ATOM   1049  N   LEU B 270      48.547  65.960  44.922  1.00 55.99      B    N  
ATOM   1050  CA  LEU B 270      48.585  64.944  43.836  1.00 55.45      B    C  
ATOM   1051  C   LEU B 270      49.421  63.719  44.264  1.00 55.22      B    C  
ATOM   1052  O   LEU B 270      50.350  63.824  45.077  1.00 54.85      B    O  
ATOM   1053  CB  LEU B 270      49.160  65.574  42.556  1.00 55.49      B    C  
ATOM   1054  CG  LEU B 270      49.046  64.791  41.241  1.00 55.41      B    C  
ATOM   1055  CD1 LEU B 270      47.580  64.622  40.852  1.00 54.19      B    C  
ATOM   1056  CD2 LEU B 270      49.801  65.532  40.152  1.00 55.12      B    C  
ATOM   1057  N   LYS B 271      49.067  62.561  43.710  1.00 53.63      B    N  
ATOM   1058  CA  LYS B 271      49.732  61.294  44.007  1.00 50.14      B    C  
ATOM   1059  C   LYS B 271      51.219  61.318  43.666  1.00 48.62      B    C  
ATOM   1060  O   LYS B 271      51.722  62.285  43.092  1.00 47.58      B    O  
ATOM   1061  CB  LYS B 271      49.082  60.166  43.197  1.00 49.43      B    C  
ATOM   1062  CG  LYS B 271      47.580  60.272  43.002  1.00 48.42      B    C  
ATOM   1063  CD  LYS B 271      46.824  59.896  44.256  1.00 49.84      B    C  
ATOM   1064  CE  LYS B 271      45.340  59.790  43.980  1.00 50.26      B    C  
ATOM   1065  NZ  LYS B 271      45.067  58.947  42.777  1.00 53.47      B    N  
ATOM   1066  N   ARG B 272      51.903  60.228  44.015  1.00 46.99      B    N  
ATOM   1067  CA  ARG B 272      53.323  60.054  43.724  1.00 44.73      B    C  
ATOM   1068  C   ARG B 272      53.756  58.593  43.921  1.00 43.99      B    C  
ATOM   1069  O   ARG B 272      53.535  58.010  44.984  1.00 44.94      B    O  
ATOM   1070  CB  ARG B 272      54.168  60.951  44.616  1.00 43.99      B    C  
ATOM   1071  CG  ARG B 272      55.567  61.093  44.078  1.00 45.57      B    C  
ATOM   1072  CD  ARG B 272      56.538  61.684  45.066  1.00 46.00      B    C  
ATOM   1073  NE  ARG B 272      57.851  61.826  44.454  1.00 47.85      B    N  
ATOM   1074  CZ  ARG B 272      58.204  62.821  43.648  1.00 48.34      B    C  
ATOM   1075  NH1 ARG B 272      57.339  63.785  43.352  1.00 49.68      B    N  
ATOM   1076  NH2 ARG B 272      59.423  62.843  43.129  1.00 47.77      B    N  
ATOM   1077  N   ASP B 273      54.366  58.000  42.902  1.00 41.62      B    N  
ATOM   1078  CA  ASP B 273      54.809  56.615  43.001  1.00 39.89      B    C  
ATOM   1079  C   ASP B 273      56.008  56.573  43.939  1.00 39.23      B    C  
ATOM   1080  O   ASP B 273      57.146  56.489  43.499  1.00 38.53      B    O  
ATOM   1081  CB  ASP B 273      55.207  56.092  41.622  1.00 39.56      B    C  
ATOM   1082  CG  ASP B 273      55.611  54.638  41.640  1.00 40.68      B    C  
ATOM   1083  OD1 ASP B 273      56.099  54.156  42.682  1.00 38.28      B    O  
ATOM   1084  OD2 ASP B 273      55.460  53.985  40.590  1.00 42.09      B    O  
ATOM   1085  N   LEU B 274      55.734  56.646  45.235  1.00 38.79      B    N  
ATOM   1086  CA  LEU B 274      56.769  56.650  46.258  1.00 39.10      B    C  
ATOM   1087  C   LEU B 274      57.790  55.550  46.037  1.00 38.57      B    C  
ATOM   1088  O   LEU B 274      59.019  55.768  46.141  1.00 37.37      B    O  
ATOM   1089  CB  LEU B 274      56.127  56.490  47.632  1.00 39.81      B    C  
ATOM   1090  CG  LEU B 274      55.177  57.652  47.968  1.00 41.17      B    C  
ATOM   1091  CD1 LEU B 274      54.013  57.210  48.862  1.00 42.29      B    C  
ATOM   1092  CD2 LEU B 274      55.992  58.749  48.628  1.00 43.26      B    C  
ATOM   1093  N   ILE B 275      57.289  54.357  45.738  1.00 39.20      B    N  
ATOM   1094  CA  ILE B 275      58.144  53.197  45.510  1.00 40.00      B    C  
ATOM   1095  C   ILE B 275      59.229  53.336  44.444  1.00 38.02      B    C  
ATOM   1096  O   ILE B 275      60.357  52.885  44.642  1.00 37.67      B    O  
ATOM   1097  CB  ILE B 275      57.284  52.032  45.172  1.00 42.75      B    C  
ATOM   1098  CG1 ILE B 275      57.791  50.850  45.945  1.00 45.59      B    C  
ATOM   1099  CG2 ILE B 275      57.202  51.886  43.684  1.00 47.41      B    C  
ATOM   1100  CD1 ILE B 275      57.584  49.645  45.210  1.00 44.16      B    C  
ATOM   1101  N   THR B 276      58.873  53.972  43.333  1.00 35.72      B    N  
ATOM   1102  CA  THR B 276      59.808  54.180  42.242  1.00 36.67      B    C  
ATOM   1103  C   THR B 276      60.743  55.346  42.542  1.00 35.93      B    C  
ATOM   1104  O   THR B 276      61.929  55.308  42.228  1.00 36.34      B    O  
ATOM   1105  CB  THR B 276      59.066  54.509  40.935  1.00 37.29      B    C  
ATOM   1106  OG1 THR B 276      57.977  53.603  40.771  1.00 40.83      B    O  
ATOM   1107  CG2 THR B 276      59.981  54.364  39.747  1.00 38.12      B    C  
ATOM   1108  N   SER B 277      60.181  56.388  43.140  1.00 34.86      B    N  
ATOM   1109  CA  SER B 277      60.908  57.599  43.459  1.00 33.59      B    C  
ATOM   1110  C   SER B 277      61.853  57.540  44.644  1.00 33.53      B    C  
ATOM   1111  O   SER B 277      62.851  58.243  44.662  1.00 33.96      B    O  
ATOM   1112  CB  SER B 277      59.918  58.739  43.668  1.00 36.42      B    C  
ATOM   1113  OG  SER B 277      59.162  58.994  42.490  1.00 37.58      B    O  
ATOM   1114  N   LEU B 278      61.528  56.737  45.651  1.00 33.82      B    N  
ATOM   1115  CA  LEU B 278      62.382  56.615  46.822  1.00 32.25      B    C  
ATOM   1116  C   LEU B 278      63.665  55.883  46.451  1.00 33.07      B    C  
ATOM   1117  O   LEU B 278      63.740  55.243  45.404  1.00 33.39      B    O  
ATOM   1118  CB  LEU B 278      61.657  55.844  47.920  1.00 32.58      B    C  
ATOM   1119  CG  LEU B 278      60.934  56.634  49.020  1.00 34.12      B    C  
ATOM   1120  CD1 LEU B 278      61.779  57.853  49.351  1.00 35.06      B    C  
ATOM   1121  CD2 LEU B 278      59.538  57.053  48.604  1.00 33.51      B    C  
ATOM   1122  N   PRO B 279      64.713  56.000  47.279  1.00 32.98      B    N  
ATOM   1123  CA  PRO B 279      65.935  55.278  46.912  1.00 32.97      B    C  
ATOM   1124  C   PRO B 279      65.710  53.788  47.141  1.00 35.60      B    C  
ATOM   1125  O   PRO B 279      65.050  53.394  48.103  1.00 35.20      B    O  
ATOM   1126  CB  PRO B 279      66.972  55.866  47.849  1.00 31.04      B    C  
ATOM   1127  CG  PRO B 279      66.500  57.263  48.002  1.00 31.67      B    C  
ATOM   1128  CD  PRO B 279      65.025  57.073  48.234  1.00 32.44      B    C  
ATOM   1129  N   PHE B 280      66.254  52.966  46.251  1.00 37.99      B    N  
ATOM   1130  CA  PHE B 280      66.090  51.529  46.345  1.00 38.91      B    C  
ATOM   1131  C   PHE B 280      65.983  51.000  47.778  1.00 40.96      B    C  
ATOM   1132  O   PHE B 280      65.007  50.323  48.117  1.00 42.55      B    O  
ATOM   1133  CB  PHE B 280      67.238  50.825  45.634  1.00 39.28      B    C  
ATOM   1134  CG  PHE B 280      67.083  49.343  45.596  1.00 40.70      B    C  
ATOM   1135  CD1 PHE B 280      65.985  48.767  44.946  1.00 41.38      B    C  
ATOM   1136  CD2 PHE B 280      67.981  48.523  46.268  1.00 39.28      B    C  
ATOM   1137  CE1 PHE B 280      65.776  47.390  44.972  1.00 43.48      B    C  
ATOM   1138  CE2 PHE B 280      67.788  47.143  46.305  1.00 41.82      B    C  
ATOM   1139  CZ  PHE B 280      66.681  46.570  45.658  1.00 43.36      B    C  
ATOM   1140  N   GLU B 281      66.991  51.301  48.601  1.00 41.14      B    N  
ATOM   1141  CA  GLU B 281      67.055  50.868  50.010  1.00 42.59      B    C  
ATOM   1142  C   GLU B 281      65.790  51.160  50.832  1.00 42.30      B    C  
ATOM   1143  O   GLU B 281      65.299  50.301  51.587  1.00 42.54      B    O  
ATOM   1144  CB  GLU B 281      68.246  51.539  50.708  1.00 45.96      B    C  
ATOM   1145  CG  GLU B 281      69.582  50.786  50.670  1.00 54.11      B    C  
ATOM   1146  CD  GLU B 281      70.094  50.441  49.274  1.00 58.95      B    C  
ATOM   1147  OE1 GLU B 281      69.541  49.517  48.653  1.00 62.99      B    O  
ATOM   1148  OE2 GLU B 281      71.050  51.091  48.792  1.00 59.81      B    O  
ATOM   1149  N   ILE B 282      65.267  52.375  50.676  1.00 39.98      B    N  
ATOM   1150  CA  ILE B 282      64.084  52.795  51.408  1.00 37.81      B    C  
ATOM   1151  C   ILE B 282      62.847  52.040  50.969  1.00 36.75      B    C  
ATOM   1152  O   ILE B 282      62.010  51.693  51.798  1.00 38.89      B    O  
ATOM   1153  CB  ILE B 282      63.854  54.332  51.279  1.00 37.11      B    C  
ATOM   1154  CG1 ILE B 282      64.767  55.072  52.257  1.00 35.47      B    C  
ATOM   1155  CG2 ILE B 282      62.399  54.692  51.562  1.00 36.07      B    C  
ATOM   1156  CD1 ILE B 282      65.805  55.926  51.590  1.00 38.16      B    C  
ATOM   1157  N   SER B 283      62.723  51.773  49.677  1.00 35.53      B    N  
ATOM   1158  CA  SER B 283      61.552  51.055  49.208  1.00 34.81      B    C  
ATOM   1159  C   SER B 283      61.532  49.660  49.785  1.00 35.74      B    C  
ATOM   1160  O   SER B 283      60.475  49.156  50.179  1.00 34.35      B    O  
ATOM   1161  CB  SER B 283      61.531  51.008  47.693  1.00 33.70      B    C  
ATOM   1162  OG  SER B 283      61.129  52.267  47.194  1.00 34.11      B    O  
ATOM   1163  N   LEU B 284      62.713  49.052  49.864  1.00 37.16      B    N  
ATOM   1164  CA  LEU B 284      62.841  47.708  50.400  1.00 38.78      B    C  
ATOM   1165  C   LEU B 284      62.438  47.636  51.859  1.00 39.39      B    C  
ATOM   1166  O   LEU B 284      61.951  46.604  52.316  1.00 38.99      B    O  
ATOM   1167  CB  LEU B 284      64.271  47.193  50.254  1.00 40.45      B    C  
ATOM   1168  CG  LEU B 284      64.705  46.653  48.889  1.00 43.27      B    C  
ATOM   1169  CD1 LEU B 284      66.089  46.018  49.049  1.00 44.33      B    C  
ATOM   1170  CD2 LEU B 284      63.703  45.616  48.359  1.00 41.70      B    C  
ATOM   1171  N   LYS B 285      62.657  48.710  52.610  1.00 39.13      B    N  
ATOM   1172  CA  LYS B 285      62.259  48.677  54.009  1.00 38.72      B    C  
ATOM   1173  C   LYS B 285      60.743  48.619  53.990  1.00 37.44      B    C  
ATOM   1174  O   LYS B 285      60.125  47.908  54.783  1.00 37.24      B    O  
ATOM   1175  CB  LYS B 285      62.728  49.933  54.752  1.00 38.92      B    C  
ATOM   1176  CG  LYS B 285      64.226  50.150  54.675  1.00 43.00      B    C  
ATOM   1177  CD  LYS B 285      64.686  51.399  55.424  1.00 45.03      B    C  
ATOM   1178  CE  LYS B 285      64.694  51.198  56.934  1.00 47.29      B    C  
ATOM   1179  NZ  LYS B 285      63.552  51.910  57.573  1.00 47.86      B    N  
ATOM   1180  N   ILE B 286      60.150  49.353  53.055  1.00 35.44      B    N  
ATOM   1181  CA  ILE B 286      58.702  49.391  52.947  1.00 35.62      B    C  
ATOM   1182  C   ILE B 286      58.135  47.992  52.728  1.00 36.82      B    C  
ATOM   1183  O   ILE B 286      57.184  47.585  53.407  1.00 37.27      B    O  
ATOM   1184  CB  ILE B 286      58.255  50.356  51.813  1.00 33.90      B    C  
ATOM   1185  CG1 ILE B 286      58.666  51.789  52.181  1.00 34.49      B    C  
ATOM   1186  CG2 ILE B 286      56.757  50.281  51.601  1.00 29.80      B    C  
ATOM   1187  CD1 ILE B 286      58.184  52.855  51.222  1.00 35.49      B    C  
ATOM   1188  N   PHE B 287      58.732  47.254  51.793  1.00 36.71      B    N  
ATOM   1189  CA  PHE B 287      58.295  45.893  51.485  1.00 35.15      B    C  
ATOM   1190  C   PHE B 287      58.501  44.905  52.601  1.00 35.42      B    C  
ATOM   1191  O   PHE B 287      57.767  43.926  52.710  1.00 36.52      B    O  
ATOM   1192  CB  PHE B 287      58.986  45.393  50.223  1.00 33.62      B    C  
ATOM   1193  CG  PHE B 287      58.423  45.990  48.992  1.00 32.09      B    C  
ATOM   1194  CD1 PHE B 287      57.105  45.710  48.637  1.00 30.37      B    C  
ATOM   1195  CD2 PHE B 287      59.142  46.927  48.257  1.00 29.48      B    C  
ATOM   1196  CE1 PHE B 287      56.504  46.347  47.585  1.00 28.06      B    C  
ATOM   1197  CE2 PHE B 287      58.551  47.575  47.192  1.00 27.99      B    C  
ATOM   1198  CZ  PHE B 287      57.221  47.285  46.859  1.00 28.55      B    C  
ATOM   1199  N   ASN B 288      59.503  45.156  53.431  1.00 36.91      B    N  
ATOM   1200  CA  ASN B 288      59.772  44.277  54.564  1.00 38.92      B    C  
ATOM   1201  C   ASN B 288      58.727  44.462  55.647  1.00 39.06      B    C  
ATOM   1202  O   ASN B 288      58.732  43.737  56.632  1.00 40.35      B    O  
ATOM   1203  CB  ASN B 288      61.144  44.555  55.164  1.00 38.26      B    C  
ATOM   1204  CG  ASN B 288      62.247  43.920  54.380  1.00 37.13      B    C  
ATOM   1205  OD1 ASN B 288      62.280  42.700  54.208  1.00 36.36      B    O  
ATOM   1206  ND2 ASN B 288      63.167  44.741  53.893  1.00 39.73      B    N  
ATOM   1207  N   TYR B 289      57.853  45.446  55.465  1.00 39.13      B    N  
ATOM   1208  CA  TYR B 289      56.793  45.713  56.418  1.00 39.27      B    C  
ATOM   1209  C   TYR B 289      55.490  45.167  55.880  1.00 40.70      B    C  
ATOM   1210  O   TYR B 289      54.426  45.443  56.425  1.00 42.47      B    O  
ATOM   1211  CB  TYR B 289      56.634  47.213  56.658  1.00 37.62      B    C  
ATOM   1212  CG  TYR B 289      57.713  47.821  57.523  1.00 37.44      B    C  
ATOM   1213  CD1 TYR B 289      58.035  47.268  58.758  1.00 35.79      B    C  
ATOM   1214  CD2 TYR B 289      58.384  48.975  57.127  1.00 37.16      B    C  
ATOM   1215  CE1 TYR B 289      58.993  47.848  59.582  1.00 34.50      B    C  
ATOM   1216  CE2 TYR B 289      59.350  49.561  57.945  1.00 36.15      B    C  
ATOM   1217  CZ  TYR B 289      59.645  48.995  59.170  1.00 34.83      B    C  
ATOM   1218  OH  TYR B 289      60.588  49.582  59.983  1.00 33.93      B    O  
ATOM   1219  N   LEU B 290      55.568  44.396  54.804  1.00 41.10      B    N  
ATOM   1220  CA  LEU B 290      54.373  43.830  54.206  1.00 41.97      B    C  
ATOM   1221  C   LEU B 290      54.370  42.307  54.255  1.00 42.47      B    C  
ATOM   1222  O   LEU B 290      55.416  41.683  54.145  1.00 43.82      B    O  
ATOM   1223  CB  LEU B 290      54.253  44.298  52.758  1.00 43.52      B    C  
ATOM   1224  CG  LEU B 290      53.941  45.785  52.565  1.00 44.99      B    C  
ATOM   1225  CD1 LEU B 290      53.951  46.147  51.076  1.00 43.01      B    C  
ATOM   1226  CD2 LEU B 290      52.580  46.089  53.191  1.00 44.79      B    C  
ATOM   1227  N   GLN B 291      53.197  41.707  54.431  1.00 43.30      B    N  
ATOM   1228  CA  GLN B 291      53.095  40.248  54.463  1.00 43.53      B    C  
ATOM   1229  C   GLN B 291      53.259  39.759  53.044  1.00 42.47      B    C  
ATOM   1230  O   GLN B 291      52.847  40.429  52.096  1.00 42.94      B    O  
ATOM   1231  CB  GLN B 291      51.733  39.795  54.972  1.00 44.67      B    C  
ATOM   1232  CG  GLN B 291      51.267  40.495  56.214  1.00 48.20      B    C  
ATOM   1233  CD  GLN B 291      49.996  39.890  56.767  1.00 51.30      B    C  
ATOM   1234  OE1 GLN B 291      49.225  39.253  56.047  1.00 51.48      B    O  
ATOM   1235  NE2 GLN B 291      49.764  40.096  58.054  1.00 53.92      B    N  
ATOM   1236  N   PHE B 292      53.822  38.571  52.898  1.00 42.57      B    N  
ATOM   1237  CA  PHE B 292      54.075  38.018  51.570  1.00 43.76      B    C  
ATOM   1238  C   PHE B 292      52.960  38.252  50.535  1.00 43.56      B    C  
ATOM   1239  O   PHE B 292      53.243  38.624  49.388  1.00 43.85      B    O  
ATOM   1240  CB  PHE B 292      54.449  36.519  51.685  1.00 43.51      B    C  
ATOM   1241  CG  PHE B 292      53.277  35.577  51.703  1.00 42.71      B    C  
ATOM   1242  CD1 PHE B 292      52.728  35.111  50.511  1.00 41.89      B    C  
ATOM   1243  CD2 PHE B 292      52.738  35.136  52.909  1.00 41.64      B    C  
ATOM   1244  CE1 PHE B 292      51.663  34.217  50.520  1.00 41.44      B    C  
ATOM   1245  CE2 PHE B 292      51.670  34.241  52.931  1.00 40.27      B    C  
ATOM   1246  CZ  PHE B 292      51.132  33.780  51.733  1.00 41.52      B    C  
ATOM   1247  N   GLU B 293      51.704  38.067  50.929  1.00 42.57      B    N  
ATOM   1248  CA  GLU B 293      50.600  38.266  49.987  1.00 41.75      B    C  
ATOM   1249  C   GLU B 293      50.694  39.638  49.307  1.00 40.70      B    C  
ATOM   1250  O   GLU B 293      50.584  39.746  48.086  1.00 38.19      B    O  
ATOM   1251  CB  GLU B 293      49.239  38.108  50.703  1.00 42.45      B    C  
ATOM   1252  CG  GLU B 293      48.957  36.691  51.273  1.00 43.99      B    C  
ATOM   1253  CD  GLU B 293      49.388  36.501  52.734  1.00 45.44      B    C  
ATOM   1254  OE1 GLU B 293      50.435  37.056  53.146  1.00 46.78      B    O  
ATOM   1255  OE2 GLU B 293      48.680  35.777  53.473  1.00 45.32      B    O  
ATOM   1256  N   ASP B 294      50.923  40.678  50.106  1.00 40.24      B    N  
ATOM   1257  CA  ASP B 294      51.019  42.029  49.580  1.00 40.36      B    C  
ATOM   1258  C   ASP B 294      52.210  42.181  48.638  1.00 39.89      B    C  
ATOM   1259  O   ASP B 294      52.164  42.955  47.678  1.00 38.66      B    O  
ATOM   1260  CB  ASP B 294      51.117  43.039  50.727  1.00 40.50      B    C  
ATOM   1261  CG  ASP B 294      49.901  43.006  51.638  1.00 39.70      B    C  
ATOM   1262  OD1 ASP B 294      48.776  42.835  51.118  1.00 39.69      B    O  
ATOM   1263  OD2 ASP B 294      50.066  43.168  52.869  1.00 39.40      B    O  
ATOM   1264  N   ILE B 295      53.269  41.426  48.901  1.00 39.28      B    N  
ATOM   1265  CA  ILE B 295      54.454  41.487  48.065  1.00 38.45      B    C  
ATOM   1266  C   ILE B 295      54.191  40.893  46.678  1.00 39.24      B    C  
ATOM   1267  O   ILE B 295      54.711  41.390  45.678  1.00 39.72      B    O  
ATOM   1268  CB  ILE B 295      55.615  40.747  48.725  1.00 38.47      B    C  
ATOM   1269  CG1 ILE B 295      55.770  41.240  50.171  1.00 37.44      B    C  
ATOM   1270  CG2 ILE B 295      56.877  40.917  47.891  1.00 38.59      B    C  
ATOM   1271  CD1 ILE B 295      57.193  41.488  50.629  1.00 36.12      B    C  
ATOM   1272  N   ILE B 296      53.389  39.832  46.616  1.00 40.54      B    N  
ATOM   1273  CA  ILE B 296      53.052  39.195  45.339  1.00 40.66      B    C  
ATOM   1274  C   ILE B 296      52.183  40.111  44.470  1.00 41.02      B    C  
ATOM   1275  O   ILE B 296      52.366  40.178  43.258  1.00 40.85      B    O  
ATOM   1276  CB  ILE B 296      52.299  37.841  45.555  1.00 40.15      B    C  
ATOM   1277  CG1 ILE B 296      53.308  36.717  45.735  1.00 38.74      B    C  
ATOM   1278  CG2 ILE B 296      51.383  37.526  44.373  1.00 39.41      B    C  
ATOM   1279  CD1 ILE B 296      53.298  36.138  47.107  1.00 40.44      B    C  
ATOM   1280  N   ASN B 297      51.231  40.799  45.092  1.00 41.81      B    N  
ATOM   1281  CA  ASN B 297      50.343  41.708  44.371  1.00 42.75      B    C  
ATOM   1282  C   ASN B 297      51.175  42.859  43.841  1.00 41.55      B    C  
ATOM   1283  O   ASN B 297      50.954  43.339  42.734  1.00 40.41      B    O  
ATOM   1284  CB  ASN B 297      49.248  42.262  45.307  1.00 44.90      B    C  
ATOM   1285  CG  ASN B 297      48.181  41.235  45.646  1.00 46.33      B    C  
ATOM   1286  OD1 ASN B 297      47.082  41.276  45.115  1.00 48.91      B    O  
ATOM   1287  ND2 ASN B 297      48.506  40.307  46.527  1.00 48.88      B    N  
ATOM   1288  N   SER B 298      52.131  43.303  44.649  1.00 40.80      B    N  
ATOM   1289  CA  SER B 298      52.984  44.414  44.261  1.00 40.34      B    C  
ATOM   1290  C   SER B 298      53.755  44.018  43.014  1.00 40.20      B    C  
ATOM   1291  O   SER B 298      53.996  44.841  42.123  1.00 39.56      B    O  
ATOM   1292  CB  SER B 298      53.946  44.762  45.400  1.00 38.45      B    C  
ATOM   1293  OG  SER B 298      53.224  45.133  46.565  1.00 39.71      B    O  
ATOM   1294  N   LEU B 299      54.130  42.744  42.957  1.00 39.22      B    N  
ATOM   1295  CA  LEU B 299      54.866  42.223  41.818  1.00 39.54      B    C  
ATOM   1296  C   LEU B 299      54.107  42.397  40.514  1.00 37.69      B    C  
ATOM   1297  O   LEU B 299      54.694  42.296  39.444  1.00 37.68      B    O  
ATOM   1298  CB  LEU B 299      55.205  40.749  42.032  1.00 40.04      B    C  
ATOM   1299  CG  LEU B 299      56.684  40.556  42.366  1.00 41.60      B    C  
ATOM   1300  CD1 LEU B 299      56.820  39.762  43.652  1.00 44.53      B    C  
ATOM   1301  CD2 LEU B 299      57.370  39.844  41.220  1.00 43.91      B    C  
ATOM   1302  N   GLY B 300      52.811  42.671  40.611  1.00 35.94      B    N  
ATOM   1303  CA  GLY B 300      52.002  42.869  39.424  1.00 36.60      B    C  
ATOM   1304  C   GLY B 300      51.453  44.280  39.283  1.00 36.10      B    C  
ATOM   1305  O   GLY B 300      50.532  44.542  38.508  1.00 35.02      B    O  
ATOM   1306  N   VAL B 301      52.026  45.203  40.036  1.00 36.66      B    N  
ATOM   1307  CA  VAL B 301      51.581  46.579  39.979  1.00 37.41      B    C  
ATOM   1308  C   VAL B 301      52.133  47.303  38.760  1.00 36.20      B    C  
ATOM   1309  O   VAL B 301      51.432  48.084  38.133  1.00 36.31      B    O  
ATOM   1310  CB  VAL B 301      51.980  47.313  41.270  1.00 38.86      B    C  
ATOM   1311  CG1 VAL B 301      52.065  48.826  41.027  1.00 37.82      B    C  
ATOM   1312  CG2 VAL B 301      50.955  46.981  42.359  1.00 36.10      B    C  
ATOM   1313  N   SER B 302      53.389  47.045  38.426  1.00 36.65      B    N  
ATOM   1314  CA  SER B 302      54.008  47.673  37.264  1.00 36.71      B    C  
ATOM   1315  C   SER B 302      55.355  47.021  36.963  1.00 36.79      B    C  
ATOM   1316  O   SER B 302      55.892  46.268  37.778  1.00 34.02      B    O  
ATOM   1317  CB  SER B 302      54.202  49.172  37.507  1.00 36.29      B    C  
ATOM   1318  OG  SER B 302      55.155  49.418  38.531  1.00 39.41      B    O  
ATOM   1319  N   GLN B 303      55.897  47.311  35.786  1.00 38.35      B    N  
ATOM   1320  CA  GLN B 303      57.185  46.755  35.386  1.00 40.13      B    C  
ATOM   1321  C   GLN B 303      58.324  47.142  36.331  1.00 39.54      B    C  
ATOM   1322  O   GLN B 303      59.211  46.338  36.621  1.00 38.56      B    O  
ATOM   1323  CB  GLN B 303      57.514  47.192  33.961  1.00 40.53      B    C  
ATOM   1324  CG  GLN B 303      56.787  46.361  32.924  1.00 44.44      B    C  
ATOM   1325  CD  GLN B 303      57.431  45.014  32.737  1.00 47.42      B    C  
ATOM   1326  OE1 GLN B 303      58.457  44.905  32.093  1.00 52.26      B    O  
ATOM   1327  NE2 GLN B 303      56.847  43.987  33.312  1.00 49.02      B    N  
ATOM   1328  N   ASN B 304      58.292  48.374  36.822  1.00 41.12      B    N  
ATOM   1329  CA  ASN B 304      59.341  48.838  37.713  1.00 41.11      B    C  
ATOM   1330  C   ASN B 304      59.233  48.204  39.100  1.00 39.76      B    C  
ATOM   1331  O   ASN B 304      60.253  47.820  39.689  1.00 38.99      B    O  
ATOM   1332  CB  ASN B 304      59.320  50.364  37.794  1.00 44.54      B    C  
ATOM   1333  CG  ASN B 304      60.642  50.931  38.271  1.00 48.16      B    C  
ATOM   1334  OD1 ASN B 304      60.826  51.183  39.456  1.00 52.01      B    O  
ATOM   1335  ND2 ASN B 304      61.576  51.120  37.350  1.00 50.58      B    N  
ATOM   1336  N   TRP B 305      58.010  48.086  39.620  1.00 38.30      B    N  
ATOM   1337  CA  TRP B 305      57.805  47.456  40.929  1.00 37.21      B    C  
ATOM   1338  C   TRP B 305      58.305  46.021  40.844  1.00 37.02      B    C  
ATOM   1339  O   TRP B 305      58.996  45.530  41.741  1.00 37.90      B    O  
ATOM   1340  CB  TRP B 305      56.321  47.435  41.318  1.00 36.47      B    C  
ATOM   1341  CG  TRP B 305      55.810  48.708  41.907  1.00 38.16      B    C  
ATOM   1342  CD1 TRP B 305      55.980  49.960  41.402  1.00 38.04      B    C  
ATOM   1343  CD2 TRP B 305      55.016  48.859  43.100  1.00 40.28      B    C  
ATOM   1344  NE1 TRP B 305      55.346  50.882  42.195  1.00 40.23      B    N  
ATOM   1345  CE2 TRP B 305      54.748  50.238  43.247  1.00 40.15      B    C  
ATOM   1346  CE3 TRP B 305      54.507  47.964  44.060  1.00 41.12      B    C  
ATOM   1347  CZ2 TRP B 305      53.994  50.755  44.314  1.00 41.09      B    C  
ATOM   1348  CZ3 TRP B 305      53.751  48.479  45.130  1.00 43.16      B    C  
ATOM   1349  CH2 TRP B 305      53.507  49.862  45.245  1.00 42.71      B    C  
ATOM   1350  N   ASN B 306      57.938  45.351  39.755  1.00 35.95      B    N  
ATOM   1351  CA  ASN B 306      58.327  43.970  39.522  1.00 35.57      B    C  
ATOM   1352  C   ASN B 306      59.834  43.908  39.546  1.00 35.02      B    C  
ATOM   1353  O   ASN B 306      60.416  43.063  40.226  1.00 34.48      B    O  
ATOM   1354  CB  ASN B 306      57.797  43.491  38.162  1.00 39.26      B    C  
ATOM   1355  CG  ASN B 306      58.068  42.010  37.903  1.00 42.16      B    C  
ATOM   1356  OD1 ASN B 306      57.971  41.182  38.796  1.00 46.00      B    O  
ATOM   1357  ND2 ASN B 306      58.377  41.678  36.672  1.00 43.67      B    N  
ATOM   1358  N   LYS B 307      60.471  44.813  38.810  1.00 34.12      B    N  
ATOM   1359  CA  LYS B 307      61.926  44.834  38.769  1.00 34.85      B    C  
ATOM   1360  C   LYS B 307      62.516  45.137  40.157  1.00 34.10      B    C  
ATOM   1361  O   LYS B 307      63.417  44.441  40.627  1.00 33.73      B    O  
ATOM   1362  CB  LYS B 307      62.427  45.856  37.731  1.00 35.91      B    C  
ATOM   1363  CG  LYS B 307      63.956  45.974  37.668  1.00 37.20      B    C  
ATOM   1364  CD  LYS B 307      64.413  47.350  37.158  1.00 39.12      B    C  
ATOM   1365  CE  LYS B 307      64.944  47.274  35.728  1.00 41.23      B    C  
ATOM   1366  NZ  LYS B 307      63.953  46.600  34.817  1.00 42.01      B    N  
ATOM   1367  N   ILE B 308      62.005  46.156  40.834  1.00 33.28      B    N  
ATOM   1368  CA  ILE B 308      62.550  46.482  42.147  1.00 33.11      B    C  
ATOM   1369  C   ILE B 308      62.485  45.324  43.130  1.00 34.61      B    C  
ATOM   1370  O   ILE B 308      63.451  45.053  43.835  1.00 35.95      B    O  
ATOM   1371  CB  ILE B 308      61.833  47.704  42.766  1.00 33.03      B    C  
ATOM   1372  CG1 ILE B 308      62.198  48.952  41.952  1.00 32.03      B    C  
ATOM   1373  CG2 ILE B 308      62.223  47.870  44.234  1.00 31.44      B    C  
ATOM   1374  CD1 ILE B 308      61.429  50.178  42.313  1.00 32.36      B    C  
ATOM   1375  N   ILE B 309      61.353  44.628  43.168  1.00 35.72      B    N  
ATOM   1376  CA  ILE B 309      61.179  43.523  44.109  1.00 34.58      B    C  
ATOM   1377  C   ILE B 309      61.978  42.266  43.779  1.00 35.80      B    C  
ATOM   1378  O   ILE B 309      62.545  41.615  44.677  1.00 36.17      B    O  
ATOM   1379  CB  ILE B 309      59.693  43.156  44.232  1.00 33.99      B    C  
ATOM   1380  CG1 ILE B 309      58.934  44.343  44.833  1.00 32.78      B    C  
ATOM   1381  CG2 ILE B 309      59.524  41.894  45.068  1.00 30.42      B    C  
ATOM   1382  CD1 ILE B 309      57.470  44.076  45.100  1.00 34.49      B    C  
ATOM   1383  N   ARG B 310      62.023  41.918  42.496  1.00 34.54      B    N  
ATOM   1384  CA  ARG B 310      62.752  40.725  42.079  1.00 33.81      B    C  
ATOM   1385  C   ARG B 310      64.259  40.932  42.190  1.00 32.69      B    C  
ATOM   1386  O   ARG B 310      65.046  40.000  42.012  1.00 30.72      B    O  
ATOM   1387  CB  ARG B 310      62.350  40.358  40.650  1.00 32.72      B    C  
ATOM   1388  CG  ARG B 310      60.867  40.242  40.521  1.00 36.95      B    C  
ATOM   1389  CD  ARG B 310      60.456  38.959  39.879  1.00 39.55      B    C  
ATOM   1390  NE  ARG B 310      60.377  39.171  38.454  1.00 41.83      B    N  
ATOM   1391  CZ  ARG B 310      61.148  38.596  37.540  1.00 43.08      B    C  
ATOM   1392  NH1 ARG B 310      62.101  37.720  37.834  1.00 42.72      B    N  
ATOM   1393  NH2 ARG B 310      60.980  38.957  36.294  1.00 43.18      B    N  
ATOM   1394  N   LYS B 311      64.649  42.165  42.496  1.00 32.33      B    N  
ATOM   1395  CA  LYS B 311      66.058  42.507  42.624  1.00 34.53      B    C  
ATOM   1396  C   LYS B 311      66.566  42.176  44.009  1.00 35.11      B    C  
ATOM   1397  O   LYS B 311      67.768  42.072  44.221  1.00 35.20      B    O  
ATOM   1398  CB  LYS B 311      66.290  44.004  42.345  1.00 36.06      B    C  
ATOM   1399  CG  LYS B 311      67.676  44.513  42.803  1.00 40.61      B    C  
ATOM   1400  CD  LYS B 311      68.118  45.871  42.167  1.00 44.78      B    C  
ATOM   1401  CE  LYS B 311      68.319  45.719  40.627  1.00 46.45      B    C  
ATOM   1402  NZ  LYS B 311      69.030  46.855  39.964  1.00 45.95      B    N  
ATOM   1403  N   SER B 312      65.641  41.980  44.941  1.00 36.33      B    N  
ATOM   1404  CA  SER B 312      65.999  41.700  46.327  1.00 39.12      B    C  
ATOM   1405  C   SER B 312      66.150  40.231  46.736  1.00 38.78      B    C  
ATOM   1406  O   SER B 312      65.339  39.384  46.372  1.00 38.39      B    O  
ATOM   1407  CB  SER B 312      64.974  42.375  47.256  1.00 41.08      B    C  
ATOM   1408  OG  SER B 312      65.273  42.151  48.630  1.00 43.11      B    O  
ATOM   1409  N   THR B 313      67.195  39.940  47.505  1.00 37.86      B    N  
ATOM   1410  CA  THR B 313      67.407  38.586  48.000  1.00 38.21      B    C  
ATOM   1411  C   THR B 313      66.992  38.563  49.457  1.00 37.11      B    C  
ATOM   1412  O   THR B 313      66.523  37.542  49.957  1.00 36.88      B    O  
ATOM   1413  CB  THR B 313      68.881  38.147  47.885  1.00 39.16      B    C  
ATOM   1414  OG1 THR B 313      69.111  37.617  46.572  1.00 41.15      B    O  
ATOM   1415  CG2 THR B 313      69.223  37.084  48.931  1.00 38.01      B    C  
ATOM   1416  N   SER B 314      67.175  39.704  50.119  1.00 36.65      B    N  
ATOM   1417  CA  SER B 314      66.822  39.881  51.527  1.00 35.15      B    C  
ATOM   1418  C   SER B 314      65.343  39.665  51.719  1.00 35.08      B    C  
ATOM   1419  O   SER B 314      64.922  38.951  52.623  1.00 35.96      B    O  
ATOM   1420  CB  SER B 314      67.152  41.294  51.996  1.00 34.88      B    C  
ATOM   1421  OG  SER B 314      68.528  41.438  52.270  1.00 39.11      B    O  
ATOM   1422  N   LEU B 315      64.559  40.306  50.861  1.00 34.65      B    N  
ATOM   1423  CA  LEU B 315      63.114  40.213  50.923  1.00 34.58      B    C  
ATOM   1424  C   LEU B 315      62.678  38.781  51.235  1.00 35.42      B    C  
ATOM   1425  O   LEU B 315      62.007  38.529  52.244  1.00 36.77      B    O  
ATOM   1426  CB  LEU B 315      62.514  40.671  49.593  1.00 32.42      B    C  
ATOM   1427  CG  LEU B 315      61.053  41.099  49.590  1.00 31.58      B    C  
ATOM   1428  CD1 LEU B 315      60.906  42.352  50.433  1.00 29.63      B    C  
ATOM   1429  CD2 LEU B 315      60.603  41.378  48.168  1.00 32.31      B    C  
ATOM   1430  N   TRP B 316      63.086  37.845  50.383  1.00 34.72      B    N  
ATOM   1431  CA  TRP B 316      62.711  36.447  50.560  1.00 34.82      B    C  
ATOM   1432  C   TRP B 316      63.494  35.696  51.635  1.00 34.11      B    C  
ATOM   1433  O   TRP B 316      62.930  34.844  52.337  1.00 34.05      B    O  
ATOM   1434  CB  TRP B 316      62.792  35.722  49.211  1.00 34.44      B    C  
ATOM   1435  CG  TRP B 316      62.000  36.451  48.189  1.00 34.27      B    C  
ATOM   1436  CD1 TRP B 316      62.475  37.326  47.263  1.00 33.49      B    C  
ATOM   1437  CD2 TRP B 316      60.571  36.517  48.108  1.00 34.74      B    C  
ATOM   1438  NE1 TRP B 316      61.432  37.942  46.614  1.00 32.99      B    N  
ATOM   1439  CE2 TRP B 316      60.254  37.463  47.113  1.00 33.78      B    C  
ATOM   1440  CE3 TRP B 316      59.531  35.872  48.784  1.00 35.79      B    C  
ATOM   1441  CZ2 TRP B 316      58.938  37.787  46.784  1.00 34.33      B    C  
ATOM   1442  CZ3 TRP B 316      58.224  36.192  48.459  1.00 36.52      B    C  
ATOM   1443  CH2 TRP B 316      57.938  37.142  47.462  1.00 36.58      B    C  
ATOM   1444  N   LYS B 317      64.781  35.994  51.774  1.00 32.57      B    N  
ATOM   1445  CA  LYS B 317      65.560  35.331  52.807  1.00 33.20      B    C  
ATOM   1446  C   LYS B 317      64.842  35.560  54.141  1.00 33.58      B    C  
ATOM   1447  O   LYS B 317      64.590  34.605  54.898  1.00 32.27      B    O  
ATOM   1448  CB  LYS B 317      66.985  35.891  52.866  1.00 34.88      B    C  
ATOM   1449  CG  LYS B 317      67.816  35.330  54.017  1.00 37.18      B    C  
ATOM   1450  CD  LYS B 317      69.189  35.991  54.089  1.00 39.01      B    C  
ATOM   1451  CE  LYS B 317      69.697  36.099  55.533  1.00 41.34      B    C  
ATOM   1452  NZ  LYS B 317      68.866  37.015  56.393  1.00 39.90      B    N  
ATOM   1453  N   LYS B 318      64.494  36.819  54.418  1.00 31.26      B    N  
ATOM   1454  CA  LYS B 318      63.795  37.144  55.653  1.00 30.83      B    C  
ATOM   1455  C   LYS B 318      62.552  36.282  55.803  1.00 31.38      B    C  
ATOM   1456  O   LYS B 318      62.427  35.549  56.782  1.00 32.06      B    O  
ATOM   1457  CB  LYS B 318      63.406  38.627  55.695  1.00 31.61      B    C  
ATOM   1458  CG  LYS B 318      64.530  39.576  56.153  1.00 30.86      B    C  
ATOM   1459  CD  LYS B 318      64.070  41.020  56.147  1.00 32.32      B    C  
ATOM   1460  CE  LYS B 318      65.185  41.973  56.579  1.00 34.58      B    C  
ATOM   1461  NZ  LYS B 318      66.344  41.977  55.639  1.00 34.90      B    N  
ATOM   1462  N   LEU B 319      61.646  36.359  54.829  1.00 31.32      B    N  
ATOM   1463  CA  LEU B 319      60.404  35.580  54.855  1.00 30.23      B    C  
ATOM   1464  C   LEU B 319      60.641  34.107  55.179  1.00 30.08      B    C  
ATOM   1465  O   LEU B 319      60.085  33.573  56.141  1.00 30.61      B    O  
ATOM   1466  CB  LEU B 319      59.678  35.714  53.517  1.00 27.73      B    C  
ATOM   1467  CG  LEU B 319      58.971  37.049  53.331  1.00 27.99      B    C  
ATOM   1468  CD1 LEU B 319      58.673  37.300  51.859  1.00 30.73      B    C  
ATOM   1469  CD2 LEU B 319      57.694  37.047  54.143  1.00 27.43      B    C  
ATOM   1470  N   LEU B 320      61.467  33.451  54.372  1.00 29.97      B    N  
ATOM   1471  CA  LEU B 320      61.791  32.041  54.585  1.00 30.05      B    C  
ATOM   1472  C   LEU B 320      62.097  31.739  56.063  1.00 29.65      B    C  
ATOM   1473  O   LEU B 320      61.629  30.742  56.633  1.00 29.69      B    O  
ATOM   1474  CB  LEU B 320      62.994  31.660  53.713  1.00 26.82      B    C  
ATOM   1475  CG  LEU B 320      62.683  31.407  52.247  1.00 27.07      B    C  
ATOM   1476  CD1 LEU B 320      63.968  31.395  51.434  1.00 26.45      B    C  
ATOM   1477  CD2 LEU B 320      61.941  30.088  52.128  1.00 24.90      B    C  
ATOM   1478  N   ILE B 321      62.898  32.615  56.661  1.00 29.20      B    N  
ATOM   1479  CA  ILE B 321      63.300  32.502  58.055  1.00 28.45      B    C  
ATOM   1480  C   ILE B 321      62.125  32.836  58.982  1.00 27.29      B    C  
ATOM   1481  O   ILE B 321      61.927  32.175  59.987  1.00 28.02      B    O  
ATOM   1482  CB  ILE B 321      64.509  33.450  58.345  1.00 28.91      B    C  
ATOM   1483  CG1 ILE B 321      65.700  33.039  57.468  1.00 25.63      B    C  
ATOM   1484  CG2 ILE B 321      64.879  33.420  59.833  1.00 26.69      B    C  
ATOM   1485  CD1 ILE B 321      66.976  33.783  57.779  1.00 26.13      B    C  
ATOM   1486  N   SER B 322      61.349  33.856  58.636  1.00 27.32      B    N  
ATOM   1487  CA  SER B 322      60.198  34.246  59.437  1.00 27.96      B    C  
ATOM   1488  C   SER B 322      59.268  33.060  59.593  1.00 28.72      B    C  
ATOM   1489  O   SER B 322      58.749  32.809  60.680  1.00 30.99      B    O  
ATOM   1490  CB  SER B 322      59.410  35.363  58.755  1.00 25.49      B    C  
ATOM   1491  OG  SER B 322      60.272  36.396  58.349  1.00 30.45      B    O  
ATOM   1492  N   GLU B 323      59.053  32.343  58.496  1.00 27.62      B    N  
ATOM   1493  CA  GLU B 323      58.158  31.199  58.482  1.00 28.24      B    C  
ATOM   1494  C   GLU B 323      58.808  29.896  58.910  1.00 27.51      B    C  
ATOM   1495  O   GLU B 323      58.155  28.846  58.949  1.00 25.95      B    O  
ATOM   1496  CB  GLU B 323      57.581  31.042  57.086  1.00 28.89      B    C  
ATOM   1497  CG  GLU B 323      56.758  32.235  56.661  1.00 30.42      B    C  
ATOM   1498  CD  GLU B 323      55.487  32.368  57.469  1.00 31.03      B    C  
ATOM   1499  OE1 GLU B 323      55.034  31.351  58.035  1.00 29.10      B    O  
ATOM   1500  OE2 GLU B 323      54.924  33.481  57.520  1.00 32.03      B    O  
ATOM   1501  N   ASN B 324      60.097  29.973  59.224  1.00 26.45      B    N  
ATOM   1502  CA  ASN B 324      60.865  28.809  59.646  1.00 28.02      B    C  
ATOM   1503  C   ASN B 324      60.956  27.744  58.541  1.00 29.33      B    C  
ATOM   1504  O   ASN B 324      60.684  26.572  58.784  1.00 29.38      B    O  
ATOM   1505  CB  ASN B 324      60.251  28.174  60.907  1.00 28.39      B    C  
ATOM   1506  CG  ASN B 324      60.045  29.174  62.040  1.00 30.46      B    C  
ATOM   1507  OD1 ASN B 324      60.999  29.724  62.605  1.00 31.96      B    O  
ATOM   1508  ND2 ASN B 324      58.790  29.412  62.375  1.00 29.23      B    N  
ATOM   1509  N   PHE B 325      61.320  28.136  57.324  1.00 28.46      B    N  
ATOM   1510  CA  PHE B 325      61.456  27.145  56.272  1.00 27.99      B    C  
ATOM   1511  C   PHE B 325      62.937  26.831  56.143  1.00 28.66      B    C  
ATOM   1512  O   PHE B 325      63.334  25.824  55.544  1.00 30.08      B    O  
ATOM   1513  CB  PHE B 325      60.872  27.678  54.967  1.00 27.10      B    C  
ATOM   1514  CG  PHE B 325      59.364  27.760  54.974  1.00 25.62      B    C  
ATOM   1515  CD1 PHE B 325      58.704  28.825  54.367  1.00 24.49      B    C  
ATOM   1516  CD2 PHE B 325      58.606  26.795  55.624  1.00 22.25      B    C  
ATOM   1517  CE1 PHE B 325      57.314  28.925  54.421  1.00 21.94      B    C  
ATOM   1518  CE2 PHE B 325      57.219  26.896  55.673  1.00 20.23      B    C  
ATOM   1519  CZ  PHE B 325      56.578  27.961  55.077  1.00 18.23      B    C  
ATOM   1520  N   VAL B 326      63.744  27.703  56.744  1.00 28.07      B    N  
ATOM   1521  CA  VAL B 326      65.200  27.582  56.759  1.00 28.76      B    C  
ATOM   1522  C   VAL B 326      65.728  28.389  57.948  1.00 29.95      B    C  
ATOM   1523  O   VAL B 326      65.040  29.263  58.475  1.00 29.94      B    O  
ATOM   1524  CB  VAL B 326      65.836  28.152  55.459  1.00 27.49      B    C  
ATOM   1525  CG1 VAL B 326      65.788  29.680  55.468  1.00 25.18      B    C  
ATOM   1526  CG2 VAL B 326      67.264  27.687  55.336  1.00 25.96      B    C  
ATOM   1527  N   SER B 327      66.948  28.105  58.373  1.00 31.73      B    N  
ATOM   1528  CA  SER B 327      67.525  28.842  59.494  1.00 35.27      B    C  
ATOM   1529  C   SER B 327      68.789  29.461  58.965  1.00 37.78      B    C  
ATOM   1530  O   SER B 327      69.297  29.043  57.923  1.00 40.13      B    O  
ATOM   1531  CB  SER B 327      67.900  27.910  60.644  1.00 35.20      B    C  
ATOM   1532  OG  SER B 327      69.127  27.246  60.376  1.00 38.35      B    O  
ATOM   1533  N   PRO B 328      69.322  30.463  59.667  1.00 38.75      B    N  
ATOM   1534  CA  PRO B 328      70.553  31.080  59.177  1.00 39.07      B    C  
ATOM   1535  C   PRO B 328      71.621  30.042  58.779  1.00 40.73      B    C  
ATOM   1536  O   PRO B 328      72.272  30.176  57.739  1.00 41.44      B    O  
ATOM   1537  CB  PRO B 328      70.975  31.954  60.350  1.00 38.05      B    C  
ATOM   1538  CG  PRO B 328      69.640  32.429  60.884  1.00 38.18      B    C  
ATOM   1539  CD  PRO B 328      68.810  31.162  60.862  1.00 38.42      B    C  
ATOM   1540  N   LYS B 329      71.790  28.998  59.585  1.00 41.85      B    N  
ATOM   1541  CA  LYS B 329      72.793  27.974  59.287  1.00 43.64      B    C  
ATOM   1542  C   LYS B 329      72.462  27.183  58.029  1.00 43.35      B    C  
ATOM   1543  O   LYS B 329      73.347  26.848  57.232  1.00 43.42      B    O  
ATOM   1544  CB  LYS B 329      72.932  26.986  60.457  1.00 44.88      B    C  
ATOM   1545  CG  LYS B 329      73.308  27.617  61.778  1.00 46.67      B    C  
ATOM   1546  CD  LYS B 329      74.622  28.364  61.679  1.00 48.70      B    C  
ATOM   1547  CE  LYS B 329      74.832  29.237  62.903  1.00 50.55      B    C  
ATOM   1548  NZ  LYS B 329      73.669  30.151  63.095  1.00 52.20      B    N  
ATOM   1549  N   GLY B 330      71.183  26.870  57.862  1.00 42.69      B    N  
ATOM   1550  CA  GLY B 330      70.770  26.096  56.709  1.00 41.56      B    C  
ATOM   1551  C   GLY B 330      70.592  26.905  55.444  1.00 41.16      B    C  
ATOM   1552  O   GLY B 330      70.365  26.334  54.378  1.00 40.45      B    O  
ATOM   1553  N   PHE B 331      70.701  28.228  55.543  1.00 40.24      B    N  
ATOM   1554  CA  PHE B 331      70.512  29.054  54.367  1.00 40.28      B    C  
ATOM   1555  C   PHE B 331      71.332  28.587  53.189  1.00 40.38      B    C  
ATOM   1556  O   PHE B 331      70.794  28.013  52.247  1.00 41.14      B    O  
ATOM   1557  CB  PHE B 331      70.852  30.515  54.624  1.00 41.01      B    C  
ATOM   1558  CG  PHE B 331      70.466  31.419  53.484  1.00 44.09      B    C  
ATOM   1559  CD1 PHE B 331      69.121  31.691  53.227  1.00 44.65      B    C  
ATOM   1560  CD2 PHE B 331      71.436  31.982  52.649  1.00 45.96      B    C  
ATOM   1561  CE1 PHE B 331      68.743  32.509  52.159  1.00 46.35      B    C  
ATOM   1562  CE2 PHE B 331      71.067  32.809  51.565  1.00 46.33      B    C  
ATOM   1563  CZ  PHE B 331      69.718  33.071  51.325  1.00 46.53      B    C  
ATOM   1564  N   ASN B 332      72.636  28.838  53.244  1.00 41.45      B    N  
ATOM   1565  CA  ASN B 332      73.534  28.471  52.154  1.00 41.41      B    C  
ATOM   1566  C   ASN B 332      73.222  27.126  51.505  1.00 40.86      B    C  
ATOM   1567  O   ASN B 332      73.087  27.044  50.286  1.00 41.17      B    O  
ATOM   1568  CB  ASN B 332      74.986  28.521  52.623  1.00 40.95      B    C  
ATOM   1569  CG  ASN B 332      75.438  29.932  52.930  1.00 42.25      B    C  
ATOM   1570  OD1 ASN B 332      74.879  30.893  52.406  1.00 43.14      B    O  
ATOM   1571  ND2 ASN B 332      76.459  30.068  53.769  1.00 43.18      B    N  
ATOM   1572  N   SER B 333      73.095  26.077  52.301  1.00 39.99      B    N  
ATOM   1573  CA  SER B 333      72.781  24.783  51.730  1.00 39.96      B    C  
ATOM   1574  C   SER B 333      71.466  24.847  50.943  1.00 40.82      B    C  
ATOM   1575  O   SER B 333      71.332  24.222  49.887  1.00 41.45      B    O  
ATOM   1576  CB  SER B 333      72.673  23.731  52.821  1.00 37.69      B    C  
ATOM   1577  OG  SER B 333      72.215  22.518  52.256  1.00 40.47      B    O  
ATOM   1578  N   LEU B 334      70.497  25.597  51.465  1.00 40.08      B    N  
ATOM   1579  CA  LEU B 334      69.211  25.746  50.795  1.00 37.93      B    C  
ATOM   1580  C   LEU B 334      69.489  26.259  49.390  1.00 38.27      B    C  
ATOM   1581  O   LEU B 334      69.027  25.680  48.398  1.00 37.44      B    O  
ATOM   1582  CB  LEU B 334      68.322  26.749  51.538  1.00 35.36      B    C  
ATOM   1583  CG  LEU B 334      67.032  27.115  50.795  1.00 34.32      B    C  
ATOM   1584  CD1 LEU B 334      66.082  25.916  50.764  1.00 30.58      B    C  
ATOM   1585  CD2 LEU B 334      66.382  28.312  51.461  1.00 32.26      B    C  
ATOM   1586  N   ASN B 335      70.256  27.347  49.321  1.00 37.58      B    N  
ATOM   1587  CA  ASN B 335      70.624  27.966  48.054  1.00 37.39      B    C  
ATOM   1588  C   ASN B 335      71.237  26.988  47.064  1.00 37.80      B    C  
ATOM   1589  O   ASN B 335      70.801  26.896  45.916  1.00 38.87      B    O  
ATOM   1590  CB  ASN B 335      71.593  29.097  48.311  1.00 35.54      B    C  
ATOM   1591  CG  ASN B 335      70.949  30.429  48.158  1.00 37.22      B    C  
ATOM   1592  OD1 ASN B 335      71.509  31.448  48.540  1.00 39.45      B    O  
ATOM   1593  ND2 ASN B 335      69.755  30.440  47.584  1.00 37.72      B    N  
ATOM   1594  N   LEU B 336      72.250  26.257  47.511  1.00 37.72      B    N  
ATOM   1595  CA  LEU B 336      72.906  25.289  46.652  1.00 38.72      B    C  
ATOM   1596  C   LEU B 336      71.849  24.345  46.073  1.00 38.24      B    C  
ATOM   1597  O   LEU B 336      71.774  24.158  44.866  1.00 40.09      B    O  
ATOM   1598  CB  LEU B 336      73.958  24.500  47.447  1.00 39.15      B    C  
ATOM   1599  CG  LEU B 336      74.959  23.687  46.618  1.00 39.35      B    C  
ATOM   1600  CD1 LEU B 336      75.934  24.620  45.920  1.00 38.40      B    C  
ATOM   1601  CD2 LEU B 336      75.710  22.742  47.520  1.00 38.88      B    C  
ATOM   1602  N   LYS B 337      71.007  23.778  46.930  1.00 37.41      B    N  
ATOM   1603  CA  LYS B 337      69.976  22.856  46.466  1.00 36.19      B    C  
ATOM   1604  C   LYS B 337      68.983  23.479  45.476  1.00 34.77      B    C  
ATOM   1605  O   LYS B 337      68.542  22.807  44.542  1.00 33.07      B    O  
ATOM   1606  CB  LYS B 337      69.219  22.273  47.661  1.00 35.39      B    C  
ATOM   1607  CG  LYS B 337      68.120  21.300  47.278  1.00 37.86      B    C  
ATOM   1608  CD  LYS B 337      67.336  20.801  48.505  1.00 42.14      B    C  
ATOM   1609  CE  LYS B 337      66.476  21.903  49.155  1.00 43.70      B    C  
ATOM   1610  NZ  LYS B 337      65.647  21.421  50.305  1.00 42.14      B    N  
ATOM   1611  N   LEU B 338      68.629  24.749  45.689  1.00 33.74      B    N  
ATOM   1612  CA  LEU B 338      67.684  25.447  44.812  1.00 31.89      B    C  
ATOM   1613  C   LEU B 338      68.324  25.713  43.449  1.00 32.49      B    C  
ATOM   1614  O   LEU B 338      67.662  25.660  42.409  1.00 32.11      B    O  
ATOM   1615  CB  LEU B 338      67.232  26.770  45.452  1.00 29.90      B    C  
ATOM   1616  CG  LEU B 338      66.115  26.748  46.519  1.00 28.12      B    C  
ATOM   1617  CD1 LEU B 338      65.923  28.148  47.132  1.00 25.64      B    C  
ATOM   1618  CD2 LEU B 338      64.813  26.276  45.886  1.00 25.23      B    C  
ATOM   1619  N   SER B 339      69.624  25.979  43.470  1.00 32.69      B    N  
ATOM   1620  CA  SER B 339      70.384  26.241  42.261  1.00 33.01      B    C  
ATOM   1621  C   SER B 339      70.542  24.961  41.443  1.00 34.16      B    C  
ATOM   1622  O   SER B 339      70.600  25.001  40.207  1.00 35.55      B    O  
ATOM   1623  CB  SER B 339      71.766  26.783  42.622  1.00 31.33      B    C  
ATOM   1624  OG  SER B 339      72.559  26.982  41.467  1.00 31.30      B    O  
ATOM   1625  N   GLN B 340      70.624  23.826  42.123  1.00 33.08      B    N  
ATOM   1626  CA  GLN B 340      70.768  22.569  41.419  1.00 34.45      B    C  
ATOM   1627  C   GLN B 340      69.432  22.251  40.801  1.00 35.68      B    C  
ATOM   1628  O   GLN B 340      69.359  21.668  39.720  1.00 36.85      B    O  
ATOM   1629  CB  GLN B 340      71.161  21.459  42.379  1.00 36.49      B    C  
ATOM   1630  CG  GLN B 340      72.246  21.881  43.345  1.00 39.61      B    C  
ATOM   1631  CD  GLN B 340      72.806  20.728  44.130  1.00 39.34      B    C  
ATOM   1632  OE1 GLN B 340      72.056  19.897  44.665  1.00 41.65      B    O  
ATOM   1633  NE2 GLN B 340      74.132  20.667  44.216  1.00 37.09      B    N  
ATOM   1634  N   LYS B 341      68.377  22.661  41.499  1.00 36.00      B    N  
ATOM   1635  CA  LYS B 341      67.004  22.443  41.070  1.00 36.33      B    C  
ATOM   1636  C   LYS B 341      66.623  23.388  39.924  1.00 37.19      B    C  
ATOM   1637  O   LYS B 341      65.973  22.983  38.964  1.00 37.34      B    O  
ATOM   1638  CB  LYS B 341      66.072  22.656  42.264  1.00 37.20      B    C  
ATOM   1639  CG  LYS B 341      64.613  22.268  42.059  1.00 39.11      B    C  
ATOM   1640  CD  LYS B 341      63.791  22.685  43.284  1.00 40.86      B    C  
ATOM   1641  CE  LYS B 341      62.309  22.304  43.173  1.00 43.05      B    C  
ATOM   1642  NZ  LYS B 341      61.480  22.987  44.234  1.00 40.73      B    N  
ATOM   1643  N   TYR B 342      67.049  24.641  40.025  1.00 37.09      B    N  
ATOM   1644  CA  TYR B 342      66.740  25.648  39.013  1.00 37.10      B    C  
ATOM   1645  C   TYR B 342      68.008  26.345  38.512  1.00 36.38      B    C  
ATOM   1646  O   TYR B 342      68.338  27.433  38.971  1.00 36.88      B    O  
ATOM   1647  CB  TYR B 342      65.805  26.687  39.618  1.00 39.09      B    C  
ATOM   1648  CG  TYR B 342      64.561  26.096  40.241  1.00 41.55      B    C  
ATOM   1649  CD1 TYR B 342      63.549  25.572  39.444  1.00 42.47      B    C  
ATOM   1650  CD2 TYR B 342      64.390  26.069  41.632  1.00 42.26      B    C  
ATOM   1651  CE1 TYR B 342      62.397  25.040  40.005  1.00 44.13      B    C  
ATOM   1652  CE2 TYR B 342      63.236  25.537  42.208  1.00 41.87      B    C  
ATOM   1653  CZ  TYR B 342      62.242  25.021  41.386  1.00 43.97      B    C  
ATOM   1654  OH  TYR B 342      61.097  24.461  41.916  1.00 43.51      B    O  
ATOM   1655  N   PRO B 343      68.730  25.737  37.552  1.00 35.43      B    N  
ATOM   1656  CA  PRO B 343      69.956  26.353  37.036  1.00 34.76      B    C  
ATOM   1657  C   PRO B 343      69.757  27.738  36.419  1.00 35.45      B    C  
ATOM   1658  O   PRO B 343      70.452  28.694  36.762  1.00 35.88      B    O  
ATOM   1659  CB  PRO B 343      70.441  25.338  35.998  1.00 32.28      B    C  
ATOM   1660  CG  PRO B 343      69.858  24.067  36.449  1.00 30.65      B    C  
ATOM   1661  CD  PRO B 343      68.478  24.459  36.866  1.00 34.91      B    C  
ATOM   1662  N   LYS B 344      68.792  27.832  35.515  1.00 36.13      B    N  
ATOM   1663  CA  LYS B 344      68.521  29.071  34.806  1.00 37.44      B    C  
ATOM   1664  C   LYS B 344      67.800  30.171  35.585  1.00 38.17      B    C  
ATOM   1665  O   LYS B 344      67.473  31.218  35.017  1.00 37.45      B    O  
ATOM   1666  CB  LYS B 344      67.756  28.752  33.526  1.00 37.66      B    C  
ATOM   1667  CG  LYS B 344      68.435  27.694  32.661  1.00 36.70      B    C  
ATOM   1668  CD  LYS B 344      67.507  27.258  31.543  1.00 37.05      B    C  
ATOM   1669  CE  LYS B 344      67.957  25.959  30.921  1.00 37.23      B    C  
ATOM   1670  NZ  LYS B 344      66.816  25.293  30.248  1.00 39.91      B    N  
ATOM   1671  N   LEU B 345      67.549  29.939  36.872  1.00 37.44      B    N  
ATOM   1672  CA  LEU B 345      66.897  30.940  37.712  1.00 34.97      B    C  
ATOM   1673  C   LEU B 345      67.935  31.706  38.504  1.00 36.09      B    C  
ATOM   1674  O   LEU B 345      69.066  31.257  38.672  1.00 35.77      B    O  
ATOM   1675  CB  LEU B 345      65.938  30.295  38.695  1.00 32.11      B    C  
ATOM   1676  CG  LEU B 345      64.604  29.840  38.133  1.00 30.71      B    C  
ATOM   1677  CD1 LEU B 345      63.746  29.318  39.280  1.00 29.48      B    C  
ATOM   1678  CD2 LEU B 345      63.923  31.004  37.427  1.00 28.76      B    C  
ATOM   1679  N   SER B 346      67.537  32.869  38.999  1.00 38.28      B    N  
ATOM   1680  CA  SER B 346      68.432  33.716  39.789  1.00 38.76      B    C  
ATOM   1681  C   SER B 346      68.166  33.496  41.275  1.00 37.50      B    C  
ATOM   1682  O   SER B 346      67.111  32.994  41.666  1.00 38.11      B    O  
ATOM   1683  CB  SER B 346      68.204  35.192  39.452  1.00 37.41      B    C  
ATOM   1684  OG  SER B 346      66.888  35.578  39.810  1.00 38.29      B    O  
ATOM   1685  N   GLN B 347      69.120  33.885  42.104  1.00 36.48      B    N  
ATOM   1686  CA  GLN B 347      68.955  33.709  43.532  1.00 37.36      B    C  
ATOM   1687  C   GLN B 347      67.649  34.298  44.044  1.00 36.30      B    C  
ATOM   1688  O   GLN B 347      66.965  33.670  44.845  1.00 35.45      B    O  
ATOM   1689  CB  GLN B 347      70.110  34.344  44.278  1.00 37.93      B    C  
ATOM   1690  CG  GLN B 347      69.982  34.244  45.768  1.00 39.12      B    C  
ATOM   1691  CD  GLN B 347      71.162  34.865  46.445  1.00 41.48      B    C  
ATOM   1692  OE1 GLN B 347      71.403  36.068  46.314  1.00 43.65      B    O  
ATOM   1693  NE2 GLN B 347      71.928  34.051  47.157  1.00 42.85      B    N  
ATOM   1694  N   GLN B 348      67.309  35.501  43.584  1.00 35.40      B    N  
ATOM   1695  CA  GLN B 348      66.080  36.149  44.023  1.00 34.86      B    C  
ATOM   1696  C   GLN B 348      64.872  35.302  43.674  1.00 33.82      B    C  
ATOM   1697  O   GLN B 348      64.173  34.806  44.554  1.00 33.73      B    O  
ATOM   1698  CB  GLN B 348      65.901  37.529  43.383  1.00 34.91      B    C  
ATOM   1699  CG  GLN B 348      66.962  38.553  43.736  1.00 34.00      B    C  
ATOM   1700  CD  GLN B 348      68.203  38.438  42.874  1.00 33.29      B    C  
ATOM   1701  OE1 GLN B 348      68.985  39.377  42.781  1.00 34.56      B    O  
ATOM   1702  NE2 GLN B 348      68.390  37.290  42.243  1.00 31.78      B    N  
ATOM   1703  N   ASP B 349      64.628  35.147  42.379  1.00 33.24      B    N  
ATOM   1704  CA  ASP B 349      63.493  34.374  41.921  1.00 32.15      B    C  
ATOM   1705  C   ASP B 349      63.504  32.968  42.511  1.00 30.65      B    C  
ATOM   1706  O   ASP B 349      62.442  32.394  42.759  1.00 30.23      B    O  
ATOM   1707  CB  ASP B 349      63.462  34.343  40.387  1.00 33.53      B    C  
ATOM   1708  CG  ASP B 349      63.198  35.724  39.782  1.00 36.83      B    C  
ATOM   1709  OD1 ASP B 349      62.223  36.394  40.208  1.00 35.84      B    O  
ATOM   1710  OD2 ASP B 349      63.963  36.140  38.878  1.00 39.04      B    O  
ATOM   1711  N   ARG B 350      64.690  32.423  42.762  1.00 28.04      B    N  
ATOM   1712  CA  ARG B 350      64.778  31.089  43.343  1.00 27.99      B    C  
ATOM   1713  C   ARG B 350      64.147  31.085  44.724  1.00 26.85      B    C  
ATOM   1714  O   ARG B 350      63.228  30.315  45.003  1.00 27.14      B    O  
ATOM   1715  CB  ARG B 350      66.233  30.638  43.465  1.00 30.32      B    C  
ATOM   1716  CG  ARG B 350      66.826  30.062  42.195  1.00 33.52      B    C  
ATOM   1717  CD  ARG B 350      68.295  29.697  42.395  1.00 35.56      B    C  
ATOM   1718  NE  ARG B 350      68.919  29.304  41.135  1.00 37.12      B    N  
ATOM   1719  CZ  ARG B 350      70.229  29.221  40.938  1.00 37.41      B    C  
ATOM   1720  NH1 ARG B 350      71.074  29.497  41.919  1.00 37.15      B    N  
ATOM   1721  NH2 ARG B 350      70.692  28.895  39.743  1.00 38.00      B    N  
ATOM   1722  N   LEU B 351      64.649  31.952  45.591  1.00 25.30      B    N  
ATOM   1723  CA  LEU B 351      64.127  32.042  46.939  1.00 24.62      B    C  
ATOM   1724  C   LEU B 351      62.613  32.254  46.953  1.00 26.68      B    C  
ATOM   1725  O   LEU B 351      61.907  31.677  47.795  1.00 26.70      B    O  
ATOM   1726  CB  LEU B 351      64.840  33.162  47.695  1.00 21.39      B    C  
ATOM   1727  CG  LEU B 351      66.259  32.770  48.106  1.00 21.23      B    C  
ATOM   1728  CD1 LEU B 351      66.907  33.886  48.878  1.00 22.79      B    C  
ATOM   1729  CD2 LEU B 351      66.218  31.515  48.958  1.00 21.73      B    C  
ATOM   1730  N   ARG B 352      62.111  33.059  46.018  1.00 25.64      B    N  
ATOM   1731  CA  ARG B 352      60.686  33.319  45.967  1.00 26.11      B    C  
ATOM   1732  C   ARG B 352      59.921  32.072  45.566  1.00 26.29      B    C  
ATOM   1733  O   ARG B 352      58.835  31.808  46.080  1.00 26.16      B    O  
ATOM   1734  CB  ARG B 352      60.378  34.461  44.999  1.00 28.23      B    C  
ATOM   1735  CG  ARG B 352      58.897  34.629  44.685  1.00 26.51      B    C  
ATOM   1736  CD  ARG B 352      58.637  35.998  44.104  1.00 30.33      B    C  
ATOM   1737  NE  ARG B 352      59.400  36.245  42.887  1.00 31.56      B    N  
ATOM   1738  CZ  ARG B 352      59.060  35.787  41.687  1.00 29.82      B    C  
ATOM   1739  NH1 ARG B 352      57.965  35.062  41.537  1.00 28.12      B    N  
ATOM   1740  NH2 ARG B 352      59.826  36.045  40.639  1.00 30.20      B    N  
ATOM   1741  N   LEU B 353      60.479  31.289  44.658  1.00 26.62      B    N  
ATOM   1742  CA  LEU B 353      59.786  30.079  44.228  1.00 28.22      B    C  
ATOM   1743  C   LEU B 353      59.689  29.145  45.443  1.00 29.24      B    C  
ATOM   1744  O   LEU B 353      58.630  28.574  45.732  1.00 28.62      B    O  
ATOM   1745  CB  LEU B 353      60.555  29.423  43.068  1.00 29.28      B    C  
ATOM   1746  CG  LEU B 353      59.889  28.348  42.197  1.00 31.50      B    C  
ATOM   1747  CD1 LEU B 353      59.715  27.044  42.973  1.00 32.68      B    C  
ATOM   1748  CD2 LEU B 353      58.547  28.864  41.711  1.00 32.98      B    C  
ATOM   1749  N   SER B 354      60.803  29.023  46.161  1.00 28.52      B    N  
ATOM   1750  CA  SER B 354      60.890  28.186  47.351  1.00 29.57      B    C  
ATOM   1751  C   SER B 354      59.869  28.617  48.410  1.00 30.39      B    C  
ATOM   1752  O   SER B 354      59.144  27.793  48.968  1.00 30.22      B    O  
ATOM   1753  CB  SER B 354      62.312  28.268  47.932  1.00 29.53      B    C  
ATOM   1754  OG  SER B 354      62.451  27.509  49.115  1.00 27.66      B    O  
ATOM   1755  N   PHE B 355      59.803  29.912  48.685  1.00 29.73      B    N  
ATOM   1756  CA  PHE B 355      58.870  30.381  49.678  1.00 29.01      B    C  
ATOM   1757  C   PHE B 355      57.442  30.099  49.262  1.00 29.79      B    C  
ATOM   1758  O   PHE B 355      56.692  29.481  50.007  1.00 30.90      B    O  
ATOM   1759  CB  PHE B 355      59.068  31.866  49.921  1.00 29.91      B    C  
ATOM   1760  CG  PHE B 355      58.138  32.429  50.937  1.00 30.50      B    C  
ATOM   1761  CD1 PHE B 355      56.870  32.852  50.574  1.00 29.71      B    C  
ATOM   1762  CD2 PHE B 355      58.514  32.496  52.275  1.00 33.17      B    C  
ATOM   1763  CE1 PHE B 355      55.986  33.333  51.532  1.00 31.33      B    C  
ATOM   1764  CE2 PHE B 355      57.635  32.976  53.246  1.00 31.68      B    C  
ATOM   1765  CZ  PHE B 355      56.369  33.395  52.870  1.00 31.69      B    C  
ATOM   1766  N   LEU B 356      57.060  30.544  48.069  1.00 30.90      B    N  
ATOM   1767  CA  LEU B 356      55.694  30.317  47.598  1.00 31.59      B    C  
ATOM   1768  C   LEU B 356      55.312  28.843  47.643  1.00 31.20      B    C  
ATOM   1769  O   LEU B 356      54.193  28.504  47.973  1.00 30.81      B    O  
ATOM   1770  CB  LEU B 356      55.508  30.864  46.172  1.00 32.04      B    C  
ATOM   1771  CG  LEU B 356      55.497  32.395  46.010  1.00 31.28      B    C  
ATOM   1772  CD1 LEU B 356      55.457  32.739  44.542  1.00 30.13      B    C  
ATOM   1773  CD2 LEU B 356      54.306  33.008  46.741  1.00 30.24      B    C  
ATOM   1774  N   GLU B 357      56.250  27.971  47.305  1.00 32.98      B    N  
ATOM   1775  CA  GLU B 357      56.013  26.538  47.327  1.00 33.13      B    C  
ATOM   1776  C   GLU B 357      55.852  26.055  48.777  1.00 33.82      B    C  
ATOM   1777  O   GLU B 357      55.010  25.210  49.067  1.00 35.07      B    O  
ATOM   1778  CB  GLU B 357      57.186  25.824  46.650  1.00 35.12      B    C  
ATOM   1779  CG  GLU B 357      57.194  24.315  46.818  1.00 39.93      B    C  
ATOM   1780  CD  GLU B 357      58.177  23.627  45.885  1.00 43.17      B    C  
ATOM   1781  OE1 GLU B 357      59.387  23.962  45.924  1.00 44.47      B    O  
ATOM   1782  OE2 GLU B 357      57.735  22.745  45.112  1.00 45.87      B    O  
ATOM   1783  N   ASN B 358      56.656  26.601  49.685  1.00 31.73      B    N  
ATOM   1784  CA  ASN B 358      56.596  26.225  51.086  1.00 30.14      B    C  
ATOM   1785  C   ASN B 358      55.374  26.760  51.821  1.00 31.61      B    C  
ATOM   1786  O   ASN B 358      54.661  26.004  52.474  1.00 32.97      B    O  
ATOM   1787  CB  ASN B 358      57.852  26.702  51.809  1.00 29.26      B    C  
ATOM   1788  CG  ASN B 358      58.940  25.643  51.844  1.00 30.75      B    C  
ATOM   1789  OD1 ASN B 358      60.111  25.937  51.635  1.00 29.80      B    O  
ATOM   1790  ND2 ASN B 358      58.555  24.401  52.120  1.00 32.01      B    N  
ATOM   1791  N   ILE B 359      55.126  28.060  51.723  1.00 31.16      B    N  
ATOM   1792  CA  ILE B 359      54.007  28.651  52.432  1.00 30.42      B    C  
ATOM   1793  C   ILE B 359      52.676  28.019  52.077  1.00 32.90      B    C  
ATOM   1794  O   ILE B 359      51.724  28.080  52.848  1.00 33.67      B    O  
ATOM   1795  CB  ILE B 359      53.911  30.180  52.188  1.00 29.10      B    C  
ATOM   1796  CG1 ILE B 359      53.037  30.811  53.268  1.00 26.36      B    C  
ATOM   1797  CG2 ILE B 359      53.282  30.478  50.829  1.00 28.38      B    C  
ATOM   1798  CD1 ILE B 359      53.510  30.542  54.684  1.00 23.04      B    C  
ATOM   1799  N   PHE B 360      52.587  27.404  50.910  1.00 34.29      B    N  
ATOM   1800  CA  PHE B 360      51.322  26.806  50.556  1.00 35.15      B    C  
ATOM   1801  C   PHE B 360      51.187  25.380  51.086  1.00 34.14      B    C  
ATOM   1802  O   PHE B 360      50.088  24.893  51.306  1.00 35.99      B    O  
ATOM   1803  CB  PHE B 360      51.093  26.940  49.041  1.00 35.93      B    C  
ATOM   1804  CG  PHE B 360      50.748  28.363  48.624  1.00 39.66      B    C  
ATOM   1805  CD1 PHE B 360      49.614  29.001  49.146  1.00 40.13      B    C  
ATOM   1806  CD2 PHE B 360      51.593  29.097  47.788  1.00 41.14      B    C  
ATOM   1807  CE1 PHE B 360      49.332  30.350  48.847  1.00 41.29      B    C  
ATOM   1808  CE2 PHE B 360      51.322  30.453  47.481  1.00 41.75      B    C  
ATOM   1809  CZ  PHE B 360      50.193  31.076  48.013  1.00 40.53      B    C  
ATOM   1810  N   ILE B 361      52.302  24.714  51.327  1.00 32.04      B    N  
ATOM   1811  CA  ILE B 361      52.239  23.375  51.889  1.00 30.94      B    C  
ATOM   1812  C   ILE B 361      51.904  23.555  53.381  1.00 31.30      B    C  
ATOM   1813  O   ILE B 361      51.108  22.802  53.958  1.00 29.87      B    O  
ATOM   1814  CB  ILE B 361      53.599  22.645  51.702  1.00 30.39      B    C  
ATOM   1815  CG1 ILE B 361      53.720  22.191  50.239  1.00 27.82      B    C  
ATOM   1816  CG2 ILE B 361      53.742  21.491  52.711  1.00 27.37      B    C  
ATOM   1817  CD1 ILE B 361      55.101  21.755  49.835  1.00 27.56      B    C  
ATOM   1818  N   LEU B 362      52.504  24.573  53.996  1.00 30.48      B    N  
ATOM   1819  CA  LEU B 362      52.247  24.845  55.395  1.00 29.96      B    C  
ATOM   1820  C   LEU B 362      50.792  25.246  55.533  1.00 30.99      B    C  
ATOM   1821  O   LEU B 362      50.150  24.935  56.536  1.00 31.94      B    O  
ATOM   1822  CB  LEU B 362      53.155  25.960  55.923  1.00 29.12      B    C  
ATOM   1823  CG  LEU B 362      52.948  26.293  57.416  1.00 30.76      B    C  
ATOM   1824  CD1 LEU B 362      53.052  25.017  58.239  1.00 29.26      B    C  
ATOM   1825  CD2 LEU B 362      53.976  27.318  57.910  1.00 28.43      B    C  
ATOM   1826  N   LYS B 363      50.263  25.933  54.521  1.00 32.24      B    N  
ATOM   1827  CA  LYS B 363      48.854  26.359  54.546  1.00 32.64      B    C  
ATOM   1828  C   LYS B 363      47.946  25.135  54.599  1.00 31.66      B    C  
ATOM   1829  O   LYS B 363      46.963  25.108  55.337  1.00 32.29      B    O  
ATOM   1830  CB  LYS B 363      48.512  27.201  53.313  1.00 32.79      B    C  
ATOM   1831  CG  LYS B 363      48.945  28.670  53.389  1.00 35.57      B    C  
ATOM   1832  CD  LYS B 363      47.910  29.561  54.080  1.00 36.44      B    C  
ATOM   1833  CE  LYS B 363      48.156  31.062  53.831  1.00 37.26      B    C  
ATOM   1834  NZ  LYS B 363      48.056  31.468  52.386  1.00 37.20      B    N  
ATOM   1835  N   ASN B 364      48.297  24.126  53.811  1.00 30.85      B    N  
ATOM   1836  CA  ASN B 364      47.551  22.878  53.759  1.00 31.13      B    C  
ATOM   1837  C   ASN B 364      47.652  22.137  55.087  1.00 29.99      B    C  
ATOM   1838  O   ASN B 364      46.651  21.665  55.611  1.00 29.95      B    O  
ATOM   1839  CB  ASN B 364      48.097  21.988  52.636  1.00 32.78      B    C  
ATOM   1840  CG  ASN B 364      47.711  22.486  51.257  1.00 33.50      B    C  
ATOM   1841  OD1 ASN B 364      48.148  21.939  50.240  1.00 32.33      B    O  
ATOM   1842  ND2 ASN B 364      46.871  23.526  51.216  1.00 35.48      B    N  
ATOM   1843  N   TRP B 365      48.863  22.027  55.621  1.00 28.20      B    N  
ATOM   1844  CA  TRP B 365      49.054  21.339  56.889  1.00 28.38      B    C  
ATOM   1845  C   TRP B 365      48.196  21.952  58.002  1.00 27.80      B    C  
ATOM   1846  O   TRP B 365      47.574  21.231  58.777  1.00 26.86      B    O  
ATOM   1847  CB  TRP B 365      50.520  21.395  57.326  1.00 27.37      B    C  
ATOM   1848  CG  TRP B 365      51.410  20.337  56.771  1.00 27.56      B    C  
ATOM   1849  CD1 TRP B 365      52.168  20.406  55.634  1.00 28.40      B    C  
ATOM   1850  CD2 TRP B 365      51.713  19.079  57.380  1.00 27.79      B    C  
ATOM   1851  NE1 TRP B 365      52.935  19.270  55.505  1.00 26.47      B    N  
ATOM   1852  CE2 TRP B 365      52.677  18.441  56.564  1.00 27.42      B    C  
ATOM   1853  CE3 TRP B 365      51.268  18.430  58.542  1.00 26.99      B    C  
ATOM   1854  CZ2 TRP B 365      53.208  17.185  56.875  1.00 27.36      B    C  
ATOM   1855  CZ3 TRP B 365      51.795  17.185  58.850  1.00 27.17      B    C  
ATOM   1856  CH2 TRP B 365      52.759  16.576  58.018  1.00 27.22      B    C  
ATOM   1857  N   TYR B 366      48.183  23.282  58.063  1.00 27.17      B    N  
ATOM   1858  CA  TYR B 366      47.458  24.033  59.083  1.00 27.59      B    C  
ATOM   1859  C   TYR B 366      45.957  24.167  58.824  1.00 28.97      B    C  
ATOM   1860  O   TYR B 366      45.205  24.584  59.717  1.00 28.08      B    O  
ATOM   1861  CB  TYR B 366      48.026  25.456  59.214  1.00 25.24      B    C  
ATOM   1862  CG  TYR B 366      49.373  25.631  59.898  1.00 23.73      B    C  
ATOM   1863  CD1 TYR B 366      49.979  24.600  60.633  1.00 22.52      B    C  
ATOM   1864  CD2 TYR B 366      49.996  26.885  59.896  1.00 22.22      B    C  
ATOM   1865  CE1 TYR B 366      51.165  24.832  61.358  1.00 18.93      B    C  
ATOM   1866  CE2 TYR B 366      51.172  27.118  60.612  1.00 20.09      B    C  
ATOM   1867  CZ  TYR B 366      51.746  26.096  61.342  1.00 19.13      B    C  
ATOM   1868  OH  TYR B 366      52.875  26.365  62.077  1.00 18.24      B    O  
ATOM   1869  N   ASN B 367      45.518  23.841  57.610  1.00 30.41      B    N  
ATOM   1870  CA  ASN B 367      44.101  23.965  57.268  1.00 32.85      B    C  
ATOM   1871  C   ASN B 367      43.275  22.775  57.769  1.00 33.96      B    C  
ATOM   1872  O   ASN B 367      43.432  21.655  57.287  1.00 35.92      B    O  
ATOM   1873  CB  ASN B 367      43.923  24.112  55.752  1.00 32.91      B    C  
ATOM   1874  CG  ASN B 367      42.478  24.412  55.363  1.00 36.00      B    C  
ATOM   1875  OD1 ASN B 367      41.548  24.091  56.111  1.00 39.33      B    O  
ATOM   1876  ND2 ASN B 367      42.281  25.016  54.193  1.00 33.37      B    N  
ATOM   1877  N   PRO B 368      42.361  23.011  58.731  1.00 34.98      B    N  
ATOM   1878  CA  PRO B 368      41.510  21.946  59.297  1.00 34.59      B    C  
ATOM   1879  C   PRO B 368      40.614  21.331  58.229  1.00 34.62      B    C  
ATOM   1880  O   PRO B 368      40.252  20.156  58.290  1.00 34.29      B    O  
ATOM   1881  CB  PRO B 368      40.678  22.683  60.349  1.00 32.02      B    C  
ATOM   1882  CG  PRO B 368      41.477  23.890  60.664  1.00 32.98      B    C  
ATOM   1883  CD  PRO B 368      42.015  24.313  59.325  1.00 33.43      B    C  
ATOM   1884  N   LYS B 369      40.249  22.162  57.261  1.00 34.75      B    N  
ATOM   1885  CA  LYS B 369      39.384  21.754  56.174  1.00 35.21      B    C  
ATOM   1886  C   LYS B 369      40.164  21.144  55.014  1.00 34.19      B    C  
ATOM   1887  O   LYS B 369      39.599  20.886  53.957  1.00 35.58      B    O  
ATOM   1888  CB  LYS B 369      38.562  22.961  55.708  1.00 37.32      B    C  
ATOM   1889  CG  LYS B 369      37.475  23.390  56.704  1.00 41.12      B    C  
ATOM   1890  CD  LYS B 369      37.186  24.894  56.646  1.00 46.21      B    C  
ATOM   1891  CE  LYS B 369      36.824  25.373  55.238  1.00 48.34      B    C  
ATOM   1892  NZ  LYS B 369      36.764  26.869  55.156  1.00 49.91      B    N  
