CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 210510185259140766

Job options:

ID        	=	 210510185259140766
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   VAL A   9      -0.353  29.472 -28.673  1.00118.20           N  
ANISOU    1  N   VAL A   9    12152  18375  14381    557    207   3276       N  
ATOM      2  CA  VAL A   9      -1.030  28.216 -28.373  1.00120.72           C  
ANISOU    2  CA  VAL A   9    12582  18706  14577    648    245   3072       C  
ATOM      3  C   VAL A   9      -1.037  27.917 -26.868  1.00116.13           C  
ANISOU    3  C   VAL A   9    12139  17900  14084    588    200   2935       C  
ATOM      4  O   VAL A   9      -1.714  27.014 -26.407  1.00 94.88           O  
ANISOU    4  O   VAL A   9     9578  15127  11344    617    209   2752       O  
ATOM      5  CB  VAL A   9      -0.512  27.065 -29.258  1.00116.32           C  
ANISOU    5  CB  VAL A   9    11926  18392  13878    760    292   3119       C  
ATOM      6  CG1 VAL A   9      -0.826  27.328 -30.709  1.00125.27           C  
ANISOU    6  CG1 VAL A   9    13010  19517  15068    728    266   3195       C  
ATOM      7  CG2 VAL A   9       0.963  26.804 -29.035  1.00107.37           C  
ANISOU    7  CG2 VAL A   9    10887  17312  12594    879    326   2920       C  
ATOM      8  N   ALA A  10      -0.269  28.701 -26.127  1.00115.59           N  
ANISOU    8  N   ALA A  10    12034  17737  14146    505    146   3032       N  
ATOM      9  CA  ALA A  10      -0.617  29.138 -24.762  1.00107.62           C  
ANISOU    9  CA  ALA A  10    11131  16488  13269    418     82   2953       C  
ATOM     10  C   ALA A  10      -1.692  30.274 -24.794  1.00122.34           C  
ANISOU   10  C   ALA A  10    13005  18243  15236    351     41   2983       C  
ATOM     11  O   ALA A  10      -1.524  31.313 -24.132  1.00134.16           O  
ANISOU   11  O   ALA A  10    14490  19601  16882    270    -35   3048       O  
ATOM     12  CB  ALA A  10       0.628  29.650 -24.049  1.00107.71           C  
ANISOU   12  CB  ALA A  10    11090  16443  13390    361     25   3053       C  
ATOM     13  N   SER A  11      -2.779  30.075 -25.551  1.00115.87           N  
ANISOU   13  N   SER A  11    12206  17479  14338    391     85   2932       N  
ATOM     14  CA  SER A  11      -3.821  31.099 -25.761  1.00116.05           C  
ANISOU   14  CA  SER A  11    12228  17425  14441    342     52   2964       C  
ATOM     15  C   SER A  11      -4.687  31.409 -24.504  1.00114.14           C  
ANISOU   15  C   SER A  11    12113  16964  14291    288     -1   2826       C  
ATOM     16  O   SER A  11      -4.950  32.581 -24.202  1.00119.04           O  
ANISOU   16  O   SER A  11    12715  17470  15042    224    -74   2884       O  
ATOM     17  CB  SER A  11      -4.709  30.693 -26.964  1.00116.51           C  
ANISOU   17  CB  SER A  11    12272  17619  14375    409    118   2942       C  
ATOM     18  OG  SER A  11      -5.892  31.478 -27.072  1.00122.99           O  
ANISOU   18  OG  SER A  11    13118  18354  15257    371     92   2930       O  
ATOM     19  N   GLY A  12      -5.178  30.368 -23.848  1.00103.17           N  
ANISOU   19  N   GLY A  12    10844  15521  12834    317     26   2649       N  
ATOM     20  CA  GLY A  12      -6.079  30.531 -22.732  1.00 95.31           C  
ANISOU   20  CA  GLY A  12     9962  14358  11893    281     -9   2514       C  
ATOM     21  C   GLY A  12      -7.503  30.308 -23.177  1.00 94.20           C  
ANISOU   21  C   GLY A  12     9867  14237  11687    307     29   2430       C  
ATOM     22  O   GLY A  12      -7.789  29.396 -23.936  1.00 95.09           O  
ANISOU   22  O   GLY A  12     9980  14468  11682    366     91   2398       O  
ATOM     23  N   SER A  13      -8.405  31.149 -22.710  1.00 86.90           N  
ANISOU   23  N   SER A  13     8977  13200  10841    269    -15   2392       N  
ATOM     24  CA  SER A  13      -9.803  31.049 -23.146  1.00 93.98           C  
ANISOU   24  CA  SER A  13     9911  14108  11686    287     15   2317       C  
ATOM     25  C   SER A  13     -10.092  31.622 -24.551  1.00108.19           C  
ANISOU   25  C   SER A  13    11619  16011  13474    302     32   2433       C  
ATOM     26  O   SER A  13     -11.235  31.563 -25.026  1.00110.27           O  
ANISOU   26  O   SER A  13    11908  16294  13696    320     58   2379       O  
ATOM     27  CB  SER A  13     -10.656  31.771 -22.132  1.00 91.61           C  
ANISOU   27  CB  SER A  13     9674  13663  11470    250    -41   2234       C  
ATOM     28  OG  SER A  13     -10.254  31.378 -20.832  1.00 92.65           O  
ANISOU   28  OG  SER A  13     9876  13710  11616    238    -63   2148       O  
ATOM     29  N   GLY A  14      -9.062  32.167 -25.209  1.00113.12           N  
ANISOU   29  N   GLY A  14    12133  16710  14136    292     17   2598       N  
ATOM     30  CA  GLY A  14      -9.208  32.804 -26.511  1.00112.45           C  
ANISOU   30  CA  GLY A  14    11945  16733  14047    300     27   2736       C  
ATOM     31  C   GLY A  14      -9.738  34.224 -26.385  1.00109.78           C  
ANISOU   31  C   GLY A  14    11581  16278  13849    238    -55   2800       C  
ATOM     32  O   GLY A  14     -10.017  34.709 -25.280  1.00 98.01           O  
ANISOU   32  O   GLY A  14    10156  14626  12455    200   -122   2723       O  
ATOM     33  N   GLU A  15      -9.928  34.891 -27.509  1.00117.76           N  
ANISOU   33  N   GLU A  15    12495  17376  14869    235    -57   2939       N  
ATOM     34  CA  GLU A  15     -10.533  36.203 -27.493  1.00122.70           C  
ANISOU   34  CA  GLU A  15    13096  17898  15624    184   -141   2999       C  
ATOM     35  C   GLU A  15     -11.943  36.018 -27.001  1.00112.32           C  
ANISOU   35  C   GLU A  15    11901  16487  14288    202   -133   2806       C  
ATOM     36  O   GLU A  15     -12.578  35.037 -27.338  1.00111.73           O  
ANISOU   36  O   GLU A  15    11880  16489  14081    255    -49   2697       O  
ATOM     37  CB  GLU A  15     -10.556  36.788 -28.898  1.00132.54           C  
ANISOU   37  CB  GLU A  15    14225  19277  16854    187   -128   3170       C  
ATOM     38  CG  GLU A  15      -9.267  36.579 -29.663  1.00141.43           C  
ANISOU   38  CG  GLU A  15    15229  20604  17902    213    -75   3337       C  
ATOM     39  CD  GLU A  15      -8.076  37.224 -28.980  1.00151.16           C  
ANISOU   39  CD  GLU A  15    16398  21809  19226    163   -129   3457       C  
ATOM     40  OE1 GLU A  15      -8.073  37.302 -27.726  1.00155.72           O  
ANISOU   40  OE1 GLU A  15    17056  22272  19836    152   -150   3346       O  
ATOM     41  OE2 GLU A  15      -7.139  37.650 -29.700  1.00146.20           O1-
ANISOU   41  OE2 GLU A  15    15630  21283  18634    134   -151   3674       O1-
ATOM     42  N   PRO A  16     -12.475  36.908 -26.184  1.00 99.40           N  
ANISOU   42  N   PRO A  16    10304  14686  12777    163   -227   2760       N  
ATOM     43  CA  PRO A  16     -13.830  36.690 -25.671  1.00 99.98           C  
ANISOU   43  CA  PRO A  16    10476  14689  12820    185   -218   2582       C  
ATOM     44  C   PRO A  16     -14.853  36.526 -26.788  1.00 97.35           C  
ANISOU   44  C   PRO A  16    10131  14450  12405    218   -159   2575       C  
ATOM     45  O   PRO A  16     -14.569  36.855 -27.919  1.00 98.24           O  
ANISOU   45  O   PRO A  16    10154  14651  12520    216   -155   2718       O  
ATOM     46  CB  PRO A  16     -14.108  37.955 -24.886  1.00 98.21           C  
ANISOU   46  CB  PRO A  16    10263  14294  12757    148   -347   2571       C  
ATOM     47  CG  PRO A  16     -12.774  38.451 -24.502  1.00 97.29           C  
ANISOU   47  CG  PRO A  16    10089  14128  12747    104   -421   2694       C  
ATOM     48  CD  PRO A  16     -11.867  38.118 -25.628  1.00 96.21           C  
ANISOU   48  CD  PRO A  16     9858  14152  12545    104   -352   2853       C  
ATOM     49  N   ARG A  17     -16.034  36.016 -26.486  1.00106.16           N  
ANISOU   49  N   ARG A  17    11332  15557  13447    249   -114   2418       N  
ATOM     50  CA  ARG A  17     -17.044  35.829 -27.545  1.00115.04           C  
ANISOU   50  CA  ARG A  17    12445  16769  14495    282    -62   2409       C  
ATOM     51  C   ARG A  17     -18.040  36.974 -27.603  1.00111.05           C  
ANISOU   51  C   ARG A  17    11935  16180  14079    265   -130   2404       C  
ATOM     52  O   ARG A  17     -18.330  37.611 -26.577  1.00109.81           O  
ANISOU   52  O   ARG A  17    11819  15891  14011    246   -205   2332       O  
ATOM     53  CB  ARG A  17     -17.802  34.516 -27.376  1.00118.36           C  
ANISOU   53  CB  ARG A  17    12948  17236  14786    323     18   2256       C  
ATOM     54  CG  ARG A  17     -16.979  33.284 -27.715  1.00121.41           C  
ANISOU   54  CG  ARG A  17    13332  17731  15065    358     87   2263       C  
ATOM     55  CD  ARG A  17     -17.184  32.242 -26.639  1.00130.04           C  
ANISOU   55  CD  ARG A  17    14524  18776  16109    363    110   2115       C  
ATOM     56  NE  ARG A  17     -18.607  31.952 -26.464  1.00131.63           N  
ANISOU   56  NE  ARG A  17    14786  18952  16273    371    128   1995       N  
ATOM     57  CZ  ARG A  17     -19.137  31.317 -25.413  1.00145.52           C  
ANISOU   57  CZ  ARG A  17    16627  20656  18009    362    135   1870       C  
ATOM     58  NH1 ARG A  17     -18.362  30.865 -24.420  1.00145.92           N1+
ANISOU   58  NH1 ARG A  17    16714  20664  18065    347    127   1839       N1+
ATOM     59  NH2 ARG A  17     -20.457  31.111 -25.367  1.00134.95           N  
ANISOU   59  NH2 ARG A  17    15326  19311  16635    368    151   1781       N  
ATOM     60  N   GLU A  18     -18.573  37.192 -28.809  1.00 99.51           N  
ANISOU   60  N   GLU A  18    10421  14802  12584    281   -106   2472       N  
ATOM     61  CA  GLU A  18     -19.541  38.254 -29.081  1.00 99.17           C  
ANISOU   61  CA  GLU A  18    10365  14695  12618    270   -169   2480       C  
ATOM     62  C   GLU A  18     -20.979  37.790 -28.860  1.00 89.26           C  
ANISOU   62  C   GLU A  18     9188  13432  11294    303   -129   2313       C  
ATOM     63  O   GLU A  18     -21.524  37.022 -29.647  1.00 89.89           O  
ANISOU   63  O   GLU A  18     9273  13616  11264    339    -51   2286       O  
ATOM     64  CB  GLU A  18     -19.373  38.767 -30.524  1.00103.70           C  
ANISOU   64  CB  GLU A  18    10836  15371  13192    267   -167   2653       C  
ATOM     65  CG  GLU A  18     -17.969  39.312 -30.828  1.00105.16           C  
ANISOU   65  CG  GLU A  18    10922  15582  13450    227   -211   2849       C  
ATOM     66  CD  GLU A  18     -17.815  40.812 -30.549  1.00107.10           C  
ANISOU   66  CD  GLU A  18    11123  15687  13881    166   -351   2949       C  
ATOM     67  OE1 GLU A  18     -18.572  41.389 -29.719  1.00 94.13           O  
ANISOU   67  OE1 GLU A  18     9544  13896  12322    160   -428   2833       O  
ATOM     68  OE2 GLU A  18     -16.922  41.423 -31.178  1.00115.08           O1-
ANISOU   68  OE2 GLU A  18    12027  16739  14955    127   -394   3149       O1-
ATOM     69  N   GLU A  19     -21.598  38.275 -27.791  1.00 82.01           N  
ANISOU   69  N   GLU A  19     8324  12392  10440    297   -189   2201       N  
ATOM     70  CA  GLU A  19     -23.055  38.117 -27.602  1.00 88.35           C  
ANISOU   70  CA  GLU A  19     9182  13187  11197    325   -168   2062       C  
ATOM     71  C   GLU A  19     -23.872  38.381 -28.895  1.00 82.40           C  
ANISOU   71  C   GLU A  19     8387  12501  10417    341   -147   2112       C  
ATOM     72  O   GLU A  19     -23.557  39.275 -29.670  1.00 80.52           O  
ANISOU   72  O   GLU A  19     8079  12262  10251    324   -198   2246       O  
ATOM     73  CB  GLU A  19     -23.562  39.061 -26.490  1.00 90.23           C  
ANISOU   73  CB  GLU A  19     9453  13293  11535    324   -265   1971       C  
ATOM     74  CG  GLU A  19     -23.274  38.593 -25.073  1.00 95.18           C  
ANISOU   74  CG  GLU A  19    10143  13871  12148    328   -268   1860       C  
ATOM     75  CD  GLU A  19     -24.222  37.480 -24.677  1.00103.49           C  
ANISOU   75  CD  GLU A  19    11257  14988  13076    353   -179   1726       C  
ATOM     76  OE1 GLU A  19     -25.412  37.762 -24.334  1.00101.00           O  
ANISOU   76  OE1 GLU A  19    10964  14658  12751    378   -193   1625       O  
ATOM     77  OE2 GLU A  19     -23.770  36.316 -24.746  1.00110.79           O1-
ANISOU   77  OE2 GLU A  19    12201  15980  13912    348   -100   1728       O1-
ATOM     78  N   ALA A  20     -24.915  37.580 -29.090  1.00 79.27           N  
ANISOU   78  N   ALA A  20     8033  12164   9920    372    -77   2009       N  
ATOM     79  CA  ALA A  20     -25.928  37.765 -30.113  1.00 71.10           C  
ANISOU   79  CA  ALA A  20     6976  11182   8855    394    -59   2016       C  
ATOM     80  C   ALA A  20     -26.506  39.180 -30.024  1.00 75.25           C  
ANISOU   80  C   ALA A  20     7480  11611   9498    383   -158   2028       C  
ATOM     81  O   ALA A  20     -26.652  39.715 -28.911  1.00 77.82           O  
ANISOU   81  O   ALA A  20     7839  11833   9896    378   -225   1950       O  
ATOM     82  CB  ALA A  20     -27.034  36.752 -29.870  1.00 70.81           C  
ANISOU   82  CB  ALA A  20     7002  11183   8717    420      7   1872       C  
ATOM     83  N   GLY A  21     -26.865  39.768 -31.173  1.00 68.85           N  
ANISOU   83  N   GLY A  21     6616  10839   8706    387   -173   2119       N  
ATOM     84  CA  GLY A  21     -27.543  41.095 -31.224  1.00 62.91           C  
ANISOU   84  CA  GLY A  21     5841   9994   8065    382   -275   2129       C  
ATOM     85  C   GLY A  21     -26.587  42.230 -30.885  1.00 70.68           C  
ANISOU   85  C   GLY A  21     6784  10872   9200    342   -393   2237       C  
ATOM     86  O   GLY A  21     -26.974  43.202 -30.244  1.00 65.63           O  
ANISOU   86  O   GLY A  21     6158  10110   8669    342   -502   2186       O  
ATOM     87  N   ALA A  22     -25.314  42.077 -31.305  1.00 84.82           N  
ANISOU   87  N   ALA A  22     8520  12711  10995    312   -379   2384       N  
ATOM     88  CA  ALA A  22     -24.273  43.111 -31.229  1.00 81.86           C  
ANISOU   88  CA  ALA A  22     8082  12254  10764    262   -491   2533       C  
ATOM     89  C   ALA A  22     -24.067  43.677 -29.804  1.00 88.75           C  
ANISOU   89  C   ALA A  22     9003  12966  11749    253   -597   2440       C  
ATOM     90  O   ALA A  22     -23.587  44.816 -29.608  1.00 82.53           O  
ANISOU   90  O   ALA A  22     8177  12061  11117    219   -735   2526       O  
ATOM     91  CB  ALA A  22     -24.592  44.212 -32.211  1.00 79.03           C  
ANISOU   91  CB  ALA A  22     7654  11880  10494    242   -569   2666       C  
ATOM     92  N   LEU A  23     -24.380  42.850 -28.804  1.00 87.61           N  
ANISOU   92  N   LEU A  23     8940  12821  11526    285   -539   2270       N  
ATOM     93  CA  LEU A  23     -24.340  43.285 -27.416  1.00 87.46           C  
ANISOU   93  CA  LEU A  23     8972  12672  11584    295   -628   2155       C  
ATOM     94  C   LEU A  23     -22.907  43.356 -26.862  1.00 83.08           C  
ANISOU   94  C   LEU A  23     8399  12066  11099    258   -674   2235       C  
ATOM     95  O   LEU A  23     -22.722  43.544 -25.665  1.00 80.68           O  
ANISOU   95  O   LEU A  23     8141  11668  10843    271   -738   2136       O  
ATOM     96  CB  LEU A  23     -25.290  42.431 -26.546  1.00 86.07           C  
ANISOU   96  CB  LEU A  23     8878  12528  11293    343   -552   1954       C  
ATOM     97  CG  LEU A  23     -26.753  42.801 -26.846  1.00 95.44           C  
ANISOU   97  CG  LEU A  23    10076  13720  12463    381   -561   1867       C  
ATOM     98  CD1 LEU A  23     -27.745  41.739 -26.378  1.00101.55           C  
ANISOU   98  CD1 LEU A  23    10910  14576  13097    418   -454   1712       C  
ATOM     99  CD2 LEU A  23     -27.115  44.179 -26.286  1.00 94.10           C  
ANISOU   99  CD2 LEU A  23     9905  13411  12434    402   -720   1819       C  
ATOM    100  N   GLY A  24     -21.901  43.251 -27.735  1.00 81.49           N  
ANISOU  100  N   GLY A  24     8126  11933  10903    216   -647   2416       N  
ATOM    101  CA  GLY A  24     -20.517  43.481 -27.317  1.00 84.85           C  
ANISOU  101  CA  GLY A  24     8518  12307  11414    174   -706   2518       C  
ATOM    102  C   GLY A  24     -19.951  42.326 -26.495  1.00 82.25           C  
ANISOU  102  C   GLY A  24     8245  12019  10987    188   -618   2429       C  
ATOM    103  O   GLY A  24     -20.668  41.359 -26.181  1.00 74.12           O  
ANISOU  103  O   GLY A  24     7283  11049   9830    228   -520   2285       O  
ATOM    104  N   PRO A  25     -18.648  42.408 -26.153  1.00 83.01           N  
ANISOU  104  N   PRO A  25     8309  12084  11147    152   -658   2522       N  
ATOM    105  CA  PRO A  25     -18.013  41.269 -25.493  1.00 78.96           C  
ANISOU  105  CA  PRO A  25     7842  11620  10539    163   -572   2455       C  
ATOM    106  C   PRO A  25     -18.694  40.888 -24.161  1.00 73.89           C  
ANISOU  106  C   PRO A  25     7303  10912   9857    203   -569   2243       C  
ATOM    107  O   PRO A  25     -19.019  41.739 -23.332  1.00 70.74           O  
ANISOU  107  O   PRO A  25     6931  10389   9557    214   -681   2167       O  
ATOM    108  CB  PRO A  25     -16.554  41.720 -25.309  1.00 80.50           C  
ANISOU  108  CB  PRO A  25     7976  11766  10841    115   -646   2598       C  
ATOM    109  CG  PRO A  25     -16.557  43.205 -25.490  1.00 82.31           C  
ANISOU  109  CG  PRO A  25     8150  11875  11249     78   -804   2700       C  
ATOM    110  CD  PRO A  25     -17.697  43.512 -26.404  1.00 82.27           C  
ANISOU  110  CD  PRO A  25     8129  11912  11215     95   -785   2703       C  
ATOM    111  N   ALA A  26     -18.951  39.601 -24.028  1.00 70.89           N  
ANISOU  111  N   ALA A  26     6974  10628   9330    228   -445   2153       N  
ATOM    112  CA  ALA A  26     -19.500  39.008 -22.823  1.00 83.08           C  
ANISOU  112  CA  ALA A  26     8606  12148  10813    259   -420   1977       C  
ATOM    113  C   ALA A  26     -18.664  39.363 -21.561  1.00 78.54           C  
ANISOU  113  C   ALA A  26     8055  11464  10319    252   -506   1942       C  
ATOM    114  O   ALA A  26     -19.205  39.656 -20.487  1.00 74.27           O  
ANISOU  114  O   ALA A  26     7566  10855   9796    284   -559   1809       O  
ATOM    115  CB  ALA A  26     -19.548  37.491 -23.024  1.00 86.22           C  
ANISOU  115  CB  ALA A  26     9038  12665  11056    271   -284   1936       C  
ATOM    116  N   TRP A  27     -17.346  39.331 -21.718  1.00 68.51           N  
ANISOU  116  N   TRP A  27     6743  10191   9095    217   -521   2062       N  
ATOM    117  CA  TRP A  27     -16.431  39.614 -20.624  1.00 68.69           C  
ANISOU  117  CA  TRP A  27     6784  10116   9199    207   -602   2045       C  
ATOM    118  C   TRP A  27     -15.145  40.080 -21.281  1.00 69.08           C  
ANISOU  118  C   TRP A  27     6747  10156   9342    156   -648   2236       C  
ATOM    119  O   TRP A  27     -15.036  40.036 -22.498  1.00 66.04           O  
ANISOU  119  O   TRP A  27     6295   9862   8934    137   -601   2365       O  
ATOM    120  CB  TRP A  27     -16.216  38.332 -19.756  1.00 64.97           C  
ANISOU  120  CB  TRP A  27     6383   9693   8608    224   -512   1938       C  
ATOM    121  CG  TRP A  27     -15.916  37.145 -20.575  1.00 60.37           C  
ANISOU  121  CG  TRP A  27     5788   9241   7906    217   -385   1992       C  
ATOM    122  CD1 TRP A  27     -16.815  36.313 -21.180  1.00 63.25           C  
ANISOU  122  CD1 TRP A  27     6174   9707   8151    238   -285   1945       C  
ATOM    123  CD2 TRP A  27     -14.630  36.720 -21.003  1.00 61.07           C  
ANISOU  123  CD2 TRP A  27     5831   9380   7990    193   -356   2110       C  
ATOM    124  CE2 TRP A  27     -14.806  35.577 -21.826  1.00 63.26           C  
ANISOU  124  CE2 TRP A  27     6109   9791   8133    212   -239   2115       C  
ATOM    125  CE3 TRP A  27     -13.341  37.136 -20.710  1.00 62.24           C  
ANISOU  125  CE3 TRP A  27     5940   9476   8231    162   -422   2204       C  
ATOM    126  NE1 TRP A  27     -16.148  35.363 -21.955  1.00 59.53           N  
ANISOU  126  NE1 TRP A  27     5678   9341   7598    236   -201   2017       N  
ATOM    127  CZ2 TRP A  27     -13.741  34.878 -22.376  1.00 60.63           C  
ANISOU  127  CZ2 TRP A  27     5738   9548   7751    210   -186   2204       C  
ATOM    128  CZ3 TRP A  27     -12.285  36.426 -21.240  1.00 63.81           C  
ANISOU  128  CZ3 TRP A  27     6096   9767   8380    152   -361   2301       C  
ATOM    129  CH2 TRP A  27     -12.494  35.318 -22.074  1.00 66.05           C  
ANISOU  129  CH2 TRP A  27     6380  10191   8523    181   -244   2297       C  
ATOM    130  N   ASP A  28     -14.168  40.533 -20.501  1.00 72.20           N  
ANISOU  130  N   ASP A  28     7137  10452   9843    135   -743   2262       N  
ATOM    131  CA  ASP A  28     -12.857  40.818 -21.062  1.00 72.47           C  
ANISOU  131  CA  ASP A  28     7083  10496   9956     82   -777   2453       C  
ATOM    132  C   ASP A  28     -11.769  40.373 -20.126  1.00 73.59           C  
ANISOU  132  C   ASP A  28     7250  10603  10108     74   -787   2432       C  
ATOM    133  O   ASP A  28     -12.027  40.045 -18.967  1.00 73.05           O  
ANISOU  133  O   ASP A  28     7267  10481  10008    108   -793   2273       O  
ATOM    134  CB  ASP A  28     -12.695  42.311 -21.406  1.00 83.11           C  
ANISOU  134  CB  ASP A  28     8358  11730  11490     41   -936   2580       C  
ATOM    135  CG  ASP A  28     -12.445  43.148 -20.207  1.00 81.55           C  
ANISOU  135  CG  ASP A  28     8195  11354  11435     45  -1095   2507       C  
ATOM    136  OD1 ASP A  28     -13.405  43.411 -19.451  1.00 87.20           O  
ANISOU  136  OD1 ASP A  28     8985  11999  12149     98  -1140   2336       O  
ATOM    137  OD2 ASP A  28     -11.280  43.504 -20.008  1.00 86.26           O1-
ANISOU  137  OD2 ASP A  28     8743  11891  12137      1  -1174   2618       O1-
ATOM    138  N   GLU A  29     -10.544  40.382 -20.636  1.00 74.57           N  
ANISOU  138  N   GLU A  29     7292  10767  10273     30   -790   2601       N  
ATOM    139  CA  GLU A  29      -9.474  39.706 -19.973  1.00 80.30           C  
ANISOU  139  CA  GLU A  29     8034  11500  10973     25   -766   2594       C  
ATOM    140  C   GLU A  29      -9.177  40.270 -18.579  1.00 76.52           C  
ANISOU  140  C   GLU A  29     7610  10856  10608     27   -893   2500       C  
ATOM    141  O   GLU A  29      -8.733  39.543 -17.704  1.00 72.09           O  
ANISOU  141  O   GLU A  29     7106  10291   9992     45   -860   2412       O  
ATOM    142  CB  GLU A  29      -8.226  39.638 -20.848  1.00 92.50           C  
ANISOU  142  CB  GLU A  29     9469  13139  12537    -17   -744   2800       C  
ATOM    143  CG  GLU A  29      -7.599  38.246 -20.736  1.00107.00           C  
ANISOU  143  CG  GLU A  29    11332  15092  14228      9   -619   2760       C  
ATOM    144  CD  GLU A  29      -6.159  38.156 -21.211  1.00114.50           C  
ANISOU  144  CD  GLU A  29    12181  16120  15202    -23   -614   2937       C  
ATOM    145  OE1 GLU A  29      -5.908  38.458 -22.401  1.00117.34           O  
ANISOU  145  OE1 GLU A  29    12432  16589  15563    -41   -595   3108       O  
ATOM    146  OE2 GLU A  29      -5.291  37.752 -20.394  1.00109.60           O1-
ANISOU  146  OE2 GLU A  29    11586  15464  14590    -26   -625   2906       O1-
ATOM    147  N   SER A  30      -9.501  41.531 -18.324  1.00 76.37           N  
ANISOU  147  N   SER A  30     7580  10698  10739     19  -1044   2502       N  
ATOM    148  CA  SER A  30      -9.261  42.100 -16.985  1.00 73.40           C  
ANISOU  148  CA  SER A  30     7257  10163  10468     37  -1180   2396       C  
ATOM    149  C   SER A  30     -10.194  41.494 -15.937  1.00 71.04           C  
ANISOU  149  C   SER A  30     7072   9867  10052    110  -1129   2165       C  
ATOM    150  O   SER A  30     -10.077  41.773 -14.743  1.00 70.61           O  
ANISOU  150  O   SER A  30     7072   9711  10045    144  -1220   2049       O  
ATOM    151  CB  SER A  30      -9.442  43.619 -17.013  1.00 72.24           C  
ANISOU  151  CB  SER A  30     7071   9860  10516     21  -1373   2445       C  
ATOM    152  OG  SER A  30     -10.738  43.914 -17.478  1.00 73.31           O  
ANISOU  152  OG  SER A  30     7222  10014  10616     52  -1358   2384       O  
ATOM    153  N   GLN A  31     -11.139  40.673 -16.373  1.00 67.73           N  
ANISOU  153  N   GLN A  31     6685   9570   9479    136   -990   2101       N  
ATOM    154  CA  GLN A  31     -11.993  39.977 -15.429  1.00 68.16           C  
ANISOU  154  CA  GLN A  31     6833   9653   9411    195   -928   1907       C  
ATOM    155  C   GLN A  31     -11.358  38.653 -14.934  1.00 68.87           C  
ANISOU  155  C   GLN A  31     6965   9819   9382    193   -818   1873       C  
ATOM    156  O   GLN A  31     -11.846  38.028 -13.959  1.00 64.65           O  
ANISOU  156  O   GLN A  31     6506   9302   8754    234   -779   1726       O  
ATOM    157  CB  GLN A  31     -13.374  39.768 -16.055  1.00 68.28           C  
ANISOU  157  CB  GLN A  31     6861   9749   9330    220   -848   1852       C  
ATOM    158  CG  GLN A  31     -13.988  41.045 -16.576  1.00 67.41           C  
ANISOU  158  CG  GLN A  31     6710   9564   9337    222   -957   1887       C  
ATOM    159  CD  GLN A  31     -15.419  40.859 -17.008  1.00 66.84           C  
ANISOU  159  CD  GLN A  31     6660   9565   9170    257   -886   1807       C  
ATOM    160  NE2 GLN A  31     -16.290  40.797 -16.048  1.00 64.35           N  
ANISOU  160  NE2 GLN A  31     6407   9240   8800    316   -894   1637       N  
ATOM    161  OE1 GLN A  31     -15.729  40.762 -18.191  1.00 67.37           O  
ANISOU  161  OE1 GLN A  31     6682   9705   9208    233   -824   1899       O  
ATOM    162  N   LEU A  32     -10.237  38.283 -15.569  1.00 66.68           N  
ANISOU  162  N   LEU A  32     6633   9586   9114    148   -781   2014       N  
ATOM    163  CA  LEU A  32      -9.569  37.043 -15.325  1.00 61.53           C  
ANISOU  163  CA  LEU A  32     6009   9011   8356    146   -681   2002       C  
ATOM    164  C   LEU A  32      -8.405  37.277 -14.391  1.00 63.75           C  
ANISOU  164  C   LEU A  32     6295   9200   8724    133   -767   2012       C  
ATOM    165  O   LEU A  32      -7.615  38.169 -14.633  1.00 60.85           O  
ANISOU  165  O   LEU A  32     5861   8762   8495     98   -868   2131       O  
ATOM    166  CB  LEU A  32      -9.036  36.492 -16.653  1.00 59.74           C  
ANISOU  166  CB  LEU A  32     5711   8907   8078    119   -590   2147       C  
ATOM    167  CG  LEU A  32     -10.045  36.045 -17.711  1.00 64.26           C  
ANISOU  167  CG  LEU A  32     6276   9592   8547    135   -492   2146       C  
ATOM    168  CD1 LEU A  32      -9.424  35.005 -18.606  1.00 67.73           C  
ANISOU  168  CD1 LEU A  32     6680  10169   8884    136   -385   2225       C  
ATOM    169  CD2 LEU A  32     -11.320  35.439 -17.149  1.00 66.70           C  
ANISOU  169  CD2 LEU A  32     6674   9916   8753    173   -437   1978       C  
ATOM    170  N   ARG A  33      -8.278  36.444 -13.360  1.00 61.51           N  
ANISOU  170  N   ARG A  33     6086   8923   8361    158   -729   1897       N  
ATOM    171  CA  ARG A  33      -7.115  36.486 -12.485  1.00 62.92           C  
ANISOU  171  CA  ARG A  33     6273   9028   8603    149   -796   1903       C  
ATOM    172  C   ARG A  33      -5.868  35.985 -13.229  1.00 64.58           C  
ANISOU  172  C   ARG A  33     6419   9304   8815    107   -747   2052       C  
ATOM    173  O   ARG A  33      -5.985  35.279 -14.222  1.00 67.06           O  
ANISOU  173  O   ARG A  33     6704   9739   9035    102   -639   2109       O  
ATOM    174  CB  ARG A  33      -7.376  35.661 -11.236  1.00 61.13           C  
ANISOU  174  CB  ARG A  33     6142   8808   8276    188   -758   1746       C  
ATOM    175  CG  ARG A  33      -8.318  36.373 -10.265  1.00 64.02           C  
ANISOU  175  CG  ARG A  33     6558   9103   8664    240   -841   1604       C  
ATOM    176  CD  ARG A  33      -8.922  35.404  -9.265  1.00 62.25           C  
ANISOU  176  CD  ARG A  33     6415   8939   8296    280   -768   1460       C  
ATOM    177  NE  ARG A  33      -9.994  35.991  -8.479  1.00 66.92           N  
ANISOU  177  NE  ARG A  33     7042   9506   8875    341   -824   1326       N  
ATOM    178  CZ  ARG A  33      -9.843  36.749  -7.392  1.00 69.28           C  
ANISOU  178  CZ  ARG A  33     7365   9717   9240    390   -946   1237       C  
ATOM    179  NH1 ARG A  33      -8.657  37.066  -6.909  1.00 73.25           N1+
ANISOU  179  NH1 ARG A  33     7863  10128   9840    379  -1035   1269       N1+
ATOM    180  NH2 ARG A  33     -10.911  37.199  -6.777  1.00 72.32           N  
ANISOU  180  NH2 ARG A  33     7777  10110   9590    458   -984   1109       N  
ATOM    181  N   SER A  34      -4.680  36.367 -12.770  1.00 62.90           N  
ANISOU  181  N   SER A  34     6177   9016   8705     82   -831   2114       N  
ATOM    182  CA  SER A  34      -3.449  35.993 -13.472  1.00 65.68           C  
ANISOU  182  CA  SER A  34     6452   9439   9064     45   -794   2266       C  
ATOM    183  C   SER A  34      -2.590  35.034 -12.641  1.00 61.47           C  
ANISOU  183  C   SER A  34     5968   8916   8472     56   -758   2210       C  
ATOM    184  O   SER A  34      -2.462  35.159 -11.429  1.00 55.76           O  
ANISOU  184  O   SER A  34     5307   8094   7783     72   -825   2109       O  
ATOM    185  CB  SER A  34      -2.645  37.233 -13.843  1.00 75.01           C  
ANISOU  185  CB  SER A  34     7533  10542  10425     -4   -921   2429       C  
ATOM    186  OG  SER A  34      -2.315  37.934 -12.666  1.00 80.16           O  
ANISOU  186  OG  SER A  34     8222  11036  11198     -2  -1060   2365       O  
ATOM    187  N   TYR A  35      -2.043  34.035 -13.310  1.00 56.85           N  
ANISOU  187  N   TYR A  35     5355   8456   7788     56   -653   2269       N  
ATOM    188  CA  TYR A  35      -1.370  32.979 -12.620  1.00 57.06           C  
ANISOU  188  CA  TYR A  35     5434   8503   7740     72   -609   2206       C  
ATOM    189  C   TYR A  35      -0.054  32.751 -13.258  1.00 54.47           C  
ANISOU  189  C   TYR A  35     5018   8248   7428     52   -592   2348       C  
ATOM    190  O   TYR A  35       0.228  33.312 -14.279  1.00 58.55           O  
ANISOU  190  O   TYR A  35     5433   8820   7993     29   -599   2495       O  
ATOM    191  CB  TYR A  35      -2.211  31.713 -12.629  1.00 54.66           C  
ANISOU  191  CB  TYR A  35     5209   8286   7271    109   -493   2089       C  
ATOM    192  CG  TYR A  35      -3.463  31.907 -11.885  1.00 51.78           C  
ANISOU  192  CG  TYR A  35     4925   7863   6886    128   -509   1953       C  
ATOM    193  CD1 TYR A  35      -3.452  32.167 -10.553  1.00 53.29           C  
ANISOU  193  CD1 TYR A  35     5177   7954   7114    139   -579   1854       C  
ATOM    194  CD2 TYR A  35      -4.659  31.837 -12.508  1.00 54.89           C  
ANISOU  194  CD2 TYR A  35     5326   8310   7218    142   -456   1922       C  
ATOM    195  CE1 TYR A  35      -4.617  32.372  -9.876  1.00 49.98           C  
ANISOU  195  CE1 TYR A  35     4820   7503   6664    167   -593   1731       C  
ATOM    196  CE2 TYR A  35      -5.842  32.031 -11.842  1.00 53.91           C  
ANISOU  196  CE2 TYR A  35     5266   8148   7069    162   -468   1802       C  
ATOM    197  CZ  TYR A  35      -5.802  32.315 -10.533  1.00 48.34           C  
ANISOU  197  CZ  TYR A  35     4614   7356   6397    177   -536   1709       C  
ATOM    198  OH  TYR A  35      -6.977  32.489  -9.897  1.00 49.72           O  
ANISOU  198  OH  TYR A  35     4840   7517   6532    208   -544   1592       O  
ATOM    199  N   SER A  36       0.726  31.895 -12.626  1.00 54.68           N  
ANISOU  199  N   SER A  36     5084   8284   7407     65   -568   2304       N  
ATOM    200  CA  SER A  36       2.094  31.619 -12.978  1.00 57.40           C  
ANISOU  200  CA  SER A  36     5351   8690   7764     54   -561   2419       C  
ATOM    201  C   SER A  36       2.269  30.611 -14.079  1.00 56.43           C  
ANISOU  201  C   SER A  36     5188   8742   7509     88   -447   2463       C  
ATOM    202  O   SER A  36       3.404  30.341 -14.460  1.00 55.57           O  
ANISOU  202  O   SER A  36     5005   8712   7395     90   -434   2560       O  
ATOM    203  CB  SER A  36       2.796  31.033 -11.747  1.00 58.36           C  
ANISOU  203  CB  SER A  36     5547   8746   7882     62   -585   2329       C  
ATOM    204  OG  SER A  36       2.489  29.656 -11.585  1.00 60.83           O  
ANISOU  204  OG  SER A  36     5939   9126   8044    103   -491   2217       O  
ATOM    205  N   PHE A  37       1.194  29.998 -14.553  1.00 52.99           N  
ANISOU  205  N   PHE A  37     4800   8371   6961    122   -369   2384       N  
ATOM    206  CA  PHE A  37       1.324  28.847 -15.445  1.00 51.53           C  
ANISOU  206  CA  PHE A  37     4599   8342   6638    171   -271   2385       C  
ATOM    207  C   PHE A  37       0.642  29.156 -16.747  1.00 55.65           C  
ANISOU  207  C   PHE A  37     5054   8966   7123    184   -228   2457       C  
ATOM    208  O   PHE A  37      -0.253  29.964 -16.801  1.00 56.27           O  
ANISOU  208  O   PHE A  37     5138   8984   7256    160   -257   2455       O  
ATOM    209  CB  PHE A  37       0.735  27.538 -14.840  1.00 46.84           C  
ANISOU  209  CB  PHE A  37     4128   7739   5926    208   -221   2217       C  
ATOM    210  CG  PHE A  37      -0.681  27.698 -14.339  1.00 46.86           C  
ANISOU  210  CG  PHE A  37     4216   7665   5921    198   -223   2107       C  
ATOM    211  CD1 PHE A  37      -1.711  27.797 -15.203  1.00 46.25           C  
ANISOU  211  CD1 PHE A  37     4126   7644   5801    210   -182   2108       C  
ATOM    212  CD2 PHE A  37      -0.933  27.882 -12.997  1.00 50.06           C  
ANISOU  212  CD2 PHE A  37     4703   7947   6369    178   -274   2012       C  
ATOM    213  CE1 PHE A  37      -3.017  27.982 -14.736  1.00 50.89           C  
ANISOU  213  CE1 PHE A  37     4783   8168   6381    202   -186   2011       C  
ATOM    214  CE2 PHE A  37      -2.203  28.102 -12.523  1.00 48.59           C  
ANISOU  214  CE2 PHE A  37     4581   7709   6172    175   -278   1919       C  
ATOM    215  CZ  PHE A  37      -3.261  28.141 -13.399  1.00 50.30           C  
ANISOU  215  CZ  PHE A  37     4784   7984   6342    185   -232   1918       C  
ATOM    216  N   PRO A  38       1.041  28.471 -17.811  1.00 55.42           N  
ANISOU  216  N   PRO A  38     4962   9100   6995    233   -160   2512       N  
ATOM    217  CA  PRO A  38       0.374  28.681 -19.075  1.00 52.40           C  
ANISOU  217  CA  PRO A  38     4517   8828   6561    256   -114   2573       C  
ATOM    218  C   PRO A  38      -0.795  27.730 -19.262  1.00 55.76           C  
ANISOU  218  C   PRO A  38     5036   9278   6869    302    -55   2429       C  
ATOM    219  O   PRO A  38      -0.847  26.665 -18.568  1.00 54.07           O  
ANISOU  219  O   PRO A  38     4920   9030   6592    326    -39   2299       O  
ATOM    220  CB  PRO A  38       1.438  28.317 -20.063  1.00 53.70           C  
ANISOU  220  CB  PRO A  38     4569   9172   6661    301    -73   2690       C  
ATOM    221  CG  PRO A  38       2.161  27.198 -19.365  1.00 56.03           C  
ANISOU  221  CG  PRO A  38     4928   9463   6898    336    -62   2594       C  
ATOM    222  CD  PRO A  38       2.261  27.682 -17.952  1.00 51.73           C  
ANISOU  222  CD  PRO A  38     4455   8728   6469    271   -135   2544       C  
ATOM    223  N   THR A  39      -1.675  28.098 -20.222  1.00 52.34           N  
ANISOU  223  N   THR A  39     4568   8907   6410    313    -27   2462       N  
ATOM    224  CA  THR A  39      -2.894  27.353 -20.546  1.00 54.54           C  
ANISOU  224  CA  THR A  39     4920   9210   6591    352     21   2344       C  
ATOM    225  C   THR A  39      -3.197  27.292 -22.016  1.00 57.13           C  
ANISOU  225  C   THR A  39     5172   9694   6840    403     71   2409       C  
ATOM    226  O   THR A  39      -2.853  28.194 -22.765  1.00 57.97           O  
ANISOU  226  O   THR A  39     5168   9868   6989    389     63   2557       O  
ATOM    227  CB  THR A  39      -4.146  27.944 -19.904  1.00 50.89           C  
ANISOU  227  CB  THR A  39     4530   8617   6187    307     -7   2267       C  
ATOM    228  CG2 THR A  39      -4.046  27.877 -18.410  1.00 51.07           C  
ANISOU  228  CG2 THR A  39     4642   8500   6263    272    -51   2176       C  
ATOM    229  OG1 THR A  39      -4.339  29.306 -20.351  1.00 49.42           O  
ANISOU  229  OG1 THR A  39     4267   8411   6097    268    -45   2381       O  
ATOM    230  N   ARG A  40      -3.870  26.221 -22.416  1.00 55.10           N  
ANISOU  230  N   ARG A  40     4972   9493   6468    463    116   2301       N  
ATOM    231  CA  ARG A  40      -4.338  26.073 -23.800  1.00 58.82           C  
ANISOU  231  CA  ARG A  40     5385  10110   6851    524    160   2334       C  
ATOM    232  C   ARG A  40      -5.887  25.972 -23.688  1.00 57.08           C  
ANISOU  232  C   ARG A  40     5253   9813   6622    510    167   2225       C  
ATOM    233  O   ARG A  40      -6.386  25.572 -22.651  1.00 52.81           O  
ANISOU  233  O   ARG A  40     4814   9151   6099    479    149   2112       O  
ATOM    234  CB  ARG A  40      -3.728  24.790 -24.375  1.00 58.06           C  
ANISOU  234  CB  ARG A  40     5282  10148   6626    622    193   2287       C  
ATOM    235  N   PRO A  41      -6.634  26.393 -24.710  1.00 55.27           N  
ANISOU  235  N   PRO A  41     4977   9656   6367    529    189   2267       N  
ATOM    236  CA  PRO A  41      -8.082  26.418 -24.579  1.00 53.01           C  
ANISOU  236  CA  PRO A  41     4764   9295   6082    510    191   2174       C  
ATOM    237  C   PRO A  41      -8.733  25.061 -24.639  1.00 51.85           C  
ANISOU  237  C   PRO A  41     4701   9161   5835    561    212   2034       C  
ATOM    238  O   PRO A  41      -8.330  24.190 -25.387  1.00 48.52           O  
ANISOU  238  O   PRO A  41     4261   8853   5320    640    231   2018       O  
ATOM    239  CB  PRO A  41      -8.576  27.241 -25.805  1.00 55.37           C  
ANISOU  239  CB  PRO A  41     4976   9685   6377    523    208   2274       C  
ATOM    240  CG  PRO A  41      -7.429  27.166 -26.794  1.00 57.73           C  
ANISOU  240  CG  PRO A  41     5161  10154   6618    580    232   2394       C  
ATOM    241  CD  PRO A  41      -6.165  26.912 -26.020  1.00 59.18           C  
ANISOU  241  CD  PRO A  41     5341  10313   6830    568    213   2413       C  
ATOM    242  N   ILE A  42      -9.817  24.921 -23.896  1.00 50.45           N  
ANISOU  242  N   ILE A  42     4613   8873   5680    520    201   1935       N  
ATOM    243  CA  ILE A  42     -10.669  23.775 -24.086  1.00 49.36           C  
ANISOU  243  CA  ILE A  42     4546   8745   5464    557    211   1821       C  
ATOM    244  C   ILE A  42     -11.535  24.092 -25.296  1.00 47.54           C  
ANISOU  244  C   ILE A  42     4272   8595   5196    591    235   1845       C  
ATOM    245  O   ILE A  42     -12.042  25.233 -25.441  1.00 42.86           O  
ANISOU  245  O   ILE A  42     3640   7980   4662    552    236   1905       O  
ATOM    246  CB  ILE A  42     -11.527  23.533 -22.817  1.00 49.39           C  
ANISOU  246  CB  ILE A  42     4646   8614   5503    494    192   1724       C  
ATOM    247  CG1 ILE A  42     -10.612  23.289 -21.640  1.00 46.14           C  
ANISOU  247  CG1 ILE A  42     4272   8132   5126    463    168   1710       C  
ATOM    248  CG2 ILE A  42     -12.516  22.380 -23.003  1.00 51.19           C  
ANISOU  248  CG2 ILE A  42     4941   8844   5665    517    192   1622       C  
ATOM    249  CD1 ILE A  42     -11.316  23.416 -20.327  1.00 42.12           C  
ANISOU  249  CD1 ILE A  42     3833   7508   4661    398    149   1646       C  
ATOM    250  N   PRO A  43     -11.745  23.091 -26.136  1.00 46.20           N  
ANISOU  250  N   PRO A  43     4111   8509   4931    668    244   1790       N  
ATOM    251  CA  PRO A  43     -12.551  23.244 -27.336  1.00 45.99           C  
ANISOU  251  CA  PRO A  43     4047   8569   4856    714    264   1800       C  
ATOM    252  C   PRO A  43     -14.025  23.448 -26.994  1.00 53.34           C  
ANISOU  252  C   PRO A  43     5036   9407   5822    661    259   1737       C  
ATOM    253  O   PRO A  43     -14.520  22.762 -26.088  1.00 50.90           O  
ANISOU  253  O   PRO A  43     4811   9003   5523    626    239   1645       O  
ATOM    254  CB  PRO A  43     -12.405  21.887 -28.035  1.00 48.26           C  
ANISOU  254  CB  PRO A  43     4356   8941   5037    814    254   1719       C  
ATOM    255  CG  PRO A  43     -11.304  21.158 -27.355  1.00 49.14           C  
ANISOU  255  CG  PRO A  43     4495   9033   5142    827    232   1692       C  
ATOM    256  CD  PRO A  43     -11.205  21.732 -25.965  1.00 47.39           C  
ANISOU  256  CD  PRO A  43     4312   8672   5020    720    224   1707       C  
ATOM    257  N   ARG A  44     -14.687  24.369 -27.713  1.00 53.02           N  
ANISOU  257  N   ARG A  44     4944   9402   5797    657    276   1794       N  
ATOM    258  CA  ARG A  44     -16.120  24.654 -27.643  1.00 59.56           C  
ANISOU  258  CA  ARG A  44     5809  10171   6649    621    275   1744       C  
ATOM    259  C   ARG A  44     -16.705  24.126 -28.889  1.00 54.03           C  
ANISOU  259  C   ARG A  44     5093   9567   5866    695    287   1717       C  
ATOM    260  O   ARG A  44     -16.430  24.657 -29.962  1.00 53.37           O  
ANISOU  260  O   ARG A  44     4930   9593   5753    741    306   1801       O  
ATOM    261  CB  ARG A  44     -16.446  26.155 -27.593  1.00 63.29           C  
ANISOU  261  CB  ARG A  44     6234  10609   7205    568    275   1826       C  
ATOM    262  CG  ARG A  44     -15.670  26.905 -26.506  1.00 70.35           C  
ANISOU  262  CG  ARG A  44     7122  11415   8190    507    249   1872       C  
ATOM    263  CD  ARG A  44     -16.137  28.369 -26.373  1.00 74.95           C  
ANISOU  263  CD  ARG A  44     7669  11938   8868    458    225   1932       C  
ATOM    264  NE  ARG A  44     -17.496  28.453 -25.845  1.00 87.98           N  
ANISOU  264  NE  ARG A  44     9378  13516  10532    431    219   1838       N  
ATOM    265  CZ  ARG A  44     -18.599  28.598 -26.585  1.00 94.51           C  
ANISOU  265  CZ  ARG A  44    10198  14375  11335    447    233   1820       C  
ATOM    266  NH1 ARG A  44     -18.534  28.719 -27.914  1.00 94.71           N1+
ANISOU  266  NH1 ARG A  44    10160  14502  11320    491    252   1890       N1+
ATOM    267  NH2 ARG A  44     -19.785  28.647 -25.988  1.00 93.66           N  
ANISOU  267  NH2 ARG A  44    10139  14205  11239    422    227   1734       N  
ATOM    268  N   LEU A  45     -17.572  23.136 -28.742  1.00 49.58           N  
ANISOU  268  N   LEU A  45     4602   8964   5270    703    270   1608       N  
ATOM    269  CA  LEU A  45     -18.094  22.393 -29.841  1.00 47.72           C  
ANISOU  269  CA  LEU A  45     4368   8807   4957    782    263   1558       C  
ATOM    270  C   LEU A  45     -19.579  22.251 -29.675  1.00 50.23           C  
ANISOU  270  C   LEU A  45     4735   9054   5294    742    252   1489       C  
ATOM    271  O   LEU A  45     -20.115  22.423 -28.564  1.00 51.74           O  
ANISOU  271  O   LEU A  45     4971   9141   5544    660    247   1464       O  
ATOM    272  CB  LEU A  45     -17.454  21.018 -29.881  1.00 48.59           C  
ANISOU  272  CB  LEU A  45     4516   8938   5006    847    229   1485       C  
ATOM    273  CG  LEU A  45     -15.922  20.955 -29.920  1.00 56.56           C  
ANISOU  273  CG  LEU A  45     5481  10018   5988    892    235   1538       C  
ATOM    274  CD1 LEU A  45     -15.429  19.508 -30.002  1.00 54.74           C  
ANISOU  274  CD1 LEU A  45     5297   9804   5694    969    188   1443       C  
ATOM    275  CD2 LEU A  45     -15.463  21.725 -31.154  1.00 61.14           C  
ANISOU  275  CD2 LEU A  45     5954  10753   6520    958    272   1640       C  
ATOM    276  N   SER A  46     -20.240  21.936 -30.793  1.00 50.70           N  
ANISOU  276  N   SER A  46     4782   9183   5298    807    246   1460       N  
ATOM    277  CA  SER A  46     -21.620  21.501 -30.780  1.00 52.57           C  
ANISOU  277  CA  SER A  46     5067   9364   5540    785    224   1384       C  
ATOM    278  C   SER A  46     -21.756  20.027 -30.398  1.00 52.13           C  
ANISOU  278  C   SER A  46     5085   9253   5466    795    167   1286       C  
ATOM    279  O   SER A  46     -20.943  19.129 -30.699  1.00 50.59           O  
ANISOU  279  O   SER A  46     4903   9095   5224    865    134   1252       O  
ATOM    280  CB  SER A  46     -22.279  21.656 -32.137  1.00 52.72           C  
ANISOU  280  CB  SER A  46     5048   9473   5510    855    229   1385       C  
ATOM    281  OG  SER A  46     -23.601  21.120 -32.081  1.00 52.33           O  
ANISOU  281  OG  SER A  46     5048   9363   5471    831    199   1307       O  
ATOM    282  N   GLN A  47     -22.836  19.783 -29.704  1.00 50.58           N  
ANISOU  282  N   GLN A  47     4935   8969   5311    723    151   1245       N  
ATOM    283  CA  GLN A  47     -23.132  18.493 -29.188  1.00 52.67           C  
ANISOU  283  CA  GLN A  47     5268   9159   5583    701     90   1172       C  
ATOM    284  C   GLN A  47     -23.275  17.471 -30.298  1.00 55.25           C  
ANISOU  284  C   GLN A  47     5609   9527   5855    799     27   1103       C  
ATOM    285  O   GLN A  47     -23.064  16.309 -30.086  1.00 54.17           O  
ANISOU  285  O   GLN A  47     5520   9347   5713    818    -41   1045       O  
ATOM    286  CB  GLN A  47     -24.376  18.631 -28.331  1.00 56.77           C  
ANISOU  286  CB  GLN A  47     5808   9607   6154    602     98   1168       C  
ATOM    287  CG  GLN A  47     -25.288  17.445 -28.274  1.00 64.81           C  
ANISOU  287  CG  GLN A  47     6873  10568   7183    572     36   1110       C  
ATOM    288  CD  GLN A  47     -26.285  17.458 -29.371  1.00 60.45           C  
ANISOU  288  CD  GLN A  47     6308  10050   6607    625      9   1076       C  
ATOM    289  NE2 GLN A  47     -26.836  16.319 -29.660  1.00 69.62           N  
ANISOU  289  NE2 GLN A  47     7513  11168   7770    639    -74   1017       N  
ATOM    290  OE1 GLN A  47     -26.545  18.477 -29.958  1.00 59.67           O  
ANISOU  290  OE1 GLN A  47     6165  10011   6494    653     54   1101       O  
ATOM    291  N   SER A  48     -23.626  17.910 -31.490  1.00 58.26           N  
ANISOU  291  N   SER A  48     5945   9997   6194    869     44   1111       N  
ATOM    292  CA  SER A  48     -23.786  17.006 -32.648  1.00 64.09           C  
ANISOU  292  CA  SER A  48     6690  10788   6872    981    -18   1038       C  
ATOM    293  C   SER A  48     -22.496  16.739 -33.340  1.00 64.67           C  
ANISOU  293  C   SER A  48     6733  10967   6870   1098    -24   1035       C  
ATOM    294  O   SER A  48     -22.459  15.931 -34.291  1.00 65.52           O  
ANISOU  294  O   SER A  48     6846  11132   6916   1213    -86    963       O  
ATOM    295  CB  SER A  48     -24.707  17.634 -33.681  1.00 60.76           C  
ANISOU  295  CB  SER A  48     6228  10431   6426   1015      5   1048       C  
ATOM    296  OG  SER A  48     -24.135  18.869 -34.061  1.00 63.69           O  
ANISOU  296  OG  SER A  48     6527  10895   6777   1029     84   1142       O  
ATOM    297  N   ASP A  49     -21.445  17.424 -32.884  1.00 62.78           N  
ANISOU  297  N   ASP A  49     6457  10760   6636   1075     33   1113       N  
ATOM    298  CA  ASP A  49     -20.134  17.332 -33.494  1.00 59.59           C  
ANISOU  298  CA  ASP A  49     6005  10477   6158   1180     42   1133       C  
ATOM    299  C   ASP A  49     -19.476  16.054 -33.062  1.00 64.47           C  
ANISOU  299  C   ASP A  49     6681  11047   6766   1218    -32   1051       C  
ATOM    300  O   ASP A  49     -19.227  15.830 -31.859  1.00 58.02           O  
ANISOU  300  O   ASP A  49     5911  10120   6011   1129    -41   1053       O  
ATOM    301  CB  ASP A  49     -19.283  18.530 -33.101  1.00 62.12           C  
ANISOU  301  CB  ASP A  49     6263  10836   6503   1129    121   1254       C  
ATOM    302  CG  ASP A  49     -17.977  18.604 -33.891  1.00 66.78           C  
ANISOU  302  CG  ASP A  49     6777  11584   7010   1239    141   1303       C  
ATOM    303  OD1 ASP A  49     -17.538  17.547 -34.381  1.00 65.88           O  
ANISOU  303  OD1 ASP A  49     6678  11526   6824   1349     88   1222       O  
ATOM    304  OD2 ASP A  49     -17.371  19.700 -33.968  1.00 65.20           O1-
ANISOU  304  OD2 ASP A  49     6500  11451   6820   1214    202   1423       O1-
ATOM    305  N   PRO A  50     -19.154  15.198 -34.033  1.00 65.92           N  
ANISOU  305  N   PRO A  50     6861  11317   6868   1359    -92    974       N  
ATOM    306  CA  PRO A  50     -18.464  13.949 -33.671  1.00 65.56           C  
ANISOU  306  CA  PRO A  50     6871  11224   6813   1410   -179    887       C  
ATOM    307  C   PRO A  50     -17.231  14.183 -32.804  1.00 65.07           C  
ANISOU  307  C   PRO A  50     6797  11158   6768   1370   -139    946       C  
ATOM    308  O   PRO A  50     -16.849  13.300 -32.042  1.00 64.04           O  
ANISOU  308  O   PRO A  50     6728  10933   6668   1351   -203    891       O  
ATOM    309  CB  PRO A  50     -18.027  13.368 -35.033  1.00 65.51           C  
ANISOU  309  CB  PRO A  50     6828  11368   6692   1598   -228    816       C  
ATOM    310  CG  PRO A  50     -18.977  13.970 -36.011  1.00 69.11           C  
ANISOU  310  CG  PRO A  50     7244  11896   7117   1626   -197    834       C  
ATOM    311  CD  PRO A  50     -19.397  15.312 -35.478  1.00 67.21           C  
ANISOU  311  CD  PRO A  50     6970  11624   6942   1486    -92    958       C  
ATOM    312  N   ARG A  51     -16.568  15.325 -32.945  1.00 63.96           N  
ANISOU  312  N   ARG A  51     6575  11117   6609   1360    -45   1058       N  
ATOM    313  CA  ARG A  51     -15.342  15.512 -32.206  1.00 66.31           C  
ANISOU  313  CA  ARG A  51     6856  11416   6922   1333    -17   1111       C  
ATOM    314  C   ARG A  51     -15.647  15.638 -30.731  1.00 64.45           C  
ANISOU  314  C   ARG A  51     6685  11010   6792   1180    -13   1126       C  
ATOM    315  O   ARG A  51     -14.844  15.249 -29.903  1.00 58.61           O  
ANISOU  315  O   ARG A  51     5974  10217   6075   1156    -32   1119       O  
ATOM    316  CB  ARG A  51     -14.543  16.703 -32.707  1.00 70.38           C  
ANISOU  316  CB  ARG A  51     7261  12075   7402   1352     69   1240       C  
ATOM    317  CG  ARG A  51     -13.950  16.451 -34.104  1.00 78.27           C  
ANISOU  317  CG  ARG A  51     8183  13279   8274   1521     67   1233       C  
ATOM    318  CD  ARG A  51     -13.465  17.727 -34.828  1.00 80.42           C  
ANISOU  318  CD  ARG A  51     8329  13714   8510   1535    153   1384       C  
ATOM    319  NE  ARG A  51     -14.565  18.662 -35.200  1.00 81.60           N  
ANISOU  319  NE  ARG A  51     8459  13850   8695   1473    192   1441       N  
ATOM    320  CZ  ARG A  51     -14.435  19.995 -35.290  1.00 74.51           C  
ANISOU  320  CZ  ARG A  51     7480  12994   7834   1407    258   1587       C  
ATOM    321  NH1 ARG A  51     -13.278  20.585 -35.055  1.00 72.57           N1+
ANISOU  321  NH1 ARG A  51     7163  12810   7599   1387    294   1701       N1+
ATOM    322  NH2 ARG A  51     -15.455  20.746 -35.653  1.00 73.83           N  
ANISOU  322  NH2 ARG A  51     7382  12891   7778   1363    280   1624       N  
ATOM    323  N   ALA A  52     -16.813  16.167 -30.404  1.00 61.68           N  
ANISOU  323  N   ALA A  52     6354  10581   6500   1085      7   1144       N  
ATOM    324  CA  ALA A  52     -17.152  16.330 -29.012  1.00 58.27           C  
ANISOU  324  CA  ALA A  52     5974  10011   6155    952     14   1158       C  
ATOM    325  C   ALA A  52     -17.431  14.955 -28.417  1.00 62.34           C  
ANISOU  325  C   ALA A  52     6577  10419   6689    936    -75   1066       C  
ATOM    326  O   ALA A  52     -16.998  14.664 -27.292  1.00 64.62           O  
ANISOU  326  O   ALA A  52     6907  10625   7021    870    -89   1068       O  
ATOM    327  CB  ALA A  52     -18.309  17.272 -28.852  1.00 56.23           C  
ANISOU  327  CB  ALA A  52     5705   9717   5943    868     58   1198       C  
ATOM    328  N   GLU A  53     -18.033  14.059 -29.173  1.00 60.64           N  
ANISOU  328  N   GLU A  53     6386  10207   6444   1002   -145    987       N  
ATOM    329  CA  GLU A  53     -18.235  12.704 -28.687  1.00 65.53           C  
ANISOU  329  CA  GLU A  53     7084  10724   7089    998   -254    902       C  
ATOM    330  C   GLU A  53     -16.942  11.971 -28.506  1.00 64.35           C  
ANISOU  330  C   GLU A  53     6954  10578   6918   1057   -298    870       C  
ATOM    331  O   GLU A  53     -16.820  11.146 -27.650  1.00 61.67           O  
ANISOU  331  O   GLU A  53     6675  10129   6627    998   -357    846       O  
ATOM    332  CB  GLU A  53     -19.093  11.883 -29.621  1.00 71.36           C  
ANISOU  332  CB  GLU A  53     7838  11474   7800   1080   -335    820       C  
ATOM    333  CG  GLU A  53     -20.532  12.316 -29.713  1.00 89.10           C  
ANISOU  333  CG  GLU A  53    10150  13585  10119    994   -418    782       C  
ATOM    334  CD  GLU A  53     -21.307  12.158 -28.430  1.00 90.93           C  
ANISOU  334  CD  GLU A  53    10378  13758  10413    845   -351    856       C  
ATOM    335  OE1 GLU A  53     -21.637  11.026 -28.068  1.00 92.92           O  
ANISOU  335  OE1 GLU A  53    10583  14060  10661    804   -242    928       O  
ATOM    336  OE2 GLU A  53     -21.605  13.181 -27.799  1.00 88.69           O1-
ANISOU  336  OE2 GLU A  53    10137  13374  10185    767   -417    841       O1-
ATOM    337  N   GLU A  54     -15.995  12.246 -29.368  1.00 63.52           N  
ANISOU  337  N   GLU A  54     6789  10607   6736   1174   -270    876       N  
ATOM    338  CA  GLU A  54     -14.623  11.745 -29.256  1.00 66.82           C  
ANISOU  338  CA  GLU A  54     7203  11065   7118   1249   -296    854       C  
ATOM    339  C   GLU A  54     -13.977  12.135 -27.916  1.00 62.15           C  
ANISOU  339  C   GLU A  54     6627  10399   6586   1137   -252    920       C  
ATOM    340  O   GLU A  54     -13.528  11.281 -27.187  1.00 64.81           O  
ANISOU  340  O   GLU A  54     7020  10652   6949   1122   -317    877       O  
ATOM    341  CB  GLU A  54     -13.770  12.337 -30.404  1.00 78.91           C  
ANISOU  341  CB  GLU A  54     8638  12791   8551   1377   -238    889       C  
ATOM    342  CG  GLU A  54     -12.755  11.398 -31.050  1.00 92.59           C  
ANISOU  342  CG  GLU A  54    10361  14617  10199   1538   -308    807       C  
ATOM    343  CD  GLU A  54     -11.884  12.070 -32.120  1.00 94.86           C  
ANISOU  343  CD  GLU A  54    10535  15126  10381   1659   -237    865       C  
ATOM    344  OE1 GLU A  54     -12.407  12.907 -32.911  1.00 92.65           O  
ANISOU  344  OE1 GLU A  54    10192  14941  10069   1670   -174    925       O  
ATOM    345  OE2 GLU A  54     -10.677  11.732 -32.182  1.00 90.28           O1-
ANISOU  345  OE2 GLU A  54     9924  14630   9746   1746   -249    854       O1-
ATOM    346  N   LEU A  55     -13.969  13.426 -27.603  1.00 54.37           N  
ANISOU  346  N   LEU A  55     5591   9439   5626   1061   -151   1021       N  
ATOM    347  CA  LEU A  55     -13.368  13.920 -26.395  1.00 54.22           C  
ANISOU  347  CA  LEU A  55     5580   9357   5662    966   -112   1082       C  
ATOM    348  C   LEU A  55     -13.981  13.251 -25.177  1.00 53.62           C  
ANISOU  348  C   LEU A  55     5590   9129   5653    862   -163   1046       C  
ATOM    349  O   LEU A  55     -13.242  12.754 -24.337  1.00 50.56           O  
ANISOU  349  O   LEU A  55     5240   8685   5286    839   -193   1036       O  
ATOM    350  CB  LEU A  55     -13.457  15.468 -26.308  1.00 54.00           C  
ANISOU  350  CB  LEU A  55     5485   9367   5663    903    -15   1189       C  
ATOM    351  CG  LEU A  55     -12.604  16.193 -27.360  1.00 54.07           C  
ANISOU  351  CG  LEU A  55     5396   9533   5615    990     35   1257       C  
ATOM    352  CD1 LEU A  55     -12.943  17.654 -27.517  1.00 59.64           C  
ANISOU  352  CD1 LEU A  55     6036  10269   6355    934    107   1360       C  
ATOM    353  CD2 LEU A  55     -11.147  16.083 -27.029  1.00 53.45           C  
ANISOU  353  CD2 LEU A  55     5292   9491   5524   1021     36   1286       C  
ATOM    354  N   ILE A  56     -15.307  13.180 -25.080  1.00 48.57           N  
ANISOU  354  N   ILE A  56     4979   8430   5043    801   -176   1032       N  
ATOM    355  CA  ILE A  56     -15.946  12.631 -23.872  1.00 49.84           C  
ANISOU  355  CA  ILE A  56     5206   8465   5264    691   -216   1022       C  
ATOM    356  C   ILE A  56     -15.619  11.136 -23.712  1.00 56.01           C  
ANISOU  356  C   ILE A  56     6052   9178   6050    722   -332    950       C  
ATOM    357  O   ILE A  56     -15.237  10.681 -22.650  1.00 65.93           O  
ANISOU  357  O   ILE A  56     7351  10357   7341    661   -362    956       O  
ATOM    358  CB  ILE A  56     -17.477  12.837 -23.931  1.00 48.22           C  
ANISOU  358  CB  ILE A  56     5005   8231   5085    627   -210   1027       C  
ATOM    359  CG1 ILE A  56     -17.835  14.333 -23.984  1.00 46.64           C  
ANISOU  359  CG1 ILE A  56     4747   8084   4889    593   -107   1093       C  
ATOM    360  CG2 ILE A  56     -18.168  12.244 -22.717  1.00 48.83           C  
ANISOU  360  CG2 ILE A  56     5135   8201   5214    515   -251   1031       C  
ATOM    361  CD1 ILE A  56     -19.204  14.592 -24.564  1.00 48.34           C  
ANISOU  361  CD1 ILE A  56     4948   8311   5106    579    -98   1087       C  
ATOM    362  N   GLU A  57     -15.747  10.399 -24.816  1.00 61.44           N  
ANISOU  362  N   GLU A  57     6744   9897   6701    826   -403    879       N  
ATOM    363  CA  GLU A  57     -15.301   9.019 -24.962  1.00 61.64           C  
ANISOU  363  CA  GLU A  57     6822   9872   6724    895   -530    794       C  
ATOM    364  C   GLU A  57     -13.880   8.841 -24.424  1.00 62.87           C  
ANISOU  364  C   GLU A  57     6984  10035   6867    923   -531    795       C  
ATOM    365  O   GLU A  57     -13.619   7.941 -23.581  1.00 64.53           O  
ANISOU  365  O   GLU A  57     7255  10141   7120    881   -612    771       O  
ATOM    366  CB  GLU A  57     -15.382   8.629 -26.454  1.00 67.11           C  
ANISOU  366  CB  GLU A  57     7494  10649   7354   1044   -583    715       C  
ATOM    367  CG  GLU A  57     -15.175   7.177 -26.833  1.00 73.92           C  
ANISOU  367  CG  GLU A  57     8412  11458   8215   1138   -741    604       C  
ATOM    368  CD  GLU A  57     -15.851   6.213 -25.889  1.00 80.68           C  
ANISOU  368  CD  GLU A  57     9346  12144   9165   1027   -850    594       C  
ATOM    369  OE1 GLU A  57     -16.907   6.573 -25.319  1.00 89.41           O  
ANISOU  369  OE1 GLU A  57    10455  13192  10323    898   -813    658       O  
ATOM    370  OE2 GLU A  57     -15.304   5.101 -25.689  1.00 83.44           O1-
ANISOU  370  OE2 GLU A  57     9747  12420   9535   1069   -974    529       O1-
ATOM    371  N   ASN A  58     -12.984   9.718 -24.852  1.00 57.48           N  
ANISOU  371  N   ASN A  58     6234   9471   6132    983   -442    834       N  
ATOM    372  CA  ASN A  58     -11.604   9.643 -24.410  1.00 61.28           C  
ANISOU  372  CA  ASN A  58     6709   9974   6600   1014   -436    842       C  
ATOM    373  C   ASN A  58     -11.419  10.298 -23.054  1.00 57.70           C  
ANISOU  373  C   ASN A  58     6265   9451   6205    882   -373    921       C  
ATOM    374  O   ASN A  58     -10.314  10.418 -22.618  1.00 55.24           O  
ANISOU  374  O   ASN A  58     5943   9155   5889    893   -355    941       O  
ATOM    375  CB  ASN A  58     -10.655  10.305 -25.409  1.00 70.89           C  
ANISOU  375  CB  ASN A  58     7837  11358   7737   1131   -371    867       C  
ATOM    376  CG  ASN A  58     -10.048   9.324 -26.401  1.00 80.43           C  
ANISOU  376  CG  ASN A  58     9041  12646   8871   1297   -456    769       C  
ATOM    377  ND2 ASN A  58     -10.804   8.997 -27.463  1.00 75.67           N  
ANISOU  377  ND2 ASN A  58     8434  12089   8228   1379   -499    708       N  
ATOM    378  OD1 ASN A  58      -8.896   8.888 -26.229  1.00 87.65           O  
ANISOU  378  OD1 ASN A  58     9954  13588   9760   1359   -485    744       O  
ATOM    379  N   GLU A  59     -12.478  10.733 -22.373  1.00 55.98           N  
ANISOU  379  N   GLU A  59     6066   9165   6037    764   -341    962       N  
ATOM    380  CA  GLU A  59     -12.292  11.412 -21.089  1.00 51.43           C  
ANISOU  380  CA  GLU A  59     5495   8538   5506    656   -284   1027       C  
ATOM    381  C   GLU A  59     -11.404  12.607 -21.122  1.00 48.21           C  
ANISOU  381  C   GLU A  59     5021   8205   5088    670   -196   1092       C  
ATOM    382  O   GLU A  59     -10.578  12.795 -20.256  1.00 50.56           O  
ANISOU  382  O   GLU A  59     5326   8473   5409    636   -183   1119       O  
ATOM    383  CB  GLU A  59     -11.763  10.415 -20.058  1.00 54.42           C  
ANISOU  383  CB  GLU A  59     5940   8822   5915    619   -358   1002       C  
ATOM    384  CG  GLU A  59     -12.888   9.422 -19.787  1.00 59.55           C  
ANISOU  384  CG  GLU A  59     6649   9380   6597    563   -443    971       C  
ATOM    385  CD  GLU A  59     -12.628   8.551 -18.630  1.00 66.03           C  
ANISOU  385  CD  GLU A  59     7530  10098   7457    496   -512    970       C  
ATOM    386  OE1 GLU A  59     -11.787   7.639 -18.774  1.00 72.25           O  
ANISOU  386  OE1 GLU A  59     8350  10860   8240    561   -595    918       O  
ATOM    387  OE2 GLU A  59     -13.256   8.828 -17.594  1.00 66.48           O1-
ANISOU  387  OE2 GLU A  59     7599  10114   7546    385   -483   1023       O1-
ATOM    388  N   GLU A  60     -11.582  13.421 -22.129  1.00 49.42           N  
ANISOU  388  N   GLU A  60     5109   8454   5213    718   -142   1122       N  
ATOM    389  CA  GLU A  60     -10.947  14.713 -22.237  1.00 50.44           C  
ANISOU  389  CA  GLU A  60     5164   8651   5346    715    -63   1204       C  
ATOM    390  C   GLU A  60     -12.027  15.812 -22.153  1.00 46.39           C  
ANISOU  390  C   GLU A  60     4628   8126   4869    644     -8   1251       C  
ATOM    391  O   GLU A  60     -13.144  15.633 -22.598  1.00 47.82           O  
ANISOU  391  O   GLU A  60     4823   8304   5041    641    -16   1222       O  
ATOM    392  CB  GLU A  60     -10.193  14.786 -23.558  1.00 53.34           C  
ANISOU  392  CB  GLU A  60     5460   9158   5647    836    -50   1216       C  
ATOM    393  CG  GLU A  60      -8.755  14.294 -23.524  1.00 59.21           C  
ANISOU  393  CG  GLU A  60     6189   9946   6360    904    -73   1209       C  
ATOM    394  CD  GLU A  60      -8.277  13.822 -24.886  1.00 64.29           C  
ANISOU  394  CD  GLU A  60     6782  10733   6913   1050    -91   1176       C  
ATOM    395  OE1 GLU A  60      -8.042  12.599 -25.055  1.00 76.65           O  
ANISOU  395  OE1 GLU A  60     8393  12288   8441   1126   -170   1081       O  
ATOM    396  OE2 GLU A  60      -8.166  14.657 -25.813  1.00 70.22           O1-
ANISOU  396  OE2 GLU A  60     7443  11610   7625   1095    -33   1244       O1-
ATOM    397  N   PRO A  61     -11.690  16.966 -21.584  1.00 45.77           N  
ANISOU  397  N   PRO A  61     4516   8039   4835    592     40   1320       N  
ATOM    398  CA  PRO A  61     -12.722  17.939 -21.412  1.00 45.05           C  
ANISOU  398  CA  PRO A  61     4410   7926   4780    531     76   1349       C  
ATOM    399  C   PRO A  61     -13.225  18.549 -22.701  1.00 44.78           C  
ANISOU  399  C   PRO A  61     4314   7978   4720    578    107   1379       C  
ATOM    400  O   PRO A  61     -12.492  18.741 -23.648  1.00 45.24           O  
ANISOU  400  O   PRO A  61     4312   8133   4744    649    122   1418       O  
ATOM    401  CB  PRO A  61     -12.030  19.019 -20.533  1.00 44.27           C  
ANISOU  401  CB  PRO A  61     4286   7794   4740    481    101   1410       C  
ATOM    402  CG  PRO A  61     -10.601  18.883 -20.859  1.00 44.87           C  
ANISOU  402  CG  PRO A  61     4325   7922   4799    535     97   1444       C  
ATOM    403  CD  PRO A  61     -10.456  17.390 -20.906  1.00 45.03           C  
ANISOU  403  CD  PRO A  61     4403   7934   4771    577     50   1366       C  
ATOM    404  N   VAL A  62     -14.477  18.952 -22.700  1.00 45.29           N  
ANISOU  404  N   VAL A  62     4386   8018   4802    537    121   1370       N  
ATOM    405  CA  VAL A  62     -15.032  19.665 -23.859  1.00 47.06           C  
ANISOU  405  CA  VAL A  62     4552   8317   5009    573    151   1404       C  
ATOM    406  C   VAL A  62     -16.163  20.590 -23.428  1.00 44.51           C  
ANISOU  406  C   VAL A  62     4229   7948   4734    505    173   1416       C  
ATOM    407  O   VAL A  62     -16.860  20.280 -22.507  1.00 43.07           O  
ANISOU  407  O   VAL A  62     4098   7696   4570    448    160   1373       O  
ATOM    408  CB  VAL A  62     -15.585  18.665 -24.913  1.00 45.66           C  
ANISOU  408  CB  VAL A  62     4389   8191   4768    644    124   1343       C  
ATOM    409  CG1 VAL A  62     -16.710  17.826 -24.354  1.00 44.79           C  
ANISOU  409  CG1 VAL A  62     4350   7997   4669    595     85   1272       C  
ATOM    410  CG2 VAL A  62     -16.051  19.408 -26.145  1.00 47.32           C  
ANISOU  410  CG2 VAL A  62     4534   8491   4953    689    157   1383       C  
ATOM    411  N   VAL A  63     -16.332  21.724 -24.086  1.00 45.30           N  
ANISOU  411  N   VAL A  63     4266   8093   4852    513    203   1477       N  
ATOM    412  CA  VAL A  63     -17.410  22.642 -23.740  1.00 45.39           C  
ANISOU  412  CA  VAL A  63     4274   8063   4909    461    215   1480       C  
ATOM    413  C   VAL A  63     -18.448  22.479 -24.854  1.00 45.88           C  
ANISOU  413  C   VAL A  63     4322   8179   4931    496    224   1461       C  
ATOM    414  O   VAL A  63     -18.129  22.669 -26.002  1.00 43.19           O  
ANISOU  414  O   VAL A  63     3929   7921   4558    555    236   1502       O  
ATOM    415  CB  VAL A  63     -16.963  24.100 -23.696  1.00 44.61           C  
ANISOU  415  CB  VAL A  63     4115   7959   4873    442    225   1563       C  
ATOM    416  CG1 VAL A  63     -18.174  25.007 -23.717  1.00 48.57           C  
ANISOU  416  CG1 VAL A  63     4606   8438   5410    414    230   1558       C  
ATOM    417  CG2 VAL A  63     -16.195  24.373 -22.434  1.00 43.23           C  
ANISOU  417  CG2 VAL A  63     3961   7712   4751    399    206   1568       C  
ATOM    418  N   LEU A  64     -19.649  22.079 -24.489  1.00 45.27           N  
ANISOU  418  N   LEU A  64     4287   8060   4851    462    216   1400       N  
ATOM    419  CA  LEU A  64     -20.759  21.876 -25.415  1.00 46.78           C  
ANISOU  419  CA  LEU A  64     4473   8289   5012    488    217   1373       C  
ATOM    420  C   LEU A  64     -21.661  23.071 -25.320  1.00 45.97           C  
ANISOU  420  C   LEU A  64     4341   8173   4950    452    239   1395       C  
ATOM    421  O   LEU A  64     -22.098  23.434 -24.231  1.00 45.06           O  
ANISOU  421  O   LEU A  64     4247   8002   4871    396    239   1378       O  
ATOM    422  CB  LEU A  64     -21.530  20.631 -25.012  1.00 47.87           C  
ANISOU  422  CB  LEU A  64     4673   8384   5131    464    183   1300       C  
ATOM    423  CG  LEU A  64     -20.596  19.417 -25.020  1.00 50.26           C  
ANISOU  423  CG  LEU A  64     5010   8682   5402    501    143   1271       C  
ATOM    424  CD1 LEU A  64     -21.253  18.223 -24.391  1.00 49.33           C  
ANISOU  424  CD1 LEU A  64     4954   8501   5287    459     94   1215       C  
ATOM    425  CD2 LEU A  64     -20.198  19.069 -26.446  1.00 55.49           C  
ANISOU  425  CD2 LEU A  64     5643   9430   6010    601    132   1265       C  
ATOM    426  N   THR A  65     -21.901  23.694 -26.451  1.00 44.46           N  
ANISOU  426  N   THR A  65     4100   8043   4750    492    254   1433       N  
ATOM    427  CA  THR A  65     -22.502  24.986 -26.490  1.00 48.88           C  
ANISOU  427  CA  THR A  65     4622   8592   5356    469    267   1468       C  
ATOM    428  C   THR A  65     -23.997  24.929 -26.683  1.00 50.68           C  
ANISOU  428  C   THR A  65     4863   8816   5575    457    269   1417       C  
ATOM    429  O   THR A  65     -24.669  25.919 -26.391  1.00 44.30           O  
ANISOU  429  O   THR A  65     4038   7984   4810    430    273   1423       O  
ATOM    430  CB  THR A  65     -21.994  25.796 -27.716  1.00 53.22           C  
ANISOU  430  CB  THR A  65     5098   9216   5904    516    280   1555       C  
ATOM    431  CG2 THR A  65     -20.524  26.062 -27.600  1.00 54.18           C  
ANISOU  431  CG2 THR A  65     5186   9354   6043    523    278   1628       C  
ATOM    432  OG1 THR A  65     -22.182  25.024 -28.897  1.00 52.37           O  
ANISOU  432  OG1 THR A  65     4982   9191   5723    582    285   1538       O  
ATOM    433  N   ASP A  66     -24.517  23.799 -27.166  1.00 51.26           N  
ANISOU  433  N   ASP A  66     4966   8912   5598    480    259   1366       N  
ATOM    434  CA  ASP A  66     -25.916  23.745 -27.504  1.00 56.23           C  
ANISOU  434  CA  ASP A  66     5598   9545   6219    472    258   1328       C  
ATOM    435  C   ASP A  66     -26.662  22.509 -26.955  1.00 55.42           C  
ANISOU  435  C   ASP A  66     5549   9407   6101    438    230   1262       C  
ATOM    436  O   ASP A  66     -27.421  21.908 -27.682  1.00 52.24           O  
ANISOU  436  O   ASP A  66     5152   9022   5673    460    211   1230       O  
ATOM    437  CB  ASP A  66     -26.024  23.805 -29.029  1.00 55.39           C  
ANISOU  437  CB  ASP A  66     5455   9514   6074    542    261   1346       C  
ATOM    438  CG  ASP A  66     -25.259  22.681 -29.727  1.00 58.91           C  
ANISOU  438  CG  ASP A  66     5914  10006   6461    610    239   1327       C  
ATOM    439  OD1 ASP A  66     -24.626  21.884 -29.038  1.00 55.84           O  
ANISOU  439  OD1 ASP A  66     5564   9581   6070    597    218   1302       O  
ATOM    440  OD2 ASP A  66     -25.288  22.583 -30.977  1.00 64.12           O1-
ANISOU  440  OD2 ASP A  66     6544  10743   7073    683    237   1332       O1-
ATOM    441  N   THR A  67     -26.410  22.057 -25.727  1.00 54.32           N  
ANISOU  441  N   THR A  67     5444   9217   5975    386    220   1248       N  
ATOM    442  CA  THR A  67     -27.076  20.812 -25.275  1.00 44.95           C  
ANISOU  442  CA  THR A  67     4300   8000   4777    349    184   1206       C  
ATOM    443  C   THR A  67     -28.511  21.063 -24.891  1.00 46.14           C  
ANISOU  443  C   THR A  67     4438   8152   4938    300    193   1192       C  
ATOM    444  O   THR A  67     -29.290  20.142 -24.938  1.00 50.87           O  
ANISOU  444  O   THR A  67     5055   8741   5531    276    160   1171       O  
ATOM    445  CB  THR A  67     -26.420  20.226 -24.028  1.00 46.56           C  
ANISOU  445  CB  THR A  67     4541   8158   4990    302    169   1206       C  
ATOM    446  CG2 THR A  67     -25.037  19.786 -24.329  1.00 51.03           C  
ANISOU  446  CG2 THR A  67     5122   8722   5543    349    153   1212       C  
ATOM    447  OG1 THR A  67     -26.438  21.185 -22.947  1.00 45.97           O  
ANISOU  447  OG1 THR A  67     4452   8074   4938    262    202   1223       O  
ATOM    448  N   ASN A  68     -28.805  22.279 -24.421  1.00 40.97           N  
ANISOU  448  N   ASN A  68     3754   7508   4305    285    230   1206       N  
ATOM    449  CA  ASN A  68     -30.031  22.636 -23.748  1.00 44.81           C  
ANISOU  449  CA  ASN A  68     4223   8006   4795    243    243   1191       C  
ATOM    450  C   ASN A  68     -30.218  21.879 -22.464  1.00 45.59           C  
ANISOU  450  C   ASN A  68     4344   8093   4885    181    232   1186       C  
ATOM    451  O   ASN A  68     -31.365  21.658 -21.994  1.00 46.30           O  
ANISOU  451  O   ASN A  68     4418   8210   4964    140    233   1180       O  
ATOM    452  CB  ASN A  68     -31.285  22.469 -24.637  1.00 47.64           C  
ANISOU  452  CB  ASN A  68     4563   8393   5144    250    236   1174       C  
ATOM    453  CG  ASN A  68     -31.283  23.398 -25.839  1.00 51.35           C  
ANISOU  453  CG  ASN A  68     5001   8887   5620    308    252   1184       C  
ATOM    454  ND2 ASN A  68     -31.151  22.831 -27.001  1.00 53.41           N  
ANISOU  454  ND2 ASN A  68     5268   9163   5862    353    233   1181       N  
ATOM    455  OD1 ASN A  68     -31.417  24.616 -25.707  1.00 53.78           O  
ANISOU  455  OD1 ASN A  68     5279   9203   5951    317    274   1194       O  
ATOM    456  N   LEU A  69     -29.111  21.499 -21.855  1.00 48.29           N  
ANISOU  456  N   LEU A  69     4716   8403   5228    174    222   1197       N  
ATOM    457  CA  LEU A  69     -29.186  20.581 -20.705  1.00 46.63           C  
ANISOU  457  CA  LEU A  69     4529   8180   5005    114    203   1202       C  
ATOM    458  C   LEU A  69     -30.047  21.192 -19.661  1.00 45.99           C  
ANISOU  458  C   LEU A  69     4418   8144   4912     81    230   1200       C  
ATOM    459  O   LEU A  69     -30.857  20.497 -19.075  1.00 46.23           O  
ANISOU  459  O   LEU A  69     4441   8200   4924     28    220   1213       O  
ATOM    460  CB  LEU A  69     -27.813  20.266 -20.166  1.00 44.94           C  
ANISOU  460  CB  LEU A  69     4350   7927   4796    116    191   1212       C  
ATOM    461  CG  LEU A  69     -27.702  19.416 -18.914  1.00 44.31           C  
ANISOU  461  CG  LEU A  69     4295   7833   4705     57    171   1225       C  
ATOM    462  CD1 LEU A  69     -28.425  18.108 -19.119  1.00 45.11           C  
ANISOU  462  CD1 LEU A  69     4410   7922   4804     14    123   1235       C  
ATOM    463  CD2 LEU A  69     -26.213  19.222 -18.591  1.00 44.27           C  
ANISOU  463  CD2 LEU A  69     4325   7785   4709     74    159   1229       C  
ATOM    464  N   VAL A  70     -29.859  22.492 -19.421  1.00 48.07           N  
ANISOU  464  N   VAL A  70     4658   8418   5186    115    258   1185       N  
ATOM    465  CA  VAL A  70     -30.630  23.200 -18.384  1.00 46.86           C  
ANISOU  465  CA  VAL A  70     4473   8317   5014    105    278   1166       C  
ATOM    466  C   VAL A  70     -31.337  24.425 -18.938  1.00 46.28           C  
ANISOU  466  C   VAL A  70     4361   8266   4956    148    291   1140       C  
ATOM    467  O   VAL A  70     -31.433  25.486 -18.260  1.00 43.17           O  
ANISOU  467  O   VAL A  70     3946   7890   4567    176    295   1110       O  
ATOM    468  CB  VAL A  70     -29.742  23.614 -17.185  1.00 46.20           C  
ANISOU  468  CB  VAL A  70     4403   8221   4929    110    277   1158       C  
ATOM    469  CG1 VAL A  70     -29.259  22.378 -16.379  1.00 46.55           C  
ANISOU  469  CG1 VAL A  70     4480   8257   4950     60    263   1185       C  
ATOM    470  CG2 VAL A  70     -28.596  24.416 -17.687  1.00 42.06           C  
ANISOU  470  CG2 VAL A  70     3889   7637   4452    154    268   1159       C  
ATOM    471  N   TYR A  71     -31.887  24.255 -20.146  1.00 47.55           N  
ANISOU  471  N   TYR A  71     4513   8428   5125    157    290   1146       N  
ATOM    472  CA  TYR A  71     -32.638  25.325 -20.793  1.00 49.62           C  
ANISOU  472  CA  TYR A  71     4739   8711   5403    195    299   1126       C  
ATOM    473  C   TYR A  71     -33.625  26.000 -19.791  1.00 49.18           C  
ANISOU  473  C   TYR A  71     4646   8716   5324    197    311   1089       C  
ATOM    474  O   TYR A  71     -33.634  27.189 -19.664  1.00 54.47           O  
ANISOU  474  O   TYR A  71     5296   9381   6016    240    304   1060       O  
ATOM    475  CB  TYR A  71     -33.312  24.830 -22.104  1.00 49.24           C  
ANISOU  475  CB  TYR A  71     4685   8670   5354    198    296   1134       C  
ATOM    476  CG  TYR A  71     -34.341  25.754 -22.663  1.00 50.31           C  
ANISOU  476  CG  TYR A  71     4781   8837   5498    227    305   1113       C  
ATOM    477  CD1 TYR A  71     -33.987  26.920 -23.343  1.00 52.16           C  
ANISOU  477  CD1 TYR A  71     5000   9049   5769    274    302   1116       C  
ATOM    478  CD2 TYR A  71     -35.679  25.510 -22.440  1.00 57.52           C  
ANISOU  478  CD2 TYR A  71     5665   9805   6385    203    312   1097       C  
ATOM    479  CE1 TYR A  71     -34.963  27.805 -23.792  1.00 55.34           C  
ANISOU  479  CE1 TYR A  71     5367   9476   6183    300    302   1095       C  
ATOM    480  CE2 TYR A  71     -36.661  26.373 -22.912  1.00 59.14           C  
ANISOU  480  CE2 TYR A  71     5832  10042   6597    232    319   1072       C  
ATOM    481  CZ  TYR A  71     -36.306  27.529 -23.569  1.00 59.65           C  
ANISOU  481  CZ  TYR A  71     5888  10075   6698    282    313   1067       C  
ATOM    482  OH  TYR A  71     -37.340  28.372 -23.998  1.00 73.76           O  
ANISOU  482  OH  TYR A  71     7639  11892   8495    311    312   1040       O  
ATOM    483  N   PRO A  72     -34.417  25.248 -19.059  1.00 50.48           N  
ANISOU  483  N   PRO A  72     4795   8941   5443    155    321   1093       N  
ATOM    484  CA  PRO A  72     -35.430  25.967 -18.249  1.00 52.54           C  
ANISOU  484  CA  PRO A  72     5007   9284   5669    174    335   1056       C  
ATOM    485  C   PRO A  72     -34.889  26.752 -17.080  1.00 54.74           C  
ANISOU  485  C   PRO A  72     5285   9575   5938    210    329   1020       C  
ATOM    486  O   PRO A  72     -35.623  27.591 -16.552  1.00 52.03           O  
ANISOU  486  O   PRO A  72     4901   9296   5571    253    329    971       O  
ATOM    487  CB  PRO A  72     -36.361  24.865 -17.732  1.00 50.07           C  
ANISOU  487  CB  PRO A  72     4667   9049   5305    112    347   1090       C  
ATOM    488  CG  PRO A  72     -36.095  23.673 -18.572  1.00 53.77           C  
ANISOU  488  CG  PRO A  72     5172   9458   5799     65    328   1135       C  
ATOM    489  CD  PRO A  72     -34.639  23.795 -19.027  1.00 57.16           C  
ANISOU  489  CD  PRO A  72     5655   9794   6269     92    313   1133       C  
ATOM    490  N   ALA A  73     -33.624  26.519 -16.693  1.00 53.68           N  
ANISOU  490  N   ALA A  73     5193   9381   5822    202    316   1035       N  
ATOM    491  CA  ALA A  73     -33.016  27.258 -15.592  1.00 51.18           C  
ANISOU  491  CA  ALA A  73     4879   9065   5502    240    300    997       C  
ATOM    492  C   ALA A  73     -32.364  28.574 -16.038  1.00 54.21           C  
ANISOU  492  C   ALA A  73     5269   9369   5957    298    264    968       C  
ATOM    493  O   ALA A  73     -31.911  29.416 -15.228  1.00 52.30           O  
ANISOU  493  O   ALA A  73     5029   9112   5731    343    231    924       O  
ATOM    494  CB  ALA A  73     -32.014  26.380 -14.898  1.00 53.40           C  
ANISOU  494  CB  ALA A  73     5198   9320   5769    201    299   1030       C  
ATOM    495  N   LEU A  74     -32.312  28.794 -17.331  1.00 52.69           N  
ANISOU  495  N   LEU A  74     5079   9127   5813    300    260    994       N  
ATOM    496  CA  LEU A  74     -31.707  30.024 -17.792  1.00 53.92           C  
ANISOU  496  CA  LEU A  74     5232   9210   6043    344    219    988       C  
ATOM    497  C   LEU A  74     -32.375  31.321 -17.314  1.00 56.63           C  
ANISOU  497  C   LEU A  74     5544   9568   6404    405    179    918       C  
ATOM    498  O   LEU A  74     -31.715  32.366 -17.219  1.00 50.87           O  
ANISOU  498  O   LEU A  74     4817   8768   5743    442    122    905       O  
ATOM    499  CB  LEU A  74     -31.583  29.992 -19.297  1.00 51.32           C  
ANISOU  499  CB  LEU A  74     4901   8845   5751    336    225   1039       C  
ATOM    500  CG  LEU A  74     -30.567  28.929 -19.718  1.00 61.31           C  
ANISOU  500  CG  LEU A  74     6199  10083   7011    300    243   1096       C  
ATOM    501  CD1 LEU A  74     -30.325  29.032 -21.213  1.00 65.66           C  
ANISOU  501  CD1 LEU A  74     6741  10614   7592    312    245   1145       C  
ATOM    502  CD2 LEU A  74     -29.238  29.050 -18.998  1.00 61.81           C  
ANISOU  502  CD2 LEU A  74     6287  10095   7102    300    221   1110       C  
ATOM    503  N   LYS A  75     -33.679  31.249 -17.030  1.00 63.17           N  
ANISOU  503  N   LYS A  75     6339  10488   7173    417    201    876       N  
ATOM    504  CA  LYS A  75     -34.435  32.390 -16.454  1.00 67.70           C  
ANISOU  504  CA  LYS A  75     6879  11099   7745    489    162    793       C  
ATOM    505  C   LYS A  75     -34.150  32.578 -14.963  1.00 67.68           C  
ANISOU  505  C   LYS A  75     6878  11135   7702    528    140    735       C  
ATOM    506  O   LYS A  75     -34.383  33.642 -14.419  1.00 67.91           O  
ANISOU  506  O   LYS A  75     6889  11168   7744    604     83    656       O  
ATOM    507  CB  LYS A  75     -35.954  32.234 -16.688  1.00 64.42           C  
ANISOU  507  CB  LYS A  75     6419  10785   7272    495    196    769       C  
ATOM    508  CG  LYS A  75     -36.518  30.909 -16.201  1.00 62.51           C  
ANISOU  508  CG  LYS A  75     6163  10645   6940    438    257    801       C  
ATOM    509  CD  LYS A  75     -38.036  30.787 -16.468  1.00 59.53           C  
ANISOU  509  CD  LYS A  75     5733  10371   6514    440    286    787       C  
ATOM    510  CE  LYS A  75     -38.630  29.770 -15.504  1.00 55.37           C  
ANISOU  510  CE  LYS A  75     5173   9970   5893    400    330    812       C  
ATOM    511  NZ  LYS A  75     -38.422  28.393 -16.046  1.00 52.64           N1+
ANISOU  511  NZ  LYS A  75     4853   9594   5552    306    357    899       N1+
ATOM    512  N   TRP A  76     -33.633  31.543 -14.308  1.00 68.24           N  
ANISOU  512  N   TRP A  76     6970  11234   7724    481    175    770       N  
ATOM    513  CA  TRP A  76     -33.301  31.640 -12.887  1.00 65.60           C  
ANISOU  513  CA  TRP A  76     6637  10944   7343    517    157    721       C  
ATOM    514  C   TRP A  76     -32.440  32.861 -12.615  1.00 69.63           C  
ANISOU  514  C   TRP A  76     7166  11355   7933    582     73    669       C  
ATOM    515  O   TRP A  76     -31.571  33.238 -13.396  1.00 68.21           O  
ANISOU  515  O   TRP A  76     7012  11055   7849    565     40    710       O  
ATOM    516  CB  TRP A  76     -32.530  30.417 -12.361  1.00 60.54           C  
ANISOU  516  CB  TRP A  76     6028  10308   6665    451    194    781       C  
ATOM    517  CG  TRP A  76     -33.299  29.168 -12.368  1.00 55.30           C  
ANISOU  517  CG  TRP A  76     5345   9737   5928    385    256    835       C  
ATOM    518  CD1 TRP A  76     -34.504  28.979 -12.914  1.00 52.05           C  
ANISOU  518  CD1 TRP A  76     4893   9393   5488    371    285    845       C  
ATOM    519  CD2 TRP A  76     -32.869  27.876 -11.894  1.00 55.99           C  
ANISOU  519  CD2 TRP A  76     5454   9843   5975    315    285    899       C  
ATOM    520  CE2 TRP A  76     -33.924  26.975 -12.131  1.00 51.80           C  
ANISOU  520  CE2 TRP A  76     4890   9396   5395    260    325    946       C  
ATOM    521  CE3 TRP A  76     -31.715  27.407 -11.263  1.00 53.00           C  
ANISOU  521  CE3 TRP A  76     5117   9418   5601    293    275    921       C  
ATOM    522  NE1 TRP A  76     -34.901  27.665 -12.770  1.00 53.59           N  
ANISOU  522  NE1 TRP A  76     5079   9652   5630    295    326    912       N  
ATOM    523  CZ2 TRP A  76     -33.861  25.656 -11.770  1.00 56.49           C  
ANISOU  523  CZ2 TRP A  76     5490  10019   5952    183    345   1018       C  
ATOM    524  CZ3 TRP A  76     -31.663  26.097 -10.888  1.00 52.53           C  
ANISOU  524  CZ3 TRP A  76     5067   9394   5497    221    301    986       C  
ATOM    525  CH2 TRP A  76     -32.694  25.227 -11.165  1.00 58.11           C  
ANISOU  525  CH2 TRP A  76     5741  10172   6164    164    331   1036       C  
ATOM    526  N   ASP A  77     -32.693  33.434 -11.454  1.00 74.58           N  
ANISOU  526  N   ASP A  77     7776  12045   8517    659     36    581       N  
ATOM    527  CA  ASP A  77     -31.969  34.547 -10.935  1.00 72.92           C  
ANISOU  527  CA  ASP A  77     7581  11751   8373    731    -59    514       C  
ATOM    528  C   ASP A  77     -32.461  34.544  -9.512  1.00 73.35           C  
ANISOU  528  C   ASP A  77     7610  11939   8319    803    -62    428       C  
ATOM    529  O   ASP A  77     -33.293  33.726  -9.188  1.00 72.24           O  
ANISOU  529  O   ASP A  77     7437  11940   8071    780     13    446       O  
ATOM    530  CB  ASP A  77     -32.275  35.832 -11.725  1.00 77.36           C  
ANISOU  530  CB  ASP A  77     8130  12230   9033    782   -137    476       C  
ATOM    531  CG  ASP A  77     -33.672  36.393 -11.479  1.00 79.09           C  
ANISOU  531  CG  ASP A  77     8301  12558   9192    863   -148    384       C  
ATOM    532  OD1 ASP A  77     -34.612  35.664 -11.112  1.00 89.58           O  
ANISOU  532  OD1 ASP A  77     9595  14036  10405    856    -72    379       O  
ATOM    533  OD2 ASP A  77     -33.824  37.610 -11.659  1.00 87.67           O1-
ANISOU  533  OD2 ASP A  77     9380  13577  10354    935   -243    318       O1-
ATOM    534  N   LEU A  78     -31.938  35.406  -8.648  1.00 82.82           N  
ANISOU  534  N   LEU A  78     8821  13103   9544    889   -150    342       N  
ATOM    535  CA  LEU A  78     -32.257  35.316  -7.213  1.00 77.42           C  
ANISOU  535  CA  LEU A  78     8112  12561   8740    966   -151    261       C  
ATOM    536  C   LEU A  78     -33.722  35.550  -6.930  1.00 75.98           C  
ANISOU  536  C   LEU A  78     7865  12547   8456   1038   -130    191       C  
ATOM    537  O   LEU A  78     -34.346  34.793  -6.199  1.00 74.11           O  
ANISOU  537  O   LEU A  78     7586  12484   8085   1036    -59    202       O  
ATOM    538  CB  LEU A  78     -31.415  36.302  -6.432  1.00 76.98           C  
ANISOU  538  CB  LEU A  78     8083  12421   8742   1058   -270    168       C  
ATOM    539  CG  LEU A  78     -29.935  35.952  -6.374  1.00 83.67           C  
ANISOU  539  CG  LEU A  78     8987  13138   9664    993   -285    234       C  
ATOM    540  CD1 LEU A  78     -29.132  37.036  -5.663  1.00 85.95           C  
ANISOU  540  CD1 LEU A  78     9300  13327  10030   1087   -421    139       C  
ATOM    541  CD2 LEU A  78     -29.731  34.618  -5.669  1.00 83.46           C  
ANISOU  541  CD2 LEU A  78     8966  13218   9526    933   -190    293       C  
ATOM    542  N   GLU A  79     -34.301  36.573  -7.531  1.00 79.35           N  
ANISOU  542  N   GLU A  79     8275  12931   8943   1099   -192    129       N  
ATOM    543  CA  GLU A  79     -35.723  36.829  -7.265  1.00 86.32           C  
ANISOU  543  CA  GLU A  79     9089  13982   9724   1178   -174     56       C  
ATOM    544  C   GLU A  79     -36.589  35.589  -7.608  1.00 80.52           C  
ANISOU  544  C   GLU A  79     8314  13382   8896   1080    -43    158       C  
ATOM    545  O   GLU A  79     -37.390  35.114  -6.772  1.00 74.63           O  
ANISOU  545  O   GLU A  79     7509  12836   8011   1110     10    145       O  
ATOM    546  CB  GLU A  79     -36.202  38.074  -8.012  1.00 95.42           C  
ANISOU  546  CB  GLU A  79    10235  15049  10971   1247   -263    -16       C  
ATOM    547  CG  GLU A  79     -37.252  38.876  -7.251  1.00108.17           C  
ANISOU  547  CG  GLU A  79    11791  16807  12499   1399   -316   -163       C  
ATOM    548  CD  GLU A  79     -37.974  39.887  -8.134  1.00111.24           C  
ANISOU  548  CD  GLU A  79    12166  17131  12969   1449   -385   -218       C  
ATOM    549  OE1 GLU A  79     -38.073  41.067  -7.727  1.00121.25           O  
ANISOU  549  OE1 GLU A  79    13429  18365  14272   1583   -513   -352       O  
ATOM    550  OE2 GLU A  79     -38.429  39.503  -9.235  1.00100.07           O1-
ANISOU  550  OE2 GLU A  79    10745  15694  11583   1359   -319   -129       O1-
ATOM    551  N   TYR A  80     -36.393  35.027  -8.807  1.00 73.17           N  
ANISOU  551  N   TYR A  80     7412  12349   8039    965      2    265       N  
ATOM    552  CA  TYR A  80     -37.138  33.836  -9.175  1.00 71.05           C  
ANISOU  552  CA  TYR A  80     7112  12181   7701    871    105    362       C  
ATOM    553  C   TYR A  80     -36.872  32.732  -8.166  1.00 71.11           C  
ANISOU  553  C   TYR A  80     7112  12295   7610    824    162    417       C  
ATOM    554  O   TYR A  80     -37.785  32.158  -7.584  1.00 70.70           O  
ANISOU  554  O   TYR A  80     6996  12423   7443    821    218    437       O  
ATOM    555  CB  TYR A  80     -36.791  33.396 -10.590  1.00 75.89           C  
ANISOU  555  CB  TYR A  80     7766  12656   8412    767    130    457       C  
ATOM    556  CG  TYR A  80     -37.535  32.158 -11.072  1.00 73.89           C  
ANISOU  556  CG  TYR A  80     7486  12482   8105    670    217    553       C  
ATOM    557  CD1 TYR A  80     -37.033  30.888 -10.820  1.00 69.31           C  
ANISOU  557  CD1 TYR A  80     6927  11910   7495    578    265    643       C  
ATOM    558  CD2 TYR A  80     -38.716  32.258 -11.817  1.00 70.48           C  
ANISOU  558  CD2 TYR A  80     7011  12103   7664    669    239    553       C  
ATOM    559  CE1 TYR A  80     -37.693  29.755 -11.251  1.00 65.86           C  
ANISOU  559  CE1 TYR A  80     6468  11530   7025    489    324    730       C  
ATOM    560  CE2 TYR A  80     -39.372  31.113 -12.267  1.00 68.15           C  
ANISOU  560  CE2 TYR A  80     6693  11868   7333    578    305    642       C  
ATOM    561  CZ  TYR A  80     -38.861  29.860 -11.957  1.00 65.03           C  
ANISOU  561  CZ  TYR A  80     6318  11477   6913    488    342    731       C  
ATOM    562  OH  TYR A  80     -39.477  28.691 -12.377  1.00 67.02           O  
ANISOU  562  OH  TYR A  80     6549  11773   7142    395    387    821       O  
ATOM    563  N   LEU A  81     -35.613  32.468  -7.865  1.00 69.72           N  
ANISOU  563  N   LEU A  81     6993  12018   7476    793    144    444       N  
ATOM    564  CA  LEU A  81     -35.368  31.345  -6.973  1.00 65.21           C  
ANISOU  564  CA  LEU A  81     6417  11542   6817    739    197    508       C  
ATOM    565  C   LEU A  81     -35.967  31.559  -5.570  1.00 67.45           C  
ANISOU  565  C   LEU A  81     6638  12026   6964    833    198    440       C  
ATOM    566  O   LEU A  81     -36.572  30.646  -5.016  1.00 65.17           O  
ANISOU  566  O   LEU A  81     6296  11897   6567    790    263    506       O  
ATOM    567  CB  LEU A  81     -33.887  30.999  -6.913  1.00 62.72           C  
ANISOU  567  CB  LEU A  81     6175  11082   6571    689    176    548       C  
ATOM    568  CG  LEU A  81     -33.313  30.504  -8.257  1.00 61.86           C  
ANISOU  568  CG  LEU A  81     6117  10818   6568    590    191    634       C  
ATOM    569  CD1 LEU A  81     -31.798  30.427  -8.151  1.00 65.12           C  
ANISOU  569  CD1 LEU A  81     6596  11095   7052    568    157    654       C  
ATOM    570  CD2 LEU A  81     -33.856  29.147  -8.651  1.00 60.25           C  
ANISOU  570  CD2 LEU A  81     5898  10673   6322    485    263    738       C  
ATOM    571  N   GLN A  82     -35.796  32.738  -5.006  1.00 70.86           N  
ANISOU  571  N   GLN A  82     7072  12450   7401    963    119    312       N  
ATOM    572  CA  GLN A  82     -36.322  33.018  -3.684  1.00 77.72           C  
ANISOU  572  CA  GLN A  82     7878  13521   8129   1080    110    226       C  
ATOM    573  C   GLN A  82     -37.807  32.742  -3.645  1.00 72.76           C  
ANISOU  573  C   GLN A  82     7153  13104   7386   1095    173    241       C  
ATOM    574  O   GLN A  82     -38.301  32.089  -2.752  1.00 70.28           O  
ANISOU  574  O   GLN A  82     6775  12991   6936   1100    226    276       O  
ATOM    575  CB  GLN A  82     -36.057  34.463  -3.328  1.00 83.38           C  
ANISOU  575  CB  GLN A  82     8612  14177   8891   1231     -5     68       C  
ATOM    576  CG  GLN A  82     -36.181  34.787  -1.862  1.00 89.23           C  
ANISOU  576  CG  GLN A  82     9308  15093   9499   1371    -39    -38       C  
ATOM    577  CD  GLN A  82     -35.942  36.247  -1.606  1.00 96.82           C  
ANISOU  577  CD  GLN A  82    10295  15961  10531   1524   -178   -204       C  
ATOM    578  NE2 GLN A  82     -35.966  37.044  -2.644  1.00 99.26           N  
ANISOU  578  NE2 GLN A  82    10588  16373  10753   1655   -235   -313       N  
ATOM    579  OE1 GLN A  82     -35.745  36.651  -0.476  1.00108.21           O  
ANISOU  579  OE1 GLN A  82    11769  17235  12108   1524   -243   -232       O  
ATOM    580  N   GLU A  83     -38.494  33.260  -4.645  1.00 70.31           N  
ANISOU  580  N   GLU A  83     6833  12741   7139   1093    166    226       N  
ATOM    581  CA  GLU A  83     -39.905  33.021  -4.909  1.00 75.53           C  
ANISOU  581  CA  GLU A  83     7409  13564   7722   1086    225    252       C  
ATOM    582  C   GLU A  83     -40.314  31.557  -4.969  1.00 76.36           C  
ANISOU  582  C   GLU A  83     7477  13765   7769    945    322    411       C  
ATOM    583  O   GLU A  83     -41.379  31.212  -4.501  1.00 73.39           O  
ANISOU  583  O   GLU A  83     7007  13602   7274    956    372    441       O  
ATOM    584  CB  GLU A  83     -40.276  33.643  -6.276  1.00 74.49           C  
ANISOU  584  CB  GLU A  83     7300  13294   7707   1075    197    232       C  
ATOM    585  CG  GLU A  83     -41.757  33.683  -6.591  1.00 83.55           C  
ANISOU  585  CG  GLU A  83     8362  14594   8788   1095    237    229       C  
ATOM    586  CD  GLU A  83     -42.536  34.530  -5.589  1.00 90.34           C  
ANISOU  586  CD  GLU A  83     9144  15651   9528   1260    204     97       C  
ATOM    587  OE1 GLU A  83     -43.685  34.176  -5.257  1.00 85.96           O  
ANISOU  587  OE1 GLU A  83     8492  15315   8852   1274    263    122       O  
ATOM    588  OE2 GLU A  83     -41.982  35.545  -5.116  1.00 91.90           O1-
ANISOU  588  OE2 GLU A  83     9375  15789   9753   1382    112    -30       O1-
ATOM    589  N   ASN A  84     -39.491  30.702  -5.581  1.00 73.78           N  
ANISOU  589  N   ASN A  84     7220  13282   7530    815    341    515       N  
ATOM    590  CA  ASN A  84     -39.944  29.379  -6.002  1.00 66.03           C  
ANISOU  590  CA  ASN A  84     6214  12337   6535    675    409    661       C  
ATOM    591  C   ASN A  84     -39.241  28.152  -5.371  1.00 65.61           C  
ANISOU  591  C   ASN A  84     6181  12294   6453    577    438    772       C  
ATOM    592  O   ASN A  84     -39.757  27.028  -5.451  1.00 59.19           O  
ANISOU  592  O   ASN A  84     5329  11550   5611    470    482    895       O  
ATOM    593  CB  ASN A  84     -39.851  29.309  -7.519  1.00 69.54           C  
ANISOU  593  CB  ASN A  84     6713  12597   7109    604    401    693       C  
ATOM    594  CG  ASN A  84     -40.995  30.011  -8.218  1.00 80.78           C  
ANISOU  594  CG  ASN A  84     8089  14065   8539    653    399    642       C  
ATOM    595  ND2 ASN A  84     -40.678  30.994  -9.090  1.00 83.70           N  
ANISOU  595  ND2 ASN A  84     8509  14280   9011    701    347    567       N  
ATOM    596  OD1 ASN A  84     -42.154  29.635  -8.023  1.00 80.24           O  
ANISOU  596  OD1 ASN A  84     7935  14164   8386    640    443    680       O  
ATOM    597  N   ILE A  85     -38.084  28.342  -4.743  1.00 69.52           N  
ANISOU  597  N   ILE A  85     6733  12717   6962    610    404    734       N  
ATOM    598  CA  ILE A  85     -37.235  27.209  -4.328  1.00 74.30           C  
ANISOU  598  CA  ILE A  85     7377  13284   7567    512    420    835       C  
ATOM    599  C   ILE A  85     -37.674  26.505  -3.003  1.00 77.24           C  
ANISOU  599  C   ILE A  85     7671  13882   7794    502    460    902       C  
ATOM    600  O   ILE A  85     -37.168  25.421  -2.650  1.00 74.61           O  
ANISOU  600  O   ILE A  85     7356  13538   7454    405    474   1009       O  
ATOM    601  CB  ILE A  85     -35.706  27.614  -4.374  1.00 71.09           C  
ANISOU  601  CB  ILE A  85     7072  12684   7255    533    367    782       C  
ATOM    602  CG1 ILE A  85     -34.805  26.401  -4.670  1.00 76.63           C  
ANISOU  602  CG1 ILE A  85     7834  13265   8014    407    378    892       C  
ATOM    603  CG2 ILE A  85     -35.240  28.337  -3.144  1.00 66.20           C  
ANISOU  603  CG2 ILE A  85     6448  12132   6571    648    331    686       C  
ATOM    604  CD1 ILE A  85     -33.328  26.719  -4.956  1.00 78.35           C  
ANISOU  604  CD1 ILE A  85     8147  13285   8336    414    332    856       C  
ATOM    605  N   GLY A  86     -38.646  27.070  -2.284  1.00 85.80           N  
ANISOU  605  N   GLY A  86     8661  15181   8757    600    475    849       N  
ATOM    606  CA  GLY A  86     -39.177  26.408  -1.055  1.00 73.03           C  
ANISOU  606  CA  GLY A  86     6949  13814   6985    593    519    929       C  
ATOM    607  C   GLY A  86     -38.519  26.905   0.211  1.00 75.39           C  
ANISOU  607  C   GLY A  86     7250  14196   7197    707    494    845       C  
ATOM    608  O   GLY A  86     -37.752  27.885   0.186  1.00 68.48           O  
ANISOU  608  O   GLY A  86     6445  13192   6382    804    435    710       O  
ATOM    609  N   ASN A  87     -38.774  26.225   1.313  1.00 82.93           N  
ANISOU  609  N   ASN A  87     8125  15371   8013    696    534    929       N  
ATOM    610  CA  ASN A  87     -38.219  26.666   2.570  1.00 91.77           C  
ANISOU  610  CA  ASN A  87     9236  16602   9029    811    512    853       C  
ATOM    611  C   ASN A  87     -37.174  25.724   3.130  1.00 88.84           C  
ANISOU  611  C   ASN A  87     8910  16181   8661    713    517    961       C  
ATOM    612  O   ASN A  87     -36.767  25.872   4.263  1.00 92.38           O  
ANISOU  612  O   ASN A  87     9330  16775   8995    786    515    941       O  
ATOM    613  CB  ASN A  87     -39.319  26.921   3.590  1.00100.57           C  
ANISOU  613  CB  ASN A  87    10212  18050   9949    929    545    828       C  
ATOM    614  CG  ASN A  87     -39.792  25.650   4.256  1.00111.87           C  
ANISOU  614  CG  ASN A  87    11543  19706  11254    832    610   1014       C  
ATOM    615  ND2 ASN A  87     -40.278  25.762   5.478  1.00113.73           N  
ANISOU  615  ND2 ASN A  87    11732  20135  11346    918    615   1000       N  
ATOM    616  OD1 ASN A  87     -39.693  24.574   3.678  1.00125.29           O  
ANISOU  616  OD1 ASN A  87    13208  21406  12990    683    649   1171       O  
ATOM    617  N   GLY A  88     -36.708  24.768   2.345  1.00 85.65           N  
ANISOU  617  N   GLY A  88     8581  15573   8388    560    517   1064       N  
ATOM    618  CA  GLY A  88     -35.657  23.883   2.812  1.00 76.08           C  
ANISOU  618  CA  GLY A  88     7436  14257   7213    469    505   1147       C  
ATOM    619  C   GLY A  88     -34.446  24.628   3.313  1.00 68.59           C  
ANISOU  619  C   GLY A  88     6569  13203   6288    569    453   1019       C  
ATOM    620  O   GLY A  88     -34.337  25.814   3.133  1.00 67.39           O  
ANISOU  620  O   GLY A  88     6448  12980   6176    685    411    870       O  
ATOM    621  N   ASP A  89     -33.502  23.912   3.900  1.00 67.98           N  
ANISOU  621  N   ASP A  89     6524  13115   6190    526    446   1078       N  
ATOM    622  CA  ASP A  89     -32.244  24.496   4.360  1.00 71.51           C  
ANISOU  622  CA  ASP A  89     7057  13433   6679    606    390    967       C  
ATOM    623  C   ASP A  89     -31.201  24.510   3.240  1.00 75.60           C  
ANISOU  623  C   ASP A  89     7691  13650   7383    539    353    951       C  
ATOM    624  O   ASP A  89     -31.122  23.568   2.483  1.00 72.83           O  
ANISOU  624  O   ASP A  89     7362  13201   7109    408    373   1058       O  
ATOM    625  CB  ASP A  89     -31.691  23.659   5.511  1.00 71.71           C  
ANISOU  625  CB  ASP A  89     7080  13548   6619    582    395   1038       C  
ATOM    626  CG  ASP A  89     -32.214  24.075   6.863  1.00 72.72           C  
ANISOU  626  CG  ASP A  89     7102  13976   6551    704    414   1005       C  
ATOM    627  OD1 ASP A  89     -32.775  25.166   6.996  1.00 76.15           O  
ANISOU  627  OD1 ASP A  89     7458  14564   6909    800    429    939       O  
ATOM    628  OD2 ASP A  89     -32.039  23.297   7.807  1.00 72.57           O1-
ANISOU  628  OD2 ASP A  89     7077  14048   6449    711    413   1044       O1-
ATOM    629  N   PHE A  90     -30.393  25.559   3.155  1.00 72.66           N  
ANISOU  629  N   PHE A  90     7384  13141   7082    632    292    820       N  
ATOM    630  CA  PHE A  90     -29.346  25.653   2.120  1.00 70.43           C  
ANISOU  630  CA  PHE A  90     7200  12593   6966    579    255    810       C  
ATOM    631  C   PHE A  90     -27.976  25.805   2.727  1.00 68.23           C  
ANISOU  631  C   PHE A  90     6990  12208   6724    609    205    766       C  
ATOM    632  O   PHE A  90     -27.764  26.710   3.539  1.00 73.53           O  
ANISOU  632  O   PHE A  90     7656  12927   7354    735    157    652       O  
ATOM    633  CB  PHE A  90     -29.618  26.830   1.155  1.00 69.20           C  
ANISOU  633  CB  PHE A  90     7055  12337   6900    645    221    709       C  
ATOM    634  CG  PHE A  90     -30.777  26.581   0.225  1.00 67.72           C  
ANISOU  634  CG  PHE A  90     6821  12194   6716    590    268    763       C  
ATOM    635  CD1 PHE A  90     -32.096  26.659   0.688  1.00 66.50           C  
ANISOU  635  CD1 PHE A  90     6569  12258   6437    634    306    762       C  
ATOM    636  CD2 PHE A  90     -30.558  26.216  -1.096  1.00 65.79           C  
ANISOU  636  CD2 PHE A  90     6622  11783   6591    497    275    820       C  
ATOM    637  CE1 PHE A  90     -33.166  26.421  -0.157  1.00 62.73           C  
ANISOU  637  CE1 PHE A  90     6047  11820   5967    581    346    814       C  
ATOM    638  CE2 PHE A  90     -31.619  25.971  -1.936  1.00 66.35           C  
ANISOU  638  CE2 PHE A  90     6652  11893   6665    449    313    866       C  
ATOM    639  CZ  PHE A  90     -32.925  26.072  -1.465  1.00 68.27           C  
ANISOU  639  CZ  PHE A  90     6801  12342   6794    488    347    864       C  
ATOM    640  N   SER A  91     -27.048  24.933   2.334  1.00 64.48           N  
ANISOU  640  N   SER A  91     6579  11589   6329    502    206    849       N  
ATOM    641  CA  SER A  91     -25.660  25.084   2.767  1.00 68.20           C  
ANISOU  641  CA  SER A  91     7120  11936   6853    524    156    811       C  
ATOM    642  C   SER A  91     -25.032  26.300   2.107  1.00 67.10           C  
ANISOU  642  C   SER A  91     7027  11630   6838    592     92    707       C  
ATOM    643  O   SER A  91     -25.048  26.411   0.884  1.00 77.21           O  
ANISOU  643  O   SER A  91     8325  12791   8218    545     96    728       O  
ATOM    644  CB  SER A  91     -24.866  23.804   2.528  1.00 65.78           C  
ANISOU  644  CB  SER A  91     6865  11532   6594    397    171    926       C  
ATOM    645  OG  SER A  91     -25.504  22.715   3.194  1.00 60.90           O  
ANISOU  645  OG  SER A  91     6198  11070   5867    331    216   1031       O  
ATOM    646  N   VAL A  92     -24.543  27.233   2.930  1.00 68.28           N  
ANISOU  646  N   VAL A  92     7186  11779   6978    706     27    597       N  
ATOM    647  CA  VAL A  92     -23.848  28.430   2.460  1.00 67.59           C  
ANISOU  647  CA  VAL A  92     7138  11523   7017    771    -55    504       C  
ATOM    648  C   VAL A  92     -22.467  28.540   3.117  1.00 75.94           C  
ANISOU  648  C   VAL A  92     8253  12478   8122    792   -117    475       C  
ATOM    649  O   VAL A  92     -22.330  28.590   4.357  1.00 78.11           O  
ANISOU  649  O   VAL A  92     8518  12853   8305    864   -141    423       O  
ATOM    650  CB  VAL A  92     -24.604  29.702   2.822  1.00 72.26           C  
ANISOU  650  CB  VAL A  92     7687  12193   7574    912   -111    372       C  
ATOM    651  CG1 VAL A  92     -23.860  30.914   2.311  1.00 73.01           C  
ANISOU  651  CG1 VAL A  92     7822  12096   7820    967   -214    291       C  
ATOM    652  CG2 VAL A  92     -26.019  29.683   2.264  1.00 70.63           C  
ANISOU  652  CG2 VAL A  92     7418  12105   7313    906    -53    389       C  
ATOM    653  N   TYR A  93     -21.445  28.617   2.276  1.00 74.24           N  
ANISOU  653  N   TYR A  93     8089  12069   8047    735   -147    508       N  
ATOM    654  CA  TYR A  93     -20.074  28.674   2.737  1.00 71.66           C  
ANISOU  654  CA  TYR A  93     7815  11629   7783    740   -204    496       C  
ATOM    655  C   TYR A  93     -19.673  30.156   2.792  1.00 76.71           C  
ANISOU  655  C   TYR A  93     8462  12163   8519    845   -318    383       C  
ATOM    656  O   TYR A  93     -20.092  30.968   1.948  1.00 78.95           O  
ANISOU  656  O   TYR A  93     8730  12389   8879    864   -347    358       O  
ATOM    657  CB  TYR A  93     -19.161  27.765   1.853  1.00 68.05           C  
ANISOU  657  CB  TYR A  93     7402  11042   7411    616   -169    609       C  
ATOM    658  CG  TYR A  93     -19.565  26.296   1.960  1.00 61.55           C  
ANISOU  658  CG  TYR A  93     6574  10316   6496    524    -82    708       C  
ATOM    659  CD1 TYR A  93     -20.595  25.818   1.203  1.00 61.70           C  
ANISOU  659  CD1 TYR A  93     6560  10395   6487    470    -20    764       C  
ATOM    660  CD2 TYR A  93     -18.994  25.430   2.920  1.00 61.49           C  
ANISOU  660  CD2 TYR A  93     6589  10348   6426    497    -74    743       C  
ATOM    661  CE1 TYR A  93     -21.053  24.511   1.332  1.00 63.06           C  
ANISOU  661  CE1 TYR A  93     6721  10653   6583    385     40    857       C  
ATOM    662  CE2 TYR A  93     -19.439  24.107   3.063  1.00 60.45           C  
ANISOU  662  CE2 TYR A  93     6446  10304   6215    410    -10    841       C  
ATOM    663  CZ  TYR A  93     -20.478  23.660   2.247  1.00 62.10           C  
ANISOU  663  CZ  TYR A  93     6621  10562   6409    353     42    899       C  
ATOM    664  OH  TYR A  93     -20.985  22.390   2.281  1.00 57.64           O  
ANISOU  664  OH  TYR A  93     6043  10070   5787    261     89   1002       O  
ATOM    665  N   SER A  94     -18.868  30.470   3.791  1.00 83.47           N  
ANISOU  665  N   SER A  94     9342  13002   9370    913   -389    316       N  
ATOM    666  CA  SER A  94     -18.438  31.815   4.067  1.00 93.91           C  
ANISOU  666  CA  SER A  94    10673  14230  10776   1025   -521    198       C  
ATOM    667  C   SER A  94     -16.953  31.955   3.876  1.00 89.11           C  
ANISOU  667  C   SER A  94    10115  13430  10311    978   -584    234       C  
ATOM    668  O   SER A  94     -16.236  30.984   3.928  1.00 90.83           O  
ANISOU  668  O   SER A  94    10360  13634  10516    894   -527    319       O  
ATOM    669  CB  SER A  94     -18.749  32.129   5.511  1.00100.92           C  
ANISOU  669  CB  SER A  94    11546  15260  11536   1154   -564     83       C  
ATOM    670  OG  SER A  94     -18.116  33.326   5.895  1.00111.05           O  
ANISOU  670  OG  SER A  94    12862  16420  12911   1239   -700    -11       O  
ATOM    671  N   ALA A  95     -16.486  33.172   3.673  1.00 88.69           N  
ANISOU  671  N   ALA A  95    10069  13230  10396   1032   -707    176       N  
ATOM    672  CA  ALA A  95     -15.024  33.405   3.601  1.00 86.34           C  
ANISOU  672  CA  ALA A  95     9809  12758  10238    999   -784    207       C  
ATOM    673  C   ALA A  95     -14.612  34.880   3.564  1.00 86.36           C  
ANISOU  673  C   ALA A  95     9810  12612  10390   1078   -949    127       C  
ATOM    674  O   ALA A  95     -15.332  35.744   3.078  1.00 88.58           O  
ANISOU  674  O   ALA A  95    10064  12874  10717   1123   -999     83       O  
ATOM    675  CB  ALA A  95     -14.405  32.688   2.407  1.00 83.95           C  
ANISOU  675  CB  ALA A  95     9514  12372  10010    862   -709    353       C  
ATOM    676  N   SER A  96     -13.413  35.132   4.063  1.00 88.18           N  
ANISOU  676  N   SER A  96    10069  12727  10705   1088  -1041    116       N  
ATOM    677  CA  SER A  96     -12.825  36.454   4.086  1.00 90.87           C  
ANISOU  677  CA  SER A  96    10412  12903  11211   1150  -1216     55       C  
ATOM    678  C   SER A  96     -11.934  36.700   2.868  1.00 87.21           C  
ANISOU  678  C   SER A  96     9938  12271  10925   1040  -1240    189       C  
ATOM    679  O   SER A  96     -11.691  37.842   2.503  1.00 94.49           O  
ANISOU  679  O   SER A  96    10845  13056  12001   1065  -1376    175       O  
ATOM    680  CB  SER A  96     -11.987  36.584   5.344  1.00 91.77           C  
ANISOU  680  CB  SER A  96    10559  12987  11321   1223  -1311    -27       C  
ATOM    681  OG  SER A  96     -11.173  35.434   5.463  1.00 94.48           O  
ANISOU  681  OG  SER A  96    10928  13347  11623   1130  -1215     68       O  
ATOM    682  N   THR A  97     -11.436  35.636   2.252  1.00 81.02           N  
ANISOU  682  N   THR A  97     9160  11503  10121    923  -1116    319       N  
ATOM    683  CA  THR A  97     -10.645  35.757   1.025  1.00 78.72           C  
ANISOU  683  CA  THR A  97     8846  11091   9970    823  -1118    456       C  
ATOM    684  C   THR A  97     -11.478  35.241  -0.153  1.00 74.45           C  
ANISOU  684  C   THR A  97     8280  10628   9380    755   -990    538       C  
ATOM    685  O   THR A  97     -12.572  34.714   0.025  1.00 75.74           O  
ANISOU  685  O   THR A  97     8444  10926   9407    776   -901    495       O  
ATOM    686  CB  THR A  97      -9.279  35.026   1.139  1.00 78.61           C  
ANISOU  686  CB  THR A  97     8853  11026   9988    753  -1094    540       C  
ATOM    687  CG2 THR A  97      -9.467  33.535   1.452  1.00 74.20           C  
ANISOU  687  CG2 THR A  97     8323  10603   9265    712   -944    563       C  
ATOM    688  OG1 THR A  97      -8.535  35.169  -0.083  1.00 85.95           O  
ANISOU  688  OG1 THR A  97     9748  11864  11043    664  -1093    678       O  
ATOM    689  N   HIS A  98     -10.970  35.416  -1.357  1.00 71.25           N  
ANISOU  689  N   HIS A  98     7843  10141   9084    678   -986    658       N  
ATOM    690  CA  HIS A  98     -11.674  34.941  -2.531  1.00 71.07           C  
ANISOU  690  CA  HIS A  98     7795  10187   9020    619   -873    736       C  
ATOM    691  C   HIS A  98     -11.604  33.413  -2.642  1.00 68.21           C  
ANISOU  691  C   HIS A  98     7456   9926   8534    556   -727    791       C  
ATOM    692  O   HIS A  98     -12.430  32.799  -3.330  1.00 65.55           O  
ANISOU  692  O   HIS A  98     7109   9675   8121    523   -626    822       O  
ATOM    693  CB  HIS A  98     -11.135  35.603  -3.804  1.00 71.37           C  
ANISOU  693  CB  HIS A  98     7787  10124   9205    562   -915    854       C  
ATOM    694  CG  HIS A  98      -9.670  35.434  -3.987  1.00 74.44           C  
ANISOU  694  CG  HIS A  98     8167  10434   9682    505   -940    953       C  
ATOM    695  CD2 HIS A  98      -8.949  34.415  -4.502  1.00 80.29           C  
ANISOU  695  CD2 HIS A  98     8906  11212  10387    437   -843   1050       C  
ATOM    696  ND1 HIS A  98      -8.755  36.367  -3.552  1.00 77.53           N  
ANISOU  696  ND1 HIS A  98     8549  10694  10213    524  -1085    952       N  
ATOM    697  CE1 HIS A  98      -7.535  35.946  -3.828  1.00 75.00           C  
ANISOU  697  CE1 HIS A  98     8216  10339   9940    462  -1070   1056       C  
ATOM    698  NE2 HIS A  98      -7.622  34.757  -4.394  1.00 74.05           N  
ANISOU  698  NE2 HIS A  98     8100  10323   9710    413   -923   1112       N  
ATOM    699  N   LYS A  99     -10.638  32.801  -1.969  1.00 72.34           N  
ANISOU  699  N   LYS A  99     8010  10434   9042    540   -725    800       N  
ATOM    700  CA  LYS A  99     -10.448  31.346  -2.078  1.00 74.25           C  
ANISOU  700  CA  LYS A  99     8275  10751   9183    480   -606    855       C  
ATOM    701  C   LYS A  99     -11.203  30.647  -1.010  1.00 70.56           C  
ANISOU  701  C   LYS A  99     7839  10396   8572    512   -558    777       C  
ATOM    702  O   LYS A  99     -10.871  30.772   0.136  1.00 69.31           O  
ANISOU  702  O   LYS A  99     7705  10236   8392    560   -610    710       O  
ATOM    703  CB  LYS A  99      -8.985  30.925  -1.991  1.00 69.87           C  
ANISOU  703  CB  LYS A  99     7734  10128   8683    440   -622    917       C  
ATOM    704  CG  LYS A  99      -8.140  31.531  -3.101  1.00 80.38           C  
ANISOU  704  CG  LYS A  99     9019  11368  10151    400   -662   1019       C  
ATOM    705  CD  LYS A  99      -6.754  30.901  -3.245  1.00 81.65           C  
ANISOU  705  CD  LYS A  99     9183  11493  10346    353   -650   1099       C  
ATOM    706  CE  LYS A  99      -5.825  31.286  -2.091  1.00 86.85           C  
ANISOU  706  CE  LYS A  99     9865  12072  11060    383   -747   1053       C  
ATOM    707  NZ  LYS A  99      -5.358  32.704  -2.190  1.00 85.99           N1+
ANISOU  707  NZ  LYS A  99     9717  11844  11110    402   -882   1067       N1+
ATOM    708  N   PHE A 100     -12.207  29.894  -1.439  1.00 70.73           N  
ANISOU  708  N   PHE A 100     7855  10521   8498    483   -460    797       N  
ATOM    709  CA  PHE A 100     -12.990  28.985  -0.634  1.00 72.59           C  
ANISOU  709  CA  PHE A 100     8108  10883   8590    487   -394    764       C  
ATOM    710  C   PHE A 100     -12.422  27.571  -0.634  1.00 84.29           C  
ANISOU  710  C   PHE A 100     9620  12383  10021    415   -327    834       C  
ATOM    711  O   PHE A 100     -12.852  26.707  -1.433  1.00 98.92           O  
ANISOU  711  O   PHE A 100    11470  14276  11838    357   -253    895       O  
ATOM    712  CB  PHE A 100     -14.379  28.863  -1.251  1.00 67.75           C  
ANISOU  712  CB  PHE A 100     7465  10360   7914    479   -330    767       C  
ATOM    713  CG  PHE A 100     -15.224  30.065  -1.073  1.00 70.29           C  
ANISOU  713  CG  PHE A 100     7758  10700   8248    559   -385    683       C  
ATOM    714  CD1 PHE A 100     -15.030  31.186  -1.863  1.00 64.98           C  
ANISOU  714  CD1 PHE A 100     7063   9924   7700    576   -454    685       C  
ATOM    715  CD2 PHE A 100     -16.245  30.073  -0.108  1.00 69.47           C  
ANISOU  715  CD2 PHE A 100     7642  10726   8026    621   -374    604       C  
ATOM    716  CE1 PHE A 100     -15.817  32.300  -1.695  1.00 66.16           C  
ANISOU  716  CE1 PHE A 100     7187  10080   7867    654   -519    601       C  
ATOM    717  CE2 PHE A 100     -17.033  31.180   0.059  1.00 68.21           C  
ANISOU  717  CE2 PHE A 100     7454  10590   7872    708   -432    515       C  
ATOM    718  CZ  PHE A 100     -16.819  32.294  -0.741  1.00 71.35           C  
ANISOU  718  CZ  PHE A 100     7839  10866   8405    725   -509    508       C  
ATOM    719  N   LEU A 101     -11.535  27.299   0.302  1.00 91.83           N  
ANISOU  719  N   LEU A 101    10608  13314  10969    424   -360    818       N  
ATOM    720  CA  LEU A 101     -11.115  25.924   0.571  1.00 90.98           C  
ANISOU  720  CA  LEU A 101    10532  13236  10797    366   -307    869       C  
ATOM    721  C   LEU A 101     -12.237  25.161   1.325  1.00 87.49           C  
ANISOU  721  C   LEU A 101    10091  12934  10216    363   -252    855       C  
ATOM    722  O   LEU A 101     -12.740  25.608   2.360  1.00 86.12           O  
ANISOU  722  O   LEU A 101     9908  12835   9977    426   -276    787       O  
ATOM    723  CB  LEU A 101      -9.838  25.932   1.417  1.00103.31           C  
ANISOU  723  CB  LEU A 101    12126  14730  12394    381   -365    854       C  
ATOM    724  CG  LEU A 101      -8.912  24.716   1.312  1.00101.79           C  
ANISOU  724  CG  LEU A 101    11968  14510  12196    318   -334    920       C  
ATOM    725  CD1 LEU A 101      -8.060  24.804   0.040  1.00102.66           C  
ANISOU  725  CD1 LEU A 101    12063  14531  12410    283   -336    986       C  
ATOM    726  CD2 LEU A 101      -8.046  24.580   2.561  1.00 94.88           C  
ANISOU  726  CD2 LEU A 101    11127  13614  11306    342   -382    886       C  
ATOM    727  N   TYR A 102     -12.603  24.015   0.767  1.00 85.15           N  
ANISOU  727  N   TYR A 102     9799  12675   9878    292   -186    925       N  
ATOM    728  CA  TYR A 102     -13.585  23.081   1.305  1.00 82.64           C  
ANISOU  728  CA  TYR A 102     9476  12479   9443    261   -136    948       C  
ATOM    729  C   TYR A 102     -12.963  22.214   2.403  1.00 71.65           C  
ANISOU  729  C   TYR A 102     8118  11108   7995    241   -145    966       C  
ATOM    730  O   TYR A 102     -11.842  21.765   2.273  1.00 83.10           O  
ANISOU  730  O   TYR A 102     9604  12469   9498    213   -165    993       O  
ATOM    731  CB  TYR A 102     -14.085  22.211   0.117  1.00 86.40           C  
ANISOU  731  CB  TYR A 102     9947  12955   9926    189    -84   1020       C  
ATOM    732  CG  TYR A 102     -14.732  20.855   0.440  1.00 98.97           C  
ANISOU  732  CG  TYR A 102    11544  14628  11432    122    -46   1081       C  
ATOM    733  CD1 TYR A 102     -16.041  20.774   0.959  1.00100.19           C  
ANISOU  733  CD1 TYR A 102    11658  14917  11493    123    -15   1085       C  
ATOM    734  CD2 TYR A 102     -14.052  19.642   0.161  1.00 95.11           C  
ANISOU  734  CD2 TYR A 102    11094  14082  10962     58    -50   1142       C  
ATOM    735  CE1 TYR A 102     -16.622  19.540   1.235  1.00 98.99           C  
ANISOU  735  CE1 TYR A 102    11500  14835  11274     52      9   1161       C  
ATOM    736  CE2 TYR A 102     -14.628  18.411   0.449  1.00 92.43           C  
ANISOU  736  CE2 TYR A 102    10757  13799  10561     -7    -35   1205       C  
ATOM    737  CZ  TYR A 102     -15.904  18.366   0.983  1.00 96.84           C  
ANISOU  737  CZ  TYR A 102    11272  14487  11035    -15     -6   1222       C  
ATOM    738  OH  TYR A 102     -16.457  17.140   1.251  1.00100.78           O  
ANISOU  738  OH  TYR A 102    11768  15040  11485    -91     -1   1303       O  
ATOM    739  N   TYR A 103     -13.679  21.952   3.479  1.00 73.40           N  
ANISOU  739  N   TYR A 103     8324  11458   8107    257   -130    957       N  
ATOM    740  CA  TYR A 103     -13.226  20.973   4.489  1.00 72.74           C  
ANISOU  740  CA  TYR A 103     8268  11411   7959    225   -133    995       C  
ATOM    741  C   TYR A 103     -14.202  19.819   4.589  1.00 69.40           C  
ANISOU  741  C   TYR A 103     7823  11095   7450    152    -85   1079       C  
ATOM    742  O   TYR A 103     -15.386  20.060   4.682  1.00 77.17           O  
ANISOU  742  O   TYR A 103     8758  12197   8366    168    -53   1076       O  
ATOM    743  CB  TYR A 103     -13.172  21.619   5.856  1.00 74.05           C  
ANISOU  743  CB  TYR A 103     8424  11655   8055    309   -166    923       C  
ATOM    744  CG  TYR A 103     -12.346  22.838   5.887  1.00 86.33           C  
ANISOU  744  CG  TYR A 103     9994  13108   9697    388   -232    835       C  
ATOM    745  CD1 TYR A 103     -10.966  22.769   5.710  1.00 94.73           C  
ANISOU  745  CD1 TYR A 103    11102  14032  10856    369   -274    843       C  
ATOM    746  CD2 TYR A 103     -12.925  24.085   6.082  1.00102.22           C  
ANISOU  746  CD2 TYR A 103    11974  15160  11704    482   -265    744       C  
ATOM    747  CE1 TYR A 103     -10.174  23.923   5.731  1.00 98.14           C  
ANISOU  747  CE1 TYR A 103    11542  14363  11383    434   -347    774       C  
ATOM    748  CE2 TYR A 103     -12.147  25.235   6.107  1.00110.96           C  
ANISOU  748  CE2 TYR A 103    13094  16155  12909    551   -347    666       C  
ATOM    749  CZ  TYR A 103     -10.770  25.146   5.924  1.00107.55           C  
ANISOU  749  CZ  TYR A 103    12703  15582  12579    521   -388    688       C  
ATOM    750  OH  TYR A 103      -9.990  26.275   5.945  1.00112.07           O  
ANISOU  750  OH  TYR A 103    13281  16039  13258    581   -478    625       O  
ATOM    751  N   ASP A 104     -13.723  18.581   4.610  1.00 62.39           N  
ANISOU  751  N   ASP A 104     6969  10169   6565     74    -87   1154       N  
ATOM    752  CA  ASP A 104     -14.592  17.446   4.842  1.00 62.25           C  
ANISOU  752  CA  ASP A 104     6930  10246   6475     -1    -61   1246       C  
ATOM    753  C   ASP A 104     -14.678  17.306   6.364  1.00 69.60           C  
ANISOU  753  C   ASP A 104     7844  11303   7297     20    -66   1256       C  
ATOM    754  O   ASP A 104     -13.673  17.080   7.063  1.00 58.98           O  
ANISOU  754  O   ASP A 104     6539   9914   5954     28   -100   1249       O  
ATOM    755  CB  ASP A 104     -14.058  16.177   4.157  1.00 62.22           C  
ANISOU  755  CB  ASP A 104     6971  10136   6534    -89    -81   1320       C  
ATOM    756  CG  ASP A 104     -14.806  14.895   4.548  1.00 66.39           C  
ANISOU  756  CG  ASP A 104     7482  10741   7002   -179    -80   1428       C  
ATOM    757  OD1 ASP A 104     -15.410  14.844   5.653  1.00 70.91           O  
ANISOU  757  OD1 ASP A 104     8013  11455   7472   -177    -65   1461       O  
ATOM    758  OD2 ASP A 104     -14.731  13.898   3.785  1.00 61.02           O1-
ANISOU  758  OD2 ASP A 104     6828   9980   6377   -249   -104   1484       O1-
ATOM    759  N   GLU A 105     -15.907  17.415   6.858  1.00 70.98           N  
ANISOU  759  N   GLU A 105     7954  11647   7369     31    -30   1278       N  
ATOM    760  CA  GLU A 105     -16.169  17.498   8.300  1.00 71.31           C  
ANISOU  760  CA  GLU A 105     7959  11852   7282     77    -26   1279       C  
ATOM    761  C   GLU A 105     -15.965  16.182   9.005  1.00 68.73           C  
ANISOU  761  C   GLU A 105     7640  11563   6908     -9    -36   1395       C  
ATOM    762  O   GLU A 105     -15.407  16.143  10.117  1.00 68.60           O  
ANISOU  762  O   GLU A 105     7634  11598   6830     25    -56   1386       O  
ATOM    763  CB  GLU A 105     -17.567  18.105   8.553  1.00 75.44           C  
ANISOU  763  CB  GLU A 105     8398  12563   7703    129     15   1262       C  
ATOM    764  CG  GLU A 105     -17.779  19.364   7.701  1.00 82.43           C  
ANISOU  764  CG  GLU A 105     9280  13385   8654    206     14   1152       C  
ATOM    765  CD  GLU A 105     -18.904  20.262   8.144  1.00 86.36           C  
ANISOU  765  CD  GLU A 105     9704  14058   9051    300     36   1091       C  
ATOM    766  OE1 GLU A 105     -19.739  19.779   8.946  1.00 88.64           O  
ANISOU  766  OE1 GLU A 105     9927  14539   9209    290     70   1156       O  
ATOM    767  OE2 GLU A 105     -18.955  21.439   7.655  1.00 82.60           O1-
ANISOU  767  OE2 GLU A 105     9228  13525   8628    382     16    983       O1-
ATOM    768  N   LYS A 106     -16.357  15.098   8.342  1.00 66.43           N  
ANISOU  768  N   LYS A 106     7350  11236   6655   -120    -33   1502       N  
ATOM    769  CA  LYS A 106     -16.069  13.734   8.830  1.00 66.03           C  
ANISOU  769  CA  LYS A 106     7316  11178   6592   -219    -64   1622       C  
ATOM    770  C   LYS A 106     -14.578  13.565   9.094  1.00 68.79           C  
ANISOU  770  C   LYS A 106     7745  11389   7001   -205   -111   1582       C  
ATOM    771  O   LYS A 106     -14.210  13.001  10.102  1.00 74.90           O  
ANISOU  771  O   LYS A 106     8526  12212   7720   -225   -133   1634       O  
ATOM    772  CB  LYS A 106     -16.576  12.673   7.835  1.00 74.36           C  
ANISOU  772  CB  LYS A 106     8373  12162   7717   -332    -78   1720       C  
ATOM    773  CG  LYS A 106     -18.101  12.775   7.512  1.00 81.14           C  
ANISOU  773  CG  LYS A 106     9150  13154   8526   -356    -34   1771       C  
ATOM    774  CD  LYS A 106     -18.621  11.994   6.281  1.00 86.48           C  
ANISOU  774  CD  LYS A 106     9831  13735   9291   -446    -54   1833       C  
ATOM    775  CE  LYS A 106     -18.269  12.579   4.880  1.00 85.99           C  
ANISOU  775  CE  LYS A 106     9816  13521   9335   -404    -52   1731       C  
ATOM    776  NZ  LYS A 106     -18.377  14.066   4.673  1.00 83.74           N1+
ANISOU  776  NZ  LYS A 106     9512  13267   9035   -294     -5   1610       N1+
ATOM    777  N   LYS A 107     -13.715  14.130   8.240  1.00 64.04           N  
ANISOU  777  N   LYS A 107     7197  10628   6505   -164   -127   1490       N  
ATOM    778  CA  LYS A 107     -12.269  13.978   8.402  1.00 61.73           C  
ANISOU  778  CA  LYS A 107     6974  10203   6276   -152   -173   1454       C  
ATOM    779  C   LYS A 107     -11.634  14.873   9.469  1.00 65.89           C  
ANISOU  779  C   LYS A 107     7507  10769   6756    -57   -184   1371       C  
ATOM    780  O   LYS A 107     -10.514  14.604   9.917  1.00 56.79           O  
ANISOU  780  O   LYS A 107     6404   9539   5632    -54   -224   1360       O  
ATOM    781  CB  LYS A 107     -11.527  14.128   7.033  1.00 57.22           C  
ANISOU  781  CB  LYS A 107     6448   9456   5835   -151   -188   1407       C  
ATOM    782  CG  LYS A 107     -11.634  12.842   6.225  1.00 57.33           C  
ANISOU  782  CG  LYS A 107     6484   9396   5900   -245   -212   1489       C  
ATOM    783  CD  LYS A 107     -11.404  12.979   4.730  1.00 56.54           C  
ANISOU  783  CD  LYS A 107     6403   9181   5898   -238   -212   1453       C  
ATOM    784  CE  LYS A 107     -11.496  11.611   4.063  1.00 52.94           C  
ANISOU  784  CE  LYS A 107     5971   8656   5484   -320   -254   1524       C  
ATOM    785  NZ  LYS A 107     -10.925  11.673   2.678  1.00 53.82           N1+
ANISOU  785  NZ  LYS A 107     6110   8652   5686   -294   -264   1476       N1+
ATOM    786  N   MET A 108     -12.326  15.932   9.864  1.00 74.18           N  
ANISOU  786  N   MET A 108     8507  11936   7739     26   -158   1306       N  
ATOM    787  CA  MET A 108     -11.795  16.831  10.887  1.00 81.13           C  
ANISOU  787  CA  MET A 108     9392  12858   8576    131   -183   1213       C  
ATOM    788  C   MET A 108     -11.489  16.211  12.238  1.00 85.68           C  
ANISOU  788  C   MET A 108     9971  13528   9054    128   -200   1257       C  
ATOM    789  O   MET A 108     -10.630  16.716  12.967  1.00 79.47           O  
ANISOU  789  O   MET A 108     9215  12716   8264    200   -239   1182       O  
ATOM    790  CB  MET A 108     -12.699  18.026  11.077  1.00 86.97           C  
ANISOU  790  CB  MET A 108    10074  13716   9253    230   -163   1129       C  
ATOM    791  CG  MET A 108     -12.235  19.166  10.206  1.00 93.15           C  
ANISOU  791  CG  MET A 108    10880  14358  10154    289   -190   1026       C  
ATOM    792  SD  MET A 108     -13.311  20.607  10.235  1.00 98.77           S  
ANISOU  792  SD  MET A 108    11530  15178  10819    406   -184    919       S  
ATOM    793  CE  MET A 108     -14.703  20.014   9.297  1.00100.01           C  
ANISOU  793  CE  MET A 108    11635  15412  10950    322   -111   1012       C  
ATOM    794  N   ALA A 109     -12.148  15.106  12.572  1.00101.80           N  
ANISOU  794  N   ALA A 109    11982  15672  11023     41   -178   1383       N  
ATOM    795  CA  ALA A 109     -11.797  14.382  13.806  1.00109.76           C  
ANISOU  795  CA  ALA A 109    12994  16764  11946     22   -198   1449       C  
ATOM    796  C   ALA A 109     -10.272  14.150  13.886  1.00104.99           C  
ANISOU  796  C   ALA A 109    12473  15985  11430     19   -254   1413       C  
ATOM    797  O   ALA A 109      -9.604  14.501  14.851  1.00 98.31           O  
ANISOU  797  O   ALA A 109    11646  15165  10542     88   -282   1359       O  
ATOM    798  CB  ALA A 109     -12.560  13.061  13.883  1.00110.54           C  
ANISOU  798  CB  ALA A 109    13056  16944  12000   -101   -185   1616       C  
ATOM    799  N   ASN A 110      -9.712  13.566  12.855  1.00106.46           N  
ANISOU  799  N   ASN A 110    12711  15995  11743    -48   -274   1433       N  
ATOM    800  CA  ASN A 110      -8.340  13.141  12.936  1.00103.67           C  
ANISOU  800  CA  ASN A 110    12428  15496  11464    -72   -325   1430       C  
ATOM    801  C   ASN A 110      -7.277  14.126  12.505  1.00102.40           C  
ANISOU  801  C   ASN A 110    12308  15197  11399      6   -350   1307       C  
ATOM    802  O   ASN A 110      -6.146  13.761  12.276  1.00 99.31           O  
ANISOU  802  O   ASN A 110    11972  14667  11091    -12   -390   1301       O  
ATOM    803  CB  ASN A 110      -8.211  11.814  12.238  1.00101.20           C  
ANISOU  803  CB  ASN A 110    12142  15088  11219   -188   -345   1531       C  
ATOM    804  CG  ASN A 110      -9.306  10.874  12.655  1.00110.50           C  
ANISOU  804  CG  ASN A 110    13277  16398  12309   -274   -342   1670       C  
ATOM    805  ND2 ASN A 110      -8.939   9.797  13.348  1.00 98.47           N  
ANISOU  805  ND2 ASN A 110    11687  14985  10740   -294   -296   1711       N  
ATOM    806  OD1 ASN A 110     -10.483  11.139  12.405  1.00104.25           O  
ANISOU  806  OD1 ASN A 110    12505  15615  11490   -323   -382   1746       O  
ATOM    807  N   PHE A 111      -7.639  15.382  12.426  1.00100.43           N  
ANISOU  807  N   PHE A 111    12027  14988  11141     96   -335   1215       N  
ATOM    808  CA  PHE A 111      -6.653  16.463  12.359  1.00101.71           C  
ANISOU  808  CA  PHE A 111    12217  15043  11382    179   -375   1104       C  
ATOM    809  C   PHE A 111      -7.101  17.645  13.244  1.00118.06           C  
ANISOU  809  C   PHE A 111    14252  17229  13376    295   -385   1010       C  
ATOM    810  O   PHE A 111      -7.969  18.445  12.848  1.00113.29           O  
ANISOU  810  O   PHE A 111    13604  16678  12760    339   -362    966       O  
ATOM    811  CB  PHE A 111      -6.473  16.967  10.926  1.00 92.43           C  
ANISOU  811  CB  PHE A 111    11045  13741  10332    171   -369   1078       C  
ATOM    812  CG  PHE A 111      -5.657  16.069  10.044  1.00 81.55           C  
ANISOU  812  CG  PHE A 111     9709  12229   9046     95   -379   1131       C  
ATOM    813  CD1 PHE A 111      -6.165  14.852   9.601  1.00 80.76           C  
ANISOU  813  CD1 PHE A 111     9612  12142   8929      6   -358   1223       C  
ATOM    814  CD2 PHE A 111      -4.402  16.467   9.599  1.00 76.80           C  
ANISOU  814  CD2 PHE A 111     9138  11490   8551    119   -417   1089       C  
ATOM    815  CE1 PHE A 111      -5.411  14.023   8.781  1.00 76.95           C  
ANISOU  815  CE1 PHE A 111     9168  11539   8527    -45   -380   1257       C  
ATOM    816  CE2 PHE A 111      -3.652  15.654   8.755  1.00 75.60           C  
ANISOU  816  CE2 PHE A 111     9017  11233   8473     64   -426   1132       C  
ATOM    817  CZ  PHE A 111      -4.155  14.429   8.348  1.00 73.34           C  
ANISOU  817  CZ  PHE A 111     8739  10963   8163    -11   -410   1208       C  
ATOM    818  N   GLN A 112      -6.507  17.765  14.434  1.00124.29           N  
ANISOU  818  N   GLN A 112    15058  18056  14111    353   -426    970       N  
ATOM    819  CA  GLN A 112      -6.852  18.866  15.333  1.00119.01           C  
ANISOU  819  CA  GLN A 112    14358  17495  13363    481   -451    864       C  
ATOM    820  C   GLN A 112      -6.099  20.164  15.018  1.00111.58           C  
ANISOU  820  C   GLN A 112    13438  16414  12542    566   -519    742       C  
ATOM    821  O   GLN A 112      -6.679  21.242  15.138  1.00105.35           O  
ANISOU  821  O   GLN A 112    12616  15679  11732    661   -540    651       O  
ATOM    822  CB  GLN A 112      -6.735  18.435  16.808  1.00123.00           C  
ANISOU  822  CB  GLN A 112    14861  18137  13735    518   -466    876       C  
ATOM    823  CG  GLN A 112      -7.993  17.719  17.306  1.00128.06           C  
ANISOU  823  CG  GLN A 112    15439  18997  14219    484   -401    972       C  
ATOM    824  CD  GLN A 112      -9.275  18.361  16.757  1.00127.56           C  
ANISOU  824  CD  GLN A 112    15312  19032  14122    516   -356    948       C  
ATOM    825  NE2 GLN A 112      -9.945  17.677  15.817  1.00113.31           N  
ANISOU  825  NE2 GLN A 112    13489  17215  12348    407   -304   1049       N  
ATOM    826  OE1 GLN A 112      -9.637  19.473  17.153  1.00123.96           O  
ANISOU  826  OE1 GLN A 112    14826  18654  13618    642   -378    833       O  
ATOM    827  N   ASN A 113      -4.863  20.050  14.561  1.00112.57           N  
ANISOU  827  N   ASN A 113    13614  16362  12794    529   -559    746       N  
ATOM    828  CA  ASN A 113      -4.083  21.197  14.123  1.00116.58           C  
ANISOU  828  CA  ASN A 113    14134  16718  13440    585   -629    661       C  
ATOM    829  C   ASN A 113      -4.678  21.572  12.780  1.00132.86           C  
ANISOU  829  C   ASN A 113    16166  18731  15583    565   -603    665       C  
ATOM    830  O   ASN A 113      -3.976  21.745  11.791  1.00123.08           O  
ANISOU  830  O   ASN A 113    14938  17349  14475    519   -614    691       O  
ATOM    831  CB  ASN A 113      -2.666  20.768  13.793  1.00116.46           C  
ANISOU  831  CB  ASN A 113    14169  16543  13538    535   -666    689       C  
ATOM    832  CG  ASN A 113      -1.758  20.791  14.996  1.00116.32           C  
ANISOU  832  CG  ASN A 113    14184  16528  13482    588   -727    645       C  
ATOM    833  ND2 ASN A 113      -0.600  21.420  14.852  1.00112.01           N  
ANISOU  833  ND2 ASN A 113    13667  15833  13058    601   -797    612       N  
ATOM    834  OD1 ASN A 113      -2.089  20.245  16.040  1.00114.20           O  
ANISOU  834  OD1 ASN A 113    13911  16402  13076    615   -712    647       O  
ATOM    835  N   PHE A 114      -5.994  21.670  12.754  1.00140.11           N  
ANISOU  835  N   PHE A 114    17039  19780  16416    604   -568    641       N  
ATOM    836  CA  PHE A 114      -6.787  22.339  11.717  1.00135.21           C  
ANISOU  836  CA  PHE A 114    16387  19139  15848    572   -529    662       C  
ATOM    837  C   PHE A 114      -7.887  23.293  12.164  1.00130.28           C  
ANISOU  837  C   PHE A 114    15711  18649  15139    651   -518    600       C  
ATOM    838  O   PHE A 114      -8.752  22.919  12.940  1.00126.32           O  
ANISOU  838  O   PHE A 114    15177  18311  14507    638   -457    639       O  
ATOM    839  CB  PHE A 114      -7.462  21.269  10.876  1.00136.69           C  
ANISOU  839  CB  PHE A 114    16576  19340  16018    454   -449    781       C  
ATOM    840  CG  PHE A 114      -7.783  21.718   9.502  1.00135.02           C  
ANISOU  840  CG  PHE A 114    16342  19074  15883    417   -417    805       C  
ATOM    841  CD1 PHE A 114      -6.876  22.470   8.793  1.00143.00           C  
ANISOU  841  CD1 PHE A 114    17365  19932  17036    416   -455    790       C  
ATOM    842  CD2 PHE A 114      -8.986  21.412   8.927  1.00133.06           C  
ANISOU  842  CD2 PHE A 114    16056  18933  15567    388   -353    843       C  
ATOM    843  CE1 PHE A 114      -7.153  22.899   7.517  1.00138.86           C  
ANISOU  843  CE1 PHE A 114    16815  19365  16578    387   -427    816       C  
ATOM    844  CE2 PHE A 114      -9.285  21.848   7.657  1.00136.84           C  
ANISOU  844  CE2 PHE A 114    16516  19360  16117    360   -327    860       C  
ATOM    845  CZ  PHE A 114      -8.364  22.590   6.951  1.00143.87           C  
ANISOU  845  CZ  PHE A 114    17419  20101  17142    361   -363    846       C  
ATOM    846  N   LYS A 115      -7.890  24.514  11.643  1.00124.73           N  
ANISOU  846  N   LYS A 115    14997  17876  14518    729   -583    508       N  
ATOM    847  CA  LYS A 115      -9.032  25.368  11.867  1.00123.72           C  
ANISOU  847  CA  LYS A 115    14823  17861  14323    823   -592    427       C  
ATOM    848  C   LYS A 115      -9.532  25.794  10.499  1.00119.86           C  
ANISOU  848  C   LYS A 115    14310  17302  13926    781   -568    453       C  
ATOM    849  O   LYS A 115      -8.776  25.748   9.531  1.00110.26           O  
ANISOU  849  O   LYS A 115    13116  15936  12841    711   -574    505       O  
ATOM    850  CB  LYS A 115      -8.630  26.577  12.723  1.00125.29           C  
ANISOU  850  CB  LYS A 115    15028  18033  14544    962   -710    287       C  
ATOM    851  CG  LYS A 115      -7.913  26.242  14.034  1.00127.62           C  
ANISOU  851  CG  LYS A 115    15352  18370  14766   1010   -750    254       C  
ATOM    852  CD  LYS A 115      -8.813  25.608  15.098  1.00128.78           C  
ANISOU  852  CD  LYS A 115    15466  18758  14706   1049   -690    261       C  
ATOM    853  CE  LYS A 115      -8.954  24.101  14.930  1.00123.95           C  
ANISOU  853  CE  LYS A 115    14857  18207  14030    912   -583    414       C  
ATOM    854  NZ  LYS A 115      -9.237  23.394  16.209  1.00120.93           N1+
ANISOU  854  NZ  LYS A 115    14456  18016  13473    939   -555    439       N1+
ATOM    855  N   PRO A 116     -10.802  26.216  10.411  1.00125.13           N  
ANISOU  855  N   PRO A 116    14931  18090  14523    828   -541    417       N  
ATOM    856  CA  PRO A 116     -11.347  26.573   9.115  1.00134.52           C  
ANISOU  856  CA  PRO A 116    16097  19221  15792    787   -514    445       C  
ATOM    857  C   PRO A 116     -11.017  28.018   8.692  1.00144.27           C  
ANISOU  857  C   PRO A 116    17330  20321  17162    859   -617    358       C  
ATOM    858  O   PRO A 116     -10.663  28.842   9.540  1.00159.07           O  
ANISOU  858  O   PRO A 116    19212  22178  19046    964   -716    253       O  
ATOM    859  CB  PRO A 116     -12.856  26.419   9.345  1.00135.22           C  
ANISOU  859  CB  PRO A 116    16131  19505  15737    815   -448    440       C  
ATOM    860  CG  PRO A 116     -13.056  26.768  10.790  1.00128.13           C  
ANISOU  860  CG  PRO A 116    15219  18746  14716    936   -491    345       C  
ATOM    861  CD  PRO A 116     -11.753  26.528  11.499  1.00126.46           C  
ANISOU  861  CD  PRO A 116    15059  18451  14537    938   -545    338       C  
ATOM    862  N   ARG A 117     -11.090  28.298   7.388  1.00141.69           N  
ANISOU  862  N   ARG A 117    16992  19898  16944    802   -604    406       N  
ATOM    863  CA  ARG A 117     -11.293  29.667   6.867  1.00145.51           C  
ANISOU  863  CA  ARG A 117    17454  20297  17534    866   -688    338       C  
ATOM    864  C   ARG A 117     -12.599  29.766   6.044  1.00137.08           C  
ANISOU  864  C   ARG A 117    16345  19307  16431    853   -623    354       C  
ATOM    865  O   ARG A 117     -12.810  30.761   5.348  1.00145.79           O  
ANISOU  865  O   ARG A 117    17429  20332  17631    880   -679    324       O  
ATOM    866  CB  ARG A 117     -10.085  30.153   6.033  1.00140.50           C  
ANISOU  866  CB  ARG A 117    16836  19463  17084    818   -753    384       C  
ATOM    867  CG  ARG A 117      -9.151  31.124   6.763  1.00146.33           C  
ANISOU  867  CG  ARG A 117    17592  20089  17915    897   -897    300       C  
ATOM    868  CD  ARG A 117      -8.042  31.639   5.849  1.00145.81           C  
ANISOU  868  CD  ARG A 117    17525  19837  18037    839   -961    369       C  
ATOM    869  NE  ARG A 117      -7.071  30.589   5.505  1.00144.41           N  
ANISOU  869  NE  ARG A 117    17369  19626  17874    739   -893    478       N  
ATOM    870  CZ  ARG A 117      -6.422  30.477   4.340  1.00138.06           C  
ANISOU  870  CZ  ARG A 117    16548  18732  17175    654   -871    585       C  
ATOM    871  NH1 ARG A 117      -6.619  31.348   3.345  1.00129.81           N1+
ANISOU  871  NH1 ARG A 117    15465  17619  16237    645   -908    615       N1+
ATOM    872  NH2 ARG A 117      -5.567  29.469   4.159  1.00132.93           N  
ANISOU  872  NH2 ARG A 117    15918  18069  16518    582   -814    666       N  
ATOM    873  N   SER A 118     -13.455  28.752   6.157  1.00123.69           N  
ANISOU  873  N   SER A 118    14632  17760  14602    807   -514    407       N  
ATOM    874  CA  SER A 118     -14.731  28.719   5.448  1.00119.39           C  
ANISOU  874  CA  SER A 118    14045  17305  14011    790   -447    428       C  
ATOM    875  C   SER A 118     -15.776  27.881   6.166  1.00119.44           C  
ANISOU  875  C   SER A 118    14021  17517  13841    792   -366    445       C  
ATOM    876  O   SER A 118     -15.763  26.663   6.082  1.00119.98           O  
ANISOU  876  O   SER A 118    14098  17628  13860    695   -289    547       O  
ATOM    877  CB  SER A 118     -14.552  28.167   4.046  1.00105.14           C  
ANISOU  877  CB  SER A 118    12244  15414  12287    675   -386    538       C  
ATOM    878  OG  SER A 118     -14.299  29.210   3.149  1.00 97.29           O  
ANISOU  878  OG  SER A 118    11251  14273  11442    685   -453    526       O  
ATOM    879  N   ASN A 119     -16.704  28.543   6.839  1.00110.99           N  
ANISOU  879  N   ASN A 119    12910  16579  12681    903   -390    349       N  
ATOM    880  CA  ASN A 119     -17.689  27.853   7.627  1.00104.53           C  
ANISOU  880  CA  ASN A 119    12046  15983  11687    917   -319    368       C  
ATOM    881  C   ASN A 119     -18.976  27.679   6.839  1.00 92.49           C  
ANISOU  881  C   ASN A 119    10470  14544  10125    875   -244    416       C  
ATOM    882  O   ASN A 119     -19.440  28.592   6.197  1.00 77.78           O  
ANISOU  882  O   ASN A 119     8591  12637   8325    919   -275    359       O  
ATOM    883  CB  ASN A 119     -17.952  28.592   8.946  1.00115.27           C  
ANISOU  883  CB  ASN A 119    13381  17468  12947   1074   -385    236       C  
ATOM    884  CG  ASN A 119     -16.792  28.499   9.935  1.00126.85           C  
ANISOU  884  CG  ASN A 119    14898  18856  14441   1114   -460    192       C  
ATOM    885  ND2 ASN A 119     -16.036  29.579  10.076  1.00128.17           N  
ANISOU  885  ND2 ASN A 119    15084  19068  14547   1038   -406    282       N  
ATOM    886  OD1 ASN A 119     -16.594  27.466  10.568  1.00127.60           O  
ANISOU  886  OD1 ASN A 119    15015  18843  14621   1209   -573     80       O  
ATOM    887  N   ARG A 120     -19.503  26.469   6.876  1.00 82.35           N  
ANISOU  887  N   ARG A 120     9164  13370   8752    782   -154    529       N  
ATOM    888  CA  ARG A 120     -20.835  26.110   6.435  1.00 78.12           C  
ANISOU  888  CA  ARG A 120     8569  12965   8146    745    -80    583       C  
ATOM    889  C   ARG A 120     -21.813  26.713   7.432  1.00 85.50           C  
ANISOU  889  C   ARG A 120     9435  14115   8935    873    -86    498       C  
ATOM    890  O   ARG A 120     -21.668  26.532   8.638  1.00 78.94           O  
ANISOU  890  O   ARG A 120     8589  13410   7993    929    -94    478       O  
ATOM    891  CB  ARG A 120     -20.978  24.586   6.442  1.00 71.76           C  
ANISOU  891  CB  ARG A 120     7759  12219   7288    614     -6    731       C  
ATOM    892  CG  ARG A 120     -22.184  24.048   5.716  1.00 69.45           C  
ANISOU  892  CG  ARG A 120     7415  12008   6965    541     61    813       C  
ATOM    893  CD  ARG A 120     -22.092  22.533   5.588  1.00 73.62           C  
ANISOU  893  CD  ARG A 120     7954  12533   7483    401    105    961       C  
ATOM    894  NE  ARG A 120     -21.842  21.908   6.890  1.00 79.53           N  
ANISOU  894  NE  ARG A 120     8691  13402   8125    401    108   1003       N  
ATOM    895  CZ  ARG A 120     -22.803  21.637   7.794  1.00 83.58           C  
ANISOU  895  CZ  ARG A 120     9124  14144   8487    421    145   1045       C  
ATOM    896  NH1 ARG A 120     -24.083  21.932   7.551  1.00 79.18           N1+
ANISOU  896  NH1 ARG A 120     8491  13723   7869    443    183   1046       N1+
ATOM    897  NH2 ARG A 120     -22.494  21.061   8.954  1.00 79.77           N  
ANISOU  897  NH2 ARG A 120     8630  13769   7909    419    144   1092       N  
ATOM    898  N   GLU A 121     -22.783  27.461   6.921  1.00 89.25           N  
ANISOU  898  N   GLU A 121     9866  14635   9409    928    -86    442       N  
ATOM    899  CA  GLU A 121     -23.896  27.972   7.709  1.00 84.43           C  
ANISOU  899  CA  GLU A 121     9177  14251   8651   1049    -81    366       C  
ATOM    900  C   GLU A 121     -25.190  27.561   6.986  1.00 85.42           C  
ANISOU  900  C   GLU A 121     9239  14481   8735    985      0    445       C  
ATOM    901  O   GLU A 121     -25.356  27.860   5.794  1.00 88.51           O  
ANISOU  901  O   GLU A 121     9649  14740   9241    941      0    450       O  
ATOM    902  CB  GLU A 121     -23.766  29.493   7.849  1.00 87.28           C  
ANISOU  902  CB  GLU A 121     9547  14550   9062   1207   -189    190       C  
ATOM    903  CG  GLU A 121     -24.250  30.034   9.198  1.00 93.79           C  
ANISOU  903  CG  GLU A 121    10317  15591   9725   1377   -226     73       C  
ATOM    904  CD  GLU A 121     -24.917  31.394   9.092  1.00 94.57           C  
ANISOU  904  CD  GLU A 121    10386  15710   9834   1530   -305    -85       C  
ATOM    905  OE1 GLU A 121     -24.282  32.346   8.582  1.00 95.61           O  
ANISOU  905  OE1 GLU A 121    10573  15631  10123   1568   -408   -170       O  
ATOM    906  OE2 GLU A 121     -26.088  31.507   9.519  1.00 95.35           O1-
ANISOU  906  OE2 GLU A 121    10402  16040   9785   1613   -269   -119       O1-
ATOM    907  N   GLU A 122     -26.067  26.832   7.676  1.00 81.77           N  
ANISOU  907  N   GLU A 122     8700  14253   8115    970     69    519       N  
ATOM    908  CA  GLU A 122     -27.355  26.418   7.126  1.00 81.63           C  
ANISOU  908  CA  GLU A 122     8610  14357   8047    912    142    599       C  
ATOM    909  C   GLU A 122     -28.342  27.559   7.290  1.00 83.13           C  
ANISOU  909  C   GLU A 122     8734  14683   8167   1062    120    470       C  
ATOM    910  O   GLU A 122     -28.396  28.191   8.325  1.00 90.10           O  
ANISOU  910  O   GLU A 122     9585  15701   8945   1206     80    363       O  
ATOM    911  CB  GLU A 122     -27.904  25.169   7.830  1.00 83.20           C  
ANISOU  911  CB  GLU A 122     8741  14761   8110    829    216    748       C  
ATOM    912  CG  GLU A 122     -27.073  23.897   7.660  1.00 82.27           C  
ANISOU  912  CG  GLU A 122     8681  14520   8057    672    233    889       C  
ATOM    913  CD  GLU A 122     -26.817  23.556   6.196  1.00 86.12           C  
ANISOU  913  CD  GLU A 122     9230  14781   8709    555    236    940       C  
ATOM    914  OE1 GLU A 122     -27.744  23.011   5.515  1.00 83.36           O  
ANISOU  914  OE1 GLU A 122     8837  14474   8360    471    282   1029       O  
ATOM    915  OE2 GLU A 122     -25.682  23.861   5.726  1.00 77.73           O1-
ANISOU  915  OE2 GLU A 122     8256  13504   7772    553    188    888       O1-
ATOM    916  N   MET A 123     -29.121  27.831   6.262  1.00 84.11           N  
ANISOU  916  N   MET A 123     8838  14772   8347   1036    139    474       N  
ATOM    917  CA  MET A 123     -30.001  28.998   6.252  1.00 84.25           C  
ANISOU  917  CA  MET A 123     8803  14881   8324   1179    105    340       C  
ATOM    918  C   MET A 123     -31.032  28.869   5.134  1.00 83.17           C  
ANISOU  918  C   MET A 123     8629  14746   8224   1108    157    398       C  
ATOM    919  O   MET A 123     -30.889  28.057   4.201  1.00 87.93           O  
ANISOU  919  O   MET A 123     9265  15225   8917    957    200    519       O  
ATOM    920  CB  MET A 123     -29.193  30.325   6.135  1.00 86.77           C  
ANISOU  920  CB  MET A 123     9192  15015   8760   1296    -12    175       C  
ATOM    921  CG  MET A 123     -28.733  30.735   4.734  1.00 86.13           C  
ANISOU  921  CG  MET A 123     9180  14667   8876   1226    -48    179       C  
ATOM    922  SD  MET A 123     -27.632  32.182   4.654  1.00 83.29           S  
ANISOU  922  SD  MET A 123     8896  14075   8672   1336   -200     23       S  
ATOM    923  CE  MET A 123     -26.265  31.578   5.645  1.00 79.89           C  
ANISOU  923  CE  MET A 123     8521  13603   8228   1314   -218     51       C  
ATOM    924  N   LYS A 124     -32.094  29.646   5.243  1.00 79.90           N  
ANISOU  924  N   LYS A 124     8142  14480   7733   1223    150    309       N  
ATOM    925  CA  LYS A 124     -33.173  29.568   4.275  1.00 78.51           C  
ANISOU  925  CA  LYS A 124     7921  14332   7577   1169    198    357       C  
ATOM    926  C   LYS A 124     -32.757  30.399   3.088  1.00 73.21           C  
ANISOU  926  C   LYS A 124     7324  13405   7084   1168    136    287       C  
ATOM    927  O   LYS A 124     -31.921  31.270   3.221  1.00 67.45           O  
ANISOU  927  O   LYS A 124     6654  12539   6433   1250     46    177       O  
ATOM    928  CB  LYS A 124     -34.469  30.116   4.880  1.00 82.92           C  
ANISOU  928  CB  LYS A 124     8366  15159   7978   1303    212    283       C  
ATOM    929  CG  LYS A 124     -34.925  29.391   6.133  1.00 82.95           C  
ANISOU  929  CG  LYS A 124     8277  15455   7785   1321    273    355       C  
ATOM    930  CD  LYS A 124     -35.409  27.976   5.831  1.00 84.26           C  
ANISOU  930  CD  LYS A 124     8398  15689   7928   1136    370    567       C  
ATOM    931  CE  LYS A 124     -35.494  27.138   7.114  1.00 81.80           C  
ANISOU  931  CE  LYS A 124     8010  15620   7447   1126    417    669       C  
ATOM    932  NZ  LYS A 124     -36.090  25.786   6.909  1.00 77.61           N1+
ANISOU  932  NZ  LYS A 124     7420  15177   6891    950    496    885       N1+
ATOM    933  N   PHE A 125     -33.347  30.163   1.923  1.00 75.41           N  
ANISOU  933  N   PHE A 125     7597  13621   7432   1078    176    354       N  
ATOM    934  CA  PHE A 125     -32.869  30.867   0.746  1.00 71.60           C  
ANISOU  934  CA  PHE A 125     7185  12898   7120   1064    120    310       C  
ATOM    935  C   PHE A 125     -32.921  32.365   0.961  1.00 76.43           C  
ANISOU  935  C   PHE A 125     7797  13483   7757   1229     19    137       C  
ATOM    936  O   PHE A 125     -31.952  33.051   0.637  1.00 70.25           O  
ANISOU  936  O   PHE A 125     7086  12499   7107   1249    -64     83       O  
ATOM    937  CB  PHE A 125     -33.631  30.472  -0.512  1.00 73.28           C  
ANISOU  937  CB  PHE A 125     7381  13074   7385    964    175    394       C  
ATOM    938  CG  PHE A 125     -32.884  30.784  -1.785  1.00 73.07           C  
ANISOU  938  CG  PHE A 125     7434  12794   7534    905    137    404       C  
ATOM    939  CD1 PHE A 125     -33.022  32.024  -2.417  1.00 76.84           C  
ANISOU  939  CD1 PHE A 125     7922  13173   8098    985     68    305       C  
ATOM    940  CD2 PHE A 125     -32.017  29.847  -2.342  1.00 72.56           C  
ANISOU  940  CD2 PHE A 125     7429  12595   7544    776    165    514       C  
ATOM    941  CE1 PHE A 125     -32.328  32.315  -3.599  1.00 79.76           C  
ANISOU  941  CE1 PHE A 125     8354  13326   8624    928     35    331       C  
ATOM    942  CE2 PHE A 125     -31.312  30.138  -3.506  1.00 72.12           C  
ANISOU  942  CE2 PHE A 125     7434  12331   7635    732    134    527       C  
ATOM    943  CZ  PHE A 125     -31.463  31.376  -4.135  1.00 74.70           C  
ANISOU  943  CZ  PHE A 125     7764  12572   8044    805     72    443       C  
ATOM    944  N   HIS A 126     -34.040  32.856   1.535  1.00 81.48           N  
ANISOU  944  N   HIS A 126     8353  14332   8271   1350     19     55       N  
ATOM    945  CA  HIS A 126     -34.267  34.303   1.722  1.00 82.15           C  
ANISOU  945  CA  HIS A 126     8431  14404   8375   1523    -89   -124       C  
ATOM    946  C   HIS A 126     -33.218  34.911   2.657  1.00 82.12           C  
ANISOU  946  C   HIS A 126     8476  14337   8387   1629   -192   -233       C  
ATOM    947  O   HIS A 126     -32.826  36.067   2.471  1.00 84.47           O  
ANISOU  947  O   HIS A 126     8815  14485   8794   1722   -315   -355       O  
ATOM    948  CB  HIS A 126     -35.724  34.621   2.195  1.00 88.31           C  
ANISOU  948  CB  HIS A 126     9104  15452   8998   1641    -64   -193       C  
ATOM    949  CG  HIS A 126     -35.968  34.420   3.663  1.00 89.79           C  
ANISOU  949  CG  HIS A 126     9223  15900   8993   1748    -47   -234       C  
ATOM    950  CD2 HIS A 126     -36.466  33.361   4.349  1.00 91.77           C  
ANISOU  950  CD2 HIS A 126     9397  16387   9084   1697     58   -121       C  
ATOM    951  ND1 HIS A 126     -35.682  35.388   4.605  1.00 93.45           N  
ANISOU  951  ND1 HIS A 126     9688  16407   9410   1935   -154   -407       N  
ATOM    952  CE1 HIS A 126     -35.976  34.926   5.810  1.00100.38           C  
ANISOU  952  CE1 HIS A 126    10493  17547  10097   2001   -107   -402       C  
ATOM    953  NE2 HIS A 126     -36.462  33.702   5.682  1.00 98.10           N  
ANISOU  953  NE2 HIS A 126    10152  17383   9736   1854     23   -222       N  
ATOM    954  N   GLU A 127     -32.752  34.128   3.631  1.00 79.56           N  
ANISOU  954  N   GLU A 127     8147  14116   7963   1610   -150   -183       N  
ATOM    955  CA  GLU A 127     -31.633  34.550   4.495  1.00 88.76           C  
ANISOU  955  CA  GLU A 127     9367  15206   9150   1691   -242   -270       C  
ATOM    956  C   GLU A 127     -30.325  34.714   3.681  1.00 88.74           C  
ANISOU  956  C   GLU A 127     9467  14894   9355   1597   -301   -234       C  
ATOM    957  O   GLU A 127     -29.499  35.604   3.951  1.00 92.32           O  
ANISOU  957  O   GLU A 127     9970  15207   9899   1682   -424   -340       O  
ATOM    958  CB  GLU A 127     -31.440  33.575   5.689  1.00 88.79           C  
ANISOU  958  CB  GLU A 127     9341  15399   8997   1679   -175   -207       C  
ATOM    959  CG  GLU A 127     -32.705  33.346   6.549  1.00 97.84           C  
ANISOU  959  CG  GLU A 127    10369  16883   9922   1768   -109   -218       C  
ATOM    960  CD  GLU A 127     -32.489  32.367   7.707  1.00 99.57           C  
ANISOU  960  CD  GLU A 127    10551  17293   9987   1747    -44   -135       C  
ATOM    961  OE1 GLU A 127     -33.092  31.263   7.693  1.00 90.54           O  
ANISOU  961  OE1 GLU A 127     9346  16295   8756   1629     68     23       O  
ATOM    962  OE2 GLU A 127     -31.696  32.683   8.624  1.00103.73           O1-
ANISOU  962  OE2 GLU A 127    11110  17816  10486   1842   -113   -221       O1-
ATOM    963  N   PHE A 128     -30.139  33.856   2.683  1.00 85.78           N  
ANISOU  963  N   PHE A 128     9118  14418   9055   1425   -218    -84       N  
ATOM    964  CA  PHE A 128     -28.983  33.965   1.797  1.00 83.68           C  
ANISOU  964  CA  PHE A 128     8934  13886   8972   1335   -261    -35       C  
ATOM    965  C   PHE A 128     -29.098  35.240   0.966  1.00 82.23           C  
ANISOU  965  C   PHE A 128     8764  13554   8924   1394   -360   -119       C  
ATOM    966  O   PHE A 128     -28.157  36.040   0.902  1.00 77.20           O  
ANISOU  966  O   PHE A 128     8178  12738   8416   1429   -472   -173       O  
ATOM    967  CB  PHE A 128     -28.871  32.721   0.896  1.00 82.15           C  
ANISOU  967  CB  PHE A 128     8758  13645   8809   1154   -151    134       C  
ATOM    968  CG  PHE A 128     -27.897  32.869  -0.277  1.00 83.21           C  
ANISOU  968  CG  PHE A 128     8958  13532   9123   1066   -183    190       C  
ATOM    969  CD1 PHE A 128     -26.526  33.006  -0.062  1.00 79.66           C  
ANISOU  969  CD1 PHE A 128     8569  12932   8763   1055   -245    189       C  
ATOM    970  CD2 PHE A 128     -28.355  32.817  -1.592  1.00 77.42           C  
ANISOU  970  CD2 PHE A 128     8221  12733   8461    993   -147    252       C  
ATOM    971  CE1 PHE A 128     -25.645  33.117  -1.133  1.00 82.36           C  
ANISOU  971  CE1 PHE A 128     8958  13075   9260    976   -268    253       C  
ATOM    972  CE2 PHE A 128     -27.469  32.939  -2.663  1.00 79.23           C  
ANISOU  972  CE2 PHE A 128     8500  12764   8840    919   -171    311       C  
ATOM    973  CZ  PHE A 128     -26.117  33.091  -2.428  1.00 79.10           C  
ANISOU  973  CZ  PHE A 128     8535  12612   8907    910   -230    315       C  
ATOM    974  N   VAL A 129     -30.263  35.445   0.356  1.00 83.83           N  
ANISOU  974  N   VAL A 129     8918  13832   9100   1405   -327   -126       N  
ATOM    975  CA  VAL A 129     -30.463  36.613  -0.504  1.00 87.68           C  
ANISOU  975  CA  VAL A 129     9415  14182   9716   1453   -419   -193       C  
ATOM    976  C   VAL A 129     -30.231  37.837   0.343  1.00 91.90           C  
ANISOU  976  C   VAL A 129     9955  14692  10269   1622   -569   -362       C  
ATOM    977  O   VAL A 129     -29.632  38.807  -0.119  1.00 86.10           O  
ANISOU  977  O   VAL A 129     9260  13759   9693   1648   -692   -407       O  
ATOM    978  CB  VAL A 129     -31.879  36.668  -1.121  1.00 88.52           C  
ANISOU  978  CB  VAL A 129     9460  14405   9768   1460   -363   -193       C  
ATOM    979  CG1 VAL A 129     -32.088  37.965  -1.894  1.00 91.46           C  
ANISOU  979  CG1 VAL A 129     9841  14638  10271   1525   -475   -275       C  
ATOM    980  CG2 VAL A 129     -32.109  35.479  -2.045  1.00 84.65           C  
ANISOU  980  CG2 VAL A 129     8967  13919   9276   1293   -232    -29       C  
ATOM    981  N   GLU A 130     -30.695  37.742   1.593  1.00 96.84           N  
ANISOU  981  N   GLU A 130    10537  15527  10730   1736   -562   -448       N  
ATOM    982  CA  GLU A 130     -30.622  38.815   2.565  1.00 99.70           C  
ANISOU  982  CA  GLU A 130    10895  15914  11071   1925   -703   -630       C  
ATOM    983  C   GLU A 130     -29.194  39.051   3.005  1.00 93.65           C  
ANISOU  983  C   GLU A 130    10200  14975  10408   1928   -801   -650       C  
ATOM    984  O   GLU A 130     -28.715  40.165   2.828  1.00 92.03           O  
ANISOU  984  O   GLU A 130    10029  14590  10346   1997   -956   -741       O  
ATOM    985  CB  GLU A 130     -31.541  38.503   3.751  1.00109.72           C  
ANISOU  985  CB  GLU A 130    12086  17490  12111   2043   -649   -699       C  
ATOM    986  CG  GLU A 130     -31.404  39.409   4.966  1.00117.54           C  
ANISOU  986  CG  GLU A 130    13070  18550  13040   2254   -786   -892       C  
ATOM    987  CD  GLU A 130     -32.235  38.911   6.143  1.00121.17           C  
ANISOU  987  CD  GLU A 130    13442  19345  13250   2357   -707   -929       C  
ATOM    988  OE1 GLU A 130     -33.203  38.128   5.923  1.00115.84           O  
ANISOU  988  OE1 GLU A 130    12698  18857  12459   2287   -566   -827       O  
ATOM    989  OE2 GLU A 130     -31.905  39.300   7.286  1.00110.05           O1-
ANISOU  989  OE2 GLU A 130    12031  18019  11762   2508   -791  -1056       O1-
ATOM    990  N   LYS A 131     -28.516  38.028   3.558  1.00 89.68           N  
ANISOU  990  N   LYS A 131     9715  14516   9841   1850   -720   -562       N  
ATOM    991  CA  LYS A 131     -27.098  38.170   3.982  1.00 86.55           C  
ANISOU  991  CA  LYS A 131     9386  13956   9542   1844   -807   -572       C  
ATOM    992  C   LYS A 131     -26.354  38.764   2.809  1.00 84.43           C  
ANISOU  992  C   LYS A 131     9168  13412   9498   1761   -883   -522       C  
ATOM    993  O   LYS A 131     -25.626  39.734   2.935  1.00 83.64           O  
ANISOU  993  O   LYS A 131     9104  13146   9528   1827  -1038   -602       O  
ATOM    994  CB  LYS A 131     -26.454  36.839   4.425  1.00 79.39           C  
ANISOU  994  CB  LYS A 131     8496  13107   8559   1730   -691   -447       C  
ATOM    995  N   LEU A 132     -26.593  38.191   1.642  1.00 91.22           N  
ANISOU  995  N   LEU A 132    10025  14232  10401   1619   -780   -386       N  
ATOM    996  CA  LEU A 132     -26.072  38.741   0.409  1.00100.18           C  
ANISOU  996  CA  LEU A 132    11191  15143  11729   1542   -837   -324       C  
ATOM    997  C   LEU A 132     -26.430  40.235   0.299  1.00 98.92           C  
ANISOU  997  C   LEU A 132    11022  14895  11666   1670  -1002   -458       C  
ATOM    998  O   LEU A 132     -25.550  41.034   0.049  1.00 93.00           O  
ANISOU  998  O   LEU A 132    10307  13944  11084   1673  -1134   -468       O  
ATOM    999  CB  LEU A 132     -26.591  37.925  -0.786  1.00112.33           C  
ANISOU  999  CB  LEU A 132    12713  16703  13262   1401   -697   -182       C  
ATOM   1000  CG  LEU A 132     -25.947  37.958  -2.176  1.00120.00           C  
ANISOU 1000  CG  LEU A 132    13712  17485  14395   1277   -694    -59       C  
ATOM   1001  CD1 LEU A 132     -26.334  39.210  -2.962  1.00131.44           C  
ANISOU 1001  CD1 LEU A 132    15148  18823  15969   1325   -802   -106       C  
ATOM   1002  CD2 LEU A 132     -24.442  37.786  -2.071  1.00121.43           C  
ANISOU 1002  CD2 LEU A 132    13942  17521  14674   1217   -733      1       C  
ATOM   1003  N   GLN A 133     -27.686  40.623   0.532  1.00101.70           N  
ANISOU 1003  N   GLN A 133    11325  15398  11919   1779  -1005   -562       N  
ATOM   1004  CA  GLN A 133     -28.074  42.051   0.463  1.00101.92           C  
ANISOU 1004  CA  GLN A 133    11345  15343  12037   1915  -1176   -704       C  
ATOM   1005  C   GLN A 133     -27.352  42.979   1.453  1.00101.44           C  
ANISOU 1005  C   GLN A 133    11313  15192  12036   2055  -1364   -850       C  
ATOM   1006  O   GLN A 133     -26.944  44.066   1.053  1.00104.30           O  
ANISOU 1006  O   GLN A 133    11699  15352  12577   2088  -1532   -894       O  
ATOM   1007  CB  GLN A 133     -29.593  42.236   0.598  1.00104.29           C  
ANISOU 1007  CB  GLN A 133    11580  15844  12199   2019  -1140   -797       C  
ATOM   1008  CG  GLN A 133     -30.360  41.463  -0.448  1.00108.61           C  
ANISOU 1008  CG  GLN A 133    12098  16458  12710   1887   -980   -662       C  
ATOM   1009  CD  GLN A 133     -31.626  42.138  -0.903  1.00110.64           C  
ANISOU 1009  CD  GLN A 133    12306  16780  12948   1967  -1006   -739       C  
ATOM   1010  NE2 GLN A 133     -32.647  42.126  -0.053  1.00107.89           N  
ANISOU 1010  NE2 GLN A 133    11899  16668  12425   2095   -981   -847       N  
ATOM   1011  OE1 GLN A 133     -31.695  42.646  -2.020  1.00115.20           O  
ANISOU 1011  OE1 GLN A 133    12896  17209  13664   1912  -1046   -695       O  
ATOM   1012  N   ASP A 134     -27.191  42.568   2.718  1.00101.77           N  
ANISOU 1012  N   ASP A 134    11351  15378  11935   2137  -1348   -922       N  
ATOM   1013  CA  ASP A 134     -26.548  43.434   3.739  1.00105.44           C  
ANISOU 1013  CA  ASP A 134    11845  15773  12444   2289  -1534  -1079       C  
ATOM   1014  C   ASP A 134     -25.153  43.858   3.261  1.00106.98           C  
ANISOU 1014  C   ASP A 134    12101  15679  12868   2200  -1650  -1009       C  
ATOM   1015  O   ASP A 134     -24.814  45.044   3.279  1.00106.00           O  
ANISOU 1015  O   ASP A 134    11996  15381  12896   2287  -1854  -1107       O  
ATOM   1016  CB  ASP A 134     -26.424  42.754   5.129  1.00103.67           C  
ANISOU 1016  CB  ASP A 134    11610  15750  12028   2368  -1479  -1136       C  
ATOM   1017  CG  ASP A 134     -27.723  42.076   5.609  1.00110.21           C  
ANISOU 1017  CG  ASP A 134    12365  16897  12612   2422  -1330  -1154       C  
ATOM   1018  OD1 ASP A 134     -28.860  42.550   5.297  1.00 96.27           O  
ANISOU 1018  OD1 ASP A 134    10550  15224  10803   2497  -1336  -1221       O  
ATOM   1019  OD2 ASP A 134     -27.580  41.045   6.323  1.00110.14           O1-
ANISOU 1019  OD2 ASP A 134    12343  17050  12455   2385  -1209  -1092       O1-
ATOM   1020  N   ILE A 135     -24.372  42.864   2.817  1.00110.07           N  
ANISOU 1020  N   ILE A 135    12516  16024  13282   2026  -1522   -834       N  
ATOM   1021  CA  ILE A 135     -22.957  43.026   2.433  1.00107.10           C  
ANISOU 1021  CA  ILE A 135    12187  15410  13093   1926  -1598   -741       C  
ATOM   1022  C   ILE A 135     -22.716  44.063   1.324  1.00114.25           C  
ANISOU 1022  C   ILE A 135    13097  16088  14223   1885  -1729   -699       C  
ATOM   1023  O   ILE A 135     -21.786  44.863   1.426  1.00108.35           O  
ANISOU 1023  O   ILE A 135    12376  15145  13644   1903  -1901   -720       O  
ATOM   1024  CB  ILE A 135     -22.343  41.671   2.005  1.00103.45           C  
ANISOU 1024  CB  ILE A 135    11739  14971  12594   1747  -1415   -555       C  
ATOM   1025  CG1 ILE A 135     -22.341  40.693   3.183  1.00105.72           C  
ANISOU 1025  CG1 ILE A 135    12027  15448  12690   1779  -1315   -583       C  
ATOM   1026  CG2 ILE A 135     -20.911  41.843   1.500  1.00104.05           C  
ANISOU 1026  CG2 ILE A 135    11854  14818  12862   1643  -1485   -449       C  
ATOM   1027  CD1 ILE A 135     -22.012  39.260   2.814  1.00100.61           C  
ANISOU 1027  CD1 ILE A 135    11389  14857  11979   1616  -1130   -414       C  
ATOM   1028  N   GLN A 136     -23.536  44.048   0.273  1.00123.07           N  
ANISOU 1028  N   GLN A 136    14185  17228  15346   1825  -1655   -633       N  
ATOM   1029  CA  GLN A 136     -23.384  45.014  -0.823  1.00133.92           C  
ANISOU 1029  CA  GLN A 136    15556  18402  16925   1782  -1773   -580       C  
ATOM   1030  C   GLN A 136     -23.864  46.359  -0.344  1.00135.53           C  
ANISOU 1030  C   GLN A 136    15754  18545  17193   1954  -1986   -764       C  
ATOM   1031  O   GLN A 136     -23.195  47.366  -0.563  1.00143.50           O  
ANISOU 1031  O   GLN A 136    16779  19339  18402   1964  -2178   -770       O  
ATOM   1032  CB  GLN A 136     -24.174  44.644  -2.086  1.00144.88           C  
ANISOU 1032  CB  GLN A 136    16913  19837  18295   1680  -1639   -466       C  
ATOM   1033  CG  GLN A 136     -23.688  43.399  -2.801  1.00157.05           C  
ANISOU 1033  CG  GLN A 136    18457  21443  19768   1518  -1433   -293       C  
ATOM   1034  CD  GLN A 136     -24.558  43.069  -3.981  1.00168.86           C  
ANISOU 1034  CD  GLN A 136    19940  23177  21041   1538  -1269   -325       C  
ATOM   1035  NE2 GLN A 136     -24.006  42.325  -4.953  1.00164.68           N  
ANISOU 1035  NE2 GLN A 136    19433  22699  20437   1490  -1187   -279       N  
ATOM   1036  OE1 GLN A 136     -25.733  43.451  -4.007  1.00178.79           O  
ANISOU 1036  OE1 GLN A 136    21161  24574  22194   1596  -1222   -388       O  
ATOM   1037  N   GLN A 137     -25.015  46.368   0.330  1.00135.23           N  
ANISOU 1037  N   GLN A 137    15691  18703  16986   2093  -1960   -913       N  
ATOM   1038  CA  GLN A 137     -25.599  47.610   0.844  1.00132.93           C  
ANISOU 1038  CA  GLN A 137    15391  18385  16730   2284  -2162  -1113       C  
ATOM   1039  C   GLN A 137     -24.600  48.368   1.718  1.00128.83           C  
ANISOU 1039  C   GLN A 137    14911  17712  16325   2380  -2378  -1220       C  
ATOM   1040  O   GLN A 137     -24.715  49.583   1.844  1.00127.67           O  
ANISOU 1040  O   GLN A 137    14769  17436  16301   2503  -2602  -1350       O  
ATOM   1041  CB  GLN A 137     -26.906  47.355   1.621  1.00127.51           C  
ANISOU 1041  CB  GLN A 137    14663  17977  15808   2432  -2084  -1260       C  
ATOM   1042  N   ARG A 138     -23.621  47.663   2.299  1.00125.94           N  
ANISOU 1042  N   ARG A 138    14573  17351  15927   2326  -2321  -1165       N  
ATOM   1043  CA  ARG A 138     -22.614  48.289   3.174  1.00126.15           C  
ANISOU 1043  CA  ARG A 138    14637  17236  16057   2413  -2519  -1261       C  
ATOM   1044  C   ARG A 138     -21.159  48.189   2.673  1.00126.51           C  
ANISOU 1044  C   ARG A 138    14714  17060  16292   2250  -2552  -1091       C  
ATOM   1045  O   ARG A 138     -20.233  48.570   3.396  1.00124.47           O  
ANISOU 1045  O   ARG A 138    14486  16685  16118   2302  -2700  -1150       O  
ATOM   1046  CB  ARG A 138     -22.723  47.709   4.599  1.00122.08           C  
ANISOU 1046  CB  ARG A 138    14124  16933  15325   2540  -2465  -1390       C  
ATOM   1047  CG  ARG A 138     -22.135  46.315   4.772  1.00123.24           C  
ANISOU 1047  CG  ARG A 138    14281  17184  15358   2403  -2253  -1245       C  
ATOM   1048  CD  ARG A 138     -22.640  45.616   6.026  1.00123.03           C  
ANISOU 1048  CD  ARG A 138    14237  17431  15076   2519  -2154  -1349       C  
ATOM   1049  NE  ARG A 138     -21.790  44.472   6.405  1.00120.81           N  
ANISOU 1049  NE  ARG A 138    13979  17196  14726   2408  -2018  -1232       N  
ATOM   1050  CZ  ARG A 138     -22.099  43.180   6.245  1.00119.35           C  
ANISOU 1050  CZ  ARG A 138    13774  17180  14391   2291  -1789  -1102       C  
ATOM   1051  NH1 ARG A 138     -21.245  42.240   6.640  1.00113.79           N1+
ANISOU 1051  NH1 ARG A 138    13097  16492  13645   2203  -1700  -1010       N1+
ATOM   1052  NH2 ARG A 138     -23.257  42.810   5.705  1.00122.35           N  
ANISOU 1052  NH2 ARG A 138    14108  17709  14667   2263  -1657  -1063       N  
ATOM   1053  N   GLY A 139     -20.951  47.680   1.457  1.00127.14           N  
ANISOU 1053  N   GLY A 139    14781  17091  16434   2063  -2419   -885       N  
ATOM   1054  CA  GLY A 139     -19.595  47.532   0.889  1.00129.51           C  
ANISOU 1054  CA  GLY A 139    15097  17209  16899   1906  -2433   -708       C  
ATOM   1055  C   GLY A 139     -18.617  46.610   1.618  1.00128.94           C  
ANISOU 1055  C   GLY A 139    15054  17180  16757   1860  -2348   -666       C  
ATOM   1056  O   GLY A 139     -17.404  46.823   1.559  1.00126.03           O  
ANISOU 1056  O   GLY A 139    14702  16641  16542   1794  -2440   -587       O  
ATOM   1057  N   GLY A 140     -19.120  45.592   2.305  1.00128.01           N  
ANISOU 1057  N   GLY A 140    14937  17289  16410   1890  -2175   -708       N  
ATOM   1058  CA  GLY A 140     -18.263  44.692   3.056  1.00118.20           C  
ANISOU 1058  CA  GLY A 140    13722  16101  15085   1854  -2093   -676       C  
ATOM   1059  C   GLY A 140     -17.245  43.972   2.201  1.00115.37           C  
ANISOU 1059  C   GLY A 140    13371  15652  14811   1662  -1989   -464       C  
ATOM   1060  O   GLY A 140     -17.401  43.868   1.001  1.00114.52           O  
ANISOU 1060  O   GLY A 140    13240  15509  14761   1547  -1912   -329       O  
ATOM   1061  N   GLU A 141     -16.186  43.486   2.828  1.00116.14           N  
ANISOU 1061  N   GLU A 141    13498  15714  14914   1636  -1993   -439       N  
ATOM   1062  CA  GLU A 141     -15.157  42.705   2.160  1.00111.83           C  
ANISOU 1062  CA  GLU A 141    12958  15105  14427   1470  -1891   -252       C  
ATOM   1063  C   GLU A 141     -15.578  41.232   2.061  1.00108.66           C  
ANISOU 1063  C   GLU A 141    12556  14897  13831   1393  -1650   -177       C  
ATOM   1064  O   GLU A 141     -15.186  40.562   1.111  1.00110.48           O  
ANISOU 1064  O   GLU A 141    12778  15107  14090   1255  -1537    -19       O  
ATOM   1065  CB  GLU A 141     -13.800  42.836   2.886  1.00105.71           C  
ANISOU 1065  CB  GLU A 141    12213  14205  13745   1474  -2002   -257       C  
ATOM   1066  N   GLU A 142     -16.370  40.751   3.010  1.00103.95           N  
ANISOU 1066  N   GLU A 142    11963  14492  13041   1483  -1580   -286       N  
ATOM   1067  CA  GLU A 142     -16.774  39.340   3.109  1.00 98.54           C  
ANISOU 1067  CA  GLU A 142    11277  13984  12176   1409  -1372   -211       C  
ATOM   1068  C   GLU A 142     -17.381  38.695   1.858  1.00 94.02           C  
ANISOU 1068  C   GLU A 142    10677  13480  11566   1308  -1224   -101       C  
ATOM   1069  O   GLU A 142     -17.770  39.389   0.936  1.00 94.13           O  
ANISOU 1069  O   GLU A 142    10665  13444  11654   1318  -1269   -106       O  
ATOM   1070  CB  GLU A 142     -17.757  39.186   4.256  1.00 95.67           C  
ANISOU 1070  CB  GLU A 142    10912  13825  11613   1528  -1337   -338       C  
ATOM   1071  CG  GLU A 142     -18.339  37.801   4.394  1.00 98.99           C  
ANISOU 1071  CG  GLU A 142    11288  14420  11901   1602  -1282   -409       C  
ATOM   1072  CD  GLU A 142     -19.503  37.772   5.343  1.00 95.09           C  
ANISOU 1072  CD  GLU A 142    10775  14177  11178   1627  -1144   -422       C  
ATOM   1073  OE1 GLU A 142     -19.814  36.704   5.879  1.00 90.13           O  
ANISOU 1073  OE1 GLU A 142    10165  13588  10491   1538  -1044   -329       O  
ATOM   1074  OE2 GLU A 142     -20.110  38.826   5.549  1.00 97.44           O1-
ANISOU 1074  OE2 GLU A 142    11030  14638  11352   1733  -1135   -518       O1-
ATOM   1075  N   ARG A 143     -17.471  37.366   1.851  1.00 85.52           N  
ANISOU 1075  N   ARG A 143     9606  12510  10376   1215  -1060     -6       N  
ATOM   1076  CA  ARG A 143     -18.007  36.635   0.692  1.00 82.62           C  
ANISOU 1076  CA  ARG A 143     9218  12188   9982   1103   -921    114       C  
ATOM   1077  C   ARG A 143     -18.688  35.367   1.057  1.00 76.64           C  
ANISOU 1077  C   ARG A 143     8455  11618   9045   1071   -770    142       C  
ATOM   1078  O   ARG A 143     -18.254  34.674   2.002  1.00 78.69           O  
ANISOU 1078  O   ARG A 143     8736  11942   9220   1075   -741    134       O  
ATOM   1079  CB  ARG A 143     -16.896  36.173  -0.234  1.00 84.06           C  
ANISOU 1079  CB  ARG A 143     9416  12247  10273    974   -886    261       C  
ATOM   1080  CG  ARG A 143     -16.047  37.267  -0.819  1.00 81.23           C  
ANISOU 1080  CG  ARG A 143     9053  11697  10111    966  -1021    290       C  
ATOM   1081  CD  ARG A 143     -14.893  36.638  -1.543  1.00 73.69           C  
ANISOU 1081  CD  ARG A 143     8106  10664   9228    848   -970    436       C  
ATOM   1082  NE  ARG A 143     -14.116  37.652  -2.218  1.00 71.28           N  
ANISOU 1082  NE  ARG A 143     7781  10191   9110    825  -1090    494       N  
ATOM   1083  CZ  ARG A 143     -14.365  38.096  -3.435  1.00 72.64           C  
ANISOU 1083  CZ  ARG A 143     7917  10318   9365    779  -1091    575       C  
ATOM   1084  NH1 ARG A 143     -15.392  37.606  -4.154  1.00 76.05           N1+
ANISOU 1084  NH1 ARG A 143     8333  10854   9707    753   -975    599       N1+
ATOM   1085  NH2 ARG A 143     -13.569  39.024  -3.944  1.00 71.73           N  
ANISOU 1085  NH2 ARG A 143     7777  10051   9424    754  -1211    642       N  
ATOM   1086  N   LEU A 144     -19.688  35.030   0.246  1.00 63.80           N  
ANISOU 1086  N   LEU A 144     6799  10068   7372   1027   -678    189       N  
ATOM   1087  CA  LEU A 144     -20.464  33.820   0.434  1.00 69.34           C  
ANISOU 1087  CA  LEU A 144     7486  10942   7917    982   -540    234       C  
ATOM   1088  C   LEU A 144     -20.554  32.968  -0.831  1.00 68.83           C  
ANISOU 1088  C   LEU A 144     7420  10855   7876    853   -435    367       C  
ATOM   1089  O   LEU A 144     -20.473  33.484  -1.951  1.00 61.50           O  
ANISOU 1089  O   LEU A 144     6485   9823   7058    821   -458    407       O  
ATOM   1090  CB  LEU A 144     -21.887  34.182   0.844  1.00 70.76           C  
ANISOU 1090  CB  LEU A 144     7617  11282   7983   1075   -529    143       C  
ATOM   1091  CG  LEU A 144     -21.975  35.144   2.038  1.00 74.28           C  
ANISOU 1091  CG  LEU A 144     8057  11771   8395   1232   -645    -13       C  
ATOM   1092  CD1 LEU A 144     -23.415  35.630   2.169  1.00 76.39           C  
ANISOU 1092  CD1 LEU A 144     8269  12188   8567   1328   -640   -101       C  
ATOM   1093  CD2 LEU A 144     -21.471  34.502   3.311  1.00 67.21           C  
ANISOU 1093  CD2 LEU A 144     7177  10964   7393   1258   -629    -32       C  
ATOM   1094  N   TYR A 145     -20.832  31.696  -0.641  1.00 63.43           N  
ANISOU 1094  N   TYR A 145     6737  10279   7082    786   -328    433       N  
ATOM   1095  CA  TYR A 145     -21.022  30.794  -1.735  1.00 64.20           C  
ANISOU 1095  CA  TYR A 145     6834  10369   7188    676   -237    545       C  
ATOM   1096  C   TYR A 145     -22.027  29.752  -1.345  1.00 65.60           C  
ANISOU 1096  C   TYR A 145     6986  10717   7221    648   -145    572       C  
ATOM   1097  O   TYR A 145     -21.774  28.972  -0.473  1.00 64.60           O  
ANISOU 1097  O   TYR A 145     6868  10663   7011    637   -120    587       O  
ATOM   1098  CB  TYR A 145     -19.712  30.115  -2.028  1.00 60.26           C  
ANISOU 1098  CB  TYR A 145     6378   9758   6757    594   -228    631       C  
ATOM   1099  CG  TYR A 145     -19.476  29.731  -3.448  1.00 57.00           C  
ANISOU 1099  CG  TYR A 145     5968   9270   6418    512   -186    726       C  
ATOM   1100  CD1 TYR A 145     -20.514  29.450  -4.295  1.00 62.26           C  
ANISOU 1100  CD1 TYR A 145     6606   9995   7052    483   -126    756       C  
ATOM   1101  CD2 TYR A 145     -18.205  29.627  -3.927  1.00 55.10           C  
ANISOU 1101  CD2 TYR A 145     5753   8913   6266    466   -205    788       C  
ATOM   1102  CE1 TYR A 145     -20.284  29.088  -5.595  1.00 62.56           C  
ANISOU 1102  CE1 TYR A 145     6646   9976   7149    420    -92    835       C  
ATOM   1103  CE2 TYR A 145     -17.965  29.271  -5.213  1.00 61.31           C  
ANISOU 1103  CE2 TYR A 145     6536   9654   7105    405   -166    872       C  
ATOM   1104  CZ  TYR A 145     -19.005  29.001  -6.045  1.00 62.72           C  
ANISOU 1104  CZ  TYR A 145     6689   9891   7250    384   -111    893       C  
ATOM   1105  OH  TYR A 145     -18.745  28.645  -7.328  1.00 56.03           O  
ANISOU 1105  OH  TYR A 145     5834   9009   6443    336    -76    969       O  
ATOM   1106  N   LEU A 146     -23.165  29.721  -2.005  1.00 62.27           N  
ANISOU 1106  N   LEU A 146     6526  10362   6770    636    -99    586       N  
ATOM   1107  CA  LEU A 146     -24.172  28.706  -1.708  1.00 62.93           C  
ANISOU 1107  CA  LEU A 146     6576  10604   6728    595    -15    632       C  
ATOM   1108  C   LEU A 146     -23.969  27.501  -2.589  1.00 59.62           C  
ANISOU 1108  C   LEU A 146     6179  10139   6334    474     45    748       C  
ATOM   1109  O   LEU A 146     -23.839  27.629  -3.840  1.00 55.24           O  
ANISOU 1109  O   LEU A 146     5635   9484   5867    438     47    781       O  
ATOM   1110  CB  LEU A 146     -25.583  29.259  -1.938  1.00 66.33           C  
ANISOU 1110  CB  LEU A 146     6949  11143   7110    645      0    587       C  
ATOM   1111  CG  LEU A 146     -26.751  28.281  -1.756  1.00 69.76           C  
ANISOU 1111  CG  LEU A 146     7332  11747   7424    597     83    648       C  
ATOM   1112  CD1 LEU A 146     -28.017  29.058  -1.375  1.00 69.55           C  
ANISOU 1112  CD1 LEU A 146     7239  11870   7317    694     79    566       C  
ATOM   1113  CD2 LEU A 146     -27.040  27.462  -3.005  1.00 72.93           C  
ANISOU 1113  CD2 LEU A 146     7741  12097   7872    488    136    747       C  
ATOM   1114  N   GLN A 147     -24.016  26.332  -1.969  1.00 53.71           N  
ANISOU 1114  N   GLN A 147     5432   9470   5504    417     88    809       N  
ATOM   1115  CA  GLN A 147     -23.754  25.097  -2.675  1.00 54.28           C  
ANISOU 1115  CA  GLN A 147     5530   9492   5601    310    126    910       C  
ATOM   1116  C   GLN A 147     -24.572  24.079  -1.977  1.00 55.81           C  
ANISOU 1116  C   GLN A 147     5689   9829   5684    263    171    969       C  
ATOM   1117  O   GLN A 147     -24.288  23.709  -0.843  1.00 57.52           O  
ANISOU 1117  O   GLN A 147     5907  10113   5833    269    168    977       O  
ATOM   1118  CB  GLN A 147     -22.278  24.707  -2.582  1.00 56.69           C  
ANISOU 1118  CB  GLN A 147     5896   9677   5967    281     98    934       C  
ATOM   1119  CG  GLN A 147     -21.306  25.816  -2.913  1.00 57.03           C  
ANISOU 1119  CG  GLN A 147     5963   9592   6113    335     41    880       C  
ATOM   1120  CD  GLN A 147     -19.824  25.425  -2.747  1.00 59.78           C  
ANISOU 1120  CD  GLN A 147     6362   9834   6515    308     13    907       C  
ATOM   1121  NE2 GLN A 147     -18.967  26.306  -3.163  1.00 58.00           N  
ANISOU 1121  NE2 GLN A 147     6149   9497   6389    340    -36    883       N  
ATOM   1122  OE1 GLN A 147     -19.473  24.371  -2.235  1.00 63.12           O  
ANISOU 1122  OE1 GLN A 147     6809  10278   6894    260     31    952       O  
ATOM   1123  N   GLN A 148     -25.625  23.657  -2.637  1.00 57.61           N  
ANISOU 1123  N   GLN A 148     5882  10111   5895    218    209   1016       N  
ATOM   1124  CA  GLN A 148     -26.588  22.800  -2.038  1.00 59.16           C  
ANISOU 1124  CA  GLN A 148     6028  10458   5992    170    246   1083       C  
ATOM   1125  C   GLN A 148     -27.147  21.862  -3.072  1.00 56.98           C  
ANISOU 1125  C   GLN A 148     5748  10150   5750     76    267   1167       C  
ATOM   1126  O   GLN A 148     -27.566  22.310  -4.127  1.00 50.97           O  
ANISOU 1126  O   GLN A 148     4982   9342   5041     87    272   1144       O  
ATOM   1127  CB  GLN A 148     -27.729  23.661  -1.515  1.00 66.43           C  
ANISOU 1127  CB  GLN A 148     6875  11537   6826    252    262   1023       C  
ATOM   1128  CG  GLN A 148     -28.950  22.882  -1.046  1.00 65.96           C  
ANISOU 1128  CG  GLN A 148     6740  11660   6660    204    308   1105       C  
ATOM   1129  CD  GLN A 148     -28.627  22.054   0.153  1.00 67.56           C  
ANISOU 1129  CD  GLN A 148     6933  11953   6783    170    312   1171       C  
ATOM   1130  NE2 GLN A 148     -29.032  20.770   0.125  1.00 70.85           N  
ANISOU 1130  NE2 GLN A 148     7329  12410   7181     56    330   1301       N  
ATOM   1131  OE1 GLN A 148     -28.001  22.547   1.100  1.00 61.56           O  
ANISOU 1131  OE1 GLN A 148     6185  11222   5981    244    291   1109       O  
ATOM   1132  N   THR A 149     -27.180  20.581  -2.723  1.00 59.24           N  
ANISOU 1132  N   THR A 149     6034  10464   6008    -11    270   1265       N  
ATOM   1133  CA  THR A 149     -27.766  19.523  -3.518  1.00 63.67           C  
ANISOU 1133  CA  THR A 149     6589  11004   6598   -105    272   1353       C  
ATOM   1134  C   THR A 149     -29.246  19.840  -3.688  1.00 65.78           C  
ANISOU 1134  C   THR A 149     6777  11400   6814    -98    306   1360       C  
ATOM   1135  O   THR A 149     -29.934  20.000  -2.689  1.00 67.55           O  
ANISOU 1135  O   THR A 149     6935  11790   6939    -76    330   1373       O  
ATOM   1136  CB  THR A 149     -27.634  18.154  -2.776  1.00 66.00           C  
ANISOU 1136  CB  THR A 149     6885  11330   6860   -198    255   1462       C  
ATOM   1137  CG2 THR A 149     -28.074  16.964  -3.621  1.00 74.72           C  
ANISOU 1137  CG2 THR A 149     7994  12376   8018   -299    230   1552       C  
ATOM   1138  OG1 THR A 149     -26.278  17.936  -2.424  1.00 71.12           O  
ANISOU 1138  OG1 THR A 149     7601  11879   7542   -194    225   1447       O  
ATOM   1139  N   LEU A 150     -29.710  19.973  -4.937  1.00 65.58           N  
ANISOU 1139  N   LEU A 150     6755  11310   6851   -107    308   1349       N  
ATOM   1140  CA  LEU A 150     -31.131  19.955  -5.269  1.00 66.95           C  
ANISOU 1140  CA  LEU A 150     6858  11589   6991   -126    333   1379       C  
ATOM   1141  C   LEU A 150     -31.784  18.677  -4.706  1.00 71.40           C  
ANISOU 1141  C   LEU A 150     7374  12246   7507   -227    330   1507       C  
ATOM   1142  O   LEU A 150     -31.187  17.597  -4.747  1.00 73.56           O  
ANISOU 1142  O   LEU A 150     7690  12433   7823   -304    293   1576       O  
ATOM   1143  CB  LEU A 150     -31.339  20.030  -6.788  1.00 69.89           C  
ANISOU 1143  CB  LEU A 150     7255  11849   7450   -135    324   1361       C  
ATOM   1144  CG  LEU A 150     -30.902  21.378  -7.436  1.00 80.53           C  
ANISOU 1144  CG  LEU A 150     8630  13121   8846    -41    325   1254       C  
ATOM   1145  CD1 LEU A 150     -30.820  21.336  -8.969  1.00 71.64           C  
ANISOU 1145  CD1 LEU A 150     7537  11874   7806    -52    313   1248       C  
ATOM   1146  CD2 LEU A 150     -31.766  22.564  -6.984  1.00 82.13           C  
ANISOU 1146  CD2 LEU A 150     8771  13446   8989     41    349   1184       C  
ATOM   1147  N   ASN A 151     -32.972  18.796  -4.121  1.00 73.05           N  
ANISOU 1147  N   ASN A 151     7490  12636   7628   -227    363   1543       N  
ATOM   1148  CA  ASN A 151     -33.695  17.597  -3.656  1.00 79.28           C  
ANISOU 1148  CA  ASN A 151     8219  13524   8380   -335    356   1687       C  
ATOM   1149  C   ASN A 151     -35.197  17.806  -3.598  1.00 83.16           C  
ANISOU 1149  C   ASN A 151     8601  14190   8804   -337    392   1726       C  
ATOM   1150  O   ASN A 151     -35.686  18.865  -3.988  1.00 73.74           O  
ANISOU 1150  O   ASN A 151     7387  13032   7596   -251    421   1631       O  
ATOM   1151  CB  ASN A 151     -33.152  17.142  -2.295  1.00 81.14           C  
ANISOU 1151  CB  ASN A 151     8443  13842   8543   -353    353   1745       C  
ATOM   1152  CG  ASN A 151     -33.191  18.250  -1.241  1.00 80.58           C  
ANISOU 1152  CG  ASN A 151     8328  13927   8359   -235    396   1662       C  
ATOM   1153  ND2 ASN A 151     -32.074  18.413  -0.530  1.00 71.32           N  
ANISOU 1153  ND2 ASN A 151     7210  12713   7174   -194    382   1618       N  
ATOM   1154  OD1 ASN A 151     -34.220  18.936  -1.051  1.00 80.42           O  
ANISOU 1154  OD1 ASN A 151     8226  14066   8262   -176    434   1633       O  
ATOM   1155  N   ASP A 152     -35.922  16.805  -3.087  1.00 93.32           N  
ANISOU 1155  N   ASP A 152     9815  15591  10051   -436    386   1871       N  
ATOM   1156  CA  ASP A 152     -37.415  16.789  -3.124  1.00 95.23           C  
ANISOU 1156  CA  ASP A 152     9942  16000  10239   -462    414   1938       C  
ATOM   1157  C   ASP A 152     -38.156  17.950  -2.421  1.00 83.37           C  
ANISOU 1157  C   ASP A 152     8351  14717   8608   -346    479   1867       C  
ATOM   1158  O   ASP A 152     -39.311  18.175  -2.718  1.00 86.53           O  
ANISOU 1158  O   ASP A 152     8670  15227   8979   -342    503   1884       O  
ATOM   1159  CB  ASP A 152     -37.986  15.430  -2.635  1.00100.62           C  
ANISOU 1159  CB  ASP A 152    10554  16765  10911   -603    383   2132       C  
ATOM   1160  CG  ASP A 152     -37.319  14.912  -1.337  1.00104.13           C  
ANISOU 1160  CG  ASP A 152    10989  17285  11288   -630    377   2209       C  
ATOM   1161  OD1 ASP A 152     -37.003  15.710  -0.430  1.00 97.61           O  
ANISOU 1161  OD1 ASP A 152    10148  16579  10359   -529    423   2137       O  
ATOM   1162  OD2 ASP A 152     -37.120  13.686  -1.229  1.00109.76           O1-
ANISOU 1162  OD2 ASP A 152    11712  17935  12055   -753    318   2343       O1-
ATOM   1163  N   THR A 153     -37.488  18.712  -1.555  1.00 81.75           N  
ANISOU 1163  N   THR A 153     8162  14566   8331   -242    498   1776       N  
ATOM   1164  CA  THR A 153     -38.142  19.796  -0.789  1.00 82.53           C  
ANISOU 1164  CA  THR A 153     8177  14881   8299   -114    545   1695       C  
ATOM   1165  C   THR A 153     -38.436  21.041  -1.636  1.00 83.00           C  
ANISOU 1165  C   THR A 153     8258  14881   8397     -7    550   1543       C  
ATOM   1166  O   THR A 153     -39.003  22.023  -1.172  1.00 81.29           O  
ANISOU 1166  O   THR A 153     7980  14817   8088    110    574   1454       O  
ATOM   1167  CB  THR A 153     -37.261  20.276   0.384  1.00 86.44           C  
ANISOU 1167  CB  THR A 153     8692  15435   8713    -21    546   1626       C  
ATOM   1168  CG2 THR A 153     -36.695  19.099   1.196  1.00 85.48           C  
ANISOU 1168  CG2 THR A 153     8574  15334   8569   -121    532   1763       C  
ATOM   1169  OG1 THR A 153     -36.192  21.096  -0.119  1.00 90.07           O  
ANISOU 1169  OG1 THR A 153     9266  15693   9263     54    515   1480       O  
ATOM   1170  N   VAL A 154     -37.975  21.041  -2.874  1.00 80.66           N  
ANISOU 1170  N   VAL A 154     8048  14363   8234    -43    521   1511       N  
ATOM   1171  CA  VAL A 154     -38.001  22.276  -3.645  1.00 79.95           C  
ANISOU 1171  CA  VAL A 154     8001  14179   8197     57    514   1366       C  
ATOM   1172  C   VAL A 154     -39.350  22.530  -4.223  1.00 79.94           C  
ANISOU 1172  C   VAL A 154     7921  14273   8177     64    538   1368       C  
ATOM   1173  O   VAL A 154     -40.092  21.619  -4.502  1.00 77.47           O  
ANISOU 1173  O   VAL A 154     7558  14004   7870    -39    545   1489       O  
ATOM   1174  CB  VAL A 154     -36.983  22.335  -4.805  1.00 78.67           C  
ANISOU 1174  CB  VAL A 154     7961  13749   8178     22    474   1336       C  
ATOM   1175  CG1 VAL A 154     -35.564  22.255  -4.308  1.00 78.39           C  
ANISOU 1175  CG1 VAL A 154     7979  13620   8186    139    455   1189       C  
ATOM   1176  CG2 VAL A 154     -37.272  21.281  -5.840  1.00 72.00           C  
ANISOU 1176  CG2 VAL A 154     7130  12804   7423    -66    463   1397       C  
ATOM   1177  N   GLY A 155     -39.633  23.796  -4.431  1.00 75.02           N  
ANISOU 1177  N   GLY A 155     7288  13675   7541    187    540   1236       N  
ATOM   1178  CA  GLY A 155     -40.954  24.215  -4.857  1.00 78.71           C  
ANISOU 1178  CA  GLY A 155     7675  14254   7976    216    562   1221       C  
ATOM   1179  C   GLY A 155     -41.357  23.832  -6.267  1.00 77.76           C  
ANISOU 1179  C   GLY A 155     7581  14000   7963    135    553   1261       C  
ATOM   1180  O   GLY A 155     -40.497  23.668  -7.148  1.00 71.16           O  
ANISOU 1180  O   GLY A 155     6843  12953   7240     99    523   1249       O  
ATOM   1181  N   ARG A 156     -42.685  23.774  -6.461  1.00 75.02           N  
ANISOU 1181  N   ARG A 156     7140  13790   7572    123    579   1300       N  
ATOM   1182  CA  ARG A 156     -43.381  23.221  -7.644  1.00 75.23           C  
ANISOU 1182  CA  ARG A 156     7162  13743   7677     35    572   1363       C  
ATOM   1183  C   ARG A 156     -42.839  23.712  -8.987  1.00 73.51           C  
ANISOU 1183  C   ARG A 156     7044  13301   7584     55    541   1281       C  
ATOM   1184  O   ARG A 156     -42.781  22.960  -9.964  1.00 73.45           O  
ANISOU 1184  O   ARG A 156     7078  13164   7664    -30    519   1339       O  
ATOM   1185  CB  ARG A 156     -44.924  23.493  -7.568  1.00 75.95           C  
ANISOU 1185  CB  ARG A 156     7129  14037   7691     59    606   1379       C  
ATOM   1186  N   LYS A 157     -42.464  24.966  -9.040  1.00 69.46           N  
ANISOU 1186  N   LYS A 157     6564  12749   7077    173    533   1148       N  
ATOM   1187  CA  LYS A 157     -41.994  25.530 -10.264  1.00 73.66           C  
ANISOU 1187  CA  LYS A 157     7173  13096   7717    196    505   1083       C  
ATOM   1188  C   LYS A 157     -40.565  25.065 -10.548  1.00 71.39           C  
ANISOU 1188  C   LYS A 157     6992  12622   7512    159    476   1093       C  
ATOM   1189  O   LYS A 157     -40.232  24.750 -11.669  1.00 65.35           O  
ANISOU 1189  O   LYS A 157     6285  11707   6836    128    457   1099       O  
ATOM   1190  CB  LYS A 157     -42.090  27.043 -10.179  1.00 85.22           C  
ANISOU 1190  CB  LYS A 157     8621  14587   9168    329    493    949       C  
ATOM   1191  CG  LYS A 157     -42.845  27.691 -11.324  1.00 94.01           C  
ANISOU 1191  CG  LYS A 157     9729  15647  10341    339    486    920       C  
ATOM   1192  CD  LYS A 157     -44.350  27.606 -11.175  1.00 97.66           C  
ANISOU 1192  CD  LYS A 157    10104  16267  10733    431    496    848       C  
ATOM   1193  CE  LYS A 157     -45.044  28.658 -12.026  1.00102.25           C  
ANISOU 1193  CE  LYS A 157    10663  16825  11359    403    501    863       C  
ATOM   1194  NZ  LYS A 157     -46.518  28.710 -11.821  1.00104.04           N1+
ANISOU 1194  NZ  LYS A 157    10799  17213  11515    488    511    799       N1+
ATOM   1195  N   ILE A 158     -39.737  24.979  -9.518  1.00 68.18           N  
ANISOU 1195  N   ILE A 158     6603  12236   7065    164    474   1101       N  
ATOM   1196  CA  ILE A 158     -38.341  24.585  -9.701  1.00 69.61           C  
ANISOU 1196  CA  ILE A 158     6876  12255   7316    130    448   1114       C  
ATOM   1197  C   ILE A 158     -38.319  23.147 -10.180  1.00 68.05           C  
ANISOU 1197  C   ILE A 158     6698  12002   7156      9    441   1227       C  
ATOM   1198  O   ILE A 158     -37.553  22.778 -11.049  1.00 68.89           O  
ANISOU 1198  O   ILE A 158     6874  11954   7344    -21    416   1235       O  
ATOM   1199  CB  ILE A 158     -37.502  24.744  -8.403  1.00 66.13           C  
ANISOU 1199  CB  ILE A 158     6447  11855   6821    169    443   1091       C  
ATOM   1200  CG1 ILE A 158     -37.469  26.196  -7.919  1.00 68.61           C  
ANISOU 1200  CG1 ILE A 158     6749  12210   7108    301    428    965       C  
ATOM   1201  CG2 ILE A 158     -36.053  24.309  -8.599  1.00 68.53           C  
ANISOU 1201  CG2 ILE A 158     6844  11994   7199    132    416   1108       C  
ATOM   1202  CD1 ILE A 158     -37.232  27.246  -8.981  1.00 70.16           C  
ANISOU 1202  CD1 ILE A 158     6987  12268   7399    357    395    885       C  
ATOM   1203  N   VAL A 159     -39.189  22.354  -9.619  1.00 67.19           N  
ANISOU 1203  N   VAL A 159     6517  12024   6986    -53    457   1314       N  
ATOM   1204  CA  VAL A 159     -39.367  20.965 -10.025  1.00 71.79           C  
ANISOU 1204  CA  VAL A 159     7105  12561   7611   -172    433   1428       C  
ATOM   1205  C   VAL A 159     -39.784  20.915 -11.489  1.00 65.73           C  
ANISOU 1205  C   VAL A 159     6360  11688   6923   -187    414   1414       C  
ATOM   1206  O   VAL A 159     -39.394  20.023 -12.198  1.00 65.40           O  
ANISOU 1206  O   VAL A 159     6370  11526   6952   -249    373   1457       O  
ATOM   1207  CB  VAL A 159     -40.467  20.249  -9.146  1.00 77.39           C  
ANISOU 1207  CB  VAL A 159     7708  13457   8238   -240    450   1540       C  
ATOM   1208  CG1 VAL A 159     -40.691  18.790  -9.548  1.00 75.77           C  
ANISOU 1208  CG1 VAL A 159     7504  13191   8093   -371    404   1668       C  
ATOM   1209  CG2 VAL A 159     -40.096  20.294  -7.674  1.00 74.25           C  
ANISOU 1209  CG2 VAL A 159     7279  13188   7745   -218    472   1558       C  
ATOM   1210  N   MET A 160     -40.617  21.838 -11.935  1.00 70.14           N  
ANISOU 1210  N   MET A 160     6878  12301   7469   -125    436   1353       N  
ATOM   1211  CA  MET A 160     -41.035  21.824 -13.349  1.00 72.13           C  
ANISOU 1211  CA  MET A 160     7151  12460   7794   -134    418   1339       C  
ATOM   1212  C   MET A 160     -39.836  22.205 -14.205  1.00 64.80           C  
ANISOU 1212  C   MET A 160     6318  11363   6940    -92    397   1276       C  
ATOM   1213  O   MET A 160     -39.601  21.617 -15.230  1.00 59.87           O  
ANISOU 1213  O   MET A 160     5738  10628   6378   -125    366   1294       O  
ATOM   1214  CB  MET A 160     -42.170  22.806 -13.620  1.00 75.73           C  
ANISOU 1214  CB  MET A 160     7542  13010   8219    -72    445   1283       C  
ATOM   1215  CG  MET A 160     -43.498  22.364 -13.006  1.00 89.57           C  
ANISOU 1215  CG  MET A 160     9188  14942   9902   -117    466   1357       C  
ATOM   1216  SD  MET A 160     -44.354  21.173 -14.049  1.00 97.35           S  
ANISOU 1216  SD  MET A 160    10156  15877  10956   -227    428   1453       S  
ATOM   1217  CE  MET A 160     -44.929  22.314 -15.308  1.00 85.23           C  
ANISOU 1217  CE  MET A 160     8628  14298   9456   -141    437   1348       C  
ATOM   1218  N   ASP A 161     -39.136  23.237 -13.776  1.00 58.88           N  
ANISOU 1218  N   ASP A 161     5590  10603   6177    -14    409   1203       N  
ATOM   1219  CA  ASP A 161     -37.836  23.599 -14.340  1.00 62.15           C  
ANISOU 1219  CA  ASP A 161     6084  10873   6655     19    388   1162       C  
ATOM   1220  C   ASP A 161     -36.876  22.402 -14.455  1.00 53.58           C  
ANISOU 1220  C   ASP A 161     5058   9694   5605    -46    361   1221       C  
ATOM   1221  O   ASP A 161     -36.413  22.096 -15.520  1.00 52.65           O  
ANISOU 1221  O   ASP A 161     4986   9471   5544    -52    338   1222       O  
ATOM   1222  CB  ASP A 161     -37.251  24.752 -13.532  1.00 61.16           C  
ANISOU 1222  CB  ASP A 161     5962  10765   6509    100    393   1090       C  
ATOM   1223  CG  ASP A 161     -37.968  26.073 -13.818  1.00 63.81           C  
ANISOU 1223  CG  ASP A 161     6261  11139   6844    183    395   1013       C  
ATOM   1224  OD1 ASP A 161     -38.943  26.071 -14.605  1.00 55.11           O  
ANISOU 1224  OD1 ASP A 161     5127  10061   5750    174    403   1018       O  
ATOM   1225  OD2 ASP A 161     -37.532  27.120 -13.294  1.00 67.59           O1-
ANISOU 1225  OD2 ASP A 161     6744  11613   7321    259    379    943       O1-
ATOM   1226  N   PHE A 162     -36.712  21.665 -13.375  1.00 55.02           N  
ANISOU 1226  N   PHE A 162     5231   9928   5746    -95    360   1273       N  
ATOM   1227  CA  PHE A 162     -35.787  20.549 -13.290  1.00 56.35           C  
ANISOU 1227  CA  PHE A 162     5453  10011   5943   -154    326   1325       C  
ATOM   1228  C   PHE A 162     -36.176  19.431 -14.237  1.00 50.98           C  
ANISOU 1228  C   PHE A 162     4786   9270   5312   -219    285   1378       C  
ATOM   1229  O   PHE A 162     -35.328  18.755 -14.844  1.00 51.52           O  
ANISOU 1229  O   PHE A 162     4918   9225   5432   -233    244   1383       O  
ATOM   1230  CB  PHE A 162     -35.784  20.033 -11.822  1.00 59.03           C  
ANISOU 1230  CB  PHE A 162     5762  10447   6218   -196    334   1381       C  
ATOM   1231  CG  PHE A 162     -34.886  18.835 -11.554  1.00 58.84           C  
ANISOU 1231  CG  PHE A 162     5790  10344   6222   -263    292   1442       C  
ATOM   1232  CD1 PHE A 162     -33.546  19.010 -11.170  1.00 62.83           C  
ANISOU 1232  CD1 PHE A 162     6355  10779   6738   -232    286   1409       C  
ATOM   1233  CD2 PHE A 162     -35.399  17.526 -11.632  1.00 59.82           C  
ANISOU 1233  CD2 PHE A 162     5899  10463   6364   -359    249   1535       C  
ATOM   1234  CE1 PHE A 162     -32.742  17.891 -10.891  1.00 70.31           C  
ANISOU 1234  CE1 PHE A 162     7348  11656   7708   -291    244   1462       C  
ATOM   1235  CE2 PHE A 162     -34.611  16.396 -11.335  1.00 65.24           C  
ANISOU 1235  CE2 PHE A 162     6633  11073   7081   -421    196   1592       C  
ATOM   1236  CZ  PHE A 162     -33.275  16.582 -10.961  1.00 70.33           C  
ANISOU 1236  CZ  PHE A 162     7339  11653   7730   -383    197   1552       C  
ATOM   1237  N   LEU A 163     -37.455  19.189 -14.301  1.00 51.75           N  
ANISOU 1237  N   LEU A 163     4821   9448   5391   -257    288   1417       N  
ATOM   1238  CA  LEU A 163     -38.003  18.128 -15.138  1.00 53.61           C  
ANISOU 1238  CA  LEU A 163     5059   9631   5678   -321    235   1468       C  
ATOM   1239  C   LEU A 163     -37.849  18.486 -16.606  1.00 50.96           C  
ANISOU 1239  C   LEU A 163     4766   9200   5395   -266    222   1404       C  
ATOM   1240  O   LEU A 163     -37.823  17.584 -17.451  1.00 49.66           O  
ANISOU 1240  O   LEU A 163     4633   8952   5282   -295    163   1422       O  
ATOM   1241  CB  LEU A 163     -39.488  17.926 -14.845  1.00 58.34           C  
ANISOU 1241  CB  LEU A 163     5568  10353   6245   -372    244   1529       C  
ATOM   1242  CG  LEU A 163     -39.910  17.046 -13.658  1.00 65.24           C  
ANISOU 1242  CG  LEU A 163     6384  11323   7080   -463    232   1641       C  
ATOM   1243  CD1 LEU A 163     -41.440  16.937 -13.754  1.00 71.48           C  
ANISOU 1243  CD1 LEU A 163     7080  12225   7853   -506    237   1699       C  
ATOM   1244  CD2 LEU A 163     -39.258  15.660 -13.627  1.00 63.92           C  
ANISOU 1244  CD2 LEU A 163     6267  11047   6971   -545    152   1713       C  
ATOM   1245  N   GLY A 164     -37.824  19.787 -16.895  1.00 44.22           N  
ANISOU 1245  N   GLY A 164     3905   8367   4528   -186    269   1333       N  
ATOM   1246  CA  GLY A 164     -37.593  20.228 -18.209  1.00 50.95           C  
ANISOU 1246  CA  GLY A 164     4790   9143   5422   -132    262   1282       C  
ATOM   1247  C   GLY A 164     -36.100  20.209 -18.635  1.00 51.69           C  
ANISOU 1247  C   GLY A 164     4956   9135   5548    -94    246   1257       C  
ATOM   1248  O   GLY A 164     -35.816  20.619 -19.762  1.00 52.06           O  
ANISOU 1248  O   GLY A 164     5024   9132   5623    -43    242   1223       O  
ATOM   1249  N   PHE A 165     -35.163  19.806 -17.760  1.00 46.54           N  
ANISOU 1249  N   PHE A 165     4334   8460   4887   -115    238   1276       N  
ATOM   1250  CA  PHE A 165     -33.764  19.692 -18.195  1.00 47.20           C  
ANISOU 1250  CA  PHE A 165     4479   8454   5001    -82    220   1258       C  
ATOM   1251  C   PHE A 165     -33.698  18.629 -19.266  1.00 48.02           C  
ANISOU 1251  C   PHE A 165     4616   8490   5138    -92    163   1266       C  
ATOM   1252  O   PHE A 165     -34.661  17.858 -19.383  1.00 45.29           O  
ANISOU 1252  O   PHE A 165     4250   8157   4800   -142    129   1296       O  
ATOM   1253  CB  PHE A 165     -32.881  19.243 -17.078  1.00 47.87           C  
ANISOU 1253  CB  PHE A 165     4589   8525   5071   -111    212   1281       C  
ATOM   1254  CG  PHE A 165     -32.666  20.254 -16.010  1.00 47.69           C  
ANISOU 1254  CG  PHE A 165     4546   8557   5016    -85    255   1260       C  
ATOM   1255  CD1 PHE A 165     -33.164  21.528 -16.100  1.00 50.06           C  
ANISOU 1255  CD1 PHE A 165     4810   8902   5306    -31    289   1217       C  
ATOM   1256  CD2 PHE A 165     -31.914  19.915 -14.911  1.00 45.53           C  
ANISOU 1256  CD2 PHE A 165     4292   8281   4723   -107    250   1279       C  
ATOM   1257  CE1 PHE A 165     -32.947  22.441 -15.101  1.00 47.61           C  
ANISOU 1257  CE1 PHE A 165     4483   8635   4969      3    310   1185       C  
ATOM   1258  CE2 PHE A 165     -31.693  20.832 -13.920  1.00 45.25           C  
ANISOU 1258  CE2 PHE A 165     4239   8295   4656    -73    279   1251       C  
ATOM   1259  CZ  PHE A 165     -32.197  22.086 -14.018  1.00 45.40           C  
ANISOU 1259  CZ  PHE A 165     4224   8357   4668    -14    305   1200       C  
ATOM   1260  N   ASN A 166     -32.605  18.602 -20.051  1.00 46.46           N  
ANISOU 1260  N   ASN A 166     4462   8228   4961    -40    148   1240       N  
ATOM   1261  CA  ASN A 166     -32.506  17.700 -21.213  1.00 49.09           C  
ANISOU 1261  CA  ASN A 166     4826   8507   5318    -21     89   1229       C  
ATOM   1262  C   ASN A 166     -31.996  16.279 -20.823  1.00 53.97           C  
ANISOU 1262  C   ASN A 166     5487   9065   5954    -65     16   1251       C  
ATOM   1263  O   ASN A 166     -30.891  15.868 -21.194  1.00 54.76           O  
ANISOU 1263  O   ASN A 166     5630   9114   6062    -24    -14   1230       O  
ATOM   1264  CB  ASN A 166     -31.745  18.352 -22.400  1.00 46.94           C  
ANISOU 1264  CB  ASN A 166     4565   8222   5047     67    106   1193       C  
ATOM   1265  CG  ASN A 166     -31.815  17.515 -23.683  1.00 44.43           C  
ANISOU 1265  CG  ASN A 166     4269   7873   4738    107     46   1168       C  
ATOM   1266  ND2 ASN A 166     -31.249  18.017 -24.772  1.00 44.18           N  
ANISOU 1266  ND2 ASN A 166     4236   7853   4695    188     60   1144       N  
ATOM   1267  OD1 ASN A 166     -32.319  16.406 -23.666  1.00 45.48           O  
ANISOU 1267  OD1 ASN A 166     4417   7973   4890     68    -20   1173       O  
ATOM   1268  N   TRP A 167     -32.834  15.576 -20.044  1.00 53.82           N  
ANISOU 1268  N   TRP A 167     5448   9058   5940   -148    -13   1300       N  
ATOM   1269  CA  TRP A 167     -32.619  14.165 -19.628  1.00 56.34           C  
ANISOU 1269  CA  TRP A 167     5800   9316   6290   -209   -100   1337       C  
ATOM   1270  C   TRP A 167     -32.397  13.193 -20.814  1.00 56.19           C  
ANISOU 1270  C   TRP A 167     5824   9212   6311   -171   -196   1301       C  
ATOM   1271  O   TRP A 167     -31.636  12.236 -20.739  1.00 59.63           O  
ANISOU 1271  O   TRP A 167     6307   9577   6772   -174   -271   1297       O  
ATOM   1272  CB  TRP A 167     -33.825  13.680 -18.759  1.00 54.95           C  
ANISOU 1272  CB  TRP A 167     5574   9187   6117   -311   -117   1415       C  
ATOM   1273  CG  TRP A 167     -33.948  14.541 -17.552  1.00 50.60           C  
ANISOU 1273  CG  TRP A 167     4980   8732   5513   -331    -31   1441       C  
ATOM   1274  CD1 TRP A 167     -34.887  15.481 -17.319  1.00 51.49           C  
ANISOU 1274  CD1 TRP A 167     5031   8943   5588   -326     36   1442       C  
ATOM   1275  CD2 TRP A 167     -33.002  14.663 -16.524  1.00 48.98           C  
ANISOU 1275  CD2 TRP A 167     4794   8531   5282   -335     -6   1451       C  
ATOM   1276  CE2 TRP A 167     -33.461  15.650 -15.642  1.00 48.28           C  
ANISOU 1276  CE2 TRP A 167     4653   8551   5139   -332     71   1457       C  
ATOM   1277  CE3 TRP A 167     -31.783  14.034 -16.256  1.00 52.59           C  
ANISOU 1277  CE3 TRP A 167     5310   8915   5757   -334    -47   1449       C  
ATOM   1278  NE1 TRP A 167     -34.619  16.137 -16.143  1.00 51.57           N  
ANISOU 1278  NE1 TRP A 167     5019   9025   5549   -325     95   1450       N  
ATOM   1279  CZ2 TRP A 167     -32.752  16.035 -14.531  1.00 51.53           C  
ANISOU 1279  CZ2 TRP A 167     5069   8995   5514   -326    107   1459       C  
ATOM   1280  CZ3 TRP A 167     -31.080  14.406 -15.150  1.00 51.09           C  
ANISOU 1280  CZ3 TRP A 167     5124   8754   5533   -336     -6   1459       C  
ATOM   1281  CH2 TRP A 167     -31.556  15.395 -14.291  1.00 51.55           C  
ANISOU 1281  CH2 TRP A 167     5131   8919   5538   -332     68   1463       C  
ATOM   1282  N   ASN A 168     -33.052  13.438 -21.916  1.00 52.07           N  
ANISOU 1282  N   ASN A 168     5288   8701   5795   -128   -201   1266       N  
ATOM   1283  CA  ASN A 168     -32.911  12.544 -23.029  1.00 55.64           C  
ANISOU 1283  CA  ASN A 168     5778   9084   6279    -79   -299   1221       C  
ATOM   1284  C   ASN A 168     -31.418  12.552 -23.449  1.00 59.30           C  
ANISOU 1284  C   ASN A 168     6288   9521   6721      9   -299   1169       C  
ATOM   1285  O   ASN A 168     -30.850  11.496 -23.710  1.00 55.29           O  
ANISOU 1285  O   ASN A 168     5826   8944   6238     32   -396   1142       O  
ATOM   1286  CB  ASN A 168     -33.811  13.019 -24.161  1.00 56.42           C  
ANISOU 1286  CB  ASN A 168     5849   9214   6373    -33   -287   1187       C  
ATOM   1287  CG  ASN A 168     -33.516  12.356 -25.500  1.00 60.28           C  
ANISOU 1287  CG  ASN A 168     6375   9652   6874     54   -374   1119       C  
ATOM   1288  ND2 ASN A 168     -33.399  13.160 -26.554  1.00 64.64           N  
ANISOU 1288  ND2 ASN A 168     6915  10254   7389    147   -324   1072       N  
ATOM   1289  OD1 ASN A 168     -33.457  11.149 -25.598  1.00 64.55           O  
ANISOU 1289  OD1 ASN A 168     6951  10115   7457     42   -492   1109       O  
ATOM   1290  N   TRP A 169     -30.820  13.742 -23.514  1.00 55.77           N  
ANISOU 1290  N   TRP A 169     5825   9131   6233     60   -200   1157       N  
ATOM   1291  CA  TRP A 169     -29.437  13.908 -23.993  1.00 57.07           C  
ANISOU 1291  CA  TRP A 169     6016   9293   6374    147   -189   1120       C  
ATOM   1292  C   TRP A 169     -28.432  13.351 -22.963  1.00 58.04           C  
ANISOU 1292  C   TRP A 169     6174   9373   6505    113   -212   1139       C  
ATOM   1293  O   TRP A 169     -27.522  12.607 -23.314  1.00 54.53           O  
ANISOU 1293  O   TRP A 169     5769   8888   6062    164   -273   1105       O  
ATOM   1294  CB  TRP A 169     -29.092  15.389 -24.361  1.00 51.66           C  
ANISOU 1294  CB  TRP A 169     5294   8678   5655    201    -86   1121       C  
ATOM   1295  CG  TRP A 169     -27.659  15.501 -24.754  1.00 48.57           C  
ANISOU 1295  CG  TRP A 169     4918   8294   5241    277    -78   1104       C  
ATOM   1296  CD1 TRP A 169     -27.123  15.276 -25.994  1.00 46.11           C  
ANISOU 1296  CD1 TRP A 169     4610   8007   4903    377   -105   1065       C  
ATOM   1297  CD2 TRP A 169     -26.565  15.784 -23.885  1.00 43.00           C  
ANISOU 1297  CD2 TRP A 169     4222   7580   4533    264    -46   1126       C  
ATOM   1298  CE2 TRP A 169     -25.391  15.721 -24.668  1.00 48.31           C  
ANISOU 1298  CE2 TRP A 169     4901   8273   5181    353    -53   1106       C  
ATOM   1299  CE3 TRP A 169     -26.462  16.105 -22.540  1.00 42.06           C  
ANISOU 1299  CE3 TRP A 169     4104   7448   4427    193    -12   1161       C  
ATOM   1300  NE1 TRP A 169     -25.777  15.415 -25.950  1.00 47.71           N  
ANISOU 1300  NE1 TRP A 169     4818   8224   5085    423    -88   1069       N  
ATOM   1301  CZ2 TRP A 169     -24.097  15.956 -24.127  1.00 45.27           C  
ANISOU 1301  CZ2 TRP A 169     4522   7885   4791    364    -30   1124       C  
ATOM   1302  CZ3 TRP A 169     -25.195  16.288 -21.987  1.00 45.35           C  
ANISOU 1302  CZ3 TRP A 169     4536   7854   4841    205      4   1171       C  
ATOM   1303  CH2 TRP A 169     -24.027  16.234 -22.789  1.00 44.63           C  
ANISOU 1303  CH2 TRP A 169     4449   7774   4732    287     -3   1155       C  
ATOM   1304  N   ILE A 170     -28.620  13.699 -21.699  1.00 55.30           N  
ANISOU 1304  N   ILE A 170     5812   9040   6159     34   -166   1188       N  
ATOM   1305  CA  ILE A 170     -27.641  13.345 -20.719  1.00 52.85           C  
ANISOU 1305  CA  ILE A 170     5532   8698   5850      8   -175   1207       C  
ATOM   1306  C   ILE A 170     -27.794  11.862 -20.358  1.00 59.32           C  
ANISOU 1306  C   ILE A 170     6387   9443   6708    -48   -286   1224       C  
ATOM   1307  O   ILE A 170     -26.823  11.201 -20.083  1.00 61.07           O  
ANISOU 1307  O   ILE A 170     6650   9613   6939    -37   -335   1215       O  
ATOM   1308  CB  ILE A 170     -27.680  14.339 -19.527  1.00 49.81           C  
ANISOU 1308  CB  ILE A 170     5116   8363   5444    -37    -88   1244       C  
ATOM   1309  CG1 ILE A 170     -26.341  14.325 -18.770  1.00 49.42           C  
ANISOU 1309  CG1 ILE A 170     5097   8289   5389    -29    -80   1247       C  
ATOM   1310  CG2 ILE A 170     -28.863  14.110 -18.646  1.00 45.68           C  
ANISOU 1310  CG2 ILE A 170     4563   7869   4923   -127    -89   1295       C  
ATOM   1311  CD1 ILE A 170     -26.242  15.361 -17.671  1.00 48.95           C  
ANISOU 1311  CD1 ILE A 170     5013   8276   5310    -53     -5   1269       C  
ATOM   1312  N   ASN A 171     -29.001  11.317 -20.409  1.00 62.67           N  
ANISOU 1312  N   ASN A 171     6793   9856   7160   -108   -337   1252       N  
ATOM   1313  CA  ASN A 171     -29.188   9.862 -20.208  1.00 60.72           C  
ANISOU 1313  CA  ASN A 171     6578   9524   6968   -164   -467   1276       C  
ATOM   1314  C   ASN A 171     -28.520   9.058 -21.348  1.00 59.65           C  
ANISOU 1314  C   ASN A 171     6494   9316   6854    -70   -569   1197       C  
ATOM   1315  O   ASN A 171     -27.875   8.062 -21.096  1.00 57.87           O  
ANISOU 1315  O   ASN A 171     6313   9013   6659    -75   -665   1190       O  
ATOM   1316  CB  ASN A 171     -30.701   9.477 -20.047  1.00 58.33           C  
ANISOU 1316  CB  ASN A 171     6234   9228   6700   -255   -507   1338       C  
ATOM   1317  CG  ASN A 171     -31.337  10.043 -18.757  1.00 57.64           C  
ANISOU 1317  CG  ASN A 171     6090   9225   6584   -347   -423   1423       C  
ATOM   1318  ND2 ASN A 171     -32.608  10.026 -18.706  1.00 55.07           N  
ANISOU 1318  ND2 ASN A 171     5714   8941   6270   -408   -426   1472       N  
ATOM   1319  OD1 ASN A 171     -30.668  10.497 -17.841  1.00 57.75           O  
ANISOU 1319  OD1 ASN A 171     6106   9274   6562   -355   -359   1439       O  
ATOM   1320  N   LYS A 172     -28.665   9.485 -22.596  1.00 57.21           N  
ANISOU 1320  N   LYS A 172     6175   9037   6522     21   -554   1135       N  
ATOM   1321  CA  LYS A 172     -27.901   8.860 -23.684  1.00 61.92           C  
ANISOU 1321  CA  LYS A 172     6814   9596   7116    135   -638   1050       C  
ATOM   1322  C   LYS A 172     -26.363   8.922 -23.388  1.00 61.88           C  
ANISOU 1322  C   LYS A 172     6837   9595   7079    190   -613   1027       C  
ATOM   1323  O   LYS A 172     -25.616   7.985 -23.616  1.00 61.56           O  
ANISOU 1323  O   LYS A 172     6840   9496   7052    242   -712    979       O  
ATOM   1324  CB  LYS A 172     -28.267   9.483 -25.035  1.00 65.85           C  
ANISOU 1324  CB  LYS A 172     7285  10155   7577    231   -604    995       C  
ATOM   1325  CG  LYS A 172     -29.291   8.668 -25.840  1.00 75.45           C  
ANISOU 1325  CG  LYS A 172     8509  11320   8836    240   -721    962       C  
ATOM   1326  CD  LYS A 172     -30.150   9.464 -26.841  1.00 79.70           C  
ANISOU 1326  CD  LYS A 172     9007  11928   9346    286   -665    941       C  
ATOM   1327  CE  LYS A 172     -29.308  10.413 -27.693  1.00 82.66           C  
ANISOU 1327  CE  LYS A 172     9364  12396   9644    405   -574    900       C  
ATOM   1328  NZ  LYS A 172     -30.124  11.033 -28.764  1.00 84.89           N1+
ANISOU 1328  NZ  LYS A 172     9611  12739   9902    457   -542    877       N1+
ATOM   1329  N   GLN A 173     -25.930  10.014 -22.811  1.00 58.85           N  
ANISOU 1329  N   GLN A 173     6426   9275   6658    175   -488   1063       N  
ATOM   1330  CA  GLN A 173     -24.551  10.163 -22.441  1.00 61.75           C  
ANISOU 1330  CA  GLN A 173     6811   9650   7000    216   -457   1053       C  
ATOM   1331  C   GLN A 173     -24.170   9.153 -21.363  1.00 59.05           C  
ANISOU 1331  C   GLN A 173     6512   9224   6697    145   -534   1079       C  
ATOM   1332  O   GLN A 173     -23.234   8.410 -21.529  1.00 61.70           O  
ANISOU 1332  O   GLN A 173     6889   9516   7038    198   -608   1037       O  
ATOM   1333  CB  GLN A 173     -24.325  11.584 -21.980  1.00 62.12           C  
ANISOU 1333  CB  GLN A 173     6815   9771   7015    201   -319   1093       C  
ATOM   1334  CG  GLN A 173     -23.067  12.243 -22.476  1.00 65.29           C  
ANISOU 1334  CG  GLN A 173     7196  10234   7375    295   -253   1074       C  
ATOM   1335  CD  GLN A 173     -22.831  12.108 -23.948  1.00 67.43           C  
ANISOU 1335  CD  GLN A 173     7471  10534   7616    415   -298   1014       C  
ATOM   1336  NE2 GLN A 173     -23.708  12.661 -24.743  1.00 67.16           N  
ANISOU 1336  NE2 GLN A 173     7407  10547   7564    461   -285    997       N  
ATOM   1337  OE1 GLN A 173     -21.844  11.542 -24.360  1.00 69.51           O  
ANISOU 1337  OE1 GLN A 173     7757  10789   7864    476   -338    984       O  
ATOM   1338  N   GLN A 174     -24.911   9.121 -20.269  1.00 54.91           N  
ANISOU 1338  N   GLN A 174     5975   8687   6198     27   -524   1151       N  
ATOM   1339  CA  GLN A 174     -24.734   8.103 -19.245  1.00 57.49           C  
ANISOU 1339  CA  GLN A 174     6336   8941   6566    -52   -606   1194       C  
ATOM   1340  C   GLN A 174     -24.656   6.683 -19.839  1.00 65.82           C  
ANISOU 1340  C   GLN A 174     7439   9894   7674    -25   -771   1151       C  
ATOM   1341  O   GLN A 174     -23.799   5.891 -19.457  1.00 65.66           O  
ANISOU 1341  O   GLN A 174     7463   9807   7675    -20   -848   1139       O  
ATOM   1342  CB  GLN A 174     -25.878   8.194 -18.281  1.00 58.72           C  
ANISOU 1342  CB  GLN A 174     6453   9120   6736   -174   -581   1283       C  
ATOM   1343  CG  GLN A 174     -25.730   7.358 -17.036  1.00 60.44           C  
ANISOU 1343  CG  GLN A 174     6690   9291   6984   -272   -641   1354       C  
ATOM   1344  CD  GLN A 174     -27.040   7.256 -16.280  1.00 61.04           C  
ANISOU 1344  CD  GLN A 174     6714   9403   7073   -390   -637   1452       C  
ATOM   1345  NE2 GLN A 174     -26.965   7.013 -14.982  1.00 64.63           N  
ANISOU 1345  NE2 GLN A 174     7160   9873   7523   -476   -632   1533       N  
ATOM   1346  OE1 GLN A 174     -28.099   7.451 -16.849  1.00 60.66           O  
ANISOU 1346  OE1 GLN A 174     6630   9384   7032   -399   -631   1458       O  
ATOM   1347  N   GLY A 175     -25.539   6.391 -20.800  1.00 67.70           N  
ANISOU 1347  N   GLY A 175     7669  10118   7935     -1   -831   1121       N  
ATOM   1348  CA  GLY A 175     -25.612   5.095 -21.459  1.00 63.40           C  
ANISOU 1348  CA  GLY A 175     7168   9472   7449     33  -1005   1069       C  
ATOM   1349  C   GLY A 175     -24.456   4.762 -22.349  1.00 61.73           C  
ANISOU 1349  C   GLY A 175     6996   9248   7209    179  -1058    961       C  
ATOM   1350  O   GLY A 175     -23.860   3.702 -22.249  1.00 63.55           O  
ANISOU 1350  O   GLY A 175     7277   9390   7479    201  -1189    926       O  
ATOM   1351  N   LYS A 176     -24.103   5.685 -23.214  1.00 65.42           N  
ANISOU 1351  N   LYS A 176     7436   9813   7605    284   -959    911       N  
ATOM   1352  CA  LYS A 176     -22.975   5.465 -24.117  1.00 64.45           C  
ANISOU 1352  CA  LYS A 176     7336   9715   7437    435   -994    814       C  
ATOM   1353  C   LYS A 176     -21.676   5.261 -23.336  1.00 66.57           C  
ANISOU 1353  C   LYS A 176     7632   9966   7696    439   -989    818       C  
ATOM   1354  O   LYS A 176     -20.884   4.442 -23.709  1.00 66.85           O  
ANISOU 1354  O   LYS A 176     7704   9963   7731    529  -1092    744       O  
ATOM   1355  CB  LYS A 176     -22.782   6.644 -25.063  1.00 67.73           C  
ANISOU 1355  CB  LYS A 176     7701  10261   7770    531   -867    790       C  
ATOM   1356  CG  LYS A 176     -23.764   6.755 -26.203  1.00 73.84           C  
ANISOU 1356  CG  LYS A 176     8453  11067   8536    583   -888    751       C  
ATOM   1357  CD  LYS A 176     -23.463   8.011 -27.022  1.00 78.62           C  
ANISOU 1357  CD  LYS A 176     9003  11810   9059    667   -753    748       C  
ATOM   1358  CE  LYS A 176     -24.359   9.188 -26.662  1.00 86.75           C  
ANISOU 1358  CE  LYS A 176     9986  12883  10091    574   -628    828       C  
ATOM   1359  NZ  LYS A 176     -24.841   9.920 -27.888  1.00 96.35           N1+
ANISOU 1359  NZ  LYS A 176    11158  14189  11259    654   -577    805       N1+
ATOM   1360  N   ARG A 177     -21.465   6.009 -22.263  1.00 64.35           N  
ANISOU 1360  N   ARG A 177     7330   9713   7405    351   -875    897       N  
ATOM   1361  CA  ARG A 177     -20.242   5.889 -21.484  1.00 67.35           C  
ANISOU 1361  CA  ARG A 177     7734  10077   7776    351   -864    905       C  
ATOM   1362  C   ARG A 177     -20.180   4.750 -20.415  1.00 71.37           C  
ANISOU 1362  C   ARG A 177     8294  10469   8354    259   -980    938       C  
ATOM   1363  O   ARG A 177     -19.170   4.609 -19.705  1.00 70.62           O  
ANISOU 1363  O   ARG A 177     8222  10356   8254    255   -976    945       O  
ATOM   1364  CB  ARG A 177     -19.945   7.227 -20.784  1.00 67.41           C  
ANISOU 1364  CB  ARG A 177     7701  10166   7747    306   -700    969       C  
ATOM   1365  CG  ARG A 177     -19.930   8.468 -21.676  1.00 67.58           C  
ANISOU 1365  CG  ARG A 177     7666  10297   7711    378   -585    960       C  
ATOM   1366  CD  ARG A 177     -19.096   8.386 -22.941  1.00 72.09           C  
ANISOU 1366  CD  ARG A 177     8230  10928   8233    527   -605    886       C  
ATOM   1367  NE  ARG A 177     -19.676   9.329 -23.875  1.00 77.54           N  
ANISOU 1367  NE  ARG A 177     8867  11707   8886    569   -527    890       N  
ATOM   1368  CZ  ARG A 177     -19.613   9.268 -25.193  1.00 81.23           C  
ANISOU 1368  CZ  ARG A 177     9315  12238   9308    688   -549    833       C  
ATOM   1369  NH1 ARG A 177     -18.936   8.301 -25.802  1.00 87.11           N1+
ANISOU 1369  NH1 ARG A 177    10087  12977  10032    796   -650    753       N1+
ATOM   1370  NH2 ARG A 177     -20.246  10.200 -25.905  1.00 83.49           N  
ANISOU 1370  NH2 ARG A 177     9551  12601   9567    705   -472    853       N  
ATOM   1371  N   GLY A 178     -21.241   3.958 -20.276  1.00 71.58           N  
ANISOU 1371  N   GLY A 178     8333  10416   8446    181  -1085    968       N  
ATOM   1372  CA  GLY A 178     -21.284   2.923 -19.250  1.00 64.35           C  
ANISOU 1372  CA  GLY A 178     7454   9393   7601     78  -1197   1023       C  
ATOM   1373  C   GLY A 178     -21.221   3.482 -17.840  1.00 67.80           C  
ANISOU 1373  C   GLY A 178     7871   9865   8024    -35  -1091   1125       C  
ATOM   1374  O   GLY A 178     -20.957   2.735 -16.848  1.00 63.43           O  
ANISOU 1374  O   GLY A 178     7346   9240   7512   -114  -1163   1179       O  
ATOM   1375  N   TRP A 179     -21.478   4.783 -17.696  1.00 64.00           N  
ANISOU 1375  N   TRP A 179     7339   9492   7486    -46   -929   1155       N  
ATOM   1376  CA  TRP A 179     -21.485   5.351 -16.332  1.00 62.39           C  
ANISOU 1376  CA  TRP A 179     7113   9329   7263   -143   -835   1242       C  
ATOM   1377  C   TRP A 179     -22.520   4.693 -15.424  1.00 59.40           C  
ANISOU 1377  C   TRP A 179     6721   8917   6930   -281   -894   1344       C  
ATOM   1378  O   TRP A 179     -23.552   4.212 -15.849  1.00 67.62           O  
ANISOU 1378  O   TRP A 179     7748   9930   8013   -319   -964   1366       O  
ATOM   1379  CB  TRP A 179     -21.687   6.879 -16.305  1.00 57.65           C  
ANISOU 1379  CB  TRP A 179     6459   8843   6600   -129   -668   1252       C  
ATOM   1380  CG  TRP A 179     -20.633   7.666 -17.013  1.00 56.05           C  
ANISOU 1380  CG  TRP A 179     6255   8686   6354    -14   -598   1184       C  
ATOM   1381  CD1 TRP A 179     -19.418   7.207 -17.497  1.00 57.42           C  
ANISOU 1381  CD1 TRP A 179     6463   8829   6523     75   -649   1120       C  
ATOM   1382  CD2 TRP A 179     -20.677   9.054 -17.326  1.00 56.29           C  
ANISOU 1382  CD2 TRP A 179     6238   8806   6341     22   -471   1180       C  
ATOM   1383  CE2 TRP A 179     -19.474   9.372 -18.022  1.00 57.04           C  
ANISOU 1383  CE2 TRP A 179     6338   8925   6409    128   -449   1127       C  
ATOM   1384  CE3 TRP A 179     -21.631  10.054 -17.145  1.00 56.74           C  
ANISOU 1384  CE3 TRP A 179     6247   8930   6381    -17   -381   1216       C  
ATOM   1385  NE1 TRP A 179     -18.723   8.225 -18.108  1.00 51.24           N  
ANISOU 1385  NE1 TRP A 179     5651   8123   5692    162   -555   1089       N  
ATOM   1386  CZ2 TRP A 179     -19.216  10.666 -18.524  1.00 55.36           C  
ANISOU 1386  CZ2 TRP A 179     6079   8792   6161    181   -344   1124       C  
ATOM   1387  CZ3 TRP A 179     -21.360  11.351 -17.650  1.00 54.51           C  
ANISOU 1387  CZ3 TRP A 179     5927   8717   6066     42   -281   1198       C  
ATOM   1388  CH2 TRP A 179     -20.162  11.638 -18.303  1.00 54.27           C  
ANISOU 1388  CH2 TRP A 179     5901   8701   6018    134   -266   1160       C  
ATOM   1389  N   GLY A 180     -22.218   4.698 -14.147  1.00 62.70           N  
ANISOU 1389  N   GLY A 180     7137   9347   7338   -356   -865   1414       N  
ATOM   1390  CA  GLY A 180     -23.205   4.421 -13.140  1.00 61.38           C  
ANISOU 1390  CA  GLY A 180     6932   9200   7186   -487   -875   1531       C  
ATOM   1391  C   GLY A 180     -24.217   5.518 -12.989  1.00 66.45           C  
ANISOU 1391  C   GLY A 180     7505   9963   7777   -514   -747   1567       C  
ATOM   1392  O   GLY A 180     -24.420   6.331 -13.893  1.00 68.33           O  
ANISOU 1392  O   GLY A 180     7727  10244   7989   -440   -679   1503       O  
ATOM   1393  N   GLN A 181     -24.901   5.502 -11.850  1.00 71.38           N  
ANISOU 1393  N   GLN A 181     8087  10651   8383   -615   -716   1672       N  
ATOM   1394  CA  GLN A 181     -26.059   6.353 -11.625  1.00 82.19           C  
ANISOU 1394  CA  GLN A 181     9381  12138   9707   -655   -622   1722       C  
ATOM   1395  C   GLN A 181     -25.698   7.779 -11.243  1.00 76.23           C  
ANISOU 1395  C   GLN A 181     8605  11484   8874   -586   -472   1669       C  
ATOM   1396  O   GLN A 181     -24.649   8.038 -10.653  1.00 70.41           O  
ANISOU 1396  O   GLN A 181     7900  10737   8113   -541   -436   1631       O  
ATOM   1397  CB  GLN A 181     -26.968   5.742 -10.555  1.00 89.65           C  
ANISOU 1397  CB  GLN A 181    10278  13130  10655   -785   -656   1864       C  
ATOM   1398  CG  GLN A 181     -27.616   4.430 -10.967  1.00102.77           C  
ANISOU 1398  CG  GLN A 181    11861  14868  12316   -853   -647   1940       C  
ATOM   1399  CD  GLN A 181     -28.488   4.572 -12.198  1.00102.63           C  
ANISOU 1399  CD  GLN A 181    11855  14751  12387   -867   -768   1933       C  
ATOM   1400  NE2 GLN A 181     -28.430   3.583 -13.082  1.00 95.56           N  
ANISOU 1400  NE2 GLN A 181    10908  13866  11534   -980   -843   2056       N  
ATOM   1401  OE1 GLN A 181     -29.206   5.560 -12.354  1.00 96.91           O  
ANISOU 1401  OE1 GLN A 181    11179  13951  11688   -774   -795   1822       O  
ATOM   1402  N   LEU A 182     -26.591   8.699 -11.586  1.00 69.55           N  
ANISOU 1402  N   LEU A 182     7704  10725   7995   -575   -393   1664       N  
ATOM   1403  CA  LEU A 182     -26.439  10.099 -11.239  1.00 68.44           C  
ANISOU 1403  CA  LEU A 182     7535  10678   7789   -520   -268   1624       C  
ATOM   1404  C   LEU A 182     -26.399  10.214  -9.725  1.00 65.27           C  
ANISOU 1404  C   LEU A 182     7106  10356   7336   -572   -232   1689       C  
ATOM   1405  O   LEU A 182     -27.342   9.823  -9.081  1.00 65.37           O  
ANISOU 1405  O   LEU A 182     7068  10437   7332   -652   -242   1779       O  
ATOM   1406  CB  LEU A 182     -27.619  10.896 -11.772  1.00 66.74           C  
ANISOU 1406  CB  LEU A 182     7261  10542   7552   -506   -209   1614       C  
ATOM   1407  CG  LEU A 182     -27.705  12.372 -11.387  1.00 64.87           C  
ANISOU 1407  CG  LEU A 182     6987  10405   7255   -453    -95   1575       C  
ATOM   1408  CD1 LEU A 182     -26.741  13.120 -12.272  1.00 61.63           C  
ANISOU 1408  CD1 LEU A 182     6615   9941   6859   -357    -68   1485       C  
ATOM   1409  CD2 LEU A 182     -29.146  12.895 -11.509  1.00 64.33           C  
ANISOU 1409  CD2 LEU A 182     6847  10436   7159   -470    -52   1596       C  
ATOM   1410  N   THR A 183     -25.339  10.754  -9.137  1.00 63.81           N  
ANISOU 1410  N   THR A 183     6949  10173   7123   -527   -190   1651       N  
ATOM   1411  CA  THR A 183     -25.338  10.820  -7.660  1.00 71.68           C  
ANISOU 1411  CA  THR A 183     7917  11253   8062   -571   -161   1711       C  
ATOM   1412  C   THR A 183     -25.957  12.080  -7.094  1.00 69.63           C  
ANISOU 1412  C   THR A 183     7596  11130   7729   -535    -63   1693       C  
ATOM   1413  O   THR A 183     -26.730  12.010  -6.148  1.00 70.91           O  
ANISOU 1413  O   THR A 183     7700  11406   7834   -584    -43   1764       O  
ATOM   1414  CB  THR A 183     -23.957  10.636  -7.064  1.00 66.20           C  
ANISOU 1414  CB  THR A 183     7280  10500   7372   -551   -179   1691       C  
ATOM   1415  CG2 THR A 183     -23.319   9.374  -7.662  1.00 67.28           C  
ANISOU 1415  CG2 THR A 183     7479  10501   7582   -573   -287   1695       C  
ATOM   1416  OG1 THR A 183     -23.170  11.807  -7.321  1.00 67.36           O  
ANISOU 1416  OG1 THR A 183     7443  10642   7506   -457   -115   1598       O  
ATOM   1417  N   SER A 184     -25.626  13.231  -7.660  1.00 62.75           N  
ANISOU 1417  N   SER A 184     6732  10252   6856   -448     -8   1602       N  
ATOM   1418  CA  SER A 184     -26.222  14.476  -7.184  1.00 62.41           C  
ANISOU 1418  CA  SER A 184     6635  10326   6752   -402     68   1570       C  
ATOM   1419  C   SER A 184     -26.174  15.544  -8.258  1.00 59.61           C  
ANISOU 1419  C   SER A 184     6283   9938   6425   -324    102   1486       C  
ATOM   1420  O   SER A 184     -25.419  15.421  -9.223  1.00 57.02           O  
ANISOU 1420  O   SER A 184     6002   9508   6153   -295     77   1451       O  
ATOM   1421  CB  SER A 184     -25.507  14.966  -5.921  1.00 64.93           C  
ANISOU 1421  CB  SER A 184     6958  10691   7020   -373     93   1555       C  
ATOM   1422  OG  SER A 184     -24.081  14.895  -6.053  1.00 62.25           O  
ANISOU 1422  OG  SER A 184     6686  10239   6724   -343     67   1515       O  
ATOM   1423  N   ASN A 185     -27.043  16.537  -8.107  1.00 53.50           N  
ANISOU 1423  N   ASN A 185     5455   9261   5610   -289    153   1461       N  
ATOM   1424  CA  ASN A 185     -26.955  17.790  -8.802  1.00 55.74           C  
ANISOU 1424  CA  ASN A 185     5735   9529   5912   -210    186   1383       C  
ATOM   1425  C   ASN A 185     -26.725  18.816  -7.779  1.00 53.55           C  
ANISOU 1425  C   ASN A 185     5439   9315   5591   -156    215   1339       C  
ATOM   1426  O   ASN A 185     -27.563  19.022  -6.918  1.00 55.59           O  
ANISOU 1426  O   ASN A 185     5645   9695   5781   -157    239   1351       O  
ATOM   1427  CB  ASN A 185     -28.267  18.180  -9.484  1.00 53.08           C  
ANISOU 1427  CB  ASN A 185     5347   9252   5568   -205    210   1378       C  
ATOM   1428  CG  ASN A 185     -28.564  17.328 -10.651  1.00 58.13           C  
ANISOU 1428  CG  ASN A 185     6003   9825   6257   -243    176   1405       C  
ATOM   1429  ND2 ASN A 185     -27.922  17.646 -11.796  1.00 63.21           N  
ANISOU 1429  ND2 ASN A 185     6682  10381   6952   -194    168   1359       N  
ATOM   1430  OD1 ASN A 185     -29.332  16.366 -10.552  1.00 53.22           O  
ANISOU 1430  OD1 ASN A 185     5360   9230   5629   -313    149   1470       O  
ATOM   1431  N   LEU A 186     -25.671  19.557  -7.925  1.00 51.05           N  
ANISOU 1431  N   LEU A 186     5158   8926   5313    -99    210   1284       N  
ATOM   1432  CA  LEU A 186     -25.380  20.576  -6.925  1.00 56.08           C  
ANISOU 1432  CA  LEU A 186     5781   9607   5917    -39    220   1232       C  
ATOM   1433  C   LEU A 186     -25.757  21.935  -7.497  1.00 57.29           C  
ANISOU 1433  C   LEU A 186     5909   9761   6096     31    230   1166       C  
ATOM   1434  O   LEU A 186     -25.433  22.271  -8.664  1.00 53.97           O  
ANISOU 1434  O   LEU A 186     5505   9258   5743     46    224   1155       O  
ATOM   1435  CB  LEU A 186     -23.873  20.589  -6.592  1.00 56.66           C  
ANISOU 1435  CB  LEU A 186     5909   9589   6028    -22    192   1217       C  
ATOM   1436  CG  LEU A 186     -23.533  21.437  -5.376  1.00 61.47           C  
ANISOU 1436  CG  LEU A 186     6510  10243   6601     34    187   1166       C  
ATOM   1437  CD1 LEU A 186     -24.009  20.740  -4.098  1.00 64.54           C  
ANISOU 1437  CD1 LEU A 186     6876  10747   6897      2    197   1205       C  
ATOM   1438  CD2 LEU A 186     -22.055  21.726  -5.284  1.00 58.04           C  
ANISOU 1438  CD2 LEU A 186     6123   9701   6225     60    155   1142       C  
ATOM   1439  N   LEU A 187     -26.350  22.766  -6.662  1.00 57.50           N  
ANISOU 1439  N   LEU A 187     5894   9882   6069     83    240   1119       N  
ATOM   1440  CA  LEU A 187     -26.693  24.108  -7.093  1.00 57.65           C  
ANISOU 1440  CA  LEU A 187     5891   9896   6118    157    233   1049       C  
ATOM   1441  C   LEU A 187     -25.691  25.072  -6.536  1.00 55.27           C  
ANISOU 1441  C   LEU A 187     5612   9536   5850    223    193    987       C  
ATOM   1442  O   LEU A 187     -25.528  25.143  -5.325  1.00 54.90           O  
ANISOU 1442  O   LEU A 187     5561   9549   5748    252    183    960       O  
ATOM   1443  CB  LEU A 187     -28.074  24.480  -6.623  1.00 58.27           C  
ANISOU 1443  CB  LEU A 187     5904  10116   6118    187    257   1023       C  
ATOM   1444  CG  LEU A 187     -28.417  25.961  -6.724  1.00 57.70           C  
ANISOU 1444  CG  LEU A 187     5807  10050   6066    282    235    932       C  
ATOM   1445  CD1 LEU A 187     -28.399  26.435  -8.163  1.00 54.98           C  
ANISOU 1445  CD1 LEU A 187     5474   9603   5812    280    226    933       C  
ATOM   1446  CD2 LEU A 187     -29.798  26.143  -6.110  1.00 58.01           C  
ANISOU 1446  CD2 LEU A 187     5776  10257   6007    315    261    908       C  
ATOM   1447  N   LEU A 188     -25.006  25.814  -7.384  1.00 53.43           N  
ANISOU 1447  N   LEU A 188     5399   9189   5711    248    165    970       N  
ATOM   1448  CA  LEU A 188     -23.972  26.707  -6.918  1.00 53.30           C  
ANISOU 1448  CA  LEU A 188     5404   9100   5746    301    112    924       C  
ATOM   1449  C   LEU A 188     -24.293  28.127  -7.247  1.00 55.85           C  
ANISOU 1449  C   LEU A 188     5701   9396   6122    370     72    863       C  
ATOM   1450  O   LEU A 188     -24.610  28.439  -8.360  1.00 55.21           O  
ANISOU 1450  O   LEU A 188     5607   9279   6090    360     79    884       O  
ATOM   1451  CB  LEU A 188     -22.638  26.342  -7.535  1.00 51.11           C  
ANISOU 1451  CB  LEU A 188     5170   8704   5545    267     96    971       C  
ATOM   1452  CG  LEU A 188     -22.151  24.944  -7.246  1.00 53.95           C  
ANISOU 1452  CG  LEU A 188     5563   9065   5868    203    119   1026       C  
ATOM   1453  CD1 LEU A 188     -22.271  24.083  -8.470  1.00 52.42           C  
ANISOU 1453  CD1 LEU A 188     5379   8839   5697    151    145   1086       C  
ATOM   1454  CD2 LEU A 188     -20.723  24.977  -6.775  1.00 53.05           C  
ANISOU 1454  CD2 LEU A 188     5487   8874   5793    210     83   1026       C  
ATOM   1455  N   ILE A 189     -24.195  28.995  -6.263  1.00 60.18           N  
ANISOU 1455  N   ILE A 189     6243   9959   6662    445     20    785       N  
ATOM   1456  CA  ILE A 189     -24.517  30.385  -6.451  1.00 58.86           C  
ANISOU 1456  CA  ILE A 189     6053   9759   6552    521    -41    714       C  
ATOM   1457  C   ILE A 189     -23.458  31.188  -5.787  1.00 58.35           C  
ANISOU 1457  C   ILE A 189     6011   9605   6551    574   -126    666       C  
ATOM   1458  O   ILE A 189     -23.311  31.151  -4.553  1.00 55.72           O  
ANISOU 1458  O   ILE A 189     5685   9327   6158    618   -147    611       O  
ATOM   1459  CB  ILE A 189     -25.884  30.744  -5.854  1.00 60.20           C  
ANISOU 1459  CB  ILE A 189     6176  10066   6629    586    -32    641       C  
ATOM   1460  CG1 ILE A 189     -26.984  29.986  -6.571  1.00 61.37           C  
ANISOU 1460  CG1 ILE A 189     6295  10297   6723    529     46    695       C  
ATOM   1461  CG2 ILE A 189     -26.110  32.227  -6.025  1.00 59.80           C  
ANISOU 1461  CG2 ILE A 189     6108   9962   6648    674   -116    557       C  
ATOM   1462  CD1 ILE A 189     -28.325  30.009  -5.873  1.00 70.34           C  
ANISOU 1462  CD1 ILE A 189     7376  11602   7745    575     73    648       C  
ATOM   1463  N   GLY A 190     -22.723  31.931  -6.601  1.00 58.62           N  
ANISOU 1463  N   GLY A 190     6053   9508   6711    569   -182    691       N  
ATOM   1464  CA  GLY A 190     -21.526  32.574  -6.107  1.00 61.24           C  
ANISOU 1464  CA  GLY A 190     6407   9733   7126    597   -269    671       C  
ATOM   1465  C   GLY A 190     -21.528  34.042  -6.333  1.00 62.43           C  
ANISOU 1465  C   GLY A 190     6540   9795   7386    661   -377    621       C  
ATOM   1466  O   GLY A 190     -22.289  34.560  -7.165  1.00 63.72           O  
ANISOU 1466  O   GLY A 190     6676   9957   7579    667   -380    624       O  
ATOM   1467  N   MET A 191     -20.665  34.709  -5.583  1.00 63.86           N  
ANISOU 1467  N   MET A 191     6738   9893   7631    706   -476    576       N  
ATOM   1468  CA  MET A 191     -20.411  36.124  -5.778  1.00 67.36           C  
ANISOU 1468  CA  MET A 191     7168  10216   8209    759   -609    540       C  
ATOM   1469  C   MET A 191     -19.222  36.297  -6.711  1.00 65.57           C  
ANISOU 1469  C   MET A 191     6940   9856   8117    685   -638    659       C  
ATOM   1470  O   MET A 191     -18.311  35.443  -6.767  1.00 64.38           O  
ANISOU 1470  O   MET A 191     6808   9697   7956    621   -583    734       O  
ATOM   1471  CB  MET A 191     -20.115  36.818  -4.450  1.00 72.70           C  
ANISOU 1471  CB  MET A 191     7860  10866   8893    857   -722    421       C  
ATOM   1472  CG  MET A 191     -21.253  36.813  -3.431  1.00 79.16           C  
ANISOU 1472  CG  MET A 191     8668  11834   9573    954   -709    293       C  
ATOM   1473  SD  MET A 191     -20.641  37.310  -1.794  1.00 80.64           S  
ANISOU 1473  SD  MET A 191     8881  12012   9745   1068   -827    163       S  
ATOM   1474  CE  MET A 191     -20.004  38.940  -2.191  1.00 82.83           C  
ANISOU 1474  CE  MET A 191     9158  12074  10238   1114  -1025    130       C  
ATOM   1475  N   GLU A 192     -19.223  37.414  -7.426  1.00 61.06           N  
ANISOU 1475  N   GLU A 192     6341   9187   7671    695   -729    679       N  
ATOM   1476  CA  GLU A 192     -18.190  37.716  -8.380  1.00 66.25           C  
ANISOU 1476  CA  GLU A 192     6978   9734   8459    627   -763    807       C  
ATOM   1477  C   GLU A 192     -16.860  37.595  -7.674  1.00 66.41           C  
ANISOU 1477  C   GLU A 192     7020   9683   8527    615   -813    825       C  
ATOM   1478  O   GLU A 192     -16.751  37.949  -6.519  1.00 65.85           O  
ANISOU 1478  O   GLU A 192     6974   9591   8454    682   -891    722       O  
ATOM   1479  CB  GLU A 192     -18.375  39.124  -8.946  1.00 75.05           C  
ANISOU 1479  CB  GLU A 192     8058  10742   9715    653   -892    814       C  
ATOM   1480  CG  GLU A 192     -18.344  40.248  -7.904  1.00 82.29           C  
ANISOU 1480  CG  GLU A 192     8987  11571  10708    747  -1058    692       C  
ATOM   1481  CD  GLU A 192     -18.953  41.555  -8.419  1.00 85.94           C  
ANISOU 1481  CD  GLU A 192     9418  11949  11283    789  -1183    669       C  
ATOM   1482  OE1 GLU A 192     -19.251  41.652  -9.638  1.00 83.94           O  
ANISOU 1482  OE1 GLU A 192     9131  11696  11065    733  -1143    768       O  
ATOM   1483  OE2 GLU A 192     -19.131  42.489  -7.598  1.00 82.11           O1-
ANISOU 1483  OE2 GLU A 192     8943  11400  10852    883  -1329    546       O1-
ATOM   1484  N   GLY A 193     -15.865  37.037  -8.349  1.00 67.13           N  
ANISOU 1484  N   GLY A 193     7102   9752   8651    536   -763    951       N  
ATOM   1485  CA  GLY A 193     -14.529  36.880  -7.769  1.00 61.74           C  
ANISOU 1485  CA  GLY A 193     6435   9003   8018    517   -806    981       C  
ATOM   1486  C   GLY A 193     -14.264  35.648  -6.913  1.00 59.72           C  
ANISOU 1486  C   GLY A 193     6226   8826   7638    511   -719    944       C  
ATOM   1487  O   GLY A 193     -13.137  35.431  -6.520  1.00 61.32           O  
ANISOU 1487  O   GLY A 193     6441   8978   7878    491   -744    977       O  
ATOM   1488  N   ASN A 194     -15.283  34.864  -6.582  1.00 62.22           N  
ANISOU 1488  N   ASN A 194     6564   9263   7814    528   -625    881       N  
ATOM   1489  CA  ASN A 194     -15.108  33.636  -5.785  1.00 60.02           C  
ANISOU 1489  CA  ASN A 194     6325   9063   7415    514   -545    860       C  
ATOM   1490  C   ASN A 194     -14.323  32.577  -6.549  1.00 59.12           C  
ANISOU 1490  C   ASN A 194     6214   8956   7290    434   -461    971       C  
ATOM   1491  O   ASN A 194     -14.608  32.350  -7.730  1.00 58.34           O  
ANISOU 1491  O   ASN A 194     6090   8881   7193    396   -405   1042       O  
ATOM   1492  CB  ASN A 194     -16.459  33.017  -5.477  1.00 58.86           C  
ANISOU 1492  CB  ASN A 194     6185   9050   7129    534   -463    798       C  
ATOM   1493  CG  ASN A 194     -17.186  33.739  -4.396  1.00 64.39           C  
ANISOU 1493  CG  ASN A 194     6886   9787   7792    628   -528    671       C  
ATOM   1494  ND2 ASN A 194     -18.216  33.105  -3.883  1.00 65.38           N  
ANISOU 1494  ND2 ASN A 194     7011  10049   7781    647   -455    624       N  
ATOM   1495  OD1 ASN A 194     -16.819  34.849  -4.003  1.00 74.26           O  
ANISOU 1495  OD1 ASN A 194     8132  10948   9133    687   -649    616       O  
ATOM   1496  N   VAL A 195     -13.386  31.922  -5.868  1.00 54.64           N  
ANISOU 1496  N   VAL A 195     5679   8378   6704    419   -456    978       N  
ATOM   1497  CA  VAL A 195     -12.536  30.909  -6.475  1.00 51.46           C  
ANISOU 1497  CA  VAL A 195     5281   7980   6289    357   -391   1069       C  
ATOM   1498  C   VAL A 195     -12.785  29.648  -5.709  1.00 53.25           C  
ANISOU 1498  C   VAL A 195     5552   8286   6392    345   -322   1034       C  
ATOM   1499  O   VAL A 195     -12.752  29.671  -4.485  1.00 50.75           O  
ANISOU 1499  O   VAL A 195     5263   7979   6040    379   -354    964       O  
ATOM   1500  CB  VAL A 195     -11.040  31.280  -6.340  1.00 57.96           C  
ANISOU 1500  CB  VAL A 195     6097   8706   7216    345   -461   1119       C  
ATOM   1501  CG1 VAL A 195     -10.094  30.195  -6.902  1.00 52.84           C  
ANISOU 1501  CG1 VAL A 195     5452   8076   6546    293   -396   1205       C  
ATOM   1502  CG2 VAL A 195     -10.772  32.635  -6.992  1.00 61.38           C  
ANISOU 1502  CG2 VAL A 195     6480   9051   7790    350   -552   1167       C  
ATOM   1503  N   THR A 196     -12.998  28.551  -6.400  1.00 50.38           N  
ANISOU 1503  N   THR A 196     5194   7983   5963    301   -236   1081       N  
ATOM   1504  CA  THR A 196     -12.966  27.250  -5.807  1.00 46.96           C  
ANISOU 1504  CA  THR A 196     4802   7602   5437    274   -185   1076       C  
ATOM   1505  C   THR A 196     -11.656  26.702  -6.267  1.00 46.80           C  
ANISOU 1505  C   THR A 196     4787   7529   5463    244   -186   1144       C  
ATOM   1506  O   THR A 196     -11.513  26.361  -7.409  1.00 46.30           O  
ANISOU 1506  O   THR A 196     4700   7472   5420    223   -153   1208       O  
ATOM   1507  CB  THR A 196     -14.072  26.352  -6.347  1.00 46.88           C  
ANISOU 1507  CB  THR A 196     4793   7677   5341    244   -109   1089       C  
ATOM   1508  CG2 THR A 196     -13.994  25.024  -5.770  1.00 44.06           C  
ANISOU 1508  CG2 THR A 196     4475   7355   4909    207    -75   1100       C  
ATOM   1509  OG1 THR A 196     -15.329  26.898  -6.007  1.00 51.06           O  
ANISOU 1509  OG1 THR A 196     5307   8269   5825    274   -105   1032       O  
ATOM   1510  N   PRO A 197     -10.683  26.628  -5.387  1.00 48.53           N  
ANISOU 1510  N   PRO A 197     5033   7706   5698    248   -224   1131       N  
ATOM   1511  CA  PRO A 197      -9.336  26.259  -5.842  1.00 48.87           C  
ANISOU 1511  CA  PRO A 197     5074   7703   5791    226   -231   1196       C  
ATOM   1512  C   PRO A 197      -9.249  24.827  -6.317  1.00 48.91           C  
ANISOU 1512  C   PRO A 197     5102   7753   5726    193   -168   1228       C  
ATOM   1513  O   PRO A 197     -10.202  24.058  -6.122  1.00 47.72           O  
ANISOU 1513  O   PRO A 197     4976   7660   5494    179   -128   1202       O  
ATOM   1514  CB  PRO A 197      -8.428  26.472  -4.608  1.00 49.55           C  
ANISOU 1514  CB  PRO A 197     5188   7734   5905    242   -291   1162       C  
ATOM   1515  CG  PRO A 197      -9.311  26.918  -3.505  1.00 53.04           C  
ANISOU 1515  CG  PRO A 197     5647   8201   6302    280   -316   1074       C  
ATOM   1516  CD  PRO A 197     -10.753  26.787  -3.924  1.00 48.57           C  
ANISOU 1516  CD  PRO A 197     5069   7716   5669    280   -262   1057       C  
ATOM   1517  N   ALA A 198      -8.110  24.519  -6.951  1.00 48.09           N  
ANISOU 1517  N   ALA A 198     4985   7625   5660    184   -170   1285       N  
ATOM   1518  CA  ALA A 198      -7.876  23.296  -7.687  1.00 46.24           C  
ANISOU 1518  CA  ALA A 198     4762   7428   5377    170   -127   1316       C  
ATOM   1519  C   ALA A 198      -8.056  22.055  -6.867  1.00 46.61           C  
ANISOU 1519  C   ALA A 198     4870   7490   5349    150   -116   1279       C  
ATOM   1520  O   ALA A 198      -7.445  21.883  -5.752  1.00 42.98           O  
ANISOU 1520  O   ALA A 198     4444   6997   4888    146   -146   1256       O  
ATOM   1521  CB  ALA A 198      -6.466  23.306  -8.288  1.00 51.12           C  
ANISOU 1521  CB  ALA A 198     5350   8026   6048    178   -142   1377       C  
ATOM   1522  N   HIS A 199      -8.933  21.196  -7.401  1.00 41.46           N  
ANISOU 1522  N   HIS A 199     4230   6885   4638    134    -80   1277       N  
ATOM   1523  CA  HIS A 199      -9.187  19.914  -6.800  1.00 40.04           C  
ANISOU 1523  CA  HIS A 199     4101   6716   4394    106    -78   1260       C  
ATOM   1524  C   HIS A 199      -9.689  18.942  -7.871  1.00 42.60           C  
ANISOU 1524  C   HIS A 199     4429   7071   4686     98    -59   1274       C  
ATOM   1525  O   HIS A 199     -10.023  19.375  -9.049  1.00 43.15           O  
ANISOU 1525  O   HIS A 199     4457   7165   4770    120    -36   1291       O  
ATOM   1526  CB  HIS A 199     -10.242  20.067  -5.756  1.00 37.57           C  
ANISOU 1526  CB  HIS A 199     3802   6436   4036     89    -73   1227       C  
ATOM   1527  CG  HIS A 199     -11.548  20.444  -6.326  1.00 38.73           C  
ANISOU 1527  CG  HIS A 199     3919   6632   4164     88    -42   1222       C  
ATOM   1528  CD2 HIS A 199     -12.643  19.717  -6.624  1.00 38.47           C  
ANISOU 1528  CD2 HIS A 199     3889   6646   4081     60    -18   1228       C  
ATOM   1529  ND1 HIS A 199     -11.788  21.705  -6.793  1.00 42.69           N  
ANISOU 1529  ND1 HIS A 199     4377   7131   4710    119    -40   1216       N  
ATOM   1530  CE1 HIS A 199     -12.968  21.733  -7.385  1.00 43.67           C  
ANISOU 1530  CE1 HIS A 199     4482   7303   4808    113    -10   1214       C  
ATOM   1531  NE2 HIS A 199     -13.538  20.564  -7.221  1.00 42.53           N  
ANISOU 1531  NE2 HIS A 199     4364   7192   4604     77      4   1220       N  
ATOM   1532  N   TYR A 200      -9.820  17.670  -7.472  1.00 39.39           N  
ANISOU 1532  N   TYR A 200     4067   6660   4237     69    -75   1268       N  
ATOM   1533  CA  TYR A 200     -10.370  16.681  -8.370  1.00 42.02           C  
ANISOU 1533  CA  TYR A 200     4410   7010   4545     62    -77   1273       C  
ATOM   1534  C   TYR A 200     -11.489  15.931  -7.680  1.00 43.43           C  
ANISOU 1534  C   TYR A 200     4615   7206   4680      9    -84   1274       C  
ATOM   1535  O   TYR A 200     -11.557  15.894  -6.480  1.00 44.67           O  
ANISOU 1535  O   TYR A 200     4789   7365   4816    -19    -91   1275       O  
ATOM   1536  CB  TYR A 200      -9.350  15.698  -8.913  1.00 41.76           C  
ANISOU 1536  CB  TYR A 200     4400   6949   4517     86   -111   1272       C  
ATOM   1537  CG  TYR A 200      -8.726  14.721  -7.908  1.00 41.65           C  
ANISOU 1537  CG  TYR A 200     4441   6891   4493     60   -157   1267       C  
ATOM   1538  CD1 TYR A 200      -7.558  15.051  -7.199  1.00 41.28           C  
ANISOU 1538  CD1 TYR A 200     4401   6813   4469     71   -168   1267       C  
ATOM   1539  CD2 TYR A 200      -9.239  13.434  -7.740  1.00 43.30           C  
ANISOU 1539  CD2 TYR A 200     4691   7081   4677     23   -199   1266       C  
ATOM   1540  CE1 TYR A 200      -6.991  14.156  -6.287  1.00 39.23           C  
ANISOU 1540  CE1 TYR A 200     4192   6513   4199     48   -211   1262       C  
ATOM   1541  CE2 TYR A 200      -8.683  12.544  -6.824  1.00 41.07           C  
ANISOU 1541  CE2 TYR A 200     4456   6755   4391     -4   -248   1269       C  
ATOM   1542  CZ  TYR A 200      -7.543  12.922  -6.131  1.00 39.87           C  
ANISOU 1542  CZ  TYR A 200     4313   6580   4255     11   -250   1265       C  
ATOM   1543  OH  TYR A 200      -6.961  12.068  -5.303  1.00 41.32           O  
ANISOU 1543  OH  TYR A 200     4543   6721   4435    -12   -298   1267       O  
ATOM   1544  N   GLU A 201     -12.342  15.331  -8.496  1.00 41.26           N  
ANISOU 1544  N   GLU A 201     4336   6948   4391     -1    -87   1278       N  
ATOM   1545  CA  GLU A 201     -13.444  14.540  -8.056  1.00 46.31           C  
ANISOU 1545  CA  GLU A 201     4990   7605   4998    -57   -102   1295       C  
ATOM   1546  C   GLU A 201     -13.226  13.133  -8.598  1.00 48.98           C  
ANISOU 1546  C   GLU A 201     5366   7898   5346    -66   -164   1298       C  
ATOM   1547  O   GLU A 201     -12.584  12.912  -9.623  1.00 52.05           O  
ANISOU 1547  O   GLU A 201     5757   8265   5751    -14   -181   1275       O  
ATOM   1548  CB  GLU A 201     -14.747  15.142  -8.632  1.00 46.51           C  
ANISOU 1548  CB  GLU A 201     4973   7684   5012    -59    -62   1296       C  
ATOM   1549  CG  GLU A 201     -15.627  15.848  -7.624  1.00 44.99           C  
ANISOU 1549  CG  GLU A 201     4755   7551   4787    -84    -28   1301       C  
ATOM   1550  CD  GLU A 201     -15.361  17.305  -7.454  1.00 43.05           C  
ANISOU 1550  CD  GLU A 201     4480   7320   4556    -38      4   1272       C  
ATOM   1551  OE1 GLU A 201     -15.302  18.110  -8.482  1.00 33.78           O  
ANISOU 1551  OE1 GLU A 201     3277   6140   3417      2     23   1261       O  
ATOM   1552  OE2 GLU A 201     -15.279  17.599  -6.225  1.00 42.97           O1-
ANISOU 1552  OE2 GLU A 201     4474   7331   4522    -44      4   1265       O1-
ATOM   1553  N   GLU A 202     -13.812  12.180  -7.933  1.00 47.62           N  
ANISOU 1553  N   GLU A 202     5217   7716   5159   -129   -204   1328       N  
ATOM   1554  CA  GLU A 202     -13.797  10.838  -8.421  1.00 52.62           C  
ANISOU 1554  CA  GLU A 202     5886   8295   5810   -143   -283   1330       C  
ATOM   1555  C   GLU A 202     -14.930  10.515  -9.397  1.00 54.22           C  
ANISOU 1555  C   GLU A 202     6071   8509   6019   -150   -298   1332       C  
ATOM   1556  O   GLU A 202     -14.849   9.489 -10.120  1.00 65.24           O  
ANISOU 1556  O   GLU A 202     7496   9853   7439   -136   -375   1314       O  
ATOM   1557  CB  GLU A 202     -13.785   9.886  -7.216  1.00 58.15           C  
ANISOU 1557  CB  GLU A 202     6620   8967   6507   -215   -338   1375       C  
ATOM   1558  CG  GLU A 202     -12.597  10.149  -6.267  1.00 63.76           C  
ANISOU 1558  CG  GLU A 202     7352   9660   7211   -202   -329   1368       C  
ATOM   1559  CD  GLU A 202     -12.386   9.029  -5.255  1.00 64.27           C  
ANISOU 1559  CD  GLU A 202     7457   9684   7276   -265   -400   1412       C  
ATOM   1560  OE1 GLU A 202     -12.780   9.214  -4.097  1.00 60.71           O  
ANISOU 1560  OE1 GLU A 202     6994   9282   6790   -315   -377   1456       O  
ATOM   1561  OE2 GLU A 202     -11.858   7.978  -5.647  1.00 65.26           O1-
ANISOU 1561  OE2 GLU A 202     7624   9734   7435   -259   -483   1400       O1-
ATOM   1562  N   GLN A 203     -15.970  11.362  -9.419  1.00 51.35           N  
ANISOU 1562  N   GLN A 203     5663   8212   5636   -165   -235   1345       N  
ATOM   1563  CA  GLN A 203     -17.082  11.279 -10.389  1.00 50.48           C  
ANISOU 1563  CA  GLN A 203     5528   8122   5530   -166   -237   1343       C  
ATOM   1564  C   GLN A 203     -16.802  12.072 -11.690  1.00 48.25           C  
ANISOU 1564  C   GLN A 203     5222   7857   5253    -82   -197   1297       C  
ATOM   1565  O   GLN A 203     -15.935  12.945 -11.739  1.00 49.21           O  
ANISOU 1565  O   GLN A 203     5332   7991   5374    -34   -153   1279       O  
ATOM   1566  CB  GLN A 203     -18.375  11.853  -9.780  1.00 56.62           C  
ANISOU 1566  CB  GLN A 203     6260   8973   6277   -219   -186   1382       C  
ATOM   1567  CG  GLN A 203     -18.999  11.047  -8.644  1.00 68.90           C  
ANISOU 1567  CG  GLN A 203     7817  10544   7817   -309   -221   1450       C  
ATOM   1568  CD  GLN A 203     -18.340  11.273  -7.279  1.00 83.86           C  
ANISOU 1568  CD  GLN A 203     9720  12460   9682   -326   -202   1468       C  
ATOM   1569  NE2 GLN A 203     -18.548  10.308  -6.388  1.00 94.59           N  
ANISOU 1569  NE2 GLN A 203    11089  13815  11033   -400   -253   1534       N  
ATOM   1570  OE1 GLN A 203     -17.650  12.284  -7.017  1.00 83.07           O  
ANISOU 1570  OE1 GLN A 203     9616  12377   9570   -273   -150   1428       O  
ATOM   1571  N   GLN A 204     -17.595  11.737 -12.704  1.00 45.70           N  
ANISOU 1571  N   GLN A 204     4889   7537   4936    -71   -220   1285       N  
ATOM   1572  CA  GLN A 204     -17.701  12.384 -13.971  1.00 46.98           C  
ANISOU 1572  CA  GLN A 204     5021   7732   5095     -3   -186   1254       C  
ATOM   1573  C   GLN A 204     -18.642  13.514 -13.756  1.00 44.75           C  
ANISOU 1573  C   GLN A 204     4692   7509   4799    -25   -112   1272       C  
ATOM   1574  O   GLN A 204     -19.563  13.350 -12.989  1.00 44.23           O  
ANISOU 1574  O   GLN A 204     4619   7461   4723    -91   -111   1303       O  
ATOM   1575  CB  GLN A 204     -18.306  11.440 -15.017  1.00 50.05           C  
ANISOU 1575  CB  GLN A 204     5423   8097   5495     14   -254   1231       C  
ATOM   1576  CG  GLN A 204     -17.595  10.090 -15.158  1.00 49.08           C  
ANISOU 1576  CG  GLN A 204     5353   7903   5392     33   -358   1205       C  
ATOM   1577  CD  GLN A 204     -16.380  10.224 -16.055  1.00 50.71           C  
ANISOU 1577  CD  GLN A 204     5559   8123   5583    140   -357   1154       C  
ATOM   1578  NE2 GLN A 204     -15.783   9.070 -16.455  1.00 43.41           N  
ANISOU 1578  NE2 GLN A 204     4676   7148   4669    187   -456   1110       N  
ATOM   1579  OE1 GLN A 204     -15.989  11.367 -16.409  1.00 43.05           O  
ANISOU 1579  OE1 GLN A 204     4548   7215   4594    184   -274   1158       O  
ATOM   1580  N   ASN A 205     -18.464  14.626 -14.484  1.00 40.85           N  
ANISOU 1580  N   ASN A 205     4163   7052   4304     30    -57   1257       N  
ATOM   1581  CA  ASN A 205     -19.210  15.853 -14.196  1.00 40.37           C  
ANISOU 1581  CA  ASN A 205     4060   7041   4237     19      5   1266       C  
ATOM   1582  C   ASN A 205     -19.567  16.595 -15.441  1.00 38.80           C  
ANISOU 1582  C   ASN A 205     3824   6875   4043     69     35   1255       C  
ATOM   1583  O   ASN A 205     -18.685  16.887 -16.260  1.00 36.72           O  
ANISOU 1583  O   ASN A 205     3550   6613   3788    128     41   1250       O  
ATOM   1584  CB  ASN A 205     -18.425  16.775 -13.228  1.00 39.63           C  
ANISOU 1584  CB  ASN A 205     3960   6946   4149     23     36   1270       C  
ATOM   1585  CG  ASN A 205     -19.196  18.032 -12.839  1.00 41.49           C  
ANISOU 1585  CG  ASN A 205     4156   7227   4381     21     82   1266       C  
ATOM   1586  ND2 ASN A 205     -18.613  18.786 -11.988  1.00 43.56           N  
ANISOU 1586  ND2 ASN A 205     4415   7483   4651     29     93   1261       N  
ATOM   1587  OD1 ASN A 205     -20.296  18.335 -13.335  1.00 42.54           O  
ANISOU 1587  OD1 ASN A 205     4259   7397   4505     19    102   1263       O  
ATOM   1588  N   PHE A 206     -20.885  16.799 -15.659  1.00 42.03           N  
ANISOU 1588  N   PHE A 206     4208   7317   4443     47     52   1256       N  
ATOM   1589  CA  PHE A 206     -21.357  17.777 -16.641  1.00 40.32           C  
ANISOU 1589  CA  PHE A 206     3949   7138   4231     88     89   1249       C  
ATOM   1590  C   PHE A 206     -21.753  18.977 -15.817  1.00 39.71           C  
ANISOU 1590  C   PHE A 206     3842   7087   4156     74    131   1252       C  
ATOM   1591  O   PHE A 206     -22.709  18.902 -15.006  1.00 39.97           O  
ANISOU 1591  O   PHE A 206     3868   7149   4169     29    138   1253       O  
ATOM   1592  CB  PHE A 206     -22.543  17.287 -17.472  1.00 41.66           C  
ANISOU 1592  CB  PHE A 206     4110   7327   4392     82     74   1241       C  
ATOM   1593  CG  PHE A 206     -22.158  16.326 -18.537  1.00 41.52           C  
ANISOU 1593  CG  PHE A 206     4115   7287   4373    125     25   1222       C  
ATOM   1594  CD1 PHE A 206     -21.371  16.728 -19.558  1.00 42.43           C  
ANISOU 1594  CD1 PHE A 206     4214   7423   4483    200     38   1214       C  
ATOM   1595  CD2 PHE A 206     -22.590  15.028 -18.499  1.00 42.60           C  
ANISOU 1595  CD2 PHE A 206     4284   7387   4512     93    -41   1215       C  
ATOM   1596  CE1 PHE A 206     -21.011  15.865 -20.581  1.00 45.43           C  
ANISOU 1596  CE1 PHE A 206     4610   7802   4849    259     -9   1185       C  
ATOM   1597  CE2 PHE A 206     -22.217  14.133 -19.472  1.00 43.73           C  
ANISOU 1597  CE2 PHE A 206     4452   7507   4656    147   -103   1182       C  
ATOM   1598  CZ  PHE A 206     -21.419  14.548 -20.531  1.00 45.74           C  
ANISOU 1598  CZ  PHE A 206     4689   7795   4892    238    -84   1161       C  
ATOM   1599  N   PHE A 207     -21.087  20.079 -16.097  1.00 39.68           N  
ANISOU 1599  N   PHE A 207     3814   7082   4178    116    152   1255       N  
ATOM   1600  CA  PHE A 207     -21.095  21.298 -15.332  1.00 42.02           C  
ANISOU 1600  CA  PHE A 207     4088   7382   4493    118    170   1249       C  
ATOM   1601  C   PHE A 207     -21.824  22.326 -16.154  1.00 40.93           C  
ANISOU 1601  C   PHE A 207     3907   7269   4373    147    189   1247       C  
ATOM   1602  O   PHE A 207     -21.330  22.798 -17.123  1.00 43.46           O  
ANISOU 1602  O   PHE A 207     4206   7585   4719    182    192   1270       O  
ATOM   1603  CB  PHE A 207     -19.637  21.683 -15.112  1.00 40.89           C  
ANISOU 1603  CB  PHE A 207     3954   7198   4385    139    157   1263       C  
ATOM   1604  CG  PHE A 207     -19.416  22.940 -14.351  1.00 42.40           C  
ANISOU 1604  CG  PHE A 207     4125   7374   4610    151    153   1253       C  
ATOM   1605  CD1 PHE A 207     -19.389  24.135 -14.979  1.00 42.41           C  
ANISOU 1605  CD1 PHE A 207     4086   7368   4658    182    151   1267       C  
ATOM   1606  CD2 PHE A 207     -19.151  22.907 -13.030  1.00 46.38           C  
ANISOU 1606  CD2 PHE A 207     4653   7863   5106    136    139   1234       C  
ATOM   1607  CE1 PHE A 207     -19.158  25.284 -14.300  1.00 44.95           C  
ANISOU 1607  CE1 PHE A 207     4393   7659   5026    196    126   1255       C  
ATOM   1608  CE2 PHE A 207     -18.918  24.049 -12.340  1.00 47.55           C  
ANISOU 1608  CE2 PHE A 207     4786   7988   5290    158    119   1215       C  
ATOM   1609  CZ  PHE A 207     -18.922  25.241 -12.978  1.00 47.90           C  
ANISOU 1609  CZ  PHE A 207     4793   8016   5389    189    107   1223       C  
ATOM   1610  N   ALA A 208     -23.031  22.657 -15.748  1.00 43.65           N  
ANISOU 1610  N   ALA A 208     4235   7651   4698    131    202   1225       N  
ATOM   1611  CA  ALA A 208     -23.953  23.343 -16.571  1.00 44.65           C  
ANISOU 1611  CA  ALA A 208     4325   7805   4832    151    217   1219       C  
ATOM   1612  C   ALA A 208     -24.178  24.772 -16.066  1.00 50.31           C  
ANISOU 1612  C   ALA A 208     5013   8523   5578    177    214   1196       C  
ATOM   1613  O   ALA A 208     -24.837  25.032 -15.005  1.00 48.62           O  
ANISOU 1613  O   ALA A 208     4793   8342   5338    171    215   1161       O  
ATOM   1614  CB  ALA A 208     -25.241  22.582 -16.647  1.00 46.18           C  
ANISOU 1614  CB  ALA A 208     4517   8043   4986    120    226   1210       C  
ATOM   1615  N   GLN A 209     -23.647  25.693 -16.868  1.00 44.33           N  
ANISOU 1615  N   GLN A 209     4231   7736   4873    210    204   1219       N  
ATOM   1616  CA  GLN A 209     -23.626  27.086 -16.508  1.00 43.89           C  
ANISOU 1616  CA  GLN A 209     4151   7657   4868    237    178   1203       C  
ATOM   1617  C   GLN A 209     -24.955  27.702 -16.893  1.00 45.31           C  
ANISOU 1617  C   GLN A 209     4300   7873   5042    253    185   1175       C  
ATOM   1618  O   GLN A 209     -25.526  27.476 -18.050  1.00 36.71           O  
ANISOU 1618  O   GLN A 209     3195   6809   3944    254    206   1196       O  
ATOM   1619  CB  GLN A 209     -22.439  27.770 -17.168  1.00 44.85           C  
ANISOU 1619  CB  GLN A 209     4254   7727   5058    255    153   1258       C  
ATOM   1620  CG  GLN A 209     -22.233  29.206 -16.750  1.00 47.96           C  
ANISOU 1620  CG  GLN A 209     4623   8071   5525    278    101   1250       C  
ATOM   1621  CD  GLN A 209     -21.877  29.400 -15.270  1.00 48.35           C  
ANISOU 1621  CD  GLN A 209     4699   8092   5579    283     68   1199       C  
ATOM   1622  NE2 GLN A 209     -21.864  30.672 -14.854  1.00 47.23           N  
ANISOU 1622  NE2 GLN A 209     4538   7903   5503    315      6   1173       N  
ATOM   1623  OE1 GLN A 209     -21.585  28.443 -14.522  1.00 45.75           O  
ANISOU 1623  OE1 GLN A 209     4404   7779   5199    263     88   1184       O  
ATOM   1624  N   ILE A 210     -25.447  28.466 -15.909  1.00 48.63           N  
ANISOU 1624  N   ILE A 210     4711   8301   5465    273    163   1122       N  
ATOM   1625  CA  ILE A 210     -26.805  29.029 -15.924  1.00 47.81           C  
ANISOU 1625  CA  ILE A 210     4578   8246   5342    295    166   1076       C  
ATOM   1626  C   ILE A 210     -26.800  30.561 -15.951  1.00 52.64           C  
ANISOU 1626  C   ILE A 210     5163   8812   6025    344    110   1050       C  
ATOM   1627  O   ILE A 210     -27.419  31.140 -16.829  1.00 50.70           O  
ANISOU 1627  O   ILE A 210     4889   8566   5805    359    105   1057       O  
ATOM   1628  CB  ILE A 210     -27.574  28.550 -14.695  1.00 49.52           C  
ANISOU 1628  CB  ILE A 210     4795   8536   5482    290    184   1027       C  
ATOM   1629  CG1 ILE A 210     -28.082  27.123 -14.932  1.00 48.88           C  
ANISOU 1629  CG1 ILE A 210     4724   8505   5340    235    229   1060       C  
ATOM   1630  CG2 ILE A 210     -28.761  29.460 -14.419  1.00 50.95           C  
ANISOU 1630  CG2 ILE A 210     4938   8770   5649    335    172    965       C  
ATOM   1631  CD1 ILE A 210     -28.232  26.363 -13.631  1.00 52.12           C  
ANISOU 1631  CD1 ILE A 210     5144   8974   5685    209    241   1051       C  
ATOM   1632  N   LYS A 211     -26.120  31.208 -14.983  1.00 53.69           N  
ANISOU 1632  N   LYS A 211     5305   8900   6193    370     58   1019       N  
ATOM   1633  CA  LYS A 211     -26.050  32.675 -14.932  1.00 51.63           C  
ANISOU 1633  CA  LYS A 211     5023   8577   6016    419    -19    990       C  
ATOM   1634  C   LYS A 211     -24.637  33.146 -14.691  1.00 51.13           C  
ANISOU 1634  C   LYS A 211     4971   8421   6035    418    -78   1025       C  
ATOM   1635  O   LYS A 211     -23.953  32.651 -13.816  1.00 50.61           O  
ANISOU 1635  O   LYS A 211     4933   8351   5946    410    -76   1013       O  
ATOM   1636  CB  LYS A 211     -26.884  33.245 -13.802  1.00 55.33           C  
ANISOU 1636  CB  LYS A 211     5483   9089   6449    477    -53    886       C  
ATOM   1637  CG  LYS A 211     -26.836  34.775 -13.718  1.00 58.91           C  
ANISOU 1637  CG  LYS A 211     5918   9465   6998    538   -157    841       C  
ATOM   1638  CD  LYS A 211     -27.814  35.344 -12.663  1.00 67.56           C  
ANISOU 1638  CD  LYS A 211     7000  10623   8044    616   -194    720       C  
ATOM   1639  CE  LYS A 211     -28.524  36.626 -13.158  1.00 71.33           C  
ANISOU 1639  CE  LYS A 211     7449  11063   8591    673   -270    676       C  
ATOM   1640  NZ  LYS A 211     -27.691  37.807 -12.808  1.00 70.57           N1+
ANISOU 1640  NZ  LYS A 211     7357  10841   8612    717   -399    650       N1+
ATOM   1641  N   GLY A 212     -24.225  34.180 -15.423  1.00 50.71           N  
ANISOU 1641  N   GLY A 212     4891   8292   6085    426   -140   1071       N  
ATOM   1642  CA  GLY A 212     -22.899  34.730 -15.259  1.00 53.09           C  
ANISOU 1642  CA  GLY A 212     5191   8499   6479    420   -208   1119       C  
ATOM   1643  C   GLY A 212     -21.835  33.854 -15.909  1.00 51.28           C  
ANISOU 1643  C   GLY A 212     4965   8276   6242    369   -155   1218       C  
ATOM   1644  O   GLY A 212     -22.151  32.888 -16.651  1.00 49.89           O  
ANISOU 1644  O   GLY A 212     4791   8168   5995    345    -74   1249       O  
ATOM   1645  N   TYR A 213     -20.589  34.200 -15.623  1.00 51.67           N  
ANISOU 1645  N   TYR A 213     5012   8254   6365    359   -208   1263       N  
ATOM   1646  CA  TYR A 213     -19.432  33.664 -16.356  1.00 51.45           C  
ANISOU 1646  CA  TYR A 213     4970   8228   6350    321   -177   1370       C  
ATOM   1647  C   TYR A 213     -18.401  33.124 -15.362  1.00 52.29           C  
ANISOU 1647  C   TYR A 213     5110   8308   6447    312   -184   1356       C  
ATOM   1648  O   TYR A 213     -18.065  33.791 -14.386  1.00 48.39           O  
ANISOU 1648  O   TYR A 213     4627   7747   6009    331   -259   1312       O  
ATOM   1649  CB  TYR A 213     -18.817  34.756 -17.230  1.00 55.40           C  
ANISOU 1649  CB  TYR A 213     5412   8671   6967    311   -243   1475       C  
ATOM   1650  CG  TYR A 213     -19.721  35.106 -18.424  1.00 57.06           C  
ANISOU 1650  CG  TYR A 213     5585   8921   7174    315   -222   1511       C  
ATOM   1651  CD1 TYR A 213     -19.592  34.420 -19.606  1.00 60.09           C  
ANISOU 1651  CD1 TYR A 213     5943   9382   7504    299   -148   1589       C  
ATOM   1652  CD2 TYR A 213     -20.740  36.079 -18.322  1.00 66.91           C  
ANISOU 1652  CD2 TYR A 213     6824  10134   8464    343   -279   1455       C  
ATOM   1653  CE1 TYR A 213     -20.408  34.674 -20.682  1.00 66.62           C  
ANISOU 1653  CE1 TYR A 213     6739  10253   8320    307   -127   1618       C  
ATOM   1654  CE2 TYR A 213     -21.581  36.361 -19.389  1.00 65.07           C  
ANISOU 1654  CE2 TYR A 213     6559   9937   8225    347   -260   1485       C  
ATOM   1655  CZ  TYR A 213     -21.402  35.653 -20.586  1.00 72.35           C  
ANISOU 1655  CZ  TYR A 213     7457  10938   9094    326   -181   1571       C  
ATOM   1656  OH  TYR A 213     -22.185  35.882 -21.726  1.00 76.84           O  
ANISOU 1656  OH  TYR A 213     7992  11551   9651    332   -159   1607       O  
ATOM   1657  N   LYS A 214     -17.975  31.881 -15.582  1.00 46.90           N  
ANISOU 1657  N   LYS A 214     4448   7680   5692    288   -111   1382       N  
ATOM   1658  CA  LYS A 214     -16.941  31.270 -14.810  1.00 46.91           C  
ANISOU 1658  CA  LYS A 214     4479   7661   5683    276   -112   1381       C  
ATOM   1659  C   LYS A 214     -15.772  30.849 -15.702  1.00 47.73           C  
ANISOU 1659  C   LYS A 214     4554   7778   5801    256    -90   1485       C  
ATOM   1660  O   LYS A 214     -15.952  30.247 -16.738  1.00 49.97           O  
ANISOU 1660  O   LYS A 214     4822   8128   6035    255    -35   1524       O  
ATOM   1661  CB  LYS A 214     -17.428  30.007 -14.123  1.00 45.35           C  
ANISOU 1661  CB  LYS A 214     4335   7520   5377    269    -53   1314       C  
ATOM   1662  CG  LYS A 214     -18.097  30.236 -12.815  1.00 47.28           C  
ANISOU 1662  CG  LYS A 214     4607   7762   5593    291    -77   1218       C  
ATOM   1663  CD  LYS A 214     -18.838  28.983 -12.329  1.00 47.80           C  
ANISOU 1663  CD  LYS A 214     4708   7904   5547    274    -13   1175       C  
ATOM   1664  CE  LYS A 214     -19.280  29.244 -10.902  1.00 47.19           C  
ANISOU 1664  CE  LYS A 214     4650   7843   5437    301    -40   1092       C  
ATOM   1665  NZ  LYS A 214     -19.972  28.067 -10.321  1.00 51.95           N1+
ANISOU 1665  NZ  LYS A 214     5276   8527   5934    278     15   1068       N1+
ATOM   1666  N   ARG A 215     -14.572  31.128 -15.235  1.00 45.50           N  
ANISOU 1666  N   ARG A 215     4266   7441   5581    248   -137   1522       N  
ATOM   1667  CA  ARG A 215     -13.399  30.609 -15.848  1.00 46.00           C  
ANISOU 1667  CA  ARG A 215     4303   7531   5643    235   -114   1609       C  
ATOM   1668  C   ARG A 215     -13.000  29.333 -15.148  1.00 44.90           C  
ANISOU 1668  C   ARG A 215     4220   7411   5426    232    -75   1558       C  
ATOM   1669  O   ARG A 215     -12.847  29.298 -13.889  1.00 46.41           O  
ANISOU 1669  O   ARG A 215     4456   7554   5622    230   -106   1495       O  
ATOM   1670  CB  ARG A 215     -12.298  31.591 -15.684  1.00 49.96           C  
ANISOU 1670  CB  ARG A 215     4761   7961   6260    223   -192   1683       C  
ATOM   1671  CG  ARG A 215     -11.035  31.214 -16.416  1.00 52.13           C  
ANISOU 1671  CG  ARG A 215     4988   8279   6539    212   -171   1793       C  
ATOM   1672  CD  ARG A 215      -9.896  31.882 -15.709  1.00 55.45           C  
ANISOU 1672  CD  ARG A 215     5390   8615   7062    194   -251   1835       C  
ATOM   1673  NE  ARG A 215      -8.656  31.836 -16.447  1.00 59.25           N  
ANISOU 1673  NE  ARG A 215     5802   9139   7571    180   -246   1964       N  
ATOM   1674  CZ  ARG A 215      -7.555  32.478 -16.051  1.00 61.33           C  
ANISOU 1674  CZ  ARG A 215     6028   9336   7938    157   -320   2034       C  
ATOM   1675  NH1 ARG A 215      -7.570  33.209 -14.944  1.00 59.76           N1+
ANISOU 1675  NH1 ARG A 215     5863   9018   7825    151   -410   1976       N1+
ATOM   1676  NH2 ARG A 215      -6.435  32.409 -16.775  1.00 61.81           N  
ANISOU 1676  NH2 ARG A 215     6013   9456   8015    145   -310   2164       N  
ATOM   1677  N   CYS A 216     -12.836  28.292 -15.966  1.00 42.82           N  
ANISOU 1677  N   CYS A 216     3956   7221   5092    236    -16   1585       N  
ATOM   1678  CA  CYS A 216     -12.548  26.945 -15.503  1.00 43.21           C  
ANISOU 1678  CA  CYS A 216     4059   7291   5065    235     15   1540       C  
ATOM   1679  C   CYS A 216     -11.187  26.550 -16.105  1.00 45.87           C  
ANISOU 1679  C   CYS A 216     4363   7657   5405    246     21   1614       C  
ATOM   1680  O   CYS A 216     -11.015  26.568 -17.342  1.00 42.95           O  
ANISOU 1680  O   CYS A 216     3940   7355   5023    267     44   1679       O  
ATOM   1681  CB  CYS A 216     -13.585  25.989 -16.017  1.00 42.73           C  
ANISOU 1681  CB  CYS A 216     4025   7290   4919    241     64   1498       C  
ATOM   1682  SG  CYS A 216     -15.273  26.442 -15.611  1.00 45.30           S  
ANISOU 1682  SG  CYS A 216     4368   7613   5231    232     69   1429       S  
ATOM   1683  N   ILE A 217     -10.223  26.276 -15.225  1.00 45.44           N  
ANISOU 1683  N   ILE A 217     4335   7562   5369    237     -3   1605       N  
ATOM   1684  CA  ILE A 217      -8.893  25.778 -15.576  1.00 40.78           C  
ANISOU 1684  CA  ILE A 217     3719   7001   4773    251      0   1662       C  
ATOM   1685  C   ILE A 217      -8.728  24.349 -15.059  1.00 42.39           C  
ANISOU 1685  C   ILE A 217     3992   7212   4902    256     16   1594       C  
ATOM   1686  O   ILE A 217      -8.834  24.056 -13.831  1.00 42.66           O  
ANISOU 1686  O   ILE A 217     4087   7189   4933    234     -2   1533       O  
ATOM   1687  CB  ILE A 217      -7.823  26.593 -14.910  1.00 45.15           C  
ANISOU 1687  CB  ILE A 217     4247   7488   5417    233    -54   1708       C  
ATOM   1688  CG1 ILE A 217      -8.062  28.100 -15.157  1.00 47.38           C  
ANISOU 1688  CG1 ILE A 217     4472   7731   5798    218   -100   1766       C  
ATOM   1689  CG2 ILE A 217      -6.471  26.189 -15.446  1.00 44.00           C  
ANISOU 1689  CG2 ILE A 217     4056   7394   5268    249    -47   1783       C  
ATOM   1690  CD1 ILE A 217      -7.206  28.952 -14.232  1.00 52.62           C  
ANISOU 1690  CD1 ILE A 217     5127   8300   6566    198   -178   1787       C  
ATOM   1691  N   LEU A 218      -8.490  23.460 -16.016  1.00 40.09           N  
ANISOU 1691  N   LEU A 218     3689   6995   4549    291     45   1607       N  
ATOM   1692  CA  LEU A 218      -8.420  22.026 -15.779  1.00 40.79           C  
ANISOU 1692  CA  LEU A 218     3838   7090   4567    305     49   1544       C  
ATOM   1693  C   LEU A 218      -6.996  21.553 -15.945  1.00 41.01           C  
ANISOU 1693  C   LEU A 218     3847   7146   4590    336     38   1576       C  
ATOM   1694  O   LEU A 218      -6.270  22.107 -16.708  1.00 43.32           O  
ANISOU 1694  O   LEU A 218     4064   7493   4901    362     46   1653       O  
ATOM   1695  CB  LEU A 218      -9.334  21.317 -16.801  1.00 42.17           C  
ANISOU 1695  CB  LEU A 218     4018   7327   4676    335     74   1516       C  
ATOM   1696  CG  LEU A 218     -10.755  21.148 -16.276  1.00 39.85           C  
ANISOU 1696  CG  LEU A 218     3775   6998   4368    297     78   1456       C  
ATOM   1697  CD1 LEU A 218     -11.385  22.461 -15.877  1.00 43.47           C  
ANISOU 1697  CD1 LEU A 218     4210   7426   4880    267     80   1470       C  
ATOM   1698  CD2 LEU A 218     -11.591  20.406 -17.247  1.00 39.43           C  
ANISOU 1698  CD2 LEU A 218     3728   6994   4258    324     90   1429       C  
ATOM   1699  N   PHE A 219      -6.594  20.536 -15.203  1.00 41.31           N  
ANISOU 1699  N   PHE A 219     3946   7149   4601    333     18   1523       N  
ATOM   1700  CA  PHE A 219      -5.328  19.907 -15.392  1.00 45.16           C  
ANISOU 1700  CA  PHE A 219     4421   7667   5070    373      6   1538       C  
ATOM   1701  C   PHE A 219      -5.594  18.411 -15.438  1.00 45.89           C  
ANISOU 1701  C   PHE A 219     4579   7762   5094    398    -10   1461       C  
ATOM   1702  O   PHE A 219      -6.428  17.890 -14.641  1.00 45.35           O  
ANISOU 1702  O   PHE A 219     4581   7630   5018    355    -26   1405       O  
ATOM   1703  CB  PHE A 219      -4.360  20.240 -14.237  1.00 44.80           C  
ANISOU 1703  CB  PHE A 219     4389   7553   5081    341    -22   1551       C  
ATOM   1704  CG  PHE A 219      -4.219  21.723 -13.951  1.00 44.38           C  
ANISOU 1704  CG  PHE A 219     4284   7463   5113    307    -31   1613       C  
ATOM   1705  CD1 PHE A 219      -5.086  22.367 -13.067  1.00 44.97           C  
ANISOU 1705  CD1 PHE A 219     4394   7466   5223    264    -45   1578       C  
ATOM   1706  CD2 PHE A 219      -3.205  22.457 -14.547  1.00 43.97           C  
ANISOU 1706  CD2 PHE A 219     4146   7453   5107    322    -36   1709       C  
ATOM   1707  CE1 PHE A 219      -4.948  23.724 -12.788  1.00 49.33           C  
ANISOU 1707  CE1 PHE A 219     4905   7973   5863    242    -74   1623       C  
ATOM   1708  CE2 PHE A 219      -3.081  23.808 -14.305  1.00 45.63           C  
ANISOU 1708  CE2 PHE A 219     4309   7615   5411    287    -63   1771       C  
ATOM   1709  CZ  PHE A 219      -3.917  24.447 -13.401  1.00 45.38           C  
ANISOU 1709  CZ  PHE A 219     4322   7496   5423    249    -89   1722       C  
ATOM   1710  N   PRO A 220      -4.889  17.705 -16.336  1.00 45.83           N  
ANISOU 1710  N   PRO A 220     4545   7828   5037    470    -16   1459       N  
ATOM   1711  CA  PRO A 220      -5.117  16.287 -16.469  1.00 44.47           C  
ANISOU 1711  CA  PRO A 220     4436   7650   4811    504    -53   1381       C  
ATOM   1712  C   PRO A 220      -4.562  15.482 -15.335  1.00 47.61           C  
ANISOU 1712  C   PRO A 220     4902   7967   5220    478    -98   1340       C  
ATOM   1713  O   PRO A 220      -3.753  15.989 -14.513  1.00 46.62           O  
ANISOU 1713  O   PRO A 220     4770   7806   5137    447    -97   1372       O  
ATOM   1714  CB  PRO A 220      -4.459  15.910 -17.803  1.00 45.46           C  
ANISOU 1714  CB  PRO A 220     4502   7893   4878    607    -51   1387       C  
ATOM   1715  CG  PRO A 220      -3.604  17.069 -18.186  1.00 46.35           C  
ANISOU 1715  CG  PRO A 220     4518   8077   5016    618    -11   1486       C  
ATOM   1716  CD  PRO A 220      -4.152  18.265 -17.487  1.00 49.31           C  
ANISOU 1716  CD  PRO A 220     4888   8380   5465    530      9   1532       C  
ATOM   1717  N   PRO A 221      -5.017  14.219 -15.250  1.00 47.59           N  
ANISOU 1717  N   PRO A 221     4967   7928   5186    485   -146   1271       N  
ATOM   1718  CA  PRO A 221      -4.677  13.470 -14.055  1.00 45.53           C  
ANISOU 1718  CA  PRO A 221     4776   7580   4941    443   -194   1241       C  
ATOM   1719  C   PRO A 221      -3.177  13.187 -13.941  1.00 46.90           C  
ANISOU 1719  C   PRO A 221     4938   7767   5113    491   -216   1242       C  
ATOM   1720  O   PRO A 221      -2.647  12.954 -12.840  1.00 43.94           O  
ANISOU 1720  O   PRO A 221     4606   7324   4765    452   -242   1236       O  
ATOM   1721  CB  PRO A 221      -5.488  12.186 -14.220  1.00 45.22           C  
ANISOU 1721  CB  PRO A 221     4799   7504   4877    445   -254   1180       C  
ATOM   1722  CG  PRO A 221      -6.690  12.603 -15.020  1.00 46.23           C  
ANISOU 1722  CG  PRO A 221     4900   7672   4992    443   -221   1186       C  
ATOM   1723  CD  PRO A 221      -6.164  13.623 -15.977  1.00 45.16           C  
ANISOU 1723  CD  PRO A 221     4680   7633   4846    501   -163   1230       C  
ATOM   1724  N   ASP A 222      -2.491  13.253 -15.068  1.00 45.92           N  
ANISOU 1724  N   ASP A 222     4749   7741   4955    579   -204   1253       N  
ATOM   1725  CA  ASP A 222      -1.083  12.964 -15.084  1.00 44.81           C  
ANISOU 1725  CA  ASP A 222     4585   7635   4804    636   -224   1256       C  
ATOM   1726  C   ASP A 222      -0.295  14.169 -14.567  1.00 46.36           C  
ANISOU 1726  C   ASP A 222     4725   7834   5053    596   -182   1338       C  
ATOM   1727  O   ASP A 222       0.906  14.138 -14.593  1.00 49.21           O  
ANISOU 1727  O   ASP A 222     5050   8234   5413    636   -189   1359       O  
ATOM   1728  CB  ASP A 222      -0.590  12.517 -16.465  1.00 44.49           C  
ANISOU 1728  CB  ASP A 222     4488   7720   4695    759   -231   1236       C  
ATOM   1729  CG  ASP A 222      -0.546  13.666 -17.475  1.00 50.85           C  
ANISOU 1729  CG  ASP A 222     5185   8648   5487    787   -160   1319       C  
ATOM   1730  OD1 ASP A 222      -0.664  14.854 -17.111  1.00 57.19           O  
ANISOU 1730  OD1 ASP A 222     5951   9431   6346    716   -114   1398       O  
ATOM   1731  OD2 ASP A 222      -0.370  13.405 -18.657  1.00 55.65           O1-
ANISOU 1731  OD2 ASP A 222     5739   9376   6028    887   -157   1310       O1-
ATOM   1732  N   GLN A 223      -0.960  15.178 -14.060  1.00 46.94           N  
ANISOU 1732  N   GLN A 223     4791   7867   5176    522   -147   1381       N  
ATOM   1733  CA  GLN A 223      -0.258  16.273 -13.470  1.00 47.35           C  
ANISOU 1733  CA  GLN A 223     4804   7891   5293    479   -132   1447       C  
ATOM   1734  C   GLN A 223      -0.283  16.159 -11.993  1.00 43.87           C  
ANISOU 1734  C   GLN A 223     4440   7339   4889    413   -162   1413       C  
ATOM   1735  O   GLN A 223       0.075  17.084 -11.336  1.00 46.22           O  
ANISOU 1735  O   GLN A 223     4720   7593   5248    370   -159   1452       O  
ATOM   1736  CB  GLN A 223      -0.898  17.588 -13.808  1.00 47.96           C  
ANISOU 1736  CB  GLN A 223     4828   7977   5414    441    -94   1509       C  
ATOM   1737  CG  GLN A 223      -1.100  17.818 -15.258  1.00 58.55           C  
ANISOU 1737  CG  GLN A 223     6097   9427   6722    491    -60   1549       C  
ATOM   1738  CD  GLN A 223      -0.010  18.623 -15.842  1.00 63.35           C  
ANISOU 1738  CD  GLN A 223     6603  10121   7343    527    -46   1640       C  
ATOM   1739  NE2 GLN A 223       0.891  17.962 -16.489  1.00 65.56           N  
ANISOU 1739  NE2 GLN A 223     6862  10485   7563    604    -53   1626       N  
ATOM   1740  OE1 GLN A 223       0.027  19.820 -15.705  1.00 67.56           O  
ANISOU 1740  OE1 GLN A 223     7073  10653   7943    490    -35   1727       O  
ATOM   1741  N   PHE A 224      -0.738  15.039 -11.472  1.00 43.04           N  
ANISOU 1741  N   PHE A 224     4416   7184   4751    402   -196   1346       N  
ATOM   1742  CA  PHE A 224      -0.663  14.807 -10.039  1.00 42.11           C  
ANISOU 1742  CA  PHE A 224     4367   6976   4657    344   -226   1322       C  
ATOM   1743  C   PHE A 224       0.635  15.354  -9.367  1.00 43.37           C  
ANISOU 1743  C   PHE A 224     4504   7111   4864    342   -238   1354       C  
ATOM   1744  O   PHE A 224       0.549  16.035  -8.320  1.00 39.65           O  
ANISOU 1744  O   PHE A 224     4050   6581   4434    292   -241   1361       O  
ATOM   1745  CB  PHE A 224      -0.807  13.352  -9.782  1.00 39.00           C  
ANISOU 1745  CB  PHE A 224     4046   6545   4225    349   -278   1263       C  
ATOM   1746  CG  PHE A 224      -0.880  12.995  -8.337  1.00 41.93           C  
ANISOU 1746  CG  PHE A 224     4486   6833   4609    286   -309   1246       C  
ATOM   1747  CD1 PHE A 224       0.295  12.847  -7.569  1.00 44.27           C  
ANISOU 1747  CD1 PHE A 224     4800   7093   4926    289   -339   1245       C  
ATOM   1748  CD2 PHE A 224      -2.073  12.723  -7.751  1.00 40.13           C  
ANISOU 1748  CD2 PHE A 224     4304   6575   4368    227   -313   1235       C  
ATOM   1749  CE1 PHE A 224       0.232  12.443  -6.241  1.00 42.48           C  
ANISOU 1749  CE1 PHE A 224     4637   6798   4703    235   -371   1231       C  
ATOM   1750  CE2 PHE A 224      -2.153  12.338  -6.419  1.00 44.00           C  
ANISOU 1750  CE2 PHE A 224     4849   7008   4858    172   -342   1229       C  
ATOM   1751  CZ  PHE A 224      -1.002  12.211  -5.653  1.00 41.94           C  
ANISOU 1751  CZ  PHE A 224     4609   6710   4616    176   -371   1226       C  
ATOM   1752  N   GLU A 225       1.796  15.128  -9.989  1.00 46.34           N  
ANISOU 1752  N   GLU A 225     4834   7539   5233    401   -245   1373       N  
ATOM   1753  CA  GLU A 225       3.127  15.431  -9.346  1.00 47.51           C  
ANISOU 1753  CA  GLU A 225     4963   7662   5424    400   -266   1401       C  
ATOM   1754  C   GLU A 225       3.339  16.916  -9.217  1.00 47.08           C  
ANISOU 1754  C   GLU A 225     4843   7602   5442    368   -247   1474       C  
ATOM   1755  O   GLU A 225       4.167  17.348  -8.430  1.00 46.09           O  
ANISOU 1755  O   GLU A 225     4713   7428   5369    348   -273   1494       O  
ATOM   1756  CB  GLU A 225       4.260  14.897 -10.200  1.00 59.20           C  
ANISOU 1756  CB  GLU A 225     6392   9225   6873    479   -274   1412       C  
ATOM   1757  CG  GLU A 225       3.959  13.554 -10.864  1.00 73.51           C  
ANISOU 1757  CG  GLU A 225     8244  11073   8611    540   -298   1341       C  
ATOM   1758  CD  GLU A 225       5.218  12.756 -11.140  1.00 88.99           C  
ANISOU 1758  CD  GLU A 225    10188  13081  10540    619   -334   1318       C  
ATOM   1759  OE1 GLU A 225       5.976  12.488 -10.158  1.00 83.42           O  
ANISOU 1759  OE1 GLU A 225     9521  12308   9864    597   -369   1305       O  
ATOM   1760  OE2 GLU A 225       5.443  12.423 -12.347  1.00 99.54           O1-
ANISOU 1760  OE2 GLU A 225    11470  14531  11820    709   -326   1312       O1-
ATOM   1761  N   CYS A 226       2.632  17.700 -10.037  1.00 43.55           N  
ANISOU 1761  N   CYS A 226     4341   7202   5001    367   -211   1515       N  
ATOM   1762  CA  CYS A 226       2.780  19.130 -10.019  1.00 43.61           C  
ANISOU 1762  CA  CYS A 226     4283   7197   5088    337   -207   1590       C  
ATOM   1763  C   CYS A 226       1.795  19.868  -9.108  1.00 43.14           C  
ANISOU 1763  C   CYS A 226     4268   7054   5069    282   -218   1561       C  
ATOM   1764  O   CYS A 226       1.990  21.091  -8.884  1.00 42.92           O  
ANISOU 1764  O   CYS A 226     4195   6990   5122    258   -239   1610       O  
ATOM   1765  CB  CYS A 226       2.624  19.714 -11.426  1.00 44.25           C  
ANISOU 1765  CB  CYS A 226     4269   7380   5164    366   -169   1665       C  
ATOM   1766  SG  CYS A 226       3.539  18.895 -12.750  1.00 46.77           S  
ANISOU 1766  SG  CYS A 226     4518   7845   5407    455   -147   1696       S  
ATOM   1767  N   LEU A 227       0.741  19.163  -8.640  1.00 43.88           N  
ANISOU 1767  N   LEU A 227     4441   7123   5109    266   -211   1486       N  
ATOM   1768  CA  LEU A 227      -0.352  19.790  -7.899  1.00 46.48           C  
ANISOU 1768  CA  LEU A 227     4803   7405   5452    227   -212   1455       C  
ATOM   1769  C   LEU A 227      -0.491  19.428  -6.420  1.00 44.08           C  
ANISOU 1769  C   LEU A 227     4575   7035   5135    199   -242   1395       C  
ATOM   1770  O   LEU A 227      -1.277  20.035  -5.749  1.00 42.45           O  
ANISOU 1770  O   LEU A 227     4386   6804   4937    179   -246   1368       O  
ATOM   1771  CB  LEU A 227      -1.645  19.555  -8.623  1.00 50.05           C  
ANISOU 1771  CB  LEU A 227     5259   7902   5854    228   -174   1437       C  
ATOM   1772  CG  LEU A 227      -1.603  20.369  -9.938  1.00 49.54           C  
ANISOU 1772  CG  LEU A 227     5107   7899   5817    252   -148   1506       C  
ATOM   1773  CD1 LEU A 227      -2.531  19.738 -10.977  1.00 49.50           C  
ANISOU 1773  CD1 LEU A 227     5102   7959   5745    274   -111   1489       C  
ATOM   1774  CD2 LEU A 227      -1.994  21.825  -9.684  1.00 48.41           C  
ANISOU 1774  CD2 LEU A 227     4928   7716   5747    227   -162   1535       C  
ATOM   1775  N   TYR A 228       0.291  18.468  -5.942  1.00 43.87           N  
ANISOU 1775  N   TYR A 228     4590   6990   5086    204   -264   1375       N  
ATOM   1776  CA  TYR A 228       0.465  18.201  -4.514  1.00 47.06           C  
ANISOU 1776  CA  TYR A 228     5058   7337   5486    180   -298   1333       C  
ATOM   1777  C   TYR A 228      -0.847  18.174  -3.664  1.00 46.70           C  
ANISOU 1777  C   TYR A 228     5059   7289   5397    150   -290   1290       C  
ATOM   1778  O   TYR A 228      -1.037  18.978  -2.749  1.00 45.13           O  
ANISOU 1778  O   TYR A 228     4865   7063   5217    144   -308   1270       O  
ATOM   1779  CB  TYR A 228       1.468  19.198  -3.943  1.00 46.94           C  
ANISOU 1779  CB  TYR A 228     5013   7272   5548    185   -336   1355       C  
ATOM   1780  CG  TYR A 228       2.817  19.253  -4.712  1.00 47.93           C  
ANISOU 1780  CG  TYR A 228     5079   7414   5717    210   -344   1413       C  
ATOM   1781  CD1 TYR A 228       3.014  20.106  -5.779  1.00 48.31           C  
ANISOU 1781  CD1 TYR A 228     5040   7500   5812    223   -329   1482       C  
ATOM   1782  CD2 TYR A 228       3.861  18.439  -4.356  1.00 47.43           C  
ANISOU 1782  CD2 TYR A 228     5041   7336   5644    223   -368   1403       C  
ATOM   1783  CE1 TYR A 228       4.235  20.136  -6.446  1.00 52.58           C  
ANISOU 1783  CE1 TYR A 228     5515   8079   6384    247   -334   1547       C  
ATOM   1784  CE2 TYR A 228       5.106  18.470  -5.012  1.00 49.12           C  
ANISOU 1784  CE2 TYR A 228     5192   7580   5890    252   -375   1457       C  
ATOM   1785  CZ  TYR A 228       5.281  19.322  -6.042  1.00 51.10           C  
ANISOU 1785  CZ  TYR A 228     5352   7882   6182    263   -356   1532       C  
ATOM   1786  OH  TYR A 228       6.503  19.352  -6.662  1.00 51.33           O  
ANISOU 1786  OH  TYR A 228     5307   7960   6234    292   -361   1597       O  
ATOM   1787  N   PRO A 229      -1.717  17.188  -3.924  1.00 46.14           N  
ANISOU 1787  N   PRO A 229     5020   7248   5262    134   -271   1276       N  
ATOM   1788  CA  PRO A 229      -2.910  17.031  -3.098  1.00 46.66           C  
ANISOU 1788  CA  PRO A 229     5120   7328   5279    101   -263   1250       C  
ATOM   1789  C   PRO A 229      -2.557  16.827  -1.603  1.00 44.42           C  
ANISOU 1789  C   PRO A 229     4882   7015   4978     85   -296   1228       C  
ATOM   1790  O   PRO A 229      -1.524  16.291  -1.290  1.00 41.75           O  
ANISOU 1790  O   PRO A 229     4569   6640   4652     89   -327   1228       O  
ATOM   1791  CB  PRO A 229      -3.587  15.788  -3.681  1.00 46.95           C  
ANISOU 1791  CB  PRO A 229     5183   7390   5266     82   -255   1253       C  
ATOM   1792  CG  PRO A 229      -2.496  15.096  -4.455  1.00 47.16           C  
ANISOU 1792  CG  PRO A 229     5209   7400   5309    114   -276   1260       C  
ATOM   1793  CD  PRO A 229      -1.602  16.143  -4.945  1.00 45.79           C  
ANISOU 1793  CD  PRO A 229     4978   7228   5189    150   -266   1283       C  
ATOM   1794  N   TYR A 230      -3.449  17.245  -0.723  1.00 41.83           N  
ANISOU 1794  N   TYR A 230     4561   6715   4615     74   -289   1207       N  
ATOM   1795  CA  TYR A 230      -3.346  16.953   0.668  1.00 43.16           C  
ANISOU 1795  CA  TYR A 230     4770   6883   4745     62   -314   1188       C  
ATOM   1796  C   TYR A 230      -3.332  15.419   0.877  1.00 42.10           C  
ANISOU 1796  C   TYR A 230     4683   6748   4565     21   -328   1211       C  
ATOM   1797  O   TYR A 230      -3.786  14.631   0.033  1.00 38.95           O  
ANISOU 1797  O   TYR A 230     4286   6357   4155      0   -319   1232       O  
ATOM   1798  CB  TYR A 230      -4.520  17.607   1.447  1.00 42.42           C  
ANISOU 1798  CB  TYR A 230     4663   6853   4600     67   -298   1162       C  
ATOM   1799  CG  TYR A 230      -4.404  19.112   1.645  1.00 43.68           C  
ANISOU 1799  CG  TYR A 230     4789   6997   4807    117   -314   1123       C  
ATOM   1800  CD1 TYR A 230      -4.912  20.005   0.712  1.00 38.87           C  
ANISOU 1800  CD1 TYR A 230     4135   6393   4240    134   -296   1123       C  
ATOM   1801  CD2 TYR A 230      -3.832  19.655   2.826  1.00 43.67           C  
ANISOU 1801  CD2 TYR A 230     4803   6976   4812    150   -360   1082       C  
ATOM   1802  CE1 TYR A 230      -4.826  21.381   0.898  1.00 39.09           C  
ANISOU 1802  CE1 TYR A 230     4133   6394   4324    178   -330   1089       C  
ATOM   1803  CE2 TYR A 230      -3.776  21.034   3.018  1.00 42.83           C  
ANISOU 1803  CE2 TYR A 230     4668   6844   4759    201   -396   1039       C  
ATOM   1804  CZ  TYR A 230      -4.199  21.881   2.002  1.00 43.82           C  
ANISOU 1804  CZ  TYR A 230     4749   6960   4940    211   -385   1047       C  
ATOM   1805  OH  TYR A 230      -4.157  23.235   2.167  1.00 48.09           O  
ANISOU 1805  OH  TYR A 230     5261   7463   5545    259   -436   1007       O  
ATOM   1806  N   PRO A 231      -2.837  14.994   2.026  1.00 41.11           N  
ANISOU 1806  N   PRO A 231     4595   6607   4416     10   -361   1206       N  
ATOM   1807  CA  PRO A 231      -3.018  13.616   2.415  1.00 39.99           C  
ANISOU 1807  CA  PRO A 231     4496   6468   4230    -37   -384   1236       C  
ATOM   1808  C   PRO A 231      -4.487  13.199   2.394  1.00 44.29           C  
ANISOU 1808  C   PRO A 231     5029   7080   4717    -80   -359   1267       C  
ATOM   1809  O   PRO A 231      -5.380  14.036   2.667  1.00 42.82           O  
ANISOU 1809  O   PRO A 231     4810   6961   4499    -69   -323   1256       O  
ATOM   1810  CB  PRO A 231      -2.461  13.614   3.811  1.00 44.07           C  
ANISOU 1810  CB  PRO A 231     5042   6980   4722    -35   -414   1226       C  
ATOM   1811  CG  PRO A 231      -1.313  14.626   3.750  1.00 40.75           C  
ANISOU 1811  CG  PRO A 231     4607   6506   4367     17   -427   1188       C  
ATOM   1812  CD  PRO A 231      -1.889  15.713   2.893  1.00 42.24           C  
ANISOU 1812  CD  PRO A 231     4744   6717   4587     43   -390   1177       C  
ATOM   1813  N   VAL A 232      -4.740  11.930   2.052  1.00 42.82           N  
ANISOU 1813  N   VAL A 232     4869   6876   4524   -126   -387   1304       N  
ATOM   1814  CA  VAL A 232      -6.083  11.465   1.837  1.00 42.79           C  
ANISOU 1814  CA  VAL A 232     4849   6924   4482   -173   -374   1343       C  
ATOM   1815  C   VAL A 232      -6.946  11.606   3.103  1.00 43.93           C  
ANISOU 1815  C   VAL A 232     4978   7160   4551   -204   -356   1375       C  
ATOM   1816  O   VAL A 232      -8.126  11.848   2.960  1.00 46.42           O  
ANISOU 1816  O   VAL A 232     5255   7548   4831   -221   -321   1394       O  
ATOM   1817  CB  VAL A 232      -6.120   9.981   1.362  1.00 44.91           C  
ANISOU 1817  CB  VAL A 232     5153   7141   4769   -219   -434   1380       C  
ATOM   1818  CG1 VAL A 232      -7.468   9.346   1.560  1.00 43.08           C  
ANISOU 1818  CG1 VAL A 232     4908   6962   4499   -287   -440   1442       C  
ATOM   1819  CG2 VAL A 232      -5.810   9.875  -0.096  1.00 44.96           C  
ANISOU 1819  CG2 VAL A 232     5156   7100   4825   -179   -441   1347       C  
ATOM   1820  N   HIS A 233      -6.384  11.386   4.292  1.00 46.10           N  
ANISOU 1820  N   HIS A 233     5277   7440   4797   -210   -382   1384       N  
ATOM   1821  CA  HIS A 233      -7.071  11.571   5.623  1.00 47.10           C  
ANISOU 1821  CA  HIS A 233     5382   7677   4835   -224   -365   1412       C  
ATOM   1822  C   HIS A 233      -7.187  13.030   6.097  1.00 45.67           C  
ANISOU 1822  C   HIS A 233     5167   7558   4625   -151   -325   1346       C  
ATOM   1823  O   HIS A 233      -7.964  13.383   7.005  1.00 44.22           O  
ANISOU 1823  O   HIS A 233     4951   7490   4358   -140   -302   1353       O  
ATOM   1824  CB  HIS A 233      -6.340  10.779   6.661  1.00 49.05           C  
ANISOU 1824  CB  HIS A 233     5670   7905   5062   -251   -414   1445       C  
ATOM   1825  CG  HIS A 233      -6.263   9.322   6.327  1.00 56.55           C  
ANISOU 1825  CG  HIS A 233     6654   8789   6042   -323   -473   1510       C  
ATOM   1826  CD2 HIS A 233      -5.302   8.600   5.698  1.00 56.65           C  
ANISOU 1826  CD2 HIS A 233     6714   8683   6126   -324   -528   1495       C  
ATOM   1827  ND1 HIS A 233      -7.260   8.421   6.666  1.00 58.83           N  
ANISOU 1827  ND1 HIS A 233     6927   9135   6290   -402   -492   1604       N  
ATOM   1828  CE1 HIS A 233      -6.921   7.215   6.238  1.00 62.67           C  
ANISOU 1828  CE1 HIS A 233     7454   9524   6831   -451   -566   1641       C  
ATOM   1829  NE2 HIS A 233      -5.740   7.302   5.639  1.00 58.97           N  
ANISOU 1829  NE2 HIS A 233     7026   8952   6427   -398   -587   1569       N  
ATOM   1830  N   HIS A 234      -6.504  13.922   5.406  1.00 45.41           N  
ANISOU 1830  N   HIS A 234     5134   7455   4662    -96   -321   1283       N  
ATOM   1831  CA  HIS A 234      -6.638  15.324   5.714  1.00 48.51           C  
ANISOU 1831  CA  HIS A 234     5495   7884   5049    -26   -303   1218       C  
ATOM   1832  C   HIS A 234      -8.022  15.796   5.254  1.00 50.25           C  
ANISOU 1832  C   HIS A 234     5666   8189   5235    -24   -256   1220       C  
ATOM   1833  O   HIS A 234      -8.541  15.259   4.303  1.00 47.37           O  
ANISOU 1833  O   HIS A 234     5294   7813   4889    -67   -239   1258       O  
ATOM   1834  CB  HIS A 234      -5.613  16.134   4.987  1.00 49.45           C  
ANISOU 1834  CB  HIS A 234     5618   7904   5266     18   -319   1171       C  
ATOM   1835  CG  HIS A 234      -5.463  17.522   5.505  1.00 52.82           C  
ANISOU 1835  CG  HIS A 234     6023   8338   5707     90   -332   1104       C  
ATOM   1836  CD2 HIS A 234      -4.598  18.059   6.394  1.00 52.01           C  
ANISOU 1836  CD2 HIS A 234     5937   8204   5619    135   -377   1059       C  
ATOM   1837  ND1 HIS A 234      -6.225  18.561   5.044  1.00 55.09           N  
ANISOU 1837  ND1 HIS A 234     6268   8655   6006    126   -313   1071       N  
ATOM   1838  CE1 HIS A 234      -5.850  19.682   5.631  1.00 55.08           C  
ANISOU 1838  CE1 HIS A 234     6259   8636   6030    192   -352   1006       C  
ATOM   1839  NE2 HIS A 234      -4.863  19.405   6.451  1.00 53.61           N  
ANISOU 1839  NE2 HIS A 234     6108   8413   5847    200   -391    997       N  
ATOM   1840  N   PRO A 235      -8.582  16.828   5.905  1.00 49.89           N  
ANISOU 1840  N   PRO A 235     5587   8225   5142     33   -243   1170       N  
ATOM   1841  CA  PRO A 235      -9.901  17.313   5.507  1.00 50.74           C  
ANISOU 1841  CA  PRO A 235     5645   8419   5214     42   -202   1166       C  
ATOM   1842  C   PRO A 235      -9.977  17.940   4.110  1.00 49.37           C  
ANISOU 1842  C   PRO A 235     5456   8175   5125     54   -187   1146       C  
ATOM   1843  O   PRO A 235     -11.057  17.980   3.528  1.00 47.12           O  
ANISOU 1843  O   PRO A 235     5137   7944   4819     38   -152   1162       O  
ATOM   1844  CB  PRO A 235     -10.250  18.338   6.625  1.00 51.61           C  
ANISOU 1844  CB  PRO A 235     5727   8626   5256    124   -208   1098       C  
ATOM   1845  CG  PRO A 235      -9.490  17.838   7.818  1.00 53.68           C  
ANISOU 1845  CG  PRO A 235     6021   8899   5474    126   -240   1106       C  
ATOM   1846  CD  PRO A 235      -8.161  17.413   7.205  1.00 52.66           C  
ANISOU 1846  CD  PRO A 235     5943   8614   5449     94   -272   1118       C  
ATOM   1847  N   CYS A 236      -8.848  18.418   3.591  1.00 45.32           N  
ANISOU 1847  N   CYS A 236     4962   7551   4705     79   -216   1118       N  
ATOM   1848  CA  CYS A 236      -8.786  18.937   2.261  1.00 45.28           C  
ANISOU 1848  CA  CYS A 236     4937   7486   4778     86   -205   1115       C  
ATOM   1849  C   CYS A 236      -8.322  17.892   1.241  1.00 45.40           C  
ANISOU 1849  C   CYS A 236     4974   7442   4832     36   -200   1167       C  
ATOM   1850  O   CYS A 236      -7.871  18.229   0.149  1.00 46.33           O  
ANISOU 1850  O   CYS A 236     5079   7505   5018     49   -198   1170       O  
ATOM   1851  CB  CYS A 236      -7.920  20.185   2.223  1.00 46.98           C  
ANISOU 1851  CB  CYS A 236     5145   7630   5076    145   -244   1067       C  
ATOM   1852  SG  CYS A 236      -8.529  21.391   3.439  1.00 50.32           S  
ANISOU 1852  SG  CYS A 236     5546   8120   5452    221   -271    985       S  
ATOM   1853  N   ASP A 237      -8.541  16.634   1.545  1.00 43.79           N  
ANISOU 1853  N   ASP A 237     4798   7257   4581    -15   -203   1210       N  
ATOM   1854  CA  ASP A 237      -8.339  15.589   0.578  1.00 43.11           C  
ANISOU 1854  CA  ASP A 237     4731   7126   4521    -55   -210   1250       C  
ATOM   1855  C   ASP A 237      -8.848  16.030  -0.769  1.00 43.45           C  
ANISOU 1855  C   ASP A 237     4741   7169   4597    -43   -180   1248       C  
ATOM   1856  O   ASP A 237      -9.871  16.637  -0.876  1.00 45.56           O  
ANISOU 1856  O   ASP A 237     4973   7497   4837    -40   -148   1241       O  
ATOM   1857  CB  ASP A 237      -9.059  14.329   1.016  1.00 43.97           C  
ANISOU 1857  CB  ASP A 237     4858   7274   4572   -120   -222   1302       C  
ATOM   1858  CG  ASP A 237      -8.841  13.171   0.102  1.00 49.27           C  
ANISOU 1858  CG  ASP A 237     5554   7888   5275   -157   -251   1334       C  
ATOM   1859  OD1 ASP A 237      -7.798  13.046  -0.517  1.00 44.30           O  
ANISOU 1859  OD1 ASP A 237     4946   7184   4701   -129   -274   1314       O  
ATOM   1860  OD2 ASP A 237      -9.726  12.348   0.021  1.00 45.37           O1-
ANISOU 1860  OD2 ASP A 237     5055   7433   4748   -211   -257   1381       O1-
ATOM   1861  N   ARG A 238      -8.083  15.711  -1.789  1.00 44.84           N  
ANISOU 1861  N   ARG A 238     4924   7284   4828    -29   -192   1250       N  
ATOM   1862  CA  ARG A 238      -8.401  15.915  -3.194  1.00 43.93           C  
ANISOU 1862  CA  ARG A 238     4779   7168   4741    -12   -170   1254       C  
ATOM   1863  C   ARG A 238      -8.217  17.333  -3.659  1.00 43.67           C  
ANISOU 1863  C   ARG A 238     4702   7139   4753     31   -147   1237       C  
ATOM   1864  O   ARG A 238      -8.439  17.634  -4.794  1.00 42.10           O  
ANISOU 1864  O   ARG A 238     4469   6950   4576     48   -124   1246       O  
ATOM   1865  CB  ARG A 238      -9.794  15.439  -3.547  1.00 44.35           C  
ANISOU 1865  CB  ARG A 238     4822   7270   4757    -47   -151   1272       C  
ATOM   1866  CG  ARG A 238      -9.956  13.953  -3.637  1.00 47.99           C  
ANISOU 1866  CG  ARG A 238     5320   7720   5190   -100   -189   1304       C  
ATOM   1867  CD  ARG A 238     -11.382  13.599  -3.969  1.00 48.72           C  
ANISOU 1867  CD  ARG A 238     5392   7861   5257   -137   -175   1328       C  
ATOM   1868  NE  ARG A 238     -12.280  14.004  -2.917  1.00 55.38           N  
ANISOU 1868  NE  ARG A 238     6207   8784   6049   -157   -142   1339       N  
ATOM   1869  CZ  ARG A 238     -13.152  14.995  -2.998  1.00 69.93           C  
ANISOU 1869  CZ  ARG A 238     8006  10687   7878   -132    -96   1319       C  
ATOM   1870  NH1 ARG A 238     -13.263  15.717  -4.092  1.00 68.50           N1+
ANISOU 1870  NH1 ARG A 238     7800  10489   7736    -91    -73   1292       N1+
ATOM   1871  NH2 ARG A 238     -13.919  15.268  -1.972  1.00 71.41           N  
ANISOU 1871  NH2 ARG A 238     8167  10959   8005   -143    -75   1325       N  
ATOM   1872  N   GLN A 239      -7.819  18.197  -2.762  1.00 39.43           N  
ANISOU 1872  N   GLN A 239     4160   6587   4231     52   -161   1214       N  
ATOM   1873  CA  GLN A 239      -7.522  19.563  -3.111  1.00 42.02           C  
ANISOU 1873  CA  GLN A 239     4448   6895   4621     92   -164   1202       C  
ATOM   1874  C   GLN A 239      -5.997  19.753  -3.189  1.00 43.49           C  
ANISOU 1874  C   GLN A 239     4634   7017   4871    110   -198   1216       C  
ATOM   1875  O   GLN A 239      -5.270  19.009  -2.513  1.00 41.88           O  
ANISOU 1875  O   GLN A 239     4470   6789   4653     99   -220   1214       O  
ATOM   1876  CB  GLN A 239      -8.080  20.475  -2.054  1.00 44.99           C  
ANISOU 1876  CB  GLN A 239     4818   7295   4981    113   -176   1159       C  
ATOM   1877  CG  GLN A 239      -9.566  20.308  -1.841  1.00 55.58           C  
ANISOU 1877  CG  GLN A 239     6150   8719   6249     99   -142   1148       C  
ATOM   1878  CD  GLN A 239     -10.026  21.186  -0.699  1.00 62.42           C  
ANISOU 1878  CD  GLN A 239     7006   9625   7084    138   -160   1095       C  
ATOM   1879  NE2 GLN A 239     -10.981  20.718   0.076  1.00 68.31           N  
ANISOU 1879  NE2 GLN A 239     7754  10461   7740    125   -139   1090       N  
ATOM   1880  OE1 GLN A 239      -9.503  22.258  -0.507  1.00 73.92           O  
ANISOU 1880  OE1 GLN A 239     8450  11036   8598    182   -199   1060       O  
ATOM   1881  N   SER A 240      -5.541  20.734  -4.001  1.00 41.74           N  
ANISOU 1881  N   SER A 240     4364   6772   4721    135   -203   1239       N  
ATOM   1882  CA  SER A 240      -4.139  21.074  -4.150  1.00 44.14           C  
ANISOU 1882  CA  SER A 240     4649   7026   5094    150   -235   1268       C  
ATOM   1883  C   SER A 240      -3.649  21.857  -2.925  1.00 47.08           C  
ANISOU 1883  C   SER A 240     5033   7347   5506    163   -289   1235       C  
ATOM   1884  O   SER A 240      -4.341  22.719  -2.445  1.00 43.22           O  
ANISOU 1884  O   SER A 240     4536   6859   5024    179   -305   1199       O  
ATOM   1885  CB  SER A 240      -3.896  21.907  -5.406  1.00 44.59           C  
ANISOU 1885  CB  SER A 240     4638   7087   5215    165   -228   1321       C  
ATOM   1886  OG  SER A 240      -2.498  22.261  -5.558  1.00 44.36           O  
ANISOU 1886  OG  SER A 240     4576   7020   5256    175   -262   1366       O  
ATOM   1887  N   GLN A 241      -2.423  21.580  -2.470  1.00 45.32           N  
ANISOU 1887  N   GLN A 241     4826   7081   5312    165   -322   1244       N  
ATOM   1888  CA  GLN A 241      -1.854  22.347  -1.370  1.00 43.37           C  
ANISOU 1888  CA  GLN A 241     4588   6777   5110    183   -383   1212       C  
ATOM   1889  C   GLN A 241      -1.277  23.633  -1.851  1.00 46.55           C  
ANISOU 1889  C   GLN A 241     4932   7128   5625    197   -429   1247       C  
ATOM   1890  O   GLN A 241      -0.936  24.497  -1.039  1.00 47.44           O  
ANISOU 1890  O   GLN A 241     5046   7183   5795    218   -496   1217       O  
ATOM   1891  CB  GLN A 241      -0.771  21.576  -0.648  1.00 42.84           C  
ANISOU 1891  CB  GLN A 241     4561   6679   5036    177   -408   1208       C  
ATOM   1892  CG  GLN A 241      -1.245  20.367   0.122  1.00 42.62           C  
ANISOU 1892  CG  GLN A 241     4595   6689   4910    158   -386   1177       C  
ATOM   1893  CD  GLN A 241      -0.059  19.619   0.628  1.00 46.87           C  
ANISOU 1893  CD  GLN A 241     5166   7187   5452    153   -414   1183       C  
ATOM   1894  NE2 GLN A 241       0.402  18.658  -0.138  1.00 44.52           N  
ANISOU 1894  NE2 GLN A 241     4873   6897   5144    141   -395   1215       N  
ATOM   1895  OE1 GLN A 241       0.481  19.953   1.668  1.00 47.88           O  
ANISOU 1895  OE1 GLN A 241     5315   7279   5597    168   -459   1153       O  
ATOM   1896  N   VAL A 242      -1.223  23.795  -3.167  1.00 47.68           N  
ANISOU 1896  N   VAL A 242     5021   7294   5799    189   -399   1313       N  
ATOM   1897  CA  VAL A 242      -0.597  24.924  -3.707  1.00 46.05           C  
ANISOU 1897  CA  VAL A 242     4749   7044   5702    192   -445   1372       C  
ATOM   1898  C   VAL A 242      -1.469  26.122  -3.734  1.00 48.14           C  
ANISOU 1898  C   VAL A 242     4989   7286   6013    204   -478   1354       C  
ATOM   1899  O   VAL A 242      -2.550  26.083  -4.308  1.00 46.76           O  
ANISOU 1899  O   VAL A 242     4809   7164   5793    204   -430   1345       O  
ATOM   1900  CB  VAL A 242      -0.180  24.649  -5.142  1.00 49.87           C  
ANISOU 1900  CB  VAL A 242     5173   7581   6192    183   -400   1461       C  
ATOM   1901  CG1 VAL A 242       0.465  25.897  -5.720  1.00 51.39           C  
ANISOU 1901  CG1 VAL A 242     5282   7737   6505    177   -451   1547       C  
ATOM   1902  CG2 VAL A 242       0.782  23.472  -5.249  1.00 48.17           C  
ANISOU 1902  CG2 VAL A 242     4974   7394   5934    184   -375   1478       C  
ATOM   1903  N   ASP A 243      -1.016  27.236  -3.214  1.00 51.14           N  
ANISOU 1903  N   ASP A 243     5350   7585   6496    217   -569   1350       N  
ATOM   1904  CA  ASP A 243      -1.752  28.472  -3.365  1.00 52.93           C  
ANISOU 1904  CA  ASP A 243     5544   7776   6788    234   -621   1336       C  
ATOM   1905  C   ASP A 243      -1.475  29.069  -4.727  1.00 49.61           C  
ANISOU 1905  C   ASP A 243     5042   7359   6447    207   -618   1452       C  
ATOM   1906  O   ASP A 243      -0.430  29.581  -4.949  1.00 48.78           O  
ANISOU 1906  O   ASP A 243     4885   7207   6443    188   -671   1536       O  
ATOM   1907  CB  ASP A 243      -1.332  29.429  -2.269  1.00 56.93           C  
ANISOU 1907  CB  ASP A 243     6063   8182   7383    265   -741   1281       C  
ATOM   1908  CG  ASP A 243      -1.976  30.774  -2.364  1.00 61.62           C  
ANISOU 1908  CG  ASP A 243     6629   8724   8060    292   -822   1255       C  
ATOM   1909  OD1 ASP A 243      -2.551  31.142  -3.375  1.00 62.70           O  
ANISOU 1909  OD1 ASP A 243     6719   8878   8224    278   -804   1307       O  
ATOM   1910  OD2 ASP A 243      -1.888  31.502  -1.392  1.00 69.61           O1-
ANISOU 1910  OD2 ASP A 243     7664   9666   9116    336   -921   1176       O1-
ATOM   1911  N   PHE A 244      -2.431  29.019  -5.633  1.00 49.15           N  
ANISOU 1911  N   PHE A 244     4966   7364   6344    203   -558   1466       N  
ATOM   1912  CA  PHE A 244      -2.221  29.502  -6.985  1.00 49.85           C  
ANISOU 1912  CA  PHE A 244     4973   7475   6492    181   -548   1581       C  
ATOM   1913  C   PHE A 244      -1.827  30.966  -7.060  1.00 56.13           C  
ANISOU 1913  C   PHE A 244     5709   8178   7440    173   -659   1640       C  
ATOM   1914  O   PHE A 244      -1.237  31.393  -8.082  1.00 56.19           O  
ANISOU 1914  O   PHE A 244     5633   8198   7518    145   -668   1768       O  
ATOM   1915  CB  PHE A 244      -3.478  29.282  -7.855  1.00 53.57           C  
ANISOU 1915  CB  PHE A 244     5440   8024   6889    185   -473   1573       C  
ATOM   1916  CG  PHE A 244      -3.561  27.914  -8.479  1.00 49.19           C  
ANISOU 1916  CG  PHE A 244     4902   7568   6219    182   -371   1580       C  
ATOM   1917  CD1 PHE A 244      -3.137  26.788  -7.797  1.00 46.71           C  
ANISOU 1917  CD1 PHE A 244     4645   7265   5834    184   -345   1533       C  
ATOM   1918  CD2 PHE A 244      -4.158  27.755  -9.706  1.00 46.08           C  
ANISOU 1918  CD2 PHE A 244     4471   7248   5786    182   -312   1624       C  
ATOM   1919  CE1 PHE A 244      -3.229  25.553  -8.383  1.00 44.75           C  
ANISOU 1919  CE1 PHE A 244     4415   7094   5492    186   -273   1535       C  
ATOM   1920  CE2 PHE A 244      -4.282  26.535 -10.270  1.00 43.82           C  
ANISOU 1920  CE2 PHE A 244     4204   7044   5401    190   -237   1618       C  
ATOM   1921  CZ  PHE A 244      -3.797  25.425  -9.624  1.00 42.74           C  
ANISOU 1921  CZ  PHE A 244     4122   6910   5204    192   -222   1574       C  
ATOM   1922  N   ASP A 245      -2.180  31.744  -6.026  1.00 60.27           N  
ANISOU 1922  N   ASP A 245     6269   8615   8016    201   -751   1551       N  
ATOM   1923  CA  ASP A 245      -1.871  33.178  -6.003  1.00 61.73           C  
ANISOU 1923  CA  ASP A 245     6403   8688   8360    198   -884   1593       C  
ATOM   1924  C   ASP A 245      -0.444  33.433  -5.565  1.00 61.85           C  
ANISOU 1924  C   ASP A 245     6395   8625   8480    178   -968   1650       C  
ATOM   1925  O   ASP A 245       0.116  34.415  -5.989  1.00 63.24           O  
ANISOU 1925  O   ASP A 245     6500   8728   8797    150  -1062   1749       O  
ATOM   1926  CB  ASP A 245      -2.816  33.944  -5.073  1.00 65.04           C  
ANISOU 1926  CB  ASP A 245     6870   9046   8795    252   -966   1460       C  
ATOM   1927  CG  ASP A 245      -4.270  33.925  -5.548  1.00 63.66           C  
ANISOU 1927  CG  ASP A 245     6705   8943   8540    271   -902   1412       C  
ATOM   1928  OD1 ASP A 245      -4.496  33.930  -6.772  1.00 58.23           O  
ANISOU 1928  OD1 ASP A 245     5966   8303   7856    238   -847   1506       O  
ATOM   1929  OD2 ASP A 245      -5.180  33.912  -4.684  1.00 62.07           O1-
ANISOU 1929  OD2 ASP A 245     6558   8756   8267    324   -906   1282       O1-
ATOM   1930  N   ASN A 246       0.116  32.557  -4.709  1.00 67.07           N  
ANISOU 1930  N   ASN A 246     7111   9297   9074    190   -940   1592       N  
ATOM   1931  CA  ASN A 246       1.473  32.690  -4.154  1.00 61.67           C  
ANISOU 1931  CA  ASN A 246     6414   8539   8478    176  -1017   1630       C  
ATOM   1932  C   ASN A 246       2.121  31.307  -4.022  1.00 62.23           C  
ANISOU 1932  C   ASN A 246     6516   8686   8439    168   -919   1630       C  
ATOM   1933  O   ASN A 246       2.253  30.761  -2.925  1.00 57.94           O  
ANISOU 1933  O   ASN A 246     6044   8127   7840    194   -923   1534       O  
ATOM   1934  CB  ASN A 246       1.478  33.435  -2.795  1.00 64.74           C  
ANISOU 1934  CB  ASN A 246     6853   8811   8934    221  -1149   1517       C  
ATOM   1935  CG  ASN A 246       2.911  33.819  -2.321  1.00 77.77           C  
ANISOU 1935  CG  ASN A 246     8475  10361  10712    202  -1258   1571       C  
ATOM   1936  ND2 ASN A 246       3.092  33.897  -1.002  1.00 75.55           N  
ANISOU 1936  ND2 ASN A 246     8259  10013  10433    249  -1334   1454       N  
ATOM   1937  OD1 ASN A 246       3.840  34.055  -3.134  1.00 82.82           O  
ANISOU 1937  OD1 ASN A 246     9030  10991  11443    148  -1274   1721       O  
ATOM   1938  N   PRO A 247       2.524  30.716  -5.155  1.00 59.86           N  
ANISOU 1938  N   PRO A 247     6161   8477   8104    139   -834   1737       N  
ATOM   1939  CA  PRO A 247       2.987  29.331  -5.110  1.00 53.35           C  
ANISOU 1939  CA  PRO A 247     5372   7730   7166    142   -743   1722       C  
ATOM   1940  C   PRO A 247       4.328  29.218  -4.443  1.00 57.15           C  
ANISOU 1940  C   PRO A 247     5850   8158   7703    135   -799   1742       C  
ATOM   1941  O   PRO A 247       5.237  29.921  -4.784  1.00 60.61           O  
ANISOU 1941  O   PRO A 247     6212   8560   8257    110   -862   1848       O  
ATOM   1942  CB  PRO A 247       3.118  28.922  -6.571  1.00 56.12           C  
ANISOU 1942  CB  PRO A 247     5651   8193   7478    127   -659   1830       C  
ATOM   1943  CG  PRO A 247       2.690  30.106  -7.416  1.00 58.76           C  
ANISOU 1943  CG  PRO A 247     5908   8514   7902    109   -697   1915       C  
ATOM   1944  CD  PRO A 247       2.488  31.295  -6.515  1.00 58.68           C  
ANISOU 1944  CD  PRO A 247     5915   8369   8010    109   -822   1869       C  
ATOM   1945  N   ASP A 248       4.432  28.298  -3.511  1.00 57.55           N  
ANISOU 1945  N   ASP A 248     5983   8212   7672    155   -775   1649       N  
ATOM   1946  CA  ASP A 248       5.634  28.036  -2.813  1.00 58.38           C  
ANISOU 1946  CA  ASP A 248     6097   8270   7811    153   -819   1653       C  
ATOM   1947  C   ASP A 248       6.486  27.024  -3.602  1.00 59.23           C  
ANISOU 1947  C   ASP A 248     6168   8469   7864    144   -744   1728       C  
ATOM   1948  O   ASP A 248       6.377  25.764  -3.442  1.00 51.11           O  
ANISOU 1948  O   ASP A 248     5201   7499   6719    160   -674   1670       O  
ATOM   1949  CB  ASP A 248       5.302  27.506  -1.435  1.00 56.08           C  
ANISOU 1949  CB  ASP A 248     5910   7948   7449    182   -830   1519       C  
ATOM   1950  CG  ASP A 248       6.546  27.388  -0.572  1.00 60.63           C  
ANISOU 1950  CG  ASP A 248     6500   8459   8075    184   -894   1514       C  
ATOM   1951  OD1 ASP A 248       7.629  27.402  -1.164  1.00 63.50           O  
ANISOU 1951  OD1 ASP A 248     6797   8828   8500    160   -903   1615       O  
ATOM   1952  OD2 ASP A 248       6.447  27.267   0.663  1.00 62.85           O1-
ANISOU 1952  OD2 ASP A 248     6853   8696   8328    210   -934   1414       O1-
ATOM   1953  N   TYR A 249       7.323  27.568  -4.478  1.00 55.77           N  
ANISOU 1953  N   TYR A 249     5626   8051   7511    121   -764   1860       N  
ATOM   1954  CA  TYR A 249       8.175  26.695  -5.290  1.00 62.41           C  
ANISOU 1954  CA  TYR A 249     6416   8998   8296    127   -697   1933       C  
ATOM   1955  C   TYR A 249       9.213  25.886  -4.518  1.00 59.69           C  
ANISOU 1955  C   TYR A 249     6111   8637   7930    139   -709   1897       C  
ATOM   1956  O   TYR A 249       9.754  24.954  -5.083  1.00 62.31           O  
ANISOU 1956  O   TYR A 249     6423   9063   8189    159   -650   1922       O  
ATOM   1957  CB  TYR A 249       8.875  27.463  -6.423  1.00 59.54           C  
ANISOU 1957  CB  TYR A 249     5915   8688   8018    102   -712   2100       C  
ATOM   1958  CG  TYR A 249       7.908  28.158  -7.331  1.00 53.65           C  
ANISOU 1958  CG  TYR A 249     5124   7974   7285     91   -694   2149       C  
ATOM   1959  CD1 TYR A 249       6.893  27.466  -7.947  1.00 52.71           C  
ANISOU 1959  CD1 TYR A 249     5040   7942   7045    118   -601   2097       C  
ATOM   1960  CD2 TYR A 249       8.032  29.513  -7.608  1.00 53.12           C  
ANISOU 1960  CD2 TYR A 249     4975   7848   7360     52   -778   2255       C  
ATOM   1961  CE1 TYR A 249       6.004  28.116  -8.793  1.00 48.90           C  
ANISOU 1961  CE1 TYR A 249     4515   7490   6574    109   -584   2142       C  
ATOM   1962  CE2 TYR A 249       7.137  30.153  -8.427  1.00 50.78           C  
ANISOU 1962  CE2 TYR A 249     4638   7576   7077     42   -766   2300       C  
ATOM   1963  CZ  TYR A 249       6.119  29.435  -9.005  1.00 50.38           C  
ANISOU 1963  CZ  TYR A 249     4628   7618   6896     72   -664   2239       C  
ATOM   1964  OH  TYR A 249       5.242  30.067  -9.873  1.00 54.67           O  
ANISOU 1964  OH  TYR A 249     5128   8192   7451     63   -650   2287       O  
ATOM   1965  N   GLU A 250       9.480  26.206  -3.259  1.00 60.25           N  
ANISOU 1965  N   GLU A 250     6238   8596   8057    135   -788   1833       N  
ATOM   1966  CA  GLU A 250      10.419  25.399  -2.515  1.00 65.32           C  
ANISOU 1966  CA  GLU A 250     6921   9222   8673    147   -798   1795       C  
ATOM   1967  C   GLU A 250       9.727  24.124  -2.043  1.00 60.79           C  
ANISOU 1967  C   GLU A 250     6456   8682   7959    172   -732   1679       C  
ATOM   1968  O   GLU A 250      10.334  23.064  -2.095  1.00 54.81           O  
ANISOU 1968  O   GLU A 250     5715   7971   7137    188   -698   1670       O  
ATOM   1969  CB  GLU A 250      11.055  26.137  -1.305  1.00 74.45           C  
ANISOU 1969  CB  GLU A 250     8099  10248   9939    139   -913   1768       C  
ATOM   1970  CG  GLU A 250      11.918  27.380  -1.628  1.00 87.18           C  
ANISOU 1970  CG  GLU A 250     9604  11803  11716    106  -1007   1892       C  
ATOM   1971  CD  GLU A 250      13.106  27.145  -2.585  1.00 93.17           C  
ANISOU 1971  CD  GLU A 250    10251  12649  12497     89   -979   2033       C  
ATOM   1972  OE1 GLU A 250      13.983  26.288  -2.308  1.00 94.82           O  
ANISOU 1972  OE1 GLU A 250    10475  12889  12663    105   -959   2020       O  
ATOM   1973  OE2 GLU A 250      13.186  27.858  -3.615  1.00 90.03           O1-
ANISOU 1973  OE2 GLU A 250     9745  12297  12163     62   -981   2163       O1-
ATOM   1974  N   ARG A 251       8.491  24.216  -1.539  1.00 56.19           N  
ANISOU 1974  N   ARG A 251     5941   8076   7331    177   -724   1593       N  
ATOM   1975  CA  ARG A 251       7.750  23.004  -1.152  1.00 56.61           C  
ANISOU 1975  CA  ARG A 251     6085   8169   7254    190   -664   1504       C  
ATOM   1976  C   ARG A 251       7.188  22.309  -2.402  1.00 51.75           C  
ANISOU 1976  C   ARG A 251     5446   7655   6560    195   -578   1533       C  
ATOM   1977  O   ARG A 251       7.099  21.089  -2.458  1.00 46.09           O  
ANISOU 1977  O   ARG A 251     4776   6981   5752    206   -537   1496       O  
ATOM   1978  CB  ARG A 251       6.587  23.316  -0.205  1.00 64.01           C  
ANISOU 1978  CB  ARG A 251     7089   9070   8159    195   -680   1412       C  
ATOM   1979  CG  ARG A 251       6.972  24.036   1.086  1.00 70.53           C  
ANISOU 1979  CG  ARG A 251     7944   9802   9049    207   -772   1361       C  
ATOM   1980  CD  ARG A 251       5.766  24.584   1.862  1.00 73.85           C  
ANISOU 1980  CD  ARG A 251     8409  10208   9439    228   -792   1274       C  
ATOM   1981  NE  ARG A 251       4.940  23.471   2.336  1.00 75.05           N  
ANISOU 1981  NE  ARG A 251     8633  10426   9457    231   -727   1213       N  
ATOM   1982  CZ  ARG A 251       3.661  23.556   2.695  1.00 68.38           C  
ANISOU 1982  CZ  ARG A 251     7817   9622   8542    244   -704   1155       C  
ATOM   1983  NH1 ARG A 251       3.014  24.713   2.689  1.00 64.59           N1+
ANISOU 1983  NH1 ARG A 251     7310   9121   8109    267   -742   1131       N1+
ATOM   1984  NH2 ARG A 251       3.036  22.457   3.071  1.00 66.03           N  
ANISOU 1984  NH2 ARG A 251     7572   9386   8128    235   -648   1124       N  
ATOM   1985  N   PHE A 252       6.802  23.089  -3.419  1.00 48.64           N  
ANISOU 1985  N   PHE A 252     4979   7296   6204    189   -562   1599       N  
ATOM   1986  CA  PHE A 252       6.080  22.509  -4.527  1.00 47.40           C  
ANISOU 1986  CA  PHE A 252     4808   7234   5968    201   -486   1611       C  
ATOM   1987  C   PHE A 252       6.779  22.744  -5.882  1.00 49.21           C  
ANISOU 1987  C   PHE A 252     4927   7546   6223    212   -462   1724       C  
ATOM   1988  O   PHE A 252       6.244  23.333  -6.798  1.00 50.68           O  
ANISOU 1988  O   PHE A 252     5055   7777   6422    208   -438   1779       O  
ATOM   1989  CB  PHE A 252       4.694  23.062  -4.504  1.00 44.53           C  
ANISOU 1989  CB  PHE A 252     4466   6859   5594    191   -474   1574       C  
ATOM   1990  CG  PHE A 252       4.010  22.979  -3.140  1.00 43.73           C  
ANISOU 1990  CG  PHE A 252     4453   6697   5463    187   -499   1474       C  
ATOM   1991  CD1 PHE A 252       3.871  21.796  -2.504  1.00 42.81           C  
ANISOU 1991  CD1 PHE A 252     4412   6592   5259    189   -478   1411       C  
ATOM   1992  CD2 PHE A 252       3.423  24.103  -2.575  1.00 44.70           C  
ANISOU 1992  CD2 PHE A 252     4577   6765   5641    186   -547   1445       C  
ATOM   1993  CE1 PHE A 252       3.192  21.709  -1.295  1.00 44.62           C  
ANISOU 1993  CE1 PHE A 252     4711   6792   5449    186   -495   1333       C  
ATOM   1994  CE2 PHE A 252       2.750  24.040  -1.391  1.00 44.60           C  
ANISOU 1994  CE2 PHE A 252     4634   6726   5585    196   -566   1353       C  
ATOM   1995  CZ  PHE A 252       2.650  22.836  -0.733  1.00 45.64           C  
ANISOU 1995  CZ  PHE A 252     4835   6883   5622    194   -535   1303       C  
ATOM   1996  N   PRO A 253       7.961  22.181  -6.038  1.00 49.51           N  
ANISOU 1996  N   PRO A 253     4936   7620   6254    231   -464   1758       N  
ATOM   1997  CA  PRO A 253       8.772  22.574  -7.193  1.00 49.74           C  
ANISOU 1997  CA  PRO A 253     4843   7740   6314    243   -450   1880       C  
ATOM   1998  C   PRO A 253       8.175  22.217  -8.566  1.00 50.64           C  
ANISOU 1998  C   PRO A 253     4912   7980   6347    276   -379   1909       C  
ATOM   1999  O   PRO A 253       8.269  23.005  -9.533  1.00 49.26           O  
ANISOU 1999  O   PRO A 253     4633   7873   6209    272   -368   2018       O  
ATOM   2000  CB  PRO A 253      10.088  21.897  -6.923  1.00 46.17           C  
ANISOU 2000  CB  PRO A 253     4381   7307   5854    265   -466   1888       C  
ATOM   2001  CG  PRO A 253       9.813  20.778  -5.942  1.00 44.68           C  
ANISOU 2001  CG  PRO A 253     4318   7062   5595    277   -469   1760       C  
ATOM   2002  CD  PRO A 253       8.577  21.133  -5.207  1.00 46.52           C  
ANISOU 2002  CD  PRO A 253     4628   7214   5831    245   -478   1689       C  
ATOM   2003  N   ASN A 254       7.532  21.059  -8.650  1.00 53.94           N  
ANISOU 2003  N   ASN A 254     5406   8429   6659    308   -339   1815       N  
ATOM   2004  CA  ASN A 254       6.858  20.683  -9.869  1.00 52.67           C  
ANISOU 2004  CA  ASN A 254     5216   8375   6420    346   -283   1822       C  
ATOM   2005  C   ASN A 254       5.682  21.557 -10.271  1.00 49.64           C  
ANISOU 2005  C   ASN A 254     4816   7982   6060    317   -265   1844       C  
ATOM   2006  O   ASN A 254       5.259  21.507 -11.394  1.00 46.33           O  
ANISOU 2006  O   ASN A 254     4349   7659   5593    346   -222   1876       O  
ATOM   2007  CB  ASN A 254       6.577  19.189  -9.927  1.00 49.44           C  
ANISOU 2007  CB  ASN A 254     4885   7995   5904    391   -264   1722       C  
ATOM   2008  CG  ASN A 254       7.868  18.412 -10.094  1.00 51.58           C  
ANISOU 2008  CG  ASN A 254     5129   8325   6142    445   -275   1727       C  
ATOM   2009  ND2 ASN A 254       8.594  18.661 -11.242  1.00 49.46           N  
ANISOU 2009  ND2 ASN A 254     4742   8192   5858    493   -250   1818       N  
ATOM   2010  OD1 ASN A 254       8.259  17.637  -9.209  1.00 51.60           O  
ANISOU 2010  OD1 ASN A 254     5207   8263   6134    445   -308   1659       O  
ATOM   2011  N   PHE A 255       5.248  22.462  -9.422  1.00 49.93           N  
ANISOU 2011  N   PHE A 255     4882   7912   6176    267   -304   1833       N  
ATOM   2012  CA  PHE A 255       4.247  23.426  -9.875  1.00 48.65           C  
ANISOU 2012  CA  PHE A 255     4691   7745   6049    245   -298   1863       C  
ATOM   2013  C   PHE A 255       4.714  24.345 -11.026  1.00 47.54           C  
ANISOU 2013  C   PHE A 255     4420   7679   5963    243   -295   2005       C  
ATOM   2014  O   PHE A 255       3.926  24.898 -11.768  1.00 44.69           O  
ANISOU 2014  O   PHE A 255     4022   7351   5605    238   -274   2041       O  
ATOM   2015  CB  PHE A 255       3.756  24.276  -8.711  1.00 47.25           C  
ANISOU 2015  CB  PHE A 255     4564   7441   5948    205   -355   1817       C  
ATOM   2016  CG  PHE A 255       2.491  25.015  -9.023  1.00 49.42           C  
ANISOU 2016  CG  PHE A 255     4836   7706   6235    193   -347   1808       C  
ATOM   2017  CD1 PHE A 255       1.330  24.327  -9.256  1.00 50.09           C  
ANISOU 2017  CD1 PHE A 255     4974   7830   6225    206   -293   1737       C  
ATOM   2018  CD2 PHE A 255       2.470  26.379  -9.103  1.00 50.22           C  
ANISOU 2018  CD2 PHE A 255     4878   7754   6445    168   -403   1872       C  
ATOM   2019  CE1 PHE A 255       0.149  24.983  -9.524  1.00 50.34           C  
ANISOU 2019  CE1 PHE A 255     5003   7856   6265    197   -284   1725       C  
ATOM   2020  CE2 PHE A 255       1.294  27.045  -9.370  1.00 52.65           C  
ANISOU 2020  CE2 PHE A 255     5188   8051   6765    161   -401   1856       C  
ATOM   2021  CZ  PHE A 255       0.135  26.348  -9.603  1.00 52.91           C  
ANISOU 2021  CZ  PHE A 255     5273   8133   6696    177   -337   1783       C  
ATOM   2022  N   GLN A 256       6.007  24.511 -11.133  1.00 45.62           N  
ANISOU 2022  N   GLN A 256     4104   7464   5765    244   -319   2091       N  
ATOM   2023  CA  GLN A 256       6.631  25.275 -12.164  1.00 46.60           C  
ANISOU 2023  CA  GLN A 256     4092   7676   5937    239   -318   2246       C  
ATOM   2024  C   GLN A 256       6.485  24.582 -13.499  1.00 44.42           C  
ANISOU 2024  C   GLN A 256     3763   7569   5543    299   -241   2272       C  
ATOM   2025  O   GLN A 256       6.776  25.196 -14.488  1.00 49.25           O  
ANISOU 2025  O   GLN A 256     4259   8280   6174    300   -228   2403       O  
ATOM   2026  CB  GLN A 256       8.169  25.387 -11.866  1.00 51.75           C  
ANISOU 2026  CB  GLN A 256     4679   8334   6650    231   -360   2328       C  
ATOM   2027  CG  GLN A 256       8.486  26.476 -10.847  1.00 56.45           C  
ANISOU 2027  CG  GLN A 256     5278   8774   7395    168   -458   2354       C  
ATOM   2028  CD  GLN A 256       9.891  26.395 -10.259  1.00 61.18           C  
ANISOU 2028  CD  GLN A 256     5846   9347   8050    160   -505   2396       C  
ATOM   2029  NE2 GLN A 256      10.261  25.249  -9.703  1.00 58.79           N  
ANISOU 2029  NE2 GLN A 256     5619   9050   7665    197   -481   2295       N  
ATOM   2030  OE1 GLN A 256      10.636  27.365 -10.323  1.00 67.84           O  
ANISOU 2030  OE1 GLN A 256     6596  10165   9015    118   -570   2523       O  
ATOM   2031  N   ASN A 257       6.178  23.292 -13.521  1.00 44.66           N  
ANISOU 2031  N   ASN A 257     3872   7639   5458    352   -199   2158       N  
ATOM   2032  CA  ASN A 257       5.878  22.546 -14.758  1.00 45.94           C  
ANISOU 2032  CA  ASN A 257     4001   7952   5502    424   -137   2152       C  
ATOM   2033  C   ASN A 257       4.410  22.342 -15.103  1.00 50.74           C  
ANISOU 2033  C   ASN A 257     4670   8550   6057    429   -106   2076       C  
ATOM   2034  O   ASN A 257       4.101  21.624 -16.059  1.00 54.43           O  
ANISOU 2034  O   ASN A 257     5126   9130   6425    494    -65   2051       O  
ATOM   2035  CB  ASN A 257       6.460  21.166 -14.651  1.00 44.76           C  
ANISOU 2035  CB  ASN A 257     3898   7848   5260    490   -129   2066       C  
ATOM   2036  CG  ASN A 257       7.903  21.187 -14.225  1.00 46.63           C  
ANISOU 2036  CG  ASN A 257     4086   8093   5537    491   -159   2121       C  
ATOM   2037  ND2 ASN A 257       8.721  21.681 -15.114  1.00 45.85           N  
ANISOU 2037  ND2 ASN A 257     3850   8128   5442    515   -143   2254       N  
ATOM   2038  OD1 ASN A 257       8.283  20.764 -13.106  1.00 47.41           O  
ANISOU 2038  OD1 ASN A 257     4264   8085   5661    472   -197   2049       O  
ATOM   2039  N   VAL A 258       3.505  22.937 -14.335  1.00 50.97           N  
ANISOU 2039  N   VAL A 258     4764   8452   6148    369   -130   2034       N  
ATOM   2040  CA  VAL A 258       2.097  22.685 -14.560  1.00 49.65           C  
ANISOU 2040  CA  VAL A 258     4658   8275   5930    372   -101   1958       C  
ATOM   2041  C   VAL A 258       1.589  23.439 -15.764  1.00 54.23           C  
ANISOU 2041  C   VAL A 258     5151   8940   6511    379    -72   2044       C  
ATOM   2042  O   VAL A 258       1.891  24.639 -15.969  1.00 56.63           O  
ANISOU 2042  O   VAL A 258     5372   9237   6904    342    -95   2158       O  
ATOM   2043  CB  VAL A 258       1.269  23.048 -13.336  1.00 50.07           C  
ANISOU 2043  CB  VAL A 258     4802   8186   6036    315   -133   1881       C  
ATOM   2044  CG1 VAL A 258       0.971  24.540 -13.266  1.00 50.54           C  
ANISOU 2044  CG1 VAL A 258     4812   8188   6200    268   -167   1951       C  
ATOM   2045  CG2 VAL A 258      -0.002  22.291 -13.395  1.00 59.04           C  
ANISOU 2045  CG2 VAL A 258     6015   9323   7094    326   -103   1784       C  
ATOM   2046  N   VAL A 259       0.812  22.717 -16.551  1.00 52.43           N  
ANISOU 2046  N   VAL A 259     4945   8788   6189    426    -29   1992       N  
ATOM   2047  CA  VAL A 259       0.178  23.224 -17.759  1.00 53.99           C  
ANISOU 2047  CA  VAL A 259     5073   9078   6363    445      4   2054       C  
ATOM   2048  C   VAL A 259      -1.342  22.900 -17.758  1.00 54.95           C  
ANISOU 2048  C   VAL A 259     5276   9156   6445    440     21   1954       C  
ATOM   2049  O   VAL A 259      -1.727  21.748 -17.614  1.00 58.98           O  
ANISOU 2049  O   VAL A 259     5864   9662   6883    470     28   1850       O  
ATOM   2050  CB  VAL A 259       0.767  22.525 -18.968  1.00 52.32           C  
ANISOU 2050  CB  VAL A 259     4790   9037   6050    534     41   2087       C  
ATOM   2051  CG1 VAL A 259       0.074  23.052 -20.200  1.00 56.62           C  
ANISOU 2051  CG1 VAL A 259     5263   9684   6564    556     76   2151       C  
ATOM   2052  CG2 VAL A 259       2.240  22.811 -19.058  1.00 54.68           C  
ANISOU 2052  CG2 VAL A 259     4994   9406   6376    544     30   2195       C  
ATOM   2053  N   GLY A 260      -2.166  23.909 -17.946  1.00 51.84           N  
ANISOU 2053  N   GLY A 260     4860   8732   6103    402     21   1992       N  
ATOM   2054  CA  GLY A 260      -3.617  23.787 -17.851  1.00 56.40           C  
ANISOU 2054  CA  GLY A 260     5506   9265   6658    388     34   1907       C  
ATOM   2055  C   GLY A 260      -4.404  23.948 -19.171  1.00 58.66           C  
ANISOU 2055  C   GLY A 260     5743   9649   6895    422     71   1938       C  
ATOM   2056  O   GLY A 260      -3.881  24.432 -20.194  1.00 58.77           O  
ANISOU 2056  O   GLY A 260     5656   9768   6905    449     87   2046       O  
ATOM   2057  N   TYR A 261      -5.658  23.494 -19.133  1.00 51.58           N  
ANISOU 2057  N   TYR A 261     4915   8725   5957    421     85   1847       N  
ATOM   2058  CA  TYR A 261      -6.632  23.654 -20.186  1.00 48.85           C  
ANISOU 2058  CA  TYR A 261     4542   8445   5573    445    115   1855       C  
ATOM   2059  C   TYR A 261      -7.669  24.603 -19.620  1.00 50.45           C  
ANISOU 2059  C   TYR A 261     4769   8554   5845    386    100   1841       C  
ATOM   2060  O   TYR A 261      -8.216  24.401 -18.506  1.00 46.49           O  
ANISOU 2060  O   TYR A 261     4346   7958   5358    349     83   1758       O  
ATOM   2061  CB  TYR A 261      -7.348  22.348 -20.476  1.00 51.30           C  
ANISOU 2061  CB  TYR A 261     4919   8782   5791    488    128   1751       C  
ATOM   2062  CG  TYR A 261      -6.524  21.249 -21.124  1.00 60.04           C  
ANISOU 2062  CG  TYR A 261     6013   9984   6816    568    131   1733       C  
ATOM   2063  CD1 TYR A 261      -5.496  20.615 -20.434  1.00 65.06           C  
ANISOU 2063  CD1 TYR A 261     6676  10592   7450    575    107   1710       C  
ATOM   2064  CD2 TYR A 261      -6.838  20.776 -22.383  1.00 77.85           C  
ANISOU 2064  CD2 TYR A 261     8237  12352   8990    645    149   1723       C  
ATOM   2065  CE1 TYR A 261      -4.780  19.590 -21.012  1.00 73.34           C  
ANISOU 2065  CE1 TYR A 261     7716  11728   8422    659    100   1680       C  
ATOM   2066  CE2 TYR A 261      -6.109  19.757 -22.984  1.00 84.21           C  
ANISOU 2066  CE2 TYR A 261     9030  13251   9713    736    140   1690       C  
ATOM   2067  CZ  TYR A 261      -5.076  19.174 -22.300  1.00 81.27           C  
ANISOU 2067  CZ  TYR A 261     8682  12852   9343    744    115   1668       C  
ATOM   2068  OH  TYR A 261      -4.354  18.151 -22.879  1.00 86.18           O  
ANISOU 2068  OH  TYR A 261     9294  13567   9882    844     97   1625       O  
ATOM   2069  N   GLU A 262      -8.050  25.603 -20.403  1.00 52.23           N  
ANISOU 2069  N   GLU A 262     4927   8814   6104    381    105   1917       N  
ATOM   2070  CA  GLU A 262      -8.806  26.713 -19.815  1.00 49.98           C  
ANISOU 2070  CA  GLU A 262     4652   8433   5904    329     74   1914       C  
ATOM   2071  C   GLU A 262      -9.974  27.080 -20.690  1.00 49.60           C  
ANISOU 2071  C   GLU A 262     4584   8424   5836    340     96   1917       C  
ATOM   2072  O   GLU A 262      -9.928  26.905 -21.894  1.00 46.81           O  
ANISOU 2072  O   GLU A 262     4176   8177   5430    380    128   1969       O  
ATOM   2073  CB  GLU A 262      -7.850  27.862 -19.673  1.00 52.28           C  
ANISOU 2073  CB  GLU A 262     4872   8690   6300    299     27   2024       C  
ATOM   2074  CG  GLU A 262      -8.486  29.176 -19.481  1.00 54.00           C  
ANISOU 2074  CG  GLU A 262     5071   8830   6614    262    -20   2050       C  
ATOM   2075  CD  GLU A 262      -7.507  30.276 -19.242  1.00 52.15           C  
ANISOU 2075  CD  GLU A 262     4772   8539   6501    226    -89   2158       C  
ATOM   2076  OE1 GLU A 262      -6.289  30.098 -19.285  1.00 57.95           O  
ANISOU 2076  OE1 GLU A 262     5464   9306   7247    226    -94   2230       O  
ATOM   2077  OE2 GLU A 262      -7.982  31.340 -18.906  1.00 59.72           O1-
ANISOU 2077  OE2 GLU A 262     5727   9411   7553    198   -149   2163       O1-
ATOM   2078  N   THR A 263     -11.030  27.563 -20.067  1.00 49.70           N  
ANISOU 2078  N   THR A 263     4640   8359   5884    309     78   1855       N  
ATOM   2079  CA  THR A 263     -12.183  28.044 -20.806  1.00 54.34           C  
ANISOU 2079  CA  THR A 263     5209   8972   6465    315     92   1856       C  
ATOM   2080  C   THR A 263     -13.052  28.969 -19.975  1.00 51.67           C  
ANISOU 2080  C   THR A 263     4898   8538   6196    282     52   1809       C  
ATOM   2081  O   THR A 263     -12.984  28.965 -18.757  1.00 50.27           O  
ANISOU 2081  O   THR A 263     4770   8285   6042    263     23   1746       O  
ATOM   2082  CB  THR A 263     -13.058  26.914 -21.326  1.00 49.98           C  
ANISOU 2082  CB  THR A 263     4699   8480   5810    347    139   1781       C  
ATOM   2083  CG2 THR A 263     -14.040  26.525 -20.340  1.00 53.84           C  
ANISOU 2083  CG2 THR A 263     5265   8905   6284    322    137   1674       C  
ATOM   2084  OG1 THR A 263     -13.751  27.391 -22.452  1.00 52.95           O  
ANISOU 2084  OG1 THR A 263     5027   8916   6176    366    157   1822       O  
ATOM   2085  N   VAL A 264     -13.839  29.801 -20.640  1.00 48.32           N  
ANISOU 2085  N   VAL A 264     4436   8122   5801    282     44   1839       N  
ATOM   2086  CA  VAL A 264     -14.851  30.539 -19.876  1.00 52.39           C  
ANISOU 2086  CA  VAL A 264     4984   8559   6362    267      7   1768       C  
ATOM   2087  C   VAL A 264     -16.214  30.093 -20.274  1.00 51.82           C  
ANISOU 2087  C   VAL A 264     4938   8531   6219    282     51   1701       C  
ATOM   2088  O   VAL A 264     -16.550  30.154 -21.451  1.00 46.32           O  
ANISOU 2088  O   VAL A 264     4200   7898   5499    298     77   1749       O  
ATOM   2089  CB  VAL A 264     -14.773  32.046 -20.034  1.00 53.74           C  
ANISOU 2089  CB  VAL A 264     5098   8670   6650    252    -64   1839       C  
ATOM   2090  CG1 VAL A 264     -15.915  32.694 -19.289  1.00 55.24           C  
ANISOU 2090  CG1 VAL A 264     5325   8793   6870    255   -104   1744       C  
ATOM   2091  CG2 VAL A 264     -13.432  32.528 -19.486  1.00 54.89           C  
ANISOU 2091  CG2 VAL A 264     5218   8754   6881    231   -124   1904       C  
ATOM   2092  N   VAL A 265     -16.985  29.630 -19.276  1.00 50.85           N  
ANISOU 2092  N   VAL A 265     4879   8381   6059    275     58   1595       N  
ATOM   2093  CA  VAL A 265     -18.347  29.229 -19.527  1.00 52.15           C  
ANISOU 2093  CA  VAL A 265     5065   8585   6163    282     93   1532       C  
ATOM   2094  C   VAL A 265     -19.345  30.295 -19.167  1.00 50.65           C  
ANISOU 2094  C   VAL A 265     4867   8357   6018    285     59   1492       C  
ATOM   2095  O   VAL A 265     -19.209  30.949 -18.138  1.00 50.87           O  
ANISOU 2095  O   VAL A 265     4907   8323   6095    283      9   1456       O  
ATOM   2096  CB  VAL A 265     -18.747  27.881 -18.863  1.00 50.93           C  
ANISOU 2096  CB  VAL A 265     4974   8451   5926    273    128   1456       C  
ATOM   2097  CG1 VAL A 265     -18.000  26.736 -19.503  1.00 54.33           C  
ANISOU 2097  CG1 VAL A 265     5412   8925   6305    284    155   1484       C  
ATOM   2098  CG2 VAL A 265     -18.541  27.837 -17.384  1.00 48.37           C  
ANISOU 2098  CG2 VAL A 265     4691   8079   5609    256    104   1402       C  
ATOM   2099  N   GLY A 266     -20.343  30.452 -20.055  1.00 49.73           N  
ANISOU 2099  N   GLY A 266     4730   8283   5881    296     80   1493       N  
ATOM   2100  CA  GLY A 266     -21.521  31.232 -19.783  1.00 49.11           C  
ANISOU 2100  CA  GLY A 266     4648   8187   5822    305     58   1437       C  
ATOM   2101  C   GLY A 266     -22.838  30.500 -19.943  1.00 48.58           C  
ANISOU 2101  C   GLY A 266     4602   8179   5675    308    107   1375       C  
ATOM   2102  O   GLY A 266     -22.882  29.274 -20.202  1.00 49.20           O  
ANISOU 2102  O   GLY A 266     4705   8304   5683    299    153   1369       O  
ATOM   2103  N   PRO A 267     -23.949  31.252 -19.818  1.00 50.99           N  
ANISOU 2103  N   PRO A 267     4896   8483   5995    322     88   1328       N  
ATOM   2104  CA  PRO A 267     -25.310  30.666 -19.793  1.00 50.60           C  
ANISOU 2104  CA  PRO A 267     4859   8492   5873    322    129   1266       C  
ATOM   2105  C   PRO A 267     -25.496  29.759 -20.994  1.00 47.21           C  
ANISOU 2105  C   PRO A 267     4426   8114   5396    316    176   1303       C  
ATOM   2106  O   PRO A 267     -25.245  30.179 -22.081  1.00 47.11           O  
ANISOU 2106  O   PRO A 267     4380   8107   5410    331    173   1362       O  
ATOM   2107  CB  PRO A 267     -26.200  31.876 -19.914  1.00 49.67           C  
ANISOU 2107  CB  PRO A 267     4711   8361   5800    349     92   1238       C  
ATOM   2108  CG  PRO A 267     -25.419  32.976 -19.326  1.00 54.26           C  
ANISOU 2108  CG  PRO A 267     5283   8865   6467    364     19   1245       C  
ATOM   2109  CD  PRO A 267     -23.997  32.719 -19.747  1.00 51.84           C  
ANISOU 2109  CD  PRO A 267     4971   8531   6192    342     19   1334       C  
ATOM   2110  N   GLY A 268     -25.811  28.489 -20.781  1.00 46.54           N  
ANISOU 2110  N   GLY A 268     4374   8065   5243    297    210   1275       N  
ATOM   2111  CA  GLY A 268     -25.977  27.559 -21.885  1.00 44.05           C  
ANISOU 2111  CA  GLY A 268     4061   7790   4884    301    238   1296       C  
ATOM   2112  C   GLY A 268     -24.872  26.580 -22.175  1.00 43.37           C  
ANISOU 2112  C   GLY A 268     3996   7707   4774    303    243   1326       C  
ATOM   2113  O   GLY A 268     -25.096  25.547 -22.856  1.00 43.69           O  
ANISOU 2113  O   GLY A 268     4052   7780   4769    312    254   1319       O  
ATOM   2114  N   ASP A 269     -23.674  26.911 -21.710  1.00 46.09           N  
ANISOU 2114  N   ASP A 269     4341   8017   5154    303    227   1358       N  
ATOM   2115  CA  ASP A 269     -22.512  26.073 -21.924  1.00 42.53           C  
ANISOU 2115  CA  ASP A 269     3905   7572   4682    311    230   1386       C  
ATOM   2116  C   ASP A 269     -22.594  24.923 -20.873  1.00 48.64           C  
ANISOU 2116  C   ASP A 269     4734   8327   5418    279    228   1335       C  
ATOM   2117  O   ASP A 269     -23.080  25.125 -19.727  1.00 42.11           O  
ANISOU 2117  O   ASP A 269     3923   7479   4596    250    223   1298       O  
ATOM   2118  CB  ASP A 269     -21.282  26.895 -21.718  1.00 45.53           C  
ANISOU 2118  CB  ASP A 269     4260   7921   5119    315    210   1442       C  
ATOM   2119  CG  ASP A 269     -21.138  28.025 -22.731  1.00 44.80           C  
ANISOU 2119  CG  ASP A 269     4104   7846   5072    337    201   1515       C  
ATOM   2120  OD1 ASP A 269     -21.697  27.946 -23.824  1.00 43.38           O  
ANISOU 2120  OD1 ASP A 269     3899   7719   4861    361    220   1529       O  
ATOM   2121  OD2 ASP A 269     -20.448  28.991 -22.416  1.00 46.26           O1-
ANISOU 2121  OD2 ASP A 269     4261   7988   5326    328    169   1561       O1-
ATOM   2122  N   VAL A 270     -22.226  23.717 -21.319  1.00 45.07           N  
ANISOU 2122  N   VAL A 270     4307   7892   4926    290    226   1331       N  
ATOM   2123  CA  VAL A 270     -21.968  22.605 -20.441  1.00 44.83           C  
ANISOU 2123  CA  VAL A 270     4325   7834   4871    261    211   1302       C  
ATOM   2124  C   VAL A 270     -20.469  22.197 -20.635  1.00 43.60           C  
ANISOU 2124  C   VAL A 270     4177   7672   4715    289    199   1329       C  
ATOM   2125  O   VAL A 270     -20.025  21.983 -21.756  1.00 41.22           O  
ANISOU 2125  O   VAL A 270     3855   7411   4394    338    199   1349       O  
ATOM   2126  CB  VAL A 270     -22.939  21.487 -20.772  1.00 44.69           C  
ANISOU 2126  CB  VAL A 270     4333   7832   4816    249    199   1270       C  
ATOM   2127  CG1 VAL A 270     -22.606  20.212 -20.043  1.00 43.52           C  
ANISOU 2127  CG1 VAL A 270     4233   7651   4650    218    168   1253       C  
ATOM   2128  CG2 VAL A 270     -24.360  21.912 -20.428  1.00 47.38           C  
ANISOU 2128  CG2 VAL A 270     4659   8187   5156    216    214   1251       C  
ATOM   2129  N   LEU A 271     -19.707  22.142 -19.529  1.00 45.58           N  
ANISOU 2129  N   LEU A 271     4452   7881   4982    263    187   1328       N  
ATOM   2130  CA  LEU A 271     -18.307  21.700 -19.506  1.00 39.18           C  
ANISOU 2130  CA  LEU A 271     3651   7061   4172    284    173   1349       C  
ATOM   2131  C   LEU A 271     -18.287  20.301 -18.938  1.00 42.14           C  
ANISOU 2131  C   LEU A 271     4084   7411   4516    263    146   1310       C  
ATOM   2132  O   LEU A 271     -18.781  20.069 -17.858  1.00 40.22           O  
ANISOU 2132  O   LEU A 271     3870   7138   4272    213    139   1289       O  
ATOM   2133  CB  LEU A 271     -17.466  22.601 -18.648  1.00 41.49           C  
ANISOU 2133  CB  LEU A 271     3932   7317   4514    269    169   1375       C  
ATOM   2134  CG  LEU A 271     -16.025  22.089 -18.407  1.00 42.48           C  
ANISOU 2134  CG  LEU A 271     4070   7427   4640    282    153   1393       C  
ATOM   2135  CD1 LEU A 271     -15.237  21.998 -19.727  1.00 43.17           C  
ANISOU 2135  CD1 LEU A 271     4114   7577   4711    340    160   1438       C  
ATOM   2136  CD2 LEU A 271     -15.324  22.959 -17.395  1.00 44.13           C  
ANISOU 2136  CD2 LEU A 271     4274   7588   4904    260    139   1412       C  
ATOM   2137  N   TYR A 272     -17.782  19.367 -19.729  1.00 41.62           N  
ANISOU 2137  N   TYR A 272     4029   7364   4420    306    125   1300       N  
ATOM   2138  CA  TYR A 272     -17.555  18.045 -19.284  1.00 43.37           C  
ANISOU 2138  CA  TYR A 272     4304   7549   4623    294     81   1267       C  
ATOM   2139  C   TYR A 272     -16.244  18.095 -18.532  1.00 45.76           C  
ANISOU 2139  C   TYR A 272     4618   7825   4942    292     75   1283       C  
ATOM   2140  O   TYR A 272     -15.183  18.350 -19.141  1.00 43.37           O  
ANISOU 2140  O   TYR A 272     4284   7555   4638    345     82   1308       O  
ATOM   2141  CB  TYR A 272     -17.419  17.057 -20.471  1.00 43.35           C  
ANISOU 2141  CB  TYR A 272     4309   7576   4585    360     44   1238       C  
ATOM   2142  CG  TYR A 272     -16.927  15.674 -20.053  1.00 44.90           C  
ANISOU 2142  CG  TYR A 272     4562   7724   4773    359    -20   1201       C  
ATOM   2143  CD1 TYR A 272     -17.423  15.034 -18.903  1.00 45.75           C  
ANISOU 2143  CD1 TYR A 272     4716   7766   4898    281    -52   1194       C  
ATOM   2144  CD2 TYR A 272     -15.945  15.000 -20.793  1.00 44.32           C  
ANISOU 2144  CD2 TYR A 272     4492   7676   4672    441    -56   1176       C  
ATOM   2145  CE1 TYR A 272     -16.921  13.803 -18.504  1.00 45.14           C  
ANISOU 2145  CE1 TYR A 272     4689   7637   4823    276   -121   1170       C  
ATOM   2146  CE2 TYR A 272     -15.506  13.735 -20.421  1.00 43.52           C  
ANISOU 2146  CE2 TYR A 272     4445   7521   4569    445   -130   1136       C  
ATOM   2147  CZ  TYR A 272     -15.988  13.154 -19.269  1.00 47.48           C  
ANISOU 2147  CZ  TYR A 272     4995   7944   5100    358   -164   1136       C  
ATOM   2148  OH  TYR A 272     -15.486  11.941 -18.861  1.00 49.28           O  
ANISOU 2148  OH  TYR A 272     5277   8112   5336    358   -245   1106       O  
ATOM   2149  N   ILE A 273     -16.316  17.808 -17.227  1.00 46.54           N  
ANISOU 2149  N   ILE A 273     4756   7874   5052    234     61   1274       N  
ATOM   2150  CA  ILE A 273     -15.117  17.681 -16.357  1.00 44.00           C  
ANISOU 2150  CA  ILE A 273     4456   7517   4745    226     47   1281       C  
ATOM   2151  C   ILE A 273     -14.931  16.192 -16.091  1.00 43.71           C  
ANISOU 2151  C   ILE A 273     4474   7444   4688    217     -7   1252       C  
ATOM   2152  O   ILE A 273     -15.702  15.593 -15.341  1.00 43.39           O  
ANISOU 2152  O   ILE A 273     4467   7376   4644    159    -29   1245       O  
ATOM   2153  CB  ILE A 273     -15.284  18.438 -15.047  1.00 43.48           C  
ANISOU 2153  CB  ILE A 273     4393   7424   4701    176     63   1289       C  
ATOM   2154  CG1 ILE A 273     -15.674  19.889 -15.331  1.00 43.10           C  
ANISOU 2154  CG1 ILE A 273     4293   7400   4680    187     98   1307       C  
ATOM   2155  CG2 ILE A 273     -13.955  18.449 -14.292  1.00 46.01           C  
ANISOU 2155  CG2 ILE A 273     4729   7709   5040    178     47   1298       C  
ATOM   2156  CD1 ILE A 273     -15.679  20.817 -14.128  1.00 43.18           C  
ANISOU 2156  CD1 ILE A 273     4302   7385   4719    162    100   1303       C  
ATOM   2157  N   PRO A 274     -13.960  15.583 -16.740  1.00 41.56           N  
ANISOU 2157  N   PRO A 274     4207   7179   4404    275    -36   1240       N  
ATOM   2158  CA  PRO A 274     -13.821  14.144 -16.634  1.00 43.38           C  
ANISOU 2158  CA  PRO A 274     4491   7367   4622    277   -107   1204       C  
ATOM   2159  C   PRO A 274     -13.273  13.772 -15.282  1.00 44.00           C  
ANISOU 2159  C   PRO A 274     4611   7388   4716    224   -129   1211       C  
ATOM   2160  O   PRO A 274     -12.585  14.579 -14.691  1.00 45.77           O  
ANISOU 2160  O   PRO A 274     4819   7615   4956    217    -94   1234       O  
ATOM   2161  CB  PRO A 274     -12.767  13.773 -17.697  1.00 43.53           C  
ANISOU 2161  CB  PRO A 274     4495   7427   4617    375   -128   1182       C  
ATOM   2162  CG  PRO A 274     -12.490  15.024 -18.507  1.00 44.67           C  
ANISOU 2162  CG  PRO A 274     4566   7650   4755    419    -61   1222       C  
ATOM   2163  CD  PRO A 274     -12.954  16.184 -17.631  1.00 46.25           C  
ANISOU 2163  CD  PRO A 274     4751   7828   4993    346    -11   1262       C  
ATOM   2164  N   MET A 275     -13.643  12.584 -14.835  1.00 39.29           N  
ANISOU 2164  N   MET A 275     4064   6740   4122    186   -195   1195       N  
ATOM   2165  CA  MET A 275     -13.260  11.925 -13.598  1.00 45.18           C  
ANISOU 2165  CA  MET A 275     4857   7429   4880    131   -235   1205       C  
ATOM   2166  C   MET A 275     -11.780  12.130 -13.336  1.00 42.82           C  
ANISOU 2166  C   MET A 275     4561   7123   4585    172   -229   1200       C  
ATOM   2167  O   MET A 275     -10.987  11.912 -14.230  1.00 40.32           O  
ANISOU 2167  O   MET A 275     4234   6826   4259    248   -246   1175       O  
ATOM   2168  CB  MET A 275     -13.492  10.433 -13.869  1.00 54.07           C  
ANISOU 2168  CB  MET A 275     6029   8500   6013    129   -335   1179       C  
ATOM   2169  CG  MET A 275     -13.716   9.557 -12.713  1.00 66.93           C  
ANISOU 2169  CG  MET A 275     7701  10067   7659     47   -393   1206       C  
ATOM   2170  SD  MET A 275     -14.039   7.867 -13.298  1.00 78.28           S  
ANISOU 2170  SD  MET A 275     9188  11428   9126     52   -534   1175       S  
ATOM   2171  CE  MET A 275     -13.158   7.700 -14.831  1.00 71.32           C  
ANISOU 2171  CE  MET A 275     8301  10568   8226    195   -563   1092       C  
ATOM   2172  N   TYR A 276     -11.417  12.604 -12.150  1.00 44.32           N  
ANISOU 2172  N   TYR A 276     4758   7296   4785    127   -205   1225       N  
ATOM   2173  CA  TYR A 276     -10.011  12.823 -11.746  1.00 45.01           C  
ANISOU 2173  CA  TYR A 276     4847   7369   4883    156   -205   1225       C  
ATOM   2174  C   TYR A 276      -9.307  14.007 -12.373  1.00 47.31           C  
ANISOU 2174  C   TYR A 276     5081   7707   5185    209   -151   1241       C  
ATOM   2175  O   TYR A 276      -8.133  14.269 -12.022  1.00 49.18           O  
ANISOU 2175  O   TYR A 276     5312   7935   5438    227   -151   1251       O  
ATOM   2176  CB  TYR A 276      -9.162  11.558 -11.964  1.00 46.28           C  
ANISOU 2176  CB  TYR A 276     5050   7493   5042    192   -280   1194       C  
ATOM   2177  CG  TYR A 276      -9.533  10.401 -11.035  1.00 48.88           C  
ANISOU 2177  CG  TYR A 276     5440   7754   5377    127   -350   1194       C  
ATOM   2178  CD1 TYR A 276      -8.995  10.291  -9.750  1.00 55.20           C  
ANISOU 2178  CD1 TYR A 276     6270   8516   6185     81   -361   1213       C  
ATOM   2179  CD2 TYR A 276     -10.325   9.384 -11.471  1.00 55.16           C  
ANISOU 2179  CD2 TYR A 276     6261   8521   6175    114   -416   1180       C  
ATOM   2180  CE1 TYR A 276      -9.299   9.215  -8.913  1.00 57.25           C  
ANISOU 2180  CE1 TYR A 276     6579   8720   6451     18   -430   1229       C  
ATOM   2181  CE2 TYR A 276     -10.640   8.286 -10.642  1.00 61.94           C  
ANISOU 2181  CE2 TYR A 276     7170   9312   7051     46   -495   1197       C  
ATOM   2182  CZ  TYR A 276     -10.137   8.203  -9.371  1.00 61.96           C  
ANISOU 2182  CZ  TYR A 276     7197   9287   7057     -3   -499   1226       C  
ATOM   2183  OH  TYR A 276     -10.485   7.105  -8.590  1.00 71.99           O  
ANISOU 2183  OH  TYR A 276     8509  10497   8344    -75   -581   1258       O  
ATOM   2184  N   TRP A 277      -9.945  14.718 -13.316  1.00 40.14           N  
ANISOU 2184  N   TRP A 277     4126   6851   4273    232   -110   1252       N  
ATOM   2185  CA  TRP A 277      -9.355  15.944 -13.754  1.00 39.70           C  
ANISOU 2185  CA  TRP A 277     4009   6835   4238    264    -65   1287       C  
ATOM   2186  C   TRP A 277      -9.453  17.013 -12.684  1.00 40.80           C  
ANISOU 2186  C   TRP A 277     4141   6947   4413    216    -42   1308       C  
ATOM   2187  O   TRP A 277     -10.506  17.237 -12.048  1.00 40.39           O  
ANISOU 2187  O   TRP A 277     4104   6885   4357    171    -31   1297       O  
ATOM   2188  CB  TRP A 277      -9.940  16.472 -15.024  1.00 39.14           C  
ANISOU 2188  CB  TRP A 277     3886   6827   4155    302    -33   1301       C  
ATOM   2189  CG  TRP A 277      -9.503  15.720 -16.206  1.00 40.51           C  
ANISOU 2189  CG  TRP A 277     4048   7051   4293    377    -54   1283       C  
ATOM   2190  CD1 TRP A 277      -9.669  14.386 -16.440  1.00 40.07           C  
ANISOU 2190  CD1 TRP A 277     4040   6977   4206    400   -110   1230       C  
ATOM   2191  CD2 TRP A 277      -8.836  16.251 -17.336  1.00 40.55           C  
ANISOU 2191  CD2 TRP A 277     3983   7139   4282    447    -27   1318       C  
ATOM   2192  CE2 TRP A 277      -8.603  15.173 -18.226  1.00 42.43           C  
ANISOU 2192  CE2 TRP A 277     4230   7420   4469    524    -65   1273       C  
ATOM   2193  CE3 TRP A 277      -8.327  17.519 -17.656  1.00 40.96           C  
ANISOU 2193  CE3 TRP A 277     3962   7237   4363    454     15   1389       C  
ATOM   2194  NE1 TRP A 277      -9.101  14.047 -17.640  1.00 40.67           N  
ANISOU 2194  NE1 TRP A 277     4084   7123   4245    493   -121   1215       N  
ATOM   2195  CZ2 TRP A 277      -7.897  15.325 -19.418  1.00 42.92           C  
ANISOU 2195  CZ2 TRP A 277     4226   7589   4491    615    -49   1294       C  
ATOM   2196  CZ3 TRP A 277      -7.701  17.682 -18.896  1.00 40.48           C  
ANISOU 2196  CZ3 TRP A 277     3831   7280   4269    531     32   1426       C  
ATOM   2197  CH2 TRP A 277      -7.505  16.590 -19.754  1.00 41.79           C  
ANISOU 2197  CH2 TRP A 277     4004   7506   4368    614      5   1377       C  
ATOM   2198  N   TRP A 278      -8.322  17.655 -12.476  1.00 40.17           N  
ANISOU 2198  N   TRP A 278     4036   6859   4367    233    -40   1335       N  
ATOM   2199  CA  TRP A 278      -8.252  18.755 -11.569  1.00 41.90           C  
ANISOU 2199  CA  TRP A 278     4243   7046   4630    204    -34   1349       C  
ATOM   2200  C   TRP A 278      -8.994  19.875 -12.184  1.00 43.99           C  
ANISOU 2200  C   TRP A 278     4457   7339   4917    208     -6   1372       C  
ATOM   2201  O   TRP A 278      -8.825  20.134 -13.385  1.00 41.20           O  
ANISOU 2201  O   TRP A 278     4054   7033   4567    244     10   1407       O  
ATOM   2202  CB  TRP A 278      -6.802  19.248 -11.416  1.00 42.25           C  
ANISOU 2202  CB  TRP A 278     4259   7073   4719    223    -50   1384       C  
ATOM   2203  CG  TRP A 278      -5.875  18.249 -10.764  1.00 43.31           C  
ANISOU 2203  CG  TRP A 278     4440   7176   4839    224    -82   1363       C  
ATOM   2204  CD1 TRP A 278      -5.173  17.249 -11.378  1.00 43.40           C  
ANISOU 2204  CD1 TRP A 278     4459   7211   4820    263    -97   1357       C  
ATOM   2205  CD2 TRP A 278      -5.546  18.181  -9.384  1.00 40.18           C  
ANISOU 2205  CD2 TRP A 278     4088   6722   4454    191   -108   1343       C  
ATOM   2206  CE2 TRP A 278      -4.664  17.112  -9.220  1.00 41.73           C  
ANISOU 2206  CE2 TRP A 278     4319   6903   4633    204   -137   1329       C  
ATOM   2207  CE3 TRP A 278      -5.947  18.909  -8.257  1.00 43.65           C  
ANISOU 2207  CE3 TRP A 278     4542   7128   4914    160   -114   1327       C  
ATOM   2208  NE1 TRP A 278      -4.449  16.550 -10.451  1.00 43.03           N  
ANISOU 2208  NE1 TRP A 278     4461   7116   4773    251   -133   1335       N  
ATOM   2209  CZ2 TRP A 278      -4.162  16.749  -7.983  1.00 40.51           C  
ANISOU 2209  CZ2 TRP A 278     4213   6696   4482    178   -168   1311       C  
ATOM   2210  CZ3 TRP A 278      -5.408  18.573  -7.029  1.00 41.46           C  
ANISOU 2210  CZ3 TRP A 278     4309   6808   4634    142   -144   1306       C  
ATOM   2211  CH2 TRP A 278      -4.537  17.489  -6.911  1.00 40.85           C  
ANISOU 2211  CH2 TRP A 278     4266   6712   4541    147   -168   1302       C  
ATOM   2212  N   HIS A 279      -9.740  20.616 -11.362  1.00 44.07           N  
ANISOU 2212  N   HIS A 279     4474   7327   4943    179     -5   1353       N  
ATOM   2213  CA  HIS A 279     -10.317  21.832 -11.855  1.00 44.56           C  
ANISOU 2213  CA  HIS A 279     4486   7402   5041    187      8   1373       C  
ATOM   2214  C   HIS A 279     -10.291  22.914 -10.829  1.00 44.66           C  
ANISOU 2214  C   HIS A 279     4496   7370   5103    178    -19   1359       C  
ATOM   2215  O   HIS A 279     -10.396  22.657  -9.640  1.00 46.72           O  
ANISOU 2215  O   HIS A 279     4798   7609   5342    162    -33   1317       O  
ATOM   2216  CB  HIS A 279     -11.772  21.600 -12.361  1.00 43.80           C  
ANISOU 2216  CB  HIS A 279     4391   7347   4901    180     36   1350       C  
ATOM   2217  CG  HIS A 279     -12.581  20.727 -11.486  1.00 43.07           C  
ANISOU 2217  CG  HIS A 279     4350   7255   4757    146     35   1307       C  
ATOM   2218  CD2 HIS A 279     -13.635  20.992 -10.688  1.00 43.34           C  
ANISOU 2218  CD2 HIS A 279     4393   7304   4770    123     42   1277       C  
ATOM   2219  ND1 HIS A 279     -12.339  19.376 -11.369  1.00 44.49           N  
ANISOU 2219  ND1 HIS A 279     4574   7430   4901    132     21   1298       N  
ATOM   2220  CE1 HIS A 279     -13.194  18.852 -10.511  1.00 42.06           C  
ANISOU 2220  CE1 HIS A 279     4296   7127   4555     92     18   1277       C  
ATOM   2221  NE2 HIS A 279     -13.982  19.809 -10.075  1.00 42.39           N  
ANISOU 2221  NE2 HIS A 279     4314   7190   4599     88     36   1265       N  
ATOM   2222  N   HIS A 280     -10.110  24.121 -11.334  1.00 46.52           N  
ANISOU 2222  N   HIS A 280     4677   7593   5403    192    -33   1397       N  
ATOM   2223  CA  HIS A 280     -10.004  25.356 -10.576  1.00 47.49           C  
ANISOU 2223  CA  HIS A 280     4787   7661   5596    195    -80   1387       C  
ATOM   2224  C   HIS A 280     -11.054  26.251 -11.192  1.00 49.50           C  
ANISOU 2224  C   HIS A 280     5004   7931   5870    204    -76   1388       C  
ATOM   2225  O   HIS A 280     -11.095  26.348 -12.406  1.00 49.90           O  
ANISOU 2225  O   HIS A 280     5013   8016   5929    209    -53   1443       O  
ATOM   2226  CB  HIS A 280      -8.665  25.965 -10.842  1.00 44.09           C  
ANISOU 2226  CB  HIS A 280     4313   7191   5246    199   -118   1455       C  
ATOM   2227  CG  HIS A 280      -8.600  27.426 -10.582  1.00 46.07           C  
ANISOU 2227  CG  HIS A 280     4528   7379   5595    204   -182   1468       C  
ATOM   2228  CD2 HIS A 280      -9.087  28.485 -11.272  1.00 51.09           C  
ANISOU 2228  CD2 HIS A 280     5113   8007   6289    208   -203   1504       C  
ATOM   2229  ND1 HIS A 280      -7.917  27.956  -9.521  1.00 49.38           N  
ANISOU 2229  ND1 HIS A 280     4962   7726   6074    206   -248   1446       N  
ATOM   2230  CE1 HIS A 280      -8.011  29.274  -9.541  1.00 49.54           C  
ANISOU 2230  CE1 HIS A 280     4945   7689   6189    214   -315   1461       C  
ATOM   2231  NE2 HIS A 280      -8.701  29.619 -10.606  1.00 50.17           N  
ANISOU 2231  NE2 HIS A 280     4983   7805   6271    213   -289   1501       N  
ATOM   2232  N   ILE A 281     -11.937  26.852 -10.391  1.00 54.97           N  
ANISOU 2232  N   ILE A 281     5711   8611   6563    212    -98   1325       N  
ATOM   2233  CA  ILE A 281     -13.141  27.492 -10.948  1.00 53.76           C  
ANISOU 2233  CA  ILE A 281     5532   8485   6410    223    -87   1312       C  
ATOM   2234  C   ILE A 281     -13.328  28.845 -10.333  1.00 52.35           C  
ANISOU 2234  C   ILE A 281     5337   8251   6301    249   -157   1277       C  
ATOM   2235  O   ILE A 281     -13.453  28.967  -9.111  1.00 47.74           O  
ANISOU 2235  O   ILE A 281     4784   7653   5700    268   -188   1206       O  
ATOM   2236  CB  ILE A 281     -14.380  26.587 -10.768  1.00 55.06           C  
ANISOU 2236  CB  ILE A 281     5727   8717   6475    214    -34   1262       C  
ATOM   2237  CG1 ILE A 281     -14.184  25.363 -11.667  1.00 57.79           C  
ANISOU 2237  CG1 ILE A 281     6082   9101   6773    195     13   1302       C  
ATOM   2238  CG2 ILE A 281     -15.636  27.313 -11.199  1.00 55.49           C  
ANISOU 2238  CG2 ILE A 281     5753   8799   6529    229    -28   1239       C  
ATOM   2239  CD1 ILE A 281     -15.311  24.392 -11.695  1.00 63.65           C  
ANISOU 2239  CD1 ILE A 281     6849   9899   7436    177     52   1272       C  
ATOM   2240  N   GLU A 282     -13.301  29.877 -11.169  1.00 49.46           N  
ANISOU 2240  N   GLU A 282     4921   7855   6017    255   -191   1326       N  
ATOM   2241  CA  GLU A 282     -13.454  31.224 -10.608  1.00 51.84           C  
ANISOU 2241  CA  GLU A 282     5207   8085   6402    285   -281   1289       C  
ATOM   2242  C   GLU A 282     -14.594  31.987 -11.311  1.00 52.34           C  
ANISOU 2242  C   GLU A 282     5239   8165   6483    301   -287   1281       C  
ATOM   2243  O   GLU A 282     -14.695  31.961 -12.544  1.00 52.12           O  
ANISOU 2243  O   GLU A 282     5174   8165   6464    282   -252   1356       O  
ATOM   2244  CB  GLU A 282     -12.130  32.012 -10.653  1.00 56.55           C  
ANISOU 2244  CB  GLU A 282     5772   8592   7121    276   -363   1359       C  
ATOM   2245  CG  GLU A 282     -11.641  32.386 -12.047  1.00 58.30           C  
ANISOU 2245  CG  GLU A 282     5927   8815   7408    248   -360   1485       C  
ATOM   2246  CD  GLU A 282     -10.178  32.870 -12.118  1.00 59.09           C  
ANISOU 2246  CD  GLU A 282     5986   8850   7615    226   -425   1581       C  
ATOM   2247  OE1 GLU A 282      -9.319  32.330 -11.428  1.00 61.93           O  
ANISOU 2247  OE1 GLU A 282     6374   9194   7963    221   -426   1570       O  
ATOM   2248  OE2 GLU A 282      -9.850  33.764 -12.914  1.00 58.76           O1-
ANISOU 2248  OE2 GLU A 282     5878   8776   7670    209   -474   1681       O1-
ATOM   2249  N   SER A 283     -15.454  32.635 -10.521  1.00 48.97           N  
ANISOU 2249  N   SER A 283     4824   7729   6052    344   -332   1186       N  
ATOM   2250  CA  SER A 283     -16.500  33.492 -11.086  1.00 52.08           C  
ANISOU 2250  CA  SER A 283     5188   8126   6473    367   -355   1168       C  
ATOM   2251  C   SER A 283     -15.854  34.829 -11.467  1.00 53.18           C  
ANISOU 2251  C   SER A 283     5286   8157   6762    371   -466   1223       C  
ATOM   2252  O   SER A 283     -15.171  35.419 -10.631  1.00 50.89           O  
ANISOU 2252  O   SER A 283     5004   7786   6543    392   -558   1195       O  
ATOM   2253  CB  SER A 283     -17.634  33.722 -10.084  1.00 53.56           C  
ANISOU 2253  CB  SER A 283     5397   8354   6598    423   -371   1042       C  
ATOM   2254  OG  SER A 283     -18.342  32.535  -9.798  1.00 48.17           O  
ANISOU 2254  OG  SER A 283     4740   7778   5784    410   -273   1011       O  
ATOM   2255  N   LEU A 284     -16.029  35.266 -12.724  1.00 52.72           N  
ANISOU 2255  N   LEU A 284     5179   8097   6753    349   -462   1309       N  
ATOM   2256  CA  LEU A 284     -15.328  36.467 -13.228  1.00 63.46           C  
ANISOU 2256  CA  LEU A 284     6488   9358   8264    336   -569   1398       C  
ATOM   2257  C   LEU A 284     -15.422  37.658 -12.297  1.00 63.05           C  
ANISOU 2257  C   LEU A 284     6445   9200   8311    383   -711   1317       C  
ATOM   2258  O   LEU A 284     -16.362  37.788 -11.552  1.00 72.10           O  
ANISOU 2258  O   LEU A 284     7624  10367   9405    439   -724   1190       O  
ATOM   2259  CB  LEU A 284     -15.824  36.885 -14.597  1.00 65.32           C  
ANISOU 2259  CB  LEU A 284     6671   9618   8529    317   -553   1484       C  
ATOM   2260  CG  LEU A 284     -15.522  35.929 -15.742  1.00 68.50           C  
ANISOU 2260  CG  LEU A 284     7048  10116   8860    278   -440   1585       C  
ATOM   2261  CD1 LEU A 284     -15.201  36.687 -17.021  1.00 68.76           C  
ANISOU 2261  CD1 LEU A 284     7003  10141   8980    250   -471   1728       C  
ATOM   2262  CD2 LEU A 284     -14.413  34.948 -15.403  1.00 63.70           C  
ANISOU 2262  CD2 LEU A 284     6459   9534   8209    257   -393   1612       C  
ATOM   2263  N   LEU A 285     -14.396  38.490 -12.309  1.00 67.96           N  
ANISOU 2263  N   LEU A 285     7034   9712   9073    364   -823   1391       N  
ATOM   2264  CA  LEU A 285     -14.368  39.658 -11.444  1.00 68.33           C  
ANISOU 2264  CA  LEU A 285     7090   9638   9233    413   -984   1314       C  
ATOM   2265  C   LEU A 285     -15.338  40.663 -12.019  1.00 68.40           C  
ANISOU 2265  C   LEU A 285     7070   9612   9304    438  -1053   1302       C  
ATOM   2266  O   LEU A 285     -15.524  40.751 -13.234  1.00 63.48           O  
ANISOU 2266  O   LEU A 285     6401   9018   8700    395  -1012   1411       O  
ATOM   2267  CB  LEU A 285     -12.951  40.245 -11.376  1.00 72.39           C  
ANISOU 2267  CB  LEU A 285     7572  10036   9897    375  -1095   1415       C  
ATOM   2268  CG  LEU A 285     -11.839  39.342 -10.840  1.00 69.10           C  
ANISOU 2268  CG  LEU A 285     7176   9640   9437    349  -1042   1439       C  
ATOM   2269  CD1 LEU A 285     -10.522  39.656 -11.520  1.00 73.97           C  
ANISOU 2269  CD1 LEU A 285     7728  10201  10175    280  -1088   1613       C  
ATOM   2270  CD2 LEU A 285     -11.680  39.452  -9.336  1.00 70.54           C  
ANISOU 2270  CD2 LEU A 285     7417   9768   9616    409  -1118   1299       C  
ATOM   2271  N   ASN A 286     -16.040  41.347 -11.134  1.00 74.68           N  
ANISOU 2271  N   ASN A 286     7895  10364  10115    518  -1149   1157       N  
ATOM   2272  CA  ASN A 286     -17.012  42.329 -11.548  1.00 78.79           C  
ANISOU 2272  CA  ASN A 286     8395  10847  10694    556  -1229   1121       C  
ATOM   2273  C   ASN A 286     -17.985  41.760 -12.584  1.00 76.60           C  
ANISOU 2273  C   ASN A 286     8100  10689  10314    531  -1090   1158       C  
ATOM   2274  O   ASN A 286     -18.539  42.507 -13.375  1.00 81.69           O  
ANISOU 2274  O   ASN A 286     8710  11301  11025    530  -1139   1194       O  
ATOM   2275  CB  ASN A 286     -16.295  43.612 -12.059  1.00 83.16           C  
ANISOU 2275  CB  ASN A 286     8897  11240  11458    525  -1402   1229       C  
ATOM   2276  CG  ASN A 286     -15.646  44.401 -10.921  1.00 87.61           C  
ANISOU 2276  CG  ASN A 286     9483  11666  12138    575  -1580   1150       C  
ATOM   2277  ND2 ASN A 286     -14.312  44.389 -10.831  1.00 81.27           N  
ANISOU 2277  ND2 ASN A 286     8662  10792  11426    519  -1625   1254       N  
ATOM   2278  OD1 ASN A 286     -16.353  44.978 -10.108  1.00 96.58           O  
ANISOU 2278  OD1 ASN A 286    10650  12770  13274    672  -1676    990       O  
ATOM   2279  N   GLY A 287     -18.211  40.447 -12.563  1.00 68.70           N  
ANISOU 2279  N   GLY A 287     7126   9819   9158    513   -928   1146       N  
ATOM   2280  CA  GLY A 287     -19.159  39.794 -13.473  1.00 60.29           C  
ANISOU 2280  CA  GLY A 287     6050   8868   7989    493   -799   1168       C  
ATOM   2281  C   GLY A 287     -20.554  39.606 -12.876  1.00 60.95           C  
ANISOU 2281  C   GLY A 287     6162   9036   7961    559   -761   1022       C  
ATOM   2282  O   GLY A 287     -21.486  39.151 -13.563  1.00 62.28           O  
ANISOU 2282  O   GLY A 287     6322   9293   8049    549   -668   1027       O  
ATOM   2283  N   GLY A 288     -20.724  39.963 -11.602  1.00 62.42           N  
ANISOU 2283  N   GLY A 288     6376   9202   8135    632   -834    891       N  
ATOM   2284  CA  GLY A 288     -21.986  39.714 -10.890  1.00 63.88           C  
ANISOU 2284  CA  GLY A 288     6579   9496   8194    701   -792    753       C  
ATOM   2285  C   GLY A 288     -22.073  38.300 -10.329  1.00 65.07           C  
ANISOU 2285  C   GLY A 288     6758   9772   8191    679   -655    737       C  
ATOM   2286  O   GLY A 288     -21.094  37.587 -10.306  1.00 61.95           O  
ANISOU 2286  O   GLY A 288     6380   9365   7792    624   -612    808       O  
ATOM   2287  N   ILE A 289     -23.267  37.882  -9.916  1.00 65.45           N  
ANISOU 2287  N   ILE A 289     6808   9945   8114    719   -590    653       N  
ATOM   2288  CA  ILE A 289     -23.430  36.572  -9.358  1.00 64.97           C  
ANISOU 2288  CA  ILE A 289     6767  10002   7914    693   -474    648       C  
ATOM   2289  C   ILE A 289     -23.408  35.506 -10.444  1.00 62.50           C  
ANISOU 2289  C   ILE A 289     6452   9727   7566    601   -358    761       C  
ATOM   2290  O   ILE A 289     -23.783  35.758 -11.614  1.00 59.70           O  
ANISOU 2290  O   ILE A 289     6073   9357   7252    577   -344    816       O  
ATOM   2291  CB  ILE A 289     -24.697  36.453  -8.508  1.00 66.35           C  
ANISOU 2291  CB  ILE A 289     6932  10312   7964    762   -446    536       C  
ATOM   2292  CG1 ILE A 289     -25.944  36.546  -9.348  1.00 69.20           C  
ANISOU 2292  CG1 ILE A 289     7260  10736   8296    762   -402    537       C  
ATOM   2293  CG2 ILE A 289     -24.705  37.531  -7.448  1.00 69.00           C  
ANISOU 2293  CG2 ILE A 289     7269  10620   8329    873   -572    410       C  
ATOM   2294  CD1 ILE A 289     -27.113  35.894  -8.646  1.00 77.53           C  
ANISOU 2294  CD1 ILE A 289     8298  11960   9199    793   -326    474       C  
ATOM   2295  N   THR A 290     -22.981  34.305 -10.057  1.00 57.09           N  
ANISOU 2295  N   THR A 290     5793   9093   6803    557   -281    791       N  
ATOM   2296  CA  THR A 290     -22.935  33.199 -11.008  1.00 52.65           C  
ANISOU 2296  CA  THR A 290     5233   8565   6203    481   -183    883       C  
ATOM   2297  C   THR A 290     -23.833  32.136 -10.529  1.00 48.40           C  
ANISOU 2297  C   THR A 290     4702   8148   5537    468   -102    855       C  
ATOM   2298  O   THR A 290     -24.030  32.015  -9.350  1.00 52.96           O  
ANISOU 2298  O   THR A 290     5288   8781   6051    501   -108    792       O  
ATOM   2299  CB  THR A 290     -21.518  32.613 -11.138  1.00 52.52           C  
ANISOU 2299  CB  THR A 290     5240   8491   6222    432   -175    960       C  
ATOM   2300  CG2 THR A 290     -20.586  33.633 -11.705  1.00 54.57           C  
ANISOU 2300  CG2 THR A 290     5480   8639   6614    433   -255   1014       C  
ATOM   2301  OG1 THR A 290     -21.035  32.191  -9.860  1.00 53.07           O  
ANISOU 2301  OG1 THR A 290     5341   8573   6247    443   -183    916       O  
ATOM   2302  N   ILE A 291     -24.389  31.352 -11.437  1.00 46.57           N  
ANISOU 2302  N   ILE A 291     4464   7963   5267    421    -30    907       N  
ATOM   2303  CA  ILE A 291     -25.193  30.251 -11.048  1.00 45.53           C  
ANISOU 2303  CA  ILE A 291     4334   7936   5028    394     38    901       C  
ATOM   2304  C   ILE A 291     -24.832  29.107 -11.931  1.00 43.64           C  
ANISOU 2304  C   ILE A 291     4112   7686   4780    326     91    982       C  
ATOM   2305  O   ILE A 291     -24.689  29.275 -13.171  1.00 46.83           O  
ANISOU 2305  O   ILE A 291     4507   8050   5235    315     95   1028       O  
ATOM   2306  CB  ILE A 291     -26.703  30.541 -11.201  1.00 49.47           C  
ANISOU 2306  CB  ILE A 291     4794   8521   5478    420     58    858       C  
ATOM   2307  CG1 ILE A 291     -27.110  31.737 -10.353  1.00 52.47           C  
ANISOU 2307  CG1 ILE A 291     5154   8919   5862    506     -4    762       C  
ATOM   2308  CG2 ILE A 291     -27.542  29.332 -10.823  1.00 48.21           C  
ANISOU 2308  CG2 ILE A 291     4628   8475   5213    379    126    874       C  
ATOM   2309  CD1 ILE A 291     -28.537  32.175 -10.637  1.00 55.63           C  
ANISOU 2309  CD1 ILE A 291     5512   9398   6226    543      6    717       C  
ATOM   2310  N   THR A 292     -24.746  27.926 -11.328  1.00 39.89           N  
ANISOU 2310  N   THR A 292     3661   7256   4239    287    127    998       N  
ATOM   2311  CA  THR A 292     -24.360  26.749 -12.031  1.00 40.87           C  
ANISOU 2311  CA  THR A 292     3807   7364   4354    231    160   1061       C  
ATOM   2312  C   THR A 292     -25.072  25.573 -11.413  1.00 43.45           C  
ANISOU 2312  C   THR A 292     4140   7769   4598    188    193   1069       C  
ATOM   2313  O   THR A 292     -25.362  25.563 -10.198  1.00 49.78           O  
ANISOU 2313  O   THR A 292     4935   8632   5346    197    193   1040       O  
ATOM   2314  CB  THR A 292     -22.832  26.528 -11.816  1.00 42.28           C  
ANISOU 2314  CB  THR A 292     4021   7470   4574    222    136   1089       C  
ATOM   2315  CG2 THR A 292     -22.345  25.361 -12.634  1.00 41.69           C  
ANISOU 2315  CG2 THR A 292     3968   7377   4493    182    160   1144       C  
ATOM   2316  OG1 THR A 292     -22.106  27.690 -12.219  1.00 40.20           O  
ANISOU 2316  OG1 THR A 292     3744   7135   4395    257     94   1093       O  
ATOM   2317  N   VAL A 293     -25.371  24.573 -12.218  1.00 42.37           N  
ANISOU 2317  N   VAL A 293     4010   7637   4449    144    216   1113       N  
ATOM   2318  CA  VAL A 293     -25.857  23.309 -11.674  1.00 46.43           C  
ANISOU 2318  CA  VAL A 293     4533   8204   4904     89    231   1141       C  
ATOM   2319  C   VAL A 293     -24.979  22.235 -12.254  1.00 48.12           C  
ANISOU 2319  C   VAL A 293     4789   8352   5141     54    218   1183       C  
ATOM   2320  O   VAL A 293     -24.762  22.221 -13.507  1.00 43.05           O  
ANISOU 2320  O   VAL A 293     4151   7669   4537     68    216   1194       O  
ATOM   2321  CB  VAL A 293     -27.328  22.982 -12.058  1.00 50.08           C  
ANISOU 2321  CB  VAL A 293     4958   8740   5330     65    254   1152       C  
ATOM   2322  CG1 VAL A 293     -27.599  21.502 -11.876  1.00 50.34           C  
ANISOU 2322  CG1 VAL A 293     5004   8791   5332     -6    250   1206       C  
ATOM   2323  CG2 VAL A 293     -28.334  23.771 -11.200  1.00 52.74           C  
ANISOU 2323  CG2 VAL A 293     5246   9176   5616     96    269   1111       C  
ATOM   2324  N   ASN A 294     -24.474  21.336 -11.393  1.00 47.85           N  
ANISOU 2324  N   ASN A 294     4784   8314   5082     17    205   1205       N  
ATOM   2325  CA  ASN A 294     -23.665  20.234 -11.928  1.00 49.69           C  
ANISOU 2325  CA  ASN A 294     5059   8483   5337     -8    181   1236       C  
ATOM   2326  C   ASN A 294     -24.421  18.957 -11.841  1.00 47.85           C  
ANISOU 2326  C   ASN A 294     4830   8273   5076    -70    166   1273       C  
ATOM   2327  O   ASN A 294     -25.456  18.885 -11.197  1.00 52.47           O  
ANISOU 2327  O   ASN A 294     5382   8932   5619   -101    179   1289       O  
ATOM   2328  CB  ASN A 294     -22.275  20.140 -11.293  1.00 44.98           C  
ANISOU 2328  CB  ASN A 294     4498   7833   4756      0    161   1236       C  
ATOM   2329  CG  ASN A 294     -22.292  19.650  -9.841  1.00 49.47           C  
ANISOU 2329  CG  ASN A 294     5078   8438   5280    -36    154   1247       C  
ATOM   2330  ND2 ASN A 294     -21.151  19.846  -9.135  1.00 48.37           N  
ANISOU 2330  ND2 ASN A 294     4965   8260   5152    -19    139   1236       N  
ATOM   2331  OD1 ASN A 294     -23.280  19.119  -9.352  1.00 45.68           O  
ANISOU 2331  OD1 ASN A 294     4578   8023   4754    -78    161   1272       O  
ATOM   2332  N   PHE A 295     -23.875  17.955 -12.509  1.00 49.67           N  
ANISOU 2332  N   PHE A 295     5097   8443   5332    -84    129   1290       N  
ATOM   2333  CA  PHE A 295     -24.459  16.637 -12.665  1.00 47.70           C  
ANISOU 2333  CA  PHE A 295     4859   8183   5079   -140     88   1326       C  
ATOM   2334  C   PHE A 295     -23.315  15.682 -12.459  1.00 51.42           C  
ANISOU 2334  C   PHE A 295     5383   8585   5568   -152     39   1336       C  
ATOM   2335  O   PHE A 295     -22.467  15.526 -13.375  1.00 47.64           O  
ANISOU 2335  O   PHE A 295     4931   8052   5118   -105     19   1310       O  
ATOM   2336  CB  PHE A 295     -24.948  16.429 -14.100  1.00 49.74           C  
ANISOU 2336  CB  PHE A 295     5113   8423   5362   -119     73   1312       C  
ATOM   2337  CG  PHE A 295     -26.138  17.283 -14.499  1.00 47.12           C  
ANISOU 2337  CG  PHE A 295     4731   8152   5017   -107    115   1302       C  
ATOM   2338  CD1 PHE A 295     -26.018  18.653 -14.627  1.00 46.92           C  
ANISOU 2338  CD1 PHE A 295     4681   8151   4994    -54    161   1270       C  
ATOM   2339  CD2 PHE A 295     -27.375  16.691 -14.795  1.00 50.68           C  
ANISOU 2339  CD2 PHE A 295     5158   8631   5464   -150     97   1326       C  
ATOM   2340  CE1 PHE A 295     -27.077  19.430 -14.987  1.00 46.11           C  
ANISOU 2340  CE1 PHE A 295     4535   8100   4883    -39    191   1255       C  
ATOM   2341  CE2 PHE A 295     -28.447  17.457 -15.217  1.00 45.54           C  
ANISOU 2341  CE2 PHE A 295     4462   8037   4803   -135    133   1313       C  
ATOM   2342  CZ  PHE A 295     -28.317  18.836 -15.250  1.00 48.16           C  
ANISOU 2342  CZ  PHE A 295     4771   8396   5129    -78    182   1275       C  
ATOM   2343  N   TRP A 296     -23.256  15.070 -11.265  1.00 49.23           N  
ANISOU 2343  N   TRP A 296     5115   8317   5270   -207     20   1374       N  
ATOM   2344  CA  TRP A 296     -22.229  14.076 -10.951  1.00 48.87           C  
ANISOU 2344  CA  TRP A 296     5121   8202   5243   -224    -35   1387       C  
ATOM   2345  C   TRP A 296     -22.736  12.628 -11.212  1.00 51.11           C  
ANISOU 2345  C   TRP A 296     5424   8443   5550   -284   -115   1428       C  
ATOM   2346  O   TRP A 296     -23.866  12.282 -10.816  1.00 55.10           O  
ANISOU 2346  O   TRP A 296     5896   8997   6043   -349   -123   1481       O  
ATOM   2347  CB  TRP A 296     -21.796  14.251  -9.502  1.00 52.94           C  
ANISOU 2347  CB  TRP A 296     5640   8748   5727   -248    -19   1407       C  
ATOM   2348  CG  TRP A 296     -20.729  15.296  -9.259  1.00 55.12           C  
ANISOU 2348  CG  TRP A 296     5924   9012   6006   -185     15   1361       C  
ATOM   2349  CD1 TRP A 296     -19.754  15.617 -10.076  1.00 63.33           C  
ANISOU 2349  CD1 TRP A 296     6984   9997   7082   -130     13   1327       C  
ATOM   2350  CD2 TRP A 296     -20.516  16.059  -8.079  1.00 62.62           C  
ANISOU 2350  CD2 TRP A 296     6861  10007   6922   -175     46   1352       C  
ATOM   2351  CE2 TRP A 296     -19.407  16.887  -8.316  1.00 55.48           C  
ANISOU 2351  CE2 TRP A 296     5971   9056   6051   -115     55   1310       C  
ATOM   2352  CE3 TRP A 296     -21.207  16.188  -6.865  1.00 77.99           C  
ANISOU 2352  CE3 TRP A 296     8778  12042   8812   -203     65   1375       C  
ATOM   2353  NE1 TRP A 296     -18.953  16.576  -9.541  1.00 60.09           N  
ANISOU 2353  NE1 TRP A 296     6570   9584   6674    -93     38   1303       N  
ATOM   2354  CZ2 TRP A 296     -18.912  17.789  -7.388  1.00 63.20           C  
ANISOU 2354  CZ2 TRP A 296     6943  10050   7019    -84     70   1285       C  
ATOM   2355  CZ3 TRP A 296     -20.723  17.108  -5.915  1.00 80.14           C  
ANISOU 2355  CZ3 TRP A 296     9045  12345   9059   -160     85   1340       C  
ATOM   2356  CH2 TRP A 296     -19.563  17.880  -6.185  1.00 75.76           C  
ANISOU 2356  CH2 TRP A 296     8513  11719   8551   -103     82   1292       C  
ATOM   2357  N   TYR A 297     -21.921  11.819 -11.886  1.00 47.61           N  
ANISOU 2357  N   TYR A 297     5029   7916   5145   -259   -180   1404       N  
ATOM   2358  CA  TYR A 297     -22.179  10.404 -12.204  1.00 49.24           C  
ANISOU 2358  CA  TYR A 297     5264   8055   5389   -300   -284   1427       C  
ATOM   2359  C   TYR A 297     -21.020   9.557 -11.741  1.00 55.22           C  
ANISOU 2359  C   TYR A 297     6075   8738   6166   -303   -350   1426       C  
ATOM   2360  O   TYR A 297     -19.862   9.941 -11.856  1.00 55.21           O  
ANISOU 2360  O   TYR A 297     6096   8719   6159   -239   -327   1381       O  
ATOM   2361  CB  TYR A 297     -22.348  10.125 -13.701  1.00 48.93           C  
ANISOU 2361  CB  TYR A 297     5234   7976   5377   -242   -326   1376       C  
ATOM   2362  CG  TYR A 297     -23.577  10.774 -14.316  1.00 53.86           C  
ANISOU 2362  CG  TYR A 297     5810   8661   5991   -241   -279   1376       C  
ATOM   2363  CD1 TYR A 297     -23.564  12.106 -14.699  1.00 51.04           C  
ANISOU 2363  CD1 TYR A 297     5420   8365   5606   -184   -186   1343       C  
ATOM   2364  CD2 TYR A 297     -24.774  10.051 -14.461  1.00 55.32           C  
ANISOU 2364  CD2 TYR A 297     5977   8839   6201   -304   -337   1417       C  
ATOM   2365  CE1 TYR A 297     -24.717  12.712 -15.157  1.00 54.23           C  
ANISOU 2365  CE1 TYR A 297     5779   8823   6000   -187   -145   1345       C  
ATOM   2366  CE2 TYR A 297     -25.913  10.641 -14.953  1.00 55.18           C  
ANISOU 2366  CE2 TYR A 297     5912   8880   6172   -307   -293   1420       C  
ATOM   2367  CZ  TYR A 297     -25.883  11.966 -15.290  1.00 52.54           C  
ANISOU 2367  CZ  TYR A 297     5550   8608   5804   -246   -196   1381       C  
ATOM   2368  OH  TYR A 297     -27.015  12.550 -15.780  1.00 54.94           O  
ANISOU 2368  OH  TYR A 297     5808   8967   6099   -246   -157   1380       O  
ATOM   2369  N   LYS A 298     -21.372   8.373 -11.310  1.00 63.00           N  
ANISOU 2369  N   LYS A 298     7079   9674   7183   -377   -443   1480       N  
ATOM   2370  CA  LYS A 298     -20.463   7.486 -10.680  1.00 67.69           C  
ANISOU 2370  CA  LYS A 298     7720  10202   7796   -400   -513   1497       C  
ATOM   2371  C   LYS A 298     -19.262   7.161 -11.497  1.00 69.44           C  
ANISOU 2371  C   LYS A 298     7992  10349   8043   -310   -563   1415       C  
ATOM   2372  O   LYS A 298     -18.174   7.212 -10.991  1.00 92.20           O  
ANISOU 2372  O   LYS A 298    10901  13213  10915   -284   -554   1398       O  
ATOM   2373  CB  LYS A 298     -21.165   6.216 -10.236  1.00 73.76           C  
ANISOU 2373  CB  LYS A 298     8491  10927   8605   -507   -619   1587       C  
ATOM   2374  CG  LYS A 298     -20.245   5.247  -9.538  1.00 84.31           C  
ANISOU 2374  CG  LYS A 298     9884  12171   9978   -530   -721   1602       C  
ATOM   2375  CD  LYS A 298     -20.943   4.514  -8.416  1.00 97.56           C  
ANISOU 2375  CD  LYS A 298    11554  13814  11699   -652   -825   1716       C  
ATOM   2376  CE  LYS A 298     -20.695   3.016  -8.513  1.00106.60           C  
ANISOU 2376  CE  LYS A 298    12761  14812  12929   -651   -997   1697       C  
ATOM   2377  NZ  LYS A 298     -21.956   2.232  -8.640  1.00111.07           N1+
ANISOU 2377  NZ  LYS A 298    13336  15322  13541   -597  -1067   1630       N1+
ATOM   2378  N   GLY A 299     -19.388   6.797 -12.744  1.00 63.96           N  
ANISOU 2378  N   GLY A 299     7309   9619   7373   -251   -616   1360       N  
ATOM   2379  CA  GLY A 299     -18.104   6.366 -13.375  1.00 57.50           C  
ANISOU 2379  CA  GLY A 299     6536   8744   6564   -157   -670   1284       C  
ATOM   2380  C   GLY A 299     -18.187   4.895 -13.706  1.00 57.78           C  
ANISOU 2380  C   GLY A 299     6617   8676   6657   -165   -831   1270       C  
ATOM   2381  O   GLY A 299     -18.636   4.119 -12.896  1.00 54.04           O  
ANISOU 2381  O   GLY A 299     6155   8153   6222   -262   -903   1340       O  
ATOM   2382  N   ALA A 300     -17.818   4.546 -14.920  1.00 64.50           N  
ANISOU 2382  N   ALA A 300     7489   9500   7517    -61   -894   1184       N  
ATOM   2383  CA  ALA A 300     -17.954   3.192 -15.396  1.00 70.05           C  
ANISOU 2383  CA  ALA A 300     8236  10096   8282    -53  -1068   1153       C  
ATOM   2384  C   ALA A 300     -17.226   2.237 -14.502  1.00 76.41           C  
ANISOU 2384  C   ALA A 300     9091  10810   9130    -98  -1169   1178       C  
ATOM   2385  O   ALA A 300     -16.283   2.612 -13.824  1.00 70.61           O  
ANISOU 2385  O   ALA A 300     8366  10099   8363    -84  -1108   1178       O  
ATOM   2386  CB  ALA A 300     -17.429   3.078 -16.802  1.00 74.25           C  
ANISOU 2386  CB  ALA A 300     8782  10632   8798     96  -1115   1036       C  
ATOM   2387  N   PRO A 301     -17.656   0.998 -14.479  1.00 83.47           N  
ANISOU 2387  N   PRO A 301    10016  11595  10101   -154  -1333   1202       N  
ATOM   2388  CA  PRO A 301     -17.023   0.006 -13.624  1.00 87.46           C  
ANISOU 2388  CA  PRO A 301    10570  12008  10653   -203  -1439   1234       C  
ATOM   2389  C   PRO A 301     -15.622  -0.273 -14.089  1.00 83.72           C  
ANISOU 2389  C   PRO A 301    10140  11510  10160    -70  -1478   1121       C  
ATOM   2390  O   PRO A 301     -15.389  -0.283 -15.277  1.00 73.62           O  
ANISOU 2390  O   PRO A 301     8863  10251   8857     58  -1494   1015       O  
ATOM   2391  CB  PRO A 301     -17.881  -1.232 -13.831  1.00 94.89           C  
ANISOU 2391  CB  PRO A 301    11532  12827  11693   -275  -1629   1274       C  
ATOM   2392  CG  PRO A 301     -19.080  -0.789 -14.591  1.00 93.80           C  
ANISOU 2392  CG  PRO A 301    11359  12721  11559   -254  -1620   1252       C  
ATOM   2393  CD  PRO A 301     -18.655   0.405 -15.364  1.00 89.26           C  
ANISOU 2393  CD  PRO A 301    10754  12270  10889   -143  -1453   1175       C  
ATOM   2394  N   THR A 302     -14.698  -0.489 -13.164  1.00 96.20           N  
ANISOU 2394  N   THR A 302    11747  13065  11737    -93  -1479   1143       N  
ATOM   2395  CA  THR A 302     -13.338  -0.822 -13.539  1.00104.26           C  
ANISOU 2395  CA  THR A 302    12805  14067  12739     32  -1518   1039       C  
ATOM   2396  C   THR A 302     -13.390  -2.146 -14.231  1.00109.38           C  
ANISOU 2396  C   THR A 302    13505  14599  13454    102  -1728    955       C  
ATOM   2397  O   THR A 302     -14.027  -3.079 -13.761  1.00 95.76           O  
ANISOU 2397  O   THR A 302    11811  12756  11816     11  -1879   1009       O  
ATOM   2398  CB  THR A 302     -12.428  -0.970 -12.326  1.00104.74           C  
ANISOU 2398  CB  THR A 302    12889  14108  12796    -15  -1499   1083       C  
ATOM   2399  CG2 THR A 302     -11.997   0.368 -11.846  1.00103.48           C  
ANISOU 2399  CG2 THR A 302    12682  14067  12567    -46  -1302   1134       C  
ATOM   2400  OG1 THR A 302     -13.143  -1.631 -11.283  1.00102.87           O  
ANISOU 2400  OG1 THR A 302    12677  13777  12630   -147  -1609   1179       O  
ATOM   2401  N   PRO A 303     -12.715  -2.264 -15.352  1.00112.73           N  
ANISOU 2401  N   PRO A 303    13932  15062  13838    265  -1747    827       N  
ATOM   2402  CA  PRO A 303     -12.829  -3.464 -16.166  1.00113.52           C  
ANISOU 2402  CA  PRO A 303    14075  15064  13993    350  -1948    731       C  
ATOM   2403  C   PRO A 303     -12.370  -4.701 -15.454  1.00120.09           C  
ANISOU 2403  C   PRO A 303    14972  15742  14913    312  -2139    734       C  
ATOM   2404  O   PRO A 303     -11.293  -4.728 -14.897  1.00122.63           O  
ANISOU 2404  O   PRO A 303    15313  16061  15217    316  -2118    737       O  
ATOM   2405  CB  PRO A 303     -11.887  -3.185 -17.311  1.00114.85           C  
ANISOU 2405  CB  PRO A 303    14227  15331  14076    546  -1911    597       C  
ATOM   2406  CG  PRO A 303     -11.917  -1.713 -17.442  1.00116.64           C  
ANISOU 2406  CG  PRO A 303    14386  15713  14218    535  -1682    647       C  
ATOM   2407  CD  PRO A 303     -11.974  -1.206 -16.039  1.00116.87           C  
ANISOU 2407  CD  PRO A 303    14409  15730  14263    378  -1587    774       C  
ATOM   2408  N   LYS A 304     -13.196  -5.732 -15.483  1.00136.63           N  
ANISOU 2408  N   LYS A 304    17098  17707  17108    261  -2327    746       N  
ATOM   2409  CA  LYS A 304     -12.767  -7.046 -15.097  1.00142.54           C  
ANISOU 2409  CA  LYS A 304    17912  18289  17958    242  -2552    734       C  
ATOM   2410  C   LYS A 304     -12.400  -7.656 -16.422  1.00146.80           C  
ANISOU 2410  C   LYS A 304    18489  18792  18496    443  -2707    550       C  
ATOM   2411  O   LYS A 304     -13.253  -8.050 -17.197  1.00139.96           O  
ANISOU 2411  O   LYS A 304    17620  17901  17656    494  -2794    494       O  
ATOM   2412  CB  LYS A 304     -13.907  -7.829 -14.453  1.00138.30           C  
ANISOU 2412  CB  LYS A 304    17381  17626  17541     73  -2688    860       C  
ATOM   2413  N   ARG A 305     -11.113  -7.691 -16.691  1.00143.13           N  
ANISOU 2413  N   ARG A 305    18051  18342  17986    570  -2729    449       N  
ATOM   2414  CA  ARG A 305     -10.154  -7.122 -15.752  1.00140.17           C  
ANISOU 2414  CA  ARG A 305    17667  18032  17557    532  -2587    503       C  
ATOM   2415  C   ARG A 305      -8.955  -6.419 -16.419  1.00139.46           C  
ANISOU 2415  C   ARG A 305    17549  18093  17346    706  -2462    393       C  
ATOM   2416  O   ARG A 305      -8.860  -6.341 -17.654  1.00137.35           O  
ANISOU 2416  O   ARG A 305    17263  17899  17023    865  -2476    275       O  
ATOM   2417  CB  ARG A 305      -9.749  -8.152 -14.689  1.00141.84           C  
ANISOU 2417  CB  ARG A 305    17939  18090  17863    446  -2744    551       C  
ATOM   2418  CG  ARG A 305     -10.122  -7.687 -13.285  1.00146.07           C  
ANISOU 2418  CG  ARG A 305    18452  18634  18411    246  -2624    732       C  
ATOM   2419  CD  ARG A 305     -10.043  -8.778 -12.235  1.00157.23           C  
ANISOU 2419  CD  ARG A 305    19918  19889  19932    130  -2796    812       C  
ATOM   2420  NE  ARG A 305     -11.379  -9.123 -11.724  1.00161.81           N  
ANISOU 2420  NE  ARG A 305    20483  20399  20599    -45  -2859    960       N  
ATOM   2421  CZ  ARG A 305     -11.964 -10.324 -11.791  1.00157.20           C  
ANISOU 2421  CZ  ARG A 305    19935  19649  20144    -98  -3100    985       C  
ATOM   2422  NH1 ARG A 305     -11.357 -11.374 -12.341  1.00158.42           N1+
ANISOU 2422  NH1 ARG A 305    20154  19671  20366     16  -3324    857       N1+
ATOM   2423  NH2 ARG A 305     -13.180 -10.482 -11.285  1.00150.74           N  
ANISOU 2423  NH2 ARG A 305    19084  18797  19393   -268  -3126   1142       N  
ATOM   2424  N   ILE A 306      -8.068  -5.906 -15.557  1.00127.44           N  
ANISOU 2424  N   ILE A 306    16018  16620  15783    669  -2342    444       N  
ATOM   2425  CA  ILE A 306      -7.100  -4.822 -15.842  1.00112.63           C  
ANISOU 2425  CA  ILE A 306    14088  14912  13792    765  -2154    413       C  
ATOM   2426  C   ILE A 306      -6.230  -5.004 -17.101  1.00103.08           C  
ANISOU 2426  C   ILE A 306    12866  13789  12511    987  -2199    256       C  
ATOM   2427  O   ILE A 306      -5.780  -6.095 -17.394  1.00 98.17           O  
ANISOU 2427  O   ILE A 306    12294  13082  11922   1086  -2387    151       O  
ATOM   2428  CB  ILE A 306      -6.175  -4.617 -14.603  1.00118.04           C  
ANISOU 2428  CB  ILE A 306    14785  15588  14475    692  -2088    479       C  
ATOM   2429  CG1 ILE A 306      -7.002  -4.299 -13.330  1.00118.78           C  
ANISOU 2429  CG1 ILE A 306    14878  15635  14615    485  -2020    638       C  
ATOM   2430  CG2 ILE A 306      -5.132  -3.526 -14.853  1.00111.44           C  
ANISOU 2430  CG2 ILE A 306    13892  14914  13536    782  -1911    458       C  
ATOM   2431  CD1 ILE A 306      -6.664  -5.152 -12.110  1.00114.83           C  
ANISOU 2431  CD1 ILE A 306    14435  15006  14187    386  -2131    695       C  
ATOM   2432  N   GLU A 307      -5.991  -3.910 -17.823  1.00 98.88           N  
ANISOU 2432  N   GLU A 307    12261  13430  11876   1067  -2029    246       N  
ATOM   2433  CA  GLU A 307      -5.165  -3.898 -19.025  1.00 93.89           C  
ANISOU 2433  CA  GLU A 307    11594  12926  11152   1278  -2037    118       C  
ATOM   2434  C   GLU A 307      -4.046  -2.885 -18.865  1.00 89.97           C  
ANISOU 2434  C   GLU A 307    11034  12580  10570   1313  -1859    155       C  
ATOM   2435  O   GLU A 307      -4.254  -1.796 -18.344  1.00 87.83           O  
ANISOU 2435  O   GLU A 307    10722  12362  10287   1201  -1688    269       O  
ATOM   2436  CB  GLU A 307      -6.025  -3.514 -20.236  1.00108.80           C  
ANISOU 2436  CB  GLU A 307    13440  14904  12996   1349  -2005     83       C  
ATOM   2437  CG  GLU A 307      -7.100  -4.549 -20.595  1.00116.34           C  
ANISOU 2437  CG  GLU A 307    14452  15716  14035   1341  -2200     29       C  
ATOM   2438  CD  GLU A 307      -7.080  -4.921 -22.068  1.00118.60           C  
ANISOU 2438  CD  GLU A 307    14723  16080  14259   1550  -2293   -120       C  
ATOM   2439  OE1 GLU A 307      -7.431  -4.060 -22.893  1.00115.13           O  
ANISOU 2439  OE1 GLU A 307    14218  15784  13740   1599  -2165   -112       O  
ATOM   2440  OE2 GLU A 307      -6.699  -6.069 -22.400  1.00113.96           O1-
ANISOU 2440  OE2 GLU A 307    14187  15411  13699   1670  -2499   -248       O1-
ATOM   2441  N   TYR A 308      -2.843  -3.205 -19.293  1.00 92.66           N  
ANISOU 2441  N   TYR A 308    11362  12990  10851   1472  -1905     58       N  
ATOM   2442  CA  TYR A 308      -1.742  -2.281 -19.078  1.00 95.00           C  
ANISOU 2442  CA  TYR A 308    11595  13423  11075   1506  -1756     98       C  
ATOM   2443  C   TYR A 308      -1.366  -1.718 -20.403  1.00107.27           C  
ANISOU 2443  C   TYR A 308    13058  15187  12513   1672  -1673     49       C  
ATOM   2444  O   TYR A 308      -1.643  -2.346 -21.400  1.00119.96           O  
ANISOU 2444  O   TYR A 308    14669  16825  14085   1817  -1783    -65       O  
ATOM   2445  CB  TYR A 308      -0.563  -3.009 -18.455  1.00 93.63           C  
ANISOU 2445  CB  TYR A 308    11466  13188  10921   1554  -1860     41       C  
ATOM   2446  CG  TYR A 308      -0.873  -3.536 -17.082  1.00 90.60           C  
ANISOU 2446  CG  TYR A 308    11162  12614  10648   1376  -1921    114       C  
ATOM   2447  CD1 TYR A 308      -0.604  -2.788 -15.962  1.00 90.10           C  
ANISOU 2447  CD1 TYR A 308    11083  12551  10596   1238  -1783    235       C  
ATOM   2448  CD2 TYR A 308      -1.472  -4.757 -16.913  1.00 90.21           C  
ANISOU 2448  CD2 TYR A 308    11196  12387  10690   1341  -2121     72       C  
ATOM   2449  CE1 TYR A 308      -0.902  -3.253 -14.716  1.00 87.46           C  
ANISOU 2449  CE1 TYR A 308    10814  12066  10350   1081  -1832    308       C  
ATOM   2450  CE2 TYR A 308      -1.774  -5.226 -15.669  1.00 91.61           C  
ANISOU 2450  CE2 TYR A 308    11435  12406  10963   1172  -2174    159       C  
ATOM   2451  CZ  TYR A 308      -1.487  -4.467 -14.576  1.00 94.07           C  
ANISOU 2451  CZ  TYR A 308    11729  12741  11272   1044  -2023    277       C  
ATOM   2452  OH  TYR A 308      -1.789  -4.933 -13.329  1.00 98.27           O  
ANISOU 2452  OH  TYR A 308    12315  13136  11886    881  -2070    369       O  
ATOM   2453  N   PRO A 309      -0.765  -0.539 -20.468  1.00112.67           N  
ANISOU 2453  N   PRO A 309    13655  16017  13134   1658  -1488    138       N  
ATOM   2454  CA  PRO A 309      -0.274   0.270 -19.360  1.00104.26           C  
ANISOU 2454  CA  PRO A 309    12575  14938  12099   1525  -1365    256       C  
ATOM   2455  C   PRO A 309      -1.412   1.018 -18.689  1.00 91.09           C  
ANISOU 2455  C   PRO A 309    10919  13197  10492   1340  -1273    370       C  
ATOM   2456  O   PRO A 309      -2.362   1.408 -19.360  1.00 83.18           O  
ANISOU 2456  O   PRO A 309     9892  12235   9475   1335  -1235    382       O  
ATOM   2457  CB  PRO A 309       0.645   1.266 -20.069  1.00109.45           C  
ANISOU 2457  CB  PRO A 309    13118  15807  12658   1623  -1228    289       C  
ATOM   2458  CG  PRO A 309      -0.069   1.537 -21.367  1.00108.53           C  
ANISOU 2458  CG  PRO A 309    12950  15806  12478   1712  -1204    261       C  
ATOM   2459  CD  PRO A 309      -0.808   0.258 -21.717  1.00109.77           C  
ANISOU 2459  CD  PRO A 309    13190  15848  12666   1768  -1385    139       C  
ATOM   2460  N   LEU A 310      -1.320   1.223 -17.375  1.00 86.02           N  
ANISOU 2460  N   LEU A 310    10313  12458   9912   1196  -1240    449       N  
ATOM   2461  CA  LEU A 310      -2.435   1.855 -16.633  1.00 77.22           C  
ANISOU 2461  CA  LEU A 310     9211  11277   8851   1027  -1165    549       C  
ATOM   2462  C   LEU A 310      -2.578   3.312 -17.010  1.00 68.26           C  
ANISOU 2462  C   LEU A 310     7991  10271   7674   1010   -996    626       C  
ATOM   2463  O   LEU A 310      -1.606   3.948 -17.408  1.00 73.69           O  
ANISOU 2463  O   LEU A 310     8610  11077   8309   1086   -922    638       O  
ATOM   2464  CB  LEU A 310      -2.235   1.752 -15.126  1.00 75.00           C  
ANISOU 2464  CB  LEU A 310     8982  10884   8631    893  -1169    612       C  
ATOM   2465  CG  LEU A 310      -2.220   0.356 -14.523  1.00 70.11           C  
ANISOU 2465  CG  LEU A 310     8451  10114   8072    870  -1339    567       C  
ATOM   2466  CD1 LEU A 310      -2.033   0.464 -13.020  1.00 67.11           C  
ANISOU 2466  CD1 LEU A 310     8107   9653   7740    733  -1314    649       C  
ATOM   2467  CD2 LEU A 310      -3.515  -0.343 -14.846  1.00 68.63           C  
ANISOU 2467  CD2 LEU A 310     8303   9844   7929    832  -1440    550       C  
ATOM   2468  N   LYS A 311      -3.796   3.826 -16.912  1.00 59.15           N  
ANISOU 2468  N   LYS A 311     6835   9093   6545    913   -945    681       N  
ATOM   2469  CA  LYS A 311      -4.006   5.235 -17.083  1.00 61.97           C  
ANISOU 2469  CA  LYS A 311     7120   9545   6879    878   -796    760       C  
ATOM   2470  C   LYS A 311      -3.627   5.997 -15.782  1.00 60.19           C  
ANISOU 2470  C   LYS A 311     6894   9281   6690    764   -718    843       C  
ATOM   2471  O   LYS A 311      -3.602   5.447 -14.682  1.00 57.40           O  
ANISOU 2471  O   LYS A 311     6603   8822   6381    686   -770    851       O  
ATOM   2472  CB  LYS A 311      -5.469   5.513 -17.478  1.00 70.06           C  
ANISOU 2472  CB  LYS A 311     8141  10561   7915    825   -774    779       C  
ATOM   2473  CG  LYS A 311      -5.881   4.908 -18.831  1.00 76.27           C  
ANISOU 2473  CG  LYS A 311     8920  11394   8662    944   -845    697       C  
ATOM   2474  CD  LYS A 311      -7.386   4.958 -19.064  1.00 78.58           C  
ANISOU 2474  CD  LYS A 311     9226  11648   8982    878   -850    711       C  
ATOM   2475  CE  LYS A 311      -7.898   6.382 -19.290  1.00 83.61           C  
ANISOU 2475  CE  LYS A 311     9795  12372   9599    834   -704    789       C  
ATOM   2476  NZ  LYS A 311      -9.248   6.432 -19.939  1.00 82.03           N1+
ANISOU 2476  NZ  LYS A 311     9590  12172   9403    818   -709    783       N1+
ATOM   2477  N   ALA A 312      -3.380   7.280 -15.940  1.00 55.82           N  
ANISOU 2477  N   ALA A 312     6270   8817   6121    757   -601    908       N  
ATOM   2478  CA  ALA A 312      -2.992   8.134 -14.875  1.00 52.40           C  
ANISOU 2478  CA  ALA A 312     5826   8360   5721    671   -532    978       C  
ATOM   2479  C   ALA A 312      -4.005   8.054 -13.754  1.00 52.11           C  
ANISOU 2479  C   ALA A 312     5848   8221   5730    543   -540   1006       C  
ATOM   2480  O   ALA A 312      -3.625   7.899 -12.603  1.00 49.12           O  
ANISOU 2480  O   ALA A 312     5508   7775   5379    482   -556   1024       O  
ATOM   2481  CB  ALA A 312      -2.799   9.565 -15.400  1.00 49.80           C  
ANISOU 2481  CB  ALA A 312     5407   8136   5378    684   -421   1045       C  
ATOM   2482  N   HIS A 313      -5.298   8.036 -14.064  1.00 54.46           N  
ANISOU 2482  N   HIS A 313     6152   8508   6030    506   -539   1008       N  
ATOM   2483  CA  HIS A 313      -6.291   8.049 -13.000  1.00 53.03           C  
ANISOU 2483  CA  HIS A 313     6009   8256   5882    386   -536   1048       C  
ATOM   2484  C   HIS A 313      -6.264   6.785 -12.212  1.00 53.87           C  
ANISOU 2484  C   HIS A 313     6188   8264   6016    344   -642   1030       C  
ATOM   2485  O   HIS A 313      -6.709   6.731 -11.047  1.00 52.81           O  
ANISOU 2485  O   HIS A 313     6083   8078   5903    243   -642   1076       O  
ATOM   2486  CB  HIS A 313      -7.731   8.355 -13.488  1.00 57.65           C  
ANISOU 2486  CB  HIS A 313     6577   8862   6465    352   -509   1062       C  
ATOM   2487  CG  HIS A 313      -8.340   7.308 -14.354  1.00 61.78           C  
ANISOU 2487  CG  HIS A 313     7125   9362   6985    393   -598   1011       C  
ATOM   2488  CD2 HIS A 313      -8.610   7.305 -15.680  1.00 69.97           C  
ANISOU 2488  CD2 HIS A 313     8131  10458   7994    479   -603    970       C  
ATOM   2489  ND1 HIS A 313      -8.787   6.103 -13.872  1.00 69.29           N  
ANISOU 2489  ND1 HIS A 313     8137  10218   7970    344   -707    998       N  
ATOM   2490  CE1 HIS A 313      -9.288   5.390 -14.865  1.00 73.37           C  
ANISOU 2490  CE1 HIS A 313     8664  10724   8487    399   -784    946       C  
ATOM   2491  NE2 HIS A 313      -9.202   6.102 -15.970  1.00 69.55           N  
ANISOU 2491  NE2 HIS A 313     8127  10338   7961    486   -719    923       N  
ATOM   2492  N   GLN A 314      -5.805   5.735 -12.852  1.00 53.71           N  
ANISOU 2492  N   GLN A 314     6195   8220   5992    422   -739    965       N  
ATOM   2493  CA  GLN A 314      -5.722   4.475 -12.168  1.00 56.62           C  
ANISOU 2493  CA  GLN A 314     6634   8481   6396    386   -860    948       C  
ATOM   2494  C   GLN A 314      -4.524   4.458 -11.228  1.00 54.75           C  
ANISOU 2494  C   GLN A 314     6416   8218   6165    377   -859    958       C  
ATOM   2495  O   GLN A 314      -4.585   3.801 -10.197  1.00 50.86           O  
ANISOU 2495  O   GLN A 314     5976   7642   5706    301   -921    983       O  
ATOM   2496  CB  GLN A 314      -5.616   3.336 -13.178  1.00 60.53           C  
ANISOU 2496  CB  GLN A 314     7156   8948   6892    484   -986    861       C  
ATOM   2497  CG  GLN A 314      -6.761   3.364 -14.200  1.00 66.00           C  
ANISOU 2497  CG  GLN A 314     7829   9670   7578    505   -991    843       C  
ATOM   2498  CD  GLN A 314      -6.640   2.230 -15.172  1.00 62.43           C  
ANISOU 2498  CD  GLN A 314     7406   9188   7127    615  -1131    745       C  
ATOM   2499  NE2 GLN A 314      -7.279   1.143 -14.864  1.00 63.62           N  
ANISOU 2499  NE2 GLN A 314     7614   9219   7336    561  -1265    738       N  
ATOM   2500  OE1 GLN A 314      -5.901   2.314 -16.143  1.00 69.00           O  
ANISOU 2500  OE1 GLN A 314     8205  10103   7906    750  -1126    679       O  
ATOM   2501  N   LYS A 315      -3.439   5.155 -11.594  1.00 48.91           N  
ANISOU 2501  N   LYS A 315     5631   7555   5397    454   -795    945       N  
ATOM   2502  CA  LYS A 315      -2.322   5.246 -10.675  1.00 51.41           C  
ANISOU 2502  CA  LYS A 315     5961   7849   5723    442   -788    959       C  
ATOM   2503  C   LYS A 315      -2.719   6.103  -9.465  1.00 49.52           C  
ANISOU 2503  C   LYS A 315     5719   7594   5500    330   -712   1034       C  
ATOM   2504  O   LYS A 315      -2.285   5.845  -8.361  1.00 50.15           O  
ANISOU 2504  O   LYS A 315     5837   7619   5599    279   -737   1052       O  
ATOM   2505  CB  LYS A 315      -1.074   5.778 -11.352  1.00 49.80           C  
ANISOU 2505  CB  LYS A 315     5699   7735   5488    547   -743    939       C  
ATOM   2506  CG  LYS A 315      -0.607   4.801 -12.415  1.00 54.28           C  
ANISOU 2506  CG  LYS A 315     6270   8326   6025    672   -832    853       C  
ATOM   2507  CD  LYS A 315       0.782   5.115 -12.906  1.00 58.26           C  
ANISOU 2507  CD  LYS A 315     6717   8925   6492    778   -802    836       C  
ATOM   2508  CE  LYS A 315       1.070   4.402 -14.222  1.00 66.54           C  
ANISOU 2508  CE  LYS A 315     7745  10047   7487    927   -867    750       C  
ATOM   2509  NZ  LYS A 315       2.517   4.508 -14.543  1.00 76.31           N1+
ANISOU 2509  NZ  LYS A 315     8928  11381   8684   1032   -854    733       N1+
ATOM   2510  N   VAL A 316      -3.583   7.075  -9.687  1.00 48.26           N  
ANISOU 2510  N   VAL A 316     5517   7486   5332    298   -627   1070       N  
ATOM   2511  CA  VAL A 316      -4.052   7.931  -8.642  1.00 52.61           C  
ANISOU 2511  CA  VAL A 316     6061   8036   5892    211   -561   1126       C  
ATOM   2512  C   VAL A 316      -4.870   7.133  -7.666  1.00 52.48           C  
ANISOU 2512  C   VAL A 316     6097   7955   5887    119   -616   1152       C  
ATOM   2513  O   VAL A 316      -4.591   7.149  -6.462  1.00 52.54           O  
ANISOU 2513  O   VAL A 316     6129   7933   5899     65   -617   1182       O  
ATOM   2514  CB  VAL A 316      -4.868   9.090  -9.177  1.00 48.77           C  
ANISOU 2514  CB  VAL A 316     5517   7616   5394    206   -472   1151       C  
ATOM   2515  CG1 VAL A 316      -5.466   9.884  -8.040  1.00 49.58           C  
ANISOU 2515  CG1 VAL A 316     5617   7719   5502    126   -420   1195       C  
ATOM   2516  CG2 VAL A 316      -3.990   9.992  -9.986  1.00 43.69           C  
ANISOU 2516  CG2 VAL A 316     4812   7040   4746    282   -417   1150       C  
ATOM   2517  N   ALA A 317      -5.866   6.452  -8.193  1.00 54.47           N  
ANISOU 2517  N   ALA A 317     6362   8190   6142    103   -664   1148       N  
ATOM   2518  CA  ALA A 317      -6.711   5.523  -7.422  1.00 54.60           C  
ANISOU 2518  CA  ALA A 317     6420   8146   6177     11   -736   1187       C  
ATOM   2519  C   ALA A 317      -5.872   4.558  -6.598  1.00 50.70           C  
ANISOU 2519  C   ALA A 317     5982   7575   5705     -6   -825   1188       C  
ATOM   2520  O   ALA A 317      -6.203   4.260  -5.473  1.00 52.42           O  
ANISOU 2520  O   ALA A 317     6221   7766   5928    -93   -845   1245       O  
ATOM   2521  CB  ALA A 317      -7.611   4.707  -8.370  1.00 51.74           C  
ANISOU 2521  CB  ALA A 317     6068   7758   5833     19   -811   1168       C  
ATOM   2522  N   ILE A 318      -4.776   4.071  -7.167  1.00 52.88           N  
ANISOU 2522  N   ILE A 318     6276   7823   5989     80   -880   1124       N  
ATOM   2523  CA  ILE A 318      -3.866   3.199  -6.407  1.00 54.03           C  
ANISOU 2523  CA  ILE A 318     6476   7894   6158     72   -968   1116       C  
ATOM   2524  C   ILE A 318      -3.244   3.955  -5.212  1.00 51.40           C  
ANISOU 2524  C   ILE A 318     6136   7581   5810     33   -895   1156       C  
ATOM   2525  O   ILE A 318      -3.243   3.421  -4.075  1.00 49.39           O  
ANISOU 2525  O   ILE A 318     5921   7277   5567    -39   -941   1200       O  
ATOM   2526  CB  ILE A 318      -2.773   2.593  -7.306  1.00 55.93           C  
ANISOU 2526  CB  ILE A 318     6729   8117   6401    191  -1039   1030       C  
ATOM   2527  CG1 ILE A 318      -3.367   1.484  -8.171  1.00 59.61           C  
ANISOU 2527  CG1 ILE A 318     7224   8530   6893    223  -1161    984       C  
ATOM   2528  CG2 ILE A 318      -1.624   2.030  -6.482  1.00 53.71           C  
ANISOU 2528  CG2 ILE A 318     6492   7778   6137    195  -1100   1018       C  
ATOM   2529  CD1 ILE A 318      -2.441   1.047  -9.302  1.00 61.15           C  
ANISOU 2529  CD1 ILE A 318     7417   8743   7072    369  -1220    882       C  
ATOM   2530  N   MET A 319      -2.757   5.194  -5.448  1.00 47.32           N  
ANISOU 2530  N   MET A 319     5571   7137   5272     78   -789   1146       N  
ATOM   2531  CA  MET A 319      -2.086   5.960  -4.381  1.00 45.46           C  
ANISOU 2531  CA  MET A 319     5329   6913   5030     55   -734   1172       C  
ATOM   2532  C   MET A 319      -3.084   6.157  -3.261  1.00 48.68           C  
ANISOU 2532  C   MET A 319     5744   7328   5424    -42   -709   1233       C  
ATOM   2533  O   MET A 319      -2.762   5.962  -2.095  1.00 47.39           O  
ANISOU 2533  O   MET A 319     5609   7140   5257    -86   -728   1261       O  
ATOM   2534  CB  MET A 319      -1.547   7.304  -4.863  1.00 47.89           C  
ANISOU 2534  CB  MET A 319     5575   7288   5331    110   -639   1162       C  
ATOM   2535  CG  MET A 319      -0.299   7.143  -5.676  1.00 47.47           C  
ANISOU 2535  CG  MET A 319     5506   7246   5284    204   -659   1118       C  
ATOM   2536  SD  MET A 319       0.548   8.628  -6.164  1.00 53.00           S  
ANISOU 2536  SD  MET A 319     6125   8023   5988    260   -566   1133       S  
ATOM   2537  CE  MET A 319      -0.437   9.226  -7.495  1.00 48.53           C  
ANISOU 2537  CE  MET A 319     5501   7532   5404    288   -509   1139       C  
ATOM   2538  N   ARG A 320      -4.324   6.461  -3.628  1.00 48.58           N  
ANISOU 2538  N   ARG A 320     5703   7357   5398    -73   -671   1257       N  
ATOM   2539  CA  ARG A 320      -5.364   6.671  -2.620  1.00 46.93           C  
ANISOU 2539  CA  ARG A 320     5486   7180   5164   -158   -643   1318       C  
ATOM   2540  C   ARG A 320      -5.579   5.423  -1.830  1.00 51.04           C  
ANISOU 2540  C   ARG A 320     6052   7647   5692   -230   -734   1365       C  
ATOM   2541  O   ARG A 320      -5.670   5.488  -0.578  1.00 54.12           O  
ANISOU 2541  O   ARG A 320     6448   8058   6056   -285   -724   1415       O  
ATOM   2542  CB  ARG A 320      -6.682   7.139  -3.225  1.00 43.71           C  
ANISOU 2542  CB  ARG A 320     5037   6829   4741   -175   -593   1334       C  
ATOM   2543  CG  ARG A 320      -6.660   8.528  -3.894  1.00 43.95           C  
ANISOU 2543  CG  ARG A 320     5015   6920   4764   -118   -499   1302       C  
ATOM   2544  CD  ARG A 320      -8.050   8.899  -4.504  1.00 44.88           C  
ANISOU 2544  CD  ARG A 320     5094   7090   4867   -137   -458   1318       C  
ATOM   2545  NE  ARG A 320      -8.956   9.048  -3.418  1.00 45.89           N  
ANISOU 2545  NE  ARG A 320     5212   7262   4962   -207   -436   1368       N  
ATOM   2546  CZ  ARG A 320      -8.979  10.081  -2.565  1.00 50.24           C  
ANISOU 2546  CZ  ARG A 320     5738   7866   5484   -206   -374   1371       C  
ATOM   2547  NH1 ARG A 320      -8.258  11.170  -2.788  1.00 49.14           N1+
ANISOU 2547  NH1 ARG A 320     5579   7732   5359   -146   -330   1330       N1+
ATOM   2548  NH2 ARG A 320      -9.776  10.038  -1.499  1.00 48.49           N  
ANISOU 2548  NH2 ARG A 320     5506   7700   5218   -262   -363   1418       N  
ATOM   2549  N   ASN A 321      -5.692   4.277  -2.509  1.00 51.34           N  
ANISOU 2549  N   ASN A 321     6121   7619   5767   -229   -832   1355       N  
ATOM   2550  CA  ASN A 321      -5.972   3.062  -1.760  1.00 50.67           C  
ANISOU 2550  CA  ASN A 321     6076   7471   5703   -309   -936   1415       C  
ATOM   2551  C   ASN A 321      -4.765   2.697  -0.860  1.00 49.89           C  
ANISOU 2551  C   ASN A 321     6020   7325   5611   -305   -979   1410       C  
ATOM   2552  O   ASN A 321      -4.968   2.293   0.240  1.00 50.61           O  
ANISOU 2552  O   ASN A 321     6125   7411   5692   -381  -1008   1481       O  
ATOM   2553  CB  ASN A 321      -6.421   1.914  -2.650  1.00 56.39           C  
ANISOU 2553  CB  ASN A 321     6825   8120   6478   -311  -1054   1404       C  
ATOM   2554  CG  ASN A 321      -7.769   2.184  -3.372  1.00 66.55           C  
ANISOU 2554  CG  ASN A 321     8070   9454   7761   -334  -1021   1425       C  
ATOM   2555  ND2 ASN A 321      -7.904   1.588  -4.549  1.00 71.62           N  
ANISOU 2555  ND2 ASN A 321     8726  10045   8441   -284  -1096   1371       N  
ATOM   2556  OD1 ASN A 321      -8.688   2.889  -2.878  1.00 71.74           O  
ANISOU 2556  OD1 ASN A 321     8682  10193   8379   -390   -935   1484       O  
ATOM   2557  N   ILE A 322      -3.524   2.876  -1.298  1.00 46.32           N  
ANISOU 2557  N   ILE A 322     5581   6847   5169   -217   -978   1335       N  
ATOM   2558  CA  ILE A 322      -2.396   2.652  -0.405  1.00 45.33           C  
ANISOU 2558  CA  ILE A 322     5492   6684   5048   -212  -1008   1330       C  
ATOM   2559  C   ILE A 322      -2.534   3.540   0.846  1.00 45.09           C  
ANISOU 2559  C   ILE A 322     5439   6719   4972   -259   -923   1380       C  
ATOM   2560  O   ILE A 322      -2.455   3.038   1.972  1.00 42.65           O  
ANISOU 2560  O   ILE A 322     5157   6392   4653   -319   -964   1433       O  
ATOM   2561  CB  ILE A 322      -1.024   2.923  -1.061  1.00 46.80           C  
ANISOU 2561  CB  ILE A 322     5679   6857   5245   -106  -1001   1246       C  
ATOM   2562  CG1 ILE A 322      -0.722   1.984  -2.232  1.00 49.84           C  
ANISOU 2562  CG1 ILE A 322     6085   7189   5661    -36  -1097   1182       C  
ATOM   2563  CG2 ILE A 322       0.119   2.849  -0.049  1.00 49.19           C  
ANISOU 2563  CG2 ILE A 322     6012   7128   5550   -105  -1020   1245       C  
ATOM   2564  CD1 ILE A 322      -0.734   0.515  -1.899  1.00 55.01           C  
ANISOU 2564  CD1 ILE A 322     6803   7740   6359    -74  -1247   1193       C  
ATOM   2565  N   GLU A 323      -2.765   4.846   0.661  1.00 43.16           N  
ANISOU 2565  N   GLU A 323     5146   6553   4699   -229   -813   1363       N  
ATOM   2566  CA  GLU A 323      -2.878   5.749   1.806  1.00 41.95           C  
ANISOU 2566  CA  GLU A 323     4972   6463   4503   -254   -743   1391       C  
ATOM   2567  C   GLU A 323      -3.989   5.294   2.763  1.00 46.22           C  
ANISOU 2567  C   GLU A 323     5509   7047   5004   -345   -757   1476       C  
ATOM   2568  O   GLU A 323      -3.807   5.306   3.959  1.00 47.46           O  
ANISOU 2568  O   GLU A 323     5675   7229   5126   -375   -757   1511       O  
ATOM   2569  CB  GLU A 323      -3.120   7.169   1.342  1.00 41.69           C  
ANISOU 2569  CB  GLU A 323     4886   6497   4456   -207   -644   1358       C  
ATOM   2570  CG  GLU A 323      -1.981   7.793   0.614  1.00 41.39           C  
ANISOU 2570  CG  GLU A 323     4836   6438   4453   -127   -623   1298       C  
ATOM   2571  CD  GLU A 323      -2.282   9.188   0.024  1.00 43.37           C  
ANISOU 2571  CD  GLU A 323     5028   6745   4703    -88   -538   1279       C  
ATOM   2572  OE1 GLU A 323      -2.623  10.167   0.762  1.00 41.20           O  
ANISOU 2572  OE1 GLU A 323     4730   6516   4407    -96   -489   1285       O  
ATOM   2573  OE2 GLU A 323      -2.046   9.327  -1.202  1.00 42.14           O1-
ANISOU 2573  OE2 GLU A 323     4848   6589   4572    -39   -527   1253       O1-
ATOM   2574  N   LYS A 324      -5.135   4.875   2.222  1.00 50.66           N  
ANISOU 2574  N   LYS A 324     6053   7624   5569   -388   -770   1515       N  
ATOM   2575  CA  LYS A 324      -6.273   4.425   3.011  1.00 53.52           C  
ANISOU 2575  CA  LYS A 324     6397   8042   5896   -480   -783   1613       C  
ATOM   2576  C   LYS A 324      -5.997   3.216   3.874  1.00 53.07           C  
ANISOU 2576  C   LYS A 324     6380   7932   5851   -548   -883   1684       C  
ATOM   2577  O   LYS A 324      -6.280   3.251   5.043  1.00 52.65           O  
ANISOU 2577  O   LYS A 324     6311   7947   5745   -597   -867   1753       O  
ATOM   2578  CB  LYS A 324      -7.481   4.091   2.123  1.00 56.61           C  
ANISOU 2578  CB  LYS A 324     6761   8442   6305   -515   -797   1643       C  
ATOM   2579  CG  LYS A 324      -8.263   5.312   1.694  1.00 62.93           C  
ANISOU 2579  CG  LYS A 324     7505   9336   7068   -483   -688   1617       C  
ATOM   2580  CD  LYS A 324      -9.299   5.002   0.601  1.00 66.85           C  
ANISOU 2580  CD  LYS A 324     7979   9827   7592   -501   -704   1627       C  
ATOM   2581  CE  LYS A 324     -10.123   6.241   0.222  1.00 69.24           C  
ANISOU 2581  CE  LYS A 324     8224  10226   7856   -471   -597   1604       C  
ATOM   2582  NZ  LYS A 324     -11.313   5.908  -0.623  1.00 72.24           N1+
ANISOU 2582  NZ  LYS A 324     8577  10616   8254   -505   -612   1632       N1+
ATOM   2583  N   MET A 325      -5.475   2.160   3.283  1.00 56.37           N  
ANISOU 2583  N   MET A 325     6846   8234   6337   -545   -991   1665       N  
ATOM   2584  CA  MET A 325      -5.151   0.927   4.004  1.00 61.05           C  
ANISOU 2584  CA  MET A 325     7483   8752   6959   -609  -1108   1730       C  
ATOM   2585  C   MET A 325      -4.085   1.118   5.058  1.00 59.15           C  
ANISOU 2585  C   MET A 325     7268   8513   6691   -591  -1098   1721       C  
ATOM   2586  O   MET A 325      -4.108   0.530   6.131  1.00 66.86           O  
ANISOU 2586  O   MET A 325     8256   9495   7650   -660  -1146   1805       O  
ATOM   2587  CB  MET A 325      -4.643  -0.123   3.014  1.00 70.57           C  
ANISOU 2587  CB  MET A 325     8740   9823   8249   -579  -1234   1678       C  
ATOM   2588  CG  MET A 325      -5.709  -0.628   2.034  1.00 81.89           C  
ANISOU 2588  CG  MET A 325    10158  11231   9724   -606  -1287   1695       C  
ATOM   2589  SD  MET A 325      -5.008  -1.401   0.547  1.00101.90           S  
ANISOU 2589  SD  MET A 325    12743  13638  12337   -508  -1403   1576       S  
ATOM   2590  CE  MET A 325      -6.525  -1.608  -0.424  1.00109.78           C  
ANISOU 2590  CE  MET A 325    13704  14644  13361   -545  -1427   1606       C  
ATOM   2591  N   LEU A 326      -3.098   1.908   4.724  1.00 55.48           N  
ANISOU 2591  N   LEU A 326     6812   8041   6226   -499  -1043   1621       N  
ATOM   2592  CA  LEU A 326      -2.054   2.185   5.645  1.00 57.38           C  
ANISOU 2592  CA  LEU A 326     7075   8278   6446   -474  -1032   1602       C  
ATOM   2593  C   LEU A 326      -2.649   2.922   6.831  1.00 57.38           C  
ANISOU 2593  C   LEU A 326     7036   8398   6365   -509   -954   1659       C  
ATOM   2594  O   LEU A 326      -2.324   2.645   7.958  1.00 56.74           O  
ANISOU 2594  O   LEU A 326     6972   8331   6254   -540   -978   1704       O  
ATOM   2595  CB  LEU A 326      -0.999   3.024   4.966  1.00 56.69           C  
ANISOU 2595  CB  LEU A 326     6988   8173   6378   -372   -981   1495       C  
ATOM   2596  CG  LEU A 326       0.420   2.803   5.398  1.00 61.13           C  
ANISOU 2596  CG  LEU A 326     7591   8671   6961   -332  -1025   1454       C  
ATOM   2597  CD1 LEU A 326       0.661   1.321   5.715  1.00 63.01           C  
ANISOU 2597  CD1 LEU A 326     7886   8817   7236   -381  -1156   1493       C  
ATOM   2598  CD2 LEU A 326       1.279   3.299   4.233  1.00 61.48           C  
ANISOU 2598  CD2 LEU A 326     7625   8690   7042   -236  -1000   1361       C  
ATOM   2599  N   GLY A 327      -3.565   3.833   6.551  1.00 57.80           N  
ANISOU 2599  N   GLY A 327     7036   8544   6381   -499   -864   1655       N  
ATOM   2600  CA  GLY A 327      -4.354   4.457   7.592  1.00 60.49           C  
ANISOU 2600  CA  GLY A 327     7330   9016   6635   -526   -798   1709       C  
ATOM   2601  C   GLY A 327      -4.995   3.439   8.510  1.00 63.95           C  
ANISOU 2601  C   GLY A 327     7764   9493   7041   -624   -856   1836       C  
ATOM   2602  O   GLY A 327      -4.872   3.536   9.728  1.00 62.26           O  
ANISOU 2602  O   GLY A 327     7542   9352   6762   -638   -845   1878       O  
ATOM   2603  N   GLU A 328      -5.694   2.478   7.918  1.00 68.83           N  
ANISOU 2603  N   GLU A 328     8381  10066   7704   -693   -923   1901       N  
ATOM   2604  CA  GLU A 328      -6.395   1.446   8.681  1.00 74.14           C  
ANISOU 2604  CA  GLU A 328     9039  10769   8362   -802   -992   2045       C  
ATOM   2605  C   GLU A 328      -5.439   0.536   9.405  1.00 66.93           C  
ANISOU 2605  C   GLU A 328     8181   9773   7475   -831  -1089   2079       C  
ATOM   2606  O   GLU A 328      -5.590   0.311  10.583  1.00 63.35           O  
ANISOU 2606  O   GLU A 328     7709   9398   6962   -883  -1095   2173       O  
ATOM   2607  CB  GLU A 328      -7.290   0.611   7.776  1.00 76.35           C  
ANISOU 2607  CB  GLU A 328     9308  10993   8707   -867  -1063   2101       C  
ATOM   2608  CG  GLU A 328      -8.677   1.198   7.690  1.00 86.08           C  
ANISOU 2608  CG  GLU A 328    10462  12361   9882   -895   -981   2153       C  
ATOM   2609  CD  GLU A 328      -9.532   0.461   6.692  1.00 97.19           C  
ANISOU 2609  CD  GLU A 328    11860  13705  11362   -951  -1051   2195       C  
ATOM   2610  OE1 GLU A 328      -9.510  -0.792   6.762  1.00104.42           O  
ANISOU 2610  OE1 GLU A 328    12804  14525  12345  -1028  -1183   2276       O  
ATOM   2611  OE2 GLU A 328     -10.207   1.126   5.856  1.00 86.41           O1-
ANISOU 2611  OE2 GLU A 328    10460  12378   9991   -917   -984   2147       O1-
ATOM   2612  N   ALA A 329      -4.422   0.058   8.693  1.00 64.76           N  
ANISOU 2612  N   ALA A 329     7971   9349   7285   -788  -1163   1997       N  
ATOM   2613  CA  ALA A 329      -3.539  -0.918   9.263  1.00 60.48           C  
ANISOU 2613  CA  ALA A 329     7486   8711   6782   -816  -1272   2025       C  
ATOM   2614  C   ALA A 329      -2.778  -0.337  10.426  1.00 60.86           C  
ANISOU 2614  C   ALA A 329     7541   8822   6762   -783  -1219   2011       C  
ATOM   2615  O   ALA A 329      -2.603  -1.042  11.416  1.00 65.75           O  
ANISOU 2615  O   ALA A 329     8175   9441   7366   -844  -1283   2100       O  
ATOM   2616  CB  ALA A 329      -2.601  -1.513   8.240  1.00 57.14           C  
ANISOU 2616  CB  ALA A 329     7127   8129   6455   -760  -1362   1927       C  
ATOM   2617  N   LEU A 330      -2.324   0.917  10.338  1.00 57.81           N  
ANISOU 2617  N   LEU A 330     7142   8485   6338   -691  -1113   1907       N  
ATOM   2618  CA  LEU A 330      -1.525   1.511  11.431  1.00 58.42           C  
ANISOU 2618  CA  LEU A 330     7228   8609   6358   -649  -1075   1879       C  
ATOM   2619  C   LEU A 330      -2.359   1.918  12.650  1.00 63.36           C  
ANISOU 2619  C   LEU A 330     7798   9401   6871   -683  -1016   1965       C  
ATOM   2620  O   LEU A 330      -1.814   2.161  13.733  1.00 64.27           O  
ANISOU 2620  O   LEU A 330     7922   9565   6930   -662  -1006   1966       O  
ATOM   2621  CB  LEU A 330      -0.713   2.686  10.938  1.00 61.09           C  
ANISOU 2621  CB  LEU A 330     7570   8931   6709   -541  -1003   1745       C  
ATOM   2622  CG  LEU A 330       0.344   2.366   9.882  1.00 62.02           C  
ANISOU 2622  CG  LEU A 330     7733   8911   6919   -490  -1054   1658       C  
ATOM   2623  CD1 LEU A 330       0.961   3.627   9.287  1.00 60.46           C  
ANISOU 2623  CD1 LEU A 330     7517   8719   6734   -394   -974   1550       C  
ATOM   2624  CD2 LEU A 330       1.423   1.471  10.469  1.00 59.68           C  
ANISOU 2624  CD2 LEU A 330     7497   8524   6654   -499  -1149   1665       C  
ATOM   2625  N   GLY A 331      -3.684   1.949  12.470  1.00 67.63           N  
ANISOU 2625  N   GLY A 331     8281  10038   7377   -733   -981   2039       N  
ATOM   2626  CA  GLY A 331      -4.600   2.314  13.532  1.00 70.35           C  
ANISOU 2626  CA  GLY A 331     8558  10567   7604   -759   -922   2125       C  
ATOM   2627  C   GLY A 331      -4.773   3.821  13.646  1.00 73.99           C  
ANISOU 2627  C   GLY A 331     8979  11137   7994   -661   -808   2026       C  
ATOM   2628  O   GLY A 331      -5.548   4.307  14.468  1.00 80.55           O  
ANISOU 2628  O   GLY A 331     9749  12139   8716   -655   -750   2070       O  
ATOM   2629  N   ASN A 332      -4.071   4.577  12.817  1.00 67.60           N  
ANISOU 2629  N   ASN A 332     8200  10237   7246   -580   -781   1893       N  
ATOM   2630  CA  ASN A 332      -4.013   5.992  13.001  1.00 70.82           C  
ANISOU 2630  CA  ASN A 332     8582  10720   7607   -484   -699   1795       C  
ATOM   2631  C   ASN A 332      -3.484   6.692  11.730  1.00 71.00           C  
ANISOU 2631  C   ASN A 332     8623  10634   7720   -421   -677   1681       C  
ATOM   2632  O   ASN A 332      -2.348   6.448  11.322  1.00 64.33           O  
ANISOU 2632  O   ASN A 332     7829   9661   6951   -399   -721   1631       O  
ATOM   2633  CB  ASN A 332      -3.093   6.296  14.173  1.00 69.02           C  
ANISOU 2633  CB  ASN A 332     8378  10512   7333   -435   -711   1762       C  
ATOM   2634  CG  ASN A 332      -2.924   7.787  14.429  1.00 79.83           C  
ANISOU 2634  CG  ASN A 332     9724  11939   8666   -328   -650   1649       C  
ATOM   2635  ND2 ASN A 332      -2.010   8.099  15.327  1.00 89.17           N  
ANISOU 2635  ND2 ASN A 332    10935  13118   9828   -275   -671   1602       N  
ATOM   2636  OD1 ASN A 332      -3.586   8.657  13.826  1.00 86.14           O  
ANISOU 2636  OD1 ASN A 332    10484  12780   9463   -290   -594   1601       O  
ATOM   2637  N   PRO A 333      -4.266   7.616  11.162  1.00 65.32           N  
ANISOU 2637  N   PRO A 333     7857   9975   6986   -386   -610   1642       N  
ATOM   2638  CA  PRO A 333      -3.860   8.299   9.910  1.00 65.41           C  
ANISOU 2638  CA  PRO A 333     7875   9898   7079   -332   -587   1552       C  
ATOM   2639  C   PRO A 333      -2.631   9.161  10.050  1.00 61.33           C  
ANISOU 2639  C   PRO A 333     7381   9322   6599   -252   -587   1458       C  
ATOM   2640  O   PRO A 333      -1.913   9.371   9.083  1.00 60.93           O  
ANISOU 2640  O   PRO A 333     7345   9176   6629   -221   -593   1407       O  
ATOM   2641  CB  PRO A 333      -5.105   9.104   9.522  1.00 66.10           C  
ANISOU 2641  CB  PRO A 333     7901  10085   7127   -318   -519   1546       C  
ATOM   2642  CG  PRO A 333      -5.827   9.296  10.807  1.00 73.25           C  
ANISOU 2642  CG  PRO A 333     8768  11143   7920   -322   -494   1590       C  
ATOM   2643  CD  PRO A 333      -5.590   8.043  11.616  1.00 68.63           C  
ANISOU 2643  CD  PRO A 333     8209  10556   7311   -395   -553   1686       C  
ATOM   2644  N   GLN A 334      -2.340   9.569  11.268  1.00 64.34           N  
ANISOU 2644  N   GLN A 334     7763   9760   6921   -220   -588   1444       N  
ATOM   2645  CA  GLN A 334      -1.182  10.390  11.544  1.00 69.14           C  
ANISOU 2645  CA  GLN A 334     8391  10310   7566   -147   -601   1360       C  
ATOM   2646  C   GLN A 334       0.140   9.679  11.307  1.00 64.76           C  
ANISOU 2646  C   GLN A 334     7891   9627   7087   -157   -658   1352       C  
ATOM   2647  O   GLN A 334       1.144  10.321  11.084  1.00 60.81           O  
ANISOU 2647  O   GLN A 334     7400   9056   6646   -103   -668   1288       O  
ATOM   2648  CB  GLN A 334      -1.225  10.852  13.019  1.00 82.53           C  
ANISOU 2648  CB  GLN A 334    10079  12106   9171   -108   -601   1346       C  
ATOM   2649  CG  GLN A 334      -2.389  11.776  13.391  1.00 91.38           C  
ANISOU 2649  CG  GLN A 334    11141  13370  10207    -65   -549   1326       C  
ATOM   2650  CD  GLN A 334      -2.355  13.078  12.583  1.00102.20           C  
ANISOU 2650  CD  GLN A 334    12489  14699  11643      1   -526   1236       C  
ATOM   2651  NE2 GLN A 334      -3.495  13.772  12.490  1.00100.15           N  
ANISOU 2651  NE2 GLN A 334    12179  14542  11332     28   -482   1221       N  
ATOM   2652  OE1 GLN A 334      -1.312  13.441  12.033  1.00108.46           O  
ANISOU 2652  OE1 GLN A 334    13307  15370  12533     27   -552   1187       O  
ATOM   2653  N   GLU A 335       0.150   8.355  11.421  1.00 64.92           N  
ANISOU 2653  N   GLU A 335     7943   9618   7104   -224   -705   1422       N  
ATOM   2654  CA  GLU A 335       1.359   7.561  11.204  1.00 65.84           C  
ANISOU 2654  CA  GLU A 335     8113   9615   7288   -230   -770   1413       C  
ATOM   2655  C   GLU A 335       1.611   7.170   9.746  1.00 56.78           C  
ANISOU 2655  C   GLU A 335     6972   8380   6221   -228   -784   1393       C  
ATOM   2656  O   GLU A 335       2.621   6.550   9.450  1.00 57.09           O  
ANISOU 2656  O   GLU A 335     7048   8328   6314   -218   -838   1374       O  
ATOM   2657  CB  GLU A 335       1.305   6.253  11.989  1.00 67.98           C  
ANISOU 2657  CB  GLU A 335     8419   9882   7527   -301   -834   1496       C  
ATOM   2658  CG  GLU A 335       1.841   6.298  13.396  1.00 78.11           C  
ANISOU 2658  CG  GLU A 335     9720  11201   8755   -290   -855   1504       C  
ATOM   2659  CD  GLU A 335       1.995   4.891  13.962  1.00 81.18           C  
ANISOU 2659  CD  GLU A 335    10149  11555   9138   -364   -934   1591       C  
ATOM   2660  OE1 GLU A 335       1.113   4.526  14.758  1.00 78.77           O  
ANISOU 2660  OE1 GLU A 335     9819  11352   8754   -418   -931   1682       O  
ATOM   2661  OE2 GLU A 335       2.972   4.163  13.582  1.00 77.23           O1-
ANISOU 2661  OE2 GLU A 335     9699  10932   8711   -366  -1002   1572       O1-
ATOM   2662  N   VAL A 336       0.690   7.483   8.859  1.00 55.28           N  
ANISOU 2662  N   VAL A 336     6744   8224   6033   -233   -739   1396       N  
ATOM   2663  CA  VAL A 336       0.880   7.202   7.439  1.00 52.36           C  
ANISOU 2663  CA  VAL A 336     6374   7789   5729   -218   -749   1371       C  
ATOM   2664  C   VAL A 336       2.136   7.844   6.905  1.00 47.82           C  
ANISOU 2664  C   VAL A 336     5797   7159   5212   -147   -743   1303       C  
ATOM   2665  O   VAL A 336       2.974   7.213   6.298  1.00 47.87           O  
ANISOU 2665  O   VAL A 336     5826   7097   5265   -127   -788   1284       O  
ATOM   2666  CB  VAL A 336      -0.328   7.640   6.628  1.00 55.18           C  
ANISOU 2666  CB  VAL A 336     6685   8204   6074   -226   -693   1381       C  
ATOM   2667  CG1 VAL A 336      -0.039   7.580   5.151  1.00 55.71           C  
ANISOU 2667  CG1 VAL A 336     6745   8220   6202   -190   -694   1343       C  
ATOM   2668  CG2 VAL A 336      -1.501   6.770   6.973  1.00 56.25           C  
ANISOU 2668  CG2 VAL A 336     6820   8383   6167   -304   -714   1461       C  
ATOM   2669  N   GLY A 337       2.322   9.108   7.162  1.00 48.83           N  
ANISOU 2669  N   GLY A 337     5893   7318   5340   -104   -696   1268       N  
ATOM   2670  CA  GLY A 337       3.496   9.753   6.611  1.00 48.51           C  
ANISOU 2670  CA  GLY A 337     5838   7228   5365    -46   -696   1222       C  
ATOM   2671  C   GLY A 337       4.830   9.201   7.054  1.00 48.54           C  
ANISOU 2671  C   GLY A 337     5880   7164   5397    -31   -754   1207       C  
ATOM   2672  O   GLY A 337       5.714   8.923   6.209  1.00 47.79           O  
ANISOU 2672  O   GLY A 337     5782   7024   5352      0   -774   1189       O  
ATOM   2673  N   PRO A 338       5.038   9.089   8.379  1.00 49.76           N  
ANISOU 2673  N   PRO A 338     6067   7321   5517    -46   -781   1213       N  
ATOM   2674  CA  PRO A 338       6.375   8.542   8.836  1.00 51.98           C  
ANISOU 2674  CA  PRO A 338     6388   7531   5828    -31   -841   1198       C  
ATOM   2675  C   PRO A 338       6.677   7.123   8.262  1.00 50.42           C  
ANISOU 2675  C   PRO A 338     6228   7278   5648    -51   -900   1212       C  
ATOM   2676  O   PRO A 338       7.830   6.797   7.856  1.00 50.06           O  
ANISOU 2676  O   PRO A 338     6193   7175   5649    -13   -937   1182       O  
ATOM   2677  CB  PRO A 338       6.243   8.478  10.389  1.00 46.64           C  
ANISOU 2677  CB  PRO A 338     5743   6884   5093    -53   -862   1213       C  
ATOM   2678  CG  PRO A 338       5.251   9.561  10.676  1.00 50.38           C  
ANISOU 2678  CG  PRO A 338     6175   7442   5524    -42   -804   1207       C  
ATOM   2679  CD  PRO A 338       4.267   9.672   9.487  1.00 48.58           C  
ANISOU 2679  CD  PRO A 338     5910   7244   5303    -56   -756   1222       C  
ATOM   2680  N   LEU A 339       5.658   6.303   8.196  1.00 48.31           N  
ANISOU 2680  N   LEU A 339     5977   7029   5348   -105   -914   1257       N  
ATOM   2681  CA  LEU A 339       5.815   5.003   7.610  1.00 51.15           C  
ANISOU 2681  CA  LEU A 339     6373   7326   5734   -120   -987   1265       C  
ATOM   2682  C   LEU A 339       6.260   5.070   6.165  1.00 48.66           C  
ANISOU 2682  C   LEU A 339     6031   6992   5465    -58   -979   1216       C  
ATOM   2683  O   LEU A 339       7.191   4.407   5.791  1.00 46.58           O  
ANISOU 2683  O   LEU A 339     5787   6674   5235    -17  -1034   1181       O  
ATOM   2684  CB  LEU A 339       4.528   4.226   7.734  1.00 52.57           C  
ANISOU 2684  CB  LEU A 339     6565   7522   5885   -193  -1013   1328       C  
ATOM   2685  CG  LEU A 339       4.555   2.719   7.613  1.00 56.97           C  
ANISOU 2685  CG  LEU A 339     7174   7990   6481   -208  -1123   1334       C  
ATOM   2686  CD1 LEU A 339       4.759   2.327   6.178  1.00 62.02           C  
ANISOU 2686  CD1 LEU A 339     7851   8617   7097   -293  -1191   1415       C  
ATOM   2687  CD2 LEU A 339       5.584   2.069   8.496  1.00 62.22           C  
ANISOU 2687  CD2 LEU A 339     7826   8637   7175   -190  -1141   1313       C  
ATOM   2688  N   LEU A 340       5.600   5.885   5.357  1.00 44.93           N  
ANISOU 2688  N   LEU A 340     5506   6573   4989    -42   -908   1211       N  
ATOM   2689  CA  LEU A 340       5.940   5.973   3.952  1.00 44.32           C  
ANISOU 2689  CA  LEU A 340     5396   6500   4944     17   -896   1175       C  
ATOM   2690  C   LEU A 340       7.361   6.463   3.754  1.00 46.67           C  
ANISOU 2690  C   LEU A 340     5670   6786   5277     82   -893   1140       C  
ATOM   2691  O   LEU A 340       8.156   5.904   2.976  1.00 46.87           O  
ANISOU 2691  O   LEU A 340     5691   6793   5321    137   -931   1108       O  
ATOM   2692  CB  LEU A 340       4.955   6.881   3.252  1.00 47.34           C  
ANISOU 2692  CB  LEU A 340     5724   6947   5315     17   -818   1185       C  
ATOM   2693  CG  LEU A 340       3.527   6.362   3.144  1.00 49.01           C  
ANISOU 2693  CG  LEU A 340     5946   7178   5496    -39   -821   1220       C  
ATOM   2694  CD1 LEU A 340       2.671   7.440   2.482  1.00 51.67           C  
ANISOU 2694  CD1 LEU A 340     6225   7582   5823    -29   -737   1223       C  
ATOM   2695  CD2 LEU A 340       3.499   5.068   2.327  1.00 49.28           C  
ANISOU 2695  CD2 LEU A 340     6011   7165   5547    -30   -899   1206       C  
ATOM   2696  N   ASN A 341       7.711   7.490   4.502  1.00 46.74           N  
ANISOU 2696  N   ASN A 341     5659   6805   5292     81   -856   1145       N  
ATOM   2697  CA  ASN A 341       9.094   7.975   4.521  1.00 48.11           C  
ANISOU 2697  CA  ASN A 341     5809   6961   5508    130   -863   1124       C  
ATOM   2698  C   ASN A 341      10.127   6.931   4.851  1.00 43.99           C  
ANISOU 2698  C   ASN A 341     5334   6383   4996    148   -939   1103       C  
ATOM   2699  O   ASN A 341      11.166   6.849   4.232  1.00 44.70           O  
ANISOU 2699  O   ASN A 341     5397   6471   5114    204   -954   1081       O  
ATOM   2700  CB  ASN A 341       9.232   9.129   5.563  1.00 51.44           C  
ANISOU 2700  CB  ASN A 341     6219   7383   5940    118   -839   1130       C  
ATOM   2701  CG  ASN A 341       8.703  10.452   5.034  1.00 58.48           C  
ANISOU 2701  CG  ASN A 341     7045   8320   6851    129   -775   1140       C  
ATOM   2702  ND2 ASN A 341       7.609  10.946   5.619  1.00 58.71           N  
ANISOU 2702  ND2 ASN A 341     7080   8379   6845     97   -747   1146       N  
ATOM   2703  OD1 ASN A 341       9.258  11.007   4.083  1.00 63.61           O  
ANISOU 2703  OD1 ASN A 341     7637   8987   7544    166   -754   1145       O  
ATOM   2704  N   THR A 342       9.890   6.221   5.937  1.00 43.43           N  
ANISOU 2704  N   THR A 342     5326   6272   4900     99   -986   1115       N  
ATOM   2705  CA  THR A 342      10.740   5.109   6.319  1.00 44.77           C  
ANISOU 2705  CA  THR A 342     5550   6380   5081    107  -1071   1097       C  
ATOM   2706  C   THR A 342      10.907   4.074   5.164  1.00 44.77           C  
ANISOU 2706  C   THR A 342     5556   6361   5091    150  -1124   1067       C  
ATOM   2707  O   THR A 342      12.026   3.615   4.860  1.00 42.89           O  
ANISOU 2707  O   THR A 342     5322   6099   4876    208  -1172   1027       O  
ATOM   2708  CB  THR A 342      10.140   4.418   7.525  1.00 49.62           C  
ANISOU 2708  CB  THR A 342     6226   6966   5661     36  -1115   1134       C  
ATOM   2709  CG2 THR A 342      10.806   3.133   7.755  1.00 48.58           C  
ANISOU 2709  CG2 THR A 342     6152   6761   5544     36  -1215   1123       C  
ATOM   2710  OG1 THR A 342      10.296   5.260   8.684  1.00 52.59           O  
ANISOU 2710  OG1 THR A 342     6601   7360   6021     21  -1085   1145       O  
ATOM   2711  N   MET A 343       9.805   3.779   4.511  1.00 43.15           N  
ANISOU 2711  N   MET A 343     5348   6176   4869    129  -1116   1079       N  
ATOM   2712  CA  MET A 343       9.771   2.901   3.352  1.00 46.55           C  
ANISOU 2712  CA  MET A 343     5781   6597   5307    177  -1168   1042       C  
ATOM   2713  C   MET A 343      10.627   3.399   2.166  1.00 48.07           C  
ANISOU 2713  C   MET A 343     5908   6848   5508    276  -1132    999       C  
ATOM   2714  O   MET A 343      11.339   2.599   1.544  1.00 43.39           O  
ANISOU 2714  O   MET A 343     5322   6242   4920    347  -1197    948       O  
ATOM   2715  CB  MET A 343       8.308   2.718   2.934  1.00 47.47           C  
ANISOU 2715  CB  MET A 343     5898   6730   5405    130  -1156   1071       C  
ATOM   2716  CG  MET A 343       7.971   1.351   2.403  1.00 54.47           C  
ANISOU 2716  CG  MET A 343     6830   7560   6305    136  -1263   1049       C  
ATOM   2717  SD  MET A 343       6.352   1.117   1.653  1.00 53.18           S  
ANISOU 2717  SD  MET A 343     6657   7414   6132     95  -1260   1075       S  
ATOM   2718  CE  MET A 343       5.470   2.049   2.836  1.00 58.84           C  
ANISOU 2718  CE  MET A 343     7359   8177   6818     -4  -1168   1158       C  
ATOM   2719  N   ILE A 344      10.633   4.708   1.877  1.00 46.76           N  
ANISOU 2719  N   ILE A 344     5672   6748   5344    285  -1035   1022       N  
ATOM   2720  CA  ILE A 344      11.394   5.155   0.726  1.00 44.98           C  
ANISOU 2720  CA  ILE A 344     5372   6594   5124    371  -1001   1002       C  
ATOM   2721  C   ILE A 344      12.786   5.654   0.985  1.00 44.87           C  
ANISOU 2721  C   ILE A 344     5321   6591   5137    410   -995   1003       C  
ATOM   2722  O   ILE A 344      13.594   5.605   0.064  1.00 45.75           O  
ANISOU 2722  O   ILE A 344     5376   6761   5245    491   -995    984       O  
ATOM   2723  CB  ILE A 344      10.663   6.192  -0.163  1.00 50.62           C  
ANISOU 2723  CB  ILE A 344     6014   7386   5830    375   -912   1033       C  
ATOM   2724  CG1 ILE A 344      10.741   7.574   0.439  1.00 61.15           C  
ANISOU 2724  CG1 ILE A 344     7308   8732   7192    336   -846   1078       C  
ATOM   2725  CG2 ILE A 344       9.208   5.858  -0.340  1.00 52.36           C  
ANISOU 2725  CG2 ILE A 344     6266   7599   6028    328   -909   1039       C  
ATOM   2726  CD1 ILE A 344      10.891   8.645  -0.604  1.00 70.67           C  
ANISOU 2726  CD1 ILE A 344     8417  10021   8412    374   -777   1109       C  
ATOM   2727  N   LYS A 345      13.129   6.140   2.180  1.00 46.85           N  
ANISOU 2727  N   LYS A 345     5592   6795   5411    362   -993   1025       N  
ATOM   2728  CA  LYS A 345      14.378   6.885   2.284  1.00 49.27           C  
ANISOU 2728  CA  LYS A 345     5844   7121   5756    396   -978   1037       C  
ATOM   2729  C   LYS A 345      15.499   5.946   2.159  1.00 46.91           C  
ANISOU 2729  C   LYS A 345     5559   6808   5455    457  -1044    996       C  
ATOM   2730  O   LYS A 345      15.612   4.978   2.921  1.00 47.16           O  
ANISOU 2730  O   LYS A 345     5670   6766   5480    440  -1117    966       O  
ATOM   2731  CB  LYS A 345      14.546   7.639   3.620  1.00 57.24           C  
ANISOU 2731  CB  LYS A 345     6875   8078   6795    341   -973   1059       C  
ATOM   2732  CG  LYS A 345      13.913   9.018   3.666  1.00 64.04           C  
ANISOU 2732  CG  LYS A 345     7688   8965   7677    308   -907   1098       C  
ATOM   2733  CD  LYS A 345      13.427   9.390   5.055  1.00 73.69           C  
ANISOU 2733  CD  LYS A 345     8963  10138   8895    251   -916   1099       C  
ATOM   2734  CE  LYS A 345      14.320  10.412   5.730  1.00 81.73           C  
ANISOU 2734  CE  LYS A 345     9952  11129   9970    258   -926   1107       C  
ATOM   2735  NZ  LYS A 345      13.476  11.129   6.721  1.00 90.94           N1+
ANISOU 2735  NZ  LYS A 345    11145  12281  11126    219   -915   1104       N1+
ATOM   2736  N   GLY A 346      16.387   6.254   1.242  1.00 45.40           N  
ANISOU 2736  N   GLY A 346     5284   6694   5270    531  -1023    999       N  
ATOM   2737  CA  GLY A 346      17.572   5.447   1.063  1.00 44.98           C  
ANISOU 2737  CA  GLY A 346     5229   6649   5211    606  -1084    956       C  
ATOM   2738  C   GLY A 346      17.254   4.105   0.363  1.00 43.99           C  
ANISOU 2738  C   GLY A 346     5147   6525   5041    665  -1150    888       C  
ATOM   2739  O   GLY A 346      18.115   3.254   0.276  1.00 46.28           O  
ANISOU 2739  O   GLY A 346     5452   6809   5322    733  -1220    835       O  
ATOM   2740  N   ARG A 347      16.024   3.954  -0.113  1.00 43.20           N  
ANISOU 2740  N   ARG A 347     5066   6429   4917    642  -1135    887       N  
ATOM   2741  CA  ARG A 347      15.503   2.675  -0.590  1.00 47.22           C  
ANISOU 2741  CA  ARG A 347     5633   6907   5399    678  -1217    824       C  
ATOM   2742  C   ARG A 347      14.947   2.791  -1.991  1.00 47.56           C  
ANISOU 2742  C   ARG A 347     5617   7047   5404    741  -1180    810       C  
ATOM   2743  O   ARG A 347      15.263   1.972  -2.857  1.00 51.02           O  
ANISOU 2743  O   ARG A 347     6049   7525   5811    843  -1240    742       O  
ATOM   2744  CB  ARG A 347      14.420   2.150   0.385  1.00 44.18           C  
ANISOU 2744  CB  ARG A 347     5346   6411   5027    573  -1261    839       C  
ATOM   2745  CG  ARG A 347      15.067   1.585   1.657  1.00 43.99           C  
ANISOU 2745  CG  ARG A 347     5392   6291   5028    535  -1333    834       C  
ATOM   2746  CD  ARG A 347      14.093   0.710   2.473  1.00 46.03           C  
ANISOU 2746  CD  ARG A 347     5745   6450   5293    447  -1405    850       C  
ATOM   2747  NE  ARG A 347      13.759  -0.591   1.832  1.00 46.26           N  
ANISOU 2747  NE  ARG A 347     5819   6433   5323    486  -1516    797       N  
ATOM   2748  CZ  ARG A 347      12.534  -1.032   1.547  1.00 44.67           C  
ANISOU 2748  CZ  ARG A 347     5645   6206   5120    441  -1544    812       C  
ATOM   2749  NH1 ARG A 347      11.475  -0.286   1.764  1.00 39.80           N1+
ANISOU 2749  NH1 ARG A 347     5010   5620   4492    361  -1458    877       N1+
ATOM   2750  NH2 ARG A 347      12.376  -2.267   1.026  1.00 49.68           N  
ANISOU 2750  NH2 ARG A 347     6324   6781   5769    483  -1671    758       N  
ATOM   2751  N   TYR A 348      14.133   3.805  -2.179  1.00 45.57           N  
ANISOU 2751  N   TYR A 348     5325   6834   5154    687  -1089    869       N  
ATOM   2752  CA  TYR A 348      13.527   4.139  -3.449  1.00 50.96           C  
ANISOU 2752  CA  TYR A 348     5945   7614   5803    734  -1038    872       C  
ATOM   2753  C   TYR A 348      13.734   5.578  -3.902  1.00 51.36           C  
ANISOU 2753  C   TYR A 348     5889   7763   5860    731   -929    946       C  
ATOM   2754  O   TYR A 348      13.159   5.948  -4.860  1.00 49.11           O  
ANISOU 2754  O   TYR A 348     5554   7556   5550    757   -881    961       O  
ATOM   2755  CB  TYR A 348      12.035   3.933  -3.378  1.00 48.88           C  
ANISOU 2755  CB  TYR A 348     5736   7297   5537    663  -1040    878       C  
ATOM   2756  CG  TYR A 348      11.629   2.493  -3.303  1.00 55.99           C  
ANISOU 2756  CG  TYR A 348     6724   8114   6434    672  -1157    815       C  
ATOM   2757  CD1 TYR A 348      11.574   1.719  -4.451  1.00 55.31           C  
ANISOU 2757  CD1 TYR A 348     6630   8068   6317    773  -1216    745       C  
ATOM   2758  CD2 TYR A 348      11.256   1.906  -2.087  1.00 53.51           C  
ANISOU 2758  CD2 TYR A 348     6499   7680   6150    580  -1219    828       C  
ATOM   2759  CE1 TYR A 348      11.183   0.391  -4.395  1.00 56.75           C  
ANISOU 2759  CE1 TYR A 348     6894   8156   6510    782  -1345    685       C  
ATOM   2760  CE2 TYR A 348      10.840   0.590  -2.036  1.00 53.22           C  
ANISOU 2760  CE2 TYR A 348     6539   7558   6124    577  -1339    786       C  
ATOM   2761  CZ  TYR A 348      10.818  -0.163  -3.192  1.00 52.35           C  
ANISOU 2761  CZ  TYR A 348     6423   7472   5995    678  -1408    712       C  
ATOM   2762  OH  TYR A 348      10.441  -1.456  -3.160  1.00 45.78           O  
ANISOU 2762  OH  TYR A 348     5666   6542   5186    679  -1547    667       O  
ATOM   2763  N   ASN A 349      14.567   6.379  -3.241  1.00 58.96           N  
ANISOU 2763  N   ASN A 349     6817   8720   6863    701   -899    995       N  
ATOM   2764  CA  ASN A 349      14.839   7.751  -3.755  1.00 61.73           C  
ANISOU 2764  CA  ASN A 349     7057   9162   7235    700   -813   1076       C  
ATOM   2765  C   ASN A 349      16.325   8.171  -4.040  1.00 63.84           C  
ANISOU 2765  C   ASN A 349     7228   9511   7517    759   -803   1114       C  
ATOM   2766  O   ASN A 349      17.297   7.578  -3.496  1.00 70.81           O  
ANISOU 2766  O   ASN A 349     8135  10360   8405    787   -858   1080       O  
ATOM   2767  CB  ASN A 349      14.158   8.748  -2.830  1.00 57.40           C  
ANISOU 2767  CB  ASN A 349     6531   8539   6737    593   -775   1125       C  
ATOM   2768  CG  ASN A 349      14.769   8.823  -1.444  1.00 53.54           C  
ANISOU 2768  CG  ASN A 349     6094   7955   6293    544   -813   1124       C  
ATOM   2769  ND2 ASN A 349      14.130   9.615  -0.618  1.00 61.16           N  
ANISOU 2769  ND2 ASN A 349     7083   8863   7291    466   -790   1152       N  
ATOM   2770  OD1 ASN A 349      15.767   8.190  -1.098  1.00 54.05           O  
ANISOU 2770  OD1 ASN A 349     6177   7999   6360    578   -864   1095       O  
TER   
END


A second structure was input as follows:


ATOM      1  N   ALA A   8     -43.382  11.102 -28.773  1.00102.34           N  
ANISOU    1  N   ALA A   8    11519  14216  13147    161   -202  -1898       N  
ATOM      2  CA  ALA A   8     -43.072  11.703 -30.062  1.00100.38           C  
ANISOU    2  CA  ALA A   8    11255  14094  12790    215   -245  -1905       C  
ATOM      3  C   ALA A   8     -42.383  13.060 -29.929  1.00100.18           C  
ANISOU    3  C   ALA A   8    11314  14066  12682    257   -258  -1762       C  
ATOM      4  O   ALA A   8     -41.288  13.244 -30.440  1.00 99.62           O  
ANISOU    4  O   ALA A   8    11287  13957  12604    255   -251  -1716       O  
ATOM      5  CB  ALA A   8     -44.325  11.802 -30.928  1.00 94.99           C  
ANISOU    5  CB  ALA A   8    10485  13555  12050    250   -282  -1999       C  
ATOM      6  N   VAL A   9     -43.014  14.010 -29.246  1.00101.83           N  
ANISOU    6  N   VAL A   9    11544  14309  12836    290   -271  -1696       N  
ATOM      7  CA  VAL A   9     -42.357  15.281 -28.957  1.00 98.70           C  
ANISOU    7  CA  VAL A   9    11226  13900  12372    325   -274  -1562       C  
ATOM      8  C   VAL A   9     -42.009  15.418 -27.465  1.00102.25           C  
ANISOU    8  C   VAL A   9    11754  14212  12882    285   -241  -1471       C  
ATOM      9  O   VAL A   9     -41.187  16.231 -27.079  1.00 96.27           O  
ANISOU    9  O   VAL A   9    11063  13422  12093    298   -236  -1374       O  
ATOM     10  CB  VAL A   9     -43.160  16.477 -29.468  1.00 94.60           C  
ANISOU   10  CB  VAL A   9    10695  13488  11758    389   -298  -1526       C  
ATOM     11  CG1 VAL A   9     -42.270  17.690 -29.612  1.00 88.89           C  
ANISOU   11  CG1 VAL A   9    10045  12762  10967    430   -294  -1401       C  
ATOM     12  CG2 VAL A   9     -43.793  16.140 -30.798  1.00 91.32           C  
ANISOU   12  CG2 VAL A   9    10195  13221  11281    433   -331  -1622       C  
ATOM     13  N   ALA A  10     -42.627  14.588 -26.646  1.00 90.17           N  
ANISOU   13  N   ALA A  10    10213  12605  11441    239   -216  -1505       N  
ATOM     14  CA  ALA A  10     -42.151  14.325 -25.318  1.00 75.68           C  
ANISOU   14  CA  ALA A  10     8441  10641   9674    199   -181  -1440       C  
ATOM     15  C   ALA A  10     -41.142  13.168 -25.382  1.00 96.00           C  
ANISOU   15  C   ALA A  10    11017  13147  12309    165   -159  -1468       C  
ATOM     16  O   ALA A  10     -41.287  12.170 -24.684  1.00102.16           O  
ANISOU   16  O   ALA A  10    11801  13835  13178    125   -122  -1480       O  
ATOM     17  CB  ALA A  10     -43.303  13.953 -24.428  1.00 69.59           C  
ANISOU   17  CB  ALA A  10     7655   9813   8971    169   -157  -1460       C  
ATOM     18  N   SER A  11     -40.131  13.294 -26.232  1.00 88.55           N  
ANISOU   18  N   SER A  11    10072  12247  11323    183   -175  -1474       N  
ATOM     19  CA  SER A  11     -39.178  12.216 -26.449  1.00 87.24           C  
ANISOU   19  CA  SER A  11     9899  12028  11218    155   -153  -1513       C  
ATOM     20  C   SER A  11     -38.190  12.030 -25.313  1.00 87.55           C  
ANISOU   20  C   SER A  11    10009  11964  11293    136   -126  -1426       C  
ATOM     21  O   SER A  11     -37.329  11.175 -25.392  1.00 80.40           O  
ANISOU   21  O   SER A  11     9103  11026  10419    123   -111  -1441       O  
ATOM     22  CB  SER A  11     -38.392  12.421 -27.744  1.00 89.96           C  
ANISOU   22  CB  SER A  11    10210  12462  11506    182   -180  -1562       C  
ATOM     23  OG  SER A  11     -38.727  13.625 -28.388  1.00 79.45           O  
ANISOU   23  OG  SER A  11     8914  11194  10078    227   -208  -1488       O  
ATOM     24  N   GLY A  12     -38.304  12.836 -24.269  1.00 83.25           N  
ANISOU   24  N   GLY A  12     9518  11373  10739    136   -120  -1339       N  
ATOM     25  CA  GLY A  12     -37.388  12.757 -23.153  1.00 77.82           C  
ANISOU   25  CA  GLY A  12     8893  10600  10072    123    -98  -1255       C  
ATOM     26  C   GLY A  12     -35.934  12.820 -23.572  1.00 81.82           C  
ANISOU   26  C   GLY A  12     9426  11119  10541    136   -110  -1220       C  
ATOM     27  O   GLY A  12     -35.557  13.686 -24.334  1.00 82.14           O  
ANISOU   27  O   GLY A  12     9472  11229  10506    166   -139  -1200       O  
ATOM     28  N   SER A  13     -35.126  11.894 -23.083  1.00 71.74           N  
ANISOU   28  N   SER A  13     8162   9776   9317    118    -83  -1212       N  
ATOM     29  CA  SER A  13     -33.692  11.926 -23.322  1.00 79.74           C  
ANISOU   29  CA  SER A  13     9200  10793  10302    128    -91  -1175       C  
ATOM     30  C   SER A  13     -33.254  11.424 -24.696  1.00 87.67           C  
ANISOU   30  C   SER A  13    10162  11857  11289    139   -104  -1243       C  
ATOM     31  O   SER A  13     -32.091  11.536 -25.061  1.00 83.71           O  
ANISOU   31  O   SER A  13     9678  11367  10759    150   -112  -1215       O  
ATOM     32  CB  SER A  13     -32.973  11.136 -22.241  1.00 77.31           C  
ANISOU   32  CB  SER A  13     8924  10397  10052    111    -56  -1131       C  
ATOM     33  OG  SER A  13     -32.762  11.933 -21.101  1.00 71.80           O  
ANISOU   33  OG  SER A  13     8275   9662   9342    111    -53  -1053       O  
ATOM     34  N   GLY A  14     -34.182  10.869 -25.454  1.00 80.58           N  
ANISOU   34  N   GLY A  14     9205  11001  10408    135   -107  -1335       N  
ATOM     35  CA  GLY A  14     -33.853  10.348 -26.754  1.00 78.98           C  
ANISOU   35  CA  GLY A  14     8955  10859  10194    144   -118  -1413       C  
ATOM     36  C   GLY A  14     -33.291   8.953 -26.663  1.00 77.98           C  
ANISOU   36  C   GLY A  14     8810  10669  10150    117    -82  -1460       C  
ATOM     37  O   GLY A  14     -33.153   8.384 -25.595  1.00 72.43           O  
ANISOU   37  O   GLY A  14     8132   9873   9514     95    -44  -1425       O  
ATOM     38  N   GLU A  15     -32.976   8.392 -27.810  1.00 84.14           N  
ANISOU   38  N   GLU A  15     9543  11501  10922    122    -89  -1539       N  
ATOM     39  CA  GLU A  15     -32.382   7.088 -27.839  1.00 90.32           C  
ANISOU   39  CA  GLU A  15    10313  12232  11773    103    -54  -1578       C  
ATOM     40  C   GLU A  15     -30.949   7.264 -27.405  1.00 80.86           C  
ANISOU   40  C   GLU A  15     9175  10983  10562    111    -47  -1476       C  
ATOM     41  O   GLU A  15     -30.266   8.141 -27.892  1.00 76.39           O  
ANISOU   41  O   GLU A  15     8637  10469   9917    138    -80  -1423       O  
ATOM     42  CB  GLU A  15     -32.475   6.517 -29.241  1.00 99.39           C  
ANISOU   42  CB  GLU A  15    11408  13465  12890    115    -73  -1669       C  
ATOM     43  CG  GLU A  15     -33.850   5.990 -29.571  1.00104.97           C  
ANISOU   43  CG  GLU A  15    12040  14221  13620    103    -76  -1792       C  
ATOM     44  CD  GLU A  15     -34.032   4.553 -29.141  1.00115.39           C  
ANISOU   44  CD  GLU A  15    13332  15443  15065     58    -18  -1851       C  
ATOM     45  OE1 GLU A  15     -33.530   3.661 -29.854  1.00117.38           O  
ANISOU   45  OE1 GLU A  15    13558  15666  15376     41     13  -1911       O  
ATOM     46  OE2 GLU A  15     -34.672   4.314 -28.092  1.00114.66           O1-
ANISOU   46  OE2 GLU A  15    13247  15300  15015     41      0  -1832       O1-
ATOM     47  N   PRO A  16     -30.506   6.449 -26.469  1.00 71.04           N  
ANISOU   47  N   PRO A  16     7951   9642   9397     90     -2  -1448       N  
ATOM     48  CA  PRO A  16     -29.106   6.534 -25.980  1.00 77.11           C  
ANISOU   48  CA  PRO A  16     8768  10375  10153    101      3  -1363       C  
ATOM     49  C   PRO A  16     -28.100   6.622 -27.145  1.00 78.77           C  
ANISOU   49  C   PRO A  16     8969  10646  10312    120    -20  -1379       C  
ATOM     50  O   PRO A  16     -28.230   5.914 -28.153  1.00 76.33           O  
ANISOU   50  O   PRO A  16     8613  10368  10020    116    -15  -1467       O  
ATOM     51  CB  PRO A  16     -28.907   5.222 -25.211  1.00 72.85           C  
ANISOU   51  CB  PRO A  16     8226   9738   9715     82     63  -1366       C  
ATOM     52  CG  PRO A  16     -30.294   4.719 -24.919  1.00 71.77           C  
ANISOU   52  CG  PRO A  16     8055   9569   9643     59     92  -1426       C  
ATOM     53  CD  PRO A  16     -31.202   5.248 -25.989  1.00 72.73           C  
ANISOU   53  CD  PRO A  16     8134   9782   9717     61     50  -1503       C  
ATOM     54  N   ARG A  17     -27.130   7.506 -27.046  1.00 81.68           N  
ANISOU   54  N   ARG A  17     9379  11036  10619    140    -44  -1301       N  
ATOM     55  CA  ARG A  17     -26.080   7.560 -28.071  1.00 87.88           C  
ANISOU   55  CA  ARG A  17    10159  11869  11361    158    -60  -1308       C  
ATOM     56  C   ARG A  17     -25.177   6.322 -27.961  1.00 78.51           C  
ANISOU   56  C   ARG A  17     8967  10624  10239    148    -23  -1319       C  
ATOM     57  O   ARG A  17     -25.032   5.722 -26.887  1.00 75.34           O  
ANISOU   57  O   ARG A  17     8583  10144   9899    135     12  -1284       O  
ATOM     58  CB  ARG A  17     -25.249   8.836 -27.937  1.00 88.46           C  
ANISOU   58  CB  ARG A  17    10278  11972  11361    180    -88  -1221       C  
ATOM     59  CG  ARG A  17     -26.076  10.109 -28.043  1.00 88.67           C  
ANISOU   59  CG  ARG A  17    10313  12051  11325    194   -118  -1202       C  
ATOM     60  CD  ARG A  17     -25.393  11.255 -27.321  1.00 94.09           C  
ANISOU   60  CD  ARG A  17    11051  12726  11973    201   -128  -1107       C  
ATOM     61  NE  ARG A  17     -25.161  11.024 -25.871  1.00 96.50           N  
ANISOU   61  NE  ARG A  17    11387  12954  12324    181   -108  -1056       N  
ATOM     62  CZ  ARG A  17     -25.881  11.534 -24.847  1.00100.21           C  
ANISOU   62  CZ  ARG A  17    11879  13396  12799    172   -107  -1022       C  
ATOM     63  NH1 ARG A  17     -26.927  12.339 -25.055  1.00 84.98           N1+
ANISOU   63  NH1 ARG A  17     9946  11503  10838    178   -122  -1031       N1+
ATOM     64  NH2 ARG A  17     -25.539  11.243 -23.581  1.00 95.81           N  
ANISOU   64  NH2 ARG A  17    11348  12777  12278    160    -88   -976       N  
ATOM     65  N   GLU A  18     -24.598   5.951 -29.094  1.00 71.27           N  
ANISOU   65  N   GLU A  18     8024   9748   9305    158    -28  -1367       N  
ATOM     66  CA  GLU A  18     -23.703   4.816 -29.195  1.00 70.09           C  
ANISOU   66  CA  GLU A  18     7866   9552   9212    152      7  -1383       C  
ATOM     67  C   GLU A  18     -22.279   5.304 -28.974  1.00 67.38           C  
ANISOU   67  C   GLU A  18     7562   9207   8830    170     -3  -1297       C  
ATOM     68  O   GLU A  18     -21.822   6.178 -29.664  1.00 61.77           O  
ANISOU   68  O   GLU A  18     6861   8561   8047    190    -37  -1279       O  
ATOM     69  CB  GLU A  18     -23.770   4.203 -30.614  1.00 75.05           C  
ANISOU   69  CB  GLU A  18     8443  10235   9838    154      5  -1485       C  
ATOM     70  CG  GLU A  18     -25.071   3.510 -31.001  1.00 74.11           C  
ANISOU   70  CG  GLU A  18     8268  10122   9765    133     20  -1595       C  
ATOM     71  CD  GLU A  18     -25.192   2.109 -30.440  1.00 73.92           C  
ANISOU   71  CD  GLU A  18     8226  10001   9858    103     83  -1634       C  
ATOM     72  OE1 GLU A  18     -24.347   1.672 -29.635  1.00 77.18           O  
ANISOU   72  OE1 GLU A  18     8671  10339  10314    103    117  -1566       O  
ATOM     73  OE2 GLU A  18     -26.163   1.442 -30.791  1.00 84.38           O1-
ANISOU   73  OE2 GLU A  18     9500  11324  11234     81    103  -1734       O1-
ATOM     74  N   GLU A  19     -21.550   4.694 -28.057  1.00 62.94           N  
ANISOU   74  N   GLU A  19     7020   8574   8317    166     29  -1246       N  
ATOM     75  CA  GLU A  19     -20.147   5.071 -27.865  1.00 57.86           C  
ANISOU   75  CA  GLU A  19     6408   7934   7641    183     19  -1173       C  
ATOM     76  C   GLU A  19     -19.319   4.700 -29.118  1.00 56.15           C  
ANISOU   76  C   GLU A  19     6169   7755   7408    194     17  -1214       C  
ATOM     77  O   GLU A  19     -19.588   3.706 -29.837  1.00 56.51           O  
ANISOU   77  O   GLU A  19     6178   7796   7497    187     41  -1293       O  
ATOM     78  CB  GLU A  19     -19.493   4.388 -26.639  1.00 55.98           C  
ANISOU   78  CB  GLU A  19     6191   7621   7458    183     56  -1112       C  
ATOM     79  CG  GLU A  19     -20.331   4.029 -25.432  1.00 68.03           C  
ANISOU   79  CG  GLU A  19     7726   9085   9036    173     86  -1092       C  
ATOM     80  CD  GLU A  19     -19.540   3.245 -24.368  1.00 86.40           C  
ANISOU   80  CD  GLU A  19    10069  11347  11410    186    128  -1029       C  
ATOM     81  OE1 GLU A  19     -18.278   3.445 -24.200  1.00 91.29           O  
ANISOU   81  OE1 GLU A  19    10705  11981  12000    204    117   -974       O  
ATOM     82  OE2 GLU A  19     -20.211   2.404 -23.701  1.00 84.37           O1-
ANISOU   82  OE2 GLU A  19     9805  11026  11223    180    176  -1036       O1-
ATOM     83  N   ALA A  20     -18.288   5.482 -29.340  1.00 50.99           N  
ANISOU   83  N   ALA A  20     5537   7136   6698    211     -7  -1161       N  
ATOM     84  CA  ALA A  20     -17.362   5.262 -30.403  1.00 57.49           C  
ANISOU   84  CA  ALA A  20     6347   7995   7501    226     -8  -1182       C  
ATOM     85  C   ALA A  20     -16.685   3.836 -30.301  1.00 57.88           C  
ANISOU   85  C   ALA A  20     6382   7985   7624    221     36  -1200       C  
ATOM     86  O   ALA A  20     -16.449   3.313 -29.180  1.00 49.30           O  
ANISOU   86  O   ALA A  20     5310   6832   6588    217     65  -1154       O  
ATOM     87  CB  ALA A  20     -16.317   6.368 -30.382  1.00 57.34           C  
ANISOU   87  CB  ALA A  20     6357   8006   7420    243    -34  -1108       C  
ATOM     88  N   GLY A  21     -16.346   3.274 -31.475  1.00 53.96           N  
ANISOU   88  N   GLY A  21     5856   7516   7128    228     43  -1261       N  
ATOM     89  CA  GLY A  21     -15.683   1.983 -31.582  1.00 49.49           C  
ANISOU   89  CA  GLY A  21     5273   6900   6628    225     88  -1285       C  
ATOM     90  C   GLY A  21     -16.592   0.815 -31.214  1.00 52.99           C  
ANISOU   90  C   GLY A  21     5692   7279   7161    203    135  -1344       C  
ATOM     91  O   GLY A  21     -16.113  -0.216 -30.761  1.00 47.25           O  
ANISOU   91  O   GLY A  21     4962   6483   6505    202    185  -1333       O  
ATOM     92  N   ALA A  22     -17.907   1.015 -31.406  1.00 55.85           N  
ANISOU   92  N   ALA A  22     6033   7663   7521    188    123  -1404       N  
ATOM     93  CA  ALA A  22     -18.956   0.018 -31.266  1.00 54.42           C  
ANISOU   93  CA  ALA A  22     5819   7432   7423    162    165  -1481       C  
ATOM     94  C   ALA A  22     -18.980  -0.585 -29.868  1.00 56.09           C  
ANISOU   94  C   ALA A  22     6052   7546   7711    155    215  -1421       C  
ATOM     95  O   ALA A  22     -19.197  -1.786 -29.702  1.00 53.50           O  
ANISOU   95  O   ALA A  22     5701   7147   7476    141    276  -1463       O  
ATOM     96  CB  ALA A  22     -18.774  -1.045 -32.328  1.00 51.88           C  
ANISOU   96  CB  ALA A  22     5454   7113   7145    155    196  -1579       C  
ATOM     97  N   LEU A  23     -18.781   0.264 -28.858  1.00 58.22           N  
ANISOU   97  N   LEU A  23     6364   7812   7942    167    191  -1324       N  
ATOM     98  CA  LEU A  23     -18.762  -0.185 -27.473  1.00 58.34           C  
ANISOU   98  CA  LEU A  23     6402   7748   8014    170    233  -1256       C  
ATOM     99  C   LEU A  23     -20.165  -0.204 -26.863  1.00 59.83           C  
ANISOU   99  C   LEU A  23     6585   7907   8241    150    248  -1281       C  
ATOM    100  O   LEU A  23     -20.313  -0.359 -25.667  1.00 66.44           O  
ANISOU  100  O   LEU A  23     7445   8688   9111    156    276  -1219       O  
ATOM    101  CB  LEU A  23     -17.817   0.673 -26.655  1.00 61.13           C  
ANISOU  101  CB  LEU A  23     6799   8117   8308    193    203  -1148       C  
ATOM    102  CG  LEU A  23     -16.348   0.624 -27.093  1.00 64.66           C  
ANISOU  102  CG  LEU A  23     7252   8586   8728    213    196  -1115       C  
ATOM    103  CD1 LEU A  23     -15.537   1.686 -26.372  1.00 68.32           C  
ANISOU  103  CD1 LEU A  23     7751   9080   9124    230    156  -1023       C  
ATOM    104  CD2 LEU A  23     -15.729  -0.734 -26.848  1.00 68.29           C  
ANISOU  104  CD2 LEU A  23     7701   8977   9267    223    261  -1108       C  
ATOM    105  N   GLY A  24     -21.197  -0.118 -27.697  1.00 62.60           N  
ANISOU  105  N   GLY A  24     6900   8294   8588    130    232  -1374       N  
ATOM    106  CA  GLY A  24     -22.579  -0.320 -27.251  1.00 58.31           C  
ANISOU  106  CA  GLY A  24     6339   7718   8095    107    253  -1415       C  
ATOM    107  C   GLY A  24     -23.228   0.965 -26.741  1.00 62.13           C  
ANISOU  107  C   GLY A  24     6850   8245   8510    111    202  -1369       C  
ATOM    108  O   GLY A  24     -22.571   2.008 -26.596  1.00 52.57           O  
ANISOU  108  O   GLY A  24     5675   7079   7219    129    155  -1299       O  
ATOM    109  N   PRO A  25     -24.527   0.903 -26.440  1.00 59.21           N  
ANISOU  109  N   PRO A  25     6463   7857   8176     91    214  -1410       N  
ATOM    110  CA  PRO A  25     -25.157   2.129 -25.951  1.00 57.97           C  
ANISOU  110  CA  PRO A  25     6332   7739   7955     95    168  -1366       C  
ATOM    111  C   PRO A  25     -24.544   2.596 -24.655  1.00 57.14           C  
ANISOU  111  C   PRO A  25     6280   7598   7831    112    169  -1249       C  
ATOM    112  O   PRO A  25     -24.259   1.800 -23.786  1.00 51.83           O  
ANISOU  112  O   PRO A  25     5619   6852   7221    116    221  -1210       O  
ATOM    113  CB  PRO A  25     -26.637   1.730 -25.767  1.00 55.66           C  
ANISOU  113  CB  PRO A  25     6005   7418   7723     70    194  -1433       C  
ATOM    114  CG  PRO A  25     -26.638   0.226 -25.769  1.00 58.71           C  
ANISOU  114  CG  PRO A  25     6359   7724   8221     53    268  -1488       C  
ATOM    115  CD  PRO A  25     -25.500  -0.177 -26.674  1.00 57.65           C  
ANISOU  115  CD  PRO A  25     6215   7614   8072     63    265  -1508       C  
ATOM    116  N   ALA A  26     -24.320   3.886 -24.530  1.00 59.79           N  
ANISOU  116  N   ALA A  26     6647   7989   8081    124    116  -1195       N  
ATOM    117  CA  ALA A  26     -23.706   4.375 -23.331  1.00 69.76           C  
ANISOU  117  CA  ALA A  26     7955   9227   9321    139    113  -1096       C  
ATOM    118  C   ALA A  26     -24.532   4.005 -22.013  1.00 63.39           C  
ANISOU  118  C   ALA A  26     7161   8353   8571    135    154  -1064       C  
ATOM    119  O   ALA A  26     -23.992   3.727 -20.938  1.00 71.78           O  
ANISOU  119  O   ALA A  26     8250   9372   9651    151    180   -993       O  
ATOM    120  CB  ALA A  26     -23.479   5.868 -23.521  1.00 66.72           C  
ANISOU  120  CB  ALA A  26     7595   8913   8842    148     53  -1059       C  
ATOM    121  N   TRP A  27     -25.842   3.923 -22.139  1.00 56.09           N  
ANISOU  121  N   TRP A  27     6214   7421   7677    115    162  -1120       N  
ATOM    122  CA  TRP A  27     -26.716   3.537 -21.017  1.00 58.13           C  
ANISOU  122  CA  TRP A  27     6479   7613   7994    110    205  -1099       C  
ATOM    123  C   TRP A  27     -28.030   3.038 -21.627  1.00 56.91           C  
ANISOU  123  C   TRP A  27     6278   7450   7895     83    224  -1198       C  
ATOM    124  O   TRP A  27     -28.221   3.081 -22.859  1.00 55.88           O  
ANISOU  124  O   TRP A  27     6110   7373   7746     72    198  -1278       O  
ATOM    125  CB  TRP A  27     -26.991   4.767 -20.111  1.00 54.31           C  
ANISOU  125  CB  TRP A  27     6036   7152   7446    118    169  -1030       C  
ATOM    126  CG  TRP A  27     -27.318   5.968 -20.932  1.00 52.16           C  
ANISOU  126  CG  TRP A  27     5761   6960   7097    113    107  -1056       C  
ATOM    127  CD1 TRP A  27     -26.424   6.820 -21.513  1.00 56.54           C  
ANISOU  127  CD1 TRP A  27     6330   7575   7577    124     61  -1034       C  
ATOM    128  CD2 TRP A  27     -28.592   6.400 -21.361  1.00 49.37           C  
ANISOU  128  CD2 TRP A  27     5385   6635   6736     99     90  -1110       C  
ATOM    129  CE2 TRP A  27     -28.405   7.547 -22.180  1.00 51.08           C  
ANISOU  129  CE2 TRP A  27     5606   6932   6867    107     34  -1111       C  
ATOM    130  CE3 TRP A  27     -29.879   5.970 -21.108  1.00 52.16           C  
ANISOU  130  CE3 TRP A  27     5714   6955   7146     81    118  -1154       C  
ATOM    131  NE1 TRP A  27     -27.076   7.785 -22.266  1.00 53.47           N  
ANISOU  131  NE1 TRP A  27     5933   7250   7133    122     20  -1065       N  
ATOM    132  CZ2 TRP A  27     -29.442   8.241 -22.738  1.00 54.36           C  
ANISOU  132  CZ2 TRP A  27     6004   7400   7250    105      6  -1151       C  
ATOM    133  CZ3 TRP A  27     -30.917   6.691 -21.648  1.00 52.97           C  
ANISOU  133  CZ3 TRP A  27     5798   7112   7215     74     84  -1198       C  
ATOM    134  CH2 TRP A  27     -30.688   7.808 -22.452  1.00 54.22           C  
ANISOU  134  CH2 TRP A  27     5961   7353   7284     88     29  -1194       C  
ATOM    135  N   ASP A  28     -28.956   2.595 -20.798  1.00 54.87           N  
ANISOU  135  N   ASP A  28     6015   7129   7702     73    270  -1197       N  
ATOM    136  CA  ASP A  28     -30.279   2.328 -21.343  1.00 59.33           C  
ANISOU  136  CA  ASP A  28     6534   7697   8313     45    280  -1293       C  
ATOM    137  C   ASP A  28     -31.399   2.744 -20.415  1.00 62.90           C  
ANISOU  137  C   ASP A  28     6998   8124   8777     40    288  -1268       C  
ATOM    138  O   ASP A  28     -31.188   3.017 -19.215  1.00 49.42           O  
ANISOU  138  O   ASP A  28     5336   6381   7061     57    301  -1175       O  
ATOM    139  CB  ASP A  28     -30.462   0.847 -21.730  1.00 66.30           C  
ANISOU  139  CB  ASP A  28     7368   8515   9306     26    350  -1372       C  
ATOM    140  CG  ASP A  28     -30.768  -0.010 -20.552  1.00 66.07           C  
ANISOU  140  CG  ASP A  28     7349   8380   9372     27    431  -1331       C  
ATOM    141  OD1 ASP A  28     -29.808  -0.395 -19.894  1.00 84.43           O  
ANISOU  141  OD1 ASP A  28     9707  10662  11708     53    463  -1253       O  
ATOM    142  OD2 ASP A  28     -31.939  -0.260 -20.237  1.00 64.70           O1-
ANISOU  142  OD2 ASP A  28     7153   8169   9259      7    464  -1370       O1-
ATOM    143  N   GLU A  29     -32.606   2.680 -20.986  1.00 61.64           N  
ANISOU  143  N   GLU A  29     6793   7983   8645     15    286  -1357       N  
ATOM    144  CA  GLU A  29     -33.733   3.315 -20.413  1.00 63.98           C  
ANISOU  144  CA  GLU A  29     7094   8282   8933      9    276  -1347       C  
ATOM    145  C   GLU A  29     -34.014   2.733 -19.050  1.00 59.92           C  
ANISOU  145  C   GLU A  29     6603   7669   8493     11    344  -1288       C  
ATOM    146  O   GLU A  29     -34.375   3.456 -18.159  1.00 54.63           O  
ANISOU  146  O   GLU A  29     5969   6996   7791     22    332  -1224       O  
ATOM    147  CB  GLU A  29     -34.924   3.232 -21.317  1.00 74.69           C  
ANISOU  147  CB  GLU A  29     8388   9679  10309    -15    265  -1460       C  
ATOM    148  CG  GLU A  29     -35.742   4.502 -21.201  1.00 89.38           C  
ANISOU  148  CG  GLU A  29    10262  11601  12097     -9    212  -1440       C  
ATOM    149  CD  GLU A  29     -37.213   4.237 -21.329  1.00101.66           C  
ANISOU  149  CD  GLU A  29    11764  13153  13707    -33    229  -1523       C  
ATOM    150  OE1 GLU A  29     -37.549   3.145 -21.833  1.00114.51           O  
ANISOU  150  OE1 GLU A  29    13336  14753  15418    -58    271  -1618       O  
ATOM    151  OE2 GLU A  29     -38.011   5.104 -20.907  1.00108.71           O1-
ANISOU  151  OE2 GLU A  29    12671  14069  14563    -28    205  -1495       O1-
ATOM    152  N   SER A  30     -33.742   1.460 -18.838  1.00 54.86           N  
ANISOU  152  N   SER A  30     5947   6948   7947      8    417  -1301       N  
ATOM    153  CA  SER A  30     -33.943   0.867 -17.496  1.00 55.90           C  
ANISOU  153  CA  SER A  30     6103   6984   8150     20    491  -1232       C  
ATOM    154  C   SER A  30     -33.156   1.511 -16.347  1.00 52.18           C  
ANISOU  154  C   SER A  30     5699   6515   7612     59    475  -1103       C  
ATOM    155  O   SER A  30     -33.477   1.306 -15.199  1.00 49.29           O  
ANISOU  155  O   SER A  30     5356   6091   7280     75    522  -1041       O  
ATOM    156  CB  SER A  30     -33.630  -0.634 -17.515  1.00 51.37           C  
ANISOU  156  CB  SER A  30     5503   6322   7691     16    581  -1259       C  
ATOM    157  OG  SER A  30     -32.238  -0.834 -17.574  1.00 52.22           O  
ANISOU  157  OG  SER A  30     5637   6437   7767     43    577  -1205       O  
ATOM    158  N   GLN A  31     -32.110   2.251 -16.670  1.00 49.61           N  
ANISOU  158  N   GLN A  31     5399   6256   7193     75    413  -1067       N  
ATOM    159  CA  GLN A  31     -31.306   2.960 -15.662  1.00 54.69           C  
ANISOU  159  CA  GLN A  31     6099   6916   7765    108    389   -958       C  
ATOM    160  C   GLN A  31     -31.877   4.320 -15.135  1.00 50.43           C  
ANISOU  160  C   GLN A  31     5589   6422   7148    109    336   -922       C  
ATOM    161  O   GLN A  31     -31.242   4.968 -14.307  1.00 48.18           O  
ANISOU  161  O   GLN A  31     5346   6155   6802    134    314   -842       O  
ATOM    162  CB  GLN A  31     -29.902   3.191 -16.250  1.00 49.98           C  
ANISOU  162  CB  GLN A  31     5513   6370   7107    122    348   -940       C  
ATOM    163  CG  GLN A  31     -29.225   1.911 -16.666  1.00 55.74           C  
ANISOU  163  CG  GLN A  31     6218   7053   7905    126    401   -963       C  
ATOM    164  CD  GLN A  31     -27.868   2.173 -17.222  1.00 53.57           C  
ANISOU  164  CD  GLN A  31     5954   6830   7570    140    360   -944       C  
ATOM    165  NE2 GLN A  31     -26.912   2.303 -16.332  1.00 47.79           N  
ANISOU  165  NE2 GLN A  31     5258   6097   6803    174    361   -853       N  
ATOM    166  OE1 GLN A  31     -27.687   2.322 -18.434  1.00 53.26           O  
ANISOU  166  OE1 GLN A  31     5890   6838   7509    123    324  -1009       O  
ATOM    167  N   LEU A  32     -33.047   4.722 -15.642  1.00 50.08           N  
ANISOU  167  N   LEU A  32     5519   6399   7108     83    316   -985       N  
ATOM    168  CA  LEU A  32     -33.655   6.023 -15.394  1.00 49.84           C  
ANISOU  168  CA  LEU A  32     5510   6417   7007     81    266   -965       C  
ATOM    169  C   LEU A  32     -34.815   5.824 -14.453  1.00 51.37           C  
ANISOU  169  C   LEU A  32     5707   6556   7255     77    310   -953       C  
ATOM    170  O   LEU A  32     -35.619   4.968 -14.695  1.00 56.92           O  
ANISOU  170  O   LEU A  32     6371   7215   8042     58    356  -1013       O  
ATOM    171  CB  LEU A  32     -34.195   6.564 -16.703  1.00 48.07           C  
ANISOU  171  CB  LEU A  32     5251   6262   6751     61    217  -1045       C  
ATOM    172  CG  LEU A  32     -33.170   6.801 -17.804  1.00 54.63           C  
ANISOU  172  CG  LEU A  32     6074   7154   7527     66    174  -1066       C  
ATOM    173  CD1 LEU A  32     -33.731   7.542 -19.005  1.00 58.77           C  
ANISOU  173  CD1 LEU A  32     6570   7759   8001     58    122  -1129       C  
ATOM    174  CD2 LEU A  32     -31.964   7.562 -17.290  1.00 57.85           C  
ANISOU  174  CD2 LEU A  32     6531   7583   7863     89    144   -980       C  
ATOM    175  N   ARG A  33     -34.903   6.590 -13.376  1.00 51.65           N  
ANISOU  175  N   ARG A  33     5786   6592   7246     94    300   -878       N  
ATOM    176  CA  ARG A  33     -36.081   6.530 -12.528  1.00 49.05           C  
ANISOU  176  CA  ARG A  33     5458   6216   6960     91    337   -868       C  
ATOM    177  C   ARG A  33     -37.356   6.974 -13.287  1.00 47.66           C  
ANISOU  177  C   ARG A  33     5246   6071   6790     62    313   -945       C  
ATOM    178  O   ARG A  33     -37.321   7.562 -14.382  1.00 45.76           O  
ANISOU  178  O   ARG A  33     4986   5900   6501     51    258   -994       O  
ATOM    179  CB  ARG A  33     -35.854   7.303 -11.271  1.00 46.87           C  
ANISOU  179  CB  ARG A  33     5236   5945   6627    117    327   -777       C  
ATOM    180  CG  ARG A  33     -34.753   6.694 -10.478  1.00 48.96           C  
ANISOU  180  CG  ARG A  33     5526   6181   6894    150    360   -707       C  
ATOM    181  CD  ARG A  33     -34.312   7.631  -9.391  1.00 49.49           C  
ANISOU  181  CD  ARG A  33     5641   6279   6882    176    332   -628       C  
ATOM    182  NE  ARG A  33     -33.239   7.072  -8.599  1.00 48.22           N  
ANISOU  182  NE  ARG A  33     5501   6104   6715    215    360   -560       N  
ATOM    183  CZ  ARG A  33     -33.375   6.206  -7.586  1.00 50.49           C  
ANISOU  183  CZ  ARG A  33     5797   6333   7051    247    429   -509       C  
ATOM    184  NH1 ARG A  33     -34.545   5.778  -7.219  1.00 48.35           N1+
ANISOU  184  NH1 ARG A  33     5518   6005   6848    241    481   -518       N1+
ATOM    185  NH2 ARG A  33     -32.307   5.778  -6.901  1.00 47.03           N  
ANISOU  185  NH2 ARG A  33     5377   5898   6593    290    448   -443       N  
ATOM    186  N   SER A  34     -38.514   6.613 -12.775  1.00 50.12           N  
ANISOU  186  N   SER A  34     5543   6333   7166     51    357   -960       N  
ATOM    187  CA  SER A  34     -39.740   7.008 -13.515  1.00 50.07           C  
ANISOU  187  CA  SER A  34     5495   6363   7166     26    333  -1038       C  
ATOM    188  C   SER A  34     -40.590   7.961 -12.688  1.00 46.55           C  
ANISOU  188  C   SER A  34     5077   5921   6685     32    321   -994       C  
ATOM    189  O   SER A  34     -40.726   7.840 -11.478  1.00 45.40           O  
ANISOU  189  O   SER A  34     4965   5722   6562     46    361   -929       O  
ATOM    190  CB  SER A  34     -40.551   5.813 -13.972  1.00 62.38           C  
ANISOU  190  CB  SER A  34     6992   7873   8835      0    389  -1128       C  
ATOM    191  OG  SER A  34     -40.913   5.107 -12.828  1.00 66.37           O  
ANISOU  191  OG  SER A  34     7511   8287   9417      5    465  -1085       O  
ATOM    192  N   TYR A  35     -41.095   8.958 -13.378  1.00 44.65           N  
ANISOU  192  N   TYR A  35     4825   5753   6385     25    264  -1025       N  
ATOM    193  CA  TYR A  35     -41.689  10.109 -12.757  1.00 48.61           C  
ANISOU  193  CA  TYR A  35     5360   6276   6834     33    240   -978       C  
ATOM    194  C   TYR A  35     -43.024  10.295 -13.420  1.00 49.21           C  
ANISOU  194  C   TYR A  35     5386   6382   6928     16    229  -1052       C  
ATOM    195  O   TYR A  35     -43.316   9.621 -14.373  1.00 47.38           O  
ANISOU  195  O   TYR A  35     5098   6166   6737      0    233  -1137       O  
ATOM    196  CB  TYR A  35     -40.769  11.358 -12.889  1.00 42.22           C  
ANISOU  196  CB  TYR A  35     4593   5530   5917     51    180   -926       C  
ATOM    197  CG  TYR A  35     -39.518  11.167 -12.052  1.00 38.99           C  
ANISOU  197  CG  TYR A  35     4229   5091   5492     69    193   -854       C  
ATOM    198  CD1 TYR A  35     -39.619  10.952 -10.720  1.00 37.98           C  
ANISOU  198  CD1 TYR A  35     4134   4908   5387     81    233   -794       C  
ATOM    199  CD2 TYR A  35     -38.227  11.115 -12.634  1.00 41.52           C  
ANISOU  199  CD2 TYR A  35     4555   5442   5777     75    167   -849       C  
ATOM    200  CE1 TYR A  35     -38.484  10.730  -9.927  1.00 40.58           C  
ANISOU  200  CE1 TYR A  35     4500   5221   5698    104    245   -729       C  
ATOM    201  CE2 TYR A  35     -37.059  10.867 -11.845  1.00 43.76           C  
ANISOU  201  CE2 TYR A  35     4875   5703   6048     94    180   -786       C  
ATOM    202  CZ  TYR A  35     -37.213  10.679 -10.496  1.00 41.22           C  
ANISOU  202  CZ  TYR A  35     4583   5334   5744    110    218   -726       C  
ATOM    203  OH  TYR A  35     -36.178  10.459  -9.650  1.00 44.47           O  
ANISOU  203  OH  TYR A  35     5025   5732   6137    135    230   -663       O  
ATOM    204  N   SER A  36     -43.791  11.245 -12.910  1.00 47.76           N  
ANISOU  204  N   SER A  36     5223   6212   6710     22    215  -1020       N  
ATOM    205  CA  SER A  36     -45.193  11.419 -13.217  1.00 47.96           C  
ANISOU  205  CA  SER A  36     5205   6256   6759     10    215  -1075       C  
ATOM    206  C   SER A  36     -45.392  12.432 -14.296  1.00 47.83           C  
ANISOU  206  C   SER A  36     5171   6338   6664     19    152  -1105       C  
ATOM    207  O   SER A  36     -46.493  12.646 -14.711  1.00 56.19           O  
ANISOU  207  O   SER A  36     6189   7431   7730     14    143  -1154       O  
ATOM    208  CB  SER A  36     -45.900  11.896 -11.939  1.00 51.27           C  
ANISOU  208  CB  SER A  36     5663   6631   7186     16    240  -1013       C  
ATOM    209  OG  SER A  36     -45.534  13.216 -11.573  1.00 46.48           O  
ANISOU  209  OG  SER A  36     5109   6062   6487     35    200   -943       O  
ATOM    210  N   PHE A  37     -44.353  13.082 -14.783  1.00 43.11           N  
ANISOU  210  N   PHE A  37     4599   5789   5989     35    110  -1074       N  
ATOM    211  CA  PHE A  37     -44.551  14.242 -15.653  1.00 41.36           C  
ANISOU  211  CA  PHE A  37     4371   5657   5685     54     58  -1079       C  
ATOM    212  C   PHE A  37     -43.892  13.918 -16.933  1.00 41.68           C  
ANISOU  212  C   PHE A  37     4378   5755   5703     58     31  -1132       C  
ATOM    213  O   PHE A  37     -43.101  13.038 -16.966  1.00 42.72           O  
ANISOU  213  O   PHE A  37     4507   5853   5869     48     48  -1144       O  
ATOM    214  CB  PHE A  37     -43.965  15.521 -15.074  1.00 41.34           C  
ANISOU  214  CB  PHE A  37     4435   5664   5608     72     38   -990       C  
ATOM    215  CG  PHE A  37     -42.515  15.347 -14.582  1.00 39.14           C  
ANISOU  215  CG  PHE A  37     4201   5351   5317     74     42   -937       C  
ATOM    216  CD1 PHE A  37     -41.478  15.343 -15.470  1.00 39.33           C  
ANISOU  216  CD1 PHE A  37     4220   5415   5305     81     16   -948       C  
ATOM    217  CD2 PHE A  37     -42.240  15.099 -13.236  1.00 39.28           C  
ANISOU  217  CD2 PHE A  37     4262   5300   5363     70     75   -881       C  
ATOM    218  CE1 PHE A  37     -40.158  15.150 -15.049  1.00 37.73           C  
ANISOU  218  CE1 PHE A  37     4054   5187   5094     83     20   -904       C  
ATOM    219  CE2 PHE A  37     -40.926  14.881 -12.809  1.00 38.94           C  
ANISOU  219  CE2 PHE A  37     4251   5235   5305     75     78   -838       C  
ATOM    220  CZ  PHE A  37     -39.905  14.871 -13.724  1.00 36.92           C  
ANISOU  220  CZ  PHE A  37     3988   5020   5018     80     50   -852       C  
ATOM    221  N   PRO A  38     -44.261  14.588 -18.015  1.00 43.34           N  
ANISOU  221  N   PRO A  38     4556   6055   5853     77     -8  -1166       N  
ATOM    222  CA  PRO A  38     -43.561  14.363 -19.266  1.00 48.64           C  
ANISOU  222  CA  PRO A  38     5198   6790   6491     87    -35  -1211       C  
ATOM    223  C   PRO A  38     -42.382  15.292 -19.458  1.00 49.51           C  
ANISOU  223  C   PRO A  38     5359   6928   6524    111    -61  -1141       C  
ATOM    224  O   PRO A  38     -42.301  16.306 -18.782  1.00 46.11           O  
ANISOU  224  O   PRO A  38     4978   6485   6056    121    -64  -1067       O  
ATOM    225  CB  PRO A  38     -44.602  14.752 -20.297  1.00 50.69           C  
ANISOU  225  CB  PRO A  38     5400   7144   6716    106    -64  -1274       C  
ATOM    226  CG  PRO A  38     -45.354  15.868 -19.622  1.00 51.05           C  
ANISOU  226  CG  PRO A  38     5476   7188   6729    120    -66  -1213       C  
ATOM    227  CD  PRO A  38     -45.463  15.390 -18.199  1.00 48.12           C  
ANISOU  227  CD  PRO A  38     5142   6711   6430     91    -23  -1176       C  
ATOM    228  N   THR A  39     -41.542  14.978 -20.445  1.00 42.63           N  
ANISOU  228  N   THR A  39     4469   6099   5629    119    -79  -1172       N  
ATOM    229  CA  THR A  39     -40.330  15.739 -20.761  1.00 46.00           C  
ANISOU  229  CA  THR A  39     4936   6551   5989    140   -100  -1114       C  
ATOM    230  C   THR A  39     -40.030  15.678 -22.220  1.00 47.87           C  
ANISOU  230  C   THR A  39     5132   6874   6181    163   -128  -1165       C  
ATOM    231  O   THR A  39     -40.470  14.783 -22.905  1.00 43.35           O  
ANISOU  231  O   THR A  39     4501   6328   5639    155   -128  -1250       O  
ATOM    232  CB  THR A  39     -39.091  15.144 -20.098  1.00 44.73           C  
ANISOU  232  CB  THR A  39     4812   6322   5859    123    -81  -1078       C  
ATOM    233  CG2 THR A  39     -39.286  15.070 -18.571  1.00 44.16           C  
ANISOU  233  CG2 THR A  39     4780   6166   5830    105    -50  -1026       C  
ATOM    234  OG1 THR A  39     -38.892  13.834 -20.624  1.00 44.03           O  
ANISOU  234  OG1 THR A  39     4680   6224   5824    108    -68  -1148       O  
ATOM    235  N   ARG A  40     -39.314  16.682 -22.667  1.00 46.36           N  
ANISOU  235  N   ARG A  40     4970   6725   5918    192   -147  -1113       N  
ATOM    236  CA  ARG A  40     -38.853  16.805 -24.008  1.00 53.44           C  
ANISOU  236  CA  ARG A  40     5839   7704   6760    221   -170  -1141       C  
ATOM    237  C   ARG A  40     -37.274  16.901 -23.943  1.00 46.99           C  
ANISOU  237  C   ARG A  40     5066   6858   5929    220   -168  -1089       C  
ATOM    238  O   ARG A  40     -36.751  17.212 -22.916  1.00 43.57           O  
ANISOU  238  O   ARG A  40     4682   6360   5510    204   -153  -1027       O  
ATOM    239  CB  ARG A  40     -39.472  18.081 -24.572  1.00 66.49           C  
ANISOU  239  CB  ARG A  40     7490   9434   8338    265   -187  -1111       C  
ATOM    240  CG  ARG A  40     -39.496  18.077 -26.096  1.00107.70           C  
ANISOU  240  CG  ARG A  40    12659  14762  13499    306   -212  -1161       C  
ATOM    241  CD  ARG A  40     -40.526  18.970 -26.796  1.00131.79           C  
ANISOU  241  CD  ARG A  40    15681  17908  16484    356   -228  -1162       C  
ATOM    242  NE  ARG A  40     -40.228  20.393 -26.627  1.00138.40           N  
ANISOU  242  NE  ARG A  40    16570  18746  17266    388   -219  -1063       N  
ATOM    243  CZ  ARG A  40     -39.291  21.063 -27.291  1.00129.72           C  
ANISOU  243  CZ  ARG A  40    15494  17680  16112    423   -218  -1015       C  
ATOM    244  NH1 ARG A  40     -39.121  22.352 -27.030  1.00120.73           N1+
ANISOU  244  NH1 ARG A  40    14401  16529  14939    448   -199   -929       N1+
ATOM    245  NH2 ARG A  40     -38.530  20.459 -28.202  1.00129.67           N  
ANISOU  245  NH2 ARG A  40    15464  17714  16089    433   -230  -1054       N  
ATOM    246  N   PRO A  41     -36.551  16.639 -25.036  1.00 49.66           N  
ANISOU  246  N   PRO A  41     5382   7248   6237    237   -181  -1118       N  
ATOM    247  CA  PRO A  41     -35.068  16.674 -24.979  1.00 45.62           C  
ANISOU  247  CA  PRO A  41     4908   6708   5718    235   -177  -1073       C  
ATOM    248  C   PRO A  41     -34.463  18.030 -24.931  1.00 46.00           C  
ANISOU  248  C   PRO A  41     5000   6766   5708    258   -179   -992       C  
ATOM    249  O   PRO A  41     -34.923  18.939 -25.607  1.00 43.49           O  
ANISOU  249  O   PRO A  41     4676   6513   5335    294   -188   -978       O  
ATOM    250  CB  PRO A  41     -34.605  15.980 -26.291  1.00 46.64           C  
ANISOU  250  CB  PRO A  41     4993   6897   5830    250   -190  -1136       C  
ATOM    251  CG  PRO A  41     -35.800  15.990 -27.200  1.00 52.62           C  
ANISOU  251  CG  PRO A  41     5694   7739   6558    274   -208  -1202       C  
ATOM    252  CD  PRO A  41     -37.044  16.075 -26.321  1.00 48.28           C  
ANISOU  252  CD  PRO A  41     5142   7156   6045    256   -199  -1205       C  
ATOM    253  N   ILE A  42     -33.396  18.162 -24.143  1.00 41.25           N  
ANISOU  253  N   ILE A  42     4443   6105   5123    239   -167   -940       N  
ATOM    254  CA  ILE A  42     -32.548  19.329 -24.267  1.00 38.21           C  
ANISOU  254  CA  ILE A  42     4094   5731   4691    257   -165   -875       C  
ATOM    255  C   ILE A  42     -31.674  19.106 -25.503  1.00 38.64           C  
ANISOU  255  C   ILE A  42     4129   5837   4715    280   -174   -894       C  
ATOM    256  O   ILE A  42     -31.135  17.984 -25.678  1.00 42.23           O  
ANISOU  256  O   ILE A  42     4565   6279   5202    264   -176   -935       O  
ATOM    257  CB  ILE A  42     -31.656  19.466 -23.045  1.00 38.71           C  
ANISOU  257  CB  ILE A  42     4202   5722   4783    227   -152   -826       C  
ATOM    258  CG1 ILE A  42     -32.510  19.796 -21.820  1.00 37.14           C  
ANISOU  258  CG1 ILE A  42     4026   5478   4607    210   -142   -803       C  
ATOM    259  CG2 ILE A  42     -30.583  20.523 -23.334  1.00 38.85           C  
ANISOU  259  CG2 ILE A  42     4247   5751   4760    242   -147   -774       C  
ATOM    260  CD1 ILE A  42     -31.856  19.522 -20.505  1.00 34.67           C  
ANISOU  260  CD1 ILE A  42     3744   5098   4328    180   -131   -774       C  
ATOM    261  N   PRO A  43     -31.506  20.156 -26.325  1.00 36.27           N  
ANISOU  261  N   PRO A  43     3834   5591   4355    319   -173   -861       N  
ATOM    262  CA  PRO A  43     -30.675  20.063 -27.500  1.00 43.20           C  
ANISOU  262  CA  PRO A  43     4696   6520   5198    347   -177   -871       C  
ATOM    263  C   PRO A  43     -29.229  19.747 -27.156  1.00 46.88           C  
ANISOU  263  C   PRO A  43     5185   6936   5689    322   -170   -849       C  
ATOM    264  O   PRO A  43     -28.633  20.341 -26.242  1.00 41.80           O  
ANISOU  264  O   PRO A  43     4581   6239   5060    302   -157   -797       O  
ATOM    265  CB  PRO A  43     -30.731  21.461 -28.118  1.00 42.42           C  
ANISOU  265  CB  PRO A  43     4611   6467   5037    394   -165   -816       C  
ATOM    266  CG  PRO A  43     -31.878  22.157 -27.472  1.00 44.56           C  
ANISOU  266  CG  PRO A  43     4893   6728   5308    395   -159   -794       C  
ATOM    267  CD  PRO A  43     -32.138  21.489 -26.173  1.00 38.61           C  
ANISOU  267  CD  PRO A  43     4151   5900   4617    342   -161   -810       C  
ATOM    268  N   ARG A  44     -28.651  18.853 -27.931  1.00 44.10           N  
ANISOU  268  N   ARG A  44     4807   6609   5339    327   -178   -892       N  
ATOM    269  CA  ARG A  44     -27.276  18.446 -27.730  1.00 50.38           C  
ANISOU  269  CA  ARG A  44     5619   7366   6158    308   -172   -876       C  
ATOM    270  C   ARG A  44     -26.510  18.901 -28.981  1.00 51.84           C  
ANISOU  270  C   ARG A  44     5796   7608   6291    346   -170   -864       C  
ATOM    271  O   ARG A  44     -26.781  18.432 -30.088  1.00 45.19           O  
ANISOU  271  O   ARG A  44     4917   6830   5422    374   -181   -912       O  
ATOM    272  CB  ARG A  44     -27.293  16.948 -27.413  1.00 50.91           C  
ANISOU  272  CB  ARG A  44     5663   7398   6281    278   -176   -933       C  
ATOM    273  CG  ARG A  44     -25.989  16.264 -27.516  1.00 62.69           C  
ANISOU  273  CG  ARG A  44     7157   8867   7794    268   -171   -933       C  
ATOM    274  CD  ARG A  44     -26.099  14.738 -27.337  1.00 62.36           C  
ANISOU  274  CD  ARG A  44     7088   8793   7811    244   -166   -991       C  
ATOM    275  NE  ARG A  44     -24.724  14.179 -27.329  1.00 65.29           N  
ANISOU  275  NE  ARG A  44     7467   9138   8201    237   -158   -978       N  
ATOM    276  CZ  ARG A  44     -23.967  14.077 -26.214  1.00 66.62           C  
ANISOU  276  CZ  ARG A  44     7664   9247   8400    217   -147   -932       C  
ATOM    277  NH1 ARG A  44     -24.471  14.434 -24.987  1.00 52.13           N1+
ANISOU  277  NH1 ARG A  44     5854   7371   6582    201   -143   -899       N1+
ATOM    278  NH2 ARG A  44     -22.725  13.570 -26.289  1.00 59.23           N  
ANISOU  278  NH2 ARG A  44     6730   8296   7477    215   -141   -922       N  
ATOM    279  N   LEU A  45     -25.600  19.866 -28.806  1.00 44.24           N  
ANISOU  279  N   LEU A  45     4867   6626   5316    350   -153   -801       N  
ATOM    280  CA  LEU A  45     -25.012  20.576 -29.920  1.00 40.76           C  
ANISOU  280  CA  LEU A  45     4424   6235   4825    393   -140   -774       C  
ATOM    281  C   LEU A  45     -23.508  20.741 -29.810  1.00 45.79           C  
ANISOU  281  C   LEU A  45     5082   6838   5476    379   -125   -740       C  
ATOM    282  O   LEU A  45     -22.900  20.602 -28.734  1.00 39.69           O  
ANISOU  282  O   LEU A  45     4330   6003   4747    338   -123   -726       O  
ATOM    283  CB  LEU A  45     -25.583  21.955 -30.047  1.00 40.85           C  
ANISOU  283  CB  LEU A  45     4453   6268   4799    424   -121   -724       C  
ATOM    284  CG  LEU A  45     -27.108  22.067 -30.252  1.00 46.41           C  
ANISOU  284  CG  LEU A  45     5136   7017   5477    448   -132   -746       C  
ATOM    285  CD1 LEU A  45     -27.571  23.526 -30.173  1.00 43.26           C  
ANISOU  285  CD1 LEU A  45     4763   6624   5050    478   -105   -682       C  
ATOM    286  CD2 LEU A  45     -27.442  21.458 -31.611  1.00 49.34           C  
ANISOU  286  CD2 LEU A  45     5462   7480   5804    492   -150   -798       C  
ATOM    287  N   SER A  46     -22.936  21.145 -30.935  1.00 44.12           N  
ANISOU  287  N   SER A  46     4863   6673   5225    419   -112   -724       N  
ATOM    288  CA  SER A  46     -21.567  21.529 -30.931  1.00 45.39           C  
ANISOU  288  CA  SER A  46     5043   6806   5397    411    -91   -686       C  
ATOM    289  C   SER A  46     -21.460  22.933 -30.466  1.00 43.67           C  
ANISOU  289  C   SER A  46     4855   6558   5178    412    -60   -625       C  
ATOM    290  O   SER A  46     -22.244  23.812 -30.824  1.00 40.13           O  
ANISOU  290  O   SER A  46     4411   6137   4697    446    -43   -599       O  
ATOM    291  CB  SER A  46     -20.885  21.432 -32.319  1.00 42.94           C  
ANISOU  291  CB  SER A  46     4714   6551   5048    455    -82   -689       C  
ATOM    292  OG  SER A  46     -19.592  22.135 -32.239  1.00 42.33           O  
ANISOU  292  OG  SER A  46     4658   6439   4983    448    -52   -639       O  
ATOM    293  N   GLN A  47     -20.408  23.125 -29.701  1.00 44.29           N  
ANISOU  293  N   GLN A  47     4951   6579   5295    374    -49   -605       N  
ATOM    294  CA  GLN A  47     -19.859  24.379 -29.294  1.00 45.18           C  
ANISOU  294  CA  GLN A  47     5089   6656   5420    365    -12   -555       C  
ATOM    295  C   GLN A  47     -19.766  25.379 -30.431  1.00 45.06           C  
ANISOU  295  C   GLN A  47     5076   6676   5368    417     27   -514       C  
ATOM    296  O   GLN A  47     -20.025  26.537 -30.239  1.00 46.09           O  
ANISOU  296  O   GLN A  47     5224   6788   5497    427     64   -472       O  
ATOM    297  CB  GLN A  47     -18.487  24.060 -28.722  1.00 55.88           C  
ANISOU  297  CB  GLN A  47     6444   7974   6813    326    -17   -562       C  
ATOM    298  CG  GLN A  47     -17.589  25.210 -28.434  1.00 58.16           C  
ANISOU  298  CG  GLN A  47     6745   8225   7125    307     16   -530       C  
ATOM    299  CD  GLN A  47     -16.896  25.687 -29.652  1.00 56.34           C  
ANISOU  299  CD  GLN A  47     6513   8019   6875    347     55   -499       C  
ATOM    300  NE2 GLN A  47     -16.825  26.980 -29.805  1.00 52.15           N  
ANISOU  300  NE2 GLN A  47     5998   7468   6347    356    101   -458       N  
ATOM    301  OE1 GLN A  47     -16.439  24.904 -30.451  1.00 57.27           O  
ANISOU  301  OE1 GLN A  47     6615   8170   6976    370     49   -510       O  
ATOM    302  N   SER A  48     -19.425  24.918 -31.625  1.00 49.13           N  
ANISOU  302  N   SER A  48     5571   7244   5850    457     25   -524       N  
ATOM    303  CA  SER A  48     -19.332  25.823 -32.826  1.00 50.75           C  
ANISOU  303  CA  SER A  48     5777   7493   6013    519     68   -478       C  
ATOM    304  C   SER A  48     -20.655  26.223 -33.422  1.00 55.10           C  
ANISOU  304  C   SER A  48     6321   8102   6512    573     71   -468       C  
ATOM    305  O   SER A  48     -20.701  27.065 -34.333  1.00 48.67           O  
ANISOU  305  O   SER A  48     5508   7325   5658    632    111   -421       O  
ATOM    306  CB  SER A  48     -18.533  25.148 -33.937  1.00 51.13           C  
ANISOU  306  CB  SER A  48     5804   7585   6036    548     64   -494       C  
ATOM    307  OG  SER A  48     -19.115  23.865 -34.208  1.00 51.59           O  
ANISOU  307  OG  SER A  48     5836   7688   6077    549     14   -557       O  
ATOM    308  N   ASP A  49     -21.741  25.607 -32.942  1.00 55.73           N  
ANISOU  308  N   ASP A  49     6390   8193   6589    557     30   -510       N  
ATOM    309  CA  ASP A  49     -23.055  25.768 -33.581  1.00 50.59           C  
ANISOU  309  CA  ASP A  49     5722   7613   5885    610     22   -514       C  
ATOM    310  C   ASP A  49     -23.732  27.039 -33.127  1.00 53.10           C  
ANISOU  310  C   ASP A  49     6065   7908   6203    623     58   -459       C  
ATOM    311  O   ASP A  49     -24.022  27.181 -31.949  1.00 51.64           O  
ANISOU  311  O   ASP A  49     5897   7661   6060    573     53   -462       O  
ATOM    312  CB  ASP A  49     -23.897  24.539 -33.229  1.00 49.27           C  
ANISOU  312  CB  ASP A  49     5530   7463   5727    581    -31   -588       C  
ATOM    313  CG  ASP A  49     -25.182  24.476 -34.013  1.00 52.98           C  
ANISOU  313  CG  ASP A  49     5969   8019   6140    635    -47   -612       C  
ATOM    314  OD1 ASP A  49     -25.629  25.542 -34.425  1.00 48.85           O  
ANISOU  314  OD1 ASP A  49     5453   7528   5577    685    -17   -560       O  
ATOM    315  OD2 ASP A  49     -25.750  23.371 -34.150  1.00 53.01           O1-
ANISOU  315  OD2 ASP A  49     5940   8057   6143    624    -88   -684       O1-
ATOM    316  N   PRO A  50     -24.036  27.962 -34.056  1.00 54.54           N  
ANISOU  316  N   PRO A  50     6246   8139   6334    694     98   -408       N  
ATOM    317  CA  PRO A  50     -24.737  29.188 -33.708  1.00 54.31           C  
ANISOU  317  CA  PRO A  50     6239   8090   6305    714    139   -352       C  
ATOM    318  C   PRO A  50     -25.994  28.995 -32.857  1.00 53.42           C  
ANISOU  318  C   PRO A  50     6124   7970   6202    688    106   -381       C  
ATOM    319  O   PRO A  50     -26.307  29.864 -32.055  1.00 55.01           O  
ANISOU  319  O   PRO A  50     6353   8116   6432    670    136   -345       O  
ATOM    320  CB  PRO A  50     -25.127  29.777 -35.077  1.00 56.94           C  
ANISOU  320  CB  PRO A  50     6557   8512   6564    811    171   -307       C  
ATOM    321  CG  PRO A  50     -24.080  29.236 -36.005  1.00 55.53           C  
ANISOU  321  CG  PRO A  50     6364   8368   6366    831    170   -319       C  
ATOM    322  CD  PRO A  50     -23.809  27.858 -35.501  1.00 54.14           C  
ANISOU  322  CD  PRO A  50     6173   8175   6223    765    107   -400       C  
ATOM    323  N   ARG A  51     -26.686  27.881 -33.002  1.00 50.95           N  
ANISOU  323  N   ARG A  51     5779   7707   5871    684     50   -447       N  
ATOM    324  CA  ARG A  51     -27.890  27.679 -32.236  1.00 51.08           C  
ANISOU  324  CA  ARG A  51     5791   7715   5899    661     23   -475       C  
ATOM    325  C   ARG A  51     -27.522  27.560 -30.815  1.00 53.53           C  
ANISOU  325  C   ARG A  51     6130   7928   6278    583     19   -482       C  
ATOM    326  O   ARG A  51     -28.276  27.989 -29.955  1.00 48.07           O  
ANISOU  326  O   ARG A  51     5454   7203   5607    564     23   -471       O  
ATOM    327  CB  ARG A  51     -28.694  26.459 -32.702  1.00 53.92           C  
ANISOU  327  CB  ARG A  51     6106   8147   6234    669    -30   -553       C  
ATOM    328  CG  ARG A  51     -29.156  26.711 -34.159  1.00 66.50           C  
ANISOU  328  CG  ARG A  51     7666   9856   7744    757    -26   -545       C  
ATOM    329  CD  ARG A  51     -29.635  25.493 -34.944  1.00 63.24           C  
ANISOU  329  CD  ARG A  51     7198   9531   7298    773    -75   -632       C  
ATOM    330  NE  ARG A  51     -28.517  24.565 -35.241  1.00 69.32           N  
ANISOU  330  NE  ARG A  51     7961  10287   8088    745    -90   -671       N  
ATOM    331  CZ  ARG A  51     -28.672  23.255 -35.450  1.00 67.97           C  
ANISOU  331  CZ  ARG A  51     7752  10144   7927    721   -131   -759       C  
ATOM    332  NH1 ARG A  51     -29.866  22.700 -35.408  1.00 70.09           N1+
ANISOU  332  NH1 ARG A  51     7983  10454   8191    718   -163   -822       N1+
ATOM    333  NH2 ARG A  51     -27.634  22.495 -35.707  1.00 73.65           N  
ANISOU  333  NH2 ARG A  51     8468  10847   8666    699   -137   -787       N  
ATOM    334  N   ALA A  52     -26.366  26.954 -30.556  1.00 54.05           N  
ANISOU  334  N   ALA A  52     6200   7955   6379    542      9   -501       N  
ATOM    335  CA  ALA A  52     -25.938  26.769 -29.201  1.00 44.81           C  
ANISOU  335  CA  ALA A  52     5053   6703   5269    473      2   -510       C  
ATOM    336  C   ALA A  52     -25.762  28.110 -28.564  1.00 46.72           C  
ANISOU  336  C   ALA A  52     5329   6890   5531    463     49   -454       C  
ATOM    337  O   ALA A  52     -26.250  28.361 -27.463  1.00 48.96           O  
ANISOU  337  O   ALA A  52     5631   7128   5843    428     47   -453       O  
ATOM    338  CB  ALA A  52     -24.647  26.021 -29.161  1.00 45.11           C  
ANISOU  338  CB  ALA A  52     5088   6717   5332    442     -9   -531       C  
ATOM    339  N   GLU A  53     -25.100  29.000 -29.280  1.00 49.26           N  
ANISOU  339  N   GLU A  53     5659   7218   5839    497     95   -407       N  
ATOM    340  CA  GLU A  53     -24.809  30.318 -28.785  1.00 50.12           C  
ANISOU  340  CA  GLU A  53     5797   7269   5974    488    151   -356       C  
ATOM    341  C   GLU A  53     -26.103  31.086 -28.563  1.00 52.61           C  
ANISOU  341  C   GLU A  53     6123   7590   6276    513    169   -329       C  
ATOM    342  O   GLU A  53     -26.243  31.838 -27.595  1.00 51.00           O  
ANISOU  342  O   GLU A  53     5942   7325   6107    480    195   -312       O  
ATOM    343  CB  GLU A  53     -23.901  31.059 -29.752  1.00 57.44           C  
ANISOU  343  CB  GLU A  53     6727   8204   6892    527    205   -310       C  
ATOM    344  CG  GLU A  53     -23.050  32.109 -29.096  1.00 67.35           C  
ANISOU  344  CG  GLU A  53     8007   9382   8201    492    260   -279       C  
ATOM    345  CD  GLU A  53     -21.765  31.576 -28.397  1.00 68.03           C  
ANISOU  345  CD  GLU A  53     8091   9423   8333    427    240   -316       C  
ATOM    346  OE1 GLU A  53     -21.578  30.367 -28.078  1.00 56.02           O  
ANISOU  346  OE1 GLU A  53     6556   7915   6812    397    181   -364       O  
ATOM    347  OE2 GLU A  53     -20.925  32.432 -28.112  1.00 68.78           O1-
ANISOU  347  OE2 GLU A  53     8197   9466   8468    404    289   -296       O1-
ATOM    348  N   GLU A  54     -27.059  30.855 -29.455  1.00 50.61           N  
ANISOU  348  N   GLU A  54     5848   7413   5968    571    154   -330       N  
ATOM    349  CA  GLU A  54     -28.355  31.463 -29.381  1.00 51.01           C  
ANISOU  349  CA  GLU A  54     5900   7483   5997    603    167   -306       C  
ATOM    350  C   GLU A  54     -29.072  30.990 -28.086  1.00 50.23           C  
ANISOU  350  C   GLU A  54     5809   7343   5934    545    129   -346       C  
ATOM    351  O   GLU A  54     -29.599  31.776 -27.351  1.00 42.85           O  
ANISOU  351  O   GLU A  54     4895   6366   5018    533    155   -320       O  
ATOM    352  CB  GLU A  54     -29.178  31.024 -30.601  1.00 61.89           C  
ANISOU  352  CB  GLU A  54     7242   8967   7306    674    143   -318       C  
ATOM    353  CG  GLU A  54     -30.269  31.973 -31.048  1.00 71.54           C  
ANISOU  353  CG  GLU A  54     8462  10233   8485    742    176   -268       C  
ATOM    354  CD  GLU A  54     -31.264  31.306 -31.987  1.00 74.44           C  
ANISOU  354  CD  GLU A  54     8784  10714   8786    799    134   -303       C  
ATOM    355  OE1 GLU A  54     -32.448  31.675 -31.940  1.00 77.91           O  
ANISOU  355  OE1 GLU A  54     9213  11186   9200    831    134   -291       O  
ATOM    356  OE2 GLU A  54     -30.877  30.392 -32.761  1.00 77.24           O1-
ANISOU  356  OE2 GLU A  54     9108  11126   9112    811     99   -348       O1-
ATOM    357  N   LEU A  55     -29.071  29.697 -27.822  1.00 42.44           N  
ANISOU  357  N   LEU A  55     4802   6365   4956    510     73   -407       N  
ATOM    358  CA  LEU A  55     -29.634  29.191 -26.597  1.00 45.58           C  
ANISOU  358  CA  LEU A  55     5207   6720   5391    458     44   -440       C  
ATOM    359  C   LEU A  55     -29.050  29.821 -25.299  1.00 44.68           C  
ANISOU  359  C   LEU A  55     5129   6520   5327    404     68   -421       C  
ATOM    360  O   LEU A  55     -29.793  30.196 -24.405  1.00 45.62           O  
ANISOU  360  O   LEU A  55     5264   6606   5462    385     73   -415       O  
ATOM    361  CB  LEU A  55     -29.515  27.658 -26.569  1.00 42.11           C  
ANISOU  361  CB  LEU A  55     4741   6295   4961    431     -7   -506       C  
ATOM    362  CG  LEU A  55     -30.430  26.961 -27.589  1.00 45.88           C  
ANISOU  362  CG  LEU A  55     5177   6857   5398    474    -36   -544       C  
ATOM    363  CD1 LEU A  55     -30.043  25.507 -27.773  1.00 41.45           C  
ANISOU  363  CD1 LEU A  55     4588   6307   4852    449    -75   -609       C  
ATOM    364  CD2 LEU A  55     -31.886  27.031 -27.168  1.00 46.46           C  
ANISOU  364  CD2 LEU A  55     5242   6941   5469    478    -46   -556       C  
ATOM    365  N   ILE A  56     -27.732  29.900 -25.178  1.00 43.33           N  
ANISOU  365  N   ILE A  56     4967   6316   5178    378     81   -417       N  
ATOM    366  CA  ILE A  56     -27.095  30.425 -23.960  1.00 43.34           C  
ANISOU  366  CA  ILE A  56     4995   6247   5224    325     99   -411       C  
ATOM    367  C   ILE A  56     -27.471  31.900 -23.792  1.00 48.17           C  
ANISOU  367  C   ILE A  56     5629   6828   5842    338    156   -364       C  
ATOM    368  O   ILE A  56     -27.765  32.370 -22.705  1.00 51.65           O  
ANISOU  368  O   ILE A  56     6089   7223   6310    304    166   -365       O  
ATOM    369  CB  ILE A  56     -25.583  30.276 -24.099  1.00 41.42           C  
ANISOU  369  CB  ILE A  56     4749   5989   5000    304    104   -417       C  
ATOM    370  CG1 ILE A  56     -25.210  28.758 -24.132  1.00 36.72           C  
ANISOU  370  CG1 ILE A  56     4132   5415   4403    289     50   -462       C  
ATOM    371  CG2 ILE A  56     -24.876  30.852 -22.943  1.00 42.38           C  
ANISOU  371  CG2 ILE A  56     4889   6050   5162    253    122   -418       C  
ATOM    372  CD1 ILE A  56     -23.819  28.497 -24.654  1.00 38.72           C  
ANISOU  372  CD1 ILE A  56     4376   5672   4663    285     54   -466       C  
ATOM    373  N   GLU A  57     -27.461  32.596 -24.920  1.00 45.34           N  
ANISOU  373  N   GLU A  57     5267   6499   5458    392    197   -323       N  
ATOM    374  CA  GLU A  57     -27.776  34.017 -25.013  1.00 54.85           C  
ANISOU  374  CA  GLU A  57     6493   7678   6670    418    264   -269       C  
ATOM    375  C   GLU A  57     -29.179  34.261 -24.482  1.00 50.13           C  
ANISOU  375  C   GLU A  57     5902   7081   6063    426    259   -263       C  
ATOM    376  O   GLU A  57     -29.390  35.200 -23.727  1.00 50.24           O  
ANISOU  376  O   GLU A  57     5939   7041   6107    407    300   -243       O  
ATOM    377  CB  GLU A  57     -27.641  34.509 -26.478  1.00 55.98           C  
ANISOU  377  CB  GLU A  57     6625   7868   6774    491    306   -222       C  
ATOM    378  CG  GLU A  57     -27.930  35.982 -26.721  1.00 60.69           C  
ANISOU  378  CG  GLU A  57     7241   8438   7378    531    388   -155       C  
ATOM    379  CD  GLU A  57     -27.151  36.939 -25.824  1.00 70.92           C  
ANISOU  379  CD  GLU A  57     8562   9642   8741    477    444   -148       C  
ATOM    380  OE1 GLU A  57     -26.305  36.495 -24.977  1.00 71.64           O  
ANISOU  380  OE1 GLU A  57     8654   9696   8870    409    415   -195       O  
ATOM    381  OE2 GLU A  57     -27.406  38.167 -25.985  1.00 74.06           O1-
ANISOU  381  OE2 GLU A  57     8976  10009   9154    507    521    -94       O1-
ATOM    382  N   ASN A  58     -30.103  33.376 -24.819  1.00 48.10           N  
ANISOU  382  N   ASN A  58     5623   6882   5770    450    210   -288       N  
ATOM    383  CA  ASN A  58     -31.479  33.461 -24.340  1.00 49.25           C  
ANISOU  383  CA  ASN A  58     5769   7034   5907    457    199   -289       C  
ATOM    384  C   ASN A  58     -31.699  32.789 -23.024  1.00 43.91           C  
ANISOU  384  C   ASN A  58     5102   6317   5265    395    160   -332       C  
ATOM    385  O   ASN A  58     -32.815  32.545 -22.644  1.00 38.02           O  
ANISOU  385  O   ASN A  58     4350   5580   4513    397    140   -344       O  
ATOM    386  CB  ASN A  58     -32.379  32.776 -25.340  1.00 59.70           C  
ANISOU  386  CB  ASN A  58     7059   8445   7179    510    164   -303       C  
ATOM    387  CG  ASN A  58     -32.567  33.595 -26.557  1.00 72.20           C  
ANISOU  387  CG  ASN A  58     8634  10081   8716    588    206   -250       C  
ATOM    388  ND2 ASN A  58     -33.367  34.632 -26.419  1.00 90.17           N  
ANISOU  388  ND2 ASN A  58    10924  12347  10988    618    250   -203       N  
ATOM    389  OD1 ASN A  58     -31.984  33.336 -27.600  1.00 81.02           O  
ANISOU  389  OD1 ASN A  58     9733  11247   9803    623    205   -247       O  
ATOM    390  N   GLU A  59     -30.646  32.389 -22.361  1.00 39.88           N  
ANISOU  390  N   GLU A  59     4599   5764   4786    343    147   -357       N  
ATOM    391  CA  GLU A  59     -30.787  31.686 -21.118  1.00 42.66           C  
ANISOU  391  CA  GLU A  59     4957   6085   5165    293    111   -394       C  
ATOM    392  C   GLU A  59     -31.699  30.482 -21.153  1.00 40.21           C  
ANISOU  392  C   GLU A  59     4623   5811   4842    299     61   -431       C  
ATOM    393  O   GLU A  59     -32.540  30.304 -20.326  1.00 40.36           O  
ANISOU  393  O   GLU A  59     4647   5811   4875    280     48   -444       O  
ATOM    394  CB  GLU A  59     -31.188  32.661 -20.045  1.00 47.28           C  
ANISOU  394  CB  GLU A  59     5571   6619   5773    273    146   -373       C  
ATOM    395  CG  GLU A  59     -29.998  33.453 -19.595  1.00 47.56           C  
ANISOU  395  CG  GLU A  59     5622   6608   5838    239    179   -368       C  
ATOM    396  CD  GLU A  59     -30.355  34.587 -18.729  1.00 54.36           C  
ANISOU  396  CD  GLU A  59     6509   7417   6725    216    220   -355       C  
ATOM    397  OE1 GLU A  59     -30.717  35.625 -19.267  1.00 61.84           O  
ANISOU  397  OE1 GLU A  59     7465   8359   7670    249    271   -314       O  
ATOM    398  OE2 GLU A  59     -30.263  34.428 -17.524  1.00 52.92           O1-
ANISOU  398  OE2 GLU A  59     6336   7205   6564    170    202   -384       O1-
ATOM    399  N   GLU A  60     -31.470  29.650 -22.133  1.00 40.53           N  
ANISOU  399  N   GLU A  60     4636   5899   4862    320     37   -452       N  
ATOM    400  CA  GLU A  60     -32.053  28.340 -22.270  1.00 42.00           C  
ANISOU  400  CA  GLU A  60     4793   6115   5047    318     -6   -500       C  
ATOM    401  C   GLU A  60     -31.005  27.223 -22.280  1.00 40.37           C  
ANISOU  401  C   GLU A  60     4576   5904   4858    292    -33   -534       C  
ATOM    402  O   GLU A  60     -29.918  27.416 -22.748  1.00 38.65           O  
ANISOU  402  O   GLU A  60     4360   5689   4635    295    -23   -522       O  
ATOM    403  CB  GLU A  60     -32.826  28.301 -23.596  1.00 45.14           C  
ANISOU  403  CB  GLU A  60     5159   6590   5400    375    -12   -504       C  
ATOM    404  CG  GLU A  60     -34.073  29.187 -23.562  1.00 52.00           C  
ANISOU  404  CG  GLU A  60     6032   7473   6251    405      8   -475       C  
ATOM    405  CD  GLU A  60     -34.751  29.190 -24.885  1.00 54.07           C  
ANISOU  405  CD  GLU A  60     6259   7823   6462    468      2   -479       C  
ATOM    406  OE1 GLU A  60     -34.754  30.218 -25.542  1.00 64.92           O  
ANISOU  406  OE1 GLU A  60     7640   9222   7803    516     37   -429       O  
ATOM    407  OE2 GLU A  60     -35.158  28.122 -25.307  1.00 57.40           O1-
ANISOU  407  OE2 GLU A  60     6643   8290   6876    471    -35   -533       O1-
ATOM    408  N   PRO A  61     -31.345  26.058 -21.757  1.00 35.70           N  
ANISOU  408  N   PRO A  61     3971   5302   4290    268    -62   -574       N  
ATOM    409  CA  PRO A  61     -30.378  25.034 -21.561  1.00 36.26           C  
ANISOU  409  CA  PRO A  61     4035   5357   4384    243    -80   -599       C  
ATOM    410  C   PRO A  61     -29.932  24.401 -22.876  1.00 38.83           C  
ANISOU  410  C   PRO A  61     4329   5733   4688    268    -93   -625       C  
ATOM    411  O   PRO A  61     -30.634  24.469 -23.890  1.00 36.70           O  
ANISOU  411  O   PRO A  61     4037   5519   4388    305    -97   -636       O  
ATOM    412  CB  PRO A  61     -31.077  24.072 -20.638  1.00 37.78           C  
ANISOU  412  CB  PRO A  61     4223   5521   4609    218    -96   -627       C  
ATOM    413  CG  PRO A  61     -32.609  24.261 -20.975  1.00 34.72           C  
ANISOU  413  CG  PRO A  61     3819   5163   4210    240    -97   -639       C  
ATOM    414  CD  PRO A  61     -32.673  25.722 -21.216  1.00 37.19           C  
ANISOU  414  CD  PRO A  61     4153   5486   4492    263    -72   -592       C  
ATOM    415  N   VAL A  62     -28.696  23.931 -22.889  1.00 34.83           N  
ANISOU  415  N   VAL A  62     3825   5213   4195    253    -97   -629       N  
ATOM    416  CA  VAL A  62     -28.067  23.287 -24.098  1.00 35.28           C  
ANISOU  416  CA  VAL A  62     3855   5314   4236    274   -108   -653       C  
ATOM    417  C   VAL A  62     -26.980  22.415 -23.559  1.00 37.55           C  
ANISOU  417  C   VAL A  62     4144   5566   4556    243   -117   -666       C  
ATOM    418  O   VAL A  62     -26.313  22.740 -22.563  1.00 38.94           O  
ANISOU  418  O   VAL A  62     4344   5700   4751    216   -109   -641       O  
ATOM    419  CB  VAL A  62     -27.534  24.330 -25.107  1.00 38.10           C  
ANISOU  419  CB  VAL A  62     4216   5705   4553    310    -85   -618       C  
ATOM    420  CG1 VAL A  62     -26.502  25.304 -24.507  1.00 36.75           C  
ANISOU  420  CG1 VAL A  62     4077   5490   4397    290    -58   -574       C  
ATOM    421  CG2 VAL A  62     -26.985  23.688 -26.371  1.00 37.07           C  
ANISOU  421  CG2 VAL A  62     4057   5625   4400    337    -96   -643       C  
ATOM    422  N   VAL A  63     -26.900  21.224 -24.079  1.00 35.74           N  
ANISOU  422  N   VAL A  63     3888   5354   4337    245   -133   -708       N  
ATOM    423  CA  VAL A  63     -25.780  20.367 -23.801  1.00 36.92           C  
ANISOU  423  CA  VAL A  63     4035   5478   4514    225   -137   -717       C  
ATOM    424  C   VAL A  63     -24.782  20.596 -24.954  1.00 40.71           C  
ANISOU  424  C   VAL A  63     4506   5994   4965    248   -133   -711       C  
ATOM    425  O   VAL A  63     -25.130  20.437 -26.116  1.00 40.38           O  
ANISOU  425  O   VAL A  63     4441   6005   4897    278   -138   -735       O  
ATOM    426  CB  VAL A  63     -26.161  18.894 -23.823  1.00 38.12           C  
ANISOU  426  CB  VAL A  63     4160   5623   4699    217   -148   -767       C  
ATOM    427  CG1 VAL A  63     -24.924  18.023 -23.788  1.00 40.28           C  
ANISOU  427  CG1 VAL A  63     4429   5879   4996    206   -148   -773       C  
ATOM    428  CG2 VAL A  63     -27.012  18.509 -22.647  1.00 38.17           C  
ANISOU  428  CG2 VAL A  63     4174   5586   4741    195   -145   -771       C  
ATOM    429  N   LEU A  64     -23.564  20.969 -24.597  1.00 39.73           N  
ANISOU  429  N   LEU A  64     4399   5847   4848    235   -124   -682       N  
ATOM    430  CA  LEU A  64     -22.486  21.151 -25.520  1.00 40.72           C  
ANISOU  430  CA  LEU A  64     4518   5997   4956    251   -117   -673       C  
ATOM    431  C   LEU A  64     -21.574  19.946 -25.482  1.00 35.24           C  
ANISOU  431  C   LEU A  64     3809   5291   4287    238   -128   -697       C  
ATOM    432  O   LEU A  64     -21.111  19.491 -24.433  1.00 37.95           O  
ANISOU  432  O   LEU A  64     4160   5596   4661    211   -132   -692       O  
ATOM    433  CB  LEU A  64     -21.691  22.400 -25.187  1.00 43.90           C  
ANISOU  433  CB  LEU A  64     4944   6380   5355    243    -93   -628       C  
ATOM    434  CG  LEU A  64     -22.545  23.653 -25.200  1.00 46.79           C  
ANISOU  434  CG  LEU A  64     5326   6750   5701    258    -73   -599       C  
ATOM    435  CD1 LEU A  64     -21.966  24.639 -24.292  1.00 52.91           C  
ANISOU  435  CD1 LEU A  64     6124   7483   6494    231    -52   -569       C  
ATOM    436  CD2 LEU A  64     -22.660  24.301 -26.528  1.00 53.70           C  
ANISOU  436  CD2 LEU A  64     6194   7671   6538    303    -53   -582       C  
ATOM    437  N   THR A  65     -21.283  19.404 -26.635  1.00 34.75           N  
ANISOU  437  N   THR A  65     3725   5266   4211    260   -131   -721       N  
ATOM    438  CA  THR A  65     -20.606  18.106 -26.631  1.00 39.56           C  
ANISOU  438  CA  THR A  65     4317   5862   4849    249   -139   -750       C  
ATOM    439  C   THR A  65     -19.085  18.214 -26.856  1.00 36.63           C  
ANISOU  439  C   THR A  65     3949   5488   4478    248   -131   -728       C  
ATOM    440  O   THR A  65     -18.376  17.231 -26.733  1.00 37.99           O  
ANISOU  440  O   THR A  65     4111   5647   4677    239   -135   -742       O  
ATOM    441  CB  THR A  65     -21.096  17.259 -27.823  1.00 42.68           C  
ANISOU  441  CB  THR A  65     4680   6301   5233    271   -147   -803       C  
ATOM    442  CG2 THR A  65     -22.585  17.124 -27.799  1.00 47.28           C  
ANISOU  442  CG2 THR A  65     5250   6897   5814    275   -155   -835       C  
ATOM    443  OG1 THR A  65     -20.744  17.978 -28.986  1.00 42.17           O  
ANISOU  443  OG1 THR A  65     4611   6286   5122    305   -140   -790       O  
ATOM    444  N   ASP A  66     -18.555  19.357 -27.223  1.00 39.13           N  
ANISOU  444  N   ASP A  66     4278   5818   4771    259   -116   -693       N  
ATOM    445  CA  ASP A  66     -17.143  19.334 -27.639  1.00 41.46           C  
ANISOU  445  CA  ASP A  66     4568   6115   5068    261   -107   -681       C  
ATOM    446  C   ASP A  66     -16.388  20.568 -27.168  1.00 44.42           C  
ANISOU  446  C   ASP A  66     4960   6470   5445    248    -87   -640       C  
ATOM    447  O   ASP A  66     -15.613  21.144 -27.932  1.00 42.43           O  
ANISOU  447  O   ASP A  66     4706   6233   5181    263    -67   -621       O  
ATOM    448  CB  ASP A  66     -17.139  19.259 -29.163  1.00 45.62           C  
ANISOU  448  CB  ASP A  66     5078   6694   5561    300   -101   -695       C  
ATOM    449  CG  ASP A  66     -17.915  20.385 -29.780  1.00 49.55           C  
ANISOU  449  CG  ASP A  66     5583   7223   6019    330    -86   -673       C  
ATOM    450  OD1 ASP A  66     -18.634  21.081 -29.014  1.00 44.91           O  
ANISOU  450  OD1 ASP A  66     5013   6615   5435    318    -83   -655       O  
ATOM    451  OD2 ASP A  66     -17.807  20.588 -31.000  1.00 48.33           O1-
ANISOU  451  OD2 ASP A  66     5417   7116   5827    370    -75   -671       O1-
ATOM    452  N   THR A  67     -16.642  21.030 -25.932  1.00 41.12           N  
ANISOU  452  N   THR A  67     4559   6020   5044    220    -89   -627       N  
ATOM    453  CA  THR A  67     -16.042  22.265 -25.466  1.00 34.15           C  
ANISOU  453  CA  THR A  67     3689   5118   4167    204    -67   -598       C  
ATOM    454  C   THR A  67     -14.604  22.007 -24.982  1.00 37.06           C  
ANISOU  454  C   THR A  67     4047   5474   4558    182    -69   -599       C  
ATOM    455  O   THR A  67     -13.812  22.913 -24.986  1.00 42.66           O  
ANISOU  455  O   THR A  67     4757   6176   5276    172    -47   -584       O  
ATOM    456  CB  THR A  67     -16.751  22.843 -24.223  1.00 37.20           C  
ANISOU  456  CB  THR A  67     4094   5477   4564    180    -69   -592       C  
ATOM    457  CG2 THR A  67     -18.174  23.104 -24.457  1.00 39.63           C  
ANISOU  457  CG2 THR A  67     4411   5792   4853    197    -67   -591       C  
ATOM    458  OG1 THR A  67     -16.629  21.909 -23.135  1.00 32.86           O  
ANISOU  458  OG1 THR A  67     3541   4912   4033    159    -94   -607       O  
ATOM    459  N   ASN A  68     -14.317  20.809 -24.467  1.00 39.20           N  
ANISOU  459  N   ASN A  68     4307   5742   4844    175    -94   -616       N  
ATOM    460  CA  ASN A  68     -13.008  20.455 -23.892  1.00 39.84           C  
ANISOU  460  CA  ASN A  68     4375   5819   4943    159   -100   -615       C  
ATOM    461  C   ASN A  68     -12.836  21.235 -22.620  1.00 39.41           C  
ANISOU  461  C   ASN A  68     4327   5748   4896    131   -100   -609       C  
ATOM    462  O   ASN A  68     -11.696  21.540 -22.200  1.00 33.66           O  
ANISOU  462  O   ASN A  68     3585   5023   4179    114    -98   -609       O  
ATOM    463  CB  ASN A  68     -11.812  20.719 -24.849  1.00 37.56           C  
ANISOU  463  CB  ASN A  68     4072   5544   4655    167    -82   -609       C  
ATOM    464  CG  ASN A  68     -11.804  19.745 -26.003  1.00 43.46           C  
ANISOU  464  CG  ASN A  68     4808   6311   5393    195    -86   -622       C  
ATOM    465  ND2 ASN A  68     -11.974  20.234 -27.224  1.00 38.41           N  
ANISOU  465  ND2 ASN A  68     4170   5691   4732    220    -67   -616       N  
ATOM    466  OD1 ASN A  68     -11.628  18.571 -25.789  1.00 39.30           O  
ANISOU  466  OD1 ASN A  68     4270   5782   4878    197   -102   -636       O  
ATOM    467  N   LEU A  69     -13.971  21.571 -21.998  1.00 36.80           N  
ANISOU  467  N   LEU A  69     4015   5405   4561    125   -103   -607       N  
ATOM    468  CA  LEU A  69     -13.929  22.390 -20.775  1.00 35.47           C  
ANISOU  468  CA  LEU A  69     3854   5224   4398     98   -102   -605       C  
ATOM    469  C   LEU A  69     -13.104  21.764 -19.752  1.00 32.59           C  
ANISOU  469  C   LEU A  69     3474   4868   4039     88   -122   -612       C  
ATOM    470  O   LEU A  69     -12.262  22.446 -19.185  1.00 37.88           O  
ANISOU  470  O   LEU A  69     4133   5545   4715     67   -118   -619       O  
ATOM    471  CB  LEU A  69     -15.314  22.636 -20.245  1.00 36.86           C  
ANISOU  471  CB  LEU A  69     4051   5385   4566     97   -104   -603       C  
ATOM    472  CG  LEU A  69     -15.369  23.582 -19.046  1.00 37.64           C  
ANISOU  472  CG  LEU A  69     4159   5472   4669     70    -99   -604       C  
ATOM    473  CD1 LEU A  69     -14.638  24.914 -19.304  1.00 41.71           C  
ANISOU  473  CD1 LEU A  69     4671   5982   5195     52    -69   -604       C  
ATOM    474  CD2 LEU A  69     -16.840  23.789 -18.634  1.00 38.43           C  
ANISOU  474  CD2 LEU A  69     4281   5557   4762     72    -99   -598       C  
ATOM    475  N   VAL A  70     -13.332  20.468 -19.475  1.00 34.99           N  
ANISOU  475  N   VAL A  70     3774   5174   4345    103   -141   -612       N  
ATOM    476  CA  VAL A  70     -12.562  19.799 -18.434  1.00 36.82           C  
ANISOU  476  CA  VAL A  70     3992   5419   4579    103   -157   -610       C  
ATOM    477  C   VAL A  70     -11.771  18.617 -18.972  1.00 36.16           C  
ANISOU  477  C   VAL A  70     3889   5345   4505    123   -161   -608       C  
ATOM    478  O   VAL A  70     -11.669  17.561 -18.322  1.00 34.57           O  
ANISOU  478  O   VAL A  70     3682   5144   4308    139   -169   -599       O  
ATOM    479  CB  VAL A  70     -13.398  19.408 -17.239  1.00 39.38           C  
ANISOU  479  CB  VAL A  70     4329   5735   4899    107   -167   -603       C  
ATOM    480  CG1 VAL A  70     -13.931  20.657 -16.556  1.00 43.03           C  
ANISOU  480  CG1 VAL A  70     4806   6193   5351     84   -163   -608       C  
ATOM    481  CG2 VAL A  70     -14.514  18.421 -17.612  1.00 35.10           C  
ANISOU  481  CG2 VAL A  70     3797   5169   4367    125   -164   -600       C  
ATOM    482  N   TYR A  71     -11.220  18.809 -20.175  1.00 38.65           N  
ANISOU  482  N   TYR A  71     4196   5665   4823    126   -150   -613       N  
ATOM    483  CA  TYR A  71     -10.466  17.726 -20.833  1.00 40.19           C  
ANISOU  483  CA  TYR A  71     4374   5868   5029    145   -150   -613       C  
ATOM    484  C   TYR A  71      -9.483  17.017 -19.885  1.00 41.21           C  
ANISOU  484  C   TYR A  71     4483   6012   5162    151   -162   -604       C  
ATOM    485  O   TYR A  71      -9.491  15.803 -19.814  1.00 44.45           O  
ANISOU  485  O   TYR A  71     4889   6416   5584    172   -162   -597       O  
ATOM    486  CB  TYR A  71      -9.812  18.203 -22.132  1.00 44.02           C  
ANISOU  486  CB  TYR A  71     4850   6361   5512    147   -136   -618       C  
ATOM    487  CG  TYR A  71      -8.769  17.247 -22.684  1.00 43.62           C  
ANISOU  487  CG  TYR A  71     4778   6321   5472    162   -135   -618       C  
ATOM    488  CD1 TYR A  71      -9.125  16.103 -23.372  1.00 45.77           C  
ANISOU  488  CD1 TYR A  71     5050   6588   5753    183   -133   -627       C  
ATOM    489  CD2 TYR A  71      -7.402  17.477 -22.423  1.00 45.18           C  
ANISOU  489  CD2 TYR A  71     4954   6537   5675    155   -136   -614       C  
ATOM    490  CE1 TYR A  71      -8.119  15.224 -23.873  1.00 48.65           C  
ANISOU  490  CE1 TYR A  71     5395   6960   6129    198   -129   -627       C  
ATOM    491  CE2 TYR A  71      -6.401  16.598 -22.871  1.00 49.46           C  
ANISOU  491  CE2 TYR A  71     5476   7090   6227    171   -135   -612       C  
ATOM    492  CZ  TYR A  71      -6.743  15.483 -23.604  1.00 47.02           C  
ANISOU  492  CZ  TYR A  71     5168   6770   5925    193   -131   -617       C  
ATOM    493  OH  TYR A  71      -5.712  14.632 -24.000  1.00 58.67           O  
ANISOU  493  OH  TYR A  71     6623   8254   7412    208   -126   -614       O  
ATOM    494  N   PRO A  72      -8.698  17.756 -19.088  1.00 40.49           N  
ANISOU  494  N   PRO A  72     4378   5942   5061    136   -170   -605       N  
ATOM    495  CA  PRO A  72      -7.686  17.067 -18.237  1.00 40.50           C  
ANISOU  495  CA  PRO A  72     4354   5972   5059    150   -183   -596       C  
ATOM    496  C   PRO A  72      -8.290  16.316 -17.116  1.00 46.29           C  
ANISOU  496  C   PRO A  72     5095   6704   5785    169   -191   -579       C  
ATOM    497  O   PRO A  72      -7.647  15.424 -16.594  1.00 41.40           O  
ANISOU  497  O   PRO A  72     4460   6105   5165    194   -195   -563       O  
ATOM    498  CB  PRO A  72      -6.867  18.233 -17.646  1.00 46.14           C  
ANISOU  498  CB  PRO A  72     5050   6717   5764    124   -190   -613       C  
ATOM    499  CG  PRO A  72      -6.978  19.336 -18.698  1.00 45.79           C  
ANISOU  499  CG  PRO A  72     5015   6652   5731    100   -170   -627       C  
ATOM    500  CD  PRO A  72      -8.438  19.199 -19.173  1.00 44.33           C  
ANISOU  500  CD  PRO A  72     4864   6433   5545    108   -162   -618       C  
ATOM    501  N   ALA A  73      -9.554  16.644 -16.741  1.00 43.05           N  
ANISOU  501  N   ALA A  73     4712   6272   5372    161   -190   -580       N  
ATOM    502  CA  ALA A  73     -10.221  15.908 -15.665  1.00 41.71           C  
ANISOU  502  CA  ALA A  73     4551   6096   5197    181   -191   -560       C  
ATOM    503  C   ALA A  73     -10.791  14.610 -16.156  1.00 39.55           C  
ANISOU  503  C   ALA A  73     4286   5789   4951    204   -173   -548       C  
ATOM    504  O   ALA A  73     -11.185  13.740 -15.362  1.00 41.21           O  
ANISOU  504  O   ALA A  73     4500   5988   5168    229   -164   -526       O  
ATOM    505  CB  ALA A  73     -11.307  16.738 -15.022  1.00 44.56           C  
ANISOU  505  CB  ALA A  73     4936   6447   5547    164   -194   -565       C  
ATOM    506  N   LEU A  74     -10.870  14.430 -17.471  1.00 43.10           N  
ANISOU  506  N   LEU A  74     4735   6220   5418    199   -164   -565       N  
ATOM    507  CA  LEU A  74     -11.455  13.197 -17.949  1.00 45.10           C  
ANISOU  507  CA  LEU A  74     4991   6441   5702    217   -145   -566       C  
ATOM    508  C   LEU A  74     -10.786  11.932 -17.481  1.00 48.80           C  
ANISOU  508  C   LEU A  74     5445   6907   6189    248   -131   -542       C  
ATOM    509  O   LEU A  74     -11.467  10.907 -17.351  1.00 49.76           O  
ANISOU  509  O   LEU A  74     5572   6993   6341    264   -108   -536       O  
ATOM    510  CB  LEU A  74     -11.623  13.206 -19.445  1.00 47.17           C  
ANISOU  510  CB  LEU A  74     5251   6694   5975    209   -139   -594       C  
ATOM    511  CG  LEU A  74     -12.514  14.368 -19.914  1.00 44.75           C  
ANISOU  511  CG  LEU A  74     4961   6389   5651    188   -145   -611       C  
ATOM    512  CD1 LEU A  74     -12.724  14.257 -21.428  1.00 44.89           C  
ANISOU  512  CD1 LEU A  74     4974   6408   5673    190   -138   -637       C  
ATOM    513  CD2 LEU A  74     -13.845  14.375 -19.236  1.00 45.96           C  
ANISOU  513  CD2 LEU A  74     5132   6519   5808    184   -143   -611       C  
ATOM    514  N   LYS A  75      -9.479  11.982 -17.188  1.00 46.62           N  
ANISOU  514  N   LYS A  75     5148   6666   5896    258   -141   -527       N  
ATOM    515  CA  LYS A  75      -8.776  10.816 -16.604  1.00 50.43           C  
ANISOU  515  CA  LYS A  75     5615   7154   6390    296   -127   -495       C  
ATOM    516  C   LYS A  75      -9.004  10.614 -15.120  1.00 53.32           C  
ANISOU  516  C   LYS A  75     5985   7534   6740    322   -126   -461       C  
ATOM    517  O   LYS A  75      -8.578   9.634 -14.583  1.00 51.82           O  
ANISOU  517  O   LYS A  75     5783   7346   6557    361   -107   -427       O  
ATOM    518  CB  LYS A  75      -7.256  10.947 -16.821  1.00 49.01           C  
ANISOU  518  CB  LYS A  75     5407   7016   6196    303   -139   -492       C  
ATOM    519  CG  LYS A  75      -6.722  12.288 -16.376  1.00 48.54           C  
ANISOU  519  CG  LYS A  75     5338   7003   6099    279   -169   -505       C  
ATOM    520  CD  LYS A  75      -5.201  12.391 -16.561  1.00 49.74           C  
ANISOU  520  CD  LYS A  75     5457   7199   6243    284   -180   -506       C  
ATOM    521  CE  LYS A  75      -4.626  13.324 -15.547  1.00 45.93           C  
ANISOU  521  CE  LYS A  75     4955   6771   5726    275   -206   -513       C  
ATOM    522  NZ  LYS A  75      -4.699  14.688 -16.074  1.00 45.37           N1+
ANISOU  522  NZ  LYS A  75     4887   6696   5652    229   -213   -549       N1+
ATOM    523  N   TRP A  76      -9.623  11.559 -14.431  1.00 54.76           N  
ANISOU  523  N   TRP A  76     6180   7728   6895    304   -143   -467       N  
ATOM    524  CA  TRP A  76      -9.902  11.417 -12.984  1.00 53.92           C  
ANISOU  524  CA  TRP A  76     6079   7640   6767    331   -142   -436       C  
ATOM    525  C   TRP A  76     -10.736  10.193 -12.641  1.00 58.32           C  
ANISOU  525  C   TRP A  76     6650   8150   7359    362   -104   -405       C  
ATOM    526  O   TRP A  76     -11.728   9.879 -13.304  1.00 59.66           O  
ANISOU  526  O   TRP A  76     6836   8266   7567    346    -84   -423       O  
ATOM    527  CB  TRP A  76     -10.681  12.619 -12.445  1.00 51.42           C  
ANISOU  527  CB  TRP A  76     5780   7332   6424    301   -162   -454       C  
ATOM    528  CG  TRP A  76      -9.918  13.864 -12.446  1.00 50.33           C  
ANISOU  528  CG  TRP A  76     5627   7239   6256    272   -192   -482       C  
ATOM    529  CD1 TRP A  76      -8.635  14.063 -12.936  1.00 47.21           C  
ANISOU  529  CD1 TRP A  76     5203   6877   5855    267   -204   -495       C  
ATOM    530  CD2 TRP A  76     -10.353  15.120 -11.983  1.00 44.77           C  
ANISOU  530  CD2 TRP A  76     4933   6548   5529    242   -208   -505       C  
ATOM    531  CE2 TRP A  76      -9.297  16.032 -12.196  1.00 46.99           C  
ANISOU  531  CE2 TRP A  76     5190   6868   5796    217   -226   -533       C  
ATOM    532  CE3 TRP A  76     -11.536  15.576 -11.417  1.00 45.92           C  
ANISOU  532  CE3 TRP A  76     5104   6674   5668    231   -205   -506       C  
ATOM    533  NE1 TRP A  76      -8.263  15.353 -12.770  1.00 44.34           N  
ANISOU  533  NE1 TRP A  76     4830   6544   5470    234   -224   -526       N  
ATOM    534  CZ2 TRP A  76      -9.383  17.343 -11.851  1.00 47.30           C  
ANISOU  534  CZ2 TRP A  76     5229   6923   5819    183   -238   -564       C  
ATOM    535  CZ3 TRP A  76     -11.618  16.892 -11.074  1.00 44.70           C  
ANISOU  535  CZ3 TRP A  76     4952   6538   5493    199   -220   -533       C  
ATOM    536  CH2 TRP A  76     -10.560  17.759 -11.277  1.00 45.26           C  
ANISOU  536  CH2 TRP A  76     4998   6644   5553    175   -235   -563       C  
ATOM    537  N   ASP A  77     -10.328   9.533 -11.567  1.00 52.99           N  
ANISOU  537  N   ASP A  77     5966   7499   6669    410    -91   -360       N  
ATOM    538  CA  ASP A  77     -11.076   8.472 -10.938  1.00 54.15           C  
ANISOU  538  CA  ASP A  77     6125   7603   6844    448    -48   -321       C  
ATOM    539  C   ASP A  77     -10.637   8.465  -9.488  1.00 53.81           C  
ANISOU  539  C   ASP A  77     6073   7618   6752    495    -53   -275       C  
ATOM    540  O   ASP A  77      -9.817   9.289  -9.080  1.00 53.80           O  
ANISOU  540  O   ASP A  77     6054   7688   6699    492    -93   -286       O  
ATOM    541  CB  ASP A  77     -10.864   7.114 -11.624  1.00 58.26           C  
ANISOU  541  CB  ASP A  77     6638   8075   7422    471     -2   -307       C  
ATOM    542  CG  ASP A  77      -9.391   6.638 -11.629  1.00 54.61           C  
ANISOU  542  CG  ASP A  77     6147   7656   6944    506     -4   -281       C  
ATOM    543  OD1 ASP A  77      -8.471   7.220 -11.026  1.00 61.44           O  
ANISOU  543  OD1 ASP A  77     6994   8594   7755    520    -38   -271       O  
ATOM    544  OD2 ASP A  77      -9.161   5.643 -12.289  1.00 62.68           O1-
ANISOU  544  OD2 ASP A  77     7162   8638   8014    520     31   -275       O1-
ATOM    545  N   LEU A  78     -11.175   7.566  -8.683  1.00 57.92           N  
ANISOU  545  N   LEU A  78     6604   8113   7289    542    -11   -227       N  
ATOM    546  CA  LEU A  78     -10.879   7.654  -7.254  1.00 54.01           C  
ANISOU  546  CA  LEU A  78     6102   7682   6736    592    -17   -183       C  
ATOM    547  C   LEU A  78      -9.380   7.506  -6.974  1.00 53.81           C  
ANISOU  547  C   LEU A  78     6041   7735   6668    631    -36   -162       C  
ATOM    548  O   LEU A  78      -8.820   8.298  -6.213  1.00 51.51           O  
ANISOU  548  O   LEU A  78     5732   7527   6312    638    -78   -170       O  
ATOM    549  CB  LEU A  78     -11.717   6.657  -6.480  1.00 58.16           C  
ANISOU  549  CB  LEU A  78     6646   8162   7289    642     40   -126       C  
ATOM    550  CG  LEU A  78     -13.221   6.877  -6.598  1.00 58.46           C  
ANISOU  550  CG  LEU A  78     6714   8131   7364    605     57   -148       C  
ATOM    551  CD1 LEU A  78     -13.947   5.804  -5.800  1.00 58.86           C  
ANISOU  551  CD1 LEU A  78     6779   8134   7449    659    124    -88       C  
ATOM    552  CD2 LEU A  78     -13.645   8.253  -6.087  1.00 58.09           C  
ANISOU  552  CD2 LEU A  78     6679   8128   7264    570      8   -179       C  
ATOM    553  N   GLU A  79      -8.706   6.598  -7.680  1.00 53.16           N  
ANISOU  553  N   GLU A  79     5945   7630   6623    650    -10   -147       N  
ATOM    554  CA  GLU A  79      -7.293   6.374  -7.392  1.00 58.93           C  
ANISOU  554  CA  GLU A  79     6639   8436   7314    693    -25   -123       C  
ATOM    555  C   GLU A  79      -6.475   7.644  -7.684  1.00 55.07           C  
ANISOU  555  C   GLU A  79     6127   8015   6782    645    -90   -181       C  
ATOM    556  O   GLU A  79      -5.741   8.191  -6.808  1.00 55.33           O  
ANISOU  556  O   GLU A  79     6131   8140   6750    667   -125   -181       O  
ATOM    557  CB  GLU A  79      -6.758   5.175  -8.204  1.00 70.22           C  
ANISOU  557  CB  GLU A  79     8060   9820   8800    716     18    -99       C  
ATOM    558  CG  GLU A  79      -5.460   4.589  -7.624  1.00 74.48           C  
ANISOU  558  CG  GLU A  79     8563  10431   9302    787     22    -48       C  
ATOM    559  CD  GLU A  79      -4.559   3.892  -8.656  1.00 83.72           C  
ANISOU  559  CD  GLU A  79     9716  11579  10514    789     40    -49       C  
ATOM    560  OE1 GLU A  79      -5.104   3.278  -9.612  1.00 68.50           O  
ANISOU  560  OE1 GLU A  79     7808   9561   8658    764     79    -63       O  
ATOM    561  OE2 GLU A  79      -3.299   3.941  -8.490  1.00 80.59           O1-
ANISOU  561  OE2 GLU A  79     9283  11259  10077    818     16    -38       O1-
ATOM    562  N   TYR A  80      -6.636   8.147  -8.910  1.00 53.14           N  
ANISOU  562  N   TYR A  80     5891   7725   6573    581   -102   -234       N  
ATOM    563  CA  TYR A  80      -5.935   9.344  -9.316  1.00 49.99           C  
ANISOU  563  CA  TYR A  80     5473   7373   6147    533   -151   -288       C  
ATOM    564  C   TYR A  80      -6.236  10.480  -8.375  1.00 50.40           C  
ANISOU  564  C   TYR A  80     5525   7475   6148    515   -185   -311       C  
ATOM    565  O   TYR A  80      -5.340  11.216  -7.961  1.00 54.89           O  
ANISOU  565  O   TYR A  80     6060   8120   6673    509   -221   -337       O  
ATOM    566  CB  TYR A  80      -6.257   9.720 -10.749  1.00 51.44           C  
ANISOU  566  CB  TYR A  80     5673   7496   6375    473   -151   -333       C  
ATOM    567  CG  TYR A  80      -5.555  10.956 -11.205  1.00 54.37           C  
ANISOU  567  CG  TYR A  80     6025   7907   6726    426   -189   -383       C  
ATOM    568  CD1 TYR A  80      -4.244  10.926 -11.711  1.00 56.56           C  
ANISOU  568  CD1 TYR A  80     6269   8220   7001    428   -200   -392       C  
ATOM    569  CD2 TYR A  80      -6.170  12.174 -11.099  1.00 50.42           C  
ANISOU  569  CD2 TYR A  80     5539   7406   6212    381   -210   -420       C  
ATOM    570  CE1 TYR A  80      -3.607  12.094 -12.134  1.00 54.13           C  
ANISOU  570  CE1 TYR A  80     5942   7941   6682    383   -229   -439       C  
ATOM    571  CE2 TYR A  80      -5.542  13.330 -11.505  1.00 48.02           C  
ANISOU  571  CE2 TYR A  80     5218   7130   5898    337   -235   -465       C  
ATOM    572  CZ  TYR A  80      -4.278  13.311 -12.030  1.00 51.14           C  
ANISOU  572  CZ  TYR A  80     5579   7555   6294    336   -243   -476       C  
ATOM    573  OH  TYR A  80      -3.742  14.527 -12.426  1.00 47.36           O  
ANISOU  573  OH  TYR A  80     5084   7095   5814    290   -261   -523       O  
ATOM    574  N   LEU A  81      -7.463  10.582  -7.913  1.00 49.35           N  
ANISOU  574  N   LEU A  81     5424   7306   6020    511   -172   -303       N  
ATOM    575  CA  LEU A  81      -7.771  11.705  -7.005  1.00 49.39           C  
ANISOU  575  CA  LEU A  81     5430   7359   5977    492   -203   -329       C  
ATOM    576  C   LEU A  81      -7.297  11.437  -5.582  1.00 51.53           C  
ANISOU  576  C   LEU A  81     5677   7713   6187    555   -212   -294       C  
ATOM    577  O   LEU A  81      -6.945  12.369  -4.821  1.00 47.59           O  
ANISOU  577  O   LEU A  81     5156   7289   5635    546   -248   -327       O  
ATOM    578  CB  LEU A  81      -9.293  12.062  -6.985  1.00 48.05           C  
ANISOU  578  CB  LEU A  81     5303   7124   5829    463   -189   -337       C  
ATOM    579  CG  LEU A  81      -9.939  12.589  -8.279  1.00 48.03           C  
ANISOU  579  CG  LEU A  81     5322   7053   5872    401   -187   -378       C  
ATOM    580  CD1 LEU A  81     -11.466  12.583  -8.176  1.00 49.40           C  
ANISOU  580  CD1 LEU A  81     5534   7165   6070    389   -166   -372       C  
ATOM    581  CD2 LEU A  81      -9.432  13.978  -8.663  1.00 43.82           C  
ANISOU  581  CD2 LEU A  81     4776   6550   5322    348   -222   -433       C  
ATOM    582  N   GLN A  82      -7.412  10.208  -5.127  1.00 54.96           N  
ANISOU  582  N   GLN A  82     6117   8138   6627    621   -174   -229       N  
ATOM    583  CA  GLN A  82      -6.901   9.962  -3.773  1.00 58.80           C  
ANISOU  583  CA  GLN A  82     6578   8716   7047    692   -181   -190       C  
ATOM    584  C   GLN A  82      -5.420  10.323  -3.731  1.00 59.02           C  
ANISOU  584  C   GLN A  82     6553   8840   7032    698   -222   -217       C  
ATOM    585  O   GLN A  82      -4.962  10.937  -2.815  1.00 56.40           O  
ANISOU  585  O   GLN A  82     6190   8602   6635    712   -256   -237       O  
ATOM    586  CB  GLN A  82      -7.044   8.523  -3.409  1.00 68.70           C  
ANISOU  586  CB  GLN A  82     7839   9944   8317    769   -126   -108       C  
ATOM    587  CG  GLN A  82      -6.583   8.302  -1.995  1.00 71.93           C  
ANISOU  587  CG  GLN A  82     8224  10456   8650    850   -131    -62       C  
ATOM    588  CD  GLN A  82      -7.088   7.004  -1.433  1.00 71.90           C  
ANISOU  588  CD  GLN A  82     8239  10415   8664    931    -64     26       C  
ATOM    589  NE2 GLN A  82      -6.286   6.398  -0.605  1.00 84.88           N  
ANISOU  589  NE2 GLN A  82     9853  12141  10255   1018    -55     83       N  
ATOM    590  OE1 GLN A  82      -8.170   6.555  -1.732  1.00 73.05           O  
ANISOU  590  OE1 GLN A  82     8424  10460   8870    917    -19     44       O  
ATOM    591  N   GLU A  83      -4.732   9.982  -4.804  1.00 60.33           N  
ANISOU  591  N   GLU A  83     6707   8977   7238    680   -216   -225       N  
ATOM    592  CA  GLU A  83      -3.316  10.195  -4.941  1.00 65.29           C  
ANISOU  592  CA  GLU A  83     7284   9682   7839    685   -248   -248       C  
ATOM    593  C   GLU A  83      -2.954  11.694  -5.023  1.00 66.24           C  
ANISOU  593  C   GLU A  83     7382   9846   7938    616   -297   -332       C  
ATOM    594  O   GLU A  83      -1.928  12.124  -4.525  1.00 62.58           O  
ANISOU  594  O   GLU A  83     6869   9480   7428    625   -331   -361       O  
ATOM    595  CB  GLU A  83      -2.871   9.452  -6.219  1.00 63.81           C  
ANISOU  595  CB  GLU A  83     7100   9431   7713    676   -222   -236       C  
ATOM    596  CG  GLU A  83      -1.398   9.416  -6.467  1.00 77.54           C  
ANISOU  596  CG  GLU A  83     8788  11238   9434    689   -243   -248       C  
ATOM    597  CD  GLU A  83      -0.719   8.565  -5.425  1.00 82.87           C  
ANISOU  597  CD  GLU A  83     9431  11997  10059    781   -236   -187       C  
ATOM    598  OE1 GLU A  83      -1.294   7.506  -5.080  1.00 83.17           O  
ANISOU  598  OE1 GLU A  83     9493  11994  10110    839   -189   -118       O  
ATOM    599  OE2 GLU A  83       0.348   8.981  -4.937  1.00 86.75           O1-
ANISOU  599  OE2 GLU A  83     9869  12592  10497    797   -274   -210       O1-
ATOM    600  N   ASN A  84      -3.803  12.512  -5.620  1.00 61.32           N  
ANISOU  600  N   ASN A  84     6793   9155   7350    547   -298   -373       N  
ATOM    601  CA  ASN A  84      -3.389  13.881  -5.962  1.00 58.14           C  
ANISOU  601  CA  ASN A  84     6370   8774   6945    478   -330   -450       C  
ATOM    602  C   ASN A  84      -4.155  15.026  -5.359  1.00 57.48           C  
ANISOU  602  C   ASN A  84     6300   8696   6842    438   -346   -493       C  
ATOM    603  O   ASN A  84      -3.671  16.175  -5.442  1.00 55.59           O  
ANISOU  603  O   ASN A  84     6035   8486   6599    386   -369   -559       O  
ATOM    604  CB  ASN A  84      -3.391  14.055  -7.480  1.00 61.61           C  
ANISOU  604  CB  ASN A  84     6827   9133   7448    425   -316   -471       C  
ATOM    605  CG  ASN A  84      -2.313  13.245  -8.135  1.00 69.23           C  
ANISOU  605  CG  ASN A  84     7765  10108   8429    450   -309   -450       C  
ATOM    606  ND2 ASN A  84      -2.681  12.122  -8.746  1.00 70.67           N  
ANISOU  606  ND2 ASN A  84     7974  10226   8649    477   -274   -403       N  
ATOM    607  OD1 ASN A  84      -1.148  13.619  -8.063  1.00 66.68           O  
ANISOU  607  OD1 ASN A  84     7396   9852   8087    446   -332   -480       O  
ATOM    608  N   ILE A  85      -5.303  14.747  -4.729  1.00 56.07           N  
ANISOU  608  N   ILE A  85     6158   8489   6654    460   -330   -459       N  
ATOM    609  CA  ILE A  85      -6.249  15.820  -4.370  1.00 58.60           C  
ANISOU  609  CA  ILE A  85     6503   8791   6970    416   -337   -498       C  
ATOM    610  C   ILE A  85      -5.839  16.539  -3.065  1.00 68.59           C  
ANISOU  610  C   ILE A  85     7732  10159   8168    426   -369   -535       C  
ATOM    611  O   ILE A  85      -6.439  17.545  -2.640  1.00 69.49           O  
ANISOU  611  O   ILE A  85     7857  10273   8272    388   -378   -577       O  
ATOM    612  CB  ILE A  85      -7.721  15.307  -4.424  1.00 50.49           C  
ANISOU  612  CB  ILE A  85     5532   7679   5971    425   -304   -453       C  
ATOM    613  CG1 ILE A  85      -8.672  16.484  -4.644  1.00 59.05           C  
ANISOU  613  CG1 ILE A  85     6645   8716   7073    362   -306   -497       C  
ATOM    614  CG2 ILE A  85      -8.125  14.495  -3.209  1.00 53.74           C  
ANISOU  614  CG2 ILE A  85     5950   8124   6342    496   -291   -397       C  
ATOM    615  CD1 ILE A  85     -10.116  16.075  -4.941  1.00 58.76           C  
ANISOU  615  CD1 ILE A  85     6660   8592   7074    360   -274   -464       C  
ATOM    616  N   GLY A  86      -4.793  16.051  -2.429  1.00 69.53           N  
ANISOU  616  N   GLY A  86     7803  10373   8240    478   -388   -524       N  
ATOM    617  CA  GLY A  86      -4.305  16.699  -1.233  1.00 63.68           C  
ANISOU  617  CA  GLY A  86     7017   9748   7428    496   -423   -565       C  
ATOM    618  C   GLY A  86      -4.929  16.201   0.042  1.00 61.78           C  
ANISOU  618  C   GLY A  86     6792   9551   7131    562   -417   -518       C  
ATOM    619  O   GLY A  86      -5.601  15.197   0.056  1.00 55.69           O  
ANISOU  619  O   GLY A  86     6061   8722   6374    607   -382   -443       O  
ATOM    620  N   ASN A  87      -4.694  16.919   1.124  1.00 63.77           N  
ANISOU  620  N   ASN A  87     7008   9902   7319    566   -450   -569       N  
ATOM    621  CA  ASN A  87      -5.213  16.492   2.398  1.00 71.12           C  
ANISOU  621  CA  ASN A  87     7942  10897   8182    635   -450   -531       C  
ATOM    622  C   ASN A  87      -6.151  17.448   3.077  1.00 68.95           C  
ANISOU  622  C   ASN A  87     7693  10611   7893    599   -454   -572       C  
ATOM    623  O   ASN A  87      -6.245  17.466   4.277  1.00 72.78           O  
ANISOU  623  O   ASN A  87     8167  11177   8308    650   -464   -563       O  
ATOM    624  CB  ASN A  87      -4.094  16.121   3.341  1.00 79.28           C  
ANISOU  624  CB  ASN A  87     8906  12083   9132    698   -484   -543       C  
ATOM    625  CG  ASN A  87      -4.316  14.780   3.969  1.00 89.21           C  
ANISOU  625  CG  ASN A  87    10172  13390  10333    808   -464   -448       C  
ATOM    626  ND2 ASN A  87      -4.556  13.785   3.143  1.00 98.42           N  
ANISOU  626  ND2 ASN A  87    11384  14459  11549    840   -416   -360       N  
ATOM    627  OD1 ASN A  87      -4.252  14.633   5.194  1.00 88.77           O  
ANISOU  627  OD1 ASN A  87    10082  13455  10192    865   -486   -454       O  
ATOM    628  N   GLY A  88      -6.872  18.221   2.299  1.00 68.44           N  
ANISOU  628  N   GLY A  88     7664  10446   7893    517   -442   -609       N  
ATOM    629  CA  GLY A  88      -7.911  19.045   2.848  1.00 62.35           C  
ANISOU  629  CA  GLY A  88     6928   9640   7119    486   -435   -631       C  
ATOM    630  C   GLY A  88      -9.038  18.164   3.296  1.00 61.01           C  
ANISOU  630  C   GLY A  88     6805   9436   6938    548   -403   -545       C  
ATOM    631  O   GLY A  88      -9.068  16.998   2.990  1.00 59.23           O  
ANISOU  631  O   GLY A  88     6595   9180   6730    601   -377   -468       O  
ATOM    632  N   ASP A  89      -9.962  18.744   4.037  1.00 63.96           N  
ANISOU  632  N   ASP A  89     7202   9814   7286    542   -402   -560       N  
ATOM    633  CA  ASP A  89     -11.254  18.094   4.371  1.00 65.41           C  
ANISOU  633  CA  ASP A  89     7440   9932   7479    580   -364   -487       C  
ATOM    634  C   ASP A  89     -12.270  18.159   3.229  1.00 59.34           C  
ANISOU  634  C   ASP A  89     6724   9023   6798    522   -333   -475       C  
ATOM    635  O   ASP A  89     -12.438  19.203   2.604  1.00 54.99           O  
ANISOU  635  O   ASP A  89     6179   8431   6283    446   -342   -536       O  
ATOM    636  CB  ASP A  89     -11.908  18.803   5.508  1.00 59.43           C  
ANISOU  636  CB  ASP A  89     6689   9220   6670    585   -372   -513       C  
ATOM    637  CG  ASP A  89     -11.280  18.497   6.832  1.00 63.39           C  
ANISOU  637  CG  ASP A  89     7149   9861   7074    665   -393   -502       C  
ATOM    638  OD1 ASP A  89     -10.549  17.512   6.961  1.00 63.89           O  
ANISOU  638  OD1 ASP A  89     7188   9975   7109    734   -391   -449       O  
ATOM    639  OD2 ASP A  89     -11.577  19.263   7.752  1.00 59.96           O1-
ANISOU  639  OD2 ASP A  89     6708   9484   6589    662   -409   -546       O1-
ATOM    640  N   PHE A  90     -12.992  17.075   3.027  1.00 55.84           N  
ANISOU  640  N   PHE A  90     6317   8512   6388    561   -294   -399       N  
ATOM    641  CA  PHE A  90     -14.087  17.037   2.022  1.00 53.76           C  
ANISOU  641  CA  PHE A  90     6100   8122   6202    514   -264   -388       C  
ATOM    642  C   PHE A  90     -15.424  16.831   2.676  1.00 57.66           C  
ANISOU  642  C   PHE A  90     6634   8574   6698    536   -233   -349       C  
ATOM    643  O   PHE A  90     -15.578  15.872   3.461  1.00 56.34           O  
ANISOU  643  O   PHE A  90     6471   8428   6506    610   -208   -283       O  
ATOM    644  CB  PHE A  90     -13.843  15.930   1.044  1.00 49.36           C  
ANISOU  644  CB  PHE A  90     5547   7509   5699    529   -239   -345       C  
ATOM    645  CG  PHE A  90     -12.718  16.211   0.140  1.00 50.79           C  
ANISOU  645  CG  PHE A  90     5696   7706   5894    494   -264   -386       C  
ATOM    646  CD1 PHE A  90     -11.387  16.026   0.581  1.00 54.24           C  
ANISOU  646  CD1 PHE A  90     6084   8241   6281    531   -289   -391       C  
ATOM    647  CD2 PHE A  90     -12.948  16.673  -1.146  1.00 50.23           C  
ANISOU  647  CD2 PHE A  90     5640   7561   5883    428   -262   -420       C  
ATOM    648  CE1 PHE A  90     -10.323  16.309  -0.268  1.00 54.15           C  
ANISOU  648  CE1 PHE A  90     6042   8245   6287    496   -311   -431       C  
ATOM    649  CE2 PHE A  90     -11.885  16.959  -1.986  1.00 53.22           C  
ANISOU  649  CE2 PHE A  90     5989   7955   6275    398   -281   -456       C  
ATOM    650  CZ  PHE A  90     -10.574  16.767  -1.544  1.00 56.77           C  
ANISOU  650  CZ  PHE A  90     6392   8495   6682    430   -305   -462       C  
ATOM    651  N   SER A  91     -16.386  17.700   2.348  1.00 52.65           N  
ANISOU  651  N   SER A  91     6030   7879   6096    477   -230   -383       N  
ATOM    652  CA  SER A  91     -17.773  17.459   2.794  1.00 55.84           C  
ANISOU  652  CA  SER A  91     6475   8226   6515    492   -196   -345       C  
ATOM    653  C   SER A  91     -18.363  16.287   2.072  1.00 48.91           C  
ANISOU  653  C   SER A  91     5619   7260   5702    509   -154   -290       C  
ATOM    654  O   SER A  91     -18.479  16.271   0.843  1.00 46.49           O  
ANISOU  654  O   SER A  91     5318   6889   5453    464   -151   -309       O  
ATOM    655  CB  SER A  91     -18.680  18.678   2.656  1.00 51.18           C  
ANISOU  655  CB  SER A  91     5909   7595   5941    429   -202   -393       C  
ATOM    656  OG  SER A  91     -18.095  19.818   3.284  1.00 56.28           O  
ANISOU  656  OG  SER A  91     6530   8317   6534    406   -236   -454       O  
ATOM    657  N   VAL A  92     -18.719  15.288   2.862  1.00 48.12           N  
ANISOU  657  N   VAL A  92     5529   7161   5592    577   -119   -224       N  
ATOM    658  CA  VAL A  92     -19.341  14.083   2.389  1.00 51.46           C  
ANISOU  658  CA  VAL A  92     5971   7500   6081    600    -68   -171       C  
ATOM    659  C   VAL A  92     -20.669  13.931   3.115  1.00 58.17           C  
ANISOU  659  C   VAL A  92     6853   8306   6941    620    -29   -136       C  
ATOM    660  O   VAL A  92     -20.700  13.874   4.359  1.00 61.53           O  
ANISOU  660  O   VAL A  92     7280   8789   7309    675    -22   -102       O  
ATOM    661  CB  VAL A  92     -18.484  12.844   2.693  1.00 50.51           C  
ANISOU  661  CB  VAL A  92     5830   7412   5949    675    -43   -110       C  
ATOM    662  CG1 VAL A  92     -19.206  11.599   2.234  1.00 54.77           C  
ANISOU  662  CG1 VAL A  92     6389   7854   6567    696     19    -59       C  
ATOM    663  CG2 VAL A  92     -17.148  12.923   1.990  1.00 48.92           C  
ANISOU  663  CG2 VAL A  92     5594   7255   5738    660    -79   -141       C  
ATOM    664  N   TYR A  93     -21.747  13.859   2.319  1.00 57.00           N  
ANISOU  664  N   TYR A  93     6729   8062   6865    576     -5   -147       N  
ATOM    665  CA  TYR A  93     -23.126  13.648   2.801  1.00 50.13           C  
ANISOU  665  CA  TYR A  93     5889   7133   6023    586     36   -118       C  
ATOM    666  C   TYR A  93     -23.421  12.165   2.801  1.00 52.97           C  
ANISOU  666  C   TYR A  93     6253   7434   6439    637    100    -55       C  
ATOM    667  O   TYR A  93     -23.075  11.423   1.872  1.00 47.67           O  
ANISOU  667  O   TYR A  93     5568   6721   5820    629    115    -56       O  
ATOM    668  CB  TYR A  93     -24.160  14.410   1.919  1.00 51.81           C  
ANISOU  668  CB  TYR A  93     6120   7279   6285    512     27   -168       C  
ATOM    669  CG  TYR A  93     -24.039  15.898   2.107  1.00 48.60           C  
ANISOU  669  CG  TYR A  93     5715   6921   5829    469    -20   -222       C  
ATOM    670  CD1 TYR A  93     -24.753  16.588   3.148  1.00 47.36           C  
ANISOU  670  CD1 TYR A  93     5576   6782   5633    475    -19   -220       C  
ATOM    671  CD2 TYR A  93     -23.124  16.598   1.360  1.00 45.80           C  
ANISOU  671  CD2 TYR A  93     5341   6598   5462    428    -62   -271       C  
ATOM    672  CE1 TYR A  93     -24.549  17.949   3.362  1.00 45.02           C  
ANISOU  672  CE1 TYR A  93     5278   6531   5294    436    -59   -274       C  
ATOM    673  CE2 TYR A  93     -22.903  17.936   1.561  1.00 50.14           C  
ANISOU  673  CE2 TYR A  93     5888   7190   5972    390    -98   -321       C  
ATOM    674  CZ  TYR A  93     -23.621  18.606   2.557  1.00 49.76           C  
ANISOU  674  CZ  TYR A  93     5858   7157   5891    393    -96   -324       C  
ATOM    675  OH  TYR A  93     -23.358  19.912   2.656  1.00 57.00           O  
ANISOU  675  OH  TYR A  93     6770   8108   6779    350   -126   -380       O  
ATOM    676  N   SER A  94     -24.120  11.758   3.836  1.00 56.87           N  
ANISOU  676  N   SER A  94     6764   7919   6926    687    143     -3       N  
ATOM    677  CA  SER A  94     -24.460  10.393   4.069  1.00 60.95           C  
ANISOU  677  CA  SER A  94     7285   8378   7494    743    216     64       C  
ATOM    678  C   SER A  94     -25.970  10.285   4.129  1.00 55.59           C  
ANISOU  678  C   SER A  94     6631   7613   6876    724    261     69       C  
ATOM    679  O   SER A  94     -26.591  11.063   4.819  1.00 62.61           O  
ANISOU  679  O   SER A  94     7537   8523   7727    718    248     63       O  
ATOM    680  CB  SER A  94     -23.882  10.021   5.440  1.00 68.24           C  
ANISOU  680  CB  SER A  94     8203   9380   8343    835    234    132       C  
ATOM    681  OG  SER A  94     -23.900   8.630   5.600  1.00 66.99           O  
ANISOU  681  OG  SER A  94     8044   9174   8233    899    309    205       O  
ATOM    682  N   ALA A  95     -26.584   9.339   3.449  1.00 57.69           N  
ANISOU  682  N   ALA A  95     6897   7784   7236    714    316     77       N  
ATOM    683  CA  ALA A  95     -28.019   9.089   3.697  1.00 56.58           C  
ANISOU  683  CA  ALA A  95     6776   7565   7156    708    370     90       C  
ATOM    684  C   ALA A  95     -28.453   7.641   3.503  1.00 58.66           C  
ANISOU  684  C   ALA A  95     7034   7736   7516    737    458    130       C  
ATOM    685  O   ALA A  95     -27.806   6.889   2.807  1.00 61.16           O  
ANISOU  685  O   ALA A  95     7332   8032   7872    739    473    129       O  
ATOM    686  CB  ALA A  95     -28.861   9.974   2.811  1.00 56.37           C  
ANISOU  686  CB  ALA A  95     6754   7504   7158    624    332     16       C  
ATOM    687  N   SER A  96     -29.576   7.278   4.117  1.00 59.94           N  
ANISOU  687  N   SER A  96     7212   7839   7722    756    520    164       N  
ATOM    688  CA  SER A  96     -30.204   6.012   3.847  1.00 66.51           C  
ANISOU  688  CA  SER A  96     8038   8567   8664    768    610    187       C  
ATOM    689  C   SER A  96     -31.367   6.118   2.856  1.00 66.13           C  
ANISOU  689  C   SER A  96     7983   8441   8703    690    615    114       C  
ATOM    690  O   SER A  96     -32.109   5.178   2.749  1.00 79.82           O  
ANISOU  690  O   SER A  96     9710  10085  10532    694    693    124       O  
ATOM    691  CB  SER A  96     -30.681   5.374   5.154  1.00 71.30           C  
ANISOU  691  CB  SER A  96     8661   9151   9275    847    692    276       C  
ATOM    692  OG  SER A  96     -31.577   6.256   5.812  1.00 80.04           O  
ANISOU  692  OG  SER A  96     9791  10274  10346    835    673    270       O  
ATOM    693  N   THR A  97     -31.491   7.216   2.116  1.00 63.52           N  
ANISOU  693  N   THR A  97     7651   8141   8340    623    537     42       N  
ATOM    694  CA  THR A  97     -32.418   7.324   0.990  1.00 55.46           C  
ANISOU  694  CA  THR A  97     6616   7063   7393    550    531    -33       C  
ATOM    695  C   THR A  97     -31.632   7.753  -0.229  1.00 53.40           C  
ANISOU  695  C   THR A  97     6337   6842   7111    505    463    -94       C  
ATOM    696  O   THR A  97     -30.582   8.294  -0.079  1.00 56.17           O  
ANISOU  696  O   THR A  97     6692   7267   7382    518    411    -83       O  
ATOM    697  CB  THR A  97     -33.499   8.384   1.224  1.00 58.70           C  
ANISOU  697  CB  THR A  97     7042   7479   7781    513    500    -63       C  
ATOM    698  CG2 THR A  97     -32.916   9.730   1.162  1.00 59.43           C  
ANISOU  698  CG2 THR A  97     7155   7664   7762    515    427    -59       C  
ATOM    699  OG1 THR A  97     -34.485   8.301   0.202  1.00 52.58           O  
ANISOU  699  OG1 THR A  97     6248   6677   7052    445    473   -142       O  
ATOM    700  N   HIS A  98     -32.140   7.532  -1.430  1.00 52.57           N  
ANISOU  700  N   HIS A  98     6209   6691   7071    453    463   -159       N  
ATOM    701  CA  HIS A  98     -31.426   7.977  -2.652  1.00 51.80           C  
ANISOU  701  CA  HIS A  98     6095   6633   6952    412    400   -217       C  
ATOM    702  C   HIS A  98     -31.417   9.520  -2.790  1.00 51.46           C  
ANISOU  702  C   HIS A  98     6065   6656   6829    378    322   -247       C  
ATOM    703  O   HIS A  98     -30.566  10.089  -3.470  1.00 49.40           O  
ANISOU  703  O   HIS A  98     5799   6445   6525    358    267   -275       O  
ATOM    704  CB  HIS A  98     -31.999   7.327  -3.905  1.00 55.91           C  
ANISOU  704  CB  HIS A  98     6585   7098   7560    370    422   -283       C  
ATOM    705  CG  HIS A  98     -33.471   7.530  -4.074  1.00 60.42           C  
ANISOU  705  CG  HIS A  98     7150   7628   8178    336    437   -323       C  
ATOM    706  CD2 HIS A  98     -34.168   8.305  -4.935  1.00 59.30           C  
ANISOU  706  CD2 HIS A  98     6997   7503   8031    287    392   -388       C  
ATOM    707  ND1 HIS A  98     -34.410   6.861  -3.311  1.00 60.11           N  
ANISOU  707  ND1 HIS A  98     7113   7524   8201    355    509   -294       N  
ATOM    708  CE1 HIS A  98     -35.622   7.218  -3.704  1.00 60.42           C  
ANISOU  708  CE1 HIS A  98     7142   7541   8274    315    505   -345       C  
ATOM    709  NE2 HIS A  98     -35.501   8.129  -4.652  1.00 58.23           N  
ANISOU  709  NE2 HIS A  98     6856   7316   7950    277    432   -399       N  
ATOM    710  N   LYS A  99     -32.309  10.199  -2.081  1.00 50.89           N  
ANISOU  710  N   LYS A  99     6014   6584   6737    375    320   -237       N  
ATOM    711  CA  LYS A  99     -32.478  11.652  -2.266  1.00 51.71           C  
ANISOU  711  CA  LYS A  99     6130   6736   6780    340    257   -269       C  
ATOM    712  C   LYS A  99     -31.653  12.472  -1.338  1.00 52.98           C  
ANISOU  712  C   LYS A  99     6311   6965   6853    363    222   -237       C  
ATOM    713  O   LYS A  99     -31.935  12.501  -0.161  1.00 54.31           O  
ANISOU  713  O   LYS A  99     6497   7137   6998    397    244   -194       O  
ATOM    714  CB  LYS A  99     -33.942  12.073  -2.088  1.00 50.73           C  
ANISOU  714  CB  LYS A  99     6014   6577   6682    319    272   -284       C  
ATOM    715  CG  LYS A  99     -34.812  11.605  -3.258  1.00 58.94           C  
ANISOU  715  CG  LYS A  99     7026   7569   7798    282    287   -341       C  
ATOM    716  CD  LYS A  99     -36.265  12.016  -3.107  1.00 64.39           C  
ANISOU  716  CD  LYS A  99     7719   8229   8514    262    300   -358       C  
ATOM    717  CE  LYS A  99     -36.980  11.278  -2.003  1.00 70.61           C  
ANISOU  717  CE  LYS A  99     8517   8963   9346    294    368   -312       C  
ATOM    718  NZ  LYS A  99     -37.833  10.176  -2.550  1.00 82.52           N1+
ANISOU  718  NZ  LYS A  99     9993  10400  10958    280    424   -345       N1+
ATOM    719  N   PHE A 100     -30.702  13.229  -1.905  1.00 50.05           N  
ANISOU  719  N   PHE A 100     5935   6647   6434    341    167   -265       N  
ATOM    720  CA  PHE A 100     -29.861  14.165  -1.149  1.00 46.67           C  
ANISOU  720  CA  PHE A 100     5519   6290   5923    352    127   -253       C  
ATOM    721  C   PHE A 100     -30.394  15.595  -1.270  1.00 43.57           C  
ANISOU  721  C   PHE A 100     5140   5915   5499    311     91   -289       C  
ATOM    722  O   PHE A 100     -29.831  16.452  -1.970  1.00 43.86           O  
ANISOU  722  O   PHE A 100     5170   5983   5510    279     50   -325       O  
ATOM    723  CB  PHE A 100     -28.426  14.070  -1.678  1.00 50.17           C  
ANISOU  723  CB  PHE A 100     5942   6777   6340    354     97   -263       C  
ATOM    724  CG  PHE A 100     -27.743  12.835  -1.244  1.00 53.80           C  
ANISOU  724  CG  PHE A 100     6392   7235   6812    406    131   -217       C  
ATOM    725  CD1 PHE A 100     -27.948  11.636  -1.927  1.00 53.04           C  
ANISOU  725  CD1 PHE A 100     6282   7080   6790    411    173   -214       C  
ATOM    726  CD2 PHE A 100     -26.961  12.836  -0.096  1.00 54.07           C  
ANISOU  726  CD2 PHE A 100     6429   7328   6785    454    127   -175       C  
ATOM    727  CE1 PHE A 100     -27.357  10.465  -1.520  1.00 51.20           C  
ANISOU  727  CE1 PHE A 100     6040   6837   6575    462    215   -167       C  
ATOM    728  CE2 PHE A 100     -26.357  11.659   0.328  1.00 57.78           C  
ANISOU  728  CE2 PHE A 100     6890   7799   7265    511    165   -123       C  
ATOM    729  CZ  PHE A 100     -26.568  10.468  -0.360  1.00 58.14           C  
ANISOU  729  CZ  PHE A 100     6924   7775   7389    516    213   -115       C  
ATOM    730  N   LEU A 101     -31.535  15.819  -0.679  1.00 45.45           N  
ANISOU  730  N   LEU A 101     5395   6125   5748    312    113   -278       N  
ATOM    731  CA  LEU A 101     -32.071  17.183  -0.482  1.00 44.86           C  
ANISOU  731  CA  LEU A 101     5338   6067   5639    283     88   -301       C  
ATOM    732  C   LEU A 101     -31.063  18.141   0.129  1.00 40.13           C  
ANISOU  732  C   LEU A 101     4744   5536   4966    284     51   -306       C  
ATOM    733  O   LEU A 101     -30.589  17.935   1.241  1.00 45.24           O  
ANISOU  733  O   LEU A 101     5396   6220   5573    322     56   -276       O  
ATOM    734  CB  LEU A 101     -33.278  17.157   0.453  1.00 37.91           C  
ANISOU  734  CB  LEU A 101     4478   5156   4770    298    122   -275       C  
ATOM    735  CG  LEU A 101     -34.154  18.418   0.543  1.00 43.21           C  
ANISOU  735  CG  LEU A 101     5166   5825   5424    267    108   -297       C  
ATOM    736  CD1 LEU A 101     -34.726  18.824  -0.834  1.00 43.50           C  
ANISOU  736  CD1 LEU A 101     5191   5837   5498    224     94   -340       C  
ATOM    737  CD2 LEU A 101     -35.315  18.213   1.537  1.00 43.04           C  
ANISOU  737  CD2 LEU A 101     5163   5770   5418    289    148   -265       C  
ATOM    738  N   TYR A 102     -30.726  19.201  -0.607  1.00 42.91           N  
ANISOU  738  N   TYR A 102     5093   5908   5302    243     16   -348       N  
ATOM    739  CA  TYR A 102     -29.856  20.253  -0.081  1.00 49.96           C  
ANISOU  739  CA  TYR A 102     5987   6859   6135    234    -14   -366       C  
ATOM    740  C   TYR A 102     -30.559  21.001   1.052  1.00 51.75           C  
ANISOU  740  C   TYR A 102     6236   7094   6331    238     -6   -361       C  
ATOM    741  O   TYR A 102     -31.721  21.392   0.907  1.00 44.09           O  
ANISOU  741  O   TYR A 102     5282   6083   5387    221      8   -364       O  
ATOM    742  CB  TYR A 102     -29.452  21.265  -1.160  1.00 50.36           C  
ANISOU  742  CB  TYR A 102     6030   6917   6187    189    -40   -410       C  
ATOM    743  CG  TYR A 102     -28.462  22.247  -0.618  1.00 52.16           C  
ANISOU  743  CG  TYR A 102     6253   7200   6364    177    -65   -434       C  
ATOM    744  CD1 TYR A 102     -27.104  21.881  -0.483  1.00 56.07           C  
ANISOU  744  CD1 TYR A 102     6725   7745   6833    193    -84   -438       C  
ATOM    745  CD2 TYR A 102     -28.865  23.507  -0.165  1.00 52.13           C  
ANISOU  745  CD2 TYR A 102     6264   7201   6341    153    -66   -458       C  
ATOM    746  CE1 TYR A 102     -26.178  22.747   0.058  1.00 54.78           C  
ANISOU  746  CE1 TYR A 102     6550   7638   6625    181   -107   -469       C  
ATOM    747  CE2 TYR A 102     -27.942  24.400   0.381  1.00 51.00           C  
ANISOU  747  CE2 TYR A 102     6111   7109   6156    139    -85   -491       C  
ATOM    748  CZ  TYR A 102     -26.599  24.015   0.478  1.00 59.54           C  
ANISOU  748  CZ  TYR A 102     7165   8242   7212    152   -106   -499       C  
ATOM    749  OH  TYR A 102     -25.657  24.874   0.978  1.00 60.70           O  
ANISOU  749  OH  TYR A 102     7296   8444   7323    135   -125   -541       O  
ATOM    750  N   TYR A 103     -29.832  21.244   2.136  1.00 46.90           N  
ANISOU  750  N   TYR A 103     5620   6538   5661    261    -18   -357       N  
ATOM    751  CA  TYR A 103     -30.269  22.190   3.167  1.00 49.74           C  
ANISOU  751  CA  TYR A 103     5997   6920   5981    258    -18   -367       C  
ATOM    752  C   TYR A 103     -29.179  23.158   3.675  1.00 53.83           C  
ANISOU  752  C   TYR A 103     6501   7509   6442    245    -50   -409       C  
ATOM    753  O   TYR A 103     -27.995  22.813   3.715  1.00 49.06           O  
ANISOU  753  O   TYR A 103     5873   6956   5811    260    -70   -414       O  
ATOM    754  CB  TYR A 103     -30.875  21.434   4.336  1.00 57.06           C  
ANISOU  754  CB  TYR A 103     6938   7847   6895    310     11   -319       C  
ATOM    755  CG  TYR A 103     -29.966  20.431   4.910  1.00 56.14           C  
ANISOU  755  CG  TYR A 103     6805   7776   6748    363     13   -284       C  
ATOM    756  CD1 TYR A 103     -29.876  19.162   4.368  1.00 55.86           C  
ANISOU  756  CD1 TYR A 103     6761   7705   6757    387     35   -249       C  
ATOM    757  CD2 TYR A 103     -29.195  20.742   6.006  1.00 61.84           C  
ANISOU  757  CD2 TYR A 103     7519   8580   7397    393     -4   -288       C  
ATOM    758  CE1 TYR A 103     -29.030  18.212   4.903  1.00 66.00           C  
ANISOU  758  CE1 TYR A 103     8031   9030   8016    443     43   -210       C  
ATOM    759  CE2 TYR A 103     -28.330  19.807   6.559  1.00 67.69           C  
ANISOU  759  CE2 TYR A 103     8242   9373   8103    452     -2   -251       C  
ATOM    760  CZ  TYR A 103     -28.248  18.546   6.020  1.00 72.72           C  
ANISOU  760  CZ  TYR A 103     8873   9969   8786    479     23   -208       C  
ATOM    761  OH  TYR A 103     -27.379  17.635   6.589  1.00 83.24           O  
ANISOU  761  OH  TYR A 103    10189  11354  10085    542     31   -166       O  
ATOM    762  N   ASP A 104     -29.588  24.391   4.004  1.00 48.75           N  
ANISOU  762  N   ASP A 104     5870   6867   5784    213    -51   -443       N  
ATOM    763  CA  ASP A 104     -28.680  25.425   4.513  1.00 49.96           C  
ANISOU  763  CA  ASP A 104     6008   7082   5892    193    -75   -495       C  
ATOM    764  C   ASP A 104     -28.639  25.386   6.058  1.00 50.46           C  
ANISOU  764  C   ASP A 104     6072   7208   5892    233    -76   -489       C  
ATOM    765  O   ASP A 104     -29.601  25.782   6.782  1.00 46.67           O  
ANISOU  765  O   ASP A 104     5616   6714   5403    238    -58   -483       O  
ATOM    766  CB  ASP A 104     -29.131  26.790   3.994  1.00 47.35           C  
ANISOU  766  CB  ASP A 104     5688   6714   5586    137    -68   -537       C  
ATOM    767  CG  ASP A 104     -28.243  27.957   4.464  1.00 55.16           C  
ANISOU  767  CG  ASP A 104     6659   7755   6542    107    -84   -601       C  
ATOM    768  OD1 ASP A 104     -27.411  27.766   5.379  1.00 55.37           O  
ANISOU  768  OD1 ASP A 104     6663   7856   6516    131   -104   -617       O  
ATOM    769  OD2 ASP A 104     -28.396  29.081   3.895  1.00 49.94           O1-
ANISOU  769  OD2 ASP A 104     6002   7060   5910     60    -72   -637       O1-
ATOM    770  N   GLU A 105     -27.492  24.950   6.561  1.00 49.28           N  
ANISOU  770  N   GLU A 105     5894   7135   5695    265    -99   -493       N  
ATOM    771  CA  GLU A 105     -27.304  24.731   8.002  1.00 47.41           C  
ANISOU  771  CA  GLU A 105     5651   6975   5387    318   -103   -483       C  
ATOM    772  C   GLU A 105     -27.460  26.020   8.765  1.00 43.62           C  
ANISOU  772  C   GLU A 105     5172   6529   4872    289   -109   -541       C  
ATOM    773  O   GLU A 105     -27.927  25.999   9.868  1.00 49.11           O  
ANISOU  773  O   GLU A 105     5879   7257   5524    325   -100   -527       O  
ATOM    774  CB  GLU A 105     -25.951  24.047   8.274  1.00 51.96           C  
ANISOU  774  CB  GLU A 105     6190   7635   5917    359   -128   -479       C  
ATOM    775  CG  GLU A 105     -25.957  22.582   7.846  1.00 56.80           C  
ANISOU  775  CG  GLU A 105     6806   8216   6559    405   -109   -406       C  
ATOM    776  CD  GLU A 105     -24.599  21.938   7.819  1.00 62.84           C  
ANISOU  776  CD  GLU A 105     7533   9049   7292    438   -132   -401       C  
ATOM    777  OE1 GLU A 105     -23.757  22.297   8.655  1.00 67.84           O  
ANISOU  777  OE1 GLU A 105     8139   9781   7856    459   -159   -433       O  
ATOM    778  OE2 GLU A 105     -24.371  21.050   6.983  1.00 54.95           O1-
ANISOU  778  OE2 GLU A 105     6531   8009   6336    446   -122   -368       O1-
ATOM    779  N   LYS A 106     -27.172  27.168   8.164  1.00 50.57           N  
ANISOU  779  N   LYS A 106     6044   7393   5777    225   -119   -606       N  
ATOM    780  CA  LYS A 106     -27.301  28.435   8.915  1.00 51.49           C  
ANISOU  780  CA  LYS A 106     6159   7537   5866    194   -119   -669       C  
ATOM    781  C   LYS A 106     -28.744  28.776   9.136  1.00 51.91           C  
ANISOU  781  C   LYS A 106     6254   7526   5943    188    -86   -645       C  
ATOM    782  O   LYS A 106     -29.038  29.499  10.031  1.00 54.11           O  
ANISOU  782  O   LYS A 106     6538   7832   6189    184    -81   -678       O  
ATOM    783  CB  LYS A 106     -26.595  29.585   8.232  1.00 54.83           C  
ANISOU  783  CB  LYS A 106     6561   7953   6319    127   -126   -744       C  
ATOM    784  CG  LYS A 106     -25.096  29.281   8.015  1.00 66.72           C  
ANISOU  784  CG  LYS A 106     8020   9527   7803    130   -159   -774       C  
ATOM    785  CD  LYS A 106     -24.323  30.345   7.236  1.00 75.73           C  
ANISOU  785  CD  LYS A 106     9136  10653   8982     63   -161   -845       C  
ATOM    786  CE  LYS A 106     -24.727  30.379   5.759  1.00 89.12           C  
ANISOU  786  CE  LYS A 106    10855  12252  10754     32   -139   -813       C  
ATOM    787  NZ  LYS A 106     -24.438  31.671   5.057  1.00 97.87           N1+
ANISOU  787  NZ  LYS A 106    11954  13320  11909    -32   -120   -872       N1+
ATOM    788  N   LYS A 107     -29.652  28.227   8.339  1.00 49.37           N  
ANISOU  788  N   LYS A 107     5959   7121   5675    190    -64   -590       N  
ATOM    789  CA  LYS A 107     -31.069  28.493   8.521  1.00 48.42           C  
ANISOU  789  CA  LYS A 107     5876   6939   5580    186    -32   -565       C  
ATOM    790  C   LYS A 107     -31.780  27.511   9.476  1.00 45.89           C  
ANISOU  790  C   LYS A 107     5573   6628   5233    249    -15   -503       C  
ATOM    791  O   LYS A 107     -32.997  27.643   9.716  1.00 51.22           O  
ANISOU  791  O   LYS A 107     6278   7254   5929    251     13   -478       O  
ATOM    792  CB  LYS A 107     -31.763  28.542   7.142  1.00 42.40           C  
ANISOU  792  CB  LYS A 107     5129   6088   4893    152    -16   -546       C  
ATOM    793  CG  LYS A 107     -31.476  29.837   6.374  1.00 43.98           C  
ANISOU  793  CG  LYS A 107     5323   6265   5121     92    -15   -601       C  
ATOM    794  CD  LYS A 107     -31.937  29.774   4.939  1.00 41.55           C  
ANISOU  794  CD  LYS A 107     5023   5888   4874     70     -4   -580       C  
ATOM    795  CE  LYS A 107     -31.768  31.089   4.252  1.00 43.23           C  
ANISOU  795  CE  LYS A 107     5233   6074   5114     20      7   -623       C  
ATOM    796  NZ  LYS A 107     -32.160  31.009   2.802  1.00 48.59           N1+
ANISOU  796  NZ  LYS A 107     5917   6698   5845      8     16   -599       N1+
ATOM    797  N   MET A 108     -31.076  26.503   9.970  1.00 52.37           N  
ANISOU  797  N   MET A 108     6377   7507   6015    303    -26   -472       N  
ATOM    798  CA  MET A 108     -31.750  25.444  10.764  1.00 57.59           C  
ANISOU  798  CA  MET A 108     7056   8166   6660    369      1   -401       C  
ATOM    799  C   MET A 108     -32.154  25.910  12.171  1.00 64.65           C  
ANISOU  799  C   MET A 108     7961   9110   7491    399      9   -407       C  
ATOM    800  O   MET A 108     -33.127  25.430  12.745  1.00 62.85           O  
ANISOU  800  O   MET A 108     7759   8853   7267    437     43   -354       O  
ATOM    801  CB  MET A 108     -30.844  24.233  10.899  1.00 63.54           C  
ANISOU  801  CB  MET A 108     7787   8967   7388    426     -6   -360       C  
ATOM    802  CG  MET A 108     -30.656  23.466   9.603  1.00 63.33           C  
ANISOU  802  CG  MET A 108     7753   8880   7428    410     -3   -338       C  
ATOM    803  SD  MET A 108     -29.517  22.095   9.834  1.00 64.98           S  
ANISOU  803  SD  MET A 108     7934   9148   7605    479     -7   -291       S  
ATOM    804  CE  MET A 108     -30.456  20.930  10.838  1.00 63.97           C  
ANISOU  804  CE  MET A 108     7831   8999   7474    560     47   -200       C  
ATOM    805  N   ALA A 109     -31.400  26.851  12.721  1.00 68.42           N  
ANISOU  805  N   ALA A 109     8417   9663   7914    381    -18   -475       N  
ATOM    806  CA  ALA A 109     -31.746  27.429  14.014  1.00 71.51           C  
ANISOU  806  CA  ALA A 109     8816  10108   8243    403    -13   -495       C  
ATOM    807  C   ALA A 109     -33.175  27.943  14.041  1.00 69.53           C  
ANISOU  807  C   ALA A 109     8605   9777   8034    380     21   -482       C  
ATOM    808  O   ALA A 109     -33.895  27.695  15.006  1.00 71.75           O  
ANISOU  808  O   ALA A 109     8907  10069   8284    425     45   -446       O  
ATOM    809  CB  ALA A 109     -30.776  28.550  14.359  1.00 71.67           C  
ANISOU  809  CB  ALA A 109     8804  10209   8218    367    -47   -591       C  
ATOM    810  N   ASN A 110     -33.594  28.629  12.976  1.00 69.18           N  
ANISOU  810  N   ASN A 110     8572   9652   8059    314     28   -507       N  
ATOM    811  CA  ASN A 110     -35.009  29.096  12.835  1.00 67.38           C  
ANISOU  811  CA  ASN A 110     8380   9341   7879    291     63   -491       C  
ATOM    812  C   ASN A 110     -36.095  28.070  12.521  1.00 61.14           C  
ANISOU  812  C   ASN A 110     7614   8478   7138    320     95   -412       C  
ATOM    813  O   ASN A 110     -37.287  28.398  12.507  1.00 56.59           O  
ANISOU  813  O   ASN A 110     7064   7841   6596    307    124   -397       O  
ATOM    814  CB  ASN A 110     -35.091  30.156  11.745  1.00 63.97           C  
ANISOU  814  CB  ASN A 110     7949   8851   7503    218     62   -537       C  
ATOM    815  CG  ASN A 110     -34.334  31.408  12.119  1.00 71.88           C  
ANISOU  815  CG  ASN A 110     8932   9903   8474    179     47   -622       C  
ATOM    816  ND2 ASN A 110     -33.662  31.996  11.158  1.00 64.41           N  
ANISOU  816  ND2 ASN A 110     7969   8940   7563    129     36   -664       N  
ATOM    817  OD1 ASN A 110     -34.356  31.844  13.274  1.00 77.83           O  
ANISOU  817  OD1 ASN A 110     9687  10711   9174    194     48   -651       O  
ATOM    818  N   PHE A 111     -35.691  26.859  12.177  1.00 58.80           N  
ANISOU  818  N   PHE A 111     7305   8182   6852    354     93   -367       N  
ATOM    819  CA  PHE A 111     -36.660  25.826  11.876  1.00 62.67           C  
ANISOU  819  CA  PHE A 111     7811   8601   7397    379    129   -301       C  
ATOM    820  C   PHE A 111     -36.251  24.585  12.630  1.00 59.53           C  
ANISOU  820  C   PHE A 111     7407   8246   6965    453    142   -244       C  
ATOM    821  O   PHE A 111     -35.840  23.591  12.052  1.00 58.46           O  
ANISOU  821  O   PHE A 111     7257   8095   6858    469    144   -214       O  
ATOM    822  CB  PHE A 111     -36.765  25.587  10.344  1.00 56.19           C  
ANISOU  822  CB  PHE A 111     6983   7714   6653    337    124   -304       C  
ATOM    823  CG  PHE A 111     -37.455  26.691   9.622  1.00 51.02           C  
ANISOU  823  CG  PHE A 111     6339   7009   6036    278    125   -341       C  
ATOM    824  CD1 PHE A 111     -36.823  27.915   9.440  1.00 51.77           C  
ANISOU  824  CD1 PHE A 111     6426   7131   6110    235    101   -401       C  
ATOM    825  CD2 PHE A 111     -38.759  26.523   9.122  1.00 46.31           C  
ANISOU  825  CD2 PHE A 111     5758   6337   5499    268    154   -315       C  
ATOM    826  CE1 PHE A 111     -37.489  28.961   8.793  1.00 52.78           C  
ANISOU  826  CE1 PHE A 111     6566   7210   6275    188    111   -427       C  
ATOM    827  CE2 PHE A 111     -39.412  27.551   8.490  1.00 44.05           C  
ANISOU  827  CE2 PHE A 111     5480   6011   5243    223    157   -343       C  
ATOM    828  CZ  PHE A 111     -38.791  28.773   8.330  1.00 47.92           C  
ANISOU  828  CZ  PHE A 111     5967   6527   5711    185    138   -395       C  
ATOM    829  N   GLN A 112     -36.406  24.679  13.940  1.00 65.03           N  
ANISOU  829  N   GLN A 112     8113   8994   7598    499    154   -229       N  
ATOM    830  CA  GLN A 112     -36.090  23.610  14.903  1.00 67.82           C  
ANISOU  830  CA  GLN A 112     8464   9401   7904    584    174   -168       C  
ATOM    831  C   GLN A 112     -36.679  22.265  14.522  1.00 63.99           C  
ANISOU  831  C   GLN A 112     7986   8839   7486    617    221    -93       C  
ATOM    832  O   GLN A 112     -36.071  21.215  14.783  1.00 68.69           O  
ANISOU  832  O   GLN A 112     8569   9465   8065    676    235    -44       O  
ATOM    833  CB  GLN A 112     -36.633  24.011  16.284  1.00 83.25           C  
ANISOU  833  CB  GLN A 112    10436  11399   9794    625    192   -158       C  
ATOM    834  CG  GLN A 112     -35.617  23.965  17.421  1.00 99.48           C  
ANISOU  834  CG  GLN A 112    12471  13583  11743    687    170   -163       C  
ATOM    835  CD  GLN A 112     -34.462  24.932  17.219  1.00 98.86           C  
ANISOU  835  CD  GLN A 112    12361  13579  11621    641    111   -253       C  
ATOM    836  NE2 GLN A 112     -33.244  24.443  17.410  1.00106.70           N  
ANISOU  836  NE2 GLN A 112    13320  14658  12560    680     83   -254       N  
ATOM    837  OE1 GLN A 112     -34.661  26.096  16.893  1.00 91.41           O  
ANISOU  837  OE1 GLN A 112    11421  12614  10696    572     94   -322       O  
ATOM    838  N   ASN A 113     -37.869  22.269  13.924  1.00 64.69           N  
ANISOU  838  N   ASN A 113     8093   8831   7653    581    250    -84       N  
ATOM    839  CA  ASN A 113     -38.494  21.011  13.513  1.00 70.80           C  
ANISOU  839  CA  ASN A 113     8869   9527   8502    604    300    -25       C  
ATOM    840  C   ASN A 113     -38.052  20.444  12.152  1.00 66.99           C  
ANISOU  840  C   ASN A 113     8365   9003   8085    569    287    -38       C  
ATOM    841  O   ASN A 113     -38.638  19.474  11.709  1.00 63.09           O  
ANISOU  841  O   ASN A 113     7869   8437   7663    578    328     -3       O  
ATOM    842  CB  ASN A 113     -40.022  21.123  13.582  1.00 76.49           C  
ANISOU  842  CB  ASN A 113     9613  10167   9279    590    343     -8       C  
ATOM    843  CG  ASN A 113     -40.542  21.169  15.020  1.00 84.65           C  
ANISOU  843  CG  ASN A 113    10670  11231  10262    647    377     32       C  
ATOM    844  ND2 ASN A 113     -41.843  21.383  15.155  1.00 83.43           N  
ANISOU  844  ND2 ASN A 113    10535  11011  10150    634    413     44       N  
ATOM    845  OD1 ASN A 113     -39.792  20.999  15.996  1.00 82.89           O  
ANISOU  845  OD1 ASN A 113    10444  11089   9958    707    373     54       O  
ATOM    846  N   PHE A 114     -37.027  21.021  11.509  1.00 61.21           N  
ANISOU  846  N   PHE A 114     7614   8314   7328    532    233    -91       N  
ATOM    847  CA  PHE A 114     -36.502  20.468  10.260  1.00 57.19           C  
ANISOU  847  CA  PHE A 114     7083   7774   6870    505    220   -103       C  
ATOM    848  C   PHE A 114     -35.502  19.369  10.578  1.00 61.73           C  
ANISOU  848  C   PHE A 114     7641   8390   7422    564    228    -61       C  
ATOM    849  O   PHE A 114     -34.475  19.629  11.237  1.00 58.66           O  
ANISOU  849  O   PHE A 114     7242   8091   6955    593    199    -68       O  
ATOM    850  CB  PHE A 114     -35.776  21.512   9.413  1.00 55.52           C  
ANISOU  850  CB  PHE A 114     6858   7590   6645    444    165   -172       C  
ATOM    851  CG  PHE A 114     -35.145  20.915   8.146  1.00 58.70           C  
ANISOU  851  CG  PHE A 114     7237   7969   7094    422    150   -182       C  
ATOM    852  CD1 PHE A 114     -35.949  20.318   7.169  1.00 54.64           C  
ANISOU  852  CD1 PHE A 114     6722   7376   6661    401    175   -175       C  
ATOM    853  CD2 PHE A 114     -33.756  20.901   7.952  1.00 61.45           C  
ANISOU  853  CD2 PHE A 114     7563   8379   7404    425    114   -202       C  
ATOM    854  CE1 PHE A 114     -35.403  19.753   6.019  1.00 55.67           C  
ANISOU  854  CE1 PHE A 114     6830   7488   6831    383    163   -188       C  
ATOM    855  CE2 PHE A 114     -33.200  20.340   6.784  1.00 59.88           C  
ANISOU  855  CE2 PHE A 114     7345   8158   7248    407    104   -210       C  
ATOM    856  CZ  PHE A 114     -34.021  19.753   5.831  1.00 58.27           C  
ANISOU  856  CZ  PHE A 114     7141   7875   7123    387    129   -203       C  
ATOM    857  N   LYS A 115     -35.779  18.148  10.116  1.00 66.32           N  
ANISOU  857  N   LYS A 115     8217   8909   8071    584    270    -19       N  
ATOM    858  CA  LYS A 115     -34.889  17.025  10.416  1.00 63.83           C  
ANISOU  858  CA  LYS A 115     7887   8622   7741    646    290     29       C  
ATOM    859  C   LYS A 115     -34.302  16.478   9.162  1.00 64.66           C  
ANISOU  859  C   LYS A 115     7969   8697   7900    616    278     10       C  
ATOM    860  O   LYS A 115     -34.937  15.675   8.481  1.00 63.63           O  
ANISOU  860  O   LYS A 115     7836   8485   7853    604    317     22       O  
ATOM    861  CB  LYS A 115     -35.587  15.924  11.223  1.00 71.15           C  
ANISOU  861  CB  LYS A 115     8827   9508   8696    714    366    108       C  
ATOM    862  CG  LYS A 115     -35.699  16.307  12.693  1.00 87.85           C  
ANISOU  862  CG  LYS A 115    10960  11690  10728    771    375    141       C  
ATOM    863  CD  LYS A 115     -34.326  16.662  13.319  1.00 98.29           C  
ANISOU  863  CD  LYS A 115    12265  13135  11943    808    326    131       C  
ATOM    864  CE  LYS A 115     -34.394  17.809  14.336  1.00 99.57           C  
ANISOU  864  CE  LYS A 115    12438  13377  12016    813    294    101       C  
ATOM    865  NZ  LYS A 115     -35.390  17.499  15.399  1.00104.35           N1+
ANISOU  865  NZ  LYS A 115    13069  13964  12614    869    353    161       N1+
ATOM    866  N   PRO A 116     -33.057  16.884   8.862  1.00 64.30           N  
ANISOU  866  N   PRO A 116     7905   8720   7805    603    224    -24       N  
ATOM    867  CA  PRO A 116     -32.460  16.534   7.559  1.00 64.28           C  
ANISOU  867  CA  PRO A 116     7881   8692   7850    567    206    -51       C  
ATOM    868  C   PRO A 116     -32.371  15.043   7.389  1.00 57.08           C  
ANISOU  868  C   PRO A 116     6960   7736   6992    611    258      1       C  
ATOM    869  O   PRO A 116     -31.997  14.363   8.311  1.00 61.91           O  
ANISOU  869  O   PRO A 116     7571   8379   7571    681    288     59       O  
ATOM    870  CB  PRO A 116     -31.066  17.158   7.615  1.00 70.72           C  
ANISOU  870  CB  PRO A 116     8678   9600   8593    563    148    -85       C  
ATOM    871  CG  PRO A 116     -30.892  17.749   8.985  1.00 69.22           C  
ANISOU  871  CG  PRO A 116     8494   9490   8316    602    137    -78       C  
ATOM    872  CD  PRO A 116     -32.075  17.419   9.828  1.00 72.60           C  
ANISOU  872  CD  PRO A 116     8949   9879   8756    638    189    -29       C  
ATOM    873  N   ARG A 117     -32.724  14.520   6.233  1.00 61.46           N  
ANISOU  873  N   ARG A 117     7505   8217   7630    573    273    -17       N  
ATOM    874  CA  ARG A 117     -32.494  13.082   5.981  1.00 62.64           C  
ANISOU  874  CA  ARG A 117     7641   8323   7837    611    325     25       C  
ATOM    875  C   ARG A 117     -31.025  12.728   5.626  1.00 61.80           C  
ANISOU  875  C   ARG A 117     7512   8269   7700    628    297     25       C  
ATOM    876  O   ARG A 117     -30.694  11.561   5.527  1.00 62.93           O  
ANISOU  876  O   ARG A 117     7643   8383   7883    667    342     65       O  
ATOM    877  CB  ARG A 117     -33.434  12.576   4.893  1.00 70.30           C  
ANISOU  877  CB  ARG A 117     8603   9197   8910    565    355     -2       C  
ATOM    878  CG  ARG A 117     -34.937  12.702   5.240  1.00 78.16           C  
ANISOU  878  CG  ARG A 117     9615  10132   9948    553    394      1       C  
ATOM    879  CD  ARG A 117     -35.661  11.388   4.975  1.00 89.18           C  
ANISOU  879  CD  ARG A 117    11000  11437  11448    566    472     24       C  
ATOM    880  NE  ARG A 117     -35.098  10.331   5.839  1.00 94.23           N  
ANISOU  880  NE  ARG A 117    11641  12077  12083    643    529    100       N  
ATOM    881  CZ  ARG A 117     -34.918   9.056   5.492  1.00 95.43           C  
ANISOU  881  CZ  ARG A 117    11777  12173  12309    665    588    124       C  
ATOM    882  NH1 ARG A 117     -34.406   8.195   6.372  1.00 95.52           N1+
ANISOU  882  NH1 ARG A 117    11792  12191  12308    744    643    202       N1+
ATOM    883  NH2 ARG A 117     -35.248   8.631   4.275  1.00 92.15           N  
ANISOU  883  NH2 ARG A 117    11337  11695  11977    613    596     70       N  
ATOM    884  N   SER A 118     -30.156  13.716   5.409  1.00 54.11           N  
ANISOU  884  N   SER A 118     6528   7366   6663    599    229    -19       N  
ATOM    885  CA  SER A 118     -28.794  13.441   5.004  1.00 58.59           C  
ANISOU  885  CA  SER A 118     7072   7982   7206    610    201    -24       C  
ATOM    886  C   SER A 118     -27.902  14.188   6.011  1.00 61.00           C  
ANISOU  886  C   SER A 118     7372   8396   7407    640    158    -25       C  
ATOM    887  O   SER A 118     -28.342  15.200   6.577  1.00 55.04           O  
ANISOU  887  O   SER A 118     6631   7668   6611    622    136    -49       O  
ATOM    888  CB  SER A 118     -28.571  13.873   3.546  1.00 51.74           C  
ANISOU  888  CB  SER A 118     6192   7091   6375    538    162    -89       C  
ATOM    889  OG  SER A 118     -28.402  15.271   3.492  1.00 57.87           O  
ANISOU  889  OG  SER A 118     6970   7913   7102    494    107   -141       O  
ATOM    890  N   ASN A 119     -26.702  13.644   6.270  1.00 61.71           N  
ANISOU  890  N   ASN A 119     7441   8548   7458    688    152      0       N  
ATOM    891  CA  ASN A 119     -25.763  14.165   7.297  1.00 64.80           C  
ANISOU  891  CA  ASN A 119     7817   9055   7747    729    114      1       C  
ATOM    892  C   ASN A 119     -24.473  14.452   6.634  1.00 53.27           C  
ANISOU  892  C   ASN A 119     6326   7647   6264    704     64    -41       C  
ATOM    893  O   ASN A 119     -24.063  13.678   5.803  1.00 62.49           O  
ANISOU  893  O   ASN A 119     7483   8779   7481    703     77    -29       O  
ATOM    894  CB  ASN A 119     -25.470  13.129   8.376  1.00 66.28           C  
ANISOU  894  CB  ASN A 119     8000   9283   7897    830    159     84       C  
ATOM    895  CG  ASN A 119     -26.715  12.465   8.845  1.00 86.35           C  
ANISOU  895  CG  ASN A 119    10571  11748  10487    863    229    142       C  
ATOM    896  ND2 ASN A 119     -26.962  11.231   8.374  1.00 91.01           N  
ANISOU  896  ND2 ASN A 119    11163  12257  11159    884    292    190       N  
ATOM    897  OD1 ASN A 119     -27.491  13.075   9.585  1.00 87.96           O  
ANISOU  897  OD1 ASN A 119    10795  11961  10663    863    231    140       O  
ATOM    898  N   ARG A 120     -23.833  15.532   7.031  1.00 53.04           N  
ANISOU  898  N   ARG A 120     6282   7705   6165    686     10    -92       N  
ATOM    899  CA  ARG A 120     -22.541  15.930   6.497  1.00 58.24           C  
ANISOU  899  CA  ARG A 120     6906   8421   6798    660    -39   -139       C  
ATOM    900  C   ARG A 120     -21.464  15.499   7.453  1.00 62.34           C  
ANISOU  900  C   ARG A 120     7395   9050   7238    737    -49   -109       C  
ATOM    901  O   ARG A 120     -21.567  15.777   8.634  1.00 66.12           O  
ANISOU  901  O   ARG A 120     7875   9599   7649    779    -53    -98       O  
ATOM    902  CB  ARG A 120     -22.485  17.437   6.359  1.00 58.14           C  
ANISOU  902  CB  ARG A 120     6891   8436   6763    590    -86   -221       C  
ATOM    903  CG  ARG A 120     -21.184  17.998   5.805  1.00 58.40           C  
ANISOU  903  CG  ARG A 120     6887   8525   6776    555   -133   -279       C  
ATOM    904  CD  ARG A 120     -21.295  19.491   5.601  1.00 57.08           C  
ANISOU  904  CD  ARG A 120     6720   8362   6605    482   -165   -358       C  
ATOM    905  NE  ARG A 120     -21.665  20.166   6.842  1.00 59.01           N  
ANISOU  905  NE  ARG A 120     6969   8661   6790    497   -171   -374       N  
ATOM    906  CZ  ARG A 120     -20.800  20.557   7.776  1.00 67.62           C  
ANISOU  906  CZ  ARG A 120     8026   9862   7802    523   -201   -406       C  
ATOM    907  NH1 ARG A 120     -19.477  20.359   7.636  1.00 72.73           N1+
ANISOU  907  NH1 ARG A 120     8631  10581   8423    536   -230   -424       N1+
ATOM    908  NH2 ARG A 120     -21.249  21.142   8.870  1.00 65.72           N  
ANISOU  908  NH2 ARG A 120     7791   9668   7510    537   -204   -422       N  
ATOM    909  N   GLU A 121     -20.458  14.809   6.930  1.00 62.66           N  
ANISOU  909  N   GLU A 121     7411   9109   7289    756    -53    -94       N  
ATOM    910  CA  GLU A 121     -19.275  14.429   7.658  1.00 60.35           C  
ANISOU  910  CA  GLU A 121     7082   8927   6921    826    -70    -71       C  
ATOM    911  C   GLU A 121     -18.062  14.991   6.915  1.00 65.09           C  
ANISOU  911  C   GLU A 121     7644   9573   7512    778   -123   -137       C  
ATOM    912  O   GLU A 121     -17.905  14.784   5.699  1.00 53.82           O  
ANISOU  912  O   GLU A 121     6219   8077   6153    732   -121   -151       O  
ATOM    913  CB  GLU A 121     -19.189  12.917   7.715  1.00 68.02           C  
ANISOU  913  CB  GLU A 121     8056   9868   7919    904    -12     20       C  
ATOM    914  CG  GLU A 121     -17.980  12.426   8.516  1.00 79.96           C  
ANISOU  914  CG  GLU A 121     9529  11502   9350    991    -23     58       C  
ATOM    915  CD  GLU A 121     -18.020  10.951   8.874  1.00 78.01           C  
ANISOU  915  CD  GLU A 121     9289  11231   9119   1087     46    164       C  
ATOM    916  OE1 GLU A 121     -18.971  10.227   8.477  1.00 81.76           O  
ANISOU  916  OE1 GLU A 121     9798  11588   9679   1083    108    207       O  
ATOM    917  OE2 GLU A 121     -17.069  10.531   9.543  1.00 74.98           O1-
ANISOU  917  OE2 GLU A 121     8873  10949   8665   1167     41    202       O1-
ATOM    918  N   GLU A 122     -17.217  15.738   7.624  1.00 61.24           N  
ANISOU  918  N   GLU A 122     7121   9202   6943    787   -171   -184       N  
ATOM    919  CA  GLU A 122     -15.967  16.186   7.045  1.00 57.26           C  
ANISOU  919  CA  GLU A 122     6574   8751   6428    751   -216   -243       C  
ATOM    920  C   GLU A 122     -14.948  15.066   7.141  1.00 63.66           C  
ANISOU  920  C   GLU A 122     7355   9617   7216    826   -208   -187       C  
ATOM    921  O   GLU A 122     -14.847  14.374   8.162  1.00 63.89           O  
ANISOU  921  O   GLU A 122     7375   9711   7186    917   -189   -125       O  
ATOM    922  CB  GLU A 122     -15.442  17.431   7.736  1.00 61.00           C  
ANISOU  922  CB  GLU A 122     7015   9328   6833    725   -267   -326       C  
ATOM    923  CG  GLU A 122     -16.425  18.602   7.714  1.00 59.04           C  
ANISOU  923  CG  GLU A 122     6796   9028   6607    653   -271   -382       C  
ATOM    924  CD  GLU A 122     -16.706  19.093   6.328  1.00 62.01           C  
ANISOU  924  CD  GLU A 122     7191   9298   7069    565   -268   -418       C  
ATOM    925  OE1 GLU A 122     -15.726  19.537   5.708  1.00 61.87           O  
ANISOU  925  OE1 GLU A 122     7141   9306   7060    525   -297   -470       O  
ATOM    926  OE2 GLU A 122     -17.894  19.049   5.874  1.00 62.25           O1-
ANISOU  926  OE2 GLU A 122     7267   9226   7157    539   -237   -395       O1-
ATOM    927  N   MET A 123     -14.210  14.846   6.069  1.00 61.55           N  
ANISOU  927  N   MET A 123     7071   9321   6993    794   -218   -203       N  
ATOM    928  CA  MET A 123     -13.299  13.735   6.070  1.00 63.38           C  
ANISOU  928  CA  MET A 123     7276   9592   7212    865   -204   -145       C  
ATOM    929  C   MET A 123     -12.343  13.908   4.917  1.00 65.37           C  
ANISOU  929  C   MET A 123     7502   9833   7502    811   -231   -192       C  
ATOM    930  O   MET A 123     -12.624  14.657   3.970  1.00 55.65           O  
ANISOU  930  O   MET A 123     6284   8533   6323    725   -244   -249       O  
ATOM    931  CB  MET A 123     -14.072  12.412   5.975  1.00 62.17           C  
ANISOU  931  CB  MET A 123     7159   9348   7112    918   -134    -51       C  
ATOM    932  CG  MET A 123     -14.549  12.089   4.560  1.00 63.91           C  
ANISOU  932  CG  MET A 123     7407   9437   7439    854   -108    -58       C  
ATOM    933  SD  MET A 123     -15.607  10.616   4.445  1.00 65.19           S  
ANISOU  933  SD  MET A 123     7610   9481   7678    902    -19     34       S  
ATOM    934  CE  MET A 123     -16.903  11.000   5.610  1.00 67.34           C  
ANISOU  934  CE  MET A 123     7914   9749   7920    923      0     55       C  
ATOM    935  N   LYS A 124     -11.212  13.213   5.023  1.00 59.36           N  
ANISOU  935  N   LYS A 124     6702   9141   6709    869   -236   -162       N  
ATOM    936  CA  LYS A 124     -10.181  13.211   4.006  1.00 55.24           C  
ANISOU  936  CA  LYS A 124     6152   8618   6219    833   -257   -195       C  
ATOM    937  C   LYS A 124     -10.564  12.327   2.837  1.00 52.62           C  
ANISOU  937  C   LYS A 124     5852   8163   5979    817   -212   -155       C  
ATOM    938  O   LYS A 124     -11.306  11.349   2.975  1.00 51.05           O  
ANISOU  938  O   LYS A 124     5684   7901   5812    862   -159    -84       O  
ATOM    939  CB  LYS A 124      -8.848  12.639   4.577  1.00 61.80           C  
ANISOU  939  CB  LYS A 124     6927   9570   6982    912   -274   -168       C  
ATOM    940  CG  LYS A 124      -8.384  13.259   5.895  1.00 64.22           C  
ANISOU  940  CG  LYS A 124     7192  10024   7183    952   -315   -199       C  
ATOM    941  CD  LYS A 124      -8.127  14.740   5.686  1.00 67.60           C  
ANISOU  941  CD  LYS A 124     7598  10480   7606    859   -368   -314       C  
ATOM    942  CE  LYS A 124      -7.841  15.522   6.962  1.00 69.70           C  
ANISOU  942  CE  LYS A 124     7823  10883   7776    882   -409   -367       C  
ATOM    943  NZ  LYS A 124      -7.732  16.961   6.546  1.00 68.57           N1+
ANISOU  943  NZ  LYS A 124     7665  10730   7656    776   -445   -481       N1+
ATOM    944  N   PHE A 125      -9.969  12.596   1.680  1.00 49.99           N  
ANISOU  944  N   PHE A 125     5506   7798   5689    758   -231   -200       N  
ATOM    945  CA  PHE A 125     -10.467  11.938   0.467  1.00 54.85           C  
ANISOU  945  CA  PHE A 125     6153   8293   6393    729   -193   -179       C  
ATOM    946  C   PHE A 125     -10.290  10.443   0.638  1.00 59.15           C  
ANISOU  946  C   PHE A 125     6697   8822   6953    810   -143    -94       C  
ATOM    947  O   PHE A 125     -11.176   9.670   0.304  1.00 54.35           O  
ANISOU  947  O   PHE A 125     6124   8119   6406    817    -91    -54       O  
ATOM    948  CB  PHE A 125      -9.785  12.477  -0.775  1.00 54.72           C  
ANISOU  948  CB  PHE A 125     6120   8256   6413    660   -220   -239       C  
ATOM    949  CG  PHE A 125     -10.492  12.111  -2.046  1.00 56.21           C  
ANISOU  949  CG  PHE A 125     6343   8327   6686    616   -190   -238       C  
ATOM    950  CD1 PHE A 125     -10.206  10.928  -2.698  1.00 57.69           C  
ANISOU  950  CD1 PHE A 125     6530   8471   6919    646   -154   -196       C  
ATOM    951  CD2 PHE A 125     -11.504  12.933  -2.572  1.00 54.81           C  
ANISOU  951  CD2 PHE A 125     6197   8085   6541    550   -193   -280       C  
ATOM    952  CE1 PHE A 125     -10.866  10.580  -3.880  1.00 58.90           C  
ANISOU  952  CE1 PHE A 125     6708   8521   7146    606   -127   -205       C  
ATOM    953  CE2 PHE A 125     -12.165  12.587  -3.739  1.00 51.30           C  
ANISOU  953  CE2 PHE A 125     5778   7546   6168    515   -167   -283       C  
ATOM    954  CZ  PHE A 125     -11.853  11.417  -4.401  1.00 53.39           C  
ANISOU  954  CZ  PHE A 125     6039   7771   6475    541   -136   -250       C  
ATOM    955  N   HIS A 126      -9.152  10.042   1.244  1.00 64.98           N  
ANISOU  955  N   HIS A 126     7395   9660   7633    877   -154    -65       N  
ATOM    956  CA  HIS A 126      -8.824   8.622   1.406  1.00 58.79           C  
ANISOU  956  CA  HIS A 126     6606   8868   6862    962   -102     20       C  
ATOM    957  C   HIS A 126      -9.867   7.935   2.287  1.00 57.09           C  
ANISOU  957  C   HIS A 126     6424   8619   6649   1024    -45     94       C  
ATOM    958  O   HIS A 126     -10.258   6.794   2.019  1.00 56.19           O  
ANISOU  958  O   HIS A 126     6331   8422   6596   1059     20    156       O  
ATOM    959  CB  HIS A 126      -7.336   8.406   1.900  1.00 63.81           C  
ANISOU  959  CB  HIS A 126     7185   9631   7427   1026   -130     36       C  
ATOM    960  CG  HIS A 126      -7.142   8.529   3.386  1.00 64.38           C  
ANISOU  960  CG  HIS A 126     7234   9827   7400   1105   -144     64       C  
ATOM    961  CD2 HIS A 126      -6.844   9.597   4.166  1.00 60.98           C  
ANISOU  961  CD2 HIS A 126     6774   9507   6889   1094   -203      6       C  
ATOM    962  ND1 HIS A 126      -7.264   7.453   4.243  1.00 65.88           N  
ANISOU  962  ND1 HIS A 126     7428  10038   7564   1212    -91    163       N  
ATOM    963  CE1 HIS A 126      -7.088   7.864   5.485  1.00 65.27           C  
ANISOU  963  CE1 HIS A 126     7327  10084   7389   1267   -119    166       C  
ATOM    964  NE2 HIS A 126      -6.832   9.161   5.462  1.00 62.22           N  
ANISOU  964  NE2 HIS A 126     6918   9754   6968   1194   -189     67       N  
ATOM    965  N   GLU A 127     -10.336   8.647   3.314  1.00 57.78           N  
ANISOU  965  N   GLU A 127     6516   8764   6673   1034    -67     82       N  
ATOM    966  CA  GLU A 127     -11.441   8.165   4.154  1.00 62.92           C  
ANISOU  966  CA  GLU A 127     7201   9378   7325   1085    -14    145       C  
ATOM    967  C   GLU A 127     -12.740   7.989   3.376  1.00 61.88           C  
ANISOU  967  C   GLU A 127     7118   9102   7292   1025     26    139       C  
ATOM    968  O   GLU A 127     -13.543   7.062   3.639  1.00 64.27           O  
ANISOU  968  O   GLU A 127     7447   9333   7639   1069     96    206       O  
ATOM    969  CB  GLU A 127     -11.670   9.125   5.342  1.00 65.86           C  
ANISOU  969  CB  GLU A 127     7568   9848   7609   1097    -54    120       C  
ATOM    970  CG  GLU A 127     -10.411   9.347   6.178  1.00 70.51           C  
ANISOU  970  CG  GLU A 127     8101  10595   8092   1157   -100    115       C  
ATOM    971  CD  GLU A 127     -10.585  10.316   7.338  1.00 75.20           C  
ANISOU  971  CD  GLU A 127     8683  11293   8595   1168   -142     78       C  
ATOM    972  OE1 GLU A 127     -10.468   9.866   8.474  1.00 81.98           O  
ANISOU  972  OE1 GLU A 127     9529  12239   9380   1266   -126    138       O  
ATOM    973  OE2 GLU A 127     -10.837  11.518   7.147  1.00 74.57           O1-
ANISOU  973  OE2 GLU A 127     8605  11212   8514   1083   -187     -9       O1-
ATOM    974  N   PHE A 128     -12.959   8.887   2.421  1.00 59.22           N  
ANISOU  974  N   PHE A 128     6788   8723   6990    927    -13     58       N  
ATOM    975  CA  PHE A 128     -14.164   8.817   1.597  1.00 55.23           C  
ANISOU  975  CA  PHE A 128     6321   8092   6571    867     17     41       C  
ATOM    976  C   PHE A 128     -14.107   7.550   0.754  1.00 58.49           C  
ANISOU  976  C   PHE A 128     6737   8420   7065    882     74     79       C  
ATOM    977  O   PHE A 128     -15.078   6.781   0.696  1.00 54.05           O  
ANISOU  977  O   PHE A 128     6201   7767   6566    894    136    114       O  
ATOM    978  CB  PHE A 128     -14.308  10.088   0.709  1.00 55.17           C  
ANISOU  978  CB  PHE A 128     6317   8068   6575    766    -37    -50       C  
ATOM    979  CG  PHE A 128     -15.267   9.917  -0.442  1.00 55.72           C  
ANISOU  979  CG  PHE A 128     6415   8022   6734    707    -11    -72       C  
ATOM    980  CD1 PHE A 128     -16.616   9.691  -0.204  1.00 56.47           C  
ANISOU  980  CD1 PHE A 128     6542   8045   6867    705     29    -53       C  
ATOM    981  CD2 PHE A 128     -14.829   9.996  -1.759  1.00 53.78           C  
ANISOU  981  CD2 PHE A 128     6159   7742   6530    655    -27   -115       C  
ATOM    982  CE1 PHE A 128     -17.504   9.554  -1.254  1.00 59.84           C  
ANISOU  982  CE1 PHE A 128     6988   8375   7371    651     49    -81       C  
ATOM    983  CE2 PHE A 128     -15.717   9.858  -2.805  1.00 56.29           C  
ANISOU  983  CE2 PHE A 128     6499   7967   6921    605     -6   -141       C  
ATOM    984  CZ  PHE A 128     -17.056   9.634  -2.555  1.00 59.99           C  
ANISOU  984  CZ  PHE A 128     6996   8371   7427    603     30   -126       C  
ATOM    985  N   VAL A 129     -12.950   7.306   0.140  1.00 59.40           N  
ANISOU  985  N   VAL A 129     6823   8565   7178    884     56     69       N  
ATOM    986  CA  VAL A 129     -12.795   6.094  -0.659  1.00 62.88           C  
ANISOU  986  CA  VAL A 129     7264   8930   7695    900    111    102       C  
ATOM    987  C   VAL A 129     -12.887   4.828   0.184  1.00 63.17           C  
ANISOU  987  C   VAL A 129     7304   8953   7741    997    186    198       C  
ATOM    988  O   VAL A 129     -13.521   3.872  -0.224  1.00 61.41           O  
ANISOU  988  O   VAL A 129     7100   8630   7603   1003    255    225       O  
ATOM    989  CB  VAL A 129     -11.469   6.055  -1.423  1.00 62.80           C  
ANISOU  989  CB  VAL A 129     7221   8960   7678    891     79     78       C  
ATOM    990  CG1 VAL A 129     -11.518   4.904  -2.415  1.00 67.64           C  
ANISOU  990  CG1 VAL A 129     7840   9478   8382    890    137     96       C  
ATOM    991  CG2 VAL A 129     -11.233   7.372  -2.153  1.00 68.50           C  
ANISOU  991  CG2 VAL A 129     7936   9707   8384    804      8     -9       C  
ATOM    992  N   GLU A 130     -12.264   4.831   1.357  1.00 68.93           N  
ANISOU  992  N   GLU A 130     8015   9787   8386   1075    177    246       N  
ATOM    993  CA  GLU A 130     -12.407   3.703   2.335  1.00 71.65           C  
ANISOU  993  CA  GLU A 130     8365  10130   8728   1181    254    350       C  
ATOM    994  C   GLU A 130     -13.856   3.455   2.674  1.00 62.48           C  
ANISOU  994  C   GLU A 130     7242   8878   7618   1179    311    374       C  
ATOM    995  O   GLU A 130     -14.329   2.347   2.612  1.00 67.88           O  
ANISOU  995  O   GLU A 130     7941   9473   8376   1215    396    430       O  
ATOM    996  CB  GLU A 130     -11.631   3.991   3.658  1.00 73.79           C  
ANISOU  996  CB  GLU A 130     8608  10549   8880   1266    222    390       C  
ATOM    997  CG  GLU A 130     -10.184   3.493   3.694  1.00 76.53           C  
ANISOU  997  CG  GLU A 130     8912  10981   9184   1329    213    423       C  
ATOM    998  CD  GLU A 130      -9.182   4.504   4.259  1.00 78.08           C  
ANISOU  998  CD  GLU A 130     9065  11332   9267   1335    124    377       C  
ATOM    999  OE1 GLU A 130      -9.431   5.116   5.327  1.00 82.23           O  
ANISOU  999  OE1 GLU A 130     9588  11942   9714   1363     97    376       O  
ATOM   1000  OE2 GLU A 130      -8.114   4.680   3.614  1.00 80.66           O1-
ANISOU 1000  OE2 GLU A 130     9359  11700   9587   1310     83    338       O1-
ATOM   1001  N   LYS A 131     -14.569   4.511   3.021  1.00 63.03           N  
ANISOU 1001  N   LYS A 131     7327   8966   7652   1133    267    328       N  
ATOM   1002  CA  LYS A 131     -15.964   4.362   3.503  1.00 65.54           C  
ANISOU 1002  CA  LYS A 131     7681   9210   8008   1135    318    353       C  
ATOM   1003  C   LYS A 131     -16.821   3.795   2.393  1.00 64.20           C  
ANISOU 1003  C   LYS A 131     7531   8901   7960   1076    367    328       C  
ATOM   1004  O   LYS A 131     -17.738   2.976   2.595  1.00 59.14           O  
ANISOU 1004  O   LYS A 131     6910   8171   7387   1100    448    372       O  
ATOM   1005  CB  LYS A 131     -16.489   5.713   3.939  1.00 62.34           C  
ANISOU 1005  CB  LYS A 131     7287   8854   7544   1087    254    296       C  
ATOM   1006  CG  LYS A 131     -17.744   5.678   4.789  1.00 69.70           C  
ANISOU 1006  CG  LYS A 131     8251   9748   8484   1110    298    332       C  
ATOM   1007  CD  LYS A 131     -17.900   7.025   5.476  1.00 72.24           C  
ANISOU 1007  CD  LYS A 131     8575  10155   8718   1085    229    285       C  
ATOM   1008  CE  LYS A 131     -19.261   7.179   6.146  1.00 81.63           C  
ANISOU 1008  CE  LYS A 131     9798  11296   9921   1087    265    304       C  
ATOM   1009  NZ  LYS A 131     -19.171   6.699   7.543  1.00 91.30           N1+
ANISOU 1009  NZ  LYS A 131    11021  12587  11078   1196    304    390       N1+
ATOM   1010  N   LEU A 132     -16.482   4.242   1.194  1.00 64.60           N  
ANISOU 1010  N   LEU A 132     7571   8935   8036    997    319    253       N  
ATOM   1011  CA  LEU A 132     -17.194   3.845   0.020  1.00 67.64           C  
ANISOU 1011  CA  LEU A 132     7968   9207   8525    934    349    211       C  
ATOM   1012  C   LEU A 132     -16.934   2.372  -0.218  1.00 74.05           C  
ANISOU 1012  C   LEU A 132     8772   9953   9410    985    434    267       C  
ATOM   1013  O   LEU A 132     -17.857   1.596  -0.456  1.00 66.37           O  
ANISOU 1013  O   LEU A 132     7813   8876   8528    978    506    277       O  
ATOM   1014  CB  LEU A 132     -16.671   4.665  -1.129  1.00 70.21           C  
ANISOU 1014  CB  LEU A 132     8280   9553   8843    855    277    127       C  
ATOM   1015  CG  LEU A 132     -17.468   4.582  -2.396  1.00 74.71           C  
ANISOU 1015  CG  LEU A 132     8859  10027   9499    780    288     66       C  
ATOM   1016  CD1 LEU A 132     -18.915   4.938  -2.091  1.00 79.93           C  
ANISOU 1016  CD1 LEU A 132     9545  10637  10184    752    303     53       C  
ATOM   1017  CD2 LEU A 132     -16.865   5.573  -3.374  1.00 73.69           C  
ANISOU 1017  CD2 LEU A 132     8717   9938   9342    713    211     -6       C  
ATOM   1018  N   GLN A 133     -15.652   2.007  -0.129  1.00 72.52           N  
ANISOU 1018  N   GLN A 133     8554   9823   9178   1035    426    301       N  
ATOM   1019  CA  GLN A 133     -15.213   0.612  -0.255  1.00 75.55           C  
ANISOU 1019  CA  GLN A 133     8927  10155   9621   1096    509    364       C  
ATOM   1020  C   GLN A 133     -15.831  -0.272   0.764  1.00 73.68           C  
ANISOU 1020  C   GLN A 133     8705   9877   9410   1177    602    454       C  
ATOM   1021  O   GLN A 133     -16.295  -1.348   0.421  1.00 72.39           O  
ANISOU 1021  O   GLN A 133     8548   9607   9349   1187    691    478       O  
ATOM   1022  CB  GLN A 133     -13.712   0.498  -0.119  1.00 73.71           C  
ANISOU 1022  CB  GLN A 133     8664  10018   9324   1149    480    394       C  
ATOM   1023  CG  GLN A 133     -13.059   0.899  -1.412  1.00 85.64           C  
ANISOU 1023  CG  GLN A 133    10158  11530  10850   1074    422    316       C  
ATOM   1024  CD  GLN A 133     -11.561   0.983  -1.305  1.00 91.39           C  
ANISOU 1024  CD  GLN A 133    10853  12361  11509   1115    381    333       C  
ATOM   1025  NE2 GLN A 133     -10.923   1.398  -2.392  1.00 88.41           N  
ANISOU 1025  NE2 GLN A 133    10460  11991  11139   1052    330    266       N  
ATOM   1026  OE1 GLN A 133     -10.981   0.684  -0.260  1.00 98.25           O  
ANISOU 1026  OE1 GLN A 133    11707  13306  12315   1204    395    405       O  
ATOM   1027  N   ASP A 134     -15.826   0.163   2.020  1.00 70.53           N  
ANISOU 1027  N   ASP A 134     8311   9563   8922   1236    586    503       N  
ATOM   1028  CA  ASP A 134     -16.454  -0.631   3.039  1.00 75.67           C  
ANISOU 1028  CA  ASP A 134     8978  10177   9593   1319    678    594       C  
ATOM   1029  C   ASP A 134     -17.906  -0.959   2.624  1.00 75.91           C  
ANISOU 1029  C   ASP A 134     9035  10070   9736   1264    740    568       C  
ATOM   1030  O   ASP A 134     -18.260  -2.121   2.499  1.00 76.55           O  
ANISOU 1030  O   ASP A 134     9119  10051   9914   1294    842    612       O  
ATOM   1031  CB  ASP A 134     -16.409   0.065   4.384  1.00 80.35           C  
ANISOU 1031  CB  ASP A 134     9574  10884  10068   1378    641    633       C  
ATOM   1032  CG  ASP A 134     -17.414  -0.512   5.328  1.00 93.05           C  
ANISOU 1032  CG  ASP A 134    11208  12440  11705   1441    730    710       C  
ATOM   1033  OD1 ASP A 134     -17.225  -1.667   5.768  1.00 97.24           O  
ANISOU 1033  OD1 ASP A 134    11738  12940  12269   1533    826    806       O  
ATOM   1034  OD2 ASP A 134     -18.437   0.156   5.583  1.00102.39           O1-
ANISOU 1034  OD2 ASP A 134    12413  13602  12886   1397    713    677       O1-
ATOM   1035  N   ILE A 135     -18.724   0.066   2.368  1.00 79.30           N  
ANISOU 1035  N   ILE A 135     9479  10494  10157   1182    680    492       N  
ATOM   1036  CA  ILE A 135     -20.113  -0.129   1.959  1.00 74.81           C  
ANISOU 1036  CA  ILE A 135     8929   9808   9687   1125    727    456       C  
ATOM   1037  C   ILE A 135     -20.293  -1.216   0.922  1.00 76.65           C  
ANISOU 1037  C   ILE A 135     9151   9924  10046   1098    799    436       C  
ATOM   1038  O   ILE A 135     -21.132  -2.095   1.099  1.00 66.58           O  
ANISOU 1038  O   ILE A 135     7885   8549   8863   1117    897    468       O  
ATOM   1039  CB  ILE A 135     -20.721   1.166   1.355  1.00 78.91           C  
ANISOU 1039  CB  ILE A 135     9456  10340  10185   1024    638    356       C  
ATOM   1040  CG1 ILE A 135     -21.241   2.065   2.484  1.00 79.20           C  
ANISOU 1040  CG1 ILE A 135     9511  10439  10141   1042    605    374       C  
ATOM   1041  CG2 ILE A 135     -21.866   0.857   0.372  1.00 71.43           C  
ANISOU 1041  CG2 ILE A 135     8513   9273   9353    948    674    293       C  
ATOM   1042  CD1 ILE A 135     -21.346   3.527   2.109  1.00 83.63           C  
ANISOU 1042  CD1 ILE A 135    10075  11055  10644    962    502    289       C  
ATOM   1043  N   GLN A 136     -19.562  -1.117  -0.183  1.00 76.14           N  
ANISOU 1043  N   GLN A 136     9068   9870   9991   1049    752    376       N  
ATOM   1044  CA  GLN A 136     -19.813  -2.011  -1.301  1.00 86.65           C  
ANISOU 1044  CA  GLN A 136    10388  11094  11441   1007    809    335       C  
ATOM   1045  C   GLN A 136     -19.509  -3.437  -0.862  1.00 88.16           C  
ANISOU 1045  C   GLN A 136    10574  11226  11696   1092    925    424       C  
ATOM   1046  O   GLN A 136     -20.349  -4.312  -1.049  1.00 80.93           O  
ANISOU 1046  O   GLN A 136     9660  10196  10894   1085   1019    424       O  
ATOM   1047  CB  GLN A 136     -19.049  -1.594  -2.571  1.00 95.74           C  
ANISOU 1047  CB  GLN A 136    11520  12275  12580    943    734    255       C  
ATOM   1048  CG  GLN A 136     -17.645  -2.151  -2.727  1.00110.32           C  
ANISOU 1048  CG  GLN A 136    13347  14162  14406    992    740    294       C  
ATOM   1049  CD  GLN A 136     -16.695  -1.196  -3.427  1.00121.26           C  
ANISOU 1049  CD  GLN A 136    14719  15635  15718    947    634    236       C  
ATOM   1050  NE2 GLN A 136     -15.398  -1.448  -3.260  1.00119.66           N  
ANISOU 1050  NE2 GLN A 136    14499  15497  15469   1000    624    280       N  
ATOM   1051  OE1 GLN A 136     -17.113  -0.236  -4.099  1.00118.56           O  
ANISOU 1051  OE1 GLN A 136    14380  15304  15361    868    565    155       O  
ATOM   1052  N   GLN A 137     -18.365  -3.632  -0.193  1.00 93.75           N  
ANISOU 1052  N   GLN A 137    11274  12014  12331   1176    923    502       N  
ATOM   1053  CA  GLN A 137     -17.908  -4.945   0.297  1.00 98.44           C  
ANISOU 1053  CA  GLN A 137    11863  12569  12972   1273   1034    602       C  
ATOM   1054  C   GLN A 137     -18.874  -5.598   1.272  1.00 95.23           C  
ANISOU 1054  C   GLN A 137    11475  12091  12616   1332   1141    678       C  
ATOM   1055  O   GLN A 137     -19.190  -6.766   1.123  1.00106.85           O  
ANISOU 1055  O   GLN A 137    12944  13451  14202   1356   1257    711       O  
ATOM   1056  CB  GLN A 137     -16.572  -4.829   1.026  1.00103.04           C  
ANISOU 1056  CB  GLN A 137    12432  13276  13440   1361    999    676       C  
ATOM   1057  CG  GLN A 137     -15.382  -4.470   0.161  1.00108.97           C  
ANISOU 1057  CG  GLN A 137    13159  14093  14150   1326    918    624       C  
ATOM   1058  CD  GLN A 137     -14.160  -4.161   1.007  1.00114.95           C  
ANISOU 1058  CD  GLN A 137    13899  14993  14782   1410    870    688       C  
ATOM   1059  NE2 GLN A 137     -13.274  -3.309   0.483  1.00117.65           N  
ANISOU 1059  NE2 GLN A 137    14245  15360  15095   1522    940    799       N  
ATOM   1060  OE1 GLN A 137     -14.006  -4.686   2.111  1.00113.86           O  
ANISOU 1060  OE1 GLN A 137    13743  14944  14573   1375    774    637       O  
ATOM   1061  N   ARG A 138     -19.318  -4.871   2.287  1.00 83.99           N  
ANISOU 1061  N   ARG A 138    10069  10731  11112   1359   1109    709       N  
ATOM   1062  CA  ARG A 138     -20.345  -5.414   3.171  1.00 89.84           C  
ANISOU 1062  CA  ARG A 138    10829  11400  11904   1408   1209    776       C  
ATOM   1063  C   ARG A 138     -21.740  -5.268   2.529  1.00 85.04           C  
ANISOU 1063  C   ARG A 138    10231  10683  11396   1310   1224    689       C  
ATOM   1064  O   ARG A 138     -22.749  -5.501   3.175  1.00 77.70           O  
ANISOU 1064  O   ARG A 138     9317   9694  10509   1329   1293    724       O  
ATOM   1065  CB  ARG A 138     -20.285  -4.781   4.567  1.00 88.26           C  
ANISOU 1065  CB  ARG A 138    10643  11311  11577   1486   1178    848       C  
ATOM   1066  CG  ARG A 138     -20.836  -3.377   4.639  1.00 98.42           C  
ANISOU 1066  CG  ARG A 138    11943  12660  12790   1413   1069    772       C  
ATOM   1067  CD  ARG A 138     -20.513  -2.686   5.954  1.00101.96           C  
ANISOU 1067  CD  ARG A 138    12399  13242  13100   1489   1023    831       C  
ATOM   1068  NE  ARG A 138     -20.719  -1.249   5.801  1.00101.64           N  
ANISOU 1068  NE  ARG A 138    12362  13271  12984   1407    903    740       N  
ATOM   1069  CZ  ARG A 138     -21.906  -0.660   5.776  1.00108.07           C  
ANISOU 1069  CZ  ARG A 138    13197  14038  13826   1344    891    692       C  
ATOM   1070  NH1 ARG A 138     -23.013  -1.371   5.910  1.00111.84           N1+
ANISOU 1070  NH1 ARG A 138    13690  14399  14403   1350    989    720       N1+
ATOM   1071  NH2 ARG A 138     -21.992   0.654   5.606  1.00112.58           N  
ANISOU 1071  NH2 ARG A 138    13771  14675  14329   1274    785    613       N  
ATOM   1072  N   GLY A 139     -21.776  -4.891   1.252  1.00 84.68           N  
ANISOU 1072  N   GLY A 139    10172  10617  11385   1207   1161    578       N  
ATOM   1073  CA  GLY A 139     -23.030  -4.768   0.504  1.00 91.22           C  
ANISOU 1073  CA  GLY A 139    11000  11353  12304   1113   1169    486       C  
ATOM   1074  C   GLY A 139     -24.092  -3.859   1.105  1.00 86.48           C  
ANISOU 1074  C   GLY A 139    10421  10771  11665   1087   1132    470       C  
ATOM   1075  O   GLY A 139     -25.277  -4.114   0.957  1.00 77.99           O  
ANISOU 1075  O   GLY A 139     9348   9603  10681   1048   1186    438       O  
ATOM   1076  N   GLY A 140     -23.680  -2.789   1.775  1.00 88.80           N  
ANISOU 1076  N   GLY A 140    10728  11184  11828   1106   1042    488       N  
ATOM   1077  CA  GLY A 140     -24.622  -1.970   2.549  1.00 84.86           C  
ANISOU 1077  CA  GLY A 140    10251  10707  11283   1099   1017    490       C  
ATOM   1078  C   GLY A 140     -25.610  -1.169   1.716  1.00 78.62           C  
ANISOU 1078  C   GLY A 140     9462   9885  10524    991    960    382       C  
ATOM   1079  O   GLY A 140     -25.522  -1.130   0.505  1.00 78.61           O  
ANISOU 1079  O   GLY A 140     9443   9859  10566    920    927    300       O  
ATOM   1080  N   GLU A 141     -26.550  -0.529   2.383  1.00 78.14           N  
ANISOU 1080  N   GLU A 141     9421   9830  10438    983    950    385       N  
ATOM   1081  CA  GLU A 141     -27.542   0.290   1.719  1.00 74.20           C  
ANISOU 1081  CA  GLU A 141     8923   9308   9960    891    897    292       C  
ATOM   1082  C   GLU A 141     -27.223   1.792   1.850  1.00 73.84           C  
ANISOU 1082  C   GLU A 141     8889   9375   9791    861    778    257       C  
ATOM   1083  O   GLU A 141     -27.783   2.578   1.104  1.00 67.69           O  
ANISOU 1083  O   GLU A 141     8108   8592   9017    783    720    176       O  
ATOM   1084  CB  GLU A 141     -28.934  -0.023   2.283  1.00 81.11           C  
ANISOU 1084  CB  GLU A 141     9811  10100  10907    894    975    310       C  
ATOM   1085  CG  GLU A 141     -30.031  -0.129   1.231  1.00 89.88           C  
ANISOU 1085  CG  GLU A 141    10905  11123  12123    807    987    216       C  
ATOM   1086  CD  GLU A 141     -29.673  -1.084   0.102  1.00 94.93           C  
ANISOU 1086  CD  GLU A 141    11513  11699  12856    778   1026    170       C  
ATOM   1087  OE1 GLU A 141     -29.576  -2.302   0.341  1.00 90.85           O  
ANISOU 1087  OE1 GLU A 141    10988  11107  12420    826   1131    221       O  
ATOM   1088  OE2 GLU A 141     -29.481  -0.619  -1.036  1.00 95.82           O1-
ANISOU 1088  OE2 GLU A 141    11609  11836  12961    711    954     83       O1-
ATOM   1089  N   GLU A 142     -26.337   2.223   2.757  1.00 67.31           N  
ANISOU 1089  N   GLU A 142     8069   8647   8855    921    740    312       N  
ATOM   1090  CA  GLU A 142     -26.129   3.663   2.881  1.00 65.85           C  
ANISOU 1090  CA  GLU A 142     7892   8558   8567    885    635    269       C  
ATOM   1091  C   GLU A 142     -25.510   4.196   1.598  1.00 64.32           C  
ANISOU 1091  C   GLU A 142     7681   8388   8369    814    560    187       C  
ATOM   1092  O   GLU A 142     -24.898   3.451   0.765  1.00 62.19           O  
ANISOU 1092  O   GLU A 142     7392   8088   8148    808    579    175       O  
ATOM   1093  CB  GLU A 142     -25.387   4.119   4.161  1.00 66.27           C  
ANISOU 1093  CB  GLU A 142     7953   8724   8502    959    607    330       C  
ATOM   1094  CG  GLU A 142     -23.879   4.240   4.073  1.00 70.76           C  
ANISOU 1094  CG  GLU A 142     8501   9386   8997    986    554    336       C  
ATOM   1095  CD  GLU A 142     -23.204   4.916   5.285  1.00 72.64           C  
ANISOU 1095  CD  GLU A 142     8738   9751   9107   1046    509    372       C  
ATOM   1096  OE1 GLU A 142     -22.441   4.251   6.004  1.00 77.44           O  
ANISOU 1096  OE1 GLU A 142     9337  10410   9677   1135    541    447       O  
ATOM   1097  OE2 GLU A 142     -23.357   6.123   5.514  1.00 65.68           O1-
ANISOU 1097  OE2 GLU A 142     7863   8929   8161   1007    439    324       O1-
ATOM   1098  N   ARG A 143     -25.765   5.488   1.429  1.00 57.91           N  
ANISOU 1098  N   ARG A 143     6877   7622   7503    758    482    129       N  
ATOM   1099  CA  ARG A 143     -25.252   6.241   0.314  1.00 57.07           C  
ANISOU 1099  CA  ARG A 143     6758   7546   7379    692    407     54       C  
ATOM   1100  C   ARG A 143     -24.445   7.423   0.735  1.00 51.72           C  
ANISOU 1100  C   ARG A 143     6081   6975   6594    690    328     42       C  
ATOM   1101  O   ARG A 143     -24.757   8.053   1.733  1.00 55.73           O  
ANISOU 1101  O   ARG A 143     6605   7525   7045    710    315     62       O  
ATOM   1102  CB  ARG A 143     -26.394   6.751  -0.545  1.00 55.85           C  
ANISOU 1102  CB  ARG A 143     6607   7338   7274    616    392    -15       C  
ATOM   1103  CG  ARG A 143     -27.027   5.677  -1.385  1.00 54.36           C  
ANISOU 1103  CG  ARG A 143     6404   7051   7196    596    454    -37       C  
ATOM   1104  CD  ARG A 143     -28.407   6.135  -1.768  1.00 57.19           C  
ANISOU 1104  CD  ARG A 143     6768   7364   7597    541    452    -89       C  
ATOM   1105  NE  ARG A 143     -29.138   5.177  -2.567  1.00 51.36           N  
ANISOU 1105  NE  ARG A 143     6009   6536   6966    515    509   -125       N  
ATOM   1106  CZ  ARG A 143     -28.863   4.867  -3.809  1.00 54.74           C  
ANISOU 1106  CZ  ARG A 143     6414   6950   7435    477    497   -183       C  
ATOM   1107  NH1 ARG A 143     -27.830   5.432  -4.478  1.00 60.76           N1+
ANISOU 1107  NH1 ARG A 143     7170   7776   8141    460    431   -209       N1+
ATOM   1108  NH2 ARG A 143     -29.646   3.990  -4.394  1.00 57.85           N  
ANISOU 1108  NH2 ARG A 143     6787   7263   7929    455    555   -220       N  
ATOM   1109  N   LEU A 144     -23.449   7.741  -0.090  1.00 49.80           N  
ANISOU 1109  N   LEU A 144     5819   6771   6330    661    277      3       N  
ATOM   1110  CA  LEU A 144     -22.646   8.884   0.122  1.00 49.58           C  
ANISOU 1110  CA  LEU A 144     5786   6836   6215    648    204    -22       C  
ATOM   1111  C   LEU A 144     -22.657   9.749  -1.111  1.00 45.52           C  
ANISOU 1111  C   LEU A 144     5268   6315   5713    569    152   -100       C  
ATOM   1112  O   LEU A 144     -22.668   9.246  -2.217  1.00 46.87           O  
ANISOU 1112  O   LEU A 144     5428   6436   5943    541    164   -126       O  
ATOM   1113  CB  LEU A 144     -21.201   8.481   0.397  1.00 51.13           C  
ANISOU 1113  CB  LEU A 144     5960   7102   6365    699    193      9       C  
ATOM   1114  CG  LEU A 144     -20.984   7.434   1.473  1.00 57.24           C  
ANISOU 1114  CG  LEU A 144     6733   7887   7128    791    252     96       C  
ATOM   1115  CD1 LEU A 144     -19.524   7.046   1.459  1.00 61.96           C  
ANISOU 1115  CD1 LEU A 144     7302   8551   7686    833    237    119       C  
ATOM   1116  CD2 LEU A 144     -21.392   7.946   2.840  1.00 56.96           C  
ANISOU 1116  CD2 LEU A 144     6711   7904   7023    831    249    129       C  
ATOM   1117  N   TYR A 145     -22.525  11.039  -0.903  1.00 44.01           N  
ANISOU 1117  N   TYR A 145     5080   6180   5460    539     96   -134       N  
ATOM   1118  CA  TYR A 145     -22.345  11.993  -1.962  1.00 49.76           C  
ANISOU 1118  CA  TYR A 145     5803   6914   6188    472     47   -200       C  
ATOM   1119  C   TYR A 145     -21.326  12.999  -1.495  1.00 52.83           C  
ANISOU 1119  C   TYR A 145     6181   7393   6500    470     -4   -218       C  
ATOM   1120  O   TYR A 145     -21.570  13.718  -0.569  1.00 54.53           O  
ANISOU 1120  O   TYR A 145     6406   7646   6666    476    -18   -217       O  
ATOM   1121  CB  TYR A 145     -23.666  12.698  -2.250  1.00 48.79           C  
ANISOU 1121  CB  TYR A 145     5700   6743   6092    425     47   -233       C  
ATOM   1122  CG  TYR A 145     -23.876  13.139  -3.665  1.00 43.91           C  
ANISOU 1122  CG  TYR A 145     5077   6096   5508    366     26   -289       C  
ATOM   1123  CD1 TYR A 145     -22.951  13.890  -4.307  1.00 43.79           C  
ANISOU 1123  CD1 TYR A 145     5045   6111   5482    348     -4   -316       C  
ATOM   1124  CD2 TYR A 145     -25.012  12.799  -4.350  1.00 43.63           C  
ANISOU 1124  CD2 TYR A 145     5053   6008   5513    334     37   -314       C  
ATOM   1125  CE1 TYR A 145     -23.131  14.287  -5.593  1.00 48.12           C  
ANISOU 1125  CE1 TYR A 145     5588   6638   6056    304    -21   -361       C  
ATOM   1126  CE2 TYR A 145     -25.204  13.197  -5.638  1.00 43.95           C  
ANISOU 1126  CE2 TYR A 145     5086   6033   5578    290     18   -362       C  
ATOM   1127  CZ  TYR A 145     -24.258  13.950  -6.250  1.00 44.66           C  
ANISOU 1127  CZ  TYR A 145     5160   6154   5652    276    -10   -384       C  
ATOM   1128  OH  TYR A 145     -24.419  14.357  -7.524  1.00 42.34           O  
ANISOU 1128  OH  TYR A 145     4858   5853   5373    239    -28   -428       O  
ATOM   1129  N   LEU A 146     -20.178  13.049  -2.138  1.00 45.67           N  
ANISOU 1129  N   LEU A 146     5251   6519   5583    460    -31   -238       N  
ATOM   1130  CA  LEU A 146     -19.157  14.031  -1.802  1.00 48.47           C  
ANISOU 1130  CA  LEU A 146     5587   6956   5873    450    -80   -266       C  
ATOM   1131  C   LEU A 146     -19.423  15.275  -2.616  1.00 45.33           C  
ANISOU 1131  C   LEU A 146     5196   6544   5483    381   -110   -327       C  
ATOM   1132  O   LEU A 146     -19.629  15.177  -3.860  1.00 44.09           O  
ANISOU 1132  O   LEU A 146     5041   6337   5374    347   -106   -348       O  
ATOM   1133  CB  LEU A 146     -17.751  13.485  -2.107  1.00 50.72           C  
ANISOU 1133  CB  LEU A 146     5840   7283   6145    474    -91   -258       C  
ATOM   1134  CG  LEU A 146     -16.571  14.438  -1.950  1.00 51.34           C  
ANISOU 1134  CG  LEU A 146     5891   7446   6169    457   -140   -298       C  
ATOM   1135  CD1 LEU A 146     -15.267  13.645  -1.640  1.00 54.43           C  
ANISOU 1135  CD1 LEU A 146     6249   7899   6531    512   -143   -267       C  
ATOM   1136  CD2 LEU A 146     -16.412  15.336  -3.158  1.00 53.04           C  
ANISOU 1136  CD2 LEU A 146     6104   7638   6410    389   -164   -356       C  
ATOM   1137  N   GLN A 147     -19.438  16.429  -1.936  1.00 43.20           N  
ANISOU 1137  N   GLN A 147     4928   6318   5168    362   -136   -354       N  
ATOM   1138  CA  GLN A 147     -19.711  17.706  -2.581  1.00 44.81           C  
ANISOU 1138  CA  GLN A 147     5139   6506   5379    300   -156   -406       C  
ATOM   1139  C   GLN A 147     -18.871  18.746  -1.940  1.00 43.04           C  
ANISOU 1139  C   GLN A 147     4896   6354   5102    287   -187   -443       C  
ATOM   1140  O   GLN A 147     -19.139  19.178  -0.821  1.00 47.05           O  
ANISOU 1140  O   GLN A 147     5408   6897   5569    300   -192   -444       O  
ATOM   1141  CB  GLN A 147     -21.199  18.088  -2.458  1.00 44.25           C  
ANISOU 1141  CB  GLN A 147     5101   6383   5329    283   -137   -405       C  
ATOM   1142  CG  GLN A 147     -22.185  16.979  -2.752  1.00 44.85           C  
ANISOU 1142  CG  GLN A 147     5192   6392   5455    302   -100   -370       C  
ATOM   1143  CD  GLN A 147     -23.684  17.455  -2.715  1.00 46.80           C  
ANISOU 1143  CD  GLN A 147     5467   6589   5725    280    -84   -375       C  
ATOM   1144  NE2 GLN A 147     -24.550  16.592  -3.139  1.00 42.85           N  
ANISOU 1144  NE2 GLN A 147     4973   6030   5275    287    -53   -359       N  
ATOM   1145  OE1 GLN A 147     -24.018  18.573  -2.315  1.00 46.21           O  
ANISOU 1145  OE1 GLN A 147     5404   6529   5625    256    -97   -397       O  
ATOM   1146  N   GLN A 148     -17.805  19.086  -2.615  1.00 45.51           N  
ANISOU 1146  N   GLN A 148     5183   6691   5415    264   -208   -474       N  
ATOM   1147  CA  GLN A 148     -16.796  19.966  -2.051  1.00 46.49           C  
ANISOU 1147  CA  GLN A 148     5278   6889   5496    251   -237   -516       C  
ATOM   1148  C   GLN A 148     -16.284  20.969  -3.058  1.00 47.50           C  
ANISOU 1148  C   GLN A 148     5395   7004   5649    194   -246   -567       C  
ATOM   1149  O   GLN A 148     -15.939  20.581  -4.181  1.00 45.38           O  
ANISOU 1149  O   GLN A 148     5122   6704   5415    185   -241   -561       O  
ATOM   1150  CB  GLN A 148     -15.618  19.086  -1.640  1.00 54.63           C  
ANISOU 1150  CB  GLN A 148     6274   7985   6495    299   -249   -495       C  
ATOM   1151  CG  GLN A 148     -14.440  19.854  -1.108  1.00 51.91           C  
ANISOU 1151  CG  GLN A 148     5889   7728   6105    289   -282   -544       C  
ATOM   1152  CD  GLN A 148     -14.825  20.738   0.034  1.00 52.38           C  
ANISOU 1152  CD  GLN A 148     5949   7830   6122    282   -292   -576       C  
ATOM   1153  NE2 GLN A 148     -14.589  22.045  -0.116  1.00 52.85           N  
ANISOU 1153  NE2 GLN A 148     5997   7896   6187    224   -303   -643       N  
ATOM   1154  OE1 GLN A 148     -15.413  20.278   0.982  1.00 47.92           O  
ANISOU 1154  OE1 GLN A 148     5398   7282   5525    327   -283   -539       O  
ATOM   1155  N   THR A 149     -16.225  22.249  -2.695  1.00 46.62           N  
ANISOU 1155  N   THR A 149     5278   6912   5524    155   -254   -616       N  
ATOM   1156  CA  THR A 149     -15.665  23.225  -3.622  1.00 48.43           C  
ANISOU 1156  CA  THR A 149     5494   7125   5782    104   -254   -661       C  
ATOM   1157  C   THR A 149     -14.169  22.974  -3.711  1.00 52.35           C  
ANISOU 1157  C   THR A 149     5945   7679   6263    111   -274   -680       C  
ATOM   1158  O   THR A 149     -13.526  22.636  -2.731  1.00 53.67           O  
ANISOU 1158  O   THR A 149     6085   7920   6387    142   -295   -684       O  
ATOM   1159  CB  THR A 149     -15.947  24.673  -3.183  1.00 49.01           C  
ANISOU 1159  CB  THR A 149     5570   7199   5853     60   -248   -712       C  
ATOM   1160  CG2 THR A 149     -17.347  25.107  -3.562  1.00 55.92           C  
ANISOU 1160  CG2 THR A 149     6488   8001   6756     43   -223   -696       C  
ATOM   1161  OG1 THR A 149     -15.922  24.724  -1.790  1.00 56.52           O  
ANISOU 1161  OG1 THR A 149     6510   8211   6754     81   -264   -725       O  
ATOM   1162  N   LEU A 150     -13.643  23.094  -4.913  1.00 53.87           N  
ANISOU 1162  N   LEU A 150     6131   7843   6494     87   -268   -689       N  
ATOM   1163  CA  LEU A 150     -12.255  22.961  -5.183  1.00 46.99           C  
ANISOU 1163  CA  LEU A 150     5216   7016   5618     86   -283   -709       C  
ATOM   1164  C   LEU A 150     -11.567  24.201  -4.632  1.00 54.83           C  
ANISOU 1164  C   LEU A 150     6177   8055   6601     47   -291   -778       C  
ATOM   1165  O   LEU A 150     -12.040  25.353  -4.830  1.00 48.38           O  
ANISOU 1165  O   LEU A 150     5373   7198   5808      2   -271   -811       O  
ATOM   1166  CB  LEU A 150     -11.994  22.879  -6.682  1.00 49.46           C  
ANISOU 1166  CB  LEU A 150     5535   7279   5978     68   -268   -702       C  
ATOM   1167  CG  LEU A 150     -12.502  21.581  -7.344  1.00 57.13           C  
ANISOU 1167  CG  LEU A 150     6529   8211   6965    104   -259   -646       C  
ATOM   1168  CD1 LEU A 150     -12.308  21.590  -8.870  1.00 57.43           C  
ANISOU 1168  CD1 LEU A 150     6571   8204   7043     85   -245   -645       C  
ATOM   1169  CD2 LEU A 150     -11.920  20.308  -6.738  1.00 58.58           C  
ANISOU 1169  CD2 LEU A 150     6693   8439   7122    156   -272   -613       C  
ATOM   1170  N   ASN A 151     -10.469  23.993  -3.912  1.00 52.26           N  
ANISOU 1170  N   ASN A 151     5805   7813   6238     65   -317   -802       N  
ATOM   1171  CA  ASN A 151      -9.701  25.152  -3.370  1.00 59.52           C  
ANISOU 1171  CA  ASN A 151     6681   8783   7149     25   -326   -881       C  
ATOM   1172  C   ASN A 151      -8.206  24.916  -3.348  1.00 57.15           C  
ANISOU 1172  C   ASN A 151     6323   8556   6836     32   -349   -911       C  
ATOM   1173  O   ASN A 151      -7.703  23.846  -3.692  1.00 54.15           O  
ANISOU 1173  O   ASN A 151     5934   8191   6447     72   -359   -867       O  
ATOM   1174  CB  ASN A 151     -10.152  25.432  -1.937  1.00 57.96           C  
ANISOU 1174  CB  ASN A 151     6480   8641   6900     39   -341   -903       C  
ATOM   1175  CG  ASN A 151     -10.009  24.191  -1.063  1.00 64.35           C  
ANISOU 1175  CG  ASN A 151     7280   9520   7648    112   -366   -855       C  
ATOM   1176  ND2 ASN A 151     -11.085  23.870  -0.374  1.00 67.66           N  
ANISOU 1176  ND2 ASN A 151     7735   9927   8042    143   -360   -817       N  
ATOM   1177  OD1 ASN A 151      -8.939  23.515  -1.009  1.00 60.85           O  
ANISOU 1177  OD1 ASN A 151     6797   9140   7183    145   -387   -849       O  
ATOM   1178  N   ASP A 152      -7.488  25.909  -2.860  1.00 68.12           N  
ANISOU 1178  N   ASP A 152     7666   9995   8221     -5   -356   -990       N  
ATOM   1179  CA  ASP A 152      -6.020  25.853  -2.879  1.00 65.16           C  
ANISOU 1179  CA  ASP A 152     7226   9690   7839     -7   -376  -1032       C  
ATOM   1180  C   ASP A 152      -5.378  24.745  -2.028  1.00 64.81           C  
ANISOU 1180  C   ASP A 152     7148   9749   7726     60   -415  -1007       C  
ATOM   1181  O   ASP A 152      -4.174  24.595  -2.094  1.00 65.21           O  
ANISOU 1181  O   ASP A 152     7144   9860   7769     65   -433  -1035       O  
ATOM   1182  CB  ASP A 152      -5.445  27.194  -2.451  1.00 71.71           C  
ANISOU 1182  CB  ASP A 152     8009  10553   8683    -66   -372  -1134       C  
ATOM   1183  CG  ASP A 152      -5.873  27.576  -1.053  1.00 72.98           C  
ANISOU 1183  CG  ASP A 152     8158  10779   8789    -58   -391  -1174       C  
ATOM   1184  OD1 ASP A 152      -6.250  26.675  -0.266  1.00 85.89           O  
ANISOU 1184  OD1 ASP A 152     9806  12465  10362      4   -416  -1126       O  
ATOM   1185  OD2 ASP A 152      -5.878  28.775  -0.760  1.00 76.82           O1-
ANISOU 1185  OD2 ASP A 152     8627  11261   9300   -113   -375  -1253       O1-
ATOM   1186  N   THR A 153      -6.102  23.956  -1.237  1.00 63.05           N  
ANISOU 1186  N   THR A 153     6951   9549   7453    118   -426   -952       N  
ATOM   1187  CA  THR A 153      -5.387  22.827  -0.609  1.00 61.82           C  
ANISOU 1187  CA  THR A 153     6763   9486   7239    191   -454   -915       C  
ATOM   1188  C   THR A 153      -5.138  21.632  -1.573  1.00 64.52           C  
ANISOU 1188  C   THR A 153     7123   9784   7608    226   -442   -840       C  
ATOM   1189  O   THR A 153      -4.488  20.662  -1.209  1.00 62.47           O  
ANISOU 1189  O   THR A 153     6837   9590   7310    288   -457   -803       O  
ATOM   1190  CB  THR A 153      -6.084  22.294   0.649  1.00 67.86           C  
ANISOU 1190  CB  THR A 153     7542  10303   7936    254   -464   -876       C  
ATOM   1191  CG2 THR A 153      -6.697  23.432   1.440  1.00 70.40           C  
ANISOU 1191  CG2 THR A 153     7868  10639   8242    216   -467   -939       C  
ATOM   1192  OG1 THR A 153      -7.060  21.309   0.276  1.00 70.52           O  
ANISOU 1192  OG1 THR A 153     7940  10562   8292    291   -438   -785       O  
ATOM   1193  N   VAL A 154      -5.639  21.670  -2.795  1.00 53.73           N  
ANISOU 1193  N   VAL A 154     5797   8310   6305    192   -413   -817       N  
ATOM   1194  CA  VAL A 154      -5.551  20.459  -3.611  1.00 56.93           C  
ANISOU 1194  CA  VAL A 154     6222   8675   6733    229   -400   -748       C  
ATOM   1195  C   VAL A 154      -4.095  20.269  -4.086  1.00 59.06           C  
ANISOU 1195  C   VAL A 154     6440   8992   7009    230   -413   -768       C  
ATOM   1196  O   VAL A 154      -3.367  21.251  -4.297  1.00 61.38           O  
ANISOU 1196  O   VAL A 154     6697   9305   7319    179   -420   -837       O  
ATOM   1197  CB  VAL A 154      -6.538  20.474  -4.853  1.00 52.19           C  
ANISOU 1197  CB  VAL A 154     5679   7953   6195    196   -367   -720       C  
ATOM   1198  CG1 VAL A 154      -7.974  20.632  -4.405  1.00 56.80           C  
ANISOU 1198  CG1 VAL A 154     6311   8493   6776    196   -353   -700       C  
ATOM   1199  CG2 VAL A 154      -6.174  21.584  -5.822  1.00 52.49           C  
ANISOU 1199  CG2 VAL A 154     5709   7952   6281    129   -355   -773       C  
ATOM   1200  N   GLY A 155      -3.689  19.026  -4.323  1.00 57.48           N  
ANISOU 1200  N   GLY A 155     6236   8800   6802    284   -411   -709       N  
ATOM   1201  CA  GLY A 155      -2.336  18.760  -4.755  1.00 60.97           C  
ANISOU 1201  CA  GLY A 155     6629   9286   7248    291   -423   -722       C  
ATOM   1202  C   GLY A 155      -2.011  19.314  -6.135  1.00 69.03           C  
ANISOU 1202  C   GLY A 155     7655  10238   8334    231   -405   -750       C  
ATOM   1203  O   GLY A 155      -2.855  19.928  -6.814  1.00 58.35           O  
ANISOU 1203  O   GLY A 155     6344   8803   7022    186   -383   -758       O  
ATOM   1204  N   ARG A 156      -0.779  19.075  -6.570  1.00 64.48           N  
ANISOU 1204  N   ARG A 156     7035   9699   7766    236   -413   -761       N  
ATOM   1205  CA  ARG A 156      -0.231  19.865  -7.672  1.00 71.86           C  
ANISOU 1205  CA  ARG A 156     7958  10590   8754    176   -398   -804       C  
ATOM   1206  C   ARG A 156      -0.695  19.448  -9.047  1.00 57.95           C  
ANISOU 1206  C   ARG A 156     6244   8731   7044    168   -367   -761       C  
ATOM   1207  O   ARG A 156      -0.827  20.299  -9.910  1.00 58.35           O  
ANISOU 1207  O   ARG A 156     6307   8724   7137    117   -345   -788       O  
ATOM   1208  CB  ARG A 156       1.312  19.901  -7.639  1.00 80.34           C  
ANISOU 1208  CB  ARG A 156     8960  11741   9821    178   -416   -841       C  
ATOM   1209  CG  ARG A 156       1.790  21.140  -6.907  1.00102.92           C  
ANISOU 1209  CG  ARG A 156    11770  14663  12671    133   -433   -930       C  
ATOM   1210  CD  ARG A 156       3.243  21.043  -6.509  1.00114.49           C  
ANISOU 1210  CD  ARG A 156    13156  16233  14113    148   -460   -970       C  
ATOM   1211  NE  ARG A 156       3.498  21.926  -5.381  1.00114.16           N  
ANISOU 1211  NE  ARG A 156    13062  16275  14035    126   -485  -1051       N  
ATOM   1212  CZ  ARG A 156       4.703  22.161  -4.889  1.00123.28           C  
ANISOU 1212  CZ  ARG A 156    14137  17532  15169    125   -512  -1114       C  
ATOM   1213  NH1 ARG A 156       4.842  22.979  -3.850  1.00134.44           N1+
ANISOU 1213  NH1 ARG A 156    15503  19025  16550    104   -534  -1196       N1+
ATOM   1214  NH2 ARG A 156       5.770  21.589  -5.440  1.00115.87           N  
ANISOU 1214  NH2 ARG A 156    13162  16619  14242    145   -516  -1099       N  
ATOM   1215  N   LYS A 157      -0.831  18.148  -9.252  1.00 46.26           N  
ANISOU 1215  N   LYS A 157     4782   7237   5558    220   -361   -697       N  
ATOM   1216  CA  LYS A 157      -1.394  17.622 -10.461  1.00 57.30           C  
ANISOU 1216  CA  LYS A 157     6223   8548   6997    218   -333   -660       C  
ATOM   1217  C   LYS A 157      -2.846  18.095 -10.620  1.00 52.50           C  
ANISOU 1217  C   LYS A 157     5669   7871   6405    193   -317   -657       C  
ATOM   1218  O   LYS A 157      -3.245  18.387 -11.728  1.00 54.39           O  
ANISOU 1218  O   LYS A 157     5936   8047   6682    164   -296   -659       O  
ATOM   1219  CB  LYS A 157      -1.282  16.097 -10.471  1.00 57.33           C  
ANISOU 1219  CB  LYS A 157     6233   8554   6995    281   -327   -598       C  
ATOM   1220  CG  LYS A 157       0.202  15.728 -10.608  1.00 67.42           C  
ANISOU 1220  CG  LYS A 157     7459   9890   8267    300   -338   -602       C  
ATOM   1221  CD  LYS A 157       0.474  14.299 -11.016  1.00 74.75           C  
ANISOU 1221  CD  LYS A 157     8391  10802   9205    353   -320   -544       C  
ATOM   1222  CE  LYS A 157       1.779  14.285 -11.812  1.00 88.03           C  
ANISOU 1222  CE  LYS A 157    10035  12504  10907    345   -321   -560       C  
ATOM   1223  NZ  LYS A 157       2.565  13.051 -11.583  1.00 98.85           N1+
ANISOU 1223  NZ  LYS A 157    11380  13914  12263    408   -318   -514       N1+
ATOM   1224  N   ILE A 158      -3.581  18.234  -9.526  1.00 51.28           N  
ANISOU 1224  N   ILE A 158     5527   7737   6218    204   -327   -655       N  
ATOM   1225  CA  ILE A 158      -4.977  18.703  -9.642  1.00 50.27           C  
ANISOU 1225  CA  ILE A 158     5449   7546   6105    180   -312   -652       C  
ATOM   1226  C   ILE A 158      -4.895  20.169 -10.031  1.00 53.34           C  
ANISOU 1226  C   ILE A 158     5832   7918   6516    119   -305   -707       C  
ATOM   1227  O   ILE A 158      -5.575  20.660 -10.931  1.00 44.32           O  
ANISOU 1227  O   ILE A 158     4722   6710   5407     91   -283   -707       O  
ATOM   1228  CB  ILE A 158      -5.800  18.507  -8.353  1.00 51.97           C  
ANISOU 1228  CB  ILE A 158     5679   7784   6282    208   -321   -635       C  
ATOM   1229  CG1 ILE A 158      -5.956  17.039  -7.956  1.00 46.86           C  
ANISOU 1229  CG1 ILE A 158     5039   7144   5619    273   -315   -573       C  
ATOM   1230  CG2 ILE A 158      -7.243  19.043  -8.544  1.00 60.33           C  
ANISOU 1230  CG2 ILE A 158     6786   8774   7359    180   -303   -634       C  
ATOM   1231  CD1 ILE A 158      -6.336  16.119  -9.076  1.00 49.46           C  
ANISOU 1231  CD1 ILE A 158     5397   7402   5994    283   -288   -536       C  
ATOM   1232  N   VAL A 159      -3.978  20.882  -9.421  1.00 59.83           N  
ANISOU 1232  N   VAL A 159     6609   8801   7323    100   -321   -756       N  
ATOM   1233  CA  VAL A 159      -3.810  22.253  -9.831  1.00 56.70           C  
ANISOU 1233  CA  VAL A 159     6203   8380   6958     41   -305   -809       C  
ATOM   1234  C   VAL A 159      -3.506  22.284 -11.347  1.00 53.32           C  
ANISOU 1234  C   VAL A 159     5786   7896   6578     25   -278   -797       C  
ATOM   1235  O   VAL A 159      -4.069  23.100 -12.101  1.00 46.88           O  
ANISOU 1235  O   VAL A 159     4997   7019   5795     -7   -248   -804       O  
ATOM   1236  CB  VAL A 159      -2.710  22.914  -8.984  1.00 62.95           C  
ANISOU 1236  CB  VAL A 159     6933   9251   7733     22   -324   -873       C  
ATOM   1237  CG1 VAL A 159      -2.137  24.128  -9.680  1.00 62.65           C  
ANISOU 1237  CG1 VAL A 159     6873   9184   7744    -36   -297   -927       C  
ATOM   1238  CG2 VAL A 159      -3.241  23.286  -7.608  1.00 62.94           C  
ANISOU 1238  CG2 VAL A 159     6928   9296   7689     25   -343   -898       C  
ATOM   1239  N   MET A 160      -2.639  21.390 -11.809  1.00 55.81           N  
ANISOU 1239  N   MET A 160     6080   8231   6894     52   -285   -776       N  
ATOM   1240  CA  MET A 160      -2.211  21.439 -13.218  1.00 54.04           C  
ANISOU 1240  CA  MET A 160     5859   7962   6709     39   -260   -768       C  
ATOM   1241  C   MET A 160      -3.393  21.037 -14.115  1.00 52.74           C  
ANISOU 1241  C   MET A 160     5749   7728   6558     51   -240   -726       C  
ATOM   1242  O   MET A 160      -3.541  21.550 -15.179  1.00 45.13           O  
ANISOU 1242  O   MET A 160     4802   6720   5624     31   -214   -727       O  
ATOM   1243  CB  MET A 160      -1.057  20.479 -13.534  1.00 61.42           C  
ANISOU 1243  CB  MET A 160     6760   8933   7642     69   -270   -752       C  
ATOM   1244  CG  MET A 160       0.270  20.796 -12.853  1.00 76.38           C  
ANISOU 1244  CG  MET A 160     8592  10903   9526     61   -290   -796       C  
ATOM   1245  SD  MET A 160       1.053  22.273 -13.536  1.00 84.17           S  
ANISOU 1245  SD  MET A 160     9548  11870  10563     -2   -261   -857       S  
ATOM   1246  CE  MET A 160       1.722  21.515 -15.030  1.00 76.84           C  
ANISOU 1246  CE  MET A 160     8622  10907   9663     16   -241   -818       C  
ATOM   1247  N   ASP A 161      -4.190  20.090 -13.669  1.00 51.40           N  
ANISOU 1247  N   ASP A 161     5605   7555   6368     85   -252   -691       N  
ATOM   1248  CA  ASP A 161      -5.419  19.737 -14.366  1.00 54.20           C  
ANISOU 1248  CA  ASP A 161     6007   7851   6735     93   -235   -662       C  
ATOM   1249  C   ASP A 161      -6.405  20.927 -14.560  1.00 46.19           C  
ANISOU 1249  C   ASP A 161     5022   6797   5732     59   -218   -678       C  
ATOM   1250  O   ASP A 161      -6.800  21.266 -15.679  1.00 48.61           O  
ANISOU 1250  O   ASP A 161     5347   7061   6059     49   -195   -673       O  
ATOM   1251  CB  ASP A 161      -6.033  18.568 -13.619  1.00 53.55           C  
ANISOU 1251  CB  ASP A 161     5938   7774   6633    134   -247   -627       C  
ATOM   1252  CG  ASP A 161      -5.258  17.257 -13.838  1.00 52.00           C  
ANISOU 1252  CG  ASP A 161     5723   7594   6438    174   -249   -599       C  
ATOM   1253  OD1 ASP A 161      -4.386  17.203 -14.770  1.00 48.95           O  
ANISOU 1253  OD1 ASP A 161     5320   7208   6071    168   -242   -606       O  
ATOM   1254  OD2 ASP A 161      -5.603  16.255 -13.144  1.00 51.34           O1-
ANISOU 1254  OD2 ASP A 161     5646   7518   6342    212   -251   -567       O1-
ATOM   1255  N   PHE A 162      -6.721  21.584 -13.461  1.00 45.47           N  
ANISOU 1255  N   PHE A 162     4929   6724   5624     44   -227   -699       N  
ATOM   1256  CA  PHE A 162      -7.619  22.694 -13.376  1.00 46.75           C  
ANISOU 1256  CA  PHE A 162     5115   6854   5794     14   -210   -714       C  
ATOM   1257  C   PHE A 162      -7.163  23.772 -14.325  1.00 47.36           C  
ANISOU 1257  C   PHE A 162     5185   6904   5904    -18   -180   -736       C  
ATOM   1258  O   PHE A 162      -7.961  24.413 -15.036  1.00 43.72           O  
ANISOU 1258  O   PHE A 162     4753   6396   5460    -29   -152   -727       O  
ATOM   1259  CB  PHE A 162      -7.590  23.188 -11.901  1.00 51.23           C  
ANISOU 1259  CB  PHE A 162     5666   7463   6335      3   -228   -744       C  
ATOM   1260  CG  PHE A 162      -8.507  24.333 -11.594  1.00 54.01           C  
ANISOU 1260  CG  PHE A 162     6041   7784   6694    -27   -210   -763       C  
ATOM   1261  CD1 PHE A 162      -9.859  24.116 -11.302  1.00 55.33           C  
ANISOU 1261  CD1 PHE A 162     6248   7923   6850    -13   -209   -736       C  
ATOM   1262  CD2 PHE A 162      -8.025  25.649 -11.580  1.00 57.77           C  
ANISOU 1262  CD2 PHE A 162     6498   8258   7194    -71   -189   -810       C  
ATOM   1263  CE1 PHE A 162     -10.679  25.195 -10.978  1.00 57.25           C  
ANISOU 1263  CE1 PHE A 162     6512   8140   7100    -40   -192   -754       C  
ATOM   1264  CE2 PHE A 162      -8.831  26.720 -11.259  1.00 55.36           C  
ANISOU 1264  CE2 PHE A 162     6213   7921   6899    -99   -167   -829       C  
ATOM   1265  CZ  PHE A 162     -10.172  26.495 -10.959  1.00 59.14           C  
ANISOU 1265  CZ  PHE A 162     6733   8375   7361    -82   -170   -799       C  
ATOM   1266  N   LEU A 163      -5.864  24.002 -14.325  1.00 45.99           N  
ANISOU 1266  N   LEU A 163     4969   6761   5740    -32   -181   -763       N  
ATOM   1267  CA  LEU A 163      -5.310  25.061 -15.118  1.00 42.93           C  
ANISOU 1267  CA  LEU A 163     4571   6349   5391    -65   -145   -786       C  
ATOM   1268  C   LEU A 163      -5.427  24.718 -16.624  1.00 39.55           C  
ANISOU 1268  C   LEU A 163     4164   5883   4980    -46   -122   -749       C  
ATOM   1269  O   LEU A 163      -5.337  25.609 -17.465  1.00 36.81           O  
ANISOU 1269  O   LEU A 163     3821   5501   4661    -63    -82   -752       O  
ATOM   1270  CB  LEU A 163      -3.806  25.194 -14.838  1.00 46.36           C  
ANISOU 1270  CB  LEU A 163     4949   6829   5835    -80   -152   -824       C  
ATOM   1271  CG  LEU A 163      -3.364  25.963 -13.610  1.00 47.87           C  
ANISOU 1271  CG  LEU A 163     5103   7062   6021   -112   -163   -882       C  
ATOM   1272  CD1 LEU A 163      -1.853  25.772 -13.485  1.00 53.97           C  
ANISOU 1272  CD1 LEU A 163     5816   7889   6799   -116   -176   -915       C  
ATOM   1273  CD2 LEU A 163      -3.775  27.444 -13.743  1.00 48.66           C  
ANISOU 1273  CD2 LEU A 163     5213   7113   6161   -157   -117   -914       C  
ATOM   1274  N   GLY A 164      -5.473  23.425 -16.919  1.00 36.69           N  
ANISOU 1274  N   GLY A 164     3808   5531   4599    -10   -144   -719       N  
ATOM   1275  CA  GLY A 164      -5.678  22.931 -18.240  1.00 36.14           C  
ANISOU 1275  CA  GLY A 164     3757   5435   4538     11   -129   -690       C  
ATOM   1276  C   GLY A 164      -7.141  22.991 -18.726  1.00 36.46           C  
ANISOU 1276  C   GLY A 164     3841   5440   4572     22   -118   -668       C  
ATOM   1277  O   GLY A 164      -7.402  22.698 -19.886  1.00 41.46           O  
ANISOU 1277  O   GLY A 164     4488   6057   5208     41   -105   -650       O  
ATOM   1278  N   PHE A 165      -8.067  23.412 -17.886  1.00 36.09           N  
ANISOU 1278  N   PHE A 165     3812   5384   4515     12   -123   -672       N  
ATOM   1279  CA  PHE A 165      -9.478  23.544 -18.298  1.00 37.41           C  
ANISOU 1279  CA  PHE A 165     4016   5520   4676     22   -112   -654       C  
ATOM   1280  C   PHE A 165      -9.570  24.543 -19.437  1.00 38.15           C  
ANISOU 1280  C   PHE A 165     4120   5589   4786     17    -73   -647       C  
ATOM   1281  O   PHE A 165      -8.612  25.344 -19.609  1.00 40.18           O  
ANISOU 1281  O   PHE A 165     4357   5844   5065     -2    -48   -661       O  
ATOM   1282  CB  PHE A 165     -10.348  23.993 -17.101  1.00 34.44           C  
ANISOU 1282  CB  PHE A 165     3655   5139   4289      8   -121   -662       C  
ATOM   1283  CG  PHE A 165     -10.568  22.925 -16.071  1.00 37.32           C  
ANISOU 1283  CG  PHE A 165     4019   5526   4635     25   -154   -656       C  
ATOM   1284  CD1 PHE A 165     -10.042  21.668 -16.212  1.00 42.16           C  
ANISOU 1284  CD1 PHE A 165     4618   6157   5243     51   -171   -644       C  
ATOM   1285  CD2 PHE A 165     -11.337  23.188 -14.940  1.00 37.93           C  
ANISOU 1285  CD2 PHE A 165     4109   5604   4698     18   -163   -660       C  
ATOM   1286  CE1 PHE A 165     -10.237  20.687 -15.251  1.00 40.07           C  
ANISOU 1286  CE1 PHE A 165     4352   5908   4963     72   -192   -631       C  
ATOM   1287  CE2 PHE A 165     -11.544  22.207 -14.005  1.00 37.53           C  
ANISOU 1287  CE2 PHE A 165     4058   5572   4628     40   -186   -649       C  
ATOM   1288  CZ  PHE A 165     -11.013  20.973 -14.150  1.00 39.44           C  
ANISOU 1288  CZ  PHE A 165     4287   5830   4868     68   -198   -632       C  
ATOM   1289  N   ASN A 166     -10.660  24.508 -20.225  1.00 36.13           N  
ANISOU 1289  N   ASN A 166     3890   5315   4520     38    -62   -627       N  
ATOM   1290  CA  ASN A 166     -10.741  25.439 -21.359  1.00 37.48           C  
ANISOU 1290  CA  ASN A 166     4070   5469   4700     45    -20   -612       C  
ATOM   1291  C   ASN A 166     -11.224  26.857 -20.958  1.00 43.49           C  
ANISOU 1291  C   ASN A 166     4845   6203   5476     23     14   -613       C  
ATOM   1292  O   ASN A 166     -12.362  27.324 -21.326  1.00 45.18           O  
ANISOU 1292  O   ASN A 166     5084   6401   5679     38     31   -593       O  
ATOM   1293  CB  ASN A 166     -11.546  24.869 -22.534  1.00 36.67           C  
ANISOU 1293  CB  ASN A 166     3982   5372   4577     83    -20   -592       C  
ATOM   1294  CG  ASN A 166     -11.407  25.721 -23.754  1.00 39.39           C  
ANISOU 1294  CG  ASN A 166     4330   5710   4923    100     23   -571       C  
ATOM   1295  ND2 ASN A 166     -11.912  25.246 -24.884  1.00 40.32           N  
ANISOU 1295  ND2 ASN A 166     4455   5847   5018    138     23   -558       N  
ATOM   1296  OD1 ASN A 166     -10.805  26.801 -23.691  1.00 37.90           O  
ANISOU 1296  OD1 ASN A 166     4137   5503   4759     82     60   -569       O  
ATOM   1297  N   TRP A 167     -10.370  27.548 -20.201  1.00 42.75           N  
ANISOU 1297  N   TRP A 167     4732   6104   5406    -11     25   -638       N  
ATOM   1298  CA  TRP A 167     -10.617  28.930 -19.738  1.00 41.22           C  
ANISOU 1298  CA  TRP A 167     4545   5880   5237    -40     65   -649       C  
ATOM   1299  C   TRP A 167     -10.824  29.882 -20.913  1.00 42.72           C  
ANISOU 1299  C   TRP A 167     4749   6038   5445    -24    125   -619       C  
ATOM   1300  O   TRP A 167     -11.611  30.843 -20.867  1.00 41.15           O  
ANISOU 1300  O   TRP A 167     4569   5808   5254    -26    162   -607       O  
ATOM   1301  CB  TRP A 167      -9.455  29.413 -18.845  1.00 38.95           C  
ANISOU 1301  CB  TRP A 167     4222   5599   4976    -82     68   -694       C  
ATOM   1302  CG  TRP A 167      -9.361  28.557 -17.621  1.00 40.12           C  
ANISOU 1302  CG  TRP A 167     4358   5787   5099    -88     11   -718       C  
ATOM   1303  CD1 TRP A 167      -8.398  27.673 -17.315  1.00 38.94           C  
ANISOU 1303  CD1 TRP A 167     4178   5676   4938    -84    -23   -732       C  
ATOM   1304  CD2 TRP A 167     -10.332  28.470 -16.587  1.00 42.37           C  
ANISOU 1304  CD2 TRP A 167     4661   6075   5362    -90    -11   -722       C  
ATOM   1305  CE2 TRP A 167      -9.889  27.485 -15.684  1.00 39.05           C  
ANISOU 1305  CE2 TRP A 167     4220   5699   4916    -85    -60   -736       C  
ATOM   1306  CE3 TRP A 167     -11.549  29.112 -16.356  1.00 41.00           C  
ANISOU 1306  CE3 TRP A 167     4518   5872   5186    -93      5   -712       C  
ATOM   1307  NE1 TRP A 167      -8.685  27.025 -16.148  1.00 42.95           N  
ANISOU 1307  NE1 TRP A 167     4685   6216   5418    -81    -66   -742       N  
ATOM   1308  CZ2 TRP A 167     -10.581  27.135 -14.592  1.00 42.43           C  
ANISOU 1308  CZ2 TRP A 167     4660   6143   5318    -80    -88   -739       C  
ATOM   1309  CZ3 TRP A 167     -12.279  28.736 -15.236  1.00 41.25           C  
ANISOU 1309  CZ3 TRP A 167     4561   5918   5193    -92    -26   -718       C  
ATOM   1310  CH2 TRP A 167     -11.815  27.752 -14.387  1.00 42.26           C  
ANISOU 1310  CH2 TRP A 167     4671   6089   5296    -85    -72   -730       C  
ATOM   1311  N   ASN A 168     -10.172  29.589 -22.007  1.00 42.72           N  
ANISOU 1311  N   ASN A 168     4739   6046   5445     -2    138   -602       N  
ATOM   1312  CA  ASN A 168     -10.325  30.451 -23.151  1.00 44.08           C  
ANISOU 1312  CA  ASN A 168     4923   6194   5629     21    199   -567       C  
ATOM   1313  C   ASN A 168     -11.808  30.493 -23.510  1.00 44.72           C  
ANISOU 1313  C   ASN A 168     5037   6276   5678     56    199   -535       C  
ATOM   1314  O   ASN A 168     -12.359  31.565 -23.664  1.00 41.02           O  
ANISOU 1314  O   ASN A 168     4585   5778   5222     62    248   -514       O  
ATOM   1315  CB  ASN A 168      -9.512  29.972 -24.334  1.00 45.13           C  
ANISOU 1315  CB  ASN A 168     5043   6344   5758     49    208   -550       C  
ATOM   1316  CG  ASN A 168      -9.689  30.867 -25.538  1.00 47.44           C  
ANISOU 1316  CG  ASN A 168     5349   6617   6057     84    275   -506       C  
ATOM   1317  ND2 ASN A 168     -10.049  30.286 -26.675  1.00 50.84           N  
ANISOU 1317  ND2 ASN A 168     5789   7078   6449    135    268   -476       N  
ATOM   1318  OD1 ASN A 168      -9.555  32.078 -25.429  1.00 55.97           O  
ANISOU 1318  OD1 ASN A 168     6432   7657   7177     67    336   -500       O  
ATOM   1319  N   TRP A 169     -12.435  29.328 -23.591  1.00 42.53           N  
ANISOU 1319  N   TRP A 169     4765   6031   5361     79    146   -535       N  
ATOM   1320  CA  TRP A 169     -13.811  29.187 -24.110  1.00 43.94           C  
ANISOU 1320  CA  TRP A 169     4967   6222   5506    117    140   -510       C  
ATOM   1321  C   TRP A 169     -14.814  29.745 -23.080  1.00 44.47           C  
ANISOU 1321  C   TRP A 169     5052   6267   5577     97    140   -515       C  
ATOM   1322  O   TRP A 169     -15.659  30.546 -23.405  1.00 45.16           O  
ANISOU 1322  O   TRP A 169     5158   6342   5660    116    174   -489       O  
ATOM   1323  CB  TRP A 169     -14.142  27.680 -24.455  1.00 44.42           C  
ANISOU 1323  CB  TRP A 169     5022   6322   5533    140     85   -521       C  
ATOM   1324  CG  TRP A 169     -15.592  27.539 -24.827  1.00 42.30           C  
ANISOU 1324  CG  TRP A 169     4769   6069   5233    172     76   -508       C  
ATOM   1325  CD1 TRP A 169     -16.140  27.849 -26.026  1.00 39.03           C  
ANISOU 1325  CD1 TRP A 169     4360   5677   4792    218    100   -482       C  
ATOM   1326  CD2 TRP A 169     -16.671  27.202 -23.955  1.00 38.47           C  
ANISOU 1326  CD2 TRP A 169     4294   5579   4740    161     46   -521       C  
ATOM   1327  CE2 TRP A 169     -17.855  27.310 -24.719  1.00 43.91           C  
ANISOU 1327  CE2 TRP A 169     4993   6290   5401    199     52   -504       C  
ATOM   1328  CE3 TRP A 169     -16.762  26.871 -22.601  1.00 41.58           C  
ANISOU 1328  CE3 TRP A 169     4692   5958   5149    126     18   -542       C  
ATOM   1329  NE1 TRP A 169     -17.474  27.675 -25.982  1.00 41.62           N  
ANISOU 1329  NE1 TRP A 169     4697   6019   5095    235     83   -482       N  
ATOM   1330  CZ2 TRP A 169     -19.120  27.058 -24.186  1.00 39.42           C  
ANISOU 1330  CZ2 TRP A 169     4433   5721   4821    200     30   -512       C  
ATOM   1331  CZ3 TRP A 169     -17.992  26.628 -22.065  1.00 41.73           C  
ANISOU 1331  CZ3 TRP A 169     4723   5974   5157    128      0   -545       C  
ATOM   1332  CH2 TRP A 169     -19.178  26.695 -22.867  1.00 42.21           C  
ANISOU 1332  CH2 TRP A 169     4792   6052   5194    163      5   -532       C  
ATOM   1333  N   ILE A 170     -14.649  29.349 -21.829  1.00 41.89           N  
ANISOU 1333  N   ILE A 170     4719   5937   5257     61    104   -547       N  
ATOM   1334  CA  ILE A 170     -15.578  29.733 -20.806  1.00 42.43           C  
ANISOU 1334  CA  ILE A 170     4805   5990   5327     44     98   -554       C  
ATOM   1335  C   ILE A 170     -15.396  31.214 -20.414  1.00 43.37           C  
ANISOU 1335  C   ILE A 170     4928   6069   5480     17    153   -556       C  
ATOM   1336  O   ILE A 170     -16.353  31.878 -20.116  1.00 46.01           O  
ANISOU 1336  O   ILE A 170     5282   6383   5814     18    173   -545       O  
ATOM   1337  CB  ILE A 170     -15.523  28.741 -19.633  1.00 45.32           C  
ANISOU 1337  CB  ILE A 170     5163   6372   5683     24     44   -582       C  
ATOM   1338  CG1 ILE A 170     -16.820  28.841 -18.809  1.00 44.71           C  
ANISOU 1338  CG1 ILE A 170     5108   6284   5595     21     32   -580       C  
ATOM   1339  CG2 ILE A 170     -14.321  28.964 -18.743  1.00 41.05           C  
ANISOU 1339  CG2 ILE A 170     4599   5832   5163    -13     40   -614       C  
ATOM   1340  CD1 ILE A 170     -16.910  27.811 -17.689  1.00 45.75           C  
ANISOU 1340  CD1 ILE A 170     5235   6432   5715     12    -14   -599       C  
ATOM   1341  N   ASN A 171     -14.189  31.751 -20.418  1.00 41.21           N  
ANISOU 1341  N   ASN A 171     4634   5782   5240     -8    182   -573       N  
ATOM   1342  CA  ASN A 171     -14.017  33.207 -20.177  1.00 41.33           C  
ANISOU 1342  CA  ASN A 171     4651   5753   5300    -34    247   -579       C  
ATOM   1343  C   ASN A 171     -14.681  34.011 -21.315  1.00 42.46           C  
ANISOU 1343  C   ASN A 171     4816   5872   5445      5    308   -526       C  
ATOM   1344  O   ASN A 171     -15.203  35.074 -21.060  1.00 43.03           O  
ANISOU 1344  O   ASN A 171     4901   5905   5540     -2    358   -517       O  
ATOM   1345  CB  ASN A 171     -12.518  33.698 -20.024  1.00 42.64           C  
ANISOU 1345  CB  ASN A 171     4783   5906   5511    -73    276   -614       C  
ATOM   1346  CG  ASN A 171     -11.767  33.028 -18.890  1.00 45.22           C  
ANISOU 1346  CG  ASN A 171     5082   6265   5833   -108    220   -667       C  
ATOM   1347  ND2 ASN A 171     -10.492  33.134 -18.973  1.00 45.57           N  
ANISOU 1347  ND2 ASN A 171     5093   6314   5906   -130    231   -694       N  
ATOM   1348  OD1 ASN A 171     -12.316  32.454 -17.931  1.00 41.66           O  
ANISOU 1348  OD1 ASN A 171     4637   5837   5353   -113    170   -682       O  
ATOM   1349  N   LYS A 172     -14.632  33.564 -22.560  1.00 43.23           N  
ANISOU 1349  N   LYS A 172     4914   5993   5518     51    311   -491       N  
ATOM   1350  CA  LYS A 172     -15.320  34.292 -23.585  1.00 47.35           C  
ANISOU 1350  CA  LYS A 172     5454   6504   6032     98    366   -438       C  
ATOM   1351  C   LYS A 172     -16.872  34.243 -23.340  1.00 51.05           C  
ANISOU 1351  C   LYS A 172     5947   6983   6466    121    346   -421       C  
ATOM   1352  O   LYS A 172     -17.585  35.213 -23.665  1.00 47.70           O  
ANISOU 1352  O   LYS A 172     5541   6536   6047    146    401   -384       O  
ATOM   1353  CB  LYS A 172     -15.071  33.736 -24.984  1.00 52.09           C  
ANISOU 1353  CB  LYS A 172     6050   7142   6601    150    366   -406       C  
ATOM   1354  CG  LYS A 172     -13.725  34.109 -25.623  1.00 65.01           C  
ANISOU 1354  CG  LYS A 172     7667   8761   8271    147    413   -400       C  
ATOM   1355  CD  LYS A 172     -13.519  33.634 -27.084  1.00 66.62           C  
ANISOU 1355  CD  LYS A 172     7868   9005   8439    206    420   -364       C  
ATOM   1356  CE  LYS A 172     -13.740  32.132 -27.216  1.00 79.73           C  
ANISOU 1356  CE  LYS A 172     9520  10721  10050    218    337   -387       C  
ATOM   1357  NZ  LYS A 172     -13.112  31.548 -28.429  1.00 81.82           N1+
ANISOU 1357  NZ  LYS A 172     9772  11022  10291    258    337   -372       N1+
ATOM   1358  N   GLN A 173     -17.381  33.103 -22.866  1.00 43.74           N  
ANISOU 1358  N   GLN A 173     5020   6090   5506    118    274   -444       N  
ATOM   1359  CA  GLN A 173     -18.800  32.990 -22.468  1.00 47.28           C  
ANISOU 1359  CA  GLN A 173     5487   6546   5929    130    252   -437       C  
ATOM   1360  C   GLN A 173     -19.146  33.995 -21.389  1.00 48.11           C  
ANISOU 1360  C   GLN A 173     5606   6606   6066     95    282   -446       C  
ATOM   1361  O   GLN A 173     -20.105  34.761 -21.539  1.00 46.44           O  
ANISOU 1361  O   GLN A 173     5413   6378   5851    117    318   -416       O  
ATOM   1362  CB  GLN A 173     -19.152  31.604 -21.986  1.00 42.77           C  
ANISOU 1362  CB  GLN A 173     4911   6008   5332    124    177   -466       C  
ATOM   1363  CG  GLN A 173     -19.216  30.575 -23.094  1.00 43.97           C  
ANISOU 1363  CG  GLN A 173     5050   6206   5449    164    148   -459       C  
ATOM   1364  CD  GLN A 173     -20.259  30.882 -24.177  1.00 45.99           C  
ANISOU 1364  CD  GLN A 173     5313   6487   5670    220    168   -424       C  
ATOM   1365  NE2 GLN A 173     -19.881  30.647 -25.425  1.00 43.55           N  
ANISOU 1365  NE2 GLN A 173     4993   6214   5340    260    177   -409       N  
ATOM   1366  OE1 GLN A 173     -21.367  31.274 -23.909  1.00 45.57           O  
ANISOU 1366  OE1 GLN A 173     5274   6431   5609    230    174   -412       O  
ATOM   1367  N   GLN A 174     -18.366  33.989 -20.308  1.00 41.27           N  
ANISOU 1367  N   GLN A 174     4729   5723   5227     43    267   -490       N  
ATOM   1368  CA  GLN A 174     -18.597  34.899 -19.209  1.00 42.31           C  
ANISOU 1368  CA  GLN A 174     4869   5817   5388      5    293   -510       C  
ATOM   1369  C   GLN A 174     -18.657  36.341 -19.737  1.00 48.63           C  
ANISOU 1369  C   GLN A 174     5679   6570   6225     13    381   -481       C  
ATOM   1370  O   GLN A 174     -19.564  37.074 -19.432  1.00 42.38           O  
ANISOU 1370  O   GLN A 174     4908   5752   5441     17    413   -465       O  
ATOM   1371  CB  GLN A 174     -17.467  34.752 -18.228  1.00 41.91           C  
ANISOU 1371  CB  GLN A 174     4795   5768   5361    -45    272   -565       C  
ATOM   1372  CG  GLN A 174     -17.430  35.796 -17.137  1.00 45.46           C  
ANISOU 1372  CG  GLN A 174     5243   6180   5846    -91    305   -600       C  
ATOM   1373  CD  GLN A 174     -16.183  35.667 -16.343  1.00 49.66           C  
ANISOU 1373  CD  GLN A 174     5743   6727   6397   -136    285   -658       C  
ATOM   1374  NE2 GLN A 174     -16.269  35.952 -15.058  1.00 50.71           N  
ANISOU 1374  NE2 GLN A 174     5870   6859   6535   -172    273   -702       N  
ATOM   1375  OE1 GLN A 174     -15.138  35.260 -16.879  1.00 50.76           O  
ANISOU 1375  OE1 GLN A 174     5859   6884   6543   -135    278   -664       O  
ATOM   1376  N   GLY A 175     -17.697  36.706 -20.590  1.00 48.88           N  
ANISOU 1376  N   GLY A 175     5698   6591   6282     21    426   -468       N  
ATOM   1377  CA  GLY A 175     -17.665  38.033 -21.204  1.00 47.61           C  
ANISOU 1377  CA  GLY A 175     5545   6381   6161     36    521   -432       C  
ATOM   1378  C   GLY A 175     -18.832  38.311 -22.100  1.00 51.76           C  
ANISOU 1378  C   GLY A 175     6094   6915   6654    101    549   -367       C  
ATOM   1379  O   GLY A 175     -19.478  39.323 -21.969  1.00 51.36           O  
ANISOU 1379  O   GLY A 175     6061   6825   6625    108    608   -342       O  
ATOM   1380  N   LYS A 176     -19.126  37.398 -23.013  1.00 51.66           N  
ANISOU 1380  N   LYS A 176     6080   6958   6587    150    507   -341       N  
ATOM   1381  CA  LYS A 176     -20.167  37.651 -23.969  1.00 51.68           C  
ANISOU 1381  CA  LYS A 176     6099   6984   6553    218    532   -282       C  
ATOM   1382  C   LYS A 176     -21.474  37.846 -23.250  1.00 53.08           C  
ANISOU 1382  C   LYS A 176     6294   7155   6716    218    518   -280       C  
ATOM   1383  O   LYS A 176     -22.221  38.680 -23.655  1.00 52.52           O  
ANISOU 1383  O   LYS A 176     6239   7072   6644    257    573   -232       O  
ATOM   1384  CB  LYS A 176     -20.368  36.487 -24.937  1.00 56.95           C  
ANISOU 1384  CB  LYS A 176     6755   7723   7158    266    475   -272       C  
ATOM   1385  CG  LYS A 176     -19.489  36.397 -26.186  1.00 60.21           C  
ANISOU 1385  CG  LYS A 176     7156   8159   7563    304    502   -245       C  
ATOM   1386  CD  LYS A 176     -19.098  34.930 -26.362  1.00 71.03           C  
ANISOU 1386  CD  LYS A 176     8506   9580   8898    298    420   -283       C  
ATOM   1387  CE  LYS A 176     -18.647  34.513 -27.737  1.00 82.04           C  
ANISOU 1387  CE  LYS A 176     9889  11023  10259    351    425   -259       C  
ATOM   1388  NZ  LYS A 176     -18.165  33.108 -27.638  1.00 77.21           N1+
ANISOU 1388  NZ  LYS A 176     9258  10445   9630    329    349   -306       N1+
ATOM   1389  N   ARG A 177     -21.765  37.051 -22.217  1.00 52.66           N  
ANISOU 1389  N   ARG A 177     6240   7114   6653    178    448   -327       N  
ATOM   1390  CA  ARG A 177     -23.023  37.144 -21.509  1.00 53.04           C  
ANISOU 1390  CA  ARG A 177     6305   7159   6688    177    432   -326       C  
ATOM   1391  C   ARG A 177     -23.101  38.281 -20.490  1.00 53.39           C  
ANISOU 1391  C   ARG A 177     6363   7140   6780    136    483   -338       C  
ATOM   1392  O   ARG A 177     -24.162  38.540 -19.944  1.00 46.72           O  
ANISOU 1392  O   ARG A 177     5535   6286   5929    139    482   -331       O  
ATOM   1393  CB  ARG A 177     -23.326  35.844 -20.725  1.00 56.01           C  
ANISOU 1393  CB  ARG A 177     6674   7567   7037    152    343   -370       C  
ATOM   1394  CG  ARG A 177     -23.399  34.554 -21.500  1.00 51.38           C  
ANISOU 1394  CG  ARG A 177     6072   7039   6407    183    286   -373       C  
ATOM   1395  CD  ARG A 177     -24.126  34.663 -22.818  1.00 53.74           C  
ANISOU 1395  CD  ARG A 177     6371   7378   6669    251    304   -329       C  
ATOM   1396  NE  ARG A 177     -23.429  33.821 -23.779  1.00 57.36           N  
ANISOU 1396  NE  ARG A 177     6809   7879   7104    273    278   -334       N  
ATOM   1397  CZ  ARG A 177     -23.554  33.916 -25.094  1.00 60.79           C  
ANISOU 1397  CZ  ARG A 177     7237   8355   7506    332    299   -300       C  
ATOM   1398  NH1 ARG A 177     -24.365  34.823 -25.612  1.00 63.76           N1+
ANISOU 1398  NH1 ARG A 177     7622   8736   7865    380    347   -252       N1+
ATOM   1399  NH2 ARG A 177     -22.844  33.111 -25.882  1.00 65.52           N  
ANISOU 1399  NH2 ARG A 177     7817   8991   8086    347    274   -312       N  
ATOM   1400  N   GLY A 178     -21.980  38.874 -20.134  1.00 48.92           N  
ANISOU 1400  N   GLY A 178     5787   6532   6265     93    521   -365       N  
ATOM   1401  CA  GLY A 178     -21.996  39.969 -19.157  1.00 46.31           C  
ANISOU 1401  CA  GLY A 178     5465   6142   5986     49    573   -388       C  
ATOM   1402  C   GLY A 178     -22.143  39.449 -17.744  1.00 45.75           C  
ANISOU 1402  C   GLY A 178     5392   6080   5908      0    510   -446       C  
ATOM   1403  O   GLY A 178     -22.473  40.179 -16.826  1.00 47.49           O  
ANISOU 1403  O   GLY A 178     5622   6265   6157    -32    537   -468       O  
ATOM   1404  N   TRP A 179     -21.869  38.178 -17.556  1.00 46.45           N  
ANISOU 1404  N   TRP A 179     5468   6218   5961     -5    430   -470       N  
ATOM   1405  CA  TRP A 179     -21.897  37.593 -16.229  1.00 47.22           C  
ANISOU 1405  CA  TRP A 179     5561   6330   6048    -45    372   -520       C  
ATOM   1406  C   TRP A 179     -20.857  38.173 -15.234  1.00 51.08           C  
ANISOU 1406  C   TRP A 179     6031   6796   6578   -105    389   -580       C  
ATOM   1407  O   TRP A 179     -19.853  38.699 -15.607  1.00 49.06           O  
ANISOU 1407  O   TRP A 179     5757   6521   6360   -122    430   -593       O  
ATOM   1408  CB  TRP A 179     -21.677  36.084 -16.300  1.00 42.50           C  
ANISOU 1408  CB  TRP A 179     4951   5786   5409    -34    293   -530       C  
ATOM   1409  CG  TRP A 179     -22.706  35.296 -17.023  1.00 42.50           C  
ANISOU 1409  CG  TRP A 179     4962   5818   5368     13    262   -492       C  
ATOM   1410  CD1 TRP A 179     -23.962  35.731 -17.449  1.00 44.89           C  
ANISOU 1410  CD1 TRP A 179     5284   6113   5657     49    286   -453       C  
ATOM   1411  CD2 TRP A 179     -22.637  33.912 -17.372  1.00 38.64           C  
ANISOU 1411  CD2 TRP A 179     4461   5372   4846     31    201   -496       C  
ATOM   1412  CE2 TRP A 179     -23.846  33.590 -18.058  1.00 42.01           C  
ANISOU 1412  CE2 TRP A 179     4898   5819   5244     75    192   -465       C  
ATOM   1413  CE3 TRP A 179     -21.664  32.923 -17.221  1.00 43.42           C  
ANISOU 1413  CE3 TRP A 179     5045   6003   5446     17    158   -523       C  
ATOM   1414  NE1 TRP A 179     -24.617  34.713 -18.077  1.00 40.93           N  
ANISOU 1414  NE1 TRP A 179     4779   5654   5117     86    242   -438       N  
ATOM   1415  CZ2 TRP A 179     -24.113  32.319 -18.570  1.00 41.79           C  
ANISOU 1415  CZ2 TRP A 179     4859   5832   5187     99    143   -467       C  
ATOM   1416  CZ3 TRP A 179     -21.920  31.644 -17.752  1.00 39.01           C  
ANISOU 1416  CZ3 TRP A 179     4480   5481   4859     44    111   -518       C  
ATOM   1417  CH2 TRP A 179     -23.151  31.353 -18.399  1.00 42.30           C  
ANISOU 1417  CH2 TRP A 179     4905   5913   5252     82    105   -494       C  
ATOM   1418  N   GLY A 180     -21.089  37.976 -13.941  1.00 50.71           N  
ANISOU 1418  N   GLY A 180     5985   6759   6521   -135    353   -621       N  
ATOM   1419  CA  GLY A 180     -20.082  38.291 -12.954  1.00 48.96           C  
ANISOU 1419  CA  GLY A 180     5738   6538   6326   -188    352   -688       C  
ATOM   1420  C   GLY A 180     -18.999  37.236 -12.825  1.00 49.43           C  
ANISOU 1420  C   GLY A 180     5767   6649   6364   -196    292   -716       C  
ATOM   1421  O   GLY A 180     -18.787  36.364 -13.686  1.00 50.80           O  
ANISOU 1421  O   GLY A 180     5938   6848   6515   -165    264   -685       O  
ATOM   1422  N   GLN A 181     -18.359  37.283 -11.681  1.00 49.45           N  
ANISOU 1422  N   GLN A 181     5746   6672   6368   -235    271   -778       N  
ATOM   1423  CA  GLN A 181     -17.193  36.491 -11.419  1.00 57.60           C  
ANISOU 1423  CA  GLN A 181     6743   7754   7386   -246    223   -812       C  
ATOM   1424  C   GLN A 181     -17.598  35.024 -11.276  1.00 53.78           C  
ANISOU 1424  C   GLN A 181     6269   7317   6846   -210    151   -784       C  
ATOM   1425  O   GLN A 181     -18.729  34.716 -10.843  1.00 43.86           O  
ANISOU 1425  O   GLN A 181     5040   6061   5563   -193    133   -762       O  
ATOM   1426  CB  GLN A 181     -16.524  36.992 -10.139  1.00 60.20           C  
ANISOU 1426  CB  GLN A 181     7042   8103   7726   -294    219   -890       C  
ATOM   1427  CG  GLN A 181     -17.288  36.559  -8.886  1.00 74.70           C  
ANISOU 1427  CG  GLN A 181     8891   9972   9518   -289    173   -902       C  
ATOM   1428  CD  GLN A 181     -16.770  37.187  -7.600  1.00 84.73           C  
ANISOU 1428  CD  GLN A 181    10131  11266  10794   -333    174   -983       C  
ATOM   1429  NE2 GLN A 181     -15.433  37.287  -7.454  1.00 84.16           N  
ANISOU 1429  NE2 GLN A 181    10080  11186  10711   -340    179   -995       N  
ATOM   1430  OE1 GLN A 181     -17.563  37.567  -6.742  1.00 96.63           O  
ANISOU 1430  OE1 GLN A 181    11595  12802  12316   -360    170  -1037       O  
ATOM   1431  N   LEU A 182     -16.674  34.146 -11.672  1.00 43.68           N  
ANISOU 1431  N   LEU A 182     4966   6073   5554   -200    118   -784       N  
ATOM   1432  CA  LEU A 182     -16.701  32.766 -11.275  1.00 44.33           C  
ANISOU 1432  CA  LEU A 182     5046   6203   5592   -175     54   -773       C  
ATOM   1433  C   LEU A 182     -16.650  32.717  -9.758  1.00 43.83           C  
ANISOU 1433  C   LEU A 182     4971   6174   5506   -192     25   -815       C  
ATOM   1434  O   LEU A 182     -15.705  33.201  -9.208  1.00 47.77           O  
ANISOU 1434  O   LEU A 182     5437   6694   6016   -223     28   -867       O  
ATOM   1435  CB  LEU A 182     -15.474  32.051 -11.793  1.00 45.68           C  
ANISOU 1435  CB  LEU A 182     5187   6406   5763   -169     32   -779       C  
ATOM   1436  CG  LEU A 182     -15.356  30.537 -11.476  1.00 47.25           C  
ANISOU 1436  CG  LEU A 182     5380   6651   5922   -139    -25   -763       C  
ATOM   1437  CD1 LEU A 182     -16.419  29.768 -12.223  1.00 43.92           C  
ANISOU 1437  CD1 LEU A 182     4988   6211   5485   -102    -34   -713       C  
ATOM   1438  CD2 LEU A 182     -13.994  29.948 -11.868  1.00 47.16           C  
ANISOU 1438  CD2 LEU A 182     5334   6673   5912   -137    -43   -775       C  
ATOM   1439  N   THR A 183     -17.609  32.105  -9.077  1.00 41.84           N  
ANISOU 1439  N   THR A 183     4742   5934   5221   -171     -3   -795       N  
ATOM   1440  CA  THR A 183     -17.546  32.017  -7.624  1.00 41.71           C  
ANISOU 1440  CA  THR A 183     4713   5958   5175   -180    -30   -830       C  
ATOM   1441  C   THR A 183     -17.043  30.722  -7.076  1.00 43.50           C  
ANISOU 1441  C   THR A 183     4922   6242   5361   -151    -81   -824       C  
ATOM   1442  O   THR A 183     -16.478  30.695  -5.972  1.00 48.22           O  
ANISOU 1442  O   THR A 183     5495   6892   5932   -157   -104   -862       O  
ATOM   1443  CB  THR A 183     -18.935  32.267  -6.965  1.00 42.57           C  
ANISOU 1443  CB  THR A 183     4857   6043   5271   -173    -22   -815       C  
ATOM   1444  CG2 THR A 183     -19.509  33.587  -7.394  1.00 38.97           C  
ANISOU 1444  CG2 THR A 183     4420   5529   4854   -197     32   -818       C  
ATOM   1445  OG1 THR A 183     -19.818  31.165  -7.296  1.00 40.79           O  
ANISOU 1445  OG1 THR A 183     4657   5813   5027   -133    -45   -760       O  
ATOM   1446  N   SER A 184     -17.290  29.609  -7.737  1.00 40.89           N  
ANISOU 1446  N   SER A 184     4604   5909   5023   -117    -99   -776       N  
ATOM   1447  CA  SER A 184     -16.926  28.313  -7.142  1.00 40.34           C  
ANISOU 1447  CA  SER A 184     4521   5888   4918    -84   -140   -762       C  
ATOM   1448  C   SER A 184     -16.954  27.270  -8.242  1.00 42.18           C  
ANISOU 1448  C   SER A 184     4761   6105   5160    -56   -147   -720       C  
ATOM   1449  O   SER A 184     -17.546  27.509  -9.286  1.00 37.00           O  
ANISOU 1449  O   SER A 184     4123   5405   4527    -58   -125   -701       O  
ATOM   1450  CB  SER A 184     -17.918  27.930  -6.051  1.00 48.16           C  
ANISOU 1450  CB  SER A 184     5533   6886   5877    -63   -153   -746       C  
ATOM   1451  OG  SER A 184     -19.263  28.334  -6.390  1.00 48.85           O  
ANISOU 1451  OG  SER A 184     5658   6919   5983    -66   -128   -723       O  
ATOM   1452  N   ASN A 185     -16.224  26.184  -8.036  1.00 42.09           N  
ANISOU 1452  N   ASN A 185     4728   6132   5130    -31   -174   -711       N  
ATOM   1453  CA  ASN A 185     -16.280  24.994  -8.828  1.00 41.17           C  
ANISOU 1453  CA  ASN A 185     4617   6006   5021     -1   -181   -674       C  
ATOM   1454  C   ASN A 185     -16.553  23.884  -7.812  1.00 45.39           C  
ANISOU 1454  C   ASN A 185     5153   6565   5527     35   -200   -649       C  
ATOM   1455  O   ASN A 185     -15.673  23.456  -7.087  1.00 48.09           O  
ANISOU 1455  O   ASN A 185     5470   6958   5844     51   -219   -655       O  
ATOM   1456  CB  ASN A 185     -14.946  24.709  -9.501  1.00 41.19           C  
ANISOU 1456  CB  ASN A 185     4588   6031   5031     -2   -188   -683       C  
ATOM   1457  CG  ASN A 185     -14.628  25.662 -10.643  1.00 47.58           C  
ANISOU 1457  CG  ASN A 185     5395   6812   5871    -30   -162   -699       C  
ATOM   1458  ND2 ASN A 185     -15.334  25.515 -11.745  1.00 43.78           N  
ANISOU 1458  ND2 ASN A 185     4935   6291   5406    -21   -147   -673       N  
ATOM   1459  OD1 ASN A 185     -13.760  26.542 -10.531  1.00 50.80           O  
ANISOU 1459  OD1 ASN A 185     5779   7233   6288    -59   -153   -734       O  
ATOM   1460  N   LEU A 186     -17.765  23.401  -7.769  1.00 42.58           N  
ANISOU 1460  N   LEU A 186     4825   6175   5176     51   -192   -620       N  
ATOM   1461  CA  LEU A 186     -18.090  22.220  -6.971  1.00 42.28           C  
ANISOU 1461  CA  LEU A 186     4792   6149   5123     91   -198   -588       C  
ATOM   1462  C   LEU A 186     -17.741  20.922  -7.647  1.00 44.23           C  
ANISOU 1462  C   LEU A 186     5029   6388   5387    118   -198   -562       C  
ATOM   1463  O   LEU A 186     -18.127  20.695  -8.814  1.00 42.14           O  
ANISOU 1463  O   LEU A 186     4773   6085   5153    112   -187   -559       O  
ATOM   1464  CB  LEU A 186     -19.615  22.216  -6.677  1.00 42.66           C  
ANISOU 1464  CB  LEU A 186     4872   6155   5179     95   -183   -569       C  
ATOM   1465  CG  LEU A 186     -20.144  21.384  -5.478  1.00 42.10           C  
ANISOU 1465  CG  LEU A 186     4811   6095   5090    132   -180   -539       C  
ATOM   1466  CD1 LEU A 186     -19.630  21.939  -4.150  1.00 42.87           C  
ANISOU 1466  CD1 LEU A 186     4898   6249   5142    136   -195   -554       C  
ATOM   1467  CD2 LEU A 186     -21.673  21.353  -5.504  1.00 41.89           C  
ANISOU 1467  CD2 LEU A 186     4814   6016   5084    131   -160   -523       C  
ATOM   1468  N   LEU A 187     -17.087  20.051  -6.878  1.00 43.10           N  
ANISOU 1468  N   LEU A 187     4869   6282   5223    153   -207   -543       N  
ATOM   1469  CA  LEU A 187     -16.719  18.702  -7.273  1.00 40.85           C  
ANISOU 1469  CA  LEU A 187     4574   5990   4954    187   -201   -513       C  
ATOM   1470  C   LEU A 187     -17.720  17.825  -6.615  1.00 41.96           C  
ANISOU 1470  C   LEU A 187     4735   6105   5102    219   -181   -477       C  
ATOM   1471  O   LEU A 187     -17.913  17.909  -5.388  1.00 40.28           O  
ANISOU 1471  O   LEU A 187     4526   5919   4856    239   -182   -463       O  
ATOM   1472  CB  LEU A 187     -15.342  18.346  -6.703  1.00 45.19           C  
ANISOU 1472  CB  LEU A 187     5092   6605   5474    212   -218   -510       C  
ATOM   1473  CG  LEU A 187     -14.944  16.865  -6.802  1.00 47.06           C  
ANISOU 1473  CG  LEU A 187     5319   6839   5723    258   -205   -470       C  
ATOM   1474  CD1 LEU A 187     -14.807  16.397  -8.216  1.00 45.02           C  
ANISOU 1474  CD1 LEU A 187     5059   6539   5507    245   -195   -474       C  
ATOM   1475  CD2 LEU A 187     -13.595  16.608  -6.156  1.00 50.20           C  
ANISOU 1475  CD2 LEU A 187     5680   7309   6082    288   -223   -464       C  
ATOM   1476  N   LEU A 188     -18.378  17.020  -7.415  1.00 39.54           N  
ANISOU 1476  N   LEU A 188     4439   5746   4838    223   -160   -464       N  
ATOM   1477  CA  LEU A 188     -19.438  16.184  -6.957  1.00 42.16           C  
ANISOU 1477  CA  LEU A 188     4788   6038   5192    247   -132   -435       C  
ATOM   1478  C   LEU A 188     -19.087  14.770  -7.274  1.00 40.34           C  
ANISOU 1478  C   LEU A 188     4544   5789   4992    280   -110   -410       C  
ATOM   1479  O   LEU A 188     -18.819  14.443  -8.395  1.00 44.09           O  
ANISOU 1479  O   LEU A 188     5009   6245   5498    267   -108   -427       O  
ATOM   1480  CB  LEU A 188     -20.730  16.567  -7.665  1.00 39.29           C  
ANISOU 1480  CB  LEU A 188     4444   5623   4862    216   -122   -455       C  
ATOM   1481  CG  LEU A 188     -21.272  17.947  -7.381  1.00 42.85           C  
ANISOU 1481  CG  LEU A 188     4910   6083   5288    186   -136   -476       C  
ATOM   1482  CD1 LEU A 188     -21.552  18.731  -8.632  1.00 48.50           C  
ANISOU 1482  CD1 LEU A 188     5630   6780   6018    150   -140   -507       C  
ATOM   1483  CD2 LEU A 188     -22.511  17.846  -6.549  1.00 39.88           C  
ANISOU 1483  CD2 LEU A 188     4555   5680   4916    198   -117   -457       C  
ATOM   1484  N   ILE A 189     -19.117  13.914  -6.287  1.00 38.52           N  
ANISOU 1484  N   ILE A 189     4314   5562   4757    325    -88   -367       N  
ATOM   1485  CA  ILE A 189     -18.808  12.517  -6.553  1.00 40.91           C  
ANISOU 1485  CA  ILE A 189     4605   5838   5097    360    -55   -338       C  
ATOM   1486  C   ILE A 189     -19.873  11.672  -5.884  1.00 45.73           C  
ANISOU 1486  C   ILE A 189     5232   6400   5741    389     -9   -302       C  
ATOM   1487  O   ILE A 189     -20.100  11.798  -4.669  1.00 42.41           O  
ANISOU 1487  O   ILE A 189     4822   6003   5287    419     -3   -270       O  
ATOM   1488  CB  ILE A 189     -17.396  12.095  -6.043  1.00 39.57           C  
ANISOU 1488  CB  ILE A 189     4412   5727   4893    401    -64   -310       C  
ATOM   1489  CG1 ILE A 189     -16.329  12.966  -6.622  1.00 42.06           C  
ANISOU 1489  CG1 ILE A 189     4709   6090   5179    370   -106   -348       C  
ATOM   1490  CG2 ILE A 189     -17.123  10.691  -6.530  1.00 45.28           C  
ANISOU 1490  CG2 ILE A 189     5125   6411   5665    431    -24   -284       C  
ATOM   1491  CD1 ILE A 189     -14.898  12.647  -6.178  1.00 46.11           C  
ANISOU 1491  CD1 ILE A 189     5192   6669   5656    407   -120   -329       C  
ATOM   1492  N   GLY A 190     -20.537  10.822  -6.664  1.00 46.95           N  
ANISOU 1492  N   GLY A 190     5387   6489   5962    381     25   -310       N  
ATOM   1493  CA  GLY A 190     -21.801  10.237  -6.192  1.00 47.39           C  
ANISOU 1493  CA  GLY A 190     5458   6487   6061    393     70   -292       C  
ATOM   1494  C   GLY A 190     -21.832   8.802  -6.563  1.00 46.51           C  
ANISOU 1494  C   GLY A 190     5334   6319   6017    416    124   -276       C  
ATOM   1495  O   GLY A 190     -21.083   8.367  -7.438  1.00 48.88           O  
ANISOU 1495  O   GLY A 190     5617   6620   6336    411    122   -293       O  
ATOM   1496  N   MET A 191     -22.692   8.089  -5.867  1.00 42.28           N  
ANISOU 1496  N   MET A 191     4808   5735   5521    442    178   -244       N  
ATOM   1497  CA  MET A 191     -22.865   6.713  -6.029  1.00 46.58           C  
ANISOU 1497  CA  MET A 191     5343   6216   6140    467    244   -225       C  
ATOM   1498  C   MET A 191     -24.028   6.586  -6.941  1.00 52.26           C  
ANISOU 1498  C   MET A 191     6056   6873   6924    419    259   -283       C  
ATOM   1499  O   MET A 191     -24.944   7.443  -6.987  1.00 52.91           O  
ANISOU 1499  O   MET A 191     6150   6959   6994    385    233   -313       O  
ATOM   1500  CB  MET A 191     -23.178   6.031  -4.666  1.00 53.76           C  
ANISOU 1500  CB  MET A 191     6265   7104   7057    527    302   -152       C  
ATOM   1501  CG  MET A 191     -21.988   6.004  -3.686  1.00 59.73           C  
ANISOU 1501  CG  MET A 191     7019   7931   7742    589    292    -89       C  
ATOM   1502  SD  MET A 191     -22.408   5.372  -2.023  1.00 61.60           S  
ANISOU 1502  SD  MET A 191     7273   8161   7971    669    358      2       S  
ATOM   1503  CE  MET A 191     -23.276   3.874  -2.456  1.00 63.23           C  
ANISOU 1503  CE  MET A 191     7474   8242   8306    676    459     12       C  
ATOM   1504  N   GLU A 192     -24.002   5.508  -7.685  1.00 50.11           N  
ANISOU 1504  N   GLU A 192     5764   6549   6724    417    302   -302       N  
ATOM   1505  CA  GLU A 192     -25.032   5.253  -8.680  1.00 52.31           C  
ANISOU 1505  CA  GLU A 192     6028   6777   7070    372    317   -370       C  
ATOM   1506  C   GLU A 192     -26.390   5.302  -8.029  1.00 48.22           C  
ANISOU 1506  C   GLU A 192     5522   6217   6583    367    348   -366       C  
ATOM   1507  O   GLU A 192     -26.533   4.804  -6.949  1.00 46.82           O  
ANISOU 1507  O   GLU A 192     5356   6013   6418    409    397   -306       O  
ATOM   1508  CB  GLU A 192     -24.781   3.867  -9.276  1.00 51.16           C  
ANISOU 1508  CB  GLU A 192     5858   6573   7006    381    378   -383       C  
ATOM   1509  CG  GLU A 192     -24.760   2.749  -8.256  1.00 52.59           C  
ANISOU 1509  CG  GLU A 192     6043   6699   7236    435    460   -314       C  
ATOM   1510  CD  GLU A 192     -24.318   1.397  -8.856  1.00 55.77           C  
ANISOU 1510  CD  GLU A 192     6423   7045   7722    446    524   -324       C  
ATOM   1511  OE1 GLU A 192     -24.056   1.268 -10.098  1.00 49.76           O  
ANISOU 1511  OE1 GLU A 192     5638   6285   6981    410    504   -390       O  
ATOM   1512  OE2 GLU A 192     -24.240   0.475  -8.014  1.00 51.20           O1-
ANISOU 1512  OE2 GLU A 192     5848   6420   7185    497    599   -259       O1-
ATOM   1513  N   GLY A 193     -27.378   5.908  -8.679  1.00 53.45           N  
ANISOU 1513  N   GLY A 193     6178   6876   7253    321    322   -426       N  
ATOM   1514  CA  GLY A 193     -28.731   5.986  -8.138  1.00 55.45           C  
ANISOU 1514  CA  GLY A 193     6439   7090   7539    313    350   -428       C  
ATOM   1515  C   GLY A 193     -28.936   7.179  -7.194  1.00 53.89           C  
ANISOU 1515  C   GLY A 193     6273   6938   7265    320    311   -391       C  
ATOM   1516  O   GLY A 193     -30.029   7.426  -6.761  1.00 51.84           O  
ANISOU 1516  O   GLY A 193     6021   6653   7020    311    325   -393       O  
ATOM   1517  N   ASN A 194     -27.891   7.929  -6.884  1.00 47.03           N  
ANISOU 1517  N   ASN A 194     5418   6134   6315    333    262   -363       N  
ATOM   1518  CA  ASN A 194     -28.063   9.131  -6.079  1.00 47.99           C  
ANISOU 1518  CA  ASN A 194     5565   6301   6367    334    223   -342       C  
ATOM   1519  C   ASN A 194     -28.889  10.173  -6.858  1.00 45.31           C  
ANISOU 1519  C   ASN A 194     5225   5973   6016    284    182   -399       C  
ATOM   1520  O   ASN A 194     -28.664  10.383  -8.043  1.00 44.30           O  
ANISOU 1520  O   ASN A 194     5080   5860   5889    256    153   -447       O  
ATOM   1521  CB  ASN A 194     -26.705   9.771  -5.755  1.00 48.09           C  
ANISOU 1521  CB  ASN A 194     5585   6387   6301    350    177   -318       C  
ATOM   1522  CG  ASN A 194     -25.990   9.118  -4.573  1.00 51.06           C  
ANISOU 1522  CG  ASN A 194     5966   6776   6657    410    208   -249       C  
ATOM   1523  ND2 ASN A 194     -24.950   9.795  -4.089  1.00 54.56           N  
ANISOU 1523  ND2 ASN A 194     6413   7292   7024    426    165   -232       N  
ATOM   1524  OD1 ASN A 194     -26.367   8.042  -4.085  1.00 52.05           O  
ANISOU 1524  OD1 ASN A 194     6092   6851   6834    445    271   -212       O  
ATOM   1525  N   VAL A 195     -29.737  10.918  -6.135  1.00 47.19           N  
ANISOU 1525  N   VAL A 195     5484   6213   6231    280    177   -387       N  
ATOM   1526  CA  VAL A 195     -30.541  11.986  -6.713  1.00 42.13           C  
ANISOU 1526  CA  VAL A 195     4845   5585   5574    241    142   -430       C  
ATOM   1527  C   VAL A 195     -30.372  13.254  -5.938  1.00 39.63           C  
ANISOU 1527  C   VAL A 195     4556   5314   5187    242    108   -408       C  
ATOM   1528  O   VAL A 195     -30.375  13.236  -4.696  1.00 37.59           O  
ANISOU 1528  O   VAL A 195     4316   5059   4907    270    124   -363       O  
ATOM   1529  CB  VAL A 195     -32.047  11.570  -6.693  1.00 47.38           C  
ANISOU 1529  CB  VAL A 195     5504   6195   6302    230    181   -448       C  
ATOM   1530  CG1 VAL A 195     -32.935  12.723  -7.097  1.00 44.58           C  
ANISOU 1530  CG1 VAL A 195     5154   5859   5923    199    148   -481       C  
ATOM   1531  CG2 VAL A 195     -32.256  10.307  -7.551  1.00 49.46           C  
ANISOU 1531  CG2 VAL A 195     5734   6412   6646    223    219   -485       C  
ATOM   1532  N   THR A 196     -30.250  14.356  -6.640  1.00 36.93           N  
ANISOU 1532  N   THR A 196     4214   5008   4807    212     63   -440       N  
ATOM   1533  CA  THR A 196     -30.335  15.663  -6.050  1.00 37.01           C  
ANISOU 1533  CA  THR A 196     4248   5051   4760    203     36   -431       C  
ATOM   1534  C   THR A 196     -31.661  16.211  -6.514  1.00 38.76           C  
ANISOU 1534  C   THR A 196     4471   5251   5003    179     38   -459       C  
ATOM   1535  O   THR A 196     -31.820  16.486  -7.664  1.00 37.58           O  
ANISOU 1535  O   THR A 196     4305   5107   4865    158     22   -497       O  
ATOM   1536  CB  THR A 196     -29.225  16.596  -6.542  1.00 40.99           C  
ANISOU 1536  CB  THR A 196     4751   5606   5216    188     -5   -447       C  
ATOM   1537  CG2 THR A 196     -29.464  17.987  -6.113  1.00 41.30           C  
ANISOU 1537  CG2 THR A 196     4810   5668   5213    172    -24   -449       C  
ATOM   1538  OG1 THR A 196     -27.973  16.182  -6.039  1.00 41.21           O  
ANISOU 1538  OG1 THR A 196     4773   5663   5222    210    -10   -425       O  
ATOM   1539  N   PRO A 197     -32.596  16.371  -5.596  1.00 36.37           N  
ANISOU 1539  N   PRO A 197     4185   4926   4706    186     59   -439       N  
ATOM   1540  CA  PRO A 197     -33.978  16.802  -5.913  1.00 40.79           C  
ANISOU 1540  CA  PRO A 197     4745   5464   5289    167     65   -461       C  
ATOM   1541  C   PRO A 197     -34.001  18.232  -6.411  1.00 39.01           C  
ANISOU 1541  C   PRO A 197     4529   5273   5020    145     31   -479       C  
ATOM   1542  O   PRO A 197     -33.078  18.982  -6.143  1.00 38.80           O  
ANISOU 1542  O   PRO A 197     4515   5280   4947    143      9   -469       O  
ATOM   1543  CB  PRO A 197     -34.689  16.784  -4.568  1.00 41.51           C  
ANISOU 1543  CB  PRO A 197     4858   5531   5381    184     94   -425       C  
ATOM   1544  CG  PRO A 197     -33.882  15.902  -3.705  1.00 43.45           C  
ANISOU 1544  CG  PRO A 197     5108   5775   5625    218    115   -386       C  
ATOM   1545  CD  PRO A 197     -32.444  16.095  -4.153  1.00 38.70           C  
ANISOU 1545  CD  PRO A 197     4499   5218   4984    217     81   -392       C  
ATOM   1546  N   ALA A 198     -35.059  18.539  -7.124  1.00 36.06           N  
ANISOU 1546  N   ALA A 198     4145   4889   4664    131     31   -504       N  
ATOM   1547  CA  ALA A 198     -35.207  19.719  -7.913  1.00 35.66           C  
ANISOU 1547  CA  ALA A 198     4095   4868   4585    115      7   -524       C  
ATOM   1548  C   ALA A 198     -35.056  20.982  -7.118  1.00 37.84           C  
ANISOU 1548  C   ALA A 198     4402   5157   4817    111      0   -501       C  
ATOM   1549  O   ALA A 198     -35.618  21.118  -6.083  1.00 33.13           O  
ANISOU 1549  O   ALA A 198     3825   4542   4220    117     17   -479       O  
ATOM   1550  CB  ALA A 198     -36.551  19.691  -8.586  1.00 38.54           C  
ANISOU 1550  CB  ALA A 198     4442   5220   4979    110     16   -548       C  
ATOM   1551  N   HIS A 199     -34.291  21.901  -7.662  1.00 35.71           N  
ANISOU 1551  N   HIS A 199     4136   4918   4514    101    -19   -507       N  
ATOM   1552  CA  HIS A 199     -34.015  23.180  -7.068  1.00 33.78           C  
ANISOU 1552  CA  HIS A 199     3915   4685   4233     91    -22   -497       C  
ATOM   1553  C   HIS A 199     -33.569  24.083  -8.158  1.00 31.81           C  
ANISOU 1553  C   HIS A 199     3660   4457   3967     81    -33   -510       C  
ATOM   1554  O   HIS A 199     -33.332  23.621  -9.292  1.00 32.24           O  
ANISOU 1554  O   HIS A 199     3692   4524   4031     85    -42   -525       O  
ATOM   1555  CB  HIS A 199     -32.915  23.116  -6.007  1.00 36.43           C  
ANISOU 1555  CB  HIS A 199     4262   5036   4544     95    -28   -484       C  
ATOM   1556  CG  HIS A 199     -31.624  22.613  -6.553  1.00 36.74           C  
ANISOU 1556  CG  HIS A 199     4283   5098   4578     97    -45   -492       C  
ATOM   1557  CD2 HIS A 199     -30.543  23.258  -7.041  1.00 39.07           C  
ANISOU 1557  CD2 HIS A 199     4572   5420   4852     84    -60   -505       C  
ATOM   1558  ND1 HIS A 199     -31.400  21.276  -6.767  1.00 36.45           N  
ANISOU 1558  ND1 HIS A 199     4229   5053   4566    112    -42   -489       N  
ATOM   1559  CE1 HIS A 199     -30.260  21.116  -7.375  1.00 39.21           C  
ANISOU 1559  CE1 HIS A 199     4563   5425   4907    111    -57   -498       C  
ATOM   1560  NE2 HIS A 199     -29.690  22.296  -7.510  1.00 39.38           N  
ANISOU 1560  NE2 HIS A 199     4591   5469   4900     94    -69   -507       N  
ATOM   1561  N   TYR A 200     -33.513  25.374  -7.844  1.00 33.46           N  
ANISOU 1561  N   TYR A 200     3888   4670   4154     70    -27   -505       N  
ATOM   1562  CA  TYR A 200     -32.912  26.379  -8.699  1.00 35.95           C  
ANISOU 1562  CA  TYR A 200     4201   5000   4455     61    -27   -512       C  
ATOM   1563  C   TYR A 200     -31.795  27.109  -7.946  1.00 37.55           C  
ANISOU 1563  C   TYR A 200     4415   5212   4639     44    -27   -516       C  
ATOM   1564  O   TYR A 200     -31.715  27.083  -6.698  1.00 32.98           O  
ANISOU 1564  O   TYR A 200     3848   4632   4049     40    -27   -514       O  
ATOM   1565  CB  TYR A 200     -33.918  27.369  -9.231  1.00 36.67           C  
ANISOU 1565  CB  TYR A 200     4301   5084   4546     64     -9   -505       C  
ATOM   1566  CG  TYR A 200     -34.546  28.267  -8.196  1.00 36.36           C  
ANISOU 1566  CG  TYR A 200     4288   5024   4503     55      9   -494       C  
ATOM   1567  CD1 TYR A 200     -35.716  27.918  -7.508  1.00 33.78           C  
ANISOU 1567  CD1 TYR A 200     3969   4679   4186     61     16   -486       C  
ATOM   1568  CD2 TYR A 200     -34.062  29.534  -8.014  1.00 34.81           C  
ANISOU 1568  CD2 TYR A 200     4105   4824   4296     40     27   -495       C  
ATOM   1569  CE1 TYR A 200     -36.257  28.806  -6.535  1.00 36.46           C  
ANISOU 1569  CE1 TYR A 200     4334   5000   4520     53     36   -477       C  
ATOM   1570  CE2 TYR A 200     -34.588  30.395  -7.080  1.00 35.51           C  
ANISOU 1570  CE2 TYR A 200     4217   4893   4382     29     48   -490       C  
ATOM   1571  CZ  TYR A 200     -35.722  30.012  -6.361  1.00 35.29           C  
ANISOU 1571  CZ  TYR A 200     4198   4849   4358     38     51   -480       C  
ATOM   1572  OH  TYR A 200     -36.188  30.873  -5.506  1.00 35.07           O  
ANISOU 1572  OH  TYR A 200     4193   4804   4327     28     72   -477       O  
ATOM   1573  N   GLU A 201     -30.930  27.745  -8.731  1.00 31.87           N  
ANISOU 1573  N   GLU A 201     3688   4505   3914     35    -26   -524       N  
ATOM   1574  CA  GLU A 201     -29.727  28.466  -8.228  1.00 35.50           C  
ANISOU 1574  CA  GLU A 201     4149   4977   4363     14    -24   -539       C  
ATOM   1575  C   GLU A 201     -29.853  29.922  -8.646  1.00 34.69           C  
ANISOU 1575  C   GLU A 201     4056   4858   4264      1      6   -539       C  
ATOM   1576  O   GLU A 201     -30.446  30.251  -9.676  1.00 36.76           O  
ANISOU 1576  O   GLU A 201     4318   5113   4534     15     21   -525       O  
ATOM   1577  CB  GLU A 201     -28.412  27.842  -8.852  1.00 34.93           C  
ANISOU 1577  CB  GLU A 201     4053   4929   4288     16    -43   -549       C  
ATOM   1578  CG  GLU A 201     -27.585  27.104  -7.876  1.00 34.29           C  
ANISOU 1578  CG  GLU A 201     3964   4869   4194     16    -63   -556       C  
ATOM   1579  CD  GLU A 201     -27.909  25.634  -7.765  1.00 33.47           C  
ANISOU 1579  CD  GLU A 201     3853   4765   4097     40    -77   -541       C  
ATOM   1580  OE1 GLU A 201     -28.225  24.933  -8.766  1.00 29.34           O  
ANISOU 1580  OE1 GLU A 201     3320   4235   3592     52    -79   -537       O  
ATOM   1581  OE2 GLU A 201     -27.787  25.170  -6.617  1.00 34.82           O1-
ANISOU 1581  OE2 GLU A 201     4028   4946   4255     49    -83   -535       O1-
ATOM   1582  N   GLU A 202     -29.372  30.812  -7.815  1.00 35.14           N  
ANISOU 1582  N   GLU A 202     4121   4912   4319    -21     19   -557       N  
ATOM   1583  CA  GLU A 202     -29.272  32.224  -8.209  1.00 39.02           C  
ANISOU 1583  CA  GLU A 202     4619   5381   4824    -37     58   -561       C  
ATOM   1584  C   GLU A 202     -27.888  32.573  -8.832  1.00 43.10           C  
ANISOU 1584  C   GLU A 202     5116   5907   5350    -52     65   -578       C  
ATOM   1585  O   GLU A 202     -27.389  33.707  -8.643  1.00 42.53           O  
ANISOU 1585  O   GLU A 202     5044   5819   5293    -77     98   -598       O  
ATOM   1586  CB  GLU A 202     -29.383  33.122  -6.957  1.00 42.80           C  
ANISOU 1586  CB  GLU A 202     5112   5847   5303    -62     78   -583       C  
ATOM   1587  CG  GLU A 202     -30.748  33.317  -6.411  1.00 49.86           C  
ANISOU 1587  CG  GLU A 202     6029   6720   6196    -53     90   -565       C  
ATOM   1588  CD  GLU A 202     -30.736  34.322  -5.241  1.00 50.09           C  
ANISOU 1588  CD  GLU A 202     6069   6736   6225    -79    113   -593       C  
ATOM   1589  OE1 GLU A 202     -29.882  34.183  -4.312  1.00 40.33           O  
ANISOU 1589  OE1 GLU A 202     4822   5527   4973    -96     95   -628       O  
ATOM   1590  OE2 GLU A 202     -31.586  35.210  -5.277  1.00 43.28           O1-
ANISOU 1590  OE2 GLU A 202     5226   5841   5377    -81    149   -581       O1-
ATOM   1591  N   GLN A 203     -27.254  31.607  -9.488  1.00 40.40           N  
ANISOU 1591  N   GLN A 203     4756   5590   5002    -38     38   -575       N  
ATOM   1592  CA  GLN A 203     -26.109  31.838 -10.367  1.00 36.48           C  
ANISOU 1592  CA  GLN A 203     4242   5102   4517    -44     46   -583       C  
ATOM   1593  C   GLN A 203     -26.287  31.023 -11.677  1.00 36.65           C  
ANISOU 1593  C   GLN A 203     4255   5136   4533    -13     33   -559       C  
ATOM   1594  O   GLN A 203     -27.074  30.078 -11.678  1.00 39.41           O  
ANISOU 1594  O   GLN A 203     4606   5493   4873      5      9   -549       O  
ATOM   1595  CB  GLN A 203     -24.856  31.359  -9.682  1.00 36.98           C  
ANISOU 1595  CB  GLN A 203     4285   5194   4572    -61     19   -613       C  
ATOM   1596  CG  GLN A 203     -24.405  32.211  -8.486  1.00 40.34           C  
ANISOU 1596  CG  GLN A 203     4708   5620   4999    -94     31   -650       C  
ATOM   1597  CD  GLN A 203     -23.008  31.907  -7.939  1.00 43.68           C  
ANISOU 1597  CD  GLN A 203     5101   6082   5412   -110      7   -687       C  
ATOM   1598  NE2 GLN A 203     -22.920  31.837  -6.601  1.00 43.87           N  
ANISOU 1598  NE2 GLN A 203     5121   6132   5414   -118    -10   -713       N  
ATOM   1599  OE1 GLN A 203     -21.991  31.859  -8.680  1.00 40.03           O  
ANISOU 1599  OE1 GLN A 203     4618   5628   4962   -115      8   -694       O  
ATOM   1600  N   GLN A 204     -25.516  31.368 -12.700  1.00 36.63           N  
ANISOU 1600  N   GLN A 204     4240   5137   4539    -10     50   -556       N  
ATOM   1601  CA  GLN A 204     -25.370  30.599 -13.906  1.00 36.02           C  
ANISOU 1601  CA  GLN A 204     4149   5080   4454     16     35   -543       C  
ATOM   1602  C   GLN A 204     -24.474  29.430 -13.714  1.00 36.38           C  
ANISOU 1602  C   GLN A 204     4176   5150   4494     12     -1   -559       C  
ATOM   1603  O   GLN A 204     -23.495  29.466 -12.877  1.00 37.56           O  
ANISOU 1603  O   GLN A 204     4318   5306   4647    -11    -10   -581       O  
ATOM   1604  CB  GLN A 204     -24.844  31.490 -15.021  1.00 40.25           C  
ANISOU 1604  CB  GLN A 204     4681   5610   5000     24     74   -528       C  
ATOM   1605  CG  GLN A 204     -25.578  32.829 -15.137  1.00 41.00           C  
ANISOU 1605  CG  GLN A 204     4795   5675   5105     28    125   -507       C  
ATOM   1606  CD  GLN A 204     -26.831  32.716 -15.995  1.00 39.88           C  
ANISOU 1606  CD  GLN A 204     4659   5546   4945     70    128   -476       C  
ATOM   1607  NE2 GLN A 204     -27.429  33.850 -16.356  1.00 36.13           N  
ANISOU 1607  NE2 GLN A 204     4198   5052   4476     87    177   -447       N  
ATOM   1608  OE1 GLN A 204     -27.243  31.607 -16.305  1.00 35.88           O  
ANISOU 1608  OE1 GLN A 204     4143   5069   4421     88     89   -480       O  
ATOM   1609  N   ASN A 205     -24.719  28.370 -14.487  1.00 34.59           N  
ANISOU 1609  N   ASN A 205     3939   4940   4260     37    -23   -553       N  
ATOM   1610  CA  ASN A 205     -23.972  27.110 -14.255  1.00 34.59           C  
ANISOU 1610  CA  ASN A 205     3923   4959   4259     37    -55   -566       C  
ATOM   1611  C   ASN A 205     -23.619  26.399 -15.569  1.00 38.57           C  
ANISOU 1611  C   ASN A 205     4409   5482   4762     59    -63   -565       C  
ATOM   1612  O   ASN A 205     -24.483  26.172 -16.413  1.00 38.50           O  
ANISOU 1612  O   ASN A 205     4399   5479   4748     81    -62   -559       O  
ATOM   1613  CB  ASN A 205     -24.737  26.238 -13.289  1.00 36.33           C  
ANISOU 1613  CB  ASN A 205     4149   5174   4478     41    -75   -566       C  
ATOM   1614  CG  ASN A 205     -24.068  24.901 -12.984  1.00 37.96           C  
ANISOU 1614  CG  ASN A 205     4341   5395   4687     48    -99   -571       C  
ATOM   1615  ND2 ASN A 205     -24.694  24.185 -12.090  1.00 35.63           N  
ANISOU 1615  ND2 ASN A 205     4051   5090   4393     55   -107   -566       N  
ATOM   1616  OD1 ASN A 205     -23.006  24.513 -13.509  1.00 39.22           O  
ANISOU 1616  OD1 ASN A 205     4482   5570   4847     50   -107   -577       O  
ATOM   1617  N   PHE A 206     -22.322  26.212 -15.792  1.00 39.32           N  
ANISOU 1617  N   PHE A 206     4489   5590   4860     52    -68   -573       N  
ATOM   1618  CA  PHE A 206     -21.849  25.206 -16.729  1.00 38.59           C  
ANISOU 1618  CA  PHE A 206     4377   5516   4766     70    -83   -577       C  
ATOM   1619  C   PHE A 206     -21.413  23.993 -15.937  1.00 39.09           C  
ANISOU 1619  C   PHE A 206     4432   5585   4836     68   -108   -585       C  
ATOM   1620  O   PHE A 206     -20.464  24.050 -15.111  1.00 41.15           O  
ANISOU 1620  O   PHE A 206     4686   5852   5095     54   -115   -590       O  
ATOM   1621  CB  PHE A 206     -20.744  25.678 -17.575  1.00 37.88           C  
ANISOU 1621  CB  PHE A 206     4277   5437   4679     70    -69   -576       C  
ATOM   1622  CG  PHE A 206     -21.132  26.653 -18.607  1.00 36.07           C  
ANISOU 1622  CG  PHE A 206     4054   5207   4444     85    -38   -559       C  
ATOM   1623  CD1 PHE A 206     -21.844  26.264 -19.695  1.00 37.96           C  
ANISOU 1623  CD1 PHE A 206     4289   5466   4668    117    -41   -554       C  
ATOM   1624  CD2 PHE A 206     -20.656  27.933 -18.556  1.00 35.82           C  
ANISOU 1624  CD2 PHE A 206     4028   5158   4421     71     -4   -551       C  
ATOM   1625  CE1 PHE A 206     -22.126  27.166 -20.698  1.00 35.42           C  
ANISOU 1625  CE1 PHE A 206     3971   5152   4334    140    -10   -533       C  
ATOM   1626  CE2 PHE A 206     -20.939  28.857 -19.536  1.00 36.83           C  
ANISOU 1626  CE2 PHE A 206     4163   5284   4546     91     33   -528       C  
ATOM   1627  CZ  PHE A 206     -21.681  28.477 -20.614  1.00 39.06           C  
ANISOU 1627  CZ  PHE A 206     4443   5591   4806    130     29   -515       C  
ATOM   1628  N   PHE A 207     -22.169  22.919 -16.172  1.00 32.42           N  
ANISOU 1628  N   PHE A 207     3583   4737   3997     85   -119   -588       N  
ATOM   1629  CA  PHE A 207     -22.134  21.686 -15.468  1.00 32.98           C  
ANISOU 1629  CA  PHE A 207     3648   4803   4080     90   -131   -589       C  
ATOM   1630  C   PHE A 207     -21.370  20.642 -16.272  1.00 35.58           C  
ANISOU 1630  C   PHE A 207     3955   5143   4418    103   -138   -598       C  
ATOM   1631  O   PHE A 207     -21.878  20.183 -17.286  1.00 35.60           O  
ANISOU 1631  O   PHE A 207     3949   5149   4428    115   -136   -612       O  
ATOM   1632  CB  PHE A 207     -23.566  21.298 -15.289  1.00 34.59           C  
ANISOU 1632  CB  PHE A 207     3859   4988   4293     97   -128   -591       C  
ATOM   1633  CG  PHE A 207     -23.789  20.056 -14.472  1.00 33.14           C  
ANISOU 1633  CG  PHE A 207     3673   4788   4130    105   -129   -588       C  
ATOM   1634  CD1 PHE A 207     -23.923  18.841 -15.076  1.00 39.06           C  
ANISOU 1634  CD1 PHE A 207     4405   5531   4904    117   -127   -601       C  
ATOM   1635  CD2 PHE A 207     -23.991  20.139 -13.151  1.00 38.36           C  
ANISOU 1635  CD2 PHE A 207     4348   5438   4786    103   -127   -572       C  
ATOM   1636  CE1 PHE A 207     -24.200  17.722 -14.336  1.00 38.47           C  
ANISOU 1636  CE1 PHE A 207     4327   5431   4855    127   -117   -595       C  
ATOM   1637  CE2 PHE A 207     -24.289  19.039 -12.408  1.00 37.47           C  
ANISOU 1637  CE2 PHE A 207     4235   5308   4693    116   -120   -562       C  
ATOM   1638  CZ  PHE A 207     -24.397  17.836 -12.999  1.00 39.56           C  
ANISOU 1638  CZ  PHE A 207     4482   5559   4988    128   -112   -571       C  
ATOM   1639  N   ALA A 208     -20.111  20.383 -15.882  1.00 34.81           N  
ANISOU 1639  N   ALA A 208     3848   5058   4319    101   -145   -594       N  
ATOM   1640  CA  ALA A 208     -19.169  19.591 -16.668  1.00 37.33           C  
ANISOU 1640  CA  ALA A 208     4147   5389   4646    111   -149   -601       C  
ATOM   1641  C   ALA A 208     -19.017  18.170 -16.161  1.00 36.87           C  
ANISOU 1641  C   ALA A 208     4079   5322   4607    126   -150   -596       C  
ATOM   1642  O   ALA A 208     -18.404  17.889 -15.102  1.00 38.07           O  
ANISOU 1642  O   ALA A 208     4229   5480   4755    131   -155   -580       O  
ATOM   1643  CB  ALA A 208     -17.845  20.285 -16.690  1.00 39.95           C  
ANISOU 1643  CB  ALA A 208     4470   5741   4967    100   -151   -599       C  
ATOM   1644  N   GLN A 209     -19.578  17.255 -16.938  1.00 37.65           N  
ANISOU 1644  N   GLN A 209     4169   5407   4727    137   -144   -611       N  
ATOM   1645  CA  GLN A 209     -19.570  15.838 -16.568  1.00 38.97           C  
ANISOU 1645  CA  GLN A 209     4327   5555   4924    152   -133   -608       C  
ATOM   1646  C   GLN A 209     -18.208  15.199 -16.952  1.00 41.49           C  
ANISOU 1646  C   GLN A 209     4627   5888   5248    163   -134   -605       C  
ATOM   1647  O   GLN A 209     -17.645  15.468 -18.083  1.00 35.56           O  
ANISOU 1647  O   GLN A 209     3866   5156   4489    160   -140   -621       O  
ATOM   1648  CB  GLN A 209     -20.697  15.165 -17.299  1.00 38.47           C  
ANISOU 1648  CB  GLN A 209     4255   5471   4888    155   -122   -636       C  
ATOM   1649  CG  GLN A 209     -21.021  13.760 -16.846  1.00 38.04           C  
ANISOU 1649  CG  GLN A 209     4193   5382   4878    167    -99   -636       C  
ATOM   1650  CD  GLN A 209     -21.396  13.662 -15.374  1.00 37.01           C  
ANISOU 1650  CD  GLN A 209     4079   5230   4751    173    -88   -603       C  
ATOM   1651  NE2 GLN A 209     -21.396  12.445 -14.880  1.00 41.78           N  
ANISOU 1651  NE2 GLN A 209     4677   5804   5394    191    -61   -591       N  
ATOM   1652  OE1 GLN A 209     -21.677  14.645 -14.684  1.00 36.04           O  
ANISOU 1652  OE1 GLN A 209     3974   5117   4600    165   -100   -588       O  
ATOM   1653  N   ILE A 210     -17.718  14.352 -16.040  1.00 40.91           N  
ANISOU 1653  N   ILE A 210     4549   5807   5186    179   -127   -582       N  
ATOM   1654  CA  ILE A 210     -16.315  13.857 -16.113  1.00 41.65           C  
ANISOU 1654  CA  ILE A 210     4626   5920   5279    193   -129   -570       C  
ATOM   1655  C   ILE A 210     -16.347  12.352 -16.130  1.00 42.38           C  
ANISOU 1655  C   ILE A 210     4707   5982   5411    216   -103   -565       C  
ATOM   1656  O   ILE A 210     -15.841  11.750 -17.063  1.00 42.15           O  
ANISOU 1656  O   ILE A 210     4663   5952   5400    220    -96   -581       O  
ATOM   1657  CB  ILE A 210     -15.514  14.366 -14.898  1.00 42.38           C  
ANISOU 1657  CB  ILE A 210     4718   6042   5340    198   -142   -544       C  
ATOM   1658  CG1 ILE A 210     -15.091  15.793 -15.143  1.00 40.75           C  
ANISOU 1658  CG1 ILE A 210     4514   5864   5105    172   -161   -559       C  
ATOM   1659  CG2 ILE A 210     -14.268  13.536 -14.553  1.00 45.12           C  
ANISOU 1659  CG2 ILE A 210     5045   6409   5688    224   -140   -523       C  
ATOM   1660  CD1 ILE A 210     -14.869  16.537 -13.842  1.00 42.15           C  
ANISOU 1660  CD1 ILE A 210     4694   6066   5253    167   -174   -548       C  
ATOM   1661  N   LYS A 211     -16.994  11.748 -15.134  1.00 42.00           N  
ANISOU 1661  N   LYS A 211     4667   5908   5380    230    -83   -543       N  
ATOM   1662  CA  LYS A 211     -17.137  10.321 -15.113  1.00 40.39           C  
ANISOU 1662  CA  LYS A 211     4454   5665   5225    252    -46   -536       C  
ATOM   1663  C   LYS A 211     -18.557   9.864 -14.896  1.00 42.61           C  
ANISOU 1663  C   LYS A 211     4744   5900   5545    249    -20   -547       C  
ATOM   1664  O   LYS A 211     -19.246  10.321 -13.965  1.00 43.92           O  
ANISOU 1664  O   LYS A 211     4926   6062   5697    249    -21   -528       O  
ATOM   1665  CB  LYS A 211     -16.298   9.712 -14.012  1.00 41.86           C  
ANISOU 1665  CB  LYS A 211     4637   5860   5406    288    -33   -487       C  
ATOM   1666  CG  LYS A 211     -16.358   8.186 -13.968  1.00 47.40           C  
ANISOU 1666  CG  LYS A 211     5328   6515   6164    317     16   -472       C  
ATOM   1667  CD  LYS A 211     -15.552   7.730 -12.750  1.00 52.96           C  
ANISOU 1667  CD  LYS A 211     6031   7239   6850    362     29   -412       C  
ATOM   1668  CE  LYS A 211     -15.513   6.202 -12.610  1.00 58.19           C  
ANISOU 1668  CE  LYS A 211     6685   7851   7572    399     89   -384       C  
ATOM   1669  NZ  LYS A 211     -14.847   5.597 -13.795  1.00 60.01           N1+
ANISOU 1669  NZ  LYS A 211     6896   8070   7834    392     98   -412       N1+
ATOM   1670  N   GLY A 212     -18.955   8.824 -15.634  1.00 40.29           N  
ANISOU 1670  N   GLY A 212     4435   5568   5305    248     10   -576       N  
ATOM   1671  CA  GLY A 212     -20.315   8.294 -15.447  1.00 43.28           C  
ANISOU 1671  CA  GLY A 212     4814   5899   5730    242     41   -594       C  
ATOM   1672  C   GLY A 212     -21.404   9.116 -16.139  1.00 40.31           C  
ANISOU 1672  C   GLY A 212     4439   5533   5342    212     18   -640       C  
ATOM   1673  O   GLY A 212     -21.129  10.099 -16.867  1.00 38.35           O  
ANISOU 1673  O   GLY A 212     4193   5329   5050    198    -18   -657       O  
ATOM   1674  N   TYR A 213     -22.670   8.749 -15.898  1.00 46.01           N  
ANISOU 1674  N   TYR A 213     5160   6217   6104    205     43   -657       N  
ATOM   1675  CA  TYR A 213     -23.781   9.384 -16.579  1.00 38.73           C  
ANISOU 1675  CA  TYR A 213     4232   5307   5174    181     25   -704       C  
ATOM   1676  C   TYR A 213     -24.735  10.010 -15.581  1.00 43.19           C  
ANISOU 1676  C   TYR A 213     4818   5861   5728    178     24   -679       C  
ATOM   1677  O   TYR A 213     -25.082   9.392 -14.574  1.00 40.44           O  
ANISOU 1677  O   TYR A 213     4478   5471   5414    191     59   -650       O  
ATOM   1678  CB  TYR A 213     -24.480   8.400 -17.515  1.00 42.13           C  
ANISOU 1678  CB  TYR A 213     4630   5711   5663    170     51   -768       C  
ATOM   1679  CG  TYR A 213     -23.544   8.026 -18.656  1.00 47.87           C  
ANISOU 1679  CG  TYR A 213     5337   6463   6388    172     43   -798       C  
ATOM   1680  CD1 TYR A 213     -22.564   6.985 -18.513  1.00 51.32           C  
ANISOU 1680  CD1 TYR A 213     5767   6871   6860    188     74   -780       C  
ATOM   1681  CD2 TYR A 213     -23.569   8.727 -19.830  1.00 46.45           C  
ANISOU 1681  CD2 TYR A 213     5146   6335   6167    162      8   -837       C  
ATOM   1682  CE1 TYR A 213     -21.663   6.682 -19.526  1.00 51.22           C  
ANISOU 1682  CE1 TYR A 213     5737   6881   6842    190     67   -805       C  
ATOM   1683  CE2 TYR A 213     -22.643   8.457 -20.828  1.00 51.15           C  
ANISOU 1683  CE2 TYR A 213     5725   6954   6752    167      0   -859       C  
ATOM   1684  CZ  TYR A 213     -21.720   7.427 -20.688  1.00 56.76           C  
ANISOU 1684  CZ  TYR A 213     6430   7636   7501    179     29   -846       C  
ATOM   1685  OH  TYR A 213     -20.888   7.192 -21.754  1.00 57.86           O  
ANISOU 1685  OH  TYR A 213     6552   7801   7631    182     21   -872       O  
ATOM   1686  N   LYS A 214     -25.181  11.232 -15.876  1.00 40.52           N  
ANISOU 1686  N   LYS A 214     4491   5559   5345    164     -9   -689       N  
ATOM   1687  CA  LYS A 214     -26.256  11.841 -15.080  1.00 39.78           C  
ANISOU 1687  CA  LYS A 214     4415   5454   5245    158     -8   -675       C  
ATOM   1688  C   LYS A 214     -27.424  12.243 -15.967  1.00 39.32           C  
ANISOU 1688  C   LYS A 214     4341   5408   5188    142    -19   -725       C  
ATOM   1689  O   LYS A 214     -27.211  12.821 -17.049  1.00 42.61           O  
ANISOU 1689  O   LYS A 214     4748   5868   5573    138    -45   -750       O  
ATOM   1690  CB  LYS A 214     -25.773  13.081 -14.346  1.00 39.43           C  
ANISOU 1690  CB  LYS A 214     4399   5440   5142    159    -35   -634       C  
ATOM   1691  CG  LYS A 214     -25.103  12.765 -13.043  1.00 40.29           C  
ANISOU 1691  CG  LYS A 214     4523   5537   5246    178    -22   -584       C  
ATOM   1692  CD  LYS A 214     -24.492  13.988 -12.391  1.00 40.57           C  
ANISOU 1692  CD  LYS A 214     4579   5611   5223    176    -51   -556       C  
ATOM   1693  CE  LYS A 214     -23.891  13.625 -11.028  1.00 43.68           C  
ANISOU 1693  CE  LYS A 214     4983   6007   5606    202    -39   -510       C  
ATOM   1694  NZ  LYS A 214     -23.423  14.841 -10.343  1.00 42.00           N1+
ANISOU 1694  NZ  LYS A 214     4785   5834   5338    195    -67   -496       N1+
ATOM   1695  N   ARG A 215     -28.647  11.943 -15.504  1.00 35.58           N  
ANISOU 1695  N   ARG A 215     3864   4901   4751    136      3   -736       N  
ATOM   1696  CA  ARG A 215     -29.882  12.454 -16.180  1.00 33.49           C  
ANISOU 1696  CA  ARG A 215     3585   4657   4483    124     -8   -779       C  
ATOM   1697  C   ARG A 215     -30.265  13.740 -15.496  1.00 33.10           C  
ANISOU 1697  C   ARG A 215     3566   4621   4388    123    -26   -741       C  
ATOM   1698  O   ARG A 215     -30.400  13.795 -14.247  1.00 37.67           O  
ANISOU 1698  O   ARG A 215     4170   5171   4972    127    -11   -700       O  
ATOM   1699  CB  ARG A 215     -30.958  11.446 -15.979  1.00 40.28           C  
ANISOU 1699  CB  ARG A 215     4422   5470   5412    116     28   -812       C  
ATOM   1700  CG  ARG A 215     -32.257  11.714 -16.645  1.00 44.96           C  
ANISOU 1700  CG  ARG A 215     4988   6083   6011    105     20   -866       C  
ATOM   1701  CD  ARG A 215     -33.308  11.093 -15.770  1.00 48.39           C  
ANISOU 1701  CD  ARG A 215     5418   6459   6507     98     60   -868       C  
ATOM   1702  NE  ARG A 215     -34.559  11.061 -16.501  1.00 47.45           N  
ANISOU 1702  NE  ARG A 215     5261   6357   6408     84     57   -934       N  
ATOM   1703  CZ  ARG A 215     -35.632  10.421 -16.066  1.00 53.84           C  
ANISOU 1703  CZ  ARG A 215     6052   7122   7283     73     94   -960       C  
ATOM   1704  NH1 ARG A 215     -35.636   9.728 -14.906  1.00 47.58           N1+
ANISOU 1704  NH1 ARG A 215     5277   6258   6543     76    142   -920       N1+
ATOM   1705  NH2 ARG A 215     -36.728  10.489 -16.818  1.00 54.96           N  
ANISOU 1705  NH2 ARG A 215     6152   7292   7435     61     85  -1027       N  
ATOM   1706  N   CYS A 216     -30.392  14.791 -16.290  1.00 34.37           N  
ANISOU 1706  N   CYS A 216     3727   4829   4502    122    -55   -752       N  
ATOM   1707  CA  CYS A 216     -30.663  16.091 -15.757  1.00 32.84           C  
ANISOU 1707  CA  CYS A 216     3561   4648   4265    121    -68   -718       C  
ATOM   1708  C   CYS A 216     -32.025  16.457 -16.284  1.00 39.21           C  
ANISOU 1708  C   CYS A 216     4353   5470   5073    120    -71   -748       C  
ATOM   1709  O   CYS A 216     -32.240  16.515 -17.535  1.00 36.56           O  
ANISOU 1709  O   CYS A 216     3989   5176   4723    126    -85   -788       O  
ATOM   1710  CB  CYS A 216     -29.659  17.051 -16.275  1.00 36.10           C  
ANISOU 1710  CB  CYS A 216     3986   5100   4629    125    -90   -701       C  
ATOM   1711  SG  CYS A 216     -27.931  16.591 -15.852  1.00 39.47           S  
ANISOU 1711  SG  CYS A 216     4421   5521   5053    127    -91   -674       S  
ATOM   1712  N   ILE A 217     -32.950  16.656 -15.350  1.00 38.45           N  
ANISOU 1712  N   ILE A 217     4271   5346   4991    115    -58   -732       N  
ATOM   1713  CA  ILE A 217     -34.304  17.158 -15.723  1.00 40.15           C  
ANISOU 1713  CA  ILE A 217     4473   5579   5203    116    -61   -755       C  
ATOM   1714  C   ILE A 217     -34.491  18.610 -15.301  1.00 36.30           C  
ANISOU 1714  C   ILE A 217     4018   5105   4669    119    -69   -714       C  
ATOM   1715  O   ILE A 217     -34.456  18.911 -14.133  1.00 36.94           O  
ANISOU 1715  O   ILE A 217     4129   5154   4750    114    -59   -678       O  
ATOM   1716  CB  ILE A 217     -35.404  16.314 -15.125  1.00 35.82           C  
ANISOU 1716  CB  ILE A 217     3910   4988   4711    107    -34   -775       C  
ATOM   1717  CG1 ILE A 217     -35.269  14.850 -15.532  1.00 38.93           C  
ANISOU 1717  CG1 ILE A 217     4268   5358   5162    101    -15   -820       C  
ATOM   1718  CG2 ILE A 217     -36.741  16.833 -15.650  1.00 38.90           C  
ANISOU 1718  CG2 ILE A 217     4278   5405   5094    109    -41   -805       C  
ATOM   1719  CD1 ILE A 217     -35.980  13.859 -14.626  1.00 41.15           C  
ANISOU 1719  CD1 ILE A 217     4543   5576   5513     93     26   -824       C  
ATOM   1720  N   LEU A 218     -34.726  19.490 -16.263  1.00 32.37           N  
ANISOU 1720  N   LEU A 218     3512   4653   4132    131    -84   -722       N  
ATOM   1721  CA  LEU A 218     -34.840  20.903 -16.012  1.00 32.94           C  
ANISOU 1721  CA  LEU A 218     3614   4736   4165    136    -85   -683       C  
ATOM   1722  C   LEU A 218     -36.250  21.398 -16.197  1.00 34.67           C  
ANISOU 1722  C   LEU A 218     3822   4970   4379    146    -82   -692       C  
ATOM   1723  O   LEU A 218     -36.974  20.881 -17.035  1.00 36.48           O  
ANISOU 1723  O   LEU A 218     4014   5229   4618    155    -89   -734       O  
ATOM   1724  CB  LEU A 218     -33.947  21.651 -17.022  1.00 32.58           C  
ANISOU 1724  CB  LEU A 218     3568   4732   4077    150    -96   -674       C  
ATOM   1725  CG  LEU A 218     -32.515  21.876 -16.533  1.00 30.67           C  
ANISOU 1725  CG  LEU A 218     3351   4473   3827    139    -96   -646       C  
ATOM   1726  CD1 LEU A 218     -31.826  20.536 -16.227  1.00 29.77           C  
ANISOU 1726  CD1 LEU A 218     3226   4339   3745    129    -98   -662       C  
ATOM   1727  CD2 LEU A 218     -31.723  22.677 -17.513  1.00 32.58           C  
ANISOU 1727  CD2 LEU A 218     3593   4751   4034    152    -99   -636       C  
ATOM   1728  N   PHE A 219     -36.607  22.435 -15.473  1.00 35.47           N  
ANISOU 1728  N   PHE A 219     3955   5056   4465    145    -72   -655       N  
ATOM   1729  CA  PHE A 219     -37.866  23.161 -15.699  1.00 37.59           C  
ANISOU 1729  CA  PHE A 219     4216   5343   4720    159    -67   -653       C  
ATOM   1730  C   PHE A 219     -37.643  24.673 -15.693  1.00 36.10           C  
ANISOU 1730  C   PHE A 219     4059   5164   4493    170    -56   -609       C  
ATOM   1731  O   PHE A 219     -36.902  25.206 -14.885  1.00 35.96           O  
ANISOU 1731  O   PHE A 219     4075   5116   4472    155    -47   -579       O  
ATOM   1732  CB  PHE A 219     -38.914  22.786 -14.600  1.00 35.83           C  
ANISOU 1732  CB  PHE A 219     4000   5079   4535    146    -52   -654       C  
ATOM   1733  CG  PHE A 219     -38.957  21.307 -14.275  1.00 36.11           C  
ANISOU 1733  CG  PHE A 219     4015   5084   4622    131    -48   -686       C  
ATOM   1734  CD1 PHE A 219     -38.044  20.764 -13.432  1.00 36.47           C  
ANISOU 1734  CD1 PHE A 219     4081   5091   4683    118    -40   -668       C  
ATOM   1735  CD2 PHE A 219     -39.949  20.465 -14.824  1.00 35.84           C  
ANISOU 1735  CD2 PHE A 219     3935   5060   4621    132    -47   -737       C  
ATOM   1736  CE1 PHE A 219     -38.085  19.450 -13.081  1.00 35.99           C  
ANISOU 1736  CE1 PHE A 219     4004   4997   4673    110    -26   -688       C  
ATOM   1737  CE2 PHE A 219     -39.981  19.128 -14.498  1.00 35.15           C  
ANISOU 1737  CE2 PHE A 219     3829   4935   4590    117    -32   -766       C  
ATOM   1738  CZ  PHE A 219     -39.034  18.608 -13.649  1.00 42.42           C  
ANISOU 1738  CZ  PHE A 219     4776   5812   5528    108    -19   -738       C  
ATOM   1739  N   PRO A 220     -38.232  25.353 -16.653  1.00 39.86           N  
ANISOU 1739  N   PRO A 220     4520   5685   4939    199    -56   -606       N  
ATOM   1740  CA  PRO A 220     -38.110  26.774 -16.705  1.00 35.09           C  
ANISOU 1740  CA  PRO A 220     3942   5083   4305    213    -35   -562       C  
ATOM   1741  C   PRO A 220     -38.645  27.540 -15.532  1.00 33.29           C  
ANISOU 1741  C   PRO A 220     3748   4812   4088    199    -14   -533       C  
ATOM   1742  O   PRO A 220     -39.500  27.049 -14.719  1.00 36.19           O  
ANISOU 1742  O   PRO A 220     4115   5153   4480    186    -14   -544       O  
ATOM   1743  CB  PRO A 220     -38.881  27.186 -17.944  1.00 38.71           C  
ANISOU 1743  CB  PRO A 220     4371   5604   4730    256    -36   -564       C  
ATOM   1744  CG  PRO A 220     -39.411  25.964 -18.526  1.00 43.87           C  
ANISOU 1744  CG  PRO A 220     4980   6293   5395    260    -62   -619       C  
ATOM   1745  CD  PRO A 220     -39.205  24.821 -17.616  1.00 41.73           C  
ANISOU 1745  CD  PRO A 220     4710   5972   5172    221    -69   -646       C  
ATOM   1746  N   PRO A 221     -38.142  28.774 -15.403  1.00 36.17           N  
ANISOU 1746  N   PRO A 221     4143   5164   4436    202     10   -496       N  
ATOM   1747  CA  PRO A 221     -38.488  29.568 -14.223  1.00 34.83           C  
ANISOU 1747  CA  PRO A 221     4007   4949   4277    184     33   -472       C  
ATOM   1748  C   PRO A 221     -40.013  29.802 -14.143  1.00 33.91           C  
ANISOU 1748  C   PRO A 221     3884   4838   4162    202     42   -466       C  
ATOM   1749  O   PRO A 221     -40.560  29.985 -13.062  1.00 34.10           O  
ANISOU 1749  O   PRO A 221     3928   4824   4201    185     54   -458       O  
ATOM   1750  CB  PRO A 221     -37.790  30.887 -14.486  1.00 35.25           C  
ANISOU 1750  CB  PRO A 221     4081   4995   4314    190     64   -440       C  
ATOM   1751  CG  PRO A 221     -36.592  30.502 -15.328  1.00 35.97           C  
ANISOU 1751  CG  PRO A 221     4159   5111   4397    193     51   -450       C  
ATOM   1752  CD  PRO A 221     -37.030  29.362 -16.178  1.00 35.28           C  
ANISOU 1752  CD  PRO A 221     4033   5067   4302    212     19   -480       C  
ATOM   1753  N   ASP A 222     -40.659  29.860 -15.301  1.00 37.73           N  
ANISOU 1753  N   ASP A 222     4338   5374   4624    239     38   -468       N  
ATOM   1754  CA  ASP A 222     -42.097  29.985 -15.311  1.00 33.75           C  
ANISOU 1754  CA  ASP A 222     3818   4885   4119    259     42   -468       C  
ATOM   1755  C   ASP A 222     -42.883  28.808 -14.747  1.00 37.96           C  
ANISOU 1755  C   ASP A 222     4330   5405   4685    239     22   -507       C  
ATOM   1756  O   ASP A 222     -44.061  28.859 -14.836  1.00 38.77           O  
ANISOU 1756  O   ASP A 222     4414   5526   4790    255     24   -512       O  
ATOM   1757  CB  ASP A 222     -42.590  30.400 -16.666  1.00 37.65           C  
ANISOU 1757  CB  ASP A 222     4281   5448   4576    310     43   -461       C  
ATOM   1758  CG  ASP A 222     -42.726  29.243 -17.633  1.00 42.81           C  
ANISOU 1758  CG  ASP A 222     4884   6159   5223    323      6   -512       C  
ATOM   1759  OD1 ASP A 222     -42.438  28.086 -17.313  1.00 46.25           O  
ANISOU 1759  OD1 ASP A 222     5308   6576   5688    291    -15   -553       O  
ATOM   1760  OD2 ASP A 222     -43.117  29.515 -18.752  1.00 47.04           O1-
ANISOU 1760  OD2 ASP A 222     5390   6762   5721    368      3   -511       O1-
ATOM   1761  N   GLN A 223     -42.268  27.736 -14.262  1.00 35.67           N  
ANISOU 1761  N   GLN A 223     4039   5089   4423    209      6   -534       N  
ATOM   1762  CA  GLN A 223     -42.975  26.644 -13.594  1.00 35.89           C  
ANISOU 1762  CA  GLN A 223     4052   5092   4492    191      1   -564       C  
ATOM   1763  C   GLN A 223     -42.950  26.792 -12.096  1.00 36.06           C  
ANISOU 1763  C   GLN A 223     4114   5052   4534    166     19   -539       C  
ATOM   1764  O   GLN A 223     -43.260  25.843 -11.347  1.00 31.62           O  
ANISOU 1764  O   GLN A 223     3547   4457   4008    149     21   -554       O  
ATOM   1765  CB  GLN A 223     -42.305  25.350 -13.881  1.00 40.56           C  
ANISOU 1765  CB  GLN A 223     4620   5684   5105    177    -17   -602       C  
ATOM   1766  CG  GLN A 223     -42.026  25.132 -15.329  1.00 57.25           C  
ANISOU 1766  CG  GLN A 223     6696   7859   7195    199    -37   -630       C  
ATOM   1767  CD  GLN A 223     -43.025  24.234 -15.947  1.00 57.08           C  
ANISOU 1767  CD  GLN A 223     6622   7870   7195    206    -48   -684       C  
ATOM   1768  NE2 GLN A 223     -43.899  24.824 -16.680  1.00 67.47           N  
ANISOU 1768  NE2 GLN A 223     7913   9239   8482    236    -52   -688       N  
ATOM   1769  OE1 GLN A 223     -43.022  23.014 -15.737  1.00 57.59           O  
ANISOU 1769  OE1 GLN A 223     6665   7911   7303    185    -51   -724       O  
ATOM   1770  N   PHE A 224     -42.541  27.954 -11.634  1.00 32.19           N  
ANISOU 1770  N   PHE A 224     3662   4546   4022    164     36   -502       N  
ATOM   1771  CA  PHE A 224     -42.566  28.213 -10.195  1.00 34.80           C  
ANISOU 1771  CA  PHE A 224     4029   4827   4364    143     53   -482       C  
ATOM   1772  C   PHE A 224     -43.852  27.712  -9.507  1.00 35.41           C  
ANISOU 1772  C   PHE A 224     4100   4882   4472    142     62   -488       C  
ATOM   1773  O   PHE A 224     -43.817  27.042  -8.459  1.00 33.17           O  
ANISOU 1773  O   PHE A 224     3828   4562   4210    126     67   -488       O  
ATOM   1774  CB  PHE A 224     -42.372  29.737  -9.954  1.00 35.06           C  
ANISOU 1774  CB  PHE A 224     4095   4850   4373    145     77   -449       C  
ATOM   1775  CG  PHE A 224     -42.280  30.103  -8.496  1.00 33.79           C  
ANISOU 1775  CG  PHE A 224     3972   4648   4220    123     94   -436       C  
ATOM   1776  CD1 PHE A 224     -43.437  30.303  -7.739  1.00 34.72           C  
ANISOU 1776  CD1 PHE A 224     4100   4742   4349    125    111   -425       C  
ATOM   1777  CD2 PHE A 224     -41.064  30.308  -7.897  1.00 34.35           C  
ANISOU 1777  CD2 PHE A 224     4063   4706   4281    103     93   -436       C  
ATOM   1778  CE1 PHE A 224     -43.365  30.658  -6.403  1.00 35.37           C  
ANISOU 1778  CE1 PHE A 224     4215   4790   4432    108    127   -414       C  
ATOM   1779  CE2 PHE A 224     -40.980  30.702  -6.560  1.00 34.39           C  
ANISOU 1779  CE2 PHE A 224     4098   4683   4285     86    107   -429       C  
ATOM   1780  CZ  PHE A 224     -42.128  30.854  -5.802  1.00 34.17           C  
ANISOU 1780  CZ  PHE A 224     4083   4633   4267     89    124   -418       C  
ATOM   1781  N   GLU A 225     -44.988  28.018 -10.116  1.00 39.11           N  
ANISOU 1781  N   GLU A 225     4547   5374   4939    161     66   -491       N  
ATOM   1782  CA  GLU A 225     -46.288  27.640  -9.527  1.00 42.23           C  
ANISOU 1782  CA  GLU A 225     4931   5749   5365    160     78   -498       C  
ATOM   1783  C   GLU A 225     -46.499  26.155  -9.474  1.00 40.63           C  
ANISOU 1783  C   GLU A 225     4697   5535   5204    149     70   -536       C  
ATOM   1784  O   GLU A 225     -47.342  25.714  -8.715  1.00 38.10           O  
ANISOU 1784  O   GLU A 225     4374   5181   4917    142     87   -538       O  
ATOM   1785  CB  GLU A 225     -47.432  28.167 -10.345  1.00 47.16           C  
ANISOU 1785  CB  GLU A 225     5527   6412   5978    187     80   -501       C  
ATOM   1786  CG  GLU A 225     -47.541  29.647 -10.342  1.00 58.14           C  
ANISOU 1786  CG  GLU A 225     6947   7806   7335    204    100   -459       C  
ATOM   1787  CD  GLU A 225     -48.988  30.074 -10.277  1.00 63.16           C  
ANISOU 1787  CD  GLU A 225     7570   8450   7977    223    116   -450       C  
ATOM   1788  OE1 GLU A 225     -49.488  30.393  -9.148  1.00 69.66           O  
ANISOU 1788  OE1 GLU A 225     8424   9227   8817    210    139   -430       O  
ATOM   1789  OE2 GLU A 225     -49.628  29.967 -11.342  1.00 70.12           O1-
ANISOU 1789  OE2 GLU A 225     8408   9387   8847    251    103   -468       O1-
ATOM   1790  N   CYS A 226     -45.818  25.382 -10.320  1.00 35.04           N  
ANISOU 1790  N   CYS A 226     3961   4852   4499    148     49   -567       N  
ATOM   1791  CA  CYS A 226     -45.953  23.905 -10.246  1.00 36.04           C  
ANISOU 1791  CA  CYS A 226     4057   4959   4676    135     50   -605       C  
ATOM   1792  C   CYS A 226     -44.992  23.187  -9.289  1.00 34.97           C  
ANISOU 1792  C   CYS A 226     3949   4779   4560    119     60   -590       C  
ATOM   1793  O   CYS A 226     -45.126  21.990  -9.116  1.00 36.19           O  
ANISOU 1793  O   CYS A 226     4081   4906   4761    111     71   -614       O  
ATOM   1794  CB  CYS A 226     -45.828  23.278 -11.629  1.00 34.33           C  
ANISOU 1794  CB  CYS A 226     3790   4793   4461    142     27   -655       C  
ATOM   1795  SG  CYS A 226     -46.798  24.163 -12.910  1.00 39.09           S  
ANISOU 1795  SG  CYS A 226     4355   5472   5023    174     11   -671       S  
ATOM   1796  N   LEU A 227     -43.972  23.899  -8.735  1.00 38.70           N  
ANISOU 1796  N   LEU A 227     4462   5244   4995    117     57   -553       N  
ATOM   1797  CA  LEU A 227     -42.854  23.217  -8.055  1.00 36.17           C  
ANISOU 1797  CA  LEU A 227     4160   4901   4681    108     58   -542       C  
ATOM   1798  C   LEU A 227     -42.680  23.588  -6.579  1.00 35.96           C  
ANISOU 1798  C   LEU A 227     4176   4842   4643    106     75   -503       C  
ATOM   1799  O   LEU A 227     -41.884  22.961  -5.873  1.00 36.05           O  
ANISOU 1799  O   LEU A 227     4199   4839   4657    106     79   -491       O  
ATOM   1800  CB  LEU A 227     -41.581  23.547  -8.811  1.00 34.41           C  
ANISOU 1800  CB  LEU A 227     3938   4711   4423    109     35   -544       C  
ATOM   1801  CG  LEU A 227     -41.545  22.743 -10.123  1.00 36.85           C  
ANISOU 1801  CG  LEU A 227     4203   5049   4748    113     19   -586       C  
ATOM   1802  CD1 LEU A 227     -40.526  23.279 -11.067  1.00 36.67           C  
ANISOU 1802  CD1 LEU A 227     4178   5065   4686    118     -1   -587       C  
ATOM   1803  CD2 LEU A 227     -41.209  21.273  -9.835  1.00 37.79           C  
ANISOU 1803  CD2 LEU A 227     4306   5139   4913    106     28   -604       C  
ATOM   1804  N   TYR A 228     -43.386  24.613  -6.141  1.00 36.21           N  
ANISOU 1804  N   TYR A 228     4229   4870   4659    107     86   -485       N  
ATOM   1805  CA  TYR A 228     -43.647  24.772  -4.734  1.00 35.49           C  
ANISOU 1805  CA  TYR A 228     4170   4747   4567    107    107   -457       C  
ATOM   1806  C   TYR A 228     -42.343  24.794  -3.887  1.00 34.52           C  
ANISOU 1806  C   TYR A 228     4073   4627   4415    106    102   -440       C  
ATOM   1807  O   TYR A 228     -42.174  23.990  -2.969  1.00 34.98           O  
ANISOU 1807  O   TYR A 228     4140   4667   4485    114    115   -425       O  
ATOM   1808  CB  TYR A 228     -44.591  23.702  -4.261  1.00 35.03           C  
ANISOU 1808  CB  TYR A 228     4096   4654   4558    112    132   -460       C  
ATOM   1809  CG  TYR A 228     -45.970  23.727  -4.967  1.00 33.28           C  
ANISOU 1809  CG  TYR A 228     3844   4433   4366    112    138   -483       C  
ATOM   1810  CD1 TYR A 228     -46.971  24.603  -4.566  1.00 33.53           C  
ANISOU 1810  CD1 TYR A 228     3890   4458   4391    116    152   -467       C  
ATOM   1811  CD2 TYR A 228     -46.249  22.879  -6.003  1.00 34.41           C  
ANISOU 1811  CD2 TYR A 228     3942   4589   4544    111    130   -523       C  
ATOM   1812  CE1 TYR A 228     -48.230  24.644  -5.193  1.00 32.98           C  
ANISOU 1812  CE1 TYR A 228     3789   4396   4346    119    156   -489       C  
ATOM   1813  CE2 TYR A 228     -47.482  22.875  -6.633  1.00 35.23           C  
ANISOU 1813  CE2 TYR A 228     4009   4703   4671    112    133   -552       C  
ATOM   1814  CZ  TYR A 228     -48.469  23.732  -6.216  1.00 36.52           C  
ANISOU 1814  CZ  TYR A 228     4186   4862   4827    118    145   -533       C  
ATOM   1815  OH  TYR A 228     -49.680  23.729  -6.914  1.00 39.59           O  
ANISOU 1815  OH  TYR A 228     4534   5271   5236    122    145   -564       O  
ATOM   1816  N   PRO A 229     -41.487  25.793  -4.147  1.00 34.66           N  
ANISOU 1816  N   PRO A 229     4104   4669   4394     97     86   -440       N  
ATOM   1817  CA  PRO A 229     -40.257  25.943  -3.323  1.00 34.19           C  
ANISOU 1817  CA  PRO A 229     4065   4622   4304     94     79   -432       C  
ATOM   1818  C   PRO A 229     -40.639  26.147  -1.854  1.00 35.72           C  
ANISOU 1818  C   PRO A 229     4286   4800   4486    100     98   -412       C  
ATOM   1819  O   PRO A 229     -41.649  26.746  -1.573  1.00 39.98           O  
ANISOU 1819  O   PRO A 229     4838   5322   5030     99    115   -405       O  
ATOM   1820  CB  PRO A 229     -39.625  27.187  -3.868  1.00 33.15           C  
ANISOU 1820  CB  PRO A 229     3940   4511   4144     80     70   -441       C  
ATOM   1821  CG  PRO A 229     -40.710  27.912  -4.657  1.00 33.42           C  
ANISOU 1821  CG  PRO A 229     3969   4539   4188     82     81   -440       C  
ATOM   1822  CD  PRO A 229     -41.541  26.799  -5.220  1.00 35.37           C  
ANISOU 1822  CD  PRO A 229     4188   4781   4469     93     79   -449       C  
ATOM   1823  N   TYR A 230     -39.814  25.666  -0.958  1.00 34.71           N  
ANISOU 1823  N   TYR A 230     4165   4683   4338    109     95   -402       N  
ATOM   1824  CA  TYR A 230     -39.850  25.990   0.445  1.00 31.13           C  
ANISOU 1824  CA  TYR A 230     3737   4232   3857    118    108   -387       C  
ATOM   1825  C   TYR A 230     -39.820  27.483   0.688  1.00 33.89           C  
ANISOU 1825  C   TYR A 230     4106   4591   4178     99    108   -400       C  
ATOM   1826  O   TYR A 230     -39.399  28.312  -0.182  1.00 31.64           O  
ANISOU 1826  O   TYR A 230     3815   4315   3889     79     99   -420       O  
ATOM   1827  CB  TYR A 230     -38.676  25.341   1.225  1.00 32.97           C  
ANISOU 1827  CB  TYR A 230     3969   4495   4061    136     97   -378       C  
ATOM   1828  CG  TYR A 230     -38.758  23.866   1.403  1.00 32.43           C  
ANISOU 1828  CG  TYR A 230     3889   4411   4019    164    112   -354       C  
ATOM   1829  CD1 TYR A 230     -38.259  23.016   0.436  1.00 32.06           C  
ANISOU 1829  CD1 TYR A 230     3818   4363   4001    163    102   -362       C  
ATOM   1830  CD2 TYR A 230     -39.321  23.304   2.562  1.00 35.35           C  
ANISOU 1830  CD2 TYR A 230     4273   4767   4391    193    141   -321       C  
ATOM   1831  CE1 TYR A 230     -38.333  21.680   0.576  1.00 35.32           C  
ANISOU 1831  CE1 TYR A 230     4219   4754   4446    187    123   -342       C  
ATOM   1832  CE2 TYR A 230     -39.371  21.946   2.714  1.00 35.54           C  
ANISOU 1832  CE2 TYR A 230     4286   4769   4447    221    164   -295       C  
ATOM   1833  CZ  TYR A 230     -38.893  21.156   1.704  1.00 33.02           C  
ANISOU 1833  CZ  TYR A 230     3941   4442   4160    216    156   -308       C  
ATOM   1834  OH  TYR A 230     -38.945  19.811   1.785  1.00 37.02           O  
ANISOU 1834  OH  TYR A 230     4434   4920   4708    241    186   -285       O  
ATOM   1835  N   PRO A 231     -40.350  27.882   1.849  1.00 34.65           N  
ANISOU 1835  N   PRO A 231     4224   4680   4257    105    126   -390       N  
ATOM   1836  CA  PRO A 231     -40.180  29.311   2.196  1.00 36.93           C  
ANISOU 1836  CA  PRO A 231     4531   4979   4521     85    131   -409       C  
ATOM   1837  C   PRO A 231     -38.701  29.743   2.173  1.00 36.92           C  
ANISOU 1837  C   PRO A 231     4521   5016   4488     69    109   -438       C  
ATOM   1838  O   PRO A 231     -37.818  28.942   2.500  1.00 36.65           O  
ANISOU 1838  O   PRO A 231     4476   5013   4436     83     91   -438       O  
ATOM   1839  CB  PRO A 231     -40.697  29.345   3.621  1.00 36.16           C  
ANISOU 1839  CB  PRO A 231     4455   4880   4402    101    149   -396       C  
ATOM   1840  CG  PRO A 231     -41.840  28.362   3.561  1.00 38.24           C  
ANISOU 1840  CG  PRO A 231     4717   5109   4702    122    167   -364       C  
ATOM   1841  CD  PRO A 231     -41.229  27.190   2.805  1.00 37.38           C  
ANISOU 1841  CD  PRO A 231     4582   5006   4613    130    150   -361       C  
ATOM   1842  N   VAL A 232     -38.450  30.998   1.825  1.00 36.65           N  
ANISOU 1842  N   VAL A 232     4491   4979   4452     42    116   -463       N  
ATOM   1843  CA  VAL A 232     -37.105  31.467   1.689  1.00 35.94           C  
ANISOU 1843  CA  VAL A 232     4389   4921   4345     23    101   -496       C  
ATOM   1844  C   VAL A 232     -36.251  31.331   2.939  1.00 38.72           C  
ANISOU 1844  C   VAL A 232     4738   5318   4654     28     87   -516       C  
ATOM   1845  O   VAL A 232     -35.040  31.084   2.838  1.00 37.31           O  
ANISOU 1845  O   VAL A 232     4540   5176   4458     25     64   -536       O  
ATOM   1846  CB  VAL A 232     -37.137  32.909   1.227  1.00 40.87           C  
ANISOU 1846  CB  VAL A 232     5020   5524   4983     -5    125   -517       C  
ATOM   1847  CG1 VAL A 232     -35.890  33.658   1.637  1.00 42.16           C  
ANISOU 1847  CG1 VAL A 232     5174   5715   5126    -31    122   -562       C  
ATOM   1848  CG2 VAL A 232     -37.353  32.943  -0.252  1.00 43.16           C  
ANISOU 1848  CG2 VAL A 232     5301   5794   5304     -5    129   -502       C  
ATOM   1849  N   HIS A 233     -36.864  31.423   4.131  1.00 38.70           N  
ANISOU 1849  N   HIS A 233     4754   5319   4629     42    100   -510       N  
ATOM   1850  CA  HIS A 233     -36.102  31.289   5.377  1.00 39.94           C  
ANISOU 1850  CA  HIS A 233     4906   5532   4736     55     86   -530       C  
ATOM   1851  C   HIS A 233     -35.936  29.879   5.862  1.00 39.12           C  
ANISOU 1851  C   HIS A 233     4796   5454   4612     99     72   -493       C  
ATOM   1852  O   HIS A 233     -35.193  29.610   6.801  1.00 41.48           O  
ANISOU 1852  O   HIS A 233     5086   5811   4864    121     58   -503       O  
ATOM   1853  CB  HIS A 233     -36.747  32.091   6.471  1.00 39.59           C  
ANISOU 1853  CB  HIS A 233     4882   5488   4671     53    107   -544       C  
ATOM   1854  CG  HIS A 233     -36.701  33.545   6.202  1.00 39.82           C  
ANISOU 1854  CG  HIS A 233     4916   5496   4717     10    127   -586       C  
ATOM   1855  CD2 HIS A 233     -35.751  34.473   6.462  1.00 41.57           C  
ANISOU 1855  CD2 HIS A 233     5123   5747   4924    -20    125   -645       C  
ATOM   1856  ND1 HIS A 233     -37.754  34.228   5.622  1.00 42.65           N  
ANISOU 1856  ND1 HIS A 233     5293   5796   5115     -3    158   -571       N  
ATOM   1857  CE1 HIS A 233     -37.472  35.513   5.548  1.00 38.83           C  
ANISOU 1857  CE1 HIS A 233     4810   5300   4642    -39    179   -613       C  
ATOM   1858  NE2 HIS A 233     -36.250  35.692   6.038  1.00 44.35           N  
ANISOU 1858  NE2 HIS A 233     5488   6049   5312    -53    161   -662       N  
ATOM   1859  N   HIS A 234     -36.632  28.970   5.232  1.00 36.98           N  
ANISOU 1859  N   HIS A 234     4526   5143   4378    115     80   -453       N  
ATOM   1860  CA  HIS A 234     -36.426  27.539   5.473  1.00 42.93           C  
ANISOU 1860  CA  HIS A 234     5271   5910   5129    156     76   -416       C  
ATOM   1861  C   HIS A 234     -35.036  27.078   4.997  1.00 41.53           C  
ANISOU 1861  C   HIS A 234     5067   5772   4938    157     47   -430       C  
ATOM   1862  O   HIS A 234     -34.494  27.648   4.043  1.00 41.92           O  
ANISOU 1862  O   HIS A 234     5104   5818   5002    123     33   -459       O  
ATOM   1863  CB  HIS A 234     -37.509  26.762   4.769  1.00 41.57           C  
ANISOU 1863  CB  HIS A 234     5102   5679   5011    163     96   -382       C  
ATOM   1864  CG  HIS A 234     -37.624  25.357   5.211  1.00 44.61           C  
ANISOU 1864  CG  HIS A 234     5484   6061   5406    206    110   -341       C  
ATOM   1865  CD2 HIS A 234     -38.428  24.782   6.127  1.00 44.18           C  
ANISOU 1865  CD2 HIS A 234     5443   5988   5353    240    140   -303       C  
ATOM   1866  ND1 HIS A 234     -36.848  24.352   4.689  1.00 45.86           N  
ANISOU 1866  ND1 HIS A 234     5620   6227   5575    220     99   -331       N  
ATOM   1867  CE1 HIS A 234     -37.188  23.209   5.248  1.00 44.87           C  
ANISOU 1867  CE1 HIS A 234     5497   6088   5464    260    126   -289       C  
ATOM   1868  NE2 HIS A 234     -38.123  23.451   6.142  1.00 46.76           N  
ANISOU 1868  NE2 HIS A 234     5757   6311   5696    274    151   -270       N  
ATOM   1869  N   PRO A 235     -34.470  26.056   5.660  1.00 41.74           N  
ANISOU 1869  N   PRO A 235     5084   5835   4938    199     42   -404       N  
ATOM   1870  CA  PRO A 235     -33.193  25.465   5.247  1.00 45.85           C  
ANISOU 1870  CA  PRO A 235     5578   6393   5447    207     17   -410       C  
ATOM   1871  C   PRO A 235     -33.194  25.007   3.798  1.00 41.32           C  
ANISOU 1871  C   PRO A 235     4993   5776   4927    187     14   -407       C  
ATOM   1872  O   PRO A 235     -32.156  25.066   3.156  1.00 38.65           O  
ANISOU 1872  O   PRO A 235     4636   5463   4586    173     -7   -430       O  
ATOM   1873  CB  PRO A 235     -33.059  24.268   6.182  1.00 50.01           C  
ANISOU 1873  CB  PRO A 235     6104   6947   5949    266     29   -363       C  
ATOM   1874  CG  PRO A 235     -33.599  24.831   7.456  1.00 50.79           C  
ANISOU 1874  CG  PRO A 235     6222   7069   6006    283     41   -362       C  
ATOM   1875  CD  PRO A 235     -34.853  25.569   6.992  1.00 48.94           C  
ANISOU 1875  CD  PRO A 235     6010   6769   5816    245     60   -371       C  
ATOM   1876  N   CYS A 236     -34.379  24.714   3.259  1.00 40.18           N  
ANISOU 1876  N   CYS A 236     4860   5572   4831    183     37   -388       N  
ATOM   1877  CA  CYS A 236     -34.477  24.175   1.925  1.00 36.42           C  
ANISOU 1877  CA  CYS A 236     4370   5063   4404    170     35   -389       C  
ATOM   1878  C   CYS A 236     -34.951  25.165   0.882  1.00 36.69           C  
ANISOU 1878  C   CYS A 236     4407   5073   4462    132     32   -415       C  
ATOM   1879  O   CYS A 236     -35.512  24.773  -0.210  1.00 39.08           O  
ANISOU 1879  O   CYS A 236     4698   5342   4805    125     36   -415       O  
ATOM   1880  CB  CYS A 236     -35.329  22.942   1.901  1.00 37.61           C  
ANISOU 1880  CB  CYS A 236     4520   5171   4598    196     63   -354       C  
ATOM   1881  SG  CYS A 236     -34.608  21.623   2.902  1.00 42.90           S  
ANISOU 1881  SG  CYS A 236     5184   5867   5248    250     76   -313       S  
ATOM   1882  N   ASP A 237     -34.685  26.434   1.189  1.00 34.86           N  
ANISOU 1882  N   ASP A 237     4184   4859   4202    109     26   -441       N  
ATOM   1883  CA  ASP A 237     -34.827  27.545   0.238  1.00 34.13           C  
ANISOU 1883  CA  ASP A 237     4092   4750   4124     76     28   -465       C  
ATOM   1884  C   ASP A 237     -34.228  27.145  -1.111  1.00 35.26           C  
ANISOU 1884  C   ASP A 237     4213   4894   4288     69     13   -471       C  
ATOM   1885  O   ASP A 237     -33.120  26.561  -1.171  1.00 35.79           O  
ANISOU 1885  O   ASP A 237     4263   4989   4343     76     -5   -476       O  
ATOM   1886  CB  ASP A 237     -34.157  28.774   0.805  1.00 34.98           C  
ANISOU 1886  CB  ASP A 237     4205   4884   4202     53     26   -497       C  
ATOM   1887  CG  ASP A 237     -34.232  30.006  -0.080  1.00 39.35           C  
ANISOU 1887  CG  ASP A 237     4760   5415   4774     21     39   -517       C  
ATOM   1888  OD1 ASP A 237     -35.249  30.270  -0.803  1.00 34.96           O  
ANISOU 1888  OD1 ASP A 237     4214   4823   4246     20     56   -502       O  
ATOM   1889  OD2 ASP A 237     -33.212  30.761  -0.039  1.00 38.02           O1-
ANISOU 1889  OD2 ASP A 237     4583   5269   4593      0     34   -551       O1-
ATOM   1890  N   ARG A 238     -35.012  27.417  -2.132  1.00 36.20           N  
ANISOU 1890  N   ARG A 238     4332   4985   4437     61     22   -469       N  
ATOM   1891  CA  ARG A 238     -34.699  27.159  -3.507  1.00 37.63           C  
ANISOU 1891  CA  ARG A 238     4493   5167   4636     57     12   -476       C  
ATOM   1892  C   ARG A 238     -34.985  25.731  -3.936  1.00 35.83           C  
ANISOU 1892  C   ARG A 238     4249   4931   4434     76      7   -466       C  
ATOM   1893  O   ARG A 238     -34.911  25.445  -5.091  1.00 36.93           O  
ANISOU 1893  O   ARG A 238     4368   5074   4590     75     -1   -476       O  
ATOM   1894  CB  ARG A 238     -33.263  27.572  -3.843  1.00 33.41           C  
ANISOU 1894  CB  ARG A 238     3946   4661   4084     42     -2   -497       C  
ATOM   1895  CG  ARG A 238     -33.030  29.061  -3.872  1.00 35.81           C  
ANISOU 1895  CG  ARG A 238     4262   4966   4376     18     10   -515       C  
ATOM   1896  CD  ARG A 238     -31.590  29.414  -4.162  1.00 36.46           C  
ANISOU 1896  CD  ARG A 238     4328   5076   4449      1      0   -540       C  
ATOM   1897  NE  ARG A 238     -30.741  28.800  -3.186  1.00 35.40           N  
ANISOU 1897  NE  ARG A 238     4183   4975   4290     10    -22   -547       N  
ATOM   1898  CZ  ARG A 238     -30.088  27.670  -3.357  1.00 42.59           C  
ANISOU 1898  CZ  ARG A 238     5077   5905   5200     27    -42   -538       C  
ATOM   1899  NH1 ARG A 238     -30.126  27.020  -4.493  1.00 34.90           N1+
ANISOU 1899  NH1 ARG A 238     4092   4919   4249     34    -45   -529       N1+
ATOM   1900  NH2 ARG A 238     -29.381  27.192  -2.373  1.00 45.80           N  
ANISOU 1900  NH2 ARG A 238     5475   6345   5579     42    -56   -539       N  
ATOM   1901  N   GLN A 239     -35.329  24.861  -3.004  1.00 33.19           N  
ANISOU 1901  N   GLN A 239     3918   4585   4104     95     16   -448       N  
ATOM   1902  CA  GLN A 239     -35.576  23.452  -3.307  1.00 34.64           C  
ANISOU 1902  CA  GLN A 239     4085   4753   4323    112     22   -440       C  
ATOM   1903  C   GLN A 239     -37.097  23.245  -3.358  1.00 35.99           C  
ANISOU 1903  C   GLN A 239     4257   4887   4529    115     44   -435       C  
ATOM   1904  O   GLN A 239     -37.834  23.905  -2.630  1.00 37.05           O  
ANISOU 1904  O   GLN A 239     4412   5011   4654    114     57   -425       O  
ATOM   1905  CB  GLN A 239     -34.981  22.451  -2.317  1.00 36.28           C  
ANISOU 1905  CB  GLN A 239     4294   4967   4524    137     28   -417       C  
ATOM   1906  CG  GLN A 239     -33.672  22.782  -1.590  1.00 38.09           C  
ANISOU 1906  CG  GLN A 239     4526   5240   4705    143     10   -416       C  
ATOM   1907  CD  GLN A 239     -32.522  22.961  -2.537  1.00 39.90           C  
ANISOU 1907  CD  GLN A 239     4737   5495   4926    127    -13   -439       C  
ATOM   1908  NE2 GLN A 239     -32.048  24.167  -2.620  1.00 41.71           N  
ANISOU 1908  NE2 GLN A 239     4971   5745   5130    104    -26   -460       N  
ATOM   1909  OE1 GLN A 239     -32.079  22.023  -3.215  1.00 38.55           O  
ANISOU 1909  OE1 GLN A 239     4547   5321   4776    136    -17   -438       O  
ATOM   1910  N   SER A 240     -37.535  22.315  -4.195  1.00 35.95           N  
ANISOU 1910  N   SER A 240     4228   4866   4565    118     49   -447       N  
ATOM   1911  CA  SER A 240     -38.945  21.971  -4.348  1.00 38.15           C  
ANISOU 1911  CA  SER A 240     4496   5113   4883    119     70   -452       C  
ATOM   1912  C   SER A 240     -39.368  21.172  -3.154  1.00 35.07           C  
ANISOU 1912  C   SER A 240     4117   4692   4515    137    101   -425       C  
ATOM   1913  O   SER A 240     -38.690  20.236  -2.805  1.00 37.63           O  
ANISOU 1913  O   SER A 240     4437   5011   4848    152    109   -411       O  
ATOM   1914  CB  SER A 240     -39.185  21.097  -5.596  1.00 37.53           C  
ANISOU 1914  CB  SER A 240     4381   5032   4846    116     67   -484       C  
ATOM   1915  OG  SER A 240     -40.570  20.746  -5.786  1.00 34.21           O  
ANISOU 1915  OG  SER A 240     3943   4587   4468    114     87   -499       O  
ATOM   1916  N   GLN A 241     -40.581  21.452  -2.656  1.00 36.97           N  
ANISOU 1916  N   GLN A 241     4368   4908   4771    137    122   -416       N  
ATOM   1917  CA  GLN A 241     -41.262  20.660  -1.578  1.00 37.30           C  
ANISOU 1917  CA  GLN A 241     4417   4911   4843    156    161   -389       C  
ATOM   1918  C   GLN A 241     -41.839  19.364  -2.069  1.00 36.66           C  
ANISOU 1918  C   GLN A 241     4304   4791   4831    159    189   -404       C  
ATOM   1919  O   GLN A 241     -42.151  18.520  -1.289  1.00 41.04           O  
ANISOU 1919  O   GLN A 241     4862   5311   5419    177    227   -379       O  
ATOM   1920  CB  GLN A 241     -42.426  21.443  -0.965  1.00 35.08           C  
ANISOU 1920  CB  GLN A 241     4155   4613   4559    154    177   -378       C  
ATOM   1921  CG  GLN A 241     -41.967  22.515   0.004  1.00 39.44           C  
ANISOU 1921  CG  GLN A 241     4743   5191   5051    158    167   -358       C  
ATOM   1922  CD  GLN A 241     -43.113  23.406   0.396  1.00 38.75           C  
ANISOU 1922  CD  GLN A 241     4672   5088   4961    152    181   -353       C  
ATOM   1923  NE2 GLN A 241     -43.486  24.264  -0.482  1.00 38.85           N  
ANISOU 1923  NE2 GLN A 241     4677   5110   4971    133    166   -375       N  
ATOM   1924  OE1 GLN A 241     -43.663  23.293   1.457  1.00 38.88           O  
ANISOU 1924  OE1 GLN A 241     4707   5086   4980    167    208   -328       O  
ATOM   1925  N   VAL A 242     -42.004  19.240  -3.373  1.00 39.75           N  
ANISOU 1925  N   VAL A 242     4664   5193   5246    141    171   -446       N  
ATOM   1926  CA  VAL A 242     -42.647  18.106  -3.926  1.00 37.60           C  
ANISOU 1926  CA  VAL A 242     4354   4887   5042    137    197   -475       C  
ATOM   1927  C   VAL A 242     -41.751  16.873  -3.888  1.00 39.61           C  
ANISOU 1927  C   VAL A 242     4598   5124   5326    149    215   -469       C  
ATOM   1928  O   VAL A 242     -40.654  16.927  -4.354  1.00 45.45           O  
ANISOU 1928  O   VAL A 242     5337   5894   6034    148    187   -473       O  
ATOM   1929  CB  VAL A 242     -43.050  18.405  -5.398  1.00 34.81           C  
ANISOU 1929  CB  VAL A 242     3966   4564   4695    117    168   -529       C  
ATOM   1930  CG1 VAL A 242     -43.736  17.225  -5.997  1.00 40.58           C  
ANISOU 1930  CG1 VAL A 242     4651   5267   5500    109    193   -573       C  
ATOM   1931  CG2 VAL A 242     -43.933  19.578  -5.538  1.00 36.17           C  
ANISOU 1931  CG2 VAL A 242     4145   4756   4840    111    154   -532       C  
ATOM   1932  N   ASP A 243     -42.246  15.736  -3.389  1.00 40.82           N  
ANISOU 1932  N   ASP A 243     4741   5224   5544    160    267   -460       N  
ATOM   1933  CA  ASP A 243     -41.510  14.454  -3.483  1.00 40.79           C  
ANISOU 1933  CA  ASP A 243     4721   5195   5582    172    295   -457       C  
ATOM   1934  C   ASP A 243     -41.805  13.869  -4.825  1.00 43.10           C  
ANISOU 1934  C   ASP A 243     4966   5483   5927    147    291   -524       C  
ATOM   1935  O   ASP A 243     -42.929  13.425  -5.097  1.00 42.51           O  
ANISOU 1935  O   ASP A 243     4861   5374   5915    133    320   -560       O  
ATOM   1936  CB  ASP A 243     -42.013  13.514  -2.434  1.00 47.44           C  
ANISOU 1936  CB  ASP A 243     5569   5975   6479    197    362   -419       C  
ATOM   1937  CG  ASP A 243     -41.270  12.180  -2.404  1.00 50.75           C  
ANISOU 1937  CG  ASP A 243     5974   6360   6945    217    404   -404       C  
ATOM   1938  OD1 ASP A 243     -40.554  11.789  -3.343  1.00 45.30           O  
ANISOU 1938  OD1 ASP A 243     5261   5685   6264    205    385   -438       O  
ATOM   1939  OD2 ASP A 243     -41.481  11.499  -1.389  1.00 52.30           O1-
ANISOU 1939  OD2 ASP A 243     6183   6511   7174    248    463   -356       O1-
ATOM   1940  N   PHE A 244     -40.840  13.936  -5.715  1.00 40.80           N  
ANISOU 1940  N   PHE A 244     4664   5230   5606    140    254   -546       N  
ATOM   1941  CA  PHE A 244     -41.070  13.519  -7.081  1.00 39.66           C  
ANISOU 1941  CA  PHE A 244     4474   5097   5497    118    242   -615       C  
ATOM   1942  C   PHE A 244     -41.425  12.014  -7.121  1.00 44.91           C  
ANISOU 1942  C   PHE A 244     5104   5698   6258    115    302   -641       C  
ATOM   1943  O   PHE A 244     -42.003  11.557  -8.075  1.00 41.44           O  
ANISOU 1943  O   PHE A 244     4619   5257   5867     94    305   -709       O  
ATOM   1944  CB  PHE A 244     -39.801  13.738  -7.912  1.00 44.99           C  
ANISOU 1944  CB  PHE A 244     5148   5820   6125    117    199   -625       C  
ATOM   1945  CG  PHE A 244     -39.691  15.092  -8.554  1.00 42.66           C  
ANISOU 1945  CG  PHE A 244     4862   5587   5759    109    144   -634       C  
ATOM   1946  CD1 PHE A 244     -40.123  16.227  -7.933  1.00 39.00           C  
ANISOU 1946  CD1 PHE A 244     4429   5137   5252    111    131   -604       C  
ATOM   1947  CD2 PHE A 244     -39.042  15.222  -9.757  1.00 38.67           C  
ANISOU 1947  CD2 PHE A 244     4337   5126   5230    102    109   -669       C  
ATOM   1948  CE1 PHE A 244     -39.986  17.483  -8.542  1.00 37.59           C  
ANISOU 1948  CE1 PHE A 244     4258   5008   5013    106     90   -608       C  
ATOM   1949  CE2 PHE A 244     -38.907  16.453 -10.366  1.00 39.28           C  
ANISOU 1949  CE2 PHE A 244     4423   5257   5245    100     68   -670       C  
ATOM   1950  CZ  PHE A 244     -39.372  17.585  -9.758  1.00 37.48           C  
ANISOU 1950  CZ  PHE A 244     4224   5036   4980    102     61   -639       C  
ATOM   1951  N   ASP A 245     -40.999  11.244  -6.126  1.00 45.15           N  
ANISOU 1951  N   ASP A 245     5154   5681   6316    140    350   -589       N  
ATOM   1952  CA  ASP A 245     -41.309   9.793  -6.082  1.00 44.63           C  
ANISOU 1952  CA  ASP A 245     5058   5544   6352    141    421   -606       C  
ATOM   1953  C   ASP A 245     -42.720   9.526  -5.524  1.00 50.83           C  
ANISOU 1953  C   ASP A 245     5833   6275   7205    135    473   -613       C  
ATOM   1954  O   ASP A 245     -43.258   8.462  -5.744  1.00 45.68           O  
ANISOU 1954  O   ASP A 245     5143   5565   6647    123    530   -651       O  
ATOM   1955  CB  ASP A 245     -40.281   9.061  -5.249  1.00 45.67           C  
ANISOU 1955  CB  ASP A 245     5216   5648   6488    179    460   -540       C  
ATOM   1956  CG  ASP A 245     -38.870   9.191  -5.827  1.00 46.00           C  
ANISOU 1956  CG  ASP A 245     5262   5740   6474    184    414   -538       C  
ATOM   1957  OD1 ASP A 245     -38.758   9.193  -7.065  1.00 51.17           O  
ANISOU 1957  OD1 ASP A 245     5886   6421   7134    156    382   -602       O  
ATOM   1958  OD2 ASP A 245     -37.890   9.231  -5.052  1.00 51.22           O1-
ANISOU 1958  OD2 ASP A 245     5955   6416   7089    218    413   -474       O1-
ATOM   1959  N   ASN A 246     -43.317  10.494  -4.834  1.00 48.57           N  
ANISOU 1959  N   ASN A 246     5575   6005   6873    140    456   -580       N  
ATOM   1960  CA  ASN A 246     -44.694  10.348  -4.292  1.00 49.81           C  
ANISOU 1960  CA  ASN A 246     5722   6113   7089    135    503   -585       C  
ATOM   1961  C   ASN A 246     -45.324  11.723  -4.198  1.00 46.37           C  
ANISOU 1961  C   ASN A 246     5305   5725   6586    127    453   -581       C  
ATOM   1962  O   ASN A 246     -45.367  12.327  -3.119  1.00 46.85           O  
ANISOU 1962  O   ASN A 246     5409   5785   6604    149    457   -519       O  
ATOM   1963  CB  ASN A 246     -44.684   9.657  -2.921  1.00 53.43           C  
ANISOU 1963  CB  ASN A 246     6209   6507   7582    171    577   -510       C  
ATOM   1964  CG  ASN A 246     -46.109   9.284  -2.441  1.00 62.08           C  
ANISOU 1964  CG  ASN A 246     7287   7539   8760    164    640   -519       C  
ATOM   1965  ND2 ASN A 246     -46.276   9.173  -1.144  1.00 66.98           N  
ANISOU 1965  ND2 ASN A 246     7944   8122   9382    200    689   -445       N  
ATOM   1966  OD1 ASN A 246     -47.041   9.127  -3.232  1.00 67.07           O  
ANISOU 1966  OD1 ASN A 246     7873   8161   9449    128    642   -594       O  
ATOM   1967  N   PRO A 247     -45.747  12.272  -5.341  1.00 39.62           N  
ANISOU 1967  N   PRO A 247     4418   4917   5716     99    406   -646       N  
ATOM   1968  CA  PRO A 247     -46.227  13.644  -5.311  1.00 41.27           C  
ANISOU 1968  CA  PRO A 247     4647   5174   5857     96    360   -636       C  
ATOM   1969  C   PRO A 247     -47.570  13.762  -4.625  1.00 45.65           C  
ANISOU 1969  C   PRO A 247     5200   5692   6450     95    396   -629       C  
ATOM   1970  O   PRO A 247     -48.491  13.022  -4.934  1.00 46.32           O  
ANISOU 1970  O   PRO A 247     5240   5742   6615     78    432   -679       O  
ATOM   1971  CB  PRO A 247     -46.345  14.048  -6.771  1.00 44.62           C  
ANISOU 1971  CB  PRO A 247     5032   5659   6260     76    308   -705       C  
ATOM   1972  CG  PRO A 247     -46.068  12.840  -7.575  1.00 46.87           C  
ANISOU 1972  CG  PRO A 247     5271   5928   6609     63    327   -762       C  
ATOM   1973  CD  PRO A 247     -45.652  11.708  -6.678  1.00 46.00           C  
ANISOU 1973  CD  PRO A 247     5175   5745   6559     76    391   -724       C  
ATOM   1974  N   ASP A 248     -47.649  14.722  -3.719  1.00 39.29           N  
ANISOU 1974  N   ASP A 248     4442   4898   5588    110    386   -573       N  
ATOM   1975  CA  ASP A 248     -48.877  15.049  -3.033  1.00 43.86           C  
ANISOU 1975  CA  ASP A 248     5027   5449   6189    111    414   -560       C  
ATOM   1976  C   ASP A 248     -49.688  16.104  -3.768  1.00 43.28           C  
ANISOU 1976  C   ASP A 248     4935   5424   6083     95    371   -596       C  
ATOM   1977  O   ASP A 248     -49.547  17.322  -3.544  1.00 42.98           O  
ANISOU 1977  O   ASP A 248     4933   5424   5972    103    336   -565       O  
ATOM   1978  CB  ASP A 248     -48.579  15.554  -1.629  1.00 41.00           C  
ANISOU 1978  CB  ASP A 248     4723   5074   5779    139    428   -481       C  
ATOM   1979  CG  ASP A 248     -49.831  15.559  -0.791  1.00 47.87           C  
ANISOU 1979  CG  ASP A 248     5598   5900   6689    144    474   -462       C  
ATOM   1980  OD1 ASP A 248     -50.925  15.674  -1.409  1.00 45.08           O  
ANISOU 1980  OD1 ASP A 248     5207   5546   6374    122    474   -511       O  
ATOM   1981  OD2 ASP A 248     -49.730  15.552   0.449  1.00 50.86           O1-
ANISOU 1981  OD2 ASP A 248     6017   6254   7054    172    507   -400       O1-
ATOM   1982  N   TYR A 249     -50.589  15.622  -4.601  1.00 46.39           N  
ANISOU 1982  N   TYR A 249     5272   5818   6536     76    379   -663       N  
ATOM   1983  CA  TYR A 249     -51.430  16.446  -5.462  1.00 45.39           C  
ANISOU 1983  CA  TYR A 249     5114   5745   6384     66    340   -706       C  
ATOM   1984  C   TYR A 249     -52.455  17.301  -4.733  1.00 46.25           C  
ANISOU 1984  C   TYR A 249     5244   5846   6480     73    350   -674       C  
ATOM   1985  O   TYR A 249     -52.961  18.276  -5.287  1.00 43.33           O  
ANISOU 1985  O   TYR A 249     4866   5528   6067     74    315   -687       O  
ATOM   1986  CB  TYR A 249     -52.131  15.552  -6.493  1.00 45.04           C  
ANISOU 1986  CB  TYR A 249     4994   5706   6411     44    349   -795       C  
ATOM   1987  CG  TYR A 249     -51.156  14.900  -7.444  1.00 44.45           C  
ANISOU 1987  CG  TYR A 249     4894   5654   6338     37    329   -837       C  
ATOM   1988  CD1 TYR A 249     -50.164  15.650  -8.097  1.00 45.56           C  
ANISOU 1988  CD1 TYR A 249     5056   5859   6395     47    273   -824       C  
ATOM   1989  CD2 TYR A 249     -51.197  13.543  -7.701  1.00 45.70           C  
ANISOU 1989  CD2 TYR A 249     5009   5769   6585     20    370   -889       C  
ATOM   1990  CE1 TYR A 249     -49.268  15.036  -8.970  1.00 41.93           C  
ANISOU 1990  CE1 TYR A 249     4573   5420   5936     41    256   -861       C  
ATOM   1991  CE2 TYR A 249     -50.301  12.960  -8.541  1.00 48.36           C  
ANISOU 1991  CE2 TYR A 249     5324   6125   6923     14    354   -926       C  
ATOM   1992  CZ  TYR A 249     -49.316  13.700  -9.157  1.00 45.24           C  
ANISOU 1992  CZ  TYR A 249     4952   5796   6441     25    296   -910       C  
ATOM   1993  OH  TYR A 249     -48.465  13.076 -10.073  1.00 45.26           O  
ANISOU 1993  OH  TYR A 249     4929   5820   6447     19    280   -953       O  
ATOM   1994  N   GLU A 250     -52.696  17.000  -3.474  1.00 42.60           N  
ANISOU 1994  N   GLU A 250     4814   5323   6048     82    400   -626       N  
ATOM   1995  CA  GLU A 250     -53.611  17.782  -2.708  1.00 48.10           C  
ANISOU 1995  CA  GLU A 250     5534   6008   6731     90    413   -592       C  
ATOM   1996  C   GLU A 250     -52.916  19.039  -2.210  1.00 45.89           C  
ANISOU 1996  C   GLU A 250     5314   5761   6358    106    379   -536       C  
ATOM   1997  O   GLU A 250     -53.449  20.124  -2.341  1.00 51.20           O  
ANISOU 1997  O   GLU A 250     5996   6466   6991    107    357   -531       O  
ATOM   1998  CB  GLU A 250     -54.099  16.980  -1.541  1.00 54.02           C  
ANISOU 1998  CB  GLU A 250     6294   6681   7546     98    482   -560       C  
ATOM   1999  CG  GLU A 250     -54.973  15.840  -2.003  1.00 71.10           C  
ANISOU 1999  CG  GLU A 250     8393   8805   9814     78    524   -623       C  
ATOM   2000  CD  GLU A 250     -55.658  15.180  -0.830  1.00 83.05           C  
ANISOU 2000  CD  GLU A 250     9918  10238  11399     87    602   -587       C  
ATOM   2001  OE1 GLU A 250     -56.088  15.917   0.100  1.00 82.32           O  
ANISOU 2001  OE1 GLU A 250     9866  10137  11273    104    611   -533       O  
ATOM   2002  OE2 GLU A 250     -55.739  13.937  -0.836  1.00 77.37           O1-
ANISOU 2002  OE2 GLU A 250     9166   9462  10769     80    657   -610       O1-
ATOM   2003  N   ARG A 251     -51.702  18.887  -1.692  1.00 47.39           N  
ANISOU 2003  N   ARG A 251     5543   5947   6515    117    376   -497       N  
ATOM   2004  CA  ARG A 251     -50.904  20.019  -1.320  1.00 41.70           C  
ANISOU 2004  CA  ARG A 251     4871   5262   5710    127    343   -458       C  
ATOM   2005  C   ARG A 251     -50.326  20.722  -2.541  1.00 40.07           C  
ANISOU 2005  C   ARG A 251     4651   5116   5455    117    289   -488       C  
ATOM   2006  O   ARG A 251     -50.218  21.938  -2.510  1.00 36.34           O  
ANISOU 2006  O   ARG A 251     4206   4674   4926    120    265   -469       O  
ATOM   2007  CB  ARG A 251     -49.762  19.595  -0.410  1.00 52.17           C  
ANISOU 2007  CB  ARG A 251     6234   6574   7014    145    355   -414       C  
ATOM   2008  CG  ARG A 251     -50.197  18.926   0.899  1.00 57.48           C  
ANISOU 2008  CG  ARG A 251     6925   7191   7722    166    414   -371       C  
ATOM   2009  CD  ARG A 251     -49.015  18.323   1.672  1.00 57.20           C  
ANISOU 2009  CD  ARG A 251     6916   7150   7665    192    427   -329       C  
ATOM   2010  NE  ARG A 251     -48.189  19.405   2.169  1.00 61.72           N  
ANISOU 2010  NE  ARG A 251     7530   7769   8149    200    390   -303       N  
ATOM   2011  CZ  ARG A 251     -46.906  19.339   2.508  1.00 55.08           C  
ANISOU 2011  CZ  ARG A 251     6708   6957   7260    216    373   -281       C  
ATOM   2012  NH1 ARG A 251     -46.216  18.250   2.425  1.00 50.61           N1+
ANISOU 2012  NH1 ARG A 251     6128   6379   6720    230    389   -274       N1+
ATOM   2013  NH2 ARG A 251     -46.319  20.418   2.942  1.00 55.17           N  
ANISOU 2013  NH2 ARG A 251     6751   7012   7199    218    341   -269       N  
ATOM   2014  N   PHE A 252     -49.974  19.955  -3.604  1.00 39.54           N  
ANISOU 2014  N   PHE A 252     4543   5065   5415    108    274   -534       N  
ATOM   2015  CA  PHE A 252     -49.264  20.491  -4.748  1.00 38.98           C  
ANISOU 2015  CA  PHE A 252     4461   5051   5297    104    227   -557       C  
ATOM   2016  C   PHE A 252     -49.974  20.268  -6.050  1.00 37.64           C  
ANISOU 2016  C   PHE A 252     4232   4916   5151     96    210   -619       C  
ATOM   2017  O   PHE A 252     -49.415  19.671  -6.970  1.00 41.16           O  
ANISOU 2017  O   PHE A 252     4647   5385   5605     91    193   -658       O  
ATOM   2018  CB  PHE A 252     -47.835  20.009  -4.792  1.00 32.09           C  
ANISOU 2018  CB  PHE A 252     3602   4183   4408    106    215   -548       C  
ATOM   2019  CG  PHE A 252     -47.133  20.034  -3.426  1.00 32.82           C  
ANISOU 2019  CG  PHE A 252     3743   4247   4477    119    233   -491       C  
ATOM   2020  CD1 PHE A 252     -47.039  21.220  -2.689  1.00 36.75           C  
ANISOU 2020  CD1 PHE A 252     4284   4758   4920    125    225   -454       C  
ATOM   2021  CD2 PHE A 252     -46.656  18.877  -2.858  1.00 34.37           C  
ANISOU 2021  CD2 PHE A 252     3941   4408   4711    128    264   -477       C  
ATOM   2022  CE1 PHE A 252     -46.380  21.223  -1.459  1.00 36.53           C  
ANISOU 2022  CE1 PHE A 252     4295   4717   4865    139    238   -411       C  
ATOM   2023  CE2 PHE A 252     -45.954  18.873  -1.623  1.00 36.89           C  
ANISOU 2023  CE2 PHE A 252     4301   4715   4999    148    279   -424       C  
ATOM   2024  CZ  PHE A 252     -45.851  20.034  -0.927  1.00 33.84           C  
ANISOU 2024  CZ  PHE A 252     3954   4350   4553    153    264   -394       C  
ATOM   2025  N   PRO A 253     -51.192  20.829  -6.171  1.00 40.87           N  
ANISOU 2025  N   PRO A 253     4624   5337   5565     98    213   -629       N  
ATOM   2026  CA  PRO A 253     -52.025  20.477  -7.343  1.00 39.09           C  
ANISOU 2026  CA  PRO A 253     4332   5150   5367     94    201   -696       C  
ATOM   2027  C   PRO A 253     -51.370  20.779  -8.689  1.00 39.37           C  
ANISOU 2027  C   PRO A 253     4344   5257   5355    101    156   -726       C  
ATOM   2028  O   PRO A 253     -51.519  20.023  -9.666  1.00 35.86           O  
ANISOU 2028  O   PRO A 253     3843   4842   4937     94    145   -790       O  
ATOM   2029  CB  PRO A 253     -53.328  21.262  -7.109  1.00 40.16           C  
ANISOU 2029  CB  PRO A 253     4463   5294   5500    101    209   -688       C  
ATOM   2030  CG  PRO A 253     -52.915  22.424  -6.247  1.00 38.73           C  
ANISOU 2030  CG  PRO A 253     4350   5102   5263    113    209   -617       C  
ATOM   2031  CD  PRO A 253     -51.893  21.775  -5.275  1.00 40.68           C  
ANISOU 2031  CD  PRO A 253     4637   5298   5522    107    228   -585       C  
ATOM   2032  N   ASN A 254     -50.582  21.831  -8.749  1.00 41.39           N  
ANISOU 2032  N   ASN A 254     4643   5540   5543    114    133   -683       N  
ATOM   2033  CA  ASN A 254     -50.067  22.249 -10.020  1.00 38.52           C  
ANISOU 2033  CA  ASN A 254     4259   5244   5131    126     96   -703       C  
ATOM   2034  C   ASN A 254     -48.830  21.413 -10.433  1.00 36.41           C  
ANISOU 2034  C   ASN A 254     3986   4976   4869    117     84   -722       C  
ATOM   2035  O   ASN A 254     -48.359  21.533 -11.508  1.00 38.75           O  
ANISOU 2035  O   ASN A 254     4261   5325   5134    126     57   -745       O  
ATOM   2036  CB  ASN A 254     -49.823  23.753 -10.058  1.00 39.60           C  
ANISOU 2036  CB  ASN A 254     4435   5409   5201    146     84   -652       C  
ATOM   2037  CG  ASN A 254     -51.109  24.604 -10.230  1.00 43.27           C  
ANISOU 2037  CG  ASN A 254     4886   5902   5652    165     89   -646       C  
ATOM   2038  ND2 ASN A 254     -51.826  24.447 -11.362  1.00 38.03           N  
ANISOU 2038  ND2 ASN A 254     4163   5302   4985    181     70   -694       N  
ATOM   2039  OD1 ASN A 254     -51.407  25.432  -9.377  1.00 49.43           O  
ANISOU 2039  OD1 ASN A 254     5707   6653   6421    167    107   -600       O  
ATOM   2040  N   PHE A 255     -48.387  20.495  -9.619  1.00 37.74           N  
ANISOU 2040  N   PHE A 255     4170   5087   5082    102    108   -715       N  
ATOM   2041  CA  PHE A 255     -47.352  19.589 -10.067  1.00 40.26           C  
ANISOU 2041  CA  PHE A 255     4477   5405   5415     94    102   -738       C  
ATOM   2042  C   PHE A 255     -47.888  18.645 -11.116  1.00 39.20           C  
ANISOU 2042  C   PHE A 255     4274   5294   5324     86     99   -816       C  
ATOM   2043  O   PHE A 255     -47.117  17.966 -11.802  1.00 36.06           O  
ANISOU 2043  O   PHE A 255     3856   4910   4934     82     88   -848       O  
ATOM   2044  CB  PHE A 255     -46.795  18.780  -8.895  1.00 38.75           C  
ANISOU 2044  CB  PHE A 255     4315   5144   5261     87    135   -706       C  
ATOM   2045  CG  PHE A 255     -45.548  18.015  -9.212  1.00 36.59           C  
ANISOU 2045  CG  PHE A 255     4040   4869   4993     84    130   -713       C  
ATOM   2046  CD1 PHE A 255     -44.329  18.672  -9.349  1.00 37.97           C  
ANISOU 2046  CD1 PHE A 255     4246   5073   5106     92    101   -682       C  
ATOM   2047  CD2 PHE A 255     -45.574  16.649  -9.317  1.00 39.20           C  
ANISOU 2047  CD2 PHE A 255     4337   5163   5392     75    158   -750       C  
ATOM   2048  CE1 PHE A 255     -43.189  17.964  -9.623  1.00 40.51           C  
ANISOU 2048  CE1 PHE A 255     4564   5393   5432     91     97   -688       C  
ATOM   2049  CE2 PHE A 255     -44.424  15.935  -9.593  1.00 41.76           C  
ANISOU 2049  CE2 PHE A 255     4660   5483   5722     74    157   -754       C  
ATOM   2050  CZ  PHE A 255     -43.237  16.592  -9.746  1.00 41.46           C  
ANISOU 2050  CZ  PHE A 255     4653   5479   5619     83    124   -722       C  
ATOM   2051  N   GLN A 256     -49.207  18.570 -11.231  1.00 37.81           N  
ANISOU 2051  N   GLN A 256     4060   5124   5180     84    109   -852       N  
ATOM   2052  CA  GLN A 256     -49.876  17.869 -12.337  1.00 35.90           C  
ANISOU 2052  CA  GLN A 256     3743   4923   4972     77    100   -939       C  
ATOM   2053  C   GLN A 256     -49.686  18.520 -13.682  1.00 34.42           C  
ANISOU 2053  C   GLN A 256     3529   4831   4716     99     54   -965       C  
ATOM   2054  O   GLN A 256     -49.954  17.882 -14.726  1.00 39.40           O  
ANISOU 2054  O   GLN A 256     4096   5509   5363     96     40  -1042       O  
ATOM   2055  CB  GLN A 256     -51.419  17.688 -12.066  1.00 41.15           C  
ANISOU 2055  CB  GLN A 256     4369   5576   5690     69    124   -973       C  
ATOM   2056  CG  GLN A 256     -51.636  16.598 -11.019  1.00 41.96           C  
ANISOU 2056  CG  GLN A 256     4476   5584   5883     46    181   -972       C  
ATOM   2057  CD  GLN A 256     -53.016  16.615 -10.417  1.00 47.83           C  
ANISOU 2057  CD  GLN A 256     5201   6297   6674     39    212   -981       C  
ATOM   2058  NE2 GLN A 256     -53.441  17.734  -9.841  1.00 44.67           N  
ANISOU 2058  NE2 GLN A 256     4839   5904   6227     56    205   -923       N  
ATOM   2059  OE1 GLN A 256     -53.701  15.612 -10.508  1.00 47.86           O  
ANISOU 2059  OE1 GLN A 256     5152   6272   6761     19    245  -1043       O  
ATOM   2060  N   ASN A 257     -49.299  19.787 -13.691  1.00 35.85           N  
ANISOU 2060  N   ASN A 257     3754   5043   4823    122     33   -904       N  
ATOM   2061  CA  ASN A 257     -49.086  20.529 -14.916  1.00 35.28           C  
ANISOU 2061  CA  ASN A 257     3663   5058   4681    151     -3   -913       C  
ATOM   2062  C   ASN A 257     -47.589  20.700 -15.275  1.00 36.28           C  
ANISOU 2062  C   ASN A 257     3822   5194   4766    156    -19   -884       C  
ATOM   2063  O   ASN A 257     -47.241  21.360 -16.255  1.00 42.29           O  
ANISOU 2063  O   ASN A 257     4576   6022   5467    183    -44   -880       O  
ATOM   2064  CB  ASN A 257     -49.682  21.883 -14.817  1.00 33.28           C  
ANISOU 2064  CB  ASN A 257     3433   4835   4377    178     -7   -864       C  
ATOM   2065  CG  ASN A 257     -51.120  21.851 -14.382  1.00 40.58           C  
ANISOU 2065  CG  ASN A 257     4331   5749   5337    175      9   -882       C  
ATOM   2066  ND2 ASN A 257     -51.950  21.385 -15.293  1.00 34.41           N  
ANISOU 2066  ND2 ASN A 257     3477   5029   4567    182     -5   -954       N  
ATOM   2067  OD1 ASN A 257     -51.501  22.279 -13.209  1.00 41.85           O  
ANISOU 2067  OD1 ASN A 257     4534   5851   5514    167     35   -832       O  
ATOM   2068  N   VAL A 258     -46.708  20.053 -14.542  1.00 40.33           N  
ANISOU 2068  N   VAL A 258     4366   5643   5313    134     -3   -867       N  
ATOM   2069  CA  VAL A 258     -45.328  20.349 -14.722  1.00 39.17           C  
ANISOU 2069  CA  VAL A 258     4253   5502   5126    138    -17   -833       C  
ATOM   2070  C   VAL A 258     -44.794  19.623 -15.966  1.00 42.10           C  
ANISOU 2070  C   VAL A 258     4581   5921   5494    142    -37   -890       C  
ATOM   2071  O   VAL A 258     -45.212  18.485 -16.259  1.00 37.99           O  
ANISOU 2071  O   VAL A 258     4012   5394   5027    127    -30   -956       O  
ATOM   2072  CB  VAL A 258     -44.544  19.944 -13.507  1.00 42.92           C  
ANISOU 2072  CB  VAL A 258     4773   5902   5629    119      5   -793       C  
ATOM   2073  CG1 VAL A 258     -44.154  18.479 -13.562  1.00 40.83           C  
ANISOU 2073  CG1 VAL A 258     4482   5606   5423    102     18   -834       C  
ATOM   2074  CG2 VAL A 258     -43.364  20.833 -13.416  1.00 53.15           C  
ANISOU 2074  CG2 VAL A 258     6114   7207   6870    127     -8   -741       C  
ATOM   2075  N   VAL A 259     -43.982  20.320 -16.739  1.00 40.47           N  
ANISOU 2075  N   VAL A 259     4385   5763   5227    163    -60   -870       N  
ATOM   2076  CA  VAL A 259     -43.379  19.707 -17.906  1.00 42.76           C  
ANISOU 2076  CA  VAL A 259     4638   6101   5507    170    -79   -919       C  
ATOM   2077  C   VAL A 259     -41.841  19.998 -17.970  1.00 42.75           C  
ANISOU 2077  C   VAL A 259     4677   6091   5473    172    -86   -876       C  
ATOM   2078  O   VAL A 259     -41.447  21.129 -18.015  1.00 44.35           O  
ANISOU 2078  O   VAL A 259     4913   6312   5626    190    -90   -825       O  
ATOM   2079  CB  VAL A 259     -43.971  20.264 -19.196  1.00 43.73           C  
ANISOU 2079  CB  VAL A 259     4719   6320   5576    206   -104   -949       C  
ATOM   2080  CG1 VAL A 259     -43.412  19.433 -20.339  1.00 51.73           C  
ANISOU 2080  CG1 VAL A 259     5688   7381   6585    210   -123  -1011       C  
ATOM   2081  CG2 VAL A 259     -45.506  20.243 -19.211  1.00 44.85           C  
ANISOU 2081  CG2 VAL A 259     4818   6487   5734    211   -102   -987       C  
ATOM   2082  N   GLY A 260     -41.033  18.962 -18.081  1.00 42.99           N  
ANISOU 2082  N   GLY A 260     4697   6100   5535    156    -84   -903       N  
ATOM   2083  CA  GLY A 260     -39.566  19.061 -18.031  1.00 46.38           C  
ANISOU 2083  CA  GLY A 260     5161   6516   5944    155    -88   -866       C  
ATOM   2084  C   GLY A 260     -38.816  19.060 -19.392  1.00 50.63           C  
ANISOU 2084  C   GLY A 260     5675   7117   6442    174   -110   -891       C  
ATOM   2085  O   GLY A 260     -39.396  18.794 -20.485  1.00 42.32           O  
ANISOU 2085  O   GLY A 260     4574   6128   5378    190   -125   -947       O  
ATOM   2086  N   TYR A 261     -37.525  19.379 -19.299  1.00 42.87           N  
ANISOU 2086  N   TYR A 261     4726   6124   5437    174   -112   -850       N  
ATOM   2087  CA  TYR A 261     -36.621  19.299 -20.389  1.00 42.10           C  
ANISOU 2087  CA  TYR A 261     4615   6071   5310    190   -127   -864       C  
ATOM   2088  C   TYR A 261     -35.531  18.342 -19.875  1.00 46.25           C  
ANISOU 2088  C   TYR A 261     5151   6545   5873    166   -119   -863       C  
ATOM   2089  O   TYR A 261     -34.984  18.508 -18.736  1.00 38.65           O  
ANISOU 2089  O   TYR A 261     4230   5531   4924    152   -107   -816       O  
ATOM   2090  CB  TYR A 261     -36.014  20.654 -20.667  1.00 45.19           C  
ANISOU 2090  CB  TYR A 261     5037   6489   5642    212   -130   -808       C  
ATOM   2091  CG  TYR A 261     -36.855  21.684 -21.363  1.00 50.26           C  
ANISOU 2091  CG  TYR A 261     5669   7188   6236    246   -134   -798       C  
ATOM   2092  CD1 TYR A 261     -37.780  22.444 -20.686  1.00 57.04           C  
ANISOU 2092  CD1 TYR A 261     6545   8031   7094    248   -122   -769       C  
ATOM   2093  CD2 TYR A 261     -36.674  21.943 -22.725  1.00 76.58           C  
ANISOU 2093  CD2 TYR A 261     8977  10597   9522    284   -146   -811       C  
ATOM   2094  CE1 TYR A 261     -38.520  23.401 -21.335  1.00 65.66           C  
ANISOU 2094  CE1 TYR A 261     7628   9178   8141    286   -121   -753       C  
ATOM   2095  CE2 TYR A 261     -37.421  22.896 -23.386  1.00 76.79           C  
ANISOU 2095  CE2 TYR A 261     8993  10683   9499    326   -145   -794       C  
ATOM   2096  CZ  TYR A 261     -38.319  23.638 -22.669  1.00 75.04           C  
ANISOU 2096  CZ  TYR A 261     8789  10441   9280    326   -132   -762       C  
ATOM   2097  OH  TYR A 261     -39.067  24.580 -23.297  1.00 83.90           O  
ANISOU 2097  OH  TYR A 261     9901  11622  10355    372   -127   -740       O  
ATOM   2098  N   GLU A 262     -35.193  17.311 -20.647  1.00 40.60           N  
ANISOU 2098  N   GLU A 262     4401   5846   5178    165   -123   -915       N  
ATOM   2099  CA  GLU A 262     -34.258  16.370 -20.055  1.00 38.94           C  
ANISOU 2099  CA  GLU A 262     4202   5581   5011    146   -108   -909       C  
ATOM   2100  C   GLU A 262     -33.115  15.967 -20.952  1.00 38.88           C  
ANISOU 2100  C   GLU A 262     4182   5599   4989    153   -118   -925       C  
ATOM   2101  O   GLU A 262     -33.193  16.117 -22.148  1.00 38.67           O  
ANISOU 2101  O   GLU A 262     4128   5634   4930    171   -134   -959       O  
ATOM   2102  CB  GLU A 262     -34.945  15.179 -19.440  1.00 40.49           C  
ANISOU 2102  CB  GLU A 262     4378   5724   5279    125    -82   -944       C  
ATOM   2103  CG  GLU A 262     -35.307  14.037 -20.314  1.00 43.17           C  
ANISOU 2103  CG  GLU A 262     4664   6077   5660    119    -76  -1025       C  
ATOM   2104  CD  GLU A 262     -35.751  12.818 -19.544  1.00 45.40           C  
ANISOU 2104  CD  GLU A 262     4933   6288   6028     97    -37  -1049       C  
ATOM   2105  OE1 GLU A 262     -36.940  12.751 -19.327  1.00 48.79           O  
ANISOU 2105  OE1 GLU A 262     5343   6709   6485     89    -27  -1076       O  
ATOM   2106  OE2 GLU A 262     -34.963  11.948 -19.133  1.00 49.07           O1-
ANISOU 2106  OE2 GLU A 262     5406   6703   6533     90    -12  -1038       O1-
ATOM   2107  N   THR A 263     -32.069  15.487 -20.332  1.00 39.12           N  
ANISOU 2107  N   THR A 263     4233   5586   5041    143   -107   -898       N  
ATOM   2108  CA  THR A 263     -30.933  15.000 -21.077  1.00 43.97           C  
ANISOU 2108  CA  THR A 263     4837   6217   5650    148   -112   -911       C  
ATOM   2109  C   THR A 263     -30.133  14.066 -20.198  1.00 41.89           C  
ANISOU 2109  C   THR A 263     4587   5895   5434    135    -90   -891       C  
ATOM   2110  O   THR A 263     -30.283  14.009 -18.948  1.00 39.76           O  
ANISOU 2110  O   THR A 263     4342   5577   5186    127    -74   -854       O  
ATOM   2111  CB  THR A 263     -30.052  16.142 -21.616  1.00 43.45           C  
ANISOU 2111  CB  THR A 263     4792   6194   5521    165   -130   -873       C  
ATOM   2112  CG2 THR A 263     -29.220  16.632 -20.530  1.00 43.28           C  
ANISOU 2112  CG2 THR A 263     4811   6136   5496    156   -125   -813       C  
ATOM   2113  OG1 THR A 263     -29.209  15.645 -22.664  1.00 38.85           O  
ANISOU 2113  OG1 THR A 263     4187   5642   4929    175   -137   -900       O  
ATOM   2114  N   VAL A 264     -29.346  13.236 -20.874  1.00 39.80           N  
ANISOU 2114  N   VAL A 264     4302   5634   5184    137    -87   -919       N  
ATOM   2115  CA  VAL A 264     -28.316  12.469 -20.127  1.00 40.70           C  
ANISOU 2115  CA  VAL A 264     4431   5701   5331    134    -67   -888       C  
ATOM   2116  C   VAL A 264     -26.951  12.876 -20.570  1.00 43.42           C  
ANISOU 2116  C   VAL A 264     4786   6075   5635    143    -84   -862       C  
ATOM   2117  O   VAL A 264     -26.620  12.840 -21.796  1.00 40.14           O  
ANISOU 2117  O   VAL A 264     4349   5701   5199    152    -97   -897       O  
ATOM   2118  CB  VAL A 264     -28.409  10.980 -20.247  1.00 45.46           C  
ANISOU 2118  CB  VAL A 264     5004   6265   6003    127    -35   -932       C  
ATOM   2119  CG1 VAL A 264     -27.295  10.343 -19.391  1.00 44.25           C  
ANISOU 2119  CG1 VAL A 264     4871   6068   5874    132    -12   -884       C  
ATOM   2120  CG2 VAL A 264     -29.787  10.530 -19.781  1.00 40.80           C  
ANISOU 2120  CG2 VAL A 264     4399   5640   5463    114    -11   -961       C  
ATOM   2121  N   VAL A 265     -26.194  13.370 -19.591  1.00 41.98           N  
ANISOU 2121  N   VAL A 265     4637   5877   5436    144    -86   -804       N  
ATOM   2122  CA  VAL A 265     -24.842  13.846 -19.853  1.00 41.92           C  
ANISOU 2122  CA  VAL A 265     4639   5893   5393    151   -100   -777       C  
ATOM   2123  C   VAL A 265     -23.828  12.802 -19.458  1.00 41.05           C  
ANISOU 2123  C   VAL A 265     4525   5755   5314    155    -84   -764       C  
ATOM   2124  O   VAL A 265     -23.956  12.184 -18.434  1.00 39.86           O  
ANISOU 2124  O   VAL A 265     4382   5565   5195    156    -63   -743       O  
ATOM   2125  CB  VAL A 265     -24.442  15.163 -19.130  1.00 37.68           C  
ANISOU 2125  CB  VAL A 265     4135   5367   4815    148   -114   -728       C  
ATOM   2126  CG1 VAL A 265     -25.057  16.366 -19.768  1.00 43.68           C  
ANISOU 2126  CG1 VAL A 265     4899   6160   5536    150   -126   -731       C  
ATOM   2127  CG2 VAL A 265     -24.670  15.141 -17.643  1.00 41.75           C  
ANISOU 2127  CG2 VAL A 265     4671   5848   5343    143   -103   -693       C  
ATOM   2128  N   GLY A 266     -22.821  12.619 -20.307  1.00 41.17           N  
ANISOU 2128  N   GLY A 266     4528   5794   5318    161    -91   -773       N  
ATOM   2129  CA  GLY A 266     -21.660  11.809 -19.917  1.00 43.06           C  
ANISOU 2129  CA  GLY A 266     4766   6014   5579    169    -77   -752       C  
ATOM   2130  C   GLY A 266     -20.314  12.518 -20.075  1.00 38.52           C  
ANISOU 2130  C   GLY A 266     4200   5472   4964    174    -96   -723       C  
ATOM   2131  O   GLY A 266     -20.229  13.764 -20.330  1.00 43.20           O  
ANISOU 2131  O   GLY A 266     4804   6095   5514    169   -116   -713       O  
ATOM   2132  N   PRO A 267     -19.230  11.740 -19.941  1.00 42.84           N  
ANISOU 2132  N   PRO A 267     4739   6010   5528    184    -86   -709       N  
ATOM   2133  CA  PRO A 267     -17.877  12.316 -19.956  1.00 39.30           C  
ANISOU 2133  CA  PRO A 267     4293   5590   5047    187   -102   -682       C  
ATOM   2134  C   PRO A 267     -17.671  13.246 -21.124  1.00 38.22           C  
ANISOU 2134  C   PRO A 267     4154   5491   4876    183   -118   -699       C  
ATOM   2135  O   PRO A 267     -17.905  12.885 -22.275  1.00 37.93           O  
ANISOU 2135  O   PRO A 267     4101   5466   4843    188   -116   -735       O  
ATOM   2136  CB  PRO A 267     -16.998  11.051 -20.070  1.00 49.36           C  
ANISOU 2136  CB  PRO A 267     5551   6849   6355    203    -83   -680       C  
ATOM   2137  CG  PRO A 267     -17.758  10.022 -19.301  1.00 48.54           C  
ANISOU 2137  CG  PRO A 267     5447   6700   6297    209    -53   -677       C  
ATOM   2138  CD  PRO A 267     -19.188  10.270 -19.759  1.00 41.91           C  
ANISOU 2138  CD  PRO A 267     4606   5853   5464    194    -54   -717       C  
ATOM   2139  N   GLY A 268     -17.312  14.479 -20.848  1.00 37.93           N  
ANISOU 2139  N   GLY A 268     4132   5474   4805    175   -132   -676       N  
ATOM   2140  CA  GLY A 268     -17.065  15.445 -21.932  1.00 37.78           C  
ANISOU 2140  CA  GLY A 268     4111   5487   4756    175   -138   -683       C  
ATOM   2141  C   GLY A 268     -18.166  16.416 -22.243  1.00 39.14           C  
ANISOU 2141  C   GLY A 268     4295   5670   4906    173   -141   -688       C  
ATOM   2142  O   GLY A 268     -17.957  17.530 -22.844  1.00 38.03           O  
ANISOU 2142  O   GLY A 268     4160   5551   4737    176   -139   -678       O  
ATOM   2143  N   ASP A 269     -19.363  16.028 -21.830  1.00 40.74           N  
ANISOU 2143  N   ASP A 269     4501   5854   5124    171   -139   -701       N  
ATOM   2144  CA  ASP A 269     -20.527  16.920 -22.039  1.00 39.40           C  
ANISOU 2144  CA  ASP A 269     4340   5694   4933    171   -141   -705       C  
ATOM   2145  C   ASP A 269     -20.507  18.076 -21.031  1.00 41.02           C  
ANISOU 2145  C   ASP A 269     4570   5889   5124    157   -141   -671       C  
ATOM   2146  O   ASP A 269     -20.072  17.927 -19.895  1.00 35.92           O  
ANISOU 2146  O   ASP A 269     3933   5223   4489    146   -142   -653       O  
ATOM   2147  CB  ASP A 269     -21.824  16.146 -21.907  1.00 37.06           C  
ANISOU 2147  CB  ASP A 269     4034   5383   4661    170   -138   -734       C  
ATOM   2148  CG  ASP A 269     -21.985  15.039 -22.977  1.00 37.24           C  
ANISOU 2148  CG  ASP A 269     4027   5419   4702    181   -135   -783       C  
ATOM   2149  OD1 ASP A 269     -21.408  15.139 -24.097  1.00 35.84           O  
ANISOU 2149  OD1 ASP A 269     3837   5277   4503    194   -140   -796       O  
ATOM   2150  OD2 ASP A 269     -22.720  14.066 -22.687  1.00 41.73           O1-
ANISOU 2150  OD2 ASP A 269     4582   5961   5309    175   -125   -811       O1-
ATOM   2151  N   VAL A 270     -20.999  19.239 -21.472  1.00 36.62           N  
ANISOU 2151  N   VAL A 270     4023   5348   4541    161   -137   -663       N  
ATOM   2152  CA  VAL A 270     -21.200  20.342 -20.538  1.00 35.55           C  
ANISOU 2152  CA  VAL A 270     3910   5198   4398    146   -131   -637       C  
ATOM   2153  C   VAL A 270     -22.711  20.792 -20.766  1.00 34.78           C  
ANISOU 2153  C   VAL A 270     3819   5104   4290    155   -128   -642       C  
ATOM   2154  O   VAL A 270     -23.173  20.917 -21.925  1.00 37.70           O  
ANISOU 2154  O   VAL A 270     4177   5504   4641    177   -126   -654       O  
ATOM   2155  CB  VAL A 270     -20.247  21.444 -20.868  1.00 36.74           C  
ANISOU 2155  CB  VAL A 270     4067   5359   4534    143   -120   -619       C  
ATOM   2156  CG1 VAL A 270     -20.562  22.671 -20.037  1.00 41.67           C  
ANISOU 2156  CG1 VAL A 270     4712   5966   5153    127   -107   -601       C  
ATOM   2157  CG2 VAL A 270     -18.778  21.032 -20.652  1.00 39.40           C  
ANISOU 2157  CG2 VAL A 270     4392   5697   4880    134   -125   -618       C  
ATOM   2158  N   LEU A 271     -23.464  20.836 -19.687  1.00 34.97           N  
ANISOU 2158  N   LEU A 271     3857   5103   4325    143   -128   -636       N  
ATOM   2159  CA  LEU A 271     -24.848  21.320 -19.662  1.00 32.21           C  
ANISOU 2159  CA  LEU A 271     3515   4753   3969    148   -123   -637       C  
ATOM   2160  C   LEU A 271     -24.906  22.759 -19.113  1.00 31.72           C  
ANISOU 2160  C   LEU A 271     3477   4680   3892    139   -109   -608       C  
ATOM   2161  O   LEU A 271     -24.410  23.073 -18.016  1.00 32.78           O  
ANISOU 2161  O   LEU A 271     3626   4793   4033    118   -107   -595       O  
ATOM   2162  CB  LEU A 271     -25.718  20.370 -18.824  1.00 34.03           C  
ANISOU 2162  CB  LEU A 271     3744   4957   4227    140   -127   -650       C  
ATOM   2163  CG  LEU A 271     -27.166  20.841 -18.613  1.00 34.79           C  
ANISOU 2163  CG  LEU A 271     3847   5049   4321    143   -122   -651       C  
ATOM   2164  CD1 LEU A 271     -27.949  20.940 -19.909  1.00 35.01           C  
ANISOU 2164  CD1 LEU A 271     3853   5116   4331    165   -125   -674       C  
ATOM   2165  CD2 LEU A 271     -27.895  19.921 -17.646  1.00 41.70           C  
ANISOU 2165  CD2 LEU A 271     4722   5890   5229    133   -120   -660       C  
ATOM   2166  N   TYR A 272     -25.366  23.695 -19.939  1.00 28.88           N  
ANISOU 2166  N   TYR A 272     3120   4340   3511    156    -95   -597       N  
ATOM   2167  CA  TYR A 272     -25.690  24.986 -19.449  1.00 30.57           C  
ANISOU 2167  CA  TYR A 272     3357   4538   3718    150    -74   -572       C  
ATOM   2168  C   TYR A 272     -26.996  24.869 -18.724  1.00 33.89           C  
ANISOU 2168  C   TYR A 272     3786   4944   4145    146    -78   -575       C  
ATOM   2169  O   TYR A 272     -28.062  24.599 -19.365  1.00 35.73           O  
ANISOU 2169  O   TYR A 272     4006   5198   4370    168    -83   -586       O  
ATOM   2170  CB  TYR A 272     -25.738  26.013 -20.540  1.00 33.18           C  
ANISOU 2170  CB  TYR A 272     3688   4891   4026    176    -49   -551       C  
ATOM   2171  CG  TYR A 272     -26.175  27.384 -20.139  1.00 34.95           C  
ANISOU 2171  CG  TYR A 272     3936   5094   4250    174    -18   -523       C  
ATOM   2172  CD1 TYR A 272     -25.657  28.006 -19.010  1.00 36.84           C  
ANISOU 2172  CD1 TYR A 272     4192   5296   4508    140     -5   -518       C  
ATOM   2173  CD2 TYR A 272     -27.208  28.012 -20.818  1.00 33.86           C  
ANISOU 2173  CD2 TYR A 272     3798   4975   4090    206      0   -505       C  
ATOM   2174  CE1 TYR A 272     -26.120  29.245 -18.612  1.00 38.61           C  
ANISOU 2174  CE1 TYR A 272     4437   5497   4736    135     27   -498       C  
ATOM   2175  CE2 TYR A 272     -27.667  29.268 -20.412  1.00 38.37           C  
ANISOU 2175  CE2 TYR A 272     4392   5522   4665    206     34   -476       C  
ATOM   2176  CZ  TYR A 272     -27.137  29.875 -19.310  1.00 38.22           C  
ANISOU 2176  CZ  TYR A 272     4391   5458   4670    168     50   -474       C  
ATOM   2177  OH  TYR A 272     -27.595  31.126 -18.889  1.00 38.77           O  
ANISOU 2177  OH  TYR A 272     4482   5499   4748    165     89   -450       O  
ATOM   2178  N   ILE A 273     -26.916  25.104 -17.407  1.00 35.86           N  
ANISOU 2178  N   ILE A 273     4054   5161   4407    121    -76   -567       N  
ATOM   2179  CA  ILE A 273     -28.076  25.270 -16.516  1.00 32.74           C  
ANISOU 2179  CA  ILE A 273     3674   4746   4019    115    -73   -563       C  
ATOM   2180  C   ILE A 273     -28.229  26.799 -16.229  1.00 34.03           C  
ANISOU 2180  C   ILE A 273     3860   4896   4174    109    -45   -540       C  
ATOM   2181  O   ILE A 273     -27.522  27.387 -15.414  1.00 35.54           O  
ANISOU 2181  O   ILE A 273     4063   5068   4369     87    -36   -536       O  
ATOM   2182  CB  ILE A 273     -27.885  24.494 -15.272  1.00 32.56           C  
ANISOU 2182  CB  ILE A 273     3656   4702   4013     98    -85   -568       C  
ATOM   2183  CG1 ILE A 273     -27.651  23.010 -15.594  1.00 31.88           C  
ANISOU 2183  CG1 ILE A 273     3547   4621   3942    106   -101   -587       C  
ATOM   2184  CG2 ILE A 273     -29.127  24.510 -14.374  1.00 37.13           C  
ANISOU 2184  CG2 ILE A 273     4248   5259   4599     95    -80   -564       C  
ATOM   2185  CD1 ILE A 273     -27.407  22.216 -14.282  1.00 32.26           C  
ANISOU 2185  CD1 ILE A 273     3602   4648   4007     97   -105   -583       C  
ATOM   2186  N   PRO A 274     -29.145  27.452 -16.933  1.00 30.25           N  
ANISOU 2186  N   PRO A 274     3382   4428   3683    132    -29   -527       N  
ATOM   2187  CA  PRO A 274     -29.319  28.875 -16.799  1.00 30.44           C  
ANISOU 2187  CA  PRO A 274     3427   4435   3704    131      5   -502       C  
ATOM   2188  C   PRO A 274     -29.845  29.212 -15.393  1.00 35.95           C  
ANISOU 2188  C   PRO A 274     4146   5099   4414    107     10   -501       C  
ATOM   2189  O   PRO A 274     -30.481  28.353 -14.774  1.00 35.52           O  
ANISOU 2189  O   PRO A 274     4089   5040   4364    103    -10   -513       O  
ATOM   2190  CB  PRO A 274     -30.388  29.205 -17.842  1.00 31.94           C  
ANISOU 2190  CB  PRO A 274     3608   4653   3873    171     17   -487       C  
ATOM   2191  CG  PRO A 274     -30.589  28.011 -18.721  1.00 32.29           C  
ANISOU 2191  CG  PRO A 274     3623   4737   3907    191    -13   -511       C  
ATOM   2192  CD  PRO A 274     -30.169  26.847 -17.824  1.00 32.57           C  
ANISOU 2192  CD  PRO A 274     3655   4752   3966    161    -41   -538       C  
ATOM   2193  N   MET A 275     -29.466  30.401 -14.894  1.00 34.16           N  
ANISOU 2193  N   MET A 275     3937   4847   4194     89     41   -491       N  
ATOM   2194  CA  MET A 275     -29.819  30.867 -13.551  1.00 37.56           C  
ANISOU 2194  CA  MET A 275     4388   5249   4634     64     50   -495       C  
ATOM   2195  C   MET A 275     -31.351  30.835 -13.448  1.00 35.13           C  
ANISOU 2195  C   MET A 275     4087   4936   4321     82     52   -482       C  
ATOM   2196  O   MET A 275     -32.071  31.128 -14.430  1.00 33.35           O  
ANISOU 2196  O   MET A 275     3857   4727   4087    112     65   -464       O  
ATOM   2197  CB  MET A 275     -29.341  32.306 -13.408  1.00 39.75           C  
ANISOU 2197  CB  MET A 275     4678   5500   4923     48     94   -488       C  
ATOM   2198  CG  MET A 275     -29.504  32.877 -12.029  1.00 41.89           C  
ANISOU 2198  CG  MET A 275     4967   5745   5204     19    105   -502       C  
ATOM   2199  SD  MET A 275     -28.561  34.379 -11.842  1.00 48.40           S  
ANISOU 2199  SD  MET A 275     5796   6539   6053    -10    157   -513       S  
ATOM   2200  CE  MET A 275     -29.162  35.285 -13.297  1.00 49.08           C  
ANISOU 2200  CE  MET A 275     5888   6614   6145     28    209   -467       C  
ATOM   2201  N   TYR A 276     -31.821  30.394 -12.288  1.00 35.05           N  
ANISOU 2201  N   TYR A 276     4087   4912   4317     67     38   -491       N  
ATOM   2202  CA  TYR A 276     -33.272  30.297 -11.926  1.00 36.13           C  
ANISOU 2202  CA  TYR A 276     4232   5040   4456     79     40   -482       C  
ATOM   2203  C   TYR A 276     -33.947  29.074 -12.540  1.00 36.63           C  
ANISOU 2203  C   TYR A 276     4272   5124   4520     99     14   -492       C  
ATOM   2204  O   TYR A 276     -35.111  28.862 -12.296  1.00 33.28           O  
ANISOU 2204  O   TYR A 276     3848   4694   4102    107     14   -490       O  
ATOM   2205  CB  TYR A 276     -34.108  31.528 -12.300  1.00 37.37           C  
ANISOU 2205  CB  TYR A 276     4401   5187   4610     94     76   -458       C  
ATOM   2206  CG  TYR A 276     -33.786  32.762 -11.519  1.00 40.83           C  
ANISOU 2206  CG  TYR A 276     4863   5592   5056     71    111   -453       C  
ATOM   2207  CD1 TYR A 276     -34.204  32.932 -10.218  1.00 41.65           C  
ANISOU 2207  CD1 TYR A 276     4985   5672   5166     51    114   -461       C  
ATOM   2208  CD2 TYR A 276     -33.071  33.789 -12.105  1.00 43.97           C  
ANISOU 2208  CD2 TYR A 276     5263   5982   5460     70    146   -444       C  
ATOM   2209  CE1 TYR A 276     -33.872  34.066  -9.482  1.00 39.06           C  
ANISOU 2209  CE1 TYR A 276     4675   5316   4847     27    147   -466       C  
ATOM   2210  CE2 TYR A 276     -32.752  34.938 -11.396  1.00 43.67           C  
ANISOU 2210  CE2 TYR A 276     5244   5910   5439     45    185   -448       C  
ATOM   2211  CZ  TYR A 276     -33.141  35.086 -10.103  1.00 45.48           C  
ANISOU 2211  CZ  TYR A 276     5488   6118   5672     22    184   -462       C  
ATOM   2212  OH  TYR A 276     -32.747  36.282  -9.504  1.00 39.84           O  
ANISOU 2212  OH  TYR A 276     4788   5372   4978     -4    226   -475       O  
ATOM   2213  N   TRP A 277     -33.272  28.328 -13.398  1.00 32.91           N  
ANISOU 2213  N   TRP A 277     3779   4678   4046    107     -4   -505       N  
ATOM   2214  CA  TRP A 277     -33.920  27.123 -13.953  1.00 32.84           C  
ANISOU 2214  CA  TRP A 277     3744   4687   4044    122    -25   -524       C  
ATOM   2215  C   TRP A 277     -33.841  26.034 -12.931  1.00 33.01           C  
ANISOU 2215  C   TRP A 277     3767   4688   4088    106    -38   -536       C  
ATOM   2216  O   TRP A 277     -32.826  25.762 -12.363  1.00 31.52           O  
ANISOU 2216  O   TRP A 277     3584   4491   3900     93    -45   -536       O  
ATOM   2217  CB  TRP A 277     -33.348  26.660 -15.285  1.00 32.25           C  
ANISOU 2217  CB  TRP A 277     3642   4649   3959    139    -38   -538       C  
ATOM   2218  CG  TRP A 277     -33.773  27.412 -16.461  1.00 32.09           C  
ANISOU 2218  CG  TRP A 277     3613   4664   3916    170    -26   -527       C  
ATOM   2219  CD1 TRP A 277     -33.616  28.744 -16.689  1.00 34.30           C  
ANISOU 2219  CD1 TRP A 277     3910   4941   4180    180      2   -495       C  
ATOM   2220  CD2 TRP A 277     -34.458  26.892 -17.600  1.00 33.24           C  
ANISOU 2220  CD2 TRP A 277     3725   4854   4048    199    -40   -546       C  
ATOM   2221  CE2 TRP A 277     -34.717  27.984 -18.462  1.00 33.18           C  
ANISOU 2221  CE2 TRP A 277     3718   4876   4010    233    -19   -519       C  
ATOM   2222  CE3 TRP A 277     -34.938  25.628 -17.948  1.00 36.64           C  
ANISOU 2222  CE3 TRP A 277     4125   5304   4492    202    -63   -587       C  
ATOM   2223  NE1 TRP A 277     -34.196  29.109 -17.867  1.00 33.68           N  
ANISOU 2223  NE1 TRP A 277     3816   4904   4077    219     10   -485       N  
ATOM   2224  CZ2 TRP A 277     -35.325  27.834 -19.680  1.00 35.54           C  
ANISOU 2224  CZ2 TRP A 277     3987   5235   4282    272    -27   -530       C  
ATOM   2225  CZ3 TRP A 277     -35.533  25.471 -19.203  1.00 34.30           C  
ANISOU 2225  CZ3 TRP A 277     3794   5065   4173    235    -73   -608       C  
ATOM   2226  CH2 TRP A 277     -35.685  26.543 -20.066  1.00 34.23           C  
ANISOU 2226  CH2 TRP A 277     3784   5095   4123    272    -58   -579       C  
ATOM   2227  N   TRP A 278     -34.977  25.429 -12.670  1.00 32.93           N  
ANISOU 2227  N   TRP A 278     3748   4667   4095    111    -39   -545       N  
ATOM   2228  CA  TRP A 278     -35.076  24.264 -11.835  1.00 32.48           C  
ANISOU 2228  CA  TRP A 278     3689   4586   4064    103    -42   -552       C  
ATOM   2229  C   TRP A 278     -34.343  23.100 -12.458  1.00 30.96           C  
ANISOU 2229  C   TRP A 278     3471   4405   3886    106    -56   -574       C  
ATOM   2230  O   TRP A 278     -34.391  22.916 -13.623  1.00 30.72           O  
ANISOU 2230  O   TRP A 278     3415   4402   3853    117    -65   -596       O  
ATOM   2231  CB  TRP A 278     -36.529  23.854 -11.673  1.00 32.86           C  
ANISOU 2231  CB  TRP A 278     3726   4620   4136    108    -34   -562       C  
ATOM   2232  CG  TRP A 278     -37.369  24.824 -10.975  1.00 35.17           C  
ANISOU 2232  CG  TRP A 278     4043   4898   4421    107    -18   -540       C  
ATOM   2233  CD1 TRP A 278     -37.991  25.857 -11.514  1.00 35.04           C  
ANISOU 2233  CD1 TRP A 278     4029   4897   4387    118    -10   -532       C  
ATOM   2234  CD2 TRP A 278     -37.662  24.853  -9.595  1.00 34.65           C  
ANISOU 2234  CD2 TRP A 278     4003   4799   4364     98     -4   -522       C  
ATOM   2235  CE2 TRP A 278     -38.474  25.945  -9.377  1.00 33.63           C  
ANISOU 2235  CE2 TRP A 278     3890   4663   4223     99      9   -507       C  
ATOM   2236  CE3 TRP A 278     -37.305  24.066  -8.519  1.00 36.76           C  
ANISOU 2236  CE3 TRP A 278     4278   5043   4645     94     -1   -516       C  
ATOM   2237  NE1 TRP A 278     -38.663  26.539 -10.581  1.00 35.42           N  
ANISOU 2237  NE1 TRP A 278     4102   4919   4434    112      7   -511       N  
ATOM   2238  CZ2 TRP A 278     -38.952  26.269  -8.143  1.00 33.46           C  
ANISOU 2238  CZ2 TRP A 278     3895   4614   4204     93     25   -490       C  
ATOM   2239  CZ3 TRP A 278     -37.777  24.385  -7.300  1.00 38.12           C  
ANISOU 2239  CZ3 TRP A 278     4476   5191   4814     92     14   -495       C  
ATOM   2240  CH2 TRP A 278     -38.588  25.479  -7.114  1.00 35.32           C  
ANISOU 2240  CH2 TRP A 278     4139   4831   4450     90     26   -485       C  
ATOM   2241  N   HIS A 279     -33.681  22.309 -11.645  1.00 33.48           N  
ANISOU 2241  N   HIS A 279     3794   4704   4220    100    -56   -569       N  
ATOM   2242  CA  HIS A 279     -33.078  21.089 -12.106  1.00 35.44           C  
ANISOU 2242  CA  HIS A 279     4019   4955   4491    104    -61   -588       C  
ATOM   2243  C   HIS A 279     -33.096  19.969 -11.101  1.00 35.16           C  
ANISOU 2243  C   HIS A 279     3987   4886   4486    106    -47   -579       C  
ATOM   2244  O   HIS A 279     -32.901  20.172  -9.944  1.00 35.79           O  
ANISOU 2244  O   HIS A 279     4090   4954   4554    107    -41   -551       O  
ATOM   2245  CB  HIS A 279     -31.667  21.338 -12.629  1.00 40.23           C  
ANISOU 2245  CB  HIS A 279     4624   5586   5073    103    -76   -586       C  
ATOM   2246  CG  HIS A 279     -30.821  22.178 -11.738  1.00 38.26           C  
ANISOU 2246  CG  HIS A 279     4400   5339   4797     94    -77   -562       C  
ATOM   2247  CD2 HIS A 279     -29.813  21.853 -10.910  1.00 40.68           C  
ANISOU 2247  CD2 HIS A 279     4712   5647   5096     91    -82   -551       C  
ATOM   2248  ND1 HIS A 279     -30.949  23.536 -11.661  1.00 41.65           N  
ANISOU 2248  ND1 HIS A 279     4847   5771   5204     87    -71   -551       N  
ATOM   2249  CE1 HIS A 279     -30.065  24.010 -10.815  1.00 41.35           C  
ANISOU 2249  CE1 HIS A 279     4823   5735   5149     75    -72   -542       C  
ATOM   2250  NE2 HIS A 279     -29.369  23.008 -10.330  1.00 37.14           N  
ANISOU 2250  NE2 HIS A 279     4283   5206   4622     79    -81   -541       N  
ATOM   2251  N   HIS A 280     -33.370  18.779 -11.590  1.00 35.34           N  
ANISOU 2251  N   HIS A 280     3982   4897   4549    110    -39   -604       N  
ATOM   2252  CA  HIS A 280     -33.329  17.548 -10.823  1.00 33.86           C  
ANISOU 2252  CA  HIS A 280     3791   4672   4401    117    -15   -595       C  
ATOM   2253  C   HIS A 280     -32.205  16.732 -11.452  1.00 32.59           C  
ANISOU 2253  C   HIS A 280     3612   4520   4250    121    -20   -607       C  
ATOM   2254  O   HIS A 280     -32.195  16.575 -12.693  1.00 38.86           O  
ANISOU 2254  O   HIS A 280     4381   5335   5049    117    -31   -644       O  
ATOM   2255  CB  HIS A 280     -34.659  16.844 -11.061  1.00 35.03           C  
ANISOU 2255  CB  HIS A 280     3917   4792   4601    114      6   -625       C  
ATOM   2256  CG  HIS A 280     -34.692  15.379 -10.729  1.00 36.33           C  
ANISOU 2256  CG  HIS A 280     4065   4913   4825    120     41   -630       C  
ATOM   2257  CD2 HIS A 280     -34.169  14.301 -11.364  1.00 38.62           C  
ANISOU 2257  CD2 HIS A 280     4328   5193   5150    121     51   -656       C  
ATOM   2258  ND1 HIS A 280     -35.390  14.886  -9.650  1.00 41.86           N  
ANISOU 2258  ND1 HIS A 280     4775   5568   5562    126     77   -607       N  
ATOM   2259  CE1 HIS A 280     -35.294  13.571  -9.629  1.00 42.08           C  
ANISOU 2259  CE1 HIS A 280     4784   5557   5648    133    112   -616       C  
ATOM   2260  NE2 HIS A 280     -34.549  13.192 -10.650  1.00 41.42           N  
ANISOU 2260  NE2 HIS A 280     4678   5494   5565    128     97   -647       N  
ATOM   2261  N   ILE A 281     -31.317  16.176 -10.653  1.00 35.10           N  
ANISOU 2261  N   ILE A 281     3940   4827   4570    133    -10   -577       N  
ATOM   2262  CA  ILE A 281     -30.086  15.514 -11.168  1.00 39.74           C  
ANISOU 2262  CA  ILE A 281     4513   5426   5159    140    -15   -581       C  
ATOM   2263  C   ILE A 281     -29.945  14.112 -10.583  1.00 38.92           C  
ANISOU 2263  C   ILE A 281     4402   5283   5103    158     20   -566       C  
ATOM   2264  O   ILE A 281     -29.904  13.916  -9.356  1.00 37.67           O  
ANISOU 2264  O   ILE A 281     4261   5109   4943    176     39   -525       O  
ATOM   2265  CB  ILE A 281     -28.785  16.306 -10.899  1.00 38.51           C  
ANISOU 2265  CB  ILE A 281     4371   5307   4951    142    -41   -558       C  
ATOM   2266  CG1 ILE A 281     -28.842  17.772 -11.325  1.00 42.87           C  
ANISOU 2266  CG1 ILE A 281     4935   5890   5461    126    -65   -566       C  
ATOM   2267  CG2 ILE A 281     -27.603  15.701 -11.595  1.00 42.71           C  
ANISOU 2267  CG2 ILE A 281     4886   5855   5486    148    -48   -566       C  
ATOM   2268  CD1 ILE A 281     -28.827  18.008 -12.794  1.00 49.65           C  
ANISOU 2268  CD1 ILE A 281     5776   6771   6317    119    -78   -597       C  
ATOM   2269  N   GLU A 282     -29.903  13.118 -11.450  1.00 35.83           N  
ANISOU 2269  N   GLU A 282     3981   4875   4756    156     35   -599       N  
ATOM   2270  CA  GLU A 282     -29.729  11.761 -10.905  1.00 40.92           C  
ANISOU 2270  CA  GLU A 282     4618   5474   5453    175     80   -581       C  
ATOM   2271  C   GLU A 282     -28.605  11.025 -11.597  1.00 39.28           C  
ANISOU 2271  C   GLU A 282     4392   5273   5257    182     81   -591       C  
ATOM   2272  O   GLU A 282     -28.450  11.113 -12.838  1.00 43.59           O  
ANISOU 2272  O   GLU A 282     4918   5842   5800    166     60   -637       O  
ATOM   2273  CB  GLU A 282     -31.034  10.943 -10.958  1.00 41.60           C  
ANISOU 2273  CB  GLU A 282     4685   5507   5610    168    122   -611       C  
ATOM   2274  CG  GLU A 282     -31.579  10.743 -12.335  1.00 48.04           C  
ANISOU 2274  CG  GLU A 282     5466   6331   6454    144    113   -682       C  
ATOM   2275  CD  GLU A 282     -32.981  10.126 -12.320  1.00 49.87           C  
ANISOU 2275  CD  GLU A 282     5675   6517   6753    131    151   -720       C  
ATOM   2276  OE1 GLU A 282     -33.791  10.523 -11.478  1.00 50.74           O  
ANISOU 2276  OE1 GLU A 282     5803   6611   6864    133    161   -695       O  
ATOM   2277  OE2 GLU A 282     -33.248   9.237 -13.145  1.00 42.59           O1-
ANISOU 2277  OE2 GLU A 282     4716   5577   5888    119    172   -777       O1-
ATOM   2278  N   SER A 283     -27.802  10.352 -10.779  1.00 42.99           N  
ANISOU 2278  N   SER A 283     4870   5730   5733    211    105   -545       N  
ATOM   2279  CA  SER A 283     -26.705   9.475 -11.273  1.00 44.32           C  
ANISOU 2279  CA  SER A 283     5021   5896   5919    224    116   -546       C  
ATOM   2280  C   SER A 283     -27.352   8.135 -11.671  1.00 45.00           C  
ANISOU 2280  C   SER A 283     5082   5921   6093    222    171   -576       C  
ATOM   2281  O   SER A 283     -28.043   7.561 -10.858  1.00 40.83           O  
ANISOU 2281  O   SER A 283     4559   5345   5608    235    217   -554       O  
ATOM   2282  CB  SER A 283     -25.678   9.235 -10.159  1.00 41.80           C  
ANISOU 2282  CB  SER A 283     4717   5590   5574    262    126   -480       C  
ATOM   2283  OG  SER A 283     -24.878  10.400  -9.940  1.00 45.26           O  
ANISOU 2283  OG  SER A 283     5169   6089   5936    259     75   -466       O  
ATOM   2284  N   LEU A 284     -27.167   7.707 -12.929  1.00 43.77           N  
ANISOU 2284  N   LEU A 284     4899   5767   5963    205    167   -632       N  
ATOM   2285  CA  LEU A 284     -27.909   6.582 -13.492  1.00 47.33           C  
ANISOU 2285  CA  LEU A 284     5317   6164   6498    192    215   -684       C  
ATOM   2286  C   LEU A 284     -27.862   5.319 -12.614  1.00 45.86           C  
ANISOU 2286  C   LEU A 284     5131   5908   6382    219    289   -644       C  
ATOM   2287  O   LEU A 284     -26.837   4.988 -12.027  1.00 45.25           O  
ANISOU 2287  O   LEU A 284     5068   5833   6290    253    302   -587       O  
ATOM   2288  CB  LEU A 284     -27.383   6.280 -14.887  1.00 47.51           C  
ANISOU 2288  CB  LEU A 284     5311   6210   6528    177    198   -743       C  
ATOM   2289  CG  LEU A 284     -28.258   6.779 -16.019  1.00 49.92           C  
ANISOU 2289  CG  LEU A 284     5593   6549   6825    147    166   -819       C  
ATOM   2290  CD1 LEU A 284     -28.507   8.269 -15.893  1.00 48.68           C  
ANISOU 2290  CD1 LEU A 284     5460   6446   6590    142    112   -799       C  
ATOM   2291  CD2 LEU A 284     -27.608   6.423 -17.369  1.00 51.35           C  
ANISOU 2291  CD2 LEU A 284     5745   6759   7006    139    152   -874       C  
ATOM   2292  N   LEU A 285     -29.005   4.681 -12.440  1.00 44.92           N  
ANISOU 2292  N   LEU A 285     4997   5731   6336    209    339   -670       N  
ATOM   2293  CA  LEU A 285     -29.054   3.388 -11.723  1.00 51.26           C  
ANISOU 2293  CA  LEU A 285     5797   6456   7222    235    424   -636       C  
ATOM   2294  C   LEU A 285     -28.095   2.394 -12.358  1.00 49.55           C  
ANISOU 2294  C   LEU A 285     5559   6220   7045    244    454   -649       C  
ATOM   2295  O   LEU A 285     -27.974   2.321 -13.573  1.00 52.17           O  
ANISOU 2295  O   LEU A 285     5864   6571   7384    216    431   -721       O  
ATOM   2296  CB  LEU A 285     -30.435   2.787 -11.777  1.00 53.97           C  
ANISOU 2296  CB  LEU A 285     6115   6735   7654    212    478   -686       C  
ATOM   2297  CG  LEU A 285     -31.586   3.677 -11.343  1.00 55.91           C  
ANISOU 2297  CG  LEU A 285     6373   6994   7875    196    454   -689       C  
ATOM   2298  CD1 LEU A 285     -32.914   3.158 -11.891  1.00 55.35           C  
ANISOU 2298  CD1 LEU A 285     6262   6878   7890    160    490   -772       C  
ATOM   2299  CD2 LEU A 285     -31.633   3.787  -9.837  1.00 55.81           C  
ANISOU 2299  CD2 LEU A 285     6397   6959   7846    235    483   -598       C  
ATOM   2300  N   ASN A 286     -27.358   1.696 -11.511  1.00 58.08           N  
ANISOU 2300  N   ASN A 286     6654   7270   8142    289    503   -576       N  
ATOM   2301  CA  ASN A 286     -26.346   0.717 -11.889  1.00 59.52           C  
ANISOU 2301  CA  ASN A 286     6823   7431   8361    309    540   -568       C  
ATOM   2302  C   ASN A 286     -25.338   1.263 -12.846  1.00 61.66           C  
ANISOU 2302  C   ASN A 286     7089   7771   8568    296    471   -596       C  
ATOM   2303  O   ASN A 286     -24.829   0.530 -13.708  1.00 55.40           O  
ANISOU 2303  O   ASN A 286     6271   6960   7815    289    491   -635       O  
ATOM   2304  CB  ASN A 286     -26.979  -0.549 -12.480  1.00 66.21           C  
ANISOU 2304  CB  ASN A 286     7633   8193   9329    289    619   -631       C  
ATOM   2305  CG  ASN A 286     -27.857  -1.250 -11.487  1.00 75.64           C  
ANISOU 2305  CG  ASN A 286     8831   9305  10601    308    705   -595       C  
ATOM   2306  ND2 ASN A 286     -29.169  -1.297 -11.756  1.00 75.68           N  
ANISOU 2306  ND2 ASN A 286     8814   9274  10664    268    723   -663       N  
ATOM   2307  OD1 ASN A 286     -27.372  -1.700 -10.451  1.00 88.81           O  
ANISOU 2307  OD1 ASN A 286    10521  10948  12274    361    754   -504       O  
ATOM   2308  N   GLY A 287     -25.020   2.541 -12.696  1.00 52.03           N  
ANISOU 2308  N   GLY A 287     5890   6625   7251    293    395   -576       N  
ATOM   2309  CA  GLY A 287     -24.113   3.164 -13.607  1.00 46.77           C  
ANISOU 2309  CA  GLY A 287     5219   6023   6525    280    332   -601       C  
ATOM   2310  C   GLY A 287     -22.716   3.303 -13.019  1.00 49.56           C  
ANISOU 2310  C   GLY A 287     5589   6415   6823    318    316   -531       C  
ATOM   2311  O   GLY A 287     -21.847   3.842 -13.671  1.00 44.24           O  
ANISOU 2311  O   GLY A 287     4913   5794   6099    310    267   -544       O  
ATOM   2312  N   GLY A 288     -22.514   2.888 -11.771  1.00 48.63           N  
ANISOU 2312  N   GLY A 288     5488   6279   6710    363    355   -456       N  
ATOM   2313  CA  GLY A 288     -21.265   3.172 -11.078  1.00 55.05           C  
ANISOU 2313  CA  GLY A 288     6313   7145   7456    403    331   -390       C  
ATOM   2314  C   GLY A 288     -21.195   4.609 -10.641  1.00 54.83           C  
ANISOU 2314  C   GLY A 288     6305   7188   7339    392    261   -381       C  
ATOM   2315  O   GLY A 288     -22.154   5.364 -10.774  1.00 46.93           O  
ANISOU 2315  O   GLY A 288     5312   6188   6328    358    236   -415       O  
ATOM   2316  N   ILE A 289     -20.033   5.013 -10.175  1.00 51.29           N  
ANISOU 2316  N   ILE A 289     5860   6799   6827    418    229   -340       N  
ATOM   2317  CA  ILE A 289     -19.888   6.355  -9.631  1.00 51.35           C  
ANISOU 2317  CA  ILE A 289     5883   6872   6753    409    169   -333       C  
ATOM   2318  C   ILE A 289     -19.808   7.414 -10.710  1.00 47.58           C  
ANISOU 2318  C   ILE A 289     5403   6429   6246    359    111   -392       C  
ATOM   2319  O   ILE A 289     -19.420   7.149 -11.894  1.00 43.45           O  
ANISOU 2319  O   ILE A 289     4862   5900   5744    340    106   -430       O  
ATOM   2320  CB  ILE A 289     -18.684   6.504  -8.678  1.00 52.42           C  
ANISOU 2320  CB  ILE A 289     6019   7070   6828    454    153   -277       C  
ATOM   2321  CG1 ILE A 289     -17.393   6.552  -9.438  1.00 59.88           C  
ANISOU 2321  CG1 ILE A 289     6944   8053   7752    450    124   -291       C  
ATOM   2322  CG2 ILE A 289     -18.724   5.388  -7.614  1.00 54.16           C  
ANISOU 2322  CG2 ILE A 289     6242   7262   7074    517    217   -208       C  
ATOM   2323  CD1 ILE A 289     -16.294   7.098  -8.554  1.00 68.70           C  
ANISOU 2323  CD1 ILE A 289     8056   9249   8795    481     89   -254       C  
ATOM   2324  N   THR A 290     -20.159   8.626 -10.282  1.00 43.93           N  
ANISOU 2324  N   THR A 290     4956   6001   5733    341     72   -396       N  
ATOM   2325  CA  THR A 290     -20.189   9.754 -11.173  1.00 41.94           C  
ANISOU 2325  CA  THR A 290     4705   5778   5451    298     25   -442       C  
ATOM   2326  C   THR A 290     -19.323  10.830 -10.616  1.00 37.38           C  
ANISOU 2326  C   THR A 290     4132   5263   4806    299    -16   -427       C  
ATOM   2327  O   THR A 290     -19.273  10.975  -9.430  1.00 40.00           O  
ANISOU 2327  O   THR A 290     4473   5614   5109    322    -15   -392       O  
ATOM   2328  CB  THR A 290     -21.618  10.320 -11.313  1.00 43.26           C  
ANISOU 2328  CB  THR A 290     4885   5922   5630    269     23   -471       C  
ATOM   2329  CG2 THR A 290     -22.490   9.290 -11.909  1.00 48.42           C  
ANISOU 2329  CG2 THR A 290     5525   6517   6352    264     63   -498       C  
ATOM   2330  OG1 THR A 290     -22.183  10.632 -10.027  1.00 40.70           O  
ANISOU 2330  OG1 THR A 290     4580   5595   5286    284     30   -436       O  
ATOM   2331  N   ILE A 291     -18.759  11.634 -11.500  1.00 37.87           N  
ANISOU 2331  N   ILE A 291     4187   5355   4844    271    -50   -459       N  
ATOM   2332  CA  ILE A 291     -18.005  12.757 -11.145  1.00 40.70           C  
ANISOU 2332  CA  ILE A 291     4547   5767   5150    261    -86   -458       C  
ATOM   2333  C   ILE A 291     -18.394  13.868 -12.053  1.00 37.21           C  
ANISOU 2333  C   ILE A 291     4111   5328   4699    222   -108   -497       C  
ATOM   2334  O   ILE A 291     -18.484  13.704 -13.306  1.00 40.28           O  
ANISOU 2334  O   ILE A 291     4491   5703   5109    209   -106   -524       O  
ATOM   2335  CB  ILE A 291     -16.484  12.474 -11.342  1.00 39.79           C  
ANISOU 2335  CB  ILE A 291     4409   5689   5020    277    -97   -450       C  
ATOM   2336  CG1 ILE A 291     -16.078  11.271 -10.500  1.00 40.90           C  
ANISOU 2336  CG1 ILE A 291     4542   5827   5171    325    -69   -404       C  
ATOM   2337  CG2 ILE A 291     -15.697  13.691 -10.999  1.00 38.41           C  
ANISOU 2337  CG2 ILE A 291     4229   5568   4796    261   -132   -459       C  
ATOM   2338  CD1 ILE A 291     -14.577  10.965 -10.529  1.00 40.32           C  
ANISOU 2338  CD1 ILE A 291     4443   5797   5077    348    -80   -390       C  
ATOM   2339  N   THR A 292     -18.549  15.022 -11.436  1.00 37.22           N  
ANISOU 2339  N   THR A 292     4124   5352   4665    207   -126   -498       N  
ATOM   2340  CA  THR A 292     -18.906  16.219 -12.163  1.00 36.13           C  
ANISOU 2340  CA  THR A 292     3993   5216   4515    174   -140   -526       C  
ATOM   2341  C   THR A 292     -18.204  17.333 -11.514  1.00 34.53           C  
ANISOU 2341  C   THR A 292     3791   5053   4276    161   -159   -529       C  
ATOM   2342  O   THR A 292     -17.995  17.330 -10.318  1.00 40.70           O  
ANISOU 2342  O   THR A 292     4573   5855   5035    174   -164   -512       O  
ATOM   2343  CB  THR A 292     -20.470  16.484 -12.026  1.00 37.75           C  
ANISOU 2343  CB  THR A 292     4219   5389   4733    164   -129   -531       C  
ATOM   2344  CG2 THR A 292     -20.869  17.613 -12.938  1.00 40.36           C  
ANISOU 2344  CG2 THR A 292     4556   5723   5055    139   -138   -555       C  
ATOM   2345  OG1 THR A 292     -21.182  15.264 -12.359  1.00 33.63           O  
ANISOU 2345  OG1 THR A 292     3693   4830   4254    178   -106   -532       O  
ATOM   2346  N   VAL A 293     -17.841  18.328 -12.285  1.00 36.06           N  
ANISOU 2346  N   VAL A 293     3981   5256   4461    136   -168   -551       N  
ATOM   2347  CA  VAL A 293     -17.433  19.596 -11.706  1.00 36.99           C  
ANISOU 2347  CA  VAL A 293     4101   5399   4554    114   -178   -563       C  
ATOM   2348  C   VAL A 293     -18.244  20.708 -12.341  1.00 36.66           C  
ANISOU 2348  C   VAL A 293     4075   5335   4516     90   -169   -577       C  
ATOM   2349  O   VAL A 293     -18.336  20.768 -13.610  1.00 34.87           O  
ANISOU 2349  O   VAL A 293     3848   5098   4304     87   -162   -583       O  
ATOM   2350  CB  VAL A 293     -15.945  19.927 -12.012  1.00 40.69           C  
ANISOU 2350  CB  VAL A 293     4543   5902   5014    106   -189   -576       C  
ATOM   2351  CG1 VAL A 293     -15.633  21.273 -11.521  1.00 38.53           C  
ANISOU 2351  CG1 VAL A 293     4267   5646   4724     78   -192   -599       C  
ATOM   2352  CG2 VAL A 293     -15.005  18.957 -11.335  1.00 45.02           C  
ANISOU 2352  CG2 VAL A 293     5070   6482   5551    133   -199   -561       C  
ATOM   2353  N   ASN A 294     -18.759  21.619 -11.512  1.00 34.11           N  
ANISOU 2353  N   ASN A 294     3767   5011   4180     75   -167   -581       N  
ATOM   2354  CA  ASN A 294     -19.620  22.700 -12.001  1.00 33.36           C  
ANISOU 2354  CA  ASN A 294     3690   4893   4090     56   -152   -588       C  
ATOM   2355  C   ASN A 294     -18.876  23.974 -11.976  1.00 36.38           C  
ANISOU 2355  C   ASN A 294     4066   5287   4468     30   -145   -607       C  
ATOM   2356  O   ASN A 294     -17.748  23.999 -11.513  1.00 34.57           O  
ANISOU 2356  O   ASN A 294     3817   5087   4230     24   -156   -620       O  
ATOM   2357  CB  ASN A 294     -20.948  22.712 -11.252  1.00 35.11           C  
ANISOU 2357  CB  ASN A 294     3934   5094   4310     60   -146   -578       C  
ATOM   2358  CG  ASN A 294     -20.887  23.427  -9.942  1.00 39.85           C  
ANISOU 2358  CG  ASN A 294     4541   5708   4891     49   -149   -584       C  
ATOM   2359  ND2 ASN A 294     -21.993  23.335  -9.179  1.00 39.81           N  
ANISOU 2359  ND2 ASN A 294     4556   5687   4883     56   -143   -572       N  
ATOM   2360  OD1 ASN A 294     -19.878  24.030  -9.585  1.00 40.87           O  
ANISOU 2360  OD1 ASN A 294     4656   5864   5008     34   -154   -603       O  
ATOM   2361  N   PHE A 295     -19.431  25.001 -12.583  1.00 36.36           N  
ANISOU 2361  N   PHE A 295     4078   5263   4474     17   -124   -609       N  
ATOM   2362  CA  PHE A 295     -18.760  26.329 -12.731  1.00 37.25           C  
ANISOU 2362  CA  PHE A 295     4185   5374   4594     -9   -103   -628       C  
ATOM   2363  C   PHE A 295     -19.861  27.344 -12.489  1.00 41.24           C  
ANISOU 2363  C   PHE A 295     4714   5851   5103    -20    -80   -624       C  
ATOM   2364  O   PHE A 295     -20.785  27.472 -13.343  1.00 37.59           O  
ANISOU 2364  O   PHE A 295     4267   5369   4645     -6    -65   -605       O  
ATOM   2365  CB  PHE A 295     -18.227  26.568 -14.155  1.00 41.00           C  
ANISOU 2365  CB  PHE A 295     4650   5843   5083     -6    -86   -623       C  
ATOM   2366  CG  PHE A 295     -17.008  25.743 -14.537  1.00 39.42           C  
ANISOU 2366  CG  PHE A 295     4425   5668   4883      1   -103   -628       C  
ATOM   2367  CD1 PHE A 295     -17.091  24.366 -14.641  1.00 41.00           C  
ANISOU 2367  CD1 PHE A 295     4620   5879   5077     25   -126   -616       C  
ATOM   2368  CD2 PHE A 295     -15.791  26.358 -14.855  1.00 44.97           C  
ANISOU 2368  CD2 PHE A 295     5107   6380   5599    -16    -89   -644       C  
ATOM   2369  CE1 PHE A 295     -16.013  23.607 -15.058  1.00 45.62           C  
ANISOU 2369  CE1 PHE A 295     5183   6485   5665     35   -137   -618       C  
ATOM   2370  CE2 PHE A 295     -14.694  25.601 -15.288  1.00 40.66           C  
ANISOU 2370  CE2 PHE A 295     4536   5856   5053     -7   -104   -646       C  
ATOM   2371  CZ  PHE A 295     -14.800  24.220 -15.343  1.00 43.92           C  
ANISOU 2371  CZ  PHE A 295     4947   6282   5456     19   -129   -633       C  
ATOM   2372  N   TRP A 296     -19.813  28.029 -11.338  1.00 39.26           N  
ANISOU 2372  N   TRP A 296     4465   5603   4847    -42    -76   -644       N  
ATOM   2373  CA  TRP A 296     -20.895  28.911 -10.926  1.00 38.10           C  
ANISOU 2373  CA  TRP A 296     4343   5429   4704    -51    -54   -642       C  
ATOM   2374  C   TRP A 296     -20.478  30.382 -11.043  1.00 43.75           C  
ANISOU 2374  C   TRP A 296     5056   6124   5441    -81    -15   -663       C  
ATOM   2375  O   TRP A 296     -19.529  30.797 -10.399  1.00 46.67           O  
ANISOU 2375  O   TRP A 296     5405   6511   5814   -107    -15   -699       O  
ATOM   2376  CB  TRP A 296     -21.327  28.602  -9.506  1.00 37.72           C  
ANISOU 2376  CB  TRP A 296     4301   5394   4634    -51    -73   -649       C  
ATOM   2377  CG  TRP A 296     -22.425  27.610  -9.315  1.00 41.20           C  
ANISOU 2377  CG  TRP A 296     4759   5828   5067    -23    -88   -621       C  
ATOM   2378  CD1 TRP A 296     -23.597  27.488 -10.059  1.00 42.09           C  
ANISOU 2378  CD1 TRP A 296     4889   5912   5189     -9    -77   -597       C  
ATOM   2379  CD2 TRP A 296     -22.568  26.705  -8.241  1.00 38.48           C  
ANISOU 2379  CD2 TRP A 296     4415   5503   4703     -7   -110   -614       C  
ATOM   2380  CE2 TRP A 296     -23.811  26.017  -8.421  1.00 38.89           C  
ANISOU 2380  CE2 TRP A 296     4484   5529   4761     13   -107   -588       C  
ATOM   2381  CE3 TRP A 296     -21.762  26.357  -7.158  1.00 41.82           C  
ANISOU 2381  CE3 TRP A 296     4821   5964   5101     -3   -129   -627       C  
ATOM   2382  NE1 TRP A 296     -24.394  26.500  -9.541  1.00 37.42           N  
ANISOU 2382  NE1 TRP A 296     4306   5319   4593     10    -90   -582       N  
ATOM   2383  CZ2 TRP A 296     -24.239  25.000  -7.575  1.00 41.26           C  
ANISOU 2383  CZ2 TRP A 296     4789   5834   5054     36   -118   -571       C  
ATOM   2384  CZ3 TRP A 296     -22.209  25.337  -6.275  1.00 41.94           C  
ANISOU 2384  CZ3 TRP A 296     4843   5991   5099     26   -142   -604       C  
ATOM   2385  CH2 TRP A 296     -23.468  24.702  -6.488  1.00 41.52           C  
ANISOU 2385  CH2 TRP A 296     4810   5902   5061     44   -132   -575       C  
ATOM   2386  N   TYR A 297     -21.155  31.112 -11.933  1.00 38.91           N  
ANISOU 2386  N   TYR A 297     4459   5478   4844    -75     20   -641       N  
ATOM   2387  CA  TYR A 297     -20.987  32.535 -12.168  1.00 38.51           C  
ANISOU 2387  CA  TYR A 297     4412   5396   4823    -97     72   -650       C  
ATOM   2388  C   TYR A 297     -22.165  33.342 -11.632  1.00 44.78           C  
ANISOU 2388  C   TYR A 297     5232   6160   5621   -101     98   -642       C  
ATOM   2389  O   TYR A 297     -23.333  32.956 -11.814  1.00 41.06           O  
ANISOU 2389  O   TYR A 297     4781   5684   5135    -75     89   -612       O  
ATOM   2390  CB  TYR A 297     -20.872  32.829 -13.660  1.00 36.41           C  
ANISOU 2390  CB  TYR A 297     4146   5115   4570    -76    104   -619       C  
ATOM   2391  CG  TYR A 297     -19.600  32.218 -14.300  1.00 39.07           C  
ANISOU 2391  CG  TYR A 297     4458   5477   4910    -74     88   -627       C  
ATOM   2392  CD1 TYR A 297     -19.558  30.871 -14.661  1.00 41.35           C  
ANISOU 2392  CD1 TYR A 297     4739   5796   5174    -49     44   -616       C  
ATOM   2393  CD2 TYR A 297     -18.438  32.969 -14.482  1.00 39.67           C  
ANISOU 2393  CD2 TYR A 297     4512   5542   5016    -99    121   -650       C  
ATOM   2394  CE1 TYR A 297     -18.398  30.292 -15.138  1.00 42.68           C  
ANISOU 2394  CE1 TYR A 297     4884   5987   5345    -47     29   -624       C  
ATOM   2395  CE2 TYR A 297     -17.260  32.401 -14.980  1.00 42.47           C  
ANISOU 2395  CE2 TYR A 297     4841   5921   5372    -99    105   -659       C  
ATOM   2396  CZ  TYR A 297     -17.263  31.052 -15.330  1.00 44.85           C  
ANISOU 2396  CZ  TYR A 297     5139   6254   5645    -71     59   -643       C  
ATOM   2397  OH  TYR A 297     -16.142  30.409 -15.836  1.00 38.60           O  
ANISOU 2397  OH  TYR A 297     4324   5487   4855    -66     43   -649       O  
ATOM   2398  N   LYS A 298     -21.862  34.459 -10.981  1.00 44.72           N  
ANISOU 2398  N   LYS A 298     5221   6131   5636   -135    133   -674       N  
ATOM   2399  CA  LYS A 298     -22.874  35.445 -10.695  1.00 43.13           C  
ANISOU 2399  CA  LYS A 298     5045   5891   5449   -140    174   -665       C  
ATOM   2400  C   LYS A 298     -23.474  35.851 -12.002  1.00 39.66           C  
ANISOU 2400  C   LYS A 298     4621   5426   5022   -109    213   -616       C  
ATOM   2401  O   LYS A 298     -22.776  36.010 -12.985  1.00 40.74           O  
ANISOU 2401  O   LYS A 298     4746   5559   5174   -101    234   -605       O  
ATOM   2402  CB  LYS A 298     -22.243  36.688 -10.047  1.00 50.19           C  
ANISOU 2402  CB  LYS A 298     5928   6761   6379   -185    218   -713       C  
ATOM   2403  CG  LYS A 298     -21.820  36.560  -8.600  1.00 57.53           C  
ANISOU 2403  CG  LYS A 298     6841   7722   7294   -215    186   -770       C  
ATOM   2404  CD  LYS A 298     -21.971  37.948  -7.948  1.00 67.00           C  
ANISOU 2404  CD  LYS A 298     8044   8883   8529   -252    241   -809       C  
ATOM   2405  CE  LYS A 298     -21.177  38.164  -6.661  1.00 73.45           C  
ANISOU 2405  CE  LYS A 298     8830   9734   9340   -292    224   -886       C  
ATOM   2406  NZ  LYS A 298     -21.152  36.923  -5.867  1.00 69.57           N1+
ANISOU 2406  NZ  LYS A 298     8333   9307   8791   -271    151   -887       N1+
ATOM   2407  N   GLY A 299     -24.767  36.099 -12.030  1.00 40.89           N  
ANISOU 2407  N   GLY A 299     4802   5564   5170    -88    226   -585       N  
ATOM   2408  CA  GLY A 299     -25.402  36.633 -13.230  1.00 43.95           C  
ANISOU 2408  CA  GLY A 299     5201   5932   5563    -53    269   -537       C  
ATOM   2409  C   GLY A 299     -25.090  38.116 -13.501  1.00 44.89           C  
ANISOU 2409  C   GLY A 299     5324   6003   5727    -65    349   -532       C  
ATOM   2410  O   GLY A 299     -24.499  38.770 -12.712  1.00 43.90           O  
ANISOU 2410  O   GLY A 299     5193   5855   5632   -107    372   -573       O  
ATOM   2411  N   ALA A 300     -25.500  38.584 -14.661  1.00 49.41           N  
ANISOU 2411  N   ALA A 300     5905   6563   6302    -25    393   -481       N  
ATOM   2412  CA  ALA A 300     -25.369  39.979 -15.108  1.00 53.77           C  
ANISOU 2412  CA  ALA A 300     6465   7065   6899    -23    482   -460       C  
ATOM   2413  C   ALA A 300     -26.032  40.907 -14.129  1.00 55.69           C  
ANISOU 2413  C   ALA A 300     6726   7265   7169    -48    521   -473       C  
ATOM   2414  O   ALA A 300     -26.996  40.505 -13.475  1.00 54.81           O  
ANISOU 2414  O   ALA A 300     6628   7167   7030    -44    483   -474       O  
ATOM   2415  CB  ALA A 300     -26.046  40.114 -16.469  1.00 51.39           C  
ANISOU 2415  CB  ALA A 300     6173   6775   6578     42    511   -391       C  
ATOM   2416  N   PRO A 301     -25.561  42.167 -14.036  1.00 66.85           N  
ANISOU 2416  N   PRO A 301     8139   8622   8639    -72    602   -484       N  
ATOM   2417  CA  PRO A 301     -26.328  43.131 -13.192  1.00 63.96           C  
ANISOU 2417  CA  PRO A 301     7792   8209   8300    -91    648   -493       C  
ATOM   2418  C   PRO A 301     -27.706  43.348 -13.814  1.00 61.65           C  
ANISOU 2418  C   PRO A 301     7526   7914   7985    -33    671   -421       C  
ATOM   2419  O   PRO A 301     -27.886  43.189 -15.025  1.00 64.48           O  
ANISOU 2419  O   PRO A 301     7884   8292   8323     20    681   -365       O  
ATOM   2420  CB  PRO A 301     -25.472  44.391 -13.197  1.00 60.23           C  
ANISOU 2420  CB  PRO A 301     7310   7673   7901   -126    740   -517       C  
ATOM   2421  CG  PRO A 301     -24.566  44.241 -14.385  1.00 65.95           C  
ANISOU 2421  CG  PRO A 301     8018   8405   8634   -103    758   -491       C  
ATOM   2422  CD  PRO A 301     -24.643  42.848 -14.959  1.00 63.37           C  
ANISOU 2422  CD  PRO A 301     7687   8151   8240    -67    670   -468       C  
ATOM   2423  N   THR A 302     -28.707  43.590 -12.999  1.00 71.72           N  
ANISOU 2423  N   THR A 302     8819   9175   9255    -38    670   -424       N  
ATOM   2424  CA  THR A 302     -30.044  43.862 -13.555  1.00 82.20           C  
ANISOU 2424  CA  THR A 302    10168  10501  10563     17    695   -358       C  
ATOM   2425  C   THR A 302     -30.017  45.239 -14.219  1.00 80.10           C  
ANISOU 2425  C   THR A 302     9911  10177  10346     40    806   -314       C  
ATOM   2426  O   THR A 302     -29.258  46.113 -13.765  1.00 80.14           O  
ANISOU 2426  O   THR A 302     9911  10125  10411     -5    867   -350       O  
ATOM   2427  CB  THR A 302     -31.105  43.912 -12.450  1.00 84.50           C  
ANISOU 2427  CB  THR A 302    10476  10783  10844      3    677   -372       C  
ATOM   2428  CG2 THR A 302     -31.174  42.611 -11.695  1.00 89.15           C  
ANISOU 2428  CG2 THR A 302    11058  11422  11391    -16    580   -411       C  
ATOM   2429  OG1 THR A 302     -30.739  44.942 -11.539  1.00 86.15           O  
ANISOU 2429  OG1 THR A 302    10691  10935  11107    -46    734   -415       O  
ATOM   2430  N   PRO A 303     -30.843  45.448 -15.265  1.00 82.74           N  
ANISOU 2430  N   PRO A 303    10255  10525  10657    111    836   -238       N  
ATOM   2431  CA  PRO A 303     -30.918  46.800 -15.830  1.00 92.44           C  
ANISOU 2431  CA  PRO A 303    11494  11693  11933    140    952   -186       C  
ATOM   2432  C   PRO A 303     -31.181  47.860 -14.738  1.00 94.85           C  
ANISOU 2432  C   PRO A 303    11816  11925  12297     95   1015   -215       C  
ATOM   2433  O   PRO A 303     -31.947  47.598 -13.801  1.00 98.18           O  
ANISOU 2433  O   PRO A 303    12248  12355  12700     75    972   -241       O  
ATOM   2434  CB  PRO A 303     -32.082  46.700 -16.838  1.00 94.67           C  
ANISOU 2434  CB  PRO A 303    11784  12021  12164    228    954   -103       C  
ATOM   2435  CG  PRO A 303     -32.149  45.250 -17.210  1.00 92.59           C  
ANISOU 2435  CG  PRO A 303    11504  11843  11833    243    846   -117       C  
ATOM   2436  CD  PRO A 303     -31.756  44.510 -15.952  1.00 88.68           C  
ANISOU 2436  CD  PRO A 303    11004  11347  11341    169    773   -198       C  
ATOM   2437  N   LYS A 304     -30.518  49.021 -14.824  1.00114.69           N  
ANISOU 2437  N   LYS A 304    14329  14364  14884     76   1119   -216       N  
ATOM   2438  CA  LYS A 304     -30.743  50.112 -13.849  1.00113.97           C  
ANISOU 2438  CA  LYS A 304    14251  14196  14856     32   1192   -249       C  
ATOM   2439  C   LYS A 304     -32.208  50.523 -13.929  1.00114.03           C  
ANISOU 2439  C   LYS A 304    14285  14197  14844     87   1222   -183       C  
ATOM   2440  O   LYS A 304     -32.774  50.977 -12.937  1.00 94.18           O  
ANISOU 2440  O   LYS A 304    11784  11648  12352     55   1238   -212       O  
ATOM   2441  CB  LYS A 304     -29.804  51.322 -14.056  1.00115.63           C  
ANISOU 2441  CB  LYS A 304    14453  14320  15159      6   1313   -259       C  
ATOM   2442  CG  LYS A 304     -28.543  51.316 -13.183  1.00118.09           C  
ANISOU 2442  CG  LYS A 304    14738  14613  15517    -83   1299   -367       C  
ATOM   2443  CD  LYS A 304     -28.218  52.702 -12.624  1.00121.05           C  
ANISOU 2443  CD  LYS A 304    15111  14889  15993   -132   1417   -409       C  
ATOM   2444  CE  LYS A 304     -26.784  52.818 -12.131  1.00117.47           C  
ANISOU 2444  CE  LYS A 304    14621  14416  15595   -211   1423   -508       C  
ATOM   2445  NZ  LYS A 304     -25.867  53.111 -13.266  1.00116.98           N1+
ANISOU 2445  NZ  LYS A 304    14544  14326  15576   -190   1490   -472       N1+
ATOM   2446  N   ARG A 305     -32.816  50.336 -15.109  1.00126.01           N  
ANISOU 2446  N   ARG A 305    15806  15756  16316    171   1226    -96       N  
ATOM   2447  CA  ARG A 305     -34.275  50.284 -15.203  1.00123.80           C  
ANISOU 2447  CA  ARG A 305    15541  15505  15990    227   1213    -41       C  
ATOM   2448  C   ARG A 305     -34.929  49.136 -16.034  1.00117.38           C  
ANISOU 2448  C   ARG A 305    14718  14793  15088    290   1123     -1       C  
ATOM   2449  O   ARG A 305     -34.473  48.696 -17.112  1.00112.64           O  
ANISOU 2449  O   ARG A 305    14102  14239  14456    332   1107     28       O  
ATOM   2450  CB  ARG A 305     -34.836  51.658 -15.554  1.00128.45           C  
ANISOU 2450  CB  ARG A 305    16149  16028  16626    273   1341     28       C  
ATOM   2451  CG  ARG A 305     -34.688  52.630 -14.386  1.00129.78           C  
ANISOU 2451  CG  ARG A 305    16330  16103  16874    204   1410    -25       C  
ATOM   2452  CD  ARG A 305     -35.710  53.741 -14.396  1.00127.82           C  
ANISOU 2452  CD  ARG A 305    16106  15801  16658    247   1510     37       C  
ATOM   2453  NE  ARG A 305     -35.885  54.271 -15.737  1.00133.53           N  
ANISOU 2453  NE  ARG A 305    16832  16526  17378    338   1590    141       N  
ATOM   2454  CZ  ARG A 305     -36.727  55.247 -16.040  1.00128.76           C  
ANISOU 2454  CZ  ARG A 305    16245  15881  16795    398   1689    219       C  
ATOM   2455  NH1 ARG A 305     -37.460  55.821 -15.095  1.00121.77           N1+
ANISOU 2455  NH1 ARG A 305    15378  14945  15942    372   1722    201       N1+
ATOM   2456  NH2 ARG A 305     -36.819  55.659 -17.296  1.00134.17           N  
ANISOU 2456  NH2 ARG A 305    16930  16578  17469    489   1760    317       N  
ATOM   2457  N   ILE A 306     -36.050  48.716 -15.458  1.00107.50           N  
ANISOU 2457  N   ILE A 306    13473  13569  13800    295   1069     -6       N  
ATOM   2458  CA  ILE A 306     -36.801  47.523 -15.779  1.00 97.24           C  
ANISOU 2458  CA  ILE A 306    12161  12358  12427    329    971      0       C  
ATOM   2459  C   ILE A 306     -37.738  47.731 -16.937  1.00 91.72           C  
ANISOU 2459  C   ILE A 306    11457  11706  11685    424    998     84       C  
ATOM   2460  O   ILE A 306     -38.496  48.693 -16.959  1.00 92.45           O  
ANISOU 2460  O   ILE A 306    11565  11766  11795    461   1072    135       O  
ATOM   2461  CB  ILE A 306     -37.671  47.147 -14.534  1.00 99.79           C  
ANISOU 2461  CB  ILE A 306    12495  12679  12742    291    919    -40       C  
ATOM   2462  CG1 ILE A 306     -36.786  46.953 -13.287  1.00106.44           C  
ANISOU 2462  CG1 ILE A 306    13331  13521  13589    212    847   -125       C  
ATOM   2463  CG2 ILE A 306     -38.623  45.976 -14.797  1.00 92.78           C  
ANISOU 2463  CG2 ILE A 306    11599  11858  11795    347    867     -6       C  
ATOM   2464  CD1 ILE A 306     -35.701  45.871 -13.387  1.00106.63           C  
ANISOU 2464  CD1 ILE A 306    13333  13584  13598    201    799   -150       C  
ATOM   2465  N   GLU A 307     -37.773  46.767 -17.839  1.00 81.04           N  
ANISOU 2465  N   GLU A 307    10081  10437  10272    465    932     93       N  
ATOM   2466  CA  GLU A 307     -38.662  46.829 -18.971  1.00 80.65           C  
ANISOU 2466  CA  GLU A 307    10018  10454  10169    560    943    164       C  
ATOM   2467  C   GLU A 307     -39.803  45.829 -18.849  1.00 75.71           C  
ANISOU 2467  C   GLU A 307     9375   9902   9488    575    853    144       C  
ATOM   2468  O   GLU A 307     -39.667  44.750 -18.286  1.00 85.51           O  
ANISOU 2468  O   GLU A 307    10607  11164  10719    524    768     80       O  
ATOM   2469  CB  GLU A 307     -37.830  46.580 -20.210  1.00 99.77           C  
ANISOU 2469  CB  GLU A 307    12421  12920  12564    602    946    188       C  
ATOM   2470  CG  GLU A 307     -36.524  47.376 -20.114  1.00114.73           C  
ANISOU 2470  CG  GLU A 307    14330  14733  14527    564   1024    185       C  
ATOM   2471  CD  GLU A 307     -35.612  47.225 -21.312  1.00122.37           C  
ANISOU 2471  CD  GLU A 307    15281  15734  15476    604   1039    213       C  
ATOM   2472  OE1 GLU A 307     -35.729  46.227 -22.051  1.00128.88           O  
ANISOU 2472  OE1 GLU A 307    16083  16649  16236    639    965    209       O  
ATOM   2473  OE2 GLU A 307     -34.758  48.109 -21.500  1.00119.26           O1-
ANISOU 2473  OE2 GLU A 307    14898  15276  15138    599   1128    236       O1-
ATOM   2474  N   TYR A 308     -40.953  46.203 -19.345  1.00 66.30           N  
ANISOU 2474  N   TYR A 308     8177   8749   8263    647    876    201       N  
ATOM   2475  CA  TYR A 308     -42.125  45.359 -19.227  1.00 76.58           C  
ANISOU 2475  CA  TYR A 308     9458  10118   9518    662    800    181       C  
ATOM   2476  C   TYR A 308     -42.355  44.764 -20.589  1.00 83.63           C  
ANISOU 2476  C   TYR A 308    10314  11118  10342    738    764    204       C  
ATOM   2477  O   TYR A 308     -41.949  45.351 -21.581  1.00 94.97           O  
ANISOU 2477  O   TYR A 308    11747  12572  11764    798    820    260       O  
ATOM   2478  CB  TYR A 308     -43.329  46.180 -18.741  1.00 73.42           C  
ANISOU 2478  CB  TYR A 308     9073   9691   9129    688    848    221       C  
ATOM   2479  CG  TYR A 308     -43.018  46.741 -17.381  1.00 72.30           C  
ANISOU 2479  CG  TYR A 308     8968   9447   9056    609    883    189       C  
ATOM   2480  CD1 TYR A 308     -43.209  45.973 -16.256  1.00 74.08           C  
ANISOU 2480  CD1 TYR A 308     9197   9659   9291    541    816    122       C  
ATOM   2481  CD2 TYR A 308     -42.421  47.984 -17.229  1.00 75.28           C  
ANISOU 2481  CD2 TYR A 308     9373   9741   9490    601    985    219       C  
ATOM   2482  CE1 TYR A 308     -42.869  46.439 -15.004  1.00 72.14           C  
ANISOU 2482  CE1 TYR A 308     8980   9329   9099    470    842     86       C  
ATOM   2483  CE2 TYR A 308     -42.068  48.452 -15.975  1.00 82.38           C  
ANISOU 2483  CE2 TYR A 308    10298  10551  10450    523   1012    175       C  
ATOM   2484  CZ  TYR A 308     -42.309  47.661 -14.866  1.00 77.56           C  
ANISOU 2484  CZ  TYR A 308     9690   9940   9837    461    937    108       C  
ATOM   2485  OH  TYR A 308     -41.998  48.070 -13.602  1.00 87.57           O  
ANISOU 2485  OH  TYR A 308    10981  11134  11155    389    958     61       O  
ATOM   2486  N   PRO A 309     -42.976  43.587 -20.655  1.00 83.11           N  
ANISOU 2486  N   PRO A 309    10217  11125  10236    736    673    158       N  
ATOM   2487  CA  PRO A 309     -43.497  42.851 -19.524  1.00 77.24           C  
ANISOU 2487  CA  PRO A 309     9475  10361   9510    672    613     97       C  
ATOM   2488  C   PRO A 309     -42.327  42.209 -18.761  1.00 63.86           C  
ANISOU 2488  C   PRO A 309     7795   8615   7853    585    577     34       C  
ATOM   2489  O   PRO A 309     -41.256  41.969 -19.341  1.00 60.77           O  
ANISOU 2489  O   PRO A 309     7397   8233   7457    582    572     27       O  
ATOM   2490  CB  PRO A 309     -44.365  41.786 -20.193  1.00 75.67           C  
ANISOU 2490  CB  PRO A 309     9229  10265   9254    711    539     72       C  
ATOM   2491  CG  PRO A 309     -43.593  41.453 -21.446  1.00 75.87           C  
ANISOU 2491  CG  PRO A 309     9231  10355   9241    752    527     79       C  
ATOM   2492  CD  PRO A 309     -42.889  42.731 -21.861  1.00 76.62           C  
ANISOU 2492  CD  PRO A 309     9353  10405   9352    786    620    149       C  
ATOM   2493  N   LEU A 310     -42.498  42.017 -17.457  1.00 57.94           N  
ANISOU 2493  N   LEU A 310     7064   7811   7138    520    558     -4       N  
ATOM   2494  CA  LEU A 310     -41.417  41.417 -16.627  1.00 59.23           C  
ANISOU 2494  CA  LEU A 310     7239   7932   7332    443    523    -63       C  
ATOM   2495  C   LEU A 310     -41.255  39.958 -16.965  1.00 53.22           C  
ANISOU 2495  C   LEU A 310     6447   7231   6543    434    440   -109       C  
ATOM   2496  O   LEU A 310     -42.231  39.295 -17.221  1.00 52.90           O  
ANISOU 2496  O   LEU A 310     6381   7242   6474    459    399   -119       O  
ATOM   2497  CB  LEU A 310     -41.772  41.483 -15.135  1.00 55.55           C  
ANISOU 2497  CB  LEU A 310     6798   7407   6900    385    519    -93       C  
ATOM   2498  CG  LEU A 310     -41.511  42.793 -14.398  1.00 53.37           C  
ANISOU 2498  CG  LEU A 310     6557   7052   6670    360    596    -77       C  
ATOM   2499  CD1 LEU A 310     -41.712  42.493 -12.929  1.00 57.69           C  
ANISOU 2499  CD1 LEU A 310     7121   7559   7238    299    569   -123       C  
ATOM   2500  CD2 LEU A 310     -40.130  43.414 -14.609  1.00 51.20           C  
ANISOU 2500  CD2 LEU A 310     6291   6736   6425    338    642    -78       C  
ATOM   2501  N   LYS A 311     -40.053  39.434 -16.907  1.00 50.47           N  
ANISOU 2501  N   LYS A 311     6098   6871   6205    396    416   -143       N  
ATOM   2502  CA  LYS A 311     -39.864  37.992 -17.140  1.00 48.52           C  
ANISOU 2502  CA  LYS A 311     5824   6673   5939    383    341   -190       C  
ATOM   2503  C   LYS A 311     -40.118  37.150 -15.888  1.00 44.40           C  
ANISOU 2503  C   LYS A 311     5307   6124   5438    328    296   -237       C  
ATOM   2504  O   LYS A 311     -40.184  37.700 -14.784  1.00 48.86           O  
ANISOU 2504  O   LYS A 311     5901   6633   6031    294    320   -238       O  
ATOM   2505  CB  LYS A 311     -38.452  37.793 -17.665  1.00 55.41           C  
ANISOU 2505  CB  LYS A 311     6691   7546   6812    371    338   -200       C  
ATOM   2506  CG  LYS A 311     -38.299  38.326 -19.107  1.00 65.26           C  
ANISOU 2506  CG  LYS A 311     7925   8840   8030    437    373   -154       C  
ATOM   2507  CD  LYS A 311     -36.866  38.717 -19.450  1.00 73.12           C  
ANISOU 2507  CD  LYS A 311     8930   9808   9043    424    405   -147       C  
ATOM   2508  CE  LYS A 311     -35.884  37.563 -19.323  1.00 88.58           C  
ANISOU 2508  CE  LYS A 311    10875  11776  11005    381    346   -200       C  
ATOM   2509  NZ  LYS A 311     -34.442  37.975 -19.375  1.00 94.88           N1+
ANISOU 2509  NZ  LYS A 311    11682  12536  11829    355    377   -200       N1+
ATOM   2510  N   ALA A 312     -40.180  35.822 -16.032  1.00 41.74           N  
ANISOU 2510  N   ALA A 312     4944   5824   5090    320    236   -277       N  
ATOM   2511  CA  ALA A 312     -40.578  34.967 -14.952  1.00 43.66           C  
ANISOU 2511  CA  ALA A 312     5190   6047   5352    281    201   -313       C  
ATOM   2512  C   ALA A 312     -39.535  35.067 -13.882  1.00 39.19           C  
ANISOU 2512  C   ALA A 312     4651   5426   4811    229    205   -329       C  
ATOM   2513  O   ALA A 312     -39.848  35.159 -12.708  1.00 38.67           O  
ANISOU 2513  O   ALA A 312     4606   5323   4764    200    209   -337       O  
ATOM   2514  CB  ALA A 312     -40.751  33.518 -15.417  1.00 49.11           C  
ANISOU 2514  CB  ALA A 312     5844   6782   6034    284    146   -353       C  
ATOM   2515  N   HIS A 313     -38.284  35.087 -14.276  1.00 39.25           N  
ANISOU 2515  N   HIS A 313     4658   5435   4820    219    206   -334       N  
ATOM   2516  CA  HIS A 313     -37.229  35.037 -13.275  1.00 36.82           C  
ANISOU 2516  CA  HIS A 313     4366   5089   4532    170    203   -359       C  
ATOM   2517  C   HIS A 313     -37.217  36.354 -12.484  1.00 37.95           C  
ANISOU 2517  C   HIS A 313     4540   5183   4696    151    255   -345       C  
ATOM   2518  O   HIS A 313     -36.858  36.370 -11.347  1.00 39.60           O  
ANISOU 2518  O   HIS A 313     4764   5363   4919    112    251   -368       O  
ATOM   2519  CB  HIS A 313     -35.883  34.685 -13.890  1.00 41.93           C  
ANISOU 2519  CB  HIS A 313     5002   5753   5177    163    190   -372       C  
ATOM   2520  CG  HIS A 313     -35.257  35.806 -14.628  1.00 47.85           C  
ANISOU 2520  CG  HIS A 313     5757   6493   5930    178    239   -344       C  
ATOM   2521  CD2 HIS A 313     -35.318  36.156 -15.934  1.00 46.70           C  
ANISOU 2521  CD2 HIS A 313     5599   6378   5766    224    261   -313       C  
ATOM   2522  ND1 HIS A 313     -34.519  36.792 -13.994  1.00 49.76           N  
ANISOU 2522  ND1 HIS A 313     6019   6689   6199    146    281   -346       N  
ATOM   2523  CE1 HIS A 313     -34.164  37.706 -14.876  1.00 50.46           C  
ANISOU 2523  CE1 HIS A 313     6108   6771   6293    170    332   -315       C  
ATOM   2524  NE2 HIS A 313     -34.641  37.347 -16.055  1.00 48.20           N  
ANISOU 2524  NE2 HIS A 313     5804   6532   5976    221    321   -290       N  
ATOM   2525  N   GLN A 314     -37.676  37.445 -13.068  1.00 40.14           N  
ANISOU 2525  N   GLN A 314     4824   5451   4974    181    305   -306       N  
ATOM   2526  CA  GLN A 314     -37.759  38.723 -12.334  1.00 38.67           C  
ANISOU 2526  CA  GLN A 314     4665   5211   4814    163    363   -295       C  
ATOM   2527  C   GLN A 314     -38.879  38.719 -11.307  1.00 36.07           C  
ANISOU 2527  C   GLN A 314     4352   4864   4488    154    359   -298       C  
ATOM   2528  O   GLN A 314     -38.726  39.324 -10.240  1.00 39.45           O  
ANISOU 2528  O   GLN A 314     4801   5249   4938    119    383   -314       O  
ATOM   2529  CB  GLN A 314     -37.957  39.890 -13.305  1.00 42.38           C  
ANISOU 2529  CB  GLN A 314     5140   5674   5288    206    429   -244       C  
ATOM   2530  CG  GLN A 314     -36.842  39.962 -14.346  1.00 45.22           C  
ANISOU 2530  CG  GLN A 314     5486   6048   5645    219    442   -236       C  
ATOM   2531  CD  GLN A 314     -37.144  40.997 -15.379  1.00 46.51           C  
ANISOU 2531  CD  GLN A 314     5651   6211   5806    274    508   -177       C  
ATOM   2532  NE2 GLN A 314     -36.423  42.073 -15.307  1.00 52.41           N  
ANISOU 2532  NE2 GLN A 314     6414   6906   6592    260    576   -165       N  
ATOM   2533  OE1 GLN A 314     -38.089  40.871 -16.179  1.00 55.10           O  
ANISOU 2533  OE1 GLN A 314     6727   7346   6860    331    503   -142       O  
ATOM   2534  N   LYS A 315     -39.964  37.999 -11.589  1.00 35.67           N  
ANISOU 2534  N   LYS A 315     4287   4847   4418    183    327   -289       N  
ATOM   2535  CA  LYS A 315     -41.035  37.784 -10.598  1.00 37.72           C  
ANISOU 2535  CA  LYS A 315     4557   5092   4683    173    317   -296       C  
ATOM   2536  C   LYS A 315     -40.575  36.892  -9.481  1.00 38.67           C  
ANISOU 2536  C   LYS A 315     4681   5202   4808    131    277   -336       C  
ATOM   2537  O   LYS A 315     -40.871  37.130  -8.319  1.00 37.61           O  
ANISOU 2537  O   LYS A 315     4567   5037   4684    108    287   -345       O  
ATOM   2538  CB  LYS A 315     -42.300  37.275 -11.247  1.00 37.28           C  
ANISOU 2538  CB  LYS A 315     4478   5076   4609    214    298   -280       C  
ATOM   2539  CG  LYS A 315     -42.919  38.317 -12.208  1.00 46.99           C  
ANISOU 2539  CG  LYS A 315     5705   6320   5827    265    344   -232       C  
ATOM   2540  CD  LYS A 315     -44.053  37.710 -13.031  1.00 51.28           C  
ANISOU 2540  CD  LYS A 315     6214   6924   6345    311    316   -225       C  
ATOM   2541  CE  LYS A 315     -44.820  38.758 -13.810  1.00 64.98           C  
ANISOU 2541  CE  LYS A 315     7946   8679   8063    369    363   -173       C  
ATOM   2542  NZ  LYS A 315     -45.714  38.138 -14.853  1.00 69.83           N1+
ANISOU 2542  NZ  LYS A 315     8516   9373   8643    420    330   -173       N1+
ATOM   2543  N   VAL A 316     -39.808  35.889  -9.816  1.00 37.58           N  
ANISOU 2543  N   VAL A 316     4524   5091   4662    125    236   -358       N  
ATOM   2544  CA  VAL A 316     -39.213  35.081  -8.771  1.00 38.27           C  
ANISOU 2544  CA  VAL A 316     4616   5171   4753     91    204   -389       C  
ATOM   2545  C   VAL A 316     -38.300  35.954  -7.888  1.00 38.47           C  
ANISOU 2545  C   VAL A 316     4662   5166   4787     56    230   -405       C  
ATOM   2546  O   VAL A 316     -38.388  35.907  -6.636  1.00 35.21           O  
ANISOU 2546  O   VAL A 316     4264   4737   4375     34    226   -422       O  
ATOM   2547  CB  VAL A 316     -38.373  33.972  -9.300  1.00 35.97           C  
ANISOU 2547  CB  VAL A 316     4302   4910   4455     90    164   -408       C  
ATOM   2548  CG1 VAL A 316     -37.727  33.174  -8.166  1.00 40.13           C  
ANISOU 2548  CG1 VAL A 316     4833   5431   4983     62    137   -434       C  
ATOM   2549  CG2 VAL A 316     -39.181  33.081 -10.206  1.00 34.73           C  
ANISOU 2549  CG2 VAL A 316     4118   4785   4291    120    139   -405       C  
ATOM   2550  N   ALA A 317     -37.496  36.790  -8.502  1.00 38.23           N  
ANISOU 2550  N   ALA A 317     4631   5128   4765     53    260   -402       N  
ATOM   2551  CA  ALA A 317     -36.616  37.646  -7.665  1.00 40.90           C  
ANISOU 2551  CA  ALA A 317     4983   5437   5118     15    288   -428       C  
ATOM   2552  C   ALA A 317     -37.439  38.544  -6.710  1.00 41.86           C  
ANISOU 2552  C   ALA A 317     5129   5523   5252      4    325   -427       C  
ATOM   2553  O   ALA A 317     -37.098  38.673  -5.519  1.00 37.52           O  
ANISOU 2553  O   ALA A 317     4588   4963   4702    -26    322   -461       O  
ATOM   2554  CB  ALA A 317     -35.736  38.511  -8.531  1.00 38.00           C  
ANISOU 2554  CB  ALA A 317     4609   5058   4767     14    327   -423       C  
ATOM   2555  N   ILE A 318     -38.525  39.100  -7.260  1.00 39.79           N  
ANISOU 2555  N   ILE A 318     4874   5247   4994     35    358   -388       N  
ATOM   2556  CA  ILE A 318     -39.460  39.915  -6.491  1.00 41.23           C  
ANISOU 2556  CA  ILE A 318     5080   5395   5189     32    396   -379       C  
ATOM   2557  C   ILE A 318     -40.037  39.131  -5.294  1.00 36.50           C  
ANISOU 2557  C   ILE A 318     4488   4802   4576     20    359   -397       C  
ATOM   2558  O   ILE A 318     -39.982  39.594  -4.122  1.00 40.35           O  
ANISOU 2558  O   ILE A 318     4993   5267   5068     -6    374   -422       O  
ATOM   2559  CB  ILE A 318     -40.543  40.518  -7.395  1.00 37.21           C  
ANISOU 2559  CB  ILE A 318     4573   4881   4684     76    433   -328       C  
ATOM   2560  CG1 ILE A 318     -39.976  41.642  -8.225  1.00 37.67           C  
ANISOU 2560  CG1 ILE A 318     4633   4916   4763     86    494   -306       C  
ATOM   2561  CG2 ILE A 318     -41.700  41.067  -6.596  1.00 37.30           C  
ANISOU 2561  CG2 ILE A 318     4606   4863   4704     78    462   -315       C  
ATOM   2562  CD1 ILE A 318     -40.800  41.928  -9.492  1.00 40.71           C  
ANISOU 2562  CD1 ILE A 318     5009   5320   5136    145    518   -249       C  
ATOM   2563  N   MET A 319     -40.506  37.931  -5.562  1.00 38.84           N  
ANISOU 2563  N   MET A 319     4771   5130   4857     40    313   -388       N  
ATOM   2564  CA  MET A 319     -41.098  37.121  -4.519  1.00 38.55           C  
ANISOU 2564  CA  MET A 319     4740   5096   4812     35    285   -398       C  
ATOM   2565  C   MET A 319     -40.069  36.860  -3.461  1.00 37.34           C  
ANISOU 2565  C   MET A 319     4590   4947   4648      4    267   -434       C  
ATOM   2566  O   MET A 319     -40.347  37.026  -2.319  1.00 37.36           O  
ANISOU 2566  O   MET A 319     4610   4939   4646     -7    273   -446       O  
ATOM   2567  CB  MET A 319     -41.699  35.838  -5.094  1.00 40.81           C  
ANISOU 2567  CB  MET A 319     5004   5410   5092     60    246   -387       C  
ATOM   2568  CG  MET A 319     -42.958  36.121  -5.912  1.00 40.36           C  
ANISOU 2568  CG  MET A 319     4939   5355   5040     93    263   -356       C  
ATOM   2569  SD  MET A 319     -43.821  34.622  -6.349  1.00 41.52           S  
ANISOU 2569  SD  MET A 319     5054   5532   5187    114    221   -359       S  
ATOM   2570  CE  MET A 319     -42.717  33.946  -7.577  1.00 38.80           C  
ANISOU 2570  CE  MET A 319     4682   5226   4833    120    190   -374       C  
ATOM   2571  N   ARG A 320     -38.851  36.488  -3.838  1.00 35.76           N  
ANISOU 2571  N   ARG A 320     4374   4769   4442     -5    244   -453       N  
ATOM   2572  CA  ARG A 320     -37.823  36.290  -2.810  1.00 34.98           C  
ANISOU 2572  CA  ARG A 320     4275   4685   4329    -31    226   -491       C  
ATOM   2573  C   ARG A 320     -37.595  37.549  -1.991  1.00 40.15           C  
ANISOU 2573  C   ARG A 320     4946   5318   4992    -59    265   -518       C  
ATOM   2574  O   ARG A 320     -37.485  37.473  -0.747  1.00 36.71           O  
ANISOU 2574  O   ARG A 320     4517   4892   4538    -72    256   -545       O  
ATOM   2575  CB  ARG A 320     -36.487  35.773  -3.375  1.00 33.38           C  
ANISOU 2575  CB  ARG A 320     4050   4511   4122    -39    199   -508       C  
ATOM   2576  CG  ARG A 320     -36.559  34.472  -4.210  1.00 37.72           C  
ANISOU 2576  CG  ARG A 320     4581   5084   4666    -14    162   -489       C  
ATOM   2577  CD  ARG A 320     -35.197  33.925  -4.779  1.00 34.85           C  
ANISOU 2577  CD  ARG A 320     4194   4747   4297    -20    136   -506       C  
ATOM   2578  NE  ARG A 320     -34.242  33.797  -3.709  1.00 36.27           N  
ANISOU 2578  NE  ARG A 320     4372   4947   4461    -39    120   -537       N  
ATOM   2579  CZ  ARG A 320     -34.219  32.818  -2.835  1.00 37.32           C  
ANISOU 2579  CZ  ARG A 320     4503   5101   4575    -30     92   -538       C  
ATOM   2580  NH1 ARG A 320     -35.129  31.820  -2.901  1.00 39.09           N1+
ANISOU 2580  NH1 ARG A 320     4729   5319   4802     -5     80   -511       N1+
ATOM   2581  NH2 ARG A 320     -33.363  32.900  -1.829  1.00 34.98           N  
ANISOU 2581  NH2 ARG A 320     4203   4830   4257    -43     82   -568       N  
ATOM   2582  N   ASN A 321     -37.519  38.711  -2.657  1.00 39.87           N  
ANISOU 2582  N   ASN A 321     4913   5252   4982    -67    311   -514       N  
ATOM   2583  CA  ASN A 321     -37.243  39.945  -1.879  1.00 39.78           C  
ANISOU 2583  CA  ASN A 321     4914   5213   4987    -99    356   -550       C  
ATOM   2584  C   ASN A 321     -38.393  40.277  -0.956  1.00 41.29           C  
ANISOU 2584  C   ASN A 321     5129   5384   5176    -95    375   -542       C  
ATOM   2585  O   ASN A 321     -38.131  40.608   0.220  1.00 42.19           O  
ANISOU 2585  O   ASN A 321     5249   5501   5281   -120    379   -584       O  
ATOM   2586  CB  ASN A 321     -36.883  41.113  -2.754  1.00 35.51           C  
ANISOU 2586  CB  ASN A 321     4371   4635   4483   -107    413   -545       C  
ATOM   2587  CG  ASN A 321     -35.484  40.999  -3.307  1.00 38.66           C  
ANISOU 2587  CG  ASN A 321     4746   5052   4888   -124    402   -571       C  
ATOM   2588  ND2 ASN A 321     -35.318  41.380  -4.548  1.00 39.04           N  
ANISOU 2588  ND2 ASN A 321     4789   5085   4958   -108    432   -540       N  
ATOM   2589  OD1 ASN A 321     -34.576  40.551  -2.635  1.00 39.50           O  
ANISOU 2589  OD1 ASN A 321     4838   5191   4978   -147    368   -615       O  
ATOM   2590  N   ILE A 322     -39.638  40.095  -1.415  1.00 37.37           N  
ANISOU 2590  N   ILE A 322     4642   4873   4682    -63    381   -494       N  
ATOM   2591  CA  ILE A 322     -40.766  40.268  -0.448  1.00 38.33           C  
ANISOU 2591  CA  ILE A 322     4786   4977   4799    -59    395   -486       C  
ATOM   2592  C   ILE A 322     -40.631  39.332   0.762  1.00 36.58           C  
ANISOU 2592  C   ILE A 322     4565   4788   4546    -63    352   -509       C  
ATOM   2593  O   ILE A 322     -40.840  39.777   1.877  1.00 37.05           O  
ANISOU 2593  O   ILE A 322     4640   4840   4597    -76    367   -532       O  
ATOM   2594  CB  ILE A 322     -42.158  40.057  -1.037  1.00 37.91           C  
ANISOU 2594  CB  ILE A 322     4738   4913   4752    -22    401   -434       C  
ATOM   2595  CG1 ILE A 322     -42.482  41.050  -2.149  1.00 41.48           C  
ANISOU 2595  CG1 ILE A 322     5191   5339   5229     -6    450   -402       C  
ATOM   2596  CG2 ILE A 322     -43.265  40.143   0.048  1.00 40.03           C  
ANISOU 2596  CG2 ILE A 322     5028   5164   5016    -19    413   -428       C  
ATOM   2597  CD1 ILE A 322     -42.337  42.511  -1.828  1.00 48.54           C  
ANISOU 2597  CD1 ILE A 322     6102   6187   6150    -27    516   -415       C  
ATOM   2598  N   GLU A 323     -40.326  38.044   0.565  1.00 35.85           N  
ANISOU 2598  N   GLU A 323     4456   4729   4434    -48    303   -501       N  
ATOM   2599  CA  GLU A 323     -40.220  37.205   1.756  1.00 33.36           C  
ANISOU 2599  CA  GLU A 323     4144   4442   4089    -44    272   -514       C  
ATOM   2600  C   GLU A 323     -39.129  37.621   2.696  1.00 38.28           C  
ANISOU 2600  C   GLU A 323     4762   5090   4690    -70    269   -566       C  
ATOM   2601  O   GLU A 323     -39.287  37.532   3.923  1.00 38.14           O  
ANISOU 2601  O   GLU A 323     4754   5089   4645    -68    265   -581       O  
ATOM   2602  CB  GLU A 323     -39.999  35.732   1.336  1.00 35.68           C  
ANISOU 2602  CB  GLU A 323     4419   4764   4373    -22    228   -495       C  
ATOM   2603  CG  GLU A 323     -41.180  35.176   0.564  1.00 35.31           C  
ANISOU 2603  CG  GLU A 323     4369   4698   4346      2    229   -454       C  
ATOM   2604  CD  GLU A 323     -40.985  33.801  -0.087  1.00 34.98           C  
ANISOU 2604  CD  GLU A 323     4306   4677   4308     19    193   -442       C  
ATOM   2605  OE1 GLU A 323     -40.739  32.798   0.593  1.00 36.17           O  
ANISOU 2605  OE1 GLU A 323     4453   4844   4445     29    173   -442       O  
ATOM   2606  OE2 GLU A 323     -41.204  33.722  -1.310  1.00 37.16           O1-
ANISOU 2606  OE2 GLU A 323     4567   4951   4600     28    191   -430       O1-
ATOM   2607  N   LYS A 324     -37.965  37.983   2.125  1.00 36.11           N  
ANISOU 2607  N   LYS A 324     4469   4826   4423    -91    267   -595       N  
ATOM   2608  CA  LYS A 324     -36.818  38.445   2.903  1.00 40.21           C  
ANISOU 2608  CA  LYS A 324     4975   5375   4926   -120    263   -655       C  
ATOM   2609  C   LYS A 324     -37.100  39.715   3.728  1.00 38.17           C  
ANISOU 2609  C   LYS A 324     4732   5094   4678   -146    308   -693       C  
ATOM   2610  O   LYS A 324     -36.816  39.759   4.907  1.00 42.68           O  
ANISOU 2610  O   LYS A 324     5299   5698   5216   -154    297   -734       O  
ATOM   2611  CB  LYS A 324     -35.652  38.715   1.962  1.00 43.45           C  
ANISOU 2611  CB  LYS A 324     5363   5789   5357   -141    264   -676       C  
ATOM   2612  CG  LYS A 324     -34.959  37.466   1.407  1.00 40.61           C  
ANISOU 2612  CG  LYS A 324     4982   5467   4979   -122    215   -659       C  
ATOM   2613  CD  LYS A 324     -33.739  37.924   0.603  1.00 45.44           C  
ANISOU 2613  CD  LYS A 324     5571   6081   5612   -146    222   -688       C  
ATOM   2614  CE  LYS A 324     -33.255  36.865  -0.338  1.00 46.69           C  
ANISOU 2614  CE  LYS A 324     5712   6260   5766   -127    186   -661       C  
ATOM   2615  NZ  LYS A 324     -31.970  37.280  -0.964  1.00 46.22           N1+
ANISOU 2615  NZ  LYS A 324     5628   6207   5723   -151    192   -692       N1+
ATOM   2616  N   MET A 325     -37.749  40.677   3.124  1.00 37.58           N  
ANISOU 2616  N   MET A 325     4672   4964   4643   -154    358   -676       N  
ATOM   2617  CA  MET A 325     -38.074  41.942   3.781  1.00 41.11           C  
ANISOU 2617  CA  MET A 325     5133   5377   5110   -179    411   -710       C  
ATOM   2618  C   MET A 325     -39.107  41.751   4.910  1.00 41.39           C  
ANISOU 2618  C   MET A 325     5190   5416   5118   -163    408   -700       C  
ATOM   2619  O   MET A 325     -39.009  42.368   5.976  1.00 39.19           O  
ANISOU 2619  O   MET A 325     4915   5144   4828   -183    425   -750       O  
ATOM   2620  CB  MET A 325     -38.699  42.871   2.739  1.00 43.26           C  
ANISOU 2620  CB  MET A 325     5418   5585   5432   -177    469   -673       C  
ATOM   2621  CG  MET A 325     -37.695  43.385   1.716  1.00 48.70           C  
ANISOU 2621  CG  MET A 325     6088   6259   6156   -195    492   -685       C  
ATOM   2622  SD  MET A 325     -38.454  44.318   0.333  1.00 62.19           S  
ANISOU 2622  SD  MET A 325     7811   7902   7915   -174    562   -622       S  
ATOM   2623  CE  MET A 325     -39.083  45.675   1.287  1.00 66.36           C  
ANISOU 2623  CE  MET A 325     8361   8377   8473   -198    633   -651       C  
ATOM   2624  N   LEU A 326     -40.092  40.903   4.648  1.00 40.47           N  
ANISOU 2624  N   LEU A 326     5086   5295   4993   -126    389   -640       N  
ATOM   2625  CA  LEU A 326     -41.071  40.541   5.672  1.00 42.53           C  
ANISOU 2625  CA  LEU A 326     5368   5562   5230   -106    385   -624       C  
ATOM   2626  C   LEU A 326     -40.436  39.867   6.863  1.00 42.42           C  
ANISOU 2626  C   LEU A 326     5345   5606   5164   -101    347   -657       C  
ATOM   2627  O   LEU A 326     -40.753  40.183   8.008  1.00 40.00           O  
ANISOU 2627  O   LEU A 326     5051   5311   4834   -102    358   -680       O  
ATOM   2628  CB  LEU A 326     -42.226  39.700   5.107  1.00 42.45           C  
ANISOU 2628  CB  LEU A 326     5365   5533   5227    -70    374   -556       C  
ATOM   2629  CG  LEU A 326     -43.172  40.459   4.168  1.00 48.71           C  
ANISOU 2629  CG  LEU A 326     6170   6276   6062    -64    417   -520       C  
ATOM   2630  CD1 LEU A 326     -44.281  39.594   3.594  1.00 47.40           C  
ANISOU 2630  CD1 LEU A 326     6003   6103   5902    -29    402   -465       C  
ATOM   2631  CD2 LEU A 326     -43.813  41.638   4.888  1.00 53.48           C  
ANISOU 2631  CD2 LEU A 326     6797   6843   6679    -77    469   -533       C  
ATOM   2632  N   GLY A 327     -39.565  38.917   6.605  1.00 42.77           N  
ANISOU 2632  N   GLY A 327     5368   5694   5188    -92    303   -656       N  
ATOM   2633  CA  GLY A 327     -38.820  38.249   7.685  1.00 46.67           C  
ANISOU 2633  CA  GLY A 327     5848   6254   5628    -80    266   -685       C  
ATOM   2634  C   GLY A 327     -38.013  39.202   8.592  1.00 47.23           C  
ANISOU 2634  C   GLY A 327     5908   6359   5678   -111    276   -764       C  
ATOM   2635  O   GLY A 327     -38.082  39.155   9.814  1.00 46.53           O  
ANISOU 2635  O   GLY A 327     5821   6311   5544    -99    269   -787       O  
ATOM   2636  N   GLU A 328     -37.305  40.092   7.954  1.00 46.57           N  
ANISOU 2636  N   GLU A 328     5808   6255   5628   -151    296   -805       N  
ATOM   2637  CA  GLU A 328     -36.634  41.181   8.622  1.00 54.96           C  
ANISOU 2637  CA  GLU A 328     6856   7333   6691   -190    318   -888       C  
ATOM   2638  C   GLU A 328     -37.516  42.170   9.344  1.00 48.53           C  
ANISOU 2638  C   GLU A 328     6065   6484   5887   -203    365   -909       C  
ATOM   2639  O   GLU A 328     -37.290  42.396  10.541  1.00 44.41           O  
ANISOU 2639  O   GLU A 328     5536   6010   5326   -209    360   -965       O  
ATOM   2640  CB  GLU A 328     -35.760  41.953   7.655  1.00 62.03           C  
ANISOU 2640  CB  GLU A 328     7731   8200   7637   -231    343   -923       C  
ATOM   2641  CG  GLU A 328     -34.372  42.002   8.245  1.00 80.28           C  
ANISOU 2641  CG  GLU A 328    10002  10580   9919   -254    315  -1004       C  
ATOM   2642  CD  GLU A 328     -33.572  43.082   7.631  1.00 92.51           C  
ANISOU 2642  CD  GLU A 328    11529  12094  11525   -304    357  -1060       C  
ATOM   2643  OE1 GLU A 328     -33.384  42.973   6.390  1.00 92.91           O  
ANISOU 2643  OE1 GLU A 328    11580  12107  11614   -304    365  -1018       O  
ATOM   2644  OE2 GLU A 328     -33.171  44.011   8.389  1.00 93.87           O1-
ANISOU 2644  OE2 GLU A 328    11684  12278  11704   -342    383  -1145       O1-
ATOM   2645  N   ALA A 329     -38.559  42.693   8.674  1.00 44.92           N  
ANISOU 2645  N   ALA A 329     5636   5952   5479   -203    410   -861       N  
ATOM   2646  CA  ALA A 329     -39.439  43.640   9.350  1.00 42.65           C  
ANISOU 2646  CA  ALA A 329     5372   5626   5205   -214    459   -877       C  
ATOM   2647  C   ALA A 329     -40.222  43.033  10.496  1.00 43.53           C  
ANISOU 2647  C   ALA A 329     5503   5771   5266   -180    439   -858       C  
ATOM   2648  O   ALA A 329     -40.442  43.677  11.484  1.00 49.47           O  
ANISOU 2648  O   ALA A 329     6262   6530   6003   -192    462   -903       O  
ATOM   2649  CB  ALA A 329     -40.342  44.340   8.367  1.00 44.11           C  
ANISOU 2649  CB  ALA A 329     5579   5728   5451   -215    514   -827       C  
ATOM   2650  N   LEU A 330     -40.666  41.783  10.397  1.00 44.20           N  
ANISOU 2650  N   LEU A 330     5595   5875   5324   -137    401   -793       N  
ATOM   2651  CA  LEU A 330     -41.473  41.201  11.464  1.00 44.40           C  
ANISOU 2651  CA  LEU A 330     5639   5923   5306   -101    391   -768       C  
ATOM   2652  C   LEU A 330     -40.595  40.709  12.619  1.00 48.59           C  
ANISOU 2652  C   LEU A 330     6150   6543   5767    -87    353   -813       C  
ATOM   2653  O   LEU A 330     -41.074  40.361  13.711  1.00 53.53           O  
ANISOU 2653  O   LEU A 330     6789   7202   6347    -56    348   -805       O  
ATOM   2654  CB  LEU A 330     -42.312  40.028  10.952  1.00 46.50           C  
ANISOU 2654  CB  LEU A 330     5917   6171   5578    -60    373   -683       C  
ATOM   2655  CG  LEU A 330     -43.344  40.490   9.945  1.00 47.28           C  
ANISOU 2655  CG  LEU A 330     6032   6195   5735    -64    409   -638       C  
ATOM   2656  CD1 LEU A 330     -43.872  39.245   9.293  1.00 46.16           C  
ANISOU 2656  CD1 LEU A 330     5888   6048   5601    -30    383   -572       C  
ATOM   2657  CD2 LEU A 330     -44.443  41.341  10.605  1.00 46.64           C  
ANISOU 2657  CD2 LEU A 330     5979   6075   5665    -66    456   -636       C  
ATOM   2658  N   GLY A 331     -39.307  40.659  12.358  1.00 49.44           N  
ANISOU 2658  N   GLY A 331     6225   6693   5865   -106    325   -859       N  
ATOM   2659  CA  GLY A 331     -38.364  40.282  13.370  1.00 53.30           C  
ANISOU 2659  CA  GLY A 331     6688   7276   6287    -92    288   -908       C  
ATOM   2660  C   GLY A 331     -38.319  38.794  13.526  1.00 52.55           C  
ANISOU 2660  C   GLY A 331     6592   7226   6149    -37    246   -846       C  
ATOM   2661  O   GLY A 331     -37.628  38.305  14.374  1.00 54.01           O  
ANISOU 2661  O   GLY A 331     6756   7493   6269    -11    214   -869       O  
ATOM   2662  N   ASN A 332     -39.044  38.038  12.734  1.00 50.66           N  
ANISOU 2662  N   ASN A 332     6371   6935   5943    -15    248   -767       N  
ATOM   2663  CA  ASN A 332     -38.988  36.599  12.902  1.00 51.83           C  
ANISOU 2663  CA  ASN A 332     6515   7120   6058     35    216   -711       C  
ATOM   2664  C   ASN A 332     -39.559  35.884  11.688  1.00 51.28           C  
ANISOU 2664  C   ASN A 332     6454   6986   6042     43    218   -643       C  
ATOM   2665  O   ASN A 332     -40.656  36.152  11.302  1.00 47.65           O  
ANISOU 2665  O   ASN A 332     6019   6464   5621     40    248   -609       O  
ATOM   2666  CB  ASN A 332     -39.676  36.239  14.218  1.00 57.83           C  
ANISOU 2666  CB  ASN A 332     7294   7910   6768     80    224   -688       C  
ATOM   2667  CG  ASN A 332     -40.277  34.863  14.240  1.00 61.60           C  
ANISOU 2667  CG  ASN A 332     7784   8373   7247    132    222   -604       C  
ATOM   2668  ND2 ASN A 332     -41.480  34.783  14.713  1.00 70.05           N  
ANISOU 2668  ND2 ASN A 332     8883   9404   8326    150    253   -565       N  
ATOM   2669  OD1 ASN A 332     -39.674  33.896  13.827  1.00 65.21           O  
ANISOU 2669  OD1 ASN A 332     8225   8849   7702    154    197   -574       O  
ATOM   2670  N   PRO A 333     -38.815  34.967  11.101  1.00 48.46           N  
ANISOU 2670  N   PRO A 333     6076   6650   5684     56    188   -624       N  
ATOM   2671  CA  PRO A 333     -39.253  34.440   9.833  1.00 51.57           C  
ANISOU 2671  CA  PRO A 333     6473   6988   6132     54    189   -578       C  
ATOM   2672  C   PRO A 333     -40.535  33.673   9.913  1.00 46.33           C  
ANISOU 2672  C   PRO A 333     5829   6284   5487     86    207   -514       C  
ATOM   2673  O   PRO A 333     -41.254  33.561   8.921  1.00 42.64           O  
ANISOU 2673  O   PRO A 333     5366   5763   5069     79    218   -485       O  
ATOM   2674  CB  PRO A 333     -38.080  33.547   9.387  1.00 49.11           C  
ANISOU 2674  CB  PRO A 333     6133   6719   5807     65    152   -577       C  
ATOM   2675  CG  PRO A 333     -37.365  33.234  10.654  1.00 51.01           C  
ANISOU 2675  CG  PRO A 333     6362   7038   5980     93    133   -597       C  
ATOM   2676  CD  PRO A 333     -37.512  34.449  11.491  1.00 44.27           C  
ANISOU 2676  CD  PRO A 333     5517   6199   5105     70    151   -651       C  
ATOM   2677  N   GLN A 334     -40.854  33.162  11.078  1.00 53.02           N  
ANISOU 2677  N   GLN A 334     6688   7160   6296    124    212   -494       N  
ATOM   2678  CA  GLN A 334     -42.061  32.327  11.197  1.00 56.64           C  
ANISOU 2678  CA  GLN A 334     7163   7576   6778    157    234   -433       C  
ATOM   2679  C   GLN A 334     -43.360  33.057  11.168  1.00 49.55           C  
ANISOU 2679  C   GLN A 334     6289   6622   5914    143    269   -423       C  
ATOM   2680  O   GLN A 334     -44.403  32.445  10.952  1.00 51.27           O  
ANISOU 2680  O   GLN A 334     6515   6796   6167    160    288   -378       O  
ATOM   2681  CB  GLN A 334     -41.945  31.427  12.419  1.00 69.03           C  
ANISOU 2681  CB  GLN A 334     8736   9193   8298    211    235   -404       C  
ATOM   2682  CG  GLN A 334     -40.703  30.552  12.231  1.00 82.87           C  
ANISOU 2682  CG  GLN A 334    10462  10995  10026    230    203   -402       C  
ATOM   2683  CD  GLN A 334     -40.690  29.258  13.001  1.00 88.59           C  
ANISOU 2683  CD  GLN A 334    11187  11747  10723    293    210   -348       C  
ATOM   2684  NE2 GLN A 334     -41.490  29.202  14.064  1.00 88.79           N  
ANISOU 2684  NE2 GLN A 334    11192  11791  10753    310    192   -331       N  
ATOM   2685  OE1 GLN A 334     -39.994  28.314  12.643  1.00 94.30           O  
ANISOU 2685  OE1 GLN A 334    11930  12475  11424    328    236   -320       O  
ATOM   2686  N   GLU A 335     -43.310  34.360  11.347  1.00 46.62           N  
ANISOU 2686  N   GLU A 335     5927   6250   5537    111    280   -468       N  
ATOM   2687  CA  GLU A 335     -44.474  35.197  11.138  1.00 49.51           C  
ANISOU 2687  CA  GLU A 335     6313   6558   5939     94    316   -460       C  
ATOM   2688  C   GLU A 335     -44.754  35.572   9.676  1.00 43.03           C  
ANISOU 2688  C   GLU A 335     5485   5689   5175     67    321   -452       C  
ATOM   2689  O   GLU A 335     -45.761  36.181   9.392  1.00 40.02           O  
ANISOU 2689  O   GLU A 335     5116   5262   4825     60    351   -438       O  
ATOM   2690  CB  GLU A 335     -44.325  36.490  11.904  1.00 52.90           C  
ANISOU 2690  CB  GLU A 335     6753   6999   6345     70    335   -511       C  
ATOM   2691  CG  GLU A 335     -44.650  36.341  13.386  1.00 61.37           C  
ANISOU 2691  CG  GLU A 335     7842   8106   7368    101    344   -510       C  
ATOM   2692  CD  GLU A 335     -44.672  37.695  13.991  1.00 68.29           C  
ANISOU 2692  CD  GLU A 335     8730   8984   8233     71    369   -566       C  
ATOM   2693  OE1 GLU A 335     -43.720  37.983  14.725  1.00 73.05           O  
ANISOU 2693  OE1 GLU A 335     9319   9649   8787     66    352   -621       O  
ATOM   2694  OE2 GLU A 335     -45.583  38.492  13.631  1.00 79.02           O1-
ANISOU 2694  OE2 GLU A 335    10106  10282   9635     52    405   -558       O1-
ATOM   2695  N   VAL A 336     -43.900  35.165   8.749  1.00 39.75           N  
ANISOU 2695  N   VAL A 336     5046   5286   4769     59    294   -458       N  
ATOM   2696  CA  VAL A 336     -44.052  35.632   7.384  1.00 34.65           C  
ANISOU 2696  CA  VAL A 336     4392   4606   4167     38    300   -455       C  
ATOM   2697  C   VAL A 336     -45.354  35.087   6.768  1.00 35.24           C  
ANISOU 2697  C   VAL A 336     4468   4641   4280     57    312   -408       C  
ATOM   2698  O   VAL A 336     -46.138  35.810   6.175  1.00 35.69           O  
ANISOU 2698  O   VAL A 336     4530   4664   4365     49    336   -398       O  
ATOM   2699  CB  VAL A 336     -42.845  35.263   6.543  1.00 39.83           C  
ANISOU 2699  CB  VAL A 336     5023   5288   4822     27    268   -471       C  
ATOM   2700  CG1 VAL A 336     -43.159  35.456   5.059  1.00 41.21           C  
ANISOU 2700  CG1 VAL A 336     5187   5430   5038     19    273   -454       C  
ATOM   2701  CG2 VAL A 336     -41.678  36.146   6.952  1.00 40.79           C  
ANISOU 2701  CG2 VAL A 336     5138   5439   4918      0    266   -526       C  
ATOM   2702  N   GLY A 337     -45.610  33.832   6.984  1.00 35.98           N  
ANISOU 2702  N   GLY A 337     4555   4740   4374     83    299   -380       N  
ATOM   2703  CA  GLY A 337     -46.774  33.207   6.421  1.00 39.64           C  
ANISOU 2703  CA  GLY A 337     5012   5171   4878     98    309   -346       C  
ATOM   2704  C   GLY A 337     -48.087  33.758   6.934  1.00 40.59           C  
ANISOU 2704  C   GLY A 337     5152   5257   5012    104    345   -328       C  
ATOM   2705  O   GLY A 337     -49.012  34.004   6.123  1.00 36.31           O  
ANISOU 2705  O   GLY A 337     4603   4688   4505    102    357   -315       O  
ATOM   2706  N   PRO A 338     -48.200  33.886   8.295  1.00 41.86           N  
ANISOU 2706  N   PRO A 338     5336   5425   5143    115    360   -328       N  
ATOM   2707  CA  PRO A 338     -49.456  34.457   8.849  1.00 40.82           C  
ANISOU 2707  CA  PRO A 338     5225   5259   5023    120    397   -311       C  
ATOM   2708  C   PRO A 338     -49.746  35.846   8.292  1.00 39.68           C  
ANISOU 2708  C   PRO A 338     5089   5094   4894     96    417   -326       C  
ATOM   2709  O   PRO A 338     -50.860  36.118   7.874  1.00 38.31           O  
ANISOU 2709  O   PRO A 338     4915   4887   4751    101    439   -304       O  
ATOM   2710  CB  PRO A 338     -49.201  34.504  10.367  1.00 40.19           C  
ANISOU 2710  CB  PRO A 338     5168   5205   4897    135    406   -318       C  
ATOM   2711  CG  PRO A 338     -48.318  33.244  10.582  1.00 45.90           C  
ANISOU 2711  CG  PRO A 338     5875   5965   5597    157    378   -309       C  
ATOM   2712  CD  PRO A 338     -47.420  33.167   9.333  1.00 41.59           C  
ANISOU 2712  CD  PRO A 338     5305   5430   5066    135    346   -329       C  
ATOM   2713  N   LEU A 339     -48.740  36.677   8.220  1.00 38.28           N  
ANISOU 2713  N   LEU A 339     4913   4933   4696     72    412   -363       N  
ATOM   2714  CA  LEU A 339     -48.911  37.958   7.595  1.00 37.30           C  
ANISOU 2714  CA  LEU A 339     4795   4783   4593     51    439   -374       C  
ATOM   2715  C   LEU A 339     -49.330  37.867   6.152  1.00 38.50           C  
ANISOU 2715  C   LEU A 339     4927   4920   4781     56    436   -349       C  
ATOM   2716  O   LEU A 339     -50.233  38.527   5.744  1.00 37.96           O  
ANISOU 2716  O   LEU A 339     4863   4821   4736     62    465   -328       O  
ATOM   2717  CB  LEU A 339     -47.661  38.780   7.690  1.00 41.36           C  
ANISOU 2717  CB  LEU A 339     5308   5316   5090     22    437   -422       C  
ATOM   2718  CG  LEU A 339     -48.034  40.206   7.385  1.00 46.70           C  
ANISOU 2718  CG  LEU A 339     5997   5952   5793      4    484   -429       C  
ATOM   2719  CD1 LEU A 339     -47.518  41.177   8.394  1.00 53.24           C  
ANISOU 2719  CD1 LEU A 339     6841   6782   6606    -21    510   -478       C  
ATOM   2720  CD2 LEU A 339     -47.584  40.564   6.008  1.00 53.12           C  
ANISOU 2720  CD2 LEU A 339     6793   6760   6630     -5    482   -428       C  
ATOM   2721  N   LEU A 340     -48.664  37.046   5.369  1.00 37.36           N  
ANISOU 2721  N   LEU A 340     4758   4799   4638     59    400   -350       N  
ATOM   2722  CA  LEU A 340     -49.060  36.947   3.934  1.00 37.45           C  
ANISOU 2722  CA  LEU A 340     4746   4805   4676     68    395   -330       C  
ATOM   2723  C   LEU A 340     -50.509  36.470   3.810  1.00 38.94           C  
ANISOU 2723  C   LEU A 340     4928   4977   4890     90    405   -300       C  
ATOM   2724  O   LEU A 340     -51.267  36.920   2.938  1.00 35.50           O  
ANISOU 2724  O   LEU A 340     4481   4533   4474    101    419   -282       O  
ATOM   2725  CB  LEU A 340     -48.144  36.053   3.166  1.00 34.46           C  
ANISOU 2725  CB  LEU A 340     4341   4455   4294     67    355   -340       C  
ATOM   2726  CG  LEU A 340     -46.746  36.615   2.876  1.00 37.63           C  
ANISOU 2726  CG  LEU A 340     4742   4875   4680     45    347   -369       C  
ATOM   2727  CD1 LEU A 340     -45.863  35.467   2.351  1.00 41.81           C  
ANISOU 2727  CD1 LEU A 340     5247   5435   5203     48    305   -376       C  
ATOM   2728  CD2 LEU A 340     -46.791  37.773   1.850  1.00 36.73           C  
ANISOU 2728  CD2 LEU A 340     4626   4745   4583     41    374   -363       C  
ATOM   2729  N   ASN A 341     -50.886  35.526   4.653  1.00 38.53           N  
ANISOU 2729  N   ASN A 341     4878   4922   4838    101    399   -292       N  
ATOM   2730  CA  ASN A 341     -52.241  35.007   4.555  1.00 41.25           C  
ANISOU 2730  CA  ASN A 341     5211   5247   5212    119    411   -268       C  
ATOM   2731  C   ASN A 341     -53.276  36.061   4.893  1.00 36.66           C  
ANISOU 2731  C   ASN A 341     4649   4640   4639    123    450   -252       C  
ATOM   2732  O   ASN A 341     -54.285  36.174   4.257  1.00 35.49           O  
ANISOU 2732  O   ASN A 341     4484   4483   4515    136    461   -236       O  
ATOM   2733  CB  ASN A 341     -52.376  33.775   5.501  1.00 43.01           C  
ANISOU 2733  CB  ASN A 341     5435   5466   5439    131    408   -260       C  
ATOM   2734  CG  ASN A 341     -51.877  32.501   4.863  1.00 44.37           C  
ANISOU 2734  CG  ASN A 341     5576   5654   5625    135    378   -266       C  
ATOM   2735  ND2 ASN A 341     -50.835  31.945   5.406  1.00 46.84           N  
ANISOU 2735  ND2 ASN A 341     5896   5985   5914    135    363   -272       N  
ATOM   2736  OD1 ASN A 341     -52.446  32.017   3.902  1.00 57.54           O  
ANISOU 2736  OD1 ASN A 341     7214   7321   7326    139    371   -266       O  
ATOM   2737  N   THR A 342     -53.047  36.787   5.976  1.00 37.36           N  
ANISOU 2737  N   THR A 342     4771   4717   4705    114    472   -260       N  
ATOM   2738  CA  THR A 342     -53.882  37.916   6.329  1.00 38.56           C  
ANISOU 2738  CA  THR A 342     4945   4841   4864    115    513   -249       C  
ATOM   2739  C   THR A 342     -53.977  38.935   5.219  1.00 36.32           C  
ANISOU 2739  C   THR A 342     4653   4551   4594    114    529   -243       C  
ATOM   2740  O   THR A 342     -55.046  39.416   4.920  1.00 37.16           O  
ANISOU 2740  O   THR A 342     4758   4640   4720    129    556   -218       O  
ATOM   2741  CB  THR A 342     -53.298  38.596   7.543  1.00 45.53           C  
ANISOU 2741  CB  THR A 342     5859   5721   5716     99    530   -272       C  
ATOM   2742  CG2 THR A 342     -54.074  39.824   7.900  1.00 44.57           C  
ANISOU 2742  CG2 THR A 342     5761   5566   5604     97    578   -266       C  
ATOM   2743  OG1 THR A 342     -53.301  37.667   8.637  1.00 44.08           O  
ANISOU 2743  OG1 THR A 342     5684   5549   5514    111    520   -270       O  
ATOM   2744  N   MET A 343     -52.866  39.202   4.565  1.00 39.08           N  
ANISOU 2744  N   MET A 343     4996   4917   4934    100    516   -261       N  
ATOM   2745  CA  MET A 343     -52.869  40.020   3.377  1.00 37.76           C  
ANISOU 2745  CA  MET A 343     4817   4747   4779    107    533   -248       C  
ATOM   2746  C   MET A 343     -53.826  39.502   2.347  1.00 33.54           C  
ANISOU 2746  C   MET A 343     4251   4229   4261    135    519   -222       C  
ATOM   2747  O   MET A 343     -54.530  40.285   1.776  1.00 31.27           O  
ANISOU 2747  O   MET A 343     3960   3934   3984    155    550   -196       O  
ATOM   2748  CB  MET A 343     -51.509  40.100   2.718  1.00 37.95           C  
ANISOU 2748  CB  MET A 343     4833   4791   4795     92    516   -269       C  
ATOM   2749  CG  MET A 343     -50.593  41.195   3.187  1.00 51.11           C  
ANISOU 2749  CG  MET A 343     6520   6434   6464     71    557   -285       C  
ATOM   2750  SD  MET A 343     -49.194  41.521   2.124  1.00 46.39           S  
ANISOU 2750  SD  MET A 343     5909   5853   5865     54    547   -308       S  
ATOM   2751  CE  MET A 343     -49.933  42.753   1.167  1.00 50.61           C  
ANISOU 2751  CE  MET A 343     6439   6420   6371     36    493   -343       C  
ATOM   2752  N   ILE A 344     -53.851  38.197   2.090  1.00 34.72           N  
ANISOU 2752  N   ILE A 344     4374   4402   4413    140    479   -228       N  
ATOM   2753  CA  ILE A 344     -54.617  37.809   0.896  1.00 36.95           C  
ANISOU 2753  CA  ILE A 344     4618   4710   4711    166    465   -215       C  
ATOM   2754  C   ILE A 344     -56.045  37.371   1.106  1.00 34.59           C  
ANISOU 2754  C   ILE A 344     4304   4404   4435    183    474   -201       C  
ATOM   2755  O   ILE A 344     -56.874  37.483   0.199  1.00 39.44           O  
ANISOU 2755  O   ILE A 344     4888   5040   5058    208    475   -188       O  
ATOM   2756  CB  ILE A 344     -53.885  36.778  -0.082  1.00 45.00           C  
ANISOU 2756  CB  ILE A 344     5602   5768   5727    165    419   -234       C  
ATOM   2757  CG1 ILE A 344     -54.071  35.336   0.340  1.00 54.00           C  
ANISOU 2757  CG1 ILE A 344     6724   6908   6882    160    394   -250       C  
ATOM   2758  CG2 ILE A 344     -52.445  37.141  -0.285  1.00 46.28           C  
ANISOU 2758  CG2 ILE A 344     5778   5938   5869    148    410   -249       C  
ATOM   2759  CD1 ILE A 344     -53.708  34.356  -0.769  1.00 66.81           C  
ANISOU 2759  CD1 ILE A 344     8305   8567   8511    165    356   -270       C  
ATOM   2760  N   LYS A 345     -56.323  36.738   2.249  1.00 38.11           N  
ANISOU 2760  N   LYS A 345     4764   4827   4890    173    477   -205       N  
ATOM   2761  CA  LYS A 345     -57.615  36.076   2.413  1.00 39.55           C  
ANISOU 2761  CA  LYS A 345     4924   5000   5101    187    484   -196       C  
ATOM   2762  C   LYS A 345     -58.720  37.041   2.367  1.00 38.09           C  
ANISOU 2762  C   LYS A 345     4743   4804   4924    205    518   -172       C  
ATOM   2763  O   LYS A 345     -58.762  38.003   3.138  1.00 36.89           O  
ANISOU 2763  O   LYS A 345     4630   4623   4762    201    552   -158       O  
ATOM   2764  CB  LYS A 345     -57.715  35.385   3.774  1.00 42.07           C  
ANISOU 2764  CB  LYS A 345     5265   5289   5428    179    494   -196       C  
ATOM   2765  CG  LYS A 345     -57.050  34.041   3.717  1.00 45.59           C  
ANISOU 2765  CG  LYS A 345     5692   5746   5882    172    464   -214       C  
ATOM   2766  CD  LYS A 345     -56.417  33.625   5.011  1.00 55.17           C  
ANISOU 2766  CD  LYS A 345     6937   6944   7079    166    470   -212       C  
ATOM   2767  CE  LYS A 345     -57.433  33.123   5.980  1.00 61.64           C  
ANISOU 2767  CE  LYS A 345     7764   7732   7923    177    500   -193       C  
ATOM   2768  NZ  LYS A 345     -56.662  32.125   6.789  1.00 75.20           N1+
ANISOU 2768  NZ  LYS A 345     9492   9448   9631    180    495   -192       N1+
ATOM   2769  N   GLY A 346     -59.640  36.779   1.465  1.00 34.72           N  
ANISOU 2769  N   GLY A 346     4273   4402   4515    226    510   -169       N  
ATOM   2770  CA  GLY A 346     -60.825  37.590   1.314  1.00 33.86           C  
ANISOU 2770  CA  GLY A 346     4159   4291   4414    250    541   -143       C  
ATOM   2771  C   GLY A 346     -60.478  38.906   0.572  1.00 37.63           C  
ANISOU 2771  C   GLY A 346     4648   4781   4866    267    560   -121       C  
ATOM   2772  O   GLY A 346     -61.312  39.746   0.474  1.00 36.15           O  
ANISOU 2772  O   GLY A 346     4462   4589   4681    291    593    -93       O  
ATOM   2773  N   ARG A 347     -59.246  39.090   0.081  1.00 34.81           N  
ANISOU 2773  N   ARG A 347     4299   4437   4488    257    545   -130       N  
ATOM   2774  CA  ARG A 347     -58.858  40.348  -0.474  1.00 36.94           C  
ANISOU 2774  CA  ARG A 347     4584   4707   4742    272    575   -107       C  
ATOM   2775  C   ARG A 347     -58.268  40.145  -1.858  1.00 39.17           C  
ANISOU 2775  C   ARG A 347     4834   5041   5008    289    546   -111       C  
ATOM   2776  O   ARG A 347     -58.529  40.918  -2.765  1.00 38.61           O  
ANISOU 2776  O   ARG A 347     4750   4994   4925    325    566    -82       O  
ATOM   2777  CB  ARG A 347     -57.792  41.014   0.418  1.00 38.94           C  
ANISOU 2777  CB  ARG A 347     4887   4918   4988    238    598   -117       C  
ATOM   2778  CG  ARG A 347     -58.296  41.377   1.834  1.00 36.96           C  
ANISOU 2778  CG  ARG A 347     4674   4621   4748    223    631   -115       C  
ATOM   2779  CD  ARG A 347     -57.260  42.155   2.602  1.00 35.47           C  
ANISOU 2779  CD  ARG A 347     4527   4401   4550    192    655   -133       C  
ATOM   2780  NE  ARG A 347     -56.983  43.483   2.058  1.00 37.12           N  
ANISOU 2780  NE  ARG A 347     4748   4592   4763    200    701   -116       N  
ATOM   2781  CZ  ARG A 347     -55.780  43.972   1.701  1.00 35.37           C  
ANISOU 2781  CZ  ARG A 347     4534   4368   4536    182    707   -132       C  
ATOM   2782  NH1 ARG A 347     -54.680  43.272   1.879  1.00 35.53           N1+
ANISOU 2782  NH1 ARG A 347     4550   4405   4541    155    666   -169       N1+
ATOM   2783  NH2 ARG A 347     -55.677  45.244   1.238  1.00 37.25           N  
ANISOU 2783  NH2 ARG A 347     4783   4580   4787    193    764   -111       N  
ATOM   2784  N   TYR A 348     -57.429  39.139  -2.020  1.00 38.69           N  
ANISOU 2784  N   TYR A 348     4759   4998   4943    268    502   -144       N  
ATOM   2785  CA  TYR A 348     -56.872  38.829  -3.320  1.00 38.59           C  
ANISOU 2785  CA  TYR A 348     4712   5036   4913    284    472   -152       C  
ATOM   2786  C   TYR A 348     -57.062  37.344  -3.783  1.00 40.85           C  
ANISOU 2786  C   TYR A 348     4951   5361   5208    282    421   -188       C  
ATOM   2787  O   TYR A 348     -56.533  36.991  -4.812  1.00 39.64           O  
ANISOU 2787  O   TYR A 348     4769   5252   5040    292    393   -202       O  
ATOM   2788  CB  TYR A 348     -55.353  39.140  -3.330  1.00 37.97           C  
ANISOU 2788  CB  TYR A 348     4661   4945   4820    260    471   -161       C  
ATOM   2789  CG  TYR A 348     -54.944  40.611  -3.193  1.00 40.83           C  
ANISOU 2789  CG  TYR A 348     5060   5273   5179    262    524   -135       C  
ATOM   2790  CD1 TYR A 348     -54.884  41.424  -4.293  1.00 39.44           C  
ANISOU 2790  CD1 TYR A 348     4874   5120   4992    297    549   -104       C  
ATOM   2791  CD2 TYR A 348     -54.548  41.167  -1.954  1.00 39.01           C  
ANISOU 2791  CD2 TYR A 348     4873   4990   4958    228    553   -143       C  
ATOM   2792  CE1 TYR A 348     -54.469  42.741  -4.186  1.00 41.73           C  
ANISOU 2792  CE1 TYR A 348     5196   5370   5288    297    607    -80       C  
ATOM   2793  CE2 TYR A 348     -54.107  42.490  -1.866  1.00 37.72           C  
ANISOU 2793  CE2 TYR A 348     4739   4791   4799    224    606   -129       C  
ATOM   2794  CZ  TYR A 348     -54.117  43.273  -2.987  1.00 39.23           C  
ANISOU 2794  CZ  TYR A 348     4920   4997   4988    259    636    -95       C  
ATOM   2795  OH  TYR A 348     -53.691  44.573  -2.992  1.00 37.93           O  
ANISOU 2795  OH  TYR A 348     4781   4792   4837    257    699    -77       O  
ATOM   2796  N   ASN A 349     -57.762  36.491  -3.049  1.00 42.06           N  
ANISOU 2796  N   ASN A 349     5095   5496   5388    268    414   -205       N  
ATOM   2797  CA  ASN A 349     -57.892  35.050  -3.471  1.00 49.41           C  
ANISOU 2797  CA  ASN A 349     5979   6455   6339    261    374   -245       C  
ATOM   2798  C   ASN A 349     -59.294  34.574  -3.842  1.00 46.24           C  
ANISOU 2798  C   ASN A 349     5526   6079   5961    281    371   -259       C  
ATOM   2799  O   ASN A 349     -60.230  35.324  -3.580  1.00 55.03           O  
ANISOU 2799  O   ASN A 349     6646   7184   7076    299    400   -232       O  
ATOM   2800  CB  ASN A 349     -57.357  34.158  -2.392  1.00 41.11           C  
ANISOU 2800  CB  ASN A 349     4950   5360   5308    227    369   -262       C  
ATOM   2801  CG  ASN A 349     -58.168  34.208  -1.136  1.00 41.41           C  
ANISOU 2801  CG  ASN A 349     5013   5351   5368    220    400   -247       C  
ATOM   2802  ND2 ASN A 349     -57.733  33.409  -0.203  1.00 50.57           N  
ANISOU 2802  ND2 ASN A 349     6191   6479   6541    199    399   -256       N  
ATOM   2803  OD1 ASN A 349     -59.149  34.978  -0.959  1.00 41.76           O  
ANISOU 2803  OD1 ASN A 349     5062   5387   5415    237    428   -224       O  
TER   
END



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