.547  19.191  18.452  1.00 84.73           H  
ATOM    838  HB2 PRO A  62      15.271  18.317  19.884  1.00103.87           H  
ATOM    839  HB3 PRO A  62      16.747  18.554  20.443  1.00103.87           H  
ATOM    840  HG2 PRO A  62      14.998  20.297  20.976  1.00108.27           H  
ATOM    841  HG3 PRO A  62      16.454  20.809  20.573  1.00108.27           H  
ATOM    842  HD2 PRO A  62      14.169  20.688  18.884  1.00 92.06           H  
ATOM    843  HD3 PRO A  62      15.209  21.886  19.010  1.00 92.06           H  
ATOM    844  N   GLY A  63      15.119  17.938  16.776  1.00 78.77           N  
ANISOU  844  N   GLY A  63     5252   6924  17753  -1343    459   -382       N  
ATOM    845  CA  GLY A  63      14.721  16.895  15.819  1.00 80.70           C  
ANISOU  845  CA  GLY A  63     5417   7174  18070  -1535     -5   -467       C  
ATOM    846  C   GLY A  63      15.717  16.688  14.698  1.00 76.89           C  
ANISOU  846  C   GLY A  63     5277   6889  17048  -1560   -641   -512       C  
ATOM    847  O   GLY A  63      15.965  15.522  14.389  1.00 92.14           O  
ANISOU  847  O   GLY A  63     7480   8784  18747  -1754   -754   -609       O  
ATOM    848  H   GLY A  63      14.525  18.621  16.848  1.00 94.84           H  
ATOM    849  HA2 GLY A  63      14.601  16.043  16.308  1.00 95.24           H  
ATOM    850  HA3 GLY A  63      13.845  17.143  15.429  1.00 95.24           H  
ATOM    851  N   GLY A  64      16.313  17.743  14.149  1.00 74.40           N  
ANISOU  851  N   GLY A  64     4990   6761  16518  -1356  -1029   -448       N  
ATOM    852  CA  GLY A  64      17.252  17.638  13.017  1.00 77.49           C  
ANISOU  852  CA  GLY A  64     5771   7335  16336  -1355  -1568   -492       C  
ATOM    853  C   GLY A  64      16.978  18.548  11.836  1.00 75.63           C  
ANISOU  853  C   GLY A  64     5451   7298  15987  -1202  -2191   -422       C  
ATOM    854  O   GLY A  64      17.717  18.452  10.866  1.00 79.53           O  
ANISOU  854  O   GLY A  64     6313   7952  15954  -1204  -2631   -460       O  
ATOM    855  H   GLY A  64      16.226  18.580  14.497  1.00 88.80           H  
ATOM    856  HA2 GLY A  64      18.160  17.833  13.356  1.00 93.31           H  
ATOM    857  HA3 GLY A  64      17.263  16.704  12.693  1.00 93.31           H  
ATOM    858  N   ALA A  65      16.031  19.467  11.913  1.00 75.63           N  
ANISOU  858  N   ALA A  65     5021   7260  16454  -1065  -2192   -304       N  
ATOM    859  CA  ALA A  65      15.651  20.326  10.772  1.00 77.97           C  
ANISOU  859  CA  ALA A  65     5249   7701  16676   -946  -2787   -187       C  
ATOM    860  C   ALA A  65      16.857  21.120  10.275  1.00 73.71           C  
ANISOU  860  C   ALA A  65     5136   7350  15519   -774  -3015   -120       C  
ATOM    861  O   ALA A  65      16.996  21.267   9.051  1.00 74.04           O  
ANISOU  861  O   ALA A  65     5416   7558  15160   -789  -3558    -89       O  
ATOM    862  CB  ALA A  65      14.555  21.253  11.199  1.00 82.30           C  
ANISOU  862  CB  ALA A  65     5298   8109  17864   -786  -2628    -41       C  
ATOM    863  H   ALA A  65      15.536  19.626  12.654  1.00 89.16           H  
ATOM    864  HA  ALA A  65      15.323  19.754  10.039  1.00 91.98           H  
ATOM    865  HB1 ALA A  65      14.343  21.857  10.468  1.00 97.17           H  
ATOM    866  HB2 ALA A  65      13.764  20.740  11.429  1.00 97.17           H  
ATOM    867  HB3 ALA A  65      14.845  21.771  11.967  1.00 97.17           H  
ATOM    868  N   ARG A  66      17.686  21.612  11.187  1.00 68.54           N  
ANISOU  868  N   ARG A  66     4603   6674  14764   -622  -2582    -97       N  
ATOM    869  CA  ARG A  66      18.894  22.396  10.844  1.00 76.33           C  
ANISOU  869  CA  ARG A  66     5979   7825  15198   -450  -2740    -37       C  
ATOM    870  C   ARG A  66      20.132  21.520  11.056  1.00 62.54           C  
ANISOU  870  C   ARG A  66     4658   6125  12978   -554  -2653   -173       C  
ATOM    871  O   ARG A  66      21.187  22.088  11.299  1.00 55.34           O  
ANISOU  871  O   ARG A  66     4150   5308  11570   -367  -2481   -127       O  
ATOM    872  CB  ARG A  66      18.917  23.697  11.653  1.00 73.89           C  
ANISOU  872  CB  ARG A  66     5526   7462  15087   -196  -2359     84       C  
ATOM    873  CG  ARG A  66      17.698  24.585  11.442  1.00 72.07           C  
ANISOU  873  CG  ARG A  66     4900   7121  15363    -91  -2410    223       C  
ATOM    874  CD  ARG A  66      17.479  24.974   9.987  1.00 70.00           C  
ANISOU  874  CD  ARG A  66     4770   7002  14826    -36  -3038    368       C  
ATOM    875  NE  ARG A  66      16.372  25.901   9.812  1.00 78.77           N  
ANISOU  875  NE  ARG A  66     5444   7996  16489    -11  -3207    502       N  
ATOM    876  CZ  ARG A  66      15.876  26.321   8.648  1.00 79.86           C  
ANISOU  876  CZ  ARG A  66     5598   8227  16518     26  -3737    669       C  
ATOM    877  NH1 ARG A  66      16.379  25.910   7.493  1.00 87.69           N  
ANISOU  877  NH1 ARG A  66     7061   9427  16830     35  -4094    708       N  
ATOM    878  NH2 ARG A  66      14.859  27.167   8.647  1.00 86.22           N  
ANISOU  878  NH2 ARG A  66     5952   8903  17905     50  -3889    805       N  
ATOM    879  H   ARG A  66      17.564  21.488  12.080  1.00 80.65           H  
ATOM    880  HA  ARG A  66      18.858  22.625   9.893  1.00 91.92           H  
ATOM    881  HB2 ARG A  66      18.983  23.473  12.605  1.00 88.99           H  
ATOM    882  HB3 ARG A  66      19.718  24.204  11.408  1.00 88.99           H  
ATOM    883  HG2 ARG A  66      16.901  24.115  11.768  1.00 86.80           H  
ATOM    884  HG3 ARG A  66      17.802  25.401  11.976  1.00 86.80           H  
ATOM    885  HD2 ARG A  66      18.299  25.379   9.635  1.00 82.41           H  
ATOM    886  HD3 ARG A  66      17.293  24.166   9.465  1.00 82.41           H  
ATOM    887  HE  ARG A  66      16.004  26.211  10.531  1.00 94.84           H  
ATOM    888 HH11 ARG A  66      17.050  25.349   7.467  1.00105.55           H  
ATOM    889 HH12 ARG A  66      16.032  26.200   6.740  1.00105.55           H  
ATOM    890 HH21 ARG A  66      14.517  27.451   9.407  1.00101.87           H  
ATOM    891 HH22 ARG A  66      14.524  27.452   7.884  1.00101.87           H  
ATOM    892  N   TYR A  67      19.995  20.189  11.025  1.00 60.48           N  
ANISOU  892  N   TYR A  67     4489   5781  12709   -808  -2649   -325       N  
ATOM    893  CA  TYR A  67      21.151  19.277  11.168  1.00 64.30           C  
ANISOU  893  CA  TYR A  67     5558   6269  12605   -845  -2446   -422       C  
ATOM    894  C   TYR A  67      21.975  19.362   9.895  1.00 56.05           C  
ANISOU  894  C   TYR A  67     4926   5377  10993   -835  -2917   -479       C  
ATOM    895  O   TYR A  67      21.370  19.303   8.815  1.00 59.26           O  
ANISOU  895  O   TYR A  67     5247   5840  11429   -975  -3441   -532       O  
ATOM    896  CB  TYR A  67      20.801  17.820  11.470  1.00 58.87           C  
ANISOU  896  CB  TYR A  67     4847   5383  12137  -1115  -2250   -557       C  
ATOM    897  CG  TYR A  67      22.027  16.952  11.517  1.00 64.56           C  
ANISOU  897  CG  TYR A  67     6140   6063  12326  -1135  -2092   -638       C  
ATOM    898  CD1 TYR A  67      22.824  16.908  12.646  1.00 52.63           C  
ANISOU  898  CD1 TYR A  67     4913   4517  10568   -991  -1602   -534       C  
ATOM    899  CD2 TYR A  67      22.443  16.250  10.402  1.00 60.62           C  
ANISOU  899  CD2 TYR A  67     5902   5547  11584  -1302  -2440   -815       C  
ATOM    900  CE1 TYR A  67      23.975  16.144  12.684  1.00 64.53           C  
ANISOU  900  CE1 TYR A  67     6875   5960  11683   -978  -1483   -565       C  
ATOM    901  CE2 TYR A  67      23.596  15.490  10.418  1.00 55.07           C  
ANISOU  901  CE2 TYR A  67     5684   4755  10486  -1292  -2238   -889       C  
ATOM    902  CZ  TYR A  67      24.360  15.429  11.566  1.00 61.97           C  
ANISOU  902  CZ  TYR A  67     6757   5583  11206  -1112  -1771   -742       C  
ATOM    903  OH  TYR A  67      25.500  14.684  11.564  1.00 61.12           O  
ANISOU  903  OH  TYR A  67     7061   5361  10800  -1074  -1595   -773       O  
ATOM    904  H   TYR A  67      19.223  19.759  10.843  1.00 70.98           H  
ATOM    905  HA  TYR A  67      21.707  19.611  11.917  1.00 77.48           H  
ATOM    906  HB2 TYR A  67      20.337  17.776  12.330  1.00 69.05           H  
ATOM    907  HB3 TYR A  67      20.194  17.487  10.777  1.00 69.05           H  
ATOM    908  HD1 TYR A  67      22.564  17.387  13.415  1.00 61.57           H  
ATOM    909  HD2 TYR A  67      21.929  16.288   9.613  1.00 73.06           H  
ATOM    910  HE1 TYR A  67      24.490  16.108  13.471  1.00 77.75           H  
ATOM    911  HE2 TYR A  67      23.857  15.011   9.651  1.00 64.49           H  
ATOM    912  HH  TYR A  67      25.792  14.572  12.362  1.00 73.66           H  
ATOM    913  N   ARG A  68      23.284  19.542  10.024  1.00 51.58           N  
ANISOU  913  N   ARG A  68     4839   4874   9887   -682  -2698   -466       N  
ATOM    914  CA  ARG A  68      24.227  19.568   8.889  1.00 53.24           C  
ANISOU  914  CA  ARG A  68     5494   5201   9535   -650  -2981   -521       C  
ATOM    915  C   ARG A  68      25.350  18.608   9.292  1.00 50.25           C  
ANISOU  915  C   ARG A  68     5525   4733   8835   -631  -2603   -598       C  
ATOM    916  O   ARG A  68      25.692  18.652  10.455  1.00 44.85           O  
ANISOU  916  O   ARG A  68     4858   4018   8167   -496  -2195   -494       O  
ATOM    917  CB  ARG A  68      24.667  21.016   8.672  1.00 53.67           C  
ANISOU  917  CB  ARG A  68     5599   5415   9380   -408  -3089   -355       C  
ATOM    918  CG  ARG A  68      25.687  21.237   7.569  1.00 62.29           C  
ANISOU  918  CG  ARG A  68     7163   6617   9889   -368  -3299   -384       C  
ATOM    919  CD  ARG A  68      25.837  22.723   7.312  1.00 56.63           C  
ANISOU  919  CD  ARG A  68     6399   6020   9100   -153  -3431   -180       C  
ATOM    920  NE  ARG A  68      26.919  23.048   6.396  1.00 54.11           N  
ANISOU  920  NE  ARG A  68     6550   5787   8222    -87  -3489   -174       N  
ATOM    921  CZ  ARG A  68      26.883  22.975   5.066  1.00 65.37           C  
ANISOU  921  CZ  ARG A  68     8257   7281   9301   -211  -3891   -210       C  
ATOM    922  NH1 ARG A  68      25.807  22.550   4.420  1.00 59.36           N  
ANISOU  922  NH1 ARG A  68     7353   6533   8669   -400  -4223   -244       N  
ATOM    923  NH2 ARG A  68      27.959  23.310   4.375  1.00 68.14           N  
ANISOU  923  NH2 ARG A  68     9059   7685   9147   -151  -3828   -203       N  
ATOM    924  H   ARG A  68      23.687  19.675  10.830  1.00 60.31           H  
ATOM    925  HA  ARG A  68      23.774  19.238   8.087  1.00 64.21           H  
ATOM    926  HB2 ARG A  68      23.870  21.550   8.471  1.00 64.73           H  
ATOM    927  HB3 ARG A  68      25.043  21.351   9.513  1.00 64.73           H  
ATOM    928  HG2 ARG A  68      26.552  20.865   7.841  1.00 75.07           H  
ATOM    929  HG3 ARG A  68      25.397  20.786   6.749  1.00 75.07           H  
ATOM    930  HD2 ARG A  68      24.994  23.080   6.963  1.00 68.28           H  
ATOM    931  HD3 ARG A  68      26.013  23.170   8.167  1.00 68.28           H  
ATOM    932  HE  ARG A  68      27.658  23.328   6.754  1.00 65.25           H  
ATOM    933 HH11 ARG A  68      25.082  22.320   4.850  1.00 71.55           H  
ATOM    934 HH12 ARG A  68      25.815  22.509   3.543  1.00 71.55           H  
ATOM    935 HH21 ARG A  68      28.685  23.587   4.791  1.00 82.09           H  
ATOM    936 HH22 ARG A  68      27.953  23.260   3.497  1.00 82.09           H  
ATOM    937  N   PRO A  69      25.932  17.759   8.418  1.00 48.49           N  
ANISOU  937  N   PRO A  69     5640   4450   8336   -768  -2722   -774       N  
ATOM    938  CA  PRO A  69      26.951  16.795   8.854  1.00 50.20           C  
ANISOU  938  CA  PRO A  69     6166   4513   8396   -741  -2343   -830       C  
ATOM    939  C   PRO A  69      28.169  17.489   9.486  1.00 45.32           C  
ANISOU  939  C   PRO A  69     5705   3982   7531   -469  -2078   -669       C  
ATOM    940  O   PRO A  69      28.430  18.583   9.100  1.00 43.50           O  
ANISOU  940  O   PRO A  69     5490   3924   7113   -326  -2204   -583       O  
ATOM    941  CB  PRO A  69      27.368  16.087   7.559  1.00 48.86           C  
ANISOU  941  CB  PRO A  69     6360   4274   7933   -903  -2530  -1068       C  
ATOM    942  CG  PRO A  69      26.213  16.290   6.629  1.00 52.72           C  
ANISOU  942  CG  PRO A  69     6694   4860   8476  -1112  -3049  -1157       C  
ATOM    943  CD  PRO A  69      25.666  17.652   6.987  1.00 51.70           C  
ANISOU  943  CD  PRO A  69     6213   4919   8513   -940  -3200   -920       C  
ATOM    944  HA  PRO A  69      26.552  16.143   9.482  1.00 60.56           H  
ATOM    945  HB2 PRO A  69      28.187  16.484   7.192  1.00 57.04           H  
ATOM    946  HB3 PRO A  69      27.525  15.132   7.719  1.00 57.04           H  
ATOM    947  HG2 PRO A  69      26.509  16.267   5.696  1.00 61.67           H  
ATOM    948  HG3 PRO A  69      25.534  15.598   6.763  1.00 61.67           H  
ATOM    949  HD2 PRO A  69      26.123  18.357   6.493  1.00 60.45           H  
ATOM    950  HD3 PRO A  69      24.712  17.697   6.799  1.00 60.45           H  
ATOM    951  N   PHE A  70      28.861  16.865  10.434  1.00 41.27           N  
ANISOU  951  N   PHE A  70     5305   3334   7040   -410  -1731   -612       N  
ATOM    952  CA  PHE A  70      29.975  17.494  11.183  1.00 43.53           C  
ANISOU  952  CA  PHE A  70     5681   3704   7156   -186  -1521   -440       C  
ATOM    953  C   PHE A  70      31.114  17.922  10.274  1.00 42.20           C  
ANISOU  953  C   PHE A  70     5764   3613   6656    -59  -1579   -477       C  
ATOM    954  O   PHE A  70      31.590  18.923  10.606  1.00 34.59           O  
ANISOU  954  O   PHE A  70     4800   2789   5556    102  -1540   -359       O  
ATOM    955  CB  PHE A  70      30.533  16.615  12.294  1.00 46.55           C  
ANISOU  955  CB  PHE A  70     6139   3917   7632   -165  -1216   -330       C  
ATOM    956  CG  PHE A  70      31.234  17.337  13.416  1.00 41.43           C  
ANISOU  956  CG  PHE A  70     5509   3376   6858     -2  -1060   -125       C  
ATOM    957  CD1 PHE A  70      30.537  18.184  14.260  1.00 45.05           C  
ANISOU  957  CD1 PHE A  70     5800   3949   7370     -3   -996    -47       C  
ATOM    958  CD2 PHE A  70      32.579  17.128  13.665  1.00 42.60           C  
ANISOU  958  CD2 PHE A  70     5835   3492   6860    139   -977    -22       C  
ATOM    959  CE1 PHE A  70      31.175  18.828  15.307  1.00 41.01           C  
ANISOU  959  CE1 PHE A  70     5366   3532   6686     99   -862    100       C  
ATOM    960  CE2 PHE A  70      33.214  17.768  14.714  1.00 43.75           C  
ANISOU  960  CE2 PHE A  70     6001   3750   6872    247   -910    158       C  
ATOM    961  CZ  PHE A  70      32.512  18.619  15.531  1.00 39.11           C  
ANISOU  961  CZ  PHE A  70     5314   3290   6257    210   -858    204       C  
ATOM    962  H   PHE A  70      28.709  16.003  10.679  1.00 47.93           H  
ATOM    963  HA  PHE A  70      29.618  18.315  11.604  1.00 52.56           H  
ATOM    964  HB2 PHE A  70      29.795  16.107  12.676  1.00 56.18           H  
ATOM    965  HB3 PHE A  70      31.155  15.974  11.891  1.00 56.18           H  
ATOM    966  HD1 PHE A  70      29.619  18.336  14.112  1.00 54.38           H  
ATOM    967  HD2 PHE A  70      33.069  16.545  13.110  1.00 51.44           H  
ATOM    968  HE1 PHE A  70      30.689  19.413  15.866  1.00 49.54           H  
ATOM    969  HE2 PHE A  70      34.135  17.625  14.863  1.00 52.82           H  
ATOM    970  HZ  PHE A  70      32.949  19.060  16.243  1.00 47.25           H  
ATOM    971  N   ARG A  71      31.494  17.240   9.209  1.00 38.48           N  
ANISOU  971  N   ARG A  71     5527   3034   6061   -145  -1626   -656       N  
ATOM    972  CA  ARG A  71      32.573  17.732   8.323  1.00 44.56           C  
ANISOU  972  CA  ARG A  71     6547   3861   6521    -41  -1610   -701       C  
ATOM    973  C   ARG A  71      32.195  19.072   7.685  1.00 42.58           C  
ANISOU  973  C   ARG A  71     6269   3830   6078    -18  -1876   -656       C  
ATOM    974  O   ARG A  71      33.103  19.807   7.395  1.00 35.98           O  
ANISOU  974  O   ARG A  71     5524   3090   5059    129  -1807   -573       O  
ATOM    975  CB  ARG A  71      32.912  16.727   7.222  1.00 41.54           C  
ANISOU  975  CB  ARG A  71     6475   3294   6015   -167  -1548   -943       C  
ATOM    976  CG  ARG A  71      34.311  16.889   6.651  1.00 59.22           C  
ANISOU  976  CG  ARG A  71     8975   5523   8001    -39  -1357   -980       C  
ATOM    977  CD  ARG A  71      34.641  15.847   5.601  1.00 79.01           C  
ANISOU  977  CD  ARG A  71    11814   7792  10414   -160  -1177  -1247       C  
ATOM    978  NE  ARG A  71      35.829  16.205   4.835  1.00 76.70           N  
ANISOU  978  NE  ARG A  71    11775   7469   9898    -57   -927  -1305       N  
ATOM    979  CZ  ARG A  71      35.891  17.120   3.862  1.00 82.78           C  
ANISOU  979  CZ  ARG A  71    12771   8403  10278   -100  -1046  -1342       C  
ATOM    980  NH1 ARG A  71      34.827  17.824   3.500  1.00 82.51           N  
ANISOU  980  NH1 ARG A  71    12714   8582  10054   -221  -1473  -1299       N  
ATOM    981  NH2 ARG A  71      37.045  17.341   3.253  1.00 77.00           N  
ANISOU  981  NH2 ARG A  71    12273   7603   9381    -18   -727  -1397       N  
ATOM    982  H   ARG A  71      31.088  16.476   8.934  1.00 44.58           H  
ATOM    983  HA  ARG A  71      33.377  17.871   8.874  1.00 53.79           H  
ATOM    984  HB2 ARG A  71      32.825  15.822   7.584  1.00 50.17           H  
ATOM    985  HB3 ARG A  71      32.259  16.826   6.498  1.00 50.17           H  
ATOM    986  HG2 ARG A  71      34.396  17.779   6.253  1.00 71.38           H  
ATOM    987  HG3 ARG A  71      34.966  16.822   7.378  1.00 71.38           H  
ATOM    988  HD2 ARG A  71      34.795  14.986   6.044  1.00 95.13           H  
ATOM    989  HD3 ARG A  71      33.878  15.737   4.995  1.00 95.13           H  
ATOM    990  HE  ARG A  71      36.564  15.779   5.027  1.00 92.36           H  
ATOM    991 HH11 ARG A  71      34.051  17.703   3.883  1.00 99.33           H  
ATOM    992 HH12 ARG A  71      34.900  18.421   2.860  1.00 99.33           H  
ATOM    993 HH21 ARG A  71      37.762  16.886   3.485  1.00 92.72           H  
ATOM    994 HH22 ARG A  71      37.099  17.945   2.614  1.00 92.72           H  
ATOM    995  N   ASP A  72      30.933  19.285   7.344  1.00 42.68           N  
ANISOU  995  N   ASP A  72     6127   3904   6185   -159  -2186   -686       N  
ATOM    996  CA  ASP A  72      30.413  20.540   6.755  1.00 44.19           C  
ANISOU  996  CA  ASP A  72     6254   4274   6263   -116  -2479   -584       C  
ATOM    997  C   ASP A  72      30.455  21.662   7.799  1.00 46.98           C  
ANISOU  997  C   ASP A  72     6347   4713   6790     76  -2350   -382       C  
ATOM    998  O   ASP A  72      30.911  22.739   7.445  1.00 39.68           O  
ANISOU  998  O   ASP A  72     5479   3888   5708    201  -2395   -275       O  
ATOM    999  CB  ASP A  72      29.032  20.290   6.153  1.00 53.21           C  
ANISOU  999  CB  ASP A  72     7224   5441   7554   -312  -2896   -638       C  
ATOM   1000  CG  ASP A  72      29.034  19.358   4.956  1.00 60.94           C  
ANISOU 1000  CG  ASP A  72     8543   6358   8252   -548  -3099   -871       C  
ATOM   1001  OD1 ASP A  72      29.719  19.671   3.969  1.00 70.46           O  
ANISOU 1001  OD1 ASP A  72    10146   7611   9014   -543  -3128   -918       O  
ATOM   1002  OD2 ASP A  72      28.355  18.326   5.024  1.00 65.42           O  
ANISOU 1002  OD2 ASP A  72     9007   6812   9036   -762  -3198  -1022       O  
ATOM   1003  H   ASP A  72      30.306  18.634   7.450  1.00 51.53           H  
ATOM   1004  HA  ASP A  72      31.015  20.796   6.017  1.00 53.35           H  
ATOM   1005  HB2 ASP A  72      28.439  19.918   6.834  1.00 64.17           H  
ATOM   1006  HB3 ASP A  72      28.665  21.144   5.868  1.00 64.17           H  
ATOM   1007  N   ILE A  73      30.070  21.399   9.041  1.00 39.22           N  
ANISOU 1007  N   ILE A  73     5114   3672   6116     80  -2158   -336       N  
ATOM   1008  CA  ILE A  73      30.154  22.392  10.144  1.00 38.39           C  
ANISOU 1008  CA  ILE A  73     4839   3626   6123    226  -1975   -193       C  
ATOM   1009  C   ILE A  73      31.634  22.735  10.367  1.00 45.02           C  
ANISOU 1009  C   ILE A  73     5896   4502   6708    362  -1777   -147       C  
ATOM   1010  O   ILE A  73      31.924  23.914  10.555  1.00 36.71           O  
ANISOU 1010  O   ILE A  73     4812   3526   5611    476  -1729    -61       O  
ATOM   1011  CB  ILE A  73      29.441  21.894  11.413  1.00 36.55           C  
ANISOU 1011  CB  ILE A  73     4383   3306   6199    163  -1751   -171       C  
ATOM   1012  CG1 ILE A  73      27.923  21.884  11.206  1.00 40.97           C  
ANISOU 1012  CG1 ILE A  73     4603   3832   7133     51  -1929   -192       C  
ATOM   1013  CG2 ILE A  73      29.852  22.709  12.634  1.00 34.91           C  
ANISOU 1013  CG2 ILE A  73     4144   3141   5980    278  -1487    -70       C  
ATOM   1014  CD1 ILE A  73      27.138  21.289  12.341  1.00 40.26           C  
ANISOU 1014  CD1 ILE A  73     4290   3617   7390    -56  -1658   -192       C  
ATOM   1015  H   ILE A  73      29.748  20.585   9.294  1.00 47.39           H  
ATOM   1016  HA  ILE A  73      29.701  23.203   9.849  1.00 46.39           H  
ATOM   1017  HB  ILE A  73      29.727  20.960  11.569  1.00 44.18           H  
ATOM   1018 HG12 ILE A  73      27.620  22.807  11.070  1.00 49.49           H  
ATOM   1019 HG13 ILE A  73      27.718  21.380  10.390  1.00 49.49           H  
ATOM   1020 HG21 ILE A  73      29.274  22.497  13.386  1.00 42.21           H  
ATOM   1021 HG22 ILE A  73      30.771  22.501  12.876  1.00 42.21           H  
ATOM   1022 HG23 ILE A  73      29.777  23.657  12.432  1.00 42.21           H  
ATOM   1023 HD11 ILE A  73      26.277  20.979  12.011  1.00 48.63           H  
ATOM   1024 HD12 ILE A  73      27.630  20.542  12.719  1.00 48.63           H  
ATOM   1025 HD13 ILE A  73      26.997  21.961  13.029  1.00 48.63           H  
ATOM   1026  N   THR A  74      32.534  21.763  10.301  1.00 31.62           N  
ANISOU 1026  N   THR A  74     4395   2723   4898    349  -1654   -204       N  
ATOM   1027  CA  THR A  74      33.986  21.973  10.482  1.00 33.45           C  
ANISOU 1027  CA  THR A  74     4768   2971   4972    474  -1494   -153       C  
ATOM   1028  C   THR A  74      34.475  22.890   9.363  1.00 35.55           C  
ANISOU 1028  C   THR A  74     5174   3312   5021    532  -1574   -166       C  
ATOM   1029  O   THR A  74      35.122  23.877   9.676  1.00 28.54           O  
ANISOU 1029  O   THR A  74     4276   2488   4082    633  -1492    -85       O  
ATOM   1030  CB  THR A  74      34.721  20.627  10.559  1.00 30.80           C  
ANISOU 1030  CB  THR A  74     4565   2483   4655    468  -1346   -200       C  
ATOM   1031  OG1 THR A  74      34.160  19.890  11.640  1.00 34.56           O  
ANISOU 1031  OG1 THR A  74     4947   2859   5326    397  -1278   -160       O  
ATOM   1032  CG2 THR A  74      36.215  20.754  10.746  1.00 38.33           C  
ANISOU 1032  CG2 THR A  74     5555   3440   5570    607  -1195   -110       C  
ATOM   1033  H   THR A  74      32.325  20.904  10.105  1.00 37.55           H  
ATOM   1034  HA  THR A  74      34.115  22.441  11.340  1.00 40.46           H  
ATOM   1035  HB  THR A  74      34.552  20.137   9.724  1.00 37.28           H  
ATOM   1036  HG1 THR A  74      33.677  19.264  11.338  1.00 41.79           H  
ATOM   1037 HG21 THR A  74      36.613  19.866  10.785  1.00 46.32           H  
ATOM   1038 HG22 THR A  74      36.600  21.245   9.999  1.00 46.32           H  
ATOM   1039 HG23 THR A  74      36.400  21.226  11.576  1.00 46.32           H  
ATOM   1040  N   LEU A  75      34.080  22.637   8.125  1.00 31.92           N  
ANISOU 1040  N   LEU A  75     4882   2835   4411    442  -1733   -269       N  
ATOM   1041  CA  LEU A  75      34.462  23.486   6.969  1.00 42.14           C  
ANISOU 1041  CA  LEU A  75     6381   4193   5438    472  -1807   -251       C  
ATOM   1042  C   LEU A  75      33.872  24.896   7.140  1.00 40.67           C  
ANISOU 1042  C   LEU A  75     6024   4111   5319    550  -1954    -94       C  
ATOM   1043  O   LEU A  75      34.594  25.856   6.883  1.00 35.79           O  
ANISOU 1043  O   LEU A  75     5473   3522   4605    647  -1855     -7       O  
ATOM   1044  CB  LEU A  75      33.997  22.821   5.676  1.00 36.63           C  
ANISOU 1044  CB  LEU A  75     5951   3470   4499    312  -2005   -389       C  
ATOM   1045  CG  LEU A  75      34.440  23.488   4.379  1.00 45.74           C  
ANISOU 1045  CG  LEU A  75     7459   4657   5261    304  -2020   -385       C  
ATOM   1046  CD1 LEU A  75      35.948  23.622   4.322  1.00 46.23           C  
ANISOU 1046  CD1 LEU A  75     7656   4641   5269    409  -1603   -408       C  
ATOM   1047  CD2 LEU A  75      33.931  22.713   3.176  1.00 44.66           C  
ANISOU 1047  CD2 LEU A  75     7660   4491   4819     89  -2225   -561       C  
ATOM   1048  H   LEU A  75      33.529  21.945   7.917  1.00 36.71           H  
ATOM   1049  HA  LEU A  75      35.442  23.561   6.965  1.00 50.89           H  
ATOM   1050  HB2 LEU A  75      34.320  21.898   5.672  1.00 44.28           H  
ATOM   1051  HB3 LEU A  75      33.020  22.788   5.684  1.00 44.28           H  
ATOM   1052  HG  LEU A  75      34.049  24.395   4.347  1.00 55.20           H  
ATOM   1053 HD11 LEU A  75      36.235  23.579   3.398  1.00 55.80           H  
ATOM   1054 HD12 LEU A  75      36.216  24.475   4.707  1.00 55.80           H  
ATOM   1055 HD13 LEU A  75      36.359  22.896   4.817  1.00 55.80           H  
ATOM   1056 HD21 LEU A  75      34.177  23.180   2.359  1.00 53.91           H  
ATOM   1057 HD22 LEU A  75      34.325  21.823   3.172  1.00 53.91           H  
ATOM   1058 HD23 LEU A  75      32.962  22.639   3.224  1.00 53.91           H  
ATOM   1059  N   ASP A  76      32.635  25.004   7.602  1.00 34.66           N  
ANISOU 1059  N   ASP A  76     5015   3371   4785    508  -2158    -56       N  
ATOM   1060  CA  ASP A  76      31.974  26.311   7.817  1.00 39.60           C  
ANISOU 1060  CA  ASP A  76     5425   4036   5584    607  -2244     94       C  
ATOM   1061  C   ASP A  76      32.759  27.088   8.873  1.00 38.34           C  
ANISOU 1061  C   ASP A  76     5214   3872   5481    722  -1943    141       C  
ATOM   1062  O   ASP A  76      33.010  28.268   8.645  1.00 33.71           O  
ANISOU 1062  O   ASP A  76     4659   3291   4858    814  -1919    236       O  
ATOM   1063  CB  ASP A  76      30.509  26.134   8.218  1.00 34.67           C  
ANISOU 1063  CB  ASP A  76     4451   3387   5336    557  -2379    109       C  
ATOM   1064  CG  ASP A  76      29.633  25.515   7.140  1.00 51.10           C  
ANISOU 1064  CG  ASP A  76     6518   5480   7419    415  -2770     74       C  
ATOM   1065  OD1 ASP A  76      29.931  25.701   5.947  1.00 57.38           O  
ANISOU 1065  OD1 ASP A  76     7594   6325   7884    377  -3010     91       O  
ATOM   1066  OD2 ASP A  76      28.671  24.837   7.503  1.00 42.22           O  
ANISOU 1066  OD2 ASP A  76     5111   4309   6621    319  -2838     28       O  
ATOM   1067  H   ASP A  76      32.136  24.285   7.843  1.00 41.91           H  
ATOM   1068  HA  ASP A  76      32.009  26.817   6.972  1.00 47.83           H  
ATOM   1069  HB2 ASP A  76      30.460  25.568   9.015  1.00 40.01           H  
ATOM   1070  HB3 ASP A  76      30.138  27.010   8.446  1.00 40.01           H  
ATOM   1071  N   ALA A  77      33.165  26.428   9.948  1.00 34.72           N  
ANISOU 1071  N   ALA A  77     4694   3392   5106    699  -1731     82       N  
ATOM   1072  CA  ALA A  77      33.879  27.069  11.060  1.00 33.32           C  
ANISOU 1072  CA  ALA A  77     4482   3225   4954    758  -1508    110       C  
ATOM   1073  C   ALA A  77      35.215  27.610  10.563  1.00 39.27           C  
ANISOU 1073  C   ALA A  77     5407   3994   5519    814  -1427    125       C  
ATOM   1074  O   ALA A  77      35.565  28.706  10.984  1.00 42.36           O  
ANISOU 1074  O   ALA A  77     5770   4393   5932    853  -1314    153       O  
ATOM   1075  CB  ALA A  77      34.011  26.102  12.188  1.00 35.89           C  
ANISOU 1075  CB  ALA A  77     4773   3533   5333    697  -1360     79       C  
ATOM   1076  H   ALA A  77      33.057  25.533  10.063  1.00 41.98           H  
ATOM   1077  HA  ALA A  77      33.338  27.833  11.371  1.00 40.30           H  
ATOM   1078  HB1 ALA A  77      34.520  26.511  12.907  1.00 43.39           H  
ATOM   1079  HB2 ALA A  77      33.128  25.863  12.516  1.00 43.39           H  
ATOM   1080  HB3 ALA A  77      34.470  25.302  11.885  1.00 43.39           H  
ATOM   1081  N   LEU A  78      35.911  26.880   9.695  1.00 38.13           N  
ANISOU 1081  N   LEU A  78     5441   3832   5216    799  -1446     85       N  
ATOM   1082  CA  LEU A  78      37.215  27.306   9.138  1.00 33.04           C  
ANISOU 1082  CA  LEU A  78     4931   3172   4449    846  -1305     96       C  
ATOM   1083  C   LEU A  78      37.014  28.547   8.274  1.00 38.26           C  
ANISOU 1083  C   LEU A  78     5692   3838   5007    881  -1357    176       C  
ATOM   1084  O   LEU A  78      37.809  29.461   8.394  1.00 30.11           O  
ANISOU 1084  O   LEU A  78     4660   2787   3993    922  -1216    222       O  
ATOM   1085  CB  LEU A  78      37.851  26.160   8.342  1.00 39.37           C  
ANISOU 1085  CB  LEU A  78     5908   3905   5145    818  -1219      8       C  
ATOM   1086  CG  LEU A  78      39.166  26.458   7.625  1.00 39.84           C  
ANISOU 1086  CG  LEU A  78     6111   3910   5118    855  -1000     -1       C  
ATOM   1087  CD1 LEU A  78      40.285  26.776   8.601  1.00 40.27           C  
ANISOU 1087  CD1 LEU A  78     5961   3957   5382    911   -860     46       C  
ATOM   1088  CD2 LEU A  78      39.564  25.293   6.732  1.00 38.76           C  
ANISOU 1088  CD2 LEU A  78     6193   3664   4870    813   -866   -129       C  
ATOM   1089  H   LEU A  78      35.620  26.073   9.390  1.00 46.08           H  
ATOM   1090  HA  LEU A  78      37.801  27.543   9.892  1.00 39.96           H  
ATOM   1091  HB2 LEU A  78      38.001  25.414   8.955  1.00 47.56           H  
ATOM   1092  HB3 LEU A  78      37.204  25.859   7.674  1.00 47.56           H  
ATOM   1093  HG  LEU A  78      39.031  27.246   7.050  1.00 48.13           H  
ATOM   1094 HD11 LEU A  78      41.057  27.103   8.110  1.00 48.64           H  
ATOM   1095 HD12 LEU A  78      39.994  27.459   9.228  1.00 48.64           H  
ATOM   1096 HD13 LEU A  78      40.527  25.973   9.088  1.00 48.64           H  
ATOM   1097 HD21 LEU A  78      40.407  25.495   6.290  1.00 46.83           H  
ATOM   1098 HD22 LEU A  78      39.667  24.489   7.270  1.00 46.83           H  
ATOM   1099 HD23 LEU A  78      38.875  25.146   6.060  1.00 46.83           H  
ATOM   1100  N   ARG A  79      35.978  28.559   7.445  1.00 34.61           N  
ANISOU 1100  N   ARG A  79     5314   3389   4446    853  -1582    211       N  
ATOM   1101  CA  ARG A  79      35.703  29.687   6.532  1.00 36.92           C  
ANISOU 1101  CA  ARG A  79     5735   3672   4622    894  -1682    349       C  
ATOM   1102  C   ARG A  79      35.408  30.943   7.355  1.00 37.21           C  
ANISOU 1102  C   ARG A  79     5551   3674   4915    985  -1645    453       C  
ATOM   1103  O   ARG A  79      35.990  31.961   7.089  1.00 33.71           O  
ANISOU 1103  O   ARG A  79     5199   3171   4440   1038  -1561    561       O  
ATOM   1104  CB  ARG A  79      34.580  29.314   5.568  1.00 39.01           C  
ANISOU 1104  CB  ARG A  79     6108   3970   4744    832  -2033    395       C  
ATOM   1105  CG  ARG A  79      35.011  28.354   4.472  1.00 57.61           C  
ANISOU 1105  CG  ARG A  79     8809   6330   6751    709  -2036    266       C  
ATOM   1106  CD  ARG A  79      33.843  27.571   3.911  1.00 42.87           C  
ANISOU 1106  CD  ARG A  79     6985   4509   4795    586  -2437    241       C  
ATOM   1107  NE  ARG A  79      34.182  26.909   2.661  1.00 48.65           N  
ANISOU 1107  NE  ARG A  79     8169   5233   5084    437  -2457    118       N  
ATOM   1108  CZ  ARG A  79      33.389  26.090   1.973  1.00 55.59           C  
ANISOU 1108  CZ  ARG A  79     9190   6142   5788    262  -2790     24       C  
ATOM   1109  NH1 ARG A  79      32.172  25.792   2.402  1.00 68.87           N  
ANISOU 1109  NH1 ARG A  79    10529   7867   7772    228  -3144     62       N  
ATOM   1110  NH2 ARG A  79      33.826  25.557   0.846  1.00 47.65           N  
ANISOU 1110  NH2 ARG A  79     8673   5111   4322    100  -2750   -127       N  
ATOM   1111  H   ARG A  79      35.372  27.881   7.407  1.00 41.85           H  
ATOM   1112  HA  ARG A  79      36.518  29.847   6.006  1.00 44.63           H  
ATOM   1113  HB2 ARG A  79      33.845  28.912   6.075  1.00 47.13           H  
ATOM   1114  HB3 ARG A  79      34.244  30.135   5.153  1.00 47.13           H  
ATOM   1115  HG2 ARG A  79      35.437  28.861   3.748  1.00 69.45           H  
ATOM   1116  HG3 ARG A  79      35.674  27.724   4.830  1.00 69.45           H  
ATOM   1117  HD2 ARG A  79      33.563  26.900   4.569  1.00 51.76           H  
ATOM   1118  HD3 ARG A  79      33.089  28.181   3.761  1.00 51.76           H  
ATOM   1119  HE  ARG A  79      34.969  27.069   2.330  1.00 58.70           H  
ATOM   1120 HH11 ARG A  79      31.859  26.130   3.146  1.00 82.96           H  
ATOM   1121 HH12 ARG A  79      31.668  25.246   1.935  1.00 82.96           H  
ATOM   1122 HH21 ARG A  79      34.633  25.745   0.550  1.00 57.50           H  
ATOM   1123 HH22 ARG A  79      33.310  25.011   0.387  1.00 57.50           H  
ATOM   1124  N   PHE A  80      34.617  30.837   8.405  1.00 35.03           N  
ANISOU 1124  N   PHE A  80     5007   3400   4903    991  -1656    412       N  
ATOM   1125  CA  PHE A  80      34.354  31.990   9.277  1.00 38.47           C  
ANISOU 1125  CA  PHE A  80     5267   3763   5586   1059  -1530    455       C  
ATOM   1126  C   PHE A  80      35.658  32.447   9.929  1.00 38.23           C  
ANISOU 1126  C   PHE A  80     5294   3717   5513   1039  -1267    383       C  
ATOM   1127  O   PHE A  80      35.944  33.635   9.852  1.00 32.50           O  
ANISOU 1127  O   PHE A  80     4589   2903   4858   1078  -1154    435       O  
ATOM   1128  CB  PHE A  80      33.322  31.683  10.355  1.00 35.63           C  
ANISOU 1128  CB  PHE A  80     4646   3388   5504   1045  -1505    395       C  
ATOM   1129  CG  PHE A  80      33.109  32.854  11.275  1.00 45.33           C  
ANISOU 1129  CG  PHE A  80     5736   4505   6982   1096  -1287    385       C  
ATOM   1130  CD1 PHE A  80      33.937  33.052  12.365  1.00 40.55           C  
ANISOU 1130  CD1 PHE A  80     5188   3903   6315   1027  -1034    255       C  
ATOM   1131  CD2 PHE A  80      32.133  33.798  11.008  1.00 45.19           C  
ANISOU 1131  CD2 PHE A  80     5542   4359   7268   1205  -1343    506       C  
ATOM   1132  CE1 PHE A  80      33.773  34.150  13.187  1.00 50.26           C  
ANISOU 1132  CE1 PHE A  80     6353   5009   7735   1036   -803    195       C  
ATOM   1133  CE2 PHE A  80      31.961  34.890  11.842  1.00 50.19           C  
ANISOU 1133  CE2 PHE A  80     6064   4837   8168   1253  -1074    465       C  
ATOM   1134  CZ  PHE A  80      32.777  35.061  12.932  1.00 45.65           C  
ANISOU 1134  CZ  PHE A  80     5600   4264   7480   1154   -782    284       C  
ATOM   1135  H   PHE A  80      34.208  30.069   8.674  1.00 42.35           H  
ATOM   1136  HA  PHE A  80      34.009  32.734   8.719  1.00 46.48           H  
ATOM   1137  HB2 PHE A  80      32.474  31.447   9.926  1.00 43.08           H  
ATOM   1138  HB3 PHE A  80      33.626  30.911  10.878  1.00 43.08           H  
ATOM   1139  HD1 PHE A  80      34.621  32.429  12.551  1.00 48.97           H  
ATOM   1140  HD2 PHE A  80      31.566  33.685  10.262  1.00 54.54           H  
ATOM   1141  HE1 PHE A  80      34.329  34.254  13.939  1.00 60.63           H  
ATOM   1142  HE2 PHE A  80      31.280  35.517  11.660  1.00 60.55           H  
ATOM   1143  HZ  PHE A  80      32.660  35.806  13.499  1.00 55.10           H  
ATOM   1144  N   ALA A  81      36.462  31.529  10.463  1.00 38.87           N  
ANISOU 1144  N   ALA A  81     5385   3866   5518    969  -1187    275       N  
ATOM   1145  CA  ALA A  81      37.685  31.881  11.208  1.00 40.64           C  
ANISOU 1145  CA  ALA A  81     5614   4090   5736    927  -1022    218       C  
ATOM   1146  C   ALA A  81      38.655  32.613  10.291  1.00 37.34           C  
ANISOU 1146  C   ALA A  81     5310   3616   5260    948   -931    270       C  
ATOM   1147  O   ALA A  81      39.251  33.575  10.747  1.00 29.36           O  
ANISOU 1147  O   ALA A  81     4270   2546   4339    921   -803    254       O  
ATOM   1148  CB  ALA A  81      38.299  30.653  11.813  1.00 36.82           C  
ANISOU 1148  CB  ALA A  81     5116   3677   5197    872  -1028    161       C  
ATOM   1149  H   ALA A  81      36.330  30.632  10.391  1.00 46.96           H  
ATOM   1150  HA  ALA A  81      37.430  32.492  11.933  1.00 49.08           H  
ATOM   1151  HB1 ALA A  81      39.079  30.906  12.336  1.00 44.50           H  
ATOM   1152  HB2 ALA A  81      37.653  30.217  12.394  1.00 44.50           H  
ATOM   1153  HB3 ALA A  81      38.566  30.038  11.109  1.00 44.50           H  
ATOM   1154  N   ALA A  82      38.787  32.175   9.050  1.00 26.95           N  
ANISOU 1154  N   ALA A  82     4152   2300   3786    971   -964    319       N  
ATOM   1155  CA  ALA A  82      39.674  32.824   8.069  1.00 39.97           C  
ANISOU 1155  CA  ALA A  82     5957   3876   5354    975   -807    378       C  
ATOM   1156  C   ALA A  82      39.179  34.241   7.757  1.00 43.72           C  
ANISOU 1156  C   ALA A  82     6483   4253   5874   1021   -810    511       C  
ATOM   1157  O   ALA A  82      40.008  35.137   7.759  1.00 39.65           O  
ANISOU 1157  O   ALA A  82     6003   3638   5423   1005   -616    545       O  
ATOM   1158  CB  ALA A  82      39.791  31.974   6.839  1.00 35.72           C  
ANISOU 1158  CB  ALA A  82     5659   3343   4571    964   -802    380       C  
ATOM   1159  H   ALA A  82      38.329  31.468   8.707  1.00 31.20           H  
ATOM   1160  HA  ALA A  82      40.570  32.899   8.475  1.00 48.28           H  
ATOM   1161  HB1 ALA A  82      40.376  32.410   6.197  1.00 43.18           H  
ATOM   1162  HB2 ALA A  82      40.164  31.107   7.076  1.00 43.18           H  
ATOM   1163  HB3 ALA A  82      38.915  31.849   6.442  1.00 43.18           H  
ATOM   1164  N   ARG A  83      37.879  34.426   7.545  1.00 38.54           N  
ANISOU 1164  N   ARG A  83     5803   3598   5244   1082  -1024    601       N  
ATOM   1165  CA  ARG A  83      37.290  35.741   7.201  1.00 41.53           C  
ANISOU 1165  CA  ARG A  83     6198   3843   5738   1161  -1047    772       C  
ATOM   1166  C   ARG A  83      37.473  36.696   8.378  1.00 47.46           C  
ANISOU 1166  C   ARG A  83     6769   4483   6782   1159   -848    694       C  
ATOM   1167  O   ARG A  83      37.950  37.804   8.148  1.00 45.59           O  
ANISOU 1167  O   ARG A  83     6593   4090   6641   1174   -690    771       O  
ATOM   1168  CB  ARG A  83      35.818  35.566   6.826  1.00 42.50           C  
ANISOU 1168  CB  ARG A  83     6254   3979   5914   1236  -1365    904       C  
ATOM   1169  CG  ARG A  83      35.195  36.737   6.082  1.00 62.54           C  
ANISOU 1169  CG  ARG A  83     8845   6398   8520   1326  -1447   1160       C  
ATOM   1170  CD  ARG A  83      33.680  36.668   6.157  1.00 68.48           C  
ANISOU 1170  CD  ARG A  83     9343   7224   9451   1362  -1676   1243       C  
ATOM   1171  NE  ARG A  83      33.184  35.363   5.723  1.00 67.07           N  
ANISOU 1171  NE  ARG A  83     9182   7214   9087   1271  -1942   1167       N  
ATOM   1172  CZ  ARG A  83      32.106  34.719   6.181  1.00 61.91           C  
ANISOU 1172  CZ  ARG A  83     8244   6621   8660   1249  -2060   1085       C  
ATOM   1173  NH1 ARG A  83      31.332  35.223   7.132  1.00 56.65           N  
ANISOU 1173  NH1 ARG A  83     7267   5863   8394   1323  -1912   1068       N  
ATOM   1174  NH2 ARG A  83      31.806  33.535   5.675  1.00 60.46           N  
ANISOU 1174  NH2 ARG A  83     8105   6551   8315   1146  -2301   1009       N  
ATOM   1175  H   ARG A  83      37.270  33.756   7.640  1.00 46.57           H  
ATOM   1176  HA  ARG A  83      37.774  36.104   6.424  1.00 50.16           H  
ATOM   1177  HB2 ARG A  83      35.739  34.766   6.267  1.00 51.32           H  
ATOM   1178  HB3 ARG A  83      35.307  35.407   7.647  1.00 51.32           H  
ATOM   1179  HG2 ARG A  83      35.500  37.581   6.476  1.00 75.37           H  
ATOM   1180  HG3 ARG A  83      35.475  36.717   5.142  1.00 75.37           H  
ATOM   1181  HD2 ARG A  83      33.408  36.844   7.080  1.00 82.49           H  
ATOM   1182  HD3 ARG A  83      33.294  37.368   5.588  1.00 82.49           H  
ATOM   1183  HE  ARG A  83      33.639  34.963   5.097  1.00 80.80           H  
ATOM   1184 HH11 ARG A  83      31.496  36.001   7.489  1.00 68.30           H  
ATOM   1185 HH12 ARG A  83      30.633  34.768   7.407  1.00 68.30           H  
ATOM   1186 HH21 ARG A  83      32.309  33.181   5.044  1.00 72.87           H  
ATOM   1187 HH22 ARG A  83      31.101  33.096   5.967  1.00 72.87           H  
ATOM   1188  N   ARG A  84      37.211  36.244   9.595  1.00 42.02           N  
ANISOU 1188  N   ARG A  84     5896   3853   6216   1119   -831    531       N  
ATOM   1189  CA  ARG A  84      37.289  37.115  10.781  1.00 47.91           C  
ANISOU 1189  CA  ARG A  84     6539   4489   7174   1076   -630    413       C  
ATOM   1190  C   ARG A  84      38.731  37.582  10.957  1.00 47.25           C  
ANISOU 1190  C   ARG A  84     6525   4372   7057    965   -457    331       C  
ATOM   1191  O   ARG A  84      38.910  38.741  11.316  1.00 38.90           O  
ANISOU 1191  O   ARG A  84     5464   3146   6169    931   -283    292       O  
ATOM   1192  CB  ARG A  84      36.773  36.442  12.054  1.00 45.93           C  
ANISOU 1192  CB  ARG A  84     6169   4325   6958   1008   -614    245       C  
ATOM   1193  CG  ARG A  84      36.430  37.453  13.142  1.00 60.00           C  
ANISOU 1193  CG  ARG A  84     7907   5965   8927    950   -379     99       C  
ATOM   1194  CD  ARG A  84      36.641  37.005  14.575  1.00 71.11           C  
ANISOU 1194  CD  ARG A  84     9336   7488  10194    792   -321    -96       C  
ATOM   1195  NE  ARG A  84      35.450  36.412  15.165  1.00 69.18           N  
ANISOU 1195  NE  ARG A  84     9003   7281  10001    821   -322   -107       N  
ATOM   1196  CZ  ARG A  84      35.335  35.960  16.413  1.00 72.51           C  
ANISOU 1196  CZ  ARG A  84     9463   7704  10384    704   -149   -265       C  
ATOM   1197  NH1 ARG A  84      36.354  36.005  17.259  1.00 69.49           N  
ANISOU 1197  NH1 ARG A  84     9237   7307   9858    537    -14   -436       N  
ATOM   1198  NH2 ARG A  84      34.183  35.448  16.811  1.00 71.27           N  
ANISOU 1198  NH2 ARG A  84     9206   7555  10319    729   -104   -256       N  
ATOM   1199  H   ARG A  84      37.009  35.375   9.772  1.00 50.74           H  
ATOM   1200  HA  ARG A  84      36.731  37.907  10.607  1.00 57.81           H  
ATOM   1201  HB2 ARG A  84      35.972  35.921  11.839  1.00 55.44           H  
ATOM   1202  HB3 ARG A  84      37.459  35.826  12.385  1.00 55.44           H  
ATOM   1203  HG2 ARG A  84      36.966  38.259  13.001  1.00 72.32           H  
ATOM   1204  HG3 ARG A  84      35.492  37.715  13.034  1.00 72.32           H  
ATOM   1205  HD2 ARG A  84      37.374  36.357  14.606  1.00 85.65           H  
ATOM   1206  HD3 ARG A  84      36.909  37.782  15.110  1.00 85.65           H  
ATOM   1207  HE  ARG A  84      34.747  36.364  14.664  1.00 83.34           H  
ATOM   1208 HH11 ARG A  84      37.127  36.335  17.018  1.00 83.71           H  
ATOM   1209 HH12 ARG A  84      36.254  35.696  18.072  1.00 83.71           H  
ATOM   1210 HH21 ARG A  84      33.498  35.411  16.257  1.00 85.85           H  
ATOM   1211 HH22 ARG A  84      34.096  35.141  17.632  1.00 85.85           H  
ATOM   1212  N   LEU A  85      39.715  36.725  10.702  1.00 45.62           N  
ANISOU 1212  N   LEU A  85     6350   4294   6688    903   -488    297       N  
ATOM   1213  CA  LEU A  85      41.139  37.049  10.965  1.00 55.02           C  
ANISOU 1213  CA  LEU A  85     7520   5454   7932    788   -347    223       C  
ATOM   1214  C   LEU A  85      41.774  37.738   9.752  1.00 41.85           C  
ANISOU 1214  C   LEU A  85     5973   3652   6277    812   -186    355       C  
ATOM   1215  O   LEU A  85      42.945  38.101   9.854  1.00 45.31           O  
ANISOU 1215  O   LEU A  85     6357   4031   6827    708    -29    302       O  
ATOM   1216  CB  LEU A  85      41.866  35.765  11.393  1.00 41.26           C  
ANISOU 1216  CB  LEU A  85     5693   3869   6114    729   -432    153       C  
ATOM   1217  CG  LEU A  85      41.423  35.153  12.721  1.00 37.07           C  
ANISOU 1217  CG  LEU A  85     5086   3463   5536    672   -576     51       C  
ATOM   1218  CD1 LEU A  85      42.069  33.795  12.918  1.00 38.84           C  
ANISOU 1218  CD1 LEU A  85     5235   3804   5719    660   -685     61       C  
ATOM   1219  CD2 LEU A  85      41.737  36.063  13.898  1.00 42.16           C  
ANISOU 1219  CD2 LEU A  85     5703   4070   6247    522   -533    -91       C  
ATOM   1220  H   LEU A  85      39.575  35.906  10.328  1.00 55.06           H  
ATOM   1221  HA  LEU A  85      41.168  37.685  11.712  1.00 66.34           H  
ATOM   1222  HB2 LEU A  85      41.746  35.097  10.689  1.00 49.83           H  
ATOM   1223  HB3 LEU A  85      42.823  35.958  11.449  1.00 49.83           H  
ATOM   1224  HG  LEU A  85      40.443  35.023  12.689  1.00 44.80           H  
ATOM   1225 HD11 LEU A  85      41.709  33.377  13.719  1.00 46.93           H  
ATOM   1226 HD12 LEU A  85      41.880  33.231  12.147  1.00 46.93           H  
ATOM   1227 HD13 LEU A  85      43.031  33.902  13.012  1.00 46.93           H  
ATOM   1228 HD21 LEU A  85      41.626  35.571  14.730  1.00 50.91           H  
ATOM   1229 HD22 LEU A  85      42.655  36.378  13.831  1.00 50.91           H  
ATOM   1230 HD23 LEU A  85      41.134  36.826  13.893  1.00 50.91           H  
ATOM   1231  N   GLY A  86      41.029  37.937   8.671  1.00 43.72           N  
ANISOU 1231  N   GLY A  86     6375   3833   6403    928   -231    537       N  
ATOM   1232  CA  GLY A  86      41.532  38.589   7.452  1.00 52.15           C  
ANISOU 1232  CA  GLY A  86     7640   4763   7410    938    -62    699       C  
ATOM   1233  C   GLY A  86      42.348  37.662   6.578  1.00 48.66           C  
ANISOU 1233  C   GLY A  86     7342   4394   6754    907     34    709       C  
ATOM   1234  O   GLY A  86      43.089  38.176   5.735  1.00 48.30           O  
ANISOU 1234  O   GLY A  86     7456   4221   6673    868    285    799       O  
ATOM   1235  H   GLY A  86      40.177  37.634   8.602  1.00 52.78           H  
ATOM   1236  HA2 GLY A  86      40.760  38.925   6.932  1.00 62.89           H  
ATOM   1237  HA3 GLY A  86      42.086  39.368   7.707  1.00 62.89           H  
ATOM   1238  N   LEU A  87      42.218  36.355   6.761  1.00 48.08           N  
ANISOU 1238  N   LEU A  87     7231   4484   6554    916   -107    615       N  
ATOM   1239  CA  LEU A  87      42.995  35.344   6.005  1.00 42.99           C  
ANISOU 1239  CA  LEU A  87     6708   3867   5758    888     44    576       C  
ATOM   1240  C   LEU A  87      42.208  34.923   4.768  1.00 44.50           C  
ANISOU 1240  C   LEU A  87     7244   4089   5576    922    -69    678       C  
ATOM   1241  O   LEU A  87      41.005  34.701   4.894  1.00 48.01           O  
ANISOU 1241  O   LEU A  87     7697   4616   5927    970   -386    719       O  
ATOM   1242  CB  LEU A  87      43.327  34.173   6.926  1.00 32.47           C  
ANISOU 1242  CB  LEU A  87     5140   2649   4546    873    -26    416       C  
ATOM   1243  CG  LEU A  87      43.969  34.524   8.268  1.00 48.85           C  
ANISOU 1243  CG  LEU A  87     6901   4741   6917    812    -52    327       C  
ATOM   1244  CD1 LEU A  87      44.133  33.282   9.128  1.00 44.97           C  
ANISOU 1244  CD1 LEU A  87     6222   4365   6498    812   -196    239       C  
ATOM   1245  CD2 LEU A  87      45.307  35.217   8.078  1.00 39.20           C  
ANISOU 1245  CD2 LEU A  87     5583   3390   5921    730    220    323       C  
ATOM   1246  H   LEU A  87      41.621  36.002   7.338  1.00 58.02           H  
ATOM   1247  HA  LEU A  87      43.833  35.760   5.708  1.00 51.90           H  
ATOM   1248  HB2 LEU A  87      42.501  33.680   7.100  1.00 39.28           H  
ATOM   1249  HB3 LEU A  87      43.929  33.571   6.446  1.00 39.28           H  
ATOM   1250  HG  LEU A  87      43.369  35.145   8.748  1.00 58.93           H  
ATOM   1251 HD11 LEU A  87      44.462  33.536  10.007  1.00 54.28           H  
ATOM   1252 HD12 LEU A  87      43.273  32.837   9.222  1.00 54.28           H  
ATOM   1253 HD13 LEU A  87      44.767  32.676   8.707  1.00 54.28           H  
ATOM   1254 HD21 LEU A  87      45.722  35.356   8.944  1.00 47.36           H  
ATOM   1255 HD22 LEU A  87      45.886  34.663   7.527  1.00 47.36           H  
ATOM   1256 HD23 LEU A  87      45.173  36.078   7.646  1.00 47.36           H  
ATOM   1257  N   ALA A  88      42.867  34.836   3.621  1.00 38.30           N  
ANISOU 1257  N   ALA A  88     6745   3226   4580    875    199    710       N  
ATOM   1258  CA  ALA A  88      42.246  34.408   2.359  1.00 49.89           C  
ANISOU 1258  CA  ALA A  88     8642   4719   5595    853    106    788       C  
ATOM   1259  C   ALA A  88      42.415  32.891   2.222  1.00 47.36           C  
ANISOU 1259  C   ALA A  88     8367   4467   5161    814    144    583       C  
ATOM   1260  O   ALA A  88      43.538  32.462   1.951  1.00 53.56           O  
ANISOU 1260  O   ALA A  88     9153   5167   6031    778    526    461       O  
ATOM   1261  CB  ALA A  88      42.871  35.151   1.216  1.00 43.01           C  
ANISOU 1261  CB  ALA A  88     8155   3700   4486    794    436    934       C  
ATOM   1262  H   ALA A  88      43.763  34.976   3.541  1.00 46.27           H  
ATOM   1263  HA  ALA A  88      41.285  34.622   2.385  1.00 60.19           H  
ATOM   1264  HB1 ALA A  88      42.465  34.862   0.382  1.00 50.02           H  
ATOM   1265  HB2 ALA A  88      42.725  36.105   1.332  1.00 50.02           H  
ATOM   1266  HB3 ALA A  88      43.826  34.972   1.189  1.00 50.02           H  
ATOM   1267  N   LEU A  89      41.338  32.122   2.361  1.00 47.95           N  
ANISOU 1267  N   LEU A  89     8458   4661   5102    818   -226    544       N  
ATOM   1268  CA  LEU A  89      41.372  30.639   2.309  1.00 46.63           C  
ANISOU 1268  CA  LEU A  89     8308   4527   4884    777   -215    339       C  
ATOM   1269  C   LEU A  89      40.978  30.164   0.914  1.00 48.35           C  
ANISOU 1269  C   LEU A  89     9035   4746   4589    663   -278    310       C  
ATOM   1270  O   LEU A  89      39.777  30.085   0.642  1.00 51.59           O  
ANISOU 1270  O   LEU A  89     9549   5256   4797    626   -708    369       O  
ATOM   1271  CB  LEU A  89      40.441  30.094   3.395  1.00 50.74           C  
ANISOU 1271  CB  LEU A  89     8489   5153   5636    820   -548    289       C  
ATOM   1272  CG  LEU A  89      40.502  28.592   3.658  1.00 46.19           C  
ANISOU 1272  CG  LEU A  89     7831   4572   5145    796   -514     99       C  
ATOM   1273  CD1 LEU A  89      41.731  28.215   4.472  1.00 58.47           C  
ANISOU 1273  CD1 LEU A  89     9114   6054   7050    853   -218     39       C  
ATOM   1274  CD2 LEU A  89      39.238  28.136   4.361  1.00 44.56           C  
ANISOU 1274  CD2 LEU A  89     7418   4463   5048    798   -880     95       C  
ATOM   1275  H   LEU A  89      40.501  32.464   2.468  1.00 57.86           H  
ATOM   1276  HA  LEU A  89      42.289  30.341   2.497  1.00 56.28           H  
ATOM   1277  HB2 LEU A  89      40.653  30.557   4.230  1.00 61.20           H  
ATOM   1278  HB3 LEU A  89      39.522  30.330   3.162  1.00 61.20           H  
ATOM   1279  HG  LEU A  89      40.557  28.128   2.789  1.00 55.74           H  
ATOM   1280 HD11 LEU A  89      41.711  27.263   4.669  1.00 70.49           H  
ATOM   1281 HD12 LEU A  89      42.534  28.420   3.964  1.00 70.49           H  
ATOM   1282 HD13 LEU A  89      41.737  28.716   5.307  1.00 70.49           H  
ATOM   1283 HD21 LEU A  89      39.313  27.194   4.585  1.00 53.79           H  
ATOM   1284 HD22 LEU A  89      39.113  28.656   5.173  1.00 53.79           H  
ATOM   1285 HD23 LEU A  89      38.473  28.266   3.774  1.00 53.79           H  
ATOM   1286  N   ASN A  90      41.964  29.832   0.083  1.00 50.16           N  
ANISOU 1286  N   ASN A  90     9583   4856   4620    590    159    208       N  
ATOM   1287  CA  ASN A  90      41.743  29.293  -1.281  1.00 67.67           C  
ANISOU 1287  CA  ASN A  90    12376   7057   6281    436    178    120       C  
ATOM   1288  C   ASN A  90      41.402  27.811  -1.153  1.00 57.39           C  
ANISOU 1288  C   ASN A  90    11059   5756   4991    375    102   -144       C  
ATOM   1289  O   ASN A  90      41.631  27.259  -0.074  1.00 59.76           O  
ANISOU 1289  O   ASN A  90    10922   6038   5746    469    132   -237       O  
ATOM   1290  CB  ASN A  90      42.924  29.583  -2.214  1.00 72.96           C  
ANISOU 1290  CB  ASN A  90    13423   7556   6742    363    786     77       C  
ATOM   1291  CG  ASN A  90      44.270  29.091  -1.721  1.00 79.71           C  
ANISOU 1291  CG  ASN A  90    13904   8257   8126    445   1312    -79       C  
ATOM   1292  OD1 ASN A  90      44.353  28.135  -0.959  1.00 83.67           O  
ANISOU 1292  OD1 ASN A  90    14085   8748   8956    504   1278   -238       O  
ATOM   1293  ND2 ASN A  90      45.338  29.733  -2.161  1.00 81.88           N  
ANISOU 1293  ND2 ASN A  90    14196   8393   8521    447   1791     -9       N  
ATOM   1294  H   ASN A  90      42.838  29.881   0.325  1.00 60.51           H  
ATOM   1295  HA  ASN A  90      40.959  29.753  -1.662  1.00 81.53           H  
ATOM   1296  HB2 ASN A  90      42.742  29.171  -3.083  1.00 87.87           H  
ATOM   1297  HB3 ASN A  90      42.975  30.551  -2.350  1.00 87.87           H  
ATOM   1298 HD21 ASN A  90      46.127  29.580  -1.793  1.00 98.57           H  
ATOM   1299 HD22 ASN A  90      45.266  30.315  -2.822  1.00 98.57           H  
ATOM   1300  N   SER A  91      40.910  27.177  -2.208  1.00 71.01           N  
ANISOU 1300  N   SER A  91    13308   7487   6185    194     -5   -260       N  
ATOM   1301  CA  SER A  91      40.440  25.769  -2.177  1.00 65.29           C  
ANISOU 1301  CA  SER A  91    12614   6741   5451     97   -117   -524       C  
ATOM   1302  C   SER A  91      41.565  24.812  -1.761  1.00 71.51           C  
ANISOU 1302  C   SER A  91    13217   7324   6628    167    437   -750       C  
ATOM   1303  O   SER A  91      41.271  23.880  -1.009  1.00 71.01           O  
ANISOU 1303  O   SER A  91    12869   7224   6887    201    348   -876       O  
ATOM   1304  CB  SER A  91      39.845  25.428  -3.492  1.00 73.09           C  
ANISOU 1304  CB  SER A  91    14282   7743   5745   -160   -268   -654       C  
ATOM   1305  OG  SER A  91      38.906  26.414  -3.881  1.00 78.90           O  
ANISOU 1305  OG  SER A  91    15196   8653   6127   -212   -809   -382       O  
ATOM   1306  H   SER A  91      40.830  27.555  -3.033  1.00 85.53           H  
ATOM   1307  HA  SER A  91      39.722  25.707  -1.490  1.00 78.66           H  
ATOM   1308  HB2 SER A  91      40.558  25.365  -4.168  1.00 88.02           H  
ATOM   1309  HB3 SER A  91      39.400  24.553  -3.433  1.00 88.02           H  
ATOM   1310  HG  SER A  91      38.605  26.212  -4.644  1.00 94.99           H  
ATOM   1311  N   ALA A  92      42.800  25.039  -2.191  1.00 74.50           N  
ANISOU 1311  N   ALA A  92    13732   7543   7031    193   1023   -782       N  
ATOM   1312  CA  ALA A  92      43.958  24.226  -1.779  1.00 60.94           C  
ANISOU 1312  CA  ALA A  92    11774   5597   5786    286   1561   -963       C  
ATOM   1313  C   ALA A  92      44.215  24.326  -0.279  1.00 72.23           C  
ANISOU 1313  C   ALA A  92    12492   7071   7882    494   1403   -823       C  
ATOM   1314  O   ALA A  92      44.332  23.273   0.355  1.00 69.85           O  
ANISOU 1314  O   ALA A  92    11925   6690   7925    558   1375   -919       O  
ATOM   1315  CB  ALA A  92      45.179  24.704  -2.504  1.00 68.28           C  
ANISOU 1315  CB  ALA A  92    12933   6335   6674    270   2242   -999       C  
ATOM   1316  H   ALA A  92      43.023  25.718  -2.755  1.00 89.72           H  
ATOM   1317  HA  ALA A  92      43.789  23.283  -2.013  1.00 73.45           H  
ATOM   1318  HB1 ALA A  92      45.947  24.180  -2.223  1.00 82.25           H  
ATOM   1319  HB2 ALA A  92      45.051  24.600  -3.462  1.00 82.25           H  
ATOM   1320  HB3 ALA A  92      45.337  25.641  -2.298  1.00 82.25           H  
ATOM   1321  N   ALA A  93      44.256  25.530   0.281  1.00 71.05           N  
ANISOU 1321  N   ALA A  93    12063   7033   7899    583   1296   -591       N  
ATOM   1322  CA  ALA A  93      44.554  25.743   1.710  1.00 68.61           C  
ANISOU 1322  CA  ALA A  93    11151   6782   8134    734   1120   -470       C  
ATOM   1323  C   ALA A  93      43.411  25.153   2.516  1.00 56.57           C  
ANISOU 1323  C   ALA A  93     9463   5399   6631    743    616   -453       C  
ATOM   1324  O   ALA A  93      43.674  24.570   3.565  1.00 58.10           O  
ANISOU 1324  O   ALA A  93     9271   5583   7220    837    535   -427       O  
ATOM   1325  CB  ALA A  93      44.769  27.201   1.995  1.00 59.97           C  
ANISOU 1325  CB  ALA A  93     9876   5776   7134    773   1070   -266       C  
ATOM   1326  H   ALA A  93      44.061  26.300  -0.161  1.00 85.58           H  
ATOM   1327  HA  ALA A  93      45.377  25.252   1.931  1.00 82.65           H  
ATOM   1328  HB1 ALA A  93      44.969  27.321   2.939  1.00 72.28           H  
ATOM   1329  HB2 ALA A  93      45.513  27.531   1.464  1.00 72.28           H  
ATOM   1330  HB3 ALA A  93      43.964  27.701   1.772  1.00 72.28           H  
ATOM   1331  N   GLU A  94      42.194  25.305   2.024  1.00 53.20           N  
ANISOU 1331  N   GLU A  94     9320   5096   5799    636    268   -447       N  
ATOM   1332  CA  GLU A  94      40.995  24.785   2.704  1.00 57.23           C  
ANISOU 1332  CA  GLU A  94     9674   5708   6364    616   -155   -454       C  
ATOM   1333  C   GLU A  94      41.119  23.264   2.782  1.00 58.81           C  
ANISOU 1333  C   GLU A  94     9879   5754   6713    588    -15   -653       C  
ATOM   1334  O   GLU A  94      40.893  22.726   3.867  1.00 51.99           O  
ANISOU 1334  O   GLU A  94     8691   4887   6177    653   -138   -621       O  
ATOM   1335  CB  GLU A  94      39.786  25.236   1.893  1.00 70.22           C  
ANISOU 1335  CB  GLU A  94    11607   7482   7590    492   -547   -411       C  
ATOM   1336  CG  GLU A  94      38.442  24.889   2.465  1.00 67.99           C  
ANISOU 1336  CG  GLU A  94    11110   7305   7419    458   -995   -395       C  
ATOM   1337  CD  GLU A  94      37.324  25.510   1.646  1.00 65.18           C  
ANISOU 1337  CD  GLU A  94    10959   7072   6733    353  -1428   -299       C  
ATOM   1338  OE1 GLU A  94      36.942  26.650   1.943  1.00 52.59           O  
ANISOU 1338  OE1 GLU A  94     9229   5563   5191    442  -1601    -77       O  
ATOM   1339  OE2 GLU A  94      36.859  24.860   0.696  1.00 66.84           O  
ANISOU 1339  OE2 GLU A  94    11473   7277   6648    176  -1609   -443       O  
ATOM   1340  H   GLU A  94      42.030  25.731   1.239  1.00 64.16           H  
ATOM   1341  HA  GLU A  94      40.946  25.161   3.613  1.00 69.00           H  
ATOM   1342  HB2 GLU A  94      39.831  26.206   1.785  1.00 84.58           H  
ATOM   1343  HB3 GLU A  94      39.849  24.839   1.001  1.00 84.58           H  
ATOM   1344  HG2 GLU A  94      38.332  23.915   2.473  1.00 81.91           H  
ATOM   1345  HG3 GLU A  94      38.382  25.213   3.389  1.00 81.91           H  
ATOM   1346  N   LYS A  95      41.516  22.613   1.691  1.00 57.73           N  
ANISOU 1346  N   LYS A  95    10143   5460   6332    483    282   -860       N  
ATOM   1347  CA  LYS A  95      41.630  21.137   1.624  1.00 72.67           C  
ANISOU 1347  CA  LYS A  95    12081   7147   8383    445    461  -1077       C  
ATOM   1348  C   LYS A  95      42.720  20.653   2.570  1.00 72.30           C  
ANISOU 1348  C   LYS A  95    11626   6927   8916    640    776  -1024       C  
ATOM   1349  O   LYS A  95      42.456  19.709   3.312  1.00 67.10           O  
ANISOU 1349  O   LYS A  95    10767   6161   8567    685    722  -1043       O  
ATOM   1350  CB  LYS A  95      41.946  20.674   0.202  1.00 57.79           C  
ANISOU 1350  CB  LYS A  95    10774   5100   6085    269    783  -1349       C  
ATOM   1351  H   LYS A  95      41.759  23.038   0.924  1.00 69.60           H  
ATOM   1352  HA  LYS A  95      40.771  20.744   1.904  1.00 87.52           H  
ATOM   1353  N   ARG A  96      43.866  21.315   2.584  1.00 56.75           N  
ANISOU 1353  N   ARG A  96     9520   4913   7131    750   1090   -936       N  
ATOM   1354  CA  ARG A  96      44.995  20.845   3.398  1.00 56.39           C  
ANISOU 1354  CA  ARG A  96     9032   4707   7688    934   1321   -852       C  
ATOM   1355  C   ARG A  96      44.546  20.862   4.850  1.00 57.03           C  
ANISOU 1355  C   ARG A  96     8699   4937   8032   1023    886   -640       C  
ATOM   1356  O   ARG A  96      44.767  19.858   5.531  1.00 58.37           O  
ANISOU 1356  O   ARG A  96     8638   4964   8576   1117    893   -596       O  
ATOM   1357  CB  ARG A  96      46.238  21.700   3.164  1.00 51.60           C  
ANISOU 1357  CB  ARG A  96     8283   4061   7262   1005   1656   -774       C  
ATOM   1358  H   ARG A  96      44.013  22.088   2.124  1.00 68.42           H  
ATOM   1359  HA  ARG A  96      45.196  19.915   3.142  1.00 67.99           H  
ATOM   1360  N   LEU A  97      43.885  21.922   5.285  1.00 45.16           N  
ANISOU 1360  N   LEU A  97     7128   3696   6334    990    531   -499       N  
ATOM   1361  CA  LEU A  97      43.507  22.046   6.705  1.00 46.66           C  
ANISOU 1361  CA  LEU A  97     6992   4024   6713   1044    182   -321       C  
ATOM   1362  C   LEU A  97      42.445  21.007   7.055  1.00 41.40           C  
ANISOU 1362  C   LEU A  97     6383   3339   6008    988    -22   -363       C  
ATOM   1363  O   LEU A  97      42.547  20.431   8.140  1.00 42.73           O  
ANISOU 1363  O   LEU A  97     6323   3479   6435   1050   -134   -241       O  
ATOM   1364  CB  LEU A  97      43.089  23.486   7.018  1.00 38.10           C  
ANISOU 1364  CB  LEU A  97     5863   3173   5439   1008    -62   -210       C  
ATOM   1365  CG  LEU A  97      44.214  24.514   7.145  1.00 48.28           C  
ANISOU 1365  CG  LEU A  97     6968   4484   6892   1057     72   -119       C  
ATOM   1366  CD1 LEU A  97      43.655  25.911   7.346  1.00 38.00           C  
ANISOU 1366  CD1 LEU A  97     5599   3372   5467   1019   -186    -18       C  
ATOM   1367  CD2 LEU A  97      45.163  24.174   8.286  1.00 57.32           C  
ANISOU 1367  CD2 LEU A  97     7752   5534   8494   1158    140    -31       C  
ATOM   1368  H   LEU A  97      43.609  22.601   4.744  1.00 54.50           H  
ATOM   1369  HA  LEU A  97      44.303  21.831   7.236  1.00 56.31           H  
ATOM   1370  HB2 LEU A  97      42.474  23.786   6.318  1.00 46.04           H  
ATOM   1371  HB3 LEU A  97      42.587  23.479   7.856  1.00 46.04           H  
ATOM   1372  HG  LEU A  97      44.727  24.510   6.302  1.00 58.26           H  
ATOM   1373 HD11 LEU A  97      44.379  26.560   7.317  1.00 45.92           H  
ATOM   1374 HD12 LEU A  97      43.014  26.111   6.641  1.00 45.92           H  
ATOM   1375 HD13 LEU A  97      43.210  25.960   8.210  1.00 45.92           H  
ATOM   1376 HD21 LEU A  97      45.726  24.940   8.478  1.00 69.11           H  
ATOM   1377 HD22 LEU A  97      44.649  23.946   9.078  1.00 69.11           H  
ATOM   1378 HD23 LEU A  97      45.722  23.419   8.036  1.00 69.11           H  
ATOM   1379  N   MET A  98      41.475  20.770   6.181  1.00 42.20           N  
ANISOU 1379  N   MET A  98     6794   3451   5788    850    -93   -521       N  
ATOM   1380  CA  MET A  98      40.436  19.730   6.410  1.00 43.01           C  
ANISOU 1380  CA  MET A  98     6927   3501   5915    765   -259   -587       C  
ATOM   1381  C   MET A  98      41.079  18.331   6.431  1.00 44.27           C  
ANISOU 1381  C   MET A  98     7085   3364   6370    816     23   -673       C  
ATOM   1382  O   MET A  98      40.693  17.533   7.290  1.00 40.45           O  
ANISOU 1382  O   MET A  98     6450   2797   6124    837    -62   -593       O  
ATOM   1383  CB  MET A  98      39.336  19.798   5.352  1.00 47.17           C  
ANISOU 1383  CB  MET A  98     7765   4095   6064    577   -443   -749       C  
ATOM   1384  CG  MET A  98      38.423  21.007   5.480  1.00 44.10           C  
ANISOU 1384  CG  MET A  98     7305   3960   5492    544   -791   -621       C  
ATOM   1385  SD  MET A  98      37.581  21.151   7.072  1.00 39.32           S  
ANISOU 1385  SD  MET A  98     6310   3467   5164    584  -1033   -447       S  
ATOM   1386  CE  MET A  98      36.364  19.846   6.938  1.00 49.22           C  
ANISOU 1386  CE  MET A  98     7607   4593   6501    418  -1143   -595       C  
ATOM   1387  H   MET A  98      41.406  21.211   5.387  1.00 50.95           H  
ATOM   1388  HA  MET A  98      40.041  19.892   7.295  1.00 51.94           H  
ATOM   1389  HB2 MET A  98      39.752  19.809   4.467  1.00 56.93           H  
ATOM   1390  HB3 MET A  98      38.796  18.986   5.412  1.00 56.93           H  
ATOM   1391  HG2 MET A  98      38.948  21.821   5.335  1.00 53.24           H  
ATOM   1392  HG3 MET A  98      37.744  20.963   4.773  1.00 53.24           H  
ATOM   1393  HE1 MET A  98      36.811  18.994   6.871  1.00 59.38           H  
ATOM   1394  HE2 MET A  98      35.802  19.853   7.719  1.00 59.38           H  
ATOM   1395  HE3 MET A  98      35.824  19.990   6.152  1.00 59.38           H  
ATOM   1396  N   ASP A  99      42.041  18.063   5.557  1.00 44.70           N  
ANISOU 1396  N   ASP A  99     7320   3225   6441    838    404   -828       N  
ATOM   1397  CA  ASP A  99      42.751  16.758   5.471  1.00 47.98           C  
ANISOU 1397  CA  ASP A  99     7722   3294   7214    908    742   -924       C  
ATOM   1398  C   ASP A  99      43.549  16.538   6.749  1.00 49.97           C  
ANISOU 1398  C   ASP A  99     7536   3469   7982   1123    732   -648       C  
ATOM   1399  O   ASP A  99      43.651  15.383   7.171  1.00 47.28           O  
ANISOU 1399  O   ASP A  99     7104   2874   7986   1193    825   -612       O  
ATOM   1400  CB  ASP A  99      43.611  16.647   4.215  1.00 53.05           C  
ANISOU 1400  CB  ASP A  99     8630   3724   7801    897   1238  -1151       C  
ATOM   1401  CG  ASP A  99      42.835  16.590   2.908  1.00 69.69           C  
ANISOU 1401  CG  ASP A  99    11278   5835   9366    645   1259  -1455       C  
ATOM   1402  OD1 ASP A  99      41.590  16.589   2.954  1.00 62.10           O  
ANISOU 1402  OD1 ASP A  99    10416   5051   8130    488    836  -1472       O  
ATOM   1403  OD2 ASP A  99      43.486  16.555   1.852  1.00 62.09           O  
ANISOU 1403  OD2 ASP A  99    10646   4691   8255    587   1701  -1679       O  
ATOM   1404  H   ASP A  99      42.353  18.687   4.978  1.00 53.96           H  
ATOM   1405  HA  ASP A  99      42.067  16.050   5.424  1.00 57.90           H  
ATOM   1406  HB2 ASP A  99      44.218  17.414   4.176  1.00 63.97           H  
ATOM   1407  HB3 ASP A  99      44.154  15.835   4.280  1.00 63.97           H  
ATOM   1408  N   GLU A 100      44.065  17.600   7.363  1.00 44.90           N  
ANISOU 1408  N   GLU A 100     6632   3026   7401   1217    600   -442       N  
ATOM   1409  CA  GLU A 100      44.784  17.478   8.650  1.00 56.85           C  
ANISOU 1409  CA  GLU A 100     7750   4514   9335   1380    469   -159       C  
ATOM   1410  C   GLU A 100      43.832  16.903   9.693  1.00 49.08           C  
ANISOU 1410  C   GLU A 100     6738   3571   8340   1344    163    -14       C  
ATOM   1411  O   GLU A 100      44.318  16.191  10.573  1.00 50.32           O  
ANISOU 1411  O   GLU A 100     6692   3684   8742   1430     89    202       O  
ATOM   1412  CB  GLU A 100      45.376  18.800   9.134  1.00 43.71           C  
ANISOU 1412  CB  GLU A 100     5863   3104   7643   1408    290     -1       C  
ATOM   1413  CG  GLU A 100      46.583  19.267   8.349  1.00 59.85           C  
ANISOU 1413  CG  GLU A 100     7819   5053   9868   1469    635    -70       C  
ATOM   1414  CD  GLU A 100      47.856  18.468   8.553  1.00 59.62           C  
ANISOU 1414  CD  GLU A 100     7471   4883  10297   1575    814     27       C  
ATOM   1415  OE1 GLU A 100      47.992  17.832   9.612  1.00 72.14           O  
ANISOU 1415  OE1 GLU A 100     8864   6494  12051   1621    574    221       O  
ATOM   1416  OE2 GLU A 100      48.704  18.484   7.646  1.00 56.53           O  
ANISOU 1416  OE2 GLU A 100     7035   4371  10073   1590   1204    -81       O  
ATOM   1417  H   GLU A 100      44.004  18.447   7.036  1.00 54.20           H  
ATOM   1418  HA  GLU A 100      45.519  16.839   8.523  1.00 68.54           H  
ATOM   1419  HB2 GLU A 100      44.685  19.486   9.082  1.00 52.77           H  
ATOM   1420  HB3 GLU A 100      45.625  18.703  10.077  1.00 52.77           H  
ATOM   1421  HG2 GLU A 100      46.366  19.249   7.398  1.00 72.14           H  
ATOM   1422  HG3 GLU A 100      46.765  20.199   8.587  1.00 72.14           H  
ATOM   1423  N   TYR A 101      42.539  17.190   9.610  1.00 43.98           N  
ANISOU 1423  N   TYR A 101     6301   3088   7323   1177    -21   -120       N  
ATOM   1424  CA  TYR A 101      41.550  16.765  10.629  1.00 46.64           C  
ANISOU 1424  CA  TYR A 101     6569   3510   7641   1130   -286     46       C  
ATOM   1425  C   TYR A 101      41.376  15.247  10.601  1.00 53.19           C  
ANISOU 1425  C   TYR A 101     7474   4041   8695   1116   -166     22       C  
ATOM   1426  O   TYR A 101      40.778  14.747  11.549  1.00 59.18           O  
ANISOU 1426  O   TYR A 101     8197   4799   9489   1075   -313    179       O  
ATOM   1427  CB  TYR A 101      40.212  17.511  10.511  1.00 58.60           C  
ANISOU 1427  CB  TYR A 101     8204   5265   8795    967   -485    -51       C  
ATOM   1428  CG  TYR A 101      39.690  18.055  11.814  1.00 44.67           C  
ANISOU 1428  CG  TYR A 101     6328   3678   6965    924   -715    129       C  
ATOM   1429  CD1 TYR A 101      40.096  19.294  12.277  1.00 48.52           C  
ANISOU 1429  CD1 TYR A 101     6704   4386   7347    958   -839    243       C  
ATOM   1430  CD2 TYR A 101      38.800  17.334  12.587  1.00 52.95           C  
ANISOU 1430  CD2 TYR A 101     7401   4659   8058    832   -763    171       C  
ATOM   1431  CE1 TYR A 101      39.628  19.805  13.474  1.00 35.27           C  
ANISOU 1431  CE1 TYR A 101     4983   2856   5561    896   -986    360       C  
ATOM   1432  CE2 TYR A 101      38.322  17.831  13.786  1.00 55.10           C  
ANISOU 1432  CE2 TYR A 101     7611   5084   8240    777   -892    322       C  
ATOM   1433  CZ  TYR A 101      38.737  19.071  14.230  1.00 40.66           C  
ANISOU 1433  CZ  TYR A 101     5710   3473   6264    809   -995    405       C  
ATOM   1434  OH  TYR A 101      38.268  19.557  15.413  1.00 59.08           O  
ANISOU 1434  OH  TYR A 101     8038   5938   8472    734  -1063    510       O  
ATOM   1435  H   TYR A 101      42.169  17.636   8.914  1.00 53.10           H  
ATOM   1436  HA  TYR A 101      41.929  16.994  11.514  1.00 56.28           H  
ATOM   1437  HB2 TYR A 101      40.316  18.256   9.885  1.00 70.63           H  
ATOM   1438  HB3 TYR A 101      39.548  16.897  10.134  1.00 70.63           H  
ATOM   1439  HD1 TYR A 101      40.704  19.802  11.766  1.00 58.55           H  
ATOM   1440  HD2 TYR A 101      38.511  16.486  12.292  1.00 63.86           H  
ATOM   1441  HE1 TYR A 101      39.915  20.652  13.772  1.00 42.64           H  
ATOM   1442  HE2 TYR A 101      37.714  17.325  14.300  1.00 66.43           H  
ATOM   1443  HH  TYR A 101      38.002  20.366  15.319  1.00 71.21           H  
ATOM   1444  N   ALA A 102      41.767  14.562   9.531  1.00 46.95           N  
ANISOU 1444  N   ALA A 102     6819   2965   8053   1132    149   -189       N  
ATOM   1445  CA  ALA A 102      41.690  13.087   9.431  1.00 49.42           C  
ANISOU 1445  CA  ALA A 102     7205   2964   8608   1121    330   -236       C  
ATOM   1446  C   ALA A 102      43.045  12.434   9.686  1.00 57.01           C  
ANISOU 1446  C   ALA A 102     7961   3829   9869   1292    507    -77       C  
ATOM   1447  O   ALA A 102      43.071  11.205   9.699  1.00 71.86           O  
ANISOU 1447  O   ALA A 102     9857   5494  11952   1297    628    -59       O  
ATOM   1448  CB  ALA A 102      41.171  12.715   8.077  1.00 65.93           C  
ANISOU 1448  CB  ALA A 102     9637   4862  10552    944    546   -640       C  
ATOM   1449  H   ALA A 102      42.099  14.947   8.776  1.00 56.66           H  
ATOM   1450  HA  ALA A 102      41.055  12.754  10.104  1.00 59.62           H  
ATOM   1451  HB1 ALA A 102      41.893  12.749   7.427  1.00 79.43           H  
ATOM   1452  HB2 ALA A 102      40.805  11.819   8.109  1.00 79.43           H  
ATOM   1453  HB3 ALA A 102      40.469  13.335   7.816  1.00 79.43           H  
ATOM   1454  N   CYS A 103      44.120  13.200   9.876  1.00 63.85           N  
ANISOU 1454  N   CYS A 103     5725   7225  11312   1777    680   1790       N  
ATOM   1455  CA  CYS A 103      45.492  12.689  10.162  1.00 59.30           C  
ANISOU 1455  CA  CYS A 103     4939   6675  10919   1897    677   1912       C  
ATOM   1456  C   CYS A 103      45.960  13.192  11.524  1.00 59.02           C  
ANISOU 1456  C   CYS A 103     4724   6486  11214   1595    433   1985       C  
ATOM   1457  O   CYS A 103      47.175  13.242  11.726  1.00 74.94           O  
ANISOU 1457  O   CYS A 103     6440   8540  13494   1638    424   2182       O  
ATOM   1458  CB  CYS A 103      46.465  13.121   9.076  1.00 62.48           C  
ANISOU 1458  CB  CYS A 103     5049   7304  11388   2174    996   2206       C  
ATOM   1459  SG  CYS A 103      47.310  14.690   9.389  1.00 72.38           S  
ANISOU 1459  SG  CYS A 103     5840   8605  13055   1958   1083   2592       S  
ATOM   1460  H   CYS A 103      44.096  14.106   9.834  1.00 76.94           H  
ATOM   1461  HA  CYS A 103      45.464  11.707  10.183  1.00 69.57           H  
ATOM   1462  HB2 CYS A 103      47.143  12.423   8.965  1.00 73.39           H  
ATOM   1463  HB3 CYS A 103      45.978  13.199   8.231  1.00 73.39           H  
ATOM   1464  HG  CYS A 103      48.119  14.295  10.186  1.00 87.17           H  
ATOM   1465  N   LEU A 104      45.053  13.518  12.438  1.00 57.69           N  
ANISOU 1465  N   LEU A 104     4742   6142  11033   1304    229   1828       N  
ATOM   1466  CA  LEU A 104      45.419  14.159  13.726  1.00 60.77           C  
ANISOU 1466  CA  LEU A 104     5024   6370  11695   1018    -16   1884       C  
ATOM   1467  C   LEU A 104      46.264  13.238  14.588  1.00 68.14           C  
ANISOU 1467  C   LEU A 104     5940   7226  12725   1053   -214   1853       C  
ATOM   1468  O   LEU A 104      46.009  12.028  14.594  1.00 64.55           O  
ANISOU 1468  O   LEU A 104     5687   6767  12073   1226   -220   1694       O  
ATOM   1469  CB  LEU A 104      44.180  14.598  14.515  1.00 55.43           C  
ANISOU 1469  CB  LEU A 104     4632   5516  10912    762   -168   1684       C  
ATOM   1470  CG  LEU A 104      43.335  15.719  13.910  1.00 53.10           C  
ANISOU 1470  CG  LEU A 104     4348   5248  10579    675    -39   1719       C  
ATOM   1471  CD1 LEU A 104      42.025  15.856  14.667  1.00 50.66           C  
ANISOU 1471  CD1 LEU A 104     4363   4791  10094    519   -144   1473       C  
ATOM   1472  CD2 LEU A 104      44.080  17.048  13.882  1.00 54.58           C  
ANISOU 1472  CD2 LEU A 104     4266   5389  11082    501    -80   1953       C  
ATOM   1473  H   LEU A 104      44.168  13.342  12.340  1.00 69.54           H  
ATOM   1474  HA  LEU A 104      45.958  14.954  13.515  1.00 73.24           H  
ATOM   1475  HB2 LEU A 104      43.609  13.815  14.640  1.00 66.83           H  
ATOM   1476  HB3 LEU A 104      44.475  14.883  15.403  1.00 66.83           H  
ATOM   1477  HG  LEU A 104      43.124  15.472  12.979  1.00 62.13           H  
ATOM   1478 HD11 LEU A 104      41.494  16.571  14.274  1.00 59.20           H  
ATOM   1479 HD12 LEU A 104      41.531  15.020  14.611  1.00 59.20           H  
ATOM   1480 HD13 LEU A 104      42.207  16.062  15.600  1.00 59.20           H  
ATOM   1481 HD21 LEU A 104      43.488  17.743  13.545  1.00 64.98           H  
ATOM   1482 HD22 LEU A 104      44.369  17.280  14.778  1.00 64.98           H  
ATOM   1483 HD23 LEU A 104      44.855  16.978  13.301  1.00 64.98           H  
ATOM   1484  N   SER A 105      47.181  13.822  15.341  1.00 59.13           N  
ANISOU 1484  N   SER A 105     4564   6003  11901    883   -406   2008       N  
ATOM   1485  CA  SER A 105      48.055  13.075  16.259  1.00 60.37           C  
ANISOU 1485  CA  SER A 105     4694   6070  12175    896   -649   1995       C  
ATOM   1486  C   SER A 105      47.239  12.505  17.402  1.00 58.18           C  
ANISOU 1486  C   SER A 105     4844   5585  11677    755   -884   1715       C  
ATOM   1487  O   SER A 105      46.234  13.125  17.743  1.00 60.09           O  
ANISOU 1487  O   SER A 105     5332   5728  11772    577   -904   1573       O  
ATOM   1488  CB  SER A 105      49.121  13.995  16.793  1.00 85.01           C  
ANISOU 1488  CB  SER A 105     7459   9133  15707    716   -852   2231       C  
ATOM   1489  OG  SER A 105      48.555  15.047  17.558  1.00 74.76           O  
ANISOU 1489  OG  SER A 105     6273   7661  14471    401  -1035   2187       O  
ATOM   1490  H   SER A 105      47.306  14.723  15.389  1.00 69.37           H  
ATOM   1491  HA  SER A 105      48.484  12.330  15.758  1.00 72.09           H  
ATOM   1492  HB2 SER A 105      49.742  13.479  17.356  1.00102.33           H  
ATOM   1493  HB3 SER A 105      49.632  14.374  16.042  1.00102.33           H  
ATOM   1494  HG  SER A 105      49.176  15.555  17.822  1.00 90.03           H  
ATOM   1495  N   THR A 106      47.657  11.376  17.967  1.00 77.34           N  
ANISOU 1495  N   THR A 106     7354   7950  14082    856  -1042   1655       N  
ATOM   1496  CA  THR A 106      47.027  10.796  19.171  1.00 57.69           C  
ANISOU 1496  CA  THR A 106     5245   5253  11421    728  -1283   1445       C  
ATOM   1497  C   THR A 106      48.007  11.051  20.299  1.00 63.27           C  
ANISOU 1497  C   THR A 106     5850   5829  12359    605  -1627   1537       C  
ATOM   1498  O   THR A 106      49.187  11.202  20.009  1.00 75.02           O  
ANISOU 1498  O   THR A 106     6967   7405  14133    699  -1674   1745       O  
ATOM   1499  CB  THR A 106      46.644   9.318  19.015  1.00 70.98           C  
ANISOU 1499  CB  THR A 106     7175   6933  12859    944  -1217   1289       C  
ATOM   1500  OG1 THR A 106      46.101   8.882  20.261  1.00 68.29           O  
ANISOU 1500  OG1 THR A 106     7206   6384  12358    804  -1431   1118       O  
ATOM   1501  CG2 THR A 106      47.787   8.400  18.639  1.00 78.03           C  
ANISOU 1501  CG2 THR A 106     7829   7920  13898   1216  -1212   1423       C  
ATOM   1502  H   THR A 106      48.387  10.913  17.687  1.00 93.13           H  
ATOM   1503  HA  THR A 106      46.208  11.303  19.359  1.00 68.91           H  
ATOM   1504  HB  THR A 106      45.943   9.252  18.322  1.00 85.49           H  
ATOM   1505  HG1 THR A 106      45.361   9.269  20.407  1.00 82.27           H  
ATOM   1506 HG21 THR A 106      47.484   7.475  18.678  1.00 93.95           H  
ATOM   1507 HG22 THR A 106      48.086   8.601  17.734  1.00 93.95           H  
ATOM   1508 HG23 THR A 106      48.526   8.522  19.261  1.00 93.95           H  
ATOM   1509  N   TYR A 107      47.527  11.140  21.523  1.00 70.91           N  
ANISOU 1509  N   TYR A 107     7144   6589  13208    401  -1870   1393       N  
ATOM   1510  CA  TYR A 107      48.407  11.292  22.695  1.00 70.25           C  
ANISOU 1510  CA  TYR A 107     7043   6355  13293    288  -2250   1451       C  
ATOM   1511  C   TYR A 107      49.215   9.989  22.776  1.00 68.95           C  
ANISOU 1511  C   TYR A 107     6843   6205  13149    507  -2352   1480       C  
ATOM   1512  O   TYR A 107      48.639   8.923  22.508  1.00 70.00           O  
ANISOU 1512  O   TYR A 107     7227   6338  13033    660  -2223   1344       O  
ATOM   1513  CB  TYR A 107      47.589  11.665  23.933  1.00 69.41           C  
ANISOU 1513  CB  TYR A 107     7381   6019  12973     70  -2457   1270       C  
ATOM   1514  CG  TYR A 107      46.768  12.922  23.804  1.00 66.99           C  
ANISOU 1514  CG  TYR A 107     7139   5677  12635   -116  -2352   1228       C  
ATOM   1515  CD2 TYR A 107      45.436  12.874  23.429  1.00 70.00           C  
ANISOU 1515  CD2 TYR A 107     7783   6070  12744   -122  -2099   1071       C  
ATOM   1516  CD1 TYR A 107      47.318  14.163  24.068  1.00 68.01           C  
ANISOU 1516  CD1 TYR A 107     7059   5749  13032   -287  -2521   1354       C  
ATOM   1517  CE2 TYR A 107      44.676  14.025  23.314  1.00 72.56           C  
ANISOU 1517  CE2 TYR A 107     8161   6361  13048   -264  -2000   1038       C  
ATOM   1518  CE1 TYR A 107      46.571  15.323  23.957  1.00 75.75           C  
ANISOU 1518  CE1 TYR A 107     8123   6674  13985   -440  -2428   1313       C  
ATOM   1519  CZ  TYR A 107      45.244  15.254  23.579  1.00 70.48           C  
ANISOU 1519  CZ  TYR A 107     7719   6032  13030   -413  -2159   1154       C  
ATOM   1520  OH  TYR A 107      44.491  16.383  23.470  1.00 69.60           O  
ANISOU 1520  OH  TYR A 107     7684   5864  12899   -537  -2064   1119       O  
ATOM   1521  H   TYR A 107      46.653  11.020  21.737  1.00 85.41           H  
ATOM   1522  HA  TYR A 107      49.033  12.035  22.509  1.00 84.62           H  
ATOM   1523  HB2 TYR A 107      46.992  10.919  24.144  1.00 83.61           H  
ATOM   1524  HB3 TYR A 107      48.205  11.769  24.687  1.00 83.61           H  
ATOM   1525  HD2 TYR A 107      45.037  12.040  23.246  1.00 84.32           H  
ATOM   1526  HD1 TYR A 107      48.222  14.222  24.328  1.00 81.93           H  
ATOM   1527  HE2 TYR A 107      43.772  13.972  23.054  1.00 87.39           H  
ATOM   1528  HE1 TYR A 107      46.966  16.158  24.142  1.00 91.22           H  
ATOM   1529  HH  TYR A 107      44.876  16.950  22.957  1.00 83.84           H  
ATOM   1530  N   PRO A 108      50.506  10.000  23.164  1.00 71.68           N  
ANISOU 1530  N   PRO A 108     6877   6551  13807    527  -2597   1661       N  
ATOM   1531  CA  PRO A 108      51.354   8.792  23.109  1.00 82.27           C  
ANISOU 1531  CA  PRO A 108     8107   7940  15210    792  -2647   1723       C  
ATOM   1532  C   PRO A 108      50.908   7.655  24.033  1.00 71.20           C  
ANISOU 1532  C   PRO A 108     7177   6360  13517    830  -2820   1534       C  
ATOM   1533  O   PRO A 108      51.291   6.549  23.788  1.00 67.89           O  
ANISOU 1533  O   PRO A 108     6759   5968  13067   1084  -2789   1540       O  
ATOM   1534  CB  PRO A 108      52.731   9.337  23.525  1.00 71.18           C  
ANISOU 1534  CB  PRO A 108     6271   6536  14237    738  -2946   1962       C  
ATOM   1535  CG  PRO A 108      52.408  10.499  24.422  1.00 71.94           C  
ANISOU 1535  CG  PRO A 108     6481   6466  14389    389  -3212   1931       C  
ATOM   1536  CD  PRO A 108      51.214  11.140  23.754  1.00 67.76           C  
ANISOU 1536  CD  PRO A 108     6130   5982  13635    303  -2880   1813       C  
ATOM   1537  HA  PRO A 108      51.399   8.467  22.175  1.00 99.04           H  
ATOM   1538  HB2 PRO A 108      53.249   8.657  24.005  1.00 84.28           H  
ATOM   1539  HB3 PRO A 108      53.242   9.631  22.741  1.00 84.28           H  
ATOM   1540  HG2 PRO A 108      52.183  10.195  25.326  1.00 86.65           H  
ATOM   1541  HG3 PRO A 108      53.160  11.125  24.472  1.00 86.65           H  
ATOM   1542  HD2 PRO A 108      50.656  11.602  24.406  1.00 79.72           H  
ATOM   1543  HD3 PRO A 108      51.493  11.772  23.067  1.00 79.72           H  
ATOM   1544  N   ASP A 109      50.119   7.959  25.047  1.00 65.69           N  
ANISOU 1544  N   ASP A 109     6890   5473  12597    604  -2983   1378       N  
ATOM   1545  CA  ASP A 109      49.664   6.980  26.057  1.00 65.30           C  
ANISOU 1545  CA  ASP A 109     7300   5237  12275    616  -3157   1236       C  
ATOM   1546  C   ASP A 109      48.299   6.372  25.729  1.00 64.79           C  
ANISOU 1546  C   ASP A 109     7595   5150  11871    642  -2866   1053       C  
ATOM   1547  O   ASP A 109      47.783   5.671  26.593  1.00 64.15           O  
ANISOU 1547  O   ASP A 109     7933   4900  11544    603  -2964    940       O  
ATOM   1548  CB  ASP A 109      49.581   7.709  27.393  1.00 66.09           C  
ANISOU 1548  CB  ASP A 109     7673   5130  12309    372  -3510   1188       C  
ATOM   1549  CG  ASP A 109      48.564   8.832  27.421  1.00 70.63           C  
ANISOU 1549  CG  ASP A 109     8466   5660  12710    160  -3358   1068       C  
ATOM   1550  OD1 ASP A 109      48.098   9.229  26.341  1.00 62.01           O  
ANISOU 1550  OD1 ASP A 109     7178   4721  11662    168  -3035   1076       O  
ATOM   1551  OD2 ASP A 109      48.275   9.309  28.516  1.00 80.47           O  
ANISOU 1551  OD2 ASP A 109    10094   6717  13764      5  -3554    969       O  
ATOM   1552  H   ASP A 109      49.791   8.794  25.164  1.00 79.15           H  
ATOM   1553  HA  ASP A 109      50.329   6.257  26.130  1.00 78.57           H  
ATOM   1554  HB2 ASP A 109      49.359   7.071  28.101  1.00 77.72           H  
ATOM   1555  HB3 ASP A 109      50.459   8.091  27.593  1.00 77.72           H  
ATOM   1556  N   THR A 110      47.705   6.641  24.566  1.00 62.77           N  
ANISOU 1556  N   THR A 110     7189   5056  11603    701  -2524   1035       N  
ATOM   1557  CA  THR A 110      46.310   6.212  24.275  1.00 59.55           C  
ANISOU 1557  CA  THR A 110     7096   4618  10914    666  -2289    865       C  
ATOM   1558  C   THR A 110      46.225   4.775  23.762  1.00 58.39           C  
ANISOU 1558  C   THR A 110     7065   4471  10647    896  -2173    801       C  
ATOM   1559  O   THR A 110      45.479   4.010  24.366  1.00 57.69           O  
ANISOU 1559  O   THR A 110     7347   4231  10340    854  -2182    679       O  
ATOM   1560  CB  THR A 110      45.628   7.202  23.328  1.00 62.39           C  
ANISOU 1560  CB  THR A 110     7279   5125  11299    596  -2022    863       C  
ATOM   1561  OG1 THR A 110      45.868   8.512  23.839  1.00 77.25           O  
ANISOU 1561  OG1 THR A 110     9109   6963  13280    376  -2140    907       O  
ATOM   1562  CG2 THR A 110      44.141   6.970  23.197  1.00 54.27           C  
ANISOU 1562  CG2 THR A 110     6535   4068  10016    557  -1808    698       C  
ATOM   1563  H   THR A 110      48.107   7.060  23.865  1.00 75.64           H  
ATOM   1564  HA  THR A 110      45.818   6.244  25.124  1.00 71.78           H  
ATOM   1565  HB  THR A 110      46.045   7.123  22.438  1.00 75.18           H  
ATOM   1566  HG1 THR A 110      45.522   9.090  23.325  1.00 93.02           H  
ATOM   1567 HG21 THR A 110      43.763   7.630  22.589  1.00 63.53           H  
ATOM   1568 HG22 THR A 110      43.980   6.080  22.845  1.00 63.53           H  
ATOM   1569 HG23 THR A 110      43.718   7.055  24.070  1.00 63.53           H  
ATOM   1570  N   VAL A 111      46.959   4.429  22.714  1.00 59.54           N  
ANISOU 1570  N   VAL A 111     6915   4775  10932   1145  -2054    886       N  
ATOM   1571  CA  VAL A 111      46.901   3.056  22.127  1.00 69.21           C  
ANISOU 1571  CA  VAL A 111     8275   5983  12040   1399  -1955    812       C  
ATOM   1572  C   VAL A 111      47.414   2.053  23.166  1.00 61.60           C  
ANISOU 1572  C   VAL A 111     7558   4818  11030   1443  -2218    799       C  
ATOM   1573  O   VAL A 111      46.725   1.069  23.386  1.00 60.97           O  
ANISOU 1573  O   VAL A 111     7852   4575  10740   1423  -2220    669       O  
ATOM   1574  CB  VAL A 111      47.622   2.936  20.775  1.00 71.86           C  
ANISOU 1574  CB  VAL A 111     8251   6527  12527   1701  -1772    924       C  
ATOM   1575  CG1 VAL A 111      47.893   1.485  20.400  1.00 63.25           C  
ANISOU 1575  CG1 VAL A 111     7317   5370  11346   2008  -1759    862       C  
ATOM   1576  CG2 VAL A 111      46.842   3.629  19.668  1.00 60.08           C  
ANISOU 1576  CG2 VAL A 111     6656   5202  10968   1693  -1477    895       C  
ATOM   1577  H   VAL A 111      47.534   4.996  22.298  1.00 70.10           H  
ATOM   1578  HA  VAL A 111      45.961   2.851  21.970  1.00 83.37           H  
ATOM   1579  HB  VAL A 111      48.493   3.387  20.856  1.00 86.55           H  
ATOM   1580 HG11 VAL A 111      48.083   1.426  19.448  1.00 74.31           H  
ATOM   1581 HG12 VAL A 111      48.659   1.154  20.900  1.00 74.31           H  
ATOM   1582 HG13 VAL A 111      47.111   0.941  20.604  1.00 74.31           H  
ATOM   1583 HG21 VAL A 111      47.411   3.736  18.887  1.00 70.50           H  
ATOM   1584 HG22 VAL A 111      46.066   3.090  19.432  1.00 70.50           H  
ATOM   1585 HG23 VAL A 111      46.547   4.504  19.974  1.00 70.50           H  
ATOM   1586  N   PRO A 112      48.497   2.319  23.920  1.00 63.88           N  
ANISOU 1586  N   PRO A 112     7649   5101  11521   1500  -2457    942       N  
ATOM   1587  CA  PRO A 112      48.924   1.393  24.950  1.00 71.87           C  
ANISOU 1587  CA  PRO A 112     8934   5907  12466   1537  -2738    934       C  
ATOM   1588  C   PRO A 112      47.868   1.163  26.030  1.00 64.04           C  
ANISOU 1588  C   PRO A 112     8417   4706  11208   1290  -2825    811       C  
ATOM   1589  O   PRO A 112      47.663   0.039  26.388  1.00 64.60           O  
ANISOU 1589  O   PRO A 112     8827   4601  11116   1352  -2890    751       O  
ATOM   1590  CB  PRO A 112      50.136   2.085  25.573  1.00 67.95           C  
ANISOU 1590  CB  PRO A 112     8118   5447  12251   1535  -3026   1113       C  
ATOM   1591  CG  PRO A 112      50.674   2.937  24.466  1.00 82.55           C  
ANISOU 1591  CG  PRO A 112     9451   7546  14368   1608  -2833   1248       C  
ATOM   1592  CD  PRO A 112      49.426   3.444  23.788  1.00 77.76           C  
ANISOU 1592  CD  PRO A 112     8899   7049  13596   1619  -2453   1136       C  
ATOM   1593  HA  PRO A 112      49.200   0.535  24.540  1.00 86.56           H  
ATOM   1594  HB2 PRO A 112      49.873   2.636  26.342  1.00 79.94           H  
ATOM   1595  HB3 PRO A 112      50.804   1.430  25.867  1.00 79.94           H  
ATOM   1596  HG2 PRO A 112      51.208   3.678  24.818  1.00 99.38           H  
ATOM   1597  HG3 PRO A 112      51.220   2.410  23.848  1.00 99.38           H  
ATOM   1598  HD2 PRO A 112      49.085   4.236  24.240  1.00 93.63           H  
ATOM   1599  HD3 PRO A 112      49.601   3.658  22.854  1.00 93.63           H  
ATOM   1600  N   ALA A 113      47.219   2.213  26.514  1.00 64.86           N  
ANISOU 1600  N   ALA A 113     8566   4815  11264   1026  -2814    784       N  
ATOM   1601  CA  ALA A 113      46.201   2.106  27.579  1.00 64.48           C  
ANISOU 1601  CA  ALA A 113     8967   4580  10953    819  -2852    686       C  
ATOM   1602  C   ALA A 113      44.994   1.338  27.053  1.00 66.20           C  
ANISOU 1602  C   ALA A 113     9421   4748  10982    815  -2592    566       C  
ATOM   1603  O   ALA A 113      44.380   0.586  27.823  1.00 60.25           O  
ANISOU 1603  O   ALA A 113     9048   3806  10039    757  -2630    522       O  
ATOM   1604  CB  ALA A 113      45.801   3.459  28.084  1.00 73.53           C  
ANISOU 1604  CB  ALA A 113    10104   5746  12088    576  -2859    676       C  
ATOM   1605  H   ALA A 113      47.328   3.065  26.208  1.00 78.16           H  
ATOM   1606  HA  ALA A 113      46.589   1.593  28.329  1.00 77.69           H  
ATOM   1607  HB1 ALA A 113      45.134   3.359  28.784  1.00 88.55           H  
ATOM   1608  HB2 ALA A 113      46.579   3.916  28.445  1.00 88.55           H  
ATOM   1609  HB3 ALA A 113      45.426   3.984  27.356  1.00 88.55           H  
ATOM   1610  N   LEU A 114      44.627   1.585  25.804  1.00 58.50           N  
ANISOU 1610  N   LEU A 114     8232   3932  10064    870  -2340    523       N  
ATOM   1611  CA  LEU A 114      43.455   0.919  25.211  1.00 57.31           C  
ANISOU 1611  CA  LEU A 114     8281   3727   9768    857  -2140    406       C  
ATOM   1612  C   LEU A 114      43.742  -0.583  25.160  1.00 60.54           C  
ANISOU 1612  C   LEU A 114     8874   3998  10132   1055  -2213    380       C  
ATOM   1613  O   LEU A 114      42.856  -1.346  25.524  1.00 61.44           O  
ANISOU 1613  O   LEU A 114     9297   3942  10105    981  -2173    306       O  
ATOM   1614  CB  LEU A 114      43.173   1.516  23.832  1.00 55.85           C  
ANISOU 1614  CB  LEU A 114     7833   3743   9644    897  -1902    367       C  
ATOM   1615  CG  LEU A 114      42.465   2.871  23.839  1.00 57.69           C  
ANISOU 1615  CG  LEU A 114     7942   4077   9900    686  -1804    378       C  
ATOM   1616  CD1 LEU A 114      42.603   3.549  22.494  1.00 53.51           C  
ANISOU 1616  CD1 LEU A 114     7066   3775   9490    783  -1633    410       C  
ATOM   1617  CD2 LEU A 114      40.995   2.742  24.212  1.00 52.80           C  
ANISOU 1617  CD2 LEU A 114     7588   3353   9121    478  -1686    284       C  
ATOM   1618  H   LEU A 114      45.074   2.155  25.254  1.00 68.61           H  
ATOM   1619  HA  LEU A 114      42.683   1.069  25.800  1.00 67.18           H  
ATOM   1620  HB2 LEU A 114      44.019   1.605  23.351  1.00 65.43           H  
ATOM   1621  HB3 LEU A 114      42.620   0.881  23.333  1.00 65.43           H  
ATOM   1622  HG  LEU A 114      42.901   3.444  24.516  1.00 69.55           H  
ATOM   1623 HD11 LEU A 114      42.177   4.420  22.533  1.00 62.62           H  
ATOM   1624 HD12 LEU A 114      43.545   3.658  22.277  1.00 62.62           H  
ATOM   1625 HD13 LEU A 114      42.174   3.007  21.809  1.00 62.62           H  
ATOM   1626 HD21 LEU A 114      40.571   3.617  24.168  1.00 61.77           H  
ATOM   1627 HD22 LEU A 114      40.552   2.139  23.590  1.00 61.77           H  
ATOM   1628 HD23 LEU A 114      40.913   2.392  25.115  1.00 61.77           H  
ATOM   1629  N   ARG A 115      44.954  -0.981  24.786  1.00 60.72           N  
ANISOU 1629  N   ARG A 115     8701   4079  10290   1311  -2316    453       N  
ATOM   1630  CA  ARG A 115      45.348  -2.407  24.702  1.00 62.59           C  
ANISOU 1630  CA  ARG A 115     9128   4164  10488   1534  -2398    429       C  
ATOM   1631  C   ARG A 115      45.252  -3.001  26.109  1.00 63.71           C  
ANISOU 1631  C   ARG A 115     9634   4058  10516   1433  -2615    458       C  
ATOM   1632  O   ARG A 115      44.728  -4.103  26.226  1.00 64.49           O  
ANISOU 1632  O   ARG A 115    10048   3954  10502   1472  -2629    403       O  
ATOM   1633  CB  ARG A 115      46.735  -2.550  24.077  1.00 64.66           C  
ANISOU 1633  CB  ARG A 115     9071   4557  10938   1858  -2442    523       C  
ATOM   1634  CG  ARG A 115      46.810  -2.300  22.577  1.00 64.23           C  
ANISOU 1634  CG  ARG A 115     8739   4722  10942   2038  -2183    496       C  
ATOM   1635  CD  ARG A 115      48.166  -2.720  22.040  1.00 66.90           C  
ANISOU 1635  CD  ARG A 115     8793   5175  11451   2411  -2180    603       C  
ATOM   1636  NE  ARG A 115      48.578  -2.038  20.819  1.00 72.42           N  
ANISOU 1636  NE  ARG A 115     9167   6128  12220   2580  -1915    637       N  
ATOM   1637  CZ  ARG A 115      48.204  -2.334  19.571  1.00 69.27           C  
ANISOU 1637  CZ  ARG A 115     8880   5762  11679   2776  -1709    516       C  
ATOM   1638  NH1 ARG A 115      47.347  -3.309  19.309  1.00 72.65           N  
ANISOU 1638  NH1 ARG A 115     9721   5967  11917   2808  -1757    346       N  
ATOM   1639  NH2 ARG A 115      48.686  -1.623  18.567  1.00 67.23           N  
ANISOU 1639  NH2 ARG A 115     8338   5745  11463   2943  -1464    572       N  
ATOM   1640  H   ARG A 115      45.614  -0.395  24.565  1.00 71.27           H  
ATOM   1641  HA  ARG A 115      44.697  -2.869  24.126  1.00 73.51           H  
ATOM   1642  HB2 ARG A 115      47.343  -1.928  24.528  1.00 75.99           H  
ATOM   1643  HB3 ARG A 115      47.057  -3.458  24.256  1.00 75.99           H  
ATOM   1644  HG2 ARG A 115      46.109  -2.812  22.122  1.00 75.48           H  
ATOM   1645  HG3 ARG A 115      46.668  -1.350  22.390  1.00 75.48           H  
ATOM   1646  HD2 ARG A 115      48.840  -2.546  22.731  1.00 78.69           H  
ATOM   1647  HD3 ARG A 115      48.161  -3.688  21.883  1.00 78.69           H  
ATOM   1648  HE  ARG A 115      49.149  -1.387  20.913  1.00 87.22           H  
ATOM   1649 HH11 ARG A 115      47.013  -3.793  19.949  1.00 87.50           H  
ATOM   1650 HH12 ARG A 115      47.115  -3.475  18.479  1.00 87.50           H  
ATOM   1651 HH21 ARG A 115      49.252  -0.967  18.720  1.00 79.09           H  
ATOM   1652 HH22 ARG A 115      48.437  -1.800  17.742  1.00 79.09           H  
ATOM   1653  N   LYS A 116      45.656  -2.269  27.142  1.00 64.08           N  
ANISOU 1653  N   LYS A 116     9671   4099  10578   1301  -2795    545       N  
ATOM   1654  CA  LYS A 116      45.611  -2.752  28.540  1.00 65.41           C  
ANISOU 1654  CA  LYS A 116    10230   4034  10590   1216  -2999    580       C  
ATOM   1655  C   LYS A 116      44.168  -3.002  28.954  1.00 69.44           C  
ANISOU 1655  C   LYS A 116    11100   4400  10884    987  -2831    508       C  
ATOM   1656  O   LYS A 116      43.925  -4.012  29.618  1.00 67.15           O  
ANISOU 1656  O   LYS A 116    11164   3887  10463    986  -2883    518       O  
ATOM   1657  CB  LYS A 116      46.272  -1.775  29.513  1.00 66.29           C  
ANISOU 1657  CB  LYS A 116    10294   4163  10729   1116  -3246    668       C  
ATOM   1658  CG  LYS A 116      47.787  -1.676  29.440  1.00 68.39           C  
ANISOU 1658  CG  LYS A 116    10207   4531  11247   1308  -3491    784       C  
ATOM   1659  CD  LYS A 116      48.344  -0.601  30.353  1.00 90.91           C  
ANISOU 1659  CD  LYS A 116    13111   7342  14089   1142  -3783    846       C  
ATOM   1660  CE  LYS A 116      49.827  -0.348  30.172  1.00 96.88           C  
ANISOU 1660  CE  LYS A 116    13441   8215  15155   1243  -4051    976       C  
ATOM   1661  NZ  LYS A 116      50.127   0.381  28.916  1.00 99.72           N  
ANISOU 1661  NZ  LYS A 116    13287   8806  15797   1408  -3849   1029       N  
ATOM   1662  H   LYS A 116      45.981  -1.424  27.048  1.00 75.31           H  
ATOM   1663  HA  LYS A 116      46.097  -3.608  28.581  1.00 76.90           H  
ATOM   1664  HB2 LYS A 116      45.897  -0.884  29.358  1.00 77.95           H  
ATOM   1665  HB3 LYS A 116      46.026  -2.040  30.424  1.00 77.95           H  
ATOM   1666  HG2 LYS A 116      48.174  -2.542  29.690  1.00 80.48           H  
ATOM   1667  HG3 LYS A 116      48.048  -1.486  28.517  1.00 80.48           H  
ATOM   1668  HD2 LYS A 116      48.182  -0.862  31.284  1.00109.41           H  
ATOM   1669  HD3 LYS A 116      47.859   0.236  30.190  1.00109.41           H  
ATOM   1670  HE2 LYS A 116      50.161   0.174  30.926  1.00116.58           H  
ATOM   1671  HE3 LYS A 116      50.303  -1.200  30.162  1.00116.58           H  
ATOM   1672  HZ1 LYS A 116      51.004   0.610  28.898  1.00119.98           H  
ATOM   1673  HZ2 LYS A 116      49.948  -0.143  28.199  1.00119.98           H  
ATOM   1674  HZ3 LYS A 116      49.627   1.136  28.867  1.00119.98           H  
ATOM   1675  N   LEU A 117      43.244  -2.114  28.597  1.00 61.94           N  
ANISOU 1675  N   LEU A 117    10053   3568   9912    793  -2624    454       N  
ATOM   1676  CA  LEU A 117      41.815  -2.262  28.958  1.00 60.99           C  
ANISOU 1676  CA  LEU A 117    10207   3335   9633    581  -2435    408       C  
ATOM   1677  C   LEU A 117      41.295  -3.515  28.272  1.00 61.30           C  
ANISOU 1677  C   LEU A 117    10365   3255   9672    638  -2339    348       C  
ATOM   1678  O   LEU A 117      40.606  -4.274  28.918  1.00 62.11           O  
ANISOU 1678  O   LEU A 117    10749   3214   9635    513  -2271    362       O  
ATOM   1679  CB  LEU A 117      41.009  -1.041  28.489  1.00 62.49           C  
ANISOU 1679  CB  LEU A 117    10202   3696   9845    412  -2224    361       C  
ATOM   1680  CG  LEU A 117      41.130   0.233  29.319  1.00 60.01           C  
ANISOU 1680  CG  LEU A 117     9883   3436   9483    285  -2279    396       C  
ATOM   1681  CD1 LEU A 117      40.587   1.431  28.555  1.00 61.19           C  
ANISOU 1681  CD1 LEU A 117     9757   3775   9719    190  -2073    346       C  
ATOM   1682  CD2 LEU A 117      40.422   0.090  30.659  1.00 63.87           C  
ANISOU 1682  CD2 LEU A 117    10792   3738   9737    139  -2264    427       C  
ATOM   1683  H   LEU A 117      43.438  -1.368  28.111  1.00 72.73           H  
ATOM   1684  HA  LEU A 117      41.738  -2.368  29.933  1.00 71.60           H  
ATOM   1685  HB2 LEU A 117      41.274  -0.835  27.572  1.00 75.30           H  
ATOM   1686  HB3 LEU A 117      40.066  -1.299  28.462  1.00 75.30           H  
ATOM   1687  HG  LEU A 117      42.087   0.388  29.489  1.00 72.33           H  
ATOM   1688 HD11 LEU A 117      40.686   2.235  29.093  1.00 73.75           H  
ATOM   1689 HD12 LEU A 117      41.081   1.538  27.723  1.00 73.75           H  
ATOM   1690 HD13 LEU A 117      39.645   1.289  28.355  1.00 73.75           H  
ATOM   1691 HD21 LEU A 117      40.325   0.965  31.072  1.00 76.96           H  
ATOM   1692 HD22 LEU A 117      39.542  -0.300  30.523  1.00 76.96           H  
ATOM   1693 HD23 LEU A 117      40.943  -0.487  31.243  1.00 76.96           H  
ATOM   1694  N   ARG A 118      41.643  -3.702  27.010  1.00 60.99           N  
ANISOU 1694  N   ARG A 118    10083   3330   9759    821  -2296    282       N  
ATOM   1695  CA  ARG A 118      41.194  -4.864  26.215  1.00 61.67           C  
ANISOU 1695  CA  ARG A 118    10312   3279   9840    898  -2249    200       C  
ATOM   1696  C   ARG A 118      41.772  -6.134  26.854  1.00 69.17           C  
ANISOU 1696  C   ARG A 118    11507   4059  10714   1020  -2398    242       C  
ATOM   1697  O   ARG A 118      41.012  -7.089  27.033  1.00 66.53           O  
ANISOU 1697  O   ARG A 118    11384   3602  10293    945  -2338    208       O  
ATOM   1698  CB  ARG A 118      41.636  -4.696  24.758  1.00 61.23           C  
ANISOU 1698  CB  ARG A 118     9972   3407   9886   1115  -2170    115       C  
ATOM   1699  CG  ARG A 118      40.981  -3.538  24.017  1.00 63.82           C  
ANISOU 1699  CG  ARG A 118    10015   3978  10255   1002  -1987     80       C  
ATOM   1700  CD  ARG A 118      39.565  -3.847  23.584  1.00 70.86           C  
ANISOU 1700  CD  ARG A 118    11010   4811  11102    815  -1852    -16       C  
ATOM   1701  NE  ARG A 118      39.502  -4.679  22.390  1.00 74.45           N  
ANISOU 1701  NE  ARG A 118    11584   5156  11547    975  -1880   -128       N  
ATOM   1702  CZ  ARG A 118      38.395  -5.222  21.887  1.00 79.77           C  
ANISOU 1702  CZ  ARG A 118    12427   5681  12203    824  -1856   -212       C  
ATOM   1703  NH1 ARG A 118      37.217  -5.050  22.467  1.00 78.38           N  
ANISOU 1703  NH1 ARG A 118    12275   5474  12032    519  -1766   -174       N  
ATOM   1704  NH2 ARG A 118      38.470  -5.955  20.791  1.00 81.07           N  
ANISOU 1704  NH2 ARG A 118    12735   5717  12352    983  -1928   -330       N  
ATOM   1705  H   ARG A 118      42.211  -3.142  26.571  1.00 71.59           H  
ATOM   1706  HA  ARG A 118      40.213  -4.909  26.254  1.00 72.41           H  
ATOM   1707  HB2 ARG A 118      42.606  -4.571  24.738  1.00 71.88           H  
ATOM   1708  HB3 ARG A 118      41.434  -5.526  24.280  1.00 71.88           H  
ATOM   1709  HG2 ARG A 118      40.961  -2.751  24.596  1.00 76.90           H  
ATOM   1710  HG3 ARG A 118      41.517  -3.314  23.227  1.00 76.90           H  
ATOM   1711  HD2 ARG A 118      39.103  -4.301  24.317  1.00 85.35           H  
ATOM   1712  HD3 ARG A 118      39.093  -3.007  23.413  1.00 85.35           H  
ATOM   1713  HE  ARG A 118      40.248  -4.823  21.963  1.00 89.66           H  
ATOM   1714 HH11 ARG A 118      37.132  -4.569  23.193  1.00 94.37           H  
ATOM   1715 HH12 ARG A 118      36.508  -5.423  22.116  1.00 94.37           H  
ATOM   1716 HH21 ARG A 118      39.242  -6.073  20.392  1.00 97.61           H  
ATOM   1717 HH22 ARG A 118      37.743  -6.320  20.452  1.00 97.61           H  
ATOM   1718  N   ALA A 119      43.042  -6.112  27.251  1.00 65.48           N  
ANISOU 1718  N   ALA A 119    10986   3602  10291   1198  -2594    327       N  
ATOM   1719  CA  ALA A 119      43.728  -7.257  27.887  1.00 79.03           C  
ANISOU 1719  CA  ALA A 119    12908   5188  11933   1330  -2744    377       C  
ATOM   1720  C   ALA A 119      43.485  -7.196  29.387  1.00 83.19           C  
ANISOU 1720  C   ALA A 119    13693   5623  12290   1136  -2828    477       C  
ATOM   1721  O   ALA A 119      44.459  -6.958  30.114  1.00 90.93           O  
ANISOU 1721  O   ALA A 119    14677   6604  13267   1210  -3045    565       O  
ATOM   1722  CB  ALA A 119      45.192  -7.216  27.555  1.00 69.96           C  
ANISOU 1722  CB  ALA A 119    11529   4112  10939   1663  -2910    423       C  
ATOM   1723  H   ALA A 119      43.563  -5.370  27.213  1.00 76.98           H  
ATOM   1724  HA  ALA A 119      43.345  -8.094  27.537  1.00 95.16           H  
ATOM   1725  HB1 ALA A 119      45.641  -7.976  27.963  1.00 84.27           H  
ATOM   1726  HB2 ALA A 119      45.305  -7.259  26.590  1.00 84.27           H  
ATOM   1727  HB3 ALA A 119      45.585  -6.391  27.886  1.00 84.27           H  
ATOM   1728  N   LEU A 120      42.251  -7.428  29.827  1.00 90.08           N  
ANISOU 1728  N   LEU A 120    14783   6418  13024    891  -2654    469       N  
ATOM   1729  CA  LEU A 120      41.873  -7.353  31.252  1.00 86.19           C  
ANISOU 1729  CA  LEU A 120    14564   5846  12338    712  -2660    566       C  
ATOM   1730  C   LEU A 120      41.085  -8.605  31.610  1.00 77.05           C  
ANISOU 1730  C   LEU A 120    13675   4528  11072    598  -2538    599       C  
ATOM   1731  O   LEU A 120      40.591  -9.230  30.674  1.00 80.19           O  
ANISOU 1731  O   LEU A 120    14024   4890  11555    570  -2415    528       O  
ATOM   1732  CB  LEU A 120      41.069  -6.081  31.498  1.00 67.33           C  
ANISOU 1732  CB  LEU A 120    12121   3556   9906    500  -2512    564       C  
ATOM   1733  H   LEU A 120      41.558  -7.629  29.271  1.00108.41           H  
ATOM   1734  HA  LEU A 120      42.690  -7.333  31.798  1.00103.75           H  
ATOM   1735  N   GLU A 121      40.927  -8.909  32.905  1.00 86.63           N  
ANISOU 1735  N   GLU A 121    15185   5632  12097    532  -2589    714       N  
ATOM   1736  CA  GLU A 121      40.302 -10.164  33.400  1.00 77.16           C  
ANISOU 1736  CA  GLU A 121    14263   4253  10802    451  -2514    791       C  
ATOM   1737  C   GLU A 121      38.896 -10.333  32.867  1.00 74.25           C  
ANISOU 1737  C   GLU A 121    13836   3854  10521    245  -2243    761       C  
ATOM   1738  O   GLU A 121      38.639 -11.421  32.329  1.00 92.98           O  
ANISOU 1738  O   GLU A 121    16197   6132  12998    275  -2240    712       O  
ATOM   1739  CB  GLU A 121      40.225 -10.110  34.925  1.00 76.83           C  
ANISOU 1739  CB  GLU A 121    14548   4131  10515    370  -2539    931       C  
ATOM   1740  H   GLU A 121      41.203  -8.354  33.572  1.00104.27           H  
ATOM   1741  HA  GLU A 121      40.853 -10.931  33.123  1.00 92.91           H  
ATOM   1742  N   PRO A 122      38.007  -9.332  32.957  1.00 73.06           N  
ANISOU 1742  N   PRO A 122    13666   3761  10334     35  -2025    797       N  
ATOM   1743  CA  PRO A 122      36.704  -9.406  32.294  1.00 71.76           C  
ANISOU 1743  CA  PRO A 122    13313   3626  10328   -139  -1802    740       C  
ATOM   1744  C   PRO A 122      36.910  -8.197  31.378  1.00 68.79           C  
ANISOU 1744  C   PRO A 122    12637   3449  10052   -104  -1788    618       C  
ATOM   1745  O   PRO A 122      37.300  -7.203  31.910  1.00 67.75           O  
ANISOU 1745  O   PRO A 122    12484   3418   9839    -85  -1814    633       O  
ATOM   1746  CB  PRO A 122      35.626  -9.304  33.372  1.00 72.76           C  
ANISOU 1746  CB  PRO A 122    13595   3685  10365   -368  -1560    884       C  
ATOM   1747  HA  PRO A 122      36.608 -10.242  31.774  1.00 84.52           H  
ATOM   1748  N   ARG A 123      36.713  -8.315  30.061  1.00 67.65           N  
ANISOU 1748  N   ARG A 123    12280   3354  10070    -87  -1764    497       N  
ATOM   1749  CA  ARG A 123      37.024  -7.212  29.118  1.00 76.41           C  
ANISOU 1749  CA  ARG A 123    13125   4644  11264      0  -1789    394       C  
ATOM   1750  C   ARG A 123      35.953  -6.133  29.240  1.00 63.41           C  
ANISOU 1750  C   ARG A 123    11336   3100   9658   -200  -1578    392       C  
ATOM   1751  O   ARG A 123      34.782  -6.466  29.042  1.00 63.79           O  
ANISOU 1751  O   ARG A 123    11359   3099   9780   -373  -1424    397       O  
ATOM   1752  CB  ARG A 123      37.094  -7.669  27.662  1.00 66.05           C  
ANISOU 1752  CB  ARG A 123    11681   3342  10073    173  -1883    262       C  
ATOM   1753  CG  ARG A 123      37.412  -6.553  26.678  1.00 66.26           C  
ANISOU 1753  CG  ARG A 123    11444   3537  10193    256  -1877    176       C  
ATOM   1754  CD  ARG A 123      38.015  -7.049  25.379  1.00 63.90           C  
ANISOU 1754  CD  ARG A 123    11051   3253   9975    498  -1974     57       C  
ATOM   1755  NE  ARG A 123      37.372  -8.244  24.856  1.00 74.91           N  
ANISOU 1755  NE  ARG A 123    12537   4536  11390    481  -1966    -37       N  
ATOM   1756  CZ  ARG A 123      36.199  -8.298  24.219  1.00 85.62           C  
ANISOU 1756  CZ  ARG A 123    13798   5922  12811    357  -1884   -127       C  
ATOM   1757  NH1 ARG A 123      35.467  -7.212  24.010  1.00 78.27           N  
ANISOU 1757  NH1 ARG A 123    12689   5120  11930    196  -1760   -110       N  
ATOM   1758  NH2 ARG A 123      35.746  -9.468  23.799  1.00 80.12           N  
ANISOU 1758  NH2 ARG A 123    13201   5111  12131    382  -1943   -233       N  
ATOM   1759  H   ARG A 123      36.349  -9.054  29.674  1.00 80.75           H  
ATOM   1760  HA  ARG A 123      37.895  -6.846  29.366  1.00 92.01           H  
ATOM   1761  HB2 ARG A 123      37.783  -8.361  27.588  1.00 79.58           H  
ATOM   1762  HB3 ARG A 123      36.235  -8.071  27.417  1.00 79.58           H  
ATOM   1763  HG2 ARG A 123      36.590  -6.060  26.476  1.00 79.83           H  
ATOM   1764  HG3 ARG A 123      38.040  -5.926  27.095  1.00 79.83           H  
ATOM   1765  HD2 ARG A 123      37.965  -6.337  24.711  1.00 77.00           H  
ATOM   1766  HD3 ARG A 123      38.963  -7.243  25.525  1.00 77.00           H  
ATOM   1767  HE  ARG A 123      37.801  -8.995  24.958  1.00 90.21           H  
ATOM   1768 HH11 ARG A 123      35.735  -6.427  24.280  1.00 94.24           H  
ATOM   1769 HH12 ARG A 123      34.697  -7.281  23.593  1.00 94.24           H  
ATOM   1770 HH21 ARG A 123      36.219 -10.199  23.931  1.00 96.47           H  
ATOM   1771 HH22 ARG A 123      34.973  -9.518  23.382  1.00 96.47           H  
ATOM   1772  N   PRO A 124      36.293  -4.863  29.542  1.00 61.95           N  
ANISOU 1772  N   PRO A 124    11068   3037   9434   -189  -1577    401       N  
ATOM   1773  CA  PRO A 124      35.301  -3.818  29.526  1.00 60.34           C  
ANISOU 1773  CA  PRO A 124    10723   2930   9272   -350  -1379    392       C  
ATOM   1774  C   PRO A 124      34.945  -3.627  28.056  1.00 58.74           C  
ANISOU 1774  C   PRO A 124    10245   2826   9248   -332  -1357    274       C  
ATOM   1775  O   PRO A 124      35.851  -3.492  27.283  1.00 61.00           O  
ANISOU 1775  O   PRO A 124    10387   3188   9602   -146  -1501    198       O  
ATOM   1776  CB  PRO A 124      36.017  -2.603  30.103  1.00 59.54           C  
ANISOU 1776  CB  PRO A 124    10624   2914   9086   -293  -1457    410       C  
ATOM   1777  CG  PRO A 124      37.478  -2.853  29.842  1.00 67.08           C  
ANISOU 1777  CG  PRO A 124    11543   3874  10070    -74  -1727    388       C  
ATOM   1778  CD  PRO A 124      37.623  -4.358  29.862  1.00 65.98           C  
ANISOU 1778  CD  PRO A 124    11568   3598   9903     -6  -1794    407       C  
ATOM   1779  HA  PRO A 124      34.521  -4.062  30.083  1.00 72.67           H  
ATOM   1780  HB2 PRO A 124      35.722  -1.781  29.657  1.00 69.86           H  
ATOM   1781  HB3 PRO A 124      35.846  -2.520  31.064  1.00 69.86           H  
ATOM   1782  HG2 PRO A 124      37.745  -2.491  28.973  1.00 80.81           H  
ATOM   1783  HG3 PRO A 124      38.031  -2.442  30.537  1.00 80.81           H  
ATOM   1784  HD2 PRO A 124      38.264  -4.647  29.190  1.00 79.49           H  
ATOM   1785  HD3 PRO A 124      37.916  -4.672  30.737  1.00 79.49           H  
ATOM   1786  N   PRO A 125      33.667  -3.641  27.637  1.00 58.65           N  
ANISOU 1786  N   PRO A 125    10156   2801   9326   -507  -1193    265       N  
ATOM   1787  CA  PRO A 125      33.354  -3.323  26.257  1.00 57.19           C  
ANISOU 1787  CA  PRO A 125     9716   2721   9292   -494  -1192    152       C  
ATOM   1788  C   PRO A 125      33.796  -1.862  26.061  1.00 58.43           C  
ANISOU 1788  C   PRO A 125     9661   3085   9456   -436  -1153    131       C  
ATOM   1789  O   PRO A 125      33.490  -1.102  26.912  1.00 54.75           O  
ANISOU 1789  O   PRO A 125     9208   2668   8925   -535  -1023    199       O  
ATOM   1790  CB  PRO A 125      31.846  -3.535  26.152  1.00 57.89           C  
ANISOU 1790  CB  PRO A 125     9761   2755   9479   -733  -1024    187       C  
ATOM   1791  CG  PRO A 125      31.501  -4.400  27.330  1.00 60.14           C  
ANISOU 1791  CG  PRO A 125    10291   2871   9689   -841   -953    315       C  
ATOM   1792  CD  PRO A 125      32.483  -4.001  28.407  1.00 60.15           C  
ANISOU 1792  CD  PRO A 125    10472   2876   9506   -724  -1004    377       C  
ATOM   1793  HA  PRO A 125      33.833  -3.934  25.643  1.00 67.03           H  
ATOM   1794  HB2 PRO A 125      31.369  -2.679  26.199  1.00 69.11           H  
ATOM   1795  HB3 PRO A 125      31.613  -3.981  25.311  1.00 69.11           H  
ATOM   1796  HG2 PRO A 125      30.581  -4.243  27.620  1.00 70.57           H  
ATOM   1797  HG3 PRO A 125      31.604  -5.347  27.105  1.00 70.57           H  
ATOM   1798  HD2 PRO A 125      32.160  -3.241  28.924  1.00 70.59           H  
ATOM   1799  HD3 PRO A 125      32.660  -4.746  29.008  1.00 70.59           H  
ATOM   1800  N   LEU A 126      34.499  -1.522  24.981  1.00 59.94           N  
ANISOU 1800  N   LEU A 126     9647   3429   9696   -255  -1238     42       N  
ATOM   1801  CA  LEU A 126      35.054  -0.170  24.726  1.00 58.39           C  
ANISOU 1801  CA  LEU A 126     9205   3466   9513   -186  -1193     37       C  
ATOM   1802  C   LEU A 126      34.370   0.416  23.494  1.00 57.64           C  
ANISOU 1802  C   LEU A 126     8858   3536   9506   -204  -1088    -33       C  
ATOM   1803  O   LEU A 126      34.080  -0.355  22.573  1.00 51.85           O  
ANISOU 1803  O   LEU A 126     8124   2759   8818   -184  -1124   -110       O  
ATOM   1804  CB  LEU A 126      36.566  -0.242  24.487  1.00 65.89           C  
ANISOU 1804  CB  LEU A 126    10083   4485  10465     49  -1351     36       C  
ATOM   1805  CG  LEU A 126      37.442  -0.826  25.595  1.00 69.37           C  
ANISOU 1805  CG  LEU A 126    10744   4777  10836    116  -1518    105       C  
ATOM   1806  CD1 LEU A 126      38.911  -0.612  25.270  1.00 64.75           C  
ANISOU 1806  CD1 LEU A 126     9968   4316  10317    347  -1653    123       C  
ATOM   1807  CD2 LEU A 126      37.126  -0.220  26.949  1.00 60.39           C  
ANISOU 1807  CD2 LEU A 126     9773   3578   9595    -47  -1487    184       C  
ATOM   1808  H   LEU A 126      34.682  -2.112  24.317  1.00 72.24           H  
ATOM   1809  HA  LEU A 126      34.866   0.406  25.498  1.00 70.38           H  
ATOM   1810  HB2 LEU A 126      36.714  -0.770  23.677  1.00 79.38           H  
ATOM   1811  HB3 LEU A 126      36.881   0.664  24.300  1.00 79.38           H  
ATOM   1812  HG  LEU A 126      37.275  -1.800  25.642  1.00 83.56           H  
ATOM   1813 HD11 LEU A 126      39.455  -1.196  25.825  1.00 78.01           H  
ATOM   1814 HD12 LEU A 126      39.072  -0.815  24.333  1.00 78.01           H  
ATOM   1815 HD13 LEU A 126      39.151   0.315  25.443  1.00 78.01           H  
ATOM   1816 HD21 LEU A 126      37.817  -0.470  27.585  1.00 72.79           H  
ATOM   1817 HD22 LEU A 126      37.098   0.748  26.869  1.00 72.79           H  
ATOM   1818 HD23 LEU A 126      36.265  -0.545  27.265  1.00 72.79           H  
ATOM   1819  N   GLY A 127      34.089   1.719  23.502  1.00 49.95           N  
ANISOU 1819  N   GLY A 127     7692   2733   8551   -236   -983     -9       N  
ATOM   1820  CA  GLY A 127      33.449   2.395  22.366  1.00 51.55           C  
ANISOU 1820  CA  GLY A 127     7658   3098   8829   -242   -889    -58       C  
ATOM   1821  C   GLY A 127      33.831   3.852  22.224  1.00 47.60           C  
ANISOU 1821  C   GLY A 127     6957   2779   8351   -214   -817    -19       C  
ATOM   1822  O   GLY A 127      34.448   4.377  23.152  1.00 57.60           O  
ANISOU 1822  O   GLY A 127     8274   4029   9582   -224   -845     39       O  
ATOM   1823  H   GLY A 127      34.259   2.257  24.216  1.00 58.34           H  
ATOM   1824  HA2 GLY A 127      33.699   1.919  21.537  1.00 62.17           H  
ATOM   1825  HA3 GLY A 127      32.466   2.326  22.467  1.00 62.17           H  
ATOM   1826  N   ILE A 128      33.505   4.466  21.091  1.00 56.19           N  
ANISOU 1826  N   ILE A 128     7832   4022   9496   -180   -747    -50       N  
ATOM   1827  CA  ILE A 128      33.709   5.923  20.854  1.00 45.70           C  
ANISOU 1827  CA  ILE A 128     6302   2854   8209   -165   -665     -5       C  
ATOM   1828  C   ILE A 128      32.331   6.557  20.697  1.00 49.76           C  
ANISOU 1828  C   ILE A 128     6728   3407   8770   -294   -523    -13       C  
ATOM   1829  O   ILE A 128      31.513   5.927  20.032  1.00 46.37           O  
ANISOU 1829  O   ILE A 128     6280   2966   8373   -329   -521    -63       O  
ATOM   1830  CB  ILE A 128      34.597   6.197  19.624  1.00 47.93           C  
ANISOU 1830  CB  ILE A 128     6391   3304   8517     33   -695     -1       C  
ATOM   1831  CG1 ILE A 128      36.082   6.028  19.955  1.00 48.93           C  
ANISOU 1831  CG1 ILE A 128     6511   3427   8652    157   -800     58       C  
ATOM   1832  CG2 ILE A 128      34.305   7.568  19.027  1.00 44.57           C  
ANISOU 1832  CG2 ILE A 128     5751   3035   8149     21   -583     44       C  
ATOM   1833  CD1 ILE A 128      36.969   5.800  18.752  1.00 46.69           C  
ANISOU 1833  CD1 ILE A 128     6076   3282   8382    394   -806     72       C  
ATOM   1834  H   ILE A 128      33.118   4.035  20.389  1.00 67.75           H  
ATOM   1835  HA  ILE A 128      34.139   6.301  21.629  1.00 53.25           H  
ATOM   1836  HB  ILE A 128      34.369   5.521  18.939  1.00 57.83           H  
ATOM   1837 HG12 ILE A 128      36.390   6.832  20.424  1.00 59.03           H  
ATOM   1838 HG13 ILE A 128      36.182   5.270  20.566  1.00 59.03           H  
ATOM   1839 HG21 ILE A 128      35.012   7.809  18.411  1.00 52.66           H  
ATOM   1840 HG22 ILE A 128      33.460   7.549  18.544  1.00 52.66           H  
ATOM   1841 HG23 ILE A 128      34.263   8.234  19.735  1.00 52.66           H  
ATOM   1842 HD11 ILE A 128      37.898   5.785  19.034  1.00 54.44           H  
ATOM   1843 HD12 ILE A 128      36.744   4.949  18.337  1.00 54.44           H  
ATOM   1844 HD13 ILE A 128      36.845   6.516  18.107  1.00 54.44           H  
ATOM   1845  N   LEU A 129      32.043   7.677  21.364  1.00 44.71           N  
ANISOU 1845  N   LEU A 129     6039   2801   8146   -360   -424     37       N  
ATOM   1846  CA  LEU A 129      30.800   8.471  21.155  1.00 44.81           C  
ANISOU 1846  CA  LEU A 129     5937   2869   8220   -444   -273     45       C  
ATOM   1847  C   LEU A 129      31.252   9.882  20.757  1.00 43.51           C  
ANISOU 1847  C   LEU A 129     5610   2827   8094   -381   -237     85       C  
ATOM   1848  O   LEU A 129      31.712  10.594  21.644  1.00 43.51           O  
ANISOU 1848  O   LEU A 129     5682   2777   8071   -402   -241    120       O  
ATOM   1849  CB  LEU A 129      29.954   8.453  22.428  1.00 56.08           C  
ANISOU 1849  CB  LEU A 129     7520   4170   9619   -583   -143     75       C  
ATOM   1850  CG  LEU A 129      28.622   9.198  22.371  1.00 68.02           C  
ANISOU 1850  CG  LEU A 129     8899   5731  11216   -653     44    100       C  
ATOM   1851  CD1 LEU A 129      27.779   8.752  21.184  1.00 58.24           C  
ANISOU 1851  CD1 LEU A 129     7462   4571  10095   -663     15     72       C  
ATOM   1852  CD2 LEU A 129      27.850   9.008  23.665  1.00 63.15           C  
ANISOU 1852  CD2 LEU A 129     8455   4983  10554   -763    210    150       C  
ATOM   1853  H   LEU A 129      32.593   8.022  22.003  1.00 53.97           H  
ATOM   1854  HA  LEU A 129      30.298   8.076  20.415  1.00 54.09           H  
ATOM   1855  HB2 LEU A 129      29.772   7.519  22.653  1.00 67.62           H  
ATOM   1856  HB3 LEU A 129      30.488   8.824  23.156  1.00 67.62           H  
ATOM   1857  HG  LEU A 129      28.813  10.163  22.268  1.00 81.95           H  
ATOM   1858 HD11 LEU A 129      26.888   9.130  21.258  1.00 70.20           H  
ATOM   1859 HD12 LEU A 129      28.188   9.057  20.355  1.00 70.20           H  
ATOM   1860 HD13 LEU A 129      27.715   7.781  21.177  1.00 70.20           H  
ATOM   1861 HD21 LEU A 129      27.026   9.515  23.622  1.00 76.09           H  
ATOM   1862 HD22 LEU A 129      27.643   8.065  23.787  1.00 76.09           H  
ATOM   1863 HD23 LEU A 129      28.384   9.323  24.414  1.00 76.09           H  
ATOM   1864  N   SER A 130      31.085  10.280  19.505  1.00 43.10           N  
ANISOU 1864  N   SER A 130     5362   2917   8096   -304   -221     82       N  
ATOM   1865  CA  SER A 130      31.625  11.546  18.958  1.00 42.56           C  
ANISOU 1865  CA  SER A 130     5135   2964   8072   -227   -198    144       C  
ATOM   1866  C   SER A 130      30.598  12.333  18.139  1.00 43.71           C  
ANISOU 1866  C   SER A 130     5120   3214   8275   -215   -106    154       C  
ATOM   1867  O   SER A 130      29.643  11.705  17.668  1.00 42.69           O  
ANISOU 1867  O   SER A 130     4962   3104   8156   -230   -109    105       O  
ATOM   1868  CB  SER A 130      32.793  11.229  18.112  1.00 42.70           C  
ANISOU 1868  CB  SER A 130     5073   3075   8075    -73   -289    172       C  
ATOM   1869  OG  SER A 130      33.176  12.330  17.316  1.00 42.51           O  
ANISOU 1869  OG  SER A 130     4860   3184   8106      7   -237    256       O  
ATOM   1870  H   SER A 130      30.637   9.794  18.879  1.00 50.12           H  
ATOM   1871  HA  SER A 130      31.929  12.117  19.711  1.00 51.12           H  
ATOM   1872  HB2 SER A 130      33.544  10.963  18.687  1.00 49.64           H  
ATOM   1873  HB3 SER A 130      32.572  10.470  17.536  1.00 49.64           H  
ATOM   1874  HG  SER A 130      33.919  12.160  16.955  1.00 49.41           H  
ATOM   1875  N   ASN A 131      30.794  13.649  17.994  1.00 42.04           N  
ANISOU 1875  N   ASN A 131     4806   3051   8116   -194    -48    223       N  
ATOM   1876  CA  ASN A 131      29.949  14.519  17.139  1.00 41.98           C  
ANISOU 1876  CA  ASN A 131     4638   3150   8162   -148     24    256       C  
ATOM   1877  C   ASN A 131      30.411  14.315  15.707  1.00 42.12           C  
ANISOU 1877  C   ASN A 131     4544   3319   8141      0    -28    280       C  
ATOM   1878  O   ASN A 131      29.689  14.667  14.801  1.00 42.36           O  
ANISOU 1878  O   ASN A 131     4473   3442   8180     56     -8    291       O  
ATOM   1879  CB  ASN A 131      29.996  15.988  17.587  1.00 41.88           C  
ANISOU 1879  CB  ASN A 131     4585   3111   8217   -165     96    329       C  
ATOM   1880  CG  ASN A 131      29.153  16.283  18.803  1.00 42.17           C  
ANISOU 1880  CG  ASN A 131     4737   3019   8266   -261    195    295       C  
ATOM   1881  OD1 ASN A 131      28.194  15.576  19.081  1.00 42.50           O  
ANISOU 1881  OD1 ASN A 131     4818   3032   8300   -314    253    247       O  
ATOM   1882  ND2 ASN A 131      29.480  17.348  19.512  1.00 42.38           N  
ANISOU 1882  ND2 ASN A 131     4828   2958   8318   -280    218    328       N  
ATOM   1883  H   ASN A 131      31.476  14.087  18.406  1.00 48.86           H  
ATOM   1884  HA  ASN A 131      29.020  14.212  17.206  1.00 48.78           H  
ATOM   1885  HB2 ASN A 131      30.926  16.227  17.778  1.00 48.66           H  
ATOM   1886  HB3 ASN A 131      29.694  16.551  16.847  1.00 48.66           H  
ATOM   1887 HD21 ASN A 131      28.970  17.602  20.186  1.00 49.27           H  
ATOM   1888 HD22 ASN A 131      30.201  17.816  19.306  1.00 49.27           H  
ATOM   1889  N   GLY A 132      31.566  13.707  15.524  1.00 42.28           N  
ANISOU 1889  N   GLY A 132     4586   3366   8111     86    -89    299       N  
ATOM   1890  CA  GLY A 132      32.127  13.445  14.198  1.00 45.03           C  
ANISOU 1890  CA  GLY A 132     4859   3861   8390    266    -98    331       C  
ATOM   1891  C   GLY A 132      31.311  12.487  13.368  1.00 43.37           C  
ANISOU 1891  C   GLY A 132     4715   3678   8087    320   -169    219       C  
ATOM   1892  O   GLY A 132      30.572  11.699  13.942  1.00 43.41           O  
ANISOU 1892  O   GLY A 132     4812   3576   8108    203   -228    122       O  
ATOM   1893  H   GLY A 132      32.113  13.481  16.199  1.00 49.14           H  
ATOM   1894  HA2 GLY A 132      32.207  14.303  13.714  1.00 54.36           H  
ATOM   1895  HA3 GLY A 132      33.040  13.077  14.308  1.00 54.36           H  
ATOM   1896  N   THR A 133      31.439  12.580  12.060  1.00 47.04           N  
ANISOU 1896  N   THR A 133     5141   4280   8453    499   -169    243       N  
ATOM   1897  CA  THR A 133      30.732  11.712  11.104  1.00 48.64           C  
ANISOU 1897  CA  THR A 133     5442   4499   8541    577   -286    124       C  
ATOM   1898  C   THR A 133      31.352  10.313  11.160  1.00 54.37           C  
ANISOU 1898  C   THR A 133     6336   5153   9169    655   -375     24       C  
ATOM   1899  O   THR A 133      32.516  10.207  11.562  1.00 48.09           O  
ANISOU 1899  O   THR A 133     5544   4351   8377    711   -323     77       O  
ATOM   1900  CB  THR A 133      30.821  12.262   9.677  1.00 48.58           C  
ANISOU 1900  CB  THR A 133     5394   4655   8410    777   -264    181       C  
ATOM   1901  OG1 THR A 133      32.152  12.016   9.243  1.00 46.87           O  
ANISOU 1901  OG1 THR A 133     5204   4531   8075    988   -186    246       O  
ATOM   1902  CG2 THR A 133      30.463  13.728   9.558  1.00 51.13           C  
ANISOU 1902  CG2 THR A 133     5547   5041   8837    727   -156    317       C  
ATOM   1903  H   THR A 133      32.054  13.115  11.661  1.00 56.77           H  
ATOM   1904  HA  THR A 133      29.789  11.669  11.374  1.00 58.69           H  
ATOM   1905  HB  THR A 133      30.205  11.743   9.110  1.00 58.61           H  
ATOM   1906  HG1 THR A 133      32.176  12.083   8.407  1.00 54.66           H  
ATOM   1907 HG21 THR A 133      30.312  13.952   8.623  1.00 61.67           H  
ATOM   1908 HG22 THR A 133      29.651  13.906  10.065  1.00 61.67           H  
ATOM   1909 HG23 THR A 133      31.187  14.276   9.907  1.00 61.67           H  
ATOM   1910  N   PRO A 134      30.647   9.246  10.732  1.00 52.35           N  
ANISOU 1910  N   PRO A 134     6577   4521   8794    -41  -1959   -770       N  
ATOM   1911  CA  PRO A 134      31.227   7.917  10.721  1.00 47.10           C  
ANISOU 1911  CA  PRO A 134     6047   3757   8092    -39  -1836   -891       C  
ATOM   1912  C   PRO A 134      32.483   7.886   9.845  1.00 46.59           C  
ANISOU 1912  C   PRO A 134     6080   3704   7917     71  -1681   -838       C  
ATOM   1913  O   PRO A 134      33.440   7.267  10.226  1.00 43.05           O  
ANISOU 1913  O   PRO A 134     5659   3139   7559    129  -1528   -835       O  
ATOM   1914  CB  PRO A 134      30.108   7.058  10.129  1.00 47.10           C  
ANISOU 1914  CB  PRO A 134     6129   3770   7997   -158  -1943  -1070       C  
ATOM   1915  CG  PRO A 134      28.854   7.797  10.473  1.00 54.26           C  
ANISOU 1915  CG  PRO A 134     6861   4735   9019   -232  -2112  -1022       C  
ATOM   1916  CD  PRO A 134      29.248   9.242  10.297  1.00 49.67           C  
ANISOU 1916  CD  PRO A 134     6190   4251   8429   -137  -2129   -836       C  
ATOM   1917  HA  PRO A 134      31.431   7.625  11.645  1.00 56.84           H  
ATOM   1918  HB2 PRO A 134      30.209   6.971   9.157  1.00 56.84           H  
ATOM   1919  HB3 PRO A 134      30.106   6.163  10.529  1.00 56.84           H  
ATOM   1920  HG2 PRO A 134      28.125   7.556   9.867  1.00 65.43           H  
ATOM   1921  HG3 PRO A 134      28.580   7.618  11.395  1.00 65.43           H  
ATOM   1922  HD2 PRO A 134      29.170   9.520   9.365  1.00 59.92           H  
ATOM   1923  HD3 PRO A 134      28.696   9.821  10.852  1.00 59.92           H  
ATOM   1924  N   GLN A 135      32.451   8.575   8.715  1.00 43.61           N  
ANISOU 1924  N   GLN A 135     5753   3456   7363    111  -1697   -773       N  
ATOM   1925  CA  GLN A 135      33.623   8.648   7.816  1.00 62.51           C  
ANISOU 1925  CA  GLN A 135     8226   5844   9681    234  -1486   -685       C  
ATOM   1926  C   GLN A 135      34.807   9.310   8.527  1.00 50.97           C  
ANISOU 1926  C   GLN A 135     6576   4306   8485    307  -1399   -504       C  
ATOM   1927  O   GLN A 135      35.907   8.766   8.445  1.00 52.74           O  
ANISOU 1927  O   GLN A 135     6786   4420   8831    379  -1228   -469       O  
ATOM   1928  CB  GLN A 135      33.339   9.489   6.578  1.00 54.20           C  
ANISOU 1928  CB  GLN A 135     7249   4938   8407    279  -1498   -583       C  
ATOM   1929  CG  GLN A 135      32.767   8.746   5.387  1.00 62.87           C  
ANISOU 1929  CG  GLN A 135     8568   6136   9182    219  -1611   -714       C  
ATOM   1930  CD  GLN A 135      32.994   9.560   4.137  1.00 88.08           C  
ANISOU 1930  CD  GLN A 135    11889   9447  12131    312  -1531   -566       C  
ATOM   1931  OE1 GLN A 135      33.775   9.187   3.266  1.00 95.71           O  
ANISOU 1931  OE1 GLN A 135    12980  10364  13023    428  -1241   -514       O  
ATOM   1932  NE2 GLN A 135      32.340  10.708   4.053  1.00 87.06           N  
ANISOU 1932  NE2 GLN A 135    11692   9451  11934    283  -1745   -451       N  
ATOM   1933  H   GLN A 135      31.714   9.026   8.429  1.00 50.75           H  
ATOM   1934  HA  GLN A 135      33.877   7.737   7.546  1.00 75.33           H  
ATOM   1935  HB2 GLN A 135      32.723  10.207   6.827  1.00 65.36           H  
ATOM   1936  HB3 GLN A 135      34.180   9.911   6.305  1.00 65.36           H  
ATOM   1937  HG2 GLN A 135      33.206   7.874   5.292  1.00 75.76           H  
ATOM   1938  HG3 GLN A 135      31.807   8.598   5.516  1.00 75.76           H  
ATOM   1939 HE21 GLN A 135      31.753  10.933   4.673  1.00104.78           H  
ATOM   1940 HE22 GLN A 135      32.487  11.250   3.371  1.00104.78           H  
ATOM   1941  N   MET A 136      34.586  10.419   9.219  1.00 47.83           N  
ANISOU 1941  N   MET A 136     6028   3956   8190    290  -1521   -371       N  
ATOM   1942  CA  MET A 136      35.686  11.171   9.860  1.00 49.44           C  
ANISOU 1942  CA  MET A 136     6069   4085   8633    329  -1488   -200       C  
ATOM   1943  C   MET A 136      36.299  10.279  10.938  1.00 41.70           C  
ANISOU 1943  C   MET A 136     5051   2967   7826    320  -1470   -232       C  
ATOM   1944  O   MET A 136      37.526  10.230  11.033  1.00 48.82           O  
ANISOU 1944  O   MET A 136     5850   3791   8907    379  -1387   -100       O  
ATOM   1945  CB  MET A 136      35.186  12.475  10.494  1.00 44.20           C  
ANISOU 1945  CB  MET A 136     5299   3442   8053    277  -1648   -125       C  
ATOM   1946  CG  MET A 136      34.965  13.614   9.518  1.00 42.94           C  
ANISOU 1946  CG  MET A 136     5119   3385   7810    318  -1647      5       C  
ATOM   1947  SD  MET A 136      34.097  15.010  10.281  1.00 47.28           S  
ANISOU 1947  SD  MET A 136     5555   3913   8495    268  -1805     73       S  
ATOM   1948  CE  MET A 136      35.338  15.604  11.426  1.00 45.12           C  
ANISOU 1948  CE  MET A 136     5180   3474   8491    245  -1799    163       C  
ATOM   1949  H   MET A 136      33.756  10.744   9.380  1.00 57.72           H  
ATOM   1950  HA  MET A 136      36.370  11.370   9.181  1.00 59.65           H  
ATOM   1951  HB2 MET A 136      34.350  12.297  10.966  1.00 53.36           H  
ATOM   1952  HB3 MET A 136      35.840  12.758  11.161  1.00 53.36           H  
ATOM   1953  HG2 MET A 136      35.832  13.925   9.181  1.00 51.84           H  
ATOM   1954  HG3 MET A 136      34.442  13.292   8.754  1.00 51.84           H  
ATOM   1955  HE1 MET A 136      35.100  16.491  11.724  1.00 54.47           H  
ATOM   1956  HE2 MET A 136      35.385  15.011  12.186  1.00 54.47           H  
ATOM   1957  HE3 MET A 136      36.195  15.634  10.984  1.00 54.47           H  
ATOM   1958  N   LEU A 137      35.464   9.605  11.706  1.00 39.97           N  
ANISOU 1958  N   LEU A 137     4902   2709   7576    248  -1549   -383       N  
ATOM   1959  CA  LEU A 137      35.925   8.736  12.804  1.00 47.36           C  
ANISOU 1959  CA  LEU A 137     5829   3511   8653    244  -1539   -394       C  
ATOM   1960  C   LEU A 137      36.716   7.539  12.249  1.00 47.11           C  
ANISOU 1960  C   LEU A 137     5860   3407   8632    326  -1348   -424       C  
ATOM   1961  O   LEU A 137      37.729   7.188  12.846  1.00 47.34           O  
ANISOU 1961  O   LEU A 137     5811   3327   8849    383  -1296   -321       O  
ATOM   1962  CB  LEU A 137      34.712   8.318  13.631  1.00 48.84           C  
ANISOU 1962  CB  LEU A 137     6084   3663   8810    148  -1636   -525       C  
ATOM   1963  CG  LEU A 137      34.166   9.375  14.583  1.00 41.52           C  
ANISOU 1963  CG  LEU A 137     5109   2739   7926     89  -1768   -480       C  
ATOM   1964  CD1 LEU A 137      32.705   9.114  14.914  1.00 51.19           C  
ANISOU 1964  CD1 LEU A 137     6382   3966   9103     11  -1798   -606       C  
ATOM   1965  CD2 LEU A 137      35.011   9.424  15.841  1.00 44.84           C  
ANISOU 1965  CD2 LEU A 137     5517   3070   8449     85  -1821   -384       C  
ATOM   1966  H   LEU A 137      34.562   9.635  11.595  1.00 46.60           H  
ATOM   1967  HA  LEU A 137      36.532   9.264  13.372  1.00 57.15           H  
ATOM   1968  HB2 LEU A 137      33.999   8.041  13.022  1.00 58.93           H  
ATOM   1969  HB3 LEU A 137      34.962   7.532  14.155  1.00 58.93           H  
ATOM   1970  HG  LEU A 137      34.228  10.257  14.136  1.00 50.14           H  
ATOM   1971 HD11 LEU A 137      32.326   9.897  15.346  1.00 61.75           H  
ATOM   1972 HD12 LEU A 137      32.211   8.932  14.096  1.00 61.75           H  
ATOM   1973 HD13 LEU A 137      32.637   8.348  15.510  1.00 61.75           H  
ATOM   1974 HD21 LEU A 137      34.586   9.993  16.495  1.00 54.12           H  
ATOM   1975 HD22 LEU A 137      35.104   8.528  16.206  1.00 54.12           H  
ATOM   1976 HD23 LEU A 137      35.892   9.779  15.630  1.00 54.12           H  
ATOM   1977  N   ASP A 138      36.279   6.945  11.146  1.00 45.98           N  
ANISOU 1977  N   ASP A 138     5867   3310   8294    335  -1246   -558       N  
ATOM   1978  CA  ASP A 138      36.942   5.759  10.556  1.00 50.73           C  
ANISOU 1978  CA  ASP A 138     6577   3806   8891    420  -1020   -617       C  
ATOM   1979  C   ASP A 138      38.325   6.118  10.030  1.00 50.40           C  
ANISOU 1979  C   ASP A 138     6438   3739   8972    562   -815   -428       C  
ATOM   1980  O   ASP A 138      39.263   5.392  10.345  1.00 51.01           O  
ANISOU 1980  O   ASP A 138     6447   3677   9258    657   -657   -348       O  
ATOM   1981  CB  ASP A 138      36.121   5.153   9.423  1.00 50.98           C  
ANISOU 1981  CB  ASP A 138     6848   3879   8642    374   -978   -832       C  
ATOM   1982  CG  ASP A 138      36.794   3.965   8.756  1.00 74.17           C  
ANISOU 1982  CG  ASP A 138     9959   6673  11551    464   -705   -926       C  
ATOM   1983  OD1 ASP A 138      37.210   3.041   9.482  1.00 75.01           O  
ANISOU 1983  OD1 ASP A 138    10021   6614  11864    500   -621   -919       O  
ATOM   1984  OD2 ASP A 138      36.913   3.982   7.518  1.00 74.02           O  
ANISOU 1984  OD2 ASP A 138    10140   6691  11292    506   -562  -1001       O  
ATOM   1985  H   ASP A 138      35.555   7.242  10.681  1.00 55.49           H  
ATOM   1986  HA  ASP A 138      37.042   5.080  11.263  1.00 61.19           H  
ATOM   1987  HB2 ASP A 138      35.256   4.860   9.775  1.00 61.49           H  
ATOM   1988  HB3 ASP A 138      35.958   5.835   8.739  1.00 61.49           H  
ATOM   1989  N   ILE A 139      38.452   7.227   9.306  1.00 47.97           N  
ANISOU 1989  N   ILE A 139     6102   3551   8571    586   -799   -330       N  
ATOM   1990  CA  ILE A 139      39.749   7.631   8.699  1.00 54.60           C  
ANISOU 1990  CA  ILE A 139     6831   4354   9562    720   -565   -128       C  
ATOM   1991  C   ILE A 139      40.731   7.913   9.839  1.00 49.47           C  
ANISOU 1991  C   ILE A 139     5891   3612   9294    731   -649     79       C  
ATOM   1992  O   ILE A 139      41.888   7.514   9.719  1.00 54.31           O  
ANISOU 1992  O   ILE A 139     6362   4117  10156    846   -448    238       O  
ATOM   1993  CB  ILE A 139      39.582   8.801   7.713  1.00 49.77           C  
ANISOU 1993  CB  ILE A 139     6254   3883   8773    734   -536    -41       C  
ATOM   1994  CG1 ILE A 139      38.658   8.423   6.549  1.00 57.66           C  
ANISOU 1994  CG1 ILE A 139     7552   4993   9364    687   -571   -246       C  
ATOM   1995  CG2 ILE A 139      40.940   9.261   7.203  1.00 63.07           C  
ANISOU 1995  CG2 ILE A 139     7864   5511  10589    885   -206    159       C  
ATOM   1996  CD1 ILE A 139      38.320   9.554   5.604  1.00 61.94           C  
ANISOU 1996  CD1 ILE A 139     8183   5672   9678    723   -525   -142       C  
ATOM   1997  H   ILE A 139      37.779   7.829   9.198  1.00 57.88           H  
ATOM   1998  HA  ILE A 139      40.090   6.868   8.197  1.00 65.84           H  
ATOM   1999  HB  ILE A 139      39.167   9.554   8.202  1.00 60.04           H  
ATOM   2000 HG12 ILE A 139      39.089   7.710   6.034  1.00 69.51           H  
ATOM   2001 HG13 ILE A 139      37.824   8.062   6.908  1.00 69.51           H  
ATOM   2002 HG21 ILE A 139      40.825   9.974   6.553  1.00 76.00           H  
ATOM   2003 HG22 ILE A 139      41.478   9.592   7.942  1.00 76.00           H  
ATOM   2004 HG23 ILE A 139      41.400   8.515   6.781  1.00 76.00           H  
ATOM   2005 HD11 ILE A 139      37.484   9.358   5.148  1.00 74.64           H  
ATOM   2006 HD12 ILE A 139      38.227  10.384   6.104  1.00 74.64           H  
ATOM   2007 HD13 ILE A 139      39.031   9.654   4.946  1.00 74.64           H  
ATOM   2008  N   ALA A 140      40.287   8.558  10.905  1.00 52.07           N  
ANISOU 2008  N   ALA A 140     6134   3969   9681    613   -944     86       N  
ATOM   2009  CA  ALA A 140      41.139   8.913  12.058  1.00 56.19           C  
ANISOU 2009  CA  ALA A 140     6428   4404  10516    591  -1091    267       C  
ATOM   2010  C   ALA A 140      41.566   7.678  12.834  1.00 44.76           C  
ANISOU 2010  C   ALA A 140     4962   2825   9219    619  -1103    265       C  
ATOM   2011  O   ALA A 140      42.724   7.625  13.210  1.00 48.92           O  
ANISOU 2011  O   ALA A 140     5281   3254  10052    667  -1122    463       O  
ATOM   2012  CB  ALA A 140      40.420   9.894  12.943  1.00 42.55           C  
ANISOU 2012  CB  ALA A 140     4690   2727   8752    455  -1382    250       C  
ATOM   2013  H   ALA A 140      39.421   8.817  11.013  1.00 62.80           H  
ATOM   2014  HA  ALA A 140      41.950   9.351  11.712  1.00 67.74           H  
ATOM   2015  HB1 ALA A 140      41.010  10.175  13.661  1.00 49.47           H  
ATOM   2016  HB2 ALA A 140      40.154  10.671  12.422  1.00 49.47           H  
ATOM   2017  HB3 ALA A 140      39.629   9.474  13.323  1.00 49.47           H  
ATOM   2018  N   ILE A 141      40.653   6.740  13.071  1.00 55.71           N  
ANISOU 2018  N   ILE A 141     6546   4197  10425    586  -1106     66       N  
ATOM   2019  CA  ILE A 141      40.941   5.490  13.835  1.00 44.73           C  
ANISOU 2019  CA  ILE A 141     5159   2663   9174    627  -1082     77       C  
ATOM   2020  C   ILE A 141      41.989   4.708  13.045  1.00 48.73           C  
ANISOU 2020  C   ILE A 141     5594   3058   9863    793   -775    171       C  
ATOM   2021  O   ILE A 141      42.935   4.233  13.648  1.00 48.47           O  
ANISOU 2021  O   ILE A 141     5390   2897  10129    872   -763    351       O  
ATOM   2022  CB  ILE A 141      39.650   4.688  14.086  1.00 58.72           C  
ANISOU 2022  CB  ILE A 141     7157   4420  10733    552  -1103   -156       C  
ATOM   2023  CG1 ILE A 141      38.768   5.338  15.159  1.00 57.27           C  
ANISOU 2023  CG1 ILE A 141     7015   4309  10434    411  -1359   -210       C  
ATOM   2024  CG2 ILE A 141      39.957   3.236  14.424  1.00 58.42           C  
ANISOU 2024  CG2 ILE A 141     7143   4208  10846    614  -1020   -136       C  
ATOM   2025  CD1 ILE A 141      37.318   4.898  15.133  1.00 41.21           C  
ANISOU 2025  CD1 ILE A 141     5160   2277   8219    325  -1358   -425       C  
ATOM   2026  H   ILE A 141      39.797   6.805  12.771  1.00 67.17           H  
ATOM   2027  HA  ILE A 141      41.324   5.737  14.698  1.00 52.09           H  
ATOM   2028  HB  ILE A 141      39.136   4.687  13.242  1.00 70.78           H  
ATOM   2029 HG12 ILE A 141      39.143   5.128  16.041  1.00 69.04           H  
ATOM   2030 HG13 ILE A 141      38.801   6.310  15.047  1.00 69.04           H  
ATOM   2031 HG21 ILE A 141      39.146   2.789  14.716  1.00 70.42           H  
ATOM   2032 HG22 ILE A 141      40.306   2.779  13.640  1.00 70.42           H  
ATOM   2033 HG23 ILE A 141      40.612   3.201  15.138  1.00 70.42           H  
ATOM   2034 HD11 ILE A 141      36.782   5.511  15.666  1.00 47.85           H  
ATOM   2035 HD12 ILE A 141      36.990   4.898  14.217  1.00 47.85           H  
ATOM   2036 HD13 ILE A 141      37.241   4.001  15.501  1.00 47.85           H  
ATOM   2037  N   LYS A 142      41.840   4.643  11.731  1.00 51.06           N  
ANISOU 2037  N   LYS A 142     6029   3392   9979    855   -516     62       N  
ATOM   2038  CA  LYS A 142      42.806   3.945  10.859  1.00 50.85           C  
ANISOU 2038  CA  LYS A 142     5984   3240  10096   1031   -146    135       C  
ATOM   2039  C   LYS A 142      44.166   4.634  10.886  1.00 52.23           C  
ANISOU 2039  C   LYS A 142     5825   3376  10643   1124    -86    450       C  
ATOM   2040  O   LYS A 142      45.147   3.919  11.093  1.00 54.19           O  
ANISOU 2040  O   LYS A 142     5888   3467  11236   1248     53    624       O  
ATOM   2041  CB  LYS A 142      42.267   3.862   9.431  1.00 52.27           C  
ANISOU 2041  CB  LYS A 142     6439   3484   9936   1062     99    -47       C  
ATOM   2042  CG  LYS A 142      41.179   2.823   9.223  1.00 55.14           C  
ANISOU 2042  CG  LYS A 142     7118   3819  10012    986     90   -352       C  
ATOM   2043  CD  LYS A 142      40.459   2.946   7.908  1.00 64.77           C  
ANISOU 2043  CD  LYS A 142     8647   5135  10826    958    196   -553       C  
ATOM   2044  CE  LYS A 142      39.829   1.637   7.483  1.00 71.27           C  
ANISOU 2044  CE  LYS A 142     9773   5824  11482    927    302   -831       C  
ATOM   2045  NZ  LYS A 142      38.833   1.820   6.403  1.00 74.62           N  
ANISOU 2045  NZ  LYS A 142    10519   6360  11475    812    220  -1079       N  
ATOM   2046  H   LYS A 142      41.146   5.038  11.293  1.00 61.59           H  
ATOM   2047  HA  LYS A 142      42.918   3.030  11.201  1.00 59.60           H  
ATOM   2048  HB2 LYS A 142      41.917   4.741   9.173  1.00 63.04           H  
ATOM   2049  HB3 LYS A 142      43.014   3.653   8.833  1.00 63.04           H  
ATOM   2050  HG2 LYS A 142      41.585   1.932   9.279  1.00 66.48           H  
ATOM   2051  HG3 LYS A 142      40.526   2.898   9.951  1.00 66.48           H  
ATOM   2052  HD2 LYS A 142      39.761   3.630   7.987  1.00 78.04           H  
ATOM   2053  HD3 LYS A 142      41.093   3.235   7.218  1.00 78.04           H  
ATOM   2054  HE2 LYS A 142      40.525   1.028   7.171  1.00 85.84           H  
ATOM   2055  HE3 LYS A 142      39.389   1.223   8.251  1.00 85.84           H  
ATOM   2056  HZ1 LYS A 142      38.577   1.010   6.085  1.00 89.87           H  
ATOM   2057  HZ2 LYS A 142      38.105   2.254   6.725  1.00 89.87           H  
ATOM   2058  HZ3 LYS A 142      39.197   2.301   5.726  1.00 89.87           H  
ATOM   2059  N   SER A 143      44.230   5.963  10.763  1.00 52.40           N  
ANISOU 2059  N   SER A 143     5744   3526  10641   1064   -193    546       N  
ATOM   2060  CA  SER A 143      45.496   6.735  10.690  1.00 53.23           C  
ANISOU 2060  CA  SER A 143     5516   3583  11126   1132   -123    849       C  
ATOM   2061  C   SER A 143      46.220   6.670  12.027  1.00 53.30           C  
ANISOU 2061  C   SER A 143     5248   3551  11452   1058   -421   1030       C  
ATOM   2062  O   SER A 143      47.435   6.805  12.019  1.00 55.60           O  
ANISOU 2062  O   SER A 143     5242   3834  12048   1086   -339   1270       O  
ATOM   2063  CB  SER A 143      45.253   8.155  10.223  1.00 52.92           C  
ANISOU 2063  CB  SER A 143     5450   3682  10976   1057   -190    900       C  
ATOM   2064  OG  SER A 143      44.687   8.967  11.241  1.00 64.71           O  
ANISOU 2064  OG  SER A 143     6903   5244  12438    882   -605    874       O  
ATOM   2065  H   SER A 143      43.492   6.496  10.754  1.00 63.20           H  
ATOM   2066  HA  SER A 143      46.074   6.289  10.015  1.00 63.39           H  
ATOM   2067  HB2 SER A 143      46.107   8.549   9.934  1.00 63.83           H  
ATOM   2068  HB3 SER A 143      44.650   8.142   9.445  1.00 63.83           H  
ATOM   2069  HG  SER A 143      44.199   8.506  11.749  1.00 77.97           H  
ATOM   2070  N   ALA A 144      45.492   6.524  13.121  1.00 51.24           N  
ANISOU 2070  N   ALA A 144     5103   3345  11021    917   -753    903       N  
ATOM   2071  CA  ALA A 144      46.057   6.460  14.481  1.00 51.95           C  
ANISOU 2071  CA  ALA A 144     5025   3472  11240    801  -1047   1031       C  
ATOM   2072  C   ALA A 144      46.335   5.014  14.907  1.00 52.98           C  
ANISOU 2072  C   ALA A 144     5162   3522  11444    879   -963   1056       C  
ATOM   2073  O   ALA A 144      46.711   4.831  16.064  1.00 67.03           O  
ANISOU 2073  O   ALA A 144     6835   5314  13319    796  -1219   1170       O  
ATOM   2074  CB  ALA A 144      45.099   7.117  15.421  1.00 49.18           C  
ANISOU 2074  CB  ALA A 144     4831   3202  10651    621  -1418    899       C  
ATOM   2075  H   ALA A 144      44.587   6.426  13.115  1.00 59.89           H  
ATOM   2076  HA  ALA A 144      46.906   6.959  14.498  1.00 62.65           H  
ATOM   2077  HB1 ALA A 144      45.525   7.245  16.285  1.00 57.42           H  
ATOM   2078  HB2 ALA A 144      44.836   7.981  15.063  1.00 57.42           H  
ATOM   2079  HB3 ALA A 144      44.311   6.557  15.529  1.00 57.42           H  
ATOM   2080  N   GLY A 145      46.113   4.030  14.033  1.00 56.85           N  
ANISOU 2080  N   GLY A 145     5802   3910  11888   1031   -619    948       N  
ATOM   2081  CA  GLY A 145      46.327   2.599  14.333  1.00 56.98           C  
ANISOU 2081  CA  GLY A 145     5832   3827  11990   1115   -500    975       C  
ATOM   2082  C   GLY A 145      45.478   2.117  15.483  1.00 55.42           C  
ANISOU 2082  C   GLY A 145     5839   3636  11583   1015   -734    840       C  
ATOM   2083  O   GLY A 145      45.990   1.344  16.294  1.00 54.96           O  
ANISOU 2083  O   GLY A 145     5730   3523  11630   1042   -771    944       O  
ATOM   2084  H   GLY A 145      45.790   4.183  13.199  1.00 68.54           H  
ATOM   2085  HA2 GLY A 145      46.115   2.067  13.524  1.00 68.69           H  
ATOM   2086  HA3 GLY A 145      47.282   2.459  14.550  1.00 68.69           H  
ATOM   2087  N   MET A 146      44.239   2.581  15.565  1.00 50.95           N  
ANISOU 2087  N   MET A 146     5499   3128  10733    905   -872    626       N  
ATOM   2088  CA  MET A 146      43.313   2.204  16.647  1.00 49.48           C  
ANISOU 2088  CA  MET A 146     5500   2958  10344    795  -1072    512       C  
ATOM   2089  C   MET A 146      42.311   1.170  16.129  1.00 49.10           C  
ANISOU 2089  C   MET A 146     5713   2818  10124    816   -867    271       C  
ATOM   2090  O   MET A 146      41.477   0.728  16.911  1.00 48.16           O  
ANISOU 2090  O   MET A 146     5746   2703   9849    727   -972    179       O  
ATOM   2091  CB  MET A 146      42.623   3.459  17.176  1.00 49.58           C  
ANISOU 2091  CB  MET A 146     5572   3097  10170    636  -1361    445       C  
ATOM   2092  CG  MET A 146      43.485   4.281  18.093  1.00 47.85           C  
ANISOU 2092  CG  MET A 146     5164   2938  10078    559  -1648    646       C  
ATOM   2093  SD  MET A 146      42.730   5.882  18.395  1.00 57.86           S  
ANISOU 2093  SD  MET A 146     6529   4315  11140    396  -1906    542       S  
ATOM   2094  CE  MET A 146      42.664   5.895  20.179  1.00 52.78           C  
ANISOU 2094  CE  MET A 146     5963   3653  10436    281  -2264    631       C  
ATOM   2095  H   MET A 146      43.889   3.156  14.954  1.00 59.55           H  
ATOM   2096  HA  MET A 146      43.830   1.794  17.372  1.00 57.79           H  
ATOM   2097  HB2 MET A 146      42.351   4.015  16.422  1.00 59.82           H  
ATOM   2098  HB3 MET A 146      41.815   3.196  17.657  1.00 59.82           H  
ATOM   2099  HG2 MET A 146      43.600   3.809  18.945  1.00 55.83           H  
ATOM   2100  HG3 MET A 146      44.368   4.411  17.689  1.00 55.83           H  
ATOM   2101  HE1 MET A 146      42.586   6.802  20.490  1.00 63.65           H  
ATOM   2102  HE2 MET A 146      41.900   5.388  20.471  1.00 63.65           H  
ATOM   2103  HE3 MET A 146      43.471   5.505  20.533  1.00 63.65           H  
ATOM   2104  N   SER A 147      42.433   0.758  14.875  1.00 50.15           N  
ANISOU 2104  N   SER A 147     5917   2857  10280    921   -569    163       N  
ATOM   2105  CA  SER A 147      41.522  -0.233  14.263  1.00 56.75           C  
ANISOU 2105  CA  SER A 147     7021   3584  10959    913   -392    -95       C  
ATOM   2106  C   SER A 147      41.560  -1.524  15.090  1.00 51.40           C  
ANISOU 2106  C   SER A 147     6390   2815  10325    925   -356    -53       C  
ATOM   2107  O   SER A 147      42.664  -2.002  15.343  1.00 53.32           O  
ANISOU 2107  O   SER A 147     6478   2995  10788   1042   -272    157       O  
ATOM   2108  CB  SER A 147      41.887  -0.468  12.838  1.00 52.38           C  
ANISOU 2108  CB  SER A 147     6560   2897  10446   1051    -41   -195       C  
ATOM   2109  OG  SER A 147      41.832   0.733  12.096  1.00 51.63           O  
ANISOU 2109  OG  SER A 147     6461   2964  10193   1020    -62   -225       O  
ATOM   2110  H   SER A 147      43.067   1.051  14.296  1.00 58.59           H  
ATOM   2111  HA  SER A 147      40.604   0.140  14.295  1.00 68.42           H  
ATOM   2112  HB2 SER A 147      42.794  -0.838  12.789  1.00 61.27           H  
ATOM   2113  HB3 SER A 147      41.268  -1.127  12.446  1.00 61.27           H  
ATOM   2114  HG  SER A 147      42.040   0.562  11.298  1.00 60.37           H  
ATOM   2115  N   GLY A 148      40.408  -2.036  15.512  1.00 50.39           N  
ANISOU 2115  N   GLY A 148     6458   2683  10005    801   -417   -234       N  
ATOM   2116  CA  GLY A 148      40.288  -3.258  16.322  1.00 51.40           C  
ANISOU 2116  CA  GLY A 148     6659   2711  10159    803   -372   -198       C  
ATOM   2117  C   GLY A 148      40.201  -3.001  17.810  1.00 53.08           C  
ANISOU 2117  C   GLY A 148     6811   3004  10354    733   -628    -31       C  
ATOM   2118  O   GLY A 148      39.884  -3.948  18.524  1.00 51.18           O  
ANISOU 2118  O   GLY A 148     6669   2678  10100    719   -600     -9       O  
ATOM   2119  H   GLY A 148      39.610  -1.630  15.350  1.00 58.88           H  
ATOM   2120  HA2 GLY A 148      39.477  -3.746  16.035  1.00 60.09           H  
ATOM   2121  HA3 GLY A 148      41.064  -3.843  16.139  1.00 60.09           H  
ATOM   2122  N   LEU A 149      40.455  -1.778  18.271  1.00 52.39           N  
ANISOU 2122  N   LEU A 149     6595   3058  10255    687   -869     81       N  
ATOM   2123  CA  LEU A 149      40.464  -1.459  19.722  1.00 57.94           C  
ANISOU 2123  CA  LEU A 149     7290   3809  10917    625  -1122    232       C  
ATOM   2124  C   LEU A 149      39.063  -1.133  20.224  1.00 55.06           C  
ANISOU 2124  C   LEU A 149     7107   3514  10301    479  -1208     79       C  
ATOM   2125  O   LEU A 149      38.853  -1.333  21.415  1.00 65.99           O  
ANISOU 2125  O   LEU A 149     8588   4869  11614    440  -1315    163       O  
ATOM   2126  CB  LEU A 149      41.438  -0.314  20.012  1.00 48.89           C  
ANISOU 2126  CB  LEU A 149     5942   2758   9876    624  -1359    417       C  
ATOM   2127  CG  LEU A 149      42.913  -0.555  19.686  1.00 51.20           C  
ANISOU 2127  CG  LEU A 149     5984   3004  10468    755  -1296    635       C  
ATOM   2128  CD1 LEU A 149      43.739   0.676  20.025  1.00 51.39           C  
ANISOU 2128  CD1 LEU A 149     5798   3132  10596    699  -1568    803       C  
ATOM   2129  CD2 LEU A 149      43.463  -1.767  20.423  1.00 53.52           C  
ANISOU 2129  CD2 LEU A 149     6262   3179  10892    839  -1263    800       C  
ATOM   2130  H   LEU A 149      40.599  -1.063  17.729  1.00 63.19           H  
ATOM   2131  HA  LEU A 149      40.769  -2.259  20.204  1.00 69.85           H  
ATOM   2132  HB2 LEU A 149      41.137   0.472  19.514  1.00 57.07           H  
ATOM   2133  HB3 LEU A 149      41.370  -0.094  20.962  1.00 57.07           H  
ATOM   2134  HG  LEU A 149      42.994  -0.722  18.715  1.00 59.85           H  
ATOM   2135 HD11 LEU A 149      44.609   0.612  19.595  1.00 60.08           H  
ATOM   2136 HD12 LEU A 149      43.280   1.473  19.709  1.00 60.08           H  
ATOM   2137 HD13 LEU A 149      43.856   0.734  20.988  1.00 60.08           H  
ATOM   2138 HD21 LEU A 149      44.434  -1.777  20.352  1.00 64.13           H  
ATOM   2139 HD22 LEU A 149      43.210  -1.722  21.362  1.00 64.13           H  
ATOM   2140 HD23 LEU A 149      43.104  -2.580  20.030  1.00 64.13           H  
ATOM   2141  N   PHE A 150      38.146  -0.668  19.377  1.00 46.50           N  
ANISOU 2141  N   PHE A 150     6071   2510   9087    406  -1153   -125       N  
ATOM   2142  CA  PHE A 150      36.797  -0.220  19.817  1.00 50.90           C  
ANISOU 2142  CA  PHE A 150     6745   3152   9443    275  -1208   -248       C  
ATOM   2143  C   PHE A 150      35.685  -1.132  19.295  1.00 50.09           C  
ANISOU 2143  C   PHE A 150     6752   2999   9279    216  -1023   -438       C  
ATOM   2144  O   PHE A 150      35.623  -1.385  18.087  1.00 48.59           O  
ANISOU 2144  O   PHE A 150     6569   2772   9122    238   -907   -566       O  
ATOM   2145  CB  PHE A 150      36.544   1.234  19.414  1.00 42.50           C  
ANISOU 2145  CB  PHE A 150     5615   2239   8295    221  -1333   -304       C  
ATOM   2146  CG  PHE A 150      37.468   2.234  20.056  1.00 42.40           C  
ANISOU 2146  CG  PHE A 150     5510   2271   8330    236  -1541   -137       C  
ATOM   2147  CD1 PHE A 150      37.247   2.669  21.350  1.00 46.62           C  
ANISOU 2147  CD1 PHE A 150     6141   2815   8756    176  -1699    -68       C  
ATOM   2148  CD2 PHE A 150      38.559   2.734  19.370  1.00 42.79           C  
ANISOU 2148  CD2 PHE A 150     5391   2330   8536    304  -1573    -48       C  
ATOM   2149  CE1 PHE A 150      38.101   3.582  21.943  1.00 48.25           C  
ANISOU 2149  CE1 PHE A 150     6293   3041   8999    162  -1933     66       C  
ATOM   2150  CE2 PHE A 150      39.411   3.647  19.966  1.00 44.91           C  
ANISOU 2150  CE2 PHE A 150     5551   2633   8879    290  -1788    110       C  
ATOM   2151  CZ  PHE A 150      39.178   4.071  21.249  1.00 45.81           C  
ANISOU 2151  CZ  PHE A 150     5776   2755   8873    208  -1993    156       C  
ATOM   2152  H   PHE A 150      38.272  -0.592  18.477  1.00 56.12           H  
ATOM   2153  HA  PHE A 150      36.771  -0.256  20.804  1.00 61.40           H  
ATOM   2154  HB2 PHE A 150      36.625   1.306  18.441  1.00 49.41           H  
ATOM   2155  HB3 PHE A 150      35.620   1.462  19.652  1.00 49.41           H  
ATOM   2156  HD1 PHE A 150      36.509   2.336  21.834  1.00 56.26           H  
ATOM   2157  HD2 PHE A 150      38.727   2.447  18.486  1.00 50.25           H  
ATOM   2158  HE1 PHE A 150      37.939   3.871  22.824  1.00 58.22           H  
ATOM   2159  HE2 PHE A 150      40.151   3.981  19.485  1.00 54.21           H  
ATOM   2160  HZ  PHE A 150      39.759   4.694  21.655  1.00 55.29           H  
ATOM   2161  N   ASP A 151      34.829  -1.606  20.191  1.00 44.33           N  
ANISOU 2161  N   ASP A 151     6126   2252   8466    135   -998   -457       N  
ATOM   2162  CA  ASP A 151      33.689  -2.482  19.831  1.00 49.63           C  
ANISOU 2162  CA  ASP A 151     6878   2866   9114     51   -847   -616       C  
ATOM   2163  C   ASP A 151      32.665  -1.696  19.015  1.00 56.95           C  
ANISOU 2163  C   ASP A 151     7761   3925   9953    -57   -892   -777       C  
ATOM   2164  O   ASP A 151      32.124  -2.291  18.071  1.00 46.13           O  
ANISOU 2164  O   ASP A 151     6421   2522   8583   -127   -826   -935       O  
ATOM   2165  CB  ASP A 151      33.113  -3.126  21.088  1.00 45.76           C  
ANISOU 2165  CB  ASP A 151     6498   2274   8615     11   -775   -543       C  
ATOM   2166  CG  ASP A 151      34.145  -3.956  21.830  1.00 62.38           C  
ANISOU 2166  CG  ASP A 151     8660   4220  10822    118   -728   -377       C  
ATOM   2167  OD1 ASP A 151      34.658  -4.922  21.231  1.00 71.36           O  
ANISOU 2167  OD1 ASP A 151     9833   5228  12052    152   -582   -421       O  
ATOM   2168  OD2 ASP A 151      34.460  -3.611  22.977  1.00 53.06           O  
ANISOU 2168  OD2 ASP A 151     7500   3031   9628    169   -853   -198       O  
ATOM   2169  H   ASP A 151      34.872  -1.397  21.074  1.00 52.48           H  
ATOM   2170  HA  ASP A 151      34.037  -3.207  19.261  1.00 59.88           H  
ATOM   2171  HB2 ASP A 151      32.765  -2.434  21.688  1.00 53.32           H  
ATOM   2172  HB3 ASP A 151      32.370  -3.710  20.834  1.00 53.32           H  
ATOM   2173  N   ARG A 152      32.390  -0.438  19.381  1.00 42.81           N  
ANISOU 2173  N   ARG A 152     5908   2265   8093    -75  -1017   -734       N  
ATOM   2174  CA  ARG A 152      31.405   0.422  18.675  1.00 46.24           C  
ANISOU 2174  CA  ARG A 152     6270   2819   8478   -154  -1079   -847       C  
ATOM   2175  C   ARG A 152      31.939   1.831  18.396  1.00 40.75           C  
ANISOU 2175  C   ARG A 152     5493   2239   7749   -104  -1218   -790       C  
ATOM   2176  O   ARG A 152      32.511   2.410  19.310  1.00 40.65           O  
ANISOU 2176  O   ARG A 152     5488   2238   7720    -60  -1284   -662       O  
ATOM   2177  CB  ARG A 152      30.117   0.546  19.486  1.00 41.87           C  
ANISOU 2177  CB  ARG A 152     5721   2271   7917   -242  -1036   -849       C  
ATOM   2178  CG  ARG A 152      29.371  -0.754  19.747  1.00 45.92           C  
ANISOU 2178  CG  ARG A 152     6294   2656   8499   -315   -896   -896       C  
ATOM   2179  CD  ARG A 152      28.755  -1.374  18.508  1.00 46.86           C  
ANISOU 2179  CD  ARG A 152     6372   2773   8662   -402   -910  -1064       C  
ATOM   2180  NE  ARG A 152      27.853  -0.474  17.804  1.00 44.28           N  
ANISOU 2180  NE  ARG A 152     5916   2569   8341   -469  -1041  -1137       N  
ATOM   2181  CZ  ARG A 152      26.589  -0.205  18.131  1.00 55.94           C  
ANISOU 2181  CZ  ARG A 152     7286   4051   9918   -556  -1043  -1139       C  
ATOM   2182  NH1 ARG A 152      26.011  -0.755  19.188  1.00 66.11           N  
ANISOU 2182  NH1 ARG A 152     8603   5223  11294   -591   -895  -1081       N  
ATOM   2183  NH2 ARG A 152      25.897   0.639  17.387  1.00 57.74           N  
ANISOU 2183  NH2 ARG A 152     7373   4376  10188   -603  -1187  -1185       N  
ATOM   2184  H   ARG A 152      32.763  -0.046  20.114  1.00 51.69           H  
ATOM   2185  HA  ARG A 152      31.191   0.003  17.814  1.00 55.80           H  
ATOM   2186  HB2 ARG A 152      30.338   0.955  20.347  1.00 50.12           H  
ATOM   2187  HB3 ARG A 152      29.518   1.163  19.016  1.00 50.12           H  
ATOM   2188  HG2 ARG A 152      29.987  -1.402  20.149  1.00 55.42           H  
ATOM   2189  HG3 ARG A 152      28.658  -0.583  20.398  1.00 55.42           H  
ATOM   2190  HD2 ARG A 152      29.473  -1.638  17.896  1.00 56.56           H  
ATOM   2191  HD3 ARG A 152      28.274  -2.190  18.759  1.00 56.56           H  
ATOM   2192  HE  ARG A 152      28.169  -0.078  17.100  1.00 53.46           H  
ATOM   2193 HH11 ARG A 152      26.441  -1.315  19.702  1.00 79.66           H  
ATOM   2194 HH12 ARG A 152      25.177  -0.555  19.379  1.00 79.66           H  
ATOM   2195 HH21 ARG A 152      26.267   1.017  16.683  1.00 69.60           H  
ATOM   2196 HH22 ARG A 152      25.062   0.829  17.595  1.00 69.60           H  
ATOM   2197  N   VAL A 153      31.780   2.337  17.173  1.00 50.87           N  
ANISOU 2197  N   VAL A 153     6717   3589   9023   -120  -1281   -887       N  
ATOM   2198  CA  VAL A 153      32.081   3.750  16.812  1.00 49.85           C  
ANISOU 2198  CA  VAL A 153     6507   3553   8879    -86  -1405   -837       C  
ATOM   2199  C   VAL A 153      30.704   4.406  16.659  1.00 53.78           C  
ANISOU 2199  C   VAL A 153     6943   4134   9356   -165  -1465   -896       C  
ATOM   2200  O   VAL A 153      30.043   4.125  15.650  1.00 41.40           O  
ANISOU 2200  O   VAL A 153     5357   2579   7794   -224  -1512  -1015       O  
ATOM   2201  CB  VAL A 153      32.963   3.852  15.561  1.00 44.44           C  
ANISOU 2201  CB  VAL A 153     5820   2835   8231    -21  -1422   -874       C  
ATOM   2202  CG1 VAL A 153      33.262   5.295  15.186  1.00 40.23           C  
ANISOU 2202  CG1 VAL A 153     5201   2374   7710     10  -1541   -798       C  
ATOM   2203  CG2 VAL A 153      34.255   3.074  15.736  1.00 40.71           C  
ANISOU 2203  CG2 VAL A 153     5373   2244   7850     77  -1320   -798       C  
ATOM   2204  H   VAL A 153      31.446   1.853  16.478  1.00 61.36           H  
ATOM   2205  HA  VAL A 153      32.548   4.173  17.553  1.00 60.13           H  
ATOM   2206  HB  VAL A 153      32.467   3.443  14.810  1.00 53.65           H  
ATOM   2207 HG11 VAL A 153      33.871   5.315  14.428  1.00 48.59           H  
ATOM   2208 HG12 VAL A 153      32.437   5.750  14.947  1.00 48.59           H  
ATOM   2209 HG13 VAL A 153      33.675   5.749  15.942  1.00 48.59           H  
ATOM   2210 HG21 VAL A 153      34.813   3.187  14.947  1.00 47.26           H  
ATOM   2211 HG22 VAL A 153      34.730   3.406  16.518  1.00 47.26           H  
ATOM   2212 HG23 VAL A 153      34.055   2.130  15.855  1.00 47.26           H  
ATOM   2213  N   LEU A 154      30.293   5.255  17.606  1.00 49.47           N  
ANISOU 2213  N   LEU A 154     6375   3622   8799   -169  -1472   -815       N  
ATOM   2214  CA  LEU A 154      28.949   5.890  17.635  1.00 49.24           C  
ANISOU 2214  CA  LEU A 154     6266   3625   8817   -224  -1487   -843       C  
ATOM   2215  C   LEU A 154      29.040   7.357  17.190  1.00 51.05           C  
ANISOU 2215  C   LEU A 154     6419   3918   9059   -186  -1599   -793       C  
ATOM   2216  O   LEU A 154      29.879   8.072  17.756  1.00 48.79           O  
ANISOU 2216  O   LEU A 154     6171   3641   8726   -136  -1616   -706       O  
ATOM   2217  CB  LEU A 154      28.392   5.750  19.052  1.00 49.23           C  
ANISOU 2217  CB  LEU A 154     6327   3556   8822   -245  -1357   -798       C  
ATOM   2218  CG  LEU A 154      28.291   4.333  19.620  1.00 49.71           C  
ANISOU 2218  CG  LEU A 154     6485   3518   8883   -277  -1231   -812       C  
ATOM   2219  CD1 LEU A 154      27.804   4.371  21.057  1.00 50.32           C  
ANISOU 2219  CD1 LEU A 154     6682   3493   8945   -285  -1094   -750       C  
ATOM   2220  CD2 LEU A 154      27.372   3.456  18.785  1.00 47.45           C  
ANISOU 2220  CD2 LEU A 154     6114   3211   8704   -362  -1219   -921       C  
ATOM   2221  H   LEU A 154      30.837   5.535  18.272  1.00 59.68           H  
ATOM   2222  HA  LEU A 154      28.363   5.411  17.011  1.00 59.40           H  
ATOM   2223  HB2 LEU A 154      28.948   6.281  19.653  1.00 59.39           H  
ATOM   2224  HB3 LEU A 154      27.498   6.147  19.064  1.00 59.39           H  
ATOM   2225  HG  LEU A 154      29.194   3.929  19.613  1.00 59.97           H  
ATOM   2226 HD11 LEU A 154      27.808   3.471  21.426  1.00 60.70           H  
ATOM   2227 HD12 LEU A 154      28.392   4.938  21.586  1.00 60.70           H  
ATOM   2228 HD13 LEU A 154      26.900   4.729  21.084  1.00 60.70           H  
ATOM   2229 HD21 LEU A 154      27.204   2.621  19.255  1.00 57.26           H  
ATOM   2230 HD22 LEU A 154      26.530   3.917  18.636  1.00 57.26           H  
ATOM   2231 HD23 LEU A 154      27.792   3.263  17.929  1.00 57.26           H  
ATOM   2232  N   SER A 155      28.217   7.795  16.232  1.00 45.25           N  
ANISOU 2232  N   SER A 155     5576   3211   8405   -223  -1697   -841       N  
ATOM   2233  CA  SER A 155      28.241   9.160  15.644  1.00 39.30           C  
ANISOU 2233  CA  SER A 155     4746   2488   7698   -190  -1813   -786       C  
ATOM   2234  C   SER A 155      26.927   9.889  15.901  1.00 55.94           C  
ANISOU 2234  C   SER A 155     6729   4567   9961   -217  -1815   -761       C  
ATOM   2235  O   SER A 155      25.883   9.244  15.810  1.00 41.46           O  
ANISOU 2235  O   SER A 155     4811   2706   8237   -288  -1806   -814       O  
ATOM   2236  CB  SER A 155      28.524   9.120  14.178  1.00 46.58           C  
ANISOU 2236  CB  SER A 155     5653   3503   8542   -189  -1932   -819       C  
ATOM   2237  OG  SER A 155      28.268  10.369  13.563  1.00 53.14           O  
ANISOU 2237  OG  SER A 155     6395   4439   9358   -142  -2006   -712       O  
ATOM   2238  H   SER A 155      27.553   7.283  15.877  1.00 54.62           H  
ATOM   2239  HA  SER A 155      28.968   9.672  16.082  1.00 47.48           H  
ATOM   2240  HB2 SER A 155      29.466   8.875  14.036  1.00 56.21           H  
ATOM   2241  HB3 SER A 155      27.963   8.431  13.757  1.00 56.21           H  
ATOM   2242  HG  SER A 155      28.744  10.963  13.928  1.00 64.09           H  
ATOM   2243  N   ALA A 156      26.978  11.192  16.173  1.00 38.73           N  
ANISOU 2243  N   ALA A 156     4520   2368   7827   -160  -1817   -672       N  
ATOM   2244  CA  ALA A 156      25.789  12.031  16.423  1.00 43.99           C  
ANISOU 2244  CA  ALA A 156     5046   3012   8657   -149  -1776   -615       C  
ATOM   2245  C   ALA A 156      24.944  12.091  15.159  1.00 48.29           C  
ANISOU 2245  C   ALA A 156     5398   3696   9255   -172  -1930   -581       C  
ATOM   2246  O   ALA A 156      23.770  12.405  15.278  1.00 48.50           O  
ANISOU 2246  O   ALA A 156     5246   3701   9481   -184  -1917   -532       O  
ATOM   2247  CB  ALA A 156      26.228  13.395  16.862  1.00 41.17           C  
ANISOU 2247  CB  ALA A 156     4729   2599   8315    -73  -1725   -528       C  
ATOM   2248  H   ALA A 156      27.757  11.666  16.214  1.00 46.79           H  
ATOM   2249  HA  ALA A 156      25.256  11.617  17.141  1.00 53.11           H  
ATOM   2250  HB1 ALA A 156      25.454  13.968  16.955  1.00 49.73           H  
ATOM   2251  HB2 ALA A 156      26.688  13.332  17.716  1.00 49.73           H  
ATOM   2252  HB3 ALA A 156      26.827  13.776  16.197  1.00 49.73           H  
ATOM   2253  N   ASP A 157      25.524  11.777  14.010  1.00 47.74           N  
ANISOU 2253  N   ASP A 157     5367   3760   9013   -175  -2073   -594       N  
ATOM   2254  CA  ASP A 157      24.815  11.753  12.712  1.00 45.97           C  
ANISOU 2254  CA  ASP A 157     5030   3675   8761   -217  -2266   -577       C  
ATOM   2255  C   ASP A 157      23.658  10.756  12.815  1.00 57.39           C  
ANISOU 2255  C   ASP A 157     6370   5088  10349   -338  -2325   -665       C  
ATOM   2256  O   ASP A 157      22.679  10.948  12.100  1.00 51.65           O  
ANISOU 2256  O   ASP A 157     5479   4449   9699   -390  -2516   -619       O  
ATOM   2257  CB  ASP A 157      25.809  11.452  11.588  1.00 44.80           C  
ANISOU 2257  CB  ASP A 157     5041   3638   8342   -206  -2346   -617       C  
ATOM   2258  CG  ASP A 157      25.287  11.569  10.171  1.00 58.78           C  
ANISOU 2258  CG  ASP A 157     6772   5568   9991   -237  -2569   -580       C  
ATOM   2259  OD1 ASP A 157      24.529  12.506   9.902  1.00 66.54           O  
ANISOU 2259  OD1 ASP A 157     7603   6613  11066   -191  -2659   -424       O  
ATOM   2260  OD2 ASP A 157      25.666  10.721   9.343  1.00 63.69           O  
ANISOU 2260  OD2 ASP A 157     7541   6242  10414   -302  -2653   -703       O  
ATOM   2261  H   ASP A 157      26.412  11.607  13.940  1.00 57.61           H  
ATOM   2262  HA  ASP A 157      24.431  12.642  12.560  1.00 55.48           H  
ATOM   2263  HB2 ASP A 157      26.571  12.060  11.671  1.00 54.08           H  
ATOM   2264  HB3 ASP A 157      26.140  10.538  11.706  1.00 54.08           H  
ATOM   2265  N   THR A 158      23.772   9.727  13.648  1.00 45.85           N  
ANISOU 2265  N   THR A 158     4988   3494   8941   -390  -2183   -772       N  
ATOM   2266  CA  THR A 158      22.701   8.730  13.863  1.00 52.05           C  
ANISOU 2266  CA  THR A 158     5651   4210   9916   -516  -2206   -841       C  
ATOM   2267  C   THR A 158      21.479   9.433  14.453  1.00 51.56           C  
ANISOU 2267  C   THR A 158     5335   4085  10169   -503  -2131   -717       C  
ATOM   2268  O   THR A 158      20.391   9.197  13.930  1.00 58.18           O  
ANISOU 2268  O   THR A 158     5945   4942  11219   -598  -2267   -693       O  
ATOM   2269  CB  THR A 158      23.218   7.554  14.707  1.00 64.23           C  
ANISOU 2269  CB  THR A 158     7354   5602  11450   -557  -2032   -954       C  
ATOM   2270  OG1 THR A 158      24.316   6.987  13.997  1.00 47.37           O  
ANISOU 2270  OG1 THR A 158     5426   3513   9060   -549  -2070  -1051       O  
ATOM   2271  CG2 THR A 158      22.170   6.494  14.967  1.00 54.06           C  
ANISOU 2271  CG2 THR A 158     5934   4250  10356   -679  -2006   -997       C  
ATOM   2272  H   THR A 158      24.521   9.549  14.132  1.00 55.34           H  
ATOM   2273  HA  THR A 158      22.448   8.377  12.980  1.00 62.78           H  
ATOM   2274  HB  THR A 158      23.536   7.904  15.571  1.00 77.40           H  
ATOM   2275  HG1 THR A 158      24.601   6.304  14.402  1.00 57.17           H  
ATOM   2276 HG21 THR A 158      22.565   5.763  15.475  1.00 65.19           H  
ATOM   2277 HG22 THR A 158      21.435   6.878  15.476  1.00 65.19           H  
ATOM   2278 HG23 THR A 158      21.834   6.153  14.119  1.00 65.19           H  
ATOM   2279  N   ALA A 159      21.653  10.296  15.445  1.00 46.95           N  
ANISOU 2279  N   ALA A 159     4789   3409   9639   -391  -1911   -637       N  
ATOM   2280  CA  ALA A 159      20.551  11.032  16.101  1.00 47.81           C  
ANISOU 2280  CA  ALA A 159     4688   3427  10051   -345  -1764   -515       C  
ATOM   2281  C   ALA A 159      20.258  12.362  15.390  1.00 47.30           C  
ANISOU 2281  C   ALA A 159     4456   3456  10059   -255  -1879   -364       C  
ATOM   2282  O   ALA A 159      19.264  12.983  15.754  1.00 48.51           O  
ANISOU 2282  O   ALA A 159     4389   3531  10513   -200  -1764   -238       O  
ATOM   2283  CB  ALA A 159      20.897  11.228  17.544  1.00 62.16           C  
ANISOU 2283  CB  ALA A 159     6691   5065  11864   -268  -1438   -519       C  
ATOM   2284  H   ALA A 159      22.471  10.518  15.780  1.00 56.65           H  
ATOM   2285  HA  ALA A 159      19.739  10.477  16.054  1.00 57.69           H  
ATOM   2286  HB1 ALA A 159      20.127  11.582  18.019  1.00 74.92           H  
ATOM   2287  HB2 ALA A 159      21.154  10.377  17.936  1.00 74.92           H  
ATOM   2288  HB3 ALA A 159      21.638  11.854  17.620  1.00 74.92           H  
ATOM   2289  N   ARG A 160      21.096  12.799  14.452  1.00 47.52           N  
ANISOU 2289  N   ARG A 160     4579   3634   9843   -225  -2074   -354       N  
ATOM   2290  CA  ARG A 160      20.966  14.104  13.746  1.00 55.45           C  
ANISOU 2290  CA  ARG A 160     5459   4716  10894   -126  -2170   -186       C  
ATOM   2291  C   ARG A 160      20.868  15.192  14.821  1.00 46.40           C  
ANISOU 2291  C   ARG A 160     4306   3400   9925     -3  -1895   -101       C  
ATOM   2292  O   ARG A 160      20.149  16.159  14.601  1.00 49.66           O  
ANISOU 2292  O   ARG A 160     4509   3785  10575     81  -1874     60       O  
ATOM   2293  CB  ARG A 160      19.820  14.086  12.729  1.00 51.57           C  
ANISOU 2293  CB  ARG A 160     4671   4332  10591   -177  -2423    -74       C  
ATOM   2294  CG  ARG A 160      20.085  13.225  11.506  1.00 59.20           C  
ANISOU 2294  CG  ARG A 160     5722   5473  11299   -298  -2740   -165       C  
ATOM   2295  CD  ARG A 160      18.854  13.100  10.634  1.00 61.98           C  
ANISOU 2295  CD  ARG A 160     5789   5918  11841   -390  -3050    -68       C  
ATOM   2296  NE  ARG A 160      18.346  14.403  10.224  1.00 80.93           N  
ANISOU 2296  NE  ARG A 160     7961   8364  14425   -270  -3129    184       N  
ATOM   2297  CZ  ARG A 160      18.769  15.130   9.189  1.00 78.68           C  
ANISOU 2297  CZ  ARG A 160     7749   8232  13913   -206  -3329    302       C  
ATOM   2298  NH1 ARG A 160      19.743  14.712   8.395  1.00 69.08           N  
ANISOU 2298  NH1 ARG A 160     6839   7140  12268   -249  -3445    182       N  
ATOM   2299  NH2 ARG A 160      18.200  16.300   8.948  1.00 71.42           N  
ANISOU 2299  NH2 ARG A 160     6603   7326  13206    -87  -3383    556       N  
ATOM   2300  H   ARG A 160      21.810  12.313  14.172  1.00 57.34           H  
ATOM   2301  HA  ARG A 160      21.802  14.250  13.250  1.00 66.86           H  
ATOM   2302  HB2 ARG A 160      19.009  13.765  13.174  1.00 62.20           H  
ATOM   2303  HB3 ARG A 160      19.654  15.005  12.431  1.00 62.20           H  
ATOM   2304  HG2 ARG A 160      20.814  13.618  10.981  1.00 71.36           H  
ATOM   2305  HG3 ARG A 160      20.364  12.331  11.794  1.00 71.36           H  
ATOM   2306  HD2 ARG A 160      19.061  12.557   9.847  1.00 74.69           H  
ATOM   2307  HD3 ARG A 160      18.156  12.633  11.140  1.00 74.69           H  
ATOM   2308  HE  ARG A 160      17.699  14.738  10.703  1.00 97.43           H  
ATOM   2309 HH11 ARG A 160      20.145  13.949   8.530  1.00 83.21           H  
ATOM   2310 HH12 ARG A 160      20.002  15.217   7.725  1.00 83.21           H  
ATOM   2311 HH21 ARG A 160      17.549  16.590   9.466  1.00 86.02           H  
ATOM   2312 HH22 ARG A 160      18.469  16.791   8.271  1.00 86.02           H  
ATOM   2313  N   ALA A 161      21.529  15.013  15.952  1.00 45.69           N  
ANISOU 2313  N   ALA A 161     4467   3181   9710      8  -1685   -210       N  
ATOM   2314  CA  ALA A 161      21.541  15.947  17.081  1.00 44.74           C  
ANISOU 2314  CA  ALA A 161     4453   2869   9677    100  -1413   -185       C  
ATOM   2315  C   ALA A 161      22.928  15.844  17.716  1.00 49.36           C  
ANISOU 2315  C   ALA A 161     5370   3405   9981     82  -1375   -301       C  
ATOM   2316  O   ALA A 161      23.324  14.707  17.997  1.00 41.90           O  
ANISOU 2316  O   ALA A 161     4549   2474   8896      6  -1395   -408       O  
ATOM   2317  CB  ALA A 161      20.466  15.560  18.041  1.00 52.49           C  
ANISOU 2317  CB  ALA A 161     5351   3685  10909    104  -1146   -185       C  
ATOM   2318  H   ALA A 161      22.050  14.282  16.112  1.00 55.14           H  
ATOM   2319  HA  ALA A 161      21.392  16.867  16.758  1.00 52.60           H  
ATOM   2320  HB1 ALA A 161      20.508  16.135  18.824  1.00 63.31           H  
ATOM   2321  HB2 ALA A 161      19.598  15.657  17.615  1.00 63.31           H  
ATOM   2322  HB3 ALA A 161      20.590  14.634  18.314  1.00 63.31           H  
ATOM   2323  N   TYR A 162      23.609  16.956  17.994  1.00 42.38           N  
ANISOU 2323  N   TYR A 162     4612   2449   9042    145  -1336   -269       N  
ATOM   2324  CA  TYR A 162      24.998  16.939  18.511  1.00 46.92           C  
ANISOU 2324  CA  TYR A 162     5451   3036   9342    109  -1362   -346       C  
ATOM   2325  C   TYR A 162      25.026  16.993  20.031  1.00 41.38           C  
ANISOU 2325  C   TYR A 162     5006   2238   8480    100  -1123   -419       C  
ATOM   2326  O   TYR A 162      24.075  17.466  20.623  1.00 43.09           O  
ANISOU 2326  O   TYR A 162     5235   2313   8823    152   -898   -407       O  
ATOM   2327  CB  TYR A 162      25.840  18.058  17.902  1.00 46.41           C  
ANISOU 2327  CB  TYR A 162     5392   3000   9241    147  -1460   -266       C  
ATOM   2328  CG  TYR A 162      26.131  17.933  16.434  1.00 47.92           C  
ANISOU 2328  CG  TYR A 162     5428   3341   9438    154  -1678   -184       C  
ATOM   2329  CD1 TYR A 162      26.991  16.959  15.970  1.00 39.50           C  
ANISOU 2329  CD1 TYR A 162     4423   2391   8195    101  -1796   -235       C  
ATOM   2330  CD2 TYR A 162      25.586  18.810  15.517  1.00 41.35           C  
ANISOU 2330  CD2 TYR A 162     4405   2576   8731    224  -1730    -37       C  
ATOM   2331  CE1 TYR A 162      27.285  16.844  14.627  1.00 42.11           C  
ANISOU 2331  CE1 TYR A 162     4664   2893   8442    115  -1931   -165       C  
ATOM   2332  CE2 TYR A 162      25.871  18.708  14.170  1.00 52.08           C  
ANISOU 2332  CE2 TYR A 162     5676   4124   9989    230  -1906     50       C  
ATOM   2333  CZ  TYR A 162      26.727  17.721  13.725  1.00 44.21           C  
ANISOU 2333  CZ  TYR A 162     4780   3234   8782    174  -1991    -26       C  
ATOM   2334  OH  TYR A 162      27.029  17.584  12.410  1.00 46.94           O  
ANISOU 2334  OH  TYR A 162     5095   3752   8990    189  -2121     51       O  
ATOM   2335  H   TYR A 162      23.271  17.795  17.910  1.00 49.65           H  
ATOM   2336  HA  TYR A 162      25.408  16.082  18.240  1.00 56.63           H  
ATOM   2337  HB2 TYR A 162      25.383  18.908  18.062  1.00 56.01           H  
ATOM   2338  HB3 TYR A 162      26.691  18.091  18.384  1.00 56.01           H  
ATOM   2339  HD1 TYR A 162      27.371  16.352  16.576  1.00 47.72           H  
ATOM   2340  HD2 TYR A 162      25.007  19.489  15.812  1.00 48.03           H  
ATOM   2341  HE1 TYR A 162      27.858  16.170  14.325  1.00 50.85           H  
ATOM   2342  HE2 TYR A 162      25.483  19.309  13.557  1.00 62.82           H  
ATOM   2343  HH  TYR A 162      27.310  18.330  12.103  1.00 56.65           H  
ATOM   2344  N   LYS A 163      26.079  16.466  20.635  1.00 44.10           N  
ANISOU 2344  N   LYS A 163     5568   2637   8553     42  -1173   -481       N  
ATOM   2345  CA  LYS A 163      26.305  16.572  22.087  1.00 41.19           C  
ANISOU 2345  CA  LYS A 163     5514   2150   7988     24  -1019   -540       C  
ATOM   2346  C   LYS A 163      26.503  18.063  22.394  1.00 43.92           C  
ANISOU 2346  C   LYS A 163     5965   2391   8333     57   -956   -528       C  
ATOM   2347  O   LYS A 163      27.058  18.752  21.535  1.00 41.68           O  
ANISOU 2347  O   LYS A 163     5542   2175   8120     69  -1095   -466       O  
ATOM   2348  CB  LYS A 163      27.561  15.795  22.479  1.00 55.36           C  
ANISOU 2348  CB  LYS A 163     7472   4021   9541    -44  -1160   -569       C  
ATOM   2349  CG  LYS A 163      27.521  14.287  22.270  1.00 50.85           C  
ANISOU 2349  CG  LYS A 163     6853   3514   8954    -71  -1177   -586       C  
ATOM   2350  CD  LYS A 163      28.826  13.670  21.833  1.00 44.37           C  
ANISOU 2350  CD  LYS A 163     6002   2823   8033   -100  -1380   -561       C  
ATOM   2351  CE  LYS A 163      29.959  13.903  22.803  1.00 46.93           C  
ANISOU 2351  CE  LYS A 163     6542   3106   8183   -135  -1466   -551       C  
ATOM   2352  NZ  LYS A 163      31.250  13.419  22.266  1.00 50.54           N  
ANISOU 2352  NZ  LYS A 163     6900   3664   8638   -143  -1668   -492       N  
ATOM   2353  H   LYS A 163      26.715  16.007  20.192  1.00 53.24           H  
ATOM   2354  HA  LYS A 163      25.528  16.214  22.565  1.00 47.84           H  
ATOM   2355  HB2 LYS A 163      28.314  16.158  21.971  1.00 66.75           H  
ATOM   2356  HB3 LYS A 163      27.741  15.965  23.426  1.00 66.75           H  
ATOM   2357  HG2 LYS A 163      27.231  13.863  23.106  1.00 61.34           H  
ATOM   2358  HG3 LYS A 163      26.854  14.090  21.593  1.00 61.34           H  
ATOM   2359  HD2 LYS A 163      28.698  12.703  21.727  1.00 53.56           H  
ATOM   2360  HD3 LYS A 163      29.077  14.035  20.960  1.00 53.56           H  
ATOM   2361  HE2 LYS A 163      30.039  14.855  22.991  1.00 56.63           H  
ATOM   2362  HE3 LYS A 163      29.770  13.441  23.642  1.00 56.63           H  
ATOM   2363  HZ1 LYS A 163      31.901  13.541  22.882  1.00 60.96           H  
ATOM   2364  HZ2 LYS A 163      31.191  12.536  22.077  1.00 60.96           H  
ATOM   2365  HZ3 LYS A 163      31.463  13.874  21.510  1.00 60.96           H  
ATOM   2366  N   PRO A 164      26.020  18.621  23.519  1.00 44.80           N  
ANISOU 2366  N   PRO A 164     6355   2308   8361     72   -730   -590       N  
ATOM   2367  CA  PRO A 164      25.641  17.877  24.715  1.00 46.51           C  
ANISOU 2367  CA  PRO A 164     6829   2392   8449     58   -544   -660       C  
ATOM   2368  C   PRO A 164      24.156  17.483  24.792  1.00 52.83           C  
ANISOU 2368  C   PRO A 164     7486   3100   9489    134   -284   -631       C  
ATOM   2369  O   PRO A 164      23.689  17.257  25.874  1.00 47.79           O  
ANISOU 2369  O   PRO A 164     7100   2286   8773    153    -40   -677       O  
ATOM   2370  CB  PRO A 164      26.077  18.868  25.796  1.00 46.77           C  
ANISOU 2370  CB  PRO A 164     7276   2219   8275     39   -430   -745       C  
ATOM   2371  CG  PRO A 164      25.678  20.204  25.237  1.00 47.41           C  
ANISOU 2371  CG  PRO A 164     7235   2256   8521    104   -386   -705       C  
ATOM   2372  CD  PRO A 164      25.903  20.062  23.748  1.00 51.54           C  
ANISOU 2372  CD  PRO A 164     7333   3017   9231    108   -627   -596       C  
ATOM   2373  HA  PRO A 164      26.202  17.066  24.787  1.00 56.13           H  
ATOM   2374  HB2 PRO A 164      25.624  18.694  26.646  1.00 54.53           H  
ATOM   2375  HB3 PRO A 164      27.047  18.826  25.938  1.00 54.53           H  
ATOM   2376  HG2 PRO A 164      24.739  20.399  25.431  1.00 55.30           H  
ATOM   2377  HG3 PRO A 164      26.235  20.918  25.608  1.00 55.30           H  
ATOM   2378  HD2 PRO A 164      25.152  20.431  23.247  1.00 62.16           H  
ATOM   2379  HD3 PRO A 164      26.718  20.524  23.478  1.00 62.16           H  
ATOM   2380  N   SER A 165      23.449  17.410  23.662  1.00 45.65           N  
ANISOU 2380  N   SER A 165     6168   2293   8883    172   -339   -545       N  
ATOM   2381  CA  SER A 165      22.022  17.000  23.605  1.00 51.92           C  
ANISOU 2381  CA  SER A 165     6724   3012   9992    223   -120   -489       C  
ATOM   2382  C   SER A 165      21.823  15.607  24.218  1.00 57.92           C  
ANISOU 2382  C   SER A 165     7583   3741  10682    165    -24   -531       C  
ATOM   2383  O   SER A 165      22.690  14.749  24.006  1.00 51.24           O  
ANISOU 2383  O   SER A 165     6834   3006   9628     84   -228   -577       O  
ATOM   2384  CB  SER A 165      21.515  16.973  22.197  1.00 56.39           C  
ANISOU 2384  CB  SER A 165     6840   3697  10889    234   -320   -387       C  
ATOM   2385  OG  SER A 165      20.167  16.541  22.145  1.00 69.64           O  
ANISOU 2385  OG  SER A 165     8242   5306  12912    245   -181   -324       O  
ATOM   2386  H   SER A 165      23.765  17.675  22.853  1.00 53.18           H  
ATOM   2387  HA  SER A 165      21.497  17.663  24.121  1.00 62.63           H  
ATOM   2388  HB2 SER A 165      21.586  17.870  21.806  1.00 67.99           H  
ATOM   2389  HB3 SER A 165      22.066  16.359  21.664  1.00 67.99           H  
ATOM   2390  HG  SER A 165      19.964  16.402  21.336  1.00 83.88           H  
ATOM   2391  N   PRO A 166      20.716  15.329  24.942  1.00 58.94           N  
ANISOU 2391  N   PRO A 166     9252   4483   8660    367   1478    117       N  
ATOM   2392  CA  PRO A 166      20.479  13.993  25.482  1.00 59.35           C  
ANISOU 2392  CA  PRO A 166     9373   4430   8749    120   1614     34       C  
ATOM   2393  C   PRO A 166      20.390  12.919  24.391  1.00 54.75           C  
ANISOU 2393  C   PRO A 166     8521   4006   8277    -21   1554   -103       C  
ATOM   2394  O   PRO A 166      20.872  11.854  24.615  1.00 61.95           O  
ANISOU 2394  O   PRO A 166     9578   4734   9227   -205   1571   -138       O  
ATOM   2395  CB  PRO A 166      19.160  14.118  26.233  1.00 55.87           C  
ANISOU 2395  CB  PRO A 166     8870   4056   8301     91   1897    -17       C  
ATOM   2396  CG  PRO A 166      18.503  15.323  25.620  1.00 64.74           C  
ANISOU 2396  CG  PRO A 166     9721   5442   9435    334   1874    -23       C  
ATOM   2397  CD  PRO A 166      19.651  16.256  25.323  1.00 49.29           C  
ANISOU 2397  CD  PRO A 166     7922   3388   7418    518   1633    108       C  
ATOM   2398  HA  PRO A 166      21.200  13.765  26.122  1.00 71.54           H  
ATOM   2399  HB2 PRO A 166      18.607  13.317  26.108  1.00 67.36           H  
ATOM   2400  HB3 PRO A 166      19.313  14.253  27.192  1.00 67.36           H  
ATOM   2401  HG2 PRO A 166      18.033  15.084  24.797  1.00 78.01           H  
ATOM   2402  HG3 PRO A 166      17.870  15.733  26.243  1.00 78.01           H  
ATOM   2403  HD2 PRO A 166      19.424  16.866  24.598  1.00 59.47           H  
ATOM   2404  HD3 PRO A 166      19.901  16.772  26.112  1.00 59.47           H  
ATOM   2405  N   ALA A 167      19.827  13.231  23.236  1.00 56.63           N  
ANISOU 2405  N   ALA A 167     8394   4570   8551     74   1474   -186       N  
ATOM   2406  CA  ALA A 167      19.661  12.271  22.130  1.00 53.16           C  
ANISOU 2406  CA  ALA A 167     7707   4303   8188    -55   1394   -352       C  
ATOM   2407  C   ALA A 167      21.030  11.751  21.686  1.00 56.13           C  
ANISOU 2407  C   ALA A 167     8255   4527   8547    -60   1219   -317       C  
ATOM   2408  O   ALA A 167      21.121  10.558  21.371  1.00 51.66           O  
ANISOU 2408  O   ALA A 167     7650   3931   8049   -223   1202   -456       O  
ATOM   2409  CB  ALA A 167      18.938  12.938  21.007  1.00 49.95           C  
ANISOU 2409  CB  ALA A 167     6902   4306   7772    100   1299   -435       C  
ATOM   2410  H   ALA A 167      19.519  14.063  23.034  1.00 68.27           H  
ATOM   2411  HA  ALA A 167      19.123  11.509  22.452  1.00 64.11           H  
ATOM   2412  HB1 ALA A 167      18.819  12.306  20.279  1.00 58.35           H  
ATOM   2413  HB2 ALA A 167      18.067  13.243  21.314  1.00 58.35           H  
ATOM   2414  HB3 ALA A 167      19.455  13.698  20.691  1.00 58.35           H  
ATOM   2415  N   ALA A 168      22.050  12.602  21.644  1.00 49.68           N  
ANISOU 2415  N   ALA A 168     7617   3603   7655    111   1097   -145       N  
ATOM   2416  CA  ALA A 168      23.422  12.214  21.252  1.00 43.91           C  
ANISOU 2416  CA  ALA A 168     7014   2743   6928    116    948   -109       C  
ATOM   2417  C   ALA A 168      23.986  11.223  22.264  1.00 45.55           C  
ANISOU 2417  C   ALA A 168     7514   2615   7176    -30    991   -101       C  
ATOM   2418  O   ALA A 168      24.618  10.267  21.835  1.00 44.01           O  
ANISOU 2418  O   ALA A 168     7349   2337   7037    -95    931   -175       O  
ATOM   2419  CB  ALA A 168      24.298  13.425  21.128  1.00 45.04           C  
ANISOU 2419  CB  ALA A 168     7245   2857   7010    302    827     70       C  
ATOM   2420  H   ALA A 168      21.984  13.481  21.875  1.00 59.93           H  
ATOM   2421  HA  ALA A 168      23.378  11.767  20.372  1.00 51.51           H  
ATOM   2422  HB1 ALA A 168      25.097  13.190  20.629  1.00 54.36           H  
ATOM   2423  HB2 ALA A 168      23.823  14.129  20.655  1.00 54.36           H  
ATOM   2424  HB3 ALA A 168      24.545  13.743  22.013  1.00 54.36           H  
ATOM   2425  N   TYR A 169      23.773  11.456  23.546  1.00 46.98           N  
ANISOU 2425  N   TYR A 169     7935   2600   7317    -61   1100    -11       N  
ATOM   2426  CA  TYR A 169      24.216  10.535  24.616  1.00 48.99           C  
ANISOU 2426  CA  TYR A 169     8407   2687   7520   -162   1062     30       C  
ATOM   2427  C   TYR A 169      23.418   9.222  24.554  1.00 51.21           C  
ANISOU 2427  C   TYR A 169     8698   2863   7897   -377   1252    -99       C  
ATOM   2428  O   TYR A 169      24.026   8.193  24.631  1.00 53.86           O  
ANISOU 2428  O   TYR A 169     9125   3137   8204   -434   1158    -82       O  
ATOM   2429  CB  TYR A 169      24.183  11.239  25.971  1.00 45.00           C  
ANISOU 2429  CB  TYR A 169     8060   2179   6860   -119   1061    150       C  
ATOM   2430  CG  TYR A 169      25.179  12.360  26.130  1.00 55.11           C  
ANISOU 2430  CG  TYR A 169     9326   3546   8066     35    835    251       C  
ATOM   2431  CD1 TYR A 169      26.542  12.131  26.039  1.00 46.57           C  
ANISOU 2431  CD1 TYR A 169     8191   2496   7007     74    585    292       C  
ATOM   2432  CD2 TYR A 169      24.760  13.653  26.386  1.00 43.51           C  
ANISOU 2432  CD2 TYR A 169     7882   2106   6543    133    899    290       C  
ATOM   2433  CE1 TYR A 169      27.460  13.155  26.184  1.00 59.70           C  
ANISOU 2433  CE1 TYR A 169     9806   4218   8661    161    421    362       C  
ATOM   2434  CE2 TYR A 169      25.665  14.686  26.536  1.00 57.98           C  
ANISOU 2434  CE2 TYR A 169     9695   3996   8337    229    704    361       C  
ATOM   2435  CZ  TYR A 169      27.019  14.438  26.441  1.00 55.19           C  
ANISOU 2435  CZ  TYR A 169     9268   3672   8029    221    475    393       C  
ATOM   2436  OH  TYR A 169      27.896  15.467  26.587  1.00 48.22           O  
ANISOU 2436  OH  TYR A 169     8344   2817   7160    273    330    447       O  
ATOM   2437  H   TYR A 169      23.309  12.174  23.860  1.00 56.70           H  
ATOM   2438  HA  TYR A 169      25.151  10.306  24.433  1.00 59.10           H  
ATOM   2439  HB2 TYR A 169      23.281  11.594  26.114  1.00 52.41           H  
ATOM   2440  HB3 TYR A 169      24.347  10.572  26.666  1.00 52.41           H  
ATOM   2441  HD1 TYR A 169      26.854  11.258  25.865  1.00 56.20           H  
ATOM   2442  HD2 TYR A 169      23.839  13.836  26.460  1.00 51.72           H  
ATOM   2443  HE1 TYR A 169      28.385  12.979  26.115  1.00 71.96           H  
ATOM   2444  HE2 TYR A 169      25.363  15.557  26.715  1.00 69.89           H  
ATOM   2445  HH  TYR A 169      28.305  15.406  27.337  1.00 58.18           H  
ATOM   2446  N   ALA A 170      22.134   9.241  24.240  1.00 51.08           N  
ANISOU 2446  N   ALA A 170     8465   2971   7971   -486   1449   -233       N  
ATOM   2447  CA  ALA A 170      21.265   8.045  24.272  1.00 50.37           C  
ANISOU 2447  CA  ALA A 170     8331   2814   7992   -749   1636   -374       C  
ATOM   2448  C   ALA A 170      21.808   6.955  23.351  1.00 58.25           C  
ANISOU 2448  C   ALA A 170     9278   3764   9092   -833   1525   -520       C  
ATOM   2449  O   ALA A 170      21.575   5.789  23.657  1.00 53.64           O  
ANISOU 2449  O   ALA A 170     8811   2964   8606  -1053   1655   -604       O  
ATOM   2450  CB  ALA A 170      19.856   8.396  23.897  1.00 55.57           C  
ANISOU 2450  CB  ALA A 170     8617   3786   8712   -832   1787   -509       C  
ATOM   2451  H   ALA A 170      21.690   9.993  23.983  1.00 61.61           H  
ATOM   2452  HA  ALA A 170      21.264   7.699  25.185  1.00 58.85           H  
ATOM   2453  HB1 ALA A 170      19.297   7.603  23.956  1.00 67.00           H  
ATOM   2454  HB2 ALA A 170      19.516   9.075  24.504  1.00 67.00           H  
ATOM   2455  HB3 ALA A 170      19.834   8.737  22.987  1.00 67.00           H  
ATOM   2456  N   LEU A 171      22.520   7.320  22.294  1.00 50.69           N  
ANISOU 2456  N   LEU A 171     8163   2989   8109   -665   1309   -555       N  
ATOM   2457  CA  LEU A 171      23.115   6.338  21.370  1.00 49.50           C  
ANISOU 2457  CA  LEU A 171     7999   2781   8029   -705   1209   -701       C  
ATOM   2458  C   LEU A 171      24.015   5.407  22.188  1.00 57.11           C  
ANISOU 2458  C   LEU A 171     9291   3423   8986   -718   1175   -596       C  
ATOM   2459  O   LEU A 171      23.988   4.202  21.923  1.00 52.91           O  
ANISOU 2459  O   LEU A 171     8787   2793   8522   -831   1174   -717       O  
ATOM   2460  CB  LEU A 171      23.927   7.063  20.296  1.00 47.76           C  
ANISOU 2460  CB  LEU A 171     7620   2794   7733   -478   1002   -691       C  
ATOM   2461  CG  LEU A 171      23.181   7.979  19.327  1.00 52.92           C  
ANISOU 2461  CG  LEU A 171     7918   3874   8317   -395    948   -764       C  
ATOM   2462  CD1 LEU A 171      24.165   8.689  18.411  1.00 46.22           C  
ANISOU 2462  CD1 LEU A 171     7011   3186   7366   -163    782   -679       C  
ATOM   2463  CD2 LEU A 171      22.152   7.220  18.507  1.00 50.18           C  
ANISOU 2463  CD2 LEU A 171     7318   3716   8034   -573    975  -1048       C  
ATOM   2464  H   LEU A 171      22.681   8.188  22.083  1.00 61.15           H  
ATOM   2465  HA  LEU A 171      22.396   5.809  20.955  1.00 57.81           H  
ATOM   2466  HB2 LEU A 171      24.613   7.595  20.747  1.00 55.72           H  
ATOM   2467  HB3 LEU A 171      24.397   6.385  19.769  1.00 55.72           H  
ATOM   2468  HG  LEU A 171      22.706   8.669  19.851  1.00 63.83           H  
ATOM   2469 HD11 LEU A 171      23.680   9.263  17.792  1.00 53.87           H  
ATOM   2470 HD12 LEU A 171      24.773   9.231  18.943  1.00 53.87           H  
ATOM   2471 HD13 LEU A 171      24.675   8.030  17.909  1.00 53.87           H  
ATOM   2472 HD21 LEU A 171      21.789   7.805  17.820  1.00 58.63           H  
ATOM   2473 HD22 LEU A 171      22.574   6.452  18.086  1.00 58.63           H  
ATOM   2474 HD23 LEU A 171      21.432   6.917  19.085  1.00 58.63           H  
ATOM   2475  N   GLY A 172      24.786   5.937  23.131  1.00 51.81           N  
ANISOU 2475  N   GLY A 172     8756   2764   8164   -562   1046   -357       N  
ATOM   2476  CA  GLY A 172      25.672   5.146  24.000  1.00 52.52           C  
ANISOU 2476  CA  GLY A 172     9001   2754   8198   -505    899   -240       C  
ATOM   2477  C   GLY A 172      24.928   4.210  24.931  1.00 61.86           C  
ANISOU 2477  C   GLY A 172    10334   3791   9378   -683   1068   -222       C  
ATOM   2478  O   GLY A 172      25.375   3.061  25.065  1.00 59.42           O  
ANISOU 2478  O   GLY A 172    10122   3339   9116   -712   1028   -234       O  
ATOM   2479  H   GLY A 172      24.817   6.834  23.286  1.00 62.49           H  
ATOM   2480  HA2 GLY A 172      26.284   4.616  23.434  1.00 63.34           H  
ATOM   2481  HA3 GLY A 172      26.223   5.765  24.533  1.00 63.34           H  
ATOM   2482  N   THR A 173      23.848   4.666  25.567  1.00 55.48           N  
ANISOU 2482  N   THR A 173     9561   2997   8523   -796   1285   -188       N  
ATOM   2483  CA  THR A 173      23.021   3.823  26.467  1.00 63.16           C  
ANISOU 2483  CA  THR A 173    10683   3823   9493   -991   1508   -167       C  
ATOM   2484  C   THR A 173      22.347   2.730  25.625  1.00 66.57           C  
ANISOU 2484  C   THR A 173    11007   4172  10115  -1234   1648   -378       C  
ATOM   2485  O   THR A 173      22.288   1.585  26.083  1.00 60.32           O  
ANISOU 2485  O   THR A 173    10358   3209   9352  -1354   1720   -363       O  
ATOM   2486  CB  THR A 173      22.034   4.636  27.310  1.00 56.10           C  
ANISOU 2486  CB  THR A 173     9828   2961   8527  -1072   1768   -114       C  
ATOM   2487  OG1 THR A 173      21.380   5.588  26.476  1.00 66.45           O  
ANISOU 2487  OG1 THR A 173    10898   4392   9957  -1109   1871   -252       O  
ATOM   2488  CG2 THR A 173      22.701   5.311  28.486  1.00 61.89           C  
ANISOU 2488  CG2 THR A 173    10750   3725   9039   -865   1644     83       C  
ATOM   2489  H   THR A 173      23.523   5.511  25.472  1.00 66.90           H  
ATOM   2490  HA  THR A 173      23.640   3.377  27.088  1.00 76.11           H  
ATOM   2491  HB  THR A 173      21.353   4.013  27.659  1.00 65.73           H  
ATOM   2492  HG1 THR A 173      20.881   5.194  25.917  1.00 80.05           H  
ATOM   2493 HG21 THR A 173      22.044   5.836  28.977  1.00 74.58           H  
ATOM   2494 HG22 THR A 173      23.079   4.635  29.076  1.00 74.58           H  
ATOM   2495 HG23 THR A 173      23.411   5.894  28.167  1.00 74.58           H  
ATOM   2496  N   ALA A 174      21.888   3.065  24.426  1.00 57.06           N  
ANISOU 2496  N   ALA A 174     9547   3081   9053  -1318   1690   -593       N  
ATOM   2497  CA  ALA A 174      21.225   2.103  23.534  1.00 60.44           C  
ANISOU 2497  CA  ALA A 174     9825   3466   9673  -1567   1782   -858       C  
ATOM   2498  C   ALA A 174      22.222   1.003  23.185  1.00 60.00           C  
ANISOU 2498  C   ALA A 174     9902   3280   9614  -1477   1583   -873       C  
ATOM   2499  O   ALA A 174      21.824  -0.163  23.197  1.00 63.82           O  
ANISOU 2499  O   ALA A 174    10427   3619  10202  -1670   1663   -987       O  
ATOM   2500  CB  ALA A 174      20.724   2.806  22.301  1.00 60.63           C  
ANISOU 2500  CB  ALA A 174     9517   3670   9848  -1637   1801  -1130       C  
ATOM   2501  H   ALA A 174      21.985   3.888  24.055  1.00 66.88           H  
ATOM   2502  HA  ALA A 174      20.461   1.701  24.010  1.00 72.85           H  
ATOM   2503  HB1 ALA A 174      20.270   2.168  21.726  1.00 73.07           H  
ATOM   2504  HB2 ALA A 174      20.103   3.509  22.555  1.00 73.07           H  
ATOM   2505  HB3 ALA A 174      21.472   3.196  21.818  1.00 73.07           H  
ATOM   2506  N   ALA A 175      23.462   1.358  22.891  1.00 57.56           N  
ANISOU 2506  N   ALA A 175     9653   3008   9209  -1188   1335   -764       N  
ATOM   2507  CA  ALA A 175      24.512   0.407  22.485  1.00 69.00           C  
ANISOU 2507  CA  ALA A 175    11184   4341  10693  -1078   1162   -815       C  
ATOM   2508  C   ALA A 175      24.999  -0.501  23.615  1.00 68.24           C  
ANISOU 2508  C   ALA A 175    11333   4031  10565  -1025   1118   -628       C  
ATOM   2509  O   ALA A 175      25.259  -1.669  23.291  1.00 62.18           O  
ANISOU 2509  O   ALA A 175    10655   3085   9886  -1037   1076   -709       O  
ATOM   2510  CB  ALA A 175      25.657   1.161  21.864  1.00 60.68           C  
ANISOU 2510  CB  ALA A 175    10058   3412   9587   -805    950   -789       C  
ATOM   2511  H   ALA A 175      23.764   2.216  22.941  1.00 67.99           H  
ATOM   2512  HA  ALA A 175      24.128  -0.175  21.787  1.00 83.12           H  
ATOM   2513  HB1 ALA A 175      26.359   0.538  21.613  1.00 73.14           H  
ATOM   2514  HB2 ALA A 175      25.348   1.633  21.073  1.00 73.14           H  
ATOM   2515  HB3 ALA A 175      26.014   1.802  22.503  1.00 73.14           H  
ATOM   2516  N   PHE A 176      25.157  -0.015  24.853  1.00 59.75           N  
ANISOU 2516  N   PHE A 176    10379   2956   9366   -964   1139   -397       N  
ATOM   2517  CA  PHE A 176      25.822  -0.790  25.934  1.00 61.33           C  
ANISOU 2517  CA  PHE A 176    10805   2970   9530   -861   1068   -221       C  
ATOM   2518  C   PHE A 176      25.001  -1.074  27.209  1.00 63.77           C  
ANISOU 2518  C   PHE A 176    11321   3159   9750  -1010   1290    -81       C  
ATOM   2519  O   PHE A 176      25.341  -2.080  27.844  1.00 85.11           O  
ANISOU 2519  O   PHE A 176    14243   5638  12457  -1012   1316     13       O  
ATOM   2520  CB  PHE A 176      27.144  -0.090  26.255  1.00 59.04           C  
ANISOU 2520  CB  PHE A 176    10496   2776   9159   -578    830    -72       C  
ATOM   2521  CG  PHE A 176      28.162  -0.095  25.144  1.00 57.63           C  
ANISOU 2521  CG  PHE A 176    10167   2646   9086   -406    631   -176       C  
ATOM   2522  CD1 PHE A 176      28.926  -1.223  24.893  1.00 59.60           C  
ANISOU 2522  CD1 PHE A 176    10488   2705   9453   -320    553   -222       C  
ATOM   2523  CD2 PHE A 176      28.377   1.028  24.361  1.00 62.36           C  
ANISOU 2523  CD2 PHE A 176    10571   3459   9664   -322    549   -225       C  
ATOM   2524  CE1 PHE A 176      29.869  -1.231  23.879  1.00 58.68           C  
ANISOU 2524  CE1 PHE A 176    10242   2624   9431   -151    411   -332       C  
ATOM   2525  CE2 PHE A 176      29.322   1.018  23.348  1.00 55.90           C  
ANISOU 2525  CE2 PHE A 176     9637   2674   8928   -167    412   -319       C  
ATOM   2526  CZ  PHE A 176      30.068  -0.111  23.111  1.00 55.80           C  
ANISOU 2526  CZ  PHE A 176     9689   2484   9030    -79    349   -380       C  
ATOM   2527  H   PHE A 176      24.908   0.825  25.108  1.00 72.01           H  
ATOM   2528  HA  PHE A 176      26.057  -1.672  25.562  1.00 72.01           H  
ATOM   2529  HB2 PHE A 176      26.948   0.838  26.499  1.00 70.73           H  
ATOM   2530  HB3 PHE A 176      27.535  -0.524  27.041  1.00 70.73           H  
ATOM   2531  HD1 PHE A 176      28.799  -1.996  25.419  1.00 69.93           H  
ATOM   2532  HD2 PHE A 176      27.869   1.809  24.517  1.00 75.15           H  
ATOM   2533  HE1 PHE A 176      30.380  -2.008  23.720  1.00 68.83           H  
ATOM   2534  HE2 PHE A 176      29.453   1.789  22.819  1.00 67.40           H  
ATOM   2535  HZ  PHE A 176      30.712  -0.119  22.422  1.00 66.65           H  
ATOM   2536  N   GLY A 177      24.073  -0.232  27.658  1.00 63.10           N  
ANISOU 2536  N   GLY A 177    11192   3202   9583  -1123   1471    -61       N  
ATOM   2537  CA  GLY A 177      23.212  -0.510  28.828  1.00 65.72           C  
ANISOU 2537  CA  GLY A 177    11738   3420   9812  -1260   1725     67       C  
ATOM   2538  C   GLY A 177      22.119   0.529  29.039  1.00 75.86           C  
ANISOU 2538  C   GLY A 177    12937   4850  11036  -1379   1960     50       C  
ATOM   2539  O   GLY A 177      22.368   1.692  28.729  1.00 73.35           O  
ANISOU 2539  O   GLY A 177    12489   4721  10661  -1240   1853     48       O  
ATOM   2540  H   GLY A 177      23.924   0.578  27.271  1.00 74.56           H  
ATOM   2541  HA2 GLY A 177      22.795  -1.400  28.712  1.00 77.27           H  
ATOM   2542  HA3 GLY A 177      23.781  -0.546  29.637  1.00 77.27           H  
ATOM   2543  N   SER A 178      20.989   0.169  29.644  1.00 78.93           N  
ANISOU 2543  N   SER A 178    13403   5138  11448  -1635   2304     43       N  
ATOM   2544  CA  SER A 178      19.843   1.086  29.892  1.00 78.61           C  
ANISOU 2544  CA  SER A 178    13228   5225  11416  -1777   2585    -13       C  
ATOM   2545  C   SER A 178      20.178   2.151  30.934  1.00 74.68           C  
ANISOU 2545  C   SER A 178    12908   4800  10667  -1570   2575    162       C  
ATOM   2546  O   SER A 178      19.711   3.275  30.745  1.00 83.53           O  
ANISOU 2546  O   SER A 178    13881   6072  11784  -1527   2632    116       O  
ATOM   2547  CB  SER A 178      18.582   0.346  30.250  1.00 79.86           C  
ANISOU 2547  CB  SER A 178    13395   5260  11686  -2123   2988    -70       C  
ATOM   2548  OG  SER A 178      18.010  -0.256  29.099  1.00102.54           O  
ANISOU 2548  OG  SER A 178    15975   8152  14835  -2371   3035   -319       O  
ATOM   2549  H   SER A 178      20.847  -0.666  29.976  1.00 95.03           H  
ATOM   2550  HA  SER A 178      19.668   1.564  29.036  1.00 94.65           H  
ATOM   2551  HB2 SER A 178      18.782  -0.345  30.921  1.00 96.14           H  
ATOM   2552  HB3 SER A 178      17.937   0.976  30.645  1.00 96.14           H  
ATOM   2553  HG  SER A 178      17.323  -0.691  29.333  1.00123.37           H  
ATOM   2554  N   ASN A 179      20.916   1.814  31.992  1.00 77.36           N  
ANISOU 2554  N   ASN A 179    13574   5022  10798  -1440   2509    351       N  
ATOM   2555  CA  ASN A 179      21.247   2.770  33.085  1.00 83.12           C  
ANISOU 2555  CA  ASN A 179    14502   5813  11267  -1266   2508    484       C  
ATOM   2556  C   ASN A 179      22.513   3.532  32.682  1.00 78.77           C  
ANISOU 2556  C   ASN A 179    13881   5394  10653   -983   2088    514       C  
ATOM   2557  O   ASN A 179      23.564   2.890  32.560  1.00 68.98           O  
ANISOU 2557  O   ASN A 179    12689   4095   9425   -863   1826    566       O  
ATOM   2558  CB  ASN A 179      21.437   2.106  34.452  1.00 70.75           C  
ANISOU 2558  CB  ASN A 179    13336   4063   9482  -1280   2670    652       C  
ATOM   2559  CG  ASN A 179      21.604   3.085  35.594  1.00 80.32           C  
ANISOU 2559  CG  ASN A 179    14796   5328  10394  -1097   2654    762       C  
ATOM   2560  OD1 ASN A 179      21.407   4.286  35.438  1.00 88.91           O  
ANISOU 2560  OD1 ASN A 179    15749   6568  11465  -1031   2654    699       O  
ATOM   2561  ND2 ASN A 179      21.958   2.573  36.759  1.00 97.37           N  
ANISOU 2561  ND2 ASN A 179    17343   7344  12310  -1024   2672    915       N  
ATOM   2562  H   ASN A 179      21.282   0.989  32.093  1.00 93.15           H  
ATOM   2563  HA  ASN A 179      20.499   3.394  33.170  1.00100.06           H  
ATOM   2564  HB2 ASN A 179      20.661   1.539  34.633  1.00 83.30           H  
ATOM   2565  HB3 ASN A 179      22.225   1.533  34.421  1.00 83.30           H  
ATOM   2566 HD21 ASN A 179      22.074   1.702  36.845  1.00117.17           H  
ATOM   2567 HD22 ASN A 179      22.076   3.104  37.455  1.00117.17           H  
ATOM   2568  N   PRO A 180      22.490   4.868  32.493  1.00 63.47           N  
ANISOU 2568  N   PRO A 180    11808   3626   8683   -880   2029    475       N  
ATOM   2569  CA  PRO A 180      23.685   5.562  32.077  1.00 65.07           C  
ANISOU 2569  CA  PRO A 180    11905   3958   8862   -649   1647    493       C  
ATOM   2570  C   PRO A 180      24.787   5.405  33.128  1.00 64.41           C  
ANISOU 2570  C   PRO A 180    12073   3817   8582   -490   1454    626       C  
ATOM   2571  O   PRO A 180      25.912   5.335  32.755  1.00 57.37           O  
ANISOU 2571  O   PRO A 180    11077   2973   7749   -347   1149    637       O  
ATOM   2572  CB  PRO A 180      23.225   7.005  31.831  1.00 62.07           C  
ANISOU 2572  CB  PRO A 180    11411   3719   8452   -593   1703    446       C  
ATOM   2573  CG  PRO A 180      21.924   7.141  32.563  1.00 67.73           C  
ANISOU 2573  CG  PRO A 180    12221   4365   9146   -761   2132    423       C  
ATOM   2574  CD  PRO A 180      21.324   5.756  32.520  1.00 72.58           C  
ANISOU 2574  CD  PRO A 180    12856   4844   9876   -986   2330    397       C  
ATOM   2575  HA  PRO A 180      23.996   5.180  31.219  1.00 78.41           H  
ATOM   2576  HB2 PRO A 180      23.882   7.639  32.172  1.00 74.80           H  
ATOM   2577  HB3 PRO A 180      23.101   7.171  30.873  1.00 74.80           H  
ATOM   2578  HG2 PRO A 180      22.071   7.429  33.486  1.00 81.59           H  
ATOM   2579  HG3 PRO A 180      21.340   7.788  32.117  1.00 81.59           H  
ATOM   2580  HD2 PRO A 180      20.772   5.598  33.307  1.00 87.41           H  
ATOM   2581  HD3 PRO A 180      20.779   5.636  31.721  1.00 87.41           H  
ATOM   2582  N   ARG A 181      24.436   5.273  34.401  1.00 63.71           N  
ANISOU 2582  N   ARG A 181    12323   3621   8261   -511   1645    722       N  
ATOM   2583  CA  ARG A 181      25.445   5.207  35.483  1.00 66.85           C  
ANISOU 2583  CA  ARG A 181    13009   3953   8437   -355   1462    839       C  
ATOM   2584  C   ARG A 181      26.361   4.020  35.224  1.00 65.44           C  
ANISOU 2584  C   ARG A 181    12852   3661   8352   -299   1274    895       C  
ATOM   2585  O   ARG A 181      27.493   4.035  35.699  1.00 72.61           O  
ANISOU 2585  O   ARG A 181    13930   4533   9127   -137   1054    976       O  
ATOM   2586  CB  ARG A 181      24.799   5.119  36.865  1.00 78.88           C  
ANISOU 2586  CB  ARG A 181    14956   5350   9666   -397   1746    930       C  
ATOM   2587  CG  ARG A 181      24.227   6.431  37.379  1.00 80.18           C  
ANISOU 2587  CG  ARG A 181    15223   5600   9641   -339   1835    898       C  
ATOM   2588  CD  ARG A 181      24.438   6.609  38.869  1.00 97.23           C  
ANISOU 2588  CD  ARG A 181    17884   7640  11417   -251   1897   1000       C  
ATOM   2589  NE  ARG A 181      25.839   6.832  39.219  1.00100.10           N  
ANISOU 2589  NE  ARG A 181    18369   8009  11655    -64   1498   1043       N  
ATOM   2590  CZ  ARG A 181      26.505   7.989  39.137  1.00 88.80           C  
ANISOU 2590  CZ  ARG A 181    16869   6690  10181     60   1235    979       C  
ATOM   2591  NH1 ARG A 181      25.926   9.097  38.694  1.00 86.77           N  
ANISOU 2591  NH1 ARG A 181    16437   6544   9989     39   1323    882       N  
ATOM   2592  NH2 ARG A 181      27.778   8.028  39.498  1.00 81.61           N  
ANISOU 2592  NH2 ARG A 181    16073   5764   9172    205    889   1011       N  
ATOM   2593  H   ARG A 181      23.571   5.234  34.681  1.00 76.77           H  
ATOM   2594  HA  ARG A 181      25.987   6.027  35.443  1.00 80.53           H  
ATOM   2595  HB2 ARG A 181      24.080   4.455  36.832  1.00 94.98           H  
ATOM   2596  HB3 ARG A 181      25.471   4.797  37.499  1.00 94.98           H  
ATOM   2597  HG2 ARG A 181      23.266   6.463  37.186  1.00 96.53           H  
ATOM   2598  HG3 ARG A 181      24.652   7.176  36.912  1.00 96.53           H  
ATOM   2599  HD2 ARG A 181      23.894   7.358  39.188  1.00116.99           H  
ATOM   2600  HD3 ARG A 181      24.124   5.801  39.329  1.00116.99           H  
ATOM   2601  HE  ARG A 181      26.280   6.144  39.518  1.00120.44           H  
ATOM   2602 HH11 ARG A 181      25.088   9.103  38.446  1.00104.45           H  
ATOM   2603 HH12 ARG A 181      26.391   9.841  38.649  1.00104.45           H  
ATOM   2604 HH21 ARG A 181      28.177   7.300  39.793  1.00 98.25           H  
ATOM   2605 HH22 ARG A 181      28.229   8.782  39.447  1.00 98.25           H  
ATOM   2606  N   GLY A 182      25.881   3.001  34.527  1.00 77.23           N  
ANISOU 2606  N   GLY A 182    14197   5079  10068   -425   1358    844       N  
ATOM   2607  CA  GLY A 182      26.695   1.824  34.186  1.00 69.27           C  
ANISOU 2607  CA  GLY A 182    13221   3928   9171   -364   1209    886       C  
ATOM   2608  C   GLY A 182      27.878   2.149  33.307  1.00 72.69           C  
ANISOU 2608  C   GLY A 182    13351   4463   9805   -226    908    812       C  
ATOM   2609  O   GLY A 182      28.928   1.531  33.536  1.00 70.23           O  
ANISOU 2609  O   GLY A 182    13081   4030   9572   -120    766    853       O  
ATOM   2610  H   GLY A 182      25.010   2.945  34.269  1.00 93.00           H  
ATOM   2611  HA2 GLY A 182      27.017   1.406  35.022  1.00 83.44           H  
ATOM   2612  HA3 GLY A 182      26.119   1.166  33.721  1.00 83.44           H  
ATOM   2613  N   ILE A 183      27.735   3.050  32.333  1.00 62.35           N  
ANISOU 2613  N   ILE A 183    11751   3357   8583   -216    832    709       N  
ATOM   2614  CA  ILE A 183      28.814   3.344  31.343  1.00 59.61           C  
ANISOU 2614  CA  ILE A 183    11113   3113   8422    -99    595    636       C  
ATOM   2615  C   ILE A 183      29.676   4.494  31.853  1.00 60.29           C  
ANISOU 2615  C   ILE A 183    11176   3327   8403     50    409    682       C  
ATOM   2616  O   ILE A 183      29.112   5.425  32.417  1.00 55.15           O  
ANISOU 2616  O   ILE A 183    10590   2763   7600     27    466    693       O  
ATOM   2617  CB  ILE A 183      28.228   3.614  29.950  1.00 64.93           C  
ANISOU 2617  CB  ILE A 183    11500   3903   9268   -201    651    484       C  
ATOM   2618  CG1 ILE A 183      27.347   2.461  29.456  1.00 63.59           C  
ANISOU 2618  CG1 ILE A 183    11363   3588   9208   -370    825    404       C  
ATOM   2619  CG2 ILE A 183      29.323   3.951  28.953  1.00 52.93           C  
ANISOU 2619  CG2 ILE A 183     9721   2489   7901    -69    437    422       C  
ATOM   2620  CD1 ILE A 183      26.098   2.897  28.736  1.00 57.88           C  
ANISOU 2620  CD1 ILE A 183    10484   2955   8551   -540   1001    266       C  
ATOM   2621  H   ILE A 183      26.995   3.572  32.241  1.00 75.14           H  
ATOM   2622  HA  ILE A 183      29.376   2.554  31.274  1.00 71.85           H  
ATOM   2623  HB  ILE A 183      27.653   4.404  30.031  1.00 78.24           H  
ATOM   2624 HG12 ILE A 183      27.871   1.904  28.848  1.00 76.62           H  
ATOM   2625 HG13 ILE A 183      27.088   1.902  30.217  1.00 76.62           H  
ATOM   2626 HG21 ILE A 183      28.974   3.859  28.053  1.00 61.95           H  
ATOM   2627 HG22 ILE A 183      29.626   4.865  29.089  1.00 61.95           H  
ATOM   2628 HG23 ILE A 183      30.070   3.341  29.065  1.00 61.95           H  
ATOM   2629 HD11 ILE A 183      25.625   2.114  28.405  1.00 69.77           H  
ATOM   2630 HD12 ILE A 183      25.521   3.387  29.347  1.00 69.77           H  
ATOM   2631 HD13 ILE A 183      26.336   3.469  27.985  1.00 69.77           H  
ATOM   2632  N   VAL A 184      30.984   4.397  31.692  1.00 61.16           N  
ANISOU 2632  N   VAL A 184    11210   3430   8598    200    202    700       N  
ATOM   2633  CA  VAL A 184      31.944   5.439  32.125  1.00 60.16           C  
ANISOU 2633  CA  VAL A 184    11058   3402   8396    324     15    728       C  
ATOM   2634  C   VAL A 184      32.330   6.253  30.895  1.00 62.27           C  
ANISOU 2634  C   VAL A 184    10974   3827   8860    328    -39    633       C  
ATOM   2635  O   VAL A 184      33.133   5.747  30.125  1.00 57.09           O  
ANISOU 2635  O   VAL A 184    10136   3156   8398    357    -56    576       O  
ATOM   2636  CB  VAL A 184      33.177   4.825  32.809  1.00 56.89           C  
ANISOU 2636  CB  VAL A 184    10811   2871   7932    495   -174    811       C  
ATOM   2637  CG1 VAL A 184      34.284   5.850  33.005  1.00 56.02           C  
ANISOU 2637  CG1 VAL A 184    10632   2862   7791    606   -397    804       C  
ATOM   2638  CG2 VAL A 184      32.808   4.170  34.129  1.00 60.04           C  
ANISOU 2638  CG2 VAL A 184    11624   3114   8073    513   -136    927       C  
ATOM   2639  H   VAL A 184      31.378   3.701  31.261  1.00 73.71           H  
ATOM   2640  HA  VAL A 184      31.508   6.008  32.758  1.00 72.51           H  
ATOM   2641  HB  VAL A 184      33.527   4.117  32.212  1.00 68.03           H  
ATOM   2642 HG11 VAL A 184      34.867   5.564  33.728  1.00 65.81           H  
ATOM   2643 HG12 VAL A 184      34.805   5.931  32.187  1.00 65.81           H  
ATOM   2644 HG13 VAL A 184      33.894   6.713  33.230  1.00 65.81           H  
ATOM   2645 HG21 VAL A 184      33.570   3.669  34.469  1.00 70.45           H  
ATOM   2646 HG22 VAL A 184      32.558   4.855  34.774  1.00 70.45           H  
ATOM   2647 HG23 VAL A 184      32.059   3.563  33.996  1.00 70.45           H  
ATOM   2648  N   PHE A 185      31.865   7.502  30.779  1.00 68.64           N  
ANISOU 2648  N   PHE A 185    11717   4762   9601    306    -53    617       N  
ATOM   2649  CA  PHE A 185      32.147   8.391  29.622  1.00 54.86           C  
ANISOU 2649  CA  PHE A 185     9683   3152   8009    304    -80    553       C  
ATOM   2650  C   PHE A 185      33.425   9.171  29.898  1.00 54.26           C  
ANISOU 2650  C   PHE A 185     9590   3106   7919    402   -258    580       C  
ATOM   2651  O   PHE A 185      33.472   9.786  30.925  1.00 48.91           O  
ANISOU 2651  O   PHE A 185     9110   2407   7065    422   -348    616       O  
ATOM   2652  CB  PHE A 185      30.971   9.328  29.362  1.00 49.77           C  
ANISOU 2652  CB  PHE A 185     8993   2602   7315    212     42    517       C  
ATOM   2653  CG  PHE A 185      31.109  10.203  28.147  1.00 53.71           C  
ANISOU 2653  CG  PHE A 185     9233   3217   7958    214     31    466       C  
ATOM   2654  CD1 PHE A 185      30.802   9.717  26.890  1.00 61.51           C  
ANISOU 2654  CD1 PHE A 185    10080   4218   9072    182     84    395       C  
ATOM   2655  CD2 PHE A 185      31.532  11.515  28.264  1.00 54.90           C  
ANISOU 2655  CD2 PHE A 185     9324   3438   8097    246    -33    487       C  
ATOM   2656  CE1 PHE A 185      30.926  10.524  25.773  1.00 56.57           C  
ANISOU 2656  CE1 PHE A 185     9280   3683   8531    202     72    362       C  
ATOM   2657  CE2 PHE A 185      31.653  12.318  27.145  1.00 54.12           C  
ANISOU 2657  CE2 PHE A 185     9025   3422   8115    252    -28    468       C  
ATOM   2658  CZ  PHE A 185      31.352  11.819  25.903  1.00 58.70           C  
ANISOU 2658  CZ  PHE A 185     9488   4023   8793    240     22    415       C  
ATOM   2659  H   PHE A 185      31.372   7.914  31.419  1.00 82.69           H  
ATOM   2660  HA  PHE A 185      32.284   7.831  28.817  1.00 66.15           H  
ATOM   2661  HB2 PHE A 185      30.161   8.783  29.266  1.00 60.04           H  
ATOM   2662  HB3 PHE A 185      30.850   9.898  30.149  1.00 60.04           H  
ATOM   2663  HD1 PHE A 185      30.510   8.825  26.792  1.00 74.13           H  
ATOM   2664  HD2 PHE A 185      31.743  11.865  29.115  1.00 66.20           H  
ATOM   2665  HE1 PHE A 185      30.718  10.183  24.923  1.00 68.20           H  
ATOM   2666  HE2 PHE A 185      31.944  13.210  27.238  1.00 65.26           H  
ATOM   2667  HZ  PHE A 185      31.434  12.365  25.140  1.00 70.76           H  
ATOM   2668  N   VAL A 186      34.392   9.148  28.988  1.00 47.59           N  
ANISOU 2668  N   VAL A 186     8547   2293   7243    459   -313    553       N  
ATOM   2669  CA  VAL A 186      35.683   9.863  29.137  1.00 50.81           C  
ANISOU 2669  CA  VAL A 186     8938   2707   7659    541   -495    570       C  
ATOM   2670  C   VAL A 186      35.746  10.988  28.103  1.00 54.17           C  
ANISOU 2670  C   VAL A 186     9152   3238   8193    494   -440    540       C  
ATOM   2671  O   VAL A 186      35.540  10.695  26.919  1.00 51.10           O  
ANISOU 2671  O   VAL A 186     8598   2891   7928    484   -319    505       O  
ATOM   2672  CB  VAL A 186      36.878   8.906  28.975  1.00 54.21           C  
ANISOU 2672  CB  VAL A 186     9366   3052   8177    681   -627    578       C  
ATOM   2673  CG1 VAL A 186      38.210   9.623  29.131  1.00 49.89           C  
ANISOU 2673  CG1 VAL A 186     8785   2503   7666    760   -885    581       C  
ATOM   2674  CG2 VAL A 186      36.786   7.721  29.925  1.00 57.81           C  
ANISOU 2674  CG2 VAL A 186    10062   3379   8523    747   -677    631       C  
ATOM   2675  H   VAL A 186      34.316   8.706  28.196  1.00 57.43           H  
ATOM   2676  HA  VAL A 186      35.723  10.252  30.019  1.00 61.29           H  
ATOM   2677  HB  VAL A 186      36.838   8.550  28.055  1.00 65.37           H  
ATOM   2678 HG11 VAL A 186      38.926   8.969  29.201  1.00 58.27           H  
ATOM   2679 HG12 VAL A 186      38.369  10.191  28.357  1.00 58.27           H  
ATOM   2680 HG13 VAL A 186      38.192  10.169  29.936  1.00 58.27           H  
ATOM   2681 HG21 VAL A 186      37.496   7.089  29.727  1.00 69.69           H  
ATOM   2682 HG22 VAL A 186      36.878   8.033  30.842  1.00 69.69           H  
ATOM   2683 HG23 VAL A 186      35.927   7.278  29.819  1.00 69.69           H  
ATOM   2684  N   SER A 187      35.994  12.222  28.524  1.00 45.86           N  
ANISOU 2684  N   SER A 187     8138   2201   7085    468   -541    550       N  
ATOM   2685  CA  SER A 187      36.203  13.356  27.594  1.00 47.26           C  
ANISOU 2685  CA  SER A 187     8156   2439   7362    426   -503    546       C  
ATOM   2686  C   SER A 187      37.159  14.352  28.213  1.00 46.06           C  
ANISOU 2686  C   SER A 187     8082   2223   7193    412   -729    547       C  
ATOM   2687  O   SER A 187      37.059  14.552  29.416  1.00 47.85           O  
ANISOU 2687  O   SER A 187     8514   2387   7278    411   -869    537       O  
ATOM   2688  CB  SER A 187      34.918  14.045  27.217  1.00 46.07           C  
ANISOU 2688  CB  SER A 187     7943   2365   7196    353   -319    544       C  
ATOM   2689  OG  SER A 187      35.103  14.947  26.138  1.00 50.14           O  
ANISOU 2689  OG  SER A 187     8312   2923   7815    337   -259    565       O  
ATOM   2690  H   SER A 187      36.016  12.473  29.400  1.00 54.37           H  
ATOM   2691  HA  SER A 187      36.621  12.997  26.772  1.00 57.03           H  
ATOM   2692  HB2 SER A 187      34.258  13.369  26.961  1.00 55.60           H  
ATOM   2693  HB3 SER A 187      34.569  14.534  27.996  1.00 55.60           H  
ATOM   2694  HG  SER A 187      35.779  14.737  25.677  1.00 60.49           H  
ATOM   2695  N   SER A 188      38.049  14.928  27.423  1.00 53.28           N  
ANISOU 2695  N   SER A 188     8852   3132   8261    391   -795    553       N  
ATOM   2696  CA  SER A 188      38.887  16.034  27.865  1.00 49.41           C  
ANISOU 2696  CA  SER A 188     8389   2555   7831    320  -1015    542       C  
ATOM   2697  C   SER A 188      38.223  17.388  27.652  1.00 58.27           C  
ANISOU 2697  C   SER A 188     9508   3695   8936    219   -847    553       C  
ATOM   2698  O   SER A 188      38.722  18.395  28.170  1.00 48.21           O  
ANISOU 2698  O   SER A 188     8301   2322   7693    134   -998    527       O  
ATOM   2699  CB  SER A 188      40.241  16.002  27.146  1.00 54.92           C  
ANISOU 2699  CB  SER A 188     8883   3192   8791    328  -1225    551       C  
ATOM   2700  OG  SER A 188      40.086  15.975  25.740  1.00 68.96           O  
ANISOU 2700  OG  SER A 188    10472   5042  10689    328  -1024    591       O  
ATOM   2701  H   SER A 188      38.132  14.736  26.588  1.00 64.26           H  
ATOM   2702  HA  SER A 188      39.066  15.934  28.813  1.00 59.61           H  
ATOM   2703  HB2 SER A 188      40.743  16.796  27.390  1.00 66.22           H  
ATOM   2704  HB3 SER A 188      40.722  15.207  27.423  1.00 66.22           H  
ATOM   2705  HG  SER A 188      40.820  15.794  25.373  1.00 83.07           H  
ATOM   2706  N   ASN A 189      37.120  17.438  26.907  1.00 54.53           N  
ANISOU 2706  N   ASN A 189     8961   3322   8438    233   -566    585       N  
ATOM   2707  CA  ASN A 189      36.340  18.662  26.774  1.00 49.10           C  
ANISOU 2707  CA  ASN A 189     8272   2641   7742    187   -418    607       C  
ATOM   2708  C   ASN A 189      35.420  18.791  27.982  1.00 48.27           C  
ANISOU 2708  C   ASN A 189     8322   2530   7486    195   -416    562       C  
ATOM   2709  O   ASN A 189      34.504  17.981  28.158  1.00 43.94           O  
ANISOU 2709  O   ASN A 189     7784   2049   6861    235   -335    555       O  
ATOM   2710  CB  ASN A 189      35.526  18.644  25.485  1.00 43.92           C  
ANISOU 2710  CB  ASN A 189     7466   2078   7145    226   -207    668       C  
ATOM   2711  CG  ASN A 189      36.396  18.647  24.241  1.00 56.40           C  
ANISOU 2711  CG  ASN A 189     8969   3648   8813    225   -201    721       C  
ATOM   2712  OD1 ASN A 189      36.128  17.918  23.282  1.00 55.82           O  
ANISOU 2712  OD1 ASN A 189     8833   3638   8736    287   -123    735       O  
ATOM   2713  ND2 ASN A 189      37.443  19.463  24.250  1.00 57.82           N  
ANISOU 2713  ND2 ASN A 189     9151   3731   9087    137   -327    742       N  
ATOM   2714  H   ASN A 189      36.802  16.771  26.466  1.00 65.76           H  
ATOM   2715  HA  ASN A 189      36.936  19.427  26.742  1.00 59.24           H  
ATOM   2716  HB2 ASN A 189      34.980  17.842  25.467  1.00 53.03           H  
ATOM   2717  HB3 ASN A 189      34.960  19.431  25.457  1.00 53.03           H  
ATOM   2718 HD21 ASN A 189      37.965  19.499  23.568  1.00 69.70           H  
ATOM   2719 HD22 ASN A 189      37.599  19.954  24.938  1.00 69.70           H  
ATOM   2720  N   ALA A 190      35.588  19.811  28.819  1.00 46.19           N  
ANISOU 2720  N   ALA A 190     8209   2166   7174    145   -515    522       N  
ATOM   2721  CA  ALA A 190      34.799  19.923  30.063  1.00 56.73           C  
ANISOU 2721  CA  ALA A 190     9766   3472   8318    165   -531    468       C  
ATOM   2722  C   ALA A 190      33.334  20.221  29.753  1.00 47.46           C  
ANISOU 2722  C   ALA A 190     8552   2362   7116    203   -329    484       C  
ATOM   2723  O   ALA A 190      32.517  19.995  30.638  1.00 46.47           O  
ANISOU 2723  O   ALA A 190     8623   2222   6810    233   -298    443       O  
ATOM   2724  CB  ALA A 190      35.408  20.933  30.986  1.00 68.84           C  
ANISOU 2724  CB  ALA A 190    11513   4850   9793    105   -720    396       C  
ATOM   2725  H   ALA A 190      36.145  20.522  28.680  1.00 55.08           H  
ATOM   2726  HA  ALA A 190      34.833  19.047  30.516  1.00 68.40           H  
ATOM   2727  HB1 ALA A 190      34.916  20.947  31.824  1.00 82.93           H  
ATOM   2728  HB2 ALA A 190      36.335  20.697  31.162  1.00 82.93           H  
ATOM   2729  HB3 ALA A 190      35.372  21.813  30.576  1.00 82.93           H  
ATOM   2730  N   TRP A 191      33.011  20.733  28.572  1.00 44.81           N  
ANISOU 2730  N   TRP A 191     8010   2083   6933    214   -213    545       N  
ATOM   2731  CA  TRP A 191      31.595  20.923  28.150  1.00 61.56           C  
ANISOU 2731  CA  TRP A 191    10108   4272   9011    274    -89    559       C  
ATOM   2732  C   TRP A 191      30.942  19.550  27.968  1.00 50.33           C  
ANISOU 2732  C   TRP A 191     8638   2947   7538    294    -35    553       C  
ATOM   2733  O   TRP A 191      29.780  19.397  28.358  1.00 42.97           O  
ANISOU 2733  O   TRP A 191     7800   2035   6490    330     67    526       O  
ATOM   2734  CB  TRP A 191      31.475  21.805  26.897  1.00 51.37           C  
ANISOU 2734  CB  TRP A 191     8671   2992   7856    298    -42    638       C  
ATOM   2735  CG  TRP A 191      32.040  21.272  25.618  1.00 51.74           C  
ANISOU 2735  CG  TRP A 191     8521   3102   8035    290    -44    713       C  
ATOM   2736  CD1 TRP A 191      33.221  21.626  25.038  1.00 43.26           C  
ANISOU 2736  CD1 TRP A 191     7362   1969   7108    241    -53    776       C  
ATOM   2737  CD2 TRP A 191      31.416  20.343  24.715  1.00 51.02           C  
ANISOU 2737  CD2 TRP A 191     8351   3120   7915    334    -16    722       C  
ATOM   2738  NE1 TRP A 191      33.391  20.961  23.857  1.00 47.42           N  
ANISOU 2738  NE1 TRP A 191     7756   2578   7683    264    -39    832       N  
ATOM   2739  CE2 TRP A 191      32.302  20.163  23.635  1.00 46.53           C  
ANISOU 2739  CE2 TRP A 191     7655   2560   7466    322    -43    791       C  
ATOM   2740  CE3 TRP A 191      30.212  19.632  24.724  1.00 57.72           C  
ANISOU 2740  CE3 TRP A 191     9257   4035   8639    380     53    669       C  
ATOM   2741  CZ2 TRP A 191      32.018  19.307  22.577  1.00 42.02           C  
ANISOU 2741  CZ2 TRP A 191     7044   2067   6854    367    -35    791       C  
ATOM   2742  CZ3 TRP A 191      29.935  18.782  23.682  1.00 41.56           C  
ANISOU 2742  CZ3 TRP A 191     7146   2056   6590    409     90    666       C  
ATOM   2743  CH2 TRP A 191      30.826  18.626  22.623  1.00 57.16           C  
ANISOU 2743  CH2 TRP A 191     9022   4046   8652    412     42    719       C  
ATOM   2744  H   TRP A 191      33.623  20.991  27.951  1.00 53.38           H  
ATOM   2745  HA  TRP A 191      31.128  21.392  28.881  1.00 74.19           H  
ATOM   2746  HB2 TRP A 191      30.525  21.993  26.758  1.00 61.96           H  
ATOM   2747  HB3 TRP A 191      31.912  22.659  27.094  1.00 61.96           H  
ATOM   2748  HD1 TRP A 191      33.846  22.232  25.404  1.00 50.36           H  
ATOM   2749  HE1 TRP A 191      34.090  21.029  23.332  1.00 57.22           H  
ATOM   2750  HE3 TRP A 191      29.603  19.731  25.437  1.00 69.59           H  
ATOM   2751  HZ2 TRP A 191      32.621  19.198  21.862  1.00 50.74           H  
ATOM   2752  HZ3 TRP A 191      29.125  18.298  23.680  1.00 50.20           H  
ATOM   2753  HH2 TRP A 191      30.608  18.037  21.925  1.00 68.92           H  
ATOM   2754  N   ASP A 192      31.667  18.607  27.372  1.00 51.04           N  
ANISOU 2754  N   ASP A 192     8610   3069   7713    274    -79    569       N  
ATOM   2755  CA  ASP A 192      31.193  17.214  27.158  1.00 54.37           C  
ANISOU 2755  CA  ASP A 192     9008   3544   8108    278    -35    549       C  
ATOM   2756  C   ASP A 192      31.047  16.500  28.502  1.00 43.58           C  
ANISOU 2756  C   ASP A 192     7841   2127   6591    264    -46    515       C  
ATOM   2757  O   ASP A 192      30.087  15.781  28.694  1.00 49.84           O  
ANISOU 2757  O   ASP A 192     8704   2925   7307    252     51    494       O  
ATOM   2758  CB  ASP A 192      32.171  16.494  26.250  1.00 56.70           C  
ANISOU 2758  CB  ASP A 192     9144   3859   8542    282    -68    568       C  
ATOM   2759  CG  ASP A 192      31.615  15.328  25.486  1.00 58.45           C  
ANISOU 2759  CG  ASP A 192     9320   4120   8769    286    -14    531       C  
ATOM   2760  OD1 ASP A 192      30.421  15.044  25.615  1.00 68.29           O  
ANISOU 2760  OD1 ASP A 192    10662   5373   9911    271     68    495       O  
ATOM   2761  OD2 ASP A 192      32.403  14.729  24.775  1.00 49.70           O  
ANISOU 2761  OD2 ASP A 192     8111   3013   7759    305    -32    526       O  
ATOM   2762  H   ASP A 192      32.526  18.753  27.107  1.00 61.56           H  
ATOM   2763  HA  ASP A 192      30.312  17.254  26.719  1.00 65.57           H  
ATOM   2764  HB2 ASP A 192      32.527  17.127  25.593  1.00 68.36           H  
ATOM   2765  HB3 ASP A 192      32.915  16.172  26.794  1.00 68.36           H  
ATOM   2766  N   VAL A 193      31.962  16.733  29.421  1.00 48.55           N  
ANISOU 2766  N   VAL A 193     8607   2685   7156    264   -166    511       N  
ATOM   2767  CA  VAL A 193      31.915  16.079  30.749  1.00 48.01           C  
ANISOU 2767  CA  VAL A 193     8807   2547   6886    270   -200    497       C  
ATOM   2768  C   VAL A 193      30.617  16.510  31.422  1.00 49.75           C  
ANISOU 2768  C   VAL A 193     9209   2751   6941    270    -54    474       C  
ATOM   2769  O   VAL A 193      29.921  15.632  31.932  1.00 51.05           O  
ANISOU 2769  O   VAL A 193     9526   2890   6979    261     60    479       O  
ATOM   2770  CB  VAL A 193      33.159  16.409  31.592  1.00 57.54           C  
ANISOU 2770  CB  VAL A 193    10192   3661   8010    284   -412    484       C  
ATOM   2771  CG1 VAL A 193      32.986  16.019  33.050  1.00 48.71           C  
ANISOU 2771  CG1 VAL A 193     9436   2452   6620    311   -462    479       C  
ATOM   2772  CG2 VAL A 193      34.424  15.784  31.025  1.00 54.05           C  
ANISOU 2772  CG2 VAL A 193     9611   3213   7711    304   -553    505       C  
ATOM   2773  H   VAL A 193      32.653  17.314  29.304  1.00 58.58           H  
ATOM   2774  HA  VAL A 193      31.884  15.114  30.613  1.00 57.93           H  
ATOM   2775  HB  VAL A 193      33.277  17.390  31.564  1.00 69.37           H  
ATOM   2776 HG11 VAL A 193      33.841  16.096  33.502  1.00 56.86           H  
ATOM   2777 HG12 VAL A 193      32.344  16.612  33.477  1.00 56.86           H  
ATOM   2778 HG13 VAL A 193      32.669  15.100  33.109  1.00 56.86           H  
ATOM   2779 HG21 VAL A 193      35.198  16.283  31.336  1.00 65.18           H  
ATOM   2780 HG22 VAL A 193      34.494  14.860  31.322  1.00 65.18           H  
ATOM   2781 HG23 VAL A 193      34.396  15.810  30.054  1.00 65.18           H  
ATOM   2782  N   ALA A 194      30.262  17.793  31.366  1.00 53.21           N  
ANISOU 2782  N   ALA A 194     9655   3181   7381    285    -28    451       N  
ATOM   2783  CA  ALA A 194      29.058  18.331  32.032  1.00 46.73           C  
ANISOU 2783  CA  ALA A 194     9040   2322   6395    317    132    419       C  
ATOM   2784  C   ALA A 194      27.786  17.760  31.415  1.00 45.97           C  
ANISOU 2784  C   ALA A 194     8846   2285   6335    322    335    428       C  
ATOM   2785  O   ALA A 194      26.861  17.497  32.168  1.00 47.12           O  
ANISOU 2785  O   ALA A 194     9193   2381   6328    328    526    412       O  
ATOM   2786  CB  ALA A 194      29.076  19.827  31.977  1.00 47.25           C  
ANISOU 2786  CB  ALA A 194     9129   2341   6483    352    113    389       C  
ATOM   2787  H   ALA A 194      30.723  18.424  30.899  1.00 64.17           H  
ATOM   2788  HA  ALA A 194      29.085  18.057  32.979  1.00 56.30           H  
ATOM   2789  HB1 ALA A 194      28.286  20.177  32.421  1.00 56.21           H  
ATOM   2790  HB2 ALA A 194      29.872  20.159  32.426  1.00 56.21           H  
ATOM   2791  HB3 ALA A 194      29.081  20.121  31.051  1.00 56.21           H  
ATOM   2792  N   GLY A 195      27.732  17.613  30.099  1.00 44.42           N  
ANISOU 2792  N   GLY A 195     8378   2173   6327    320    319    448       N  
ATOM   2793  CA  GLY A 195      26.573  17.024  29.407  1.00 46.27           C  
ANISOU 2793  CA  GLY A 195     8552   2442   6588    322    497    437       C  
ATOM   2794  C   GLY A 195      26.356  15.575  29.796  1.00 53.72           C  
ANISOU 2794  C   GLY A 195     9569   3354   7489    242    574    427       C  
ATOM   2795  O   GLY A 195      25.194  15.203  29.971  1.00 47.48           O  
ANISOU 2795  O   GLY A 195     8851   2525   6662    212    805    401       O  
ATOM   2796  H   GLY A 195      28.418  17.857  29.551  1.00 51.71           H  
ATOM   2797  HA2 GLY A 195      25.765  17.546  29.630  1.00 55.85           H  
ATOM   2798  HA3 GLY A 195      26.716  17.084  28.431  1.00 55.85           H  
ATOM   2799  N   ALA A 196      27.429  14.801  29.921  1.00 44.47           N  
ANISOU 2799  N   ALA A 196     8387   2172   6339    208    413    448       N  
ATOM   2800  CA  ALA A 196      27.372  13.390  30.362  1.00 58.34           C  
ANISOU 2800  CA  ALA A 196    10244   3868   8053    143    475    454       C  
ATOM   2801  C   ALA A 196      26.938  13.322  31.820  1.00 54.03           C  
ANISOU 2801  C   ALA A 196    10029   3223   7277    133    586    477       C  
ATOM   2802  O   ALA A 196      26.109  12.467  32.126  1.00 52.12           O  
ANISOU 2802  O   ALA A 196     9925   2909   6969     63    784    484       O  
ATOM   2803  CB  ALA A 196      28.704  12.738  30.130  1.00 50.77           C  
ANISOU 2803  CB  ALA A 196     9180   2908   7200    154    281    476       C  
ATOM   2804  H   ALA A 196      28.279  15.093  29.779  1.00 51.78           H  
ATOM   2805  HA  ALA A 196      26.696  12.922  29.817  1.00 70.32           H  
ATOM   2806  HB1 ALA A 196      28.676  11.821  30.446  1.00 61.24           H  
ATOM   2807  HB2 ALA A 196      28.905  12.745  29.179  1.00 61.24           H  
ATOM   2808  HB3 ALA A 196      29.395  13.224  30.608  1.00 61.24           H  
ATOM   2809  N   VAL A 197      27.437  14.226  32.660  1.00 48.07           N  
ANISOU 2809  N   VAL A 197     9436   2441   6387    194    482    485       N  
ATOM   2810  CA  VAL A 197      27.095  14.258  34.110  1.00 54.57           C  
ANISOU 2810  CA  VAL A 197    10644   3155   6936    204    600    499       C  
ATOM   2811  C   VAL A 197      25.600  14.520  34.215  1.00 57.76           C  
ANISOU 2811  C   VAL A 197    11146   3526   7275    184    932    474       C  
ATOM   2812  O   VAL A 197      24.959  13.885  35.050  1.00 53.22           O  
ANISOU 2812  O   VAL A 197    10834   2851   6537    138   1164    500       O  
ATOM   2813  CB  VAL A 197      27.930  15.300  34.882  1.00 54.50           C  
ANISOU 2813  CB  VAL A 197    10816   3107   6786    274    418    477       C  
ATOM   2814  CG1 VAL A 197      27.367  15.578  36.266  1.00 54.59           C  
ANISOU 2814  CG1 VAL A 197    11275   2993   6472    304    580    470       C  
ATOM   2815  CG2 VAL A 197      29.397  14.926  34.987  1.00 51.56           C  
ANISOU 2815  CG2 VAL A 197    10425   2721   6444    292    132    504       C  
ATOM   2816  H   VAL A 197      27.997  14.891  32.394  1.00 56.72           H  
ATOM   2817  HA  VAL A 197      27.280  13.378  34.485  1.00 65.81           H  
ATOM   2818  HB  VAL A 197      27.879  16.143  34.371  1.00 65.72           H  
ATOM   2819 HG11 VAL A 197      28.034  16.048  36.798  1.00 65.82           H  
ATOM   2820 HG12 VAL A 197      26.570  16.131  36.192  1.00 65.82           H  
ATOM   2821 HG13 VAL A 197      27.142  14.738  36.702  1.00 65.82           H  
ATOM   2822 HG21 VAL A 197      29.935  15.735  35.045  1.00 62.19           H  
ATOM   2823 HG22 VAL A 197      29.539  14.387  35.785  1.00 62.19           H  
ATOM   2824 HG23 VAL A 197      29.663  14.419  34.204  1.00 62.19           H  
ATOM   2825  N   TRP A 198      25.070  15.427  33.405  1.00 50.03           N  
ANISOU 2825  N   TRP A 198     9972   2611   6425    225    989    431       N  
ATOM   2826  CA  TRP A 198      23.627  15.762  33.390  1.00 53.99           C  
ANISOU 2826  CA  TRP A 198    10550   3064   6900    241   1333    401       C  
ATOM   2827  C   TRP A 198      22.808  14.592  32.857  1.00 52.34           C  
ANISOU 2827  C   TRP A 198    10235   2837   6817    121   1568    398       C  
ATOM   2828  O   TRP A 198      21.721  14.384  33.395  1.00 58.49           O  
ANISOU 2828  O   TRP A 198    11155   3518   7551     74   1933    385       O  
ATOM   2829  CB  TRP A 198      23.367  17.043  32.584  1.00 50.13           C  
ANISOU 2829  CB  TRP A 198     9880   2633   6535    356   1317    366       C  
ATOM   2830  CG  TRP A 198      23.838  18.316  33.222  1.00 51.01           C  
ANISOU 2830  CG  TRP A 198    10139   2711   6532    457   1195    344       C  
ATOM   2831  CD1 TRP A 198      23.891  18.618  34.552  1.00 52.62           C  
ANISOU 2831  CD1 TRP A 198    10693   2811   6490    478   1217    325       C  
ATOM   2832  CD2 TRP A 198      24.291  19.495  32.533  1.00 49.78           C  
ANISOU 2832  CD2 TRP A 198     9816   2600   6498    542   1046    333       C  
ATOM   2833  NE1 TRP A 198      24.355  19.891  34.736  1.00 65.82           N  
ANISOU 2833  NE1 TRP A 198    12416   4455   8140    561   1082    281       N  
ATOM   2834  CE2 TRP A 198      24.613  20.452  33.516  1.00 51.58           C  
ANISOU 2834  CE2 TRP A 198    10286   2737   6574    592    982    292       C  
ATOM   2835  CE3 TRP A 198      24.465  19.830  31.187  1.00 50.26           C  
ANISOU 2835  CE3 TRP A 198     9581   2748   6766    581    971    359       C  
ATOM   2836  CZ2 TRP A 198      25.099  21.715  33.191  1.00 58.64           C  
ANISOU 2836  CZ2 TRP A 198    11109   3616   7556    655    853    273       C  
ATOM   2837  CZ3 TRP A 198      24.943  21.080  30.867  1.00 56.44           C  
ANISOU 2837  CZ3 TRP A 198    10308   3525   7613    656    850    364       C  
ATOM   2838  CH2 TRP A 198      25.253  22.009  31.857  1.00 49.67           C  
ANISOU 2838  CH2 TRP A 198     9669   2564   6639    681    796    319       C  
ATOM   2839  H   TRP A 198      25.561  15.890  32.794  1.00 59.51           H  
ATOM   2840  HA  TRP A 198      23.351  15.929  34.318  1.00 65.11           H  
ATOM   2841  HB2 TRP A 198      23.799  16.947  31.710  1.00 58.57           H  
ATOM   2842  HB3 TRP A 198      22.404  17.108  32.428  1.00 58.57           H  
ATOM   2843  HD1 TRP A 198      23.647  18.036  35.254  1.00 61.55           H  
ATOM   2844  HE1 TRP A 198      24.475  20.280  35.513  1.00 79.31           H  
ATOM   2845  HE3 TRP A 198      24.258  19.208  30.510  1.00 60.62           H  
ATOM   2846  HZ2 TRP A 198      25.306  22.342  33.858  1.00 70.69           H  
ATOM   2847  HZ3 TRP A 198      25.065  21.312  29.960  1.00 68.05           H  
ATOM   2848  HH2 TRP A 198      25.581  22.855  31.609  1.00 58.01           H  
ATOM   2849  N   PHE A 199      23.276  13.895  31.818  1.00 60.08           N  
ANISOU 2849  N   PHE A 199    10967   3888   7972     60   1396    396       N  
ATOM   2850  CA  PHE A 199      22.592  12.710  31.222  1.00 60.72           C  
ANISOU 2850  CA  PHE A 199    10952   3931   8189    -84   1596    363       C  
ATOM   2851  C   PHE A 199      22.532  11.582  32.256  1.00 58.49           C  
ANISOU 2851  C   PHE A 199    10905   3535   7783   -205   1719    409       C  
ATOM   2852  O   PHE A 199      21.498  10.917  32.313  1.00 60.26           O  
ANISOU 2852  O   PHE A 199    11145   3676   8077   -363   2028    382       O  
ATOM   2853  CB  PHE A 199      23.261  12.292  29.913  1.00 57.89           C  
ANISOU 2853  CB  PHE A 199    10320   3659   8016    -96   1365    332       C  
ATOM   2854  CG  PHE A 199      22.521  11.243  29.129  1.00 58.80           C  
ANISOU 2854  CG  PHE A 199    10315   3727   8298   -255   1554    252       C  
ATOM   2855  CD1 PHE A 199      21.397  11.575  28.395  1.00 64.50           C  
ANISOU 2855  CD1 PHE A 199    10888   4436   9185   -300   1818    159       C  
ATOM   2856  CD2 PHE A 199      22.957   9.931  29.113  1.00 58.30           C  
ANISOU 2856  CD2 PHE A 199    10273   3613   8265   -360   1475    251       C  
ATOM   2857  CE1 PHE A 199      20.720  10.615  27.663  1.00 61.15           C  
ANISOU 2857  CE1 PHE A 199    10310   3960   8962   -498   1995     35       C  
ATOM   2858  CE2 PHE A 199      22.279   8.974  28.382  1.00 59.14           C  
ANISOU 2858  CE2 PHE A 199    10269   3663   8539   -537   1642    145       C  
ATOM   2859  CZ  PHE A 199      21.163   9.317  27.660  1.00 64.62           C  
ANISOU 2859  CZ  PHE A 199    10789   4361   9404   -632   1899     22       C  
ATOM   2860  H   PHE A 199      24.072  14.080  31.414  1.00 72.41           H  
ATOM   2861  HA  PHE A 199      21.660  12.973  31.014  1.00 73.19           H  
ATOM   2862  HB2 PHE A 199      23.362  13.088  29.351  1.00 69.79           H  
ATOM   2863  HB3 PHE A 199      24.159  11.959  30.119  1.00 69.79           H  
ATOM   2864  HD1 PHE A 199      21.090  12.468  28.392  1.00 77.72           H  
ATOM   2865  HD2 PHE A 199      23.725   9.686  29.606  1.00 70.28           H  
ATOM   2866  HE1 PHE A 199      19.952  10.854  27.169  1.00 73.69           H  
ATOM   2867  HE2 PHE A 199      22.584   8.087  28.380  1.00 71.29           H  
ATOM   2868  HZ  PHE A 199      20.699   8.661  27.168  1.00 77.87           H  
ATOM   2869  N   GLY A 200      23.581  11.407  33.057  1.00 54.94           N  
ANISOU 2869  N   GLY A 200    10640   3066   7168   -144   1502    478       N  
ATOM   2870  CA  GLY A 200      23.617  10.405  34.136  1.00 55.27           C  
ANISOU 2870  CA  GLY A 200    10962   2980   7058   -215   1603    548       C  
ATOM   2871  C   GLY A 200      24.764   9.414  34.040  1.00 65.00           C  
ANISOU 2871  C   GLY A 200    12165   4197   8334   -194   1323    595       C  
ATOM   2872  O   GLY A 200      24.874   8.598  34.936  1.00 57.30           O  
ANISOU 2872  O   GLY A 200    11455   3096   7219   -219   1378    672       O  
ATOM   2873  H   GLY A 200      24.322  11.933  33.004  1.00 66.25           H  
ATOM   2874  HA2 GLY A 200      23.681  10.881  35.001  1.00 64.73           H  
ATOM   2875  HA3 GLY A 200      22.767   9.903  34.141  1.00 64.73           H  
ATOM   2876  N   TYR A 201      25.611   9.499  33.027  1.00 58.64           N  
ANISOU 2876  N   TYR A 201    11067   3493   7719   -137   1055    559       N  
ATOM   2877  CA  TYR A 201      26.789   8.623  32.899  1.00 52.71           C  
ANISOU 2877  CA  TYR A 201    10293   2709   7027    -85    820    601       C  
ATOM   2878  C   TYR A 201      27.739   8.839  34.059  1.00 56.51           C  
ANISOU 2878  C   TYR A 201    11051   3134   7287     24    673    678       C  
ATOM   2879  O   TYR A 201      27.770   9.963  34.563  1.00 54.69           O  
ANISOU 2879  O   TYR A 201    10926   2942   6913     81    636    667       O  
ATOM   2880  CB  TYR A 201      27.602   8.896  31.635  1.00 55.39           C  
ANISOU 2880  CB  TYR A 201    10288   3166   7593    -27    599    546       C  
ATOM   2881  CG  TYR A 201      27.010   8.444  30.327  1.00 63.28           C  
ANISOU 2881  CG  TYR A 201    11066   4189   8790   -113    681    461       C  
ATOM   2882  CD1 TYR A 201      26.726   7.111  30.096  1.00 61.70           C  
ANISOU 2882  CD1 TYR A 201    10919   3870   8655   -207    773    444       C  
ATOM   2883  CD2 TYR A 201      26.798   9.334  29.290  1.00 56.54           C  
ANISOU 2883  CD2 TYR A 201     9984   3454   8044    -98    662    392       C  
ATOM   2884  CE1 TYR A 201      26.206   6.677  28.891  1.00 59.93           C  
ANISOU 2884  CE1 TYR A 201    10526   3649   8596   -301    844    334       C  
ATOM   2885  CE2 TYR A 201      26.278   8.916  28.079  1.00 62.84           C  
ANISOU 2885  CE2 TYR A 201    10631   4259   8984   -171    738    297       C  
ATOM   2886  CZ  TYR A 201      25.978   7.583  27.877  1.00 54.63           C  
ANISOU 2886  CZ  TYR A 201     9644   3104   8007   -281    826    253       C  
ATOM   2887  OH  TYR A 201      25.463   7.153  26.693  1.00 49.39           O  
ANISOU 2887  OH  TYR A 201     8847   2435   7483   -373    908    119       O  
ATOM   2888  H   TYR A 201      25.516  10.073  32.327  1.00 70.68           H  
ATOM   2889  HA  TYR A 201      26.494   7.691  32.899  1.00 61.67           H  
ATOM   2890  HB2 TYR A 201      27.767   9.861  31.586  1.00 66.79           H  
ATOM   2891  HB3 TYR A 201      28.473   8.460  31.740  1.00 66.79           H  
ATOM   2892  HD1 TYR A 201      26.876   6.487  30.779  1.00 74.36           H  
ATOM   2893  HD2 TYR A 201      26.995  10.247  29.414  1.00 68.17           H  
ATOM   2894  HE1 TYR A 201      26.001   5.769  28.763  1.00 72.24           H  
ATOM   2895  HE2 TYR A 201      26.132   9.537  27.394  1.00 75.72           H  
ATOM   2896  HH  TYR A 201      25.874   7.528  26.041  1.00 59.58           H  
ATOM   2897  N   THR A 202      28.398   7.789  34.541  1.00 57.32           N  
ANISOU 2897  N   THR A 202    11307   3123   7348     58    590    749       N  
ATOM   2898  CA  THR A 202      29.505   7.929  35.501  1.00 56.78           C  
ANISOU 2898  CA  THR A 202    11417   3016   7140    197    341    804       C  
ATOM   2899  C   THR A 202      30.512   8.591  34.584  1.00 54.44           C  
ANISOU 2899  C   THR A 202    10791   2838   7057    268    101    750       C  
ATOM   2900  O   THR A 202      30.491   8.201  33.453  1.00 52.97           O  
ANISOU 2900  O   THR A 202    10307   2698   7121    244     97    710       O  
ATOM   2901  CB  THR A 202      29.929   6.596  36.123  1.00 62.20           C  
ANISOU 2901  CB  THR A 202    12339   3538   7757    241    314    902       C  
ATOM   2902  OG1 THR A 202      28.907   6.194  37.034  1.00 74.74           O  
ANISOU 2902  OG1 THR A 202    14271   5001   9128    161    577    967       O  
ATOM   2903  CG2 THR A 202      31.255   6.681  36.847  1.00 60.91           C  
ANISOU 2903  CG2 THR A 202    12374   3326   7441    409     21    956       C  
ATOM   2904  H   THR A 202      28.246   6.928  34.285  1.00 69.10           H  
ATOM   2905  HA  THR A 202      29.236   8.553  36.208  1.00 66.54           H  
ATOM   2906  HB  THR A 202      30.004   5.923  35.404  1.00 74.96           H  
ATOM   2907  HG1 THR A 202      28.182   6.058  36.620  1.00 90.01           H  
ATOM   2908 HG21 THR A 202      31.427   5.842  37.309  1.00 71.49           H  
ATOM   2909 HG22 THR A 202      31.969   6.848  36.206  1.00 71.49           H  
ATOM   2910 HG23 THR A 202      31.225   7.406  37.496  1.00 71.49           H  
ATOM   2911  N   THR A 203      31.313   9.558  35.013  1.00 61.58           N  
ANISOU 2911  N   THR A 203    11772   3773   7853    345    -87    739       N  
ATOM   2912  CA  THR A 203      32.146  10.360  34.073  1.00 63.19           C  
ANISOU 2912  CA  THR A 203    11660   4086   8263    372   -243    682       C  
ATOM   2913  C   THR A 203      33.555  10.625  34.550  1.00 53.58           C  
ANISOU 2913  C   THR A 203    10564   2819   6973    481   -540    695       C  
ATOM   2914  O   THR A 203      33.704  10.915  35.723  1.00 56.34           O  
ANISOU 2914  O   THR A 203    11269   3082   7057    530   -660    714       O  
ATOM   2915  CB  THR A 203      31.491  11.723  33.813  1.00 59.96           C  
ANISOU 2915  CB  THR A 203    11132   3778   7874    316   -156    619       C  
ATOM   2916  OG1 THR A 203      31.079  12.268  35.066  1.00 62.34           O  
ANISOU 2916  OG1 THR A 203    11769   4014   7901    339   -181    615       O  
ATOM   2917  CG2 THR A 203      30.319  11.643  32.864  1.00 49.74           C  
ANISOU 2917  CG2 THR A 203     9706   2534   6660    228     95    594       C  
ATOM   2918  H   THR A 203      31.391   9.818  35.880  1.00 74.22           H  
ATOM   2919  HA  THR A 203      32.197   9.878  33.221  1.00 76.15           H  
ATOM   2920  HB  THR A 203      32.173  12.320  33.420  1.00 72.28           H  
ATOM   2921  HG1 THR A 203      30.327  11.953  35.297  1.00 75.12           H  
ATOM   2922 HG21 THR A 203      29.867  12.504  32.834  1.00 60.01           H  
ATOM   2923 HG22 THR A 203      30.639  11.415  31.974  1.00 60.01           H  
ATOM   2924 HG23 THR A 203      29.695  10.963  33.166  1.00 60.01           H  
ATOM   2925  N   PHE A 204      34.519  10.587  33.643  1.00 52.56           N  
ANISOU 2925  N   PHE A 204    10166   2734   7069    521   -669    675       N  
ATOM   2926  CA  PHE A 204      35.925  10.917  33.952  1.00 53.88           C  
ANISOU 2926  CA  PHE A 204    10397   2851   7224    618   -986    670       C  
ATOM   2927  C   PHE A 204      36.381  12.042  33.031  1.00 58.47           C  
ANISOU 2927  C   PHE A 204    10692   3518   8006    570  -1036    610       C  
ATOM   2928  O   PHE A 204      36.209  11.899  31.822  1.00 56.05           O  
ANISOU 2928  O   PHE A 204    10088   3293   7915    541   -888    599       O  
ATOM   2929  CB  PHE A 204      36.857   9.720  33.786  1.00 55.38           C  
ANISOU 2929  CB  PHE A 204    10586   2965   7491    748  -1118    720       C  
ATOM   2930  CG  PHE A 204      38.300   9.957  34.153  1.00 57.33           C  
ANISOU 2930  CG  PHE A 204    10898   3149   7737    876  -1508    712       C  
ATOM   2931  CD2 PHE A 204      39.228  10.326  33.194  1.00 56.53           C  
ANISOU 2931  CD2 PHE A 204    10498   3091   7888    897  -1634    666       C  
ATOM   2932  CD1 PHE A 204      38.741   9.767  35.451  1.00 70.17           C  
ANISOU 2932  CD1 PHE A 204    12896   4657   9108    986  -1779    747       C  
ATOM   2933  CE2 PHE A 204      40.555  10.524  33.533  1.00 58.78           C  
ANISOU 2933  CE2 PHE A 204    10805   3303   8226   1014  -2048    648       C  
ATOM   2934  CE1 PHE A 204      40.070   9.961  35.786  1.00 62.69           C  
ANISOU 2934  CE1 PHE A 204    11991   3643   8183   1119  -2215    725       C  
ATOM   2935  CZ  PHE A 204      40.974  10.338  34.826  1.00 61.88           C  
ANISOU 2935  CZ  PHE A 204    11539   3584   8389   1129  -2362    671       C  
ATOM   2936  H   PHE A 204      34.395  10.356  32.771  1.00 61.48           H  
ATOM   2937  HA  PHE A 204      35.978  11.221  34.874  1.00 64.73           H  
ATOM   2938  HB2 PHE A 204      36.511   8.987  34.338  1.00 65.65           H  
ATOM   2939  HB3 PHE A 204      36.815   9.428  32.852  1.00 65.65           H  
ATOM   2940  HD2 PHE A 204      38.950  10.456  32.302  1.00 66.24           H  
ATOM   2941  HD1 PHE A 204      38.125   9.505  36.117  1.00 84.52           H  
ATOM   2942  HE2 PHE A 204      41.174  10.784  32.872  1.00 68.94           H  
ATOM   2943  HE1 PHE A 204      40.353   9.836  36.678  1.00 73.63           H  
ATOM   2944  HZ  PHE A 204      41.879  10.473  35.055  1.00 72.66           H  
ATOM   2945  N   TRP A 205      36.990  13.086  33.580  1.00 54.29           N  
ANISOU 2945  N   TRP A 205    10288   2943   7397    560  -1255    569       N  
ATOM   2946  CA  TRP A 205      37.511  14.232  32.797  1.00 57.31           C  
ANISOU 2946  CA  TRP A 205    10451   3361   7962    490  -1313    519       C  
ATOM   2947  C   TRP A 205      39.000  14.012  32.567  1.00 53.70           C  
ANISOU 2947  C   TRP A 205     9912   2830   7660    557  -1653    509       C  
ATOM   2948  O   TRP A 205      39.724  13.993  33.517  1.00 56.27           O  
ANISOU 2948  O   TRP A 205    10455   3035   7891    612  -2011    484       O  
ATOM   2949  CB  TRP A 205      37.186  15.541  33.541  1.00 52.85           C  
ANISOU 2949  CB  TRP A 205    10078   2748   7253    418  -1357    462       C  
ATOM   2950  CG  TRP A 205      37.766  16.801  32.973  1.00 52.59           C  
ANISOU 2950  CG  TRP A 205     9879   2700   7404    327  -1432    413       C  
ATOM   2951  CD1 TRP A 205      38.137  17.050  31.685  1.00 55.50           C  
ANISOU 2951  CD1 TRP A 205     9924   3132   8031    283  -1336    434       C  
ATOM   2952  CD2 TRP A 205      38.017  18.017  33.698  1.00 54.31           C  
ANISOU 2952  CD2 TRP A 205    10282   2801   7551    257  -1613    334       C  
ATOM   2953  NE1 TRP A 205      38.615  18.325  31.564  1.00 58.22           N  
ANISOU 2953  NE1 TRP A 205    10229   3405   8487    179  -1427    391       N  
ATOM   2954  CE2 TRP A 205      38.549  18.944  32.781  1.00 53.81           C  
ANISOU 2954  CE2 TRP A 205     9967   2731   7746    154  -1601    318       C  
ATOM   2955  CE3 TRP A 205      37.850  18.408  35.029  1.00 56.56           C  
ANISOU 2955  CE3 TRP A 205    10956   2965   7567    270  -1781    268       C  
ATOM   2956  CZ2 TRP A 205      38.922  20.232  33.158  1.00 55.52           C  
ANISOU 2956  CZ2 TRP A 205    10277   2818   8000     43  -1744    235       C  
ATOM   2957  CZ3 TRP A 205      38.213  19.683  35.399  1.00 58.19           C  
ANISOU 2957  CZ3 TRP A 205    11269   3049   7792    175  -1944    167       C  
ATOM   2958  CH2 TRP A 205      38.742  20.578  34.475  1.00 57.67           C  
ANISOU 2958  CH2 TRP A 205    10914   2974   8025     53  -1920    149       C  
ATOM   2959  H   TRP A 205      37.167  13.146  34.470  1.00 65.47           H  
ATOM   2960  HA  TRP A 205      37.046  14.253  31.935  1.00 69.09           H  
ATOM   2961  HB2 TRP A 205      36.213  15.632  33.572  1.00 61.82           H  
ATOM   2962  HB3 TRP A 205      37.497  15.447  34.465  1.00 61.82           H  
ATOM   2963  HD1 TRP A 205      38.085  16.433  30.975  1.00 66.92           H  
ATOM   2964  HE1 TRP A 205      38.913  18.687  30.824  1.00 70.18           H  
ATOM   2965  HE3 TRP A 205      37.496  17.806  35.664  1.00 66.27           H  
ATOM   2966  HZ2 TRP A 205      39.278  20.840  32.533  1.00 66.09           H  
ATOM   2967  HZ3 TRP A 205      38.105  19.955  36.297  1.00 68.23           H  
ATOM   2968  HH2 TRP A 205      38.982  21.439  34.757  1.00 67.62           H  
ATOM   2969  N   LEU A 206      39.427  13.826  31.333  1.00 53.29           N  
ANISOU 2969  N   LEU A 206     9555   2838   7853    566  -1575    521       N  
ATOM   2970  CA  LEU A 206      40.856  13.684  30.998  1.00 54.06           C  
ANISOU 2970  CA  LEU A 206     9498   2868   8174    639  -1892    509       C  
ATOM   2971  C   LEU A 206      41.434  15.090  30.824  1.00 57.34           C  
ANISOU 2971  C   LEU A 206     9788   3231   8766    502  -2046    462       C  
ATOM   2972  O   LEU A 206      41.627  15.509  29.686  1.00 55.97           O  
ANISOU 2972  O   LEU A 206     9355   3104   8809    425  -1909    474       O  
ATOM   2973  CB  LEU A 206      40.971  12.809  29.748  1.00 67.66           C  
ANISOU 2973  CB  LEU A 206    10972   4657  10077    716  -1724    533       C  
ATOM   2974  CG  LEU A 206      42.352  12.253  29.414  1.00 68.21           C  
ANISOU 2974  CG  LEU A 206    10861   4662  10395    872  -2023    525       C  
ATOM   2975  CD1 LEU A 206      42.808  11.239  30.449  1.00 77.79           C  
ANISOU 2975  CD1 LEU A 206    12287   5794  11475   1060  -2263    548       C  
ATOM   2976  CD2 LEU A 206      42.342  11.622  28.034  1.00 66.13           C  
ANISOU 2976  CD2 LEU A 206    10352   4470  10304    924  -1787    525       C  
ATOM   2977  H   LEU A 206      38.873  13.823  30.611  1.00 64.26           H  
ATOM   2978  HA  LEU A 206      41.314  13.243  31.748  1.00 64.76           H  
ATOM   2979  HB2 LEU A 206      40.360  12.053  29.857  1.00 81.50           H  
ATOM   2980  HB3 LEU A 206      40.652  13.322  28.979  1.00 81.50           H  
ATOM   2981  HG  LEU A 206      42.997  13.001  29.409  1.00 82.18           H  
ATOM   2982 HD11 LEU A 206      43.596  10.778  30.120  1.00 93.66           H  
ATOM   2983 HD12 LEU A 206      43.026  11.694  31.281  1.00 93.66           H  
ATOM   2984 HD13 LEU A 206      42.100  10.591  30.607  1.00 93.66           H  
ATOM   2985 HD21 LEU A 206      43.186  11.170  27.877  1.00 79.67           H  
ATOM   2986 HD22 LEU A 206      41.616  10.978  27.977  1.00 79.67           H  
ATOM   2987 HD23 LEU A 206      42.214  12.314  27.362  1.00 79.67           H  
ATOM   2988  N   ASN A 207      41.757  15.765  31.923  1.00 64.58           N  
ANISOU 2988  N   ASN A 207    10922   4026   9589    462  -2345    408       N  
ATOM   2989  CA  ASN A 207      42.257  17.165  31.909  1.00 62.22           C  
ANISOU 2989  CA  ASN A 207    10553   3632   9456    287  -2493    342       C  
ATOM   2990  C   ASN A 207      43.752  17.192  31.640  1.00 61.60           C  
ANISOU 2990  C   ASN A 207    10227   3419   9759    285  -2919    306       C  
ATOM   2991  O   ASN A 207      44.516  17.381  32.581  1.00 69.35           O  
ANISOU 2991  O   ASN A 207    11324   4238  10789    310  -3387    228       O  
ATOM   2992  CB  ASN A 207      41.922  17.868  33.217  1.00 59.46           C  
ANISOU 2992  CB  ASN A 207    10565   3184   8843    234  -2629    266       C  
ATOM   2993  CG  ASN A 207      42.302  19.335  33.219  1.00 60.53           C  
ANISOU 2993  CG  ASN A 207    10653   3198   9149     28  -2761    171       C  
ATOM   2994  OD1 ASN A 207      42.691  19.892  32.197  1.00 60.16           O  
ANISOU 2994  OD1 ASN A 207    10292   3151   9414    -99  -2689    189       O  
ATOM   2995  ND2 ASN A 207      42.191  19.972  34.368  1.00 62.59           N  
ANISOU 2995  ND2 ASN A 207    11242   3337   9203    -16  -2953     67       N  
ATOM   2996  H   ASN A 207      41.726  15.393  32.754  1.00 77.81           H  
ATOM   2997  HA  ASN A 207      41.796  17.650  31.184  1.00 74.98           H  
ATOM   2998  HB2 ASN A 207      40.962  17.787  33.377  1.00 71.67           H  
ATOM   2999  HB3 ASN A 207      42.385  17.416  33.952  1.00 71.67           H  
ATOM   3000 HD21 ASN A 207      42.697  20.678  34.532  1.00 73.52           H  
ATOM   3001 HD22 ASN A 207      41.614  19.694  34.974  1.00 73.52           H  
ATOM   3002  N   ARG A 208      44.147  16.978  30.400  1.00 65.40           N  
ANISOU 3002  N   ARG A 208    10343   3954  10551    262  -2774    356       N  
ATOM   3003  CA  ARG A 208      45.571  16.959  30.001  1.00 73.83           C  
ANISOU 3003  CA  ARG A 208    10985   5098  11967    260  -3035    310       C  
ATOM   3004  C   ARG A 208      46.183  18.359  30.022  1.00 77.89           C  
ANISOU 3004  C   ARG A 208    11294   5614  12685    -26  -3147    220       C  
ATOM   3005  O   ARG A 208      47.338  18.467  30.444  1.00 82.49           O  
ANISOU 3005  O   ARG A 208    11612   6291  13440    -68  -3482    116       O  
ATOM   3006  CB  ARG A 208      45.703  16.367  28.601  1.00 76.04           C  
ANISOU 3006  CB  ARG A 208    10900   5542  12448    334  -2753    378       C  
ATOM   3007  CG  ARG A 208      45.176  14.947  28.437  1.00 74.56           C  
ANISOU 3007  CG  ARG A 208    10869   5341  12120    599  -2643    436       C  
ATOM   3008  CD  ARG A 208      45.311  14.556  26.982  1.00 75.15           C  
ANISOU 3008  CD  ARG A 208    10573   5586  12393    636  -2355    463       C  
ATOM   3009  NE  ARG A 208      45.020  13.167  26.652  1.00 89.99           N  
ANISOU 3009  NE  ARG A 208    12559   7447  14187    860  -2218    486       N  
ATOM   3010  CZ  ARG A 208      45.823  12.123  26.867  1.00 77.61           C  
ANISOU 3010  CZ  ARG A 208    10911   5894  12684   1105  -2388    460       C  
ATOM   3011  NH1 ARG A 208      46.991  12.261  27.475  1.00 79.28           N  
ANISOU 3011  NH1 ARG A 208    10909   6178  13036   1176  -2730    412       N  
ATOM   3012  NH2 ARG A 208      45.436  10.920  26.480  1.00 78.12           N  
ANISOU 3012  NH2 ARG A 208    11094   5936  12653   1269  -2204    466       N  
ATOM   3013  H   ARG A 208      43.562  16.900  29.707  1.00 78.80           H  
ATOM   3014  HA  ARG A 208      46.064  16.389  30.634  1.00 88.91           H  
ATOM   3015  HB2 ARG A 208      45.230  16.951  27.972  1.00 91.56           H  
ATOM   3016  HB3 ARG A 208      46.652  16.376  28.356  1.00 91.56           H  
ATOM   3017  HG2 ARG A 208      45.690  14.331  28.999  1.00 89.79           H  
ATOM   3018  HG3 ARG A 208      44.235  14.902  28.701  1.00 89.79           H  
ATOM   3019  HD2 ARG A 208      44.707  15.123  26.458  1.00 90.49           H  
ATOM   3020  HD3 ARG A 208      46.222  14.762  26.688  1.00 90.49           H  
ATOM   3021  HE  ARG A 208      44.273  13.013  26.233  1.00108.31           H  
ATOM   3022 HH11 ARG A 208      47.276  13.043  27.737  1.00 95.46           H  
ATOM   3023 HH12 ARG A 208      47.495  11.555  27.610  1.00 95.46           H  
ATOM   3024 HH21 ARG A 208      44.663  10.810  26.074  1.00 94.07           H  
ATOM   3025 HH22 ARG A 208      45.954  10.224  26.626  1.00 94.07           H  
ATOM   3026  N   THR A 209      45.463  19.382  29.575  1.00 68.85           N  
ANISOU 3026  N   THR A 209    10265   4360  11537   -223  -2878    255       N  
ATOM   3027  CA  THR A 209      45.988  20.765  29.414  1.00 77.23           C  
ANISOU 3027  CA  THR A 209    11127   5381  12836   -520  -2913    192       C  
ATOM   3028  C   THR A 209      46.279  21.456  30.742  1.00 76.78           C  
ANISOU 3028  C   THR A 209    11316   5173  12683   -641  -3276     26       C  
ATOM   3029  O   THR A 209      47.135  22.346  30.732  1.00 77.83           O  
ANISOU 3029  O   THR A 209    11217   5293  13063   -895  -3430    -81       O  
ATOM   3030  CB  THR A 209      45.004  21.599  28.593  1.00 75.76           C  
ANISOU 3030  CB  THR A 209    11041   5086  12658   -654  -2507    302       C  
ATOM   3031  OG1 THR A 209      43.717  21.377  29.166  1.00 77.56           O  
ANISOU 3031  OG1 THR A 209    11673   5344  12454   -518  -2302    316       O  
ATOM   3032  CG2 THR A 209      45.004  21.243  27.123  1.00 73.06           C  
ANISOU 3032  CG2 THR A 209    10384   4930  12446   -588  -2176    442       C  
ATOM   3033  H   THR A 209      44.577  19.317  29.372  1.00 82.94           H  
ATOM   3034  HA  THR A 209      46.832  20.705  28.911  1.00 93.00           H  
ATOM   3035  HB  THR A 209      45.241  22.552  28.693  1.00 91.23           H  
ATOM   3036  HG1 THR A 209      43.130  21.801  28.728  1.00 93.40           H  
ATOM   3037 HG21 THR A 209      44.384  21.823  26.646  1.00 87.99           H  
ATOM   3038 HG22 THR A 209      45.899  21.361  26.758  1.00 87.99           H  
ATOM   3039 HG23 THR A 209      44.729  20.315  27.011  1.00 87.99           H  
ATOM   3040  N   GLY A 210      45.631  21.065  31.830  1.00 76.66           N  
ANISOU 3040  N   GLY A 210    11769   5045  12314   -481  -3405     -6       N  
ATOM   3041  CA  GLY A 210      45.734  21.783  33.113  1.00 78.04           C  
ANISOU 3041  CA  GLY A 210    12273   5056  12321   -588  -3688   -169       C  
ATOM   3042  C   GLY A 210      44.604  22.777  33.222  1.00 70.46           C  
ANISOU 3042  C   GLY A 210    11600   4035  11138   -675  -3334   -161       C  
ATOM   3043  O   GLY A 210      44.648  23.614  34.134  1.00 78.26           O  
ANISOU 3043  O   GLY A 210    12798   4906  12033   -806  -3497   -315       O  
ATOM   3044  H   GLY A 210      45.089  20.331  31.843  1.00 92.31           H  
ATOM   3045  HA2 GLY A 210      45.674  21.131  33.856  1.00 93.96           H  
ATOM   3046  HA3 GLY A 210      46.602  22.251  33.172  1.00 93.96           H  
ATOM   3047  N   ALA A 211      43.607  22.672  32.354  1.00 71.75           N  
ANISOU 3047  N   ALA A 211    11726   4354  11182   -580  -2829     -6       N  
ATOM   3048  CA  ALA A 211      42.489  23.621  32.277  1.00 74.24           C  
ANISOU 3048  CA  ALA A 211    12204   4689  11313   -614  -2451      3       C  
ATOM   3049  C   ALA A 211      41.698  23.626  33.584  1.00 71.96           C  
ANISOU 3049  C   ALA A 211    12323   4379  10640   -496  -2490    -78       C  
ATOM   3050  O   ALA A 211      41.675  22.602  34.258  1.00 63.50           O  
ANISOU 3050  O   ALA A 211    11425   3337   9366   -344  -2670    -76       O  
ATOM   3051  CB  ALA A 211      41.614  23.261  31.111  1.00 59.43           C  
ANISOU 3051  CB  ALA A 211    10170   2994   9418   -512  -1970    166       C  
ATOM   3052  H   ALA A 211      43.521  21.988  31.762  1.00 86.42           H  
ATOM   3053  HA  ALA A 211      42.870  24.508  32.123  1.00 89.40           H  
ATOM   3054  HB1 ALA A 211      40.849  23.860  31.085  1.00 71.44           H  
ATOM   3055  HB2 ALA A 211      42.119  23.349  30.286  1.00 71.44           H  
ATOM   3056  HB3 ALA A 211      41.301  22.346  31.206  1.00 71.44           H  
ATOM   3057  N   PRO A 212      41.080  24.752  33.990  1.00 64.05           N  
ANISOU 3057  N   PRO A 212    11495   3311   9531   -551  -2305   -139       N  
ATOM   3058  CA  PRO A 212      40.319  24.821  35.209  1.00 64.99           C  
ANISOU 3058  CA  PRO A 212    12013   3388   9292   -447  -2343   -228       C  
ATOM   3059  C   PRO A 212      38.940  24.198  35.051  1.00 61.87           C  
ANISOU 3059  C   PRO A 212    11647   3170   8689   -261  -1958   -108       C  
ATOM   3060  O   PRO A 212      38.534  23.988  33.955  1.00 59.09           O  
ANISOU 3060  O   PRO A 212    11014   2962   8474   -225  -1641     16       O  
ATOM   3061  CB  PRO A 212      40.130  26.317  35.504  1.00 67.21           C  
ANISOU 3061  CB  PRO A 212    12410   3507   9621   -587  -2277   -351       C  
ATOM   3062  CG  PRO A 212      40.907  27.035  34.436  1.00 67.97           C  
ANISOU 3062  CG  PRO A 212    12165   3537  10123   -803  -2275   -330       C  
ATOM   3063  CD  PRO A 212      41.018  26.049  33.299  1.00 64.54           C  
ANISOU 3063  CD  PRO A 212    11430   3293   9800   -706  -2065   -137       C  
ATOM   3064  HA  PRO A 212      40.818  24.392  35.948  1.00 76.40           H  
ATOM   3065  HB2 PRO A 212      39.181  26.562  35.464  1.00 79.07           H  
ATOM   3066  HB3 PRO A 212      40.475  26.542  36.394  1.00 79.07           H  
ATOM   3067  HG2 PRO A 212      40.437  27.844  34.149  1.00 79.97           H  
ATOM   3068  HG3 PRO A 212      41.795  27.286  34.763  1.00 79.97           H  
ATOM   3069  HD2 PRO A 212      40.239  26.096  32.714  1.00 75.86           H  
ATOM   3070  HD3 PRO A 212      41.819  26.225  32.775  1.00 75.86           H  
ATOM   3071  N   ALA A 213      38.269  23.954  36.156  1.00 62.74           N  
ANISOU 3071  N   ALA A 213    12114   3261   8464   -153  -2006   -157       N  
ATOM   3072  CA  ALA A 213      36.910  23.398  36.166  1.00 60.50           C  
ANISOU 3072  CA  ALA A 213    11865   3121   8001    -15  -1658    -69       C  
ATOM   3073  C   ALA A 213      35.916  24.439  35.681  1.00 59.74           C  
ANISOU 3073  C   ALA A 213    11664   3040   7995    -21  -1326    -65       C  
ATOM   3074  O   ALA A 213      36.161  25.620  35.909  1.00 61.59           O  
ANISOU 3074  O   ALA A 213    12007   3122   8272    -95  -1371   -165       O  
ATOM   3075  CB  ALA A 213      36.565  22.951  37.552  1.00 62.36           C  
ANISOU 3075  CB  ALA A 213    12565   3292   7838     86  -1770   -120       C  
ATOM   3076  H   ALA A 213      38.580  24.145  36.989  1.00 73.70           H  
ATOM   3077  HA  ALA A 213      36.880  22.621  35.561  1.00 71.01           H  
ATOM   3078  HB1 ALA A 213      35.686  22.536  37.548  1.00 73.25           H  
ATOM   3079  HB2 ALA A 213      37.224  22.306  37.859  1.00 73.25           H  
ATOM   3080  HB3 ALA A 213      36.557  23.716  38.150  1.00 73.25           H  
ATOM   3081  N   GLU A 214      34.824  23.993  35.085  1.00 63.55           N  
ANISOU 3081  N   GLU A 214    11938   3689   8521     62  -1018     43       N  
ATOM   3082  CA  GLU A 214      33.755  24.871  34.589  1.00 56.33           C  
ANISOU 3082  CA  GLU A 214    10955   2782   7665    105   -753     54       C  
ATOM   3083  C   GLU A 214      32.907  25.230  35.799  1.00 59.56           C  
ANISOU 3083  C   GLU A 214    11744   3115   7773    189   -689    -33       C  
ATOM   3084  O   GLU A 214      33.163  24.644  36.853  1.00 66.21           O  
ANISOU 3084  O   GLU A 214    12877   3938   8341    227   -784    -65       O  
ATOM   3085  CB  GLU A 214      32.986  24.190  33.458  1.00 53.37           C  
ANISOU 3085  CB  GLU A 214    10252   2598   7428    166   -520    181       C  
ATOM   3086  CG  GLU A 214      33.832  23.850  32.239  1.00 52.13           C  
ANISOU 3086  CG  GLU A 214     9769   2518   7519    105   -554    269       C  
ATOM   3087  CD  GLU A 214      34.315  25.005  31.373  1.00 55.02           C  
ANISOU 3087  CD  GLU A 214     9991   2791   8124     30   -523    295       C  
ATOM   3088  OE1 GLU A 214      33.881  26.142  31.595  1.00 63.97           O  
ANISOU 3088  OE1 GLU A 214    11234   3809   9262     38   -463    256       O  
ATOM   3089  OE2 GLU A 214      35.125  24.756  30.464  1.00 51.89           O  
ANISOU 3089  OE2 GLU A 214     9394   2417   7904    -34   -546    360       O  
ATOM   3090  H   GLU A 214      34.640  23.105  35.001  1.00 76.58           H  
ATOM   3091  HA  GLU A 214      34.166  25.694  34.239  1.00 66.00           H  
ATOM   3092  HB2 GLU A 214      32.587  23.364  33.806  1.00 63.25           H  
ATOM   3093  HB3 GLU A 214      32.253  24.778  33.182  1.00 63.25           H  
ATOM   3094  HG2 GLU A 214      34.619  23.352  32.539  1.00 62.87           H  
ATOM   3095  HG3 GLU A 214      33.313  23.245  31.667  1.00 62.87           H  
ATOM   3096  N   GLU A 215      31.994  26.186  35.667  1.00 58.75           N  
ANISOU 3096  N   GLU A 215    11672   2944   7707    234   -524    -67       N  
ATOM   3097  CA  GLU A 215      31.105  26.619  36.767  1.00 60.74           C  
ANISOU 3097  CA  GLU A 215    12296   3103   7681    334   -415   -161       C  
ATOM   3098  C   GLU A 215      29.694  26.192  36.384  1.00 59.20           C  
ANISOU 3098  C   GLU A 215    12010   3034   7449    462   -117    -86       C  
ATOM   3099  O   GLU A 215      28.771  26.978  36.590  1.00 60.03           O  
ANISOU 3099  O   GLU A 215    12159   3086   7564    559     60   -113       O  
ATOM   3100  CB  GLU A 215      31.293  28.118  37.015  1.00 63.37           C  
ANISOU 3100  CB  GLU A 215    12774   3231   8071    315   -442   -277       C  
ATOM   3101  CG  GLU A 215      31.121  28.537  38.463  1.00 66.60           C  
ANISOU 3101  CG  GLU A 215    13676   3484   8147    380   -458   -433       C  
ATOM   3102  CD  GLU A 215      32.289  28.247  39.390  1.00 74.36           C  
ANISOU 3102  CD  GLU A 215    14946   4353   8956    279   -795   -545       C  
ATOM   3103  OE1 GLU A 215      33.408  28.016  38.900  1.00 76.30           O  
ANISOU 3103  OE1 GLU A 215    14995   4577   9418    136  -1025   -543       O  
ATOM   3104  OE2 GLU A 215      32.072  28.262  40.609  1.00 83.11           O  
ANISOU 3104  OE2 GLU A 215    16496   5384   9698    349   -837   -639       O  
ATOM   3105  H   GLU A 215      31.852  26.628  34.883  1.00 68.91           H  
ATOM   3106  HA  GLU A 215      31.357  26.136  37.584  1.00 71.30           H  
ATOM   3107  HB2 GLU A 215      32.189  28.371  36.714  1.00 74.45           H  
ATOM   3108  HB3 GLU A 215      30.651  28.612  36.465  1.00 74.45           H  
ATOM   3109  HG2 GLU A 215      30.946  29.501  38.489  1.00 78.33           H  
ATOM   3110  HG3 GLU A 215      30.327  28.089  38.826  1.00 78.33           H  
ATOM   3111  N   LEU A 216      29.537  24.985  35.844  1.00 57.43           N  
ANISOU 3111  N   LEU A 216    11669   2963   7191    463    -69      1       N  
ATOM   3112  CA  LEU A 216      28.234  24.513  35.325  1.00 55.80           C  
ANISOU 3112  CA  LEU A 216    11321   2877   7004    546    189     70       C  
ATOM   3113  C   LEU A 216      27.448  23.693  36.349  1.00 56.88           C  
ANISOU 3113  C   LEU A 216    11768   3000   6843    602    361     56       C  
ATOM   3114  O   LEU A 216      26.314  23.341  36.030  1.00 57.59           O  
ANISOU 3114  O   LEU A 216    11787   3156   6939    663    611     95       O  
ATOM   3115  CB  LEU A 216      28.502  23.706  34.057  1.00 66.06           C  
ANISOU 3115  CB  LEU A 216    12215   4343   8542    488    154    178       C  
ATOM   3116  CG  LEU A 216      29.072  24.466  32.861  1.00 54.21           C  
ANISOU 3116  CG  LEU A 216    10400   2871   7328    475    119    231       C  
ATOM   3117  CD1 LEU A 216      29.713  23.502  31.872  1.00 60.18           C  
ANISOU 3117  CD1 LEU A 216    10824   3774   8266    420     74    325       C  
ATOM   3118  CD2 LEU A 216      27.993  25.290  32.179  1.00 55.25           C  
ANISOU 3118  CD2 LEU A 216    10528   2986   7477    604    310    236       C  
ATOM   3119  H   LEU A 216      30.207  24.371  35.798  1.00 69.24           H  
ATOM   3120  HA  LEU A 216      27.695  25.300  35.088  1.00 65.37           H  
ATOM   3121  HB2 LEU A 216      29.119  22.982  34.284  1.00 79.59           H  
ATOM   3122  HB3 LEU A 216      27.663  23.291  33.779  1.00 79.59           H  
ATOM   3123  HG  LEU A 216      29.772  25.083  33.188  1.00 65.37           H  
ATOM   3124 HD11 LEU A 216      30.085  24.002  31.125  1.00 72.53           H  
ATOM   3125 HD12 LEU A 216      30.425  23.007  32.313  1.00 72.53           H  
ATOM   3126 HD13 LEU A 216      29.042  22.880  31.543  1.00 72.53           H  
ATOM   3127 HD21 LEU A 216      28.368  25.732  31.398  1.00 66.61           H  
ATOM   3128 HD22 LEU A 216      27.265  24.708  31.900  1.00 66.61           H  
ATOM   3129 HD23 LEU A 216      27.654  25.959  32.796  1.00 66.61           H  
ATOM   3130  N   GLY A 217      27.980  23.424  37.535  1.00 58.86           N  
ANISOU 3130  N   GLY A 217    12392   3147   6823    585    246      4       N  
ATOM   3131  CA  GLY A 217      27.254  22.671  38.583  1.00 60.23           C  
ANISOU 3131  CA  GLY A 217    12908   3286   6692    631    433     19       C  
ATOM   3132  C   GLY A 217      27.167  21.183  38.267  1.00 59.40           C  
ANISOU 3132  C   GLY A 217    12641   3293   6636    570    465    129       C  
ATOM   3133  O   GLY A 217      26.301  20.532  38.863  1.00 73.90           O  
ANISOU 3133  O   GLY A 217    14675   5106   8299    591    719    167       O  
ATOM   3134  H   GLY A 217      28.833  23.651  37.752  1.00 69.03           H  
ATOM   3135  HA2 GLY A 217      27.711  22.795  39.449  1.00 70.69           H  
ATOM   3136  HA3 GLY A 217      26.341  23.041  38.669  1.00 70.69           H  
ATOM   3137  N   ALA A 218      27.985  20.673  37.349  1.00 57.98           N  
ANISOU 3137  N   ALA A 218    12119   3214   6698    493    241    179       N  
ATOM   3138  CA  ALA A 218      28.086  19.260  36.938  1.00 65.96           C  
ANISOU 3138  CA  ALA A 218    12939   4323   7800    442    257    271       C  
ATOM   3139  C   ALA A 218      29.530  18.784  37.116  1.00 55.20           C  
ANISOU 3139  C   ALA A 218    11583   2944   6445    408    -58    293       C  
ATOM   3140  O   ALA A 218      30.222  18.617  36.121  1.00 53.36           O  
ANISOU 3140  O   ALA A 218    10996   2801   6479    368   -188    323       O  
ATOM   3141  CB  ALA A 218      27.684  19.196  35.496  1.00 57.05           C  
ANISOU 3141  CB  ALA A 218    11351   3336   6991    417    351    308       C  
ATOM   3142  H   ALA A 218      28.396  21.198  36.764  1.00 69.90           H  
ATOM   3143  HA  ALA A 218      27.479  18.703  37.477  1.00 79.47           H  
ATOM   3144  HB1 ALA A 218      27.738  18.281  35.181  1.00 68.78           H  
ATOM   3145  HB2 ALA A 218      26.774  19.510  35.405  1.00 68.78           H  
ATOM   3146  HB3 ALA A 218      28.270  19.757  34.962  1.00 68.78           H  
ATOM   3147  N   PRO A 219      30.016  18.573  38.354  1.00 65.90           N  
ANISOU 3147  N   PRO A 219    13376   4172   7490    443   -185    278       N  
ATOM   3148  CA  PRO A 219      31.364  18.042  38.571  1.00 67.76           C  
ANISOU 3148  CA  PRO A 219    13671   4367   7709    444   -524    297       C  
ATOM   3149  C   PRO A 219      31.555  16.559  38.181  1.00 70.17           C  
ANISOU 3149  C   PRO A 219    13812   4742   8109    440   -490    401       C  
ATOM   3150  O   PRO A 219      30.650  15.794  38.405  1.00 57.78           O  
ANISOU 3150  O   PRO A 219    12333   3177   6444    436   -236    458       O  
ATOM   3151  CB  PRO A 219      31.551  18.214  40.075  1.00 63.86           C  
ANISOU 3151  CB  PRO A 219    13783   3693   6788    513   -659    251       C  
ATOM   3152  CG  PRO A 219      30.164  18.112  40.636  1.00 68.93           C  
ANISOU 3152  CG  PRO A 219    14684   4303   7202    544   -277    265       C  
ATOM   3153  CD  PRO A 219      29.304  18.806  39.607  1.00 80.24           C  
ANISOU 3153  CD  PRO A 219    15704   5854   8931    505    -30    241       C  
ATOM   3154  HA  PRO A 219      32.014  18.615  38.096  1.00 81.64           H  
ATOM   3155  HB2 PRO A 219      32.128  17.509  40.439  1.00 76.95           H  
ATOM   3156  HB3 PRO A 219      31.947  19.087  40.281  1.00 76.95           H  
ATOM   3157  HG2 PRO A 219      29.896  17.177  40.742  1.00 83.03           H  
ATOM   3158  HG3 PRO A 219      30.103  18.562  41.503  1.00 83.03           H  
ATOM   3159  HD2 PRO A 219      28.410  18.417  39.585  1.00 96.61           H  
ATOM   3160  HD3 PRO A 219      29.231  19.760  39.796  1.00 96.61           H  
ATOM   3161  N   PRO A 220      32.705  16.142  37.598  1.00 65.98           N  
ANISOU 3161  N   PRO A 220    13056   4243   7772    440   -727    424       N  
ATOM   3162  CA  PRO A 220      32.906  14.757  37.186  1.00 59.53           C  
ANISOU 3162  CA  PRO A 220    12100   3467   7053    455   -695    514       C  
ATOM   3163  C   PRO A 220      33.151  13.788  38.353  1.00 67.70           C  
ANISOU 3163  C   PRO A 220    13578   4370   7774    536   -790    574       C  
ATOM   3164  O   PRO A 220      33.593  14.239  39.388  1.00 61.82           O  
ANISOU 3164  O   PRO A 220    13253   3502   6732    597   -980    543       O  
ATOM   3165  CB  PRO A 220      34.150  14.792  36.306  1.00 72.96           C  
ANISOU 3165  CB  PRO A 220    13475   5214   9034    458   -920    506       C  
ATOM   3166  CG  PRO A 220      34.914  16.010  36.755  1.00 63.51           C  
ANISOU 3166  CG  PRO A 220    12397   3940   7795    449  -1179    423       C  
ATOM   3167  CD  PRO A 220      33.873  16.970  37.286  1.00 60.22           C  
ANISOU 3167  CD  PRO A 220    12191   3491   7199    421  -1016    364       C  
ATOM   3168  HA  PRO A 220      32.132  14.457  36.648  1.00 71.76           H  
ATOM   3169  HB2 PRO A 220      34.686  13.982  36.433  1.00 87.87           H  
ATOM   3170  HB3 PRO A 220      33.908  14.858  35.367  1.00 87.87           H  
ATOM   3171  HG2 PRO A 220      35.558  15.776  37.455  1.00 76.53           H  
ATOM   3172  HG3 PRO A 220      35.399  16.409  36.004  1.00 76.53           H  
ATOM   3173  HD2 PRO A 220      34.198  17.423  38.086  1.00 72.58           H  
ATOM   3174  HD3 PRO A 220      33.651  17.640  36.615  1.00 72.58           H  
ATOM   3175  N   ASP A 221      32.873  12.495  38.162  1.00 59.22           N  
ANISOU 3175  N   ASP A 221    12439   3303   6760    542   -663    662       N  
ATOM   3176  CA  ASP A 221      33.085  11.459  39.212  1.00 75.59           C  
ANISOU 3176  CA  ASP A 221    14921   5240   8560    633   -743    748       C  
ATOM   3177  C   ASP A 221      34.587  11.330  39.464  1.00 68.18           C  
ANISOU 3177  C   ASP A 221    14067   4237   7601    759  -1169    753       C  
ATOM   3178  O   ASP A 221      34.947  11.108  40.614  1.00 67.28           O  
ANISOU 3178  O   ASP A 221    14406   3991   7165    873  -1375    786       O  
ATOM   3179  CB  ASP A 221      32.392  10.142  38.851  1.00 62.57           C  
ANISOU 3179  CB  ASP A 221    13164   3585   7025    593   -495    838       C  
ATOM   3180  CG  ASP A 221      30.881  10.215  38.966  1.00 71.31           C  
ANISOU 3180  CG  ASP A 221    14342   4694   8060    481   -105    842       C  
ATOM   3181  OD1 ASP A 221      30.388  10.364  40.095  1.00 67.68           O  
ANISOU 3181  OD1 ASP A 221    14321   4132   7261    501     11    865       O  
ATOM   3182  OD2 ASP A 221      30.213  10.146  37.927  1.00 68.36           O  
ANISOU 3182  OD2 ASP A 221    13609   4411   7954    380     86    817       O  
ATOM   3183  H   ASP A 221      32.574  12.167  37.365  1.00 69.48           H  
ATOM   3184  HA  ASP A 221      32.670  11.789  40.043  1.00 91.03           H  
ATOM   3185  HB2 ASP A 221      32.627   9.884  37.938  1.00 75.40           H  
ATOM   3186  HB3 ASP A 221      32.712   9.441  39.455  1.00 75.40           H  
ATOM   3187  N   GLY A 222      35.430  11.523  38.452  1.00 62.09           N  
ANISOU 3187  N   GLY A 222    12886   3547   7158    755  -1315    721       N  
ATOM   3188  CA  GLY A 222      36.872  11.475  38.612  1.00 63.82           C  
ANISOU 3188  CA  GLY A 222    13139   3702   7407    878  -1742    711       C  
ATOM   3189  C   GLY A 222      37.557  12.271  37.521  1.00 61.64           C  
ANISOU 3189  C   GLY A 222    12443   3512   7466    816  -1854    632       C  
ATOM   3190  O   GLY A 222      36.957  12.604  36.494  1.00 58.67           O  
ANISOU 3190  O   GLY A 222    11723   3257   7311    701  -1573    610       O  
ATOM   3191  H   GLY A 222      35.173  11.625  37.637  1.00 72.91           H  
ATOM   3192  HA2 GLY A 222      37.119  11.848  39.473  1.00 74.99           H  
ATOM   3193  HA3 GLY A 222      37.177  10.556  38.567  1.00 74.99           H  
ATOM   3194  N   THR A 223      38.832  12.573  37.755  1.00 63.57           N  
ANISOU 3194  N   THR A 223    12728   3677   7748    900  -2290    591       N  
ATOM   3195  CA  THR A 223      39.609  13.362  36.808  1.00 69.15           C  
ANISOU 3195  CA  THR A 223    13070   4424   8782    831  -2433    519       C  
ATOM   3196  C   THR A 223      41.087  13.018  36.952  1.00 66.23           C  
ANISOU 3196  C   THR A 223    12673   3960   8530    983  -2928    511       C  
ATOM   3197  O   THR A 223      41.530  12.500  37.980  1.00 81.12           O  
ANISOU 3197  O   THR A 223    14887   5746  10190   1146  -3233    539       O  
ATOM   3198  CB  THR A 223      39.373  14.866  37.005  1.00 79.17           C  
ANISOU 3198  CB  THR A 223    14399   5662  10020    688  -2460    415       C  
ATOM   3199  OG1 THR A 223      40.161  15.615  36.068  1.00 61.18           O  
ANISOU 3199  OG1 THR A 223    11767   3393   8084    598  -2584    359       O  
ATOM   3200  CG2 THR A 223      39.736  15.286  38.430  1.00 79.11           C  
ANISOU 3200  CG2 THR A 223    14881   5479   9698    751  -2843    352       C  
ATOM   3201  H   THR A 223      39.269  12.333  38.456  1.00 76.54           H  
ATOM   3202  HA  THR A 223      39.343  13.129  35.904  1.00 83.30           H  
ATOM   3203  HB  THR A 223      38.435  15.064  36.859  1.00 95.32           H  
ATOM   3204  HG1 THR A 223      39.979  15.375  35.284  1.00 71.82           H  
ATOM   3205 HG21 THR A 223      39.587  16.238  38.543  1.00 95.25           H  
ATOM   3206 HG22 THR A 223      39.187  14.804  39.068  1.00 95.25           H  
ATOM   3207 HG23 THR A 223      40.669  15.090  38.606  1.00 95.25           H  
ATOM   3208  N   GLY A 224      41.879  13.278  35.907  1.00 63.98           N  
ANISOU 3208  N   GLY A 224    11987   3711   8613    946  -3013    476       N  
ATOM   3209  CA  GLY A 224      43.328  13.045  35.928  1.00 66.67           C  
ANISOU 3209  CA  GLY A 224    12187   3975   9169   1101  -3495    459       C  
ATOM   3210  C   GLY A 224      44.015  13.661  34.735  1.00 65.47           C  
ANISOU 3210  C   GLY A 224    11578   3843   9454    992  -3527    407       C  
ATOM   3211  O   GLY A 224      43.306  14.072  33.838  1.00 65.16           O  
ANISOU 3211  O   GLY A 224    11357   3895   9507    813  -3139    404       O  
ATOM   3212  H   GLY A 224      41.566  13.577  35.101  1.00 75.19           H  
ATOM   3213  HA2 GLY A 224      43.707  13.429  36.757  1.00 78.41           H  
ATOM   3214  HA3 GLY A 224      43.494  12.078  35.935  1.00 78.41           H  
ATOM   3215  N   THR A 225      45.345  13.691  34.695  1.00 75.58           N  
ANISOU 3215  N   THR A 225    12651   5043  11022   1122  -4008    372       N  
ATOM   3216  CA  THR A 225      46.127  14.367  33.631  1.00 83.38           C  
ANISOU 3216  CA  THR A 225    13118   6117  12446    979  -4041    303       C  
ATOM   3217  C   THR A 225      46.467  13.422  32.488  1.00 87.24           C  
ANISOU 3217  C   THR A 225    13210   6727  13210   1119  -3871    357       C  
ATOM   3218  O   THR A 225      47.021  13.904  31.491  1.00 85.48           O  
ANISOU 3218  O   THR A 225    12518   6658  13301    978  -3748    312       O  
ATOM   3219  CB  THR A 225      47.406  14.972  34.226  1.00 82.50           C  
ANISOU 3219  CB  THR A 225    12758   6132  12456    928  -4520    157       C  
ATOM   3220  OG1 THR A 225      47.037  15.573  35.466  1.00 80.82           O  
ANISOU 3220  OG1 THR A 225    12976   5800  11933    847  -4741     79       O  
ATOM   3221  CG2 THR A 225      48.081  15.990  33.331  1.00 75.62           C  
ANISOU 3221  CG2 THR A 225    11342   5404  11986    652  -4426     67       C  
ATOM   3222  H   THR A 225      45.873  13.266  35.304  1.00 91.01           H  
ATOM   3223  HA  THR A 225      45.581  15.096  33.273  1.00100.38           H  
ATOM   3224  HB  THR A 225      48.040  14.237  34.404  1.00 99.32           H  
ATOM   3225  HG1 THR A 225      47.730  15.811  35.891  1.00 97.31           H  
ATOM   3226 HG21 THR A 225      48.687  16.539  33.860  1.00 91.06           H  
ATOM   3227 HG22 THR A 225      48.589  15.535  32.637  1.00 91.06           H  
ATOM   3228 HG23 THR A 225      47.409  16.563  32.920  1.00 91.06           H  
ATOM   3229  N   GLY A 226      46.144  12.136  32.600  1.00 75.80           N  
ANISOU 3229  N   GLY A 226    11933   5246  11622   1373  -3815    442       N  
ATOM   3230  CA  GLY A 226      46.546  11.150  31.584  1.00 86.76           C  
ANISOU 3230  CA  GLY A 226    12991   6729  13246   1531  -3650    467       C  
ATOM   3231  C   GLY A 226      45.696   9.908  31.592  1.00 67.17           C  
ANISOU 3231  C   GLY A 226    10768   4295  10460   1609  -3270    534       C  
ATOM   3232  O   GLY A 226      44.919   9.728  32.541  1.00 65.78           O  
ANISOU 3232  O   GLY A 226    10983   4081   9930   1581  -3206    577       O  
ATOM   3233  H   GLY A 226      45.694  11.793  33.312  1.00 91.28           H  
ATOM   3234  HA2 GLY A 226      46.488  11.569  30.688  1.00104.43           H  
ATOM   3235  HA3 GLY A 226      47.490  10.898  31.739  1.00104.43           H  
ATOM   3236  N   MET A 227      45.840   9.082  30.565  1.00 64.81           N  
ANISOU 3236  N   MET A 227    10237   4058  10331   1707  -3019    536       N  
ATOM   3237  CA  MET A 227      45.073   7.815  30.441  1.00 71.55           C  
ANISOU 3237  CA  MET A 227    11317   4901  10968   1776  -2697    591       C  
ATOM   3238  C   MET A 227      45.399   6.910  31.633  1.00 75.69           C  
ANISOU 3238  C   MET A 227    12129   5340  11289   1988  -2934    657       C  
ATOM   3239  O   MET A 227      44.505   6.167  32.051  1.00 74.46           O  
ANISOU 3239  O   MET A 227    12244   5126  10920   1982  -2682    727       O  
ATOM   3240  CB  MET A 227      45.391   7.118  29.119  1.00 75.16           C  
ANISOU 3240  CB  MET A 227    11538   5389  11629   1900  -2468    560       C  
ATOM   3241  CG  MET A 227      44.682   7.728  27.937  1.00 70.82           C  
ANISOU 3241  CG  MET A 227    10767   4923  11217   1723  -2144    505       C  
ATOM   3242  SD  MET A 227      42.914   7.351  27.870  1.00135.28           S  
ANISOU 3242  SD  MET A 227    19169  13132  19101   1422  -1723    530       S  
ATOM   3243  CE  MET A 227      42.931   5.634  27.357  1.00110.30           C  
ANISOU 3243  CE  MET A 227    16251   9871  15789   1508  -1482    564       C  
ATOM   3244  H   MET A 227      46.419   9.243  29.882  1.00 77.57           H  
ATOM   3245  HA  MET A 227      44.113   8.035  30.472  1.00 86.18           H  
ATOM   3246  HB2 MET A 227      46.356   7.149  28.965  1.00 90.51           H  
ATOM   3247  HB3 MET A 227      45.135   6.179  29.193  1.00 90.51           H  
ATOM   3248  HG2 MET A 227      44.785   8.699  27.981  1.00 85.30           H  
ATOM   3249  HG3 MET A 227      45.107   7.417  27.110  1.00 85.30           H  
ATOM   3250  HE1 MET A 227      43.558   5.520  26.631  1.00132.68           H  
ATOM   3251  HE2 MET A 227      43.194   5.080  28.101  1.00132.68           H  
ATOM   3252  HE3 MET A 227      42.047   5.379  27.065  1.00132.68           H  
ATOM   3253  N   ALA A 228      46.599   7.003  32.204  1.00 71.10           N  
ANISOU 3253  N   ALA A 228    11469   4752  10794   2188  -3420    642       N  
ATOM   3254  CA  ALA A 228      46.994   6.214  33.390  1.00 74.88           C  
ANISOU 3254  CA  ALA A 228    12215   5168  11067   2438  -3653    716       C  
ATOM   3255  C   ALA A 228      46.050   6.505  34.552  1.00 79.19           C  
ANISOU 3255  C   ALA A 228    13254   5633  11200   2311  -3626    780       C  
ATOM   3256  O   ALA A 228      45.607   5.538  35.206  1.00 76.51           O  
ANISOU 3256  O   ALA A 228    13243   5208  10618   2408  -3516    883       O  
ATOM   3257  CB  ALA A 228      48.400   6.557  33.789  1.00 78.85           C  
ANISOU 3257  CB  ALA A 228    12452   5741  11765   2673  -4216    660       C  
ATOM   3258  H   ALA A 228      47.268   7.535  31.894  1.00 84.25           H  
ATOM   3259  HA  ALA A 228      46.943   5.254  33.168  1.00 88.26           H  
ATOM   3260  HB1 ALA A 228      48.647   6.045  34.576  1.00 93.03           H  
ATOM   3261  HB2 ALA A 228      49.007   6.342  33.061  1.00 93.03           H  
ATOM   3262  HB3 ALA A 228      48.460   7.506  33.991  1.00 93.03           H  
ATOM   3263  N   ASP A 229      45.711   7.765  34.775  1.00 73.74           N  
ANISOU 3263  N   ASP A 229    12619   4952  10447   2113  -3762    717       N  
ATOM   3264  CA  ASP A 229      44.826   8.165  35.894  1.00 77.06           C  
ANISOU 3264  CA  ASP A 229    13441   5323  10517   1931  -3622    739       C  
ATOM   3265  C   ASP A 229      43.453   7.527  35.679  1.00 70.09           C  
ANISOU 3265  C   ASP A 229    12699   4442   9489   1787  -3064    808       C  
ATOM   3266  O   ASP A 229      42.822   7.158  36.674  1.00 71.23           O  
ANISOU 3266  O   ASP A 229    13225   4521   9317   1780  -2985    875       O  
ATOM   3267  CB  ASP A 229      44.788   9.687  36.041  1.00 82.05           C  
ANISOU 3267  CB  ASP A 229    13924   5970  11282   1722  -3745    633       C  
ATOM   3268  CG  ASP A 229      46.131  10.318  36.364  1.00 93.10           C  
ANISOU 3268  CG  ASP A 229    15328   7314  12733   1838  -4377    564       C  
ATOM   3269  OD1 ASP A 229      46.244  10.910  37.450  1.00104.38           O  
ANISOU 3269  OD1 ASP A 229    17122   8689  13848   1986  -4687    585       O  
ATOM   3270  OD2 ASP A 229      47.044  10.224  35.521  1.00 96.06           O  
ANISOU 3270  OD2 ASP A 229    15254   7732  13511   1910  -4637    510       O  
ATOM   3271  H   ASP A 229      45.975   8.451  34.237  1.00 86.90           H  
ATOM   3272  HA  ASP A 229      45.207   7.796  36.724  1.00 92.80           H  
ATOM   3273  HB2 ASP A 229      44.458  10.076  35.205  1.00 98.78           H  
ATOM   3274  HB3 ASP A 229      44.159   9.918  36.755  1.00 98.78           H  
ATOM   3275  N   LEU A 230      42.988   7.429  34.436  1.00 67.10           N  
ANISOU 3275  N   LEU A 230    12028   4133   9336   1686  -2703    791       N  
ATOM   3276  CA  LEU A 230      41.683   6.787  34.123  1.00 72.71           C  
ANISOU 3276  CA  LEU A 230    12822   4845   9958   1549  -2238    837       C  
ATOM   3277  C   LEU A 230      41.727   5.306  34.502  1.00 68.72           C  
ANISOU 3277  C   LEU A 230    12513   4217   9378   1713  -2186    937       C  
ATOM   3278  O   LEU A 230      40.777   4.856  35.141  1.00 79.23           O  
ANISOU 3278  O   LEU A 230    14099   5482  10523   1631  -1962   1005       O  
ATOM   3279  CB  LEU A 230      41.350   6.951  32.637  1.00 61.77           C  
ANISOU 3279  CB  LEU A 230    11075   3562   8832   1423  -1951    771       C  
ATOM   3280  CG  LEU A 230      40.181   6.122  32.104  1.00 65.64           C  
ANISOU 3280  CG  LEU A 230    11562   4043   9335   1321  -1539    792       C  
ATOM   3281  CD1 LEU A 230      38.860   6.549  32.723  1.00 59.02           C  
ANISOU 3281  CD1 LEU A 230    10892   3229   8303   1132  -1322    809       C  
ATOM   3282  CD2 LEU A 230      40.115   6.211  30.594  1.00 57.76           C  
ANISOU 3282  CD2 LEU A 230    10239   3128   8578   1253  -1322    715       C  
ATOM   3283  H   LEU A 230      43.435   7.756  33.713  1.00 78.93           H  
ATOM   3284  HA  LEU A 230      40.987   7.229  34.663  1.00 87.57           H  
ATOM   3285  HB2 LEU A 230      41.156   7.895  32.472  1.00 72.53           H  
ATOM   3286  HB3 LEU A 230      42.140   6.722  32.115  1.00 72.53           H  
ATOM   3287  HG  LEU A 230      40.337   5.178  32.336  1.00 79.09           H  
ATOM   3288 HD11 LEU A 230      38.137   6.019  32.343  1.00 69.23           H  
ATOM   3289 HD12 LEU A 230      38.887   6.411  33.685  1.00 69.23           H  
ATOM   3290 HD13 LEU A 230      38.702   7.489  32.535  1.00 69.23           H  
ATOM   3291 HD21 LEU A 230      39.379   5.663  30.269  1.00 67.71           H  
ATOM   3292 HD22 LEU A 230      39.974   7.135  30.330  1.00 67.71           H  
ATOM   3293 HD23 LEU A 230      40.949   5.888  30.211  1.00 67.71           H  
ATOM   3294  N   LEU A 231      42.804   4.591  34.180  1.00 70.31           N  
ANISOU 3294  N   LEU A 231    12591   4376   9745   1950  -2382    948       N  
ATOM   3295  CA  LEU A 231      42.869   3.124  34.428  1.00 72.66           C  
ANISOU 3295  CA  LEU A 231    13077   4529  10000   2118  -2314   1050       C  
ATOM   3296  C   LEU A 231      42.750   2.906  35.933  1.00 75.98           C  
ANISOU 3296  C   LEU A 231    13942   4846  10080   2209  -2487   1163       C  
ATOM   3297  O   LEU A 231      42.004   2.009  36.312  1.00 77.48           O  
ANISOU 3297  O   LEU A 231    14397   4899  10141   2204  -2282   1268       O  
ATOM   3298  CB  LEU A 231      44.157   2.534  33.853  1.00 74.90           C  
ANISOU 3298  CB  LEU A 231    13134   4799  10524   2399  -2521   1032       C  
ATOM   3299  CG  LEU A 231      44.343   2.647  32.338  1.00 79.58           C  
ANISOU 3299  CG  LEU A 231    13342   5461  11433   2362  -2315    927       C  
ATOM   3300  CD1 LEU A 231      45.735   2.195  31.927  1.00 78.52           C  
ANISOU 3300  CD1 LEU A 231    12962   5346  11527   2681  -2589    893       C  
ATOM   3301  CD2 LEU A 231      43.286   1.863  31.580  1.00 79.55           C  
ANISOU 3301  CD2 LEU A 231    13401   5353  11470   2235  -1889    938       C  
ATOM   3302  H   LEU A 231      43.562   4.960  33.839  1.00 84.69           H  
ATOM   3303  HA  LEU A 231      42.094   2.704  33.994  1.00 86.42           H  
ATOM   3304  HB2 LEU A 231      44.914   2.972  34.289  1.00 88.28           H  
ATOM   3305  HB3 LEU A 231      44.191   1.587  34.096  1.00 88.28           H  
ATOM   3306  HG  LEU A 231      44.249   3.596  32.087  1.00 95.81           H  
ATOM   3307 HD11 LEU A 231      45.834   2.278  30.963  1.00 94.55           H  
ATOM   3308 HD12 LEU A 231      46.400   2.751  32.369  1.00 94.55           H  
ATOM   3309 HD13 LEU A 231      45.865   1.266  32.187  1.00 94.55           H  
ATOM   3310 HD21 LEU A 231      43.511   1.852  30.634  1.00 95.77           H  
ATOM   3311 HD22 LEU A 231      43.252   0.951  31.915  1.00 95.77           H  
ATOM   3312 HD23 LEU A 231      42.418   2.284  31.699  1.00 95.77           H  
ATOM   3313  N   ALA A 232      43.404   3.732  36.747  1.00 85.73           N  
ANISOU 3313  N   ALA A 232    15281   6130  11165   2292  -2882   1137       N  
ATOM   3314  CA  ALA A 232      43.341   3.657  38.223  1.00 80.95           C  
ANISOU 3314  CA  ALA A 232    15142   5434  10180   2383  -3062   1228       C  
ATOM   3315  C   ALA A 232      41.935   3.949  38.732  1.00 79.17           C  
ANISOU 3315  C   ALA A 232    15186   5178   9716   2132  -2704   1257       C  
ATOM   3316  O   ALA A 232      41.520   3.267  39.671  1.00 81.53           O  
ANISOU 3316  O   ALA A 232    15847   5350   9778   2164  -2567   1378       O  
ATOM   3317  CB  ALA A 232      44.336   4.616  38.813  1.00 82.96           C  
ANISOU 3317  CB  ALA A 232    15433   5754  10336   2497  -3588   1152       C  
ATOM   3318  H   ALA A 232      43.923   4.421  36.451  1.00103.20           H  
ATOM   3319  HA  ALA A 232      43.585   2.742  38.497  1.00 95.54           H  
ATOM   3320  HB1 ALA A 232      44.319   4.545  39.782  1.00 97.96           H  
ATOM   3321  HB2 ALA A 232      45.227   4.401  38.490  1.00 97.96           H  
ATOM   3322  HB3 ALA A 232      44.109   5.525  38.553  1.00 97.96           H  
ATOM   3323  N   PHE A 233      41.239   4.934  38.168  1.00 75.35           N  
ANISOU 3323  N   PHE A 233    14520   4807   9301   1889  -2543   1150       N  
ATOM   3324  CA  PHE A 233      39.870   5.338  38.597  1.00 73.72           C  
ANISOU 3324  CA  PHE A 233    14503   4602   8907   1667  -2197   1160       C  
ATOM   3325  C   PHE A 233      38.943   4.156  38.356  1.00 82.76           C  
ANISOU 3325  C   PHE A 233    15647   5671  10127   1586  -1795   1242       C  
ATOM   3326  O   PHE A 233      38.025   3.941  39.152  1.00 86.52           O  
ANISOU 3326  O   PHE A 233    16401   6084  10388   1481  -1562   1300       O  
ATOM   3327  CB  PHE A 233      39.396   6.593  37.852  1.00 69.74           C  
ANISOU 3327  CB  PHE A 233    13715   4244   8540   1452  -2078   1032       C  
ATOM   3328  CG  PHE A 233      37.906   6.819  37.842  1.00 67.60           C  
ANISOU 3328  CG  PHE A 233    13478   4010   8196   1236  -1663   1028       C  
ATOM   3329  CD1 PHE A 233      37.261   7.348  38.945  1.00 68.77           C  
ANISOU 3329  CD1 PHE A 233    14000   4120   8011   1187  -1625   1036       C  
ATOM   3330  CD2 PHE A 233      37.153   6.521  36.720  1.00 64.79           C  
ANISOU 3330  CD2 PHE A 233    12791   3723   8103   1100  -1332   1005       C  
ATOM   3331  CE1 PHE A 233      35.894   7.562  38.931  1.00 67.20           C  
ANISOU 3331  CE1 PHE A 233    13816   3957   7761   1012  -1250   1029       C  
ATOM   3332  CE2 PHE A 233      35.786   6.733  36.709  1.00 63.26           C  
ANISOU 3332  CE2 PHE A 233    12604   3568   7864    920  -1002    993       C  
ATOM   3333  CZ  PHE A 233      35.159   7.252  37.814  1.00 75.50           C  
ANISOU 3333  CZ  PHE A 233    14501   5085   9100    879   -953   1008       C  
ATOM   3334  H   PHE A 233      41.558   5.435  37.478  1.00 88.82           H  
ATOM   3335  HA  PHE A 233      39.886   5.532  39.568  1.00 86.87           H  
ATOM   3336  HB2 PHE A 233      39.827   7.372  38.260  1.00 82.10           H  
ATOM   3337  HB3 PHE A 233      39.705   6.540  36.924  1.00 82.10           H  
ATOM   3338  HD1 PHE A 233      37.760   7.562  39.717  1.00 80.93           H  
ATOM   3339  HD2 PHE A 233      37.575   6.160  35.956  1.00 76.15           H  
ATOM   3340  HE1 PHE A 233      35.466   7.921  39.692  1.00 79.05           H  
ATOM   3341  HE2 PHE A 233      35.283   6.521  35.939  1.00 76.00           H  
ATOM   3342  HZ  PHE A 233      34.226   7.401  37.804  1.00 90.92           H  
ATOM   3343  N   LEU A 234      39.172   3.433  37.270  1.00 73.75           N  
ANISOU 3343  N   LEU A 234    14212   4515   9292   1632  -1715   1237       N  
ATOM   3344  CA  LEU A 234      38.342   2.269  36.893  1.00 76.38           C  
ANISOU 3344  CA  LEU A 234    14551   4738   9731   1546  -1381   1291       C  
ATOM   3345  C   LEU A 234      38.701   1.067  37.784  1.00 77.46           C  
ANISOU 3345  C   LEU A 234    15052   4661   9718   1733  -1450   1444       C  
ATOM   3346  O   LEU A 234      37.769   0.312  38.092  1.00 80.96           O  
ANISOU 3346  O   LEU A 234    15683   4963  10115   1633  -1185   1521       O  
ATOM   3347  CB  LEU A 234      38.558   1.960  35.410  1.00 70.54           C  
ANISOU 3347  CB  LEU A 234    13390   4044   9367   1519  -1265   1200       C  
ATOM   3348  CG  LEU A 234      38.084   3.011  34.405  1.00 66.19           C  
ANISOU 3348  CG  LEU A 234    12488   3687   8974   1322  -1123   1066       C  
ATOM   3349  CD1 LEU A 234      38.828   2.859  33.090  1.00 67.79           C  
ANISOU 3349  CD1 LEU A 234    12328   3944   9484   1386  -1134    976       C  
ATOM   3350  CD2 LEU A 234      36.585   2.923  34.174  1.00 73.85           C  
ANISOU 3350  CD2 LEU A 234    13454   4665   9940   1082   -788   1045       C  
ATOM   3351  H   LEU A 234      39.866   3.598  36.704  1.00 88.81           H  
ATOM   3352  HA  LEU A 234      37.397   2.499  37.043  1.00 91.97           H  
ATOM   3353  HB2 LEU A 234      39.512   1.806  35.266  1.00 83.05           H  
ATOM   3354  HB3 LEU A 234      38.099   1.120  35.209  1.00 83.05           H  
ATOM   3355  HG  LEU A 234      38.285   3.906  34.771  1.00 77.84           H  
ATOM   3356 HD11 LEU A 234      38.460   3.476  32.434  1.00 81.66           H  
ATOM   3357 HD12 LEU A 234      39.771   3.053  33.224  1.00 81.66           H  
ATOM   3358 HD13 LEU A 234      38.729   1.947  32.766  1.00 81.66           H  
ATOM   3359 HD21 LEU A 234      36.313   3.615  33.547  1.00 88.94           H  
ATOM   3360 HD22 LEU A 234      36.363   2.051  33.807  1.00 88.94           H  
ATOM   3361 HD23 LEU A 234      36.116   3.049  35.017  1.00 88.94           H  
ATOM   3362  N   ALA A 235      39.966   0.894  38.209  1.00 83.29           N  
ANISOU 3362  N   ALA A 235    15896   5366  10386   2008  -1815   1493       N  
ATOM   3363  CA  ALA A 235      40.316  -0.268  39.017  1.00 86.18           C  
ANISOU 3363  CA  ALA A 235    16612   5527  10604   2226  -1902   1654       C  
ATOM   3364  C   ALA A 235      39.648  -0.226  40.385  1.00 88.22           C  
ANISOU 3364  C   ALA A 235    17372   5699  10447   2193  -1857   1767       C  
ATOM   3365  O   ALA A 235      39.429  -1.277  40.998  1.00102.26           O  
ANISOU 3365  O   ALA A 235    19483   7275  12095   2275  -1760   1922       O  
ATOM   3366  CB  ALA A 235      41.833  -0.362  39.175  1.00 88.16           C  
ANISOU 3366  CB  ALA A 235    16813   5796  10887   2562  -2344   1668       C  
ATOM   3367  H   ALA A 235      40.609   1.451  38.082  1.00100.27           H  
ATOM   3368  HA  ALA A 235      40.010  -1.067  38.559  1.00103.73           H  
ATOM   3369  HB1 ALA A 235      42.048  -1.140  39.712  1.00104.20           H  
ATOM   3370  HB2 ALA A 235      42.238  -0.444  38.297  1.00104.20           H  
ATOM   3371  HB3 ALA A 235      42.155   0.442  39.613  1.00104.20           H  
ATOM   3372  N   ALA A 236      39.324   0.965  40.879  1.00 95.18           N  
ANISOU 3372  N   ALA A 236    18342   6710  11113   2081  -1914   1694       N  
ATOM   3373  CA  ALA A 236      38.669   1.110  42.174  1.00100.72           C  
ANISOU 3373  CA  ALA A 236    19544   7334  11390   2056  -1850   1780       C  
ATOM   3374  C   ALA A 236      37.164   1.285  41.995  1.00101.00           C  
ANISOU 3374  C   ALA A 236    19574   7379  11422   1751  -1391   1754       C  
ATOM   3375  O   ALA A 236      36.526   0.542  41.250  1.00 98.71           O  
ANISOU 3375  O   ALA A 236    19094   7030  11382   1613  -1094   1767       O  
ATOM   3376  CB  ALA A 236      39.254   2.291  42.938  1.00101.13           C  
ANISOU 3376  CB  ALA A 236    19764   7489  11172   2149  -2219   1701       C  
ATOM   3377  H   ALA A 236      39.473   1.712  40.479  1.00114.54           H  
ATOM   3378  HA  ALA A 236      38.824   0.311  42.701  1.00121.18           H  
ATOM   3379  HB1 ALA A 236      38.802   2.370  43.792  1.00121.67           H  
ATOM   3380  HB2 ALA A 236      40.202   2.138  43.078  1.00121.67           H  
ATOM   3381  HB3 ALA A 236      39.123   3.099  42.418  1.00121.67           H  
TER    3382      ALA A 236                                                                                            
HETATM10131  O   HOH S   1      42.025  40.124  14.732  1.00 37.49           O  
HETATM10132  O   HOH S   2      32.415  13.128   6.909  1.00 49.86           O  
HETATM10133  O   HOH S   3      18.340  21.090  13.953  1.00 62.13           O  
HETATM10134  O   HOH S   4      48.829  23.961  20.520  1.00 49.24           O  
HETATM10135  O   HOH S   5      58.905  15.493  30.372  1.00 55.85           O  
HETATM10136  O   HOH S   6      25.896   5.706  15.750  1.00 43.26           O  
HETATM10137  O   HOH S   7      14.763  25.684  11.844  1.00 62.17           O  
HETATM10138  O   HOH S   8      47.777 -15.298  20.426  1.00 32.97           O  
HETATM10139  O   HOH S   9      62.106  34.796  14.405  1.00 42.58           O  
HETATM10140  O   HOH S  10      30.175  23.313  39.237  1.00 57.20           O  
HETATM10141  O   HOH S  11      55.546  -9.192  36.520  1.00 48.05           O  
HETATM10142  O   HOH S  12      85.117  24.948   9.719  1.00 38.17           O  
HETATM10143  O   HOH S  13      30.016  21.709  36.966  1.00 60.79           O  
HETATM10144  O   HOH S  14      42.171  12.988  12.478  1.00 50.31           O  
HETATM10145  O   HOH S  15      54.219 -15.958  23.479  1.00 46.08           O  
HETATM10146  O   HOH S  16      51.156  21.297  16.489  1.00 51.96           O  
HETATM10147  O   HOH S  17      36.805  32.178   4.982  1.00 33.90           O  
HETATM10148  O   HOH S  18      61.097  -8.229   9.597  1.00 49.90           O  
HETATM10149  O   HOH S  19      39.387  27.113  20.719  1.00 40.01           O  
HETATM10150  O   HOH S  20      61.959  20.427  38.704  1.00 61.02           O  
HETATM10151  O   HOH S  21      54.410  -7.635  21.483  1.00 45.79           O  
HETATM10152  O   HOH S  22      38.603  33.508   2.832  1.00 45.83           O  
HETATM10153  O   HOH S  23      91.026  19.621  18.116  1.00 55.42           O  
HETATM10154  O   HOH S  24      52.595  -4.530   1.449  1.00 49.64           O  
HETATM10155  O   HOH S  25      86.949  31.626   7.547  1.00 58.02           O  
HETATM10156  O   HOH S  26      80.268  13.663  20.877  1.00 44.62           O  
HETATM10157  O   HOH S  27      60.275 -14.714  22.505  1.00 47.19           O  
HETATM10158  O   HOH S  28      63.049  -2.717  38.418  1.00 68.64           O  
HETATM10159  O   HOH S  29      33.129  14.914  19.322  1.00 39.62           O  
HETATM10160  O   HOH S  30      47.153  10.290  13.046  1.00 59.98           O  
HETATM10161  O   HOH S  31      62.482   2.290  17.704  1.00 53.16           O  
HETATM10162  O   HOH S  32      64.983 -18.112  12.151  1.00 44.01           O  
HETATM10163  O   HOH S  33      83.071  -2.889   8.879  1.00 57.56           O  
HETATM10164  O   HOH S  34      85.281  -3.805   7.082  1.00 62.72           O  
HETATM10165  O   HOH S  35      34.532  13.772  19.042  1.00 34.09           O  
HETATM10166  O   HOH S  36      37.229  23.929  31.839  1.00 39.54           O  
HETATM10167  O   HOH S  37      41.851  32.770  17.975  1.00 35.54           O  
HETATM10168  O   HOH S  38      33.006  27.563  21.412  1.00 49.26           O  
HETATM10169  O   HOH S  39      49.795  19.042  26.356  1.00 52.88           O  
HETATM10170  O   HOH S  40      27.524  25.575   9.548  1.00 46.73           O  
HETATM10171  O   HOH S  41      23.144   0.408  32.455  1.00 61.61           O  
HETATM10172  O   HOH S  42      83.287   8.106  21.017  1.00 54.67           O  
HETATM10173  O   HOH S  43      52.387  22.731   4.963  1.00 49.55           O  
HETATM10174  O   HOH S  44      81.779 -11.667  16.190  1.00 55.78           O  
HETATM10175  O   HOH S  45      53.860  24.892   3.201  1.00 57.30           O  
HETATM10176  O   HOH S  46      49.602  17.046  25.490  1.00 59.43           O  
HETATM10177  O   HOH S  47      34.602  -8.709   7.600  1.00 55.05           O  
HETATM10178  O   HOH S  48      52.105 -15.209  31.459  1.00 43.92           O  
HETATM10179  O   HOH S  49      28.005  14.327  12.351  1.00 43.19           O  
HETATM10180  O   HOH S  50      68.092   1.671  12.778  1.00 67.01           O  
HETATM10181  O   HOH S  51      30.522  -4.920  18.815  1.00 53.49           O  
HETATM10182  O   HOH S  52      41.670 -15.311  20.927  1.00 38.42           O  
HETATM10183  O   HOH S  53      37.301  22.130  -0.746  1.00 64.04           O  
HETATM10184  O   HOH S  54      41.105  18.480  36.477  1.00 51.20           O  
HETATM10185  O   HOH S  55      60.589   7.123  22.234  1.00 53.13           O  
HETATM10186  O   HOH S  56      80.788  40.662  12.154  1.00 57.81           O  
HETATM10187  O   HOH S  57      74.694  40.645  19.250  1.00 48.54           O  
HETATM10188  O   HOH S  58      39.242   0.499  11.376  1.00 44.97           O  
HETATM10189  O   HOH S  59      50.022  21.169   4.987  1.00 51.60           O  
HETATM10190  O   HOH S  60      51.268  35.485   6.733  1.00 49.90           O  
HETATM10191  O   HOH S  61      41.905 -16.117  18.659  1.00 41.81           O  
HETATM10192  O   HOH S  62      38.306  -0.827  13.656  1.00 42.92           O  
HETATM10193  O   HOH S  63      78.664   4.805  28.227  1.00 72.67           O  
HETATM10194  O   HOH S  64      49.358  19.887  11.286  1.00 47.16           O  
HETATM10195  O   HOH S  65      72.082  41.443  20.315  1.00 53.96           O  
HETATM10196  O   HOH S  66      76.078  -2.983  43.168  1.00 57.84           O  
HETATM10197  O   HOH S  67      76.624  -4.104  41.522  1.00 66.51           O  
HETATM10198  O   HOH S  68      32.993  -2.670  37.144  1.00 75.46           O  
HETATM10199  O   HOH S  69      45.623  39.851  11.404  1.00 49.52           O  
HETATM10200  O   HOH S  70      41.197  -9.925  27.091  1.00 60.24           O  
HETATM10201  O   HOH S  71      91.252   8.679  19.565  1.00 55.03           O  
HETATM10202  O   HOH S  72      76.118 -16.880  19.928  1.00 62.95           O  
HETATM10203  O   HOH S  73      41.216  40.652  13.317  1.00 51.63           O  
HETATM10204  O   HOH S  74      69.815 -10.942   1.261  1.00 56.26           O  
HETATM10205  O   HOH S  75      42.664 -12.265  -0.867  1.00 49.99           O  
HETATM10206  O   HOH S  76      72.525  25.201  19.421  1.00 41.92           O  
HETATM10207  O   HOH S  77      70.899  24.336  18.866  1.00 41.51           O  
HETATM10208  O   HOH S  78      38.496  -7.589  15.754  1.00 51.31           O  
HETATM10209  O   HOH S  79      22.687   0.486  18.400  1.00 49.35           O  
HETATM10210  O   HOH S  80      21.095  10.557   9.806  1.00 54.38           O  
HETATM10211  O   HOH S  81      74.454  40.765  17.180  1.00 49.17           O  
HETATM10212  O   HOH S  82      61.751  40.091  20.887  1.00 64.04           O  
HETATM10213  O   HOH S  83      84.249  -1.962   8.316  1.00 61.01           O  
HETATM10214  O   HOH S  84      68.006  21.104   9.924  1.00 47.18           O  
HETATM10215  O   HOH S  85      63.517   4.821  29.140  1.00 54.99           O  
HETATM10216  O   HOH S  86      48.615   0.084  14.861  1.00 50.07           O  
HETATM10217  O   HOH S  87      41.995 -17.188  23.267  1.00 45.48           O  
HETATM10218  O   HOH S  88      32.794   4.216  10.905  1.00 42.69           O  
HETATM10219  O   HOH S  89      52.003   1.253   6.993  1.00 67.10           O  
HETATM10220  O   HOH S  90      73.220 -26.477  24.699  1.00 44.86           O  
HETATM10221  O   HOH S  91      52.228  18.943  14.577  1.00 46.56           O  
HETATM10222  O   HOH S  92      14.410  14.477  21.567  1.00 61.53           O  
HETATM10223  O   HOH S  93      61.432  33.977   6.306  1.00 49.54           O  
HETATM10224  O   HOH S  94      19.042  -1.965  21.953  1.00 61.83           O  
HETATM10225  O   HOH S  95      54.935  35.994  14.652  1.00 58.66           O  
HETATM10226  O   HOH S  96      68.206 -18.980  41.498  1.00 52.62           O  
HETATM10227  O   HOH S  97      77.824  18.687  27.292  1.00 52.01           O  
HETATM10228  O   HOH S  98      32.651 -16.488   3.852  1.00 47.82           O  
HETATM10229  O   HOH S  99      42.336 -22.906  16.195  1.00 47.63           O  
HETATM10230  O   HOH S 100      23.540   3.646  18.675  1.00 53.92           O  
HETATM10231  O   HOH S 101      49.273  34.792   5.880  1.00 46.49           O  
HETATM10232  O   HOH S 102      46.620   9.302  42.324  1.00 57.56           O  
HETATM10233  O   HOH S 103      51.969  37.363  14.828  1.00 53.77           O  
HETATM10234  O   HOH S 104      74.203 -31.588  17.767  1.00 59.53           O  
HETATM10235  O   HOH S 105      64.028 -31.782   2.816  1.00 58.56           O  
HETATM10236  O   HOH S 106      54.367  16.355   7.839  1.00 45.56           O  
HETATM10237  O   HOH S 107      53.103   2.696  28.745  1.00 48.02           O  
HETATM10238  O   HOH S 108      46.759  -8.201  19.214  1.00 45.41           O  
HETATM10239  O   HOH S 109      91.654  11.135  19.748  1.00 56.02           O  
HETATM10240  O   HOH S 110      41.523  22.683  21.422  1.00 60.94           O  
HETATM10241  O   HOH S 111      90.591   1.923   1.912  1.00 68.38           O  
HETATM10242  O   HOH S 112      40.801  23.501  24.185  1.00 52.94           O  
HETATM10243  O   HOH S 113      66.521  15.151  -2.835  1.00 50.04           O  
HETATM10244  O   HOH S 114      69.312  20.408   1.485  1.00 56.91           O  
HETATM10245  O   HOH S 115      31.003  19.466  -0.993  1.00 55.46           O  
HETATM10246  O   HOH S 116      15.606  14.207  24.897  1.00 56.02           O  
HETATM10247  O   HOH S 117      65.975  48.185  32.624  1.00 60.69           O  
HETATM10248  O   HOH S 118      14.920  13.207  23.073  1.00 57.67           O  
HETATM10249  O   HOH S 119      24.203   4.233  17.387  1.00 50.30           O  
HETATM10250  O   HOH S 120      44.201  25.090  18.195  1.00 43.87           O  
HETATM10251  O   HOH S 121      72.445 -34.429  22.340  1.00 44.25           O  
HETATM10252  O   HOH S 122      57.668  -4.693  -1.404  1.00 53.81           O  
HETATM10253  O   HOH S 123      56.052  34.450  10.935  1.00 47.13           O  
HETATM10254  O   HOH S 124      83.150 -26.443  25.197  1.00 54.32           O  
HETATM10255  O   HOH S 125      80.319  -2.770  27.027  1.00 76.91           O  
HETATM10256  O   HOH S 126      60.593  34.992   3.359  1.00 55.22           O  
HETATM10257  O   HOH S 127      11.540  13.450  22.869  1.00 65.40           O  
HETATM10258  O   HOH S 128      80.494   6.622   0.301  1.00 59.38           O  
HETATM10259  O   HOH S 129      39.249 -23.303  19.467  1.00 46.94           O  
HETATM10260  O   HOH S 130      77.323 -33.965  21.393  1.00 52.96           O  
HETATM10261  O   HOH S 131      42.117  23.511  18.337  1.00 37.40           O  
HETATM10262  O   HOH S 132      48.009  32.331  26.338  1.00 53.62           O  
HETATM10263  O   HOH S 133      81.771 -36.474  23.911  1.00 50.57           O  
HETATM10264  O   HOH S 134      40.538  35.832  17.723  1.00 54.01           O  
HETATM10265  O   HOH S 135      46.045  -5.317  20.638  1.00 53.80           O  
HETATM10266  O   HOH S 136      42.804  32.521  20.685  1.00 42.97           O  
HETATM10267  O   HOH S 137      65.991 -24.039  28.866  1.00 54.37           O  
HETATM10268  O   HOH S 138      65.955  12.886  -1.792  1.00 64.98           O  
HETATM10269  O   HOH S 139      29.435  -4.552  20.936  1.00 50.74           O  
HETATM10270  O   HOH S 140      61.923  13.041   2.276  1.00 43.63           O  
HETATM10271  O   HOH S 141      79.468 -15.973  18.491  1.00 52.44           O  
HETATM10272  O   HOH S 142      49.025  -3.082  11.460  1.00 46.13           O  
HETATM10273  O   HOH S 143      84.593 -25.308  24.215  1.00 53.37           O  
HETATM10274  O   HOH S 144      79.757 -36.189  13.265  1.00 50.89           O  
HETATM10275  O   HOH S 145      75.877  13.682  15.522  1.00 47.90           O  
HETATM10276  O   HOH S 146      60.985  29.983   1.549  1.00 55.06           O  
HETATM10277  O   HOH S 147      48.885   5.923  21.112  1.00 56.15           O  
HETATM10278  O   HOH S 148      37.999 -10.377  16.540  1.00 46.16           O  
HETATM10279  O   HOH S 149      39.989  -1.420  36.007  1.00 52.49           O  
HETATM10280  O   HOH S 150      32.310   4.224   9.299  1.00 62.17           O  
HETATM10281  O   HOH S 151      76.763  16.374  -6.254  1.00 56.05           O  
HETATM10282  O   HOH S 152      20.748   4.125  18.794  1.00 49.71           O  
HETATM10283  O   HOH S 153      77.624 -34.288  24.910  1.00 61.22           O  
HETATM10284  O   HOH S 154      51.742  11.809  36.905  1.00 51.14           O  
HETATM10285  O   HOH S 155      62.126   5.845  28.881  1.00 67.91           O  
HETATM10286  O   HOH S 156      75.458  36.497   9.193  1.00 52.43           O  
HETATM10287  O   HOH S 157      80.485 -12.089  20.868  1.00 64.52           O  
HETATM10288  O   HOH S 158      16.475  11.266  24.035  1.00 52.75           O  
HETATM10289  O   HOH S 159      58.852  33.770  39.134  1.00 68.13           O  
HETATM10290  O   HOH S 160      32.810 -18.612   0.846  1.00 54.88           O  
HETATM10291  O   HOH S 161      77.876 -38.421  10.913  1.00 59.99           O  
HETATM10292  O   HOH S 162      85.171 -29.914  28.811  1.00 66.47           O  
HETATM10293  O   HOH S 163      11.555  10.712  22.973  1.00 68.35           O  
HETATM10294  O   HOH S 164      86.200 -33.782  22.419  1.00 62.16           O  
HETATM10295  O   HOH S 165      81.184 -38.064  18.589  1.00 61.23           O  
HETATM10296  O   HOH S 166      75.193  23.933  19.854  1.00 49.39           O  
HETATM10297  O   HOH S 167      87.342 -28.757  31.457  1.00 46.34           O  
HETATM10298  O   HOH S 168      70.966  14.697  28.061  1.00 60.82           O  
HETATM10299  O   HOH S 169      29.194   0.764  15.636  1.00 50.66           O  
HETATM10300  O   HOH S 170      80.223 -38.090  22.291  1.00 56.73           O  
HETATM10301  O   HOH S 171      76.002 -33.666  10.310  1.00 60.64           O  
HETATM10302  O   HOH S 172      76.348 -39.245  24.747  1.00 57.74           O  
HETATM10303  O   HOH S 173      58.605  33.013  37.424  1.00 67.15           O  
HETATM10304  O   HOH S 174      55.365  -1.019  -0.248  1.00 56.87           O  
HETATM10305  O   HOH S 175      72.345 -17.666   9.543  1.00 54.24           O  
HETATM10306  O   HOH S 176      81.004 -41.409  14.014  1.00 61.59           O  
HETATM10307  O   HOH S 177      37.750  -6.005  35.656  1.00 51.45           O  
HETATM10308  O   HOH S 178      51.039  -6.904  -1.954  1.00 51.75           O  
HETATM10309  O   HOH S 179      78.395  15.873  43.737  1.00 61.39           O  
HETATM10310  O   HOH S 180      80.352 -31.608  30.656  1.00 64.40           O  
HETATM10311  O   HOH S 181      74.692 -23.711  32.024  1.00 57.24           O  
HETATM10312  O   HOH S 182      78.447  17.170  40.894  1.00 57.42           O  
HETATM10313  O   HOH S 183      76.651 -35.249  25.067  1.00 65.98           O  
END



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