CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 181212110356139184

Job options:

ID        	=	 181212110356139184
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:


HETATM    1  C   ACE B   0      18.142  -9.447  -5.158  1.00 87.92           C  
ANISOU    1  C   ACE B   0    10301  12059  11044  -1684   1207    778       C  
HETATM    2  O   ACE B   0      18.469  -9.137  -4.066  1.00 92.61           O  
ANISOU    2  O   ACE B   0    10948  12792  11448  -1545   1306    888       O  
HETATM    3  CH3 ACE B   0      16.771 -10.072  -5.365  1.00 91.56           C  
ANISOU    3  CH3 ACE B   0    10519  12624  11646  -2030   1306    797       C  
ATOM      4  N   MET B   1      19.047  -9.222  -6.269  1.00 83.20           N  
ANISOU    4  N   MET B   1     9858  11225  10528  -1538   1000    620       N  
ATOM      5  CA  MET B   1      20.355  -8.623  -6.007  1.00 77.86           C  
ANISOU    5  CA  MET B   1     9370  10482   9733  -1243    924    606       C  
ATOM      6  C   MET B   1      20.302  -7.105  -6.052  1.00 72.88           C  
ANISOU    6  C   MET B   1     8589  10097   9007  -1003    862    424       C  
ATOM      7  O   MET B   1      19.729  -6.538  -7.015  1.00 79.09           O  
ANISOU    7  O   MET B   1     9227  10945   9881   -994    768    256       O  
ATOM      8  CB  MET B   1      21.404  -9.069  -7.027  1.00 77.53           C  
ANISOU    8  CB  MET B   1     9550  10101   9807  -1193    782    542       C  
ATOM      9  CG  MET B   1      21.431 -10.579  -7.223  1.00 84.73           C  
ANISOU    9  CG  MET B   1    10638  10697  10858  -1418    825    672       C  
ATOM     10  SD  MET B   1      22.002 -11.301  -5.663  1.00 89.46           S  
ANISOU   10  SD  MET B   1    11427  11240  11325  -1377    966    994       S  
ATOM     11  CE  MET B   1      20.944 -12.709  -5.243  1.00 93.24           C  
ANISOU   11  CE  MET B   1    11939  11578  11911  -1767   1148   1222       C  
ATOM     12  N   ASN B   2      20.910  -6.452  -5.066  1.00 66.00           N  
ANISOU   12  N   ASN B   2     7774   9347   7957   -805    896    450       N  
ATOM     13  CA  ASN B   2      21.063  -4.992  -5.035  1.00 63.10           C  
ANISOU   13  CA  ASN B   2     7330   9139   7506   -566    835    266       C  
ATOM     14  C   ASN B   2      21.906  -4.469  -6.226  1.00 63.43           C  
ANISOU   14  C   ASN B   2     7472   8975   7652   -453    660    121       C  
ATOM     15  O   ASN B   2      23.026  -4.941  -6.454  1.00 66.52           O  
ANISOU   15  O   ASN B   2     8050   9154   8073   -432    597    165       O  
ATOM     16  CB  ASN B   2      21.708  -4.573  -3.693  1.00 59.31           C  
ANISOU   16  CB  ASN B   2     6937   8794   6803   -414    892    314       C  
ATOM     17  CG  ASN B   2      21.450  -3.109  -3.347  1.00 62.66           C  
ANISOU   17  CG  ASN B   2     7252   9432   7125   -212    894    118       C  
ATOM     18  ND2 ASN B   2      22.507  -2.396  -2.915  1.00 56.50           N  
ANISOU   18  ND2 ASN B   2     6603   8630   6236    -45    815     34       N  
ATOM     19  OD1 ASN B   2      20.314  -2.615  -3.486  1.00 62.64           O  
ANISOU   19  OD1 ASN B   2     7042   9606   7153   -204    959     32       O  
ATOM     20  N   ILE B   3      21.393  -3.515  -7.000  1.00 57.63           N  
ANISOU   20  N   ILE B   3     6619   8308   6971   -368    589    -39       N  
ATOM     21  CA  ILE B   3      22.205  -2.837  -8.010  1.00 61.97           C  
ANISOU   21  CA  ILE B   3     7278   8690   7575   -248    453   -155       C  
ATOM     22  C   ILE B   3      22.389  -1.398  -7.569  1.00 59.90           C  
ANISOU   22  C   ILE B   3     6999   8529   7231    -35    443   -275       C  
ATOM     23  O   ILE B   3      21.410  -0.679  -7.353  1.00 63.46           O  
ANISOU   23  O   ILE B   3     7291   9161   7659     46    479   -346       O  
ATOM     24  CB  ILE B   3      21.586  -2.922  -9.418  1.00 66.19           C  
ANISOU   24  CB  ILE B   3     7755   9169   8227   -317    356   -226       C  
ATOM     25  CG1 ILE B   3      21.688  -4.341  -9.986  1.00 67.48           C  
ANISOU   25  CG1 ILE B   3     8005   9155   8480   -530    345   -156       C  
ATOM     26  CG2 ILE B   3      22.334  -2.030 -10.366  1.00 64.81           C  
ANISOU   26  CG2 ILE B   3     7696   8864   8065   -173    246   -326       C  
ATOM     27  CD1 ILE B   3      20.436  -5.124  -9.919  1.00 72.71           C  
ANISOU   27  CD1 ILE B   3     8497   9926   9202   -746    393   -113       C  
ATOM     28  N   ARG B   4      23.640  -0.977  -7.413  1.00 56.37           N  
ANISOU   28  N   ARG B   4     6704   7963   6751     54    397   -309       N  
ATOM     29  CA  ARG B   4      23.898   0.378  -6.946  1.00 52.70           C  
ANISOU   29  CA  ARG B   4     6251   7551   6219    222    385   -442       C  
ATOM     30  C   ARG B   4      25.228   0.886  -7.471  1.00 55.34           C  
ANISOU   30  C   ARG B   4     6733   7690   6602    264    298   -502       C  
ATOM     31  O   ARG B   4      26.090   0.123  -7.925  1.00 54.92           O  
ANISOU   31  O   ARG B   4     6761   7505   6601    189    265   -432       O  
ATOM     32  CB  ARG B   4      23.882   0.472  -5.422  1.00 49.02           C  
ANISOU   32  CB  ARG B   4     5766   7276   5584    268    472   -439       C  
ATOM     33  CG  ARG B   4      25.064  -0.182  -4.768  1.00 44.99           C  
ANISOU   33  CG  ARG B   4     5376   6723   4994    230    447   -350       C  
ATOM     34  CD  ARG B   4      24.969  -0.080  -3.233  1.00 43.13           C  
ANISOU   34  CD  ARG B   4     5133   6720   4533    282    523   -342       C  
ATOM     35  NE  ARG B   4      25.980  -0.916  -2.578  1.00 50.49           N  
ANISOU   35  NE  ARG B   4     6170   7643   5369    254    484   -204       N  
ATOM     36  CZ  ARG B   4      27.287  -0.643  -2.582  1.00 54.83           C  
ANISOU   36  CZ  ARG B   4     6800   8109   5926    307    360   -262       C  
ATOM     37  NH1 ARG B   4      27.748   0.447  -3.198  1.00 55.47           N1+
ANISOU   37  NH1 ARG B   4     6885   8086   6107    354    285   -450       N1+
ATOM     38  NH2 ARG B   4      28.142  -1.453  -1.976  1.00 51.38           N  
ANISOU   38  NH2 ARG B   4     6431   7692   5401    313    310   -122       N  
ATOM     39  N   ASN B   5      25.372   2.204  -7.396  1.00 53.34           N  
ANISOU   39  N   ASN B   5     6509   7416   6341    384    274   -639       N  
ATOM     40  CA  ASN B   5      26.564   2.862  -7.908  1.00 53.18           C  
ANISOU   40  CA  ASN B   5     6610   7212   6383    395    210   -705       C  
ATOM     41  C   ASN B   5      27.753   2.467  -7.048  1.00 53.88           C  
ANISOU   41  C   ASN B   5     6735   7329   6409    353    193   -693       C  
ATOM     42  O   ASN B   5      27.661   2.457  -5.810  1.00 54.73           O  
ANISOU   42  O   ASN B   5     6815   7601   6380    386    216   -715       O  
ATOM     43  CB  ASN B   5      26.348   4.382  -7.918  1.00 56.81           C  
ANISOU   43  CB  ASN B   5     7112   7612   6861    519    199   -852       C  
ATOM     44  CG  ASN B   5      27.639   5.178  -8.069  1.00 53.57           C  
ANISOU   44  CG  ASN B   5     6822   7028   6504    491    157   -937       C  
ATOM     45  ND2 ASN B   5      28.248   5.105  -9.234  1.00 51.27           N  
ANISOU   45  ND2 ASN B   5     6596   6576   6310    424    135   -877       N  
ATOM     46  OD1 ASN B   5      28.061   5.872  -7.150  1.00 62.15           O  
ANISOU   46  OD1 ASN B   5     7938   8136   7538    517    149  -1067       O  
ATOM     47  N   ALA B   6      28.855   2.100  -7.703  1.00 53.92           N  
ANISOU   47  N   ALA B   6     6790   7202   6494    294    154   -656       N  
ATOM     48  CA  ALA B   6      30.032   1.654  -6.963  1.00 55.50           C  
ANISOU   48  CA  ALA B   6     6987   7449   6651    278    115   -634       C  
ATOM     49  C   ALA B   6      30.741   2.838  -6.338  1.00 59.87           C  
ANISOU   49  C   ALA B   6     7549   8028   7172    299     64   -797       C  
ATOM     50  O   ALA B   6      30.811   3.926  -6.921  1.00 70.99           O  
ANISOU   50  O   ALA B   6     9003   9306   8664    292     63   -908       O  
ATOM     51  CB  ALA B   6      31.015   0.908  -7.860  1.00 52.84           C  
ANISOU   51  CB  ALA B   6     6668   6983   6426    233    101   -562       C  
ATOM     52  N   ARG B   7      31.272   2.617  -5.152  1.00 55.61           N  
ANISOU   52  N   ARG B   7     6980   7647   6503    318     13   -810       N  
ATOM     53  CA  ARG B   7      32.035   3.611  -4.425  1.00 59.61           C  
ANISOU   53  CA  ARG B   7     7484   8206   6957    312    -63   -990       C  
ATOM     54  C   ARG B   7      33.462   3.114  -4.176  1.00 62.47           C  
ANISOU   54  C   ARG B   7     7776   8630   7332    279   -164   -962       C  
ATOM     55  O   ARG B   7      33.754   1.923  -4.320  1.00 70.80           O  
ANISOU   55  O   ARG B   7     8797   9704   8397    305   -167   -788       O  
ATOM     56  CB  ARG B   7      31.298   3.954  -3.123  1.00 63.83           C  
ANISOU   56  CB  ARG B   7     8038   8937   7279    385    -52  -1076       C  
ATOM     57  CG  ARG B   7      29.976   4.719  -3.354  1.00 75.13           C  
ANISOU   57  CG  ARG B   7     9504  10317   8725    450     47  -1157       C  
ATOM     58  CD  ARG B   7      29.153   4.866  -2.066  1.00 98.44           C  
ANISOU   58  CD  ARG B   7    12452  13502  11447    541    103  -1227       C  
ATOM     59  NE  ARG B   7      28.923   3.577  -1.395  1.00113.72           N  
ANISOU   59  NE  ARG B   7    14344  15639  13224    533    141  -1023       N  
ATOM     60  CZ  ARG B   7      28.308   3.430  -0.220  1.00124.12           C  
ANISOU   60  CZ  ARG B   7    15658  17204  14299    591    212  -1022       C  
ATOM     61  NH1 ARG B   7      28.156   2.217   0.302  1.00127.37           N1+
ANISOU   61  NH1 ARG B   7    16057  17759  14580    562    256   -793       N1+
ATOM     62  NH2 ARG B   7      27.849   4.492   0.439  1.00129.56           N  
ANISOU   62  NH2 ARG B   7    16372  17985  14868    680    252  -1247       N  
ATOM     63  N   PRO B   8      34.387   4.008  -3.872  1.00 58.83           N  
ANISOU   63  N   PRO B   8     7278   8183   6890    220   -251  -1137       N  
ATOM     64  CA  PRO B   8      35.788   3.585  -3.685  1.00 56.17           C  
ANISOU   64  CA  PRO B   8     6816   7940   6585    192   -361  -1123       C  
ATOM     65  C   PRO B   8      36.013   2.379  -2.765  1.00 59.22           C  
ANISOU   65  C   PRO B   8     7157   8540   6805    302   -439   -964       C  
ATOM     66  O   PRO B   8      36.896   1.567  -3.065  1.00 61.47           O  
ANISOU   66  O   PRO B   8     7348   8836   7173    338   -483   -851       O  
ATOM     67  CB  PRO B   8      36.430   4.860  -3.115  1.00 60.48           C  
ANISOU   67  CB  PRO B   8     7335   8526   7120     94   -458  -1380       C  
ATOM     68  CG  PRO B   8      35.673   5.966  -3.739  1.00 53.52           C  
ANISOU   68  CG  PRO B   8     6582   7415   6337     44   -356  -1492       C  
ATOM     69  CD  PRO B   8      34.254   5.474  -3.921  1.00 56.06           C  
ANISOU   69  CD  PRO B   8     6994   7716   6590    163   -245  -1356       C  
ATOM     70  N   GLU B   9      35.278   2.244  -1.646  1.00 65.68           N  
ANISOU   70  N   GLU B   9     8043   9529   7384    372   -451   -944       N  
ATOM     71  CA  GLU B   9      35.392   1.042  -0.802  1.00 68.06           C  
ANISOU   71  CA  GLU B   9     8344  10007   7507    481   -505   -736       C  
ATOM     72  C   GLU B   9      34.829  -0.225  -1.462  1.00 65.23           C  
ANISOU   72  C   GLU B   9     8042   9502   7241    517   -387   -478       C  
ATOM     73  O   GLU B   9      34.907  -1.313  -0.871  1.00 65.28           O  
ANISOU   73  O   GLU B   9     8081   9588   7134    605   -413   -268       O  
ATOM     74  CB  GLU B   9      34.695   1.241   0.543  1.00 71.80           C  
ANISOU   74  CB  GLU B   9     8896  10714   7670    531   -513   -766       C  
ATOM     75  CG  GLU B   9      33.414   2.031   0.447  1.00 81.83           C  
ANISOU   75  CG  GLU B   9    10244  11926   8921    500   -365   -888       C  
ATOM     76  CD  GLU B   9      32.539   1.852   1.657  1.00 94.47           C  
ANISOU   76  CD  GLU B   9    11916  13765  10213    568   -303   -845       C  
ATOM     77  OE1 GLU B   9      33.083   1.731   2.783  1.00107.44           O  
ANISOU   77  OE1 GLU B   9    13572  15651  11598    622   -420   -853       O  
ATOM     78  OE2 GLU B   9      31.303   1.812   1.470  1.00 98.90           O1-
ANISOU   78  OE2 GLU B   9    12508  14292  10779    569   -134   -799       O1-
ATOM     79  N   ASP B  10      34.276  -0.128  -2.662  1.00 63.21           N  
ANISOU   79  N   ASP B  10     7812   9025   7178    451   -269   -487       N  
ATOM     80  CA  ASP B  10      33.803  -1.314  -3.357  1.00 64.89           C  
ANISOU   80  CA  ASP B  10     8081   9086   7490    457   -176   -288       C  
ATOM     81  C   ASP B  10      34.826  -1.898  -4.314  1.00 69.83           C  
ANISOU   81  C   ASP B  10     8661   9562   8310    481   -195   -246       C  
ATOM     82  O   ASP B  10      34.642  -3.036  -4.766  1.00 71.53           O  
ANISOU   82  O   ASP B  10     8938   9642   8596    509   -139    -90       O  
ATOM     83  CB  ASP B  10      32.527  -0.989  -4.117  1.00 55.69           C  
ANISOU   83  CB  ASP B  10     6963   7803   6394    380    -51   -324       C  
ATOM     84  CG  ASP B  10      31.376  -0.735  -3.201  1.00 59.76           C  
ANISOU   84  CG  ASP B  10     7502   8476   6730    382      9   -323       C  
ATOM     85  OD1 ASP B  10      31.332  -1.387  -2.140  1.00 68.44           O  
ANISOU   85  OD1 ASP B  10     8626   9725   7651    423      3   -192       O  
ATOM     86  OD2 ASP B  10      30.506   0.076  -3.560  1.00 63.31           O1-
ANISOU   86  OD2 ASP B  10     7942   8901   7210    357     71   -438       O1-
ATOM     87  N   LEU B  11      35.917  -1.174  -4.592  1.00 67.37           N  
ANISOU   87  N   LEU B  11     8238   9274   8085    466   -264   -389       N  
ATOM     88  CA  LEU B  11      36.734  -1.529  -5.747  1.00 63.36           C  
ANISOU   88  CA  LEU B  11     7674   8623   7777    471   -225   -385       C  
ATOM     89  C   LEU B  11      37.548  -2.804  -5.516  1.00 62.79           C  
ANISOU   89  C   LEU B  11     7559   8568   7730    621   -277   -229       C  
ATOM     90  O   LEU B  11      37.655  -3.639  -6.419  1.00 65.97           O  
ANISOU   90  O   LEU B  11     8004   8798   8265    664   -195   -159       O  
ATOM     91  CB  LEU B  11      37.613  -0.343  -6.158  1.00 59.55           C  
ANISOU   91  CB  LEU B  11     7072   8161   7394    378   -249   -573       C  
ATOM     92  CG  LEU B  11      36.805   0.903  -6.562  1.00 63.78           C  
ANISOU   92  CG  LEU B  11     7694   8602   7938    254   -184   -706       C  
ATOM     93  CD1 LEU B  11      37.729   2.121  -6.783  1.00 64.44           C  
ANISOU   93  CD1 LEU B  11     7683   8682   8120    133   -210   -881       C  
ATOM     94  CD2 LEU B  11      35.897   0.657  -7.786  1.00 62.58           C  
ANISOU   94  CD2 LEU B  11     7663   8254   7859    230    -54   -642       C  
ATOM     95  N   MET B  12      38.128  -2.977  -4.329  1.00 61.19           N  
ANISOU   95  N   MET B  12     7286   8571   7395    721   -419   -179       N  
ATOM     96  CA  MET B  12      38.791  -4.241  -4.035  1.00 65.28           C  
ANISOU   96  CA  MET B  12     7788   9090   7924    909   -479      7       C  
ATOM     97  C   MET B  12      37.855  -5.428  -4.238  1.00 67.03           C  
ANISOU   97  C   MET B  12     8217   9099   8154    941   -369    209       C  
ATOM     98  O   MET B  12      38.262  -6.463  -4.787  1.00 64.95           O  
ANISOU   98  O   MET B  12     7990   8661   8025   1056   -331    312       O  
ATOM     99  CB  MET B  12      39.362  -4.250  -2.602  1.00 75.54           C  
ANISOU   99  CB  MET B  12     9012  10671   9018   1025   -673     63       C  
ATOM    100  CG  MET B  12      40.563  -3.321  -2.377  1.00 86.74           C  
ANISOU  100  CG  MET B  12    10183  12314  10460   1003   -824   -135       C  
ATOM    101  SD  MET B  12      41.459  -3.414  -0.818  1.00 92.98           S  
ANISOU  101  SD  MET B  12    10839  13480  11010   1159  -1107    -94       S  
ATOM    102  CE  MET B  12      41.448  -5.131  -0.566  1.00 86.23           C  
ANISOU  102  CE  MET B  12    10116  12524  10123   1431  -1111    262       C  
ATOM    103  N   ASN B  13      36.613  -5.303  -3.769  1.00 65.84           N  
ANISOU  103  N   ASN B  13     8195   8958   7864    839   -310    256       N  
ATOM    104  CA  ASN B  13      35.623  -6.354  -3.987  1.00 62.98           C  
ANISOU  104  CA  ASN B  13     8009   8394   7526    804   -192    429       C  
ATOM    105  C   ASN B  13      35.321  -6.554  -5.466  1.00 68.03           C  
ANISOU  105  C   ASN B  13     8689   8782   8376    717    -77    344       C  
ATOM    106  O   ASN B  13      35.157  -7.695  -5.928  1.00 70.73           O  
ANISOU  106  O   ASN B  13     9153   8900   8822    741    -14    458       O  
ATOM    107  CB  ASN B  13      34.340  -6.024  -3.247  1.00 58.31           C  
ANISOU  107  CB  ASN B  13     7487   7914   6754    687   -132    465       C  
ATOM    108  CG  ASN B  13      34.531  -6.013  -1.777  1.00 66.01           C  
ANISOU  108  CG  ASN B  13     8470   9137   7474    776   -224    572       C  
ATOM    109  ND2 ASN B  13      33.663  -5.296  -1.072  1.00 74.99           N  
ANISOU  109  ND2 ASN B  13     9613  10458   8422    695   -181    512       N  
ATOM    110  OD1 ASN B  13      35.445  -6.673  -1.258  1.00 68.98           O  
ANISOU  110  OD1 ASN B  13     8850   9554   7806    938   -334    713       O  
ATOM    111  N   MET B  14      35.205  -5.452  -6.216  1.00 65.35           N  
ANISOU  111  N   MET B  14     8275   8467   8089    613    -49    144       N  
ATOM    112  CA  MET B  14      35.113  -5.571  -7.664  1.00 65.10           C  
ANISOU  112  CA  MET B  14     8280   8238   8218    554     42     58       C  
ATOM    113  C   MET B  14      36.316  -6.319  -8.207  1.00 65.49           C  
ANISOU  113  C   MET B  14     8300   8184   8400    694     44     72       C  
ATOM    114  O   MET B  14      36.171  -7.252  -9.002  1.00 71.10           O  
ANISOU  114  O   MET B  14     9123   8681   9212    710    120    100       O  
ATOM    115  CB  MET B  14      35.024  -4.198  -8.320  1.00 69.64           C  
ANISOU  115  CB  MET B  14     8787   8865   8808    454     60   -126       C  
ATOM    116  CG  MET B  14      33.701  -3.493  -8.172  1.00 78.58           C  
ANISOU  116  CG  MET B  14     9958  10043   9855    345     84   -164       C  
ATOM    117  SD  MET B  14      33.752  -1.950  -9.095  1.00 90.29           S  
ANISOU  117  SD  MET B  14    11405  11513  11387    271    103   -349       S  
ATOM    118  CE  MET B  14      34.321  -2.512 -10.703  1.00 86.36           C  
ANISOU  118  CE  MET B  14    10954  10836  11024    265    181   -365       C  
ATOM    119  N   GLN B  15      37.520  -5.932  -7.768  1.00 58.83           N  
ANISOU  119  N   GLN B  15     7293   7501   7560    800    -41     36       N  
ATOM    120  CA  GLN B  15      38.727  -6.569  -8.279  1.00 58.13           C  
ANISOU  120  CA  GLN B  15     7120   7358   7610    960    -31     34       C  
ATOM    121  C   GLN B  15      38.712  -8.062  -7.990  1.00 64.67           C  
ANISOU  121  C   GLN B  15     8085   8015   8472   1125    -33    220       C  
ATOM    122  O   GLN B  15      39.152  -8.869  -8.818  1.00 70.85           O  
ANISOU  122  O   GLN B  15     8913   8611   9395   1234     46    207       O  
ATOM    123  CB  GLN B  15      39.969  -5.917  -7.681  1.00 57.53           C  
ANISOU  123  CB  GLN B  15     6798   7533   7529   1036   -148    -27       C  
ATOM    124  CG  GLN B  15      41.277  -6.504  -8.180  1.00 59.11           C  
ANISOU  124  CG  GLN B  15     6842   7732   7884   1222   -133    -40       C  
ATOM    125  CD  GLN B  15      42.452  -6.208  -7.245  1.00 63.44           C  
ANISOU  125  CD  GLN B  15     7126   8567   8411   1340   -305    -45       C  
ATOM    126  NE2 GLN B  15      43.526  -5.623  -7.781  1.00 59.13           N  
ANISOU  126  NE2 GLN B  15     6323   8153   7990   1321   -280   -190       N  
ATOM    127  OE1 GLN B  15      42.381  -6.494  -6.053  1.00 72.16           O  
ANISOU  127  OE1 GLN B  15     8251   9791   9376   1437   -458     83       O  
ATOM    128  N   HIS B  16      38.174  -8.451  -6.834  1.00 57.21           N  
ANISOU  128  N   HIS B  16     7232   7112   7392   1146   -105    395       N  
ATOM    129  CA  HIS B  16      38.078  -9.869  -6.510  1.00 58.69           C  
ANISOU  129  CA  HIS B  16     7596   7093   7612   1284    -96    609       C  
ATOM    130  C   HIS B  16      37.133 -10.558  -7.480  1.00 67.02           C  
ANISOU  130  C   HIS B  16     8853   7835   8775   1149     47    591       C  
ATOM    131  O   HIS B  16      37.448 -11.618  -8.045  1.00 68.50           O  
ANISOU  131  O   HIS B  16     9161   7759   9108   1266    102    624       O  
ATOM    132  CB  HIS B  16      37.601 -10.029  -5.064  1.00 57.79           C  
ANISOU  132  CB  HIS B  16     7553   7112   7291   1294   -180    819       C  
ATOM    133  CG  HIS B  16      37.237 -11.429  -4.680  1.00 67.85           C  
ANISOU  133  CG  HIS B  16     9063   8137   8582   1374   -144   1081       C  
ATOM    134  CD2 HIS B  16      36.038 -11.991  -4.399  1.00 72.28           C  
ANISOU  134  CD2 HIS B  16     9825   8547   9091   1211    -49   1230       C  
ATOM    135  ND1 HIS B  16      38.171 -12.432  -4.533  1.00 77.49           N  
ANISOU  135  ND1 HIS B  16    10331   9222   9892   1649   -201   1230       N  
ATOM    136  CE1 HIS B  16      37.563 -13.553  -4.187  1.00 77.58           C  
ANISOU  136  CE1 HIS B  16    10601   8969   9908   1651   -142   1469       C  
ATOM    137  NE2 HIS B  16      36.269 -13.313  -4.100  1.00 75.04           N  
ANISOU  137  NE2 HIS B  16    10369   8640   9503   1365    -44   1473       N  
ATOM    138  N   CYS B  17      35.975  -9.939  -7.707  1.00 63.77           N  
ANISOU  138  N   CYS B  17     8475   7456   8300    910    101    515       N  
ATOM    139  CA  CYS B  17      35.002 -10.494  -8.629  1.00 68.39           C  
ANISOU  139  CA  CYS B  17     9218   7796   8972    749    207    471       C  
ATOM    140  C   CYS B  17      35.608 -10.664 -10.011  1.00 68.41           C  
ANISOU  140  C   CYS B  17     9228   7647   9116    802    269    295       C  
ATOM    141  O   CYS B  17      35.514 -11.741 -10.615  1.00 65.97           O  
ANISOU  141  O   CYS B  17     9088   7058   8921    823    332    295       O  
ATOM    142  CB  CYS B  17      33.777  -9.593  -8.677  1.00 67.13           C  
ANISOU  142  CB  CYS B  17     9017   7771   8716    522    228    394       C  
ATOM    143  SG  CYS B  17      32.411 -10.401  -9.459  1.00 71.29           S  
ANISOU  143  SG  CYS B  17     9705   8060   9323    299    315    382       S  
ATOM    144  N   ASN B  18      36.266  -9.613 -10.503  1.00 63.58           N  
ANISOU  144  N   ASN B  18     8449   7213   8495    821    264    140       N  
ATOM    145  CA  ASN B  18      36.968  -9.655 -11.778  1.00 58.72           C  
ANISOU  145  CA  ASN B  18     7818   6514   7979    880    348    -20       C  
ATOM    146  C   ASN B  18      37.916 -10.839 -11.849  1.00 64.82           C  
ANISOU  146  C   ASN B  18     8637   7114   8878   1120    376     27       C  
ATOM    147  O   ASN B  18      37.835 -11.671 -12.763  1.00 66.16           O  
ANISOU  147  O   ASN B  18     8964   7039   9135   1146    467    -52       O  
ATOM    148  CB  ASN B  18      37.740  -8.354 -11.975  1.00 64.94           C  
ANISOU  148  CB  ASN B  18     8393   7543   8739    873    341   -134       C  
ATOM    149  CG  ASN B  18      38.676  -8.406 -13.174  1.00 69.89           C  
ANISOU  149  CG  ASN B  18     8969   8132   9455    955    456   -273       C  
ATOM    150  ND2 ASN B  18      38.138  -8.098 -14.350  1.00 60.33           N  
ANISOU  150  ND2 ASN B  18     7860   6855   8210    822    546   -393       N  
ATOM    151  OD1 ASN B  18      39.874  -8.708 -13.041  1.00 76.47           O  
ANISOU  151  OD1 ASN B  18     9662   9020  10374   1146    465   -270       O  
ATOM    152  N   LEU B  19      38.817 -10.932 -10.870  1.00 62.50           N  
ANISOU  152  N   LEU B  19     8210   6948   8590   1316    287    146       N  
ATOM    153  CA  LEU B  19      39.801 -12.006 -10.864  1.00 57.69           C  
ANISOU  153  CA  LEU B  19     7614   6196   8110   1604    296    205       C  
ATOM    154  C   LEU B  19      39.146 -13.382 -10.867  1.00 61.34           C  
ANISOU  154  C   LEU B  19     8377   6286   8643   1634    337    320       C  
ATOM    155  O   LEU B  19      39.711 -14.340 -11.413  1.00 71.18           O  
ANISOU  155  O   LEU B  19     9721   7293  10031   1834    406    286       O  
ATOM    156  CB  LEU B  19      40.720 -11.855  -9.654  1.00 58.64           C  
ANISOU  156  CB  LEU B  19     7536   6553   8191   1806    146    345       C  
ATOM    157  CG  LEU B  19      41.902 -10.896  -9.793  1.00 66.75           C  
ANISOU  157  CG  LEU B  19     8229   7891   9242   1869    115    209       C  
ATOM    158  CD1 LEU B  19      42.188 -10.139  -8.477  1.00 67.81           C  
ANISOU  158  CD1 LEU B  19     8177   8348   9239   1863    -74    291       C  
ATOM    159  CD2 LEU B  19      43.104 -11.686 -10.215  1.00 78.22           C  
ANISOU  159  CD2 LEU B  19     9574   9288  10860   2180    158    187       C  
ATOM    160  N   LEU B  20      37.976 -13.521 -10.253  1.00 59.10           N  
ANISOU  160  N   LEU B  20     8244   5936   8274   1437    308    452       N  
ATOM    161  CA  LEU B  20      37.360 -14.844 -10.256  1.00 66.54           C  
ANISOU  161  CA  LEU B  20     9477   6497   9307   1419    359    567       C  
ATOM    162  C   LEU B  20      36.799 -15.191 -11.625  1.00 67.24           C  
ANISOU  162  C   LEU B  20     9719   6344   9486   1262    473    347       C  
ATOM    163  O   LEU B  20      36.777 -16.367 -11.998  1.00 65.20           O  
ANISOU  163  O   LEU B  20     9691   5720   9363   1327    533    345       O  
ATOM    164  CB  LEU B  20      36.245 -14.938  -9.214  1.00 66.90           C  
ANISOU  164  CB  LEU B  20     9625   6556   9239   1222    325    781       C  
ATOM    165  CG  LEU B  20      36.599 -15.021  -7.732  1.00 68.52           C  
ANISOU  165  CG  LEU B  20     9798   6914   9324   1377    220   1058       C  
ATOM    166  CD1 LEU B  20      35.310 -14.995  -6.989  1.00 69.15           C  
ANISOU  166  CD1 LEU B  20     9974   7024   9274   1116    247   1211       C  
ATOM    167  CD2 LEU B  20      37.418 -16.255  -7.365  1.00 70.90           C  
ANISOU  167  CD2 LEU B  20    10250   6952   9736   1688    194   1255       C  
ATOM    168  N   CYS B  21      36.395 -14.177 -12.393  1.00 67.01           N  
ANISOU  168  N   CYS B  21     9578   6508   9375   1073    495    154       N  
ATOM    169  CA  CYS B  21      35.424 -14.305 -13.469  1.00 72.50           C  
ANISOU  169  CA  CYS B  21    10411   7062  10075    836    554    -21       C  
ATOM    170  C   CYS B  21      35.976 -14.143 -14.866  1.00 77.55           C  
ANISOU  170  C   CYS B  21    11050   7687  10730    896    638   -276       C  
ATOM    171  O   CYS B  21      35.381 -14.674 -15.803  1.00 82.12           O  
ANISOU  171  O   CYS B  21    11808   8066  11327    769    684   -431       O  
ATOM    172  CB  CYS B  21      34.331 -13.249 -13.302  1.00 74.07           C  
ANISOU  172  CB  CYS B  21    10501   7506  10135    573    504    -27       C  
ATOM    173  SG  CYS B  21      33.134 -13.697 -12.093  1.00 78.93           S  
ANISOU  173  SG  CYS B  21    11190   8076  10724    386    469    204       S  
ATOM    174  N   LEU B  22      37.050 -13.385 -15.031  1.00 74.17           N  
ANISOU  174  N   LEU B  22    10419   7486  10277   1058    661   -330       N  
ATOM    175  CA  LEU B  22      37.502 -12.919 -16.329  1.00 70.47           C  
ANISOU  175  CA  LEU B  22     9912   7095   9768   1069    763   -550       C  
ATOM    176  C   LEU B  22      39.009 -13.055 -16.450  1.00 74.64           C  
ANISOU  176  C   LEU B  22    10294   7683  10383   1362    844   -587       C  
ATOM    177  O   LEU B  22      39.721 -13.085 -15.442  1.00 76.77           O  
ANISOU  177  O   LEU B  22    10410   8045  10714   1535    777   -437       O  
ATOM    178  CB  LEU B  22      37.104 -11.456 -16.538  1.00 66.29           C  
ANISOU  178  CB  LEU B  22     9236   6857   9095    881    733   -584       C  
ATOM    179  CG  LEU B  22      35.626 -11.330 -16.867  1.00 58.48           C  
ANISOU  179  CG  LEU B  22     8378   5825   8018    620    677   -617       C  
ATOM    180  CD1 LEU B  22      35.234  -9.839 -16.785  1.00 50.88           C  
ANISOU  180  CD1 LEU B  22     7262   5138   6931    490    626   -601       C  
ATOM    181  CD2 LEU B  22      35.351 -11.961 -18.224  1.00 46.52           C  
ANISOU  181  CD2 LEU B  22     7061   4137   6479    570    748   -819       C  
ATOM    182  N   PRO B  23      39.528 -13.133 -17.676  1.00 77.47           N  
ANISOU  182  N   PRO B  23    10679   8022  10734   1431    989   -789       N  
ATOM    183  CA  PRO B  23      40.982 -13.248 -17.843  1.00 76.15           C  
ANISOU  183  CA  PRO B  23    10325   7949  10658   1717   1095   -838       C  
ATOM    184  C   PRO B  23      41.703 -11.905 -17.802  1.00 71.86           C  
ANISOU  184  C   PRO B  23     9467   7776  10058   1670   1116   -833       C  
ATOM    185  O   PRO B  23      42.885 -11.846 -17.436  1.00 73.74           O  
ANISOU  185  O   PRO B  23     9453   8170  10395   1876   1139   -806       O  
ATOM    186  CB  PRO B  23      41.122 -13.905 -19.219  1.00 75.17           C  
ANISOU  186  CB  PRO B  23    10386   7652  10522   1786   1270  -1076       C  
ATOM    187  CG  PRO B  23      39.694 -14.206 -19.686  1.00 73.04           C  
ANISOU  187  CG  PRO B  23    10416   7178  10158   1520   1215  -1146       C  
ATOM    188  CD  PRO B  23      38.823 -13.274 -18.960  1.00 69.94           C  
ANISOU  188  CD  PRO B  23     9936   6957   9682   1274   1065   -988       C  
ATOM    189  N   GLU B  24      41.016 -10.824 -18.189  1.00 61.65           N  
ANISOU  189  N   GLU B  24     8182   6620   8621   1401   1105   -861       N  
ATOM    190  CA  GLU B  24      41.634  -9.500 -18.221  1.00 71.37           C  
ANISOU  190  CA  GLU B  24     9161   8146   9809   1314   1139   -859       C  
ATOM    191  C   GLU B  24      41.514  -8.883 -16.826  1.00 73.43           C  
ANISOU  191  C   GLU B  24     9268   8543  10088   1255    955   -701       C  
ATOM    192  O   GLU B  24      40.415  -8.574 -16.351  1.00 63.30           O  
ANISOU  192  O   GLU B  24     8100   7224   8725   1090    839   -630       O  
ATOM    193  CB  GLU B  24      41.005  -8.608 -19.299  1.00 76.31           C  
ANISOU  193  CB  GLU B  24     9896   8828  10269   1086   1216   -944       C  
ATOM    194  CG  GLU B  24      41.348  -8.980 -20.763  1.00 83.60           C  
ANISOU  194  CG  GLU B  24    10937   9709  11116   1142   1423  -1117       C  
ATOM    195  CD  GLU B  24      40.401 -10.035 -21.348  1.00 96.15           C  
ANISOU  195  CD  GLU B  24    12844  11041  12647   1133   1402  -1220       C  
ATOM    196  OE1 GLU B  24      39.166  -9.892 -21.151  1.00 99.96           O  
ANISOU  196  OE1 GLU B  24    13465  11455  13059    950   1256  -1172       O  
ATOM    197  OE2 GLU B  24      40.891 -11.023 -21.965  1.00101.06           O1-
ANISOU  197  OE2 GLU B  24    13565  11528  13307   1311   1530  -1360       O1-
ATOM    198  N   ASN B  25      42.651  -8.720 -16.165  1.00 78.98           N  
ANISOU  198  N   ASN B  25     9699   9424  10887   1398    926   -661       N  
ATOM    199  CA  ASN B  25      42.712  -8.252 -14.797  1.00 74.62           C  
ANISOU  199  CA  ASN B  25     8995   9024  10334   1379    739   -536       C  
ATOM    200  C   ASN B  25      43.470  -6.939 -14.738  1.00 81.03           C  
ANISOU  200  C   ASN B  25     9531  10107  11150   1254    749   -592       C  
ATOM    201  O   ASN B  25      44.230  -6.595 -15.647  1.00 90.59           O  
ANISOU  201  O   ASN B  25    10613  11402  12404   1239    914   -695       O  
ATOM    202  CB  ASN B  25      43.366  -9.306 -13.918  1.00 70.56           C  
ANISOU  202  CB  ASN B  25     8407   8482   9919   1667    644   -428       C  
ATOM    203  CG  ASN B  25      42.808 -10.676 -14.197  1.00 67.32           C  
ANISOU  203  CG  ASN B  25     8289   7742   9549   1796    685   -392       C  
ATOM    204  ND2 ASN B  25      41.476 -10.772 -14.206  1.00 61.54           N  
ANISOU  204  ND2 ASN B  25     7814   6841   8727   1598    655   -357       N  
ATOM    205  OD1 ASN B  25      43.546 -11.630 -14.437  1.00 74.36           O  
ANISOU  205  OD1 ASN B  25     9171   8523  10560   2064    748   -410       O  
ATOM    206  N   TYR B  26      43.237  -6.190 -13.667  1.00 81.89           N  
ANISOU  206  N   TYR B  26     9561  10347  11208   1145    584   -532       N  
ATOM    207  CA  TYR B  26      43.864  -4.888 -13.502  1.00 78.11           C  
ANISOU  207  CA  TYR B  26     8849  10088  10743    982    570   -601       C  
ATOM    208  C   TYR B  26      44.403  -4.767 -12.086  1.00 79.73           C  
ANISOU  208  C   TYR B  26     8844  10493  10955   1054    359   -551       C  
ATOM    209  O   TYR B  26      44.046  -5.537 -11.187  1.00 83.89           O  
ANISOU  209  O   TYR B  26     9460  10986  11430   1201    221   -433       O  
ATOM    210  CB  TYR B  26      42.866  -3.772 -13.836  1.00 72.81           C  
ANISOU  210  CB  TYR B  26     8345   9352   9968    719    593   -632       C  
ATOM    211  CG  TYR B  26      42.070  -4.101 -15.084  1.00 71.35           C  
ANISOU  211  CG  TYR B  26     8416   8971   9723    683    738   -651       C  
ATOM    212  CD1 TYR B  26      42.585  -3.832 -16.350  1.00 70.76           C  
ANISOU  212  CD1 TYR B  26     8326   8901   9660    636    935   -728       C  
ATOM    213  CD2 TYR B  26      40.824  -4.727 -15.003  1.00 73.57           C  
ANISOU  213  CD2 TYR B  26     8944   9085   9925    690    678   -596       C  
ATOM    214  CE1 TYR B  26      41.873  -4.147 -17.504  1.00 72.69           C  
ANISOU  214  CE1 TYR B  26     8815   8996   9807    610   1047   -759       C  
ATOM    215  CE2 TYR B  26      40.096  -5.046 -16.159  1.00 72.62           C  
ANISOU  215  CE2 TYR B  26     9041   8812   9740    644    780   -640       C  
ATOM    216  CZ  TYR B  26      40.635  -4.755 -17.403  1.00 78.51           C  
ANISOU  216  CZ  TYR B  26     9786   9575  10470    615    953   -725       C  
ATOM    217  OH  TYR B  26      39.950  -5.071 -18.554  1.00 87.21           O  
ANISOU  217  OH  TYR B  26    11111  10557  11468    578   1035   -781       O  
ATOM    218  N   GLN B  27      45.300  -3.816 -11.906  1.00 83.58           N  
ANISOU  218  N   GLN B  27     9056  11200  11502    941    336   -639       N  
ATOM    219  CA  GLN B  27      45.772  -3.508 -10.568  1.00 83.80           C  
ANISOU  219  CA  GLN B  27     8882  11453  11503    962    107   -631       C  
ATOM    220  C   GLN B  27      44.843  -2.487  -9.925  1.00 82.31           C  
ANISOU  220  C   GLN B  27     8845  11249  11179    740      8   -660       C  
ATOM    221  O   GLN B  27      44.123  -1.748 -10.609  1.00 79.91           O  
ANISOU  221  O   GLN B  27     8713  10798  10852    548    125   -708       O  
ATOM    222  CB  GLN B  27      47.211  -3.002 -10.606  1.00 81.14           C  
ANISOU  222  CB  GLN B  27     8142  11380  11307    928    106   -738       C  
ATOM    223  CG  GLN B  27      48.022  -3.739 -11.637  1.00 86.41           C  
ANISOU  223  CG  GLN B  27     8670  12043  12119   1098    303   -752       C  
ATOM    224  CD  GLN B  27      49.408  -4.042 -11.166  1.00 97.82           C  
ANISOU  224  CD  GLN B  27     9691  13783  13695   1280    207   -778       C  
ATOM    225  NE2 GLN B  27      49.696  -5.316 -10.997  1.00104.48           N  
ANISOU  225  NE2 GLN B  27    10520  14601  14577   1639    167   -682       N  
ATOM    226  OE1 GLN B  27      50.219  -3.141 -10.945  1.00109.54           O  
ANISOU  226  OE1 GLN B  27    10853  15512  15254   1100    163   -885       O  
ATOM    227  N   MET B  28      44.837  -2.489  -8.586  1.00 75.52           N  
ANISOU  227  N   MET B  28     7934  10546  10213    798   -213   -627       N  
ATOM    228  CA  MET B  28      43.911  -1.642  -7.849  1.00 68.02           C  
ANISOU  228  CA  MET B  28     7141   9592   9110    636   -303   -666       C  
ATOM    229  C   MET B  28      44.002  -0.197  -8.312  1.00 71.61           C  
ANISOU  229  C   MET B  28     7555  10027   9627    358   -233   -835       C  
ATOM    230  O   MET B  28      42.975   0.485  -8.443  1.00 72.96           O  
ANISOU  230  O   MET B  28     7945  10049   9728    228   -184   -864       O  
ATOM    231  CB  MET B  28      44.196  -1.738  -6.348  1.00 74.63           C  
ANISOU  231  CB  MET B  28     7878  10672   9807    732   -551   -644       C  
ATOM    232  CG  MET B  28      43.458  -2.854  -5.600  1.00 71.34           C  
ANISOU  232  CG  MET B  28     7661  10213   9233    937   -621   -440       C  
ATOM    233  SD  MET B  28      41.653  -2.898  -5.852  1.00 68.85           S  
ANISOU  233  SD  MET B  28     7715   9637   8809    835   -480   -369       S  
ATOM    234  CE  MET B  28      41.154  -1.155  -5.671  1.00 59.21           C  
ANISOU  234  CE  MET B  28     6513   8462   7524    570   -487   -585       C  
ATOM    235  N   LYS B  29      45.229   0.285  -8.588  1.00 67.80           N  
ANISOU  235  N   LYS B  29     6786   9686   9290    264   -217   -941       N  
ATOM    236  CA  LYS B  29      45.393   1.667  -9.030  1.00 63.28           C  
ANISOU  236  CA  LYS B  29     6187   9060   8798    -31   -136  -1085       C  
ATOM    237  C   LYS B  29      44.528   1.989 -10.252  1.00 67.98           C  
ANISOU  237  C   LYS B  29     7052   9375   9401   -123     84  -1041       C  
ATOM    238  O   LYS B  29      43.962   3.081 -10.341  1.00 71.75           O  
ANISOU  238  O   LYS B  29     7684   9718   9860   -308    110  -1105       O  
ATOM    239  CB  LYS B  29      46.857   1.969  -9.322  1.00 62.74           C  
ANISOU  239  CB  LYS B  29     5749   9179   8911   -134   -103  -1180       C  
ATOM    240  CG  LYS B  29      47.136   3.471  -9.302  1.00 71.55           C  
ANISOU  240  CG  LYS B  29     6810  10272  10105   -479    -93  -1345       C  
ATOM    241  CD  LYS B  29      48.612   3.794  -9.466  1.00 87.66           C  
ANISOU  241  CD  LYS B  29     8434  12535  12337   -629    -73  -1449       C  
ATOM    242  CE  LYS B  29      48.842   5.306  -9.521  1.00 99.18           C  
ANISOU  242  CE  LYS B  29     9880  13906  13899  -1021    -37  -1609       C  
ATOM    243  NZ  LYS B  29      47.934   6.004 -10.500  1.00103.88           N1+
ANISOU  243  NZ  LYS B  29    10842  14144  14486  -1160    184  -1545       N1+
ATOM    244  N   TYR B  30      44.404   1.058 -11.204  1.00 68.17           N  
ANISOU  244  N   TYR B  30     7152   9306   9445     17    233   -938       N  
ATOM    245  CA  TYR B  30      43.503   1.289 -12.335  1.00 65.32           C  
ANISOU  245  CA  TYR B  30     7061   8713   9046    -51    405   -894       C  
ATOM    246  C   TYR B  30      42.046   1.398 -11.877  1.00 64.14           C  
ANISOU  246  C   TYR B  30     7180   8434   8754    -31    316   -853       C  
ATOM    247  O   TYR B  30      41.292   2.239 -12.382  1.00 65.04           O  
ANISOU  247  O   TYR B  30     7477   8400   8835   -150    378   -864       O  
ATOM    248  CB  TYR B  30      43.670   0.177 -13.378  1.00 59.81           C  
ANISOU  248  CB  TYR B  30     6395   7961   8371    104    561   -827       C  
ATOM    249  CG  TYR B  30      43.189   0.521 -14.773  1.00 65.14           C  
ANISOU  249  CG  TYR B  30     7273   8470   9008      7    759   -810       C  
ATOM    250  CD1 TYR B  30      43.581   1.698 -15.402  1.00 68.09           C  
ANISOU  250  CD1 TYR B  30     7624   8823   9425   -212    885   -844       C  
ATOM    251  CD2 TYR B  30      42.341  -0.339 -15.478  1.00 68.32           C  
ANISOU  251  CD2 TYR B  30     7903   8735   9319    123    815   -755       C  
ATOM    252  CE1 TYR B  30      43.137   2.020 -16.699  1.00 61.21           C  
ANISOU  252  CE1 TYR B  30     6965   7812   8479   -284   1062   -797       C  
ATOM    253  CE2 TYR B  30      41.890  -0.022 -16.772  1.00 64.21           C  
ANISOU  253  CE2 TYR B  30     7575   8097   8723     43    971   -743       C  
ATOM    254  CZ  TYR B  30      42.296   1.160 -17.368  1.00 62.00           C  
ANISOU  254  CZ  TYR B  30     7280   7815   8460   -146   1092   -751       C  
ATOM    255  OH  TYR B  30      41.854   1.479 -18.632  1.00 66.09           O  
ANISOU  255  OH  TYR B  30     8010   8232   8868   -207   1236   -710       O  
ATOM    256  N   TYR B  31      41.629   0.568 -10.917  1.00 63.39           N  
ANISOU  256  N   TYR B  31     7108   8404   8573    125    179   -794       N  
ATOM    257  CA  TYR B  31      40.281   0.707 -10.360  1.00 64.92           C  
ANISOU  257  CA  TYR B  31     7508   8526   8633    130    111   -762       C  
ATOM    258  C   TYR B  31      40.076   2.090  -9.734  1.00 60.50           C  
ANISOU  258  C   TYR B  31     6960   7986   8040    -17     42   -884       C  
ATOM    259  O   TYR B  31      39.085   2.781 -10.035  1.00 53.69           O  
ANISOU  259  O   TYR B  31     6275   6987   7139    -78     85   -899       O  
ATOM    260  CB  TYR B  31      40.008  -0.384  -9.324  1.00 62.09           C  
ANISOU  260  CB  TYR B  31     7155   8256   8179    298     -7   -661       C  
ATOM    261  CG  TYR B  31      39.797  -1.759  -9.907  1.00 65.65           C  
ANISOU  261  CG  TYR B  31     7694   8593   8657    437     66   -538       C  
ATOM    262  CD1 TYR B  31      40.887  -2.581 -10.191  1.00 68.50           C  
ANISOU  262  CD1 TYR B  31     7919   8988   9121    572     91   -510       C  
ATOM    263  CD2 TYR B  31      38.513  -2.253 -10.162  1.00 60.37           C  
ANISOU  263  CD2 TYR B  31     7233   7782   7923    436    109   -464       C  
ATOM    264  CE1 TYR B  31      40.716  -3.833 -10.712  1.00 67.27           C  
ANISOU  264  CE1 TYR B  31     7872   8687   9001    709    161   -424       C  
ATOM    265  CE2 TYR B  31      38.339  -3.523 -10.691  1.00 60.48           C  
ANISOU  265  CE2 TYR B  31     7344   7660   7975    533    170   -378       C  
ATOM    266  CZ  TYR B  31      39.445  -4.306 -10.959  1.00 65.90           C  
ANISOU  266  CZ  TYR B  31     7933   8343   8763    675    197   -363       C  
ATOM    267  OH  TYR B  31      39.305  -5.571 -11.481  1.00 74.57           O  
ANISOU  267  OH  TYR B  31     9155   9267   9912    785    263   -302       O  
ATOM    268  N   PHE B  32      41.009   2.514  -8.862  1.00 52.04           N  
ANISOU  268  N   PHE B  32     5699   7085   6988    -67    -77   -984       N  
ATOM    269  CA  PHE B  32      40.958   3.875  -8.332  1.00 57.65           C  
ANISOU  269  CA  PHE B  32     6430   7784   7691   -232   -138  -1144       C  
ATOM    270  C   PHE B  32      40.855   4.905  -9.453  1.00 65.31           C  
ANISOU  270  C   PHE B  32     7508   8531   8775   -403     16  -1180       C  
ATOM    271  O   PHE B  32      40.053   5.844  -9.380  1.00 70.02           O  
ANISOU  271  O   PHE B  32     8283   8980   9341   -464     23  -1240       O  
ATOM    272  CB  PHE B  32      42.195   4.156  -7.486  1.00 63.30           C  
ANISOU  272  CB  PHE B  32     6889   8720   8441   -304   -285  -1272       C  
ATOM    273  CG  PHE B  32      42.227   3.402  -6.191  1.00 68.25           C  
ANISOU  273  CG  PHE B  32     7448   9581   8903   -137   -475  -1243       C  
ATOM    274  CD1 PHE B  32      41.077   2.828  -5.676  1.00 67.64           C  
ANISOU  274  CD1 PHE B  32     7565   9485   8649      9   -490  -1135       C  
ATOM    275  CD2 PHE B  32      43.397   3.280  -5.484  1.00 66.60           C  
ANISOU  275  CD2 PHE B  32     6973   9628   8703   -131   -639  -1312       C  
ATOM    276  CE1 PHE B  32      41.105   2.138  -4.499  1.00 62.34           C  
ANISOU  276  CE1 PHE B  32     6860   9026   7801    155   -644  -1074       C  
ATOM    277  CE2 PHE B  32      43.429   2.590  -4.304  1.00 66.06           C  
ANISOU  277  CE2 PHE B  32     6866   9786   8449     42   -826  -1257       C  
ATOM    278  CZ  PHE B  32      42.288   2.015  -3.807  1.00 62.08           C  
ANISOU  278  CZ  PHE B  32     6592   9241   7754    185   -820  -1127       C  
ATOM    279  N   TYR B  33      41.660   4.733 -10.500  1.00 62.68           N  
ANISOU  279  N   TYR B  33     7076   8173   8568   -463    151  -1135       N  
ATOM    280  CA  TYR B  33      41.620   5.623 -11.648  1.00 64.02           C  
ANISOU  280  CA  TYR B  33     7366   8138   8819   -622    319  -1123       C  
ATOM    281  C   TYR B  33      40.199   5.801 -12.160  1.00 63.97           C  
ANISOU  281  C   TYR B  33     7654   7938   8715   -547    362  -1042       C  
ATOM    282  O   TYR B  33      39.796   6.909 -12.533  1.00 60.18           O  
ANISOU  282  O   TYR B  33     7336   7269   8260   -651    413  -1061       O  
ATOM    283  CB  TYR B  33      42.521   5.072 -12.756  1.00 63.12           C  
ANISOU  283  CB  TYR B  33     7123   8066   8794   -637    488  -1051       C  
ATOM    284  CG  TYR B  33      42.523   5.915 -13.997  1.00 61.33           C  
ANISOU  284  CG  TYR B  33     7037   7652   8614   -799    684  -1003       C  
ATOM    285  CD1 TYR B  33      43.045   7.221 -13.968  1.00 63.25           C  
ANISOU  285  CD1 TYR B  33     7261   7801   8971  -1053    725  -1078       C  
ATOM    286  CD2 TYR B  33      42.025   5.417 -15.208  1.00 58.42           C  
ANISOU  286  CD2 TYR B  33     6838   7195   8165   -711    828   -880       C  
ATOM    287  CE1 TYR B  33      43.059   8.025 -15.109  1.00 67.03           C  
ANISOU  287  CE1 TYR B  33     7900   8083   9483  -1210    919   -995       C  
ATOM    288  CE2 TYR B  33      42.041   6.211 -16.369  1.00 65.87           C  
ANISOU  288  CE2 TYR B  33     7933   7984   9109   -851   1008   -808       C  
ATOM    289  CZ  TYR B  33      42.556   7.517 -16.305  1.00 73.58           C  
ANISOU  289  CZ  TYR B  33     8903   8853  10202  -1096   1060   -847       C  
ATOM    290  OH  TYR B  33      42.577   8.314 -17.432  1.00 81.73           O  
ANISOU  290  OH  TYR B  33    10115   9711  11227  -1239   1249   -738       O  
ATOM    291  N   HIS B  34      39.422   4.723 -12.193  1.00 63.48           N  
ANISOU  291  N   HIS B  34     7657   7913   8550   -366    339   -949       N  
ATOM    292  CA  HIS B  34      38.055   4.866 -12.678  1.00 60.10           C  
ANISOU  292  CA  HIS B  34     7455   7344   8035   -301    361   -884       C  
ATOM    293  C   HIS B  34      37.201   5.609 -11.661  1.00 55.04           C  
ANISOU  293  C   HIS B  34     6892   6686   7336   -279    253   -964       C  
ATOM    294  O   HIS B  34      36.510   6.576 -12.009  1.00 54.07           O  
ANISOU  294  O   HIS B  34     6928   6402   7215   -299    280   -976       O  
ATOM    295  CB  HIS B  34      37.430   3.505 -12.968  1.00 56.85           C  
ANISOU  295  CB  HIS B  34     7079   6975   7546   -155    362   -785       C  
ATOM    296  CG  HIS B  34      37.868   2.874 -14.245  1.00 61.33           C  
ANISOU  296  CG  HIS B  34     7664   7503   8136   -150    492   -724       C  
ATOM    297  CD2 HIS B  34      37.221   2.716 -15.423  1.00 62.18           C  
ANISOU  297  CD2 HIS B  34     7932   7514   8179   -134    569   -665       C  
ATOM    298  ND1 HIS B  34      39.080   2.227 -14.379  1.00 67.93           N  
ANISOU  298  ND1 HIS B  34     8334   8429   9046   -134    550   -734       N  
ATOM    299  CE1 HIS B  34      39.177   1.731 -15.599  1.00 66.44           C  
ANISOU  299  CE1 HIS B  34     8217   8188   8839   -112    682   -695       C  
ATOM    300  NE2 HIS B  34      38.058   2.007 -16.249  1.00 65.69           N  
ANISOU  300  NE2 HIS B  34     8330   7983   8647   -121    687   -655       N  
ATOM    301  N   GLY B  35      37.213   5.146 -10.401  1.00 48.60           N  
ANISOU  301  N   GLY B  35     5977   6037   6452   -213    137  -1012       N  
ATOM    302  CA  GLY B  35      36.302   5.688  -9.405  1.00 59.83           C  
ANISOU  302  CA  GLY B  35     7475   7481   7777   -161     58  -1093       C  
ATOM    303  C   GLY B  35      36.556   7.145  -9.056  1.00 64.28           C  
ANISOU  303  C   GLY B  35     8090   7937   8397   -275     36  -1260       C  
ATOM    304  O   GLY B  35      35.652   7.826  -8.559  1.00 65.68           O  
ANISOU  304  O   GLY B  35     8384   8057   8514   -214     13  -1340       O  
ATOM    305  N   LEU B  36      37.765   7.636  -9.321  1.00 56.31           N  
ANISOU  305  N   LEU B  36     6992   6889   7513   -442     53  -1324       N  
ATOM    306  CA  LEU B  36      38.148   9.013  -9.089  1.00 61.32           C  
ANISOU  306  CA  LEU B  36     7684   7375   8240   -606     42  -1489       C  
ATOM    307  C   LEU B  36      38.184   9.821 -10.387  1.00 70.72           C  
ANISOU  307  C   LEU B  36     9022   8287   9562   -718    188  -1413       C  
ATOM    308  O   LEU B  36      38.596  10.994 -10.379  1.00 73.91           O  
ANISOU  308  O   LEU B  36     9498   8503  10081   -892    209  -1523       O  
ATOM    309  CB  LEU B  36      39.497   9.051  -8.353  1.00 56.05           C  
ANISOU  309  CB  LEU B  36     6789   6882   7625   -757    -57  -1628       C  
ATOM    310  CG  LEU B  36      39.284   8.921  -6.839  1.00 62.10           C  
ANISOU  310  CG  LEU B  36     7512   7857   8226   -671   -231  -1771       C  
ATOM    311  CD1 LEU B  36      39.070   7.485  -6.418  1.00 63.10           C  
ANISOU  311  CD1 LEU B  36     7542   8229   8204   -474   -285  -1624       C  
ATOM    312  CD2 LEU B  36      40.426   9.500  -6.039  1.00 69.90           C  
ANISOU  312  CD2 LEU B  36     8337   8963   9259   -857   -364  -1987       C  
ATOM    313  N   SER B  37      37.739   9.230 -11.495  1.00 66.75           N  
ANISOU  313  N   SER B  37     8586   7744   9031   -629    288  -1227       N  
ATOM    314  CA  SER B  37      37.586   9.960 -12.751  1.00 65.75           C  
ANISOU  314  CA  SER B  37     8643   7371   8966   -694    420  -1118       C  
ATOM    315  C   SER B  37      36.155   9.987 -13.247  1.00 65.71           C  
ANISOU  315  C   SER B  37     8836   7269   8863   -500    416  -1014       C  
ATOM    316  O   SER B  37      35.701  11.004 -13.766  1.00 68.13           O  
ANISOU  316  O   SER B  37     9345   7337   9204   -498    458   -975       O  
ATOM    317  CB  SER B  37      38.475   9.355 -13.848  1.00 59.31           C  
ANISOU  317  CB  SER B  37     7736   6613   8187   -782    556   -995       C  
ATOM    318  OG  SER B  37      39.834   9.401 -13.463  1.00 60.87           O  
ANISOU  318  OG  SER B  37     7708   6920   8501   -963    568  -1090       O  
ATOM    319  N   TRP B  38      35.435   8.885 -13.112  1.00 68.07           N  
ANISOU  319  N   TRP B  38     9073   7744   9047   -338    364   -960       N  
ATOM    320  CA  TRP B  38      34.055   8.787 -13.579  1.00 63.61           C  
ANISOU  320  CA  TRP B  38     8633   7144   8392   -167    343   -872       C  
ATOM    321  C   TRP B  38      33.262   8.054 -12.511  1.00 58.85           C  
ANISOU  321  C   TRP B  38     7926   6734   7702    -38    251   -926       C  
ATOM    322  O   TRP B  38      32.709   6.973 -12.739  1.00 65.86           O  
ANISOU  322  O   TRP B  38     8761   7747   8516     34    238   -843       O  
ATOM    323  CB  TRP B  38      33.997   8.080 -14.931  1.00 61.49           C  
ANISOU  323  CB  TRP B  38     8409   6887   8069   -154    412   -718       C  
ATOM    324  CG  TRP B  38      34.975   8.612 -15.904  1.00 57.44           C  
ANISOU  324  CG  TRP B  38     7968   6244   7613   -302    538   -654       C  
ATOM    325  CD1 TRP B  38      34.834   9.730 -16.689  1.00 60.46           C  
ANISOU  325  CD1 TRP B  38     8555   6405   8013   -335    601   -570       C  
ATOM    326  CD2 TRP B  38      36.258   8.066 -16.210  1.00 57.16           C  
ANISOU  326  CD2 TRP B  38     7798   6294   7624   -433    637   -652       C  
ATOM    327  CE2 TRP B  38      36.848   8.900 -17.193  1.00 62.36           C  
ANISOU  327  CE2 TRP B  38     8576   6797   8322   -571    779   -569       C  
ATOM    328  CE3 TRP B  38      36.969   6.957 -15.756  1.00 56.10           C  
ANISOU  328  CE3 TRP B  38     7454   6355   7507   -433    627   -701       C  
ATOM    329  NE1 TRP B  38      35.958   9.905 -17.473  1.00 61.20           N  
ANISOU  329  NE1 TRP B  38     8657   6447   8151   -511    751   -507       N  
ATOM    330  CZ2 TRP B  38      38.118   8.647 -17.726  1.00 60.84           C  
ANISOU  330  CZ2 TRP B  38     8265   6670   8182   -721    929   -551       C  
ATOM    331  CZ3 TRP B  38      38.224   6.710 -16.282  1.00 58.60           C  
ANISOU  331  CZ3 TRP B  38     7652   6726   7887   -546    753   -692       C  
ATOM    332  CH2 TRP B  38      38.785   7.549 -17.268  1.00 55.40           C  
ANISOU  332  CH2 TRP B  38     7336   6194   7517   -696    912   -624       C  
ATOM    333  N   PRO B  39      33.196   8.625 -11.320  1.00 60.92           N  
ANISOU  333  N   PRO B  39     8167   7021   7961    -24    194  -1070       N  
ATOM    334  CA  PRO B  39      32.526   7.940 -10.210  1.00 55.73           C  
ANISOU  334  CA  PRO B  39     7411   6575   7190     84    132  -1112       C  
ATOM    335  C   PRO B  39      31.095   7.509 -10.538  1.00 56.67           C  
ANISOU  335  C   PRO B  39     7545   6749   7240    231    137  -1021       C  
ATOM    336  O   PRO B  39      30.680   6.413 -10.150  1.00 59.78           O  
ANISOU  336  O   PRO B  39     7838   7320   7555    263    124   -963       O  
ATOM    337  CB  PRO B  39      32.554   8.997  -9.095  1.00 48.67           C  
ANISOU  337  CB  PRO B  39     6555   5650   6286     89     91  -1308       C  
ATOM    338  CG  PRO B  39      33.398  10.143  -9.593  1.00 48.54           C  
ANISOU  338  CG  PRO B  39     6645   5386   6414    -54    119  -1375       C  
ATOM    339  CD  PRO B  39      33.368  10.067 -11.060  1.00 61.31           C  
ANISOU  339  CD  PRO B  39     8340   6863   8093    -73    197  -1196       C  
ATOM    340  N   GLN B  40      30.334   8.330 -11.260  1.00 49.30           N  
ANISOU  340  N   GLN B  40     6728   5666   6339    317    149   -997       N  
ATOM    341  CA  GLN B  40      28.957   7.989 -11.556  1.00 49.48           C  
ANISOU  341  CA  GLN B  40     6718   5777   6304    460    130   -927       C  
ATOM    342  C   GLN B  40      28.814   6.763 -12.447  1.00 60.35           C  
ANISOU  342  C   GLN B  40     8042   7240   7648    411    127   -792       C  
ATOM    343  O   GLN B  40      27.695   6.264 -12.580  1.00 67.93           O  
ANISOU  343  O   GLN B  40     8930   8319   8562    486     98   -748       O  
ATOM    344  CB  GLN B  40      28.257   9.175 -12.219  1.00 52.73           C  
ANISOU  344  CB  GLN B  40     7266   6008   6761    594    121   -917       C  
ATOM    345  CG  GLN B  40      28.099  10.394 -11.326  1.00 57.47           C  
ANISOU  345  CG  GLN B  40     7941   6495   7401    689    126  -1076       C  
ATOM    346  CD  GLN B  40      29.325  11.334 -11.339  1.00 65.26           C  
ANISOU  346  CD  GLN B  40     9078   7229   8489    543    155  -1151       C  
ATOM    347  NE2 GLN B  40      29.277  12.384 -10.513  1.00 64.18           N  
ANISOU  347  NE2 GLN B  40     9029   6961   8394    598    155  -1329       N  
ATOM    348  OE1 GLN B  40      30.298  11.110 -12.072  1.00 67.68           O  
ANISOU  348  OE1 GLN B  40     9413   7465   8838    375    186  -1063       O  
ATOM    349  N   LEU B  41      29.892   6.260 -13.054  1.00 61.91           N  
ANISOU  349  N   LEU B  41     8264   7388   7872    287    161   -742       N  
ATOM    350  CA  LEU B  41      29.727   5.341 -14.183  1.00 60.93           C  
ANISOU  350  CA  LEU B  41     8153   7285   7713    260    165   -640       C  
ATOM    351  C   LEU B  41      29.758   3.857 -13.810  1.00 62.71           C  
ANISOU  351  C   LEU B  41     8270   7642   7913    213    163   -617       C  
ATOM    352  O   LEU B  41      29.157   3.045 -14.525  1.00 62.87           O  
ANISOU  352  O   LEU B  41     8294   7696   7899    204    145   -568       O  
ATOM    353  CB  LEU B  41      30.796   5.616 -15.244  1.00 55.56           C  
ANISOU  353  CB  LEU B  41     7580   6471   7061    173    234   -597       C  
ATOM    354  CG  LEU B  41      30.640   6.980 -15.926  1.00 59.63           C  
ANISOU  354  CG  LEU B  41     8257   6812   7589    209    247   -560       C  
ATOM    355  CD1 LEU B  41      31.460   7.055 -17.210  1.00 60.12           C  
ANISOU  355  CD1 LEU B  41     8436   6779   7628    119    337   -471       C  
ATOM    356  CD2 LEU B  41      29.145   7.279 -16.196  1.00 54.00           C  
ANISOU  356  CD2 LEU B  41     7574   6128   6816    374    157   -522       C  
ATOM    357  N   SER B  42      30.432   3.458 -12.733  1.00 54.77           N  
ANISOU  357  N   SER B  42     7185   6705   6920    183    171   -649       N  
ATOM    358  CA  SER B  42      30.532   2.041 -12.400  1.00 55.19           C  
ANISOU  358  CA  SER B  42     7173   6837   6958    155    174   -595       C  
ATOM    359  C   SER B  42      29.462   1.639 -11.387  1.00 58.61           C  
ANISOU  359  C   SER B  42     7532   7407   7331    186    152   -576       C  
ATOM    360  O   SER B  42      29.162   2.386 -10.450  1.00 64.70           O  
ANISOU  360  O   SER B  42     8268   8256   8059    238    144   -635       O  
ATOM    361  CB  SER B  42      31.935   1.702 -11.894  1.00 49.76           C  
ANISOU  361  CB  SER B  42     6439   6161   6308    129    186   -604       C  
ATOM    362  OG  SER B  42      32.896   2.205 -12.813  1.00 53.67           O  
ANISOU  362  OG  SER B  42     6969   6556   6866     84    235   -628       O  
ATOM    363  N   TYR B  43      28.861   0.466 -11.607  1.00 53.89           N  
ANISOU  363  N   TYR B  43     6916   6834   6728    143    158   -502       N  
ATOM    364  CA  TYR B  43      27.773  -0.048 -10.783  1.00 54.10           C  
ANISOU  364  CA  TYR B  43     6858   6991   6705    129    169   -458       C  
ATOM    365  C   TYR B  43      28.125  -1.456 -10.323  1.00 60.04           C  
ANISOU  365  C   TYR B  43     7623   7727   7463     66    195   -356       C  
ATOM    366  O   TYR B  43      28.940  -2.141 -10.944  1.00 62.54           O  
ANISOU  366  O   TYR B  43     8010   7915   7838     46    196   -334       O  
ATOM    367  CB  TYR B  43      26.426  -0.027 -11.564  1.00 48.81           C  
ANISOU  367  CB  TYR B  43     6140   6360   6045    109    145   -464       C  
ATOM    368  CG  TYR B  43      25.743   1.313 -11.455  1.00 53.33           C  
ANISOU  368  CG  TYR B  43     6667   7003   6595    226    125   -535       C  
ATOM    369  CD1 TYR B  43      26.280   2.431 -12.089  1.00 58.54           C  
ANISOU  369  CD1 TYR B  43     7427   7540   7277    301     98   -587       C  
ATOM    370  CD2 TYR B  43      24.603   1.490 -10.658  1.00 55.04           C  
ANISOU  370  CD2 TYR B  43     6744   7396   6773    272    153   -548       C  
ATOM    371  CE1 TYR B  43      25.684   3.679 -11.966  1.00 65.67           C  
ANISOU  371  CE1 TYR B  43     8323   8454   8177    434     81   -648       C  
ATOM    372  CE2 TYR B  43      24.006   2.742 -10.529  1.00 60.59           C  
ANISOU  372  CE2 TYR B  43     7409   8145   7466    426    142   -630       C  
ATOM    373  CZ  TYR B  43      24.555   3.838 -11.185  1.00 68.14           C  
ANISOU  373  CZ  TYR B  43     8497   8935   8457    515     99   -680       C  
ATOM    374  OH  TYR B  43      23.992   5.096 -11.074  1.00 72.07           O  
ANISOU  374  OH  TYR B  43     8996   9422   8965    688     88   -756       O  
ATOM    375  N   ILE B  44      27.511  -1.899  -9.225  1.00 61.01           N  
ANISOU  375  N   ILE B  44     7688   7974   7519     46    230   -284       N  
ATOM    376  CA  ILE B  44      27.748  -3.254  -8.740  1.00 58.23           C  
ANISOU  376  CA  ILE B  44     7379   7576   7170    -12    261   -148       C  
ATOM    377  C   ILE B  44      26.432  -3.971  -8.488  1.00 60.31           C  
ANISOU  377  C   ILE B  44     7587   7904   7427   -133    321    -65       C  
ATOM    378  O   ILE B  44      25.360  -3.366  -8.389  1.00 67.82           O  
ANISOU  378  O   ILE B  44     8420   9004   8346   -147    343   -115       O  
ATOM    379  CB  ILE B  44      28.606  -3.285  -7.457  1.00 59.30           C  
ANISOU  379  CB  ILE B  44     7527   7800   7206     70    253    -86       C  
ATOM    380  CG1 ILE B  44      27.914  -2.506  -6.335  1.00 65.12           C  
ANISOU  380  CG1 ILE B  44     8189   8760   7796    105    284   -117       C  
ATOM    381  CG2 ILE B  44      30.029  -2.776  -7.735  1.00 55.23           C  
ANISOU  381  CG2 ILE B  44     7029   7225   6730    155    188   -165       C  
ATOM    382  CD1 ILE B  44      28.469  -2.804  -4.967  1.00 69.22           C  
ANISOU  382  CD1 ILE B  44     8733   9409   8159    161    277    -26       C  
ATOM    383  N   ALA B  45      26.529  -5.290  -8.389  1.00 58.51           N  
ANISOU  383  N   ALA B  45     7437   7550   7243   -223    355     63       N  
ATOM    384  CA  ALA B  45      25.423  -6.123  -7.950  1.00 52.79           C  
ANISOU  384  CA  ALA B  45     6670   6866   6520   -382    435    177       C  
ATOM    385  C   ALA B  45      25.895  -6.896  -6.733  1.00 57.99           C  
ANISOU  385  C   ALA B  45     7420   7517   7097   -364    493    371       C  
ATOM    386  O   ALA B  45      26.892  -7.625  -6.809  1.00 62.02           O  
ANISOU  386  O   ALA B  45     8070   7839   7656   -305    462    445       O  
ATOM    387  CB  ALA B  45      24.958  -7.060  -9.062  1.00 53.64           C  
ANISOU  387  CB  ALA B  45     6824   6783   6772   -548    423    156       C  
ATOM    388  N   GLU B  46      25.204  -6.718  -5.609  1.00 57.56           N  
ANISOU  388  N   GLU B  46     7286   7681   6904   -390    580    456       N  
ATOM    389  CA  GLU B  46      25.598  -7.364  -4.368  1.00 63.37           C  
ANISOU  389  CA  GLU B  46     8121   8452   7503   -360    635    665       C  
ATOM    390  C   GLU B  46      24.403  -8.101  -3.784  1.00 64.14           C  
ANISOU  390  C   GLU B  46     8180   8622   7568   -558    790    832       C  
ATOM    391  O   GLU B  46      23.261  -7.885  -4.194  1.00 67.25           O  
ANISOU  391  O   GLU B  46     8412   9111   8027   -698    849    751       O  
ATOM    392  CB  GLU B  46      26.174  -6.359  -3.358  1.00 68.32           C  
ANISOU  392  CB  GLU B  46     8719   9318   7921   -177    596    612       C  
ATOM    393  CG  GLU B  46      25.291  -5.162  -3.064  1.00 72.80           C  
ANISOU  393  CG  GLU B  46     9126  10143   8390   -155    647    454       C  
ATOM    394  CD  GLU B  46      25.931  -4.203  -2.078  1.00 73.61           C  
ANISOU  394  CD  GLU B  46     9238  10445   8287     13    600    364       C  
ATOM    395  OE1 GLU B  46      25.230  -3.288  -1.577  1.00 68.89           O  
ANISOU  395  OE1 GLU B  46     8540  10063   7571     58    664    240       O  
ATOM    396  OE2 GLU B  46      27.141  -4.377  -1.807  1.00 82.24           O1-
ANISOU  396  OE2 GLU B  46    10430  11480   9337    107    493    402       O1-
ATOM    397  N   ASP B  47      24.690  -8.999  -2.835  1.00 59.99           N  
ANISOU  397  N   ASP B  47     7799   8052   6942   -572    856   1082       N  
ATOM    398  CA  ASP B  47      23.720  -9.918  -2.261  1.00 62.26           C  
ANISOU  398  CA  ASP B  47     8102   8345   7210   -794   1028   1302       C  
ATOM    399  C   ASP B  47      23.440  -9.524  -0.816  1.00 74.08           C  
ANISOU  399  C   ASP B  47     9563  10175   8411   -735   1144   1424       C  
ATOM    400  O   ASP B  47      23.901  -8.478  -0.342  1.00 72.89           O  
ANISOU  400  O   ASP B  47     9363  10247   8085   -532   1075   1290       O  
ATOM    401  CB  ASP B  47      24.225 -11.356  -2.378  1.00 71.33           C  
ANISOU  401  CB  ASP B  47     9495   9125   8482   -866   1032   1523       C  
ATOM    402  CG  ASP B  47      25.379 -11.689  -1.404  1.00 88.85           C  
ANISOU  402  CG  ASP B  47    11910  11320  10527   -643    979   1733       C  
ATOM    403  OD1 ASP B  47      25.933 -10.789  -0.723  1.00 93.17           O  
ANISOU  403  OD1 ASP B  47    12403  12135  10861   -439    907   1671       O  
ATOM    404  OD2 ASP B  47      25.737 -12.888  -1.321  1.00 95.18           O1-
ANISOU  404  OD2 ASP B  47    12932  11822  11411   -668    998   1959       O1-
ATOM    405  N   GLU B  48      22.683 -10.374  -0.116  1.00 78.71           N  
ANISOU  405  N   GLU B  48    10185  10788   8932   -930   1330   1675       N  
ATOM    406  CA  GLU B  48      22.289 -10.089   1.259  1.00 82.14           C  
ANISOU  406  CA  GLU B  48    10592  11567   9052   -900   1483   1809       C  
ATOM    407  C   GLU B  48      23.460  -9.629   2.105  1.00 84.69           C  
ANISOU  407  C   GLU B  48    11055  12013   9110   -614   1357   1829       C  
ATOM    408  O   GLU B  48      23.294  -8.762   2.975  1.00 83.77           O  
ANISOU  408  O   GLU B  48    10862  12245   8722   -502   1404   1746       O  
ATOM    409  CB  GLU B  48      21.711 -11.351   1.896  1.00 97.35           C  
ANISOU  409  CB  GLU B  48    12641  13405  10942  -1139   1688   2165       C  
ATOM    410  CG  GLU B  48      20.855 -12.194   0.980  1.00114.38           C  
ANISOU  410  CG  GLU B  48    14735  15307  13417  -1465   1767   2187       C  
ATOM    411  CD  GLU B  48      19.875 -13.044   1.773  1.00136.00           C  
ANISOU  411  CD  GLU B  48    17480  18107  16088  -1762   2043   2487       C  
ATOM    412  OE1 GLU B  48      19.744 -14.258   1.479  1.00142.79           O  
ANISOU  412  OE1 GLU B  48    18504  18607  17145  -2003   2100   2685       O  
ATOM    413  OE2 GLU B  48      19.245 -12.490   2.707  1.00145.93           O1-
ANISOU  413  OE2 GLU B  48    18587  19768  17090  -1756   2218   2523       O1-
ATOM    414  N   ASN B  49      24.653 -10.181   1.853  1.00 81.32           N  
ANISOU  414  N   ASN B  49    10820  11319   8759   -485   1188   1914       N  
ATOM    415  CA  ASN B  49      25.810  -9.969   2.708  1.00 83.97           C  
ANISOU  415  CA  ASN B  49    11281  11774   8850   -231   1048   1979       C  
ATOM    416  C   ASN B  49      26.830  -8.999   2.110  1.00 82.41           C  
ANISOU  416  C   ASN B  49    11002  11580   8731    -33    824   1679       C  
ATOM    417  O   ASN B  49      28.005  -9.032   2.492  1.00 85.29           O  
ANISOU  417  O   ASN B  49    11454  11954   8998    164    659   1721       O  
ATOM    418  CB  ASN B  49      26.473 -11.310   3.030  1.00 85.33           C  
ANISOU  418  CB  ASN B  49    11712  11684   9027   -191   1020   2328       C  
ATOM    419  CG  ASN B  49      25.580 -12.211   3.821  1.00 91.25           C  
ANISOU  419  CG  ASN B  49    12581  12442   9646   -386   1250   2668       C  
ATOM    420  ND2 ASN B  49      25.656 -13.515   3.569  1.00 91.62           N  
ANISOU  420  ND2 ASN B  49    12836  12103   9873   -484   1293   2937       N  
ATOM    421  OD1 ASN B  49      24.815 -11.739   4.653  1.00101.34           O  
ANISOU  421  OD1 ASN B  49    13774  14064  10669   -451   1406   2687       O  
ATOM    422  N   GLY B  50      26.408  -8.119   1.210  1.00 78.02           N  
ANISOU  422  N   GLY B  50    10271  11031   8343    -81    815   1388       N  
ATOM    423  CA  GLY B  50      27.355  -7.197   0.613  1.00 74.51           C  
ANISOU  423  CA  GLY B  50     9765  10564   7982     71    631   1128       C  
ATOM    424  C   GLY B  50      28.468  -7.845  -0.184  1.00 76.49           C  
ANISOU  424  C   GLY B  50    10103  10519   8441    145    496   1165       C  
ATOM    425  O   GLY B  50      29.526  -7.230  -0.369  1.00 85.22           O  
ANISOU  425  O   GLY B  50    11169  11649   9562    291    343   1014       O  
ATOM    426  N   LYS B  51      28.262  -9.071  -0.675  1.00 72.05           N  
ANISOU  426  N   LYS B  51     9654   9672   8049     43    558   1346       N  
ATOM    427  CA  LYS B  51      29.235  -9.735  -1.534  1.00 69.35           C  
ANISOU  427  CA  LYS B  51     9399   9026   7924    129    458   1352       C  
ATOM    428  C   LYS B  51      28.905  -9.450  -2.986  1.00 65.38           C  
ANISOU  428  C   LYS B  51     8817   8360   7665     21    465   1124       C  
ATOM    429  O   LYS B  51      27.750  -9.586  -3.398  1.00 70.72           O  
ANISOU  429  O   LYS B  51     9453   9002   8415   -179    569   1100       O  
ATOM    430  CB  LYS B  51      29.256 -11.241  -1.270  1.00 78.46           C  
ANISOU  430  CB  LYS B  51    10765   9915   9131    102    518   1659       C  
ATOM    431  CG  LYS B  51      30.366 -11.584  -0.281  1.00 96.84           C  
ANISOU  431  CG  LYS B  51    13198  12310  11287    349    403   1859       C  
ATOM    432  CD  LYS B  51      30.265 -12.956   0.346  1.00108.52           C  
ANISOU  432  CD  LYS B  51    14919  13579  12736    346    476   2232       C  
ATOM    433  CE  LYS B  51      30.639 -14.024  -0.654  1.00110.29           C  
ANISOU  433  CE  LYS B  51    15287  13347  13272    361    474   2266       C  
ATOM    434  NZ  LYS B  51      31.467 -15.079  -0.021  1.00114.02           N1+
ANISOU  434  NZ  LYS B  51    15978  13633  13711    586    412   2580       N1+
ATOM    435  N   ILE B  52      29.913  -9.059  -3.759  1.00 58.56           N  
ANISOU  435  N   ILE B  52     7918   7419   6912    149    354    960       N  
ATOM    436  CA  ILE B  52      29.697  -8.627  -5.142  1.00 59.82           C  
ANISOU  436  CA  ILE B  52     8013   7467   7248     72    352    739       C  
ATOM    437  C   ILE B  52      29.515  -9.850  -6.031  1.00 64.43           C  
ANISOU  437  C   ILE B  52     8730   7724   8024    -23    400    791       C  
ATOM    438  O   ILE B  52      30.366 -10.739  -6.072  1.00 70.10           O  
ANISOU  438  O   ILE B  52     9576   8239   8821     93    376    891       O  
ATOM    439  CB  ILE B  52      30.856  -7.754  -5.647  1.00 61.17           C  
ANISOU  439  CB  ILE B  52     8105   7683   7456    220    249    559       C  
ATOM    440  CG1 ILE B  52      30.809  -6.382  -4.985  1.00 68.40           C  
ANISOU  440  CG1 ILE B  52     8895   8879   8215    252    207    437       C  
ATOM    441  CG2 ILE B  52      30.823  -7.636  -7.161  1.00 53.19           C  
ANISOU  441  CG2 ILE B  52     7090   6502   6616    160    261    391       C  
ATOM    442  CD1 ILE B  52      31.669  -5.373  -5.646  1.00 70.14           C  
ANISOU  442  CD1 ILE B  52     9031   9116   8502    314    135    238       C  
ATOM    443  N   VAL B  53      28.397  -9.907  -6.744  1.00 64.46           N  
ANISOU  443  N   VAL B  53     8704   7678   8108   -225    458    710       N  
ATOM    444  CA  VAL B  53      28.167 -10.969  -7.719  1.00 65.53           C  
ANISOU  444  CA  VAL B  53     8968   7506   8427   -348    486    691       C  
ATOM    445  C   VAL B  53      28.313 -10.476  -9.144  1.00 65.85           C  
ANISOU  445  C   VAL B  53     8970   7497   8554   -347    433    445       C  
ATOM    446  O   VAL B  53      28.398 -11.304 -10.065  1.00 63.84           O  
ANISOU  446  O   VAL B  53     8841   6984   8430   -402    439    380       O  
ATOM    447  CB  VAL B  53      26.789 -11.647  -7.518  1.00 67.16           C  
ANISOU  447  CB  VAL B  53     9180   7670   8668   -622    582    788       C  
ATOM    448  CG1 VAL B  53      26.743 -12.348  -6.152  1.00 70.04           C  
ANISOU  448  CG1 VAL B  53     9642   8029   8940   -631    666   1081       C  
ATOM    449  CG2 VAL B  53      25.616 -10.633  -7.668  1.00 56.72           C  
ANISOU  449  CG2 VAL B  53     7629   6636   7284   -750    593    656       C  
ATOM    450  N   GLY B  54      28.352  -9.162  -9.353  1.00 66.18           N  
ANISOU  450  N   GLY B  54     8866   7763   8517   -283    386    307       N  
ATOM    451  CA  GLY B  54      28.570  -8.594 -10.665  1.00 66.36           C  
ANISOU  451  CA  GLY B  54     8872   7756   8586   -264    342    110       C  
ATOM    452  C   GLY B  54      29.028  -7.164 -10.518  1.00 72.32           C  
ANISOU  452  C   GLY B  54     9509   8716   9253   -142    301     28       C  
ATOM    453  O   GLY B  54      28.887  -6.551  -9.456  1.00 78.09           O  
ANISOU  453  O   GLY B  54    10156   9630   9884   -103    299     81       O  
ATOM    454  N   TYR B  55      29.589  -6.635 -11.601  1.00 67.61           N  
ANISOU  454  N   TYR B  55     8924   8078   8686    -92    279   -108       N  
ATOM    455  CA  TYR B  55      29.986  -5.239 -11.649  1.00 62.41           C  
ANISOU  455  CA  TYR B  55     8181   7561   7971    -15    250   -192       C  
ATOM    456  C   TYR B  55      29.999  -4.804 -13.100  1.00 60.74           C  
ANISOU  456  C   TYR B  55     8011   7289   7777    -35    246   -313       C  
ATOM    457  O   TYR B  55      29.978  -5.627 -14.011  1.00 63.82           O  
ANISOU  457  O   TYR B  55     8497   7543   8209    -79    262   -352       O  
ATOM    458  CB  TYR B  55      31.365  -5.007 -11.021  1.00 56.01           C  
ANISOU  458  CB  TYR B  55     7337   6784   7159    115    239   -171       C  
ATOM    459  CG  TYR B  55      32.473  -5.638 -11.816  1.00 63.06           C  
ANISOU  459  CG  TYR B  55     8284   7533   8143    187    269   -200       C  
ATOM    460  CD1 TYR B  55      32.852  -6.952 -11.575  1.00 71.45           C  
ANISOU  460  CD1 TYR B  55     9423   8455   9268    246    286   -108       C  
ATOM    461  CD2 TYR B  55      33.134  -4.937 -12.834  1.00 67.76           C  
ANISOU  461  CD2 TYR B  55     8864   8121   8761    204    298   -314       C  
ATOM    462  CE1 TYR B  55      33.856  -7.559 -12.315  1.00 71.44           C  
ANISOU  462  CE1 TYR B  55     9465   8320   9358    348    329   -154       C  
ATOM    463  CE2 TYR B  55      34.158  -5.538 -13.579  1.00 62.33           C  
ANISOU  463  CE2 TYR B  55     8206   7329   8146    282    357   -352       C  
ATOM    464  CZ  TYR B  55      34.500  -6.848 -13.314  1.00 66.62           C  
ANISOU  464  CZ  TYR B  55     8811   7745   8759    366    371   -285       C  
ATOM    465  OH  TYR B  55      35.487  -7.458 -14.031  1.00 72.03           O  
ANISOU  465  OH  TYR B  55     9519   8326   9523    479    441   -341       O  
ATOM    466  N   VAL B  56      30.051  -3.497 -13.305  1.00 55.42           N  
ANISOU  466  N   VAL B  56     7290   6707   7060      1    227   -374       N  
ATOM    467  CA  VAL B  56      30.418  -2.934 -14.591  1.00 56.05           C  
ANISOU  467  CA  VAL B  56     7430   6734   7131      9    240   -453       C  
ATOM    468  C   VAL B  56      31.384  -1.804 -14.296  1.00 59.03           C  
ANISOU  468  C   VAL B  56     7762   7152   7513     68    258   -475       C  
ATOM    469  O   VAL B  56      31.023  -0.833 -13.618  1.00 59.77           O  
ANISOU  469  O   VAL B  56     7804   7327   7581     83    225   -484       O  
ATOM    470  CB  VAL B  56      29.207  -2.437 -15.408  1.00 61.71           C  
ANISOU  470  CB  VAL B  56     8164   7494   7788    -36    186   -490       C  
ATOM    471  CG1 VAL B  56      28.397  -1.386 -14.648  1.00 61.88           C  
ANISOU  471  CG1 VAL B  56     8088   7642   7781      1    144   -478       C  
ATOM    472  CG2 VAL B  56      29.664  -1.882 -16.763  1.00 63.40           C  
ANISOU  472  CG2 VAL B  56     8480   7658   7953    -17    204   -540       C  
ATOM    473  N   LEU B  57      32.617  -1.946 -14.764  1.00 56.02           N  
ANISOU  473  N   LEU B  57     7392   6716   7175     95    319   -497       N  
ATOM    474  CA  LEU B  57      33.636  -0.922 -14.601  1.00 54.49           C  
ANISOU  474  CA  LEU B  57     7135   6558   7010    104    346   -529       C  
ATOM    475  C   LEU B  57      33.693  -0.121 -15.904  1.00 59.35           C  
ANISOU  475  C   LEU B  57     7840   7117   7594     64    407   -557       C  
ATOM    476  O   LEU B  57      33.996  -0.673 -16.969  1.00 64.64           O  
ANISOU  476  O   LEU B  57     8582   7737   8243     63    478   -571       O  
ATOM    477  CB  LEU B  57      34.966  -1.579 -14.255  1.00 51.12           C  
ANISOU  477  CB  LEU B  57     6618   6148   6659    160    381   -526       C  
ATOM    478  CG  LEU B  57      36.160  -0.648 -14.127  1.00 57.79           C  
ANISOU  478  CG  LEU B  57     7348   7053   7559    136    411   -574       C  
ATOM    479  CD1 LEU B  57      35.932   0.289 -12.965  1.00 56.74           C  
ANISOU  479  CD1 LEU B  57     7156   7001   7402    105    318   -599       C  
ATOM    480  CD2 LEU B  57      37.429  -1.466 -13.948  1.00 55.41           C  
ANISOU  480  CD2 LEU B  57     6918   6797   7338    220    440   -571       C  
ATOM    481  N   ALA B  58      33.383   1.173 -15.828  1.00 57.34           N  
ANISOU  481  N   ALA B  58     7605   6858   7323     40    385   -563       N  
ATOM    482  CA  ALA B  58      33.149   1.982 -17.018  1.00 60.34           C  
ANISOU  482  CA  ALA B  58     8112   7169   7645     17    424   -544       C  
ATOM    483  C   ALA B  58      33.818   3.352 -16.906  1.00 62.14           C  
ANISOU  483  C   ALA B  58     8349   7336   7926    -36    469   -550       C  
ATOM    484  O   ALA B  58      34.077   3.859 -15.811  1.00 64.01           O  
ANISOU  484  O   ALA B  58     8500   7591   8229    -50    430   -599       O  
ATOM    485  CB  ALA B  58      31.645   2.158 -17.287  1.00 56.48           C  
ANISOU  485  CB  ALA B  58     7691   6694   7076     61    328   -521       C  
ATOM    486  N   LYS B  59      34.055   3.954 -18.075  1.00 62.64           N  
ANISOU  486  N   LYS B  59     8537   7320   7944    -75    554   -501       N  
ATOM    487  CA  LYS B  59      34.773   5.212 -18.232  1.00 61.50           C  
ANISOU  487  CA  LYS B  59     8437   7071   7859   -167    635   -481       C  
ATOM    488  C   LYS B  59      34.167   5.983 -19.400  1.00 67.82           C  
ANISOU  488  C   LYS B  59     9452   7764   8552   -147    659   -375       C  
ATOM    489  O   LYS B  59      33.353   5.460 -20.170  1.00 68.17           O  
ANISOU  489  O   LYS B  59     9584   7856   8462    -67    611   -333       O  
ATOM    490  CB  LYS B  59      36.260   4.980 -18.535  1.00 64.95           C  
ANISOU  490  CB  LYS B  59     8772   7543   8362   -273    783   -498       C  
ATOM    491  CG  LYS B  59      36.460   4.738 -20.031  1.00 73.17           C  
ANISOU  491  CG  LYS B  59     9940   8576   9284   -285    920   -425       C  
ATOM    492  CD  LYS B  59      37.881   4.777 -20.511  1.00 84.79           C  
ANISOU  492  CD  LYS B  59    11319  10087  10812   -397   1115   -426       C  
ATOM    493  CE  LYS B  59      38.802   3.905 -19.708  1.00 92.36           C  
ANISOU  493  CE  LYS B  59    12021  11175  11897   -376   1117   -525       C  
ATOM    494  NZ  LYS B  59      40.194   4.077 -20.248  1.00102.35           N1+
ANISOU  494  NZ  LYS B  59    13154  12505  13230   -488   1324   -529       N1+
ATOM    495  N   MET B  60      34.591   7.232 -19.548  1.00 66.56           N  
ANISOU  495  N   MET B  60     9387   7454   8447   -228    728   -327       N  
ATOM    496  CA  MET B  60      34.455   7.926 -20.816  1.00 67.03           C  
ANISOU  496  CA  MET B  60     9670   7401   8398   -236    806   -183       C  
ATOM    497  C   MET B  60      35.758   7.802 -21.591  1.00 76.39           C  
ANISOU  497  C   MET B  60    10843   8606   9574   -389   1014   -143       C  
ATOM    498  O   MET B  60      36.839   7.777 -21.002  1.00 73.59           O  
ANISOU  498  O   MET B  60    10313   8282   9368   -516   1096   -222       O  
ATOM    499  CB  MET B  60      34.099   9.389 -20.596  1.00 67.13           C  
ANISOU  499  CB  MET B  60     9836   7191   8480   -230    778   -125       C  
ATOM    500  CG  MET B  60      32.724   9.575 -19.984  1.00 67.09           C  
ANISOU  500  CG  MET B  60     9843   7183   8466    -36    595   -160       C  
ATOM    501  SD  MET B  60      31.407   8.976 -21.056  1.00 63.49           S  
ANISOU  501  SD  MET B  60     9475   6858   7792    150    475    -58       S  
ATOM    502  CE  MET B  60      31.371  10.228 -22.313  1.00 74.00           C  
ANISOU  502  CE  MET B  60    11119   7977   9020    183    533    161       C  
ATOM    503  N   GLU B  61      35.660   7.693 -22.913  1.00 88.55           N  
ANISOU  503  N   GLU B  61    12553  10164  10928   -370   1100    -28       N  
ATOM    504  CA  GLU B  61      36.872   7.620 -23.714  1.00 89.53           C  
ANISOU  504  CA  GLU B  61    12669  10330  11019   -510   1338     16       C  
ATOM    505  C   GLU B  61      37.609   8.947 -23.639  1.00 95.16           C  
ANISOU  505  C   GLU B  61    13433  10860  11863   -696   1471    103       C  
ATOM    506  O   GLU B  61      37.024  10.009 -23.887  1.00 89.76           O  
ANISOU  506  O   GLU B  61    12977   9978  11150   -683   1436    235       O  
ATOM    507  CB  GLU B  61      36.548   7.274 -25.161  1.00 92.88           C  
ANISOU  507  CB  GLU B  61    13299  10826  11167   -445   1405    118       C  
ATOM    508  CG  GLU B  61      37.761   7.339 -26.098  1.00102.97           C  
ANISOU  508  CG  GLU B  61    14598  12156  12370   -587   1695    184       C  
ATOM    509  CD  GLU B  61      38.945   6.516 -25.601  1.00110.10           C  
ANISOU  509  CD  GLU B  61    15200  13199  13434   -654   1823     28       C  
ATOM    510  OE1 GLU B  61      40.104   6.996 -25.712  1.00108.63           O  
ANISOU  510  OE1 GLU B  61    14908  13019  13349   -829   2042     60       O  
ATOM    511  OE2 GLU B  61      38.708   5.394 -25.089  1.00114.04           O1-
ANISOU  511  OE2 GLU B  61    15563  13799  13968   -531   1703   -119       O1-
ATOM    512  N   GLU B  62      38.910   8.873 -23.329  1.00101.10           N  
ANISOU  512  N   GLU B  62    13970  11675  12767   -871   1627     32       N  
ATOM    513  CA  GLU B  62      39.670  10.065 -22.961  1.00104.01           C  
ANISOU  513  CA  GLU B  62    14319  11875  13325  -1100   1726     58       C  
ATOM    514  C   GLU B  62      39.954  10.973 -24.162  1.00110.60           C  
ANISOU  514  C   GLU B  62    15402  12559  14061  -1241   1944    277       C  
ATOM    515  O   GLU B  62      39.887  12.202 -24.035  1.00115.91           O  
ANISOU  515  O   GLU B  62    16243  12963  14834  -1361   1959    367       O  
ATOM    516  CB  GLU B  62      40.967   9.657 -22.261  1.00101.11           C  
ANISOU  516  CB  GLU B  62    13596  11669  13152  -1250   1803    -95       C  
ATOM    517  CG  GLU B  62      40.804   9.215 -20.799  1.00 92.73           C  
ANISOU  517  CG  GLU B  62    12320  10689  12224  -1165   1574   -284       C  
ATOM    518  CD  GLU B  62      41.024   7.717 -20.615  1.00 94.70           C  
ANISOU  518  CD  GLU B  62    12356  11193  12433  -1005   1537   -377       C  
ATOM    519  OE1 GLU B  62      41.735   7.327 -19.661  1.00 92.50           O  
ANISOU  519  OE1 GLU B  62    11800  11050  12295  -1026   1473   -505       O  
ATOM    520  OE2 GLU B  62      40.479   6.926 -21.423  1.00 97.18           O1-
ANISOU  520  OE2 GLU B  62    12792  11562  12572   -853   1559   -325       O1-
ATOM    521  N   ASP B  63      40.291  10.409 -25.327  1.00113.84           N  
ANISOU  521  N   ASP B  63    15862  13123  14269  -1231   2128    367       N  
ATOM    522  CA  ASP B  63      40.465  11.197 -26.551  1.00124.82           C  
ANISOU  522  CA  ASP B  63    17529  14400  15497  -1342   2344    610       C  
ATOM    523  C   ASP B  63      39.540  10.653 -27.638  1.00121.59           C  
ANISOU  523  C   ASP B  63    17368  14091  14738  -1116   2288    714       C  
ATOM    524  O   ASP B  63      39.990  10.011 -28.595  1.00123.50           O  
ANISOU  524  O   ASP B  63    17622  14529  14774  -1115   2472    737       O  
ATOM    525  CB  ASP B  63      41.920  11.239 -27.033  1.00134.67           C  
ANISOU  525  CB  ASP B  63    18609  15760  16800  -1600   2680    638       C  
ATOM    526  CG  ASP B  63      42.467   9.868 -27.441  1.00139.67           C  
ANISOU  526  CG  ASP B  63    19022  16728  17319  -1500   2793    507       C  
ATOM    527  OD1 ASP B  63      41.891   8.836 -27.018  1.00143.19           O  
ANISOU  527  OD1 ASP B  63    19381  17292  17733  -1274   2587    349       O  
ATOM    528  OD2 ASP B  63      43.470   9.832 -28.197  1.00137.90           O1-
ANISOU  528  OD2 ASP B  63    18720  16637  17040  -1648   3104    564       O1-
ATOM    529  N   PRO B  64      38.238  10.905 -27.528  1.00116.12           N  
ANISOU  529  N   PRO B  64    16868  13287  13965   -917   2034    763       N  
ATOM    530  CA  PRO B  64      37.310  10.389 -28.540  1.00113.40           C  
ANISOU  530  CA  PRO B  64    16733  13070  13285   -710   1937    842       C  
ATOM    531  C   PRO B  64      37.679  10.909 -29.925  1.00118.12           C  
ANISOU  531  C   PRO B  64    17611  13657  13611   -787   2168   1091       C  
ATOM    532  O   PRO B  64      37.963  12.099 -30.103  1.00118.42           O  
ANISOU  532  O   PRO B  64    17831  13459  13704   -921   2293   1301       O  
ATOM    533  CB  PRO B  64      35.946  10.912 -28.070  1.00111.12           C  
ANISOU  533  CB  PRO B  64    16567  12632  13020   -514   1640    880       C  
ATOM    534  CG  PRO B  64      36.264  12.120 -27.241  1.00112.48           C  
ANISOU  534  CG  PRO B  64    16753  12510  13475   -642   1671    921       C  
ATOM    535  CD  PRO B  64      37.574  11.815 -26.575  1.00114.31           C  
ANISOU  535  CD  PRO B  64    16692  12807  13934   -877   1842    760       C  
ATOM    536  N   ASP B  65      37.717   9.987 -30.901  1.00118.74           N  
ANISOU  536  N   ASP B  65    17737  13989  13390   -713   2242   1061       N  
ATOM    537  CA  ASP B  65      38.002  10.373 -32.285  1.00117.95           C  
ANISOU  537  CA  ASP B  65    17926  13936  12954   -761   2464   1296       C  
ATOM    538  C   ASP B  65      36.865  11.211 -32.860  1.00130.01           C  
ANISOU  538  C   ASP B  65    19815  15324  14260   -601   2272   1549       C  
ATOM    539  O   ASP B  65      37.094  12.149 -33.631  1.00129.35           O  
ANISOU  539  O   ASP B  65    20016  15111  14019   -679   2440   1841       O  
ATOM    540  CB  ASP B  65      38.254   9.127 -33.145  1.00100.53           C  
ANISOU  540  CB  ASP B  65    15691  12049  10457   -693   2570   1153       C  
ATOM    541  N   ASP B  66      35.631  10.898 -32.477  1.00142.73           N  
ANISOU  541  N   ASP B  66    21409  16959  15864   -373   1923   1454       N  
ATOM    542  CA  ASP B  66      34.452  11.671 -32.794  1.00146.69           C  
ANISOU  542  CA  ASP B  66    22174  17340  16223   -171   1683   1659       C  
ATOM    543  C   ASP B  66      33.839  12.195 -31.484  1.00139.50           C  
ANISOU  543  C   ASP B  66    21123  16207  15674    -94   1469   1580       C  
ATOM    544  O   ASP B  66      34.587  12.593 -30.566  1.00138.94           O  
ANISOU  544  O   ASP B  66    20902  15956  15933   -271   1596   1507       O  
ATOM    545  CB  ASP B  66      33.512  10.805 -33.631  1.00155.01           C  
ANISOU  545  CB  ASP B  66    23307  18683  16906     35   1466   1601       C  
ATOM    546  CG  ASP B  66      33.252   9.405 -33.017  1.00161.54           C  
ANISOU  546  CG  ASP B  66    23818  19720  17839     67   1321   1244       C  
ATOM    547  OD1 ASP B  66      33.794   9.080 -31.928  1.00161.21           O  
ANISOU  547  OD1 ASP B  66    23499  19614  18138    -41   1384   1061       O  
ATOM    548  OD2 ASP B  66      32.489   8.624 -33.631  1.00164.57           O1-
ANISOU  548  OD2 ASP B  66    24243  20330  17957    196   1135   1151       O1-
ATOM    549  N   VAL B  67      32.509  12.187 -31.401  1.00121.37           N  
ANISOU  549  N   VAL B  67    18859  13949  13308    164   1152   1578       N  
ATOM    550  CA  VAL B  67      31.702  12.504 -30.225  1.00103.50           C  
ANISOU  550  CA  VAL B  67    16442  11555  11327    297    928   1470       C  
ATOM    551  C   VAL B  67      32.206  11.929 -28.905  1.00 95.77           C  
ANISOU  551  C   VAL B  67    15122  10589  10676    160    965   1187       C  
ATOM    552  O   VAL B  67      32.904  10.907 -28.897  1.00 90.45           O  
ANISOU  552  O   VAL B  67    14272  10104   9992     28   1079   1025       O  
ATOM    553  CB  VAL B  67      30.277  12.014 -30.461  1.00 91.85           C  
ANISOU  553  CB  VAL B  67    14930  10292   9677    567    602   1427       C  
ATOM    554  CG1 VAL B  67      29.693  12.714 -31.667  1.00 85.48           C  
ANISOU  554  CG1 VAL B  67    14459   9472   8548    748    511   1725       C  
ATOM    555  CG2 VAL B  67      30.311  10.500 -30.627  1.00 80.65           C  
ANISOU  555  CG2 VAL B  67    13307   9197   8139    506    570   1186       C  
ATOM    556  N   PRO B  68      31.804  12.505 -27.769  1.00 89.96           N  
ANISOU  556  N   PRO B  68    14292   9677  10213    220    855   1113       N  
ATOM    557  CA  PRO B  68      32.078  11.857 -26.484  1.00 84.83           C  
ANISOU  557  CA  PRO B  68    13322   9097   9813    136    837    844       C  
ATOM    558  C   PRO B  68      31.282  10.574 -26.336  1.00 81.30           C  
ANISOU  558  C   PRO B  68    12672   8940   9278    254    655    675       C  
ATOM    559  O   PRO B  68      30.106  10.491 -26.703  1.00 78.26           O  
ANISOU  559  O   PRO B  68    12330   8654   8751    453    450    717       O  
ATOM    560  CB  PRO B  68      31.641  12.899 -25.456  1.00 79.33           C  
ANISOU  560  CB  PRO B  68    12638   8147   9358    216    748    822       C  
ATOM    561  CG  PRO B  68      30.643  13.720 -26.191  1.00 79.12           C  
ANISOU  561  CG  PRO B  68    12874   8002   9186    453    619   1040       C  
ATOM    562  CD  PRO B  68      31.104  13.786 -27.600  1.00 84.16           C  
ANISOU  562  CD  PRO B  68    13756   8661   9558    386    751   1269       C  
ATOM    563  N   HIS B  69      31.942   9.559 -25.792  1.00 79.98           N  
ANISOU  563  N   HIS B  69    12276   8907   9205    125    728    488       N  
ATOM    564  CA  HIS B  69      31.301   8.264 -25.680  1.00 75.50           C  
ANISOU  564  CA  HIS B  69    11544   8573   8571    194    588    334       C  
ATOM    565  C   HIS B  69      31.928   7.509 -24.523  1.00 69.50           C  
ANISOU  565  C   HIS B  69    10526   7856   8025     90    638    146       C  
ATOM    566  O   HIS B  69      33.114   7.675 -24.217  1.00 68.32           O  
ANISOU  566  O   HIS B  69    10318   7640   7999    -55    810    124       O  
ATOM    567  CB  HIS B  69      31.401   7.481 -26.997  1.00 76.77           C  
ANISOU  567  CB  HIS B  69    11820   8900   8451    183    629    355       C  
ATOM    568  CG  HIS B  69      32.771   6.955 -27.299  1.00 74.53           C  
ANISOU  568  CG  HIS B  69    11504   8649   8163     21    881    303       C  
ATOM    569  CD2 HIS B  69      33.371   5.785 -26.967  1.00 71.51           C  
ANISOU  569  CD2 HIS B  69    10941   8374   7857    -42    952    123       C  
ATOM    570  ND1 HIS B  69      33.689   7.658 -28.047  1.00 77.37           N  
ANISOU  570  ND1 HIS B  69    12024   8932   8440    -83   1107    454       N  
ATOM    571  CE1 HIS B  69      34.799   6.948 -28.155  1.00 75.76           C  
ANISOU  571  CE1 HIS B  69    11705   8818   8264   -201   1312    353       C  
ATOM    572  NE2 HIS B  69      34.632   5.808 -27.509  1.00 72.23           N  
ANISOU  572  NE2 HIS B  69    11056   8472   7914   -159   1213    151       N  
ATOM    573  N   GLY B  70      31.099   6.715 -23.862  1.00 62.89           N  
ANISOU  573  N   GLY B  70     9527   7138   7229    165    479     24       N  
ATOM    574  CA  GLY B  70      31.561   5.871 -22.795  1.00 56.92           C  
ANISOU  574  CA  GLY B  70     8553   6438   6634     97    503   -124       C  
ATOM    575  C   GLY B  70      32.119   4.552 -23.301  1.00 65.77           C  
ANISOU  575  C   GLY B  70     9633   7672   7685     39    580   -206       C  
ATOM    576  O   GLY B  70      31.879   4.122 -24.430  1.00 71.53           O  
ANISOU  576  O   GLY B  70    10489   8471   8219     59    577   -192       O  
ATOM    577  N   HIS B  71      32.866   3.906 -22.415  1.00 65.98           N  
ANISOU  577  N   HIS B  71     9488   7715   7866    -16    638   -303       N  
ATOM    578  CA  HIS B  71      33.620   2.712 -22.737  1.00 65.50           C  
ANISOU  578  CA  HIS B  71     9378   7719   7791    -45    739   -387       C  
ATOM    579  C   HIS B  71      33.551   1.749 -21.565  1.00 66.17           C  
ANISOU  579  C   HIS B  71     9288   7834   8019    -25    666   -478       C  
ATOM    580  O   HIS B  71      33.852   2.133 -20.429  1.00 70.37           O  
ANISOU  580  O   HIS B  71     9691   8352   8693    -37    647   -481       O  
ATOM    581  CB  HIS B  71      35.082   3.048 -23.039  1.00 63.18           C  
ANISOU  581  CB  HIS B  71     9056   7408   7543   -127    954   -368       C  
ATOM    582  CG  HIS B  71      35.917   1.840 -23.302  1.00 67.94           C  
ANISOU  582  CG  HIS B  71     9581   8081   8153   -111   1072   -467       C  
ATOM    583  CD2 HIS B  71      36.746   1.132 -22.497  1.00 67.54           C  
ANISOU  583  CD2 HIS B  71     9336   8061   8267    -93   1111   -545       C  
ATOM    584  ND1 HIS B  71      35.922   1.201 -24.527  1.00 69.22           N  
ANISOU  584  ND1 HIS B  71     9883   8290   8128    -82   1154   -504       N  
ATOM    585  CE1 HIS B  71      36.733   0.159 -24.469  1.00 71.93           C  
ANISOU  585  CE1 HIS B  71    10125   8666   8538    -41   1259   -613       C  
ATOM    586  NE2 HIS B  71      37.247   0.096 -23.251  1.00 73.21           N  
ANISOU  586  NE2 HIS B  71    10078   8819   8920    -38   1229   -625       N  
ATOM    587  N   ILE B  72      33.174   0.505 -21.845  1.00 60.37           N  
ANISOU  587  N   ILE B  72     8570   7132   7237      0    628   -551       N  
ATOM    588  CA  ILE B  72      33.122  -0.547 -20.833  1.00 59.85           C  
ANISOU  588  CA  ILE B  72     8380   7063   7296     16    577   -606       C  
ATOM    589  C   ILE B  72      34.532  -1.111 -20.657  1.00 62.82           C  
ANISOU  589  C   ILE B  72     8673   7426   7770     39    717   -645       C  
ATOM    590  O   ILE B  72      35.038  -1.833 -21.524  1.00 66.98           O  
ANISOU  590  O   ILE B  72     9268   7939   8243     64    821   -708       O  
ATOM    591  CB  ILE B  72      32.144  -1.662 -21.231  1.00 56.51           C  
ANISOU  591  CB  ILE B  72     8027   6638   6808      7    485   -671       C  
ATOM    592  CG1 ILE B  72      30.713  -1.126 -21.353  1.00 57.42           C  
ANISOU  592  CG1 ILE B  72     8160   6815   6842     -6    328   -638       C  
ATOM    593  CG2 ILE B  72      32.271  -2.813 -20.270  1.00 44.18           C  
ANISOU  593  CG2 ILE B  72     6380   5026   5382     14    474   -699       C  
ATOM    594  CD1 ILE B  72      30.318  -0.182 -20.266  1.00 53.96           C  
ANISOU  594  CD1 ILE B  72     7609   6406   6490     22    271   -569       C  
ATOM    595  N   THR B  73      35.171  -0.800 -19.529  1.00 61.41           N  
ANISOU  595  N   THR B  73     8337   7269   7727     44    714   -622       N  
ATOM    596  CA  THR B  73      36.463  -1.420 -19.260  1.00 60.18           C  
ANISOU  596  CA  THR B  73     8054   7135   7676     95    812   -656       C  
ATOM    597  C   THR B  73      36.302  -2.898 -18.913  1.00 59.47           C  
ANISOU  597  C   THR B  73     7972   6991   7633    184    771   -686       C  
ATOM    598  O   THR B  73      37.086  -3.735 -19.366  1.00 59.05           O  
ANISOU  598  O   THR B  73     7915   6908   7613    266    874   -741       O  
ATOM    599  CB  THR B  73      37.190  -0.662 -18.149  1.00 60.73           C  
ANISOU  599  CB  THR B  73     7941   7271   7862     70    785   -634       C  
ATOM    600  CG2 THR B  73      38.496  -1.308 -17.824  1.00 54.76           C  
ANISOU  600  CG2 THR B  73     7010   6579   7219    144    853   -665       C  
ATOM    601  OG1 THR B  73      37.479   0.667 -18.609  1.00 75.82           O  
ANISOU  601  OG1 THR B  73     9872   9180   9757    -37    855   -615       O  
ATOM    602  N   SER B  74      35.276  -3.244 -18.137  1.00 55.69           N  
ANISOU  602  N   SER B  74     7514   6487   7159    171    639   -649       N  
ATOM    603  CA  SER B  74      35.083  -4.622 -17.710  1.00 48.57           C  
ANISOU  603  CA  SER B  74     6643   5494   6316    227    607   -646       C  
ATOM    604  C   SER B  74      33.642  -4.823 -17.269  1.00 51.08           C  
ANISOU  604  C   SER B  74     7014   5795   6599    144    491   -607       C  
ATOM    605  O   SER B  74      33.011  -3.897 -16.759  1.00 60.44           O  
ANISOU  605  O   SER B  74     8142   7075   7748     98    424   -567       O  
ATOM    606  CB  SER B  74      36.040  -4.983 -16.574  1.00 52.02           C  
ANISOU  606  CB  SER B  74     6937   5962   6866    333    598   -590       C  
ATOM    607  OG  SER B  74      36.258  -6.371 -16.551  1.00 66.27           O  
ANISOU  607  OG  SER B  74     8808   7633   8740    433    620   -589       O  
ATOM    608  N   LEU B  75      33.130  -6.031 -17.490  1.00 57.09           N  
ANISOU  608  N   LEU B  75     7879   6431   7380    122    479   -632       N  
ATOM    609  CA  LEU B  75      31.785  -6.405 -17.071  1.00 58.61           C  
ANISOU  609  CA  LEU B  75     8092   6611   7565     10    389   -596       C  
ATOM    610  C   LEU B  75      31.756  -7.897 -16.757  1.00 60.66           C  
ANISOU  610  C   LEU B  75     8443   6685   7921      5    404   -576       C  
ATOM    611  O   LEU B  75      32.083  -8.722 -17.614  1.00 65.42           O  
ANISOU  611  O   LEU B  75     9177   7133   8547     25    455   -676       O  
ATOM    612  CB  LEU B  75      30.734  -6.073 -18.148  1.00 59.26           C  
ANISOU  612  CB  LEU B  75     8239   6736   7542    -95    331   -679       C  
ATOM    613  CG  LEU B  75      29.349  -6.018 -17.493  1.00 61.36           C  
ANISOU  613  CG  LEU B  75     8423   7082   7809   -204    234   -627       C  
ATOM    614  CD1 LEU B  75      28.478  -4.881 -17.965  1.00 59.80           C  
ANISOU  614  CD1 LEU B  75     8168   7041   7511   -223    153   -644       C  
ATOM    615  CD2 LEU B  75      28.656  -7.314 -17.749  1.00 63.35           C  
ANISOU  615  CD2 LEU B  75     8755   7207   8108   -334    209   -675       C  
ATOM    616  N   ALA B  76      31.374  -8.244 -15.530  1.00 59.83           N  
ANISOU  616  N   ALA B  76     8289   6580   7864    -19    372   -445       N  
ATOM    617  CA  ALA B  76      31.313  -9.642 -15.146  1.00 64.65           C  
ANISOU  617  CA  ALA B  76     9013   6978   8573    -33    393   -383       C  
ATOM    618  C   ALA B  76      30.088  -9.892 -14.288  1.00 66.65           C  
ANISOU  618  C   ALA B  76     9236   7263   8826   -194    357   -270       C  
ATOM    619  O   ALA B  76      29.676  -9.044 -13.506  1.00 72.51           O  
ANISOU  619  O   ALA B  76     9841   8211   9497   -208    329   -198       O  
ATOM    620  CB  ALA B  76      32.580 -10.074 -14.397  1.00 68.22           C  
ANISOU  620  CB  ALA B  76     9456   7369   9095    169    428   -282       C  
ATOM    621  N   VAL B  77      29.510 -11.074 -14.449  1.00 66.71           N  
ANISOU  621  N   VAL B  77     9374   7056   8917   -326    372   -266       N  
ATOM    622  CA  VAL B  77      28.481 -11.587 -13.557  1.00 64.11           C  
ANISOU  622  CA  VAL B  77     9028   6713   8617   -499    377   -126       C  
ATOM    623  C   VAL B  77      28.857 -13.029 -13.230  1.00 68.88           C  
ANISOU  623  C   VAL B  77     9834   6987   9351   -491    434    -23       C  
ATOM    624  O   VAL B  77      28.947 -13.858 -14.138  1.00 74.04           O  
ANISOU  624  O   VAL B  77    10653   7383  10095   -534    448   -154       O  
ATOM    625  CB  VAL B  77      27.076 -11.520 -14.190  1.00 59.32           C  
ANISOU  625  CB  VAL B  77     8358   6179   8001   -751    330   -235       C  
ATOM    626  CG1 VAL B  77      26.029 -12.072 -13.235  1.00 60.29           C  
ANISOU  626  CG1 VAL B  77     8429   6310   8170   -956    369    -82       C  
ATOM    627  CG2 VAL B  77      26.731 -10.119 -14.620  1.00 49.94           C  
ANISOU  627  CG2 VAL B  77     7001   5281   6693   -710    263   -327       C  
ATOM    628  N   LYS B  78      29.100 -13.322 -11.951  1.00 70.14           N  
ANISOU  628  N   LYS B  78    10002   7142   9506   -420    466    208       N  
ATOM    629  CA  LYS B  78      29.392 -14.695 -11.551  1.00 72.13           C  
ANISOU  629  CA  LYS B  78    10472   7053   9880   -398    519    356       C  
ATOM    630  C   LYS B  78      28.326 -15.622 -12.112  1.00 82.07           C  
ANISOU  630  C   LYS B  78    11861   8063  11258   -698    550    289       C  
ATOM    631  O   LYS B  78      27.134 -15.313 -12.061  1.00 91.64           O  
ANISOU  631  O   LYS B  78    12944   9438  12436   -952    544    273       O  
ATOM    632  CB  LYS B  78      29.453 -14.818 -10.020  1.00 71.31           C  
ANISOU  632  CB  LYS B  78    10358   7031   9705   -337    542    653       C  
ATOM    633  CG  LYS B  78      30.333 -13.754  -9.354  1.00 71.03           C  
ANISOU  633  CG  LYS B  78    10155   7309   9522    -95    482    691       C  
ATOM    634  CD  LYS B  78      31.175 -14.317  -8.206  1.00 76.64           C  
ANISOU  634  CD  LYS B  78    10952   7968  10198    121    468    946       C  
ATOM    635  CE  LYS B  78      30.543 -14.086  -6.821  1.00 79.20           C  
ANISOU  635  CE  LYS B  78    11232   8515  10347     44    488   1173       C  
ATOM    636  NZ  LYS B  78      31.569 -13.906  -5.721  1.00 76.54           N1+
ANISOU  636  NZ  LYS B  78    10870   8344   9867    314    408   1341       N1+
ATOM    637  N   ARG B  79      28.770 -16.740 -12.694  1.00 81.21           N  
ANISOU  637  N   ARG B  79    11994   7564  11296   -664    580    224       N  
ATOM    638  CA  ARG B  79      27.846 -17.709 -13.274  1.00 69.11           C  
ANISOU  638  CA  ARG B  79    10618   5742   9897   -968    600    124       C  
ATOM    639  C   ARG B  79      26.819 -18.178 -12.255  1.00 72.74           C  
ANISOU  639  C   ARG B  79    11072   6168  10397  -1241    659    363       C  
ATOM    640  O   ARG B  79      25.696 -18.535 -12.625  1.00 79.37           O  
ANISOU  640  O   ARG B  79    11895   6951  11309  -1587    661    274       O  
ATOM    641  CB  ARG B  79      28.646 -18.890 -13.831  1.00 73.97           C  
ANISOU  641  CB  ARG B  79    11538   5892  10673   -833    642     41       C  
ATOM    642  CG  ARG B  79      27.831 -20.119 -14.222  1.00 81.94           C  
ANISOU  642  CG  ARG B  79    12783   6490  11859  -1146    674    -35       C  
ATOM    643  CD  ARG B  79      28.683 -21.226 -14.829  1.00 77.28           C  
ANISOU  643  CD  ARG B  79    12519   5416  11429   -966    720   -159       C  
ATOM    644  NE  ARG B  79      27.832 -22.200 -15.499  1.00 83.75           N  
ANISOU  644  NE  ARG B  79    13550   5875  12398  -1312    725   -345       N  
ATOM    645  CZ  ARG B  79      27.916 -22.476 -16.794  1.00 94.50           C  
ANISOU  645  CZ  ARG B  79    15040   7093  13775  -1338    694   -709       C  
ATOM    646  NH1 ARG B  79      28.827 -21.844 -17.534  1.00100.39           N1+
ANISOU  646  NH1 ARG B  79    15721   8035  14389  -1029    681   -891       N1+
ATOM    647  NH2 ARG B  79      27.105 -23.378 -17.344  1.00 96.49           N  
ANISOU  647  NH2 ARG B  79    15485   7014  14162  -1685    681   -897       N  
ATOM    648  N   SER B  80      27.178 -18.179 -10.964  1.00 77.70           N  
ANISOU  648  N   SER B  80    11703   6855  10966  -1102    709    668       N  
ATOM    649  CA  SER B  80      26.226 -18.583  -9.928  1.00 82.70           C  
ANISOU  649  CA  SER B  80    12332   7492  11599  -1358    799    927       C  
ATOM    650  C   SER B  80      25.009 -17.668  -9.910  1.00 81.88           C  
ANISOU  650  C   SER B  80    11919   7796  11394  -1606    793    846       C  
ATOM    651  O   SER B  80      23.916 -18.098  -9.523  1.00 82.08           O  
ANISOU  651  O   SER B  80    11901   7813  11471  -1932    876    949       O  
ATOM    652  CB  SER B  80      26.900 -18.610  -8.549  1.00 79.63           C  
ANISOU  652  CB  SER B  80    11997   7165  11094  -1121    840   1265       C  
ATOM    653  OG  SER B  80      27.516 -17.375  -8.233  1.00 82.40           O  
ANISOU  653  OG  SER B  80    12133   7921  11254   -861    765   1228       O  
ATOM    654  N   HIS B  81      25.170 -16.421 -10.358  1.00 74.07           N  
ANISOU  654  N   HIS B  81    10711   7155  10278  -1458    702    662       N  
ATOM    655  CA  HIS B  81      24.070 -15.479 -10.453  1.00 71.16           C  
ANISOU  655  CA  HIS B  81    10049   7166   9825  -1626    677    563       C  
ATOM    656  C   HIS B  81      23.731 -15.140 -11.903  1.00 73.12           C  
ANISOU  656  C   HIS B  81    10224   7450  10107  -1704    561    247       C  
ATOM    657  O   HIS B  81      23.115 -14.101 -12.179  1.00 68.26           O  
ANISOU  657  O   HIS B  81     9365   7173   9398  -1717    497    135       O  
ATOM    658  CB  HIS B  81      24.399 -14.241  -9.629  1.00 75.93           C  
ANISOU  658  CB  HIS B  81    10472   8146  10232  -1392    671    641       C  
ATOM    659  CG  HIS B  81      24.437 -14.516  -8.157  1.00 83.42           C  
ANISOU  659  CG  HIS B  81    11460   9146  11090  -1366    779    942       C  
ATOM    660  CD2 HIS B  81      23.657 -14.076  -7.144  1.00 85.16           C  
ANISOU  660  CD2 HIS B  81    11514   9665  11179  -1454    869   1079       C  
ATOM    661  ND1 HIS B  81      25.355 -15.371  -7.588  1.00 86.04           N  
ANISOU  661  ND1 HIS B  81    12037   9210  11444  -1222    809   1147       N  
ATOM    662  CE1 HIS B  81      25.147 -15.437  -6.285  1.00 88.96           C  
ANISOU  662  CE1 HIS B  81    12406   9717  11679  -1229    900   1413       C  
ATOM    663  NE2 HIS B  81      24.122 -14.659  -5.990  1.00 88.89           N  
ANISOU  663  NE2 HIS B  81    12149  10056  11568  -1376    951   1369       N  
ATOM    664  N   ARG B  82      24.111 -16.022 -12.826  1.00 81.41           N  
ANISOU  664  N   ARG B  82    11499   8152  11280  -1742    532    103       N  
ATOM    665  CA  ARG B  82      23.615 -16.003 -14.193  1.00 84.66           C  
ANISOU  665  CA  ARG B  82    11890   8562  11715  -1889    425   -194       C  
ATOM    666  C   ARG B  82      22.088 -16.005 -14.219  1.00 83.85           C  
ANISOU  666  C   ARG B  82    11566   8643  11648  -2250    395   -234       C  
ATOM    667  O   ARG B  82      21.423 -16.474 -13.285  1.00 86.66           O  
ANISOU  667  O   ARG B  82    11866   8985  12077  -2460    498    -40       O  
ATOM    668  CB  ARG B  82      24.149 -17.224 -14.945  1.00 96.93           C  
ANISOU  668  CB  ARG B  82    13764   9656  13409  -1920    434   -326       C  
ATOM    669  CG  ARG B  82      23.604 -17.429 -16.333  1.00107.71           C  
ANISOU  669  CG  ARG B  82    15158  10982  14784  -2112    321   -651       C  
ATOM    670  CD  ARG B  82      23.966 -18.818 -16.869  1.00111.36           C  
ANISOU  670  CD  ARG B  82    15967  10933  15411  -2196    357   -781       C  
ATOM    671  NE  ARG B  82      23.985 -19.840 -15.831  1.00106.04           N  
ANISOU  671  NE  ARG B  82    15462   9912  14914  -2291    484   -528       N  
ATOM    672  CZ  ARG B  82      23.312 -20.987 -15.905  1.00115.48           C  
ANISOU  672  CZ  ARG B  82    16825  10752  16299  -2635    514   -566       C  
ATOM    673  NH1 ARG B  82      23.375 -21.864 -14.927  1.00124.22           N1+
ANISOU  673  NH1 ARG B  82    18110  11530  17556  -2703    643   -291       N1+
ATOM    674  NH2 ARG B  82      22.581 -21.286 -16.966  1.00117.08           N  
ANISOU  674  NH2 ARG B  82    17034  10914  16539  -2923    408   -879       N  
ATOM    675  N   ARG B  83      21.531 -15.444 -15.298  1.00 80.29           N  
ANISOU  675  N   ARG B  83    10973   8399  11135  -2315    253   -479       N  
ATOM    676  CA  ARG B  83      20.132 -15.608 -15.687  1.00 79.65           C  
ANISOU  676  CA  ARG B  83    10684   8468  11110  -2667    174   -598       C  
ATOM    677  C   ARG B  83      19.180 -14.787 -14.828  1.00 78.18           C  
ANISOU  677  C   ARG B  83    10139   8692  10875  -2717    209   -455       C  
ATOM    678  O   ARG B  83      18.007 -15.141 -14.694  1.00 73.43           O  
ANISOU  678  O   ARG B  83     9333   8201  10367  -3043    213   -463       O  
ATOM    679  CB  ARG B  83      19.718 -17.088 -15.682  1.00 85.55           C  
ANISOU  679  CB  ARG B  83    11608   8832  12066  -3028    229   -613       C  
ATOM    680  CG  ARG B  83      18.802 -17.454 -16.834  1.00 96.12           C  
ANISOU  680  CG  ARG B  83    12875  10190  13454  -3345     67   -911       C  
ATOM    681  CD  ARG B  83      18.594 -18.946 -16.964  1.00106.72           C  
ANISOU  681  CD  ARG B  83    14466  11065  15016  -3695    115   -976       C  
ATOM    682  NE  ARG B  83      18.528 -19.334 -18.368  1.00115.84           N  
ANISOU  682  NE  ARG B  83    15757  12097  16158  -3808    -56  -1344       N  
ATOM    683  CZ  ARG B  83      18.484 -20.591 -18.807  1.00124.20           C  
ANISOU  683  CZ  ARG B  83    17096  12707  17389  -4078    -53  -1509       C  
ATOM    684  NH1 ARG B  83      18.500 -21.612 -17.952  1.00124.25           N1+
ANISOU  684  NH1 ARG B  83    17288  12306  17614  -4268    119  -1308       N1+
ATOM    685  NH2 ARG B  83      18.424 -20.823 -20.114  1.00127.86           N  
ANISOU  685  NH2 ARG B  83    17674  13117  17788  -4157   -224  -1877       N  
ATOM    686  N   LEU B  84      19.667 -13.697 -14.235  1.00 85.17           N  
ANISOU  686  N   LEU B  84    10933   9807  11620  -2406    243   -340       N  
ATOM    687  CA  LEU B  84      18.844 -12.736 -13.509  1.00 84.25           C  
ANISOU  687  CA  LEU B  84    10486  10097  11429  -2377    275   -252       C  
ATOM    688  C   LEU B  84      18.889 -11.353 -14.135  1.00 78.89           C  
ANISOU  688  C   LEU B  84     9665   9703  10608  -2112    140   -382       C  
ATOM    689  O   LEU B  84      18.423 -10.388 -13.523  1.00 72.19           O  
ANISOU  689  O   LEU B  84     8582   9162   9685  -1992    169   -321       O  
ATOM    690  CB  LEU B  84      19.276 -12.622 -12.050  1.00 85.67           C  
ANISOU  690  CB  LEU B  84    10695  10301  11555  -2250    451      9       C  
ATOM    691  CG  LEU B  84      19.026 -13.801 -11.125  1.00 86.67           C  
ANISOU  691  CG  LEU B  84    10919  10227  11785  -2500    619    225       C  
ATOM    692  CD1 LEU B  84      19.764 -13.565  -9.825  1.00 81.48           C  
ANISOU  692  CD1 LEU B  84    10354   9601  11003  -2276    750    469       C  
ATOM    693  CD2 LEU B  84      17.524 -14.013 -10.909  1.00 94.34           C  
ANISOU  693  CD2 LEU B  84    11589  11419  12836  -2851    679    234       C  
ATOM    694  N   GLY B  85      19.447 -11.230 -15.331  1.00 79.75           N  
ANISOU  694  N   GLY B  85     9928   9705  10670  -2010      9   -554       N  
ATOM    695  CA  GLY B  85      19.425  -9.960 -16.009  1.00 72.45           C  
ANISOU  695  CA  GLY B  85     8896   9024   9608  -1785   -118   -652       C  
ATOM    696  C   GLY B  85      20.371  -8.921 -15.469  1.00 65.03           C  
ANISOU  696  C   GLY B  85     8009   8130   8569  -1465    -54   -554       C  
ATOM    697  O   GLY B  85      20.261  -7.763 -15.862  1.00 63.84           O  
ANISOU  697  O   GLY B  85     7764   8174   8320  -1282   -137   -602       O  
ATOM    698  N   LEU B  86      21.328  -9.286 -14.617  1.00 60.82           N  
ANISOU  698  N   LEU B  86     7634   7416   8059  -1387     77   -421       N  
ATOM    699  CA  LEU B  86      22.141  -8.252 -13.992  1.00 57.91           C  
ANISOU  699  CA  LEU B  86     7272   7133   7599  -1118    122   -346       C  
ATOM    700  C   LEU B  86      23.008  -7.533 -15.019  1.00 61.02           C  
ANISOU  700  C   LEU B  86     7784   7481   7918   -930     45   -457       C  
ATOM    701  O   LEU B  86      23.261  -6.327 -14.890  1.00 63.45           O  
ANISOU  701  O   LEU B  86     8035   7925   8149   -746     31   -452       O  
ATOM    702  CB  LEU B  86      23.022  -8.844 -12.889  1.00 60.53           C  
ANISOU  702  CB  LEU B  86     7737   7308   7953  -1069    245   -183       C  
ATOM    703  CG  LEU B  86      22.414  -9.738 -11.819  1.00 61.31           C  
ANISOU  703  CG  LEU B  86     7801   7386   8107  -1254    358    -18       C  
ATOM    704  CD1 LEU B  86      23.516 -10.250 -10.913  1.00 57.66           C  
ANISOU  704  CD1 LEU B  86     7522   6753   7632  -1135    440    149       C  
ATOM    705  CD2 LEU B  86      21.417  -8.906 -11.079  1.00 61.61           C  
ANISOU  705  CD2 LEU B  86     7578   7757   8074  -1260    397     18       C  
ATOM    706  N   ALA B  87      23.497  -8.256 -16.034  1.00 63.51           N  
ANISOU  706  N   ALA B  87     8283   7596   8254   -979     12   -559       N  
ATOM    707  CA  ALA B  87      24.361  -7.626 -17.031  1.00 55.14           C  
ANISOU  707  CA  ALA B  87     7342   6506   7102   -814    -25   -651       C  
ATOM    708  C   ALA B  87      23.619  -6.514 -17.749  1.00 56.32           C  
ANISOU  708  C   ALA B  87     7376   6880   7143   -762   -144   -713       C  
ATOM    709  O   ALA B  87      24.167  -5.420 -17.941  1.00 58.46           O  
ANISOU  709  O   ALA B  87     7668   7209   7335   -584   -142   -695       O  
ATOM    710  CB  ALA B  87      24.872  -8.662 -18.031  1.00 59.64           C  
ANISOU  710  CB  ALA B  87     8125   6846   7689   -879    -25   -777       C  
ATOM    711  N   GLN B  88      22.353  -6.763 -18.137  1.00 53.54           N  
ANISOU  711  N   GLN B  88     6891   6657   6794   -918   -254   -780       N  
ATOM    712  CA  GLN B  88      21.559  -5.696 -18.738  1.00 62.20           C  
ANISOU  712  CA  GLN B  88     7850   7994   7790   -829   -389   -816       C  
ATOM    713  C   GLN B  88      21.328  -4.547 -17.745  1.00 65.70           C  
ANISOU  713  C   GLN B  88     8127   8594   8239   -663   -343   -706       C  
ATOM    714  O   GLN B  88      21.522  -3.370 -18.080  1.00 66.67           O  
ANISOU  714  O   GLN B  88     8272   8779   8280   -467   -383   -692       O  
ATOM    715  CB  GLN B  88      20.231  -6.244 -19.249  1.00 73.91           C  
ANISOU  715  CB  GLN B  88     9170   9624   9289  -1032   -533   -915       C  
ATOM    716  CG  GLN B  88      19.387  -5.130 -19.863  1.00 95.55           C  
ANISOU  716  CG  GLN B  88    11746  12637  11920   -894   -700   -936       C  
ATOM    717  CD  GLN B  88      18.155  -5.624 -20.620  1.00117.06           C  
ANISOU  717  CD  GLN B  88    14298  15550  14630  -1080   -895  -1064       C  
ATOM    718  NE2 GLN B  88      17.271  -4.685 -20.971  1.00124.02           N  
ANISOU  718  NE2 GLN B  88    14973  16710  15439   -938  -1052  -1059       N  
ATOM    719  OE1 GLN B  88      17.994  -6.826 -20.882  1.00119.02           O  
ANISOU  719  OE1 GLN B  88    14595  15690  14940  -1344   -913  -1172       O  
ATOM    720  N   LYS B  89      20.938  -4.874 -16.505  1.00 60.62           N  
ANISOU  720  N   LYS B  89     7344   8002   7687   -738   -246   -627       N  
ATOM    721  CA  LYS B  89      20.619  -3.843 -15.528  1.00 59.67           C  
ANISOU  721  CA  LYS B  89     7066   8050   7555   -582   -193   -559       C  
ATOM    722  C   LYS B  89      21.829  -3.003 -15.169  1.00 59.33           C  
ANISOU  722  C   LYS B  89     7177   7898   7468   -386   -125   -521       C  
ATOM    723  O   LYS B  89      21.732  -1.768 -15.101  1.00 58.81           O  
ANISOU  723  O   LYS B  89     7070   7915   7359   -204   -149   -528       O  
ATOM    724  CB  LYS B  89      20.006  -4.463 -14.276  1.00 57.42           C  
ANISOU  724  CB  LYS B  89     6621   7856   7339   -719    -75   -480       C  
ATOM    725  CG  LYS B  89      19.009  -5.500 -14.567  1.00 65.20           C  
ANISOU  725  CG  LYS B  89     7475   8893   8403   -985   -111   -511       C  
ATOM    726  CD  LYS B  89      17.952  -5.595 -13.491  1.00 70.27           C  
ANISOU  726  CD  LYS B  89     7845   9762   9092  -1084     -7   -440       C  
ATOM    727  CE  LYS B  89      17.081  -6.795 -13.721  1.00 83.24           C  
ANISOU  727  CE  LYS B  89     9370  11412  10845  -1420    -18   -459       C  
ATOM    728  NZ  LYS B  89      17.604  -7.798 -12.795  1.00100.48           N1+
ANISOU  728  NZ  LYS B  89    11711  13390  13076  -1568    153   -318       N1+
ATOM    729  N   LEU B  90      22.955  -3.660 -14.890  1.00 53.92           N  
ANISOU  729  N   LEU B  90     6658   7023   6806   -421    -43   -485       N  
ATOM    730  CA  LEU B  90      24.216  -2.946 -14.739  1.00 58.93           C  
ANISOU  730  CA  LEU B  90     7421   7561   7410   -269      2   -472       C  
ATOM    731  C   LEU B  90      24.497  -2.053 -15.950  1.00 61.86           C  
ANISOU  731  C   LEU B  90     7884   7901   7718   -168    -68   -528       C  
ATOM    732  O   LEU B  90      24.802  -0.857 -15.812  1.00 59.78           O  
ANISOU  732  O   LEU B  90     7635   7651   7429    -30    -63   -522       O  
ATOM    733  CB  LEU B  90      25.346  -3.957 -14.542  1.00 54.05           C  
ANISOU  733  CB  LEU B  90     6942   6758   6836   -315     73   -436       C  
ATOM    734  CG  LEU B  90      25.382  -4.710 -13.214  1.00 55.35           C  
ANISOU  734  CG  LEU B  90     7072   6923   7036   -366    151   -330       C  
ATOM    735  CD1 LEU B  90      26.394  -5.840 -13.290  1.00 54.90           C  
ANISOU  735  CD1 LEU B  90     7169   6652   7038   -387    194   -293       C  
ATOM    736  CD2 LEU B  90      25.701  -3.743 -12.057  1.00 51.90           C  
ANISOU  736  CD2 LEU B  90     6567   6612   6539   -237    187   -293       C  
ATOM    737  N   MET B  91      24.390  -2.625 -17.155  1.00 60.96           N  
ANISOU  737  N   MET B  91     7856   7737   7570   -243   -131   -585       N  
ATOM    738  CA  MET B  91      24.726  -1.864 -18.351  1.00 59.72           C  
ANISOU  738  CA  MET B  91     7821   7557   7312   -152   -182   -613       C  
ATOM    739  C   MET B  91      23.784  -0.681 -18.532  1.00 62.56           C  
ANISOU  739  C   MET B  91     8087   8062   7621    -29   -282   -592       C  
ATOM    740  O   MET B  91      24.226   0.422 -18.878  1.00 64.02           O  
ANISOU  740  O   MET B  91     8368   8200   7756    104   -275   -554       O  
ATOM    741  CB  MET B  91      24.690  -2.765 -19.577  1.00 64.30           C  
ANISOU  741  CB  MET B  91     8517   8089   7824   -255   -236   -699       C  
ATOM    742  CG  MET B  91      25.067  -2.055 -20.875  1.00 74.10           C  
ANISOU  742  CG  MET B  91     9915   9330   8912   -166   -272   -712       C  
ATOM    743  SD  MET B  91      26.807  -1.581 -20.966  1.00 78.15           S  
ANISOU  743  SD  MET B  91    10588   9685   9421    -84    -95   -669       S  
ATOM    744  CE  MET B  91      27.530  -3.194 -20.874  1.00 75.20           C  
ANISOU  744  CE  MET B  91    10273   9174   9124   -186     -2   -755       C  
ATOM    745  N   ASP B  92      22.485  -0.881 -18.276  1.00 61.45           N  
ANISOU  745  N   ASP B  92     7749   8092   7505    -67   -367   -609       N  
ATOM    746  CA  ASP B  92      21.530   0.217 -18.415  1.00 62.60           C  
ANISOU  746  CA  ASP B  92     7774   8394   7618     96   -469   -590       C  
ATOM    747  C   ASP B  92      21.838   1.356 -17.443  1.00 66.40           C  
ANISOU  747  C   ASP B  92     8247   8837   8144    264   -380   -548       C  
ATOM    748  O   ASP B  92      21.644   2.531 -17.778  1.00 71.14           O  
ANISOU  748  O   ASP B  92     8888   9432   8711    451   -433   -520       O  
ATOM    749  CB  ASP B  92      20.106  -0.300 -18.215  1.00 60.16           C  
ANISOU  749  CB  ASP B  92     7195   8312   7351     12   -558   -628       C  
ATOM    750  CG  ASP B  92      19.572  -1.008 -19.441  1.00 75.93           C  
ANISOU  750  CG  ASP B  92     9191  10382   9276   -115   -717   -700       C  
ATOM    751  OD1 ASP B  92      19.991  -0.636 -20.558  1.00 81.84           O  
ANISOU  751  OD1 ASP B  92    10128  11075   9894    -35   -797   -702       O  
ATOM    752  OD2 ASP B  92      18.757  -1.953 -19.297  1.00 83.35           O1-
ANISOU  752  OD2 ASP B  92     9953  11437  10280   -312   -759   -758       O1-
ATOM    753  N   GLN B  93      22.318   1.032 -16.232  1.00 58.81           N  
ANISOU  753  N   GLN B  93     7254   7841   7250    208   -252   -545       N  
ATOM    754  CA  GLN B  93      22.629   2.079 -15.267  1.00 52.76           C  
ANISOU  754  CA  GLN B  93     6491   7048   6507    350   -178   -544       C  
ATOM    755  C   GLN B  93      23.851   2.890 -15.703  1.00 62.30           C  
ANISOU  755  C   GLN B  93     7918   8052   7701    410   -148   -532       C  
ATOM    756  O   GLN B  93      23.825   4.127 -15.673  1.00 71.16           O  
ANISOU  756  O   GLN B  93     9095   9113   8828    560   -157   -535       O  
ATOM    757  CB  GLN B  93      22.842   1.493 -13.862  1.00 43.43           C  
ANISOU  757  CB  GLN B  93     5229   5916   5355    271    -65   -543       C  
ATOM    758  CG  GLN B  93      21.560   1.042 -13.145  1.00 50.96           C  
ANISOU  758  CG  GLN B  93     5946   7094   6323    232    -43   -541       C  
ATOM    759  CD  GLN B  93      20.503   2.158 -13.000  1.00 57.67           C  
ANISOU  759  CD  GLN B  93     6642   8098   7172    432    -75   -587       C  
ATOM    760  NE2 GLN B  93      19.242   1.761 -12.971  1.00 51.05           N  
ANISOU  760  NE2 GLN B  93     5558   7482   6356    394    -98   -591       N  
ATOM    761  OE1 GLN B  93      20.822   3.353 -12.941  1.00 70.99           O  
ANISOU  761  OE1 GLN B  93     8427   9696   8851    617    -79   -623       O  
ATOM    762  N   ALA B  94      24.935   2.230 -16.108  1.00 53.01           N  
ANISOU  762  N   ALA B  94     6865   6758   6519    293   -101   -520       N  
ATOM    763  CA  ALA B  94      26.095   2.995 -16.545  1.00 57.52           C  
ANISOU  763  CA  ALA B  94     7605   7165   7086    321    -51   -505       C  
ATOM    764  C   ALA B  94      25.766   3.830 -17.787  1.00 61.31           C  
ANISOU  764  C   ALA B  94     8205   7597   7493    412   -118   -458       C  
ATOM    765  O   ALA B  94      26.258   4.958 -17.952  1.00 61.62           O  
ANISOU  765  O   ALA B  94     8369   7503   7542    482    -84   -424       O  
ATOM    766  CB  ALA B  94      27.257   2.048 -16.813  1.00 52.74           C  
ANISOU  766  CB  ALA B  94     7068   6483   6490    200     23   -507       C  
ATOM    767  N   SER B  95      24.946   3.277 -18.678  1.00 49.91           N  
ANISOU  767  N   SER B  95     6738   6256   5968    402   -220   -449       N  
ATOM    768  CA  SER B  95      24.502   4.020 -19.839  1.00 51.44           C  
ANISOU  768  CA  SER B  95     7043   6450   6054    515   -316   -386       C  
ATOM    769  C   SER B  95      23.797   5.311 -19.432  1.00 57.20           C  
ANISOU  769  C   SER B  95     7737   7170   6825    717   -367   -349       C  
ATOM    770  O   SER B  95      24.182   6.406 -19.864  1.00 60.66           O  
ANISOU  770  O   SER B  95     8355   7449   7243    820   -349   -271       O  
ATOM    771  CB  SER B  95      23.592   3.134 -20.676  1.00 64.41           C  
ANISOU  771  CB  SER B  95     8617   8260   7598    465   -455   -417       C  
ATOM    772  OG  SER B  95      24.340   2.092 -21.265  1.00 68.47           O  
ANISOU  772  OG  SER B  95     9233   8725   8055    308   -400   -464       O  
ATOM    773  N   ARG B  96      22.772   5.207 -18.578  1.00 53.15           N  
ANISOU  773  N   ARG B  96     7002   6814   6378    781   -412   -403       N  
ATOM    774  CA  ARG B  96      22.076   6.408 -18.125  1.00 56.15           C  
ANISOU  774  CA  ARG B  96     7337   7189   6809   1011   -444   -395       C  
ATOM    775  C   ARG B  96      23.033   7.426 -17.499  1.00 56.90           C  
ANISOU  775  C   ARG B  96     7599   7042   6978   1052   -324   -406       C  
ATOM    776  O   ARG B  96      22.871   8.638 -17.691  1.00 61.31           O  
ANISOU  776  O   ARG B  96     8281   7456   7558   1236   -346   -364       O  
ATOM    777  CB  ARG B  96      20.971   6.042 -17.134  1.00 50.51           C  
ANISOU  777  CB  ARG B  96     6330   6706   6157   1050   -454   -473       C  
ATOM    778  CG  ARG B  96      20.215   7.285 -16.639  1.00 47.64           C  
ANISOU  778  CG  ARG B  96     5905   6347   5848   1331   -471   -493       C  
ATOM    779  CD  ARG B  96      19.052   6.964 -15.701  1.00 57.01           C  
ANISOU  779  CD  ARG B  96     6768   7809   7083   1387   -454   -573       C  
ATOM    780  NE  ARG B  96      18.356   8.189 -15.306  1.00 66.25           N  
ANISOU  780  NE  ARG B  96     7889   8978   8307   1701   -460   -609       N  
ATOM    781  CZ  ARG B  96      17.081   8.243 -14.954  1.00 72.04           C  
ANISOU  781  CZ  ARG B  96     8324   9975   9073   1861   -489   -655       C  
ATOM    782  NH1 ARG B  96      16.536   9.409 -14.615  1.00 71.93           N1+
ANISOU  782  NH1 ARG B  96     8290   9926   9115   2187   -482   -700       N1+
ATOM    783  NH2 ARG B  96      16.359   7.130 -14.946  1.00 76.55           N  
ANISOU  783  NH2 ARG B  96     8614  10837   9636   1692   -517   -663       N  
ATOM    784  N   ALA B  97      24.040   6.955 -16.756  1.00 49.64           N  
ANISOU  784  N   ALA B  97     6690   6068   6102    882   -207   -464       N  
ATOM    785  CA  ALA B  97      24.952   7.877 -16.084  1.00 51.59           C  
ANISOU  785  CA  ALA B  97     7061   6117   6424    884   -113   -508       C  
ATOM    786  C   ALA B  97      25.864   8.581 -17.073  1.00 63.13           C  
ANISOU  786  C   ALA B  97     8765   7346   7877    845    -79   -418       C  
ATOM    787  O   ALA B  97      26.159   9.780 -16.905  1.00 61.84           O  
ANISOU  787  O   ALA B  97     8745   6970   7781    912    -44   -421       O  
ATOM    788  CB  ALA B  97      25.801   7.145 -15.054  1.00 44.56           C  
ANISOU  788  CB  ALA B  97     6093   5274   5564    719    -28   -587       C  
ATOM    789  N   MET B  98      26.362   7.840 -18.078  1.00 62.78           N  
ANISOU  789  N   MET B  98     8778   7326   7751    721    -69   -346       N  
ATOM    790  CA  MET B  98      27.207   8.456 -19.099  1.00 61.92           C  
ANISOU  790  CA  MET B  98     8893   7030   7602    672     -6   -240       C  
ATOM    791  C   MET B  98      26.459   9.570 -19.809  1.00 63.53           C  
ANISOU  791  C   MET B  98     9255   7122   7761    868    -85   -121       C  
ATOM    792  O   MET B  98      27.055  10.586 -20.189  1.00 66.65           O  
ANISOU  792  O   MET B  98     9864   7278   8182    864    -14    -32       O  
ATOM    793  CB  MET B  98      27.677   7.415 -20.107  1.00 59.41           C  
ANISOU  793  CB  MET B  98     8604   6802   7166    547     21   -199       C  
ATOM    794  CG  MET B  98      28.491   6.286 -19.540  1.00 66.00           C  
ANISOU  794  CG  MET B  98     9312   7712   8053    389    100   -294       C  
ATOM    795  SD  MET B  98      28.569   4.919 -20.732  1.00 67.98           S  
ANISOU  795  SD  MET B  98     9592   8082   8157    310     97   -291       S  
ATOM    796  CE  MET B  98      29.733   3.821 -19.908  1.00 66.28           C  
ANISOU  796  CE  MET B  98     9253   7878   8054    177    213   -386       C  
ATOM    797  N   ILE B  99      25.145   9.396 -19.985  1.00 62.67           N  
ANISOU  797  N   ILE B  99     9036   7182   7592   1041   -234   -111       N  
ATOM    798  CA  ILE B  99      24.338  10.416 -20.638  1.00 63.86           C  
ANISOU  798  CA  ILE B  99     9311   7255   7697   1283   -340     13       C  
ATOM    799  C   ILE B  99      24.208  11.639 -19.748  1.00 66.25           C  
ANISOU  799  C   ILE B  99     9670   7346   8156   1437   -303    -30       C  
ATOM    800  O   ILE B  99      24.513  12.762 -20.164  1.00 68.35           O  
ANISOU  800  O   ILE B  99    10190   7332   8449   1518   -271     82       O  
ATOM    801  CB  ILE B  99      22.957   9.859 -21.013  1.00 58.27           C  
ANISOU  801  CB  ILE B  99     8409   6834   6897   1429   -529     13       C  
ATOM    802  CG1 ILE B  99      23.093   8.780 -22.073  1.00 55.72           C  
ANISOU  802  CG1 ILE B  99     8097   6676   6399   1278   -583     42       C  
ATOM    803  CG2 ILE B  99      22.073  10.963 -21.541  1.00 49.16           C  
ANISOU  803  CG2 ILE B  99     7348   5620   5712   1738   -661    140       C  
ATOM    804  CD1 ILE B  99      21.788   8.099 -22.350  1.00 56.57           C  
ANISOU  804  CD1 ILE B  99     7975   7085   6434   1352   -777      0       C  
ATOM    805  N   GLU B 100      23.742  11.443 -18.514  1.00 66.80           N  
ANISOU  805  N   GLU B 100     9524   7533   8322   1480   -295   -194       N  
ATOM    806  CA  GLU B 100      23.563  12.580 -17.614  1.00 74.29           C  
ANISOU  806  CA  GLU B 100    10530   8294   9404   1645   -256   -281       C  
ATOM    807  C   GLU B 100      24.873  13.326 -17.377  1.00 67.71           C  
ANISOU  807  C   GLU B 100     9929   7134   8663   1479   -124   -303       C  
ATOM    808  O   GLU B 100      24.900  14.559 -17.345  1.00 70.58           O  
ANISOU  808  O   GLU B 100    10502   7198   9117   1605   -103   -287       O  
ATOM    809  CB  GLU B 100      22.986  12.121 -16.277  1.00 81.72           C  
ANISOU  809  CB  GLU B 100    11201   9456  10391   1678   -235   -468       C  
ATOM    810  CG  GLU B 100      21.660  11.435 -16.373  1.00 92.15           C  
ANISOU  810  CG  GLU B 100    12248  11108  11656   1809   -342   -463       C  
ATOM    811  CD  GLU B 100      21.217  10.866 -15.042  1.00 96.03           C  
ANISOU  811  CD  GLU B 100    12479  11833  12175   1783   -274   -623       C  
ATOM    812  OE1 GLU B 100      22.103  10.501 -14.228  1.00 94.44           O  
ANISOU  812  OE1 GLU B 100    12297  11602  11982   1587   -170   -709       O  
ATOM    813  OE2 GLU B 100      19.983  10.786 -14.823  1.00100.77           O1-
ANISOU  813  OE2 GLU B 100    12845  12665  12778   1962   -326   -654       O1-
ATOM    814  N   ASN B 101      25.965  12.606 -17.192  1.00 63.23           N  
ANISOU  814  N   ASN B 101     9322   6612   8090   1198    -37   -348       N  
ATOM    815  CA  ASN B 101      27.138  13.272 -16.668  1.00 64.48           C  
ANISOU  815  CA  ASN B 101     9610   6526   8362   1026     76   -427       C  
ATOM    816  C   ASN B 101      28.090  13.732 -17.733  1.00 68.12           C  
ANISOU  816  C   ASN B 101    10301   6758   8824    873    157   -267       C  
ATOM    817  O   ASN B 101      28.852  14.676 -17.493  1.00 71.33           O  
ANISOU  817  O   ASN B 101    10869   6881   9353    764    242   -300       O  
ATOM    818  CB  ASN B 101      27.869  12.357 -15.703  1.00 67.75           C  
ANISOU  818  CB  ASN B 101     9828   7125   8787    824    122   -576       C  
ATOM    819  CG  ASN B 101      27.110  12.184 -14.436  1.00 68.84           C  
ANISOU  819  CG  ASN B 101     9794   7435   8928    947     84   -740       C  
ATOM    820  ND2 ASN B 101      26.370  11.086 -14.351  1.00 71.45           N  
ANISOU  820  ND2 ASN B 101     9919   8056   9171    987     37   -722       N  
ATOM    821  OD1 ASN B 101      27.142  13.050 -13.549  1.00 63.91           O  
ANISOU  821  OD1 ASN B 101     9228   6678   8376   1004    106   -888       O  
ATOM    822  N   PHE B 102      28.063  13.095 -18.901  1.00 71.25           N  
ANISOU  822  N   PHE B 102    10721   7273   9079    848    143   -106       N  
ATOM    823  CA  PHE B 102      29.038  13.376 -19.934  1.00 63.11           C  
ANISOU  823  CA  PHE B 102     9889   6083   8009    680    258     51       C  
ATOM    824  C   PHE B 102      28.434  13.505 -21.314  1.00 66.77           C  
ANISOU  824  C   PHE B 102    10527   6551   8294    824    197    277       C  
ATOM    825  O   PHE B 102      29.175  13.741 -22.277  1.00 72.38           O  
ANISOU  825  O   PHE B 102    11426   7149   8925    697    308    436       O  
ATOM    826  CB  PHE B 102      30.116  12.300 -19.901  1.00 55.45           C  
ANISOU  826  CB  PHE B 102     8762   5288   7019    429    356    -15       C  
ATOM    827  CG  PHE B 102      30.698  12.099 -18.526  1.00 55.24           C  
ANISOU  827  CG  PHE B 102     8549   5303   7135    311    380   -223       C  
ATOM    828  CD1 PHE B 102      31.496  13.080 -17.955  1.00 52.69           C  
ANISOU  828  CD1 PHE B 102     8305   4747   6968    176    456   -297       C  
ATOM    829  CD2 PHE B 102      30.400  10.965 -17.786  1.00 53.27           C  
ANISOU  829  CD2 PHE B 102     8062   5321   6857    332    315   -342       C  
ATOM    830  CE1 PHE B 102      32.022  12.912 -16.690  1.00 53.34           C  
ANISOU  830  CE1 PHE B 102     8217   4902   7148     73    448   -501       C  
ATOM    831  CE2 PHE B 102      30.933  10.781 -16.528  1.00 53.65           C  
ANISOU  831  CE2 PHE B 102     7959   5429   6996    243    323   -508       C  
ATOM    832  CZ  PHE B 102      31.742  11.765 -15.977  1.00 56.70           C  
ANISOU  832  CZ  PHE B 102     8412   5619   7511    121    378   -596       C  
ATOM    833  N   ASN B 103      27.113  13.425 -21.420  1.00 70.62           N  
ANISOU  833  N   ASN B 103    10951   7174   8708   1088     26    297       N  
ATOM    834  CA  ASN B 103      26.405  13.548 -22.690  1.00 81.42           C  
ANISOU  834  CA  ASN B 103    12461   8593   9881   1263    -86    503       C  
ATOM    835  C   ASN B 103      26.962  12.576 -23.729  1.00 79.22           C  
ANISOU  835  C   ASN B 103    12202   8500   9399   1087    -40    569       C  
ATOM    836  O   ASN B 103      27.155  12.919 -24.896  1.00 85.65           O  
ANISOU  836  O   ASN B 103    13253   9249  10039   1100    -16    771       O  
ATOM    837  CB  ASN B 103      26.424  14.987 -23.213  1.00 90.05           C  
ANISOU  837  CB  ASN B 103    13888   9329  10997   1397    -61    709       C  
ATOM    838  CG  ASN B 103      25.271  15.260 -24.168  1.00112.51           C  
ANISOU  838  CG  ASN B 103    16830  12255  13662   1709   -255    901       C  
ATOM    839  ND2 ASN B 103      25.342  16.368 -24.908  1.00122.33           N  
ANISOU  839  ND2 ASN B 103    18415  13202  14863   1829   -236   1149       N  
ATOM    840  OD1 ASN B 103      24.327  14.465 -24.246  1.00119.40           O  
ANISOU  840  OD1 ASN B 103    17470  13462  14436   1834   -427    832       O  
ATOM    841  N   ALA B 104      27.235  11.352 -23.289  1.00 72.42           N  
ANISOU  841  N   ALA B 104    11106   7861   8548    932    -17    399       N  
ATOM    842  CA  ALA B 104      27.671  10.307 -24.201  1.00 66.97           C  
ANISOU  842  CA  ALA B 104    10419   7353   7674    795     21    411       C  
ATOM    843  C   ALA B 104      26.644  10.109 -25.295  1.00 69.75           C  
ANISOU  843  C   ALA B 104    10837   7878   7786    963   -162    513       C  
ATOM    844  O   ALA B 104      25.438  10.134 -25.046  1.00 74.74           O  
ANISOU  844  O   ALA B 104    11339   8632   8429   1151   -355    484       O  
ATOM    845  CB  ALA B 104      27.879   8.987 -23.449  1.00 52.47           C  
ANISOU  845  CB  ALA B 104     8320   5706   5913    661     36    206       C  
ATOM    846  N   LYS B 105      27.124   9.907 -26.514  1.00 72.69           N  
ANISOU  846  N   LYS B 105    11398   8291   7928    894   -102    624       N  
ATOM    847  CA  LYS B 105      26.240   9.521 -27.601  1.00 73.17           C  
ANISOU  847  CA  LYS B 105    11515   8573   7712   1021   -294    685       C  
ATOM    848  C   LYS B 105      26.250   8.016 -27.867  1.00 77.30           C  
ANISOU  848  C   LYS B 105    11892   9348   8128    881   -324    495       C  
ATOM    849  O   LYS B 105      25.368   7.535 -28.589  1.00 84.31           O  
ANISOU  849  O   LYS B 105    12763  10456   8814    961   -525    475       O  
ATOM    850  CB  LYS B 105      26.605  10.287 -28.871  1.00 67.11           C  
ANISOU  850  CB  LYS B 105    11092   7713   6694   1066   -234    938       C  
ATOM    851  CG  LYS B 105      26.945  11.740 -28.623  1.00 69.87           C  
ANISOU  851  CG  LYS B 105    11645   7720   7182   1130   -128   1134       C  
ATOM    852  CD  LYS B 105      25.679  12.563 -28.481  1.00 80.98           C  
ANISOU  852  CD  LYS B 105    13065   9082   8621   1447   -364   1235       C  
ATOM    853  CE  LYS B 105      25.976  14.012 -28.120  1.00 87.67           C  
ANISOU  853  CE  LYS B 105    14135   9526   9651   1524   -259   1400       C  
ATOM    854  NZ  LYS B 105      24.718  14.827 -28.182  1.00 96.77           N1+
ANISOU  854  NZ  LYS B 105    15337  10632  10800   1898   -494   1526       N1+
ATOM    855  N   TYR B 106      27.192   7.265 -27.288  1.00 66.40           N  
ANISOU  855  N   TYR B 106    10405   7936   6886    684   -145    348       N  
ATOM    856  CA  TYR B 106      27.167   5.810 -27.402  1.00 66.28           C  
ANISOU  856  CA  TYR B 106    10262   8103   6819    570   -172    156       C  
ATOM    857  C   TYR B 106      28.143   5.171 -26.412  1.00 69.29           C  
ANISOU  857  C   TYR B 106    10496   8403   7430    415      8     22       C  
ATOM    858  O   TYR B 106      28.956   5.844 -25.773  1.00 70.13           O  
ANISOU  858  O   TYR B 106    10600   8347   7700    372    156     69       O  
ATOM    859  CB  TYR B 106      27.471   5.348 -28.834  1.00 64.48           C  
ANISOU  859  CB  TYR B 106    10240   7988   6272    532   -142    172       C  
ATOM    860  CG  TYR B 106      28.860   5.660 -29.334  1.00 57.34           C  
ANISOU  860  CG  TYR B 106     9517   6968   5303    432    140    259       C  
ATOM    861  CD1 TYR B 106      29.933   4.818 -29.045  1.00 56.64           C  
ANISOU  861  CD1 TYR B 106     9339   6862   5318    285    344    114       C  
ATOM    862  CD2 TYR B 106      29.095   6.760 -30.132  1.00 56.30           C  
ANISOU  862  CD2 TYR B 106     9636   6755   5001    488    211    493       C  
ATOM    863  CE1 TYR B 106      31.208   5.082 -29.514  1.00 59.82           C  
ANISOU  863  CE1 TYR B 106     9855   7201   5672    191    617    183       C  
ATOM    864  CE2 TYR B 106      30.381   7.036 -30.610  1.00 67.29           C  
ANISOU  864  CE2 TYR B 106    11172   8060   6334    361    502    580       C  
ATOM    865  CZ  TYR B 106      31.434   6.186 -30.287  1.00 67.04           C  
ANISOU  865  CZ  TYR B 106    11001   8048   6422    210    706    412       C  
ATOM    866  OH  TYR B 106      32.709   6.432 -30.750  1.00 72.54           O  
ANISOU  866  OH  TYR B 106    11785   8701   7077     84   1007    484       O  
ATOM    867  N   VAL B 107      28.052   3.846 -26.307  1.00 68.59           N  
ANISOU  867  N   VAL B 107    10290   8424   7349    330    -20   -148       N  
ATOM    868  CA  VAL B 107      28.920   3.053 -25.450  1.00 62.70           C  
ANISOU  868  CA  VAL B 107     9412   7618   6792    218    122   -265       C  
ATOM    869  C   VAL B 107      29.633   2.044 -26.313  1.00 61.75           C  
ANISOU  869  C   VAL B 107     9386   7537   6539    142    234   -362       C  
ATOM    870  O   VAL B 107      28.999   1.370 -27.132  1.00 68.95           O  
ANISOU  870  O   VAL B 107    10368   8560   7270    141    121   -442       O  
ATOM    871  CB  VAL B 107      28.163   2.280 -24.361  1.00 60.31           C  
ANISOU  871  CB  VAL B 107     8890   7368   6656    198      7   -375       C  
ATOM    872  CG1 VAL B 107      29.123   1.942 -23.211  1.00 63.40           C  
ANISOU  872  CG1 VAL B 107     9162   7668   7259    132    147   -421       C  
ATOM    873  CG2 VAL B 107      26.993   3.021 -23.920  1.00 62.05           C  
ANISOU  873  CG2 VAL B 107     9021   7642   6914    304   -154   -318       C  
ATOM    874  N   SER B 108      30.923   1.876 -26.068  1.00 61.69           N  
ANISOU  874  N   SER B 108     9356   7452   6631     82    445   -384       N  
ATOM    875  CA  SER B 108      31.740   0.956 -26.837  1.00 66.68           C  
ANISOU  875  CA  SER B 108    10063   8113   7157     43    594   -489       C  
ATOM    876  C   SER B 108      32.417  -0.018 -25.886  1.00 68.53           C  
ANISOU  876  C   SER B 108    10128   8290   7619     15    672   -606       C  
ATOM    877  O   SER B 108      32.570   0.262 -24.693  1.00 69.04           O  
ANISOU  877  O   SER B 108    10033   8302   7897      9    656   -571       O  
ATOM    878  CB  SER B 108      32.769   1.713 -27.677  1.00 64.58           C  
ANISOU  878  CB  SER B 108     9934   7842   6763     23    813   -381       C  
ATOM    879  OG  SER B 108      33.663   2.391 -26.812  1.00 73.01           O  
ANISOU  879  OG  SER B 108    10871   8815   8056    -27    943   -313       O  
ATOM    880  N   LEU B 109      32.815  -1.175 -26.420  1.00 71.11           N  
ANISOU  880  N   LEU B 109    10507   8624   7887     14    749   -750       N  
ATOM    881  CA  LEU B 109      33.551  -2.175 -25.652  1.00 70.04           C  
ANISOU  881  CA  LEU B 109    10242   8414   7955     29    833   -847       C  
ATOM    882  C   LEU B 109      34.369  -3.008 -26.634  1.00 69.73           C  
ANISOU  882  C   LEU B 109    10313   8381   7802     67   1009   -981       C  
ATOM    883  O   LEU B 109      34.312  -2.800 -27.848  1.00 75.34           O  
ANISOU  883  O   LEU B 109    11198   9170   8257     64   1062  -1002       O  
ATOM    884  CB  LEU B 109      32.600  -3.025 -24.797  1.00 65.42           C  
ANISOU  884  CB  LEU B 109     9584   7775   7500      7    654   -904       C  
ATOM    885  CG  LEU B 109      31.487  -3.814 -25.524  1.00 68.55           C  
ANISOU  885  CG  LEU B 109    10103   8188   7756    -43    507  -1025       C  
ATOM    886  CD1 LEU B 109      31.991  -5.128 -26.138  1.00 75.09           C  
ANISOU  886  CD1 LEU B 109    11050   8927   8552    -34    602  -1211       C  
ATOM    887  CD2 LEU B 109      30.276  -4.079 -24.620  1.00 58.15           C  
ANISOU  887  CD2 LEU B 109     8667   6866   6561   -109    316  -1009       C  
ATOM    888  N   HIS B 110      35.133  -3.958 -26.100  1.00 66.68           N  
ANISOU  888  N   HIS B 110     9829   7915   7591    125   1101  -1072       N  
ATOM    889  CA  HIS B 110      35.984  -4.820 -26.911  1.00 63.12           C  
ANISOU  889  CA  HIS B 110     9458   7453   7070    204   1289  -1224       C  
ATOM    890  C   HIS B 110      35.771  -6.281 -26.507  1.00 65.74           C  
ANISOU  890  C   HIS B 110     9816   7625   7536    257   1226  -1373       C  
ATOM    891  O   HIS B 110      35.509  -6.594 -25.340  1.00 58.21           O  
ANISOU  891  O   HIS B 110     8745   6579   6794    254   1113  -1312       O  
ATOM    892  CB  HIS B 110      37.483  -4.448 -26.784  1.00 58.96           C  
ANISOU  892  CB  HIS B 110     8767   6989   6645    266   1531  -1180       C  
ATOM    893  CG  HIS B 110      37.871  -3.179 -27.489  1.00 70.71           C  
ANISOU  893  CG  HIS B 110    10284   8607   7977    190   1667  -1057       C  
ATOM    894  CD2 HIS B 110      38.058  -2.907 -28.804  1.00 75.18           C  
ANISOU  894  CD2 HIS B 110    11024   9273   8267    176   1822  -1071       C  
ATOM    895  ND1 HIS B 110      38.152  -2.006 -26.818  1.00 75.35           N  
ANISOU  895  ND1 HIS B 110    10727   9216   8687    108   1665   -892       N  
ATOM    896  CE1 HIS B 110      38.481  -1.067 -27.690  1.00 73.40           C  
ANISOU  896  CE1 HIS B 110    10571   9046   8271     35   1817   -794       C  
ATOM    897  NE2 HIS B 110      38.426  -1.586 -28.902  1.00 73.57           N  
ANISOU  897  NE2 HIS B 110    10787   9132   8036     80   1917   -885       N  
ATOM    898  N   VAL B 111      35.877  -7.175 -27.494  1.00 65.29           N  
ANISOU  898  N   VAL B 111     9940   7523   7343    303   1307  -1568       N  
ATOM    899  CA  VAL B 111      35.574  -8.588 -27.316  1.00 65.35           C  
ANISOU  899  CA  VAL B 111    10044   7326   7460    333   1248  -1735       C  
ATOM    900  C   VAL B 111      36.461  -9.379 -28.249  1.00 76.70           C  
ANISOU  900  C   VAL B 111    11612   8720   8810    472   1463  -1945       C  
ATOM    901  O   VAL B 111      36.588  -9.053 -29.434  1.00 84.57           O  
ANISOU  901  O   VAL B 111    12744   9859   9529    468   1568  -2033       O  
ATOM    902  CB  VAL B 111      34.102  -8.922 -27.616  1.00 65.93           C  
ANISOU  902  CB  VAL B 111    10265   7360   7426    173   1017  -1816       C  
ATOM    903  CG1 VAL B 111      33.229  -8.515 -26.487  1.00 60.27           C  
ANISOU  903  CG1 VAL B 111     9395   6643   6863     70    826  -1643       C  
ATOM    904  CG2 VAL B 111      33.675  -8.209 -28.891  1.00 75.10           C  
ANISOU  904  CG2 VAL B 111    11569   8719   8245    115    990  -1855       C  
ATOM    905  N   ARG B 112      37.059 -10.433 -27.717  1.00 75.64           N  
ANISOU  905  N   ARG B 112    11450   8389   8898    614   1534  -2024       N  
ATOM    906  CA  ARG B 112      37.714 -11.391 -28.586  1.00 77.57           C  
ANISOU  906  CA  ARG B 112    11856   8540   9079    768   1719  -2273       C  
ATOM    907  C   ARG B 112      36.703 -11.903 -29.602  1.00 78.91           C  
ANISOU  907  C   ARG B 112    12322   8651   9011    638   1612  -2497       C  
ATOM    908  O   ARG B 112      35.530 -12.119 -29.281  1.00 80.74           O  
ANISOU  908  O   ARG B 112    12616   8786   9275    461   1375  -2488       O  
ATOM    909  CB  ARG B 112      38.305 -12.538 -27.763  1.00 77.71           C  
ANISOU  909  CB  ARG B 112    11831   8293   9402    956   1762  -2311       C  
ATOM    910  CG  ARG B 112      39.124 -12.031 -26.569  1.00 85.44           C  
ANISOU  910  CG  ARG B 112    12493   9355  10615   1061   1784  -2072       C  
ATOM    911  CD  ARG B 112      39.766 -13.155 -25.752  1.00 92.38           C  
ANISOU  911  CD  ARG B 112    13329   9993  11777   1294   1810  -2077       C  
ATOM    912  NE  ARG B 112      41.008 -12.737 -25.099  1.00 92.36           N  
ANISOU  912  NE  ARG B 112    13010  10156  11928   1479   1914  -1943       N  
ATOM    913  CZ  ARG B 112      42.236 -12.976 -25.569  1.00101.07           C  
ANISOU  913  CZ  ARG B 112    13997  11340  13066   1720   2146  -2052       C  
ATOM    914  NH1 ARG B 112      43.288 -12.539 -24.892  1.00107.22           N1+
ANISOU  914  NH1 ARG B 112    14438  12304  13998   1854   2202  -1922       N1+
ATOM    915  NH2 ARG B 112      42.434 -13.650 -26.704  1.00100.68           N  
ANISOU  915  NH2 ARG B 112    14149  11209  12895   1831   2324  -2308       N  
ATOM    916  N   LYS B 113      37.152 -12.063 -30.851  1.00 74.25           N  
ANISOU  916  N   LYS B 113    11900   8151   8161    716   1789  -2706       N  
ATOM    917  CA  LYS B 113      36.231 -12.523 -31.878  1.00 69.16           C  
ANISOU  917  CA  LYS B 113    11545   7488   7246    591   1670  -2948       C  
ATOM    918  C   LYS B 113      35.785 -13.952 -31.667  1.00 72.80           C  
ANISOU  918  C   LYS B 113    12181   7595   7884    574   1575  -3179       C  
ATOM    919  O   LYS B 113      34.820 -14.374 -32.312  1.00 86.03           O  
ANISOU  919  O   LYS B 113    14070   9228   9389    406   1407  -3381       O  
ATOM    920  CB  LYS B 113      36.829 -12.410 -33.279  1.00 77.06           C  
ANISOU  920  CB  LYS B 113    12716   8679   7882    686   1894  -3138       C  
ATOM    921  CG  LYS B 113      37.617 -11.161 -33.561  1.00 76.69           C  
ANISOU  921  CG  LYS B 113    12515   8938   7687    733   2093  -2922       C  
ATOM    922  CD  LYS B 113      38.522 -11.363 -34.758  1.00 68.53           C  
ANISOU  922  CD  LYS B 113    11621   8047   6371    884   2408  -3125       C  
ATOM    923  CE  LYS B 113      38.029 -10.513 -35.928  1.00 73.94           C  
ANISOU  923  CE  LYS B 113    12494   9021   6579    762   2387  -3093       C  
ATOM    924  NZ  LYS B 113      38.948 -10.500 -37.095  1.00 73.70           N1+
ANISOU  924  NZ  LYS B 113    12517   9217   6267    886   2680  -3195       N1+
ATOM    925  N   SER B 114      36.480 -14.710 -30.817  1.00 74.30           N  
ANISOU  925  N   SER B 114    12298   7528   8405    743   1673  -3157       N  
ATOM    926  CA  SER B 114      36.192 -16.121 -30.583  1.00 79.25           C  
ANISOU  926  CA  SER B 114    13125   7750   9236    753   1619  -3355       C  
ATOM    927  C   SER B 114      35.430 -16.344 -29.295  1.00 81.16           C  
ANISOU  927  C   SER B 114    13268   7798   9769    601   1409  -3140       C  
ATOM    928  O   SER B 114      35.099 -17.489 -28.970  1.00 94.83           O  
ANISOU  928  O   SER B 114    15169   9161  11700    565   1355  -3249       O  
ATOM    929  CB  SER B 114      37.488 -16.930 -30.554  1.00 84.39           C  
ANISOU  929  CB  SER B 114    13776   8226  10061   1088   1862  -3458       C  
ATOM    930  OG  SER B 114      38.288 -16.520 -29.461  1.00 89.20           O  
ANISOU  930  OG  SER B 114    14088   8960  10844   1265   1980  -3194       O  
ATOM    931  N   ASN B 115      35.160 -15.280 -28.557  1.00 75.77           N  
ANISOU  931  N   ASN B 115    12332   7345   9112    509   1308  -2839       N  
ATOM    932  CA  ASN B 115      34.378 -15.339 -27.329  1.00 77.49           C  
ANISOU  932  CA  ASN B 115    12436   7451   9555    355   1125  -2620       C  
ATOM    933  C   ASN B 115      32.905 -15.333 -27.716  1.00 75.67           C  
ANISOU  933  C   ASN B 115    12298   7257   9197     41    898  -2710       C  
ATOM    934  O   ASN B 115      32.255 -14.285 -27.753  1.00 66.00           O  
ANISOU  934  O   ASN B 115    10931   6319   7827    -87    773  -2582       O  
ATOM    935  CB  ASN B 115      34.748 -14.172 -26.423  1.00 76.46           C  
ANISOU  935  CB  ASN B 115    12002   7568   9481    408   1125  -2305       C  
ATOM    936  CG  ASN B 115      33.966 -14.158 -25.128  1.00 83.03           C  
ANISOU  936  CG  ASN B 115    12713   8332  10503    267    958  -2080       C  
ATOM    937  ND2 ASN B 115      34.485 -13.433 -24.152  1.00 83.66           N  
ANISOU  937  ND2 ASN B 115    12559   8548  10679    361    976  -1838       N  
ATOM    938  OD1 ASN B 115      32.890 -14.746 -25.013  1.00 89.49           O  
ANISOU  938  OD1 ASN B 115    13635   9000  11367     58    819  -2130       O  
ATOM    939  N   ARG B 116      32.380 -16.534 -27.991  1.00 79.40           N  
ANISOU  939  N   ARG B 116    13004   7423   9743    -79    841  -2939       N  
ATOM    940  CA  ARG B 116      30.981 -16.693 -28.389  1.00 81.53           C  
ANISOU  940  CA  ARG B 116    13344   7719   9916   -404    613  -3069       C  
ATOM    941  C   ARG B 116      30.035 -16.184 -27.309  1.00 80.06           C  
ANISOU  941  C   ARG B 116    12915   7637   9866   -597    448  -2791       C  
ATOM    942  O   ARG B 116      29.068 -15.463 -27.595  1.00 73.28           O  
ANISOU  942  O   ARG B 116    11940   7055   8849   -775    272  -2770       O  
ATOM    943  CB  ARG B 116      30.684 -18.165 -28.666  1.00 91.87           C  
ANISOU  943  CB  ARG B 116    14940   8611  11355   -520    597  -3354       C  
ATOM    944  CG  ARG B 116      30.676 -18.555 -30.111  1.00102.89           C  
ANISOU  944  CG  ARG B 116    16578  10031  12486   -532    594  -3736       C  
ATOM    945  CD  ARG B 116      30.395 -20.028 -30.237  1.00112.68           C  
ANISOU  945  CD  ARG B 116    17974  10900  13940   -618    530  -3930       C  
ATOM    946  NE  ARG B 116      29.756 -20.323 -31.509  1.00126.76           N  
ANISOU  946  NE  ARG B 116    19865  12813  15484   -766    372  -4247       N  
ATOM    947  CZ  ARG B 116      28.445 -20.476 -31.668  1.00136.19           C  
ANISOU  947  CZ  ARG B 116    21032  14057  16658  -1114    117  -4340       C  
ATOM    948  NH1 ARG B 116      27.637 -20.356 -30.620  1.00134.54           N1+
ANISOU  948  NH1 ARG B 116    20679  13780  16659  -1359     16  -4130       N1+
ATOM    949  NH2 ARG B 116      27.944 -20.746 -32.874  1.00142.51           N  
ANISOU  949  NH2 ARG B 116    21927  14997  17223  -1214    -38  -4645       N  
ATOM    950  N   ALA B 117      30.276 -16.598 -26.060  1.00 83.86           N  
ANISOU  950  N   ALA B 117    13324   7903  10636   -551    503  -2580       N  
ATOM    951  CA  ALA B 117      29.404 -16.226 -24.952  1.00 83.82           C  
ANISOU  951  CA  ALA B 117    13104   7986  10758   -728    383  -2323       C  
ATOM    952  C   ALA B 117      29.163 -14.738 -24.936  1.00 74.93           C  
ANISOU  952  C   ALA B 117    11733   7283   9454   -706    313  -2167       C  
ATOM    953  O   ALA B 117      28.017 -14.276 -25.021  1.00 72.59           O  
ANISOU  953  O   ALA B 117    11317   7184   9079   -911    144  -2155       O  
ATOM    954  CB  ALA B 117      30.025 -16.662 -23.627  1.00 86.04           C  
ANISOU  954  CB  ALA B 117    13344   8047  11299   -590    489  -2078       C  
ATOM    955  N   ALA B 118      30.257 -13.976 -24.867  1.00 73.34           N  
ANISOU  955  N   ALA B 118    11453   7217   9197   -455    444  -2056       N  
ATOM    956  CA  ALA B 118      30.177 -12.528 -24.728  1.00 71.43           C  
ANISOU  956  CA  ALA B 118    11001   7313   8825   -417    404  -1883       C  
ATOM    957  C   ALA B 118      29.553 -11.879 -25.959  1.00 75.77           C  
ANISOU  957  C   ALA B 118    11597   8100   9092   -500    296  -2014       C  
ATOM    958  O   ALA B 118      28.730 -10.960 -25.841  1.00 77.87           O  
ANISOU  958  O   ALA B 118    11713   8595   9278   -581    158  -1902       O  
ATOM    959  CB  ALA B 118      31.571 -11.971 -24.461  1.00 66.82           C  
ANISOU  959  CB  ALA B 118    10339   6787   8264   -165    579  -1769       C  
ATOM    960  N   LEU B 119      29.941 -12.337 -27.155  1.00 73.15           N  
ANISOU  960  N   LEU B 119    11480   7725   8589   -458    356  -2252       N  
ATOM    961  CA  LEU B 119      29.332 -11.823 -28.377  1.00 72.47           C  
ANISOU  961  CA  LEU B 119    11473   7873   8188   -532    235  -2381       C  
ATOM    962  C   LEU B 119      27.816 -11.956 -28.320  1.00 74.00           C  
ANISOU  962  C   LEU B 119    11592   8142   8383   -783    -27  -2422       C  
ATOM    963  O   LEU B 119      27.087 -10.988 -28.578  1.00 73.90           O  
ANISOU  963  O   LEU B 119    11459   8408   8211   -818   -180  -2332       O  
ATOM    964  CB  LEU B 119      29.887 -12.559 -29.599  1.00 73.22           C  
ANISOU  964  CB  LEU B 119    11842   7883   8094   -473    337  -2677       C  
ATOM    965  CG  LEU B 119      31.311 -12.234 -30.052  1.00 71.99           C  
ANISOU  965  CG  LEU B 119    11745   7772   7835   -224    604  -2670       C  
ATOM    966  CD1 LEU B 119      31.757 -13.190 -31.136  1.00 68.24           C  
ANISOU  966  CD1 LEU B 119    11548   7177   7203   -165    718  -3003       C  
ATOM    967  CD2 LEU B 119      31.430 -10.791 -30.525  1.00 74.75           C  
ANISOU  967  CD2 LEU B 119    12015   8451   7936   -170    617  -2494       C  
ATOM    968  N   HIS B 120      27.328 -13.156 -27.970  1.00 75.99           N  
ANISOU  968  N   HIS B 120    11903   8139   8830   -960    -77  -2552       N  
ATOM    969  CA  HIS B 120      25.888 -13.387 -27.889  1.00 85.82           C  
ANISOU  969  CA  HIS B 120    13040   9457  10110  -1241   -312  -2608       C  
ATOM    970  C   HIS B 120      25.250 -12.513 -26.813  1.00 78.33           C  
ANISOU  970  C   HIS B 120    11784   8697   9283  -1266   -380  -2321       C  
ATOM    971  O   HIS B 120      24.193 -11.912 -27.044  1.00 80.01           O  
ANISOU  971  O   HIS B 120    11829   9180   9389  -1370   -576  -2307       O  
ATOM    972  CB  HIS B 120      25.621 -14.873 -27.649  1.00106.98           C  
ANISOU  972  CB  HIS B 120    15862  11771  13014  -1447   -308  -2785       C  
ATOM    973  CG  HIS B 120      24.173 -15.221 -27.491  1.00125.36           C  
ANISOU  973  CG  HIS B 120    18050  14156  15424  -1788   -525  -2847       C  
ATOM    974  CD2 HIS B 120      23.558 -16.117 -26.682  1.00131.53           C  
ANISOU  974  CD2 HIS B 120    18789  14700  16487  -2040   -536  -2824       C  
ATOM    975  ND1 HIS B 120      23.175 -14.632 -28.237  1.00131.38           N  
ANISOU  975  ND1 HIS B 120    18683  15267  15969  -1909   -763  -2940       N  
ATOM    976  CE1 HIS B 120      22.007 -15.139 -27.880  1.00134.79           C  
ANISOU  976  CE1 HIS B 120    18958  15699  16559  -2226   -915  -2988       C  
ATOM    977  NE2 HIS B 120      22.211 -16.044 -26.941  1.00133.76           N  
ANISOU  977  NE2 HIS B 120    18884  15207  16732  -2329   -767  -2916       N  
ATOM    978  N   LEU B 121      25.901 -12.380 -25.655  1.00 72.60           N  
ANISOU  978  N   LEU B 121    10972   7856   8757  -1144   -224  -2098       N  
ATOM    979  CA  LEU B 121      25.380 -11.485 -24.626  1.00 73.04           C  
ANISOU  979  CA  LEU B 121    10757   8101   8895  -1138   -265  -1848       C  
ATOM    980  C   LEU B 121      25.272 -10.049 -25.143  1.00 76.29           C  
ANISOU  980  C   LEU B 121    11071   8830   9087  -1000   -339  -1768       C  
ATOM    981  O   LEU B 121      24.181  -9.460 -25.143  1.00 75.01           O  
ANISOU  981  O   LEU B 121    10730   8898   8874  -1076   -507  -1728       O  
ATOM    982  CB  LEU B 121      26.252 -11.548 -23.367  1.00 72.93           C  
ANISOU  982  CB  LEU B 121    10702   7931   9078  -1004    -91  -1643       C  
ATOM    983  CG  LEU B 121      25.825 -10.585 -22.233  1.00 74.26           C  
ANISOU  983  CG  LEU B 121    10613   8296   9306   -974   -111  -1405       C  
ATOM    984  CD1 LEU B 121      24.458 -10.996 -21.639  1.00 66.18           C  
ANISOU  984  CD1 LEU B 121     9429   7321   8395  -1222   -215  -1377       C  
ATOM    985  CD2 LEU B 121      26.902 -10.420 -21.115  1.00 71.57           C  
ANISOU  985  CD2 LEU B 121    10244   7864   9085   -795     45  -1218       C  
ATOM    986  N   TYR B 122      26.386  -9.478 -25.627  1.00 75.42           N  
ANISOU  986  N   TYR B 122    11076   8734   8848   -794   -210  -1742       N  
ATOM    987  CA  TYR B 122      26.382  -8.060 -25.985  1.00 80.73           C  
ANISOU  987  CA  TYR B 122    11682   9649   9342   -662   -248  -1616       C  
ATOM    988  C   TYR B 122      25.518  -7.781 -27.222  1.00 86.99           C  
ANISOU  988  C   TYR B 122    12533  10653   9868   -716   -444  -1732       C  
ATOM    989  O   TYR B 122      24.746  -6.814 -27.239  1.00 87.90           O  
ANISOU  989  O   TYR B 122    12511  10984   9905   -680   -588  -1618       O  
ATOM    990  CB  TYR B 122      27.821  -7.574 -26.181  1.00 81.01           C  
ANISOU  990  CB  TYR B 122    11819   9637   9325   -473    -37  -1552       C  
ATOM    991  CG  TYR B 122      28.675  -7.688 -24.923  1.00 82.03           C  
ANISOU  991  CG  TYR B 122    11847   9621   9699   -398    116  -1423       C  
ATOM    992  CD1 TYR B 122      28.203  -7.227 -23.697  1.00 85.94           C  
ANISOU  992  CD1 TYR B 122    12146  10160  10346   -416     66  -1260       C  
ATOM    993  CD2 TYR B 122      29.945  -8.273 -24.958  1.00 78.56           C  
ANISOU  993  CD2 TYR B 122    11502   9024   9323   -291    304  -1474       C  
ATOM    994  CE1 TYR B 122      28.971  -7.327 -22.544  1.00 85.66           C  
ANISOU  994  CE1 TYR B 122    12029  10026  10493   -344    179  -1147       C  
ATOM    995  CE2 TYR B 122      30.722  -8.386 -23.814  1.00 76.15           C  
ANISOU  995  CE2 TYR B 122    11088   8620   9226   -204    408  -1353       C  
ATOM    996  CZ  TYR B 122      30.224  -7.908 -22.609  1.00 88.69           C  
ANISOU  996  CZ  TYR B 122    12499  10264  10935   -238    334  -1187       C  
ATOM    997  OH  TYR B 122      30.958  -8.005 -21.445  1.00 99.89           O  
ANISOU  997  OH  TYR B 122    13816  11617  12519   -152    410  -1068       O  
ATOM    998  N   SER B 123      25.603  -8.625 -28.255  1.00 88.79           N  
ANISOU  998  N   SER B 123    12966  10826   9946   -787   -468  -1968       N  
ATOM    999  CA  SER B 123      24.830  -8.372 -29.469  1.00 90.85           C  
ANISOU  999  CA  SER B 123    13295  11319   9904   -830   -677  -2089       C  
ATOM   1000  C   SER B 123      23.347  -8.664 -29.265  1.00 99.58           C  
ANISOU 1000  C   SER B 123    14200  12553  11082  -1033   -941  -2154       C  
ATOM   1001  O   SER B 123      22.487  -7.838 -29.604  1.00101.02           O  
ANISOU 1001  O   SER B 123    14251  13014  11119   -998  -1144  -2083       O  
ATOM   1002  CB  SER B 123      25.373  -9.202 -30.631  1.00 88.75           C  
ANISOU 1002  CB  SER B 123    13320  10975   9426   -849   -621  -2356       C  
ATOM   1003  OG  SER B 123      24.739  -8.836 -31.852  1.00 91.65           O  
ANISOU 1003  OG  SER B 123    13778  11608   9436   -860   -825  -2456       O  
ATOM   1004  N   ASN B 124      23.020  -9.838 -28.716  1.00104.28           N  
ANISOU 1004  N   ASN B 124    14761  12950  11911  -1246   -940  -2283       N  
ATOM   1005  CA  ASN B 124      21.619 -10.254 -28.718  1.00109.53           C  
ANISOU 1005  CA  ASN B 124    15238  13749  12630  -1496  -1185  -2395       C  
ATOM   1006  C   ASN B 124      20.806  -9.647 -27.577  1.00106.86           C  
ANISOU 1006  C   ASN B 124    14554  13553  12494  -1515  -1231  -2173       C  
ATOM   1007  O   ASN B 124      19.632  -9.323 -27.784  1.00107.92           O  
ANISOU 1007  O   ASN B 124    14461  13965  12577  -1600  -1460  -2196       O  
ATOM   1008  CB  ASN B 124      21.535 -11.780 -28.700  1.00114.84           C  
ANISOU 1008  CB  ASN B 124    16039  14130  13464  -1761  -1164  -2638       C  
ATOM   1009  CG  ASN B 124      21.594 -12.380 -30.099  1.00125.49           C  
ANISOU 1009  CG  ASN B 124    17654  15479  14549  -1832  -1272  -2965       C  
ATOM   1010  ND2 ASN B 124      21.622 -11.505 -31.107  1.00126.18           N  
ANISOU 1010  ND2 ASN B 124    17801  15858  14283  -1667  -1381  -2967       N  
ATOM   1011  OD1 ASN B 124      21.607 -13.597 -30.280  1.00132.91           O  
ANISOU 1011  OD1 ASN B 124    18761  16152  15585  -2030  -1256  -3211       O  
ATOM   1012  N   THR B 125      21.396  -9.444 -26.398  1.00105.38           N  
ANISOU 1012  N   THR B 125    14308  13217  12516  -1419  -1024  -1969       N  
ATOM   1013  CA  THR B 125      20.629  -8.975 -25.251  1.00104.82           C  
ANISOU 1013  CA  THR B 125    13926  13274  12625  -1444  -1038  -1787       C  
ATOM   1014  C   THR B 125      20.812  -7.488 -24.957  1.00101.11           C  
ANISOU 1014  C   THR B 125    13355  12982  12079  -1167  -1015  -1575       C  
ATOM   1015  O   THR B 125      19.876  -6.847 -24.471  1.00104.22           O  
ANISOU 1015  O   THR B 125    13480  13595  12523  -1146  -1111  -1481       O  
ATOM   1016  CB  THR B 125      20.989  -9.790 -24.001  1.00105.76           C  
ANISOU 1016  CB  THR B 125    14040  13125  13017  -1548   -843  -1701       C  
ATOM   1017  CG2 THR B 125      20.862 -11.282 -24.265  1.00102.00           C  
ANISOU 1017  CG2 THR B 125    13713  12395  12648  -1820   -846  -1898       C  
ATOM   1018  OG1 THR B 125      22.336  -9.508 -23.615  1.00115.83           O  
ANISOU 1018  OG1 THR B 125    15475  14228  14305  -1327   -642  -1582       O  
ATOM   1019  N   LEU B 126      21.989  -6.915 -25.235  1.00 93.50           N  
ANISOU 1019  N   LEU B 126    12592  11925  11009   -959   -881  -1504       N  
ATOM   1020  CA  LEU B 126      22.261  -5.517 -24.907  1.00 89.51           C  
ANISOU 1020  CA  LEU B 126    12026  11521  10462   -725   -838  -1307       C  
ATOM   1021  C   LEU B 126      22.232  -4.593 -26.122  1.00 97.35           C  
ANISOU 1021  C   LEU B 126    13134  12675  11179   -572   -953  -1292       C  
ATOM   1022  O   LEU B 126      22.565  -3.408 -25.990  1.00 97.83           O  
ANISOU 1022  O   LEU B 126    13206  12767  11200   -379   -904  -1126       O  
ATOM   1023  CB  LEU B 126      23.614  -5.396 -24.195  1.00 82.08           C  
ANISOU 1023  CB  LEU B 126    11190  10369   9626   -618   -596  -1204       C  
ATOM   1024  CG  LEU B 126      23.886  -6.434 -23.092  1.00 81.07           C  
ANISOU 1024  CG  LEU B 126    11023  10049   9731   -737   -471  -1202       C  
ATOM   1025  CD1 LEU B 126      25.187  -6.173 -22.364  1.00 78.51           C  
ANISOU 1025  CD1 LEU B 126    10759   9580   9490   -598   -277  -1090       C  
ATOM   1026  CD2 LEU B 126      22.761  -6.467 -22.093  1.00 78.73           C  
ANISOU 1026  CD2 LEU B 126    10472   9867   9576   -842   -535  -1136       C  
ATOM   1027  N   ASN B 127      21.833  -5.102 -27.289  1.00104.87           N  
ANISOU 1027  N   ASN B 127    14190  13724  11933   -659  -1109  -1458       N  
ATOM   1028  CA  ASN B 127      21.824  -4.354 -28.550  1.00107.05           C  
ANISOU 1028  CA  ASN B 127    14620  14166  11887   -518  -1227  -1441       C  
ATOM   1029  C   ASN B 127      23.140  -3.610 -28.787  1.00 94.86           C  
ANISOU 1029  C   ASN B 127    13300  12497  10245   -343  -1005  -1303       C  
ATOM   1030  O   ASN B 127      23.170  -2.401 -29.033  1.00100.19           O  
ANISOU 1030  O   ASN B 127    14010  13254  10803   -166  -1025  -1122       O  
ATOM   1031  CB  ASN B 127      20.638  -3.389 -28.627  1.00121.22           C  
ANISOU 1031  CB  ASN B 127    16207  16233  13618   -403  -1465  -1329       C  
ATOM   1032  CG  ASN B 127      20.413  -2.851 -30.054  1.00134.70           C  
ANISOU 1032  CG  ASN B 127    18083  18144  14953   -281  -1653  -1325       C  
ATOM   1033  ND2 ASN B 127      21.192  -1.837 -30.437  1.00136.49           N  
ANISOU 1033  ND2 ASN B 127    18517  18316  15027    -77  -1535  -1138       N  
ATOM   1034  OD1 ASN B 127      19.566  -3.355 -30.802  1.00140.98           O  
ANISOU 1034  OD1 ASN B 127    18830  19143  15592   -383  -1901  -1486       O  
ATOM   1035  N   PHE B 128      24.241  -4.344 -28.707  1.00 80.81           N  
ANISOU 1035  N   PHE B 128    11667  10509   8529   -395   -788  -1387       N  
ATOM   1036  CA  PHE B 128      25.514  -3.852 -29.198  1.00 71.02           C  
ANISOU 1036  CA  PHE B 128    10633   9190   7159   -272   -574  -1311       C  
ATOM   1037  C   PHE B 128      25.736  -4.365 -30.610  1.00 78.41           C  
ANISOU 1037  C   PHE B 128    11818  10195   7778   -293   -588  -1482       C  
ATOM   1038  O   PHE B 128      25.270  -5.444 -30.979  1.00 77.66           O  
ANISOU 1038  O   PHE B 128    11760  10100   7645   -431   -697  -1715       O  
ATOM   1039  CB  PHE B 128      26.667  -4.310 -28.321  1.00 64.73           C  
ANISOU 1039  CB  PHE B 128     9823   8167   6606   -277   -321  -1306       C  
ATOM   1040  CG  PHE B 128      26.948  -3.427 -27.158  1.00 65.92           C  
ANISOU 1040  CG  PHE B 128     9814   8267   6965   -201   -240  -1108       C  
ATOM   1041  CD1 PHE B 128      26.252  -3.584 -25.966  1.00 72.08           C  
ANISOU 1041  CD1 PHE B 128    10379   9033   7974   -254   -315  -1074       C  
ATOM   1042  CD2 PHE B 128      27.958  -2.477 -27.220  1.00 63.45           C  
ANISOU 1042  CD2 PHE B 128     9568   7918   6622    -95    -70   -968       C  
ATOM   1043  CE1 PHE B 128      26.556  -2.789 -24.846  1.00 68.06           C  
ANISOU 1043  CE1 PHE B 128     9741   8484   7635   -179   -236   -922       C  
ATOM   1044  CE2 PHE B 128      28.256  -1.680 -26.113  1.00 62.23           C  
ANISOU 1044  CE2 PHE B 128     9276   7702   6665    -46     -5   -824       C  
ATOM   1045  CZ  PHE B 128      27.559  -1.852 -24.923  1.00 62.74           C  
ANISOU 1045  CZ  PHE B 128     9143   7761   6932    -78    -93   -812       C  
ATOM   1046  N   GLN B 129      26.449  -3.572 -31.405  1.00 86.40           N  
ANISOU 1046  N   GLN B 129    13014  11265   8550   -169   -470  -1370       N  
ATOM   1047  CA  GLN B 129      26.624  -3.842 -32.822  1.00 85.49           C  
ANISOU 1047  CA  GLN B 129    13156  11271   8055   -160   -477  -1500       C  
ATOM   1048  C   GLN B 129      28.110  -3.805 -33.133  1.00 82.86           C  
ANISOU 1048  C   GLN B 129    12984  10835   7664    -96   -137  -1480       C  
ATOM   1049  O   GLN B 129      28.852  -3.027 -32.530  1.00 88.26           O  
ANISOU 1049  O   GLN B 129    13597  11431   8507    -32     45  -1279       O  
ATOM   1050  CB  GLN B 129      25.831  -2.834 -33.671  1.00 91.19           C  
ANISOU 1050  CB  GLN B 129    13951  12240   8458    -62   -695  -1351       C  
ATOM   1051  CG  GLN B 129      24.431  -2.549 -33.102  1.00104.01           C  
ANISOU 1051  CG  GLN B 129    15321  13981  10218    -70  -1003  -1299       C  
ATOM   1052  CD  GLN B 129      23.388  -2.183 -34.150  1.00120.47           C  
ANISOU 1052  CD  GLN B 129    17461  16359  11955     -8  -1320  -1293       C  
ATOM   1053  NE2 GLN B 129      22.196  -2.770 -34.024  1.00121.52           N  
ANISOU 1053  NE2 GLN B 129    17386  16635  12150   -120  -1604  -1455       N  
ATOM   1054  OE1 GLN B 129      23.643  -1.380 -35.053  1.00131.46           O  
ANISOU 1054  OE1 GLN B 129    19069  17858  13022    135  -1311  -1135       O  
ATOM   1055  N   ILE B 130      28.558  -4.696 -34.014  1.00 83.95           N  
ANISOU 1055  N   ILE B 130    13319  10981   7597   -122    -44  -1715       N  
ATOM   1056  CA  ILE B 130      29.960  -4.702 -34.404  1.00 86.10           C  
ANISOU 1056  CA  ILE B 130    13721  11200   7794    -46    299  -1717       C  
ATOM   1057  C   ILE B 130      30.247  -3.438 -35.197  1.00 85.20           C  
ANISOU 1057  C   ILE B 130    13747  11253   7372     40    382  -1474       C  
ATOM   1058  O   ILE B 130      29.504  -3.089 -36.125  1.00 90.69           O  
ANISOU 1058  O   ILE B 130    14599  12145   7715     60    192  -1449       O  
ATOM   1059  CB  ILE B 130      30.297  -5.957 -35.231  1.00 93.72           C  
ANISOU 1059  CB  ILE B 130    14882  12144   8583    -68    383  -2055       C  
ATOM   1060  CG1 ILE B 130      29.936  -7.227 -34.466  1.00 97.52           C  
ANISOU 1060  CG1 ILE B 130    15264  12407   9380   -167    290  -2281       C  
ATOM   1061  CG2 ILE B 130      31.775  -5.989 -35.583  1.00 90.06           C  
ANISOU 1061  CG2 ILE B 130    14505  11648   8063     35    769  -2067       C  
ATOM   1062  CD1 ILE B 130      30.854  -7.494 -33.291  1.00 97.92           C  
ANISOU 1062  CD1 ILE B 130    15143  12224   9836   -117    505  -2207       C  
ATOM   1063  N   SER B 131      31.319  -2.746 -34.851  1.00 81.40           N  
ANISOU 1063  N   SER B 131    13215  10697   7016     83    658  -1286       N  
ATOM   1064  CA  SER B 131      31.685  -1.624 -35.698  1.00 89.49           C  
ANISOU 1064  CA  SER B 131    14415  11848   7738    134    784  -1052       C  
ATOM   1065  C   SER B 131      33.020  -1.814 -36.400  1.00 92.81           C  
ANISOU 1065  C   SER B 131    14958  12310   7996    151   1162  -1103       C  
ATOM   1066  O   SER B 131      33.085  -1.624 -37.612  1.00110.89           O  
ANISOU 1066  O   SER B 131    17499  14778   9855    181   1230  -1087       O  
ATOM   1067  CB  SER B 131      31.672  -0.301 -34.901  1.00 96.32           C  
ANISOU 1067  CB  SER B 131    15154  12619   8825    147    777   -733       C  
ATOM   1068  OG  SER B 131      32.647  -0.262 -33.879  1.00 99.97           O  
ANISOU 1068  OG  SER B 131    15411  12916   9657    109    993   -707       O  
ATOM   1069  N   GLU B 132      34.067  -2.252 -35.700  1.00 82.15           N  
ANISOU 1069  N   GLU B 132    13430  10827   6956    145   1407  -1178       N  
ATOM   1070  CA  GLU B 132      35.430  -2.247 -36.229  1.00 77.90           C  
ANISOU 1070  CA  GLU B 132    12927  10347   6323    170   1802  -1187       C  
ATOM   1071  C   GLU B 132      36.249  -3.309 -35.514  1.00 80.43           C  
ANISOU 1071  C   GLU B 132    13048  10537   6975    211   1956  -1405       C  
ATOM   1072  O   GLU B 132      35.948  -3.678 -34.375  1.00 85.51           O  
ANISOU 1072  O   GLU B 132    13498  11016   7976    200   1795  -1436       O  
ATOM   1073  CB  GLU B 132      36.074  -0.874 -36.015  1.00 77.41           C  
ANISOU 1073  CB  GLU B 132    12797  10277   6337    117   1985   -856       C  
ATOM   1074  CG  GLU B 132      35.838  -0.465 -34.594  1.00 92.85           C  
ANISOU 1074  CG  GLU B 132    14497  12052   8730     77   1830   -748       C  
ATOM   1075  CD  GLU B 132      36.229   0.939 -34.277  1.00107.66           C  
ANISOU 1075  CD  GLU B 132    16326  13869  10709      5   1933   -446       C  
ATOM   1076  OE1 GLU B 132      35.335   1.821 -34.241  1.00113.24           O  
ANISOU 1076  OE1 GLU B 132    17130  14537  11358      7   1722   -256       O  
ATOM   1077  OE2 GLU B 132      37.434   1.145 -34.038  1.00112.75           O1-
ANISOU 1077  OE2 GLU B 132    16824  14501  11516    -53   2221   -410       O1-
ATOM   1078  N   VAL B 133      37.293  -3.789 -36.172  1.00 80.16           N  
ANISOU 1078  N   VAL B 133    13061  10583   6814    277   2276  -1545       N  
ATOM   1079  CA  VAL B 133      38.198  -4.765 -35.571  1.00 78.01           C  
ANISOU 1079  CA  VAL B 133    12595  10197   6849    368   2449  -1739       C  
ATOM   1080  C   VAL B 133      39.525  -4.080 -35.261  1.00 82.05           C  
ANISOU 1080  C   VAL B 133    12872  10770   7533    366   2773  -1571       C  
ATOM   1081  O   VAL B 133      40.055  -3.323 -36.091  1.00 86.22           O  
ANISOU 1081  O   VAL B 133    13483  11471   7805    321   3017  -1439       O  
ATOM   1082  CB  VAL B 133      38.397  -6.012 -36.465  1.00 66.83           C  
ANISOU 1082  CB  VAL B 133    11373   8805   5214    482   2568  -2088       C  
ATOM   1083  CG1 VAL B 133      37.086  -6.485 -37.048  1.00 67.74           C  
ANISOU 1083  CG1 VAL B 133    11754   8920   5064    432   2255  -2251       C  
ATOM   1084  CG2 VAL B 133      39.417  -5.795 -37.511  1.00 81.90           C  
ANISOU 1084  CG2 VAL B 133    13365  10926   6827    543   2953  -2110       C  
ATOM   1085  N   GLU B 134      40.040  -4.322 -34.041  1.00 81.19           N  
ANISOU 1085  N   GLU B 134    12464  10530   7855    398   2766  -1565       N  
ATOM   1086  CA  GLU B 134      41.392  -3.992 -33.597  1.00 77.41           C  
ANISOU 1086  CA  GLU B 134    11689  10114   7611    413   3047  -1488       C  
ATOM   1087  C   GLU B 134      42.307  -5.199 -33.827  1.00 78.06           C  
ANISOU 1087  C   GLU B 134    11690  10215   7754    611   3277  -1753       C  
ATOM   1088  O   GLU B 134      42.218  -6.190 -33.094  1.00 79.59           O  
ANISOU 1088  O   GLU B 134    11805  10237   8198    734   3144  -1900       O  
ATOM   1089  CB  GLU B 134      41.374  -3.576 -32.124  1.00 73.47           C  
ANISOU 1089  CB  GLU B 134    10916   9487   7513    355   2863  -1344       C  
ATOM   1090  CG  GLU B 134      40.907  -2.145 -31.861  1.00 85.08           C  
ANISOU 1090  CG  GLU B 134    12400  10952   8974    174   2750  -1070       C  
ATOM   1091  CD  GLU B 134      41.885  -1.058 -32.388  1.00101.31           C  
ANISOU 1091  CD  GLU B 134    14392  13147  10953     49   3061   -894       C  
ATOM   1092  OE1 GLU B 134      43.017  -1.395 -32.836  1.00102.46           O  
ANISOU 1092  OE1 GLU B 134    14409  13433  11087     97   3380   -980       O  
ATOM   1093  OE2 GLU B 134      41.513   0.146 -32.349  1.00105.70           O1-
ANISOU 1093  OE2 GLU B 134    15026  13663  11471    -98   2996   -665       O1-
ATOM   1094  N   PRO B 135      43.175  -5.183 -34.834  1.00 80.13           N  
ANISOU 1094  N   PRO B 135    11981  10672   7791    662   3633  -1820       N  
ATOM   1095  CA  PRO B 135      44.036  -6.351 -35.059  1.00 87.33           C  
ANISOU 1095  CA  PRO B 135    12812  11599   8769    894   3863  -2096       C  
ATOM   1096  C   PRO B 135      45.015  -6.546 -33.914  1.00 93.76           C  
ANISOU 1096  C   PRO B 135    13207  12378  10039    995   3922  -2068       C  
ATOM   1097  O   PRO B 135      45.527  -5.582 -33.348  1.00 98.44           O  
ANISOU 1097  O   PRO B 135    13533  13064  10807    860   3967  -1848       O  
ATOM   1098  CB  PRO B 135      44.750  -6.025 -36.381  1.00 91.26           C  
ANISOU 1098  CB  PRO B 135    13402  12373   8899    896   4255  -2123       C  
ATOM   1099  CG  PRO B 135      44.686  -4.554 -36.501  1.00 93.70           C  
ANISOU 1099  CG  PRO B 135    13704  12800   9096    649   4295  -1790       C  
ATOM   1100  CD  PRO B 135      43.386  -4.144 -35.854  1.00 89.24           C  
ANISOU 1100  CD  PRO B 135    13267  12039   8599    526   3856  -1647       C  
ATOM   1101  N   LYS B 136      45.240  -7.814 -33.559  1.00 97.50           N  
ANISOU 1101  N   LYS B 136    13640  12701  10704   1236   3898  -2295       N  
ATOM   1102  CA  LYS B 136      46.171  -8.211 -32.495  1.00 92.04           C  
ANISOU 1102  CA  LYS B 136    12567  11977  10428   1404   3927  -2289       C  
ATOM   1103  C   LYS B 136      46.025  -7.336 -31.249  1.00 91.42           C  
ANISOU 1103  C   LYS B 136    12247  11873  10614   1230   3691  -2024       C  
ATOM   1104  O   LYS B 136      47.007  -6.944 -30.609  1.00 92.91           O  
ANISOU 1104  O   LYS B 136    12056  12197  11047   1244   3787  -1930       O  
ATOM   1105  CB  LYS B 136      47.614  -8.221 -32.995  1.00 91.78           C  
ANISOU 1105  CB  LYS B 136    12255  12203  10413   1549   4344  -2366       C  
ATOM   1106  CG  LYS B 136      47.809  -8.961 -34.328  1.00 99.57           C  
ANISOU 1106  CG  LYS B 136    13448  13283  11101   1697   4495  -2589       C  
ATOM   1107  CD  LYS B 136      49.016  -8.479 -35.108  1.00103.20           C  
ANISOU 1107  CD  LYS B 136    13656  14106  11448   1702   4837  -2549       C  
ATOM   1108  CE  LYS B 136      49.457  -9.525 -36.137  1.00111.30           C  
ANISOU 1108  CE  LYS B 136    14777  15218  12292   1956   4968  -2823       C  
ATOM   1109  NZ  LYS B 136      50.803 -10.123 -35.887  1.00114.14           N1+
ANISOU 1109  NZ  LYS B 136    14734  15723  12910   2240   5148  -2926       N1+
ATOM   1110  N   TYR B 137      44.773  -7.041 -30.893  1.00 87.77           N  
ANISOU 1110  N   TYR B 137    11996  11253  10101   1069   3373  -1922       N  
ATOM   1111  CA  TYR B 137      44.491  -6.226 -29.716  1.00 87.19           C  
ANISOU 1111  CA  TYR B 137    11744  11140  10243    914   3140  -1700       C  
ATOM   1112  C   TYR B 137      45.010  -6.893 -28.447  1.00 95.01           C  
ANISOU 1112  C   TYR B 137    12459  12045  11596   1082   3027  -1711       C  
ATOM   1113  O   TYR B 137      45.792  -6.299 -27.693  1.00 98.82           O  
ANISOU 1113  O   TYR B 137    12609  12652  12285   1046   3047  -1596       O  
ATOM   1114  CB  TYR B 137      42.990  -5.976 -29.631  1.00 76.68           C  
ANISOU 1114  CB  TYR B 137    10694   9660   8781    764   2836  -1630       C  
ATOM   1115  CG  TYR B 137      42.517  -5.092 -28.498  1.00 79.14           C  
ANISOU 1115  CG  TYR B 137    10877   9927   9266    611   2598  -1423       C  
ATOM   1116  CD1 TYR B 137      42.757  -3.711 -28.497  1.00 78.24           C  
ANISOU 1116  CD1 TYR B 137    10671   9929   9129    426   2660  -1237       C  
ATOM   1117  CD2 TYR B 137      41.767  -5.627 -27.453  1.00 79.19           C  
ANISOU 1117  CD2 TYR B 137    10885   9760   9445    642   2321  -1416       C  
ATOM   1118  CE1 TYR B 137      42.281  -2.897 -27.460  1.00 74.35           C  
ANISOU 1118  CE1 TYR B 137    10090   9372   8787    299   2441  -1083       C  
ATOM   1119  CE2 TYR B 137      41.289  -4.824 -26.435  1.00 82.68           C  
ANISOU 1119  CE2 TYR B 137    11226  10178  10011    517   2118  -1250       C  
ATOM   1120  CZ  TYR B 137      41.548  -3.460 -26.438  1.00 79.34           C  
ANISOU 1120  CZ  TYR B 137    10714   9865   9566    356   2174  -1100       C  
ATOM   1121  OH  TYR B 137      41.057  -2.687 -25.402  1.00 78.58           O  
ANISOU 1121  OH  TYR B 137    10538   9724   9593    250   1974   -972       O  
ATOM   1122  N   TYR B 138      44.607  -8.135 -28.202  1.00 94.67           N  
ANISOU 1122  N   TYR B 138    12557  11785  11627   1263   2904  -1848       N  
ATOM   1123  CA  TYR B 138      44.975  -8.815 -26.971  1.00 93.91           C  
ANISOU 1123  CA  TYR B 138    12258  11578  11846   1439   2767  -1820       C  
ATOM   1124  C   TYR B 138      46.451  -9.212 -26.984  1.00101.87           C  
ANISOU 1124  C   TYR B 138    12952  12735  13018   1691   3009  -1900       C  
ATOM   1125  O   TYR B 138      47.069  -9.362 -28.044  1.00102.79           O  
ANISOU 1125  O   TYR B 138    13078  12977  13002   1780   3301  -2045       O  
ATOM   1126  CB  TYR B 138      44.065 -10.022 -26.768  1.00 88.43           C  
ANISOU 1126  CB  TYR B 138    11848  10571  11181   1536   2584  -1921       C  
ATOM   1127  CG  TYR B 138      42.622  -9.585 -26.627  1.00 87.03           C  
ANISOU 1127  CG  TYR B 138    11893  10296  10877   1281   2334  -1831       C  
ATOM   1128  CD1 TYR B 138      42.115  -9.204 -25.395  1.00 74.78           C  
ANISOU 1128  CD1 TYR B 138    10235   8703   9473   1181   2095  -1646       C  
ATOM   1129  CD2 TYR B 138      41.773  -9.505 -27.739  1.00 88.84           C  
ANISOU 1129  CD2 TYR B 138    12422  10515  10820   1149   2338  -1935       C  
ATOM   1130  CE1 TYR B 138      40.812  -8.771 -25.260  1.00 68.88           C  
ANISOU 1130  CE1 TYR B 138     9650   7900   8621    969   1889  -1570       C  
ATOM   1131  CE2 TYR B 138      40.452  -9.075 -27.603  1.00 79.62           C  
ANISOU 1131  CE2 TYR B 138    11406   9296   9549    936   2097  -1851       C  
ATOM   1132  CZ  TYR B 138      39.986  -8.708 -26.354  1.00 76.04           C  
ANISOU 1132  CZ  TYR B 138    10817   8798   9275    853   1885  -1668       C  
ATOM   1133  OH  TYR B 138      38.686  -8.272 -26.175  1.00 83.47           O  
ANISOU 1133  OH  TYR B 138    11870   9713  10133    666   1664  -1589       O  
ATOM   1134  N   ALA B 139      47.033  -9.320 -25.782  1.00105.33           N  
ANISOU 1134  N   ALA B 139    13088  13199  13735   1807   2884  -1800       N  
ATOM   1135  CA  ALA B 139      48.431  -9.731 -25.666  1.00107.28           C  
ANISOU 1135  CA  ALA B 139    12978  13611  14171   2079   3069  -1867       C  
ATOM   1136  C   ALA B 139      48.616 -11.154 -26.157  1.00103.79           C  
ANISOU 1136  C   ALA B 139    12706  12972  13756   2423   3185  -2073       C  
ATOM   1137  O   ALA B 139      49.683 -11.512 -26.667  1.00100.21           O  
ANISOU 1137  O   ALA B 139    12050  12670  13357   2662   3451  -2206       O  
ATOM   1138  CB  ALA B 139      48.904  -9.603 -24.217  1.00109.11           C  
ANISOU 1138  CB  ALA B 139    12875  13913  14671   2145   2848  -1713       C  
ATOM   1139  N   ASP B 140      47.588 -11.975 -25.978  1.00105.76           N  
ANISOU 1139  N   ASP B 140    13318  12880  13987   2450   2993  -2107       N  
ATOM   1140  CA  ASP B 140      47.421 -13.251 -26.645  1.00106.77           C  
ANISOU 1140  CA  ASP B 140    13748  12736  14082   2682   3088  -2336       C  
ATOM   1141  C   ASP B 140      47.777 -13.139 -28.125  1.00109.45           C  
ANISOU 1141  C   ASP B 140    14182  13235  14170   2691   3419  -2556       C  
ATOM   1142  O   ASP B 140      48.465 -13.998 -28.689  1.00114.44           O  
ANISOU 1142  O   ASP B 140    14814  13844  14822   2975   3593  -2754       O  
ATOM   1143  CB  ASP B 140      45.969 -13.686 -26.455  1.00104.69           C  
ANISOU 1143  CB  ASP B 140    13888  12140  13750   2506   2832  -2325       C  
ATOM   1144  CG  ASP B 140      45.746 -15.126 -26.763  1.00113.98           C  
ANISOU 1144  CG  ASP B 140    15378  12945  14984   2731   2853  -2533       C  
ATOM   1145  OD1 ASP B 140      46.703 -15.816 -27.190  1.00120.08           O  
ANISOU 1145  OD1 ASP B 140    16084  13707  15834   3057   3069  -2704       O  
ATOM   1146  OD2 ASP B 140      44.595 -15.568 -26.571  1.00116.77           O1-
ANISOU 1146  OD2 ASP B 140    16037  13014  15315   2571   2650  -2531       O1-
ATOM   1147  N   GLY B 141      47.301 -12.073 -28.764  1.00107.62           N  
ANISOU 1147  N   GLY B 141    14029  13187  13673   2370   3457  -2497       N  
ATOM   1148  CA  GLY B 141      47.447 -11.873 -30.193  1.00104.19           C  
ANISOU 1148  CA  GLY B 141    13751  12914  12921   2329   3746  -2667       C  
ATOM   1149  C   GLY B 141      46.149 -11.923 -30.971  1.00 98.82           C  
ANISOU 1149  C   GLY B 141    13529  12090  11929   2125   3625  -2758       C  
ATOM   1150  O   GLY B 141      46.177 -11.753 -32.190  1.00102.10           O  
ANISOU 1150  O   GLY B 141    14100  12666  12027   2071   3795  -2876       O  
ATOM   1151  N   GLU B 142      45.017 -12.154 -30.315  1.00 94.18           N  
ANISOU 1151  N   GLU B 142    13127  11249  11410   1994   3291  -2686       N  
ATOM   1152  CA  GLU B 142      43.742 -12.248 -31.005  1.00 91.53           C  
ANISOU 1152  CA  GLU B 142    13181  10796  10801   1796   3140  -2784       C  
ATOM   1153  C   GLU B 142      43.214 -10.855 -31.332  1.00 89.37           C  
ANISOU 1153  C   GLU B 142    12908  10760  10287   1500   3082  -2587       C  
ATOM   1154  O   GLU B 142      43.353  -9.916 -30.540  1.00 92.88           O  
ANISOU 1154  O   GLU B 142    13104  11313  10872   1383   3004  -2335       O  
ATOM   1155  CB  GLU B 142      42.735 -13.006 -30.140  1.00 92.50           C  
ANISOU 1155  CB  GLU B 142    13457  10577  11113   1748   2821  -2767       C  
ATOM   1156  CG  GLU B 142      41.380 -13.233 -30.784  1.00 98.98           C  
ANISOU 1156  CG  GLU B 142    14666  11237  11705   1583   2668  -2950       C  
ATOM   1157  CD  GLU B 142      40.442 -14.034 -29.891  1.00100.69           C  
ANISOU 1157  CD  GLU B 142    14986  11133  12139   1486   2372  -2902       C  
ATOM   1158  OE1 GLU B 142      40.840 -14.377 -28.757  1.00100.54           O  
ANISOU 1158  OE1 GLU B 142    14768  11010  12421   1573   2299  -2718       O  
ATOM   1159  OE2 GLU B 142      39.306 -14.322 -30.318  1.00 99.42           O1-
ANISOU 1159  OE2 GLU B 142    15098  10841  11837   1312   2213  -3044       O1-
ATOM   1160  N   ASP B 143      42.611 -10.721 -32.509  1.00 84.91           N  
ANISOU 1160  N   ASP B 143    12639  10271   9353   1391   3114  -2707       N  
ATOM   1161  CA  ASP B 143      41.917  -9.491 -32.855  1.00 78.27           C  
ANISOU 1161  CA  ASP B 143    11866   9606   8268   1137   3011  -2511       C  
ATOM   1162  C   ASP B 143      40.708  -9.296 -31.950  1.00 75.76           C  
ANISOU 1162  C   ASP B 143    11570   9130   8085    970   2635  -2365       C  
ATOM   1163  O   ASP B 143      40.103 -10.258 -31.462  1.00 74.18           O  
ANISOU 1163  O   ASP B 143    11462   8685   8037    998   2449  -2477       O  
ATOM   1164  CB  ASP B 143      41.464  -9.521 -34.313  1.00 81.95           C  
ANISOU 1164  CB  ASP B 143    12669  10190   8276   1088   3086  -2679       C  
ATOM   1165  CG  ASP B 143      42.586  -9.851 -35.256  1.00 91.64           C  
ANISOU 1165  CG  ASP B 143    13897  11582   9340   1266   3465  -2856       C  
ATOM   1166  OD1 ASP B 143      43.744  -9.759 -34.818  1.00 95.26           O  
ANISOU 1166  OD1 ASP B 143    14043  12118  10032   1391   3687  -2792       O  
ATOM   1167  OD2 ASP B 143      42.323 -10.193 -36.432  1.00100.50           O1-
ANISOU 1167  OD2 ASP B 143    15245  12805  10135   1270   3461  -3021       O1-
ATOM   1168  N   ALA B 144      40.368  -8.034 -31.717  1.00 72.97           N  
ANISOU 1168  N   ALA B 144    11133   8909   7685    795   2543  -2112       N  
ATOM   1169  CA  ALA B 144      39.166  -7.662 -30.995  1.00 67.45           C  
ANISOU 1169  CA  ALA B 144    10451   8117   7059    641   2215  -1972       C  
ATOM   1170  C   ALA B 144      38.155  -7.084 -31.968  1.00 72.85           C  
ANISOU 1170  C   ALA B 144    11381   8914   7384    504   2093  -1953       C  
ATOM   1171  O   ALA B 144      38.522  -6.504 -32.993  1.00 73.57           O  
ANISOU 1171  O   ALA B 144    11579   9190   7185    495   2273  -1929       O  
ATOM   1172  CB  ALA B 144      39.467  -6.630 -29.910  1.00 63.43           C  
ANISOU 1172  CB  ALA B 144     9666   7654   6779    572   2172  -1710       C  
ATOM   1173  N   TYR B 145      36.879  -7.296 -31.674  1.00 70.71           N  
ANISOU 1173  N   TYR B 145    11197   8548   7121    405   1790  -1965       N  
ATOM   1174  CA  TYR B 145      35.834  -6.480 -32.256  1.00 61.82           C  
ANISOU 1174  CA  TYR B 145    10209   7555   5727    283   1604  -1866       C  
ATOM   1175  C   TYR B 145      35.616  -5.329 -31.310  1.00 61.19           C  
ANISOU 1175  C   TYR B 145     9936   7489   5825    216   1503  -1584       C  
ATOM   1176  O   TYR B 145      35.613  -5.520 -30.096  1.00 59.92           O  
ANISOU 1176  O   TYR B 145     9584   7203   5980    216   1425  -1533       O  
ATOM   1177  CB  TYR B 145      34.506  -7.222 -32.397  1.00 57.51           C  
ANISOU 1177  CB  TYR B 145     9802   6936   5114    198   1313  -2026       C  
ATOM   1178  CG  TYR B 145      34.368  -8.286 -33.450  1.00 66.13           C  
ANISOU 1178  CG  TYR B 145    11146   8011   5972    216   1330  -2342       C  
ATOM   1179  CD1 TYR B 145      34.512  -8.004 -34.793  1.00 61.91           C  
ANISOU 1179  CD1 TYR B 145    10828   7678   5017    240   1429  -2420       C  
ATOM   1180  CD2 TYR B 145      34.026  -9.581 -33.081  1.00 67.45           C  
ANISOU 1180  CD2 TYR B 145    11357   7944   6328    194   1235  -2567       C  
ATOM   1181  CE1 TYR B 145      34.352  -8.999 -35.716  1.00 72.67           C  
ANISOU 1181  CE1 TYR B 145    12434   9026   6150    253   1430  -2746       C  
ATOM   1182  CE2 TYR B 145      33.869 -10.560 -33.990  1.00 62.90           C  
ANISOU 1182  CE2 TYR B 145    11026   7311   5561    194   1238  -2886       C  
ATOM   1183  CZ  TYR B 145      34.022 -10.288 -35.298  1.00 75.54           C  
ANISOU 1183  CZ  TYR B 145    12833   9130   6741    225   1327  -2997       C  
ATOM   1184  OH  TYR B 145      33.840 -11.337 -36.190  1.00 85.20           O  
ANISOU 1184  OH  TYR B 145    14322  10290   7759    221   1318  -3365       O  
ATOM   1185  N   ALA B 146      35.402  -4.145 -31.857  1.00 68.68           N  
ANISOU 1185  N   ALA B 146    10958   8578   6561    167   1498  -1403       N  
ATOM   1186  CA  ALA B 146      34.838  -3.059 -31.074  1.00 70.07           C  
ANISOU 1186  CA  ALA B 146    11017   8738   6868    107   1338  -1171       C  
ATOM   1187  C   ALA B 146      33.343  -3.045 -31.337  1.00 73.50           C  
ANISOU 1187  C   ALA B 146    11560   9216   7152     68   1029  -1184       C  
ATOM   1188  O   ALA B 146      32.904  -3.220 -32.482  1.00 75.09           O  
ANISOU 1188  O   ALA B 146    11972   9535   7025     71    973  -1269       O  
ATOM   1189  CB  ALA B 146      35.473  -1.715 -31.418  1.00 60.59           C  
ANISOU 1189  CB  ALA B 146     9834   7615   5573     80   1511   -944       C  
ATOM   1190  N   MET B 147      32.567  -2.900 -30.278  1.00 70.63           N  
ANISOU 1190  N   MET B 147    11038   8781   7017     36    827  -1118       N  
ATOM   1191  CA  MET B 147      31.121  -2.902 -30.393  1.00 73.15           C  
ANISOU 1191  CA  MET B 147    11384   9166   7244     -1    531  -1133       C  
ATOM   1192  C   MET B 147      30.602  -1.594 -29.833  1.00 72.44           C  
ANISOU 1192  C   MET B 147    11198   9099   7226     23    423   -898       C  
ATOM   1193  O   MET B 147      31.145  -1.070 -28.858  1.00 67.37           O  
ANISOU 1193  O   MET B 147    10412   8362   6822     29    518   -789       O  
ATOM   1194  CB  MET B 147      30.515  -4.093 -29.659  1.00 80.47           C  
ANISOU 1194  CB  MET B 147    12203   9992   8381    -68    396  -1300       C  
ATOM   1195  CG  MET B 147      31.103  -5.438 -30.097  1.00 85.88           C  
ANISOU 1195  CG  MET B 147    13002  10578   9050    -74    519  -1544       C  
ATOM   1196  SD  MET B 147      30.282  -6.891 -29.415  1.00 84.57           S  
ANISOU 1196  SD  MET B 147    12784  10242   9108   -189    355  -1735       S  
ATOM   1197  CE  MET B 147      28.735  -6.820 -30.293  1.00 86.79           C  
ANISOU 1197  CE  MET B 147    13138  10709   9129   -308     47  -1828       C  
ATOM   1198  N   LYS B 148      29.592  -1.040 -30.485  1.00 77.02           N  
ANISOU 1198  N   LYS B 148    11867   9807   7588     52    222   -830       N  
ATOM   1199  CA  LYS B 148      28.981   0.202 -30.049  1.00 73.46           C  
ANISOU 1199  CA  LYS B 148    11351   9365   7194    118    103   -618       C  
ATOM   1200  C   LYS B 148      27.518  -0.078 -29.757  1.00 69.95           C  
ANISOU 1200  C   LYS B 148    10774   9020   6783    118   -195   -679       C  
ATOM   1201  O   LYS B 148      26.887  -0.886 -30.444  1.00 68.24           O  
ANISOU 1201  O   LYS B 148    10604   8921   6401     68   -345   -838       O  
ATOM   1202  CB  LYS B 148      29.098   1.314 -31.113  1.00 80.79           C  
ANISOU 1202  CB  LYS B 148    12504  10362   7831    199    135   -422       C  
ATOM   1203  CG  LYS B 148      30.498   1.582 -31.676  1.00 89.55           C  
ANISOU 1203  CG  LYS B 148    13762  11423   8841    169    454   -356       C  
ATOM   1204  CD  LYS B 148      30.520   2.864 -32.555  1.00 99.39           C  
ANISOU 1204  CD  LYS B 148    15237  12697   9829    234    490    -93       C  
ATOM   1205  CE  LYS B 148      31.944   3.219 -33.060  1.00106.07           C  
ANISOU 1205  CE  LYS B 148    16204  13501  10598    165    850      1       C  
ATOM   1206  NZ  LYS B 148      31.984   4.325 -34.090  1.00107.63           N1+
ANISOU 1206  NZ  LYS B 148    16681  13729  10486    206    915    272       N1+
ATOM   1207  N   ARG B 149      26.988   0.569 -28.726  1.00 68.96           N  
ANISOU 1207  N   ARG B 149    10468   8856   6875    163   -275   -574       N  
ATOM   1208  CA  ARG B 149      25.550   0.649 -28.500  1.00 69.42           C  
ANISOU 1208  CA  ARG B 149    10372   9051   6953    200   -544   -582       C  
ATOM   1209  C   ARG B 149      25.180   2.118 -28.578  1.00 68.49           C  
ANISOU 1209  C   ARG B 149    10292   8945   6784    375   -613   -362       C  
ATOM   1210  O   ARG B 149      25.740   2.930 -27.838  1.00 60.85           O  
ANISOU 1210  O   ARG B 149     9312   7822   5988    420   -474   -246       O  
ATOM   1211  CB  ARG B 149      25.160   0.047 -27.148  1.00 73.85           C  
ANISOU 1211  CB  ARG B 149    10675   9566   7817    119   -559   -663       C  
ATOM   1212  CG  ARG B 149      23.716   0.280 -26.723  1.00 84.96           C  
ANISOU 1212  CG  ARG B 149    11862  11130   9289    162   -787   -652       C  
ATOM   1213  CD  ARG B 149      23.545  -0.199 -25.268  1.00 96.99           C  
ANISOU 1213  CD  ARG B 149    13155  12594  11103     78   -725   -694       C  
ATOM   1214  NE  ARG B 149      22.314   0.269 -24.621  1.00102.60           N  
ANISOU 1214  NE  ARG B 149    13622  13452  11911    149   -870   -655       N  
ATOM   1215  CZ  ARG B 149      21.906  -0.114 -23.412  1.00 99.94           C  
ANISOU 1215  CZ  ARG B 149    13066  13127  11780     78   -832   -684       C  
ATOM   1216  NH1 ARG B 149      22.611  -0.991 -22.712  1.00 99.16           N1+
ANISOU 1216  NH1 ARG B 149    12980  12887  11809    -60   -678   -733       N1+
ATOM   1217  NH2 ARG B 149      20.776   0.358 -22.912  1.00100.69           N  
ANISOU 1217  NH2 ARG B 149    12926  13389  11942    161   -943   -656       N  
ATOM   1218  N   ASP B 150      24.291   2.459 -29.514  1.00 76.00           N  
ANISOU 1218  N   ASP B 150    11311  10072   7492    479   -831   -309       N  
ATOM   1219  CA  ASP B 150      23.832   3.832 -29.663  1.00 69.97           C  
ANISOU 1219  CA  ASP B 150    10607   9307   6673    689   -925    -84       C  
ATOM   1220  C   ASP B 150      23.027   4.240 -28.449  1.00 74.94           C  
ANISOU 1220  C   ASP B 150    10967   9925   7584    775  -1012    -75       C  
ATOM   1221  O   ASP B 150      22.120   3.517 -28.019  1.00 79.65           O  
ANISOU 1221  O   ASP B 150    11311  10677   8273    720  -1159   -216       O  
ATOM   1222  CB  ASP B 150      22.971   3.992 -30.912  1.00 76.87           C  
ANISOU 1222  CB  ASP B 150    11587  10411   7210    808  -1182    -32       C  
ATOM   1223  CG  ASP B 150      22.261   5.351 -30.963  1.00 87.44           C  
ANISOU 1223  CG  ASP B 150    12947  11752   8524   1076  -1331    206       C  
ATOM   1224  OD1 ASP B 150      22.900   6.342 -31.389  1.00 88.49           O  
ANISOU 1224  OD1 ASP B 150    13347  11722   8553   1175  -1205    429       O  
ATOM   1225  OD2 ASP B 150      21.073   5.431 -30.553  1.00 89.77           O1-
ANISOU 1225  OD2 ASP B 150    12987  12201   8920   1190  -1561    174       O1-
ATOM   1226  N   LEU B 151      23.357   5.409 -27.900  1.00 75.72           N  
ANISOU 1226  N   LEU B 151    11121   9834   7813    899   -907     83       N  
ATOM   1227  CA  LEU B 151      22.722   5.908 -26.689  1.00 69.09           C  
ANISOU 1227  CA  LEU B 151    10059   8962   7232   1002   -945     78       C  
ATOM   1228  C   LEU B 151      21.714   7.009 -26.948  1.00 75.04           C  
ANISOU 1228  C   LEU B 151    10810   9766   7934   1286  -1136    227       C  
ATOM   1229  O   LEU B 151      21.194   7.572 -25.986  1.00 73.09           O  
ANISOU 1229  O   LEU B 151    10400   9480   7891   1416  -1149    222       O  
ATOM   1230  CB  LEU B 151      23.785   6.426 -25.721  1.00 64.08           C  
ANISOU 1230  CB  LEU B 151     9473   8064   6810    945   -701    101       C  
ATOM   1231  CG  LEU B 151      24.510   5.347 -24.922  1.00 63.18           C  
ANISOU 1231  CG  LEU B 151     9234   7928   6843    726   -551    -61       C  
ATOM   1232  CD1 LEU B 151      25.451   5.974 -23.924  1.00 57.82           C  
ANISOU 1232  CD1 LEU B 151     8571   7037   6361    694   -363    -43       C  
ATOM   1233  CD2 LEU B 151      23.524   4.433 -24.199  1.00 63.22           C  
ANISOU 1233  CD2 LEU B 151     8954   8113   6953    680   -668   -203       C  
ATOM   1234  N   THR B 152      21.415   7.351 -28.209  1.00 76.52           N  
ANISOU 1234  N   THR B 152    11182  10047   7845   1411  -1285    360       N  
ATOM   1235  CA  THR B 152      20.592   8.546 -28.388  1.00 76.57           C  
ANISOU 1235  CA  THR B 152    11221  10045   7827   1730  -1450    542       C  
ATOM   1236  C   THR B 152      19.104   8.279 -28.134  1.00 78.27           C  
ANISOU 1236  C   THR B 152    11081  10565   8094   1875  -1721    447       C  
ATOM   1237  O   THR B 152      18.376   9.222 -27.807  1.00 83.65           O  
ANISOU 1237  O   THR B 152    11683  11227   8873   2162  -1820    546       O  
ATOM   1238  CB  THR B 152      20.821   9.184 -29.775  1.00 76.22           C  
ANISOU 1238  CB  THR B 152    11531   9972   7457   1855  -1511    777       C  
ATOM   1239  CG2 THR B 152      22.305   9.254 -30.118  1.00 70.63           C  
ANISOU 1239  CG2 THR B 152    11130   9027   6680   1655  -1215    850       C  
ATOM   1240  OG1 THR B 152      20.113   8.492 -30.806  1.00 77.58           O  
ANISOU 1240  OG1 THR B 152    11661  10480   7336   1867  -1764    730       O  
ATOM   1241  N   GLN B 153      18.617   7.035 -28.262  1.00 77.52           N  
ANISOU 1241  N   GLN B 153    10759  10744   7952   1686  -1839    252       N  
ATOM   1242  CA  GLN B 153      17.207   6.818 -27.944  1.00 85.69           C  
ANISOU 1242  CA  GLN B 153    11406  12081   9071   1790  -2075    160       C  
ATOM   1243  C   GLN B 153      16.982   6.829 -26.447  1.00 89.50           C  
ANISOU 1243  C   GLN B 153    11614  12507   9884   1772  -1930     63       C  
ATOM   1244  O   GLN B 153      16.006   7.407 -25.957  1.00 97.04           O  
ANISOU 1244  O   GLN B 153    12324  13587  10961   2008  -2034     80       O  
ATOM   1245  CB  GLN B 153      16.653   5.536 -28.593  1.00 91.40           C  
ANISOU 1245  CB  GLN B 153    11964  13116   9646   1571  -2268    -23       C  
ATOM   1246  CG  GLN B 153      15.114   5.388 -28.412  1.00106.52           C  
ANISOU 1246  CG  GLN B 153    13440  15396  11636   1673  -2545   -106       C  
ATOM   1247  CD  GLN B 153      14.313   6.198 -29.464  1.00122.08           C  
ANISOU 1247  CD  GLN B 153    15435  17586  13365   2005  -2865     50       C  
ATOM   1248  NE2 GLN B 153      14.703   6.088 -30.734  1.00125.60           N  
ANISOU 1248  NE2 GLN B 153    16187  18069  13466   1983  -2977    110       N  
ATOM   1249  OE1 GLN B 153      13.356   6.914 -29.118  1.00126.17           O  
ANISOU 1249  OE1 GLN B 153    15697  18245  13997   2297  -3007    119       O  
ATOM   1250  N   MET B 154      17.879   6.209 -25.713  1.00 87.74           N  
ANISOU 1250  N   MET B 154    11430  12115   9793   1518  -1688    -37       N  
ATOM   1251  CA  MET B 154      17.818   6.343 -24.271  1.00 81.86           C  
ANISOU 1251  CA  MET B 154    10491  11297   9315   1517  -1529   -104       C  
ATOM   1252  C   MET B 154      17.832   7.808 -23.851  1.00 84.61           C  
ANISOU 1252  C   MET B 154    10943  11451   9753   1821  -1477     23       C  
ATOM   1253  O   MET B 154      17.019   8.240 -23.024  1.00 91.72           O  
ANISOU 1253  O   MET B 154    11604  12439  10806   1999  -1494    -17       O  
ATOM   1254  CB  MET B 154      18.978   5.592 -23.614  1.00 72.12           C  
ANISOU 1254  CB  MET B 154     9350   9877   8174   1235  -1284   -190       C  
ATOM   1255  CG  MET B 154      18.804   5.469 -22.146  1.00 73.18           C  
ANISOU 1255  CG  MET B 154     9261  10013   8531   1197  -1151   -276       C  
ATOM   1256  SD  MET B 154      20.228   4.872 -21.265  1.00 78.89           S  
ANISOU 1256  SD  MET B 154    10111  10505   9356    954   -886   -333       S  
ATOM   1257  CE  MET B 154      20.056   3.122 -21.508  1.00 85.35           C  
ANISOU 1257  CE  MET B 154    10810  11469  10149    654   -921   -453       C  
ATOM   1258  N   ALA B 155      18.743   8.589 -24.421  1.00 81.74           N  
ANISOU 1258  N   ALA B 155    10943  10815   9301   1881  -1398    171       N  
ATOM   1259  CA  ALA B 155      18.805   9.998 -24.063  1.00 80.19           C  
ANISOU 1259  CA  ALA B 155    10895  10367   9206   2148  -1343    289       C  
ATOM   1260  C   ALA B 155      17.467  10.684 -24.318  1.00 83.50           C  
ANISOU 1260  C   ALA B 155    11160  10953   9612   2514  -1574    363       C  
ATOM   1261  O   ALA B 155      17.000  11.478 -23.492  1.00 89.11           O  
ANISOU 1261  O   ALA B 155    11774  11585  10499   2749  -1541    342       O  
ATOM   1262  CB  ALA B 155      19.938  10.695 -24.824  1.00 72.48           C  
ANISOU 1262  CB  ALA B 155    10342   9077   8119   2120  -1232    466       C  
ATOM   1263  N   ASP B 156      16.805  10.342 -25.426  1.00 83.85           N  
ANISOU 1263  N   ASP B 156    11156  11258   9446   2578  -1818    427       N  
ATOM   1264  CA  ASP B 156      15.536  10.987 -25.755  1.00 88.46           C  
ANISOU 1264  CA  ASP B 156    11570  12039  10003   2956  -2073    511       C  
ATOM   1265  C   ASP B 156      14.432  10.560 -24.805  1.00 88.59           C  
ANISOU 1265  C   ASP B 156    11091  12359  10211   3000  -2124    326       C  
ATOM   1266  O   ASP B 156      13.592  11.379 -24.430  1.00 93.57           O  
ANISOU 1266  O   ASP B 156    11557  13038  10957   3353  -2197    355       O  
ATOM   1267  CB  ASP B 156      15.137  10.681 -27.194  1.00 94.32           C  
ANISOU 1267  CB  ASP B 156    12373  13026  10437   2996  -2348    615       C  
ATOM   1268  CG  ASP B 156      15.980  11.432 -28.195  1.00101.23           C  
ANISOU 1268  CG  ASP B 156    13744  13625  11095   3075  -2316    865       C  
ATOM   1269  OD1 ASP B 156      16.838  12.244 -27.771  1.00 99.07           O  
ANISOU 1269  OD1 ASP B 156    13748  12951  10944   3094  -2083    961       O  
ATOM   1270  OD2 ASP B 156      15.773  11.213 -29.409  1.00108.29           O1-
ANISOU 1270  OD2 ASP B 156    14749  14713  11684   3105  -2522    964       O1-
ATOM   1271  N   GLU B 157      14.415   9.283 -24.405  1.00 91.18           N  
ANISOU 1271  N   GLU B 157    11179  12887  10578   2650  -2069    139       N  
ATOM   1272  CA  GLU B 157      13.419   8.811 -23.446  1.00 98.46           C  
ANISOU 1272  CA  GLU B 157    11630  14099  11683   2633  -2069    -24       C  
ATOM   1273  C   GLU B 157      13.593   9.458 -22.077  1.00100.95           C  
ANISOU 1273  C   GLU B 157    11913  14225  12219   2750  -1826    -77       C  
ATOM   1274  O   GLU B 157      12.615   9.587 -21.329  1.00105.90           O  
ANISOU 1274  O   GLU B 157    12178  15076  12984   2908  -1827   -163       O  
ATOM   1275  CB  GLU B 157      13.489   7.289 -23.329  1.00102.43           C  
ANISOU 1275  CB  GLU B 157    11958  14781  12182   2196  -2036   -184       C  
ATOM   1276  CG  GLU B 157      13.249   6.563 -24.641  1.00116.42           C  
ANISOU 1276  CG  GLU B 157    13746  16757  13731   2056  -2284   -193       C  
ATOM   1277  CD  GLU B 157      13.498   5.068 -24.530  1.00123.52           C  
ANISOU 1277  CD  GLU B 157    14562  17725  14644   1609  -2219   -362       C  
ATOM   1278  OE1 GLU B 157      13.784   4.426 -25.571  1.00125.67           O  
ANISOU 1278  OE1 GLU B 157    15000  18030  14718   1437  -2339   -395       O  
ATOM   1279  OE2 GLU B 157      13.413   4.539 -23.398  1.00125.97           O1-
ANISOU 1279  OE2 GLU B 157    14665  18046  15154   1437  -2039   -461       O1-
ATOM   1280  N   LEU B 158      14.822   9.873 -21.738  1.00 98.25           N  
ANISOU 1280  N   LEU B 158    11931  13496  11903   2670  -1615    -41       N  
ATOM   1281  CA  LEU B 158      15.116  10.530 -20.464  1.00 96.79           C  
ANISOU 1281  CA  LEU B 158    11770  13109  11898   2761  -1395   -116       C  
ATOM   1282  C   LEU B 158      14.664  11.984 -20.455  1.00107.17           C  
ANISOU 1282  C   LEU B 158    13181  14259  13279   3209  -1444    -34       C  
ATOM   1283  O   LEU B 158      14.146  12.463 -19.437  1.00112.10           O  
ANISOU 1283  O   LEU B 158    13630  14911  14053   3404  -1349   -145       O  
ATOM   1284  CB  LEU B 158      16.615  10.464 -20.176  1.00 89.34           C  
ANISOU 1284  CB  LEU B 158    11161  11827  10958   2501  -1186   -119       C  
ATOM   1285  CG  LEU B 158      17.232   9.091 -19.916  1.00 81.82           C  
ANISOU 1285  CG  LEU B 158    10143  10964   9981   2095  -1087   -211       C  
ATOM   1286  CD1 LEU B 158      18.677   9.251 -19.585  1.00 76.49           C  
ANISOU 1286  CD1 LEU B 158     9764   9968   9330   1923   -896   -209       C  
ATOM   1287  CD2 LEU B 158      16.514   8.395 -18.782  1.00 81.43           C  
ANISOU 1287  CD2 LEU B 158     9727  11173  10040   2013  -1016   -356       C  
ATOM   1288  N   ARG B 159      14.860  12.694 -21.578  1.00112.13           N  
ANISOU 1288  N   ARG B 159    14110  14705  13790   3385  -1579    164       N  
ATOM   1289  CA  ARG B 159      14.519  14.113 -21.646  1.00118.48           C  
ANISOU 1289  CA  ARG B 159    15081  15271  14664   3824  -1625    277       C  
ATOM   1290  C   ARG B 159      13.014  14.327 -21.569  1.00131.80           C  
ANISOU 1290  C   ARG B 159    16370  17299  16407   4203  -1810    247       C  
ATOM   1291  O   ARG B 159      12.547  15.333 -21.017  1.00140.79           O  
ANISOU 1291  O   ARG B 159    17497  18304  17693   4578  -1774    227       O  
ATOM   1292  CB  ARG B 159      15.104  14.734 -22.920  1.00117.43           C  
ANISOU 1292  CB  ARG B 159    15385  14868  14366   3896  -1719    538       C  
ATOM   1293  CG  ARG B 159      14.720  16.211 -23.147  1.00127.24           C  
ANISOU 1293  CG  ARG B 159    16855  15820  15672   4374  -1791    708       C  
ATOM   1294  CD  ARG B 159      13.975  16.422 -24.480  1.00133.41           C  
ANISOU 1294  CD  ARG B 159    17664  16783  16245   4662  -2099    947       C  
ATOM   1295  NE  ARG B 159      13.566  17.808 -24.729  1.00137.62           N  
ANISOU 1295  NE  ARG B 159    18427  17025  16839   5160  -2185   1143       N  
ATOM   1296  CZ  ARG B 159      12.337  18.168 -25.101  1.00139.16           C  
ANISOU 1296  CZ  ARG B 159    18395  17466  17012   5614  -2449   1228       C  
ATOM   1297  NH1 ARG B 159      11.403  17.240 -25.257  1.00137.76           N1+
ANISOU 1297  NH1 ARG B 159    17730  17854  16759   5590  -2651   1115       N1+
ATOM   1298  NH2 ARG B 159      12.040  19.450 -25.319  1.00140.57           N  
ANISOU 1298  NH2 ARG B 159    18790  17334  17284   5904  -2442   1388       N  
ATOM   1299  N   ARG B 160      12.250  13.404 -22.130  1.00135.11           N  
ANISOU 1299  N   ARG B 160    16457  18158  16719   4113  -2010    231       N  
ATOM   1300  CA  ARG B 160      10.781  13.392 -22.014  1.00142.56           C  
ANISOU 1300  CA  ARG B 160    16910  19527  17729   4403  -2189    170       C  
ATOM   1301  C   ARG B 160      10.321  13.571 -20.568  1.00144.23           C  
ANISOU 1301  C   ARG B 160    16827  19809  18165   4507  -1974    -28       C  
ATOM   1302  O   ARG B 160      10.701  12.807 -19.676  1.00140.30           O  
ANISOU 1302  O   ARG B 160    16226  19357  17723   4161  -1762   -185       O  
ATOM   1303  CB  ARG B 160      10.230  12.076 -22.570  1.00144.09           C  
ANISOU 1303  CB  ARG B 160    16757  20185  17806   4106  -2371    104       C  
ATOM   1304  CG  ARG B 160      10.006  12.021 -24.085  1.00149.41           C  
ANISOU 1304  CG  ARG B 160    17537  20998  18232   4183  -2699    270       C  
ATOM   1305  CD  ARG B 160       8.996  10.917 -24.417  1.00155.87           C  
ANISOU 1305  CD  ARG B 160    17858  22365  19002   4001  -2924    141       C  
ATOM   1306  NE  ARG B 160       8.724  10.072 -23.250  1.00158.72           N  
ANISOU 1306  NE  ARG B 160    17842  22906  19560   3710  -2718    -78       N  
ATOM   1307  CZ  ARG B 160       9.217   8.848 -23.068  1.00157.55           C  
ANISOU 1307  CZ  ARG B 160    17684  22782  19395   3210  -2602   -200       C  
ATOM   1308  NH1 ARG B 160       8.919   8.168 -21.966  1.00155.95           N1+
ANISOU 1308  NH1 ARG B 160    17157  22728  19368   2980  -2406   -358       N1+
ATOM   1309  NH2 ARG B 160      10.008   8.303 -23.986  1.00156.53           N  
ANISOU 1309  NH2 ARG B 160    17884  22524  19068   2952  -2670   -156       N  
TER    1310      ARG B 160 
HETATM 1311  O   HOH B 301      22.944   3.627  -6.649  1.00 57.11           O  
CONECT    1    2    3    4
CONECT    2    1
CONECT    3    1
CONECT    4    1
END


A second structure was input as follows:


ATOM      1  N   ASP B   2      29.421  26.128  14.039  1.00 50.43           N  
ANISOU    1  N   ASP B   2     6898   6491   5771    969  -1058     46       N  
ATOM      2  CA  ASP B   2      29.045  25.707  12.700  1.00 45.64           C  
ANISOU    2  CA  ASP B   2     6250   5836   5253    984   -952     54       C  
ATOM      3  C   ASP B   2      28.106  26.723  12.057  1.00 34.83           C  
ANISOU    3  C   ASP B   2     4869   4468   3895    856   -831     17       C  
ATOM      4  O   ASP B   2      28.131  26.888  10.846  1.00 33.15           O  
ANISOU    4  O   ASP B   2     4548   4255   3793    813   -742    -13       O  
ATOM      5  CB  ASP B   2      28.395  24.316  12.714  1.00 51.69           C  
ANISOU    5  CB  ASP B   2     7163   6493   5984   1026   -869    137       C  
ATOM      6  CG  ASP B   2      29.327  23.225  12.210  1.00 60.62           C  
ANISOU    6  CG  ASP B   2     8221   7596   7216   1135   -892    151       C  
ATOM      7  OD1 ASP B   2      30.553  23.335  12.448  1.00 67.11           O  
ANISOU    7  OD1 ASP B   2     8911   8488   8099   1196  -1003    122       O  
ATOM      8  OD2 ASP B   2      28.840  22.255  11.576  1.00 59.16           O1-
ANISOU    8  OD2 ASP B   2     8107   7319   7052   1155   -794    188       O1-
ATOM      9  N   ILE B   3      27.278  27.390  12.861  1.00 29.48           N  
ANISOU    9  N   ILE B   3     4305   3787   3109    787   -811     17       N  
ATOM     10  CA  ILE B   3      26.310  28.376  12.347  1.00 22.76           C  
ANISOU   10  CA  ILE B   3     3443   2927   2279    670   -685    -14       C  
ATOM     11  C   ILE B   3      26.513  29.749  12.970  1.00 20.95           C  
ANISOU   11  C   ILE B   3     3192   2750   2019    603   -732    -84       C  
ATOM     12  O   ILE B   3      26.594  29.880  14.189  1.00 21.61           O  
ANISOU   12  O   ILE B   3     3377   2849   1984    618   -812    -88       O  
ATOM     13  CB  ILE B   3      24.847  27.907  12.563  1.00 27.78           C  
ANISOU   13  CB  ILE B   3     4231   3490   2835    640   -566     47       C  
ATOM     14  CG1 ILE B   3      24.430  26.917  11.480  1.00 27.67           C  
ANISOU   14  CG1 ILE B   3     4205   3421   2889    648   -477     90       C  
ATOM     15  CG2 ILE B   3      23.881  29.074  12.503  1.00 26.37           C  
ANISOU   15  CG2 ILE B   3     4052   3312   2654    543   -472     13       C  
ATOM     16  CD1 ILE B   3      24.891  25.523  11.729  1.00 37.48           C  
ANISOU   16  CD1 ILE B   3     5521   4614   4104    749   -526    146       C  
ATOM     17  N   ARG B   4      26.576  30.783  12.141  1.00 17.37           N  
ANISOU   17  N   ARG B   4     2626   2314   1661    524   -678   -140       N  
ATOM     18  CA  ARG B   4      26.822  32.146  12.633  1.00 19.97           C  
ANISOU   18  CA  ARG B   4     2937   2676   1975    450   -712   -216       C  
ATOM     19  C   ARG B   4      26.100  33.135  11.721  1.00 17.25           C  
ANISOU   19  C   ARG B   4     2554   2294   1704    364   -586   -236       C  
ATOM     20  O   ARG B   4      25.713  32.776  10.606  1.00 17.45           O  
ANISOU   20  O   ARG B   4     2532   2295   1803    360   -503   -199       O  
ATOM     21  CB  ARG B   4      28.333  32.454  12.636  1.00 22.52           C  
ANISOU   21  CB  ARG B   4     3118   3078   2362    452   -842   -280       C  
ATOM     22  CG  ARG B   4      29.017  32.287  11.254  1.00 27.47           C  
ANISOU   22  CG  ARG B   4     3572   3725   3140    447   -802   -292       C  
ATOM     23  CD  ARG B   4      30.329  33.072  11.154  1.00 26.43           C  
ANISOU   23  CD  ARG B   4     3280   3672   3091    396   -885   -378       C  
ATOM     24  NE  ARG B   4      31.103  32.763   9.947  1.00 25.27           N  
ANISOU   24  NE  ARG B   4     2967   3553   3081    402   -844   -392       N  
ATOM     25  CZ  ARG B   4      31.019  33.420   8.788  1.00 20.53           C  
ANISOU   25  CZ  ARG B   4     2301   2933   2566    312   -728   -414       C  
ATOM     26  NH1 ARG B   4      30.169  34.422   8.638  1.00 17.91           N1+
ANISOU   26  NH1 ARG B   4     2050   2548   2207    221   -648   -417       N1+
ATOM     27  NH2 ARG B   4      31.779  33.055   7.764  1.00 17.83           N  
ANISOU   27  NH2 ARG B   4     1821   2622   2333    320   -685   -430       N  
ATOM     28  N   PRO B   5      25.900  34.373  12.191  1.00 18.74           N  
ANISOU   28  N   PRO B   5     2777   2474   1870    296   -574   -294       N  
ATOM     29  CA  PRO B   5      25.335  35.414  11.325  1.00 17.13           C  
ANISOU   29  CA  PRO B   5     2538   2226   1745    226   -468   -310       C  
ATOM     30  C   PRO B   5      26.116  35.584  10.009  1.00 19.82           C  
ANISOU   30  C   PRO B   5     2733   2587   2210    189   -459   -321       C  
ATOM     31  O   PRO B   5      27.337  35.462   9.976  1.00 18.28           O  
ANISOU   31  O   PRO B   5     2443   2451   2054    187   -542   -361       O  
ATOM     32  CB  PRO B   5      25.473  36.680  12.182  1.00 21.86           C  
ANISOU   32  CB  PRO B   5     3191   2813   2302    166   -492   -390       C  
ATOM     33  CG  PRO B   5      25.400  36.161  13.618  1.00 23.84           C  
ANISOU   33  CG  PRO B   5     3566   3084   2408    211   -561   -393       C  
ATOM     34  CD  PRO B   5      26.125  34.854  13.579  1.00 15.47           C  
ANISOU   34  CD  PRO B   5     2458   2078   1342    285   -655   -345       C  
ATOM     35  N   ALA B   6      25.402  35.864   8.929  1.00 19.43           N  
ANISOU   35  N   ALA B   6     2668   2495   2221    159   -357   -285       N  
ATOM     36  CA  ALA B   6      26.035  36.096   7.625  1.00 20.79           C  
ANISOU   36  CA  ALA B   6     2731   2678   2492    110   -327   -291       C  
ATOM     37  C   ALA B   6      26.689  37.469   7.578  1.00 22.34           C  
ANISOU   37  C   ALA B   6     2890   2866   2734     20   -334   -360       C  
ATOM     38  O   ALA B   6      26.194  38.408   8.198  1.00 23.08           O  
ANISOU   38  O   ALA B   6     3061   2912   2797     -9   -319   -386       O  
ATOM     39  CB  ALA B   6      24.995  35.973   6.522  1.00 17.59           C  
ANISOU   39  CB  ALA B   6     2343   2229   2112    102   -230   -224       C  
ATOM     40  N   ARG B   7      27.797  37.594   6.853  1.00 21.56           N  
ANISOU   40  N   ARG B   7     2674   2806   2711    -30   -343   -396       N  
ATOM     41  CA  ARG B   7      28.404  38.912   6.614  1.00 22.46           C  
ANISOU   41  CA  ARG B   7     2753   2900   2879   -141   -327   -458       C  
ATOM     42  C   ARG B   7      28.567  39.160   5.128  1.00 21.58           C  
ANISOU   42  C   ARG B   7     2589   2770   2842   -203   -235   -431       C  
ATOM     43  O   ARG B   7      28.510  38.218   4.340  1.00 17.87           O  
ANISOU   43  O   ARG B   7     2082   2324   2383   -161   -202   -386       O  
ATOM     44  CB  ARG B   7      29.773  39.023   7.274  1.00 27.57           C  
ANISOU   44  CB  ARG B   7     3301   3626   3550   -176   -429   -545       C  
ATOM     45  CG  ARG B   7      30.084  37.949   8.271  1.00 37.85           C  
ANISOU   45  CG  ARG B   7     4591   4998   4794    -75   -543   -545       C  
ATOM     46  CD  ARG B   7      31.574  37.980   8.570  1.00 51.58           C  
ANISOU   46  CD  ARG B   7     6178   6832   6586   -107   -649   -624       C  
ATOM     47  NE  ARG B   7      32.000  36.916   9.472  1.00 57.79           N  
ANISOU   47  NE  ARG B   7     6945   7690   7324      4   -779   -615       N  
ATOM     48  CZ  ARG B   7      32.099  37.060  10.789  1.00 59.96           C  
ANISOU   48  CZ  ARG B   7     7285   7992   7504     17   -900   -647       C  
ATOM     49  NH1 ARG B   7      31.804  38.225  11.352  1.00 61.61           N1+
ANISOU   49  NH1 ARG B   7     7584   8160   7663    -79   -896   -703       N1+
ATOM     50  NH2 ARG B   7      32.494  36.042  11.541  1.00 60.28           N  
ANISOU   50  NH2 ARG B   7     7317   8092   7493    127  -1026   -623       N  
ATOM     51  N   ILE B   8      28.786  40.421   4.752  1.00 19.24           N  
ANISOU   51  N   ILE B   8     2303   2422   2586   -308   -189   -461       N  
ATOM     52  CA  ILE B   8      29.014  40.797   3.352  1.00 21.47           C  
ANISOU   52  CA  ILE B   8     2556   2678   2923   -386    -96   -435       C  
ATOM     53  C   ILE B   8      30.164  40.006   2.731  1.00 22.27           C  
ANISOU   53  C   ILE B   8     2514   2869   3078   -399    -90   -465       C  
ATOM     54  O   ILE B   8      30.132  39.655   1.554  1.00 18.50           O  
ANISOU   54  O   ILE B   8     2023   2390   2615   -414    -11   -424       O  
ATOM     55  CB  ILE B   8      29.307  42.321   3.203  1.00 27.82           C  
ANISOU   55  CB  ILE B   8     3398   3406   3764   -512    -53   -474       C  
ATOM     56  CG1 ILE B   8      28.071  43.134   3.568  1.00 35.53           C  
ANISOU   56  CG1 ILE B   8     4524   4272   4703   -484    -31   -435       C  
ATOM     57  CG2 ILE B   8      29.691  42.670   1.774  1.00 20.79           C  
ANISOU   57  CG2 ILE B   8     2487   2494   2921   -604     45   -446       C  
ATOM     58  CD1 ILE B   8      26.974  43.016   2.542  1.00 33.20           C  
ANISOU   58  CD1 ILE B   8     4294   3924   4395   -439     33   -327       C  
ATOM     59  N   SER B   9      31.174  39.704   3.539  1.00 25.28           N  
ANISOU   59  N   SER B   9     2788   3332   3486   -388   -176   -539       N  
ATOM     60  CA  SER B   9      32.350  38.995   3.053  1.00 19.76           C  
ANISOU   60  CA  SER B   9     1927   2723   2859   -387   -172   -579       C  
ATOM     61  C   SER B   9      32.088  37.507   2.764  1.00 21.83           C  
ANISOU   61  C   SER B   9     2178   3015   3102   -257   -172   -527       C  
ATOM     62  O   SER B   9      32.941  36.820   2.202  1.00 23.47           O  
ANISOU   62  O   SER B   9     2264   3282   3372   -237   -144   -554       O  
ATOM     63  CB  SER B   9      33.493  39.154   4.061  1.00 19.99           C  
ANISOU   63  CB  SER B   9     1829   2836   2928   -406   -286   -672       C  
ATOM     64  OG  SER B   9      33.100  38.663   5.336  1.00 21.96           O  
ANISOU   64  OG  SER B   9     2139   3101   3102   -302   -409   -663       O  
ATOM     65  N   ASP B  10      30.893  37.026   3.089  1.00 20.85           N  
ANISOU   65  N   ASP B  10     2183   2842   2897   -176   -186   -458       N  
ATOM     66  CA  ASP B  10      30.532  35.629   2.837  1.00 14.24           C  
ANISOU   66  CA  ASP B  10     1362   2013   2035    -68   -179   -408       C  
ATOM     67  C   ASP B  10      30.008  35.374   1.424  1.00 14.07           C  
ANISOU   67  C   ASP B  10     1382   1954   2010   -100    -63   -360       C  
ATOM     68  O   ASP B  10      29.710  34.231   1.064  1.00 17.84           O  
ANISOU   68  O   ASP B  10     1882   2429   2467    -31    -43   -327       O  
ATOM     69  CB  ASP B  10      29.468  35.165   3.838  1.00 15.46           C  
ANISOU   69  CB  ASP B  10     1638   2135   2101     17   -239   -358       C  
ATOM     70  CG  ASP B  10      30.026  34.954   5.237  1.00 24.31           C  
ANISOU   70  CG  ASP B  10     2736   3302   3198     77   -365   -396       C  
ATOM     71  OD1 ASP B  10      31.188  34.503   5.371  1.00 21.72           O  
ANISOU   71  OD1 ASP B  10     2285   3043   2926    112   -424   -440       O  
ATOM     72  OD2 ASP B  10      29.298  35.260   6.207  1.00 25.09           O1-
ANISOU   72  OD2 ASP B  10     2941   3372   3221     91   -406   -382       O1-
ATOM     73  N   LEU B  11      29.867  36.428   0.630  1.00 19.14           N  
ANISOU   73  N   LEU B  11     2051   2560   2662   -208      9   -352       N  
ATOM     74  CA  LEU B  11      29.241  36.313  -0.689  1.00 16.51           C  
ANISOU   74  CA  LEU B  11     1784   2189   2299   -247    103   -296       C  
ATOM     75  C   LEU B  11      29.884  35.237  -1.576  1.00 19.61           C  
ANISOU   75  C   LEU B  11     2115   2623   2715   -228    166   -316       C  
ATOM     76  O   LEU B  11      29.180  34.475  -2.238  1.00 19.43           O  
ANISOU   76  O   LEU B  11     2164   2578   2641   -202    203   -270       O  
ATOM     77  CB  LEU B  11      29.266  37.657  -1.428  1.00 16.88           C  
ANISOU   77  CB  LEU B  11     1867   2190   2355   -370    168   -286       C  
ATOM     78  CG  LEU B  11      28.676  37.586  -2.842  1.00 17.41           C  
ANISOU   78  CG  LEU B  11     2016   2225   2376   -416    252   -221       C  
ATOM     79  CD1 LEU B  11      27.224  37.148  -2.782  1.00 16.83           C  
ANISOU   79  CD1 LEU B  11     2042   2117   2234   -347    213   -143       C  
ATOM     80  CD2 LEU B  11      28.816  38.918  -3.560  1.00 20.52           C  
ANISOU   80  CD2 LEU B  11     2459   2565   2774   -536    316   -204       C  
ATOM     81  N   THR B  12      31.213  35.201  -1.623  1.00 13.73           N  
ANISOU   81  N   THR B  12     1234   1936   2048   -246    186   -391       N  
ATOM     82  CA  THR B  12      31.902  34.220  -2.457  1.00 14.30           C  
ANISOU   82  CA  THR B  12     1237   2043   2155   -220    266   -423       C  
ATOM     83  C   THR B  12      31.584  32.792  -2.026  1.00 24.25           C  
ANISOU   83  C   THR B  12     2520   3299   3395    -80    218   -405       C  
ATOM     84  O   THR B  12      31.196  31.958  -2.851  1.00 21.02           O  
ANISOU   84  O   THR B  12     2176   2862   2949    -63    287   -384       O  
ATOM     85  CB  THR B  12      33.424  34.426  -2.443  1.00 31.45           C  
ANISOU   85  CB  THR B  12     3225   4289   4437   -250    292   -515       C  
ATOM     86  CG2 THR B  12      34.107  33.406  -3.348  1.00 28.35           C  
ANISOU   86  CG2 THR B  12     2759   3926   4088   -212    397   -554       C  
ATOM     87  OG1 THR B  12      33.726  35.750  -2.908  1.00 36.30           O  
ANISOU   87  OG1 THR B  12     3831   4894   5069   -401    354   -532       O  
ATOM     88  N   GLY B  13      31.715  32.522  -0.732  1.00 14.02           N  
ANISOU   88  N   GLY B  13     1193   2024   2112     11     99   -412       N  
ATOM     89  CA  GLY B  13      31.387  31.201  -0.216  1.00 17.27           C  
ANISOU   89  CA  GLY B  13     1651   2416   2497    142     50   -383       C  
ATOM     90  C   GLY B  13      29.945  30.821  -0.498  1.00 12.61           C  
ANISOU   90  C   GLY B  13     1223   1756   1811    136     74   -309       C  
ATOM     91  O   GLY B  13      29.634  29.681  -0.846  1.00 14.20           O  
ANISOU   91  O   GLY B  13     1482   1925   1990    191    107   -291       O  
ATOM     92  N   MET B  14      29.049  31.783  -0.332  1.00 14.99           N  
ANISOU   92  N   MET B  14     1598   2034   2063     69     59   -269       N  
ATOM     93  CA  MET B  14      27.640  31.569  -0.630  1.00 11.09           C  
ANISOU   93  CA  MET B  14     1231   1490   1493     53     77   -200       C  
ATOM     94  C   MET B  14      27.432  31.240  -2.110  1.00 15.09           C  
ANISOU   94  C   MET B  14     1774   1981   1978     -8    173   -190       C  
ATOM     95  O   MET B  14      26.727  30.281  -2.445  1.00 16.78           O  
ANISOU   95  O   MET B  14     2063   2167   2146     12    192   -162       O  
ATOM     96  CB  MET B  14      26.815  32.791  -0.229  1.00 10.37           C  
ANISOU   96  CB  MET B  14     1188   1377   1373      2     49   -166       C  
ATOM     97  CG  MET B  14      26.673  32.952   1.251  1.00 13.36           C  
ANISOU   97  CG  MET B  14     1580   1759   1739     61    -36   -171       C  
ATOM     98  CE  MET B  14      25.204  34.419   3.377  1.00 32.68           C  
ANISOU   98  CE  MET B  14     4144   4158   4113     75   -115   -146       C  
ATOM     99  S   MET B  14      26.011  34.748   1.636  1.00 34.98           S  
ANISOU   99  S   MET B  14     4360   4461   4469    -11    -44   -160       S  
ATOM    100  N   GLN B  15      28.048  32.028  -2.985  1.00 13.19           N  
ANISOU  100  N   GLN B  15     1491   1759   1763    -94    237   -216       N  
ATOM    101  CA  GLN B  15      28.009  31.741  -4.422  1.00 14.75           C  
ANISOU  101  CA  GLN B  15     1732   1948   1925   -161    336   -214       C  
ATOM    102  C   GLN B  15      28.477  30.320  -4.702  1.00 16.25           C  
ANISOU  102  C   GLN B  15     1910   2138   2128    -94    381   -256       C  
ATOM    103  O   GLN B  15      27.881  29.609  -5.504  1.00 14.68           O  
ANISOU  103  O   GLN B  15     1802   1911   1866   -116    427   -240       O  
ATOM    104  CB  GLN B  15      28.871  32.736  -5.207  1.00 15.35           C  
ANISOU  104  CB  GLN B  15     1756   2044   2030   -262    413   -247       C  
ATOM    105  CG  GLN B  15      28.234  34.125  -5.313  1.00 26.29           C  
ANISOU  105  CG  GLN B  15     3204   3400   3385   -343    392   -191       C  
ATOM    106  CD  GLN B  15      29.197  35.224  -5.765  1.00 27.93           C  
ANISOU  106  CD  GLN B  15     3361   3616   3635   -446    460   -225       C  
ATOM    107  NE2 GLN B  15      28.651  36.413  -6.020  1.00 25.17           N  
ANISOU  107  NE2 GLN B  15     3091   3219   3254   -518    455   -169       N  
ATOM    108  OE1 GLN B  15      30.406  35.013  -5.879  1.00 34.09           O  
ANISOU  108  OE1 GLN B  15     4030   4440   4481   -459    518   -300       O  
ATOM    109  N   ASN B  16      29.535  29.899  -4.021  1.00 13.12           N  
ANISOU  109  N   ASN B  16     1403   1768   1812     -9    362   -311       N  
ATOM    110  CA  ASN B  16      30.095  28.596  -4.301  1.00 16.38           C  
ANISOU  110  CA  ASN B  16     1798   2169   2255     72    414   -355       C  
ATOM    111  C   ASN B  16      29.155  27.466  -3.875  1.00 17.44           C  
ANISOU  111  C   ASN B  16     2049   2244   2335    144    371   -311       C  
ATOM    112  O   ASN B  16      29.299  26.344  -4.330  1.00 19.79           O  
ANISOU  112  O   ASN B  16     2386   2502   2632    189    430   -336       O  
ATOM    113  CB  ASN B  16      31.491  28.458  -3.682  1.00 22.71           C  
ANISOU  113  CB  ASN B  16     2436   3022   3173    159    392   -420       C  
ATOM    114  CG  ASN B  16      32.511  29.401  -4.321  1.00 30.37           C  
ANISOU  114  CG  ASN B  16     3280   4052   4208     67    471   -480       C  
ATOM    115  ND2 ASN B  16      33.602  29.676  -3.611  1.00 26.72           N  
ANISOU  115  ND2 ASN B  16     2652   3653   3849    112    421   -532       N  
ATOM    116  OD1 ASN B  16      32.315  29.874  -5.440  1.00 34.87           O  
ANISOU  116  OD1 ASN B  16     3905   4613   4731    -49    574   -478       O  
ATOM    117  N   CYS B  17      28.168  27.761  -3.031  1.00 13.21           N  
ANISOU  117  N   CYS B  17     1576   1693   1752    146    282   -249       N  
ATOM    118  CA  CYS B  17      27.166  26.749  -2.686  1.00 16.74           C  
ANISOU  118  CA  CYS B  17     2138   2082   2140    185    258   -204       C  
ATOM    119  C   CYS B  17      26.214  26.452  -3.849  1.00 16.75           C  
ANISOU  119  C   CYS B  17     2243   2054   2067     89    322   -185       C  
ATOM    120  O   CYS B  17      25.495  25.450  -3.837  1.00 14.48           O  
ANISOU  120  O   CYS B  17     2050   1715   1737     99    327   -166       O  
ATOM    121  CB  CYS B  17      26.321  27.214  -1.498  1.00 17.08           C  
ANISOU  121  CB  CYS B  17     2214   2124   2150    199    165   -148       C  
ATOM    122  SG  CYS B  17      27.177  27.278   0.076  1.00 19.35           S  
ANISOU  122  SG  CYS B  17     2433   2436   2483    314     63   -161       S  
ATOM    123  N   ASN B  18      26.171  27.347  -4.826  1.00 15.04           N  
ANISOU  123  N   ASN B  18     2018   1868   1827    -12    364   -186       N  
ATOM    124  CA  ASN B  18      25.146  27.275  -5.864  1.00 16.44           C  
ANISOU  124  CA  ASN B  18     2296   2033   1918   -111    392   -154       C  
ATOM    125  C   ASN B  18      25.706  26.860  -7.211  1.00 15.24           C  
ANISOU  125  C   ASN B  18     2177   1877   1735   -169    499   -207       C  
ATOM    126  O   ASN B  18      25.049  27.007  -8.244  1.00 14.36           O  
ANISOU  126  O   ASN B  18     2148   1770   1540   -270    521   -186       O  
ATOM    127  CB  ASN B  18      24.426  28.625  -5.984  1.00 16.87           C  
ANISOU  127  CB  ASN B  18     2349   2117   1945   -183    345    -94       C  
ATOM    128  CG  ASN B  18      23.632  28.964  -4.735  1.00 17.37           C  
ANISOU  128  CG  ASN B  18     2400   2176   2023   -134    257    -46       C  
ATOM    129  ND2 ASN B  18      23.711  30.219  -4.289  1.00 11.62           N  
ANISOU  129  ND2 ASN B  18     1625   1465   1325   -139    223    -27       N  
ATOM    130  OD1 ASN B  18      22.963  28.091  -4.166  1.00 14.50           O  
ANISOU  130  OD1 ASN B  18     2080   1788   1643    -98    232    -29       O  
ATOM    131  N   LEU B  19      26.910  26.298  -7.170  1.00 14.33           N  
ANISOU  131  N   LEU B  19     2000   1756   1689    -99    563   -277       N  
ATOM    132  CA  LEU B  19      27.628  25.824  -8.341  1.00 16.46           C  
ANISOU  132  CA  LEU B  19     2289   2018   1946   -134    690   -346       C  
ATOM    133  C   LEU B  19      26.752  24.941  -9.227  1.00 21.56           C  
ANISOU  133  C   LEU B  19     3088   2618   2487   -202    728   -348       C  
ATOM    134  O   LEU B  19      26.870  24.986 -10.457  1.00 22.08           O  
ANISOU  134  O   LEU B  19     3218   2690   2483   -296    818   -380       O  
ATOM    135  CB  LEU B  19      28.871  25.060  -7.879  1.00 24.79           C  
ANISOU  135  CB  LEU B  19     3247   3061   3111     -6    736   -418       C  
ATOM    136  CG  LEU B  19      30.175  25.040  -8.672  1.00 39.87           C  
ANISOU  136  CG  LEU B  19     5073   4997   5080     -6    872   -506       C  
ATOM    137  CD1 LEU B  19      31.222  24.325  -7.841  1.00 42.58           C  
ANISOU  137  CD1 LEU B  19     5292   5333   5555    158    864   -555       C  
ATOM    138  CD2 LEU B  19      30.009  24.339 -10.005  1.00 47.38           C  
ANISOU  138  CD2 LEU B  19     6150   5905   5945    -78   1002   -554       C  
ATOM    139  N   HIS B  20      25.857  24.159  -8.620  1.00 15.45           N  
ANISOU  139  N   HIS B  20     2381   1797   1692   -169    663   -314       N  
ATOM    140  CA  HIS B  20      25.040  23.227  -9.399  1.00 17.55           C  
ANISOU  140  CA  HIS B  20     2791   2015   1864   -243    695   -327       C  
ATOM    141  C   HIS B  20      23.575  23.615  -9.489  1.00 18.51           C  
ANISOU  141  C   HIS B  20     2970   2161   1903   -342    601   -252       C  
ATOM    142  O   HIS B  20      22.738  22.815  -9.916  1.00 19.12           O  
ANISOU  142  O   HIS B  20     3152   2204   1908   -409    600   -256       O  
ATOM    143  CB  HIS B  20      25.211  21.799  -8.869  1.00 26.34           C  
ANISOU  143  CB  HIS B  20     3955   3037   3016   -148    723   -365       C  
ATOM    144  CG  HIS B  20      26.625  21.327  -8.922  1.00 26.46           C  
ANISOU  144  CG  HIS B  20     3908   3025   3119    -39    818   -443       C  
ATOM    145  CD2 HIS B  20      27.559  21.198  -7.950  1.00 28.22           C  
ANISOU  145  CD2 HIS B  20     4022   3244   3458    110    797   -452       C  
ATOM    146  ND1 HIS B  20      27.249  20.993 -10.104  1.00 32.73           N  
ANISOU  146  ND1 HIS B  20     4742   3805   3888    -79    953   -526       N  
ATOM    147  CE1 HIS B  20      28.501  20.655  -9.855  1.00 34.73           C  
ANISOU  147  CE1 HIS B  20     4899   4044   4254     48   1021   -585       C  
ATOM    148  NE2 HIS B  20      28.714  20.773  -8.557  1.00 32.54           N  
ANISOU  148  NE2 HIS B  20     4524   3775   4064    166    917   -539       N  
ATOM    149  N   ASN B  21      23.279  24.843  -9.076  1.00 15.68           N  
ANISOU  149  N   ASN B  21     2536   1859   1561   -349    525   -187       N  
ATOM    150  CA  ASN B  21      21.963  25.434  -9.249  1.00 16.50           C  
ANISOU  150  CA  ASN B  21     2668   1998   1604   -429    438   -113       C  
ATOM    151  C   ASN B  21      22.112  26.941  -9.351  1.00 17.15           C  
ANISOU  151  C   ASN B  21     2687   2131   1699   -446    406    -66       C  
ATOM    152  O   ASN B  21      21.718  27.707  -8.455  1.00 14.08           O  
ANISOU  152  O   ASN B  21     2234   1756   1358   -403    335    -14       O  
ATOM    153  CB  ASN B  21      21.003  25.040  -8.133  1.00 16.61           C  
ANISOU  153  CB  ASN B  21     2671   1994   1645   -388    365    -70       C  
ATOM    154  CG  ASN B  21      21.706  24.794  -6.809  1.00 23.04           C  
ANISOU  154  CG  ASN B  21     3427   2778   2549   -261    364    -83       C  
ATOM    155  ND2 ASN B  21      21.943  25.872  -6.057  1.00 15.55           N  
ANISOU  155  ND2 ASN B  21     2391   1865   1652   -213    318    -53       N  
ATOM    156  OD1 ASN B  21      22.019  23.647  -6.454  1.00 19.99           O  
ANISOU  156  OD1 ASN B  21     3085   2332   2180   -206    399   -119       O  
ATOM    157  N   LEU B  22      22.689  27.357 -10.469  1.00 12.00           N  
ANISOU  157  N   LEU B  22     2068   1495    995   -516    470    -86       N  
ATOM    158  CA  LEU B  22      23.112  28.740 -10.652  1.00 14.01           C  
ANISOU  158  CA  LEU B  22     2280   1778   1265   -539    469    -52       C  
ATOM    159  C   LEU B  22      22.018  29.806 -10.562  1.00 12.42           C  
ANISOU  159  C   LEU B  22     2082   1596   1041   -564    364     45       C  
ATOM    160  O   LEU B  22      22.322  30.952 -10.260  1.00 11.41           O  
ANISOU  160  O   LEU B  22     1908   1469    957   -551    351     75       O  
ATOM    161  CB  LEU B  22      23.866  28.871 -11.972  1.00 13.01           C  
ANISOU  161  CB  LEU B  22     2216   1660   1068   -626    575    -91       C  
ATOM    162  CG  LEU B  22      25.206  28.129 -11.997  1.00 21.20           C  
ANISOU  162  CG  LEU B  22     3208   2682   2164   -583    702   -195       C  
ATOM    163  CD1 LEU B  22      25.735  28.021 -13.440  1.00 20.73           C  
ANISOU  163  CD1 LEU B  22     3240   2627   2008   -685    828   -242       C  
ATOM    164  CD2 LEU B  22      26.220  28.837 -11.096  1.00 15.43           C  
ANISOU  164  CD2 LEU B  22     2335   1967   1560   -512    711   -213       C  
ATOM    165  N   PRO B  23      20.752  29.449 -10.849  1.00 14.98           N  
ANISOU  165  N   PRO B  23     2457   1932   1301   -602    289     91       N  
ATOM    166  CA  PRO B  23      19.738  30.491 -10.651  1.00 14.87           C  
ANISOU  166  CA  PRO B  23     2420   1938   1294   -598    188    183       C  
ATOM    167  C   PRO B  23      19.661  31.067  -9.237  1.00 16.41           C  
ANISOU  167  C   PRO B  23     2519   2119   1598   -500    154    200       C  
ATOM    168  O   PRO B  23      19.251  32.207  -9.064  1.00 13.63           O  
ANISOU  168  O   PRO B  23     2145   1765   1271   -483    105    261       O  
ATOM    169  CB  PRO B  23      18.441  29.766 -10.995  1.00 14.70           C  
ANISOU  169  CB  PRO B  23     2433   1942   1210   -645    115    211       C  
ATOM    170  CG  PRO B  23      18.865  28.816 -12.095  1.00 21.31           C  
ANISOU  170  CG  PRO B  23     3372   2777   1949   -731    181    149       C  
ATOM    171  CD  PRO B  23      20.220  28.329 -11.653  1.00 16.10           C  
ANISOU  171  CD  PRO B  23     2690   2077   1351   -674    296     64       C  
ATOM    172  N   GLU B  24      20.092  30.318  -8.236  1.00 13.34           N  
ANISOU  172  N   GLU B  24     2087   1713   1269   -433    182    146       N  
ATOM    173  CA  GLU B  24      20.078  30.872  -6.886  1.00 14.79           C  
ANISOU  173  CA  GLU B  24     2199   1886   1535   -349    151    156       C  
ATOM    174  C   GLU B  24      21.097  32.023  -6.701  1.00 17.82           C  
ANISOU  174  C   GLU B  24     2544   2260   1967   -336    176    143       C  
ATOM    175  O   GLU B  24      21.078  32.721  -5.690  1.00 15.83           O  
ANISOU  175  O   GLU B  24     2247   1996   1771   -282    146    149       O  
ATOM    176  CB  GLU B  24      20.248  29.758  -5.838  1.00 17.00           C  
ANISOU  176  CB  GLU B  24     2463   2149   1849   -282    162    113       C  
ATOM    177  CG  GLU B  24      19.734  30.139  -4.441  1.00 28.53           C  
ANISOU  177  CG  GLU B  24     3879   3603   3358   -211    118    136       C  
ATOM    178  CD  GLU B  24      18.222  30.465  -4.392  1.00 32.40           C  
ANISOU  178  CD  GLU B  24     4364   4110   3838   -231     70    200       C  
ATOM    179  OE1 GLU B  24      17.459  29.973  -5.260  1.00 32.29           O  
ANISOU  179  OE1 GLU B  24     4377   4114   3776   -296     55    222       O  
ATOM    180  OE2 GLU B  24      17.798  31.217  -3.475  1.00 25.29           O1-
ANISOU  180  OE2 GLU B  24     3425   3205   2979   -181     47    222       O1-
ATOM    181  N   ASN B  25      21.975  32.232  -7.682  1.00 18.62           N  
ANISOU  181  N   ASN B  25     2669   2364   2041   -396    237    118       N  
ATOM    182  CA  ASN B  25      22.915  33.353  -7.611  1.00 10.33           C  
ANISOU  182  CA  ASN B  25     1585   1304   1037   -411    271    104       C  
ATOM    183  C   ASN B  25      22.362  34.640  -8.245  1.00 11.00           C  
ANISOU  183  C   ASN B  25     1724   1367   1088   -464    245    182       C  
ATOM    184  O   ASN B  25      22.961  35.709  -8.099  1.00 14.84           O  
ANISOU  184  O   ASN B  25     2197   1826   1614   -483    267    181       O  
ATOM    185  CB  ASN B  25      24.242  33.008  -8.282  1.00 11.00           C  
ANISOU  185  CB  ASN B  25     1654   1401   1123   -453    371     33       C  
ATOM    186  CG  ASN B  25      25.090  32.031  -7.472  1.00 16.52           C  
ANISOU  186  CG  ASN B  25     2273   2112   1890   -374    392    -46       C  
ATOM    187  ND2 ASN B  25      26.037  31.393  -8.143  1.00 16.42           N  
ANISOU  187  ND2 ASN B  25     2246   2112   1879   -392    485   -111       N  
ATOM    188  OD1 ASN B  25      24.909  31.863  -6.265  1.00 15.81           O  
ANISOU  188  OD1 ASN B  25     2140   2020   1849   -293    329    -47       O  
ATOM    189  N   TYR B  26      21.242  34.524  -8.965  1.00 10.83           N  
ANISOU  189  N   TYR B  26     1766   1353    995   -491    194    250       N  
ATOM    190  CA  TYR B  26      20.731  35.633  -9.777  1.00 17.80           C  
ANISOU  190  CA  TYR B  26     2718   2214   1831   -536    161    336       C  
ATOM    191  C   TYR B  26      20.501  36.893  -8.944  1.00 13.54           C  
ANISOU  191  C   TYR B  26     2149   1626   1370   -480    126    374       C  
ATOM    192  O   TYR B  26      20.802  38.001  -9.389  1.00 19.98           O  
ANISOU  192  O   TYR B  26     3017   2394   2179   -519    144    413       O  
ATOM    193  CB  TYR B  26      19.438  35.257 -10.529  1.00 16.90           C  
ANISOU  193  CB  TYR B  26     2655   2131   1636   -556     79    406       C  
ATOM    194  CG  TYR B  26      19.558  34.196 -11.620  1.00 25.14           C  
ANISOU  194  CG  TYR B  26     3769   3212   2572   -639    110    376       C  
ATOM    195  CD1 TYR B  26      20.796  33.831 -12.145  1.00 23.98           C  
ANISOU  195  CD1 TYR B  26     3655   3061   2395   -694    224    303       C  
ATOM    196  CD2 TYR B  26      18.420  33.581 -12.137  1.00 19.91           C  
ANISOU  196  CD2 TYR B  26     3130   2588   1847   -661     27    408       C  
ATOM    197  CE1 TYR B  26      20.902  32.879 -13.154  1.00 23.30           C  
ANISOU  197  CE1 TYR B  26     3626   2996   2232   -745    255    252       C  
ATOM    198  CE2 TYR B  26      18.512  32.629 -13.141  1.00 24.70           C  
ANISOU  198  CE2 TYR B  26     3797   3216   2370   -727     50    355       C  
ATOM    199  CZ  TYR B  26      19.758  32.278 -13.641  1.00 24.72           C  
ANISOU  199  CZ  TYR B  26     3840   3202   2350   -765    167    277       C  
ATOM    200  OH  TYR B  26      19.855  31.326 -14.623  1.00 19.29           O  
ANISOU  200  OH  TYR B  26     3222   2524   1583   -829    199    219       O  
ATOM    201  N   GLN B  27      19.955  36.720  -7.746  1.00 15.18           N  
ANISOU  201  N   GLN B  27     2288   1836   1644   -395     84    361       N  
ATOM    202  CA  GLN B  27      19.637  37.875  -6.903  1.00 22.53           C  
ANISOU  202  CA  GLN B  27     3201   2714   2646   -338     59    386       C  
ATOM    203  C   GLN B  27      20.415  37.872  -5.597  1.00 17.43           C  
ANISOU  203  C   GLN B  27     2495   2059   2069   -298     88    304       C  
ATOM    204  O   GLN B  27      20.117  38.658  -4.701  1.00 16.71           O  
ANISOU  204  O   GLN B  27     2392   1927   2030   -247     72    305       O  
ATOM    205  CB  GLN B  27      18.135  37.923  -6.578  1.00 26.29           C  
ANISOU  205  CB  GLN B  27     3653   3196   3138   -268    -15    449       C  
ATOM    206  CG  GLN B  27      17.213  37.843  -7.786  1.00 35.85           C  
ANISOU  206  CG  GLN B  27     4905   4435   4282   -299    -77    535       C  
ATOM    207  CD  GLN B  27      16.537  39.168  -8.064  1.00 52.27           C  
ANISOU  207  CD  GLN B  27     7017   6458   6385   -259   -127    627       C  
ATOM    208  NE2 GLN B  27      17.330  40.234  -8.113  1.00 53.09           N  
ANISOU  208  NE2 GLN B  27     7180   6484   6507   -277    -82    630       N  
ATOM    209  OE1 GLN B  27      15.319  39.238  -8.242  1.00 60.43           O  
ANISOU  209  OE1 GLN B  27     8020   7514   7427   -212   -206    696       O  
ATOM    210  N   LEU B  28      21.419  37.007  -5.503  1.00 18.30           N  
ANISOU  210  N   LEU B  28     2571   2207   2176   -318    129    230       N  
ATOM    211  CA  LEU B  28      22.127  36.764  -4.246  1.00 17.19           C  
ANISOU  211  CA  LEU B  28     2367   2075   2089   -271    132    155       C  
ATOM    212  C   LEU B  28      22.766  38.018  -3.648  1.00 10.03           C  
ANISOU  212  C   LEU B  28     1450   1125   1235   -285    140    126       C  
ATOM    213  O   LEU B  28      22.633  38.277  -2.463  1.00 11.98           O  
ANISOU  213  O   LEU B  28     1678   1359   1514   -232    111     99       O  
ATOM    214  CB  LEU B  28      23.211  35.702  -4.439  1.00 12.20           C  
ANISOU  214  CB  LEU B  28     1694   1488   1455   -284    172     88       C  
ATOM    215  CG  LEU B  28      23.819  35.153  -3.142  1.00 16.47           C  
ANISOU  215  CG  LEU B  28     2170   2048   2038   -214    148     24       C  
ATOM    216  CD1 LEU B  28      22.722  34.676  -2.250  1.00 18.21           C  
ANISOU  216  CD1 LEU B  28     2413   2264   2242   -145     99     54       C  
ATOM    217  CD2 LEU B  28      24.809  34.015  -3.417  1.00 19.24           C  
ANISOU  217  CD2 LEU B  28     2476   2436   2397   -203    184    -33       C  
ATOM    218  N   LYS B  29      23.468  38.787  -4.464  1.00 11.43           N  
ANISOU  218  N   LYS B  29     1651   1277   1415   -367    187    127       N  
ATOM    219  CA  LYS B  29      24.152  39.974  -3.948  1.00 12.54           C  
ANISOU  219  CA  LYS B  29     1787   1368   1607   -404    204     91       C  
ATOM    220  C   LYS B  29      23.135  40.988  -3.404  1.00 11.75           C  
ANISOU  220  C   LYS B  29     1748   1193   1525   -357    168    139       C  
ATOM    221  O   LYS B  29      23.284  41.486  -2.297  1.00 11.37           O  
ANISOU  221  O   LYS B  29     1687   1118   1516   -331    153     89       O  
ATOM    222  CB  LYS B  29      25.022  40.612  -5.026  1.00 15.03           C  
ANISOU  222  CB  LYS B  29     2131   1662   1917   -517    277     91       C  
ATOM    223  CG  LYS B  29      25.965  41.690  -4.485  1.00 19.30           C  
ANISOU  223  CG  LYS B  29     2651   2161   2521   -583    305     30       C  
ATOM    224  CD  LYS B  29      26.865  42.260  -5.576  1.00 22.11           C  
ANISOU  224  CD  LYS B  29     3032   2496   2871   -714    399     28       C  
ATOM    225  CE  LYS B  29      27.947  43.134  -4.968  1.00 30.70           C  
ANISOU  225  CE  LYS B  29     4070   3561   4033   -797    429    -55       C  
ATOM    226  NZ  LYS B  29      28.549  44.045  -5.975  1.00 37.23           N1+
ANISOU  226  NZ  LYS B  29     4961   4329   4854   -938    529    -36       N1+
ATOM    227  N   TYR B  30      22.101  41.269  -4.188  1.00 11.42           N  
ANISOU  227  N   TYR B  30     1770   1117   1451   -341    153    233       N  
ATOM    228  CA  TYR B  30      21.004  42.114  -3.734  1.00 14.31           C  
ANISOU  228  CA  TYR B  30     2177   1414   1847   -271    121    285       C  
ATOM    229  C   TYR B  30      20.428  41.664  -2.374  1.00 16.35           C  
ANISOU  229  C   TYR B  30     2384   1697   2131   -180     93    243       C  
ATOM    230  O   TYR B  30      20.322  42.456  -1.413  1.00 11.31           O  
ANISOU  230  O   TYR B  30     1764   1000   1533   -145     99    210       O  
ATOM    231  CB  TYR B  30      19.919  42.093  -4.806  1.00 13.71           C  
ANISOU  231  CB  TYR B  30     2144   1335   1730   -250     85    394       C  
ATOM    232  CG  TYR B  30      18.692  42.877  -4.468  1.00 12.62           C  
ANISOU  232  CG  TYR B  30     2026   1135   1635   -158     48    458       C  
ATOM    233  CD1 TYR B  30      18.677  44.269  -4.569  1.00 13.23           C  
ANISOU  233  CD1 TYR B  30     2183   1096   1749   -153     63    495       C  
ATOM    234  CD2 TYR B  30      17.539  42.233  -4.056  1.00 15.44           C  
ANISOU  234  CD2 TYR B  30     2320   1543   2002    -75      5    479       C  
ATOM    235  CE1 TYR B  30      17.528  44.998  -4.251  1.00 15.56           C  
ANISOU  235  CE1 TYR B  30     2491   1325   2097    -46     35    552       C  
ATOM    236  CE2 TYR B  30      16.395  42.948  -3.734  1.00 19.52           C  
ANISOU  236  CE2 TYR B  30     2832   2009   2574     20    -19    531       C  
ATOM    237  CZ  TYR B  30      16.397  44.325  -3.840  1.00 17.06           C  
ANISOU  237  CZ  TYR B  30     2597   1581   2306     43     -6    568       C  
ATOM    238  OH  TYR B  30      15.252  44.997  -3.528  1.00 20.23           O  
ANISOU  238  OH  TYR B  30     2986   1928   2774    157    -25    618       O  
ATOM    239  N   TYR B  31      20.085  40.389  -2.280  1.00 10.34           N  
ANISOU  239  N   TYR B  31     1574   1016   1339   -150     72    240       N  
ATOM    240  CA  TYR B  31      19.504  39.858  -1.048  1.00  9.90           C  
ANISOU  240  CA  TYR B  31     1486    985   1293    -75     56    209       C  
ATOM    241  C   TYR B  31      20.464  39.841   0.140  1.00 14.01           C  
ANISOU  241  C   TYR B  31     1991   1510   1821    -75     61    117       C  
ATOM    242  O   TYR B  31      20.057  40.080   1.290  1.00 13.49           O  
ANISOU  242  O   TYR B  31     1938   1425   1764    -23     59     88       O  
ATOM    243  CB  TYR B  31      18.903  38.469  -1.292  1.00 13.47           C  
ANISOU  243  CB  TYR B  31     1903   1508   1705    -59     39    232       C  
ATOM    244  CG  TYR B  31      17.577  38.537  -2.017  1.00 20.20           C  
ANISOU  244  CG  TYR B  31     2755   2364   2556    -40     13    316       C  
ATOM    245  CD1 TYR B  31      16.621  39.476  -1.645  1.00 23.09           C  
ANISOU  245  CD1 TYR B  31     3119   2683   2970     23      8    354       C  
ATOM    246  CD2 TYR B  31      17.274  37.666  -3.068  1.00 15.78           C  
ANISOU  246  CD2 TYR B  31     2191   1856   1949    -82     -8    354       C  
ATOM    247  CE1 TYR B  31      15.392  39.551  -2.295  1.00 23.46           C  
ANISOU  247  CE1 TYR B  31     3140   2744   3029     52    -30    433       C  
ATOM    248  CE2 TYR B  31      16.036  37.732  -3.724  1.00 18.44           C  
ANISOU  248  CE2 TYR B  31     2515   2210   2283    -70    -53    431       C  
ATOM    249  CZ  TYR B  31      15.107  38.679  -3.328  1.00 23.65           C  
ANISOU  249  CZ  TYR B  31     3152   2833   3002      2    -69    473       C  
ATOM    250  OH  TYR B  31      13.881  38.771  -3.952  1.00 31.78           O  
ANISOU  250  OH  TYR B  31     4144   3888   4042     26   -126    551       O  
ATOM    251  N   LEU B  32      21.740  39.593  -0.132  1.00  9.94           N  
ANISOU  251  N   LEU B  32     1448   1024   1303   -134     66     68       N  
ATOM    252  CA  LEU B  32      22.753  39.686   0.920  1.00 10.18           C  
ANISOU  252  CA  LEU B  32     1452   1069   1348   -141     50    -19       C  
ATOM    253  C   LEU B  32      22.853  41.094   1.481  1.00 12.49           C  
ANISOU  253  C   LEU B  32     1788   1286   1670   -165     59    -51       C  
ATOM    254  O   LEU B  32      22.931  41.268   2.687  1.00 13.68           O  
ANISOU  254  O   LEU B  32     1952   1432   1813   -138     36   -107       O  
ATOM    255  CB  LEU B  32      24.135  39.241   0.424  1.00 10.42           C  
ANISOU  255  CB  LEU B  32     1416   1151   1391   -199     57    -67       C  
ATOM    256  CG  LEU B  32      25.256  39.226   1.470  1.00 16.79           C  
ANISOU  256  CG  LEU B  32     2168   1996   2218   -203     16   -157       C  
ATOM    257  CD1 LEU B  32      24.859  38.440   2.752  1.00 17.15           C  
ANISOU  257  CD1 LEU B  32     2225   2070   2221   -114    -41   -170       C  
ATOM    258  CD2 LEU B  32      26.530  38.649   0.859  1.00 18.07           C  
ANISOU  258  CD2 LEU B  32     2235   2220   2410   -244     30   -198       C  
ATOM    259  N   TYR B  33      22.873  42.099   0.606  1.00 11.35           N  
ANISOU  259  N   TYR B  33     1686   1075   1553   -221     95    -16       N  
ATOM    260  CA  TYR B  33      22.902  43.475   1.077  1.00 12.15           C  
ANISOU  260  CA  TYR B  33     1851   1078   1688   -245    114    -44       C  
ATOM    261  C   TYR B  33      21.668  43.771   1.917  1.00 12.12           C  
ANISOU  261  C   TYR B  33     1895   1026   1685   -149    113    -27       C  
ATOM    262  O   TYR B  33      21.761  44.363   2.984  1.00 16.47           O  
ANISOU  262  O   TYR B  33     2484   1535   2241   -142    116    -95       O  
ATOM    263  CB  TYR B  33      22.952  44.455  -0.097  1.00 15.61           C  
ANISOU  263  CB  TYR B  33     2350   1433   2148   -310    158     14       C  
ATOM    264  CG  TYR B  33      24.332  44.843  -0.571  1.00 22.02           C  
ANISOU  264  CG  TYR B  33     3143   2245   2978   -438    192    -36       C  
ATOM    265  CD1 TYR B  33      25.291  45.298   0.316  1.00 26.10           C  
ANISOU  265  CD1 TYR B  33     3634   2759   3523   -501    186   -140       C  
ATOM    266  CD2 TYR B  33      24.650  44.812  -1.922  1.00 28.97           C  
ANISOU  266  CD2 TYR B  33     4035   3128   3843   -508    234     19       C  
ATOM    267  CE1 TYR B  33      26.538  45.673  -0.116  1.00 28.93           C  
ANISOU  267  CE1 TYR B  33     3955   3125   3911   -629    222   -191       C  
ATOM    268  CE2 TYR B  33      25.895  45.198  -2.369  1.00 32.03           C  
ANISOU  268  CE2 TYR B  33     4401   3517   4253   -635    286    -30       C  
ATOM    269  CZ  TYR B  33      26.835  45.620  -1.465  1.00 32.53           C  
ANISOU  269  CZ  TYR B  33     4416   3584   4361   -696    282   -136       C  
ATOM    270  OH  TYR B  33      28.077  46.010  -1.912  1.00 38.94           O  
ANISOU  270  OH  TYR B  33     5184   4405   5206   -835    339   -190       O  
ATOM    271  N   HIS B  34      20.498  43.363   1.449  1.00 11.71           N  
ANISOU  271  N   HIS B  34     1838    984   1628    -78    112     55       N  
ATOM    272  CA  HIS B  34      19.311  43.568   2.264  1.00 11.84           C  
ANISOU  272  CA  HIS B  34     1873    967   1656     16    125     65       C  
ATOM    273  C   HIS B  34      19.388  42.793   3.577  1.00 14.19           C  
ANISOU  273  C   HIS B  34     2154   1326   1912     46    115     -5       C  
ATOM    274  O   HIS B  34      19.001  43.313   4.623  1.00 17.95           O  
ANISOU  274  O   HIS B  34     2675   1757   2388     86    142    -51       O  
ATOM    275  CB  HIS B  34      18.026  43.260   1.498  1.00 12.96           C  
ANISOU  275  CB  HIS B  34     1988   1124   1812     80    118    165       C  
ATOM    276  CG  HIS B  34      17.580  44.388   0.628  1.00 14.88           C  
ANISOU  276  CG  HIS B  34     2280   1274   2101     94    124    238       C  
ATOM    277  CD2 HIS B  34      17.733  44.605  -0.700  1.00 21.90           C  
ANISOU  277  CD2 HIS B  34     3193   2149   2981     49    104    314       C  
ATOM    278  ND1 HIS B  34      16.927  45.496   1.122  1.00 16.74           N  
ANISOU  278  ND1 HIS B  34     2563   1403   2392    164    157    240       N  
ATOM    279  CE1 HIS B  34      16.681  46.337   0.135  1.00 22.89           C  
ANISOU  279  CE1 HIS B  34     3392   2103   3203    172    148    323       C  
ATOM    280  NE2 HIS B  34      17.156  45.820  -0.980  1.00 25.13           N  
ANISOU  280  NE2 HIS B  34     3666   2443   3440     98    113    371       N  
ATOM    281  N   ALA B  35      19.929  41.578   3.529  1.00 15.74           N  
ANISOU  281  N   ALA B  35     2299   1615   2067     27     81    -15       N  
ATOM    282  CA  ALA B  35      20.065  40.745   4.727  1.00 18.97           C  
ANISOU  282  CA  ALA B  35     2707   2077   2422     57     61    -66       C  
ATOM    283  C   ALA B  35      20.845  41.451   5.826  1.00 15.27           C  
ANISOU  283  C   ALA B  35     2284   1582   1936     31     46   -158       C  
ATOM    284  O   ALA B  35      20.400  41.519   6.975  1.00 19.97           O  
ANISOU  284  O   ALA B  35     2931   2165   2491     71     59   -196       O  
ATOM    285  CB  ALA B  35      20.734  39.435   4.389  1.00 22.43           C  
ANISOU  285  CB  ALA B  35     3093   2600   2831     43     22    -61       C  
ATOM    286  N   ILE B  36      22.003  41.982   5.447  1.00 16.53           N  
ANISOU  286  N   ILE B  36     2424   1734   2122    -46     24   -199       N  
ATOM    287  CA  ILE B  36      22.917  42.646   6.367  1.00 17.11           C  
ANISOU  287  CA  ILE B  36     2526   1794   2182    -98     -6   -296       C  
ATOM    288  C   ILE B  36      22.259  43.810   7.113  1.00 19.60           C  
ANISOU  288  C   ILE B  36     2941   2007   2497    -85     41   -333       C  
ATOM    289  O   ILE B  36      22.580  44.087   8.278  1.00 20.08           O  
ANISOU  289  O   ILE B  36     3055   2064   2509   -100     18   -417       O  
ATOM    290  CB  ILE B  36      24.177  43.126   5.600  1.00 39.89           C  
ANISOU  290  CB  ILE B  36     5357   4682   5116   -202    -19   -327       C  
ATOM    291  CG1 ILE B  36      25.037  41.922   5.219  1.00 36.84           C  
ANISOU  291  CG1 ILE B  36     4865   4405   4726   -206    -65   -325       C  
ATOM    292  CG2 ILE B  36      25.015  44.054   6.433  1.00 44.31           C  
ANISOU  292  CG2 ILE B  36     5947   5213   5676   -280    -45   -431       C  
ATOM    293  CD1 ILE B  36      25.371  41.036   6.363  1.00 39.42           C  
ANISOU  293  CD1 ILE B  36     5175   4808   4995   -155   -141   -367       C  
ATOM    294  N   SER B  37      21.322  44.471   6.443  1.00 17.12           N  
ANISOU  294  N   SER B  37     2659   1611   2236    -51    104   -271       N  
ATOM    295  CA  SER B  37      20.603  45.601   7.024  1.00 19.54           C  
ANISOU  295  CA  SER B  37     3060   1802   2562    -17    164   -299       C  
ATOM    296  C   SER B  37      19.492  45.161   7.988  1.00 19.76           C  
ANISOU  296  C   SER B  37     3113   1846   2550     79    202   -302       C  
ATOM    297  O   SER B  37      18.859  46.004   8.625  1.00 18.74           O  
ANISOU  297  O   SER B  37     3060   1627   2432    119    267   -340       O  
ATOM    298  CB  SER B  37      20.064  46.537   5.919  1.00 22.92           C  
ANISOU  298  CB  SER B  37     3512   2125   3071     -4    211   -224       C  
ATOM    299  OG  SER B  37      19.025  45.935   5.170  1.00 22.45           O  
ANISOU  299  OG  SER B  37     3396   2101   3033     75    216   -120       O  
ATOM    300  N   TRP B  38      19.275  43.846   8.089  1.00 18.27           N  
ANISOU  300  N   TRP B  38     2865   1762   2314    111    173   -266       N  
ATOM    301  CA  TRP B  38      18.404  43.239   9.111  1.00 14.31           C  
ANISOU  301  CA  TRP B  38     2391   1291   1754    177    212   -276       C  
ATOM    302  C   TRP B  38      19.183  42.226   9.939  1.00 14.12           C  
ANISOU  302  C   TRP B  38     2379   1356   1630    151    145   -316       C  
ATOM    303  O   TRP B  38      19.070  41.008   9.723  1.00 18.13           O  
ANISOU  303  O   TRP B  38     2838   1939   2111    170    119   -263       O  
ATOM    304  CB  TRP B  38      17.167  42.559   8.485  1.00 13.32           C  
ANISOU  304  CB  TRP B  38     2196   1198   1668    243    250   -182       C  
ATOM    305  CG  TRP B  38      16.271  43.537   7.802  1.00 13.27           C  
ANISOU  305  CG  TRP B  38     2175   1109   1757    292    303   -135       C  
ATOM    306  CD1 TRP B  38      16.245  43.839   6.465  1.00 18.06           C  
ANISOU  306  CD1 TRP B  38     2735   1696   2431    284    274    -60       C  
ATOM    307  CD2 TRP B  38      15.299  44.383   8.421  1.00 14.26           C  
ANISOU  307  CD2 TRP B  38     2341   1156   1923    366    392   -160       C  
ATOM    308  CE2 TRP B  38      14.719  45.169   7.402  1.00 16.18           C  
ANISOU  308  CE2 TRP B  38     2550   1330   2267    412    402    -90       C  
ATOM    309  CE3 TRP B  38      14.871  44.562   9.739  1.00 15.05           C  
ANISOU  309  CE3 TRP B  38     2509   1232   1978    400    470   -236       C  
ATOM    310  NE1 TRP B  38      15.312  44.811   6.219  1.00 13.85           N  
ANISOU  310  NE1 TRP B  38     2211   1076   1977    355    324    -26       N  
ATOM    311  CZ2 TRP B  38      13.722  46.116   7.661  1.00 21.46           C  
ANISOU  311  CZ2 TRP B  38     3236   1905   3012    507    484    -92       C  
ATOM    312  CZ3 TRP B  38      13.884  45.507   9.999  1.00 16.53           C  
ANISOU  312  CZ3 TRP B  38     2716   1327   2237    483    568   -249       C  
ATOM    313  CH2 TRP B  38      13.317  46.270   8.965  1.00 20.28           C  
ANISOU  313  CH2 TRP B  38     3141   1732   2831    543    573   -177       C  
ATOM    314  N   PRO B  39      19.995  42.722  10.881  1.00 14.03           N  
ANISOU  314  N   PRO B  39     2438   1333   1560    106    109   -409       N  
ATOM    315  CA  PRO B  39      20.891  41.891  11.691  1.00 17.37           C  
ANISOU  315  CA  PRO B  39     2875   1840   1885     83     18   -448       C  
ATOM    316  C   PRO B  39      20.130  40.758  12.375  1.00 18.36           C  
ANISOU  316  C   PRO B  39     3037   2013   1927    146     41   -408       C  
ATOM    317  O   PRO B  39      18.981  40.959  12.775  1.00 19.68           O  
ANISOU  317  O   PRO B  39     3254   2140   2085    188    141   -401       O  
ATOM    318  CB  PRO B  39      21.427  42.870  12.737  1.00 24.81           C  
ANISOU  318  CB  PRO B  39     3916   2741   2770     31     -1   -560       C  
ATOM    319  CG  PRO B  39      21.312  44.201  12.098  1.00 25.52           C  
ANISOU  319  CG  PRO B  39     4014   2726   2957     -3     60   -580       C  
ATOM    320  CD  PRO B  39      20.108  44.151  11.220  1.00 24.39           C  
ANISOU  320  CD  PRO B  39     3829   2544   2896     71    148   -485       C  
ATOM    321  N   MET B  40      20.768  39.592  12.449  1.00 14.85           N  
ANISOU  321  N   MET B  40     2563   1647   1433    152    -42   -380       N  
ATOM    322  CA  MET B  40      20.291  38.408  13.170  1.00 13.65           C  
ANISOU  322  CA  MET B  40     2468   1534   1185    198    -37   -341       C  
ATOM    323  C   MET B  40      19.237  37.618  12.417  1.00 21.16           C  
ANISOU  323  C   MET B  40     3367   2486   2185    233     39   -252       C  
ATOM    324  O   MET B  40      18.712  36.643  12.928  1.00 23.35           O  
ANISOU  324  O   MET B  40     3694   2784   2394    259     65   -215       O  
ATOM    325  CB  MET B  40      19.820  38.762  14.587  1.00 14.75           C  
ANISOU  325  CB  MET B  40     2747   1648   1207    203      9   -397       C  
ATOM    326  CG  MET B  40      20.921  39.363  15.424  1.00 26.15           C  
ANISOU  326  CG  MET B  40     4256   3105   2575    156    -89   -488       C  
ATOM    327  CE  MET B  40      21.974  36.848  16.689  1.00 33.39           C  
ANISOU  327  CE  MET B  40     5261   4153   3270    221   -290   -411       C  
ATOM    328  S   MET B  40      22.548  38.261  15.422  1.00 55.26           S  
ANISOU  328  S   MET B  40     7877   6896   6224    157   -288   -471       S  
ATOM    329  N   LEU B  41      18.947  38.022  11.188  1.00 20.13           N  
ANISOU  329  N   LEU B  41     3145   2336   2168    225     68   -218       N  
ATOM    330  CA  LEU B  41      17.984  37.300  10.376  1.00 17.04           C  
ANISOU  330  CA  LEU B  41     2694   1956   1824    245    120   -139       C  
ATOM    331  C   LEU B  41      18.648  36.258   9.475  1.00 18.01           C  
ANISOU  331  C   LEU B  41     2755   2123   1964    232     56    -96       C  
ATOM    332  O   LEU B  41      18.018  35.273   9.090  1.00 13.28           O  
ANISOU  332  O   LEU B  41     2139   1542   1364    240     82    -40       O  
ATOM    333  CB  LEU B  41      17.161  38.280   9.537  1.00 20.00           C  
ANISOU  333  CB  LEU B  41     3013   2286   2301    251    180   -117       C  
ATOM    334  CG  LEU B  41      15.702  38.458   9.957  1.00 23.31           C  
ANISOU  334  CG  LEU B  41     3437   2684   2736    293    285   -102       C  
ATOM    335  CD1 LEU B  41      15.578  38.506  11.468  1.00 17.40           C  
ANISOU  335  CD1 LEU B  41     2797   1924   1890    305    334   -163       C  
ATOM    336  CD2 LEU B  41      15.041  39.670   9.288  1.00 12.09           C  
ANISOU  336  CD2 LEU B  41     1968   1204   1421    321    328    -89       C  
ATOM    337  N   SER B  42      19.923  36.467   9.167  1.00 11.69           N  
ANISOU  337  N   SER B  42     1922   1340   1181    208    -21   -129       N  
ATOM    338  CA  SER B  42      20.599  35.693   8.138  1.00 12.70           C  
ANISOU  338  CA  SER B  42     1979   1501   1346    197    -61    -99       C  
ATOM    339  C   SER B  42      21.844  35.018   8.680  1.00 14.10           C  
ANISOU  339  C   SER B  42     2156   1720   1482    215   -149   -131       C  
ATOM    340  O   SER B  42      22.581  35.616   9.455  1.00 14.44           O  
ANISOU  340  O   SER B  42     2216   1773   1498    205   -204   -190       O  
ATOM    341  CB  SER B  42      20.964  36.604   6.977  1.00  9.98           C  
ANISOU  341  CB  SER B  42     1567   1139   1085    150    -54   -104       C  
ATOM    342  OG  SER B  42      19.799  37.234   6.500  1.00 13.81           O  
ANISOU  342  OG  SER B  42     2055   1584   1608    151     10    -64       O  
ATOM    343  N   TYR B  43      22.069  33.773   8.249  1.00 13.09           N  
ANISOU  343  N   TYR B  43     2009   1613   1352    243   -165    -93       N  
ATOM    344  CA  TYR B  43      23.047  32.872   8.858  1.00 13.36           C  
ANISOU  344  CA  TYR B  43     2054   1678   1345    292   -248   -103       C  
ATOM    345  C   TYR B  43      23.770  32.062   7.791  1.00 16.66           C  
ANISOU  345  C   TYR B  43     2391   2113   1825    306   -258    -90       C  
ATOM    346  O   TYR B  43      23.190  31.766   6.757  1.00 18.10           O  
ANISOU  346  O   TYR B  43     2557   2277   2044    281   -191    -56       O  
ATOM    347  CB  TYR B  43      22.332  31.918   9.840  1.00 16.13           C  
ANISOU  347  CB  TYR B  43     2521   2009   1597    338   -237    -60       C  
ATOM    348  CG  TYR B  43      21.713  32.656  11.005  1.00 18.00           C  
ANISOU  348  CG  TYR B  43     2849   2233   1758    327   -216    -83       C  
ATOM    349  CD1 TYR B  43      22.466  32.952  12.131  1.00 16.72           C  
ANISOU  349  CD1 TYR B  43     2740   2094   1520    342   -303   -128       C  
ATOM    350  CD2 TYR B  43      20.396  33.107  10.957  1.00 11.32           C  
ANISOU  350  CD2 TYR B  43     2028   1356    918    301   -110    -67       C  
ATOM    351  CE1 TYR B  43      21.928  33.667  13.200  1.00 17.47           C  
ANISOU  351  CE1 TYR B  43     2934   2172   1531    325   -274   -163       C  
ATOM    352  CE2 TYR B  43      19.846  33.827  12.022  1.00 15.01           C  
ANISOU  352  CE2 TYR B  43     2578   1806   1321    295    -71   -101       C  
ATOM    353  CZ  TYR B  43      20.615  34.093  13.138  1.00 20.23           C  
ANISOU  353  CZ  TYR B  43     3314   2482   1892    304   -147   -151       C  
ATOM    354  OH  TYR B  43      20.089  34.806  14.192  1.00 17.51           O  
ANISOU  354  OH  TYR B  43     3069   2115   1469    292    -99   -194       O  
ATOM    355  N   VAL B  44      25.037  31.730   8.038  1.00 19.81           N  
ANISOU  355  N   VAL B  44     2738   2551   2240    345   -341   -123       N  
ATOM    356  CA  VAL B  44      25.775  30.776   7.212  1.00 18.41           C  
ANISOU  356  CA  VAL B  44     2492   2384   2119    384   -345   -116       C  
ATOM    357  C   VAL B  44      26.133  29.593   8.075  1.00 17.06           C  
ANISOU  357  C   VAL B  44     2379   2209   1896    483   -416    -89       C  
ATOM    358  O   VAL B  44      26.336  29.742   9.285  1.00 17.03           O  
ANISOU  358  O   VAL B  44     2427   2222   1822    515   -499    -95       O  
ATOM    359  CB  VAL B  44      27.093  31.345   6.634  1.00 18.75           C  
ANISOU  359  CB  VAL B  44     2393   2480   2252    358   -375   -179       C  
ATOM    360  CG1 VAL B  44      26.814  32.432   5.620  1.00 15.72           C  
ANISOU  360  CG1 VAL B  44     1969   2086   1918    257   -295   -195       C  
ATOM    361  CG2 VAL B  44      28.000  31.864   7.738  1.00 21.59           C  
ANISOU  361  CG2 VAL B  44     2716   2891   2597    374   -489   -231       C  
ATOM    362  N   ALA B  45      26.190  28.421   7.453  1.00 14.53           N  
ANISOU  362  N   ALA B  45     2065   1857   1600    531   -383    -58       N  
ATOM    363  CA  ALA B  45      26.692  27.209   8.081  1.00 13.21           C  
ANISOU  363  CA  ALA B  45     1948   1667   1402    641   -449    -27       C  
ATOM    364  C   ALA B  45      28.096  26.999   7.542  1.00 19.62           C  
ANISOU  364  C   ALA B  45     2616   2522   2316    699   -494    -73       C  
ATOM    365  O   ALA B  45      28.333  27.094   6.334  1.00 17.70           O  
ANISOU  365  O   ALA B  45     2286   2285   2155    658   -416   -104       O  
ATOM    366  CB  ALA B  45      25.825  26.034   7.735  1.00 17.05           C  
ANISOU  366  CB  ALA B  45     2547   2073   1859    654   -370     31       C  
ATOM    367  N   THR B  46      29.024  26.708   8.441  1.00 15.27           N  
ANISOU  367  N   THR B  46     2039   2006   1758    795   -619    -77       N  
ATOM    368  CA  THR B  46      30.444  26.714   8.126  1.00 21.21           C  
ANISOU  368  CA  THR B  46     2617   2824   2619    851   -681   -131       C  
ATOM    369  C   THR B  46      31.076  25.386   8.543  1.00 21.94           C  
ANISOU  369  C   THR B  46     2728   2885   2721   1013   -757    -92       C  
ATOM    370  O   THR B  46      30.757  24.873   9.608  1.00 27.01           O  
ANISOU  370  O   THR B  46     3509   3493   3261   1078   -836    -30       O  
ATOM    371  CB  THR B  46      31.094  27.900   8.868  1.00 29.63           C  
ANISOU  371  CB  THR B  46     3594   3982   3682    804   -790   -188       C  
ATOM    372  CG2 THR B  46      32.491  27.599   9.254  1.00 37.77           C  
ANISOU  372  CG2 THR B  46     4482   5087   4781    903   -923   -220       C  
ATOM    373  OG1 THR B  46      31.069  29.070   8.028  1.00 31.02           O  
ANISOU  373  OG1 THR B  46     3679   4187   3919    671   -705   -246       O  
ATOM    374  N   ASP B  47      31.936  24.812   7.699  1.00 22.22           N  
ANISOU  374  N   ASP B  47     2640   2925   2877   1082   -724   -123       N  
ATOM    375  CA  ASP B  47      32.596  23.537   8.023  1.00 25.19           C  
ANISOU  375  CA  ASP B  47     3027   3260   3285   1258   -792    -86       C  
ATOM    376  C   ASP B  47      33.839  23.802   8.899  1.00 28.15           C  
ANISOU  376  C   ASP B  47     3268   3732   3696   1304   -942   -105       C  
ATOM    377  O   ASP B  47      34.152  24.965   9.154  1.00 28.46           O  
ANISOU  377  O   ASP B  47     3203   3870   3740   1225  -1005   -161       O  
ATOM    378  CB  ASP B  47      32.894  22.737   6.735  1.00 28.18           C  
ANISOU  378  CB  ASP B  47     3350   3585   3774   1301   -660   -114       C  
ATOM    379  CG  ASP B  47      34.055  23.304   5.920  1.00 34.30           C  
ANISOU  379  CG  ASP B  47     3881   4457   4695   1286   -630   -208       C  
ATOM    380  OD1 ASP B  47      34.228  22.854   4.767  1.00 41.92           O  
ANISOU  380  OD1 ASP B  47     4805   5385   5737   1288   -494   -246       O  
ATOM    381  OD2 ASP B  47      34.809  24.172   6.409  1.00 29.46           O1-
ANISOU  381  OD2 ASP B  47     3120   3955   4119   1266   -734   -251       O1-
ATOM    382  N   PRO B  48      34.554  22.747   9.354  1.00 31.36           N  
ANISOU  382  N   PRO B  48     3676   4109   4129   1417   -994    -60       N  
ATOM    383  CA  PRO B  48      35.723  22.978  10.218  1.00 32.31           C  
ANISOU  383  CA  PRO B  48     3670   4325   4280   1455  -1141    -68       C  
ATOM    384  C   PRO B  48      36.759  24.009   9.751  1.00 38.38           C  
ANISOU  384  C   PRO B  48     4186   5224   5171   1397  -1163   -166       C  
ATOM    385  O   PRO B  48      37.437  24.598  10.594  1.00 44.67           O  
ANISOU  385  O   PRO B  48     4904   6113   5955   1372  -1293   -182       O  
ATOM    386  CB  PRO B  48      36.377  21.598  10.277  1.00 34.94           C  
ANISOU  386  CB  PRO B  48     4005   4595   4675   1602  -1152    -12       C  
ATOM    387  CG  PRO B  48      35.248  20.667  10.187  1.00 32.92           C  
ANISOU  387  CG  PRO B  48     3977   4197   4334   1619  -1061     56       C  
ATOM    388  CD  PRO B  48      34.257  21.304   9.248  1.00 29.58           C  
ANISOU  388  CD  PRO B  48     3590   3756   3894   1510   -934     11       C  
ATOM    389  N   LYS B  49      36.888  24.232   8.450  1.00 34.27           N  
ANISOU  389  N   LYS B  49     3546   4714   4763   1362  -1033   -233       N  
ATOM    390  CA  LYS B  49      37.883  25.185   7.961  1.00 32.61           C  
ANISOU  390  CA  LYS B  49     3098   4622   4672   1286  -1027   -328       C  
ATOM    391  C   LYS B  49      37.372  26.606   7.758  1.00 31.09           C  
ANISOU  391  C   LYS B  49     2885   4481   4447   1123  -1005   -392       C  
ATOM    392  O   LYS B  49      38.125  27.480   7.351  1.00 35.86           O  
ANISOU  392  O   LYS B  49     3310   5173   5143   1028   -986   -472       O  
ATOM    393  CB  LYS B  49      38.527  24.674   6.665  1.00 36.86           C  
ANISOU  393  CB  LYS B  49     3495   5151   5359   1326   -881   -373       C  
ATOM    394  CG  LYS B  49      39.616  23.632   6.865  1.00 40.64           C  
ANISOU  394  CG  LYS B  49     3882   5630   5929   1472   -921   -342       C  
ATOM    395  CD  LYS B  49      40.323  23.329   5.550  1.00 45.24           C  
ANISOU  395  CD  LYS B  49     4311   6218   6662   1490   -757   -405       C  
ATOM    396  CE  LYS B  49      41.617  22.558   5.750  1.00 47.99           C  
ANISOU  396  CE  LYS B  49     4509   6597   7127   1627   -801   -388       C  
ATOM    397  NZ  LYS B  49      42.306  22.308   4.449  1.00 52.55           N1+
ANISOU  397  NZ  LYS B  49     4942   7182   7844   1639   -621   -455       N1+
ATOM    398  N   GLY B  50      36.115  26.856   8.093  1.00 28.40           N  
ANISOU  398  N   GLY B  50     2732   4083   3977   1083  -1007   -355       N  
ATOM    399  CA  GLY B  50      35.538  28.172   7.879  1.00 25.97           C  
ANISOU  399  CA  GLY B  50     2439   3797   3633    915   -957   -399       C  
ATOM    400  C   GLY B  50      34.801  28.304   6.558  1.00 27.19           C  
ANISOU  400  C   GLY B  50     2644   3883   3805    819   -755   -399       C  
ATOM    401  O   GLY B  50      34.313  29.380   6.216  1.00 29.68           O  
ANISOU  401  O   GLY B  50     2984   4196   4096    673   -687   -421       O  
ATOM    402  N   ARG B  51      34.706  27.208   5.813  1.00 23.33           N  
ANISOU  402  N   ARG B  51     2182   3330   3352    903   -664   -372       N  
ATOM    403  CA  ARG B  51      34.037  27.253   4.526  1.00 19.39           C  
ANISOU  403  CA  ARG B  51     1738   2773   2858    811   -486   -373       C  
ATOM    404  C   ARG B  51      32.525  27.247   4.688  1.00 16.71           C  
ANISOU  404  C   ARG B  51     1612   2349   2387    756   -448   -303       C  
ATOM    405  O   ARG B  51      31.970  26.427   5.400  1.00 20.26           O  
ANISOU  405  O   ARG B  51     2196   2741   2763    839   -497   -240       O  
ATOM    406  CB  ARG B  51      34.474  26.075   3.643  1.00 20.67           C  
ANISOU  406  CB  ARG B  51     1862   2893   3098    909   -393   -384       C  
ATOM    407  CG  ARG B  51      33.763  26.042   2.302  1.00 18.33           C  
ANISOU  407  CG  ARG B  51     1644   2537   2782    808   -217   -387       C  
ATOM    408  CD  ARG B  51      34.363  24.999   1.367  1.00 25.28           C  
ANISOU  408  CD  ARG B  51     2476   3383   3746    890   -109   -424       C  
ATOM    409  NE  ARG B  51      33.984  23.636   1.721  1.00 29.42           N  
ANISOU  409  NE  ARG B  51     3135   3807   4236   1025   -129   -370       N  
ATOM    410  CZ  ARG B  51      33.620  22.715   0.831  1.00 31.19           C  
ANISOU  410  CZ  ARG B  51     3457   3940   4452   1038     -4   -373       C  
ATOM    411  NH1 ARG B  51      33.584  23.022  -0.464  1.00 23.23           N1+
ANISOU  411  NH1 ARG B  51     2430   2939   3457    926    143   -425       N1+
ATOM    412  NH2 ARG B  51      33.295  21.490   1.227  1.00 31.91           N  
ANISOU  412  NH2 ARG B  51     3682   3927   4515   1155    -24   -324       N  
ATOM    413  N   VAL B  52      31.865  28.177   4.017  1.00 15.54           N  
ANISOU  413  N   VAL B  52     1494   2194   2217    616   -359   -311       N  
ATOM    414  CA  VAL B  52      30.407  28.228   3.997  1.00 18.32           C  
ANISOU  414  CA  VAL B  52     2017   2477   2469    560   -311   -250       C  
ATOM    415  C   VAL B  52      29.835  27.041   3.227  1.00 20.90           C  
ANISOU  415  C   VAL B  52     2434   2729   2780    593   -221   -214       C  
ATOM    416  O   VAL B  52      30.163  26.847   2.057  1.00 15.62           O  
ANISOU  416  O   VAL B  52     1715   2058   2164    564   -124   -247       O  
ATOM    417  CB  VAL B  52      29.930  29.550   3.358  1.00 17.27           C  
ANISOU  417  CB  VAL B  52     1876   2354   2331    415   -244   -265       C  
ATOM    418  CG1 VAL B  52      28.431  29.534   3.123  1.00 12.06           C  
ANISOU  418  CG1 VAL B  52     1361   1632   1591    367   -187   -203       C  
ATOM    419  CG2 VAL B  52      30.337  30.735   4.240  1.00 18.98           C  
ANISOU  419  CG2 VAL B  52     2041   2622   2549    371   -329   -302       C  
ATOM    420  N   VAL B  53      28.979  26.244   3.864  1.00 16.44           N  
ANISOU  420  N   VAL B  53     2011   2100   2136    642   -243   -152       N  
ATOM    421  CA  VAL B  53      28.382  25.114   3.156  1.00 13.34           C  
ANISOU  421  CA  VAL B  53     1717   1626   1725    654   -156   -125       C  
ATOM    422  C   VAL B  53      26.874  25.219   3.062  1.00 14.75           C  
ANISOU  422  C   VAL B  53     2022   1764   1820    562   -109    -75       C  
ATOM    423  O   VAL B  53      26.209  24.335   2.537  1.00 13.87           O  
ANISOU  423  O   VAL B  53     2001   1588   1681    545    -44    -53       O  
ATOM    424  CB  VAL B  53      28.771  23.771   3.794  1.00 15.25           C  
ANISOU  424  CB  VAL B  53     2020   1808   1966    797   -202    -97       C  
ATOM    425  CG1 VAL B  53      30.284  23.621   3.778  1.00 15.76           C  
ANISOU  425  CG1 VAL B  53     1932   1922   2136    903   -250   -148       C  
ATOM    426  CG2 VAL B  53      28.221  23.683   5.228  1.00 16.78           C  
ANISOU  426  CG2 VAL B  53     2327   1983   2067    835   -296    -34       C  
ATOM    427  N   GLY B  54      26.333  26.303   3.596  1.00 15.59           N  
ANISOU  427  N   GLY B  54     2127   1906   1890    501   -141    -63       N  
ATOM    428  CA  GLY B  54      24.911  26.566   3.497  1.00 14.75           C  
ANISOU  428  CA  GLY B  54     2105   1776   1725    419    -95    -22       C  
ATOM    429  C   GLY B  54      24.601  27.941   4.058  1.00 16.11           C  
ANISOU  429  C   GLY B  54     2249   1989   1883    371   -127    -26       C  
ATOM    430  O   GLY B  54      25.435  28.516   4.754  1.00 13.25           O  
ANISOU  430  O   GLY B  54     1833   1665   1535    403   -196    -58       O  
ATOM    431  N   TYR B  55      23.426  28.477   3.751  1.00  9.61           N  
ANISOU  431  N   TYR B  55     1458   1156   1036    298    -81      2       N  
ATOM    432  CA  TYR B  55      23.060  29.798   4.246  1.00  9.36           C  
ANISOU  432  CA  TYR B  55     1411   1147   1000    263    -96     -4       C  
ATOM    433  C   TYR B  55      21.560  30.023   4.138  1.00  8.85           C  
ANISOU  433  C   TYR B  55     1394   1062    909    216    -46     40       C  
ATOM    434  O   TYR B  55      20.867  29.353   3.369  1.00  8.62           O  
ANISOU  434  O   TYR B  55     1383   1017    874    183     -4     70       O  
ATOM    435  CB  TYR B  55      23.831  30.912   3.498  1.00 14.21           C  
ANISOU  435  CB  TYR B  55     1934   1791   1675    213    -94    -45       C  
ATOM    436  CG  TYR B  55      23.429  31.037   2.049  1.00 14.91           C  
ANISOU  436  CG  TYR B  55     2008   1873   1785    145    -30    -27       C  
ATOM    437  CD1 TYR B  55      22.291  31.751   1.682  1.00 14.64           C  
ANISOU  437  CD1 TYR B  55     1999   1825   1739     95     -4     13       C  
ATOM    438  CD2 TYR B  55      24.163  30.417   1.049  1.00  9.20           C  
ANISOU  438  CD2 TYR B  55     1250   1158   1088    135      3    -49       C  
ATOM    439  CE1 TYR B  55      21.893  31.847   0.360  1.00 13.07           C  
ANISOU  439  CE1 TYR B  55     1798   1625   1543     34     34     39       C  
ATOM    440  CE2 TYR B  55      23.783  30.523  -0.283  1.00  9.17           C  
ANISOU  440  CE2 TYR B  55     1256   1150   1079     64     60    -32       C  
ATOM    441  CZ  TYR B  55      22.644  31.230  -0.618  1.00 13.64           C  
ANISOU  441  CZ  TYR B  55     1854   1707   1622     12     65     15       C  
ATOM    442  OH  TYR B  55      22.251  31.322  -1.930  1.00 16.50           O  
ANISOU  442  OH  TYR B  55     2235   2070   1963    -58    101     40       O  
ATOM    443  N   VAL B  56      21.059  30.969   4.925  1.00  9.00           N  
ANISOU  443  N   VAL B  56     1426   1082    912    213    -51     38       N  
ATOM    444  CA  VAL B  56      19.693  31.448   4.779  1.00  9.27           C  
ANISOU  444  CA  VAL B  56     1469   1105    947    178     -2     72       C  
ATOM    445  C   VAL B  56      19.726  32.969   4.754  1.00  9.22           C  
ANISOU  445  C   VAL B  56     1428   1096    978    161     -4     51       C  
ATOM    446  O   VAL B  56      20.389  33.594   5.585  1.00 15.31           O  
ANISOU  446  O   VAL B  56     2211   1867   1740    178    -36      7       O  
ATOM    447  CB  VAL B  56      18.759  30.937   5.897  1.00  8.83           C  
ANISOU  447  CB  VAL B  56     1485   1035    835    200     27     94       C  
ATOM    448  CG1 VAL B  56      19.202  31.417   7.286  1.00  9.33           C  
ANISOU  448  CG1 VAL B  56     1600   1096    850    241     -3     60       C  
ATOM    449  CG2 VAL B  56      17.317  31.365   5.624  1.00 17.22           C  
ANISOU  449  CG2 VAL B  56     2523   2098   1921    166     86    126       C  
ATOM    450  N   LEU B  57      19.087  33.566   3.754  1.00  8.37           N  
ANISOU  450  N   LEU B  57     1286    984    911    123     22     81       N  
ATOM    451  CA  LEU B  57      18.952  35.021   3.712  1.00  9.93           C  
ANISOU  451  CA  LEU B  57     1469   1155   1147    114     29     74       C  
ATOM    452  C   LEU B  57      17.508  35.408   3.951  1.00 14.38           C  
ANISOU  452  C   LEU B  57     2035   1703   1725    135     68    110       C  
ATOM    453  O   LEU B  57      16.591  34.768   3.453  1.00 12.03           O  
ANISOU  453  O   LEU B  57     1715   1426   1428    125     83    155       O  
ATOM    454  CB  LEU B  57      19.408  35.632   2.364  1.00  8.88           C  
ANISOU  454  CB  LEU B  57     1303   1016   1053     64     25     88       C  
ATOM    455  CG  LEU B  57      20.868  35.399   1.983  1.00  9.74           C  
ANISOU  455  CG  LEU B  57     1387   1145   1167     35      8     44       C  
ATOM    456  CD1 LEU B  57      21.230  36.177   0.710  1.00  9.55           C  
ANISOU  456  CD1 LEU B  57     1348   1108   1173    -28     27     60       C  
ATOM    457  CD2 LEU B  57      21.828  35.711   3.140  1.00  8.96           C  
ANISOU  457  CD2 LEU B  57     1285   1051   1068     55    -26    -22       C  
ATOM    458  N   ALA B  58      17.319  36.500   4.680  1.00  9.48           N  
ANISOU  458  N   ALA B  58     1436   1046   1122    161     86     84       N  
ATOM    459  CA  ALA B  58      15.986  36.953   4.989  1.00 14.40           C  
ANISOU  459  CA  ALA B  58     2047   1650   1772    197    136    109       C  
ATOM    460  C   ALA B  58      15.965  38.472   5.139  1.00 14.49           C  
ANISOU  460  C   ALA B  58     2076   1597   1832    219    154     88       C  
ATOM    461  O   ALA B  58      17.014  39.133   5.101  1.00 10.45           O  
ANISOU  461  O   ALA B  58     1594   1056   1322    191    128     49       O  
ATOM    462  CB  ALA B  58      15.501  36.281   6.282  1.00  9.72           C  
ANISOU  462  CB  ALA B  58     1496   1072   1125    223    179     87       C  
ATOM    463  N   LYS B  59      14.766  39.026   5.292  1.00 10.55           N  
ANISOU  463  N   LYS B  59     1554   1073   1380    269    204    112       N  
ATOM    464  CA  LYS B  59      14.614  40.457   5.577  1.00 11.61           C  
ANISOU  464  CA  LYS B  59     1721   1124   1565    308    237     88       C  
ATOM    465  C   LYS B  59      13.213  40.721   6.089  1.00 12.03           C  
ANISOU  465  C   LYS B  59     1740   1165   1666    382    311     99       C  
ATOM    466  O   LYS B  59      12.325  39.885   5.921  1.00 14.33           O  
ANISOU  466  O   LYS B  59     1960   1520   1966    389    324    141       O  
ATOM    467  CB  LYS B  59      14.884  41.296   4.335  1.00 15.63           C  
ANISOU  467  CB  LYS B  59     2222   1589   2129    293    198    136       C  
ATOM    468  CG  LYS B  59      13.891  41.082   3.220  1.00 17.45           C  
ANISOU  468  CG  LYS B  59     2378   1850   2404    314    173    228       C  
ATOM    469  CD  LYS B  59      14.344  41.842   1.980  1.00 20.14           C  
ANISOU  469  CD  LYS B  59     2741   2145   2767    285    128    281       C  
ATOM    470  CE  LYS B  59      13.276  42.801   1.519  1.00 32.29           C  
ANISOU  470  CE  LYS B  59     4258   3626   4384    365    127    350       C  
ATOM    471  NZ  LYS B  59      12.193  42.097   0.799  1.00 34.87           N1+
ANISOU  471  NZ  LYS B  59     4490   4034   4726    385     84    425       N1+
ATOM    472  N   MET B  60      13.023  41.858   6.750  1.00 12.89           N  
ANISOU  472  N   MET B  60     1897   1193   1808    431    368     54       N  
ATOM    473  CA  MET B  60      11.683  42.301   7.103  1.00 13.86           C  
ANISOU  473  CA  MET B  60     1972   1292   2002    518    451     64       C  
ATOM    474  C   MET B  60      11.170  43.218   5.994  1.00 14.41           C  
ANISOU  474  C   MET B  60     1990   1308   2179    575    421    137       C  
ATOM    475  O   MET B  60      11.953  43.861   5.290  1.00 14.28           O  
ANISOU  475  O   MET B  60     2024   1235   2168    545    366    155       O  
ATOM    476  CB  MET B  60      11.682  43.059   8.439  1.00 14.77           C  
ANISOU  476  CB  MET B  60     2181   1334   2096    553    545    -31       C  
ATOM    477  CG  MET B  60      12.175  42.245   9.634  1.00 17.14           C  
ANISOU  477  CG  MET B  60     2560   1682   2272    503    567    -99       C  
ATOM    478  CE  MET B  60       9.443  41.586  10.543  1.00 16.05           C  
ANISOU  478  CE  MET B  60     2281   1610   2209    608    785    -82       C  
ATOM    479  S   MET B  60      11.094  40.648  10.072  1.00 30.12           S  
ANISOU  479  S   MET B  60     4131   3439   3875    497    628    -63       S  
ATOM    480  N   GLU B  61       9.853  43.266   5.840  1.00 16.87           N  
ANISOU  480  N   GLU B  61     2197   1640   2574    654    456    182       N  
ATOM    481  CA  GLU B  61       9.237  44.198   4.928  1.00 17.76           C  
ANISOU  481  CA  GLU B  61     2259   1697   2793    735    424    256       C  
ATOM    482  C   GLU B  61       9.521  45.599   5.446  1.00 22.80           C  
ANISOU  482  C   GLU B  61     3004   2187   3471    795    484    206       C  
ATOM    483  O   GLU B  61       9.391  45.850   6.642  1.00 17.58           O  
ANISOU  483  O   GLU B  61     2392   1488   2800    823    587    117       O  
ATOM    484  CB  GLU B  61       7.734  43.939   4.867  1.00 20.57           C  
ANISOU  484  CB  GLU B  61     2459   2115   3240    817    453    300       C  
ATOM    485  CG  GLU B  61       6.966  45.021   4.175  1.00 24.52           C  
ANISOU  485  CG  GLU B  61     2902   2548   3866    938    427    372       C  
ATOM    486  CD  GLU B  61       7.347  45.120   2.721  1.00 35.62           C  
ANISOU  486  CD  GLU B  61     4319   3958   5258    903    288    473       C  
ATOM    487  OE1 GLU B  61       7.465  44.054   2.089  1.00 42.28           O  
ANISOU  487  OE1 GLU B  61     5116   4911   6037    811    214    507       O  
ATOM    488  OE2 GLU B  61       7.556  46.253   2.226  1.00 43.24           O1-
ANISOU  488  OE2 GLU B  61     5357   4807   6266    960    261    516       O1-
ATOM    489  N   GLU B  62       9.890  46.520   4.559  1.00 19.71           N  
ANISOU  489  N   GLU B  62     2665   1704   3118    808    428    260       N  
ATOM    490  CA  GLU B  62      10.284  47.866   4.999  1.00 19.14           C  
ANISOU  490  CA  GLU B  62     2720   1471   3080    845    486    208       C  
ATOM    491  C   GLU B  62       9.111  48.768   5.352  1.00 26.45           C  
ANISOU  491  C   GLU B  62     3611   2322   4118    988    558    208       C  
ATOM    492  O   GLU B  62       9.176  49.560   6.302  1.00 31.32           O  
ANISOU  492  O   GLU B  62     4312   2857   4731   1001    639    113       O  
ATOM    493  CB  GLU B  62      11.154  48.540   3.940  1.00 18.34           C  
ANISOU  493  CB  GLU B  62     2707   1290   2973    789    412    265       C  
ATOM    494  CG  GLU B  62      12.482  47.816   3.685  1.00 24.00           C  
ANISOU  494  CG  GLU B  62     3461   2079   3579    634    354    238       C  
ATOM    495  CD  GLU B  62      13.577  48.193   4.683  1.00 26.18           C  
ANISOU  495  CD  GLU B  62     3849   2298   3800    556    401    115       C  
ATOM    496  OE1 GLU B  62      13.335  49.071   5.547  1.00 26.69           O  
ANISOU  496  OE1 GLU B  62     3987   2255   3900    609    480     47       O  
ATOM    497  OE2 GLU B  62      14.691  47.620   4.593  1.00 21.97           O1-
ANISOU  497  OE2 GLU B  62     3328   1829   3191    440    355     83       O1-
ATOM    498  N   GLU B  63       8.037  48.674   4.585  1.00 24.09           N  
ANISOU  498  N   GLU B  63     3178   2081   3895   1066    504    301       N  
ATOM    499  CA  GLU B  63       6.894  49.538   4.833  1.00 30.19           C  
ANISOU  499  CA  GLU B  63     3893   2814   4763   1184    542    295       C  
ATOM    500  C   GLU B  63       5.666  48.673   4.927  1.00 28.74           C  
ANISOU  500  C   GLU B  63     3521   2768   4632   1237    556    318       C  
ATOM    501  O   GLU B  63       4.880  48.595   3.988  1.00 30.21           O  
ANISOU  501  O   GLU B  63     3587   3012   4880   1288    465    411       O  
ATOM    502  CB  GLU B  63       6.745  50.583   3.721  1.00 35.78           C  
ANISOU  502  CB  GLU B  63     4633   3436   5526   1239    446    385       C  
ATOM    503  CG  GLU B  63       7.996  51.402   3.472  1.00 34.37           C  
ANISOU  503  CG  GLU B  63     4638   3124   5296   1162    430    374       C  
ATOM    504  CD  GLU B  63       7.836  52.368   2.311  1.00 36.74           C  
ANISOU  504  CD  GLU B  63     4984   3337   5637   1208    335    475       C  
ATOM    505  OE1 GLU B  63       7.314  53.468   2.532  1.00 35.88           O  
ANISOU  505  OE1 GLU B  63     4910   3123   5600   1302    363    460       O  
ATOM    506  OE2 GLU B  63       8.222  52.019   1.176  1.00 40.28           O1-
ANISOU  506  OE2 GLU B  63     5442   3821   6040   1151    234    570       O1-
ATOM    507  N   PRO B  64       5.523  47.977   6.057  1.00 28.75           N  
ANISOU  507  N   PRO B  64     3500   2826   4597   1209    667    231       N  
ATOM    508  CA  PRO B  64       4.437  47.007   6.181  1.00 28.36           C  
ANISOU  508  CA  PRO B  64     3271   2915   4590   1228    695    248       C  
ATOM    509  C   PRO B  64       3.074  47.696   6.219  1.00 33.35           C  
ANISOU  509  C   PRO B  64     3779   3550   5342   1347    720    253       C  
ATOM    510  O   PRO B  64       2.933  48.738   6.863  1.00 36.01           O  
ANISOU  510  O   PRO B  64     4188   3785   5709   1412    795    189       O  
ATOM    511  CB  PRO B  64       4.731  46.325   7.514  1.00 31.43           C  
ANISOU  511  CB  PRO B  64     3719   3332   4891   1164    826    143       C  
ATOM    512  CG  PRO B  64       5.546  47.337   8.287  1.00 33.26           C  
ANISOU  512  CG  PRO B  64     4139   3430   5069   1156    880     53       C  
ATOM    513  CD  PRO B  64       6.368  48.047   7.262  1.00 25.00           C  
ANISOU  513  CD  PRO B  64     3173   2295   4030   1147    767    114       C  
ATOM    514  N   LYS B  65       2.083  47.112   5.552  1.00 35.69           N  
ANISOU  514  N   LYS B  65     3888   3965   5708   1372    657    322       N  
ATOM    515  CA  LYS B  65       0.725  47.625   5.640  1.00 40.48           C  
ANISOU  515  CA  LYS B  65     4350   4597   6434   1486    682    318       C  
ATOM    516  C   LYS B  65       0.303  47.606   7.113  1.00 45.46           C  
ANISOU  516  C   LYS B  65     4983   5225   7063   1495    867    198       C  
ATOM    517  O   LYS B  65       0.462  46.601   7.807  1.00 42.03           O  
ANISOU  517  O   LYS B  65     4549   4863   6558   1402    950    152       O  
ATOM    518  CB  LYS B  65      -0.246  46.769   4.818  1.00 45.21           C  
ANISOU  518  CB  LYS B  65     4733   5352   7091   1480    588    392       C  
ATOM    519  CG  LYS B  65      -1.698  47.151   5.059  1.00 54.44           C  
ANISOU  519  CG  LYS B  65     5727   6571   8387   1591    629    369       C  
ATOM    520  CD  LYS B  65      -2.413  47.592   3.786  1.00 63.93           C  
ANISOU  520  CD  LYS B  65     6814   7806   9671   1679    458    468       C  
ATOM    521  CE  LYS B  65      -2.951  46.422   2.966  1.00 67.03           C  
ANISOU  521  CE  LYS B  65     7033   8371  10065   1598    346    530       C  
ATOM    522  NZ  LYS B  65      -4.295  46.006   3.491  1.00 69.73           N1+
ANISOU  522  NZ  LYS B  65     7153   8835  10504   1625    422    477       N1+
ATOM    523  N   ASP B  66      -0.198  48.739   7.590  1.00 50.66           N  
ANISOU  523  N   ASP B  66     5663   5795   7792   1604    934    149       N  
ATOM    524  CA  ASP B  66      -0.702  48.870   8.953  1.00 52.88           C  
ANISOU  524  CA  ASP B  66     5951   6069   8073   1623   1111     36       C  
ATOM    525  C   ASP B  66       0.370  48.678  10.030  1.00 51.17           C  
ANISOU  525  C   ASP B  66     5934   5796   7712   1518   1210    -54       C  
ATOM    526  O   ASP B  66       0.063  48.554  11.214  1.00 54.94           O  
ANISOU  526  O   ASP B  66     6440   6285   8151   1500   1355   -146       O  
ATOM    527  CB  ASP B  66      -1.901  47.955   9.172  1.00 54.35           C  
ANISOU  527  CB  ASP B  66     5925   6410   8316   1617   1169     30       C  
ATOM    528  CG  ASP B  66      -3.165  48.490   8.513  1.00 58.77           C  
ANISOU  528  CG  ASP B  66     6288   7010   9031   1753   1110     75       C  
ATOM    529  OD1 ASP B  66      -3.400  49.712   8.596  1.00 56.14           O  
ANISOU  529  OD1 ASP B  66     5996   6567   8767   1879   1125     55       O  
ATOM    530  OD2 ASP B  66      -3.905  47.699   7.884  1.00 63.03           O1-
ANISOU  530  OD2 ASP B  66     6636   7690   9624   1734   1041    129       O1-
ATOM    531  N   GLY B  67       1.632  48.666   9.619  1.00 46.95           N  
ANISOU  531  N   GLY B  67     5542   5204   7092   1447   1127    -28       N  
ATOM    532  CA  GLY B  67       2.729  48.541  10.562  1.00 47.07           C  
ANISOU  532  CA  GLY B  67     5748   5170   6967   1349   1191   -113       C  
ATOM    533  C   GLY B  67       2.818  47.174  11.213  1.00 43.67           C  
ANISOU  533  C   GLY B  67     5305   4851   6437   1247   1252   -142       C  
ATOM    534  O   GLY B  67       3.516  47.001  12.209  1.00 47.20           O  
ANISOU  534  O   GLY B  67     5903   5275   6758   1172   1318   -222       O  
ATOM    535  N   ILE B  68       2.097  46.207  10.656  1.00 38.70           N  
ANISOU  535  N   ILE B  68     4501   4344   5857   1238   1225    -76       N  
ATOM    536  CA  ILE B  68       2.172  44.824  11.117  1.00 32.16           C  
ANISOU  536  CA  ILE B  68     3661   3620   4937   1133   1275    -88       C  
ATOM    537  C   ILE B  68       3.424  44.173  10.546  1.00 26.40           C  
ANISOU  537  C   ILE B  68     3022   2892   4116   1053   1174    -46       C  
ATOM    538  O   ILE B  68       3.489  43.875   9.356  1.00 29.54           O  
ANISOU  538  O   ILE B  68     3329   3327   4567   1057   1057     47       O  
ATOM    539  CB  ILE B  68       0.961  44.026  10.645  1.00 32.52           C  
ANISOU  539  CB  ILE B  68     3481   3797   5076   1135   1274    -34       C  
ATOM    540  CG1 ILE B  68      -0.333  44.696  11.113  1.00 37.03           C  
ANISOU  540  CG1 ILE B  68     3937   4376   5756   1227   1368    -76       C  
ATOM    541  CG2 ILE B  68       1.048  42.594  11.125  1.00 31.95           C  
ANISOU  541  CG2 ILE B  68     3415   3820   4904   1012   1334    -46       C  
ATOM    542  CD1 ILE B  68      -1.577  43.996  10.626  1.00 42.14           C  
ANISOU  542  CD1 ILE B  68     4344   5160   6505   1227   1357    -31       C  
ATOM    543  N   PRO B  69       4.411  43.914  11.406  1.00 25.06           N  
ANISOU  543  N   PRO B  69     3031   2689   3801    979   1214   -115       N  
ATOM    544  CA  PRO B  69       5.714  43.450  10.936  1.00 20.27           C  
ANISOU  544  CA  PRO B  69     2526   2074   3102    909   1111    -90       C  
ATOM    545  C   PRO B  69       5.639  42.057  10.309  1.00 19.15           C  
ANISOU  545  C   PRO B  69     2294   2060   2924    817   1026    -18       C  
ATOM    546  O   PRO B  69       4.959  41.169  10.824  1.00 21.93           O  
ANISOU  546  O   PRO B  69     2590   2489   3254    779   1109    -27       O  
ATOM    547  CB  PRO B  69       6.556  43.426  12.215  1.00 22.71           C  
ANISOU  547  CB  PRO B  69     3031   2342   3256    849   1174   -193       C  
ATOM    548  CG  PRO B  69       5.775  44.256  13.230  1.00 25.75           C  
ANISOU  548  CG  PRO B  69     3436   2686   3662    891   1289   -266       C  
ATOM    549  CD  PRO B  69       4.356  44.039  12.873  1.00 25.14           C  
ANISOU  549  CD  PRO B  69     3159   2678   3714    948   1339   -218       C  
ATOM    550  N   HIS B  70       6.322  41.865   9.194  1.00 17.97           N  
ANISOU  550  N   HIS B  70     2138   1925   2766    773    872     49       N  
ATOM    551  CA  HIS B  70       6.406  40.526   8.649  1.00 18.32           C  
ANISOU  551  CA  HIS B  70     2132   2072   2756    676    797    101       C  
ATOM    552  C   HIS B  70       7.672  40.357   7.864  1.00 18.36           C  
ANISOU  552  C   HIS B  70     2217   2065   2694    611    660    130       C  
ATOM    553  O   HIS B  70       8.222  41.327   7.346  1.00 17.85           O  
ANISOU  553  O   HIS B  70     2193   1928   2660    644    604    140       O  
ATOM    554  CB  HIS B  70       5.168  40.138   7.827  1.00 22.93           C  
ANISOU  554  CB  HIS B  70     2520   2741   3452    694    778    172       C  
ATOM    555  CG  HIS B  70       4.882  41.044   6.674  1.00 19.24           C  
ANISOU  555  CG  HIS B  70     1966   2246   3097    773    683    241       C  
ATOM    556  CD2 HIS B  70       4.299  42.264   6.621  1.00 22.08           C  
ANISOU  556  CD2 HIS B  70     2275   2537   3577    903    714    249       C  
ATOM    557  ND1 HIS B  70       5.166  40.694   5.371  1.00 17.76           N  
ANISOU  557  ND1 HIS B  70     1746   2102   2901    723    536    320       N  
ATOM    558  CE1 HIS B  70       4.787  41.676   4.564  1.00 19.14           C  
ANISOU  558  CE1 HIS B  70     1861   2236   3174    816    472    381       C  
ATOM    559  NE2 HIS B  70       4.263  42.636   5.297  1.00 25.76           N  
ANISOU  559  NE2 HIS B  70     2685   3002   4099    931    575    342       N  
ATOM    560  N   GLY B  71       8.124  39.112   7.788  1.00 14.60           N  
ANISOU  560  N   GLY B  71     1766   1655   2128    519    618    141       N  
ATOM    561  CA  GLY B  71       9.412  38.797   7.212  1.00 17.60           C  
ANISOU  561  CA  GLY B  71     2223   2029   2437    457    510    152       C  
ATOM    562  C   GLY B  71       9.320  38.019   5.914  1.00 15.91           C  
ANISOU  562  C   GLY B  71     1931   1878   2235    403    418    223       C  
ATOM    563  O   GLY B  71       8.272  37.464   5.566  1.00 13.24           O  
ANISOU  563  O   GLY B  71     1485   1602   1942    392    429    261       O  
ATOM    564  N   HIS B  72      10.442  38.005   5.202  1.00 13.80           N  
ANISOU  564  N   HIS B  72     1720   1596   1927    362    332    233       N  
ATOM    565  CA  HIS B  72      10.596  37.254   3.975  1.00 11.40           C  
ANISOU  565  CA  HIS B  72     1379   1342   1609    301    251    286       C  
ATOM    566  C   HIS B  72      11.876  36.480   4.057  1.00 15.48           C  
ANISOU  566  C   HIS B  72     1983   1861   2038    242    221    254       C  
ATOM    567  O   HIS B  72      12.907  37.046   4.413  1.00 15.03           O  
ANISOU  567  O   HIS B  72     1995   1759   1957    250    211    214       O  
ATOM    568  CB  HIS B  72      10.738  38.181   2.767  1.00 14.24           C  
ANISOU  568  CB  HIS B  72     1721   1674   2017    316    179    338       C  
ATOM    569  CG  HIS B  72       9.664  39.211   2.659  1.00 17.55           C  
ANISOU  569  CG  HIS B  72     2065   2067   2534    403    192    376       C  
ATOM    570  CD2 HIS B  72       9.706  40.558   2.793  1.00 19.29           C  
ANISOU  570  CD2 HIS B  72     2317   2200   2812    478    209    374       C  
ATOM    571  ND1 HIS B  72       8.364  38.898   2.332  1.00 23.20           N  
ANISOU  571  ND1 HIS B  72     2655   2848   3311    424    185    422       N  
ATOM    572  CE1 HIS B  72       7.644  40.005   2.290  1.00 22.11           C  
ANISOU  572  CE1 HIS B  72     2463   2668   3271    524    194    450       C  
ATOM    573  NE2 HIS B  72       8.434  41.025   2.564  1.00 24.77           N  
ANISOU  573  NE2 HIS B  72     2904   2903   3605    561    213    423       N  
ATOM    574  N   ILE B  73      11.812  35.204   3.680  1.00 14.52           N  
ANISOU  574  N   ILE B  73     1852   1789   1876    184    203    271       N  
ATOM    575  CA  ILE B  73      13.002  34.418   3.391  1.00  9.44           C  
ANISOU  575  CA  ILE B  73     1272   1146   1167    138    164    253       C  
ATOM    576  C   ILE B  73      13.280  34.621   1.931  1.00 11.79           C  
ANISOU  576  C   ILE B  73     1545   1455   1480    102    102    290       C  
ATOM    577  O   ILE B  73      12.403  34.382   1.092  1.00 12.90           O  
ANISOU  577  O   ILE B  73     1629   1633   1641     74     78    336       O  
ATOM    578  CB  ILE B  73      12.773  32.920   3.655  1.00 18.63           C  
ANISOU  578  CB  ILE B  73     2459   2337   2280     95    186    253       C  
ATOM    579  CG1 ILE B  73      12.595  32.679   5.163  1.00 18.90           C  
ANISOU  579  CG1 ILE B  73     2549   2355   2276    124    253    223       C  
ATOM    580  CG2 ILE B  73      13.926  32.081   3.099  1.00 15.24           C  
ANISOU  580  CG2 ILE B  73     2084   1904   1804     61    145    241       C  
ATOM    581  CD1 ILE B  73      13.861  32.784   5.954  1.00 21.61           C  
ANISOU  581  CD1 ILE B  73     2981   2667   2562    154    231    179       C  
ATOM    582  N   THR B  74      14.492  35.065   1.618  1.00 11.64           N  
ANISOU  582  N   THR B  74     1567   1407   1447     95     77    268       N  
ATOM    583  CA  THR B  74      14.800  35.474   0.260  1.00  8.93           C  
ANISOU  583  CA  THR B  74     1219   1065   1110     57     35    303       C  
ATOM    584  C   THR B  74      15.703  34.483  -0.465  1.00 14.31           C  
ANISOU  584  C   THR B  74     1929   1768   1739     -1     22    285       C  
ATOM    585  O   THR B  74      15.686  34.408  -1.693  1.00 12.31           O  
ANISOU  585  O   THR B  74     1679   1531   1467    -51     -3    317       O  
ATOM    586  CB  THR B  74      15.457  36.838   0.267  1.00 14.96           C  
ANISOU  586  CB  THR B  74     2007   1772   1903     77     34    292       C  
ATOM    587  CG2 THR B  74      14.495  37.871   0.871  1.00 12.67           C  
ANISOU  587  CG2 THR B  74     1698   1445   1673    145     55    309       C  
ATOM    588  OG1 THR B  74      16.628  36.777   1.084  1.00 16.14           O  
ANISOU  588  OG1 THR B  74     2193   1908   2034     76     48    224       O  
ATOM    589  N   SER B  75      16.497  33.736   0.288  1.00 13.98           N  
ANISOU  589  N   SER B  75     1916   1724   1672      9     40    235       N  
ATOM    590  CA  SER B  75      17.328  32.685  -0.299  1.00 15.80           C  
ANISOU  590  CA  SER B  75     2170   1967   1866    -26     40    212       C  
ATOM    591  C   SER B  75      17.784  31.700   0.763  1.00 10.62           C  
ANISOU  591  C   SER B  75     1544   1303   1186     12     52    175       C  
ATOM    592  O   SER B  75      18.137  32.076   1.877  1.00 10.63           O  
ANISOU  592  O   SER B  75     1556   1293   1191     59     48    149       O  
ATOM    593  CB  SER B  75      18.544  33.254  -1.024  1.00 19.13           C  
ANISOU  593  CB  SER B  75     2591   2382   2295    -51     39    188       C  
ATOM    594  OG  SER B  75      19.263  32.220  -1.691  1.00 25.58           O  
ANISOU  594  OG  SER B  75     3424   3211   3084    -80     56    162       O  
ATOM    595  N   VAL B  76      17.755  30.423   0.415  1.00 10.46           N  
ANISOU  595  N   VAL B  76     1555   1285   1137    -10     64    174       N  
ATOM    596  CA  VAL B  76      18.303  29.396   1.286  1.00 14.06           C  
ANISOU  596  CA  VAL B  76     2057   1718   1567     34     71    150       C  
ATOM    597  C   VAL B  76      19.021  28.416   0.369  1.00 16.12           C  
ANISOU  597  C   VAL B  76     2340   1966   1817     15     84    128       C  
ATOM    598  O   VAL B  76      18.568  28.164  -0.743  1.00 17.70           O  
ANISOU  598  O   VAL B  76     2544   2174   2005    -51     99    139       O  
ATOM    599  CB  VAL B  76      17.194  28.723   2.104  1.00 17.63           C  
ANISOU  599  CB  VAL B  76     2549   2158   1992     32     97    176       C  
ATOM    600  CG1 VAL B  76      16.145  28.171   1.179  1.00 17.38           C  
ANISOU  600  CG1 VAL B  76     2510   2139   1956    -45    115    204       C  
ATOM    601  CG2 VAL B  76      17.748  27.625   3.010  1.00 16.02           C  
ANISOU  601  CG2 VAL B  76     2423   1915   1749     80    101    165       C  
ATOM    602  N   SER B  77      20.169  27.914   0.804  1.00 15.65           N  
ANISOU  602  N   SER B  77     2292   1889   1764     75     76     93       N  
ATOM    603  CA  SER B  77      20.965  27.038  -0.034  1.00 11.11           C  
ANISOU  603  CA  SER B  77     1730   1297   1194     75    103     62       C  
ATOM    604  C   SER B  77      21.909  26.178   0.816  1.00 16.60           C  
ANISOU  604  C   SER B  77     2449   1960   1898    171     86     41       C  
ATOM    605  O   SER B  77      22.499  26.655   1.772  1.00 11.25           O  
ANISOU  605  O   SER B  77     1740   1300   1233    232     37     32       O  
ATOM    606  CB  SER B  77      21.749  27.889  -1.050  1.00 11.38           C  
ANISOU  606  CB  SER B  77     1700   1365   1259     40    115     33       C  
ATOM    607  OG  SER B  77      22.460  27.085  -1.982  1.00 19.29           O  
ANISOU  607  OG  SER B  77     2715   2353   2263     31    163     -5       O  
ATOM    608  N   VAL B  78      22.027  24.900   0.483  1.00  9.70           N  
ANISOU  608  N   VAL B  78     1638   1034   1013    188    120     33       N  
ATOM    609  CA  VAL B  78      22.981  24.035   1.139  1.00 10.41           C  
ANISOU  609  CA  VAL B  78     1752   1083   1120    296    101     19       C  
ATOM    610  C   VAL B  78      23.750  23.338   0.027  1.00 10.95           C  
ANISOU  610  C   VAL B  78     1812   1125   1223    305    158    -29       C  
ATOM    611  O   VAL B  78      23.131  22.807  -0.893  1.00 10.94           O  
ANISOU  611  O   VAL B  78     1872   1092   1192    229    217    -35       O  
ATOM    612  CB  VAL B  78      22.257  22.990   1.976  1.00 11.71           C  
ANISOU  612  CB  VAL B  78     2039   1177   1233    320    103     64       C  
ATOM    613  CG1 VAL B  78      23.258  21.991   2.560  1.00 11.71           C  
ANISOU  613  CG1 VAL B  78     2084   1118   1249    447     77     61       C  
ATOM    614  CG2 VAL B  78      21.434  23.667   3.093  1.00 10.36           C  
ANISOU  614  CG2 VAL B  78     1883   1033   1020    304     69    105       C  
ATOM    615  N   MET B  79      25.078  23.332   0.062  1.00 11.58           N  
ANISOU  615  N   MET B  79     1813   1220   1364    392    146    -71       N  
ATOM    616  CA  MET B  79      25.777  22.678  -1.051  1.00 18.65           C  
ANISOU  616  CA  MET B  79     2699   2089   2297    400    226   -127       C  
ATOM    617  C   MET B  79      25.475  21.194  -1.072  1.00 16.25           C  
ANISOU  617  C   MET B  79     2526   1678   1971    440    267   -120       C  
ATOM    618  O   MET B  79      25.187  20.601  -0.022  1.00 13.12           O  
ANISOU  618  O   MET B  79     2205   1229   1552    505    219    -73       O  
ATOM    619  CB  MET B  79      27.284  22.938  -1.044  1.00 19.02           C  
ANISOU  619  CB  MET B  79     2611   2181   2434    487    218   -181       C  
ATOM    620  CG  MET B  79      28.031  22.422   0.151  1.00 17.75           C  
ANISOU  620  CG  MET B  79     2425   2004   2314    638    134   -169       C  
ATOM    621  CE  MET B  79      30.091  24.340  -0.919  1.00 17.13           C  
ANISOU  621  CE  MET B  79     2016   2105   2388    578    177   -293       C  
ATOM    622  S   MET B  79      29.971  22.483  -0.211  1.00 42.69           S  
ANISOU  622  S   MET B  79     5382   5224   5616    745    148   -256       S  
ATOM    623  N   ARG B  80      25.547  20.599  -2.261  1.00 13.33           N  
ANISOU  623  N   ARG B  80     2198   1268   1598    396    360   -168       N  
ATOM    624  CA  ARG B  80      25.080  19.229  -2.442  1.00 13.98           C  
ANISOU  624  CA  ARG B  80     2428   1234   1648    398    414   -169       C  
ATOM    625  C   ARG B  80      25.673  18.259  -1.430  1.00 14.96           C  
ANISOU  625  C   ARG B  80     2600   1271   1812    558    383   -148       C  
ATOM    626  O   ARG B  80      24.953  17.458  -0.847  1.00 15.17           O  
ANISOU  626  O   ARG B  80     2761   1210   1792    558    376   -101       O  
ATOM    627  CB  ARG B  80      25.388  18.733  -3.861  1.00 14.64           C  
ANISOU  627  CB  ARG B  80     2547   1286   1730    347    526   -246       C  
ATOM    628  CG  ARG B  80      24.511  19.350  -4.922  1.00 20.07           C  
ANISOU  628  CG  ARG B  80     3254   2030   2342    173    552   -252       C  
ATOM    629  CD  ARG B  80      25.020  18.977  -6.305  1.00 17.26           C  
ANISOU  629  CD  ARG B  80     2932   1653   1971    127    665   -335       C  
ATOM    630  NE  ARG B  80      25.079  17.528  -6.478  1.00 19.14           N  
ANISOU  630  NE  ARG B  80     3303   1761   2208    166    738   -378       N  
ATOM    631  CZ  ARG B  80      24.105  16.802  -7.025  1.00 27.53           C  
ANISOU  631  CZ  ARG B  80     4512   2759   3188     50    771   -389       C  
ATOM    632  NH1 ARG B  80      22.987  17.380  -7.444  1.00 29.56           N1+
ANISOU  632  NH1 ARG B  80     4784   3085   3362   -106    725   -357       N1+
ATOM    633  NH2 ARG B  80      24.234  15.493  -7.133  1.00 25.12           N  
ANISOU  633  NH2 ARG B  80     4338   2318   2888     89    845   -433       N  
ATOM    634  N   SER B  81      26.981  18.360  -1.205  1.00 15.70           N  
ANISOU  634  N   SER B  81     2582   1392   1992    691    360   -178       N  
ATOM    635  CA  SER B  81      27.670  17.483  -0.262  1.00 22.88           C  
ANISOU  635  CA  SER B  81     3522   2226   2947    867    309   -151       C  
ATOM    636  C   SER B  81      27.055  17.464   1.134  1.00 21.23           C  
ANISOU  636  C   SER B  81     3393   2000   2675    894    206    -61       C  
ATOM    637  O   SER B  81      27.178  16.471   1.844  1.00 17.67           O  
ANISOU  637  O   SER B  81     3052   1445   2217   1005    180    -17       O  
ATOM    638  CB  SER B  81      29.127  17.900  -0.126  1.00 28.62           C  
ANISOU  638  CB  SER B  81     4065   3028   3781    995    268   -193       C  
ATOM    639  OG  SER B  81      29.857  17.579  -1.283  1.00 42.99           O  
ANISOU  639  OG  SER B  81     5829   4835   5672   1011    384   -279       O  
ATOM    640  N   TYR B  82      26.437  18.570   1.541  1.00 15.43           N  
ANISOU  640  N   TYR B  82     2611   1360   1891    800    154    -33       N  
ATOM    641  CA  TYR B  82      25.931  18.701   2.914  1.00 19.98           C  
ANISOU  641  CA  TYR B  82     3254   1935   2402    823     65     42       C  
ATOM    642  C   TYR B  82      24.421  18.593   3.024  1.00 18.70           C  
ANISOU  642  C   TYR B  82     3215   1739   2151    689    109     85       C  
ATOM    643  O   TYR B  82      23.857  18.826   4.091  1.00 16.28           O  
ANISOU  643  O   TYR B  82     2963   1441   1782    682     62    141       O  
ATOM    644  CB  TYR B  82      26.397  20.021   3.535  1.00 17.04           C  
ANISOU  644  CB  TYR B  82     2743   1690   2042    831    -29     36       C  
ATOM    645  CG  TYR B  82      27.811  19.955   4.040  1.00 17.59           C  
ANISOU  645  CG  TYR B  82     2711   1790   2182    985   -117     19       C  
ATOM    646  CD1 TYR B  82      28.885  20.145   3.177  1.00 16.46           C  
ANISOU  646  CD1 TYR B  82     2414   1694   2144   1020    -86    -54       C  
ATOM    647  CD2 TYR B  82      28.075  19.661   5.372  1.00 17.45           C  
ANISOU  647  CD2 TYR B  82     2751   1756   2124   1094   -231     76       C  
ATOM    648  CE1 TYR B  82      30.188  20.059   3.628  1.00 23.25           C  
ANISOU  648  CE1 TYR B  82     3153   2593   3086   1163   -170    -75       C  
ATOM    649  CE2 TYR B  82      29.372  19.572   5.840  1.00 21.62           C  
ANISOU  649  CE2 TYR B  82     3173   2322   2719   1242   -334     63       C  
ATOM    650  CZ  TYR B  82      30.426  19.777   4.965  1.00 30.45           C  
ANISOU  650  CZ  TYR B  82     4112   3496   3961   1278   -305    -14       C  
ATOM    651  OH  TYR B  82      31.718  19.690   5.422  1.00 35.99           O  
ANISOU  651  OH  TYR B  82     4678   4251   4747   1414   -407    -31       O  
ATOM    652  N   ARG B  83      23.760  18.240   1.926  1.00 15.88           N  
ANISOU  652  N   ARG B  83     2900   1347   1785    579    202     56       N  
ATOM    653  CA  ARG B  83      22.301  18.130   1.938  1.00 13.71           C  
ANISOU  653  CA  ARG B  83     2714   1055   1442    440    241     90       C  
ATOM    654  C   ARG B  83      21.824  16.880   2.671  1.00 14.65           C  
ANISOU  654  C   ARG B  83     3011   1043   1512    461    266    141       C  
ATOM    655  O   ARG B  83      22.569  15.916   2.818  1.00 15.76           O  
ANISOU  655  O   ARG B  83     3232   1082   1676    574    271    143       O  
ATOM    656  CB  ARG B  83      21.751  18.130   0.510  1.00 13.35           C  
ANISOU  656  CB  ARG B  83     2657   1023   1394    306    314     41       C  
ATOM    657  CG  ARG B  83      21.899  19.485  -0.175  1.00 12.42           C  
ANISOU  657  CG  ARG B  83     2390   1030   1299    253    293     12       C  
ATOM    658  CD  ARG B  83      21.413  19.466  -1.624  1.00 12.30           C  
ANISOU  658  CD  ARG B  83     2381   1029   1262    125    352    -30       C  
ATOM    659  NE  ARG B  83      21.806  20.719  -2.275  1.00 15.94           N  
ANISOU  659  NE  ARG B  83     2719   1594   1745     97    334    -51       N  
ATOM    660  CZ  ARG B  83      21.569  21.019  -3.545  1.00 17.49           C  
ANISOU  660  CZ  ARG B  83     2906   1826   1914     -6    369    -81       C  
ATOM    661  NH1 ARG B  83      20.927  20.162  -4.326  1.00 12.09           N1+
ANISOU  661  NH1 ARG B  83     2321   1092   1179    -98    416   -102       N1+
ATOM    662  NH2 ARG B  83      21.976  22.189  -4.024  1.00 12.72           N  
ANISOU  662  NH2 ARG B  83     2205   1303   1326    -25    355    -89       N  
ATOM    663  N   HIS B  84      20.563  16.922   3.104  1.00 15.81           N  
ANISOU  663  N   HIS B  84     3218   1191   1598    349    289    182       N  
ATOM    664  CA  HIS B  84      19.877  15.786   3.707  1.00 15.25           C  
ANISOU  664  CA  HIS B  84     3325    996   1472    319    336    230       C  
ATOM    665  C   HIS B  84      20.412  15.526   5.102  1.00 16.02           C  
ANISOU  665  C   HIS B  84     3478   1072   1537    445    273    285       C  
ATOM    666  O   HIS B  84      20.321  14.421   5.619  1.00 17.18           O  
ANISOU  666  O   HIS B  84     3733   1143   1653    458    294    306       O  
ATOM    667  CB  HIS B  84      19.985  14.551   2.810  1.00 16.16           C  
ANISOU  667  CB  HIS B  84     3549    986   1605    297    411    192       C  
ATOM    668  CG  HIS B  84      19.718  14.849   1.365  1.00 16.19           C  
ANISOU  668  CG  HIS B  84     3473   1045   1633    181    453    119       C  
ATOM    669  CD2 HIS B  84      20.496  14.702   0.263  1.00 18.19           C  
ANISOU  669  CD2 HIS B  84     3692   1289   1929    208    481     49       C  
ATOM    670  ND1 HIS B  84      18.519  15.362   0.923  1.00 16.68           N  
ANISOU  670  ND1 HIS B  84     3483   1187   1667     13    468    114       N  
ATOM    671  CE1 HIS B  84      18.564  15.522  -0.390  1.00 14.69           C  
ANISOU  671  CE1 HIS B  84     3181    973   1428    -59    489     51       C  
ATOM    672  NE2 HIS B  84      19.751  15.128  -0.816  1.00 15.20           N  
ANISOU  672  NE2 HIS B  84     3263    983   1530     51    507      7       N  
ATOM    673  N   LEU B  85      20.967  16.574   5.693  1.00 15.49           N  
ANISOU  673  N   LEU B  85     3322   1091   1472    524    190    298       N  
ATOM    674  CA  LEU B  85      21.474  16.512   7.051  1.00 21.65           C  
ANISOU  674  CA  LEU B  85     4124   1891   2210    619    110    335       C  
ATOM    675  C   LEU B  85      20.617  17.350   7.992  1.00 20.17           C  
ANISOU  675  C   LEU B  85     3930   1778   1955    546    104    358       C  
ATOM    676  O   LEU B  85      20.852  17.361   9.200  1.00 20.44           O  
ANISOU  676  O   LEU B  85     4002   1828   1935    597     49    385       O  
ATOM    677  CB  LEU B  85      22.934  16.979   7.122  1.00 18.89           C  
ANISOU  677  CB  LEU B  85     3668   1591   1917    771      5    316       C  
ATOM    678  CG  LEU B  85      24.067  16.035   6.686  1.00 22.91           C  
ANISOU  678  CG  LEU B  85     4167   2038   2500    892    -10    295       C  
ATOM    679  CD1 LEU B  85      23.780  14.596   7.045  1.00 18.99           C  
ANISOU  679  CD1 LEU B  85     3823   1427   1967    892     34    332       C  
ATOM    680  CD2 LEU B  85      24.361  16.131   5.241  1.00 38.59           C  
ANISOU  680  CD2 LEU B  85     6082   4010   4570    884     55    229       C  
ATOM    681  N   GLY B  86      19.596  18.011   7.445  1.00 15.78           N  
ANISOU  681  N   GLY B  86     3327   1267   1403    422    166    346       N  
ATOM    682  CA  GLY B  86      18.740  18.887   8.232  1.00 15.30           C  
ANISOU  682  CA  GLY B  86     3234   1280   1298    355    178    356       C  
ATOM    683  C   GLY B  86      19.289  20.293   8.383  1.00 16.64           C  
ANISOU  683  C   GLY B  86     3303   1546   1475    407    105    342       C  
ATOM    684  O   GLY B  86      18.822  21.090   9.217  1.00 13.78           O  
ANISOU  684  O   GLY B  86     2924   1240   1071    381    104    343       O  
ATOM    685  N   LEU B  87      20.278  20.618   7.572  1.00 13.15           N  
ANISOU  685  N   LEU B  87     2747   1141   1110    460     54    296       N  
ATOM    686  CA  LEU B  87      20.908  21.919   7.673  1.00 12.60           C  
ANISOU  686  CA  LEU B  87     2546   1171   1071    489    -16    257       C  
ATOM    687  C   LEU B  87      19.971  23.057   7.269  1.00 14.93           C  
ANISOU  687  C   LEU B  87     2750   1537   1387    384     30    234       C  
ATOM    688  O   LEU B  87      19.906  24.076   7.945  1.00 15.23           O  
ANISOU  688  O   LEU B  87     2754   1628   1404    386      2    224       O  
ATOM    689  CB  LEU B  87      22.173  21.955   6.833  1.00 19.78           C  
ANISOU  689  CB  LEU B  87     3349   2102   2065    555    -62    210       C  
ATOM    690  CG  LEU B  87      23.411  22.620   7.410  1.00 32.49           C  
ANISOU  690  CG  LEU B  87     4876   3775   3696    648   -170    184       C  
ATOM    691  CD1 LEU B  87      23.731  22.028   8.767  1.00 38.15           C  
ANISOU  691  CD1 LEU B  87     5712   4453   4332    744   -247    234       C  
ATOM    692  CD2 LEU B  87      24.585  22.417   6.446  1.00 32.45           C  
ANISOU  692  CD2 LEU B  87     4759   3781   3789    705   -183    135       C  
ATOM    693  N   ALA B  88      19.265  22.901   6.153  1.00 18.58           N  
ANISOU  693  N   ALA B  88     3175   1997   1889    296     94    225       N  
ATOM    694  CA  ALA B  88      18.335  23.934   5.704  1.00 14.69           C  
ANISOU  694  CA  ALA B  88     2590   1568   1422    210    125    215       C  
ATOM    695  C   ALA B  88      17.237  24.137   6.751  1.00 11.27           C  
ANISOU  695  C   ALA B  88     2207   1139    938    177    170    245       C  
ATOM    696  O   ALA B  88      16.818  25.268   7.011  1.00 12.29           O  
ANISOU  696  O   ALA B  88     2269   1320   1079    164    174    234       O  
ATOM    697  CB  ALA B  88      17.718  23.556   4.370  1.00 11.80           C  
ANISOU  697  CB  ALA B  88     2193   1200   1090    120    171    209       C  
ATOM    698  N   LYS B  89      16.758  23.038   7.306  1.00 20.34           N  
ANISOU  698  N   LYS B  89     3980   1731   2018    580   -152    484       N  
ATOM    699  CA  LYS B  89      15.793  23.071   8.397  1.00 22.99           C  
ANISOU  699  CA  LYS B  89     4476   1981   2277    426    -62    566       C  
ATOM    700  C   LYS B  89      16.299  23.931   9.548  1.00 22.64           C  
ANISOU  700  C   LYS B  89     4412   2023   2168    495   -114    605       C  
ATOM    701  O   LYS B  89      15.597  24.819  10.043  1.00 19.82           O  
ANISOU  701  O   LYS B  89     3972   1750   1810    361    -32    625       O  
ATOM    702  CB  LYS B  89      15.574  21.654   8.921  1.00 31.02           C  
ANISOU  702  CB  LYS B  89     5855   2739   3193    421    -58    623       C  
ATOM    703  CG  LYS B  89      14.125  21.221   8.988  1.00 48.97           C  
ANISOU  703  CG  LYS B  89     8232   4919   5454    147    110    640       C  
ATOM    704  CD  LYS B  89      14.009  19.823   9.608  1.00 62.78           C  
ANISOU  704  CD  LYS B  89    10261   6479   7114    119    113    646       C  
ATOM    705  CE  LYS B  89      12.552  19.443   9.896  1.00 73.29           C  
ANISOU  705  CE  LYS B  89    11670   7758   8418   -177    290    641       C  
ATOM    706  NZ  LYS B  89      12.397  18.079  10.520  1.00 78.78           N1+
ANISOU  706  NZ  LYS B  89    12667   8261   9004   -225    304    651       N1+
ATOM    707  N   ARG B  90      17.526  23.662   9.968  1.00 21.53           N  
ANISOU  707  N   ARG B  90     4339   1870   1972    717   -261    598       N  
ATOM    708  CA  ARG B  90      18.132  24.370  11.078  1.00 21.70           C  
ANISOU  708  CA  ARG B  90     4333   1983   1929    796   -331    609       C  
ATOM    709  C   ARG B  90      18.265  25.875  10.791  1.00 19.89           C  
ANISOU  709  C   ARG B  90     3804   1974   1779    746   -310    564       C  
ATOM    710  O   ARG B  90      17.977  26.722  11.638  1.00 19.51           O  
ANISOU  710  O   ARG B  90     3733   1987   1693    677   -279    592       O  
ATOM    711  CB  ARG B  90      19.495  23.765  11.347  1.00 23.21           C  
ANISOU  711  CB  ARG B  90     4548   2180   2089   1030   -492    540       C  
ATOM    712  CG  ARG B  90      20.244  24.362  12.495  1.00 43.66           C  
ANISOU  712  CG  ARG B  90     7099   4871   4617   1118   -577    521       C  
ATOM    713  CD  ARG B  90      21.436  23.483  12.801  1.00 46.94           C  
ANISOU  713  CD  ARG B  90     7587   5260   4987   1341   -726    444       C  
ATOM    714  NE  ARG B  90      22.297  24.061  13.823  1.00 52.81           N  
ANISOU  714  NE  ARG B  90     8269   6121   5677   1445   -824    401       N  
ATOM    715  CZ  ARG B  90      23.554  23.684  14.023  1.00 58.24           C  
ANISOU  715  CZ  ARG B  90     8920   6870   6339   1658   -970    294       C  
ATOM    716  NH1 ARG B  90      24.280  24.268  14.969  1.00 62.66           N1+
ANISOU  716  NH1 ARG B  90     9416   7543   6849   1738  -1054    246       N1+
ATOM    717  NH2 ARG B  90      24.090  22.732  13.263  1.00 56.44           N  
ANISOU  717  NH2 ARG B  90     8713   6597   6133   1794  -1033    220       N  
ATOM    718  N   LEU B  91      18.703  26.196   9.581  1.00 18.96           N  
ANISOU  718  N   LEU B  91     3464   1973   1769    768   -321    484       N  
ATOM    719  CA  LEU B  91      18.900  27.582   9.211  1.00 17.57           C  
ANISOU  719  CA  LEU B  91     3029   1983   1663    706   -298    437       C  
ATOM    720  C   LEU B  91      17.565  28.322   9.180  1.00 19.70           C  
ANISOU  720  C   LEU B  91     3261   2258   1967    508   -169    477       C  
ATOM    721  O   LEU B  91      17.473  29.455   9.662  1.00 17.18           O  
ANISOU  721  O   LEU B  91     2852   2027   1648    457   -153    476       O  
ATOM    722  CB  LEU B  91      19.616  27.677   7.851  1.00 17.14           C  
ANISOU  722  CB  LEU B  91     2780   2039   1693    749   -319    346       C  
ATOM    723  CG  LEU B  91      21.086  27.231   7.842  1.00 20.38           C  
ANISOU  723  CG  LEU B  91     3140   2521   2083    955   -450    257       C  
ATOM    724  CD1 LEU B  91      21.635  27.073   6.421  1.00 19.72           C  
ANISOU  724  CD1 LEU B  91     2888   2532   2071    980   -442    159       C  
ATOM    725  CD2 LEU B  91      21.961  28.192   8.644  1.00 20.39           C  
ANISOU  725  CD2 LEU B  91     3022   2671   2054   1002   -518    213       C  
ATOM    726  N   MET B  92      16.541  27.690   8.600  1.00 16.37           N  
ANISOU  726  N   MET B  92     2898   1748   1573    404    -83    493       N  
ATOM    727  CA  MET B  92      15.217  28.311   8.483  1.00 15.60           C  
ANISOU  727  CA  MET B  92     2736   1678   1512    235     29    499       C  
ATOM    728  C   MET B  92      14.617  28.596   9.867  1.00 16.07           C  
ANISOU  728  C   MET B  92     2901   1712   1492    168     79    544       C  
ATOM    729  O   MET B  92      14.039  29.645  10.092  1.00 17.87           O  
ANISOU  729  O   MET B  92     3021   2027   1743     98    125    527       O  
ATOM    730  CB  MET B  92      14.248  27.415   7.717  1.00 15.88           C  
ANISOU  730  CB  MET B  92     2819   1633   1580    134    105    486       C  
ATOM    731  CG  MET B  92      14.558  27.257   6.239  1.00 29.89           C  
ANISOU  731  CG  MET B  92     4473   3450   3432    169     78    430       C  
ATOM    732  CE  MET B  92      12.216  28.853   5.319  1.00 49.62           C  
ANISOU  732  CE  MET B  92     6707   6116   6031    -59    207    361       C  
ATOM    733  S   MET B  92      14.175  28.936   5.295  1.00 49.09           S  
ANISOU  733  S   MET B  92     6648   6062   5943    113     94    387       S  
ATOM    734  N   VAL B  93      14.733  27.634  10.776  1.00 18.84           N  
ANISOU  734  N   VAL B  93     3484   1935   1741    194     69    599       N  
ATOM    735  CA  VAL B  93      14.173  27.777  12.113  1.00 19.04           C  
ANISOU  735  CA  VAL B  93     3644   1930   1662    117    129    644       C  
ATOM    736  C   VAL B  93      14.830  28.942  12.836  1.00 20.83           C  
ANISOU  736  C   VAL B  93     3775   2273   1866    195     62    634       C  
ATOM    737  O   VAL B  93      14.146  29.766  13.438  1.00 18.38           O  
ANISOU  737  O   VAL B  93     3415   2028   1541    105    133    623       O  
ATOM    738  CB  VAL B  93      14.314  26.476  12.914  1.00 22.16           C  
ANISOU  738  CB  VAL B  93     4358   2139   1922    140    118    718       C  
ATOM    739  CG1 VAL B  93      13.980  26.693  14.383  1.00 22.76           C  
ANISOU  739  CG1 VAL B  93     4531   2221   1896     78    158    739       C  
ATOM    740  CG2 VAL B  93      13.406  25.419  12.316  1.00 20.76           C  
ANISOU  740  CG2 VAL B  93     4283   1839   1764     -2    220    716       C  
ATOM    741  N   GLN B  94      16.150  29.038  12.730  1.00 17.68           N  
ANISOU  741  N   GLN B  94     3331   1917   1471    359    -71    616       N  
ATOM    742  CA  GLN B  94      16.875  30.112  13.376  1.00 17.43           C  
ANISOU  742  CA  GLN B  94     3201   2001   1419    422   -141    586       C  
ATOM    743  C   GLN B  94      16.461  31.480  12.819  1.00 16.00           C  
ANISOU  743  C   GLN B  94     2802   1939   1340    328    -85    536       C  
ATOM    744  O   GLN B  94      16.305  32.439  13.570  1.00 15.87           O  
ANISOU  744  O   GLN B  94     2753   1980   1296    296    -73    523       O  
ATOM    745  CB  GLN B  94      18.373  29.891  13.222  1.00 27.78           C  
ANISOU  745  CB  GLN B  94     4468   3362   2725    605   -290    543       C  
ATOM    746  CG  GLN B  94      19.217  30.849  14.027  1.00 37.75           C  
ANISOU  746  CG  GLN B  94     5647   4748   3950    668   -374    497       C  
ATOM    747  CD  GLN B  94      20.446  30.185  14.616  1.00 49.40           C  
ANISOU  747  CD  GLN B  94     7201   6231   5336    873   -535    471       C  
ATOM    748  NE2 GLN B  94      21.274  30.975  15.294  1.00 55.96           N  
ANISOU  748  NE2 GLN B  94     7938   7192   6132    934   -622    407       N  
ATOM    749  OE1 GLN B  94      20.646  28.973  14.474  1.00 49.18           O  
ANISOU  749  OE1 GLN B  94     7315   6093   5276    976   -583    492       O  
ATOM    750  N   SER B  95      16.270  31.567  11.504  1.00 15.13           N  
ANISOU  750  N   SER B  95     2563   1852   1333    293    -58    506       N  
ATOM    751  CA  SER B  95      15.802  32.812  10.910  1.00 14.07           C  
ANISOU  751  CA  SER B  95     2271   1798   1277    217    -17    469       C  
ATOM    752  C   SER B  95      14.378  33.141  11.378  1.00 14.35           C  
ANISOU  752  C   SER B  95     2328   1820   1304    112     83    472       C  
ATOM    753  O   SER B  95      14.095  34.277  11.786  1.00 13.78           O  
ANISOU  753  O   SER B  95     2196   1801   1237     89     94    443       O  
ATOM    754  CB  SER B  95      15.921  32.782   9.384  1.00 13.42           C  
ANISOU  754  CB  SER B  95     2078   1741   1281    209    -17    441       C  
ATOM    755  OG  SER B  95      15.503  34.026   8.830  1.00 13.43           O  
ANISOU  755  OG  SER B  95     1970   1797   1334    151      6    415       O  
ATOM    756  N   GLN B  96      13.493  32.150  11.340  1.00 16.74           N  
ANISOU  756  N   GLN B  96     2715   2054   1591     45    157    490       N  
ATOM    757  CA  GLN B  96      12.134  32.291  11.889  1.00 17.80           C  
ANISOU  757  CA  GLN B  96     2858   2200   1705    -70    268    467       C  
ATOM    758  C   GLN B  96      12.105  32.804  13.324  1.00 18.16           C  
ANISOU  758  C   GLN B  96     2975   2267   1657    -77    286    475       C  
ATOM    759  O   GLN B  96      11.363  33.727  13.655  1.00 17.29           O  
ANISOU  759  O   GLN B  96     2779   2229   1560   -119    335    420       O  
ATOM    760  CB  GLN B  96      11.404  30.942  11.912  1.00 22.78           C  
ANISOU  760  CB  GLN B  96     3615   2743   2298   -169    355    486       C  
ATOM    761  CG  GLN B  96      10.788  30.511  10.609  1.00 43.75           C  
ANISOU  761  CG  GLN B  96     6178   5401   5044   -222    385    442       C  
ATOM    762  CD  GLN B  96       9.970  29.235  10.763  1.00 54.22           C  
ANISOU  762  CD  GLN B  96     7637   6638   6326   -361    490    443       C  
ATOM    763  NE2 GLN B  96       9.413  28.756   9.656  1.00 54.85           N  
ANISOU  763  NE2 GLN B  96     7641   6720   6478   -418    516    391       N  
ATOM    764  OE1 GLN B  96       9.821  28.704  11.872  1.00 57.53           O  
ANISOU  764  OE1 GLN B  96     8238   6985   6637   -429    552    486       O  
ATOM    765  N   ARG B  97      12.871  32.153  14.182  1.00 16.38           N  
ANISOU  765  N   ARG B  97     2919   1977   1328    -26    242    535       N  
ATOM    766  CA  ARG B  97      12.876  32.518  15.580  1.00 17.17           C  
ANISOU  766  CA  ARG B  97     3116   2094   1314    -32    255    546       C  
ATOM    767  C   ARG B  97      13.344  33.964  15.760  1.00 18.63           C  
ANISOU  767  C   ARG B  97     3161   2380   1538     27    193    493       C  
ATOM    768  O   ARG B  97      12.761  34.709  16.537  1.00 19.55           O  
ANISOU  768  O   ARG B  97     3263   2548   1617    -18    246    454       O  
ATOM    769  CB  ARG B  97      13.694  31.518  16.395  1.00 18.41           C  
ANISOU  769  CB  ARG B  97     3506   2154   1337     43    189    623       C  
ATOM    770  CG  ARG B  97      13.036  30.142  16.404  1.00 34.02           C  
ANISOU  770  CG  ARG B  97     5681   3996   3249    -51    277    678       C  
ATOM    771  CD  ARG B  97      13.863  29.097  17.118  1.00 39.08           C  
ANISOU  771  CD  ARG B  97     6524   4525   3802     50    180    728       C  
ATOM    772  NE  ARG B  97      13.375  28.833  18.462  1.00 47.75           N  
ANISOU  772  NE  ARG B  97     7769   5589   4785    -32    243    742       N  
ATOM    773  CZ  ARG B  97      13.766  29.494  19.543  1.00 52.00           C  
ANISOU  773  CZ  ARG B  97     8326   6190   5240     21    197    739       C  
ATOM    774  NH1 ARG B  97      14.662  30.468  19.445  1.00 58.09           N1+
ANISOU  774  NH1 ARG B  97     8973   7064   6034    149     85    712       N1+
ATOM    775  NH2 ARG B  97      13.247  29.178  20.719  1.00 47.34           N  
ANISOU  775  NH2 ARG B  97     7884   5564   4538    -65    267    753       N  
ATOM    776  N   ALA B  98      14.355  34.377  15.008  1.00 15.64           N  
ANISOU  776  N   ALA B  98     2679   2030   1232    111     91    479       N  
ATOM    777  CA  ALA B  98      14.847  35.748  15.118  1.00 16.66           C  
ANISOU  777  CA  ALA B  98     2697   2236   1395    137     40    425       C  
ATOM    778  C   ALA B  98      13.844  36.758  14.569  1.00 20.93           C  
ANISOU  778  C   ALA B  98     3126   2806   2020     77    101    373       C  
ATOM    779  O   ALA B  98      13.709  37.862  15.114  1.00 17.75           O  
ANISOU  779  O   ALA B  98     2695   2438   1610     74     99    326       O  
ATOM    780  CB  ALA B  98      16.176  35.894  14.440  1.00 14.82           C  
ANISOU  780  CB  ALA B  98     2385   2037   1208    207    -63    410       C  
ATOM    781  N   MET B  99      13.125  36.386  13.508  1.00 14.07           N  
ANISOU  781  N   MET B  99     2202   1921   1225     43    146    372       N  
ATOM    782  CA  MET B  99      12.062  37.258  12.994  1.00 16.00           C  
ANISOU  782  CA  MET B  99     2348   2196   1537     17    185    312       C  
ATOM    783  C   MET B  99      11.053  37.595  14.080  1.00 14.57           C  
ANISOU  783  C   MET B  99     2178   2053   1304    -20    262    258       C  
ATOM    784  O   MET B  99      10.686  38.759  14.256  1.00 14.63           O  
ANISOU  784  O   MET B  99     2132   2093   1334      8    252    193       O  
ATOM    785  CB  MET B  99      11.303  36.616  11.847  1.00 15.52           C  
ANISOU  785  CB  MET B  99     2229   2127   1539    -13    221    304       C  
ATOM    786  CG  MET B  99      12.048  36.593  10.554  1.00 19.67           C  
ANISOU  786  CG  MET B  99     2714   2635   2125     22    155    330       C  
ATOM    787  CE  MET B  99      12.125  35.988   7.694  1.00 14.47           C  
ANISOU  787  CE  MET B  99     1958   1966   1572     32    112    335       C  
ATOM    788  S   MET B  99      10.965  35.650   9.224  1.00 30.23           S  
ANISOU  788  S   MET B  99     3991   3972   3524    -21    201    306       S  
ATOM    789  N   VAL B 100      10.596  36.563  14.782  1.00 15.36           N  
ANISOU  789  N   VAL B 100     2364   2144   1328    -88    345    280       N  
ATOM    790  CA  VAL B 100       9.587  36.725  15.821  1.00 16.38           C  
ANISOU  790  CA  VAL B 100     2505   2330   1391   -155    449    219       C  
ATOM    791  C   VAL B 100      10.140  37.440  17.043  1.00 17.04           C  
ANISOU  791  C   VAL B 100     2658   2431   1388   -117    418    214       C  
ATOM    792  O   VAL B 100       9.573  38.433  17.492  1.00 17.41           O  
ANISOU  792  O   VAL B 100     2639   2539   1438   -106    443    127       O  
ATOM    793  CB  VAL B 100       9.019  35.344  16.258  1.00 17.45           C  
ANISOU  793  CB  VAL B 100     2753   2434   1441   -277    563    252       C  
ATOM    794  CG1 VAL B 100       8.075  35.489  17.439  1.00 19.22           C  
ANISOU  794  CG1 VAL B 100     3002   2732   1569   -374    692    185       C  
ATOM    795  CG2 VAL B 100       8.316  34.696  15.095  1.00 19.09           C  
ANISOU  795  CG2 VAL B 100     2876   2640   1737   -335    604    227       C  
ATOM    796  N   GLU B 101      11.246  36.923  17.572  1.00 16.93           N  
ANISOU  796  N   GLU B 101     2775   2367   1293    -84    355    295       N  
ATOM    797  CA  GLU B 101      11.824  37.394  18.835  1.00 17.60           C  
ANISOU  797  CA  GLU B 101     2946   2472   1267    -50    318    292       C  
ATOM    798  C   GLU B 101      12.449  38.793  18.776  1.00 17.03           C  
ANISOU  798  C   GLU B 101     2782   2436   1254     18    227    232       C  
ATOM    799  O   GLU B 101      12.410  39.533  19.756  1.00 17.65           O  
ANISOU  799  O   GLU B 101     2885   2554   1267     24    230    179       O  
ATOM    800  CB  GLU B 101      12.870  36.397  19.332  1.00 18.16           C  
ANISOU  800  CB  GLU B 101     3183   2485   1232     -4    246    383       C  
ATOM    801  CG  GLU B 101      12.294  35.038  19.671  1.00 21.24           C  
ANISOU  801  CG  GLU B 101     3744   2805   1522    -83    338    451       C  
ATOM    802  CD  GLU B 101      13.356  34.007  20.008  1.00 22.33           C  
ANISOU  802  CD  GLU B 101     4074   2854   1557      4    237    544       C  
ATOM    803  OE1 GLU B 101      14.530  34.375  20.212  1.00 25.64           O  
ANISOU  803  OE1 GLU B 101     4476   3302   1964    130     96    539       O  
ATOM    804  OE2 GLU B 101      13.015  32.814  20.070  1.00 30.18           O1-
ANISOU  804  OE2 GLU B 101     5241   3749   2478    -51    294    612       O1-
ATOM    805  N   VAL B 102      13.047  39.144  17.636  1.00 16.05           N  
ANISOU  805  N   VAL B 102     2567   2290   1240     56    153    238       N  
ATOM    806  CA  VAL B 102      13.720  40.435  17.527  1.00 16.52           C  
ANISOU  806  CA  VAL B 102     2571   2361   1345     87     76    186       C  
ATOM    807  C   VAL B 102      12.802  41.509  16.956  1.00 16.86           C  
ANISOU  807  C   VAL B 102     2540   2394   1474     86    105    118       C  
ATOM    808  O   VAL B 102      12.634  42.565  17.549  1.00 19.09           O  
ANISOU  808  O   VAL B 102     2829   2683   1743    101     96     48       O  
ATOM    809  CB  VAL B 102      15.032  40.366  16.685  1.00 18.47           C  
ANISOU  809  CB  VAL B 102     2776   2599   1642    109    -16    215       C  
ATOM    810  CG1 VAL B 102      15.693  41.753  16.590  1.00 16.57           C  
ANISOU  810  CG1 VAL B 102     2494   2364   1438     95    -71    152       C  
ATOM    811  CG2 VAL B 102      16.002  39.380  17.287  1.00 16.23           C  
ANISOU  811  CG2 VAL B 102     2557   2336   1272    155    -74    256       C  
ATOM    812  N   TYR B 103      12.195  41.221  15.812  1.00 15.01           N  
ANISOU  812  N   TYR B 103     2244   2139   1319     84    127    132       N  
ATOM    813  CA  TYR B 103      11.452  42.224  15.052  1.00 14.94           C  
ANISOU  813  CA  TYR B 103     2178   2109   1388    119    116     72       C  
ATOM    814  C   TYR B 103       9.936  42.077  15.178  1.00 17.33           C  
ANISOU  814  C   TYR B 103     2417   2467   1701    128    194     -2       C  
ATOM    815  O   TYR B 103       9.181  42.826  14.579  1.00 16.58           O  
ANISOU  815  O   TYR B 103     2267   2368   1665    190    171    -70       O  
ATOM    816  CB  TYR B 103      11.876  42.167  13.576  1.00 14.45           C  
ANISOU  816  CB  TYR B 103     2090   2001   1400    122     66    121       C  
ATOM    817  CG  TYR B 103      13.356  42.396  13.376  1.00 14.30           C  
ANISOU  817  CG  TYR B 103     2102   1958   1374     94      4    162       C  
ATOM    818  CD1 TYR B 103      13.883  43.682  13.388  1.00 14.23           C  
ANISOU  818  CD1 TYR B 103     2131   1904   1371     83    -42    127       C  
ATOM    819  CD2 TYR B 103      14.230  41.333  13.192  1.00 13.58           C  
ANISOU  819  CD2 TYR B 103     2001   1891   1267     76     -6    218       C  
ATOM    820  CE1 TYR B 103      15.224  43.908  13.217  1.00 14.26           C  
ANISOU  820  CE1 TYR B 103     2140   1911   1367     27    -82    137       C  
ATOM    821  CE2 TYR B 103      15.585  41.550  13.019  1.00 13.61           C  
ANISOU  821  CE2 TYR B 103     1994   1910   1266     53    -60    221       C  
ATOM    822  CZ  TYR B 103      16.074  42.847  13.026  1.00 13.96           C  
ANISOU  822  CZ  TYR B 103     2054   1932   1317     14    -91    176       C  
ATOM    823  OH  TYR B 103      17.415  43.096  12.860  1.00 14.26           O  
ANISOU  823  OH  TYR B 103     2061   2008   1348    -40   -129    154       O  
ATOM    824  N   GLY B 104       9.482  41.091  15.934  1.00 15.99           N  
ANISOU  824  N   GLY B 104     2259   2351   1466     66    286      2       N  
ATOM    825  CA  GLY B 104       8.055  40.951  16.170  1.00 17.30           C  
ANISOU  825  CA  GLY B 104     2342   2601   1630     42    383    -97       C  
ATOM    826  C   GLY B 104       7.229  40.551  14.967  1.00 16.72           C  
ANISOU  826  C   GLY B 104     2159   2553   1642     43    394   -128       C  
ATOM    827  O   GLY B 104       6.058  40.914  14.858  1.00 17.54           O  
ANISOU  827  O   GLY B 104     2145   2740   1778     73    428   -252       O  
ATOM    828  N   ALA B 105       7.828  39.766  14.072  1.00 15.87           N  
ANISOU  828  N   ALA B 105     2078   2386   1564     19    361    -31       N  
ATOM    829  CA  ALA B 105       7.127  39.304  12.875  1.00 15.75           C  
ANISOU  829  CA  ALA B 105     1969   2394   1622     15    362    -59       C  
ATOM    830  C   ALA B 105       5.836  38.597  13.240  1.00 16.88           C  
ANISOU  830  C   ALA B 105     2025   2641   1748    -77    487   -155       C  
ATOM    831  O   ALA B 105       5.799  37.800  14.181  1.00 17.49           O  
ANISOU  831  O   ALA B 105     2177   2727   1743   -191    591   -131       O  
ATOM    832  CB  ALA B 105       8.009  38.378  12.087  1.00 14.87           C  
ANISOU  832  CB  ALA B 105     1917   2210   1524    -16    331     53       C  
ATOM    833  N   LYS B 106       4.768  38.916  12.522  1.00 17.43           N  
ANISOU  833  N   LYS B 106     1943   2795   1883    -31    477   -276       N  
ATOM    834  CA  LYS B 106       3.476  38.258  12.730  1.00 18.77           C  
ANISOU  834  CA  LYS B 106     1985   3099   2049   -136    601   -405       C  
ATOM    835  C   LYS B 106       3.311  37.086  11.780  1.00 18.62           C  
ANISOU  835  C   LYS B 106     1944   3067   2062   -229    625   -378       C  
ATOM    836  O   LYS B 106       2.530  36.170  12.028  1.00 23.44           O  
ANISOU  836  O   LYS B 106     2506   3751   2649   -384    754   -446       O  
ATOM    837  CB  LYS B 106       2.336  39.243  12.532  1.00 19.86           C  
ANISOU  837  CB  LYS B 106     1938   3369   2238    -17    566   -592       C  
ATOM    838  CG  LYS B 106       2.319  40.326  13.579  1.00 26.35           C  
ANISOU  838  CG  LYS B 106     2777   4214   3022     64    563   -653       C  
ATOM    839  CD  LYS B 106       2.208  39.725  14.965  1.00 36.72           C  
ANISOU  839  CD  LYS B 106     4139   5580   4231    -99    728   -660       C  
ATOM    840  CE  LYS B 106       2.005  40.823  16.026  1.00 46.47           C  
ANISOU  840  CE  LYS B 106     5362   6871   5424    -17    736   -761       C  
ATOM    841  NZ  LYS B 106       1.444  40.277  17.301  1.00 48.49           N1+
ANISOU  841  NZ  LYS B 106     5611   7243   5570   -183    923   -833       N1+
ATOM    842  N   TYR B 107       4.058  37.122  10.691  1.00 17.41           N  
ANISOU  842  N   TYR B 107     1835   2822   1957   -149    509   -285       N  
ATOM    843  CA  TYR B 107       4.027  36.034   9.721  1.00 17.21           C  
ANISOU  843  CA  TYR B 107     1803   2772   1962   -221    518   -257       C  
ATOM    844  C   TYR B 107       5.214  36.211   8.804  1.00 17.32           C  
ANISOU  844  C   TYR B 107     1909   2672   2001   -129    398   -132       C  
ATOM    845  O   TYR B 107       5.938  37.208   8.896  1.00 15.51           O  
ANISOU  845  O   TYR B 107     1732   2393   1767    -28    317    -81       O  
ATOM    846  CB  TYR B 107       2.707  36.006   8.926  1.00 20.54           C  
ANISOU  846  CB  TYR B 107     2028   3333   2443   -219    520   -422       C  
ATOM    847  CG  TYR B 107       2.469  37.207   8.026  1.00 23.35           C  
ANISOU  847  CG  TYR B 107     2296   3722   2852    -20    369   -482       C  
ATOM    848  CD1 TYR B 107       1.860  38.354   8.514  1.00 23.89           C  
ANISOU  848  CD1 TYR B 107     2283   3869   2925    101    333   -594       C  
ATOM    849  CD2 TYR B 107       2.831  37.179   6.679  1.00 22.98           C  
ANISOU  849  CD2 TYR B 107     2271   3623   2838     53    259   -430       C  
ATOM    850  CE1 TYR B 107       1.643  39.449   7.704  1.00 26.25           C  
ANISOU  850  CE1 TYR B 107     2550   4166   3257    300    179   -642       C  
ATOM    851  CE2 TYR B 107       2.611  38.272   5.858  1.00 23.44           C  
ANISOU  851  CE2 TYR B 107     2298   3689   2918    234    115   -471       C  
ATOM    852  CZ  TYR B 107       2.018  39.406   6.380  1.00 25.73           C  
ANISOU  852  CZ  TYR B 107     2534   4033   3210    363     70   -572       C  
ATOM    853  OH  TYR B 107       1.793  40.513   5.585  1.00 26.74           O  
ANISOU  853  OH  TYR B 107     2676   4139   3345    563    -88   -609       O  
ATOM    854  N   MET B 108       5.431  35.233   7.934  1.00 17.50           N  
ANISOU  854  N   MET B 108     1952   2654   2042   -179    396    -92       N  
ATOM    855  CA  MET B 108       6.495  35.344   6.965  1.00 20.01           C  
ANISOU  855  CA  MET B 108     2333   2892   2379   -103    297      2       C  
ATOM    856  C   MET B 108       6.059  34.776   5.632  1.00 19.38           C  
ANISOU  856  C   MET B 108     2186   2839   2340   -111    270    -39       C  
ATOM    857  O   MET B 108       5.126  33.968   5.572  1.00 18.27           O  
ANISOU  857  O   MET B 108     1975   2755   2213   -206    340   -124       O  
ATOM    858  CB  MET B 108       7.757  34.638   7.445  1.00 22.93           C  
ANISOU  858  CB  MET B 108     2848   3161   2705   -136    311    121       C  
ATOM    859  CG  MET B 108       7.558  33.184   7.833  1.00 25.82           C  
ANISOU  859  CG  MET B 108     3288   3483   3038   -255    403    135       C  
ATOM    860  CE  MET B 108       9.377  32.676   5.738  1.00 71.29           C  
ANISOU  860  CE  MET B 108     9088   9153   8844   -138    259    231       C  
ATOM    861  S   MET B 108       9.284  32.300   7.652  1.00 53.95           S  
ANISOU  861  S   MET B 108     7013   6915   6571   -205    343    264       S  
ATOM    862  N   SER B 109       6.738  35.220   4.575  1.00 16.70           N  
ANISOU  862  N   SER B 109     1872   2463   2012    -25    173     11       N  
ATOM    863  CA  SER B 109       6.427  34.830   3.200  1.00 16.59           C  
ANISOU  863  CA  SER B 109     1808   2475   2021    -12    127    -24       C  
ATOM    864  C   SER B 109       7.665  34.504   2.418  1.00 14.49           C  
ANISOU  864  C   SER B 109     1631   2135   1739      0     92     71       C  
ATOM    865  O   SER B 109       8.760  34.970   2.740  1.00 14.88           O  
ANISOU  865  O   SER B 109     1758   2132   1766     26     74    152       O  
ATOM    866  CB  SER B 109       5.748  35.976   2.465  1.00 20.01           C  
ANISOU  866  CB  SER B 109     2174   2966   2461    110     26    -90       C  
ATOM    867  OG  SER B 109       4.705  36.507   3.240  1.00 28.37           O  
ANISOU  867  OG  SER B 109     3137   4107   3534    137     43   -196       O  
ATOM    868  N   LEU B 110       7.483  33.733   1.355  1.00 15.41           N  
ANISOU  868  N   LEU B 110     1722   2265   1867    -22     81     41       N  
ATOM    869  CA  LEU B 110       8.561  33.508   0.409  1.00 12.82           C  
ANISOU  869  CA  LEU B 110     1457   1896   1519      0     45    103       C  
ATOM    870  C   LEU B 110       8.002  33.126  -0.963  1.00 13.59           C  
ANISOU  870  C   LEU B 110     1506   2040   1618      8      5     41       C  
ATOM    871  O   LEU B 110       6.808  32.864  -1.120  1.00 15.43           O  
ANISOU  871  O   LEU B 110     1648   2339   1875    -12      6    -58       O  
ATOM    872  CB  LEU B 110       9.514  32.416   0.913  1.00 14.41           C  
ANISOU  872  CB  LEU B 110     1734   2026   1716    -47     99    155       C  
ATOM    873  CG  LEU B 110       8.936  31.035   1.289  1.00 19.07           C  
ANISOU  873  CG  LEU B 110     2344   2580   2322   -137    172    116       C  
ATOM    874  CD1 LEU B 110       8.551  30.228   0.061  1.00 21.68           C  
ANISOU  874  CD1 LEU B 110     2643   2925   2669   -165    163     53       C  
ATOM    875  CD2 LEU B 110       9.936  30.212   2.114  1.00 19.07           C  
ANISOU  875  CD2 LEU B 110     2468   2480   2296   -142    201    185       C  
ATOM    876  N   HIS B 111       8.883  33.096  -1.947  1.00 13.09           N  
ANISOU  876  N   HIS B 111     1493   1959   1521     32    -28     83       N  
ATOM    877  CA  HIS B 111       8.551  32.548  -3.255  1.00 13.36           C  
ANISOU  877  CA  HIS B 111     1502   2033   1542     33    -60     28       C  
ATOM    878  C   HIS B 111       9.529  31.432  -3.573  1.00 15.44           C  
ANISOU  878  C   HIS B 111     1812   2251   1803     -6    -17     48       C  
ATOM    879  O   HIS B 111      10.692  31.480  -3.158  1.00 12.68           O  
ANISOU  879  O   HIS B 111     1514   1862   1443      4      5    112       O  
ATOM    880  CB  HIS B 111       8.602  33.639  -4.335  1.00 17.56           C  
ANISOU  880  CB  HIS B 111     2070   2593   2009    110   -148     47       C  
ATOM    881  CG  HIS B 111       7.523  34.669  -4.195  1.00 17.11           C  
ANISOU  881  CG  HIS B 111     1979   2574   1949    190   -222      5       C  
ATOM    882  CD2 HIS B 111       6.252  34.697  -4.658  1.00 16.13           C  
ANISOU  882  CD2 HIS B 111     1766   2531   1831    244   -288   -103       C  
ATOM    883  ND1 HIS B 111       7.691  35.827  -3.468  1.00 22.59           N  
ANISOU  883  ND1 HIS B 111     2724   3226   2633    237   -241     54       N  
ATOM    884  CE1 HIS B 111       6.571  36.531  -3.500  1.00 23.86           C  
ANISOU  884  CE1 HIS B 111     2840   3431   2794    332   -320    -18       C  
ATOM    885  NE2 HIS B 111       5.682  35.862  -4.212  1.00 21.23           N  
ANISOU  885  NE2 HIS B 111     2410   3185   2471    343   -353   -119       N  
ATOM    886  N   VAL B 112       9.044  30.431  -4.312  1.00 16.37           N  
ANISOU  886  N   VAL B 112     1904   2384   1932    -41    -11    -26       N  
ATOM    887  CA  VAL B 112       9.849  29.299  -4.747  1.00 14.03           C  
ANISOU  887  CA  VAL B 112     1658   2040   1634    -59     18    -32       C  
ATOM    888  C   VAL B 112       9.469  28.980  -6.175  1.00 15.14           C  
ANISOU  888  C   VAL B 112     1769   2238   1744    -57    -21   -106       C  
ATOM    889  O   VAL B 112       8.294  28.987  -6.520  1.00 14.98           O  
ANISOU  889  O   VAL B 112     1682   2274   1734    -78    -50   -184       O  
ATOM    890  CB  VAL B 112       9.479  28.006  -4.027  1.00 21.14           C  
ANISOU  890  CB  VAL B 112     2593   2859   2579   -135     81    -68       C  
ATOM    891  CG1 VAL B 112      10.622  26.991  -4.158  1.00 19.50           C  
ANISOU  891  CG1 VAL B 112     2476   2569   2365   -106     97    -54       C  
ATOM    892  CG2 VAL B 112       9.155  28.259  -2.616  1.00 29.78           C  
ANISOU  892  CG2 VAL B 112     3703   3919   3693   -169    124    -29       C  
ATOM    893  N   ARG B 113      10.454  28.659  -6.995  1.00 14.38           N  
ANISOU  893  N   ARG B 113     1712   2144   1609    -31    -21   -101       N  
ATOM    894  CA  ARG B 113      10.166  28.224  -8.351  1.00 20.63           C  
ANISOU  894  CA  ARG B 113     2490   2987   2360    -32    -53   -178       C  
ATOM    895  C   ARG B 113       9.245  26.995  -8.351  1.00 22.14           C  
ANISOU  895  C   ARG B 113     2658   3148   2605   -101    -33   -279       C  
ATOM    896  O   ARG B 113       9.426  26.062  -7.564  1.00 15.92           O  
ANISOU  896  O   ARG B 113     1920   2260   1867   -145     25   -281       O  
ATOM    897  CB  ARG B 113      11.474  27.963  -9.097  1.00 26.56           C  
ANISOU  897  CB  ARG B 113     3281   3750   3058     -2    -34   -171       C  
ATOM    898  CG  ARG B 113      12.491  29.080  -8.876  1.00 30.98           C  
ANISOU  898  CG  ARG B 113     3861   4337   3572     22    -23    -83       C  
ATOM    899  CD  ARG B 113      13.793  28.819  -9.602  1.00 32.38           C  
ANISOU  899  CD  ARG B 113     4045   4562   3695     33     13   -106       C  
ATOM    900  NE  ARG B 113      13.605  29.122 -10.998  1.00 34.85           N  
ANISOU  900  NE  ARG B 113     4381   4950   3910     19     -8   -135       N  
ATOM    901  CZ  ARG B 113      14.038  30.212 -11.614  1.00 30.82           C  
ANISOU  901  CZ  ARG B 113     3920   4496   3297     -6     -4    -84       C  
ATOM    902  NH1 ARG B 113      14.757  31.133 -10.997  1.00 27.46           N1+
ANISOU  902  NH1 ARG B 113     3509   4065   2859    -33     27    -13       N1+
ATOM    903  NH2 ARG B 113      13.759  30.351 -12.880  1.00 29.60           N  
ANISOU  903  NH2 ARG B 113     3813   4396   3037    -14    -30   -111       N  
ATOM    904  N   LYS B 114       8.240  27.015  -9.224  1.00 23.69           N  
ANISOU  904  N   LYS B 114     2792   3426   2781   -115    -84   -369       N  
ATOM    905  CA  LYS B 114       7.307  25.896  -9.369  1.00 23.15           C  
ANISOU  905  CA  LYS B 114     2686   3350   2758   -208    -63   -493       C  
ATOM    906  C   LYS B 114       7.967  24.516  -9.506  1.00 24.51           C  
ANISOU  906  C   LYS B 114     2952   3411   2949   -250     -7   -525       C  
ATOM    907  O   LYS B 114       7.438  23.507  -9.037  1.00 31.13           O  
ANISOU  907  O   LYS B 114     3821   4167   3839   -355     47   -586       O  
ATOM    908  CB  LYS B 114       6.410  26.132 -10.581  1.00 32.49           C  
ANISOU  908  CB  LYS B 114     3786   4664   3894   -189   -150   -600       C  
ATOM    909  CG  LYS B 114       4.942  26.187 -10.257  1.00 37.27           C  
ANISOU  909  CG  LYS B 114     4260   5354   4545   -247   -170   -714       C  
ATOM    910  CD  LYS B 114       4.186  25.214 -11.147  1.00 49.26           C  
ANISOU  910  CD  LYS B 114     5719   6932   6067   -326   -188   -880       C  
ATOM    911  CE  LYS B 114       3.281  25.950 -12.106  1.00 54.52           C  
ANISOU  911  CE  LYS B 114     6270   7771   6673   -238   -322   -978       C  
ATOM    912  NZ  LYS B 114       4.063  26.959 -12.867  1.00 56.30           N1+
ANISOU  912  NZ  LYS B 114     6591   8008   6791    -85   -407   -862       N1+
ATOM    913  N   SER B 115       9.127  24.467 -10.137  1.00 22.08           N  
ANISOU  913  N   SER B 115     2699   3096   2594   -171    -17   -492       N  
ATOM    914  CA  SER B 115       9.760  23.186 -10.416  1.00 25.06           C  
ANISOU  914  CA  SER B 115     3161   3379   2983   -173     16   -547       C  
ATOM    915  C   SER B 115      10.641  22.669  -9.281  1.00 24.30           C  
ANISOU  915  C   SER B 115     3165   3142   2926   -140     61   -478       C  
ATOM    916  O   SER B 115      11.173  21.563  -9.358  1.00 21.90           O  
ANISOU  916  O   SER B 115     2958   2731   2634   -115     76   -524       O  
ATOM    917  CB  SER B 115      10.568  23.301 -11.701  1.00 24.75           C  
ANISOU  917  CB  SER B 115     3116   3424   2866    -98    -12   -578       C  
ATOM    918  OG  SER B 115      11.584  24.268 -11.527  1.00 25.27           O  
ANISOU  918  OG  SER B 115     3173   3539   2890    -28     -8   -481       O  
ATOM    919  N   ASN B 116      10.784  23.458  -8.219  1.00 20.69           N  
ANISOU  919  N   ASN B 116     2697   2680   2483   -125     71   -376       N  
ATOM    920  CA  ASN B 116      11.732  23.137  -7.154  1.00 21.08           C  
ANISOU  920  CA  ASN B 116     2838   2621   2549    -65     91   -307       C  
ATOM    921  C   ASN B 116      11.128  22.199  -6.121  1.00 22.38           C  
ANISOU  921  C   ASN B 116     3125   2627   2751   -149    136   -303       C  
ATOM    922  O   ASN B 116      10.754  22.618  -5.035  1.00 21.27           O  
ANISOU  922  O   ASN B 116     2997   2464   2622   -194    163   -237       O  
ATOM    923  CB  ASN B 116      12.198  24.422  -6.457  1.00 22.57           C  
ANISOU  923  CB  ASN B 116     2972   2879   2725    -20     81   -206       C  
ATOM    924  CG  ASN B 116      13.422  24.204  -5.585  1.00 20.08           C  
ANISOU  924  CG  ASN B 116     2720   2499   2410     74     77   -156       C  
ATOM    925  ND2 ASN B 116      14.104  25.289  -5.257  1.00 18.16           N  
ANISOU  925  ND2 ASN B 116     2414   2339   2147    116     65    -96       N  
ATOM    926  OD1 ASN B 116      13.752  23.073  -5.209  1.00 18.73           O  
ANISOU  926  OD1 ASN B 116     2665   2201   2251    112     78   -178       O  
ATOM    927  N   ARG B 117      11.055  20.923  -6.455  1.00 23.93           N  
ANISOU  927  N   ARG B 117     3432   2703   2956   -178    150   -377       N  
ATOM    928  CA  ARG B 117      10.334  19.946  -5.642  1.00 21.06           C  
ANISOU  928  CA  ARG B 117     3222   2169   2612   -304    208   -385       C  
ATOM    929  C   ARG B 117      10.873  19.805  -4.228  1.00 20.14           C  
ANISOU  929  C   ARG B 117     3256   1916   2479   -261    221   -277       C  
ATOM    930  O   ARG B 117      10.100  19.655  -3.280  1.00 25.96           O  
ANISOU  930  O   ARG B 117     4072   2580   3213   -394    286   -244       O  
ATOM    931  CB  ARG B 117      10.339  18.591  -6.358  1.00 25.83           C  
ANISOU  931  CB  ARG B 117     3953   2642   3219   -329    211   -487       C  
ATOM    932  CG  ARG B 117       9.732  17.437  -5.581  1.00 39.58           C  
ANISOU  932  CG  ARG B 117     5914   4161   4963   -474    279   -496       C  
ATOM    933  CD  ARG B 117       9.696  16.163  -6.436  1.00 50.40           C  
ANISOU  933  CD  ARG B 117     7414   5400   6338   -505    277   -614       C  
ATOM    934  NE  ARG B 117       8.645  15.250  -6.000  1.00 60.51           N  
ANISOU  934  NE  ARG B 117     8851   6519   7622   -741    367   -661       N  
ATOM    935  CZ  ARG B 117       8.796  14.357  -5.027  1.00 67.49           C  
ANISOU  935  CZ  ARG B 117    10028   7143   8474   -785    407   -601       C  
ATOM    936  NH1 ARG B 117       9.956  14.264  -4.389  1.00 69.46           N1+
ANISOU  936  NH1 ARG B 117    10428   7275   8689   -574    342   -497       N1+
ATOM    937  NH2 ARG B 117       7.789  13.559  -4.688  1.00 70.08           N  
ANISOU  937  NH2 ARG B 117    10505   7329   8794  -1043    511   -651       N  
ATOM    938  N   ALA B 118      12.192  19.858  -4.079  1.00 19.85           N  
ANISOU  938  N   ALA B 118     3255   1864   2423    -77    160   -234       N  
ATOM    939  CA  ALA B 118      12.811  19.725  -2.762  1.00 20.10           C  
ANISOU  939  CA  ALA B 118     3433   1778   2425      0    144   -140       C  
ATOM    940  C   ALA B 118      12.448  20.886  -1.842  1.00 19.90           C  
ANISOU  940  C   ALA B 118     3317   1850   2396    -54    171    -54       C  
ATOM    941  O   ALA B 118      12.111  20.690  -0.663  1.00 19.50           O  
ANISOU  941  O   ALA B 118     3401   1692   2315   -118    209     12       O  
ATOM    942  CB  ALA B 118      14.322  19.606  -2.893  1.00 20.21           C  
ANISOU  942  CB  ALA B 118     3453   1804   2423    227     57   -150       C  
ATOM    943  N   ALA B 119      12.512  22.100  -2.376  1.00 18.20           N  
ANISOU  943  N   ALA B 119     2893   1828   2197    -33    153    -56       N  
ATOM    944  CA  ALA B 119      12.252  23.265  -1.552  1.00 17.82           C  
ANISOU  944  CA  ALA B 119     2762   1864   2144    -62    167     14       C  
ATOM    945  C   ALA B 119      10.768  23.335  -1.219  1.00 18.54           C  
ANISOU  945  C   ALA B 119     2834   1962   2250   -236    241     -6       C  
ATOM    946  O   ALA B 119      10.406  23.725  -0.118  1.00 16.94           O  
ANISOU  946  O   ALA B 119     2656   1747   2031   -287    280     46       O  
ATOM    947  CB  ALA B 119      12.719  24.539  -2.237  1.00 15.82           C  
ANISOU  947  CB  ALA B 119     2332   1785   1893      1    127     17       C  
ATOM    948  N   ILE B 120       9.915  22.945  -2.160  1.00 18.42           N  
ANISOU  948  N   ILE B 120     2761   1978   2260   -329    263    -98       N  
ATOM    949  CA  ILE B 120       8.484  22.922  -1.891  1.00 18.12           C  
ANISOU  949  CA  ILE B 120     2672   1974   2240   -503    336   -157       C  
ATOM    950  C   ILE B 120       8.170  21.964  -0.741  1.00 23.62           C  
ANISOU  950  C   ILE B 120     3566   2501   2908   -630    425   -129       C  
ATOM    951  O   ILE B 120       7.401  22.290   0.181  1.00 21.70           O  
ANISOU  951  O   ILE B 120     3306   2287   2653   -745    498   -121       O  
ATOM    952  CB  ILE B 120       7.668  22.483  -3.125  1.00 23.80           C  
ANISOU  952  CB  ILE B 120     3300   2757   2986   -584    335   -287       C  
ATOM    953  CG1 ILE B 120       7.931  23.409  -4.313  1.00 28.75           C  
ANISOU  953  CG1 ILE B 120     3770   3541   3612   -464    245   -309       C  
ATOM    954  CG2 ILE B 120       6.173  22.443  -2.796  1.00 22.27           C  
ANISOU  954  CG2 ILE B 120     3018   2630   2812   -774    414   -381       C  
ATOM    955  CD1 ILE B 120       7.673  24.845  -4.016  1.00 33.51           C  
ANISOU  955  CD1 ILE B 120     4245   4275   4212   -412    214   -268       C  
ATOM    956  N   HIS B 121       8.759  20.774  -0.785  1.00 22.04           N  
ANISOU  956  N   HIS B 121     3572   2116   2686   -609    420   -117       N  
ATOM    957  CA  HIS B 121       8.537  19.836   0.308  1.00 21.87           C  
ANISOU  957  CA  HIS B 121     3804   1894   2612   -726    498    -72       C  
ATOM    958  C   HIS B 121       9.038  20.418   1.636  1.00 21.41           C  
ANISOU  958  C   HIS B 121     3819   1816   2500   -655    492     49       C  
ATOM    959  O   HIS B 121       8.350  20.327   2.657  1.00 22.64           O  
ANISOU  959  O   HIS B 121     4068   1926   2609   -807    588     76       O  
ATOM    960  CB  HIS B 121       9.184  18.481   0.019  1.00 41.88           C  
ANISOU  960  CB  HIS B 121     6588   4203   5122   -673    468    -76       C  
ATOM    961  CG  HIS B 121       8.433  17.652  -0.981  1.00 51.22           C  
ANISOU  961  CG  HIS B 121     7769   5352   6340   -819    511   -203       C  
ATOM    962  CD2 HIS B 121       8.067  16.346  -0.963  1.00 55.62           C  
ANISOU  962  CD2 HIS B 121     8567   5693   6872   -961    571   -245       C  
ATOM    963  ND1 HIS B 121       7.960  18.162  -2.174  1.00 51.87           N  
ANISOU  963  ND1 HIS B 121     7593   5633   6480   -833    487   -309       N  
ATOM    964  CE1 HIS B 121       7.347  17.205  -2.848  1.00 51.62           C  
ANISOU  964  CE1 HIS B 121     7620   5528   6464   -973    528   -421       C  
ATOM    965  NE2 HIS B 121       7.399  16.093  -2.138  1.00 50.66           N  
ANISOU  965  NE2 HIS B 121     7801   5151   6298  -1063    586   -387       N  
ATOM    966  N   LEU B 122      10.220  21.029   1.617  1.00 20.24           N  
ANISOU  966  N   LEU B 122     3619   1718   2351   -438    387    106       N  
ATOM    967  CA  LEU B 122      10.804  21.617   2.822  1.00 23.35           C  
ANISOU  967  CA  LEU B 122     4069   2110   2694   -354    362    206       C  
ATOM    968  C   LEU B 122       9.857  22.655   3.416  1.00 19.23           C  
ANISOU  968  C   LEU B 122     3402   1728   2178   -475    435    206       C  
ATOM    969  O   LEU B 122       9.543  22.609   4.601  1.00 19.93           O  
ANISOU  969  O   LEU B 122     3612   1757   2202   -556    498    258       O  
ATOM    970  CB  LEU B 122      12.161  22.272   2.523  1.00 18.71           C  
ANISOU  970  CB  LEU B 122     3378   1611   2119   -128    243    228       C  
ATOM    971  CG  LEU B 122      12.694  23.212   3.607  1.00 23.06           C  
ANISOU  971  CG  LEU B 122     3904   2225   2632    -52    210    303       C  
ATOM    972  CD1 LEU B 122      12.953  22.466   4.929  1.00 20.42           C  
ANISOU  972  CD1 LEU B 122     3842   1715   2203    -30    207    381       C  
ATOM    973  CD2 LEU B 122      13.956  23.917   3.142  1.00 22.04           C  
ANISOU  973  CD2 LEU B 122     3632   2218   2527    125    111    291       C  
ATOM    974  N   TYR B 123       9.395  23.589   2.597  1.00 20.02           N  
ANISOU  974  N   TYR B 123     3256   2009   2342   -480    423    142       N  
ATOM    975  CA  TYR B 123       8.512  24.632   3.111  1.00 23.16           C  
ANISOU  975  CA  TYR B 123     3506   2545   2749   -556    472    122       C  
ATOM    976  C   TYR B 123       7.125  24.093   3.457  1.00 25.29           C  
ANISOU  976  C   TYR B 123     3785   2813   3011   -780    601     45       C  
ATOM    977  O   TYR B 123       6.639  24.287   4.578  1.00 26.79           O  
ANISOU  977  O   TYR B 123     4015   3008   3154   -875    683     62       O  
ATOM    978  CB  TYR B 123       8.388  25.770   2.112  1.00 21.13           C  
ANISOU  978  CB  TYR B 123     3019   2461   2550   -477    406     72       C  
ATOM    979  CG  TYR B 123       9.704  26.359   1.699  1.00 22.57           C  
ANISOU  979  CG  TYR B 123     3181   2663   2732   -304    306    132       C  
ATOM    980  CD1 TYR B 123      10.757  26.502   2.601  1.00 24.00           C  
ANISOU  980  CD1 TYR B 123     3456   2789   2872   -213    274    215       C  
ATOM    981  CD2 TYR B 123       9.902  26.767   0.394  1.00 22.99           C  
ANISOU  981  CD2 TYR B 123     3120   2803   2814   -242    247     92       C  
ATOM    982  CE1 TYR B 123      11.972  27.060   2.191  1.00 23.49           C  
ANISOU  982  CE1 TYR B 123     3342   2774   2810    -78    194    240       C  
ATOM    983  CE2 TYR B 123      11.086  27.303  -0.014  1.00 25.01           C  
ANISOU  983  CE2 TYR B 123     3353   3091   3059   -123    181    131       C  
ATOM    984  CZ  TYR B 123      12.114  27.453   0.872  1.00 26.51           C  
ANISOU  984  CZ  TYR B 123     3608   3243   3221    -48    159    197       C  
ATOM    985  OH  TYR B 123      13.267  28.001   0.381  1.00 29.50           O  
ANISOU  985  OH  TYR B 123     3932   3684   3591     45    106    206       O  
ATOM    986  N   ARG B 124       6.489  23.422   2.494  1.00 24.24           N  
ANISOU  986  N   ARG B 124     3606   2687   2919   -877    625    -55       N  
ATOM    987  CA  ARG B 124       5.113  22.960   2.686  1.00 26.22           C  
ANISOU  987  CA  ARG B 124     3815   2977   3171  -1115    753   -168       C  
ATOM    988  C   ARG B 124       4.982  21.852   3.719  1.00 30.75           C  
ANISOU  988  C   ARG B 124     4663   3357   3663  -1291    874   -121       C  
ATOM    989  O   ARG B 124       4.127  21.918   4.590  1.00 30.45           O  
ANISOU  989  O   ARG B 124     4621   3364   3586  -1469   1000   -158       O  
ATOM    990  CB  ARG B 124       4.471  22.504   1.377  1.00 24.92           C  
ANISOU  990  CB  ARG B 124     3526   2877   3064  -1182    741   -304       C  
ATOM    991  CG  ARG B 124       3.078  21.907   1.566  1.00 27.91           C  
ANISOU  991  CG  ARG B 124     3852   3306   3445  -1457    882   -449       C  
ATOM    992  CD  ARG B 124       2.544  21.297   0.277  1.00 38.70           C  
ANISOU  992  CD  ARG B 124     5122   4720   4863  -1529    862   -592       C  
ATOM    993  NE  ARG B 124       3.415  20.238  -0.229  1.00 45.12           N  
ANISOU  993  NE  ARG B 124     6165   5318   5662  -1489    825   -533       N  
ATOM    994  CZ  ARG B 124       3.403  19.805  -1.487  1.00 52.45           C  
ANISOU  994  CZ  ARG B 124     7038   6263   6627  -1465    764   -622       C  
ATOM    995  NH1 ARG B 124       2.563  20.343  -2.362  1.00 56.05           N1+
ANISOU  995  NH1 ARG B 124     7226   6941   7129  -1476    723   -766       N1+
ATOM    996  NH2 ARG B 124       4.233  18.846  -1.877  1.00 52.39           N  
ANISOU  996  NH2 ARG B 124     7247   6056   6604  -1413    732   -577       N  
ATOM    997  N   ASP B 125       5.812  20.824   3.612  1.00 34.34           N  
ANISOU  997  N   ASP B 125     5372   3594   4083  -1243    840    -49       N  
ATOM    998  CA  ASP B 125       5.649  19.659   4.474  1.00 34.92           C  
ANISOU  998  CA  ASP B 125     5766   3440   4062  -1416    947     -3       C  
ATOM    999  C   ASP B 125       6.367  19.753   5.815  1.00 36.92           C  
ANISOU  999  C   ASP B 125     6246   3573   4209  -1335    938    147       C  
ATOM   1000  O   ASP B 125       5.736  19.590   6.863  1.00 37.49           O  
ANISOU 1000  O   ASP B 125     6382   3660   4203  -1456   1025    143       O  
ATOM   1001  CB  ASP B 125       6.043  18.368   3.742  1.00 39.60           C  
ANISOU 1001  CB  ASP B 125     6570   3820   4655  -1416    916    -15       C  
ATOM   1002  CG  ASP B 125       5.309  18.201   2.419  1.00 47.15           C  
ANISOU 1002  CG  ASP B 125     7317   4895   5704  -1509    925   -174       C  
ATOM   1003  OD1 ASP B 125       4.217  18.791   2.268  1.00 47.82           O  
ANISOU 1003  OD1 ASP B 125     7147   5192   5832  -1651    994   -289       O  
ATOM   1004  OD2 ASP B 125       5.824  17.484   1.530  1.00 52.48           O1-
ANISOU 1004  OD2 ASP B 125     8076   5461   6404  -1427    855   -198       O1-
ATOM   1005  N   THR B 126       7.672  19.999   5.818  1.00 33.09           N  
ANISOU 1005  N   THR B 126     5813   3042   3718  -1065    789    242       N  
ATOM   1006  CA  THR B 126       8.370  19.944   7.105  1.00 35.04           C  
ANISOU 1006  CA  THR B 126     6296   3169   3851   -977    761    370       C  
ATOM   1007  C   THR B 126       8.264  21.227   7.935  1.00 28.36           C  
ANISOU 1007  C   THR B 126     5290   2498   2988   -954    775    398       C  
ATOM   1008  O   THR B 126       8.262  21.159   9.156  1.00 30.62           O  
ANISOU 1008  O   THR B 126     5699   2756   3180   -962    792    444       O  
ATOM   1009  CB  THR B 126       9.834  19.409   6.989  1.00 38.61           C  
ANISOU 1009  CB  THR B 126     6936   3460   4273   -708    599    447       C  
ATOM   1010  CG2 THR B 126      10.076  18.834   5.628  1.00 25.13           C  
ANISOU 1010  CG2 THR B 126     5172   1724   2653   -645    542    368       C  
ATOM   1011  OG1 THR B 126      10.782  20.447   7.247  1.00 40.94           O  
ANISOU 1011  OG1 THR B 126     7082   3892   4582   -488    482    489       O  
ATOM   1012  N   LEU B 127       8.135  22.385   7.289  1.00 25.41           N  
ANISOU 1012  N   LEU B 127     4587   2349   2717   -882    733    333       N  
ATOM   1013  CA  LEU B 127       8.036  23.639   8.036  1.00 22.77           C  
ANISOU 1013  CA  LEU B 127     4107   2172   2375   -846    736    346       C  
ATOM   1014  C   LEU B 127       6.602  24.161   8.073  1.00 24.15           C  
ANISOU 1014  C   LEU B 127     4081   2512   2583  -1038    864    232       C  
ATOM   1015  O   LEU B 127       6.341  25.233   8.617  1.00 24.76           O  
ANISOU 1015  O   LEU B 127     4016   2730   2661  -1014    874    215       O  
ATOM   1016  CB  LEU B 127       8.969  24.717   7.464  1.00 19.41           C  
ANISOU 1016  CB  LEU B 127     3487   1867   2020   -621    593    357       C  
ATOM   1017  CG  LEU B 127      10.466  24.383   7.493  1.00 23.67           C  
ANISOU 1017  CG  LEU B 127     4161   2304   2530   -414    461    437       C  
ATOM   1018  CD1 LEU B 127      11.294  25.421   6.777  1.00 21.18           C  
ANISOU 1018  CD1 LEU B 127     3632   2130   2287   -250    353    419       C  
ATOM   1019  CD2 LEU B 127      10.948  24.216   8.921  1.00 27.13           C  
ANISOU 1019  CD2 LEU B 127     4818   2643   2845   -375    452    529       C  
ATOM   1020  N   GLN B 128       5.692  23.421   7.450  1.00 26.48           N  
ANISOU 1020  N   GLN B 128     4349   2801   2910  -1217    951    136       N  
ATOM   1021  CA  GLN B 128       4.251  23.696   7.508  1.00 29.97           C  
ANISOU 1021  CA  GLN B 128     4598   3412   3377  -1424   1084     -9       C  
ATOM   1022  C   GLN B 128       3.821  25.068   6.953  1.00 31.69           C  
ANISOU 1022  C   GLN B 128     4475   3876   3691  -1307   1016   -106       C  
ATOM   1023  O   GLN B 128       2.913  25.697   7.480  1.00 27.80           O  
ANISOU 1023  O   GLN B 128     3828   3540   3195  -1390   1095   -201       O  
ATOM   1024  CB  GLN B 128       3.707  23.482   8.932  1.00 33.27           C  
ANISOU 1024  CB  GLN B 128     5138   3814   3689  -1553   1193     -6       C  
ATOM   1025  CG  GLN B 128       3.752  22.033   9.403  1.00 41.08           C  
ANISOU 1025  CG  GLN B 128     6430   4594   4587  -1651   1231     35       C  
ATOM   1026  CD  GLN B 128       3.585  21.888  10.920  1.00 53.75           C  
ANISOU 1026  CD  GLN B 128     8203   6156   6065  -1709   1292     74       C  
ATOM   1027  NE2 GLN B 128       3.212  22.978  11.589  1.00 58.20           N  
ANISOU 1027  NE2 GLN B 128     8600   6887   6627  -1701   1323     40       N  
ATOM   1028  OE1 GLN B 128       3.793  20.810  11.477  1.00 53.88           O  
ANISOU 1028  OE1 GLN B 128     8502   5988   5981  -1758   1308    129       O  
ATOM   1029  N   PHE B 129       4.443  25.506   5.863  1.00 31.69           N  
ANISOU 1029  N   PHE B 129     4371   3906   3766  -1116    870    -93       N  
ATOM   1030  CA  PHE B 129       3.972  26.692   5.154  1.00 25.93           C  
ANISOU 1030  CA  PHE B 129     3365   3374   3112  -1010    794   -186       C  
ATOM   1031  C   PHE B 129       2.702  26.365   4.392  1.00 26.66           C  
ANISOU 1031  C   PHE B 129     3277   3596   3256  -1145    845   -363       C  
ATOM   1032  O   PHE B 129       2.500  25.234   3.934  1.00 27.45           O  
ANISOU 1032  O   PHE B 129     3456   3616   3357  -1280    896   -400       O  
ATOM   1033  CB  PHE B 129       5.001  27.169   4.137  1.00 21.63           C  
ANISOU 1033  CB  PHE B 129     2796   2812   2608   -800    639   -120       C  
ATOM   1034  CG  PHE B 129       6.107  27.999   4.710  1.00 25.58           C  
ANISOU 1034  CG  PHE B 129     3359   3277   3081   -643    565      0       C  
ATOM   1035  CD1 PHE B 129       6.979  27.478   5.643  1.00 27.23           C  
ANISOU 1035  CD1 PHE B 129     3774   3348   3225   -634    581    111       C  
ATOM   1036  CD2 PHE B 129       6.298  29.297   4.278  1.00 24.14           C  
ANISOU 1036  CD2 PHE B 129     3045   3196   2933   -501    471     -3       C  
ATOM   1037  CE1 PHE B 129       8.015  28.248   6.136  1.00 28.99           C  
ANISOU 1037  CE1 PHE B 129     4028   3562   3423   -492    505    197       C  
ATOM   1038  CE2 PHE B 129       7.322  30.070   4.771  1.00 22.19           C  
ANISOU 1038  CE2 PHE B 129     2851   2920   2662   -385    411     91       C  
ATOM   1039  CZ  PHE B 129       8.186  29.546   5.688  1.00 25.71           C  
ANISOU 1039  CZ  PHE B 129     3461   3255   3051   -382    428    182       C  
ATOM   1040  N   ASP B 130       1.857  27.375   4.245  1.00 21.23           N  
ANISOU 1040  N   ASP B 130     2348   3110   2609  -1096    819   -485       N  
ATOM   1041  CA  ASP B 130       0.696  27.307   3.379  1.00 31.52           C  
ANISOU 1041  CA  ASP B 130     3425   4582   3967  -1160    818   -677       C  
ATOM   1042  C   ASP B 130       1.072  27.836   2.004  1.00 30.72           C  
ANISOU 1042  C   ASP B 130     3244   4516   3912   -957    644   -672       C  
ATOM   1043  O   ASP B 130       2.019  28.605   1.860  1.00 29.31           O  
ANISOU 1043  O   ASP B 130     3131   4280   3726   -772    538   -546       O  
ATOM   1044  CB  ASP B 130      -0.408  28.169   3.958  1.00 41.35           C  
ANISOU 1044  CB  ASP B 130     4447   6041   5225  -1174    861   -831       C  
ATOM   1045  CG  ASP B 130      -0.488  28.046   5.454  1.00 60.16           C  
ANISOU 1045  CG  ASP B 130     6933   8388   7538  -1316   1015   -794       C  
ATOM   1046  OD1 ASP B 130      -0.483  26.897   5.943  1.00 66.98           O  
ANISOU 1046  OD1 ASP B 130     7974   9129   8347  -1533   1151   -759       O  
ATOM   1047  OD2 ASP B 130      -0.516  29.091   6.143  1.00 66.32           O1-
ANISOU 1047  OD2 ASP B 130     7649   9244   8307  -1205    994   -793       O1-
ATOM   1048  N   VAL B 131       0.332  27.416   0.989  1.00 28.98           N  
ANISOU 1048  N   VAL B 131     2889   4393   3727  -1007    618   -816       N  
ATOM   1049  CA  VAL B 131       0.552  27.908  -0.360  1.00 25.41           C  
ANISOU 1049  CA  VAL B 131     2367   3991   3297   -824    455   -826       C  
ATOM   1050  C   VAL B 131      -0.583  28.881  -0.672  1.00 30.06           C  
ANISOU 1050  C   VAL B 131     2701   4809   3912   -726    375  -1000       C  
ATOM   1051  O   VAL B 131      -1.739  28.483  -0.772  1.00 28.97           O  
ANISOU 1051  O   VAL B 131     2381   4826   3799   -850    425  -1198       O  
ATOM   1052  CB  VAL B 131       0.535  26.756  -1.358  1.00 27.80           C  
ANISOU 1052  CB  VAL B 131     2705   4247   3609   -922    457   -878       C  
ATOM   1053  CG1 VAL B 131       1.026  27.217  -2.723  1.00 23.35           C  
ANISOU 1053  CG1 VAL B 131     2128   3705   3040   -731    295   -850       C  
ATOM   1054  CG2 VAL B 131       1.391  25.614  -0.843  1.00 30.78           C  
ANISOU 1054  CG2 VAL B 131     3335   4400   3961  -1043    557   -751       C  
ATOM   1055  N   GLN B 132      -0.259  30.156  -0.804  1.00 21.41           N  
ANISOU 1055  N   GLN B 132     1596   3733   2805   -504    248   -938       N  
ATOM   1056  CA  GLN B 132      -1.269  31.172  -1.061  1.00 28.74           C  
ANISOU 1056  CA  GLN B 132     2318   4855   3749   -358    144  -1096       C  
ATOM   1057  C   GLN B 132      -1.754  31.101  -2.509  1.00 25.14           C  
ANISOU 1057  C   GLN B 132     1759   4502   3292   -270      6  -1209       C  
ATOM   1058  O   GLN B 132      -2.940  31.291  -2.799  1.00 26.71           O  
ANISOU 1058  O   GLN B 132     1731   4905   3512   -235    -47  -1424       O  
ATOM   1059  CB  GLN B 132      -0.681  32.553  -0.758  1.00 39.05           C  
ANISOU 1059  CB  GLN B 132     3706   6102   5029   -147     45   -978       C  
ATOM   1060  CG  GLN B 132      -1.694  33.666  -0.557  1.00 53.97           C  
ANISOU 1060  CG  GLN B 132     5417   8157   6930     13    -41  -1135       C  
ATOM   1061  CD  GLN B 132      -1.076  35.053  -0.712  1.00 61.86           C  
ANISOU 1061  CD  GLN B 132     6547   9064   7894    250   -185  -1016       C  
ATOM   1062  NE2 GLN B 132      -1.848  36.088  -0.375  1.00 64.70           N  
ANISOU 1062  NE2 GLN B 132     6794   9531   8260    413   -264  -1139       N  
ATOM   1063  OE1 GLN B 132       0.084  35.191  -1.119  1.00 60.01           O  
ANISOU 1063  OE1 GLN B 132     6514   8664   7624    280   -221   -828       O  
ATOM   1064  N   GLY B 133      -0.828  30.818  -3.421  1.00 22.15           N  
ANISOU 1064  N   GLY B 133     1538   3995   2882   -229    -54  -1078       N  
ATOM   1065  CA  GLY B 133      -1.148  30.771  -4.832  1.00 22.84           C  
ANISOU 1065  CA  GLY B 133     1569   4165   2946   -137   -190  -1162       C  
ATOM   1066  C   GLY B 133       0.094  30.847  -5.707  1.00 24.38           C  
ANISOU 1066  C   GLY B 133     1972   4210   3083    -52   -258   -981       C  
ATOM   1067  O   GLY B 133       1.234  30.732  -5.235  1.00 20.38           O  
ANISOU 1067  O   GLY B 133     1635   3541   2568    -89   -186   -807       O  
ATOM   1068  N   ILE B 134      -0.146  31.010  -7.003  1.00 27.84           N  
ANISOU 1068  N   ILE B 134     2388   4719   3473     58   -396  -1040       N  
ATOM   1069  CA  ILE B 134       0.902  31.068  -8.014  1.00 28.83           C  
ANISOU 1069  CA  ILE B 134     2692   4738   3523    126   -457   -903       C  
ATOM   1070  C   ILE B 134       1.117  32.507  -8.431  1.00 28.33           C  
ANISOU 1070  C   ILE B 134     2723   4661   3379    339   -602   -820       C  
ATOM   1071  O   ILE B 134       0.149  33.220  -8.677  1.00 31.13           O  
ANISOU 1071  O   ILE B 134     2978   5134   3715    483   -732   -936       O  
ATOM   1072  CB  ILE B 134       0.481  30.308  -9.271  1.00 33.81           C  
ANISOU 1072  CB  ILE B 134     3267   5455   4123    103   -519  -1025       C  
ATOM   1073  CG1 ILE B 134       0.466  28.806  -9.018  1.00 41.55           C  
ANISOU 1073  CG1 ILE B 134     4220   6399   5169   -122   -373  -1087       C  
ATOM   1074  CG2 ILE B 134       1.448  30.601 -10.401  1.00 34.52           C  
ANISOU 1074  CG2 ILE B 134     3536   5470   4110    200   -597   -900       C  
ATOM   1075  CD1 ILE B 134       1.755  28.130  -9.421  1.00 47.17           C  
ANISOU 1075  CD1 ILE B 134     5120   6952   5851   -167   -317   -951       C  
ATOM   1076  N   GLU B 135       2.376  32.938  -8.508  1.00 22.91           N  
ANISOU 1076  N   GLU B 135     2233   3830   2640    360   -584   -633       N  
ATOM   1077  CA  GLU B 135       2.683  34.238  -9.096  1.00 25.71           C  
ANISOU 1077  CA  GLU B 135     2734   4142   2894    528   -712   -543       C  
ATOM   1078  C   GLU B 135       3.245  34.015 -10.506  1.00 24.06           C  
ANISOU 1078  C   GLU B 135     2648   3917   2576    541   -764   -498       C  
ATOM   1079  O   GLU B 135       4.296  33.399 -10.686  1.00 26.11           O  
ANISOU 1079  O   GLU B 135     2988   4105   2826    431   -665   -413       O  
ATOM   1080  CB  GLU B 135       3.651  35.029  -8.209  1.00 29.42           C  
ANISOU 1080  CB  GLU B 135     3337   4476   3365    522   -650   -384       C  
ATOM   1081  CG  GLU B 135       3.898  36.464  -8.678  1.00 37.10           C  
ANISOU 1081  CG  GLU B 135     4490   5376   4230    672   -771   -293       C  
ATOM   1082  CD  GLU B 135       2.738  37.409  -8.372  1.00 39.82           C  
ANISOU 1082  CD  GLU B 135     4773   5777   4580    850   -902   -393       C  
ATOM   1083  OE1 GLU B 135       2.124  37.266  -7.290  1.00 38.59           O  
ANISOU 1083  OE1 GLU B 135     4454   5683   4525    829   -848   -483       O  
ATOM   1084  OE2 GLU B 135       2.434  38.287  -9.219  1.00 38.03           O1-
ANISOU 1084  OE2 GLU B 135     4671   5533   4247   1019  -1062   -388       O1-
ATOM   1085  N   SER B 136       2.499  34.454 -11.510  1.00 23.90           N  
ANISOU 1085  N   SER B 136     2633   3980   2470    682   -925   -576       N  
ATOM   1086  CA  SER B 136       2.883  34.259 -12.902  1.00 24.26           C  
ANISOU 1086  CA  SER B 136     2799   4030   2390    700   -985   -551       C  
ATOM   1087  C   SER B 136       4.179  34.988 -13.233  1.00 24.59           C  
ANISOU 1087  C   SER B 136     3091   3932   2321    690   -952   -357       C  
ATOM   1088  O   SER B 136       4.365  36.128 -12.816  1.00 21.67           O  
ANISOU 1088  O   SER B 136     2843   3475   1916    764   -988   -264       O  
ATOM   1089  CB  SER B 136       1.775  34.760 -13.819  1.00 28.28           C  
ANISOU 1089  CB  SER B 136     3286   4653   2807    887  -1191   -669       C  
ATOM   1090  OG  SER B 136       2.168  34.678 -15.176  1.00 32.04           O  
ANISOU 1090  OG  SER B 136     3915   5127   3133    912  -1256   -632       O  
ATOM   1091  N   LYS B 137       5.075  34.317 -13.954  1.00 21.69           N  
ANISOU 1091  N   LYS B 137     2795   3549   1899    586   -873   -313       N  
ATOM   1092  CA  LYS B 137       6.308  34.938 -14.452  1.00 27.79           C  
ANISOU 1092  CA  LYS B 137     3786   4226   2545    547   -827   -160       C  
ATOM   1093  C   LYS B 137       7.083  35.764 -13.418  1.00 28.44           C  
ANISOU 1093  C   LYS B 137     3948   4195   2665    506   -749    -35       C  
ATOM   1094  O   LYS B 137       7.578  36.850 -13.725  1.00 26.83           O  
ANISOU 1094  O   LYS B 137     3947   3906   2341    527   -776     75       O  
ATOM   1095  CB  LYS B 137       5.991  35.818 -15.666  1.00 33.49           C  
ANISOU 1095  CB  LYS B 137     4702   4948   3074    672   -980   -132       C  
ATOM   1096  CG  LYS B 137       4.955  35.220 -16.606  1.00 39.54           C  
ANISOU 1096  CG  LYS B 137     5380   5847   3798    761  -1108   -280       C  
ATOM   1097  CD  LYS B 137       5.605  34.410 -17.712  1.00 47.26           C  
ANISOU 1097  CD  LYS B 137     6411   6867   4680    666  -1050   -289       C  
ATOM   1098  CE  LYS B 137       5.239  34.958 -19.076  1.00 48.43           C  
ANISOU 1098  CE  LYS B 137     6733   7036   4631    774  -1192   -284       C  
ATOM   1099  NZ  LYS B 137       3.767  35.126 -19.201  1.00 53.70           N1+
ANISOU 1099  NZ  LYS B 137     7273   7761   5369    918  -1336   -405       N1+
ATOM   1100  N   TYR B 138       7.179  35.240 -12.202  1.00 22.85           N  
ANISOU 1100  N   TYR B 138     3094   3479   2111    438   -652    -54       N  
ATOM   1101  CA  TYR B 138       7.841  35.925 -11.100  1.00 20.61           C  
ANISOU 1101  CA  TYR B 138     2854   3103   1873    401   -583     41       C  
ATOM   1102  C   TYR B 138       9.358  36.092 -11.283  1.00 21.61           C  
ANISOU 1102  C   TYR B 138     3099   3175   1938    288   -475    146       C  
ATOM   1103  O   TYR B 138       9.920  37.121 -10.913  1.00 24.67           O  
ANISOU 1103  O   TYR B 138     3606   3482   2284    269   -460    236       O  
ATOM   1104  CB  TYR B 138       7.557  35.176  -9.801  1.00 16.93           C  
ANISOU 1104  CB  TYR B 138     2213   2654   1566    353   -506    -14       C  
ATOM   1105  CG  TYR B 138       8.231  35.759  -8.582  1.00 17.20           C  
ANISOU 1105  CG  TYR B 138     2277   2609   1649    316   -436     69       C  
ATOM   1106  CD1 TYR B 138       7.654  36.817  -7.893  1.00 20.16           C  
ANISOU 1106  CD1 TYR B 138     2675   2949   2036    399   -497     78       C  
ATOM   1107  CD2 TYR B 138       9.441  35.248  -8.114  1.00 16.18           C  
ANISOU 1107  CD2 TYR B 138     2148   2449   1552    212   -321    122       C  
ATOM   1108  CE1 TYR B 138       8.261  37.360  -6.783  1.00 21.79           C  
ANISOU 1108  CE1 TYR B 138     2912   3086   2282    362   -438    144       C  
ATOM   1109  CE2 TYR B 138      10.062  35.793  -6.991  1.00 21.56           C  
ANISOU 1109  CE2 TYR B 138     2849   3072   2271    183   -271    185       C  
ATOM   1110  CZ  TYR B 138       9.461  36.843  -6.333  1.00 22.65           C  
ANISOU 1110  CZ  TYR B 138     3017   3173   2418    248   -325    198       C  
ATOM   1111  OH  TYR B 138      10.046  37.388  -5.222  1.00 23.60           O  
ANISOU 1111  OH  TYR B 138     3158   3238   2569    217   -279    248       O  
ATOM   1112  N   TYR B 139      10.016  35.077 -11.832  1.00 21.49           N  
ANISOU 1112  N   TYR B 139     3039   3210   1916    208   -398    116       N  
ATOM   1113  CA  TYR B 139      11.463  35.114 -12.002  1.00 21.07           C  
ANISOU 1113  CA  TYR B 139     3046   3146   1812    101   -287    174       C  
ATOM   1114  C   TYR B 139      11.856  35.712 -13.347  1.00 30.24           C  
ANISOU 1114  C   TYR B 139     4382   4319   2790     72   -301    217       C  
ATOM   1115  O   TYR B 139      11.122  35.585 -14.318  1.00 30.53           O  
ANISOU 1115  O   TYR B 139     4464   4391   2745    137   -388    179       O  
ATOM   1116  CB  TYR B 139      12.051  33.723 -11.827  1.00 20.37           C  
ANISOU 1116  CB  TYR B 139     2825   3107   1810     49   -198    106       C  
ATOM   1117  CG  TYR B 139      11.783  33.179 -10.441  1.00 24.67           C  
ANISOU 1117  CG  TYR B 139     3252   3615   2505     60   -175     86       C  
ATOM   1118  CD1 TYR B 139      12.608  33.508  -9.372  1.00 23.42           C  
ANISOU 1118  CD1 TYR B 139     3084   3418   2395     26   -115    139       C  
ATOM   1119  CD2 TYR B 139      10.682  32.366 -10.198  1.00 15.36           C  
ANISOU 1119  CD2 TYR B 139     1981   2446   1408     90   -209      8       C  
ATOM   1120  CE1 TYR B 139      12.349  33.029  -8.101  1.00 18.56           C  
ANISOU 1120  CE1 TYR B 139     2393   2766   1894     37    -97    129       C  
ATOM   1121  CE2 TYR B 139      10.411  31.892  -8.939  1.00 17.10           C  
ANISOU 1121  CE2 TYR B 139     2128   2627   1742     76   -173     -4       C  
ATOM   1122  CZ  TYR B 139      11.251  32.221  -7.893  1.00 17.96           C  
ANISOU 1122  CZ  TYR B 139     2251   2688   1884     57   -120     64       C  
ATOM   1123  OH  TYR B 139      10.987  31.734  -6.640  1.00 20.67           O  
ANISOU 1123  OH  TYR B 139     2548   2989   2317     43    -86     58       O  
ATOM   1124  N   ALA B 140      13.019  36.359 -13.387  1.00 36.48           N  
ANISOU 1124  N   ALA B 140     5272   5085   3506    -37   -210    286       N  
ATOM   1125  CA  ALA B 140      13.507  37.051 -14.584  1.00 36.48           C  
ANISOU 1125  CA  ALA B 140     5474   5081   3306   -108   -192    340       C  
ATOM   1126  C   ALA B 140      13.562  36.167 -15.823  1.00 34.03           C  
ANISOU 1126  C   ALA B 140     5149   4872   2909   -118   -178    270       C  
ATOM   1127  O   ALA B 140      13.392  36.645 -16.948  1.00 39.61           O  
ANISOU 1127  O   ALA B 140     6040   5575   3434   -120   -221    304       O  
ATOM   1128  CB  ALA B 140      14.878  37.646 -14.312  1.00 37.79           C  
ANISOU 1128  CB  ALA B 140     5693   5237   3429   -273    -54    389       C  
ATOM   1129  N   ASP B 141      13.788  34.874 -15.621  1.00 29.64           N  
ANISOU 1129  N   ASP B 141     4395   4396   2470   -118   -125    171       N  
ATOM   1130  CA  ASP B 141      13.866  33.958 -16.746  1.00 29.09           C  
ANISOU 1130  CA  ASP B 141     4301   4421   2330   -125   -109     85       C  
ATOM   1131  C   ASP B 141      12.503  33.408 -17.141  1.00 29.86           C  
ANISOU 1131  C   ASP B 141     4362   4532   2451     -6   -242     18       C  
ATOM   1132  O   ASP B 141      12.391  32.577 -18.046  1.00 29.72           O  
ANISOU 1132  O   ASP B 141     4317   4589   2385      0   -248    -70       O  
ATOM   1133  CB  ASP B 141      14.894  32.849 -16.471  1.00 35.53           C  
ANISOU 1133  CB  ASP B 141     4951   5310   3239   -177     12     -4       C  
ATOM   1134  CG  ASP B 141      14.520  31.964 -15.298  1.00 37.01           C  
ANISOU 1134  CG  ASP B 141     4977   5455   3628   -108     -9    -51       C  
ATOM   1135  OD1 ASP B 141      13.519  32.243 -14.610  1.00 26.59           O  
ANISOU 1135  OD1 ASP B 141     3650   4068   2385    -47    -92    -18       O  
ATOM   1136  OD2 ASP B 141      15.266  30.995 -15.040  1.00 42.95           O1-
ANISOU 1136  OD2 ASP B 141     5621   6244   4456   -114     61   -126       O1-
ATOM   1137  N   GLY B 142      11.463  33.906 -16.478  1.00 29.25           N  
ANISOU 1137  N   GLY B 142     4276   4395   2443     87   -350     43       N  
ATOM   1138  CA  GLY B 142      10.103  33.586 -16.863  1.00 27.29           C  
ANISOU 1138  CA  GLY B 142     3981   4184   2204    198   -488    -39       C  
ATOM   1139  C   GLY B 142       9.366  32.588 -15.988  1.00 30.26           C  
ANISOU 1139  C   GLY B 142     4149   4578   2772    218   -492   -140       C  
ATOM   1140  O   GLY B 142       8.135  32.508 -16.055  1.00 29.92           O  
ANISOU 1140  O   GLY B 142     4036   4574   2756    300   -604   -219       O  
ATOM   1141  N   GLU B 143      10.091  31.820 -15.177  1.00 26.59           N  
ANISOU 1141  N   GLU B 143     3587   4087   2429    143   -373   -148       N  
ATOM   1142  CA  GLU B 143       9.431  30.775 -14.394  1.00 29.42           C  
ANISOU 1142  CA  GLU B 143     3793   4439   2944    134   -361   -238       C  
ATOM   1143  C   GLU B 143       8.463  31.376 -13.372  1.00 22.45           C  
ANISOU 1143  C   GLU B 143     2853   3532   2145    181   -416   -227       C  
ATOM   1144  O   GLU B 143       8.710  32.446 -12.799  1.00 22.72           O  
ANISOU 1144  O   GLU B 143     2951   3517   2165    207   -423   -131       O  
ATOM   1145  CB  GLU B 143      10.428  29.845 -13.695  1.00 29.85           C  
ANISOU 1145  CB  GLU B 143     3801   4447   3093     69   -240   -240       C  
ATOM   1146  CG  GLU B 143       9.803  28.519 -13.261  1.00 36.62           C  
ANISOU 1146  CG  GLU B 143     4565   5279   4070     39   -222   -343       C  
ATOM   1147  CD  GLU B 143      10.815  27.556 -12.665  1.00 46.06           C  
ANISOU 1147  CD  GLU B 143     5760   6405   5335      9   -128   -345       C  
ATOM   1148  OE1 GLU B 143      10.434  26.415 -12.315  1.00 47.28           O  
ANISOU 1148  OE1 GLU B 143     5890   6502   5571    -24   -105   -419       O  
ATOM   1149  OE2 GLU B 143      11.996  27.943 -12.545  1.00 49.69           O1-
ANISOU 1149  OE2 GLU B 143     6251   6866   5763     18    -81   -283       O1-
ATOM   1150  N   ASP B 144       7.353  30.681 -13.171  1.00 18.90           N  
ANISOU 1150  N   ASP B 144     2280   3125   1777    181   -450   -343       N  
ATOM   1151  CA  ASP B 144       6.351  31.073 -12.199  1.00 20.43           C  
ANISOU 1151  CA  ASP B 144     2379   3328   2054    211   -485   -374       C  
ATOM   1152  C   ASP B 144       6.805  30.673 -10.802  1.00 20.44           C  
ANISOU 1152  C   ASP B 144     2348   3248   2169    131   -367   -328       C  
ATOM   1153  O   ASP B 144       7.631  29.778 -10.658  1.00 21.37           O  
ANISOU 1153  O   ASP B 144     2490   3311   2318     61   -279   -312       O  
ATOM   1154  CB  ASP B 144       5.055  30.377 -12.550  1.00 27.50           C  
ANISOU 1154  CB  ASP B 144     3136   4325   2987    205   -543   -542       C  
ATOM   1155  CG  ASP B 144       4.662  30.613 -13.994  1.00 34.01           C  
ANISOU 1155  CG  ASP B 144     3998   5239   3686    292   -671   -601       C  
ATOM   1156  OD1 ASP B 144       4.718  31.774 -14.450  1.00 32.92           O  
ANISOU 1156  OD1 ASP B 144     3972   5098   3437    409   -769   -527       O  
ATOM   1157  OD2 ASP B 144       4.348  29.629 -14.686  1.00 38.21           O1-
ANISOU 1157  OD2 ASP B 144     4471   5830   4217    241   -675   -717       O1-
ATOM   1158  N   ALA B 145       6.279  31.343  -9.780  1.00 17.10           N  
ANISOU 1158  N   ALA B 145     1881   2818   1799    157   -376   -313       N  
ATOM   1159  CA  ALA B 145       6.581  30.992  -8.392  1.00 16.26           C  
ANISOU 1159  CA  ALA B 145     1752   2642   1783     84   -272   -274       C  
ATOM   1160  C   ALA B 145       5.325  30.627  -7.633  1.00 17.87           C  
ANISOU 1160  C   ALA B 145     1825   2898   2067     36   -253   -384       C  
ATOM   1161  O   ALA B 145       4.272  31.189  -7.890  1.00 19.07           O  
ANISOU 1161  O   ALA B 145     1886   3149   2210    103   -338   -473       O  
ATOM   1162  CB  ALA B 145       7.257  32.162  -7.680  1.00 19.37           C  
ANISOU 1162  CB  ALA B 145     2222   2979   2159    131   -270   -154       C  
ATOM   1163  N   TYR B 146       5.443  29.716  -6.672  1.00 16.59           N  
ANISOU 1163  N   TYR B 146     1660   2673   1971    -77   -142   -384       N  
ATOM   1164  CA  TYR B 146       4.409  29.586  -5.659  1.00 17.17           C  
ANISOU 1164  CA  TYR B 146     1631   2787   2104   -149    -90   -464       C  
ATOM   1165  C   TYR B 146       4.689  30.652  -4.625  1.00 18.72           C  
ANISOU 1165  C   TYR B 146     1854   2957   2302    -88    -86   -375       C  
ATOM   1166  O   TYR B 146       5.832  30.794  -4.182  1.00 15.44           O  
ANISOU 1166  O   TYR B 146     1552   2443   1872    -76    -54   -249       O  
ATOM   1167  CB  TYR B 146       4.476  28.220  -4.976  1.00 19.81           C  
ANISOU 1167  CB  TYR B 146     2008   3034   2483   -309     35   -481       C  
ATOM   1168  CG  TYR B 146       3.953  27.080  -5.823  1.00 22.11           C  
ANISOU 1168  CG  TYR B 146     2267   3348   2786   -405     47   -603       C  
ATOM   1169  CD1 TYR B 146       2.616  27.015  -6.185  1.00 26.93           C  
ANISOU 1169  CD1 TYR B 146     2712   4102   3417   -458     24   -773       C  
ATOM   1170  CD2 TYR B 146       4.804  26.083  -6.274  1.00 22.88           C  
ANISOU 1170  CD2 TYR B 146     2489   3332   2873   -435     75   -567       C  
ATOM   1171  CE1 TYR B 146       2.139  25.979  -6.957  1.00 28.30           C  
ANISOU 1171  CE1 TYR B 146     2852   4301   3600   -561     34   -900       C  
ATOM   1172  CE2 TYR B 146       4.339  25.043  -7.051  1.00 22.90           C  
ANISOU 1172  CE2 TYR B 146     2476   3340   2884   -526     85   -687       C  
ATOM   1173  CZ  TYR B 146       3.006  25.003  -7.394  1.00 30.08           C  
ANISOU 1173  CZ  TYR B 146     3226   4389   3813   -599     66   -851       C  
ATOM   1174  OH  TYR B 146       2.529  23.975  -8.164  1.00 38.74           O  
ANISOU 1174  OH  TYR B 146     4301   5499   4918   -705     76   -986       O  
ATOM   1175  N   ALA B 147       3.666  31.406  -4.242  1.00 17.13           N  
ANISOU 1175  N   ALA B 147     1540   2851   2116    -41   -122   -457       N  
ATOM   1176  CA  ALA B 147       3.800  32.305  -3.101  1.00 16.66           C  
ANISOU 1176  CA  ALA B 147     1499   2766   2064      0   -102   -398       C  
ATOM   1177  C   ALA B 147       3.412  31.493  -1.867  1.00 19.97           C  
ANISOU 1177  C   ALA B 147     1882   3178   2527   -153     36   -437       C  
ATOM   1178  O   ALA B 147       2.355  30.849  -1.836  1.00 24.19           O  
ANISOU 1178  O   ALA B 147     2294   3805   3092   -254     85   -578       O  
ATOM   1179  CB  ALA B 147       2.907  33.533  -3.255  1.00 17.47           C  
ANISOU 1179  CB  ALA B 147     1513   2969   2156    146   -213   -478       C  
ATOM   1180  N   MET B 148       4.284  31.470  -0.872  1.00 17.31           N  
ANISOU 1180  N   MET B 148     1660   2734   2182   -184    103   -318       N  
ATOM   1181  CA  MET B 148       4.001  30.703   0.338  1.00 17.14           C  
ANISOU 1181  CA  MET B 148     1658   2683   2172   -331    234   -332       C  
ATOM   1182  C   MET B 148       4.108  31.535   1.606  1.00 16.30           C  
ANISOU 1182  C   MET B 148     1570   2571   2051   -301    264   -287       C  
ATOM   1183  O   MET B 148       4.933  32.433   1.689  1.00 18.76           O  
ANISOU 1183  O   MET B 148     1946   2837   2344   -188    199   -192       O  
ATOM   1184  CB  MET B 148       4.903  29.473   0.425  1.00 16.28           C  
ANISOU 1184  CB  MET B 148     1708   2430   2049   -415    294   -246       C  
ATOM   1185  CG  MET B 148       4.787  28.563  -0.790  1.00 33.93           C  
ANISOU 1185  CG  MET B 148     3935   4661   4298   -452    273   -305       C  
ATOM   1186  CE  MET B 148       4.435  26.111   0.868  1.00 53.49           C  
ANISOU 1186  CE  MET B 148     6652   6922   6750   -799    524   -308       C  
ATOM   1187  S   MET B 148       5.622  26.827  -0.496  1.00 51.58           S  
ANISOU 1187  S   MET B 148     6386   6696   6516   -565    359   -238      SE  
ATOM   1188  N   HIS B 149       3.292  31.184   2.599  1.00 18.16           N  
ANISOU 1188  N   HIS B 149     1758   2855   2287   -425    375   -362       N  
ATOM   1189  CA  HIS B 149       3.152  31.963   3.824  1.00 22.84           C  
ANISOU 1189  CA  HIS B 149     2344   3476   2860   -408    414   -357       C  
ATOM   1190  C   HIS B 149       3.104  31.046   5.046  1.00 18.88           C  
ANISOU 1190  C   HIS B 149     1944   2915   2314   -586    566   -332       C  
ATOM   1191  O   HIS B 149       2.630  29.919   4.971  1.00 20.00           O  
ANISOU 1191  O   HIS B 149     2104   3042   2452   -750    659   -383       O  
ATOM   1192  CB  HIS B 149       1.868  32.808   3.781  1.00 36.48           C  
ANISOU 1192  CB  HIS B 149     3862   5382   4616   -351    388   -528       C  
ATOM   1193  CG  HIS B 149       1.844  33.832   2.684  1.00 53.16           C  
ANISOU 1193  CG  HIS B 149     5916   7534   6747   -151    221   -549       C  
ATOM   1194  CD2 HIS B 149       1.497  33.731   1.378  1.00 57.22           C  
ANISOU 1194  CD2 HIS B 149     6361   8101   7278    -91    126   -611       C  
ATOM   1195  ND1 HIS B 149       2.242  35.139   2.874  1.00 54.92           N  
ANISOU 1195  ND1 HIS B 149     6186   7725   6956     10    131   -495       N  
ATOM   1196  CE1 HIS B 149       2.120  35.804   1.736  1.00 57.18           C  
ANISOU 1196  CE1 HIS B 149     6454   8029   7242    160    -11   -515       C  
ATOM   1197  NE2 HIS B 149       1.676  34.971   0.813  1.00 57.62           N  
ANISOU 1197  NE2 HIS B 149     6437   8144   7313    109    -20   -584       N  
ATOM   1198  N   LYS B 150       3.626  31.544   6.160  1.00 17.67           N  
ANISOU 1198  N   LYS B 150     1881   2716   2116   -557    588   -252       N  
ATOM   1199  CA  LYS B 150       3.548  30.860   7.435  1.00 18.54           C  
ANISOU 1199  CA  LYS B 150     2113   2775   2155   -709    725   -223       C  
ATOM   1200  C   LYS B 150       3.117  31.880   8.476  1.00 22.02           C  
ANISOU 1200  C   LYS B 150     2482   3314   2569   -680    758   -276       C  
ATOM   1201  O   LYS B 150       3.786  32.891   8.654  1.00 24.04           O  
ANISOU 1201  O   LYS B 150     2755   3551   2826   -528    665   -215       O  
ATOM   1202  CB  LYS B 150       4.907  30.277   7.811  1.00 19.41           C  
ANISOU 1202  CB  LYS B 150     2459   2704   2211   -681    700    -52       C  
ATOM   1203  CG  LYS B 150       4.889  29.469   9.122  1.00 27.99           C  
ANISOU 1203  CG  LYS B 150     3736   3704   3196   -828    826     -1       C  
ATOM   1204  CD  LYS B 150       3.830  28.367   9.035  1.00 41.20           C  
ANISOU 1204  CD  LYS B 150     5415   5383   4856  -1054    967    -93       C  
ATOM   1205  CE  LYS B 150       3.690  27.537  10.318  1.00 43.76           C  
ANISOU 1205  CE  LYS B 150     5967   5607   5054  -1239   1114    -42       C  
ATOM   1206  NZ  LYS B 150       4.835  26.616  10.521  1.00 45.74           N1+
ANISOU 1206  NZ  LYS B 150     6515   5630   5234  -1194   1065    118       N1+
ATOM   1207  N   ASP B 151       1.994  31.629   9.132  1.00 20.52           N  
ANISOU 1207  N   ASP B 151     2207   3237   2355   -834    896   -403       N  
ATOM   1208  CA  ASP B 151       1.512  32.505  10.175  1.00 27.88           C  
ANISOU 1208  CA  ASP B 151     3065   4277   3252   -818    947   -477       C  
ATOM   1209  C   ASP B 151       2.218  32.154  11.482  1.00 30.01           C  
ANISOU 1209  C   ASP B 151     3566   4429   3408   -895   1027   -347       C  
ATOM   1210  O   ASP B 151       2.425  30.988  11.792  1.00 30.05           O  
ANISOU 1210  O   ASP B 151     3751   4321   3345  -1049   1116   -271       O  
ATOM   1211  CB  ASP B 151      -0.004  32.358  10.329  1.00 37.24           C  
ANISOU 1211  CB  ASP B 151     4036   5665   4449   -962   1075   -698       C  
ATOM   1212  CG  ASP B 151      -0.629  33.458  11.192  1.00 45.44           C  
ANISOU 1212  CG  ASP B 151     4934   6860   5471   -895   1104   -825       C  
ATOM   1213  OD1 ASP B 151       0.083  34.090  12.001  1.00 38.04           O  
ANISOU 1213  OD1 ASP B 151     4120   5849   4483   -808   1076   -725       O  
ATOM   1214  OD2 ASP B 151      -1.852  33.674  11.069  1.00 53.75           O1-
ANISOU 1214  OD2 ASP B 151     5765   8094   6563   -912   1126  -1030       O1-
ATOM   1215  N   PHE B 152       2.594  33.172  12.242  1.00 20.80           N  
ANISOU 1215  N   PHE B 152     2413   3280   2212   -780    984   -323       N  
ATOM   1216  CA  PHE B 152       3.233  32.954  13.531  1.00 24.57           C  
ANISOU 1216  CA  PHE B 152     3100   3668   2568   -832   1043   -214       C  
ATOM   1217  C   PHE B 152       2.240  33.074  14.673  1.00 36.30           C  
ANISOU 1217  C   PHE B 152     4538   5283   3971   -974   1208   -334       C  
ATOM   1218  O   PHE B 152       2.640  33.123  15.827  1.00 43.55           O  
ANISOU 1218  O   PHE B 152     5614   6159   4774  -1003   1255   -267       O  
ATOM   1219  CB  PHE B 152       4.388  33.930  13.750  1.00 22.62           C  
ANISOU 1219  CB  PHE B 152     2916   3356   2322   -639    899   -116       C  
ATOM   1220  CG  PHE B 152       5.537  33.740  12.804  1.00 28.39           C  
ANISOU 1220  CG  PHE B 152     3716   3966   3105   -528    761      4       C  
ATOM   1221  CD1 PHE B 152       5.991  32.471  12.488  1.00 30.54           C  
ANISOU 1221  CD1 PHE B 152     4130   4121   3353   -596    775     92       C  
ATOM   1222  CD2 PHE B 152       6.169  34.836  12.246  1.00 26.73           C  
ANISOU 1222  CD2 PHE B 152     3442   3756   2960   -362    625     20       C  
ATOM   1223  CE1 PHE B 152       7.057  32.300  11.627  1.00 30.59           C  
ANISOU 1223  CE1 PHE B 152     4178   4039   3405   -486    654    178       C  
ATOM   1224  CE2 PHE B 152       7.230  34.683  11.392  1.00 26.78           C  
ANISOU 1224  CE2 PHE B 152     3498   3675   3004   -284    519    112       C  
ATOM   1225  CZ  PHE B 152       7.682  33.405  11.083  1.00 29.63           C  
ANISOU 1225  CZ  PHE B 152     3967   3946   3345   -339    534    184       C  
ATOM   1226  N   SER B 153       0.952  33.130  14.348  1.00 45.74           N  
ANISOU 1226  N   SER B 153     5507   6655   5218  -1058   1293   -524       N  
ATOM   1227  CA  SER B 153      -0.100  33.146  15.367  1.00 56.94           C  
ANISOU 1227  CA  SER B 153     6867   8177   6591  -1170   1396   -651       C  
ATOM   1228  C   SER B 153       0.034  31.973  16.328  1.00 59.67           C  
ANISOU 1228  C   SER B 153     7474   8380   6819  -1356   1490   -545       C  
ATOM   1229  O   SER B 153      -0.268  32.099  17.511  1.00 64.75           O  
ANISOU 1229  O   SER B 153     8175   9053   7375  -1421   1564   -570       O  
ATOM   1230  CB  SER B 153      -1.487  33.125  14.717  1.00 62.14           C  
ANISOU 1230  CB  SER B 153     7262   9006   7342  -1216   1411   -866       C  
ATOM   1231  OG  SER B 153      -1.687  31.931  13.978  1.00 66.27           O  
ANISOU 1231  OG  SER B 153     7831   9460   7889  -1354   1435   -851       O  
CONECT   90   92
CONECT   92   90   93
CONECT   93   92   94   96
CONECT   94   93   95  100
CONECT   95   94
CONECT   96   93   97
CONECT   97   96   99
CONECT   98   99
CONECT   99   97   98
CONECT  100   94
CONECT  316  321
CONECT  321  316  322
CONECT  322  321  323  325
CONECT  323  322  324  329
CONECT  324  323
CONECT  325  322  326
CONECT  326  325  328
CONECT  327  328
CONECT  328  326  327
CONECT  329  323
CONECT  465  472
CONECT  472  465  473
CONECT  473  472  474  476
CONECT  474  473  475  480
CONECT  475  474
CONECT  476  473  477
CONECT  477  476  479
CONECT  478  479
CONECT  479  477  478
CONECT  480  474
CONECT  610  615
CONECT  615  610  616
CONECT  616  615  617  619
CONECT  617  616  618  623
CONECT  618  617
CONECT  619  616  620
CONECT  620  619  622
CONECT  621  622
CONECT  622  620  621
CONECT  623  617
CONECT  720  726
CONECT  726  720  727
CONECT  727  726  728  730
CONECT  728  727  729  734
CONECT  729  728
CONECT  730  727  731
CONECT  731  730  733
CONECT  732  733
CONECT  733  731  732
CONECT  734  728
CONECT  778  781
CONECT  781  778  782
CONECT  782  781  783  785
CONECT  783  782  784  789
CONECT  784  783
CONECT  785  782  786
CONECT  786  785  788
CONECT  787  788
CONECT  788  786  787
CONECT  789  783
CONECT  844  854
CONECT  854  844  855
CONECT  855  854  856  858
CONECT  856  855  857  862
CONECT  857  856
CONECT  858  855  859
CONECT  859  858  861
CONECT  860  861
CONECT  861  859  860
CONECT  862  856
CONECT 1177 1180
CONECT 1180 1177 1181
CONECT 1181 1180 1182 1184
CONECT 1182 1181 1183 1188
CONECT 1183 1182
CONECT 1184 1181 1185
CONECT 1185 1184 1187
CONECT 1186 1187
CONECT 1187 1185 1186
CONECT 1188 1182
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.