ATOM    981  N   PRO A 119      62.337  15.226  14.885  1.00 29.95
ATOM    982  CA  PRO A 119      62.815  15.550  13.537  1.00 30.19
ATOM    983  C   PRO A 119      61.744  15.524  12.456  1.00 29.57
ATOM    984  O   PRO A 119      60.691  14.900  12.619  1.00 29.84
ATOM    985  CB  PRO A 119      63.878  14.480  13.295  1.00 31.18
ATOM    986  CG  PRO A 119      63.351  13.314  14.067  1.00 31.67
ATOM    987  CD  PRO A 119      62.920  13.959  15.353  1.00 30.63
ATOM    988  N   ARG A 120      62.011  16.220  11.354  1.00 29.02
ATOM    989  CA  ARG A 120      61.078  16.243  10.240  1.00 28.78
ATOM    990  C   ARG A 120      60.925  14.827   9.705  1.00 28.60
ATOM    991  O   ARG A 120      61.850  14.004   9.786  1.00 29.12
ATOM    992  CB  ARG A 120      61.586  17.159   9.132  1.00 27.82
ATOM    993  CG  ARG A 120      61.890  18.546   9.614  1.00 29.00
ATOM    994  CD  ARG A 120      62.474  19.392   8.511  1.00 29.38
ATOM    995  NE  ARG A 120      61.516  19.600   7.438  1.00 31.62
ATOM    996  CZ  ARG A 120      61.803  20.180   6.274  1.00 33.27
ATOM    997  NH1 ARG A 120      63.036  20.613   6.022  1.00 33.80
ATOM    998  NH2 ARG A 120      60.850  20.344   5.362  1.00 33.82
ATOM    999  N   PRO A 121      59.729  14.495   9.206  1.00 29.01
ATOM   1000  CA  PRO A 121      59.508  13.154   8.669  1.00 29.31
ATOM   1001  C   PRO A 121      60.033  13.096   7.226  1.00 29.60
ATOM   1002  O   PRO A 121      59.267  12.896   6.277  1.00 29.40
ATOM   1003  CB  PRO A 121      57.989  13.017   8.750  1.00 27.94
ATOM   1004  CG  PRO A 121      57.531  14.416   8.435  1.00 27.83
ATOM   1005  CD  PRO A 121      58.465  15.257   9.269  1.00 28.74
ATOM   1006  N   LEU A 122      61.347  13.262   7.081  1.00 30.03
ATOM   1007  CA  LEU A 122      61.998  13.253   5.770  1.00 30.38
ATOM   1008  C   LEU A 122      61.705  12.004   4.942  1.00 31.44
ATOM   1009  O   LEU A 122      61.395  12.108   3.756  1.00 31.82
ATOM   1010  CB  LEU A 122      63.504  13.506   5.921  1.00 29.11
ATOM   1011  CG  LEU A 122      63.785  14.936   6.421  1.00 28.32
ATOM   1012  CD1 LEU A 122      65.255  15.171   6.696  1.00 27.18
ATOM   1013  CD2 LEU A 122      63.269  15.926   5.401  1.00 27.96
ATOM   1014  N   GLU A 123      61.724  10.838   5.576  1.00 32.17
ATOM   1015  CA  GLU A 123      61.435   9.591   4.877  1.00 33.99
ATOM   1016  C   GLU A 123      60.040   9.591   4.253  1.00 34.55
ATOM   1017  O   GLU A 123      59.866   9.137   3.117  1.00 34.80
ATOM   1018  CB  GLU A 123      61.583   8.388   5.810  1.00 35.95
ATOM   1019  CG  GLU A 123      61.277   7.032   5.137  1.00 41.10
ATOM   1020  CD  GLU A 123      61.359   5.820   6.088  1.00 44.21
ATOM   1021  OE1 GLU A 123      62.459   5.567   6.647  1.00 47.55
ATOM   1022  OE2 GLU A 123      60.337   5.102   6.261  1.00 44.75
ATOM   1023  N   ASN A 124      59.051  10.124   4.973  1.00 34.04
ATOM   1024  CA  ASN A 124      57.681  10.158   4.462  1.00 33.60
ATOM   1025  C   ASN A 124      57.450  11.262   3.439  1.00 32.35
ATOM   1026  O   ASN A 124      56.629  11.113   2.537  1.00 32.87
ATOM   1027  CB  ASN A 124      56.672  10.273   5.613  1.00 34.90
ATOM   1028  CG  ASN A 124      56.787   9.129   6.587  1.00 35.62
ATOM   1029  OD1 ASN A 124      56.336   8.020   6.317  1.00 35.70
ATOM   1030  ND2 ASN A 124      57.463   9.373   7.702  1.00 37.85
ATOM   1031  N   LEU A 125      58.161  12.376   3.579  1.00 31.53
ATOM   1032  CA  LEU A 125      58.015  13.484   2.641  1.00 31.24
ATOM   1033  C   LEU A 125      58.530  13.104   1.247  1.00 32.42
ATOM   1034  O   LEU A 125      58.069  13.633   0.229  1.00 31.52
ATOM   1035  CB  LEU A 125      58.760  14.714   3.145  1.00 30.43
ATOM   1036  CG  LEU A 125      58.316  15.370   4.454  1.00 30.30
ATOM   1037  CD1 LEU A 125      59.165  16.600   4.694  1.00 30.04
ATOM   1038  CD2 LEU A 125      56.858  15.765   4.378  1.00 30.62
ATOM   1039  N   GLU A 126      59.492  12.189   1.215  1.00 33.78
ATOM   1040  CA  GLU A 126      60.078  11.727  -0.026  1.00 35.72
ATOM   1041  C   GLU A 126      59.326  10.541  -0.622  1.00 35.57
ATOM   1042  O   GLU A 126      58.944  10.566  -1.789  1.00 36.48
ATOM   1043  CB  GLU A 126      61.543  11.339   0.202  1.00 37.46
ATOM   1044  CG  GLU A 126      62.208  10.724  -1.022  1.00 41.76
ATOM   1045  CD  GLU A 126      63.634  10.273  -0.762  1.00 43.93
ATOM   1046  OE1 GLU A 126      63.824   9.134  -0.271  1.00 44.62
ATOM   1047  OE2 GLU A 126      64.565  11.059  -1.065  1.00 44.98
ATOM   1048  N   LYS A 127      59.107   9.517   0.195  1.00 35.53
ATOM   1049  CA  LYS A 127      58.449   8.282  -0.227  1.00 35.66
ATOM   1050  C   LYS A 127      56.924   8.267  -0.296  1.00 34.61
ATOM   1051  O   LYS A 127      56.352   7.575  -1.140  1.00 34.62
ATOM   1052  CB  LYS A 127      58.935   7.124   0.654  1.00 38.14
ATOM   1053  CG  LYS A 127      60.433   6.813   0.516  1.00 41.60
ATOM   1054  CD  LYS A 127      60.725   6.063  -0.790  1.00 44.31
ATOM   1055  CE  LYS A 127      62.214   6.097  -1.183  1.00 46.56
ATOM   1056  NZ  LYS A 127      62.531   5.192  -2.351  1.00 48.05
ATOM   1057  N   GLY A 128      56.261   9.036   0.561  1.00 32.87
ATOM   1058  CA  GLY A 128      54.808   9.039   0.560  1.00 31.42
ATOM   1059  C   GLY A 128      54.278   8.014   1.545  1.00 30.02
ATOM   1060  O   GLY A 128      55.033   7.182   2.038  1.00 30.35
ATOM   1061  N   VAL A 129      52.984   8.048   1.836  1.00 28.69
ATOM   1062  CA  VAL A 129      52.436   7.102   2.795  1.00 27.56
ATOM   1063  C   VAL A 129      51.179   6.407   2.315  1.00 27.56
ATOM   1064  O   VAL A 129      50.653   6.700   1.237  1.00 27.56
ATOM   1065  CB  VAL A 129      52.107   7.794   4.143  1.00 26.81
ATOM   1066  CG1 VAL A 129      53.341   8.457   4.712  1.00 26.31
ATOM   1067  CG2 VAL A 129      50.991   8.816   3.954  1.00 25.86
ATOM   1068  N   LYS A 130      50.714   5.471   3.133  1.00 27.21
ATOM   1069  CA  LYS A 130      49.498   4.734   2.866  1.00 27.65
ATOM   1070  C   LYS A 130      48.433   5.261   3.828  1.00 26.95
ATOM   1071  O   LYS A 130      48.732   5.561   4.985  1.00 25.51
ATOM   1072  CB  LYS A 130      49.717   3.244   3.114  1.00 28.96
ATOM   1073  CG  LYS A 130      50.632   2.576   2.119  1.00 32.07
ATOM   1074  CD  LYS A 130      50.880   1.132   2.519  1.00 35.41
ATOM   1075  CE  LYS A 130      51.628   1.049   3.833  1.00 36.79
ATOM   1076  NZ  LYS A 130      51.885  -0.384   4.185  1.00 40.75
ATOM   1077  N   ALA A 131      47.200   5.358   3.341  1.00 26.85
ATOM   1078  CA  ALA A 131      46.061   5.834   4.117  1.00 26.39
ATOM   1079  C   ALA A 131      44.915   4.854   3.955  1.00 26.76
ATOM   1080  O   ALA A 131      44.990   3.920   3.145  1.00 25.70
ATOM   1081  CB  ALA A 131      45.622   7.203   3.624  1.00 25.58
ATOM   1082  N   THR A 132      43.857   5.066   4.735  1.00 26.55
ATOM   1083  CA  THR A 132      42.661   4.237   4.680  1.00 25.40
ATOM   1084  C   THR A 132      41.461   5.135   4.939  1.00 25.03
ATOM   1085  O   THR A 132      41.608   6.212   5.523  1.00 26.05
ATOM   1086  CB  THR A 132      42.704   3.106   5.724  1.00 25.92
ATOM   1087  OG1 THR A 132      41.444   2.430   5.729  1.00 27.03
ATOM   1088  CG2 THR A 132      42.998   3.644   7.112  1.00 24.48
ATOM   1089  N   PHE A 133      40.295   4.742   4.439  1.00 24.08
ATOM   1090  CA  PHE A 133      39.076   5.517   4.645  1.00 23.03
ATOM   1091  C   PHE A 133      38.343   5.076   5.916  1.00 22.23
ATOM   1092  O   PHE A 133      38.081   3.892   6.105  1.00 19.93
ATOM   1093  CB  PHE A 133      38.129   5.362   3.466  1.00 23.70
ATOM   1094  CG  PHE A 133      38.591   6.041   2.220  1.00 25.95
ATOM   1095  CD1 PHE A 133      38.932   7.392   2.231  1.00 26.89
ATOM   1096  CD2 PHE A 133      38.647   5.341   1.013  1.00 26.26
ATOM   1097  CE1 PHE A 133      39.319   8.045   1.057  1.00 26.11
ATOM   1098  CE2 PHE A 133      39.029   5.981  -0.166  1.00 26.00
ATOM   1099  CZ  PHE A 133      39.366   7.337  -0.143  1.00 26.79
ATOM   1100  N   VAL A 134      37.977   6.040   6.756  1.00 22.38
ATOM   1101  CA  VAL A 134      37.262   5.759   7.994  1.00 23.03
ATOM   1102  C   VAL A 134      36.085   6.725   8.042  1.00 23.55
ATOM   1103  O   VAL A 134      36.237   7.896   7.709  1.00 24.50
ATOM   1104  CB  VAL A 134      38.186   5.942   9.230  1.00 23.12
ATOM   1105  CG1 VAL A 134      37.449   5.603  10.513  1.00 23.05
ATOM   1106  CG2 VAL A 134      39.396   5.046   9.105  1.00 22.39
ATOM   1107  N   GLU A 135      34.893   6.211   8.340  1.00 25.26
ATOM   1108  CA  GLU A 135      33.697   7.045   8.407  1.00 26.85
ATOM   1109  C   GLU A 135      33.893   8.072   9.513  1.00 26.35
ATOM   1110  O   GLU A 135      34.406   7.759  10.588  1.00 26.04
ATOM   1111  CB  GLU A 135      32.440   6.207   8.680  1.00 29.57
ATOM   1112  CG  GLU A 135      31.103   6.958   8.448  1.00 33.28
ATOM   1113  CD  GLU A 135      29.864   6.110   8.765  1.00 36.83
ATOM   1114  OE1 GLU A 135      29.970   4.856   8.811  1.00 39.65
ATOM   1115  OE2 GLU A 135      28.771   6.695   8.987  1.00 39.29
ATOM   1116  N   ASP A 136      33.545   9.312   9.206  1.00 24.50
ATOM   1117  CA  ASP A 136      33.676  10.413  10.142  1.00 24.11
ATOM   1118  C   ASP A 136      32.434  10.453  11.028  1.00 24.41
ATOM   1119  O   ASP A 136      31.365  10.856  10.579  1.00 23.91
ATOM   1120  CB  ASP A 136      33.798  11.726   9.363  1.00 22.94
ATOM   1121  CG  ASP A 136      34.258  12.873  10.216  1.00 24.13
ATOM   1122  OD1 ASP A 136      34.201  12.766  11.459  1.00 23.16
ATOM   1123  OD2 ASP A 136      34.682  13.899   9.644  1.00 24.01
ATOM   1124  N   ILE A 137      32.575  10.051  12.283  1.00 23.48
ATOM   1125  CA  ILE A 137      31.433  10.054  13.190  1.00 23.73
ATOM   1126  C   ILE A 137      31.574  11.104  14.275  1.00 23.25
ATOM   1127  O   ILE A 137      30.899  11.038  15.294  1.00 23.11
ATOM   1128  CB  ILE A 137      31.245   8.682  13.874  1.00 23.34
ATOM   1129  CG1 ILE A 137      32.492   8.326  14.683  1.00 23.14
ATOM   1130  CG2 ILE A 137      30.913   7.625  12.827  1.00 23.48
ATOM   1131  CD1 ILE A 137      32.297   7.234  15.693  1.00 23.01
ATOM   1132  N   ARG A 138      32.417  12.096  14.025  1.00 21.97
ATOM   1133  CA  ARG A 138      32.680  13.141  14.993  1.00 21.12
ATOM   1134  C   ARG A 138      31.537  14.124  15.089  1.00 20.81
ATOM   1135  O   ARG A 138      30.567  14.056  14.331  1.00 21.77
ATOM   1136  CB  ARG A 138      33.997  13.854  14.649  1.00 19.63
ATOM   1137  CG  ARG A 138      35.174  12.907  14.556  1.00 18.75
ATOM   1138  CD  ARG A 138      36.422  13.613  14.077  1.00 19.18
ATOM   1139  NE  ARG A 138      36.243  14.188  12.750  1.00 17.12
ATOM   1140  CZ  ARG A 138      36.994  15.155  12.233  1.00 18.00
ATOM   1141  NH1 ARG A 138      37.991  15.676  12.926  1.00 16.41
ATOM   1142  NH2 ARG A 138      36.752  15.589  11.006  1.00 16.18
ATOM   1143  N   TRP A 139      31.636  15.030  16.046  1.00 19.83
ATOM   1144  CA  TRP A 139      30.587  15.998  16.225  1.00 18.35
ATOM   1145  C   TRP A 139      30.576  17.013  15.089  1.00 19.20
ATOM   1146  O   TRP A 139      31.479  17.038  14.249  1.00 18.32
ATOM   1147  CB  TRP A 139      30.703  16.654  17.600  1.00 17.30
ATOM   1148  CG  TRP A 139      31.824  17.629  17.776  1.00 16.87
ATOM   1149  CD1 TRP A 139      33.067  17.594  17.197  1.00 15.59
ATOM   1150  CD2 TRP A 139      31.826  18.744  18.663  1.00 16.15
ATOM   1151  NE1 TRP A 139      33.841  18.614  17.688  1.00 16.37
ATOM   1152  CE2 TRP A 139      33.109  19.335  18.591  1.00 15.30
ATOM   1153  CE3 TRP A 139      30.870  19.300  19.523  1.00 16.10
ATOM   1154  CZ2 TRP A 139      33.466  20.452  19.356  1.00 17.06
ATOM   1155  CZ3 TRP A 139      31.219  20.412  20.282  1.00 16.97
ATOM   1156  CH2 TRP A 139      32.513  20.976  20.193  1.00 15.65
ATOM   1157  N   LEU A 140      29.572  17.876  15.087  1.00 18.41
ATOM   1158  CA  LEU A 140      29.424  18.862  14.033  1.00 18.72
ATOM   1159  C   LEU A 140      30.161  20.161  14.241  1.00 18.27
ATOM   1160  O   LEU A 140      29.876  21.147  13.574  1.00 19.79
ATOM   1161  CB  LEU A 140      27.939  19.132  13.773  1.00 18.72
ATOM   1162  CG  LEU A 140      27.105  17.851  13.672  1.00 19.87
ATOM   1163  CD1 LEU A 140      25.644  18.181  13.449  1.00 21.17
ATOM   1164  CD2 LEU A 140      27.624  16.953  12.562  1.00 20.54
ATOM   1165  N   ARG A 141      31.118  20.197  15.151  1.00 18.49
ATOM   1166  CA  ARG A 141      31.861  21.440  15.344  1.00 18.37
ATOM   1167  C   ARG A 141      33.359  21.187  15.265  1.00 18.07
ATOM   1168  O   ARG A 141      34.130  21.595  16.139  1.00 17.52
ATOM   1169  CB  ARG A 141      31.481  22.147  16.659  1.00 18.48
ATOM   1170  CG  ARG A 141      30.172  22.906  16.621  1.00 17.28
ATOM   1171  CD  ARG A 141      30.117  23.902  15.480  1.00 18.43
ATOM   1172  NE  ARG A 141      31.108  24.971  15.585  1.00 19.35
ATOM   1173  CZ  ARG A 141      30.922  26.093  16.262  1.00 19.57
ATOM   1174  NH1 ARG A 141      29.808  26.272  16.954  1.00 22.09
ATOM   1175  NH2 ARG A 141      31.866  27.017  16.292  1.00 20.08
ATOM   1176  N   CYS A 142      33.767  20.549  14.174  1.00 17.19
ATOM   1177  CA  CYS A 142      35.158  20.215  13.960  1.00 17.08
ATOM   1178  C   CYS A 142      36.069  21.418  13.744  1.00 16.98
ATOM   1179  O   CYS A 142      37.295  21.275  13.760  1.00 18.75
ATOM   1180  CB  CYS A 142      35.268  19.202  12.832  1.00 16.84
ATOM   1181  SG  CYS A 142      34.578  17.619  13.260  1.00 20.82
ATOM   1182  N   ASP A 143      35.480  22.600  13.552  1.00 15.59
ATOM   1183  CA  ASP A 143      36.253  23.836  13.394  1.00 15.71
ATOM   1184  C   ASP A 143      36.885  24.286  14.728  1.00 15.61
ATOM   1185  O   ASP A 143      37.771  25.139  14.757  1.00 15.58
ATOM   1186  CB  ASP A 143      35.375  24.976  12.845  1.00 14.65
ATOM   1187  CG  ASP A 143      34.154  25.259  13.719  1.00 15.22
ATOM   1188  OD1 ASP A 143      33.321  24.346  13.851  1.00 18.17
ATOM   1189  OD2 ASP A 143      34.031  26.374  14.283  1.00 16.86
ATOM   1190  N   ILE A 144      36.392  23.751  15.834  1.00 15.03
ATOM   1191  CA  ILE A 144      36.916  24.123  17.132  1.00 14.77
ATOM   1192  C   ILE A 144      38.006  23.128  17.461  1.00 13.49
ATOM   1193  O   ILE A 144      37.758  21.937  17.440  1.00 14.26
ATOM   1194  CB  ILE A 144      35.805  24.036  18.225  1.00 16.35
ATOM   1195  CG1 ILE A 144      34.601  24.897  17.822  1.00 14.97
ATOM   1196  CG2 ILE A 144      36.363  24.486  19.585  1.00 16.21
ATOM   1197  CD1 ILE A 144      33.506  24.968  18.854  1.00 15.22
ATOM   1198  N   LYS A 145      39.209  23.591  17.763  1.00 14.19
ATOM   1199  CA  LYS A 145      40.274  22.658  18.102  1.00 14.80
ATOM   1200  C   LYS A 145      40.219  22.314  19.592  1.00 14.33
ATOM   1201  O   LYS A 145      41.059  22.757  20.381  1.00 13.78
ATOM   1202  CB  LYS A 145      41.631  23.227  17.722  1.00 17.33
ATOM   1203  CG  LYS A 145      41.864  23.294  16.231  1.00 22.52
ATOM   1204  CD  LYS A 145      43.338  23.155  15.890  1.00 26.04
ATOM   1205  CE  LYS A 145      43.892  21.865  16.432  1.00 27.67
ATOM   1206  NZ  LYS A 145      45.142  21.428  15.779  1.00 31.02
ATOM   1207  N   SER A 146      39.223  21.523  19.974  1.00 14.24
ATOM   1208  CA  SER A 146      39.037  21.143  21.367  1.00 14.27
ATOM   1209  C   SER A 146      39.690  19.819  21.777  1.00 14.39
ATOM   1210  O   SER A 146      40.143  19.047  20.941  1.00 14.36
ATOM   1211  CB  SER A 146      37.547  21.102  21.694  1.00 14.78
ATOM   1212  OG  SER A 146      37.004  19.822  21.422  1.00 14.64
ATOM   1213  N   LEU A 147      39.669  19.541  23.078  1.00 15.03
ATOM   1214  CA  LEU A 147      40.244  18.317  23.628  1.00 14.03
ATOM   1215  C   LEU A 147      39.339  17.089  23.467  1.00 14.94
ATOM   1216  O   LEU A 147      39.686  15.990  23.892  1.00 14.06
ATOM   1217  CB  LEU A 147      40.633  18.526  25.099  1.00 14.47
ATOM   1218  CG  LEU A 147      41.632  19.630  25.459  1.00 15.52
ATOM   1219  CD1 LEU A 147      41.681  19.829  26.968  1.00 16.26
ATOM   1220  CD2 LEU A 147      42.999  19.304  24.923  1.00 13.21
ATOM   1221  N   ASN A 148      38.153  17.273  22.894  1.00 14.70
ATOM   1222  CA  ASN A 148      37.261  16.139  22.661  1.00 15.07
ATOM   1223  C   ASN A 148      37.827  15.487  21.400  1.00 15.81
ATOM   1224  O   ASN A 148      37.423  15.818  20.281  1.00 14.68
ATOM   1225  CB  ASN A 148      35.828  16.603  22.394  1.00 13.52
ATOM   1226  CG  ASN A 148      35.041  16.846  23.662  1.00 13.69
ATOM   1227  OD1 ASN A 148      33.857  16.523  23.732  1.00 14.38
ATOM   1228  ND2 ASN A 148      35.676  17.433  24.655  1.00 12.81
ATOM   1229  N   LEU A 149      38.754  14.556  21.580  1.00 15.37
ATOM   1230  CA  LEU A 149      39.400  13.932  20.436  1.00 16.92
ATOM   1231  C   LEU A 149      39.237  12.430  20.329  1.00 16.60
ATOM   1232  O   LEU A 149      39.951  11.790  19.550  1.00 17.14
ATOM   1233  CB  LEU A 149      40.896  14.301  20.423  1.00 14.39
ATOM   1234  CG  LEU A 149      41.240  15.765  20.146  1.00 14.02
ATOM   1235  CD1 LEU A 149      42.659  16.044  20.578  1.00 16.36
ATOM   1236  CD2 LEU A 149      41.038  16.114  18.662  1.00 16.18
ATOM   1237  N   LEU A 150      38.235  11.871  21.000  1.00 16.18
ATOM   1238  CA  LEU A 150      38.039  10.427  20.950  1.00 16.13
ATOM   1239  C   LEU A 150      37.729   9.910  19.549  1.00 16.55
ATOM   1240  O   LEU A 150      38.092   8.791  19.205  1.00 15.58
ATOM   1241  CB  LEU A 150      36.971   9.987  21.940  1.00 16.01
ATOM   1242  CG  LEU A 150      36.855   8.495  22.258  1.00 16.91
ATOM   1243  CD1 LEU A 150      38.212   7.876  22.545  1.00 16.88
ATOM   1244  CD2 LEU A 150      35.919   8.351  23.446  1.00 18.45
ATOM   1245  N   GLY A 151      37.062  10.712  18.735  1.00 17.10
ATOM   1246  CA  GLY A 151      36.787  10.264  17.378  1.00 18.10
ATOM   1247  C   GLY A 151      38.075  10.122  16.573  1.00 19.46
ATOM   1248  O   GLY A 151      38.275   9.135  15.861  1.00 20.45
ATOM   1249  N   ALA A 152      38.973  11.097  16.707  1.00 19.68
ATOM   1250  CA  ALA A 152      40.249  11.071  15.996  1.00 20.02
ATOM   1251  C   ALA A 152      41.144   9.958  16.544  1.00 20.63
ATOM   1252  O   ALA A 152      41.905   9.353  15.801  1.00 21.89
ATOM   1253  CB  ALA A 152      40.936  12.404  16.097  1.00 18.57
ATOM   1254  N   VAL A 153      41.025   9.665  17.836  1.00 20.89
ATOM   1255  CA  VAL A 153      41.810   8.606  18.462  1.00 20.32
ATOM   1256  C   VAL A 153      41.441   7.244  17.870  1.00 20.84
ATOM   1257  O   VAL A 153      42.321   6.450  17.535  1.00 20.46
ATOM   1258  CB  VAL A 153      41.587   8.573  20.011  1.00 20.92
ATOM   1259  CG1 VAL A 153      42.131   7.285  20.627  1.00 19.62
ATOM   1260  CG2 VAL A 153      42.252   9.772  20.654  1.00 20.72
ATOM   1261  N   LEU A 154      40.140   6.987  17.729  1.00 21.03
ATOM   1262  CA  LEU A 154      39.657   5.723  17.189  1.00 21.76
ATOM   1263  C   LEU A 154      39.980   5.560  15.701  1.00 22.14
ATOM   1264  O   LEU A 154      40.198   4.452  15.232  1.00 22.92
ATOM   1265  CB  LEU A 154      38.151   5.584  17.442  1.00 21.35
ATOM   1266  CG  LEU A 154      37.698   5.523  18.914  1.00 20.83
ATOM   1267  CD1 LEU A 154      36.175   5.586  19.000  1.00 21.50
ATOM   1268  CD2 LEU A 154      38.207   4.257  19.578  1.00 17.85
ATOM   1269  N   ALA A 155      39.971   6.666  14.966  1.00 21.60
ATOM   1270  CA  ALA A 155      40.287   6.662  13.543  1.00 21.35
ATOM   1271  C   ALA A 155      41.781   6.406  13.347  1.00 21.47
ATOM   1272  O   ALA A 155      42.173   5.550  12.549  1.00 20.37
ATOM   1273  CB  ALA A 155      39.883   7.984  12.915  1.00 21.22
ATOM   1274  N   LYS A 156      42.614   7.097  14.116  1.00 22.63
ATOM   1275  CA  LYS A 156      44.057   6.917  14.006  1.00 23.48
ATOM   1276  C   LYS A 156      44.449   5.484  14.319  1.00 24.57
ATOM   1277  O   LYS A 156      45.296   4.910  13.636  1.00 24.92
ATOM   1278  CB  LYS A 156      44.810   7.862  14.941  1.00 24.96
ATOM   1279  CG  LYS A 156      46.334   7.771  14.826  1.00 25.49
ATOM   1280  CD  LYS A 156      46.869   8.484  13.578  1.00 28.72
ATOM   1281  CE  LYS A 156      46.778  10.009  13.716  1.00 28.75
ATOM   1282  NZ  LYS A 156      47.149  10.712  12.450  1.00 30.07
ATOM   1283  N   GLN A 157      43.839   4.905  15.350  1.00 24.31
ATOM   1284  CA  GLN A 157      44.142   3.531  15.726  1.00 25.82
ATOM   1285  C   GLN A 157      43.703   2.508  14.681  1.00 26.44
ATOM   1286  O   GLN A 157      44.333   1.461  14.548  1.00 26.51
ATOM   1287  CB  GLN A 157      43.537   3.187  17.091  1.00 24.48
ATOM   1288  CG  GLN A 157      43.732   1.732  17.508  1.00 25.39
ATOM   1289  CD  GLN A 157      45.162   1.373  17.874  1.00 24.56
ATOM   1290  OE1 GLN A 157      46.053   2.227  17.946  1.00 25.67
ATOM   1291  NE2 GLN A 157      45.380   0.101  18.147  1.00 25.09
ATOM   1292  N   GLU A 158      42.621   2.792  13.959  1.00 27.93
ATOM   1293  CA  GLU A 158      42.142   1.875  12.927  1.00 29.92
ATOM   1294  C   GLU A 158      43.147   1.882  11.771  1.00 30.85
ATOM   1295  O   GLU A 158      43.482   0.839  11.203  1.00 31.13
ATOM   1296  CB  GLU A 158      40.758   2.296  12.418  1.00 30.57
ATOM   1297  CG  GLU A 158      40.103   1.259  11.509  1.00 33.22
ATOM   1298  CD  GLU A 158      38.726   1.673  11.025  1.00 35.19
ATOM   1299  OE1 GLU A 158      37.936   2.222  11.829  1.00 35.32
ATOM   1300  OE2 GLU A 158      38.429   1.442   9.833  1.00 36.56
ATOM   1301  N   ALA A 159      43.630   3.070  11.433  1.00 31.72
ATOM   1302  CA  ALA A 159      44.615   3.221  10.371  1.00 33.57
ATOM   1303  C   ALA A 159      45.919   2.566  10.815  1.00 34.36
ATOM   1304  O   ALA A 159      46.532   1.784  10.084  1.00 35.22
ATOM   1305  CB  ALA A 159      44.843   4.698  10.088  1.00 31.43
ATOM   1306  N   HIS A 160      46.308   2.870  12.043  1.00 35.64
ATOM   1307  CA  HIS A 160      47.527   2.358  12.642  1.00 37.63
ATOM   1308  C   HIS A 160      47.513   0.829  12.602  1.00 38.38
ATOM   1309  O   HIS A 160      48.541   0.201  12.354  1.00 38.99
ATOM   1310  CB  HIS A 160      47.621   2.894  14.080  1.00 39.24
ATOM   1311  CG  HIS A 160      48.915   2.603  14.774  1.00 41.65
ATOM   1312  ND1 HIS A 160      50.005   3.448  14.712  1.00 42.69
ATOM   1313  CD2 HIS A 160      49.279   1.584  15.591  1.00 42.85
ATOM   1314  CE1 HIS A 160      50.981   2.962  15.459  1.00 43.41
ATOM   1315  NE2 HIS A 160      50.565   1.831  16.004  1.00 43.67
ATOM   1316  N   GLU A 161      46.342   0.233  12.806  1.00 38.98
ATOM   1317  CA  GLU A 161      46.219  -1.220  12.795  1.00 40.02
ATOM   1318  C   GLU A 161      46.316  -1.851  11.415  1.00 40.41
ATOM   1319  O   GLU A 161      46.620  -3.041  11.296  1.00 41.93
ATOM   1320  CB  GLU A 161      44.925  -1.659  13.467  1.00 40.26
ATOM   1321  CG  GLU A 161      45.069  -1.904  14.947  1.00 40.99
ATOM   1322  CD  GLU A 161      43.735  -2.081  15.641  1.00 41.93
ATOM   1323  OE1 GLU A 161      42.734  -2.417  14.970  1.00 42.20
ATOM   1324  OE2 GLU A 161      43.689  -1.869  16.870  1.00 41.86
ATOM   1325  N   LYS A 162      46.021  -1.079  10.377  1.00 39.78
ATOM   1326  CA  LYS A 162      46.101  -1.598   9.015  1.00 39.10
ATOM   1327  C   LYS A 162      47.461  -1.255   8.409  1.00 37.99
ATOM   1328  O   LYS A 162      47.662  -1.394   7.206  1.00 38.84
ATOM   1329  CB  LYS A 162      44.985  -1.012   8.143  1.00 38.64
ATOM   1330  CG  LYS A 162      43.570  -1.439   8.503  1.00 38.97
ATOM   1331  CD  LYS A 162      42.567  -0.520   7.808  1.00 39.57
ATOM   1332  CE  LYS A 162      41.127  -0.971   7.968  1.00 40.13
ATOM   1333  NZ  LYS A 162      40.171   0.109   7.543  1.00 40.72
ATOM   1334  N   GLY A 163      48.393  -0.808   9.245  1.00 36.99
ATOM   1335  CA  GLY A 163      49.709  -0.437   8.750  1.00 35.09
ATOM   1336  C   GLY A 163      49.740   0.893   8.000  1.00 34.05
ATOM   1337  O   GLY A 163      50.766   1.252   7.416  1.00 35.22
ATOM   1338  N   CYS A 164      48.636   1.637   8.037  1.00 32.29
ATOM   1339  CA  CYS A 164      48.537   2.931   7.367  1.00 30.19
ATOM   1340  C   CYS A 164      48.966   4.078   8.275  1.00 29.12
ATOM   1341  O   CYS A 164      48.899   3.976   9.504  1.00 30.11
ATOM   1342  CB  CYS A 164      47.116   3.162   6.874  1.00 30.91
ATOM   1343  SG  CYS A 164      46.530   1.857   5.794  1.00 33.45
ATOM   1344  N   TYR A 165      49.357   5.190   7.662  1.00 27.30
ATOM   1345  CA  TYR A 165      49.840   6.357   8.390  1.00 25.83
ATOM   1346  C   TYR A 165      48.746   7.311   8.854  1.00 26.08
ATOM   1347  O   TYR A 165      48.846   7.928   9.914  1.00 25.70
ATOM   1348  CB  TYR A 165      50.853   7.107   7.518  1.00 24.57
ATOM   1349  CG  TYR A 165      51.310   8.426   8.073  1.00 23.20
ATOM   1350  CD1 TYR A 165      52.290   8.483   9.052  1.00 22.72
ATOM   1351  CD2 TYR A 165      50.750   9.620   7.629  1.00 22.23
ATOM   1352  CE1 TYR A 165      52.699   9.689   9.580  1.00 24.34
ATOM   1353  CE2 TYR A 165      51.156  10.830   8.144  1.00 22.90
ATOM   1354  CZ  TYR A 165      52.132  10.858   9.123  1.00 23.36
ATOM   1355  OH  TYR A 165      52.566  12.052   9.649  1.00 26.30
ATOM   1356  N   GLU A 166      47.692   7.428   8.062  1.00 25.31
ATOM   1357  CA  GLU A 166      46.623   8.347   8.398  1.00 24.63
ATOM   1358  C   GLU A 166      45.289   7.797   7.956  1.00 24.33
ATOM   1359  O   GLU A 166      45.216   6.956   7.061  1.00 24.67
ATOM   1360  CB  GLU A 166      46.894   9.714   7.744  1.00 23.22
ATOM   1361  CG  GLU A 166      45.806  10.788   7.901  1.00 21.69
ATOM   1362  CD  GLU A 166      45.536  11.163   9.349  1.00 19.65
ATOM   1363  OE1 GLU A 166      45.245  10.267  10.149  1.00 19.62
ATOM   1364  OE2 GLU A 166      45.582  12.355   9.684  1.00 18.51
ATOM   1365  N   ALA A 167      44.257   8.179   8.692  1.00 23.45
ATOM   1366  CA  ALA A 167      42.904   7.792   8.393  1.00 23.04
ATOM   1367  C   ALA A 167      42.288   9.000   7.737  1.00 22.42
ATOM   1368  O   ALA A 167      42.365  10.111   8.275  1.00 23.49
ATOM   1369  CB  ALA A 167      42.156   7.465   9.670  1.00 23.09
ATOM   1370  N   ILE A 168      41.773   8.819   6.529  1.00 22.09
ATOM   1371  CA  ILE A 168      41.113   9.905   5.824  1.00 21.80
ATOM   1372  C   ILE A 168      39.626   9.691   6.134  1.00 21.34
ATOM   1373  O   ILE A 168      39.071   8.623   5.859  1.00 20.92
ATOM   1374  CB  ILE A 168      41.422   9.867   4.293  1.00 21.49
ATOM   1375  CG1 ILE A 168      42.907  10.191   4.061  1.00 21.72
ATOM   1376  CG2 ILE A 168      40.557  10.881   3.550  1.00 20.69
ATOM   1377  CD1 ILE A 168      43.391  10.024   2.633  1.00 22.42
ATOM   1378  N   LEU A 169      39.003  10.700   6.734  1.00 20.89
ATOM   1379  CA  LEU A 169      37.602  10.634   7.146  1.00 20.07
ATOM   1380  C   LEU A 169      36.612  11.112   6.101  1.00 20.39
ATOM   1381  O   LEU A 169      36.920  11.976   5.282  1.00 21.05
ATOM   1382  CB  LEU A 169      37.420  11.451   8.429  1.00 18.69
ATOM   1383  CG  LEU A 169      38.494  11.251   9.503  1.00 16.96
ATOM   1384  CD1 LEU A 169      38.188  12.109  10.698  1.00 16.64
ATOM   1385  CD2 LEU A 169      38.557   9.789   9.891  1.00 17.67
ATOM   1386  N   HIS A 170      35.395  10.577   6.160  1.00 21.13
ATOM   1387  CA  HIS A 170      34.362  10.954   5.207  1.00 21.92
ATOM   1388  C   HIS A 170      32.959  10.952   5.798  1.00 22.97
ATOM   1389  O   HIS A 170      32.626  10.080   6.594  1.00 21.98
ATOM   1390  CB  HIS A 170      34.402  10.047   3.966  1.00 20.52
ATOM   1391  CG  HIS A 170      34.207   8.592   4.257  1.00 18.77
ATOM   1392  ND1 HIS A 170      32.999   7.956   4.075  1.00 19.55
ATOM   1393  CD2 HIS A 170      35.063   7.647   4.703  1.00 18.31
ATOM   1394  CE1 HIS A 170      33.121   6.680   4.401  1.00 19.02
ATOM   1395  NE2 HIS A 170      34.364   6.469   4.786  1.00 18.49
ATOM   1396  N   ARG A 171      32.159  11.948   5.434  1.00 24.70
ATOM   1397  CA  ARG A 171      30.773  12.031   5.899  1.00 28.95
ATOM   1398  C   ARG A 171      29.930  11.589   4.708  1.00 30.70
ATOM   1399  O   ARG A 171      29.820  12.327   3.728  1.00 31.64
ATOM   1400  CB  ARG A 171      30.356  13.466   6.241  1.00 28.54
ATOM   1401  CG  ARG A 171      31.097  14.148   7.364  1.00 29.72
ATOM   1402  CD  ARG A 171      30.518  13.844   8.732  1.00 30.87
ATOM   1403  NE  ARG A 171      31.278  14.576   9.742  1.00 31.42
ATOM   1404  CZ  ARG A 171      30.993  14.606  11.037  1.00 30.16
ATOM   1405  NH1 ARG A 171      30.000  13.882  11.515  1.00 28.80
ATOM   1406  NH2 ARG A 171      31.751  15.306  11.854  1.00 30.31
ATOM   1407  N   ASN A 172      29.345  10.396   4.782  1.00 33.05
ATOM   1408  CA  ASN A 172      28.506   9.883   3.701  1.00 35.12
ATOM   1409  C   ASN A 172      29.247   9.998   2.375  1.00 34.87
ATOM   1410  O   ASN A 172      28.816  10.685   1.438  1.00 35.18
ATOM   1411  CB  ASN A 172      27.172  10.641   3.657  1.00 37.75
ATOM   1412  CG  ASN A 172      26.423  10.575   4.979  1.00 40.16
ATOM   1413  OD1 ASN A 172      26.582   9.626   5.761  1.00 41.27
ATOM   1414  ND2 ASN A 172      25.606  11.583   5.242  1.00 42.11
ATOM   1415  N   ASN A 173      30.442   9.423   2.383  1.00 33.85
ATOM   1416  CA  ASN A 173      31.333   9.385   1.234  1.00 32.75
ATOM   1417  C   ASN A 173      32.029  10.674   0.798  1.00 31.66
ATOM   1418  O   ASN A 173      32.909  10.620  -0.054  1.00 30.64
ATOM   1419  CB  ASN A 173      30.657   8.674   0.069  1.00 34.63
ATOM   1420  CG  ASN A 173      30.513   7.184   0.319  1.00 36.78
ATOM   1421  OD1 ASN A 173      31.409   6.556   0.879  1.00 38.18
ATOM   1422  ND2 ASN A 173      29.378   6.611  -0.077  1.00 38.00
ATOM   1423  N   THR A 174      31.669  11.816   1.389  1.00 29.67
ATOM   1424  CA  THR A 174      32.328  13.083   1.069  1.00 27.29
ATOM   1425  C   THR A 174      33.566  13.209   1.985  1.00 26.16
ATOM   1426  O   THR A 174      33.443  13.175   3.218  1.00 24.09
ATOM   1427  CB  THR A 174      31.404  14.289   1.334  1.00 27.39
ATOM   1428  OG1 THR A 174      30.216  14.186   0.543  1.00 31.04
ATOM   1429  CG2 THR A 174      32.103  15.576   0.984  1.00 29.33
ATOM   1430  N   VAL A 175      34.753  13.327   1.392  1.00 24.34
ATOM   1431  CA  VAL A 175      35.983  13.454   2.173  1.00 21.31
ATOM   1432  C   VAL A 175      36.011  14.763   2.931  1.00 19.43
ATOM   1433  O   VAL A 175      35.672  15.813   2.384  1.00 19.03
ATOM   1434  CB  VAL A 175      37.248  13.344   1.276  1.00 21.85
ATOM   1435  CG1 VAL A 175      38.506  13.694   2.065  1.00 19.43
ATOM   1436  CG2 VAL A 175      37.363  11.926   0.728  1.00 21.32
ATOM   1437  N   THR A 176      36.377  14.692   4.207  1.00 19.02
ATOM   1438  CA  THR A 176      36.460  15.890   5.027  1.00 17.93
ATOM   1439  C   THR A 176      37.922  16.265   5.300  1.00 18.36
ATOM   1440  O   THR A 176      38.454  17.198   4.678  1.00 18.56
ATOM   1441  CB  THR A 176      35.641  15.747   6.344  1.00 16.29
ATOM   1442  OG1 THR A 176      35.995  14.536   7.015  1.00 14.98
ATOM   1443  CG2 THR A 176      34.175  15.683   6.030  1.00 17.05
ATOM   1444  N   GLU A 177      38.571  15.542   6.212  1.00 17.89
ATOM   1445  CA  GLU A 177      39.968  15.789   6.570  1.00 17.79
ATOM   1446  C   GLU A 177      40.501  14.478   7.116  1.00 18.59
ATOM   1447  O   GLU A 177      39.840  13.442   6.988  1.00 20.34
ATOM   1448  CB  GLU A 177      40.065  16.908   7.630  1.00 17.23
ATOM   1449  CG  GLU A 177      39.364  16.578   8.950  1.00 17.02
ATOM   1450  CD  GLU A 177      39.328  17.729   9.943  1.00 17.37
ATOM   1451  OE1 GLU A 177      40.158  18.646   9.854  1.00 15.23
ATOM   1452  OE2 GLU A 177      38.450  17.707  10.828  1.00 17.44
ATOM   1453  N   GLY A 178      41.709  14.486   7.658  1.00 18.53
ATOM   1454  CA  GLY A 178      42.248  13.266   8.230  1.00 18.00
ATOM   1455  C   GLY A 178      42.071  13.332   9.732  1.00 18.46
ATOM   1456  O   GLY A 178      41.604  14.351  10.240  1.00 19.46
ATOM   1457  N   SER A 179      42.484  12.294  10.458  1.00 20.13
ATOM   1458  CA  SER A 179      42.341  12.279  11.924  1.00 20.46
ATOM   1459  C   SER A 179      43.122  13.387  12.624  1.00 20.89
ATOM   1460  O   SER A 179      42.753  13.817  13.724  1.00 20.73
ATOM   1461  CB  SER A 179      42.681  10.903  12.514  1.00 20.18
ATOM   1462  OG  SER A 179      44.043  10.567  12.341  1.00 19.51
ATOM   1463  N   SER A 180      44.221  13.813  12.005  1.00 20.71
ATOM   1464  CA  SER A 180      45.038  14.903  12.519  1.00 20.63
ATOM   1465  C   SER A 180      45.650  15.714  11.372  1.00 20.23
ATOM   1466  O   SER A 180      46.699  16.326  11.529  1.00 21.16
ATOM   1467  CB  SER A 180      46.132  14.382  13.454  1.00 21.02
ATOM   1468  OG  SER A 180      46.853  13.326  12.855  1.00 22.71
ATOM   1469  N   SER A 181      44.969  15.758  10.233  1.00 17.86
ATOM   1470  CA  SER A 181      45.485  16.501   9.088  1.00 16.98
ATOM   1471  C   SER A 181      44.383  16.919   8.133  1.00 16.01
ATOM   1472  O   SER A 181      43.220  16.606   8.347  1.00 15.49
ATOM   1473  CB  SER A 181      46.517  15.661   8.328  1.00 15.93
ATOM   1474  OG  SER A 181      45.988  14.402   7.948  1.00 15.06
ATOM   1475  N   ASN A 182      44.741  17.737   7.153  1.00 15.42
ATOM   1476  CA  ASN A 182      43.799  18.166   6.137  1.00 15.15
ATOM   1477  C   ASN A 182      44.174  17.405   4.864  1.00 15.76
ATOM   1478  O   ASN A 182      45.337  17.052   4.678  1.00 15.48
ATOM   1479  CB  ASN A 182      43.858  19.675   5.943  1.00 14.00
ATOM   1480  CG  ASN A 182      43.208  20.427   7.092  1.00 14.23
ATOM   1481  OD1 ASN A 182      43.883  21.103   7.856  1.00 12.39
ATOM   1482  ND2 ASN A 182      41.884  20.324   7.205  1.00 12.90
ATOM   1483  N   VAL A 183      43.185  17.100   4.027  1.00 15.81
ATOM   1484  CA  VAL A 183      43.423  16.321   2.819  1.00 16.42
ATOM   1485  C   VAL A 183      43.295  17.186   1.583  1.00 16.15
ATOM   1486  O   VAL A 183      42.420  18.046   1.515  1.00 14.73
ATOM   1487  CB  VAL A 183      42.451  15.113   2.740  1.00 17.65
ATOM   1488  CG1 VAL A 183      42.680  14.302   1.470  1.00 17.04
ATOM   1489  CG2 VAL A 183      42.622  14.225   3.972  1.00 18.62
ATOM   1490  N   PHE A 184      44.238  17.013   0.657  1.00 16.03
ATOM   1491  CA  PHE A 184      44.245  17.755  -0.605  1.00 16.98
ATOM   1492  C   PHE A 184      44.342  16.751  -1.747  1.00 16.79
ATOM   1493  O   PHE A 184      45.024  15.737  -1.634  1.00 14.10
ATOM   1494  CB  PHE A 184      45.461  18.663  -0.698  1.00 15.82
ATOM   1495  CG  PHE A 184      45.364  19.894   0.115  1.00 14.98
ATOM   1496  CD1 PHE A 184      45.714  19.881   1.456  1.00 15.76
ATOM   1497  CD2 PHE A 184      44.979  21.091  -0.471  1.00 15.42
ATOM   1498  CE1 PHE A 184      45.688  21.037   2.203  1.00 14.44
ATOM   1499  CE2 PHE A 184      44.950  22.266   0.270  1.00 14.78
ATOM   1500  CZ  PHE A 184      45.309  22.230   1.617  1.00 15.71
ATOM   1501  N   GLY A 185      43.639  17.039  -2.829  1.00 17.99
ATOM   1502  CA  GLY A 185      43.676  16.182  -3.997  1.00 18.32
ATOM   1503  C   GLY A 185      44.055  17.050  -5.183  1.00 19.33
ATOM   1504  O   GLY A 185      43.728  18.236  -5.218  1.00 19.16
ATOM   1505  N   ILE A 186      44.805  16.486  -6.119  1.00 19.88
ATOM   1506  CA  ILE A 186      45.218  17.216  -7.315  1.00 20.03
ATOM   1507  C   ILE A 186      44.760  16.472  -8.561  1.00 19.40
ATOM   1508  O   ILE A 186      45.014  15.282  -8.702  1.00 17.56
ATOM   1509  CB  ILE A 186      46.745  17.377  -7.386  1.00 19.05
ATOM   1510  CG1 ILE A 186      47.238  18.212  -6.199  1.00 20.00
ATOM   1511  CG2 ILE A 186      47.141  18.054  -8.707  1.00 20.22
ATOM   1512  CD1 ILE A 186      48.751  18.289  -6.064  1.00 18.53
ATOM   1513  N   LYS A 187      44.077  17.192  -9.446  1.00 22.37
ATOM   1514  CA  LYS A 187      43.586  16.655 -10.715  1.00 24.20
ATOM   1515  C   LYS A 187      43.829  17.722 -11.792  1.00 24.88
ATOM   1516  O   LYS A 187      43.363  18.855 -11.676  1.00 24.55
ATOM   1517  CB  LYS A 187      42.089  16.320 -10.633  1.00 25.23
ATOM   1518  CG  LYS A 187      41.585  15.487 -11.807  1.00 26.28
ATOM   1519  CD  LYS A 187      42.398  14.211 -11.897  1.00 27.61
ATOM   1520  CE  LYS A 187      41.987  13.358 -13.061  1.00 31.07
ATOM   1521  NZ  LYS A 187      42.851  12.146 -13.096  1.00 32.22
ATOM   1522  N   ASP A 188      44.614  17.361 -12.806  1.00 26.46
ATOM   1523  CA  ASP A 188      44.967  18.263 -13.914  1.00 26.06
ATOM   1524  C   ASP A 188      45.563  19.584 -13.464  1.00 25.20
ATOM   1525  O   ASP A 188      45.216  20.638 -13.994  1.00 26.25
ATOM   1526  CB  ASP A 188      43.776  18.541 -14.845  1.00 28.11
ATOM   1527  CG  ASP A 188      43.152  17.278 -15.394  1.00 31.61
ATOM   1528  OD1 ASP A 188      43.877  16.275 -15.612  1.00 33.16
ATOM   1529  OD2 ASP A 188      41.918  17.290 -15.585  1.00 33.78
ATOM   1530  N   GLY A 189      46.441  19.531 -12.469  1.00 24.26
ATOM   1531  CA  GLY A 189      47.098  20.731 -11.984  1.00 22.54
ATOM   1532  C   GLY A 189      46.227  21.649 -11.147  1.00 22.18
ATOM   1533  O   GLY A 189      46.626  22.770 -10.848  1.00 22.16
ATOM   1534  N   ILE A 190      45.048  21.175 -10.763  1.00 22.22
ATOM   1535  CA  ILE A 190      44.117  21.958  -9.957  1.00 21.64
ATOM   1536  C   ILE A 190      44.071  21.345  -8.556  1.00 20.92
ATOM   1537  O   ILE A 190      43.980  20.128  -8.400  1.00 19.98
ATOM   1538  CB  ILE A 190      42.712  21.994 -10.613  1.00 23.04
ATOM   1539  CG1 ILE A 190      42.825  22.590 -12.026  1.00 23.74
ATOM   1540  CG2 ILE A 190      41.734  22.820  -9.762  1.00 21.90
ATOM   1541  CD1 ILE A 190      41.505  22.734 -12.764  1.00 24.37
ATOM   1542  N   LEU A 191      44.209  22.196  -7.547  1.00 20.33
ATOM   1543  CA  LEU A 191      44.231  21.742  -6.165  1.00 19.54
ATOM   1544  C   LEU A 191      42.850  21.726  -5.530  1.00 19.24
ATOM   1545  O   LEU A 191      42.167  22.735  -5.510  1.00 21.05
ATOM   1546  CB  LEU A 191      45.182  22.621  -5.361  1.00 18.25
ATOM   1547  CG  LEU A 191      45.516  22.238  -3.917  1.00 16.27
ATOM   1548  CD1 LEU A 191      46.269  20.922  -3.870  1.00 14.85
ATOM   1549  CD2 LEU A 191      46.312  23.353  -3.275  1.00 15.83
ATOM   1550  N   TYR A 192      42.439  20.579  -5.015  1.00 19.83
ATOM   1551  CA  TYR A 192      41.125  20.460  -4.393  1.00 21.77
ATOM   1552  C   TYR A 192      41.224  20.138  -2.908  1.00 21.15
ATOM   1553  O   TYR A 192      42.049  19.324  -2.506  1.00 21.75
ATOM   1554  CB  TYR A 192      40.314  19.340  -5.055  1.00 23.16
ATOM   1555  CG  TYR A 192      39.977  19.583  -6.504  1.00 24.84
ATOM   1556  CD1 TYR A 192      38.921  20.409  -6.861  1.00 26.07
ATOM   1557  CD2 TYR A 192      40.729  18.994  -7.518  1.00 25.81
ATOM   1558  CE1 TYR A 192      38.621  20.648  -8.186  1.00 26.70
ATOM   1559  CE2 TYR A 192      40.438  19.223  -8.843  1.00 26.76
ATOM   1560  CZ  TYR A 192      39.386  20.053  -9.175  1.00 27.82
ATOM   1561  OH  TYR A 192      39.127  20.309 -10.500  1.00 29.04
ATOM   1562  N   THR A 193      40.363  20.763  -2.110  1.00 20.39
ATOM   1563  CA  THR A 193      40.304  20.509  -0.681  1.00 19.19
ATOM   1564  C   THR A 193      38.959  21.010  -0.142  1.00 18.27
ATOM   1565  O   THR A 193      38.415  22.020  -0.602  1.00 16.63
ATOM   1566  CB  THR A 193      41.495  21.154   0.079  1.00 20.23
ATOM   1567  OG1 THR A 193      41.695  20.472   1.326  1.00 20.46
ATOM   1568  CG2 THR A 193      41.257  22.628   0.340  1.00 19.51
ATOM   1569  N   HIS A 194      38.409  20.254   0.801  1.00 17.33
ATOM   1570  CA  HIS A 194      37.124  20.554   1.422  1.00 16.47
ATOM   1571  C   HIS A 194      37.169  21.961   1.998  1.00 16.15
ATOM   1572  O   HIS A 194      38.178  22.345   2.591  1.00 17.13
ATOM   1573  CB  HIS A 194      36.886  19.538   2.544  1.00 16.20
ATOM   1574  CG  HIS A 194      35.526  19.620   3.159  1.00 15.36
ATOM   1575  ND1 HIS A 194      35.087  20.725   3.854  1.00 16.59
ATOM   1576  CD2 HIS A 194      34.508  18.731   3.187  1.00 16.12
ATOM   1577  CE1 HIS A 194      33.855  20.516   4.279  1.00 16.64
ATOM   1578  NE2 HIS A 194      33.480  19.315   3.887  1.00 15.63
ATOM   1579  N   PRO A 195      36.093  22.758   1.820  1.00 16.31
ATOM   1580  CA  PRO A 195      36.117  24.122   2.373  1.00 17.09
ATOM   1581  C   PRO A 195      36.168  24.175   3.912  1.00 17.28
ATOM   1582  O   PRO A 195      35.846  23.204   4.592  1.00 17.53
ATOM   1583  CB  PRO A 195      34.860  24.772   1.773  1.00 16.47
ATOM   1584  CG  PRO A 195      33.955  23.621   1.511  1.00 17.03
ATOM   1585  CD  PRO A 195      34.890  22.545   1.001  1.00 15.89
ATOM   1586  N   ALA A 196      36.610  25.306   4.441  1.00 18.73
ATOM   1587  CA  ALA A 196      36.761  25.496   5.875  1.00 19.73
ATOM   1588  C   ALA A 196      35.468  25.874   6.557  1.00 19.68
ATOM   1589  O   ALA A 196      35.201  27.060   6.760  1.00 19.67
ATOM   1590  CB  ALA A 196      37.810  26.566   6.143  1.00 19.79
ATOM   1591  N   ASN A 197      34.623  24.887   6.818  1.00 19.88
ATOM   1592  CA  ASN A 197      33.369  25.157   7.521  1.00 20.63
ATOM   1593  C   ASN A 197      33.376  24.361   8.825  1.00 21.84
ATOM   1594  O   ASN A 197      34.431  23.899   9.255  1.00 21.57
ATOM   1595  CB  ASN A 197      32.135  24.844   6.656  1.00 20.68
ATOM   1596  CG  ASN A 197      32.091  23.415   6.169  1.00 21.23
ATOM   1597  OD1 ASN A 197      32.838  22.560   6.625  1.00 22.61
ATOM   1598  ND2 ASN A 197      31.200  23.148   5.224  1.00 23.70
ATOM   1599  N   ASN A 198      32.209  24.135   9.416  1.00 22.11
ATOM   1600  CA  ASN A 198      32.133  23.408  10.674  1.00 23.01
ATOM   1601  C   ASN A 198      32.564  21.953  10.585  1.00 22.87
ATOM   1602  O   ASN A 198      32.752  21.308  11.613  1.00 22.33
ATOM   1603  CB  ASN A 198      30.716  23.475  11.234  1.00 24.52
ATOM   1604  CG  ASN A 198      29.694  22.777  10.340  1.00 26.61
ATOM   1605  OD1 ASN A 198      29.673  22.980   9.121  1.00 28.43
ATOM   1606  ND2 ASN A 198      28.842  21.955  10.943  1.00 26.44
ATOM   1607  N   MET A 199      32.776  21.457   9.367  1.00 22.38
ATOM   1608  CA  MET A 199      33.144  20.057   9.142  1.00 21.30
ATOM   1609  C   MET A 199      34.620  19.717   9.270  1.00 18.86
ATOM   1610  O   MET A 199      34.966  18.552   9.352  1.00 18.39
ATOM   1611  CB  MET A 199      32.638  19.584   7.774  1.00 25.11
ATOM   1612  CG  MET A 199      31.125  19.694   7.550  1.00 28.09
ATOM   1613  SD  MET A 199      30.227  18.344   8.260  1.00 30.50
ATOM   1614  CE  MET A 199      29.646  19.109   9.743  1.00 31.88
ATOM   1615  N   ILE A 200      35.498  20.707   9.244  1.00 16.78
ATOM   1616  CA  ILE A 200      36.912  20.420   9.381  1.00 16.23
ATOM   1617  C   ILE A 200      37.622  21.472  10.211  1.00 16.50
ATOM   1618  O   ILE A 200      37.050  22.510  10.509  1.00 17.34
ATOM   1619  CB  ILE A 200      37.641  20.393   8.018  1.00 15.60
ATOM   1620  CG1 ILE A 200      37.585  21.767   7.358  1.00 15.74
ATOM   1621  CG2 ILE A 200      37.071  19.319   7.116  1.00 15.54
ATOM   1622  CD1 ILE A 200      38.559  21.926   6.173  1.00 13.43
ATOM   1623  N   ALA A 201      38.868  21.187  10.585  1.00 16.29
ATOM   1624  CA  ALA A 201      39.694  22.145  11.299  1.00 16.99
ATOM   1625  C   ALA A 201      40.327  22.978  10.174  1.00 17.38
ATOM   1626  O   ALA A 201      40.677  22.454   9.121  1.00 18.62
ATOM   1627  CB  ALA A 201      40.788  21.437  12.084  1.00 16.61
ATOM   1628  N   LYS A 202      40.402  24.277  10.361  1.00 17.34
ATOM   1629  CA  LYS A 202      41.016  25.134   9.364  1.00 18.07
ATOM   1630  C   LYS A 202      42.510  25.082   9.680  1.00 17.98
ATOM   1631  O   LYS A 202      43.027  25.941  10.386  1.00 18.77
ATOM   1632  CB  LYS A 202      40.482  26.557   9.492  1.00 18.31
ATOM   1633  CG  LYS A 202      40.801  27.456   8.308  1.00 21.09
ATOM   1634  CD  LYS A 202      40.112  28.794   8.444  1.00 22.71
ATOM   1635  CE  LYS A 202      40.342  29.647   7.215  1.00 27.13
ATOM   1636  NZ  LYS A 202      41.677  30.305   7.181  1.00 28.43
ATOM   1637  N   GLY A 203      43.177  24.033   9.200  1.00 18.66
ATOM   1638  CA  GLY A 203      44.592  23.866   9.449  1.00 16.80
ATOM   1639  C   GLY A 203      45.454  25.043   9.033  1.00 17.27
ATOM   1640  O   GLY A 203      45.213  25.691   8.022  1.00 17.21
ATOM   1641  N   ILE A 204      46.486  25.313   9.815  1.00 16.34
ATOM   1642  CA  ILE A 204      47.414  26.390   9.506  1.00 16.85
ATOM   1643  C   ILE A 204      48.331  25.946   8.353  1.00 15.83
ATOM   1644  O   ILE A 204      48.651  26.723   7.450  1.00 15.64
ATOM   1645  CB  ILE A 204      48.166  26.821  10.775  1.00 17.36
ATOM   1646  CG1 ILE A 204      47.167  27.541  11.673  1.00 18.28
ATOM   1647  CG2 ILE A 204      49.327  27.767  10.452  1.00 16.94
ATOM   1648  CD1 ILE A 204      47.691  27.956  12.969  1.00 23.34
ATOM   1649  N   THR A 205      48.681  24.670   8.341  1.00 15.92
ATOM   1650  CA  THR A 205      49.519  24.141   7.272  1.00 14.96
ATOM   1651  C   THR A 205      48.729  24.188   5.961  1.00 15.16
ATOM   1652  O   THR A 205      49.266  24.520   4.903  1.00 14.87
ATOM   1653  CB  THR A 205      49.936  22.735   7.585  1.00 16.17
ATOM   1654  OG1 THR A 205      50.418  22.701   8.928  1.00 18.73
ATOM   1655  CG2 THR A 205      51.059  22.297   6.655  1.00 16.76
ATOM   1656  N   ARG A 206      47.439  23.899   6.062  1.00 14.67
ATOM   1657  CA  ARG A 206      46.512  23.927   4.937  1.00 15.95
ATOM   1658  C   ARG A 206      46.508  25.294   4.279  1.00 16.59
ATOM   1659  O   ARG A 206      46.585  25.384   3.048  1.00 17.64
ATOM   1660  CB  ARG A 206      45.103  23.609   5.437  1.00 14.04
ATOM   1661  CG  ARG A 206      43.998  23.857   4.476  1.00 11.77
ATOM   1662  CD  ARG A 206      42.700  23.849   5.258  1.00 15.96
ATOM   1663  NE  ARG A 206      41.515  23.876   4.411  1.00 13.65
ATOM   1664  CZ  ARG A 206      40.946  24.981   3.950  1.00 13.81
ATOM   1665  NH1 ARG A 206      41.437  26.174   4.252  1.00 12.64
ATOM   1666  NH2 ARG A 206      39.902  24.891   3.144  1.00 14.88
ATOM   1667  N   ASP A 207      46.401  26.348   5.093  1.00 17.63
ATOM   1668  CA  ASP A 207      46.379  27.722   4.592  1.00 18.70
ATOM   1669  C   ASP A 207      47.727  28.141   4.019  1.00 19.65
ATOM   1670  O   ASP A 207      47.799  28.980   3.121  1.00 18.84
ATOM   1671  CB  ASP A 207      45.960  28.708   5.682  1.00 19.76
ATOM   1672  CG  ASP A 207      44.502  28.545   6.110  1.00 22.10
ATOM   1673  OD1 ASP A 207      43.775  27.676   5.580  1.00 22.46
ATOM   1674  OD2 ASP A 207      44.093  29.293   7.015  1.00 24.15
ATOM   1675  N   VAL A 208      48.803  27.598   4.576  1.00 20.74
ATOM   1676  CA  VAL A 208      50.130  27.899   4.064  1.00 20.73
ATOM   1677  C   VAL A 208      50.267  27.261   2.676  1.00 21.11
ATOM   1678  O   VAL A 208      50.777  27.890   1.757  1.00 22.75
ATOM   1679  CB  VAL A 208      51.231  27.374   4.996  1.00 20.74
ATOM   1680  CG1 VAL A 208      52.585  27.481   4.323  1.00 20.11
ATOM   1681  CG2 VAL A 208      51.240  28.184   6.283  1.00 21.30
ATOM   1682  N   VAL A 209      49.767  26.037   2.521  1.00 21.77
ATOM   1683  CA  VAL A 209      49.820  25.302   1.259  1.00 21.29
ATOM   1684  C   VAL A 209      49.009  26.003   0.165  1.00 22.44
ATOM   1685  O   VAL A 209      49.438  26.076  -0.993  1.00 22.35
ATOM   1686  CB  VAL A 209      49.336  23.835   1.432  1.00 21.67
ATOM   1687  CG1 VAL A 209      49.236  23.137   0.084  1.00 21.93
ATOM   1688  CG2 VAL A 209      50.296  23.068   2.300  1.00 19.87
ATOM   1689  N   ILE A 210      47.845  26.530   0.535  1.00 22.02
ATOM   1690  CA  ILE A 210      46.980  27.245  -0.398  1.00 20.90
ATOM   1691  C   ILE A 210      47.665  28.535  -0.831  1.00 21.58
ATOM   1692  O   ILE A 210      47.507  28.974  -1.963  1.00 20.95
ATOM   1693  CB  ILE A 210      45.613  27.550   0.250  1.00 20.60
ATOM   1694  CG1 ILE A 210      44.821  26.251   0.400  1.00 20.29
ATOM   1695  CG2 ILE A 210      44.841  28.581  -0.548  1.00 20.82
ATOM   1696  CD1 ILE A 210      43.537  26.415   1.189  1.00 20.52
ATOM   1697  N   ALA A 211      48.413  29.146   0.082  1.00 21.60
ATOM   1698  CA  ALA A 211      49.158  30.369  -0.202  1.00 21.40
ATOM   1699  C   ALA A 211      50.305  30.020  -1.158  1.00 21.99
ATOM   1700  O   ALA A 211      50.619  30.798  -2.062  1.00 23.27
ATOM   1701  CB  ALA A 211      49.718  30.967   1.096  1.00 21.69
ATOM   1702  N   CYS A 212      50.926  28.862  -0.950  1.00 21.41
ATOM   1703  CA  CYS A 212      52.015  28.385  -1.803  1.00 22.46
ATOM   1704  C   CYS A 212      51.475  28.174  -3.221  1.00 24.01
ATOM   1705  O   CYS A 212      52.146  28.502  -4.199  1.00 23.59
ATOM   1706  CB  CYS A 212      52.574  27.058  -1.282  1.00 21.72
ATOM   1707  SG  CYS A 212      53.689  27.213   0.120  1.00 21.44
ATOM   1708  N   ALA A 213      50.267  27.614  -3.311  1.00 23.68
ATOM   1709  CA  ALA A 213      49.604  27.358  -4.586  1.00 24.57
ATOM   1710  C   ALA A 213      49.360  28.670  -5.318  1.00 24.09
ATOM   1711  O   ALA A 213      49.645  28.784  -6.508  1.00 24.14
ATOM   1712  CB  ALA A 213      48.285  26.607  -4.367  1.00 24.69
ATOM   1713  N   ASN A 214      48.844  29.668  -4.614  1.00 24.47
ATOM   1714  CA  ASN A 214      48.617  30.965  -5.234  1.00 24.70
ATOM   1715  C   ASN A 214      49.955  31.541  -5.723  1.00 24.83
ATOM   1716  O   ASN A 214      50.028  32.150  -6.790  1.00 24.75
ATOM   1717  CB  ASN A 214      47.952  31.928  -4.251  1.00 25.71
ATOM   1718  CG  ASN A 214      46.535  31.506  -3.872  1.00 27.89
ATOM   1719  OD1 ASN A 214      45.977  30.556  -4.423  1.00 28.59
ATOM   1720  ND2 ASN A 214      45.952  32.209  -2.912  1.00 26.53
ATOM   1721  N   GLU A 215      51.025  31.305  -4.968  1.00 24.44
ATOM   1722  CA  GLU A 215      52.347  31.803  -5.347  1.00 25.16
ATOM   1723  C   GLU A 215      52.881  31.170  -6.629  1.00 23.89
ATOM   1724  O   GLU A 215      53.504  31.856  -7.441  1.00 25.83
ATOM   1725  CB  GLU A 215      53.350  31.643  -4.196  1.00 27.87
ATOM   1726  CG  GLU A 215      53.163  32.681  -3.086  1.00 30.05
ATOM   1727  CD  GLU A 215      53.858  32.330  -1.763  1.00 32.62
ATOM   1728  OE1 GLU A 215      54.739  31.442  -1.727  1.00 33.27
ATOM   1729  OE2 GLU A 215      53.507  32.958  -0.737  1.00 35.06
ATOM   1730  N   ILE A 216      52.670  29.873  -6.820  1.00 21.43
ATOM   1731  CA  ILE A 216      53.132  29.234  -8.049  1.00 20.77
ATOM   1732  C   ILE A 216      52.027  29.139  -9.106  1.00 20.58
ATOM   1733  O   ILE A 216      52.055  28.268  -9.975  1.00 22.03
ATOM   1734  CB  ILE A 216      53.739  27.854  -7.803  1.00 19.00
ATOM   1735  CG1 ILE A 216      52.699  26.923  -7.176  1.00 19.38
ATOM   1736  CG2 ILE A 216      54.985  28.003  -6.944  1.00 20.81
ATOM   1737  CD1 ILE A 216      53.164  25.495  -6.998  1.00 17.51
ATOM   1738  N   ASN A 217      51.049  30.029  -9.000  1.00 20.13
ATOM   1739  CA  ASN A 217      49.924  30.122  -9.931  1.00 20.82
ATOM   1740  C   ASN A 217      49.140  28.853 -10.231  1.00 20.61
ATOM   1741  O   ASN A 217      48.627  28.703 -11.344  1.00 19.91
ATOM   1742  CB  ASN A 217      50.359  30.782 -11.243  1.00 21.11
ATOM   1743  CG  ASN A 217      50.779  32.222 -11.064  1.00 22.87
ATOM   1744  OD1 ASN A 217      49.999  33.060 -10.610  1.00 23.36
ATOM   1745  ND2 ASN A 217      52.016  32.528 -11.445  1.00 22.09
ATOM   1746  N   MET A 218      49.037  27.961  -9.239  1.00 21.03
ATOM   1747  CA  MET A 218      48.274  26.704  -9.340  1.00 22.02
ATOM   1748  C   MET A 218      46.853  27.017  -8.856  1.00 23.07
ATOM   1749  O   MET A 218      46.682  27.583  -7.777  1.00 24.23
ATOM   1750  CB  MET A 218      48.908  25.630  -8.445  1.00 21.76
ATOM   1751  CG  MET A 218      48.062  24.388  -8.237  1.00 21.79
ATOM   1752  SD  MET A 218      48.894  23.110  -7.298  1.00 23.73
ATOM   1753  CE  MET A 218      48.172  21.648  -7.948  1.00 22.81
ATOM   1754  N   PRO A 219      45.822  26.708  -9.668  1.00 23.37
ATOM   1755  CA  PRO A 219      44.409  26.958  -9.342  1.00 22.98
ATOM   1756  C   PRO A 219      43.984  26.168  -8.129  1.00 21.75
ATOM   1757  O   PRO A 219      44.235  24.966  -8.045  1.00 21.47
ATOM   1758  CB  PRO A 219      43.666  26.436 -10.579  1.00 23.01
ATOM   1759  CG  PRO A 219      44.687  26.473 -11.655  1.00 23.58
ATOM   1760  CD  PRO A 219      45.919  25.979 -10.937  1.00 23.74
ATOM   1761  N   VAL A 220      43.280  26.823  -7.222  1.00 21.89
ATOM   1762  CA  VAL A 220      42.840  26.158  -6.002  1.00 22.88
ATOM   1763  C   VAL A 220      41.334  26.155  -5.948  1.00 23.79
ATOM   1764  O   VAL A 220      40.718  27.203  -6.057  1.00 24.83
ATOM   1765  CB  VAL A 220      43.332  26.905  -4.747  1.00 22.73
ATOM   1766  CG1 VAL A 220      42.919  26.150  -3.500  1.00 21.98
ATOM   1767  CG2 VAL A 220      44.838  27.100  -4.792  1.00 21.98
ATOM   1768  N   LYS A 221      40.738  24.987  -5.800  1.00 25.25
ATOM   1769  CA  LYS A 221      39.301  24.904  -5.698  1.00 27.84
ATOM   1770  C   LYS A 221      38.940  24.276  -4.350  1.00 27.21
ATOM   1771  O   LYS A 221      39.358  23.164  -4.038  1.00 26.74
ATOM   1772  CB  LYS A 221      38.723  24.088  -6.864  1.00 30.56
ATOM   1773  CG  LYS A 221      38.832  24.789  -8.221  1.00 33.68
ATOM   1774  CD  LYS A 221      38.275  23.927  -9.363  1.00 36.86
ATOM   1775  CE  LYS A 221      38.236  24.702 -10.697  1.00 38.84
ATOM   1776  NZ  LYS A 221      37.325  25.904 -10.648  1.00 40.48
ATOM   1777  N   GLU A 222      38.243  25.038  -3.516  1.00 27.49
ATOM   1778  CA  GLU A 222      37.811  24.549  -2.211  1.00 27.11
ATOM   1779  C   GLU A 222      36.420  23.966  -2.403  1.00 26.25
ATOM   1780  O   GLU A 222      35.409  24.611  -2.143  1.00 26.66
ATOM   1781  CB  GLU A 222      37.802  25.691  -1.192  1.00 27.06
ATOM   1782  CG  GLU A 222      39.175  26.237  -0.911  1.00 28.49
ATOM   1783  CD  GLU A 222      39.194  27.214   0.238  1.00 29.75
ATOM   1784  OE1 GLU A 222      38.911  26.798   1.375  1.00 31.15
ATOM   1785  OE2 GLU A 222      39.503  28.398   0.009  1.00 30.87
ATOM   1786  N   ILE A 223      36.390  22.738  -2.889  1.00 26.24
ATOM   1787  CA  ILE A 223      35.157  22.035  -3.180  1.00 26.55
ATOM   1788  C   ILE A 223      35.380  20.639  -2.664  1.00 25.37
ATOM   1789  O   ILE A 223      36.443  20.071  -2.880  1.00 25.64
ATOM   1790  CB  ILE A 223      34.940  21.957  -4.716  1.00 28.26
ATOM   1791  CG1 ILE A 223      34.660  23.345  -5.287  1.00 29.46
ATOM   1792  CG2 ILE A 223      33.805  21.017  -5.062  1.00 29.52
ATOM   1793  CD1 ILE A 223      34.573  23.356  -6.824  1.00 32.33
ATOM   1794  N   PRO A 224      34.386  20.064  -1.977  1.00 24.63
ATOM   1795  CA  PRO A 224      34.534  18.714  -1.444  1.00 25.61
ATOM   1796  C   PRO A 224      34.583  17.665  -2.527  1.00 25.54
ATOM   1797  O   PRO A 224      33.964  17.811  -3.575  1.00 27.89
ATOM   1798  CB  PRO A 224      33.263  18.534  -0.613  1.00 24.54
ATOM   1799  CG  PRO A 224      32.821  19.901  -0.316  1.00 25.27
ATOM   1800  CD  PRO A 224      33.086  20.628  -1.585  1.00 24.76
ATOM   1801  N   PHE A 225      35.283  16.579  -2.258  1.00 26.34
ATOM   1802  CA  PHE A 225      35.343  15.488  -3.208  1.00 25.64
ATOM   1803  C   PHE A 225      35.054  14.180  -2.488  1.00 25.97
ATOM   1804  O   PHE A 225      35.295  14.058  -1.290  1.00 26.97
ATOM   1805  CB  PHE A 225      36.665  15.463  -3.979  1.00 24.79
ATOM   1806  CG  PHE A 225      37.897  15.488  -3.119  1.00 22.56
ATOM   1807  CD1 PHE A 225      38.480  14.306  -2.686  1.00 22.27
ATOM   1808  CD2 PHE A 225      38.519  16.693  -2.808  1.00 22.36
ATOM   1809  CE1 PHE A 225      39.670  14.322  -1.960  1.00 21.59
ATOM   1810  CE2 PHE A 225      39.703  16.716  -2.085  1.00 21.08
ATOM   1811  CZ  PHE A 225      40.280  15.524  -1.661  1.00 19.38
ATOM   1812  N   THR A 226      34.498  13.222  -3.211  1.00 25.48
ATOM   1813  CA  THR A 226      34.126  11.945  -2.640  1.00 25.43
ATOM   1814  C   THR A 226      35.302  11.002  -2.501  1.00 25.78
ATOM   1815  O   THR A 226      36.383  11.262  -3.034  1.00 25.96
ATOM   1816  CB  THR A 226      33.016  11.265  -3.485  1.00 26.29
ATOM   1817  OG1 THR A 226      33.531  10.947  -4.789  1.00 28.11
ATOM   1818  CG2 THR A 226      31.814  12.200  -3.642  1.00 25.51
ATOM   1819  N   THR A 227      35.084   9.902  -1.783  1.00 26.17
ATOM   1820  CA  THR A 227      36.122   8.901  -1.578  1.00 27.63
ATOM   1821  C   THR A 227      36.492   8.301  -2.935  1.00 28.14
ATOM   1822  O   THR A 227      37.657   8.020  -3.211  1.00 29.05
ATOM   1823  CB  THR A 227      35.664   7.770  -0.590  1.00 27.75
ATOM   1824  OG1 THR A 227      34.487   7.117  -1.083  1.00 28.75
ATOM   1825  CG2 THR A 227      35.376   8.337   0.792  1.00 27.08
ATOM   1826  N   HIS A 228      35.490   8.172  -3.795  1.00 29.11
ATOM   1827  CA  HIS A 228      35.664   7.615  -5.132  1.00 29.53
ATOM   1828  C   HIS A 228      36.378   8.621  -6.030  1.00 28.97
ATOM   1829  O   HIS A 228      37.202   8.249  -6.855  1.00 29.94
ATOM   1830  CB  HIS A 228      34.300   7.237  -5.725  1.00 30.53
ATOM   1831  CG  HIS A 228      33.398   6.534  -4.756  1.00 30.98
ATOM   1832  ND1 HIS A 228      32.114   6.961  -4.489  1.00 31.18
ATOM   1833  CD2 HIS A 228      33.614   5.461  -3.956  1.00 31.06
ATOM   1834  CE1 HIS A 228      31.578   6.184  -3.564  1.00 31.50
ATOM   1835  NE2 HIS A 228      32.468   5.267  -3.223  1.00 31.77
ATOM   1836  N   GLU A 229      36.076   9.900  -5.867  1.00 28.98
ATOM   1837  CA  GLU A 229      36.742  10.907  -6.672  1.00 29.33
ATOM   1838  C   GLU A 229      38.207  11.002  -6.257  1.00 30.09
ATOM   1839  O   GLU A 229      39.084  11.157  -7.105  1.00 30.60
ATOM   1840  CB  GLU A 229      36.050  12.256  -6.543  1.00 29.72
ATOM   1841  CG  GLU A 229      34.762  12.345  -7.331  1.00 31.20
ATOM   1842  CD  GLU A 229      34.018  13.638  -7.099  1.00 32.25
ATOM   1843  OE1 GLU A 229      34.108  14.179  -5.989  1.00 34.23
ATOM   1844  OE2 GLU A 229      33.332  14.123  -8.019  1.00 34.17
ATOM   1845  N   ALA A 230      38.481  10.844  -4.962  1.00 30.84
ATOM   1846  CA  ALA A 230      39.853  10.906  -4.463  1.00 30.04
ATOM   1847  C   ALA A 230      40.699   9.802  -5.087  1.00 30.33
ATOM   1848  O   ALA A 230      41.845  10.027  -5.454  1.00 30.13
ATOM   1849  CB  ALA A 230      39.883  10.795  -2.952  1.00 30.04
ATOM   1850  N   LEU A 231      40.130   8.612  -5.211  1.00 30.80
ATOM   1851  CA  LEU A 231      40.843   7.488  -5.808  1.00 31.46
ATOM   1852  C   LEU A 231      41.143   7.721  -7.301  1.00 31.72
ATOM   1853  O   LEU A 231      41.963   7.025  -7.898  1.00 32.08
ATOM   1854  CB  LEU A 231      40.049   6.188  -5.605  1.00 32.01
ATOM   1855  CG  LEU A 231      39.906   5.664  -4.167  1.00 32.70
ATOM   1856  CD1 LEU A 231      38.975   4.465  -4.138  1.00 31.92
ATOM   1857  CD2 LEU A 231      41.269   5.285  -3.592  1.00 32.54
ATOM   1858  N   LYS A 232      40.496   8.713  -7.901  1.00 32.24
ATOM   1859  CA  LYS A 232      40.727   9.019  -9.313  1.00 32.72
ATOM   1860  C   LYS A 232      41.568  10.295  -9.465  1.00 32.07
ATOM   1861  O   LYS A 232      41.618  10.891 -10.543  1.00 32.68
ATOM   1862  CB  LYS A 232      39.396   9.174 -10.063  1.00 33.40
ATOM   1863  CG  LYS A 232      38.517   7.927 -10.089  1.00 34.53
ATOM   1864  CD  LYS A 232      37.175   8.203 -10.778  1.00 36.02
ATOM   1865  CE  LYS A 232      36.141   7.134 -10.437  1.00 36.37
ATOM   1866  NZ  LYS A 232      36.416   5.840 -11.104  1.00 37.02
ATOM   1867  N   MET A 233      42.178  10.749  -8.373  1.00 30.13
ATOM   1868  CA  MET A 233      43.012  11.943  -8.415  1.00 28.53
ATOM   1869  C   MET A 233      44.394  11.597  -8.974  1.00 27.55
ATOM   1870  O   MET A 233      44.823  10.440  -8.918  1.00 27.09
ATOM   1871  CB  MET A 233      43.166  12.532  -7.005  1.00 28.29
ATOM   1872  CG  MET A 233      41.902  13.132  -6.414  1.00 27.17
ATOM   1873  SD  MET A 233      41.512  14.716  -7.108  1.00 28.77
ATOM   1874  CE  MET A 233      39.853  14.924  -6.526  1.00 29.26
ATOM   1875  N   ASP A 234      45.079  12.600  -9.523  1.00 26.84
ATOM   1876  CA  ASP A 234      46.432  12.418 -10.051  1.00 25.30
ATOM   1877  C   ASP A 234      47.389  12.348  -8.871  1.00 24.85
ATOM   1878  O   ASP A 234      48.318  11.544  -8.845  1.00 23.67
ATOM   1879  CB  ASP A 234      46.826  13.599 -10.941  1.00 25.36
ATOM   1880  CG  ASP A 234      46.141  13.572 -12.302  1.00 25.35
ATOM   1881  OD1 ASP A 234      45.873  12.464 -12.817  1.00 26.91
ATOM   1882  OD2 ASP A 234      45.886  14.661 -12.858  1.00 23.01
ATOM   1883  N   GLU A 235      47.152  13.214  -7.891  1.00 24.35
ATOM   1884  CA  GLU A 235      47.975  13.261  -6.696  1.00 23.82
ATOM   1885  C   GLU A 235      47.108  13.523  -5.467  1.00 23.57
ATOM   1886  O   GLU A 235      46.021  14.098  -5.568  1.00 21.68
ATOM   1887  CB  GLU A 235      49.010  14.358  -6.823  1.00 23.03
ATOM   1888  CG  GLU A 235      49.815  14.290  -8.083  1.00 24.82
ATOM   1889  CD  GLU A 235      50.678  15.497  -8.242  1.00 25.13
ATOM   1890  OE1 GLU A 235      51.467  15.773  -7.328  1.00 27.23
ATOM   1891  OE2 GLU A 235      50.549  16.198  -9.254  1.00 26.56
ATOM   1892  N   LEU A 236      47.612  13.113  -4.309  1.00 23.94
ATOM   1893  CA  LEU A 236      46.901  13.283  -3.050  1.00 24.06
ATOM   1894  C   LEU A 236      47.911  13.447  -1.926  1.00 22.33
ATOM   1895  O   LEU A 236      48.963  12.803  -1.934  1.00 20.83
ATOM   1896  CB  LEU A 236      46.044  12.046  -2.753  1.00 26.88
ATOM   1897  CG  LEU A 236      44.829  12.293  -1.859  1.00 28.61
ATOM   1898  CD1 LEU A 236      43.659  12.701  -2.735  1.00 31.15
ATOM   1899  CD2 LEU A 236      44.480  11.057  -1.072  1.00 30.18
ATOM   1900  N   PHE A 237      47.587  14.299  -0.957  1.00 20.96
ATOM   1901  CA  PHE A 237      48.472  14.508   0.177  1.00 19.68
ATOM   1902  C   PHE A 237      47.730  15.073   1.373  1.00 18.95
ATOM   1903  O   PHE A 237      46.639  15.633   1.232  1.00 17.51
ATOM   1904  CB  PHE A 237      49.682  15.405  -0.189  1.00 17.87
ATOM   1905  CG  PHE A 237      49.341  16.854  -0.497  1.00 17.33
ATOM   1906  CD1 PHE A 237      49.165  17.785   0.526  1.00 16.62
ATOM   1907  CD2 PHE A 237      49.250  17.298  -1.816  1.00 17.06
ATOM   1908  CE1 PHE A 237      48.907  19.121   0.240  1.00 18.09
ATOM   1909  CE2 PHE A 237      48.996  18.630  -2.107  1.00 17.83
ATOM   1910  CZ  PHE A 237      48.822  19.549  -1.077  1.00 16.57
ATOM   1911  N   VAL A 238      48.314  14.883   2.551  1.00 18.56
ATOM   1912  CA  VAL A 238      47.743  15.418   3.781  1.00 18.03
ATOM   1913  C   VAL A 238      48.739  16.396   4.382  1.00 18.63
ATOM   1914  O   VAL A 238      49.962  16.291   4.157  1.00 19.15
ATOM   1915  CB  VAL A 238      47.405  14.323   4.831  1.00 18.49
ATOM   1916  CG1 VAL A 238      46.357  13.377   4.286  1.00 17.09
ATOM   1917  CG2 VAL A 238      48.649  13.580   5.269  1.00 17.27
ATOM   1918  N   THR A 239      48.206  17.369   5.114  1.00 17.61
ATOM   1919  CA  THR A 239      49.010  18.393   5.761  1.00 16.27
ATOM   1920  C   THR A 239      48.686  18.506   7.256  1.00 16.18
ATOM   1921  O   THR A 239      47.557  18.275   7.672  1.00 16.03
ATOM   1922  CB  THR A 239      48.733  19.788   5.133  1.00 14.02
ATOM   1923  OG1 THR A 239      47.349  20.109   5.288  1.00 11.00
ATOM   1924  CG2 THR A 239      49.051  19.802   3.652  1.00 13.95
ATOM   1925  N   SER A 240      49.699  18.811   8.052  1.00 17.09
ATOM   1926  CA  SER A 240      49.561  19.046   9.494  1.00 18.42
ATOM   1927  C   SER A 240      50.882  19.679   9.903  1.00 19.84
ATOM   1928  O   SER A 240      51.861  19.622   9.151  1.00 20.38
ATOM   1929  CB  SER A 240      49.251  17.767  10.302  1.00 18.28
ATOM   1930  OG  SER A 240      50.407  17.022  10.618  1.00 18.50
ATOM   1931  N   THR A 241      50.870  20.398  11.013  1.00 21.04
ATOM   1932  CA  THR A 241      52.055  21.061  11.526  1.00 21.37
ATOM   1933  C   THR A 241      53.235  20.115  11.612  1.00 22.28
ATOM   1934  O   THR A 241      54.368  20.518  11.380  1.00 22.91
ATOM   1935  CB  THR A 241      51.772  21.633  12.900  1.00 20.54
ATOM   1936  OG1 THR A 241      50.813  22.679  12.765  1.00 21.53
ATOM   1937  CG2 THR A 241      53.030  22.188  13.530  1.00 18.90
ATOM   1938  N   THR A 242      52.968  18.861  11.957  1.00 23.15
ATOM   1939  CA  THR A 242      54.025  17.861  12.071  1.00 25.05
ATOM   1940  C   THR A 242      54.269  17.046  10.801  1.00 23.80
ATOM   1941  O   THR A 242      55.361  16.540  10.604  1.00 24.96
ATOM   1942  CB  THR A 242      53.766  16.907  13.251  1.00 25.03
ATOM   1943  OG1 THR A 242      52.393  16.512  13.244  1.00 27.44
ATOM   1944  CG2 THR A 242      54.068  17.604  14.558  1.00 25.40
ATOM   1945  N   SER A 243      53.248  16.890   9.966  1.00 23.74
ATOM   1946  CA  SER A 243      53.391  16.142   8.719  1.00 23.28
ATOM   1947  C   SER A 243      53.868  17.028   7.587  1.00 22.53
ATOM   1948  O   SER A 243      54.353  16.541   6.575  1.00 21.85
ATOM   1949  CB  SER A 243      52.047  15.538   8.299  1.00 23.47
ATOM   1950  OG  SER A 243      51.664  14.472   9.148  1.00 26.26
ATOM   1951  N   GLU A 244      53.742  18.335   7.766  1.00 23.39
ATOM   1952  CA  GLU A 244      54.086  19.288   6.716  1.00 23.52
ATOM   1953  C   GLU A 244      53.292  18.843   5.477  1.00 23.59
ATOM   1954  O   GLU A 244      52.067  18.742   5.557  1.00 23.31
ATOM   1955  CB  GLU A 244      55.588  19.295   6.469  1.00 24.01
ATOM   1956  CG  GLU A 244      56.384  19.680   7.706  1.00 23.10
ATOM   1957  CD  GLU A 244      57.866  19.615   7.475  1.00 23.36
ATOM   1958  OE1 GLU A 244      58.292  19.563   6.303  1.00 24.33
ATOM   1959  OE2 GLU A 244      58.610  19.626   8.461  1.00 22.99
ATOM   1960  N   ILE A 245      53.962  18.536   4.368  1.00 21.86
ATOM   1961  CA  ILE A 245      53.268  18.078   3.168  1.00 22.92
ATOM   1962  C   ILE A 245      53.620  16.615   2.918  1.00 22.40
ATOM   1963  O   ILE A 245      54.636  16.312   2.286  1.00 22.62
ATOM   1964  CB  ILE A 245      53.620  18.961   1.929  1.00 23.17
ATOM   1965  CG1 ILE A 245      53.096  20.379   2.158  1.00 22.48
ATOM   1966  CG2 ILE A 245      53.009  18.374   0.660  1.00 23.74
ATOM   1967  CD1 ILE A 245      53.467  21.360   1.121  1.00 22.61
ATOM   1968  N   THR A 246      52.781  15.715   3.418  1.00 21.43
ATOM   1969  CA  THR A 246      53.009  14.286   3.269  1.00 21.07
ATOM   1970  C   THR A 246      52.177  13.675   2.155  1.00 21.54
ATOM   1971  O   THR A 246      50.953  13.709   2.182  1.00 22.01
ATOM   1972  CB  THR A 246      52.738  13.518   4.578  1.00 20.97
ATOM   1973  OG1 THR A 246      53.666  13.945   5.590  1.00 23.42
ATOM   1974  CG2 THR A 246      52.870  12.012   4.347  1.00 18.95
ATOM   1975  N   PRO A 247      52.849  13.125   1.139  1.00 22.08
ATOM   1976  CA  PRO A 247      52.225  12.488  -0.017  1.00 21.79
ATOM   1977  C   PRO A 247      51.548  11.187   0.371  1.00 22.98
ATOM   1978  O   PRO A 247      52.099  10.400   1.140  1.00 22.18
ATOM   1979  CB  PRO A 247      53.421  12.194  -0.930  1.00 22.72
ATOM   1980  CG  PRO A 247      54.448  13.228  -0.538  1.00 21.62
ATOM   1981  CD  PRO A 247      54.308  13.260   0.953  1.00 22.42
ATOM   1982  N   VAL A 248      50.358  10.952  -0.167  1.00 23.57
ATOM   1983  CA  VAL A 248      49.641   9.710   0.085  1.00 26.04
ATOM   1984  C   VAL A 248      49.700   9.015  -1.262  1.00 28.07
ATOM   1985  O   VAL A 248      49.200   9.553  -2.254  1.00 29.23
ATOM   1986  CB  VAL A 248      48.161   9.954   0.474  1.00 24.70
ATOM   1987  CG1 VAL A 248      47.371   8.648   0.418  1.00 22.29
ATOM   1988  CG2 VAL A 248      48.091  10.555   1.875  1.00 24.55
ATOM   1989  N   ILE A 249      50.359   7.865  -1.318  1.00 30.12
ATOM   1990  CA  ILE A 249      50.487   7.147  -2.581  1.00 31.95
ATOM   1991  C   ILE A 249      49.555   5.952  -2.716  1.00 32.83
ATOM   1992  O   ILE A 249      49.331   5.464  -3.817  1.00 33.33
ATOM   1993  CB  ILE A 249      51.941   6.693  -2.819  1.00 32.06
ATOM   1994  CG1 ILE A 249      52.398   5.790  -1.678  1.00 33.53
ATOM   1995  CG2 ILE A 249      52.855   7.907  -2.935  1.00 32.22
ATOM   1996  CD1 ILE A 249      53.716   5.110  -1.927  1.00 35.96
ATOM   1997  N   GLU A 250      48.977   5.509  -1.607  1.00 34.16
ATOM   1998  CA  GLU A 250      48.083   4.356  -1.624  1.00 34.97
ATOM   1999  C   GLU A 250      46.994   4.457  -0.553  1.00 34.63
ATOM   2000  O   GLU A 250      47.269   4.828   0.586  1.00 34.38
ATOM   2001  CB  GLU A 250      48.910   3.098  -1.386  1.00 37.33
ATOM   2002  CG  GLU A 250      48.107   1.828  -1.218  1.00 40.32
ATOM   2003  CD  GLU A 250      48.958   0.680  -0.713  1.00 42.86
ATOM   2004  OE1 GLU A 250      50.037   0.431  -1.303  1.00 44.36
ATOM   2005  OE2 GLU A 250      48.552   0.032   0.283  1.00 44.82
ATOM   2006  N   ILE A 251      45.761   4.138  -0.923  1.00 34.08
ATOM   2007  CA  ILE A 251      44.645   4.172   0.020  1.00 35.04
ATOM   2008  C   ILE A 251      43.886   2.873  -0.098  1.00 35.82
ATOM   2009  O   ILE A 251      43.245   2.628  -1.111  1.00 36.39
ATOM   2010  CB  ILE A 251      43.637   5.297  -0.275  1.00 33.71
ATOM   2011  CG1 ILE A 251      44.318   6.659  -0.238  1.00 32.66
ATOM   2012  CG2 ILE A 251      42.514   5.269   0.760  1.00 34.67
ATOM   2013  CD1 ILE A 251      43.390   7.776  -0.561  1.00 31.17
ATOM   2014  N   ASP A 252      43.990   2.029   0.922  1.00 37.80
ATOM   2015  CA  ASP A 252      43.295   0.748   0.949  1.00 39.09
ATOM   2016  C   ASP A 252      43.692  -0.176  -0.199  1.00 39.95
ATOM   2017  O   ASP A 252      42.838  -0.787  -0.838  1.00 39.96
ATOM   2018  CB  ASP A 252      41.764   0.956   0.976  1.00 39.19
ATOM   2019  CG  ASP A 252      41.257   1.478   2.325  1.00 40.23
ATOM   2020  OD1 ASP A 252      41.886   1.161   3.360  1.00 41.19
ATOM   2021  OD2 ASP A 252      40.225   2.191   2.352  1.00 39.11
ATOM   2022  N   GLY A 253      44.994  -0.293  -0.444  1.00 40.51
ATOM   2023  CA  GLY A 253      45.461  -1.164  -1.506  1.00 40.96
ATOM   2024  C   GLY A 253      45.415  -0.567  -2.902  1.00 41.48
ATOM   2025  O   GLY A 253      46.122  -1.037  -3.795  1.00 42.64
ATOM   2026  N   LYS A 254      44.567   0.431  -3.115  1.00 41.03
ATOM   2027  CA  LYS A 254      44.477   1.080  -4.414  1.00 40.20
ATOM   2028  C   LYS A 254      45.504   2.197  -4.432  1.00 39.82
ATOM   2029  O   LYS A 254      45.512   3.060  -3.554  1.00 39.33
ATOM   2030  CB  LYS A 254      43.081   1.661  -4.640  1.00 41.07
ATOM   2031  CG  LYS A 254      41.953   0.659  -4.487  1.00 42.28
ATOM   2032  CD  LYS A 254      40.610   1.333  -4.687  1.00 43.40
ATOM   2033  CE  LYS A 254      39.473   0.514  -4.091  1.00 44.02
ATOM   2034  NZ  LYS A 254      39.708   0.166  -2.660  1.00 44.18
ATOM   2035  N   LEU A 255      46.427   2.117  -5.381  1.00 39.60
ATOM   2036  CA  LEU A 255      47.470   3.119  -5.536  1.00 38.66
ATOM   2037  C   LEU A 255      46.860   4.340  -6.191  1.00 37.43
ATOM   2038  O   LEU A 255      45.858   4.232  -6.894  1.00 37.35
ATOM   2039  CB  LEU A 255      48.601   2.584  -6.416  1.00 39.65
ATOM   2040  CG  LEU A 255      49.474   1.469  -5.853  1.00 40.62
ATOM   2041  CD1 LEU A 255      48.709   0.159  -5.770  1.00 41.46
ATOM   2042  CD2 LEU A 255      50.677   1.316  -6.756  1.00 42.61
ATOM   2043  N   ILE A 256      47.430   5.505  -5.903  1.00 35.98
ATOM   2044  CA  ILE A 256      46.952   6.759  -6.473  1.00 34.75
ATOM   2045  C   ILE A 256      47.809   6.899  -7.732  1.00 35.73
ATOM   2046  O   ILE A 256      49.044   6.898  -7.652  1.00 35.79
ATOM   2047  CB  ILE A 256      47.169   7.944  -5.485  1.00 32.16
ATOM   2048  CG1 ILE A 256      46.471   7.653  -4.144  1.00 31.22
ATOM   2049  CG2 ILE A 256      46.627   9.250  -6.064  1.00 31.51
ATOM   2050  CD1 ILE A 256      44.963   7.597  -4.203  1.00 28.90
ATOM   2051  N   ARG A 257      47.152   6.973  -8.886  1.00 36.75
ATOM   2052  CA  ARG A 257      47.835   7.056 -10.183  1.00 38.82
ATOM   2053  C   ARG A 257      48.846   5.908 -10.280  1.00 38.50
ATOM   2054  O   ARG A 257      48.449   4.759 -10.474  1.00 39.33
ATOM   2055  CB  ARG A 257      48.502   8.427 -10.417  1.00 40.30
ATOM   2056  CG  ARG A 257      48.956   8.670 -11.877  1.00 43.13
ATOM   2057  CD  ARG A 257      49.441  10.128 -12.136  1.00 45.67
ATOM   2058  NE  ARG A 257      50.648  10.465 -11.368  1.00 48.84
ATOM   2059  CZ  ARG A 257      51.242  11.661 -11.356  1.00 49.64
ATOM   2060  NH1 ARG A 257      50.761  12.673 -12.073  1.00 49.58
ATOM   2061  NH2 ARG A 257      52.305  11.855 -10.580  1.00 51.72
ATOM   2062  N   ASP A 258      50.129   6.185 -10.078  1.00 38.68
ATOM   2063  CA  ASP A 258      51.128   5.122 -10.162  1.00 39.32
ATOM   2064  C   ASP A 258      51.750   4.705  -8.834  1.00 38.85
ATOM   2065  O   ASP A 258      52.457   3.697  -8.753  1.00 38.30
ATOM   2066  CB  ASP A 258      52.221   5.478 -11.186  1.00 41.26
ATOM   2067  CG  ASP A 258      52.773   6.897 -11.019  1.00 42.58
ATOM   2068  OD1 ASP A 258      52.475   7.573 -10.002  1.00 42.51
ATOM   2069  OD2 ASP A 258      53.511   7.332 -11.936  1.00 43.68
ATOM   2070  N   GLY A 259      51.459   5.461  -7.784  1.00 38.64
ATOM   2071  CA  GLY A 259      52.021   5.138  -6.486  1.00 37.92
ATOM   2072  C   GLY A 259      53.344   5.848  -6.300  1.00 37.91
ATOM   2073  O   GLY A 259      54.216   5.409  -5.543  1.00 37.29
ATOM   2074  N   LYS A 260      53.494   6.954  -7.016  1.00 38.09
ATOM   2075  CA  LYS A 260      54.697   7.768  -6.950  1.00 38.27
ATOM   2076  C   LYS A 260      54.237   9.167  -6.579  1.00 37.13
ATOM   2077  O   LYS A 260      53.102   9.548  -6.885  1.00 37.57
ATOM   2078  CB  LYS A 260      55.401   7.796  -8.317  1.00 39.96
ATOM   2079  CG  LYS A 260      55.849   6.428  -8.812  1.00 42.09
ATOM   2080  CD  LYS A 260      56.567   6.490 -10.158  1.00 44.31
ATOM   2081  CE  LYS A 260      57.069   5.095 -10.551  1.00 45.35
ATOM   2082  NZ  LYS A 260      57.745   5.068 -11.889  1.00 48.00
ATOM   2083  N   VAL A 261      55.096   9.919  -5.901  1.00 35.35
ATOM   2084  CA  VAL A 261      54.757  11.275  -5.510  1.00 34.36
ATOM   2085  C   VAL A 261      54.656  12.103  -6.779  1.00 34.65
ATOM   2086  O   VAL A 261      55.597  12.152  -7.567  1.00 36.34
ATOM   2087  CB  VAL A 261      55.829  11.892  -4.581  1.00 33.32
ATOM   2088  CG1 VAL A 261      55.439  13.310  -4.204  1.00 31.48
ATOM   2089  CG2 VAL A 261      56.017  11.032  -3.336  1.00 30.65
ATOM   2090  N   GLY A 262      53.515  12.741  -6.980  1.00 34.21
ATOM   2091  CA  GLY A 262      53.335  13.542  -8.173  1.00 33.65
ATOM   2092  C   GLY A 262      54.197  14.786  -8.273  1.00 33.79
ATOM   2093  O   GLY A 262      54.802  15.227  -7.299  1.00 34.26
ATOM   2094  N   GLU A 263      54.157  15.399  -9.451  1.00 33.38
ATOM   2095  CA  GLU A 263      54.907  16.606  -9.792  1.00 32.77
ATOM   2096  C   GLU A 263      54.440  17.873  -9.067  1.00 30.90
ATOM   2097  O   GLU A 263      55.257  18.696  -8.667  1.00 29.65
ATOM   2098  CB  GLU A 263      54.843  16.824 -11.321  1.00 35.04
ATOM   2099  CG  GLU A 263      55.541  18.097 -11.831  1.00 39.70
ATOM   2100  CD  GLU A 263      55.262  18.401 -13.315  1.00 42.93
ATOM   2101  OE1 GLU A 263      54.219  19.043 -13.608  1.00 44.29
ATOM   2102  OE2 GLU A 263      56.099  18.030 -14.189  1.00 45.14
ATOM   2103  N   TRP A 264      53.126  18.064  -8.944  1.00 30.18
ATOM   2104  CA  TRP A 264      52.612  19.259  -8.277  1.00 28.63
ATOM   2105  C   TRP A 264      52.851  19.199  -6.771  1.00 27.73
ATOM   2106  O   TRP A 264      53.111  20.225  -6.143  1.00 26.84
ATOM   2107  CB  TRP A 264      51.135  19.477  -8.605  1.00 29.98
ATOM   2108  CG  TRP A 264      50.900  19.825 -10.045  1.00 29.60
ATOM   2109  CD1 TRP A 264      50.550  18.967 -11.051  1.00 29.54
ATOM   2110  CD2 TRP A 264      51.002  21.122 -10.639  1.00 29.59
ATOM   2111  NE1 TRP A 264      50.427  19.652 -12.235  1.00 30.30
ATOM   2112  CE2 TRP A 264      50.697  20.977 -12.013  1.00 30.14
ATOM   2113  CE3 TRP A 264      51.315  22.396 -10.145  1.00 31.00
ATOM   2114  CZ2 TRP A 264      50.697  22.059 -12.903  1.00 31.05
ATOM   2115  CZ3 TRP A 264      51.314  23.482 -11.036  1.00 31.95
ATOM   2116  CH2 TRP A 264      51.005  23.302 -12.397  1.00 31.85
ATOM   2117  N   THR A 265      52.792  17.990  -6.212  1.00 26.30
ATOM   2118  CA  THR A 265      53.053  17.787  -4.796  1.00 26.60
ATOM   2119  C   THR A 265      54.496  18.248  -4.569  1.00 26.29
ATOM   2120  O   THR A 265      54.761  19.054  -3.676  1.00 26.60
ATOM   2121  CB  THR A 265      52.881  16.300  -4.381  1.00 26.28
ATOM   2122  OG1 THR A 265      51.497  15.936  -4.457  1.00 27.83
ATOM   2123  CG2 THR A 265      53.373  16.060  -2.959  1.00 26.72
ATOM   2124  N   ARG A 266      55.400  17.838  -5.459  1.00 25.17
ATOM   2125  CA  ARG A 266      56.809  18.228  -5.364  1.00 23.30
ATOM   2126  C   ARG A 266      56.981  19.735  -5.467  1.00 22.91
ATOM   2127  O   ARG A 266      57.770  20.327  -4.753  1.00 22.45
ATOM   2128  CB  ARG A 266      57.651  17.519  -6.428  1.00 23.60
ATOM   2129  CG  ARG A 266      57.852  16.019  -6.189  1.00 23.09
ATOM   2130  CD  ARG A 266      58.749  15.737  -4.993  1.00 23.65
ATOM   2131  NE  ARG A 266      59.064  14.311  -4.873  1.00 25.59
ATOM   2132  CZ  ARG A 266      59.203  13.660  -3.718  1.00 26.28
ATOM   2133  NH1 ARG A 266      59.062  14.304  -2.564  1.00 26.53
ATOM   2134  NH2 ARG A 266      59.432  12.351  -3.713  1.00 24.44
ATOM   2135  N   LYS A 267      56.240  20.371  -6.356  1.00 23.50
ATOM   2136  CA  LYS A 267      56.325  21.820  -6.484  1.00 23.70
ATOM   2137  C   LYS A 267      55.823  22.542  -5.223  1.00 23.48
ATOM   2138  O   LYS A 267      56.323  23.618  -4.841  1.00 23.19
ATOM   2139  CB  LYS A 267      55.540  22.270  -7.710  1.00 26.55
ATOM   2140  CG  LYS A 267      56.284  21.938  -8.971  1.00 30.99
ATOM   2141  CD  LYS A 267      55.587  22.445 -10.188  1.00 32.36
ATOM   2142  CE  LYS A 267      56.458  22.136 -11.391  1.00 34.93
ATOM   2143  NZ  LYS A 267      55.755  22.438 -12.639  1.00 36.18
ATOM   2144  N   LEU A 268      54.823  21.945  -4.584  1.00 21.73
ATOM   2145  CA  LEU A 268      54.269  22.518  -3.368  1.00 20.70
ATOM   2146  C   LEU A 268      55.270  22.349  -2.233  1.00 20.20
ATOM   2147  O   LEU A 268      55.563  23.309  -1.518  1.00 21.59
ATOM   2148  CB  LEU A 268      52.929  21.879  -3.026  1.00 16.09
ATOM   2149  CG  LEU A 268      51.834  22.281  -4.007  1.00 16.11
ATOM   2150  CD1 LEU A 268      50.587  21.434  -3.796  1.00 11.44
ATOM   2151  CD2 LEU A 268      51.518  23.761  -3.883  1.00 13.56
ATOM   2152  N   GLN A 269      55.858  21.165  -2.132  1.00 20.99
ATOM   2153  CA  GLN A 269      56.861  20.894  -1.117  1.00 22.88
ATOM   2154  C   GLN A 269      58.024  21.886  -1.194  1.00 23.86
ATOM   2155  O   GLN A 269      58.525  22.340  -0.161  1.00 23.80
ATOM   2156  CB  GLN A 269      57.400  19.479  -1.268  1.00 23.81
ATOM   2157  CG  GLN A 269      56.446  18.408  -0.799  1.00 25.59
ATOM   2158  CD  GLN A 269      57.041  17.021  -0.881  1.00 27.52
ATOM   2159  OE1 GLN A 269      57.844  16.719  -1.775  1.00 28.89
ATOM   2160  NE2 GLN A 269      56.650  16.161   0.050  1.00 27.42
ATOM   2161  N   LYS A 270      58.453  22.219  -2.414  1.00 23.92
ATOM   2162  CA  LYS A 270      59.554  23.153  -2.621  1.00 23.70
ATOM   2163  C   LYS A 270      59.184  24.580  -2.282  1.00 21.69
ATOM   2164  O   LYS A 270      59.994  25.335  -1.755  1.00 21.44
ATOM   2165  CB  LYS A 270      60.065  23.070  -4.060  1.00 26.19
ATOM   2166  CG  LYS A 270      60.880  21.817  -4.301  1.00 29.93
ATOM   2167  CD  LYS A 270      61.340  21.648  -5.748  1.00 34.91
ATOM   2168  CE  LYS A 270      62.258  22.788  -6.217  1.00 37.03
ATOM   2169  NZ  LYS A 270      61.522  24.054  -6.592  1.00 38.59
ATOM   2170  N   GLN A 271      57.962  24.960  -2.596  1.00 20.62
ATOM   2171  CA  GLN A 271      57.528  26.303  -2.293  1.00 19.70
ATOM   2172  C   GLN A 271      57.342  26.398  -0.769  1.00 20.03
ATOM   2173  O   GLN A 271      57.695  27.401  -0.163  1.00 19.63
ATOM   2174  CB  GLN A 271      56.241  26.608  -3.056  1.00 19.31
ATOM   2175  CG  GLN A 271      55.844  28.090  -3.089  1.00 23.14
ATOM   2176  CD  GLN A 271      56.933  28.990  -3.648  1.00 21.87
ATOM   2177  OE1 GLN A 271      57.870  28.529  -4.281  1.00 22.48
ATOM   2178  NE2 GLN A 271      56.813  30.284  -3.398  1.00 24.67
ATOM   2179  N   PHE A 272      56.893  25.307  -0.152  1.00 20.34
ATOM   2180  CA  PHE A 272      56.669  25.258   1.298  1.00 23.13
ATOM   2181  C   PHE A 272      58.001  25.441   2.009  1.00 23.56
ATOM   2182  O   PHE A 272      58.119  26.225   2.939  1.00 23.72
ATOM   2183  CB  PHE A 272      56.073  23.902   1.699  1.00 23.13
ATOM   2184  CG  PHE A 272      55.732  23.784   3.169  1.00 23.94
ATOM   2185  CD1 PHE A 272      54.555  24.332   3.671  1.00 24.85
ATOM   2186  CD2 PHE A 272      56.582  23.124   4.045  1.00 24.25
ATOM   2187  CE1 PHE A 272      54.234  24.222   5.029  1.00 24.54
ATOM   2188  CE2 PHE A 272      56.270  23.012   5.402  1.00 23.45
ATOM   2189  CZ  PHE A 272      55.097  23.561   5.892  1.00 24.06
ATOM   2190  N   GLU A 273      59.001  24.708   1.527  1.00 25.99
ATOM   2191  CA  GLU A 273      60.366  24.717   2.052  1.00 26.46
ATOM   2192  C   GLU A 273      61.024  26.085   2.105  1.00 26.31
ATOM   2193  O   GLU A 273      61.960  26.285   2.875  1.00 27.26
ATOM   2194  CB  GLU A 273      61.244  23.802   1.204  1.00 27.83
ATOM   2195  CG  GLU A 273      62.629  23.526   1.788  1.00 30.49
ATOM   2196  CD  GLU A 273      62.638  22.351   2.743  1.00 31.68
ATOM   2197  OE1 GLU A 273      61.749  21.482   2.612  1.00 33.29
ATOM   2198  OE2 GLU A 273      63.546  22.283   3.608  1.00 32.81
ATOM   2199  N   THR A 274      60.586  26.996   1.246  1.00 26.61
ATOM   2200  CA  THR A 274      61.143  28.338   1.189  1.00 26.99
ATOM   2201  C   THR A 274      60.661  29.156   2.377  1.00 28.86
ATOM   2202  O   THR A 274      61.209  30.220   2.671  1.00 29.53
ATOM   2203  CB  THR A 274      60.727  29.077  -0.126  1.00 26.74
ATOM   2204  OG1 THR A 274      59.345  29.451  -0.062  1.00 26.49
ATOM   2205  CG2 THR A 274      60.952  28.180  -1.340  1.00 24.91
ATOM   2206  N   LYS A 275      59.621  28.660   3.045  1.00 30.09
ATOM   2207  CA  LYS A 275      59.028  29.338   4.191  1.00 31.11
ATOM   2208  C   LYS A 275      59.532  28.875   5.554  1.00 32.01
ATOM   2209  O   LYS A 275      59.431  29.617   6.531  1.00 31.78
ATOM   2210  CB  LYS A 275      57.507  29.206   4.133  1.00 30.53
ATOM   2211  CG  LYS A 275      56.915  29.833   2.903  1.00 29.23
ATOM   2212  CD  LYS A 275      55.441  29.624   2.825  1.00 29.17
ATOM   2213  CE  LYS A 275      54.923  30.131   1.491  1.00 29.00
ATOM   2214  NZ  LYS A 275      55.293  31.539   1.256  1.00 28.87
ATOM   2215  N   ILE A 276      60.055  27.659   5.633  1.00 33.21
ATOM   2216  CA  ILE A 276      60.526  27.168   6.912  1.00 36.00
ATOM   2217  C   ILE A 276      61.888  27.761   7.258  1.00 38.45
ATOM   2218  O   ILE A 276      62.741  27.961   6.386  1.00 39.10
ATOM   2219  CB  ILE A 276      60.548  25.623   7.004  1.00 35.41
ATOM   2220  CG1 ILE A 276      61.689  25.035   6.205  1.00 35.82
ATOM   2221  CG2 ILE A 276      59.267  25.038   6.459  1.00 35.50
ATOM   2222  CD1 ILE A 276      61.976  23.619   6.567  1.00 36.23
ATOM   2223  N   PRO A 277      62.084  28.103   8.538  1.00 39.66
ATOM   2224  CA  PRO A 277      63.327  28.686   9.030  1.00 40.72
ATOM   2225  C   PRO A 277      64.498  27.724   8.830  1.00 42.02
ATOM   2226  O   PRO A 277      64.398  26.533   9.127  1.00 41.34
ATOM   2227  CB  PRO A 277      63.044  28.873  10.518  1.00 41.01
ATOM   2228  CG  PRO A 277      61.553  28.977  10.586  1.00 40.74
ATOM   2229  CD  PRO A 277      61.128  27.917   9.638  1.00 39.79
