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***    ***

elNémo ID: 200115093526128829

Job options:

ID        	=	 200115093526128829
JOBID     	=	 
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:


REMARK Date 2015-09-03 Time 11:44:17 W. Europe Daylight Time +0200 (1441273457.1
REMARK PHENIX refinement                                                        
REMARK                                                                          
REMARK ****************** INPUT FILES AND LABELS ****************************** 
REMARK Reflections:                                                             
REMARK   file name      : D:\ACP\t1_hires.mtz                                   
REMARK   labels         : ['FP,SIGFP']                                          
REMARK R-free flags:                                                            
REMARK   file name      : D:\ACP\t1_hires.mtz                                   
REMARK   label          : FreeRflag                                             
REMARK   test_flag_value: 0                                                     
REMARK Model file name(s):                                                      
REMARK   D:\ACP\ksACP_refine_13-coot-0.pdb                                      
REMARK                                                                          
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* 
REMARK Start: r_work = 0.2259 r_free = 0.3027 bonds = 0.008 angles = 1.053      
REMARK Final: r_work = 0.2215 r_free = 0.3014 bonds = 0.008 angles = 1.000      
REMARK ************************************************************************ 
REMARK                                                                          
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ****************** 
REMARK leading digit, like 1_, means number of macro-cycle                      
REMARK   0  : statistics at the very beginning when nothing is done yet         
REMARK   1 s: bulk solvent correction and/or (anisotropic) scaling              
REMARK   1 z: refinement of coordinates                                         
REMARK   1 p: refinement of ADPs (Atomic Displacement Parameters)               
REMARK ------------------------------------------------------------------------ 
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift  
REMARK       0    : 0.4235 0.6209 0.008  1.05  21.2 125.9  52.7  18      0.000  
REMARK       1_bss: 0.2259 0.3027 0.008  1.05  21.2 125.9  52.7  18      0.000  
REMARK   1 ttarget: 0.2259 0.3027 0.008  1.05  21.2 125.9  52.7  18      0.000  
REMARK   1 dcbetar: 0.2259 0.3027 0.008  1.05  21.2 125.9  52.7  18      0.000  
REMARK    1_weight: 0.2259 0.3027 0.008  1.05  21.2 125.9  52.7  18      0.000  
REMARK    1_xyzrec: 0.2183 0.3011 0.008  1.05  21.2 125.9  52.7  18      0.100  
REMARK       1_adp: 0.2075 0.3068 0.008  1.05  23.6 175.2  58.6  18      0.100  
REMARK       2_bss: 0.2042 0.3068 0.008  1.05  23.6 175.2  58.6  18      0.100  
REMARK   2 ttarget: 0.2042 0.3068 0.008  1.05  23.6 175.2  58.6  18      0.100  
REMARK   2 realsrl: 0.2104 0.3005 0.008  1.19  23.6 175.2  58.6  18      0.126  
REMARK    2_weight: 0.2104 0.3005 0.008  1.19  23.6 175.2  58.6  18      0.126  
REMARK    2_xyzrec: 0.2127 0.3060 0.007  1.05  23.6 175.2  58.6  18      0.096  
REMARK       2_adp: 0.2159 0.3013 0.007  1.05  24.6 178.1  58.0  18      0.096  
REMARK       3_bss: 0.2164 0.3038 0.007  1.05  24.6 178.1  58.0  18      0.096  
REMARK   3 ttarget: 0.2164 0.3038 0.007  1.05  24.6 178.1  58.0  18      0.096  
REMARK   3 realsrl: 0.2184 0.3059 0.007  1.32  24.6 178.1  58.0  18      0.115  
REMARK    3_weight: 0.2184 0.3059 0.007  1.32  24.6 178.1  58.0  18      0.115  
REMARK    3_xyzrec: 0.2153 0.3066 0.008  1.00  24.6 178.1  58.0  18      0.113  
REMARK       3_adp: 0.2157 0.3044 0.008  1.00  25.8 179.2  57.4  18      0.113  
REMARK         end: 0.2215 0.3014 0.008  1.00  25.8 179.2  57.4  18      0.113  
REMARK ------------------------------------------------------------------------ 
REMARK MODEL CONTENT.                                                           
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM                        
REMARK        C                      442          442.00                        
REMARK       Zn                        7            7.00                        
REMARK        O                      164          164.00                        
REMARK        N                      105          105.00                        
REMARK    TOTAL                      718          718.00                        
REMARK -----------------------------------------------------------------------  
REMARK r_free_flags.md5.hexdigest 1bd22ba7d87793813b9c02b7ea5e707d              
REMARK                                                                          
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.        
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (phenix.refine: 1.9_1692)                     
REMARK   3   AUTHORS     : Adams,Afonine,Burnley,Chen,Davis,Echols,Gildea,      
REMARK   3               : Gopal,Gros,Grosse-Kunstleve,Headd,Hung,Immormino,    
REMARK   3               : Ioerger,McCoy,McKee,Moriarty,Pai,Read,Richardson,    
REMARK   3               : Richardson,Romo,Sacchettini,Sauter,Smith,Storoni,    
REMARK   3               : Terwilliger,Zwart                                    
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ML                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.000                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.405                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.37                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.67                          
REMARK   3   NUMBER OF REFLECTIONS             : 7210                           
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 7210                       
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2252                          
REMARK   3   R VALUE            (WORKING SET) : 0.2215                          
REMARK   3   FREE R VALUE                     : 0.3014                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.02                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 362                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.4121 -  2.8847    1.00     2330   123  0.1971 0.2883        
REMARK   3     2  2.8847 -  2.2898    1.00     2260   120  0.2870 0.3052        
REMARK   3     3  2.2898 -  2.0003    1.00     2258   119  0.2536 0.3818        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   GRID STEP FACTOR   : 4.00                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.31             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 41.86            
REMARK   3                                                                      
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT                       
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD     MAX  COUNT                                  
REMARK   3   BOND      :  0.008   0.044    698                                  
REMARK   3   ANGLE     :  1.000   5.176    943                                  
REMARK   3   CHIRALITY :  0.038   0.102    119                                  
REMARK   3   PLANARITY :  0.004   0.012    119                                  
REMARK   3   DIHEDRAL  : 16.003  77.157    260                                  
REMARK   3   MIN NONBONDED DISTANCE : 1.717                                     
REMARK   3                                                                      
REMARK   3  MOLPROBITY STATISTICS.                                              
REMARK   3   ALL-ATOM CLASHSCORE : 5.05                                         
REMARK   3   RAMACHANDRAN PLOT:                                                 
REMARK   3     OUTLIERS : 0.00  %                                               
REMARK   3     ALLOWED  : 4.55  %                                               
REMARK   3     FAVORED  : 95.45 %                                               
REMARK   3   ROTAMER OUTLIERS : 2.63 %                                          
REMARK   3   CBETA DEVIATIONS : 0                                               
REMARK   3                                                                      
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.                                     
REMARK   3   WILSON B : 37.63                                                   
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 15.00                            
REMARK   3   ATOMS          NUMBER OF ATOMS                                     
REMARK   3                    ISO.  ANISO.                                      
REMARK   3    ALL         :    718     718                                      
REMARK   3    ALL (NO H)  :    718     718                                      
REMARK   3    SOLVENT     :     18      18                                      
REMARK   3    NON-SOLVENT :    700     700                                      
REMARK   3    HYDROGENS   :      0       0                                      
REMARK   3                                                                      
REMARK   3  TLS DETAILS.                                                        
REMARK   3   NUMBER OF TLS GROUPS: 1                                            
REMARK   3   ORIGIN: CENTER OF MASS                                             
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2718  28.0238   0.6001              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3421 T22:   0.3261                                     
REMARK   3      T33:   0.3814 T12:  -0.0385                                     
REMARK   3      T13:  -0.0874 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3921 L22:   2.4969                                     
REMARK   3      L33:   3.1135 L12:  -0.6363                                     
REMARK   3      L13:   0.4267 L23:  -0.9011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3403 S12:  -0.0436 S13:  -0.5595                       
REMARK   3      S21:  -0.0376 S22:  -0.1610 S23:   0.1994                       
REMARK   3      S31:   0.0887 S32:  -0.1603 S33:  -0.1361                       
REMARK   3                                                                      
CRYST1   76.810   76.810   30.900  90.00  90.00 120.00 P 64                     
SCALE1      0.013019  0.007517  0.000000        0.00000                         
SCALE2      0.000000  0.015033  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.032362        0.00000                         
ATOM      1  N   ASP A   2      16.835  24.687  -1.804  1.00 46.56           N  
ANISOU    1  N   ASP A   2     5324   5930   6436    482   -829    414       N  
ATOM      2  CA  ASP A   2      17.440  26.016  -1.674  1.00 33.60           C  
ANISOU    2  CA  ASP A   2     3615   4474   4678    351   -733    517       C  
ATOM      3  CB  ASP A   2      17.974  26.464  -3.029  1.00 54.22           C  
ANISOU    3  CB  ASP A   2     6187   7223   7191    513   -591    459       C  
ATOM      4  CG  ASP A   2      18.632  27.825  -2.973  1.00 80.36           C  
ANISOU    4  CG  ASP A   2     9419  10703  10411    365   -491    586       C  
ATOM      5  OD1 ASP A   2      19.060  28.242  -1.875  1.00 94.67           O  
ANISOU    5  OD1 ASP A   2    11166  12545  12258    167   -548    716       O  
ATOM      6  OD2 ASP A   2      18.717  28.481  -4.030  1.00 82.03           O  
ANISOU    6  OD2 ASP A   2     9640  11015  10512    440   -364    559       O  
ATOM      7  C   ASP A   2      16.481  27.080  -1.114  1.00 56.39           C  
ANISOU    7  C   ASP A   2     6614   7342   7469    131   -730    527       C  
ATOM      8  O   ASP A   2      15.449  27.349  -1.709  1.00 46.77           O  
ANISOU    8  O   ASP A   2     5515   6068   6188    154   -703    415       O  
ATOM      9  N   ASP A   3      16.864  27.717  -0.006  1.00 48.38           N  
ANISOU    9  N   ASP A   3     5561   6386   6436    -68   -760    655       N  
ATOM     10  CA  ASP A   3      15.969  28.572   0.784  1.00 32.21           C  
ANISOU   10  CA  ASP A   3     3631   4302   4305   -262   -772    659       C  
ATOM     11  CB  ASP A   3      16.755  29.284   1.884  1.00 46.05           C  
ANISOU   11  CB  ASP A   3     5328   6148   6021   -457   -810    783       C  
ATOM     12  CG  ASP A   3      17.154  28.358   3.012  1.00 69.24           C  
ANISOU   12  CG  ASP A   3     8191   9084   9031   -496   -938    890       C  
ATOM     13  OD1 ASP A   3      16.309  27.538   3.444  1.00 48.92           O  
ANISOU   13  OD1 ASP A   3     5684   6403   6502   -474   -996    880       O  
ATOM     14  OD2 ASP A   3      18.321  28.438   3.454  1.00 55.71           O  
ANISOU   14  OD2 ASP A   3     6343   7485   7337   -550   -985   1002       O  
ATOM     15  C   ASP A   3      15.203  29.620  -0.019  1.00 63.30           C  
ANISOU   15  C   ASP A   3     7680   8236   8134   -263   -670    569       C  
ATOM     16  O   ASP A   3      13.970  29.700   0.057  1.00 43.17           O  
ANISOU   16  O   ASP A   3     5244   5602   5556   -280   -678    498       O  
ATOM     17  N   GLU A   4      15.939  30.425  -0.773  1.00 45.78           N  
ANISOU   17  N   GLU A   4     5415   6117   5861   -243   -573    595       N  
ATOM     18  CA  GLU A   4      15.356  31.515  -1.539  1.00 50.63           C  
ANISOU   18  CA  GLU A   4     6131   6733   6373   -244   -473    549       C  
ATOM     19  CB  GLU A   4      16.457  32.364  -2.169  1.00 48.12           C  
ANISOU   19  CB  GLU A   4     5727   6537   6020   -261   -371    641       C  
ATOM     20  CG  GLU A   4      15.953  33.633  -2.838  1.00 67.24           C  
ANISOU   20  CG  GLU A   4     8259   8944   8344   -289   -269    639       C  
ATOM     21  CD  GLU A   4      17.014  34.308  -3.688  1.00 83.75           C  
ANISOU   21  CD  GLU A   4    10249  11161  10410   -278   -151    753       C  
ATOM     22  OE1 GLU A   4      16.811  34.420  -4.917  1.00 81.50           O  
ANISOU   22  OE1 GLU A   4     9989  10935  10043   -117    -51    734       O  
ATOM     23  OE2 GLU A   4      18.052  34.721  -3.127  1.00 69.38           O  
ANISOU   23  OE2 GLU A   4     8317   9396   8647   -436   -162    871       O  
ATOM     24  C   GLU A   4      14.416  30.991  -2.613  1.00 71.94           C  
ANISOU   24  C   GLU A   4     8903   9388   9045    -56   -455    420       C  
ATOM     25  O   GLU A   4      13.324  31.521  -2.818  1.00 33.59           O  
ANISOU   25  O   GLU A   4     4160   4478   4126    -65   -438    361       O  
ATOM     26  N   GLU A   5      14.852  29.948  -3.304  1.00 30.00           N  
ANISOU   26  N   GLU A   5     3522   4100   3777    122   -467    369       N  
ATOM     27  CA  GLU A   5      14.041  29.297  -4.325  1.00 46.79           C  
ANISOU   27  CA  GLU A   5     5721   6181   5877    302   -483    219       C  
ATOM     28  C   GLU A   5      12.726  28.792  -3.728  1.00 34.00           C  
ANISOU   28  C   GLU A   5     4184   4414   4320    236   -596    150       C  
ATOM     29  O   GLU A   5      11.658  28.956  -4.322  1.00 44.60           O  
ANISOU   29  O   GLU A   5     5610   5727   5609    281   -605     56       O  
ATOM     30  CB  GLU A   5      14.810  28.141  -4.967  1.00 30.00           C  
ATOM     31  CG  GLU A   5      15.206  28.386  -6.415  1.00 30.00           C  
ATOM     32  CD  GLU A   5      16.028  27.250  -6.993  1.00 30.00           C  
ATOM     33  OE1 GLU A   5      16.449  26.366  -6.220  1.00 30.00           O  
ATOM     34  OE2 GLU A   5      16.254  27.243  -8.222  1.00 30.00           O  
ATOM     35  N   ILE A   6      12.799  28.191  -2.542  1.00 42.07           N  
ANISOU   35  N   ILE A   6     5169   5361   5455    127   -681    216       N  
ATOM     36  CA  ILE A   6      11.597  27.675  -1.884  1.00 40.34           C  
ANISOU   36  CA  ILE A   6     5003   5019   5307     48   -774    191       C  
ATOM     37  CB  ILE A   6      11.940  26.828  -0.657  1.00 50.19           C  
ANISOU   37  CB  ILE A   6     6194   6200   6676    -42   -863    297       C  
ATOM     38  CG1 ILE A   6      12.708  25.578  -1.082  1.00 38.50           C  
ANISOU   38  CG1 ILE A   6     4654   4657   5319    113   -924    267       C  
ATOM     39  CD1 ILE A   6      13.467  24.955   0.039  1.00 36.86           C  
ANISOU   39  CD1 ILE A   6     4366   4427   5212     51   -991    414       C  
ATOM     40  CG2 ILE A   6      10.670  26.429   0.089  1.00 42.40           C  
ANISOU   40  CG2 ILE A   6     5248   5112   5748   -147   -932    312       C  
ATOM     41  C   ILE A   6      10.680  28.809  -1.447  1.00 43.50           C  
ANISOU   41  C   ILE A   6     5475   5441   5614    -77   -724    215       C  
ATOM     42  O   ILE A   6       9.461  28.742  -1.638  1.00 31.60           O  
ANISOU   42  O   ILE A   6     4014   3883   4109    -70   -750    151       O  
ATOM     43  N   GLU A   7      11.275  29.842  -0.856  1.00 32.41           N  
ANISOU   43  N   GLU A   7     4072   4106   4136   -189   -658    303       N  
ATOM     44  CA  GLU A   7      10.529  31.018  -0.428  1.00 32.29           C  
ANISOU   44  CA  GLU A   7     4145   4096   4029   -287   -599    313       C  
ATOM     45  CB  GLU A   7      11.459  32.014   0.280  1.00 34.14           C  
ANISOU   45  CB  GLU A   7     4385   4380   4205   -423   -557    397       C  
ATOM     46  CG  GLU A   7      11.878  31.538   1.656  1.00 43.04           C  
ANISOU   46  CG  GLU A   7     5472   5514   5365   -551   -637    476       C  
ATOM     47  CD  GLU A   7      12.854  32.483   2.328  1.00 82.69           C  
ANISOU   47  CD  GLU A   7    10497  10593  10329   -698   -630    540       C  
ATOM     48  OE1 GLU A   7      13.189  33.517   1.715  1.00 50.07           O  
ANISOU   48  OE1 GLU A   7     6397   6472   6154   -712   -557    531       O  
ATOM     49  OE2 GLU A   7      13.287  32.187   3.463  1.00 79.41           O  
ANISOU   49  OE2 GLU A   7    10050  10209   9911   -807   -709    607       O  
ATOM     50  C   GLU A   7       9.823  31.689  -1.585  1.00 39.61           C  
ANISOU   50  C   GLU A   7     5136   5035   4881   -180   -534    237       C  
ATOM     51  O   GLU A   7       8.674  32.118  -1.448  1.00 35.24           O  
ANISOU   51  O   GLU A   7     4641   4452   4295   -190   -521    209       O  
ATOM     52  N   LYS A   8      10.485  31.782  -2.734  1.00 30.59           N  
ANISOU   52  N   LYS A   8     3972   3952   3699    -63   -487    217       N  
ATOM     53  CA  LYS A   8       9.852  32.451  -3.874  1.00 38.69           C  
ANISOU   53  CA  LYS A   8     5063   5010   4628     49   -428    167       C  
ATOM     54  CB  LYS A   8      10.889  32.872  -4.918  1.00 44.51           C  
ANISOU   54  CB  LYS A   8     5774   5848   5288    140   -337    205       C  
ATOM     55  CG  LYS A   8      11.960  33.831  -4.371  1.00 44.39           C  
ANISOU   55  CG  LYS A   8     5734   5861   5272     -3   -261    337       C  
ATOM     56  CD  LYS A   8      12.526  34.750  -5.442  1.00 65.59           C  
ANISOU   56  CD  LYS A   8     8423   8633   7864     56   -139    413       C  
ATOM     57  CE  LYS A   8      13.730  35.547  -4.921  1.00 72.56           C  
ANISOU   57  CE  LYS A   8     9246   9540   8784   -113    -85    554       C  
ATOM     58  NZ  LYS A   8      13.551  36.135  -3.554  1.00 51.85           N  
ANISOU   58  NZ  LYS A   8     6685   6804   6212   -320   -140    569       N  
ATOM     59  C   LYS A   8       8.773  31.557  -4.505  1.00 44.45           C  
ANISOU   59  C   LYS A   8     5801   5709   5380    165   -516     46       C  
ATOM     60  O   LYS A   8       7.669  32.017  -4.828  1.00 30.38           O  
ANISOU   60  O   LYS A   8     4067   3924   3551    197   -517     12       O  
ATOM     61  N   GLY A   9       9.083  30.274  -4.645  1.00 29.79           N  
ANISOU   61  N   GLY A   9     3892   3819   3609    224   -602    -17       N  
ATOM     62  CA  GLY A   9       8.157  29.333  -5.251  1.00 31.50           C  
ANISOU   62  CA  GLY A   9     4119   3981   3870    313   -714   -148       C  
ATOM     63  C   GLY A   9       6.850  29.221  -4.488  1.00 33.74           C  
ANISOU   63  C   GLY A   9     4398   4190   4231    200   -782   -138       C  
ATOM     64  O   GLY A   9       5.774  29.154  -5.085  1.00 39.88           O  
ANISOU   64  O   GLY A   9     5187   4969   4995    249   -842   -217       O  
ATOM     65  N   VAL A  10       6.938  29.193  -3.165  1.00 30.77           N  
ANISOU   65  N   VAL A  10     3993   3771   3926     52   -775    -34       N  
ATOM     66  CA  VAL A  10       5.747  29.078  -2.341  1.00 32.12           C  
ANISOU   66  CA  VAL A  10     4143   3901   4161    -52   -812      3       C  
ATOM     67  CB  VAL A  10       6.087  28.728  -0.890  1.00 33.01           C  
ANISOU   67  CB  VAL A  10     4223   3978   4342   -196   -816    124       C  
ATOM     68  CG1 VAL A  10       4.847  28.792  -0.018  1.00 33.48           C  
ANISOU   68  CG1 VAL A  10     4255   4037   4428   -294   -811    184       C  
ATOM     69  CG2 VAL A  10       6.742  27.318  -0.813  1.00 28.83           C  
ANISOU   69  CG2 VAL A  10     3646   3352   3957   -186   -923    125       C  
ATOM     70  C   VAL A  10       4.960  30.398  -2.396  1.00 38.02           C  
ANISOU   70  C   VAL A  10     4934   4718   4793    -47   -718     20       C  
ATOM     71  O   VAL A  10       3.741  30.375  -2.411  1.00 30.40           O  
ANISOU   71  O   VAL A  10     3938   3757   3854    -47   -748      5       O  
ATOM     72  N   THR A  11       5.660  31.532  -2.440  1.00 28.22           N  
ANISOU   72  N   THR A  11     3756   3525   3441    -40   -609     60       N  
ATOM     73  CA  THR A  11       4.991  32.829  -2.578  1.00 25.89           C  
ANISOU   73  CA  THR A  11     3526   3263   3049    -10   -519     75       C  
ATOM     74  CB  THR A  11       5.969  34.007  -2.514  1.00 25.76           C  
ANISOU   74  CB  THR A  11     3587   3254   2946    -39   -413    132       C  
ATOM     75  OG1 THR A  11       6.667  33.972  -1.265  1.00 31.15           O  
ANISOU   75  OG1 THR A  11     4269   3912   3655   -185   -409    187       O  
ATOM     76  CG2 THR A  11       5.198  35.326  -2.596  1.00 25.90           C  
ANISOU   76  CG2 THR A  11     3692   3261   2888      1   -326    148       C  
ATOM     77  C   THR A  11       4.232  32.891  -3.889  1.00 28.95           C  
ANISOU   77  C   THR A  11     3913   3693   3393    137   -551      4       C  
ATOM     78  O   THR A  11       3.078  33.290  -3.917  1.00 29.34           O  
ANISOU   78  O   THR A  11     3954   3762   3432    170   -549      2       O  
ATOM     79  N   SER A  12       4.882  32.466  -4.966  1.00 30.34           N  
ANISOU   79  N   SER A  12     4092   3902   3534    235   -583    -53       N  
ATOM     80  CA  SER A  12       4.261  32.373  -6.282  1.00 27.81           C  
ANISOU   80  CA  SER A  12     3779   3645   3143    384   -639   -137       C  
ATOM     81  CB  SER A  12       5.231  31.738  -7.281  1.00 39.81           C  
ANISOU   81  CB  SER A  12     5309   5207   4609    494   -662   -212       C  
ATOM     82  OG  SER A  12       6.128  32.706  -7.797  1.00 53.64           O  
ANISOU   82  OG  SER A  12     7109   7037   6236    549   -529   -132       O  
ATOM     83  C   SER A  12       2.964  31.574  -6.248  1.00 31.95           C  
ANISOU   83  C   SER A  12     4234   4145   3760    372   -775   -209       C  
ATOM     84  O   SER A  12       1.946  32.009  -6.777  1.00 28.58           O  
ANISOU   84  O   SER A  12     3797   3776   3285    442   -802   -224       O  
ATOM     85  N   ILE A  13       3.006  30.401  -5.624  1.00 37.51           N  
ANISOU   85  N   ILE A  13     4880   4762   4609    279   -866   -236       N  
ATOM     86  CA  ILE A  13       1.826  29.544  -5.549  1.00 35.80           C  
ANISOU   86  CA  ILE A  13     4580   4503   4517    230  -1006   -285       C  
ATOM     87  CB  ILE A  13       2.168  28.205  -4.889  1.00 40.83           C  
ANISOU   87  CB  ILE A  13     5175   5010   5328    125  -1099   -292       C  
ATOM     88  CG1 ILE A  13       3.109  27.411  -5.797  1.00 40.41           C  
ANISOU   88  CG1 ILE A  13     5177   4911   5267    235  -1170   -422       C  
ATOM     89  CD1 ILE A  13       3.675  26.166  -5.145  1.00 34.87           C  
ANISOU   89  CD1 ILE A  13     4453   4057   4740    163  -1245   -414       C  
ATOM     90  CG2 ILE A  13       0.891  27.421  -4.569  1.00 37.64           C  
ANISOU   90  CG2 ILE A  13     4667   4549   5086     22  -1228   -291       C  
ATOM     91  C   ILE A  13       0.687  30.202  -4.780  1.00 28.74           C  
ANISOU   91  C   ILE A  13     3625   3650   3647    162   -954   -188       C  
ATOM     92  O   ILE A  13      -0.418  30.332  -5.286  1.00 31.35           O  
ANISOU   92  O   ILE A  13     3897   4039   3977    208  -1016   -216       O  
ATOM     93  N   VAL A  14       0.963  30.608  -3.550  1.00 30.98           N  
ANISOU   93  N   VAL A  14     3915   3915   3941     64   -844    -78       N  
ATOM     94  CA  VAL A  14      -0.051  31.233  -2.718  1.00 35.97           C  
ANISOU   94  CA  VAL A  14     4496   4594   4576     22   -768      7       C  
ATOM     95  CB  VAL A  14       0.540  31.557  -1.351  1.00 39.37           C  
ANISOU   95  CB  VAL A  14     4970   5004   4986    -83   -656    100       C  
ATOM     96  CG1 VAL A  14      -0.368  32.477  -0.563  1.00 39.97           C  
ANISOU   96  CG1 VAL A  14     5036   5143   5008    -77   -538    165       C  
ATOM     97  CG2 VAL A  14       0.864  30.258  -0.596  1.00 42.05           C  
ANISOU   97  CG2 VAL A  14     5246   5275   5456   -213   -737    145       C  
ATOM     98  C   VAL A  14      -0.648  32.505  -3.377  1.00 40.24           C  
ANISOU   98  C   VAL A  14     5075   5216   4996    159   -694      4       C  
ATOM     99  O   VAL A  14      -1.870  32.721  -3.328  1.00 33.50           O  
ANISOU   99  O   VAL A  14     4132   4426   4170    190   -699     30       O  
ATOM    100  N   ALA A  15       0.191  33.332  -4.001  1.00 33.36           N  
ANISOU  100  N   ALA A  15     4323   4347   4004    244   -625    -10       N  
ATOM    101  CA  ALA A  15      -0.308  34.496  -4.785  1.00 28.18           C  
ANISOU  101  CA  ALA A  15     3717   3750   3240    389   -568      4       C  
ATOM    102  CB  ALA A  15       0.844  35.218  -5.430  1.00 34.46           C  
ANISOU  102  CB  ALA A  15     4639   4531   3922    445   -494     18       C  
ATOM    103  C   ALA A  15      -1.311  34.065  -5.861  1.00 40.84           C  
ANISOU  103  C   ALA A  15     5233   5438   4848    489   -702    -54       C  
ATOM    104  O   ALA A  15      -2.400  34.644  -6.010  1.00 34.98           O  
ANISOU  104  O   ALA A  15     4435   4762   4093    571   -695    -19       O  
ATOM    105  N   GLU A  16      -0.923  33.045  -6.618  1.00 35.29           N  
ANISOU  105  N   GLU A  16     4517   4733   4159    492   -832   -153       N  
ATOM    106  CA  GLU A  16      -1.733  32.541  -7.722  1.00 37.26           C  
ANISOU  106  CA  GLU A  16     4704   5060   4394    577   -995   -244       C  
ATOM    107  CB  GLU A  16      -0.998  31.408  -8.463  1.00 37.19           C  
ANISOU  107  CB  GLU A  16     4732   5015   4384    586  -1121   -384       C  
ATOM    108  CG  GLU A  16      -1.712  30.922  -9.719  1.00 78.98           C  
ANISOU  108  CG  GLU A  16     9998  10391   9621    685  -1308   -515       C  
ATOM    109  CD  GLU A  16      -0.945  29.839 -10.472  1.00105.44           C  
ANISOU  109  CD  GLU A  16    13418  13697  12948    725  -1422   -685       C  
ATOM    110  OE1 GLU A  16       0.134  29.412  -9.997  1.00 78.90           O  
ANISOU  110  OE1 GLU A  16    10105  10239   9636    681  -1352   -686       O  
ATOM    111  OE2 GLU A  16      -1.427  29.415 -11.546  1.00102.54           O  
ANISOU  111  OE2 GLU A  16    13057  13397  12505    813  -1587   -825       O  
ATOM    112  C   GLU A  16      -3.075  32.049  -7.202  1.00 41.95           C  
ANISOU  112  C   GLU A  16     5133   5670   5135    495  -1089   -226       C  
ATOM    113  O   GLU A  16      -4.134  32.386  -7.748  1.00 35.63           O  
ANISOU  113  O   GLU A  16     4252   4974   4312    577  -1153   -219       O  
ATOM    114  N   VAL A  17      -3.029  31.293  -6.111  1.00 31.47           N  
ANISOU  114  N   VAL A  17     3743   4256   3959    334  -1089   -193       N  
ATOM    115  CA  VAL A  17      -4.251  30.713  -5.551  1.00 46.00           C  
ANISOU  115  CA  VAL A  17     5404   6116   5959    228  -1167   -147       C  
ATOM    116  CB  VAL A  17      -3.942  29.721  -4.415  1.00 48.60           C  
ANISOU  116  CB  VAL A  17     5689   6331   6447     44  -1171    -95       C  
ATOM    117  CG1 VAL A  17      -5.234  29.280  -3.727  1.00 33.44           C  
ANISOU  117  CG1 VAL A  17     3566   4455   4686    -74  -1209      5       C  
ATOM    118  CG2 VAL A  17      -3.168  28.535  -4.950  1.00 32.58           C  
ANISOU  118  CG2 VAL A  17     3718   4175   4487      4  -1321   -215       C  
ATOM    119  C   VAL A  17      -5.179  31.785  -5.008  1.00 50.96           C  
ANISOU  119  C   VAL A  17     5958   6850   6556    285  -1034    -28       C  
ATOM    120  O   VAL A  17      -6.387  31.772  -5.260  1.00 34.49           O  
ANISOU  120  O   VAL A  17     3713   4863   4527    309  -1108     -3       O  
ATOM    121  N   THR A  18      -4.616  32.707  -4.244  1.00 34.83           N  
ANISOU  121  N   THR A  18     4023   4784   4427    309   -843     40       N  
ATOM    122  CA  THR A  18      -5.435  33.722  -3.594  1.00 40.30           C  
ANISOU  122  CA  THR A  18     4672   5552   5089    380   -698    135       C  
ATOM    123  CB  THR A  18      -4.748  34.234  -2.335  1.00 38.76           C  
ANISOU  123  CB  THR A  18     4588   5293   4844    322   -523    186       C  
ATOM    124  OG1 THR A  18      -3.552  34.929  -2.703  1.00 44.80           O  
ANISOU  124  OG1 THR A  18     5550   5978   5495    368   -467    145       O  
ATOM    125  CG2 THR A  18      -4.402  33.067  -1.430  1.00 33.05           C  
ANISOU  125  CG2 THR A  18     3810   4523   4227    134   -563    215       C  
ATOM    126  C   THR A  18      -5.756  34.907  -4.501  1.00 32.39           C  
ANISOU  126  C   THR A  18     3729   4611   3967    582   -660    135       C  
ATOM    127  O   THR A  18      -6.515  35.809  -4.113  1.00 42.92           O  
ANISOU  127  O   THR A  18     5028   5999   5279    685   -546    206       O  
ATOM    128  N   GLU A  19      -5.203  34.893  -5.711  1.00 32.82           N  
ANISOU  128  N   GLU A  19     3871   4661   3938    654   -751     65       N  
ATOM    129  CA  GLU A  19      -5.344  35.999  -6.657  1.00 47.01           C  
ANISOU  129  CA  GLU A  19     5747   6511   5604    846   -717     90       C  
ATOM    130  CB  GLU A  19      -6.778  36.063  -7.191  1.00 40.61           C  
ANISOU  130  CB  GLU A  19     4762   5844   4824    953   -819    118       C  
ATOM    131  CG  GLU A  19      -7.130  34.875  -8.073  1.00 35.60           C  
ANISOU  131  CG  GLU A  19     4013   5280   4232    901  -1059     18       C  
ATOM    132  CD  GLU A  19      -8.585  34.910  -8.522  1.00 48.09           C  
ANISOU  132  CD  GLU A  19     5389   7022   5862    979  -1183     54       C  
ATOM    133  OE1 GLU A  19      -9.322  35.827  -8.102  1.00 68.38           O  
ANISOU  133  OE1 GLU A  19     7891   9652   8439   1089  -1063    168       O  
ATOM    134  OE2 GLU A  19      -8.976  34.018  -9.301  1.00 57.68           O  
ANISOU  134  OE2 GLU A  19     6510   8300   7108    935  -1408    -39       O  
ATOM    135  C   GLU A  19      -4.953  37.348  -6.048  1.00 52.38           C  
ANISOU  135  C   GLU A  19     6574   7111   6216    912   -512    167       C  
ATOM    136  O   GLU A  19      -5.686  38.333  -6.190  1.00 36.76           O  
ANISOU  136  O   GLU A  19     4594   5167   4204   1066   -446    233       O  
ATOM    137  N   LEU A  20      -3.812  37.361  -5.361  1.00 39.95           N  
ANISOU  137  N   LEU A  20     5124   5422   4632    796   -426    155       N  
ATOM    138  CA  LEU A  20      -3.190  38.575  -4.824  1.00 32.88           C  
ANISOU  138  CA  LEU A  20     4400   4418   3676    817   -261    200       C  
ATOM    139  CB  LEU A  20      -3.142  38.537  -3.299  1.00 36.62           C  
ANISOU  139  CB  LEU A  20     4880   4837   4196    698   -168    200       C  
ATOM    140  CG  LEU A  20      -4.465  38.270  -2.586  1.00 45.84           C  
ANISOU  140  CG  LEU A  20     5886   6101   5431    722   -150    227       C  
ATOM    141  CD1 LEU A  20      -4.205  37.896  -1.135  1.00 51.11           C  
ANISOU  141  CD1 LEU A  20     6556   6745   6118    575    -78    229       C  
ATOM    142  CD2 LEU A  20      -5.345  39.501  -2.677  1.00 47.46           C  
ANISOU  142  CD2 LEU A  20     6116   6318   5598    921    -45    270       C  
ATOM    143  C   LEU A  20      -1.766  38.730  -5.362  1.00 45.35           C  
ANISOU  143  C   LEU A  20     6119   5927   5187    773   -249    194       C  
ATOM    144  O   LEU A  20      -1.245  37.826  -6.015  1.00 38.50           O  
ANISOU  144  O   LEU A  20     5213   5102   4312    736   -350    145       O  
ATOM    145  N   ASP A  21      -1.146  39.862  -5.034  1.00 30.02           N  
ANISOU  145  N   ASP A  21     4333   3871   3204    773   -124    241       N  
ATOM    146  CA  ASP A  21       0.182  40.264  -5.498  1.00 30.92           C  
ANISOU  146  CA  ASP A  21     4567   3918   3264    725    -86    273       C  
ATOM    147  CB  ASP A  21       0.305  41.801  -5.372  1.00 37.30           C  
ANISOU  147  CB  ASP A  21     5538   4588   4045    778     38    349       C  
ATOM    148  CG  ASP A  21       1.660  42.332  -5.822  1.00 52.53           C  
ANISOU  148  CG  ASP A  21     7577   6441   5941    703     86    416       C  
ATOM    149  OD1 ASP A  21       2.071  42.041  -6.962  1.00 54.89           O  
ANISOU  149  OD1 ASP A  21     7843   6835   6177    758     53    459       O  
ATOM    150  OD2 ASP A  21       2.308  43.052  -5.033  1.00100.10           O  
ANISOU  150  OD2 ASP A  21    13715  12319  11998    587    156    427       O  
ATOM    151  C   ASP A  21       1.283  39.573  -4.706  1.00 28.65           C  
ANISOU  151  C   ASP A  21     4276   3593   3016    535    -96    234       C  
ATOM    152  O   ASP A  21       1.212  39.501  -3.480  1.00 36.49           O  
ANISOU  152  O   ASP A  21     5272   4539   4052    433    -68    209       O  
ATOM    153  N   GLU A  22       2.308  39.057  -5.389  1.00 32.04           N  
ANISOU  153  N   GLU A  22     4694   4060   3422    501   -133    235       N  
ATOM    154  CA  GLU A  22       3.366  38.317  -4.697  1.00 27.51           C  
ANISOU  154  CA  GLU A  22     4091   3466   2896    343   -155    210       C  
ATOM    155  CB  GLU A  22       4.380  37.801  -5.719  1.00 45.15           C  
ANISOU  155  CB  GLU A  22     6296   5769   5091    372   -181    215       C  
ATOM    156  CG  GLU A  22       3.716  37.036  -6.858  1.00 64.18           C  
ANISOU  156  CG  GLU A  22     8642   8286   7457    518   -274    149       C  
ATOM    157  CD  GLU A  22       4.713  36.452  -7.831  1.00134.37           C  
ANISOU  157  CD  GLU A  22    17514  17257  16284    574   -289    127       C  
ATOM    158  OE1 GLU A  22       5.723  37.128  -8.120  1.00179.17           O  
ANISOU  158  OE1 GLU A  22    23232  22940  21905    561   -188    219       O  
ATOM    159  OE2 GLU A  22       4.487  35.320  -8.310  1.00133.67           O  
ANISOU  159  OE2 GLU A  22    17365  17221  16202    632   -400     19       O  
ATOM    160  C   GLU A  22       4.061  39.175  -3.629  1.00 27.49           C  
ANISOU  160  C   GLU A  22     4187   3352   2905    208    -74    247       C  
ATOM    161  O   GLU A  22       4.316  38.720  -2.512  1.00 29.53           O  
ANISOU  161  O   GLU A  22     4424   3592   3204     81    -96    219       O  
ATOM    162  N   LYS A  23       4.334  40.430  -3.966  1.00 30.74           N  
ANISOU  162  N   LYS A  23     4716   3683   3280    233     10    311       N  
ATOM    163  CA  LYS A  23       4.965  41.335  -3.017  1.00 31.26           C  
ANISOU  163  CA  LYS A  23     4899   3616   3364     96     66    327       C  
ATOM    164  CB  LYS A  23       5.246  42.707  -3.652  1.00 34.90           C  
ANISOU  164  CB  LYS A  23     5491   3961   3809    130    148    417       C  
ATOM    165  CG  LYS A  23       5.764  43.727  -2.646  1.00 45.43           C  
ANISOU  165  CG  LYS A  23     6971   5115   5175    -18    186    406       C  
ATOM    166  CD  LYS A  23       5.899  45.119  -3.259  1.00 72.91           C  
ANISOU  166  CD  LYS A  23    10597   8433   8671     16    261    504       C  
ATOM    167  CE  LYS A  23       6.493  46.102  -2.260  1.00 73.55           C  
ANISOU  167  CE  LYS A  23    10838   8305   8802   -158    273    469       C  
ATOM    168  NZ  LYS A  23       6.518  47.503  -2.771  1.00 99.87           N  
ANISOU  168  NZ  LYS A  23    14339  11426  12182   -128    340    563       N  
ATOM    169  C   LYS A  23       4.078  41.514  -1.818  1.00 28.76           C  
ANISOU  169  C   LYS A  23     4626   3251   3051     87     82    256       C  
ATOM    170  O   LYS A  23       4.529  41.489  -0.683  1.00 30.84           O  
ANISOU  170  O   LYS A  23     4926   3475   3316    -52     74    216       O  
ATOM    171  N   GLU A  24       2.786  41.726  -2.075  1.00 35.30           N  
ANISOU  171  N   GLU A  24     5445   4100   3868    250    108    244       N  
ATOM    172  CA  GLU A  24       1.850  41.922  -0.987  1.00 29.56           C  
ANISOU  172  CA  GLU A  24     4741   3356   3134    278    151    187       C  
ATOM    173  CB  GLU A  24       0.452  42.199  -1.541  1.00 45.20           C  
ANISOU  173  CB  GLU A  24     6675   5385   5115    487    180    204       C  
ATOM    174  CG  GLU A  24      -0.640  41.961  -0.518  1.00 84.82           C  
ANISOU  174  CG  GLU A  24    11627  10467  10134    529    220    161       C  
ATOM    175  CD  GLU A  24      -1.894  42.751  -0.801  1.00121.88           C  
ANISOU  175  CD  GLU A  24    16321  15162  14826    748    291    181       C  
ATOM    176  OE1 GLU A  24      -1.968  43.402  -1.864  1.00137.09           O  
ANISOU  176  OE1 GLU A  24    18293  17042  16751    871    290    236       O  
ATOM    177  OE2 GLU A  24      -2.811  42.720   0.046  1.00 83.08           O  
ANISOU  177  OE2 GLU A  24    11351  10310   9906    809    354    157       O  
ATOM    178  C   GLU A  24       1.781  40.749  -0.015  1.00 28.79           C  
ANISOU  178  C   GLU A  24     4531   3358   3049    169     99    149       C  
ATOM    179  O   GLU A  24       1.829  40.939   1.201  1.00 58.42           O  
ANISOU  179  O   GLU A  24     8347   7083   6766     91    135    108       O  
ATOM    180  N   ILE A  25       1.637  39.534  -0.530  1.00 28.65           N  
ANISOU  180  N   ILE A  25     4356   3451   3079    169     10    161       N  
ATOM    181  CA  ILE A  25       1.534  38.405   0.385  1.00 27.56           C  
ANISOU  181  CA  ILE A  25     4112   3383   2974     64    -40    153       C  
ATOM    182  CB  ILE A  25       1.092  37.114  -0.310  1.00 42.06           C  
ANISOU  182  CB  ILE A  25     5783   5305   4891     88   -148    158       C  
ATOM    183  CG1 ILE A  25       1.969  36.801  -1.507  1.00 44.67           C  
ANISOU  183  CG1 ILE A  25     6113   5630   5229    110   -214    147       C  
ATOM    184  CD1 ILE A  25       1.754  35.389  -1.997  1.00 61.35           C  
ANISOU  184  CD1 ILE A  25     8094   7794   7423    108   -339    117       C  
ATOM    185  CG2 ILE A  25      -0.368  37.190  -0.727  1.00 58.06           C  
ANISOU  185  CG2 ILE A  25     7720   7398   6940    222   -144    162       C  
ATOM    186  C   ILE A  25       2.877  38.160   1.100  1.00 28.06           C  
ANISOU  186  C   ILE A  25     4222   3412   3027   -106    -71    156       C  
ATOM    187  O   ILE A  25       2.896  37.713   2.247  1.00 51.02           O  
ANISOU  187  O   ILE A  25     7113   6353   5920   -202    -79    160       O  
ATOM    188  N   TRP A  26       3.986  38.484   0.430  1.00 26.94           N  
ANISOU  188  N   TRP A  26     4127   3224   2885   -140    -85    171       N  
ATOM    189  CA  TRP A  26       5.312  38.354   1.089  1.00 27.92           C  
ANISOU  189  CA  TRP A  26     4272   3329   3007   -303   -121    187       C  
ATOM    190  CB  TRP A  26       6.460  38.733   0.140  1.00 28.94           C  
ANISOU  190  CB  TRP A  26     4413   3433   3151   -322   -120    230       C  
ATOM    191  CG  TRP A  26       7.832  38.618   0.781  1.00 27.41           C  
ANISOU  191  CG  TRP A  26     4203   3241   2970   -492   -165    261       C  
ATOM    192  CD1 TRP A  26       8.750  39.628   0.961  1.00 38.02           C  
ANISOU  192  CD1 TRP A  26     5629   4512   4304   -610   -146    287       C  
ATOM    193  NE1 TRP A  26       9.881  39.133   1.589  1.00 30.32           N  
ANISOU  193  NE1 TRP A  26     4578   3589   3353   -757   -222    320       N  
ATOM    194  CE2 TRP A  26       9.698  37.796   1.839  1.00 28.38           C  
ANISOU  194  CE2 TRP A  26     4214   3436   3131   -720   -283    321       C  
ATOM    195  CD2 TRP A  26       8.414  37.434   1.342  1.00 29.47           C  
ANISOU  195  CD2 TRP A  26     4349   3578   3270   -567   -251    280       C  
ATOM    196  CE3 TRP A  26       7.991  36.106   1.477  1.00 41.48           C  
ANISOU  196  CE3 TRP A  26     5763   5159   4840   -525   -314    279       C  
ATOM    197  CZ3 TRP A  26       8.836  35.184   2.088  1.00 31.82           C  
ANISOU  197  CZ3 TRP A  26     4453   3979   3660   -612   -396    324       C  
ATOM    198  CH2 TRP A  26      10.088  35.569   2.571  1.00 34.68           C  
ANISOU  198  CH2 TRP A  26     4813   4356   4007   -739   -422    368       C  
ATOM    199  CZ2 TRP A  26      10.542  36.867   2.451  1.00 36.40           C  
ANISOU  199  CZ2 TRP A  26     5122   4526   4182   -806   -372    364       C  
ATOM    200  C   TRP A  26       5.318  39.250   2.316  1.00 30.13           C  
ANISOU  200  C   TRP A  26     4687   3547   3216   -386    -74    151       C  
ATOM    201  O   TRP A  26       5.631  38.825   3.417  1.00 28.25           O  
ANISOU  201  O   TRP A  26     4442   3348   2946   -498   -112    147       O  
ATOM    202  N   GLU A  27       4.941  40.512   2.118  1.00 33.06           N  
ANISOU  202  N   GLU A  27     5195   3815   3553   -318      6    122       N  
ATOM    203  CA  GLU A  27       4.767  41.427   3.246  1.00 40.29           C  
ANISOU  203  CA  GLU A  27     6270   4647   4390   -360     56     50       C  
ATOM    204  CB  GLU A  27       4.205  42.765   2.757  1.00 30.73           C  
ANISOU  204  CB  GLU A  27     5207   3293   3176   -233    147     23       C  
ATOM    205  CG  GLU A  27       5.128  43.487   1.826  1.00 31.06           C  
ANISOU  205  CG  GLU A  27     5309   3218   3273   -282    140     83       C  
ATOM    206  CD  GLU A  27       4.538  44.834   1.397  1.00 47.00           C  
ANISOU  206  CD  GLU A  27     7492   5065   5301   -151    227     78       C  
ATOM    207  OE1 GLU A  27       3.353  45.078   1.702  1.00 67.67           O  
ANISOU  207  OE1 GLU A  27    10146   7682   7885     10    293     25       O  
ATOM    208  OE2 GLU A  27       5.259  45.630   0.760  1.00 71.96           O  
ANISOU  208  OE2 GLU A  27    10734   8094   8511   -205    235    142       O  
ATOM    209  C   GLU A  27       3.856  40.873   4.339  1.00 35.72           C  
ANISOU  209  C   GLU A  27     5654   4171   3746   -332     80     16       C  
ATOM    210  O   GLU A  27       4.071  41.119   5.525  1.00 45.36           O  
ANISOU  210  O   GLU A  27     6970   5392   4873   -417     84    -40       O  
ATOM    211  N   LYS A  28       2.835  40.128   3.949  1.00 29.30           N  
ANISOU  211  N   LYS A  28     4699   3458   2976   -218     94     54       N  
ATOM    212  CA  LYS A  28       1.935  39.543   4.941  1.00 34.66           C  
ANISOU  212  CA  LYS A  28     5308   4254   3608   -200    130     60       C  
ATOM    213  CB  LYS A  28       0.477  39.725   4.519  1.00 33.82           C  
ANISOU  213  CB  LYS A  28     5129   4193   3526    -14    212     69       C  
ATOM    214  CG  LYS A  28      -0.053  41.149   4.778  1.00 32.93           C  
ANISOU  214  CG  LYS A  28     5185   3990   3335    122    335     -7       C  
ATOM    215  CD  LYS A  28      -1.191  41.503   3.843  1.00 60.57           C  
ANISOU  215  CD  LYS A  28     8613   7505   6897    326    386     21       C  
ATOM    216  CE  LYS A  28      -1.272  43.008   3.654  1.00 77.60           C  
ANISOU  216  CE  LYS A  28    10971   9493   9020    458    473    -39       C  
ATOM    217  NZ  LYS A  28      -2.403  43.404   2.778  1.00 74.98           N  
ANISOU  217  NZ  LYS A  28    10565   9183   8742    681    521      7       N  
ATOM    218  C   LYS A  28       2.250  38.066   5.165  1.00 38.77           C  
ANISOU  218  C   LYS A  28     5669   4877   4187   -309     33    138       C  
ATOM    219  O   LYS A  28       1.347  37.231   5.334  1.00 41.75           O  
ANISOU  219  O   LYS A  28     5907   5351   4605   -278     36    193       O  
ATOM    220  N   ARG A  29       3.540  37.747   5.181  1.00 42.40           N  
ANISOU  220  N   ARG A  29     6139   5308   4663   -439    -57    154       N  
ATOM    221  CA  ARG A  29       3.968  36.358   5.317  1.00 48.91           C  
ANISOU  221  CA  ARG A  29     6824   6199   5561   -524   -157    231       C  
ATOM    222  CB  ARG A  29       5.469  36.226   5.024  1.00 29.52           C  
ANISOU  222  CB  ARG A  29     4372   3705   3139   -621   -243    246       C  
ATOM    223  CG  ARG A  29       6.386  37.165   5.813  1.00 38.27           C  
ANISOU  223  CG  ARG A  29     5615   4781   4144   -737   -246    209       C  
ATOM    224  CD  ARG A  29       7.774  37.209   5.184  1.00 40.40           C  
ANISOU  224  CD  ARG A  29     5852   5019   4478   -813   -314    238       C  
ATOM    225  NE  ARG A  29       8.664  38.182   5.829  1.00 37.70           N  
ANISOU  225  NE  ARG A  29     5625   4633   4064   -950   -337    204       N  
ATOM    226  CZ  ARG A  29       8.760  39.464   5.479  1.00 29.59           C  
ANISOU  226  CZ  ARG A  29     4731   3490   3023   -957   -285    148       C  
ATOM    227  NH1 ARG A  29       8.046  39.933   4.464  1.00 36.02           N  
ANISOU  227  NH1 ARG A  29     5573   4236   3876   -817   -198    137       N  
ATOM    228  NH2 ARG A  29       9.606  40.266   6.131  1.00 30.87           N  
ANISOU  228  NH2 ARG A  29     4995   3596   3137  -1113   -335    110       N  
ATOM    229  C   ARG A  29       3.644  35.769   6.691  1.00 43.56           C  
ANISOU  229  C   ARG A  29     6117   5618   4814   -596   -152    287       C  
ATOM    230  O   ARG A  29       3.557  34.551   6.846  1.00 40.86           O  
ANISOU  230  O   ARG A  29     5647   5325   4554   -639   -216    377       O  
ATOM    231  N   ASP A  30       3.464  36.628   7.686  1.00 31.70           N  
ANISOU  231  N   ASP A  30     4746   4140   3158   -604    -75    236       N  
ATOM    232  CA  ASP A  30       3.145  36.172   9.034  1.00 35.93           C  
ANISOU  232  CA  ASP A  30     5271   4800   3580   -657    -51    293       C  
ATOM    233  CB  ASP A  30       3.993  36.909  10.071  1.00 50.80           C  
ANISOU  233  CB  ASP A  30     7326   6691   5286   -750    -69    222       C  
ATOM    234  CG  ASP A  30       5.429  36.435  10.095  1.00 57.36           C  
ANISOU  234  CG  ASP A  30     8130   7507   6158   -897   -219    268       C  
ATOM    235  OD1 ASP A  30       5.675  35.256   9.757  1.00 63.35           O  
ANISOU  235  OD1 ASP A  30     8734   8290   7047   -924   -295    383       O  
ATOM    236  OD2 ASP A  30       6.312  37.238  10.465  1.00116.43           O  
ANISOU  236  OD2 ASP A  30    15741  14947  13550   -985   -266    188       O  
ATOM    237  C   ASP A  30       1.661  36.349   9.371  1.00 43.94           C  
ANISOU  237  C   ASP A  30     6251   5900   4544   -535     88    301       C  
ATOM    238  O   ASP A  30       1.253  36.169  10.518  1.00 49.76           O  
ANISOU  238  O   ASP A  30     6992   6765   5150   -550    151    347       O  
ATOM    239  N   ALA A  31       0.859  36.705   8.374  1.00 41.10           N  
ANISOU  239  N   ALA A  31     5845   5493   4279   -405    139    269       N  
ATOM    240  CA  ALA A  31      -0.558  36.930   8.610  1.00 56.18           C  
ANISOU  240  CA  ALA A  31     7690   7497   6159   -271    273    285       C  
ATOM    241  CB  ALA A  31      -1.142  37.839   7.542  1.00 50.26           C  
ANISOU  241  CB  ALA A  31     6967   6663   5467   -109    324    210       C  
ATOM    242  C   ALA A  31      -1.284  35.598   8.640  1.00 54.84           C  
ANISOU  242  C   ALA A  31     7291   7438   6109   -315    244    436       C  
ATOM    243  O   ALA A  31      -0.938  34.692   7.888  1.00 48.99           O  
ANISOU  243  O   ALA A  31     6448   6641   5527   -385    115    484       O  
ATOM    244  N   ASN A  32      -2.279  35.472   9.512  1.00 59.01           N  
ANISOU  244  N   ASN A  32     7738   8118   6563   -274    364    512       N  
ATOM    245  CA  ASN A  32      -3.093  34.265   9.543  1.00 46.78           C  
ANISOU  245  CA  ASN A  32     5952   6669   5153   -331    345    679       C  
ATOM    246  CB  ASN A  32      -4.018  34.264  10.763  1.00 62.93           C  
ANISOU  246  CB  ASN A  32     7928   8919   7065   -295    513    783       C  
ATOM    247  CG  ASN A  32      -4.679  32.909  11.008  1.00 70.03           C  
ANISOU  247  CG  ASN A  32     8582   9918   8110   -411    486   1003       C  
ATOM    248  OD1 ASN A  32      -5.240  32.300  10.099  1.00 64.27           O  
ANISOU  248  OD1 ASN A  32     7676   9142   7601   -434    401   1051       O  
ATOM    249  ND2 ASN A  32      -4.609  32.436  12.247  1.00 79.10           N  
ANISOU  249  ND2 ASN A  32     9722  11201   9132   -491    549   1141       N  
ATOM    250  C   ASN A  32      -3.886  34.168   8.242  1.00 61.67           C  
ANISOU  250  C   ASN A  32     7693   8512   7225   -251    299    667       C  
ATOM    251  O   ASN A  32      -4.484  35.142   7.790  1.00 59.48           O  
ANISOU  251  O   ASN A  32     7446   8239   6916    -92    382    585       O  
ATOM    252  N   PHE A  33      -3.874  32.989   7.636  1.00 61.35           N  
ANISOU  252  N   PHE A  33     7507   8425   7378   -357    154    743       N  
ATOM    253  CA  PHE A  33      -4.500  32.767   6.338  1.00 43.97           C  
ANISOU  253  CA  PHE A  33     5179   6180   5346   -304     63    712       C  
ATOM    254  CB  PHE A  33      -4.139  31.368   5.849  1.00 58.78           C  
ANISOU  254  CB  PHE A  33     6959   7961   7413   -448   -121    764       C  
ATOM    255  CG  PHE A  33      -2.974  31.332   4.910  1.00 50.83           C  
ANISOU  255  CG  PHE A  33     6080   6803   6428   -442   -245    641       C  
ATOM    256  CD1 PHE A  33      -2.318  32.497   4.546  1.00 59.32           C  
ANISOU  256  CD1 PHE A  33     7328   7841   7370   -341   -191    523       C  
ATOM    257  CE1 PHE A  33      -1.250  32.456   3.681  1.00 41.20           C  
ANISOU  257  CE1 PHE A  33     5124   5437   5092   -336   -285    438       C  
ATOM    258  CZ  PHE A  33      -0.808  31.244   3.187  1.00 67.31           C  
ANISOU  258  CZ  PHE A  33     8368   8669   8538   -407   -432    444       C  
ATOM    259  CE2 PHE A  33      -1.449  30.074   3.550  1.00 42.59           C  
ANISOU  259  CE2 PHE A  33     5091   5541   5551   -504   -501    541       C  
ATOM    260  CD2 PHE A  33      -2.520  30.125   4.410  1.00 56.79           C  
ANISOU  260  CD2 PHE A  33     6784   7451   7343   -535   -409    651       C  
ATOM    261  C   PHE A  33      -6.024  32.936   6.341  1.00 64.87           C  
ANISOU  261  C   PHE A  33     7635   8975   8039   -214    155    783       C  
ATOM    262  O   PHE A  33      -6.569  33.714   5.563  1.00 76.66           O  
ANISOU  262  O   PHE A  33     9118  10477   9532    -63    179    709       O  
ATOM    263  N   PHE A  34      -6.703  32.191   7.207  1.00 89.00           N  
ANISOU  263  N   PHE A  34    10522  12155  11139   -306    208    948       N  
ATOM    264  CA  PHE A  34      -8.162  32.172   7.235  1.00 90.74           C  
ANISOU  264  CA  PHE A  34    10501  12541  11436   -248    290   1053       C  
ATOM    265  CB  PHE A  34      -8.659  30.975   8.052  1.00 82.81           C  
ANISOU  265  CB  PHE A  34     9292  11632  10540   -425    294   1274       C  
ATOM    266  CG  PHE A  34      -8.346  29.640   7.433  1.00108.77           C  
ANISOU  266  CG  PHE A  34    12499  14762  14066   -617     65   1318       C  
ATOM    267  CD1 PHE A  34      -7.052  29.143   7.440  1.00 76.70           C  
ANISOU  267  CD1 PHE A  34     8613  10528  10001   -708    -50   1268       C  
ATOM    268  CE1 PHE A  34      -6.763  27.923   6.870  1.00 71.57           C  
ANISOU  268  CE1 PHE A  34     7907   9713   9573   -854   -254   1291       C  
ATOM    269  CZ  PHE A  34      -7.771  27.175   6.289  1.00 82.65           C  
ANISOU  269  CZ  PHE A  34     9087  11108  11208   -938   -365   1356       C  
ATOM    270  CE2 PHE A  34      -9.064  27.656   6.275  1.00 92.89           C  
ANISOU  270  CE2 PHE A  34    10188  12591  12517   -874   -267   1417       C  
ATOM    271  CD2 PHE A  34      -9.346  28.884   6.842  1.00110.39           C  
ANISOU  271  CD2 PHE A  34    12451  14985  14507   -701    -44   1404       C  
ATOM    272  C   PHE A  34      -8.744  33.461   7.807  1.00 92.79           C  
ANISOU  272  C   PHE A  34    10813  12939  11504    -41    515   1015       C  
ATOM    273  O   PHE A  34      -9.865  33.848   7.479  1.00 80.34           O  
ANISOU  273  O   PHE A  34     9070  11480   9976     90    583   1045       O  
ATOM    274  N   GLN A  35      -7.970  34.125   8.656  1.00 92.29           N  
ANISOU  274  N   GLN A  35    10982  12857  11225     -5    619    942       N  
ATOM    275  CA  GLN A  35      -8.466  35.274   9.402  1.00 88.68           C  
ANISOU  275  CA  GLN A  35    10609  12518  10567    190    840    890       C  
ATOM    276  CB  GLN A  35      -7.854  35.280  10.802  1.00 72.55           C  
ANISOU  276  CB  GLN A  35     8719  10543   8304    128    939    907       C  
ATOM    277  CG  GLN A  35      -8.005  33.959  11.530  1.00 79.56           C  
ANISOU  277  CG  GLN A  35     9427  11554   9247    -61    920   1129       C  
ATOM    278  CD  GLN A  35      -9.059  34.016  12.617  1.00132.58           C  
ANISOU  278  CD  GLN A  35    16001  18542  15833     21   1150   1272       C  
ATOM    279  OE1 GLN A  35      -9.229  35.041  13.277  1.00148.93           O  
ANISOU  279  OE1 GLN A  35    18212  20705  17669    202   1331   1168       O  
ATOM    280  NE2 GLN A  35      -9.782  32.917  12.799  1.00133.95           N  
ANISOU  280  NE2 GLN A  35    15893  18842  16161   -109   1149   1512       N  
ATOM    281  C   GLN A  35      -8.197  36.613   8.714  1.00 94.83           C  
ANISOU  281  C   GLN A  35    11594  13158  11279    376    859    697       C  
ATOM    282  O   GLN A  35      -9.036  37.513   8.748  1.00124.54           O  
ANISOU  282  O   GLN A  35    15340  16994  14984    589   1006    662       O  
ATOM    283  N   ASP A  36      -7.033  36.743   8.086  1.00 85.16           N  
ANISOU  283  N   ASP A  36    10554  11734  10070    302    718    588       N  
ATOM    284  CA  ASP A  36      -6.629  38.018   7.503  1.00103.65           C  
ANISOU  284  CA  ASP A  36    13112  13923  12349    445    736    430       C  
ATOM    285  CB  ASP A  36      -5.228  38.400   7.993  1.00 95.09           C  
ANISOU  285  CB  ASP A  36    12296  12698  11135    341    700    323       C  
ATOM    286  CG  ASP A  36      -5.185  38.678   9.485  1.00106.74           C  
ANISOU  286  CG  ASP A  36    13883  14271  12402    341    834    301       C  
ATOM    287  OD1 ASP A  36      -5.925  39.573   9.944  1.00117.57           O  
ANISOU  287  OD1 ASP A  36    15314  15697  13661    531   1001    240       O  
ATOM    288  OD2 ASP A  36      -4.412  38.003  10.199  1.00 99.17           O  
ANISOU  288  OD2 ASP A  36    12958  13342  11382    168    771    342       O  
ATOM    289  C   ASP A  36      -6.653  38.020   5.977  1.00 93.32           C  
ANISOU  289  C   ASP A  36    11748  12514  11195    484    599    410       C  
ATOM    290  O   ASP A  36      -7.027  39.019   5.363  1.00 92.48           O  
ANISOU  290  O   ASP A  36    11702  12356  11079    667    647    352       O  
ATOM    291  N   LEU A  37      -6.260  36.909   5.364  1.00 86.06           N  
ANISOU  291  N   LEU A  37    10723  11568  10408    326    428    458       N  
ATOM    292  CA  LEU A  37      -6.094  36.875   3.913  1.00 72.22           C  
ANISOU  292  CA  LEU A  37     8956   9727   8758    358    288    416       C  
ATOM    293  CB  LEU A  37      -4.696  36.362   3.552  1.00 67.38           C  
ANISOU  293  CB  LEU A  37     8461   8981   8160    210    156    370       C  
ATOM    294  CG  LEU A  37      -3.585  37.410   3.674  1.00 70.42           C  
ANISOU  294  CG  LEU A  37     9100   9234   8421    226    206    279       C  
ATOM    295  CD1 LEU A  37      -2.272  36.893   3.117  1.00 69.51           C  
ANISOU  295  CD1 LEU A  37     9048   9021   8342    103     77    253       C  
ATOM    296  CD2 LEU A  37      -3.988  38.692   2.969  1.00 52.32           C  
ANISOU  296  CD2 LEU A  37     6900   6885   6092    419    275    230       C  
ATOM    297  C   LEU A  37      -7.145  36.045   3.178  1.00 71.69           C  
ANISOU  297  C   LEU A  37     8624   9762   8851    358    185    492       C  
ATOM    298  O   LEU A  37      -6.905  35.601   2.057  1.00119.22           O  
ANISOU  298  O   LEU A  37    14619  15726  14955    332     25    456       O  
ATOM    299  N   GLU A  38      -8.300  35.840   3.809  1.00 48.84           N  
ANISOU  299  N   GLU A  38     5533   7031   5993    386    273    594       N  
ATOM    300  CA  GLU A  38      -9.484  35.300   3.128  1.00 82.16           C  
ANISOU  300  CA  GLU A  38     9478  11370  10370    405    186    671       C  
ATOM    301  CB  GLU A  38     -10.042  36.349   2.150  1.00 84.82           C  
ANISOU  301  CB  GLU A  38     9822  11723  10683    635    194    620       C  
ATOM    302  CG  GLU A  38      -9.883  37.802   2.600  1.00125.60           C  
ANISOU  302  CG  GLU A  38    15197  16839  15686    835    387    560       C  
ATOM    303  CD  GLU A  38     -10.404  38.794   1.575  1.00125.18           C  
ANISOU  303  CD  GLU A  38    15156  16776  15629   1068    382    536       C  
ATOM    304  OE1 GLU A  38      -9.867  38.816   0.445  1.00 85.77           O  
ANISOU  304  OE1 GLU A  38    10248  11690  10652   1064    239    488       O  
ATOM    305  OE2 GLU A  38     -11.331  39.565   1.902  1.00138.92           O  
ANISOU  305  OE2 GLU A  38    16828  18610  17345   1271    527    574       O  
ATOM    306  C   GLU A  38      -9.267  33.990   2.353  1.00 78.21           C  
ANISOU  306  C   GLU A  38     8871  10809  10036    224    -48    675       C  
ATOM    307  O   GLU A  38      -9.675  33.889   1.198  1.00 67.44           O  
ANISOU  307  O   GLU A  38     7423   9452   8749    273   -190    636       O  
ATOM    308  N   ILE A  39      -8.628  32.991   2.955  1.00 54.76           N  
ANISOU  308  N   ILE A  39     5916   7775   7115     27    -99    716       N  
ATOM    309  CA  ILE A  39      -8.486  31.719   2.249  1.00 64.60           C  
ANISOU  309  CA  ILE A  39     7071   8936   8538   -130   -321    708       C  
ATOM    310  CB  ILE A  39      -7.021  31.245   2.184  1.00 67.20           C  
ANISOU  310  CB  ILE A  39     7601   9090   8842   -222   -403    630       C  
ATOM    311  CG1 ILE A  39      -6.601  30.605   3.501  1.00 70.68           C  
ANISOU  311  CG1 ILE A  39     8049   9521   9287   -373   -339    748       C  
ATOM    312  CD1 ILE A  39      -5.936  29.264   3.326  1.00 86.86           C  
ANISOU  312  CD1 ILE A  39    10093  11421  11487   -536   -513    758       C  
ATOM    313  CG2 ILE A  39      -6.104  32.396   1.803  1.00 68.19           C  
ANISOU  313  CG2 ILE A  39     7963   9154   8792    -84   -334    510       C  
ATOM    314  C   ILE A  39      -9.339  30.608   2.869  1.00 79.17           C  
ANISOU  314  C   ILE A  39     8665  10856  10559   -301   -356    871       C  
ATOM    315  O   ILE A  39      -9.561  30.572   4.080  1.00 74.20           O  
ANISOU  315  O   ILE A  39     7983  10320   9888   -349   -202   1006       O  
ATOM    316  N   ASP A  40      -9.820  29.712   2.010  1.00 79.30           N  
ANISOU  316  N   ASP A  40     8529  10833  10767   -397   -565    860       N  
ATOM    317  CA  ASP A  40     -10.711  28.622   2.405  1.00 40.97           C  
ANISOU  317  CA  ASP A  40     3412   6025   6129   -587   -636   1020       C  
ATOM    318  CB  ASP A  40     -11.789  28.390   1.347  1.00 42.65           C  
ANISOU  318  CB  ASP A  40     3406   6302   6497   -589   -814    993       C  
ATOM    319  CG  ASP A  40     -12.639  29.611   1.095  1.00 69.09           C  
ANISOU  319  CG  ASP A  40     6664   9852   9735   -368   -693    996       C  
ATOM    320  OD1 ASP A  40     -12.338  30.694   1.640  1.00118.30           O  
ANISOU  320  OD1 ASP A  40    13040  16140  15770   -198   -475    989       O  
ATOM    321  OD2 ASP A  40     -13.626  29.480   0.355  1.00 62.28           O  
ANISOU  321  OD2 ASP A  40     5584   9087   8991   -363   -827   1007       O  
ATOM    322  C   ASP A  40      -9.984  27.313   2.609  1.00 61.53           C  
ANISOU  322  C   ASP A  40     6067   8434   8877   -796   -777   1045       C  
ATOM    323  O   ASP A  40      -8.815  27.193   2.267  1.00 39.08           O  
ANISOU  323  O   ASP A  40     3444   5429   5975   -778   -843    915       O  
ATOM    324  N   SER A  41     -10.702  26.318   3.124  1.00 56.57           N  
ANISOU  324  N   SER A  41     5220   7818   8455   -993   -825   1224       N  
ATOM    325  CA  SER A  41     -10.164  24.973   3.195  1.00 65.99           C  
ANISOU  325  CA  SER A  41     6443   8791   9839  -1196   -993   1258       C  
ATOM    326  CB  SER A  41     -11.151  24.024   3.870  1.00 80.40           C  
ANISOU  326  CB  SER A  41     7994  10655  11902  -1421  -1013   1508       C  
ATOM    327  OG  SER A  41     -11.931  23.336   2.904  1.00 90.17           O  
ANISOU  327  OG  SER A  41     9059  11819  13383  -1537  -1256   1456       O  
ATOM    328  C   SER A  41      -9.839  24.503   1.781  1.00 58.18           C  
ANISOU  328  C   SER A  41     5540   7618   8949  -1188  -1255   1029       C  
ATOM    329  O   SER A  41      -8.822  23.860   1.554  1.00 63.29           O  
ANISOU  329  O   SER A  41     6361   8054   9631  -1222  -1363    934       O  
ATOM    330  N   LEU A  42     -10.689  24.872   0.828  1.00 46.86           N  
ANISOU  330  N   LEU A  42     3986   6283   7537  -1119  -1352    937       N  
ATOM    331  CA  LEU A  42     -10.475  24.525  -0.577  1.00 43.94           C  
ANISOU  331  CA  LEU A  42     3700   5783   7211  -1086  -1601    703       C  
ATOM    332  CB  LEU A  42     -11.673  24.945  -1.431  1.00 45.47           C  
ANISOU  332  CB  LEU A  42     3698   6148   7431  -1029  -1704    662       C  
ATOM    333  CG  LEU A  42     -12.831  23.961  -1.527  1.00 51.03           C  
ANISOU  333  CG  LEU A  42     4114   6849   8427  -1257  -1900    756       C  
ATOM    334  CD1 LEU A  42     -13.833  24.444  -2.568  1.00 50.59           C  
ANISOU  334  CD1 LEU A  42     3894   6969   8360  -1168  -2040    673       C  
ATOM    335  CD2 LEU A  42     -12.338  22.573  -1.881  1.00 61.86           C  
ANISOU  335  CD2 LEU A  42     5575   7921  10006  -1446  -2150    654       C  
ATOM    336  C   LEU A  42      -9.214  25.167  -1.136  1.00 41.89           C  
ANISOU  336  C   LEU A  42     3733   5461   6724   -892  -1558    513       C  
ATOM    337  O   LEU A  42      -8.472  24.549  -1.890  1.00 49.05           O  
ANISOU  337  O   LEU A  42     4786   6192   7658   -891  -1720    346       O  
ATOM    338  N   LEU A  43      -8.976  26.422  -0.776  1.00 43.47           N  
ANISOU  338  N   LEU A  43     4016   5801   6700   -725  -1337    539       N  
ATOM    339  CA  LEU A  43      -7.787  27.107  -1.277  1.00 37.51           C  
ANISOU  339  CA  LEU A  43     3518   4994   5741   -562  -1285    390       C  
ATOM    340  CB  LEU A  43      -7.864  28.600  -0.924  1.00 57.30           C  
ANISOU  340  CB  LEU A  43     6078   7656   8038   -391  -1058    431       C  
ATOM    341  CG  LEU A  43      -9.070  29.323  -1.546  1.00 45.21           C  
ANISOU  341  CG  LEU A  43     4397   6296   6487   -268  -1066    435       C  
ATOM    342  CD1 LEU A  43      -9.185  30.755  -1.055  1.00 47.96           C  
ANISOU  342  CD1 LEU A  43     4806   6761   6655    -91   -830    486       C  
ATOM    343  CD2 LEU A  43      -8.956  29.314  -3.067  1.00 37.85           C  
ANISOU  343  CD2 LEU A  43     3528   5337   5514   -171  -1256    263       C  
ATOM    344  C   LEU A  43      -6.518  26.456  -0.718  1.00 55.69           C  
ANISOU  344  C   LEU A  43     5977   7125   8059   -640  -1274    391       C  
ATOM    345  O   LEU A  43      -5.536  26.240  -1.448  1.00 46.92           O  
ANISOU  345  O   LEU A  43     5027   5897   6902   -578  -1356    242       O  
ATOM    346  N   ALA A  44      -6.551  26.119   0.569  1.00 36.72           N  
ANISOU  346  N   ALA A  44     3515   4725   5714   -766  -1171    571       N  
ATOM    347  CA  ALA A  44      -5.405  25.500   1.237  1.00 41.40           C  
ANISOU  347  CA  ALA A  44     4233   5177   6322   -840  -1161    612       C  
ATOM    348  CB  ALA A  44      -5.702  25.290   2.710  1.00 55.46           C  
ANISOU  348  CB  ALA A  44     5920   7024   8128   -965  -1029    845       C  
ATOM    349  C   ALA A  44      -5.037  24.180   0.587  1.00 37.73           C  
ANISOU  349  C   ALA A  44     3790   4490   6055   -924  -1385    525       C  
ATOM    350  O   ALA A  44      -3.857  23.781   0.516  1.00 43.06           O  
ANISOU  350  O   ALA A  44     4615   5029   6718   -895  -1420    461       O  
ATOM    351  N   LEU A  45      -6.064  23.477   0.135  1.00 38.86           N  
ANISOU  351  N   LEU A  45     3777   4594   6393  -1028  -1544    523       N  
ATOM    352  CA  LEU A  45      -5.852  22.196  -0.500  1.00 40.24           C  
ANISOU  352  CA  LEU A  45     3982   4531   6778  -1115  -1780    418       C  
ATOM    353  CB  LEU A  45      -7.180  21.483  -0.725  1.00 54.73           C  
ANISOU  353  CB  LEU A  45     5602   6339   8852  -1286  -1947    466       C  
ATOM    354  CG  LEU A  45      -7.048  20.070  -1.260  1.00 44.93           C  
ANISOU  354  CG  LEU A  45     4399   4806   7868  -1410  -2210    361       C  
ATOM    355  CD1 LEU A  45      -6.190  19.219  -0.328  1.00 62.62           C  
ANISOU  355  CD1 LEU A  45     6722   6842  10228  -1499  -2179    499       C  
ATOM    356  CD2 LEU A  45      -8.439  19.469  -1.446  1.00 57.31           C  
ANISOU  356  CD2 LEU A  45     5730   6363   9684  -1612  -2384    422       C  
ATOM    357  C   LEU A  45      -5.142  22.426  -1.817  1.00 66.72           C  
ANISOU  357  C   LEU A  45     7508   7840  10004   -934  -1872    150       C  
ATOM    358  O   LEU A  45      -4.254  21.663  -2.202  1.00 39.51           O  
ANISOU  358  O   LEU A  45     4196   4203   6615   -908  -1977     32       O  
ATOM    359  N   GLU A  46      -5.525  23.496  -2.504  1.00 38.64           N  
ANISOU  359  N   GLU A  46     3946   4469   6266   -792  -1821     66       N  
ATOM    360  CA  GLU A  46      -4.956  23.743  -3.813  1.00 55.08           C  
ANISOU  360  CA  GLU A  46     6178   6544   8205   -618  -1903   -166       C  
ATOM    361  CB  GLU A  46      -5.783  24.742  -4.602  1.00 50.53           C  
ANISOU  361  CB  GLU A  46     5541   6172   7485   -499  -1899   -218       C  
ATOM    362  CG  GLU A  46      -5.227  24.937  -5.988  1.00 47.54           C  
ANISOU  362  CG  GLU A  46     5316   5806   6940   -319  -1989   -439       C  
ATOM    363  CD  GLU A  46      -6.181  25.628  -6.913  1.00 66.50           C  
ANISOU  363  CD  GLU A  46     7643   8389   9234   -218  -2059   -494       C  
ATOM    364  OE1 GLU A  46      -6.920  26.527  -6.445  1.00 49.81           O  
ANISOU  364  OE1 GLU A  46     5411   6430   7083   -200  -1933   -347       O  
ATOM    365  OE2 GLU A  46      -6.193  25.259  -8.107  1.00 69.63           O  
ANISOU  365  OE2 GLU A  46     8103   8778   9576   -144  -2245   -687       O  
ATOM    366  C   GLU A  46      -3.519  24.243  -3.722  1.00 54.29           C  
ANISOU  366  C   GLU A  46     6266   6433   7927   -485  -1756   -197       C  
ATOM    367  O   GLU A  46      -2.710  23.935  -4.598  1.00 36.53           O  
ANISOU  367  O   GLU A  46     4150   4108   5623   -375  -1832   -367       O  
ATOM    368  N   ILE A  47      -3.231  25.033  -2.689  1.00 34.61           N  
ANISOU  368  N   ILE A  47     3777   4032   5340   -491  -1549    -39       N  
ATOM    369  CA  ILE A  47      -1.865  25.471  -2.389  1.00 32.91           C  
ANISOU  369  CA  ILE A  47     3710   3806   4989   -414  -1419    -35       C  
ATOM    370  CB  ILE A  47      -1.802  26.332  -1.139  1.00 41.38           C  
ANISOU  370  CB  ILE A  47     4774   4982   5968   -455  -1221    134       C  
ATOM    371  CG1 ILE A  47      -2.543  27.659  -1.369  1.00 31.42           C  
ANISOU  371  CG1 ILE A  47     3492   3887   4557   -356  -1108    135       C  
ATOM    372  CD1 ILE A  47      -2.676  28.486  -0.103  1.00 37.13           C  
ANISOU  372  CD1 ILE A  47     4212   4706   5191   -388   -919    276       C  
ATOM    373  CG2 ILE A  47      -0.341  26.554  -0.708  1.00 36.16           C  
ANISOU  373  CG2 ILE A  47     4242   4287   5210   -425  -1134    149       C  
ATOM    374  C   ILE A  47      -1.017  24.220  -2.181  1.00 44.38           C  
ANISOU  374  C   ILE A  47     5210   5063   6590   -474  -1519    -49       C  
ATOM    375  O   ILE A  47       0.032  24.072  -2.772  1.00 42.37           O  
ANISOU  375  O   ILE A  47     5069   4754   6277   -363  -1535   -162       O  
ATOM    376  N   LEU A  48      -1.522  23.305  -1.360  1.00 40.16           N  
ANISOU  376  N   LEU A  48     4577   4427   6256   -641  -1582     79       N  
ATOM    377  CA  LEU A  48      -0.764  22.103  -1.030  1.00 50.58           C  
ANISOU  377  CA  LEU A  48     5940   5536   7740   -698  -1674    102       C  
ATOM    378  CB  LEU A  48      -1.496  21.265   0.011  1.00 42.14           C  
ANISOU  378  CB  LEU A  48     4745   4381   6886   -904  -1716    307       C  
ATOM    379  CG  LEU A  48      -0.770  20.006   0.507  1.00 64.20           C  
ANISOU  379  CG  LEU A  48     7582   6938   9874   -972  -1808    383       C  
ATOM    380  CD1 LEU A  48      -1.148  19.684   1.941  1.00 74.57           C  
ANISOU  380  CD1 LEU A  48     8790   8265  11277  -1149  -1737    677       C  
ATOM    381  CD2 LEU A  48      -1.112  18.846  -0.387  1.00 42.07           C  
ANISOU  381  CD2 LEU A  48     4791   3890   7302  -1004  -2040    231       C  
ATOM    382  C   LEU A  48      -0.500  21.318  -2.298  1.00 36.69           C  
ANISOU  382  C   LEU A  48     4263   3621   6057   -606  -1856   -130       C  
ATOM    383  O   LEU A  48       0.627  20.949  -2.579  1.00 43.63           O  
ANISOU  383  O   LEU A  48     5253   4406   6920   -498  -1868   -213       O  
ATOM    384  N   ALA A  49      -1.544  21.100  -3.084  1.00 38.09           N  
ANISOU  384  N   ALA A  49     4381   3789   6303   -637  -2000   -243       N  
ATOM    385  CA  ALA A  49      -1.417  20.325  -4.311  1.00 51.33           C  
ANISOU  385  CA  ALA A  49     6148   5318   8036   -553  -2198   -494       C  
ATOM    386  CB  ALA A  49      -2.774  20.156  -4.972  1.00 60.50           C  
ANISOU  386  CB  ALA A  49     7207   6500   9280   -638  -2373   -581       C  
ATOM    387  C   ALA A  49      -0.421  20.948  -5.289  1.00 51.22           C  
ANISOU  387  C   ALA A  49     6282   5407   7773   -311  -2128   -671       C  
ATOM    388  O   ALA A  49       0.309  20.222  -5.984  1.00 39.76           O  
ANISOU  388  O   ALA A  49     4949   3818   6341   -196  -2221   -848       O  
ATOM    389  N   LEU A  50      -0.362  22.281  -5.327  1.00 40.97           N  
ANISOU  389  N   LEU A  50     4978   4342   6246   -229  -1955   -613       N  
ATOM    390  CA  LEU A  50       0.542  22.962  -6.236  1.00 44.93           C  
ANISOU  390  CA  LEU A  50     5599   4959   6512    -18  -1869   -735       C  
ATOM    391  CB  LEU A  50       0.098  24.411  -6.452  1.00 52.27           C  
ANISOU  391  CB  LEU A  50     6505   6121   7235     41  -1736   -675       C  
ATOM    392  CG  LEU A  50      -1.207  24.615  -7.224  1.00 64.60           C  
ANISOU  392  CG  LEU A  50     7999   7773   8772     47  -1860   -752       C  
ATOM    393  CD1 LEU A  50      -1.530  26.101  -7.397  1.00 59.05           C  
ANISOU  393  CD1 LEU A  50     7286   7282   7868    137  -1710   -669       C  
ATOM    394  CD2 LEU A  50      -1.146  23.928  -8.562  1.00 45.38           C  
ANISOU  394  CD2 LEU A  50     5651   5296   6293    162  -2045   -998       C  
ATOM    395  C   LEU A  50       1.987  22.921  -5.724  1.00 40.97           C  
ANISOU  395  C   LEU A  50     5165   4420   5983     40  -1741   -671       C  
ATOM    396  O   LEU A  50       2.918  22.906  -6.515  1.00 36.83           O  
ANISOU  396  O   LEU A  50     4732   3917   5343    210  -1717   -793       O  
ATOM    397  N   ILE A  51       2.165  22.930  -4.406  1.00 33.97           N  
ANISOU  397  N   ILE A  51     4221   3503   5185    -94  -1658   -470       N  
ATOM    398  CA  ILE A  51       3.488  22.784  -3.827  1.00 33.34           C  
ANISOU  398  CA  ILE A  51     4178   3387   5102    -60  -1572   -392       C  
ATOM    399  CB  ILE A  51       3.478  23.049  -2.304  1.00 50.14           C  
ANISOU  399  CB  ILE A  51     6238   5542   7271   -221  -1478   -156       C  
ATOM    400  CG1 ILE A  51       3.217  24.532  -2.014  1.00 36.69           C  
ANISOU  400  CG1 ILE A  51     4526   4040   5373   -232  -1317    -83       C  
ATOM    401  CD1 ILE A  51       3.037  24.778  -0.576  1.00 30.31           C  
ANISOU  401  CD1 ILE A  51     3668   3270   4577   -377  -1236    112       C  
ATOM    402  CG2 ILE A  51       4.815  22.672  -1.665  1.00 51.89           C  
ANISOU  402  CG2 ILE A  51     6481   5712   7522   -200  -1440    -68       C  
ATOM    403  C   ILE A  51       4.060  21.403  -4.107  1.00 37.65           C  
ANISOU  403  C   ILE A  51     4770   3717   5817     -4  -1708   -492       C  
ATOM    404  O   ILE A  51       5.263  21.247  -4.332  1.00 47.46           O  
ANISOU  404  O   ILE A  51     6063   4953   7015    133  -1660   -529       O  
ATOM    405  N   GLU A  52       3.201  20.393  -4.085  1.00 39.43           N  
ANISOU  405  N   GLU A  52     4972   3758   6251   -107  -1879   -529       N  
ATOM    406  CA  GLU A  52       3.663  19.056  -4.380  1.00 38.80           C  
ANISOU  406  CA  GLU A  52     4960   3426   6357    -50  -2025   -641       C  
ATOM    407  CB  GLU A  52       2.531  18.064  -4.212  1.00 40.81           C  
ANISOU  407  CB  GLU A  52     5172   3464   6869   -227  -2219   -643       C  
ATOM    408  CG  GLU A  52       2.119  17.863  -2.779  1.00 47.05           C  
ANISOU  408  CG  GLU A  52     5850   4211   7818   -447  -2183   -352       C  
ATOM    409  CD  GLU A  52       1.145  16.707  -2.653  1.00 70.81           C  
ANISOU  409  CD  GLU A  52     8812   6966  11125   -629  -2384   -335       C  
ATOM    410  OE1 GLU A  52       0.418  16.455  -3.633  1.00 89.45           O  
ANISOU  410  OE1 GLU A  52    11191   9270  13528   -631  -2541   -540       O  
ATOM    411  OE2 GLU A  52       1.108  16.058  -1.592  1.00 79.97           O  
ANISOU  411  OE2 GLU A  52     9918   7990  12477   -777  -2394   -110       O  
ATOM    412  C   GLU A  52       4.237  18.984  -5.787  1.00 61.49           C  
ANISOU  412  C   GLU A  52     7951   6320   9094    189  -2057   -911       C  
ATOM    413  O   GLU A  52       5.360  18.520  -5.992  1.00 47.57           O  
ANISOU  413  O   GLU A  52     6252   4490   7334    349  -2031   -972       O  
ATOM    414  N   LYS A  53       3.462  19.479  -6.739  1.00 39.86           N  
ANISOU  414  N   LYS A  53     5228   3699   6218    226  -2104  -1060       N  
ATOM    415  CA  LYS A  53       3.821  19.486  -8.153  1.00 56.02           C  
ANISOU  415  CA  LYS A  53     7389   5809   8086    453  -2139  -1320       C  
ATOM    416  CB  LYS A  53       2.647  20.019  -8.984  1.00 57.71           C  
ANISOU  416  CB  LYS A  53     7592   6158   8176    433  -2229  -1430       C  
ATOM    417  CG  LYS A  53       2.967  20.324 -10.443  1.00 92.33           C  
ANISOU  417  CG  LYS A  53    12093  10694  12294    676  -2233  -1661       C  
ATOM    418  CD  LYS A  53       1.698  20.329 -11.289  1.00107.19           C  
ANISOU  418  CD  LYS A  53    13976  12625  14126    642  -2426  -1816       C  
ATOM    419  CE  LYS A  53       1.802  21.279 -12.478  1.00 94.56           C  
ANISOU  419  CE  LYS A  53    12441  11306  12182    847  -2354  -1911       C  
ATOM    420  NZ  LYS A  53       1.854  22.714 -12.071  1.00 80.73           N  
ANISOU  420  NZ  LYS A  53    10610   9779  10286    831  -2130  -1667       N  
ATOM    421  C   LYS A  53       5.069  20.318  -8.424  1.00 59.40           C  
ANISOU  421  C   LYS A  53     7846   6441   8283    640  -1926  -1285       C  
ATOM    422  O   LYS A  53       5.956  19.897  -9.159  1.00 64.08           O  
ANISOU  422  O   LYS A  53     8524   7020   8804    849  -1913  -1437       O  
ATOM    423  N   LYS A  54       5.132  21.502  -7.831  1.00 46.28           N  
ANISOU  423  N   LYS A  54     6110   4967   6508    566  -1756  -1084       N  
ATOM    424  CA  LYS A  54       6.257  22.403  -8.082  1.00 48.03           C  
ANISOU  424  CA  LYS A  54     6341   5384   6525    703  -1559  -1026       C  
ATOM    425  CB  LYS A  54       6.032  23.758  -7.406  1.00 47.52           C  
ANISOU  425  CB  LYS A  54     6211   5483   6362    579  -1411   -823       C  
ATOM    426  CG  LYS A  54       7.172  24.758  -7.645  1.00 37.71           C  
ANISOU  426  CG  LYS A  54     4972   4424   4933    681  -1218   -743       C  
ATOM    427  CD  LYS A  54       6.696  26.182  -7.424  1.00 78.17           C  
ANISOU  427  CD  LYS A  54    10081   9690   9931    597  -1105   -616       C  
ATOM    428  CE  LYS A  54       7.183  27.099  -8.530  1.00 76.20           C  
ANISOU  428  CE  LYS A  54     9877   9622   9453    753   -986   -638       C  
ATOM    429  NZ  LYS A  54       6.377  28.349  -8.582  1.00 50.51           N  
ANISOU  429  NZ  LYS A  54     6637   6464   6093    703   -924   -555       N  
ATOM    430  C   LYS A  54       7.571  21.803  -7.609  1.00 56.56           C  
ANISOU  430  C   LYS A  54     7409   6387   7695    773  -1503   -971       C  
ATOM    431  O   LYS A  54       8.552  21.765  -8.351  1.00 53.57           O  
ANISOU  431  O   LYS A  54     7065   6089   7202    976  -1428  -1057       O  
ATOM    432  N   PHE A  55       7.582  21.316  -6.377  1.00 47.08           N  
ANISOU  432  N   PHE A  55     6148   5045   6693    616  -1538   -816       N  
ATOM    433  CA  PHE A  55       8.812  20.832  -5.775  1.00 49.14           C  
ANISOU  433  CA  PHE A  55     6374   5253   7043    670  -1490   -718       C  
ATOM    434  CB  PHE A  55       8.863  21.257  -4.315  1.00 45.01           C  
ANISOU  434  CB  PHE A  55     5764   4759   6579    466  -1433   -460       C  
ATOM    435  CG  PHE A  55       8.880  22.757  -4.137  1.00 62.24           C  
ANISOU  435  CG  PHE A  55     7914   7172   8561    397  -1281   -359       C  
ATOM    436  CD1 PHE A  55      10.083  23.447  -4.100  1.00 32.51           C  
ANISOU  436  CD1 PHE A  55     4109   3560   4682    457  -1148   -279       C  
ATOM    437  CE1 PHE A  55      10.109  24.838  -3.952  1.00 61.99           C  
ANISOU  437  CE1 PHE A  55     7832   7467   8256    381  -1021   -192       C  
ATOM    438  CZ  PHE A  55       8.920  25.545  -3.844  1.00 43.59           C  
ANISOU  438  CZ  PHE A  55     5535   5159   5867    276  -1016   -189       C  
ATOM    439  CE2 PHE A  55       7.711  24.864  -3.887  1.00 44.24           C  
ANISOU  439  CE2 PHE A  55     5634   5122   6052    233  -1138   -260       C  
ATOM    440  CD2 PHE A  55       7.697  23.476  -4.036  1.00 63.45           C  
ANISOU  440  CD2 PHE A  55     8073   7380   8655    278  -1275   -343       C  
ATOM    441  C   PHE A  55       8.955  19.324  -5.908  1.00 55.50           C  
ANISOU  441  C   PHE A  55     7235   5792   8062    755  -1643   -837       C  
ATOM    442  O   PHE A  55       9.744  18.706  -5.190  1.00 47.67           O  
ANISOU  442  O   PHE A  55     6204   4697   7210    771  -1645   -723       O  
ATOM    443  N   LYS A  56       8.201  18.768  -6.856  1.00 50.84           N  
ANISOU  443  N   LYS A  56     6737   5090   7489    815  -1781  -1068       N  
ATOM    444  CA  LYS A  56       8.178  17.342  -7.151  1.00 51.01           C  
ANISOU  444  CA  LYS A  56     6847   4817   7718    895  -1956  -1235       C  
ATOM    445  CB  LYS A  56       9.298  16.969  -8.127  1.00 53.98           C  
ANISOU  445  CB  LYS A  56     7303   5216   7992   1211  -1904  -1429       C  
ATOM    446  CG  LYS A  56       8.964  17.301  -9.579  1.00 59.02           C  
ANISOU  446  CG  LYS A  56     8042   5994   8388   1374  -1916  -1697       C  
ATOM    447  CD  LYS A  56      10.040  16.822 -10.536  1.00 68.82           C  
ANISOU  447  CD  LYS A  56     9369   7262   9519   1709  -1856  -1900       C  
ATOM    448  CE  LYS A  56       9.553  15.648 -11.375  1.00100.18           C  
ANISOU  448  CE  LYS A  56    13516  10976  13573   1827  -2073  -2234       C  
ATOM    449  NZ  LYS A  56       8.230  15.923 -11.994  1.00110.99           N  
ANISOU  449  NZ  LYS A  56    14943  12377  14851   1700  -2223  -2378       N  
ATOM    450  C   LYS A  56       8.293  16.545  -5.871  1.00 59.79           C  
ANISOU  450  C   LYS A  56     7905   5706   9105    751  -2017  -1031       C  
ATOM    451  O   LYS A  56       9.308  15.916  -5.622  1.00 52.59           O  
ANISOU  451  O   LYS A  56     6998   4694   8289    883  -1999   -995       O  
ATOM    452  N   VAL A  57       7.256  16.611  -5.046  1.00 65.39           N  
ANISOU  452  N   VAL A  57     8552   6363   9929    489  -2078   -875       N  
ATOM    453  CA  VAL A  57       7.309  16.047  -3.707  1.00 49.08           C  
ANISOU  453  CA  VAL A  57     6420   4148   8078    328  -2105   -620       C  
ATOM    454  CB  VAL A  57       7.963  17.044  -2.736  1.00 70.71           C  
ANISOU  454  CB  VAL A  57     9058   7137  10670    272  -1922   -372       C  
ATOM    455  CG1 VAL A  57       7.204  18.360  -2.729  1.00 66.53           C  
ANISOU  455  CG1 VAL A  57     8483   6859   9936    156  -1820   -338       C  
ATOM    456  CG2 VAL A  57       8.072  16.463  -1.351  1.00 84.49           C  
ANISOU  456  CG2 VAL A  57    10742   8763  12597    125  -1953   -102       C  
ATOM    457  C   VAL A  57       5.906  15.662  -3.226  1.00 72.37           C  
ANISOU  457  C   VAL A  57     9332   6957  11209     71  -2235   -541       C  
ATOM    458  O   VAL A  57       4.921  16.267  -3.635  1.00 60.02           O  
ANISOU  458  O   VAL A  57     7742   5514   9550    -16  -2247   -608       O  
ATOM    459  N   GLN A  58       5.805  14.639  -2.385  1.00 78.29           N  
ANISOU  459  N   GLN A  58    10067   7453  12227    -48  -2335   -382       N  
ATOM    460  CA  GLN A  58       4.508  14.250  -1.842  1.00 57.46           C  
ANISOU  460  CA  GLN A  58     7362   4692   9778   -313  -2442   -257       C  
ATOM    461  CB  GLN A  58       4.340  12.724  -1.886  1.00 49.32           C  
ANISOU  461  CB  GLN A  58     6402   3245   9092   -356  -2654   -296       C  
ATOM    462  CG  GLN A  58       4.057  12.164  -3.271  1.00104.46           C  
ANISOU  462  CG  GLN A  58    13516  10044  16130   -243  -2831   -663       C  
ATOM    463  CD  GLN A  58       2.709  12.605  -3.813  1.00128.71           C  
ANISOU  463  CD  GLN A  58    16530  13221  19155   -402  -2913   -768       C  
ATOM    464  OE1 GLN A  58       2.552  12.834  -5.012  1.00128.89           O  
ANISOU  464  OE1 GLN A  58    16632  13308  19033   -274  -2977  -1063       O  
ATOM    465  NE2 GLN A  58       1.728  12.725  -2.928  1.00124.21           N  
ANISOU  465  NE2 GLN A  58    15809  12689  18696   -673  -2909   -514       N  
ATOM    466  C   GLN A  58       4.323  14.775  -0.417  1.00 55.83           C  
ANISOU  466  C   GLN A  58     7029   4649   9535   -496  -2312     86       C  
ATOM    467  O   GLN A  58       5.206  14.667   0.419  1.00 56.70           O  
ANISOU  467  O   GLN A  58     7127   4772   9645   -464  -2242    270       O  
ATOM    468  N   ILE A  59       3.172  15.384  -0.161  1.00 63.12           N  
ANISOU  468  N   ILE A  59     7855   5721  10406   -673  -2278    164       N  
ATOM    469  CA  ILE A  59       2.854  15.906   1.166  1.00 42.62           C  
ANISOU  469  CA  ILE A  59     5146   3298   7748   -836  -2146    467       C  
ATOM    470  CB  ILE A  59       2.667  17.444   1.165  1.00 39.98           C  
ANISOU  470  CB  ILE A  59     4772   3311   7107   -807  -1967    449       C  
ATOM    471  CG1 ILE A  59       3.899  18.162   0.604  1.00 64.60           C  
ANISOU  471  CG1 ILE A  59     7976   6558  10009   -593  -1873    307       C  
ATOM    472  CD1 ILE A  59       3.640  19.635   0.277  1.00 50.12           C  
ANISOU  472  CD1 ILE A  59     6133   5003   7909   -553  -1731    240       C  
ATOM    473  CG2 ILE A  59       2.315  17.939   2.563  1.00 64.74           C  
ANISOU  473  CG2 ILE A  59     7814   6619  10167   -959  -1833    735       C  
ATOM    474  C   ILE A  59       1.567  15.268   1.653  1.00 68.93           C  
ANISOU  474  C   ILE A  59     8373   6510  11305  -1078  -2237    624       C  
ATOM    475  O   ILE A  59       0.544  15.368   0.982  1.00 67.24           O  
ANISOU  475  O   ILE A  59     8111   6305  11132  -1146  -2312    500       O  
ATOM    476  N   PRO A  60       1.601  14.620   2.824  1.00103.60           N  
ANISOU  476  N   PRO A  60    12714  10806  15843  -1212  -2232    916       N  
ATOM    477  CA  PRO A  60       0.361  14.019   3.320  1.00 89.05           C  
ANISOU  477  CA  PRO A  60    10747   8864  14223  -1460  -2301   1107       C  
ATOM    478  CB  PRO A  60       0.795  13.334   4.617  1.00 66.92           C  
ANISOU  478  CB  PRO A  60     7926   5970  11531  -1549  -2273   1445       C  
ATOM    479  CG  PRO A  60       2.011  14.086   5.047  1.00 67.27           C  
ANISOU  479  CG  PRO A  60     8036   6223  11301  -1377  -2129   1463       C  
ATOM    480  CD  PRO A  60       2.712  14.476   3.778  1.00 77.69           C  
ANISOU  480  CD  PRO A  60     9466   7539  12514  -1155  -2158   1114       C  
ATOM    481  C   PRO A  60      -0.697  15.084   3.579  1.00103.00           C  
ANISOU  481  C   PRO A  60    12373  10947  15814  -1557  -2164   1173       C  
ATOM    482  O   PRO A  60      -0.361  16.189   4.001  1.00 90.51           O  
ANISOU  482  O   PRO A  60    10794   9649  13949  -1474  -1981   1206       O  
ATOM    483  N   GLU A  61      -1.956  14.753   3.312  1.00 98.42           N  
ANISOU  483  N   GLU A  61    11670  10312  15412  -1727  -2259   1187       N  
ATOM    484  CA  GLU A  61      -3.049  15.705   3.457  1.00 98.46           C  
ANISOU  484  CA  GLU A  61    11518  10613  15279  -1797  -2139   1242       C  
ATOM    485  CB  GLU A  61      -4.350  15.096   2.928  1.00103.28           C  
ANISOU  485  CB  GLU A  61    11988  11116  16140  -1972  -2302   1220       C  
ATOM    486  CG  GLU A  61      -5.067  15.957   1.896  1.00103.45           C  
ANISOU  486  CG  GLU A  61    11950  11317  16040  -1907  -2331    989       C  
ATOM    487  CD  GLU A  61      -5.801  15.133   0.849  1.00122.38           C  
ANISOU  487  CD  GLU A  61    14336  13534  18627  -1959  -2558    800       C  
ATOM    488  OE1 GLU A  61      -6.893  14.608   1.160  1.00118.09           O  
ANISOU  488  OE1 GLU A  61    13640  13000  18230  -2119  -2576    954       O  
ATOM    489  OE2 GLU A  61      -5.297  15.031  -0.291  1.00116.90           O  
ANISOU  489  OE2 GLU A  61    13796  12717  17904  -1822  -2704    490       O  
ATOM    490  C   GLU A  61      -3.224  16.152   4.906  1.00 84.81           C  
ANISOU  490  C   GLU A  61     9688   9114  13420  -1880  -1926   1570       C  
ATOM    491  O   GLU A  61      -3.748  17.234   5.169  1.00 74.55           O  
ANISOU  491  O   GLU A  61     8310   8112  11904  -1850  -1759   1596       O  
ATOM    492  N   GLU A  62      -2.766  15.331   5.846  1.00 57.69           N  
ANISOU  492  N   GLU A  62     6270   5545  10106  -1966  -1932   1817       N  
ATOM    493  CA  GLU A  62      -2.861  15.681   7.259  1.00 51.05           C  
ANISOU  493  CA  GLU A  62     5353   4933   9112  -2035  -1738   2134       C  
ATOM    494  CB  GLU A  62      -2.436  14.514   8.145  1.00 80.45           C  
ANISOU  494  CB  GLU A  62     9102   8484  12980  -2101  -1780   2390       C  
ATOM    495  CG  GLU A  62      -1.365  13.614   7.553  1.00106.51           C  
ANISOU  495  CG  GLU A  62    12563  11454  16451  -1998  -1959   2249       C  
ATOM    496  CD  GLU A  62      -1.946  12.542   6.647  1.00126.06           C  
ANISOU  496  CD  GLU A  62    15040  13648  19210  -2034  -2150   2095       C  
ATOM    497  OE1 GLU A  62      -2.944  12.826   5.952  1.00132.74           O  
ANISOU  497  OE1 GLU A  62    15800  14549  20086  -2093  -2183   1958       O  
ATOM    498  OE2 GLU A  62      -1.411  11.414   6.634  1.00127.00           O  
ANISOU  498  OE2 GLU A  62    15244  13494  19515  -2001  -2272   2112       O  
ATOM    499  C   GLU A  62      -2.021  16.918   7.587  1.00 76.13           C  
ANISOU  499  C   GLU A  62     8635   8377  11914  -1852  -1563   2050       C  
ATOM    500  O   GLU A  62      -2.200  17.530   8.635  1.00 88.37           O  
ANISOU  500  O   GLU A  62    10138  10180  13258  -1875  -1385   2235       O  
ATOM    501  N   LYS A  63      -1.114  17.283   6.684  1.00 74.28           N  
ANISOU  501  N   LYS A  63     8544   8087  11592  -1673  -1615   1771       N  
ATOM    502  CA  LYS A  63      -0.272  18.462   6.874  1.00 65.27           C  
ANISOU  502  CA  LYS A  63     7501   7168  10130  -1519  -1472   1678       C  
ATOM    503  C   LYS A  63      -1.016  19.757   6.568  1.00 52.62           C  
ANISOU  503  C   LYS A  63     5858   5813   8323  -1466  -1340   1555       C  
ATOM    504  O   LYS A  63      -0.436  20.845   6.616  1.00 52.77           O  
ANISOU  504  O   LYS A  63     5965   5997   8089  -1347  -1227   1456       O  
ATOM    505  CB  LYS A  63       0.979  18.364   5.999  1.00 30.00           C  
ATOM    506  CG  LYS A  63       1.863  17.166   6.310  1.00 30.00           C  
ATOM    507  CD  LYS A  63       2.436  17.251   7.715  1.00 30.00           C  
ATOM    508  CE  LYS A  63       3.377  16.092   7.999  1.00 30.00           C  
ATOM    509  NZ  LYS A  63       3.927  16.150   9.381  1.00 30.00           N  
ATOM    510  N   LEU A  64      -2.297  19.646   6.251  1.00 53.09           N  
ANISOU  510  N   LEU A  64     5778   5888   8504  -1556  -1362   1569       N  
ATOM    511  CA  LEU A  64      -3.118  20.828   6.024  1.00 72.37           C  
ANISOU  511  CA  LEU A  64     8158   8568  10773  -1495  -1234   1487       C  
ATOM    512  CB  LEU A  64      -4.514  20.434   5.549  1.00 72.16           C  
ANISOU  512  CB  LEU A  64     7943   8526  10950  -1607  -1312   1512       C  
ATOM    513  CG  LEU A  64      -4.655  20.060   4.075  1.00 91.62           C  
ANISOU  513  CG  LEU A  64    10430  10816  13566  -1571  -1520   1259       C  
ATOM    514  CD1 LEU A  64      -6.107  19.765   3.757  1.00101.15           C  
ANISOU  514  CD1 LEU A  64    11419  12053  14959  -1706  -1600   1310       C  
ATOM    515  CD2 LEU A  64      -4.136  21.166   3.183  1.00 69.14           C  
ANISOU  515  CD2 LEU A  64     7714   8069  10485  -1357  -1475   1005       C  
ATOM    516  C   LEU A  64      -3.207  21.665   7.294  1.00 77.29           C  
ANISOU  516  C   LEU A  64     8768   9447  11151  -1489  -1013   1655       C  
ATOM    517  O   LEU A  64      -3.431  22.872   7.235  1.00 86.64           O  
ANISOU  517  O   LEU A  64     9977  10819  12122  -1378   -879   1556       O  
ATOM    518  N   VAL A  65      -3.015  21.013   8.439  1.00 71.46           N  
ANISOU  518  N   VAL A  65     8004   8708  10438  -1600   -982   1908       N  
ATOM    519  CA  VAL A  65      -2.967  21.691   9.733  1.00 78.54           C  
ANISOU  519  CA  VAL A  65     8918   9852  11073  -1590   -786   2066       C  
ATOM    520  CB  VAL A  65      -2.610  20.709  10.876  1.00 99.09           C  
ANISOU  520  CB  VAL A  65    11505  12417  13729  -1715   -800   2363       C  
ATOM    521  CG1 VAL A  65      -1.377  19.875  10.528  1.00100.87           C  
ANISOU  521  CG1 VAL A  65    11846  12384  14095  -1701   -980   2320       C  
ATOM    522  CG2 VAL A  65      -2.412  21.452  12.187  1.00105.07           C  
ANISOU  522  CG2 VAL A  65    12313  13448  14159  -1683   -614   2491       C  
ATOM    523  C   VAL A  65      -1.945  22.827   9.737  1.00 79.81           C  
ANISOU  523  C   VAL A  65     9263  10107  10954  -1437   -716   1881       C  
ATOM    524  O   VAL A  65      -2.122  23.845  10.411  1.00 63.80           O  
ANISOU  524  O   VAL A  65     7271   8297   8672  -1379   -549   1882       O  
ATOM    525  N   ASP A  66      -0.894  22.665   8.942  1.00 67.46           N  
ANISOU  525  N   ASP A  66     7812   8374   9445  -1369   -844   1715       N  
ATOM    526  CA  ASP A  66       0.265  23.537   9.027  1.00 95.07           C  
ANISOU  526  CA  ASP A  66    11465  11935  12721  -1265   -804   1589       C  
ATOM    527  CB  ASP A  66       1.535  22.690   8.795  1.00110.75           C  
ANISOU  527  CB  ASP A  66    13515  13738  14826  -1254   -953   1586       C  
ATOM    528  CG  ASP A  66       1.747  21.645   9.901  1.00121.18           C  
ANISOU  528  CG  ASP A  66    14796  15023  16224  -1364   -995   1861       C  
ATOM    529  OD1 ASP A  66       1.249  21.887  11.016  1.00128.46           O  
ANISOU  529  OD1 ASP A  66    15684  16126  17000  -1432   -880   2039       O  
ATOM    530  OD2 ASP A  66       2.426  20.613   9.678  1.00104.85           O  
ANISOU  530  OD2 ASP A  66    12738  12753  14347  -1366  -1135   1906       O  
ATOM    531  C   ASP A  66       0.146  24.721   8.048  1.00 75.80           C  
ANISOU  531  C   ASP A  66     9084   9544  10172  -1136   -753   1342       C  
ATOM    532  O   ASP A  66       0.882  25.709   8.170  1.00109.04           O  
ANISOU  532  O   ASP A  66    13414  13834  14183  -1064   -687   1243       O  
ATOM    533  N   ILE A  67      -0.820  24.646   7.130  1.00 56.48           N  
ANISOU  533  N   ILE A  67     6548   7056   7855  -1118   -787   1260       N  
ATOM    534  CA  ILE A  67      -0.994  25.692   6.123  1.00 54.25           C  
ANISOU  534  CA  ILE A  67     6315   6815   7482   -987   -751   1052       C  
ATOM    535  CB  ILE A  67      -1.633  25.114   4.851  1.00 48.04           C  
ANISOU  535  CB  ILE A  67     5447   5912   6892   -974   -890    946       C  
ATOM    536  CG1 ILE A  67      -0.908  23.832   4.438  1.00 74.39           C  
ANISOU  536  CG1 ILE A  67     8809   9032  10425  -1018  -1066    928       C  
ATOM    537  CD1 ILE A  67      -1.094  23.458   2.984  1.00 84.21           C  
ANISOU  537  CD1 ILE A  67    10055  10151  11791   -953  -1215    732       C  
ATOM    538  CG2 ILE A  67      -1.604  26.110   3.722  1.00 43.00           C  
ANISOU  538  CG2 ILE A  67     4879   5311   6147   -823   -874    744       C  
ATOM    539  C   ILE A  67      -1.841  26.847   6.677  1.00 63.09           C  
ANISOU  539  C   ILE A  67     7416   8134   8421   -939   -571   1073       C  
ATOM    540  O   ILE A  67      -2.997  27.042   6.291  1.00 47.27           O  
ANISOU  540  O   ILE A  67     5296   6193   6470   -913   -542   1066       O  
ATOM    541  N   THR A  68      -1.243  27.585   7.609  1.00 53.42           N  
ANISOU  541  N   THR A  68     6306   7008   6984   -921   -458   1094       N  
ATOM    542  CA  THR A  68      -1.929  28.615   8.379  1.00 53.78           C  
ANISOU  542  CA  THR A  68     6365   7234   6835   -866   -277   1113       C  
ATOM    543  CB  THR A  68      -1.701  28.385   9.879  1.00 40.55           C  
ANISOU  543  CB  THR A  68     4712   5674   5022   -949   -202   1280       C  
ATOM    544  OG1 THR A  68      -0.295  28.322  10.135  1.00 54.78           O  
ANISOU  544  OG1 THR A  68     6650   7410   6754   -983   -282   1250       O  
ATOM    545  CG2 THR A  68      -2.329  27.067  10.325  1.00 60.10           C  
ANISOU  545  CG2 THR A  68     7012   8151   7672  -1080   -243   1510       C  
ATOM    546  C   THR A  68      -1.461  30.034   8.013  1.00 52.39           C  
ANISOU  546  C   THR A  68     6356   7067   6483   -739   -206    927       C  
ATOM    547  O   THR A  68      -2.172  31.015   8.244  1.00 61.65           O  
ANISOU  547  O   THR A  68     7550   8343   7532   -643    -67    886       O  
ATOM    548  N   SER A  69      -0.256  30.131   7.460  1.00 41.95           N  
ANISOU  548  N   SER A  69     5146   5631   5162   -734   -297    827       N  
ATOM    549  CA  SER A  69       0.312  31.417   7.038  1.00 44.93           C  
ANISOU  549  CA  SER A  69     5677   5987   5406   -643   -246    675       C  
ATOM    550  CB  SER A  69       0.894  32.167   8.227  1.00 35.88           C  
ANISOU  550  CB  SER A  69     4670   4911   4052   -676   -167    672       C  
ATOM    551  OG  SER A  69       2.037  31.500   8.727  1.00 44.55           O  
ANISOU  551  OG  SER A  69     5788   5987   5151   -785   -266    737       O  
ATOM    552  C   SER A  69       1.394  31.168   6.000  1.00 63.58           C  
ANISOU  552  C   SER A  69     8078   8226   7854   -636   -366    596       C  
ATOM    553  O   SER A  69       1.836  30.028   5.828  1.00 44.81           O  
ANISOU  553  O   SER A  69     5634   5783   5609   -694   -480    648       O  
ATOM    554  N   LEU A  70       1.844  32.211   5.311  1.00 40.82           N  
ANISOU  554  N   LEU A  70     5302   5308   4899   -559   -333    480       N  
ATOM    555  CA  LEU A  70       2.850  31.981   4.289  1.00 45.38           C  
ANISOU  555  CA  LEU A  70     5897   5802   5542   -538   -422    422       C  
ATOM    556  CB  LEU A  70       3.146  33.250   3.497  1.00 32.36           C  
ANISOU  556  CB  LEU A  70     4356   4129   3811   -451   -360    327       C  
ATOM    557  CG  LEU A  70       4.230  33.119   2.432  1.00 37.25           C  
ANISOU  557  CG  LEU A  70     4985   4697   4470   -421   -420    286       C  
ATOM    558  CD1 LEU A  70       3.805  32.141   1.352  1.00 31.60           C  
ANISOU  558  CD1 LEU A  70     4176   3960   3869   -344   -508    251       C  
ATOM    559  CD2 LEU A  70       4.579  34.463   1.816  1.00 41.44           C  
ANISOU  559  CD2 LEU A  70     5626   5206   4913   -362   -343    237       C  
ATOM    560  C   LEU A  70       4.113  31.434   4.952  1.00 40.09           C  
ANISOU  560  C   LEU A  70     5240   5119   4872   -639   -487    482       C  
ATOM    561  O   LEU A  70       4.741  30.511   4.429  1.00 34.29           O  
ANISOU  561  O   LEU A  70     4448   4326   4253   -637   -585    492       O  
ATOM    562  N   SER A  71       4.460  31.969   6.122  1.00 33.83           N  
ANISOU  562  N   SER A  71     4522   4386   3947   -715   -441    518       N  
ATOM    563  CA  SER A  71       5.644  31.490   6.826  1.00 42.33           C  
ANISOU  563  CA  SER A  71     5598   5477   5010   -812   -520    589       C  
ATOM    564  CB  SER A  71       5.964  32.376   8.031  1.00 36.69           C  
ANISOU  564  CB  SER A  71     4996   4841   4104   -889   -475    586       C  
ATOM    565  OG  SER A  71       6.434  33.646   7.599  1.00 46.87           O  
ANISOU  565  OG  SER A  71     6398   6089   5323   -875   -434    472       O  
ATOM    566  C   SER A  71       5.509  30.040   7.273  1.00 43.12           C  
ANISOU  566  C   SER A  71     5587   5571   5227   -858   -601    721       C  
ATOM    567  O   SER A  71       6.494  29.310   7.281  1.00 38.76           O  
ANISOU  567  O   SER A  71     4994   4985   4750   -885   -697    776       O  
ATOM    568  N   ALA A  72       4.300  29.615   7.639  1.00 42.75           N  
ANISOU  568  N   ALA A  72     5480   5552   5211   -866   -562    787       N  
ATOM    569  CA  ALA A  72       4.092  28.237   8.077  1.00 35.31           C  
ANISOU  569  CA  ALA A  72     4432   4579   4404   -929   -639    940       C  
ATOM    570  CB  ALA A  72       2.788  28.109   8.838  1.00 48.65           C  
ANISOU  570  CB  ALA A  72     6062   6359   6065   -967   -554   1047       C  
ATOM    571  C   ALA A  72       4.106  27.297   6.884  1.00 43.78           C  
ANISOU  571  C   ALA A  72     5433   5503   5699   -881   -746    895       C  
ATOM    572  O   ALA A  72       4.564  26.156   6.973  1.00 48.10           O  
ANISOU  572  O   ALA A  72     5930   5958   6387   -912   -850    981       O  
ATOM    573  N   THR A  73       3.610  27.788   5.759  1.00 34.35           N  
ANISOU  573  N   THR A  73     4244   4280   4526   -792   -724    754       N  
ATOM    574  CA  THR A  73       3.582  26.993   4.552  1.00 39.71           C  
ANISOU  574  CA  THR A  73     4879   4834   5376   -731   -830    672       C  
ATOM    575  CB  THR A  73       2.706  27.653   3.490  1.00 39.46           C  
ANISOU  575  CB  THR A  73     4846   4823   5323   -640   -797    542       C  
ATOM    576  OG1 THR A  73       1.352  27.775   3.980  1.00 37.82           O  
ANISOU  576  OG1 THR A  73     4563   4686   5123   -683   -742    610       O  
ATOM    577  CG2 THR A  73       2.688  26.809   2.235  1.00 40.20           C  
ANISOU  577  CG2 THR A  73     4910   4801   5562   -573   -924    435       C  
ATOM    578  C   THR A  73       5.025  26.778   4.040  1.00 46.37           C  
ANISOU  578  C   THR A  73     5763   5619   6235   -673   -889    618       C  
ATOM    579  O   THR A  73       5.418  25.672   3.692  1.00 35.21           O  
ANISOU  579  O   THR A  73     4315   4090   4973   -650   -995    621       O  
ATOM    580  N   ILE A  74       5.821  27.836   4.018  1.00 38.80           N  
ANISOU  580  N   ILE A  74     4875   4738   5129   -648   -819    574       N  
ATOM    581  CA  ILE A  74       7.221  27.705   3.604  1.00 34.01           C  
ANISOU  581  CA  ILE A  74     4273   4113   4534   -600   -857    551       C  
ATOM    582  CB  ILE A  74       7.922  29.059   3.638  1.00 36.34           C  
ANISOU  582  CB  ILE A  74     4635   4499   4671   -613   -772    520       C  
ATOM    583  CG1 ILE A  74       7.352  29.950   2.539  1.00 30.67           C  
ANISOU  583  CG1 ILE A  74     3969   3787   3899   -522   -699    404       C  
ATOM    584  CD1 ILE A  74       7.564  31.446   2.794  1.00 27.20           C  
ANISOU  584  CD1 ILE A  74     3622   3401   3312   -561   -601    388       C  
ATOM    585  CG2 ILE A  74       9.435  28.893   3.462  1.00 35.61           C  
ANISOU  585  CG2 ILE A  74     4506   4426   4600   -596   -810    545       C  
ATOM    586  C   ILE A  74       7.945  26.713   4.500  1.00 29.08           C  
ANISOU  586  C   ILE A  74     3599   3461   3990   -660   -941    685       C  
ATOM    587  O   ILE A  74       8.621  25.805   4.022  1.00 41.83           O  
ANISOU  587  O   ILE A  74     5171   4991   5731   -589  -1019    680       O  
ATOM    588  N   GLY A  75       7.775  26.876   5.804  1.00 35.45           N  
ANISOU  588  N   GLY A  75     4415   4341   4714   -774   -921    808       N  
ATOM    589  CA  GLY A  75       8.400  26.002   6.769  1.00 41.51           C  
ANISOU  589  CA  GLY A  75     5138   5104   5531   -833  -1002    968       C  
ATOM    590  C   GLY A  75       7.990  24.556   6.559  1.00 52.34           C  
ANISOU  590  C   GLY A  75     6448   6320   7121   -811  -1095   1032       C  
ATOM    591  O   GLY A  75       8.801  23.637   6.694  1.00 41.26           O  
ANISOU  591  O   GLY A  75     5004   4840   5833   -781  -1186   1114       O  
ATOM    592  N   LEU A  76       6.723  24.357   6.217  1.00 37.46           N  
ANISOU  592  N   LEU A  76     4550   4377   5306   -825  -1079    997       N  
ATOM    593  CA  LEU A  76       6.221  23.022   5.937  1.00 39.88           C  
ANISOU  593  CA  LEU A  76     4804   4504   5845   -829  -1182   1040       C  
ATOM    594  C   LEU A  76       6.969  22.459   4.750  1.00 41.80           C  
ANISOU  594  C   LEU A  76     5061   4609   6212   -691  -1266    895       C  
ATOM    595  O   LEU A  76       7.465  21.323   4.781  1.00 38.34           O  
ANISOU  595  O   LEU A  76     4604   4017   5945   -658  -1369    953       O  
ATOM    596  CB  LEU A  76       4.729  23.047   5.639  1.00 40.80           C  
ANISOU  596  CB  LEU A  76     4884   4605   6014   -878  -1160   1007       C  
ATOM    597  CG  LEU A  76       4.232  21.672   5.195  1.00 40.01           C  
ANISOU  597  CG  LEU A  76     4734   4287   6182   -902  -1296   1022       C  
ATOM    598  CD1 LEU A  76       4.407  20.694   6.331  1.00 38.47           C  
ANISOU  598  CD1 LEU A  76     4500   4018   6098  -1004  -1347   1266       C  
ATOM    599  CD2 LEU A  76       2.783  21.766   4.752  1.00 35.76           C  
ANISOU  599  CD2 LEU A  76     4133   3751   5702   -955  -1294    972       C  
ATOM    600  N   THR A  77       7.073  23.289   3.719  1.00 31.00           N  
ANISOU  600  N   THR A  77     3732   3302   4746   -594  -1211    714       N  
ATOM    601  CA  THR A  77       7.653  22.868   2.463  1.00 37.39           C  
ANISOU  601  CA  THR A  77     4560   4020   5628   -439  -1264    554       C  
ATOM    602  CB  THR A  77       7.520  23.958   1.384  1.00 43.53           C  
ANISOU  602  CB  THR A  77     5380   4904   6254   -350  -1181    387       C  
ATOM    603  OG1 THR A  77       6.129  24.251   1.158  1.00 40.28           O  
ANISOU  603  OG1 THR A  77     4970   4500   5833   -400  -1175    341       O  
ATOM    604  CG2 THR A  77       8.152  23.489   0.078  1.00 30.69           C  
ANISOU  604  CG2 THR A  77     3778   3215   4668   -171  -1223    225       C  
ATOM    605  C   THR A  77       9.125  22.514   2.711  1.00 40.12           C  
ANISOU  605  C   THR A  77     4883   4366   5994   -368  -1284    618       C  
ATOM    606  O   THR A  77       9.616  21.499   2.217  1.00 37.93           O  
ANISOU  606  O   THR A  77     4600   3945   5865   -256  -1367    573       O  
ATOM    607  N   LYS A  78       9.809  23.329   3.510  1.00 38.99           N  
ANISOU  607  N   LYS A  78     4725   4382   5709   -433  -1218    721       N  
ATOM    608  CA  LYS A  78      11.234  23.085   3.799  1.00 45.94           C  
ANISOU  608  CA  LYS A  78     5550   5301   6603   -378  -1245    801       C  
ATOM    609  CB  LYS A  78      11.826  24.204   4.650  1.00 39.06           C  
ANISOU  609  CB  LYS A  78     4669   4623   5551   -488  -1186    888       C  
ATOM    610  CG  LYS A  78      11.990  25.525   3.933  1.00 39.36           C  
ANISOU  610  CG  LYS A  78     4741   4772   5442   -474  -1080    767       C  
ATOM    611  CD  LYS A  78      12.703  26.540   4.834  1.00 33.85           C  
ANISOU  611  CD  LYS A  78     4038   4227   4597   -602  -1055    848       C  
ATOM    612  CE  LYS A  78      12.917  27.872   4.117  1.00 54.11           C  
ANISOU  612  CE  LYS A  78     6643   6869   7047   -604   -955    747       C  
ATOM    613  NZ  LYS A  78      13.476  28.923   5.029  1.00 48.01           N  
ANISOU  613  NZ  LYS A  78     5891   6208   6142   -758   -949    802       N  
ATOM    614  C   LYS A  78      11.448  21.749   4.509  1.00 56.01           C  
ANISOU  614  C   LYS A  78     6787   6440   8056   -380  -1359    952       C  
ATOM    615  O   LYS A  78      12.325  20.974   4.127  1.00 50.48           O  
ANISOU  615  O   LYS A  78     6048   5657   7476   -242  -1415    946       O  
ATOM    616  N   SER A  79      10.645  21.498   5.543  1.00 36.67           N  
ANISOU  616  N   SER A  79     4345   3972   5617   -525  -1383   1098       N  
ATOM    617  CA  SER A  79      10.748  20.285   6.344  1.00 42.66           C  
ANISOU  617  CA  SER A  79     5072   4601   6537   -552  -1486   1290       C  
ATOM    618  CB  SER A  79       9.774  20.343   7.519  1.00 59.01           C  
ANISOU  618  CB  SER A  79     7147   6728   8546   -731  -1466   1466       C  
ATOM    619  OG  SER A  79       8.437  20.322   7.057  1.00 95.36           O  
ANISOU  619  OG  SER A  79    11769  11255  13208   -784  -1439   1383       O  
ATOM    620  C   SER A  79      10.474  19.045   5.506  1.00 41.20           C  
ANISOU  620  C   SER A  79     4903   4144   6606   -449  -1581   1209       C  
ATOM    621  O   SER A  79      11.085  17.981   5.704  1.00 39.59           O  
ANISOU  621  O   SER A  79     4679   3787   6575   -374  -1675   1308       O  
ATOM    622  N   VAL A  80       9.548  19.190   4.570  1.00 42.79           N  
ANISOU  622  N   VAL A  80     5147   4280   6831   -440  -1566   1025       N  
ATOM    623  CA  VAL A  80       9.178  18.107   3.679  1.00 43.28           C  
ANISOU  623  CA  VAL A  80     5247   4081   7117   -357  -1674    897       C  
ATOM    624  CB  VAL A  80       7.834  18.425   2.983  1.00 63.23           C  
ANISOU  624  CB  VAL A  80     7799   6591   9633   -425  -1669    747       C  
ATOM    625  CG1 VAL A  80       7.546  17.466   1.871  1.00 51.42           C  
ANISOU  625  CG1 VAL A  80     6359   4849   8327   -327  -1795    550       C  
ATOM    626  CG2 VAL A  80       6.716  18.354   3.997  1.00 39.76           C  
ANISOU  626  CG2 VAL A  80     4778   3629   6698   -636  -1665    940       C  
ATOM    627  C   VAL A  80      10.312  17.864   2.676  1.00 41.38           C  
ANISOU  627  C   VAL A  80     5027   3798   6898   -123  -1685    730       C  
ATOM    628  O   VAL A  80      10.796  16.731   2.519  1.00 39.96           O  
ANISOU  628  O   VAL A  80     4863   3406   6915     -8  -1782    730       O  
ATOM    629  N   LEU A  81      10.787  18.931   2.046  1.00 45.15           N  
ANISOU  629  N   LEU A  81     5499   4480   7174    -45  -1576    607       N  
ATOM    630  CA  LEU A  81      11.972  18.836   1.192  1.00 48.57           C  
ANISOU  630  CA  LEU A  81     5922   4942   7592    178  -1548    490       C  
ATOM    631  CB  LEU A  81      12.341  20.213   0.643  1.00 37.03           C  
ANISOU  631  CB  LEU A  81     4442   3736   5893    203  -1408    411       C  
ATOM    632  CG  LEU A  81      11.506  20.623  -0.568  1.00 45.38           C  
ANISOU  632  CG  LEU A  81     5577   4799   6867    255  -1379    192       C  
ATOM    633  CD1 LEU A  81      11.754  22.062  -0.953  1.00 39.91           C  
ANISOU  633  CD1 LEU A  81     4873   4345   5947    247  -1238    168       C  
ATOM    634  CD2 LEU A  81      11.797  19.702  -1.737  1.00 41.58           C  
ANISOU  634  CD2 LEU A  81     5147   4179   6472    481  -1435     -7       C  
ATOM    635  C   LEU A  81      13.164  18.208   1.925  1.00 51.61           C  
ANISOU  635  C   LEU A  81     6229   5306   8073    248  -1586    664       C  
ATOM    636  O   LEU A  81      13.914  17.415   1.344  1.00 50.90           O  
ANISOU  636  O   LEU A  81     6135   5104   8100    457  -1622    590       O  
ATOM    637  N   ALA A  82      13.320  18.530   3.207  1.00 45.51           N  
ANISOU  637  N   ALA A  82     5399   4646   7247     90  -1585    893       N  
ATOM    638  CA  ALA A  82      14.417  17.979   4.013  1.00 43.18           C  
ANISOU  638  CA  ALA A  82     5018   4362   7027    143  -1640   1090       C  
ATOM    639  CB  ALA A  82      14.469  18.660   5.355  1.00 42.18           C  
ANISOU  639  CB  ALA A  82     4844   4428   6754    -56  -1629   1304       C  
ATOM    640  C   ALA A  82      14.289  16.469   4.214  1.00 79.52           C  
ANISOU  640  C   ALA A  82     9651   8665  11897    215  -1770   1167       C  
ATOM    641  O   ALA A  82      15.289  15.737   4.336  1.00 49.15           O  
ANISOU  641  O   ALA A  82     5748   4753   8174    374  -1823   1252       O  
ATOM    642  N   GLU A  83      13.042  16.018   4.278  1.00 50.78           N  
ANISOU  642  N   GLU A  83     6092   4842   8360     91  -1824   1155       N  
ATOM    643  CA  GLU A  83      12.726  14.611   4.475  1.00 56.92           C  
ANISOU  643  CA  GLU A  83     6916   5294   9418    110  -1957   1237       C  
ATOM    644  CB  GLU A  83      11.255  14.468   4.897  1.00 47.86           C  
ANISOU  644  CB  GLU A  83     5808   4047   8331   -125  -1991   1307       C  
ATOM    645  CG  GLU A  83      11.023  14.897   6.343  1.00 57.66           C  
ANISOU  645  CG  GLU A  83     6988   5475   9447   -326  -1951   1601       C  
ATOM    646  CD  GLU A  83       9.587  14.759   6.796  1.00 87.01           C  
ANISOU  646  CD  GLU A  83    10714   9129  13217   -546  -1957   1700       C  
ATOM    647  OE1 GLU A  83       8.694  14.644   5.930  1.00119.29           O  
ANISOU  647  OE1 GLU A  83    14841  13089  17395   -571  -1981   1512       O  
ATOM    648  OE2 GLU A  83       9.353  14.768   8.024  1.00 96.11           O  
ANISOU  648  OE2 GLU A  83    11824  10382  14310   -692  -1938   1972       O  
ATOM    649  C   GLU A  83      13.027  13.829   3.197  1.00 45.85           C  
ANISOU  649  C   GLU A  83     5586   3661   8176    350  -2010    983       C  
ATOM    650  O   GLU A  83      13.292  12.620   3.219  1.00 50.86           O  
ANISOU  650  O   GLU A  83     6259   4009   9057    462  -2120   1022       O  
ATOM    651  N   SER A  84      13.012  14.554   2.083  1.00 52.54           N  
ANISOU  651  N   SER A  84     6459   4637   8868    442  -1927    724       N  
ATOM    652  CA  SER A  84      13.222  13.979   0.765  1.00 71.16           C  
ANISOU  652  CA  SER A  84     8901   6831  11304    679  -1957    442       C  
ATOM    653  CB  SER A  84      12.392  14.746  -0.272  1.00 54.41           C  
ANISOU  653  CB  SER A  84     6844   4814   9017    647  -1907    193       C  
ATOM    654  OG  SER A  84      12.232  14.009  -1.472  1.00105.74           O  
ANISOU  654  OG  SER A  84    13462  11107  15606    830  -1984    -91       O  
ATOM    655  C   SER A  84      14.700  13.982   0.360  1.00 77.56           C  
ANISOU  655  C   SER A  84     9644   7760  12066    953  -1882    407       C  
ATOM    656  O   SER A  84      15.056  13.423  -0.679  1.00 71.10           O  
ANISOU  656  O   SER A  84     8892   6821  11303   1201  -1892    182       O  
ATOM    657  N   GLY A  85      15.550  14.608   1.174  1.00 55.43           N  
ANISOU  657  N   GLY A  85     6703   5204   9154    912  -1811    624       N  
ATOM    658  CA  GLY A  85      16.962  14.751   0.846  1.00 49.46           C  
ANISOU  658  CA  GLY A  85     5830   4617   8344   1143  -1729    627       C  
ATOM    659  C   GLY A  85      17.160  15.739  -0.296  1.00 78.23           C  
ANISOU  659  C   GLY A  85     9464   8494  11766   1232  -1583    420       C  
ATOM    660  O   GLY A  85      18.025  15.541  -1.150  1.00 55.15           O  
ANISOU  660  O   GLY A  85     6503   5624   8829   1499  -1513    299       O  
ATOM    661  N   LYS A  86      16.356  16.802  -0.319  1.00 54.79           N  
ANISOU  661  N   LYS A  86     6528   5669   8620   1024  -1527    389       N  
ATOM    662  CA  LYS A  86      16.398  17.761  -1.420  1.00 57.65           C  
ANISOU  662  CA  LYS A  86     6900   6233   8773   1093  -1394    214       C  
ATOM    663  CB  LYS A  86      15.082  17.738  -2.201  1.00 62.23           C  
ANISOU  663  CB  LYS A  86     7635   6686   9322   1050  -1435     -2       C  
ATOM    664  CG  LYS A  86      14.673  16.376  -2.721  1.00 73.93           C  
ANISOU  664  CG  LYS A  86     9239   7849  11003   1191  -1570   -174       C  
ATOM    665  CD  LYS A  86      13.376  16.456  -3.516  1.00 75.09           C  
ANISOU  665  CD  LYS A  86     9518   7910  11102   1125  -1629   -389       C  
ATOM    666  CE  LYS A  86      13.576  17.194  -4.832  1.00 88.77           C  
ANISOU  666  CE  LYS A  86    11281   9853  12593   1292  -1512   -594       C  
ATOM    667  NZ  LYS A  86      12.358  17.153  -5.692  1.00 76.13           N  
ANISOU  667  NZ  LYS A  86     9810   8170  10944   1261  -1599   -819       N  
ATOM    668  C   LYS A  86      16.679  19.192  -0.961  1.00 74.93           C  
ANISOU  668  C   LYS A  86     8992   8715  10763    915  -1285    349       C  
ATOM    669  O   LYS A  86      16.986  20.062  -1.777  1.00102.68           O  
ANISOU  669  O   LYS A  86    12482  12420  14112    973  -1160    267       O  
ATOM    670  N   LEU A  87      16.565  19.439   0.338  1.00 46.23           N  
ANISOU  670  N   LEU A  87     5313   5111   7140    698  -1335    557       N  
ATOM    671  CA  LEU A  87      16.788  20.781   0.874  1.00 55.58           C  
ANISOU  671  CA  LEU A  87     6435   6539   8146    513  -1256    666       C  
ATOM    672  CB  LEU A  87      16.259  20.888   2.305  1.00 36.90           C  
ANISOU  672  CB  LEU A  87     4083   4157   5779    275  -1333    845       C  
ATOM    673  CG  LEU A  87      16.321  22.263   2.960  1.00 40.08           C  
ANISOU  673  CG  LEU A  87     4465   4773   5992     70  -1273    923       C  
ATOM    674  CD1 LEU A  87      15.349  23.172   2.271  1.00 35.50           C  
ANISOU  674  CD1 LEU A  87     3989   4211   5287     15  -1184    770       C  
ATOM    675  CD2 LEU A  87      16.016  22.192   4.452  1.00 50.46           C  
ANISOU  675  CD2 LEU A  87     5787   6097   7290   -119  -1355   1106       C  
ATOM    676  C   LEU A  87      18.263  21.116   0.861  1.00 59.47           C  
ANISOU  676  C   LEU A  87     6759   7232   8605    600  -1197    763       C  
ATOM    677  O   LEU A  87      18.996  20.633   1.711  1.00 55.22           O  
ANISOU  677  O   LEU A  87     6116   6709   8156    600  -1271    933       O  
ATOM    678  N   GLU A  88      18.725  21.930  -0.081  1.00 38.01           N  
ANISOU  678  N   GLU A  88     3997   4683   5763    671  -1067    681       N  
ATOM    679  CA  GLU A  88      20.157  22.216  -0.073  1.00 94.56           C  
ANISOU  679  CA  GLU A  88    10961  12051  12917    739  -1009    801       C  
ATOM    680  CB  GLU A  88      20.811  21.967  -1.434  1.00117.05           C  
ANISOU  680  CB  GLU A  88    13750  14970  15752   1024   -888    679       C  
ATOM    681  CG  GLU A  88      22.069  21.061  -1.369  1.00116.84           C  
ANISOU  681  CG  GLU A  88    13545  14985  15865   1251   -899    770       C  
ATOM    682  CD  GLU A  88      23.182  21.577  -0.456  1.00108.81           C  
ANISOU  682  CD  GLU A  88    12300  14182  14860   1121   -920   1014       C  
ATOM    683  OE1 GLU A  88      23.474  22.788  -0.479  1.00 80.48           O  
ANISOU  683  OE1 GLU A  88     8637  10794  11148    948   -844   1076       O  
ATOM    684  OE2 GLU A  88      23.775  20.762   0.284  1.00 77.11           O  
ANISOU  684  OE2 GLU A  88     8180  10130  10987   1189  -1024   1148       O  
ATOM    685  C   GLU A  88      20.305  23.650   0.367  1.00 64.80           C  
ANISOU  685  C   GLU A  88     7149   8469   9001    495   -959    893       C  
ATOM    686  O   GLU A  88      20.853  24.490  -0.348  1.00 88.55           O  
ANISOU  686  O   GLU A  88    10083  11644  11917    512   -837    883       O  
HETATM  703 ZN    ZN B   1     -14.407  28.509  -0.825  1.00 65.01          Zn  
ANISOU  703 ZN    ZN B   1     5711   9421   9569   -505  -1163    959      Zn  
HETATM  704 ZN    ZN B   2      14.994  34.110   2.879  1.00 80.40          Zn  
ANISOU  704 ZN    ZN B   2    10149  10407   9994   -955   -640    654      Zn  
HETATM  705 ZN    ZN B   3     -10.625  34.407 -10.349  1.00 83.50          Zn  
ANISOU  705 ZN    ZN B   3     9553  11819  10353   1101  -1599      9      Zn  
HETATM  706 ZN    ZN B   4      19.932  29.937  -5.397  1.00 91.96          Zn  
ANISOU  706 ZN    ZN B   4    10753  12568  11620    477   -110    702      Zn  
HETATM  707 ZN    ZN B   5       8.879  36.063   9.988  1.00109.90          Zn  
ANISOU  707 ZN    ZN B   5    14717  14132  12906  -1198   -536    341      Zn  
HETATM  708 ZN    ZN B   6       0.887  41.521  -9.893  1.00115.77          Zn  
ANISOU  708 ZN    ZN B   6    15446  14879  13663   1139    -95    509      Zn  
TER     709       ZN B   6                                                      
HETATM  710 ZN    ZN B   7      -0.067  13.779  -2.713  1.00132.29          Zn  
ANISOU  710 ZN    ZN B   7    16609  14025  19631   -945  -2873   -381      Zn  
TER     711       ZN B   7                                                      
HETATM  712  O   HOH S   1       0.452  34.631   5.480  1.00 34.36           O  
ANISOU  712  O   HOH S   1     4631   4557   3867   -369    -87    367       O  
HETATM  713  O   HOH S   2       1.544  39.084  -9.364  1.00 58.11           O  
ANISOU  713  O   HOH S   2     7972   7668   6440    952   -253    277       O  
HETATM  714  O   HOH S   3      14.417  33.061   5.110  1.00 45.20           O  
ANISOU  714  O   HOH S   3     5728   5965   5481  -1068   -800    688       O  
HETATM  715  O   HOH S   4      19.451  35.696  -0.924  1.00 54.85           O  
ANISOU  715  O   HOH S   4     6366   7554   6921   -907   -332   1029       O  
HETATM  716  O   HOH S   5       0.109  42.195 -11.935  1.00 47.72           O  
ANISOU  716  O   HOH S   5     6855   6447   4828   1449   -141    646       O  
HETATM  717  O   HOH S   6      18.197  25.307   6.438  1.00 47.81           O  
ANISOU  717  O   HOH S   6     5278   6361   6527   -550  -1349   1337       O  
HETATM  718  O   HOH S   7      21.368  21.634   3.515  1.00 53.87           O  
ANISOU  718  O   HOH S   7     5571   6990   7908    405  -1334   1354       O  
HETATM  719  O   HOH S   8       4.563  39.589   8.016  1.00 46.48           O  
ANISOU  719  O   HOH S   8     7042   5780   4837   -640    -12     -9       O  
HETATM  720  O   HOH S   9      15.495  38.086  -3.763  1.00 68.08           O  
ANISOU  720  O   HOH S   9     8669   8901   8296   -573    -11    825       O  
HETATM  721  O   HOH S  10     -15.387  26.465   0.155  1.00 59.95           O  
ANISOU  721  O   HOH S  10     4666   8744   9367   -976  -1301   1238       O  
HETATM  722  O   HOH S  11      -3.625  45.038  -0.941  1.00 62.83           O  
ANISOU  722  O   HOH S  11     9000   7538   7336   1173    486    211       O  
HETATM  723  O   HOH S  12       3.212  28.970  -8.979  1.00 53.74           O  
ANISOU  723  O   HOH S  12     7020   6911   6489    643  -1110   -610       O  
HETATM  724  O   HOH S  13      10.872  24.064   8.642  1.00 49.33           O  
ANISOU  724  O   HOH S  13     5997   6109   6637   -881  -1244   1361       O  
HETATM  725  O   HOH S  14     -16.146  29.809  -0.483  1.00 53.40           O  
ANISOU  725  O   HOH S  14     3885   8342   8061   -270   -942   1152       O  
HETATM  726  O   HOH S  15       7.657  30.490  -9.497  1.00 71.99           O  
ANISOU  726  O   HOH S  15     9403   9443   8508    819   -626   -369       O  
HETATM  727  O   HOH S  16      -2.498  41.722  -3.909  1.00 43.75           O  
ANISOU  727  O   HOH S  16     6175   5497   4950    941     68    291       O  
HETATM  728  O   HOH S  17      -1.782  15.042  -0.692  1.00 56.63           O  
ANISOU  728  O   HOH S  17     6648   4872   9997  -1329  -2611    198       O  
HETATM  729  O   HOH S  18      23.513  28.389   2.574  1.00 70.20           O  
ANISOU  729  O   HOH S  18     7349   9911   9411   -406   -965   1414       O  
TER     730      HOH S  18                                                      
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.