CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 16-APR-09 3H38  ***

elNémo ID: 20051012400131612

Job options:

ID        	=	 20051012400131612
JOBID     	=	 TRANSFERASE 16-APR-09 3H38
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             16-APR-09   3H38              
TITLE     THE STRUCTURE OF CCA-ADDING ENZYME APO FORM II                                         
ATOM      1  N   MET A   1      56.412 -11.277   8.703  1.00 77.25           N  
ANISOU    1  N   MET A   1     9754  10307   9289    571   -817     97       N  
ATOM      2  CA  MET A   1      55.071 -11.273   9.234  1.00 70.87           C  
ANISOU    2  CA  MET A   1     9074   9440   8414    640   -770    117       C  
ATOM      3  C   MET A   1      54.100 -11.793   8.226  1.00 54.79           C  
ANISOU    3  C   MET A   1     7076   7317   6425    641   -692    173       C  
ATOM      4  O   MET A   1      53.950 -11.230   7.180  1.00 50.57           O  
ANISOU    4  O   MET A   1     6483   6754   5977    578   -675    184       O  
ATOM      5  CB  MET A   1      54.690  -9.891   9.701  1.00 78.92           C  
ANISOU    5  CB  MET A   1    10158  10396   9432    597   -760     69       C  
ATOM      6  CG  MET A   1      53.554  -9.896  10.676  1.00 88.35           C  
ANISOU    6  CG  MET A   1    11301  11656  10612    558   -840     -4       C  
ATOM      7  SD  MET A   1      53.901  -9.299  12.316  1.00 79.60           S  
ANISOU    7  SD  MET A   1    10309  10477   9457    557   -825    -49       S  
ATOM      8  CE  MET A   1      53.117 -10.579  13.195  1.00 25.91           C  
ANISOU    8  CE  MET A   1     3636   3643   2566    685   -757     14       C  
ATOM      9  N   GLN A   2      53.482 -12.908   8.568  1.00 48.40           N  
ANISOU    9  N   GLN A   2     6369   6463   5559    715   -641    205       N  
ATOM     10  CA  GLN A   2      52.601 -13.645   7.676  1.00 47.25           C  
ANISOU   10  CA  GLN A   2     6261   6235   5457    716   -568    248       C  
ATOM     11  C   GLN A   2      51.249 -12.956   7.492  1.00 47.54           C  
ANISOU   11  C   GLN A   2     6318   6171   5574    636   -518    229       C  
ATOM     12  O   GLN A   2      50.577 -12.613   8.478  1.00 45.15           O  
ANISOU   12  O   GLN A   2     6076   5826   5253    624   -498    203       O  
ATOM     13  CB  GLN A   2      52.397 -15.076   8.173  1.00 42.29           C  
ANISOU   13  CB  GLN A   2     5737   5582   4750    814   -520    284       C  
ATOM     14  CG  GLN A   2      51.793 -15.987   7.111  1.00 41.98           C  
ANISOU   14  CG  GLN A   2     5722   5476   4754    820   -458    323       C  
ATOM     15  CD  GLN A   2      51.786 -17.445   7.525  1.00 45.22           C  
ANISOU   15  CD  GLN A   2     6235   5862   5086    919   -406    361       C  
ATOM     16  OE1 GLN A   2      52.424 -17.835   8.504  1.00 47.01           O  
ANISOU   16  OE1 GLN A   2     6509   6140   5213   1001   -422    367       O  
ATOM     17  NE2 GLN A   2      51.051 -18.252   6.789  1.00 39.15           N  
ANISOU   17  NE2 GLN A   2     5505   5013   4359    914   -342    383       N  
ATOM     18  N   ILE A   3      50.858 -12.785   6.256  1.00 41.44           N  
ANISOU   18  N   ILE A   3     5496   5366   4882    591   -498    242       N  
ATOM     19  CA  ILE A   3      49.602 -12.213   5.927  1.00 35.85           C  
ANISOU   19  CA  ILE A   3     4797   4574   4249    525   -453    225       C  
ATOM     20  C   ILE A   3      48.561 -13.245   5.602  1.00 41.35           C  
ANISOU   20  C   ILE A   3     5555   5196   4959    550   -385    244       C  
ATOM     21  O   ILE A   3      47.489 -13.223   6.123  1.00 37.38           O  
ANISOU   21  O   ILE A   3     5105   4624   4475    527   -334    228       O  
ATOM     22  CB  ILE A   3      49.787 -11.249   4.817  1.00 42.62           C  
ANISOU   22  CB  ILE A   3     5568   5438   5187    470   -467    223       C  
ATOM     23  CG1 ILE A   3      50.934 -10.340   5.184  1.00 40.56           C  
ANISOU   23  CG1 ILE A   3     5231   5252   4927    442   -527    210       C  
ATOM     24  CG2 ILE A   3      48.516 -10.520   4.542  1.00 37.67           C  
ANISOU   24  CG2 ILE A   3     4953   4735   4626    412   -424    201       C  
ATOM     25  CD1 ILE A   3      51.100  -9.282   4.273  1.00 50.31           C  
ANISOU   25  CD1 ILE A   3     6488   6525   6101    445   -566    175       C  
ATOM     26  N   PHE A   4      48.911 -14.178   4.756  1.00 40.04           N  
ANISOU   26  N   PHE A   4     5382   5043   4789    593   -381    276       N  
ATOM     27  CA  PHE A   4      47.956 -15.200   4.326  1.00 36.09           C  
ANISOU   27  CA  PHE A   4     4930   4468   4313    607   -319    285       C  
ATOM     28  C   PHE A   4      48.209 -16.559   4.984  1.00 41.08           C  
ANISOU   28  C   PHE A   4     5649   5088   4871    681   -284    312       C  
ATOM     29  O   PHE A   4      49.344 -17.026   5.090  1.00 34.49           O  
ANISOU   29  O   PHE A   4     4816   4321   3969    745   -319    340       O  
ATOM     30  CB  PHE A   4      47.941 -15.331   2.803  1.00 35.73           C  
ANISOU   30  CB  PHE A   4     4829   4425   4323    602   -329    294       C  
ATOM     31  CG  PHE A   4      47.972 -14.012   2.079  1.00 27.74           C  
ANISOU   31  CG  PHE A   4     3736   3437   3368    551   -362    279       C  
ATOM     32  CD1 PHE A   4      49.170 -13.480   1.632  1.00 32.02           C  
ANISOU   32  CD1 PHE A   4     4213   4053   3900    559   -412    297       C  
ATOM     33  CD2 PHE A   4      46.809 -13.296   1.869  1.00 25.05           C  
ANISOU   33  CD2 PHE A   4     3385   3044   3089    498   -335    247       C  
ATOM     34  CE1 PHE A   4      49.204 -12.261   0.972  1.00 38.02           C  
ANISOU   34  CE1 PHE A   4     4909   4823   4715    514   -426    287       C  
ATOM     35  CE2 PHE A   4      46.827 -12.076   1.208  1.00 25.44           C  
ANISOU   35  CE2 PHE A   4     3374   3109   3184    462   -355    237       C  
ATOM     36  CZ  PHE A   4      48.023 -11.559   0.749  1.00 28.42           C  
ANISOU   36  CZ  PHE A   4     3696   3549   3554    468   -396    258       C  
ATOM     37  N   ARG A   5      47.125 -17.183   5.422  1.00 43.78           N  
ANISOU   37  N   ARG A   5     6063   5343   5228    675   -210    306       N  
ATOM     38  CA  ARG A   5      47.187 -18.389   6.226  1.00 33.44           C  
ANISOU   38  CA  ARG A   5     4855   4000   3850    744   -154    332       C  
ATOM     39  C   ARG A   5      45.940 -19.236   5.922  1.00 28.26           C  
ANISOU   39  C   ARG A   5     4246   3236   3257    716    -65    323       C  
ATOM     40  O   ARG A   5      44.852 -18.703   5.731  1.00 31.33           O  
ANISOU   40  O   ARG A   5     4604   3575   3724    645    -40    289       O  
ATOM     41  CB  ARG A   5      47.240 -17.973   7.691  1.00 32.59           C  
ANISOU   41  CB  ARG A   5     4801   3901   3680    766   -148    327       C  
ATOM     42  CG  ARG A   5      47.248 -19.094   8.681  1.00 45.55           C  
ANISOU   42  CG  ARG A   5     6562   5504   5241    848    -80    356       C  
ATOM     43  CD  ARG A   5      47.234 -18.542  10.111  1.00 44.76           C  
ANISOU   43  CD  ARG A   5     6514   5415   5076    876    -79    346       C  
ATOM     44  NE  ARG A   5      48.137 -17.402  10.293  1.00 33.95           N  
ANISOU   44  NE  ARG A   5     5070   4149   3680    865   -183    321       N  
ATOM     45  CZ  ARG A   5      49.316 -17.458  10.911  1.00 43.95           C  
ANISOU   45  CZ  ARG A   5     6344   5508   4847    943   -244    326       C  
ATOM     46  NH1 ARG A   5      49.761 -18.599  11.434  1.00 43.70           N  
ANISOU   46  NH1 ARG A   5     6400   5484   4720   1053   -210    362       N  
ATOM     47  NH2 ARG A   5      50.049 -16.360  11.024  1.00 44.73           N  
ANISOU   47  NH2 ARG A   5     6363   5693   4941    914   -337    291       N  
ATOM     48  N   ASP A   6      46.094 -20.552   5.827  1.00 39.49           N  
ANISOU   48  N   ASP A   6     5739   4621   4646    771    -16    349       N  
ATOM     49  CA  ASP A   6      44.964 -21.403   5.458  1.00 33.66           C  
ANISOU   49  CA  ASP A   6     5038   3776   3977    735     68    332       C  
ATOM     50  C   ASP A   6      44.248 -21.780   6.744  1.00 32.42           C  
ANISOU   50  C   ASP A   6     4975   3539   3803    742    165    338       C  
ATOM     51  O   ASP A   6      44.809 -22.533   7.561  1.00 27.50           O  
ANISOU   51  O   ASP A   6     4449   2909   3090    824    204    377       O  
ATOM     52  CB  ASP A   6      45.491 -22.662   4.767  1.00 41.07           C  
ANISOU   52  CB  ASP A   6     6019   4700   4887    791     83    357       C  
ATOM     53  CG  ASP A   6      44.378 -23.566   4.237  1.00 49.81           C  
ANISOU   53  CG  ASP A   6     7156   5696   6075    744    163    327       C  
ATOM     54  OD1 ASP A   6      44.712 -24.612   3.646  1.00 50.26           O  
ANISOU   54  OD1 ASP A   6     7256   5728   6114    784    181    341       O  
ATOM     55  OD2 ASP A   6      43.182 -23.239   4.393  1.00 52.92           O  
ANISOU   55  OD2 ASP A   6     7527   6029   6551    668    207    286       O  
ATOM     56  N   VAL A   7      43.039 -21.254   6.946  1.00 27.62           N  
ANISOU   56  N   VAL A   7     4344   2875   3276    667    207    302       N  
ATOM     57  CA  VAL A   7      42.288 -21.579   8.169  1.00 27.96           C  
ANISOU   57  CA  VAL A   7     4477   2837   3309    673    311    311       C  
ATOM     58  C   VAL A   7      41.096 -22.483   7.888  1.00 38.38           C  
ANISOU   58  C   VAL A   7     5821   4041   4721    621    418    289       C  
ATOM     59  O   VAL A   7      40.127 -22.504   8.650  1.00 43.43           O  
ANISOU   59  O   VAL A   7     6497   4606   5398    591    509    283       O  
ATOM     60  CB  VAL A   7      41.822 -20.337   8.969  1.00 34.82           C  
ANISOU   60  CB  VAL A   7     5322   3723   4185    641    298    295       C  
ATOM     61  CG1 VAL A   7      43.017 -19.495   9.427  1.00 43.66           C  
ANISOU   61  CG1 VAL A   7     6429   4949   5212    691    200    309       C  
ATOM     62  CG2 VAL A   7      40.829 -19.511   8.188  1.00 21.67           C  
ANISOU   62  CG2 VAL A   7     3554   2048   2630    546    280    247       C  
ATOM     63  N   SER A   8      41.207 -23.247   6.803  1.00 34.85           N  
ANISOU   63  N   SER A   8     5355   3579   4309    611    409    277       N  
ATOM     64  CA  SER A   8      40.172 -24.169   6.351  1.00 33.48           C  
ANISOU   64  CA  SER A   8     5192   3299   4230    554    497    242       C  
ATOM     65  C   SER A   8      39.792 -25.219   7.356  1.00 27.39           C  
ANISOU   65  C   SER A   8     4546   2418   3443    579    638    270       C  
ATOM     66  O   SER A   8      38.613 -25.476   7.558  1.00 35.19           O  
ANISOU   66  O   SER A   8     5534   3314   4523    511    733    239       O  
ATOM     67  CB  SER A   8      40.597 -24.866   5.040  1.00 29.17           C  
ANISOU   67  CB  SER A   8     4620   2763   3699    560    451    226       C  
ATOM     68  OG  SER A   8      40.272 -24.019   3.967  1.00 47.07           O  
ANISOU   68  OG  SER A   8     6764   5087   6035    504    363    178       O  
ATOM     69  N   LYS A   9      40.775 -25.843   7.970  1.00 35.38           N  
ANISOU   69  N   LYS A   9     5665   3438   4340    682    658    329       N  
ATOM     70  CA  LYS A   9      40.541 -26.851   8.966  1.00 25.41           C  
ANISOU   70  CA  LYS A   9     4543   2068   3044    728    802    366       C  
ATOM     71  C   LYS A   9      39.819 -26.271  10.138  1.00 34.00           C  
ANISOU   71  C   LYS A   9     5653   3125   4140    715    866    373       C  
ATOM     72  O   LYS A   9      38.831 -26.810  10.560  1.00 44.77           O  
ANISOU   72  O   LYS A   9     7065   4373   5572    674   1000    367       O  
ATOM     73  CB  LYS A   9      41.838 -27.449   9.424  1.00 24.22           C  
ANISOU   73  CB  LYS A   9     4500   1958   2746    863    795    431       C  
ATOM     74  CG  LYS A   9      42.398 -28.468   8.532  1.00 33.94           C  
ANISOU   74  CG  LYS A   9     5765   3170   3962    895    795    440       C  
ATOM     75  CD  LYS A   9      43.743 -28.889   9.014  1.00 50.13           C  
ANISOU   75  CD  LYS A   9     7889   5304   5855   1037    752    503       C  
ATOM     76  CE  LYS A   9      44.783 -27.846   8.710  1.00 67.82           C  
ANISOU   76  CE  LYS A   9    10012   7705   8053   1051    587    497       C  
ATOM     77  NZ  LYS A   9      46.064 -28.367   8.176  1.00 68.84           N  
ANISOU   77  NZ  LYS A   9    10163   7923   8071   1160    522    540       N  
ATOM     78  N   LEU A  10      40.266 -25.125  10.605  1.00 34.11           N  
ANISOU   78  N   LEU A  10     5630   3240   4090    746    775    382       N  
ATOM     79  CA  LEU A  10      39.677 -24.448  11.720  1.00 30.82           C  
ANISOU   79  CA  LEU A  10     5241   2802   3669    744    825    389       C  
ATOM     80  C   LEU A  10      38.219 -24.116  11.467  1.00 33.28           C  
ANISOU   80  C   LEU A  10     5479   3043   4123    627    886    341       C  
ATOM     81  O   LEU A  10      37.429 -24.244  12.337  1.00 39.27           O  
ANISOU   81  O   LEU A  10     6295   3719   4905    622   1003    353       O  
ATOM     82  CB  LEU A  10      40.482 -23.200  11.996  1.00 34.38           C  
ANISOU   82  CB  LEU A  10     5647   3376   4039    781    699    391       C  
ATOM     83  CG  LEU A  10      40.578 -22.508  13.343  1.00 41.55           C  
ANISOU   83  CG  LEU A  10     6605   4268   4914    803    743    401       C  
ATOM     84  CD1 LEU A  10      40.192 -21.109  13.324  1.00 48.80           C  
ANISOU   84  CD1 LEU A  10     7682   5124   5734    914    855    456       C  
ATOM     85  CD2 LEU A  10      39.926 -23.240  14.451  1.00 28.32           C  
ANISOU   85  CD2 LEU A  10     4874   2712   3176    820    608    387       C  
ATOM     86  N   LEU A  11      37.865 -23.721  10.266  1.00 26.93           N  
ANISOU   86  N   LEU A  11     4547   2274   3411    542    809    286       N  
ATOM     87  CA  LEU A  11      36.478 -23.399   9.941  1.00 29.11           C  
ANISOU   87  CA  LEU A  11     4738   2500   3821    437    854    233       C  
ATOM     88  C   LEU A  11      35.603 -24.640  10.012  1.00 44.44           C  
ANISOU   88  C   LEU A  11     6729   4309   5846    395   1002    221       C  
ATOM     89  O   LEU A  11      34.510 -24.604  10.587  1.00 41.55           O  
ANISOU   89  O   LEU A  11     6363   3871   5553    348   1106    210       O  
ATOM     90  CB  LEU A  11      36.368 -22.798   8.537  1.00 41.14           C  
ANISOU   90  CB  LEU A  11     6121   4095   5415    372    737    175       C  
ATOM     91  CG  LEU A  11      36.750 -21.339   8.264  1.00 38.71           C  
ANISOU   91  CG  LEU A  11     5729   3901   5079    372    610    165       C  
ATOM     92  CD1 LEU A  11      37.000 -21.158   6.786  1.00 25.48           C  
ANISOU   92  CD1 LEU A  11     3953   2286   3443    344    507    126       C  
ATOM     93  CD2 LEU A  11      35.682 -20.342   8.744  1.00 35.76           C  
ANISOU   93  CD2 LEU A  11     5307   3519   4760    323    637    142       C  
ATOM     94  N   VAL A  12      36.069 -25.738   9.408  1.00 45.26           N  
ANISOU   94  N   VAL A  12     6875   4377   5945    411   1016    223       N  
ATOM     95  CA  VAL A  12      35.258 -26.950   9.380  1.00 44.91           C  
ANISOU   95  CA  VAL A  12     6877   4197   5989    360   1158    203       C  
ATOM     96  C   VAL A  12      35.110 -27.485  10.801  1.00 45.85           C  
ANISOU   96  C   VAL A  12     7140   4221   6059    419   1313    266       C  
ATOM     97  O   VAL A  12      34.053 -27.996  11.179  1.00 44.76           O  
ANISOU   97  O   VAL A  12     7022   3968   6016    359   1456    252       O  
ATOM     98  CB  VAL A  12      35.783 -28.038   8.375  1.00 51.17           C  
ANISOU   98  CB  VAL A  12     7693   4963   6786    364   1142    187       C  
ATOM     99  CG1 VAL A  12      36.551 -27.385   7.241  1.00 49.78           C  
ANISOU   99  CG1 VAL A  12     7420   4916   6580    375    967    164       C  
ATOM    100  CG2 VAL A  12      36.643 -29.059   9.074  1.00 53.08           C  
ANISOU  100  CG2 VAL A  12     8102   5150   6916    470   1223    260       C  
ATOM    101  N   GLU A  13      36.161 -27.331  11.597  1.00 49.41           N  
ANISOU  101  N   GLU A  13     7688   4724   6361    539   1286    334       N  
ATOM    102  CA  GLU A  13      36.080 -27.706  12.998  1.00 46.64           C  
ANISOU  102  CA  GLU A  13     7481   4298   5942    618   1422    397       C  
ATOM    103  C   GLU A  13      35.044 -26.848  13.741  1.00 52.99           C  
ANISOU  103  C   GLU A  13     8247   5084   6802    573   1473    388       C  
ATOM    104  O   GLU A  13      34.100 -27.372  14.320  1.00 57.63           O  
ANISOU  104  O   GLU A  13     8886   5552   7459    543   1634    397       O  
ATOM    105  CB  GLU A  13      37.442 -27.622  13.686  1.00 37.18           C  
ANISOU  105  CB  GLU A  13     6383   3181   4563    767   1361    462       C  
ATOM    106  CG  GLU A  13      37.414 -28.340  15.025  1.00 49.87           C  
ANISOU  106  CG  GLU A  13     8166   4695   6089    871   1520    530       C  
ATOM    107  CD  GLU A  13      38.336 -27.744  16.093  1.00 61.59           C  
ANISOU  107  CD  GLU A  13     9725   6273   7405   1011   1459    579       C  
ATOM    108  OE1 GLU A  13      39.484 -27.360  15.767  1.00 72.56           O  
ANISOU  108  OE1 GLU A  13    11079   7788   8702   1067   1311    579       O  
ATOM    109  OE2 GLU A  13      37.906 -27.686  17.271  1.00 55.99           O  
ANISOU  109  OE2 GLU A  13     9110   5507   6656   1068   1565    616       O  
ATOM    110  N   ARG A  14      35.183 -25.541  13.730  1.00 45.91           N  
ANISOU  110  N   ARG A  14     7260   4302   5882    566   1342    370       N  
ATOM    111  CA  ARG A  14      34.355 -24.702  14.556  1.00 50.93           C  
ANISOU  111  CA  ARG A  14     7886   4933   6533    556   1381    375       C  
ATOM    112  C   ARG A  14      33.003 -24.271  14.045  1.00 46.81           C  
ANISOU  112  C   ARG A  14     7238   4375   6172    427   1419    315       C  
ATOM    113  O   ARG A  14      32.155 -23.967  14.816  1.00 49.05           O  
ANISOU  113  O   ARG A  14     7540   4607   6490    417   1518    328       O  
ATOM    114  CB  ARG A  14      35.156 -23.491  14.941  1.00 54.26           C  
ANISOU  114  CB  ARG A  14     8286   5485   6845    615   1234    384       C  
ATOM    115  CG  ARG A  14      36.525 -23.828  15.384  1.00 59.29           C  
ANISOU  115  CG  ARG A  14     9029   6178   7320    746   1182    434       C  
ATOM    116  CD  ARG A  14      36.879 -22.979  16.528  1.00 83.98           C  
ANISOU  116  CD  ARG A  14    12294   9272  10341    855   1267    488       C  
ATOM    117  NE  ARG A  14      37.707 -23.674  17.491  1.00 99.14           N  
ANISOU  117  NE  ARG A  14    14321  11247  12101    993   1226    531       N  
ATOM    118  CZ  ARG A  14      38.857 -23.209  17.938  1.00105.44           C  
ANISOU  118  CZ  ARG A  14    15104  12169  12790   1057   1086    527       C  
ATOM    119  NH1 ARG A  14      39.311 -22.047  17.510  1.00109.51           N  
ANISOU  119  NH1 ARG A  14    15514  12757  13339    993    980    485       N  
ATOM    120  NH2 ARG A  14      39.555 -23.900  18.810  1.00103.83           N  
ANISOU  120  NH2 ARG A  14    14990  12017  12443   1188   1055    562       N  
ATOM    121  N   VAL A  15      32.796 -24.231  12.757  1.00 45.17           N  
ANISOU  121  N   VAL A  15     6905   4200   6059    339   1342    250       N  
ATOM    122  CA  VAL A  15      31.561 -23.656  12.214  1.00 50.85           C  
ANISOU  122  CA  VAL A  15     7485   4921   6914    231   1342    185       C  
ATOM    123  C   VAL A  15      30.506 -24.718  11.866  1.00 55.49           C  
ANISOU  123  C   VAL A  15     8044   5394   7646    139   1472    141       C  
ATOM    124  O   VAL A  15      30.827 -25.786  11.327  1.00 48.68           O  
ANISOU  124  O   VAL A  15     7214   4480   6801    128   1496    129       O  
ATOM    125  CB  VAL A  15      31.860 -22.721  10.992  1.00 47.56           C  
ANISOU  125  CB  VAL A  15     6932   4628   6510    197   1164    132       C  
ATOM    126  CG1 VAL A  15      30.664 -21.790  10.670  1.00 40.33           C  
ANISOU  126  CG1 VAL A  15     5884   3742   5697    119   1150     76       C  
ATOM    127  CG2 VAL A  15      33.127 -21.892  11.260  1.00 39.94           C  
ANISOU  127  CG2 VAL A  15     6005   3765   5404    283   1041    175       C  
ATOM    128  N   ASP A  16      29.248 -24.427  12.196  1.00 58.97           N  
ANISOU  128  N   ASP A  16     8423   5793   8191     74   1560    115       N  
ATOM    129  CA  ASP A  16      28.145 -25.306  11.818  1.00 58.95           C  
ANISOU  129  CA  ASP A  16     8363   5691   8345    -31   1677     57       C  
ATOM    130  C   ASP A  16      28.231 -25.582  10.321  1.00 45.85           C  
ANISOU  130  C   ASP A  16     6593   4077   6751    -96   1564    -26       C  
ATOM    131  O   ASP A  16      28.425 -24.670   9.527  1.00 47.91           O  
ANISOU  131  O   ASP A  16     6752   4455   6996    -98   1412    -62       O  
ATOM    132  CB  ASP A  16      26.795 -24.666  12.161  1.00 70.59           C  
ANISOU  132  CB  ASP A  16     9740   7156   9925    -96   1745     27       C  
ATOM    133  CG  ASP A  16      25.616 -25.618  11.945  1.00 80.94           C  
ANISOU  133  CG  ASP A  16    10991   8356  11408   -208   1888    -33       C  
ATOM    134  OD1 ASP A  16      25.724 -26.806  12.324  1.00 85.29           O  
ANISOU  134  OD1 ASP A  16    11649   8783  11974   -210   2023     -6       O  
ATOM    135  OD2 ASP A  16      24.571 -25.176  11.411  1.00 80.92           O  
ANISOU  135  OD2 ASP A  16    10832   8389  11525   -294   1869   -108       O  
ATOM    136  N   PRO A  17      28.108 -26.847   9.937  1.00 48.19           N  
ANISOU  136  N   PRO A  17     6918   4275   7116   -143   1644    -56       N  
ATOM    137  CA  PRO A  17      28.204 -27.260   8.539  1.00 53.08           C  
ANISOU  137  CA  PRO A  17     7451   4925   7792   -197   1546   -137       C  
ATOM    138  C   PRO A  17      27.102 -26.664   7.654  1.00 56.60           C  
ANISOU  138  C   PRO A  17     7707   5431   8368   -294   1481   -242       C  
ATOM    139  O   PRO A  17      27.387 -26.294   6.519  1.00 57.70           O  
ANISOU  139  O   PRO A  17     7759   5665   8500   -295   1332   -294       O  
ATOM    140  CB  PRO A  17      28.050 -28.780   8.627  1.00 53.48           C  
ANISOU  140  CB  PRO A  17     7590   4825   7905   -237   1693   -146       C  
ATOM    141  CG  PRO A  17      27.285 -28.982   9.927  1.00 51.47           C  
ANISOU  141  CG  PRO A  17     7402   4462   7693   -249   1884    -99       C  
ATOM    142  CD  PRO A  17      27.941 -28.008  10.826  1.00 52.73           C  
ANISOU  142  CD  PRO A  17     7629   4698   7708   -137   1838    -10       C  
ATOM    143  N   LYS A  18      25.905 -26.523   8.159  1.00 61.61           N  
ANISOU  143  N   LYS A  18     8278   6015   9116   -365   1591   -271       N  
ATOM    144  CA  LYS A  18      24.862 -25.998   7.325  1.00 71.28           C  
ANISOU  144  CA  LYS A  18     9316   7309  10459   -445   1529   -373       C  
ATOM    145  C   LYS A  18      25.276 -24.637   6.813  1.00 70.67           C  
ANISOU  145  C   LYS A  18     9172   7388  10291   -382   1349   -368       C  
ATOM    146  O   LYS A  18      25.050 -24.285   5.679  1.00 63.14           O  
ANISOU  146  O   LYS A  18     8096   6521   9374   -405   1225   -448       O  
ATOM    147  CB  LYS A  18      23.575 -25.932   8.111  1.00 78.10           C  
ANISOU  147  CB  LYS A  18    10130   8117  11428   -505   1674   -379       C  
ATOM    148  CG  LYS A  18      22.689 -24.816   7.705  1.00 87.01           C  
ANISOU  148  CG  LYS A  18    11071   9347  12640   -553   1601   -460       C  
ATOM    149  CD  LYS A  18      21.431 -25.309   7.057  1.00 96.98           C  
ANISOU  149  CD  LYS A  18    12186  10625  14036   -648   1551   -594       C  
ATOM    150  CE  LYS A  18      20.957 -24.321   6.041  1.00 98.67           C  
ANISOU  150  CE  LYS A  18    12222  10979  14291   -658   1430   -671       C  
ATOM    151  NZ  LYS A  18      19.486 -24.070   6.123  1.00 97.21           N  
ANISOU  151  NZ  LYS A  18    11960  10792  14184   -692   1532   -672       N  
ATOM    152  N   ILE A  19      25.909 -23.904   7.703  1.00 64.93           N  
ANISOU  152  N   ILE A  19     8538   6690   9442   -297   1343   -274       N  
ATOM    153  CA  ILE A  19      26.405 -22.556   7.505  1.00 53.57           C  
ANISOU  153  CA  ILE A  19     7067   5378   7910   -234   1204   -251       C  
ATOM    154  C   ILE A  19      27.733 -22.496   6.723  1.00 55.17           C  
ANISOU  154  C   ILE A  19     7304   5649   8010   -174   1064   -234       C  
ATOM    155  O   ILE A  19      27.945 -21.594   5.905  1.00 50.75           O  
ANISOU  155  O   ILE A  19     6665   5195   7423   -154    932   -260       O  
ATOM    156  CB  ILE A  19      26.559 -21.907   8.885  1.00 51.66           C  
ANISOU  156  CB  ILE A  19     6921   5122   7584   -173   1267   -162       C  
ATOM    157  CG1 ILE A  19      25.208 -21.351   9.339  1.00 47.53           C  
ANISOU  157  CG1 ILE A  19     6315   4591   7152   -220   1346   -187       C  
ATOM    158  CG2 ILE A  19      27.633 -20.842   8.895  1.00 55.05           C  
ANISOU  158  CG2 ILE A  19     7387   5652   7877    -90   1135   -114       C  
ATOM    159  CD1 ILE A  19      25.282 -20.573  10.627  1.00 54.73           C  
ANISOU  159  CD1 ILE A  19     7315   5500   7979   -154   1397   -106       C  
ATOM    160  N   LEU A  20      28.616 -23.458   6.969  1.00 52.62           N  
ANISOU  160  N   LEU A  20     7101   5264   7627   -138   1101   -188       N  
ATOM    161  CA  LEU A  20      29.833 -23.592   6.183  1.00 44.15           C  
ANISOU  161  CA  LEU A  20     6057   4248   6470    -84    984   -175       C  
ATOM    162  C   LEU A  20      29.493 -23.735   4.717  1.00 49.42           C  
ANISOU  162  C   LEU A  20     6605   4958   7213   -133    894   -267       C  
ATOM    163  O   LEU A  20      30.136 -23.119   3.861  1.00 44.52           O  
ANISOU  163  O   LEU A  20     5942   4434   6539    -92    761   -273       O  
ATOM    164  CB  LEU A  20      30.652 -24.812   6.619  1.00 39.21           C  
ANISOU  164  CB  LEU A  20     5575   3538   5786    -43   1058   -121       C  
ATOM    165  CG  LEU A  20      32.057 -24.518   7.135  1.00 42.14           C  
ANISOU  165  CG  LEU A  20     6051   3961   6000     64   1001    -34       C  
ATOM    166  CD1 LEU A  20      33.034 -25.603   6.758  1.00 42.11           C  
ANISOU  166  CD1 LEU A  20     6133   3928   5939    110    996    -11       C  
ATOM    167  CD2 LEU A  20      32.521 -23.190   6.584  1.00 45.12           C  
ANISOU  167  CD2 LEU A  20     6344   4470   6328     90    848    -39       C  
ATOM    168  N   ASN A  21      28.495 -24.569   4.432  1.00 45.62           N  
ANISOU  168  N   ASN A  21     6073   4402   6858   -217    972   -341       N  
ATOM    169  CA  ASN A  21      28.101 -24.823   3.054  1.00 52.00           C  
ANISOU  169  CA  ASN A  21     6769   5246   7742   -262    889   -443       C  
ATOM    170  C   ASN A  21      27.572 -23.585   2.359  1.00 54.74           C  
ANISOU  170  C   ASN A  21     6976   5713   8108   -260    777   -494       C  
ATOM    171  O   ASN A  21      27.726 -23.430   1.147  1.00 53.15           O  
ANISOU  171  O   ASN A  21     6705   5584   7906   -244    661   -550       O  
ATOM    172  CB  ASN A  21      27.095 -25.962   2.977  1.00 55.36           C  
ANISOU  172  CB  ASN A  21     7164   5563   8309   -362   1000   -523       C  
ATOM    173  CG  ASN A  21      27.773 -27.312   2.797  1.00 68.69           C  
ANISOU  173  CG  ASN A  21     8964   7156   9980   -359   1046   -513       C  
ATOM    174  OD1 ASN A  21      28.941 -27.393   2.376  1.00 62.46           O  
ANISOU  174  OD1 ASN A  21     8243   6406   9082   -281    963   -468       O  
ATOM    175  ND2 ASN A  21      27.047 -28.382   3.115  1.00 76.24           N  
ANISOU  175  ND2 ASN A  21     9940   7983  11045   -441   1186   -553       N  
ATOM    176  N   LEU A  22      26.957 -22.716   3.156  1.00 52.01           N  
ANISOU  176  N   LEU A  22     6603   5386   7773   -265    819   -471       N  
ATOM    177  CA  LEU A  22      26.475 -21.410   2.731  1.00 54.21           C  
ANISOU  177  CA  LEU A  22     6772   5775   8051   -248    731   -499       C  
ATOM    178  C   LEU A  22      27.628 -20.483   2.329  1.00 48.68           C  
ANISOU  178  C   LEU A  22     6104   5167   7225   -160    606   -445       C  
ATOM    179  O   LEU A  22      27.608 -19.908   1.244  1.00 45.69           O  
ANISOU  179  O   LEU A  22     5643   4876   6842   -136    497   -491       O  
ATOM    180  CB  LEU A  22      25.702 -20.777   3.888  1.00 47.03           C  
ANISOU  180  CB  LEU A  22     5859   4846   7164   -263    825   -466       C  
ATOM    181  CG  LEU A  22      25.085 -19.409   3.635  1.00 33.95           C  
ANISOU  181  CG  LEU A  22     4102   3291   5507   -242    760   -489       C  
ATOM    182  CD1 LEU A  22      24.219 -19.428   2.404  1.00 39.24           C  
ANISOU  182  CD1 LEU A  22     4620   4022   6267   -276    693   -603       C  
ATOM    183  CD2 LEU A  22      24.249 -18.976   4.837  1.00 41.25           C  
ANISOU  183  CD2 LEU A  22     5032   4180   6461   -260    873   -456       C  
ATOM    184  N   PHE A  23      28.608 -20.327   3.229  1.00 35.41           N  
ANISOU  184  N   PHE A  23     4544   3468   5444   -110    627   -349       N  
ATOM    185  CA  PHE A  23      29.829 -19.589   2.936  1.00 36.31           C  
ANISOU  185  CA  PHE A  23     4695   3658   5445    -36    522   -295       C  
ATOM    186  C   PHE A  23      30.376 -20.076   1.596  1.00 39.97           C  
ANISOU  186  C   PHE A  23     5127   4156   5903    -18    431   -334       C  
ATOM    187  O   PHE A  23      30.790 -19.277   0.757  1.00 39.08           O  
ANISOU  187  O   PHE A  23     4969   4129   5750     25    326   -338       O  
ATOM    188  CB  PHE A  23      30.889 -19.772   4.039  1.00 41.44           C  
ANISOU  188  CB  PHE A  23     5480   4271   5994     11    561   -202       C  
ATOM    189  CG  PHE A  23      30.607 -18.999   5.329  1.00 49.59           C  
ANISOU  189  CG  PHE A  23     6555   5292   6995     21    621   -155       C  
ATOM    190  CD1 PHE A  23      30.127 -17.702   5.303  1.00 48.69           C  
ANISOU  190  CD1 PHE A  23     6376   5240   6883     24    579   -166       C  
ATOM    191  CD2 PHE A  23      30.872 -19.568   6.566  1.00 59.62           C  
ANISOU  191  CD2 PHE A  23     7941   6487   8223     41    718    -96       C  
ATOM    192  CE1 PHE A  23      29.886 -16.998   6.471  1.00 53.88           C  
ANISOU  192  CE1 PHE A  23     7080   5884   7507     38    632   -124       C  
ATOM    193  CE2 PHE A  23      30.628 -18.868   7.750  1.00 61.05           C  
ANISOU  193  CE2 PHE A  23     8170   6658   8368     62    771    -54       C  
ATOM    194  CZ  PHE A  23      30.135 -17.584   7.700  1.00 60.89           C  
ANISOU  194  CZ  PHE A  23     8082   6699   8355     57    726    -69       C  
ATOM    195  N   ARG A  24      30.351 -21.393   1.395  1.00 34.25           N  
ANISOU  195  N   ARG A  24     4435   3359   5221    -49    478   -361       N  
ATOM    196  CA  ARG A  24      30.790 -21.989   0.128  1.00 32.18           C  
ANISOU  196  CA  ARG A  24     4151   3118   4958    -32    400   -403       C  
ATOM    197  C   ARG A  24      29.957 -21.499  -1.065  1.00 36.76           C  
ANISOU  197  C   ARG A  24     4595   3769   5602    -46    318   -499       C  
ATOM    198  O   ARG A  24      30.503 -20.961  -2.039  1.00 43.95           O  
ANISOU  198  O   ARG A  24     5476   4761   6462     13    211   -501       O  
ATOM    199  CB  ARG A  24      30.837 -23.517   0.216  1.00 24.78           C  
ANISOU  199  CB  ARG A  24     3284   2076   4057    -66    479   -419       C  
ATOM    200  CG  ARG A  24      31.989 -24.037   1.078  1.00 30.19           C  
ANISOU  200  CG  ARG A  24     4113   2713   4643    -13    529   -319       C  
ATOM    201  CD  ARG A  24      32.159 -25.579   1.030  1.00 44.16           C  
ANISOU  201  CD  ARG A  24     5968   4377   6434    -30    606   -329       C  
ATOM    202  NE  ARG A  24      33.516 -25.977   1.426  1.00 44.63           N  
ANISOU  202  NE  ARG A  24     6154   4432   6373     53    606   -238       N  
ATOM    203  CZ  ARG A  24      33.803 -26.581   2.574  1.00 53.26           C  
ANISOU  203  CZ  ARG A  24     7367   5447   7424     75    716   -173       C  
ATOM    204  NH1 ARG A  24      32.816 -26.890   3.411  1.00 62.14           N  
ANISOU  204  NH1 ARG A  24     8506   6480   8624     13    843   -187       N  
ATOM    205  NH2 ARG A  24      35.065 -26.897   2.881  1.00 47.61           N  
ANISOU  205  NH2 ARG A  24     6756   4745   6589    163    704    -94       N  
ATOM    206  N   LEU A  25      28.656 -21.599  -0.954  1.00 34.69           N  
ANISOU  206  N   LEU A  25     4250   3482   5449   -116    370   -576       N  
ATOM    207  CA  LEU A  25      27.780 -21.116  -1.986  1.00 44.28           C  
ANISOU  207  CA  LEU A  25     5329   4776   6718   -119    289   -672       C  
ATOM    208  C   LEU A  25      28.029 -19.699  -2.333  1.00 37.03           C  
ANISOU  208  C   LEU A  25     4380   3964   5724    -44    203   -635       C  
ATOM    209  O   LEU A  25      28.052 -19.363  -3.461  1.00 40.78           O  
ANISOU  209  O   LEU A  25     4803   4516   6175      8    103   -672       O  
ATOM    210  CB  LEU A  25      26.359 -21.187  -1.514  1.00 55.83           C  
ANISOU  210  CB  LEU A  25     6696   6212   8306   -201    363   -751       C  
ATOM    211  CG  LEU A  25      25.672 -22.511  -1.566  1.00 65.72           C  
ANISOU  211  CG  LEU A  25     7960   7353   9659   -290    458   -806       C  
ATOM    212  CD1 LEU A  25      24.267 -22.242  -2.006  1.00 69.83           C  
ANISOU  212  CD1 LEU A  25     8348   7871  10314   -372    509   -904       C  
ATOM    213  CD2 LEU A  25      26.397 -23.362  -2.538  1.00 64.14           C  
ANISOU  213  CD2 LEU A  25     7772   7146   9451   -277    385   -860       C  
ATOM    214  N   LEU A  26      28.189 -18.867  -1.323  1.00 45.53           N  
ANISOU  214  N   LEU A  26     5498   5040   6762    -36    248   -562       N  
ATOM    215  CA  LEU A  26      28.418 -17.448  -1.517  1.00 40.74           C  
ANISOU  215  CA  LEU A  26     4869   4520   6089     26    182   -528       C  
ATOM    216  C   LEU A  26      29.710 -17.242  -2.300  1.00 43.14           C  
ANISOU  216  C   LEU A  26     5218   4871   6304     97     91   -486       C  
ATOM    217  O   LEU A  26      29.766 -16.401  -3.212  1.00 49.92           O  
ANISOU  217  O   LEU A  26     6026   5808   7133    153     12   -501       O  
ATOM    218  CB  LEU A  26      28.450 -16.704  -0.185  1.00 42.08           C  
ANISOU  218  CB  LEU A  26     5097   4669   6224     22    247   -455       C  
ATOM    219  CG  LEU A  26      27.134 -16.643   0.603  1.00 46.37           C  
ANISOU  219  CG  LEU A  26     5592   5178   6848    -34    339   -486       C  
ATOM    220  CD1 LEU A  26      27.362 -16.185   2.034  1.00 37.28           C  
ANISOU  220  CD1 LEU A  26     4531   3985   5649    -31    414   -403       C  
ATOM    221  CD2 LEU A  26      26.115 -15.746  -0.071  1.00 44.17           C  
ANISOU  221  CD2 LEU A  26     5193   4982   6608    -19    294   -551       C  
ATOM    222  N   GLY A  27      30.735 -18.019  -1.956  1.00 31.80           N  
ANISOU  222  N   GLY A  27     3875   3384   4822    101    110   -431       N  
ATOM    223  CA  GLY A  27      32.008 -17.937  -2.648  1.00 40.57           C  
ANISOU  223  CA  GLY A  27     5027   4536   5851    167     34   -386       C  
ATOM    224  C   GLY A  27      31.761 -18.233  -4.111  1.00 41.08           C  
ANISOU  224  C   GLY A  27     5024   4643   5942    195    -40   -459       C  
ATOM    225  O   GLY A  27      32.194 -17.496  -5.000  1.00 34.85           O  
ANISOU  225  O   GLY A  27     4209   3925   5106    262   -118   -451       O  
ATOM    226  N   LYS A  28      31.037 -19.310  -4.331  1.00 46.20           N  
ANISOU  226  N   LYS A  28     5644   5241   6667    145    -11   -535       N  
ATOM    227  CA  LYS A  28      30.690 -19.785  -5.646  1.00 47.61           C  
ANISOU  227  CA  LYS A  28     5762   5451   6878    165    -80   -622       C  
ATOM    228  C   LYS A  28      29.917 -18.772  -6.455  1.00 48.10           C  
ANISOU  228  C   LYS A  28     5721   5607   6949    208   -148   -676       C  
ATOM    229  O   LYS A  28      30.244 -18.590  -7.599  1.00 47.93           O  
ANISOU  229  O   LYS A  28     5681   5649   6882    286   -234   -690       O  
ATOM    230  CB  LYS A  28      29.932 -21.099  -5.549  1.00 53.60           C  
ANISOU  230  CB  LYS A  28     6500   6130   7735     83    -24   -708       C  
ATOM    231  CG  LYS A  28      30.436 -22.205  -6.426  1.00 62.70           C  
ANISOU  231  CG  LYS A  28     7678   7260   8886    101    -68   -754       C  
ATOM    232  CD  LYS A  28      30.017 -22.061  -7.867  1.00 72.25           C  
ANISOU  232  CD  LYS A  28     8805   8562  10085    169   -184   -829       C  
ATOM    233  CE  LYS A  28      31.215 -22.162  -8.833  1.00 73.58           C  
ANISOU  233  CE  LYS A  28     9026   8718  10212    219   -239   -843       C  
ATOM    234  NZ  LYS A  28      30.881 -22.237 -10.287  1.00 63.04           N  
ANISOU  234  NZ  LYS A  28     7626   7474   8853    305   -355   -912       N  
ATOM    235  N   PHE A  29      28.934 -18.097  -5.854  1.00 34.00           N  
ANISOU  235  N   PHE A  29     3874   3830   5214    168   -107   -702       N  
ATOM    236  CA  PHE A  29      28.240 -16.986  -6.515  1.00 32.55           C  
ANISOU  236  CA  PHE A  29     3600   3740   5028    221   -164   -745       C  
ATOM    237  C   PHE A  29      29.224 -15.889  -6.869  1.00 31.00           C  
ANISOU  237  C   PHE A  29     3450   3600   4729    311   -216   -664       C  
ATOM    238  O   PHE A  29      29.063 -15.215  -7.882  1.00 45.12           O  
ANISOU  238  O   PHE A  29     5190   5465   6488    389   -284   -693       O  
ATOM    239  CB  PHE A  29      27.148 -16.368  -5.640  1.00 44.58           C  
ANISOU  239  CB  PHE A  29     5069   5266   6604    174   -101   -760       C  
ATOM    240  CG  PHE A  29      26.080 -17.326  -5.222  1.00 54.59           C  
ANISOU  240  CG  PHE A  29     6279   6478   7986     79    -35   -839       C  
ATOM    241  CD1 PHE A  29      25.268 -17.039  -4.136  1.00 53.12           C  
ANISOU  241  CD1 PHE A  29     6070   6262   7850     22     53   -829       C  
ATOM    242  CD2 PHE A  29      25.891 -18.525  -5.902  1.00 55.83           C  
ANISOU  242  CD2 PHE A  29     6406   6606   8201     44    -55   -923       C  
ATOM    243  CE1 PHE A  29      24.280 -17.928  -3.740  1.00 55.25           C  
ANISOU  243  CE1 PHE A  29     6282   6475   8234    -71    128   -900       C  
ATOM    244  CE2 PHE A  29      24.906 -19.414  -5.510  1.00 54.23           C  
ANISOU  244  CE2 PHE A  29     6148   6343   8115    -55     16  -1001       C  
ATOM    245  CZ  PHE A  29      24.103 -19.118  -4.427  1.00 56.49           C  
ANISOU  245  CZ  PHE A  29     6406   6600   8458   -114    111   -988       C  
ATOM    246  N   GLY A  30      30.235 -15.697  -6.023  1.00 27.43           N  
ANISOU  246  N   GLY A  30     3091   3110   4223    303   -179   -563       N  
ATOM    247  CA  GLY A  30      31.223 -14.654  -6.245  1.00 28.80           C  
ANISOU  247  CA  GLY A  30     3306   3327   4311    372   -216   -485       C  
ATOM    248  C   GLY A  30      31.880 -14.866  -7.596  1.00 40.12           C  
ANISOU  248  C   GLY A  30     4738   4803   5703    450   -293   -495       C  
ATOM    249  O   GLY A  30      31.899 -13.967  -8.429  1.00 43.93           O  
ANISOU  249  O   GLY A  30     5193   5349   6149    526   -340   -495       O  
ATOM    250  N   ASP A  31      32.403 -16.069  -7.811  1.00 38.36           N  
ANISOU  250  N   ASP A  31     4551   4541   5483    437   -298   -500       N  
ATOM    251  CA  ASP A  31      33.039 -16.438  -9.068  1.00 39.48           C  
ANISOU  251  CA  ASP A  31     4701   4715   5585    513   -366   -509       C  
ATOM    252  C   ASP A  31      32.098 -16.294 -10.261  1.00 42.29           C  
ANISOU  252  C   ASP A  31     4973   5131   5965    566   -429   -607       C  
ATOM    253  O   ASP A  31      32.509 -15.865 -11.336  1.00 47.09           O  
ANISOU  253  O   ASP A  31     5578   5794   6519    663   -488   -600       O  
ATOM    254  CB  ASP A  31      33.522 -17.883  -9.013  1.00 42.88           C  
ANISOU  254  CB  ASP A  31     5185   5083   6025    482   -352   -513       C  
ATOM    255  CG  ASP A  31      34.791 -18.038  -8.212  1.00 56.15           C  
ANISOU  255  CG  ASP A  31     6956   6731   7649    477   -316   -408       C  
ATOM    256  OD1 ASP A  31      35.252 -17.012  -7.661  1.00 60.82           O  
ANISOU  256  OD1 ASP A  31     7560   7346   8203    485   -306   -341       O  
ATOM    257  OD2 ASP A  31      35.326 -19.174  -8.141  1.00 52.44           O  
ANISOU  257  OD2 ASP A  31     6543   6212   7170    468   -300   -397       O  
ATOM    258  N   GLU A  32      30.842 -16.663 -10.068  1.00 32.16           N  
ANISOU  258  N   GLU A  32     3620   3837   4761    507   -413   -699       N  
ATOM    259  CA  GLU A  32      29.894 -16.709 -11.169  1.00 46.70           C  
ANISOU  259  CA  GLU A  32     5372   5740   6632    553   -479   -811       C  
ATOM    260  C   GLU A  32      29.474 -15.317 -11.604  1.00 56.62           C  
ANISOU  260  C   GLU A  32     6580   7082   7850    636   -510   -810       C  
ATOM    261  O   GLU A  32      28.896 -15.149 -12.673  1.00 63.33           O  
ANISOU  261  O   GLU A  32     7368   8003   8693    713   -577   -888       O  
ATOM    262  CB  GLU A  32      28.675 -17.547 -10.796  1.00 46.62           C  
ANISOU  262  CB  GLU A  32     5289   5694   6729    455   -448   -918       C  
ATOM    263  CG  GLU A  32      28.941 -19.048 -10.852  1.00 41.39           C  
ANISOU  263  CG  GLU A  32     4666   4954   6105    397   -435   -954       C  
ATOM    264  CD  GLU A  32      27.853 -19.855 -10.166  1.00 48.67           C  
ANISOU  264  CD  GLU A  32     5534   5814   7146    276   -369  -1036       C  
ATOM    265  OE1 GLU A  32      27.936 -21.099 -10.194  1.00 56.42           O  
ANISOU  265  OE1 GLU A  32     6546   6721   8170    220   -347  -1076       O  
ATOM    266  OE2 GLU A  32      26.921 -19.251  -9.589  1.00 41.35           O  
ANISOU  266  OE2 GLU A  32     4536   4907   6268    237   -333  -1059       O  
ATOM    267  N   VAL A  33      29.771 -14.325 -10.770  1.00 53.73           N  
ANISOU  267  N   VAL A  33     6250   6709   7455    626   -461   -723       N  
ATOM    268  CA  VAL A  33      29.518 -12.931 -11.109  1.00 46.83           C  
ANISOU  268  CA  VAL A  33     5354   5903   6535    708   -476   -703       C  
ATOM    269  C   VAL A  33      30.805 -12.123 -10.991  1.00 43.28           C  
ANISOU  269  C   VAL A  33     4992   5444   6009    749   -460   -585       C  
ATOM    270  O   VAL A  33      30.784 -10.900 -10.949  1.00 31.78           O  
ANISOU  270  O   VAL A  33     3544   4015   4515    795   -446   -544       O  
ATOM    271  CB  VAL A  33      28.438 -12.326 -10.210  1.00 55.07           C  
ANISOU  271  CB  VAL A  33     6348   6950   7625    656   -424   -725       C  
ATOM    272  CG1 VAL A  33      27.110 -13.006 -10.473  1.00 48.86           C  
ANISOU  272  CG1 VAL A  33     5455   6190   6921    624   -443   -851       C  
ATOM    273  CG2 VAL A  33      28.833 -12.462  -8.730  1.00 59.15           C  
ANISOU  273  CG2 VAL A  33     6927   7385   8162    553   -343   -652       C  
ATOM    274  N   ASN A  34      31.932 -12.823 -10.930  1.00 45.99           N  
ANISOU  274  N   ASN A  34     5400   5745   6331    731   -460   -531       N  
ATOM    275  CA  ASN A  34      33.233 -12.161 -10.930  1.00 52.85           C  
ANISOU  275  CA  ASN A  34     6338   6610   7133    769   -451   -427       C  
ATOM    276  C   ASN A  34      33.470 -11.135  -9.820  1.00 45.97           C  
ANISOU  276  C   ASN A  34     5499   5716   6251    724   -395   -358       C  
ATOM    277  O   ASN A  34      34.055 -10.082 -10.060  1.00 48.70           O  
ANISOU  277  O   ASN A  34     5871   6081   6550    774   -390   -301       O  
ATOM    278  CB  ASN A  34      33.501 -11.525 -12.296  1.00 60.36           C  
ANISOU  278  CB  ASN A  34     7285   7622   8027    897   -499   -422       C  
ATOM    279  CG  ASN A  34      33.610 -12.555 -13.395  1.00 68.16           C  
ANISOU  279  CG  ASN A  34     8264   8628   9007    953   -558   -473       C  
ATOM    280  OD1 ASN A  34      34.531 -13.380 -13.400  1.00 72.74           O  
ANISOU  280  OD1 ASN A  34     8890   9174   9574    938   -561   -436       O  
ATOM    281  ND2 ASN A  34      32.661 -12.527 -14.330  1.00 68.25           N  
ANISOU  281  ND2 ASN A  34     8215   8694   9021   1024   -609   -562       N  
ATOM    282  N   MET A  35      33.033 -11.458  -8.607  1.00 43.61           N  
ANISOU  282  N   MET A  35     5203   5372   5995    630   -348   -365       N  
ATOM    283  CA  MET A  35      33.336 -10.649  -7.422  1.00 35.30           C  
ANISOU  283  CA  MET A  35     4194   4290   4929    582   -296   -303       C  
ATOM    284  C   MET A  35      34.084 -11.504  -6.409  1.00 33.62           C  
ANISOU  284  C   MET A  35     4036   4020   4717    512   -266   -262       C  
ATOM    285  O   MET A  35      33.654 -12.613  -6.098  1.00 33.03           O  
ANISOU  285  O   MET A  35     3955   3910   4684    466   -249   -300       O  
ATOM    286  CB  MET A  35      32.052 -10.150  -6.780  1.00 21.94           C  
ANISOU  286  CB  MET A  35     2462   2597   3276    550   -259   -344       C  
ATOM    287  CG  MET A  35      31.284  -9.096  -7.606  1.00 12.30           C  
ANISOU  287  CG  MET A  35     1193   1438   2041    630   -280   -377       C  
ATOM    288  SD  MET A  35      29.756  -8.715  -6.760  1.00 35.66           S  
ANISOU  288  SD  MET A  35     4100   4399   5051    588   -231   -427       S  
ATOM    289  CE  MET A  35      28.629  -8.357  -8.122  1.00 45.18           C  
ANISOU  289  CE  MET A  35     5211   5696   6259    690   -284   -514       C  
ATOM    290  N   PRO A  36      35.229 -11.015  -5.914  1.00 34.52           N  
ANISOU  290  N   PRO A  36     4206   4126   4784    509   -259   -186       N  
ATOM    291  CA  PRO A  36      35.853 -11.682  -4.755  1.00 34.82           C  
ANISOU  291  CA  PRO A  36     4299   4118   4814    451   -227   -148       C  
ATOM    292  C   PRO A  36      34.977 -11.551  -3.510  1.00 27.19           C  
ANISOU  292  C   PRO A  36     3342   3112   3878    390   -169   -163       C  
ATOM    293  O   PRO A  36      34.550 -10.444  -3.210  1.00 36.86           O  
ANISOU  293  O   PRO A  36     4558   4347   5099    390   -155   -160       O  
ATOM    294  CB  PRO A  36      37.166 -10.918  -4.573  1.00 33.30           C  
ANISOU  294  CB  PRO A  36     4144   3941   4566    466   -240    -77       C  
ATOM    295  CG  PRO A  36      37.456 -10.349  -5.982  1.00 28.96           C  
ANISOU  295  CG  PRO A  36     3564   3440   4001    540   -280    -73       C  
ATOM    296  CD  PRO A  36      36.097  -9.986  -6.512  1.00 23.97           C  
ANISOU  296  CD  PRO A  36     2882   2823   3401    563   -280   -136       C  
ATOM    297  N   VAL A  37      34.699 -12.662  -2.828  1.00 29.62           N  
ANISOU  297  N   VAL A  37     3671   3371   4214    344   -131   -177       N  
ATOM    298  CA  VAL A  37      33.843 -12.659  -1.641  1.00 32.88           C  
ANISOU  298  CA  VAL A  37     4097   3739   4658    291    -64   -187       C  
ATOM    299  C   VAL A  37      34.613 -12.960  -0.343  1.00 33.74           C  
ANISOU  299  C   VAL A  37     4290   3807   4724    268    -25   -130       C  
ATOM    300  O   VAL A  37      35.469 -13.840  -0.321  1.00 34.10           O  
ANISOU  300  O   VAL A  37     4377   3838   4742    277    -32   -104       O  
ATOM    301  CB  VAL A  37      32.706 -13.680  -1.766  1.00 29.25           C  
ANISOU  301  CB  VAL A  37     3594   3246   4274    254    -28   -254       C  
ATOM    302  CG1 VAL A  37      31.658 -13.404  -0.716  1.00 29.46           C  
ANISOU  302  CG1 VAL A  37     3614   3238   4340    209     45   -267       C  
ATOM    303  CG2 VAL A  37      32.078 -13.603  -3.124  1.00 37.64           C  
ANISOU  303  CG2 VAL A  37     4573   4359   5371    287    -81   -321       C  
ATOM    304  N   TYR A  38      34.286 -12.236   0.731  1.00 30.34           N  
ANISOU  304  N   TYR A  38     3888   3358   4283    247     16   -113       N  
ATOM    305  CA  TYR A  38      34.914 -12.428   2.040  1.00 25.75           C  
ANISOU  305  CA  TYR A  38     3389   2742   3654    237     51    -65       C  
ATOM    306  C   TYR A  38      33.948 -12.319   3.232  1.00 30.92           C  
ANISOU  306  C   TYR A  38     4071   3347   4329    207    130    -69       C  
ATOM    307  O   TYR A  38      33.011 -11.509   3.244  1.00 27.35           O  
ANISOU  307  O   TYR A  38     3580   2903   3907    197    146    -93       O  
ATOM    308  CB  TYR A  38      35.983 -11.366   2.286  1.00 29.41           C  
ANISOU  308  CB  TYR A  38     3880   3243   4051    257      5    -24       C  
ATOM    309  CG  TYR A  38      36.894 -11.050   1.137  1.00 31.62           C  
ANISOU  309  CG  TYR A  38     4127   3576   4312    288    -65    -13       C  
ATOM    310  CD1 TYR A  38      36.498 -10.193   0.140  1.00 24.52           C  
ANISOU  310  CD1 TYR A  38     3171   2710   3435    306    -92    -34       C  
ATOM    311  CD2 TYR A  38      38.180 -11.583   1.079  1.00 35.97           C  
ANISOU  311  CD2 TYR A  38     4705   4145   4817    309    -99     23       C  
ATOM    312  CE1 TYR A  38      37.347  -9.881  -0.909  1.00 39.26           C  
ANISOU  312  CE1 TYR A  38     5014   4620   5283    342   -144    -18       C  
ATOM    313  CE2 TYR A  38      39.028 -11.288   0.031  1.00 32.60           C  
ANISOU  313  CE2 TYR A  38     4245   3766   4377    340   -154     38       C  
ATOM    314  CZ  TYR A  38      38.611 -10.435  -0.959  1.00 31.59           C  
ANISOU  314  CZ  TYR A  38     4066   3663   4274    356   -173     19       C  
ATOM    315  OH  TYR A  38      39.465 -10.123  -1.990  1.00 29.00           O  
ANISOU  315  OH  TYR A  38     3712   3375   3930    394   -216     41       O  
ATOM    316  N   VAL A  39      34.223 -13.102   4.267  1.00 29.29           N  
ANISOU  316  N   VAL A  39     3939   3092   4097    203    181    -40       N  
ATOM    317  CA  VAL A  39      33.613 -12.860   5.560  1.00 30.50           C  
ANISOU  317  CA  VAL A  39     4143   3202   4245    191    255    -26       C  
ATOM    318  C   VAL A  39      34.643 -12.053   6.367  1.00 31.56           C  
ANISOU  318  C   VAL A  39     4344   3360   4289    220    219     16       C  
ATOM    319  O   VAL A  39      35.855 -12.274   6.237  1.00 33.32           O  
ANISOU  319  O   VAL A  39     4591   3611   4458    245    166     41       O  
ATOM    320  CB  VAL A  39      33.188 -14.177   6.248  1.00 26.21           C  
ANISOU  320  CB  VAL A  39     3648   2582   3728    177    348    -21       C  
ATOM    321  CG1 VAL A  39      34.400 -14.967   6.697  1.00 35.11           C  
ANISOU  321  CG1 VAL A  39     4861   3698   4781    214    342     24       C  
ATOM    322  CG2 VAL A  39      32.241 -13.894   7.409  1.00 29.55           C  
ANISOU  322  CG2 VAL A  39     4105   2957   4165    165    439    -13       C  
ATOM    323  N   VAL A  40      34.177 -11.072   7.140  1.00 25.25           N  
ANISOU  323  N   VAL A  40     3566   2553   3474    218    242     20       N  
ATOM    324  CA  VAL A  40      35.097 -10.125   7.775  1.00 25.96           C  
ANISOU  324  CA  VAL A  40     3707   2670   3487    239    195     44       C  
ATOM    325  C   VAL A  40      34.780  -9.856   9.247  1.00 38.54           C  
ANISOU  325  C   VAL A  40     5384   4223   5037    253    252     62       C  
ATOM    326  O   VAL A  40      33.698 -10.186   9.735  1.00 30.32           O  
ANISOU  326  O   VAL A  40     4354   3133   4033    246    336     59       O  
ATOM    327  CB  VAL A  40      35.058  -8.771   7.051  1.00 26.98           C  
ANISOU  327  CB  VAL A  40     3784   2842   3627    230    143     27       C  
ATOM    328  CG1 VAL A  40      35.458  -8.939   5.602  1.00 24.83           C  
ANISOU  328  CG1 VAL A  40     3439   2611   3384    231     86     14       C  
ATOM    329  CG2 VAL A  40      33.664  -8.169   7.137  1.00 35.93           C  
ANISOU  329  CG2 VAL A  40     4891   3954   4805    218    197      5       C  
ATOM    330  N   GLY A  41      35.739  -9.255   9.947  1.00 44.90           N  
ANISOU  330  N   GLY A  41     6245   5050   5764    275    206     77       N  
ATOM    331  CA  GLY A  41      35.465  -8.630  11.229  1.00 40.83           C  
ANISOU  331  CA  GLY A  41     5806   4507   5199    294    241     86       C  
ATOM    332  C   GLY A  41      35.361  -9.520  12.444  1.00 35.93           C  
ANISOU  332  C   GLY A  41     5277   3840   4534    335    311    112       C  
ATOM    333  O   GLY A  41      36.220 -10.372  12.662  1.00 39.42           O  
ANISOU  333  O   GLY A  41     5756   4291   4930    367    296    130       O  
ATOM    334  N   GLY A  42      34.315  -9.297  13.243  1.00 42.18           N  
ANISOU  334  N   GLY A  42     6110   4583   5335    343    393    119       N  
ATOM    335  CA  GLY A  42      34.142  -9.955  14.536  1.00 38.76           C  
ANISOU  335  CA  GLY A  42     5780   4097   4851    394    473    150       C  
ATOM    336  C   GLY A  42      34.016 -11.445  14.367  1.00 39.37           C  
ANISOU  336  C   GLY A  42     5862   4133   4962    398    540    168       C  
ATOM    337  O   GLY A  42      34.621 -12.234  15.089  1.00 34.34           O  
ANISOU  337  O   GLY A  42     5310   3479   4259    453    564    197       O  
ATOM    338  N   PHE A  43      33.248 -11.843  13.369  1.00 45.82           N  
ANISOU  338  N   PHE A  43     6590   4937   5881    343    568    147       N  
ATOM    339  CA  PHE A  43      33.139 -13.256  13.074  1.00 43.03           C  
ANISOU  339  CA  PHE A  43     6237   4540   5571    335    628    155       C  
ATOM    340  C   PHE A  43      34.502 -13.944  12.917  1.00 44.58           C  
ANISOU  340  C   PHE A  43     6472   4767   5699    374    567    173       C  
ATOM    341  O   PHE A  43      34.683 -15.095  13.310  1.00 44.84           O  
ANISOU  341  O   PHE A  43     6572   4754   5713    406    632    199       O  
ATOM    342  CB  PHE A  43      32.320 -13.509  11.814  1.00 36.95           C  
ANISOU  342  CB  PHE A  43     5351   3771   4918    268    633    113       C  
ATOM    343  CG  PHE A  43      32.363 -14.939  11.388  1.00 37.70           C  
ANISOU  343  CG  PHE A  43     5446   3823   5056    254    678    111       C  
ATOM    344  CD1 PHE A  43      31.416 -15.841  11.858  1.00 39.27           C  
ANISOU  344  CD1 PHE A  43     5668   3935   5316    234    809    115       C  
ATOM    345  CD2 PHE A  43      33.391 -15.402  10.571  1.00 39.00           C  
ANISOU  345  CD2 PHE A  43     5595   4027   5195    263    599    109       C  
ATOM    346  CE1 PHE A  43      31.461 -17.194  11.488  1.00 41.77           C  
ANISOU  346  CE1 PHE A  43     5997   4199   5676    217    861    111       C  
ATOM    347  CE2 PHE A  43      33.462 -16.746  10.200  1.00 44.85           C  
ANISOU  347  CE2 PHE A  43     6351   4722   5968    256    644    108       C  
ATOM    348  CZ  PHE A  43      32.491 -17.651  10.663  1.00 45.57           C  
ANISOU  348  CZ  PHE A  43     6470   4720   6125    231    776    107       C  
ATOM    349  N   VAL A  44      35.451 -13.261  12.301  1.00 35.23           N  
ANISOU  349  N   VAL A  44     5244   3660   4481    372    450    159       N  
ATOM    350  CA  VAL A  44      36.755 -13.869  12.093  1.00 32.14           C  
ANISOU  350  CA  VAL A  44     4875   3310   4028    411    389    176       C  
ATOM    351  C   VAL A  44      37.592 -13.855  13.389  1.00 30.48           C  
ANISOU  351  C   VAL A  44     4771   3112   3698    488    381    205       C  
ATOM    352  O   VAL A  44      38.271 -14.835  13.723  1.00 32.46           O  
ANISOU  352  O   VAL A  44     5084   3358   3890    545    396    232       O  
ATOM    353  CB  VAL A  44      37.499 -13.163  10.940  1.00 24.99           C  
ANISOU  353  CB  VAL A  44     3878   2482   3134    382    273    153       C  
ATOM    354  CG1 VAL A  44      38.950 -13.638  10.860  1.00 20.42           C  
ANISOU  354  CG1 VAL A  44     3321   1958   2481    429    205    173       C  
ATOM    355  CG2 VAL A  44      36.773 -13.419   9.631  1.00 20.78           C  
ANISOU  355  CG2 VAL A  44     3254   1940   2702    330    279    126       C  
ATOM    356  N   ARG A  45      37.561 -12.722  14.089  1.00 28.58           N  
ANISOU  356  N   ARG A  45     4551   2890   3418    494    352    195       N  
ATOM    357  CA  ARG A  45      38.105 -12.606  15.431  1.00 30.94           C  
ANISOU  357  CA  ARG A  45     4953   3195   3606    571    351    211       C  
ATOM    358  C   ARG A  45      37.586 -13.755  16.307  1.00 31.69           C  
ANISOU  358  C   ARG A  45     5152   3213   3677    630    476    251       C  
ATOM    359  O   ARG A  45      38.364 -14.525  16.894  1.00 29.64           O  
ANISOU  359  O   ARG A  45     4971   2961   3329    710    481    278       O  
ATOM    360  CB  ARG A  45      37.644 -11.277  16.023  1.00 29.21           C  
ANISOU  360  CB  ARG A  45     4746   2976   3375    557    337    190       C  
ATOM    361  CG  ARG A  45      38.220 -10.911  17.399  1.00 21.39           C  
ANISOU  361  CG  ARG A  45     3860   2002   2265    635    315    193       C  
ATOM    362  CD  ARG A  45      37.364  -9.767  17.988  1.00 32.57           C  
ANISOU  362  CD  ARG A  45     5302   3387   3687    620    341    178       C  
ATOM    363  NE  ARG A  45      35.963 -10.180  18.132  1.00 34.45           N  
ANISOU  363  NE  ARG A  45     5555   3543   3991    610    471    204       N  
ATOM    364  CZ  ARG A  45      34.911  -9.387  17.921  1.00 38.12           C  
ANISOU  364  CZ  ARG A  45     5980   3981   4521    562    507    193       C  
ATOM    365  NH1 ARG A  45      35.078  -8.105  17.559  1.00 33.44           N  
ANISOU  365  NH1 ARG A  45     5343   3429   3933    523    426    158       N  
ATOM    366  NH2 ARG A  45      33.686  -9.881  18.061  1.00 31.86           N  
ANISOU  366  NH2 ARG A  45     5192   3121   3793    554    628    215       N  
ATOM    367  N   ASP A  46      36.259 -13.868  16.357  1.00 26.17           N  
ANISOU  367  N   ASP A  46     4447   2438   3058    592    582    255       N  
ATOM    368  CA  ASP A  46      35.583 -14.851  17.185  1.00 33.71           C  
ANISOU  368  CA  ASP A  46     5496   3303   4010    636    723    294       C  
ATOM    369  C   ASP A  46      35.980 -16.278  16.810  1.00 38.48           C  
ANISOU  369  C   ASP A  46     6125   3877   4619    655    766    316       C  
ATOM    370  O   ASP A  46      36.301 -17.083  17.685  1.00 42.49           O  
ANISOU  370  O   ASP A  46     6748   4348   5048    742    834    357       O  
ATOM    371  CB  ASP A  46      34.071 -14.616  17.153  1.00 30.36           C  
ANISOU  371  CB  ASP A  46     5033   2813   3691    576    823    286       C  
ATOM    372  CG  ASP A  46      33.676 -13.267  17.816  1.00 45.99           C  
ANISOU  372  CG  ASP A  46     7026   4810   5639    584    802    277       C  
ATOM    373  OD1 ASP A  46      34.464 -12.750  18.641  1.00 42.23           O  
ANISOU  373  OD1 ASP A  46     6625   4369   5050    652    745    283       O  
ATOM    374  OD2 ASP A  46      32.590 -12.712  17.521  1.00 47.05           O  
ANISOU  374  OD2 ASP A  46     7096   4924   5857    528    841    260       O  
ATOM    375  N   LEU A  47      36.019 -16.578  15.515  1.00 29.11           N  
ANISOU  375  N   LEU A  47     4839   2709   3513    587    725    291       N  
ATOM    376  CA  LEU A  47      36.470 -17.895  15.058  1.00 33.98           C  
ANISOU  376  CA  LEU A  47     5480   3300   4131    604    755    308       C  
ATOM    377  C   LEU A  47      37.830 -18.239  15.656  1.00 37.11           C  
ANISOU  377  C   LEU A  47     5964   3747   4390    710    704    340       C  
ATOM    378  O   LEU A  47      38.017 -19.322  16.229  1.00 42.31           O  
ANISOU  378  O   LEU A  47     6728   4353   4996    781    790    380       O  
ATOM    379  CB  LEU A  47      36.515 -17.993  13.515  1.00 31.94           C  
ANISOU  379  CB  LEU A  47     5100   3075   3961    527    686    270       C  
ATOM    380  CG  LEU A  47      37.073 -19.309  12.939  1.00 33.20           C  
ANISOU  380  CG  LEU A  47     5285   3213   4116    547    703    284       C  
ATOM    381  CD1 LEU A  47      36.124 -20.455  13.208  1.00 25.40           C  
ANISOU  381  CD1 LEU A  47     4353   2105   3193    530    857    295       C  
ATOM    382  CD2 LEU A  47      37.332 -19.204  11.449  1.00 30.44           C  
ANISOU  382  CD2 LEU A  47     4821   2918   3828    490    608    247       C  
ATOM    383  N   LEU A  48      38.779 -17.318  15.528  1.00 33.06           N  
ANISOU  383  N   LEU A  48     5408   3336   3818    722    569    321       N  
ATOM    384  CA  LEU A  48      40.152 -17.586  15.962  1.00 34.57           C  
ANISOU  384  CA  LEU A  48     5654   3598   3884    817    501    341       C  
ATOM    385  C   LEU A  48      40.248 -17.690  17.501  1.00 45.20           C  
ANISOU  385  C   LEU A  48     7135   4924   5114    926    555    370       C  
ATOM    386  O   LEU A  48      41.046 -18.468  18.022  1.00 48.08           O  
ANISOU  386  O   LEU A  48     7586   5307   5377   1030    564    401       O  
ATOM    387  CB  LEU A  48      41.103 -16.521  15.414  1.00 37.02           C  
ANISOU  387  CB  LEU A  48     5870   4021   4176    790    347    305       C  
ATOM    388  CG  LEU A  48      41.271 -16.485  13.876  1.00 42.14           C  
ANISOU  388  CG  LEU A  48     6397   4702   4913    711    286    285       C  
ATOM    389  CD1 LEU A  48      42.054 -15.285  13.428  1.00 28.71           C  
ANISOU  389  CD1 LEU A  48     4608   3096   3206    677    157    253       C  
ATOM    390  CD2 LEU A  48      41.956 -17.765  13.344  1.00 37.75           C  
ANISOU  390  CD2 LEU A  48     5862   4151   4332    756    295    313       C  
ATOM    391  N   LEU A  49      39.432 -16.915  18.218  1.00 42.75           N  
ANISOU  391  N   LEU A  49     6849   4579   4816    913    594    362       N  
ATOM    392  CA  LEU A  49      39.348 -17.028  19.689  1.00 42.96           C  
ANISOU  392  CA  LEU A  49     7013   4572   4736   1022    662    392       C  
ATOM    393  C   LEU A  49      38.541 -18.241  20.121  1.00 46.83           C  
ANISOU  393  C   LEU A  49     7602   4943   5247   1059    838    443       C  
ATOM    394  O   LEU A  49      38.513 -18.581  21.297  1.00 45.58           O  
ANISOU  394  O   LEU A  49     7576   4748   4996   1168    917    480       O  
ATOM    395  CB  LEU A  49      38.740 -15.766  20.330  1.00 26.70           C  
ANISOU  395  CB  LEU A  49     4955   2513   2678   1001    649    368       C  
ATOM    396  CG  LEU A  49      39.684 -14.560  20.292  1.00 37.04           C  
ANISOU  396  CG  LEU A  49     6208   3933   3934    993    486    319       C  
ATOM    397  CD1 LEU A  49      38.973 -13.273  20.663  1.00 32.02           C  
ANISOU  397  CD1 LEU A  49     5560   3284   3322    949    476    291       C  
ATOM    398  CD2 LEU A  49      40.937 -14.806  21.169  1.00 29.69           C  
ANISOU  398  CD2 LEU A  49     5359   3074   2848   1120    419    321       C  
ATOM    399  N   GLY A  50      37.898 -18.899  19.161  1.00 49.87           N  
ANISOU  399  N   GLY A  50     7926   5268   5756    971    902    441       N  
ATOM    400  CA  GLY A  50      37.031 -20.018  19.460  1.00 33.10           C  
ANISOU  400  CA  GLY A  50     5879   3018   3679    980   1078    480       C  
ATOM    401  C   GLY A  50      35.796 -19.559  20.211  1.00 47.23           C  
ANISOU  401  C   GLY A  50     7696   4733   5516    960   1186    489       C  
ATOM    402  O   GLY A  50      35.365 -20.206  21.172  1.00 56.84           O  
ANISOU  402  O   GLY A  50     9036   5861   6699   1033   1331    537       O  
ATOM    403  N   ILE A  51      35.228 -18.439  19.775  1.00 48.51           N  
ANISOU  403  N   ILE A  51     7748   4930   5752    871   1123    446       N  
ATOM    404  CA  ILE A  51      34.038 -17.866  20.392  1.00 51.99           C  
ANISOU  404  CA  ILE A  51     8198   5313   6241    849   1214    451       C  
ATOM    405  C   ILE A  51      32.862 -17.917  19.431  1.00 52.72           C  
ANISOU  405  C   ILE A  51     8167   5363   6503    719   1266    419       C  
ATOM    406  O   ILE A  51      32.897 -17.312  18.373  1.00 55.53           O  
ANISOU  406  O   ILE A  51     8396   5782   6920    638   1158    371       O  
ATOM    407  CB  ILE A  51      34.270 -16.399  20.789  1.00 50.37           C  
ANISOU  407  CB  ILE A  51     7976   5187   5974    863   1102    425       C  
ATOM    408  CG1 ILE A  51      35.269 -16.317  21.942  1.00 47.35           C  
ANISOU  408  CG1 ILE A  51     7724   4844   5424   1000   1062    449       C  
ATOM    409  CG2 ILE A  51      32.938 -15.703  21.153  1.00 40.65           C  
ANISOU  409  CG2 ILE A  51     6726   3905   4813    823   1185    424       C  
ATOM    410  CD1 ILE A  51      35.531 -14.879  22.412  1.00 42.34           C  
ANISOU  410  CD1 ILE A  51     7084   4280   4724   1014    951    415       C  
ATOM    411  N   LYS A  52      31.817 -18.611  19.813  1.00 57.39           N  
ANISOU  411  N   LYS A  52     8793   5845   7167    704   1434    444       N  
ATOM    412  CA  LYS A  52      30.649 -18.719  18.994  1.00 52.39           C  
ANISOU  412  CA  LYS A  52     8039   5168   6698    584   1495    407       C  
ATOM    413  C   LYS A  52      30.205 -17.368  18.528  1.00 48.06           C  
ANISOU  413  C   LYS A  52     7375   4699   6188    527   1392    362       C  
ATOM    414  O   LYS A  52      30.168 -16.444  19.282  1.00 39.06           O  
ANISOU  414  O   LYS A  52     6279   3587   4976    577   1367    376       O  
ATOM    415  CB  LYS A  52      29.536 -19.381  19.772  1.00 63.06           C  
ANISOU  415  CB  LYS A  52     9455   6397   8107    590   1698    444       C  
ATOM    416  CG  LYS A  52      28.906 -20.519  19.069  1.00 75.30           C  
ANISOU  416  CG  LYS A  52    10966   7857   9789    509   1813    429       C  
ATOM    417  CD  LYS A  52      27.559 -20.164  18.550  1.00 77.95           C  
ANISOU  417  CD  LYS A  52    11129   8199  10288    378   1813    364       C  
ATOM    418  CE  LYS A  52      26.500 -20.720  19.431  1.00 84.37           C  
ANISOU  418  CE  LYS A  52    11945   8918  11193    351   1994    382       C  
ATOM    419  NZ  LYS A  52      25.712 -19.694  20.148  1.00 85.96           N  
ANISOU  419  NZ  LYS A  52    12217   9135  11309    433   2015    427       N  
ATOM    420  N   ASN A  53      29.883 -17.269  17.257  1.00 56.40           N  
ANISOU  420  N   ASN A  53     8289   5792   7350    429   1330    306       N  
ATOM    421  CA  ASN A  53      29.485 -15.995  16.654  1.00 54.71           C  
ANISOU  421  CA  ASN A  53     7962   5652   7174    380   1234    263       C  
ATOM    422  C   ASN A  53      28.633 -16.315  15.451  1.00 56.87           C  
ANISOU  422  C   ASN A  53     8094   5923   7592    279   1243    207       C  
ATOM    423  O   ASN A  53      29.160 -16.679  14.413  1.00 51.68           O  
ANISOU  423  O   ASN A  53     7378   5301   6956    247   1162    176       O  
ATOM    424  CB  ASN A  53      30.697 -15.189  16.184  1.00 45.23           C  
ANISOU  424  CB  ASN A  53     6745   4553   5887    402   1063    248       C  
ATOM    425  CG  ASN A  53      30.294 -13.946  15.380  1.00 46.59           C  
ANISOU  425  CG  ASN A  53     6801   4794   6106    348    973    202       C  
ATOM    426  OD1 ASN A  53      29.295 -13.959  14.659  1.00 51.91           O  
ANISOU  426  OD1 ASN A  53     7372   5462   6891    283   1003    167       O  
ATOM    427  ND2 ASN A  53      31.062 -12.866  15.518  1.00 35.25           N  
ANISOU  427  ND2 ASN A  53     5384   3425   4586    380    866    201       N  
ATOM    428  N   LEU A  54      27.321 -16.176  15.577  1.00 63.64           N  
ANISOU  428  N   LEU A  54     8892   6743   8546    234   1337    192       N  
ATOM    429  CA  LEU A  54      26.442 -16.834  14.621  1.00 74.05           C  
ANISOU  429  CA  LEU A  54    10088   8038  10008    142   1377    136       C  
ATOM    430  C   LEU A  54      26.257 -16.100  13.315  1.00 78.60           C  
ANISOU  430  C   LEU A  54    10520   8710  10636     91   1250     69       C  
ATOM    431  O   LEU A  54      26.148 -16.729  12.260  1.00 82.33           O  
ANISOU  431  O   LEU A  54    10906   9189  11185     35   1220     17       O  
ATOM    432  CB  LEU A  54      25.085 -17.127  15.247  1.00 78.11           C  
ANISOU  432  CB  LEU A  54    10585   8475  10620    109   1541    140       C  
ATOM    433  CG  LEU A  54      25.217 -18.091  16.421  1.00 81.63           C  
ANISOU  433  CG  LEU A  54    11178   8809  11030    157   1692    206       C  
ATOM    434  CD1 LEU A  54      25.117 -17.335  17.758  1.00 82.82           C  
ANISOU  434  CD1 LEU A  54    11435   8946  11086    244   1746    269       C  
ATOM    435  CD2 LEU A  54      24.162 -19.170  16.314  1.00 80.34           C  
ANISOU  435  CD2 LEU A  54    10963   8547  11014     78   1847    183       C  
ATOM    436  N   ASP A  55      26.230 -14.776  13.386  1.00 73.71           N  
ANISOU  436  N   ASP A  55     9880   8158   9967    119   1177     70       N  
ATOM    437  CA  ASP A  55      25.795 -13.977  12.257  1.00 77.51           C  
ANISOU  437  CA  ASP A  55    10229   8722  10501     83   1085     12       C  
ATOM    438  C   ASP A  55      26.792 -13.996  11.092  1.00 81.98           C  
ANISOU  438  C   ASP A  55    10757   9352  11040     79    948    -16       C  
ATOM    439  O   ASP A  55      27.970 -14.321  11.260  1.00 82.94           O  
ANISOU  439  O   ASP A  55    10961   9471  11081    113    905     18       O  
ATOM    440  CB  ASP A  55      25.517 -12.552  12.718  1.00 76.30           C  
ANISOU  440  CB  ASP A  55    10084   8612  10293    122   1059     28       C  
ATOM    441  CG  ASP A  55      26.745 -11.886  13.272  1.00 65.08           C  
ANISOU  441  CG  ASP A  55     8774   7215   8740    184    983     71       C  
ATOM    442  OD1 ASP A  55      26.625 -11.192  14.314  1.00 46.19           O  
ANISOU  442  OD1 ASP A  55     6460   4806   6283    229   1019    107       O  
ATOM    443  OD2 ASP A  55      27.826 -12.071  12.661  1.00 61.49           O  
ANISOU  443  OD2 ASP A  55     8324   6795   8245    187    888     65       O  
ATOM    444  N   ILE A  56      26.307 -13.649   9.906  1.00 76.94           N  
ANISOU  444  N   ILE A  56     9993   8775  10467     45    883    -76       N  
ATOM    445  CA  ILE A  56      27.145 -13.701   8.722  1.00 74.99           C  
ANISOU  445  CA  ILE A  56     9706   8585  10202     46    764   -102       C  
ATOM    446  C   ILE A  56      27.269 -12.330   8.034  1.00 68.32           C  
ANISOU  446  C   ILE A  56     8809   7829   9322     72    660   -118       C  
ATOM    447  O   ILE A  56      26.283 -11.700   7.653  1.00 61.98           O  
ANISOU  447  O   ILE A  56     7920   7062   8568     64    662   -155       O  
ATOM    448  CB  ILE A  56      26.664 -14.797   7.759  1.00 81.50           C  
ANISOU  448  CB  ILE A  56    10443   9394  11128     -9    774   -164       C  
ATOM    449  CG1 ILE A  56      25.783 -14.219   6.663  1.00 86.36           C  
ANISOU  449  CG1 ILE A  56    10918  10082  11813    -29    719   -236       C  
ATOM    450  CG2 ILE A  56      25.923 -15.905   8.526  1.00 75.91           C  
ANISOU  450  CG2 ILE A  56     9761   8587  10495    -52    918   -163       C  
ATOM    451  CD1 ILE A  56      25.481 -15.232   5.597  1.00 93.19           C  
ANISOU  451  CD1 ILE A  56    11698  10945  12765    -75    700   -308       C  
ATOM    452  N   ASP A  57      28.507 -11.876   7.900  1.00 65.57           N  
ANISOU  452  N   ASP A  57     8513   7514   8885    108    574    -87       N  
ATOM    453  CA  ASP A  57      28.799 -10.518   7.486  1.00 58.74           C  
ANISOU  453  CA  ASP A  57     7630   6714   7973    136    494    -87       C  
ATOM    454  C   ASP A  57      29.689 -10.543   6.252  1.00 40.07           C  
ANISOU  454  C   ASP A  57     5228   4403   5595    145    392   -102       C  
ATOM    455  O   ASP A  57      30.892 -10.815   6.374  1.00 28.29           O  
ANISOU  455  O   ASP A  57     3795   2911   4044    160    352    -70       O  
ATOM    456  CB  ASP A  57      29.515  -9.791   8.630  1.00 65.94           C  
ANISOU  456  CB  ASP A  57     8652   7613   8791    169    494    -35       C  
ATOM    457  CG  ASP A  57      29.315  -8.290   8.583  1.00 74.92           C  
ANISOU  457  CG  ASP A  57     9782   8788   9897    190    460    -36       C  
ATOM    458  OD1 ASP A  57      29.045  -7.760   7.484  1.00 75.28           O  
ANISOU  458  OD1 ASP A  57     9748   8884   9972    191    411    -68       O  
ATOM    459  OD2 ASP A  57      29.420  -7.637   9.646  1.00 80.05           O  
ANISOU  459  OD2 ASP A  57    10512   9416  10488    211    484     -7       O  
ATOM    460  N   ILE A  58      29.113 -10.243   5.079  1.00 36.01           N  
ANISOU  460  N   ILE A  58     4615   3938   5128    146    352   -150       N  
ATOM    461  CA  ILE A  58      29.830 -10.446   3.804  1.00 35.19           C  
ANISOU  461  CA  ILE A  58     4471   3879   5019    161    266   -168       C  
ATOM    462  C   ILE A  58      30.340  -9.194   3.108  1.00 39.55           C  
ANISOU  462  C   ILE A  58     5012   4492   5525    202    193   -159       C  
ATOM    463  O   ILE A  58      29.601  -8.224   2.928  1.00 38.79           O  
ANISOU  463  O   ILE A  58     4881   4422   5434    221    197   -175       O  
ATOM    464  CB  ILE A  58      28.991 -11.235   2.776  1.00 36.24           C  
ANISOU  464  CB  ILE A  58     4506   4028   5237    143    261   -236       C  
ATOM    465  CG1 ILE A  58      28.582 -12.582   3.348  1.00 33.39           C  
ANISOU  465  CG1 ILE A  58     4157   3597   4933     93    339   -248       C  
ATOM    466  CG2 ILE A  58      29.807 -11.497   1.546  1.00 33.43           C  
ANISOU  466  CG2 ILE A  58     4126   3712   4863    169    176   -248       C  
ATOM    467  CD1 ILE A  58      29.783 -13.391   3.786  1.00 39.97           C  
ANISOU  467  CD1 ILE A  58     5085   4388   5714     97    341   -199       C  
ATOM    468  N   VAL A  59      31.606  -9.236   2.697  1.00 33.74           N  
ANISOU  468  N   VAL A  59     4306   3773   4741    218    134   -131       N  
ATOM    469  CA  VAL A  59      32.177  -8.156   1.896  1.00 37.07           C  
ANISOU  469  CA  VAL A  59     4715   4243   5126    255     73   -121       C  
ATOM    470  C   VAL A  59      32.524  -8.588   0.448  1.00 33.43           C  
ANISOU  470  C   VAL A  59     4198   3823   4679    284     13   -143       C  
ATOM    471  O   VAL A  59      33.202  -9.610   0.219  1.00 29.53           O  
ANISOU  471  O   VAL A  59     3715   3321   4184    278     -6   -136       O  
ATOM    472  CB  VAL A  59      33.378  -7.514   2.621  1.00 36.97           C  
ANISOU  472  CB  VAL A  59     4779   4222   5045    254     55    -70       C  
ATOM    473  CG1 VAL A  59      33.962  -6.387   1.810  1.00 32.39           C  
ANISOU  473  CG1 VAL A  59     4188   3681   4439    282      8    -60       C  
ATOM    474  CG2 VAL A  59      32.933  -6.981   3.958  1.00 43.79           C  
ANISOU  474  CG2 VAL A  59     5700   5049   5889    238    108    -57       C  
ATOM    475  N   VAL A  60      32.035  -7.834  -0.537  1.00 24.61           N  
ANISOU  475  N   VAL A  60     3028   2751   3570    325    -13   -169       N  
ATOM    476  CA  VAL A  60      32.339  -8.197  -1.931  1.00 25.32           C  
ANISOU  476  CA  VAL A  60     3072   2883   3665    368    -70   -190       C  
ATOM    477  C   VAL A  60      33.138  -7.093  -2.602  1.00 34.09           C  
ANISOU  477  C   VAL A  60     4200   4025   4727    418   -104   -154       C  
ATOM    478  O   VAL A  60      32.938  -5.909  -2.309  1.00 27.09           O  
ANISOU  478  O   VAL A  60     3334   3139   3820    429    -83   -139       O  
ATOM    479  CB  VAL A  60      31.075  -8.523  -2.763  1.00 28.09           C  
ANISOU  479  CB  VAL A  60     3337   3267   4070    390    -78   -263       C  
ATOM    480  CG1 VAL A  60      30.345  -9.768  -2.201  1.00 20.02           C  
ANISOU  480  CG1 VAL A  60     2290   2205   3112    329    -37   -304       C  
ATOM    481  CG2 VAL A  60      30.147  -7.338  -2.802  1.00 36.09           C  
ANISOU  481  CG2 VAL A  60     4322   4310   5080    425    -61   -279       C  
ATOM    482  N   GLU A  61      34.097  -7.470  -3.440  1.00 32.18           N  
ANISOU  482  N   GLU A  61     3958   3802   4467    447   -147   -137       N  
ATOM    483  CA  GLU A  61      34.739  -6.464  -4.279  1.00 39.87           C  
ANISOU  483  CA  GLU A  61     4939   4805   5404    502   -170   -107       C  
ATOM    484  C   GLU A  61      33.938  -6.367  -5.574  1.00 37.55           C  
ANISOU  484  C   GLU A  61     4588   4557   5121    577   -194   -152       C  
ATOM    485  O   GLU A  61      34.313  -6.956  -6.595  1.00 37.85           O  
ANISOU  485  O   GLU A  61     4606   4621   5153    622   -234   -160       O  
ATOM    486  CB  GLU A  61      36.188  -6.809  -4.594  1.00 37.49           C  
ANISOU  486  CB  GLU A  61     4661   4507   5075    506   -199    -60       C  
ATOM    487  CG  GLU A  61      37.136  -6.726  -3.426  1.00 39.13           C  
ANISOU  487  CG  GLU A  61     4920   4685   5261    448   -186    -18       C  
ATOM    488  CD  GLU A  61      38.570  -6.764  -3.903  1.00 54.04           C  
ANISOU  488  CD  GLU A  61     6818   6593   7123    465   -215     28       C  
ATOM    489  OE1 GLU A  61      39.462  -7.118  -3.103  1.00 54.85           O  
ANISOU  489  OE1 GLU A  61     6948   6687   7207    427   -221     55       O  
ATOM    490  OE2 GLU A  61      38.794  -6.445  -5.097  1.00 60.84           O  
ANISOU  490  OE2 GLU A  61     7656   7481   7979    523   -231     36       O  
ATOM    491  N   GLY A  62      32.820  -5.652  -5.496  1.00 28.66           N  
ANISOU  491  N   GLY A  62     3440   3446   4005    597   -171   -183       N  
ATOM    492  CA  GLY A  62      31.950  -5.423  -6.623  1.00 31.15           C  
ANISOU  492  CA  GLY A  62     3699   3815   4321    680   -194   -231       C  
ATOM    493  C   GLY A  62      30.677  -4.823  -6.097  1.00 39.32           C  
ANISOU  493  C   GLY A  62     4709   4859   5373    679   -158   -265       C  
ATOM    494  O   GLY A  62      30.660  -4.343  -4.969  1.00 31.10           O  
ANISOU  494  O   GLY A  62     3709   3777   4329    626   -113   -235       O  
ATOM    495  N   ASN A  63      29.613  -4.881  -6.893  1.00 44.08           N  
ANISOU  495  N   ASN A  63     5240   5518   5989    742   -181   -330       N  
ATOM    496  CA  ASN A  63      28.345  -4.250  -6.547  1.00 45.61           C  
ANISOU  496  CA  ASN A  63     5396   5738   6195    760   -150   -364       C  
ATOM    497  C   ASN A  63      27.510  -5.129  -5.607  1.00 45.98           C  
ANISOU  497  C   ASN A  63     5396   5762   6311    671   -122   -408       C  
ATOM    498  O   ASN A  63      27.046  -6.198  -5.991  1.00 45.21           O  
ANISOU  498  O   ASN A  63     5228   5683   6265    652   -151   -472       O  
ATOM    499  CB  ASN A  63      27.577  -3.917  -7.838  1.00 48.82           C  
ANISOU  499  CB  ASN A  63     5741   6228   6582    878   -190   -420       C  
ATOM    500  CG  ASN A  63      26.263  -3.193  -7.578  1.00 58.00           C  
ANISOU  500  CG  ASN A  63     6859   7432   7747    916   -160   -456       C  
ATOM    501  OD1 ASN A  63      26.095  -2.036  -7.979  1.00 59.45           O  
ANISOU  501  OD1 ASN A  63     7072   7643   7872   1009   -145   -433       O  
ATOM    502  ND2 ASN A  63      25.317  -3.874  -6.916  1.00 47.58           N  
ANISOU  502  ND2 ASN A  63     5469   6114   6494    848   -145   -510       N  
ATOM    503  N   ALA A  64      27.329  -4.671  -4.372  1.00 49.36           N  
ANISOU  503  N   ALA A  64     5867   6146   6742    619    -62   -372       N  
ATOM    504  CA  ALA A  64      26.600  -5.425  -3.352  1.00 46.81           C  
ANISOU  504  CA  ALA A  64     5515   5790   6481    538    -17   -398       C  
ATOM    505  C   ALA A  64      25.212  -5.885  -3.816  1.00 49.08           C  
ANISOU  505  C   ALA A  64     5685   6133   6831    551    -23   -487       C  
ATOM    506  O   ALA A  64      24.846  -7.057  -3.638  1.00 51.59           O  
ANISOU  506  O   ALA A  64     5952   6431   7219    486    -15   -534       O  
ATOM    507  CB  ALA A  64      26.498  -4.603  -2.058  1.00 43.82           C  
ANISOU  507  CB  ALA A  64     5205   5366   6080    509     50   -346       C  
ATOM    508  N   LEU A  65      24.462  -4.991  -4.438  1.00 54.72           N  
ANISOU  508  N   LEU A  65     6356   6916   7521    637    -35   -514       N  
ATOM    509  CA  LEU A  65      23.144  -5.343  -4.957  1.00 54.94           C  
ANISOU  509  CA  LEU A  65     6257   7018   7600    667    -54   -609       C  
ATOM    510  C   LEU A  65      23.145  -6.394  -6.038  1.00 53.07           C  
ANISOU  510  C   LEU A  65     5946   6814   7403    668   -124   -685       C  
ATOM    511  O   LEU A  65      22.425  -7.343  -5.936  1.00 51.81           O  
ANISOU  511  O   LEU A  65     5703   6652   7329    600   -116   -756       O  
ATOM    512  CB  LEU A  65      22.385  -4.124  -5.429  1.00 61.38           C  
ANISOU  512  CB  LEU A  65     7049   7913   8358    787    -65   -620       C  
ATOM    513  CG  LEU A  65      22.094  -3.064  -4.388  1.00 70.25           C  
ANISOU  513  CG  LEU A  65     8201   9026   9463    795      8   -582       C  
ATOM    514  CD1 LEU A  65      20.632  -2.820  -4.362  1.00 78.99           C  
ANISOU  514  CD1 LEU A  65     9183  10194  10637    792     26   -660       C  
ATOM    515  CD2 LEU A  65      22.575  -3.462  -3.042  1.00 66.09           C  
ANISOU  515  CD2 LEU A  65     7779   8396   8936    700     71   -503       C  
ATOM    516  N   GLU A  66      23.951  -6.229  -7.063  1.00 39.46           N  
ANISOU  516  N   GLU A  66     4255   5118   5621    743   -187   -673       N  
ATOM    517  CA  GLU A  66      24.095  -7.285  -8.019  1.00 48.06           C  
ANISOU  517  CA  GLU A  66     5292   6231   6739    749   -256   -740       C  
ATOM    518  C   GLU A  66      24.192  -8.603  -7.329  1.00 52.49           C  
ANISOU  518  C   GLU A  66     5845   6719   7380    621   -226   -758       C  
ATOM    519  O   GLU A  66      23.558  -9.546  -7.714  1.00 63.73           O  
ANISOU  519  O   GLU A  66     7179   8159   8877    584   -247   -851       O  
ATOM    520  CB  GLU A  66      25.390  -7.175  -8.774  1.00 55.26           C  
ANISOU  520  CB  GLU A  66     6281   7135   7581    808   -301   -687       C  
ATOM    521  CG  GLU A  66      25.521  -6.070  -9.713  1.00 70.04           C  
ANISOU  521  CG  GLU A  66     8194   9053   9364    933   -314   -645       C  
ATOM    522  CD  GLU A  66      26.601  -6.334 -10.684  1.00 79.98           C  
ANISOU  522  CD  GLU A  66     9504  10316  10569   1000   -362   -613       C  
ATOM    523  OE1 GLU A  66      27.425  -5.452 -10.918  1.00 86.72           O  
ANISOU  523  OE1 GLU A  66    10428  11168  11353   1074   -346   -544       O  
ATOM    524  OE2 GLU A  66      26.629  -7.441 -11.220  1.00 73.78           O  
ANISOU  524  OE2 GLU A  66     8692   9529   9813    979   -409   -657       O  
ATOM    525  N   PHE A  67      25.066  -8.678  -6.349  1.00 40.90           N  
ANISOU  525  N   PHE A  67     4476   5168   5896    557   -176   -670       N  
ATOM    526  CA  PHE A  67      25.410  -9.930  -5.681  1.00 38.30           C  
ANISOU  526  CA  PHE A  67     4170   4760   5621    454   -143   -667       C  
ATOM    527  C   PHE A  67      24.234 -10.434  -4.853  1.00 38.95           C  
ANISOU  527  C   PHE A  67     4187   4819   5795    373    -77   -718       C  
ATOM    528  O   PHE A  67      23.858 -11.591  -4.935  1.00 36.85           O  
ANISOU  528  O   PHE A  67     3870   4526   5604    311    -70   -782       O  
ATOM    529  CB  PHE A  67      26.638  -9.732  -4.789  1.00 39.82           C  
ANISOU  529  CB  PHE A  67     4484   4883   5762    422   -106   -561       C  
ATOM    530  CG  PHE A  67      27.123 -10.983  -4.170  1.00 37.32           C  
ANISOU  530  CG  PHE A  67     4208   4490   5480    340    -74   -548       C  
ATOM    531  CD1 PHE A  67      28.115 -11.727  -4.779  1.00 35.69           C  
ANISOU  531  CD1 PHE A  67     4038   4272   5251    351   -119   -537       C  
ATOM    532  CD2 PHE A  67      26.574 -11.441  -2.985  1.00 43.01           C  
ANISOU  532  CD2 PHE A  67     4937   5151   6255    262      8   -546       C  
ATOM    533  CE1 PHE A  67      28.563 -12.913  -4.219  1.00 47.75           C  
ANISOU  533  CE1 PHE A  67     5611   5727   6804    285    -84   -523       C  
ATOM    534  CE2 PHE A  67      27.024 -12.643  -2.400  1.00 37.43           C  
ANISOU  534  CE2 PHE A  67     4279   4366   5575    196     49   -531       C  
ATOM    535  CZ  PHE A  67      28.020 -13.372  -3.024  1.00 46.61           C  
ANISOU  535  CZ  PHE A  67     5481   5519   6711    209      2   -520       C  
ATOM    536  N   ALA A  68      23.666  -9.560  -4.032  1.00 46.20           N  
ANISOU  536  N   ALA A  68     5109   5739   6707    374    -21   -687       N  
ATOM    537  CA  ALA A  68      22.500  -9.940  -3.253  1.00 46.37           C  
ANISOU  537  CA  ALA A  68     5062   5741   6814    306     51   -730       C  
ATOM    538  C   ALA A  68      21.389 -10.452  -4.178  1.00 54.06           C  
ANISOU  538  C   ALA A  68     5890   6786   7864    312      9   -854       C  
ATOM    539  O   ALA A  68      20.776 -11.473  -3.897  1.00 64.54           O  
ANISOU  539  O   ALA A  68     7155   8077   9289    227     49   -914       O  
ATOM    540  CB  ALA A  68      22.024  -8.772  -2.402  1.00 36.46           C  
ANISOU  540  CB  ALA A  68     3832   4493   5527    331    108   -680       C  
ATOM    541  N   GLU A  69      21.136  -9.759  -5.272  1.00 53.88           N  
ANISOU  541  N   GLU A  69     5814   6863   7796    415    -70   -896       N  
ATOM    542  CA  GLU A  69      20.129 -10.166  -6.223  1.00 60.21           C  
ANISOU  542  CA  GLU A  69     6469   7749   8658    437   -126  -1024       C  
ATOM    543  C   GLU A  69      20.408 -11.551  -6.776  1.00 60.22           C  
ANISOU  543  C   GLU A  69     6447   7714   8718    376   -164  -1089       C  
ATOM    544  O   GLU A  69      19.553 -12.403  -6.823  1.00 59.24           O  
ANISOU  544  O   GLU A  69     6221   7589   8700    303   -151  -1186       O  
ATOM    545  CB  GLU A  69      20.051  -9.149  -7.356  1.00 58.86           C  
ANISOU  545  CB  GLU A  69     6268   7692   8404    584   -209  -1047       C  
ATOM    546  CG  GLU A  69      19.045  -8.035  -7.137  1.00 69.43           C  
ANISOU  546  CG  GLU A  69     7558   9100   9721    649   -178  -1046       C  
ATOM    547  CD  GLU A  69      19.396  -6.748  -7.865  1.00 87.78           C  
ANISOU  547  CD  GLU A  69     9935  11492  11924    801   -223  -1003       C  
ATOM    548  OE1 GLU A  69      20.429  -6.688  -8.544  1.00 92.58           O  
ANISOU  548  OE1 GLU A  69    10619  12091  12468    852   -273   -968       O  
ATOM    549  OE2 GLU A  69      18.629  -5.777  -7.780  1.00 92.92           O  
ANISOU  549  OE2 GLU A  69    10557  12204  12543    873   -201  -1001       O  
ATOM    550  N   TYR A  70      21.631 -11.752  -7.205  1.00 56.55           N  
ANISOU  550  N   TYR A  70     6080   7218   8187    405   -206  -1036       N  
ATOM    551  CA  TYR A  70      22.085 -13.033  -7.720  1.00 51.00           C  
ANISOU  551  CA  TYR A  70     5383   6474   7522    359   -240  -1082       C  
ATOM    552  C   TYR A  70      21.942 -14.127  -6.680  1.00 54.41           C  
ANISOU  552  C   TYR A  70     5829   6799   8046    223   -149  -1082       C  
ATOM    553  O   TYR A  70      21.409 -15.200  -6.969  1.00 43.85           O  
ANISOU  553  O   TYR A  70     4421   5442   6799    158   -152  -1179       O  
ATOM    554  CB  TYR A  70      23.547 -12.945  -8.141  1.00 44.96           C  
ANISOU  554  CB  TYR A  70     4736   5685   6660    415   -281   -997       C  
ATOM    555  CG  TYR A  70      24.018 -14.189  -8.827  1.00 45.16           C  
ANISOU  555  CG  TYR A  70     4770   5679   6709    392   -325  -1046       C  
ATOM    556  CD1 TYR A  70      23.558 -14.514 -10.094  1.00 44.92           C  
ANISOU  556  CD1 TYR A  70     4656   5722   6689    450   -416  -1156       C  
ATOM    557  CD2 TYR A  70      24.910 -15.053  -8.209  1.00 51.71           C  
ANISOU  557  CD2 TYR A  70     5694   6409   7544    321   -278   -986       C  
ATOM    558  CE1 TYR A  70      23.980 -15.661 -10.736  1.00 43.07           C  
ANISOU  558  CE1 TYR A  70     4437   5455   6473    432   -458  -1204       C  
ATOM    559  CE2 TYR A  70      25.341 -16.210  -8.842  1.00 48.67           C  
ANISOU  559  CE2 TYR A  70     5326   5992   7176    306   -314  -1029       C  
ATOM    560  CZ  TYR A  70      24.871 -16.506 -10.106  1.00 49.05           C  
ANISOU  560  CZ  TYR A  70     5294   6107   7237    358   -404  -1138       C  
ATOM    561  OH  TYR A  70      25.287 -17.651 -10.742  1.00 51.76           O  
ANISOU  561  OH  TYR A  70     5660   6414   7594    345   -440  -1185       O  
ATOM    562  N   ALA A  71      22.445 -13.848  -5.476  1.00 55.19           N  
ANISOU  562  N   ALA A  71     6026   6825   8119    185    -65   -975       N  
ATOM    563  CA  ALA A  71      22.301 -14.746  -4.334  1.00 52.29           C  
ANISOU  563  CA  ALA A  71     5690   6351   7825     73     40   -957       C  
ATOM    564  C   ALA A  71      20.835 -15.082  -4.088  1.00 58.48           C  
ANISOU  564  C   ALA A  71     6344   7144   8730      5     93  -1052       C  
ATOM    565  O   ALA A  71      20.491 -16.229  -3.791  1.00 52.69           O  
ANISOU  565  O   ALA A  71     5588   6337   8093    -91    152  -1099       O  
ATOM    566  CB  ALA A  71      22.907 -14.117  -3.078  1.00 44.63           C  
ANISOU  566  CB  ALA A  71     4837   5326   6796     69    114   -833       C  
ATOM    567  N   LYS A  72      19.969 -14.084  -4.198  1.00 62.07           N  
ANISOU  567  N   LYS A  72     6715   7689   9179     58     76  -1078       N  
ATOM    568  CA  LYS A  72      18.585 -14.264  -3.839  1.00 63.51           C  
ANISOU  568  CA  LYS A  72     6769   7892   9470      3    135  -1154       C  
ATOM    569  C   LYS A  72      17.909 -15.346  -4.614  1.00 64.19           C  
ANISOU  569  C   LYS A  72     6726   7994   9668    -58    101  -1297       C  
ATOM    570  O   LYS A  72      17.072 -16.015  -4.089  1.00 73.54           O  
ANISOU  570  O   LYS A  72     7826   9142  10972   -153    182  -1355       O  
ATOM    571  CB  LYS A  72      17.787 -12.982  -3.986  1.00 65.96           C  
ANISOU  571  CB  LYS A  72     7013   8313   9734     96    106  -1158       C  
ATOM    572  CG  LYS A  72      16.486 -13.010  -3.221  1.00 68.74           C  
ANISOU  572  CG  LYS A  72     7263   8678  10178     47    194  -1193       C  
ATOM    573  CD  LYS A  72      15.316 -12.619  -4.059  1.00 70.09           C  
ANISOU  573  CD  LYS A  72     7245   8932  10455     24    151  -1348       C  
ATOM    574  CE  LYS A  72      14.049 -12.705  -3.259  1.00 73.14           C  
ANISOU  574  CE  LYS A  72     7517   9340  10931    -18    243  -1378       C  
ATOM    575  NZ  LYS A  72      13.318 -11.421  -3.150  1.00 70.41           N  
ANISOU  575  NZ  LYS A  72     7193   9065  10496     85    252  -1308       N  
ATOM    576  N   ARG A  73      18.249 -15.519  -5.874  1.00 56.98           N  
ANISOU  576  N   ARG A  73     5796   7133   8720     -3    -13  -1358       N  
ATOM    577  CA  ARG A  73      17.563 -16.505  -6.665  1.00 58.21           C  
ANISOU  577  CA  ARG A  73     5825   7314   8979    -54    -60  -1509       C  
ATOM    578  C   ARG A  73      18.012 -17.912  -6.482  1.00 70.47           C  
ANISOU  578  C   ARG A  73     7441   8743  10593   -157    -18  -1522       C  
ATOM    579  O   ARG A  73      17.594 -18.789  -7.204  1.00 71.50           O  
ANISOU  579  O   ARG A  73     7496   8881  10790   -192    -72  -1644       O  
ATOM    580  CB  ARG A  73      17.604 -16.177  -8.131  1.00 61.92           C  
ANISOU  580  CB  ARG A  73     6230   7911   9385     65   -208  -1591       C  
ATOM    581  CG  ARG A  73      18.863 -15.723  -8.671  1.00 61.20           C  
ANISOU  581  CG  ARG A  73     6270   7831   9153    175   -276  -1498       C  
ATOM    582  CD  ARG A  73      18.839 -15.963 -10.124  1.00 68.05           C  
ANISOU  582  CD  ARG A  73     7088   8775   9992    254   -407  -1600       C  
ATOM    583  NE  ARG A  73      19.354 -14.835 -10.862  1.00 75.73           N  
ANISOU  583  NE  ARG A  73     8125   9823  10825    408   -482  -1535       N  
ATOM    584  CZ  ARG A  73      20.130 -14.934 -11.928  1.00 78.41           C  
ANISOU  584  CZ  ARG A  73     8500  10197  11095    497   -577  -1556       C  
ATOM    585  NH1 ARG A  73      20.468 -16.114 -12.385  1.00 76.86           N  
ANISOU  585  NH1 ARG A  73     8285   9967  10953    447   -617  -1644       N  
ATOM    586  NH2 ARG A  73      20.561 -13.852 -12.537  1.00 76.50           N  
ANISOU  586  NH2 ARG A  73     8320  10016  10730    637   -625  -1487       N  
ATOM    587  N   PHE A  74      18.859 -18.142  -5.506  1.00 70.62           N  
ANISOU  587  N   PHE A  74     7600   8648  10584   -199     77  -1401       N  
ATOM    588  CA  PHE A  74      19.309 -19.493  -5.223  1.00 71.69           C  
ANISOU  588  CA  PHE A  74     7807   8657  10776   -292    139  -1403       C  
ATOM    589  C   PHE A  74      19.149 -19.719  -3.743  1.00 69.94           C  
ANISOU  589  C   PHE A  74     7647   8326  10602   -375    296  -1323       C  
ATOM    590  O   PHE A  74      19.162 -20.856  -3.268  1.00 72.92           O  
ANISOU  590  O   PHE A  74     8065   8586  11056   -469    388  -1332       O  
ATOM    591  CB  PHE A  74      20.751 -19.699  -5.686  1.00 69.52           C  
ANISOU  591  CB  PHE A  74     7670   8357  10388   -229     77  -1330       C  
ATOM    592  CG  PHE A  74      20.963 -19.351  -7.127  1.00 71.44           C  
ANISOU  592  CG  PHE A  74     7866   8709  10568   -127    -71  -1392       C  
ATOM    593  CD1 PHE A  74      21.257 -18.053  -7.504  1.00 74.18           C  
ANISOU  593  CD1 PHE A  74     8221   9156  10808     -8   -141  -1339       C  
ATOM    594  CD2 PHE A  74      20.838 -20.312  -8.111  1.00 74.52           C  
ANISOU  594  CD2 PHE A  74     8210   9099  11006   -146   -136  -1507       C  
ATOM    595  CE1 PHE A  74      21.438 -17.725  -8.838  1.00 74.42           C  
ANISOU  595  CE1 PHE A  74     8217   9284  10775     99   -268  -1391       C  
ATOM    596  CE2 PHE A  74      21.017 -19.987  -9.445  1.00 75.33           C  
ANISOU  596  CE2 PHE A  74     8275   9304  11042    -38   -272  -1565       C  
ATOM    597  CZ  PHE A  74      21.316 -18.690  -9.807  1.00 72.65           C  
ANISOU  597  CZ  PHE A  74     7948   9065  10592     88   -335  -1503       C  
ATOM    598  N   LEU A  75      18.970 -18.611  -3.031  1.00 65.93           N  
ANISOU  598  N   LEU A  75     7149   7855  10045   -331    329  -1245       N  
ATOM    599  CA  LEU A  75      18.710 -18.619  -1.600  1.00 71.37           C  
ANISOU  599  CA  LEU A  75     7893   8458  10768   -387    474  -1167       C  
ATOM    600  C   LEU A  75      17.421 -17.872  -1.331  1.00 81.37           C  
ANISOU  600  C   LEU A  75     9028   9794  12095   -391    507  -1210       C  
ATOM    601  O   LEU A  75      17.443 -16.670  -1.074  1.00 87.28           O  
ANISOU  601  O   LEU A  75     9794  10607  12761   -312    487  -1147       O  
ATOM    602  CB  LEU A  75      19.840 -17.930  -0.849  1.00 71.21           C  
ANISOU  602  CB  LEU A  75     8034   8410  10613   -320    488  -1019       C  
ATOM    603  CG  LEU A  75      21.243 -18.473  -1.084  1.00 69.82           C  
ANISOU  603  CG  LEU A  75     7990   8184  10354   -295    447   -961       C  
ATOM    604  CD1 LEU A  75      22.223 -17.701  -0.226  1.00 70.36           C  
ANISOU  604  CD1 LEU A  75     8196   8237  10302   -235    465   -826       C  
ATOM    605  CD2 LEU A  75      21.286 -19.954  -0.760  1.00 66.07           C  
ANISOU  605  CD2 LEU A  75     7557   7586   9959   -386    537   -983       C  
ATOM    606  N   PRO A  76      16.288 -18.583  -1.391  1.00 86.70           N  
ANISOU  606  N   PRO A  76     9568  10457  12918   -484    560  -1320       N  
ATOM    607  CA  PRO A  76      14.970 -17.961  -1.233  1.00 87.34           C  
ANISOU  607  CA  PRO A  76     9498  10618  13071   -490    587  -1377       C  
ATOM    608  C   PRO A  76      14.849 -17.202   0.085  1.00 89.89           C  
ANISOU  608  C   PRO A  76     9893  10905  13355   -471    699  -1257       C  
ATOM    609  O   PRO A  76      14.860 -17.802   1.164  1.00 89.91           O  
ANISOU  609  O   PRO A  76     9969  10786  13406   -542    839  -1198       O  
ATOM    610  CB  PRO A  76      14.017 -19.156  -1.252  1.00 86.85           C  
ANISOU  610  CB  PRO A  76     9312  10499  13187   -624    662  -1497       C  
ATOM    611  CG  PRO A  76      14.767 -20.226  -2.000  1.00 87.91           C  
ANISOU  611  CG  PRO A  76     9500  10575  13326   -658    606  -1545       C  
ATOM    612  CD  PRO A  76      16.197 -20.038  -1.609  1.00 86.24           C  
ANISOU  612  CD  PRO A  76     9493  10305  12971   -593    602  -1399       C  
ATOM    613  N   GLY A  77      14.743 -15.883  -0.014  1.00 88.25           N  
ANISOU  613  N   GLY A  77     9674  10802  13056   -368    640  -1220       N  
ATOM    614  CA  GLY A  77      14.604 -15.037   1.156  1.00 85.65           C  
ANISOU  614  CA  GLY A  77     9413  10451  12679   -336    732  -1113       C  
ATOM    615  C   GLY A  77      14.150 -13.635   0.792  1.00 79.18           C  
ANISOU  615  C   GLY A  77     8534   9765  11787   -228    661  -1114       C  
ATOM    616  O   GLY A  77      13.896 -13.337  -0.377  1.00 77.48           O  
ANISOU  616  O   GLY A  77     8217   9662  11559   -172    543  -1199       O  
ATOM    617  N   LYS A  78      14.077 -12.768   1.786  1.00 72.03           N  
ANISOU  617  N   LYS A  78     7700   8843  10826   -189    735  -1017       N  
ATOM    618  CA  LYS A  78      13.649 -11.409   1.555  1.00 74.36           C  
ANISOU  618  CA  LYS A  78     7958   9248  11046    -82    691  -1004       C  
ATOM    619  C   LYS A  78      14.801 -10.453   1.482  1.00 72.72           C  
ANISOU  619  C   LYS A  78     7902   9048  10682     12    617   -912       C  
ATOM    620  O   LYS A  78      15.644 -10.409   2.341  1.00 73.50           O  
ANISOU  620  O   LYS A  78     8153   9053  10719      0    663   -813       O  
ATOM    621  CB  LYS A  78      12.662 -10.983   2.626  1.00 79.25           C  
ANISOU  621  CB  LYS A  78     8568   9842  11702    -95    823   -956       C  
ATOM    622  CG  LYS A  78      12.866  -9.637   3.198  1.00 78.54           C  
ANISOU  622  CG  LYS A  78     8512   9824  11507     18    811   -897       C  
ATOM    623  CD  LYS A  78      12.082  -9.541   4.463  1.00 81.94           C  
ANISOU  623  CD  LYS A  78     8961  10200  11972     -4    957   -836       C  
ATOM    624  CE  LYS A  78      11.716  -8.119   4.787  1.00 80.83           C  
ANISOU  624  CE  LYS A  78     8926  10085  11701    104    960   -744       C  
ATOM    625  NZ  LYS A  78      11.618  -7.948   6.237  1.00 76.34           N  
ANISOU  625  NZ  LYS A  78     8470   9413  11123     84   1097   -647       N  
ATOM    626  N   LEU A  79      14.824  -9.691   0.418  1.00 72.56           N  
ANISOU  626  N   LEU A  79     7838   9138  10594    107    503   -949       N  
ATOM    627  CA  LEU A  79      15.980  -8.845   0.134  1.00 74.94           C  
ANISOU  627  CA  LEU A  79     8272   9444  10758    191    434   -872       C  
ATOM    628  C   LEU A  79      15.710  -7.371   0.426  1.00 75.45           C  
ANISOU  628  C   LEU A  79     8374   9560  10732    289    444   -815       C  
ATOM    629  O   LEU A  79      14.970  -6.699  -0.297  1.00 77.45           O  
ANISOU  629  O   LEU A  79     8534   9923  10971    370    397   -868       O  
ATOM    630  CB  LEU A  79      16.446  -9.042  -1.310  1.00 78.58           C  
ANISOU  630  CB  LEU A  79     8693   9970  11192    237    306   -936       C  
ATOM    631  CG  LEU A  79      17.860  -8.576  -1.674  1.00 82.05           C  
ANISOU  631  CG  LEU A  79     9272  10390  11515    294    242   -860       C  
ATOM    632  CD1 LEU A  79      17.841  -7.226  -2.362  1.00 86.64           C  
ANISOU  632  CD1 LEU A  79     9859  11063  11997    423    181   -846       C  
ATOM    633  CD2 LEU A  79      18.759  -8.550  -0.452  1.00 81.39           C  
ANISOU  633  CD2 LEU A  79     9340  10195  11390    248    314   -749       C  
ATOM    634  N   VAL A  80      16.316  -6.889   1.505  1.00 73.08           N  
ANISOU  634  N   VAL A  80     8218   9180  10369    286    506   -710       N  
ATOM    635  CA  VAL A  80      16.199  -5.500   1.928  1.00 73.63           C  
ANISOU  635  CA  VAL A  80     8354   9274  10347    370    526   -646       C  
ATOM    636  C   VAL A  80      17.405  -4.696   1.424  1.00 73.96           C  
ANISOU  636  C   VAL A  80     8514   9317  10272    437    450   -593       C  
ATOM    637  O   VAL A  80      18.550  -5.044   1.719  1.00 73.01           O  
ANISOU  637  O   VAL A  80     8498   9122  10121    396    441   -543       O  
ATOM    638  CB  VAL A  80      16.110  -5.417   3.486  1.00 62.51           C  
ANISOU  638  CB  VAL A  80     7039   7774   8939    329    644   -567       C  
ATOM    639  CG1 VAL A  80      16.109  -3.965   3.992  1.00 57.25           C  
ANISOU  639  CG1 VAL A  80     6466   7118   8168    415    665   -498       C  
ATOM    640  CG2 VAL A  80      14.882  -6.152   3.989  1.00 60.24           C  
ANISOU  640  CG2 VAL A  80     6634   7481   8772    267    736   -614       C  
ATOM    641  N   LYS A  81      17.194  -3.610   0.701  1.00 77.94           N  
ANISOU  641  N   LYS A  81     8997   9906  10711    543    400   -605       N  
ATOM    642  CA  LYS A  81      18.318  -2.730   0.418  1.00 81.22           C  
ANISOU  642  CA  LYS A  81     9535  10309  11014    608    356   -542       C  
ATOM    643  C   LYS A  81      18.551  -1.946   1.661  1.00 80.48           C  
ANISOU  643  C   LYS A  81     9575  10135  10868    594    430   -453       C  
ATOM    644  O   LYS A  81      18.000  -2.261   2.689  1.00 88.31           O  
ANISOU  644  O   LYS A  81    10566  11081  11905    539    508   -439       O  
ATOM    645  CB  LYS A  81      18.099  -1.782  -0.741  1.00 82.97           C  
ANISOU  645  CB  LYS A  81     9718  10632  11175    736    308   -568       C  
ATOM    646  CG  LYS A  81      17.115  -2.259  -1.743  1.00 90.27           C  
ANISOU  646  CG  LYS A  81    10569  11628  12100    783    210   -634       C  
ATOM    647  CD  LYS A  81      17.779  -2.933  -2.897  1.00 97.35           C  
ANISOU  647  CD  LYS A  81    11293  12635  13059    820    181   -742       C  
ATOM    648  CE  LYS A  81      16.895  -4.021  -3.427  1.00 97.24           C  
ANISOU  648  CE  LYS A  81    11180  12610  13156    718    156   -819       C  
ATOM    649  NZ  LYS A  81      17.183  -4.287  -4.825  1.00 94.15           N  
ANISOU  649  NZ  LYS A  81    10792  12237  12743    742     61   -851       N  
ATOM    650  N   HIS A  82      19.355  -0.914   1.605  1.00 71.01           N  
ANISOU  650  N   HIS A  82     8492   8915   9575    643    411   -395       N  
ATOM    651  CA  HIS A  82      19.620  -0.190   2.816  1.00 72.13           C  
ANISOU  651  CA  HIS A  82     8763   8983   9661    634    473   -321       C  
ATOM    652  C   HIS A  82      20.046   1.164   2.458  1.00 73.04           C  
ANISOU  652  C   HIS A  82     8966   9107   9679    719    460   -283       C  
ATOM    653  O   HIS A  82      20.229   1.493   1.309  1.00 65.33           O  
ANISOU  653  O   HIS A  82     7972   8179   8673    779    403   -300       O  
ATOM    654  CB  HIS A  82      20.770  -0.798   3.629  1.00 70.95           C  
ANISOU  654  CB  HIS A  82     8708   8741   9508    548    476   -277       C  
ATOM    655  CG  HIS A  82      20.399  -2.002   4.430  1.00 70.53           C  
ANISOU  655  CG  HIS A  82     8624   8644   9531    470    533   -286       C  
ATOM    656  ND1 HIS A  82      19.246  -2.081   5.170  1.00 70.69           N  
ANISOU  656  ND1 HIS A  82     8609   8661   9589    468    617   -288       N  
ATOM    657  CD2 HIS A  82      21.054  -3.161   4.636  1.00 67.79           C  
ANISOU  657  CD2 HIS A  82     8283   8248   9226    395    529   -287       C  
ATOM    658  CE1 HIS A  82      19.196  -3.249   5.774  1.00 70.07           C  
ANISOU  658  CE1 HIS A  82     8516   8529   9577    393    667   -291       C  
ATOM    659  NE2 HIS A  82      20.283  -3.923   5.468  1.00 67.26           N  
ANISOU  659  NE2 HIS A  82     8189   8144   9223    349    615   -291       N  
ATOM    660  N   ASP A  83      20.176   1.970   3.482  1.00 85.96           N  
ANISOU  660  N   ASP A  83    10706  10690  11266    726    520   -230       N  
ATOM    661  CA  ASP A  83      20.765   3.249   3.323  1.00 92.91           C  
ANISOU  661  CA  ASP A  83    11705  11541  12055    778    516   -185       C  
ATOM    662  C   ASP A  83      22.132   3.076   3.956  1.00 90.07           C  
ANISOU  662  C   ASP A  83    11448  11098  11675    701    495   -147       C  
ATOM    663  O   ASP A  83      22.293   3.213   5.151  1.00 89.73           O  
ANISOU  663  O   ASP A  83    11469  10994  11632    647    532   -120       O  
ATOM    664  CB  ASP A  83      19.964   4.269   4.106  1.00 99.56           C  
ANISOU  664  CB  ASP A  83    12608  12370  12849    832    590   -155       C  
ATOM    665  CG  ASP A  83      18.702   4.702   3.401  1.00101.74           C  
ANISOU  665  CG  ASP A  83    12803  12739  13114    939    601   -186       C  
ATOM    666  OD1 ASP A  83      18.776   5.267   2.305  1.00 99.45           O  
ANISOU  666  OD1 ASP A  83    12476  12506  12806   1001    550   -210       O  
ATOM    667  OD2 ASP A  83      17.629   4.502   3.965  1.00101.98           O  
ANISOU  667  OD2 ASP A  83    12809  12789  13151    970    663   -184       O  
ATOM    668  N   LYS A  84      23.102   2.756   3.123  1.00 81.19           N  
ANISOU  668  N   LYS A  84    10336   9978  10533    703    435   -146       N  
ATOM    669  CA  LYS A  84      24.536   2.694   3.418  1.00 76.64           C  
ANISOU  669  CA  LYS A  84     9832   9343   9944    635    400   -119       C  
ATOM    670  C   LYS A  84      25.088   2.587   2.025  1.00 77.59           C  
ANISOU  670  C   LYS A  84     9900   9504  10076    653    335   -136       C  
ATOM    671  O   LYS A  84      24.489   1.936   1.206  1.00 74.26           O  
ANISOU  671  O   LYS A  84     9377   9130   9707    649    305   -177       O  
ATOM    672  CB  LYS A  84      24.881   1.497   4.249  1.00 78.77           C  
ANISOU  672  CB  LYS A  84    10097   9575  10256    552    408   -118       C  
ATOM    673  CG  LYS A  84      26.205   1.611   4.960  1.00 86.76           C  
ANISOU  673  CG  LYS A  84    11225  10514  11227    516    446    -79       C  
ATOM    674  CD  LYS A  84      26.136   2.522   6.143  1.00 83.98           C  
ANISOU  674  CD  LYS A  84    10953  10120  10837    472    398    -57       C  
ATOM    675  CE  LYS A  84      27.336   2.374   6.999  1.00 80.98           C  
ANISOU  675  CE  LYS A  84    10659   9679  10430    428    420    -34       C  
ATOM    676  NZ  LYS A  84      27.482   0.964   7.293  1.00 81.23           N  
ANISOU  676  NZ  LYS A  84    10784   9672  10409    401    382    -19       N  
ATOM    677  N   PHE A  85      26.231   3.172   1.738  1.00 79.83           N  
ANISOU  677  N   PHE A  85    10254   9764  10312    671    319   -108       N  
ATOM    678  CA  PHE A  85      26.591   3.414   0.370  1.00 90.87           C  
ANISOU  678  CA  PHE A  85    11617  11200  11710    709    270   -115       C  
ATOM    679  C   PHE A  85      26.282   2.246  -0.545  1.00 84.45           C  
ANISOU  679  C   PHE A  85    10684  10453  10950    721    225   -164       C  
ATOM    680  O   PHE A  85      25.693   2.469  -1.580  1.00 91.75           O  
ANISOU  680  O   PHE A  85    11546  11445  11871    805    212   -196       O  
ATOM    681  CB  PHE A  85      28.063   3.878   0.286  1.00100.40           C  
ANISOU  681  CB  PHE A  85    12890  12355  12903    653    243    -80       C  
ATOM    682  CG  PHE A  85      28.780   3.461  -0.964  1.00102.21           C  
ANISOU  682  CG  PHE A  85    13086  12617  13134    690    199    -80       C  
ATOM    683  CD1 PHE A  85      28.453   3.995  -2.179  1.00101.42           C  
ANISOU  683  CD1 PHE A  85    12979  12553  13003    791    209    -82       C  
ATOM    684  CD2 PHE A  85      29.812   2.552  -0.903  1.00102.22           C  
ANISOU  684  CD2 PHE A  85    13067  12612  13159    634    152    -75       C  
ATOM    685  CE1 PHE A  85      29.126   3.615  -3.303  1.00105.08           C  
ANISOU  685  CE1 PHE A  85    13420  13044  13463    837    174    -77       C  
ATOM    686  CE2 PHE A  85      30.476   2.158  -2.025  1.00104.35           C  
ANISOU  686  CE2 PHE A  85    13310  12910  13428    674    116    -71       C  
ATOM    687  CZ  PHE A  85      30.140   2.682  -3.222  1.00107.91           C  
ANISOU  687  CZ  PHE A  85    13756  13394  13849    775    128    -71       C  
ATOM    688  N   MET A  86      26.599   1.027  -0.161  1.00 60.42           N  
ANISOU  688  N   MET A  86     7612   7392   7952    642    200   -173       N  
ATOM    689  CA  MET A  86      26.185  -0.170  -0.894  1.00 59.30           C  
ANISOU  689  CA  MET A  86     7365   7301   7865    641    160   -225       C  
ATOM    690  C   MET A  86      25.976  -1.348   0.050  1.00 51.12           C  
ANISOU  690  C   MET A  86     6306   6232   6886    554    180   -238       C  
ATOM    691  O   MET A  86      26.875  -2.144   0.273  1.00 42.18           O  
ANISOU  691  O   MET A  86     5198   5065   5765    497    160   -223       O  
ATOM    692  CB  MET A  86      27.225  -0.550  -1.934  1.00 54.26           C  
ANISOU  692  CB  MET A  86     6722   6676   7220    653    100   -220       C  
ATOM    693  CG  MET A  86      27.346   0.429  -3.067  1.00 56.28           C  
ANISOU  693  CG  MET A  86     6989   6969   7427    752     86   -212       C  
ATOM    694  SD  MET A  86      27.480  -0.446  -4.626  1.00124.39           S  
ANISOU  694  SD  MET A  86    15533  15661  16068    810     13   -256       S  
ATOM    695  CE  MET A  86      25.983  -1.439  -4.554  1.00 63.15           C  
ANISOU  695  CE  MET A  86     7654   7959   8381    797      3   -342       C  
ATOM    696  N   THR A  87      24.777  -1.458   0.589  1.00 46.27           N  
ANISOU  696  N   THR A  87     5645   5628   6306    550    227   -264       N  
ATOM    697  CA  THR A  87      24.546  -2.360   1.684  1.00 53.27           C  
ANISOU  697  CA  THR A  87     6534   6466   7240    474    273   -263       C  
ATOM    698  C   THR A  87      23.210  -3.045   1.496  1.00 52.30           C  
ANISOU  698  C   THR A  87     6293   6384   7193    469    297   -326       C  
ATOM    699  O   THR A  87      22.204  -2.423   1.126  1.00 53.86           O  
ANISOU  699  O   THR A  87     6431   6641   7394    528    306   -356       O  
ATOM    700  CB  THR A  87      24.609  -1.604   3.022  1.00 60.68           C  
ANISOU  700  CB  THR A  87     7575   7347   8134    460    333   -211       C  
ATOM    701  OG1 THR A  87      25.982  -1.364   3.357  1.00 62.17           O  
ANISOU  701  OG1 THR A  87     7862   7490   8271    435    306   -165       O  
ATOM    702  CG2 THR A  87      23.968  -2.405   4.131  1.00 66.52           C  
ANISOU  702  CG2 THR A  87     8306   8046   8921    408    400   -212       C  
ATOM    703  N   ALA A  88      23.207  -4.344   1.732  1.00 38.01           N  
ANISOU  703  N   ALA A  88     4449   4545   5449    399    308   -348       N  
ATOM    704  CA  ALA A  88      21.999  -5.112   1.541  1.00 43.36           C  
ANISOU  704  CA  ALA A  88     5006   5253   6216    376    333   -417       C  
ATOM    705  C   ALA A  88      21.991  -6.175   2.601  1.00 52.96           C  
ANISOU  705  C   ALA A  88     6247   6389   7485    290    403   -403       C  
ATOM    706  O   ALA A  88      23.032  -6.474   3.191  1.00 59.96           O  
ANISOU  706  O   ALA A  88     7234   7212   8335    260    408   -350       O  
ATOM    707  CB  ALA A  88      21.982  -5.740   0.156  1.00 37.20           C  
ANISOU  707  CB  ALA A  88     4131   4532   5470    393    255   -487       C  
ATOM    708  N   SER A  89      20.812  -6.733   2.851  1.00 57.53           N  
ANISOU  708  N   SER A  89     6735   6972   8151    256    463   -450       N  
ATOM    709  CA  SER A  89      20.679  -7.880   3.736  1.00 54.71           C  
ANISOU  709  CA  SER A  89     6391   6535   7860    174    544   -444       C  
ATOM    710  C   SER A  89      19.687  -8.876   3.142  1.00 53.72           C  
ANISOU  710  C   SER A  89     6122   6434   7854    125    556   -536       C  
ATOM    711  O   SER A  89      18.580  -8.500   2.781  1.00 56.98           O  
ANISOU  711  O   SER A  89     6423   6916   8309    148    559   -591       O  
ATOM    712  CB  SER A  89      20.250  -7.421   5.125  1.00 54.27           C  
ANISOU  712  CB  SER A  89     6402   6429   7789    173    645   -386       C  
ATOM    713  OG  SER A  89      21.220  -6.543   5.666  1.00 54.79           O  
ANISOU  713  OG  SER A  89     6602   6470   7747    212    625   -313       O  
ATOM    714  N   LEU A  90      20.070 -10.133   3.069  1.00 57.98           N  
ANISOU  714  N   LEU A  90     6664   6922   8445     61    559   -558       N  
ATOM    715  CA  LEU A  90      19.146 -11.127   2.600  1.00 58.18           C  
ANISOU  715  CA  LEU A  90     6560   6951   8593     -3    582   -651       C  
ATOM    716  C   LEU A  90      18.696 -11.911   3.796  1.00 65.86           C  
ANISOU  716  C   LEU A  90     7554   7825   9643    -81    719   -630       C  
ATOM    717  O   LEU A  90      19.479 -12.516   4.500  1.00 69.96           O  
ANISOU  717  O   LEU A  90     8186   8253  10144   -114    766   -575       O  
ATOM    718  CB  LEU A  90      19.770 -12.033   1.556  1.00 62.89           C  
ANISOU  718  CB  LEU A  90     7139   7550   9206    -23    501   -702       C  
ATOM    719  CG  LEU A  90      18.921 -12.964   0.705  1.00 64.75           C  
ANISOU  719  CG  LEU A  90     7225   7817   9560    -74    485   -824       C  
ATOM    720  CD1 LEU A  90      17.651 -12.373   0.262  1.00 66.87           C  
ANISOU  720  CD1 LEU A  90     7351   8186   9871    -41    474   -893       C  
ATOM    721  CD2 LEU A  90      19.660 -13.396  -0.474  1.00 60.29           C  
ANISOU  721  CD2 LEU A  90     6650   7284   8974    -53    372   -872       C  
ATOM    722  N   PHE A  91      17.403 -11.874   4.022  1.00 65.01           N  
ANISOU  722  N   PHE A  91     7342   7740   9617   -102    789   -671       N  
ATOM    723  CA  PHE A  91      16.784 -12.603   5.116  1.00 66.92           C  
ANISOU  723  CA  PHE A  91     7591   7891   9945   -174    935   -654       C  
ATOM    724  C   PHE A  91      16.235 -13.922   4.612  1.00 73.00           C  
ANISOU  724  C   PHE A  91     8252   8631  10854   -270    964   -749       C  
ATOM    725  O   PHE A  91      15.212 -13.954   3.928  1.00 79.69           O  
ANISOU  725  O   PHE A  91     8936   9552  11790   -291    941   -848       O  
ATOM    726  CB  PHE A  91      15.643 -11.784   5.712  1.00 72.85           C  
ANISOU  726  CB  PHE A  91     8279   8680  10719   -148   1006   -646       C  
ATOM    727  CG  PHE A  91      16.086 -10.497   6.335  1.00 68.34           C  
ANISOU  727  CG  PHE A  91     7825   8123  10017    -60    995   -554       C  
ATOM    728  CD1 PHE A  91      16.423 -10.446   7.677  1.00 66.99           C  
ANISOU  728  CD1 PHE A  91     7793   7861   9800    -56   1093   -459       C  
ATOM    729  CD2 PHE A  91      16.168  -9.337   5.579  1.00 65.13           C  
ANISOU  729  CD2 PHE A  91     7396   7819   9533     24    891   -564       C  
ATOM    730  CE1 PHE A  91      16.838  -9.250   8.260  1.00 66.68           C  
ANISOU  730  CE1 PHE A  91     7864   7832   9640     22   1078   -384       C  
ATOM    731  CE2 PHE A  91      16.578  -8.147   6.152  1.00 62.70           C  
ANISOU  731  CE2 PHE A  91     7200   7513   9109     98    886   -484       C  
ATOM    732  CZ  PHE A  91      16.918  -8.105   7.498  1.00 61.34           C  
ANISOU  732  CZ  PHE A  91     7162   7249   8894     93    977   -398       C  
ATOM    733  N   LEU A  92      16.912 -15.011   4.953  1.00 76.35           N  
ANISOU  733  N   LEU A  92     8766   8948  11294   -325   1014   -723       N  
ATOM    734  CA  LEU A  92      16.500 -16.335   4.504  1.00 86.92           C  
ANISOU  734  CA  LEU A  92    10025  10238  12764   -422   1049   -812       C  
ATOM    735  C   LEU A  92      15.354 -16.885   5.340  1.00101.91           C  
ANISOU  735  C   LEU A  92    11860  12068  14795   -503   1211   -830       C  
ATOM    736  O   LEU A  92      15.371 -16.794   6.569  1.00108.01           O  
ANISOU  736  O   LEU A  92    12733  12763  15544   -495   1331   -738       O  
ATOM    737  CB  LEU A  92      17.680 -17.292   4.569  1.00 80.96           C  
ANISOU  737  CB  LEU A  92     9404   9388  11968   -441   1052   -770       C  
ATOM    738  CG  LEU A  92      18.922 -16.675   3.943  1.00 75.81           C  
ANISOU  738  CG  LEU A  92     8832   8796  11177   -355    910   -729       C  
ATOM    739  CD1 LEU A  92      20.089 -17.624   4.095  1.00 69.59           C  
ANISOU  739  CD1 LEU A  92     8177   7919  10346   -367    921   -682       C  
ATOM    740  CD2 LEU A  92      18.646 -16.327   2.478  1.00 74.13           C  
ANISOU  740  CD2 LEU A  92     8487   8703  10977   -329    770   -829       C  
ATOM    741  N   LYS A  93      14.366 -17.465   4.667  1.00107.35           N  
ANISOU  741  N   LYS A  93    12380  12786  15624   -579   1214   -953       N  
ATOM    742  CA  LYS A  93      13.206 -18.032   5.341  1.00113.83           C  
ANISOU  742  CA  LYS A  93    13113  13545  16594   -669   1371   -985       C  
ATOM    743  C   LYS A  93      13.608 -19.056   6.405  1.00114.92           C  
ANISOU  743  C   LYS A  93    13394  13512  16760   -727   1532   -909       C  
ATOM    744  O   LYS A  93      12.947 -19.181   7.442  1.00115.22           O  
ANISOU  744  O   LYS A  93    13440  13478  16859   -758   1691   -866       O  
ATOM    745  CB  LYS A  93      12.259 -18.656   4.318  1.00118.79           C  
ANISOU  745  CB  LYS A  93    13536  14225  17372   -754   1332  -1146       C  
ATOM    746  CG  LYS A  93      11.745 -17.665   3.287  1.00121.85           C  
ANISOU  746  CG  LYS A  93    13775  14790  17731   -683   1181  -1228       C  
ATOM    747  CD  LYS A  93      10.965 -16.538   3.954  1.00124.38           C  
ANISOU  747  CD  LYS A  93    14052  15178  18030   -623   1232  -1179       C  
ATOM    748  CE  LYS A  93       9.765 -17.077   4.726  1.00126.31           C  
ANISOU  748  CE  LYS A  93    14191  15366  18435   -721   1400  -1210       C  
ATOM    749  NZ  LYS A  93       8.823 -16.000   5.143  1.00126.30           N  
ANISOU  749  NZ  LYS A  93    14105  15457  18427   -660   1434  -1190       N  
ATOM    750  N   GLY A  94      14.698 -19.776   6.145  1.00112.02           N  
ANISOU  750  N   GLY A  94    13144  13080  16339   -730   1494   -888       N  
ATOM    751  CA  GLY A  94      15.221 -20.743   7.093  1.00109.37           C  
ANISOU  751  CA  GLY A  94    12964  12585  16005   -762   1636   -810       C  
ATOM    752  C   GLY A  94      15.522 -20.127   8.447  1.00105.61           C  
ANISOU  752  C   GLY A  94    12634  12066  15428   -687   1728   -672       C  
ATOM    753  O   GLY A  94      15.680 -20.839   9.439  1.00102.33           O  
ANISOU  753  O   GLY A  94    12339  11520  15022   -704   1879   -603       O  
ATOM    754  N   GLY A  95      15.604 -18.798   8.483  1.00103.87           N  
ANISOU  754  N   GLY A  95    12410  11952  15105   -598   1639   -635       N  
ATOM    755  CA  GLY A  95      15.855 -18.070   9.715  1.00 99.87           C  
ANISOU  755  CA  GLY A  95    12035  11417  14494   -520   1707   -515       C  
ATOM    756  C   GLY A  95      16.984 -17.053   9.638  1.00 89.12           C  
ANISOU  756  C   GLY A  95    10779  10125  12958   -415   1570   -451       C  
ATOM    757  O   GLY A  95      16.795 -15.878   9.942  1.00 75.31           O  
ANISOU  757  O   GLY A  95     9032   8442  11141   -350   1540   -416       O  
ATOM    758  N   LEU A  96      18.161 -17.504   9.220  1.00 92.46           N  
ANISOU  758  N   LEU A  96    11289  10531  13310   -400   1490   -438       N  
ATOM    759  CA  LEU A  96      19.356 -16.672   9.303  1.00 94.27           C  
ANISOU  759  CA  LEU A  96    11633  10806  13379   -309   1382   -369       C  
ATOM    760  C   LEU A  96      19.419 -15.604   8.210  1.00 88.69           C  
ANISOU  760  C   LEU A  96    10834  10233  12631   -269   1221   -416       C  
ATOM    761  O   LEU A  96      18.761 -15.714   7.173  1.00 87.67           O  
ANISOU  761  O   LEU A  96    10559  10165  12586   -307   1167   -510       O  
ATOM    762  CB  LEU A  96      20.623 -17.534   9.306  1.00 96.88           C  
ANISOU  762  CB  LEU A  96    12090  11075  13645   -299   1362   -331       C  
ATOM    763  CG  LEU A  96      21.597 -17.199  10.444  1.00 95.71           C  
ANISOU  763  CG  LEU A  96    12120  10889  13358   -219   1385   -222       C  
ATOM    764  CD1 LEU A  96      22.724 -18.216  10.511  1.00 95.87           C  
ANISOU  764  CD1 LEU A  96    12256  10845  13326   -208   1387   -188       C  
ATOM    765  CD2 LEU A  96      22.145 -15.770  10.350  1.00 91.19           C  
ANISOU  765  CD2 LEU A  96    11565  10413  12669   -145   1261   -193       C  
ATOM    766  N   ARG A  97      20.219 -14.571   8.455  1.00 80.69           N  
ANISOU  766  N   ARG A  97     9910   9263  11487   -190   1148   -352       N  
ATOM    767  CA  ARG A  97      20.227 -13.398   7.595  1.00 74.46           C  
ANISOU  767  CA  ARG A  97     9054   8589  10650   -141   1022   -381       C  
ATOM    768  C   ARG A  97      21.634 -12.950   7.160  1.00 67.73           C  
ANISOU  768  C   ARG A  97     8287   7769   9678    -87    900   -344       C  
ATOM    769  O   ARG A  97      22.547 -12.782   7.979  1.00 60.42           O  
ANISOU  769  O   ARG A  97     7494   6803   8659    -53    910   -268       O  
ATOM    770  CB  ARG A  97      19.469 -12.257   8.277  1.00 71.28           C  
ANISOU  770  CB  ARG A  97     8643   8216  10223    -98   1065   -350       C  
ATOM    771  CG  ARG A  97      20.303 -11.384   9.193  1.00 62.88           C  
ANISOU  771  CG  ARG A  97     7729   7134   9027    -30   1058   -259       C  
ATOM    772  CD  ARG A  97      20.410  -9.978   8.646  1.00 66.85           C  
ANISOU  772  CD  ARG A  97     8213   7730   9458     32    957   -262       C  
ATOM    773  NE  ARG A  97      20.559  -9.012   9.731  1.00 81.05           N  
ANISOU  773  NE  ARG A  97    10122   9508  11166     86    993   -191       N  
ATOM    774  CZ  ARG A  97      20.236  -7.725   9.636  1.00 96.25           C  
ANISOU  774  CZ  ARG A  97    12038  11491  13042    141    960   -186       C  
ATOM    775  NH1 ARG A  97      19.741  -7.244   8.501  1.00101.84           N  
ANISOU  775  NH1 ARG A  97    12631  12286  13778    156    893   -244       N  
ATOM    776  NH2 ARG A  97      20.404  -6.916  10.675  1.00 96.77           N  
ANISOU  776  NH2 ARG A  97    12216  11526  13025    187    996   -125       N  
ATOM    777  N   ILE A  98      21.777 -12.750   5.855  1.00 64.24           N  
ANISOU  777  N   ILE A  98     7762   7406   9240    -75    786   -402       N  
ATOM    778  CA  ILE A  98      23.045 -12.397   5.234  1.00 57.25           C  
ANISOU  778  CA  ILE A  98     6935   6558   8261    -30    674   -377       C  
ATOM    779  C   ILE A  98      23.184 -10.892   5.048  1.00 54.86           C  
ANISOU  779  C   ILE A  98     6638   6327   7878     38    608   -353       C  
ATOM    780  O   ILE A  98      22.394 -10.277   4.337  1.00 58.40           O  
ANISOU  780  O   ILE A  98     6988   6848   8354     61    574   -403       O  
ATOM    781  CB  ILE A  98      23.145 -13.065   3.851  1.00 58.61           C  
ANISOU  781  CB  ILE A  98     7020   6769   8479    -47    592   -451       C  
ATOM    782  CG1 ILE A  98      22.781 -14.549   3.965  1.00 58.25           C  
ANISOU  782  CG1 ILE A  98     6954   6647   8531   -123    667   -491       C  
ATOM    783  CG2 ILE A  98      24.529 -12.872   3.252  1.00 61.99           C  
ANISOU  783  CG2 ILE A  98     7515   7223   8814     -1    492   -417       C  
ATOM    784  CD1 ILE A  98      22.499 -15.234   2.637  1.00 60.36           C  
ANISOU  784  CD1 ILE A  98     7113   6952   8869   -150    600   -588       C  
ATOM    785  N   ASP A  99      24.176 -10.301   5.702  1.00 48.19           N  
ANISOU  785  N   ASP A  99     5912   5464   6935     72    593   -281       N  
ATOM    786  CA  ASP A  99      24.548  -8.923   5.430  1.00 46.22           C  
ANISOU  786  CA  ASP A  99     5684   5270   6606    130    525   -259       C  
ATOM    787  C   ASP A  99      25.526  -8.935   4.255  1.00 52.55           C  
ANISOU  787  C   ASP A  99     6474   6117   7376    151    419   -272       C  
ATOM    788  O   ASP A  99      26.365  -9.837   4.131  1.00 56.45           O  
ANISOU  788  O   ASP A  99     7002   6582   7865    130    399   -262       O  
ATOM    789  CB  ASP A  99      25.202  -8.292   6.656  1.00 50.08           C  
ANISOU  789  CB  ASP A  99     6302   5717   7010    151    554   -187       C  
ATOM    790  CG  ASP A  99      24.209  -8.052   7.808  1.00 66.41           C  
ANISOU  790  CG  ASP A  99     8392   7747   9095    150    658   -168       C  
ATOM    791  OD1 ASP A  99      23.090  -7.557   7.538  1.00 67.41           O  
ANISOU  791  OD1 ASP A  99     8436   7911   9265    161    682   -200       O  
ATOM    792  OD2 ASP A  99      24.557  -8.348   8.984  1.00 65.82           O  
ANISOU  792  OD2 ASP A  99     8418   7606   8983    148    718   -119       O  
ATOM    793  N   ILE A 100      25.407  -7.952   3.374  1.00 43.61           N  
ANISOU  793  N   ILE A 100     5297   5053   6219    200    357   -291       N  
ATOM    794  CA  ILE A 100      26.280  -7.893   2.216  1.00 34.37           C  
ANISOU  794  CA  ILE A 100     4116   3925   5017    230    266   -299       C  
ATOM    795  C   ILE A 100      26.641  -6.460   1.929  1.00 37.32           C  
ANISOU  795  C   ILE A 100     4523   4337   5321    289    228   -270       C  
ATOM    796  O   ILE A 100      25.756  -5.638   1.690  1.00 35.78           O  
ANISOU  796  O   ILE A 100     4284   4182   5128    328    238   -291       O  
ATOM    797  CB  ILE A 100      25.606  -8.435   0.949  1.00 40.50           C  
ANISOU  797  CB  ILE A 100     4776   4756   5856    239    224   -377       C  
ATOM    798  CG1 ILE A 100      24.666  -9.582   1.281  1.00 48.43           C  
ANISOU  798  CG1 ILE A 100     5718   5726   6956    176    286   -427       C  
ATOM    799  CG2 ILE A 100      26.656  -8.880  -0.050  1.00 40.07           C  
ANISOU  799  CG2 ILE A 100     4731   4718   5776    258    146   -378       C  
ATOM    800  CD1 ILE A 100      24.194 -10.336   0.053  1.00 52.02           C  
ANISOU  800  CD1 ILE A 100     6065   6226   7476    172    234   -514       C  
ATOM    801  N   ALA A 101      27.940  -6.167   1.934  1.00 37.35           N  
ANISOU  801  N   ALA A 101     4601   4329   5263    296    188   -223       N  
ATOM    802  CA  ALA A 101      28.430  -4.832   1.644  1.00 39.33           C  
ANISOU  802  CA  ALA A 101     4890   4601   5452    342    159   -194       C  
ATOM    803  C   ALA A 101      29.601  -4.842   0.653  1.00 33.20           C  
ANISOU  803  C   ALA A 101     4120   3849   4647    364     91   -181       C  
ATOM    804  O   ALA A 101      30.377  -5.788   0.606  1.00 28.01           O  
ANISOU  804  O   ALA A 101     3472   3176   3993    336     68   -172       O  
ATOM    805  CB  ALA A 101      28.813  -4.115   2.947  1.00 36.74           C  
ANISOU  805  CB  ALA A 101     4661   4225   5074    324    197   -146       C  
ATOM    806  N   THR A 102      29.694  -3.779  -0.145  1.00 31.22           N  
ANISOU  806  N   THR A 102     3866   3632   4364    420     67   -176       N  
ATOM    807  CA  THR A 102      30.782  -3.547  -1.100  1.00 28.34           C  
ANISOU  807  CA  THR A 102     3513   3287   3969    451     16   -154       C  
ATOM    808  C   THR A 102      32.041  -3.082  -0.369  1.00 27.96           C  
ANISOU  808  C   THR A 102     3546   3199   3878    415     16   -101       C  
ATOM    809  O   THR A 102      31.970  -2.218   0.498  1.00 24.64           O  
ANISOU  809  O   THR A 102     3181   2748   3432    400     49    -83       O  
ATOM    810  CB  THR A 102      30.377  -2.412  -2.084  1.00 36.06           C  
ANISOU  810  CB  THR A 102     4474   4305   4921    533     11   -161       C  
ATOM    811  OG1 THR A 102      29.163  -2.767  -2.760  1.00 40.37           O  
ANISOU  811  OG1 THR A 102     4935   4902   5500    577      3   -219       O  
ATOM    812  CG2 THR A 102      31.475  -2.131  -3.111  1.00 25.68           C  
ANISOU  812  CG2 THR A 102     3176   3006   3577    573    -27   -133       C  
ATOM    813  N   ALA A 103      33.202  -3.627  -0.708  1.00 28.84           N  
ANISOU  813  N   ALA A 103     3665   3313   3980    403    -23    -80       N  
ATOM    814  CA  ALA A 103      34.447  -3.158  -0.068  1.00 28.12           C  
ANISOU  814  CA  ALA A 103     3637   3196   3853    369    -30    -39       C  
ATOM    815  C   ALA A 103      34.642  -1.657  -0.257  1.00 34.34           C  
ANISOU  815  C   ALA A 103     4458   3975   4614    389    -15    -21       C  
ATOM    816  O   ALA A 103      34.531  -1.158  -1.401  1.00 33.56           O  
ANISOU  816  O   ALA A 103     4335   3902   4514    445    -20    -21       O  
ATOM    817  CB  ALA A 103      35.658  -3.920  -0.604  1.00 18.68           C  
ANISOU  817  CB  ALA A 103     2429   2018   2652    366    -76    -19       C  
ATOM    818  N   ARG A 104      34.925  -0.928   0.832  1.00 21.90           N  
ANISOU  818  N   ARG A 104     2946   2362   3014    350      6     -7       N  
ATOM    819  CA  ARG A 104      35.030   0.541   0.724  1.00 30.79           C  
ANISOU  819  CA  ARG A 104     4114   3466   4117    363     32      5       C  
ATOM    820  C   ARG A 104      36.227   1.144   1.443  1.00 29.41           C  
ANISOU  820  C   ARG A 104     3995   3260   3921    308     22     22       C  
ATOM    821  O   ARG A 104      36.735   0.565   2.397  1.00 32.18           O  
ANISOU  821  O   ARG A 104     4362   3603   4261    264      1     20       O  
ATOM    822  CB  ARG A 104      33.746   1.230   1.182  1.00 32.21           C  
ANISOU  822  CB  ARG A 104     4319   3631   4289    388     80    -10       C  
ATOM    823  CG  ARG A 104      33.498   1.128   2.689  1.00 44.54           C  
ANISOU  823  CG  ARG A 104     5931   5156   5836    342    101    -13       C  
ATOM    824  CD  ARG A 104      32.012   1.131   3.011  1.00 48.38           C  
ANISOU  824  CD  ARG A 104     6404   5645   6332    373    147    -31       C  
ATOM    825  NE  ARG A 104      31.301   0.111   2.247  1.00 55.58           N  
ANISOU  825  NE  ARG A 104     7229   6601   7288    397    136    -56       N  
ATOM    826  CZ  ARG A 104      29.983   0.091   2.076  1.00 60.51           C  
ANISOU  826  CZ  ARG A 104     7807   7249   7934    434    167    -81       C  
ATOM    827  NH1 ARG A 104      29.226   1.041   2.614  1.00 56.59           N  
ANISOU  827  NH1 ARG A 104     7349   6737   7415    458    215    -77       N  
ATOM    828  NH2 ARG A 104      29.419  -0.874   1.359  1.00 61.32           N  
ANISOU  828  NH2 ARG A 104     7824   7393   8082    448    150   -114       N  
ATOM    829  N   LEU A 105      36.698   2.292   0.956  1.00 32.15           N  
ANISOU  829  N   LEU A 105     4367   3587   4261    315     40     36       N  
ATOM    830  CA  LEU A 105      37.719   3.034   1.685  1.00 27.81           C  
ANISOU  830  CA  LEU A 105     3866   3001   3698    254     36     39       C  
ATOM    831  C   LEU A 105      37.081   4.200   2.417  1.00 33.92           C  
ANISOU  831  C   LEU A 105     4714   3725   4449    248     82     28       C  
ATOM    832  O   LEU A 105      35.930   4.593   2.129  1.00 26.93           O  
ANISOU  832  O   LEU A 105     3839   2836   3557    303    124     27       O  
ATOM    833  CB  LEU A 105      38.862   3.538   0.790  1.00 33.04           C  
ANISOU  833  CB  LEU A 105     4513   3664   4378    245     32     59       C  
ATOM    834  CG  LEU A 105      38.709   4.527  -0.384  1.00 36.89           C  
ANISOU  834  CG  LEU A 105     5011   4134   4873    297     82     80       C  
ATOM    835  CD1 LEU A 105      38.012   3.835  -1.515  1.00 44.31           C  
ANISOU  835  CD1 LEU A 105     5899   5121   5816    381     76     87       C  
ATOM    836  CD2 LEU A 105      38.003   5.877  -0.046  1.00 29.47           C  
ANISOU  836  CD2 LEU A 105     4147   3137   3912    309    144     74       C  
ATOM    837  N   GLU A 106      37.831   4.747   3.367  1.00 28.91           N  
ANISOU  837  N   GLU A 106     4129   3055   3799    187     73     16       N  
ATOM    838  CA  GLU A 106      37.412   5.966   4.054  1.00 30.41           C  
ANISOU  838  CA  GLU A 106     4402   3187   3964    177    116      4       C  
ATOM    839  C   GLU A 106      38.555   6.924   3.992  1.00 29.14           C  
ANISOU  839  C   GLU A 106     4269   2988   3814    121    117     -3       C  
ATOM    840  O   GLU A 106      39.686   6.579   4.343  1.00 32.96           O  
ANISOU  840  O   GLU A 106     4728   3488   4308     63     67    -16       O  
ATOM    841  CB  GLU A 106      37.065   5.686   5.525  1.00 23.02           C  
ANISOU  841  CB  GLU A 106     3514   2238   2995    155    104    -17       C  
ATOM    842  CG  GLU A 106      35.778   4.906   5.733  1.00 22.04           C  
ANISOU  842  CG  GLU A 106     3373   2136   2866    205    125    -12       C  
ATOM    843  CD  GLU A 106      35.663   4.381   7.166  1.00 40.10           C  
ANISOU  843  CD  GLU A 106     5703   4412   5121    186    114    -24       C  
ATOM    844  OE1 GLU A 106      36.531   4.726   8.008  1.00 46.38           O  
ANISOU  844  OE1 GLU A 106     6547   5187   5889    143     84    -42       O  
ATOM    845  OE2 GLU A 106      34.720   3.610   7.443  1.00 37.53           O  
ANISOU  845  OE2 GLU A 106     5361   4099   4799    217    137    -19       O  
ATOM    846  N   TYR A 107      38.271   8.135   3.541  1.00 33.20           N  
ANISOU  846  N   TYR A 107     4834   3452   4328    140    178      5       N  
ATOM    847  CA  TYR A 107      39.277   9.167   3.551  1.00 28.11           C  
ANISOU  847  CA  TYR A 107     4226   2753   3701     77    196     -6       C  
ATOM    848  C   TYR A 107      38.747  10.254   4.453  1.00 31.79           C  
ANISOU  848  C   TYR A 107     4794   3150   4134     64    237    -29       C  
ATOM    849  O   TYR A 107      37.573  10.626   4.329  1.00 28.10           O  
ANISOU  849  O   TYR A 107     4369   2668   3638    134    288    -14       O  
ATOM    850  CB  TYR A 107      39.501   9.717   2.147  1.00 34.43           C  
ANISOU  850  CB  TYR A 107     5012   3540   4531    113    250     28       C  
ATOM    851  CG  TYR A 107      40.400  10.940   2.143  1.00 32.26           C  
ANISOU  851  CG  TYR A 107     4787   3190   4282     47    294     18       C  
ATOM    852  CD1 TYR A 107      41.787  10.807   2.065  1.00 26.70           C  
ANISOU  852  CD1 TYR A 107     4030   2493   3623    -32    262      7       C  
ATOM    853  CD2 TYR A 107      39.872  12.214   2.256  1.00 32.22           C  
ANISOU  853  CD2 TYR A 107     4879   3104   4258     60    371     16       C  
ATOM    854  CE1 TYR A 107      42.621  11.906   2.054  1.00 19.73           C  
ANISOU  854  CE1 TYR A 107     3181   1538   2777   -105    307     -9       C  
ATOM    855  CE2 TYR A 107      40.704  13.333   2.276  1.00 30.34           C  
ANISOU  855  CE2 TYR A 107     4691   2784   4051    -11    419      1       C  
ATOM    856  CZ  TYR A 107      42.074  13.164   2.165  1.00 32.94           C  
ANISOU  856  CZ  TYR A 107     4957   3121   4436    -98    387    -13       C  
ATOM    857  OH  TYR A 107      42.912  14.251   2.180  1.00 40.48           O  
ANISOU  857  OH  TYR A 107     5952   3995   5435   -179    439    -34       O  
ATOM    858  N   TYR A 108      39.599  10.745   5.358  1.00 31.84           N  
ANISOU  858  N   TYR A 108     4839   3119   4141    -20    212    -69       N  
ATOM    859  CA  TYR A 108      39.210  11.767   6.340  1.00 33.75           C  
ANISOU  859  CA  TYR A 108     5187   3290   4347    -39    243   -100       C  
ATOM    860  C   TYR A 108      39.704  13.169   6.021  1.00 30.33           C  
ANISOU  860  C   TYR A 108     4817   2769   3937    -83    305   -112       C  
ATOM    861  O   TYR A 108      40.891  13.451   6.113  1.00 38.43           O  
ANISOU  861  O   TYR A 108     5822   3776   5002   -171    281   -143       O  
ATOM    862  CB  TYR A 108      39.721  11.391   7.729  1.00 35.61           C  
ANISOU  862  CB  TYR A 108     5437   3538   4556    -95    170   -149       C  
ATOM    863  CG  TYR A 108      38.932  10.282   8.330  1.00 33.52           C  
ANISOU  863  CG  TYR A 108     5157   3327   4253    -41    139   -137       C  
ATOM    864  CD1 TYR A 108      39.299   8.961   8.117  1.00 31.01           C  
ANISOU  864  CD1 TYR A 108     4749   3084   3949    -34     85   -123       C  
ATOM    865  CD2 TYR A 108      37.789  10.539   9.074  1.00 27.56           C  
ANISOU  865  CD2 TYR A 108     4478   2544   3449      8    175   -135       C  
ATOM    866  CE1 TYR A 108      38.565   7.940   8.613  1.00 23.47           C  
ANISOU  866  CE1 TYR A 108     3784   2167   2967     13     72   -110       C  
ATOM    867  CE2 TYR A 108      37.042   9.499   9.597  1.00 24.74           C  
ANISOU  867  CE2 TYR A 108     4103   2231   3066     56    162   -120       C  
ATOM    868  CZ  TYR A 108      37.439   8.193   9.365  1.00 32.23           C  
ANISOU  868  CZ  TYR A 108     4964   3246   4035     55    112   -108       C  
ATOM    869  OH  TYR A 108      36.728   7.115   9.898  1.00 38.84           O  
ANISOU  869  OH  TYR A 108     5788   4117   4853     98    109    -94       O  
ATOM    870  N   GLU A 109      38.786  14.054   5.668  1.00 39.92           N  
ANISOU  870  N   GLU A 109     6110   3929   5128    -22    389    -88       N  
ATOM    871  CA  GLU A 109      39.149  15.442   5.387  1.00 45.21           C  
ANISOU  871  CA  GLU A 109     6861   4500   5815    -56    466    -95       C  
ATOM    872  C   GLU A 109      39.381  16.160   6.727  1.00 35.93           C  
ANISOU  872  C   GLU A 109     5776   3260   4617   -129    451   -157       C  
ATOM    873  O   GLU A 109      40.328  16.915   6.866  1.00 39.63           O  
ANISOU  873  O   GLU A 109     6270   3665   5123   -221    462   -196       O  
ATOM    874  CB  GLU A 109      38.059  16.138   4.553  1.00 45.77           C  
ANISOU  874  CB  GLU A 109     6996   4539   5857     52    566    -46       C  
ATOM    875  CG  GLU A 109      36.968  15.176   4.008  1.00122.26           C  
ANISOU  875  CG  GLU A 109    16619  14319  15517    165    551     -6       C  
ATOM    876  CD  GLU A 109      35.954  14.708   5.075  1.00117.81           C  
ANISOU  876  CD  GLU A 109    16072  13786  14903    197    518    -20       C  
ATOM    877  OE1 GLU A 109      34.750  15.023   4.938  1.00116.71           O  
ANISOU  877  OE1 GLU A 109    15974  13650  14722    290    570      2       O  
ATOM    878  OE2 GLU A 109      36.350  14.022   6.045  1.00112.58           O  
ANISOU  878  OE2 GLU A 109    15384  13150  14241    136    446    -52       O  
ATOM    879  N   SER A 110      38.565  15.824   7.711  1.00 32.26           N  
ANISOU  879  N   SER A 110     5355   2812   4092    -89    426   -167       N  
ATOM    880  CA  SER A 110      38.604  16.365   9.065  1.00 42.96           C  
ANISOU  880  CA  SER A 110     6794   4120   5410   -142    395   -228       C  
ATOM    881  C   SER A 110      38.417  15.270  10.098  1.00 28.01           C  
ANISOU  881  C   SER A 110     4865   2300   3476   -126    310   -243       C  
ATOM    882  O   SER A 110      38.083  14.187   9.739  1.00 39.79           O  
ANISOU  882  O   SER A 110     6280   3870   4970    -71    290   -203       O  
ATOM    883  CB  SER A 110      37.510  17.401   9.238  1.00 43.21           C  
ANISOU  883  CB  SER A 110     6961   4069   5387    -86    480   -219       C  
ATOM    884  OG  SER A 110      37.793  18.534   8.467  1.00 54.81           O  
ANISOU  884  OG  SER A 110     8478   5461   6886    -87    572   -199       O  
ATOM    885  N   PRO A 111      38.537  15.571  11.384  1.00 39.09           N  
ANISOU  885  N   PRO A 111     6330   3680   4844   -171    261   -303       N  
ATOM    886  CA  PRO A 111      38.289  14.514  12.369  1.00 33.92           C  
ANISOU  886  CA  PRO A 111     5685   3074   4129   -134    202   -314       C  
ATOM    887  C   PRO A 111      36.787  14.379  12.632  1.00 58.92           C  
ANISOU  887  C   PRO A 111     8883   6258   7247    -24    253   -259       C  
ATOM    888  O   PRO A 111      36.334  14.555  13.763  1.00 54.47           O  
ANISOU  888  O   PRO A 111     8362   5706   6627     10    230   -269       O  
ATOM    889  CB  PRO A 111      39.000  15.032  13.619  1.00 41.98           C  
ANISOU  889  CB  PRO A 111     6801   4036   5114   -190    169   -391       C  
ATOM    890  CG  PRO A 111      40.091  15.895  13.094  1.00 38.62           C  
ANISOU  890  CG  PRO A 111     6327   3585   4763   -300    150   -436       C  
ATOM    891  CD  PRO A 111      39.543  16.540  11.853  1.00 41.66           C  
ANISOU  891  CD  PRO A 111     6687   3944   5199   -278    240   -373       C  
ATOM    892  N   ALA A 112      36.033  14.064  11.580  1.00 60.23           N  
ANISOU  892  N   ALA A 112     9015   6433   7437     32    318   -203       N  
ATOM    893  CA  ALA A 112      34.584  13.875  11.670  1.00 44.12           C  
ANISOU  893  CA  ALA A 112     6981   4417   5367    132    373   -155       C  
ATOM    894  C   ALA A 112      34.115  12.648  10.883  1.00 47.62           C  
ANISOU  894  C   ALA A 112     7299   4945   5851    173    365   -112       C  
ATOM    895  O   ALA A 112      34.592  11.534  11.099  1.00 51.27           O  
ANISOU  895  O   ALA A 112     7675   5460   6346    135    302   -117       O  
ATOM    896  CB  ALA A 112      33.856  15.124  11.194  1.00 55.67           C  
ANISOU  896  CB  ALA A 112     8525   5815   6812    180    464   -134       C  
ATOM    897  N   LYS A 113      33.179  12.875   9.962  1.00 31.74           N  
ANISOU  897  N   LYS A 113     5278   2948   3834    255    428    -74       N  
ATOM    898  CA  LYS A 113      32.644  11.815   9.077  1.00 38.37           C  
ANISOU  898  CA  LYS A 113     6001   3867   4710    300    421    -43       C  
ATOM    899  C   LYS A 113      33.345  11.747   7.679  1.00 45.78           C  
ANISOU  899  C   LYS A 113     6866   4830   5700    287    409    -32       C  
ATOM    900  O   LYS A 113      33.340  12.710   6.903  1.00 40.44           O  
ANISOU  900  O   LYS A 113     6224   4117   5023    311    459    -19       O  
ATOM    901  CB  LYS A 113      31.129  11.999   8.903  1.00 38.57           C  
ANISOU  901  CB  LYS A 113     6033   3908   4712    397    488    -16       C  
ATOM    902  CG  LYS A 113      30.313  10.753   9.065  1.00 49.35           C  
ANISOU  902  CG  LYS A 113     7314   5341   6095    428    477     -6       C  
ATOM    903  CD  LYS A 113      30.077  10.400  10.534  1.00 52.22           C  
ANISOU  903  CD  LYS A 113     7733   5685   6425    417    476    -13       C  
ATOM    904  CE  LYS A 113      28.612  10.641  10.930  1.00 68.94           C  
ANISOU  904  CE  LYS A 113     9876   7805   8514    496    547      7       C  
ATOM    905  NZ  LYS A 113      28.368  11.055  12.376  1.00 70.21           N  
ANISOU  905  NZ  LYS A 113    10152   7911   8615    505    573      4       N  
ATOM    906  N   LEU A 114      33.913  10.585   7.372  1.00 40.11           N  
ANISOU  906  N   LEU A 114     6052   4170   5019    257    349    -32       N  
ATOM    907  CA  LEU A 114      34.779  10.330   6.199  1.00 42.57           C  
ANISOU  907  CA  LEU A 114     6290   4508   5376    238    325    -22       C  
ATOM    908  C   LEU A 114      34.071  10.238   4.826  1.00 33.29           C  
ANISOU  908  C   LEU A 114     5059   3373   4218    320    358      7       C  
ATOM    909  O   LEU A 114      32.883   9.891   4.759  1.00 26.00           O  
ANISOU  909  O   LEU A 114     4111   2486   3282    387    378     15       O  
ATOM    910  CB  LEU A 114      35.516   9.020   6.454  1.00 36.08           C  
ANISOU  910  CB  LEU A 114     5392   3738   4577    192    249    -32       C  
ATOM    911  CG  LEU A 114      34.632   8.125   7.339  1.00 41.78           C  
ANISOU  911  CG  LEU A 114     6109   4487   5277    219    243    -33       C  
ATOM    912  CD1 LEU A 114      34.446   8.676   8.750  1.00 49.87           C  
ANISOU  912  CD1 LEU A 114     7233   5462   6253    204    254    -53       C  
ATOM    913  CD2 LEU A 114      33.261   7.908   6.737  1.00 51.97           C  
ANISOU  913  CD2 LEU A 114     7363   5809   6575    297    288    -14       C  
ATOM    914  N   PRO A 115      34.769  10.628   3.740  1.00 43.14           N  
ANISOU  914  N   PRO A 115     6289   4612   5489    321    370     22       N  
ATOM    915  CA  PRO A 115      34.301  10.149   2.429  1.00 35.16           C  
ANISOU  915  CA  PRO A 115     5204   3661   4494    401    375     45       C  
ATOM    916  C   PRO A 115      34.539   8.667   2.119  1.00 33.00           C  
ANISOU  916  C   PRO A 115     4826   3461   4253    390    307     41       C  
ATOM    917  O   PRO A 115      35.564   8.032   2.415  1.00 30.35           O  
ANISOU  917  O   PRO A 115     4459   3133   3939    320    255     34       O  
ATOM    918  CB  PRO A 115      35.008  11.091   1.434  1.00 39.59           C  
ANISOU  918  CB  PRO A 115     5797   4180   5065    412    421     67       C  
ATOM    919  CG  PRO A 115      34.962  12.449   2.171  1.00 30.50           C  
ANISOU  919  CG  PRO A 115     4765   2938   3885    388    482     59       C  
ATOM    920  CD  PRO A 115      35.329  11.998   3.630  1.00 68.05           C  
ANISOU  920  CD  PRO A 115     9529   7686   8639    296    424     23       C  
ATOM    921  N   ASP A 116      33.511   8.096   1.520  1.00 38.52           N  
ANISOU  921  N   ASP A 116     5468   4216   4952    465    308     42       N  
ATOM    922  CA  ASP A 116      33.538   6.701   1.156  1.00 34.58           C  
ANISOU  922  CA  ASP A 116     4874   3780   4483    463    252     34       C  
ATOM    923  C   ASP A 116      33.417   6.594  -0.354  1.00 36.78           C  
ANISOU  923  C   ASP A 116     5100   4104   4771    542    251     45       C  
ATOM    924  O   ASP A 116      32.628   7.311  -0.976  1.00 37.38           O  
ANISOU  924  O   ASP A 116     5193   4187   4822    627    294     50       O  
ATOM    925  CB  ASP A 116      32.368   5.987   1.813  1.00 37.14           C  
ANISOU  925  CB  ASP A 116     5169   4134   4809    478    251     15       C  
ATOM    926  CG  ASP A 116      32.471   4.501   1.700  1.00 72.10           C  
ANISOU  926  CG  ASP A 116     9515   8608   9271    455    200      2       C  
ATOM    927  OD1 ASP A 116      32.704   4.001   0.576  1.00 91.44           O  
ANISOU  927  OD1 ASP A 116    11904  11099  11741    486    172      3       O  
ATOM    928  OD2 ASP A 116      32.316   3.823   2.736  1.00 82.44           O  
ANISOU  928  OD2 ASP A 116    10829   9910  10586    412    193     -7       O  
ATOM    929  N   VAL A 117      34.205   5.714  -0.901  1.00 25.84           N  
ANISOU  929  N   VAL A 117     3657   2748   3412    523    204     50       N  
ATOM    930  CA  VAL A 117      34.011   5.264  -2.220  1.00 31.08           C  
ANISOU  930  CA  VAL A 117     4258   3468   4084    601    186     50       C  
ATOM    931  C   VAL A 117      34.213   3.785  -2.156  1.00 36.10           C  
ANISOU  931  C   VAL A 117     4823   4142   4750    558    122     36       C  
ATOM    932  O   VAL A 117      34.930   3.272  -1.361  1.00 31.18           O  
ANISOU  932  O   VAL A 117     4211   3498   4137    477     99     39       O  
ATOM    933  CB  VAL A 117      34.827   5.994  -3.314  1.00 51.45           C  
ANISOU  933  CB  VAL A 117     6863   6032   6655    647    214     84       C  
ATOM    934  CG1 VAL A 117      34.098   7.255  -3.830  1.00 14.35           C  
ANISOU  934  CG1 VAL A 117     2232   1304   1915    735    291     99       C  
ATOM    935  CG2 VAL A 117      36.190   6.263  -2.869  1.00 46.12           C  
ANISOU  935  CG2 VAL A 117     6212   5313   6000    556    209    104       C  
ATOM    936  N   GLU A 118      33.516   3.106  -3.028  1.00 42.83           N  
ANISOU  936  N   GLU A 118     5608   5051   5614    618     95     15       N  
ATOM    937  CA  GLU A 118      33.496   1.679  -3.051  1.00 45.64           C  
ANISOU  937  CA  GLU A 118     5904   5439   6000    585     43     -3       C  
ATOM    938  C   GLU A 118      34.837   1.330  -3.522  1.00 30.58           C  
ANISOU  938  C   GLU A 118     3996   3528   4095    566     16     28       C  
ATOM    939  O   GLU A 118      35.238   0.231  -3.381  1.00 31.07           O  
ANISOU  939  O   GLU A 118     4033   3600   4173    522    -23     28       O  
ATOM    940  CB  GLU A 118      32.449   1.130  -4.019  1.00 53.01           C  
ANISOU  940  CB  GLU A 118     6763   6431   6946    656     20    -42       C  
ATOM    941  CG  GLU A 118      32.926   0.871  -5.431  1.00 59.33           C  
ANISOU  941  CG  GLU A 118     7545   7269   7728    753      7    -35       C  
ATOM    942  CD  GLU A 118      31.882   0.204  -6.322  1.00 73.65           C  
ANISOU  942  CD  GLU A 118     9278   9150   9557    817    -35    -88       C  
ATOM    943  OE1 GLU A 118      30.875   0.825  -6.634  1.00 80.53           O  
ANISOU  943  OE1 GLU A 118    10111  10039  10448    805    -81   -100       O  
ATOM    944  OE2 GLU A 118      32.064  -0.938  -6.747  1.00 71.54           O  
ANISOU  944  OE2 GLU A 118     8984   8918   9280    882    -23   -123       O  
ATOM    945  N   MET A 119      35.537   2.326  -3.990  1.00 28.44           N  
ANISOU  945  N   MET A 119     3760   3238   3807    600     46     59       N  
ATOM    946  CA  MET A 119      36.628   2.189  -4.856  1.00 63.45           C  
ANISOU  946  CA  MET A 119     8183   7682   8245    620     34     91       C  
ATOM    947  C   MET A 119      37.643   1.799  -3.883  1.00 85.39           C  
ANISOU  947  C   MET A 119    10943  10461  11042    537     -9     97       C  
ATOM    948  O   MET A 119      38.534   2.542  -3.512  1.00107.40           O  
ANISOU  948  O   MET A 119    13706  13265  13835    543    -31    122       O  
ATOM    949  CB  MET A 119      37.060   3.537  -5.457  1.00 55.78           C  
ANISOU  949  CB  MET A 119     7268   6665   7262    635     93    127       C  
ATOM    950  CG  MET A 119      36.286   3.981  -6.679  1.00 45.72           C  
ANISOU  950  CG  MET A 119     6011   5402   5959    756    135    136       C  
ATOM    951  SD  MET A 119      34.494   4.150  -6.430  1.00138.38           S  
ANISOU  951  SD  MET A 119    17694  17208  17675    855    104     86       S  
ATOM    952  CE  MET A 119      33.985   3.919  -8.116  1.00 51.94           C  
ANISOU  952  CE  MET A 119     6782   6235   6717    827    141     61       C  
ATOM    953  N   SER A 120      37.473   0.575  -3.456  1.00 59.79           N  
ANISOU  953  N   SER A 120     7715   7202   7802    471    -17     77       N  
ATOM    954  CA  SER A 120      38.354  -0.034  -2.600  1.00 54.30           C  
ANISOU  954  CA  SER A 120     7010   6511   7112    406    -55     78       C  
ATOM    955  C   SER A 120      38.379  -1.483  -2.891  1.00 44.74           C  
ANISOU  955  C   SER A 120     5749   5340   5912    428    -97     70       C  
ATOM    956  O   SER A 120      37.413  -2.118  -3.200  1.00 36.46           O  
ANISOU  956  O   SER A 120     4670   4309   4873    465   -101     42       O  
ATOM    957  CB  SER A 120      37.910   0.200  -1.190  1.00 57.35           C  
ANISOU  957  CB  SER A 120     7434   6867   7489    352    -44     58       C  
ATOM    958  OG  SER A 120      38.993  -0.028  -0.358  1.00 73.14           O  
ANISOU  958  OG  SER A 120     9441   8867   9480    295    -77     63       O  
ATOM    959  N   THR A 121      39.567  -1.975  -2.695  1.00 46.85           N  
ANISOU  959  N   THR A 121     6005   5618   6176    400   -127     92       N  
ATOM    960  CA  THR A 121      39.899  -3.351  -2.630  1.00 42.69           C  
ANISOU  960  CA  THR A 121     5456   5115   5651    396   -163     88       C  
ATOM    961  C   THR A 121      39.603  -3.736  -1.206  1.00 37.85           C  
ANISOU  961  C   THR A 121     4874   4478   5029    342   -158     71       C  
ATOM    962  O   THR A 121      39.294  -2.915  -0.406  1.00 27.08           O  
ANISOU  962  O   THR A 121     3546   3085   3657    313   -133     63       O  
ATOM    963  CB  THR A 121      41.360  -3.482  -2.868  1.00 41.80           C  
ANISOU  963  CB  THR A 121     5331   5022   5528    386   -190    123       C  
ATOM    964  OG1 THR A 121      42.036  -2.552  -2.038  1.00 35.06           O  
ANISOU  964  OG1 THR A 121     4505   4150   4668    327   -182    130       O  
ATOM    965  CG2 THR A 121      41.649  -3.152  -4.270  1.00 37.56           C  
ANISOU  965  CG2 THR A 121     4769   4504   4999    447   -185    148       C  
ATOM    966  N   ILE A 122      39.711  -5.000  -0.907  1.00 28.27           N  
ANISOU  966  N   ILE A 122     3656   3273   3812    336   -178     69       N  
ATOM    967  CA  ILE A 122      39.449  -5.466   0.432  1.00 32.98           C  
ANISOU  967  CA  ILE A 122     4291   3845   4394    299   -164     60       C  
ATOM    968  C   ILE A 122      40.507  -4.876   1.376  1.00 36.97           C  
ANISOU  968  C   ILE A 122     4832   4349   4865    263   -179     75       C  
ATOM    969  O   ILE A 122      40.241  -4.626   2.545  1.00 33.00           O  
ANISOU  969  O   ILE A 122     4375   3822   4343    237   -163     65       O  
ATOM    970  CB  ILE A 122      39.482  -6.988   0.495  1.00 33.45           C  
ANISOU  970  CB  ILE A 122     4347   3907   4454    308   -171     59       C  
ATOM    971  CG1 ILE A 122      39.149  -7.471   1.912  1.00 38.58           C  
ANISOU  971  CG1 ILE A 122     5049   4524   5087    281   -142     54       C  
ATOM    972  CG2 ILE A 122      40.849  -7.505  -0.007  1.00 29.01           C  
ANISOU  972  CG2 ILE A 122     3772   3381   3870    326   -214     90       C  
ATOM    973  CD1 ILE A 122      37.713  -7.135   2.364  1.00 36.20           C  
ANISOU  973  CD1 ILE A 122     4755   4186   4813    268    -91     27       C  
ATOM    974  N   LYS A 123      41.700  -4.627   0.856  1.00 30.08           N  
ANISOU  974  N   LYS A 123     3936   3507   3987    263   -211     97       N  
ATOM    975  CA  LYS A 123      42.738  -4.109   1.701  1.00 29.19           C  
ANISOU  975  CA  LYS A 123     3840   3401   3848    224   -233    100       C  
ATOM    976  C   LYS A 123      42.298  -2.816   2.379  1.00 39.73           C  
ANISOU  976  C   LYS A 123     5215   4699   5183    189   -208     79       C  
ATOM    977  O   LYS A 123      42.292  -2.718   3.625  1.00 30.38           O  
ANISOU  977  O   LYS A 123     4076   3500   3968    165   -211     63       O  
ATOM    978  CB  LYS A 123      44.041  -3.880   0.948  1.00 20.66           C  
ANISOU  978  CB  LYS A 123     2715   2358   2775    224   -261    123       C  
ATOM    979  CG  LYS A 123      45.121  -3.420   1.928  1.00 28.92           C  
ANISOU  979  CG  LYS A 123     3769   3422   3799    177   -292    113       C  
ATOM    980  CD  LYS A 123      46.545  -3.683   1.482  1.00 20.48           C  
ANISOU  980  CD  LYS A 123     2645   2407   2729    179   -329    135       C  
ATOM    981  CE  LYS A 123      47.466  -3.155   2.562  1.00 28.44           C  
ANISOU  981  CE  LYS A 123     3654   3436   3717    129   -364    108       C  
ATOM    982  NZ  LYS A 123      48.853  -3.381   2.159  1.00 28.37           N  
ANISOU  982  NZ  LYS A 123     3580   3488   3713    128   -400    125       N  
ATOM    983  N   LYS A 124      41.903  -1.849   1.578  1.00 37.64           N  
ANISOU  983  N   LYS A 124     4940   4415   4945    196   -179     81       N  
ATOM    984  CA  LYS A 124      41.473  -0.560   2.041  1.00 34.97           C  
ANISOU  984  CA  LYS A 124     4647   4035   4604    168   -149     64       C  
ATOM    985  C   LYS A 124      40.266  -0.642   2.935  1.00 34.02           C  
ANISOU  985  C   LYS A 124     4571   3885   4470    176   -118     45       C  
ATOM    986  O   LYS A 124      40.123   0.121   3.845  1.00 32.22           O  
ANISOU  986  O   LYS A 124     4396   3623   4222    149   -103     29       O  
ATOM    987  CB  LYS A 124      41.186   0.333   0.863  1.00 30.16           C  
ANISOU  987  CB  LYS A 124     4030   3409   4022    185   -113     76       C  
ATOM    988  CG  LYS A 124      42.094   1.455   0.743  1.00 35.56           C  
ANISOU  988  CG  LYS A 124     4675   4112   4725    172   -127     99       C  
ATOM    989  CD  LYS A 124      43.095   1.251  -0.321  1.00 43.33           C  
ANISOU  989  CD  LYS A 124     5678   5054   5730    166    -76    108       C  
ATOM    990  CE  LYS A 124      43.976   2.450  -0.507  1.00 40.75           C  
ANISOU  990  CE  LYS A 124     5312   4740   5432    137    -81    128       C  
ATOM    991  NZ  LYS A 124      45.262   2.232   0.103  1.00 47.80           N  
ANISOU  991  NZ  LYS A 124     6182   5661   6317     72   -137    108       N  
ATOM    992  N   ASP A 125      39.380  -1.550   2.632  1.00 24.72           N  
ANISOU  992  N   ASP A 125     3371   2717   3304    211   -107     45       N  
ATOM    993  CA  ASP A 125      38.185  -1.730   3.451  1.00 30.37           C  
ANISOU  993  CA  ASP A 125     4119   3406   4015    216    -71     29       C  
ATOM    994  C   ASP A 125      38.534  -2.270   4.840  1.00 33.59           C  
ANISOU  994  C   ASP A 125     4575   3803   4386    192    -80     26       C  
ATOM    995  O   ASP A 125      37.779  -2.085   5.791  1.00 35.94           O  
ANISOU  995  O   ASP A 125     4920   4069   4668    191    -46     17       O  
ATOM    996  CB  ASP A 125      37.189  -2.672   2.791  1.00 37.52           C  
ANISOU  996  CB  ASP A 125     4979   4325   4953    249    -55     21       C  
ATOM    997  CG  ASP A 125      35.961  -2.916   3.655  1.00 41.49           C  
ANISOU  997  CG  ASP A 125     5504   4799   5460    248     -9      5       C  
ATOM    998  OD1 ASP A 125      35.068  -2.039   3.746  1.00 50.75           O  
ANISOU  998  OD1 ASP A 125     6689   5956   6636    260     27     -5       O  
ATOM    999  OD2 ASP A 125      35.887  -4.000   4.246  1.00 37.30           O  
ANISOU  999  OD2 ASP A 125     4982   4260   4930    239     -1      5       O  
ATOM   1000  N   LEU A 126      39.666  -2.955   4.950  1.00 25.73           N  
ANISOU 1000  N   LEU A 126     3569   2836   3372    185   -124     37       N  
ATOM   1001  CA  LEU A 126      40.092  -3.517   6.239  1.00 34.35           C  
ANISOU 1001  CA  LEU A 126     4710   3926   4416    180   -136     35       C  
ATOM   1002  C   LEU A 126      40.912  -2.453   6.981  1.00 32.49           C  
ANISOU 1002  C   LEU A 126     4509   3690   4147    149   -167     18       C  
ATOM   1003  O   LEU A 126      40.799  -2.274   8.196  1.00 31.24           O  
ANISOU 1003  O   LEU A 126     4412   3513   3946    148   -163      4       O  
ATOM   1004  CB  LEU A 126      40.957  -4.763   6.013  1.00 30.95           C  
ANISOU 1004  CB  LEU A 126     4254   3534   3973    199   -170     53       C  
ATOM   1005  CG  LEU A 126      40.426  -6.197   6.162  1.00 42.26           C  
ANISOU 1005  CG  LEU A 126     5698   4954   5405    228   -141     64       C  
ATOM   1006  CD1 LEU A 126      38.887  -6.363   5.990  1.00 25.32           C  
ANISOU 1006  CD1 LEU A 126     3549   2767   3305    230    -79     53       C  
ATOM   1007  CD2 LEU A 126      41.206  -7.145   5.265  1.00 26.15           C  
ANISOU 1007  CD2 LEU A 126     3614   2952   3371    248   -173     82       C  
ATOM   1008  N   TYR A 127      41.719  -1.737   6.205  1.00 24.21           N  
ANISOU 1008  N   TYR A 127     3418   2659   3120    124   -194     18       N  
ATOM   1009  CA  TYR A 127      42.615  -0.726   6.709  1.00 30.28           C  
ANISOU 1009  CA  TYR A 127     4202   3429   3874     81   -225     -6       C  
ATOM   1010  C   TYR A 127      41.891   0.399   7.421  1.00 31.73           C  
ANISOU 1010  C   TYR A 127     4452   3559   4046     64   -191    -30       C  
ATOM   1011  O   TYR A 127      42.524   1.147   8.154  1.00 24.76           O  
ANISOU 1011  O   TYR A 127     3599   2668   3140     27   -218    -61       O  
ATOM   1012  CB  TYR A 127      43.436  -0.125   5.576  1.00 30.75           C  
ANISOU 1012  CB  TYR A 127     4203   3505   3977     56   -236      3       C  
ATOM   1013  CG  TYR A 127      44.879   0.064   5.952  1.00 29.89           C  
ANISOU 1013  CG  TYR A 127     4066   3434   3857     17   -292    -16       C  
ATOM   1014  CD1 TYR A 127      45.244   0.519   7.226  1.00 24.90           C  
ANISOU 1014  CD1 TYR A 127     3477   2798   3186    -14   -323    -59       C  
ATOM   1015  CD2 TYR A 127      45.881  -0.189   5.032  1.00 25.32           C  
ANISOU 1015  CD2 TYR A 127     3414   2898   3307     12   -314      4       C  
ATOM   1016  CE1 TYR A 127      46.584   0.692   7.560  1.00 23.70           C  
ANISOU 1016  CE1 TYR A 127     3286   2692   3027    -51   -382    -88       C  
ATOM   1017  CE2 TYR A 127      47.214  -0.032   5.349  1.00 19.60           C  
ANISOU 1017  CE2 TYR A 127     2649   2218   2579    -25   -365    -17       C  
ATOM   1018  CZ  TYR A 127      47.564   0.401   6.607  1.00 29.48           C  
ANISOU 1018  CZ  TYR A 127     3934   3471   3795    -59   -402    -66       C  
ATOM   1019  OH  TYR A 127      48.901   0.563   6.878  1.00 33.98           O  
ANISOU 1019  OH  TYR A 127     4450   4095   4367    -97   -459    -96       O  
ATOM   1020  N   ARG A 128      40.584   0.535   7.178  1.00 24.02           N  
ANISOU 1020  N   ARG A 128     3494   2547   3084     90   -135    -19       N  
ATOM   1021  CA  ARG A 128      39.803   1.632   7.735  1.00 19.44           C  
ANISOU 1021  CA  ARG A 128     2979   1917   2492     85    -95    -35       C  
ATOM   1022  C   ARG A 128      39.103   1.228   9.029  1.00 27.43           C  
ANISOU 1022  C   ARG A 128     4055   2907   3459    108    -76    -42       C  
ATOM   1023  O   ARG A 128      38.428   2.048   9.641  1.00 40.52           O  
ANISOU 1023  O   ARG A 128     5775   4523   5097    111    -41    -53       O  
ATOM   1024  CB  ARG A 128      38.696   2.020   6.772  1.00 21.56           C  
ANISOU 1024  CB  ARG A 128     3229   2166   2795    115    -40    -20       C  
ATOM   1025  CG  ARG A 128      37.502   1.074   6.908  1.00 25.68           C  
ANISOU 1025  CG  ARG A 128     3743   2693   3322    156     -7    -10       C  
ATOM   1026  CD  ARG A 128      36.437   1.339   5.866  1.00 35.37           C  
ANISOU 1026  CD  ARG A 128     4933   3922   4585    193     35     -3       C  
ATOM   1027  NE  ARG A 128      35.605   0.166   5.613  1.00 41.97           N  
ANISOU 1027  NE  ARG A 128     5722   4778   5447    220     49     -1       N  
ATOM   1028  CZ  ARG A 128      34.555  -0.193   6.346  1.00 34.77           C  
ANISOU 1028  CZ  ARG A 128     4828   3848   4534    233     92     -5       C  
ATOM   1029  NH1 ARG A 128      33.849  -1.262   6.016  1.00 33.20           N  
ANISOU 1029  NH1 ARG A 128     4577   3665   4372    247    109    -10       N  
ATOM   1030  NH2 ARG A 128      34.199   0.525   7.394  1.00 38.26           N  
ANISOU 1030  NH2 ARG A 128     5342   4254   4942    232    123     -8       N  
ATOM   1031  N   ARG A 129      39.230  -0.039   9.420  1.00 29.78           N  
ANISOU 1031  N   ARG A 129     4345   3231   3739    130    -90    -30       N  
ATOM   1032  CA  ARG A 129      38.572  -0.539  10.623  1.00 37.81           C  
ANISOU 1032  CA  ARG A 129     5428   4225   4714    161    -58    -29       C  
ATOM   1033  C   ARG A 129      39.404  -0.273  11.888  1.00 41.22           C  
ANISOU 1033  C   ARG A 129     5926   4660   5077    159   -102    -54       C  
ATOM   1034  O   ARG A 129      40.575   0.104  11.807  1.00 36.36           O  
ANISOU 1034  O   ARG A 129     5288   4075   4452    128   -165    -78       O  
ATOM   1035  CB  ARG A 129      38.254  -2.015  10.465  1.00 41.56           C  
ANISOU 1035  CB  ARG A 129     5875   4713   5202    191    -37     -4       C  
ATOM   1036  CG  ARG A 129      37.247  -2.279   9.362  1.00 33.29           C  
ANISOU 1036  CG  ARG A 129     4766   3661   4220    196      6      8       C  
ATOM   1037  CD  ARG A 129      37.278  -3.720   8.909  1.00 35.35           C  
ANISOU 1037  CD  ARG A 129     4985   3941   4506    210      8     23       C  
ATOM   1038  NE  ARG A 129      36.344  -3.897   7.812  1.00 40.43           N  
ANISOU 1038  NE  ARG A 129     5564   4586   5213    213     38     21       N  
ATOM   1039  CZ  ARG A 129      35.117  -4.383   7.951  1.00 42.34           C  
ANISOU 1039  CZ  ARG A 129     5797   4802   5487    223     99     17       C  
ATOM   1040  NH1 ARG A 129      34.320  -4.473   6.879  1.00 35.57           N  
ANISOU 1040  NH1 ARG A 129     4869   3959   4688    227    112      3       N  
ATOM   1041  NH2 ARG A 129      34.691  -4.778   9.156  1.00 28.56           N  
ANISOU 1041  NH2 ARG A 129     4114   3020   3717    233    148     26       N  
ATOM   1042  N   ASP A 130      38.795  -0.459  13.056  1.00 35.62           N  
ANISOU 1042  N   ASP A 130     5294   3921   4318    196    -68    -53       N  
ATOM   1043  CA  ASP A 130      39.368   0.122  14.270  1.00 34.91           C  
ANISOU 1043  CA  ASP A 130     5282   3827   4157    202   -107    -87       C  
ATOM   1044  C   ASP A 130      40.679  -0.507  14.781  1.00 31.20           C  
ANISOU 1044  C   ASP A 130     4807   3412   3635    216   -183   -105       C  
ATOM   1045  O   ASP A 130      41.688   0.194  14.932  1.00 31.08           O  
ANISOU 1045  O   ASP A 130     4782   3423   3603    181   -253   -149       O  
ATOM   1046  CB  ASP A 130      38.310   0.274  15.393  1.00 33.84           C  
ANISOU 1046  CB  ASP A 130     5243   3640   3976    249    -45    -80       C  
ATOM   1047  CG  ASP A 130      37.600  -1.043  15.771  1.00 39.08           C  
ANISOU 1047  CG  ASP A 130     5923   4292   4632    304     18    -39       C  
ATOM   1048  OD1 ASP A 130      36.638  -0.961  16.592  1.00 34.18           O  
ANISOU 1048  OD1 ASP A 130     5375   3626   3986    343     86    -25       O  
ATOM   1049  OD2 ASP A 130      37.986  -2.135  15.275  1.00 40.48           O  
ANISOU 1049  OD2 ASP A 130     6049   4500   4830    309      9    -20       O  
ATOM   1050  N   PHE A 131      40.668  -1.820  15.013  1.00 14.94           N  
ANISOU 1050  N   PHE A 131     2753   1372   1552    266   -167    -75       N  
ATOM   1051  CA  PHE A 131      41.806  -2.521  15.626  1.00 28.81           C  
ANISOU 1051  CA  PHE A 131     4520   3185   3242    304   -231    -86       C  
ATOM   1052  C   PHE A 131      42.209  -3.769  14.846  1.00 33.77           C  
ANISOU 1052  C   PHE A 131     5086   3852   3894    319   -233    -51       C  
ATOM   1053  O   PHE A 131      41.372  -4.371  14.148  1.00 38.30           O  
ANISOU 1053  O   PHE A 131     5635   4394   4523    318   -169    -15       O  
ATOM   1054  CB  PHE A 131      41.469  -2.882  17.082  1.00 31.33           C  
ANISOU 1054  CB  PHE A 131     4950   3483   3470    381   -204    -85       C  
ATOM   1055  CG  PHE A 131      40.924  -1.722  17.853  1.00 22.64           C  
ANISOU 1055  CG  PHE A 131     3923   2337   2343    376   -192   -115       C  
ATOM   1056  CD1 PHE A 131      41.717  -0.621  18.091  1.00 17.80           C  
ANISOU 1056  CD1 PHE A 131     3309   1744   1709    336   -270   -175       C  
ATOM   1057  CD2 PHE A 131      39.605  -1.700  18.274  1.00 23.58           C  
ANISOU 1057  CD2 PHE A 131     4106   2390   2464    406    -99    -84       C  
ATOM   1058  CE1 PHE A 131      41.226   0.488  18.750  1.00 22.33           C  
ANISOU 1058  CE1 PHE A 131     3956   2269   2258    329   -258   -206       C  
ATOM   1059  CE2 PHE A 131      39.091  -0.564  18.957  1.00 21.99           C  
ANISOU 1059  CE2 PHE A 131     3978   2145   2234    407    -85   -110       C  
ATOM   1060  CZ  PHE A 131      39.902   0.506  19.201  1.00 21.30           C  
ANISOU 1060  CZ  PHE A 131     3900   2074   2119    370   -165   -170       C  
ATOM   1061  N   THR A 132      43.481  -4.159  14.975  1.00 21.61           N  
ANISOU 1061  N   THR A 132     3520   2380   2311    337   -307    -65       N  
ATOM   1062  CA  THR A 132      44.018  -5.275  14.180  1.00 30.51           C  
ANISOU 1062  CA  THR A 132     4589   3549   3456    354   -316    -32       C  
ATOM   1063  C   THR A 132      43.221  -6.553  14.352  1.00 27.12           C  
ANISOU 1063  C   THR A 132     4208   3080   3016    411   -236     15       C  
ATOM   1064  O   THR A 132      43.047  -7.323  13.413  1.00 38.71           O  
ANISOU 1064  O   THR A 132     5630   4544   4535    405   -208     45       O  
ATOM   1065  CB  THR A 132      45.471  -5.599  14.509  1.00 26.75           C  
ANISOU 1065  CB  THR A 132     4088   3159   2917    385   -403    -53       C  
ATOM   1066  OG1 THR A 132      45.542  -6.109  15.845  1.00 27.48           O  
ANISOU 1066  OG1 THR A 132     4275   3260   2908    469   -403    -57       O  
ATOM   1067  CG2 THR A 132      46.325  -4.352  14.396  1.00 30.10           C  
ANISOU 1067  CG2 THR A 132     4456   3622   3359    319   -480   -108       C  
ATOM   1068  N   ILE A 133      42.712  -6.789  15.545  1.00 27.92           N  
ANISOU 1068  N   ILE A 133     4408   3146   3055    468   -192     20       N  
ATOM   1069  CA  ILE A 133      41.937  -8.004  15.744  1.00 35.23           C  
ANISOU 1069  CA  ILE A 133     5384   4022   3978    517   -100     66       C  
ATOM   1070  C   ILE A 133      40.566  -7.945  15.058  1.00 26.54           C  
ANISOU 1070  C   ILE A 133     4256   2854   2975    468    -17     82       C  
ATOM   1071  O   ILE A 133      39.947  -8.978  14.803  1.00 29.26           O  
ANISOU 1071  O   ILE A 133     4606   3160   3353    481     56    113       O  
ATOM   1072  CB  ILE A 133      41.813  -8.361  17.240  1.00 37.39           C  
ANISOU 1072  CB  ILE A 133     5779   4275   4153    606    -64     74       C  
ATOM   1073  CG1 ILE A 133      41.283  -7.150  18.013  1.00 36.74           C  
ANISOU 1073  CG1 ILE A 133     5745   4163   4051    595    -63     44       C  
ATOM   1074  CG2 ILE A 133      43.174  -8.801  17.777  1.00 18.85           C  
ANISOU 1074  CG2 ILE A 133     3451   2006   1705    676   -143     63       C  
ATOM   1075  CD1 ILE A 133      40.461  -7.538  19.208  1.00 29.58           C  
ANISOU 1075  CD1 ILE A 133     4957   3195   3087    671     27     71       C  
ATOM   1076  N   ASN A 134      40.096  -6.744  14.753  1.00 30.92           N  
ANISOU 1076  N   ASN A 134     4780   3396   3573    413    -26     58       N  
ATOM   1077  CA  ASN A 134      38.824  -6.594  14.037  1.00 34.58           C  
ANISOU 1077  CA  ASN A 134     5204   3811   4124    373     42     67       C  
ATOM   1078  C   ASN A 134      38.962  -6.426  12.505  1.00 37.97           C  
ANISOU 1078  C   ASN A 134     5527   4268   4631    321      8     61       C  
ATOM   1079  O   ASN A 134      37.940  -6.262  11.808  1.00 28.45           O  
ANISOU 1079  O   ASN A 134     4279   3035   3495    294     53     60       O  
ATOM   1080  CB  ASN A 134      38.009  -5.430  14.627  1.00 24.43           C  
ANISOU 1080  CB  ASN A 134     3961   2488   2835    363     71     51       C  
ATOM   1081  CG  ASN A 134      37.683  -5.635  16.102  1.00 23.79           C  
ANISOU 1081  CG  ASN A 134     3991   2370   2679    426    120     63       C  
ATOM   1082  OD1 ASN A 134      37.626  -6.767  16.584  1.00 36.20           O  
ANISOU 1082  OD1 ASN A 134     5606   3924   4223    475    169     91       O  
ATOM   1083  ND2 ASN A 134      37.468  -4.549  16.816  1.00 27.53           N  
ANISOU 1083  ND2 ASN A 134     4518   2827   3115    430    114     42       N  
ATOM   1084  N   ALA A 135      40.202  -6.493  11.996  1.00 24.88           N  
ANISOU 1084  N   ALA A 135     3826   2669   2959    314    -69     55       N  
ATOM   1085  CA  ALA A 135      40.525  -6.048  10.628  1.00 29.36           C  
ANISOU 1085  CA  ALA A 135     4303   3266   3587    271   -108     49       C  
ATOM   1086  C   ALA A 135      40.971  -7.209   9.731  1.00 28.92           C  
ANISOU 1086  C   ALA A 135     4198   3238   3552    285   -119     71       C  
ATOM   1087  O   ALA A 135      41.883  -7.091   8.922  1.00 35.90           O  
ANISOU 1087  O   ALA A 135     5024   4169   4447    273   -174     71       O  
ATOM   1088  CB  ALA A 135      41.600  -4.990  10.676  1.00 27.75           C  
ANISOU 1088  CB  ALA A 135     4082   3102   3360    243   -181     23       C  
ATOM   1089  N   MET A 136      40.336  -8.348   9.918  1.00 32.90           N  
ANISOU 1089  N   MET A 136     4731   3708   4062    312    -61     89       N  
ATOM   1090  CA  MET A 136      40.780  -9.556   9.269  1.00 33.43           C  
ANISOU 1090  CA  MET A 136     4775   3792   4136    334    -66    109       C  
ATOM   1091  C   MET A 136      39.657 -10.116   8.430  1.00 24.28           C  
ANISOU 1091  C   MET A 136     3580   2592   3054    315    -10    106       C  
ATOM   1092  O   MET A 136      38.466  -9.892   8.686  1.00 26.67           O  
ANISOU 1092  O   MET A 136     3890   2848   3394    298     49     94       O  
ATOM   1093  CB  MET A 136      41.282 -10.581  10.285  1.00 29.31           C  
ANISOU 1093  CB  MET A 136     4329   3267   3539    392    -49    131       C  
ATOM   1094  CG  MET A 136      42.668 -10.245  10.820  1.00 34.47           C  
ANISOU 1094  CG  MET A 136     4993   3989   4114    420   -128    127       C  
ATOM   1095  SD  MET A 136      43.322 -11.528  11.912  1.00 40.66           S  
ANISOU 1095  SD  MET A 136     5870   4784   4795    514   -111    155       S  
ATOM   1096  CE  MET A 136      42.305 -11.298  13.388  1.00 39.51           C  
ANISOU 1096  CE  MET A 136     5831   4570   4612    541    -35    153       C  
ATOM   1097  N   ALA A 137      40.051 -10.811   7.387  1.00 18.54           N  
ANISOU 1097  N   ALA A 137     2805   1887   2351    320    -34    112       N  
ATOM   1098  CA  ALA A 137      39.073 -11.339   6.468  1.00 27.33           C  
ANISOU 1098  CA  ALA A 137     3875   2971   3539    302      4     97       C  
ATOM   1099  C   ALA A 137      39.421 -12.782   6.109  1.00 25.14           C  
ANISOU 1099  C   ALA A 137     3610   2683   3258    327     16    112       C  
ATOM   1100  O   ALA A 137      40.563 -13.257   6.318  1.00 21.77           O  
ANISOU 1100  O   ALA A 137     3213   2288   2770    365    -17    139       O  
ATOM   1101  CB  ALA A 137      38.977 -10.426   5.216  1.00 10.66           C  
ANISOU 1101  CB  ALA A 137     1682    894   1473    282    -42     79       C  
ATOM   1102  N   ILE A 138      38.409 -13.493   5.641  1.00 25.14           N  
ANISOU 1102  N   ILE A 138     3591   2638   3323    308     67     91       N  
ATOM   1103  CA  ILE A 138      38.601 -14.824   5.105  1.00 31.09           C  
ANISOU 1103  CA  ILE A 138     4353   3372   4087    324     82     96       C  
ATOM   1104  C   ILE A 138      37.868 -14.863   3.785  1.00 27.03           C  
ANISOU 1104  C   ILE A 138     3758   2861   3652    298     68     54       C  
ATOM   1105  O   ILE A 138      36.687 -14.508   3.692  1.00 24.86           O  
ANISOU 1105  O   ILE A 138     3444   2564   3439    263    100     18       O  
ATOM   1106  CB  ILE A 138      38.037 -15.937   6.011  1.00 35.27           C  
ANISOU 1106  CB  ILE A 138     4957   3824   4619    327    178    104       C  
ATOM   1107  CG1 ILE A 138      38.802 -16.010   7.342  1.00 39.40           C  
ANISOU 1107  CG1 ILE A 138     5574   4348   5049    376    194    147       C  
ATOM   1108  CG2 ILE A 138      38.114 -17.298   5.271  1.00 18.85           C  
ANISOU 1108  CG2 ILE A 138     2884   1714   2565    334    199     99       C  
ATOM   1109  CD1 ILE A 138      38.054 -16.763   8.448  1.00 37.93           C  
ANISOU 1109  CD1 ILE A 138     5473   4077   4863    384    307    160       C  
ATOM   1110  N   LYS A 139      38.581 -15.294   2.767  1.00 24.10           N  
ANISOU 1110  N   LYS A 139     3361   2523   3272    322     17     58       N  
ATOM   1111  CA  LYS A 139      38.060 -15.261   1.421  1.00 28.26           C  
ANISOU 1111  CA  LYS A 139     3814   3066   3857    315    -14     18       C  
ATOM   1112  C   LYS A 139      37.201 -16.479   1.178  1.00 24.82           C  
ANISOU 1112  C   LYS A 139     3379   2571   3479    293     38    -21       C  
ATOM   1113  O   LYS A 139      37.608 -17.594   1.495  1.00 27.72           O  
ANISOU 1113  O   LYS A 139     3809   2900   3825    306     72     -1       O  
ATOM   1114  CB  LYS A 139      39.220 -15.206   0.429  1.00 21.57           C  
ANISOU 1114  CB  LYS A 139     2946   2278   2973    359    -86     42       C  
ATOM   1115  CG  LYS A 139      38.787 -15.100  -1.000  1.00 20.70           C  
ANISOU 1115  CG  LYS A 139     2767   2191   2907    370   -124      4       C  
ATOM   1116  CD  LYS A 139      39.962 -14.681  -1.855  1.00 21.92           C  
ANISOU 1116  CD  LYS A 139     2901   2407   3019    418   -188     38       C  
ATOM   1117  CE  LYS A 139      39.487 -14.301  -3.276  1.00 26.16           C  
ANISOU 1117  CE  LYS A 139     3374   2973   3591    444   -225      3       C  
ATOM   1118  NZ  LYS A 139      40.648 -14.306  -4.180  1.00 27.69           N  
ANISOU 1118  NZ  LYS A 139     3562   3213   3746    500   -272     41       N  
ATOM   1119  N   LEU A 140      36.031 -16.269   0.581  1.00 29.80           N  
ANISOU 1119  N   LEU A 140     3942   3196   4184    262     45    -79       N  
ATOM   1120  CA  LEU A 140      35.106 -17.368   0.287  1.00 27.25           C  
ANISOU 1120  CA  LEU A 140     3603   2818   3934    227     92   -133       C  
ATOM   1121  C   LEU A 140      35.119 -17.965  -1.131  1.00 29.66           C  
ANISOU 1121  C   LEU A 140     3861   3143   4267    244     38   -178       C  
ATOM   1122  O   LEU A 140      34.508 -19.002  -1.347  1.00 28.91           O  
ANISOU 1122  O   LEU A 140     3762   2995   4228    213     75   -226       O  
ATOM   1123  CB  LEU A 140      33.680 -16.967   0.671  1.00 24.99           C  
ANISOU 1123  CB  LEU A 140     3266   2508   3721    177    144   -180       C  
ATOM   1124  CG  LEU A 140      33.613 -16.513   2.138  1.00 29.30           C  
ANISOU 1124  CG  LEU A 140     3872   3023   4237    166    208   -134       C  
ATOM   1125  CD1 LEU A 140      32.174 -16.356   2.614  1.00 23.88           C  
ANISOU 1125  CD1 LEU A 140     3144   2301   3629    117    281   -175       C  
ATOM   1126  CD2 LEU A 140      34.369 -17.512   3.034  1.00 31.06           C  
ANISOU 1126  CD2 LEU A 140     4201   3191   4411    181    261    -83       C  
ATOM   1127  N   ASN A 141      35.788 -17.322  -2.088  1.00 30.40           N  
ANISOU 1127  N   ASN A 141     3922   3306   4321    294    -43   -166       N  
ATOM   1128  CA  ASN A 141      35.791 -17.829  -3.456  1.00 32.24           C  
ANISOU 1128  CA  ASN A 141     4117   3562   4572    325    -97   -209       C  
ATOM   1129  C   ASN A 141      36.504 -19.178  -3.458  1.00 39.88           C  
ANISOU 1129  C   ASN A 141     5154   4483   5514    337    -79   -189       C  
ATOM   1130  O   ASN A 141      37.482 -19.352  -2.709  1.00 31.52           O  
ANISOU 1130  O   ASN A 141     4166   3417   4392    357    -61   -120       O  
ATOM   1131  CB  ASN A 141      36.479 -16.859  -4.417  1.00 28.84           C  
ANISOU 1131  CB  ASN A 141     3652   3209   4095    389   -175   -186       C  
ATOM   1132  CG  ASN A 141      35.818 -15.476  -4.450  1.00 36.38           C  
ANISOU 1132  CG  ASN A 141     4551   4205   5065    387   -186   -201       C  
ATOM   1133  OD1 ASN A 141      34.932 -15.197  -5.287  1.00 34.83           O  
ANISOU 1133  OD1 ASN A 141     4289   4036   4908    402   -212   -262       O  
ATOM   1134  ND2 ASN A 141      36.254 -14.599  -3.550  1.00 34.50           N  
ANISOU 1134  ND2 ASN A 141     4343   3972   4792    377   -168   -147       N  
ATOM   1135  N   PRO A 142      35.994 -20.141  -4.265  1.00 35.33           N  
ANISOU 1135  N   PRO A 142     4561   3878   4986    329    -84   -253       N  
ATOM   1136  CA  PRO A 142      36.387 -21.560  -4.241  1.00 28.96           C  
ANISOU 1136  CA  PRO A 142     3826   3006   4171    329    -48   -250       C  
ATOM   1137  C   PRO A 142      37.896 -21.825  -4.190  1.00 32.38           C  
ANISOU 1137  C   PRO A 142     4335   3461   4507    398    -69   -164       C  
ATOM   1138  O   PRO A 142      38.343 -22.509  -3.265  1.00 32.63           O  
ANISOU 1138  O   PRO A 142     4449   3443   4505    397     -8   -119       O  
ATOM   1139  CB  PRO A 142      35.766 -22.103  -5.525  1.00 35.50           C  
ANISOU 1139  CB  PRO A 142     4602   3835   5052    330    -92   -339       C  
ATOM   1140  CG  PRO A 142      34.473 -21.318  -5.636  1.00 34.82           C  
ANISOU 1140  CG  PRO A 142     4415   3774   5040    287    -99   -410       C  
ATOM   1141  CD  PRO A 142      34.812 -19.922  -5.127  1.00 32.48           C  
ANISOU 1141  CD  PRO A 142     4106   3537   4697    310   -114   -347       C  
ATOM   1142  N   LYS A 143      38.677 -21.295  -5.127  1.00 25.88           N  
ANISOU 1142  N   LYS A 143     3485   2713   3636    463   -148   -140       N  
ATOM   1143  CA  LYS A 143      40.120 -21.532  -5.064  1.00 26.75           C  
ANISOU 1143  CA  LYS A 143     3654   2852   3659    527   -165    -59       C  
ATOM   1144  C   LYS A 143      40.751 -21.030  -3.746  1.00 35.70           C  
ANISOU 1144  C   LYS A 143     4824   3996   4743    521   -135      9       C  
ATOM   1145  O   LYS A 143      41.692 -21.637  -3.230  1.00 39.11           O  
ANISOU 1145  O   LYS A 143     5325   4424   5110    559   -117     64       O  
ATOM   1146  CB  LYS A 143      40.876 -20.922  -6.273  1.00 28.40           C  
ANISOU 1146  CB  LYS A 143     3821   3141   3830    598   -246    -38       C  
ATOM   1147  CG  LYS A 143      42.403 -20.898  -6.041  1.00 35.78           C  
ANISOU 1147  CG  LYS A 143     4796   4120   4679    657   -261     52       C  
ATOM   1148  CD  LYS A 143      43.221 -20.670  -7.283  1.00 36.06           C  
ANISOU 1148  CD  LYS A 143     4807   4218   4678    734   -322     79       C  
ATOM   1149  CE  LYS A 143      44.368 -19.700  -7.010  1.00 30.60           C  
ANISOU 1149  CE  LYS A 143     4093   3596   3938    761   -344    152       C  
ATOM   1150  NZ  LYS A 143      45.346 -20.124  -6.000  1.00 32.68           N  
ANISOU 1150  NZ  LYS A 143     4406   3867   4143    772   -322    211       N  
ATOM   1151  N   ASP A 144      40.256 -19.918  -3.208  1.00 36.27           N  
ANISOU 1151  N   ASP A 144     4854   4088   4839    483   -133      2       N  
ATOM   1152  CA  ASP A 144      40.891 -19.331  -2.025  1.00 39.28           C  
ANISOU 1152  CA  ASP A 144     5267   4489   5170    482   -118     58       C  
ATOM   1153  C   ASP A 144      40.110 -19.564  -0.743  1.00 42.99           C  
ANISOU 1153  C   ASP A 144     5780   4893   5662    433    -39     48       C  
ATOM   1154  O   ASP A 144      40.465 -19.024   0.297  1.00 48.80           O  
ANISOU 1154  O   ASP A 144     6544   5641   6357    434    -27     84       O  
ATOM   1155  CB  ASP A 144      41.233 -17.832  -2.240  1.00 13.22           C  
ANISOU 1155  CB  ASP A 144     1905   1260   1859    487   -172     74       C  
ATOM   1156  CG  ASP A 144      42.297 -17.629  -3.361  1.00 48.80           C  
ANISOU 1156  CG  ASP A 144     6382   5830   6328    547   -236    105       C  
ATOM   1157  OD1 ASP A 144      42.312 -16.563  -4.039  1.00 35.71           O  
ANISOU 1157  OD1 ASP A 144     4668   4217   4685    555   -274    102       O  
ATOM   1158  OD2 ASP A 144      43.109 -18.566  -3.578  1.00 46.70           O  
ANISOU 1158  OD2 ASP A 144     6156   5567   6019    593   -242    135       O  
ATOM   1159  N   PHE A 145      39.067 -20.392  -0.810  1.00 43.13           N  
ANISOU 1159  N   PHE A 145     5805   4838   5746    393     17     -2       N  
ATOM   1160  CA  PHE A 145      38.225 -20.662   0.355  1.00 38.34           C  
ANISOU 1160  CA  PHE A 145     5238   4159   5172    345    108    -11       C  
ATOM   1161  C   PHE A 145      39.032 -20.980   1.624  1.00 39.86           C  
ANISOU 1161  C   PHE A 145     5529   4334   5283    382    152     56       C  
ATOM   1162  O   PHE A 145      39.895 -21.863   1.606  1.00 33.44           O  
ANISOU 1162  O   PHE A 145     4780   3513   4411    433    157     92       O  
ATOM   1163  CB  PHE A 145      37.261 -21.807   0.066  1.00 35.12           C  
ANISOU 1163  CB  PHE A 145     4836   3667   4842    301    171    -69       C  
ATOM   1164  CG  PHE A 145      36.300 -22.081   1.183  1.00 29.49           C  
ANISOU 1164  CG  PHE A 145     4154   2872   4177    247    279    -80       C  
ATOM   1165  CD1 PHE A 145      36.545 -23.099   2.099  1.00 34.78           C  
ANISOU 1165  CD1 PHE A 145     4933   3463   4817    260    371    -41       C  
ATOM   1166  CD2 PHE A 145      35.155 -21.315   1.329  1.00 29.75           C  
ANISOU 1166  CD2 PHE A 145     4113   2907   4282    192    294   -125       C  
ATOM   1167  CE1 PHE A 145      35.649 -23.355   3.156  1.00 40.33           C  
ANISOU 1167  CE1 PHE A 145     5673   4085   5567    216    485    -44       C  
ATOM   1168  CE2 PHE A 145      34.239 -21.567   2.366  1.00 33.29           C  
ANISOU 1168  CE2 PHE A 145     4588   3279   4780    144    403   -131       C  
ATOM   1169  CZ  PHE A 145      34.493 -22.592   3.291  1.00 33.19           C  
ANISOU 1169  CZ  PHE A 145     4687   3182   4741    155    502    -89       C  
ATOM   1170  N   GLY A 146      38.743 -20.257   2.715  1.00 33.33           N  
ANISOU 1170  N   GLY A 146     4715   3504   4445    366    183     71       N  
ATOM   1171  CA  GLY A 146      39.407 -20.478   3.989  1.00 33.21           C  
ANISOU 1171  CA  GLY A 146     4794   3477   4347    410    223    127       C  
ATOM   1172  C   GLY A 146      40.751 -19.783   4.145  1.00 26.02           C  
ANISOU 1172  C   GLY A 146     3883   2659   3346    465    140    170       C  
ATOM   1173  O   GLY A 146      41.528 -20.105   5.055  1.00 26.69           O  
ANISOU 1173  O   GLY A 146     4043   2752   3347    520    155    214       O  
ATOM   1174  N   LEU A 147      41.023 -18.833   3.255  1.00 24.27           N  
ANISOU 1174  N   LEU A 147     3575   2506   3140    453     56    156       N  
ATOM   1175  CA  LEU A 147      42.249 -18.040   3.308  1.00 26.85           C  
ANISOU 1175  CA  LEU A 147     3881   2920   3401    489    -20    189       C  
ATOM   1176  C   LEU A 147      42.115 -16.873   4.281  1.00 31.36           C  
ANISOU 1176  C   LEU A 147     4451   3508   3957    466    -26    187       C  
ATOM   1177  O   LEU A 147      41.295 -15.982   4.084  1.00 30.26           O  
ANISOU 1177  O   LEU A 147     4262   3361   3873    418    -27    156       O  
ATOM   1178  CB  LEU A 147      42.625 -17.488   1.916  1.00 23.08           C  
ANISOU 1178  CB  LEU A 147     3318   2500   2950    488    -94    179       C  
ATOM   1179  CG  LEU A 147      44.027 -16.852   1.900  1.00 30.78           C  
ANISOU 1179  CG  LEU A 147     4270   3561   3863    524   -163    216       C  
ATOM   1180  CD1 LEU A 147      45.110 -17.831   2.354  1.00 34.54           C  
ANISOU 1180  CD1 LEU A 147     4806   4059   4258    590   -164    259       C  
ATOM   1181  CD2 LEU A 147      44.383 -16.287   0.541  1.00 33.98           C  
ANISOU 1181  CD2 LEU A 147     4599   4015   4297    528   -219    214       C  
ATOM   1182  N   LEU A 148      42.928 -16.877   5.330  1.00 29.80           N  
ANISOU 1182  N   LEU A 148     4308   3336   3678    507    -32    218       N  
ATOM   1183  CA  LEU A 148      42.933 -15.778   6.269  1.00 26.58           C  
ANISOU 1183  CA  LEU A 148     3905   2948   3246    492    -48    211       C  
ATOM   1184  C   LEU A 148      43.739 -14.691   5.573  1.00 35.71           C  
ANISOU 1184  C   LEU A 148     4980   4182   4405    477   -135    206       C  
ATOM   1185  O   LEU A 148      44.880 -14.917   5.109  1.00 29.01           O  
ANISOU 1185  O   LEU A 148     4108   3393   3521    512   -187    228       O  
ATOM   1186  CB  LEU A 148      43.605 -16.170   7.592  1.00 26.94           C  
ANISOU 1186  CB  LEU A 148     4036   3004   3195    554    -35    238       C  
ATOM   1187  CG  LEU A 148      43.175 -15.604   8.965  1.00 28.20           C  
ANISOU 1187  CG  LEU A 148     4254   3139   3320    556     -3    232       C  
ATOM   1188  CD1 LEU A 148      44.398 -15.330   9.829  1.00 32.38           C  
ANISOU 1188  CD1 LEU A 148     4813   3743   3748    615    -64    243       C  
ATOM   1189  CD2 LEU A 148      42.257 -14.381   8.930  1.00 20.94           C  
ANISOU 1189  CD2 LEU A 148     3291   2201   2464    488     -2    199       C  
ATOM   1190  N   ILE A 149      43.134 -13.516   5.465  1.00 28.69           N  
ANISOU 1190  N   ILE A 149     4050   3287   3562    426   -143    180       N  
ATOM   1191  CA  ILE A 149      43.863 -12.369   4.976  1.00 22.91           C  
ANISOU 1191  CA  ILE A 149     3255   2614   2834    407   -209    175       C  
ATOM   1192  C   ILE A 149      44.036 -11.427   6.136  1.00 23.82           C  
ANISOU 1192  C   ILE A 149     3398   2739   2912    391   -221    163       C  
ATOM   1193  O   ILE A 149      43.061 -10.865   6.655  1.00 29.06           O  
ANISOU 1193  O   ILE A 149     4086   3358   3598    363   -184    143       O  
ATOM   1194  CB  ILE A 149      43.145 -11.666   3.848  1.00 33.81           C  
ANISOU 1194  CB  ILE A 149     4574   3985   4289    371   -209    155       C  
ATOM   1195  CG1 ILE A 149      43.117 -12.567   2.608  1.00 32.10           C  
ANISOU 1195  CG1 ILE A 149     4326   3770   4101    395   -212    162       C  
ATOM   1196  CG2 ILE A 149      43.848 -10.351   3.549  1.00 27.72           C  
ANISOU 1196  CG2 ILE A 149     3754   3258   3520    349   -257    153       C  
ATOM   1197  CD1 ILE A 149      41.863 -12.422   1.841  1.00 26.71           C  
ANISOU 1197  CD1 ILE A 149     3610   3051   3486    373   -185    129       C  
ATOM   1198  N   ASP A 150      45.281 -11.310   6.572  1.00 25.63           N  
ANISOU 1198  N   ASP A 150     3626   3030   3084    415   -276    171       N  
ATOM   1199  CA  ASP A 150      45.598 -10.554   7.768  1.00 35.40           C  
ANISOU 1199  CA  ASP A 150     4895   4283   4272    410   -299    151       C  
ATOM   1200  C   ASP A 150      46.781  -9.615   7.520  1.00 35.05           C  
ANISOU 1200  C   ASP A 150     4784   4310   4225    385   -373    137       C  
ATOM   1201  O   ASP A 150      47.945  -9.978   7.673  1.00 36.28           O  
ANISOU 1201  O   ASP A 150     4920   4532   4332    419   -422    144       O  
ATOM   1202  CB  ASP A 150      45.850 -11.496   8.938  1.00 31.46           C  
ANISOU 1202  CB  ASP A 150     4478   3787   3689    477   -283    165       C  
ATOM   1203  CG  ASP A 150      46.346 -10.775  10.167  1.00 31.18           C  
ANISOU 1203  CG  ASP A 150     4475   3783   3588    487   -323    138       C  
ATOM   1204  OD1 ASP A 150      47.173 -11.358  10.874  1.00 39.51           O  
ANISOU 1204  OD1 ASP A 150     5564   4886   4561    553   -351    145       O  
ATOM   1205  OD2 ASP A 150      45.939  -9.620  10.412  1.00 45.77           O  
ANISOU 1205  OD2 ASP A 150     6315   5611   5463    436   -329    108       O  
ATOM   1206  N   PHE A 151      46.456  -8.398   7.117  1.00 33.87           N  
ANISOU 1206  N   PHE A 151     4597   4142   4130    325   -376    115       N  
ATOM   1207  CA  PHE A 151      47.469  -7.474   6.652  1.00 27.96           C  
ANISOU 1207  CA  PHE A 151     3779   3443   3402    288   -428    103       C  
ATOM   1208  C   PHE A 151      48.176  -6.882   7.849  1.00 31.15           C  
ANISOU 1208  C   PHE A 151     4200   3882   3755    277   -475     66       C  
ATOM   1209  O   PHE A 151      49.321  -6.443   7.734  1.00 37.31           O  
ANISOU 1209  O   PHE A 151     4919   4722   4535    257   -530     51       O  
ATOM   1210  CB  PHE A 151      46.833  -6.351   5.790  1.00 20.91           C  
ANISOU 1210  CB  PHE A 151     2854   2508   2583    234   -401     95       C  
ATOM   1211  CG  PHE A 151      46.263  -6.827   4.474  1.00 31.63           C  
ANISOU 1211  CG  PHE A 151     4183   3847   3989    252   -369    122       C  
ATOM   1212  CD1 PHE A 151      47.116  -7.185   3.421  1.00 37.58           C  
ANISOU 1212  CD1 PHE A 151     4877   4645   4756    272   -392    149       C  
ATOM   1213  CD2 PHE A 151      44.884  -6.917   4.278  1.00 20.44           C  
ANISOU 1213  CD2 PHE A 151     2793   2372   2600    254   -317    118       C  
ATOM   1214  CE1 PHE A 151      46.611  -7.639   2.180  1.00 28.81           C  
ANISOU 1214  CE1 PHE A 151     3745   3520   3683    299   -368    170       C  
ATOM   1215  CE2 PHE A 151      44.377  -7.361   3.041  1.00 43.93           C  
ANISOU 1215  CE2 PHE A 151     5735   5338   5617    275   -298    132       C  
ATOM   1216  CZ  PHE A 151      45.252  -7.727   1.984  1.00 31.20           C  
ANISOU 1216  CZ  PHE A 151     4073   3769   4013    300   -326    157       C  
ATOM   1217  N   PHE A 152      47.508  -6.892   9.007  1.00 24.28           N  
ANISOU 1217  N   PHE A 152     3409   2975   2840    293   -455     49       N  
ATOM   1218  CA  PHE A 152      47.909  -5.989  10.083  1.00 23.32           C  
ANISOU 1218  CA  PHE A 152     3310   2869   2680    272   -497      1       C  
ATOM   1219  C   PHE A 152      48.469  -6.565  11.380  1.00 31.72           C  
ANISOU 1219  C   PHE A 152     4428   3978   3645    337   -535    -15       C  
ATOM   1220  O   PHE A 152      48.782  -5.802  12.299  1.00 33.77           O  
ANISOU 1220  O   PHE A 152     4709   4254   3868    324   -577    -64       O  
ATOM   1221  CB  PHE A 152      46.785  -4.980  10.360  1.00 31.50           C  
ANISOU 1221  CB  PHE A 152     4393   3828   3747    229   -452    -20       C  
ATOM   1222  CG  PHE A 152      46.170  -4.393   9.097  1.00 27.11           C  
ANISOU 1222  CG  PHE A 152     3791   3231   3277    182   -412     -4       C  
ATOM   1223  CD1 PHE A 152      46.848  -3.439   8.370  1.00 19.25           C  
ANISOU 1223  CD1 PHE A 152     2731   2252   2330    127   -437    -18       C  
ATOM   1224  CD2 PHE A 152      44.905  -4.792   8.656  1.00 24.47           C  
ANISOU 1224  CD2 PHE A 152     3480   2843   2976    197   -345     22       C  
ATOM   1225  CE1 PHE A 152      46.278  -2.890   7.199  1.00 25.44           C  
ANISOU 1225  CE1 PHE A 152     3484   2998   3183    101   -394      0       C  
ATOM   1226  CE2 PHE A 152      44.337  -4.244   7.505  1.00 32.65           C  
ANISOU 1226  CE2 PHE A 152     4474   3851   4079    169   -314     31       C  
ATOM   1227  CZ  PHE A 152      45.026  -3.297   6.778  1.00 27.02           C  
ANISOU 1227  CZ  PHE A 152     3708   3154   3404    128   -337     24       C  
ATOM   1228  N   GLY A 153      48.610  -7.886  11.452  1.00 35.26           N  
ANISOU 1228  N   GLY A 153     4904   4448   4046    413   -520     23       N  
ATOM   1229  CA  GLY A 153      49.208  -8.530  12.606  1.00 32.81           C  
ANISOU 1229  CA  GLY A 153     4649   4187   3630    496   -553     14       C  
ATOM   1230  C   GLY A 153      48.148  -8.892  13.634  1.00 33.79           C  
ANISOU 1230  C   GLY A 153     4891   4241   3706    545   -486     24       C  
ATOM   1231  O   GLY A 153      48.437  -9.062  14.813  1.00 25.19           O  
ANISOU 1231  O   GLY A 153     3869   3178   2524    613   -507      7       O  
ATOM   1232  N   GLY A 154      46.915  -9.001  13.155  1.00 29.72           N  
ANISOU 1232  N   GLY A 154     4398   3640   3256    514   -403     52       N  
ATOM   1233  CA  GLY A 154      45.766  -9.373  13.949  1.00 27.82           C  
ANISOU 1233  CA  GLY A 154     4256   3322   2994    548   -320     68       C  
ATOM   1234  C   GLY A 154      45.790 -10.752  14.566  1.00 34.94           C  
ANISOU 1234  C   GLY A 154     5239   4214   3821    645   -273    107       C  
ATOM   1235  O   GLY A 154      45.354 -10.900  15.701  1.00 40.85           O  
ANISOU 1235  O   GLY A 154     6085   4929   4508    701   -231    110       O  
ATOM   1236  N   TYR A 155      46.282 -11.753  13.834  1.00 32.70           N  
ANISOU 1236  N   TYR A 155     4926   3956   3542    672   -271    139       N  
ATOM   1237  CA  TYR A 155      46.379 -13.138  14.349  1.00 36.56           C  
ANISOU 1237  CA  TYR A 155     5501   4432   3958    770   -218    180       C  
ATOM   1238  C   TYR A 155      47.278 -13.170  15.567  1.00 40.15           C  
ANISOU 1238  C   TYR A 155     6014   4955   4287    865   -270    165       C  
ATOM   1239  O   TYR A 155      46.905 -13.676  16.629  1.00 40.94           O  
ANISOU 1239  O   TYR A 155     6226   5018   4313    946   -211    183       O  
ATOM   1240  CB  TYR A 155      46.985 -14.061  13.292  1.00 36.22           C  
ANISOU 1240  CB  TYR A 155     5409   4420   3933    783   -227    211       C  
ATOM   1241  CG  TYR A 155      47.046 -15.545  13.633  1.00 43.71           C  
ANISOU 1241  CG  TYR A 155     6450   5342   4816    881   -160    257       C  
ATOM   1242  CD1 TYR A 155      45.976 -16.400  13.331  1.00 39.60           C  
ANISOU 1242  CD1 TYR A 155     5978   4718   4351    867    -50    286       C  
ATOM   1243  CD2 TYR A 155      48.190 -16.107  14.214  1.00 45.24           C  
ANISOU 1243  CD2 TYR A 155     6679   5615   4895    986   -203    270       C  
ATOM   1244  CE1 TYR A 155      46.030 -17.773  13.620  1.00 35.37           C  
ANISOU 1244  CE1 TYR A 155     5535   4144   3760    952     25    330       C  
ATOM   1245  CE2 TYR A 155      48.260 -17.472  14.504  1.00 44.26           C  
ANISOU 1245  CE2 TYR A 155     6651   5462   4704   1085   -132    317       C  
ATOM   1246  CZ  TYR A 155      47.178 -18.312  14.207  1.00 47.77           C  
ANISOU 1246  CZ  TYR A 155     7154   5789   5207   1066    -13    349       C  
ATOM   1247  OH  TYR A 155      47.250 -19.682  14.496  1.00 42.88           O  
ANISOU 1247  OH  TYR A 155     6641   5127   4525   1161     70    397       O  
ATOM   1248  N   ARG A 156      48.477 -12.631  15.360  1.00 36.04           N  
ANISOU 1248  N   ARG A 156     5411   4538   3744    856   -380    132       N  
ATOM   1249  CA  ARG A 156      49.501 -12.428  16.368  1.00 33.65           C  
ANISOU 1249  CA  ARG A 156     5126   4327   3331    931   -462     96       C  
ATOM   1250  C   ARG A 156      48.979 -11.602  17.551  1.00 41.38           C  
ANISOU 1250  C   ARG A 156     6177   5277   4270    938   -462     57       C  
ATOM   1251  O   ARG A 156      49.310 -11.895  18.690  1.00 34.68           O  
ANISOU 1251  O   ARG A 156     5411   4461   3305   1044   -477     47       O  
ATOM   1252  CB  ARG A 156      50.697 -11.711  15.720  1.00 26.07           C  
ANISOU 1252  CB  ARG A 156     4033   3472   2400    876   -575     55       C  
ATOM   1253  CG  ARG A 156      51.960 -11.615  16.585  1.00 38.15           C  
ANISOU 1253  CG  ARG A 156     5549   5123   3822    952   -677     10       C  
ATOM   1254  CD  ARG A 156      52.057 -10.265  17.325  1.00 46.17           C  
ANISOU 1254  CD  ARG A 156     6550   6158   4834    900   -747    -70       C  
ATOM   1255  NE  ARG A 156      51.867  -9.129  16.426  1.00 50.66           N  
ANISOU 1255  NE  ARG A 156     7024   6696   5529    757   -760    -96       N  
ATOM   1256  CZ  ARG A 156      52.850  -8.377  15.926  1.00 52.47           C  
ANISOU 1256  CZ  ARG A 156     7133   6999   5804    687   -843   -142       C  
ATOM   1257  NH1 ARG A 156      52.559  -7.361  15.117  1.00 42.85           N  
ANISOU 1257  NH1 ARG A 156     5849   5733   4698    565   -833   -157       N  
ATOM   1258  NH2 ARG A 156      54.122  -8.627  16.231  1.00 51.91           N  
ANISOU 1258  NH2 ARG A 156     7005   7050   5668    742   -931   -174       N  
ATOM   1259  N   ASP A 157      48.186 -10.563  17.282  1.00 37.97           N  
ANISOU 1259  N   ASP A 157     5719   4785   3924    836   -446     34       N  
ATOM   1260  CA  ASP A 157      47.726  -9.665  18.348  1.00 27.65           C  
ANISOU 1260  CA  ASP A 157     4478   3449   2580    838   -452     -7       C  
ATOM   1261  C   ASP A 157      46.669 -10.341  19.215  1.00 30.48           C  
ANISOU 1261  C   ASP A 157     4970   3721   2891    916   -340     36       C  
ATOM   1262  O   ASP A 157      46.496  -9.978  20.370  1.00 38.04           O  
ANISOU 1262  O   ASP A 157     6014   4670   3770    974   -342     14       O  
ATOM   1263  CB  ASP A 157      47.192  -8.330  17.789  1.00 19.70           C  
ANISOU 1263  CB  ASP A 157     3410   2400   1674    713   -461    -41       C  
ATOM   1264  CG  ASP A 157      48.308  -7.356  17.446  1.00 31.75           C  
ANISOU 1264  CG  ASP A 157     4834   4008   3222    647   -574   -102       C  
ATOM   1265  OD1 ASP A 157      48.074  -6.362  16.699  1.00 23.82           O  
ANISOU 1265  OD1 ASP A 157     3765   2975   2312    542   -578   -122       O  
ATOM   1266  OD2 ASP A 157      49.440  -7.603  17.918  1.00 37.99           O  
ANISOU 1266  OD2 ASP A 157     5607   4893   3936    704   -655   -132       O  
ATOM   1267  N   LEU A 158      45.943 -11.296  18.644  1.00 35.93           N  
ANISOU 1267  N   LEU A 158     5677   4343   3632    915   -240     96       N  
ATOM   1268  CA  LEU A 158      45.064 -12.174  19.426  1.00 47.86           C  
ANISOU 1268  CA  LEU A 158     7314   5771   5101    995   -120    144       C  
ATOM   1269  C   LEU A 158      45.868 -13.033  20.416  1.00 49.36           C  
ANISOU 1269  C   LEU A 158     7598   6011   5147   1143   -129    159       C  
ATOM   1270  O   LEU A 158      45.552 -13.086  21.603  1.00 54.35           O  
ANISOU 1270  O   LEU A 158     8344   6614   5692   1233    -87    165       O  
ATOM   1271  CB  LEU A 158      44.230 -13.094  18.509  1.00 38.46           C  
ANISOU 1271  CB  LEU A 158     6108   4500   4005    954    -15    195       C  
ATOM   1272  CG  LEU A 158      43.219 -12.440  17.550  1.00 30.55           C  
ANISOU 1272  CG  LEU A 158     5026   3442   3140    829     16    185       C  
ATOM   1273  CD1 LEU A 158      42.636 -13.465  16.627  1.00 24.26           C  
ANISOU 1273  CD1 LEU A 158     4205   2588   2423    800     96    222       C  
ATOM   1274  CD2 LEU A 158      42.098 -11.783  18.312  1.00 36.01           C  
ANISOU 1274  CD2 LEU A 158     5776   4063   3842    818     81    180       C  
ATOM   1275  N   LYS A 159      46.906 -13.699  19.915  1.00 40.87           N  
ANISOU 1275  N   LYS A 159     6475   5011   4041   1179   -183    168       N  
ATOM   1276  CA  LYS A 159      47.734 -14.599  20.724  1.00 40.81           C  
ANISOU 1276  CA  LYS A 159     6551   5062   3892   1331   -193    186       C  
ATOM   1277  C   LYS A 159      48.525 -13.851  21.801  1.00 45.17           C  
ANISOU 1277  C   LYS A 159     7123   5709   4331   1401   -302    124       C  
ATOM   1278  O   LYS A 159      49.085 -14.468  22.720  1.00 37.83           O  
ANISOU 1278  O   LYS A 159     6282   4828   3263   1549   -310    132       O  
ATOM   1279  CB  LYS A 159      48.665 -15.455  19.822  1.00 38.81           C  
ANISOU 1279  CB  LYS A 159     6234   4874   3639   1350   -227    211       C  
ATOM   1280  CG  LYS A 159      48.019 -16.772  19.349  1.00 41.25           C  
ANISOU 1280  CG  LYS A 159     6606   5087   3981   1371    -94    283       C  
ATOM   1281  CD  LYS A 159      48.879 -17.595  18.379  1.00 46.12           C  
ANISOU 1281  CD  LYS A 159     7164   5758   4600   1388   -124    308       C  
ATOM   1282  CE  LYS A 159      48.174 -18.928  18.050  1.00 63.39           C  
ANISOU 1282  CE  LYS A 159     9437   7835   6814   1414     17    374       C  
ATOM   1283  NZ  LYS A 159      48.885 -19.770  17.027  1.00 76.77           N  
ANISOU 1283  NZ  LYS A 159    11085   9566   8517   1426      0    401       N  
ATOM   1284  N   GLU A 160      48.546 -12.521  21.698  1.00 44.87           N  
ANISOU 1284  N   GLU A 160     7008   5694   4348   1300   -383     60       N  
ATOM   1285  CA  GLU A 160      49.248 -11.685  22.670  1.00 44.64           C  
ANISOU 1285  CA  GLU A 160     6987   5749   4225   1345   -493    -15       C  
ATOM   1286  C   GLU A 160      48.297 -10.812  23.470  1.00 44.54           C  
ANISOU 1286  C   GLU A 160     7052   5659   4211   1327   -458    -38       C  
ATOM   1287  O   GLU A 160      48.737  -9.983  24.298  1.00 40.05           O  
ANISOU 1287  O   GLU A 160     6500   5146   3573   1354   -548   -109       O  
ATOM   1288  CB  GLU A 160      50.288 -10.818  21.970  1.00 45.82           C  
ANISOU 1288  CB  GLU A 160     6982   5999   4429   1248   -629    -83       C  
ATOM   1289  CG  GLU A 160      51.182 -11.631  21.075  1.00 61.95           C  
ANISOU 1289  CG  GLU A 160     8940   8115   6484   1259   -657    -54       C  
ATOM   1290  CD  GLU A 160      52.546 -11.012  20.872  1.00 73.01           C  
ANISOU 1290  CD  GLU A 160    10211   9652   7878   1229   -802   -126       C  
ATOM   1291  OE1 GLU A 160      53.478 -11.766  20.496  1.00 76.37           O  
ANISOU 1291  OE1 GLU A 160    10585  10165   8266   1286   -838   -108       O  
ATOM   1292  OE2 GLU A 160      52.682  -9.785  21.087  1.00 71.65           O  
ANISOU 1292  OE2 GLU A 160     9989   9496   7738   1148   -874   -201       O  
ATOM   1293  N   GLY A 161      46.997 -11.003  23.219  1.00 32.53           N  
ANISOU 1293  N   GLY A 161     5578   4015   2768   1284   -328     18       N  
ATOM   1294  CA  GLY A 161      45.957 -10.303  23.962  1.00 29.64           C  
ANISOU 1294  CA  GLY A 161     5294   3567   2402   1278   -270     12       C  
ATOM   1295  C   GLY A 161      46.035  -8.795  23.826  1.00 31.52           C  
ANISOU 1295  C   GLY A 161     5463   3824   2691   1170   -360    -63       C  
ATOM   1296  O   GLY A 161      45.903  -8.072  24.834  1.00 38.39           O  
ANISOU 1296  O   GLY A 161     6407   4690   3491   1211   -387   -105       O  
ATOM   1297  N   VAL A 162      46.223  -8.323  22.583  1.00 27.67           N  
ANISOU 1297  N   VAL A 162     4842   3350   2322   1038   -399    -77       N  
ATOM   1298  CA  VAL A 162      46.557  -6.919  22.315  1.00 34.44           C  
ANISOU 1298  CA  VAL A 162     5621   4234   3230    932   -490   -150       C  
ATOM   1299  C   VAL A 162      45.497  -6.153  21.523  1.00 38.55           C  
ANISOU 1299  C   VAL A 162     6105   4666   3876    813   -427   -136       C  
ATOM   1300  O   VAL A 162      44.938  -6.657  20.545  1.00 39.14           O  
ANISOU 1300  O   VAL A 162     6134   4699   4038    768   -358    -84       O  
ATOM   1301  CB  VAL A 162      47.940  -6.794  21.616  1.00 46.27           C  
ANISOU 1301  CB  VAL A 162     6990   5842   4749    886   -608   -194       C  
ATOM   1302  CG1 VAL A 162      47.960  -5.635  20.636  1.00 44.79           C  
ANISOU 1302  CG1 VAL A 162     6695   5640   4682    737   -641   -229       C  
ATOM   1303  CG2 VAL A 162      49.037  -6.632  22.646  1.00 40.73           C  
ANISOU 1303  CG2 VAL A 162     6307   5242   3926    968   -721   -264       C  
ATOM   1304  N   ILE A 163      45.207  -4.939  21.979  1.00 40.66           N  
ANISOU 1304  N   ILE A 163     6399   4906   4143    773   -452   -186       N  
ATOM   1305  CA  ILE A 163      44.383  -4.005  21.226  1.00 35.72           C  
ANISOU 1305  CA  ILE A 163     5733   4213   3626    664   -411   -185       C  
ATOM   1306  C   ILE A 163      45.316  -3.000  20.571  1.00 41.38           C  
ANISOU 1306  C   ILE A 163     6346   4980   4395    564   -510   -249       C  
ATOM   1307  O   ILE A 163      46.019  -2.274  21.263  1.00 46.08           O  
ANISOU 1307  O   ILE A 163     6955   5616   4937    564   -596   -321       O  
ATOM   1308  CB  ILE A 163      43.381  -3.251  22.115  1.00 35.19           C  
ANISOU 1308  CB  ILE A 163     5772   4071   3528    685   -359   -193       C  
ATOM   1309  CG1 ILE A 163      42.467  -4.233  22.849  1.00 37.83           C  
ANISOU 1309  CG1 ILE A 163     6212   4351   3811    787   -248   -128       C  
ATOM   1310  CG2 ILE A 163      42.549  -2.260  21.264  1.00 26.27           C  
ANISOU 1310  CG2 ILE A 163     4597   2878   2506    579   -316   -190       C  
ATOM   1311  CD1 ILE A 163      41.655  -5.101  21.899  1.00 29.37           C  
ANISOU 1311  CD1 ILE A 163     5094   3232   2833    757   -147    -57       C  
ATOM   1312  N   ARG A 164      45.327  -2.983  19.241  1.00 41.02           N  
ANISOU 1312  N   ARG A 164     6199   4932   4455    482   -496   -224       N  
ATOM   1313  CA  ARG A 164      46.245  -2.148  18.476  1.00 42.61           C  
ANISOU 1313  CA  ARG A 164     6296   5176   4717    388   -572   -272       C  
ATOM   1314  C   ARG A 164      45.497  -1.511  17.303  1.00 36.66           C  
ANISOU 1314  C   ARG A 164     5493   4359   4077    300   -511   -245       C  
ATOM   1315  O   ARG A 164      44.770  -2.190  16.592  1.00 38.49           O  
ANISOU 1315  O   ARG A 164     5710   4560   4354    308   -441   -185       O  
ATOM   1316  CB  ARG A 164      47.426  -2.989  17.955  1.00 33.24           C  
ANISOU 1316  CB  ARG A 164     5021   4083   3527    403   -632   -265       C  
ATOM   1317  CG  ARG A 164      48.593  -2.177  17.432  1.00 26.33           C  
ANISOU 1317  CG  ARG A 164     4038   3268   2699    319   -719   -324       C  
ATOM   1318  CD  ARG A 164      49.586  -3.032  16.637  1.00 31.94           C  
ANISOU 1318  CD  ARG A 164     4648   4061   3426    329   -755   -299       C  
ATOM   1319  NE  ARG A 164      49.919  -4.266  17.351  1.00 43.41           N  
ANISOU 1319  NE  ARG A 164     6147   5571   4776    448   -771   -277       N  
ATOM   1320  CZ  ARG A 164      51.057  -4.510  18.005  1.00 40.58           C  
ANISOU 1320  CZ  ARG A 164     5766   5315   4339    503   -862   -323       C  
ATOM   1321  NH1 ARG A 164      51.236  -5.682  18.602  1.00 47.53           N  
ANISOU 1321  NH1 ARG A 164     6703   6238   5120    626   -860   -292       N  
ATOM   1322  NH2 ARG A 164      52.024  -3.609  18.054  1.00 33.77           N  
ANISOU 1322  NH2 ARG A 164     4822   4513   3496    438   -953   -402       N  
ATOM   1323  N   VAL A 165      45.672  -0.207  17.111  1.00 36.56           N  
ANISOU 1323  N   VAL A 165     5460   4326   4106    220   -538   -294       N  
ATOM   1324  CA  VAL A 165      45.097   0.479  15.956  1.00 36.23           C  
ANISOU 1324  CA  VAL A 165     5373   4230   4162    146   -484   -271       C  
ATOM   1325  C   VAL A 165      45.938   0.236  14.686  1.00 36.12           C  
ANISOU 1325  C   VAL A 165     5241   4265   4219     99   -510   -256       C  
ATOM   1326  O   VAL A 165      47.137  -0.106  14.764  1.00 28.01           O  
ANISOU 1326  O   VAL A 165     4156   3314   3171    100   -583   -281       O  
ATOM   1327  CB  VAL A 165      44.942   2.012  16.209  1.00 27.36           C  
ANISOU 1327  CB  VAL A 165     4287   3053   3056     83   -487   -325       C  
ATOM   1328  CG1 VAL A 165      43.889   2.292  17.280  1.00 20.92           C  
ANISOU 1328  CG1 VAL A 165     3593   2177   2179    134   -441   -326       C  
ATOM   1329  CG2 VAL A 165      46.292   2.657  16.546  1.00 20.51           C  
ANISOU 1329  CG2 VAL A 165     3379   2236   2179     30   -583   -404       C  
ATOM   1330  N   LEU A 166      45.319   0.430  13.523  1.00 25.21           N  
ANISOU 1330  N   LEU A 166     3820   2843   2914     66   -450   -215       N  
ATOM   1331  CA  LEU A 166      46.000   0.143  12.251  1.00 34.00           C  
ANISOU 1331  CA  LEU A 166     4831   3996   4091     36   -463   -191       C  
ATOM   1332  C   LEU A 166      46.931   1.229  11.705  1.00 25.86           C  
ANISOU 1332  C   LEU A 166     3736   2974   3115    -46   -496   -229       C  
ATOM   1333  O   LEU A 166      47.718   0.953  10.804  1.00 39.05           O  
ANISOU 1333  O   LEU A 166     5321   4689   4828    -64   -514   -212       O  
ATOM   1334  CB  LEU A 166      44.989  -0.232  11.159  1.00 46.88           C  
ANISOU 1334  CB  LEU A 166     6445   5589   5777     50   -389   -133       C  
ATOM   1335  CG  LEU A 166      43.813  -1.167  11.468  1.00 50.33           C  
ANISOU 1335  CG  LEU A 166     6935   5998   6191    111   -332    -96       C  
ATOM   1336  CD1 LEU A 166      43.275  -1.734  10.172  1.00 45.27           C  
ANISOU 1336  CD1 LEU A 166     6238   5351   5611    118   -290    -52       C  
ATOM   1337  CD2 LEU A 166      44.213  -2.282  12.390  1.00 53.20           C  
ANISOU 1337  CD2 LEU A 166     7333   6400   6482    171   -358    -91       C  
ATOM   1338  N   HIS A 167      46.819   2.460  12.205  1.00 30.99           N  
ANISOU 1338  N   HIS A 167     4431   3575   3768    -95   -494   -278       N  
ATOM   1339  CA  HIS A 167      47.697   3.572  11.789  1.00 32.74           C  
ANISOU 1339  CA  HIS A 167     4601   3790   4048   -184   -515   -322       C  
ATOM   1340  C   HIS A 167      47.676   4.682  12.826  1.00 36.55           C  
ANISOU 1340  C   HIS A 167     5155   4228   4503   -224   -534   -394       C  
ATOM   1341  O   HIS A 167      46.805   4.697  13.722  1.00 30.41           O  
ANISOU 1341  O   HIS A 167     4474   3415   3665   -178   -518   -398       O  
ATOM   1342  CB  HIS A 167      47.252   4.167  10.455  1.00 26.07           C  
ANISOU 1342  CB  HIS A 167     3731   2891   3284   -216   -439   -279       C  
ATOM   1343  CG  HIS A 167      45.896   4.788  10.511  1.00 25.88           C  
ANISOU 1343  CG  HIS A 167     3795   2784   3256   -198   -366   -263       C  
ATOM   1344  ND1 HIS A 167      44.739   4.073  10.301  1.00 24.89           N  
ANISOU 1344  ND1 HIS A 167     3696   2647   3114   -130   -319   -210       N  
ATOM   1345  CD2 HIS A 167      45.509   6.066  10.786  1.00 27.86           C  
ANISOU 1345  CD2 HIS A 167     4111   2959   3514   -237   -331   -294       C  
ATOM   1346  CE1 HIS A 167      43.693   4.878  10.426  1.00 27.90           C  
ANISOU 1346  CE1 HIS A 167     4149   2959   3493   -124   -259   -209       C  
ATOM   1347  NE2 HIS A 167      44.138   6.086  10.731  1.00 34.07           N  
ANISOU 1347  NE2 HIS A 167     4961   3699   4284   -184   -265   -256       N  
ATOM   1348  N   THR A 168      48.598   5.634  12.659  1.00 22.63           N  
ANISOU 1348  N   THR A 168     3346   2461   2791   -312   -561   -450       N  
ATOM   1349  CA  THR A 168      48.816   6.738  13.618  1.00 27.28           C  
ANISOU 1349  CA  THR A 168     3992   3011   3362   -367   -593   -537       C  
ATOM   1350  C   THR A 168      47.700   7.765  13.852  1.00 28.70           C  
ANISOU 1350  C   THR A 168     4285   3082   3536   -374   -521   -538       C  
ATOM   1351  O   THR A 168      47.680   8.418  14.882  1.00 29.75           O  
ANISOU 1351  O   THR A 168     4492   3186   3626   -389   -552   -605       O  
ATOM   1352  CB  THR A 168      50.115   7.506  13.298  1.00 34.41           C  
ANISOU 1352  CB  THR A 168     4807   3931   4337   -473   -631   -602       C  
ATOM   1353  OG1 THR A 168      51.220   6.635  13.534  1.00 46.91           O  
ANISOU 1353  OG1 THR A 168     6296   5628   5898   -458   -721   -626       O  
ATOM   1354  CG2 THR A 168      50.285   8.724  14.215  1.00 44.67           C  
ANISOU 1354  CG2 THR A 168     6168   5175   5628   -541   -658   -700       C  
ATOM   1355  N   LEU A 169      46.785   7.919  12.916  1.00 32.04           N  
ANISOU 1355  N   LEU A 169     4726   3450   3999   -357   -430   -469       N  
ATOM   1356  CA  LEU A 169      45.768   8.953  13.025  1.00 23.85           C  
ANISOU 1356  CA  LEU A 169     3790   2313   2958   -359   -357   -467       C  
ATOM   1357  C   LEU A 169      44.455   8.310  13.414  1.00 20.07           C  
ANISOU 1357  C   LEU A 169     3380   1827   2420   -264   -319   -415       C  
ATOM   1358  O   LEU A 169      43.377   8.903  13.272  1.00 21.13           O  
ANISOU 1358  O   LEU A 169     3585   1893   2552   -240   -244   -388       O  
ATOM   1359  CB  LEU A 169      45.618   9.671  11.672  1.00 31.02           C  
ANISOU 1359  CB  LEU A 169     4672   3167   3949   -396   -275   -427       C  
ATOM   1360  CG  LEU A 169      46.504  10.899  11.462  1.00 39.86           C  
ANISOU 1360  CG  LEU A 169     5781   4234   5130   -501   -266   -484       C  
ATOM   1361  CD1 LEU A 169      47.681  10.946  12.444  1.00 38.36           C  
ANISOU 1361  CD1 LEU A 169     5558   4090   4927   -564   -367   -578       C  
ATOM   1362  CD2 LEU A 169      46.989  10.975  10.026  1.00 28.96           C  
ANISOU 1362  CD2 LEU A 169     4315   2853   3835   -531   -216   -438       C  
ATOM   1363  N   SER A 170      44.530   7.078  13.892  1.00 23.02           N  
ANISOU 1363  N   SER A 170     3733   2269   2746   -205   -363   -399       N  
ATOM   1364  CA  SER A 170      43.293   6.331  14.104  1.00 32.09           C  
ANISOU 1364  CA  SER A 170     4929   3408   3855   -120   -313   -343       C  
ATOM   1365  C   SER A 170      42.360   6.977  15.142  1.00 39.35           C  
ANISOU 1365  C   SER A 170     5971   4265   4716    -87   -279   -360       C  
ATOM   1366  O   SER A 170      41.136   7.006  14.966  1.00 37.61           O  
ANISOU 1366  O   SER A 170     5791   4003   4495    -43   -203   -313       O  
ATOM   1367  CB  SER A 170      43.568   4.871  14.445  1.00 25.28           C  
ANISOU 1367  CB  SER A 170     4033   2619   2952    -63   -353   -320       C  
ATOM   1368  OG  SER A 170      42.329   4.218  14.661  1.00 34.74           O  
ANISOU 1368  OG  SER A 170     5279   3795   4125      8   -291   -269       O  
ATOM   1369  N   PHE A 171      42.930   7.514  16.214  1.00 37.39           N  
ANISOU 1369  N   PHE A 171     5779   4010   4416   -106   -336   -430       N  
ATOM   1370  CA  PHE A 171      42.093   8.136  17.232  1.00 32.06           C  
ANISOU 1370  CA  PHE A 171     5229   3275   3679    -67   -305   -447       C  
ATOM   1371  C   PHE A 171      41.607   9.503  16.815  1.00 29.32           C  
ANISOU 1371  C   PHE A 171     4932   2842   3367   -112   -244   -455       C  
ATOM   1372  O   PHE A 171      40.476   9.874  17.115  1.00 27.12           O  
ANISOU 1372  O   PHE A 171     4738   2509   3058    -63   -177   -428       O  
ATOM   1373  CB  PHE A 171      42.814   8.211  18.570  1.00 29.95           C  
ANISOU 1373  CB  PHE A 171     5016   3032   3332    -57   -391   -523       C  
ATOM   1374  CG  PHE A 171      43.019   6.864  19.197  1.00 25.91           C  
ANISOU 1374  CG  PHE A 171     4493   2594   2757     22   -431   -504       C  
ATOM   1375  CD1 PHE A 171      41.920   6.067  19.503  1.00 23.59           C  
ANISOU 1375  CD1 PHE A 171     4251   2287   2427    111   -363   -436       C  
ATOM   1376  CD2 PHE A 171      44.303   6.377  19.441  1.00 22.44           C  
ANISOU 1376  CD2 PHE A 171     3991   2238   2299     10   -530   -553       C  
ATOM   1377  CE1 PHE A 171      42.076   4.799  20.046  1.00 25.08           C  
ANISOU 1377  CE1 PHE A 171     4440   2531   2560    187   -383   -412       C  
ATOM   1378  CE2 PHE A 171      44.477   5.103  20.010  1.00 28.03           C  
ANISOU 1378  CE2 PHE A 171     4699   3011   2939     98   -559   -530       C  
ATOM   1379  CZ  PHE A 171      43.359   4.319  20.312  1.00 27.63           C  
ANISOU 1379  CZ  PHE A 171     4712   2934   2851    186   -481   -457       C  
ATOM   1380  N   VAL A 172      42.472  10.221  16.106  1.00 25.16           N  
ANISOU 1380  N   VAL A 172     4351   2302   2905   -200   -260   -490       N  
ATOM   1381  CA  VAL A 172      42.233  11.589  15.671  1.00 29.96           C  
ANISOU 1381  CA  VAL A 172     5010   2822   3550   -251   -200   -504       C  
ATOM   1382  C   VAL A 172      41.120  11.609  14.614  1.00 27.32           C  
ANISOU 1382  C   VAL A 172     4671   2459   3250   -205   -101   -421       C  
ATOM   1383  O   VAL A 172      40.218  12.433  14.676  1.00 30.05           O  
ANISOU 1383  O   VAL A 172     5104   2735   3578   -179    -31   -407       O  
ATOM   1384  CB  VAL A 172      43.516  12.151  15.058  1.00 36.37           C  
ANISOU 1384  CB  VAL A 172     5748   3634   4436   -357   -233   -553       C  
ATOM   1385  CG1 VAL A 172      43.234  13.437  14.355  1.00 41.26           C  
ANISOU 1385  CG1 VAL A 172     6414   4156   5106   -402   -147   -548       C  
ATOM   1386  CG2 VAL A 172      44.588  12.328  16.127  1.00 29.29           C  
ANISOU 1386  CG2 VAL A 172     4855   2764   3510   -408   -334   -653       C  
ATOM   1387  N   ASP A 173      41.234  10.700  13.642  1.00 15.72           N  
ANISOU 1387  N   ASP A 173     3098   1049   1827   -192    -99   -370       N  
ATOM   1388  CA  ASP A 173      40.187  10.348  12.671  1.00 29.87           C  
ANISOU 1388  CA  ASP A 173     4863   2844   3644   -133    -27   -295       C  
ATOM   1389  C   ASP A 173      38.816  10.069  13.309  1.00 37.63           C  
ANISOU 1389  C   ASP A 173     5913   3814   4572    -49     19   -264       C  
ATOM   1390  O   ASP A 173      37.829  10.744  13.002  1.00 42.08           O  
ANISOU 1390  O   ASP A 173     6524   4330   5133    -14     93   -238       O  
ATOM   1391  CB  ASP A 173      40.611   9.092  11.870  1.00 18.15           C  
ANISOU 1391  CB  ASP A 173     3261   1440   2197   -123    -59   -259       C  
ATOM   1392  CG  ASP A 173      41.619   9.396  10.745  1.00 33.75           C  
ANISOU 1392  CG  ASP A 173     5157   3423   4242   -183    -66   -260       C  
ATOM   1393  OD1 ASP A 173      41.967   8.464   9.960  1.00 37.00           O  
ANISOU 1393  OD1 ASP A 173     5477   3895   4685   -171    -85   -226       O  
ATOM   1394  OD2 ASP A 173      42.046  10.565  10.628  1.00 40.37           O  
ANISOU 1394  OD2 ASP A 173     6029   4203   5105   -241    -44   -291       O  
ATOM   1395  N   ASP A 174      38.751   9.040  14.155  1.00 32.53           N  
ANISOU 1395  N   ASP A 174     5266   3211   3882    -12    -19   -262       N  
ATOM   1396  CA  ASP A 174      37.514   8.689  14.860  1.00 25.27           C  
ANISOU 1396  CA  ASP A 174     4407   2278   2915     64     30   -232       C  
ATOM   1397  C   ASP A 174      37.762   8.461  16.362  1.00 32.74           C  
ANISOU 1397  C   ASP A 174     5432   3225   3783     87    -13   -267       C  
ATOM   1398  O   ASP A 174      38.121   7.358  16.790  1.00 38.23           O  
ANISOU 1398  O   ASP A 174     6099   3972   4456    111    -52   -262       O  
ATOM   1399  CB  ASP A 174      36.864   7.464  14.235  1.00 28.15           C  
ANISOU 1399  CB  ASP A 174     4692   2692   3312    108     58   -177       C  
ATOM   1400  CG  ASP A 174      35.513   7.178  14.828  1.00 34.69           C  
ANISOU 1400  CG  ASP A 174     5569   3501   4109    178    125   -144       C  
ATOM   1401  OD1 ASP A 174      34.830   6.235  14.377  1.00 45.71           O  
ANISOU 1401  OD1 ASP A 174     6902   4927   5537    210    158   -105       O  
ATOM   1402  OD2 ASP A 174      35.132   7.923  15.742  1.00 34.34           O  
ANISOU 1402  OD2 ASP A 174     5626   3410   4012    200    148   -159       O  
ATOM   1403  N   PRO A 175      37.583   9.519  17.165  1.00 39.06           N  
ANISOU 1403  N   PRO A 175     6340   3966   4535     89     -3   -304       N  
ATOM   1404  CA  PRO A 175      37.914   9.514  18.594  1.00 36.73           C  
ANISOU 1404  CA  PRO A 175     6133   3667   4156    114    -52   -350       C  
ATOM   1405  C   PRO A 175      36.986   8.570  19.342  1.00 39.34           C  
ANISOU 1405  C   PRO A 175     6502   4009   4435    207     -9   -302       C  
ATOM   1406  O   PRO A 175      37.180   8.289  20.521  1.00 42.06           O  
ANISOU 1406  O   PRO A 175     6918   4360   4704    253    -41   -325       O  
ATOM   1407  CB  PRO A 175      37.653  10.975  19.015  1.00 34.01           C  
ANISOU 1407  CB  PRO A 175     5899   3241   3783     99    -26   -389       C  
ATOM   1408  CG  PRO A 175      37.680  11.775  17.744  1.00 28.79           C  
ANISOU 1408  CG  PRO A 175     5192   2547   3198     39     14   -378       C  
ATOM   1409  CD  PRO A 175      37.076  10.835  16.733  1.00 39.71           C  
ANISOU 1409  CD  PRO A 175     6476   3978   4633     72     57   -305       C  
ATOM   1410  N   THR A 176      35.977   8.090  18.627  1.00 38.84           N  
ANISOU 1410  N   THR A 176     6391   3950   4418    237     67   -236       N  
ATOM   1411  CA  THR A 176      35.006   7.142  19.140  1.00 37.25           C  
ANISOU 1411  CA  THR A 176     6205   3755   4194    313    127   -185       C  
ATOM   1412  C   THR A 176      35.726   5.827  19.515  1.00 35.30           C  
ANISOU 1412  C   THR A 176     5922   3562   3927    330     77   -183       C  
ATOM   1413  O   THR A 176      35.310   5.103  20.411  1.00 29.28           O  
ANISOU 1413  O   THR A 176     5213   2797   3115    398    109   -159       O  
ATOM   1414  CB  THR A 176      33.873   6.987  18.102  1.00 37.39           C  
ANISOU 1414  CB  THR A 176     6154   3772   4281    324    208   -131       C  
ATOM   1415  OG1 THR A 176      32.643   7.465  18.654  1.00 47.98           O  
ANISOU 1415  OG1 THR A 176     7570   5070   5591    384    291   -106       O  
ATOM   1416  CG2 THR A 176      33.746   5.593  17.558  1.00 26.45           C  
ANISOU 1416  CG2 THR A 176     4669   2435   2945    331    218    -95       C  
ATOM   1417  N   ARG A 177      36.866   5.596  18.876  1.00 30.64           N  
ANISOU 1417  N   ARG A 177     5252   3019   3372    272      2   -210       N  
ATOM   1418  CA  ARG A 177      37.683   4.420  19.100  1.00 28.48           C  
ANISOU 1418  CA  ARG A 177     4939   2804   3079    287    -51   -210       C  
ATOM   1419  C   ARG A 177      38.399   4.471  20.432  1.00 33.34           C  
ANISOU 1419  C   ARG A 177     5639   3431   3597    325   -115   -258       C  
ATOM   1420  O   ARG A 177      38.989   3.469  20.887  1.00 29.22           O  
ANISOU 1420  O   ARG A 177     5112   2958   3033    367   -153   -256       O  
ATOM   1421  CB  ARG A 177      38.722   4.280  17.983  1.00 34.62           C  
ANISOU 1421  CB  ARG A 177     5603   3630   3920    217   -113   -224       C  
ATOM   1422  CG  ARG A 177      38.175   3.722  16.673  1.00 29.88           C  
ANISOU 1422  CG  ARG A 177     4908   3041   3403    203    -63   -172       C  
ATOM   1423  CD  ARG A 177      39.076   4.102  15.466  1.00 38.61           C  
ANISOU 1423  CD  ARG A 177     5922   4175   4574    131   -109   -188       C  
ATOM   1424  NE  ARG A 177      38.333   3.938  14.223  1.00 45.91           N  
ANISOU 1424  NE  ARG A 177     6779   5096   5570    129    -54   -146       N  
ATOM   1425  CZ  ARG A 177      38.742   4.299  13.012  1.00 36.44           C  
ANISOU 1425  CZ  ARG A 177     5507   3908   4430     86    -64   -143       C  
ATOM   1426  NH1 ARG A 177      39.931   4.867  12.818  1.00 35.84           N  
ANISOU 1426  NH1 ARG A 177     5409   3845   4365     30   -120   -178       N  
ATOM   1427  NH2 ARG A 177      37.940   4.075  11.985  1.00 32.70           N  
ANISOU 1427  NH2 ARG A 177     4983   3436   4007    104    -14   -107       N  
ATOM   1428  N   ILE A 178      38.365   5.641  21.059  1.00 32.56           N  
ANISOU 1428  N   ILE A 178     5625   3290   3457    318   -129   -305       N  
ATOM   1429  CA  ILE A 178      38.959   5.774  22.378  1.00 20.09           C  
ANISOU 1429  CA  ILE A 178     4136   1720   1777    363   -193   -360       C  
ATOM   1430  C   ILE A 178      38.135   4.916  23.347  1.00 25.71           C  
ANISOU 1430  C   ILE A 178     4933   2419   2417    476   -128   -309       C  
ATOM   1431  O   ILE A 178      38.694   4.169  24.133  1.00 21.88           O  
ANISOU 1431  O   ILE A 178     4480   1975   1860    539   -170   -320       O  
ATOM   1432  CB  ILE A 178      39.041   7.237  22.824  1.00 28.56           C  
ANISOU 1432  CB  ILE A 178     5289   2741   2823    329   -218   -426       C  
ATOM   1433  CG1 ILE A 178      40.161   7.958  22.058  1.00 20.21           C  
ANISOU 1433  CG1 ILE A 178     4150   1701   1829    216   -293   -489       C  
ATOM   1434  CG2 ILE A 178      39.247   7.328  24.359  1.00 42.04           C  
ANISOU 1434  CG2 ILE A 178     7119   4446   4407    408   -263   -474       C  
ATOM   1435  CD1 ILE A 178      40.095   9.477  22.172  1.00 22.68           C  
ANISOU 1435  CD1 ILE A 178     4532   1941   2145    162   -289   -544       C  
ATOM   1436  N   LEU A 179      36.807   5.006  23.243  1.00 32.27           N  
ANISOU 1436  N   LEU A 179     5795   3195   3272    504    -20   -250       N  
ATOM   1437  CA  LEU A 179      35.884   4.265  24.101  1.00 23.95           C  
ANISOU 1437  CA  LEU A 179     4818   2115   2167    605     66   -195       C  
ATOM   1438  C   LEU A 179      35.827   2.802  23.659  1.00 30.20           C  
ANISOU 1438  C   LEU A 179     5534   2942   3000    621    102   -140       C  
ATOM   1439  O   LEU A 179      35.823   1.897  24.508  1.00 24.19           O  
ANISOU 1439  O   LEU A 179     4832   2185   2175    704    128   -115       O  
ATOM   1440  CB  LEU A 179      34.488   4.918  24.105  1.00 21.46           C  
ANISOU 1440  CB  LEU A 179     4548   1734   1871    624    172   -155       C  
ATOM   1441  CG  LEU A 179      34.413   6.349  24.706  1.00 34.87           C  
ANISOU 1441  CG  LEU A 179     6352   3385   3513    627    153   -202       C  
ATOM   1442  CD1 LEU A 179      33.100   7.064  24.443  1.00 27.19           C  
ANISOU 1442  CD1 LEU A 179     5404   2356   2570    639    255   -161       C  
ATOM   1443  CD2 LEU A 179      34.635   6.306  26.213  1.00 47.32           C  
ANISOU 1443  CD2 LEU A 179     8064   4951   4965    721    130   -228       C  
ATOM   1444  N   ARG A 180      35.828   2.578  22.339  1.00 27.46           N  
ANISOU 1444  N   ARG A 180     5064   2615   2754    547    105   -123       N  
ATOM   1445  CA  ARG A 180      35.808   1.224  21.774  1.00 26.64           C  
ANISOU 1445  CA  ARG A 180     4883   2540   2699    550    135    -78       C  
ATOM   1446  C   ARG A 180      37.009   0.382  22.186  1.00 30.76           C  
ANISOU 1446  C   ARG A 180     5408   3117   3162    581     60    -96       C  
ATOM   1447  O   ARG A 180      36.870  -0.834  22.426  1.00 31.88           O  
ANISOU 1447  O   ARG A 180     5560   3263   3291    635    107    -54       O  
ATOM   1448  CB  ARG A 180      35.717   1.260  20.252  1.00 26.94           C  
ANISOU 1448  CB  ARG A 180     4794   2596   2846    469    133    -69       C  
ATOM   1449  CG  ARG A 180      34.396   1.783  19.720  1.00 36.56           C  
ANISOU 1449  CG  ARG A 180     5992   3773   4126    456    219    -41       C  
ATOM   1450  CD  ARG A 180      34.465   2.038  18.249  1.00 33.01           C  
ANISOU 1450  CD  ARG A 180     5430   3347   3765    387    199    -45       C  
ATOM   1451  NE  ARG A 180      34.673   0.791  17.542  1.00 24.42           N  
ANISOU 1451  NE  ARG A 180     4255   2295   2728    375    198    -22       N  
ATOM   1452  CZ  ARG A 180      33.680   0.007  17.143  1.00 42.55           C  
ANISOU 1452  CZ  ARG A 180     6506   4582   5080    387    274     14       C  
ATOM   1453  NH1 ARG A 180      33.939  -1.143  16.510  1.00 42.93           N  
ANISOU 1453  NH1 ARG A 180     6483   4657   5172    374    269     28       N  
ATOM   1454  NH2 ARG A 180      32.425   0.387  17.367  1.00 35.99           N  
ANISOU 1454  NH2 ARG A 180     5696   3713   4264    411    356     32       N  
ATOM   1455  N   ALA A 181      38.180   1.017  22.270  1.00 29.28           N  
ANISOU 1455  N   ALA A 181     5212   2972   2942    549    -51   -161       N  
ATOM   1456  CA  ALA A 181      39.389   0.309  22.706  1.00 27.85           C  
ANISOU 1456  CA  ALA A 181     5029   2858   2696    586   -134   -187       C  
ATOM   1457  C   ALA A 181      39.226  -0.215  24.126  1.00 28.00           C  
ANISOU 1457  C   ALA A 181     5174   2866   2599    707   -108   -176       C  
ATOM   1458  O   ALA A 181      39.465  -1.383  24.407  1.00 31.66           O  
ANISOU 1458  O   ALA A 181     5651   3355   3024    775    -90   -143       O  
ATOM   1459  CB  ALA A 181      40.619   1.195  22.593  1.00 28.18           C  
ANISOU 1459  CB  ALA A 181     5030   2948   2728    524   -257   -269       C  
ATOM   1460  N   ILE A 182      38.788   0.645  25.028  1.00 30.11           N  
ANISOU 1460  N   ILE A 182     5543   3091   2806    743    -97   -200       N  
ATOM   1461  CA  ILE A 182      38.545   0.195  26.383  1.00 31.98           C  
ANISOU 1461  CA  ILE A 182     5912   3312   2928    871    -62   -184       C  
ATOM   1462  C   ILE A 182      37.530  -0.942  26.365  1.00 37.02           C  
ANISOU 1462  C   ILE A 182     6567   3905   3594    924     76    -92       C  
ATOM   1463  O   ILE A 182      37.748  -1.983  27.008  1.00 42.23           O  
ANISOU 1463  O   ILE A 182     7284   4577   4185   1019    102    -62       O  
ATOM   1464  CB  ILE A 182      38.066   1.365  27.270  1.00 40.24           C  
ANISOU 1464  CB  ILE A 182     7070   4308   3912    900    -58   -219       C  
ATOM   1465  CG1 ILE A 182      39.220   2.342  27.511  1.00 28.80           C  
ANISOU 1465  CG1 ILE A 182     5619   2905   2420    860   -201   -323       C  
ATOM   1466  CG2 ILE A 182      37.476   0.866  28.578  1.00 46.68           C  
ANISOU 1466  CG2 ILE A 182     8028   5087   4620   1043     17   -180       C  
ATOM   1467  CD1 ILE A 182      38.775   3.774  27.490  1.00 24.32           C  
ANISOU 1467  CD1 ILE A 182     5088   2280   1873    801   -200   -362       C  
ATOM   1468  N   ARG A 183      36.459  -0.778  25.621  1.00 34.51           N  
ANISOU 1468  N   ARG A 183     6199   3536   3378    864    165    -50       N  
ATOM   1469  CA  ARG A 183      35.449  -1.784  25.564  1.00 36.74           C  
ANISOU 1469  CA  ARG A 183     6480   3771   3707    896    302     28       C  
ATOM   1470  C   ARG A 183      35.908  -3.152  25.164  1.00 35.99           C  
ANISOU 1470  C   ARG A 183     6340   3707   3627    910    308     57       C  
ATOM   1471  O   ARG A 183      35.539  -4.090  25.783  1.00 31.08           O  
ANISOU 1471  O   ARG A 183     5788   3053   2968    993    397    107       O  
ATOM   1472  CB  ARG A 183      34.269  -1.375  24.723  1.00 41.82           C  
ANISOU 1472  CB  ARG A 183     7037   4380   4473    814    371     53       C  
ATOM   1473  CG  ARG A 183      33.428  -2.512  24.334  1.00 33.18           C  
ANISOU 1473  CG  ARG A 183     5927   3241   3440    835    508    122       C  
ATOM   1474  CD  ARG A 183      32.055  -2.124  24.014  1.00 38.48           C  
ANISOU 1474  CD  ARG A 183     6541   3876   4204    786    587    140       C  
ATOM   1475  NE  ARG A 183      32.045  -1.247  22.873  1.00 43.54           N  
ANISOU 1475  NE  ARG A 183     7040   4549   4955    690    557    128       N  
ATOM   1476  CZ  ARG A 183      31.817  -1.631  21.637  1.00 58.39           C  
ANISOU 1476  CZ  ARG A 183     8864   6448   6875    630    506     97       C  
ATOM   1477  NH1 ARG A 183      31.854  -0.774  20.654  1.00 42.27           N  
ANISOU 1477  NH1 ARG A 183     6701   4437   4924    559    482     89       N  
ATOM   1478  NH2 ARG A 183      31.549  -2.875  21.394  1.00 78.91           N  
ANISOU 1478  NH2 ARG A 183    11537   9030   9416    647    483     73       N  
ATOM   1479  N   PHE A 184      36.693  -3.265  24.107  1.00 43.46           N  
ANISOU 1479  N   PHE A 184     7172   4708   4631    831    226     32       N  
ATOM   1480  CA  PHE A 184      37.210  -4.572  23.687  1.00 33.64           C  
ANISOU 1480  CA  PHE A 184     5886   3495   3402    844    231     60       C  
ATOM   1481  C   PHE A 184      38.358  -4.991  24.608  1.00 34.74           C  
ANISOU 1481  C   PHE A 184     6098   3687   3414    938    159     38       C  
ATOM   1482  O   PHE A 184      38.646  -6.167  24.751  1.00 35.56           O  
ANISOU 1482  O   PHE A 184     6225   3800   3487   1000    191     73       O  
ATOM   1483  CB  PHE A 184      37.677  -4.555  22.223  1.00 19.64           C  
ANISOU 1483  CB  PHE A 184     3970   1764   1727    739    170     43       C  
ATOM   1484  CG  PHE A 184      36.558  -4.370  21.205  1.00 29.89           C  
ANISOU 1484  CG  PHE A 184     5189   3021   3148    662    241     66       C  
ATOM   1485  CD1 PHE A 184      36.541  -3.269  20.365  1.00 34.91           C  
ANISOU 1485  CD1 PHE A 184     5752   3670   3842    581    191     32       C  
ATOM   1486  CD2 PHE A 184      35.562  -5.313  21.053  1.00 37.43           C  
ANISOU 1486  CD2 PHE A 184     6138   3926   4159    673    357    116       C  
ATOM   1487  CE1 PHE A 184      35.534  -3.106  19.413  1.00 38.22           C  
ANISOU 1487  CE1 PHE A 184     6097   4063   4363    526    250     50       C  
ATOM   1488  CE2 PHE A 184      34.559  -5.150  20.105  1.00 41.60           C  
ANISOU 1488  CE2 PHE A 184     6581   4429   4797    605    411    125       C  
ATOM   1489  CZ  PHE A 184      34.549  -4.044  19.284  1.00 36.15           C  
ANISOU 1489  CZ  PHE A 184     5821   3763   4153    539    353     92       C  
ATOM   1490  N   GLU A 185      39.029  -4.023  25.216  1.00 41.60           N  
ANISOU 1490  N   GLU A 185     7005   4594   4208    952     58    -25       N  
ATOM   1491  CA  GLU A 185      40.025  -4.339  26.241  1.00 52.27           C  
ANISOU 1491  CA  GLU A 185     8433   6002   5424   1059    -14    -56       C  
ATOM   1492  C   GLU A 185      39.407  -5.116  27.405  1.00 46.16           C  
ANISOU 1492  C   GLU A 185     7802   5177   4559   1198     95      0       C  
ATOM   1493  O   GLU A 185      39.947  -6.127  27.830  1.00 41.61           O  
ANISOU 1493  O   GLU A 185     7272   4631   3908   1294    100     22       O  
ATOM   1494  CB  GLU A 185      40.688  -3.073  26.777  1.00 51.70           C  
ANISOU 1494  CB  GLU A 185     8383   5970   5292   1047   -134   -144       C  
ATOM   1495  CG  GLU A 185      42.181  -3.218  26.988  1.00 45.20           C  
ANISOU 1495  CG  GLU A 185     7527   5252   4394   1077   -272   -208       C  
ATOM   1496  CD  GLU A 185      42.745  -2.143  27.894  1.00 43.40           C  
ANISOU 1496  CD  GLU A 185     7355   5057   4079   1100   -379   -300       C  
ATOM   1497  OE1 GLU A 185      41.946  -1.367  28.479  1.00 44.48           O  
ANISOU 1497  OE1 GLU A 185     7579   5127   4196   1112   -336   -306       O  
ATOM   1498  OE2 GLU A 185      43.988  -2.081  28.034  1.00 43.16           O  
ANISOU 1498  OE2 GLU A 185     7280   5121   3999   1108   -506   -371       O  
ATOM   1499  N   GLN A 186      38.277  -4.654  27.926  1.00 39.98           N  
ANISOU 1499  N   GLN A 186     7095   4316   3780   1218    189     26       N  
ATOM   1500  CA  GLN A 186      37.650  -5.401  29.009  1.00 46.96           C  
ANISOU 1500  CA  GLN A 186     8115   5142   4584   1352    309     87       C  
ATOM   1501  C   GLN A 186      36.868  -6.613  28.496  1.00 41.60           C  
ANISOU 1501  C   GLN A 186     7410   4403   3992   1340    454    170       C  
ATOM   1502  O   GLN A 186      36.701  -7.584  29.225  1.00 46.95           O  
ANISOU 1502  O   GLN A 186     8187   5045   4605   1452    549    223       O  
ATOM   1503  CB  GLN A 186      36.741  -4.527  29.924  1.00 53.68           C  
ANISOU 1503  CB  GLN A 186     9074   5931   5390   1400    367     91       C  
ATOM   1504  CG  GLN A 186      37.257  -3.135  30.293  1.00 48.49           C  
ANISOU 1504  CG  GLN A 186     8438   5311   4676   1382    238      4       C  
ATOM   1505  CD  GLN A 186      38.680  -3.148  30.818  1.00 54.43           C  
ANISOU 1505  CD  GLN A 186     9213   6156   5313   1443     91    -69       C  
ATOM   1506  OE1 GLN A 186      39.058  -4.032  31.569  1.00 52.37           O  
ANISOU 1506  OE1 GLN A 186     9034   5917   4949   1573    107    -47       O  
ATOM   1507  NE2 GLN A 186      39.479  -2.159  30.416  1.00 55.55           N  
ANISOU 1507  NE2 GLN A 186     9279   6354   5473   1353    -49   -157       N  
ATOM   1508  N   ARG A 187      36.366  -6.562  27.267  1.00 44.41           N  
ANISOU 1508  N   ARG A 187     7638   4743   4491   1211    476    178       N  
ATOM   1509  CA  ARG A 187      35.512  -7.647  26.764  1.00 48.40           C  
ANISOU 1509  CA  ARG A 187     8113   5186   5091   1188    615    245       C  
ATOM   1510  C   ARG A 187      36.226  -8.996  26.542  1.00 61.21           C  
ANISOU 1510  C   ARG A 187     9733   6829   6696   1227    623    271       C  
ATOM   1511  O   ARG A 187      35.641 -10.054  26.766  1.00 69.62           O  
ANISOU 1511  O   ARG A 187    10848   7826   7777   1270    758    332       O  
ATOM   1512  CB  ARG A 187      34.774  -7.236  25.496  1.00 42.46           C  
ANISOU 1512  CB  ARG A 187     7222   4419   4490   1050    628    238       C  
ATOM   1513  CG  ARG A 187      34.151  -8.421  24.765  1.00 35.30           C  
ANISOU 1513  CG  ARG A 187     6254   3468   3689   1008    735    284       C  
ATOM   1514  CD  ARG A 187      34.179  -8.167  23.288  1.00 44.99           C  
ANISOU 1514  CD  ARG A 187     7329   4732   5035    882    672    253       C  
ATOM   1515  NE  ARG A 187      32.931  -7.631  22.743  1.00 51.76           N  
ANISOU 1515  NE  ARG A 187     8116   5552   5998    810    736    256       N  
ATOM   1516  CZ  ARG A 187      32.224  -8.234  21.784  1.00 63.08           C  
ANISOU 1516  CZ  ARG A 187     9451   6963   7552    740    796    266       C  
ATOM   1517  NH1 ARG A 187      31.106  -7.671  21.323  1.00 69.06           N  
ANISOU 1517  NH1 ARG A 187    10141   7702   8398    685    844    261       N  
ATOM   1518  NH2 ARG A 187      32.640  -9.400  21.270  1.00 48.25           N  
ANISOU 1518  NH2 ARG A 187     7542   5087   5704    728    806    278       N  
ATOM   1519  N   PHE A 188      37.470  -8.951  26.075  1.00 59.31           N  
ANISOU 1519  N   PHE A 188     9432   6677   6425   1208    486    227       N  
ATOM   1520  CA  PHE A 188      38.375 -10.093  26.150  1.00 54.85           C  
ANISOU 1520  CA  PHE A 188     8895   6150   5797   1282    472    245       C  
ATOM   1521  C   PHE A 188      39.284  -9.679  27.271  1.00 55.62           C  
ANISOU 1521  C   PHE A 188     9085   6311   5737   1396    378    206       C  
ATOM   1522  O   PHE A 188      39.084  -8.613  27.845  1.00 70.98           O  
ANISOU 1522  O   PHE A 188    11066   8257   7647   1401    340    169       O  
ATOM   1523  CB  PHE A 188      39.146 -10.201  24.846  1.00 52.69           C  
ANISOU 1523  CB  PHE A 188     8480   5942   5596   1184    375    217       C  
ATOM   1524  CG  PHE A 188      38.299  -9.945  23.648  1.00 47.70           C  
ANISOU 1524  CG  PHE A 188     7733   5272   5119   1048    411    220       C  
ATOM   1525  CD1 PHE A 188      37.489 -10.947  23.122  1.00 52.73           C  
ANISOU 1525  CD1 PHE A 188     8350   5841   5845   1020    532    269       C  
ATOM   1526  CD2 PHE A 188      38.283  -8.696  23.052  1.00 48.54           C  
ANISOU 1526  CD2 PHE A 188     7753   5409   5282    953    328    172       C  
ATOM   1527  CE1 PHE A 188      36.684 -10.705  22.014  1.00 44.93           C  
ANISOU 1527  CE1 PHE A 188     7250   4827   4996    903    557    263       C  
ATOM   1528  CE2 PHE A 188      37.493  -8.448  21.959  1.00 36.09           C  
ANISOU 1528  CE2 PHE A 188     6075   3803   3835    846    360    174       C  
ATOM   1529  CZ  PHE A 188      36.689  -9.457  21.435  1.00 41.78           C  
ANISOU 1529  CZ  PHE A 188     6769   4467   4640    823    470    217       C  
ATOM   1530  N   ASP A 189      40.287 -10.450  27.628  1.00 44.21           N  
ANISOU 1530  N   ASP A 189     7682   4925   4190   1496    335    208       N  
ATOM   1531  CA  ASP A 189      41.101  -9.894  28.713  1.00 58.94           C  
ANISOU 1531  CA  ASP A 189     9627   6863   5906   1605    230    155       C  
ATOM   1532  C   ASP A 189      42.325  -9.216  28.118  1.00 54.18           C  
ANISOU 1532  C   ASP A 189     8903   6375   5307   1533     49     72       C  
ATOM   1533  O   ASP A 189      43.469  -9.650  28.308  1.00 48.49           O  
ANISOU 1533  O   ASP A 189     8178   5747   4498   1607    -40     46       O  
ATOM   1534  CB  ASP A 189      41.465 -10.931  29.784  1.00 70.41           C  
ANISOU 1534  CB  ASP A 189    11224   8319   7208   1794    283    195       C  
ATOM   1535  CG  ASP A 189      42.023 -10.291  31.057  1.00 75.65           C  
ANISOU 1535  CG  ASP A 189    11991   9043   7710   1922    193    139       C  
ATOM   1536  OD1 ASP A 189      42.198  -9.052  31.088  1.00 75.18           O  
ANISOU 1536  OD1 ASP A 189    11884   9021   7660   1854     83     63       O  
ATOM   1537  OD2 ASP A 189      42.297 -11.033  32.025  1.00 84.13           O  
ANISOU 1537  OD2 ASP A 189    13196  10125   8643   2097    233    169       O  
ATOM   1538  N   PHE A 190      42.087  -8.148  27.372  1.00 53.29           N  
ANISOU 1538  N   PHE A 190     8688   6258   5301   1389     -2     31       N  
ATOM   1539  CA  PHE A 190      43.170  -7.622  26.559  1.00 53.49           C  
ANISOU 1539  CA  PHE A 190     8581   6378   5366   1298   -146    -34       C  
ATOM   1540  C   PHE A 190      43.797  -6.392  27.124  1.00 47.91           C  
ANISOU 1540  C   PHE A 190     7874   5727   4601   1289   -274   -127       C  
ATOM   1541  O   PHE A 190      43.236  -5.753  28.001  1.00 54.54           O  
ANISOU 1541  O   PHE A 190     8810   6523   5390   1330   -252   -143       O  
ATOM   1542  CB  PHE A 190      42.733  -7.415  25.118  1.00 53.57           C  
ANISOU 1542  CB  PHE A 190     8461   6356   5537   1145   -122    -18       C  
ATOM   1543  CG  PHE A 190      42.714  -8.678  24.333  1.00 52.12           C  
ANISOU 1543  CG  PHE A 190     8237   6163   5404   1143    -58     43       C  
ATOM   1544  CD1 PHE A 190      42.597  -8.665  22.957  1.00 45.04           C  
ANISOU 1544  CD1 PHE A 190     7216   5262   4636   1024    -60     51       C  
ATOM   1545  CD2 PHE A 190      42.837  -9.890  24.983  1.00 39.18           C  
ANISOU 1545  CD2 PHE A 190     6693   4516   3677   1271      6     91       C  
ATOM   1546  CE1 PHE A 190      42.578  -9.837  22.261  1.00 44.91           C  
ANISOU 1546  CE1 PHE A 190     7170   5232   4660   1026     -3    101       C  
ATOM   1547  CE2 PHE A 190      42.824 -11.058  24.293  1.00 36.19           C  
ANISOU 1547  CE2 PHE A 190     6289   4119   3341   1271     70    145       C  
ATOM   1548  CZ  PHE A 190      42.693 -11.045  22.932  1.00 43.85           C  
ANISOU 1548  CZ  PHE A 190     7134   5085   4441   1146     63    148       C  
ATOM   1549  N   ARG A 191      44.990  -6.090  26.633  1.00 46.83           N  
ANISOU 1549  N   ARG A 191     7630   5689   4473   1237   -407   -190       N  
ATOM   1550  CA  ARG A 191      45.666  -4.856  27.001  1.00 51.77           C  
ANISOU 1550  CA  ARG A 191     8231   6370   5071   1197   -536   -292       C  
ATOM   1551  C   ARG A 191      45.885  -4.011  25.743  1.00 44.48           C  
ANISOU 1551  C   ARG A 191     7162   5451   4288   1024   -583   -324       C  
ATOM   1552  O   ARG A 191      46.088  -4.538  24.641  1.00 49.03           O  
ANISOU 1552  O   ARG A 191     7639   6043   4949    964   -568   -286       O  
ATOM   1553  CB  ARG A 191      46.996  -5.152  27.702  1.00 52.76           C  
ANISOU 1553  CB  ARG A 191     8358   6619   5070   1298   -660   -354       C  
ATOM   1554  CG  ARG A 191      48.087  -5.691  26.747  1.00 65.94           C  
ANISOU 1554  CG  ARG A 191     9888   8383   6783   1254   -730   -360       C  
ATOM   1555  CD  ARG A 191      49.389  -5.991  27.484  1.00 74.37           C  
ANISOU 1555  CD  ARG A 191    10952   9586   7721   1366   -855   -425       C  
ATOM   1556  NE  ARG A 191      50.556  -5.479  26.768  1.00 78.01           N  
ANISOU 1556  NE  ARG A 191    11252  10146   8241   1264   -982   -499       N  
ATOM   1557  CZ  ARG A 191      51.367  -6.217  26.015  1.00 79.84           C  
ANISOU 1557  CZ  ARG A 191    11384  10456   8497   1262  -1011   -476       C  
ATOM   1558  NH1 ARG A 191      52.402  -5.643  25.406  1.00 71.97           N  
ANISOU 1558  NH1 ARG A 191    10239   9546   7561   1164  -1121   -546       N  
ATOM   1559  NH2 ARG A 191      51.147  -7.525  25.873  1.00 81.83           N  
ANISOU 1559  NH2 ARG A 191    11686  10694   8712   1357   -924   -383       N  
ATOM   1560  N   ILE A 192      45.834  -2.699  25.911  1.00 36.54           N  
ANISOU 1560  N   ILE A 192     6154   4427   3304    951   -633   -392       N  
ATOM   1561  CA  ILE A 192      46.164  -1.773  24.837  1.00 41.54           C  
ANISOU 1561  CA  ILE A 192     6663   5064   4058    797   -680   -432       C  
ATOM   1562  C   ILE A 192      47.677  -1.618  24.722  1.00 42.59           C  
ANISOU 1562  C   ILE A 192     6696   5313   4175    770   -820   -512       C  
ATOM   1563  O   ILE A 192      48.337  -1.113  25.633  1.00 39.08           O  
ANISOU 1563  O   ILE A 192     6280   4921   3647    806   -917   -599       O  
ATOM   1564  CB  ILE A 192      45.473  -0.412  25.043  1.00 38.99           C  
ANISOU 1564  CB  ILE A 192     6386   4662   3766    729   -665   -470       C  
ATOM   1565  CG1 ILE A 192      43.954  -0.585  24.883  1.00 43.33           C  
ANISOU 1565  CG1 ILE A 192     7001   5106   4357    740   -521   -384       C  
ATOM   1566  CG2 ILE A 192      46.026   0.643  24.054  1.00 31.74           C  
ANISOU 1566  CG2 ILE A 192     5350   3752   2958    578   -723   -525       C  
ATOM   1567  CD1 ILE A 192      43.093   0.490  25.555  1.00 39.97           C  
ANISOU 1567  CD1 ILE A 192     6675   4601   3909    740   -485   -405       C  
ATOM   1568  N   GLU A 193      48.236  -2.073  23.609  1.00 40.89           N  
ANISOU 1568  N   GLU A 193     6358   5141   4038    711   -831   -486       N  
ATOM   1569  CA  GLU A 193      49.687  -2.087  23.492  1.00 34.74           C  
ANISOU 1569  CA  GLU A 193     5475   4481   3244    697   -954   -552       C  
ATOM   1570  C   GLU A 193      50.220  -0.677  23.596  1.00 32.80           C  
ANISOU 1570  C   GLU A 193     5181   4246   3036    592  -1041   -658       C  
ATOM   1571  O   GLU A 193      49.525   0.293  23.266  1.00 43.14           O  
ANISOU 1571  O   GLU A 193     6506   5464   4421    500   -994   -663       O  
ATOM   1572  CB  GLU A 193      50.132  -2.769  22.193  1.00 39.83           C  
ANISOU 1572  CB  GLU A 193     5998   5162   3974    649   -939   -498       C  
ATOM   1573  CG  GLU A 193      49.765  -2.051  20.903  1.00 31.81           C  
ANISOU 1573  CG  GLU A 193     4899   4083   3105    506   -894   -478       C  
ATOM   1574  CD  GLU A 193      50.853  -1.091  20.465  1.00 47.95           C  
ANISOU 1574  CD  GLU A 193     6824   6182   5211    398   -987   -559       C  
ATOM   1575  OE1 GLU A 193      51.983  -1.178  21.019  1.00 49.61           O  
ANISOU 1575  OE1 GLU A 193     6991   6497   5360    431  -1092   -627       O  
ATOM   1576  OE2 GLU A 193      50.591  -0.269  19.557  1.00 53.20           O  
ANISOU 1576  OE2 GLU A 193     7438   6788   5987    284   -951   -555       O  
ATOM   1577  N   GLU A 194      51.440  -0.563  24.058  1.00 34.39           N  
ANISOU 1577  N   GLU A 194     5320   4559   3187    607  -1166   -747       N  
ATOM   1578  CA  GLU A 194      52.094   0.692  24.316  1.00 42.70           C  
ANISOU 1578  CA  GLU A 194     6338   5629   4257    521  -1261   -869       C  
ATOM   1579  C   GLU A 194      51.870   1.811  23.362  1.00 39.51           C  
ANISOU 1579  C   GLU A 194     5864   5145   4002    349  -1225   -880       C  
ATOM   1580  O   GLU A 194      51.432   2.862  23.734  1.00 41.37           O  
ANISOU 1580  O   GLU A 194     6161   5304   4254    292  -1218   -931       O  
ATOM   1581  CB  GLU A 194      53.573   0.462  24.408  1.00 55.18           C  
ANISOU 1581  CB  GLU A 194     7813   7358   5794    541  -1400   -958       C  
ATOM   1582  CG  GLU A 194      54.279   1.352  25.334  1.00 74.16           C  
ANISOU 1582  CG  GLU A 194    10179   9788   8210    456  -1508  -1101       C  
ATOM   1583  CD  GLU A 194      55.666   0.843  25.626  1.00 93.54           C  
ANISOU 1583  CD  GLU A 194    12474  12387  10679    424  -1634  -1188       C  
ATOM   1584  OE1 GLU A 194      56.496   0.844  24.711  1.00107.00           O  
ANISOU 1584  OE1 GLU A 194    14109  14108  12437    313  -1714  -1307       O  
ATOM   1585  OE2 GLU A 194      55.918   0.426  26.768  1.00 88.75           O  
ANISOU 1585  OE2 GLU A 194    11811  11876  10034    507  -1649  -1139       O  
ATOM   1586  N   THR A 195      52.247   1.599  22.129  1.00 39.09           N  
ANISOU 1586  N   THR A 195     5690   5109   4053    275  -1201   -834       N  
ATOM   1587  CA  THR A 195      52.154   2.648  21.116  1.00 39.85           C  
ANISOU 1587  CA  THR A 195     5721   5135   4287    124  -1162   -842       C  
ATOM   1588  C   THR A 195      50.730   3.174  20.970  1.00 28.26           C  
ANISOU 1588  C   THR A 195     4358   3531   2848    106  -1050   -787       C  
ATOM   1589  O   THR A 195      50.495   4.392  21.009  1.00 35.73           O  
ANISOU 1589  O   THR A 195     5333   4405   3838     22  -1040   -837       O  
ATOM   1590  CB  THR A 195      52.655   2.165  19.772  1.00 43.95           C  
ANISOU 1590  CB  THR A 195     6110   5689   4900     73  -1138   -783       C  
ATOM   1591  OG1 THR A 195      53.983   1.651  19.938  1.00 34.58           O  
ANISOU 1591  OG1 THR A 195     4822   4636   3680     99  -1240   -831       O  
ATOM   1592  CG2 THR A 195      52.634   3.327  18.763  1.00 41.33           C  
ANISOU 1592  CG2 THR A 195     5717   5283   4703    -74  -1095   -794       C  
ATOM   1593  N   THR A 196      49.770   2.267  20.830  1.00 23.67           N  
ANISOU 1593  N   THR A 196     3837   2914   2241    186   -963   -687       N  
ATOM   1594  CA  THR A 196      48.403   2.730  20.672  1.00 28.41           C  
ANISOU 1594  CA  THR A 196     4524   3397   2872    174   -858   -636       C  
ATOM   1595  C   THR A 196      47.926   3.445  21.925  1.00 33.53           C  
ANISOU 1595  C   THR A 196     5300   3999   3440    211   -869   -691       C  
ATOM   1596  O   THR A 196      47.202   4.439  21.824  1.00 33.21           O  
ANISOU 1596  O   THR A 196     5311   3869   3439    157   -818   -696       O  
ATOM   1597  CB  THR A 196      47.391   1.689  20.059  1.00 39.88           C  
ANISOU 1597  CB  THR A 196     5995   4814   4345    228   -752   -520       C  
ATOM   1598  OG1 THR A 196      46.221   1.599  20.875  1.00 45.11           O  
ANISOU 1598  OG1 THR A 196     6784   5409   4946    302   -683   -489       O  
ATOM   1599  CG2 THR A 196      47.990   0.348  19.900  1.00 33.40           C  
ANISOU 1599  CG2 THR A 196     5124   4076   3492    296   -775   -482       C  
ATOM   1600  N   GLU A 197      48.416   3.009  23.086  1.00 29.54           N  
ANISOU 1600  N   GLU A 197     4845   3559   2819    306   -943   -737       N  
ATOM   1601  CA  GLU A 197      48.077   3.670  24.354  1.00 33.36           C  
ANISOU 1601  CA  GLU A 197     5456   4009   3212    355   -967   -799       C  
ATOM   1602  C   GLU A 197      48.519   5.142  24.370  1.00 39.91           C  
ANISOU 1602  C   GLU A 197     6267   4808   4090    237  -1024   -903       C  
ATOM   1603  O   GLU A 197      47.751   6.050  24.732  1.00 36.73           O  
ANISOU 1603  O   GLU A 197     5961   4312   3682    220   -981   -918       O  
ATOM   1604  CB  GLU A 197      48.654   2.918  25.570  1.00 32.75           C  
ANISOU 1604  CB  GLU A 197     5432   4020   2991    492  -1047   -837       C  
ATOM   1605  CG  GLU A 197      48.926   3.849  26.757  1.00 40.62           C  
ANISOU 1605  CG  GLU A 197     6510   5020   3905    511  -1133   -952       C  
ATOM   1606  CD  GLU A 197      48.813   3.177  28.124  1.00 56.90           C  
ANISOU 1606  CD  GLU A 197     8698   7120   5803    687  -1157   -957       C  
ATOM   1607  OE1 GLU A 197      48.931   1.938  28.208  1.00 55.78           O  
ANISOU 1607  OE1 GLU A 197     8556   7033   5604    793  -1138   -894       O  
ATOM   1608  OE2 GLU A 197      48.614   3.900  29.126  1.00 59.60           O  
ANISOU 1608  OE2 GLU A 197     9146   7432   6066    725  -1191  -1026       O  
ATOM   1609  N   ARG A 198      49.747   5.388  24.001  1.00 31.18           N  
ANISOU 1609  N   ARG A 198     5037   3776   3033    157  -1116   -976       N  
ATOM   1610  CA  ARG A 198      50.175   6.722  23.833  1.00 35.69           C  
ANISOU 1610  CA  ARG A 198     5578   4310   3673     27  -1156  -1074       C  
ATOM   1611  C   ARG A 198      49.336   7.510  22.876  1.00 35.34           C  
ANISOU 1611  C   ARG A 198     5549   4143   3736    -64  -1039  -1013       C  
ATOM   1612  O   ARG A 198      49.029   8.629  23.124  1.00 47.12           O  
ANISOU 1612  O   ARG A 198     7118   5548   5237   -114  -1018  -1059       O  
ATOM   1613  CB  ARG A 198      51.613   6.757  23.418  1.00 44.16           C  
ANISOU 1613  CB  ARG A 198     6493   5483   4804    -54  -1255  -1149       C  
ATOM   1614  CG  ARG A 198      52.039   8.063  22.943  1.00 51.39           C  
ANISOU 1614  CG  ARG A 198     7362   6352   5813   -206  -1282  -1247       C  
ATOM   1615  CD  ARG A 198      53.467   8.343  23.216  1.00 70.77           C  
ANISOU 1615  CD  ARG A 198     9675   8923   8292   -265  -1407  -1356       C  
ATOM   1616  NE  ARG A 198      53.624   9.700  23.716  1.00 93.37           N  
ANISOU 1616  NE  ARG A 198    12516  11733  11229   -406  -1441  -1476       N  
ATOM   1617  CZ  ARG A 198      54.784  10.287  23.974  1.00107.02           C  
ANISOU 1617  CZ  ARG A 198    14304  13468  12891   -405  -1532  -1606       C  
ATOM   1618  NH1 ARG A 198      54.812  11.526  24.436  1.00106.62           N  
ANISOU 1618  NH1 ARG A 198    14230  13356  12923   -548  -1551  -1714       N  
ATOM   1619  NH2 ARG A 198      55.918   9.639  23.764  1.00114.40           N  
ANISOU 1619  NH2 ARG A 198    15326  14466  13675   -258  -1601  -1629       N  
ATOM   1620  N   LEU A 199      48.992   6.921  21.753  1.00 49.26           N  
ANISOU 1620  N   LEU A 199     7248   5898   5570    -74   -961   -911       N  
ATOM   1621  CA  LEU A 199      48.122   7.582  20.779  1.00 42.59           C  
ANISOU 1621  CA  LEU A 199     6416   4949   4816   -140   -850   -851       C  
ATOM   1622  C   LEU A 199      46.764   7.974  21.389  1.00 38.15           C  
ANISOU 1622  C   LEU A 199     6003   4293   4200    -81   -773   -818       C  
ATOM   1623  O   LEU A 199      46.236   9.063  21.145  1.00 36.32           O  
ANISOU 1623  O   LEU A 199     5821   3969   4011   -139   -718   -827       O  
ATOM   1624  CB  LEU A 199      47.927   6.673  19.563  1.00 36.41           C  
ANISOU 1624  CB  LEU A 199     5547   4189   4098   -132   -789   -747       C  
ATOM   1625  CG  LEU A 199      48.810   6.844  18.312  1.00 37.20           C  
ANISOU 1625  CG  LEU A 199     5509   4316   4309   -230   -796   -746       C  
ATOM   1626  CD1 LEU A 199      49.967   7.800  18.524  1.00 30.18           C  
ANISOU 1626  CD1 LEU A 199     4565   3445   3456   -332   -874   -858       C  
ATOM   1627  CD2 LEU A 199      49.310   5.500  17.774  1.00 26.12           C  
ANISOU 1627  CD2 LEU A 199     4012   3007   2906   -181   -817   -689       C  
ATOM   1628  N   LEU A 200      46.216   7.069  22.186  1.00 36.11           N  
ANISOU 1628  N   LEU A 200     5817   4058   3847     41   -764   -778       N  
ATOM   1629  CA  LEU A 200      44.945   7.266  22.875  1.00 30.09           C  
ANISOU 1629  CA  LEU A 200     5192   3218   3023    115   -689   -741       C  
ATOM   1630  C   LEU A 200      45.022   8.487  23.796  1.00 39.64           C  
ANISOU 1630  C   LEU A 200     6499   4377   4184     94   -730   -835       C  
ATOM   1631  O   LEU A 200      44.141   9.355  23.772  1.00 38.73           O  
ANISOU 1631  O   LEU A 200     6466   4168   4083     77   -657   -821       O  
ATOM   1632  CB  LEU A 200      44.596   5.980  23.659  1.00 30.70           C  
ANISOU 1632  CB  LEU A 200     5322   3338   3003    251   -679   -690       C  
ATOM   1633  CG  LEU A 200      43.189   5.779  24.254  1.00 39.03           C  
ANISOU 1633  CG  LEU A 200     6502   4324   4005    345   -576   -621       C  
ATOM   1634  CD1 LEU A 200      42.685   4.344  24.166  1.00 34.51           C  
ANISOU 1634  CD1 LEU A 200     5921   3776   3417    432   -512   -527       C  
ATOM   1635  CD2 LEU A 200      43.128   6.262  25.699  1.00 26.70           C  
ANISOU 1635  CD2 LEU A 200     5076   2745   2325    420   -615   -682       C  
ATOM   1636  N   LYS A 201      46.096   8.560  24.582  1.00 41.98           N  
ANISOU 1636  N   LYS A 201     6786   4740   4424     96   -849   -936       N  
ATOM   1637  CA  LYS A 201      46.285   9.626  25.564  1.00 41.18           C  
ANISOU 1637  CA  LYS A 201     6779   4603   4266     82   -907  -1044       C  
ATOM   1638  C   LYS A 201      46.410  10.993  24.916  1.00 40.81           C  
ANISOU 1638  C   LYS A 201     6714   4473   4318    -59   -886  -1094       C  
ATOM   1639  O   LYS A 201      45.903  11.996  25.444  1.00 39.57           O  
ANISOU 1639  O   LYS A 201     6673   4230   4133    -67   -863  -1134       O  
ATOM   1640  CB  LYS A 201      47.546   9.382  26.397  1.00 42.99           C  
ANISOU 1640  CB  LYS A 201     6971   4939   4426    105  -1054  -1155       C  
ATOM   1641  CG  LYS A 201      47.494   8.179  27.320  1.00 52.09           C  
ANISOU 1641  CG  LYS A 201     8176   6167   5449    267  -1084  -1125       C  
ATOM   1642  CD  LYS A 201      48.554   8.311  28.412  1.00 47.57           C  
ANISOU 1642  CD  LYS A 201     7612   5682   4779    307  -1232  -1258       C  
ATOM   1643  CE  LYS A 201      48.787   7.012  29.172  1.00 45.61           C  
ANISOU 1643  CE  LYS A 201     7389   5534   4405    471  -1272  -1231       C  
ATOM   1644  NZ  LYS A 201      49.663   7.265  30.353  1.00 57.68           N  
ANISOU 1644  NZ  LYS A 201     8951   7144   5821    531  -1417  -1368       N  
ATOM   1645  N   GLN A 202      47.128  11.038  23.798  1.00 35.16           N  
ANISOU 1645  N   GLN A 202     5861   3783   3715   -165   -891  -1093       N  
ATOM   1646  CA  GLN A 202      47.319  12.295  23.063  1.00 43.96           C  
ANISOU 1646  CA  GLN A 202     6954   4815   4935   -302   -855  -1132       C  
ATOM   1647  C   GLN A 202      45.964  12.832  22.646  1.00 35.55           C  
ANISOU 1647  C   GLN A 202     5986   3635   3886   -284   -723  -1048       C  
ATOM   1648  O   GLN A 202      45.614  13.980  22.940  1.00 35.98           O  
ANISOU 1648  O   GLN A 202     6139   3595   3938   -321   -692  -1092       O  
ATOM   1649  CB  GLN A 202      48.211  12.091  21.828  1.00 44.38           C  
ANISOU 1649  CB  GLN A 202     6842   4914   5106   -399   -860  -1119       C  
ATOM   1650  CG  GLN A 202      49.651  11.722  22.154  1.00 55.63           C  
ANISOU 1650  CG  GLN A 202     8152   6454   6529   -433   -991  -1213       C  
ATOM   1651  CD  GLN A 202      50.542  11.577  20.913  1.00 65.64           C  
ANISOU 1651  CD  GLN A 202     9257   7764   7919   -529   -987  -1196       C  
ATOM   1652  OE1 GLN A 202      51.768  11.561  21.022  1.00 74.81           O  
ANISOU 1652  OE1 GLN A 202    10311   9006   9106   -587  -1082  -1282       O  
ATOM   1653  NE2 GLN A 202      49.931  11.471  19.737  1.00 58.28           N  
ANISOU 1653  NE2 GLN A 202     8303   6781   7058   -541   -877  -1088       N  
ATOM   1654  N   ALA A 203      45.200  11.966  21.981  1.00 34.56           N  
ANISOU 1654  N   ALA A 203     5832   3524   3775   -222   -646   -930       N  
ATOM   1655  CA  ALA A 203      43.873  12.303  21.472  1.00 31.64           C  
ANISOU 1655  CA  ALA A 203     5530   3068   3424   -193   -521   -842       C  
ATOM   1656  C   ALA A 203      42.989  12.803  22.603  1.00 26.37           C  
ANISOU 1656  C   ALA A 203     5022   2337   2660   -118   -496   -855       C  
ATOM   1657  O   ALA A 203      42.303  13.799  22.464  1.00 27.92           O  
ANISOU 1657  O   ALA A 203     5300   2440   2868   -136   -424   -848       O  
ATOM   1658  CB  ALA A 203      43.235  11.081  20.806  1.00 19.17           C  
ANISOU 1658  CB  ALA A 203     3891   1534   1860   -125   -465   -729       C  
ATOM   1659  N   VAL A 204      43.018  12.103  23.732  1.00 35.04           N  
ANISOU 1659  N   VAL A 204     6171   3486   3656    -25   -552   -872       N  
ATOM   1660  CA  VAL A 204      42.203  12.503  24.875  1.00 33.65           C  
ANISOU 1660  CA  VAL A 204     6153   3255   3378     62   -528   -882       C  
ATOM   1661  C   VAL A 204      42.608  13.880  25.338  1.00 33.12           C  
ANISOU 1661  C   VAL A 204     6162   3120   3301     -8   -568   -990       C  
ATOM   1662  O   VAL A 204      41.777  14.775  25.433  1.00 43.88           O  
ANISOU 1662  O   VAL A 204     7633   4388   4653     -1   -493   -976       O  
ATOM   1663  CB  VAL A 204      42.280  11.502  26.036  1.00 29.93           C  
ANISOU 1663  CB  VAL A 204     5728   2852   2792    184   -582   -885       C  
ATOM   1664  CG1 VAL A 204      41.730  12.124  27.355  1.00 23.34           C  
ANISOU 1664  CG1 VAL A 204     5066   1961   1843    267   -581   -925       C  
ATOM   1665  CG2 VAL A 204      41.536  10.229  25.665  1.00 27.62           C  
ANISOU 1665  CG2 VAL A 204     5397   2591   2505    263   -505   -766       C  
ATOM   1666  N   GLU A 205      43.892  14.069  25.590  1.00 32.51           N  
ANISOU 1666  N   GLU A 205     6027   3092   3233    -78   -684  -1100       N  
ATOM   1667  CA  GLU A 205      44.319  15.349  26.136  1.00 26.68           C  
ANISOU 1667  CA  GLU A 205     5365   2289   2485   -149   -730  -1219       C  
ATOM   1668  C   GLU A 205      44.508  16.473  25.111  1.00 41.50           C  
ANISOU 1668  C   GLU A 205     7209   4079   4482   -290   -673  -1238       C  
ATOM   1669  O   GLU A 205      44.917  17.570  25.484  1.00 43.92           O  
ANISOU 1669  O   GLU A 205     7573   4319   4795   -366   -704  -1342       O  
ATOM   1670  CB  GLU A 205      45.577  15.182  26.984  1.00 40.00           C  
ANISOU 1670  CB  GLU A 205     7012   4063   4124   -162   -884  -1349       C  
ATOM   1671  CG  GLU A 205      46.882  15.038  26.224  1.00 55.34           C  
ANISOU 1671  CG  GLU A 205     8779   6078   6169   -282   -955  -1404       C  
ATOM   1672  CD  GLU A 205      48.079  15.081  27.174  1.00 71.13           C  
ANISOU 1672  CD  GLU A 205    10749   8162   8116   -295  -1113  -1554       C  
ATOM   1673  OE1 GLU A 205      48.342  14.066  27.860  1.00 65.81           O  
ANISOU 1673  OE1 GLU A 205    10063   7595   7348   -183  -1188  -1555       O  
ATOM   1674  OE2 GLU A 205      48.752  16.136  27.244  1.00 81.99           O  
ANISOU 1674  OE2 GLU A 205    12114   9495   9543   -415  -1160  -1674       O  
ATOM   1675  N   GLU A 206      44.217  16.228  23.833  1.00 43.64           N  
ANISOU 1675  N   GLU A 206     7394   4343   4846   -323   -587  -1142       N  
ATOM   1676  CA  GLU A 206      44.237  17.329  22.860  1.00 38.20           C  
ANISOU 1676  CA  GLU A 206     6699   3558   4259   -433   -509  -1144       C  
ATOM   1677  C   GLU A 206      42.855  17.769  22.370  1.00 37.83           C  
ANISOU 1677  C   GLU A 206     6744   3420   4208   -377   -370  -1042       C  
ATOM   1678  O   GLU A 206      42.766  18.543  21.418  1.00 43.24           O  
ANISOU 1678  O   GLU A 206     7424   4033   4973   -445   -289  -1020       O  
ATOM   1679  CB  GLU A 206      45.124  17.013  21.654  1.00 37.31           C  
ANISOU 1679  CB  GLU A 206     6419   3494   4264   -527   -515  -1129       C  
ATOM   1680  CG  GLU A 206      46.613  16.927  21.932  1.00 44.51           C  
ANISOU 1680  CG  GLU A 206     7225   4479   5208   -616   -639  -1244       C  
ATOM   1681  CD  GLU A 206      47.386  16.300  20.761  1.00 56.66           C  
ANISOU 1681  CD  GLU A 206     8591   6089   6850   -676   -641  -1203       C  
ATOM   1682  OE1 GLU A 206      48.543  15.869  20.967  1.00 63.99           O  
ANISOU 1682  OE1 GLU A 206     9409   7110   7793   -718   -746  -1274       O  
ATOM   1683  OE2 GLU A 206      46.836  16.230  19.633  1.00 54.79           O  
ANISOU 1683  OE2 GLU A 206     8327   5817   6672   -672   -538  -1100       O  
ATOM   1684  N   GLY A 207      41.786  17.267  22.989  1.00 39.18           N  
ANISOU 1684  N   GLY A 207     6998   3599   4288   -250   -336   -977       N  
ATOM   1685  CA  GLY A 207      40.438  17.767  22.729  1.00 24.52           C  
ANISOU 1685  CA  GLY A 207     5240   1663   2415   -186   -212   -895       C  
ATOM   1686  C   GLY A 207      39.608  16.982  21.737  1.00 21.19           C  
ANISOU 1686  C   GLY A 207     4741   1278   2034   -132   -130   -771       C  
ATOM   1687  O   GLY A 207      38.559  17.417  21.276  1.00 44.80           O  
ANISOU 1687  O   GLY A 207     7783   4213   5027    -89    -26   -704       O  
ATOM   1688  N   TYR A 208      40.050  15.789  21.424  1.00 29.65           N  
ANISOU 1688  N   TYR A 208     5688   2447   3131   -126   -178   -744       N  
ATOM   1689  CA  TYR A 208      39.412  15.087  20.321  1.00 41.23           C  
ANISOU 1689  CA  TYR A 208     7066   3946   4653    -96   -108   -642       C  
ATOM   1690  C   TYR A 208      37.998  14.570  20.603  1.00 40.12           C  
ANISOU 1690  C   TYR A 208     6978   3806   4460     22    -32   -557       C  
ATOM   1691  O   TYR A 208      37.127  14.622  19.721  1.00 39.58           O  
ANISOU 1691  O   TYR A 208     6885   3722   4430     48     55   -485       O  
ATOM   1692  CB  TYR A 208      40.371  14.078  19.682  1.00 33.49           C  
ANISOU 1692  CB  TYR A 208     5934   3058   3731   -139   -172   -638       C  
ATOM   1693  CG  TYR A 208      41.361  14.803  18.788  1.00 31.81           C  
ANISOU 1693  CG  TYR A 208     5654   2823   3610   -257   -184   -681       C  
ATOM   1694  CD1 TYR A 208      40.938  15.419  17.610  1.00 30.91           C  
ANISOU 1694  CD1 TYR A 208     5528   2655   3563   -281    -91   -630       C  
ATOM   1695  CD2 TYR A 208      42.701  14.912  19.135  1.00 30.86           C  
ANISOU 1695  CD2 TYR A 208     5484   2734   3506   -339   -282   -773       C  
ATOM   1696  CE1 TYR A 208      41.835  16.096  16.785  1.00 34.43           C  
ANISOU 1696  CE1 TYR A 208     5919   3069   4093   -384    -85   -663       C  
ATOM   1697  CE2 TYR A 208      43.606  15.590  18.322  1.00 40.32           C  
ANISOU 1697  CE2 TYR A 208     6616   3907   4798   -453   -281   -812       C  
ATOM   1698  CZ  TYR A 208      43.166  16.180  17.146  1.00 45.23           C  
ANISOU 1698  CZ  TYR A 208     7233   4464   5487   -475   -176   -753       C  
ATOM   1699  OH  TYR A 208      44.055  16.863  16.340  1.00 49.73           O  
ANISOU 1699  OH  TYR A 208     7745   4998   6151   -583   -159   -785       O  
ATOM   1700  N   LEU A 209      37.770  14.149  21.845  1.00 32.65           N  
ANISOU 1700  N   LEU A 209     6106   2875   3424     95    -62   -570       N  
ATOM   1701  CA  LEU A 209      36.448  13.744  22.300  1.00 28.38           C  
ANISOU 1701  CA  LEU A 209     5628   2325   2831    206     17   -497       C  
ATOM   1702  C   LEU A 209      35.434  14.891  22.116  1.00 43.98           C  
ANISOU 1702  C   LEU A 209     7698   4216   4798    229    113   -471       C  
ATOM   1703  O   LEU A 209      34.384  14.706  21.492  1.00 47.01           O  
ANISOU 1703  O   LEU A 209     8053   4600   5208    277    201   -394       O  
ATOM   1704  CB  LEU A 209      36.518  13.273  23.760  1.00 35.53           C  
ANISOU 1704  CB  LEU A 209     6620   3248   3632    282    -30   -525       C  
ATOM   1705  CG  LEU A 209      36.732  11.783  24.130  1.00 29.26           C  
ANISOU 1705  CG  LEU A 209     5767   2537   2815    338    -65   -496       C  
ATOM   1706  CD1 LEU A 209      37.135  10.928  22.973  1.00 33.15           C  
ANISOU 1706  CD1 LEU A 209     6106   3092   3398    286    -75   -460       C  
ATOM   1707  CD2 LEU A 209      37.709  11.609  25.286  1.00 26.14           C  
ANISOU 1707  CD2 LEU A 209     5423   2175   2334    359   -172   -576       C  
ATOM   1708  N   GLU A 210      35.758  16.080  22.628  1.00 38.52           N  
ANISOU 1708  N   GLU A 210     7116   3451   4070    197     97   -540       N  
ATOM   1709  CA  GLU A 210      34.897  17.240  22.425  1.00 39.33           C  
ANISOU 1709  CA  GLU A 210     7317   3465   4160    219    190   -519       C  
ATOM   1710  C   GLU A 210      34.682  17.534  20.962  1.00 44.23           C  
ANISOU 1710  C   GLU A 210     7858   4079   4870    180    255   -471       C  
ATOM   1711  O   GLU A 210      33.636  18.066  20.586  1.00 45.19           O  
ANISOU 1711  O   GLU A 210     8027   4161   4983    237    351   -417       O  
ATOM   1712  CB  GLU A 210      35.465  18.499  23.071  1.00 28.91           C  
ANISOU 1712  CB  GLU A 210     6122   2060   2801    169    158   -612       C  
ATOM   1713  CG  GLU A 210      36.907  18.392  23.393  1.00 50.49           C  
ANISOU 1713  CG  GLU A 210     8810   4822   5552     77     37   -711       C  
ATOM   1714  CD  GLU A 210      37.103  17.585  24.644  1.00 53.53           C  
ANISOU 1714  CD  GLU A 210     9225   5264   5850    144    -41   -741       C  
ATOM   1715  OE1 GLU A 210      38.148  16.919  24.803  1.00 50.92           O  
ANISOU 1715  OE1 GLU A 210     8810   5006   5531    103   -142   -792       O  
ATOM   1716  OE2 GLU A 210      36.174  17.616  25.459  1.00 54.46           O  
ANISOU 1716  OE2 GLU A 210     9455   5356   5883    248      5   -707       O  
ATOM   1717  N   ARG A 211      35.689  17.244  20.146  1.00 39.88           N  
ANISOU 1717  N   ARG A 211     5473   4214   5467    770    895    601       N  
ATOM   1718  CA  ARG A 211      35.574  17.534  18.723  1.00 39.24           C  
ANISOU 1718  CA  ARG A 211     5387   4172   5352    968    980    753       C  
ATOM   1719  C   ARG A 211      34.621  16.567  18.045  1.00 36.52           C  
ANISOU 1719  C   ARG A 211     5070   3977   4828   1101    878    737       C  
ATOM   1720  O   ARG A 211      34.112  16.876  16.995  1.00 34.52           O  
ANISOU 1720  O   ARG A 211     4811   3782   4522   1278    941    832       O  
ATOM   1721  CB  ARG A 211      36.930  17.515  18.026  1.00 37.33           C  
ANISOU 1721  CB  ARG A 211     5103   3936   5145   1013   1032    865       C  
ATOM   1722  CG  ARG A 211      37.654  18.864  18.078  1.00 37.46           C  
ANISOU 1722  CG  ARG A 211     5072   3795   5367    970   1202    950       C  
ATOM   1723  CD  ARG A 211      39.165  18.691  17.927  1.00 43.43           C  
ANISOU 1723  CD  ARG A 211     5779   4544   6177    928   1220   1003       C  
ATOM   1724  NE  ARG A 211      39.750  18.995  16.604  1.00 52.47           N  
ANISOU 1724  NE  ARG A 211     6884   5722   7330   1102   1329   1203       N  
ATOM   1725  CZ  ARG A 211      39.091  19.263  15.470  1.00 58.33           C  
ANISOU 1725  CZ  ARG A 211     7627   6530   8006   1313   1402   1342       C  
ATOM   1726  NH1 ARG A 211      39.785  19.526  14.365  1.00 50.84           N  
ANISOU 1726  NH1 ARG A 211     6626   5625   7067   1469   1505   1530       N  
ATOM   1727  NH2 ARG A 211      37.757  19.265  15.412  1.00 60.03           N  
ANISOU 1727  NH2 ARG A 211     7884   6786   8137   1384   1376   1300       N  
ATOM   1728  N   THR A 212      34.372  15.401  18.646  1.00 40.35           N  
ANISOU 1728  N   THR A 212     5576   4529   5228   1021    727    616       N  
ATOM   1729  CA  THR A 212      33.382  14.488  18.078  1.00 31.87           C  
ANISOU 1729  CA  THR A 212     4516   3579   4015   1131    628    574       C  
ATOM   1730  C   THR A 212      31.963  14.813  18.554  1.00 37.21           C  
ANISOU 1730  C   THR A 212     5217   4243   4678   1114    622    508       C  
ATOM   1731  O   THR A 212      31.790  15.529  19.518  1.00 39.70           O  
ANISOU 1731  O   THR A 212     5544   4460   5081    993    664    472       O  
ATOM   1732  CB  THR A 212      33.796  12.951  18.160  1.00 45.15           C  
ANISOU 1732  CB  THR A 212     6196   5343   5617   1099    476    498       C  
ATOM   1733  OG1 THR A 212      32.714  12.145  18.649  1.00 41.81           O  
ANISOU 1733  OG1 THR A 212     5788   4957   5142   1057    367    385       O  
ATOM   1734  CG2 THR A 212      34.998  12.745  19.019  1.00 28.50           C  
ANISOU 1734  CG2 THR A 212     4080   3176   3573    947    459    480       C  
ATOM   1735  N   THR A 213      30.949  14.338  17.834  1.00 40.38           N  
ANISOU 1735  N   THR A 213     5619   4755   4970   1245    572    486       N  
ATOM   1736  CA  THR A 213      29.573  14.695  18.157  1.00 36.40           C  
ANISOU 1736  CA  THR A 213     5133   4254   4443   1248    575    435       C  
ATOM   1737  C   THR A 213      29.065  13.855  19.318  1.00 43.16           C  
ANISOU 1737  C   THR A 213     6001   5101   5295   1091    452    306       C  
ATOM   1738  O   THR A 213      29.484  12.708  19.500  1.00 37.03           O  
ANISOU 1738  O   THR A 213     5214   4358   4497   1039    346    253       O  
ATOM   1739  CB  THR A 213      28.620  14.535  16.938  1.00 47.41           C  
ANISOU 1739  CB  THR A 213     6509   5789   5715   1458    571    451       C  
ATOM   1740  OG1 THR A 213      28.427  13.144  16.621  1.00 34.74           O  
ANISOU 1740  OG1 THR A 213     4881   4292   4025   1485    426    354       O  
ATOM   1741  CG2 THR A 213      29.177  15.260  15.732  1.00 47.18           C  
ANISOU 1741  CG2 THR A 213     6453   5800   5673   1642    695    600       C  
ATOM   1742  N   GLY A 214      28.166  14.442  20.100  1.00 43.64           N  
ANISOU 1742  N   GLY A 214     6082   5120   5381   1026    473    266       N  
ATOM   1743  CA  GLY A 214      27.537  13.759  21.212  1.00 41.13           C  
ANISOU 1743  CA  GLY A 214     5766   4807   5056    896    373    164       C  
ATOM   1744  C   GLY A 214      26.949  12.389  20.924  1.00 44.98           C  
ANISOU 1744  C   GLY A 214     6233   5386   5470    925    247     97       C  
ATOM   1745  O   GLY A 214      27.306  11.398  21.578  1.00 42.96           O  
ANISOU 1745  O   GLY A 214     5965   5125   5233    822    160     51       O  
ATOM   1746  N   PRO A 215      26.026  12.319  19.955  1.00 45.43           N  
ANISOU 1746  N   PRO A 215     6279   5531   5451   1069    241     87       N  
ATOM   1747  CA  PRO A 215      25.304  11.076  19.635  1.00 41.86           C  
ANISOU 1747  CA  PRO A 215     5793   5164   4949   1102    123     -4       C  
ATOM   1748  C   PRO A 215      26.218   9.895  19.303  1.00 40.01           C  
ANISOU 1748  C   PRO A 215     5533   4944   4725   1097     40    -28       C  
ATOM   1749  O   PRO A 215      25.879   8.745  19.611  1.00 36.46           O  
ANISOU 1749  O   PRO A 215     5056   4503   4295   1040    -63   -109       O  
ATOM   1750  CB  PRO A 215      24.481  11.464  18.398  1.00 47.24           C  
ANISOU 1750  CB  PRO A 215     6454   5956   5539   1297    158      1       C  
ATOM   1751  CG  PRO A 215      24.256  12.938  18.548  1.00 41.53           C  
ANISOU 1751  CG  PRO A 215     5768   5187   4826   1322    290     86       C  
ATOM   1752  CD  PRO A 215      25.494  13.480  19.217  1.00 38.53           C  
ANISOU 1752  CD  PRO A 215     5415   4680   4543   1207    352    153       C  
ATOM   1753  N   ARG A 216      27.355  10.166  18.671  1.00 33.03           N  
ANISOU 1753  N   ARG A 216     4654   4060   3837   1161     88     45       N  
ATOM   1754  CA  ARG A 216      28.246   9.088  18.293  1.00 38.91           C  
ANISOU 1754  CA  ARG A 216     5376   4827   4580   1173     12     24       C  
ATOM   1755  C   ARG A 216      28.865   8.551  19.575  1.00 40.40           C  
ANISOU 1755  C   ARG A 216     5578   4927   4844    986    -29     12       C  
ATOM   1756  O   ARG A 216      28.885   7.355  19.832  1.00 46.81           O  
ANISOU 1756  O   ARG A 216     6369   5738   5679    937   -124    -48       O  
ATOM   1757  CB  ARG A 216      29.295   9.584  17.289  1.00 38.49           C  
ANISOU 1757  CB  ARG A 216     5320   4811   4494   1299     82    120       C  
ATOM   1758  CG  ARG A 216      28.689  10.230  16.008  1.00 27.66           C  
ANISOU 1758  CG  ARG A 216     3923   3552   3034   1514    144    159       C  
ATOM   1759  CD  ARG A 216      29.751  10.380  14.881  1.00 30.24           C  
ANISOU 1759  CD  ARG A 216     4225   3950   3314   1668    191    255       C  
ATOM   1760  NE  ARG A 216      30.365   9.078  14.612  1.00 44.29           N  
ANISOU 1760  NE  ARG A 216     5978   5777   5075   1673     71    182       N  
ATOM   1761  CZ  ARG A 216      31.669   8.824  14.608  1.00 46.45           C  
ANISOU 1761  CZ  ARG A 216     6256   6023   5371   1643     70    237       C  
ATOM   1762  NH1 ARG A 216      32.079   7.577  14.368  1.00 51.04           N  
ANISOU 1762  NH1 ARG A 216     6812   6647   5932   1655    -45    156       N  
ATOM   1763  NH2 ARG A 216      32.560   9.798  14.822  1.00 34.57           N  
ANISOU 1763  NH2 ARG A 216     4774   4446   3916   1603    185    366       N  
ATOM   1764  N   LEU A 217      29.329   9.471  20.401  1.00 41.78           N  
ANISOU 1764  N   LEU A 217     5781   5029   5064    889     49     66       N  
ATOM   1765  CA  LEU A 217      29.912   9.160  21.686  1.00 31.54           C  
ANISOU 1765  CA  LEU A 217     4487   3675   3822    726     25     56       C  
ATOM   1766  C   LEU A 217      28.902   8.428  22.593  1.00 37.59           C  
ANISOU 1766  C   LEU A 217     5237   4444   4602    641    -49    -10       C  
ATOM   1767  O   LEU A 217      29.242   7.439  23.256  1.00 26.56           O  
ANISOU 1767  O   LEU A 217     3821   3038   3233    560   -112    -25       O  
ATOM   1768  CB  LEU A 217      30.352  10.469  22.334  1.00 28.56           C  
ANISOU 1768  CB  LEU A 217     4126   3235   3491    658    126     97       C  
ATOM   1769  CG  LEU A 217      31.801  10.972  22.408  1.00 24.26           C  
ANISOU 1769  CG  LEU A 217     3579   2648   2992    620    187    150       C  
ATOM   1770  CD1 LEU A 217      32.720  10.314  21.439  1.00 23.73           C  
ANISOU 1770  CD1 LEU A 217     3503   2620   2892    703    162    192       C  
ATOM   1771  CD2 LEU A 217      31.836  12.495  22.280  1.00 28.80           C  
ANISOU 1771  CD2 LEU A 217     4161   3157   3623    638    314    195       C  
ATOM   1772  N   ARG A 218      27.657   8.902  22.617  1.00 32.31           N  
ANISOU 1772  N   ARG A 218     4572   3790   3916    666    -35    -37       N  
ATOM   1773  CA  ARG A 218      26.677   8.317  23.515  1.00 31.90           C  
ANISOU 1773  CA  ARG A 218     4498   3742   3881    585    -92    -84       C  
ATOM   1774  C   ARG A 218      26.525   6.863  23.132  1.00 40.58           C  
ANISOU 1774  C   ARG A 218     5560   4859   5001    603   -188   -130       C  
ATOM   1775  O   ARG A 218      26.464   5.956  23.981  1.00 47.60           O  
ANISOU 1775  O   ARG A 218     6419   5725   5941    510   -240   -138       O  
ATOM   1776  CB  ARG A 218      25.334   9.054  23.421  1.00 35.23           C  
ANISOU 1776  CB  ARG A 218     4926   4189   4269    629    -63   -107       C  
ATOM   1777  CG  ARG A 218      24.154   8.281  23.968  1.00 31.71           C  
ANISOU 1777  CG  ARG A 218     4445   3767   3836    582   -132   -159       C  
ATOM   1778  CD  ARG A 218      22.914   9.139  24.198  1.00 29.15           C  
ANISOU 1778  CD  ARG A 218     4131   3472   3474    599    -96   -174       C  
ATOM   1779  NE  ARG A 218      21.807   8.284  24.611  1.00 37.10           N  
ANISOU 1779  NE  ARG A 218     5091   4505   4499    560   -165   -220       N  
ATOM   1780  CZ  ARG A 218      20.581   8.712  24.906  1.00 34.99           C  
ANISOU 1780  CZ  ARG A 218     4817   4276   4200    564   -157   -241       C  
ATOM   1781  NH1 ARG A 218      19.648   7.854  25.271  1.00 36.92           N  
ANISOU 1781  NH1 ARG A 218     5009   4541   4478    523   -220   -276       N  
ATOM   1782  NH2 ARG A 218      20.282   9.989  24.827  1.00 28.70           N  
ANISOU 1782  NH2 ARG A 218     4063   3493   3350    612    -82   -222       N  
ATOM   1783  N   GLN A 219      26.491   6.628  21.834  1.00 30.14           N  
ANISOU 1783  N   GLN A 219     4228   3580   3645    732   -209   -160       N  
ATOM   1784  CA  GLN A 219      26.212   5.301  21.386  1.00 23.68           C  
ANISOU 1784  CA  GLN A 219     3362   2776   2860    759   -303   -234       C  
ATOM   1785  C   GLN A 219      27.336   4.339  21.747  1.00 25.32           C  
ANISOU 1785  C   GLN A 219     3562   2937   3122    695   -344   -212       C  
ATOM   1786  O   GLN A 219      27.077   3.174  22.062  1.00 26.98           O  
ANISOU 1786  O   GLN A 219     3731   3113   3407    647   -411   -254       O  
ATOM   1787  CB  GLN A 219      25.936   5.270  19.889  1.00 32.45           C  
ANISOU 1787  CB  GLN A 219     4449   3972   3910    931   -323   -292       C  
ATOM   1788  CG  GLN A 219      25.590   3.863  19.445  1.00 47.76           C  
ANISOU 1788  CG  GLN A 219     6323   5921   5904    956   -430   -403       C  
ATOM   1789  CD  GLN A 219      26.287   3.469  18.162  1.00 71.68           C  
ANISOU 1789  CD  GLN A 219     9329   9020   8888   1102   -466   -444       C  
ATOM   1790  OE1 GLN A 219      27.310   2.765  18.181  1.00 81.58           O  
ANISOU 1790  OE1 GLN A 219    10583  10236  10178   1079   -499   -430       O  
ATOM   1791  NE2 GLN A 219      25.745   3.927  17.031  1.00 69.62           N  
ANISOU 1791  NE2 GLN A 219     9040   8876   8535   1267   -458   -490       N  
ATOM   1792  N   GLU A 220      28.581   4.805  21.703  1.00 28.47           N  
ANISOU 1792  N   GLU A 220     3995   3331   3493    696   -298   -145       N  
ATOM   1793  CA  GLU A 220      29.685   3.947  22.120  1.00 35.66           C  
ANISOU 1793  CA  GLU A 220     4900   4209   4442    637   -330   -118       C  
ATOM   1794  C   GLU A 220      29.624   3.772  23.644  1.00 35.86           C  
ANISOU 1794  C   GLU A 220     4918   4195   4514    493   -321    -82       C  
ATOM   1795  O   GLU A 220      30.065   2.762  24.201  1.00 31.73           O  
ANISOU 1795  O   GLU A 220     4370   3647   4039    437   -359    -66       O  
ATOM   1796  CB  GLU A 220      31.033   4.516  21.671  1.00 40.26           C  
ANISOU 1796  CB  GLU A 220     5512   4808   4978    677   -281    -55       C  
ATOM   1797  CG  GLU A 220      31.294   4.407  20.152  1.00 55.47           C  
ANISOU 1797  CG  GLU A 220     7429   6794   6852    839   -299    -75       C  
ATOM   1798  CD  GLU A 220      31.187   2.978  19.594  1.00 57.85           C  
ANISOU 1798  CD  GLU A 220     7689   7108   7182    892   -404   -159       C  
ATOM   1799  OE1 GLU A 220      31.617   2.034  20.277  1.00 53.69           O  
ANISOU 1799  OE1 GLU A 220     7152   6529   6717    806   -446   -158       O  
ATOM   1800  OE2 GLU A 220      30.670   2.797  18.467  1.00 57.59           O  
ANISOU 1800  OE2 GLU A 220     7625   7143   7113   1028   -441   -229       O  
ATOM   1801  N   LEU A 221      29.043   4.760  24.311  1.00 38.26           N  
ANISOU 1801  N   LEU A 221     5235   4504   4799    446   -269    -68       N  
ATOM   1802  CA  LEU A 221      28.849   4.678  25.747  1.00 36.37           C  
ANISOU 1802  CA  LEU A 221     4975   4259   4585    332   -261    -41       C  
ATOM   1803  C   LEU A 221      27.814   3.635  26.114  1.00 36.83           C  
ANISOU 1803  C   LEU A 221     4987   4303   4705    304   -317    -61       C  
ATOM   1804  O   LEU A 221      28.065   2.814  26.985  1.00 37.18           O  
ANISOU 1804  O   LEU A 221     4996   4337   4795    239   -334    -19       O  
ATOM   1805  CB  LEU A 221      28.462   6.036  26.323  1.00 38.61           C  
ANISOU 1805  CB  LEU A 221     5279   4558   4834    300   -195    -38       C  
ATOM   1806  CG  LEU A 221      29.419   6.698  27.323  1.00 47.79           C  
ANISOU 1806  CG  LEU A 221     6441   5733   5985    224   -147    -11       C  
ATOM   1807  CD1 LEU A 221      30.782   6.031  27.380  1.00 43.78           C  
ANISOU 1807  CD1 LEU A 221     5923   5230   5482    206   -161     21       C  
ATOM   1808  CD2 LEU A 221      29.557   8.199  27.033  1.00 50.30           C  
ANISOU 1808  CD2 LEU A 221     6792   6031   6290    245    -68    -22       C  
ATOM   1809  N   GLU A 222      26.649   3.660  25.471  1.00 34.11           N  
ANISOU 1809  N   GLU A 222     4632   3962   4366    356   -339   -119       N  
ATOM   1810  CA  GLU A 222      25.638   2.659  25.802  1.00 33.63           C  
ANISOU 1810  CA  GLU A 222     4514   3878   4387    322   -389   -143       C  
ATOM   1811  C   GLU A 222      26.237   1.278  25.565  1.00 35.50           C  
ANISOU 1811  C   GLU A 222     4715   4063   4712    321   -442   -148       C  
ATOM   1812  O   GLU A 222      26.016   0.329  26.324  1.00 47.79           O  
ANISOU 1812  O   GLU A 222     6220   5576   6361    257   -459   -112       O  
ATOM   1813  CB  GLU A 222      24.355   2.876  24.992  1.00 34.96           C  
ANISOU 1813  CB  GLU A 222     4667   4070   4545    390   -411   -226       C  
ATOM   1814  CG  GLU A 222      23.527   4.062  25.475  1.00 39.83           C  
ANISOU 1814  CG  GLU A 222     5308   4730   5094    377   -359   -212       C  
ATOM   1815  CD  GLU A 222      22.868   4.851  24.354  1.00 51.70           C  
ANISOU 1815  CD  GLU A 222     6834   6284   6527    490   -345   -271       C  
ATOM   1816  OE1 GLU A 222      23.350   4.789  23.192  1.00 61.17           O  
ANISOU 1816  OE1 GLU A 222     8042   7503   7697    591   -356   -306       O  
ATOM   1817  OE2 GLU A 222      21.870   5.557  24.641  1.00 50.41           O  
ANISOU 1817  OE2 GLU A 222     6675   6154   6324    490   -318   -278       O  
ATOM   1818  N   LYS A 223      27.010   1.159  24.516  1.00 28.45           N  
ANISOU 1818  N   LYS A 223     3845   3173   3790    399   -460   -180       N  
ATOM   1819  CA  LYS A 223      27.609  -0.093  24.146  1.00 40.67           C  
ANISOU 1819  CA  LYS A 223     5359   4672   5420    418   -517   -207       C  
ATOM   1820  C   LYS A 223      28.570  -0.605  25.184  1.00 34.79           C  
ANISOU 1820  C   LYS A 223     4612   3899   4706    336   -495   -105       C  
ATOM   1821  O   LYS A 223      28.503  -1.738  25.561  1.00 39.81           O  
ANISOU 1821  O   LYS A 223     5199   4472   5454    300   -521    -87       O  
ATOM   1822  CB  LYS A 223      28.339   0.081  22.837  1.00 49.77           C  
ANISOU 1822  CB  LYS A 223     6535   5863   6514    540   -544   -266       C  
ATOM   1823  CG  LYS A 223      27.945  -0.806  21.742  1.00 63.74           C  
ANISOU 1823  CG  LYS A 223     8247   7600   8371    603   -627   -371       C  
ATOM   1824  CD  LYS A 223      28.190  -0.031  20.509  1.00 76.55           C  
ANISOU 1824  CD  LYS A 223     9859   9307   9921    751   -660   -480       C  
ATOM   1825  CE  LYS A 223      27.977  -0.803  19.269  1.00 83.92           C  
ANISOU 1825  CE  LYS A 223    10843  10314  10729    844   -626   -430       C  
ATOM   1826  NZ  LYS A 223      28.542  -0.025  18.135  1.00 84.57           N  
ANISOU 1826  NZ  LYS A 223    10900  10503  10731   1016   -655   -522       N  
ATOM   1827  N   ILE A 224      29.432   0.251  25.680  1.00 25.51           N  
ANISOU 1827  N   ILE A 224     3483   2772   3439    313   -441    -41       N  
ATOM   1828  CA  ILE A 224      30.192  -0.076  26.891  1.00 32.81           C  
ANISOU 1828  CA  ILE A 224     4392   3706   4369    238   -412     51       C  
ATOM   1829  C   ILE A 224      29.284  -0.572  28.034  1.00 39.87           C  
ANISOU 1829  C   ILE A 224     5229   4588   5333    169   -404    101       C  
ATOM   1830  O   ILE A 224      29.579  -1.579  28.681  1.00 32.43           O  
ANISOU 1830  O   ILE A 224     4243   3620   4459    140   -404    169       O  
ATOM   1831  CB  ILE A 224      30.992   1.116  27.417  1.00 41.31           C  
ANISOU 1831  CB  ILE A 224     5505   4849   5343    210   -353     87       C  
ATOM   1832  CG1 ILE A 224      32.360   1.167  26.740  1.00 43.23           C  
ANISOU 1832  CG1 ILE A 224     5780   5104   5541    253   -352     92       C  
ATOM   1833  CG2 ILE A 224      31.180   0.988  28.925  1.00 44.56           C  
ANISOU 1833  CG2 ILE A 224     5875   5308   5747    133   -322    160       C  
ATOM   1834  CD1 ILE A 224      33.061   2.483  26.940  1.00 28.22           C  
ANISOU 1834  CD1 ILE A 224     3909   3250   3564    234   -291    102       C  
ATOM   1835  N   LEU A 225      28.170   0.119  28.266  1.00 37.32           N  
ANISOU 1835  N   LEU A 225     4902   4286   4993    153   -391     77       N  
ATOM   1836  CA  LEU A 225      27.312  -0.229  29.396  1.00 43.73           C  
ANISOU 1836  CA  LEU A 225     5654   5107   5856     94   -376    137       C  
ATOM   1837  C   LEU A 225      26.721  -1.615  29.255  1.00 43.95           C  
ANISOU 1837  C   LEU A 225     5617   5045   6037     88   -412    144       C  
ATOM   1838  O   LEU A 225      26.482  -2.290  30.247  1.00 56.25           O  
ANISOU 1838  O   LEU A 225     7112   6595   7665     45   -388    238       O  
ATOM   1839  CB  LEU A 225      26.215   0.823  29.601  1.00 49.08           C  
ANISOU 1839  CB  LEU A 225     6341   5829   6477     86   -358    104       C  
ATOM   1840  CG  LEU A 225      26.897   2.168  29.872  1.00 48.61           C  
ANISOU 1840  CG  LEU A 225     6334   5840   6297     84   -313     99       C  
ATOM   1841  CD1 LEU A 225      25.953   3.283  30.321  1.00 43.43           C  
ANISOU 1841  CD1 LEU A 225     5685   5232   5583     72   -285     76       C  
ATOM   1842  CD2 LEU A 225      28.019   1.949  30.874  1.00 29.71           C  
ANISOU 1842  CD2 LEU A 225     3917   3497   3876     46   -288    172       C  
ATOM   1843  N   GLU A 226      26.527  -2.050  28.038  1.00 39.24           N  
ANISOU 1843  N   GLU A 226     5024   4385   5501    139   -464     43       N  
ATOM   1844  CA  GLU A 226      25.969  -3.349  27.816  1.00 42.66           C  
ANISOU 1844  CA  GLU A 226     5384   4716   6110    131   -502     18       C  
ATOM   1845  C   GLU A 226      27.024  -4.424  27.751  1.00 31.92           C  
ANISOU 1845  C   GLU A 226     4011   3291   4827    141   -512     58       C  
ATOM   1846  O   GLU A 226      26.708  -5.547  27.540  1.00 31.83           O  
ANISOU 1846  O   GLU A 226     3936   3173   4985    137   -539     36       O  
ATOM   1847  CB  GLU A 226      25.117  -3.379  26.540  1.00 56.05           C  
ANISOU 1847  CB  GLU A 226     7066   6386   7843    189   -562   -138       C  
ATOM   1848  CG  GLU A 226      23.857  -2.555  26.540  1.00 72.40           C  
ANISOU 1848  CG  GLU A 226     9146   8525   9836    190   -550   -177       C  
ATOM   1849  CD  GLU A 226      23.259  -2.350  27.902  1.00 79.20           C  
ANISOU 1849  CD  GLU A 226     9968   9399  10724    108   -504    -69       C  
ATOM   1850  OE1 GLU A 226      23.112  -1.198  28.316  1.00 73.42           O  
ANISOU 1850  OE1 GLU A 226     9280   8755   9863     99   -465    -32       O  
ATOM   1851  OE2 GLU A 226      22.906  -3.338  28.547  1.00 79.61           O  
ANISOU 1851  OE2 GLU A 226     9941   9376  10933     60   -504    -19       O  
ATOM   1852  N   GLU A 227      28.283  -4.054  27.881  1.00 36.34           N  
ANISOU 1852  N   GLU A 227     4626   3909   5273    156   -489    108       N  
ATOM   1853  CA  GLU A 227      29.354  -5.046  27.856  1.00 34.81           C  
ANISOU 1853  CA  GLU A 227     4424   3667   5136    172   -495    153       C  
ATOM   1854  C   GLU A 227      29.384  -5.814  29.183  1.00 48.96           C  
ANISOU 1854  C   GLU A 227     6152   5439   7010    118   -441    303       C  
ATOM   1855  O   GLU A 227      28.538  -5.611  30.057  1.00 54.25           O  
ANISOU 1855  O   GLU A 227     6781   6135   7697     74   -405    366       O  
ATOM   1856  CB  GLU A 227      30.701  -4.377  27.563  1.00 32.06           C  
ANISOU 1856  CB  GLU A 227     4147   3399   4635    208   -486    160       C  
ATOM   1857  CG  GLU A 227      31.855  -5.346  27.249  1.00 47.63           C  
ANISOU 1857  CG  GLU A 227     6121   5332   6645    245   -505    182       C  
ATOM   1858  CD  GLU A 227      31.459  -6.395  26.232  1.00 54.21           C  
ANISOU 1858  CD  GLU A 227     6919   6054   7625    292   -572     78       C  
ATOM   1859  OE1 GLU A 227      31.173  -5.981  25.076  1.00 61.43           O  
ANISOU 1859  OE1 GLU A 227     7854   6986   8500    355   -623    -49       O  
ATOM   1860  OE2 GLU A 227      31.420  -7.612  26.598  1.00 38.52           O  
ANISOU 1860  OE2 GLU A 227     4874   3966   5796    274   -570    122       O  
ATOM   1861  N   LYS A 228      30.267  -6.773  29.321  1.00 63.82           N  
ANISOU 1861  N   LYS A 228     8024   7287   8937    135   -431    369       N  
ATOM   1862  CA  LYS A 228      30.229  -7.571  30.524  1.00 68.38           C  
ANISOU 1862  CA  LYS A 228     8532   7842   9606    109   -370    527       C  
ATOM   1863  C   LYS A 228      30.580  -6.949  31.847  1.00 72.28           C  
ANISOU 1863  C   LYS A 228     9017   8490   9955     85   -305    645       C  
ATOM   1864  O   LYS A 228      29.809  -7.098  32.767  1.00 86.11           O  
ANISOU 1864  O   LYS A 228    10713  10265  11738     53   -271    708       O  
ATOM   1865  CB  LYS A 228      30.936  -8.911  30.350  1.00 67.32           C  
ANISOU 1865  CB  LYS A 228     8397   7653   9528    149   -370    571       C  
ATOM   1866  CG  LYS A 228      32.412  -8.870  30.243  1.00 82.14           C  
ANISOU 1866  CG  LYS A 228    10187   9457  11564    139   -306    728       C  
ATOM   1867  CD  LYS A 228      32.865  -9.910  29.216  1.00 91.30           C  
ANISOU 1867  CD  LYS A 228    11266  10491  12931     98   -302    723       C  
ATOM   1868  CE  LYS A 228      34.317 -10.296  29.337  1.00 92.56           C  
ANISOU 1868  CE  LYS A 228    11328  10555  13287     94   -224    900       C  
ATOM   1869  NZ  LYS A 228      34.543 -11.155  30.517  1.00 89.82           N  
ANISOU 1869  NZ  LYS A 228    10957  10366  12804    111   -134   1101       N  
ATOM   1870  N   ASN A 229      31.704  -6.255  31.974  1.00 58.15           N  
ANISOU 1870  N   ASN A 229     7271   6815   8008    103   -288    666       N  
ATOM   1871  CA  ASN A 229      32.042  -5.662  33.264  1.00 48.81           C  
ANISOU 1871  CA  ASN A 229     6060   5795   6690     91   -230    760       C  
ATOM   1872  C   ASN A 229      32.236  -4.189  33.116  1.00 41.72           C  
ANISOU 1872  C   ASN A 229     5222   4998   5633     75   -243    659       C  
ATOM   1873  O   ASN A 229      33.335  -3.724  33.028  1.00 43.42           O  
ANISOU 1873  O   ASN A 229     5472   5294   5731     85   -237    635       O  
ATOM   1874  CB  ASN A 229      33.312  -6.266  33.859  1.00 52.99           C  
ANISOU 1874  CB  ASN A 229     6561   6399   7172    125   -186    875       C  
ATOM   1875  CG  ASN A 229      33.120  -7.678  34.362  1.00 74.23           C  
ANISOU 1875  CG  ASN A 229     9172   9003  10030    146   -143   1019       C  
ATOM   1876  OD1 ASN A 229      32.138  -7.982  35.011  1.00 78.65           O  
ANISOU 1876  OD1 ASN A 229     9728   9526  10630    184   -130   1078       O  
ATOM   1877  ND2 ASN A 229      34.073  -8.549  34.076  1.00 79.31           N  
ANISOU 1877  ND2 ASN A 229     9747   9609  10780    123   -115   1084       N  
ATOM   1878  N   PRO A 230      31.135  -3.470  33.109  1.00 36.09           N  
ANISOU 1878  N   PRO A 230     4512   4274   4925     49   -254    602       N  
ATOM   1879  CA  PRO A 230      31.112  -2.040  32.810  1.00 32.98           C  
ANISOU 1879  CA  PRO A 230     4177   3940   4415     38   -262    499       C  
ATOM   1880  C   PRO A 230      32.010  -1.282  33.772  1.00 40.88           C  
ANISOU 1880  C   PRO A 230     5164   5092   5278     29   -222    522       C  
ATOM   1881  O   PRO A 230      32.700  -0.350  33.375  1.00 52.88           O  
ANISOU 1881  O   PRO A 230     6733   6641   6718     26   -224    444       O  
ATOM   1882  CB  PRO A 230      29.646  -1.645  33.037  1.00 36.84           C  
ANISOU 1882  CB  PRO A 230     4644   4420   4935     16   -263    480       C  
ATOM   1883  CG  PRO A 230      28.871  -2.933  33.074  1.00 43.37           C  
ANISOU 1883  CG  PRO A 230     5408   5149   5921     13   -270    545       C  
ATOM   1884  CD  PRO A 230      29.831  -3.978  33.572  1.00 29.39           C  
ANISOU 1884  CD  PRO A 230     3597   3380   4189     30   -242    657       C  
ATOM   1885  N   LEU A 231      32.001  -1.686  35.032  1.00 40.87           N  
ANISOU 1885  N   LEU A 231     5082   5191   5254     32   -184    626       N  
ATOM   1886  CA  LEU A 231      32.706  -0.958  36.077  1.00 39.57           C  
ANISOU 1886  CA  LEU A 231     4879   5204   4952     33   -150    629       C  
ATOM   1887  C   LEU A 231      34.213  -0.906  35.792  1.00 43.30           C  
ANISOU 1887  C   LEU A 231     5379   5714   5360     45   -149    602       C  
ATOM   1888  O   LEU A 231      34.865   0.101  36.070  1.00 44.42           O  
ANISOU 1888  O   LEU A 231     5521   5953   5402     30   -139    525       O  
ATOM   1889  CB  LEU A 231      32.441  -1.638  37.418  1.00 36.86           C  
ANISOU 1889  CB  LEU A 231     4429   4980   4596     62   -107    767       C  
ATOM   1890  CG  LEU A 231      32.316  -0.868  38.737  1.00 38.40           C  
ANISOU 1890  CG  LEU A 231     4546   5382   4663     76    -77    769       C  
ATOM   1891  CD1 LEU A 231      33.221  -1.574  39.658  1.00 36.42           C  
ANISOU 1891  CD1 LEU A 231     4213   5279   4347    132    -35    882       C  
ATOM   1892  CD2 LEU A 231      32.693   0.615  38.677  1.00 41.30           C  
ANISOU 1892  CD2 LEU A 231     4950   5815   4929     46    -93    607       C  
ATOM   1893  N   LYS A 232      34.728  -1.958  35.204  1.00 39.23           N  
ANISOU 1893  N   LYS A 232     4878   5119   4909     71   -159    661       N  
ATOM   1894  CA  LYS A 232      36.092  -2.058  34.787  1.00 45.28           C  
ANISOU 1894  CA  LYS A 232     5676   5908   5620     88   -164    641       C  
ATOM   1895  C   LYS A 232      36.446  -1.049  33.748  1.00 39.82           C  
ANISOU 1895  C   LYS A 232     5063   5164   4901     67   -190    514       C  
ATOM   1896  O   LYS A 232      37.490  -0.476  33.783  1.00 38.23           O  
ANISOU 1896  O   LYS A 232     4868   5040   4616     60   -177    469       O  
ATOM   1897  CB  LYS A 232      36.253  -3.391  34.108  1.00 51.44           C  
ANISOU 1897  CB  LYS A 232     6476   6569   6499    124   -183    701       C  
ATOM   1898  CG  LYS A 232      36.854  -4.402  34.922  1.00 64.80           C  
ANISOU 1898  CG  LYS A 232     8098   8255   8269    153   -150    844       C  
ATOM   1899  CD  LYS A 232      38.310  -4.130  35.023  1.00 68.00           C  
ANISOU 1899  CD  LYS A 232     8527   8559   8751    193   -166    879       C  
ATOM   1900  CE  LYS A 232      39.041  -4.914  34.033  1.00 66.17           C  
ANISOU 1900  CE  LYS A 232     8301   8455   8385    223   -149    897       C  
ATOM   1901  NZ  LYS A 232      40.434  -4.922  34.446  1.00 52.25           N  
ANISOU 1901  NZ  LYS A 232     6561   6817   6475    193   -153    795       N  
ATOM   1902  N   SER A 233      35.538  -0.897  32.809  1.00 28.91           N  
ANISOU 1902  N   SER A 233     3732   3652   3599     67   -222    464       N  
ATOM   1903  CA  SER A 233      35.641   0.015  31.664  1.00 29.59           C  
ANISOU 1903  CA  SER A 233     3889   3678   3674     71   -239    367       C  
ATOM   1904  C   SER A 233      35.618   1.458  32.152  1.00 30.64           C  
ANISOU 1904  C   SER A 233     4020   3883   3740     32   -205    303       C  
ATOM   1905  O   SER A 233      36.478   2.284  31.812  1.00 29.87           O  
ANISOU 1905  O   SER A 233     3946   3803   3600     25   -186    254       O  
ATOM   1906  CB  SER A 233      34.448  -0.186  30.734  1.00 28.11           C  
ANISOU 1906  CB  SER A 233     3733   3374   3573     91   -275    329       C  
ATOM   1907  OG  SER A 233      34.517  -1.413  30.042  1.00 37.28           O  
ANISOU 1907  OG  SER A 233     4897   4451   4816    132   -315    348       O  
ATOM   1908  N   ILE A 234      34.615   1.742  32.969  1.00 25.07           N  
ANISOU 1908  N   ILE A 234     3278   3214   3035      8   -193    305       N  
ATOM   1909  CA  ILE A 234      34.484   3.018  33.630  1.00 29.51           C  
ANISOU 1909  CA  ILE A 234     3820   3850   3541    -26   -163    238       C  
ATOM   1910  C   ILE A 234      35.762   3.392  34.386  1.00 23.97           C  
ANISOU 1910  C   ILE A 234     3072   3274   2763    -43   -137    215       C  
ATOM   1911  O   ILE A 234      36.249   4.521  34.285  1.00 25.57           O  
ANISOU 1911  O   ILE A 234     3282   3486   2949    -70   -114    127       O  
ATOM   1912  CB  ILE A 234      33.295   2.989  34.567  1.00 33.79           C  
ANISOU 1912  CB  ILE A 234     4312   4443   4082    -36   -161    263       C  
ATOM   1913  CG1 ILE A 234      32.001   2.879  33.743  1.00 34.59           C  
ANISOU 1913  CG1 ILE A 234     4459   4425   4258    -25   -185    255       C  
ATOM   1914  CG2 ILE A 234      33.303   4.217  35.463  1.00 30.16           C  
ANISOU 1914  CG2 ILE A 234     3813   4091   3554    -62   -134    185       C  
ATOM   1915  CD1 ILE A 234      30.732   2.901  34.615  1.00 30.64           C  
ANISOU 1915  CD1 ILE A 234     3909   3974   3760    -35   -181    282       C  
ATOM   1916  N   ARG A 235      36.349   2.439  35.092  1.00 21.49           N  
ANISOU 1916  N   ARG A 235     2702   3052   2411    -23   -136    292       N  
ATOM   1917  CA  ARG A 235      37.545   2.777  35.866  1.00 25.74           C  
ANISOU 1917  CA  ARG A 235     3180   3739   2861    -31   -113    260       C  
ATOM   1918  C   ARG A 235      38.673   2.976  34.906  1.00 27.79           C  
ANISOU 1918  C   ARG A 235     3491   3940   3127    -36   -114    225       C  
ATOM   1919  O   ARG A 235      39.601   3.737  35.156  1.00 30.14           O  
ANISOU 1919  O   ARG A 235     3758   4312   3383    -62    -93    150       O  
ATOM   1920  CB  ARG A 235      37.860   1.707  36.907  1.00 25.18           C  
ANISOU 1920  CB  ARG A 235     3028   3808   2733     12   -101    366       C  
ATOM   1921  CG  ARG A 235      36.705   1.536  37.892  1.00 25.54           C  
ANISOU 1921  CG  ARG A 235     3009   3924   2770     28    -92    419       C  
ATOM   1922  CD  ARG A 235      36.931   0.359  38.804  1.00 26.31           C  
ANISOU 1922  CD  ARG A 235     3024   4143   2829     88    -66    563       C  
ATOM   1923  NE  ARG A 235      36.361   0.567  40.132  1.00 45.55           N  
ANISOU 1923  NE  ARG A 235     5356   6761   5190    120    -42    590       N  
ATOM   1924  CZ  ARG A 235      35.931  -0.421  40.916  1.00 48.33           C  
ANISOU 1924  CZ  ARG A 235     5632   7189   5542    180    -10    748       C  
ATOM   1925  NH1 ARG A 235      35.407  -0.173  42.141  1.00 27.22           N  
ANISOU 1925  NH1 ARG A 235     2852   4707   2783    226     13    777       N  
ATOM   1926  NH2 ARG A 235      36.005  -1.664  40.452  1.00 39.37           N  
ANISOU 1926  NH2 ARG A 235     4521   5936   4501    202      2    880       N  
ATOM   1927  N   ARG A 236      38.565   2.313  33.766  1.00 31.58           N  
ANISOU 1927  N   ARG A 236     4042   4288   3668     -8   -139    272       N  
ATOM   1928  CA  ARG A 236      39.596   2.431  32.750  1.00 29.54           C  
ANISOU 1928  CA  ARG A 236     3832   3981   3412      4   -143    255       C  
ATOM   1929  C   ARG A 236      39.524   3.819  32.107  1.00 24.36           C  
ANISOU 1929  C   ARG A 236     3211   3259   2785    -24   -118    168       C  
ATOM   1930  O   ARG A 236      40.547   4.462  31.897  1.00 37.45           O  
ANISOU 1930  O   ARG A 236     4862   4937   4429    -41    -92    128       O  
ATOM   1931  CB  ARG A 236      39.459   1.297  31.724  1.00 31.56           C  
ANISOU 1931  CB  ARG A 236     4141   4131   3720     58   -182    318       C  
ATOM   1932  CG  ARG A 236      40.617   1.195  30.760  1.00 35.47           C  
ANISOU 1932  CG  ARG A 236     4674   4606   4197     90   -191    319       C  
ATOM   1933  CD  ARG A 236      41.980   1.107  31.446  1.00 29.78           C  
ANISOU 1933  CD  ARG A 236     3906   4014   3396     79   -169    334       C  
ATOM   1934  NE  ARG A 236      42.901   0.370  30.594  1.00 35.02           N  
ANISOU 1934  NE  ARG A 236     4604   4656   4047    131   -193    376       N  
ATOM   1935  CZ  ARG A 236      44.223   0.493  30.592  1.00 44.01           C  
ANISOU 1935  CZ  ARG A 236     5726   5876   5119    134   -178    376       C  
ATOM   1936  NH1 ARG A 236      44.944  -0.241  29.760  1.00 52.94           N  
ANISOU 1936  NH1 ARG A 236     6892   6985   6239    192   -206    418       N  
ATOM   1937  NH2 ARG A 236      44.828   1.343  31.399  1.00 47.46           N  
ANISOU 1937  NH2 ARG A 236     6105   6421   5505     81   -139    325       N  
ATOM   1938  N   MET A 237      38.310   4.287  31.822  1.00 24.16           N  
ANISOU 1938  N   MET A 237     3217   3156   2808    -25   -119    143       N  
ATOM   1939  CA  MET A 237      38.093   5.641  31.294  1.00 24.15           C  
ANISOU 1939  CA  MET A 237     3244   3088   2845    -42    -82     75       C  
ATOM   1940  C   MET A 237      38.698   6.654  32.248  1.00 33.89           C  
ANISOU 1940  C   MET A 237     4414   4401   4061   -102    -41     -6       C  
ATOM   1941  O   MET A 237      39.382   7.577  31.846  1.00 33.75           O  
ANISOU 1941  O   MET A 237     4398   4347   4080   -123      0    -53       O  
ATOM   1942  CB  MET A 237      36.592   5.925  31.160  1.00 23.62           C  
ANISOU 1942  CB  MET A 237     3204   2959   2812    -32    -88     62       C  
ATOM   1943  CG  MET A 237      35.927   5.157  29.992  1.00 31.65           C  
ANISOU 1943  CG  MET A 237     4276   3888   3862     33   -126    106       C  
ATOM   1944  SD  MET A 237      34.101   5.286  29.873  1.00 36.38           S  
ANISOU 1944  SD  MET A 237     4892   4436   4493     48   -142     89       S  
ATOM   1945  CE  MET A 237      33.621   3.652  30.430  1.00 75.44           C  
ANISOU 1945  CE  MET A 237     9800   9402   9462     48   -197    152       C  
ATOM   1946  N   ALA A 238      38.441   6.464  33.537  1.00 40.23           N  
ANISOU 1946  N   ALA A 238     5149   5322   4814   -124    -51    -25       N  
ATOM   1947  CA  ALA A 238      38.933   7.387  34.521  1.00 32.74           C  
ANISOU 1947  CA  ALA A 238     4121   4473   3844   -171    -23   -129       C  
ATOM   1948  C   ALA A 238      40.460   7.309  34.539  1.00 26.50           C  
ANISOU 1948  C   ALA A 238     3293   3750   3025   -185    -11   -147       C  
ATOM   1949  O   ALA A 238      41.136   8.327  34.492  1.00 28.24           O  
ANISOU 1949  O   ALA A 238     3484   3956   3289   -228     26   -241       O  
ATOM   1950  CB  ALA A 238      38.330   7.074  35.857  1.00 31.63           C  
ANISOU 1950  CB  ALA A 238     3907   4476   3635   -165    -41   -134       C  
ATOM   1951  N   GLN A 239      41.015   6.139  34.424  1.00 23.48           N  
ANISOU 1951  N   GLN A 239     2910   3427   2583   -147    -37    -57       N  
ATOM   1952  CA  GLN A 239      42.442   6.009  34.389  1.00 25.98           C  
ANISOU 1952  CA  GLN A 239     3197   3808   2865   -153    -26    -68       C  
ATOM   1953  C   GLN A 239      42.987   6.800  33.256  1.00 33.09           C  
ANISOU 1953  C   GLN A 239     4148   4577   3846   -171      4    -91       C  
ATOM   1954  O   GLN A 239      44.072   7.271  33.323  1.00 32.56           O  
ANISOU 1954  O   GLN A 239     4036   4553   3782   -203     30   -145       O  
ATOM   1955  CB  GLN A 239      42.826   4.589  34.136  1.00 34.41           C  
ANISOU 1955  CB  GLN A 239     4285   4912   3876    -97    -56     51       C  
ATOM   1956  CG  GLN A 239      43.149   3.814  35.313  1.00 52.94           C  
ANISOU 1956  CG  GLN A 239     6561   7418   6136    -64    -66    105       C  
ATOM   1957  CD  GLN A 239      43.620   2.440  34.965  1.00 64.45           C  
ANISOU 1957  CD  GLN A 239     8048   8873   7567     -5    -85    231       C  
ATOM   1958  OE1 GLN A 239      44.583   2.276  34.238  1.00 56.43           O  
ANISOU 1958  OE1 GLN A 239     7074   7810   6555      5    -91    243       O  
ATOM   1959  NE2 GLN A 239      42.946   1.439  35.492  1.00 54.99           N  
ANISOU 1959  NE2 GLN A 239     6823   7720   6352     39    -90    331       N  
ATOM   1960  N   PHE A 240      42.234   6.873  32.178  1.00 37.04           N  
ANISOU 1960  N   PHE A 240     4734   4929   4409   -142      3    -43       N  
ATOM   1961  CA  PHE A 240      42.684   7.589  30.983  1.00 44.76           C  
ANISOU 1961  CA  PHE A 240     5755   5793   5458   -134     42    -36       C  
ATOM   1962  C   PHE A 240      42.224   9.039  30.933  1.00 48.04           C  
ANISOU 1962  C   PHE A 240     6162   6121   5970   -175    101   -113       C  
ATOM   1963  O   PHE A 240      42.491   9.734  29.958  1.00 52.46           O  
ANISOU 1963  O   PHE A 240     6750   6578   6604   -161    151    -91       O  
ATOM   1964  CB  PHE A 240      42.240   6.870  29.703  1.00 44.82           C  
ANISOU 1964  CB  PHE A 240     5849   5712   5470    -52     12     60       C  
ATOM   1965  CG  PHE A 240      43.112   5.690  29.325  1.00 41.98           C  
ANISOU 1965  CG  PHE A 240     5502   5401   5049     -4    -28    130       C  
ATOM   1966  CD1 PHE A 240      44.496   5.796  29.341  1.00 37.51           C  
ANISOU 1966  CD1 PHE A 240     4899   4897   4455    -20     -8    128       C  
ATOM   1967  CD2 PHE A 240      42.545   4.481  28.944  1.00 31.39           C  
ANISOU 1967  CD2 PHE A 240     4201   4038   3687     57    -86    190       C  
ATOM   1968  CE1 PHE A 240      45.301   4.718  28.975  1.00 36.41           C  
ANISOU 1968  CE1 PHE A 240     4774   4806   4253     32    -46    194       C  
ATOM   1969  CE2 PHE A 240      43.337   3.417  28.587  1.00 31.67           C  
ANISOU 1969  CE2 PHE A 240     4246   4107   3679    105   -122    247       C  
ATOM   1970  CZ  PHE A 240      44.725   3.538  28.602  1.00 33.98           C  
ANISOU 1970  CZ  PHE A 240     4512   4471   3929     96   -102    253       C  
ATOM   1971  N   ASP A 241      41.525   9.483  31.973  1.00 40.55           N  
ANISOU 1971  N   ASP A 241     5170   5216   5022   -217    100   -194       N  
ATOM   1972  CA  ASP A 241      40.985  10.842  32.023  1.00 42.21           C  
ANISOU 1972  CA  ASP A 241     5369   5338   5330   -253    155   -277       C  
ATOM   1973  C   ASP A 241      39.849  11.103  31.053  1.00 39.73           C  
ANISOU 1973  C   ASP A 241     5140   4893   5062   -201    171   -215       C  
ATOM   1974  O   ASP A 241      39.542  12.249  30.758  1.00 43.15           O  
ANISOU 1974  O   ASP A 241     5579   5226   5590   -213    234   -252       O  
ATOM   1975  CB  ASP A 241      42.087  11.873  31.790  1.00 49.52           C  
ANISOU 1975  CB  ASP A 241     6247   6212   6355   -303    223   -339       C  
ATOM   1976  CG  ASP A 241      43.039  11.973  32.962  1.00 47.52           C  
ANISOU 1976  CG  ASP A 241     5882   6100   6072   -366    213   -458       C  
ATOM   1977  OD1 ASP A 241      44.252  12.185  32.742  1.00 40.17           O  
ANISOU 1977  OD1 ASP A 241     4908   5176   5177   -395    242   -477       O  
ATOM   1978  OD2 ASP A 241      42.571  11.816  34.107  1.00 58.26           O  
ANISOU 1978  OD2 ASP A 241     7190   7581   7366   -378    175   -531       O  
ATOM   1979  N   VAL A 242      39.215  10.049  30.558  1.00 44.49           N  
ANISOU 1979  N   VAL A 242     5801   5498   5604   -139    118   -127       N  
ATOM   1980  CA  VAL A 242      38.159  10.204  29.550  1.00 38.00           C  
ANISOU 1980  CA  VAL A 242     5052   4577   4811    -74    128    -76       C  
ATOM   1981  C   VAL A 242      36.905  10.840  30.133  1.00 36.40           C  
ANISOU 1981  C   VAL A 242     4847   4357   4626    -93    137   -131       C  
ATOM   1982  O   VAL A 242      36.306  11.741  29.526  1.00 36.84           O  
ANISOU 1982  O   VAL A 242     4936   4322   4741    -65    189   -131       O  
ATOM   1983  CB  VAL A 242      37.766   8.837  28.935  1.00 30.06           C  
ANISOU 1983  CB  VAL A 242     4090   3586   3745     -6     58      3       C  
ATOM   1984  CG1 VAL A 242      36.456   8.924  28.183  1.00 20.68           C  
ANISOU 1984  CG1 VAL A 242     2953   2334   2570     57     53     22       C  
ATOM   1985  CG2 VAL A 242      38.886   8.289  28.064  1.00 29.52           C  
ANISOU 1985  CG2 VAL A 242     4037   3520   3661     39     51     61       C  
ATOM   1986  N   ILE A 243      36.502  10.374  31.315  1.00 24.72           N  
ANISOU 1986  N   ILE A 243     3325   2976   3091   -128     91   -167       N  
ATOM   1987  CA  ILE A 243      35.222  10.804  31.859  1.00 24.85           C  
ANISOU 1987  CA  ILE A 243     3340   2995   3107   -133     88   -206       C  
ATOM   1988  C   ILE A 243      35.080  12.322  31.884  1.00 35.85           C  
ANISOU 1988  C   ILE A 243     4726   4314   4583   -159    158   -287       C  
ATOM   1989  O   ILE A 243      34.038  12.847  31.491  1.00 43.52           O  
ANISOU 1989  O   ILE A 243     5739   5218   5579   -126    181   -281       O  
ATOM   1990  CB  ILE A 243      34.977  10.310  33.273  1.00 32.63           C  
ANISOU 1990  CB  ILE A 243     4257   4119   4023   -165     45   -237       C  
ATOM   1991  CG1 ILE A 243      35.106   8.796  33.344  1.00 28.33           C  
ANISOU 1991  CG1 ILE A 243     3710   3637   3419   -138    -10   -143       C  
ATOM   1992  CG2 ILE A 243      33.607  10.790  33.738  1.00 34.03           C  
ANISOU 1992  CG2 ILE A 243     4434   4299   4195   -160     42   -270       C  
ATOM   1993  CD1 ILE A 243      34.984   8.233  34.723  1.00 35.32           C  
ANISOU 1993  CD1 ILE A 243     4514   4673   4232   -150    -38   -142       C  
ATOM   1994  N   LYS A 244      36.115  13.020  32.352  1.00 33.26           N  
ANISOU 1994  N   LYS A 244     4337   3996   4305   -215    196   -368       N  
ATOM   1995  CA  LYS A 244      36.052  14.483  32.452  1.00 36.29           C  
ANISOU 1995  CA  LYS A 244     4698   4290   4801   -248    269   -461       C  
ATOM   1996  C   LYS A 244      35.952  15.195  31.086  1.00 42.11           C  
ANISOU 1996  C   LYS A 244     5500   4864   5636   -200    349   -386       C  
ATOM   1997  O   LYS A 244      35.291  16.235  30.971  1.00 33.12           O  
ANISOU 1997  O   LYS A 244     4374   3633   4577   -192    409   -418       O  
ATOM   1998  CB  LYS A 244      37.201  15.044  33.310  1.00 38.73           C  
ANISOU 1998  CB  LYS A 244     4906   4649   5159   -324    288   -589       C  
ATOM   1999  CG  LYS A 244      38.374  15.663  32.545  1.00 51.11           C  
ANISOU 1999  CG  LYS A 244     6462   6109   6848   -349    362   -582       C  
ATOM   2000  CD  LYS A 244      39.597  14.730  32.438  1.00 57.42           C  
ANISOU 2000  CD  LYS A 244     7240   6996   7582   -355    328   -536       C  
ATOM   2001  CE  LYS A 244      40.803  15.223  33.254  1.00 58.00           C  
ANISOU 2001  CE  LYS A 244     7199   7134   7706   -435    344   -675       C  
ATOM   2002  NZ  LYS A 244      40.791  14.771  34.684  1.00 65.55           N  
ANISOU 2002  NZ  LYS A 244     8070   8289   8547   -456    274   -782       N  
ATOM   2003  N   HIS A 245      36.597  14.637  30.057  1.00 40.10           N  
ANISOU 2003  N   HIS A 245     5283   4584   5370   -155    354   -283       N  
ATOM   2004  CA  HIS A 245      36.448  15.163  28.699  1.00 26.49           C  
ANISOU 2004  CA  HIS A 245     3614   2742   3710    -77    428   -187       C  
ATOM   2005  C   HIS A 245      35.100  14.807  28.105  1.00 34.18           C  
ANISOU 2005  C   HIS A 245     4655   3715   4616     10    402   -126       C  
ATOM   2006  O   HIS A 245      34.669  15.410  27.123  1.00 42.94           O  
ANISOU 2006  O   HIS A 245     5802   4747   5766     89    469    -61       O  
ATOM   2007  CB  HIS A 245      37.528  14.641  27.775  1.00 23.91           C  
ANISOU 2007  CB  HIS A 245     3296   2416   3374    -38    435    -96       C  
ATOM   2008  CG  HIS A 245      38.873  15.234  28.032  1.00 32.54           C  
ANISOU 2008  CG  HIS A 245     4322   3480   4561   -110    490   -137       C  
ATOM   2009  ND1 HIS A 245      39.213  16.496  27.615  1.00 41.13           N  
ANISOU 2009  ND1 HIS A 245     5385   4438   5804   -118    605   -131       N  
ATOM   2010  CD2 HIS A 245      39.969  14.717  28.640  1.00 38.93           C  
ANISOU 2010  CD2 HIS A 245     5078   4376   5339   -172    450   -183       C  
ATOM   2011  CE1 HIS A 245      40.471  16.747  27.964  1.00 45.39           C  
ANISOU 2011  CE1 HIS A 245     5852   4978   6415   -194    631   -182       C  
ATOM   2012  NE2 HIS A 245      40.945  15.684  28.589  1.00 45.71           N  
ANISOU 2012  NE2 HIS A 245     5876   5159   6332   -225    535   -218       N  
ATOM   2013  N   LEU A 246      34.432  13.813  28.669  1.00 32.54           N  
ANISOU 2013  N   LEU A 246     4454   3601   4308      3    309   -141       N  
ATOM   2014  CA  LEU A 246      33.057  13.564  28.244  1.00 33.90           C  
ANISOU 2014  CA  LEU A 246     4675   3776   4431     72    284   -109       C  
ATOM   2015  C   LEU A 246      32.088  14.492  29.004  1.00 35.43           C  
ANISOU 2015  C   LEU A 246     4858   3951   4651     43    312   -180       C  
ATOM   2016  O   LEU A 246      31.143  15.043  28.424  1.00 32.63           O  
ANISOU 2016  O   LEU A 246     4543   3549   4305    107    351   -155       O  
ATOM   2017  CB  LEU A 246      32.670  12.084  28.416  1.00 18.13           C  
ANISOU 2017  CB  LEU A 246     2682   1866   2342     82    181    -86       C  
ATOM   2018  CG  LEU A 246      33.508  11.059  27.651  1.00 26.64           C  
ANISOU 2018  CG  LEU A 246     3770   2961   3392    122    143    -26       C  
ATOM   2019  CD1 LEU A 246      32.931   9.660  27.796  1.00 21.79           C  
ANISOU 2019  CD1 LEU A 246     3156   2403   2721    134     51    -11       C  
ATOM   2020  CD2 LEU A 246      33.602  11.445  26.166  1.00 33.67           C  
ANISOU 2020  CD2 LEU A 246     4699   3795   4298    227    192     36       C  
ATOM   2021  N   PHE A 247      32.353  14.668  30.297  1.00 32.47           N  
ANISOU 2021  N   PHE A 247     4425   3630   4281    -44    291   -272       N  
ATOM   2022  CA  PHE A 247      31.497  15.457  31.192  1.00 45.22           C  
ANISOU 2022  CA  PHE A 247     6017   5256   5908    -72    302   -357       C  
ATOM   2023  C   PHE A 247      32.387  16.343  32.037  1.00 55.80           C  
ANISOU 2023  C   PHE A 247     7284   6586   7330   -149    340   -473       C  
ATOM   2024  O   PHE A 247      33.011  15.883  32.988  1.00 53.60           O  
ANISOU 2024  O   PHE A 247     6940   6417   7009   -202    291   -534       O  
ATOM   2025  CB  PHE A 247      30.662  14.555  32.099  1.00 36.40           C  
ANISOU 2025  CB  PHE A 247     4879   4266   4684    -81    214   -366       C  
ATOM   2026  CG  PHE A 247      30.072  13.390  31.389  1.00 42.00           C  
ANISOU 2026  CG  PHE A 247     5635   4994   5330    -26    161   -269       C  
ATOM   2027  CD1 PHE A 247      30.721  12.174  31.382  1.00 37.99           C  
ANISOU 2027  CD1 PHE A 247     5112   4538   4783    -35    107   -220       C  
ATOM   2028  CD2 PHE A 247      28.898  13.528  30.666  1.00 47.48           C  
ANISOU 2028  CD2 PHE A 247     6380   5650   6011     39    169   -234       C  
ATOM   2029  CE1 PHE A 247      30.190  11.098  30.685  1.00 36.72           C  
ANISOU 2029  CE1 PHE A 247     4984   4378   4590     15     58   -150       C  
ATOM   2030  CE2 PHE A 247      28.365  12.466  29.965  1.00 42.04           C  
ANISOU 2030  CE2 PHE A 247     5718   4978   5278     91    118   -171       C  
ATOM   2031  CZ  PHE A 247      29.008  11.240  29.980  1.00 33.07           C  
ANISOU 2031  CZ  PHE A 247     4563   3880   4121     75     60   -134       C  
ATOM   2032  N   PRO A 248      32.429  17.628  31.688  1.00 58.41           N  
ANISOU 2032  N   PRO A 248     7618   6788   7788   -149    433   -508       N  
ATOM   2033  CA  PRO A 248      33.438  18.602  32.110  1.00 57.32           C  
ANISOU 2033  CA  PRO A 248     7408   6585   7785   -219    494   -615       C  
ATOM   2034  C   PRO A 248      33.267  19.030  33.563  1.00 52.20           C  
ANISOU 2034  C   PRO A 248     6675   6024   7133   -281    457   -786       C  
ATOM   2035  O   PRO A 248      34.146  19.677  34.124  1.00 57.60           O  
ANISOU 2035  O   PRO A 248     7275   6694   7916   -347    484   -913       O  
ATOM   2036  CB  PRO A 248      33.179  19.795  31.173  1.00 55.78           C  
ANISOU 2036  CB  PRO A 248     7252   6208   7735   -177    615   -570       C  
ATOM   2037  CG  PRO A 248      32.140  19.300  30.152  1.00 46.85           C  
ANISOU 2037  CG  PRO A 248     6215   5077   6510    -68    609   -426       C  
ATOM   2038  CD  PRO A 248      31.378  18.248  30.870  1.00 51.69           C  
ANISOU 2038  CD  PRO A 248     6834   5842   6965    -73    492   -446       C  
ATOM   2039  N   LYS A 249      32.130  18.694  34.154  1.00 44.68           N  
ANISOU 2039  N   LYS A 249     5735   5170   6070   -253    396   -795       N  
ATOM   2040  CA  LYS A 249      31.897  18.983  35.560  1.00 42.24           C  
ANISOU 2040  CA  LYS A 249     5339   4985   5725   -288    350   -947       C  
ATOM   2041  C   LYS A 249      31.890  17.743  36.447  1.00 39.04           C  
ANISOU 2041  C   LYS A 249     4889   4791   5153   -285    251   -930       C  
ATOM   2042  O   LYS A 249      31.634  17.846  37.647  1.00 47.91           O  
ANISOU 2042  O   LYS A 249     5931   6058   6214   -291    206  -1037       O  
ATOM   2043  CB  LYS A 249      30.590  19.747  35.746  1.00 39.89           C  
ANISOU 2043  CB  LYS A 249     5069   4652   5437   -252    367   -984       C  
ATOM   2044  CG  LYS A 249      30.794  21.202  36.052  1.00 44.62           C  
ANISOU 2044  CG  LYS A 249     5615   5138   6199   -287    438  -1138       C  
ATOM   2045  CD  LYS A 249      31.291  21.951  34.854  1.00 43.10           C  
ANISOU 2045  CD  LYS A 249     5470   4725   6180   -285    553  -1072       C  
ATOM   2046  CE  LYS A 249      31.775  23.329  35.263  1.00 49.33           C  
ANISOU 2046  CE  LYS A 249     6180   5390   7174   -340    629  -1241       C  
ATOM   2047  NZ  LYS A 249      31.952  24.212  34.078  1.00 50.25           N  
ANISOU 2047  NZ  LYS A 249     6345   5270   7478   -318    766  -1148       N  
ATOM   2048  N   THR A 250      32.144  16.573  35.870  1.00 35.10           N  
ANISOU 2048  N   THR A 250     4436   4316   4585   -264    219   -792       N  
ATOM   2049  CA  THR A 250      32.228  15.362  36.690  1.00 46.69           C  
ANISOU 2049  CA  THR A 250     5855   5968   5917   -258    141   -756       C  
ATOM   2050  C   THR A 250      33.682  14.942  36.957  1.00 47.17           C  
ANISOU 2050  C   THR A 250     5853   6102   5969   -293    133   -782       C  
ATOM   2051  O   THR A 250      34.520  14.820  36.039  1.00 46.30           O  
ANISOU 2051  O   THR A 250     5783   5893   5916   -304    164   -728       O  
ATOM   2052  CB  THR A 250      31.413  14.121  36.160  1.00 40.10           C  
ANISOU 2052  CB  THR A 250     5091   5145   5002   -208     98   -593       C  
ATOM   2053  OG1 THR A 250      32.302  13.167  35.589  1.00 42.24           O  
ANISOU 2053  OG1 THR A 250     5381   5407   5261   -208     85   -506       O  
ATOM   2054  CG2 THR A 250      30.327  14.474  35.159  1.00 18.03           C  
ANISOU 2054  CG2 THR A 250     2388   2218   2244   -168    126   -536       C  
ATOM   2055  N   TYR A 251      33.952  14.716  38.236  1.00 37.21           N  
ANISOU 2055  N   TYR A 251     4485   5031   4622   -298     91   -863       N  
ATOM   2056  CA  TYR A 251      35.259  14.308  38.719  1.00 44.33           C  
ANISOU 2056  CA  TYR A 251     5305   6052   5486   -320     77   -905       C  
ATOM   2057  C   TYR A 251      35.104  12.911  39.283  1.00 44.71           C  
ANISOU 2057  C   TYR A 251     5329   6269   5389   -271     23   -785       C  
ATOM   2058  O   TYR A 251      34.302  12.691  40.209  1.00 37.49           O  
ANISOU 2058  O   TYR A 251     4363   5495   4387   -232    -10   -784       O  
ATOM   2059  CB  TYR A 251      35.739  15.292  39.795  1.00 44.56           C  
ANISOU 2059  CB  TYR A 251     5205   6188   5538   -351     80  -1119       C  
ATOM   2060  CG  TYR A 251      35.525  16.699  39.330  1.00 54.70           C  
ANISOU 2060  CG  TYR A 251     6512   7284   6989   -392    140  -1230       C  
ATOM   2061  CD1 TYR A 251      36.432  17.312  38.464  1.00 52.80           C  
ANISOU 2061  CD1 TYR A 251     6292   6871   6900   -444    205  -1251       C  
ATOM   2062  CD2 TYR A 251      34.382  17.400  39.698  1.00 69.35           C  
ANISOU 2062  CD2 TYR A 251     8370   9122   8857   -372    139  -1293       C  
ATOM   2063  CE1 TYR A 251      36.222  18.600  38.001  1.00 61.28           C  
ANISOU 2063  CE1 TYR A 251     7383   7752   8148   -474    278  -1328       C  
ATOM   2064  CE2 TYR A 251      34.158  18.696  39.241  1.00 78.32           C  
ANISOU 2064  CE2 TYR A 251     9531  10069  10159   -402    205  -1382       C  
ATOM   2065  CZ  TYR A 251      35.081  19.290  38.393  1.00 77.89           C  
ANISOU 2065  CZ  TYR A 251     9492   9834  10268   -453    279  -1394       C  
ATOM   2066  OH  TYR A 251      34.855  20.577  37.947  1.00 84.40           O  
ANISOU 2066  OH  TYR A 251    10332  10458  11277   -476    360  -1464       O  
ATOM   2067  N   TYR A 252      35.842  11.961  38.703  1.00 38.83           N  
ANISOU 2067  N   TYR A 252     4621   5505   4626   -266     18   -672       N  
ATOM   2068  CA  TYR A 252      35.765  10.586  39.166  1.00 33.09           C  
ANISOU 2068  CA  TYR A 252     3872   4912   3788   -217    -20   -543       C  
ATOM   2069  C   TYR A 252      36.693  10.379  40.348  1.00 32.81           C  
ANISOU 2069  C   TYR A 252     3705   5107   3654   -202    -33   -610       C  
ATOM   2070  O   TYR A 252      37.906  10.266  40.169  1.00 33.55           O  
ANISOU 2070  O   TYR A 252     3777   5222   3749   -221    -23   -634       O  
ATOM   2071  CB  TYR A 252      36.158   9.612  38.078  1.00 33.12           C  
ANISOU 2071  CB  TYR A 252     3963   4805   3816   -208    -22   -403       C  
ATOM   2072  CG  TYR A 252      35.634   8.214  38.352  1.00 24.57           C  
ANISOU 2072  CG  TYR A 252     2879   3789   2668   -158    -53   -252       C  
ATOM   2073  CD1 TYR A 252      34.284   7.913  38.143  1.00 23.09           C  
ANISOU 2073  CD1 TYR A 252     2738   3536   2501   -138    -67   -179       C  
ATOM   2074  CD2 TYR A 252      36.466   7.211  38.857  1.00 25.97           C  
ANISOU 2074  CD2 TYR A 252     3000   4096   2772   -128    -62   -181       C  
ATOM   2075  CE1 TYR A 252      33.778   6.654  38.387  1.00 28.78           C  
ANISOU 2075  CE1 TYR A 252     3445   4295   3195    -99    -87    -42       C  
ATOM   2076  CE2 TYR A 252      35.963   5.915  39.107  1.00 32.26           C  
ANISOU 2076  CE2 TYR A 252     3788   4931   3537    -80    -76    -27       C  
ATOM   2077  CZ  TYR A 252      34.619   5.654  38.860  1.00 33.87           C  
ANISOU 2077  CZ  TYR A 252     4035   5046   3788    -70    -87     39       C  
ATOM   2078  OH  TYR A 252      34.089   4.409  39.083  1.00 30.79           O  
ANISOU 2078  OH  TYR A 252     3627   4669   3401    -31    -94    187       O  
ATOM   2079  N   THR A 253      36.121  10.325  41.542  1.00 27.14           N  
ANISOU 2079  N   THR A 253     2894   4578   2841   -156    -54   -637       N  
ATOM   2080  CA  THR A 253      36.906  10.274  42.777  1.00 32.12           C  
ANISOU 2080  CA  THR A 253     3375   5470   3358   -120    -66   -724       C  
ATOM   2081  C   THR A 253      36.701   8.919  43.449  1.00 31.18           C  
ANISOU 2081  C   THR A 253     3208   5525   3113    -35    -78   -548       C  
ATOM   2082  O   THR A 253      35.861   8.132  43.021  1.00 31.54           O  
ANISOU 2082  O   THR A 253     3329   5472   3181    -17    -78   -382       O  
ATOM   2083  CB  THR A 253      36.439  11.370  43.779  1.00 27.46           C  
ANISOU 2083  CB  THR A 253     2682   5010   2742   -109    -79   -912       C  
ATOM   2084  OG1 THR A 253      35.011  11.323  43.885  1.00 31.61           O  
ANISOU 2084  OG1 THR A 253     3248   5506   3258    -77    -90   -836       O  
ATOM   2085  CG2 THR A 253      36.865  12.783  43.325  1.00 23.23           C  
ANISOU 2085  CG2 THR A 253     2155   4323   2348   -191    -56  -1114       C  
ATOM   2086  N   PRO A 254      37.464   8.642  44.516  1.00 44.08           N  
ANISOU 2086  N   PRO A 254     4705   7423   4620     25    -82   -585       N  
ATOM   2087  CA  PRO A 254      37.159   7.439  45.305  1.00 44.69           C  
ANISOU 2087  CA  PRO A 254     4716   7688   4577    126    -77   -404       C  
ATOM   2088  C   PRO A 254      35.724   7.440  45.821  1.00 39.90           C  
ANISOU 2088  C   PRO A 254     4092   7119   3948    171    -86   -340       C  
ATOM   2089  O   PRO A 254      35.093   6.385  45.906  1.00 45.74           O  
ANISOU 2089  O   PRO A 254     4843   7861   4674    221    -72   -136       O  
ATOM   2090  CB  PRO A 254      38.175   7.504  46.427  1.00 44.51           C  
ANISOU 2090  CB  PRO A 254     4528   7973   4410    194    -78   -504       C  
ATOM   2091  CG  PRO A 254      39.385   8.207  45.753  1.00 48.34           C  
ANISOU 2091  CG  PRO A 254     5042   8354   4972    104    -78   -669       C  
ATOM   2092  CD  PRO A 254      38.731   9.276  44.932  1.00 43.89           C  
ANISOU 2092  CD  PRO A 254     4581   7532   4565      8    -82   -771       C  
ATOM   2093  N   SER A 255      35.197   8.622  46.091  1.00 38.61           N  
ANISOU 2093  N   SER A 255     3906   6964   3801    148   -105   -512       N  
ATOM   2094  CA  SER A 255      33.782   8.793  46.433  1.00 40.02           C  
ANISOU 2094  CA  SER A 255     4086   7151   3970    179   -115   -470       C  
ATOM   2095  C   SER A 255      32.859   8.400  45.278  1.00 37.59           C  
ANISOU 2095  C   SER A 255     3934   6563   3786    125   -108   -331       C  
ATOM   2096  O   SER A 255      31.857   7.704  45.461  1.00 41.09           O  
ANISOU 2096  O   SER A 255     4379   7018   4216    166   -105   -174       O  
ATOM   2097  CB  SER A 255      33.525  10.254  46.843  1.00 38.83           C  
ANISOU 2097  CB  SER A 255     3886   7040   3826    159   -138   -712       C  
ATOM   2098  OG  SER A 255      32.153  10.521  47.026  1.00 35.71           O  
ANISOU 2098  OG  SER A 255     3511   6627   3431    182   -149   -680       O  
ATOM   2099  N   MET A 256      33.183   8.846  44.078  1.00 39.63           N  
ANISOU 2099  N   MET A 256     4313   6579   4167     39   -103   -388       N  
ATOM   2100  CA  MET A 256      32.319   8.509  42.944  1.00 43.68           C  
ANISOU 2100  CA  MET A 256     4961   6852   4784      3   -100   -277       C  
ATOM   2101  C   MET A 256      32.394   7.028  42.604  1.00 34.18           C  
ANISOU 2101  C   MET A 256     3785   5610   3592     27    -93    -76       C  
ATOM   2102  O   MET A 256      31.392   6.422  42.259  1.00 32.52           O  
ANISOU 2102  O   MET A 256     3620   5307   3430     34    -96     43       O  
ATOM   2103  CB  MET A 256      32.654   9.331  41.692  1.00 28.71           C  
ANISOU 2103  CB  MET A 256     3178   4722   3007    -72    -87   -371       C  
ATOM   2104  CG  MET A 256      31.620   9.125  40.592  1.00 33.45           C  
ANISOU 2104  CG  MET A 256     3899   5116   3693    -88    -87   -281       C  
ATOM   2105  SD  MET A 256      31.851  10.307  39.265  1.00 41.45           S  
ANISOU 2105  SD  MET A 256     5024   5899   4828   -144    -59   -387       S  
ATOM   2106  CE  MET A 256      31.110  11.760  39.987  1.00 24.98           C  
ANISOU 2106  CE  MET A 256     2894   3857   2740   -149    -50   -545       C  
ATOM   2107  N   ASP A 257      33.597   6.469  42.697  1.00 35.18           N  
ANISOU 2107  N   ASP A 257     3878   5805   3684     39    -84    -49       N  
ATOM   2108  CA  ASP A 257      33.846   5.075  42.374  1.00 32.93           C  
ANISOU 2108  CA  ASP A 257     3615   5477   3421     65    -73    130       C  
ATOM   2109  C   ASP A 257      33.039   4.133  43.273  1.00 34.47           C  
ANISOU 2109  C   ASP A 257     3727   5797   3572    139    -58    297       C  
ATOM   2110  O   ASP A 257      32.519   3.106  42.822  1.00 42.63           O  
ANISOU 2110  O   ASP A 257     4800   6710   4688    143    -49    449       O  
ATOM   2111  CB  ASP A 257      35.328   4.789  42.525  1.00 36.48           C  
ANISOU 2111  CB  ASP A 257     4024   6024   3814     78    -62    114       C  
ATOM   2112  CG  ASP A 257      35.690   3.387  42.095  1.00 41.51           C  
ANISOU 2112  CG  ASP A 257     4692   6595   4484    105    -48    289       C  
ATOM   2113  OD1 ASP A 257      36.067   2.573  42.965  1.00 52.73           O  
ANISOU 2113  OD1 ASP A 257     6019   8192   5824    179    -23    398       O  
ATOM   2114  OD2 ASP A 257      35.583   3.093  40.888  1.00 30.98           O  
ANISOU 2114  OD2 ASP A 257     3471   5042   3259     63    -61    317       O  
ATOM   2115  N   GLU A 258      32.914   4.503  44.541  1.00 27.15           N  
ANISOU 2115  N   GLU A 258     2676   5116   2525    201    -53    264       N  
ATOM   2116  CA  GLU A 258      32.191   3.677  45.495  1.00 39.33           C  
ANISOU 2116  CA  GLU A 258     4118   6811   4013    288    -27    436       C  
ATOM   2117  C   GLU A 258      30.749   3.652  45.095  1.00 39.99           C  
ANISOU 2117  C   GLU A 258     4260   6746   4189    259    -37    495       C  
ATOM   2118  O   GLU A 258      30.106   2.604  45.138  1.00 39.62           O  
ANISOU 2118  O   GLU A 258     4196   6656   4202    287    -11    681       O  
ATOM   2119  CB  GLU A 258      32.313   4.211  46.935  1.00 36.61           C  
ANISOU 2119  CB  GLU A 258     3616   6793   3500    379    -25    369       C  
ATOM   2120  CG  GLU A 258      33.741   4.299  47.444  1.00 46.74           C  
ANISOU 2120  CG  GLU A 258     4816   8269   4674    419    -19    285       C  
ATOM   2121  CD  GLU A 258      33.832   4.561  48.957  1.00 57.66           C  
ANISOU 2121  CD  GLU A 258     6014  10024   5872    544    -14    246       C  
ATOM   2122  OE1 GLU A 258      34.911   4.288  49.536  1.00 52.71           O  
ANISOU 2122  OE1 GLU A 258     5289   9606   5134    612      3    235       O  
ATOM   2123  OE2 GLU A 258      32.834   5.038  49.563  1.00 59.35           O  
ANISOU 2123  OE2 GLU A 258     6172  10335   6042    583    -28    221       O  
ATOM   2124  N   LYS A 259      30.229   4.817  44.723  1.00 46.59           N  
ANISOU 2124  N   LYS A 259     5155   7502   5044    205    -68    335       N  
ATOM   2125  CA  LYS A 259      28.814   4.914  44.390  1.00 41.19           C  
ANISOU 2125  CA  LYS A 259     4520   6704   4428    185    -78    374       C  
ATOM   2126  C   LYS A 259      28.622   4.103  43.152  1.00 30.80           C  
ANISOU 2126  C   LYS A 259     3311   5137   3255    132    -78    461       C  
ATOM   2127  O   LYS A 259      27.636   3.389  43.009  1.00 31.03           O  
ANISOU 2127  O   LYS A 259     3340   5093   3357    136    -72    583       O  
ATOM   2128  CB  LYS A 259      28.404   6.346  44.099  1.00 36.67           C  
ANISOU 2128  CB  LYS A 259     4002   6076   3854    141   -105    183       C  
ATOM   2129  CG  LYS A 259      28.375   7.251  45.292  1.00 38.74           C  
ANISOU 2129  CG  LYS A 259     4156   6573   3992    193   -115     65       C  
ATOM   2130  CD  LYS A 259      28.314   8.711  44.815  1.00 38.81           C  
ANISOU 2130  CD  LYS A 259     4231   6476   4038    135   -132   -147       C  
ATOM   2131  CE  LYS A 259      28.186   9.691  45.984  1.00 38.17           C  
ANISOU 2131  CE  LYS A 259     4037   6616   3850    186   -149   -298       C  
ATOM   2132  NZ  LYS A 259      28.237  11.108  45.539  1.00 44.80           N  
ANISOU 2132  NZ  LYS A 259     4933   7334   4754    129   -156   -508       N  
ATOM   2133  N   MET A 260      29.555   4.216  42.241  1.00 25.13           N  
ANISOU 2133  N   MET A 260     2673   4294   2580     87    -86    389       N  
ATOM   2134  CA  MET A 260      29.487   3.504  41.006  1.00 29.14           C  
ANISOU 2134  CA  MET A 260     3282   4575   3216     47    -95    440       C  
ATOM   2135  C   MET A 260      29.536   2.010  41.232  1.00 40.06           C  
ANISOU 2135  C   MET A 260     4609   5963   4648     85    -72    628       C  
ATOM   2136  O   MET A 260      28.768   1.286  40.653  1.00 43.91           O  
ANISOU 2136  O   MET A 260     5120   6314   5250     72    -75    709       O  
ATOM   2137  CB  MET A 260      30.597   3.982  40.101  1.00 24.31           C  
ANISOU 2137  CB  MET A 260     2748   3868   2620     10   -103    339       C  
ATOM   2138  CG  MET A 260      30.301   3.981  38.657  1.00 37.53           C  
ANISOU 2138  CG  MET A 260     4540   5319   4402    -26   -123    312       C  
ATOM   2139  SD  MET A 260      28.798   4.722  38.065  1.00 42.80           S  
ANISOU 2139  SD  MET A 260     5258   5910   5095    -44   -135    234       S  
ATOM   2140  CE  MET A 260      28.801   6.230  38.869  1.00117.89           C  
ANISOU 2140  CE  MET A 260    14772  15481  14541    -65   -119     68       C  
ATOM   2141  N   GLU A 261      30.410   1.557  42.104  1.00 20.94           N  
ANISOU 2141  N   GLU A 261     2104   3704   2148    136    -43    696       N  
ATOM   2142  CA  GLU A 261      30.391   0.154  42.500  1.00 38.27           C  
ANISOU 2142  CA  GLU A 261     4232   5915   4394    186     -3    896       C  
ATOM   2143  C   GLU A 261      29.032  -0.287  43.099  1.00 40.78           C  
ANISOU 2143  C   GLU A 261     4479   6258   4759    214     20   1027       C  
ATOM   2144  O   GLU A 261      28.420  -1.238  42.614  1.00 41.33           O  
ANISOU 2144  O   GLU A 261     4560   6165   4979    197     31   1135       O  
ATOM   2145  CB  GLU A 261      31.533  -0.129  43.457  1.00 46.89           C  
ANISOU 2145  CB  GLU A 261     5229   7224   5362    258     33    950       C  
ATOM   2146  CG  GLU A 261      31.554  -1.530  43.971  1.00 48.69           C  
ANISOU 2146  CG  GLU A 261     5376   7486   5637    328     92   1177       C  
ATOM   2147  CD  GLU A 261      32.757  -1.790  44.852  1.00 57.64           C  
ANISOU 2147  CD  GLU A 261     6417   8852   6631    414    131   1229       C  
ATOM   2148  OE1 GLU A 261      33.636  -0.898  44.915  1.00 52.04           O  
ANISOU 2148  OE1 GLU A 261     5717   8251   5804    403    102   1064       O  
ATOM   2149  OE2 GLU A 261      32.822  -2.878  45.478  1.00 65.13           O  
ANISOU 2149  OE2 GLU A 261     7277   9875   7594    497    196   1435       O  
ATOM   2150  N   ASN A 262      28.548   0.415  44.125  1.00 32.16           N  
ANISOU 2150  N   ASN A 262     3305   5366   3547    258     25   1008       N  
ATOM   2151  CA  ASN A 262      27.202   0.164  44.638  1.00 31.68           C  
ANISOU 2151  CA  ASN A 262     3181   5335   3522    283     43   1121       C  
ATOM   2152  C   ASN A 262      26.163   0.139  43.530  1.00 36.93           C  
ANISOU 2152  C   ASN A 262     3942   5754   4337    203     11   1082       C  
ATOM   2153  O   ASN A 262      25.267  -0.707  43.524  1.00 46.09           O  
ANISOU 2153  O   ASN A 262     5062   6833   5617    203     34   1218       O  
ATOM   2154  CB  ASN A 262      26.774   1.219  45.663  1.00 34.44           C  
ANISOU 2154  CB  ASN A 262     3455   5917   3712    332     33   1046       C  
ATOM   2155  CG  ASN A 262      27.641   1.219  46.912  1.00 43.29           C  
ANISOU 2155  CG  ASN A 262     4447   7335   4668    436     63   1081       C  
ATOM   2156  OD1 ASN A 262      27.715   2.218  47.630  1.00 43.39           O  
ANISOU 2156  OD1 ASN A 262     4403   7547   4536    475     41    951       O  
ATOM   2157  ND2 ASN A 262      28.312   0.111  47.165  1.00 37.90           N  
ANISOU 2157  ND2 ASN A 262     3708   6687   4005    489    115   1246       N  
ATOM   2158  N   LEU A 263      26.280   1.096  42.613  1.00 33.63           N  
ANISOU 2158  N   LEU A 263     3638   5227   3912    141    -38    896       N  
ATOM   2159  CA  LEU A 263      25.335   1.263  41.521  1.00 35.70           C  
ANISOU 2159  CA  LEU A 263     3990   5292   4282     82    -71    832       C  
ATOM   2160  C   LEU A 263      25.176  -0.058  40.777  1.00 42.79           C  
ANISOU 2160  C   LEU A 263     4899   6004   5354     60    -65    932       C  
ATOM   2161  O   LEU A 263      24.092  -0.622  40.738  1.00 40.97           O  
ANISOU 2161  O   LEU A 263     4632   5705   5228     51    -59   1009       O  
ATOM   2162  CB  LEU A 263      25.848   2.352  40.573  1.00 29.28           C  
ANISOU 2162  CB  LEU A 263     3293   4393   3438     40   -107    644       C  
ATOM   2163  CG  LEU A 263      24.998   2.942  39.438  1.00 34.90           C  
ANISOU 2163  CG  LEU A 263     4103   4949   4210      0   -139    540       C  
ATOM   2164  CD1 LEU A 263      25.491   2.487  38.069  1.00 40.56           C  
ANISOU 2164  CD1 LEU A 263     4905   5482   5023    -25   -160    503       C  
ATOM   2165  CD2 LEU A 263      23.503   2.699  39.633  1.00 30.52           C  
ANISOU 2165  CD2 LEU A 263     3509   4386   3700      2   -142    601       C  
ATOM   2166  N   PHE A 264      26.272  -0.554  40.210  1.00 46.06           N  
ANISOU 2166  N   PHE A 264     5355   6341   5805     54    -67    924       N  
ATOM   2167  CA  PHE A 264      26.229  -1.744  39.363  1.00 43.79           C  
ANISOU 2167  CA  PHE A 264     5086   5861   5691     34    -71    980       C  
ATOM   2168  C   PHE A 264      25.801  -2.982  40.120  1.00 46.00           C  
ANISOU 2168  C   PHE A 264     5253   6146   6080     63    -16   1180       C  
ATOM   2169  O   PHE A 264      24.964  -3.737  39.630  1.00 56.83           O  
ANISOU 2169  O   PHE A 264     6607   7361   7623     35    -19   1217       O  
ATOM   2170  CB  PHE A 264      27.560  -1.952  38.627  1.00 33.03           C  
ANISOU 2170  CB  PHE A 264     3790   4432   4326     32    -87    926       C  
ATOM   2171  CG  PHE A 264      27.736  -1.027  37.446  1.00 43.70           C  
ANISOU 2171  CG  PHE A 264     5257   5697   5650      0   -137    750       C  
ATOM   2172  CD1 PHE A 264      28.669   0.004  37.479  1.00 39.47           C  
ANISOU 2172  CD1 PHE A 264     4764   5248   4985      0   -141    655       C  
ATOM   2173  CD2 PHE A 264      26.916  -1.163  36.311  1.00 43.95           C  
ANISOU 2173  CD2 PHE A 264     5340   5569   5789    -23   -177    680       C  
ATOM   2174  CE1 PHE A 264      28.820   0.868  36.385  1.00 41.25           C  
ANISOU 2174  CE1 PHE A 264     5087   5388   5199    -21   -171    518       C  
ATOM   2175  CE2 PHE A 264      27.044  -0.300  35.205  1.00 40.67           C  
ANISOU 2175  CE2 PHE A 264     5021   5094   5339    -30   -213    537       C  
ATOM   2176  CZ  PHE A 264      27.998   0.714  35.231  1.00 39.63           C  
ANISOU 2176  CZ  PHE A 264     4935   5034   5087    -28   -205    468       C  
ATOM   2177  N   ARG A 265      26.356  -3.170  41.315  1.00 39.79           N  
ANISOU 2177  N   ARG A 265     4377   5544   5198    126     38   1305       N  
ATOM   2178  CA  ARG A 265      25.960  -4.274  42.189  1.00 43.09           C  
ANISOU 2178  CA  ARG A 265     4670   5998   5706    175    111   1529       C  
ATOM   2179  C   ARG A 265      24.448  -4.384  42.302  1.00 49.32           C  
ANISOU 2179  C   ARG A 265     5408   6733   6597    152    117   1581       C  
ATOM   2180  O   ARG A 265      23.880  -5.483  42.258  1.00 62.52           O  
ANISOU 2180  O   ARG A 265     7016   8275   8465    144    158   1717       O  
ATOM   2181  CB  ARG A 265      26.555  -4.131  43.611  1.00 35.88           C  
ANISOU 2181  CB  ARG A 265     3650   5366   4617    271    168   1645       C  
ATOM   2182  CG  ARG A 265      26.114  -5.276  44.567  1.00 41.01           C  
ANISOU 2182  CG  ARG A 265     4154   6071   5357    345    262   1914       C  
ATOM   2183  CD  ARG A 265      26.145  -4.918  46.097  1.00 44.50           C  
ANISOU 2183  CD  ARG A 265     4462   6845   5601    461    315   2029       C  
ATOM   2184  NE  ARG A 265      27.327  -4.130  46.413  1.00 46.97           N  
ANISOU 2184  NE  ARG A 265     4793   7352   5700    500    288   1902       N  
ATOM   2185  CZ  ARG A 265      27.337  -2.927  46.982  1.00 47.03           C  
ANISOU 2185  CZ  ARG A 265     4785   7572   5513    525    249   1765       C  
ATOM   2186  NH1 ARG A 265      28.502  -2.318  47.156  1.00 49.59           N  
ANISOU 2186  NH1 ARG A 265     5121   8038   5682    548    226   1635       N  
ATOM   2187  NH2 ARG A 265      26.219  -2.343  47.401  1.00 47.24           N  
ANISOU 2187  NH2 ARG A 265     4773   7673   5502    531    235   1751       N  
ATOM   2188  N   ASN A 266      23.799  -3.238  42.448  1.00 43.21           N  
ANISOU 2188  N   ASN A 266     4659   6055   5702    140     79   1471       N  
ATOM   2189  CA  ASN A 266      22.399  -3.208  42.812  1.00 47.84           C  
ANISOU 2189  CA  ASN A 266     5183   6657   6337    136     89   1533       C  
ATOM   2190  C   ASN A 266      21.478  -3.133  41.617  1.00 50.79           C  
ANISOU 2190  C   ASN A 266     5632   6825   6842     56     35   1408       C  
ATOM   2191  O   ASN A 266      20.268  -3.326  41.730  1.00 55.76           O  
ANISOU 2191  O   ASN A 266     6207   7424   7557     40     43   1460       O  
ATOM   2192  CB  ASN A 266      22.144  -2.053  43.775  1.00 52.72           C  
ANISOU 2192  CB  ASN A 266     5767   7522   6741    185     83   1496       C  
ATOM   2193  CG  ASN A 266      22.666  -2.344  45.167  1.00 61.41           C  
ANISOU 2193  CG  ASN A 266     6738   8868   7728    289    148   1661       C  
ATOM   2194  OD1 ASN A 266      22.406  -3.410  45.712  1.00 67.38           O  
ANISOU 2194  OD1 ASN A 266     7386   9630   8585    333    219   1878       O  
ATOM   2195  ND2 ASN A 266      23.416  -1.404  45.744  1.00 59.30           N  
ANISOU 2195  ND2 ASN A 266     6470   8807   7255    336    129   1560       N  
ATOM   2196  N   ILE A 267      22.056  -2.866  40.460  1.00 53.51           N  
ANISOU 2196  N   ILE A 267     6093   7040   7199     16    -19   1246       N  
ATOM   2197  CA  ILE A 267      21.253  -2.663  39.267  1.00 55.33           C  
ANISOU 2197  CA  ILE A 267     6393   7112   7517    -38    -75   1104       C  
ATOM   2198  C   ILE A 267      20.398  -3.884  38.868  1.00 66.34           C  
ANISOU 2198  C   ILE A 267     7719   8333   9153    -72    -65   1172       C  
ATOM   2199  O   ILE A 267      19.241  -3.731  38.467  1.00 65.19           O  
ANISOU 2199  O   ILE A 267     7566   8136   9068   -103    -91   1112       O  
ATOM   2200  CB  ILE A 267      22.119  -2.118  38.113  1.00 49.60           C  
ANISOU 2200  CB  ILE A 267     5795   6308   6743    -54   -127    931       C  
ATOM   2201  CG1 ILE A 267      22.173  -0.580  38.212  1.00 47.72           C  
ANISOU 2201  CG1 ILE A 267     5625   6192   6314    -44   -148    810       C  
ATOM   2202  CG2 ILE A 267      21.585  -2.582  36.747  1.00 39.48           C  
ANISOU 2202  CG2 ILE A 267     4553   4833   5613    -87   -175    825       C  
ATOM   2203  CD1 ILE A 267      23.037   0.089  37.175  1.00 41.94           C  
ANISOU 2203  CD1 ILE A 267     5007   5400   5530    -51   -182    663       C  
ATOM   2204  N   PRO A 268      20.946  -5.101  39.010  1.00 68.80           N  
ANISOU 2204  N   PRO A 268     7971   8556   9612    -65    -22   1295       N  
ATOM   2205  CA  PRO A 268      20.168  -6.251  38.547  1.00 68.78           C  
ANISOU 2205  CA  PRO A 268     7899   8360   9874   -106    -13   1333       C  
ATOM   2206  C   PRO A 268      19.037  -6.571  39.521  1.00 63.37           C  
ANISOU 2206  C   PRO A 268     7085   7728   9266   -103     48   1501       C  
ATOM   2207  O   PRO A 268      17.972  -7.015  39.087  1.00 63.49           O  
ANISOU 2207  O   PRO A 268     7049   7616   9459   -151     37   1473       O  
ATOM   2208  CB  PRO A 268      21.199  -7.387  38.518  1.00 71.84           C  
ANISOU 2208  CB  PRO A 268     8261   8645  10391    -89     27   1428       C  
ATOM   2209  CG  PRO A 268      22.544  -6.743  38.818  1.00 70.07           C  
ANISOU 2209  CG  PRO A 268     8110   8570   9945    -42     25   1415       C  
ATOM   2210  CD  PRO A 268      22.235  -5.514  39.586  1.00 70.17           C  
ANISOU 2210  CD  PRO A 268     8130   8796   9735    -19     24   1403       C  
ATOM   2211  N   TRP A 269      19.271  -6.345  40.812  1.00 56.87           N  
ANISOU 2211  N   TRP A 269     6199   7102   8306    -42    110   1667       N  
ATOM   2212  CA  TRP A 269      18.222  -6.480  41.827  1.00 55.46           C  
ANISOU 2212  CA  TRP A 269     5896   7024   8153    -18    169   1838       C  
ATOM   2213  C   TRP A 269      17.077  -5.516  41.531  1.00 58.10           C  
ANISOU 2213  C   TRP A 269     6267   7402   8407    -51    109   1702       C  
ATOM   2214  O   TRP A 269      16.004  -5.641  42.099  1.00 58.03           O  
ANISOU 2214  O   TRP A 269     6161   7439   8448    -48    143   1809       O  
ATOM   2215  CB  TRP A 269      18.782  -6.181  43.220  1.00 51.13           C  
ANISOU 2215  CB  TRP A 269     5281   6736   7409     79    231   2003       C  
ATOM   2216  CG  TRP A 269      17.821  -6.408  44.372  1.00 63.72           C  
ANISOU 2216  CG  TRP A 269     6727   8466   9016    131    305   2216       C  
ATOM   2217  CD1 TRP A 269      17.821  -7.469  45.229  1.00 77.22           C  
ANISOU 2217  CD1 TRP A 269     8292  10197  10852    190    414   2487       C  
ATOM   2218  CD2 TRP A 269      16.752  -5.551  44.805  1.00 57.28           C  
ANISOU 2218  CD2 TRP A 269     5888   7796   8080    142    281   2191       C  
ATOM   2219  NE1 TRP A 269      16.817  -7.336  46.155  1.00 71.67           N  
ANISOU 2219  NE1 TRP A 269     7471   9646  10113    238    461   2638       N  
ATOM   2220  CE2 TRP A 269      16.145  -6.167  45.919  1.00 61.90           C  
ANISOU 2220  CE2 TRP A 269     6308   8491   8721    208    376   2454       C  
ATOM   2221  CE3 TRP A 269      16.244  -4.330  44.357  1.00 46.17           C  
ANISOU 2221  CE3 TRP A 269     4579   6437   6525    109    196   1983       C  
ATOM   2222  CZ2 TRP A 269      15.064  -5.606  46.593  1.00 61.58           C  
ANISOU 2222  CZ2 TRP A 269     6199   8615   8583    242    379   2506       C  
ATOM   2223  CZ3 TRP A 269      15.169  -3.774  45.024  1.00 53.46           C  
ANISOU 2223  CZ3 TRP A 269     5440   7514   7357    140    199   2028       C  
ATOM   2224  CH2 TRP A 269      14.590  -4.412  46.133  1.00 60.93           C  
ANISOU 2224  CH2 TRP A 269     6222   8577   8352    205    286   2284       C  
ATOM   2225  N   VAL A 270      17.311  -4.550  40.647  1.00 56.36           N  
ANISOU 2225  N   VAL A 270     6181   7171   8061    -75     28   1478       N  
ATOM   2226  CA  VAL A 270      16.285  -3.568  40.317  1.00 60.00           C  
ANISOU 2226  CA  VAL A 270     6687   7678   8432    -94    -23   1347       C  
ATOM   2227  C   VAL A 270      15.571  -3.948  39.035  1.00 67.09           C  
ANISOU 2227  C   VAL A 270     7610   8379   9502   -156    -73   1207       C  
ATOM   2228  O   VAL A 270      14.361  -3.753  38.911  1.00 70.85           O  
ANISOU 2228  O   VAL A 270     8052   8857  10009   -177    -89   1174       O  
ATOM   2229  CB  VAL A 270      16.861  -2.153  40.141  1.00 52.46           C  
ANISOU 2229  CB  VAL A 270     5855   6841   7235    -70    -70   1189       C  
ATOM   2230  CG1 VAL A 270      15.788  -1.213  39.609  1.00 44.40           C  
ANISOU 2230  CG1 VAL A 270     4888   5833   6148    -86   -119   1050       C  
ATOM   2231  CG2 VAL A 270      17.420  -1.635  41.448  1.00 53.82           C  
ANISOU 2231  CG2 VAL A 270     5986   7237   7225     -5    -32   1286       C  
ATOM   2232  N   GLU A 271      16.331  -4.463  38.073  1.00 70.24           N  
ANISOU 2232  N   GLU A 271     8063   8626  10000   -177   -102   1114       N  
ATOM   2233  CA  GLU A 271      15.749  -4.982  36.841  1.00 69.84           C  
ANISOU 2233  CA  GLU A 271     8013   8397  10127   -222   -153    970       C  
ATOM   2234  C   GLU A 271      14.916  -6.201  37.206  1.00 79.86           C  
ANISOU 2234  C   GLU A 271     9133   9552  11658   -261   -105   1098       C  
ATOM   2235  O   GLU A 271      13.955  -6.557  36.511  1.00 79.80           O  
ANISOU 2235  O   GLU A 271     9079   9435  11805   -304   -138    996       O  
ATOM   2236  CB  GLU A 271      16.837  -5.371  35.840  1.00 57.88           C  
ANISOU 2236  CB  GLU A 271     6571   6760   8662   -219   -191    859       C  
ATOM   2237  CG  GLU A 271      17.692  -4.215  35.359  1.00 54.62           C  
ANISOU 2237  CG  GLU A 271     6297   6437   8020   -183   -231    736       C  
ATOM   2238  CD  GLU A 271      18.594  -4.603  34.200  1.00 55.18           C  
ANISOU 2238  CD  GLU A 271     6431   6389   8145   -173   -276    614       C  
ATOM   2239  OE1 GLU A 271      18.568  -3.912  33.157  1.00 57.03           O  
ANISOU 2239  OE1 GLU A 271     6747   6626   8294   -152   -331    446       O  
ATOM   2240  OE2 GLU A 271      19.330  -5.603  34.330  1.00 55.01           O  
ANISOU 2240  OE2 GLU A 271     6373   6281   8248   -177   -252    692       O  
ATOM   2241  N   GLU A 272      15.337  -6.845  38.293  1.00 79.23           N  
ANISOU 2241  N   GLU A 272     8968   9505  11629   -240    -22   1324       N  
ATOM   2242  CA  GLU A 272      14.657  -7.977  38.898  1.00 80.37           C  
ANISOU 2242  CA  GLU A 272     8957   9547  12033   -266     51   1499       C  
ATOM   2243  C   GLU A 272      13.333  -7.676  39.572  1.00 73.62           C  
ANISOU 2243  C   GLU A 272     8023   8797  11151   -273     70   1568       C  
ATOM   2244  O   GLU A 272      12.336  -8.261  39.272  1.00 72.63           O  
ANISOU 2244  O   GLU A 272     7816   8553  11226   -329     64   1531       O  
ATOM   2245  CB  GLU A 272      15.607  -8.536  39.961  1.00 91.55           C  
ANISOU 2245  CB  GLU A 272    10306  11004  13476   -215    148   1746       C  
ATOM   2246  CG  GLU A 272      15.248  -9.838  40.649  1.00104.68           C  
ANISOU 2246  CG  GLU A 272    11792  12589  15391   -221    253   1987       C  
ATOM   2247  CD  GLU A 272      16.206 -10.167  41.818  1.00112.37           C  
ANISOU 2247  CD  GLU A 272    12700  13269  16728   -294    257   1935       C  
ATOM   2248  OE1 GLU A 272      15.726 -10.289  42.967  1.00114.07           O  
ANISOU 2248  OE1 GLU A 272    12762  13380  17200   -312    347   2119       O  
ATOM   2249  OE2 GLU A 272      17.435 -10.310  41.596  1.00114.13           O  
ANISOU 2249  OE2 GLU A 272    13013  13365  16986   -327    173   1709       O  
ATOM   2250  N   ASN A 273      13.312  -6.694  40.432  1.00 68.35           N  
ANISOU 2250  N   ASN A 273     7371   8362  10235   -213     90   1658       N  
ATOM   2251  CA  ASN A 273      12.115  -6.375  41.189  1.00 66.08           C  
ANISOU 2251  CA  ASN A 273     6996   8201   9910   -202    118   1759       C  
ATOM   2252  C   ASN A 273      11.252  -5.266  40.563  1.00 70.02           C  
ANISOU 2252  C   ASN A 273     7578   8762  10263   -221     34   1555       C  
ATOM   2253  O   ASN A 273      10.085  -5.105  40.933  1.00 73.92           O  
ANISOU 2253  O   ASN A 273     7999   9324  10765   -226     45   1604       O  
ATOM   2254  CB  ASN A 273      12.479  -6.052  42.645  1.00 54.76           C  
ANISOU 2254  CB  ASN A 273     5508   7007   8291   -110    186   1970       C  
ATOM   2255  CG  ASN A 273      13.080  -7.256  43.388  1.00 64.34           C  
ANISOU 2255  CG  ASN A 273     6603   8178   9667    -74    291   2223       C  
ATOM   2256  OD1 ASN A 273      12.371  -7.976  44.102  1.00 65.34           O  
ANISOU 2256  OD1 ASN A 273     6578   8303   9944    -60    376   2440       O  
ATOM   2257  ND2 ASN A 273      14.388  -7.476  43.223  1.00 62.00           N  
ANISOU 2257  ND2 ASN A 273     6370   7849   9339    -51    294   2206       N  
ATOM   2258  N   PHE A 274      11.806  -4.523  39.604  1.00 60.64           N  
ANISOU 2258  N   PHE A 274     6536   7554   8949   -224    -41   1337       N  
ATOM   2259  CA  PHE A 274      11.118  -3.328  39.101  1.00 55.86           C  
ANISOU 2259  CA  PHE A 274     6017   7036   8170   -218   -105   1165       C  
ATOM   2260  C   PHE A 274      11.036  -3.124  37.584  1.00 56.33           C  
ANISOU 2260  C   PHE A 274     6168   6974   8261   -245   -181    923       C  
ATOM   2261  O   PHE A 274      10.338  -2.214  37.121  1.00 50.60           O  
ANISOU 2261  O   PHE A 274     5499   6316   7410   -231   -224    795       O  
ATOM   2262  CB  PHE A 274      11.668  -2.068  39.776  1.00 49.14           C  
ANISOU 2262  CB  PHE A 274     5250   6388   7034   -154   -108   1163       C  
ATOM   2263  CG  PHE A 274      11.241  -1.927  41.209  1.00 53.91           C  
ANISOU 2263  CG  PHE A 274     5755   7180   7550   -105    -54   1352       C  
ATOM   2264  CD1 PHE A 274      10.014  -1.365  41.527  1.00 56.02           C  
ANISOU 2264  CD1 PHE A 274     5986   7556   7743    -93    -63   1355       C  
ATOM   2265  CD2 PHE A 274      12.050  -2.386  42.238  1.00 56.98           C  
ANISOU 2265  CD2 PHE A 274     6074   7653   7921    -59      8   1532       C  
ATOM   2266  CE1 PHE A 274       9.606  -1.245  42.855  1.00 58.58           C  
ANISOU 2266  CE1 PHE A 274     6208   8074   7976    -34    -15   1533       C  
ATOM   2267  CE2 PHE A 274      11.646  -2.274  43.567  1.00 58.13           C  
ANISOU 2267  CE2 PHE A 274     6112   8003   7973      8     60   1712       C  
ATOM   2268  CZ  PHE A 274      10.422  -1.703  43.873  1.00 56.74           C  
ANISOU 2268  CZ  PHE A 274     5901   7936   7723     21     47   1712       C  
ATOM   2269  N   GLY A 275      11.718  -3.960  36.809  1.00 56.99           N  
ANISOU 2269  N   GLY A 275     6258   6890   8504   -271   -196    863       N  
ATOM   2270  CA  GLY A 275      11.631  -3.851  35.361  1.00 59.22           C  
ANISOU 2270  CA  GLY A 275     6606   7079   8816   -278   -269    635       C  
ATOM   2271  C   GLY A 275      12.918  -3.385  34.707  1.00 69.92           C  
ANISOU 2271  C   GLY A 275     8090   8427  10048   -241   -300    537       C  
ATOM   2272  O   GLY A 275      13.962  -3.325  35.355  1.00 74.72           O  
ANISOU 2272  O   GLY A 275     8731   9076  10585   -224   -265    641       O  
ATOM   2273  N   GLU A 276      12.837  -2.983  33.446  1.00 72.40           N  
ANISOU 2273  N   GLU A 276     8470   8705  10332   -220   -362    338       N  
ATOM   2274  CA  GLU A 276      14.001  -2.584  32.668  1.00 78.39           C  
ANISOU 2274  CA  GLU A 276     9341   9452  10991   -179   -388    248       C  
ATOM   2275  C   GLU A 276      14.722  -1.370  33.233  1.00 72.55           C  
ANISOU 2275  C   GLU A 276     8703   8848  10015   -143   -362    296       C  
ATOM   2276  O   GLU A 276      14.104  -0.426  33.664  1.00 68.36           O  
ANISOU 2276  O   GLU A 276     8188   8433   9354   -130   -349    311       O  
ATOM   2277  CB  GLU A 276      13.617  -2.333  31.194  1.00 92.00           C  
ANISOU 2277  CB  GLU A 276    11101  11145  12709   -139   -455     35       C  
ATOM   2278  CG  GLU A 276      13.631  -3.597  30.282  1.00106.24           C  
ANISOU 2278  CG  GLU A 276    12915  13052  14400   -111   -472    -51       C  
ATOM   2279  CD  GLU A 276      13.736  -3.314  28.752  1.00115.26           C  
ANISOU 2279  CD  GLU A 276    14070  14187  15535    -52   -533   -258       C  
ATOM   2280  OE1 GLU A 276      12.865  -2.608  28.179  1.00113.06           O  
ANISOU 2280  OE1 GLU A 276    13804  14006  15149    -10   -545   -337       O  
ATOM   2281  OE2 GLU A 276      14.682  -3.835  28.112  1.00120.33           O  
ANISOU 2281  OE2 GLU A 276    14707  14744  16270    -34   -569   -343       O  
ATOM   2282  N   VAL A 277      16.045  -1.403  33.211  1.00 64.32           N  
ANISOU 2282  N   VAL A 277     7721   7788   8929   -128   -354    312       N  
ATOM   2283  CA  VAL A 277      16.835  -0.274  33.683  1.00 62.34           C  
ANISOU 2283  CA  VAL A 277     7556   7648   8482   -100   -331    332       C  
ATOM   2284  C   VAL A 277      17.748   0.245  32.568  1.00 65.94           C  
ANISOU 2284  C   VAL A 277     8116   8072   8868    -61   -358    211       C  
ATOM   2285  O   VAL A 277      18.644  -0.471  32.112  1.00 73.95           O  
ANISOU 2285  O   VAL A 277     9137   9005   9957    -60   -370    204       O  
ATOM   2286  CB  VAL A 277      17.696  -0.662  34.908  1.00 59.08           C  
ANISOU 2286  CB  VAL A 277     7102   7282   8063   -113   -283    489       C  
ATOM   2287  CG1 VAL A 277      18.943   0.217  34.999  1.00 63.35           C  
ANISOU 2287  CG1 VAL A 277     7730   7890   8449    -88   -274    460       C  
ATOM   2288  CG2 VAL A 277      16.879  -0.585  36.192  1.00 52.96           C  
ANISOU 2288  CG2 VAL A 277     6243   6619   7261   -120   -245    617       C  
ATOM   2289  N   ASP A 278      17.517   1.478  32.123  1.00 52.64           N  
ANISOU 2289  N   ASP A 278     6508   6449   7044    -22   -360    126       N  
ATOM   2290  CA  ASP A 278      18.433   2.109  31.182  1.00 51.39           C  
ANISOU 2290  CA  ASP A 278     6442   6274   6809     25   -366     43       C  
ATOM   2291  C   ASP A 278      19.748   2.438  31.887  1.00 48.06           C  
ANISOU 2291  C   ASP A 278     6054   5884   6323     10   -332    109       C  
ATOM   2292  O   ASP A 278      19.829   3.374  32.690  1.00 50.93           O  
ANISOU 2292  O   ASP A 278     6436   6332   6583      4   -300    134       O  
ATOM   2293  CB  ASP A 278      17.824   3.363  30.552  1.00 55.35           C  
ANISOU 2293  CB  ASP A 278     7008   6830   7194     80   -360    -44       C  
ATOM   2294  CG  ASP A 278      18.746   4.006  29.521  1.00 62.70           C  
ANISOU 2294  CG  ASP A 278     8022   7741   8059    141   -352   -107       C  
ATOM   2295  OD1 ASP A 278      18.249   4.765  28.663  1.00 62.44           O  
ANISOU 2295  OD1 ASP A 278     8029   7734   7960    209   -347   -179       O  
ATOM   2296  OD2 ASP A 278      19.972   3.761  29.571  1.00 66.76           O  
ANISOU 2296  OD2 ASP A 278     8556   8222   8586    128   -346    -76       O  
ATOM   2297  N   ARG A 279      20.778   1.661  31.577  1.00 42.78           N  
ANISOU 2297  N   ARG A 279     5386   5152   5717      7   -343    125       N  
ATOM   2298  CA  ARG A 279      22.055   1.789  32.259  1.00 48.21           C  
ANISOU 2298  CA  ARG A 279     6090   5876   6352     -8   -314    188       C  
ATOM   2299  C   ARG A 279      22.760   3.097  31.970  1.00 48.26           C  
ANISOU 2299  C   ARG A 279     6177   5921   6237     17   -291    128       C  
ATOM   2300  O   ARG A 279      23.482   3.612  32.836  1.00 45.68           O  
ANISOU 2300  O   ARG A 279     5850   5663   5843     -2   -260    161       O  
ATOM   2301  CB  ARG A 279      22.959   0.615  31.923  1.00 48.30           C  
ANISOU 2301  CB  ARG A 279     6083   5808   6459    -10   -330    218       C  
ATOM   2302  CG  ARG A 279      22.277  -0.685  32.203  1.00 54.32           C  
ANISOU 2302  CG  ARG A 279     6757   6506   7377    -37   -340    280       C  
ATOM   2303  CD  ARG A 279      23.250  -1.795  32.420  1.00 56.64           C  
ANISOU 2303  CD  ARG A 279     7017   6744   7758    -44   -332    358       C  
ATOM   2304  NE  ARG A 279      22.522  -3.049  32.522  1.00 69.33           N  
ANISOU 2304  NE  ARG A 279     8534   8254   9554    -69   -335    408       N  
ATOM   2305  CZ  ARG A 279      23.097  -4.243  32.525  1.00 78.91           C  
ANISOU 2305  CZ  ARG A 279     9705   9376  10903    -73   -329    468       C  
ATOM   2306  NH1 ARG A 279      22.341  -5.333  32.607  1.00 80.51           N  
ANISOU 2306  NH1 ARG A 279     9814   9470  11307   -100   -324    508       N  
ATOM   2307  NH2 ARG A 279      24.423  -4.342  32.439  1.00 79.40           N  
ANISOU 2307  NH2 ARG A 279     9811   9449  10910    -50   -324    487       N  
ATOM   2308  N   PHE A 280      22.552   3.628  30.763  1.00 33.82           N  
ANISOU 2308  N   PHE A 280     4407   4054   4389     66   -303     41       N  
ATOM   2309  CA  PHE A 280      23.136   4.907  30.391  1.00 32.01           C  
ANISOU 2309  CA  PHE A 280     4249   3843   4071     96   -267     -3       C  
ATOM   2310  C   PHE A 280      22.682   6.011  31.379  1.00 35.54           C  
ANISOU 2310  C   PHE A 280     4696   4363   4446     73   -229      0       C  
ATOM   2311  O   PHE A 280      23.493   6.779  31.886  1.00 33.73           O  
ANISOU 2311  O   PHE A 280     4482   4162   4170     55   -194     -5       O  
ATOM   2312  CB  PHE A 280      22.786   5.261  28.933  1.00 30.12           C  
ANISOU 2312  CB  PHE A 280     4056   3569   3821    174   -275    -76       C  
ATOM   2313  CG  PHE A 280      23.305   6.609  28.489  1.00 28.15           C  
ANISOU 2313  CG  PHE A 280     3872   3324   3499    216   -220    -98       C  
ATOM   2314  CD1 PHE A 280      24.668   6.875  28.473  1.00 31.51           C  
ANISOU 2314  CD1 PHE A 280     4323   3732   3918    206   -193    -78       C  
ATOM   2315  CD2 PHE A 280      22.430   7.603  28.078  1.00 24.67           C  
ANISOU 2315  CD2 PHE A 280     3461   2902   3009    269   -189   -132       C  
ATOM   2316  CE1 PHE A 280      25.152   8.122  28.073  1.00 30.57           C  
ANISOU 2316  CE1 PHE A 280     4253   3600   3764    239   -130    -90       C  
ATOM   2317  CE2 PHE A 280      22.903   8.849  27.673  1.00 32.92           C  
ANISOU 2317  CE2 PHE A 280     4559   3934   4015    311   -122   -137       C  
ATOM   2318  CZ  PHE A 280      24.279   9.108  27.682  1.00 28.17           C  
ANISOU 2318  CZ  PHE A 280     3976   3299   3427    291    -91   -114       C  
ATOM   2319  N   TYR A 281      21.384   6.072  31.642  1.00 35.35           N  
ANISOU 2319  N   TYR A 281     4645   4370   4416     74   -238     -3       N  
ATOM   2320  CA  TYR A 281      20.832   7.053  32.561  1.00 36.74           C  
ANISOU 2320  CA  TYR A 281     4815   4622   4521     63   -210     -7       C  
ATOM   2321  C   TYR A 281      21.140   6.745  34.029  1.00 36.98           C  
ANISOU 2321  C   TYR A 281     4775   4739   4535     18   -207     58       C  
ATOM   2322  O   TYR A 281      21.373   7.661  34.823  1.00 29.41           O  
ANISOU 2322  O   TYR A 281     3813   3853   3509     12   -181     34       O  
ATOM   2323  CB  TYR A 281      19.331   7.142  32.375  1.00 36.41           C  
ANISOU 2323  CB  TYR A 281     4761   4601   4471     87   -224    -24       C  
ATOM   2324  CG  TYR A 281      18.956   8.039  31.254  1.00 34.46           C  
ANISOU 2324  CG  TYR A 281     4582   4325   4185    153   -204    -94       C  
ATOM   2325  CD1 TYR A 281      18.218   9.177  31.492  1.00 34.66           C  
ANISOU 2325  CD1 TYR A 281     4634   4395   4142    179   -172   -122       C  
ATOM   2326  CD2 TYR A 281      19.376   7.779  29.954  1.00 48.12           C  
ANISOU 2326  CD2 TYR A 281     6347   5994   5942    203   -213   -128       C  
ATOM   2327  CE1 TYR A 281      17.886  10.022  30.484  1.00 44.81           C  
ANISOU 2327  CE1 TYR A 281     5978   5658   5390    253   -139   -168       C  
ATOM   2328  CE2 TYR A 281      19.043   8.636  28.920  1.00 44.00           C  
ANISOU 2328  CE2 TYR A 281     5878   5468   5372    286   -183   -175       C  
ATOM   2329  CZ  TYR A 281      18.294   9.750  29.207  1.00 40.42           C  
ANISOU 2329  CZ  TYR A 281     5450   5053   4856    310   -141   -188       C  
ATOM   2330  OH  TYR A 281      17.929  10.625  28.245  1.00 43.32           O  
ANISOU 2330  OH  TYR A 281     5864   5420   5174    403    -98   -216       O  
ATOM   2331  N   ALA A 282      21.121   5.466  34.385  1.00 28.95           N  
ANISOU 2331  N   ALA A 282     3695   3722   3584     -5   -228    139       N  
ATOM   2332  CA  ALA A 282      21.493   5.078  35.733  1.00 33.89           C  
ANISOU 2332  CA  ALA A 282     4243   4447   4187    -26   -215    224       C  
ATOM   2333  C   ALA A 282      22.869   5.658  36.026  1.00 36.73           C  
ANISOU 2333  C   ALA A 282     4623   4844   4487    -30   -194    189       C  
ATOM   2334  O   ALA A 282      23.072   6.314  37.055  1.00 35.02           O  
ANISOU 2334  O   ALA A 282     4369   4746   4192    -29   -177    175       O  
ATOM   2335  CB  ALA A 282      21.521   3.576  35.860  1.00 35.42           C  
ANISOU 2335  CB  ALA A 282     4371   4602   4484    -40   -226    328       C  
ATOM   2336  N   VAL A 283      23.811   5.435  35.111  1.00 29.96           N  
ANISOU 2336  N   VAL A 283     3818   3897   3668    -30   -198    163       N  
ATOM   2337  CA  VAL A 283      25.178   5.934  35.296  1.00 33.03           C  
ANISOU 2337  CA  VAL A 283     4221   4313   4014    -39   -177    129       C  
ATOM   2338  C   VAL A 283      25.247   7.457  35.292  1.00 31.32           C  
ANISOU 2338  C   VAL A 283     4045   4109   3745    -38   -149     27       C  
ATOM   2339  O   VAL A 283      26.108   8.047  35.938  1.00 32.95           O  
ANISOU 2339  O   VAL A 283     4227   4381   3912    -53   -129    -16       O  
ATOM   2340  CB  VAL A 283      26.156   5.384  34.227  1.00 33.69           C  
ANISOU 2340  CB  VAL A 283     4353   4298   4149    -32   -187    129       C  
ATOM   2341  CG1 VAL A 283      27.578   5.810  34.538  1.00 34.21           C  
ANISOU 2341  CG1 VAL A 283     4419   4407   4173    -46   -164    103       C  
ATOM   2342  CG2 VAL A 283      26.099   3.888  34.200  1.00 27.16           C  
ANISOU 2342  CG2 VAL A 283     3486   3439   3396    -32   -212    216       C  
ATOM   2343  N   LEU A 284      24.350   8.103  34.562  1.00 30.29           N  
ANISOU 2343  N   LEU A 284     3968   3918   3624    -15   -143    -16       N  
ATOM   2344  CA  LEU A 284      24.370   9.562  34.532  1.00 32.34           C  
ANISOU 2344  CA  LEU A 284     4264   4168   3855     -9   -104   -103       C  
ATOM   2345  C   LEU A 284      23.835  10.147  35.839  1.00 33.85           C  
ANISOU 2345  C   LEU A 284     4396   4478   3987    -19   -101   -133       C  
ATOM   2346  O   LEU A 284      24.233  11.245  36.247  1.00 30.39           O  
ANISOU 2346  O   LEU A 284     3954   4059   3533    -27    -72   -219       O  
ATOM   2347  CB  LEU A 284      23.582  10.113  33.339  1.00 34.90           C  
ANISOU 2347  CB  LEU A 284     4661   4403   4198     37    -87   -128       C  
ATOM   2348  CG  LEU A 284      24.082   9.840  31.918  1.00 28.97           C  
ANISOU 2348  CG  LEU A 284     3965   3554   3487     75    -82   -118       C  
ATOM   2349  CD1 LEU A 284      23.175  10.505  30.877  1.00 21.52           C  
ANISOU 2349  CD1 LEU A 284     3076   2565   2536    144    -57   -142       C  
ATOM   2350  CD2 LEU A 284      25.510  10.312  31.732  1.00 28.70           C  
ANISOU 2350  CD2 LEU A 284     3949   3482   3475     60    -45   -136       C  
ATOM   2351  N   HIS A 285      22.932   9.419  36.495  1.00 32.14           N  
ANISOU 2351  N   HIS A 285     4124   4342   3746    -13   -131    -66       N  
ATOM   2352  CA  HIS A 285      22.434   9.848  37.801  1.00 28.13           C  
ANISOU 2352  CA  HIS A 285     3545   3978   3165     -6   -133    -81       C  
ATOM   2353  C   HIS A 285      23.621  10.113  38.720  1.00 32.54           C  
ANISOU 2353  C   HIS A 285     4043   4637   3684    -18   -125   -127       C  
ATOM   2354  O   HIS A 285      23.591  11.042  39.514  1.00 34.48           O  
ANISOU 2354  O   HIS A 285     4249   4974   3878     -9   -118   -216       O  
ATOM   2355  CB  HIS A 285      21.496   8.823  38.423  1.00 18.28           C  
ANISOU 2355  CB  HIS A 285     2227   2813   1905      6   -159     31       C  
ATOM   2356  CG  HIS A 285      20.060   9.018  38.069  1.00 30.09           C  
ANISOU 2356  CG  HIS A 285     3746   4284   3401     24   -167     35       C  
ATOM   2357  ND1 HIS A 285      19.154   9.609  38.926  1.00 37.79           N  
ANISOU 2357  ND1 HIS A 285     4680   5376   4303     48   -170     22       N  
ATOM   2358  CD2 HIS A 285      19.351   8.678  36.960  1.00 30.90           C  
ANISOU 2358  CD2 HIS A 285     3902   4278   3562     28   -178     46       C  
ATOM   2359  CE1 HIS A 285      17.957   9.623  38.371  1.00 36.95           C  
ANISOU 2359  CE1 HIS A 285     4604   5228   4209     62   -178     33       C  
ATOM   2360  NE2 HIS A 285      18.052   9.053  37.175  1.00 40.92           N  
ANISOU 2360  NE2 HIS A 285     5160   5596   4791     50   -183     42       N  
ATOM   2361  N   VAL A 286      24.681   9.318  38.571  1.00 40.77           N  
ANISOU 2361  N   VAL A 286     5074   5665   4751    -35   -127    -80       N  
ATOM   2362  CA  VAL A 286      25.883   9.503  39.378  1.00 40.20           C  
ANISOU 2362  CA  VAL A 286     4938   5701   4636    -42   -119   -129       C  
ATOM   2363  C   VAL A 286      26.804  10.574  38.811  1.00 35.17           C  
ANISOU 2363  C   VAL A 286     4350   4973   4040    -71    -91   -253       C  
ATOM   2364  O   VAL A 286      27.146  11.534  39.493  1.00 31.33           O  
ANISOU 2364  O   VAL A 286     3817   4558   3530    -77    -80   -371       O  
ATOM   2365  CB  VAL A 286      26.671   8.197  39.568  1.00 34.90           C  
ANISOU 2365  CB  VAL A 286     4224   5072   3965    -39   -126    -19       C  
ATOM   2366  CG1 VAL A 286      27.910   8.466  40.419  1.00 34.59           C  
ANISOU 2366  CG1 VAL A 286     4110   5171   3863    -36   -118    -82       C  
ATOM   2367  CG2 VAL A 286      25.786   7.141  40.240  1.00 34.33           C  
ANISOU 2367  CG2 VAL A 286     4082   5085   3875     -7   -138    121       C  
ATOM   2368  N   PHE A 287      27.202  10.399  37.560  1.00 39.29           N  
ANISOU 2368  N   PHE A 287     4955   5340   4632    -84    -79   -229       N  
ATOM   2369  CA  PHE A 287      28.078  11.346  36.877  1.00 26.77           C  
ANISOU 2369  CA  PHE A 287     3416   3651   3105   -106    -40   -315       C  
ATOM   2370  C   PHE A 287      27.653  12.779  37.041  1.00 25.70           C  
ANISOU 2370  C   PHE A 287     3287   3486   2992   -109     -6   -429       C  
ATOM   2371  O   PHE A 287      28.474  13.673  37.270  1.00 30.49           O  
ANISOU 2371  O   PHE A 287     3867   4080   3639   -137     26   -535       O  
ATOM   2372  CB  PHE A 287      28.128  11.007  35.395  1.00 30.52           C  
ANISOU 2372  CB  PHE A 287     3983   3974   3640    -91    -30   -254       C  
ATOM   2373  CG  PHE A 287      29.057   9.872  35.071  1.00 31.11           C  
ANISOU 2373  CG  PHE A 287     4054   4047   3719    -94    -51   -182       C  
ATOM   2374  CD1 PHE A 287      29.987   9.443  36.002  1.00 34.59           C  
ANISOU 2374  CD1 PHE A 287     4422   4602   4118   -115    -62   -181       C  
ATOM   2375  CD2 PHE A 287      29.030   9.266  33.836  1.00 37.41           C  
ANISOU 2375  CD2 PHE A 287     4917   4742   4556    -66    -61   -124       C  
ATOM   2376  CE1 PHE A 287      30.854   8.430  35.721  1.00 35.01           C  
ANISOU 2376  CE1 PHE A 287     4475   4655   4174   -112    -77   -113       C  
ATOM   2377  CE2 PHE A 287      29.918   8.242  33.534  1.00 39.05           C  
ANISOU 2377  CE2 PHE A 287     5120   4945   4771    -64    -82    -67       C  
ATOM   2378  CZ  PHE A 287      30.825   7.823  34.471  1.00 40.47           C  
ANISOU 2378  CZ  PHE A 287     5237   5226   4914    -90    -88    -56       C  
ATOM   2379  N   LEU A 288      26.354  12.998  36.958  1.00 34.43           N  
ANISOU 2379  N   LEU A 288     4422   4580   4081    -80    -11   -412       N  
ATOM   2380  CA  LEU A 288      25.835  14.353  36.856  1.00 38.57           C  
ANISOU 2380  CA  LEU A 288     4973   5042   4639    -71     30   -504       C  
ATOM   2381  C   LEU A 288      25.349  14.971  38.186  1.00 38.34           C  
ANISOU 2381  C   LEU A 288     4864   5148   4554    -66     13   -599       C  
ATOM   2382  O   LEU A 288      24.762  16.049  38.203  1.00 43.58           O  
ANISOU 2382  O   LEU A 288     5547   5768   5244    -52     42   -677       O  
ATOM   2383  CB  LEU A 288      24.761  14.416  35.763  1.00 37.06           C  
ANISOU 2383  CB  LEU A 288     4870   4748   4464    -27     46   -442       C  
ATOM   2384  CG  LEU A 288      25.185  14.737  34.311  1.00 39.02           C  
ANISOU 2384  CG  LEU A 288     5199   4839   4787     -4     99   -412       C  
ATOM   2385  CD1 LEU A 288      26.597  14.305  33.949  1.00 33.24           C  
ANISOU 2385  CD1 LEU A 288     4461   4071   4096    -34    105   -394       C  
ATOM   2386  CD2 LEU A 288      24.190  14.170  33.325  1.00 31.11           C  
ANISOU 2386  CD2 LEU A 288     4254   3804   3762     52     84   -331       C  
ATOM   2387  N   GLU A 289      25.619  14.308  39.300  1.00 36.01           N  
ANISOU 2387  N   GLU A 289     4475   5027   4179    -67    -30   -593       N  
ATOM   2388  CA  GLU A 289      25.342  14.931  40.585  1.00 41.07           C  
ANISOU 2388  CA  GLU A 289     5022   5826   4756    -48    -49   -700       C  
ATOM   2389  C   GLU A 289      26.015  16.297  40.697  1.00 41.25           C  
ANISOU 2389  C   GLU A 289     5026   5789   4859    -75    -12   -882       C  
ATOM   2390  O   GLU A 289      27.172  16.466  40.293  1.00 40.35           O  
ANISOU 2390  O   GLU A 289     4915   5595   4822   -118     16   -924       O  
ATOM   2391  CB  GLU A 289      25.789  14.029  41.734  1.00 35.84           C  
ANISOU 2391  CB  GLU A 289     4245   5381   3992    -27    -90   -664       C  
ATOM   2392  CG  GLU A 289      24.886  12.820  41.927  1.00 33.06           C  
ANISOU 2392  CG  GLU A 289     3882   5106   3575      9   -118   -491       C  
ATOM   2393  CD  GLU A 289      25.279  11.980  43.140  1.00 41.99           C  
ANISOU 2393  CD  GLU A 289     4885   6466   4604     50   -141   -432       C  
ATOM   2394  OE1 GLU A 289      24.446  11.161  43.579  1.00 42.03           O  
ANISOU 2394  OE1 GLU A 289     4850   6563   4557     90   -155   -297       O  
ATOM   2395  OE2 GLU A 289      26.417  12.136  43.654  1.00 41.30           O  
ANISOU 2395  OE2 GLU A 289     4730   6473   4491     47   -141   -516       O  
ATOM   2396  N   PHE A 290      25.267  17.268  41.221  1.00 37.21           N  
ANISOU 2396  N   PHE A 290     4491   5308   4341    -51    -10   -988       N  
ATOM   2397  CA  PHE A 290      25.809  18.575  41.627  1.00 40.49           C  
ANISOU 2397  CA  PHE A 290     4853   5692   4839    -73     18  -1191       C  
ATOM   2398  C   PHE A 290      26.148  19.493  40.464  1.00 49.02           C  
ANISOU 2398  C   PHE A 290     6023   6516   6088   -110     98  -1219       C  
ATOM   2399  O   PHE A 290      26.923  20.450  40.603  1.00 49.15           O  
ANISOU 2399  O   PHE A 290     5993   6459   6222   -148    136  -1372       O  
ATOM   2400  CB  PHE A 290      27.006  18.403  42.564  1.00 37.26           C  
ANISOU 2400  CB  PHE A 290     4318   5441   4400    -92    -12  -1301       C  
ATOM   2401  CG  PHE A 290      26.677  17.630  43.803  1.00 44.10           C  
ANISOU 2401  CG  PHE A 290     5076   6586   5094    -32    -78  -1273       C  
ATOM   2402  CD1 PHE A 290      27.236  16.383  44.025  1.00 42.36           C  
ANISOU 2402  CD1 PHE A 290     4818   6487   4790    -21   -103  -1149       C  
ATOM   2403  CD2 PHE A 290      25.768  18.139  44.730  1.00 48.57           C  
ANISOU 2403  CD2 PHE A 290     5575   7298   5581     27   -110  -1356       C  
ATOM   2404  CE1 PHE A 290      26.923  15.658  45.152  1.00 45.43           C  
ANISOU 2404  CE1 PHE A 290     5099   7135   5026     50   -147  -1094       C  
ATOM   2405  CE2 PHE A 290      25.447  17.423  45.865  1.00 52.14           C  
ANISOU 2405  CE2 PHE A 290     5918   8025   5869    100   -163  -1309       C  
ATOM   2406  CZ  PHE A 290      26.022  16.177  46.077  1.00 55.54           C  
ANISOU 2406  CZ  PHE A 290     6307   8572   6222    114   -177  -1169       C  
ATOM   2407  N   TYR A 291      25.539  19.201  39.322  1.00 45.35           N  
ANISOU 2407  N   TYR A 291     5673   5920   5639    -91    128  -1071       N  
ATOM   2408  CA  TYR A 291      25.738  20.002  38.130  1.00 41.37           C  
ANISOU 2408  CA  TYR A 291     5253   5188   5276    -99    215  -1057       C  
ATOM   2409  C   TYR A 291      24.895  21.266  38.209  1.00 40.95           C  
ANISOU 2409  C   TYR A 291     5217   5059   5284    -69    261  -1144       C  
ATOM   2410  O   TYR A 291      23.699  21.226  38.491  1.00 46.81           O  
ANISOU 2410  O   TYR A 291     5977   5876   5933    -20    231  -1118       O  
ATOM   2411  CB  TYR A 291      25.368  19.203  36.872  1.00 39.58           C  
ANISOU 2411  CB  TYR A 291     5129   4884   5024    -66    226   -875       C  
ATOM   2412  CG  TYR A 291      26.538  18.585  36.143  1.00 34.65           C  
ANISOU 2412  CG  TYR A 291     4522   4199   4444    -95    239   -807       C  
ATOM   2413  CD1 TYR A 291      26.710  18.798  34.784  1.00 37.74           C  
ANISOU 2413  CD1 TYR A 291     4994   4433   4912    -68    305   -721       C  
ATOM   2414  CD2 TYR A 291      27.464  17.787  36.806  1.00 38.20           C  
ANISOU 2414  CD2 TYR A 291     4902   4766   4847   -136    187   -823       C  
ATOM   2415  CE1 TYR A 291      27.779  18.243  34.095  1.00 36.86           C  
ANISOU 2415  CE1 TYR A 291     4895   4277   4833    -84    315   -657       C  
ATOM   2416  CE2 TYR A 291      28.545  17.221  36.124  1.00 39.00           C  
ANISOU 2416  CE2 TYR A 291     5020   4814   4983   -158    198   -760       C  
ATOM   2417  CZ  TYR A 291      28.690  17.458  34.762  1.00 38.16           C  
ANISOU 2417  CZ  TYR A 291     4997   4547   4955   -133    260   -679       C  
ATOM   2418  OH  TYR A 291      29.741  16.925  34.048  1.00 36.35           O  
ANISOU 2418  OH  TYR A 291     4784   4275   4754   -144    270   -615       O  
ATOM   2419  N   ASP A 292      25.542  22.392  37.965  1.00 45.07           N  
ANISOU 2419  N   ASP A 292     5727   5424   5972    -98    339  -1245       N  
ATOM   2420  CA  ASP A 292      24.855  23.664  37.840  1.00 53.78           C  
ANISOU 2420  CA  ASP A 292     6856   6404   7174    -67    407  -1314       C  
ATOM   2421  C   ASP A 292      24.002  23.678  36.565  1.00 58.54           C  
ANISOU 2421  C   ASP A 292     7581   6890   7770      1    469  -1143       C  
ATOM   2422  O   ASP A 292      24.257  22.921  35.627  1.00 65.66           O  
ANISOU 2422  O   ASP A 292     8540   7763   8646     13    476  -1000       O  
ATOM   2423  CB  ASP A 292      25.888  24.791  37.818  1.00 54.34           C  
ANISOU 2423  CB  ASP A 292     6873   6310   7462   -122    489  -1452       C  
ATOM   2424  CG  ASP A 292      27.136  24.431  36.998  1.00 67.99           C  
ANISOU 2424  CG  ASP A 292     8614   7939   9279   -168    533  -1373       C  
ATOM   2425  OD1 ASP A 292      27.675  23.292  37.133  1.00 65.96           O  
ANISOU 2425  OD1 ASP A 292     8340   7812   8909   -189    463  -1316       O  
ATOM   2426  OD2 ASP A 292      27.584  25.305  36.230  1.00 68.85           O  
ANISOU 2426  OD2 ASP A 292     8744   7840   9577   -176    645  -1362       O  
ATOM   2427  N   ASP A 293      23.046  24.574  36.503  1.00 51.93           N  
ANISOU 2427  N   ASP A 293     6777   6003   6951     55    510  -1168       N  
ATOM   2428  CA  ASP A 293      22.086  24.634  35.438  1.00 53.29           C  
ANISOU 2428  CA  ASP A 293     7053   6098   7098    140    569  -1023       C  
ATOM   2429  C   ASP A 293      22.666  24.817  34.055  1.00 53.43           C  
ANISOU 2429  C   ASP A 293     7132   5945   7224    167    673   -896       C  
ATOM   2430  O   ASP A 293      22.159  24.292  33.113  1.00 48.05           O  
ANISOU 2430  O   ASP A 293     6519   5279   6458    235    679   -750       O  
ATOM   2431  CB  ASP A 293      21.137  25.787  35.715  1.00 59.19           C  
ANISOU 2431  CB  ASP A 293     7811   6798   7879    192    616  -1096       C  
ATOM   2432  CG  ASP A 293      19.992  25.389  36.597  1.00 67.38           C  
ANISOU 2432  CG  ASP A 293     8833   8035   8735    222    516  -1122       C  
ATOM   2433  OD1 ASP A 293      19.652  24.211  36.588  1.00 55.39           O  
ANISOU 2433  OD1 ASP A 293     7290   6529   7225    248    521  -1232       O  
ATOM   2434  OD2 ASP A 293      19.406  26.230  37.282  1.00 79.06           O  
ANISOU 2434  OD2 ASP A 293    10319   9654  10067    222    434  -1028       O  
ATOM   2435  N   GLU A 294      23.702  25.612  33.925  1.00 57.46           N  
ANISOU 2435  N   GLU A 294     7606   6302   7924    121    755   -955       N  
ATOM   2436  CA  GLU A 294      24.319  25.862  32.629  1.00 55.98           C  
ANISOU 2436  CA  GLU A 294     7462   5955   7851    156    867   -824       C  
ATOM   2437  C   GLU A 294      25.242  24.709  32.241  1.00 59.37           C  
ANISOU 2437  C   GLU A 294     7887   6448   8221    121    812   -748       C  
ATOM   2438  O   GLU A 294      25.367  24.371  31.060  1.00 62.69           O  
ANISOU 2438  O   GLU A 294     8362   6830   8628    185    857   -598       O  
ATOM   2439  CB  GLU A 294      25.066  27.201  32.610  1.00 67.45           C  
ANISOU 2439  CB  GLU A 294     8870   7198   9559    123    993   -900       C  
ATOM   2440  CG  GLU A 294      26.052  27.409  33.747  1.00 85.53           C  
ANISOU 2440  CG  GLU A 294    11050   9499  11948      3    948  -1101       C  
ATOM   2441  CD  GLU A 294      25.375  27.518  35.110  1.00 99.57           C  
ANISOU 2441  CD  GLU A 294    12775  11419  13639    -19    850  -1279       C  
ATOM   2442  OE1 GLU A 294      25.104  26.466  35.725  1.00107.14           O  
ANISOU 2442  OE1 GLU A 294    13721  12588  14398    -28    724  -1283       O  
ATOM   2443  OE2 GLU A 294      25.125  28.652  35.577  1.00 98.07           O  
ANISOU 2443  OE2 GLU A 294    12546  11131  13584    -22    901  -1413       O  
ATOM   2444  N   SER A 295      25.884  24.100  33.233  1.00 48.28           N  
ANISOU 2444  N   SER A 295     6413   5157   6774     32    716   -853       N  
ATOM   2445  CA  SER A 295      26.680  22.910  32.966  1.00 49.55           C  
ANISOU 2445  CA  SER A 295     6571   5395   6860      4    655   -783       C  
ATOM   2446  C   SER A 295      25.752  21.798  32.511  1.00 45.04           C  
ANISOU 2446  C   SER A 295     6062   4939   6113     68    584   -662       C  
ATOM   2447  O   SER A 295      26.055  21.095  31.554  1.00 42.34           O  
ANISOU 2447  O   SER A 295     5759   4589   5738    104    585   -545       O  
ATOM   2448  CB  SER A 295      27.484  22.494  34.190  1.00 50.93           C  
ANISOU 2448  CB  SER A 295     6651   5689   7011    -89    571   -916       C  
ATOM   2449  OG  SER A 295      28.496  23.456  34.432  1.00 49.20           O  
ANISOU 2449  OG  SER A 295     6364   5355   6974   -151    639  -1034       O  
ATOM   2450  N   TRP A 296      24.606  21.685  33.180  1.00 38.32           N  
ANISOU 2450  N   TRP A 296     5212   4192   5156     87    526   -697       N  
ATOM   2451  CA  TRP A 296      23.545  20.771  32.770  1.00 38.31           C  
ANISOU 2451  CA  TRP A 296     5259   4286   5011    148    468   -597       C  
ATOM   2452  C   TRP A 296      23.041  21.014  31.343  1.00 43.49           C  
ANISOU 2452  C   TRP A 296     5992   4857   5675    249    543   -480       C  
ATOM   2453  O   TRP A 296      23.001  20.088  30.531  1.00 41.22           O  
ANISOU 2453  O   TRP A 296     5733   4608   5321    290    511   -389       O  
ATOM   2454  CB  TRP A 296      22.369  20.854  33.744  1.00 30.76           C  
ANISOU 2454  CB  TRP A 296     4282   3443   3961    155    413   -657       C  
ATOM   2455  CG  TRP A 296      21.035  20.423  33.170  1.00 33.40           C  
ANISOU 2455  CG  TRP A 296     4670   3831   4188    232    392   -568       C  
ATOM   2456  CD1 TRP A 296      19.931  21.218  32.950  1.00 32.24           C  
ANISOU 2456  CD1 TRP A 296     4563   3663   4022    303    437   -567       C  
ATOM   2457  CD2 TRP A 296      20.659  19.098  32.757  1.00 37.54           C  
ANISOU 2457  CD2 TRP A 296     5206   4440   4616    247    320   -480       C  
ATOM   2458  NE1 TRP A 296      18.897  20.464  32.429  1.00 33.53           N  
ANISOU 2458  NE1 TRP A 296     4757   3908   4073    361    395   -487       N  
ATOM   2459  CE2 TRP A 296      19.318  19.164  32.299  1.00 35.40           C  
ANISOU 2459  CE2 TRP A 296     4975   4204   4273    324    323   -440       C  
ATOM   2460  CE3 TRP A 296      21.324  17.861  32.729  1.00 37.29           C  
ANISOU 2460  CE3 TRP A 296     5150   4455   4564    205    257   -438       C  
ATOM   2461  CZ2 TRP A 296      18.638  18.042  31.818  1.00 37.45           C  
ANISOU 2461  CZ2 TRP A 296     5240   4539   4451    352    261   -373       C  
ATOM   2462  CZ3 TRP A 296      20.641  16.742  32.244  1.00 36.66           C  
ANISOU 2462  CZ3 TRP A 296     5082   4436   4413    235    199   -365       C  
ATOM   2463  CH2 TRP A 296      19.310  16.843  31.804  1.00 35.34           C  
ANISOU 2463  CH2 TRP A 296     4943   4298   4185    304    200   -341       C  
ATOM   2464  N   LYS A 297      22.627  22.238  31.032  1.00 41.27           N  
ANISOU 2464  N   LYS A 297     5737   4471   5471    303    643   -485       N  
ATOM   2465  CA  LYS A 297      22.060  22.448  29.711  1.00 46.62           C  
ANISOU 2465  CA  LYS A 297     6478   5104   6130    424    718   -364       C  
ATOM   2466  C   LYS A 297      23.058  22.093  28.611  1.00 42.50           C  
ANISOU 2466  C   LYS A 297     5967   4527   5653    455    760   -265       C  
ATOM   2467  O   LYS A 297      22.663  21.571  27.557  1.00 40.19           O  
ANISOU 2467  O   LYS A 297     5710   4284   5278    554    760   -167       O  
ATOM   2468  CB  LYS A 297      21.493  23.857  29.550  1.00 55.70           C  
ANISOU 2468  CB  LYS A 297     7653   6146   7366    489    836   -367       C  
ATOM   2469  CG  LYS A 297      20.178  24.014  30.295  1.00 58.36           C  
ANISOU 2469  CG  LYS A 297     7997   6576   7603    505    785   -429       C  
ATOM   2470  CD  LYS A 297      19.573  25.388  30.134  1.00 62.51           C  
ANISOU 2470  CD  LYS A 297     8549   6995   8208    578    903   -431       C  
ATOM   2471  CE  LYS A 297      18.430  25.577  31.125  1.00 65.15           C  
ANISOU 2471  CE  LYS A 297     8877   7428   8449    574    840   -522       C  
ATOM   2472  NZ  LYS A 297      18.342  26.987  31.573  1.00 60.19           N  
ANISOU 2472  NZ  LYS A 297     8239   6672   7958    581    932   -604       N  
ATOM   2473  N   GLU A 298      24.343  22.345  28.882  1.00 37.73           N  
ANISOU 2473  N   GLU A 298     5324   3839   5172    375    789   -302       N  
ATOM   2474  CA  GLU A 298      25.428  22.056  27.947  1.00 42.47           C  
ANISOU 2474  CA  GLU A 298     5925   4390   5823    396    830   -211       C  
ATOM   2475  C   GLU A 298      25.488  20.563  27.691  1.00 47.68           C  
ANISOU 2475  C   GLU A 298     6592   5181   6345    398    714   -176       C  
ATOM   2476  O   GLU A 298      25.623  20.099  26.555  1.00 45.79           O  
ANISOU 2476  O   GLU A 298     6376   4959   6064    487    727    -76       O  
ATOM   2477  CB  GLU A 298      26.771  22.498  28.532  1.00 52.88           C  
ANISOU 2477  CB  GLU A 298     7184   5616   7291    286    862   -285       C  
ATOM   2478  CG  GLU A 298      26.996  24.000  28.560  1.00 72.12           C  
ANISOU 2478  CG  GLU A 298     9600   7878   9924    282   1000   -314       C  
ATOM   2479  CD  GLU A 298      28.476  24.379  28.555  1.00 84.22           C  
ANISOU 2479  CD  GLU A 298    11074   9298  11629    206   1061   -335       C  
ATOM   2480  OE1 GLU A 298      29.311  23.512  28.204  1.00 86.14           O  
ANISOU 2480  OE1 GLU A 298    11309   9597  11822    190   1015   -284       O  
ATOM   2481  OE2 GLU A 298      28.799  25.546  28.888  1.00 87.47           O  
ANISOU 2481  OE2 GLU A 298    11440   9560  12233    163   1157   -407       O  
ATOM   2482  N   VAL A 299      25.394  19.810  28.776  1.00 39.90           N  
ANISOU 2482  N   VAL A 299     5576   4292   5293    308    603   -259       N  
ATOM   2483  CA  VAL A 299      25.450  18.376  28.693  1.00 48.03           C  
ANISOU 2483  CA  VAL A 299     6603   5429   6219    297    496   -231       C  
ATOM   2484  C   VAL A 299      24.114  17.820  28.212  1.00 39.81           C  
ANISOU 2484  C   VAL A 299     5593   4467   5066    379    451   -193       C  
ATOM   2485  O   VAL A 299      24.068  16.938  27.344  1.00 35.61           O  
ANISOU 2485  O   VAL A 299     5075   3978   4479    437    413   -138       O  
ATOM   2486  CB  VAL A 299      25.892  17.773  30.048  1.00 52.88           C  
ANISOU 2486  CB  VAL A 299     7160   6121   6812    182    410   -315       C  
ATOM   2487  CG1 VAL A 299      25.127  16.519  30.343  1.00 55.83           C  
ANISOU 2487  CG1 VAL A 299     7527   6613   7071    182    305   -296       C  
ATOM   2488  CG2 VAL A 299      27.404  17.537  30.043  1.00 43.06           C  
ANISOU 2488  CG2 VAL A 299     5884   4847   5628    126    416   -317       C  
ATOM   2489  N   ARG A 300      23.020  18.335  28.760  1.00 38.29           N  
ANISOU 2489  N   ARG A 300     5406   4301   4842    386    453   -234       N  
ATOM   2490  CA  ARG A 300      21.718  17.881  28.295  1.00 46.58           C  
ANISOU 2490  CA  ARG A 300     6478   5431   5789    464    415   -205       C  
ATOM   2491  C   ARG A 300      21.641  17.950  26.764  1.00 44.13           C  
ANISOU 2491  C   ARG A 300     6203   5104   5462    595    472   -123       C  
ATOM   2492  O   ARG A 300      21.093  17.066  26.127  1.00 41.25           O  
ANISOU 2492  O   ARG A 300     5836   4818   5018    653    413   -105       O  
ATOM   2493  CB  ARG A 300      20.588  18.709  28.900  1.00 45.95           C  
ANISOU 2493  CB  ARG A 300     6406   5369   5683    478    438   -247       C  
ATOM   2494  CG  ARG A 300      19.228  18.347  28.310  1.00 44.94           C  
ANISOU 2494  CG  ARG A 300     6299   5328   5450    569    410   -217       C  
ATOM   2495  CD  ARG A 300      18.233  19.442  28.550  1.00 41.96           C  
ANISOU 2495  CD  ARG A 300     5943   4945   5053    619    469   -236       C  
ATOM   2496  NE  ARG A 300      18.674  20.688  27.937  1.00 55.35           N  
ANISOU 2496  NE  ARG A 300     7672   6522   6838    684    600   -201       N  
ATOM   2497  CZ  ARG A 300      18.367  21.896  28.401  1.00 58.05           C  
ANISOU 2497  CZ  ARG A 300     8026   6797   7235    692    675   -234       C  
ATOM   2498  NH1 ARG A 300      18.805  22.985  27.772  1.00 55.95           N  
ANISOU 2498  NH1 ARG A 300     7782   6400   7075    755    808   -185       N  
ATOM   2499  NH2 ARG A 300      17.630  22.012  29.499  1.00 53.95           N  
ANISOU 2499  NH2 ARG A 300     7489   6340   6670    643    620   -312       N  
ATOM   2500  N   ASP A 301      22.197  19.004  26.181  1.00 34.33           N  
ANISOU 2500  N   ASP A 301     4980   3762   4301    649    589    -76       N  
ATOM   2501  CA  ASP A 301      22.051  19.225  24.748  1.00 44.28           C  
ANISOU 2501  CA  ASP A 301     6264   5028   5534    802    662     19       C  
ATOM   2502  C   ASP A 301      23.060  18.445  23.934  1.00 45.38           C  
ANISOU 2502  C   ASP A 301     6389   5181   5672    830    640     69       C  
ATOM   2503  O   ASP A 301      22.748  18.047  22.818  1.00 37.21           O  
ANISOU 2503  O   ASP A 301     5356   4223   4560    959    637    118       O  
ATOM   2504  CB  ASP A 301      22.172  20.717  24.385  1.00 47.20           C  
ANISOU 2504  CB  ASP A 301     6652   5282   6001    872    819     80       C  
ATOM   2505  CG  ASP A 301      20.936  21.541  24.782  1.00 55.66           C  
ANISOU 2505  CG  ASP A 301     7744   6356   7047    907    858     52       C  
ATOM   2506  OD1 ASP A 301      19.814  20.980  24.880  1.00 50.88           O  
ANISOU 2506  OD1 ASP A 301     7145   5870   6317    934    779     19       O  
ATOM   2507  OD2 ASP A 301      21.099  22.768  24.984  1.00 61.95           O  
ANISOU 2507  OD2 ASP A 301     8549   7029   7962    909    972     63       O  
ATOM   2508  N   ARG A 302      24.268  18.248  24.465  1.00 44.35           N  
ANISOU 2508  N   ARG A 302     6239   4992   5620    720    623     49       N  
ATOM   2509  CA  ARG A 302      25.325  17.586  23.698  1.00 42.79           C  
ANISOU 2509  CA  ARG A 302     6030   4804   5426    749    609    102       C  
ATOM   2510  C   ARG A 302      24.993  16.112  23.430  1.00 45.07           C  
ANISOU 2510  C   ARG A 302     6307   5206   5610    764    480     73       C  
ATOM   2511  O   ARG A 302      24.974  15.654  22.279  1.00 46.92           O  
ANISOU 2511  O   ARG A 302     6538   5503   5786    886    472    115       O  
ATOM   2512  CB  ARG A 302      26.687  17.738  24.385  1.00 32.12           C  
ANISOU 2512  CB  ARG A 302     4654   3370   4179    625    623     81       C  
ATOM   2513  CG  ARG A 302      27.815  16.937  23.740  1.00 29.27           C  
ANISOU 2513  CG  ARG A 302     4279   3031   3810    641    593    128       C  
ATOM   2514  CD  ARG A 302      29.172  17.592  23.958  1.00 36.55           C  
ANISOU 2514  CD  ARG A 302     5177   3853   4857    572    668    146       C  
ATOM   2515  NE  ARG A 302      30.311  16.697  23.709  1.00 43.50           N  
ANISOU 2515  NE  ARG A 302     6039   4768   5720    550    615    167       N  
ATOM   2516  CZ  ARG A 302      30.843  16.472  22.509  1.00 43.18           C  
ANISOU 2516  CZ  ARG A 302     6000   4749   5657    662    644    262       C  
ATOM   2517  NH1 ARG A 302      31.894  15.677  22.387  1.00 38.67           N  
ANISOU 2517  NH1 ARG A 302     5412   4211   5071    635    593    273       N  
ATOM   2518  NH2 ARG A 302      30.332  17.049  21.428  1.00 40.07           N  
ANISOU 2518  NH2 ARG A 302     5618   4358   5247    813    728    352       N  
ATOM   2519  N   TYR A 303      24.679  15.394  24.487  1.00 38.80           N  
ANISOU 2519  N   TYR A 303     5498   4443   4803    647    384     -1       N  
ATOM   2520  CA  TYR A 303      24.132  14.065  24.445  1.00 39.03           C  
ANISOU 2520  CA  TYR A 303     5508   4559   4761    650    270    -36       C  
ATOM   2521  C   TYR A 303      22.689  14.382  24.518  1.00 41.97           C  
ANISOU 2521  C   TYR A 303     5890   4978   5080    705    279    -57       C  
ATOM   2522  O   TYR A 303      22.371  15.415  24.970  1.00 59.97           O  
ANISOU 2522  O   TYR A 303     8193   7216   7378    730    367    -40       O  
ATOM   2523  CB  TYR A 303      24.624  13.307  25.642  1.00 34.90           C  
ANISOU 2523  CB  TYR A 303     4958   4041   4263    508    193    -78       C  
ATOM   2524  CG  TYR A 303      26.086  13.441  25.744  1.00 29.74           C  
ANISOU 2524  CG  TYR A 303     4299   3332   3668    456    224    -57       C  
ATOM   2525  CD1 TYR A 303      26.640  14.221  26.686  1.00 24.13           C  
ANISOU 2525  CD1 TYR A 303     3578   2574   3016    370    272    -84       C  
ATOM   2526  CD2 TYR A 303      26.915  12.839  24.838  1.00 33.62           C  
ANISOU 2526  CD2 TYR A 303     4790   3826   4158    505    210    -18       C  
ATOM   2527  CE1 TYR A 303      27.962  14.364  26.751  1.00 32.86           C  
ANISOU 2527  CE1 TYR A 303     4669   3635   4183    321    303    -75       C  
ATOM   2528  CE2 TYR A 303      28.226  12.989  24.900  1.00 27.38           C  
ANISOU 2528  CE2 TYR A 303     3993   2993   3418    463    242      7       C  
ATOM   2529  CZ  TYR A 303      28.758  13.734  25.866  1.00 27.40           C  
ANISOU 2529  CZ  TYR A 303     3981   2947   3483    366    288    -22       C  
ATOM   2530  OH  TYR A 303      30.082  13.901  25.946  1.00 21.08           O  
ANISOU 2530  OH  TYR A 303     3162   2109   2737    322    320     -8       O  
ATOM   2531  N   SER A 304      21.787  13.616  23.979  1.00 35.94           N  
ANISOU 2531  N   SER A 304     5105   4294   4258    732    198    -95       N  
ATOM   2532  CA  SER A 304      20.422  14.135  23.993  1.00 47.03           C  
ANISOU 2532  CA  SER A 304     6518   5750   5601    805    224   -109       C  
ATOM   2533  C   SER A 304      19.521  13.694  25.128  1.00 52.59           C  
ANISOU 2533  C   SER A 304     7199   6490   6293    711    156   -160       C  
ATOM   2534  O   SER A 304      18.680  12.875  24.917  1.00 51.76           O  
ANISOU 2534  O   SER A 304     7061   6455   6151    731     86   -198       O  
ATOM   2535  CB  SER A 304      19.759  13.904  22.653  1.00 54.55           C  
ANISOU 2535  CB  SER A 304     7455   6792   6478    962    215   -113       C  
ATOM   2536  OG  SER A 304      20.410  14.652  21.665  1.00 59.77           O  
ANISOU 2536  OG  SER A 304     8136   7439   7135   1083    310    -40       O  
ATOM   2537  N   LEU A 305      19.658  14.299  26.303  1.00 48.45           N  
ANISOU 2537  N   LEU A 305     6682   5923   5804    614    179   -165       N  
ATOM   2538  CA  LEU A 305      19.037  13.847  27.547  1.00 39.44           C  
ANISOU 2538  CA  LEU A 305     5507   4826   4654    517    115   -197       C  
ATOM   2539  C   LEU A 305      17.643  14.416  27.779  1.00 39.68           C  
ANISOU 2539  C   LEU A 305     5541   4912   4622    556    127   -216       C  
ATOM   2540  O   LEU A 305      17.339  15.527  27.338  1.00 51.07           O  
ANISOU 2540  O   LEU A 305     7024   6336   6045    635    206   -207       O  
ATOM   2541  CB  LEU A 305      19.962  14.202  28.703  1.00 39.88           C  
ANISOU 2541  CB  LEU A 305     5551   4842   4758    414    128   -205       C  
ATOM   2542  CG  LEU A 305      21.405  13.801  28.368  1.00 45.69           C  
ANISOU 2542  CG  LEU A 305     6287   5524   5549    388    130   -184       C  
ATOM   2543  CD1 LEU A 305      22.386  14.101  29.527  1.00 34.35           C  
ANISOU 2543  CD1 LEU A 305     4825   4070   4157    288    139   -208       C  
ATOM   2544  CD2 LEU A 305      21.492  12.303  27.900  1.00 28.63           C  
ANISOU 2544  CD2 LEU A 305     4099   3393   3385    389     48   -168       C  
ATOM   2545  N   ARG A 306      16.819  13.709  28.526  1.00 40.00           N  
ANISOU 2545  N   ARG A 306     5537   5022   4639    507     54   -232       N  
ATOM   2546  CA  ARG A 306      15.513  14.198  28.877  1.00 33.41           C  
ANISOU 2546  CA  ARG A 306     4698   4254   3741    530     57   -249       C  
ATOM   2547  C   ARG A 306      15.668  15.448  29.676  1.00 39.44           C  
ANISOU 2547  C   ARG A 306     5490   4989   4506    511    119   -260       C  
ATOM   2548  O   ARG A 306      16.605  15.596  30.390  1.00 43.28           O  
ANISOU 2548  O   ARG A 306     5965   5439   5042    436    122   -269       O  
ATOM   2549  CB  ARG A 306      14.796  13.205  29.732  1.00 30.80           C  
ANISOU 2549  CB  ARG A 306     4301   3993   3408    457    -25   -248       C  
ATOM   2550  CG  ARG A 306      14.623  11.892  29.106  1.00 48.73           C  
ANISOU 2550  CG  ARG A 306     6526   6281   5709    466    -90   -256       C  
ATOM   2551  CD  ARG A 306      13.431  11.140  29.608  1.00 58.73           C  
ANISOU 2551  CD  ARG A 306     7715   7594   7007    385   -154   -236       C  
ATOM   2552  NE  ARG A 306      13.020  10.153  28.619  1.00 71.82           N  
ANISOU 2552  NE  ARG A 306     9363   9326   8598    380   -142   -228       N  
ATOM   2553  CZ  ARG A 306      11.868   9.482  28.626  1.00 70.06           C  
ANISOU 2553  CZ  ARG A 306     9123   9135   8361    325   -135   -197       C  
ATOM   2554  NH1 ARG A 306      10.973   9.674  29.585  1.00 57.01           N  
ANISOU 2554  NH1 ARG A 306     7457   7450   6756    265   -138   -172       N  
ATOM   2555  NH2 ARG A 306      11.620   8.604  27.668  1.00 65.46           N  
ANISOU 2555  NH2 ARG A 306     8530   8634   7708    339   -128   -199       N  
ATOM   2556  N   ARG A 307      14.743  16.372  29.539  1.00 41.21           N  
ANISOU 2556  N   ARG A 307     5745   5235   4678    582    169   -270       N  
ATOM   2557  CA  ARG A 307      14.878  17.645  30.238  1.00 50.37           C  
ANISOU 2557  CA  ARG A 307     6929   6353   5856    574    233   -296       C  
ATOM   2558  C   ARG A 307      14.714  17.482  31.756  1.00 52.22           C  
ANISOU 2558  C   ARG A 307     7111   6655   6075    484    175   -333       C  
ATOM   2559  O   ARG A 307      15.413  18.121  32.539  1.00 56.10           O  
ANISOU 2559  O   ARG A 307     7592   7111   6611    437    197   -378       O  
ATOM   2560  CB  ARG A 307      13.870  18.674  29.694  1.00 65.07           C  
ANISOU 2560  CB  ARG A 307     8835   8225   7664    685    304   -291       C  
ATOM   2561  CG  ARG A 307      14.109  19.125  28.243  1.00 67.45           C  
ANISOU 2561  CG  ARG A 307     9182   8471   7976    803    390   -241       C  
ATOM   2562  CD  ARG A 307      13.170  20.265  27.828  1.00 71.81           C  
ANISOU 2562  CD  ARG A 307     9774   9033   8478    923    479   -223       C  
ATOM   2563  NE  ARG A 307      13.386  21.498  28.596  1.00 80.11           N  
ANISOU 2563  NE  ARG A 307    10847   9993   9598    897    550   -251       N  
ATOM   2564  CZ  ARG A 307      14.222  22.474  28.238  1.00 83.78           C  
ANISOU 2564  CZ  ARG A 307    11340  10319  10173    925    661   -225       C  
ATOM   2565  NH1 ARG A 307      14.928  22.358  27.119  1.00 85.78           N  
ANISOU 2565  NH1 ARG A 307    11606  10524  10464    987    716   -152       N  
ATOM   2566  NH2 ARG A 307      14.356  23.566  28.996  1.00 77.46           N  
ANISOU 2566  NH2 ARG A 307    10546   9429   9456    894    719   -274       N  
ATOM   2567  N   ASN A 308      13.820  16.610  32.151  1.00 51.73           N  
ANISOU 2567  N   ASN A 308     7005   6699   5952    467    103   -317       N  
ATOM   2568  CA  ASN A 308      13.500  16.384  33.535  1.00 54.90           C  
ANISOU 2568  CA  ASN A 308     7343   7195   6321    405     50   -327       C  
ATOM   2569  C   ASN A 308      14.598  15.727  34.330  1.00 47.78           C  
ANISOU 2569  C   ASN A 308     6388   6299   5466    321     14   -321       C  
ATOM   2570  O   ASN A 308      14.514  15.678  35.504  1.00 54.15           O  
ANISOU 2570  O   ASN A 308     7136   7196   6242    287    -14   -334       O  
ATOM   2571  CB  ASN A 308      12.250  15.522  33.628  1.00 62.56           C  
ANISOU 2571  CB  ASN A 308     8268   8272   7231    413     -7   -289       C  
ATOM   2572  CG  ASN A 308      11.184  16.136  34.490  1.00 80.75           C  
ANISOU 2572  CG  ASN A 308    10578  10655   9449    464      6   -312       C  
ATOM   2573  OD1 ASN A 308      10.988  15.747  35.640  1.00 89.57           O  
ANISOU 2573  OD1 ASN A 308    11654  11849  10529    442    -11   -329       O  
ATOM   2574  ND2 ASN A 308      10.486  17.113  33.945  1.00 78.88           N  
ANISOU 2574  ND2 ASN A 308    10385  10418   9168    545     36   -314       N  
ATOM   2575  N   LEU A 309      15.590  15.170  33.668  1.00 40.28           N  
ANISOU 2575  N   LEU A 309     5454   5269   4581    301     18   -300       N  
ATOM   2576  CA  LEU A 309      16.581  14.309  34.298  1.00 41.70           C  
ANISOU 2576  CA  LEU A 309     5581   5465   4797    230    -20   -278       C  
ATOM   2577  C   LEU A 309      17.330  15.013  35.418  1.00 43.32           C  
ANISOU 2577  C   LEU A 309     5752   5705   5002    194     -7   -336       C  
ATOM   2578  O   LEU A 309      17.634  14.404  36.463  1.00 37.70           O  
ANISOU 2578  O   LEU A 309     4966   5090   4269    154    -47   -318       O  
ATOM   2579  CB  LEU A 309      17.574  13.761  33.258  1.00 40.23           C  
ANISOU 2579  CB  LEU A 309     5427   5182   4677    226    -12   -255       C  
ATOM   2580  CG  LEU A 309      18.739  12.961  33.845  1.00 38.60           C  
ANISOU 2580  CG  LEU A 309     5174   4984   4507    160    -41   -232       C  
ATOM   2581  CD1 LEU A 309      18.275  11.587  34.432  1.00 42.30           C  
ANISOU 2581  CD1 LEU A 309     5571   5530   4972    128   -104   -162       C  
ATOM   2582  CD2 LEU A 309      19.890  12.822  32.856  1.00 29.21           C  
ANISOU 2582  CD2 LEU A 309     4027   3695   3377    164    -19   -228       C  
ATOM   2583  N   ILE A 310      17.631  16.292  35.196  1.00 36.79           N  
ANISOU 2583  N   ILE A 310     4970   4803   4206    215     55   -407       N  
ATOM   2584  CA  ILE A 310      18.335  17.066  36.197  1.00 35.60           C  
ANISOU 2584  CA  ILE A 310     4777   4676   4073    183     68   -497       C  
ATOM   2585  C   ILE A 310      17.476  17.177  37.464  1.00 43.89           C  
ANISOU 2585  C   ILE A 310     5760   5881   5034    192     25   -527       C  
ATOM   2586  O   ILE A 310      17.997  17.137  38.569  1.00 45.47           O  
ANISOU 2586  O   ILE A 310     5882   6184   5211    166     -3   -576       O  
ATOM   2587  CB  ILE A 310      18.774  18.431  35.677  1.00 41.84           C  
ANISOU 2587  CB  ILE A 310     5618   5331   4948    201    152   -569       C  
ATOM   2588  CG1 ILE A 310      19.871  19.011  36.579  1.00 42.53           C  
ANISOU 2588  CG1 ILE A 310     5645   5422   5092    148    161   -680       C  
ATOM   2589  CG2 ILE A 310      17.575  19.378  35.548  1.00 46.30           C  
ANISOU 2589  CG2 ILE A 310     6222   5886   5482    267    189   -592       C  
ATOM   2590  CD1 ILE A 310      21.095  18.126  36.725  1.00 35.18           C  
ANISOU 2590  CD1 ILE A 310     4673   4513   4181     91    130   -659       C  
ATOM   2591  N   ASN A 311      16.159  17.252  37.300  1.00 46.56           N  
ANISOU 2591  N   ASN A 311     6120   6258   5312    240     18   -494       N  
ATOM   2592  CA  ASN A 311      15.258  17.268  38.449  1.00 48.98           C  
ANISOU 2592  CA  ASN A 311     6360   6727   5525    259    -25   -502       C  
ATOM   2593  C   ASN A 311      15.401  16.025  39.329  1.00 48.81           C  
ANISOU 2593  C   ASN A 311     6243   6841   5460    229    -85   -425       C  
ATOM   2594  O   ASN A 311      15.436  16.142  40.561  1.00 51.55           O  
ANISOU 2594  O   ASN A 311     6504   7337   5744    238   -113   -458       O  
ATOM   2595  CB  ASN A 311      13.794  17.403  38.013  1.00 49.25           C  
ANISOU 2595  CB  ASN A 311     6432   6781   5499    314    -24   -462       C  
ATOM   2596  CG  ASN A 311      13.502  18.719  37.336  1.00 55.12           C  
ANISOU 2596  CG  ASN A 311     7256   7420   6266    367     45   -527       C  
ATOM   2597  OD1 ASN A 311      14.056  19.752  37.703  1.00 52.69           O  
ANISOU 2597  OD1 ASN A 311     6951   7065   6003    366     82   -625       O  
ATOM   2598  ND2 ASN A 311      12.619  18.690  36.336  1.00 55.25           N  
ANISOU 2598  ND2 ASN A 311     7331   7401   6259    419     66   -476       N  
ATOM   2599  N   GLU A 312      15.462  14.850  38.691  1.00 41.86           N  
ANISOU 2599  N   GLU A 312     5371   5917   4617    204   -101   -324       N  
ATOM   2600  CA  GLU A 312      15.458  13.552  39.385  1.00 42.50           C  
ANISOU 2600  CA  GLU A 312     5363   6103   4682    181   -144   -220       C  
ATOM   2601  C   GLU A 312      16.777  13.272  40.075  1.00 45.47           C  
ANISOU 2601  C   GLU A 312     5683   6525   5069    152   -148   -231       C  
ATOM   2602  O   GLU A 312      16.811  12.734  41.188  1.00 46.43           O  
ANISOU 2602  O   GLU A 312     5704   6802   5137    162   -172   -178       O  
ATOM   2603  CB  GLU A 312      15.161  12.416  38.414  1.00 49.08           C  
ANISOU 2603  CB  GLU A 312     6220   6848   5581    161   -156   -129       C  
ATOM   2604  CG  GLU A 312      13.819  12.550  37.703  1.00 64.35           C  
ANISOU 2604  CG  GLU A 312     8191   8759   7499    195   -158   -123       C  
ATOM   2605  CD  GLU A 312      13.851  12.037  36.264  1.00 70.84           C  
ANISOU 2605  CD  GLU A 312     9072   9451   8393    194   -155   -117       C  
ATOM   2606  OE1 GLU A 312      13.328  12.746  35.379  1.00 72.31           O  
ANISOU 2606  OE1 GLU A 312     9326   9589   8559    242   -130   -166       O  
ATOM   2607  OE2 GLU A 312      14.404  10.939  36.017  1.00 75.27           O  
ANISOU 2607  OE2 GLU A 312     9606   9966   9026    158   -175    -66       O  
ATOM   2608  N   ILE A 313      17.859  13.634  39.398  1.00 45.25           N  
ANISOU 2608  N   ILE A 313     5712   6374   5107    125   -120   -292       N  
ATOM   2609  CA  ILE A 313      19.189  13.558  39.974  1.00 45.35           C  
ANISOU 2609  CA  ILE A 313     5675   6427   5129     98   -120   -329       C  
ATOM   2610  C   ILE A 313      19.235  14.422  41.222  1.00 46.23           C  
ANISOU 2610  C   ILE A 313     5709   6687   5169    123   -128   -435       C  
ATOM   2611  O   ILE A 313      19.683  13.986  42.281  1.00 52.20           O  
ANISOU 2611  O   ILE A 313     6363   7605   5865    135   -152   -422       O  
ATOM   2612  CB  ILE A 313      20.253  14.026  38.957  1.00 41.84           C  
ANISOU 2612  CB  ILE A 313     5309   5816   4774     67    -81   -389       C  
ATOM   2613  CG1 ILE A 313      20.425  12.955  37.872  1.00 36.59           C  
ANISOU 2613  CG1 ILE A 313     4693   5046   4164     53    -86   -288       C  
ATOM   2614  CG2 ILE A 313      21.572  14.349  39.648  1.00 34.85           C  
ANISOU 2614  CG2 ILE A 313     4365   4980   3896     40    -75   -474       C  
ATOM   2615  CD1 ILE A 313      21.472  13.282  36.796  1.00 33.45           C  
ANISOU 2615  CD1 ILE A 313     4365   4501   3844     37    -49   -322       C  
ATOM   2616  N   ARG A 314      18.734  15.643  41.090  1.00 44.49           N  
ANISOU 2616  N   ARG A 314     5531   6421   4952    144   -106   -539       N  
ATOM   2617  CA  ARG A 314      18.768  16.613  42.166  1.00 41.79           C  
ANISOU 2617  CA  ARG A 314     5118   6200   4561    172   -115   -675       C  
ATOM   2618  C   ARG A 314      17.951  16.146  43.352  1.00 35.44           C  
ANISOU 2618  C   ARG A 314     4211   5625   3630    225   -162   -621       C  
ATOM   2619  O   ARG A 314      18.334  16.367  44.497  1.00 34.95           O  
ANISOU 2619  O   ARG A 314     4041   5739   3498    257   -187   -699       O  
ATOM   2620  CB  ARG A 314      18.308  17.982  41.670  1.00 44.98           C  
ANISOU 2620  CB  ARG A 314     5595   6479   5016    187    -73   -785       C  
ATOM   2621  CG  ARG A 314      19.371  18.634  40.816  1.00 45.50           C  
ANISOU 2621  CG  ARG A 314     5722   6350   5215    143    -15   -858       C  
ATOM   2622  CD  ARG A 314      18.995  20.020  40.358  1.00 47.97           C  
ANISOU 2622  CD  ARG A 314     6097   6527   5603    164     45   -954       C  
ATOM   2623  NE  ARG A 314      20.182  20.724  39.877  1.00 56.49           N  
ANISOU 2623  NE  ARG A 314     7193   7446   6825    121    105  -1039       N  
ATOM   2624  CZ  ARG A 314      20.149  21.751  39.035  1.00 55.47           C  
ANISOU 2624  CZ  ARG A 314     7137   7129   6811    132    187  -1069       C  
ATOM   2625  NH1 ARG A 314      21.278  22.333  38.648  1.00 48.88           N  
ANISOU 2625  NH1 ARG A 314     6302   6150   6122     88    248  -1133       N  
ATOM   2626  NH2 ARG A 314      18.984  22.195  38.584  1.00 58.36           N  
ANISOU 2626  NH2 ARG A 314     7568   7455   7150    191    216  -1027       N  
ATOM   2627  N   HIS A 315      16.837  15.478  43.084  1.00 37.31           N  
ANISOU 2627  N   HIS A 315     4468   5872   3835    242   -173   -487       N  
ATOM   2628  CA  HIS A 315      16.057  14.904  44.168  1.00 35.51           C  
ANISOU 2628  CA  HIS A 315     4135   5859   3498    295   -209   -399       C  
ATOM   2629  C   HIS A 315      16.934  13.947  44.979  1.00 40.58           C  
ANISOU 2629  C   HIS A 315     4669   6641   4109    300   -222   -325       C  
ATOM   2630  O   HIS A 315      16.962  14.014  46.200  1.00 42.74           O  
ANISOU 2630  O   HIS A 315     4823   7137   4278    362   -244   -343       O  
ATOM   2631  CB  HIS A 315      14.803  14.204  43.631  1.00 39.60           C  
ANISOU 2631  CB  HIS A 315     4686   6340   4021    297   -213   -257       C  
ATOM   2632  CG  HIS A 315      13.966  13.549  44.693  1.00 48.00           C  
ANISOU 2632  CG  HIS A 315     5633   7612   4991    350   -238   -138       C  
ATOM   2633  ND1 HIS A 315      13.503  14.229  45.809  1.00 55.42           N  
ANISOU 2633  ND1 HIS A 315     6493   8754   5811    423   -260   -196       N  
ATOM   2634  CD2 HIS A 315      13.490  12.288  44.810  1.00 41.15           C  
ANISOU 2634  CD2 HIS A 315     4709   6785   4143    345   -241     41       C  
ATOM   2635  CE1 HIS A 315      12.794  13.412  46.559  1.00 48.18           C  
ANISOU 2635  CE1 HIS A 315     5474   8003   4829    468   -273    -44       C  
ATOM   2636  NE2 HIS A 315      12.762  12.225  45.975  1.00 46.56           N  
ANISOU 2636  NE2 HIS A 315     5280   7694   4718    417   -257    106       N  
ATOM   2637  N   VAL A 316      17.685  13.083  44.297  1.00 47.97           N  
ANISOU 2637  N   VAL A 316     5641   7457   5130    247   -207   -247       N  
ATOM   2638  CA  VAL A 316      18.509  12.096  44.997  1.00 50.82           C  
ANISOU 2638  CA  VAL A 316     5903   7941   5464    258   -211   -157       C  
ATOM   2639  C   VAL A 316      19.691  12.767  45.686  1.00 50.61           C  
ANISOU 2639  C   VAL A 316     5816   8020   5393    273   -215   -307       C  
ATOM   2640  O   VAL A 316      19.940  12.540  46.869  1.00 50.52           O  
ANISOU 2640  O   VAL A 316     5674   8243   5278    338   -229   -294       O  
ATOM   2641  CB  VAL A 316      18.968  10.934  44.053  1.00 38.39           C  
ANISOU 2641  CB  VAL A 316     4385   6203   3999    202   -195    -33       C  
ATOM   2642  CG1 VAL A 316      19.940   9.976  44.746  1.00 30.16           C  
ANISOU 2642  CG1 VAL A 316     3248   5278   2935    219   -188     58       C  
ATOM   2643  CG2 VAL A 316      17.766  10.166  43.553  1.00 40.72           C  
ANISOU 2643  CG2 VAL A 316     4702   6427   4341    194   -196    101       C  
ATOM   2644  N   GLU A 317      20.408  13.623  44.967  1.00 49.98           N  
ANISOU 2644  N   GLU A 317     5818   7780   5393    220   -199   -452       N  
ATOM   2645  CA  GLU A 317      21.571  14.256  45.577  1.00 51.02           C  
ANISOU 2645  CA  GLU A 317     5881   7998   5506    222   -203   -612       C  
ATOM   2646  C   GLU A 317      21.175  15.073  46.794  1.00 52.03           C  
ANISOU 2646  C   GLU A 317     5899   8344   5527    295   -232   -743       C  
ATOM   2647  O   GLU A 317      21.949  15.195  47.734  1.00 55.69           O  
ANISOU 2647  O   GLU A 317     6244   8995   5922    334   -250   -838       O  
ATOM   2648  CB  GLU A 317      22.373  15.094  44.578  1.00 53.21           C  
ANISOU 2648  CB  GLU A 317     6256   8049   5912    150   -170   -741       C  
ATOM   2649  CG  GLU A 317      21.636  16.292  44.018  1.00 60.85           C  
ANISOU 2649  CG  GLU A 317     7308   8873   6940    142   -148   -840       C  
ATOM   2650  CD  GLU A 317      22.374  16.941  42.854  1.00 68.82           C  
ANISOU 2650  CD  GLU A 317     8418   9637   8095     80    -97   -906       C  
ATOM   2651  OE1 GLU A 317      22.703  16.234  41.863  1.00 59.97           O  
ANISOU 2651  OE1 GLU A 317     7372   8385   7028     46    -79   -792       O  
ATOM   2652  OE2 GLU A 317      22.622  18.167  42.935  1.00 76.70           O  
ANISOU 2652  OE2 GLU A 317     9410  10573   9158     70    -72  -1072       O  
ATOM   2653  N   LYS A 318      19.964  15.620  46.789  1.00 56.24           N  
ANISOU 2653  N   LYS A 318     6464   8868   6037    324   -240   -753       N  
ATOM   2654  CA  LYS A 318      19.532  16.468  47.900  1.00 55.83           C  
ANISOU 2654  CA  LYS A 318     6310   9019   5882    402   -272   -892       C  
ATOM   2655  C   LYS A 318      18.956  15.653  49.050  1.00 55.76           C  
ANISOU 2655  C   LYS A 318     6168   9301   5718    500   -303   -758       C  
ATOM   2656  O   LYS A 318      19.210  15.961  50.211  1.00 57.26           O  
ANISOU 2656  O   LYS A 318     6219   9744   5795    583   -334   -860       O  
ATOM   2657  CB  LYS A 318      18.535  17.534  47.434  1.00 57.07           C  
ANISOU 2657  CB  LYS A 318     6556   9049   6079    400   -264   -975       C  
ATOM   2658  CG  LYS A 318      19.173  18.640  46.599  1.00 61.65           C  
ANISOU 2658  CG  LYS A 318     7227   9388   6809    333   -224  -1143       C  
ATOM   2659  CD  LYS A 318      18.131  19.619  46.076  1.00 62.95           C  
ANISOU 2659  CD  LYS A 318     7484   9421   7014    344   -201  -1191       C  
ATOM   2660  CE  LYS A 318      18.776  20.725  45.257  1.00 66.07           C  
ANISOU 2660  CE  LYS A 318     7958   9569   7576    287   -143  -1334       C  
ATOM   2661  NZ  LYS A 318      19.706  21.571  46.064  1.00 68.87           N  
ANISOU 2661  NZ  LYS A 318     8207   9986   7974    285   -154  -1566       N  
ATOM   2662  N   SER A 319      18.207  14.601  48.730  1.00 57.01           N  
ANISOU 2662  N   SER A 319     6357   9430   5876    497   -290   -531       N  
ATOM   2663  CA  SER A 319      17.565  13.781  49.763  1.00 53.86           C  
ANISOU 2663  CA  SER A 319     5828   9287   5351    592   -303   -366       C  
ATOM   2664  C   SER A 319      18.431  12.615  50.252  1.00 54.78           C  
ANISOU 2664  C   SER A 319     5848   9528   5439    619   -285   -225       C  
ATOM   2665  O   SER A 319      18.059  11.902  51.193  1.00 45.94           O  
ANISOU 2665  O   SER A 319     4598   8641   4216    714   -281    -72       O  
ATOM   2666  CB  SER A 319      16.218  13.245  49.272  1.00 51.98           C  
ANISOU 2666  CB  SER A 319     5647   8963   5141    580   -292   -190       C  
ATOM   2667  OG  SER A 319      16.396  12.101  48.465  1.00 58.80           O  
ANISOU 2667  OG  SER A 319     6567   9659   6115    512   -262    -23       O  
ATOM   2668  N   ALA A 320      19.579  12.414  49.611  1.00 58.85           N  
ANISOU 2668  N   ALA A 320     6421   9894   6045    545   -268   -264       N  
ATOM   2669  CA  ALA A 320      20.451  11.293  49.962  1.00 58.21           C  
ANISOU 2669  CA  ALA A 320     6263   9909   5946    569   -245   -128       C  
ATOM   2670  C   ALA A 320      20.969  11.340  51.408  1.00 62.16           C  
ANISOU 2670  C   ALA A 320     6577  10763   6279    695   -259   -169       C  
ATOM   2671  O   ALA A 320      20.848  10.357  52.139  1.00 66.18           O  
ANISOU 2671  O   ALA A 320     6972  11462   6710    782   -236     28       O  
ATOM   2672  CB  ALA A 320      21.610  11.164  48.970  1.00 51.80           C  
ANISOU 2672  CB  ALA A 320     5552   8875   5255    469   -228   -179       C  
ATOM   2673  N   PRO A 321      21.556  12.476  51.825  1.00 66.53           N  
ANISOU 2673  N   PRO A 321     7087  11411   6782    712   -293   -428       N  
ATOM   2674  CA  PRO A 321      22.007  12.582  53.222  1.00 63.78           C  
ANISOU 2674  CA  PRO A 321     6542  11433   6258    849   -316   -499       C  
ATOM   2675  C   PRO A 321      20.887  12.269  54.225  1.00 66.85           C  
ANISOU 2675  C   PRO A 321     6809  12090   6501    986   -323   -356       C  
ATOM   2676  O   PRO A 321      21.127  11.577  55.217  1.00 69.61           O  
ANISOU 2676  O   PRO A 321     6999  12733   6715   1114   -308   -233       O  
ATOM   2677  CB  PRO A 321      22.430  14.043  53.340  1.00 63.83           C  
ANISOU 2677  CB  PRO A 321     6540  11439   6275    828   -358   -832       C  
ATOM   2678  CG  PRO A 321      22.809  14.441  51.931  1.00 64.40           C  
ANISOU 2678  CG  PRO A 321     6798  11125   6545    668   -336   -901       C  
ATOM   2679  CD  PRO A 321      21.858  13.694  51.045  1.00 63.00           C  
ANISOU 2679  CD  PRO A 321     6752  10741   6446    615   -306   -665       C  
ATOM   2680  N   ALA A 322      19.680  12.769  53.967  1.00 65.29           N  
ANISOU 2680  N   ALA A 322     6679  11803   6326    969   -339   -359       N  
ATOM   2681  CA  ALA A 322      18.534  12.487  54.836  1.00 64.22           C  
ANISOU 2681  CA  ALA A 322     6434  11905   6060   1094   -344   -210       C  
ATOM   2682  C   ALA A 322      18.180  11.003  54.838  1.00 63.96           C  
ANISOU 2682  C   ALA A 322     6371  11879   6051   1114   -285    129       C  
ATOM   2683  O   ALA A 322      17.729  10.456  55.845  1.00 65.61           O  
ANISOU 2683  O   ALA A 322     6427  12369   6134   1252   -268    299       O  
ATOM   2684  CB  ALA A 322      17.323  13.313  54.411  1.00 52.21           C  
ANISOU 2684  CB  ALA A 322     5011  10254   4573   1057   -370   -281       C  
ATOM   2685  N   LEU A 323      18.391  10.355  53.701  1.00 54.30           N  
ANISOU 2685  N   LEU A 323     5286  10344   5001    983   -250    229       N  
ATOM   2686  CA  LEU A 323      17.977   8.978  53.547  1.00 54.68           C  
ANISOU 2686  CA  LEU A 323     5319  10335   5122    980   -193    531       C  
ATOM   2687  C   LEU A 323      18.870   8.086  54.383  1.00 53.45           C  
ANISOU 2687  C   LEU A 323     5017  10403   4889   1082   -151    672       C  
ATOM   2688  O   LEU A 323      18.384   7.157  55.031  1.00 60.87           O  
ANISOU 2688  O   LEU A 323     5839  11494   5794   1176   -101    927       O  
ATOM   2689  CB  LEU A 323      18.028   8.557  52.081  1.00 54.77           C  
ANISOU 2689  CB  LEU A 323     5509   9962   5340    820   -176    563       C  
ATOM   2690  CG  LEU A 323      17.157   7.369  51.646  1.00 55.50           C  
ANISOU 2690  CG  LEU A 323     5615   9913   5558    785   -132    822       C  
ATOM   2691  CD1 LEU A 323      17.871   6.581  50.546  1.00 50.39           C  
ANISOU 2691  CD1 LEU A 323     5076   8987   5084    673   -106    869       C  
ATOM   2692  CD2 LEU A 323      16.805   6.444  52.790  1.00 49.96           C  
ANISOU 2692  CD2 LEU A 323     4734   9467   4782    913    -82   1074       C  
ATOM   2693  N   LEU A 324      20.170   8.369  54.371  1.00 46.54           N  
ANISOU 2693  N   LEU A 324     4142   9551   3989   1069   -164    515       N  
ATOM   2694  CA  LEU A 324      21.116   7.587  55.163  1.00 53.64           C  
ANISOU 2694  CA  LEU A 324     4900  10684   4796   1176   -123    629       C  
ATOM   2695  C   LEU A 324      20.735   7.644  56.633  1.00 63.10           C  
ANISOU 2695  C   LEU A 324     5887  12308   5782   1376   -121    691       C  
ATOM   2696  O   LEU A 324      20.736   6.629  57.326  1.00 75.19           O  
ANISOU 2696  O   LEU A 324     7286  14029   7254   1495    -57    947       O  
ATOM   2697  CB  LEU A 324      22.546   8.105  55.012  1.00 53.07           C  
ANISOU 2697  CB  LEU A 324     4845  10613   4706   1140   -149    401       C  
ATOM   2698  CG  LEU A 324      23.407   7.642  53.836  1.00 54.42           C  
ANISOU 2698  CG  LEU A 324     5163  10470   5044    998   -128    409       C  
ATOM   2699  CD1 LEU A 324      23.236   6.154  53.551  1.00 53.86           C  
ANISOU 2699  CD1 LEU A 324     5102  10292   5072    994    -58    723       C  
ATOM   2700  CD2 LEU A 324      23.077   8.461  52.627  1.00 52.34           C  
ANISOU 2700  CD2 LEU A 324     5087   9875   4926    843   -164    245       C  
ATOM   2701  N   GLU A 325      20.420   8.840  57.111  1.00 62.80           N  
ANISOU 2701  N   GLU A 325     5809  12423   5629   1423   -188    457       N  
ATOM   2702  CA  GLU A 325      20.069   9.013  58.507  1.00 69.29           C  
ANISOU 2702  CA  GLU A 325     6422  13676   6230   1628   -200    478       C  
ATOM   2703  C   GLU A 325      18.845   8.196  58.876  1.00 63.97           C  
ANISOU 2703  C   GLU A 325     5683  13078   5543   1707   -148    797       C  
ATOM   2704  O   GLU A 325      18.819   7.591  59.948  1.00 57.26           O  
ANISOU 2704  O   GLU A 325     4643  12566   4547   1889   -104    985       O  
ATOM   2705  CB  GLU A 325      19.835  10.486  58.833  1.00 85.81           C  
ANISOU 2705  CB  GLU A 325     8498  15875   8230   1651   -288    149       C  
ATOM   2706  CG  GLU A 325      21.106  11.299  59.013  1.00 97.88           C  
ANISOU 2706  CG  GLU A 325     9988  17488   9715   1647   -336   -171       C  
ATOM   2707  CD  GLU A 325      20.850  12.574  59.792  1.00115.71           C  
ANISOU 2707  CD  GLU A 325    12143  19984  11839   1742   -416   -466       C  
ATOM   2708  OE1 GLU A 325      21.827  13.201  60.258  1.00123.24           O  
ANISOU 2708  OE1 GLU A 325    12998  21105  12723   1784   -457   -733       O  
ATOM   2709  OE2 GLU A 325      19.664  12.942  59.948  1.00119.70           O  
ANISOU 2709  OE2 GLU A 325    12657  20513  12312   1776   -438   -439       O  
ATOM   2710  N   MET A 326      17.839   8.184  57.995  1.00 64.07           N  
ANISOU 2710  N   MET A 326     5843  12791   5711   1578   -148    859       N  
ATOM   2711  CA  MET A 326      16.599   7.437  58.241  1.00 63.59           C  
ANISOU 2711  CA  MET A 326     5726  12764   5670   1629    -98   1151       C  
ATOM   2712  C   MET A 326      16.840   5.924  58.287  1.00 60.10           C  
ANISOU 2712  C   MET A 326     5222  12290   5323   1652      3   1487       C  
ATOM   2713  O   MET A 326      16.137   5.192  58.981  1.00 59.52           O  
ANISOU 2713  O   MET A 326     5012  12387   5215   1768     66   1763       O  
ATOM   2714  CB  MET A 326      15.545   7.705  57.163  1.00 63.49           C  
ANISOU 2714  CB  MET A 326     5889  12416   5820   1471   -120   1128       C  
ATOM   2715  CG  MET A 326      14.926   9.092  57.087  1.00 59.38           C  
ANISOU 2715  CG  MET A 326     5432  11902   5229   1456   -201    867       C  
ATOM   2716  SD  MET A 326      13.914   9.077  55.570  1.00 84.73           S  
ANISOU 2716  SD  MET A 326     8861  14671   8661   1260   -201    889       S  
ATOM   2717  CE  MET A 326      13.558  10.819  55.310  1.00 64.01           C  
ANISOU 2717  CE  MET A 326     6340  12007   5973   1231   -286    545       C  
ATOM   2718  N   LEU A 327      17.812   5.447  57.521  1.00 56.92           N  
ANISOU 2718  N   LEU A 327     4918  11656   5054   1543     25   1473       N  
ATOM   2719  CA  LEU A 327      18.098   4.016  57.505  1.00 62.48           C  
ANISOU 2719  CA  LEU A 327     5572  12300   5869   1560    124   1778       C  
ATOM   2720  C   LEU A 327      18.977   3.629  58.698  1.00 69.64           C  
ANISOU 2720  C   LEU A 327     6282  13588   6590   1757    172   1877       C  
ATOM   2721  O   LEU A 327      19.064   2.452  59.068  1.00 73.34           O  
ANISOU 2721  O   LEU A 327     6648  14116   7102   1839    272   2182       O  
ATOM   2722  CB  LEU A 327      18.760   3.605  56.183  1.00 53.18           C  
ANISOU 2722  CB  LEU A 327     4575  10726   4905   1375    128   1729       C  
ATOM   2723  CG  LEU A 327      17.903   3.716  54.918  1.00 52.22           C  
ANISOU 2723  CG  LEU A 327     4633  10226   4983   1195     99   1679       C  
ATOM   2724  CD1 LEU A 327      18.753   3.454  53.681  1.00 55.83           C  
ANISOU 2724  CD1 LEU A 327     5253  10353   5607   1042     91   1588       C  
ATOM   2725  CD2 LEU A 327      16.693   2.769  54.958  1.00 45.63           C  
ANISOU 2725  CD2 LEU A 327     3742   9321   4276   1200    162   1963       C  
ATOM   2726  N   SER A 328      19.634   4.625  59.286  1.00 71.86           N  
ANISOU 2726  N   SER A 328     6504  14128   6673   1838    104   1615       N  
ATOM   2727  CA  SER A 328      20.449   4.396  60.474  1.00 87.62           C  
ANISOU 2727  CA  SER A 328     8294  16541   8456   2046    137   1667       C  
ATOM   2728  C   SER A 328      19.548   4.054  61.651  1.00 83.49           C  
ANISOU 2728  C   SER A 328     7566  16373   7785   2258    187   1911       C  
ATOM   2729  O   SER A 328      19.844   3.156  62.433  1.00 78.56           O  
ANISOU 2729  O   SER A 328     6775  15995   7081   2426    279   2174       O  
ATOM   2730  CB  SER A 328      21.296   5.626  60.813  1.00 94.86           C  
ANISOU 2730  CB  SER A 328     9182  17653   9207   2078     41   1286       C  
ATOM   2731  OG  SER A 328      22.408   5.739  59.944  1.00 98.16           O  
ANISOU 2731  OG  SER A 328     9737  17824   9736   1929     21   1116       O  
ATOM   2732  N   GLU A 329      18.433   4.766  61.743  1.00 82.58           N  
ANISOU 2732  N   GLU A 329     7463  16277   7636   2253    132   1836       N  
ATOM   2733  CA  GLU A 329      17.554   4.669  62.891  1.00 88.16           C  
ANISOU 2733  CA  GLU A 329     7971  17354   8172   2463    161   2020       C  
ATOM   2734  C   GLU A 329      16.361   3.772  62.634  1.00 92.02           C  
ANISOU 2734  C   GLU A 329     8470  17663   8829   2423    243   2360       C  
ATOM   2735  O   GLU A 329      15.325   3.919  63.278  1.00 98.77           O  
ANISOU 2735  O   GLU A 329     9218  18721   9589   2536    246   2472       O  
ATOM   2736  CB  GLU A 329      17.069   6.058  63.253  1.00 90.58           C  
ANISOU 2736  CB  GLU A 329     8265  17833   8318   2503     45   1712       C  
ATOM   2737  CG  GLU A 329      18.126   7.108  63.042  1.00 96.61           C  
ANISOU 2737  CG  GLU A 329     9091  18590   9026   2443    -49   1305       C  
ATOM   2738  CD  GLU A 329      17.521   8.465  62.818  1.00109.30           C  
ANISOU 2738  CD  GLU A 329    10785  20132  10612   2375   -157    991       C  
ATOM   2739  OE1 GLU A 329      16.281   8.575  62.946  1.00117.50           O  
ANISOU 2739  OE1 GLU A 329    11817  21187  11639   2402   -162   1095       O  
ATOM   2740  OE2 GLU A 329      18.274   9.413  62.510  1.00111.35           O  
ANISOU 2740  OE2 GLU A 329    11114  20317  10877   2296   -232    646       O  
ATOM   2741  N   ARG A 330      16.442   2.955  61.625  1.00 90.77           N  
ANISOU 2741  N   ARG A 330     8433  17129   8925   2266    307   2517       N  
ATOM   2742  CA  ARG A 330      15.437   1.962  61.459  1.00 90.28           C  
ANISOU 2742  CA  ARG A 330     8383  16844   9075   2201    388   2821       C  
ATOM   2743  C   ARG A 330      14.076   2.632  61.524  1.00 87.90           C  
ANISOU 2743  C   ARG A 330     8094  16555   8750   2186    336   2785       C  
ATOM   2744  O   ARG A 330      13.102   2.069  61.994  1.00 91.48           O  
ANISOU 2744  O   ARG A 330     8447  17048   9265   2242    409   3073       O  
ATOM   2745  CB  ARG A 330      15.632   0.921  62.536  1.00 91.63           C  
ANISOU 2745  CB  ARG A 330     8349  17222   9245   2380    532   3228       C  
ATOM   2746  CG  ARG A 330      16.906   0.118  62.376  1.00 93.39           C  
ANISOU 2746  CG  ARG A 330     8492  17629   9362   2492    576   3245       C  
ATOM   2747  CD  ARG A 330      16.683  -0.938  61.324  1.00102.34           C  
ANISOU 2747  CD  ARG A 330     9618  18539  10727   2458    711   3566       C  
ATOM   2748  NE  ARG A 330      17.901  -1.616  60.908  1.00111.65           N  
ANISOU 2748  NE  ARG A 330    11031  19224  12166   2196    673   3424       N  
ATOM   2749  CZ  ARG A 330      18.056  -2.933  60.888  1.00113.43           C  
ANISOU 2749  CZ  ARG A 330    11310  19227  12562   2131    739   3530       C  
ATOM   2750  NH1 ARG A 330      17.054  -3.738  61.243  1.00108.10           N  
ANISOU 2750  NH1 ARG A 330    10844  18126  12104   1903    690   3374       N  
ATOM   2751  NH2 ARG A 330      19.202  -3.445  60.498  1.00113.31           N  
ANISOU 2751  NH2 ARG A 330    11135  19424  12493   2304    856   3791       N  
ATOM   2752  N   VAL A 331      14.001   3.812  60.953  1.00 80.03           N  
ANISOU 2752  N   VAL A 331     7217  15518   7672   2110    215   2435       N  
ATOM   2753  CA  VAL A 331      12.758   4.514  60.874  1.00 82.99           C  
ANISOU 2753  CA  VAL A 331     7634  15871   8026   2078    157   2360       C  
ATOM   2754  C   VAL A 331      11.814   3.692  60.026  1.00 83.39           C  
ANISOU 2754  C   VAL A 331     7778  15566   8341   1922    208   2556       C  
ATOM   2755  O   VAL A 331      12.232   2.880  59.237  1.00 74.48           O  
ANISOU 2755  O   VAL A 331     6779  14089   7430   1760    231   2562       O  
ATOM   2756  CB  VAL A 331      12.937   5.862  60.219  1.00 85.96           C  
ANISOU 2756  CB  VAL A 331     8171  16141   8348   1975     32   1944       C  
ATOM   2757  CG1 VAL A 331      11.626   6.438  59.917  1.00 81.14           C  
ANISOU 2757  CG1 VAL A 331     7607  15515   7708   1953    -24   1868       C  
ATOM   2758  CG2 VAL A 331      13.704   6.789  61.108  1.00 85.02           C  
ANISOU 2758  CG2 VAL A 331     7947  16359   7996   2118    -21   1719       C  
ATOM   2759  N   PRO A 332      10.521   3.923  60.218  1.00 88.56           N  
ANISOU 2759  N   PRO A 332     8354  16319   8976   1977    223   2708       N  
ATOM   2760  CA  PRO A 332       9.447   3.162  59.571  1.00 83.39           C  
ANISOU 2760  CA  PRO A 332     7756  15368   8559   1843    266   2881       C  
ATOM   2761  C   PRO A 332       9.323   3.368  58.069  1.00 77.05           C  
ANISOU 2761  C   PRO A 332     7192  14124   7958   1602    210   2666       C  
ATOM   2762  O   PRO A 332       9.706   4.398  57.574  1.00 64.34           O  
ANISOU 2762  O   PRO A 332     5719  12450   6277   1541    123   2359       O  
ATOM   2763  CB  PRO A 332       8.206   3.705  60.268  1.00 76.19           C  
ANISOU 2763  CB  PRO A 332     6771  14676   7502   1934    228   2892       C  
ATOM   2764  CG  PRO A 332       8.675   4.138  61.518  1.00 82.56           C  
ANISOU 2764  CG  PRO A 332     7383  15958   8027   2180    231   2933       C  
ATOM   2765  CD  PRO A 332       9.981   4.744  61.302  1.00 85.48           C  
ANISOU 2765  CD  PRO A 332     7786  16374   8317   2195    202   2733       C  
ATOM   2766  N   ALA A 333       8.792   2.382  57.362  1.00 77.43           N  
ANISOU 2766  N   ALA A 333     7276  13880   8263   1477    265   2830       N  
ATOM   2767  CA  ALA A 333       8.667   2.525  55.920  1.00 75.94           C  
ANISOU 2767  CA  ALA A 333     7291  13302   8261   1269    215   2644       C  
ATOM   2768  C   ALA A 333       7.969   3.827  55.542  1.00 78.41           C  
ANISOU 2768  C   ALA A 333     7721  13615   8458   1230    115   2386       C  
ATOM   2769  O   ALA A 333       8.329   4.467  54.548  1.00 81.69           O  
ANISOU 2769  O   ALA A 333     8314  13814   8911   1111     52   2135       O  
ATOM   2770  CB  ALA A 333       7.925   1.334  55.328  1.00 75.43           C  
ANISOU 2770  CB  ALA A 333     7203  12975   8481   1165    287   2861       C  
ATOM   2771  N   SER A 334       6.974   4.222  56.330  1.00 72.36           N  
ANISOU 2771  N   SER A 334     6850  13094   7549   1339    106   2456       N  
ATOM   2772  CA  SER A 334       6.175   5.402  55.996  1.00 67.27           C  
ANISOU 2772  CA  SER A 334     6308  12449   6802   1310     20   2237       C  
ATOM   2773  C   SER A 334       7.026   6.656  55.776  1.00 64.22           C  
ANISOU 2773  C   SER A 334     6048  12072   6281   1302    -64   1906       C  
ATOM   2774  O   SER A 334       6.613   7.576  55.062  1.00 59.90           O  
ANISOU 2774  O   SER A 334     5643  11393   5725   1227   -126   1693       O  
ATOM   2775  CB  SER A 334       5.089   5.662  57.053  1.00 68.03           C  
ANISOU 2775  CB  SER A 334     6253  12864   6730   1460     22   2367       C  
ATOM   2776  OG  SER A 334       5.586   5.593  58.378  1.00 76.38           O  
ANISOU 2776  OG  SER A 334     7132  14287   7601   1653     49   2479       O  
ATOM   2777  N   PHE A 335       8.214   6.681  56.381  1.00 61.86           N  
ANISOU 2777  N   PHE A 335     5690  11926   5888   1381    -58   1867       N  
ATOM   2778  CA  PHE A 335       9.074   7.866  56.352  1.00 63.78           C  
ANISOU 2778  CA  PHE A 335     6014  12212   6007   1387   -131   1555       C  
ATOM   2779  C   PHE A 335       9.952   8.025  55.114  1.00 66.08           C  
ANISOU 2779  C   PHE A 335     6492  12166   6449   1223   -149   1374       C  
ATOM   2780  O   PHE A 335      10.397   9.141  54.809  1.00 61.00           O  
ANISOU 2780  O   PHE A 335     5948  11477   5751   1193   -208   1101       O  
ATOM   2781  CB  PHE A 335       9.956   7.901  57.583  1.00 63.97           C  
ANISOU 2781  CB  PHE A 335     5875  12582   5848   1555   -125   1563       C  
ATOM   2782  CG  PHE A 335       9.250   8.371  58.795  1.00 69.42           C  
ANISOU 2782  CG  PHE A 335     6405  13655   6318   1740   -147   1596       C  
ATOM   2783  CD1 PHE A 335       8.465   7.500  59.534  1.00 78.08           C  
ANISOU 2783  CD1 PHE A 335     7336  14941   7388   1852    -80   1916       C  
ATOM   2784  CD2 PHE A 335       9.358   9.686  59.199  1.00 71.21           C  
ANISOU 2784  CD2 PHE A 335     6635  14051   6371   1808   -232   1310       C  
ATOM   2785  CE1 PHE A 335       7.804   7.931  60.667  1.00 78.02           C  
ANISOU 2785  CE1 PHE A 335     7171  15312   7162   2040   -101   1957       C  
ATOM   2786  CE2 PHE A 335       8.700  10.126  60.328  1.00 80.39           C  
ANISOU 2786  CE2 PHE A 335     7641  15584   7319   1993   -260   1328       C  
ATOM   2787  CZ  PHE A 335       7.922   9.246  61.065  1.00 79.71           C  
ANISOU 2787  CZ  PHE A 335     7391  15709   7186   2114   -197   1655       C  
ATOM   2788  N   VAL A 336      10.209   6.915  54.423  1.00 59.47           N  
ANISOU 2788  N   VAL A 336     5691  11096   5807   1125    -94   1526       N  
ATOM   2789  CA  VAL A 336      10.974   6.952  53.185  1.00 64.92           C  
ANISOU 2789  CA  VAL A 336     6552  11469   6646    977   -109   1380       C  
ATOM   2790  C   VAL A 336      10.040   6.897  51.974  1.00 65.74           C  
ANISOU 2790  C   VAL A 336     6787  11287   6905    847   -119   1359       C  
ATOM   2791  O   VAL A 336      10.485   6.857  50.824  1.00 60.20           O  
ANISOU 2791  O   VAL A 336     6224  10315   6336    729   -129   1256       O  
ATOM   2792  CB  VAL A 336      12.004   5.795  53.110  1.00 74.87           C  
ANISOU 2792  CB  VAL A 336     7776  12652   8020    956    -49   1525       C  
ATOM   2793  CG1 VAL A 336      12.782   5.674  54.426  1.00 68.12           C  
ANISOU 2793  CG1 VAL A 336     6756  12130   6997   1113    -25   1596       C  
ATOM   2794  CG2 VAL A 336      11.313   4.490  52.770  1.00 77.34           C  
ANISOU 2794  CG2 VAL A 336     8050  12809   8528    905     15   1780       C  
ATOM   2795  N   TYR A 337       8.738   6.888  52.236  1.00 66.92           N  
ANISOU 2795  N   TYR A 337     6882  11514   7031    880   -118   1458       N  
ATOM   2796  CA  TYR A 337       7.785   6.875  51.140  1.00 63.43           C  
ANISOU 2796  CA  TYR A 337     6547  10838   6717    771   -131   1425       C  
ATOM   2797  C   TYR A 337       8.021   8.078  50.257  1.00 57.88           C  
ANISOU 2797  C   TYR A 337     6017   9995   5979    712   -188   1149       C  
ATOM   2798  O   TYR A 337       8.238   7.928  49.061  1.00 68.92           O  
ANISOU 2798  O   TYR A 337     7538  11133   7514    604   -191   1075       O  
ATOM   2799  CB  TYR A 337       6.347   6.890  51.646  1.00 67.95           C  
ANISOU 2799  CB  TYR A 337     7030  11554   7233    827   -128   1545       C  
ATOM   2800  CG  TYR A 337       5.314   6.651  50.564  1.00 66.42           C  
ANISOU 2800  CG  TYR A 337     6914  11137   7185    720   -133   1540       C  
ATOM   2801  CD1 TYR A 337       5.260   5.435  49.896  1.00 65.97           C  
ANISOU 2801  CD1 TYR A 337     6843  10865   7357    624    -91   1665       C  
ATOM   2802  CD2 TYR A 337       4.383   7.634  50.220  1.00 64.67           C  
ANISOU 2802  CD2 TYR A 337     6770  10929   6873    721   -180   1403       C  
ATOM   2803  CE1 TYR A 337       4.320   5.199  48.902  1.00 69.25           C  
ANISOU 2803  CE1 TYR A 337     7312  11094   7907    532   -101   1637       C  
ATOM   2804  CE2 TYR A 337       3.430   7.405  49.222  1.00 68.17           C  
ANISOU 2804  CE2 TYR A 337     7273  11193   7437    634   -185   1391       C  
ATOM   2805  CZ  TYR A 337       3.408   6.179  48.566  1.00 67.72           C  
ANISOU 2805  CZ  TYR A 337     7191  10934   7605    539   -148   1501       C  
ATOM   2806  OH  TYR A 337       2.480   5.916  47.581  1.00 59.71           O  
ANISOU 2806  OH  TYR A 337     6216   9758   6713    457   -158   1467       O  
ATOM   2807  N   PRO A 338       8.005   9.281  50.848  1.00 56.26           N  
ANISOU 2807  N   PRO A 338     5815   9966   5597    791   -229    996       N  
ATOM   2808  CA  PRO A 338       7.996  10.494  50.023  1.00 58.97           C  
ANISOU 2808  CA  PRO A 338     6314  10169   5922    743   -269    754       C  
ATOM   2809  C   PRO A 338       9.241  10.624  49.148  1.00 52.47           C  
ANISOU 2809  C   PRO A 338     5608   9131   5198    658   -266    622       C  
ATOM   2810  O   PRO A 338       9.236  11.407  48.204  1.00 58.26           O  
ANISOU 2810  O   PRO A 338     6478   9691   5967    603   -280    464       O  
ATOM   2811  CB  PRO A 338       7.962  11.634  51.061  1.00 60.09           C  
ANISOU 2811  CB  PRO A 338     6399  10564   5869    859   -306    623       C  
ATOM   2812  CG  PRO A 338       7.662  10.984  52.386  1.00 66.31           C  
ANISOU 2812  CG  PRO A 338     6994  11648   6551    978   -291    816       C  
ATOM   2813  CD  PRO A 338       8.191   9.592  52.277  1.00 68.88           C  
ANISOU 2813  CD  PRO A 338     7266  11895   7010    935   -237   1020       C  
ATOM   2814  N   LEU A 339      10.291   9.875  49.465  1.00 54.21           N  
ANISOU 2814  N   LEU A 339     5769   9372   5457    656   -242    696       N  
ATOM   2815  CA  LEU A 339      11.549   9.986  48.731  1.00 57.76           C  
ANISOU 2815  CA  LEU A 339     6315   9645   5986    584   -240    577       C  
ATOM   2816  C   LEU A 339      11.547   9.166  47.442  1.00 50.74           C  
ANISOU 2816  C   LEU A 339     5521   8480   5279    476   -221    636       C  
ATOM   2817  O   LEU A 339      12.193   9.542  46.451  1.00 41.48           O  
ANISOU 2817  O   LEU A 339     4470   7116   4173    410   -227    507       O  
ATOM   2818  CB  LEU A 339      12.733   9.578  49.614  1.00 60.06           C  
ANISOU 2818  CB  LEU A 339     6501  10092   6226    637   -226    616       C  
ATOM   2819  CG  LEU A 339      13.061  10.490  50.798  1.00 58.61           C  
ANISOU 2819  CG  LEU A 339     6223  10185   5863    747   -254    492       C  
ATOM   2820  CD1 LEU A 339      14.353  10.041  51.468  1.00 47.28           C  
ANISOU 2820  CD1 LEU A 339     4692   8885   4386    792   -238    512       C  
ATOM   2821  CD2 LEU A 339      13.177  11.921  50.315  1.00 64.30           C  
ANISOU 2821  CD2 LEU A 339     7056  10808   6568    714   -290    230       C  
ATOM   2822  N   VAL A 340      10.817   8.053  47.458  1.00 50.52           N  
ANISOU 2822  N   VAL A 340     5425   8436   5336    465   -196    828       N  
ATOM   2823  CA  VAL A 340      10.789   7.132  46.321  1.00 50.47           C  
ANISOU 2823  CA  VAL A 340     5478   8183   5515    370   -182    879       C  
ATOM   2824  C   VAL A 340       9.401   6.974  45.716  1.00 52.24           C  
ANISOU 2824  C   VAL A 340     5718   8327   5803    338   -190    908       C  
ATOM   2825  O   VAL A 340       9.196   6.103  44.866  1.00 53.45           O  
ANISOU 2825  O   VAL A 340     5888   8301   6118    268   -181    953       O  
ATOM   2826  CB  VAL A 340      11.213   5.733  46.755  1.00 50.97           C  
ANISOU 2826  CB  VAL A 340     5432   8252   5683    370   -137   1083       C  
ATOM   2827  CG1 VAL A 340      12.521   5.791  47.561  1.00 54.33           C  
ANISOU 2827  CG1 VAL A 340     5808   8817   6019    426   -123   1083       C  
ATOM   2828  CG2 VAL A 340      10.094   5.106  47.578  1.00 53.16           C  
ANISOU 2828  CG2 VAL A 340     5567   8665   5965    420   -107   1283       C  
ATOM   2829  N   LYS A 341       8.461   7.812  46.152  1.00 56.95           N  
ANISOU 2829  N   LYS A 341     6303   9062   6273    392   -209    869       N  
ATOM   2830  CA  LYS A 341       7.033   7.584  45.911  1.00 60.79           C  
ANISOU 2830  CA  LYS A 341     6762   9541   6793    382   -212    932       C  
ATOM   2831  C   LYS A 341       6.671   7.019  44.531  1.00 62.72           C  
ANISOU 2831  C   LYS A 341     7077   9549   7204    291   -216    897       C  
ATOM   2832  O   LYS A 341       6.119   5.910  44.430  1.00 69.03           O  
ANISOU 2832  O   LYS A 341     7792  10289   8146    252   -196   1027       O  
ATOM   2833  CB  LYS A 341       6.204   8.835  46.211  1.00 65.81           C  
ANISOU 2833  CB  LYS A 341     7429  10314   7261    445   -241    831       C  
ATOM   2834  CG  LYS A 341       4.739   8.676  45.808  1.00 70.35           C  
ANISOU 2834  CG  LYS A 341     7990  10874   7864    431   -247    874       C  
ATOM   2835  CD  LYS A 341       3.920   9.917  46.116  1.00 67.38           C  
ANISOU 2835  CD  LYS A 341     7648  10640   7315    503   -274    779       C  
ATOM   2836  CE  LYS A 341       2.485   9.756  45.637  1.00 63.90           C  
ANISOU 2836  CE  LYS A 341     7196  10187   6895    489   -280    814       C  
ATOM   2837  NZ  LYS A 341       1.683  10.979  45.920  1.00 62.59           N  
ANISOU 2837  NZ  LYS A 341     7068  10160   6553    566   -304    723       N  
ATOM   2838  N   GLY A 342       6.964   7.772  43.475  1.00 49.99           N  
ANISOU 2838  N   GLY A 342     5606   7808   5581    265   -238    721       N  
ATOM   2839  CA  GLY A 342       6.671   7.295  42.129  1.00 51.58           C  
ANISOU 2839  CA  GLY A 342     5866   7815   5917    202   -247    666       C  
ATOM   2840  C   GLY A 342       7.818   7.652  41.207  1.00 53.88           C  
ANISOU 2840  C   GLY A 342     6278   7962   6232    178   -252    536       C  
ATOM   2841  O   GLY A 342       7.677   8.436  40.279  1.00 49.92           O  
ANISOU 2841  O   GLY A 342     5882   7391   5694    187   -262    405       O  
ATOM   2842  N   VAL A 343       8.975   7.075  41.480  1.00 51.55           N  
ANISOU 2842  N   VAL A 343     5962   7631   5995    157   -238    585       N  
ATOM   2843  CA  VAL A 343      10.189   7.504  40.823  1.00 45.69           C  
ANISOU 2843  CA  VAL A 343     5322   6784   5255    143   -239    475       C  
ATOM   2844  C   VAL A 343      10.643   6.483  39.801  1.00 43.41           C  
ANISOU 2844  C   VAL A 343     5052   6316   5125     88   -242    479       C  
ATOM   2845  O   VAL A 343      10.232   5.314  39.830  1.00 38.78           O  
ANISOU 2845  O   VAL A 343     4380   5687   4666     55   -239    581       O  
ATOM   2846  CB  VAL A 343      11.323   7.727  41.854  1.00 46.81           C  
ANISOU 2846  CB  VAL A 343     5430   7030   5325    167   -225    497       C  
ATOM   2847  CG1 VAL A 343      10.937   8.815  42.857  1.00 35.85           C  
ANISOU 2847  CG1 VAL A 343     4016   5829   3775    232   -230    457       C  
ATOM   2848  CG2 VAL A 343      11.655   6.410  42.577  1.00 32.54           C  
ANISOU 2848  CG2 VAL A 343     3503   5261   3598    158   -203    671       C  
ATOM   2849  N   SER A 344      11.497   6.938  38.892  1.00 46.29           N  
ANISOU 2849  N   SER A 344     5522   6575   5492     81   -246    367       N  
ATOM   2850  CA  SER A 344      12.068   6.073  37.877  1.00 44.73           C  
ANISOU 2850  CA  SER A 344     5348   6221   5425     44   -256    350       C  
ATOM   2851  C   SER A 344      12.910   4.982  38.520  1.00 50.22           C  
ANISOU 2851  C   SER A 344     5968   6905   6207     15   -241    469       C  
ATOM   2852  O   SER A 344      13.511   5.181  39.578  1.00 59.46           O  
ANISOU 2852  O   SER A 344     7101   8187   7303     34   -221    528       O  
ATOM   2853  CB  SER A 344      12.955   6.889  36.939  1.00 41.30           C  
ANISOU 2853  CB  SER A 344     5034   5707   4953     60   -254    227       C  
ATOM   2854  OG  SER A 344      14.203   7.178  37.544  1.00 38.42           O  
ANISOU 2854  OG  SER A 344     4679   5371   4547     56   -236    234       O  
ATOM   2855  N   ASN A 345      12.949   3.827  37.872  1.00 50.03           N  
ANISOU 2855  N   ASN A 345     5914   6753   6341    -22   -249    497       N  
ATOM   2856  CA  ASN A 345      13.905   2.787  38.221  1.00 42.48           C  
ANISOU 2856  CA  ASN A 345     4908   5750   5483    -45   -230    597       C  
ATOM   2857  C   ASN A 345      15.314   3.333  38.346  1.00 42.65           C  
ANISOU 2857  C   ASN A 345     4995   5796   5415    -29   -222    557       C  
ATOM   2858  O   ASN A 345      16.085   2.896  39.192  1.00 44.73           O  
ANISOU 2858  O   ASN A 345     5203   6119   5672    -22   -196    656       O  
ATOM   2859  CB  ASN A 345      13.908   1.714  37.142  1.00 44.11           C  
ANISOU 2859  CB  ASN A 345     5107   5781   5870    -82   -251    566       C  
ATOM   2860  CG  ASN A 345      12.667   0.863  37.170  1.00 52.52           C  
ANISOU 2860  CG  ASN A 345     6070   6808   7079   -111   -251    623       C  
ATOM   2861  OD1 ASN A 345      12.619  -0.193  36.535  1.00 54.16           O  
ANISOU 2861  OD1 ASN A 345     6234   6874   7469   -146   -262    613       O  
ATOM   2862  ND2 ASN A 345      11.649   1.310  37.916  1.00 48.58           N  
ANISOU 2862  ND2 ASN A 345     5522   6430   6506    -96   -239    677       N  
ATOM   2863  N   GLU A 346      15.657   4.281  37.476  1.00 44.52           N  
ANISOU 2863  N   GLU A 346     5342   5989   5585    -18   -239    417       N  
ATOM   2864  CA  GLU A 346      17.006   4.827  37.460  1.00 46.62           C  
ANISOU 2864  CA  GLU A 346     5668   6257   5788    -11   -228    368       C  
ATOM   2865  C   GLU A 346      17.294   5.578  38.757  1.00 47.20           C  
ANISOU 2865  C   GLU A 346     5703   6494   5735     13   -208    387       C  
ATOM   2866  O   GLU A 346      18.389   5.459  39.323  1.00 43.99           O  
ANISOU 2866  O   GLU A 346     5274   6140   5302     15   -194    413       O  
ATOM   2867  CB  GLU A 346      17.230   5.712  36.226  1.00 50.85           C  
ANISOU 2867  CB  GLU A 346     6318   6707   6297      3   -238    231       C  
ATOM   2868  CG  GLU A 346      17.356   4.916  34.923  1.00 54.57           C  
ANISOU 2868  CG  GLU A 346     6819   7040   6877     -2   -262    197       C  
ATOM   2869  CD  GLU A 346      16.030   4.328  34.455  1.00 57.14           C  
ANISOU 2869  CD  GLU A 346     7100   7332   7277     -3   -288    191       C  
ATOM   2870  OE1 GLU A 346      14.990   4.999  34.601  1.00 60.98           O  
ANISOU 2870  OE1 GLU A 346     7588   7884   7699     16   -286    167       O  
ATOM   2871  OE2 GLU A 346      16.022   3.196  33.931  1.00 64.28           O  
ANISOU 2871  OE2 GLU A 346     7965   8146   8313    -23   -310    201       O  
ATOM   2872  N   THR A 347      16.300   6.336  39.222  1.00 42.71           N  
ANISOU 2872  N   THR A 347     5121   6019   5086     37   -210    366       N  
ATOM   2873  CA  THR A 347      16.396   7.051  40.481  1.00 46.23           C  
ANISOU 2873  CA  THR A 347     5515   6642   5409     73   -199    367       C  
ATOM   2874  C   THR A 347      16.592   6.054  41.620  1.00 41.88           C  
ANISOU 2874  C   THR A 347     4838   6211   4862     91   -182    522       C  
ATOM   2875  O   THR A 347      17.290   6.328  42.596  1.00 30.29           O  
ANISOU 2875  O   THR A 347     3315   4891   3303    126   -171    528       O  
ATOM   2876  CB  THR A 347      15.126   7.879  40.759  1.00 48.47           C  
ANISOU 2876  CB  THR A 347     5796   7006   5613    104   -207    331       C  
ATOM   2877  OG1 THR A 347      15.081   9.004  39.876  1.00 48.89           O  
ANISOU 2877  OG1 THR A 347     5961   6974   5641    107   -208    191       O  
ATOM   2878  CG2 THR A 347      15.115   8.380  42.215  1.00 46.10           C  
ANISOU 2878  CG2 THR A 347     5409   6920   5188    155   -203    349       C  
ATOM   2879  N   ILE A 348      15.969   4.894  41.486  1.00 42.37           N  
ANISOU 2879  N   ILE A 348     4845   6214   5038     73   -175    647       N  
ATOM   2880  CA  ILE A 348      16.062   3.887  42.532  1.00 51.12           C  
ANISOU 2880  CA  ILE A 348     5825   7426   6174     99   -141    827       C  
ATOM   2881  C   ILE A 348      17.501   3.439  42.635  1.00 45.99           C  
ANISOU 2881  C   ILE A 348     5174   6766   5535    100   -124    849       C  
ATOM   2882  O   ILE A 348      18.109   3.523  43.706  1.00 42.44           O  
ANISOU 2882  O   ILE A 348     4649   6492   4984    154   -103    901       O  
ATOM   2883  CB  ILE A 348      15.155   2.679  42.242  1.00 54.12           C  
ANISOU 2883  CB  ILE A 348     6142   7699   6721     68   -128    955       C  
ATOM   2884  CG1 ILE A 348      13.702   3.004  42.608  1.00 50.81           C  
ANISOU 2884  CG1 ILE A 348     5674   7363   6267     85   -132    984       C  
ATOM   2885  CG2 ILE A 348      15.637   1.459  42.989  1.00 50.64           C  
ANISOU 2885  CG2 ILE A 348     5589   7289   6364     87    -77   1147       C  
ATOM   2886  CD1 ILE A 348      12.761   1.847  42.421  1.00 52.19           C  
ANISOU 2886  CD1 ILE A 348     5766   7441   6621     50   -114   1107       C  
ATOM   2887  N   CYS A 349      18.043   2.983  41.506  1.00 42.56           N  
ANISOU 2887  N   CYS A 349     4817   6141   5212     50   -136    801       N  
ATOM   2888  CA  CYS A 349      19.452   2.599  41.407  1.00 42.45           C  
ANISOU 2888  CA  CYS A 349     4821   6099   5210     48   -125    805       C  
ATOM   2889  C   CYS A 349      20.327   3.665  42.047  1.00 48.79           C  
ANISOU 2889  C   CYS A 349     5633   7052   5853     80   -126    713       C  
ATOM   2890  O   CYS A 349      21.236   3.369  42.829  1.00 51.88           O  
ANISOU 2890  O   CYS A 349     5959   7564   6190    115   -103    771       O  
ATOM   2891  CB  CYS A 349      19.848   2.478  39.937  1.00 47.87           C  
ANISOU 2891  CB  CYS A 349     5618   6579   5992      0   -154    702       C  
ATOM   2892  SG  CYS A 349      18.840   1.343  38.970  1.00 54.94           S  
ANISOU 2892  SG  CYS A 349     6501   7287   7086    -39   -169    740       S  
ATOM   2893  N   HIS A 350      20.029   4.914  41.693  1.00 38.97           N  
ANISOU 2893  N   HIS A 350     4464   5802   4542     71   -150    562       N  
ATOM   2894  CA  HIS A 350      20.750   6.076  42.178  1.00 34.17           C  
ANISOU 2894  CA  HIS A 350     3865   5304   3813     90   -153    436       C  
ATOM   2895  C   HIS A 350      20.690   6.108  43.710  1.00 38.66           C  
ANISOU 2895  C   HIS A 350     4302   6123   4264    159   -141    499       C  
ATOM   2896  O   HIS A 350      21.685   6.364  44.368  1.00 44.79           O  
ANISOU 2896  O   HIS A 350     5030   7028   4960    188   -135    455       O  
ATOM   2897  CB  HIS A 350      20.134   7.336  41.549  1.00 32.40           C  
ANISOU 2897  CB  HIS A 350     3732   5012   3568     76   -170    290       C  
ATOM   2898  CG  HIS A 350      20.901   8.594  41.792  1.00 34.85           C  
ANISOU 2898  CG  HIS A 350     4065   5371   3806     81   -168    136       C  
ATOM   2899  ND1 HIS A 350      22.165   8.614  42.355  1.00 39.40           N  
ANISOU 2899  ND1 HIS A 350     4594   6035   4343     86   -160    103       N  
ATOM   2900  CD2 HIS A 350      20.602   9.890  41.507  1.00 34.30           C  
ANISOU 2900  CD2 HIS A 350     4055   5264   3713     79   -167     -1       C  
ATOM   2901  CE1 HIS A 350      22.593   9.859  42.431  1.00 36.14           C  
ANISOU 2901  CE1 HIS A 350     4202   5633   3895     81   -159    -58       C  
ATOM   2902  NE2 HIS A 350      21.661  10.656  41.930  1.00 38.45           N  
ANISOU 2902  NE2 HIS A 350     4562   5844   4204     77   -159   -119       N  
ATOM   2903  N   PHE A 351      19.529   5.829  44.286  1.00 36.45           N  
ANISOU 2903  N   PHE A 351     3951   5929   3968    193   -136    601       N  
ATOM   2904  CA  PHE A 351      19.474   5.683  45.738  1.00 45.86           C  
ANISOU 2904  CA  PHE A 351     5000   7380   5046    280   -118    694       C  
ATOM   2905  C   PHE A 351      20.353   4.518  46.189  1.00 42.04           C  
ANISOU 2905  C   PHE A 351     4435   6952   4588    310    -79    848       C  
ATOM   2906  O   PHE A 351      21.120   4.635  47.154  1.00 42.33           O  
ANISOU 2906  O   PHE A 351     4381   7197   4505    381    -67    849       O  
ATOM   2907  CB  PHE A 351      18.040   5.517  46.234  1.00 45.90           C  
ANISOU 2907  CB  PHE A 351     4937   7465   5037    316   -114    803       C  
ATOM   2908  CG  PHE A 351      17.326   6.822  46.471  1.00 47.19           C  
ANISOU 2908  CG  PHE A 351     5123   7715   5092    339   -147    660       C  
ATOM   2909  CD1 PHE A 351      16.121   7.098  45.839  1.00 43.23           C  
ANISOU 2909  CD1 PHE A 351     4684   7106   4634    307   -163    641       C  
ATOM   2910  CD2 PHE A 351      17.867   7.780  47.322  1.00 44.27           C  
ANISOU 2910  CD2 PHE A 351     4705   7537   4578    398   -164    533       C  
ATOM   2911  CE1 PHE A 351      15.459   8.307  46.061  1.00 47.21           C  
ANISOU 2911  CE1 PHE A 351     5211   7689   5037    336   -189    515       C  
ATOM   2912  CE2 PHE A 351      17.211   8.990  47.551  1.00 45.19           C  
ANISOU 2912  CE2 PHE A 351     4839   7724   4608    423   -194    391       C  
ATOM   2913  CZ  PHE A 351      16.007   9.254  46.916  1.00 48.02           C  
ANISOU 2913  CZ  PHE A 351     5269   7967   5009    393   -204    390       C  
ATOM   2914  N   LEU A 352      20.283   3.407  45.469  1.00 35.51           N  
ANISOU 2914  N   LEU A 352     3635   5940   3916    264    -59    964       N  
ATOM   2915  CA  LEU A 352      21.104   2.266  45.849  1.00 47.03           C  
ANISOU 2915  CA  LEU A 352     5022   7431   5417    296    -13   1120       C  
ATOM   2916  C   LEU A 352      22.603   2.521  45.681  1.00 46.86           C  
ANISOU 2916  C   LEU A 352     5042   7422   5340    291    -21   1016       C  
ATOM   2917  O   LEU A 352      23.425   1.840  46.309  1.00 48.66           O  
ANISOU 2917  O   LEU A 352     5189   7763   5535    347     18   1125       O  
ATOM   2918  CB  LEU A 352      20.673   1.005  45.105  1.00 51.18           C  
ANISOU 2918  CB  LEU A 352     5560   7738   6148    246     11   1255       C  
ATOM   2919  CG  LEU A 352      19.333   0.423  45.568  1.00 52.02           C  
ANISOU 2919  CG  LEU A 352     5571   7866   6328    266     42   1418       C  
ATOM   2920  CD1 LEU A 352      18.692  -0.383  44.452  1.00 48.88           C  
ANISOU 2920  CD1 LEU A 352     5222   7199   6151    182     36   1438       C  
ATOM   2921  CD2 LEU A 352      19.514  -0.419  46.820  1.00 53.40           C  
ANISOU 2921  CD2 LEU A 352     5587   8226   6477    363    116   1651       C  
ATOM   2922  N   ALA A 353      22.971   3.503  44.857  1.00 33.47           N  
ANISOU 2922  N   ALA A 353     3464   5619   3634    230    -63    816       N  
ATOM   2923  CA  ALA A 353      24.397   3.784  44.674  1.00 37.03           C  
ANISOU 2923  CA  ALA A 353     3948   6077   4044    219    -68    715       C  
ATOM   2924  C   ALA A 353      25.054   4.294  45.959  1.00 41.15           C  
ANISOU 2924  C   ALA A 353     4356   6881   4399    298    -61    671       C  
ATOM   2925  O   ALA A 353      26.268   4.246  46.103  1.00 39.80           O  
ANISOU 2925  O   ALA A 353     4166   6773   4182    310    -54    631       O  
ATOM   2926  CB  ALA A 353      24.638   4.762  43.520  1.00 34.13           C  
ANISOU 2926  CB  ALA A 353     3719   5534   3716    144   -103    525       C  
ATOM   2927  N   TYR A 354      24.247   4.764  46.901  1.00 46.13           N  
ANISOU 2927  N   TYR A 354     4900   7697   4931    360    -65    674       N  
ATOM   2928  CA  TYR A 354      24.782   5.325  48.134  1.00 46.61           C  
ANISOU 2928  CA  TYR A 354     4837   8052   4822    450    -67    602       C  
ATOM   2929  C   TYR A 354      24.895   4.297  49.255  1.00 57.93           C  
ANISOU 2929  C   TYR A 354     6114   9719   6177    568    -18    813       C  
ATOM   2930  O   TYR A 354      25.453   4.587  50.331  1.00 49.01           O  
ANISOU 2930  O   TYR A 354     4857   8875   4888    668    -15    771       O  
ATOM   2931  CB  TYR A 354      23.882   6.447  48.623  1.00 44.94           C  
ANISOU 2931  CB  TYR A 354     4600   7948   4527    477   -101    478       C  
ATOM   2932  CG  TYR A 354      24.149   7.796  48.017  1.00 48.68           C  
ANISOU 2932  CG  TYR A 354     5172   8308   5018    405   -140    225       C  
ATOM   2933  CD1 TYR A 354      23.521   8.193  46.842  1.00 49.15           C  
ANISOU 2933  CD1 TYR A 354     5375   8105   5194    317   -151    176       C  
ATOM   2934  CD2 TYR A 354      25.007   8.692  48.638  1.00 53.94           C  
ANISOU 2934  CD2 TYR A 354     5772   9133   5589    435   -159     33       C  
ATOM   2935  CE1 TYR A 354      23.755   9.450  46.295  1.00 51.11           C  
ANISOU 2935  CE1 TYR A 354     5706   8245   5470    264   -170    -33       C  
ATOM   2936  CE2 TYR A 354      25.252   9.944  48.103  1.00 56.98           C  
ANISOU 2936  CE2 TYR A 354     6235   9393   6021    367   -182   -193       C  
ATOM   2937  CZ  TYR A 354      24.623  10.324  46.933  1.00 55.11           C  
ANISOU 2937  CZ  TYR A 354     6146   8887   5906    284   -182   -213       C  
ATOM   2938  OH  TYR A 354      24.868  11.581  46.414  1.00 52.23           O  
ANISOU 2938  OH  TYR A 354     5851   8394   5599    229   -189   -415       O  
ATOM   2939  N   LEU A 355      24.349   3.103  49.058  1.00 58.72           N  
ANISOU 2939  N   LEU A 355     6206   9716   6390    568     26   1041       N  
ATOM   2940  CA  LEU A 355      24.389   2.197  50.195  1.00 59.70           C  
ANISOU 2940  CA  LEU A 355     6167  10074   6443    696     89   1263       C  
ATOM   2941  C   LEU A 355      24.927   0.776  50.017  1.00 62.78           C  
ANISOU 2941  C   LEU A 355     6536  10373   6944    709    156   1480       C  
ATOM   2942  O   LEU A 355      25.056   0.243  48.903  1.00 55.63           O  
ANISOU 2942  O   LEU A 355     5746   9182   6209    608    153   1489       O  
ATOM   2943  CB  LEU A 355      23.071   2.208  50.984  1.00 58.12           C  
ANISOU 2943  CB  LEU A 355     5867  10019   6198    770    105   1383       C  
ATOM   2944  CG  LEU A 355      21.766   1.783  50.342  1.00 51.75           C  
ANISOU 2944  CG  LEU A 355     5116   8990   5558    698    112   1489       C  
ATOM   2945  CD1 LEU A 355      20.834   2.978  50.236  1.00 40.13           C  
ANISOU 2945  CD1 LEU A 355     3695   7527   4027    668     50   1319       C  
ATOM   2946  CD2 LEU A 355      22.027   1.114  48.992  1.00 57.45           C  
ANISOU 2946  CD2 LEU A 355     5972   9369   6486    573    111   1492       C  
ATOM   2947  N   SER A 356      25.267   0.203  51.169  1.00 68.07           N  
ANISOU 2947  N   SER A 356     7047  11313   7504    850    218   1649       N  
ATOM   2948  CA  SER A 356      25.717  -1.169  51.281  1.00 73.88           C  
ANISOU 2948  CA  SER A 356     7727  12017   8328    900    303   1895       C  
ATOM   2949  C   SER A 356      25.278  -1.680  52.645  1.00 69.02           C  
ANISOU 2949  C   SER A 356     6914  11702   7610   1070    382   2135       C  
ATOM   2950  O   SER A 356      24.674  -0.941  53.423  1.00 62.67           O  
ANISOU 2950  O   SER A 356     6027  11126   6660   1143    359   2086       O  
ATOM   2951  CB  SER A 356      27.238  -1.247  51.132  1.00 71.87           C  
ANISOU 2951  CB  SER A 356     7496  11802   8009    908    302   1815       C  
ATOM   2952  OG  SER A 356      27.858  -0.169  51.807  1.00 67.44           O  
ANISOU 2952  OG  SER A 356     6879  11514   7232    967    256   1616       O  
ATOM   2953  N   GLY A 357      25.566  -2.948  52.912  1.00 67.82           N  
ANISOU 2953  N   GLY A 357     6683  11544   7540   1141    481   2401       N  
ATOM   2954  CA  GLY A 357      25.266  -3.564  54.189  1.00 73.83           C  
ANISOU 2954  CA  GLY A 357     7245  12593   8214   1323    579   2673       C  
ATOM   2955  C   GLY A 357      23.826  -3.486  54.664  1.00 76.37           C  
ANISOU 2955  C   GLY A 357     7487  12969   8560   1357    597   2795       C  
ATOM   2956  O   GLY A 357      22.881  -3.897  53.977  1.00 76.03           O  
ANISOU 2956  O   GLY A 357     7508  12643   8737   1247    604   2865       O  
ATOM   2957  N   GLU A 358      23.668  -2.954  55.870  1.00 73.88           N  
ANISOU 2957  N   GLU A 358     7020  13041   8011   1518    603   2814       N  
ATOM   2958  CA  GLU A 358      22.384  -2.962  56.545  1.00 75.06           C  
ANISOU 2958  CA  GLU A 358     7056  13318   8146   1594    635   2974       C  
ATOM   2959  C   GLU A 358      21.424  -1.955  55.960  1.00 67.08           C  
ANISOU 2959  C   GLU A 358     6162  12165   7160   1465    531   2751       C  
ATOM   2960  O   GLU A 358      20.226  -2.232  55.818  1.00 62.60           O  
ANISOU 2960  O   GLU A 358     5586  11475   6725   1425    553   2878       O  
ATOM   2961  CB  GLU A 358      22.570  -2.687  58.035  1.00 83.75           C  
ANISOU 2961  CB  GLU A 358     7945  14914   8962   1832    670   3054       C  
ATOM   2962  CG  GLU A 358      22.908  -3.916  58.832  1.00 93.25           C  
ANISOU 2962  CG  GLU A 358     8976  16287  10167   2007    817   3414       C  
ATOM   2963  CD  GLU A 358      21.961  -5.078  58.556  1.00102.39           C  
ANISOU 2963  CD  GLU A 358    10112  17182  11609   1964    924   3737       C  
ATOM   2964  OE1 GLU A 358      22.073  -5.704  57.473  1.00 99.06           O  
ANISOU 2964  OE1 GLU A 358     9828  16360  11450   1798    932   3741       O  
ATOM   2965  OE2 GLU A 358      21.115  -5.374  59.435  1.00110.31           O  
ANISOU 2965  OE2 GLU A 358    10949  18385  12578   2103   1002   3985       O  
ATOM   2966  N   LYS A 359      21.950  -0.792  55.626  1.00 64.25           N  
ANISOU 2966  N   LYS A 359     5904  11830   6679   1404    425   2423       N  
ATOM   2967  CA  LYS A 359      21.147   0.241  55.025  1.00 65.64           C  
ANISOU 2967  CA  LYS A 359     6198  11870   6872   1288    330   2198       C  
ATOM   2968  C   LYS A 359      20.574  -0.153  53.684  1.00 58.83           C  
ANISOU 2968  C   LYS A 359     5497  10580   6277   1104    321   2207       C  
ATOM   2969  O   LYS A 359      19.453   0.148  53.397  1.00 58.98           O  
ANISOU 2969  O   LYS A 359     5547  10500   6362   1051    298   2204       O  
ATOM   2970  CB  LYS A 359      21.920   1.513  54.909  1.00 62.55           C  
ANISOU 2970  CB  LYS A 359     5876  11561   6330   1258    233   1853       C  
ATOM   2971  CG  LYS A 359      22.445   1.926  56.176  1.00 68.14           C  
ANISOU 2971  CG  LYS A 359     6410  12702   6777   1441    232   1803       C  
ATOM   2972  CD  LYS A 359      22.542   3.397  56.207  1.00 84.67           C  
ANISOU 2972  CD  LYS A 359     8448  14895   8827   1506    284   1870       C  
ATOM   2973  CE  LYS A 359      23.747   3.851  56.991  1.00 95.59           C  
ANISOU 2973  CE  LYS A 359     9942  16191  10187   1405    208   1558       C  
ATOM   2974  NZ  LYS A 359      23.573   5.228  57.526  1.00 99.85           N  
ANISOU 2974  NZ  LYS A 359    10464  16890  10585   1417    118   1261       N  
ATOM   2975  N   GLU A 360      21.361  -0.833  52.882  1.00 55.70           N  
ANISOU 2975  N   GLU A 360     5190   9948   6025   1020    339   2216       N  
ATOM   2976  CA  GLU A 360      20.905  -1.359  51.588  1.00 55.28           C  
ANISOU 2976  CA  GLU A 360     5271   9505   6227    863    330   2218       C  
ATOM   2977  C   GLU A 360      19.845  -2.425  51.807  1.00 57.51           C  
ANISOU 2977  C   GLU A 360     5457   9713   6680    881    411   2496       C  
ATOM   2978  O   GLU A 360      18.745  -2.325  51.273  1.00 51.25           O  
ANISOU 2978  O   GLU A 360     4711   8757   6004    797    384   2472       O  
ATOM   2979  CB  GLU A 360      22.081  -1.940  50.806  1.00 55.13           C  
ANISOU 2979  CB  GLU A 360     5341   9297   6310    800    338   2187       C  
ATOM   2980  CG  GLU A 360      21.718  -2.812  49.617  1.00 56.25           C  
ANISOU 2980  CG  GLU A 360     5577   9070   6726    674    347   2236       C  
ATOM   2981  CD  GLU A 360      22.957  -3.429  48.944  1.00 63.93           C  
ANISOU 2981  CD  GLU A 360     6622   9890   7780    636    356   2215       C  
ATOM   2982  OE1 GLU A 360      23.996  -2.736  48.829  1.00 66.96           O  
ANISOU 2982  OE1 GLU A 360     7067  10353   8023    635    310   2042       O  
ATOM   2983  OE2 GLU A 360      22.897  -4.609  48.528  1.00 60.05           O  
ANISOU 2983  OE2 GLU A 360     6120   9197   7501    607    410   2369       O  
ATOM   2984  N   GLY A 361      20.176  -3.430  52.617  1.00 65.46           N  
ANISOU 2984  N   GLY A 361     6319  10848   7703    999    516   2764       N  
ATOM   2985  CA  GLY A 361      19.232  -4.473  52.985  1.00 65.78           C  
ANISOU 2985  CA  GLY A 361     6237  10840   7916   1036    615   3064       C  
ATOM   2986  C   GLY A 361      17.877  -3.971  53.468  1.00 63.64           C  
ANISOU 2986  C   GLY A 361     5898  10690   7594   1064    601   3100       C  
ATOM   2987  O   GLY A 361      16.834  -4.456  53.038  1.00 60.45           O  
ANISOU 2987  O   GLY A 361     5491  10083   7396    985    623   3191       O  
ATOM   2988  N   LEU A 362      17.856  -2.992  54.353  1.00 67.48           N  
ANISOU 2988  N   LEU A 362     6319  11515   7804   1180    564   3020       N  
ATOM   2989  CA  LEU A 362      16.601  -2.453  54.823  1.00 67.47           C  
ANISOU 2989  CA  LEU A 362     6256  11663   7715   1221    539   3028       C  
ATOM   2990  C   LEU A 362      15.845  -1.668  53.786  1.00 73.67           C  
ANISOU 2990  C   LEU A 362     7215  12167   8610   1044    446   2801       C  
ATOM   2991  O   LEU A 362      14.750  -2.032  53.407  1.00 79.82           O  
ANISOU 2991  O   LEU A 362     7999  12741   9589    963    468   2897       O  
ATOM   2992  CB  LEU A 362      16.917  -1.448  55.920  1.00 68.28           C  
ANISOU 2992  CB  LEU A 362     6290  12160   7494   1363    487   2889       C  
ATOM   2993  CG  LEU A 362      16.031  -1.124  57.114  1.00 67.71           C  
ANISOU 2993  CG  LEU A 362     6040  12457   7231   1538    509   3015       C  
ATOM   2994  CD1 LEU A 362      16.185   0.299  57.481  1.00 62.54           C  
ANISOU 2994  CD1 LEU A 362     5409  12040   6314   1586    398   2709       C  
ATOM   2995  CD2 LEU A 362      14.613  -1.485  56.931  1.00 60.76           C  
ANISOU 2995  CD2 LEU A 362     5125  11466   6494   1499    539   3180       C  
ATOM   2996  N   PHE A 363      16.481  -0.642  53.254  1.00 71.31           N  
ANISOU 2996  N   PHE A 363     7047  11867   8179    992    346   2498       N  
ATOM   2997  CA  PHE A 363      15.953   0.107  52.123  1.00 65.48           C  
ANISOU 2997  CA  PHE A 363     6478  10892   7508    845    259   2263       C  
ATOM   2998  C   PHE A 363      15.427  -0.801  50.999  1.00 61.62           C  
ANISOU 2998  C   PHE A 363     6060  10047   7304    709    278   2328       C  
ATOM   2999  O   PHE A 363      14.363  -0.540  50.443  1.00 53.39           O  
ANISOU 2999  O   PHE A 363     5069   8880   6335    635    243   2269       O  
ATOM   3000  CB  PHE A 363      17.029   1.072  51.617  1.00 60.46           C  
ANISOU 3000  CB  PHE A 363     5975  10228   6768    798    184   1977       C  
ATOM   3001  CG  PHE A 363      16.599   1.923  50.454  1.00 64.93           C  
ANISOU 3001  CG  PHE A 363     6714  10569   7389    667    105   1741       C  
ATOM   3002  CD1 PHE A 363      15.612   2.884  50.605  1.00 60.63           C  
ANISOU 3002  CD1 PHE A 363     6182  10105   6749    678     58   1639       C  
ATOM   3003  CD2 PHE A 363      17.205   1.778  49.206  1.00 62.26           C  
ANISOU 3003  CD2 PHE A 363     6520   9951   7185    549     80   1625       C  
ATOM   3004  CE1 PHE A 363      15.232   3.670  49.527  1.00 54.75           C  
ANISOU 3004  CE1 PHE A 363     5593   9161   6050    573     -3   1437       C  
ATOM   3005  CE2 PHE A 363      16.825   2.564  48.133  1.00 50.00           C  
ANISOU 3005  CE2 PHE A 363     5114   8212   5670    451     18   1424       C  
ATOM   3006  CZ  PHE A 363      15.841   3.510  48.294  1.00 48.55           C  
ANISOU 3006  CZ  PHE A 363     4943   8108   5396    464    -19   1335       C  
ATOM   3007  N   LYS A 364      16.150  -1.876  50.686  1.00 59.08           N  
ANISOU 3007  N   LYS A 364     5732   9573   7141    684    334   2445       N  
ATOM   3008  CA  LYS A 364      15.714  -2.796  49.634  1.00 56.50           C  
ANISOU 3008  CA  LYS A 364     5456   8912   7100    562    350   2488       C  
ATOM   3009  C   LYS A 364      14.311  -3.336  49.897  1.00 70.80           C  
ANISOU 3009  C   LYS A 364     7158  10693   9050    559    398   2668       C  
ATOM   3010  O   LYS A 364      13.522  -3.529  48.968  1.00 73.21           O  
ANISOU 3010  O   LYS A 364     7521  10763   9533    446    369   2598       O  
ATOM   3011  CB  LYS A 364      16.681  -3.970  49.504  1.00 48.93           C  
ANISOU 3011  CB  LYS A 364     4470   7830   6291    565    420   2626       C  
ATOM   3012  CG  LYS A 364      17.854  -3.707  48.609  1.00 56.72           C  
ANISOU 3012  CG  LYS A 364     5605   8685   7262    499    361   2421       C  
ATOM   3013  CD  LYS A 364      18.782  -4.901  48.557  1.00 59.05           C  
ANISOU 3013  CD  LYS A 364     5864   8876   7696    516    433   2572       C  
ATOM   3014  CE  LYS A 364      19.736  -4.803  47.374  1.00 63.19           C  
ANISOU 3014  CE  LYS A 364     6546   9198   8265    425    369   2367       C  
ATOM   3015  NZ  LYS A 364      20.459  -6.094  47.207  1.00 69.21           N  
ANISOU 3015  NZ  LYS A 364     7274   9818   9205    432    439   2520       N  
ATOM   3016  N   SER A 365      14.034  -3.761  51.123  1.00 72.82           N  
ANISOU 3016  N   SER A 365     7245  11200   9224    691    475   2903       N  
ATOM   3017  CA  SER A 365      12.693  -4.199  51.457  1.00 79.52           C  
ANISOU 3017  CA  SER A 365     7965  12025  10223    698    540   3119       C  
ATOM   3018  C   SER A 365      11.675  -3.111  51.603  1.00 80.89           C  
ANISOU 3018  C   SER A 365     8133  12365  10237    720    482   3036       C  
ATOM   3019  O   SER A 365      10.589  -3.207  51.106  1.00 85.61           O  
ANISOU 3019  O   SER A 365     8682  12873  10973    673    498   3115       O  
ATOM   3020  CB  SER A 365      12.639  -5.179  52.611  1.00 80.01           C  
ANISOU 3020  CB  SER A 365     7830  12255  10315    839    675   3465       C  
ATOM   3021  OG  SER A 365      12.295  -6.457  52.102  1.00 83.34           O  
ANISOU 3021  OG  SER A 365     8138  12530  10999    805    757   3688       O  
ATOM   3022  N   TYR A 366      12.048  -2.048  52.270  1.00 76.19           N  
ANISOU 3022  N   TYR A 366     7580  12013   9357    794    416   2873       N  
ATOM   3023  CA  TYR A 366      11.111  -0.943  52.379  1.00 73.15           C  
ANISOU 3023  CA  TYR A 366     7225  11751   8816    802    343   2735       C  
ATOM   3024  C   TYR A 366      10.567  -0.657  50.984  1.00 78.67           C  
ANISOU 3024  C   TYR A 366     8086  12151   9654    638    272   2527       C  
ATOM   3025  O   TYR A 366       9.389  -0.348  50.802  1.00 88.79           O  
ANISOU 3025  O   TYR A 366     9368  13418  10950    608    246   2504       O  
ATOM   3026  CB  TYR A 366      11.818   0.293  52.930  1.00 67.87           C  
ANISOU 3026  CB  TYR A 366     6592  11339   7855    890    277   2542       C  
ATOM   3027  CG  TYR A 366      11.859   0.352  54.436  1.00 75.35           C  
ANISOU 3027  CG  TYR A 366     7356  12674   8598   1082    323   2708       C  
ATOM   3028  CD1 TYR A 366      12.156   1.539  55.097  1.00 77.53           C  
ANISOU 3028  CD1 TYR A 366     7624  13229   8603   1181    258   2527       C  
ATOM   3029  CD2 TYR A 366      11.575  -0.774  55.203  1.00 80.93           C  
ANISOU 3029  CD2 TYR A 366     7883  13476   9389   1176    437   3045       C  
ATOM   3030  CE1 TYR A 366      12.185   1.598  56.487  1.00 81.55           C  
ANISOU 3030  CE1 TYR A 366     7949  14128   8909   1376    293   2664       C  
ATOM   3031  CE2 TYR A 366      11.598  -0.725  56.585  1.00 82.75           C  
ANISOU 3031  CE2 TYR A 366     7931  14093   9417   1376    484   3211       C  
ATOM   3032  CZ  TYR A 366      11.906   0.464  57.227  1.00 83.45           C  
ANISOU 3032  CZ  TYR A 366     8012  14480   9214   1481    407   3012       C  
ATOM   3033  OH  TYR A 366      11.934   0.515  58.610  1.00 81.96           O  
ANISOU 3033  OH  TYR A 366     7627  14708   8807   1699    448   3161       O  
ATOM   3034  N   LEU A 367      11.451  -0.783  50.004  1.00 67.84           N  
ANISOU 3034  N   LEU A 367     6843  10558   8375    546    243   2382       N  
ATOM   3035  CA  LEU A 367      11.153  -0.546  48.599  1.00 63.60           C  
ANISOU 3035  CA  LEU A 367     6459   9750   7958    410    177   2175       C  
ATOM   3036  C   LEU A 367      10.133  -1.555  48.072  1.00 67.72           C  
ANISOU 3036  C   LEU A 367     6923  10065   8743    330    212   2289       C  
ATOM   3037  O   LEU A 367       9.227  -1.213  47.298  1.00 60.09           O  
ANISOU 3037  O   LEU A 367     6018   8989   7825    257    161   2160       O  
ATOM   3038  CB  LEU A 367      12.457  -0.699  47.823  1.00 63.43           C  
ANISOU 3038  CB  LEU A 367     6549   9566   7986    355    157   2053       C  
ATOM   3039  CG  LEU A 367      12.846   0.177  46.639  1.00 68.82           C  
ANISOU 3039  CG  LEU A 367     7415  10103   8631    276     74   1773       C  
ATOM   3040  CD1 LEU A 367      12.400   1.624  46.813  1.00 63.08           C  
ANISOU 3040  CD1 LEU A 367     6748   9525   7694    307     15   1608       C  
ATOM   3041  CD2 LEU A 367      14.357   0.088  46.495  1.00 69.49           C  
ANISOU 3041  CD2 LEU A 367     7555  10161   8688    280     75   1720       C  
ATOM   3042  N   LEU A 368      10.297  -2.808  48.490  1.00 71.41           N  
ANISOU 3042  N   LEU A 368     7263  10479   9389    347    303   2528       N  
ATOM   3043  CA  LEU A 368       9.430  -3.889  48.041  1.00 72.60           C  
ANISOU 3043  CA  LEU A 368     7335  10412   9836    267    349   2642       C  
ATOM   3044  C   LEU A 368       8.090  -3.811  48.743  1.00 77.16           C  
ANISOU 3044  C   LEU A 368     7788  11130  10399    306    379   2785       C  
ATOM   3045  O   LEU A 368       7.046  -4.073  48.147  1.00 77.83           O  
ANISOU 3045  O   LEU A 368     7854  11067  10649    222    367   2753       O  
ATOM   3046  CB  LEU A 368      10.091  -5.247  48.283  1.00 67.12           C  
ANISOU 3046  CB  LEU A 368     6542   9600   9361    277    449   2860       C  
ATOM   3047  CG  LEU A 368      11.133  -5.528  47.195  1.00 65.12           C  
ANISOU 3047  CG  LEU A 368     6420   9116   9207    198    408   2689       C  
ATOM   3048  CD1 LEU A 368      11.765  -6.900  47.334  1.00 59.60           C  
ANISOU 3048  CD1 LEU A 368     5630   8270   8744    203    506   2891       C  
ATOM   3049  CD2 LEU A 368      10.497  -5.362  45.818  1.00 61.99           C  
ANISOU 3049  CD2 LEU A 368     6128   8490   8937     71    322   2450       C  
ATOM   3050  N   LYS A 369       8.162  -3.336  49.964  1.00 79.16           N  
ANISOU 3050  N   LYS A 369     7947  11687  10443    443    416   2933       N  
ATOM   3051  CA  LYS A 369       7.015  -3.121  50.775  1.00 86.88           C  
ANISOU 3051  CA  LYS A 369     8802  12849  11358    506    441   3073       C  
ATOM   3052  C   LYS A 369       6.166  -2.090  50.092  1.00 87.65           C  
ANISOU 3052  C   LYS A 369     9019  12945  11338    448    336   2825       C  
ATOM   3053  O   LYS A 369       4.981  -2.141  50.200  1.00 96.15           O  
ANISOU 3053  O   LYS A 369    10024  14071  12438    446    341   2889       O  
ATOM   3054  CB  LYS A 369       7.455  -2.605  52.132  1.00 91.28           C  
ANISOU 3054  CB  LYS A 369     9245  13773  11664    687    484   3238       C  
ATOM   3055  CG  LYS A 369       6.706  -3.157  53.318  1.00 97.04           C  
ANISOU 3055  CG  LYS A 369     9781  14691  12398    781    561   3511       C  
ATOM   3056  CD  LYS A 369       7.552  -3.011  54.584  1.00105.42           C  
ANISOU 3056  CD  LYS A 369    10696  16115  13245    984    627   3720       C  
ATOM   3057  CE  LYS A 369       6.733  -2.524  55.770  1.00109.33           C  
ANISOU 3057  CE  LYS A 369    11061  16555  13925   1036    762   4012       C  
ATOM   3058  NZ  LYS A 369       7.532  -1.814  56.821  1.00107.77           N  
ANISOU 3058  NZ  LYS A 369    10980  16208  13760    987    744   3882       N  
ATOM   3059  N   ILE A 370       6.780  -1.065  49.531  1.00 79.90           N  
ANISOU 3059  N   ILE A 370     8215  11908  10235    407    248   2552       N  
ATOM   3060  CA  ILE A 370       6.116  -0.085  48.680  1.00 68.41           C  
ANISOU 3060  CA  ILE A 370     6885  10439   8669    362    157   2313       C  
ATOM   3061  C   ILE A 370       5.571  -0.542  47.332  1.00 66.22           C  
ANISOU 3061  C   ILE A 370     6688   9866   8607    225    123   2175       C  
ATOM   3062  O   ILE A 370       4.534  -0.118  46.909  1.00 61.16           O  
ANISOU 3062  O   ILE A 370     6091   9212   7934    192     75   2055       O  
ATOM   3063  CB  ILE A 370       6.929   1.153  48.551  1.00 58.77           C  
ANISOU 3063  CB  ILE A 370     5808   9312   7211    397     86   2086       C  
ATOM   3064  CG1 ILE A 370       7.126   1.733  49.932  1.00 52.16           C  
ANISOU 3064  CG1 ILE A 370     4885   8801   6133    541     99   2164       C  
ATOM   3065  CG2 ILE A 370       6.236   2.111  47.651  1.00 52.66           C  
ANISOU 3065  CG2 ILE A 370     5173   8474   6361    345      6   1846       C  
ATOM   3066  CD1 ILE A 370       8.186   2.724  50.034  1.00 47.25           C  
ANISOU 3066  CD1 ILE A 370     4377   8258   5316    572     41   1944       C  
ATOM   3067  N   LYS A 371       6.322  -1.387  46.656  1.00 71.69           N  
ANISOU 3067  N   LYS A 371     7395  10337   9507    157    146   2181       N  
ATOM   3068  CA  LYS A 371       5.981  -1.852  45.334  1.00 75.50           C  
ANISOU 3068  CA  LYS A 371     7941  10552  10194     40    108   2027       C  
ATOM   3069  C   LYS A 371       4.717  -2.622  45.348  1.00 82.03           C  
ANISOU 3069  C   LYS A 371     8637  11299  11230    -12    140   2128       C  
ATOM   3070  O   LYS A 371       3.908  -2.545  44.448  1.00 80.20           O  
ANISOU 3070  O   LYS A 371     8447  10984  11040    -73     85   1966       O  
ATOM   3071  CB  LYS A 371       7.027  -2.798  44.819  1.00 74.87           C  
ANISOU 3071  CB  LYS A 371     7884  10264  10301    -10    128   2024       C  
ATOM   3072  CG  LYS A 371       6.633  -3.356  43.503  1.00 75.29           C  
ANISOU 3072  CG  LYS A 371     7956  10054  10597   -119     94   1885       C  
ATOM   3073  CD  LYS A 371       7.111  -4.747  43.330  1.00 83.05           C  
ANISOU 3073  CD  LYS A 371     8873  10826  11857   -164    148   1979       C  
ATOM   3074  CE  LYS A 371       7.054  -5.169  41.898  1.00 82.71           C  
ANISOU 3074  CE  LYS A 371     8855  10531  12040   -263     97   1786       C  
ATOM   3075  NZ  LYS A 371       7.394  -6.595  41.755  1.00 83.37           N  
ANISOU 3075  NZ  LYS A 371     8862  10395  12421   -307    150   1873       N  
ATOM   3076  N   ASN A 372       4.598  -3.413  46.387  1.00 89.34           N  
ANISOU 3076  N   ASN A 372     9396  12248  12302     15    235   2399       N  
ATOM   3077  CA  ASN A 372       3.492  -4.293  46.601  1.00 99.08           C  
ANISOU 3077  CA  ASN A 372    10476  13436  13735    -23    284   2538       C  
ATOM   3078  C   ASN A 372       3.029  -3.874  47.934  1.00102.91           C  
ANISOU 3078  C   ASN A 372    10834  14200  14066     93    344   2781       C  
ATOM   3079  O   ASN A 372       3.767  -3.302  48.656  1.00100.78           O  
ANISOU 3079  O   ASN A 372    10609  14160  13521    199    331   2791       O  
ATOM   3080  CB  ASN A 372       3.976  -5.717  46.798  1.00 99.68           C  
ANISOU 3080  CB  ASN A 372    10441  13245  14189   -103    356   2652       C  
ATOM   3081  CG  ASN A 372       4.611  -6.292  45.591  1.00 99.40           C  
ANISOU 3081  CG  ASN A 372    10429  13146  14192    -72    401   2730       C  
ATOM   3082  OD1 ASN A 372       4.214  -6.019  44.475  1.00 99.53           O  
ANISOU 3082  OD1 ASN A 372    10504  12929  14384   -148    379   2604       O  
ATOM   3083  ND2 ASN A 372       5.596  -7.128  45.805  1.00 96.59           N  
ANISOU 3083  ND2 ASN A 372    10023  13015  13662     49    461   2932       N  
ATOM   3084  N   THR A 373       1.798  -4.161  48.259  1.00108.35           N  
ANISOU 3084  N   THR A 373    11356  14878  14934     78    411   2971       N  
ATOM   3085  CA  THR A 373       1.297  -4.010  49.604  1.00112.29           C  
ANISOU 3085  CA  THR A 373    11730  15663  15273    194    460   3190       C  
ATOM   3086  C   THR A 373       1.369  -2.528  49.820  1.00104.00           C  
ANISOU 3086  C   THR A 373    10814  14865  13836    278    366   3013       C  
ATOM   3087  O   THR A 373       1.351  -1.988  50.902  1.00 93.15           O  
ANISOU 3087  O   THR A 373     9404  13759  12229    412    384   3120       O  
ATOM   3088  CB  THR A 373       2.087  -4.869  50.602  1.00118.26           C  
ANISOU 3088  CB  THR A 373    12315  16523  16097    300    593   3542       C  
ATOM   3089  OG1 THR A 373       1.669  -6.236  50.470  1.00126.55           O  
ANISOU 3089  OG1 THR A 373    13445  17699  16941    389    582   3515       O  
ATOM   3090  CG2 THR A 373       1.824  -4.428  52.017  1.00108.87           C  
ANISOU 3090  CG2 THR A 373    11007  15034  15326    208    691   3697       C  
ATOM   3091  N   LYS A 374       1.488  -1.908  48.677  1.00106.38           N  
ANISOU 3091  N   LYS A 374    11266  15073  14082    201    267   2728       N  
ATOM   3092  CA  LYS A 374       1.020  -0.598  48.394  1.00114.59           C  
ANISOU 3092  CA  LYS A 374    12438  16299  14802    262    181   2538       C  
ATOM   3093  C   LYS A 374      -0.334  -1.023  47.931  1.00121.86           C  
ANISOU 3093  C   LYS A 374    13355  17235  15713    225    140   2456       C  
ATOM   3094  O   LYS A 374      -0.679  -2.182  48.000  1.00126.16           O  
ANISOU 3094  O   LYS A 374    13869  18015  16050    311    125   2494       O  
ATOM   3095  CB  LYS A 374       1.741   0.014  47.199  1.00113.83           C  
ANISOU 3095  CB  LYS A 374    12536  16068  14645    216    110   2275       C  
ATOM   3096  CG  LYS A 374       1.541  -0.786  45.923  1.00110.84           C  
ANISOU 3096  CG  LYS A 374    12195  15376  14542     88    104   2176       C  
ATOM   3097  CD  LYS A 374       1.501   0.069  44.668  1.00103.37           C  
ANISOU 3097  CD  LYS A 374    11392  14321  13561     23     17   1893       C  
ATOM   3098  CE  LYS A 374       2.754  -0.073  43.846  1.00 93.54           C  
ANISOU 3098  CE  LYS A 374    10324  13028  12188     29    -35   1696       C  
ATOM   3099  NZ  LYS A 374       3.772   0.902  44.262  1.00 85.79           N  
ANISOU 3099  NZ  LYS A 374     9425  11809  11362    -59    -77   1507       N  
ATOM   3100  N   LEU A 375      -1.099  -0.093  47.392  1.00122.06           N  
ANISOU 3100  N   LEU A 375    13399  17017  15962    103    121   2338       N  
ATOM   3101  CA  LEU A 375      -2.334  -0.485  46.755  1.00118.17           C  
ANISOU 3101  CA  LEU A 375    12902  16528  15471     61     78   2232       C  
ATOM   3102  C   LEU A 375      -3.447  -0.591  47.766  1.00112.44           C  
ANISOU 3102  C   LEU A 375    12014  16005  14703    124    127   2455       C  
ATOM   3103  O   LEU A 375      -3.551  -1.565  48.511  1.00110.38           O  
ANISOU 3103  O   LEU A 375    11596  15793  14549    162    216   2726       O  
ATOM   3104  CB  LEU A 375      -2.159  -1.819  46.027  1.00118.41           C  
ANISOU 3104  CB  LEU A 375    12908  16280  15802    -72     69   2117       C  
ATOM   3105  CG  LEU A 375      -3.396  -2.368  45.311  1.00120.25           C  
ANISOU 3105  CG  LEU A 375    13020  16286  16385   -148    142   2253       C  
ATOM   3106  CD1 LEU A 375      -4.502  -2.676  46.309  1.00120.19           C  
ANISOU 3106  CD1 LEU A 375    12826  16378  16462    -92    253   2600       C  
ATOM   3107  CD2 LEU A 375      -3.881  -1.391  44.251  1.00121.62           C  
ANISOU 3107  CD2 LEU A 375    13132  16241  16836   -270    121   2116       C  
ATOM   3108  N   GLU A 376      -4.287   0.425  47.770  1.00108.30           N  
ANISOU 3108  N   GLU A 376    11527  15610  14011    147     73   2350       N  
ATOM   3109  CA  GLU A 376      -5.463   0.445  48.587  1.00101.52           C  
ANISOU 3109  CA  GLU A 376    10521  14955  13096    209    109   2542       C  
ATOM   3110  C   GLU A 376      -6.245  -0.738  48.116  1.00 98.66           C  
ANISOU 3110  C   GLU A 376    10000  14425  13061    102    160   2640       C  
ATOM   3111  O   GLU A 376      -6.223  -1.074  46.958  1.00 98.94           O  
ANISOU 3111  O   GLU A 376    10077  14257  13258     -9    121   2447       O  
ATOM   3112  CB  GLU A 376      -6.225   1.735  48.421  1.00 99.63           C  
ANISOU 3112  CB  GLU A 376    10382  14911  12563    274     32   2385       C  
ATOM   3113  CG  GLU A 376      -6.083   2.619  49.607  1.00 97.72           C  
ANISOU 3113  CG  GLU A 376    10059  14989  12083    419     50   2559       C  
ATOM   3114  CD  GLU A 376      -4.912   2.221  50.441  1.00 96.26           C  
ANISOU 3114  CD  GLU A 376     9870  14926  11780    519     78   2660       C  
ATOM   3115  OE1 GLU A 376      -3.979   1.612  49.898  1.00 98.45           O  
ANISOU 3115  OE1 GLU A 376    10069  15487  11850    656     89   2792       O  
ATOM   3116  OE2 GLU A 376      -4.923   2.507  51.642  1.00 91.38           O  
ANISOU 3116  OE2 GLU A 376     9319  14134  11266    468     85   2602       O  
ATOM   3117  N   LYS A 377      -6.904  -1.391  49.044  1.00 97.27           N  
ANISOU 3117  N   LYS A 377     9628  14340  12990    142    252   2941       N  
ATOM   3118  CA  LYS A 377      -7.629  -2.607  48.783  1.00 98.46           C  
ANISOU 3118  CA  LYS A 377     9593  14328  13488     44    323   3080       C  
ATOM   3119  C   LYS A 377      -9.079  -2.365  48.466  1.00 97.93           C  
ANISOU 3119  C   LYS A 377     9492  14334  13384     11    279   2987       C  
ATOM   3120  O   LYS A 377      -9.574  -2.694  47.399  1.00 94.33           O  
ANISOU 3120  O   LYS A 377     9051  13690  13101   -107    237   2786       O  
ATOM   3121  CB  LYS A 377      -7.595  -3.412  50.066  1.00101.72           C  
ANISOU 3121  CB  LYS A 377     9802  14842  14004    122    452   3467       C  
ATOM   3122  CG  LYS A 377      -7.868  -2.556  51.287  1.00 94.39           C  
ANISOU 3122  CG  LYS A 377     8841  14293  12731    298    456   3627       C  
ATOM   3123  CD  LYS A 377      -6.934  -1.406  51.339  1.00 79.48           C  
ANISOU 3123  CD  LYS A 377     7149  12557  10493    391    370   3439       C  
ATOM   3124  CE  LYS A 377      -7.392  -0.352  52.264  1.00 70.81           C  
ANISOU 3124  CE  LYS A 377     6069  11794   9041    525    317   3426       C  
ATOM   3125  NZ  LYS A 377      -7.641  -0.867  53.587  1.00 69.03           N  
ANISOU 3125  NZ  LYS A 377     5674  11842   8712    684    399   3743       N  
ATOM   3126  N   ILE A 378      -9.742  -1.744  49.413  1.00101.03           N  
ANISOU 3126  N   ILE A 378     9835  15019  13534    127    283   3121       N  
ATOM   3127  CA  ILE A 378     -11.156  -1.436  49.272  1.00111.48           C  
ANISOU 3127  CA  ILE A 378    11097  16445  14815    113    255   3086       C  
ATOM   3128  C   ILE A 378     -11.440   0.063  49.172  1.00109.74           C  
ANISOU 3128  C   ILE A 378    11046  16450  14201    204    154   2888       C  
ATOM   3129  O   ILE A 378     -12.236   0.494  48.335  1.00107.39           O  
ANISOU 3129  O   ILE A 378    10806  16133  13864    155     90   2684       O  
ATOM   3130  CB  ILE A 378     -11.960  -2.024  50.442  1.00124.05           C  
ANISOU 3130  CB  ILE A 378    12452  18190  16491    170    357   3439       C  
ATOM   3131  CG1 ILE A 378     -11.525  -1.382  51.758  1.00130.47           C  
ANISOU 3131  CG1 ILE A 378    13261  19321  16992    357    376   3627       C  
ATOM   3132  CG2 ILE A 378     -11.773  -3.534  50.513  1.00126.74           C  
ANISOU 3132  CG2 ILE A 378    12610  18283  17261     76    474   3650       C  
ATOM   3133  CD1 ILE A 378     -12.408  -1.746  52.924  1.00135.25           C  
ANISOU 3133  CD1 ILE A 378    13640  20143  17604    449    465   3967       C  
ATOM   3134  N   ASN A 379     -10.788   0.852  50.023  1.00108.25           N  
ANISOU 3134  N   ASN A 379    10927  16475  13727    342    141   2941       N  
ATOM   3135  CA  ASN A 379     -11.018   2.298  50.067  1.00103.30           C  
ANISOU 3135  CA  ASN A 379    10448  16064  12738    441     55   2768       C  
ATOM   3136  C   ASN A 379     -10.702   3.061  48.794  1.00 94.97           C  
ANISOU 3136  C   ASN A 379     9610  14869  11605    386    -32   2430       C  
ATOM   3137  O   ASN A 379      -9.540   3.193  48.407  1.00 91.72           O  
ANISOU 3137  O   ASN A 379     9323  14331  11194    369    -50   2313       O  
ATOM   3138  CB  ASN A 379     -10.226   2.930  51.198  1.00104.04           C  
ANISOU 3138  CB  ASN A 379    10563  16390  12576    595     57   2861       C  
ATOM   3139  CG  ASN A 379     -10.903   2.772  52.519  1.00112.65           C  
ANISOU 3139  CG  ASN A 379    11464  17758  13579    717    113   3148       C  
ATOM   3140  OD1 ASN A 379     -10.643   3.523  53.453  1.00116.94           O  
ANISOU 3140  OD1 ASN A 379    12013  18570  13850    869     93   3189       O  
ATOM   3141  ND2 ASN A 379     -11.793   1.792  52.611  1.00115.37           N  
ANISOU 3141  ND2 ASN A 379    11627  18049  14159    656    183   3348       N  
ATOM   3142  N   GLY A 380     -11.744   3.571  48.153  1.00 88.92           N  
ANISOU 3142  N   GLY A 380     8883  14138  10765    368    -81   2284       N  
ATOM   3143  CA  GLY A 380     -11.566   4.572  47.127  1.00 80.15           C  
ANISOU 3143  CA  GLY A 380     7977  12979   9498    368   -157   1990       C  
ATOM   3144  C   GLY A 380     -11.841   5.915  47.772  1.00 81.49           C  
ANISOU 3144  C   GLY A 380     8230  13413   9321    510   -197   1958       C  
ATOM   3145  O   GLY A 380     -12.222   5.994  48.944  1.00 81.81           O  
ANISOU 3145  O   GLY A 380     8160  13675   9250    602   -173   2149       O  
ATOM   3146  N   GLU A 381     -11.630   6.977  47.008  1.00 84.25           N  
ANISOU 3146  N   GLU A 381     8768  13740   9504    537   -253   1718       N  
ATOM   3147  CA  GLU A 381     -12.108   8.306  47.362  1.00 82.98           C  
ANISOU 3147  CA  GLU A 381     8693  13795   9039    660   -293   1642       C  
ATOM   3148  C   GLU A 381     -13.631   8.223  47.495  1.00 75.30           C  
ANISOU 3148  C   GLU A 381     7609  12973   8030    675   -294   1715       C  
ATOM   3149  O   GLU A 381     -14.261   8.885  48.330  1.00 61.13           O  
ANISOU 3149  O   GLU A 381     5783  11422   6022    787   -306   1786       O  
ATOM   3150  CB  GLU A 381     -11.746   9.298  46.246  1.00 93.03           C  
ANISOU 3150  CB  GLU A 381    10175  14964  10207    666   -336   1374       C  
ATOM   3151  CG  GLU A 381     -10.248   9.371  45.878  1.00100.54           C  
ANISOU 3151  CG  GLU A 381    11245  15736  11219    635   -334   1278       C  
ATOM   3152  CD  GLU A 381      -9.762   8.202  45.016  1.00106.72           C  
ANISOU 3152  CD  GLU A 381    11997  16270  12282    504   -315   1264       C  
ATOM   3153  OE1 GLU A 381      -9.483   8.421  43.814  1.00111.96           O  
ANISOU 3153  OE1 GLU A 381    12778  16781  12979    466   -336   1078       O  
ATOM   3154  OE2 GLU A 381      -9.652   7.069  45.536  1.00105.52           O  
ANISOU 3154  OE2 GLU A 381    11698  16075  12318    448   -276   1441       O  
ATOM   3155  N   TYR A 382     -14.217   7.383  46.651  1.00 78.69           N  
ANISOU 3155  N   TYR A 382     7968  13257   8674    562   -284   1688       N  
ATOM   3156  CA  TYR A 382     -15.653   7.184  46.650  1.00 75.38           C  
ANISOU 3156  CA  TYR A 382     7427  12954   8259    555   -282   1742       C  
ATOM   3157  C   TYR A 382     -16.191   6.238  47.728  1.00 80.07           C  
ANISOU 3157  C   TYR A 382     7793  13643   8986    546   -224   2033       C  
ATOM   3158  O   TYR A 382     -17.393   6.233  47.998  1.00 82.79           O  
ANISOU 3158  O   TYR A 382     8030  14142   9286    568   -221   2112       O  
ATOM   3159  CB  TYR A 382     -16.168   6.848  45.240  1.00 74.36           C  
ANISOU 3159  CB  TYR A 382     7315  12666   8274    455   -304   1548       C  
ATOM   3160  CG  TYR A 382     -16.867   8.043  44.686  1.00 79.34           C  
ANISOU 3160  CG  TYR A 382     8073  13432   8641    540   -352   1370       C  
ATOM   3161  CD1 TYR A 382     -18.164   8.326  45.071  1.00 87.41           C  
ANISOU 3161  CD1 TYR A 382     9012  14667   9534    594   -359   1433       C  
ATOM   3162  CD2 TYR A 382     -16.210   8.950  43.864  1.00 85.81           C  
ANISOU 3162  CD2 TYR A 382     9094  14182   9328    583   -383   1160       C  
ATOM   3163  CE1 TYR A 382     -18.813   9.444  44.619  1.00 91.66           C  
ANISOU 3163  CE1 TYR A 382     9666  15342   9820    686   -396   1283       C  
ATOM   3164  CE2 TYR A 382     -16.861  10.080  43.398  1.00 90.55           C  
ANISOU 3164  CE2 TYR A 382     9807  14911   9686    677   -412   1019       C  
ATOM   3165  CZ  TYR A 382     -18.167  10.315  43.790  1.00 94.55           C  
ANISOU 3165  CZ  TYR A 382    10230  15629  10067    730   -419   1081       C  
ATOM   3166  OH  TYR A 382     -18.853  11.423  43.359  1.00 99.34           O  
ANISOU 3166  OH  TYR A 382    10944  16372  10429    833   -443    952       O  
ATOM   3167  N   LEU A 383     -15.317   5.457  48.360  1.00 79.84           N  
ANISOU 3167  N   LEU A 383     7685  13536   9113    524   -171   2205       N  
ATOM   3168  CA  LEU A 383     -15.731   4.730  49.551  1.00 80.28           C  
ANISOU 3168  CA  LEU A 383     7528  13725   9249    558   -103   2515       C  
ATOM   3169  C   LEU A 383     -15.791   5.760  50.665  1.00 85.38           C  
ANISOU 3169  C   LEU A 383     8199  14685   9555    734   -126   2590       C  
ATOM   3170  O   LEU A 383     -16.523   5.608  51.648  1.00 89.91           O  
ANISOU 3170  O   LEU A 383     8616  15478  10068    814    -92   2813       O  
ATOM   3171  CB  LEU A 383     -14.755   3.606  49.908  1.00 76.85           C  
ANISOU 3171  CB  LEU A 383     7000  13127   9074    502    -30   2689       C  
ATOM   3172  CG  LEU A 383     -15.380   2.424  50.678  1.00 75.15           C  
ANISOU 3172  CG  LEU A 383     6526  12933   9095    477     67   3008       C  
ATOM   3173  CD1 LEU A 383     -15.680   2.725  52.146  1.00 54.29           C  
ANISOU 3173  CD1 LEU A 383     3766  10619   6242    643    103   3271       C  
ATOM   3174  CD2 LEU A 383     -16.647   1.942  49.959  1.00 78.41           C  
ANISOU 3174  CD2 LEU A 383     6838  13258   9696    364     68   2958       C  
ATOM   3175  N   ILE A 384     -15.023   6.828  50.482  1.00 80.87           N  
ANISOU 3175  N   ILE A 384     7822  14135   8770    799   -183   2394       N  
ATOM   3176  CA  ILE A 384     -14.929   7.884  51.475  1.00 77.80           C  
ANISOU 3176  CA  ILE A 384     7470  14024   8068    967   -215   2411       C  
ATOM   3177  C   ILE A 384     -16.064   8.902  51.363  1.00 72.36           C  
ANISOU 3177  C   ILE A 384     6835  13517   7140   1043   -268   2305       C  
ATOM   3178  O   ILE A 384     -16.627   9.309  52.383  1.00 72.28           O  
ANISOU 3178  O   ILE A 384     6742  13787   6936   1174   -274   2429       O  
ATOM   3179  CB  ILE A 384     -13.554   8.592  51.428  1.00 86.31           C  
ANISOU 3179  CB  ILE A 384     8712  15041   9040   1005   -247   2248       C  
ATOM   3180  CG1 ILE A 384     -12.470   7.698  52.045  1.00 89.02           C  
ANISOU 3180  CG1 ILE A 384     8963  15328   9533    993   -191   2416       C  
ATOM   3181  CG2 ILE A 384     -13.612   9.918  52.163  1.00 90.13           C  
ANISOU 3181  CG2 ILE A 384     9263  15784   9197   1168   -299   2168       C  
ATOM   3182  CD1 ILE A 384     -11.183   8.428  52.381  1.00 86.16           C  
ANISOU 3182  CD1 ILE A 384     8714  14998   9024   1066   -220   2297       C  
ATOM   3183  N   ARG A 385     -16.407   9.310  50.141  1.00 64.23           N  
ANISOU 3183  N   ARG A 385     5939  12348   6117    975   -304   2082       N  
ATOM   3184  CA  ARG A 385     -17.503  10.261  49.959  1.00 70.43           C  
ANISOU 3184  CA  ARG A 385     6780  13301   6679   1051   -348   1981       C  
ATOM   3185  C   ARG A 385     -18.841   9.772  50.552  1.00 76.67           C  
ANISOU 3185  C   ARG A 385     7377  14284   7471   1073   -325   2182       C  
ATOM   3186  O   ARG A 385     -19.783  10.554  50.703  1.00 76.32           O  
ANISOU 3186  O   ARG A 385     7350  14440   7208   1164   -359   2147       O  
ATOM   3187  CB  ARG A 385     -17.659  10.683  48.489  1.00 70.83           C  
ANISOU 3187  CB  ARG A 385     6989  13178   6745    985   -378   1724       C  
ATOM   3188  CG  ARG A 385     -17.190  12.109  48.170  1.00 66.80           C  
ANISOU 3188  CG  ARG A 385     6693  12685   6002   1079   -419   1511       C  
ATOM   3189  CD  ARG A 385     -15.815  12.167  47.519  1.00 83.18           C  
ANISOU 3189  CD  ARG A 385     8905  14520   8180   1021   -416   1373       C  
ATOM   3190  NE  ARG A 385     -15.808  13.144  46.419  1.00105.35           N  
ANISOU 3190  NE  ARG A 385    11898  17245  10885   1045   -437   1142       N  
ATOM   3191  CZ  ARG A 385     -14.844  13.281  45.505  1.00109.74           C  
ANISOU 3191  CZ  ARG A 385    12586  17586  11525    996   -433    994       C  
ATOM   3192  NH1 ARG A 385     -13.762  12.508  45.539  1.00109.66           N  
ANISOU 3192  NH1 ARG A 385    12552  17413  11702    912   -415   1037       N  
ATOM   3193  NH2 ARG A 385     -14.966  14.202  44.548  1.00106.63           N  
ANISOU 3193  NH2 ARG A 385    12343  17146  11025   1040   -440    813       N  
ATOM   3194  N   LYS A 386     -18.921   8.490  50.900  1.00 80.31           N  
ANISOU 3194  N   LYS A 386     7649  14682   8184    993   -263   2401       N  
ATOM   3195  CA  LYS A 386     -20.052   7.990  51.682  1.00 89.35           C  
ANISOU 3195  CA  LYS A 386     8584  16022   9342   1027   -226   2642       C  
ATOM   3196  C   LYS A 386     -19.760   8.175  53.182  1.00 96.75           C  
ANISOU 3196  C   LYS A 386     9425  17224  10110   1186   -206   2863       C  
ATOM   3197  O   LYS A 386     -19.524   7.207  53.911  1.00 95.16           O  
ANISOU 3197  O   LYS A 386     9049  17032  10075   1181   -133   3120       O  
ATOM   3198  CB  LYS A 386     -20.336   6.517  51.359  1.00 89.79           C  
ANISOU 3198  CB  LYS A 386     8461  15880   9777    870   -156   2784       C  
ATOM   3199  CG  LYS A 386     -19.976   6.095  49.924  1.00 88.16           C  
ANISOU 3199  CG  LYS A 386     8347  15349   9799    707   -170   2554       C  
ATOM   3200  CD  LYS A 386     -20.904   6.705  48.856  1.00 80.17           C  
ANISOU 3200  CD  LYS A 386     7425  14349   8687    684   -230   2312       C  
ATOM   3201  CE  LYS A 386     -20.326   6.568  47.437  1.00 67.68           C  
ANISOU 3201  CE  LYS A 386     5973  12492   7249    572   -258   2047       C  
ATOM   3202  NZ  LYS A 386     -20.086   5.161  46.954  1.00 57.30           N  
ANISOU 3202  NZ  LYS A 386     4526  10914   6332    410   -212   2083       N  
ATOM   3203  N   GLY A 387     -19.759   9.432  53.626  1.00 99.87           N  
ANISOU 3203  N   GLY A 387     9930  17839  10178   1337   -268   2756       N  
ATOM   3204  CA  GLY A 387     -19.459   9.769  55.008  1.00 98.55           C  
ANISOU 3204  CA  GLY A 387     9680  17954   9809   1512   -267   2910       C  
ATOM   3205  C   GLY A 387     -18.650  11.049  55.167  1.00 99.16           C  
ANISOU 3205  C   GLY A 387     9939  18106   9633   1623   -337   2687       C  
ATOM   3206  O   GLY A 387     -18.576  11.602  56.268  1.00100.90           O  
ANISOU 3206  O   GLY A 387    10103  18607   9627   1793   -359   2749       O  
ATOM   3207  N   ILE A 388     -18.056  11.527  54.072  1.00 92.36           N  
ANISOU 3207  N   ILE A 388     9280  16997   8814   1534   -369   2423       N  
ATOM   3208  CA  ILE A 388     -17.112  12.647  54.117  1.00 86.40           C  
ANISOU 3208  CA  ILE A 388     8695  16244   7888   1611   -420   2205       C  
ATOM   3209  C   ILE A 388     -16.894  13.308  52.769  1.00 99.50           C  
ANISOU 3209  C   ILE A 388    10574  17659   9572   1526   -449   1928       C  
ATOM   3210  O   ILE A 388     -16.555  12.643  51.785  1.00 96.84           O  
ANISOU 3210  O   ILE A 388    10280  17055   9459   1379   -423   1883       O  
ATOM   3211  CB  ILE A 388     -15.711  12.178  54.468  1.00 75.06           C  
ANISOU 3211  CB  ILE A 388     7244  14710   6564   1590   -394   2242       C  
ATOM   3212  CG1 ILE A 388     -15.595  11.752  55.934  1.00 69.33           C  
ANISOU 3212  CG1 ILE A 388     6317  14264   5762   1723   -366   2491       C  
ATOM   3213  CG2 ILE A 388     -14.711  13.276  54.134  1.00 69.99           C  
ANISOU 3213  CG2 ILE A 388     6799  13978   5817   1616   -443   1970       C  
ATOM   3214  CD1 ILE A 388     -14.275  11.071  56.203  1.00 56.07           C  
ANISOU 3214  CD1 ILE A 388     4600  12478   4225   1691   -326   2558       C  
ATOM   3215  N   THR A 389     -17.003  14.629  52.734  1.00111.10           N  
ANISOU 3215  N   THR A 389    12180  19218  10816   1628   -499   1742       N  
ATOM   3216  CA  THR A 389     -16.846  15.351  51.474  1.00113.49           C  
ANISOU 3216  CA  THR A 389    12687  19309  11125   1573   -513   1498       C  
ATOM   3217  C   THR A 389     -15.389  15.638  51.097  1.00117.57           C  
ANISOU 3217  C   THR A 389    13335  19612  11724   1530   -511   1346       C  
ATOM   3218  O   THR A 389     -14.458  15.164  51.752  1.00122.01           O  
ANISOU 3218  O   THR A 389    13830  20173  12356   1524   -500   1425       O  
ATOM   3219  CB  THR A 389     -17.648  16.664  51.475  1.00108.46           C  
ANISOU 3219  CB  THR A 389    12108  18776  10325   1687   -495   1333       C  
ATOM   3220  OG1 THR A 389     -17.467  17.332  50.223  1.00 94.91           O  
ANISOU 3220  OG1 THR A 389    10573  16843   8646   1645   -487   1118       O  
ATOM   3221  CG2 THR A 389     -17.197  17.572  52.625  1.00114.08           C  
ANISOU 3221  CG2 THR A 389    12786  19644  10914   1832   -486   1265       C  
ATOM   3222  N   SER A 390     -15.218  16.420  50.033  1.00116.29           N  
ANISOU 3222  N   SER A 390    13355  19281  11549   1507   -517   1137       N  
ATOM   3223  CA  SER A 390     -13.909  16.758  49.473  1.00114.24           C  
ANISOU 3223  CA  SER A 390    13233  18796  11377   1459   -509    983       C  
ATOM   3224  C   SER A 390     -12.916  17.324  50.496  1.00107.96           C  
ANISOU 3224  C   SER A 390    12432  18085  10502   1542   -526    941       C  
ATOM   3225  O   SER A 390     -13.295  17.705  51.605  1.00105.02           O  
ANISOU 3225  O   SER A 390    11951  17939  10012   1658   -525    977       O  
ATOM   3226  CB  SER A 390     -14.084  17.734  48.299  1.00117.11           C  
ANISOU 3226  CB  SER A 390    13774  19015  11709   1467   -495    779       C  
ATOM   3227  OG  SER A 390     -14.925  18.819  48.653  1.00118.91           O  
ANISOU 3227  OG  SER A 390    13995  19373  11814   1592   -473    700       O  
ATOM   3228  N   GLY A 391     -11.642  17.367  50.120  1.00105.09           N  
ANISOU 3228  N   GLY A 391    12155  17526  10250   1481   -516    841       N  
ATOM   3229  CA  GLY A 391     -11.188  16.881  48.827  1.00100.89           C  
ANISOU 3229  CA  GLY A 391    11715  16713   9907   1350   -485    787       C  
ATOM   3230  C   GLY A 391      -9.695  16.625  48.851  1.00100.99           C  
ANISOU 3230  C   GLY A 391    11756  16571  10046   1291   -473    748       C  
ATOM   3231  O   GLY A 391      -9.214  15.572  48.425  1.00 97.61           O  
ANISOU 3231  O   GLY A 391    11293  15994   9801   1183   -449    822       O  
ATOM   3232  N   LYS A 392      -8.957  17.594  49.337  1.00103.20           N  
ANISOU 3232  N   LYS A 392    12093  16885  10232   1365   -490    619       N  
ATOM   3233  CA  LYS A 392      -7.573  17.425  49.667  1.00102.65           C  
ANISOU 3233  CA  LYS A 392    12021  16733  10250   1331   -485    585       C  
ATOM   3234  C   LYS A 392      -7.593  16.499  50.863  1.00 97.19           C  
ANISOU 3234  C   LYS A 392    11139  16258   9530   1372   -493    775       C  
ATOM   3235  O   LYS A 392      -6.691  15.717  51.093  1.00 91.76           O  
ANISOU 3235  O   LYS A 392    10394  15528   8943   1330   -478    838       O  
ATOM   3236  CB  LYS A 392      -6.963  18.773  50.038  1.00107.47           C  
ANISOU 3236  CB  LYS A 392    12723  17345  10767   1407   -503    380       C  
ATOM   3237  CG  LYS A 392      -5.456  18.796  50.106  1.00107.20           C  
ANISOU 3237  CG  LYS A 392    12787  17075  10870   1331   -481    255       C  
ATOM   3238  CD  LYS A 392      -4.960  19.855  51.105  1.00106.55           C  
ANISOU 3238  CD  LYS A 392    12883  16775  10827   1310   -450     99       C  
ATOM   3239  CE  LYS A 392      -4.795  21.202  50.453  1.00103.54           C  
ANISOU 3239  CE  LYS A 392    12547  16284  10511   1245   -424    172       C  
ATOM   3240  NZ  LYS A 392      -5.342  22.261  51.320  1.00 98.64           N  
ANISOU 3240  NZ  LYS A 392    12088  15464   9926   1241   -384     38       N  
ATOM   3241  N   ILE A 393      -8.647  16.641  51.644  1.00 93.28           N  
ANISOU 3241  N   ILE A 393    10543  16006   8893   1465   -512    876       N  
ATOM   3242  CA  ILE A 393      -8.782  16.000  52.947  1.00 92.69           C  
ANISOU 3242  CA  ILE A 393    10274  16191   8752   1545   -515   1070       C  
ATOM   3243  C   ILE A 393      -8.962  14.488  52.835  1.00 88.70           C  
ANISOU 3243  C   ILE A 393     9651  15624   8428   1451   -466   1308       C  
ATOM   3244  O   ILE A 393      -8.476  13.730  53.674  1.00 81.73           O  
ANISOU 3244  O   ILE A 393     8627  14848   7578   1479   -443   1469       O  
ATOM   3245  CB  ILE A 393      -9.964  16.599  53.745  1.00 92.46           C  
ANISOU 3245  CB  ILE A 393    10171  16455   8505   1687   -549   1108       C  
ATOM   3246  CG1 ILE A 393      -9.889  18.131  53.761  1.00 99.26           C  
ANISOU 3246  CG1 ILE A 393    11151  17341   9223   1776   -585    853       C  
ATOM   3247  CG2 ILE A 393      -9.989  16.047  55.162  1.00 78.69           C  
ANISOU 3247  CG2 ILE A 393     8217  15012   6668   1801   -551   1304       C  
ATOM   3248  CD1 ILE A 393     -10.314  18.804  52.458  1.00 99.44           C  
ANISOU 3248  CD1 ILE A 393    11352  17133   9297   1712   -567    701       C  
ATOM   3249  N   ILE A 394      -9.672  14.053  51.801  1.00 92.14           N  
ANISOU 3249  N   ILE A 394    10132  15891   8985   1346   -447   1325       N  
ATOM   3250  CA  ILE A 394      -9.837  12.628  51.546  1.00 89.94           C  
ANISOU 3250  CA  ILE A 394     9746  15506   8923   1238   -400   1516       C  
ATOM   3251  C   ILE A 394      -8.502  12.029  51.106  1.00 84.37           C  
ANISOU 3251  C   ILE A 394     9084  14572   8400   1141   -375   1488       C  
ATOM   3252  O   ILE A 394      -8.079  10.998  51.620  1.00 81.77           O  
ANISOU 3252  O   ILE A 394     8628  14249   8191   1119   -334   1668       O  
ATOM   3253  CB  ILE A 394     -10.937  12.356  50.490  1.00 90.35           C  
ANISOU 3253  CB  ILE A 394     9828  15440   9062   1152   -394   1499       C  
ATOM   3254  CG1 ILE A 394     -10.663  13.145  49.212  1.00 89.39           C  
ANISOU 3254  CG1 ILE A 394     9910  15115   8941   1105   -414   1252       C  
ATOM   3255  CG2 ILE A 394     -12.315  12.716  51.033  1.00 86.71           C  
ANISOU 3255  CG2 ILE A 394     9288  15224   8435   1245   -411   1576       C  
ATOM   3256  CD1 ILE A 394     -11.890  13.363  48.368  1.00 92.00           C  
ANISOU 3256  CD1 ILE A 394    10279  15436   9242   1089   -423   1193       C  
ATOM   3257  N   GLY A 395      -7.837  12.689  50.161  1.00 81.47           N  
ANISOU 3257  N   GLY A 395     8894  14010   8052   1092   -392   1271       N  
ATOM   3258  CA  GLY A 395      -6.521  12.265  49.726  1.00 74.97           C  
ANISOU 3258  CA  GLY A 395     8125  12981   7378   1010   -374   1224       C  
ATOM   3259  C   GLY A 395      -5.596  12.156  50.918  1.00 75.13           C  
ANISOU 3259  C   GLY A 395     8053  13153   7341   1084   -369   1301       C  
ATOM   3260  O   GLY A 395      -4.885  11.163  51.085  1.00 70.35           O  
ANISOU 3260  O   GLY A 395     7374  12480   6877   1035   -333   1424       O  
ATOM   3261  N   GLU A 396      -5.603  13.192  51.750  1.00 81.78           N  
ANISOU 3261  N   GLU A 396     8893  14208   7973   1211   -405   1220       N  
ATOM   3262  CA  GLU A 396      -4.859  13.165  52.999  1.00 92.28           C  
ANISOU 3262  CA  GLU A 396    10107  15748   9208   1313   -408   1280       C  
ATOM   3263  C   GLU A 396      -5.184  11.864  53.717  1.00 92.61           C  
ANISOU 3263  C   GLU A 396     9955  15911   9322   1329   -359   1575       C  
ATOM   3264  O   GLU A 396      -4.290  11.094  54.061  1.00 95.07           O  
ANISOU 3264  O   GLU A 396    10194  16205   9724   1317   -323   1680       O  
ATOM   3265  CB  GLU A 396      -5.227  14.363  53.886  1.00103.00           C  
ANISOU 3265  CB  GLU A 396    11444  17371  10319   1468   -460   1172       C  
ATOM   3266  CG  GLU A 396      -4.647  15.707  53.432  1.00111.29           C  
ANISOU 3266  CG  GLU A 396    12660  18316  11311   1473   -498    879       C  
ATOM   3267  CD  GLU A 396      -5.174  16.899  54.240  1.00117.79           C  
ANISOU 3267  CD  GLU A 396    13461  19383  11909   1624   -550    759       C  
ATOM   3268  OE1 GLU A 396      -6.059  16.707  55.105  1.00116.63           O  
ANISOU 3268  OE1 GLU A 396    13179  19503  11631   1729   -562    902       O  
ATOM   3269  OE2 GLU A 396      -4.701  18.035  54.004  1.00120.65           O  
ANISOU 3269  OE2 GLU A 396    13938  19669  12236   1640   -575    520       O  
ATOM   3270  N   VAL A 397      -6.475  11.618  53.920  1.00 88.01           N  
ANISOU 3270  N   VAL A 397     9286  15446   8708   1357   -351   1715       N  
ATOM   3271  CA  VAL A 397      -6.939  10.403  54.583  1.00 77.59           C  
ANISOU 3271  CA  VAL A 397     7769  14235   7477   1374   -291   2017       C  
ATOM   3272  C   VAL A 397      -6.402   9.126  53.945  1.00 66.36           C  
ANISOU 3272  C   VAL A 397     6329  12547   6337   1232   -230   2129       C  
ATOM   3273  O   VAL A 397      -5.870   8.273  54.635  1.00 62.30           O  
ANISOU 3273  O   VAL A 397     5681  12095   5894   1264   -175   2325       O  
ATOM   3274  CB  VAL A 397      -8.470  10.320  54.599  1.00 83.76           C  
ANISOU 3274  CB  VAL A 397     8481  15117   8228   1389   -289   2127       C  
ATOM   3275  CG1 VAL A 397      -8.917   8.979  55.167  1.00 87.12           C  
ANISOU 3275  CG1 VAL A 397     8697  15603   8800   1385   -211   2453       C  
ATOM   3276  CG2 VAL A 397      -9.046  11.461  55.408  1.00 86.91           C  
ANISOU 3276  CG2 VAL A 397     8866  15817   8339   1551   -345   2057       C  
ATOM   3277  N   LEU A 398      -6.547   9.000  52.629  1.00 68.23           N  
ANISOU 3277  N   LEU A 398     6694  12499   6733   1087   -237   2004       N  
ATOM   3278  CA  LEU A 398      -6.122   7.794  51.922  1.00 63.88           C  
ANISOU 3278  CA  LEU A 398     6126  11684   6463    950   -187   2083       C  
ATOM   3279  C   LEU A 398      -4.645   7.502  52.128  1.00 64.99           C  
ANISOU 3279  C   LEU A 398     6284  11757   6653    947   -167   2079       C  
ATOM   3280  O   LEU A 398      -4.244   6.351  52.298  1.00 62.14           O  
ANISOU 3280  O   LEU A 398     5820  11316   6475    907   -105   2260       O  
ATOM   3281  CB  LEU A 398      -6.428   7.889  50.425  1.00 58.47           C  
ANISOU 3281  CB  LEU A 398     5584  10732   5899    819   -214   1895       C  
ATOM   3282  CG  LEU A 398      -7.825   7.507  49.927  1.00 66.62           C  
ANISOU 3282  CG  LEU A 398     6559  11734   7018    763   -209   1942       C  
ATOM   3283  CD1 LEU A 398      -8.557   6.668  50.965  1.00 69.78           C  
ANISOU 3283  CD1 LEU A 398     6741  12301   7470    807   -153   2231       C  
ATOM   3284  CD2 LEU A 398      -8.628   8.742  49.567  1.00 74.21           C  
ANISOU 3284  CD2 LEU A 398     7632  12791   7772    815   -266   1765       C  
ATOM   3285  N   GLU A 399      -3.829   8.546  52.117  1.00 71.41           N  
ANISOU 3285  N   GLU A 399     7221  12599   7312    991   -216   1873       N  
ATOM   3286  CA  GLU A 399      -2.402   8.349  52.296  1.00 80.29           C  
ANISOU 3286  CA  GLU A 399     8363  13672   8470    990   -203   1847       C  
ATOM   3287  C   GLU A 399      -2.042   8.031  53.744  1.00 79.71           C  
ANISOU 3287  C   GLU A 399     8115  13881   8290   1128   -170   2036       C  
ATOM   3288  O   GLU A 399      -1.105   7.282  53.995  1.00 82.94           O  
ANISOU 3288  O   GLU A 399     8467  14255   8790   1123   -125   2139       O  
ATOM   3289  CB  GLU A 399      -1.605   9.548  51.785  1.00 90.56           C  
ANISOU 3289  CB  GLU A 399     9843  14898   9669    984   -259   1562       C  
ATOM   3290  CG  GLU A 399      -0.138   9.226  51.567  1.00 98.72           C  
ANISOU 3290  CG  GLU A 399    10922  15794  10795    936   -243   1512       C  
ATOM   3291  CD  GLU A 399       0.539  10.214  50.650  1.00106.66           C  
ANISOU 3291  CD  GLU A 399    12116  16627  11784    883   -283   1243       C  
ATOM   3292  OE1 GLU A 399       0.352  11.431  50.860  1.00107.14           O  
ANISOU 3292  OE1 GLU A 399    12235  16792  11681    951   -325   1085       O  
ATOM   3293  OE2 GLU A 399       1.256   9.774  49.722  1.00111.49           O  
ANISOU 3293  OE2 GLU A 399    12812  16997  12552    779   -270   1195       O  
ATOM   3294  N   LYS A 400      -2.765   8.586  54.693  1.00 80.09           N  
ANISOU 3294  N   LYS A 400     8070  14225   8135   1265   -190   2086       N  
ATOM   3295  CA  LYS A 400      -2.555   8.232  56.082  1.00 84.52           C  
ANISOU 3295  CA  LYS A 400     8439  15098   8575   1424   -156   2284       C  
ATOM   3296  C   LYS A 400      -2.890   6.776  56.303  1.00 81.84           C  
ANISOU 3296  C   LYS A 400     7935  14735   8427   1404    -60   2615       C  
ATOM   3297  O   LYS A 400      -2.236   6.078  57.030  1.00 81.25           O  
ANISOU 3297  O   LYS A 400     7721  14796   8353   1491      0   2803       O  
ATOM   3298  CB  LYS A 400      -3.363   9.122  57.000  1.00 90.43           C  
ANISOU 3298  CB  LYS A 400     9116  16187   9056   1590   -204   2260       C  
ATOM   3299  CG  LYS A 400      -2.715  10.447  57.266  1.00 95.64           C  
ANISOU 3299  CG  LYS A 400     9844  16994   9502   1685   -279   1991       C  
ATOM   3300  CD  LYS A 400      -2.321  11.149  55.996  1.00 97.06           C  
ANISOU 3300  CD  LYS A 400    10256  16878   9745   1552   -328   1692       C  
ATOM   3301  CE  LYS A 400      -2.151  12.617  56.268  1.00 98.42           C  
ANISOU 3301  CE  LYS A 400    10491  17191   9713   1647   -403   1420       C  
ATOM   3302  NZ  LYS A 400      -1.821  13.407  55.069  1.00 95.70           N  
ANISOU 3302  NZ  LYS A 400    10365  16560   9437   1529   -435   1168       N  
ATOM   3303  N   ILE A 401      -3.926   6.313  55.667  1.00 76.95           N  
ANISOU 3303  N   ILE A 401     7321  13941   7976   1294    -39   2685       N  
ATOM   3304  CA  ILE A 401      -4.273   4.899  55.771  1.00 79.31           C  
ANISOU 3304  CA  ILE A 401     7466  14153   8517   1247     60   2981       C  
ATOM   3305  C   ILE A 401      -3.234   4.015  55.063  1.00 69.75           C  
ANISOU 3305  C   ILE A 401     6307  12643   7553   1122    102   2980       C  
ATOM   3306  O   ILE A 401      -2.735   3.057  55.650  1.00 65.53           O  
ANISOU 3306  O   ILE A 401     5637  12136   7125   1162    187   3214       O  
ATOM   3307  CB  ILE A 401      -5.762   4.595  55.380  1.00 80.51           C  
ANISOU 3307  CB  ILE A 401     7567  14245   8779   1179     72   3068       C  
ATOM   3308  CG1 ILE A 401      -5.930   3.166  54.875  1.00 78.72           C  
ANISOU 3308  CG1 ILE A 401     7251  13754   8905   1046    160   3252       C  
ATOM   3309  CG2 ILE A 401      -6.283   5.562  54.349  1.00 82.17           C  
ANISOU 3309  CG2 ILE A 401     7962  14335   8922   1098    -17   2777       C  
ATOM   3310  CD1 ILE A 401      -7.378   2.836  54.543  1.00 78.59           C  
ANISOU 3310  CD1 ILE A 401     7159  13690   9010    978    175   3330       C  
ATOM   3311  N   LEU A 402      -2.888   4.365  53.826  1.00 75.64           N  
ANISOU 3311  N   LEU A 402     7244  13120   8376    986     46   2723       N  
ATOM   3312  CA  LEU A 402      -1.753   3.759  53.124  1.00 76.17           C  
ANISOU 3312  CA  LEU A 402     7388  12928   8627    884     66   2667       C  
ATOM   3313  C   LEU A 402      -0.538   3.671  54.060  1.00 80.38           C  
ANISOU 3313  C   LEU A 402     7860  13625   9056    996     96   2749       C  
ATOM   3314  O   LEU A 402       0.111   2.625  54.178  1.00 73.59           O  
ANISOU 3314  O   LEU A 402     6924  12673   8365    977    170   2916       O  
ATOM   3315  CB  LEU A 402      -1.374   4.633  51.921  1.00 74.93           C  
ANISOU 3315  CB  LEU A 402     7455  12575   8439    790    -17   2341       C  
ATOM   3316  CG  LEU A 402      -0.993   4.096  50.525  1.00 72.65           C  
ANISOU 3316  CG  LEU A 402     7281  11936   8386    630    -22   2219       C  
ATOM   3317  CD1 LEU A 402      -0.171   5.146  49.748  1.00 67.45           C  
ANISOU 3317  CD1 LEU A 402     6825  11185   7618    604    -90   1930       C  
ATOM   3318  CD2 LEU A 402      -0.260   2.766  50.560  1.00 64.79           C  
ANISOU 3318  CD2 LEU A 402     6199  10793   7625    581     52   2391       C  
ATOM   3319  N   MET A 403      -0.191   4.817  54.635  1.00 81.42           N  
ANISOU 3319  N   MET A 403     8015  14010   8910   1119     40   2623       N  
ATOM   3320  CA  MET A 403       1.000   4.962  55.460  1.00 83.72           C  
ANISOU 3320  CA  MET A 403     8277  14461   9071   1221     44   2606       C  
ATOM   3321  C   MET A 403       1.007   4.195  56.782  1.00 92.03           C  
ANISOU 3321  C   MET A 403     9100  15793  10074   1378    127   2917       C  
ATOM   3322  O   MET A 403       1.946   3.468  57.078  1.00 93.37           O  
ANISOU 3322  O   MET A 403     9207  15981  10288   1416    183   3025       O  
ATOM   3323  CB  MET A 403       1.234   6.441  55.721  1.00 84.98           C  
ANISOU 3323  CB  MET A 403     8529  14789   8971   1297    -49   2333       C  
ATOM   3324  CG  MET A 403       2.608   6.931  55.322  1.00 91.15           C  
ANISOU 3324  CG  MET A 403     9409  15504   9720   1278    -78   2136       C  
ATOM   3325  SD  MET A 403       2.892   7.109  53.565  1.00 89.47           S  
ANISOU 3325  SD  MET A 403     9454  14908   9631   1092   -134   1837       S  
ATOM   3326  CE  MET A 403       2.531   5.507  52.940  1.00 40.11           C  
ANISOU 3326  CE  MET A 403     3216   8336   3687    935    -78   1997       C  
ATOM   3327  N   LYS A 404      -0.069   4.292  57.546  1.00 93.85           N  
ANISOU 3327  N   LYS A 404     9199  16257  10201   1483    141   3070       N  
ATOM   3328  CA  LYS A 404      -0.210   3.444  58.713  1.00 93.75           C  
ANISOU 3328  CA  LYS A 404     8953  16493  10176   1632    240   3414       C  
ATOM   3329  C   LYS A 404      -0.139   1.992  58.227  1.00 92.84           C  
ANISOU 3329  C   LYS A 404     8784  16092  10398   1515    348   3646       C  
ATOM   3330  O   LYS A 404       0.416   1.127  58.905  1.00 95.98           O  
ANISOU 3330  O   LYS A 404     9037  16578  10852   1603    445   3895       O  
ATOM   3331  CB  LYS A 404      -1.528   3.735  59.444  1.00 93.57           C  
ANISOU 3331  CB  LYS A 404     8802  16735  10015   1747    239   3549       C  
ATOM   3332  CG  LYS A 404      -1.596   5.102  60.152  1.00 93.57           C  
ANISOU 3332  CG  LYS A 404     8813  17071   9669   1903    140   3350       C  
ATOM   3333  CD  LYS A 404      -1.321   5.010  61.666  1.00 98.13           C  
ANISOU 3333  CD  LYS A 404     9168  18093  10025   2156    181   3545       C  
ATOM   3334  CE  LYS A 404       0.128   5.351  62.044  1.00 99.24           C  
ANISOU 3334  CE  LYS A 404     9323  18352  10031   2236    154   3389       C  
ATOM   3335  NZ  LYS A 404       1.101   4.229  61.840  1.00 98.27           N  
ANISOU 3335  NZ  LYS A 404     9174  18053  10110   2179    247   3549       N  
ATOM   3336  N   LYS A 405      -0.689   1.734  57.065  1.00 87.37           N  
ANISOU 3336  N   LYS A 405     8205  15058   9934   1323    331   3552       N  
ATOM   3337  CA  LYS A 405      -0.603   0.417  56.493  1.00 82.60           C  
ANISOU 3337  CA  LYS A 405     7549  14156   9680   1199    423   3733       C  
ATOM   3338  C   LYS A 405       0.790  -0.017  56.076  1.00 83.37           C  
ANISOU 3338  C   LYS A 405     7731  14044   9900   1131    440   3665       C  
ATOM   3339  O   LYS A 405       1.077  -1.177  56.129  1.00 84.36           O  
ANISOU 3339  O   LYS A 405     7762  14020  10272   1098    541   3882       O  
ATOM   3340  CB  LYS A 405      -1.608   0.200  55.379  1.00 74.03           C  
ANISOU 3340  CB  LYS A 405     6533  12799   8797   1027    395   3638       C  
ATOM   3341  CG  LYS A 405      -1.525  -1.172  54.821  1.00 70.87           C  
ANISOU 3341  CG  LYS A 405     6052  12090   8785    897    489   3810       C  
ATOM   3342  CD  LYS A 405      -2.821  -1.604  54.222  1.00 75.52           C  
ANISOU 3342  CD  LYS A 405     6634  12502   9559    766    474   3768       C  
ATOM   3343  CE  LYS A 405      -3.192  -0.804  53.021  1.00 80.36           C  
ANISOU 3343  CE  LYS A 405     7463  12872  10199    619    366   3410       C  
ATOM   3344  NZ  LYS A 405      -3.718  -1.690  51.964  1.00 81.04           N  
ANISOU 3344  NZ  LYS A 405     7520  12662  10609    456    383   3383       N  
ATOM   3345  N   LEU A 406       1.629   0.885  55.587  1.00 83.48           N  
ANISOU 3345  N   LEU A 406     7918  14043   9756   1111    346   3370       N  
ATOM   3346  CA  LEU A 406       2.941   0.458  55.084  1.00 87.26           C  
ANISOU 3346  CA  LEU A 406     8480  14360  10313   1061    354   3292       C  
ATOM   3347  C   LEU A 406       3.835  -0.168  56.153  1.00 86.17           C  
ANISOU 3347  C   LEU A 406     8185  14458  10099   1221    440   3526       C  
ATOM   3348  O   LEU A 406       4.483  -1.162  55.924  1.00 77.25           O  
ANISOU 3348  O   LEU A 406     7063  13198   9092   1194    488   3578       O  
ATOM   3349  CB  LEU A 406       3.686   1.633  54.467  1.00 87.17           C  
ANISOU 3349  CB  LEU A 406     8668  14324  10128   1026    241   2939       C  
ATOM   3350  CG  LEU A 406       3.625   1.858  52.977  1.00 90.20           C  
ANISOU 3350  CG  LEU A 406     9247  14363  10660    845    180   2696       C  
ATOM   3351  CD1 LEU A 406       4.637   2.844  52.668  1.00 90.57           C  
ANISOU 3351  CD1 LEU A 406     9459  14442  10513    848     88   2392       C  
ATOM   3352  CD2 LEU A 406       3.899   0.618  52.263  1.00 89.83           C  
ANISOU 3352  CD2 LEU A 406     9211  14034  10885    741    235   2770       C  
ATOM   3353  N   ASP A 407       3.806   0.440  57.320  1.00 88.57           N  
ANISOU 3353  N   ASP A 407     8340  15129  10185   1402    457   3664       N  
ATOM   3354  CA  ASP A 407       4.360  -0.018  58.565  1.00 93.31           C  
ANISOU 3354  CA  ASP A 407     8772  16019  10662   1590    536   3880       C  
ATOM   3355  C   ASP A 407       3.535  -1.259  58.757  1.00 94.47           C  
ANISOU 3355  C   ASP A 407     8706  16189  11000   1652    685   4298       C  
ATOM   3356  O   ASP A 407       3.963  -2.308  59.201  1.00 89.48           O  
ANISOU 3356  O   ASP A 407     7973  15569  10457   1718    789   4515       O  
ATOM   3357  CB  ASP A 407       4.101   1.066  59.569  1.00 95.34           C  
ANISOU 3357  CB  ASP A 407     8977  16697  10551   1776    465   3766       C  
ATOM   3358  CG  ASP A 407       4.450   2.407  59.003  1.00 90.70           C  
ANISOU 3358  CG  ASP A 407     8596  16048   9818   1701    327   3350       C  
ATOM   3359  OD1 ASP A 407       4.038   3.451  59.506  1.00 84.33           O  
ANISOU 3359  OD1 ASP A 407     7811  15418   8811   1757    244   3188       O  
ATOM   3360  OD2 ASP A 407       5.178   2.404  58.018  1.00 88.90           O  
ANISOU 3360  OD2 ASP A 407     8505  15586   9688   1587    306   3192       O  
ATOM   3361  N   GLY A 408       2.288  -1.168  58.332  1.00101.44           N  
ANISOU 3361  N   GLY A 408     9521  17064  11958   1628    701   4412       N  
ATOM   3362  CA  GLY A 408       1.421  -2.327  58.222  1.00100.73           C  
ANISOU 3362  CA  GLY A 408     9223  16972  12079   1673    846   4808       C  
ATOM   3363  C   GLY A 408       0.444  -2.609  59.327  1.00103.76           C  
ANISOU 3363  C   GLY A 408     9554  17390  12480   1646    829   4856       C  
ATOM   3364  O   GLY A 408       0.803  -2.623  60.479  1.00 99.61           O  
ANISOU 3364  O   GLY A 408     9033  17147  11667   1748    747   4745       O  
ATOM   3365  N   ASP A 409      -0.817  -2.729  58.933  1.00111.59           N  
ANISOU 3365  N   ASP A 409    10490  18095  13815   1510    905   5013       N  
ATOM   3366  CA  ASP A 409      -1.893  -3.286  59.710  1.00117.68           C  
ANISOU 3366  CA  ASP A 409    11216  18857  14639   1456    887   5039       C  
ATOM   3367  C   ASP A 409      -2.605  -4.115  58.689  1.00128.00           C  
ANISOU 3367  C   ASP A 409    12259  20447  15928   1629   1009   5441       C  
ATOM   3368  O   ASP A 409      -3.071  -3.605  57.696  1.00131.35           O  
ANISOU 3368  O   ASP A 409    12512  20872  16524   1703   1159   5776       O  
ATOM   3369  CB  ASP A 409      -2.798  -2.188  60.221  1.00114.08           C  
ANISOU 3369  CB  ASP A 409    10822  17952  14571   1215    898   4967       C  
ATOM   3370  CG  ASP A 409      -2.025  -1.019  60.752  1.00110.79           C  
ANISOU 3370  CG  ASP A 409    10185  17394  14515   1197   1066   5346       C  
ATOM   3371  OD1 ASP A 409      -0.777  -1.014  60.585  1.00109.80           O  
ANISOU 3371  OD1 ASP A 409    10035  17047  14637   1149   1152   5452       O  
ATOM   3372  OD2 ASP A 409      -2.650  -0.119  61.348  1.00103.53           O  
ANISOU 3372  OD2 ASP A 409     9112  16583  13640   1232   1118   5543       O  
ATOM   3373  N   THR A 410      -2.653  -5.398  58.951  1.00135.21           N  
ANISOU 3373  N   THR A 410    13137  21602  16634   1701    952   5418       N  
ATOM   3374  CA  THR A 410      -3.203  -6.371  58.036  1.00145.26           C  
ANISOU 3374  CA  THR A 410    14159  23131  17903   1852   1062   5795       C  
ATOM   3375  C   THR A 410      -4.728  -6.334  57.836  1.00149.50           C  
ANISOU 3375  C   THR A 410    14585  23339  18880   1695   1179   6017       C  
ATOM   3376  O   THR A 410      -5.234  -6.854  56.862  1.00150.01           O  
ANISOU 3376  O   THR A 410    14762  23112  19122   1490   1113   5807       O  
ATOM   3377  CB  THR A 410      -2.687  -7.777  58.389  1.00 88.04           C  
ANISOU 3377  CB  THR A 410     6910  16200  10341   1951    963   5695       C  
ATOM   3378  OG1 THR A 410      -3.434  -8.763  57.668  1.00 93.07           O  
ANISOU 3378  OG1 THR A 410     7512  17267  10585   2188    917   5665       O  
ATOM   3379  CG2 THR A 410      -2.820  -8.030  59.875  1.00 81.75           C  
ANISOU 3379  CG2 THR A 410     5892  15496   9673   1998   1068   6037       C  
ATOM   3380  N   ARG A 411      -5.477  -5.753  58.749  1.00 20.00           N  
ATOM   3381  CA  ARG A 411      -6.919  -5.798  58.537  1.00 20.00           C  
ATOM   3382  C   ARG A 411      -7.439  -4.522  57.877  1.00 20.00           C  
ATOM   3383  O   ARG A 411      -6.888  -4.089  56.887  1.00 20.00           O  
ATOM   3384  CB  ARG A 411      -7.681  -6.159  59.828  1.00 20.00           C  
ATOM   3385  CG  ARG A 411      -7.252  -7.491  60.486  1.00 20.00           C  
ATOM   3386  CD  ARG A 411      -8.090  -8.719  60.075  1.00 20.00           C  
ATOM   3387  NE  ARG A 411      -8.046  -9.777  61.101  1.00 20.00           N  
ATOM   3388  CZ  ARG A 411      -8.794 -10.886  61.102  1.00 20.00           C  
ATOM   3389  NH1 ARG A 411      -9.658 -11.121  60.124  1.00 20.00           N  
ATOM   3390  NH2 ARG A 411      -8.674 -11.768  62.081  1.00 20.00           N  
ATOM   3391  N   ASP A 412      -8.524  -3.933  58.367  1.00119.09           N  
ANISOU 3391  N   ASP A 412    11045  19084  15120   1260    892   5329       N  
ATOM   3392  CA  ASP A 412      -8.962  -2.702  57.691  1.00124.26           C  
ANISOU 3392  CA  ASP A 412    11945  19548  15720   1108    745   4908       C  
ATOM   3393  C   ASP A 412     -10.051  -1.906  58.354  1.00131.72           C  
ANISOU 3393  C   ASP A 412    12956  20758  16334   1183    635   4747       C  
ATOM   3394  O   ASP A 412     -10.504  -2.285  59.416  1.00133.46           O  
ANISOU 3394  O   ASP A 412    13308  21171  16231   1280    540   4550       O  
ATOM   3395  CB  ASP A 412      -9.425  -3.092  56.290  1.00121.91           C  
ANISOU 3395  CB  ASP A 412    11655  18841  15823    878    765   4831       C  
ATOM   3396  CG  ASP A 412      -9.541  -1.921  55.360  1.00116.27           C  
ANISOU 3396  CG  ASP A 412    11165  17976  15037    744    620   4419       C  
ATOM   3397  OD1 ASP A 412      -9.264  -0.785  55.765  1.00115.12           O  
ANISOU 3397  OD1 ASP A 412    11045  17507  15188    564    617   4295       O  
ATOM   3398  OD2 ASP A 412      -9.918  -2.151  54.209  1.00111.47           O  
ANISOU 3398  OD2 ASP A 412    10697  17573  14082    824    514   4218       O  
ATOM   3399  N   GLU A 413     -10.476  -0.826  57.689  1.00133.53           N  
ANISOU 3399  N   GLU A 413    13092  20986  16657   1133    648   4822       N  
ATOM   3400  CA  GLU A 413     -11.699  -0.118  58.040  1.00128.05           C  
ANISOU 3400  CA  GLU A 413    12437  20560  15656   1216    557   4711       C  
ATOM   3401  C   GLU A 413     -12.032   0.058  59.467  1.00123.89           C  
ANISOU 3401  C   GLU A 413    11802  20469  14800   1469    571   4893       C  
ATOM   3402  O   GLU A 413     -13.124   0.405  59.863  1.00119.60           O  
ANISOU 3402  O   GLU A 413    11315  20191  13936   1578    479   4764       O  
ATOM   3403  CB  GLU A 413     -12.897  -1.079  58.052  1.00130.80           C  
ANISOU 3403  CB  GLU A 413    12661  20851  16185   1130    590   4816       C  
ATOM   3404  CG  GLU A 413     -13.691  -1.206  56.747  1.00134.52           C  
ANISOU 3404  CG  GLU A 413    12931  21088  17093   1029    736   5103       C  
ATOM   3405  CD  GLU A 413     -13.375  -2.469  55.963  1.00131.83           C  
ANISOU 3405  CD  GLU A 413    12685  20312  17093    790    717   4880       C  
ATOM   3406  OE1 GLU A 413     -12.279  -3.026  56.104  1.00128.95           O  
ANISOU 3406  OE1 GLU A 413    12333  19711  16953    724    770   4904       O  
ATOM   3407  OE2 GLU A 413     -14.232  -2.915  55.187  1.00130.17           O  
ANISOU 3407  OE2 GLU A 413    12532  20011  16915    678    646   4674       O  
ATOM   3408  N   GLU A 414     -10.992  -0.211  60.271  1.00121.99           N  
ANISOU 3408  N   GLU A 414    11399  20309  14641   1571    687   5192       N  
ATOM   3409  CA  GLU A 414     -10.644   0.192  61.585  1.00118.92           C  
ANISOU 3409  CA  GLU A 414    10896  20350  13940   1829    704   5359       C  
ATOM   3410  C   GLU A 414      -9.614   1.238  61.347  1.00113.66           C  
ANISOU 3410  C   GLU A 414    10421  19779  12987   1890    586   5039       C  
ATOM   3411  O   GLU A 414      -9.574   2.227  62.068  1.00112.49           O  
ANISOU 3411  O   GLU A 414    10242  20002  12497   2088    532   5007       O  
ATOM   3412  CB  GLU A 414     -10.093  -1.003  62.306  1.00122.05           C  
ANISOU 3412  CB  GLU A 414    11069  20788  14515   1924    871   5761       C  
ATOM   3413  CG  GLU A 414     -10.502  -2.334  61.712  1.00123.68           C  
ANISOU 3413  CG  GLU A 414    11104  20759  15128   1805   1007   6054       C  
ATOM   3414  CD  GLU A 414     -10.398  -3.484  62.695  1.00125.59           C  
ANISOU 3414  CD  GLU A 414    11124  21037  15558   1914   1189   6473       C  
ATOM   3415  OE1 GLU A 414     -10.359  -3.215  63.903  1.00122.31           O  
ANISOU 3415  OE1 GLU A 414    10598  21003  14873   2159   1223   6649       O  
ATOM   3416  OE2 GLU A 414     -10.356  -4.651  62.257  1.00127.92           O  
ANISOU 3416  OE2 GLU A 414    11347  20985  16273   1762   1300   6623       O  
ATOM   3417  N   GLU A 415      -8.763   1.032  60.345  1.00110.42           N  
ANISOU 3417  N   GLU A 415    10196  19031  12727   1720    547   4798       N  
ATOM   3418  CA  GLU A 415      -7.746   2.030  60.102  1.00107.63           C  
ANISOU 3418  CA  GLU A 415    10044  18698  12153   1736    434   4461       C  
ATOM   3419  C   GLU A 415      -8.336   3.402  59.815  1.00 94.49           C  
ANISOU 3419  C   GLU A 415     8528  17142  10232   1746    299   4163       C  
ATOM   3420  O   GLU A 415      -7.818   4.416  60.263  1.00 86.79           O  
ANISOU 3420  O   GLU A 415     7623  16381   8971   1866    218   3977       O  
ATOM   3421  CB  GLU A 415      -6.790   1.541  59.010  1.00112.35           C  
ANISOU 3421  CB  GLU A 415    10803  18887  12996   1539    428   4285       C  
ATOM   3422  CG  GLU A 415      -5.525   2.331  58.917  1.00121.57           C  
ANISOU 3422  CG  GLU A 415    11869  19981  14341   1561    539   4506       C  
ATOM   3423  CD  GLU A 415      -4.429   1.596  58.175  1.00133.35           C  
ANISOU 3423  CD  GLU A 415    13428  21635  15603   1675    497   4373       C  
ATOM   3424  OE1 GLU A 415      -3.322   2.156  58.022  1.00134.52           O  
ANISOU 3424  OE1 GLU A 415    13432  21929  15749   1800    588   4608       O  
ATOM   3425  OE2 GLU A 415      -4.665   0.456  57.730  1.00138.18           O  
ANISOU 3425  OE2 GLU A 415    14229  22230  16042   1641    376   4033       O  
ATOM   3426  N   ILE A 416      -9.433   3.431  59.069  1.00 92.57           N  
ANISOU 3426  N   ILE A 416     8325  16749  10097   1624    278   4110       N  
ATOM   3427  CA  ILE A 416     -10.107   4.694  58.775  1.00 93.60           C  
ANISOU 3427  CA  ILE A 416     8589  16980   9993   1641    163   3852       C  
ATOM   3428  C   ILE A 416     -10.670   5.308  60.052  1.00102.51           C  
ANISOU 3428  C   ILE A 416     9582  18552  10814   1869    146   3973       C  
ATOM   3429  O   ILE A 416     -10.504   6.502  60.298  1.00106.93           O  
ANISOU 3429  O   ILE A 416    10239  19297  11091   1970     50   3749       O  
ATOM   3430  CB  ILE A 416     -11.229   4.539  57.720  1.00 84.20           C  
ANISOU 3430  CB  ILE A 416     7454  15561   8976   1474    148   3779       C  
ATOM   3431  CG1 ILE A 416     -11.398   5.831  56.922  1.00 72.48           C  
ANISOU 3431  CG1 ILE A 416     6197  14033   7310   1437     28   3417       C  
ATOM   3432  CG2 ILE A 416     -12.542   4.165  58.376  1.00 87.86           C  
ANISOU 3432  CG2 ILE A 416     7718  16223   9441   1541    201   4047       C  
ATOM   3433  CD1 ILE A 416     -12.040   6.953  57.697  1.00 70.64           C  
ANISOU 3433  CD1 ILE A 416     5952  14149   6740   1610    -37   3370       C  
ATOM   3434  N   LEU A 417     -11.388   4.496  60.795  1.00104.47           N  
ANISOU 3434  N   LEU A 417     9598  18970  11125   1955    243   4329       N  
ATOM   3435  CA  LEU A 417     -12.009   4.981  61.985  1.00113.11           C  
ANISOU 3435  CA  LEU A 417    10535  20513  11930   2192    237   4483       C  
ATOM   3436  C   LEU A 417     -10.869   5.406  62.878  1.00120.55           C  
ANISOU 3436  C   LEU A 417    11444  21707  12652   2373    221   4451       C  
ATOM   3437  O   LEU A 417     -10.921   6.428  63.556  1.00122.51           O  
ANISOU 3437  O   LEU A 417    11691  22278  12578   2547    139   4320       O  
ATOM   3438  CB  LEU A 417     -12.830   3.869  62.627  1.00117.78           C  
ANISOU 3438  CB  LEU A 417    10866  21212  12673   2245    367   4910       C  
ATOM   3439  CG  LEU A 417     -13.623   2.916  61.725  1.00115.25           C  
ANISOU 3439  CG  LEU A 417    10522  20584  12682   2040    422   5001       C  
ATOM   3440  CD1 LEU A 417     -14.182   1.755  62.520  1.00113.27           C  
ANISOU 3440  CD1 LEU A 417     9985  20446  12606   2111    572   5457       C  
ATOM   3441  CD2 LEU A 417     -14.749   3.611  60.957  1.00112.35           C  
ANISOU 3441  CD2 LEU A 417    10279  20222  12188   1981    317   4768       C  
ATOM   3442  N   GLU A 418      -9.818   4.605  62.852  1.00123.87           N  
ANISOU 3442  N   GLU A 418    11833  21976  13256   2331    300   4560       N  
ATOM   3443  CA  GLU A 418      -8.694   4.820  63.729  1.00122.84           C  
ANISOU 3443  CA  GLU A 418    11659  22057  12956   2488    299   4542       C  
ATOM   3444  C   GLU A 418      -8.021   6.132  63.481  1.00121.57           C  
ANISOU 3444  C   GLU A 418    11678  21983  12531   2526    155   4135       C  
ATOM   3445  O   GLU A 418      -7.615   6.804  64.419  1.00119.62           O  
ANISOU 3445  O   GLU A 418    11346  22100  12005   2737    115   4092       O  
ATOM   3446  CB  GLU A 418      -7.666   3.721  63.534  1.00118.63           C  
ANISOU 3446  CB  GLU A 418    11154  21219  12701   2362    381   4612       C  
ATOM   3447  CG  GLU A 418      -7.029   3.281  64.809  1.00117.02           C  
ANISOU 3447  CG  GLU A 418    10886  21224  12352   2519    398   4629       C  
ATOM   3448  CD  GLU A 418      -5.762   2.554  64.577  1.00122.72           C  
ANISOU 3448  CD  GLU A 418    11374  22039  13214   2622    560   5057       C  
ATOM   3449  OE1 GLU A 418      -4.803   3.232  64.186  1.00123.15           O  
ANISOU 3449  OE1 GLU A 418    11388  21801  13603   2477    662   5269       O  
ATOM   3450  OE2 GLU A 418      -5.716   1.330  64.787  1.00126.40           O  
ANISOU 3450  OE2 GLU A 418    11688  22873  13464   2854    590   5179       O  
ATOM   3451  N   GLU A 419      -7.867   6.497  62.222  1.00117.15           N  
ANISOU 3451  N   GLU A 419    11354  21089  12069   2327     81   3836       N  
ATOM   3452  CA  GLU A 419      -7.154   7.723  61.946  1.00117.34           C  
ANISOU 3452  CA  GLU A 419    11564  21099  11920   2326    -35   3449       C  
ATOM   3453  C   GLU A 419      -8.018   8.975  61.859  1.00105.73           C  
ANISOU 3453  C   GLU A 419    10215  19676  10281   2328   -137   3210       C  
ATOM   3454  O   GLU A 419      -7.516  10.084  61.906  1.00 97.72           O  
ANISOU 3454  O   GLU A 419     9344  18657   9127   2339   -228   2893       O  
ATOM   3455  CB  GLU A 419      -6.249   7.550  60.724  1.00127.84           C  
ANISOU 3455  CB  GLU A 419    13077  22028  13468   2126    -36   3272       C  
ATOM   3456  CG  GLU A 419      -5.273   6.345  60.791  1.00138.83           C  
ANISOU 3456  CG  GLU A 419    14370  23384  14996   2138     55   3462       C  
ATOM   3457  CD  GLU A 419      -4.335   6.339  62.004  1.00144.11           C  
ANISOU 3457  CD  GLU A 419    14934  24406  15416   2349     37   3435       C  
ATOM   3458  OE1 GLU A 419      -3.795   7.405  62.357  1.00146.89           O  
ANISOU 3458  OE1 GLU A 419    15388  24852  15571   2395    -66   3124       O  
ATOM   3459  OE2 GLU A 419      -4.136   5.254  62.594  1.00142.87           O  
ANISOU 3459  OE2 GLU A 419    14585  24432  15268   2472    130   3722       O  
ATOM   3460  N   VAL A 420      -9.322   8.801  61.764  1.00106.33           N  
ANISOU 3460  N   VAL A 420    10231  19791  10379   2319   -119   3360       N  
ATOM   3461  CA  VAL A 420     -10.217   9.955  61.759  1.00111.28           C  
ANISOU 3461  CA  VAL A 420    10930  20559  10791   2379   -210   3177       C  
ATOM   3462  C   VAL A 420     -10.363  10.402  63.206  1.00116.77           C  
ANISOU 3462  C   VAL A 420    11446  21736  11187   2647   -234   3264       C  
ATOM   3463  O   VAL A 420     -10.641  11.567  63.494  1.00116.76           O  
ANISOU 3463  O   VAL A 420    11496  21923  10944   2755   -328   3049       O  
ATOM   3464  CB  VAL A 420     -11.598   9.667  61.120  1.00107.59           C  
ANISOU 3464  CB  VAL A 420    10472  19968  10440   2271   -191   3274       C  
ATOM   3465  CG1 VAL A 420     -11.474   9.568  59.598  1.00100.51           C  
ANISOU 3465  CG1 VAL A 420     9782  18631   9778   2030   -199   3086       C  
ATOM   3466  CG2 VAL A 420     -12.227   8.413  61.715  1.00110.29           C  
ANISOU 3466  CG2 VAL A 420    10577  20412  10915   2305    -80   3680       C  
ATOM   3467  N   LEU A 421     -10.156   9.448  64.109  1.00120.12           N  
ANISOU 3467  N   LEU A 421    11650  22358  11631   2762   -145   3583       N  
ATOM   3468  CA  LEU A 421     -10.003   9.734  65.525  1.00122.46           C  
ANISOU 3468  CA  LEU A 421    11752  23134  11645   3038   -158   3676       C  
ATOM   3469  C   LEU A 421      -8.735  10.554  65.756  1.00122.33           C  
ANISOU 3469  C   LEU A 421    11811  23192  11477   3107   -236   3367       C  
ATOM   3470  O   LEU A 421      -8.743  11.513  66.525  1.00125.37           O  
ANISOU 3470  O   LEU A 421    12150  23877  11608   3273   -269   3176       O  
ATOM   3471  CB  LEU A 421      -9.953   8.433  66.326  1.00125.95           C  
ANISOU 3471  CB  LEU A 421    11943  23735  12176   3139    -23   4107       C  
ATOM   3472  CG  LEU A 421     -11.292   7.842  66.788  1.00127.76           C  
ANISOU 3472  CG  LEU A 421    11987  24133  12423   3210     50   4458       C  
ATOM   3473  CD1 LEU A 421     -12.348   7.864  65.681  1.00122.80           C  
ANISOU 3473  CD1 LEU A 421    11498  23186  11974   2992     34   4395       C  
ATOM   3474  CD2 LEU A 421     -11.094   6.429  67.337  1.00128.00           C  
ANISOU 3474  CD2 LEU A 421    11794  24203  12636   3261    210   4892       C  
ATOM   3475  N   ALA A 422      -7.648  10.179  65.085  1.00120.95           N  
ANISOU 3475  N   ALA A 422    11748  22713  11495   2956   -210   3278       N  
ATOM   3476  CA  ALA A 422      -6.414  10.960  65.141  1.00120.90           C  
ANISOU 3476  CA  ALA A 422    11831  22720  11385   2985   -283   2962       C  
ATOM   3477  C   ALA A 422      -6.656  12.399  64.674  1.00124.31           C  
ANISOU 3477  C   ALA A 422    12448  23089  11695   2952   -404   2578       C  
ATOM   3478  O   ALA A 422      -6.132  13.347  65.263  1.00126.20           O  
ANISOU 3478  O   ALA A 422    12673  23532  11747   3078   -459   2322       O  
ATOM   3479  CB  ALA A 422      -5.315  10.301  64.308  1.00113.60           C  
ANISOU 3479  CB  ALA A 422    11018  21429  10715   2798   -233   2934       C  
ATOM   3480  N   SER A 423      -7.460  12.550  63.623  1.00122.92           N  
ANISOU 3480  N   SER A 423    12434  22619  11651   2780   -413   2524       N  
ATOM   3481  CA  SER A 423      -7.767  13.864  63.057  1.00119.99           C  
ANISOU 3481  CA  SER A 423    12246  22138  11207   2734   -488   2179       C  
ATOM   3482  C   SER A 423      -8.462  14.786  64.052  1.00121.23           C  
ANISOU 3482  C   SER A 423    12294  22652  11114   2935   -496   2077       C  
ATOM   3483  O   SER A 423      -8.431  16.010  63.903  1.00120.58           O  
ANISOU 3483  O   SER A 423    12324  22545  10947   2954   -555   1755       O  
ATOM   3484  CB  SER A 423      -8.633  13.729  61.805  1.00114.93           C  
ANISOU 3484  CB  SER A 423    11765  21169  10733   2543   -486   2193       C  
ATOM   3485  OG  SER A 423      -9.305  14.947  61.541  1.00113.57           O  
ANISOU 3485  OG  SER A 423    11705  20987  10460   2556   -519   1937       O  
ATOM   3486  N   LEU A 424      -9.106  14.190  65.051  1.00121.20           N  
ANISOU 3486  N   LEU A 424    12068  22978  11003   3091   -436   2360       N  
ATOM   3487  CA  LEU A 424      -9.714  14.948  66.140  1.00119.89           C  
ANISOU 3487  CA  LEU A 424    11763  23210  10579   3315   -439   2294       C  
ATOM   3488  C   LEU A 424      -8.762  14.990  67.335  1.00118.99           C  
ANISOU 3488  C   LEU A 424    11473  23453  10285   3525   -444   2270       C  
ATOM   3489  O   LEU A 424      -7.543  15.138  67.170  1.00113.34           O  
ANISOU 3489  O   LEU A 424    10821  22635   9608   3487   -489   2096       O  
ATOM   3490  CB  LEU A 424     -11.071  14.350  66.547  1.00115.85           C  
ANISOU 3490  CB  LEU A 424    11101  22884  10031   3379   -366   2615       C  
ATOM   3491  CG  LEU A 424     -12.317  14.765  65.752  1.00108.57           C  
ANISOU 3491  CG  LEU A 424    10303  21783   9164   3266   -374   2558       C  
ATOM   3492  CD1 LEU A 424     -12.198  14.403  64.276  1.00108.51           C  
ANISOU 3492  CD1 LEU A 424    10509  21301   9420   2999   -392   2522       C  
ATOM   3493  CD2 LEU A 424     -13.571  14.147  66.352  1.00106.55           C  
ANISOU 3493  CD2 LEU A 424     9859  21776   8851   3359   -303   2889       C  
TER    3494      LEU A 424                                                      
HETATM 3495  O   HOH A 442      38.333  11.299  34.148  1.00 10.58           O  
HETATM 3496  O   HOH A 443      44.152  -4.995  18.242  1.00 20.82           O  
HETATM 3497  O   HOH A 444      35.379   2.475  14.088  1.00 48.10           O  
HETATM 3498  O   HOH A 445      42.737   1.894  13.403  1.00 29.61           O  
HETATM 3499  O   HOH A 446      40.837   5.712  10.240  1.00 36.49           O  
HETATM 3500  O   HOH A 447      39.049  -9.885  12.287  1.00 26.94           O  
HETATM 3501  O   HOH A 448      39.086  14.417  24.285  1.00 33.29           O  
HETATM 3502  O   HOH A 449      41.641   2.392  10.583  1.00 28.58           O  
HETATM 3503  O   HOH A 450      35.684  -0.308  12.697  1.00 34.24           O  
HETATM 3504  O   HOH A 451      46.335  10.438  18.757  1.00 31.88           O  
HETATM 3505  O   HOH A 452      44.214 -21.258  -2.923  1.00 34.61           O  
HETATM 3506  O   HOH A 453      49.889  -0.826  13.492  1.00 42.21           O  
HETATM 3507  O   HOH A 454      12.453  10.031  39.061  1.00 39.39           O  
HETATM 3508  O   HOH A 455      35.507  10.257  12.653  1.00 36.81           O  
HETATM 3509  O   HOH A 456      42.094   9.411   5.293  1.00 26.88           O  
HETATM 3510  O   HOH A 457      30.213  13.377  12.423  1.00 32.67           O  
HETATM 3511  O   HOH A 458      38.217  -7.826  31.423  1.00 30.52           O  
HETATM 3512  O   HOH A 459      29.344  18.525  39.734  1.00 49.40           O  
HETATM 3513  O   HOH A 460      38.045 -19.225  -7.133  1.00 35.30           O  
HETATM 3514  O   HOH A 461      32.841  15.832  25.048  1.00 34.28           O  
HETATM 3515  O   HOH A 462      30.189  14.870  10.121  1.00 39.25           O  
HETATM 3516  O   HOH A 463      43.182  11.746   5.839  1.00 43.80           O  
HETATM 3517  O   HOH A 464      44.115 -14.882  22.691  1.00 41.16           O  
HETATM 3518  O   HOH A 465      40.253   2.881   3.977  1.00 29.82           O  
HETATM 3519  O   HOH A 466      30.897   9.424   1.089  1.00 41.05           O  
HETATM 3520  O   HOH A 467      32.108  19.835  22.598  1.00 36.50           O  
HETATM 3521  O   HOH A 468      41.187  10.979  35.642  1.00 38.51           O  
HETATM 3522  O   HOH A 469      27.218  17.652  19.280  1.00 41.62           O  
HETATM 3523  O   HOH A 470      33.809  -5.838  15.572  1.00 49.33           O  
HETATM 3524  O   HOH A 471      31.472  -3.938   6.391  1.00 58.95           O  
HETATM 3525  O   HOH A 472      54.950  -5.345  18.426  1.00 52.23           O  
HETATM 3526  O   HOH A 473      33.945 -21.498  -2.106  1.00 38.78           O  
HETATM 3527  O   HOH A 474      29.296 -27.943   5.661  1.00 51.54           O  
HETATM 3528  O   HOH A 475      43.350 -24.453  10.390  1.00 55.25           O  
HETATM 3529  O   HOH A 476      29.440  14.951  39.633  1.00 38.23           O  
HETATM 3530  O   HOH A 477      43.999 -17.541  18.204  1.00 47.23           O  
HETATM 3531  O   HOH A 478      26.475  20.912  23.929  1.00 41.61           O  
HETATM 3532  O   HOH A 479      48.634 -13.588   9.919  1.00 48.62           O  
HETATM 3533  O   HOH A 480      43.977 -20.169  16.634  1.00 47.99           O  
HETATM 3534  O   HOH A 481      35.560  -5.207  11.862  1.00 26.64           O  
HETATM 3535  O   HOH A 482      50.138 -10.132   9.439  1.00 26.99           O  
HETATM 3536  O   HOH A 483      23.120   8.032  20.239  1.00 39.86           O  
HETATM 3537  O   HOH A 484      24.349  13.339  47.821  1.00 55.63           O  
HETATM 3538  O   HOH A 485      28.706  26.844  34.519  1.00 54.33           O  
HETATM 3539  O   HOH A 486      50.252   4.803  10.687  1.00 42.88           O  
HETATM 3540  O   HOH A 487      30.996   8.888   5.550  1.00 43.51           O  
HETATM 3541  O   HOH A 488      25.576  -4.390  50.628  1.00 62.76           O  
HETATM 3542  O   HOH A 489      38.966 -17.589  -9.033  1.00 39.67           O  
HETATM 3543  O   HOH A 490      31.765  15.609  40.046  1.00 50.88           O  
HETATM 3544  O   HOH A 491      43.483  15.159  29.818  1.00 43.73           O  
HETATM 3545  O   HOH A 492      29.941   8.144  -1.873  1.00 44.19           O  
HETATM 3546  O   HOH A 493      37.252  13.269  36.184  1.00 40.72           O  
HETATM 3547  O   HOH A 494      31.403 -12.537  19.889  1.00 41.23           O  
HETATM 3548  O   HOH A 495      22.357  10.740  21.465  1.00 41.78           O  
HETATM 3549  O   HOH A 496      26.762   5.886  16.002  1.00 41.68           O  
HETATM 3550  O   HOH A 497      49.814 -11.957  12.534  1.00 30.04           O  
HETATM 3551  O   HOH A 498      32.406  18.918  25.482  1.00 47.23           O  
HETATM 3552  O   HOH A 499      29.336   5.932  17.359  1.00 39.05           O  
HETATM 3553  O   HOH A 500      34.100 -23.970  -1.504  1.00 46.72           O  
HETATM 3554  O   HOH A 501      29.049  21.650  24.558  1.00 37.80           O  
HETATM 3555  O   HOH A 502      29.947  21.319  39.592  1.00 44.58           O  
HETATM 3556  O   HOH A 503      53.696  -3.113  24.440  1.00 55.30           O  
HETATM 3557  O   HOH A 504      51.830  -7.868   9.001  1.00 50.19           O  
HETATM 3558  O   HOH A 505      50.537  -6.309  14.804  1.00 31.81           O  
HETATM 3559  O   HOH A 506      53.667  -6.953  21.380  1.00 52.34           O  
HETATM 3560  O   HOH A 507      11.373  22.763  30.594  1.00 62.40           O  
HETATM 3561  O   HOH A 508      21.176  -7.333  56.098  1.00 78.04           O  
HETATM 3562  O   HOH A 509      22.299  -6.029  52.610  1.00 62.60           O  
HETATM 3563  O   HOH A 510      37.386 -26.546   3.077  1.00 30.00           O  
HETATM 3564  O   HOH A 511      45.340 -21.764  11.286  1.00 30.00           O  
HETATM 3565  O   HOH A 512      10.733 -19.751   7.826  1.00 30.00           O  
HETATM 3566  O   HOH A 513      31.759  13.462  14.246  1.00 30.00           O  
HETATM 3567  O   HOH A 514      43.897  -7.848   7.692  1.00 30.00           O  
HETATM 3568  O   HOH A 515      51.908 -13.202  11.623  1.00 30.00           O  
HETATM 3569  O   HOH A 516      46.559  -9.481  28.096  1.00 30.00           O  
HETATM 3570  O   HOH A 517      50.361   2.139  14.968  1.00 30.00           O  
HETATM 3571  O   HOH A 518      36.951  18.418  13.476  1.00 30.00           O  
HETATM 3572  O   HOH A 519      40.071  -0.977  34.990  1.00 30.00           O  
HETATM 3573  O   HOH A 520      44.490  15.012  34.702  1.00 30.00           O  
HETATM 3574  O   HOH A 521      29.325  13.778  42.681  1.00 30.00           O  
HETATM 3575  O   HOH A 522       1.249   3.553  46.694  1.00 30.00           O  
HETATM 3576  O   HOH A 523      -6.309   7.827  66.289  1.00 30.00           O  
HETATM 3577  O   HOH A 524      16.580  25.790  28.640  1.00 30.00           O  
MASTER      308    0    0   26   12    0    0    6 3576    1    0   34          
END                                                                             


A second structure was input as follows:


HEADER    TRANSFERASE                             16-APR-09   3H39              
TITLE     THE COMPLEX STRUCTURE OF CCA-ADDING ENZYME WITH ATP                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA NUCLEOTIDYL TRANSFERASE-RELATED PROTEIN;              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 437-863;                                      
COMPND   5 SYNONYM: TRNA NUCLEOTIDYLTRANSFERASE, TRNA ADENYL-/CYTIDYL-          
COMPND   6 TRANSFERASE, TRNA CCA-PYROPHOSPHORYLASE, TRNA-NT;                    
COMPND   7 EC: 2.7.7.25;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;                            
SOURCE   3 ORGANISM_TAXID: 2336;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-22B                                   
KEYWDS    TRANSFERASE/RNA, NUCLEOTIDE-BINDING, NUCLEOTIDYLTRANSFERASE, RNA-     
KEYWDS   2 BINDING, TRANSFERASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TOH,K.TOMITA                                                        
REVDAT   2   05-FEB-14 3H39    1       JRNL   VERSN                             
REVDAT   1   13-OCT-09 3H39    0                                                
JRNL        AUTH   Y.TOH,D.TAKESHITA,T.NUMATA,S.FUKAI,O.NUREKI,K.TOMITA         
JRNL        TITL   MECHANISM FOR THE DEFINITION OF ELONGATION AND TERMINATION   
JRNL        TITL 2 BY THE CLASS II CCA-ADDING ENZYME                            
JRNL        REF    EMBO J.                       V.  28  3353 2009              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   19745807                                                     
JRNL        DOI    10.1038/EMBOJ.2009.260                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.03                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.480                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40034                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2030                            
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 36.0378 -  6.8649    0.99     2897   156  0.1995 0.2217        
REMARK   3     2  6.8649 -  5.4550    0.99     2812   154  0.2198 0.2511        
REMARK   3     3  5.4550 -  4.7672    0.99     2808   156  0.1723 0.2108        
REMARK   3     4  4.7672 -  4.3321    0.99     2782   137  0.1558 0.2172        
REMARK   3     5  4.3321 -  4.0221    0.99     2777   140  0.1733 0.2134        
REMARK   3     6  4.0221 -  3.7852    0.99     2738   155  0.1912 0.2219        
REMARK   3     7  3.7852 -  3.5958    0.99     2747   165  0.2014 0.2517        
REMARK   3     8  3.5958 -  3.4394    0.99     2763   132  0.2102 0.2693        
REMARK   3     9  3.4394 -  3.3071    0.97     2679   141  0.2249 0.2568        
REMARK   3    10  3.3071 -  3.1931    0.96     2670   134  0.2410 0.3063        
REMARK   3    11  3.1931 -  3.0933    0.95     2667   140  0.2564 0.3356        
REMARK   3    12  3.0933 -  3.0049    0.94     2634   140  0.2560 0.3106        
REMARK   3    13  3.0049 -  2.9258    0.93     2551   143  0.2781 0.3378        
REMARK   3    14  2.9258 -  2.8545    0.89     2479   137  0.2928 0.3055        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.30                                          
REMARK   3   B_SOL              : 50.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.940            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.09200                                              
REMARK   3    B22 (A**2) : 6.94500                                              
REMARK   3    B33 (A**2) : -1.30700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.32900                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           7057                                  
REMARK   3   ANGLE     :  1.650           9496                                  
REMARK   3   CHIRALITY :  0.108           1055                                  
REMARK   3   PLANARITY :  0.006           1198                                  
REMARK   3   DIHEDRAL  : 21.847           2711                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3H39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052636.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40051                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200   FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51000                            
REMARK 200   FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3H37                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ETHYLENE GLYCOL, 0.05M TRIS-CL       
REMARK 280  PH8.4, 2MM ATP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       93.04250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.03500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       93.04250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.03500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   106                                                      
REMARK 465     TYR A   107                                                      
REMARK 465     TYR A   108                                                      
REMARK 465     GLU A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     PRO A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     LYS A   113                                                      
REMARK 465     LEU A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     THR A   426                                                      
REMARK 465     GLU A   427                                                      
REMARK 465     GLY A   428                                                      
REMARK 465     LYS A   429                                                      
REMARK 465     LEU A   430                                                      
REMARK 465     ALA A   431                                                      
REMARK 465     ALA A   432                                                      
REMARK 465     ALA A   433                                                      
REMARK 465     LEU A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
REMARK 465     GLU B   106                                                      
REMARK 465     TYR B   107                                                      
REMARK 465     TYR B   108                                                      
REMARK 465     GLU B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     PRO B   111                                                      
REMARK 465     ALA B   112                                                      
REMARK 465     LYS B   113                                                      
REMARK 465     LEU B   114                                                      
REMARK 465     PRO B   115                                                      
REMARK 465     ASP B   116                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     ALA B   433                                                      
REMARK 465     LEU B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 465     HIS B   440                                                      
REMARK 465     HIS B   441                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 104   CB  -  CA  -  C   ANGL. DEV. = -34.1 DEGREES          
REMARK 500    LEU B 105   C   -  N   -  CA  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    LYS B 392   CB  -  CA  -  C   ANGL. DEV. = -22.0 DEGREES          
REMARK 500    GLU B 425   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    LEU B 430   CB  -  CA  -  C   ANGL. DEV. =  19.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A  86      102.94    -24.31                                   
REMARK 500    GLU A 118      -42.16    154.75                                   
REMARK 500    GLU A 329       63.88     62.75                                   
REMARK 500    THR A 373       30.59    -98.86                                   
REMARK 500    LYS A 377     -131.88     49.05                                   
REMARK 500    GLU A 381      -10.93     71.60                                   
REMARK 500    THR A 410     -158.85   -119.79                                   
REMARK 500    ASP A 412      -76.41     16.96                                   
REMARK 500    GLU A 413       18.93   -140.75                                   
REMARK 500    ASN B  63       81.03    161.66                                   
REMARK 500    ALA B  64      -51.89    -26.88                                   
REMARK 500    ASP B 174       86.52   -151.64                                   
REMARK 500    GLU B 227     -177.43    -66.93                                   
REMARK 500    GLU B 329       79.76     81.65                                   
REMARK 500    ARG B 330       82.31    -69.68                                   
REMARK 500    LEU B 375       29.56     45.98                                   
REMARK 500    GLU B 381     -102.22     61.15                                   
REMARK 500    TYR B 382       -4.23    -56.35                                   
REMARK 500    THR B 389      145.23    134.64                                   
REMARK 500    LYS B 392       -8.59     57.74                                   
REMARK 500    THR B 410     -131.07   -128.98                                   
REMARK 500    ASP B 412       -4.65    109.45                                   
REMARK 500    THR B 426      136.03    147.33                                   
REMARK 500    GLU B 427      -78.96   -140.33                                   
REMARK 500    LYS B 429      123.26    148.62                                   
REMARK 500    LEU B 430     -171.00    114.86                                   
REMARK 500    ALA B 431       27.18    105.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B  104     LEU B  105                 -145.41                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3H37   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H38   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3H3A   RELATED DB: PDB                                   
DBREF  3H39 A    2   428  UNP    Q9WZH4   Q9WZH4_THEMA   437    863             
DBREF  3H39 B    2   428  UNP    Q9WZH4   Q9WZH4_THEMA   437    863             
SEQADV 3H39 MET A    1  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 LYS A  429  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 LEU A  430  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 ALA A  431  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 ALA A  432  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 ALA A  433  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 LEU A  434  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 GLU A  435  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS A  436  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS A  437  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS A  438  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS A  439  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS A  440  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS A  441  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 MET B    1  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 LYS B  429  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 LEU B  430  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 ALA B  431  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 ALA B  432  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 ALA B  433  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 LEU B  434  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 GLU B  435  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS B  436  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS B  437  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS B  438  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS B  439  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS B  440  UNP  Q9WZH4              EXPRESSION TAG                 
SEQADV 3H39 HIS B  441  UNP  Q9WZH4              EXPRESSION TAG                 
SEQRES   1 A  441  MET GLN ILE PHE ARG ASP VAL SER LYS LEU LEU VAL GLU          
SEQRES   2 A  441  ARG VAL ASP PRO LYS ILE LEU ASN LEU PHE ARG LEU LEU          
SEQRES   3 A  441  GLY LYS PHE GLY ASP GLU VAL ASN MET PRO VAL TYR VAL          
SEQRES   4 A  441  VAL GLY GLY PHE VAL ARG ASP LEU LEU LEU GLY ILE LYS          
SEQRES   5 A  441  ASN LEU ASP ILE ASP ILE VAL VAL GLU GLY ASN ALA LEU          
SEQRES   6 A  441  GLU PHE ALA GLU TYR ALA LYS ARG PHE LEU PRO GLY LYS          
SEQRES   7 A  441  LEU VAL LYS HIS ASP LYS PHE MET THR ALA SER LEU PHE          
SEQRES   8 A  441  LEU LYS GLY GLY LEU ARG ILE ASP ILE ALA THR ALA ARG          
SEQRES   9 A  441  LEU GLU TYR TYR GLU SER PRO ALA LYS LEU PRO ASP VAL          
SEQRES  10 A  441  GLU MET SER THR ILE LYS LYS ASP LEU TYR ARG ARG ASP          
SEQRES  11 A  441  PHE THR ILE ASN ALA MET ALA ILE LYS LEU ASN PRO LYS          
SEQRES  12 A  441  ASP PHE GLY LEU LEU ILE ASP PHE PHE GLY GLY TYR ARG          
SEQRES  13 A  441  ASP LEU LYS GLU GLY VAL ILE ARG VAL LEU HIS THR LEU          
SEQRES  14 A  441  SER PHE VAL ASP ASP PRO THR ARG ILE LEU ARG ALA ILE          
SEQRES  15 A  441  ARG PHE GLU GLN ARG PHE ASP PHE ARG ILE GLU GLU THR          
SEQRES  16 A  441  THR GLU ARG LEU LEU LYS GLN ALA VAL GLU GLU GLY TYR          
SEQRES  17 A  441  LEU GLU ARG THR THR GLY PRO ARG LEU ARG GLN GLU LEU          
SEQRES  18 A  441  GLU LYS ILE LEU GLU GLU LYS ASN PRO LEU LYS SER ILE          
SEQRES  19 A  441  ARG ARG MET ALA GLN PHE ASP VAL ILE LYS HIS LEU PHE          
SEQRES  20 A  441  PRO LYS THR TYR TYR THR PRO SER MET ASP GLU LYS MET          
SEQRES  21 A  441  GLU ASN LEU PHE ARG ASN ILE PRO TRP VAL GLU GLU ASN          
SEQRES  22 A  441  PHE GLY GLU VAL ASP ARG PHE TYR ALA VAL LEU HIS VAL          
SEQRES  23 A  441  PHE LEU GLU PHE TYR ASP ASP GLU SER TRP LYS GLU VAL          
SEQRES  24 A  441  ARG ASP ARG TYR SER LEU ARG ARG ASN LEU ILE ASN GLU          
SEQRES  25 A  441  ILE ARG HIS VAL GLU LYS SER ALA PRO ALA LEU LEU GLU          
SEQRES  26 A  441  MET LEU SER GLU ARG VAL PRO ALA SER PHE VAL TYR PRO          
SEQRES  27 A  441  LEU VAL LYS GLY VAL SER ASN GLU THR ILE CYS HIS PHE          
SEQRES  28 A  441  LEU ALA TYR LEU SER GLY GLU LYS GLU GLY LEU PHE LYS          
SEQRES  29 A  441  SER TYR LEU LEU LYS ILE LYS ASN THR LYS LEU GLU LYS          
SEQRES  30 A  441  ILE ASN GLY GLU TYR LEU ILE ARG LYS GLY ILE THR SER          
SEQRES  31 A  441  GLY LYS ILE ILE GLY GLU VAL LEU GLU LYS ILE LEU MET          
SEQRES  32 A  441  LYS LYS LEU ASP GLY ASP THR ARG ASP GLU GLU GLU ILE          
SEQRES  33 A  441  LEU GLU GLU VAL LEU ALA SER LEU GLU THR GLU GLY LYS          
SEQRES  34 A  441  LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  441  MET GLN ILE PHE ARG ASP VAL SER LYS LEU LEU VAL GLU          
SEQRES   2 B  441  ARG VAL ASP PRO LYS ILE LEU ASN LEU PHE ARG LEU LEU          
SEQRES   3 B  441  GLY LYS PHE GLY ASP GLU VAL ASN MET PRO VAL TYR VAL          
SEQRES   4 B  441  VAL GLY GLY PHE VAL ARG ASP LEU LEU LEU GLY ILE LYS          
SEQRES   5 B  441  ASN LEU ASP ILE ASP ILE VAL VAL GLU GLY ASN ALA LEU          
SEQRES   6 B  441  GLU PHE ALA GLU TYR ALA LYS ARG PHE LEU PRO GLY LYS          
SEQRES   7 B  441  LEU VAL LYS HIS ASP LYS PHE MET THR ALA SER LEU PHE          
SEQRES   8 B  441  LEU LYS GLY GLY LEU ARG ILE ASP ILE ALA THR ALA ARG          
SEQRES   9 B  441  LEU GLU TYR TYR GLU SER PRO ALA LYS LEU PRO ASP VAL          
SEQRES  10 B  441  GLU MET SER THR ILE LYS LYS ASP LEU TYR ARG ARG ASP          
SEQRES  11 B  441  PHE THR ILE ASN ALA MET ALA ILE LYS LEU ASN PRO LYS          
SEQRES  12 B  441  ASP PHE GLY LEU LEU ILE ASP PHE PHE GLY GLY TYR ARG          
SEQRES  13 B  441  ASP LEU LYS GLU GLY VAL ILE ARG VAL LEU HIS THR LEU          
SEQRES  14 B  441  SER PHE VAL ASP ASP PRO THR ARG ILE LEU ARG ALA ILE          
SEQRES  15 B  441  ARG PHE GLU GLN ARG PHE ASP PHE ARG ILE GLU GLU THR          
SEQRES  16 B  441  THR GLU ARG LEU LEU LYS GLN ALA VAL GLU GLU GLY TYR          
SEQRES  17 B  441  LEU GLU ARG THR THR GLY PRO ARG LEU ARG GLN GLU LEU          
SEQRES  18 B  441  GLU LYS ILE LEU GLU GLU LYS ASN PRO LEU LYS SER ILE          
SEQRES  19 B  441  ARG ARG MET ALA GLN PHE ASP VAL ILE LYS HIS LEU PHE          
SEQRES  20 B  441  PRO LYS THR TYR TYR THR PRO SER MET ASP GLU LYS MET          
SEQRES  21 B  441  GLU ASN LEU PHE ARG ASN ILE PRO TRP VAL GLU GLU ASN          
SEQRES  22 B  441  PHE GLY GLU VAL ASP ARG PHE TYR ALA VAL LEU HIS VAL          
SEQRES  23 B  441  PHE LEU GLU PHE TYR ASP ASP GLU SER TRP LYS GLU VAL          
SEQRES  24 B  441  ARG ASP ARG TYR SER LEU ARG ARG ASN LEU ILE ASN GLU          
SEQRES  25 B  441  ILE ARG HIS VAL GLU LYS SER ALA PRO ALA LEU LEU GLU          
SEQRES  26 B  441  MET LEU SER GLU ARG VAL PRO ALA SER PHE VAL TYR PRO          
SEQRES  27 B  441  LEU VAL LYS GLY VAL SER ASN GLU THR ILE CYS HIS PHE          
SEQRES  28 B  441  LEU ALA TYR LEU SER GLY GLU LYS GLU GLY LEU PHE LYS          
SEQRES  29 B  441  SER TYR LEU LEU LYS ILE LYS ASN THR LYS LEU GLU LYS          
SEQRES  30 B  441  ILE ASN GLY GLU TYR LEU ILE ARG LYS GLY ILE THR SER          
SEQRES  31 B  441  GLY LYS ILE ILE GLY GLU VAL LEU GLU LYS ILE LEU MET          
SEQRES  32 B  441  LYS LYS LEU ASP GLY ASP THR ARG ASP GLU GLU GLU ILE          
SEQRES  33 B  441  LEU GLU GLU VAL LEU ALA SER LEU GLU THR GLU GLY LYS          
SEQRES  34 B  441  LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS              
HET    ATP  A 501      31                                                       
HET    ATP  B 502      31                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   5  HOH   *40(H2 O)                                                     
HELIX    1   1 VAL A    7  VAL A   15  1                                   9    
HELIX    2   2 ASP A   16  VAL A   33  1                                  18    
HELIX    3   3 GLY A   41  GLY A   50  1                                  10    
HELIX    4   4 ASN A   63  ARG A   73  1                                  11    
HELIX    5   5 THR A  121  ARG A  128  1                                   8    
HELIX    6   6 PHE A  131  ALA A  135  5                                   5    
HELIX    7   7 ASN A  141  PHE A  145  5                                   5    
HELIX    8   8 GLY A  153  GLU A  160  1                                   8    
HELIX    9   9 LEU A  169  ASP A  174  1                                   6    
HELIX   10  10 PRO A  175  PHE A  188  1                                  14    
HELIX   11  11 GLU A  193  GLY A  207  1                                  15    
HELIX   12  12 THR A  213  GLU A  226  1                                  14    
HELIX   13  13 ASN A  229  PHE A  240  1                                  12    
HELIX   14  14 THR A  253  GLY A  275  1                                  23    
HELIX   15  15 ASP A  278  LEU A  288  1                                  11    
HELIX   16  16 ASP A  292  TYR A  303  1                                  12    
HELIX   17  17 ASN A  308  SER A  328  1                                  21    
HELIX   18  18 PRO A  332  VAL A  340  5                                   9    
HELIX   19  19 SER A  344  ALA A  353  1                                  10    
HELIX   20  20 SER A  356  THR A  373  1                                  18    
HELIX   21  21 GLU A  381  GLY A  387  1                                   7    
HELIX   22  22 SER A  390  LYS A  392  5                                   3    
HELIX   23  23 ILE A  393  GLY A  408  1                                  16    
HELIX   24  24 GLU A  413  LEU A  421  1                                   9    
HELIX   25  25 VAL B    7  VAL B   15  1                                   9    
HELIX   26  26 ASP B   16  VAL B   33  1                                  18    
HELIX   27  27 GLY B   41  GLY B   50  1                                  10    
HELIX   28  28 ASN B   63  ARG B   73  1                                  11    
HELIX   29  29 THR B  121  ARG B  128  1                                   8    
HELIX   30  30 PHE B  131  ALA B  135  5                                   5    
HELIX   31  31 ASN B  141  PHE B  145  5                                   5    
HELIX   32  32 GLY B  153  GLY B  161  1                                   9    
HELIX   33  33 LEU B  169  ASP B  174  1                                   6    
HELIX   34  34 PRO B  175  PHE B  188  1                                  14    
HELIX   35  35 GLU B  193  GLU B  206  1                                  14    
HELIX   36  36 THR B  213  GLU B  227  1                                  15    
HELIX   37  37 ASN B  229  PHE B  240  1                                  12    
HELIX   38  38 VAL B  242  PHE B  247  1                                   6    
HELIX   39  39 THR B  253  PHE B  274  1                                  22    
HELIX   40  40 ASP B  278  LEU B  288  1                                  11    
HELIX   41  41 ASP B  292  SER B  304  1                                  13    
HELIX   42  42 ASN B  308  SER B  328  1                                  21    
HELIX   43  43 PRO B  332  PHE B  335  5                                   4    
HELIX   44  44 VAL B  336  LYS B  341  1                                   6    
HELIX   45  45 SER B  344  ALA B  353  1                                  10    
HELIX   46  46 TYR B  354  SER B  356  5                                   3    
HELIX   47  47 GLY B  357  LYS B  374  1                                  18    
HELIX   48  48 GLU B  381  LYS B  386  1                                   6    
HELIX   49  49 ILE B  393  LEU B  406  1                                  14    
HELIX   50  50 GLU B  413  ALA B  422  1                                  10    
SHEET    1   A 8 PHE A   4  ASP A   6  0                                        
SHEET    2   A 8 LEU A 147  ILE A 149 -1  O  LEU A 148   N  ARG A   5           
SHEET    3   A 8 ALA A 137  LYS A 139 -1  N  ALA A 137   O  ILE A 149           
SHEET    4   A 8 VAL A  37  VAL A  40 -1  N  VAL A  39   O  ILE A 138           
SHEET    5   A 8 ASP A  55  VAL A  60 -1  O  VAL A  59   N  TYR A  38           
SHEET    6   A 8 LEU A  96  THR A 102  1  O  ASP A  99   N  ILE A  58           
SHEET    7   A 8 THR A  87  LEU A  92 -1  N  ALA A  88   O  ILE A 100           
SHEET    8   A 8 LYS A  78  HIS A  82 -1  N  LYS A  78   O  PHE A  91           
SHEET    1   B 2 VAL A 162  ILE A 163  0                                        
SHEET    2   B 2 ARG A 191  ILE A 192  1  O  ARG A 191   N  ILE A 163           
SHEET    1   C 8 PHE B   4  ASP B   6  0                                        
SHEET    2   C 8 LEU B 147  ILE B 149 -1  O  LEU B 148   N  ARG B   5           
SHEET    3   C 8 ALA B 137  LYS B 139 -1  N  ALA B 137   O  ILE B 149           
SHEET    4   C 8 VAL B  37  VAL B  40 -1  N  VAL B  39   O  ILE B 138           
SHEET    5   C 8 ILE B  56  VAL B  60 -1  O  VAL B  59   N  TYR B  38           
SHEET    6   C 8 LEU B  96  THR B 102  1  O  ASP B  99   N  ILE B  58           
SHEET    7   C 8 THR B  87  LEU B  92 -1  N  LEU B  90   O  ILE B  98           
SHEET    8   C 8 LYS B  78  HIS B  82 -1  N  LYS B  78   O  PHE B  91           
SHEET    1   D 2 VAL B 162  ILE B 163  0                                        
SHEET    2   D 2 ARG B 191  ILE B 192  1  O  ARG B 191   N  ILE B 163           
SITE     1 AC1 16 GLY A  41  GLY A  42  ARG A  45  ARG A 129                    
SITE     2 AC1 16 ASP A 130  ASN A 134  ASP A 174  THR A 176                    
SITE     3 AC1 16 ARG A 177  ARG A 180  ARG A 183  PHE A 184                    
SITE     4 AC1 16 ARG A 187  LYS A 223  HOH A 461  HOH A 462                    
SITE     1 AC2 10 GLY B  42  ARG B  45  ARG B 129  ASP B 130                    
SITE     2 AC2 10 ASN B 134  ASP B 174  ARG B 177  ARG B 180                    
SITE     3 AC2 10 ARG B 183  ARG B 187                                          
CRYST1  186.085   64.070  151.772  90.00 100.88  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005374  0.000000  0.001033        0.00000                         
SCALE2      0.000000  0.015608  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006709        0.00000                         
ATOM      1  N   MET A   1      48.078  -0.653  72.578  1.00106.89           N  
ANISOU    1  N   MET A   1    13117  10365  17133  -1429   2812  -2704       N  
ATOM      2  CA  MET A   1      48.432  -0.776  73.984  1.00104.22           C  
ANISOU    2  CA  MET A   1    12592   9905  17102  -1186   2703  -2278       C  
ATOM      3  C   MET A   1      47.174  -0.828  74.825  1.00 99.58           C  
ANISOU    3  C   MET A   1    11973   9495  16367  -1209   2449  -2272       C  
ATOM      4  O   MET A   1      46.072  -0.603  74.321  1.00103.01           O  
ANISOU    4  O   MET A   1    12525  10174  16439  -1394   2312  -2557       O  
ATOM      5  CB  MET A   1      49.271   0.421  74.425  1.00103.34           C  
ANISOU    5  CB  MET A   1    12411   9958  16895   -975   2371  -1935       C  
ATOM      6  CG  MET A   1      50.651   0.467  73.812  1.00110.33           C  
ANISOU    6  CG  MET A   1    13282  10642  17995   -898   2605  -1835       C  
ATOM      7  SD  MET A   1      51.260   2.151  73.720  1.00122.09           S  
ANISOU    7  SD  MET A   1    14787  12445  19158   -770   2177  -1652       S  
ATOM      8  CE  MET A   1      49.906   2.931  72.844  1.00 94.56           C  
ANISOU    8  CE  MET A   1    11483   9355  15090   -970   1928  -2049       C  
ATOM      9  N   GLN A   2      47.340  -1.125  76.109  1.00 82.16           N  
ANISOU    9  N   GLN A   2     9594   7185  14437  -1025   2389  -1920       N  
ATOM     10  CA  GLN A   2      46.246  -0.984  77.054  1.00 64.99           C  
ANISOU   10  CA  GLN A   2     7381   5205  12107  -1001   2094  -1845       C  
ATOM     11  C   GLN A   2      45.657   0.419  76.905  1.00 69.03           C  
ANISOU   11  C   GLN A   2     8003   6124  12101  -1019   1649  -1894       C  
ATOM     12  O   GLN A   2      46.364   1.428  77.065  1.00 61.69           O  
ANISOU   12  O   GLN A   2     7061   5320  11059   -896   1433  -1698       O  
ATOM     13  CB  GLN A   2      46.745  -1.208  78.480  1.00 57.20           C  
ANISOU   13  CB  GLN A   2     6178   4126  11430   -777   2029  -1392       C  
ATOM     14  CG  GLN A   2      45.664  -1.500  79.490  1.00 69.45           C  
ANISOU   14  CG  GLN A   2     7663   5767  12956   -752   1867  -1317       C  
ATOM     15  CD  GLN A   2      46.194  -2.232  80.710  1.00 87.97           C  
ANISOU   15  CD  GLN A   2     9760   7936  15730   -572   1980   -907       C  
ATOM     16  OE1 GLN A   2      45.485  -2.402  81.709  1.00 85.78           O  
ANISOU   16  OE1 GLN A   2     9393   7747  15451   -510   1824   -761       O  
ATOM     17  NE2 GLN A   2      47.449  -2.676  80.634  1.00 97.52           N  
ANISOU   17  NE2 GLN A   2    10836   8905  17313   -483   2263   -689       N  
ATOM     18  N   ILE A   3      44.378   0.478  76.566  1.00 68.50           N  
ANISOU   18  N   ILE A   3     8034   6257  11737  -1181   1536  -2144       N  
ATOM     19  CA  ILE A   3      43.667   1.728  76.421  1.00 54.68           C  
ANISOU   19  CA  ILE A   3     6368   4886   9523  -1204   1165  -2172       C  
ATOM     20  C   ILE A   3      42.872   2.116  77.627  1.00 56.00           C  
ANISOU   20  C   ILE A   3     6478   5191   9610  -1080    867  -1943       C  
ATOM     21  O   ILE A   3      42.674   3.271  77.877  1.00 44.94           O  
ANISOU   21  O   ILE A   3     5104   4018   7954   -995    569  -1805       O  
ATOM     22  CB  ILE A   3      42.706   1.654  75.315  1.00 20.00           C  
ATOM     23  CG1 ILE A   3      43.453   1.508  74.025  1.00 20.00           C  
ATOM     24  CG2 ILE A   3      41.936   2.879  75.283  1.00 20.00           C  
ATOM     25  CD1 ILE A   3      42.605   1.708  72.876  1.00 20.00           C  
ATOM     26  N   PHE A   4      42.405   1.137  78.375  1.00 61.41           N  
ANISOU   26  N   PHE A   4     7086   5724  10524  -1074    972  -1904       N  
ATOM     27  CA  PHE A   4      41.643   1.419  79.586  1.00 59.09           C  
ANISOU   27  CA  PHE A   4     6739   5553  10158   -961    712  -1693       C  
ATOM     28  C   PHE A   4      42.345   0.955  80.858  1.00 60.34           C  
ANISOU   28  C   PHE A   4     6732   5533  10662   -774    746  -1359       C  
ATOM     29  O   PHE A   4      43.004  -0.069  80.862  1.00 70.26           O  
ANISOU   29  O   PHE A   4     7883   6514  12300   -755   1049  -1317       O  
ATOM     30  CB  PHE A   4      40.246   0.843  79.467  1.00 53.71           C  
ANISOU   30  CB  PHE A   4     6092   4936   9381  -1103    726  -1881       C  
ATOM     31  CG  PHE A   4      39.448   1.456  78.363  1.00 60.11           C  
ANISOU   31  CG  PHE A   4     7028   6022   9790  -1292    623  -2127       C  
ATOM     32  CD1 PHE A   4      39.207   0.764  77.197  1.00 59.95           C  
ANISOU   32  CD1 PHE A   4     7067   5975   9737  -1539    859  -2459       C  
ATOM     33  CD2 PHE A   4      38.961   2.748  78.481  1.00 67.31           C  
ANISOU   33  CD2 PHE A   4     7987   7232  10355  -1235    309  -2013       C  
ATOM     34  CE1 PHE A   4      38.481   1.341  76.184  1.00 61.61           C  
ANISOU   34  CE1 PHE A   4     7360   6500   9548  -1732    749  -2648       C  
ATOM     35  CE2 PHE A   4      38.229   3.330  77.462  1.00 63.52           C  
ANISOU   35  CE2 PHE A   4     7579   7036   9518  -1399    224  -2177       C  
ATOM     36  CZ  PHE A   4      37.993   2.626  76.316  1.00 59.97           C  
ANISOU   36  CZ  PHE A   4     7165   6609   9011  -1648    428  -2480       C  
ATOM     37  N   ARG A   5      42.224   1.729  81.929  1.00 53.32           N  
ANISOU   37  N   ARG A   5     5810   4811   9638   -646    453  -1109       N  
ATOM     38  CA  ARG A   5      42.907   1.403  83.174  1.00 55.69           C  
ANISOU   38  CA  ARG A   5     5934   5025  10202   -492    444   -761       C  
ATOM     39  C   ARG A   5      42.106   1.848  84.375  1.00 56.63           C  
ANISOU   39  C   ARG A   5     6039   5329  10149   -418    169   -591       C  
ATOM     40  O   ARG A   5      41.408   2.856  84.325  1.00 60.20           O  
ANISOU   40  O   ARG A   5     6630   5993  10251   -446    -62   -672       O  
ATOM     41  CB  ARG A   5      44.264   2.084  83.250  1.00 52.58           C  
ANISOU   41  CB  ARG A   5     5496   4653   9830   -420    384   -565       C  
ATOM     42  CG  ARG A   5      45.280   1.569  82.285  1.00 54.42           C  
ANISOU   42  CG  ARG A   5     5703   4666  10309   -448    682   -637       C  
ATOM     43  CD  ARG A   5      46.499   2.457  82.338  1.00 51.88           C  
ANISOU   43  CD  ARG A   5     5354   4416   9941   -382    561   -442       C  
ATOM     44  NE  ARG A   5      47.480   2.088  81.332  1.00 49.14           N  
ANISOU   44  NE  ARG A   5     5000   3864   9806   -401    841   -509       N  
ATOM     45  CZ  ARG A   5      48.364   1.117  81.495  1.00 62.85           C  
ANISOU   45  CZ  ARG A   5     6564   5346  11972   -335   1135   -302       C  
ATOM     46  NH1 ARG A   5      48.369   0.421  82.620  1.00 66.42           N  
ANISOU   46  NH1 ARG A   5     6814   5746  12676   -247   1172     -5       N  
ATOM     47  NH2 ARG A   5      49.241   0.845  80.539  1.00 75.45           N  
ANISOU   47  NH2 ARG A   5     8173   6741  13755   -350   1411   -369       N  
ATOM     48  N   ASP A   6      42.254   1.157  85.476  1.00 51.56           N  
ANISOU   48  N   ASP A   6     5217   4606   9769   -318    219   -331       N  
ATOM     49  CA  ASP A   6      41.539   1.508  86.661  1.00 56.57           C  
ANISOU   49  CA  ASP A   6     5821   5410  10263   -244    -18   -144       C  
ATOM     50  C   ASP A   6      42.455   2.277  87.574  1.00 61.54           C  
ANISOU   50  C   ASP A   6     6391   6203  10789   -182   -220    138       C  
ATOM     51  O   ASP A   6      43.336   1.726  88.191  1.00 76.17           O  
ANISOU   51  O   ASP A   6     8037   8006  12898   -118   -141    423       O  
ATOM     52  CB  ASP A   6      41.100   0.218  87.325  1.00 64.32           C  
ANISOU   52  CB  ASP A   6     6621   6247  11572   -177    144     -3       C  
ATOM     53  CG  ASP A   6      40.265   0.437  88.528  1.00 74.39           C  
ANISOU   53  CG  ASP A   6     7891   7693  12681   -113    -82    135       C  
ATOM     54  OD1 ASP A   6      40.453  -0.271  89.513  1.00 76.30           O  
ANISOU   54  OD1 ASP A   6     7932   7893  13165    -15    -25    394       O  
ATOM     55  OD2 ASP A   6      39.409   1.304  88.497  1.00 76.94           O  
ANISOU   55  OD2 ASP A   6     8402   8191  12642   -154   -297      3       O  
ATOM     56  N   VAL A   7      42.220   3.567  87.684  1.00 51.70           N  
ANISOU   56  N   VAL A   7     5311   5160   9173   -215   -466     74       N  
ATOM     57  CA  VAL A   7      43.031   4.413  88.544  1.00 53.81           C  
ANISOU   57  CA  VAL A   7     5543   5593   9308   -201   -653    298       C  
ATOM     58  C   VAL A   7      42.199   4.871  89.730  1.00 59.75           C  
ANISOU   58  C   VAL A   7     6339   6523   9841   -185   -854    395       C  
ATOM     59  O   VAL A   7      42.429   5.937  90.286  1.00 66.84           O  
ANISOU   59  O   VAL A   7     7319   7592  10484   -225  -1035    450       O  
ATOM     60  CB  VAL A   7      43.668   5.637  87.789  1.00 46.80           C  
ANISOU   60  CB  VAL A   7     4804   4779   8199   -262   -742    173       C  
ATOM     61  CG1 VAL A   7      44.457   5.174  86.593  1.00 37.93           C  
ANISOU   61  CG1 VAL A   7     3647   3479   7284   -274   -532     73       C  
ATOM     62  CG2 VAL A   7      42.607   6.666  87.352  1.00 48.14           C  
ANISOU   62  CG2 VAL A   7     5202   5058   8032   -302   -863    -59       C  
ATOM     63  N   SER A   8      41.230   4.058  90.127  1.00 62.85           N  
ANISOU   63  N   SER A   8     6679   6863  10337   -135   -802    408       N  
ATOM     64  CA  SER A   8      40.395   4.422  91.264  1.00 56.13           C  
ANISOU   64  CA  SER A   8     5869   6166   9292   -108   -970    508       C  
ATOM     65  C   SER A   8      41.195   4.387  92.568  1.00 54.88           C  
ANISOU   65  C   SER A   8     5536   6156   9158    -95  -1065    834       C  
ATOM     66  O   SER A   8      41.096   5.292  93.386  1.00 56.67           O  
ANISOU   66  O   SER A   8     5853   6575   9103   -143  -1244    888       O  
ATOM     67  CB  SER A   8      39.170   3.517  91.346  1.00 34.33           C  
ANISOU   67  CB  SER A   8     3078   3310   6654    -51   -888    460       C  
ATOM     68  OG  SER A   8      39.584   2.179  91.465  1.00 59.58           O  
ANISOU   68  OG  SER A   8     6044   6353  10242      6   -694    602       O  
ATOM     69  N   LYS A   9      41.997   3.351  92.762  1.00 62.12           N  
ANISOU   69  N   LYS A   9     6194   6997  10411    -47   -927   1062       N  
ATOM     70  CA  LYS A   9      42.784   3.258  93.991  1.00 81.09           C  
ANISOU   70  CA  LYS A   9     8380   9595  12837    -49  -1019   1428       C  
ATOM     71  C   LYS A   9      43.792   4.401  94.023  1.00 85.50           C  
ANISOU   71  C   LYS A   9     9011  10325  13151   -169  -1174   1452       C  
ATOM     72  O   LYS A   9      43.960   5.077  95.040  1.00 87.89           O  
ANISOU   72  O   LYS A   9     9319  10881  13196   -254  -1362   1584       O  
ATOM     73  CB  LYS A   9      43.466   1.889  94.136  1.00 86.79           C  
ANISOU   73  CB  LYS A   9     8767  10193  14015     42   -800   1726       C  
ATOM     74  CG  LYS A   9      44.153   1.362  92.870  1.00104.59           C  
ANISOU   74  CG  LYS A   9    10991  12177  16572     58   -545   1621       C  
ATOM     75  CD  LYS A   9      43.196   1.250  91.669  1.00104.48           C  
ANISOU   75  CD  LYS A   9    11208  11942  16546     45   -425   1198       C  
ATOM     76  CE  LYS A   9      43.539   0.067  90.762  1.00106.76           C  
ANISOU   76  CE  LYS A   9    11382  11916  17266     79    -69   1145       C  
ATOM     77  NZ  LYS A   9      43.229  -1.268  91.374  1.00102.50           N  
ANISOU   77  NZ  LYS A   9    10596  11239  17110    181    140   1355       N  
ATOM     78  N   LEU A  10      44.437   4.628  92.887  1.00 77.53           N  
ANISOU   78  N   LEU A  10     8066   9178  12212   -190  -1084   1305       N  
ATOM     79  CA  LEU A  10      45.330   5.758  92.742  1.00 70.39           C  
ANISOU   79  CA  LEU A  10     7253   8402  11091   -298  -1216   1286       C  
ATOM     80  C   LEU A  10      44.621   7.048  93.145  1.00 61.27           C  
ANISOU   80  C   LEU A  10     6357   7404   9519   -386  -1408   1099       C  
ATOM     81  O   LEU A  10      45.197   7.912  93.794  1.00 53.57           O  
ANISOU   81  O   LEU A  10     5410   6628   8317   -507  -1559   1179       O  
ATOM     82  CB  LEU A  10      45.783   5.866  91.297  1.00 69.16           C  
ANISOU   82  CB  LEU A  10     7185   8047  11045   -287  -1079   1079       C  
ATOM     83  CG  LEU A  10      46.889   6.875  91.035  1.00 65.02           C  
ANISOU   83  CG  LEU A  10     6706   7616  10382   -376  -1177   1098       C  
ATOM     84  CD1 LEU A  10      48.148   6.398  91.722  1.00 61.98           C  
ANISOU   84  CD1 LEU A  10     6033   7333  10184   -396  -1179   1495       C  
ATOM     85  CD2 LEU A  10      47.108   7.029  89.540  1.00 67.71           C  
ANISOU   85  CD2 LEU A  10     7164   7762  10800   -351  -1040    854       C  
ATOM     86  N   LEU A  11      43.361   7.178  92.762  1.00 55.24           N  
ANISOU   86  N   LEU A  11     5777   6548   8662   -338  -1382    859       N  
ATOM     87  CA  LEU A  11      42.631   8.388  93.080  1.00 57.20           C  
ANISOU   87  CA  LEU A  11     6269   6903   8562   -401  -1506    702       C  
ATOM     88  C   LEU A  11      42.505   8.597  94.584  1.00 65.82           C  
ANISOU   88  C   LEU A  11     7329   8206   9475   -465  -1638    879       C  
ATOM     89  O   LEU A  11      42.821   9.681  95.075  1.00 71.52           O  
ANISOU   89  O   LEU A  11     8173   9073   9927   -597  -1744    847       O  
ATOM     90  CB  LEU A  11      41.251   8.417  92.401  1.00 48.51           C  
ANISOU   90  CB  LEU A  11     5333   5681   7417   -329  -1441    474       C  
ATOM     91  CG  LEU A  11      41.174   8.979  90.979  1.00 37.20           C  
ANISOU   91  CG  LEU A  11     4041   4150   5945   -335  -1372    234       C  
ATOM     92  CD1 LEU A  11      39.825   8.668  90.377  1.00 39.14           C  
ANISOU   92  CD1 LEU A  11     4365   4320   6187   -279  -1305     86       C  
ATOM     93  CD2 LEU A  11      41.431  10.477  90.964  1.00 31.99           C  
ANISOU   93  CD2 LEU A  11     3557   3579   5018   -414  -1452    149       C  
ATOM     94  N   VAL A  12      42.056   7.577  95.318  1.00 58.38           N  
ANISOU   94  N   VAL A  12     6221   7284   8675   -388  -1619   1060       N  
ATOM     95  CA  VAL A  12      41.725   7.789  96.728  1.00 65.42           C  
ANISOU   95  CA  VAL A  12     7103   8391   9361   -446  -1739   1205       C  
ATOM     96  C   VAL A  12      42.970   8.020  97.585  1.00 73.96           C  
ANISOU   96  C   VAL A  12     8027   9734  10341   -599  -1856   1446       C  
ATOM     97  O   VAL A  12      42.901   8.676  98.633  1.00 81.07           O  
ANISOU   97  O   VAL A  12     8998  10860  10944   -737  -1977   1484       O  
ATOM     98  CB  VAL A  12      40.871   6.654  97.352  1.00 56.75           C  
ANISOU   98  CB  VAL A  12     5855   7270   8438   -314  -1693   1360       C  
ATOM     99  CG1 VAL A  12      39.948   5.993  96.304  1.00 45.85           C  
ANISOU   99  CG1 VAL A  12     4523   5619   7278   -173  -1546   1181       C  
ATOM    100  CG2 VAL A  12      41.765   5.639  98.035  1.00 62.06           C  
ANISOU  100  CG2 VAL A  12     6175   8064   9341   -297  -1682   1727       C  
ATOM    101  N   GLU A  13      44.106   7.499  97.133  1.00 68.76           N  
ANISOU  101  N   GLU A  13     7155   9052   9919   -593  -1809   1612       N  
ATOM    102  CA  GLU A  13      45.341   7.647  97.882  1.00 62.40           C  
ANISOU  102  CA  GLU A  13     6152   8518   9039   -744  -1922   1895       C  
ATOM    103  C   GLU A  13      46.037   8.985  97.602  1.00 71.70           C  
ANISOU  103  C   GLU A  13     7521   9776   9947   -928  -2019   1724       C  
ATOM    104  O   GLU A  13      46.601   9.605  98.507  1.00 86.77           O  
ANISOU  104  O   GLU A  13     9408  11971  11589  -1136  -2164   1832       O  
ATOM    105  CB  GLU A  13      46.269   6.446  97.646  1.00 66.63           C  
ANISOU  105  CB  GLU A  13     6332   9004   9981   -647  -1805   2227       C  
ATOM    106  CG  GLU A  13      47.314   6.639  96.566  1.00 90.05           C  
ANISOU  106  CG  GLU A  13     9285  11831  13099   -655  -1732   2191       C  
ATOM    107  CD  GLU A  13      48.081   5.359  96.247  1.00103.71           C  
ANISOU  107  CD  GLU A  13    10679  13434  15291   -526  -1541   2510       C  
ATOM    108  OE1 GLU A  13      47.525   4.257  96.493  1.00105.72           O  
ANISOU  108  OE1 GLU A  13    10772  13589  15807   -385  -1405   2641       O  
ATOM    109  OE2 GLU A  13      49.229   5.463  95.739  1.00 99.27           O  
ANISOU  109  OE2 GLU A  13    10016  12852  14849   -560  -1504   2633       O  
ATOM    110  N   ARG A  14      45.975   9.451  96.362  1.00 67.20           N  
ANISOU  110  N   ARG A  14     7135   8967   9430   -869  -1934   1453       N  
ATOM    111  CA  ARG A  14      46.676  10.678  95.991  1.00 56.12           C  
ANISOU  111  CA  ARG A  14     5890   7606   7828  -1019  -1998   1303       C  
ATOM    112  C   ARG A  14      45.787  11.907  96.035  1.00 48.80           C  
ANISOU  112  C   ARG A  14     5298   6652   6593  -1088  -2013    988       C  
ATOM    113  O   ARG A  14      46.294  13.011  96.103  1.00 63.41           O  
ANISOU  113  O   ARG A  14     7280   8581   8232  -1253  -2067    881       O  
ATOM    114  CB  ARG A  14      47.336  10.559  94.601  1.00 61.44           C  
ANISOU  114  CB  ARG A  14     6540   8063   8743   -924  -1888   1234       C  
ATOM    115  CG  ARG A  14      48.491   9.545  94.504  1.00 59.51           C  
ANISOU  115  CG  ARG A  14     5970   7827   8815   -880  -1836   1568       C  
ATOM    116  CD  ARG A  14      49.175   9.547  93.131  1.00 71.36           C  
ANISOU  116  CD  ARG A  14     7482   9106  10527   -802  -1711   1477       C  
ATOM    117  NE  ARG A  14      50.013   8.357  92.921  1.00 89.13           N  
ANISOU  117  NE  ARG A  14     9432  11273  13160   -707  -1573   1782       N  
ATOM    118  CZ  ARG A  14      50.914   8.208  91.946  1.00 89.81           C  
ANISOU  118  CZ  ARG A  14     9455  11199  13468   -655  -1452   1815       C  
ATOM    119  NH1 ARG A  14      51.128   9.175  91.064  1.00 91.42           N  
ANISOU  119  NH1 ARG A  14     9863  11332  13541   -688  -1474   1565       N  
ATOM    120  NH2 ARG A  14      51.607   7.082  91.852  1.00 83.91           N  
ANISOU  120  NH2 ARG A  14     8430  10355  13096   -562  -1282   2118       N  
ATOM    121  N   VAL A  15      44.468  11.736  95.989  1.00 50.53           N  
ANISOU  121  N   VAL A  15     5646   6748   6805   -965  -1945    852       N  
ATOM    122  CA  VAL A  15      43.579  12.903  95.906  1.00 53.99           C  
ANISOU  122  CA  VAL A  15     6390   7121   7003  -1000  -1908    585       C  
ATOM    123  C   VAL A  15      42.974  13.317  97.242  1.00 60.58           C  
ANISOU  123  C   VAL A  15     7334   8115   7570  -1117  -1959    594       C  
ATOM    124  O   VAL A  15      42.287  12.536  97.906  1.00 71.76           O  
ANISOU  124  O   VAL A  15     8668   9575   9024  -1040  -1971    716       O  
ATOM    125  CB  VAL A  15      42.441  12.761  94.836  1.00 45.70           C  
ANISOU  125  CB  VAL A  15     5455   5835   6073   -810  -1782    408       C  
ATOM    126  CG1 VAL A  15      41.510  13.984  94.875  1.00 43.77           C  
ANISOU  126  CG1 VAL A  15     5490   5541   5600   -839  -1720    210       C  
ATOM    127  CG2 VAL A  15      43.011  12.609  93.437  1.00 36.76           C  
ANISOU  127  CG2 VAL A  15     4272   4562   5134   -737  -1715    336       C  
ATOM    128  N   ASP A  16      43.242  14.559  97.623  1.00 58.16           N  
ANISOU  128  N   ASP A  16     7216   7886   6996  -1313  -1969    456       N  
ATOM    129  CA  ASP A  16      42.682  15.141  98.835  1.00 67.50           C  
ANISOU  129  CA  ASP A  16     8558   9199   7890  -1464  -1973    404       C  
ATOM    130  C   ASP A  16      41.162  15.008  98.843  1.00 68.75           C  
ANISOU  130  C   ASP A  16     8856   9195   8071  -1285  -1862    328       C  
ATOM    131  O   ASP A  16      40.503  15.341  97.856  1.00 67.89           O  
ANISOU  131  O   ASP A  16     8869   8865   8062  -1140  -1744    188       O  
ATOM    132  CB  ASP A  16      43.086  16.609  98.936  1.00 75.63           C  
ANISOU  132  CB  ASP A  16     9820  10241   8675  -1690  -1922    190       C  
ATOM    133  CG  ASP A  16      42.298  17.350  99.974  1.00 89.25           C  
ANISOU  133  CG  ASP A  16    11782  12009  10120  -1830  -1840     61       C  
ATOM    134  OD1 ASP A  16      41.408  18.123  99.581  1.00 98.28           O  
ANISOU  134  OD1 ASP A  16    13161  12929  11252  -1750  -1658   -127       O  
ATOM    135  OD2 ASP A  16      42.552  17.152 101.179  1.00 98.05           O  
ANISOU  135  OD2 ASP A  16    12838  13387  11030  -2021  -1940    163       O  
ATOM    136  N   PRO A  17      40.603  14.504  99.958  1.00 64.99           N  
ANISOU  136  N   PRO A  17     8341   8851   7503  -1296  -1904    450       N  
ATOM    137  CA  PRO A  17      39.182  14.149 100.086  1.00 61.02           C  
ANISOU  137  CA  PRO A  17     7916   8216   7051  -1111  -1820    445       C  
ATOM    138  C   PRO A  17      38.150  15.221  99.754  1.00 60.74           C  
ANISOU  138  C   PRO A  17     8181   7979   6919  -1070  -1645    234       C  
ATOM    139  O   PRO A  17      37.106  14.838  99.229  1.00 64.29           O  
ANISOU  139  O   PRO A  17     8642   8268   7516   -865  -1575    245       O  
ATOM    140  CB  PRO A  17      39.070  13.678 101.532  1.00 49.16           C  
ANISOU  140  CB  PRO A  17     6328   6952   5397  -1201  -1906    614       C  
ATOM    141  CG  PRO A  17      40.377  13.033 101.760  1.00 53.46           C  
ANISOU  141  CG  PRO A  17     6586   7724   6001  -1304  -2054    825       C  
ATOM    142  CD  PRO A  17      41.383  13.942 101.068  1.00 55.65           C  
ANISOU  142  CD  PRO A  17     6946   7978   6222  -1452  -2054    677       C  
ATOM    143  N   LYS A  18      38.405  16.498 100.020  1.00 59.27           N  
ANISOU  143  N   LYS A  18     8215   7793   6513  -1259  -1558     64       N  
ATOM    144  CA  LYS A  18      37.468  17.523  99.557  1.00 68.84           C  
ANISOU  144  CA  LYS A  18     9680   8776   7700  -1192  -1341    -98       C  
ATOM    145  C   LYS A  18      37.287  17.412  98.029  1.00 66.78           C  
ANISOU  145  C   LYS A  18     9354   8341   7678   -993  -1299   -115       C  
ATOM    146  O   LYS A  18      36.185  17.583  97.505  1.00 65.91           O  
ANISOU  146  O   LYS A  18     9322   8076   7645   -831  -1169   -119       O  
ATOM    147  CB  LYS A  18      37.927  18.938  99.947  1.00 76.94           C  
ANISOU  147  CB  LYS A  18    10940   9793   8501  -1437  -1208   -294       C  
ATOM    148  CG  LYS A  18      38.396  19.095 101.406  1.00 93.35           C  
ANISOU  148  CG  LYS A  18    13073  12109  10288  -1722  -1270   -311       C  
ATOM    149  CD  LYS A  18      37.238  19.100 102.413  1.00103.86           C  
ANISOU  149  CD  LYS A  18    14554  13422  11486  -1703  -1156   -300       C  
ATOM    150  CE  LYS A  18      36.807  20.518 102.805  1.00107.24           C  
ANISOU  150  CE  LYS A  18    15324  13692  11732  -1863   -866   -531       C  
ATOM    151  NZ  LYS A  18      35.519  20.553 103.578  1.00105.25           N  
ANISOU  151  NZ  LYS A  18    15235  13346  11410  -1783   -698   -508       N  
ATOM    152  N   ILE A  19      38.399  17.242  97.345  1.00 57.86           N  
ANISOU  152  N   ILE A  19     8065   7261   6658  -1015  -1409   -102       N  
ATOM    153  CA  ILE A  19      38.445  17.068  95.908  1.00 52.60           C  
ANISOU  153  CA  ILE A  19     7345   6464   6176   -878  -1367   -145       C  
ATOM    154  C   ILE A  19      37.956  15.762  95.342  1.00 57.03           C  
ANISOU  154  C   ILE A  19     7713   7001   6953   -699  -1434    -37       C  
ATOM    155  O   ILE A  19      37.297  15.749  94.353  1.00 58.22           O  
ANISOU  155  O   ILE A  19     7859   7047   7214   -573  -1365    -75       O  
ATOM    156  CB  ILE A  19      39.821  17.323  95.381  1.00 20.00           C  
ATOM    157  CG1 ILE A  19      40.174  18.774  95.604  1.00 20.00           C  
ATOM    158  CG2 ILE A  19      39.864  17.020  93.938  1.00 20.00           C  
ATOM    159  CD1 ILE A  19      41.537  19.085  95.233  1.00 20.00           C  
ATOM    160  N   LEU A  20      38.312  14.660  95.969  1.00 62.95           N  
ANISOU  160  N   LEU A  20     8291   7859   7767   -704  -1555    104       N  
ATOM    161  CA  LEU A  20      37.852  13.341  95.535  1.00 57.06           C  
ANISOU  161  CA  LEU A  20     7368   7063   7248   -546  -1578    198       C  
ATOM    162  C   LEU A  20      36.334  13.303  95.712  1.00 61.69           C  
ANISOU  162  C   LEU A  20     8055   7575   7809   -430  -1505    204       C  
ATOM    163  O   LEU A  20      35.608  12.712  94.915  1.00 60.24           O  
ANISOU  163  O   LEU A  20     7816   7305   7769   -307  -1469    200       O  
ATOM    164  CB  LEU A  20      38.494  12.233  96.362  1.00 47.43           C  
ANISOU  164  CB  LEU A  20     5925   5968   6127   -567  -1684    389       C  
ATOM    165  CG  LEU A  20      38.761  10.884  95.680  1.00 46.49           C  
ANISOU  165  CG  LEU A  20     5571   5776   6316   -453  -1676    477       C  
ATOM    166  CD1 LEU A  20      38.589   9.709  96.655  1.00 35.63           C  
ANISOU  166  CD1 LEU A  20     3995   4476   5068   -395  -1716    698       C  
ATOM    167  CD2 LEU A  20      37.878  10.696  94.478  1.00 39.73           C  
ANISOU  167  CD2 LEU A  20     4772   4753   5570   -338  -1580    339       C  
ATOM    168  N   ASN A  21      35.856  13.962  96.759  1.00 57.00           N  
ANISOU  168  N   ASN A  21     7614   7021   7022   -487  -1473    212       N  
ATOM    169  CA  ASN A  21      34.435  13.996  97.023  1.00 50.74           C  
ANISOU  169  CA  ASN A  21     6922   6152   6206   -373  -1389    249       C  
ATOM    170  C   ASN A  21      33.687  14.746  95.930  1.00 57.08           C  
ANISOU  170  C   ASN A  21     7839   6824   7026   -295  -1254    172       C  
ATOM    171  O   ASN A  21      32.621  14.326  95.471  1.00 64.08           O  
ANISOU  171  O   ASN A  21     8692   7652   8003   -165  -1218    233       O  
ATOM    172  CB  ASN A  21      34.160  14.561  98.421  1.00 45.80           C  
ANISOU  172  CB  ASN A  21     6447   5591   5364   -465  -1355    270       C  
ATOM    173  CG  ASN A  21      34.242  13.486  99.510  1.00 53.85           C  
ANISOU  173  CG  ASN A  21     7305   6756   6400   -462  -1481    433       C  
ATOM    174  OD1 ASN A  21      34.242  12.289  99.223  1.00 56.42           O  
ANISOU  174  OD1 ASN A  21     7414   7085   6939   -350  -1557    545       O  
ATOM    175  ND2 ASN A  21      34.308  13.913 100.758  1.00 58.81           N  
ANISOU  175  ND2 ASN A  21     8033   7507   6805   -595  -1481    447       N  
ATOM    176  N   LEU A  22      34.270  15.852  95.501  1.00 52.59           N  
ANISOU  176  N   LEU A  22     7381   6226   6373   -382  -1178     58       N  
ATOM    177  CA  LEU A  22      33.733  16.625  94.396  1.00 45.31           C  
ANISOU  177  CA  LEU A  22     6526   5211   5479   -313  -1041     19       C  
ATOM    178  C   LEU A  22      33.664  15.806  93.113  1.00 53.98           C  
ANISOU  178  C   LEU A  22     7451   6324   6736   -227  -1105     28       C  
ATOM    179  O   LEU A  22      32.778  16.031  92.290  1.00 59.50           O  
ANISOU  179  O   LEU A  22     8149   6998   7460   -144  -1021     67       O  
ATOM    180  CB  LEU A  22      34.617  17.834  94.167  1.00 45.48           C  
ANISOU  180  CB  LEU A  22     6657   5206   5418   -428   -958   -102       C  
ATOM    181  CG  LEU A  22      34.033  18.988  93.379  1.00 56.08           C  
ANISOU  181  CG  LEU A  22     8101   6444   6762   -369   -750   -111       C  
ATOM    182  CD1 LEU A  22      32.686  19.431  93.955  1.00 57.25           C  
ANISOU  182  CD1 LEU A  22     8380   6502   6871   -291   -574    -11       C  
ATOM    183  CD2 LEU A  22      35.041  20.123  93.397  1.00 59.34           C  
ANISOU  183  CD2 LEU A  22     8621   6819   7105   -506   -664   -242       C  
ATOM    184  N   PHE A  23      34.600  14.874  92.924  1.00 46.98           N  
ANISOU  184  N   PHE A  23     6411   5486   5952   -262  -1233      4       N  
ATOM    185  CA  PHE A  23      34.535  13.999  91.757  1.00 54.43           C  
ANISOU  185  CA  PHE A  23     7207   6427   7047   -208  -1260    -19       C  
ATOM    186  C   PHE A  23      33.359  13.033  91.863  1.00 55.29           C  
ANISOU  186  C   PHE A  23     7246   6527   7236   -121  -1271     63       C  
ATOM    187  O   PHE A  23      32.559  12.907  90.939  1.00 59.47           O  
ANISOU  187  O   PHE A  23     7745   7064   7787    -82  -1230     58       O  
ATOM    188  CB  PHE A  23      35.840  13.227  91.519  1.00 47.74           C  
ANISOU  188  CB  PHE A  23     6216   5594   6328   -261  -1341    -55       C  
ATOM    189  CG  PHE A  23      36.972  14.080  91.042  1.00 46.28           C  
ANISOU  189  CG  PHE A  23     6069   5418   6097   -338  -1332   -136       C  
ATOM    190  CD1 PHE A  23      36.730  15.250  90.357  1.00 54.41           C  
ANISOU  190  CD1 PHE A  23     7213   6432   7029   -335  -1240   -200       C  
ATOM    191  CD2 PHE A  23      38.285  13.710  91.272  1.00 44.59           C  
ANISOU  191  CD2 PHE A  23     5755   5230   5956   -405  -1404   -116       C  
ATOM    192  CE1 PHE A  23      37.779  16.041  89.920  1.00 55.24           C  
ANISOU  192  CE1 PHE A  23     7344   6535   7109   -399  -1225   -270       C  
ATOM    193  CE2 PHE A  23      39.335  14.503  90.842  1.00 40.49           C  
ANISOU  193  CE2 PHE A  23     5267   4716   5400   -473  -1394   -173       C  
ATOM    194  CZ  PHE A  23      39.086  15.664  90.168  1.00 42.86           C  
ANISOU  194  CZ  PHE A  23     5693   4987   5603   -463  -1301   -258       C  
ATOM    195  N   ARG A  24      33.262  12.352  92.991  1.00 52.19           N  
ANISOU  195  N   ARG A  24     6813   6139   6878   -101  -1329    152       N  
ATOM    196  CA  ARG A  24      32.153  11.446  93.222  1.00 52.16           C  
ANISOU  196  CA  ARG A  24     6741   6115   6963    -12  -1336    242       C  
ATOM    197  C   ARG A  24      30.813  12.133  92.969  1.00 45.22           C  
ANISOU  197  C   ARG A  24     5972   5222   5988     50  -1253    295       C  
ATOM    198  O   ARG A  24      29.882  11.519  92.467  1.00 47.61           O  
ANISOU  198  O   ARG A  24     6201   5527   6361     98  -1249    339       O  
ATOM    199  CB  ARG A  24      32.193  10.918  94.654  1.00 47.25           C  
ANISOU  199  CB  ARG A  24     6081   5517   6353     10  -1394    362       C  
ATOM    200  CG  ARG A  24      33.473  10.231  95.046  1.00 41.92           C  
ANISOU  200  CG  ARG A  24     5256   4890   5783    -45  -1468    390       C  
ATOM    201  CD  ARG A  24      33.374   9.811  96.491  1.00 51.15           C  
ANISOU  201  CD  ARG A  24     6373   6133   6930    -27  -1522    549       C  
ATOM    202  NE  ARG A  24      34.249   8.703  96.852  1.00 52.48           N  
ANISOU  202  NE  ARG A  24     6312   6341   7287    -35  -1560    663       N  
ATOM    203  CZ  ARG A  24      35.260   8.808  97.708  1.00 55.73           C  
ANISOU  203  CZ  ARG A  24     6647   6902   7626   -122  -1642    772       C  
ATOM    204  NH1 ARG A  24      35.519   9.982  98.278  1.00 42.71           N  
ANISOU  204  NH1 ARG A  24     5170   5358   5698   -244  -1677    720       N  
ATOM    205  NH2 ARG A  24      36.006   7.740  97.989  1.00 50.84           N  
ANISOU  205  NH2 ARG A  24     5778   6322   7216   -109  -1651    936       N  
ATOM    206  N   LEU A  25      30.703  13.403  93.325  1.00 34.30           N  
ANISOU  206  N   LEU A  25     4757   3823   4452     39  -1167    307       N  
ATOM    207  CA  LEU A  25      29.430  14.085  93.161  1.00 47.06           C  
ANISOU  207  CA  LEU A  25     6461   5410   6009    115  -1047    414       C  
ATOM    208  C   LEU A  25      29.193  14.456  91.709  1.00 57.48           C  
ANISOU  208  C   LEU A  25     7726   6779   7336    112   -997    402       C  
ATOM    209  O   LEU A  25      28.133  14.156  91.161  1.00 67.02           O  
ANISOU  209  O   LEU A  25     8861   8035   8569    161   -982    509       O  
ATOM    210  CB  LEU A  25      29.329  15.323  94.056  1.00 49.02           C  
ANISOU  210  CB  LEU A  25     6913   5589   6122    104   -909    439       C  
ATOM    211  CG  LEU A  25      29.286  15.025  95.551  1.00 43.07           C  
ANISOU  211  CG  LEU A  25     6226   4825   5313     95   -941    476       C  
ATOM    212  CD1 LEU A  25      29.380  16.298  96.379  1.00 42.35           C  
ANISOU  212  CD1 LEU A  25     6361   4667   5063     25   -778    435       C  
ATOM    213  CD2 LEU A  25      28.018  14.300  95.841  1.00 35.35           C  
ANISOU  213  CD2 LEU A  25     5187   3835   4409    213   -940    620       C  
ATOM    214  N   LEU A  26      30.173  15.108  91.088  1.00 45.78           N  
ANISOU  214  N   LEU A  26     6263   5310   5822     45   -974    289       N  
ATOM    215  CA  LEU A  26      30.059  15.470  89.684  1.00 43.80           C  
ANISOU  215  CA  LEU A  26     5940   5139   5564     35   -930    283       C  
ATOM    216  C   LEU A  26      29.629  14.244  88.888  1.00 54.37           C  
ANISOU  216  C   LEU A  26     7117   6569   6973     14  -1025    267       C  
ATOM    217  O   LEU A  26      28.728  14.307  88.052  1.00 63.38           O  
ANISOU  217  O   LEU A  26     8185   7818   8078     18   -992    360       O  
ATOM    218  CB  LEU A  26      31.391  15.990  89.160  1.00 44.92           C  
ANISOU  218  CB  LEU A  26     6092   5281   5696    -37   -932    139       C  
ATOM    219  CG  LEU A  26      31.900  17.304  89.740  1.00 42.75           C  
ANISOU  219  CG  LEU A  26     5973   4921   5350    -55   -816    121       C  
ATOM    220  CD1 LEU A  26      33.172  17.711  89.020  1.00 46.83           C  
ANISOU  220  CD1 LEU A  26     6464   5453   5876   -123   -833     -8       C  
ATOM    221  CD2 LEU A  26      30.833  18.384  89.611  1.00 28.90           C  
ANISOU  221  CD2 LEU A  26     4289   3135   3557     22   -617    275       C  
ATOM    222  N   GLY A  27      30.275  13.120  89.167  1.00 46.31           N  
ANISOU  222  N   GLY A  27     6028   5512   6056    -23  -1126    160       N  
ATOM    223  CA  GLY A  27      29.900  11.862  88.564  1.00 43.41           C  
ANISOU  223  CA  GLY A  27     5524   5186   5784    -62  -1177    113       C  
ATOM    224  C   GLY A  27      28.434  11.548  88.784  1.00 53.99           C  
ANISOU  224  C   GLY A  27     6837   6562   7113    -11  -1173    263       C  
ATOM    225  O   GLY A  27      27.733  11.223  87.831  1.00 55.64           O  
ANISOU  225  O   GLY A  27     6958   6887   7297    -71  -1174    270       O  
ATOM    226  N   LYS A  28      27.963  11.635  90.029  1.00 54.71           N  
ANISOU  226  N   LYS A  28     7000   6574   7213     83  -1170    389       N  
ATOM    227  CA  LYS A  28      26.563  11.331  90.293  1.00 46.90           C  
ANISOU  227  CA  LYS A  28     5989   5594   6238    117  -1123    526       C  
ATOM    228  C   LYS A  28      25.636  12.334  89.623  1.00 46.13           C  
ANISOU  228  C   LYS A  28     5903   5598   6027    128  -1026    673       C  
ATOM    229  O   LYS A  28      24.627  11.940  89.059  1.00 46.51           O  
ANISOU  229  O   LYS A  28     5850   5749   6073    101  -1030    772       O  
ATOM    230  CB  LYS A  28      26.230  11.200  91.785  1.00 38.52           C  
ANISOU  230  CB  LYS A  28     4990   4437   5210    171  -1080    583       C  
ATOM    231  CG  LYS A  28      25.317   9.988  92.028  1.00 43.20           C  
ANISOU  231  CG  LYS A  28     5473   5021   5919    175  -1101    632       C  
ATOM    232  CD  LYS A  28      24.161  10.262  92.947  1.00 54.57           C  
ANISOU  232  CD  LYS A  28     6945   6459   7330    229  -1007    765       C  
ATOM    233  CE  LYS A  28      23.022   9.273  92.700  1.00 53.25           C  
ANISOU  233  CE  LYS A  28     6655   6321   7257    217  -1023    847       C  
ATOM    234  NZ  LYS A  28      22.190   9.686  91.541  1.00 59.52           N  
ANISOU  234  NZ  LYS A  28     7399   7233   7983    184  -1003    954       N  
ATOM    235  N   PHE A  29      25.971  13.622  89.674  1.00 43.30           N  
ANISOU  235  N   PHE A  29     5649   5219   5585    164   -931    711       N  
ATOM    236  CA  PHE A  29      25.157  14.624  88.996  1.00 46.47           C  
ANISOU  236  CA  PHE A  29     6024   5716   5916    190   -800    891       C  
ATOM    237  C   PHE A  29      25.067  14.272  87.522  1.00 46.30           C  
ANISOU  237  C   PHE A  29     5851   5900   5842    108   -888    902       C  
ATOM    238  O   PHE A  29      24.005  14.376  86.917  1.00 45.51           O  
ANISOU  238  O   PHE A  29     5638   5954   5701     89   -845   1088       O  
ATOM    239  CB  PHE A  29      25.758  16.026  89.091  1.00 59.66           C  
ANISOU  239  CB  PHE A  29     7823   7312   7533    237   -668    911       C  
ATOM    240  CG  PHE A  29      25.999  16.514  90.486  1.00 57.33           C  
ANISOU  240  CG  PHE A  29     7706   6840   7236    282   -580    872       C  
ATOM    241  CD1 PHE A  29      26.835  17.592  90.703  1.00 56.66           C  
ANISOU  241  CD1 PHE A  29     7781   6641   7107    282   -483    833       C  
ATOM    242  CD2 PHE A  29      25.401  15.913  91.570  1.00 48.77           C  
ANISOU  242  CD2 PHE A  29     6637   5709   6183    308   -589    880       C  
ATOM    243  CE1 PHE A  29      27.071  18.050  91.973  1.00 56.60           C  
ANISOU  243  CE1 PHE A  29     7958   6485   7064    280   -398    786       C  
ATOM    244  CE2 PHE A  29      25.639  16.379  92.840  1.00 46.73           C  
ANISOU  244  CE2 PHE A  29     6552   5323   5881    333   -517    851       C  
ATOM    245  CZ  PHE A  29      26.475  17.440  93.041  1.00 46.58           C  
ANISOU  245  CZ  PHE A  29     6711   5193   5796    310   -426    807       C  
ATOM    246  N   GLY A  30      26.200  13.890  86.940  1.00 44.70           N  
ANISOU  246  N   GLY A  30     5624   5719   5642     20   -974    676       N  
ATOM    247  CA  GLY A  30      26.224  13.461  85.560  1.00 37.85           C  
ANISOU  247  CA  GLY A  30     4614   5052   4716   -115  -1022    596       C  
ATOM    248  C   GLY A  30      25.170  12.406  85.324  1.00 41.83           C  
ANISOU  248  C   GLY A  30     5003   5669   5223   -189  -1094    646       C  
ATOM    249  O   GLY A  30      24.348  12.535  84.413  1.00 43.93           O  
ANISOU  249  O   GLY A  30     5147   6168   5377   -270  -1092    781       O  
ATOM    250  N   ASP A  31      25.188  11.363  86.151  1.00 38.81           N  
ANISOU  250  N   ASP A  31     4641   5137   4969   -170  -1154    556       N  
ATOM    251  CA  ASP A  31      24.185  10.292  86.088  1.00 36.03           C  
ANISOU  251  CA  ASP A  31     4186   4848   4654   -235  -1210    593       C  
ATOM    252  C   ASP A  31      22.737  10.772  86.267  1.00 42.68           C  
ANISOU  252  C   ASP A  31     4992   5797   5429   -167  -1185    914       C  
ATOM    253  O   ASP A  31      21.827  10.276  85.620  1.00 44.35           O  
ANISOU  253  O   ASP A  31     5073   6196   5582   -280  -1232    993       O  
ATOM    254  CB  ASP A  31      24.510   9.194  87.097  1.00 27.13           C  
ANISOU  254  CB  ASP A  31     3081   3511   3718   -185  -1247    481       C  
ATOM    255  CG  ASP A  31      25.470   8.178  86.545  1.00 54.67           C  
ANISOU  255  CG  ASP A  31     6514   6948   7311   -316  -1251    198       C  
ATOM    256  OD1 ASP A  31      25.826   8.300  85.355  1.00 71.22           O  
ANISOU  256  OD1 ASP A  31     8572   9179   9311   -460  -1233     66       O  
ATOM    257  OD2 ASP A  31      25.862   7.252  87.286  1.00 59.23           O  
ANISOU  257  OD2 ASP A  31     7074   7352   8077   -274  -1252    125       O  
ATOM    258  N   GLU A  32      22.540  11.744  87.146  1.00 41.03           N  
ANISOU  258  N   GLU A  32     4895   5450   5244    -26  -1049   1067       N  
ATOM    259  CA  GLU A  32      21.219  12.283  87.389  1.00 37.10           C  
ANISOU  259  CA  GLU A  32     4349   5008   4741     24   -928   1343       C  
ATOM    260  C   GLU A  32      20.672  13.065  86.193  1.00 38.78           C  
ANISOU  260  C   GLU A  32     4424   5486   4823    -31   -885   1561       C  
ATOM    261  O   GLU A  32      19.474  13.034  85.949  1.00 47.67           O  
ANISOU  261  O   GLU A  32     5412   6768   5931    -58   -857   1804       O  
ATOM    262  CB  GLU A  32      21.191  13.131  88.674  1.00 36.60           C  
ANISOU  262  CB  GLU A  32     4412   4750   4743    164   -764   1379       C  
ATOM    263  CG  GLU A  32      21.252  12.320  89.959  1.00 38.33           C  
ANISOU  263  CG  GLU A  32     4704   4796   5062    203   -794   1261       C  
ATOM    264  CD  GLU A  32      21.626  13.162  91.153  1.00 50.21           C  
ANISOU  264  CD  GLU A  32     6359   6158   6559    300   -674   1221       C  
ATOM    265  OE1 GLU A  32      22.223  12.616  92.101  1.00 49.10           O  
ANISOU  265  OE1 GLU A  32     6292   5909   6454    306   -733   1083       O  
ATOM    266  OE2 GLU A  32      21.346  14.378  91.139  1.00 51.02           O  
ANISOU  266  OE2 GLU A  32     6501   6266   6619    368   -513   1342       O  
ATOM    267  N   VAL A  33      21.532  13.769  85.461  1.00 33.76           N  
ANISOU  267  N   VAL A  33     3802   4923   4101    -49   -877   1501       N  
ATOM    268  CA  VAL A  33      21.087  14.540  84.301  1.00 39.39           C  
ANISOU  268  CA  VAL A  33     4356   5922   4687   -101   -827   1732       C  
ATOM    269  C   VAL A  33      21.382  13.796  83.006  1.00 46.19           C  
ANISOU  269  C   VAL A  33     5088   7074   5388   -310  -1004   1582       C  
ATOM    270  O   VAL A  33      21.347  14.379  81.910  1.00 31.50           O  
ANISOU  270  O   VAL A  33     3090   5484   3393   -396   -974   1695       O  
ATOM    271  CB  VAL A  33      21.736  15.927  84.222  1.00 39.00           C  
ANISOU  271  CB  VAL A  33     4368   5806   4646      8   -665   1791       C  
ATOM    272  CG1 VAL A  33      21.366  16.759  85.440  1.00 37.75           C  
ANISOU  272  CG1 VAL A  33     4312   5398   4634    179   -451   1895       C  
ATOM    273  CG2 VAL A  33      23.239  15.793  84.072  1.00 46.39           C  
ANISOU  273  CG2 VAL A  33     5426   6643   5557    -23   -761   1472       C  
ATOM    274  N   ASN A  34      21.711  12.514  83.134  1.00 41.17           N  
ANISOU  274  N   ASN A  34     4479   6362   4802   -421  -1121   1293       N  
ATOM    275  CA  ASN A  34      22.021  11.651  81.990  1.00 45.75           C  
ANISOU  275  CA  ASN A  34     4961   7140   5283   -672  -1205   1036       C  
ATOM    276  C   ASN A  34      23.186  12.045  81.060  1.00 46.19           C  
ANISOU  276  C   ASN A  34     5014   7284   5251   -748  -1174    859       C  
ATOM    277  O   ASN A  34      23.077  11.886  79.844  1.00 48.05           O  
ANISOU  277  O   ASN A  34     5108   7841   5307   -938  -1197    863       O  
ATOM    278  CB  ASN A  34      20.758  11.419  81.153  1.00 38.61           C  
ANISOU  278  CB  ASN A  34     3861   6590   4219   -858  -1266   1224       C  
ATOM    279  CG  ASN A  34      20.985  10.447  80.012  1.00 65.66           C  
ANISOU  279  CG  ASN A  34     7230  10132   7586  -1147  -1347    892       C  
ATOM    280  OD1 ASN A  34      22.046   9.832  79.906  1.00 79.90           O  
ANISOU  280  OD1 ASN A  34     8881  12300   9178  -1393  -1387    909       O  
ATOM    281  ND2 ASN A  34      19.985  10.303  79.150  1.00 74.15           N  
ANISOU  281  ND2 ASN A  34     8420  10903   8852  -1130  -1349    597       N  
ATOM    282  N   MET A  35      24.292  12.541  81.613  1.00 33.95           N  
ANISOU  282  N   MET A  35     3611   5472   3816   -617  -1127    709       N  
ATOM    283  CA  MET A  35      25.462  12.863  80.787  1.00 39.59           C  
ANISOU  283  CA  MET A  35     4334   6226   4482   -681  -1103    513       C  
ATOM    284  C   MET A  35      26.724  12.190  81.334  1.00 42.53           C  
ANISOU  284  C   MET A  35     4835   6305   5018   -660  -1116    201       C  
ATOM    285  O   MET A  35      26.958  12.210  82.529  1.00 39.08           O  
ANISOU  285  O   MET A  35     4511   5620   4719   -514  -1112    218       O  
ATOM    286  CB  MET A  35      25.734  14.367  80.735  1.00 37.50           C  
ANISOU  286  CB  MET A  35     4086   5971   4192   -533   -999    714       C  
ATOM    287  CG  MET A  35      24.540  15.293  80.691  1.00 40.08           C  
ANISOU  287  CG  MET A  35     4311   6466   4453   -448   -917   1121       C  
ATOM    288  SD  MET A  35      25.095  17.012  80.569  1.00 48.41           S  
ANISOU  288  SD  MET A  35     5387   7469   5537   -281   -733   1302       S  
ATOM    289  CE  MET A  35      23.570  17.884  80.821  1.00 42.26           C  
ANISOU  289  CE  MET A  35     4498   6795   4765   -152   -585   1814       C  
ATOM    290  N   PRO A  36      27.545  11.598  80.454  1.00 46.01           N  
ANISOU  290  N   PRO A  36     5250   6790   5440   -813  -1119    -63       N  
ATOM    291  CA  PRO A  36      28.887  11.160  80.850  1.00 43.80           C  
ANISOU  291  CA  PRO A  36     5067   6246   5330   -775  -1101   -298       C  
ATOM    292  C   PRO A  36      29.686  12.336  81.356  1.00 46.36           C  
ANISOU  292  C   PRO A  36     5482   6448   5685   -609  -1071   -214       C  
ATOM    293  O   PRO A  36      29.726  13.357  80.663  1.00 50.14           O  
ANISOU  293  O   PRO A  36     5926   7079   6045   -597  -1032   -114       O  
ATOM    294  CB  PRO A  36      29.501  10.691  79.535  1.00 43.33           C  
ANISOU  294  CB  PRO A  36     4959   6305   5199   -957  -1048   -524       C  
ATOM    295  CG  PRO A  36      28.347  10.305  78.695  1.00 42.72           C  
ANISOU  295  CG  PRO A  36     4763   6527   4940  -1153  -1075   -493       C  
ATOM    296  CD  PRO A  36      27.208  11.182  79.085  1.00 46.91           C  
ANISOU  296  CD  PRO A  36     5237   7208   5377  -1052  -1130   -153       C  
ATOM    297  N   VAL A  37      30.292  12.200  82.535  1.00 32.25           N  
ANISOU  297  N   VAL A  37     3794   4408   4050   -497  -1083   -242       N  
ATOM    298  CA  VAL A  37      31.185  13.220  83.058  1.00 34.22           C  
ANISOU  298  CA  VAL A  37     4139   4538   4324   -388  -1056   -209       C  
ATOM    299  C   VAL A  37      32.659  12.755  83.035  1.00 47.75           C  
ANISOU  299  C   VAL A  37     5874   6109   6161   -413  -1058   -399       C  
ATOM    300  O   VAL A  37      32.994  11.690  83.549  1.00 51.99           O  
ANISOU  300  O   VAL A  37     6400   6511   6841   -417  -1066   -474       O  
ATOM    301  CB  VAL A  37      30.746  13.664  84.482  1.00 38.80           C  
ANISOU  301  CB  VAL A  37     4821   4984   4938   -260  -1053    -56       C  
ATOM    302  CG1 VAL A  37      31.733  14.677  85.082  1.00 43.53           C  
ANISOU  302  CG1 VAL A  37     5533   5460   5548   -197  -1015    -64       C  
ATOM    303  CG2 VAL A  37      29.388  14.292  84.429  1.00 29.24           C  
ANISOU  303  CG2 VAL A  37     3591   3890   3630   -210  -1001    172       C  
ATOM    304  N   TYR A  38      33.540  13.540  82.423  1.00 51.20           N  
ANISOU  304  N   TYR A  38     6324   6570   6561   -411  -1022   -439       N  
ATOM    305  CA  TYR A  38      34.974  13.227  82.471  1.00 45.57           C  
ANISOU  305  CA  TYR A  38     5629   5713   5973   -402  -1001   -554       C  
ATOM    306  C   TYR A  38      35.752  14.372  83.078  1.00 39.76           C  
ANISOU  306  C   TYR A  38     4974   4901   5231   -335  -1010   -496       C  
ATOM    307  O   TYR A  38      35.409  15.537  82.868  1.00 37.00           O  
ANISOU  307  O   TYR A  38     4653   4631   4776   -312   -986   -421       O  
ATOM    308  CB  TYR A  38      35.537  12.946  81.076  1.00 37.43           C  
ANISOU  308  CB  TYR A  38     4531   4766   4923   -487   -942   -692       C  
ATOM    309  CG  TYR A  38      34.718  11.961  80.284  1.00 39.81           C  
ANISOU  309  CG  TYR A  38     4760   5188   5177   -614   -916   -786       C  
ATOM    310  CD1 TYR A  38      33.613  12.376  79.546  1.00 31.11           C  
ANISOU  310  CD1 TYR A  38     3601   4336   3883   -688   -931   -717       C  
ATOM    311  CD2 TYR A  38      35.057  10.618  80.256  1.00 42.80           C  
ANISOU  311  CD2 TYR A  38     5109   5447   5705   -682   -866   -938       C  
ATOM    312  CE1 TYR A  38      32.878  11.482  78.814  1.00 31.74           C  
ANISOU  312  CE1 TYR A  38     3610   4562   3888   -848   -915   -812       C  
ATOM    313  CE2 TYR A  38      34.322   9.720  79.529  1.00 37.35           C  
ANISOU  313  CE2 TYR A  38     4365   4859   4968   -837   -822  -1062       C  
ATOM    314  CZ  TYR A  38      33.233  10.153  78.813  1.00 37.47           C  
ANISOU  314  CZ  TYR A  38     4337   5143   4757   -931   -856  -1007       C  
ATOM    315  OH  TYR A  38      32.491   9.238  78.101  1.00 44.47           O  
ANISOU  315  OH  TYR A  38     5165   6164   5568  -1129   -820  -1139       O  
ATOM    316  N   VAL A  39      36.790  14.043  83.840  1.00 36.41           N  
ANISOU  316  N   VAL A  39     4572   4337   4924   -314  -1034   -516       N  
ATOM    317  CA  VAL A  39      37.822  15.029  84.132  1.00 40.71           C  
ANISOU  317  CA  VAL A  39     5175   4834   5460   -297  -1036   -501       C  
ATOM    318  C   VAL A  39      38.948  14.805  83.142  1.00 41.10           C  
ANISOU  318  C   VAL A  39     5159   4876   5583   -317  -1004   -587       C  
ATOM    319  O   VAL A  39      39.264  13.669  82.799  1.00 46.20           O  
ANISOU  319  O   VAL A  39     5731   5483   6341   -346   -991   -657       O  
ATOM    320  CB  VAL A  39      38.362  14.946  85.551  1.00 41.51           C  
ANISOU  320  CB  VAL A  39     5322   4843   5607   -297  -1099   -445       C  
ATOM    321  CG1 VAL A  39      39.037  13.606  85.792  1.00 37.74           C  
ANISOU  321  CG1 VAL A  39     4741   4302   5296   -315  -1139   -457       C  
ATOM    322  CG2 VAL A  39      39.338  16.055  85.744  1.00 42.07           C  
ANISOU  322  CG2 VAL A  39     5455   4893   5636   -320  -1094   -444       C  
ATOM    323  N   VAL A  40      39.530  15.886  82.646  1.00 45.59           N  
ANISOU  323  N   VAL A  40     5751   5470   6101   -310   -978   -592       N  
ATOM    324  CA  VAL A  40      40.473  15.763  81.533  1.00 47.83           C  
ANISOU  324  CA  VAL A  40     5970   5764   6438   -325   -942   -673       C  
ATOM    325  C   VAL A  40      41.653  16.706  81.608  1.00 44.26           C  
ANISOU  325  C   VAL A  40     5544   5258   6013   -311   -950   -654       C  
ATOM    326  O   VAL A  40      41.711  17.589  82.458  1.00 54.50           O  
ANISOU  326  O   VAL A  40     6919   6523   7267   -309   -970   -597       O  
ATOM    327  CB  VAL A  40      39.791  16.011  80.167  1.00 42.70           C  
ANISOU  327  CB  VAL A  40     5268   5280   5675   -355   -889   -721       C  
ATOM    328  CG1 VAL A  40      38.815  14.873  79.799  1.00 34.31           C  
ANISOU  328  CG1 VAL A  40     4157   4294   4584   -418   -875   -778       C  
ATOM    329  CG2 VAL A  40      39.113  17.348  80.167  1.00 29.48           C  
ANISOU  329  CG2 VAL A  40     3621   3701   3880   -327   -882   -628       C  
ATOM    330  N   GLY A  41      42.597  16.491  80.698  1.00 50.14           N  
ANISOU  330  N   GLY A  41     6227   5991   6832   -319   -924   -717       N  
ATOM    331  CA  GLY A  41      43.791  17.315  80.577  1.00 52.26           C  
ANISOU  331  CA  GLY A  41     6500   6212   7144   -310   -932   -701       C  
ATOM    332  C   GLY A  41      44.841  17.247  81.680  1.00 50.94           C  
ANISOU  332  C   GLY A  41     6344   5942   7070   -337  -1007   -631       C  
ATOM    333  O   GLY A  41      45.261  16.165  82.147  1.00 37.50           O  
ANISOU  333  O   GLY A  41     4583   4176   5490   -366  -1047   -606       O  
ATOM    334  N   GLY A  42      45.249  18.437  82.106  1.00 50.20           N  
ANISOU  334  N   GLY A  42     6311   5841   6920   -353  -1022   -596       N  
ATOM    335  CA  GLY A  42      46.391  18.600  82.979  1.00 35.93           C  
ANISOU  335  CA  GLY A  42     4502   3985   5164   -422  -1102   -532       C  
ATOM    336  C   GLY A  42      46.285  17.836  84.272  1.00 44.58           C  
ANISOU  336  C   GLY A  42     5594   5082   6264   -483  -1187   -458       C  
ATOM    337  O   GLY A  42      47.283  17.307  84.731  1.00 46.30           O  
ANISOU  337  O   GLY A  42     5723   5284   6583   -549  -1268   -376       O  
ATOM    338  N   PHE A  43      45.096  17.782  84.872  1.00 46.91           N  
ANISOU  338  N   PHE A  43     5960   5406   6459   -472  -1174   -465       N  
ATOM    339  CA  PHE A  43      44.956  17.098  86.154  1.00 40.94           C  
ANISOU  339  CA  PHE A  43     5192   4667   5697   -533  -1259   -388       C  
ATOM    340  C   PHE A  43      45.213  15.610  85.981  1.00 45.35           C  
ANISOU  340  C   PHE A  43     5601   5190   6440   -516  -1290   -346       C  
ATOM    341  O   PHE A  43      45.768  14.947  86.864  1.00 34.68           O  
ANISOU  341  O   PHE A  43     4148   3859   5171   -585  -1379   -231       O  
ATOM    342  CB  PHE A  43      43.570  17.312  86.772  1.00 42.17           C  
ANISOU  342  CB  PHE A  43     5453   4845   5725   -515  -1228   -404       C  
ATOM    343  CG  PHE A  43      43.297  16.405  87.945  1.00 40.27           C  
ANISOU  343  CG  PHE A  43     5175   4631   5495   -557  -1314   -324       C  
ATOM    344  CD1 PHE A  43      43.552  16.829  89.237  1.00 51.06           C  
ANISOU  344  CD1 PHE A  43     6597   6058   6744   -677  -1383   -275       C  
ATOM    345  CD2 PHE A  43      42.835  15.107  87.753  1.00 40.88           C  
ANISOU  345  CD2 PHE A  43     5147   4684   5701   -498  -1322   -303       C  
ATOM    346  CE1 PHE A  43      43.337  15.979  90.326  1.00 55.88           C  
ANISOU  346  CE1 PHE A  43     7142   6731   7357   -719  -1473   -177       C  
ATOM    347  CE2 PHE A  43      42.622  14.253  88.830  1.00 46.85           C  
ANISOU  347  CE2 PHE A  43     5834   5469   6497   -529  -1400   -208       C  
ATOM    348  CZ  PHE A  43      42.871  14.693  90.119  1.00 52.56           C  
ANISOU  348  CZ  PHE A  43     6596   6279   7094   -629  -1483   -130       C  
ATOM    349  N   VAL A  44      44.799  15.076  84.836  1.00 40.64           N  
ANISOU  349  N   VAL A  44     4971   4555   5916   -445  -1204   -434       N  
ATOM    350  CA  VAL A  44      44.919  13.658  84.642  1.00 31.25           C  
ANISOU  350  CA  VAL A  44     3653   3295   4925   -453  -1182   -432       C  
ATOM    351  C   VAL A  44      46.378  13.381  84.527  1.00 41.29           C  
ANISOU  351  C   VAL A  44     4815   4508   6366   -465  -1172   -332       C  
ATOM    352  O   VAL A  44      46.894  12.411  85.066  1.00 58.48           O  
ANISOU  352  O   VAL A  44     6861   6636   8721   -465  -1161   -192       O  
ATOM    353  CB  VAL A  44      44.167  13.191  83.411  1.00 32.65           C  
ANISOU  353  CB  VAL A  44     3839   3458   5109   -414  -1067   -576       C  
ATOM    354  CG1 VAL A  44      44.358  11.686  83.216  1.00 32.87           C  
ANISOU  354  CG1 VAL A  44     3753   3371   5367   -422   -973   -587       C  
ATOM    355  CG2 VAL A  44      42.688  13.520  83.579  1.00 32.50           C  
ANISOU  355  CG2 VAL A  44     3910   3529   4910   -376  -1063   -597       C  
ATOM    356  N   ARG A  45      47.055  14.279  83.840  1.00 41.71           N  
ANISOU  356  N   ARG A  45     4904   4567   6377   -467  -1167   -373       N  
ATOM    357  CA  ARG A  45      48.481  14.152  83.643  1.00 35.99           C  
ANISOU  357  CA  ARG A  45     4076   3787   5810   -473  -1157   -261       C  
ATOM    358  C   ARG A  45      49.237  14.259  84.968  1.00 47.82           C  
ANISOU  358  C   ARG A  45     5502   5356   7312   -553  -1284    -55       C  
ATOM    359  O   ARG A  45      50.069  13.408  85.286  1.00 54.91           O  
ANISOU  359  O   ARG A  45     6239   6221   8405   -554  -1270    135       O  
ATOM    360  CB  ARG A  45      48.973  15.229  82.689  1.00 24.98           C  
ANISOU  360  CB  ARG A  45     2741   2399   4350   -456  -1136   -343       C  
ATOM    361  CG  ARG A  45      50.486  15.283  82.629  1.00 36.63           C  
ANISOU  361  CG  ARG A  45     4115   3829   5973   -467  -1149   -197       C  
ATOM    362  CD  ARG A  45      50.947  16.633  82.187  1.00 38.42           C  
ANISOU  362  CD  ARG A  45     4410   4090   6097   -475  -1179   -244       C  
ATOM    363  NE  ARG A  45      50.528  17.695  83.087  1.00 30.56           N  
ANISOU  363  NE  ARG A  45     3520   3185   4905   -558  -1272   -267       N  
ATOM    364  CZ  ARG A  45      50.046  18.864  82.684  1.00 33.70           C  
ANISOU  364  CZ  ARG A  45     4029   3603   5171   -543  -1234   -384       C  
ATOM    365  NH1 ARG A  45      49.901  19.110  81.394  1.00 34.25           N  
ANISOU  365  NH1 ARG A  45     4098   3652   5263   -444  -1134   -467       N  
ATOM    366  NH2 ARG A  45      49.714  19.787  83.570  1.00 24.81           N  
ANISOU  366  NH2 ARG A  45     3013   2524   3888   -610  -1255   -393       N  
ATOM    367  N   ASP A  46      48.958  15.308  85.733  1.00 38.39           N  
ANISOU  367  N   ASP A  46     4417   4267   5902   -635  -1389    -79       N  
ATOM    368  CA  ASP A  46      49.654  15.516  86.986  1.00 55.79           C  
ANISOU  368  CA  ASP A  46     6563   6589   8047   -763  -1518     91       C  
ATOM    369  C   ASP A  46      49.335  14.423  88.016  1.00 60.86           C  
ANISOU  369  C   ASP A  46     7090   7289   8746   -776  -1558    249       C  
ATOM    370  O   ASP A  46      50.204  14.013  88.783  1.00 55.97           O  
ANISOU  370  O   ASP A  46     6308   6765   8193   -850  -1633    484       O  
ATOM    371  CB  ASP A  46      49.366  16.912  87.533  1.00 60.08           C  
ANISOU  371  CB  ASP A  46     7279   7213   8337   -877  -1575    -20       C  
ATOM    372  CG  ASP A  46      49.939  18.002  86.657  1.00 63.12           C  
ANISOU  372  CG  ASP A  46     7735   7545   8704   -864  -1523   -110       C  
ATOM    373  OD1 ASP A  46      50.918  17.719  85.937  1.00 68.96           O  
ANISOU  373  OD1 ASP A  46     8357   8237   9609   -828  -1516    -38       O  
ATOM    374  OD2 ASP A  46      49.419  19.139  86.685  1.00 56.86           O  
ANISOU  374  OD2 ASP A  46     7108   6747   7751   -875  -1459   -232       O  
ATOM    375  N   LEU A  47      48.101  13.935  88.020  1.00 58.48           N  
ANISOU  375  N   LEU A  47     6848   6945   8428   -702  -1506    150       N  
ATOM    376  CA  LEU A  47      47.724  12.884  88.951  1.00 54.64           C  
ANISOU  376  CA  LEU A  47     6244   6499   8016   -693  -1528    300       C  
ATOM    377  C   LEU A  47      48.630  11.683  88.797  1.00 54.84           C  
ANISOU  377  C   LEU A  47     6034   6458   8344   -642  -1456    512       C  
ATOM    378  O   LEU A  47      49.067  11.094  89.779  1.00 55.63           O  
ANISOU  378  O   LEU A  47     5959   6660   8519   -680  -1510    767       O  
ATOM    379  CB  LEU A  47      46.275  12.424  88.735  1.00 46.59           C  
ANISOU  379  CB  LEU A  47     5308   5409   6984   -602  -1458    157       C  
ATOM    380  CG  LEU A  47      45.983  11.151  89.548  1.00 39.91           C  
ANISOU  380  CG  LEU A  47     4304   4569   6290   -565  -1448    328       C  
ATOM    381  CD1 LEU A  47      45.784  11.481  91.045  1.00 45.51           C  
ANISOU  381  CD1 LEU A  47     5019   5463   6811   -657  -1589    457       C  
ATOM    382  CD2 LEU A  47      44.817  10.343  89.018  1.00 39.30           C  
ANISOU  382  CD2 LEU A  47     4252   4373   6309   -468  -1337    202       C  
ATOM    383  N   LEU A  48      48.881  11.303  87.552  1.00 55.00           N  
ANISOU  383  N   LEU A  48     6041   6310   8545   -556  -1310    420       N  
ATOM    384  CA  LEU A  48      49.700  10.137  87.262  1.00 55.15           C  
ANISOU  384  CA  LEU A  48     5854   6206   8896   -493  -1167    603       C  
ATOM    385  C   LEU A  48      51.192  10.396  87.509  1.00 57.24           C  
ANISOU  385  C   LEU A  48     5969   6536   9242   -546  -1222    861       C  
ATOM    386  O   LEU A  48      51.977   9.459  87.607  1.00 61.13           O  
ANISOU  386  O   LEU A  48     6242   6964  10020   -503  -1115   1121       O  
ATOM    387  CB  LEU A  48      49.447   9.672  85.823  1.00 43.74           C  
ANISOU  387  CB  LEU A  48     4472   4557   7592   -414   -965    383       C  
ATOM    388  CG  LEU A  48      48.063   9.088  85.534  1.00 42.34           C  
ANISOU  388  CG  LEU A  48     4380   4316   7392   -382   -882    175       C  
ATOM    389  CD1 LEU A  48      47.742   9.079  84.059  1.00 42.56           C  
ANISOU  389  CD1 LEU A  48     4518   4240   7413   -371   -739    -95       C  
ATOM    390  CD2 LEU A  48      48.031   7.687  86.059  1.00 51.14           C  
ANISOU  390  CD2 LEU A  48     5314   5326   8791   -337   -750    341       C  
ATOM    391  N   LEU A  49      51.575  11.669  87.611  1.00 51.72           N  
ANISOU  391  N   LEU A  49     5379   5963   8311   -643  -1371    807       N  
ATOM    392  CA  LEU A  49      52.963  12.043  87.876  1.00 44.58           C  
ANISOU  392  CA  LEU A  49     4340   5154   7444   -725  -1452   1047       C  
ATOM    393  C   LEU A  49      53.186  12.379  89.341  1.00 47.84           C  
ANISOU  393  C   LEU A  49     4675   5837   7665   -895  -1650   1247       C  
ATOM    394  O   LEU A  49      54.307  12.641  89.771  1.00 52.15           O  
ANISOU  394  O   LEU A  49     5078   6528   8207  -1008  -1747   1488       O  
ATOM    395  CB  LEU A  49      53.370  13.257  87.050  1.00 32.13           C  
ANISOU  395  CB  LEU A  49     2916   3550   5743   -751  -1480    866       C  
ATOM    396  CG  LEU A  49      53.597  13.128  85.553  1.00 31.87           C  
ANISOU  396  CG  LEU A  49     2923   3309   5877   -620  -1309    728       C  
ATOM    397  CD1 LEU A  49      54.128  14.454  85.007  1.00 30.61           C  
ANISOU  397  CD1 LEU A  49     2873   3176   5580   -661  -1373    622       C  
ATOM    398  CD2 LEU A  49      54.530  11.991  85.231  1.00 24.20           C  
ANISOU  398  CD2 LEU A  49     1738   2205   5253   -540  -1155    973       C  
ATOM    399  N   GLY A  50      52.110  12.390  90.106  1.00 42.91           N  
ANISOU  399  N   GLY A  50     4144   5298   6862   -928  -1709   1149       N  
ATOM    400  CA  GLY A  50      52.196  12.691  91.517  1.00 47.10           C  
ANISOU  400  CA  GLY A  50     4622   6103   7171  -1109  -1883   1305       C  
ATOM    401  C   GLY A  50      52.284  14.177  91.789  1.00 58.56           C  
ANISOU  401  C   GLY A  50     6278   7675   8297  -1294  -2004   1118       C  
ATOM    402  O   GLY A  50      52.676  14.573  92.883  1.00 64.27           O  
ANISOU  402  O   GLY A  50     6955   8651   8812  -1506  -2149   1242       O  
ATOM    403  N   ILE A  51      51.928  14.994  90.796  1.00 57.96           N  
ANISOU  403  N   ILE A  51     6417   7427   8178  -1228  -1927    826       N  
ATOM    404  CA  ILE A  51      51.886  16.444  90.968  1.00 52.14           C  
ANISOU  404  CA  ILE A  51     5891   6747   7174  -1382  -1978    621       C  
ATOM    405  C   ILE A  51      50.502  16.936  91.362  1.00 56.22           C  
ANISOU  405  C   ILE A  51     6633   7240   7488  -1385  -1938    389       C  
ATOM    406  O   ILE A  51      49.487  16.422  90.888  1.00 66.49           O  
ANISOU  406  O   ILE A  51     7983   8409   8873  -1213  -1845    296       O  
ATOM    407  CB  ILE A  51      52.295  17.201  89.694  1.00 49.01           C  
ANISOU  407  CB  ILE A  51     5583   6186   6853  -1304  -1895    468       C  
ATOM    408  CG1 ILE A  51      53.784  17.019  89.377  1.00 53.21           C  
ANISOU  408  CG1 ILE A  51     5920   6747   7550  -1334  -1938    695       C  
ATOM    409  CG2 ILE A  51      52.021  18.661  89.865  1.00 34.49           C  
ANISOU  409  CG2 ILE A  51     3970   4359   4776  -1430  -1886    245       C  
ATOM    410  CD1 ILE A  51      54.097  15.800  88.535  1.00 52.31           C  
ANISOU  410  CD1 ILE A  51     5634   6481   7759  -1134  -1826    841       C  
ATOM    411  N   LYS A  52      50.471  17.951  92.218  1.00 54.41           N  
ANISOU  411  N   LYS A  52     6551   7131   6991  -1587  -1980    301       N  
ATOM    412  CA  LYS A  52      49.225  18.560  92.663  1.00 60.51           C  
ANISOU  412  CA  LYS A  52     7561   7859   7572  -1594  -1889    104       C  
ATOM    413  C   LYS A  52      48.656  19.487  91.576  1.00 64.53           C  
ANISOU  413  C   LYS A  52     8257   8154   8107  -1455  -1714   -116       C  
ATOM    414  O   LYS A  52      49.401  20.163  90.857  1.00 67.79           O  
ANISOU  414  O   LYS A  52     8679   8509   8570  -1463  -1682   -161       O  
ATOM    415  CB  LYS A  52      49.477  19.349  93.954  1.00 71.91           C  
ANISOU  415  CB  LYS A  52     9099   9500   8725  -1892  -1956     73       C  
ATOM    416  CG  LYS A  52      48.502  19.059  95.087  1.00 82.27           C  
ANISOU  416  CG  LYS A  52    10477  10916   9867  -1954  -1972     66       C  
ATOM    417  CD  LYS A  52      48.625  20.085  96.209  1.00 87.26           C  
ANISOU  417  CD  LYS A  52    11272  11707  10174  -2276  -1981    -56       C  
ATOM    418  CE  LYS A  52      48.140  21.467  95.766  1.00 87.81           C  
ANISOU  418  CE  LYS A  52    11624  11563  10176  -2290  -1771   -348       C  
ATOM    419  NZ  LYS A  52      47.621  22.275  96.916  1.00 85.62           N  
ANISOU  419  NZ  LYS A  52    11570  11356   9606  -2546  -1693   -525       N  
ATOM    420  N   ASN A  53      47.333  19.505  91.453  1.00 61.73           N  
ANISOU  420  N   ASN A  53     8026   7699   7728  -1326  -1602   -222       N  
ATOM    421  CA  ASN A  53      46.654  20.378  90.507  1.00 53.67           C  
ANISOU  421  CA  ASN A  53     7144   6523   6725  -1199  -1433   -377       C  
ATOM    422  C   ASN A  53      45.336  20.770  91.145  1.00 62.88           C  
ANISOU  422  C   ASN A  53     8477   7659   7757  -1204  -1335   -464       C  
ATOM    423  O   ASN A  53      44.686  19.932  91.761  1.00 70.38           O  
ANISOU  423  O   ASN A  53     9396   8657   8690  -1177  -1392   -399       O  
ATOM    424  CB  ASN A  53      46.406  19.636  89.191  1.00 47.47           C  
ANISOU  424  CB  ASN A  53     6253   5647   6136   -975  -1394   -353       C  
ATOM    425  CG  ASN A  53      46.319  20.566  87.983  1.00 53.91           C  
ANISOU  425  CG  ASN A  53     7125   6368   6992   -878  -1263   -454       C  
ATOM    426  OD1 ASN A  53      46.004  21.764  88.098  1.00 59.45           O  
ANISOU  426  OD1 ASN A  53     7961   7027   7599   -929  -1155   -549       O  
ATOM    427  ND2 ASN A  53      46.602  20.010  86.807  1.00 39.17           N  
ANISOU  427  ND2 ASN A  53     5144   4464   5273   -750  -1256   -435       N  
ATOM    428  N   LEU A  54      44.962  22.043  91.025  1.00 66.58           N  
ANISOU  428  N   LEU A  54     9114   8033   8150  -1242  -1176   -603       N  
ATOM    429  CA  LEU A  54      43.708  22.566  91.586  1.00 66.85           C  
ANISOU  429  CA  LEU A  54     9325   7995   8079  -1252  -1036   -689       C  
ATOM    430  C   LEU A  54      42.925  23.310  90.502  1.00 74.36           C  
ANISOU  430  C   LEU A  54    10335   8791   9128  -1093   -843   -744       C  
ATOM    431  O   LEU A  54      41.991  24.080  90.774  1.00 70.53           O  
ANISOU  431  O   LEU A  54    10002   8200   8595  -1082   -645   -793       O  
ATOM    432  CB  LEU A  54      43.987  23.497  92.778  1.00 60.86           C  
ANISOU  432  CB  LEU A  54     8742   7261   7121  -1521   -977   -810       C  
ATOM    433  CG  LEU A  54      44.914  22.951  93.881  1.00 64.92           C  
ANISOU  433  CG  LEU A  54     9181   7991   7494  -1746  -1180   -745       C  
ATOM    434  CD1 LEU A  54      45.328  24.034  94.887  1.00 62.98           C  
ANISOU  434  CD1 LEU A  54     9116   7794   7020  -2068  -1108   -905       C  
ATOM    435  CD2 LEU A  54      44.356  21.707  94.593  1.00 46.83           C  
ANISOU  435  CD2 LEU A  54     6796   5820   5177  -1696  -1319   -611       C  
ATOM    436  N   ASP A  55      43.347  23.086  89.265  1.00 79.95           N  
ANISOU  436  N   ASP A  55    10904   9498   9975   -959   -871   -698       N  
ATOM    437  CA  ASP A  55      42.688  23.649  88.109  1.00 77.51           C  
ANISOU  437  CA  ASP A  55    10590   9104   9756   -805   -715   -701       C  
ATOM    438  C   ASP A  55      42.188  22.449  87.333  1.00 72.77           C  
ANISOU  438  C   ASP A  55     9844   8574   9231   -656   -815   -621       C  
ATOM    439  O   ASP A  55      42.901  21.920  86.476  1.00 67.83           O  
ANISOU  439  O   ASP A  55     9085   7992   8694   -605   -895   -601       O  
ATOM    440  CB  ASP A  55      43.679  24.461  87.283  1.00 96.20           C  
ANISOU  440  CB  ASP A  55    12919  11431  12202   -812   -662   -740       C  
ATOM    441  CG  ASP A  55      43.034  25.664  86.615  1.00121.54           C  
ANISOU  441  CG  ASP A  55    16177  14537  15465   -712   -402   -732       C  
ATOM    442  OD1 ASP A  55      43.238  26.795  87.109  1.00131.60           O  
ANISOU  442  OD1 ASP A  55    17580  15701  16721   -817   -233   -810       O  
ATOM    443  OD2 ASP A  55      42.313  25.482  85.607  1.00128.15           O  
ANISOU  443  OD2 ASP A  55    16914  15414  16364   -542   -350   -638       O  
ATOM    444  N   ILE A  56      40.989  21.990  87.652  1.00 65.67           N  
ANISOU  444  N   ILE A  56     8974   7684   8295   -592   -787   -570       N  
ATOM    445  CA  ILE A  56      40.454  20.786  87.051  1.00 64.24           C  
ANISOU  445  CA  ILE A  56     8670   7571   8168   -492   -878   -513       C  
ATOM    446  C   ILE A  56      39.406  21.009  85.996  1.00 57.75           C  
ANISOU  446  C   ILE A  56     7796   6781   7365   -365   -761   -455       C  
ATOM    447  O   ILE A  56      38.441  21.686  86.215  1.00 58.79           O  
ANISOU  447  O   ILE A  56     8001   6879   7459   -319   -605   -390       O  
ATOM    448  CB  ILE A  56      39.843  19.892  88.099  1.00 20.00           C  
ATOM    449  CG1 ILE A  56      38.524  20.472  88.581  1.00 20.00           C  
ATOM    450  CG2 ILE A  56      40.776  19.753  89.268  1.00 20.00           C  
ATOM    451  CD1 ILE A  56      38.573  20.969  89.997  1.00 20.00           C  
ATOM    452  N   ASP A  57      39.632  20.384  84.852  1.00 46.33           N  
ANISOU  452  N   ASP A  57     6214   5412   5977   -323   -821   -466       N  
ATOM    453  CA  ASP A  57      38.781  20.473  83.666  1.00 41.20           C  
ANISOU  453  CA  ASP A  57     5476   4867   5312   -242   -744   -403       C  
ATOM    454  C   ASP A  57      37.826  19.284  83.597  1.00 40.72           C  
ANISOU  454  C   ASP A  57     5353   4883   5235   -234   -815   -380       C  
ATOM    455  O   ASP A  57      38.272  18.129  83.547  1.00 38.71           O  
ANISOU  455  O   ASP A  57     5042   4627   5039   -275   -921   -458       O  
ATOM    456  CB  ASP A  57      39.616  20.457  82.384  1.00 33.32           C  
ANISOU  456  CB  ASP A  57     4369   3934   4356   -234   -755   -453       C  
ATOM    457  CG  ASP A  57      40.365  21.723  82.152  1.00 56.16           C  
ANISOU  457  CG  ASP A  57     7290   6774   7276   -217   -658   -447       C  
ATOM    458  OD1 ASP A  57      40.280  22.648  82.981  1.00 72.81           O  
ANISOU  458  OD1 ASP A  57     9511   8781   9374   -231   -564   -427       O  
ATOM    459  OD2 ASP A  57      41.050  21.794  81.116  1.00 71.70           O  
ANISOU  459  OD2 ASP A  57     9168   8796   9280   -198   -658   -473       O  
ATOM    460  N   ILE A  58      36.524  19.580  83.589  1.00 31.58           N  
ANISOU  460  N   ILE A  58     4198   3783   4017   -182   -734   -258       N  
ATOM    461  CA  ILE A  58      35.482  18.592  83.333  1.00 21.01           C  
ANISOU  461  CA  ILE A  58     2782   2549   2650   -183   -788   -215       C  
ATOM    462  C   ILE A  58      34.964  18.698  81.876  1.00 31.01           C  
ANISOU  462  C   ILE A  58     3909   4023   3850   -185   -745   -153       C  
ATOM    463  O   ILE A  58      34.746  19.790  81.342  1.00 30.65           O  
ANISOU  463  O   ILE A  58     3827   4048   3772   -131   -625    -27       O  
ATOM    464  CB  ILE A  58      34.318  18.720  84.328  1.00 27.22           C  
ANISOU  464  CB  ILE A  58     3644   3291   3408   -136   -743    -87       C  
ATOM    465  CG1 ILE A  58      34.588  17.959  85.634  1.00 33.46           C  
ANISOU  465  CG1 ILE A  58     4515   3960   4238   -165   -842   -154       C  
ATOM    466  CG2 ILE A  58      33.062  18.109  83.746  1.00 30.96           C  
ANISOU  466  CG2 ILE A  58     4009   3918   3835   -129   -757     19       C  
ATOM    467  CD1 ILE A  58      35.987  17.885  86.037  1.00 39.31           C  
ANISOU  467  CD1 ILE A  58     5287   4622   5026   -226   -912   -275       C  
ATOM    468  N   VAL A  59      34.799  17.559  81.218  1.00 22.14           N  
ANISOU  468  N   VAL A  59     2695   3009   2709   -261   -827   -239       N  
ATOM    469  CA  VAL A  59      34.062  17.539  79.967  1.00 30.29           C  
ANISOU  469  CA  VAL A  59     3590   4295   3625   -309   -801   -170       C  
ATOM    470  C   VAL A  59      32.791  16.701  80.121  1.00 34.38           C  
ANISOU  470  C   VAL A  59     4062   4912   4090   -360   -848   -107       C  
ATOM    471  O   VAL A  59      32.841  15.560  80.583  1.00 36.76           O  
ANISOU  471  O   VAL A  59     4393   5118   4458   -413   -922   -239       O  
ATOM    472  CB  VAL A  59      34.904  16.940  78.847  1.00 35.06           C  
ANISOU  472  CB  VAL A  59     4124   4984   4215   -408   -832   -351       C  
ATOM    473  CG1 VAL A  59      34.141  17.007  77.536  1.00 29.94           C  
ANISOU  473  CG1 VAL A  59     3323   4654   3397   -492   -807   -275       C  
ATOM    474  CG2 VAL A  59      36.232  17.650  78.761  1.00 25.74           C  
ANISOU  474  CG2 VAL A  59     2986   3684   3111   -353   -800   -409       C  
ATOM    475  N   VAL A  60      31.646  17.252  79.754  1.00 31.46           N  
ANISOU  475  N   VAL A  60     3603   4733   3618   -340   -794    119       N  
ATOM    476  CA  VAL A  60      30.439  16.428  79.769  1.00 42.24           C  
ANISOU  476  CA  VAL A  60     4901   6227   4920   -411   -850    190       C  
ATOM    477  C   VAL A  60      30.007  16.128  78.355  1.00 42.16           C  
ANISOU  477  C   VAL A  60     4719   6557   4744   -567   -873    202       C  
ATOM    478  O   VAL A  60      30.354  16.860  77.445  1.00 48.98           O  
ANISOU  478  O   VAL A  60     5497   7583   5530   -573   -820    260       O  
ATOM    479  CB  VAL A  60      29.283  17.070  80.545  1.00 39.72           C  
ANISOU  479  CB  VAL A  60     4596   5886   4608   -294   -780    475       C  
ATOM    480  CG1 VAL A  60      29.732  17.382  81.965  1.00 30.54           C  
ANISOU  480  CG1 VAL A  60     3620   4408   3575   -176   -746    434       C  
ATOM    481  CG2 VAL A  60      28.805  18.319  79.840  1.00 42.60           C  
ANISOU  481  CG2 VAL A  60     4843   6439   4905   -233   -647    757       C  
ATOM    482  N   GLU A  61      29.300  15.018  78.169  1.00 48.93           N  
ANISOU  482  N   GLU A  61     5523   7526   5542   -711   -948    133       N  
ATOM    483  CA  GLU A  61      28.606  14.743  76.911  1.00 48.93           C  
ANISOU  483  CA  GLU A  61     5349   7910   5333   -906   -974    178       C  
ATOM    484  C   GLU A  61      27.157  15.116  77.128  1.00 49.95           C  
ANISOU  484  C   GLU A  61     5370   8221   5387   -873   -973    525       C  
ATOM    485  O   GLU A  61      26.399  14.368  77.735  1.00 60.08           O  
ANISOU  485  O   GLU A  61     6674   9448   6706   -903  -1027    536       O  
ATOM    486  CB  GLU A  61      28.722  13.279  76.515  1.00 37.30           C  
ANISOU  486  CB  GLU A  61     3882   6453   3836  -1128  -1030   -134       C  
ATOM    487  CG  GLU A  61      30.099  12.882  76.048  1.00 38.67           C  
ANISOU  487  CG  GLU A  61     4128   6490   4075  -1184   -993   -445       C  
ATOM    488  CD  GLU A  61      30.197  11.415  75.698  1.00 49.70           C  
ANISOU  488  CD  GLU A  61     5551   7840   5494  -1388   -960   -744       C  
ATOM    489  OE1 GLU A  61      31.266  10.824  75.876  1.00 54.80           O  
ANISOU  489  OE1 GLU A  61     6294   8215   6313  -1363   -889   -966       O  
ATOM    490  OE2 GLU A  61      29.205  10.835  75.242  1.00 69.70           O  
ANISOU  490  OE2 GLU A  61     7997  10605   7880  -1584   -989   -747       O  
ATOM    491  N   GLY A  62      26.788  16.300  76.668  1.00 51.41           N  
ANISOU  491  N   GLY A  62     5431   8607   5497   -794   -891    839       N  
ATOM    492  CA  GLY A  62      25.463  16.821  76.913  1.00 54.34           C  
ANISOU  492  CA  GLY A  62     5684   9124   5837   -724   -845   1241       C  
ATOM    493  C   GLY A  62      25.437  18.322  76.791  1.00 47.24           C  
ANISOU  493  C   GLY A  62     4708   8258   4983   -543   -675   1571       C  
ATOM    494  O   GLY A  62      25.460  18.864  75.702  1.00 51.66           O  
ANISOU  494  O   GLY A  62     5080   9130   5417   -599   -638   1723       O  
ATOM    495  N   ASN A  63      25.284  19.008  77.903  1.00 41.41           N  
ANISOU  495  N   ASN A  63     4112   7193   4429   -330   -550   1682       N  
ATOM    496  CA  ASN A  63      25.299  20.443  77.931  1.00 45.13           C  
ANISOU  496  CA  ASN A  63     4524   7636   4988   -154   -329   1997       C  
ATOM    497  C   ASN A  63      26.019  20.960  79.137  1.00 50.06           C  
ANISOU  497  C   ASN A  63     5403   7807   5809     13   -207   1864       C  
ATOM    498  O   ASN A  63      25.496  20.907  80.205  1.00 48.12           O  
ANISOU  498  O   ASN A  63     5281   7349   5653     98   -157   1932       O  
ATOM    499  CB  ASN A  63      23.891  20.934  78.019  1.00 49.83           C  
ANISOU  499  CB  ASN A  63     4933   8432   5568    -98   -222   2484       C  
ATOM    500  CG  ASN A  63      23.756  22.340  77.612  1.00 56.18           C  
ANISOU  500  CG  ASN A  63     5612   9255   6480     75     54   2870       C  
ATOM    501  OD1 ASN A  63      23.132  22.637  76.638  1.00 65.68           O  
ANISOU  501  OD1 ASN A  63     6528  10832   7597     50    113   3259       O  
ATOM    502  ND2 ASN A  63      24.312  23.220  78.372  1.00 48.85           N  
ANISOU  502  ND2 ASN A  63     4883   7935   5744    237    237   2772       N  
ATOM    503  N   ALA A  64      27.196  21.521  78.969  1.00 59.68           N  
ANISOU  503  N   ALA A  64     6701   8893   7083     42   -163   1670       N  
ATOM    504  CA  ALA A  64      27.951  22.066  80.096  1.00 55.52           C  
ANISOU  504  CA  ALA A  64     6414   7970   6711    149    -59   1512       C  
ATOM    505  C   ALA A  64      27.093  23.026  80.929  1.00 52.32           C  
ANISOU  505  C   ALA A  64     6063   7389   6429    302    194   1806       C  
ATOM    506  O   ALA A  64      26.984  22.888  82.132  1.00 45.78           O  
ANISOU  506  O   ALA A  64     5430   6299   5664    340    219   1718       O  
ATOM    507  CB  ALA A  64      29.197  22.751  79.603  1.00 58.45           C  
ANISOU  507  CB  ALA A  64     6800   8285   7124    163     -3   1370       C  
ATOM    508  N   LEU A  65      26.460  23.983  80.267  1.00 57.45           N  
ANISOU  508  N   LEU A  65     6523   8193   7113    387    403   2178       N  
ATOM    509  CA  LEU A  65      25.580  24.942  80.924  1.00 44.62           C  
ANISOU  509  CA  LEU A  65     4918   6397   5637    542    708   2512       C  
ATOM    510  C   LEU A  65      24.533  24.288  81.823  1.00 42.99           C  
ANISOU  510  C   LEU A  65     4767   6125   5442    561    659   2570       C  
ATOM    511  O   LEU A  65      24.510  24.534  83.032  1.00 52.56           O  
ANISOU  511  O   LEU A  65     6189   7016   6765    632    783   2458       O  
ATOM    512  CB  LEU A  65      24.905  25.801  79.870  1.00 44.98           C  
ANISOU  512  CB  LEU A  65     4641   6719   5729    626    895   2946       C  
ATOM    513  CG  LEU A  65      25.938  26.453  78.970  1.00 57.92           C  
ANISOU  513  CG  LEU A  65     6207   8434   7366    617    955   2900       C  
ATOM    514  CD1 LEU A  65      25.268  26.987  77.717  1.00 68.91           C  
ANISOU  514  CD1 LEU A  65     7211  10226   8745    666   1041   3331       C  
ATOM    515  CD2 LEU A  65      26.676  27.542  79.739  1.00 59.84           C  
ANISOU  515  CD2 LEU A  65     6660   8257   7818    727   1235   2782       C  
ATOM    516  N   GLU A  66      23.655  23.482  81.233  1.00 36.81           N  
ANISOU  516  N   GLU A  66     3775   5663   4547    485    487   2722       N  
ATOM    517  CA  GLU A  66      22.764  22.628  82.009  1.00 47.03           C  
ANISOU  517  CA  GLU A  66     5099   6920   5849    471    386   2707       C  
ATOM    518  C   GLU A  66      23.483  21.872  83.116  1.00 54.00           C  
ANISOU  518  C   GLU A  66     6287   7508   6723    431    244   2322       C  
ATOM    519  O   GLU A  66      23.158  22.019  84.290  1.00 59.88           O  
ANISOU  519  O   GLU A  66     7173   8004   7576    518    358   2281       O  
ATOM    520  CB  GLU A  66      22.085  21.616  81.115  1.00 60.48           C  
ANISOU  520  CB  GLU A  66     6586   9015   7378    313    153   2813       C  
ATOM    521  CG  GLU A  66      21.103  22.220  80.158  1.00 74.34           C  
ANISOU  521  CG  GLU A  66     7988  11128   9130    335    263   3261       C  
ATOM    522  CD  GLU A  66      20.281  21.160  79.494  1.00 79.25           C  
ANISOU  522  CD  GLU A  66     8418  12133   9559    139     35   3367       C  
ATOM    523  OE1 GLU A  66      19.824  21.415  78.364  1.00 78.69           O  
ANISOU  523  OE1 GLU A  66     8049  12480   9368     57     25   3669       O  
ATOM    524  OE2 GLU A  66      20.107  20.075  80.108  1.00 78.71           O  
ANISOU  524  OE2 GLU A  66     8490  11959   9457     57   -132   3149       O  
ATOM    525  N   PHE A  67      24.458  21.053  82.747  1.00 50.89           N  
ANISOU  525  N   PHE A  67     5962   7164   6211    303      4   2029       N  
ATOM    526  CA  PHE A  67      25.158  20.288  83.754  1.00 47.18           C  
ANISOU  526  CA  PHE A  67     5705   6454   5767    269   -134   1682       C  
ATOM    527  C   PHE A  67      25.652  21.198  84.899  1.00 48.81           C  
ANISOU  527  C   PHE A  67     6143   6325   6079    367     57   1616       C  
ATOM    528  O   PHE A  67      25.497  20.852  86.084  1.00 41.62           O  
ANISOU  528  O   PHE A  67     5395   5222   5198    392     43   1538       O  
ATOM    529  CB  PHE A  67      26.295  19.455  83.158  1.00 37.18           C  
ANISOU  529  CB  PHE A  67     4425   5264   4439    131   -346   1337       C  
ATOM    530  CG  PHE A  67      27.094  18.738  84.198  1.00 38.59           C  
ANISOU  530  CG  PHE A  67     4784   5207   4670    109   -461   1040       C  
ATOM    531  CD1 PHE A  67      26.771  17.449  84.565  1.00 41.77           C  
ANISOU  531  CD1 PHE A  67     5178   5616   5075     53   -624    944       C  
ATOM    532  CD2 PHE A  67      28.127  19.376  84.857  1.00 35.73           C  
ANISOU  532  CD2 PHE A  67     4584   4629   4363    139   -393    888       C  
ATOM    533  CE1 PHE A  67      27.479  16.804  85.542  1.00 38.75           C  
ANISOU  533  CE1 PHE A  67     4923   5041   4758     46   -713    731       C  
ATOM    534  CE2 PHE A  67      28.836  18.732  85.838  1.00 36.55           C  
ANISOU  534  CE2 PHE A  67     4819   4568   4500    105   -503    670       C  
ATOM    535  CZ  PHE A  67      28.512  17.454  86.182  1.00 38.63           C  
ANISOU  535  CZ  PHE A  67     5051   4851   4776     70   -659    609       C  
ATOM    536  N   ALA A  68      26.207  22.364  84.560  1.00 37.43           N  
ANISOU  536  N   ALA A  68     4711   4821   4688    409    251   1649       N  
ATOM    537  CA  ALA A  68      26.751  23.250  85.596  1.00 44.54           C  
ANISOU  537  CA  ALA A  68     5843   5408   5674    452    450   1539       C  
ATOM    538  C   ALA A  68      25.663  23.954  86.419  1.00 54.73           C  
ANISOU  538  C   ALA A  68     7204   6532   7059    571    735   1778       C  
ATOM    539  O   ALA A  68      25.787  24.103  87.639  1.00 50.72           O  
ANISOU  539  O   ALA A  68     6920   5784   6569    568    821   1640       O  
ATOM    540  CB  ALA A  68      27.762  24.260  85.025  1.00 25.82           C  
ANISOU  540  CB  ALA A  68     3468   2991   3350    446    583   1459       C  
ATOM    541  N   GLU A  69      24.585  24.382  85.779  1.00 50.74           N  
ANISOU  541  N   GLU A  69     6462   6190   6627    674    891   2094       N  
ATOM    542  CA  GLU A  69      23.499  24.921  86.580  1.00 57.35           C  
ANISOU  542  CA  GLU A  69     7309   6891   7590    811   1159   2272       C  
ATOM    543  C   GLU A  69      22.969  23.858  87.546  1.00 57.25           C  
ANISOU  543  C   GLU A  69     7381   6854   7519    782    987   2157       C  
ATOM    544  O   GLU A  69      22.805  24.121  88.735  1.00 51.35           O  
ANISOU  544  O   GLU A  69     6835   5872   6805    824   1140   2080       O  
ATOM    545  CB  GLU A  69      22.389  25.483  85.715  1.00 69.19           C  
ANISOU  545  CB  GLU A  69     8491   8594   9204    943   1337   2686       C  
ATOM    546  CG  GLU A  69      21.878  26.802  86.232  1.00 82.00           C  
ANISOU  546  CG  GLU A  69    10151   9968  11037   1125   1785   2885       C  
ATOM    547  CD  GLU A  69      22.039  27.882  85.203  1.00 95.85           C  
ANISOU  547  CD  GLU A  69    11710  11790  12919   1216   2007   3133       C  
ATOM    548  OE1 GLU A  69      21.896  27.569  83.996  1.00 91.67           O  
ANISOU  548  OE1 GLU A  69    10892  11617  12322   1185   1823   3320       O  
ATOM    549  OE2 GLU A  69      22.326  29.031  85.604  1.00104.08           O  
ANISOU  549  OE2 GLU A  69    12890  12532  14124   1305   2374   3135       O  
ATOM    550  N   TYR A  70      22.742  22.650  87.039  1.00 59.39           N  
ANISOU  550  N   TYR A  70     7506   7361   7697    695    681   2136       N  
ATOM    551  CA  TYR A  70      22.357  21.536  87.895  1.00 51.46           C  
ANISOU  551  CA  TYR A  70     6564   6333   6655    657    505   2009       C  
ATOM    552  C   TYR A  70      23.332  21.317  89.045  1.00 55.51           C  
ANISOU  552  C   TYR A  70     7361   6609   7120    606    438   1702       C  
ATOM    553  O   TYR A  70      22.912  20.992  90.148  1.00 59.76           O  
ANISOU  553  O   TYR A  70     8002   7041   7663    634    455   1654       O  
ATOM    554  CB  TYR A  70      22.184  20.246  87.100  1.00 42.83           C  
ANISOU  554  CB  TYR A  70     5300   5494   5480    537    204   1986       C  
ATOM    555  CG  TYR A  70      21.649  19.108  87.926  1.00 39.48           C  
ANISOU  555  CG  TYR A  70     4901   5040   5061    510     63   1897       C  
ATOM    556  CD1 TYR A  70      20.305  19.008  88.204  1.00 39.73           C  
ANISOU  556  CD1 TYR A  70     4802   5135   5160    578    154   2121       C  
ATOM    557  CD2 TYR A  70      22.497  18.143  88.449  1.00 46.26           C  
ANISOU  557  CD2 TYR A  70     5892   5806   5879    429   -144   1610       C  
ATOM    558  CE1 TYR A  70      19.801  17.976  88.982  1.00 46.96           C  
ANISOU  558  CE1 TYR A  70     5734   6015   6092    556     42   2047       C  
ATOM    559  CE2 TYR A  70      22.007  17.094  89.214  1.00 52.67           C  
ANISOU  559  CE2 TYR A  70     6704   6588   6721    413   -250   1548       C  
ATOM    560  CZ  TYR A  70      20.656  17.017  89.479  1.00 52.63           C  
ANISOU  560  CZ  TYR A  70     6584   6640   6772    473   -156   1758       C  
ATOM    561  OH  TYR A  70      20.149  15.986  90.234  1.00 48.07           O  
ANISOU  561  OH  TYR A  70     6000   6031   6233    460   -248   1708       O  
ATOM    562  N   ALA A  71      24.627  21.497  88.815  1.00 55.76           N  
ANISOU  562  N   ALA A  71     7509   6575   7101    526    360   1517       N  
ATOM    563  CA  ALA A  71      25.571  21.306  89.917  1.00 57.25           C  
ANISOU  563  CA  ALA A  71     7940   6571   7241    458    285   1269       C  
ATOM    564  C   ALA A  71      25.529  22.428  90.967  1.00 60.65           C  
ANISOU  564  C   ALA A  71     8602   6750   7694    487    586   1266       C  
ATOM    565  O   ALA A  71      25.538  22.156  92.161  1.00 65.03           O  
ANISOU  565  O   ALA A  71     9322   7188   8199    457    570   1165       O  
ATOM    566  CB  ALA A  71      26.989  21.077  89.407  1.00 52.64           C  
ANISOU  566  CB  ALA A  71     7366   6022   6614    349    104   1041       C  
ATOM    567  N   LYS A  72      25.484  23.682  90.529  1.00 61.88           N  
ANISOU  567  N   LYS A  72     8768   6817   7927    536    880   1382       N  
ATOM    568  CA  LYS A  72      25.425  24.815  91.453  1.00 65.09           C  
ANISOU  568  CA  LYS A  72     9408   6947   8378    544   1234   1369       C  
ATOM    569  C   LYS A  72      24.367  24.581  92.531  1.00 70.63           C  
ANISOU  569  C   LYS A  72    10182   7578   9076    620   1337   1436       C  
ATOM    570  O   LYS A  72      24.545  24.942  93.696  1.00 76.10           O  
ANISOU  570  O   LYS A  72    11143   8052   9720    552   1488   1316       O  
ATOM    571  CB  LYS A  72      25.077  26.097  90.700  1.00 70.00           C  
ANISOU  571  CB  LYS A  72     9935   7510   9151    650   1594   1576       C  
ATOM    572  CG  LYS A  72      25.945  27.303  91.053  1.00 73.28           C  
ANISOU  572  CG  LYS A  72    10586   7642   9614    556   1889   1438       C  
ATOM    573  CD  LYS A  72      26.492  27.244  92.470  1.00 67.14           C  
ANISOU  573  CD  LYS A  72    10118   6675   8717    393   1890   1139       C  
ATOM    574  CE  LYS A  72      25.518  27.776  93.501  1.00 69.25           C  
ANISOU  574  CE  LYS A  72    10577   6700   9036    447   2248   1249       C  
ATOM    575  NZ  LYS A  72      26.155  27.836  94.856  1.00 74.46           N  
ANISOU  575  NZ  LYS A  72    11534   7218   9539    244   2266    913       N  
ATOM    576  N   ARG A  73      23.253  23.985  92.125  1.00 65.49           N  
ANISOU  576  N   ARG A  73     9291   7118   8476    741   1263   1635       N  
ATOM    577  CA  ARG A  73      22.168  23.661  93.033  1.00 63.09           C  
ANISOU  577  CA  ARG A  73     9006   6779   8188    830   1341   1727       C  
ATOM    578  C   ARG A  73      22.676  23.046  94.320  1.00 64.56           C  
ANISOU  578  C   ARG A  73     9428   6862   8240    725   1194   1497       C  
ATOM    579  O   ARG A  73      22.190  23.358  95.411  1.00 73.23           O  
ANISOU  579  O   ARG A  73    10708   7791   9326    758   1396   1509       O  
ATOM    580  CB  ARG A  73      21.227  22.676  92.356  1.00 65.95           C  
ANISOU  580  CB  ARG A  73     9058   7414   8586    889   1133   1895       C  
ATOM    581  CG  ARG A  73      20.209  23.331  91.463  1.00 56.98           C  
ANISOU  581  CG  ARG A  73     7672   6382   7596   1027   1350   2235       C  
ATOM    582  CD  ARG A  73      18.854  23.090  92.012  1.00 63.82           C  
ANISOU  582  CD  ARG A  73     8441   7267   8542   1148   1458   2440       C  
ATOM    583  NE  ARG A  73      18.161  22.058  91.254  1.00 70.30           N  
ANISOU  583  NE  ARG A  73     8967   8384   9361   1113   1199   2574       N  
ATOM    584  CZ  ARG A  73      17.331  21.170  91.794  1.00 75.37           C  
ANISOU  584  CZ  ARG A  73     9541   9090  10008   1121   1095   2611       C  
ATOM    585  NH1 ARG A  73      17.113  21.165  93.109  1.00 71.68           N  
ANISOU  585  NH1 ARG A  73     9273   8429   9534   1182   1211   2525       N  
ATOM    586  NH2 ARG A  73      16.733  20.276  91.017  1.00 76.72           N  
ANISOU  586  NH2 ARG A  73     9454   9518  10178   1052    880   2734       N  
ATOM    587  N   PHE A  74      23.669  22.179  94.190  1.00 58.93           N  
ANISOU  587  N   PHE A  74     8706   6250   7433    600    854   1310       N  
ATOM    588  CA  PHE A  74      24.104  21.377  95.317  1.00 62.93           C  
ANISOU  588  CA  PHE A  74     9351   6728   7833    515    661   1152       C  
ATOM    589  C   PHE A  74      25.496  21.669  95.804  1.00 55.28           C  
ANISOU  589  C   PHE A  74     8605   5633   6764    337    605    951       C  
ATOM    590  O   PHE A  74      25.982  20.957  96.657  1.00 60.44           O  
ANISOU  590  O   PHE A  74     9299   6349   7318    251    415    808       O  
ATOM    591  CB  PHE A  74      23.995  19.900  94.973  1.00 69.98           C  
ANISOU  591  CB  PHE A  74    10012   7841   8736    519    319   1131       C  
ATOM    592  CG  PHE A  74      22.663  19.523  94.424  1.00 74.93           C  
ANISOU  592  CG  PHE A  74    10404   8607   9459    629    351   1319       C  
ATOM    593  CD1 PHE A  74      22.513  19.211  93.088  1.00 65.06           C  
ANISOU  593  CD1 PHE A  74     8926   7532   8263    618    248   1392       C  
ATOM    594  CD2 PHE A  74      21.550  19.507  95.247  1.00 80.72           C  
ANISOU  594  CD2 PHE A  74    11150   9297  10222    728    494   1440       C  
ATOM    595  CE1 PHE A  74      21.285  18.874  92.586  1.00 69.29           C  
ANISOU  595  CE1 PHE A  74     9245   8209   8874    679    272   1591       C  
ATOM    596  CE2 PHE A  74      20.323  19.174  94.755  1.00 79.53           C  
ANISOU  596  CE2 PHE A  74    10770   9277  10169    813    525   1638       C  
ATOM    597  CZ  PHE A  74      20.186  18.856  93.423  1.00 78.49           C  
ANISOU  597  CZ  PHE A  74    10408   9331  10085    777    408   1720       C  
ATOM    598  N   LEU A  75      26.127  22.711  95.279  1.00 55.25           N  
ANISOU  598  N   LEU A  75     8652   5561   6778    274    778    862       N  
ATOM    599  CA  LEU A  75      27.523  23.031  95.608  1.00 61.93           C  
ANISOU  599  CA  LEU A  75     9602   6412   7517     79    717    563       C  
ATOM    600  C   LEU A  75      27.708  24.518  95.875  1.00 79.35           C  
ANISOU  600  C   LEU A  75    12017   8401   9730      1   1100    480       C  
ATOM    601  O   LEU A  75      27.312  25.356  95.072  1.00 84.24           O  
ANISOU  601  O   LEU A  75    12595   8923  10489    102   1351    629       O  
ATOM    602  CB  LEU A  75      28.453  22.649  94.453  1.00 58.22           C  
ANISOU  602  CB  LEU A  75     8940   6103   7079     50    481    483       C  
ATOM    603  CG  LEU A  75      29.148  21.293  94.305  1.00 56.04           C  
ANISOU  603  CG  LEU A  75     8503   6019   6770      6    100    390       C  
ATOM    604  CD1 LEU A  75      28.494  20.221  95.115  1.00 52.40           C  
ANISOU  604  CD1 LEU A  75     8016   5605   6289     56    -42    470       C  
ATOM    605  CD2 LEU A  75      29.187  20.894  92.826  1.00 55.99           C  
ANISOU  605  CD2 LEU A  75     8277   6139   6859     78    -21    459       C  
ATOM    606  N   PRO A  76      28.354  24.855  96.992  1.00 90.78           N  
ANISOU  606  N   PRO A  76    13679   9788  11027   -196   1158    242       N  
ATOM    607  CA  PRO A  76      28.601  26.257  97.319  1.00 88.39           C  
ANISOU  607  CA  PRO A  76    13601   9261  10724   -319   1548    107       C  
ATOM    608  C   PRO A  76      29.640  26.860  96.384  1.00 78.06           C  
ANISOU  608  C   PRO A  76    12219   7967   9473   -388   1544    -10       C  
ATOM    609  O   PRO A  76      30.677  26.251  96.161  1.00 80.05           O  
ANISOU  609  O   PRO A  76    12365   8409   9643   -487   1213   -145       O  
ATOM    610  CB  PRO A  76      29.196  26.146  98.715  1.00 91.38           C  
ANISOU  610  CB  PRO A  76    14182   9676  10863   -569   1489   -149       C  
ATOM    611  CG  PRO A  76      30.043  24.919  98.588  1.00 91.08           C  
ANISOU  611  CG  PRO A  76    13946   9927  10734   -617   1007   -200       C  
ATOM    612  CD  PRO A  76      29.074  23.965  97.920  1.00 93.60           C  
ANISOU  612  CD  PRO A  76    14053  10313  11199   -354    854     73       C  
ATOM    613  N   GLY A  77      29.378  28.047  95.859  1.00 75.57           N  
ANISOU  613  N   GLY A  77    11950   7447   9316   -328   1928     62       N  
ATOM    614  CA  GLY A  77      30.363  28.727  95.034  1.00 79.30           C  
ANISOU  614  CA  GLY A  77    12363   7911   9857   -392   1965    -48       C  
ATOM    615  C   GLY A  77      29.704  29.634  94.015  1.00 83.91           C  
ANISOU  615  C   GLY A  77    12841   8353  10689   -194   2310    210       C  
ATOM    616  O   GLY A  77      28.471  29.724  93.973  1.00 90.15           O  
ANISOU  616  O   GLY A  77    13599   9058  11594    -15   2521    491       O  
ATOM    617  N   LYS A  78      30.515  30.301  93.194  1.00 76.05           N  
ANISOU  617  N   LYS A  78    11769   7344   9783   -220   2373    148       N  
ATOM    618  CA  LYS A  78      29.993  31.214  92.177  1.00 77.80           C  
ANISOU  618  CA  LYS A  78    11850   7457  10252    -33   2711    420       C  
ATOM    619  C   LYS A  78      30.103  30.602  90.770  1.00 82.20           C  
ANISOU  619  C   LYS A  78    12084   8297  10850    113   2407    609       C  
ATOM    620  O   LYS A  78      31.149  30.063  90.391  1.00 81.44           O  
ANISOU  620  O   LYS A  78    11915   8375  10654     21   2067    423       O  
ATOM    621  CB  LYS A  78      30.715  32.566  92.263  1.00 81.42           C  
ANISOU  621  CB  LYS A  78    12453   7663  10818   -156   3092    242       C  
ATOM    622  CG  LYS A  78      29.988  33.738  91.606  1.00 89.29           C  
ANISOU  622  CG  LYS A  78    13365   8444  12117     32   3611    544       C  
ATOM    623  CD  LYS A  78      30.772  34.349  90.432  1.00 89.36           C  
ANISOU  623  CD  LYS A  78    13181   8500  12272     80   3645    582       C  
ATOM    624  CE  LYS A  78      32.025  35.077  90.914  1.00 93.48           C  
ANISOU  624  CE  LYS A  78    13910   8850  12759   -171   3754    187       C  
ATOM    625  NZ  LYS A  78      32.825  35.666  89.796  1.00 98.51           N  
ANISOU  625  NZ  LYS A  78    14357   9523  13548   -116   3783    224       N  
ATOM    626  N   LEU A  79      29.014  30.679  90.009  1.00 80.43           N  
ANISOU  626  N   LEU A  79    11661   8132  10765    326   2542    990       N  
ATOM    627  CA  LEU A  79      28.976  30.130  88.658  1.00 78.01           C  
ANISOU  627  CA  LEU A  79    11044   8126  10469    438   2285   1185       C  
ATOM    628  C   LEU A  79      29.100  31.222  87.587  1.00 74.91           C  
ANISOU  628  C   LEU A  79    10478   7713  10270    543   2572   1388       C  
ATOM    629  O   LEU A  79      28.332  32.184  87.590  1.00 79.41           O  
ANISOU  629  O   LEU A  79    11032   8104  11036    662   3011   1658       O  
ATOM    630  CB  LEU A  79      27.684  29.326  88.436  1.00 75.75           C  
ANISOU  630  CB  LEU A  79    10601   8016  10164    571   2171   1499       C  
ATOM    631  CG  LEU A  79      27.580  28.662  87.053  1.00 75.09           C  
ANISOU  631  CG  LEU A  79    10201   8286  10042    635   1893   1677       C  
ATOM    632  CD1 LEU A  79      28.759  27.720  86.828  1.00 80.75           C  
ANISOU  632  CD1 LEU A  79    10916   9161  10603    497   1472   1339       C  
ATOM    633  CD2 LEU A  79      26.277  27.919  86.851  1.00 63.96           C  
ANISOU  633  CD2 LEU A  79     8611   7083   8609    741   1786   1946       C  
ATOM    634  N   VAL A  80      30.072  31.075  86.686  1.00 66.08           N  
ANISOU  634  N   VAL A  80     9222   6771   9116    507   2346   1278       N  
ATOM    635  CA  VAL A  80      30.168  31.933  85.506  1.00 64.82           C  
ANISOU  635  CA  VAL A  80     8835   6672   9122    625   2553   1511       C  
ATOM    636  C   VAL A  80      29.859  31.110  84.273  1.00 72.20           C  
ANISOU  636  C   VAL A  80     9463   8001   9967    700   2248   1722       C  
ATOM    637  O   VAL A  80      30.532  30.119  83.997  1.00 73.52           O  
ANISOU  637  O   VAL A  80     9609   8357   9967    604   1849   1499       O  
ATOM    638  CB  VAL A  80      31.586  32.491  85.290  1.00 63.28           C  
ANISOU  638  CB  VAL A  80     8697   6390   8956    525   2549   1231       C  
ATOM    639  CG1 VAL A  80      31.638  33.286  84.001  1.00 58.74           C  
ANISOU  639  CG1 VAL A  80     7851   5914   8555    669   2741   1506       C  
ATOM    640  CG2 VAL A  80      32.032  33.335  86.458  1.00 66.01           C  
ANISOU  640  CG2 VAL A  80     9348   6371   9361    390   2843    972       C  
ATOM    641  N   LYS A  81      28.853  31.528  83.520  1.00 69.42           N  
ANISOU  641  N   LYS A  81     8867   7783   9728    856   2456   2161       N  
ATOM    642  CA  LYS A  81      28.543  30.866  82.269  1.00 61.45           C  
ANISOU  642  CA  LYS A  81     7547   7192   8610    891   2197   2376       C  
ATOM    643  C   LYS A  81      29.148  31.595  81.057  1.00 67.89           C  
ANISOU  643  C   LYS A  81     8132   8153   9511    949   2293   2503       C  
ATOM    644  O   LYS A  81      29.223  32.826  81.010  1.00 72.40           O  
ANISOU  644  O   LYS A  81     8673   8524  10310   1056   2680   2648       O  
ATOM    645  CB  LYS A  81      27.039  30.726  82.118  1.00 58.54           C  
ANISOU  645  CB  LYS A  81     6971   6987   8284   1032   2260   2755       C  
ATOM    646  CG  LYS A  81      26.363  30.117  83.318  1.00 67.49           C  
ANISOU  646  CG  LYS A  81     8305   7969   9369   1010   2210   2654       C  
ATOM    647  CD  LYS A  81      25.138  29.288  82.921  1.00 77.20           C  
ANISOU  647  CD  LYS A  81     9289   9520  10523   1063   2016   2911       C  
ATOM    648  CE  LYS A  81      23.891  30.141  82.729  1.00 88.38           C  
ANISOU  648  CE  LYS A  81    10459  10956  12165   1290   2345   3363       C  
ATOM    649  NZ  LYS A  81      22.716  29.319  82.316  1.00 91.12           N  
ANISOU  649  NZ  LYS A  81    10541  11654  12428   1307   2136   3631       N  
ATOM    650  N   HIS A  82      29.582  30.836  80.068  1.00 71.26           N  
ANISOU  650  N   HIS A  82     8397   8914   9766    884   1947   2425       N  
ATOM    651  CA  HIS A  82      30.064  31.401  78.830  1.00 75.71           C  
ANISOU  651  CA  HIS A  82     8709   9685  10374    939   1999   2572       C  
ATOM    652  C   HIS A  82      29.239  30.757  77.761  1.00 84.45           C  
ANISOU  652  C   HIS A  82     9498  11271  11319    937   1823   2883       C  
ATOM    653  O   HIS A  82      29.561  29.712  77.272  1.00 80.78           O  
ANISOU  653  O   HIS A  82     9001  11056  10635    807   1462   2679       O  
ATOM    654  CB  HIS A  82      31.530  31.092  78.612  1.00 65.62           C  
ANISOU  654  CB  HIS A  82     7544   8366   9023    834   1760   2154       C  
ATOM    655  CG  HIS A  82      32.336  31.044  79.867  1.00 71.41           C  
ANISOU  655  CG  HIS A  82     8621   8714   9799    746   1768   1770       C  
ATOM    656  ND1 HIS A  82      32.580  32.148  80.643  1.00 75.60           N  
ANISOU  656  ND1 HIS A  82     9291   8902  10532    782   2126   1743       N  
ATOM    657  CD2 HIS A  82      32.983  30.022  80.461  1.00 75.63           C  
ANISOU  657  CD2 HIS A  82     9371   9173  10193    605   1473   1411       C  
ATOM    658  CE1 HIS A  82      33.326  31.807  81.673  1.00 77.72           C  
ANISOU  658  CE1 HIS A  82     9852   8932  10747    642   2028   1371       C  
ATOM    659  NE2 HIS A  82      33.586  30.520  81.585  1.00 80.30           N  
ANISOU  659  NE2 HIS A  82    10215   9425  10871    544   1628   1187       N  
ATOM    660  N   ASP A  83      28.111  31.342  77.423  1.00 94.69           N  
ANISOU  660  N   ASP A  83    10553  12671  12753   1108   2034   3334       N  
ATOM    661  CA  ASP A  83      27.192  30.733  76.473  1.00 84.10           C  
ANISOU  661  CA  ASP A  83     8900  11795  11259   1101   1850   3660       C  
ATOM    662  C   ASP A  83      27.668  30.556  75.061  1.00 81.17           C  
ANISOU  662  C   ASP A  83     8268  11871  10703   1017   1661   3726       C  
ATOM    663  O   ASP A  83      27.312  29.601  74.417  1.00 81.06           O  
ANISOU  663  O   ASP A  83     8121  12253  10427    857   1392   3748       O  
ATOM    664  CB  ASP A  83      25.890  31.510  76.410  1.00 73.42           C  
ANISOU  664  CB  ASP A  83     7310  10450  10135   1333   2128   4172       C  
ATOM    665  CG  ASP A  83      25.026  31.290  77.594  1.00 81.21           C  
ANISOU  665  CG  ASP A  83     8432  11254  11171   1362   2172   4186       C  
ATOM    666  OD1 ASP A  83      24.041  30.564  77.464  1.00 84.11           O  
ANISOU  666  OD1 ASP A  83     8598  11950  11411   1324   1994   4412       O  
ATOM    667  OD2 ASP A  83      25.306  31.859  78.646  1.00 85.28           O  
ANISOU  667  OD2 ASP A  83     9252  11311  11838   1403   2383   3965       O  
ATOM    668  N   LYS A  84      28.490  31.457  74.568  1.00 73.45           N  
ANISOU  668  N   LYS A  84     7214  10837   9855   1113   1812   3758       N  
ATOM    669  CA  LYS A  84      28.733  31.466  73.154  1.00 83.82           C  
ANISOU  669  CA  LYS A  84     8230  12612  11006   1071   1667   3911       C  
ATOM    670  C   LYS A  84      29.264  30.136  72.751  1.00 88.69           C  
ANISOU  670  C   LYS A  84     8926  13473  11301    800   1324   3517       C  
ATOM    671  O   LYS A  84      28.825  29.559  71.781  1.00 84.40           O  
ANISOU  671  O   LYS A  84     8156  13410  10504    663   1130   3640       O  
ATOM    672  CB  LYS A  84      29.739  32.537  72.807  1.00 89.62           C  
ANISOU  672  CB  LYS A  84     8907  13205  11940   1220   1869   3966       C  
ATOM    673  CG  LYS A  84      29.686  32.917  71.359  1.00 88.28           C  
ANISOU  673  CG  LYS A  84     8375  13528  11639   1241   1785   4277       C  
ATOM    674  CD  LYS A  84      29.223  31.748  70.561  1.00 86.85           C  
ANISOU  674  CD  LYS A  84     8046  13885  11067    998   1446   4231       C  
ATOM    675  CE  LYS A  84      29.351  32.012  69.102  1.00 85.36           C  
ANISOU  675  CE  LYS A  84     7526  14228  10680    956   1343   4464       C  
ATOM    676  NZ  LYS A  84      28.591  31.013  68.345  1.00 87.52           N  
ANISOU  676  NZ  LYS A  84     7631  15044  10577    692   1075   4491       N  
ATOM    677  N   PHE A  85      30.193  29.626  73.533  1.00 93.85           N  
ANISOU  677  N   PHE A  85     9907  13776  11974    732   1218   3029       N  
ATOM    678  CA  PHE A  85      30.650  28.251  73.401  1.00 93.81           C  
ANISOU  678  CA  PHE A  85    10029  13880  11733    536    847   2626       C  
ATOM    679  C   PHE A  85      30.332  27.421  74.633  1.00 83.72           C  
ANISOU  679  C   PHE A  85     9025  12339  10445    473    724   2388       C  
ATOM    680  O   PHE A  85      31.189  27.250  75.481  1.00 87.69           O  
ANISOU  680  O   PHE A  85     9800  12490  11029    464    673   2040       O  
ATOM    681  CB  PHE A  85      32.140  28.194  73.086  1.00 98.78           C  
ANISOU  681  CB  PHE A  85    10768  14388  12374    507    746   2266       C  
ATOM    682  CG  PHE A  85      32.938  29.332  73.650  1.00 97.58           C  
ANISOU  682  CG  PHE A  85    10742  13848  12486    654    985   2223       C  
ATOM    683  CD1 PHE A  85      32.735  29.773  74.935  1.00 97.45           C  
ANISOU  683  CD1 PHE A  85    10946  13439  12641    716   1154   2186       C  
ATOM    684  CD2 PHE A  85      33.937  29.927  72.891  1.00 96.93           C  
ANISOU  684  CD2 PHE A  85    10567  13793  12469    707   1039   2193       C  
ATOM    685  CE1 PHE A  85      33.496  30.795  75.442  1.00101.02           C  
ANISOU  685  CE1 PHE A  85    11526  13543  13314    802   1381   2105       C  
ATOM    686  CE2 PHE A  85      34.700  30.942  73.394  1.00 87.23           C  
ANISOU  686  CE2 PHE A  85     9454  12208  11481    816   1255   2132       C  
ATOM    687  CZ  PHE A  85      34.489  31.365  74.671  1.00 93.47           C  
ANISOU  687  CZ  PHE A  85    10470  12615  12428    847   1426   2073       C  
ATOM    688  N   MET A  86      29.139  26.849  74.692  1.00 74.97           N  
ANISOU  688  N   MET A  86     7823  11432   9229    421    666   2597       N  
ATOM    689  CA  MET A  86      28.670  26.190  75.887  1.00 81.58           C  
ANISOU  689  CA  MET A  86     8882  12020  10095    406    612   2481       C  
ATOM    690  C   MET A  86      29.835  25.758  76.696  1.00 79.82           C  
ANISOU  690  C   MET A  86     8978  11446   9903    350    459   1993       C  
ATOM    691  O   MET A  86      30.431  24.742  76.428  1.00 78.99           O  
ANISOU  691  O   MET A  86     8935  11413   9663    206    198   1707       O  
ATOM    692  CB  MET A  86      27.943  24.918  75.514  1.00 92.36           C  
ANISOU  692  CB  MET A  86    10108  13712  11274    285    444   2638       C  
ATOM    693  CG  MET A  86      26.529  25.062  75.097  1.00 96.48           C  
ANISOU  693  CG  MET A  86    10483  14637  11537     74    185   2492       C  
ATOM    694  SD  MET A  86      26.099  23.498  74.366  1.00117.09           S  
ANISOU  694  SD  MET A  86    12913  17621  13953    -74     54   2752       S  
ATOM    695  CE  MET A  86      24.345  23.500  74.528  1.00105.82           C  
ANISOU  695  CE  MET A  86    11306  16187  12712    155    386   3385       C  
ATOM    696  N   THR A  87      30.101  26.512  77.744  1.00 70.34           N  
ANISOU  696  N   THR A  87     7965   9871   8891    456    654   1929       N  
ATOM    697  CA  THR A  87      31.242  26.265  78.614  1.00 44.23           C  
ANISOU  697  CA  THR A  87     4930   6244   5631    410    561   1529       C  
ATOM    698  C   THR A  87      30.901  26.960  79.936  1.00 44.92           C  
ANISOU  698  C   THR A  87     5219   5985   5862    486    788   1567       C  
ATOM    699  O   THR A  87      30.050  27.840  79.970  1.00 47.42           O  
ANISOU  699  O   THR A  87     5456   6273   6288    600   1069   1892       O  
ATOM    700  CB  THR A  87      32.493  26.905  78.002  1.00 37.96           C  
ANISOU  700  CB  THR A  87     4111   5412   4899    426    604   1407       C  
ATOM    701  OG1 THR A  87      33.558  25.962  77.966  1.00 54.30           O  
ANISOU  701  OG1 THR A  87     6279   7460   6891    311    343   1054       O  
ATOM    702  CG2 THR A  87      32.927  28.114  78.768  1.00 40.61           C  
ANISOU  702  CG2 THR A  87     4593   5409   5427    510    874   1399       C  
ATOM    703  N   ALA A  88      31.525  26.555  81.035  1.00 46.34           N  
ANISOU  703  N   ALA A  88     5650   5914   6042    416    687   1258       N  
ATOM    704  CA  ALA A  88      31.270  27.213  82.325  1.00 48.12           C  
ANISOU  704  CA  ALA A  88     6092   5824   6369    449    909   1250       C  
ATOM    705  C   ALA A  88      32.342  26.920  83.360  1.00 58.97           C  
ANISOU  705  C   ALA A  88     7712   6979   7715    332    782    884       C  
ATOM    706  O   ALA A  88      33.071  25.938  83.252  1.00 68.87           O  
ANISOU  706  O   ALA A  88     8967   8320   8879    242    493    670       O  
ATOM    707  CB  ALA A  88      29.891  26.863  82.871  1.00 33.81           C  
ANISOU  707  CB  ALA A  88     4282   4024   4539    497    957   1464       C  
ATOM    708  N   SER A  89      32.442  27.800  84.349  1.00 57.51           N  
ANISOU  708  N   SER A  89     7723   6518   7610    322   1022    828       N  
ATOM    709  CA  SER A  89      33.380  27.625  85.440  1.00 61.97           C  
ANISOU  709  CA  SER A  89     8514   6911   8119    178    921    513       C  
ATOM    710  C   SER A  89      32.619  27.768  86.749  1.00 72.16           C  
ANISOU  710  C   SER A  89    10004   8017   9396    158   1076    519       C  
ATOM    711  O   SER A  89      31.831  28.704  86.923  1.00 74.11           O  
ANISOU  711  O   SER A  89    10290   8115   9752    241   1423    702       O  
ATOM    712  CB  SER A  89      34.496  28.669  85.383  1.00 63.55           C  
ANISOU  712  CB  SER A  89     8784   6962   8399    120   1073    369       C  
ATOM    713  OG  SER A  89      34.834  29.005  84.051  1.00 67.36           O  
ANISOU  713  OG  SER A  89     9058   7581   8953    205   1088    482       O  
ATOM    714  N   LEU A  90      32.891  26.850  87.671  1.00 71.09           N  
ANISOU  714  N   LEU A  90     9981   7892   9138     53    836    340       N  
ATOM    715  CA  LEU A  90      32.333  26.894  89.012  1.00 69.53           C  
ANISOU  715  CA  LEU A  90     9990   7537   8890      1    943    296       C  
ATOM    716  C   LEU A  90      33.487  27.247  89.937  1.00 72.38           C  
ANISOU  716  C   LEU A  90    10546   7779   9176   -198    940      6       C  
ATOM    717  O   LEU A  90      34.539  26.608  89.902  1.00 68.72           O  
ANISOU  717  O   LEU A  90    10039   7430   8643   -300    662   -156       O  
ATOM    718  CB  LEU A  90      31.736  25.540  89.395  1.00 71.28           C  
ANISOU  718  CB  LEU A  90    10169   7894   9019     11    661    316       C  
ATOM    719  CG  LEU A  90      31.100  25.449  90.784  1.00 83.21           C  
ANISOU  719  CG  LEU A  90    11795   9314  10506     54    768    425       C  
ATOM    720  CD1 LEU A  90      32.141  25.679  91.868  1.00 90.09           C  
ANISOU  720  CD1 LEU A  90    12908   9934  11389    -14   1111    352       C  
ATOM    721  CD2 LEU A  90      29.954  26.440  90.916  1.00 89.19           C  
ANISOU  721  CD2 LEU A  90    12389  10155  11346    227    850    744       C  
ATOM    722  N   PHE A  91      33.297  28.276  90.754  1.00 72.97           N  
ANISOU  722  N   PHE A  91    10830   7631   9266   -268   1264    -52       N  
ATOM    723  CA  PHE A  91      34.374  28.784  91.606  1.00 67.37           C  
ANISOU  723  CA  PHE A  91    10312   6825   8460   -504   1295   -338       C  
ATOM    724  C   PHE A  91      34.219  28.365  93.056  1.00 75.01           C  
ANISOU  724  C   PHE A  91    11471   7779   9249   -660   1238   -469       C  
ATOM    725  O   PHE A  91      33.304  28.807  93.758  1.00 72.96           O  
ANISOU  725  O   PHE A  91    11369   7358   8995   -644   1516   -422       O  
ATOM    726  CB  PHE A  91      34.482  30.299  91.508  1.00 63.20           C  
ANISOU  726  CB  PHE A  91     9897   6053   8064   -537   1727   -376       C  
ATOM    727  CG  PHE A  91      35.106  30.773  90.231  1.00 66.45           C  
ANISOU  727  CG  PHE A  91    10129   6500   8619   -451   1742   -316       C  
ATOM    728  CD1 PHE A  91      36.461  30.578  89.988  1.00 65.82           C  
ANISOU  728  CD1 PHE A  91    10005   6527   8478   -581   1490   -501       C  
ATOM    729  CD2 PHE A  91      34.341  31.411  89.265  1.00 59.35           C  
ANISOU  729  CD2 PHE A  91     9082   5547   7921   -235   2012    -42       C  
ATOM    730  CE1 PHE A  91      37.046  31.017  88.799  1.00 48.43           C  
ANISOU  730  CE1 PHE A  91     7635   4355   6410   -491   1509   -441       C  
ATOM    731  CE2 PHE A  91      34.915  31.841  88.099  1.00 48.66           C  
ANISOU  731  CE2 PHE A  91     7547   4252   6689   -155   2025     27       C  
ATOM    732  CZ  PHE A  91      36.271  31.641  87.865  1.00 42.64           C  
ANISOU  732  CZ  PHE A  91     6763   3577   5861   -280   1772   -186       C  
ATOM    733  N   LEU A  92      35.128  27.500  93.492  1.00 85.61           N  
ANISOU  733  N   LEU A  92    12783   9302  10441   -806    888   -610       N  
ATOM    734  CA  LEU A  92      35.077  26.953  94.837  1.00 91.40           C  
ANISOU  734  CA  LEU A  92    13646  10098  10985   -959    776   -704       C  
ATOM    735  C   LEU A  92      36.256  27.443  95.676  1.00109.94           C  
ANISOU  735  C   LEU A  92    16139  12473  13162  -1274    759   -960       C  
ATOM    736  O   LEU A  92      37.249  27.968  95.151  1.00109.77           O  
ANISOU  736  O   LEU A  92    16083  12449  13177  -1364    751  -1060       O  
ATOM    737  CB  LEU A  92      35.041  25.425  94.803  1.00 77.50           C  
ANISOU  737  CB  LEU A  92    11699   8556   9190   -875    393   -600       C  
ATOM    738  CG  LEU A  92      33.940  24.721  93.992  1.00 72.16           C  
ANISOU  738  CG  LEU A  92    10860   7908   8650   -612    347   -368       C  
ATOM    739  CD1 LEU A  92      33.848  23.256  94.397  1.00 66.00           C  
ANISOU  739  CD1 LEU A  92     9961   7297   7818   -587     34   -315       C  
ATOM    740  CD2 LEU A  92      32.563  25.383  94.104  1.00 60.44           C  
ANISOU  740  CD2 LEU A  92     9477   6249   7238   -478    675   -216       C  
ATOM    741  N   LYS A  93      36.139  27.253  96.987  1.00118.74           N  
ANISOU  741  N   LYS A  93    17404  13637  14075  -1454    745  -1055       N  
ATOM    742  CA  LYS A  93      37.052  27.873  97.937  1.00119.65           C  
ANISOU  742  CA  LYS A  93    17694  13788  13980  -1805    793  -1304       C  
ATOM    743  C   LYS A  93      38.360  27.113  98.080  1.00120.24           C  
ANISOU  743  C   LYS A  93    17607  14153  13925  -1974    393  -1338       C  
ATOM    744  O   LYS A  93      38.375  25.878  98.157  1.00114.07           O  
ANISOU  744  O   LYS A  93    16644  13570  13129  -1881     83  -1190       O  
ATOM    745  CB  LYS A  93      36.380  28.011  99.300  1.00117.68           C  
ANISOU  745  CB  LYS A  93    17673  13505  13536  -1958    959  -1390       C  
ATOM    746  CG  LYS A  93      34.977  28.590  99.241  1.00114.92           C  
ANISOU  746  CG  LYS A  93    17464  12866  13335  -1759   1357  -1294       C  
ATOM    747  CD  LYS A  93      33.957  27.552  98.808  1.00107.04           C  
ANISOU  747  CD  LYS A  93    16285  11920  12466  -1432   1196  -1007       C  
ATOM    748  CE  LYS A  93      32.631  28.215  98.520  1.00107.19           C  
ANISOU  748  CE  LYS A  93    16393  11661  12675  -1215   1596   -850       C  
ATOM    749  NZ  LYS A  93      32.794  29.253  97.469  1.00109.05           N  
ANISOU  749  NZ  LYS A  93    16600  11713  13122  -1137   1863   -830       N  
ATOM    750  N   GLY A  94      39.454  27.871  98.119  1.00124.37           N  
ANISOU  750  N   GLY A  94    18189  14690  14375  -2223    425  -1518       N  
ATOM    751  CA  GLY A  94      40.779  27.311  98.298  1.00127.65           C  
ANISOU  751  CA  GLY A  94    18450  15383  14667  -2416     79  -1528       C  
ATOM    752  C   GLY A  94      41.568  27.227  97.005  1.00126.95           C  
ANISOU  752  C   GLY A  94    18162  15289  14784  -2272    -51  -1451       C  
ATOM    753  O   GLY A  94      42.296  26.256  96.783  1.00125.71           O  
ANISOU  753  O   GLY A  94    17785  15338  14641  -2245   -372  -1324       O  
ATOM    754  N   GLY A  95      41.421  28.242  96.155  1.00122.44           N  
ANISOU  754  N   GLY A  95    17658  14478  14386  -2174    222  -1511       N  
ATOM    755  CA  GLY A  95      42.108  28.295  94.871  1.00111.91           C  
ANISOU  755  CA  GLY A  95    16147  13125  13248  -2028    140  -1443       C  
ATOM    756  C   GLY A  95      41.601  27.284  93.855  1.00100.58           C  
ANISOU  756  C   GLY A  95    14497  11732  11987  -1696    -20  -1225       C  
ATOM    757  O   GLY A  95      42.327  26.917  92.927  1.00 92.16           O  
ANISOU  757  O   GLY A  95    13250  10732  11035  -1604   -185  -1156       O  
ATOM    758  N   LEU A  96      40.345  26.861  94.016  1.00 95.30           N  
ANISOU  758  N   LEU A  96    13854  11019  11336  -1530     49  -1124       N  
ATOM    759  CA  LEU A  96      39.808  25.698  93.300  1.00 83.40           C  
ANISOU  759  CA  LEU A  96    12152   9596   9941  -1280   -136   -938       C  
ATOM    760  C   LEU A  96      38.758  26.042  92.236  1.00 76.69           C  
ANISOU  760  C   LEU A  96    11261   8615   9262  -1022     66   -815       C  
ATOM    761  O   LEU A  96      37.570  26.220  92.541  1.00 63.54           O  
ANISOU  761  O   LEU A  96     9682   6855   7604   -931    248   -741       O  
ATOM    762  CB  LEU A  96      39.238  24.693  94.308  1.00 72.67           C  
ANISOU  762  CB  LEU A  96    10797   8350   8466  -1296   -281   -876       C  
ATOM    763  CG  LEU A  96      38.935  23.270  93.834  1.00 65.49           C  
ANISOU  763  CG  LEU A  96     9676   7555   7652  -1110   -516   -715       C  
ATOM    764  CD1 LEU A  96      40.170  22.617  93.228  1.00 64.63           C  
ANISOU  764  CD1 LEU A  96     9375   7568   7613  -1132   -747   -696       C  
ATOM    765  CD2 LEU A  96      38.392  22.426  94.985  1.00 55.18           C  
ANISOU  765  CD2 LEU A  96     8385   6343   6237  -1142   -620   -655       C  
ATOM    766  N   ARG A  97      39.207  26.121  90.985  1.00 77.60           N  
ANISOU  766  N   ARG A  97    11226   8746   9511   -909     31   -768       N  
ATOM    767  CA  ARG A  97      38.328  26.471  89.867  1.00 78.37           C  
ANISOU  767  CA  ARG A  97    11239   8786   9753   -688    204   -620       C  
ATOM    768  C   ARG A  97      38.001  25.234  89.056  1.00 73.03           C  
ANISOU  768  C   ARG A  97    10364   8268   9117   -540    -22   -498       C  
ATOM    769  O   ARG A  97      38.903  24.572  88.526  1.00 75.38           O  
ANISOU  769  O   ARG A  97    10536   8669   9435   -557   -234   -534       O  
ATOM    770  CB  ARG A  97      38.964  27.554  88.967  1.00 78.58           C  
ANISOU  770  CB  ARG A  97    11229   8732   9895   -668    371   -643       C  
ATOM    771  CG  ARG A  97      38.694  27.408  87.462  1.00 72.89           C  
ANISOU  771  CG  ARG A  97    10296   8098   9299   -462    360   -480       C  
ATOM    772  CD  ARG A  97      39.327  28.516  86.607  1.00 81.08           C  
ANISOU  772  CD  ARG A  97    11282   9064  10460   -430    538   -479       C  
ATOM    773  NE  ARG A  97      38.435  29.666  86.424  1.00 93.26           N  
ANISOU  773  NE  ARG A  97    12855  10460  12120   -326    917   -346       N  
ATOM    774  CZ  ARG A  97      38.358  30.394  85.308  1.00 97.30           C  
ANISOU  774  CZ  ARG A  97    13219  10974  12778   -184   1096   -195       C  
ATOM    775  NH1 ARG A  97      37.514  31.420  85.225  1.00 99.97           N  
ANISOU  775  NH1 ARG A  97    13563  11169  13251    -82   1474    -29       N  
ATOM    776  NH2 ARG A  97      39.115  30.092  84.265  1.00 91.55           N  
ANISOU  776  NH2 ARG A  97    12320  10391  12072   -135    917   -186       N  
ATOM    777  N   ILE A  98      36.708  24.925  88.967  1.00 64.47           N  
ANISOU  777  N   ILE A  98     9254   7193   8048   -409     42   -353       N  
ATOM    778  CA  ILE A  98      36.248  23.773  88.203  1.00 66.71           C  
ANISOU  778  CA  ILE A  98     9362   7627   8358   -299   -141   -252       C  
ATOM    779  C   ILE A  98      35.584  24.202  86.867  1.00 44.76           C  
ANISOU  779  C   ILE A  98     6442   4907   5656   -154    -11    -90       C  
ATOM    780  O   ILE A  98      34.491  24.757  86.845  1.00 53.34           O  
ANISOU  780  O   ILE A  98     7541   5955   6772    -63    192     76       O  
ATOM    781  CB  ILE A  98      35.388  22.825  89.111  1.00 75.06           C  
ANISOU  781  CB  ILE A  98    10453   8708   9359   -288   -237   -203       C  
ATOM    782  CG1 ILE A  98      35.275  21.411  88.528  1.00 82.65           C  
ANISOU  782  CG1 ILE A  98    11243   9812  10350   -239   -465   -172       C  
ATOM    783  CG2 ILE A  98      34.040  23.416  89.403  1.00 77.64           C  
ANISOU  783  CG2 ILE A  98    10858   8949   9693   -196     -7    -53       C  
ATOM    784  CD1 ILE A  98      34.370  21.292  87.332  1.00 84.73           C  
ANISOU  784  CD1 ILE A  98    11369  10173  10653   -125   -419    -35       C  
ATOM    785  N   ASP A  99      36.292  23.982  85.761  1.00 36.98           N  
ANISOU  785  N   ASP A  99     5315   4030   4705   -140   -114   -118       N  
ATOM    786  CA  ASP A  99      35.799  24.355  84.437  1.00 42.84           C  
ANISOU  786  CA  ASP A  99     5896   4891   5489    -31    -16     39       C  
ATOM    787  C   ASP A  99      35.071  23.211  83.700  1.00 50.35           C  
ANISOU  787  C   ASP A  99     6692   6045   6392      0   -170    116       C  
ATOM    788  O   ASP A  99      35.549  22.083  83.648  1.00 63.91           O  
ANISOU  788  O   ASP A  99     8378   7817   8088    -61   -376    -13       O  
ATOM    789  CB  ASP A  99      36.949  24.853  83.586  1.00 54.30           C  
ANISOU  789  CB  ASP A  99     7279   6360   6991    -42    -15    -34       C  
ATOM    790  CG  ASP A  99      37.488  26.179  84.054  1.00 68.88           C  
ANISOU  790  CG  ASP A  99     9246   8020   8904    -69    196    -76       C  
ATOM    791  OD1 ASP A  99      36.728  27.161  84.105  1.00 73.60           O  
ANISOU  791  OD1 ASP A  99     9869   8533   9564      4    467     66       O  
ATOM    792  OD2 ASP A  99      38.689  26.241  84.358  1.00 82.15           O  
ANISOU  792  OD2 ASP A  99    10990   9636  10588   -170    107   -243       O  
ATOM    793  N   ILE A 100      33.910  23.493  83.142  1.00 43.55           N  
ANISOU  793  N   ILE A 100     5725   5300   5523     84    -50    340       N  
ATOM    794  CA  ILE A 100      33.124  22.471  82.494  1.00 45.77           C  
ANISOU  794  CA  ILE A 100     5867   5791   5732     77   -182    421       C  
ATOM    795  C   ILE A 100      32.854  22.774  81.046  1.00 48.82           C  
ANISOU  795  C   ILE A 100     6040   6431   6077    100   -140    574       C  
ATOM    796  O   ILE A 100      32.407  23.837  80.723  1.00 48.82           O  
ANISOU  796  O   ILE A 100     5960   6474   6115    188     65    810       O  
ATOM    797  CB  ILE A 100      31.804  22.337  83.196  1.00 20.00           C  
ATOM    798  CG1 ILE A 100      32.038  22.398  84.677  1.00 20.00           C  
ATOM    799  CG2 ILE A 100      31.147  21.057  82.843  1.00 20.00           C  
ATOM    800  CD1 ILE A 100      30.879  22.802  85.405  1.00 20.00           C  
ATOM    801  N   ALA A 101      33.125  21.815  80.175  1.00 43.93           N  
ANISOU  801  N   ALA A 101     5318   5990   5384     13   -311    453       N  
ATOM    802  CA  ALA A 101      32.874  22.009  78.750  1.00 45.28           C  
ANISOU  802  CA  ALA A 101     5281   6454   5470     -2   -288    584       C  
ATOM    803  C   ALA A 101      32.036  20.900  78.140  1.00 42.19           C  
ANISOU  803  C   ALA A 101     4766   6322   4941   -115   -420    599       C  
ATOM    804  O   ALA A 101      31.909  19.806  78.696  1.00 46.15           O  
ANISOU  804  O   ALA A 101     5347   6748   5441   -186   -547    443       O  
ATOM    805  CB  ALA A 101      34.175  22.188  77.972  1.00 23.87           C  
ANISOU  805  CB  ALA A 101     2540   3754   2774    -25   -314    425       C  
ATOM    806  N   THR A 102      31.470  21.209  76.982  1.00 35.30           N  
ANISOU  806  N   THR A 102     3685   5774   3954   -144   -379    799       N  
ATOM    807  CA  THR A 102      30.642  20.270  76.260  1.00 39.84           C  
ANISOU  807  CA  THR A 102     4120   6659   4358   -297   -493    824       C  
ATOM    808  C   THR A 102      31.458  19.676  75.146  1.00 41.79           C  
ANISOU  808  C   THR A 102     4307   7074   4498   -443   -581    592       C  
ATOM    809  O   THR A 102      32.006  20.410  74.325  1.00 62.72           O  
ANISOU  809  O   THR A 102     6860   9847   7122   -411   -513    652       O  
ATOM    810  CB  THR A 102      29.408  20.953  75.649  1.00 51.98           C  
ANISOU  810  CB  THR A 102     5431   8522   5798   -275   -397   1236       C  
ATOM    811  OG1 THR A 102      28.758  21.766  76.641  1.00 62.61           O  
ANISOU  811  OG1 THR A 102     6836   9666   7288   -104   -238   1488       O  
ATOM    812  CG2 THR A 102      28.457  19.907  75.161  1.00 53.63           C  
ANISOU  812  CG2 THR A 102     5519   9036   5822   -465   -534   1256       C  
ATOM    813  N   ALA A 103      31.570  18.350  75.136  1.00 33.33           N  
ANISOU  813  N   ALA A 103     3296   5985   3383   -597   -705    324       N  
ATOM    814  CA  ALA A 103      32.249  17.646  74.059  1.00 38.53           C  
ANISOU  814  CA  ALA A 103     3912   6792   3937   -767   -753     79       C  
ATOM    815  C   ALA A 103      31.342  17.647  72.832  1.00 59.90           C  
ANISOU  815  C   ALA A 103     6395   9978   6385   -934   -764    238       C  
ATOM    816  O   ALA A 103      30.126  17.396  72.940  1.00 61.26           O  
ANISOU  816  O   ALA A 103     6480  10335   6460  -1006   -801    410       O  
ATOM    817  CB  ALA A 103      32.587  16.228  74.475  1.00 29.01           C  
ANISOU  817  CB  ALA A 103     2834   5386   2801   -882   -825   -240       C  
ATOM    818  N   ARG A 104      31.938  17.871  71.678  1.00 69.07           N  
ANISOU  818  N   ARG A 104     7456  11360   7429  -1007   -738    189       N  
ATOM    819  CA  ARG A 104      31.260  18.045  70.404  1.00 83.91           C  
ANISOU  819  CA  ARG A 104     9089  13760   9034  -1167   -742    383       C  
ATOM    820  C   ARG A 104      30.635  16.841  69.711  1.00 97.84           C  
ANISOU  820  C   ARG A 104    10793  15818  10563  -1482   -833    237       C  
ATOM    821  O   ARG A 104      30.822  15.706  70.100  1.00 96.70           O  
ANISOU  821  O   ARG A 104    10801  15444  10497  -1564   -880    -16       O  
ATOM    822  CB  ARG A 104      32.218  18.716  69.445  1.00 98.21           C  
ANISOU  822  CB  ARG A 104    10823  15712  10782  -1165   -687    335       C  
ATOM    823  CG  ARG A 104      33.628  18.222  69.606  1.00117.60           C  
ANISOU  823  CG  ARG A 104    13492  17766  13426  -1102   -671    -17       C  
ATOM    824  CD  ARG A 104      34.459  18.638  68.426  1.00129.99           C  
ANISOU  824  CD  ARG A 104    14975  19507  14910  -1123   -619    -68       C  
ATOM    825  NE  ARG A 104      33.940  19.862  67.842  1.00133.94           N  
ANISOU  825  NE  ARG A 104    15220  20393  15279  -1064   -567    314       N  
ATOM    826  CZ  ARG A 104      34.636  20.657  67.047  1.00133.21           C  
ANISOU  826  CZ  ARG A 104    15015  20422  15175   -981   -496    403       C  
ATOM    827  NH1 ARG A 104      35.893  20.373  66.753  1.00128.46           N  
ANISOU  827  NH1 ARG A 104    14550  19577  14681   -947   -477    128       N  
ATOM    828  NH2 ARG A 104      34.073  21.746  66.558  1.00136.42           N  
ANISOU  828  NH2 ARG A 104    15156  21195  15482   -920   -432    799       N  
ATOM    829  N   LEU A 105      29.862  17.136  68.673  1.00112.73           N  
ANISOU  829  N   LEU A 105    12440  18232  12159  -1666   -848    413       N  
ATOM    830  CA  LEU A 105      29.081  16.141  67.923  1.00109.57           C  
ANISOU  830  CA  LEU A 105    11943  18225  11464  -2028   -929    299       C  
ATOM    831  C   LEU A 105      29.425  14.691  68.273  1.00 98.32           C  
ANISOU  831  C   LEU A 105    10743  16504  10109  -2201   -950   -179       C  
ATOM    832  O   LEU A 105      29.525  13.829  67.395  1.00 89.88           O  
ANISOU  832  O   LEU A 105     9672  15644   8835  -2516   -948   -471       O  
ATOM    833  CB  LEU A 105      29.251  16.352  66.406  1.00117.33           C  
ANISOU  833  CB  LEU A 105    12725  19726  12129  -2249   -921    316       C  
ATOM    834  CG  LEU A 105      29.012  17.707  65.717  1.00116.25           C  
ANISOU  834  CG  LEU A 105    12299  19986  11883  -2128   -878    791       C  
ATOM    835  CD1 LEU A 105      30.212  18.634  65.905  1.00109.10           C  
ANISOU  835  CD1 LEU A 105    11478  18743  11233  -1813   -771    795       C  
ATOM    836  CD2 LEU A 105      28.699  17.524  64.217  1.00113.66           C  
ANISOU  836  CD2 LEU A 105    11726  20328  11130  -2477   -921    824       C  
ATOM    837  N   ASP A 116      35.877   1.714  72.805  1.00111.28           N  
ANISOU  837  N   ASP A 116    13766  13800  14715  -2582    679  -3301       N  
ATOM    838  CA  ASP A 116      35.052   2.643  72.019  1.00119.44           C  
ANISOU  838  CA  ASP A 116    14770  15331  15282  -2718    466  -3253       C  
ATOM    839  C   ASP A 116      33.602   2.206  72.046  1.00124.21           C  
ANISOU  839  C   ASP A 116    15326  16160  15708  -2924    389  -3284       C  
ATOM    840  O   ASP A 116      32.973   2.056  70.985  1.00123.51           O  
ANISOU  840  O   ASP A 116    15228  16402  15300  -3264    413  -3479       O  
ATOM    841  CB  ASP A 116      35.516   2.724  70.559  1.00122.56           C  
ANISOU  841  CB  ASP A 116    15211  15915  15442  -2979    600  -3520       C  
ATOM    842  CG  ASP A 116      37.004   2.978  70.439  1.00116.66           C  
ANISOU  842  CG  ASP A 116    14519  14901  14906  -2805    723  -3528       C  
ATOM    843  OD1 ASP A 116      37.389   4.035  69.870  1.00108.68           O  
ANISOU  843  OD1 ASP A 116    13493  14119  13681  -2743    599  -3428       O  
ATOM    844  OD2 ASP A 116      37.790   2.098  70.896  1.00119.28           O  
ANISOU  844  OD2 ASP A 116    14895  14790  15636  -2734    961  -3619       O  
ATOM    845  N   VAL A 117      32.993   2.108  73.197  1.00124.39           N  
ANISOU  845  N   VAL A 117    15313  16026  15925  -2735    292  -3087       N  
ATOM    846  CA  VAL A 117      31.603   1.707  73.195  1.00122.95           C  
ANISOU  846  CA  VAL A 117    15071  16063  15581  -2869    168  -3030       C  
ATOM    847  C   VAL A 117      30.641   2.627  72.408  1.00150.17           C  
ANISOU  847  C   VAL A 117    18455  20056  18547  -3090     -5  -2969       C  
ATOM    848  O   VAL A 117      29.725   2.143  71.754  1.00152.48           O  
ANISOU  848  O   VAL A 117    18739  20579  18618  -3473     87  -3232       O  
ATOM    849  CB  VAL A 117      31.089   1.632  74.620  1.00107.71           C  
ANISOU  849  CB  VAL A 117    13105  13967  13854  -2543      3  -2705       C  
ATOM    850  CG1 VAL A 117      32.109   0.962  75.497  1.00 94.60           C  
ANISOU  850  CG1 VAL A 117    11460  11842  12643  -2442    201  -2798       C  
ATOM    851  CG2 VAL A 117      30.766   3.025  75.116  1.00103.97           C  
ANISOU  851  CG2 VAL A 117    12561  13753  13189  -2630   -170  -2561       C  
ATOM    852  N   GLU A 118      30.856   3.930  72.367  1.00140.84           N  
ANISOU  852  N   GLU A 118    17217  19084  17211  -2867   -236  -2618       N  
ATOM    853  CA  GLU A 118      29.903   4.705  71.593  1.00126.54           C  
ANISOU  853  CA  GLU A 118    15303  17797  14981  -3022   -395  -2466       C  
ATOM    854  C   GLU A 118      29.923   6.120  72.165  1.00109.16           C  
ANISOU  854  C   GLU A 118    13052  15681  12742  -2693   -585  -2053       C  
ATOM    855  O   GLU A 118      29.909   7.107  71.448  1.00 93.63           O  
ANISOU  855  O   GLU A 118    10999  14060  10515  -2725   -667  -1903       O  
ATOM    856  CB  GLU A 118      28.625   3.921  71.568  1.00131.10           C  
ANISOU  856  CB  GLU A 118    15791  18683  15337  -3326   -459  -2482       C  
ATOM    857  CG  GLU A 118      28.199   3.483  72.964  1.00139.70           C  
ANISOU  857  CG  GLU A 118    16910  19472  16698  -3293   -420  -2528       C  
ATOM    858  CD  GLU A 118      26.698   3.605  73.184  1.00138.43           C  
ANISOU  858  CD  GLU A 118    16743  19108  16747  -2894   -569  -2165       C  
ATOM    859  OE1 GLU A 118      25.917   2.972  72.428  1.00141.30           O  
ANISOU  859  OE1 GLU A 118    17047  19529  17111  -2904   -668  -2016       O  
ATOM    860  OE2 GLU A 118      26.302   4.340  74.116  1.00130.25           O  
ANISOU  860  OE2 GLU A 118    15762  17854  15873  -2588   -581  -2038       O  
ATOM    861  N   MET A 119      29.959   6.170  73.470  1.00101.94           N  
ANISOU  861  N   MET A 119    12184  14453  12096  -2391   -635  -1872       N  
ATOM    862  CA  MET A 119      29.817   7.401  74.196  1.00 80.46           C  
ANISOU  862  CA  MET A 119     9469  11684   9419  -2071   -747  -1559       C  
ATOM    863  C   MET A 119      31.221   7.961  74.056  1.00 79.93           C  
ANISOU  863  C   MET A 119     9473  11431   9466  -1960   -659  -1673       C  
ATOM    864  O   MET A 119      31.639   8.869  74.743  1.00 64.11           O  
ANISOU  864  O   MET A 119     7518   9227   7614  -1697   -695  -1521       O  
ATOM    865  CB  MET A 119      29.423   7.162  75.648  1.00 69.78           C  
ANISOU  865  CB  MET A 119     8165  10032   8315  -1821   -803  -1391       C  
ATOM    866  CG  MET A 119      28.449   8.193  76.161  1.00 70.99           C  
ANISOU  866  CG  MET A 119     8249  10334   8390  -1849   -914  -1190       C  
ATOM    867  SD  MET A 119      26.945   7.528  76.888  1.00199.79           S  
ANISOU  867  SD  MET A 119    24439  27052  24421  -1800  -1052   -790       S  
ATOM    868  CE  MET A 119      25.875   8.956  77.021  1.00 47.34           C  
ANISOU  868  CE  MET A 119     5082   7743   5162  -1744  -1150   -544       C  
ATOM    869  N   SER A 120      31.938   7.333  73.133  1.00 99.09           N  
ANISOU  869  N   SER A 120    11908  13923  11818  -2181   -534  -1951       N  
ATOM    870  CA  SER A 120      33.313   7.683  72.797  1.00 94.11           C  
ANISOU  870  CA  SER A 120    11332  13141  11285  -2084   -451  -2041       C  
ATOM    871  C   SER A 120      33.368   8.718  71.637  1.00 80.60           C  
ANISOU  871  C   SER A 120     9542  11810   9271  -2164   -506  -1974       C  
ATOM    872  O   SER A 120      33.634   8.473  70.453  1.00 48.87           O  
ANISOU  872  O   SER A 120     5506   7985   5076  -2401   -422  -2186       O  
ATOM    873  CB  SER A 120      34.195   6.442  72.759  1.00 76.25           C  
ANISOU  873  CB  SER A 120     9151  10542   9278  -2168   -243  -2350       C  
ATOM    874  OG  SER A 120      33.909   5.718  73.963  1.00 50.59           O  
ANISOU  874  OG  SER A 120     5921   7011   6291  -2053   -237  -2299       O  
ATOM    875  N   THR A 121      32.999   9.897  72.122  1.00 92.41           N  
ANISOU  875  N   THR A 121    10984  13408  10718  -1956   -644  -1647       N  
ATOM    876  CA  THR A 121      32.844  11.160  71.473  1.00 80.39           C  
ANISOU  876  CA  THR A 121     9350  12215   8978  -1920   -725  -1430       C  
ATOM    877  C   THR A 121      33.844  11.980  72.275  1.00 70.17           C  
ANISOU  877  C   THR A 121     8135  10610   7915  -1612   -730  -1314       C  
ATOM    878  O   THR A 121      34.229  13.080  71.857  1.00 68.43           O  
ANISOU  878  O   THR A 121     7858  10517   7625  -1511   -747  -1170       O  
ATOM    879  CB  THR A 121      31.424  11.723  71.805  1.00 63.39           C  
ANISOU  879  CB  THR A 121     7079  10327   6681  -1898   -847  -1106       C  
ATOM    880  OG1 THR A 121      30.402  10.768  71.451  1.00 57.58           O  
ANISOU  880  OG1 THR A 121     6286   9803   5787  -2174   -860  -1200       O  
ATOM    881  CG2 THR A 121      31.169  13.077  71.130  1.00 59.62           C  
ANISOU  881  CG2 THR A 121     6441  10205   6005  -1836   -885   -800       C  
ATOM    882  N   ILE A 122      34.239  11.456  73.448  1.00 58.40           N  
ANISOU  882  N   ILE A 122     6761   8731   6697  -1468   -707  -1355       N  
ATOM    883  CA  ILE A 122      35.358  12.041  74.186  1.00 65.40           C  
ANISOU  883  CA  ILE A 122     7727   9326   7795  -1235   -704  -1295       C  
ATOM    884  C   ILE A 122      36.592  11.778  73.361  1.00 65.28           C  
ANISOU  884  C   ILE A 122     7733   9238   7831  -1295   -606  -1501       C  
ATOM    885  O   ILE A 122      37.482  12.622  73.303  1.00 68.36           O  
ANISOU  885  O   ILE A 122     8134   9568   8272  -1166   -616  -1436       O  
ATOM    886  CB  ILE A 122      35.648  11.411  75.582  1.00 69.45           C  
ANISOU  886  CB  ILE A 122     8332   9481   8575  -1100   -701  -1291       C  
ATOM    887  CG1 ILE A 122      34.711  10.253  75.855  1.00 60.19           C  
ANISOU  887  CG1 ILE A 122     7149   8300   7422  -1220   -688  -1370       C  
ATOM    888  CG2 ILE A 122      35.809  12.506  76.732  1.00 19.57           C  
ANISOU  888  CG2 ILE A 122     2065   3037   2335   -872   -782  -1061       C  
ATOM    889  CD1 ILE A 122      35.179   9.021  75.149  1.00 71.35           C  
ANISOU  889  CD1 ILE A 122     8568   9634   8908  -1407   -548  -1661       C  
ATOM    890  N   LYS A 123      36.652  10.610  72.722  1.00 56.75           N  
ANISOU  890  N   LYS A 123     6665   8150   6749  -1502   -496  -1759       N  
ATOM    891  CA  LYS A 123      37.770  10.326  71.824  1.00 50.09           C  
ANISOU  891  CA  LYS A 123     5849   7239   5943  -1585   -371  -1973       C  
ATOM    892  C   LYS A 123      37.965  11.415  70.750  1.00 46.71           C  
ANISOU  892  C   LYS A 123     5348   7117   5283  -1598   -407  -1902       C  
ATOM    893  O   LYS A 123      39.089  11.812  70.477  1.00 58.86           O  
ANISOU  893  O   LYS A 123     6910   8537   6918  -1495   -353  -1914       O  
ATOM    894  CB  LYS A 123      37.683   8.933  71.201  1.00 42.95           C  
ANISOU  894  CB  LYS A 123     4978   6291   5049  -1849   -202  -2290       C  
ATOM    895  CG  LYS A 123      38.859   8.653  70.285  1.00 36.83           C  
ANISOU  895  CG  LYS A 123     4250   5413   4330  -1926    -29  -2507       C  
ATOM    896  CD  LYS A 123      38.994   7.210  69.875  1.00 44.12           C  
ANISOU  896  CD  LYS A 123     5240   6160   5364  -2159    213  -2837       C  
ATOM    897  CE  LYS A 123      39.781   7.080  68.568  1.00 50.60           C  
ANISOU  897  CE  LYS A 123     6097   7039   6089  -2314    403  -3063       C  
ATOM    898  NZ  LYS A 123      40.338   5.711  68.359  1.00 56.13           N  
ANISOU  898  NZ  LYS A 123     6891   7403   7031  -2466    719  -3368       N  
ATOM    899  N   LYS A 124      36.878  11.911  70.169  1.00 45.06           N  
ANISOU  899  N   LYS A 124     5027   7309   4783  -1707   -485  -1782       N  
ATOM    900  CA  LYS A 124      36.934  13.072  69.276  1.00 53.73           C  
ANISOU  900  CA  LYS A 124     6009   8729   5676  -1672   -514  -1614       C  
ATOM    901  C   LYS A 124      37.327  14.361  70.009  1.00 56.13           C  
ANISOU  901  C   LYS A 124     6307   8899   6122  -1369   -574  -1337       C  
ATOM    902  O   LYS A 124      37.885  15.272  69.400  1.00 68.34           O  
ANISOU  902  O   LYS A 124     7788  10554   7624  -1282   -552  -1236       O  
ATOM    903  CB  LYS A 124      35.604  13.289  68.533  1.00 57.94           C  
ANISOU  903  CB  LYS A 124     6381   9762   5871  -1864   -578  -1482       C  
ATOM    904  CG  LYS A 124      35.077  12.070  67.798  1.00 76.50           C  
ANISOU  904  CG  LYS A 124     8733  12302   8031  -2221   -524  -1762       C  
ATOM    905  CD  LYS A 124      34.293  12.477  66.547  1.00 95.60           C  
ANISOU  905  CD  LYS A 124    10959  15317  10046  -2454   -565  -1654       C  
ATOM    906  CE  LYS A 124      33.272  11.410  66.121  1.00105.32           C  
ANISOU  906  CE  LYS A 124    12162  16812  11043  -2831   -568  -1839       C  
ATOM    907  NZ  LYS A 124      32.034  11.395  66.976  1.00106.40           N  
ANISOU  907  NZ  LYS A 124    12239  16997  11192  -2795   -692  -1607       N  
ATOM    908  N   ASP A 125      37.019  14.437  71.304  1.00 41.37           N  
ANISOU  908  N   ASP A 125     4502   6798   4417  -1225   -636  -1222       N  
ATOM    909  CA  ASP A 125      37.421  15.567  72.140  1.00 40.51           C  
ANISOU  909  CA  ASP A 125     4423   6516   4452   -977   -667  -1013       C  
ATOM    910  C   ASP A 125      38.912  15.474  72.493  1.00 51.07           C  
ANISOU  910  C   ASP A 125     5864   7522   6020   -874   -631  -1134       C  
ATOM    911  O   ASP A 125      39.648  16.460  72.429  1.00 44.77           O  
ANISOU  911  O   ASP A 125     5056   6678   5276   -739   -619  -1034       O  
ATOM    912  CB  ASP A 125      36.594  15.602  73.430  1.00 33.51           C  
ANISOU  912  CB  ASP A 125     3588   5502   3643   -890   -730   -875       C  
ATOM    913  CG  ASP A 125      36.872  16.832  74.273  1.00 41.69           C  
ANISOU  913  CG  ASP A 125     4665   6385   4790   -678   -730   -675       C  
ATOM    914  OD1 ASP A 125      36.249  17.887  74.043  1.00 47.56           O  
ANISOU  914  OD1 ASP A 125     5319   7308   5443   -608   -698   -444       O  
ATOM    915  OD2 ASP A 125      37.708  16.743  75.191  1.00 52.82           O  
ANISOU  915  OD2 ASP A 125     6188   7497   6383   -593   -746   -741       O  
ATOM    916  N   LEU A 126      39.328  14.273  72.872  1.00 50.25           N  
ANISOU  916  N   LEU A 126     5840   7189   6063   -941   -602  -1327       N  
ATOM    917  CA  LEU A 126      40.686  13.990  73.263  1.00 48.61           C  
ANISOU  917  CA  LEU A 126     5703   6674   6094   -860   -558  -1404       C  
ATOM    918  C   LEU A 126      41.642  14.121  72.073  1.00 53.93           C  
ANISOU  918  C   LEU A 126     6349   7398   6745   -891   -464  -1504       C  
ATOM    919  O   LEU A 126      42.752  14.646  72.206  1.00 48.89           O  
ANISOU  919  O   LEU A 126     5727   6604   6244   -765   -456  -1448       O  
ATOM    920  CB  LEU A 126      40.746  12.583  73.842  1.00 47.83           C  
ANISOU  920  CB  LEU A 126     5655   6349   6169   -931   -506  -1547       C  
ATOM    921  CG  LEU A 126      40.603  12.306  75.354  1.00 47.20           C  
ANISOU  921  CG  LEU A 126     5615   6060   6258   -813   -563  -1421       C  
ATOM    922  CD1 LEU A 126      39.932  13.395  76.143  1.00 33.29           C  
ANISOU  922  CD1 LEU A 126     3867   4378   4403   -696   -677  -1211       C  
ATOM    923  CD2 LEU A 126      39.899  10.979  75.590  1.00 52.48           C  
ANISOU  923  CD2 LEU A 126     6282   6671   6987   -922   -504  -1533       C  
ATOM    924  N   TYR A 127      41.213  13.650  70.906  1.00 46.76           N  
ANISOU  924  N   TYR A 127     5397   6721   5649  -1075   -391  -1652       N  
ATOM    925  CA  TYR A 127      42.069  13.667  69.719  1.00 49.37           C  
ANISOU  925  CA  TYR A 127     5709   7114   5935  -1129   -280  -1771       C  
ATOM    926  C   TYR A 127      42.370  15.099  69.279  1.00 58.69           C  
ANISOU  926  C   TYR A 127     6807   8465   7029   -985   -332  -1572       C  
ATOM    927  O   TYR A 127      43.402  15.377  68.668  1.00 63.87           O  
ANISOU  927  O   TYR A 127     7456   9069   7742   -930   -264  -1600       O  
ATOM    928  CB  TYR A 127      41.398  12.894  68.589  1.00 39.24           C  
ANISOU  928  CB  TYR A 127     4398   6099   4414  -1402   -192  -1982       C  
ATOM    929  CG  TYR A 127      42.259  12.577  67.382  1.00 52.05           C  
ANISOU  929  CG  TYR A 127     6033   7751   5991  -1512    -31  -2179       C  
ATOM    930  CD1 TYR A 127      42.033  13.201  66.161  1.00 64.24           C  
ANISOU  930  CD1 TYR A 127     7474   9693   7241  -1608    -32  -2157       C  
ATOM    931  CD2 TYR A 127      43.268  11.628  67.447  1.00 63.30           C  
ANISOU  931  CD2 TYR A 127     7562   8819   7670  -1524    144  -2368       C  
ATOM    932  CE1 TYR A 127      42.799  12.905  65.043  1.00 68.55           C  
ANISOU  932  CE1 TYR A 127     8040  10281   7724  -1719    125  -2346       C  
ATOM    933  CE2 TYR A 127      44.041  11.320  66.330  1.00 70.22           C  
ANISOU  933  CE2 TYR A 127     8466   9702   8513  -1627    326  -2553       C  
ATOM    934  CZ  TYR A 127      43.800  11.962  65.131  1.00 70.82           C  
ANISOU  934  CZ  TYR A 127     8458  10179   8270  -1730    311  -2557       C  
ATOM    935  OH  TYR A 127      44.554  11.659  64.016  1.00 66.49           O  
ANISOU  935  OH  TYR A 127     7944   9651   7668  -1841    501  -2749       O  
ATOM    936  N   ARG A 128      41.466  16.012  69.596  1.00 53.44           N  
ANISOU  936  N   ARG A 128     6070   7987   6249   -915   -428  -1354       N  
ATOM    937  CA  ARG A 128      41.638  17.397  69.193  1.00 46.73           C  
ANISOU  937  CA  ARG A 128     5118   7292   5344   -775   -438  -1139       C  
ATOM    938  C   ARG A 128      42.699  18.148  70.026  1.00 48.72           C  
ANISOU  938  C   ARG A 128     5437   7230   5843   -566   -453  -1047       C  
ATOM    939  O   ARG A 128      42.943  19.339  69.826  1.00 43.53           O  
ANISOU  939  O   ARG A 128     4710   6635   5195   -436   -438   -876       O  
ATOM    940  CB  ARG A 128      40.291  18.125  69.249  1.00 37.29           C  
ANISOU  940  CB  ARG A 128     3808   6384   3978   -767   -486   -903       C  
ATOM    941  CG  ARG A 128      39.381  17.853  68.070  1.00 67.57           C  
ANISOU  941  CG  ARG A 128     7498  10666   7510   -969   -477   -900       C  
ATOM    942  CD  ARG A 128      38.380  18.994  67.906  1.00 88.30           C  
ANISOU  942  CD  ARG A 128     9941  13604  10005   -893   -489   -550       C  
ATOM    943  NE  ARG A 128      37.759  19.341  69.182  1.00107.29           N  
ANISOU  943  NE  ARG A 128    12408  15809  12548   -764   -522   -393       N  
ATOM    944  CZ  ARG A 128      38.159  20.339  69.967  1.00113.36           C  
ANISOU  944  CZ  ARG A 128    13223  16333  13514   -547   -484   -247       C  
ATOM    945  NH1 ARG A 128      37.536  20.572  71.117  1.00108.23           N  
ANISOU  945  NH1 ARG A 128    12646  15514  12963   -464   -494   -134       N  
ATOM    946  NH2 ARG A 128      39.177  21.107  69.599  1.00117.13           N  
ANISOU  946  NH2 ARG A 128    13679  16736  14090   -427   -424   -221       N  
ATOM    947  N   ARG A 129      43.320  17.451  70.966  1.00 44.03           N  
ANISOU  947  N   ARG A 129     4963   6313   5452   -548   -473  -1145       N  
ATOM    948  CA  ARG A 129      44.190  18.112  71.915  1.00 41.27           C  
ANISOU  948  CA  ARG A 129     4671   5710   5300   -399   -512  -1046       C  
ATOM    949  C   ARG A 129      45.626  18.137  71.445  1.00 47.85           C  
ANISOU  949  C   ARG A 129     5506   6401   6275   -347   -460  -1092       C  
ATOM    950  O   ARG A 129      45.886  17.776  70.305  1.00 66.56           O  
ANISOU  950  O   ARG A 129     7832   8880   8576   -409   -378  -1193       O  
ATOM    951  CB  ARG A 129      44.050  17.467  73.278  1.00 41.16           C  
ANISOU  951  CB  ARG A 129     4751   5478   5411   -407   -578  -1062       C  
ATOM    952  CG  ARG A 129      42.826  17.970  74.008  1.00 33.41           C  
ANISOU  952  CG  ARG A 129     3779   4584   4331   -387   -632   -940       C  
ATOM    953  CD  ARG A 129      42.445  17.024  75.132  1.00 46.77           C  
ANISOU  953  CD  ARG A 129     5545   6125   6100   -430   -688   -985       C  
ATOM    954  NE  ARG A 129      41.056  17.215  75.510  1.00 41.38           N  
ANISOU  954  NE  ARG A 129     4859   5574   5291   -442   -717   -895       N  
ATOM    955  CZ  ARG A 129      40.644  18.144  76.361  1.00 44.67           C  
ANISOU  955  CZ  ARG A 129     5316   5954   5703   -356   -735   -748       C  
ATOM    956  NH1 ARG A 129      39.348  18.252  76.635  1.00 54.96           N  
ANISOU  956  NH1 ARG A 129     6607   7370   6905   -361   -737   -647       N  
ATOM    957  NH2 ARG A 129      41.525  18.959  76.944  1.00 35.75           N  
ANISOU  957  NH2 ARG A 129     4241   4669   4673   -280   -734   -703       N  
ATOM    958  N   ASP A 130      46.564  18.655  72.251  1.00 42.14           N  
ANISOU  958  N   ASP A 130     4828   5451   5734   -249   -504  -1011       N  
ATOM    959  CA  ASP A 130      47.949  18.861  71.763  1.00 33.13           C  
ANISOU  959  CA  ASP A 130     3666   4191   4731   -180   -464   -997       C  
ATOM    960  C   ASP A 130      49.001  17.738  71.872  1.00 38.50           C  
ANISOU  960  C   ASP A 130     4377   4662   5589   -222   -408  -1090       C  
ATOM    961  O   ASP A 130      49.525  17.297  70.849  1.00 57.73           O  
ANISOU  961  O   ASP A 130     6794   7127   8013   -269   -291  -1205       O  
ATOM    962  CB  ASP A 130      48.524  20.145  72.373  1.00 37.42           C  
ANISOU  962  CB  ASP A 130     4215   4632   5369    -73   -520   -849       C  
ATOM    963  CG  ASP A 130      48.574  20.098  73.888  1.00 47.53           C  
ANISOU  963  CG  ASP A 130     5577   5743   6739    -97   -616   -807       C  
ATOM    964  OD1 ASP A 130      48.180  19.064  74.466  1.00 32.83           O  
ANISOU  964  OD1 ASP A 130     3742   3826   4907    -60   -653   -717       O  
ATOM    965  OD2 ASP A 130      49.008  21.097  74.501  1.00 52.88           O  
ANISOU  965  OD2 ASP A 130     6287   6349   7456   -165   -640   -864       O  
ATOM    966  N   PHE A 131      49.294  17.254  73.077  1.00 27.27           N  
ANISOU  966  N   PHE A 131     2993   3038   4332   -213   -470  -1028       N  
ATOM    967  CA  PHE A 131      50.188  16.102  73.218  1.00 40.61           C  
ANISOU  967  CA  PHE A 131     4678   4514   6239   -234   -391  -1048       C  
ATOM    968  C   PHE A 131      49.532  14.935  73.990  1.00 39.84           C  
ANISOU  968  C   PHE A 131     4604   4339   6195   -313   -381  -1098       C  
ATOM    969  O   PHE A 131      48.596  15.133  74.773  1.00 25.96           O  
ANISOU  969  O   PHE A 131     2874   2658   4330   -332   -486  -1075       O  
ATOM    970  CB  PHE A 131      51.527  16.550  73.845  1.00 36.04           C  
ANISOU  970  CB  PHE A 131     4067   3776   5850   -157   -449   -872       C  
ATOM    971  CG  PHE A 131      51.947  17.918  73.422  1.00 32.59           C  
ANISOU  971  CG  PHE A 131     3612   3420   5351    -80   -494   -804       C  
ATOM    972  CD1 PHE A 131      52.409  18.146  72.140  1.00 33.65           C  
ANISOU  972  CD1 PHE A 131     3708   3599   5477    -31   -391   -845       C  
ATOM    973  CD2 PHE A 131      51.822  18.991  74.287  1.00 36.07           C  
ANISOU  973  CD2 PHE A 131     4075   3893   5738    -65   -616   -709       C  
ATOM    974  CE1 PHE A 131      52.761  19.409  71.737  1.00 37.04           C  
ANISOU  974  CE1 PHE A 131     4102   4103   5869     54   -418   -767       C  
ATOM    975  CE2 PHE A 131      52.177  20.270  73.893  1.00 30.91           C  
ANISOU  975  CE2 PHE A 131     3400   3290   5055      4   -620   -652       C  
ATOM    976  CZ  PHE A 131      52.644  20.477  72.619  1.00 36.12           C  
ANISOU  976  CZ  PHE A 131     4001   3994   5728     75   -527   -668       C  
ATOM    977  N   THR A 132      50.064  13.750  73.843  1.00 36.52           N  
ANISOU  977  N   THR A 132     4167   3749   5959   -350   -229  -1158       N  
ATOM    978  CA  THR A 132      49.448  12.594  74.447  1.00 33.32           C  
ANISOU  978  CA  THR A 132     3766   3250   5645   -416   -182  -1201       C  
ATOM    979  C   THR A 132      49.343  12.622  75.951  1.00 33.53           C  
ANISOU  979  C   THR A 132     3773   3242   5724   -380   -343  -1025       C  
ATOM    980  O   THR A 132      48.370  12.206  76.491  1.00 33.41           O  
ANISOU  980  O   THR A 132     3781   3281   5632   -423   -393  -1062       O  
ATOM    981  CB  THR A 132      50.146  11.361  74.024  1.00 33.67           C  
ANISOU  981  CB  THR A 132     3777   3054   5961   -439     51  -1239       C  
ATOM    982  OG1 THR A 132      51.478  11.432  74.484  1.00 59.19           O  
ANISOU  982  OG1 THR A 132     6940   6130   9421   -339     56  -1022       O  
ATOM    983  CG2 THR A 132      50.175  11.290  72.576  1.00 24.85           C  
ANISOU  983  CG2 THR A 132     2705   1981   4754   -525    238  -1471       C  
ATOM    984  N   ILE A 133      50.309  13.159  76.642  1.00 35.84           N  
ANISOU  984  N   ILE A 133     4018   3459   6142   -317   -422   -828       N  
ATOM    985  CA  ILE A 133      50.191  13.218  78.073  1.00 41.16           C  
ANISOU  985  CA  ILE A 133     4670   4140   6828   -320   -571   -671       C  
ATOM    986  C   ILE A 133      49.060  14.122  78.452  1.00 41.28           C  
ANISOU  986  C   ILE A 133     4774   4329   6583   -336   -716   -718       C  
ATOM    987  O   ILE A 133      48.569  14.051  79.543  1.00 43.27           O  
ANISOU  987  O   ILE A 133     5036   4605   6800   -357   -819   -639       O  
ATOM    988  CB  ILE A 133      51.473  13.635  78.743  1.00 20.00           C  
ATOM    989  CG1 ILE A 133      52.029  14.875  78.093  1.00 20.00           C  
ATOM    990  CG2 ILE A 133      52.468  12.586  78.581  1.00 20.00           C  
ATOM    991  CD1 ILE A 133      52.868  15.652  78.995  1.00 20.00           C  
ATOM    992  N   ASN A 134      48.671  15.008  77.554  1.00 27.57           N  
ANISOU  992  N   ASN A 134     3089   2714   4673   -323   -703   -827       N  
ATOM    993  CA  ASN A 134      47.589  15.962  77.864  1.00 25.37           C  
ANISOU  993  CA  ASN A 134     2877   2583   4180   -324   -788   -838       C  
ATOM    994  C   ASN A 134      46.221  15.528  77.274  1.00 36.17           C  
ANISOU  994  C   ASN A 134     4261   4076   5407   -365   -738   -961       C  
ATOM    995  O   ASN A 134      45.225  16.246  77.337  1.00 31.82           O  
ANISOU  995  O   ASN A 134     3743   3659   4688   -358   -776   -945       O  
ATOM    996  CB  ASN A 134      47.942  17.374  77.382  1.00 18.50           C  
ANISOU  996  CB  ASN A 134     2021   1783   3225   -273   -801   -806       C  
ATOM    997  CG  ASN A 134      49.157  17.978  78.095  1.00 37.46           C  
ANISOU  997  CG  ASN A 134     4416   4090   5728   -265   -871   -686       C  
ATOM    998  OD1 ASN A 134      49.512  17.591  79.207  1.00 24.62           O  
ANISOU  998  OD1 ASN A 134     2783   2400   4172   -312   -949   -600       O  
ATOM    999  ND2 ASN A 134      49.784  18.961  77.447  1.00 42.48           N  
ANISOU  999  ND2 ASN A 134     5038   4740   6362   -217   -847   -667       N  
ATOM   1000  N   ALA A 135      46.158  14.343  76.717  1.00 29.04           N  
ANISOU 1000  N   ALA A 135     3328   3123   4581   -420   -634  -1073       N  
ATOM   1001  CA  ALA A 135      44.981  13.868  76.041  1.00 33.02           C  
ANISOU 1001  CA  ALA A 135     3837   3769   4939   -505   -577  -1212       C  
ATOM   1002  C   ALA A 135      44.346  12.659  76.650  1.00 38.67           C  
ANISOU 1002  C   ALA A 135     4555   4409   5730   -569   -553  -1264       C  
ATOM   1003  O   ALA A 135      43.931  11.805  75.937  1.00 50.01           O  
ANISOU 1003  O   ALA A 135     5986   5904   7113   -678   -459  -1419       O  
ATOM   1004  CB  ALA A 135      45.292  13.592  74.641  1.00 38.47           C  
ANISOU 1004  CB  ALA A 135     4503   4505   5609   -564   -439  -1356       C  
ATOM   1005  N   MET A 136      44.304  12.564  77.960  1.00 36.65           N  
ANISOU 1005  N   MET A 136     4299   4038   5587   -518   -634  -1136       N  
ATOM   1006  CA  MET A 136      43.723  11.428  78.621  1.00 33.75           C  
ANISOU 1006  CA  MET A 136     3917   3603   5305   -553   -619  -1147       C  
ATOM   1007  C   MET A 136      42.582  11.915  79.455  1.00 43.07           C  
ANISOU 1007  C   MET A 136     5138   4911   6317   -506   -731  -1048       C  
ATOM   1008  O   MET A 136      42.438  13.086  79.651  1.00 57.05           O  
ANISOU 1008  O   MET A 136     6955   6779   7943   -446   -805   -955       O  
ATOM   1009  CB  MET A 136      44.736  10.732  79.482  1.00 27.58           C  
ANISOU 1009  CB  MET A 136     3069   2618   4793   -510   -588  -1024       C  
ATOM   1010  CG  MET A 136      45.816  10.050  78.748  1.00 36.34           C  
ANISOU 1010  CG  MET A 136     4123   3564   6119   -524   -402  -1078       C  
ATOM   1011  SD  MET A 136      46.951   9.366  79.870  1.00 50.22           S  
ANISOU 1011  SD  MET A 136     5751   5114   8217   -454   -357   -832       S  
ATOM   1012  CE  MET A 136      47.866  10.780  80.314  1.00 38.31           C  
ANISOU 1012  CE  MET A 136     4249   3702   6605   -399   -550   -652       C  
ATOM   1013  N   ALA A 137      41.731  11.009  79.889  1.00 39.44           N  
ANISOU 1013  N   ALA A 137     4661   4421   5902   -538   -718  -1067       N  
ATOM   1014  CA  ALA A 137      40.491  11.361  80.589  1.00 41.30           C  
ANISOU 1014  CA  ALA A 137     4938   4763   5993   -501   -802   -978       C  
ATOM   1015  C   ALA A 137      40.173  10.366  81.686  1.00 45.97           C  
ANISOU 1015  C   ALA A 137     5495   5237   6736   -497   -824   -929       C  
ATOM   1016  O   ALA A 137      40.419   9.174  81.522  1.00 52.86           O  
ANISOU 1016  O   ALA A 137     6301   5977   7805   -558   -728  -1016       O  
ATOM   1017  CB  ALA A 137      39.342  11.407  79.607  1.00 34.09           C  
ANISOU 1017  CB  ALA A 137     4026   4032   4895   -575   -765  -1062       C  
ATOM   1018  N   ILE A 138      39.612  10.836  82.796  1.00 43.06           N  
ANISOU 1018  N   ILE A 138     5168   4898   6294   -434   -927   -793       N  
ATOM   1019  CA  ILE A 138      39.124   9.920  83.837  1.00 39.19           C  
ANISOU 1019  CA  ILE A 138     4634   4328   5928   -430   -959   -734       C  
ATOM   1020  C   ILE A 138      37.602  10.055  83.983  1.00 39.27           C  
ANISOU 1020  C   ILE A 138     4692   4443   5786   -416   -989   -710       C  
ATOM   1021  O   ILE A 138      37.106  11.134  84.316  1.00 43.57           O  
ANISOU 1021  O   ILE A 138     5320   5072   6161   -367  -1042   -619       O  
ATOM   1022  CB  ILE A 138      39.834  10.152  85.195  1.00 38.18           C  
ANISOU 1022  CB  ILE A 138     4491   4151   5866   -392  -1057   -573       C  
ATOM   1023  CG1 ILE A 138      41.352   9.960  85.067  1.00 50.41           C  
ANISOU 1023  CG1 ILE A 138     5961   5616   7578   -398  -1019   -534       C  
ATOM   1024  CG2 ILE A 138      39.337   9.176  86.208  1.00 45.26           C  
ANISOU 1024  CG2 ILE A 138     5315   4995   6888   -359  -1067   -474       C  
ATOM   1025  CD1 ILE A 138      42.132  10.122  86.401  1.00 46.82           C  
ANISOU 1025  CD1 ILE A 138     5454   5173   7163   -383  -1118   -332       C  
ATOM   1026  N   LYS A 139      36.865   8.977  83.696  1.00 42.72           N  
ANISOU 1026  N   LYS A 139     5073   4860   6300   -476   -935   -791       N  
ATOM   1027  CA  LYS A 139      35.387   8.983  83.767  1.00 42.16           C  
ANISOU 1027  CA  LYS A 139     5024   4895   6101   -484   -969   -757       C  
ATOM   1028  C   LYS A 139      34.921   9.007  85.216  1.00 40.41           C  
ANISOU 1028  C   LYS A 139     4817   4622   5914   -399  -1061   -600       C  
ATOM   1029  O   LYS A 139      35.448   8.279  86.036  1.00 47.18           O  
ANISOU 1029  O   LYS A 139     5612   5358   6956   -368  -1062   -552       O  
ATOM   1030  CB  LYS A 139      34.769   7.781  83.044  1.00 35.87           C  
ANISOU 1030  CB  LYS A 139     4159   4096   5375   -606   -882   -907       C  
ATOM   1031  CG  LYS A 139      33.310   8.001  82.590  1.00 38.46           C  
ANISOU 1031  CG  LYS A 139     4496   4617   5501   -668   -918   -884       C  
ATOM   1032  CD  LYS A 139      32.534   6.677  82.478  1.00 39.87           C  
ANISOU 1032  CD  LYS A 139     4605   4757   5785   -783   -864   -991       C  
ATOM   1033  CE  LYS A 139      31.201   6.786  81.743  1.00 38.23           C  
ANISOU 1033  CE  LYS A 139     4377   4787   5361   -908   -895   -990       C  
ATOM   1034  NZ  LYS A 139      31.435   6.901  80.270  1.00 58.85           N  
ANISOU 1034  NZ  LYS A 139     6976   7575   7810  -1080   -822  -1156       N  
ATOM   1035  N   LEU A 140      33.948   9.855  85.529  1.00 34.63           N  
ANISOU 1035  N   LEU A 140     4159   3990   5009   -354  -1115   -493       N  
ATOM   1036  CA  LEU A 140      33.543  10.092  86.911  1.00 36.39           C  
ANISOU 1036  CA  LEU A 140     4426   4175   5224   -270  -1183   -344       C  
ATOM   1037  C   LEU A 140      32.155   9.525  87.251  1.00 47.71           C  
ANISOU 1037  C   LEU A 140     5836   5631   6662   -243  -1194   -266       C  
ATOM   1038  O   LEU A 140      31.755   9.488  88.421  1.00 50.56           O  
ANISOU 1038  O   LEU A 140     6223   5949   7040   -161  -1231   -137       O  
ATOM   1039  CB  LEU A 140      33.563  11.593  87.213  1.00 30.96           C  
ANISOU 1039  CB  LEU A 140     3863   3537   4362   -228  -1194   -265       C  
ATOM   1040  CG  LEU A 140      34.900  12.335  87.213  1.00 39.57           C  
ANISOU 1040  CG  LEU A 140     4997   4598   5438   -245  -1192   -306       C  
ATOM   1041  CD1 LEU A 140      34.747  13.697  87.872  1.00 31.84           C  
ANISOU 1041  CD1 LEU A 140     4153   3629   4314   -218  -1179   -232       C  
ATOM   1042  CD2 LEU A 140      35.997  11.529  87.897  1.00 35.81           C  
ANISOU 1042  CD2 LEU A 140     4446   4040   5119   -261  -1237   -304       C  
ATOM   1043  N   ASN A 141      31.406   9.093  86.242  1.00 37.87           N  
ANISOU 1043  N   ASN A 141     4535   4468   5384   -325  -1163   -338       N  
ATOM   1044  CA  ASN A 141      30.095   8.521  86.529  1.00 46.20           C  
ANISOU 1044  CA  ASN A 141     5552   5552   6448   -314  -1179   -254       C  
ATOM   1045  C   ASN A 141      30.242   7.304  87.418  1.00 52.43           C  
ANISOU 1045  C   ASN A 141     6270   6187   7464   -271  -1172   -249       C  
ATOM   1046  O   ASN A 141      31.139   6.496  87.223  1.00 62.87           O  
ANISOU 1046  O   ASN A 141     7522   7403   8962   -314  -1112   -365       O  
ATOM   1047  CB  ASN A 141      29.333   8.187  85.254  1.00 41.04           C  
ANISOU 1047  CB  ASN A 141     4834   5054   5707   -460  -1154   -341       C  
ATOM   1048  CG  ASN A 141      29.250   9.356  84.321  1.00 41.62           C  
ANISOU 1048  CG  ASN A 141     4933   5314   5566   -499  -1152   -307       C  
ATOM   1049  OD1 ASN A 141      28.237  10.034  84.257  1.00 39.27           O  
ANISOU 1049  OD1 ASN A 141     4634   5154   5132   -471  -1167   -129       O  
ATOM   1050  ND2 ASN A 141      30.328   9.617  83.608  1.00 43.52           N  
ANISOU 1050  ND2 ASN A 141     5185   5556   5795   -548  -1113   -443       N  
ATOM   1051  N   PRO A 142      29.370   7.180  88.415  1.00 50.03           N  
ANISOU 1051  N   PRO A 142     5972   5861   7176   -174  -1213    -90       N  
ATOM   1052  CA  PRO A 142      29.597   6.127  89.399  1.00 50.85           C  
ANISOU 1052  CA  PRO A 142     5988   5830   7502   -106  -1205    -39       C  
ATOM   1053  C   PRO A 142      29.929   4.760  88.790  1.00 50.56           C  
ANISOU 1053  C   PRO A 142     5821   5689   7702   -195  -1103   -192       C  
ATOM   1054  O   PRO A 142      30.851   4.072  89.268  1.00 43.06           O  
ANISOU 1054  O   PRO A 142     4780   4612   6968   -157  -1047   -180       O  
ATOM   1055  CB  PRO A 142      28.292   6.127  90.184  1.00 40.77           C  
ANISOU 1055  CB  PRO A 142     4728   4575   6188    -14  -1250    134       C  
ATOM   1056  CG  PRO A 142      27.929   7.585  90.196  1.00 43.38           C  
ANISOU 1056  CG  PRO A 142     5202   5006   6274     19  -1278    224       C  
ATOM   1057  CD  PRO A 142      28.287   8.090  88.827  1.00 47.07           C  
ANISOU 1057  CD  PRO A 142     5681   5569   6634    -98  -1250     86       C  
ATOM   1058  N   LYS A 143      29.215   4.379  87.737  1.00 47.06           N  
ANISOU 1058  N   LYS A 143     5356   5304   7219   -327  -1059   -326       N  
ATOM   1059  CA  LYS A 143      29.424   3.057  87.138  1.00 40.20           C  
ANISOU 1059  CA  LYS A 143     4385   4315   6574   -446   -918   -509       C  
ATOM   1060  C   LYS A 143      30.881   2.805  86.777  1.00 45.92           C  
ANISOU 1060  C   LYS A 143     5083   4918   7447   -475   -805   -629       C  
ATOM   1061  O   LYS A 143      31.400   1.734  87.049  1.00 57.59           O  
ANISOU 1061  O   LYS A 143     6453   6209   9221   -460   -667   -650       O  
ATOM   1062  CB  LYS A 143      28.547   2.870  85.906  1.00 31.49           C  
ANISOU 1062  CB  LYS A 143     3286   3350   5330   -648   -891   -673       C  
ATOM   1063  CG  LYS A 143      28.738   1.544  85.209  1.00 47.28           C  
ANISOU 1063  CG  LYS A 143     5207   5218   7538   -820   -706   -916       C  
ATOM   1064  CD  LYS A 143      28.142   1.531  83.800  1.00 62.36           C  
ANISOU 1064  CD  LYS A 143     7138   7325   9230  -1087   -681  -1126       C  
ATOM   1065  CE  LYS A 143      28.226   2.908  83.145  1.00 68.43           C  
ANISOU 1065  CE  LYS A 143     7984   8345   9672  -1104   -803  -1074       C  
ATOM   1066  NZ  LYS A 143      28.565   2.809  81.695  1.00 73.74           N  
ANISOU 1066  NZ  LYS A 143     8666   9144  10207  -1353   -711  -1334       N  
ATOM   1067  N   ASP A 144      31.532   3.791  86.161  1.00 48.10           N  
ANISOU 1067  N   ASP A 144     5444   5292   7540   -509   -846   -682       N  
ATOM   1068  CA  ASP A 144      32.904   3.644  85.681  1.00 47.86           C  
ANISOU 1068  CA  ASP A 144     5393   5159   7631   -543   -740   -789       C  
ATOM   1069  C   ASP A 144      33.852   4.599  86.390  1.00 53.41           C  
ANISOU 1069  C   ASP A 144     6136   5881   8278   -421   -840   -633       C  
ATOM   1070  O   ASP A 144      34.762   5.124  85.758  1.00 56.52           O  
ANISOU 1070  O   ASP A 144     6566   6290   8618   -458   -820   -706       O  
ATOM   1071  CB  ASP A 144      32.990   3.965  84.185  1.00 53.46           C  
ANISOU 1071  CB  ASP A 144     6161   5980   8170   -713   -688  -1008       C  
ATOM   1072  CG  ASP A 144      32.014   3.166  83.342  1.00 62.44           C  
ANISOU 1072  CG  ASP A 144     7274   7170   9280   -901   -604  -1191       C  
ATOM   1073  OD1 ASP A 144      31.208   3.784  82.602  1.00 61.07           O  
ANISOU 1073  OD1 ASP A 144     7142   7235   8828  -1009   -687  -1222       O  
ATOM   1074  OD2 ASP A 144      32.064   1.924  83.411  1.00 63.13           O  
ANISOU 1074  OD2 ASP A 144     7288   7070   9629   -954   -440  -1291       O  
ATOM   1075  N   PHE A 145      33.654   4.808  87.692  1.00 55.43           N  
ANISOU 1075  N   PHE A 145     6383   6142   8537   -294   -940   -427       N  
ATOM   1076  CA  PHE A 145      34.274   5.921  88.422  1.00 41.50           C  
ANISOU 1076  CA  PHE A 145     4689   4450   6629   -224  -1056   -295       C  
ATOM   1077  C   PHE A 145      35.776   6.129  88.236  1.00 56.46           C  
ANISOU 1077  C   PHE A 145     6554   6304   8594   -242  -1028   -304       C  
ATOM   1078  O   PHE A 145      36.238   7.260  88.098  1.00 76.67           O  
ANISOU 1078  O   PHE A 145     9211   8947  10975   -255  -1096   -310       O  
ATOM   1079  CB  PHE A 145      33.907   5.924  89.906  1.00 34.47           C  
ANISOU 1079  CB  PHE A 145     3781   3575   5740   -118  -1142    -88       C  
ATOM   1080  CG  PHE A 145      34.609   6.999  90.700  1.00 37.90           C  
ANISOU 1080  CG  PHE A 145     4294   4092   6015    -97  -1240     16       C  
ATOM   1081  CD1 PHE A 145      35.670   6.692  91.523  1.00 46.45           C  
ANISOU 1081  CD1 PHE A 145     5268   5170   7211    -82  -1261    149       C  
ATOM   1082  CD2 PHE A 145      34.233   8.323  90.587  1.00 33.56           C  
ANISOU 1082  CD2 PHE A 145     3913   3631   5209   -111  -1291    -12       C  
ATOM   1083  CE1 PHE A 145      36.321   7.685  92.212  1.00 49.44           C  
ANISOU 1083  CE1 PHE A 145     5720   5651   7413   -113  -1354    221       C  
ATOM   1084  CE2 PHE A 145      34.877   9.314  91.288  1.00 32.59           C  
ANISOU 1084  CE2 PHE A 145     3876   3565   4941   -125  -1350     45       C  
ATOM   1085  CZ  PHE A 145      35.918   9.005  92.094  1.00 37.38           C  
ANISOU 1085  CZ  PHE A 145     4390   4188   5625   -143  -1393    144       C  
ATOM   1086  N   GLY A 146      36.568   5.082  88.217  1.00 46.01           N  
ANISOU 1086  N   GLY A 146     5089   4845   7548   -241   -909   -289       N  
ATOM   1087  CA  GLY A 146      37.987   5.370  88.083  1.00 57.60           C  
ANISOU 1087  CA  GLY A 146     6520   6288   9076   -250   -890   -250       C  
ATOM   1088  C   GLY A 146      38.613   5.230  86.702  1.00 54.52           C  
ANISOU 1088  C   GLY A 146     6145   5822   8750   -331   -753   -441       C  
ATOM   1089  O   GLY A 146      39.832   5.081  86.598  1.00 51.49           O  
ANISOU 1089  O   GLY A 146     5685   5361   8519   -324   -684   -382       O  
ATOM   1090  N   LEU A 147      37.804   5.282  85.647  1.00 40.47           N  
ANISOU 1090  N   LEU A 147     4451   4081   6845   -416   -712   -651       N  
ATOM   1091  CA  LEU A 147      38.243   4.787  84.344  1.00 36.27           C  
ANISOU 1091  CA  LEU A 147     3913   3465   6402   -520   -536   -859       C  
ATOM   1092  C   LEU A 147      39.199   5.713  83.626  1.00 45.56           C  
ANISOU 1092  C   LEU A 147     5152   4697   7463   -538   -558   -904       C  
ATOM   1093  O   LEU A 147      38.816   6.819  83.243  1.00 47.47           O  
ANISOU 1093  O   LEU A 147     5495   5108   7433   -554   -677   -939       O  
ATOM   1094  CB  LEU A 147      37.047   4.511  83.443  1.00 40.79           C  
ANISOU 1094  CB  LEU A 147     4541   4116   6841   -649   -494  -1066       C  
ATOM   1095  CG  LEU A 147      37.365   3.713  82.190  1.00 39.62           C  
ANISOU 1095  CG  LEU A 147     4384   3872   6798   -802   -271  -1316       C  
ATOM   1096  CD1 LEU A 147      38.089   2.479  82.614  1.00 52.64           C  
ANISOU 1096  CD1 LEU A 147     5913   5244   8842   -762    -56  -1276       C  
ATOM   1097  CD2 LEU A 147      36.104   3.333  81.475  1.00 31.36           C  
ANISOU 1097  CD2 LEU A 147     3371   2940   5606   -968   -244  -1504       C  
ATOM   1098  N   LEU A 148      40.441   5.251  83.448  1.00 43.93           N  
ANISOU 1098  N   LEU A 148     4868   4338   7486   -524   -424   -877       N  
ATOM   1099  CA  LEU A 148      41.454   6.007  82.722  1.00 46.40           C  
ANISOU 1099  CA  LEU A 148     5223   4675   7732   -535   -423   -912       C  
ATOM   1100  C   LEU A 148      41.291   5.678  81.257  1.00 48.88           C  
ANISOU 1100  C   LEU A 148     5589   4974   8008   -661   -260  -1180       C  
ATOM   1101  O   LEU A 148      41.406   4.518  80.869  1.00 54.06           O  
ANISOU 1101  O   LEU A 148     6194   5456   8890   -725    -35  -1292       O  
ATOM   1102  CB  LEU A 148      42.864   5.651  83.212  1.00 62.67           C  
ANISOU 1102  CB  LEU A 148     7160   6588  10062   -464   -348   -721       C  
ATOM   1103  CG  LEU A 148      44.113   6.504  82.898  1.00 54.11           C  
ANISOU 1103  CG  LEU A 148     6086   5527   8945   -441   -391   -651       C  
ATOM   1104  CD1 LEU A 148      44.758   6.080  81.606  1.00 62.53           C  
ANISOU 1104  CD1 LEU A 148     7159   6462  10139   -491   -171   -813       C  
ATOM   1105  CD2 LEU A 148      43.805   7.982  82.857  1.00 43.46           C  
ANISOU 1105  CD2 LEU A 148     4867   4381   7264   -445   -599   -680       C  
ATOM   1106  N   ILE A 149      40.990   6.707  80.463  1.00 38.93           N  
ANISOU 1106  N   ILE A 149     4424   3908   6460   -708   -357  -1277       N  
ATOM   1107  CA  ILE A 149      40.737   6.568  79.036  1.00 36.68           C  
ANISOU 1107  CA  ILE A 149     4184   3698   6053   -855   -238  -1521       C  
ATOM   1108  C   ILE A 149      41.861   7.191  78.200  1.00 50.59           C  
ANISOU 1108  C   ILE A 149     5968   5463   7791   -845   -193  -1554       C  
ATOM   1109  O   ILE A 149      42.016   8.412  78.103  1.00 56.50           O  
ANISOU 1109  O   ILE A 149     6752   6362   8355   -785   -338  -1472       O  
ATOM   1110  CB  ILE A 149      39.391   7.175  78.658  1.00 43.12           C  
ANISOU 1110  CB  ILE A 149     5045   4795   6544   -912   -357  -1556       C  
ATOM   1111  CG1 ILE A 149      38.318   6.674  79.634  1.00 47.08           C  
ANISOU 1111  CG1 ILE A 149     5525   5285   7079   -887   -423  -1474       C  
ATOM   1112  CG2 ILE A 149      39.063   6.871  77.175  1.00 23.11           C  
ANISOU 1112  CG2 ILE A 149     2528   2396   3856  -1109   -229  -1801       C  
ATOM   1113  CD1 ILE A 149      36.945   7.133  79.313  1.00 41.45           C  
ANISOU 1113  CD1 ILE A 149     4836   4828   6086   -940   -515  -1464       C  
ATOM   1114  N   ASP A 150      42.638   6.322  77.582  1.00 45.31           N  
ANISOU 1114  N   ASP A 150     5276   4608   7332   -901     39  -1674       N  
ATOM   1115  CA  ASP A 150      43.887   6.717  77.007  1.00 47.44           C  
ANISOU 1115  CA  ASP A 150     5546   4810   7668   -858    109  -1656       C  
ATOM   1116  C   ASP A 150      44.055   6.030  75.663  1.00 57.03           C  
ANISOU 1116  C   ASP A 150     6799   5968   8900  -1015    365  -1927       C  
ATOM   1117  O   ASP A 150      44.729   5.010  75.563  1.00 70.59           O  
ANISOU 1117  O   ASP A 150     8485   7419  10917  -1033    624  -1973       O  
ATOM   1118  CB  ASP A 150      45.009   6.322  77.957  1.00 50.62           C  
ANISOU 1118  CB  ASP A 150     5853   4980   8399   -725    159  -1424       C  
ATOM   1119  CG  ASP A 150      46.362   6.588  77.386  1.00 60.18           C  
ANISOU 1119  CG  ASP A 150     7047   6090   9727   -677    258  -1376       C  
ATOM   1120  OD1 ASP A 150      46.496   7.609  76.683  1.00 68.51           O  
ANISOU 1120  OD1 ASP A 150     8165   7307  10558   -681    159  -1430       O  
ATOM   1121  OD2 ASP A 150      47.283   5.780  77.636  1.00 60.98           O  
ANISOU 1121  OD2 ASP A 150     7056   5951  10161   -627    446  -1258       O  
ATOM   1122  N   PHE A 151      43.425   6.597  74.636  1.00 50.85           N  
ANISOU 1122  N   PHE A 151     6077   5448   7797  -1139    312  -2092       N  
ATOM   1123  CA  PHE A 151      43.545   6.105  73.267  1.00 44.51           C  
ANISOU 1123  CA  PHE A 151     5321   4666   6924  -1328    534  -2371       C  
ATOM   1124  C   PHE A 151      44.922   6.343  72.632  1.00 57.10           C  
ANISOU 1124  C   PHE A 151     6925   6132   8640  -1262    669  -2362       C  
ATOM   1125  O   PHE A 151      45.327   5.589  71.742  1.00 64.52           O  
ANISOU 1125  O   PHE A 151     7905   6946   9663  -1395    947  -2579       O  
ATOM   1126  CB  PHE A 151      42.467   6.737  72.370  1.00 42.34           C  
ANISOU 1126  CB  PHE A 151     5071   4785   6231  -1488    409  -2495       C  
ATOM   1127  CG  PHE A 151      41.058   6.510  72.853  1.00 52.77           C  
ANISOU 1127  CG  PHE A 151     6376   6259   7416  -1571    286  -2493       C  
ATOM   1128  CD1 PHE A 151      40.422   5.293  72.645  1.00 57.68           C  
ANISOU 1128  CD1 PHE A 151     7015   6814   8087  -1778    457  -2718       C  
ATOM   1129  CD2 PHE A 151      40.370   7.508  73.515  1.00 45.12           C  
ANISOU 1129  CD2 PHE A 151     5376   5484   6285  -1445     28  -2263       C  
ATOM   1130  CE1 PHE A 151      39.141   5.085  73.095  1.00 51.31           C  
ANISOU 1130  CE1 PHE A 151     6181   6151   7165  -1843    342  -2690       C  
ATOM   1131  CE2 PHE A 151      39.099   7.303  73.953  1.00 35.04           C  
ANISOU 1131  CE2 PHE A 151     4075   4342   4896  -1490    -60  -2217       C  
ATOM   1132  CZ  PHE A 151      38.478   6.096  73.745  1.00 41.63           C  
ANISOU 1132  CZ  PHE A 151     4915   5130   5774  -1687     80  -2422       C  
ATOM   1133  N   PHE A 152      45.652   7.368  73.075  1.00 58.59           N  
ANISOU 1133  N   PHE A 152     7081   6339   8843  -1071    496  -2122       N  
ATOM   1134  CA  PHE A 152      46.830   7.786  72.307  1.00 54.98           C  
ANISOU 1134  CA  PHE A 152     6629   5825   8435  -1017    589  -2112       C  
ATOM   1135  C   PHE A 152      48.209   7.454  72.869  1.00 51.80           C  
ANISOU 1135  C   PHE A 152     6169   5106   8406   -867    703  -1916       C  
ATOM   1136  O   PHE A 152      49.209   7.903  72.339  1.00 51.76           O  
ANISOU 1136  O   PHE A 152     6159   5057   8452   -798    752  -1860       O  
ATOM   1137  CB  PHE A 152      46.707   9.249  71.899  1.00 44.82           C  
ANISOU 1137  CB  PHE A 152     5343   4832   6856   -959    367  -2032       C  
ATOM   1138  CG  PHE A 152      45.362   9.579  71.353  1.00 45.19           C  
ANISOU 1138  CG  PHE A 152     5404   5214   6554  -1099    267  -2153       C  
ATOM   1139  CD1 PHE A 152      44.844   8.853  70.298  1.00 48.76           C  
ANISOU 1139  CD1 PHE A 152     5888   5777   6860  -1328    433  -2424       C  
ATOM   1140  CD2 PHE A 152      44.593  10.571  71.914  1.00 44.48           C  
ANISOU 1140  CD2 PHE A 152     5287   5329   6283  -1022     29  -1988       C  
ATOM   1141  CE1 PHE A 152      43.577   9.131  69.804  1.00 52.24           C  
ANISOU 1141  CE1 PHE A 152     6311   6574   6962  -1482    328  -2497       C  
ATOM   1142  CE2 PHE A 152      43.345  10.857  71.417  1.00 44.85           C  
ANISOU 1142  CE2 PHE A 152     5317   5694   6031  -1144    -48  -2041       C  
ATOM   1143  CZ  PHE A 152      42.830  10.135  70.365  1.00 46.07           C  
ANISOU 1143  CZ  PHE A 152     5480   6001   6025  -1377     85  -2281       C  
ATOM   1144  N   GLY A 153      48.251   6.628  73.906  1.00 54.12           N  
ANISOU 1144  N   GLY A 153     6400   5194   8968   -820    759  -1791       N  
ATOM   1145  CA  GLY A 153      49.502   6.161  74.470  1.00 51.17           C  
ANISOU 1145  CA  GLY A 153     5929   4542   8972   -693    893  -1555       C  
ATOM   1146  C   GLY A 153      50.177   7.229  75.298  1.00 48.43           C  
ANISOU 1146  C   GLY A 153     5516   4283   8603   -541    623  -1252       C  
ATOM   1147  O   GLY A 153      51.395   7.331  75.306  1.00 59.41           O  
ANISOU 1147  O   GLY A 153     6838   5542  10192   -450    687  -1065       O  
ATOM   1148  N   GLY A 154      49.375   8.032  75.984  1.00 38.93           N  
ANISOU 1148  N   GLY A 154     4336   3300   7156   -529    338  -1204       N  
ATOM   1149  CA  GLY A 154      49.870   9.038  76.895  1.00 42.53           C  
ANISOU 1149  CA  GLY A 154     4749   3847   7564   -429     92   -954       C  
ATOM   1150  C   GLY A 154      50.337   8.468  78.222  1.00 52.09           C  
ANISOU 1150  C   GLY A 154     5830   4944   9016   -372     66   -679       C  
ATOM   1151  O   GLY A 154      51.182   9.079  78.898  1.00 52.94           O  
ANISOU 1151  O   GLY A 154     5868   5087   9158   -315    -75   -439       O  
ATOM   1152  N   TYR A 155      49.801   7.304  78.603  1.00 47.16           N  
ANISOU 1152  N   TYR A 155     5158   4204   8558   -398    203   -700       N  
ATOM   1153  CA  TYR A 155      50.222   6.656  79.849  1.00 47.46           C  
ANISOU 1153  CA  TYR A 155     5033   4151   8848   -338    205   -401       C  
ATOM   1154  C   TYR A 155      51.657   6.164  79.730  1.00 54.07           C  
ANISOU 1154  C   TYR A 155     5727   4790  10026   -271    400   -169       C  
ATOM   1155  O   TYR A 155      52.505   6.429  80.586  1.00 46.06           O  
ANISOU 1155  O   TYR A 155     4575   3823   9104   -218    282    157       O  
ATOM   1156  CB  TYR A 155      49.318   5.477  80.222  1.00 48.77           C  
ANISOU 1156  CB  TYR A 155     5161   4216   9152   -367    344   -465       C  
ATOM   1157  CG  TYR A 155      49.668   4.864  81.566  1.00 50.23           C  
ANISOU 1157  CG  TYR A 155     5151   4355   9581   -293    330   -122       C  
ATOM   1158  CD1 TYR A 155      49.283   5.481  82.748  1.00 56.13           C  
ANISOU 1158  CD1 TYR A 155     5876   5315  10136   -281     40     35       C  
ATOM   1159  CD2 TYR A 155      50.393   3.677  81.656  1.00 57.81           C  
ANISOU 1159  CD2 TYR A 155     5933   5065  10966   -241    629     66       C  
ATOM   1160  CE1 TYR A 155      49.603   4.932  83.995  1.00 68.15           C  
ANISOU 1160  CE1 TYR A 155     7197   6848  11847   -230     15    371       C  
ATOM   1161  CE2 TYR A 155      50.725   3.117  82.906  1.00 69.09           C  
ANISOU 1161  CE2 TYR A 155     7136   6491  12623   -169    618    441       C  
ATOM   1162  CZ  TYR A 155      50.320   3.751  84.072  1.00 74.07           C  
ANISOU 1162  CZ  TYR A 155     7742   7383  13019   -170    293    590       C  
ATOM   1163  OH  TYR A 155      50.622   3.228  85.316  1.00 69.63           O  
ANISOU 1163  OH  TYR A 155     6942   6874  12639   -117    265    971       O  
ATOM   1164  N   ARG A 156      51.943   5.442  78.676  1.00 56.64           N  
ANISOU 1164  N   ARG A 156     6080   4901  10540   -291    717   -328       N  
ATOM   1165  CA  ARG A 156      53.285   4.988  78.463  1.00 50.31           C  
ANISOU 1165  CA  ARG A 156     5148   3874  10092   -217    957   -103       C  
ATOM   1166  C   ARG A 156      54.152   6.165  78.230  1.00 46.18           C  
ANISOU 1166  C   ARG A 156     4646   3462   9437   -176    790     -5       C  
ATOM   1167  O   ARG A 156      55.283   6.189  78.620  1.00 49.95           O  
ANISOU 1167  O   ARG A 156     4973   3852  10154   -100    843    316       O  
ATOM   1168  CB  ARG A 156      53.357   4.043  77.293  1.00 58.62           C  
ANISOU 1168  CB  ARG A 156     6246   4635  11393   -265   1393   -327       C  
ATOM   1169  CG  ARG A 156      54.032   4.605  76.109  1.00 79.46           C  
ANISOU 1169  CG  ARG A 156     8935   7131  14125   -249   1604   -386       C  
ATOM   1170  CD  ARG A 156      53.162   4.372  74.936  1.00 98.25           C  
ANISOU 1170  CD  ARG A 156    11524   9713  16093   -347   1471   -755       C  
ATOM   1171  NE  ARG A 156      53.891   4.148  73.716  1.00110.04           N  
ANISOU 1171  NE  ARG A 156    13121  11031  17659   -423   1817  -1019       N  
ATOM   1172  CZ  ARG A 156      53.590   4.733  72.576  1.00110.81           C  
ANISOU 1172  CZ  ARG A 156    13377  11304  17420   -531   1772  -1342       C  
ATOM   1173  NH1 ARG A 156      52.594   5.591  72.525  1.00 94.68           N  
ANISOU 1173  NH1 ARG A 156    11392   9598  14984   -553   1411  -1409       N  
ATOM   1174  NH2 ARG A 156      54.287   4.460  71.491  1.00118.32           N  
ANISOU 1174  NH2 ARG A 156    14420  12103  18435   -623   2110  -1581       N  
ATOM   1175  N   ASP A 157      53.620   7.146  77.544  1.00 43.56           N  
ANISOU 1175  N   ASP A 157     4481   3332   8738   -224    589   -250       N  
ATOM   1176  CA  ASP A 157      54.403   8.339  77.224  1.00 52.70           C  
ANISOU 1176  CA  ASP A 157     5661   4600   9762   -183    426   -173       C  
ATOM   1177  C   ASP A 157      54.796   9.105  78.484  1.00 56.45           C  
ANISOU 1177  C   ASP A 157     6042   5238  10167   -163    132    118       C  
ATOM   1178  O   ASP A 157      55.824   9.788  78.500  1.00 59.49           O  
ANISOU 1178  O   ASP A 157     6370   5652  10580   -128     45    304       O  
ATOM   1179  CB  ASP A 157      53.680   9.246  76.221  1.00 46.08           C  
ANISOU 1179  CB  ASP A 157     4997   3931   8579   -232    336   -489       C  
ATOM   1180  CG  ASP A 157      54.009   8.901  74.795  1.00 53.43           C  
ANISOU 1180  CG  ASP A 157     5992   4740   9569   -249    601   -688       C  
ATOM   1181  OD1 ASP A 157      53.484   9.555  73.867  1.00 49.82           O  
ANISOU 1181  OD1 ASP A 157     5646   4445   8840   -296    555   -920       O  
ATOM   1182  OD2 ASP A 157      54.800   7.960  74.602  1.00 66.49           O  
ANISOU 1182  OD2 ASP A 157     7574   6139  11550   -219    878   -595       O  
ATOM   1183  N   LEU A 158      53.984   8.982  79.532  1.00 42.63           N  
ANISOU 1183  N   LEU A 158     4276   3601   8319   -201    -15    153       N  
ATOM   1184  CA  LEU A 158      54.366   9.488  80.850  1.00 44.77           C  
ANISOU 1184  CA  LEU A 158     4444   4031   8537   -219   -257    436       C  
ATOM   1185  C   LEU A 158      55.458   8.633  81.463  1.00 58.91           C  
ANISOU 1185  C   LEU A 158     5993   5717  10673   -177   -144    825       C  
ATOM   1186  O   LEU A 158      56.368   9.148  82.115  1.00 75.60           O  
ANISOU 1186  O   LEU A 158     7987   7950  12788   -199   -299   1110       O  
ATOM   1187  CB  LEU A 158      53.181   9.523  81.807  1.00 44.02           C  
ANISOU 1187  CB  LEU A 158     4397   4083   8247   -270   -417    373       C  
ATOM   1188  CG  LEU A 158      52.320  10.780  81.856  1.00 47.09           C  
ANISOU 1188  CG  LEU A 158     4968   4662   8263   -321   -632    166       C  
ATOM   1189  CD1 LEU A 158      51.270  10.618  82.922  1.00 48.94           C  
ANISOU 1189  CD1 LEU A 158     5222   5003   8369   -359   -749    166       C  
ATOM   1190  CD2 LEU A 158      53.174  12.004  82.139  1.00 39.54           C  
ANISOU 1190  CD2 LEU A 158     4015   3825   7182   -355   -809    283       C  
ATOM   1191  N   LYS A 159      55.374   7.322  81.270  1.00 57.94           N  
ANISOU 1191  N   LYS A 159     5782   5378  10853   -130    143    856       N  
ATOM   1192  CA  LYS A 159      56.375   6.447  81.861  1.00 59.37           C  
ANISOU 1192  CA  LYS A 159     5697   5449  11411    -72    297   1280       C  
ATOM   1193  C   LYS A 159      57.725   6.632  81.193  1.00 61.28           C  
ANISOU 1193  C   LYS A 159     5864   5574  11847    -17    419   1463       C  
ATOM   1194  O   LYS A 159      58.766   6.549  81.849  1.00 69.07           O  
ANISOU 1194  O   LYS A 159     6620   6607  13016      5    388   1895       O  
ATOM   1195  CB  LYS A 159      55.941   4.991  81.811  1.00 57.10           C  
ANISOU 1195  CB  LYS A 159     5327   4920  11447    -27    629   1273       C  
ATOM   1196  CG  LYS A 159      54.798   4.683  82.767  1.00 80.49           C  
ANISOU 1196  CG  LYS A 159     8283   8009  14291    -63    500   1231       C  
ATOM   1197  CD  LYS A 159      55.222   4.798  84.219  1.00 92.12           C  
ANISOU 1197  CD  LYS A 159     9530   9708  15764    -69    282   1661       C  
ATOM   1198  CE  LYS A 159      54.036   5.098  85.116  1.00100.01           C  
ANISOU 1198  CE  LYS A 159    10611  10925  16464   -130     31   1540       C  
ATOM   1199  NZ  LYS A 159      54.404   4.820  86.524  1.00111.46           N  
ANISOU 1199  NZ  LYS A 159    11798  12567  17984   -139    -92   1977       N  
ATOM   1200  N   GLU A 160      57.698   6.898  79.891  1.00 48.50           N  
ANISOU 1200  N   GLU A 160     4426   3828  10174     -2    550   1154       N  
ATOM   1201  CA  GLU A 160      58.919   7.032  79.119  1.00 50.42           C  
ANISOU 1201  CA  GLU A 160     4619   3928  10610     65    701   1295       C  
ATOM   1202  C   GLU A 160      59.333   8.466  78.931  1.00 48.88           C  
ANISOU 1202  C   GLU A 160     4508   3932  10134     42    412   1265       C  
ATOM   1203  O   GLU A 160      60.235   8.734  78.156  1.00 52.67           O  
ANISOU 1203  O   GLU A 160     4981   4308  10723    100    513   1326       O  
ATOM   1204  CB  GLU A 160      58.762   6.396  77.746  1.00 59.70           C  
ANISOU 1204  CB  GLU A 160     5931   4832  11919     90   1065    987       C  
ATOM   1205  CG  GLU A 160      58.431   4.932  77.777  1.00 72.75           C  
ANISOU 1205  CG  GLU A 160     7517   6226  13900    101   1431    979       C  
ATOM   1206  CD  GLU A 160      58.002   4.456  76.424  1.00 88.68           C  
ANISOU 1206  CD  GLU A 160     9730   8039  15925     53   1748    556       C  
ATOM   1207  OE1 GLU A 160      57.697   3.248  76.282  1.00 97.49           O  
ANISOU 1207  OE1 GLU A 160    10827   8905  17310     33   2104    474       O  
ATOM   1208  OE2 GLU A 160      57.970   5.310  75.506  1.00 91.24           O  
ANISOU 1208  OE2 GLU A 160    10221   8465  15980     23   1649    307       O  
ATOM   1209  N   GLY A 161      58.664   9.387  79.616  1.00 51.02           N  
ANISOU 1209  N   GLY A 161     4860   4466  10058    -41     83   1167       N  
ATOM   1210  CA  GLY A 161      58.969  10.805  79.504  1.00 40.53           C  
ANISOU 1210  CA  GLY A 161     3617   3314   8469    -77   -168   1118       C  
ATOM   1211  C   GLY A 161      59.023  11.348  78.087  1.00 45.68           C  
ANISOU 1211  C   GLY A 161     4423   3885   9048    -23    -69    851       C  
ATOM   1212  O   GLY A 161      59.998  11.979  77.697  1.00 51.86           O  
ANISOU 1212  O   GLY A 161     5170   4659   9877     15    -98    975       O  
ATOM   1213  N   VAL A 162      57.956  11.135  77.323  1.00 50.35           N  
ANISOU 1213  N   VAL A 162     5174   4448   9508    -31     37    495       N  
ATOM   1214  CA  VAL A 162      57.928  11.559  75.931  1.00 47.72           C  
ANISOU 1214  CA  VAL A 162     4968   4081   9083      3    146    245       C  
ATOM   1215  C   VAL A 162      56.857  12.601  75.632  1.00 42.42           C  
ANISOU 1215  C   VAL A 162     4450   3627   8040    -41    -34    -29       C  
ATOM   1216  O   VAL A 162      55.704  12.462  76.052  1.00 49.07           O  
ANISOU 1216  O   VAL A 162     5357   4567   8721   -102   -105   -172       O  
ATOM   1217  CB  VAL A 162      57.775  10.335  75.006  1.00 50.16           C  
ANISOU 1217  CB  VAL A 162     5310   4169   9579     11    499     79       C  
ATOM   1218  CG1 VAL A 162      57.113  10.699  73.689  1.00 34.32           C  
ANISOU 1218  CG1 VAL A 162     3467   2237   7335    -24    569   -284       C  
ATOM   1219  CG2 VAL A 162      59.134   9.719  74.768  1.00 61.52           C  
ANISOU 1219  CG2 VAL A 162     6617   5363  11393     97    738    345       C  
ATOM   1220  N   ILE A 163      57.247  13.660  74.926  1.00 40.10           N  
ANISOU 1220  N   ILE A 163     4198   3406   7634      1    -97    -70       N  
ATOM   1221  CA  ILE A 163      56.286  14.659  74.442  1.00 47.50           C  
ANISOU 1221  CA  ILE A 163     5250   4538   8259    -18   -207   -294       C  
ATOM   1222  C   ILE A 163      55.936  14.336  72.983  1.00 50.00           C  
ANISOU 1222  C   ILE A 163     5631   4852   8513    -13     -7   -533       C  
ATOM   1223  O   ILE A 163      56.818  14.328  72.122  1.00 52.03           O  
ANISOU 1223  O   ILE A 163     5866   5014   8889     48    128   -506       O  
ATOM   1224  CB  ILE A 163      56.852  16.091  74.503  1.00 41.08           C  
ANISOU 1224  CB  ILE A 163     4428   3822   7358     21   -372   -196       C  
ATOM   1225  CG1 ILE A 163      56.469  16.848  75.786  1.00 36.58           C  
ANISOU 1225  CG1 ILE A 163     3876   3374   6650    -49   -595   -125       C  
ATOM   1226  CG2 ILE A 163      56.291  16.889  73.356  1.00 45.23           C  
ANISOU 1226  CG2 ILE A 163     5023   4477   7686     58   -340   -387       C  
ATOM   1227  CD1 ILE A 163      56.121  16.020  76.981  1.00 40.16           C  
ANISOU 1227  CD1 ILE A 163     4298   3816   7144   -123   -650    -42       C  
ATOM   1228  N   ARG A 164      54.657  14.073  72.708  1.00 44.22           N  
ANISOU 1228  N   ARG A 164     4975   4241   7584    -91     12   -757       N  
ATOM   1229  CA  ARG A 164      54.247  13.557  71.400  1.00 43.18           C  
ANISOU 1229  CA  ARG A 164     4898   4141   7366   -148    211   -998       C  
ATOM   1230  C   ARG A 164      52.901  14.101  70.917  1.00 48.91           C  
ANISOU 1230  C   ARG A 164     5679   5150   7756   -222    124  -1181       C  
ATOM   1231  O   ARG A 164      51.899  14.013  71.634  1.00 54.07           O  
ANISOU 1231  O   ARG A 164     6354   5888   8302   -276     18  -1207       O  
ATOM   1232  CB  ARG A 164      54.140  12.029  71.467  1.00 40.41           C  
ANISOU 1232  CB  ARG A 164     4558   3592   7205   -225    435  -1088       C  
ATOM   1233  CG  ARG A 164      54.100  11.343  70.112  1.00 38.48           C  
ANISOU 1233  CG  ARG A 164     4375   3307   6938   -312    711  -1338       C  
ATOM   1234  CD  ARG A 164      53.519   9.941  70.208  1.00 41.49           C  
ANISOU 1234  CD  ARG A 164     4793   3544   7427   -440    926  -1507       C  
ATOM   1235  NE  ARG A 164      54.202   9.088  71.184  1.00 47.39           N  
ANISOU 1235  NE  ARG A 164     5458   4000   8547   -371   1033  -1292       N  
ATOM   1236  CZ  ARG A 164      55.188   8.245  70.874  1.00 52.91           C  
ANISOU 1236  CZ  ARG A 164     6125   4403   9577   -337   1341  -1228       C  
ATOM   1237  NH1 ARG A 164      55.755   7.500  71.817  1.00 57.57           N  
ANISOU 1237  NH1 ARG A 164     6599   4760  10515   -266   1437   -972       N  
ATOM   1238  NH2 ARG A 164      55.606   8.148  69.616  1.00 37.83           N  
ANISOU 1238  NH2 ARG A 164     4285   2436   7652   -373   1569  -1400       N  
ATOM   1239  N   VAL A 165      52.868  14.614  69.689  1.00 33.06           N  
ANISOU 1239  N   VAL A 165     3675   3299   5586   -224    182  -1283       N  
ATOM   1240  CA  VAL A 165      51.629  15.113  69.114  1.00 32.42           C  
ANISOU 1240  CA  VAL A 165     3603   3529   5186   -300    119  -1404       C  
ATOM   1241  C   VAL A 165      50.678  13.956  68.719  1.00 40.82           C  
ANISOU 1241  C   VAL A 165     4717   4653   6140   -485    245  -1640       C  
ATOM   1242  O   VAL A 165      51.125  12.844  68.445  1.00 32.15           O  
ANISOU 1242  O   VAL A 165     3658   3357   5201   -555    450  -1763       O  
ATOM   1243  CB  VAL A 165      51.889  16.030  67.897  1.00 34.24           C  
ANISOU 1243  CB  VAL A 165     3785   3957   5269   -252    145  -1403       C  
ATOM   1244  CG1 VAL A 165      52.438  17.364  68.313  1.00 25.35           C  
ANISOU 1244  CG1 VAL A 165     2604   2831   4198    -91      3  -1186       C  
ATOM   1245  CG2 VAL A 165      52.788  15.370  66.925  1.00 23.74           C  
ANISOU 1245  CG2 VAL A 165     2472   2504   4043   -272    359  -1505       C  
ATOM   1246  N   LEU A 166      49.384  14.205  68.746  1.00 42.22           N  
ANISOU 1246  N   LEU A 166     4888   5096   6057   -574    145  -1697       N  
ATOM   1247  CA  LEU A 166      48.387  13.195  68.437  1.00 37.35           C  
ANISOU 1247  CA  LEU A 166     4315   4535   5342   -770    242  -1911       C  
ATOM   1248  C   LEU A 166      48.348  12.753  66.999  1.00 44.82           C  
ANISOU 1248  C   LEU A 166     5272   5663   6095   -941    413  -2136       C  
ATOM   1249  O   LEU A 166      47.931  11.669  66.673  1.00 45.71           O  
ANISOU 1249  O   LEU A 166     5441   5757   6171  -1141    569  -2369       O  
ATOM   1250  CB  LEU A 166      47.016  13.649  68.892  1.00 32.05           C  
ANISOU 1250  CB  LEU A 166     3625   4077   4475   -814     72  -1864       C  
ATOM   1251  CG  LEU A 166      47.087  14.088  70.325  1.00 38.95           C  
ANISOU 1251  CG  LEU A 166     4497   4824   5478   -658    -98  -1647       C  
ATOM   1252  CD1 LEU A 166      45.776  14.116  70.905  1.00 45.19           C  
ANISOU 1252  CD1 LEU A 166     5292   5755   6125   -722   -203  -1636       C  
ATOM   1253  CD2 LEU A 166      47.873  13.118  71.006  1.00 41.94           C  
ANISOU 1253  CD2 LEU A 166     4902   4856   6178   -597    -40  -1602       C  
ATOM   1254  N   HIS A 167      48.720  13.659  66.139  1.00 44.62           N  
ANISOU 1254  N   HIS A 167     5189   5824   5942   -876    393  -2069       N  
ATOM   1255  CA  HIS A 167      48.659  13.477  64.693  1.00 45.78           C  
ANISOU 1255  CA  HIS A 167     5328   6207   5859  -1038    538  -2255       C  
ATOM   1256  C   HIS A 167      49.616  14.412  63.967  1.00 44.85           C  
ANISOU 1256  C   HIS A 167     5149   6143   5750   -887    550  -2132       C  
ATOM   1257  O   HIS A 167      49.957  15.491  64.452  1.00 45.23           O  
ANISOU 1257  O   HIS A 167     5131   6173   5883   -679    400  -1889       O  
ATOM   1258  CB  HIS A 167      47.230  13.672  64.159  1.00 40.72           C  
ANISOU 1258  CB  HIS A 167     4620   6020   4832  -1229    447  -2312       C  
ATOM   1259  CG  HIS A 167      46.775  15.094  64.155  1.00 42.57           C  
ANISOU 1259  CG  HIS A 167     4716   6550   4908  -1088    253  -2040       C  
ATOM   1260  ND1 HIS A 167      46.186  15.694  65.250  1.00 40.22           N  
ANISOU 1260  ND1 HIS A 167     4390   6225   4668   -961     81  -1837       N  
ATOM   1261  CD2 HIS A 167      46.845  16.049  63.197  1.00 43.88           C  
ANISOU 1261  CD2 HIS A 167     4757   7030   4887  -1047    235  -1924       C  
ATOM   1262  CE1 HIS A 167      45.915  16.956  64.969  1.00 44.13           C  
ANISOU 1262  CE1 HIS A 167     4755   6975   5039   -848     -9  -1612       C  
ATOM   1263  NE2 HIS A 167      46.307  17.196  63.732  1.00 53.84           N  
ANISOU 1263  NE2 HIS A 167     5911   8421   6125   -889     75  -1645       N  
ATOM   1264  N   THR A 168      50.022  13.961  62.793  1.00 49.47           N  
ANISOU 1264  N   THR A 168     5763   6790   6244  -1011    748  -2319       N  
ATOM   1265  CA  THR A 168      50.853  14.686  61.838  1.00 53.85           C  
ANISOU 1265  CA  THR A 168     6258   7442   6759   -909    801  -2247       C  
ATOM   1266  C   THR A 168      50.584  16.168  61.598  1.00 56.43           C  
ANISOU 1266  C   THR A 168     6425   8093   6921   -762    610  -1994       C  
ATOM   1267  O   THR A 168      51.516  16.944  61.373  1.00 58.78           O  
ANISOU 1267  O   THR A 168     6669   8318   7348   -567    606  -1835       O  
ATOM   1268  CB  THR A 168      50.748  13.982  60.490  1.00 55.71           C  
ANISOU 1268  CB  THR A 168     6538   7872   6756  -1163   1022  -2533       C  
ATOM   1269  OG1 THR A 168      51.820  13.052  60.385  1.00 43.74           O  
ANISOU 1269  OG1 THR A 168     5150   5947   5523  -1163   1288  -2678       O  
ATOM   1270  CG2 THR A 168      50.801  14.977  59.333  1.00 61.32           C  
ANISOU 1270  CG2 THR A 168     7117   8986   7197  -1138    984  -2441       C  
ATOM   1271  N   LEU A 169      49.323  16.567  61.624  1.00 56.79           N  
ANISOU 1271  N   LEU A 169     6382   8491   6704   -850    473  -1936       N  
ATOM   1272  CA  LEU A 169      48.990  17.951  61.300  1.00 53.01           C  
ANISOU 1272  CA  LEU A 169     5724   8335   6083   -717    347  -1671       C  
ATOM   1273  C   LEU A 169      48.846  18.852  62.509  1.00 53.81           C  
ANISOU 1273  C   LEU A 169     5794   8283   6368   -506    189  -1423       C  
ATOM   1274  O   LEU A 169      48.435  19.994  62.369  1.00 54.90           O  
ANISOU 1274  O   LEU A 169     5784   8653   6422   -397    118  -1192       O  
ATOM   1275  CB  LEU A 169      47.734  18.003  60.461  1.00 50.12           C  
ANISOU 1275  CB  LEU A 169     5233   8499   5313   -931    320  -1686       C  
ATOM   1276  CG  LEU A 169      48.006  17.569  59.019  1.00 52.98           C  
ANISOU 1276  CG  LEU A 169     5575   9124   5430  -1124    474  -1876       C  
ATOM   1277  CD1 LEU A 169      46.727  17.124  58.323  1.00 35.28           C  
ANISOU 1277  CD1 LEU A 169     3258   7380   2768  -1453    461  -1989       C  
ATOM   1278  CD2 LEU A 169      48.678  18.706  58.289  1.00 39.97           C  
ANISOU 1278  CD2 LEU A 169     3773   7633   3781   -926    478  -1654       C  
ATOM   1279  N   SER A 170      49.207  18.330  63.683  1.00 42.58           N  
ANISOU 1279  N   SER A 170     4504   6472   5202   -459    159  -1463       N  
ATOM   1280  CA  SER A 170      49.115  19.051  64.944  1.00 35.49           C  
ANISOU 1280  CA  SER A 170     3611   5405   4468   -303     23  -1274       C  
ATOM   1281  C   SER A 170      49.683  20.490  64.919  1.00 36.95           C  
ANISOU 1281  C   SER A 170     3696   5596   4748    -90    -17  -1037       C  
ATOM   1282  O   SER A 170      48.956  21.421  65.237  1.00 41.57           O  
ANISOU 1282  O   SER A 170     4200   6323   5272    -24    -79   -867       O  
ATOM   1283  CB  SER A 170      49.740  18.223  66.077  1.00 48.03           C  
ANISOU 1283  CB  SER A 170     5336   6586   6326   -289     15  -1341       C  
ATOM   1284  OG  SER A 170      49.197  18.534  67.360  1.00 40.66           O  
ANISOU 1284  OG  SER A 170     4432   5565   5452   -244   -117  -1234       O  
ATOM   1285  N   PHE A 171      50.956  20.675  64.555  1.00 34.15           N  
ANISOU 1285  N   PHE A 171     3341   5072   4561     19     43  -1017       N  
ATOM   1286  CA  PHE A 171      51.579  22.010  64.558  1.00 35.28           C  
ANISOU 1286  CA  PHE A 171     3392   5186   4828    216     18   -804       C  
ATOM   1287  C   PHE A 171      51.050  22.910  63.445  1.00 49.76           C  
ANISOU 1287  C   PHE A 171     5042   7401   6463    260     63   -674       C  
ATOM   1288  O   PHE A 171      50.972  24.122  63.599  1.00 50.09           O  
ANISOU 1288  O   PHE A 171     4979   7487   6567    403     52   -467       O  
ATOM   1289  CB  PHE A 171      53.112  21.942  64.448  1.00 27.65           C  
ANISOU 1289  CB  PHE A 171     2460   3941   4105    321     66   -792       C  
ATOM   1290  CG  PHE A 171      53.764  21.200  65.560  1.00 28.70           C  
ANISOU 1290  CG  PHE A 171     2719   3721   4463    301     25   -833       C  
ATOM   1291  CD1 PHE A 171      53.745  21.699  66.843  1.00 40.26           C  
ANISOU 1291  CD1 PHE A 171     4217   5038   6042    339    -97   -729       C  
ATOM   1292  CD2 PHE A 171      54.396  20.008  65.328  1.00 29.58           C  
ANISOU 1292  CD2 PHE A 171     2905   3657   4677    236    132   -959       C  
ATOM   1293  CE1 PHE A 171      54.340  21.005  67.877  1.00 41.04           C  
ANISOU 1293  CE1 PHE A 171     4400   4867   6327    305   -145   -730       C  
ATOM   1294  CE2 PHE A 171      54.994  19.318  66.354  1.00 34.92           C  
ANISOU 1294  CE2 PHE A 171     3656   4031   5582    227    110   -937       C  
ATOM   1295  CZ  PHE A 171      54.966  19.817  67.625  1.00 37.37           C  
ANISOU 1295  CZ  PHE A 171     3976   4245   5979    260    -44   -811       C  
ATOM   1296  N   VAL A 172      50.711  22.316  62.312  1.00 54.99           N  
ANISOU 1296  N   VAL A 172     5658   8346   6891    124    136   -789       N  
ATOM   1297  CA  VAL A 172      50.069  23.054  61.235  1.00 47.16           C  
ANISOU 1297  CA  VAL A 172     4458   7801   5658    126    169   -641       C  
ATOM   1298  C   VAL A 172      48.708  23.640  61.666  1.00 45.02           C  
ANISOU 1298  C   VAL A 172     4080   7765   5261    111    105   -463       C  
ATOM   1299  O   VAL A 172      48.370  24.757  61.269  1.00 47.71           O  
ANISOU 1299  O   VAL A 172     4221   8340   5568    232    136   -201       O  
ATOM   1300  CB  VAL A 172      49.938  22.159  59.975  1.00 35.88           C  
ANISOU 1300  CB  VAL A 172     3017   6664   3953    -83    257   -836       C  
ATOM   1301  CG1 VAL A 172      48.774  22.574  59.123  1.00 38.93           C  
ANISOU 1301  CG1 VAL A 172     3191   7606   3995   -192    246   -701       C  
ATOM   1302  CG2 VAL A 172      51.177  22.234  59.188  1.00 29.39           C  
ANISOU 1302  CG2 VAL A 172     2191   5747   3228     11    359   -864       C  
ATOM   1303  N   ASP A 173      47.940  22.897  62.474  1.00 34.37           N  
ANISOU 1303  N   ASP A 173     2850   6342   3866    -23     39   -580       N  
ATOM   1304  CA  ASP A 173      46.636  23.374  62.952  1.00 44.71           C  
ANISOU 1304  CA  ASP A 173     4072   7841   5075    -35    -10   -404       C  
ATOM   1305  C   ASP A 173      46.807  24.507  63.944  1.00 53.17           C  
ANISOU 1305  C   ASP A 173     5144   8659   6399    177    -11   -204       C  
ATOM   1306  O   ASP A 173      45.989  25.410  64.022  1.00 63.76           O  
ANISOU 1306  O   ASP A 173     6344  10170   7713    251     26     42       O  
ATOM   1307  CB  ASP A 173      45.861  22.275  63.687  1.00 55.40           C  
ANISOU 1307  CB  ASP A 173     5571   9122   6357   -214    -80   -583       C  
ATOM   1308  CG  ASP A 173      45.378  21.158  62.782  1.00 55.31           C  
ANISOU 1308  CG  ASP A 173     5556   9394   6064   -478    -60   -791       C  
ATOM   1309  OD1 ASP A 173      45.103  20.064  63.343  1.00 49.15           O  
ANISOU 1309  OD1 ASP A 173     4929   8454   5292   -623    -85  -1004       O  
ATOM   1310  OD2 ASP A 173      45.253  21.370  61.552  1.00 52.85           O  
ANISOU 1310  OD2 ASP A 173     5087   9470   5523   -553    -10   -742       O  
ATOM   1311  N   ASP A 174      47.804  24.365  64.800  1.00 49.97           N  
ANISOU 1311  N   ASP A 174     4899   7844   6244    254    -36   -306       N  
ATOM   1312  CA  ASP A 174      48.112  25.328  65.828  1.00 40.33           C  
ANISOU 1312  CA  ASP A 174     3729   6349   5247    390    -42   -188       C  
ATOM   1313  C   ASP A 174      49.605  25.394  66.031  1.00 39.48           C  
ANISOU 1313  C   ASP A 174     3710   5914   5375    475    -53   -253       C  
ATOM   1314  O   ASP A 174      50.150  24.587  66.717  1.00 44.23           O  
ANISOU 1314  O   ASP A 174     4469   6258   6080    412   -126   -398       O  
ATOM   1315  CB  ASP A 174      47.465  24.861  67.104  1.00 36.88           C  
ANISOU 1315  CB  ASP A 174     3435   5775   4804    298   -119   -264       C  
ATOM   1316  CG  ASP A 174      47.456  25.884  68.155  1.00 55.45           C  
ANISOU 1316  CG  ASP A 174     5853   7876   7338    394   -105   -162       C  
ATOM   1317  OD1 ASP A 174      48.034  26.929  67.966  1.00 59.38           O  
ANISOU 1317  OD1 ASP A 174     6462   8275   7823    328   -157   -203       O  
ATOM   1318  OD2 ASP A 174      46.887  25.653  69.203  1.00 42.81           O  
ANISOU 1318  OD2 ASP A 174     4199   6177   5890    522    -32    -52       O  
ATOM   1319  N   PRO A 175      50.275  26.371  65.458  1.00 35.97           N  
ANISOU 1319  N   PRO A 175     3144   5497   5027    618     23   -118       N  
ATOM   1320  CA  PRO A 175      51.731  26.469  65.616  1.00 36.42           C  
ANISOU 1320  CA  PRO A 175     3263   5270   5305    695      9   -154       C  
ATOM   1321  C   PRO A 175      52.079  26.888  67.026  1.00 39.84           C  
ANISOU 1321  C   PRO A 175     3820   5392   5926    702    -48   -148       C  
ATOM   1322  O   PRO A 175      53.231  26.892  67.444  1.00 61.32           O  
ANISOU 1322  O   PRO A 175     6605   7870   8825    724    -90   -169       O  
ATOM   1323  CB  PRO A 175      52.132  27.560  64.616  1.00 32.69           C  
ANISOU 1323  CB  PRO A 175     2603   4936   4883    856    116     28       C  
ATOM   1324  CG  PRO A 175      51.027  27.609  63.645  1.00 42.11           C  
ANISOU 1324  CG  PRO A 175     3629   6543   5828    826    175    118       C  
ATOM   1325  CD  PRO A 175      49.773  27.302  64.438  1.00 37.71           C  
ANISOU 1325  CD  PRO A 175     3135   6039   5153    713    129     96       C  
ATOM   1326  N   THR A 176      51.049  27.206  67.775  1.00 31.59           N  
ANISOU 1326  N   THR A 176     2807   4373   4824    665    -45   -114       N  
ATOM   1327  CA  THR A 176      51.190  27.627  69.152  1.00 33.33           C  
ANISOU 1327  CA  THR A 176     3155   4338   5172    634    -82   -127       C  
ATOM   1328  C   THR A 176      51.675  26.462  70.029  1.00 38.67           C  
ANISOU 1328  C   THR A 176     3988   4833   5873    509   -224   -280       C  
ATOM   1329  O   THR A 176      52.283  26.664  71.087  1.00 31.98           O  
ANISOU 1329  O   THR A 176     3235   3774   5141    464   -285   -295       O  
ATOM   1330  CB  THR A 176      49.845  28.177  69.610  1.00 31.66           C  
ANISOU 1330  CB  THR A 176     2933   4218   4878    628     -7    -45       C  
ATOM   1331  OG1 THR A 176      50.028  29.520  70.044  1.00 35.89           O  
ANISOU 1331  OG1 THR A 176     3452   4611   5572    706    118     63       O  
ATOM   1332  CG2 THR A 176      49.169  27.284  70.674  1.00 26.91           C  
ANISOU 1332  CG2 THR A 176     2485   3551   4189    492   -112   -165       C  
ATOM   1333  N   ARG A 177      51.413  25.246  69.557  1.00 34.11           N  
ANISOU 1333  N   ARG A 177     3421   4355   5185    440   -259   -383       N  
ATOM   1334  CA  ARG A 177      51.909  24.030  70.175  1.00 38.20           C  
ANISOU 1334  CA  ARG A 177     4046   4708   5761    344   -346   -498       C  
ATOM   1335  C   ARG A 177      53.410  23.821  69.988  1.00 40.81           C  
ANISOU 1335  C   ARG A 177     4369   4861   6275    385   -354   -478       C  
ATOM   1336  O   ARG A 177      54.021  23.039  70.716  1.00 38.70           O  
ANISOU 1336  O   ARG A 177     4165   4422   6119    324   -417   -498       O  
ATOM   1337  CB  ARG A 177      51.163  22.822  69.615  1.00 42.64           C  
ANISOU 1337  CB  ARG A 177     4615   5411   6174    252   -327   -624       C  
ATOM   1338  CG  ARG A 177      49.693  23.062  69.476  1.00 38.43           C  
ANISOU 1338  CG  ARG A 177     4044   5116   5441    217   -311   -604       C  
ATOM   1339  CD  ARG A 177      48.939  21.815  69.138  1.00 37.78           C  
ANISOU 1339  CD  ARG A 177     3985   5158   5210     82   -311   -747       C  
ATOM   1340  NE  ARG A 177      47.510  22.107  69.099  1.00 45.95           N  
ANISOU 1340  NE  ARG A 177     4967   6434   6057     44   -313   -684       N  
ATOM   1341  CZ  ARG A 177      46.643  21.527  68.278  1.00 45.19           C  
ANISOU 1341  CZ  ARG A 177     4810   6611   5751    -69   -288   -743       C  
ATOM   1342  NH1 ARG A 177      45.379  21.875  68.322  1.00 38.17           N  
ANISOU 1342  NH1 ARG A 177     3851   5944   4709    -96   -296   -630       N  
ATOM   1343  NH2 ARG A 177      47.037  20.616  67.404  1.00 54.65           N  
ANISOU 1343  NH2 ARG A 177     6012   7863   6889   -170   -239   -908       N  
ATOM   1344  N   ILE A 178      54.008  24.494  69.011  1.00 42.52           N  
ANISOU 1344  N   ILE A 178     4489   5129   6537    495   -282   -407       N  
ATOM   1345  CA  ILE A 178      55.462  24.490  68.902  1.00 50.84           C  
ANISOU 1345  CA  ILE A 178     5526   6001   7788    552   -288   -347       C  
ATOM   1346  C   ILE A 178      56.013  24.983  70.241  1.00 52.82           C  
ANISOU 1346  C   ILE A 178     5834   6069   8167    507   -393   -277       C  
ATOM   1347  O   ILE A 178      56.889  24.353  70.852  1.00 39.64           O  
ANISOU 1347  O   ILE A 178     4194   4242   6626    454   -462   -242       O  
ATOM   1348  CB  ILE A 178      55.950  25.365  67.719  1.00 34.89           C  
ANISOU 1348  CB  ILE A 178     3384   4072   5801    695   -195   -257       C  
ATOM   1349  CG1 ILE A 178      55.575  24.706  66.397  1.00 35.77           C  
ANISOU 1349  CG1 ILE A 178     3443   4387   5762    696    -98   -338       C  
ATOM   1350  CG2 ILE A 178      57.471  25.581  67.758  1.00 32.15           C  
ANISOU 1350  CG2 ILE A 178     3016   3518   5682    762   -212   -157       C  
ATOM   1351  CD1 ILE A 178      55.887  25.558  65.205  1.00 38.99           C  
ANISOU 1351  CD1 ILE A 178     3708   4945   6160    833     -6   -236       C  
ATOM   1352  N   LEU A 179      55.460  26.101  70.705  1.00 47.11           N  
ANISOU 1352  N   LEU A 179     5116   5379   7403    511   -385   -246       N  
ATOM   1353  CA  LEU A 179      55.861  26.662  71.974  1.00 39.62           C  
ANISOU 1353  CA  LEU A 179     4238   4287   6529    423   -462   -218       C  
ATOM   1354  C   LEU A 179      55.478  25.749  73.118  1.00 43.71           C  
ANISOU 1354  C   LEU A 179     4857   4767   6982    280   -570   -280       C  
ATOM   1355  O   LEU A 179      56.294  25.480  74.003  1.00 39.55           O  
ANISOU 1355  O   LEU A 179     4358   4133   6537    184   -675   -236       O  
ATOM   1356  CB  LEU A 179      55.259  28.044  72.156  1.00 40.82           C  
ANISOU 1356  CB  LEU A 179     4388   4461   6662    452   -365   -196       C  
ATOM   1357  CG  LEU A 179      55.907  29.073  71.237  1.00 37.44           C  
ANISOU 1357  CG  LEU A 179     3839   4026   6359    593   -258    -97       C  
ATOM   1358  CD1 LEU A 179      55.515  30.470  71.655  1.00 50.33           C  
ANISOU 1358  CD1 LEU A 179     5477   5604   8041    600   -129    -66       C  
ATOM   1359  CD2 LEU A 179      57.378  28.920  71.342  1.00 34.09           C  
ANISOU 1359  CD2 LEU A 179     3402   3461   6089    576   -347    -48       C  
ATOM   1360  N   ARG A 180      54.243  25.257  73.096  1.00 47.70           N  
ANISOU 1360  N   ARG A 180     5399   5383   7342    261   -547   -359       N  
ATOM   1361  CA  ARG A 180      53.777  24.379  74.168  1.00 40.41           C  
ANISOU 1361  CA  ARG A 180     4562   4430   6363    140   -639   -411       C  
ATOM   1362  C   ARG A 180      54.678  23.156  74.347  1.00 33.13           C  
ANISOU 1362  C   ARG A 180     3619   3411   5556    100   -705   -383       C  
ATOM   1363  O   ARG A 180      55.081  22.851  75.473  1.00 34.10           O  
ANISOU 1363  O   ARG A 180     3770   3463   5724     -1   -807   -330       O  
ATOM   1364  CB  ARG A 180      52.296  24.007  73.997  1.00 32.46           C  
ANISOU 1364  CB  ARG A 180     3581   3560   5191    134   -597   -487       C  
ATOM   1365  CG  ARG A 180      51.340  25.152  74.334  1.00 28.65           C  
ANISOU 1365  CG  ARG A 180     3128   3132   4624    148   -530   -464       C  
ATOM   1366  CD  ARG A 180      49.865  24.849  73.990  1.00 29.73           C  
ANISOU 1366  CD  ARG A 180     3253   3438   4604    159   -480   -484       C  
ATOM   1367  NE  ARG A 180      49.317  23.738  74.750  1.00 32.52           N  
ANISOU 1367  NE  ARG A 180     3683   3776   4898     63   -568   -556       N  
ATOM   1368  CZ  ARG A 180      48.921  23.839  76.013  1.00 39.98           C  
ANISOU 1368  CZ  ARG A 180     4727   4643   5820     -9   -615   -561       C  
ATOM   1369  NH1 ARG A 180      48.442  22.774  76.652  1.00 36.51           N  
ANISOU 1369  NH1 ARG A 180     4336   4198   5340    -80   -693   -610       N  
ATOM   1370  NH2 ARG A 180      49.010  25.012  76.633  1.00 29.44           N  
ANISOU 1370  NH2 ARG A 180     3445   3231   4509    -16   -563   -524       N  
ATOM   1371  N   ALA A 181      55.019  22.476  73.252  1.00 26.88           N  
ANISOU 1371  N   ALA A 181     2770   2622   4820    170   -626   -400       N  
ATOM   1372  CA  ALA A 181      55.892  21.291  73.331  1.00 34.33           C  
ANISOU 1372  CA  ALA A 181     3684   3437   5923    151   -622   -350       C  
ATOM   1373  C   ALA A 181      57.178  21.561  74.114  1.00 42.43           C  
ANISOU 1373  C   ALA A 181     4666   4346   7110    121   -716   -175       C  
ATOM   1374  O   ALA A 181      57.623  20.756  74.927  1.00 41.51           O  
ANISOU 1374  O   ALA A 181     4524   4157   7092     51   -771    -75       O  
ATOM   1375  CB  ALA A 181      56.244  20.781  71.940  1.00 22.58           C  
ANISOU 1375  CB  ALA A 181     2151   1942   4486    232   -478   -397       C  
ATOM   1376  N   ILE A 182      57.856  22.646  73.817  1.00 36.55           N  
ANISOU 1376  N   ILE A 182     3892   3599   6395    168   -728   -116       N  
ATOM   1377  CA  ILE A 182      59.077  22.965  74.513  1.00 37.73           C  
ANISOU 1377  CA  ILE A 182     3986   3664   6684    120   -819     54       C  
ATOM   1378  C   ILE A 182      58.866  23.270  75.967  1.00 43.66           C  
ANISOU 1378  C   ILE A 182     4787   4453   7349    -52   -959     76       C  
ATOM   1379  O   ILE A 182      59.584  22.814  76.786  1.00 56.72           O  
ANISOU 1379  O   ILE A 182     6385   6086   9081   -148  -1053    226       O  
ATOM   1380  CB  ILE A 182      59.775  24.125  73.863  1.00 20.00           C  
ATOM   1381  CG1 ILE A 182      60.158  23.771  72.444  1.00 20.00           C  
ATOM   1382  CG2 ILE A 182      60.998  24.453  74.604  1.00 20.00           C  
ATOM   1383  CD1 ILE A 182      60.526  24.923  71.638  1.00 20.00           C  
ATOM   1384  N   ARG A 183      57.863  24.048  76.296  1.00 38.45           N  
ANISOU 1384  N   ARG A 183     4221   3860   6527    -94   -955    -55       N  
ATOM   1385  CA  ARG A 183      57.571  24.334  77.687  1.00 33.72           C  
ANISOU 1385  CA  ARG A 183     3695   3300   5816   -272  -1058    -71       C  
ATOM   1386  C   ARG A 183      57.382  23.067  78.521  1.00 40.67           C  
ANISOU 1386  C   ARG A 183     4563   4208   6683   -354  -1143    -16       C  
ATOM   1387  O   ARG A 183      57.912  22.974  79.620  1.00 42.43           O  
ANISOU 1387  O   ARG A 183     4760   4470   6891   -510  -1266     92       O  
ATOM   1388  CB  ARG A 183      56.319  25.205  77.781  1.00 34.31           C  
ANISOU 1388  CB  ARG A 183     3883   3415   5738   -271   -976   -227       C  
ATOM   1389  CG  ARG A 183      56.020  25.652  79.185  1.00 36.69           C  
ANISOU 1389  CG  ARG A 183     4287   3739   5916   -465  -1043   -272       C  
ATOM   1390  CD  ARG A 183      54.924  26.665  79.231  1.00 36.37           C  
ANISOU 1390  CD  ARG A 183     4353   3691   5774   -451   -906   -399       C  
ATOM   1391  NE  ARG A 183      53.633  26.037  79.454  1.00 38.82           N  
ANISOU 1391  NE  ARG A 183     4723   4056   5972   -426   -887   -459       N  
ATOM   1392  CZ  ARG A 183      52.534  26.413  78.823  1.00 53.90           C  
ANISOU 1392  CZ  ARG A 183     6650   5991   7838   -307   -748   -505       C  
ATOM   1393  NH1 ARG A 183      51.380  25.810  79.062  1.00 64.27           N  
ANISOU 1393  NH1 ARG A 183     8007   7362   9050   -296   -743   -540       N  
ATOM   1394  NH2 ARG A 183      52.605  27.387  77.931  1.00 67.44           N  
ANISOU 1394  NH2 ARG A 183     8316   7687   9620   -195   -610   -486       N  
ATOM   1395  N   PHE A 184      56.608  22.103  78.017  1.00 41.70           N  
ANISOU 1395  N   PHE A 184     4697   4336   6811   -265  -1070    -84       N  
ATOM   1396  CA  PHE A 184      56.326  20.876  78.770  1.00 38.98           C  
ANISOU 1396  CA  PHE A 184     4330   3999   6481   -324  -1116    -33       C  
ATOM   1397  C   PHE A 184      57.521  19.951  78.815  1.00 42.50           C  
ANISOU 1397  C   PHE A 184     4636   4373   7140   -318  -1125    178       C  
ATOM   1398  O   PHE A 184      57.820  19.379  79.851  1.00 54.17           O  
ANISOU 1398  O   PHE A 184     6045   5886   8651   -418  -1214    331       O  
ATOM   1399  CB  PHE A 184      55.132  20.109  78.195  1.00 41.57           C  
ANISOU 1399  CB  PHE A 184     4704   4336   6756   -249  -1017   -180       C  
ATOM   1400  CG  PHE A 184      53.827  20.766  78.428  1.00 37.88           C  
ANISOU 1400  CG  PHE A 184     4348   3954   6091   -268  -1016   -321       C  
ATOM   1401  CD1 PHE A 184      52.963  21.004  77.377  1.00 41.92           C  
ANISOU 1401  CD1 PHE A 184     4886   4519   6522   -178   -910   -441       C  
ATOM   1402  CD2 PHE A 184      53.460  21.166  79.698  1.00 39.58           C  
ANISOU 1402  CD2 PHE A 184     4631   4212   6195   -386  -1107   -314       C  
ATOM   1403  CE1 PHE A 184      51.754  21.630  77.594  1.00 43.96           C  
ANISOU 1403  CE1 PHE A 184     5222   4859   6622   -185   -890   -516       C  
ATOM   1404  CE2 PHE A 184      52.264  21.786  79.914  1.00 35.49           C  
ANISOU 1404  CE2 PHE A 184     4219   3744   5522   -392  -1070   -423       C  
ATOM   1405  CZ  PHE A 184      51.408  22.014  78.867  1.00 34.38           C  
ANISOU 1405  CZ  PHE A 184     4088   3643   5331   -282   -958   -506       C  
ATOM   1406  N   GLU A 185      58.178  19.781  77.675  1.00 43.18           N  
ANISOU 1406  N   GLU A 185     4665   4365   7375   -196  -1013    207       N  
ATOM   1407  CA  GLU A 185      59.457  19.040  77.634  1.00 47.58           C  
ANISOU 1407  CA  GLU A 185     5080   4824   8173   -170   -983    446       C  
ATOM   1408  C   GLU A 185      60.546  19.563  78.539  1.00 43.65           C  
ANISOU 1408  C   GLU A 185     4493   4399   7694   -304  -1152    677       C  
ATOM   1409  O   GLU A 185      61.398  18.796  78.952  1.00 47.81           O  
ANISOU 1409  O   GLU A 185     4883   4928   8356   -355  -1184    924       O  
ATOM   1410  CB  GLU A 185      60.109  19.241  76.262  1.00 49.16           C  
ANISOU 1410  CB  GLU A 185     5255   4922   8500    -29   -848    439       C  
ATOM   1411  CG  GLU A 185      61.465  18.603  76.147  1.00 38.17           C  
ANISOU 1411  CG  GLU A 185     3716   3407   7381     14   -788    713       C  
ATOM   1412  CD  GLU A 185      62.160  18.931  74.833  1.00 46.05           C  
ANISOU 1412  CD  GLU A 185     4700   4305   8492    155   -658    709       C  
ATOM   1413  OE1 GLU A 185      62.320  20.126  74.493  1.00 44.23           O  
ANISOU 1413  OE1 GLU A 185     4499   4133   8173    178   -725    659       O  
ATOM   1414  OE2 GLU A 185      62.549  17.977  74.134  1.00 48.26           O  
ANISOU 1414  OE2 GLU A 185     4938   4436   8963    244   -464    757       O  
ATOM   1415  N   GLN A 186      60.536  20.836  78.853  1.00 44.96           N  
ANISOU 1415  N   GLN A 186     4722   4635   7727   -373  -1244    609       N  
ATOM   1416  CA  GLN A 186      61.458  21.440  79.813  1.00 40.36           C  
ANISOU 1416  CA  GLN A 186     4068   4147   7120   -549  -1406    789       C  
ATOM   1417  C   GLN A 186      60.955  21.444  81.252  1.00 50.49           C  
ANISOU 1417  C   GLN A 186     5383   5588   8212   -762  -1548    789       C  
ATOM   1418  O   GLN A 186      61.762  21.372  82.186  1.00 66.24           O  
ANISOU 1418  O   GLN A 186     7261   7706  10201   -934  -1687   1014       O  
ATOM   1419  CB  GLN A 186      61.841  22.868  79.347  1.00 22.27           C  
ANISOU 1419  CB  GLN A 186     1830   1841   4789   -555  -1412    704       C  
ATOM   1420  CG  GLN A 186      62.509  22.873  77.977  1.00 46.63           C  
ANISOU 1420  CG  GLN A 186     4853   4793   8070   -351  -1289    756       C  
ATOM   1421  CD  GLN A 186      63.694  21.903  77.895  1.00 47.76           C  
ANISOU 1421  CD  GLN A 186     4819   4873   8453   -311  -1281   1066       C  
ATOM   1422  OE1 GLN A 186      64.620  21.959  78.703  1.00 50.27           O  
ANISOU 1422  OE1 GLN A 186     5017   5268   8815   -453  -1414   1313       O  
ATOM   1423  NE2 GLN A 186      63.667  21.023  76.912  1.00 35.08           N  
ANISOU 1423  NE2 GLN A 186     3191   3135   7004   -130  -1108   1065       N  
ATOM   1424  N   ARG A 187      59.650  21.482  81.455  1.00 49.15           N  
ANISOU 1424  N   ARG A 187     5358   5436   7879   -757  -1513    559       N  
ATOM   1425  CA  ARG A 187      59.107  21.395  82.784  1.00 43.96           C  
ANISOU 1425  CA  ARG A 187     4745   4919   7039   -941  -1624    547       C  
ATOM   1426  C   ARG A 187      59.362  20.075  83.439  1.00 50.76           C  
ANISOU 1426  C   ARG A 187     5436   5840   8010   -966  -1677    804       C  
ATOM   1427  O   ARG A 187      59.821  20.005  84.551  1.00 56.12           O  
ANISOU 1427  O   ARG A 187     5990   6669   8664  -1141  -1815   1031       O  
ATOM   1428  CB  ARG A 187      57.618  21.547  82.725  1.00 40.77           C  
ANISOU 1428  CB  ARG A 187     4515   4497   6480   -892  -1548    285       C  
ATOM   1429  CG  ARG A 187      57.017  21.252  84.012  1.00 31.40           C  
ANISOU 1429  CG  ARG A 187     3357   3430   5144  -1031  -1635    294       C  
ATOM   1430  CD  ARG A 187      55.576  21.204  83.919  1.00 35.90           C  
ANISOU 1430  CD  ARG A 187     4085   3964   5592   -957  -1546     69       C  
ATOM   1431  NE  ARG A 187      55.062  22.417  83.366  1.00 36.14           N  
ANISOU 1431  NE  ARG A 187     4267   3952   5511   -962  -1462   -123       N  
ATOM   1432  CZ  ARG A 187      53.788  22.722  83.316  1.00 45.84           C  
ANISOU 1432  CZ  ARG A 187     5616   5145   6655   -877  -1353   -284       C  
ATOM   1433  NH1 ARG A 187      53.420  23.852  82.795  1.00 47.17           N  
ANISOU 1433  NH1 ARG A 187     5892   5264   6766   -868  -1238   -410       N  
ATOM   1434  NH2 ARG A 187      52.896  21.912  83.794  1.00 37.17           N  
ANISOU 1434  NH2 ARG A 187     4513   4058   5551   -799  -1342   -296       N  
ATOM   1435  N   PHE A 188      59.095  19.015  82.708  1.00 51.53           N  
ANISOU 1435  N   PHE A 188     5517   5835   8227   -806  -1557    777       N  
ATOM   1436  CA  PHE A 188      59.295  17.671  83.167  1.00 47.63           C  
ANISOU 1436  CA  PHE A 188     4833   5328   7935   -773  -1527   1043       C  
ATOM   1437  C   PHE A 188      60.477  17.418  82.362  1.00 59.10           C  
ANISOU 1437  C   PHE A 188     6150   6678   9627   -690  -1460   1248       C  
ATOM   1438  O   PHE A 188      60.630  18.009  81.329  1.00 74.70           O  
ANISOU 1438  O   PHE A 188     8207   8585  11590   -632  -1428   1120       O  
ATOM   1439  CB  PHE A 188      58.245  16.724  82.658  1.00 43.72           C  
ANISOU 1439  CB  PHE A 188     4389   4702   7521   -625  -1366    895       C  
ATOM   1440  CG  PHE A 188      56.873  17.220  82.752  1.00 43.60           C  
ANISOU 1440  CG  PHE A 188     4577   4721   7267   -632  -1376    583       C  
ATOM   1441  CD1 PHE A 188      56.197  17.573  81.641  1.00 47.65           C  
ANISOU 1441  CD1 PHE A 188     5214   5143   7746   -513  -1257    339       C  
ATOM   1442  CD2 PHE A 188      56.243  17.306  83.940  1.00 38.24           C  
ANISOU 1442  CD2 PHE A 188     3952   4186   6392   -765  -1498    561       C  
ATOM   1443  CE1 PHE A 188      54.949  18.012  81.729  1.00 46.75           C  
ANISOU 1443  CE1 PHE A 188     5257   5078   7427   -517  -1257    111       C  
ATOM   1444  CE2 PHE A 188      54.993  17.759  84.008  1.00 38.98           C  
ANISOU 1444  CE2 PHE A 188     4226   4294   6290   -760  -1484    310       C  
ATOM   1445  CZ  PHE A 188      54.357  18.108  82.906  1.00 44.22           C  
ANISOU 1445  CZ  PHE A 188     4994   4864   6942   -631  -1362    102       C  
ATOM   1446  N   ASP A 189      61.408  16.619  82.800  1.00 56.98           N  
ANISOU 1446  N   ASP A 189     5662   6392   9594   -672  -1421   1590       N  
ATOM   1447  CA  ASP A 189      62.533  16.521  81.915  1.00 67.10           C  
ANISOU 1447  CA  ASP A 189     6832   7546  11118   -571  -1326   1780       C  
ATOM   1448  C   ASP A 189      62.383  15.457  80.864  1.00 66.68           C  
ANISOU 1448  C   ASP A 189     6775   7232  11327   -360  -1045   1730       C  
ATOM   1449  O   ASP A 189      63.158  14.541  80.778  1.00 69.70           O  
ANISOU 1449  O   ASP A 189     6981   7491  12012   -278   -894   2020       O  
ATOM   1450  CB  ASP A 189      63.853  16.538  82.666  1.00 77.45           C  
ANISOU 1450  CB  ASP A 189     7902   9007  12518   -702  -1461   2215       C  
ATOM   1451  CG  ASP A 189      64.216  17.943  83.128  1.00102.25           C  
ANISOU 1451  CG  ASP A 189    11110  12331  15410   -898  -1681   2152       C  
ATOM   1452  OD1 ASP A 189      63.878  18.329  84.262  1.00110.02           O  
ANISOU 1452  OD1 ASP A 189    12183  13209  16409   -827  -1647   2018       O  
ATOM   1453  OD2 ASP A 189      64.823  18.685  82.335  1.00108.66           O  
ANISOU 1453  OD2 ASP A 189    11891  13391  16005  -1132  -1873   2219       O  
ATOM   1454  N   PHE A 190      61.366  15.661  80.038  1.00 59.52           N  
ANISOU 1454  N   PHE A 190     6071   6255  10288   -289   -963   1352       N  
ATOM   1455  CA  PHE A 190      60.971  14.785  78.956  1.00 50.98           C  
ANISOU 1455  CA  PHE A 190     5041   4969   9360   -146   -703   1194       C  
ATOM   1456  C   PHE A 190      61.704  15.172  77.692  1.00 49.76           C  
ANISOU 1456  C   PHE A 190     4909   4687   9311    -33   -579   1161       C  
ATOM   1457  O   PHE A 190      62.381  16.183  77.671  1.00 54.02           O  
ANISOU 1457  O   PHE A 190     5433   5297   9794    -54   -710   1239       O  
ATOM   1458  CB  PHE A 190      59.467  14.903  78.762  1.00 41.34           C  
ANISOU 1458  CB  PHE A 190     4009   3798   7901   -158   -706    828       C  
ATOM   1459  CG  PHE A 190      58.669  14.248  79.856  1.00 42.65           C  
ANISOU 1459  CG  PHE A 190     4152   4040   8014   -234   -767    853       C  
ATOM   1460  CD1 PHE A 190      57.282  14.117  79.763  1.00 36.34           C  
ANISOU 1460  CD1 PHE A 190     3495   3270   7042   -241   -750    570       C  
ATOM   1461  CD2 PHE A 190      59.306  13.740  80.975  1.00 30.88           C  
ANISOU 1461  CD2 PHE A 190     2475   2609   6648   -298   -839   1189       C  
ATOM   1462  CE1 PHE A 190      56.559  13.496  80.784  1.00 36.96           C  
ANISOU 1462  CE1 PHE A 190     3547   3410   7088   -298   -802    609       C  
ATOM   1463  CE2 PHE A 190      58.580  13.115  81.994  1.00 37.77           C  
ANISOU 1463  CE2 PHE A 190     3308   3565   7477   -358   -890   1234       C  
ATOM   1464  CZ  PHE A 190      57.211  12.996  81.902  1.00 29.52           C  
ANISOU 1464  CZ  PHE A 190     2422   2521   6272   -352   -870    935       C  
ATOM   1465  N   ARG A 191      61.605  14.351  76.651  1.00 42.94           N  
ANISOU 1465  N   ARG A 191     4078   3634   8605     74   -314   1046       N  
ATOM   1466  CA  ARG A 191      62.184  14.698  75.357  1.00 49.99           C  
ANISOU 1466  CA  ARG A 191     5010   4416   9567    181   -176    976       C  
ATOM   1467  C   ARG A 191      61.135  14.549  74.265  1.00 53.35           C  
ANISOU 1467  C   ARG A 191     5603   4825   9841    208    -29    591       C  
ATOM   1468  O   ARG A 191      60.419  13.548  74.219  1.00 55.67           O  
ANISOU 1468  O   ARG A 191     5935   5049  10168    179    121    456       O  
ATOM   1469  CB  ARG A 191      63.394  13.815  75.025  1.00 66.24           C  
ANISOU 1469  CB  ARG A 191     6921   6248  12001    273     58   1267       C  
ATOM   1470  CG  ARG A 191      63.035  12.342  74.886  1.00 79.68           C  
ANISOU 1470  CG  ARG A 191     8607   7753  13913    294    352   1231       C  
ATOM   1471  CD  ARG A 191      63.878  11.569  73.863  1.00 82.18           C  
ANISOU 1471  CD  ARG A 191     8889   7783  14553    406    716   1310       C  
ATOM   1472  NE  ARG A 191      63.131  10.403  73.387  1.00 80.88           N  
ANISOU 1472  NE  ARG A 191     8811   7445  14475    389   1023   1064       N  
ATOM   1473  CZ  ARG A 191      62.666   9.439  74.183  1.00 86.49           C  
ANISOU 1473  CZ  ARG A 191     9451   8098  15314    344   1104   1133       C  
ATOM   1474  NH1 ARG A 191      61.988   8.412  73.671  1.00 85.43           N  
ANISOU 1474  NH1 ARG A 191     9407   7790  15262    312   1405    877       N  
ATOM   1475  NH2 ARG A 191      62.875   9.496  75.497  1.00 87.09           N  
ANISOU 1475  NH2 ARG A 191     9359   8303  15427    316    889   1457       N  
ATOM   1476  N   ILE A 192      61.042  15.550  73.396  1.00 49.81           N  
ANISOU 1476  N   ILE A 192     5238   4461   9225    250    -70    429       N  
ATOM   1477  CA  ILE A 192      60.162  15.488  72.235  1.00 43.66           C  
ANISOU 1477  CA  ILE A 192     4584   3724   8282    262     64    107       C  
ATOM   1478  C   ILE A 192      60.605  14.346  71.308  1.00 44.35           C  
ANISOU 1478  C   ILE A 192     4670   3597   8584    303    386     65       C  
ATOM   1479  O   ILE A 192      61.695  14.370  70.765  1.00 41.28           O  
ANISOU 1479  O   ILE A 192     4225   3073   8386    393    505    213       O  
ATOM   1480  CB  ILE A 192      60.129  16.850  71.501  1.00 34.51           C  
ANISOU 1480  CB  ILE A 192     3464   2716   6933    316    -34     21       C  
ATOM   1481  CG1 ILE A 192      59.598  17.937  72.448  1.00 34.21           C  
ANISOU 1481  CG1 ILE A 192     3446   2849   6704    260   -288     34       C  
ATOM   1482  CG2 ILE A 192      59.268  16.788  70.263  1.00 37.35           C  
ANISOU 1482  CG2 ILE A 192     3911   3176   7103    314    100   -263       C  
ATOM   1483  CD1 ILE A 192      59.970  19.360  72.015  1.00 30.34           C  
ANISOU 1483  CD1 ILE A 192     2944   2443   6139    325   -372     61       C  
ATOM   1484  N   GLU A 193      59.756  13.339  71.146  1.00 49.27           N  
ANISOU 1484  N   GLU A 193     5359   4175   9185    227    547   -140       N  
ATOM   1485  CA  GLU A 193      60.109  12.172  70.348  1.00 51.60           C  
ANISOU 1485  CA  GLU A 193     5674   4236   9697    229    904   -216       C  
ATOM   1486  C   GLU A 193      60.383  12.542  68.895  1.00 47.28           C  
ANISOU 1486  C   GLU A 193     5198   3708   9058    264   1048   -385       C  
ATOM   1487  O   GLU A 193      59.923  13.568  68.417  1.00 51.61           O  
ANISOU 1487  O   GLU A 193     5789   4496   9326    266    882   -506       O  
ATOM   1488  CB  GLU A 193      59.044  11.048  70.471  1.00 76.15           C  
ANISOU 1488  CB  GLU A 193     8850   7301  12783    107   1055   -444       C  
ATOM   1489  CG  GLU A 193      57.678  11.280  69.787  1.00 64.67           C  
ANISOU 1489  CG  GLU A 193     7530   6085  10958    -14   1007   -816       C  
ATOM   1490  CD  GLU A 193      57.682  10.954  68.296  1.00 70.29           C  
ANISOU 1490  CD  GLU A 193     8335   6777  11594    -75   1276  -1083       C  
ATOM   1491  OE1 GLU A 193      58.409  10.025  67.881  1.00 85.27           O  
ANISOU 1491  OE1 GLU A 193    10236   8395  13766    -68   1603  -1079       O  
ATOM   1492  OE2 GLU A 193      56.949  11.619  67.534  1.00 63.08           O  
ANISOU 1492  OE2 GLU A 193     7483   6138  10347   -138   1180  -1286       O  
ATOM   1493  N   GLU A 194      61.129  11.682  68.209  1.00 60.55           N  
ANISOU 1493  N   GLU A 194     6882   5132  10991    294   1385   -375       N  
ATOM   1494  CA  GLU A 194      61.610  11.912  66.843  1.00 68.11           C  
ANISOU 1494  CA  GLU A 194     7899   6068  11911    335   1570   -497       C  
ATOM   1495  C   GLU A 194      60.571  12.511  65.885  1.00 64.22           C  
ANISOU 1495  C   GLU A 194     7512   5889  11001    239   1492   -835       C  
ATOM   1496  O   GLU A 194      60.755  13.613  65.367  1.00 55.85           O  
ANISOU 1496  O   GLU A 194     6427   5012   9780    316   1344   -801       O  
ATOM   1497  CB  GLU A 194      62.157  10.598  66.274  1.00 72.55           C  
ANISOU 1497  CB  GLU A 194     8499   6294  12774    316   2023   -546       C  
ATOM   1498  CG  GLU A 194      63.032  10.721  65.042  1.00 82.84           C  
ANISOU 1498  CG  GLU A 194     9840   7488  14149    391   2262   -569       C  
ATOM   1499  CD  GLU A 194      63.590   9.369  64.615  1.00100.48           C  
ANISOU 1499  CD  GLU A 194    12117   9334  16728    368   2762   -600       C  
ATOM   1500  OE1 GLU A 194      64.409   9.323  63.671  1.00115.12           O  
ANISOU 1500  OE1 GLU A 194    14006  11035  18700    435   3019   -592       O  
ATOM   1501  OE2 GLU A 194      63.210   8.348  65.229  1.00 97.37           O  
ANISOU 1501  OE2 GLU A 194    11720   8771  16505    288   2923   -625       O  
ATOM   1502  N   THR A 195      59.483  11.788  65.647  1.00 59.40           N  
ANISOU 1502  N   THR A 195     6996   5353  10221     66   1599  -1136       N  
ATOM   1503  CA  THR A 195      58.508  12.223  64.654  1.00 46.77           C  
ANISOU 1503  CA  THR A 195     5470   4081   8220    -56   1557  -1430       C  
ATOM   1504  C   THR A 195      58.009  13.621  64.932  1.00 46.40           C  
ANISOU 1504  C   THR A 195     5359   4351   7920     12   1197  -1329       C  
ATOM   1505  O   THR A 195      57.967  14.454  64.032  1.00 51.05           O  
ANISOU 1505  O   THR A 195     5929   5165   8302     41   1152  -1369       O  
ATOM   1506  CB  THR A 195      57.297  11.284  64.564  1.00 45.54           C  
ANISOU 1506  CB  THR A 195     5406   3998   7899   -281   1669  -1741       C  
ATOM   1507  OG1 THR A 195      57.733   9.949  64.264  1.00 50.54           O  
ANISOU 1507  OG1 THR A 195     6109   4302   8790   -362   2065  -1866       O  
ATOM   1508  CG2 THR A 195      56.375  11.763  63.480  1.00 34.07           C  
ANISOU 1508  CG2 THR A 195     3995   2934   6017   -425   1620  -1995       C  
ATOM   1509  N   THR A 196      57.627  13.872  66.180  1.00 44.28           N  
ANISOU 1509  N   THR A 196     5051   4095   7677     34    967  -1191       N  
ATOM   1510  CA  THR A 196      57.121  15.177  66.560  1.00 36.45           C  
ANISOU 1510  CA  THR A 196     4012   3357   6480     89    671  -1099       C  
ATOM   1511  C   THR A 196      58.189  16.243  66.297  1.00 39.94           C  
ANISOU 1511  C   THR A 196     4379   3782   7014    255    601   -892       C  
ATOM   1512  O   THR A 196      57.897  17.321  65.786  1.00 42.09           O  
ANISOU 1512  O   THR A 196     4615   4285   7094    303    496   -889       O  
ATOM   1513  CB  THR A 196      56.631  15.208  68.021  1.00 32.27           C  
ANISOU 1513  CB  THR A 196     3471   2808   5984     73    470   -989       C  
ATOM   1514  OG1 THR A 196      55.577  14.258  68.192  1.00 43.91           O  
ANISOU 1514  OG1 THR A 196     5006   4311   7368    -72    536  -1182       O  
ATOM   1515  CG2 THR A 196      56.041  16.556  68.351  1.00 32.40           C  
ANISOU 1515  CG2 THR A 196     3460   3061   5791    113    226   -925       C  
ATOM   1516  N   GLU A 197      59.438  15.925  66.600  1.00 40.57           N  
ANISOU 1516  N   GLU A 197     4418   3591   7405    345    679   -696       N  
ATOM   1517  CA  GLU A 197      60.530  16.877  66.393  1.00 42.37           C  
ANISOU 1517  CA  GLU A 197     4568   3782   7749    496    613   -481       C  
ATOM   1518  C   GLU A 197      60.738  17.270  64.911  1.00 41.97           C  
ANISOU 1518  C   GLU A 197     4520   3841   7586    553    749   -583       C  
ATOM   1519  O   GLU A 197      60.956  18.432  64.589  1.00 31.71           O  
ANISOU 1519  O   GLU A 197     3156   2677   6216    655    633   -489       O  
ATOM   1520  CB  GLU A 197      61.818  16.335  67.011  1.00 33.28           C  
ANISOU 1520  CB  GLU A 197     3351   2331   6961    566    682   -213       C  
ATOM   1521  CG  GLU A 197      62.941  17.333  66.993  1.00 51.42           C  
ANISOU 1521  CG  GLU A 197     5555   4598   9386    702    576     39       C  
ATOM   1522  CD  GLU A 197      64.215  16.777  67.576  1.00 64.18           C  
ANISOU 1522  CD  GLU A 197     7077   5952  11357    758    642    351       C  
ATOM   1523  OE1 GLU A 197      64.136  16.140  68.649  1.00 68.00           O  
ANISOU 1523  OE1 GLU A 197     7525   6367  11946    687    596    463       O  
ATOM   1524  OE2 GLU A 197      65.288  16.983  66.966  1.00 65.22           O  
ANISOU 1524  OE2 GLU A 197     7146   5991  11645    853    742    512       O  
ATOM   1525  N   ARG A 198      60.678  16.290  64.020  1.00 40.86           N  
ANISOU 1525  N   ARG A 198     4451   3640   7434    476   1016   -777       N  
ATOM   1526  CA  ARG A 198      60.696  16.542  62.590  1.00 44.88           C  
ANISOU 1526  CA  ARG A 198     4973   4308   7770    480   1157   -918       C  
ATOM   1527  C   ARG A 198      59.530  17.484  62.223  1.00 49.21           C  
ANISOU 1527  C   ARG A 198     5484   5268   7946    431    975  -1018       C  
ATOM   1528  O   ARG A 198      59.714  18.523  61.586  1.00 47.46           O  
ANISOU 1528  O   ARG A 198     5176   5227   7628    540    911   -930       O  
ATOM   1529  CB  ARG A 198      60.584  15.203  61.844  1.00 55.49           C  
ANISOU 1529  CB  ARG A 198     6432   5536   9117    330   1489  -1176       C  
ATOM   1530  CG  ARG A 198      61.152  15.193  60.424  1.00 69.50           C  
ANISOU 1530  CG  ARG A 198     8232   7338  10837    348   1725  -1274       C  
ATOM   1531  CD  ARG A 198      60.691  13.984  59.614  1.00 70.52           C  
ANISOU 1531  CD  ARG A 198     8498   7448  10848    120   2049  -1624       C  
ATOM   1532  NE  ARG A 198      59.238  13.939  59.446  1.00 68.44           N  
ANISOU 1532  NE  ARG A 198     8265   7545  10194    -99   1943  -1878       N  
ATOM   1533  CZ  ARG A 198      58.468  12.941  59.874  1.00 78.56           C  
ANISOU 1533  CZ  ARG A 198     9633   8763  11453   -292   2028  -2079       C  
ATOM   1534  NH1 ARG A 198      57.158  12.986  59.684  1.00 83.76           N  
ANISOU 1534  NH1 ARG A 198    10300   9780  11746   -490   1911  -2278       N  
ATOM   1535  NH2 ARG A 198      59.009  11.890  60.485  1.00 84.73           N  
ANISOU 1535  NH2 ARG A 198    10474   9126  12593   -286   2244  -2057       N  
ATOM   1536  N   LEU A 199      58.329  17.109  62.639  1.00 45.90           N  
ANISOU 1536  N   LEU A 199     5110   4992   7339    277    907  -1173       N  
ATOM   1537  CA  LEU A 199      57.148  17.948  62.476  1.00 42.17           C  
ANISOU 1537  CA  LEU A 199     4581   4896   6546    231    738  -1209       C  
ATOM   1538  C   LEU A 199      57.331  19.352  63.066  1.00 42.44           C  
ANISOU 1538  C   LEU A 199     4513   4979   6632    401    523   -962       C  
ATOM   1539  O   LEU A 199      57.071  20.352  62.403  1.00 50.61           O  
ANISOU 1539  O   LEU A 199     5449   6268   7511    468    479   -897       O  
ATOM   1540  CB  LEU A 199      55.938  17.258  63.112  1.00 35.90           C  
ANISOU 1540  CB  LEU A 199     3851   4173   5616     55    688  -1361       C  
ATOM   1541  CG  LEU A 199      55.062  16.344  62.249  1.00 38.78           C  
ANISOU 1541  CG  LEU A 199     4278   4730   5725   -178    844  -1652       C  
ATOM   1542  CD1 LEU A 199      55.641  16.167  60.860  1.00 35.86           C  
ANISOU 1542  CD1 LEU A 199     3916   4430   5278   -213   1059  -1770       C  
ATOM   1543  CD2 LEU A 199      54.801  15.005  62.933  1.00 38.18           C  
ANISOU 1543  CD2 LEU A 199     4312   4412   5781   -315    951  -1804       C  
ATOM   1544  N   LEU A 200      57.772  19.428  64.313  1.00 46.67           N  
ANISOU 1544  N   LEU A 200     5064   5280   7387    455    405   -819       N  
ATOM   1545  CA  LEU A 200      57.973  20.720  64.962  1.00 48.41           C  
ANISOU 1545  CA  LEU A 200     5213   5517   7663    573    227   -621       C  
ATOM   1546  C   LEU A 200      58.960  21.580  64.170  1.00 47.42           C  
ANISOU 1546  C   LEU A 200     4996   5387   7634    734    269   -482       C  
ATOM   1547  O   LEU A 200      58.678  22.745  63.869  1.00 40.87           O  
ANISOU 1547  O   LEU A 200     4077   4739   6714    816    212   -401       O  
ATOM   1548  CB  LEU A 200      58.437  20.542  66.416  1.00 38.71           C  
ANISOU 1548  CB  LEU A 200     4018   4050   6641    562    107   -500       C  
ATOM   1549  CG  LEU A 200      58.569  21.787  67.302  1.00 36.97           C  
ANISOU 1549  CG  LEU A 200     3757   3832   6458    617    -68   -343       C  
ATOM   1550  CD1 LEU A 200      58.269  21.491  68.784  1.00 40.60           C  
ANISOU 1550  CD1 LEU A 200     4274   4203   6949    514   -201   -319       C  
ATOM   1551  CD2 LEU A 200      59.928  22.426  67.162  1.00 27.92           C  
ANISOU 1551  CD2 LEU A 200     2540   2548   5522    737    -75   -159       C  
ATOM   1552  N   LYS A 201      60.111  20.994  63.837  1.00 36.20           N  
ANISOU 1552  N   LYS A 201     3588   3746   6422    786    390   -435       N  
ATOM   1553  CA  LYS A 201      61.140  21.663  63.044  1.00 30.18           C  
ANISOU 1553  CA  LYS A 201     2742   2949   5777    945    448   -296       C  
ATOM   1554  C   LYS A 201      60.572  22.161  61.712  1.00 46.08           C  
ANISOU 1554  C   LYS A 201     4690   5277   7542    971    528   -382       C  
ATOM   1555  O   LYS A 201      60.817  23.292  61.293  1.00 40.86           O  
ANISOU 1555  O   LYS A 201     3913   4727   6885   1108    489   -243       O  
ATOM   1556  CB  LYS A 201      62.286  20.699  62.747  1.00 31.18           C  
ANISOU 1556  CB  LYS A 201     2905   2798   6143    978    625   -256       C  
ATOM   1557  CG  LYS A 201      63.317  20.473  63.865  1.00 42.38           C  
ANISOU 1557  CG  LYS A 201     4308   3918   7878   1015    556    -30       C  
ATOM   1558  CD  LYS A 201      64.714  20.279  63.250  1.00 54.03           C  
ANISOU 1558  CD  LYS A 201     5746   5209   9573   1086    708    147       C  
ATOM   1559  CE  LYS A 201      65.595  19.317  64.032  1.00 64.87           C  
ANISOU 1559  CE  LYS A 201     7106   6306  11235   1046    781    329       C  
ATOM   1560  NZ  LYS A 201      65.376  17.892  63.638  1.00 72.25           N  
ANISOU 1560  NZ  LYS A 201     8136   7038  12279   1051   1063    157       N  
ATOM   1561  N   GLN A 202      59.801  21.311  61.044  1.00 45.23           N  
ANISOU 1561  N   GLN A 202     4642   5331   7212    823    647   -605       N  
ATOM   1562  CA  GLN A 202      59.272  21.670  59.746  1.00 32.40           C  
ANISOU 1562  CA  GLN A 202     2939   4059   5313    805    724   -677       C  
ATOM   1563  C   GLN A 202      58.321  22.863  59.793  1.00 43.25           C  
ANISOU 1563  C   GLN A 202     4177   5750   6505    846    581   -566       C  
ATOM   1564  O   GLN A 202      58.360  23.741  58.909  1.00 34.32           O  
ANISOU 1564  O   GLN A 202     2899   4855   5287    953    607   -450       O  
ATOM   1565  CB  GLN A 202      58.598  20.475  59.093  1.00 35.64           C  
ANISOU 1565  CB  GLN A 202     3447   4600   5494    580    878   -959       C  
ATOM   1566  CG  GLN A 202      58.346  20.678  57.594  1.00 54.32           C  
ANISOU 1566  CG  GLN A 202     5733   7333   7572    530    995  -1039       C  
ATOM   1567  CD  GLN A 202      57.546  19.549  56.976  1.00 70.53           C  
ANISOU 1567  CD  GLN A 202     7887   9571   9342    245   1139  -1350       C  
ATOM   1568  OE1 GLN A 202      57.384  18.478  57.574  1.00 73.74           O  
ANISOU 1568  OE1 GLN A 202     8439   9746   9831    107   1206  -1521       O  
ATOM   1569  NE2 GLN A 202      57.043  19.779  55.766  1.00 74.27           N  
ANISOU 1569  NE2 GLN A 202     8269  10476   9475    140   1195  -1419       N  
ATOM   1570  N   ALA A 203      57.463  22.901  60.815  1.00 40.28           N  
ANISOU 1570  N   ALA A 203     3838   5379   6088    771    452   -578       N  
ATOM   1571  CA  ALA A 203      56.506  23.999  60.907  1.00 39.19           C  
ANISOU 1571  CA  ALA A 203     3573   5509   5807    811    362   -454       C  
ATOM   1572  C   ALA A 203      57.238  25.308  61.171  1.00 41.58           C  
ANISOU 1572  C   ALA A 203     3775   5694   6331   1019    319   -222       C  
ATOM   1573  O   ALA A 203      56.872  26.340  60.632  1.00 50.47           O  
ANISOU 1573  O   ALA A 203     4742   7051   7384   1116    342    -74       O  
ATOM   1574  CB  ALA A 203      55.450  23.740  61.963  1.00 30.16           C  
ANISOU 1574  CB  ALA A 203     2505   4368   4588    690    258   -514       C  
ATOM   1575  N   VAL A 204      58.277  25.261  61.998  1.00 32.66           N  
ANISOU 1575  N   VAL A 204     2724   4211   5473   1074    269   -174       N  
ATOM   1576  CA  VAL A 204      59.086  26.442  62.257  1.00 34.88           C  
ANISOU 1576  CA  VAL A 204     3042   4333   5877   1114    223     29       C  
ATOM   1577  C   VAL A 204      59.712  26.920  60.955  1.00 36.70           C  
ANISOU 1577  C   VAL A 204     3189   4666   6088   1216    324    134       C  
ATOM   1578  O   VAL A 204      59.556  28.077  60.566  1.00 35.79           O  
ANISOU 1578  O   VAL A 204     3013   4669   5917   1267    348    288       O  
ATOM   1579  CB  VAL A 204      60.230  26.163  63.258  1.00 36.09           C  
ANISOU 1579  CB  VAL A 204     3301   4144   6268   1059    151     74       C  
ATOM   1580  CG1 VAL A 204      61.186  27.370  63.342  1.00 37.38           C  
ANISOU 1580  CG1 VAL A 204     3454   4195   6552   1067    142    259       C  
ATOM   1581  CG2 VAL A 204      59.698  25.800  64.620  1.00 30.53           C  
ANISOU 1581  CG2 VAL A 204     2670   3346   5585    962     39      4       C  
ATOM   1582  N   GLU A 205      60.413  26.015  60.283  1.00 32.16           N  
ANISOU 1582  N   GLU A 205     2611   4033   5574   1255    412     57       N  
ATOM   1583  CA  GLU A 205      61.148  26.375  59.082  1.00 41.78           C  
ANISOU 1583  CA  GLU A 205     3762   5319   6795   1358    515    155       C  
ATOM   1584  C   GLU A 205      60.269  27.005  58.014  1.00 46.55           C  
ANISOU 1584  C   GLU A 205     4204   6335   7148   1411    569    194       C  
ATOM   1585  O   GLU A 205      60.685  27.944  57.332  1.00 52.41           O  
ANISOU 1585  O   GLU A 205     4886   7143   7884   1501    602    381       O  
ATOM   1586  CB  GLU A 205      61.919  25.177  58.504  1.00 42.39           C  
ANISOU 1586  CB  GLU A 205     3864   5267   6975   1391    657     33       C  
ATOM   1587  CG  GLU A 205      61.775  25.053  56.997  1.00 65.98           C  
ANISOU 1587  CG  GLU A 205     6722   8558   9791   1461    828    -43       C  
ATOM   1588  CD  GLU A 205      63.095  24.955  56.258  1.00 83.48           C  
ANISOU 1588  CD  GLU A 205     8965  10586  12166   1563    949     47       C  
ATOM   1589  OE1 GLU A 205      63.359  23.866  55.709  1.00 94.74           O  
ANISOU 1589  OE1 GLU A 205    10452  11953  13591   1525   1142   -135       O  
ATOM   1590  OE2 GLU A 205      63.854  25.960  56.201  1.00 80.61           O  
ANISOU 1590  OE2 GLU A 205     8602  10126  11900   1628    878    297       O  
ATOM   1591  N   GLU A 206      59.056  26.489  57.872  1.00 42.46           N  
ANISOU 1591  N   GLU A 206     3592   6120   6420   1338    588     41       N  
ATOM   1592  CA  GLU A 206      58.194  26.906  56.778  1.00 45.03           C  
ANISOU 1592  CA  GLU A 206     3711   6927   6471   1342    652     93       C  
ATOM   1593  C   GLU A 206      57.516  28.247  56.979  1.00 47.52           C  
ANISOU 1593  C   GLU A 206     3972   7365   6720   1387    584    349       C  
ATOM   1594  O   GLU A 206      57.108  28.859  56.008  1.00 55.82           O  
ANISOU 1594  O   GLU A 206     4846   8767   7596   1438    640    506       O  
ATOM   1595  CB  GLU A 206      57.168  25.827  56.466  1.00 45.69           C  
ANISOU 1595  CB  GLU A 206     3846   7281   6235   1095    679   -140       C  
ATOM   1596  CG  GLU A 206      57.758  24.687  55.682  1.00 45.57           C  
ANISOU 1596  CG  GLU A 206     3958   7219   6139    977    813   -365       C  
ATOM   1597  CD  GLU A 206      56.911  23.454  55.731  1.00 52.80           C  
ANISOU 1597  CD  GLU A 206     5019   8230   6813    688    841   -647       C  
ATOM   1598  OE1 GLU A 206      57.357  22.405  55.225  1.00 62.12           O  
ANISOU 1598  OE1 GLU A 206     6339   9307   7957    560    992   -872       O  
ATOM   1599  OE2 GLU A 206      55.798  23.534  56.277  1.00 53.52           O  
ANISOU 1599  OE2 GLU A 206     5085   8484   6766    588    734   -644       O  
ATOM   1600  N   GLY A 207      57.414  28.700  58.228  1.00 49.61           N  
ANISOU 1600  N   GLY A 207     4377   7345   7127   1362    499    398       N  
ATOM   1601  CA  GLY A 207      56.784  29.973  58.561  1.00 45.53           C  
ANISOU 1601  CA  GLY A 207     3827   6871   6600   1396    507    620       C  
ATOM   1602  C   GLY A 207      55.520  29.888  59.426  1.00 52.19           C  
ANISOU 1602  C   GLY A 207     4678   7792   7359   1308    460    578       C  
ATOM   1603  O   GLY A 207      54.776  30.858  59.584  1.00 51.58           O  
ANISOU 1603  O   GLY A 207     4539   7803   7256   1342    511    773       O  
ATOM   1604  N   TYR A 208      55.262  28.732  60.015  1.00 45.59           N  
ANISOU 1604  N   TYR A 208     3913   6906   6505   1201    387    343       N  
ATOM   1605  CA  TYR A 208      54.013  28.575  60.711  1.00 34.77           C  
ANISOU 1605  CA  TYR A 208     2529   5651   5030   1114    347    309       C  
ATOM   1606  C   TYR A 208      53.806  29.554  61.853  1.00 47.73           C  
ANISOU 1606  C   TYR A 208     4278   7041   6816   1132    340    430       C  
ATOM   1607  O   TYR A 208      52.718  30.089  62.016  1.00 50.77           O  
ANISOU 1607  O   TYR A 208     4589   7586   7114   1132    383    558       O  
ATOM   1608  CB  TYR A 208      53.791  27.131  61.104  1.00 25.56           C  
ANISOU 1608  CB  TYR A 208     1426   4467   3818    976    288     38       C  
ATOM   1609  CG  TYR A 208      53.173  26.425  59.967  1.00 39.07           C  
ANISOU 1609  CG  TYR A 208     3069   6558   5216    836    332    -50       C  
ATOM   1610  CD1 TYR A 208      51.793  26.260  59.890  1.00 42.04           C  
ANISOU 1610  CD1 TYR A 208     3380   7262   5332    697    309    -36       C  
ATOM   1611  CD2 TYR A 208      53.953  25.992  58.909  1.00 41.53           C  
ANISOU 1611  CD2 TYR A 208     3368   6935   5477    832    408   -130       C  
ATOM   1612  CE1 TYR A 208      51.209  25.627  58.789  1.00 37.89           C  
ANISOU 1612  CE1 TYR A 208     2776   7144   4475    522    344   -119       C  
ATOM   1613  CE2 TYR A 208      53.386  25.368  57.812  1.00 45.66           C  
ANISOU 1613  CE2 TYR A 208     3833   7844   5673    662    464   -235       C  
ATOM   1614  CZ  TYR A 208      52.017  25.192  57.754  1.00 41.97           C  
ANISOU 1614  CZ  TYR A 208     3297   7726   4925    494    424   -233       C  
ATOM   1615  OH  TYR A 208      51.485  24.572  56.655  1.00 50.65           O  
ANISOU 1615  OH  TYR A 208     4332   9241   5670    282    473   -347       O  
ATOM   1616  N   LEU A 209      54.851  29.791  62.632  1.00 45.78           N  
ANISOU 1616  N   LEU A 209     4182   6420   6792   1132    305    396       N  
ATOM   1617  CA  LEU A 209      54.819  30.810  63.675  1.00 35.71           C  
ANISOU 1617  CA  LEU A 209     2980   4918   5671   1124    333    481       C  
ATOM   1618  C   LEU A 209      54.507  32.185  63.081  1.00 42.41           C  
ANISOU 1618  C   LEU A 209     3708   5870   6536   1224    489    740       C  
ATOM   1619  O   LEU A 209      53.690  32.935  63.624  1.00 48.23           O  
ANISOU 1619  O   LEU A 209     4423   6594   7310   1234    575    845       O  
ATOM   1620  CB  LEU A 209      56.165  30.875  64.394  1.00 38.10           C  
ANISOU 1620  CB  LEU A 209     3403   4882   6191   1081    273    419       C  
ATOM   1621  CG  LEU A 209      56.523  30.147  65.691  1.00 38.69           C  
ANISOU 1621  CG  LEU A 209     3608   4732   6362    974    139    259       C  
ATOM   1622  CD1 LEU A 209      55.919  28.766  65.859  1.00 27.98           C  
ANISOU 1622  CD1 LEU A 209     2281   3462   4889    927     52    101       C  
ATOM   1623  CD2 LEU A 209      58.033  30.069  65.732  1.00 28.81           C  
ANISOU 1623  CD2 LEU A 209     2392   3276   5280    957     94    272       C  
ATOM   1624  N   GLU A 210      55.157  32.535  61.970  1.00 28.90           N  
ANISOU 1624  N   GLU A 210     1910   4251   4821   1311    549    863       N  
ATOM   1625  CA  GLU A 210      54.970  33.882  61.455  1.00 38.09           C  
ANISOU 1625  CA  GLU A 210     2950   5477   6044   1418    713   1143       C  
ATOM   1626  C   GLU A 210      53.542  33.999  60.969  1.00 41.22           C  
ANISOU 1626  C   GLU A 210     3186   6232   6244   1460    777   1308       C  
ATOM   1627  O   GLU A 210      52.990  35.086  60.907  1.00 48.58           O  
ANISOU 1627  O   GLU A 210     4015   7197   7248   1541    930   1567       O  
ATOM   1628  CB  GLU A 210      56.027  34.316  60.420  1.00 26.71           C  
ANISOU 1628  CB  GLU A 210     1445   4043   4659   1508    769   1267       C  
ATOM   1629  CG  GLU A 210      56.893  33.215  59.887  1.00 39.63           C  
ANISOU 1629  CG  GLU A 210     3131   5694   6231   1486    660   1095       C  
ATOM   1630  CD  GLU A 210      58.044  32.852  60.778  1.00 49.86           C  
ANISOU 1630  CD  GLU A 210     4592   6627   7726   1400    572    933       C  
ATOM   1631  OE1 GLU A 210      57.984  31.764  61.408  1.00 60.79           O  
ANISOU 1631  OE1 GLU A 210     6074   7943   9082   1311    456    728       O  
ATOM   1632  OE2 GLU A 210      59.016  33.636  60.827  1.00 50.43           O  
ANISOU 1632  OE2 GLU A 210     4672   6503   7986   1417    622   1030       O  
ATOM   1633  N   ARG A 211      52.939  32.837  60.742  1.00 42.62           N  
ANISOU 1633  N   ARG A 211     3335   6660   6198   1388    666   1157       N  
ATOM   1634  CA  ARG A 211      51.562  32.674  60.286  1.00 41.24           C  
ANISOU 1634  CA  ARG A 211     2983   6897   5789   1373    687   1282       C  
ATOM   1635  C   ARG A 211      50.537  32.781  61.412  1.00 50.25           C  
ANISOU 1635  C   ARG A 211     4181   7943   6967   1319    699   1286       C  
ATOM   1636  O   ARG A 211      49.343  32.808  61.147  1.00 65.41           O  
ANISOU 1636  O   ARG A 211     5947  10180   8725   1309    734   1449       O  
ATOM   1637  CB  ARG A 211      51.446  31.288  59.638  1.00 45.02           C  
ANISOU 1637  CB  ARG A 211     3403   7673   6030   1265    572   1058       C  
ATOM   1638  CG  ARG A 211      50.370  31.085  58.587  1.00 54.40           C  
ANISOU 1638  CG  ARG A 211     4323   9436   6909   1216    593   1200       C  
ATOM   1639  CD  ARG A 211      50.870  30.059  57.544  1.00 62.22           C  
ANISOU 1639  CD  ARG A 211     5225  10695   7722   1126    553    990       C  
ATOM   1640  NE  ARG A 211      49.871  29.119  57.019  1.00 54.33           N  
ANISOU 1640  NE  ARG A 211     4048  10182   6413    916    526    882       N  
ATOM   1641  CZ  ARG A 211      48.561  29.338  56.962  1.00 64.23           C  
ANISOU 1641  CZ  ARG A 211     5135  11795   7474    838    527   1081       C  
ATOM   1642  NH1 ARG A 211      47.762  28.404  56.460  1.00 72.26           N  
ANISOU 1642  NH1 ARG A 211     6084  13217   8153    579    476    956       N  
ATOM   1643  NH2 ARG A 211      48.043  30.485  57.391  1.00 69.48           N  
ANISOU 1643  NH2 ARG A 211     5780  12373   8248    988    581   1414       N  
ATOM   1644  N   THR A 212      50.984  32.798  62.668  1.00 47.90           N  
ANISOU 1644  N   THR A 212     4088   7242   6871   1273    666   1116       N  
ATOM   1645  CA  THR A 212      50.043  32.859  63.794  1.00 48.44           C  
ANISOU 1645  CA  THR A 212     4218   7211   6977   1222    685   1096       C  
ATOM   1646  C   THR A 212      50.011  34.222  64.499  1.00 48.49           C  
ANISOU 1646  C   THR A 212     4251   6942   7231   1291    869   1260       C  
ATOM   1647  O   THR A 212      50.969  34.975  64.473  1.00 49.82           O  
ANISOU 1647  O   THR A 212     4451   6893   7587   1336    942   1293       O  
ATOM   1648  CB  THR A 212      50.216  31.678  64.782  1.00 45.30           C  
ANISOU 1648  CB  THR A 212     3992   6648   6572   1095    514    775       C  
ATOM   1649  OG1 THR A 212      50.287  32.165  66.124  1.00 47.45           O  
ANISOU 1649  OG1 THR A 212     4402   6593   7034   1070    546    716       O  
ATOM   1650  CG2 THR A 212      51.459  30.936  64.496  1.00 40.13           C  
ANISOU 1650  CG2 THR A 212     3415   5885   5947   1067    400    587       C  
ATOM   1651  N   THR A 213      48.881  34.566  65.095  1.00 52.62           N  
ANISOU 1651  N   THR A 213     4746   7478   7770   1298    973   1373       N  
ATOM   1652  CA  THR A 213      48.726  35.939  65.576  1.00 62.20           C  
ANISOU 1652  CA  THR A 213     5943   8453   9237   1381   1220   1566       C  
ATOM   1653  C   THR A 213      49.710  36.282  66.682  1.00 59.72           C  
ANISOU 1653  C   THR A 213     5808   7725   9157   1316   1233   1334       C  
ATOM   1654  O   THR A 213      50.063  35.426  67.503  1.00 58.38           O  
ANISOU 1654  O   THR A 213     5788   7447   8947   1202   1055   1048       O  
ATOM   1655  CB  THR A 213      47.307  36.219  66.099  1.00 53.49           C  
ANISOU 1655  CB  THR A 213     4786   7403   8135   1405   1362   1734       C  
ATOM   1656  OG1 THR A 213      47.217  35.850  67.484  1.00 53.07           O  
ANISOU 1656  OG1 THR A 213     4920   7098   8148   1301   1321   1467       O  
ATOM   1657  CG2 THR A 213      46.334  35.431  65.328  1.00 49.42           C  
ANISOU 1657  CG2 THR A 213     4120   7326   7330   1391   1252   1855       C  
ATOM   1658  N   GLY A 214      50.122  37.548  66.712  1.00 54.37           N  
ANISOU 1658  N   GLY A 214     5094   6833   8730   1385   1455   1473       N  
ATOM   1659  CA  GLY A 214      50.913  38.075  67.810  1.00 51.12           C  
ANISOU 1659  CA  GLY A 214     4815   6054   8554   1311   1522   1271       C  
ATOM   1660  C   GLY A 214      50.309  37.760  69.169  1.00 43.54           C  
ANISOU 1660  C   GLY A 214     3991   4957   7597   1219   1525   1069       C  
ATOM   1661  O   GLY A 214      50.936  37.170  70.045  1.00 40.22           O  
ANISOU 1661  O   GLY A 214     3712   4407   7164   1108   1356    788       O  
ATOM   1662  N   PRO A 215      49.071  38.165  69.368  1.00 39.38           N  
ANISOU 1662  N   PRO A 215     3416   4458   7090   1274   1727   1236       N  
ATOM   1663  CA  PRO A 215      48.500  37.872  70.677  1.00 38.46           C  
ANISOU 1663  CA  PRO A 215     3443   4202   6969   1187   1751   1037       C  
ATOM   1664  C   PRO A 215      48.638  36.427  71.128  1.00 46.63           C  
ANISOU 1664  C   PRO A 215     4589   5347   7781   1081   1415    777       C  
ATOM   1665  O   PRO A 215      49.002  36.237  72.279  1.00 58.60           O  
ANISOU 1665  O   PRO A 215     6295   6651   9318    960   1353    533       O  
ATOM   1666  CB  PRO A 215      47.052  38.281  70.499  1.00 34.20           C  
ANISOU 1666  CB  PRO A 215     2800   3766   6430   1279   1977   1327       C  
ATOM   1667  CG  PRO A 215      47.156  39.476  69.597  1.00 38.27           C  
ANISOU 1667  CG  PRO A 215     3153   4248   7140   1419   2229   1652       C  
ATOM   1668  CD  PRO A 215      48.279  39.162  68.630  1.00 47.80           C  
ANISOU 1668  CD  PRO A 215     4308   5589   8263   1423   2009   1622       C  
ATOM   1669  N   ARG A 216      48.368  35.430  70.292  1.00 52.07           N  
ANISOU 1669  N   ARG A 216     5204   6334   8245   1087   1204    828       N  
ATOM   1670  CA  ARG A 216      48.476  34.055  70.803  1.00 57.63           C  
ANISOU 1670  CA  ARG A 216     6015   7092   8788    987    927    583       C  
ATOM   1671  C   ARG A 216      49.925  33.649  71.106  1.00 53.60           C  
ANISOU 1671  C   ARG A 216     5624   6413   8328    907    736    373       C  
ATOM   1672  O   ARG A 216      50.191  32.989  72.100  1.00 51.24           O  
ANISOU 1672  O   ARG A 216     5521   5983   7964    749    573    186       O  
ATOM   1673  CB  ARG A 216      47.831  33.031  69.876  1.00 57.31           C  
ANISOU 1673  CB  ARG A 216     5872   7396   8507    984    779    647       C  
ATOM   1674  CG  ARG A 216      46.637  33.516  69.097  1.00 57.45           C  
ANISOU 1674  CG  ARG A 216     5717   7668   8445   1064    939    951       C  
ATOM   1675  CD  ARG A 216      45.991  32.347  68.404  1.00 59.63           C  
ANISOU 1675  CD  ARG A 216     5902   8299   8455   1009    768    942       C  
ATOM   1676  NE  ARG A 216      45.838  31.235  69.341  1.00 68.51           N  
ANISOU 1676  NE  ARG A 216     7190   9340   9502    880    591    688       N  
ATOM   1677  CZ  ARG A 216      45.939  29.951  69.005  1.00 72.80           C  
ANISOU 1677  CZ  ARG A 216     7780  10021   9861    767    385    523       C  
ATOM   1678  NH1 ARG A 216      45.778  29.012  69.943  1.00 54.34           N  
ANISOU 1678  NH1 ARG A 216     5640   7548   7458    635    240    328       N  
ATOM   1679  NH2 ARG A 216      46.203  29.611  67.736  1.00 72.67           N  
ANISOU 1679  NH2 ARG A 216     7610  10272   9731    781    347    553       N  
ATOM   1680  N   LEU A 217      50.846  34.035  70.229  1.00 54.42           N  
ANISOU 1680  N   LEU A 217     5647   6527   8503    960    744    449       N  
ATOM   1681  CA  LEU A 217      52.277  33.874  70.472  1.00 53.02           C  
ANISOU 1681  CA  LEU A 217     5542   6180   8423    906    607    313       C  
ATOM   1682  C   LEU A 217      52.726  34.521  71.793  1.00 50.47           C  
ANISOU 1682  C   LEU A 217     5360   5564   8251    811    660    181       C  
ATOM   1683  O   LEU A 217      53.419  33.903  72.601  1.00 52.40           O  
ANISOU 1683  O   LEU A 217     5755   5704   8449    649    465     28       O  
ATOM   1684  CB  LEU A 217      53.065  34.459  69.299  1.00 42.73           C  
ANISOU 1684  CB  LEU A 217     4133   4920   7182    973    670    462       C  
ATOM   1685  CG  LEU A 217      53.592  33.436  68.290  1.00 43.43           C  
ANISOU 1685  CG  LEU A 217     4195   5179   7126    977    503    448       C  
ATOM   1686  CD1 LEU A 217      52.939  32.055  68.413  1.00 39.30           C  
ANISOU 1686  CD1 LEU A 217     3714   4804   6413    926    347    322       C  
ATOM   1687  CD2 LEU A 217      53.454  33.980  66.904  1.00 34.99           C  
ANISOU 1687  CD2 LEU A 217     2987   4298   6008   1086    626    663       C  
ATOM   1688  N   ARG A 218      52.320  35.760  72.018  1.00 53.88           N  
ANISOU 1688  N   ARG A 218     5130   6064   9278    796     46  -2436       N  
ATOM   1689  CA  ARG A 218      52.681  36.450  73.250  1.00 51.90           C  
ANISOU 1689  CA  ARG A 218     4959   5783   8977    614    244  -2314       C  
ATOM   1690  C   ARG A 218      52.265  35.700  74.487  1.00 50.39           C  
ANISOU 1690  C   ARG A 218     4651   5566   8930    367    478  -2392       C  
ATOM   1691  O   ARG A 218      53.010  35.653  75.454  1.00 50.35           O  
ANISOU 1691  O   ARG A 218     4768   5567   8797    181    645  -2218       O  
ATOM   1692  CB  ARG A 218      52.037  37.831  73.313  1.00 47.31           C  
ANISOU 1692  CB  ARG A 218     4356   5154   8466    720    183  -2411       C  
ATOM   1693  CG  ARG A 218      52.278  38.511  74.616  1.00 43.42           C  
ANISOU 1693  CG  ARG A 218     3907   4637   7952    534    389  -2349       C  
ATOM   1694  CD  ARG A 218      52.073  39.993  74.473  1.00 56.04           C  
ANISOU 1694  CD  ARG A 218     5542   6179   9573    666    294  -2370       C  
ATOM   1695  NE  ARG A 218      52.202  40.699  75.743  1.00 57.46           N  
ANISOU 1695  NE  ARG A 218     5733   6339   9761    495    485  -2368       N  
ATOM   1696  CZ  ARG A 218      52.341  42.012  75.822  1.00 61.50           C  
ANISOU 1696  CZ  ARG A 218     6301   6791  10275    566    441  -2339       C  
ATOM   1697  NH1 ARG A 218      52.449  42.605  76.998  1.00 60.62           N  
ANISOU 1697  NH1 ARG A 218     6184   6673  10177    411    613  -2372       N  
ATOM   1698  NH2 ARG A 218      52.381  42.726  74.704  1.00 70.52           N  
ANISOU 1698  NH2 ARG A 218     7517   7875  11401    797    219  -2275       N  
ATOM   1699  N   GLN A 219      51.049  35.164  74.472  1.00 55.95           N  
ANISOU 1699  N   GLN A 219     5121   6234   9903    367    492  -2663       N  
ATOM   1700  CA  GLN A 219      50.515  34.481  75.637  1.00 56.32           C  
ANISOU 1700  CA  GLN A 219     5052   6242  10104    120    752  -2749       C  
ATOM   1701  C   GLN A 219      51.302  33.216  75.907  1.00 52.83           C  
ANISOU 1701  C   GLN A 219     4694   5799   9581    -32    843  -2563       C  
ATOM   1702  O   GLN A 219      51.632  32.900  77.046  1.00 53.66           O  
ANISOU 1702  O   GLN A 219     4886   5889   9612   -257   1057  -2432       O  
ATOM   1703  CB  GLN A 219      49.051  34.114  75.443  1.00 50.00           C  
ANISOU 1703  CB  GLN A 219     3954   5385   9658    155    752  -3103       C  
ATOM   1704  CG  GLN A 219      48.498  33.332  76.618  1.00 62.89           C  
ANISOU 1704  CG  GLN A 219     5473   6965  11456   -123   1066  -3182       C  
ATOM   1705  CD  GLN A 219      47.087  32.819  76.394  1.00 90.00           C  
ANISOU 1705  CD  GLN A 219     8578  10324  15293   -108   1092  -3552       C  
ATOM   1706  OE1 GLN A 219      46.779  31.673  76.730  1.00104.17           O  
ANISOU 1706  OE1 GLN A 219    10264  12057  17260   -272   1260  -3600       O  
ATOM   1707  NE2 GLN A 219      46.221  33.662  75.828  1.00 88.50           N  
ANISOU 1707  NE2 GLN A 219     8222  10120  15284     89    921  -3821       N  
ATOM   1708  N   GLU A 220      51.589  32.485  74.845  1.00 48.50           N  
ANISOU 1708  N   GLU A 220     4121   5262   9044    100    667  -2561       N  
ATOM   1709  CA  GLU A 220      52.285  31.233  74.988  1.00 51.35           C  
ANISOU 1709  CA  GLU A 220     4526   5599   9384    -21    721  -2418       C  
ATOM   1710  C   GLU A 220      53.687  31.513  75.497  1.00 49.45           C  
ANISOU 1710  C   GLU A 220     4543   5390   8854   -104    761  -2105       C  
ATOM   1711  O   GLU A 220      54.253  30.722  76.253  1.00 51.47           O  
ANISOU 1711  O   GLU A 220     4877   5606   9074   -281    877  -1949       O  
ATOM   1712  CB  GLU A 220      52.232  30.429  73.684  1.00 46.21           C  
ANISOU 1712  CB  GLU A 220     3764   4961   8834    155    514  -2538       C  
ATOM   1713  CG  GLU A 220      51.063  29.446  73.679  1.00 59.70           C  
ANISOU 1713  CG  GLU A 220     5198   6587  10900    107    565  -2809       C  
ATOM   1714  CD  GLU A 220      51.186  28.430  74.824  1.00 80.03           C  
ANISOU 1714  CD  GLU A 220     7776   9061  13571   -176    817  -2691       C  
ATOM   1715  OE1 GLU A 220      52.345  28.173  75.242  1.00 94.50           O  
ANISOU 1715  OE1 GLU A 220     9814  10898  15195   -272    854  -2410       O  
ATOM   1716  OE2 GLU A 220      50.154  27.894  75.307  1.00 68.42           O  
ANISOU 1716  OE2 GLU A 220     6110   7498  12387   -302    979  -2875       O  
ATOM   1717  N   LEU A 221      54.189  32.686  75.126  1.00 40.70           N  
ANISOU 1717  N   LEU A 221     3561   4339   7563     24    662  -2025       N  
ATOM   1718  CA  LEU A 221      55.499  33.187  75.532  1.00 44.11           C  
ANISOU 1718  CA  LEU A 221     4213   4796   7751    -31    686  -1768       C  
ATOM   1719  C   LEU A 221      55.546  33.559  76.996  1.00 40.35           C  
ANISOU 1719  C   LEU A 221     3815   4304   7214   -232    879  -1695       C  
ATOM   1720  O   LEU A 221      56.515  33.285  77.683  1.00 51.66           O  
ANISOU 1720  O   LEU A 221     5391   5730   8506   -355    933  -1503       O  
ATOM   1721  CB  LEU A 221      55.820  34.447  74.738  1.00 45.02           C  
ANISOU 1721  CB  LEU A 221     4417   4951   7738    156    554  -1733       C  
ATOM   1722  CG  LEU A 221      57.186  34.489  74.092  1.00 39.79           C  
ANISOU 1722  CG  LEU A 221     3912   4320   6888    220    473  -1535       C  
ATOM   1723  CD1 LEU A 221      57.737  33.079  74.020  1.00 45.76           C  
ANISOU 1723  CD1 LEU A 221     4642   5069   7676    144    472  -1487       C  
ATOM   1724  CD2 LEU A 221      57.054  35.075  72.717  1.00 41.10           C  
ANISOU 1724  CD2 LEU A 221     4097   4524   6994    455    305  -1578       C  
ATOM   1725  N   GLU A 222      54.491  34.217  77.449  1.00 41.48           N  
ANISOU 1725  N   GLU A 222     3858   4441   7462   -254    969  -1869       N  
ATOM   1726  CA  GLU A 222      54.369  34.655  78.825  1.00 52.78           C  
ANISOU 1726  CA  GLU A 222     5348   5877   8829   -439   1169  -1852       C  
ATOM   1727  C   GLU A 222      54.271  33.470  79.764  1.00 53.68           C  
ANISOU 1727  C   GLU A 222     5479   5959   8958   -661   1350  -1794       C  
ATOM   1728  O   GLU A 222      54.897  33.448  80.820  1.00 61.57           O  
ANISOU 1728  O   GLU A 222     6644   6972   9776   -816   1459  -1635       O  
ATOM   1729  CB  GLU A 222      53.157  35.574  78.961  1.00 50.03           C  
ANISOU 1729  CB  GLU A 222     4846   5525   8640   -398   1223  -2104       C  
ATOM   1730  CG  GLU A 222      53.388  36.915  78.292  1.00 46.15           C  
ANISOU 1730  CG  GLU A 222     4392   5040   8101   -203   1057  -2107       C  
ATOM   1731  CD  GLU A 222      52.232  37.861  78.447  1.00 70.81           C  
ANISOU 1731  CD  GLU A 222     7356   8138  11410   -150   1082  -2363       C  
ATOM   1732  OE1 GLU A 222      51.127  37.395  78.787  1.00 87.53           O  
ANISOU 1732  OE1 GLU A 222     9288  10236  13733   -228   1202  -2586       O  
ATOM   1733  OE2 GLU A 222      52.420  39.077  78.224  1.00 83.28           O  
ANISOU 1733  OE2 GLU A 222     8983   9701  12958    -31    985  -2353       O  
ATOM   1734  N   LYS A 223      53.494  32.483  79.345  1.00 42.25           N  
ANISOU 1734  N   LYS A 223     3864   4459   7730   -667   1366  -1923       N  
ATOM   1735  CA  LYS A 223      53.305  31.239  80.068  1.00 37.41           C  
ANISOU 1735  CA  LYS A 223     3250   3779   7185   -869   1536  -1866       C  
ATOM   1736  C   LYS A 223      54.641  30.510  80.259  1.00 51.63           C  
ANISOU 1736  C   LYS A 223     5250   5558   8808   -923   1464  -1578       C  
ATOM   1737  O   LYS A 223      54.842  29.851  81.282  1.00 64.49           O  
ANISOU 1737  O   LYS A 223     7000   7142  10362  -1117   1609  -1431       O  
ATOM   1738  CB  LYS A 223      52.274  30.362  79.318  1.00 34.14           C  
ANISOU 1738  CB  LYS A 223     2579   3293   7099   -823   1522  -2090       C  
ATOM   1739  CG  LYS A 223      51.473  29.420  80.182  1.00 36.32           C  
ANISOU 1739  CG  LYS A 223     2772   3478   7550  -1053   1787  -2145       C  
ATOM   1740  CD  LYS A 223      50.208  30.076  80.763  1.00 65.14           C  
ANISOU 1740  CD  LYS A 223     6269   7136  11346  -1136   2001  -2401       C  
ATOM   1741  CE  LYS A 223      48.936  29.745  79.959  1.00 65.80           C  
ANISOU 1741  CE  LYS A 223     6016   7153  11831  -1044   1972  -2749       C  
ATOM   1742  NZ  LYS A 223      48.627  28.267  79.928  1.00 67.83           N  
ANISOU 1742  NZ  LYS A 223     6160   7283  12331  -1166   2072  -2760       N  
ATOM   1743  N   ILE A 224      55.546  30.615  79.280  1.00 50.66           N  
ANISOU 1743  N   ILE A 224     5166   5462   8621   -752   1242  -1501       N  
ATOM   1744  CA  ILE A 224      56.902  30.057  79.411  1.00 47.97           C  
ANISOU 1744  CA  ILE A 224     4991   5097   8137   -783   1152  -1260       C  
ATOM   1745  C   ILE A 224      57.666  30.811  80.479  1.00 48.26           C  
ANISOU 1745  C   ILE A 224     5236   5174   7925   -876   1205  -1099       C  
ATOM   1746  O   ILE A 224      58.401  30.237  81.273  1.00 52.21           O  
ANISOU 1746  O   ILE A 224     5889   5634   8315   -996   1218   -915       O  
ATOM   1747  CB  ILE A 224      57.730  30.158  78.100  1.00 34.19           C  
ANISOU 1747  CB  ILE A 224     3231   3385   6373   -582    933  -1244       C  
ATOM   1748  CG1 ILE A 224      57.424  28.994  77.156  1.00 36.38           C  
ANISOU 1748  CG1 ILE A 224     3347   3615   6859   -513    846  -1350       C  
ATOM   1749  CG2 ILE A 224      59.259  30.152  78.387  1.00 26.51           C  
ANISOU 1749  CG2 ILE A 224     2440   2409   5225   -606    854  -1021       C  
ATOM   1750  CD1 ILE A 224      57.675  29.315  75.671  1.00 28.75           C  
ANISOU 1750  CD1 ILE A 224     2320   2722   5882   -282    661  -1443       C  
ATOM   1751  N   LEU A 225      57.499  32.118  80.473  1.00 48.25           N  
ANISOU 1751  N   LEU A 225     5239   5243   7850   -806   1212  -1179       N  
ATOM   1752  CA  LEU A 225      58.157  32.948  81.445  1.00 49.37           C  
ANISOU 1752  CA  LEU A 225     5549   5428   7782   -878   1255  -1077       C  
ATOM   1753  C   LEU A 225      57.588  32.766  82.861  1.00 51.30           C  
ANISOU 1753  C   LEU A 225     5868   5681   7943  -1087   1469  -1076       C  
ATOM   1754  O   LEU A 225      58.233  33.133  83.834  1.00 55.20           O  
ANISOU 1754  O   LEU A 225     6535   6210   8229  -1173   1496   -967       O  
ATOM   1755  CB  LEU A 225      58.098  34.401  80.993  1.00 45.14           C  
ANISOU 1755  CB  LEU A 225     4978   4942   7231   -742   1203  -1176       C  
ATOM   1756  CG  LEU A 225      58.761  34.658  79.632  1.00 47.61           C  
ANISOU 1756  CG  LEU A 225     5269   5251   7571   -547   1017  -1140       C  
ATOM   1757  CD1 LEU A 225      58.396  36.033  79.130  1.00 53.91           C  
ANISOU 1757  CD1 LEU A 225     6024   6068   8392   -411    981  -1243       C  
ATOM   1758  CD2 LEU A 225      60.294  34.488  79.642  1.00 37.43           C  
ANISOU 1758  CD2 LEU A 225     4117   3947   6157   -550    921   -947       C  
ATOM   1759  N   GLU A 226      56.398  32.184  82.990  1.00 48.03           N  
ANISOU 1759  N   GLU A 226     5328   5235   7687  -1174   1628  -1204       N  
ATOM   1760  CA  GLU A 226      55.875  31.871  84.330  1.00 53.83           C  
ANISOU 1760  CA  GLU A 226     6154   5972   8327  -1398   1874  -1183       C  
ATOM   1761  C   GLU A 226      56.292  30.485  84.814  1.00 52.68           C  
ANISOU 1761  C   GLU A 226     6143   5737   8136  -1535   1902   -966       C  
ATOM   1762  O   GLU A 226      55.737  30.000  85.779  1.00 43.74           O  
ANISOU 1762  O   GLU A 226     5085   4581   6952  -1728   2125   -932       O  
ATOM   1763  CB  GLU A 226      54.343  31.926  84.412  1.00 51.92           C  
ANISOU 1763  CB  GLU A 226     5708   5723   8295  -1467   2092  -1439       C  
ATOM   1764  CG  GLU A 226      53.643  33.151  83.857  1.00 73.17           C  
ANISOU 1764  CG  GLU A 226     8217   8467  11119  -1324   2059  -1699       C  
ATOM   1765  CD  GLU A 226      52.198  32.837  83.430  1.00 90.49           C  
ANISOU 1765  CD  GLU A 226    10134  10607  13640  -1325   2172  -1975       C  
ATOM   1766  OE1 GLU A 226      51.683  33.514  82.508  1.00 98.20           O  
ANISOU 1766  OE1 GLU A 226    10929  11585  14796  -1138   2035  -2176       O  
ATOM   1767  OE2 GLU A 226      51.589  31.896  84.001  1.00 89.24           O  
ANISOU 1767  OE2 GLU A 226     9942  10392  13572  -1509   2391  -1991       O  
ATOM   1768  N   GLU A 227      57.233  29.831  84.142  1.00 49.60           N  
ANISOU 1768  N   GLU A 227     5781   5284   7779  -1441   1687   -824       N  
ATOM   1769  CA  GLU A 227      57.614  28.476  84.520  1.00 38.89           C  
ANISOU 1769  CA  GLU A 227     4531   3811   6434  -1552   1682   -626       C  
ATOM   1770  C   GLU A 227      58.710  28.542  85.545  1.00 51.62           C  
ANISOU 1770  C   GLU A 227     6425   5437   7751  -1622   1615   -394       C  
ATOM   1771  O   GLU A 227      59.205  29.633  85.838  1.00 52.82           O  
ANISOU 1771  O   GLU A 227     6657   5693   7718  -1571   1563   -413       O  
ATOM   1772  CB  GLU A 227      58.112  27.713  83.307  1.00 35.75           C  
ANISOU 1772  CB  GLU A 227     4007   3334   6241  -1411   1471   -618       C  
ATOM   1773  CG  GLU A 227      57.028  27.296  82.350  1.00 45.33           C  
ANISOU 1773  CG  GLU A 227     4952   4509   7761  -1353   1514   -838       C  
ATOM   1774  CD  GLU A 227      56.343  26.000  82.755  1.00 56.39           C  
ANISOU 1774  CD  GLU A 227     6308   5766   9353  -1518   1670   -808       C  
ATOM   1775  OE1 GLU A 227      55.101  25.959  82.660  1.00 43.25           O  
ANISOU 1775  OE1 GLU A 227     4460   4085   7887  -1566   1842  -1012       O  
ATOM   1776  OE2 GLU A 227      57.040  25.033  83.153  1.00 66.28           O  
ANISOU 1776  OE2 GLU A 227     7696   6905  10583  -1597   1617   -590       O  
ATOM   1777  N   LYS A 228      59.133  27.410  86.072  1.00 56.31           N  
ANISOU 1777  N   LYS A 228     7164   5913   8318  -1727   1594   -182       N  
ATOM   1778  CA  LYS A 228      60.214  27.408  87.031  1.00 44.59           C  
ANISOU 1778  CA  LYS A 228     5965   4423   6554  -1779   1481     49       C  
ATOM   1779  C   LYS A 228      61.532  27.834  86.494  1.00 49.14           C  
ANISOU 1779  C   LYS A 228     6528   5034   7108  -1600   1203     53       C  
ATOM   1780  O   LYS A 228      62.167  28.697  87.042  1.00 61.30           O  
ANISOU 1780  O   LYS A 228     8172   6676   8443  -1573   1159     41       O  
ATOM   1781  CB  LYS A 228      60.415  26.017  87.553  1.00 47.31           C  
ANISOU 1781  CB  LYS A 228     6455   4596   6926  -1889   1453    287       C  
ATOM   1782  CG  LYS A 228      60.103  25.884  88.973  1.00 57.10           C  
ANISOU 1782  CG  LYS A 228     8036   5837   7822  -2042   1511    510       C  
ATOM   1783  CD  LYS A 228      60.694  24.640  89.523  1.00 74.67           C  
ANISOU 1783  CD  LYS A 228    10443   7878  10050  -2061   1309    788       C  
ATOM   1784  CE  LYS A 228      62.164  24.738  89.645  1.00 92.58           C  
ANISOU 1784  CE  LYS A 228    13085  10130  11960  -2230   1395   1036       C  
ATOM   1785  NZ  LYS A 228      62.641  23.754  90.645  1.00 96.68           N  
ANISOU 1785  NZ  LYS A 228    13811  10446  12478  -2241   1170   1330       N  
ATOM   1786  N   ASN A 229      61.932  27.255  85.385  1.00 45.29           N  
ANISOU 1786  N   ASN A 229     5898   4462   6849  -1483   1034     46       N  
ATOM   1787  CA  ASN A 229      63.153  27.704  84.713  1.00 54.83           C  
ANISOU 1787  CA  ASN A 229     7071   5690   8072  -1324    801     36       C  
ATOM   1788  C   ASN A 229      62.992  28.108  83.242  1.00 57.30           C  
ANISOU 1788  C   ASN A 229     7146   6049   8577  -1164    764   -148       C  
ATOM   1789  O   ASN A 229      63.352  27.348  82.344  1.00 52.79           O  
ANISOU 1789  O   ASN A 229     6459   5407   8190  -1086    648   -161       O  
ATOM   1790  CB  ASN A 229      64.229  26.636  84.835  1.00 60.21           C  
ANISOU 1790  CB  ASN A 229     7837   6232   8807  -1318    591    208       C  
ATOM   1791  CG  ASN A 229      64.480  26.245  86.266  1.00 71.84           C  
ANISOU 1791  CG  ASN A 229     9585   7653  10057  -1452    582    416       C  
ATOM   1792  OD1 ASN A 229      64.334  25.074  86.643  1.00 82.10           O  
ANISOU 1792  OD1 ASN A 229    10969   8810  11416  -1543    579    569       O  
ATOM   1793  ND2 ASN A 229      64.837  27.231  87.088  1.00 70.57           N  
ANISOU 1793  ND2 ASN A 229     9578   7603   9634  -1465    575    423       N  
ATOM   1794  N   PRO A 230      62.462  29.318  82.993  1.00 58.62           N  
ANISOU 1794  N   PRO A 230     7249   6332   8693  -1110    856   -292       N  
ATOM   1795  CA  PRO A 230      62.291  29.826  81.625  1.00 61.57           C  
ANISOU 1795  CA  PRO A 230     7442   6753   9198   -947    811   -445       C  
ATOM   1796  C   PRO A 230      63.535  29.758  80.725  1.00 57.57           C  
ANISOU 1796  C   PRO A 230     6906   6227   8740   -821    629   -412       C  
ATOM   1797  O   PRO A 230      63.373  29.459  79.541  1.00 58.48           O  
ANISOU 1797  O   PRO A 230     6880   6347   8992   -711    584   -506       O  
ATOM   1798  CB  PRO A 230      61.844  31.272  81.850  1.00 51.44           C  
ANISOU 1798  CB  PRO A 230     6167   5571   7807   -924    904   -546       C  
ATOM   1799  CG  PRO A 230      61.088  31.210  83.101  1.00 44.96           C  
ANISOU 1799  CG  PRO A 230     5432   4762   6887  -1089   1074   -536       C  
ATOM   1800  CD  PRO A 230      61.778  30.183  83.968  1.00 48.01           C  
ANISOU 1800  CD  PRO A 230     5988   5072   7183  -1205   1026   -337       C  
ATOM   1801  N   LEU A 231      64.729  30.016  81.258  1.00 53.17           N  
ANISOU 1801  N   LEU A 231     6469   5653   8081   -833    530   -305       N  
ATOM   1802  CA  LEU A 231      65.955  29.931  80.458  1.00 41.65           C  
ANISOU 1802  CA  LEU A 231     4962   4164   6698   -731    383   -296       C  
ATOM   1803  C   LEU A 231      66.036  28.602  79.700  1.00 49.22           C  
ANISOU 1803  C   LEU A 231     5810   5046   7845   -699    304   -310       C  
ATOM   1804  O   LEU A 231      66.427  28.581  78.540  1.00 46.77           O  
ANISOU 1804  O   LEU A 231     5387   4758   7627   -587    255   -394       O  
ATOM   1805  CB  LEU A 231      67.185  30.073  81.346  1.00 42.53           C  
ANISOU 1805  CB  LEU A 231     5203   4231   6727   -772    267   -191       C  
ATOM   1806  CG  LEU A 231      68.320  30.944  80.818  1.00 48.71           C  
ANISOU 1806  CG  LEU A 231     5948   5029   7530   -681    200   -235       C  
ATOM   1807  CD1 LEU A 231      69.674  30.330  81.172  1.00 33.25           C  
ANISOU 1807  CD1 LEU A 231     4019   2972   5644   -687     17   -173       C  
ATOM   1808  CD2 LEU A 231      68.181  31.153  79.313  1.00 58.92           C  
ANISOU 1808  CD2 LEU A 231     7099   6365   8924   -564    248   -335       C  
ATOM   1809  N   LYS A 232      65.664  27.501  80.365  1.00 45.81           N  
ANISOU 1809  N   LYS A 232     5416   4520   7470   -803    302   -229       N  
ATOM   1810  CA  LYS A 232      65.617  26.182  79.735  1.00 38.20           C  
ANISOU 1810  CA  LYS A 232     4331   3457   6725   -785    233   -254       C  
ATOM   1811  C   LYS A 232      64.849  26.242  78.431  1.00 45.73           C  
ANISOU 1811  C   LYS A 232     5098   4485   7791   -675    284   -442       C  
ATOM   1812  O   LYS A 232      65.338  25.798  77.394  1.00 45.70           O  
ANISOU 1812  O   LYS A 232     4974   4478   7912   -574    191   -528       O  
ATOM   1813  CB  LYS A 232      64.930  25.152  80.625  1.00 42.89           C  
ANISOU 1813  CB  LYS A 232     4988   3935   7374   -927    289   -148       C  
ATOM   1814  CG  LYS A 232      65.760  24.572  81.725  1.00 48.31           C  
ANISOU 1814  CG  LYS A 232     5857   4499   7998  -1016    174     56       C  
ATOM   1815  CD  LYS A 232      65.070  23.349  82.274  1.00 67.75           C  
ANISOU 1815  CD  LYS A 232     8357   6812  10573  -1142    232    163       C  
ATOM   1816  CE  LYS A 232      65.554  23.010  83.670  1.00 94.28           C  
ANISOU 1816  CE  LYS A 232    11984  10075  13763  -1257    169    407       C  
ATOM   1817  NZ  LYS A 232      64.577  22.130  84.387  1.00113.75           N  
ANISOU 1817  NZ  LYS A 232    14539  12424  16258  -1420    329    533       N  
ATOM   1818  N   SER A 233      63.629  26.774  78.497  1.00 41.81           N  
ANISOU 1818  N   SER A 233     4576   4057   7251   -691    423   -521       N  
ATOM   1819  CA  SER A 233      62.789  26.879  77.316  1.00 37.26           C  
ANISOU 1819  CA  SER A 233     3832   3551   6773   -571    441   -713       C  
ATOM   1820  C   SER A 233      63.327  27.877  76.267  1.00 36.21           C  
ANISOU 1820  C   SER A 233     3688   3531   6538   -412    386   -778       C  
ATOM   1821  O   SER A 233      63.332  27.603  75.064  1.00 34.33           O  
ANISOU 1821  O   SER A 233     3339   3335   6370   -285    320   -898       O  
ATOM   1822  CB  SER A 233      61.354  27.195  77.708  1.00 40.67           C  
ANISOU 1822  CB  SER A 233     4222   4008   7221   -627    590   -803       C  
ATOM   1823  OG  SER A 233      60.660  26.015  78.055  1.00 47.37           O  
ANISOU 1823  OG  SER A 233     4995   4746   8257   -733    649   -818       O  
ATOM   1824  N   ILE A 234      63.801  29.031  76.710  1.00 40.58           N  
ANISOU 1824  N   ILE A 234     4363   4131   6923   -419    418   -701       N  
ATOM   1825  CA  ILE A 234      64.366  29.975  75.759  1.00 41.99           C  
ANISOU 1825  CA  ILE A 234     4550   4388   7016   -287    390   -732       C  
ATOM   1826  C   ILE A 234      65.498  29.298  75.000  1.00 41.34           C  
ANISOU 1826  C   ILE A 234     4423   4284   7002   -234    298   -732       C  
ATOM   1827  O   ILE A 234      65.649  29.483  73.800  1.00 39.31           O  
ANISOU 1827  O   ILE A 234     4116   4095   6725   -110    280   -814       O  
ATOM   1828  CB  ILE A 234      64.920  31.218  76.443  1.00 35.85           C  
ANISOU 1828  CB  ILE A 234     3899   3626   6098   -322    435   -642       C  
ATOM   1829  CG1 ILE A 234      63.828  31.943  77.199  1.00 29.85           C  
ANISOU 1829  CG1 ILE A 234     3169   2892   5280   -373    534   -672       C  
ATOM   1830  CG2 ILE A 234      65.613  32.145  75.417  1.00 33.39           C  
ANISOU 1830  CG2 ILE A 234     3600   3362   5723   -200    428   -650       C  
ATOM   1831  CD1 ILE A 234      64.342  33.234  77.817  1.00 48.15           C  
ANISOU 1831  CD1 ILE A 234     5590   5225   7480   -395    571   -617       C  
ATOM   1832  N   ARG A 235      66.293  28.513  75.716  1.00 33.84           N  
ANISOU 1832  N   ARG A 235     3496   3236   6126   -327    235   -645       N  
ATOM   1833  CA  ARG A 235      67.444  27.860  75.117  1.00 34.10           C  
ANISOU 1833  CA  ARG A 235     3464   3228   6263   -287    142   -667       C  
ATOM   1834  C   ARG A 235      67.007  26.809  74.122  1.00 37.55           C  
ANISOU 1834  C   ARG A 235     3750   3672   6847   -216     99   -806       C  
ATOM   1835  O   ARG A 235      67.570  26.672  73.030  1.00 35.40           O  
ANISOU 1835  O   ARG A 235     3399   3450   6602   -120     72   -907       O  
ATOM   1836  CB  ARG A 235      68.316  27.246  76.198  1.00 28.53           C  
ANISOU 1836  CB  ARG A 235     2817   2395   5628   -391     47   -550       C  
ATOM   1837  CG  ARG A 235      69.383  28.221  76.664  1.00 27.77           C  
ANISOU 1837  CG  ARG A 235     2812   2301   5438   -404     35   -485       C  
ATOM   1838  CD  ARG A 235      70.015  27.860  77.967  1.00 31.97           C  
ANISOU 1838  CD  ARG A 235     3445   2723   5980   -499    -76   -365       C  
ATOM   1839  NE  ARG A 235      71.153  28.738  78.150  1.00 48.82           N  
ANISOU 1839  NE  ARG A 235     5610   4857   8084   -483   -109   -364       N  
ATOM   1840  CZ  ARG A 235      71.863  28.860  79.262  1.00 50.42           C  
ANISOU 1840  CZ  ARG A 235     5910   4990   8256   -539   -218   -288       C  
ATOM   1841  NH1 ARG A 235      72.873  29.710  79.283  1.00 50.83           N  
ANISOU 1841  NH1 ARG A 235     5949   5039   8324   -514   -239   -331       N  
ATOM   1842  NH2 ARG A 235      71.572  28.146  80.336  1.00 45.12           N  
ANISOU 1842  NH2 ARG A 235     5354   4249   7541   -617   -306   -174       N  
ATOM   1843  N   ARG A 236      65.977  26.076  74.503  1.00 35.50           N  
ANISOU 1843  N   ARG A 236     3443   3360   6686   -269    106   -826       N  
ATOM   1844  CA  ARG A 236      65.466  25.035  73.657  1.00 35.74           C  
ANISOU 1844  CA  ARG A 236     3307   3377   6895   -209     58   -981       C  
ATOM   1845  C   ARG A 236      64.886  25.679  72.426  1.00 46.36           C  
ANISOU 1845  C   ARG A 236     4598   4875   8140    -56     80  -1137       C  
ATOM   1846  O   ARG A 236      65.077  25.191  71.315  1.00 46.70           O  
ANISOU 1846  O   ARG A 236     4534   4971   8240     51     20  -1284       O  
ATOM   1847  CB  ARG A 236      64.400  24.264  74.399  1.00 39.05           C  
ANISOU 1847  CB  ARG A 236     3688   3695   7456   -313     95   -969       C  
ATOM   1848  CG  ARG A 236      63.942  23.051  73.672  1.00 38.92           C  
ANISOU 1848  CG  ARG A 236     3477   3622   7687   -270     35  -1134       C  
ATOM   1849  CD  ARG A 236      65.014  22.008  73.630  1.00 32.55           C  
ANISOU 1849  CD  ARG A 236     2618   2693   7055   -288    -83  -1108       C  
ATOM   1850  NE  ARG A 236      64.469  20.779  73.072  1.00 33.71           N  
ANISOU 1850  NE  ARG A 236     2566   2759   7485   -265   -136  -1273       N  
ATOM   1851  CZ  ARG A 236      65.159  19.946  72.320  1.00 35.70           C  
ANISOU 1851  CZ  ARG A 236     2678   2973   7914   -196   -250  -1399       C  
ATOM   1852  NH1 ARG A 236      64.589  18.858  71.837  1.00 35.53           N  
ANISOU 1852  NH1 ARG A 236     2460   2871   8170   -174   -298  -1572       N  
ATOM   1853  NH2 ARG A 236      66.419  20.216  72.055  1.00 40.78           N  
ANISOU 1853  NH2 ARG A 236     3361   3653   8480   -153   -308  -1375       N  
ATOM   1854  N   MET A 237      64.174  26.784  72.621  1.00 47.73           N  
ANISOU 1854  N   MET A 237     4854   5120   8161    -39    156  -1113       N  
ATOM   1855  CA  MET A 237      63.641  27.520  71.488  1.00 48.32           C  
ANISOU 1855  CA  MET A 237     4914   5327   8117    122    149  -1233       C  
ATOM   1856  C   MET A 237      64.778  27.814  70.503  1.00 43.84           C  
ANISOU 1856  C   MET A 237     4388   4835   7434    215    130  -1232       C  
ATOM   1857  O   MET A 237      64.732  27.441  69.340  1.00 49.02           O  
ANISOU 1857  O   MET A 237     4972   5572   8080    338     77  -1375       O  
ATOM   1858  CB  MET A 237      62.941  28.799  71.944  1.00 42.08           C  
ANISOU 1858  CB  MET A 237     4221   4573   7194    123    221  -1181       C  
ATOM   1859  CG  MET A 237      61.573  28.549  72.578  1.00 42.72           C  
ANISOU 1859  CG  MET A 237     4220   4612   7400     63    260  -1262       C  
ATOM   1860  SD  MET A 237      60.597  30.054  72.802  1.00 33.76           S  
ANISOU 1860  SD  MET A 237     3144   3532   6153    111    319  -1287       S  
ATOM   1861  CE  MET A 237      60.993  30.493  74.476  1.00 48.61           C  
ANISOU 1861  CE  MET A 237     5151   5345   7972    -92    448  -1108       C  
ATOM   1862  N   ALA A 238      65.826  28.447  70.992  1.00 29.19           N  
ANISOU 1862  N   ALA A 238     2641   2950   5498    150    181  -1086       N  
ATOM   1863  CA  ALA A 238      66.984  28.728  70.170  1.00 29.48           C  
ANISOU 1863  CA  ALA A 238     2707   3037   5457    206    205  -1086       C  
ATOM   1864  C   ALA A 238      67.521  27.476  69.420  1.00 39.49           C  
ANISOU 1864  C   ALA A 238     3834   4307   6865    240    139  -1227       C  
ATOM   1865  O   ALA A 238      67.866  27.550  68.239  1.00 31.83           O  
ANISOU 1865  O   ALA A 238     2852   3441   5802    344    161  -1325       O  
ATOM   1866  CB  ALA A 238      68.045  29.372  71.013  1.00 23.36           C  
ANISOU 1866  CB  ALA A 238     2021   2190   4665    104    256   -939       C  
ATOM   1867  N   GLN A 239      67.570  26.328  70.084  1.00 31.52           N  
ANISOU 1867  N   GLN A 239     2723   3178   6075    155     62  -1243       N  
ATOM   1868  CA  GLN A 239      67.940  25.114  69.380  1.00 30.16           C  
ANISOU 1868  CA  GLN A 239     2390   2991   6078    194    -14  -1404       C  
ATOM   1869  C   GLN A 239      67.048  24.801  68.173  1.00 44.54           C  
ANISOU 1869  C   GLN A 239     4121   4937   7865    336    -46  -1608       C  
ATOM   1870  O   GLN A 239      67.524  24.196  67.214  1.00 51.60           O  
ANISOU 1870  O   GLN A 239     4912   5889   8803    410    -76  -1772       O  
ATOM   1871  CB  GLN A 239      67.977  23.909  70.308  1.00 27.36           C  
ANISOU 1871  CB  GLN A 239     1948   2457   5991     85   -107  -1373       C  
ATOM   1872  CG  GLN A 239      69.084  23.901  71.353  1.00 50.34           C  
ANISOU 1872  CG  GLN A 239     4925   5234   8967    -27   -141  -1214       C  
ATOM   1873  CD  GLN A 239      68.911  22.771  72.350  1.00 62.61           C  
ANISOU 1873  CD  GLN A 239     6445   6600  10743   -130   -241  -1139       C  
ATOM   1874  OE1 GLN A 239      68.587  21.649  71.970  1.00 59.21           O  
ANISOU 1874  OE1 GLN A 239     5867   6103  10527   -112   -308  -1257       O  
ATOM   1875  NE2 GLN A 239      69.100  23.070  73.637  1.00 65.99           N  
ANISOU 1875  NE2 GLN A 239     7020   6937  11116   -239   -252   -940       N  
ATOM   1876  N   PHE A 240      65.769  25.184  68.215  1.00 38.01           N  
ANISOU 1876  N   PHE A 240     3317   4153   6972    379    -49  -1626       N  
ATOM   1877  CA  PHE A 240      64.834  24.873  67.111  1.00 43.78           C  
ANISOU 1877  CA  PHE A 240     3950   4995   7688    531   -120  -1847       C  
ATOM   1878  C   PHE A 240      64.582  26.046  66.200  1.00 48.13           C  
ANISOU 1878  C   PHE A 240     4640   5711   7936    678    -96  -1850       C  
ATOM   1879  O   PHE A 240      63.609  26.039  65.445  1.00 44.04           O  
ANISOU 1879  O   PHE A 240     4081   5285   7369    818   -180  -2010       O  
ATOM   1880  CB  PHE A 240      63.452  24.437  67.608  1.00 41.36           C  
ANISOU 1880  CB  PHE A 240     3540   4619   7557    508   -163  -1923       C  
ATOM   1881  CG  PHE A 240      63.421  23.075  68.197  1.00 49.37           C  
ANISOU 1881  CG  PHE A 240     4394   5470   8893    397   -201  -1967       C  
ATOM   1882  CD1 PHE A 240      64.079  22.029  67.586  1.00 52.75           C  
ANISOU 1882  CD1 PHE A 240     4685   5876   9481    428   -275  -2106       C  
ATOM   1883  CD2 PHE A 240      62.711  22.831  69.355  1.00 44.43           C  
ANISOU 1883  CD2 PHE A 240     3757   4704   8420    258   -153  -1874       C  
ATOM   1884  CE1 PHE A 240      64.049  20.774  68.134  1.00 47.93           C  
ANISOU 1884  CE1 PHE A 240     3930   5085   9198    328   -321  -2134       C  
ATOM   1885  CE2 PHE A 240      62.676  21.574  69.897  1.00 39.95           C  
ANISOU 1885  CE2 PHE A 240     3068   3963   8150    149   -177  -1884       C  
ATOM   1886  CZ  PHE A 240      63.349  20.548  69.290  1.00 36.11           C  
ANISOU 1886  CZ  PHE A 240     2445   3434   7840    188   -272  -2006       C  
ATOM   1887  N   ASP A 241      65.413  27.073  66.312  1.00 42.67           N  
ANISOU 1887  N   ASP A 241     4115   5039   7057    648      7  -1674       N  
ATOM   1888  CA  ASP A 241      65.297  28.215  65.431  1.00 46.82           C  
ANISOU 1888  CA  ASP A 241     4802   5695   7292    779     42  -1638       C  
ATOM   1889  C   ASP A 241      64.026  29.009  65.670  1.00 42.23           C  
ANISOU 1889  C   ASP A 241     4279   5118   6649    842     -6  -1613       C  
ATOM   1890  O   ASP A 241      63.664  29.881  64.898  1.00 51.16           O  
ANISOU 1890  O   ASP A 241     5537   6341   7562    981    -28  -1601       O  
ATOM   1891  CB  ASP A 241      65.346  27.742  63.989  1.00 53.44           C  
ANISOU 1891  CB  ASP A 241     5609   6684   8011    934    -12  -1829       C  
ATOM   1892  CG  ASP A 241      66.643  28.045  63.346  1.00 69.11           C  
ANISOU 1892  CG  ASP A 241     7687   8734   9836    927    118  -1777       C  
ATOM   1893  OD1 ASP A 241      67.242  27.121  62.761  1.00 81.62           O  
ANISOU 1893  OD1 ASP A 241     9155  10365  11491    937    115  -1939       O  
ATOM   1894  OD2 ASP A 241      67.065  29.218  63.435  1.00 79.85           O  
ANISOU 1894  OD2 ASP A 241     9226  10089  11024    904    234  -1586       O  
ATOM   1895  N   VAL A 242      63.349  28.698  66.755  1.00 39.92           N  
ANISOU 1895  N   VAL A 242     3897   4716   6556    737    -20  -1608       N  
ATOM   1896  CA  VAL A 242      62.068  29.310  67.034  1.00 34.06           C  
ANISOU 1896  CA  VAL A 242     3157   3966   5819    785    -60  -1639       C  
ATOM   1897  C   VAL A 242      62.171  30.811  67.268  1.00 29.85           C  
ANISOU 1897  C   VAL A 242     2806   3434   5103    797      8  -1466       C  
ATOM   1898  O   VAL A 242      61.328  31.559  66.814  1.00 40.76           O  
ANISOU 1898  O   VAL A 242     4235   4857   6394    929    -59  -1508       O  
ATOM   1899  CB  VAL A 242      61.369  28.591  68.194  1.00 33.74           C  
ANISOU 1899  CB  VAL A 242     2976   3804   6040    641    -42  -1676       C  
ATOM   1900  CG1 VAL A 242      60.416  29.518  68.913  1.00 28.05           C  
ANISOU 1900  CG1 VAL A 242     2290   3049   5318    617     -3  -1644       C  
ATOM   1901  CG2 VAL A 242      60.634  27.390  67.646  1.00 41.67           C  
ANISOU 1901  CG2 VAL A 242     3779   4813   7241    704   -147  -1916       C  
ATOM   1902  N   ILE A 243      63.214  31.253  67.952  1.00 35.82           N  
ANISOU 1902  N   ILE A 243     3654   4131   5825    669    124  -1284       N  
ATOM   1903  CA  ILE A 243      63.370  32.669  68.288  1.00 42.02           C  
ANISOU 1903  CA  ILE A 243     4592   4890   6485    660    197  -1128       C  
ATOM   1904  C   ILE A 243      63.530  33.559  67.064  1.00 38.79           C  
ANISOU 1904  C   ILE A 243     4329   4560   5848    822    189  -1083       C  
ATOM   1905  O   ILE A 243      62.866  34.570  66.944  1.00 35.00           O  
ANISOU 1905  O   ILE A 243     3936   4072   5291    908    158  -1046       O  
ATOM   1906  CB  ILE A 243      64.546  32.885  69.260  1.00 43.06           C  
ANISOU 1906  CB  ILE A 243     4771   4938   6653    493    309   -974       C  
ATOM   1907  CG1 ILE A 243      64.251  32.194  70.588  1.00 36.47           C  
ANISOU 1907  CG1 ILE A 243     3847   4020   5990    340    309   -981       C  
ATOM   1908  CG2 ILE A 243      64.784  34.372  69.494  1.00 36.80           C  
ANISOU 1908  CG2 ILE A 243     4118   4111   5753    493    387   -836       C  
ATOM   1909  CD1 ILE A 243      65.459  32.000  71.385  1.00 42.99           C  
ANISOU 1909  CD1 ILE A 243     4699   4773   6861    204    355   -872       C  
ATOM   1910  N   LYS A 244      64.428  33.173  66.167  1.00 46.55           N  
ANISOU 1910  N   LYS A 244     5348   5612   6727    858    223  -1087       N  
ATOM   1911  CA  LYS A 244      64.641  33.868  64.902  1.00 46.84           C  
ANISOU 1911  CA  LYS A 244     5552   5739   6507   1005    238  -1038       C  
ATOM   1912  C   LYS A 244      63.296  34.215  64.259  1.00 44.91           C  
ANISOU 1912  C   LYS A 244     5345   5552   6165   1197     72  -1125       C  
ATOM   1913  O   LYS A 244      63.118  35.306  63.739  1.00 49.85           O  
ANISOU 1913  O   LYS A 244     6149   6182   6609   1306     63  -1013       O  
ATOM   1914  CB  LYS A 244      65.470  32.964  63.977  1.00 60.99           C  
ANISOU 1914  CB  LYS A 244     7311   7631   8230   1026    272  -1131       C  
ATOM   1915  CG  LYS A 244      66.212  33.646  62.833  1.00 75.07           C  
ANISOU 1915  CG  LYS A 244     9291   9497   9734   1103    387  -1035       C  
ATOM   1916  CD  LYS A 244      66.903  32.604  61.927  1.00 86.48           C  
ANISOU 1916  CD  LYS A 244    10669  11062  11126   1125    421  -1191       C  
ATOM   1917  CE  LYS A 244      65.907  31.939  60.966  1.00 90.67           C  
ANISOU 1917  CE  LYS A 244    11166  11739  11545   1315    234  -1398       C  
ATOM   1918  NZ  LYS A 244      66.469  30.751  60.244  1.00 85.64           N  
ANISOU 1918  NZ  LYS A 244    10406  11212  10922   1328    243  -1608       N  
ATOM   1919  N   HIS A 245      62.350  33.279  64.330  1.00 45.33           N  
ANISOU 1919  N   HIS A 245     5222   5631   6369   1239    -66  -1332       N  
ATOM   1920  CA  HIS A 245      61.038  33.386  63.684  1.00 43.78           C  
ANISOU 1920  CA  HIS A 245     5007   5491   6137   1435   -261  -1486       C  
ATOM   1921  C   HIS A 245      59.955  34.082  64.531  1.00 43.36           C  
ANISOU 1921  C   HIS A 245     4902   5335   6236   1429   -313  -1496       C  
ATOM   1922  O   HIS A 245      58.778  34.001  64.212  1.00 54.60           O  
ANISOU 1922  O   HIS A 245     6240   6778   7729   1568   -484  -1676       O  
ATOM   1923  CB  HIS A 245      60.509  31.991  63.381  1.00 31.75           C  
ANISOU 1923  CB  HIS A 245     3270   4024   4768   1475   -379  -1749       C  
ATOM   1924  CG  HIS A 245      61.153  31.315  62.221  1.00 39.18           C  
ANISOU 1924  CG  HIS A 245     4239   5102   5544   1565   -402  -1838       C  
ATOM   1925  ND1 HIS A 245      60.868  31.641  60.908  1.00 35.15           N  
ANISOU 1925  ND1 HIS A 245     3870   4732   4754   1788   -527  -1900       N  
ATOM   1926  CD2 HIS A 245      62.020  30.279  62.160  1.00 42.61           C  
ANISOU 1926  CD2 HIS A 245     4572   5559   6060   1470   -327  -1901       C  
ATOM   1927  CE1 HIS A 245      61.543  30.852  60.100  1.00 41.66           C  
ANISOU 1927  CE1 HIS A 245     4679   5675   5475   1817   -505  -2004       C  
ATOM   1928  NE2 HIS A 245      62.257  30.015  60.834  1.00 45.99           N  
ANISOU 1928  NE2 HIS A 245     5066   6148   6261   1625   -384  -2016       N  
ATOM   1929  N   LEU A 246      60.331  34.723  65.628  1.00 33.91           N  
ANISOU 1929  N   LEU A 246     3736   4032   5117   1268   -173  -1340       N  
ATOM   1930  CA  LEU A 246      59.357  35.323  66.518  1.00 39.15           C  
ANISOU 1930  CA  LEU A 246     4330   4606   5940   1238   -193  -1379       C  
ATOM   1931  C   LEU A 246      59.749  36.756  66.560  1.00 50.33           C  
ANISOU 1931  C   LEU A 246     5933   5964   7227   1259   -136  -1181       C  
ATOM   1932  O   LEU A 246      58.916  37.674  66.610  1.00 55.49           O  
ANISOU 1932  O   LEU A 246     6609   6562   7912   1353   -218  -1200       O  
ATOM   1933  CB  LEU A 246      59.480  34.745  67.923  1.00 40.50           C  
ANISOU 1933  CB  LEU A 246     4369   4701   6318   1008    -62  -1382       C  
ATOM   1934  CG  LEU A 246      58.815  33.400  68.168  1.00 42.06           C  
ANISOU 1934  CG  LEU A 246     4357   4901   6724    958   -100  -1578       C  
ATOM   1935  CD1 LEU A 246      59.143  32.905  69.568  1.00 42.37           C  
ANISOU 1935  CD1 LEU A 246     4337   4856   6905    719     49  -1509       C  
ATOM   1936  CD2 LEU A 246      57.317  33.546  67.974  1.00 33.16           C  
ANISOU 1936  CD2 LEU A 246     3101   3767   5730   1081   -227  -1793       C  
ATOM   1937  N   PHE A 247      61.059  36.922  66.532  1.00 50.14           N  
ANISOU 1937  N   PHE A 247     6027   5936   7088   1167      7  -1002       N  
ATOM   1938  CA  PHE A 247      61.682  38.216  66.508  1.00 49.77           C  
ANISOU 1938  CA  PHE A 247     6158   5818   6934   1164     98   -799       C  
ATOM   1939  C   PHE A 247      62.755  38.159  65.444  1.00 55.27           C  
ANISOU 1939  C   PHE A 247     7005   6581   7414   1204    173   -684       C  
ATOM   1940  O   PHE A 247      63.854  37.671  65.681  1.00 62.04           O  
ANISOU 1940  O   PHE A 247     7835   7442   8295   1068    308   -641       O  
ATOM   1941  CB  PHE A 247      62.267  38.498  67.870  1.00 38.47           C  
ANISOU 1941  CB  PHE A 247     4677   4291   5649    957    243   -724       C  
ATOM   1942  CG  PHE A 247      61.322  38.228  68.991  1.00 45.63           C  
ANISOU 1942  CG  PHE A 247     5424   5164   6750    877    213   -860       C  
ATOM   1943  CD1 PHE A 247      61.526  37.167  69.842  1.00 46.76           C  
ANISOU 1943  CD1 PHE A 247     5445   5315   7007    720    267   -918       C  
ATOM   1944  CD2 PHE A 247      60.224  39.042  69.192  1.00 55.71           C  
ANISOU 1944  CD2 PHE A 247     6677   6391   8101    956    139   -930       C  
ATOM   1945  CE1 PHE A 247      60.657  36.921  70.873  1.00 47.65           C  
ANISOU 1945  CE1 PHE A 247     5435   5396   7274    630    278  -1028       C  
ATOM   1946  CE2 PHE A 247      59.357  38.807  70.219  1.00 50.97           C  
ANISOU 1946  CE2 PHE A 247     5922   5765   7681    867    150  -1074       C  
ATOM   1947  CZ  PHE A 247      59.572  37.744  71.061  1.00 52.38           C  
ANISOU 1947  CZ  PHE A 247     5999   5961   7941    697    235  -1116       C  
ATOM   1948  N   PRO A 248      62.428  38.666  64.258  1.00 57.30           N  
ANISOU 1948  N   PRO A 248     7427   6888   7458   1396     82   -641       N  
ATOM   1949  CA  PRO A 248      63.206  38.414  63.045  1.00 62.44           C  
ANISOU 1949  CA  PRO A 248     8224   7645   7856   1463    141   -582       C  
ATOM   1950  C   PRO A 248      64.608  39.017  63.076  1.00 60.64           C  
ANISOU 1950  C   PRO A 248     8120   7353   7567   1329    388   -375       C  
ATOM   1951  O   PRO A 248      65.475  38.509  62.388  1.00 76.44           O  
ANISOU 1951  O   PRO A 248    10163   9441   9440   1305    500   -373       O  
ATOM   1952  CB  PRO A 248      62.355  39.059  61.936  1.00 60.42           C  
ANISOU 1952  CB  PRO A 248     8154   7432   7372   1710    -37   -556       C  
ATOM   1953  CG  PRO A 248      61.068  39.407  62.568  1.00 61.97           C  
ANISOU 1953  CG  PRO A 248     8237   7547   7762   1777   -218   -663       C  
ATOM   1954  CD  PRO A 248      61.351  39.633  64.016  1.00 56.14           C  
ANISOU 1954  CD  PRO A 248     7360   6685   7286   1561    -76   -631       C  
ATOM   1955  N   LYS A 249      64.825  40.072  63.845  1.00 54.16           N  
ANISOU 1955  N   LYS A 249     7337   6382   6859   1241    476   -233       N  
ATOM   1956  CA  LYS A 249      66.172  40.606  64.019  1.00 62.55           C  
ANISOU 1956  CA  LYS A 249     8467   7361   7939   1094    714    -74       C  
ATOM   1957  C   LYS A 249      66.899  40.154  65.283  1.00 58.17           C  
ANISOU 1957  C   LYS A 249     7721   6745   7637    887    804   -133       C  
ATOM   1958  O   LYS A 249      67.977  40.666  65.560  1.00 63.20           O  
ANISOU 1958  O   LYS A 249     8380   7291   8341    766    979    -32       O  
ATOM   1959  CB  LYS A 249      66.170  42.136  64.000  1.00 60.79           C  
ANISOU 1959  CB  LYS A 249     8416   6985   7695   1122    775    130       C  
ATOM   1960  CG  LYS A 249      66.822  42.728  62.793  1.00 56.22           C  
ANISOU 1960  CG  LYS A 249     8086   6406   6869   1179    919    318       C  
ATOM   1961  CD  LYS A 249      66.129  42.246  61.545  1.00 63.66           C  
ANISOU 1961  CD  LYS A 249     9160   7510   7517   1384    767    273       C  
ATOM   1962  CE  LYS A 249      66.506  43.092  60.350  1.00 78.27           C  
ANISOU 1962  CE  LYS A 249    11328   9344   9068   1473    881    506       C  
ATOM   1963  NZ  LYS A 249      65.429  43.023  59.333  1.00 89.09           N  
ANISOU 1963  NZ  LYS A 249    12863  10826  10162   1728    631    482       N  
ATOM   1964  N   THR A 250      66.381  39.178  66.012  1.00 43.26           N  
ANISOU 1964  N   THR A 250     5651   4891   5895    845    686   -291       N  
ATOM   1965  CA  THR A 250      67.060  38.704  67.214  1.00 43.63           C  
ANISOU 1965  CA  THR A 250     5558   4880   6138    659    757   -322       C  
ATOM   1966  C   THR A 250      67.851  37.455  66.923  1.00 46.38           C  
ANISOU 1966  C   THR A 250     5800   5304   6519    606    770   -424       C  
ATOM   1967  O   THR A 250      67.311  36.488  66.431  1.00 46.86           O  
ANISOU 1967  O   THR A 250     5792   5461   6550    680    660   -551       O  
ATOM   1968  CB  THR A 250      66.082  38.352  68.298  1.00 38.30           C  
ANISOU 1968  CB  THR A 250     4783   4141   5630    584    685   -373       C  
ATOM   1969  OG1 THR A 250      65.809  39.503  69.074  1.00 47.92           O  
ANISOU 1969  OG1 THR A 250     5856   5390   6963    488    637   -482       O  
ATOM   1970  CG2 THR A 250      66.685  37.370  69.196  1.00 32.45           C  
ANISOU 1970  CG2 THR A 250     4060   3413   4857    711    564   -421       C  
ATOM   1971  N   TYR A 251      69.142  37.478  67.231  1.00 47.20           N  
ANISOU 1971  N   TYR A 251     5877   5349   6706    485    904   -383       N  
ATOM   1972  CA  TYR A 251      70.015  36.361  66.894  1.00 46.21           C  
ANISOU 1972  CA  TYR A 251     5649   5274   6635    438    934   -482       C  
ATOM   1973  C   TYR A 251      70.617  35.820  68.181  1.00 43.52           C  
ANISOU 1973  C   TYR A 251     5167   4841   6526    292    896   -521       C  
ATOM   1974  O   TYR A 251      71.471  36.456  68.791  1.00 41.14           O  
ANISOU 1974  O   TYR A 251     4866   4439   6326    196    979   -460       O  
ATOM   1975  CB  TYR A 251      71.100  36.805  65.910  1.00 28.17           C  
ANISOU 1975  CB  TYR A 251     3450   2999   4254    433   1131   -426       C  
ATOM   1976  CG  TYR A 251      70.581  37.283  64.564  1.00 85.87           C  
ANISOU 1976  CG  TYR A 251    10942  10407  11276    584   1169   -365       C  
ATOM   1977  CD1 TYR A 251      70.258  36.380  63.555  1.00 87.01           C  
ANISOU 1977  CD1 TYR A 251    11082  10707  11270    693   1106   -490       C  
ATOM   1978  CD2 TYR A 251      70.423  38.643  64.297  1.00 90.20           C  
ANISOU 1978  CD2 TYR A 251    11679  10887  11704    625   1254   -185       C  
ATOM   1979  CE1 TYR A 251      69.791  36.816  62.321  1.00 92.61           C  
ANISOU 1979  CE1 TYR A 251    11988  11520  11678    846   1116   -436       C  
ATOM   1980  CE2 TYR A 251      69.948  39.091  63.066  1.00 89.45           C  
ANISOU 1980  CE2 TYR A 251    11791  10873  11322    776   1265   -103       C  
ATOM   1981  CZ  TYR A 251      69.638  38.174  62.082  1.00 94.48           C  
ANISOU 1981  CZ  TYR A 251    12439  11684  11775    889   1191   -228       C  
ATOM   1982  OH  TYR A 251      69.174  38.613  60.856  1.00 93.83           O  
ANISOU 1982  OH  TYR A 251    12588  11696  11369   1053   1179   -150       O  
ATOM   1983  N   TYR A 252      70.149  34.647  68.593  1.00 40.87           N  
ANISOU 1983  N   TYR A 252     4716   4531   6280    281    759   -625       N  
ATOM   1984  CA  TYR A 252      70.458  34.135  69.920  1.00 39.22           C  
ANISOU 1984  CA  TYR A 252     4417   4231   6253    158    686   -632       C  
ATOM   1985  C   TYR A 252      71.838  33.488  69.938  1.00 43.77           C  
ANISOU 1985  C   TYR A 252     4896   4756   6980     85    706   -685       C  
ATOM   1986  O   TYR A 252      71.980  32.293  69.670  1.00 48.32           O  
ANISOU 1986  O   TYR A 252     5364   5351   7644     93    632   -790       O  
ATOM   1987  CB  TYR A 252      69.351  33.182  70.403  1.00 29.16           C  
ANISOU 1987  CB  TYR A 252     3076   2977   5025    162    551   -696       C  
ATOM   1988  CG  TYR A 252      69.391  32.880  71.871  1.00 31.76           C  
ANISOU 1988  CG  TYR A 252     3380   3215   5471     38    487   -657       C  
ATOM   1989  CD1 TYR A 252      68.790  33.724  72.803  1.00 33.78           C  
ANISOU 1989  CD1 TYR A 252     3707   3445   5681     -5    504   -593       C  
ATOM   1990  CD2 TYR A 252      70.052  31.758  72.335  1.00 35.88           C  
ANISOU 1990  CD2 TYR A 252     3816   3674   6142    -32    405   -687       C  
ATOM   1991  CE1 TYR A 252      68.840  33.442  74.171  1.00 36.96           C  
ANISOU 1991  CE1 TYR A 252     4115   3783   6144   -121    454   -556       C  
ATOM   1992  CE2 TYR A 252      70.109  31.463  73.675  1.00 40.11           C  
ANISOU 1992  CE2 TYR A 252     4368   4126   6746   -138    333   -629       C  
ATOM   1993  CZ  TYR A 252      69.507  32.299  74.595  1.00 44.24           C  
ANISOU 1993  CZ  TYR A 252     4982   4646   7181   -185    365   -561       C  
ATOM   1994  OH  TYR A 252      69.593  31.962  75.926  1.00 40.40           O  
ANISOU 1994  OH  TYR A 252     4537   4093   6720   -290    298   -502       O  
ATOM   1995  N   THR A 253      72.839  34.307  70.267  1.00 41.88           N  
ANISOU 1995  N   THR A 253     4675   4435   6801     18    800   -632       N  
ATOM   1996  CA  THR A 253      74.248  33.935  70.245  1.00 43.30           C  
ANISOU 1996  CA  THR A 253     4747   4548   7156    -48    837   -704       C  
ATOM   1997  C   THR A 253      74.758  33.662  71.651  1.00 46.73           C  
ANISOU 1997  C   THR A 253     5120   4866   7770   -141    699   -705       C  
ATOM   1998  O   THR A 253      74.088  33.990  72.630  1.00 49.96           O  
ANISOU 1998  O   THR A 253     5598   5255   8128   -167    623   -632       O  
ATOM   1999  CB  THR A 253      75.101  35.088  69.674  1.00 40.86           C  
ANISOU 1999  CB  THR A 253     4486   4205   6833    -68   1047   -663       C  
ATOM   2000  OG1 THR A 253      74.869  36.274  70.439  1.00 42.09           O  
ANISOU 2000  OG1 THR A 253     4728   4290   6973   -100   1068   -555       O  
ATOM   2001  CG2 THR A 253      74.737  35.363  68.251  1.00 39.08           C  
ANISOU 2001  CG2 THR A 253     4360   4092   6395     24   1189   -640       C  
ATOM   2002  N   PRO A 254      75.966  33.086  71.759  1.00 45.74           N  
ANISOU 2002  N   PRO A 254     4867   4663   7851   -188    663   -800       N  
ATOM   2003  CA  PRO A 254      76.583  32.819  73.050  1.00 43.34           C  
ANISOU 2003  CA  PRO A 254     4514   4239   7715   -257    498   -809       C  
ATOM   2004  C   PRO A 254      76.484  34.050  73.907  1.00 43.44           C  
ANISOU 2004  C   PRO A 254     4623   4214   7668   -296    525   -724       C  
ATOM   2005  O   PRO A 254      76.239  33.967  75.107  1.00 53.39           O  
ANISOU 2005  O   PRO A 254     5930   5436   8918   -333    378   -682       O  
ATOM   2006  CB  PRO A 254      78.026  32.549  72.667  1.00 30.78           C  
ANISOU 2006  CB  PRO A 254     2765   2569   6360   -283    529   -947       C  
ATOM   2007  CG  PRO A 254      77.910  31.917  71.392  1.00 29.87           C  
ANISOU 2007  CG  PRO A 254     2595   2545   6211   -231    625  -1027       C  
ATOM   2008  CD  PRO A 254      76.859  32.677  70.671  1.00 40.78           C  
ANISOU 2008  CD  PRO A 254     4127   4051   7315   -174    772   -924       C  
ATOM   2009  N   SER A 255      76.639  35.195  73.266  1.00 33.27           N  
ANISOU 2009  N   SER A 255     3373   2937   6332   -287    720   -698       N  
ATOM   2010  CA  SER A 255      76.522  36.459  73.957  1.00 31.25           C  
ANISOU 2010  CA  SER A 255     3192   2634   6047   -318    763   -635       C  
ATOM   2011  C   SER A 255      75.128  36.706  74.500  1.00 38.37           C  
ANISOU 2011  C   SER A 255     4215   3604   6761   -293    706   -547       C  
ATOM   2012  O   SER A 255      74.966  36.939  75.694  1.00 43.00           O  
ANISOU 2012  O   SER A 255     4833   4160   7345   -337    604   -538       O  
ATOM   2013  CB  SER A 255      76.958  37.594  73.053  1.00 25.42           C  
ANISOU 2013  CB  SER A 255     2473   1867   5318   -315    998   -609       C  
ATOM   2014  OG  SER A 255      78.286  37.366  72.618  1.00 48.26           O  
ANISOU 2014  OG  SER A 255     5232   4690   8415   -357   1080   -717       O  
ATOM   2015  N   MET A 256      74.124  36.671  73.631  1.00 41.53           N  
ANISOU 2015  N   MET A 256     4679   4099   7003   -220    770   -502       N  
ATOM   2016  CA  MET A 256      72.763  36.968  74.063  1.00 36.39           C  
ANISOU 2016  CA  MET A 256     4113   3502   6210   -193    731   -451       C  
ATOM   2017  C   MET A 256      72.394  36.001  75.174  1.00 43.32           C  
ANISOU 2017  C   MET A 256     4975   4383   7100   -248    574   -469       C  
ATOM   2018  O   MET A 256      71.876  36.387  76.231  1.00 43.71           O  
ANISOU 2018  O   MET A 256     5078   4428   7101   -293    536   -449       O  
ATOM   2019  CB  MET A 256      71.781  36.826  72.905  1.00 33.67           C  
ANISOU 2019  CB  MET A 256     3812   3255   5727    -89    775   -437       C  
ATOM   2020  CG  MET A 256      70.369  37.281  73.239  1.00 27.46           C  
ANISOU 2020  CG  MET A 256     3088   2509   4837    -49    745   -415       C  
ATOM   2021  SD  MET A 256      69.245  37.376  71.836  1.00 46.06           S  
ANISOU 2021  SD  MET A 256     5497   4961   7043    105    761   -417       S  
ATOM   2022  CE  MET A 256      70.137  38.420  70.699  1.00 43.59           C  
ANISOU 2022  CE  MET A 256     5277   4615   6671    154    918   -327       C  
ATOM   2023  N   ASP A 257      72.694  34.731  74.933  1.00 28.51           N  
ANISOU 2023  N   ASP A 257     3029   2509   5293   -249    492   -509       N  
ATOM   2024  CA  ASP A 257      72.412  33.710  75.910  1.00 31.79           C  
ANISOU 2024  CA  ASP A 257     3445   2902   5731   -304    347   -498       C  
ATOM   2025  C   ASP A 257      73.127  33.940  77.239  1.00 39.61           C  
ANISOU 2025  C   ASP A 257     4473   3814   6764   -382    248   -478       C  
ATOM   2026  O   ASP A 257      72.562  33.670  78.283  1.00 45.19           O  
ANISOU 2026  O   ASP A 257     5257   4523   7390   -435    175   -431       O  
ATOM   2027  CB  ASP A 257      72.774  32.358  75.355  1.00 41.31           C  
ANISOU 2027  CB  ASP A 257     4554   4089   7053   -285    268   -552       C  
ATOM   2028  CG  ASP A 257      72.925  31.345  76.419  1.00 36.56           C  
ANISOU 2028  CG  ASP A 257     3958   3407   6525   -350    101   -519       C  
ATOM   2029  OD1 ASP A 257      74.034  31.219  76.985  1.00 43.53           O  
ANISOU 2029  OD1 ASP A 257     4817   4199   7522   -383     -6   -530       O  
ATOM   2030  OD2 ASP A 257      71.928  30.676  76.676  1.00 24.88           O  
ANISOU 2030  OD2 ASP A 257     2507   1946   5000   -367     75   -485       O  
ATOM   2031  N   GLU A 258      74.377  34.398  77.199  1.00 38.97           N  
ANISOU 2031  N   GLU A 258     4334   3663   6808   -389    245   -525       N  
ATOM   2032  CA  GLU A 258      75.086  34.774  78.420  1.00 27.86           C  
ANISOU 2032  CA  GLU A 258     2954   2186   5447   -442    132   -538       C  
ATOM   2033  C   GLU A 258      74.356  35.912  79.112  1.00 41.23           C  
ANISOU 2033  C   GLU A 258     4745   3923   6996   -465    199   -509       C  
ATOM   2034  O   GLU A 258      74.267  35.951  80.331  1.00 41.76           O  
ANISOU 2034  O   GLU A 258     4890   3988   6987   -512     95   -499       O  
ATOM   2035  CB  GLU A 258      76.510  35.208  78.115  1.00 34.55           C  
ANISOU 2035  CB  GLU A 258     3685   2942   6501   -440    144   -633       C  
ATOM   2036  CG  GLU A 258      77.317  35.701  79.317  1.00 25.22           C  
ANISOU 2036  CG  GLU A 258     2505   1681   5396   -477      7   -687       C  
ATOM   2037  CD  GLU A 258      78.797  35.897  78.974  1.00 50.28           C  
ANISOU 2037  CD  GLU A 258     5517   4742   8847   -476      1   -821       C  
ATOM   2038  OE1 GLU A 258      79.249  35.274  77.978  1.00 44.81           O  
ANISOU 2038  OE1 GLU A 258     4715   4030   8281   -457     60   -866       O  
ATOM   2039  OE2 GLU A 258      79.508  36.662  79.687  1.00 43.87           O  
ANISOU 2039  OE2 GLU A 258     4669   3858   8141   -496    -57   -904       O  
ATOM   2040  N   LYS A 259      73.826  36.845  78.331  1.00 43.76           N  
ANISOU 2040  N   LYS A 259     5069   4282   7275   -426    369   -500       N  
ATOM   2041  CA  LYS A 259      73.057  37.923  78.915  1.00 46.07           C  
ANISOU 2041  CA  LYS A 259     5432   4605   7466   -438    430   -493       C  
ATOM   2042  C   LYS A 259      71.812  37.339  79.553  1.00 50.44           C  
ANISOU 2042  C   LYS A 259     6061   5238   7865   -465    394   -461       C  
ATOM   2043  O   LYS A 259      71.535  37.603  80.714  1.00 51.56           O  
ANISOU 2043  O   LYS A 259     6271   5399   7921   -522    355   -475       O  
ATOM   2044  CB  LYS A 259      72.690  38.964  77.869  1.00 40.51           C  
ANISOU 2044  CB  LYS A 259     4724   3902   6765   -377    595   -475       C  
ATOM   2045  CG  LYS A 259      73.865  39.772  77.439  1.00 35.30           C  
ANISOU 2045  CG  LYS A 259     4006   3145   6261   -379    677   -498       C  
ATOM   2046  CD  LYS A 259      73.505  40.773  76.373  1.00 31.92           C  
ANISOU 2046  CD  LYS A 259     3612   2701   5817   -320    846   -440       C  
ATOM   2047  CE  LYS A 259      74.760  41.451  75.871  1.00 36.56           C  
ANISOU 2047  CE  LYS A 259     4140   3174   6579   -344    966   -453       C  
ATOM   2048  NZ  LYS A 259      74.491  42.719  75.132  1.00 41.29           N  
ANISOU 2048  NZ  LYS A 259     4799   3710   7179   -305   1133   -373       N  
ATOM   2049  N   MET A 260      71.071  36.535  78.794  1.00 47.07           N  
ANISOU 2049  N   MET A 260     5619   4859   7408   -428    418   -435       N  
ATOM   2050  CA  MET A 260      69.831  35.937  79.286  1.00 42.96           C  
ANISOU 2050  CA  MET A 260     5142   4397   6783   -462    416   -421       C  
ATOM   2051  C   MET A 260      70.041  35.225  80.633  1.00 45.80           C  
ANISOU 2051  C   MET A 260     5580   4737   7086   -559    308   -383       C  
ATOM   2052  O   MET A 260      69.196  35.295  81.528  1.00 45.64           O  
ANISOU 2052  O   MET A 260     5635   4761   6945   -623    345   -378       O  
ATOM   2053  CB  MET A 260      69.259  34.972  78.240  1.00 30.32           C  
ANISOU 2053  CB  MET A 260     3480   2825   5214   -405    423   -425       C  
ATOM   2054  CG  MET A 260      67.760  34.837  78.267  1.00 41.66           C  
ANISOU 2054  CG  MET A 260     4916   4321   6591   -403    481   -455       C  
ATOM   2055  SD  MET A 260      66.876  36.404  78.066  1.00 55.78           S  
ANISOU 2055  SD  MET A 260     6716   6150   8327   -343    588   -508       S  
ATOM   2056  CE  MET A 260      67.230  36.762  76.371  1.00 40.96           C  
ANISOU 2056  CE  MET A 260     4806   4277   6481   -199    604   -502       C  
ATOM   2057  N   GLU A 261      71.181  34.556  80.784  1.00 42.69           N  
ANISOU 2057  N   GLU A 261     5172   4271   6776   -567    174   -361       N  
ATOM   2058  CA  GLU A 261      71.477  33.835  82.015  1.00 41.07           C  
ANISOU 2058  CA  GLU A 261     5069   4029   6508   -640     32   -302       C  
ATOM   2059  C   GLU A 261      71.661  34.778  83.192  1.00 50.16           C  
ANISOU 2059  C   GLU A 261     6317   5206   7536   -684      9   -328       C  
ATOM   2060  O   GLU A 261      71.134  34.553  84.274  1.00 62.75           O  
ANISOU 2060  O   GLU A 261     8044   6839   8959   -756     -7   -283       O  
ATOM   2061  CB  GLU A 261      72.721  32.991  81.855  1.00 39.67           C  
ANISOU 2061  CB  GLU A 261     4837   3749   6487   -616   -141   -296       C  
ATOM   2062  CG  GLU A 261      73.143  32.376  83.147  1.00 47.49           C  
ANISOU 2062  CG  GLU A 261     5955   4684   7405   -669   -330   -226       C  
ATOM   2063  CD  GLU A 261      74.112  31.242  82.969  1.00 55.25           C  
ANISOU 2063  CD  GLU A 261     6880   5544   8568   -640   -526   -210       C  
ATOM   2064  OE1 GLU A 261      74.110  30.623  81.892  1.00 54.49           O  
ANISOU 2064  OE1 GLU A 261     6655   5422   8627   -601   -487   -240       O  
ATOM   2065  OE2 GLU A 261      74.874  30.962  83.915  1.00 64.68           O  
ANISOU 2065  OE2 GLU A 261     8158   6665   9751   -648   -736   -181       O  
ATOM   2066  N   ASN A 262      72.426  35.835  82.970  1.00 45.07           N  
ANISOU 2066  N   ASN A 262     5604   4537   6982   -644     20   -411       N  
ATOM   2067  CA  ASN A 262      72.562  36.894  83.941  1.00 39.41           C  
ANISOU 2067  CA  ASN A 262     4943   3846   6186   -671     12   -479       C  
ATOM   2068  C   ASN A 262      71.212  37.528  84.245  1.00 42.28           C  
ANISOU 2068  C   ASN A 262     5358   4305   6400   -705    171   -499       C  
ATOM   2069  O   ASN A 262      70.913  37.878  85.377  1.00 44.52           O  
ANISOU 2069  O   ASN A 262     5739   4646   6529   -761    163   -535       O  
ATOM   2070  CB  ASN A 262      73.491  37.976  83.389  1.00 41.56           C  
ANISOU 2070  CB  ASN A 262     5094   4052   6646   -621     44   -573       C  
ATOM   2071  CG  ASN A 262      74.921  37.501  83.203  1.00 43.24           C  
ANISOU 2071  CG  ASN A 262     5224   4160   7047   -597   -104   -607       C  
ATOM   2072  OD1 ASN A 262      75.691  38.156  82.509  1.00 46.56           O  
ANISOU 2072  OD1 ASN A 262     5522   4511   7659   -566    -39   -676       O  
ATOM   2073  ND2 ASN A 262      75.286  36.369  83.819  1.00 34.52           N  
ANISOU 2073  ND2 ASN A 262     4181   3029   5905   -611   -297   -560       N  
ATOM   2074  N   LEU A 263      70.413  37.704  83.204  1.00 49.24           N  
ANISOU 2074  N   LEU A 263     6167   5207   7336   -662    311   -496       N  
ATOM   2075  CA  LEU A 263      69.112  38.322  83.332  1.00 47.25           C  
ANISOU 2075  CA  LEU A 263     5924   5027   7003   -675    452   -544       C  
ATOM   2076  C   LEU A 263      68.304  37.486  84.305  1.00 54.66           C  
ANISOU 2076  C   LEU A 263     6966   6029   7772   -771    465   -511       C  
ATOM   2077  O   LEU A 263      67.750  38.007  85.265  1.00 55.62           O  
ANISOU 2077  O   LEU A 263     7152   6215   7766   -834    529   -574       O  
ATOM   2078  CB  LEU A 263      68.426  38.390  81.965  1.00 46.72           C  
ANISOU 2078  CB  LEU A 263     5767   4958   7025   -592    545   -539       C  
ATOM   2079  CG  LEU A 263      67.360  39.467  81.698  1.00 48.67           C  
ANISOU 2079  CG  LEU A 263     5976   5234   7284   -551    663   -618       C  
ATOM   2080  CD1 LEU A 263      65.951  38.910  81.701  1.00 34.72           C  
ANISOU 2080  CD1 LEU A 263     4193   3529   5470   -569    731   -652       C  
ATOM   2081  CD2 LEU A 263      67.493  40.622  82.668  1.00 57.89           C  
ANISOU 2081  CD2 LEU A 263     7164   6401   8432   -589    686   -706       C  
ATOM   2082  N   PHE A 264      68.260  36.178  84.085  1.00 47.82           N  
ANISOU 2082  N   PHE A 264     6119   5138   6911   -790    415   -415       N  
ATOM   2083  CA  PHE A 264      67.423  35.344  84.930  1.00 47.74           C  
ANISOU 2083  CA  PHE A 264     6213   5165   6760   -894    464   -362       C  
ATOM   2084  C   PHE A 264      67.975  35.192  86.339  1.00 57.64           C  
ANISOU 2084  C   PHE A 264     7642   6432   7825   -976    368   -310       C  
ATOM   2085  O   PHE A 264      67.214  35.099  87.312  1.00 59.82           O  
ANISOU 2085  O   PHE A 264     8038   6775   7915  -1077    465   -303       O  
ATOM   2086  CB  PHE A 264      67.116  33.995  84.271  1.00 47.67           C  
ANISOU 2086  CB  PHE A 264     6163   5105   6845   -894    448   -281       C  
ATOM   2087  CG  PHE A 264      66.008  34.077  83.272  1.00 50.47           C  
ANISOU 2087  CG  PHE A 264     6384   5488   7305   -846    577   -361       C  
ATOM   2088  CD1 PHE A 264      66.278  34.103  81.916  1.00 55.11           C  
ANISOU 2088  CD1 PHE A 264     6848   6052   8039   -727    540   -391       C  
ATOM   2089  CD2 PHE A 264      64.695  34.205  83.691  1.00 48.92           C  
ANISOU 2089  CD2 PHE A 264     6184   5346   7056   -913    736   -427       C  
ATOM   2090  CE1 PHE A 264      65.251  34.225  80.994  1.00 52.79           C  
ANISOU 2090  CE1 PHE A 264     6447   5791   7820   -660    623   -476       C  
ATOM   2091  CE2 PHE A 264      63.669  34.328  82.779  1.00 45.33           C  
ANISOU 2091  CE2 PHE A 264     5591   4910   6723   -850    821   -531       C  
ATOM   2092  CZ  PHE A 264      63.945  34.337  81.432  1.00 47.10           C  
ANISOU 2092  CZ  PHE A 264     5708   5112   7074   -715    747   -551       C  
ATOM   2093  N   ARG A 265      69.295  35.198  86.459  1.00 57.68           N  
ANISOU 2093  N   ARG A 265     7664   6376   7874   -929    179   -290       N  
ATOM   2094  CA  ARG A 265      69.914  35.090  87.775  1.00 60.08           C  
ANISOU 2094  CA  ARG A 265     8143   6691   7995   -978     34   -254       C  
ATOM   2095  C   ARG A 265      69.512  36.259  88.668  1.00 61.13           C  
ANISOU 2095  C   ARG A 265     8335   6934   7958  -1018    127   -378       C  
ATOM   2096  O   ARG A 265      69.311  36.081  89.861  1.00 60.30           O  
ANISOU 2096  O   ARG A 265     8415   6896   7602  -1097    113   -348       O  
ATOM   2097  CB  ARG A 265      71.441  34.992  87.662  1.00 53.22           C  
ANISOU 2097  CB  ARG A 265     7236   5724   7263   -900   -208   -260       C  
ATOM   2098  CG  ARG A 265      72.146  34.422  88.897  1.00 42.83           C  
ANISOU 2098  CG  ARG A 265     6113   4383   5776   -925   -438   -187       C  
ATOM   2099  CD  ARG A 265      73.676  34.306  88.694  1.00 56.35           C  
ANISOU 2099  CD  ARG A 265     7740   5977   7694   -832   -699   -234       C  
ATOM   2100  NE  ARG A 265      74.281  35.535  88.178  1.00 59.29           N  
ANISOU 2100  NE  ARG A 265     7932   6342   8255   -772   -661   -410       N  
ATOM   2101  CZ  ARG A 265      74.568  35.755  86.894  1.00 57.36           C  
ANISOU 2101  CZ  ARG A 265     7486   6038   8271   -722   -567   -459       C  
ATOM   2102  NH1 ARG A 265      75.099  36.907  86.506  1.00 60.50           N  
ANISOU 2102  NH1 ARG A 265     7745   6413   8829   -683   -508   -598       N  
ATOM   2103  NH2 ARG A 265      74.324  34.827  85.991  1.00 57.29           N  
ANISOU 2103  NH2 ARG A 265     7419   5988   8361   -713   -523   -372       N  
ATOM   2104  N   ASN A 266      69.367  37.443  88.077  1.00 64.68           N  
ANISOU 2104  N   ASN A 266     8634   7398   8543   -964    227   -515       N  
ATOM   2105  CA  ASN A 266      69.196  38.675  88.849  1.00 60.56           C  
ANISOU 2105  CA  ASN A 266     8125   6954   7931   -982    284   -670       C  
ATOM   2106  C   ASN A 266      67.766  39.169  89.015  1.00 64.28           C  
ANISOU 2106  C   ASN A 266     8577   7519   8328  -1039    515   -759       C  
ATOM   2107  O   ASN A 266      67.519  40.092  89.784  1.00 69.85           O  
ANISOU 2107  O   ASN A 266     9299   8299   8941  -1068    573   -905       O  
ATOM   2108  CB  ASN A 266      70.075  39.793  88.277  1.00 50.08           C  
ANISOU 2108  CB  ASN A 266     6645   5553   6829   -890    230   -783       C  
ATOM   2109  CG  ASN A 266      71.536  39.556  88.540  1.00 58.36           C  
ANISOU 2109  CG  ASN A 266     7709   6525   7940   -851     -1   -776       C  
ATOM   2110  OD1 ASN A 266      71.950  39.445  89.685  1.00 67.55           O  
ANISOU 2110  OD1 ASN A 266     9005   7733   8929   -878   -143   -804       O  
ATOM   2111  ND2 ASN A 266      72.326  39.453  87.483  1.00 62.57           N  
ANISOU 2111  ND2 ASN A 266     8108   6946   8718   -783    -45   -750       N  
ATOM   2112  N   ILE A 267      66.824  38.562  88.303  1.00 67.88           N  
ANISOU 2112  N   ILE A 267     8978   7967   8847  -1052    641   -701       N  
ATOM   2113  CA  ILE A 267      65.428  38.979  88.407  1.00 65.16           C  
ANISOU 2113  CA  ILE A 267     8581   7695   8482  -1102    855   -814       C  
ATOM   2114  C   ILE A 267      64.857  38.777  89.811  1.00 64.69           C  
ANISOU 2114  C   ILE A 267     8684   7749   8148  -1242    962   -846       C  
ATOM   2115  O   ILE A 267      64.115  39.631  90.313  1.00 71.84           O  
ANISOU 2115  O   ILE A 267     9552   8735   9009  -1282   1109  -1019       O  
ATOM   2116  CB  ILE A 267      64.534  38.330  87.342  1.00 53.71           C  
ANISOU 2116  CB  ILE A 267     7020   6207   7182  -1077    946   -775       C  
ATOM   2117  CG1 ILE A 267      64.922  38.852  85.956  1.00 54.22           C  
ANISOU 2117  CG1 ILE A 267     6935   6191   7475   -932    878   -783       C  
ATOM   2118  CG2 ILE A 267      63.102  38.702  87.576  1.00 55.92           C  
ANISOU 2118  CG2 ILE A 267     7232   6552   7463  -1134   1153   -921       C  
ATOM   2119  CD1 ILE A 267      64.052  38.368  84.867  1.00 49.94           C  
ANISOU 2119  CD1 ILE A 267     6282   5625   7067   -879    937   -780       C  
ATOM   2120  N   PRO A 268      65.218  37.668  90.465  1.00 48.46           N  
ANISOU 2120  N   PRO A 268     6816   5693   5903  -1316    890   -681       N  
ATOM   2121  CA  PRO A 268      64.809  37.558  91.868  1.00 56.73           C  
ANISOU 2121  CA  PRO A 268     8065   6857   6634  -1450    991   -695       C  
ATOM   2122  C   PRO A 268      65.287  38.753  92.664  1.00 65.71           C  
ANISOU 2122  C   PRO A 268     9232   8081   7652  -1427    934   -868       C  
ATOM   2123  O   PRO A 268      64.484  39.535  93.169  1.00 71.40           O  
ANISOU 2123  O   PRO A 268     9918   8905   8305  -1483   1116  -1052       O  
ATOM   2124  CB  PRO A 268      65.538  36.307  92.356  1.00 53.82           C  
ANISOU 2124  CB  PRO A 268     7915   6436   6097  -1486    826   -459       C  
ATOM   2125  CG  PRO A 268      65.676  35.472  91.152  1.00 60.20           C  
ANISOU 2125  CG  PRO A 268     8597   7110   7168  -1423    760   -340       C  
ATOM   2126  CD  PRO A 268      65.875  36.446  89.985  1.00 55.34           C  
ANISOU 2126  CD  PRO A 268     7732   6459   6834  -1290    737   -481       C  
ATOM   2127  N   TRP A 269      66.600  38.894  92.767  1.00 69.87           N  
ANISOU 2127  N   TRP A 269     9801   8561   8186  -1343    679   -835       N  
ATOM   2128  CA  TRP A 269      67.168  39.973  93.551  1.00 67.66           C  
ANISOU 2128  CA  TRP A 269     9541   8352   7816  -1314    591  -1017       C  
ATOM   2129  C   TRP A 269      66.535  41.313  93.217  1.00 60.88           C  
ANISOU 2129  C   TRP A 269     8473   7517   7142  -1286    750  -1252       C  
ATOM   2130  O   TRP A 269      66.385  42.161  94.082  1.00 57.36           O  
ANISOU 2130  O   TRP A 269     8048   7174   6572  -1315    795  -1446       O  
ATOM   2131  CB  TRP A 269      68.680  40.051  93.369  1.00 62.28           C  
ANISOU 2131  CB  TRP A 269     8839   7571   7255  -1202    295   -992       C  
ATOM   2132  CG  TRP A 269      69.291  41.077  94.247  1.00 63.66           C  
ANISOU 2132  CG  TRP A 269     9030   7811   7346  -1171    183  -1196       C  
ATOM   2133  CD1 TRP A 269      69.799  40.886  95.500  1.00 73.22           C  
ANISOU 2133  CD1 TRP A 269    10462   9115   8244  -1192     21  -1214       C  
ATOM   2134  CD2 TRP A 269      69.438  42.469  93.961  1.00 62.83           C  
ANISOU 2134  CD2 TRP A 269     8716   7680   7476  -1109    216  -1424       C  
ATOM   2135  NE1 TRP A 269      70.262  42.075  96.007  1.00 74.26           N  
ANISOU 2135  NE1 TRP A 269    10515   9291   8408  -1143    -55  -1467       N  
ATOM   2136  CE2 TRP A 269      70.053  43.066  95.078  1.00 69.88           C  
ANISOU 2136  CE2 TRP A 269     9689   8654   8210  -1097     71  -1598       C  
ATOM   2137  CE3 TRP A 269      69.109  43.274  92.866  1.00 59.80           C  
ANISOU 2137  CE3 TRP A 269     8096   7203   7424  -1057    344  -1494       C  
ATOM   2138  CZ2 TRP A 269      70.350  44.425  95.134  1.00 70.38           C  
ANISOU 2138  CZ2 TRP A 269     9575   8696   8471  -1044     61  -1854       C  
ATOM   2139  CZ3 TRP A 269      69.407  44.627  92.919  1.00 61.52           C  
ANISOU 2139  CZ3 TRP A 269     8160   7387   7828  -1006    338  -1715       C  
ATOM   2140  CH2 TRP A 269      70.018  45.188  94.045  1.00 68.07           C  
ANISOU 2140  CH2 TRP A 269     9046   8287   8529  -1004    204  -1900       C  
ATOM   2141  N   VAL A 270      66.162  41.520  91.965  1.00 64.74           N  
ANISOU 2141  N   VAL A 270     8763   7907   7928  -1221    822  -1244       N  
ATOM   2142  CA  VAL A 270      65.489  42.770  91.638  1.00 68.20           C  
ANISOU 2142  CA  VAL A 270     9014   8344   8553  -1186    955  -1452       C  
ATOM   2143  C   VAL A 270      64.110  42.798  92.294  1.00 73.17           C  
ANISOU 2143  C   VAL A 270     9664   9098   9041  -1299   1195  -1577       C  
ATOM   2144  O   VAL A 270      63.864  43.571  93.205  1.00 75.50           O  
ANISOU 2144  O   VAL A 270     9970   9492   9223  -1345   1267  -1778       O  
ATOM   2145  CB  VAL A 270      65.419  43.023  90.129  1.00 57.59           C  
ANISOU 2145  CB  VAL A 270     7484   6862   7534  -1075    954  -1402       C  
ATOM   2146  CG1 VAL A 270      64.347  44.042  89.813  1.00 57.66           C  
ANISOU 2146  CG1 VAL A 270     7331   6867   7710  -1050   1108  -1584       C  
ATOM   2147  CG2 VAL A 270      66.764  43.529  89.646  1.00 59.07           C  
ANISOU 2147  CG2 VAL A 270     7615   6936   7893   -977    777  -1375       C  
ATOM   2148  N   GLU A 271      63.222  41.929  91.848  1.00 72.40           N  
ANISOU 2148  N   GLU A 271     9556   8991   8961  -1348   1327  -1480       N  
ATOM   2149  CA  GLU A 271      61.943  41.765  92.509  1.00 71.13           C  
ANISOU 2149  CA  GLU A 271     9414   8938   8674  -1479   1579  -1593       C  
ATOM   2150  C   GLU A 271      62.030  41.998  94.013  1.00 74.87           C  
ANISOU 2150  C   GLU A 271    10070   9567   8809  -1591   1642  -1695       C  
ATOM   2151  O   GLU A 271      61.395  42.903  94.536  1.00 80.99           O  
ANISOU 2151  O   GLU A 271    10764  10428   9579  -1628   1788  -1947       O  
ATOM   2152  CB  GLU A 271      61.388  40.370  92.230  1.00 71.56           C  
ANISOU 2152  CB  GLU A 271     9533   8966   8692  -1557   1670  -1407       C  
ATOM   2153  CG  GLU A 271      60.581  40.295  90.959  1.00 71.17           C  
ANISOU 2153  CG  GLU A 271     9260   8822   8959  -1484   1727  -1439       C  
ATOM   2154  CD  GLU A 271      60.188  38.888  90.631  1.00 77.74           C  
ANISOU 2154  CD  GLU A 271    10135   9607   9794  -1548   1782  -1267       C  
ATOM   2155  OE1 GLU A 271      59.371  38.709  89.700  1.00 91.45           O  
ANISOU 2155  OE1 GLU A 271    11691  11283  11771  -1502   1844  -1323       O  
ATOM   2156  OE2 GLU A 271      60.702  37.964  91.304  1.00 67.03           O  
ANISOU 2156  OE2 GLU A 271     8993   8265   8212  -1637   1746  -1081       O  
ATOM   2157  N   GLU A 272      62.926  41.304  94.685  1.00 77.08           N  
ANISOU 2157  N   GLU A 272    10599   9884   8803  -1637   1518  -1512       N  
ATOM   2158  CA  GLU A 272      63.027  41.410  96.128  1.00 90.65           C  
ANISOU 2158  CA  GLU A 272    12545  11768  10131  -1744   1572  -1584       C  
ATOM   2159  C   GLU A 272      63.238  42.812  96.548  1.00 88.68           C  
ANISOU 2159  C   GLU A 272    12246  11580   9869  -1669   1444  -1822       C  
ATOM   2160  O   GLU A 272      62.895  43.157  97.651  1.00 89.44           O  
ANISOU 2160  O   GLU A 272    12548  11805   9629  -1711   1378  -1870       O  
ATOM   2161  CB  GLU A 272      64.280  40.773  96.678  1.00107.84           C  
ANISOU 2161  CB  GLU A 272    15030  13951  11995  -1799   1441  -1301       C  
ATOM   2162  CG  GLU A 272      64.510  39.334  96.491  1.00122.40           C  
ANISOU 2162  CG  GLU A 272    16926  15701  13881  -1663   1075  -1180       C  
ATOM   2163  CD  GLU A 272      65.897  38.999  96.981  1.00132.67           C  
ANISOU 2163  CD  GLU A 272    18424  17121  14864  -1653    905  -1273       C  
ATOM   2164  OE1 GLU A 272      66.466  39.863  97.681  1.00132.09           O  
ANISOU 2164  OE1 GLU A 272    18320  16977  14891  -1526    608  -1285       O  
ATOM   2165  OE2 GLU A 272      66.427  37.912  96.664  1.00136.08           O  
ANISOU 2165  OE2 GLU A 272    19037  17722  14947  -1772   1076  -1351       O  
ATOM   2166  N   ASN A 273      63.910  43.611  95.750  1.00 80.24           N  
ANISOU 2166  N   ASN A 273    10908  10413   9166  -1555   1408  -1976       N  
ATOM   2167  CA  ASN A 273      64.176  44.958  96.227  1.00 76.73           C  
ANISOU 2167  CA  ASN A 273    10371   9981   8803  -1477   1287  -2209       C  
ATOM   2168  C   ASN A 273      63.525  46.081  95.485  1.00 82.75           C  
ANISOU 2168  C   ASN A 273    10841  10660   9942  -1410   1389  -2427       C  
ATOM   2169  O   ASN A 273      63.643  47.208  95.877  1.00 92.04           O  
ANISOU 2169  O   ASN A 273    11916  11853  11203  -1373   1358  -2674       O  
ATOM   2170  CB  ASN A 273      65.654  45.221  96.264  1.00 72.98           C  
ANISOU 2170  CB  ASN A 273     9917   9392   8420  -1361    978  -2089       C  
ATOM   2171  CG  ASN A 273      66.380  44.119  96.865  1.00 75.62           C  
ANISOU 2171  CG  ASN A 273    10496   9839   8399  -1383    801  -2082       C  
ATOM   2172  OD1 ASN A 273      67.314  44.313  97.601  1.00 86.91           O  
ANISOU 2172  OD1 ASN A 273    11960  11397   9666  -1403    806  -2320       O  
ATOM   2173  ND2 ASN A 273      65.935  42.923  96.591  1.00 73.20           N  
ANISOU 2173  ND2 ASN A 273    10358   9481   7972  -1370    621  -1823       N  
ATOM   2174  N   PHE A 274      62.837  45.793  94.409  1.00 78.71           N  
ANISOU 2174  N   PHE A 274    10192  10046   9667  -1385   1488  -2340       N  
ATOM   2175  CA  PHE A 274      62.238  46.866  93.616  1.00 78.94           C  
ANISOU 2175  CA  PHE A 274     9961   9968  10065  -1299   1547  -2510       C  
ATOM   2176  C   PHE A 274      60.818  46.525  93.188  1.00 86.97           C  
ANISOU 2176  C   PHE A 274    10876  10990  11178  -1345   1757  -2550       C  
ATOM   2177  O   PHE A 274      60.087  47.379  92.700  1.00 96.92           O  
ANISOU 2177  O   PHE A 274    11928  12180  12718  -1283   1818  -2729       O  
ATOM   2178  CB  PHE A 274      63.110  47.198  92.402  1.00 80.60           C  
ANISOU 2178  CB  PHE A 274    10069   9984  10570  -1151   1360  -2369       C  
ATOM   2179  CG  PHE A 274      64.462  47.766  92.767  1.00 91.36           C  
ANISOU 2179  CG  PHE A 274    11460  11309  11944  -1101   1170  -2399       C  
ATOM   2180  CD1 PHE A 274      64.705  49.127  92.684  1.00 89.52           C  
ANISOU 2180  CD1 PHE A 274    11060  10981  11973  -1028   1136  -2597       C  
ATOM   2181  CD2 PHE A 274      65.483  46.939  93.215  1.00 93.17           C  
ANISOU 2181  CD2 PHE A 274    11871  11580  11950  -1123   1017  -2247       C  
ATOM   2182  CE1 PHE A 274      65.941  49.647  93.024  1.00 89.14           C  
ANISOU 2182  CE1 PHE A 274    11010  10884  11977   -987    968  -2654       C  
ATOM   2183  CE2 PHE A 274      66.717  47.457  93.561  1.00 91.48           C  
ANISOU 2183  CE2 PHE A 274    11656  11323  11781  -1070    828  -2313       C  
ATOM   2184  CZ  PHE A 274      66.945  48.811  93.463  1.00 90.68           C  
ANISOU 2184  CZ  PHE A 274    11371  11130  11953  -1006    812  -2523       C  
ATOM   2185  N   GLY A 275      60.425  45.273  93.385  1.00 86.59           N  
ANISOU 2185  N   GLY A 275    10968  11012  10922  -1450   1857  -2394       N  
ATOM   2186  CA  GLY A 275      59.064  44.851  93.117  1.00 86.86           C  
ANISOU 2186  CA  GLY A 275    10898  11056  11047  -1516   2074  -2461       C  
ATOM   2187  C   GLY A 275      58.829  44.144  91.792  1.00 87.13           C  
ANISOU 2187  C   GLY A 275    10848  10959  11300  -1433   2014  -2278       C  
ATOM   2188  O   GLY A 275      59.765  43.754  91.100  1.00 83.90           O  
ANISOU 2188  O   GLY A 275    10497  10463  10917  -1346   1821  -2056       O  
ATOM   2189  N   GLU A 276      57.588  44.045  91.402  1.00 87.92           N  
ANISOU 2189  N   GLU A 276    10797  11047  11563  -1463   2183  -2403       N  
ATOM   2190  CA  GLU A 276      57.243  43.232  90.293  1.00 81.13           C  
ANISOU 2190  CA  GLU A 276     9830  10076  10918  -1381   2134  -2291       C  
ATOM   2191  C   GLU A 276      58.084  43.509  89.093  1.00 71.32           C  
ANISOU 2191  C   GLU A 276     8578   8709   9812  -1202   1875  -2111       C  
ATOM   2192  O   GLU A 276      58.233  44.629  88.677  1.00 63.31           O  
ANISOU 2192  O   GLU A 276     7472   7624   8960  -1082   1772  -2190       O  
ATOM   2193  CB  GLU A 276      55.812  43.596  89.939  1.00 92.49           C  
ANISOU 2193  CB  GLU A 276    11018  11480  12643  -1350   2261  -2560       C  
ATOM   2194  CG  GLU A 276      55.246  42.930  88.738  1.00107.18           C  
ANISOU 2194  CG  GLU A 276    12752  13245  14728  -1269   2221  -2507       C  
ATOM   2195  CD  GLU A 276      54.468  41.717  89.099  1.00117.42           C  
ANISOU 2195  CD  GLU A 276    14050  14593  15972  -1436   2446  -2528       C  
ATOM   2196  OE1 GLU A 276      53.960  41.671  90.229  1.00114.02           O  
ANISOU 2196  OE1 GLU A 276    13591  14251  15481  -1591   2697  -2729       O  
ATOM   2197  OE2 GLU A 276      54.366  40.813  88.257  1.00118.40           O  
ANISOU 2197  OE2 GLU A 276    14196  14662  16130  -1418   2387  -2354       O  
ATOM   2198  N   VAL A 277      58.621  42.442  88.520  1.00 69.14           N  
ANISOU 2198  N   VAL A 277     8395   8396   9479  -1189   1783  -1870       N  
ATOM   2199  CA  VAL A 277      59.303  42.522  87.240  1.00 57.70           C  
ANISOU 2199  CA  VAL A 277     6906   6834   8182  -1026   1586  -1726       C  
ATOM   2200  C   VAL A 277      58.439  41.824  86.228  1.00 53.39           C  
ANISOU 2200  C   VAL A 277     6247   6240   7797   -969   1599  -1716       C  
ATOM   2201  O   VAL A 277      58.066  40.669  86.431  1.00 61.51           O  
ANISOU 2201  O   VAL A 277     7315   7299   8758  -1067   1682  -1656       O  
ATOM   2202  CB  VAL A 277      60.633  41.793  87.239  1.00 52.76           C  
ANISOU 2202  CB  VAL A 277     6442   6195   7408  -1032   1446  -1488       C  
ATOM   2203  CG1 VAL A 277      61.205  41.781  85.809  1.00 41.94           C  
ANISOU 2203  CG1 VAL A 277     5014   4716   6204   -876   1292  -1361       C  
ATOM   2204  CG2 VAL A 277      61.591  42.430  88.230  1.00 46.23           C  
ANISOU 2204  CG2 VAL A 277     5724   5410   6430  -1072   1392  -1510       C  
ATOM   2205  N   ASP A 278      58.108  42.515  85.144  1.00 44.97           N  
ANISOU 2205  N   ASP A 278     5046   5090   6949   -808   1509  -1777       N  
ATOM   2206  CA  ASP A 278      57.393  41.856  84.066  1.00 52.06           C  
ANISOU 2206  CA  ASP A 278     5843   5946   7993   -721   1469  -1773       C  
ATOM   2207  C   ASP A 278      58.416  41.174  83.166  1.00 63.74           C  
ANISOU 2207  C   ASP A 278     7413   7387   9420   -644   1318  -1539       C  
ATOM   2208  O   ASP A 278      59.090  41.818  82.353  1.00 55.67           O  
ANISOU 2208  O   ASP A 278     6407   6302   8443   -513   1191  -1457       O  
ATOM   2209  CB  ASP A 278      56.531  42.816  83.254  1.00 56.66           C  
ANISOU 2209  CB  ASP A 278     6259   6456   8813   -563   1409  -1940       C  
ATOM   2210  CG  ASP A 278      55.810  42.113  82.114  1.00 84.59           C  
ANISOU 2210  CG  ASP A 278     9696   9958  12488   -453   1330  -1956       C  
ATOM   2211  OD1 ASP A 278      55.810  42.664  81.000  1.00 93.68           O  
ANISOU 2211  OD1 ASP A 278    10815  11036  13744   -266   1171  -1933       O  
ATOM   2212  OD2 ASP A 278      55.267  40.997  82.320  1.00 96.56           O  
ANISOU 2212  OD2 ASP A 278    11173  11512  14004   -550   1424  -1987       O  
ATOM   2213  N   ARG A 279      58.523  39.861  83.330  1.00 65.29           N  
ANISOU 2213  N   ARG A 279     7666   7611   9532   -735   1346  -1436       N  
ATOM   2214  CA  ARG A 279      59.530  39.072  82.648  1.00 54.10           C  
ANISOU 2214  CA  ARG A 279     6326   6163   8068   -687   1217  -1238       C  
ATOM   2215  C   ARG A 279      59.443  39.162  81.113  1.00 50.24           C  
ANISOU 2215  C   ARG A 279     5754   5624   7712   -502   1091  -1228       C  
ATOM   2216  O   ARG A 279      60.453  39.249  80.415  1.00 51.89           O  
ANISOU 2216  O   ARG A 279     6021   5802   7891   -420    984  -1098       O  
ATOM   2217  CB  ARG A 279      59.439  37.648  83.164  1.00 40.59           C  
ANISOU 2217  CB  ARG A 279     4668   4468   6285   -821   1277  -1159       C  
ATOM   2218  CG  ARG A 279      59.758  37.592  84.634  1.00 44.78           C  
ANISOU 2218  CG  ARG A 279     5345   5050   6620   -988   1371  -1118       C  
ATOM   2219  CD  ARG A 279      58.887  36.617  85.378  1.00 54.49           C  
ANISOU 2219  CD  ARG A 279     6593   6302   7809  -1149   1543  -1136       C  
ATOM   2220  NE  ARG A 279      59.160  36.675  86.806  1.00 73.59           N  
ANISOU 2220  NE  ARG A 279     9187   8786   9986  -1303   1639  -1095       N  
ATOM   2221  CZ  ARG A 279      59.887  35.777  87.463  1.00 87.41           C  
ANISOU 2221  CZ  ARG A 279    11127  10527  11558  -1395   1597   -901       C  
ATOM   2222  NH1 ARG A 279      60.091  35.920  88.767  1.00 83.10           N  
ANISOU 2222  NH1 ARG A 279    10763  10055  10756  -1519   1670   -874       N  
ATOM   2223  NH2 ARG A 279      60.413  34.736  86.816  1.00 90.51           N  
ANISOU 2223  NH2 ARG A 279    11529  10834  12025  -1355   1467   -743       N  
ATOM   2224  N   PHE A 280      58.241  39.190  80.578  1.00 38.95           N  
ANISOU 2224  N   PHE A 280     4188   4188   6425   -431   1103  -1380       N  
ATOM   2225  CA  PHE A 280      58.129  39.367  79.149  1.00 48.61           C  
ANISOU 2225  CA  PHE A 280     5360   5376   7734   -238    960  -1377       C  
ATOM   2226  C   PHE A 280      58.889  40.622  78.696  1.00 60.49           C  
ANISOU 2226  C   PHE A 280     6940   6833   9210   -129    884  -1294       C  
ATOM   2227  O   PHE A 280      59.623  40.572  77.709  1.00 66.64           O  
ANISOU 2227  O   PHE A 280     7783   7592   9946    -27    791  -1165       O  
ATOM   2228  CB  PHE A 280      56.670  39.394  78.726  1.00 36.98           C  
ANISOU 2228  CB  PHE A 280     3720   3894   6438   -158    953  -1590       C  
ATOM   2229  CG  PHE A 280      56.464  39.462  77.243  1.00 43.10           C  
ANISOU 2229  CG  PHE A 280     4459   4644   7272     56    776  -1597       C  
ATOM   2230  CD1 PHE A 280      56.944  38.464  76.418  1.00 44.80           C  
ANISOU 2230  CD1 PHE A 280     4705   4884   7434    105    695  -1503       C  
ATOM   2231  CD2 PHE A 280      55.747  40.509  76.673  1.00 54.24           C  
ANISOU 2231  CD2 PHE A 280     5809   6008   8793    218    679  -1712       C  
ATOM   2232  CE1 PHE A 280      56.737  38.510  75.043  1.00 46.24           C  
ANISOU 2232  CE1 PHE A 280     4872   5066   7630    309    531  -1524       C  
ATOM   2233  CE2 PHE A 280      55.533  40.554  75.305  1.00 56.74           C  
ANISOU 2233  CE2 PHE A 280     6126   6310   9124    429    496  -1710       C  
ATOM   2234  CZ  PHE A 280      56.031  39.554  74.493  1.00 52.61           C  
ANISOU 2234  CZ  PHE A 280     5648   5834   8506    472    428  -1618       C  
ATOM   2235  N   TYR A 281      58.733  41.732  79.418  1.00 48.66           N  
ANISOU 2235  N   TYR A 281     5432   5311   7744   -160    941  -1373       N  
ATOM   2236  CA  TYR A 281      59.473  42.960  79.097  1.00 49.34           C  
ANISOU 2236  CA  TYR A 281     5582   5323   7841    -76    887  -1295       C  
ATOM   2237  C   TYR A 281      60.979  42.887  79.390  1.00 52.08           C  
ANISOU 2237  C   TYR A 281     6048   5664   8075   -149    893  -1127       C  
ATOM   2238  O   TYR A 281      61.791  43.504  78.699  1.00 40.79           O  
ANISOU 2238  O   TYR A 281     4675   4165   6657    -69    847  -1014       O  
ATOM   2239  CB  TYR A 281      58.843  44.202  79.766  1.00 50.25           C  
ANISOU 2239  CB  TYR A 281     5624   5396   8074    -79    934  -1459       C  
ATOM   2240  CG  TYR A 281      57.820  44.807  78.860  1.00 51.01           C  
ANISOU 2240  CG  TYR A 281     5630   5422   8331     94    838  -1560       C  
ATOM   2241  CD1 TYR A 281      58.165  45.794  77.964  1.00 52.22           C  
ANISOU 2241  CD1 TYR A 281     5841   5465   8537    247    732  -1459       C  
ATOM   2242  CD2 TYR A 281      56.518  44.333  78.849  1.00 48.85           C  
ANISOU 2242  CD2 TYR A 281     5215   5181   8164    110    845  -1751       C  
ATOM   2243  CE1 TYR A 281      57.224  46.311  77.098  1.00 63.47           C  
ANISOU 2243  CE1 TYR A 281     7208   6816  10093    426    605  -1534       C  
ATOM   2244  CE2 TYR A 281      55.577  44.841  77.999  1.00 42.77           C  
ANISOU 2244  CE2 TYR A 281     4353   4340   7556    288    716  -1862       C  
ATOM   2245  CZ  TYR A 281      55.926  45.822  77.116  1.00 54.20           C  
ANISOU 2245  CZ  TYR A 281     5883   5682   9030    456    579  -1746       C  
ATOM   2246  OH  TYR A 281      54.974  46.319  76.250  1.00 63.19           O  
ANISOU 2246  OH  TYR A 281     6953   6740  10317    654    412  -1846       O  
ATOM   2247  N   ALA A 282      61.335  42.134  80.422  1.00 53.70           N  
ANISOU 2247  N   ALA A 282     6291   5933   8179   -300    951  -1117       N  
ATOM   2248  CA  ALA A 282      62.715  42.007  80.837  1.00 44.97           C  
ANISOU 2248  CA  ALA A 282     5280   4818   6987   -367    928   -995       C  
ATOM   2249  C   ALA A 282      63.472  41.257  79.760  1.00 57.21           C  
ANISOU 2249  C   ALA A 282     6861   6348   8527   -301    853   -853       C  
ATOM   2250  O   ALA A 282      64.590  41.613  79.413  1.00 63.13           O  
ANISOU 2250  O   ALA A 282     7652   7045   9290   -275    824   -763       O  
ATOM   2251  CB  ALA A 282      62.794  41.273  82.140  1.00 37.29           C  
ANISOU 2251  CB  ALA A 282     4362   3916   5889   -524    975  -1010       C  
ATOM   2252  N   VAL A 283      62.848  40.215  79.229  1.00 62.99           N  
ANISOU 2252  N   VAL A 283     7556   7119   9257   -277    835   -857       N  
ATOM   2253  CA  VAL A 283      63.456  39.398  78.189  1.00 59.28           C  
ANISOU 2253  CA  VAL A 283     7098   6646   8780   -213    767   -761       C  
ATOM   2254  C   VAL A 283      63.563  40.165  76.876  1.00 62.06           C  
ANISOU 2254  C   VAL A 283     7459   6962   9159    -57    733   -724       C  
ATOM   2255  O   VAL A 283      64.507  39.984  76.110  1.00 64.25           O  
ANISOU 2255  O   VAL A 283     7777   7223   9411    -17    713   -628       O  
ATOM   2256  CB  VAL A 283      62.626  38.117  77.942  1.00 52.00           C  
ANISOU 2256  CB  VAL A 283     6110   5768   7879   -220    752   -810       C  
ATOM   2257  CG1 VAL A 283      62.816  37.634  76.541  1.00 59.89           C  
ANISOU 2257  CG1 VAL A 283     7088   6775   8893    -92    676   -781       C  
ATOM   2258  CG2 VAL A 283      63.013  37.050  78.895  1.00 23.05           C  
ANISOU 2258  CG2 VAL A 283     2478   2109   4171   -365    766   -760       C  
ATOM   2259  N   LEU A 284      62.576  41.006  76.604  1.00 56.96           N  
ANISOU 2259  N   LEU A 284     6782   6298   8564     31    728   -802       N  
ATOM   2260  CA  LEU A 284      62.533  41.692  75.330  1.00 48.86           C  
ANISOU 2260  CA  LEU A 284     5797   5231   7538    194    676   -748       C  
ATOM   2261  C   LEU A 284      63.681  42.670  75.278  1.00 57.53           C  
ANISOU 2261  C   LEU A 284     6977   6244   8637    183    725   -628       C  
ATOM   2262  O   LEU A 284      64.228  42.950  74.206  1.00 62.41           O  
ANISOU 2262  O   LEU A 284     7671   6828   9213    272    724   -516       O  
ATOM   2263  CB  LEU A 284      61.191  42.379  75.111  1.00 39.41           C  
ANISOU 2263  CB  LEU A 284     4543   4011   6421    304    625   -868       C  
ATOM   2264  CG  LEU A 284      60.017  41.508  74.634  1.00 42.47           C  
ANISOU 2264  CG  LEU A 284     4835   4461   6839    378    548  -1000       C  
ATOM   2265  CD1 LEU A 284      58.749  42.338  74.446  1.00 45.47           C  
ANISOU 2265  CD1 LEU A 284     5140   4795   7341    500    475  -1144       C  
ATOM   2266  CD2 LEU A 284      60.372  40.806  73.327  1.00 47.66           C  
ANISOU 2266  CD2 LEU A 284     5546   5164   7399    492    465   -924       C  
ATOM   2267  N   HIS A 285      64.055  43.159  76.457  1.00 55.26           N  
ANISOU 2267  N   HIS A 285     6673   5924   8398     67    780   -663       N  
ATOM   2268  CA  HIS A 285      65.200  44.050  76.611  1.00 56.36           C  
ANISOU 2268  CA  HIS A 285     6855   5970   8589     32    830   -587       C  
ATOM   2269  C   HIS A 285      66.464  43.416  76.062  1.00 54.57           C  
ANISOU 2269  C   HIS A 285     6668   5743   8323      8    847   -477       C  
ATOM   2270  O   HIS A 285      67.353  44.098  75.573  1.00 61.25           O  
ANISOU 2270  O   HIS A 285     7552   6500   9220     23    905   -393       O  
ATOM   2271  CB  HIS A 285      65.412  44.398  78.082  1.00 55.20           C  
ANISOU 2271  CB  HIS A 285     6671   5820   8482    -94    858   -683       C  
ATOM   2272  CG  HIS A 285      64.837  45.720  78.482  1.00 52.62           C  
ANISOU 2272  CG  HIS A 285     6308   5420   8266    -68    881   -774       C  
ATOM   2273  ND1 HIS A 285      65.515  46.904  78.309  1.00 51.92           N  
ANISOU 2273  ND1 HIS A 285     6231   5197   8299    -44    912   -731       N  
ATOM   2274  CD2 HIS A 285      63.656  46.036  79.064  1.00 51.51           C  
ANISOU 2274  CD2 HIS A 285     6102   5309   8162    -67    884   -925       C  
ATOM   2275  CE1 HIS A 285      64.771  47.900  78.767  1.00 56.57           C  
ANISOU 2275  CE1 HIS A 285     6765   5731   8998    -21    915   -849       C  
ATOM   2276  NE2 HIS A 285      63.642  47.403  79.222  1.00 55.90           N  
ANISOU 2276  NE2 HIS A 285     6629   5749   8862    -33    899   -976       N  
ATOM   2277  N   VAL A 286      66.544  42.100  76.162  1.00 50.16           N  
ANISOU 2277  N   VAL A 286     6087   5271   7701    -36    807   -490       N  
ATOM   2278  CA  VAL A 286      67.687  41.378  75.649  1.00 43.57           C  
ANISOU 2278  CA  VAL A 286     5261   4437   6858    -55    812   -422       C  
ATOM   2279  C   VAL A 286      67.469  41.000  74.192  1.00 42.87           C  
ANISOU 2279  C   VAL A 286     5202   4388   6699     63    811   -375       C  
ATOM   2280  O   VAL A 286      68.263  41.353  73.343  1.00 58.15           O  
ANISOU 2280  O   VAL A 286     7184   6284   8627     98    877   -297       O  
ATOM   2281  CB  VAL A 286      67.989  40.162  76.517  1.00 36.76           C  
ANISOU 2281  CB  VAL A 286     4362   3621   5985   -158    750   -458       C  
ATOM   2282  CG1 VAL A 286      69.229  39.438  76.009  1.00 33.60           C  
ANISOU 2282  CG1 VAL A 286     3942   3202   5623   -173    738   -417       C  
ATOM   2283  CG2 VAL A 286      68.155  40.614  77.962  1.00 27.65           C  
ANISOU 2283  CG2 VAL A 286     3213   2445   4848   -261    741   -506       C  
ATOM   2284  N   PHE A 287      66.370  40.319  73.900  1.00 53.51           N  
ANISOU 2284  N   PHE A 287     6523   5814   7995    124    743   -436       N  
ATOM   2285  CA  PHE A 287      66.068  39.899  72.537  1.00 54.65           C  
ANISOU 2285  CA  PHE A 287     6693   6017   8055    253    710   -425       C  
ATOM   2286  C   PHE A 287      66.249  41.076  71.613  1.00 46.67           C  
ANISOU 2286  C   PHE A 287     5793   4955   6983    363    753   -327       C  
ATOM   2287  O   PHE A 287      66.865  40.960  70.569  1.00 54.81           O  
ANISOU 2287  O   PHE A 287     6893   6016   7918    430    786   -265       O  
ATOM   2288  CB  PHE A 287      64.643  39.369  72.441  1.00 56.83           C  
ANISOU 2288  CB  PHE A 287     6908   6358   8327    323    616   -538       C  
ATOM   2289  CG  PHE A 287      64.455  37.995  72.973  1.00 48.07           C  
ANISOU 2289  CG  PHE A 287     5702   5298   7266    239    581   -618       C  
ATOM   2290  CD1 PHE A 287      65.526  37.162  73.166  1.00 37.92           C  
ANISOU 2290  CD1 PHE A 287     4401   4008   5999    152    594   -579       C  
ATOM   2291  CD2 PHE A 287      63.178  37.518  73.239  1.00 52.24           C  
ANISOU 2291  CD2 PHE A 287     6143   5857   7847    251    534   -740       C  
ATOM   2292  CE1 PHE A 287      65.337  35.880  73.647  1.00 44.44           C  
ANISOU 2292  CE1 PHE A 287     5149   4850   6886     78    549   -633       C  
ATOM   2293  CE2 PHE A 287      62.978  36.240  73.712  1.00 41.33           C  
ANISOU 2293  CE2 PHE A 287     4679   4496   6530    164    520   -798       C  
ATOM   2294  CZ  PHE A 287      64.057  35.416  73.919  1.00 38.28           C  
ANISOU 2294  CZ  PHE A 287     4299   4094   6151     79    522   -731       C  
ATOM   2295  N   LEU A 288      65.711  42.211  71.977  1.00 45.32           N  
ANISOU 2295  N   LEU A 288     5647   4705   6869    381    758   -316       N  
ATOM   2296  CA  LEU A 288      65.641  43.345  71.070  1.00 55.84           C  
ANISOU 2296  CA  LEU A 288     7099   5964   8155    508    768   -214       C  
ATOM   2297  C   LEU A 288      66.767  44.350  70.958  1.00 57.07           C  
ANISOU 2297  C   LEU A 288     7338   5996   8350    459    909    -71       C  
ATOM   2298  O   LEU A 288      66.625  45.328  70.283  1.00 59.54           O  
ANISOU 2298  O   LEU A 288     7773   6223   8627    555    931     46       O  
ATOM   2299  CB  LEU A 288      64.355  44.104  71.308  1.00 51.77           C  
ANISOU 2299  CB  LEU A 288     6552   5397   7723    574    683   -289       C  
ATOM   2300  CG  LEU A 288      63.080  43.301  71.268  1.00 48.04           C  
ANISOU 2300  CG  LEU A 288     6068   4982   7203    734    532   -377       C  
ATOM   2301  CD1 LEU A 288      61.990  44.178  71.635  1.00 45.64           C  
ANISOU 2301  CD1 LEU A 288     5735   4816   6789    770    476   -434       C  
ATOM   2302  CD2 LEU A 288      62.836  42.708  69.947  1.00 50.87           C  
ANISOU 2302  CD2 LEU A 288     6290   5323   7714    703    484   -549       C  
ATOM   2303  N   GLU A 289      67.868  44.145  71.634  1.00 46.57           N  
ANISOU 2303  N   GLU A 289     5943   4640   7111    314    996    -83       N  
ATOM   2304  CA  GLU A 289      68.931  45.097  71.572  1.00 41.67           C  
ANISOU 2304  CA  GLU A 289     5362   3883   6587    253   1141     15       C  
ATOM   2305  C   GLU A 289      69.388  45.301  70.167  1.00 47.18           C  
ANISOU 2305  C   GLU A 289     6202   4558   7168    324   1254    167       C  
ATOM   2306  O   GLU A 289      69.394  44.388  69.395  1.00 48.15           O  
ANISOU 2306  O   GLU A 289     6360   4802   7134    374   1244    167       O  
ATOM   2307  CB  GLU A 289      70.112  44.574  72.343  1.00 45.65           C  
ANISOU 2307  CB  GLU A 289     5758   4381   7206    107   1187    -53       C  
ATOM   2308  CG  GLU A 289      70.047  44.762  73.788  1.00 53.77           C  
ANISOU 2308  CG  GLU A 289     6696   5355   8378     14   1146   -151       C  
ATOM   2309  CD  GLU A 289      71.310  44.390  74.434  1.00 53.98           C  
ANISOU 2309  CD  GLU A 289     6632   5362   8515   -106   1161   -214       C  
ATOM   2310  OE1 GLU A 289      71.591  44.857  75.523  1.00 45.57           O  
ANISOU 2310  OE1 GLU A 289     5505   4260   7550   -178   1115   -302       O  
ATOM   2311  OE2 GLU A 289      72.022  43.592  73.858  1.00 60.45           O  
ANISOU 2311  OE2 GLU A 289     7438   6205   9327   -121   1208   -193       O  
ATOM   2312  N   PHE A 290      69.767  46.531  69.865  1.00 40.69           N  
ANISOU 2312  N   PHE A 290     5462   3574   6424    320   1372    290       N  
ATOM   2313  CA  PHE A 290      70.371  46.960  68.603  1.00 43.50           C  
ANISOU 2313  CA  PHE A 290     5980   3874   6674    356   1535    466       C  
ATOM   2314  C   PHE A 290      69.435  46.826  67.427  1.00 52.48           C  
ANISOU 2314  C   PHE A 290     7291   5101   7549    533   1444    556       C  
ATOM   2315  O   PHE A 290      69.860  46.647  66.295  1.00 56.17           O  
ANISOU 2315  O   PHE A 290     7899   5614   7830    572   1553    663       O  
ATOM   2316  CB  PHE A 290      71.701  46.249  68.346  1.00 38.03           C  
ANISOU 2316  CB  PHE A 290     5228   3220   6002    241   1697    439       C  
ATOM   2317  CG  PHE A 290      72.729  46.551  69.374  1.00 47.45           C  
ANISOU 2317  CG  PHE A 290     6264   4294   7472     85   1779    356       C  
ATOM   2318  CD1 PHE A 290      73.059  45.610  70.340  1.00 38.89           C  
ANISOU 2318  CD1 PHE A 290     5008   3286   6484      5   1676    184       C  
ATOM   2319  CD2 PHE A 290      73.318  47.803  69.425  1.00 65.48           C  
ANISOU 2319  CD2 PHE A 290     8571   6375   9934     28   1937    444       C  
ATOM   2320  CE1 PHE A 290      73.981  45.894  71.320  1.00 40.69           C  
ANISOU 2320  CE1 PHE A 290     5097   3408   6957   -117   1708     89       C  
ATOM   2321  CE2 PHE A 290      74.259  48.097  70.401  1.00 75.20           C  
ANISOU 2321  CE2 PHE A 290     9635   7493  11446   -105   1989    330       C  
ATOM   2322  CZ  PHE A 290      74.589  47.138  71.353  1.00 65.56           C  
ANISOU 2322  CZ  PHE A 290     8248   6368  10295   -170   1860    145       C  
ATOM   2323  N   TYR A 291      68.145  46.934  67.705  1.00 61.71           N  
ANISOU 2323  N   TYR A 291     8447   6294   8705    644   1242    493       N  
ATOM   2324  CA  TYR A 291      67.143  46.911  66.656  1.00 66.60           C  
ANISOU 2324  CA  TYR A 291     9219   6980   9106    839   1102    551       C  
ATOM   2325  C   TYR A 291      67.078  48.254  65.940  1.00 65.89           C  
ANISOU 2325  C   TYR A 291     9343   6716   8975    932   1148    773       C  
ATOM   2326  O   TYR A 291      66.997  49.313  66.577  1.00 60.98           O  
ANISOU 2326  O   TYR A 291     8693   5912   8564    901   1159    808       O  
ATOM   2327  CB  TYR A 291      65.782  46.596  67.255  1.00 64.91           C  
ANISOU 2327  CB  TYR A 291     8882   6828   8952    921    872    375       C  
ATOM   2328  CG  TYR A 291      65.325  45.175  67.088  1.00 57.36           C  
ANISOU 2328  CG  TYR A 291     7835   6070   7891    954    761    217       C  
ATOM   2329  CD1 TYR A 291      64.091  44.899  66.541  1.00 52.90           C  
ANISOU 2329  CD1 TYR A 291     7287   5582   7231   1130    557    134       C  
ATOM   2330  CD2 TYR A 291      66.118  44.110  67.483  1.00 53.66           C  
ANISOU 2330  CD2 TYR A 291     7246   5693   7448    817    845    135       C  
ATOM   2331  CE1 TYR A 291      63.659  43.614  66.390  1.00 56.56           C  
ANISOU 2331  CE1 TYR A 291     7645   6207   7640   1157    460    -29       C  
ATOM   2332  CE2 TYR A 291      65.686  42.808  67.331  1.00 45.22           C  
ANISOU 2332  CE2 TYR A 291     6085   4778   6319    845    742    -10       C  
ATOM   2333  CZ  TYR A 291      64.456  42.574  66.787  1.00 49.92           C  
ANISOU 2333  CZ  TYR A 291     6691   5444   6831   1010    560    -94       C  
ATOM   2334  OH  TYR A 291      63.999  41.300  66.621  1.00 55.94           O  
ANISOU 2334  OH  TYR A 291     7342   6342   7570   1039    460   -255       O  
ATOM   2335  N   ASP A 292      67.113  48.211  64.614  1.00 64.32           N  
ANISOU 2335  N   ASP A 292     9369   6568   8500   1047   1170    923       N  
ATOM   2336  CA  ASP A 292      66.889  49.420  63.832  1.00 73.81           C  
ANISOU 2336  CA  ASP A 292    10823   7605   9615   1165   1175   1164       C  
ATOM   2337  C   ASP A 292      65.484  49.966  64.118  1.00 75.50           C  
ANISOU 2337  C   ASP A 292    11017   7748   9920   1332    890   1103       C  
ATOM   2338  O   ASP A 292      64.647  49.282  64.714  1.00 69.85           O  
ANISOU 2338  O   ASP A 292    10111   7148   9279   1364    708    871       O  
ATOM   2339  CB  ASP A 292      67.090  49.166  62.331  1.00 67.12           C  
ANISOU 2339  CB  ASP A 292    10252   6861   8389   1275   1231   1330       C  
ATOM   2340  CG  ASP A 292      66.097  48.164  61.765  1.00 63.99           C  
ANISOU 2340  CG  ASP A 292     9862   6690   7761   1455    973   1181       C  
ATOM   2341  OD1 ASP A 292      66.059  47.033  62.270  1.00 69.80           O  
ANISOU 2341  OD1 ASP A 292    10374   7584   8562   1391    927    950       O  
ATOM   2342  OD2 ASP A 292      65.363  48.491  60.805  1.00 62.80           O  
ANISOU 2342  OD2 ASP A 292     9941   6550   7370   1665    805   1290       O  
ATOM   2343  N   ASP A 293      65.233  51.200  63.699  1.00 74.55           N  
ANISOU 2343  N   ASP A 293    11085   7422   9818   1431    860   1306       N  
ATOM   2344  CA  ASP A 293      63.955  51.838  63.966  1.00 75.66           C  
ANISOU 2344  CA  ASP A 293    11193   7458  10097   1593    587   1239       C  
ATOM   2345  C   ASP A 293      62.797  51.078  63.329  1.00 70.12           C  
ANISOU 2345  C   ASP A 293    10518   6934   9189   1806    298   1112       C  
ATOM   2346  O   ASP A 293      61.755  50.879  63.943  1.00 70.70           O  
ANISOU 2346  O   ASP A 293    10396   7036   9431   1871     90    880       O  
ATOM   2347  CB  ASP A 293      63.970  53.283  63.474  1.00 85.09           C  
ANISOU 2347  CB  ASP A 293    12617   8374  11339   1678    597   1512       C  
ATOM   2348  CG  ASP A 293      64.135  54.276  64.603  1.00 93.10           C  
ANISOU 2348  CG  ASP A 293    13457   9157  12759   1558    668   1464       C  
ATOM   2349  OD1 ASP A 293      64.819  55.306  64.415  1.00102.77           O  
ANISOU 2349  OD1 ASP A 293    14815  10147  14087   1501    837   1691       O  
ATOM   2350  OD2 ASP A 293      63.573  54.025  65.683  1.00 89.14           O  
ANISOU 2350  OD2 ASP A 293    12684   8709  12476   1516    563   1191       O  
ATOM   2351  N   GLU A 294      62.988  50.651  62.094  1.00 63.29           N  
ANISOU 2351  N   GLU A 294     9889   6190   7968   1912    295   1244       N  
ATOM   2352  CA  GLU A 294      61.914  50.028  61.346  1.00 63.67           C  
ANISOU 2352  CA  GLU A 294     9990   6395   7807   2142     -3   1128       C  
ATOM   2353  C   GLU A 294      61.580  48.649  61.890  1.00 66.12           C  
ANISOU 2353  C   GLU A 294    10014   6928   8182   2083    -62    808       C  
ATOM   2354  O   GLU A 294      60.417  48.279  61.998  1.00 74.07           O  
ANISOU 2354  O   GLU A 294    10886   7993   9263   2219   -325    591       O  
ATOM   2355  CB  GLU A 294      62.282  49.941  59.854  1.00 66.19           C  
ANISOU 2355  CB  GLU A 294    10662   6802   7686   2270     22   1351       C  
ATOM   2356  CG  GLU A 294      61.082  49.756  58.944  1.00 83.31           C  
ANISOU 2356  CG  GLU A 294    12963   9059   9631   2571   -349   1288       C  
ATOM   2357  CD  GLU A 294      59.955  50.752  59.252  1.00100.73           C  
ANISOU 2357  CD  GLU A 294    15148  11051  12075   2741   -641   1272       C  
ATOM   2358  OE1 GLU A 294      58.792  50.305  59.365  1.00112.45           O  
ANISOU 2358  OE1 GLU A 294    16461  12609  13655   2897   -947   1004       O  
ATOM   2359  OE2 GLU A 294      60.225  51.971  59.388  1.00 91.03           O  
ANISOU 2359  OE2 GLU A 294    14052   9568  10969   2718   -563   1506       O  
ATOM   2360  N   SER A 295      62.609  47.886  62.228  1.00 68.11           N  
ANISOU 2360  N   SER A 295    10165   7285   8428   1878    182    774       N  
ATOM   2361  CA  SER A 295      62.408  46.515  62.654  1.00 65.77           C  
ANISOU 2361  CA  SER A 295     9629   7184   8178   1816    140    508       C  
ATOM   2362  C   SER A 295      61.733  46.527  63.996  1.00 61.30           C  
ANISOU 2362  C   SER A 295     8788   6557   7947   1735     69    306       C  
ATOM   2363  O   SER A 295      61.095  45.560  64.400  1.00 73.50           O  
ANISOU 2363  O   SER A 295    10132   8221   9574   1730    -35     70       O  
ATOM   2364  CB  SER A 295      63.740  45.767  62.728  1.00 57.62           C  
ANISOU 2364  CB  SER A 295     8556   6245   7092   1618    408    530       C  
ATOM   2365  OG  SER A 295      64.220  45.484  61.422  1.00 49.89           O  
ANISOU 2365  OG  SER A 295     7799   5378   5778   1699    470    645       O  
ATOM   2366  N   TRP A 296      61.885  47.640  64.687  1.00 58.42           N  
ANISOU 2366  N   TRP A 296     8417   6000   7781   1666    141    395       N  
ATOM   2367  CA  TRP A 296      61.257  47.802  65.979  1.00 63.67           C  
ANISOU 2367  CA  TRP A 296     8840   6605   8747   1586     95    201       C  
ATOM   2368  C   TRP A 296      59.763  48.030  65.830  1.00 73.99           C  
ANISOU 2368  C   TRP A 296    10088   7886  10138   1785   -183     47       C  
ATOM   2369  O   TRP A 296      58.970  47.373  66.502  1.00 80.14           O  
ANISOU 2369  O   TRP A 296    10641   8743  11065   1759   -262   -207       O  
ATOM   2370  CB  TRP A 296      61.896  48.957  66.733  1.00 67.74           C  
ANISOU 2370  CB  TRP A 296     9356   6924   9460   1460    251    312       C  
ATOM   2371  CG  TRP A 296      60.956  49.578  67.649  1.00 69.36           C  
ANISOU 2371  CG  TRP A 296     9396   7027   9932   1477    140    147       C  
ATOM   2372  CD1 TRP A 296      60.377  50.787  67.512  1.00 72.52           C  
ANISOU 2372  CD1 TRP A 296     9857   7235  10464   1603     24    201       C  
ATOM   2373  CD2 TRP A 296      60.429  49.000  68.852  1.00 66.64           C  
ANISOU 2373  CD2 TRP A 296     8796   6765   9761   1364    135   -117       C  
ATOM   2374  NE1 TRP A 296      59.530  51.018  68.561  1.00 78.87           N  
ANISOU 2374  NE1 TRP A 296    10434   8002  11532   1575    -49    -41       N  
ATOM   2375  CE2 TRP A 296      59.543  49.946  69.387  1.00 71.55           C  
ANISOU 2375  CE2 TRP A 296     9321   7247  10616   1425     32   -232       C  
ATOM   2376  CE3 TRP A 296      60.627  47.797  69.511  1.00 61.45           C  
ANISOU 2376  CE3 TRP A 296     7993   6271   9083   1219    214   -257       C  
ATOM   2377  CZ2 TRP A 296      58.858  49.703  70.580  1.00 67.86           C  
ANISOU 2377  CZ2 TRP A 296     8614   6825  10343   1329     36   -498       C  
ATOM   2378  CZ3 TRP A 296      59.938  47.566  70.686  1.00 53.10           C  
ANISOU 2378  CZ3 TRP A 296     6725   5245   8204   1127    210   -485       C  
ATOM   2379  CH2 TRP A 296      59.069  48.514  71.206  1.00 61.17           C  
ANISOU 2379  CH2 TRP A 296     7656   6150   9437   1177    136   -609       C  
ATOM   2380  N   LYS A 297      59.344  48.863  64.912  1.00 76.88           N  
ANISOU 2380  N   LYS A 297    10657   8128  10425   1982   -330    199       N  
ATOM   2381  CA  LYS A 297      57.938  49.069  64.818  1.00 78.33           C  
ANISOU 2381  CA  LYS A 297    10805   8280  10678   2214   -644     50       C  
ATOM   2382  C   LYS A 297      57.258  47.772  64.507  1.00 72.94           C  
ANISOU 2382  C   LYS A 297     9952   7808   9955   2255   -764   -213       C  
ATOM   2383  O   LYS A 297      56.320  47.413  65.170  1.00 71.22           O  
ANISOU 2383  O   LYS A 297     9475   7604   9982   2232   -842   -485       O  
ATOM   2384  CB  LYS A 297      57.652  50.044  63.698  1.00 90.84           C  
ANISOU 2384  CB  LYS A 297    12710   9783  12021   2459   -821    283       C  
ATOM   2385  CG  LYS A 297      57.903  49.479  62.322  1.00100.67           C  
ANISOU 2385  CG  LYS A 297    14205  10825  13219   2418   -659    624       C  
ATOM   2386  CD  LYS A 297      56.759  49.822  61.361  1.00 98.84           C  
ANISOU 2386  CD  LYS A 297    13904  10331  13320   2458   -754    616       C  
ATOM   2387  CE  LYS A 297      56.801  48.965  60.096  1.00 87.82           C  
ANISOU 2387  CE  LYS A 297    12799   8698  11870   2475   -650    980       C  
ATOM   2388  NZ  LYS A 297      55.480  48.365  59.754  1.00 86.01           N  
ANISOU 2388  NZ  LYS A 297    12506   8192  11983   2554   -794    963       N  
ATOM   2389  N   GLU A 298      57.775  46.983  63.598  1.00 65.75           N  
ANISOU 2389  N   GLU A 298     9181   7056   8744   2306   -759   -143       N  
ATOM   2390  CA  GLU A 298      57.082  45.760  63.277  1.00 56.38           C  
ANISOU 2390  CA  GLU A 298     7852   6056   7513   2377   -899   -390       C  
ATOM   2391  C   GLU A 298      56.922  44.837  64.453  1.00 58.41           C  
ANISOU 2391  C   GLU A 298     7787   6366   8041   2175   -787   -633       C  
ATOM   2392  O   GLU A 298      55.856  44.343  64.682  1.00 75.26           O  
ANISOU 2392  O   GLU A 298     9710   8514  10371   2235   -941   -898       O  
ATOM   2393  CB  GLU A 298      57.842  45.042  62.202  1.00 52.32           C  
ANISOU 2393  CB  GLU A 298     7515   5709   6654   2400   -833   -281       C  
ATOM   2394  CG  GLU A 298      58.387  45.957  61.170  1.00 84.50           C  
ANISOU 2394  CG  GLU A 298    11956   9738  10412   2559   -871      7       C  
ATOM   2395  CD  GLU A 298      59.043  45.201  60.051  1.00111.59           C  
ANISOU 2395  CD  GLU A 298    15559  13368  13474   2606   -821     62       C  
ATOM   2396  OE1 GLU A 298      59.373  44.029  60.273  1.00122.61           O  
ANISOU 2396  OE1 GLU A 298    16768  14919  14898   2498   -744   -121       O  
ATOM   2397  OE2 GLU A 298      59.228  45.758  58.954  1.00114.20           O  
ANISOU 2397  OE2 GLU A 298    16215  13691  13483   2749   -854    288       O  
ATOM   2398  N   VAL A 299      57.958  44.628  65.228  1.00 43.45           N  
ANISOU 2398  N   VAL A 299     5858   4489   6162   1934   -519   -546       N  
ATOM   2399  CA  VAL A 299      57.844  43.826  66.434  1.00 52.22           C  
ANISOU 2399  CA  VAL A 299     6713   5646   7482   1736   -406   -733       C  
ATOM   2400  C   VAL A 299      56.922  44.476  67.468  1.00 52.09           C  
ANISOU 2400  C   VAL A 299     6524   5517   7752   1704   -440   -890       C  
ATOM   2401  O   VAL A 299      56.158  43.794  68.152  1.00 46.39           O  
ANISOU 2401  O   VAL A 299     5579   4840   7206   1639   -448  -1125       O  
ATOM   2402  CB  VAL A 299      59.240  43.495  67.045  1.00 49.17           C  
ANISOU 2402  CB  VAL A 299     6347   5282   7055   1501   -144   -596       C  
ATOM   2403  CG1 VAL A 299      59.203  43.546  68.566  1.00 49.01           C  
ANISOU 2403  CG1 VAL A 299     6150   5210   7261   1300    -19   -691       C  
ATOM   2404  CG2 VAL A 299      59.701  42.128  66.585  1.00 46.83           C  
ANISOU 2404  CG2 VAL A 299     6022   5141   6632   1466   -115   -642       C  
ATOM   2405  N   ARG A 300      56.995  45.795  67.582  1.00 58.37           N  
ANISOU 2405  N   ARG A 300     7415   6157   8606   1743   -443   -768       N  
ATOM   2406  CA  ARG A 300      56.167  46.509  68.548  1.00 65.91           C  
ANISOU 2406  CA  ARG A 300     8199   6998   9844   1716   -467   -935       C  
ATOM   2407  C   ARG A 300      54.697  46.443  68.152  1.00 61.35           C  
ANISOU 2407  C   ARG A 300     7493   6411   9406   1916   -725  -1177       C  
ATOM   2408  O   ARG A 300      53.810  46.563  68.989  1.00 54.19           O  
ANISOU 2408  O   ARG A 300     6363   5464   8763   1873   -732  -1419       O  
ATOM   2409  CB  ARG A 300      56.597  47.965  68.667  1.00 69.44           C  
ANISOU 2409  CB  ARG A 300     8772   7259  10352   1729   -431   -758       C  
ATOM   2410  CG  ARG A 300      55.783  48.753  69.673  1.00 68.35           C  
ANISOU 2410  CG  ARG A 300     8444   7002  10522   1701   -452   -956       C  
ATOM   2411  CD  ARG A 300      55.665  50.195  69.245  1.00 72.70           C  
ANISOU 2411  CD  ARG A 300     9120   7337  11165   1853   -572   -827       C  
ATOM   2412  NE  ARG A 300      55.083  50.300  67.908  1.00 74.18           N  
ANISOU 2412  NE  ARG A 300     9460   7496  11229   2123   -839   -756       N  
ATOM   2413  CZ  ARG A 300      55.201  51.371  67.133  1.00 70.98           C  
ANISOU 2413  CZ  ARG A 300     9274   6915  10781   2286   -961   -535       C  
ATOM   2414  NH1 ARG A 300      54.636  51.383  65.929  1.00 57.91           N  
ANISOU 2414  NH1 ARG A 300     7779   5252   8973   2543  -1229   -476       N  
ATOM   2415  NH2 ARG A 300      55.889  52.426  67.568  1.00 65.98           N  
ANISOU 2415  NH2 ARG A 300     8706   6106  10258   2193   -820   -373       N  
ATOM   2416  N   ASP A 301      54.437  46.222  66.873  1.00 61.24           N  
ANISOU 2416  N   ASP A 301     7611   6441   9216   2135   -935  -1136       N  
ATOM   2417  CA  ASP A 301      53.062  46.139  66.414  1.00 65.63           C  
ANISOU 2417  CA  ASP A 301     8039   6985   9913   2351  -1221  -1387       C  
ATOM   2418  C   ASP A 301      52.555  44.701  66.369  1.00 64.58           C  
ANISOU 2418  C   ASP A 301     7711   7012   9813   2327  -1247  -1634       C  
ATOM   2419  O   ASP A 301      51.360  44.461  66.518  1.00 64.74           O  
ANISOU 2419  O   ASP A 301     7502   7018  10080   2407  -1394  -1936       O  
ATOM   2420  CB  ASP A 301      52.906  46.802  65.044  1.00 65.34           C  
ANISOU 2420  CB  ASP A 301     8260   6889   9676   2643  -1495  -1230       C  
ATOM   2421  CG  ASP A 301      53.235  48.286  65.066  1.00 72.86           C  
ANISOU 2421  CG  ASP A 301     9393   7635  10657   2686  -1495   -995       C  
ATOM   2422  OD1 ASP A 301      53.126  48.938  66.140  1.00 62.44           O  
ANISOU 2422  OD1 ASP A 301     7922   6194   9610   2555  -1379  -1067       O  
ATOM   2423  OD2 ASP A 301      53.608  48.798  63.989  1.00 83.24           O  
ANISOU 2423  OD2 ASP A 301    11009   8905  11713   2850  -1607   -737       O  
ATOM   2424  N   ARG A 302      53.453  43.745  66.156  1.00 64.55           N  
ANISOU 2424  N   ARG A 302     7780   7147   9599   2216  -1104  -1525       N  
ATOM   2425  CA  ARG A 302      53.032  42.348  66.057  1.00 64.67           C  
ANISOU 2425  CA  ARG A 302     7612   7295   9663   2193  -1131  -1750       C  
ATOM   2426  C   ARG A 302      52.551  41.919  67.424  1.00 61.85           C  
ANISOU 2426  C   ARG A 302     6980   6914   9605   1974   -955  -1952       C  
ATOM   2427  O   ARG A 302      51.464  41.364  67.573  1.00 71.97           O  
ANISOU 2427  O   ARG A 302     8024   8202  11119   2006  -1041  -2246       O  
ATOM   2428  CB  ARG A 302      54.158  41.440  65.528  1.00 52.04           C  
ANISOU 2428  CB  ARG A 302     6145   5833   7794   2123  -1017  -1592       C  
ATOM   2429  CG  ARG A 302      54.136  40.004  66.062  1.00 53.14           C  
ANISOU 2429  CG  ARG A 302     6068   6064   8057   1956   -900  -1764       C  
ATOM   2430  CD  ARG A 302      54.685  38.983  65.067  1.00 36.59           C  
ANISOU 2430  CD  ARG A 302     4043   4110   5751   2019   -946  -1751       C  
ATOM   2431  NE  ARG A 302      53.618  38.493  64.213  1.00 49.50           N  
ANISOU 2431  NE  ARG A 302     5569   5800   7438   2240  -1214  -2011       N  
ATOM   2432  CZ  ARG A 302      53.266  37.221  64.079  1.00 54.19           C  
ANISOU 2432  CZ  ARG A 302     5968   6472   8150   2225  -1252  -2238       C  
ATOM   2433  NH1 ARG A 302      52.267  36.905  63.274  1.00 69.47           N  
ANISOU 2433  NH1 ARG A 302     7798   8448  10149   2448  -1523  -2497       N  
ATOM   2434  NH2 ARG A 302      53.912  36.266  64.724  1.00 49.58           N  
ANISOU 2434  NH2 ARG A 302     5291   5913   7635   2000  -1039  -2214       N  
ATOM   2435  N   TYR A 303      53.329  42.273  68.411  1.00 52.79           N  
ANISOU 2435  N   TYR A 303     5873   5737   8447   1749   -704  -1797       N  
ATOM   2436  CA  TYR A 303      52.996  42.055  69.781  1.00 63.51           C  
ANISOU 2436  CA  TYR A 303     7031   7068  10031   1530   -513  -1942       C  
ATOM   2437  C   TYR A 303      52.673  43.461  70.175  1.00 73.31           C  
ANISOU 2437  C   TYR A 303     8263   8176  11416   1582   -550  -1972       C  
ATOM   2438  O   TYR A 303      52.990  44.383  69.446  1.00 80.29           O  
ANISOU 2438  O   TYR A 303     9302   8984  12220   1777   -722  -1852       O  
ATOM   2439  CB  TYR A 303      54.219  41.526  70.502  1.00 64.36           C  
ANISOU 2439  CB  TYR A 303     7218   7227  10007   1287   -264  -1753       C  
ATOM   2440  CG  TYR A 303      54.890  40.404  69.744  1.00 57.69           C  
ANISOU 2440  CG  TYR A 303     6438   6489   8993   1300   -283  -1676       C  
ATOM   2441  CD1 TYR A 303      55.967  40.643  68.941  1.00 54.54           C  
ANISOU 2441  CD1 TYR A 303     6258   6118   8348   1358   -290  -1439       C  
ATOM   2442  CD2 TYR A 303      54.412  39.120  69.805  1.00 56.65           C  
ANISOU 2442  CD2 TYR A 303     6132   6420   8974   1264   -295  -1865       C  
ATOM   2443  CE1 TYR A 303      56.551  39.644  68.240  1.00 59.98           C  
ANISOU 2443  CE1 TYR A 303     6985   6911   8895   1376   -306  -1407       C  
ATOM   2444  CE2 TYR A 303      54.995  38.117  69.103  1.00 53.52           C  
ANISOU 2444  CE2 TYR A 303     5769   6111   8454   1289   -329  -1828       C  
ATOM   2445  CZ  TYR A 303      56.058  38.382  68.323  1.00 54.02           C  
ANISOU 2445  CZ  TYR A 303     6045   6217   8262   1347   -338  -1608       C  
ATOM   2446  OH  TYR A 303      56.659  37.378  67.631  1.00 47.56           O  
ANISOU 2446  OH  TYR A 303     5242   5494   7335   1369   -362  -1606       O  
ATOM   2447  N   SER A 304      51.972  43.684  71.259  1.00 61.24           N  
ANISOU 2447  N   SER A 304     6563   6609  10097   1422   -398  -2131       N  
ATOM   2448  CA  SER A 304      51.696  45.065  71.528  1.00 66.63           C  
ANISOU 2448  CA  SER A 304     7219   7156  10940   1496   -458  -2189       C  
ATOM   2449  C   SER A 304      52.616  45.579  72.586  1.00 67.54           C  
ANISOU 2449  C   SER A 304     7419   7230  11014   1317   -251  -2037       C  
ATOM   2450  O   SER A 304      52.400  45.366  73.754  1.00 80.16           O  
ANISOU 2450  O   SER A 304     8877   8836  12745   1140    -74  -2188       O  
ATOM   2451  CB  SER A 304      50.250  45.225  71.900  1.00 73.65           C  
ANISOU 2451  CB  SER A 304     7826   7999  12159   1539   -524  -2557       C  
ATOM   2452  OG  SER A 304      49.468  44.980  70.755  1.00 80.17           O  
ANISOU 2452  OG  SER A 304     8617   8809  13035   1798   -820  -2673       O  
ATOM   2453  N   LEU A 305      53.624  46.307  72.137  1.00 53.06           N  
ANISOU 2453  N   LEU A 305     5818   5352   8992   1367   -270  -1749       N  
ATOM   2454  CA  LEU A 305      54.742  46.748  72.956  1.00 58.56           C  
ANISOU 2454  CA  LEU A 305     6602   6029   9618   1184    -68  -1586       C  
ATOM   2455  C   LEU A 305      54.715  48.243  73.303  1.00 57.02           C  
ANISOU 2455  C   LEU A 305     6415   5668   9581   1221    -83  -1581       C  
ATOM   2456  O   LEU A 305      54.705  49.102  72.423  1.00 61.64           O  
ANISOU 2456  O   LEU A 305     7122   6126  10174   1405   -240  -1456       O  
ATOM   2457  CB  LEU A 305      56.068  46.352  72.289  1.00 63.25           C  
ANISOU 2457  CB  LEU A 305     7411   6674   9948   1164    -21  -1298       C  
ATOM   2458  CG  LEU A 305      56.280  44.872  71.952  1.00 65.57           C  
ANISOU 2458  CG  LEU A 305     7697   7119  10096   1119     -1  -1295       C  
ATOM   2459  CD1 LEU A 305      57.753  44.554  71.759  1.00 62.36           C  
ANISOU 2459  CD1 LEU A 305     7452   6754   9488   1025    116  -1055       C  
ATOM   2460  CD2 LEU A 305      55.709  44.010  73.048  1.00 72.32           C  
ANISOU 2460  CD2 LEU A 305     8359   8051  11070    950    113  -1504       C  
ATOM   2461  N   ARG A 306      54.714  48.540  74.599  1.00 49.76           N  
ANISOU 2461  N   ARG A 306     5375   4749   8784   1046     81  -1716       N  
ATOM   2462  CA  ARG A 306      54.738  49.916  75.076  1.00 51.31           C  
ANISOU 2462  CA  ARG A 306     5546   4792   9159   1056     88  -1750       C  
ATOM   2463  C   ARG A 306      55.723  50.761  74.236  1.00 57.59           C  
ANISOU 2463  C   ARG A 306     6562   5449   9870   1154     29  -1445       C  
ATOM   2464  O   ARG A 306      56.900  50.460  74.161  1.00 64.04           O  
ANISOU 2464  O   ARG A 306     7517   6311  10504   1059    142  -1236       O  
ATOM   2465  CB  ARG A 306      55.003  49.960  76.598  1.00 54.55           C  
ANISOU 2465  CB  ARG A 306     5850   5266   9612    822    308  -1890       C  
ATOM   2466  CG  ARG A 306      56.429  50.341  77.043  1.00 82.16           C  
ANISOU 2466  CG  ARG A 306     9479   8742  12995    697    433  -1694       C  
ATOM   2467  CD  ARG A 306      56.524  50.642  78.556  1.00 96.29           C  
ANISOU 2467  CD  ARG A 306    11158  10579  14850    509    598  -1882       C  
ATOM   2468  NE  ARG A 306      55.945  49.568  79.371  1.00111.95           N  
ANISOU 2468  NE  ARG A 306    13045  12736  16754    366    716  -2055       N  
ATOM   2469  CZ  ARG A 306      56.619  48.821  80.249  1.00110.35           C  
ANISOU 2469  CZ  ARG A 306    12898  12667  16364    180    860  -2017       C  
ATOM   2470  NH1 ARG A 306      57.917  49.029  80.455  1.00104.80           N  
ANISOU 2470  NH1 ARG A 306    12319  11949  15550    119    888  -1844       N  
ATOM   2471  NH2 ARG A 306      55.987  47.868  80.934  1.00101.75           N  
ANISOU 2471  NH2 ARG A 306    11737  11711  15211     55    974  -2155       N  
ATOM   2472  N   ARG A 307      55.253  51.824  73.633  1.00 73.60           N  
ANISOU 2472  N   ARG A 307     8621   7298  12047   1347   -148  -1424       N  
ATOM   2473  CA  ARG A 307      55.989  52.532  72.614  1.00 82.33           C  
ANISOU 2473  CA  ARG A 307     9964   8253  13064   1468   -217  -1112       C  
ATOM   2474  C   ARG A 307      57.317  53.043  73.097  1.00 77.75           C  
ANISOU 2474  C   ARG A 307     9469   7614  12460   1303    -12   -939       C  
ATOM   2475  O   ARG A 307      58.226  53.260  72.321  1.00 69.09           O  
ANISOU 2475  O   ARG A 307     8579   6457  11215   1325     27   -656       O  
ATOM   2476  CB  ARG A 307      55.152  53.697  72.115  1.00101.22           C  
ANISOU 2476  CB  ARG A 307    12358  10418  15682   1685   -439  -1140       C  
ATOM   2477  CG  ARG A 307      54.250  53.382  70.947  1.00114.83           C  
ANISOU 2477  CG  ARG A 307    13943  12164  17523   1866   -677  -1384       C  
ATOM   2478  CD  ARG A 307      53.411  54.579  70.559  1.00124.10           C  
ANISOU 2478  CD  ARG A 307    15144  13086  18921   2109   -943  -1382       C  
ATOM   2479  NE  ARG A 307      53.546  54.925  69.148  1.00129.54           N  
ANISOU 2479  NE  ARG A 307    16153  13674  19393   2293  -1093  -1030       N  
ATOM   2480  CZ  ARG A 307      52.764  54.469  68.179  1.00129.73           C  
ANISOU 2480  CZ  ARG A 307    16302  13765  19224   2495  -1315   -976       C  
ATOM   2481  NH1 ARG A 307      51.780  53.633  68.447  1.00125.18           N  
ANISOU 2481  NH1 ARG A 307    15532  13344  18686   2541  -1423  -1266       N  
ATOM   2482  NH2 ARG A 307      52.968  54.853  66.933  1.00130.11           N  
ANISOU 2482  NH2 ARG A 307    16674  13726  19037   2649  -1423   -638       N  
ATOM   2483  N   ASN A 308      57.463  53.254  74.388  1.00 76.95           N  
ANISOU 2483  N   ASN A 308     9203   7528  12506   1136    122  -1125       N  
ATOM   2484  CA  ASN A 308      58.709  53.792  74.905  1.00 71.22           C  
ANISOU 2484  CA  ASN A 308     8522   6737  11802    990    287  -1016       C  
ATOM   2485  C   ASN A 308      59.737  52.735  75.125  1.00 68.02           C  
ANISOU 2485  C   ASN A 308     8191   6499  11155    838    432   -901       C  
ATOM   2486  O   ASN A 308      60.863  53.015  75.445  1.00 84.14           O  
ANISOU 2486  O   ASN A 308    10290   8482  13197    739    551   -779       O  
ATOM   2487  CB  ASN A 308      58.470  54.521  76.215  1.00 79.45           C  
ANISOU 2487  CB  ASN A 308     9366   7745  13076    880    359  -1282       C  
ATOM   2488  CG  ASN A 308      59.578  55.479  76.554  1.00 90.37           C  
ANISOU 2488  CG  ASN A 308    10777   8976  14582    796    463  -1194       C  
ATOM   2489  OD1 ASN A 308      60.307  55.937  75.688  1.00 89.35           O  
ANISOU 2489  OD1 ASN A 308    10806   8694  14448    852    466   -932       O  
ATOM   2490  ND2 ASN A 308      59.698  55.801  77.818  1.00 95.05           N  
ANISOU 2490  ND2 ASN A 308    11217   9609  15289    657    558  -1425       N  
ATOM   2491  N   LEU A 309      59.398  51.493  74.893  1.00 63.58           N  
ANISOU 2491  N   LEU A 309     7610   6128  10421    823    415   -954       N  
ATOM   2492  CA  LEU A 309      60.348  50.468  75.232  1.00 64.17           C  
ANISOU 2492  CA  LEU A 309     7728   6357  10295    679    531   -877       C  
ATOM   2493  C   LEU A 309      61.656  50.592  74.502  1.00 64.85           C  
ANISOU 2493  C   LEU A 309     7977   6377  10285    665    604   -617       C  
ATOM   2494  O   LEU A 309      62.707  50.512  75.099  1.00 61.14           O  
ANISOU 2494  O   LEU A 309     7499   5926   9807    517    724   -593       O  
ATOM   2495  CB  LEU A 309      59.751  49.116  74.904  1.00 59.72           C  
ANISOU 2495  CB  LEU A 309     7145   5961   9585    709    473   -929       C  
ATOM   2496  CG  LEU A 309      60.647  47.944  75.239  1.00 56.88           C  
ANISOU 2496  CG  LEU A 309     6830   5741   9042    580    566   -844       C  
ATOM   2497  CD1 LEU A 309      60.898  47.880  76.697  1.00 46.94           C  
ANISOU 2497  CD1 LEU A 309     5496   4535   7804    381    688   -940       C  
ATOM   2498  CD2 LEU A 309      60.006  46.703  74.754  1.00 46.74           C  
ANISOU 2498  CD2 LEU A 309     5515   4591   7654    630    494   -900       C  
ATOM   2499  N   ILE A 310      61.586  50.836  73.215  1.00 64.93           N  
ANISOU 2499  N   ILE A 310     8136   6310  10224    820    531   -434       N  
ATOM   2500  CA  ILE A 310      62.783  50.853  72.372  1.00 68.42           C  
ANISOU 2500  CA  ILE A 310     8747   6709  10540    809    628   -186       C  
ATOM   2501  C   ILE A 310      63.781  51.938  72.768  1.00 73.68           C  
ANISOU 2501  C   ILE A 310     9425   7194  11377    716    762   -101       C  
ATOM   2502  O   ILE A 310      64.982  51.819  72.510  1.00 70.96           O  
ANISOU 2502  O   ILE A 310     9148   6829  10983    630    902     35       O  
ATOM   2503  CB  ILE A 310      62.438  50.974  70.876  1.00 63.53           C  
ANISOU 2503  CB  ILE A 310     8317   6054   9768   1002    526     -6       C  
ATOM   2504  CG1 ILE A 310      63.715  50.941  70.031  1.00 64.47           C  
ANISOU 2504  CG1 ILE A 310     8613   6146   9737    964    679    240       C  
ATOM   2505  CG2 ILE A 310      61.644  52.236  70.609  1.00 61.81           C  
ANISOU 2505  CG2 ILE A 310     8139   5637   9709   1154    398     20       C  
ATOM   2506  CD1 ILE A 310      64.211  49.541  69.755  1.00 58.97           C  
ANISOU 2506  CD1 ILE A 310     7913   5656   8836    903    729    223       C  
ATOM   2507  N   ASN A 311      63.278  52.992  73.398  1.00 72.98           N  
ANISOU 2507  N   ASN A 311     9246   6963  11520    733    723   -208       N  
ATOM   2508  CA  ASN A 311      64.147  54.006  73.970  1.00 73.31           C  
ANISOU 2508  CA  ASN A 311     9248   6830  11776    634    840   -192       C  
ATOM   2509  C   ASN A 311      64.827  53.463  75.217  1.00 69.71           C  
ANISOU 2509  C   ASN A 311     8654   6497  11334    450    928   -360       C  
ATOM   2510  O   ASN A 311      66.030  53.641  75.401  1.00 74.23           O  
ANISOU 2510  O   ASN A 311     9228   7008  11969    345   1048   -302       O  
ATOM   2511  CB  ASN A 311      63.359  55.273  74.313  1.00 80.80           C  
ANISOU 2511  CB  ASN A 311    10119   7588  12993    712    755   -293       C  
ATOM   2512  CG  ASN A 311      62.663  55.879  73.108  1.00 83.15           C  
ANISOU 2512  CG  ASN A 311    10569   7734  13290    915    625   -118       C  
ATOM   2513  OD1 ASN A 311      63.208  55.911  72.003  1.00 77.53           O  
ANISOU 2513  OD1 ASN A 311    10061   6959  12436    970    668    152       O  
ATOM   2514  ND2 ASN A 311      61.455  56.378  73.322  1.00 88.67           N  
ANISOU 2514  ND2 ASN A 311    11172   8370  14150   1030    462   -280       N  
ATOM   2515  N   GLU A 312      64.058  52.793  76.071  1.00 64.51           N  
ANISOU 2515  N   GLU A 312     7881   6008  10621    413    867   -572       N  
ATOM   2516  CA  GLU A 312      64.598  52.276  77.328  1.00 72.76           C  
ANISOU 2516  CA  GLU A 312     8827   7177  11643    250    927   -727       C  
ATOM   2517  C   GLU A 312      65.686  51.231  77.082  1.00 67.26           C  
ANISOU 2517  C   GLU A 312     8196   6579  10779    171    985   -606       C  
ATOM   2518  O   GLU A 312      66.720  51.214  77.761  1.00 56.43           O  
ANISOU 2518  O   GLU A 312     6784   5201   9454     57   1042   -643       O  
ATOM   2519  CB  GLU A 312      63.488  51.685  78.184  1.00 79.59           C  
ANISOU 2519  CB  GLU A 312     9590   8204  12445    221    878   -945       C  
ATOM   2520  CG  GLU A 312      62.151  52.380  78.026  1.00 87.72           C  
ANISOU 2520  CG  GLU A 312    10551   9162  13615    340    796  -1064       C  
ATOM   2521  CD  GLU A 312      61.259  52.143  79.216  1.00102.53           C  
ANISOU 2521  CD  GLU A 312    12284  11164  15508    261    813  -1341       C  
ATOM   2522  OE1 GLU A 312      60.079  51.775  79.014  1.00109.64           O  
ANISOU 2522  OE1 GLU A 312    13127  12124  16409    328    756  -1445       O  
ATOM   2523  OE2 GLU A 312      61.755  52.314  80.356  1.00105.07           O  
ANISOU 2523  OE2 GLU A 312    12551  11528  15841    131    887  -1465       O  
ATOM   2524  N   ILE A 313      65.439  50.359  76.111  1.00 57.49           N  
ANISOU 2524  N   ILE A 313     7047   5430   9367    242    953   -488       N  
ATOM   2525  CA  ILE A 313      66.444  49.401  75.698  1.00 52.17           C  
ANISOU 2525  CA  ILE A 313     6428   4832   8562    186   1005   -380       C  
ATOM   2526  C   ILE A 313      67.635  50.178  75.173  1.00 53.54           C  
ANISOU 2526  C   ILE A 313     6656   4842   8846    164   1121   -237       C  
ATOM   2527  O   ILE A 313      68.774  49.947  75.579  1.00 53.72           O  
ANISOU 2527  O   ILE A 313     6634   4857   8920     54   1189   -253       O  
ATOM   2528  CB  ILE A 313      65.903  48.451  74.604  1.00 54.26           C  
ANISOU 2528  CB  ILE A 313     6772   5208   8635    287    948   -295       C  
ATOM   2529  CG1 ILE A 313      64.934  47.437  75.212  1.00 47.66           C  
ANISOU 2529  CG1 ILE A 313     5855   4534   7721    269    865   -450       C  
ATOM   2530  CG2 ILE A 313      67.034  47.703  73.903  1.00 53.79           C  
ANISOU 2530  CG2 ILE A 313     6776   5188   8473    250   1023   -172       C  
ATOM   2531  CD1 ILE A 313      64.030  46.779  74.215  1.00 32.09           C  
ANISOU 2531  CD1 ILE A 313     3920   2642   5632    399    775   -433       C  
ATOM   2532  N   ARG A 314      67.366  51.119  74.277  1.00 53.08           N  
ANISOU 2532  N   ARG A 314     6692   4635   8841    269   1140   -102       N  
ATOM   2533  CA  ARG A 314      68.443  51.854  73.633  1.00 56.35           C  
ANISOU 2533  CA  ARG A 314     7180   4874   9355    243   1287     65       C  
ATOM   2534  C   ARG A 314      69.287  52.583  74.651  1.00 62.29           C  
ANISOU 2534  C   ARG A 314     7802   5500  10364    119   1361    -46       C  
ATOM   2535  O   ARG A 314      70.466  52.839  74.426  1.00 70.68           O  
ANISOU 2535  O   ARG A 314     8862   6454  11539     40   1502     23       O  
ATOM   2536  CB  ARG A 314      67.915  52.806  72.569  1.00 51.58           C  
ANISOU 2536  CB  ARG A 314     6729   4110   8759    381   1285    250       C  
ATOM   2537  CG  ARG A 314      67.822  52.167  71.189  1.00 52.55           C  
ANISOU 2537  CG  ARG A 314     7036   4320   8610    481   1290    434       C  
ATOM   2538  CD  ARG A 314      67.038  53.035  70.236  1.00 60.33           C  
ANISOU 2538  CD  ARG A 314     8195   5171   9558    651   1216    603       C  
ATOM   2539  NE  ARG A 314      66.727  52.347  68.994  1.00 65.26           N  
ANISOU 2539  NE  ARG A 314     8998   5921   9877    774   1167    733       N  
ATOM   2540  CZ  ARG A 314      66.105  52.920  67.974  1.00 69.00           C  
ANISOU 2540  CZ  ARG A 314     9673   6308  10237    946   1079    906       C  
ATOM   2541  NH1 ARG A 314      65.851  52.232  66.865  1.00 73.39           N  
ANISOU 2541  NH1 ARG A 314    10393   7004  10486   1064   1020    999       N  
ATOM   2542  NH2 ARG A 314      65.739  54.189  68.071  1.00 65.64           N  
ANISOU 2542  NH2 ARG A 314     9284   5647  10008   1007   1034    979       N  
ATOM   2543  N   HIS A 315      68.678  52.900  75.784  1.00 67.51           N  
ANISOU 2543  N   HIS A 315     8344   6182  11126     99   1269   -245       N  
ATOM   2544  CA  HIS A 315      69.416  53.505  76.877  1.00 58.40           C  
ANISOU 2544  CA  HIS A 315     7053   4944  10193    -10   1305   -402       C  
ATOM   2545  C   HIS A 315      70.449  52.535  77.406  1.00 56.51           C  
ANISOU 2545  C   HIS A 315     6759   4825   9886   -122   1318   -471       C  
ATOM   2546  O   HIS A 315      71.608  52.893  77.566  1.00 60.89           O  
ANISOU 2546  O   HIS A 315     7250   5266  10620   -200   1399   -490       O  
ATOM   2547  CB  HIS A 315      68.485  53.923  78.003  1.00 49.51           C  
ANISOU 2547  CB  HIS A 315     5818   3858   9137     -7   1204   -628       C  
ATOM   2548  CG  HIS A 315      69.214  54.451  79.194  1.00 53.88           C  
ANISOU 2548  CG  HIS A 315     6233   4362   9877   -111   1217   -825       C  
ATOM   2549  ND1 HIS A 315      70.041  55.543  79.122  1.00 59.45           N  
ANISOU 2549  ND1 HIS A 315     6881   4836  10872   -139   1301   -816       N  
ATOM   2550  CD2 HIS A 315      69.251  54.020  80.475  1.00 63.93           C  
ANISOU 2550  CD2 HIS A 315     7421   5788  11081   -191   1151  -1042       C  
ATOM   2551  CE1 HIS A 315      70.565  55.773  80.320  1.00 66.33           C  
ANISOU 2551  CE1 HIS A 315     7616   5724  11863   -224   1269  -1047       C  
ATOM   2552  NE2 HIS A 315      70.100  54.865  81.155  1.00 67.31           N  
ANISOU 2552  NE2 HIS A 315     7737   6087  11750   -252   1173  -1180       N  
ATOM   2553  N   VAL A 316      70.029  51.299  77.661  1.00 61.82           N  
ANISOU 2553  N   VAL A 316     7448   5711  10328   -128   1231   -512       N  
ATOM   2554  CA  VAL A 316      70.907  50.303  78.274  1.00 62.47           C  
ANISOU 2554  CA  VAL A 316     7485   5904  10345   -222   1199   -583       C  
ATOM   2555  C   VAL A 316      72.016  49.854  77.332  1.00 57.77           C  
ANISOU 2555  C   VAL A 316     6920   5264   9765   -242   1294   -452       C  
ATOM   2556  O   VAL A 316      73.156  49.727  77.741  1.00 53.56           O  
ANISOU 2556  O   VAL A 316     6306   4690   9356   -322   1309   -522       O  
ATOM   2557  CB  VAL A 316      70.137  49.058  78.778  1.00 60.40           C  
ANISOU 2557  CB  VAL A 316     7246   5858   9847   -228   1089   -641       C  
ATOM   2558  CG1 VAL A 316      71.008  48.258  79.724  1.00 50.32           C  
ANISOU 2558  CG1 VAL A 316     5925   4660   8534   -324   1020   -733       C  
ATOM   2559  CG2 VAL A 316      68.856  49.466  79.472  1.00 68.19           C  
ANISOU 2559  CG2 VAL A 316     8209   6896  10805   -204   1040   -764       C  
ATOM   2560  N   GLU A 317      71.682  49.615  76.072  1.00 59.68           N  
ANISOU 2560  N   GLU A 317     7272   5517   9885   -165   1352   -282       N  
ATOM   2561  CA  GLU A 317      72.675  49.139  75.128  1.00 55.35           C  
ANISOU 2561  CA  GLU A 317     6757   4951   9324   -188   1468   -174       C  
ATOM   2562  C   GLU A 317      73.714  50.227  74.845  1.00 62.34           C  
ANISOU 2562  C   GLU A 317     7610   5617  10460   -245   1641   -129       C  
ATOM   2563  O   GLU A 317      74.850  49.930  74.477  1.00 67.07           O  
ANISOU 2563  O   GLU A 317     8166   6174  11144   -313   1756   -120       O  
ATOM   2564  CB  GLU A 317      72.009  48.646  73.842  1.00 57.53           C  
ANISOU 2564  CB  GLU A 317     7175   5311   9374    -84   1485    -20       C  
ATOM   2565  CG  GLU A 317      71.685  49.738  72.840  1.00 78.41           C  
ANISOU 2565  CG  GLU A 317     9953   7814  12027      0   1585    155       C  
ATOM   2566  CD  GLU A 317      70.880  49.222  71.662  1.00 83.72           C  
ANISOU 2566  CD  GLU A 317    10778   8595  12435    130   1546    279       C  
ATOM   2567  OE1 GLU A 317      70.214  48.186  71.838  1.00 89.83           O  
ANISOU 2567  OE1 GLU A 317    11521   9545  13064    166   1410    191       O  
ATOM   2568  OE2 GLU A 317      70.908  49.841  70.573  1.00 77.33           O  
ANISOU 2568  OE2 GLU A 317    10124   7693  11563    198   1646    462       O  
ATOM   2569  N   LYS A 318      73.330  51.487  75.037  1.00 63.37           N  
ANISOU 2569  N   LYS A 318     7743   5592  10744   -221   1666   -116       N  
ATOM   2570  CA  LYS A 318      74.244  52.614  74.806  1.00 63.05           C  
ANISOU 2570  CA  LYS A 318     7664   5306  10987   -281   1842    -72       C  
ATOM   2571  C   LYS A 318      75.184  52.894  75.982  1.00 58.18           C  
ANISOU 2571  C   LYS A 318     6848   4615  10642   -389   1819   -295       C  
ATOM   2572  O   LYS A 318      76.372  53.189  75.801  1.00 46.93           O  
ANISOU 2572  O   LYS A 318     5338   3046   9449   -474   1965   -314       O  
ATOM   2573  CB  LYS A 318      73.463  53.874  74.446  1.00 55.46           C  
ANISOU 2573  CB  LYS A 318     6790   4173  10111   -203   1871     45       C  
ATOM   2574  CG  LYS A 318      73.165  54.008  72.969  1.00 60.59           C  
ANISOU 2574  CG  LYS A 318     7654   4775  10592   -118   1980    319       C  
ATOM   2575  CD  LYS A 318      72.001  54.972  72.704  1.00 69.05           C  
ANISOU 2575  CD  LYS A 318     8832   5730  11673      9   1897    420       C  
ATOM   2576  CE  LYS A 318      72.106  55.540  71.291  1.00 77.25           C  
ANISOU 2576  CE  LYS A 318    10097   6616  12639     68   2051    722       C  
ATOM   2577  NZ  LYS A 318      70.832  55.408  70.527  1.00 79.59           N  
ANISOU 2577  NZ  LYS A 318    10579   6993  12669    248   1893    851       N  
ATOM   2578  N   SER A 319      74.650  52.792  77.190  1.00 57.80           N  
ANISOU 2578  N   SER A 319     6724   4670  10568   -384   1636   -480       N  
ATOM   2579  CA  SER A 319      75.434  53.100  78.377  1.00 65.68           C  
ANISOU 2579  CA  SER A 319     7551   5616  11790   -463   1571   -714       C  
ATOM   2580  C   SER A 319      76.164  51.915  79.004  1.00 61.67           C  
ANISOU 2580  C   SER A 319     6977   5257  11198   -515   1451   -840       C  
ATOM   2581  O   SER A 319      76.923  52.096  79.948  1.00 68.63           O  
ANISOU 2581  O   SER A 319     7723   6099  12254   -567   1370  -1040       O  
ATOM   2582  CB  SER A 319      74.554  53.788  79.425  1.00 75.36           C  
ANISOU 2582  CB  SER A 319     8731   6859  13044   -436   1449   -872       C  
ATOM   2583  OG  SER A 319      73.270  53.201  79.479  1.00 75.42           O  
ANISOU 2583  OG  SER A 319     8841   7053  12763   -369   1351   -835       O  
ATOM   2584  N   ALA A 320      75.952  50.711  78.484  1.00 56.30           N  
ANISOU 2584  N   ALA A 320     6388   4736  10267   -490   1420   -734       N  
ATOM   2585  CA  ALA A 320      76.513  49.509  79.111  1.00 55.87           C  
ANISOU 2585  CA  ALA A 320     6286   4815  10127   -525   1272   -840       C  
ATOM   2586  C   ALA A 320      78.040  49.491  79.231  1.00 55.66           C  
ANISOU 2586  C   ALA A 320     6108   4668  10374   -594   1296   -960       C  
ATOM   2587  O   ALA A 320      78.566  49.118  80.286  1.00 48.06           O  
ANISOU 2587  O   ALA A 320     5061   3745   9454   -619   1116  -1137       O  
ATOM   2588  CB  ALA A 320      76.005  48.240  78.433  1.00 52.70           C  
ANISOU 2588  CB  ALA A 320     5993   4577   9455   -485   1245   -708       C  
ATOM   2589  N   PRO A 321      78.758  49.886  78.163  1.00 59.73           N  
ANISOU 2589  N   PRO A 321     6590   5032  11071   -625   1517   -873       N  
ATOM   2590  CA  PRO A 321      80.217  49.909  78.291  1.00 62.26           C  
ANISOU 2590  CA  PRO A 321     6729   5221  11706   -700   1558  -1026       C  
ATOM   2591  C   PRO A 321      80.620  50.922  79.354  1.00 60.61           C  
ANISOU 2591  C   PRO A 321     6376   4880  11773   -731   1485  -1234       C  
ATOM   2592  O   PRO A 321      81.524  50.641  80.136  1.00 67.02           O  
ANISOU 2592  O   PRO A 321     7038   5672  12753   -759   1337  -1448       O  
ATOM   2593  CB  PRO A 321      80.696  50.360  76.904  1.00 60.39           C  
ANISOU 2593  CB  PRO A 321     6511   4838  11598   -740   1872   -874       C  
ATOM   2594  CG  PRO A 321      79.568  50.100  76.001  1.00 63.15           C  
ANISOU 2594  CG  PRO A 321     7076   5307  11613   -665   1930   -635       C  
ATOM   2595  CD  PRO A 321      78.327  50.303  76.823  1.00 68.41           C  
ANISOU 2595  CD  PRO A 321     7817   6074  12102   -596   1738   -646       C  
ATOM   2596  N   ALA A 322      79.956  52.073  79.397  1.00 45.66           N  
ANISOU 2596  N   ALA A 322     4519   2893   9937   -716   1562  -1192       N  
ATOM   2597  CA  ALA A 322      80.289  53.061  80.427  1.00 63.39           C  
ANISOU 2597  CA  ALA A 322     6612   5015  12458   -739   1486  -1420       C  
ATOM   2598  C   ALA A 322      80.083  52.475  81.826  1.00 72.00           C  
ANISOU 2598  C   ALA A 322     7688   6293  13375   -710   1182  -1620       C  
ATOM   2599  O   ALA A 322      80.934  52.621  82.703  1.00 68.52           O  
ANISOU 2599  O   ALA A 322     7094   5803  13138   -732   1045  -1864       O  
ATOM   2600  CB  ALA A 322      79.491  54.359  80.250  1.00 50.38           C  
ANISOU 2600  CB  ALA A 322     5007   3234  10903   -718   1602  -1345       C  
ATOM   2601  N   LEU A 323      78.956  51.801  82.022  1.00 67.73           N  
ANISOU 2601  N   LEU A 323     7315   5964  12457   -660   1080  -1518       N  
ATOM   2602  CA  LEU A 323      78.671  51.154  83.293  1.00 69.50           C  
ANISOU 2602  CA  LEU A 323     7575   6378  12454   -643    826  -1661       C  
ATOM   2603  C   LEU A 323      79.824  50.222  83.648  1.00 73.77           C  
ANISOU 2603  C   LEU A 323     8042   6939  13049   -660    666  -1767       C  
ATOM   2604  O   LEU A 323      80.525  50.440  84.634  1.00 74.48           O  
ANISOU 2604  O   LEU A 323     8024   7000  13274   -664    496  -1999       O  
ATOM   2605  CB  LEU A 323      77.355  50.365  83.219  1.00 64.56           C  
ANISOU 2605  CB  LEU A 323     7138   5959  11434   -605    793  -1502       C  
ATOM   2606  CG  LEU A 323      76.558  50.182  84.517  1.00 58.87           C  
ANISOU 2606  CG  LEU A 323     6489   5416  10462   -598    624  -1623       C  
ATOM   2607  CD1 LEU A 323      75.661  48.987  84.384  1.00 62.98           C  
ANISOU 2607  CD1 LEU A 323     7168   6123  10638   -585    589  -1468       C  
ATOM   2608  CD2 LEU A 323      77.443  50.009  85.727  1.00 52.77           C  
ANISOU 2608  CD2 LEU A 323     5654   4674   9721   -616    412  -1843       C  
ATOM   2609  N   LEU A 324      79.998  49.174  82.846  1.00 69.77           N  
ANISOU 2609  N   LEU A 324     7589   6480  12440   -658    701  -1614       N  
ATOM   2610  CA  LEU A 324      81.134  48.273  82.980  1.00 54.38           C  
ANISOU 2610  CA  LEU A 324     5548   4515  10599   -668    564  -1709       C  
ATOM   2611  C   LEU A 324      82.373  49.036  83.426  1.00 59.34           C  
ANISOU 2611  C   LEU A 324     5957   4962  11629   -697    526  -1960       C  
ATOM   2612  O   LEU A 324      82.968  48.732  84.457  1.00 55.76           O  
ANISOU 2612  O   LEU A 324     5441   4534  11213   -675    264  -2158       O  
ATOM   2613  CB  LEU A 324      81.411  47.616  81.638  1.00 47.23           C  
ANISOU 2613  CB  LEU A 324     4645   3582   9717   -681    739  -1547       C  
ATOM   2614  CG  LEU A 324      80.974  46.173  81.420  1.00 50.90           C  
ANISOU 2614  CG  LEU A 324     5233   4212   9895   -649    634  -1419       C  
ATOM   2615  CD1 LEU A 324      80.207  45.606  82.605  1.00 45.46           C  
ANISOU 2615  CD1 LEU A 324     4675   3688   8909   -619    388  -1430       C  
ATOM   2616  CD2 LEU A 324      80.185  46.059  80.116  1.00 44.49           C  
ANISOU 2616  CD2 LEU A 324     4532   3445   8928   -635    859  -1195       C  
ATOM   2617  N   GLU A 325      82.750  50.036  82.632  1.00 64.45           N  
ANISOU 2617  N   GLU A 325     6492   5415  12581   -743    788  -1949       N  
ATOM   2618  CA  GLU A 325      83.931  50.847  82.906  1.00 57.32           C  
ANISOU 2618  CA  GLU A 325     5348   4301  12131   -785    808  -2193       C  
ATOM   2619  C   GLU A 325      83.933  51.457  84.292  1.00 51.92           C  
ANISOU 2619  C   GLU A 325     4598   3630  11498   -755    572  -2446       C  
ATOM   2620  O   GLU A 325      84.898  51.282  85.002  1.00 55.36           O  
ANISOU 2620  O   GLU A 325     4883   4023  12130   -743    365  -2695       O  
ATOM   2621  CB  GLU A 325      84.135  51.917  81.839  1.00 66.74           C  
ANISOU 2621  CB  GLU A 325     6469   5272  13618   -852   1166  -2099       C  
ATOM   2622  CG  GLU A 325      84.944  51.417  80.658  1.00 72.74           C  
ANISOU 2622  CG  GLU A 325     7168   5945  14525   -909   1387  -2012       C  
ATOM   2623  CD  GLU A 325      84.864  52.346  79.474  1.00 81.49           C  
ANISOU 2623  CD  GLU A 325     8308   6877  15779   -972   1771  -1821       C  
ATOM   2624  OE1 GLU A 325      85.341  51.950  78.387  1.00 82.40           O  
ANISOU 2624  OE1 GLU A 325     8427   6953  15930  -1022   2000  -1709       O  
ATOM   2625  OE2 GLU A 325      84.325  53.470  79.631  1.00 79.40           O  
ANISOU 2625  OE2 GLU A 325     8072   6509  15586   -970   1845  -1784       O  
ATOM   2626  N   MET A 326      82.864  52.159  84.675  1.00 57.35           N  
ANISOU 2626  N   MET A 326     5392   4381  12018   -735    592  -2406       N  
ATOM   2627  CA  MET A 326      82.728  52.708  86.035  1.00 53.52           C  
ANISOU 2627  CA  MET A 326     4866   3951  11519   -703    372  -2660       C  
ATOM   2628  C   MET A 326      82.863  51.625  87.083  1.00 54.62           C  
ANISOU 2628  C   MET A 326     5095   4292  11366   -652     37  -2759       C  
ATOM   2629  O   MET A 326      83.494  51.820  88.114  1.00 72.06           O  
ANISOU 2629  O   MET A 326     7205   6498  13677   -623   -198  -3034       O  
ATOM   2630  CB  MET A 326      81.370  53.375  86.248  1.00 57.13           C  
ANISOU 2630  CB  MET A 326     5451   4491  11764   -686    445  -2584       C  
ATOM   2631  CG  MET A 326      81.207  54.736  85.638  1.00 65.35           C  
ANISOU 2631  CG  MET A 326     6392   5308  13129   -715    691  -2564       C  
ATOM   2632  SD  MET A 326      79.474  55.190  85.657  1.00 82.68           S  
ANISOU 2632  SD  MET A 326     8762   7620  15033   -677    761  -2424       S  
ATOM   2633  CE  MET A 326      79.364  56.099  84.126  1.00 45.46           C  
ANISOU 2633  CE  MET A 326     4036   2635  10600   -700   1092  -2173       C  
ATOM   2634  N   LEU A 327      82.233  50.488  86.841  1.00 46.84           N  
ANISOU 2634  N   LEU A 327     4308   3479  10009   -637      6  -2533       N  
ATOM   2635  CA  LEU A 327      82.300  49.417  87.807  1.00 53.88           C  
ANISOU 2635  CA  LEU A 327     5321   4545  10606   -594   -301  -2579       C  
ATOM   2636  C   LEU A 327      83.759  49.049  88.059  1.00 56.10           C  
ANISOU 2636  C   LEU A 327     5429   4711  11174   -571   -510  -2780       C  
ATOM   2637  O   LEU A 327      84.233  49.232  89.162  1.00 66.20           O  
ANISOU 2637  O   LEU A 327     6666   6011  12476   -527   -773  -3023       O  
ATOM   2638  CB  LEU A 327      81.421  48.236  87.394  1.00 60.21           C  
ANISOU 2638  CB  LEU A 327     6340   5510  11026   -592   -273  -2296       C  
ATOM   2639  CG  LEU A 327      79.939  48.630  87.474  1.00 63.57           C  
ANISOU 2639  CG  LEU A 327     6920   6065  11169   -604   -133  -2177       C  
ATOM   2640  CD1 LEU A 327      79.006  47.447  87.226  1.00 63.32           C  
ANISOU 2640  CD1 LEU A 327     7091   6199  10770   -604   -124  -1938       C  
ATOM   2641  CD2 LEU A 327      79.641  49.253  88.819  1.00 66.83           C  
ANISOU 2641  CD2 LEU A 327     7362   6571  11459   -593   -278  -2390       C  
ATOM   2642  N   SER A 328      84.485  48.561  87.054  1.00 63.00           N  
ANISOU 2642  N   SER A 328     6194   5464  12280   -594   -401  -2710       N  
ATOM   2643  CA  SER