2gaa.cif

ATOM   896  C CA  . GLU A 1 119 ? 17.567 35.980 24.217  1.00 61.88 ? 119  GLU A CA  1 
ATOM   897  C C   . GLU A 1 119 ? 19.054 35.712 24.007  1.00 60.47 ? 119  GLU A C   1 
ATOM   898  O O   . GLU A 1 119 ? 19.566 35.849 22.897  1.00 59.89 ? 119  GLU A O   1 
ATOM   899  C CB  . GLU A 1 119 ? 16.778 34.666 24.193  1.00 63.98 ? 119  GLU A CB  1 
ATOM   900  C CG  . GLU A 1 119 ? 16.030 34.392 22.894  1.00 65.78 ? 119  GLU A CG  1 
ATOM   901  C CD  . GLU A 1 119 ? 16.933 34.426 21.677  1.00 67.92 ? 119  GLU A CD  1 
ATOM   902  O OE1 . GLU A 1 119 ? 17.946 33.693 21.662  1.00 70.21 ? 119  GLU A OE1 1 
ATOM   903  O OE2 . GLU A 1 119 ? 16.627 35.184 20.732  1.00 68.60 ? 119  GLU A OE2 1 
ATOM   904  N N   . GLU A 1 120 ? 19.742 35.325 25.077  1.00 59.33 ? 120  GLU A N   1 
ATOM   905  C CA  . GLU A 1 120 ? 21.178 35.072 25.010  1.00 58.67 ? 120  GLU A CA  1 
ATOM   906  C C   . GLU A 1 120 ? 21.569 33.858 24.174  1.00 56.73 ? 120  GLU A C   1 
ATOM   907  O O   . GLU A 1 120 ? 20.845 32.864 24.108  1.00 56.81 ? 120  GLU A O   1 
ATOM   908  C CB  . GLU A 1 120 ? 21.760 34.915 26.417  1.00 59.87 ? 120  GLU A CB  1 
ATOM   909  C CG  . GLU A 1 120 ? 21.475 33.570 27.067  1.00 62.50 ? 120  GLU A CG  1 
ATOM   910  C CD  . GLU A 1 120 ? 22.159 33.424 28.412  1.00 64.50 ? 120  GLU A CD  1 
ATOM   911  O OE1 . GLU A 1 120 ? 23.390 33.637 28.475  1.00 65.37 ? 120  GLU A OE1 1 
ATOM   912  O OE2 . GLU A 1 120 ? 21.470 33.093 29.403  1.00 65.57 ? 120  GLU A OE2 1 
HETATM 913  N N   . CME A 1 121 ? 22.681 33.432 23.934  1.00 53.95 ? 121  CME A N   1 
HETATM 914  C CA  . CME A 1 121 ? 23.138 32.366 23.055  1.00 50.85 ? 121  CME A CA  1 
HETATM 915  C CB  . CME A 1 121 ? 22.518 32.503 21.668  1.00 49.18 ? 121  CME A CB  1 
HETATM 916  S SG  . CME A 1 121 ? 23.094 31.225 20.506  1.00 45.22 ? 121  CME A SG  1 
HETATM 917  S SD  . CME A 1 121 ? 21.606 29.848 20.552  1.00 45.67 ? 121  CME A SD  1 
HETATM 918  C CE  . CME A 1 121 ? 20.406 30.456 19.325  1.00 46.46 ? 121  CME A CE  1 
HETATM 919  C CZ  . CME A 1 121 ? 20.908 30.297 17.904  1.00 48.56 ? 121  CME A CZ  1 
HETATM 920  O OH  . CME A 1 121 ? 20.186 30.881 17.031  1.00 49.17 ? 121  CME A OH  1 
HETATM 921  C C   . CME A 1 121 ? 24.653 32.431 22.930  1.00 50.21 ? 121  CME A C   1 
HETATM 922  O O   . CME A 1 121 ? 25.260 33.455 23.226  1.00 48.74 ? 121  CME A O   1 
ATOM   923  N N   . THR A 1 122 ? 24.983 30.976 23.355  1.00 25.24 ? 122  THR A N   1 
ATOM   924  C CA  . THR A 1 122 ? 26.408 30.759 23.623  1.00 25.22 ? 122  THR A CA  1 
ATOM   925  C C   . THR A 1 122 ? 27.044 30.122 22.400  1.00 25.36 ? 122  THR A C   1 
ATOM   926  O O   . THR A 1 122 ? 26.585 29.126 21.868  1.00 25.93 ? 122  THR A O   1 
ATOM   927  C CB  . THR A 1 122 ? 26.586 29.833 24.822  1.00 26.13 ? 122  THR A CB  1 
ATOM   928  O OG1 . THR A 1 122 ? 25.914 30.377 25.958  1.00 28.26 ? 122  THR A OG1 1 
ATOM   929  C CG2 . THR A 1 122 ? 28.061 29.644 25.175  1.00 25.41 ? 122  THR A CG2 1 
ATOM   930  N N   . ALA A 1 123 ? 28.080 30.673 21.929  1.00 24.88 ? 123  ALA A N   1 
ATOM   931  C CA  . ALA A 1 123 ? 28.729 30.131 20.746  1.00 24.45 ? 123  ALA A CA  1 
ATOM   932  C C   . ALA A 1 123 ? 30.019 29.431 21.142  1.00 23.77 ? 123  ALA A C   1 
ATOM   933  O O   . ALA A 1 123 ? 30.781 29.930 21.976  1.00 23.99 ? 123  ALA A O   1 
ATOM   934  C CB  . ALA A 1 123 ? 29.032 31.257 19.769  1.00 24.95 ? 123  ALA A CB  1 
ATOM   935  N N   . VAL A 1 124 ? 30.236 28.254 20.571  1.00 21.68 ? 124  VAL A N   1 
ATOM   936  C CA  . VAL A 1 124 ? 31.440 27.495 20.854  1.00 19.61 ? 124  VAL A CA  1 
ATOM   937  C C   . VAL A 1 124 ? 32.189 27.336 19.543  1.00 18.74 ? 124  VAL A C   1 
ATOM   938  O O   . VAL A 1 124 ? 31.662 26.774 18.584  1.00 17.73 ? 124  VAL A O   1 
ATOM   939  C CB  . VAL A 1 124 ? 31.109 26.108 21.430  1.00 19.97 ? 124  VAL A CB  1 
ATOM   940  C CG1 . VAL A 1 124 ? 32.395 25.326 21.672  1.00 20.60 ? 124  VAL A CG1 1 
ATOM   941  C CG2 . VAL A 1 124 ? 30.320 26.258 22.722  1.00 21.13 ? 124  VAL A CG2 1 
ATOM   942  N N   . VAL A 1 125 ? 33.418 27.839 19.505  1.00 17.99 ? 125  VAL A N   1 
ATOM   943  C CA  . VAL A 1 125 ? 34.227 27.763 18.300  1.00 18.43 ? 125  VAL A CA  1 
ATOM   944  C C   . VAL A 1 125 ? 35.603 27.175 18.566  1.00 19.12 ? 125  VAL A C   1 
ATOM   945  O O   . VAL A 1 125 ? 36.102 27.213 19.692  1.00 18.99 ? 125  VAL A O   1 
ATOM   946  C CB  . VAL A 1 125 ? 34.409 29.162 17.654  1.00 19.68 ? 125  VAL A CB  1 
ATOM   947  C CG1 . VAL A 1 125 ? 33.093 29.660 17.099  1.00 16.83 ? 125  VAL A CG1 1 
ATOM   948  C CG2 . VAL A 1 125 ? 34.932 30.147 18.685  1.00 18.42 ? 125  VAL A CG2 1 
ATOM   949  N N   . ALA A 1 126 ? 36.201 26.617 17.517  1.00 19.07 ? 126  ALA A N   1 
ATOM   950  C CA  . ALA A 1 126 ? 37.529 26.036 17.606  1.00 19.45 ? 126  ALA A CA  1 
ATOM   951  C C   . ALA A 1 126 ? 38.370 26.561 16.440  1.00 20.32 ? 126  ALA A C   1 
ATOM   952  O O   . ALA A 1 126 ? 38.141 27.674 15.968  1.00 20.32 ? 126  ALA A O   1 
ATOM   953  C CB  . ALA A 1 126 ? 37.448 24.519 17.591  1.00 19.13 ? 126  ALA A CB  1 
ATOM   954  N N   . ARG A 1 127 ? 39.321 25.770 15.955  1.00 19.72 ? 127  ARG A N   1 
ATOM   955  C CA  . ARG A 1 127 ? 40.199 26.245 14.890  1.00 20.55 ? 127  ARG A CA  1 
ATOM   956  C C   . ARG A 1 127 ? 39.552 26.748 13.595  1.00 19.36 ? 127  ARG A C   1 
ATOM   957  O O   . ARG A 1 127 ? 40.183 27.480 12.841  1.00 23.51 ? 127  ARG A O   1 
ATOM   958  C CB  . ARG A 1 127 ? 41.276 25.195 14.584  1.00 18.75 ? 127  ARG A CB  1 
ATOM   959  C CG  . ARG A 1 127 ? 40.903 24.038 13.664  1.00 15.59 ? 127  ARG A CG  1 
ATOM   960  C CD  . ARG A 1 127 ? 42.126 23.119 13.563  1.00 17.15 ? 127  ARG A CD  1 
ATOM   961  N NE  . ARG A 1 127 ? 42.295 22.455 12.270  1.00 16.85 ? 127  ARG A NE  1 
ATOM   962  C CZ  . ARG A 1 127 ? 41.918 21.210 12.006  1.00 16.12 ? 127  ARG A CZ  1 
ATOM   963  N NH1 . ARG A 1 127 ? 41.335 20.473 12.943  1.00 17.75 ? 127  ARG A NH1 1 
ATOM   964  N NH2 . ARG A 1 127 ? 42.145 20.694 10.808  1.00 16.11 ? 127  ARG A NH2 1 
ATOM   965  N N   . GLY A 1 128 ? 38.302 26.379 13.346  1.00 19.80 ? 128  GLY A N   1 
ATOM   966  C CA  . GLY A 1 128 ? 37.625 26.832 12.142  1.00 18.10 ? 128  GLY A CA  1 
ATOM   967  C C   . GLY A 1 128 ? 36.935 28.180 12.300  1.00 20.02 ? 128  GLY A C   1 
ATOM   968  O O   . GLY A 1 128 ? 36.433 28.755 11.331  1.00 19.46 ? 128  GLY A O   1 
ATOM   969  N N   . GLY A 1 129 ? 36.903 28.693 13.524  1.00 19.53 ? 129  GLY A N   1 
ATOM   970  C CA  . GLY A 1 129 ? 36.270 29.977 13.756  1.00 19.31 ? 129  GLY A CA  1 
ATOM   971  C C   . GLY A 1 129 ? 34.753 29.928 13.709  1.00 18.25 ? 129  GLY A C   1 
ATOM   972  O O   . GLY A 1 129 ? 34.147 28.856 13.797  1.00 17.58 ? 129  GLY A O   1 
ATOM   973  N N   . THR A 1 130 ? 34.137 31.095 13.544  1.00 19.08 ? 130  THR A N   1 
ATOM   974  C CA  . THR A 1 130 ? 32.681 31.202 13.523  1.00 20.39 ? 130  THR A CA  1 
ATOM   975  C C   . THR A 1 130 ? 31.962 30.329 12.507  1.00 19.67 ? 130  THR A C   1 
ATOM   976  O O   . THR A 1 130 ? 30.827 29.930 12.735  1.00 20.62 ? 130  THR A O   1 
ATOM   977  C CB  . THR A 1 130 ? 32.228 32.658 13.294  1.00 19.47 ? 130  THR A CB  1 
ATOM   978  O OG1 . THR A 1 130 ? 32.785 33.145 12.066  1.00 21.34 ? 130  THR A OG1 1 
ATOM   979  C CG2 . THR A 1 130 ? 32.678 33.539 14.444  1.00 20.90 ? 130  THR A CG2 1 
ATOM   980  N N   . ALA A 1 131 ? 32.611 30.030 11.390  1.00 19.13 ? 131  ALA A N   1 
ATOM   981  C CA  . ALA A 1 131 ? 31.968 29.222 10.354  1.00 18.58 ? 131  ALA A CA  1 
ATOM   982  C C   . ALA A 1 131 ? 31.545 27.821 10.811  1.00 18.42 ? 131  ALA A C   1 
ATOM   983  O O   . ALA A 1 131 ? 30.598 27.254 10.270  1.00 17.41 ? 131  ALA A O   1 
ATOM   984  C CB  . ALA A 1 131 ? 32.886 29.123 9.132   1.00 19.73 ? 131  ALA A CB  1 
ATOM   985  N N   . ASN A 1 132 ? 32.238 27.258 11.799  1.00 17.79 ? 132  ASN A N   1 
ATOM   986  C CA  . ASN A 1 132 ? 31.900 25.922 12.289  1.00 17.13 ? 132  ASN A CA  1 
ATOM   987  C C   . ASN A 1 132 ? 31.388 25.969 13.726  1.00 18.59 ? 132  ASN A C   1 
ATOM   988  O O   . ASN A 1 132 ? 31.398 24.966 14.439  1.00 17.70 ? 132  ASN A O   1 
ATOM   989  C CB  . ASN A 1 132 ? 33.129 25.013 12.218  1.00 17.92 ? 132  ASN A CB  1 
ATOM   990  C CG  . ASN A 1 132 ? 33.737 24.964 10.834  1.00 17.42 ? 132  ASN A CG  1 
ATOM   991  O OD1 . ASN A 1 132 ? 34.919 25.257 10.655  1.00 18.58 ? 132  ASN A OD1 1 
ATOM   992  N ND2 . ASN A 1 132 ? 32.933 24.590 9.845   1.00 15.67 ? 132  ASN A ND2 1 
ATOM   993  N N   . ALA A 1 133 ? 30.925 27.139 14.141  1.00 18.58 ? 133  ALA A N   1 
ATOM   994  C CA  . ALA A 1 133 ? 30.440 27.322 15.498  1.00 18.88 ? 133  ALA A CA  1 
ATOM   995  C C   . ALA A 1 133 ? 29.239 26.457 15.864  1.00 17.68 ? 133  ALA A C   1 
ATOM   996  O O   . ALA A 1 133 ? 28.389 26.149 15.032  1.00 19.22 ? 133  ALA A O   1 
ATOM   997  C CB  . ALA A 1 133 ? 30.106 28.805 15.730  1.00 18.10 ? 133  ALA A CB  1 
ATOM   998  N N   . ILE A 1 134 ? 29.200 26.058 17.128  1.00 19.15 ? 134  ILE A N   1 
ATOM   999  C CA  . ILE A 1 134 ? 28.101 25.279 17.686  1.00 19.18 ? 134  ILE A CA  1 
ATOM   1000 C C   . ILE A 1 134 ? 27.415 26.330 18.540  1.00 19.81 ? 134  ILE A C   1 
ATOM   1001 O O   . ILE A 1 134 ? 28.096 27.098 19.214  1.00 18.94 ? 134  ILE A O   1 
ATOM   1002 C CB  . ILE A 1 134 ? 28.617 24.157 18.609  1.00 17.51 ? 134  ILE A CB  1 
ATOM   1003 C CG1 . ILE A 1 134 ? 29.398 23.124 17.788  1.00 17.61 ? 134  ILE A CG1 1 
ATOM   1004 C CG2 . ILE A 1 134 ? 27.447 23.509 19.351  1.00 19.49 ? 134  ILE A CG2 1 
ATOM   1005 C CD1 . ILE A 1 134 ? 30.148 22.114 18.641  1.00 12.41 ? 134  ILE A CD1 1 
ATOM   1006 N N   . ARG A 1 135 ? 26.086 26.387 18.512  1.00 21.73 ? 135  ARG A N   1 
ATOM   1007 C CA  . ARG A 1 135 ? 25.378 27.387 19.305  1.00 21.76 ? 135  ARG A CA  1 
ATOM   1008 C C   . ARG A 1 135 ? 24.417 26.776 20.308  1.00 21.65 ? 135  ARG A C   1 
ATOM   1009 O O   . ARG A 1 135 ? 23.626 25.903 19.970  1.00 20.79 ? 135  ARG A O   1 
ATOM   1010 C CB  . ARG A 1 135 ? 24.639 28.371 18.384  1.00 24.84 ? 135  ARG A CB  1 
ATOM   1011 C CG  . ARG A 1 135 ? 25.594 29.258 17.593  1.00 28.56 ? 135  ARG A CG  1 
ATOM   1012 C CD  . ARG A 1 135 ? 24.896 30.443 16.945  1.00 35.00 ? 135  ARG A CD  1 
ATOM   1013 N NE  . ARG A 1 135 ? 25.874 31.376 16.386  1.00 38.87 ? 135  ARG A NE  1 
ATOM   1014 C CZ  . ARG A 1 135 ? 26.670 31.097 15.358  1.00 40.50 ? 135  ARG A CZ  1 
ATOM   1015 N NH1 . ARG A 1 135 ? 26.600 29.912 14.764  1.00 41.91 ? 135  ARG A NH1 1 
ATOM   1016 N NH2 . ARG A 1 135 ? 27.555 31.993 14.938  1.00 40.31 ? 135  ARG A NH2 1 
ATOM   1017 N N   . ILE A 1 136 ? 24.499 27.245 21.548  1.00 21.59 ? 136  ILE A N   1 
ATOM   1018 C CA  . ILE A 1 136 ? 23.651 26.740 22.619  1.00 24.43 ? 136  ILE A CA  1 
ATOM   1019 C C   . ILE A 1 136 ? 22.742 27.845 23.159  1.00 27.29 ? 136  ILE A C   1 
ATOM   1020 O O   . ILE A 1 136 ? 23.202 28.936 23.483  1.00 25.11 ? 136  ILE A O   1 
ATOM   1021 C CB  . ILE A 1 136 ? 24.517 26.170 23.760  1.00 24.71 ? 136  ILE A CB  1 
ATOM   1022 C CG1 . ILE A 1 136 ? 25.550 25.200 23.176  1.00 23.08 ? 136  ILE A CG1 1 
ATOM   1023 C CG2 . ILE A 1 136 ? 23.636 25.455 24.781  1.00 26.24 ? 136  ILE A CG2 1 
ATOM   1024 C CD1 . ILE A 1 136 ? 26.556 24.681 24.178  1.00 24.74 ? 136  ILE A CD1 1 
ATOM   1025 N N   . ALA A 1 137 ? 21.448 27.553 23.249  1.00 30.12 ? 137  ALA A N   1 
ATOM   1026 C CA  . ALA A 1 137 ? 20.470 28.522 23.732  1.00 34.76 ? 137  ALA A CA  1 
ATOM   1027 C C   . ALA A 1 137 ? 20.306 28.513 25.252  1.00 38.65 ? 137  ALA A C   1 
ATOM   1028 O O   . ALA A 1 137 ? 20.808 27.626 25.941  1.00 40.53 ? 137  ALA A O   1 
ATOM   1029 C CB  . ALA A 1 137 ? 19.128 28.270 23.059  1.00 34.19 ? 137  ALA A CB  1 
ATOM   1030 N N   . ALA A 1 138 ? 19.598 29.514 25.768  1.00 42.99 ? 138  ALA A N   1 
ATOM   1031 C CA  . ALA A 1 138 ? 19.356 29.638 27.204  1.00 44.62 ? 138  ALA A CA  1 
ATOM   1032 C C   . ALA A 1 138 ? 18.719 28.374 27.773  1.00 45.98 ? 138  ALA A C   1 
ATOM   1033 O O   . ALA A 1 138 ? 17.501 28.303 27.946  1.00 46.09 ? 138  ALA A O   1 
ATOM   1034 C CB  . ALA A 1 138 ? 18.458 30.839 27.476  1.00 44.84 ? 138  ALA A CB  1 
ATOM   1035 N N   . SER A 1 152 ? 5.387  17.451 14.429  1.00 44.08 ? 152  SER A N   1 
ATOM   1036 C CA  . SER A 1 152 ? 6.024  18.604 15.061  1.00 43.77 ? 152  SER A CA  1 
ATOM   1037 C C   . SER A 1 152 ? 7.084  18.179 16.074  1.00 41.25 ? 152  SER A C   1 
ATOM   1038 O O   . SER A 1 152 ? 8.180  18.742 16.111  1.00 42.29 ? 152  SER A O   1 
ATOM   1039 C CB  . SER A 1 152 ? 4.978  19.475 15.757  1.00 44.61 ? 152  SER A CB  1 
ATOM   1040 O OG  . SER A 1 152 ? 5.603  20.547 16.443  1.00 48.48 ? 152  SER A OG  1 
ATOM   1041 N N   . ILE A 1 153 ? 6.752  17.197 16.907  1.00 37.74 ? 153  ILE A N   1 
ATOM   1042 C CA  . ILE A 1 153 ? 7.702  16.710 17.898  1.00 33.92 ? 153  ILE A CA  1 
ATOM   1043 C C   . ILE A 1 153 ? 8.481  15.550 17.302  1.00 29.76 ? 153  ILE A C   1 
ATOM   1044 O O   . ILE A 1 153 ? 7.922  14.487 17.042  1.00 29.22 ? 153  ILE A O   1 
ATOM   1045 C CB  . ILE A 1 153 ? 6.999  16.214 19.183  1.00 34.71 ? 153  ILE A CB  1 
ATOM   1046 C CG1 . ILE A 1 153 ? 6.265  17.373 19.864  1.00 35.80 ? 153  ILE A CG1 1 
ATOM   1047 C CG2 . ILE A 1 153 ? 8.027  15.617 20.143  1.00 34.54 ? 153  ILE A CG2 1 
ATOM   1048 C CD1 . ILE A 1 153 ? 7.176  18.479 20.372  1.00 34.61 ? 153  ILE A CD1 1 
ATOM   1049 N N   . ASN A 1 154 ? 9.769  15.762 17.071  1.00 25.95 ? 154  ASN A N   1 
ATOM   1050 C CA  . ASN A 1 154 ? 10.616 14.720 16.512  1.00 24.16 ? 154  ASN A CA  1 
ATOM   1051 C C   . ASN A 1 154 ? 11.634 14.277 17.548  1.00 21.47 ? 154  ASN A C   1 
ATOM   1052 O O   . ASN A 1 154 ? 12.224 15.109 18.238  1.00 19.28 ? 154  ASN A O   1 
ATOM   1053 C CB  . ASN A 1 154 ? 11.326 15.229 15.259  1.00 26.60 ? 154  ASN A CB  1 
ATOM   1054 C CG  . ASN A 1 154 ? 10.356 15.591 14.159  1.00 27.62 ? 154  ASN A CG  1 
ATOM   1055 O OD1 . ASN A 1 154 ? 9.521  14.781 13.769  1.00 28.71 ? 154  ASN A OD1 1 
ATOM   1056 N ND2 . ASN A 1 154 ? 10.457 16.810 13.656  1.00 32.27 ? 154  ASN A ND2 1 
ATOM   1057 N N   . ILE A 1 155 ? 11.833 12.967 17.654  1.00 17.89 ? 155  ILE A N   1 
ATOM   1058 C CA  . ILE A 1 155 ? 12.770 12.426 18.623  1.00 16.79 ? 155  ILE A CA  1 
ATOM   1059 C C   . ILE A 1 155 ? 14.117 12.036 18.010  1.00 16.33 ? 155  ILE A C   1 
ATOM   1060 O O   . ILE A 1 155 ? 15.065 11.727 18.731  1.00 15.72 ? 155  ILE A O   1 
ATOM   1061 C CB  . ILE A 1 155 ? 12.170 11.200 19.339  1.00 15.97 ? 155  ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 155 ? 11.754 10.149 18.302  1.00 15.90 ? 155  ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 155 ? 10.974 11.633 20.208  1.00 15.32 ? 155  ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 155 ? 11.307 8.829  18.899  1.00 16.79 ? 155  ILE A CD1 1 
ATOM   1065 N N   . ALA A 1 156 ? 14.192 12.046 16.684  1.00 16.56 ? 156  ALA A N   1 
ATOM   1066 C CA  . ALA A 1 156 ? 15.425 11.697 15.988  1.00 15.35 ? 156  ALA A CA  1 
ATOM   1067 C C   . ALA A 1 156 ? 15.877 12.855 15.128  1.00 15.81 ? 156  ALA A C   1 
ATOM   1068 O O   . ALA A 1 156 ? 15.069 13.508 14.466  1.00 17.00 ? 156  ALA A O   1 
ATOM   1069 C CB  . ALA A 1 156 ? 15.219 10.453 15.122  1.00 14.71 ? 156  ALA A CB  1 
ATOM   1070 N N   . GLN A 1 157 ? 17.178 13.109 15.144  1.00 15.28 ? 157  GLN A N   1 
ATOM   1071 C CA  . GLN A 1 157 ? 17.763 14.188 14.365  1.00 16.47 ? 157  GLN A CA  1 
ATOM   1072 C C   . GLN A 1 157 ? 19.105 13.698 13.823  1.00 17.18 ? 157  GLN A C   1 
ATOM   1073 O O   . GLN A 1 157 ? 19.739 12.819 14.414  1.00 14.87 ? 157  GLN A O   1 
ATOM   1074 C CB  . GLN A 1 157 ? 17.966 15.416 15.261  1.00 16.11 ? 157  GLN A CB  1 
ATOM   1075 C CG  . GLN A 1 157 ? 18.640 16.607 14.606  1.00 18.31 ? 157  GLN A CG  1 
ATOM   1076 C CD  . GLN A 1 157 ? 17.867 17.146 13.412  1.00 21.45 ? 157  GLN A CD  1 
ATOM   1077 O OE1 . GLN A 1 157 ? 17.791 16.504 12.359  1.00 22.30 ? 157  GLN A OE1 1 
ATOM   1078 N NE2 . GLN A 1 157 ? 17.286 18.332 13.573  1.00 20.89 ? 157  GLN A NE2 1 
ATOM   1079 N N   . ILE A 1 158 ? 19.524 14.247 12.690  1.00 16.80 ? 158  ILE A N   1 
ATOM   1080 C CA  . ILE A 1 158 ? 20.803 13.860 12.102  1.00 20.04 ? 158  ILE A CA  1 
ATOM   1081 C C   . ILE A 1 158 ? 21.829 14.962 12.291  1.00 20.55 ? 158  ILE A C   1 
ATOM   1082 O O   . ILE A 1 158 ? 21.491 16.145 12.298  1.00 20.83 ? 158  ILE A O   1 
ATOM   1083 C CB  . ILE A 1 158 ? 20.700 13.602 10.579  1.00 20.82 ? 158  ILE A CB  1 
ATOM   1084 C CG1 . ILE A 1 158 ? 20.261 14.883 9.864   1.00 24.24 ? 158  ILE A CG1 1 
ATOM   1085 C CG2 . ILE A 1 158 ? 19.724 12.472 10.299  1.00 19.47 ? 158  ILE A CG2 1 
ATOM   1086 C CD1 . ILE A 1 158 ? 20.329 14.792 8.339   1.00 26.06 ? 158  ILE A CD1 1 
ATOM   1087 N N   . VAL A 1 159 ? 23.086 14.568 12.456  1.00 20.97 ? 159  VAL A N   1 
ATOM   1088 C CA  . VAL A 1 159 ? 24.170 15.528 12.594  1.00 20.47 ? 159  VAL A CA  1 
ATOM   1089 C C   . VAL A 1 159 ? 25.195 15.219 11.507  1.00 19.92 ? 159  VAL A C   1 
ATOM   1090 O O   . VAL A 1 159 ? 25.974 14.285 11.634  1.00 18.51 ? 159  VAL A O   1 
ATOM   1091 C CB  . VAL A 1 159 ? 24.869 15.433 13.968  1.00 22.06 ? 159  VAL A CB  1 
ATOM   1092 C CG1 . VAL A 1 159 ? 26.123 16.305 13.970  1.00 22.66 ? 159  VAL A CG1 1 
ATOM   1093 C CG2 . VAL A 1 159 ? 23.925 15.872 15.069  1.00 21.64 ? 159  VAL A CG2 1 
ATOM   1094 N N   . PRO A 1 160 ? 25.175 15.977 10.403  1.00 19.65 ? 160  PRO A N   1 
ATOM   1095 C CA  . PRO A 1 160 ? 26.136 15.740 9.320   1.00 20.72 ? 160  PRO A CA  1 
ATOM   1096 C C   . PRO A 1 160 ? 27.497 16.310 9.706   1.00 21.58 ? 160  PRO A C   1 
ATOM   1097 O O   . PRO A 1 160 ? 27.585 17.358 10.345  1.00 21.72 ? 160  PRO A O   1 
ATOM   1098 C CB  . PRO A 1 160 ? 25.530 16.500 8.135   1.00 22.38 ? 160  PRO A CB  1 
ATOM   1099 C CG  . PRO A 1 160 ? 24.068 16.618 8.486   1.00 22.20 ? 160  PRO A CG  1 
ATOM   1100 C CD  . PRO A 1 160 ? 24.120 16.901 9.963   1.00 22.06 ? 160  PRO A CD  1 
ATOM   1101 N N   . MET A 1 161 ? 28.558 15.618 9.320   1.00 21.61 ? 161  MET A N   1 
ATOM   1102 C CA  . MET A 1 161 ? 29.905 16.083 9.615   1.00 22.41 ? 161  MET A CA  1 
ATOM   1103 C C   . MET A 1 161 ? 30.247 17.222 8.639   1.00 22.46 ? 161  MET A C   1 
ATOM   1104 O O   . MET A 1 161 ? 31.104 18.065 8.916   1.00 19.53 ? 161  MET A O   1 
ATOM   1105 C CB  . MET A 1 161 ? 30.881 14.920 9.445   1.00 21.01 ? 161  MET A CB  1 
ATOM   1106 C CG  . MET A 1 161 ? 32.219 15.104 10.106  1.00 24.62 ? 161  MET A CG  1 
ATOM   1107 S SD  . MET A 1 161 ? 33.309 13.734 9.696   1.00 22.52 ? 161  MET A SD  1 
ATOM   1108 C CE  . MET A 1 161 ? 33.971 14.321 8.175   1.00 21.03 ? 161  MET A CE  1 
ATOM   1109 N N   . ASP A 1 162 ? 29.554 17.244 7.502   1.00 22.90 ? 162  ASP A N   1 
ATOM   1110 C CA  . ASP A 1 162 ? 29.767 18.253 6.458   1.00 24.93 ? 162  ASP A CA  1 
ATOM   1111 C C   . ASP A 1 162 ? 29.806 19.692 6.964   1.00 22.86 ? 162  ASP A C   1 
ATOM   1112 O O   . ASP A 1 162 ? 30.544 20.521 6.433   1.00 20.69 ? 162  ASP A O   1 
ATOM   1113 C CB  . ASP A 1 162 ? 28.665 18.165 5.397   1.00 29.29 ? 162  ASP A CB  1 
ATOM   1114 C CG  . ASP A 1 162 ? 28.732 16.896 4.584   1.00 33.72 ? 162  ASP A CG  1 
ATOM   1115 O OD1 . ASP A 1 162 ? 29.707 16.721 3.825   1.00 36.08 ? 162  ASP A OD1 1 
ATOM   1116 O OD2 . ASP A 1 162 ? 27.803 16.070 4.703   1.00 36.92 ? 162  ASP A OD2 1 
ATOM   1117 N N   . GLY A 1 163 ? 28.993 19.989 7.974   1.00 20.28 ? 163  GLY A N   1 
ATOM   1118 C CA  . GLY A 1 163 ? 28.938 21.336 8.504   1.00 17.65 ? 163  GLY A CA  1 
ATOM   1119 C C   . GLY A 1 163 ? 30.235 21.794 9.130   1.00 18.50 ? 163  GLY A C   1 
ATOM   1120 O O   . GLY A 1 163 ? 30.431 22.988 9.374   1.00 16.61 ? 163  GLY A O   1 
ATOM   1121 N N   . PHE A 1 164 ? 31.134 20.853 9.392   1.00 16.79 ? 164  PHE A N   1 
ATOM   1122 C CA  . PHE A 1 164 ? 32.400 21.208 10.005  1.00 17.47 ? 164  PHE A CA  1 
ATOM   1123 C C   . PHE A 1 164 ? 33.562 21.350 9.024   1.00 17.66 ? 164  PHE A C   1 
ATOM   1124 O O   . PHE A 1 164 ? 34.719 21.384 9.433   1.00 18.44 ? 164  PHE A O   1 
ATOM   1125 C CB  . PHE A 1 164 ? 32.720 20.221 11.127  1.00 15.15 ? 164  PHE A CB  1 
ATOM   1126 C CG  . PHE A 1 164 ? 31.788 20.349 12.307  1.00 15.72 ? 164  PHE A CG  1 
ATOM   1127 C CD1 . PHE A 1 164 ? 32.186 21.024 13.458  1.00 14.88 ? 164  PHE A CD1 1 
ATOM   1128 C CD2 . PHE A 1 164 ? 30.481 19.866 12.230  1.00 14.40 ? 164  PHE A CD2 1 
ATOM   1129 C CE1 . PHE A 1 164 ? 31.293 21.224 14.521  1.00 14.25 ? 164  PHE A CE1 1 
ATOM   1130 C CE2 . PHE A 1 164 ? 29.580 20.060 13.290  1.00 14.94 ? 164  PHE A CE2 1 
ATOM   1131 C CZ  . PHE A 1 164 ? 29.992 20.741 14.432  1.00 13.33 ? 164  PHE A CZ  1 
ATOM   1132 N N   . HIS A 1 165 ? 33.249 21.432 7.730   1.00 18.65 ? 165  HIS A N   1 
ATOM   1133 C CA  . HIS A 1 165 ? 34.282 21.655 6.714   1.00 16.99 ? 165  HIS A CA  1 
ATOM   1134 C C   . HIS A 1 165 ? 34.876 23.000 7.085   1.00 17.96 ? 165  HIS A C   1 
ATOM   1135 O O   . HIS A 1 165 ? 34.133 23.925 7.401   1.00 17.81 ? 165  HIS A O   1 
ATOM   1136 C CB  . HIS A 1 165 ? 33.688 21.856 5.312   1.00 18.37 ? 165  HIS A CB  1 
ATOM   1137 C CG  . HIS A 1 165 ? 33.593 20.614 4.486   1.00 20.22 ? 165  HIS A CG  1 
ATOM   1138 N ND1 . HIS A 1 165 ? 32.478 19.803 4.486   1.00 21.21 ? 165  HIS A ND1 1 
ATOM   1139 C CD2 . HIS A 1 165 ? 34.453 20.071 3.592   1.00 21.27 ? 165  HIS A CD2 1 
ATOM   1140 C CE1 . HIS A 1 165 ? 32.654 18.816 3.625   1.00 21.13 ? 165  HIS A CE1 1 
ATOM   1141 N NE2 . HIS A 1 165 ? 33.844 18.955 3.070   1.00 21.25 ? 165  HIS A NE2 1 
ATOM   1142 N N   . LEU A 1 166 ? 36.194 23.133 7.050   1.00 17.82 ? 166  LEU A N   1 
ATOM   1143 C CA  . LEU A 1 166 ? 36.773 24.436 7.326   1.00 18.85 ? 166  LEU A CA  1 
ATOM   1144 C C   . LEU A 1 166 ? 36.333 25.284 6.126   1.00 19.24 ? 166  LEU A C   1 
ATOM   1145 O O   . LEU A 1 166 ? 36.206 24.771 5.013   1.00 20.20 ? 166  LEU A O   1 
ATOM   1146 C CB  . LEU A 1 166 ? 38.301 24.347 7.397   1.00 18.55 ? 166  LEU A CB  1 
ATOM   1147 C CG  . LEU A 1 166 ? 38.846 23.510 8.560   1.00 17.39 ? 166  LEU A CG  1 
ATOM   1148 C CD1 . LEU A 1 166 ? 40.359 23.378 8.453   1.00 13.24 ? 166  LEU A CD1 1 
ATOM   1149 C CD2 . LEU A 1 166 ? 38.452 24.156 9.873   1.00 17.63 ? 166  LEU A CD2 1 
ATOM   1150 N N   . SER A 1 167 ? 36.073 26.566 6.345   1.00 19.70 ? 167  SER A N   1 
ATOM   1151 C CA  . SER A 1 167 ? 35.641 27.422 5.250   1.00 20.38 ? 167  SER A CA  1 
ATOM   1152 C C   . SER A 1 167 ? 36.771 27.569 4.238   1.00 21.04 ? 167  SER A C   1 
ATOM   1153 O O   . SER A 1 167 ? 37.935 27.318 4.555   1.00 21.86 ? 167  SER A O   1 
ATOM   1154 C CB  . SER A 1 167 ? 35.228 28.800 5.778   1.00 18.97 ? 167  SER A CB  1 
ATOM   1155 O OG  . SER A 1 167 ? 36.346 29.521 6.258   1.00 19.99 ? 167  SER A OG  1 
ATOM   1156 N N   . ARG A 1 168 ? 36.428 27.964 3.018   1.00 21.81 ? 168  ARG A N   1 
ATOM   1157 C CA  . ARG A 1 168 ? 37.436 28.145 1.981   1.00 23.42 ? 168  ARG A CA  1 
ATOM   1158 C C   . ARG A 1 168 ? 38.392 29.258 2.390   1.00 23.49 ? 168  ARG A C   1 
ATOM   1159 O O   . ARG A 1 168 ? 39.579 29.215 2.074   1.00 24.06 ? 168  ARG A O   1 
ATOM   1160 C CB  . ARG A 1 168 ? 36.773 28.485 0.647   1.00 24.79 ? 168  ARG A CB  1 
ATOM   1161 C CG  . ARG A 1 168 ? 35.924 27.365 0.059   1.00 29.52 ? 168  ARG A CG  1 
ATOM   1162 C CD  . ARG A 1 168 ? 35.218 27.848 -1.202  1.00 33.66 ? 168  ARG A CD  1 
ATOM   1163 N NE  . ARG A 1 168 ? 34.394 29.018 -0.920  1.00 37.23 ? 168  ARG A NE  1 
ATOM   1164 C CZ  . ARG A 1 168 ? 33.940 29.858 -1.844  1.00 40.85 ? 168  ARG A CZ  1 
ATOM   1165 N NH1 . ARG A 1 168 ? 33.196 30.896 -1.487  1.00 42.81 ? 168  ARG A NH1 1 
ATOM   1166 N NH2 . ARG A 1 168 ? 34.234 29.666 -3.124  1.00 43.69 ? 168  ARG A NH2 1 
ATOM   1167 N N   . ARG A 1 169 ? 37.876 30.265 3.086   1.00 24.58 ? 169  ARG A N   1 
ATOM   1168 C CA  . ARG A 1 169 ? 38.732 31.356 3.533   1.00 26.53 ? 169  ARG A CA  1 
ATOM   1169 C C   . ARG A 1 169 ? 39.684 30.815 4.596   1.00 25.65 ? 169  ARG A C   1 
ATOM   1170 O O   . ARG A 1 169 ? 40.828 31.246 4.701   1.00 25.97 ? 169  ARG A O   1 
ATOM   1171 C CB  . ARG A 1 169 ? 37.899 32.507 4.101   1.00 29.26 ? 169  ARG A CB  1 
ATOM   1172 C CG  . ARG A 1 169 ? 38.742 33.578 4.776   1.00 36.70 ? 169  ARG A CG  1 
ATOM   1173 C CD  . ARG A 1 169 ? 37.977 34.875 5.031   1.00 42.10 ? 169  ARG A CD  1 
ATOM   1174 N NE  . ARG A 1 169 ? 37.758 35.648 3.810   1.00 47.01 ? 169  ARG A NE  1 
ATOM   1175 C CZ  . ARG A 1 169 ? 36.790 35.410 2.930   1.00 49.45 ? 169  ARG A CZ  1 
ATOM   1176 N NH1 . ARG A 1 169 ? 35.933 34.417 3.129   1.00 50.28 ? 169  ARG A NH1 1 
ATOM   1177 N NH2 . ARG A 1 169 ? 36.680 36.166 1.844   1.00 51.15 ? 169  ARG A NH2 1 
ATOM   1178 N N   . CYS A 1 170 ? 39.206 29.858 5.381   1.00 24.73 ? 170  CYS A N   1 
ATOM   1179 C CA  . CYS A 1 170 ? 40.030 29.251 6.414   1.00 25.18 ? 170  CYS A CA  1 
ATOM   1180 C C   . CYS A 1 170 ? 41.148 28.461 5.727   1.00 24.94 ? 170  CYS A C   1 
ATOM   1181 O O   . CYS A 1 170 ? 42.290 28.450 6.181   1.00 24.16 ? 170  CYS A O   1 
ATOM   1182 C CB  . CYS A 1 170 ? 39.172 28.323 7.279   1.00 26.84 ? 170  CYS A CB  1 
ATOM   1183 S SG  . CYS A 1 170 ? 39.959 27.752 8.786   1.00 30.55 ? 170  CYS A SG  1 
ATOM   1184 N N   . LEU A 1 171 ? 40.815 27.807 4.620   1.00 24.27 ? 171  LEU A N   1 
ATOM   1185 C CA  . LEU A 1 171 ? 41.803 27.028 3.888   1.00 24.69 ? 171  LEU A CA  1 
ATOM   1186 C C   . LEU A 1 171 ? 42.879 27.925 3.264   1.00 25.58 ? 171  LEU A C   1 
ATOM   1187 O O   . LEU A 1 171 ? 44.009 27.489 3.061   1.00 26.72 ? 171  LEU A O   1 
ATOM   1188 C CB  . LEU A 1 171 ? 41.118 26.178 2.806   1.00 21.45 ? 171  LEU A CB  1 
ATOM   1189 C CG  . LEU A 1 171 ? 40.168 25.063 3.278   1.00 21.57 ? 171  LEU A CG  1 
ATOM   1190 C CD1 . LEU A 1 171 ? 39.633 24.300 2.072   1.00 22.36 ? 171  LEU A CD1 1 
ATOM   1191 C CD2 . LEU A 1 171 ? 40.898 24.100 4.212   1.00 21.61 ? 171  LEU A CD2 1 
ATOM   1192 N N   . ASP A 1 172 ? 42.533 29.177 2.972   1.00 26.93 ? 172  ASP A N   1 
ATOM   1193 C CA  . ASP A 1 172 ? 43.491 30.110 2.380   1.00 29.31 ? 172  ASP A CA  1 
ATOM   1194 C C   . ASP A 1 172 ? 44.609 30.443 3.356   1.00 29.43 ? 172  ASP A C   1 
ATOM   1195 O O   . ASP A 1 172 ? 45.693 30.869 2.956   1.00 31.18 ? 172  ASP A O   1 
ATOM   1196 C CB  . ASP A 1 172 ? 42.814 31.424 1.965   1.00 29.64 ? 172  ASP A CB  1 
ATOM   1197 C CG  . ASP A 1 172 ? 41.895 31.266 0.766   1.00 32.06 ? 172  ASP A CG  1 
ATOM   1198 O OD1 . ASP A 1 172 ? 42.211 30.464 -0.135  1.00 34.07 ? 172  ASP A OD1 1 
ATOM   1199 O OD2 . ASP A 1 172 ? 40.860 31.965 0.715   1.00 34.67 ? 172  ASP A OD2 1 
ATOM   1200 N N   . LEU A 1 173 ? 44.340 30.254 4.641   1.00 28.49 ? 173  LEU A N   1 
ATOM   1201 C CA  . LEU A 1 173 ? 45.323 30.552 5.669   1.00 28.44 ? 173  LEU A CA  1 
ATOM   1202 C C   . LEU A 1 173 ? 46.237 29.377 5.974   1.00 28.34 ? 173  LEU A C   1 
ATOM   1203 O O   . LEU A 1 173 ? 47.124 29.487 6.815   1.00 27.90 ? 173  LEU A O   1 
ATOM   1204 C CB  . LEU A 1 173 ? 44.620 31.011 6.949   1.00 28.11 ? 173  LEU A CB  1 
ATOM   1205 C CG  . LEU A 1 173 ? 43.718 32.236 6.771   1.00 29.71 ? 173  LEU A CG  1 
ATOM   1206 C CD1 . LEU A 1 173 ? 42.974 32.521 8.072   1.00 30.41 ? 173  LEU A CD1 1 
ATOM   1207 C CD2 . LEU A 1 173 ? 44.553 33.436 6.346   1.00 28.12 ? 173  LEU A CD2 1 
ATOM   1208 N N   . PHE A 1 174 ? 46.016 28.250 5.306   1.00 28.35 ? 174  PHE A N   1 
ATOM   1209 C CA  . PHE A 1 174 ? 46.866 27.082 5.515   1.00 31.00 ? 174  PHE A CA  1 
ATOM   1210 C C   . PHE A 1 174 ? 48.256 27.426 4.998   1.00 33.70 ? 174  PHE A C   1 
ATOM   1211 O O   . PHE A 1 174 ? 48.393 28.213 4.060   1.00 32.58 ? 174  PHE A O   1 
ATOM   1212 C CB  . PHE A 1 174 ? 46.314 25.870 4.758   1.00 29.61 ? 174  PHE A CB  1 
ATOM   1213 C CG  . PHE A 1 174 ? 45.334 25.048 5.554   1.00 30.66 ? 174  PHE A CG  1 
ATOM   1214 C CD1 . PHE A 1 174 ? 44.268 25.651 6.212   1.00 31.41 ? 174  PHE A CD1 1 
ATOM   1215 C CD2 . PHE A 1 174 ? 45.471 23.667 5.631   1.00 30.28 ? 174  PHE A CD2 1 
ATOM   1216 C CE1 . PHE A 1 174 ? 43.347 24.886 6.938   1.00 32.10 ? 174  PHE A CE1 1 
ATOM   1217 C CE2 . PHE A 1 174 ? 44.559 22.895 6.351   1.00 31.44 ? 174  PHE A CE2 1 
ATOM   1218 C CZ  . PHE A 1 174 ? 43.495 23.506 7.006   1.00 30.21 ? 174  PHE A CZ  1 
ATOM   1219 N N   . LYS A 1 175 ? 49.285 26.845 5.606   1.00 36.19 ? 175  LYS A N   1 
ATOM   1220 C CA  . LYS A 1 175 ? 50.653 27.121 5.180   1.00 39.66 ? 175  LYS A CA  1 
ATOM   1221 C C   . LYS A 1 175 ? 50.780 26.844 3.685   1.00 40.22 ? 175  LYS A C   1 
ATOM   1222 O O   . LYS A 1 175 ? 51.528 27.515 2.978   1.00 41.77 ? 175  LYS A O   1 
ATOM   1223 C CB  . LYS A 1 175 ? 51.644 26.264 5.971   1.00 42.68 ? 175  LYS A CB  1 
ATOM   1224 C CG  . LYS A 1 175 ? 53.057 26.836 5.995   1.00 48.11 ? 175  LYS A CG  1 
ATOM   1225 C CD  . LYS A 1 175 ? 53.067 28.243 6.601   1.00 51.21 ? 175  LYS A CD  1 
ATOM   1226 C CE  . LYS A 1 175 ? 54.436 28.908 6.476   1.00 53.33 ? 175  LYS A CE  1 
ATOM   1227 N NZ  . LYS A 1 175 ? 54.434 30.307 7.000   1.00 53.83 ? 175  LYS A NZ  1 
ATOM   1228 N N   . ASP A 1 176 ? 50.035 25.854 3.209   1.00 39.80 ? 176  ASP A N   1 
ATOM   1229 C CA  . ASP A 1 176 ? 50.035 25.504 1.794   1.00 40.02 ? 176  ASP A CA  1 
ATOM   1230 C C   . ASP A 1 176 ? 48.587 25.431 1.312   1.00 38.95 ? 176  ASP A C   1 
ATOM   1231 O O   . ASP A 1 176 ? 48.005 24.350 1.212   1.00 37.36 ? 176  ASP A O   1 
ATOM   1232 C CB  . ASP A 1 176 ? 50.735 24.164 1.569   1.00 40.57 ? 176  ASP A CB  1 
ATOM   1233 C CG  . ASP A 1 176 ? 50.658 23.712 0.130   1.00 42.58 ? 176  ASP A CG  1 
ATOM   1234 O OD1 . ASP A 1 176 ? 50.724 24.583 -0.762  1.00 42.61 ? 176  ASP A OD1 1 
ATOM   1235 O OD2 . ASP A 1 176 ? 50.541 22.493 -0.112  1.00 43.52 ? 176  ASP A OD2 1 
ATOM   1236 N N   . PRO A 1 177 ? 47.990 26.594 1.006   1.00 38.94 ? 177  PRO A N   1 
ATOM   1237 C CA  . PRO A 1 177 ? 46.605 26.706 0.536   1.00 39.28 ? 177  PRO A CA  1 
ATOM   1238 C C   . PRO A 1 177 ? 46.278 25.845 -0.678  1.00 39.58 ? 177  PRO A C   1 
ATOM   1239 O O   . PRO A 1 177 ? 45.212 25.230 -0.737  1.00 38.02 ? 177  PRO A O   1 
ATOM   1240 C CB  . PRO A 1 177 ? 46.464 28.194 0.228   1.00 37.91 ? 177  PRO A CB  1 
ATOM   1241 C CG  . PRO A 1 177 ? 47.430 28.830 1.164   1.00 39.82 ? 177  PRO A CG  1 
ATOM   1242 C CD  . PRO A 1 177 ? 48.625 27.921 1.056   1.00 38.16 ? 177  PRO A CD  1 
ATOM   1243 N N   . GLN A 1 178 ? 47.200 25.810 -1.639  1.00 40.10 ? 178  GLN A N   1 
ATOM   1244 C CA  . GLN A 1 178 ? 47.012 25.050 -2.873  1.00 41.67 ? 178  GLN A CA  1 
ATOM   1245 C C   . GLN A 1 178 ? 46.590 23.610 -2.610  1.00 40.51 ? 178  GLN A C   1 
ATOM   1246 O O   . GLN A 1 178 ? 45.574 23.148 -3.128  1.00 40.66 ? 178  GLN A O   1 
ATOM   1247 C CB  . GLN A 1 178 ? 48.298 25.071 -3.718  1.00 44.90 ? 178  GLN A CB  1 
ATOM   1248 C CG  . GLN A 1 178 ? 49.430 24.193 -3.187  1.00 49.23 ? 178  GLN A CG  1 
ATOM   1249 C CD  . GLN A 1 178 ? 50.694 24.260 -4.034  1.00 52.47 ? 178  GLN A CD  1 
ATOM   1250 O OE1 . GLN A 1 178 ? 50.651 24.105 -5.258  1.00 54.58 ? 178  GLN A OE1 1 
ATOM   1251 N NE2 . GLN A 1 178 ? 51.831 24.478 -3.380  1.00 53.34 ? 178  GLN A NE2 1 
ATOM   1252 N N   . THR A 1 179 ? 47.373 22.903 -1.804  1.00 39.74 ? 179  THR A N   1 
ATOM   1253 C CA  . THR A 1 179 ? 47.073 21.518 -1.480  1.00 39.11 ? 179  THR A CA  1 
ATOM   1254 C C   . THR A 1 179 ? 45.839 21.456 -0.583  1.00 37.29 ? 179  THR A C   1 
ATOM   1255 O O   . THR A 1 179 ? 45.041 20.524 -0.675  1.00 37.08 ? 179  THR A O   1 
ATOM   1256 C CB  . THR A 1 179 ? 48.277 20.850 -0.773  1.00 40.55 ? 179  THR A CB  1 
ATOM   1257 O OG1 . THR A 1 179 ? 49.400 20.838 -1.664  1.00 43.22 ? 179  THR A OG1 1 
ATOM   1258 C CG2 . THR A 1 179 ? 47.950 19.420 -0.370  1.00 41.03 ? 179  THR A CG2 1 
ATOM   1259 N N   . ALA A 1 180 ? 45.681 22.459 0.275   1.00 34.96 ? 180  ALA A N   1 
ATOM   1260 C CA  . ALA A 1 180 ? 44.536 22.504 1.177   1.00 34.53 ? 180  ALA A CA  1 
ATOM   1261 C C   . ALA A 1 180 ? 43.239 22.450 0.375   1.00 33.74 ? 180  ALA A C   1 
ATOM   1262 O O   . ALA A 1 180 ? 42.346 21.657 0.673   1.00 34.47 ? 180  ALA A O   1 
ATOM   1263 C CB  . ALA A 1 180 ? 44.583 23.775 2.026   1.00 31.88 ? 180  ALA A CB  1 
ATOM   1264 N N   . HIS A 1 181 ? 43.144 23.291 -0.651  1.00 33.57 ? 181  HIS A N   1 
ATOM   1265 C CA  . HIS A 1 181 ? 41.953 23.329 -1.492  1.00 32.70 ? 181  HIS A CA  1 
ATOM   1266 C C   . HIS A 1 181 ? 41.820 22.099 -2.381  1.00 32.85 ? 181  HIS A C   1 
ATOM   1267 O O   . HIS A 1 181 ? 40.757 21.487 -2.456  1.00 32.84 ? 181  HIS A O   1 
ATOM   1268 C CB  . HIS A 1 181 ? 41.955 24.582 -2.370  1.00 30.57 ? 181  HIS A CB  1 
ATOM   1269 C CG  . HIS A 1 181 ? 41.613 25.837 -1.632  1.00 29.75 ? 181  HIS A CG  1 
ATOM   1270 N ND1 . HIS A 1 181 ? 42.569 26.670 -1.093  1.00 30.51 ? 181  HIS A ND1 1 
ATOM   1271 C CD2 . HIS A 1 181 ? 40.416 26.394 -1.332  1.00 30.06 ? 181  HIS A CD2 1 
ATOM   1272 C CE1 . HIS A 1 181 ? 41.976 27.689 -0.496  1.00 28.59 ? 181  HIS A CE1 1 
ATOM   1273 N NE2 . HIS A 1 181 ? 40.670 27.545 -0.626  1.00 30.87 ? 181  HIS A NE2 1 
ATOM   1274 N N   . LYS A 1 182 ? 42.903 21.742 -3.059  1.00 33.91 ? 182  LYS A N   1 
ATOM   1275 C CA  . LYS A 1 182 ? 42.893 20.591 -3.949  1.00 35.19 ? 182  LYS A CA  1 
ATOM   1276 C C   . LYS A 1 182 ? 42.517 19.324 -3.185  1.00 34.78 ? 182  LYS A C   1 
ATOM   1277 O O   . LYS A 1 182 ? 41.895 18.416 -3.735  1.00 34.82 ? 182  LYS A O   1 
ATOM   1278 C CB  . LYS A 1 182 ? 44.271 20.437 -4.601  1.00 36.29 ? 182  LYS A CB  1 
ATOM   1279 C CG  . LYS A 1 182 ? 44.335 19.445 -5.754  1.00 41.12 ? 182  LYS A CG  1 
ATOM   1280 C CD  . LYS A 1 182 ? 44.447 18.007 -5.274  1.00 43.72 ? 182  LYS A CD  1 
ATOM   1281 C CE  . LYS A 1 182 ? 44.519 17.039 -6.449  1.00 45.97 ? 182  LYS A CE  1 
ATOM   1282 N NZ  . LYS A 1 182 ? 45.683 17.316 -7.341  1.00 47.41 ? 182  LYS A NZ  1 
ATOM   1283 N N   . ARG A 1 183 ? 42.881 19.276 -1.909  1.00 34.06 ? 183  ARG A N   1 
ATOM   1284 C CA  . ARG A 1 183 ? 42.591 18.112 -1.084  1.00 34.08 ? 183  ARG A CA  1 
ATOM   1285 C C   . ARG A 1 183 ? 41.423 18.350 -0.130  1.00 31.07 ? 183  ARG A C   1 
ATOM   1286 O O   . ARG A 1 183 ? 41.284 17.644 0.866   1.00 30.06 ? 183  ARG A O   1 
ATOM   1287 C CB  . ARG A 1 183 ? 43.836 17.735 -0.285  1.00 37.19 ? 183  ARG A CB  1 
ATOM   1288 C CG  . ARG A 1 183 ? 43.863 16.302 0.196   1.00 44.99 ? 183  ARG A CG  1 
ATOM   1289 C CD  . ARG A 1 183 ? 45.195 15.992 0.858   1.00 49.02 ? 183  ARG A CD  1 
ATOM   1290 N NE  . ARG A 1 183 ? 45.353 14.571 1.145   1.00 52.53 ? 183  ARG A NE  1 
ATOM   1291 C CZ  . ARG A 1 183 ? 46.421 14.048 1.736   1.00 54.74 ? 183  ARG A CZ  1 
ATOM   1292 N NH1 . ARG A 1 183 ? 47.426 14.834 2.106   1.00 55.14 ? 183  ARG A NH1 1 
ATOM   1293 N NH2 . ARG A 1 183 ? 46.488 12.740 1.952   1.00 55.91 ? 183  ARG A NH2 1 
ATOM   1294 N N   . ARG A 1 184 ? 40.585 19.338 -0.432  1.00 27.74 ? 184  ARG A N   1 
ATOM   1295 C CA  . ARG A 1 184 ? 39.449 19.634 0.433   1.00 26.61 ? 184  ARG A CA  1 
ATOM   1296 C C   . ARG A 1 184 ? 38.582 18.392 0.589   1.00 26.14 ? 184  ARG A C   1 
ATOM   1297 O O   . ARG A 1 184 ? 38.160 17.785 -0.394  1.00 25.40 ? 184  ARG A O   1 
ATOM   1298 C CB  . ARG A 1 184 ? 38.606 20.787 -0.126  1.00 26.57 ? 184  ARG A CB  1 
ATOM   1299 C CG  . ARG A 1 184 ? 37.560 21.286 0.874   1.00 25.00 ? 184  ARG A CG  1 
ATOM   1300 C CD  . ARG A 1 184 ? 36.740 22.460 0.357   1.00 25.97 ? 184  ARG A CD  1 
ATOM   1301 N NE  . ARG A 1 184 ? 36.155 23.206 1.472   1.00 25.59 ? 184  ARG A NE  1 
ATOM   1302 C CZ  . ARG A 1 184 ? 35.196 24.120 1.352   1.00 27.34 ? 184  ARG A CZ  1 
ATOM   1303 N NH1 . ARG A 1 184 ? 34.696 24.415 0.156   1.00 23.01 ? 184  ARG A NH1 1 
ATOM   1304 N NH2 . ARG A 1 184 ? 34.734 24.734 2.433   1.00 23.06 ? 184  ARG A NH2 1 
ATOM   1305 N N   . GLY A 1 185 ? 38.315 18.022 1.833   1.00 24.68 ? 185  GLY A N   1 
ATOM   1306 C CA  . GLY A 1 185 ? 37.519 16.842 2.093   1.00 22.54 ? 185  GLY A CA  1 
ATOM   1307 C C   . GLY A 1 185 ? 38.371 15.845 2.857   1.00 23.27 ? 185  GLY A C   1 
ATOM   1308 O O   . GLY A 1 185 ? 37.871 14.845 3.368   1.00 21.76 ? 185  GLY A O   1 
ATOM   1309 N N   . SER A 1 186 ? 39.671 16.117 2.925   1.00 21.58 ? 186  SER A N   1 
ATOM   1310 C CA  . SER A 1 186 ? 40.586 15.247 3.656   1.00 20.98 ? 186  SER A CA  1 
ATOM   1311 C C   . SER A 1 186 ? 40.320 15.504 5.138   1.00 19.69 ? 186  SER A C   1 
ATOM   1312 O O   . SER A 1 186 ? 39.743 16.533 5.493   1.00 17.18 ? 186  SER A O   1 
ATOM   1313 C CB  . SER A 1 186 ? 42.039 15.596 3.327   1.00 22.61 ? 186  SER A CB  1 
ATOM   1314 O OG  . SER A 1 186 ? 42.407 16.838 3.904   1.00 27.30 ? 186  SER A OG  1 
ATOM   1315 N N   . PRO A 1 187 ? 40.750 14.582 6.018   1.00 17.80 ? 187  PRO A N   1 
ATOM   1316 C CA  . PRO A 1 187 ? 40.551 14.713 7.464   1.00 17.84 ? 187  PRO A CA  1 
ATOM   1317 C C   . PRO A 1 187 ? 41.078 16.028 8.035   1.00 18.51 ? 187  PRO A C   1 
ATOM   1318 O O   . PRO A 1 187 ? 40.549 16.546 9.019   1.00 18.56 ? 187  PRO A O   1 
ATOM   1319 C CB  . PRO A 1 187 ? 41.321 13.517 8.032   1.00 17.44 ? 187  PRO A CB  1 
ATOM   1320 C CG  . PRO A 1 187 ? 41.306 12.534 6.928   1.00 20.26 ? 187  PRO A CG  1 
ATOM   1321 C CD  . PRO A 1 187 ? 41.536 13.374 5.711   1.00 17.95 ? 187  PRO A CD  1 
ATOM   1322 N N   . SER A 1 188 ? 42.129 16.562 7.424   1.00 16.85 ? 188  SER A N   1 
ATOM   1323 C CA  . SER A 1 188 ? 42.723 17.800 7.911   1.00 17.68 ? 188  SER A CA  1 
ATOM   1324 C C   . SER A 1 188 ? 42.015 19.070 7.442   1.00 17.03 ? 188  SER A C   1 
ATOM   1325 O O   . SER A 1 188 ? 42.437 20.174 7.790   1.00 17.97 ? 188  SER A O   1 
ATOM   1326 C CB  . SER A 1 188 ? 44.206 17.859 7.521   1.00 19.66 ? 188  SER A CB  1 
ATOM   1327 O OG  . SER A 1 188 ? 44.354 17.989 6.118   1.00 23.45 ? 188  SER A OG  1 
ATOM   1328 N N   . THR A 1 189 ? 40.945 18.933 6.661   1.00 16.39 ? 189  THR A N   1 
ATOM   1329 C CA  . THR A 1 189 ? 40.231 20.117 6.196   1.00 14.69 ? 189  THR A CA  1 
ATOM   1330 C C   . THR A 1 189 ? 38.873 20.293 6.874   1.00 15.86 ? 189  THR A C   1 
ATOM   1331 O O   . THR A 1 189 ? 37.970 20.935 6.334   1.00 14.18 ? 189  THR A O   1 
ATOM   1332 C CB  . THR A 1 189 ? 40.051 20.120 4.650   1.00 17.13 ? 189  THR A CB  1 
ATOM   1333 O OG1 . THR A 1 189 ? 39.383 18.927 4.230   1.00 18.08 ? 189  THR A OG1 1 
ATOM   1334 C CG2 . THR A 1 189 ? 41.414 20.210 3.961   1.00 17.81 ? 189  THR A CG2 1 
ATOM   1335 N N   . PHE A 1 190 ? 38.749 19.726 8.070   1.00 13.96 ? 190  PHE A N   1 
ATOM   1336 C CA  . PHE A 1 190 ? 37.535 19.825 8.874   1.00 17.29 ? 190  PHE A CA  1 
ATOM   1337 C C   . PHE A 1 190 ? 37.954 20.343 10.249  1.00 17.66 ? 190  PHE A C   1 
ATOM   1338 O O   . PHE A 1 190 ? 39.099 20.151 10.666  1.00 16.48 ? 190  PHE A O   1 
ATOM   1339 C CB  . PHE A 1 190 ? 36.884 18.450 9.052   1.00 16.50 ? 190  PHE A CB  1 
ATOM   1340 C CG  . PHE A 1 190 ? 36.161 17.939 7.829   1.00 20.89 ? 190  PHE A CG  1 
ATOM   1341 C CD1 . PHE A 1 190 ? 34.793 18.157 7.668   1.00 19.20 ? 190  PHE A CD1 1 
ATOM   1342 C CD2 . PHE A 1 190 ? 36.844 17.227 6.848   1.00 20.06 ? 190  PHE A CD2 1 
ATOM   1343 C CE1 . PHE A 1 190 ? 34.118 17.669 6.550   1.00 22.36 ? 190  PHE A CE1 1 
ATOM   1344 C CE2 . PHE A 1 190 ? 36.177 16.736 5.725   1.00 20.79 ? 190  PHE A CE2 1 
ATOM   1345 C CZ  . PHE A 1 190 ? 34.812 16.956 5.575   1.00 20.78 ? 190  PHE A CZ  1 
ATOM   1346 N N   . ASP A 1 191 ? 37.036 21.000 10.949  1.00 15.78 ? 191  ASP A N   1 
ATOM   1347 C CA  . ASP A 1 191 ? 37.335 21.484 12.288  1.00 17.13 ? 191  ASP A CA  1 
ATOM   1348 C C   . ASP A 1 191 ? 37.081 20.288 13.207  1.00 17.33 ? 191  ASP A C   1 
ATOM   1349 O O   . ASP A 1 191 ? 36.042 20.199 13.879  1.00 16.00 ? 191  ASP A O   1 
ATOM   1350 C CB  . ASP A 1 191 ? 36.410 22.644 12.675  1.00 16.91 ? 191  ASP A CB  1 
ATOM   1351 C CG  . ASP A 1 191 ? 36.838 23.326 13.967  1.00 16.84 ? 191  ASP A CG  1 
ATOM   1352 O OD1 . ASP A 1 191 ? 37.560 22.695 14.770  1.00 16.51 ? 191  ASP A OD1 1 
ATOM   1353 O OD2 . ASP A 1 191 ? 36.446 24.487 14.183  1.00 14.73 ? 191  ASP A OD2 1 
ATOM   1354 N N   . SER A 1 192 ? 38.029 19.358 13.212  1.00 16.37 ? 192  SER A N   1 
ATOM   1355 C CA  . SER A 1 192 ? 37.916 18.160 14.028  1.00 15.95 ? 192  SER A CA  1 
ATOM   1356 C C   . SER A 1 192 ? 37.801 18.524 15.503  1.00 16.29 ? 192  SER A C   1 
ATOM   1357 O O   . SER A 1 192 ? 37.148 17.808 16.271  1.00 15.20 ? 192  SER A O   1 
ATOM   1358 C CB  . SER A 1 192 ? 39.135 17.254 13.800  1.00 15.27 ? 192  SER A CB  1 
ATOM   1359 O OG  . SER A 1 192 ? 40.323 17.894 14.230  1.00 14.97 ? 192  SER A OG  1 
ATOM   1360 N N   . ASN A 1 193 ? 38.430 19.637 15.886  1.00 12.85 ? 193  ASN A N   1 
ATOM   1361 C CA  . ASN A 1 193 ? 38.423 20.123 17.272  1.00 14.99 ? 193  ASN A CA  1 
ATOM   1362 C C   . ASN A 1 193 ? 36.993 20.353 17.755  1.00 15.38 ? 193  ASN A C   1 
ATOM   1363 O O   . ASN A 1 193 ? 36.581 19.861 18.808  1.00 14.72 ? 193  ASN A O   1 
ATOM   1364 C CB  . ASN A 1 193 ? 39.159 21.474 17.397  1.00 14.31 ? 193  ASN A CB  1 
ATOM   1365 C CG  . ASN A 1 193 ? 40.537 21.481 16.741  1.00 19.66 ? 193  ASN A CG  1 
ATOM   1366 O OD1 . ASN A 1 193 ? 40.747 20.882 15.683  1.00 17.84 ? 193  ASN A OD1 1 
ATOM   1367 N ND2 . ASN A 1 193 ? 41.478 22.197 17.361  1.00 18.12 ? 193  ASN A ND2 1 
ATOM   1368 N N   . ASN A 1 194 ? 36.243 21.137 16.988  1.00 15.61 ? 194  ASN A N   1 
ATOM   1369 C CA  . ASN A 1 194 ? 34.874 21.449 17.363  1.00 15.04 ? 194  ASN A CA  1 
ATOM   1370 C C   . ASN A 1 194 ? 33.912 20.283 17.182  1.00 15.64 ? 194  ASN A C   1 
ATOM   1371 O O   . ASN A 1 194 ? 32.923 20.187 17.908  1.00 15.13 ? 194  ASN A O   1 
ATOM   1372 C CB  . ASN A 1 194 ? 34.366 22.674 16.592  1.00 16.26 ? 194  ASN A CB  1 
ATOM   1373 C CG  . ASN A 1 194 ? 33.647 23.666 17.496  1.00 15.75 ? 194  ASN A CG  1 
ATOM   1374 O OD1 . ASN A 1 194 ? 32.772 24.412 17.055  1.00 16.91 ? 194  ASN A OD1 1 
ATOM   1375 N ND2 . ASN A 1 194 ? 34.026 23.684 18.765  1.00 11.34 ? 194  ASN A ND2 1 
ATOM   1376 N N   . PHE A 1 195 ? 34.169 19.397 16.222  1.00 13.92 ? 195  PHE A N   1 
ATOM   1377 C CA  . PHE A 1 195 ? 33.263 18.265 16.079  1.00 14.22 ? 195  PHE A CA  1 
ATOM   1378 C C   . PHE A 1 195 ? 33.418 17.399 17.338  1.00 14.29 ? 195  PHE A C   1 
ATOM   1379 O O   . PHE A 1 195 ? 32.431 16.934 17.915  1.00 11.70 ? 195  PHE A O   1 
ATOM   1380 C CB  . PHE A 1 195 ? 33.568 17.421 14.839  1.00 14.20 ? 195  PHE A CB  1 
ATOM   1381 C CG  . PHE A 1 195 ? 32.466 16.446 14.509  1.00 16.51 ? 195  PHE A CG  1 
ATOM   1382 C CD1 . PHE A 1 195 ? 31.332 16.868 13.821  1.00 14.41 ? 195  PHE A CD1 1 
ATOM   1383 C CD2 . PHE A 1 195 ? 32.520 15.130 14.964  1.00 16.57 ? 195  PHE A CD2 1 
ATOM   1384 C CE1 . PHE A 1 195 ? 30.273 15.991 13.597  1.00 14.39 ? 195  PHE A CE1 1 
ATOM   1385 C CE2 . PHE A 1 195 ? 31.465 14.257 14.744  1.00 11.85 ? 195  PHE A CE2 1 
ATOM   1386 C CZ  . PHE A 1 195 ? 30.344 14.690 14.061  1.00 15.02 ? 195  PHE A CZ  1 
ATOM   1387 N N   . LEU A 1 196 ? 34.659 17.177 17.760  1.00 14.04 ? 196  LEU A N   1 
ATOM   1388 C CA  . LEU A 1 196 ? 34.898 16.408 18.978  1.00 15.34 ? 196  LEU A CA  1 
ATOM   1389 C C   . LEU A 1 196 ? 34.168 17.094 20.132  1.00 15.64 ? 196  LEU A C   1 
ATOM   1390 O O   . LEU A 1 196 ? 33.538 16.436 20.958  1.00 16.99 ? 196  LEU A O   1 
ATOM   1391 C CB  . LEU A 1 196 ? 36.400 16.336 19.282  1.00 16.92 ? 196  LEU A CB  1 
ATOM   1392 C CG  . LEU A 1 196 ? 36.806 15.765 20.648  1.00 17.69 ? 196  LEU A CG  1 
ATOM   1393 C CD1 . LEU A 1 196 ? 36.226 14.370 20.830  1.00 16.94 ? 196  LEU A CD1 1 
ATOM   1394 C CD2 . LEU A 1 196 ? 38.330 15.730 20.752  1.00 18.16 ? 196  LEU A CD2 1 
ATOM   1395 N N   . GLN A 1 197 ? 34.243 18.422 20.177  1.00 16.57 ? 197  GLN A N   1 
ATOM   1396 C CA  . GLN A 1 197 ? 33.584 19.191 21.228  1.00 16.73 ? 197  GLN A CA  1 
ATOM   1397 C C   . GLN A 1 197 ? 32.078 18.974 21.157  1.00 16.53 ? 197  GLN A C   1 
ATOM   1398 O O   . GLN A 1 197 ? 31.418 18.893 22.184  1.00 18.15 ? 197  GLN A O   1 
ATOM   1399 C CB  . GLN A 1 197 ? 33.909 20.680 21.093  1.00 16.87 ? 197  GLN A CB  1 
ATOM   1400 C CG  . GLN A 1 197 ? 33.365 21.554 22.226  1.00 18.89 ? 197  GLN A CG  1 
ATOM   1401 C CD  . GLN A 1 197 ? 33.817 21.081 23.599  1.00 21.20 ? 197  GLN A CD  1 
ATOM   1402 O OE1 . GLN A 1 197 ? 34.990 20.774 23.807  1.00 20.27 ? 197  GLN A OE1 1 
ATOM   1403 N NE2 . GLN A 1 197 ? 32.886 21.026 24.545  1.00 21.40 ? 197  GLN A NE2 1 
ATOM   1404 N N   . LEU A 1 198 ? 31.527 18.891 19.949  1.00 17.23 ? 198  LEU A N   1 
ATOM   1405 C CA  . LEU A 1 198 ? 30.095 18.635 19.819  1.00 16.26 ? 198  LEU A CA  1 
ATOM   1406 C C   . LEU A 1 198 ? 29.802 17.274 20.446  1.00 14.22 ? 198  LEU A C   1 
ATOM   1407 O O   . LEU A 1 198 ? 28.814 17.114 21.159  1.00 14.38 ? 198  LEU A O   1 
ATOM   1408 C CB  . LEU A 1 198 ? 29.659 18.624 18.350  1.00 14.79 ? 198  LEU A CB  1 
ATOM   1409 C CG  . LEU A 1 198 ? 28.219 18.161 18.060  1.00 13.90 ? 198  LEU A CG  1 
ATOM   1410 C CD1 . LEU A 1 198 ? 27.217 18.979 18.854  1.00 13.94 ? 198  LEU A CD1 1 
ATOM   1411 C CD2 . LEU A 1 198 ? 27.939 18.278 16.556  1.00 13.30 ? 198  LEU A CD2 1 
ATOM   1412 N N   . CYS A 1 199 ? 30.665 16.296 20.185  1.00 11.73 ? 199  CYS A N   1 
ATOM   1413 C CA  . CYS A 1 199 ? 30.467 14.957 20.744  1.00 15.25 ? 199  CYS A CA  1 
ATOM   1414 C C   . CYS A 1 199 ? 30.533 14.982 22.267  1.00 14.62 ? 199  CYS A C   1 
ATOM   1415 O O   . CYS A 1 199 ? 29.758 14.299 22.934  1.00 15.27 ? 199  CYS A O   1 
ATOM   1416 C CB  . CYS A 1 199 ? 31.493 13.977 20.181  1.00 13.66 ? 199  CYS A CB  1 
ATOM   1417 S SG  . CYS A 1 199 ? 31.240 13.642 18.424  1.00 15.41 ? 199  CYS A SG  1 
ATOM   1418 N N   . LYS A 1 200 ? 31.432 15.790 22.818  1.00 14.97 ? 200  LYS A N   1 
ATOM   1419 C CA  . LYS A 1 200 ? 31.540 15.898 24.275  1.00 16.34 ? 200  LYS A CA  1 
ATOM   1420 C C   . LYS A 1 200 ? 30.261 16.491 24.870  1.00 17.13 ? 200  LYS A C   1 
ATOM   1421 O O   . LYS A 1 200 ? 29.830 16.108 25.959  1.00 17.60 ? 200  LYS A O   1 
ATOM   1422 C CB  . LYS A 1 200 ? 32.733 16.774 24.662  1.00 16.63 ? 200  LYS A CB  1 
ATOM   1423 C CG  . LYS A 1 200 ? 34.084 16.113 24.459  1.00 17.87 ? 200  LYS A CG  1 
ATOM   1424 C CD  . LYS A 1 200 ? 35.205 17.025 24.938  1.00 20.47 ? 200  LYS A CD  1 
ATOM   1425 C CE  . LYS A 1 200 ? 36.564 16.364 24.776  1.00 22.54 ? 200  LYS A CE  1 
ATOM   1426 N NZ  . LYS A 1 200 ? 37.660 17.264 25.226  1.00 25.14 ? 200  LYS A NZ  1 
ATOM   1427 N N   . ILE A 1 201 ? 29.670 17.442 24.153  1.00 16.37 ? 201  ILE A N   1 
ATOM   1428 C CA  . ILE A 1 201 ? 28.445 18.082 24.588  1.00 14.57 ? 201  ILE A CA  1 
ATOM   1429 C C   . ILE A 1 201 ? 27.308 17.063 24.533  1.00 15.15 ? 201  ILE A C   1 
ATOM   1430 O O   . ILE A 1 201 ? 26.496 16.971 25.455  1.00 14.12 ? 201  ILE A O   1 
ATOM   1431 C CB  . ILE A 1 201 ? 28.130 19.309 23.696  1.00 15.86 ? 201  ILE A CB  1 
ATOM   1432 C CG1 . ILE A 1 201 ? 29.054 20.472 24.086  1.00 16.04 ? 201  ILE A CG1 1 
ATOM   1433 C CG2 . ILE A 1 201 ? 26.670 19.710 23.831  1.00 17.16 ? 201  ILE A CG2 1 
ATOM   1434 C CD1 . ILE A 1 201 ? 28.993 21.646 23.144  1.00 20.39 ? 201  ILE A CD1 1 
ATOM   1435 N N   . LEU A 1 202 ? 27.255 16.288 23.454  1.00 13.54 ? 202  LEU A N   1 
ATOM   1436 C CA  . LEU A 1 202 ? 26.223 15.266 23.323  1.00 14.65 ? 202  LEU A CA  1 
ATOM   1437 C C   . LEU A 1 202 ? 26.334 14.212 24.421  1.00 15.38 ? 202  LEU A C   1 
ATOM   1438 O O   . LEU A 1 202 ? 25.326 13.794 24.994  1.00 15.86 ? 202  LEU A O   1 
ATOM   1439 C CB  . LEU A 1 202 ? 26.314 14.590 21.953  1.00 14.41 ? 202  LEU A CB  1 
ATOM   1440 C CG  . LEU A 1 202 ? 25.963 15.484 20.761  1.00 14.47 ? 202  LEU A CG  1 
ATOM   1441 C CD1 . LEU A 1 202 ? 26.198 14.724 19.466  1.00 16.84 ? 202  LEU A CD1 1 
ATOM   1442 C CD2 . LEU A 1 202 ? 24.515 15.934 20.870  1.00 14.94 ? 202  LEU A CD2 1 
ATOM   1443 N N   . ALA A 1 203 ? 27.554 13.780 24.719  1.00 15.98 ? 203  ALA A N   1 
ATOM   1444 C CA  . ALA A 1 203 ? 27.757 12.762 25.751  1.00 15.43 ? 203  ALA A CA  1 
ATOM   1445 C C   . ALA A 1 203 ? 27.293 13.273 27.107  1.00 17.27 ? 203  ALA A C   1 
ATOM   1446 O O   . ALA A 1 203 ? 26.724 12.526 27.915  1.00 14.27 ? 203  ALA A O   1 
ATOM   1447 C CB  . ALA A 1 203 ? 29.229 12.364 25.813  1.00 14.96 ? 203  ALA A CB  1 
ATOM   1448 N N   . LYS A 1 204 ? 27.542 14.554 27.352  1.00 17.40 ? 204  LYS A N   1 
ATOM   1449 C CA  . LYS A 1 204 ? 27.145 15.173 28.604  1.00 18.78 ? 204  LYS A CA  1 
ATOM   1450 C C   . LYS A 1 204 ? 25.620 15.270 28.681  1.00 19.99 ? 204  LYS A C   1 
ATOM   1451 O O   . LYS A 1 204 ? 25.032 15.077 29.746  1.00 18.31 ? 204  LYS A O   1 
ATOM   1452 C CB  . LYS A 1 204 ? 27.784 16.557 28.718  1.00 19.99 ? 204  LYS A CB  1 
ATOM   1453 C CG  . LYS A 1 204 ? 27.625 17.194 30.080  1.00 27.56 ? 204  LYS A CG  1 
ATOM   1454 C CD  . LYS A 1 204 ? 28.494 18.435 30.226  1.00 30.52 ? 204  LYS A CD  1 
ATOM   1455 C CE  . LYS A 1 204 ? 28.333 19.027 31.619  1.00 33.59 ? 204  LYS A CE  1 
ATOM   1456 N NZ  . LYS A 1 204 ? 29.223 20.202 31.835  1.00 36.42 ? 204  LYS A NZ  1 
ATOM   1457 N N   . THR A 1 205 ? 24.973 15.562 27.552  1.00 19.36 ? 205  THR A N   1 
ATOM   1458 C CA  . THR A 1 205 ? 23.518 15.655 27.549  1.00 20.33 ? 205  THR A CA  1 
ATOM   1459 C C   . THR A 1 205 ? 22.911 14.262 27.626  1.00 20.50 ? 205  THR A C   1 
ATOM   1460 O O   . THR A 1 205 ? 21.718 14.113 27.869  1.00 23.58 ? 205  THR A O   1 
ATOM   1461 C CB  . THR A 1 205 ? 22.967 16.357 26.277  1.00 20.46 ? 205  THR A CB  1 
ATOM   1462 O OG1 . THR A 1 205 ? 23.398 15.653 25.101  1.00 19.10 ? 205  THR A OG1 1 
ATOM   1463 C CG2 . THR A 1 205 ? 23.427 17.790 26.223  1.00 20.27 ? 205  THR A CG2 1 
ATOM   1464 N N   . SER A 1 206 ? 23.736 13.243 27.416  1.00 19.45 ? 206  SER A N   1 
ATOM   1465 C CA  . SER A 1 206 ? 23.275 11.861 27.469  1.00 19.26 ? 206  SER A CA  1 
ATOM   1466 C C   . SER A 1 206 ? 23.480 11.264 28.856  1.00 21.34 ? 206  SER A C   1 
ATOM   1467 O O   . SER A 1 206 ? 22.640 10.510 29.353  1.00 21.24 ? 206  SER A O   1 
ATOM   1468 C CB  . SER A 1 206 ? 24.028 11.011 26.448  1.00 19.61 ? 206  SER A CB  1 
ATOM   1469 O OG  . SER A 1 206 ? 23.695 9.643  26.606  1.00 21.18 ? 206  SER A OG  1 
ATOM   1470 N N   . LEU A 1 207 ? 24.594 11.620 29.486  1.00 21.72 ? 207  LEU A N   1 
ATOM   1471 C CA  . LEU A 1 207 ? 24.930 11.097 30.810  1.00 22.27 ? 207  LEU A CA  1 
ATOM   1472 C C   . LEU A 1 207 ? 24.384 11.902 31.981  1.00 24.42 ? 207  LEU A C   1 
ATOM   1473 O O   . LEU A 1 207 ? 24.687 11.603 33.136  1.00 27.29 ? 207  LEU A O   1 
ATOM   1474 C CB  . LEU A 1 207 ? 26.449 10.968 30.934  1.00 20.59 ? 207  LEU A CB  1 
ATOM   1475 C CG  . LEU A 1 207 ? 27.015 9.908  29.982  1.00 19.56 ? 207  LEU A CG  1 
ATOM   1476 C CD1 . LEU A 1 207 ? 28.522 10.036 29.852  1.00 20.62 ? 207  LEU A CD1 1 
ATOM   1477 C CD2 . LEU A 1 207 ? 26.622 8.533  30.491  1.00 20.14 ? 207  LEU A CD2 1 
HETATM 1478 N N   . CME A 1 208 ? 23.549 12.667 31.865  0.50 21.71 ? 208  CME A N   1 
HETATM 1479 C CA  . CME A 1 208 ? 22.971 13.489 32.913  0.50 23.80 ? 208  CME A CA  1 
HETATM 1480 C CB  . CME A 1 208 ? 22.178 14.640 32.296  0.50 24.08 ? 208  CME A CB  1 
HETATM 1481 S SG  . CME A 1 208 ? 21.058 14.105 30.969  0.70 27.36 ? 208  CME A SG  1 
HETATM 1482 S SD  . CME A 1 208 ? 19.549 13.160 31.942  0.70 30.06 ? 208  CME A SD  1 
HETATM 1483 C CE  . CME A 1 208 ? 18.186 14.351 31.890  0.70 28.20 ? 208  CME A CE  1 
HETATM 1484 C CZ  . CME A 1 208 ? 18.647 15.721 32.312  0.70 30.71 ? 208  CME A CZ  1 
HETATM 1485 O OH  . CME A 1 208 ? 19.191 15.757 33.463  0.75 32.13 ? 208  CME A OH  1 
HETATM 1486 C C   . CME A 1 208 ? 22.063 12.639 33.790  0.50 23.27 ? 208  CME A C   1 
HETATM 1487 O O   . CME A 1 208 ? 21.652 11.543 33.400  0.50 23.65 ? 208  CME A O   1 
ATOM   1488 N N   . LYS A 1 209 ? 21.088 13.142 34.741  1.00 48.67 ? 209  LYS A N   1 
ATOM   1489 C CA  . LYS A 1 209 ? 20.383 12.044 35.394  1.00 51.51 ? 209  LYS A CA  1 
ATOM   1490 C C   . LYS A 1 209 ? 18.876 12.171 35.211  1.00 47.31 ? 209  LYS A C   1 
ATOM   1491 O O   . LYS A 1 209 ? 18.339 13.276 35.075  1.00 46.21 ? 209  LYS A O   1 
ATOM   1492 C CB  . LYS A 1 209 ? 20.728 12.042 36.896  1.00 50.51 ? 209  LYS A CB  1 
ATOM   1493 C CG  . LYS A 1 209 ? 19.658 11.382 37.755  1.00 50.44 ? 209  LYS A CG  1 
ATOM   1494 C CD  . LYS A 1 209 ? 19.866 11.614 39.251  1.00 48.86 ? 209  LYS A CD  1 
ATOM   1495 C CE  . LYS A 1 209 ? 21.036 12.547 39.548  1.00 48.27 ? 209  LYS A CE  1 
ATOM   1496 N NZ  . LYS A 1 209 ? 21.885 12.070 40.647  1.00 47.61 ? 209  LYS A NZ  1 
ATOM   1497 N N   . VAL A 1 210 ? 18.452 10.871 34.526  1.00 49.44 ? 210  VAL A N   1 
ATOM   1498 C CA  . VAL A 1 210 ? 17.159 10.728 33.863  1.00 49.55 ? 210  VAL A CA  1 
ATOM   1499 C C   . VAL A 1 210 ? 16.125 10.361 34.915  1.00 50.82 ? 210  VAL A C   1 
ATOM   1500 O O   . VAL A 1 210 ? 16.387 9.533  35.786  1.00 50.74 ? 210  VAL A O   1 
ATOM   1501 C CB  . VAL A 1 210 ? 17.193 9.613  32.787  1.00 48.21 ? 210  VAL A CB  1 
ATOM   1502 C CG1 . VAL A 1 210 ? 15.817 9.461  32.152  1.00 46.66 ? 210  VAL A CG1 1 
ATOM   1503 C CG2 . VAL A 1 210 ? 18.229 9.924  31.730  1.00 45.54 ? 210  VAL A CG2 1 
ATOM   1504 N N   . SER A 1 211 ? 14.993 11.019 34.806  1.00 51.80 ? 211  SER A N   1 
ATOM   1505 C CA  . SER A 1 211 ? 13.885 10.727 35.714  1.00 53.70 ? 211  SER A CA  1 
ATOM   1506 C C   . SER A 1 211 ? 14.287 10.899 37.175  1.00 54.60 ? 211  SER A C   1 
ATOM   1507 O O   . SER A 1 211 ? 13.809 10.175 38.052  1.00 55.75 ? 211  SER A O   1 
ATOM   1508 C CB  . SER A 1 211 ? 13.386 9.295  35.483  1.00 53.15 ? 211  SER A CB  1 
ATOM   1509 O OG  . SER A 1 211 ? 12.313 8.976  36.352  1.00 55.79 ? 211  SER A OG  1 
ATOM   1510 N N   . SER A 1 218 ? 6.162  0.964  34.697  1.00 49.91 ? 218  SER A N   1 
ATOM   1511 C CA  . SER A 1 218 ? 5.704  -0.416 34.559  1.00 48.82 ? 218  SER A CA  1 
ATOM   1512 C C   . SER A 1 218 ? 5.392  -0.743 33.103  1.00 47.13 ? 218  SER A C   1 
ATOM   1513 O O   . SER A 1 218 ? 5.134  -1.897 32.759  1.00 47.70 ? 218  SER A O   1 
ATOM   1514 C CB  . SER A 1 218 ? 4.452  -0.648 35.408  1.00 49.12 ? 218  SER A CB  1 
ATOM   1515 O OG  . SER A 1 218 ? 3.373  0.150  34.954  1.00 50.63 ? 218  SER A OG  1 
ATOM   1516 N N   . THR A 1 219 ? 5.412  0.277  32.251  1.00 44.13 ? 219  THR A N   1 
ATOM   1517 C CA  . THR A 1 219 ? 5.127  0.083  30.835  1.00 40.38 ? 219  THR A CA  1 
ATOM   1518 C C   . THR A 1 219 ? 6.272  -0.641 30.141  1.00 38.36 ? 219  THR A C   1 
ATOM   1519 O O   . THR A 1 219 ? 7.322  -0.882 30.742  1.00 37.52 ? 219  THR A O   1 
ATOM   1520 C CB  . THR A 1 219 ? 4.906  1.424  30.117  1.00 39.67 ? 219  THR A CB  1 
ATOM   1521 O OG1 . THR A 1 219 ? 4.657  1.184  28.726  1.00 40.41 ? 219  THR A OG1 1 
ATOM   1522 C CG2 . THR A 1 219 ? 6.130  2.311  30.260  1.00 39.50 ? 219  THR A CG2 1 
ATOM   1523 N N   . SER A 1 220 ? 6.057  -0.987 28.875  1.00 33.56 ? 220  SER A N   1 
ATOM   1524 C CA  . SER A 1 220 ? 7.070  -1.672 28.083  1.00 32.47 ? 220  SER A CA  1 
ATOM   1525 C C   . SER A 1 220 ? 7.308  -0.918 26.775  1.00 27.89 ? 220  SER A C   1 
ATOM   1526 O O   . SER A 1 220 ? 8.276  -1.184 26.061  1.00 32.04 ? 220  SER A O   1 
ATOM   1527 C CB  . SER A 1 220 ? 6.626  -3.109 27.789  1.00 33.35 ? 220  SER A CB  1 
ATOM   1528 O OG  . SER A 1 220 ? 5.357  -3.122 27.159  1.00 34.14 ? 220  SER A OG  1 
ATOM   1529 N N   . SER A 1 221 ? 6.423  0.025  26.470  1.00 24.41 ? 221  SER A N   1 
ATOM   1530 C CA  . SER A 1 221 ? 6.536  0.815  25.254  1.00 22.19 ? 221  SER A CA  1 
ATOM   1531 C C   . SER A 1 221 ? 7.679  1.821  25.348  1.00 21.11 ? 221  SER A C   1 
ATOM   1532 O O   . SER A 1 221 ? 7.699  2.662  26.247  1.00 19.54 ? 221  SER A O   1 
ATOM   1533 C CB  . SER A 1 221 ? 5.237  1.571  24.989  1.00 25.31 ? 221  SER A CB  1 
ATOM   1534 O OG  . SER A 1 221 ? 5.419  2.502  23.934  1.00 28.26 ? 221  SER A OG  1 
ATOM   1535 N N   . VAL A 1 222 ? 8.626  1.742  24.419  1.00 19.35 ? 222  VAL A N   1 
ATOM   1536 C CA  . VAL A 1 222 ? 9.741  2.671  24.441  1.00 18.20 ? 222  VAL A CA  1 
ATOM   1537 C C   . VAL A 1 222 ? 9.216  4.098  24.247  1.00 18.04 ? 222  VAL A C   1 
ATOM   1538 O O   . VAL A 1 222 ? 9.676  5.032  24.901  1.00 17.73 ? 222  VAL A O   1 
ATOM   1539 C CB  . VAL A 1 222 ? 10.797 2.328  23.353  1.00 17.90 ? 222  VAL A CB  1 
ATOM   1540 C CG1 . VAL A 1 222 ? 10.184 2.416  21.954  1.00 17.00 ? 222  VAL A CG1 1 
ATOM   1541 C CG2 . VAL A 1 222 ? 11.991 3.271  23.488  1.00 17.24 ? 222  VAL A CG2 1 
ATOM   1542 N N   . PHE A 1 223 ? 8.223  4.269  23.383  1.00 17.54 ? 223  PHE A N   1 
ATOM   1543 C CA  . PHE A 1 223 ? 7.685  5.611  23.164  1.00 17.79 ? 223  PHE A CA  1 
ATOM   1544 C C   . PHE A 1 223 ? 6.990  6.171  24.402  1.00 18.81 ? 223  PHE A C   1 
ATOM   1545 O O   . PHE A 1 223 ? 7.062  7.371  24.678  1.00 18.81 ? 223  PHE A O   1 
ATOM   1546 C CB  . PHE A 1 223 ? 6.749  5.621  21.958  1.00 17.02 ? 223  PHE A CB  1 
ATOM   1547 C CG  . PHE A 1 223 ? 7.443  5.305  20.662  1.00 16.80 ? 223  PHE A CG  1 
ATOM   1548 C CD1 . PHE A 1 223 ? 8.718  5.805  20.404  1.00 17.87 ? 223  PHE A CD1 1 
ATOM   1549 C CD2 . PHE A 1 223 ? 6.824  4.521  19.695  1.00 18.33 ? 223  PHE A CD2 1 
ATOM   1550 C CE1 . PHE A 1 223 ? 9.370  5.530  19.203  1.00 16.82 ? 223  PHE A CE1 1 
ATOM   1551 C CE2 . PHE A 1 223 ? 7.471  4.240  18.487  1.00 22.10 ? 223  PHE A CE2 1 
ATOM   1552 C CZ  . PHE A 1 223 ? 8.750  4.748  18.243  1.00 18.51 ? 223  PHE A CZ  1 
ATOM   1553 N N   . GLU A 1 224 ? 6.331  5.299  25.157  1.00 20.52 ? 224  GLU A N   1 
ATOM   1554 C CA  . GLU A 1 224 ? 5.659  5.712  26.383  1.00 22.51 ? 224  GLU A CA  1 
ATOM   1555 C C   . GLU A 1 224 ? 6.722  6.187  27.373  1.00 21.00 ? 224  GLU A C   1 
ATOM   1556 O O   . GLU A 1 224 ? 6.603  7.252  27.984  1.00 18.84 ? 224  GLU A O   1 
ATOM   1557 C CB  . GLU A 1 224 ? 4.905  4.528  26.985  1.00 25.78 ? 224  GLU A CB  1 
ATOM   1558 C CG  . GLU A 1 224 ? 4.233  4.822  28.312  1.00 33.97 ? 224  GLU A CG  1 
ATOM   1559 C CD  . GLU A 1 224 ? 2.920  5.554  28.138  1.00 38.55 ? 224  GLU A CD  1 
ATOM   1560 O OE1 . GLU A 1 224 ? 2.104  5.085  27.316  1.00 40.67 ? 224  GLU A OE1 1 
ATOM   1561 O OE2 . GLU A 1 224 ? 2.703  6.581  28.821  1.00 40.72 ? 224  GLU A OE2 1 
ATOM   1562 N N   . LYS A 1 225 ? 7.761  5.377  27.534  1.00 19.89 ? 225  LYS A N   1 
ATOM   1563 C CA  . LYS A 1 225 ? 8.848  5.708  28.446  1.00 20.42 ? 225  LYS A CA  1 
ATOM   1564 C C   . LYS A 1 225 ? 9.531  7.026  28.094  1.00 19.42 ? 225  LYS A C   1 
ATOM   1565 O O   . LYS A 1 225 ? 9.717  7.880  28.957  1.00 18.98 ? 225  LYS A O   1 
ATOM   1566 C CB  . LYS A 1 225 ? 9.885  4.584  28.455  1.00 23.61 ? 225  LYS A CB  1 
ATOM   1567 C CG  . LYS A 1 225 ? 9.374  3.276  29.040  1.00 24.30 ? 225  LYS A CG  1 
ATOM   1568 C CD  . LYS A 1 225 ? 10.387 2.165  28.846  1.00 25.42 ? 225  LYS A CD  1 
ATOM   1569 C CE  . LYS A 1 225 ? 9.806  0.816  29.226  1.00 27.65 ? 225  LYS A CE  1 
ATOM   1570 N NZ  . LYS A 1 225 ? 10.771 -0.279 28.966  1.00 28.12 ? 225  LYS A NZ  1 
ATOM   1571 N N   . LEU A 1 226 ? 9.900  7.211  26.831  1.00 19.11 ? 226  LEU A N   1 
ATOM   1572 C CA  . LEU A 1 226 ? 10.568 8.452  26.466  1.00 20.69 ? 226  LEU A CA  1 
ATOM   1573 C C   . LEU A 1 226 ? 9.654  9.672  26.569  1.00 19.29 ? 226  LEU A C   1 
ATOM   1574 O O   . LEU A 1 226 ? 10.111 10.765 26.896  1.00 19.24 ? 226  LEU A O   1 
ATOM   1575 C CB  . LEU A 1 226 ? 11.163 8.349  25.060  1.00 23.84 ? 226  LEU A CB  1 
ATOM   1576 C CG  . LEU A 1 226 ? 10.253 8.290  23.837  1.00 25.11 ? 226  LEU A CG  1 
ATOM   1577 C CD1 . LEU A 1 226 ? 9.770  9.692  23.483  1.00 28.77 ? 226  LEU A CD1 1 
ATOM   1578 C CD2 . LEU A 1 226 ? 11.044 7.696  22.667  1.00 26.36 ? 226  LEU A CD2 1 
ATOM   1579 N N   . SER A 1 227 ? 8.365  9.480  26.309  1.00 18.81 ? 227  SER A N   1 
ATOM   1580 C CA  . SER A 1 227 ? 7.402  10.580 26.364  1.00 19.35 ? 227  SER A CA  1 
ATOM   1581 C C   . SER A 1 227 ? 7.256  11.182 27.755  1.00 20.47 ? 227  SER A C   1 
ATOM   1582 O O   . SER A 1 227 ? 6.949  12.365 27.899  1.00 19.77 ? 227  SER A O   1 
ATOM   1583 C CB  . SER A 1 227 ? 6.032  10.110 25.876  1.00 21.10 ? 227  SER A CB  1 
ATOM   1584 O OG  . SER A 1 227 ? 6.059  9.781  24.499  1.00 20.38 ? 227  SER A OG  1 
ATOM   1585 N N   . LYS A 1 228 ? 7.483  10.365 28.778  1.00 21.68 ? 228  LYS A N   1 
ATOM   1586 C CA  . LYS A 1 228 ? 7.358  10.822 30.154  1.00 24.47 ? 228  LYS A CA  1 
ATOM   1587 C C   . LYS A 1 228 ? 8.686  11.256 30.752  1.00 24.76 ? 228  LYS A C   1 
ATOM   1588 O O   . LYS A 1 228 ? 8.740  11.668 31.907  1.00 25.90 ? 228  LYS A O   1 
ATOM   1589 C CB  . LYS A 1 228 ? 6.764  9.709  31.023  1.00 26.50 ? 228  LYS A CB  1 
ATOM   1590 C CG  . LYS A 1 228 ? 5.373  9.245  30.608  1.00 29.55 ? 228  LYS A CG  1 
ATOM   1591 C CD  . LYS A 1 228 ? 4.354  10.357 30.737  1.00 31.97 ? 228  LYS A CD  1 
ATOM   1592 C CE  . LYS A 1 228 ? 2.938  9.831  30.544  1.00 34.70 ? 228  LYS A CE  1 
ATOM   1593 N NZ  . LYS A 1 228 ? 1.925  10.924 30.619  1.00 33.87 ? 228  LYS A NZ  1 
ATOM   1594 N N   . THR A 1 229 ? 9.758  11.181 29.971  1.00 24.24 ? 229  THR A N   1 
ATOM   1595 C CA  . THR A 1 229 ? 11.064 11.546 30.493  1.00 21.95 ? 229  THR A CA  1 
ATOM   1596 C C   . THR A 1 229 ? 11.814 12.673 29.784  1.00 20.84 ? 229  THR A C   1 
ATOM   1597 O O   . THR A 1 229 ? 13.022 12.806 29.957  1.00 21.49 ? 229  THR A O   1 
ATOM   1598 C CB  . THR A 1 229 ? 11.971 10.299 30.569  1.00 22.59 ? 229  THR A CB  1 
ATOM   1599 O OG1 . THR A 1 229 ? 12.060 9.681  29.278  1.00 22.45 ? 229  THR A OG1 1 
ATOM   1600 C CG2 . THR A 1 229 ? 11.399 9.301  31.573  1.00 24.05 ? 229  THR A CG2 1 
ATOM   1601 N N   . PHE A 1 230 ? 11.113 13.474 28.984  1.00 19.71 ? 230  PHE A N   1 
ATOM   1602 C CA  . PHE A 1 230 ? 11.750 14.608 28.323  1.00 20.84 ? 230  PHE A CA  1 
ATOM   1603 C C   . PHE A 1 230 ? 12.191 15.521 29.468  1.00 22.58 ? 230  PHE A C   1 
ATOM   1604 O O   . PHE A 1 230 ? 11.483 15.633 30.476  1.00 21.98 ? 230  PHE A O   1 
ATOM   1605 C CB  . PHE A 1 230 ? 10.754 15.349 27.426  1.00 21.07 ? 230  PHE A CB  1 
ATOM   1606 C CG  . PHE A 1 230 ? 10.423 14.626 26.149  1.00 20.23 ? 230  PHE A CG  1 
ATOM   1607 C CD1 . PHE A 1 230 ? 11.412 14.370 25.204  1.00 18.02 ? 230  PHE A CD1 1 
ATOM   1608 C CD2 . PHE A 1 230 ? 9.120  14.212 25.884  1.00 18.99 ? 230  PHE A CD2 1 
ATOM   1609 C CE1 . PHE A 1 230 ? 11.107 13.709 24.008  1.00 19.01 ? 230  PHE A CE1 1 
ATOM   1610 C CE2 . PHE A 1 230 ? 8.802  13.553 24.693  1.00 19.65 ? 230  PHE A CE2 1 
ATOM   1611 C CZ  . PHE A 1 230 ? 9.801  13.301 23.752  1.00 18.31 ? 230  PHE A CZ  1 
ATOM   1612 N N   . SER A 1 231 ? 13.348 16.165 29.331  1.00 20.05 ? 231  SER A N   1 
ATOM   1613 C CA  . SER A 1 231 ? 13.849 17.027 30.401  1.00 22.47 ? 231  SER A CA  1 
ATOM   1614 C C   . SER A 1 231 ? 13.977 18.512 30.068  1.00 23.46 ? 231  SER A C   1 
ATOM   1615 O O   . SER A 1 231 ? 14.599 18.894 29.077  1.00 23.16 ? 231  SER A O   1 
ATOM   1616 C CB  . SER A 1 231 ? 15.203 16.514 30.894  1.00 21.77 ? 231  SER A CB  1 
ATOM   1617 O OG  . SER A 1 231 ? 15.697 17.327 31.945  1.00 22.74 ? 231  SER A OG  1 
ATOM   1618 N N   . GLN A 1 232 ? 13.403 19.348 30.927  1.00 25.41 ? 232  GLN A N   1 
ATOM   1619 C CA  . GLN A 1 232 ? 13.451 20.790 30.734  1.00 25.89 ? 232  GLN A CA  1 
ATOM   1620 C C   . GLN A 1 232 ? 14.876 21.330 30.875  1.00 23.48 ? 232  GLN A C   1 
ATOM   1621 O O   . GLN A 1 232 ? 15.169 22.445 30.456  1.00 24.05 ? 232  GLN A O   1 
ATOM   1622 C CB  . GLN A 1 232 ? 12.540 21.480 31.751  1.00 30.59 ? 232  GLN A CB  1 
ATOM   1623 C CG  . GLN A 1 232 ? 12.284 22.942 31.445  1.00 35.89 ? 232  GLN A CG  1 
ATOM   1624 C CD  . GLN A 1 232 ? 11.724 23.141 30.049  1.00 39.76 ? 232  GLN A CD  1 
ATOM   1625 O OE1 . GLN A 1 232 ? 10.657 22.626 29.716  1.00 41.31 ? 232  GLN A OE1 1 
ATOM   1626 N NE2 . GLN A 1 232 ? 12.447 23.889 29.221  1.00 44.72 ? 232  GLN A NE2 1 
ATOM   1627 N N   . THR A 1 233 ? 15.766 20.533 31.450  1.00 21.33 ? 233  THR A N   1 
ATOM   1628 C CA  . THR A 1 233 ? 17.148 20.966 31.648  1.00 20.76 ? 233  THR A CA  1 
ATOM   1629 C C   . THR A 1 233 ? 18.026 20.924 30.396  1.00 20.06 ? 233  THR A C   1 
ATOM   1630 O O   . THR A 1 233 ? 19.123 21.478 30.393  1.00 19.75 ? 233  THR A O   1 
ATOM   1631 C CB  . THR A 1 233 ? 17.841 20.115 32.712  1.00 20.95 ? 233  THR A CB  1 
ATOM   1632 O OG1 . THR A 1 233 ? 17.906 18.760 32.256  1.00 19.72 ? 233  THR A OG1 1 
ATOM   1633 C CG2 . THR A 1 233 ? 17.077 20.174 34.026  1.00 22.49 ? 233  THR A CG2 1 
ATOM   1634 N N   . ILE A 1 234 ? 17.554 20.269 29.339  1.00 18.89 ? 234  ILE A N   1 
ATOM   1635 C CA  . ILE A 1 234 ? 18.330 20.160 28.104  1.00 18.93 ? 234  ILE A CA  1 
ATOM   1636 C C   . ILE A 1 234 ? 18.071 21.332 27.160  1.00 20.28 ? 234  ILE A C   1 
ATOM   1637 O O   . ILE A 1 234 ? 16.961 21.513 26.666  1.00 22.40 ? 234  ILE A O   1 
ATOM   1638 C CB  . ILE A 1 234 ? 18.011 18.835 27.364  1.00 17.25 ? 234  ILE A CB  1 
ATOM   1639 C CG1 . ILE A 1 234 ? 18.300 17.641 28.283  1.00 19.04 ? 234  ILE A CG1 1 
ATOM   1640 C CG2 . ILE A 1 234 ? 18.821 18.747 26.063  1.00 18.67 ? 234  ILE A CG2 1 
ATOM   1641 C CD1 . ILE A 1 234 ? 19.763 17.470 28.674  1.00 18.07 ? 234  ILE A CD1 1 
ATOM   1642 N N   . PRO A 1 235 ? 19.105 22.138 26.885  1.00 20.95 ? 235  PRO A N   1 
ATOM   1643 C CA  . PRO A 1 235 ? 18.982 23.299 25.998  1.00 21.67 ? 235  PRO A CA  1 
ATOM   1644 C C   . PRO A 1 235 ? 19.037 22.926 24.523  1.00 21.06 ? 235  PRO A C   1 
ATOM   1645 O O   . PRO A 1 235 ? 19.456 21.823 24.169  1.00 19.47 ? 235  PRO A O   1 
ATOM   1646 C CB  . PRO A 1 235 ? 20.171 24.153 26.408  1.00 24.22 ? 235  PRO A CB  1 
ATOM   1647 C CG  . PRO A 1 235 ? 21.230 23.101 26.647  1.00 23.43 ? 235  PRO A CG  1 
ATOM   1648 C CD  . PRO A 1 235 ? 20.472 22.039 27.436  1.00 22.95 ? 235  PRO A CD  1 
ATOM   1649 N N   . ASP A 1 236 ? 18.604 23.841 23.662  1.00 20.98 ? 236  ASP A N   1 
ATOM   1650 C CA  . ASP A 1 236 ? 18.653 23.582 22.230  1.00 21.18 ? 236  ASP A CA  1 
ATOM   1651 C C   . ASP A 1 236 ? 20.107 23.723 21.817  1.00 20.70 ? 236  ASP A C   1 
ATOM   1652 O O   . ASP A 1 236 ? 20.813 24.601 22.311  1.00 18.84 ? 236  ASP A O   1 
ATOM   1653 C CB  . ASP A 1 236 ? 17.807 24.589 21.438  1.00 22.64 ? 236  ASP A CB  1 
ATOM   1654 C CG  . ASP A 1 236 ? 16.315 24.406 21.648  1.00 27.80 ? 236  ASP A CG  1 
ATOM   1655 O OD1 . ASP A 1 236 ? 15.868 23.274 21.946  1.00 26.46 ? 236  ASP A OD1 1 
ATOM   1656 O OD2 . ASP A 1 236 ? 15.582 25.401 21.489  1.00 31.40 ? 236  ASP A OD2 1 
ATOM   1657 N N   . ILE A 1 237 ? 20.549 22.851 20.921  1.00 19.12 ? 237  ILE A N   1 
ATOM   1658 C CA  . ILE A 1 237 ? 21.922 22.870 20.431  1.00 19.73 ? 237  ILE A CA  1 
ATOM   1659 C C   . ILE A 1 237 ? 21.863 23.004 18.914  1.00 19.34 ? 237  ILE A C   1 
ATOM   1660 O O   . ILE A 1 237 ? 21.260 22.174 18.239  1.00 23.41 ? 237  ILE A O   1 
ATOM   1661 C CB  . ILE A 1 237 ? 22.658 21.557 20.795  1.00 17.34 ? 237  ILE A CB  1 
ATOM   1662 C CG1 . ILE A 1 237 ? 22.709 21.395 22.318  1.00 16.37 ? 237  ILE A CG1 1 
ATOM   1663 C CG2 . ILE A 1 237 ? 24.073 21.572 20.208  1.00 19.46 ? 237  ILE A CG2 1 
ATOM   1664 C CD1 . ILE A 1 237 ? 23.281 20.064 22.770  1.00 16.29 ? 237  ILE A CD1 1 
ATOM   1665 N N   . PHE A 1 238 ? 22.487 24.047 18.384  1.00 19.56 ? 238  PHE A N   1 
ATOM   1666 C CA  . PHE A 1 238 ? 22.486 24.297 16.944  1.00 20.54 ? 238  PHE A CA  1 
ATOM   1667 C C   . PHE A 1 238 ? 23.834 23.970 16.315  1.00 19.51 ? 238  PHE A C   1 
ATOM   1668 O O   . PHE A 1 238 ? 24.872 24.429 16.784  1.00 19.44 ? 238  PHE A O   1 
ATOM   1669 C CB  . PHE A 1 238 ? 22.138 25.762 16.680  1.00 22.52 ? 238  PHE A CB  1 
ATOM   1670 C CG  . PHE A 1 238 ? 20.783 26.156 17.188  1.00 26.58 ? 238  PHE A CG  1 
ATOM   1671 C CD1 . PHE A 1 238 ? 19.676 26.119 16.354  1.00 28.24 ? 238  PHE A CD1 1 
ATOM   1672 C CD2 . PHE A 1 238 ? 20.607 26.523 18.519  1.00 27.29 ? 238  PHE A CD2 1 
ATOM   1673 C CE1 . PHE A 1 238 ? 18.405 26.441 16.842  1.00 28.64 ? 238  PHE A CE1 1 
ATOM   1674 C CE2 . PHE A 1 238 ? 19.342 26.845 19.012  1.00 26.22 ? 238  PHE A CE2 1 
ATOM   1675 C CZ  . PHE A 1 238 ? 18.244 26.803 18.170  1.00 25.08 ? 238  PHE A CZ  1 
ATOM   1676 N N   . VAL A 1 239 ? 23.815 23.175 15.253  1.00 18.70 ? 239  VAL A N   1 
ATOM   1677 C CA  . VAL A 1 239 ? 25.050 22.809 14.583  1.00 19.81 ? 239  VAL A CA  1 
ATOM   1678 C C   . VAL A 1 239 ? 25.028 23.264 13.127  1.00 20.70 ? 239  VAL A C   1 
ATOM   1679 O O   . VAL A 1 239 ? 23.973 23.315 12.491  1.00 18.68 ? 239  VAL A O   1 
ATOM   1680 C CB  . VAL A 1 239 ? 25.306 21.275 14.671  1.00 20.36 ? 239  VAL A CB  1 
ATOM   1681 C CG1 . VAL A 1 239 ? 25.330 20.845 16.135  1.00 21.08 ? 239  VAL A CG1 1 
ATOM   1682 C CG2 . VAL A 1 239 ? 24.243 20.515 13.920  1.00 22.42 ? 239  VAL A CG2 1 
ATOM   1683 N N   . PRO A 1 240 ? 26.205 23.614 12.584  1.00 21.15 ? 240  PRO A N   1 
ATOM   1684 C CA  . PRO A 1 240 ? 26.327 24.072 11.199  1.00 18.93 ? 240  PRO A CA  1 
ATOM   1685 C C   . PRO A 1 240 ? 26.016 23.009 10.151  1.00 20.40 ? 240  PRO A C   1 
ATOM   1686 O O   . PRO A 1 240 ? 26.052 21.806 10.422  1.00 18.82 ? 240  PRO A O   1 
ATOM   1687 C CB  . PRO A 1 240 ? 27.773 24.546 11.127  1.00 18.34 ? 240  PRO A CB  1 
ATOM   1688 C CG  . PRO A 1 240 ? 28.469 23.596 12.066  1.00 19.95 ? 240  PRO A CG  1 
ATOM   1689 C CD  . PRO A 1 240 ? 27.525 23.578 13.242  1.00 20.56 ? 240  PRO A CD  1 
ATOM   1690 N N   . GLY A 1 241 ? 25.694 23.477 8.952   1.00 20.54 ? 241  GLY A N   1 
ATOM   1691 C CA  . GLY A 1 241 ? 25.403 22.587 7.848   1.00 21.45 ? 241  GLY A CA  1 
ATOM   1692 C C   . GLY A 1 241 ? 26.334 23.001 6.730   1.00 22.30 ? 241  GLY A C   1 
ATOM   1693 O O   . GLY A 1 241 ? 27.118 23.931 6.898   1.00 23.77 ? 241  GLY A O   1 
ATOM   1694 N N   . PHE A 1 242 ? 26.263 22.323 5.593   1.00 23.81 ? 242  PHE A N   1 
ATOM   1695 C CA  . PHE A 1 242 ? 27.119 22.677 4.475   1.00 25.77 ? 242  PHE A CA  1 
ATOM   1696 C C   . PHE A 1 242 ? 26.282 23.104 3.272   1.00 28.60 ? 242  PHE A C   1 
ATOM   1697 O O   . PHE A 1 242 ? 25.460 22.337 2.770   1.00 28.53 ? 242  PHE A O   1 
ATOM   1698 C CB  . PHE A 1 242 ? 28.008 21.496 4.082   1.00 23.20 ? 242  PHE A CB  1 
ATOM   1699 C CG  . PHE A 1 242 ? 29.110 21.865 3.131   1.00 25.25 ? 242  PHE A CG  1 
ATOM   1700 C CD1 . PHE A 1 242 ? 30.227 22.562 3.579   1.00 23.11 ? 242  PHE A CD1 1 
ATOM   1701 C CD2 . PHE A 1 242 ? 29.021 21.542 1.780   1.00 26.74 ? 242  PHE A CD2 1 
ATOM   1702 C CE1 . PHE A 1 242 ? 31.241 22.935 2.699   1.00 24.39 ? 242  PHE A CE1 1 
ATOM   1703 C CE2 . PHE A 1 242 ? 30.034 21.914 0.890   1.00 27.15 ? 242  PHE A CE2 1 
ATOM   1704 C CZ  . PHE A 1 242 ? 31.145 22.612 1.356   1.00 25.77 ? 242  PHE A CZ  1 
ATOM   1705 N N   . ASN A 1 243 ? 26.486 24.336 2.824   1.00 31.25 ? 243  ASN A N   1 
ATOM   1706 C CA  . ASN A 1 243 ? 25.771 24.850 1.664   1.00 34.15 ? 243  ASN A CA  1 
ATOM   1707 C C   . ASN A 1 243 ? 26.565 24.446 0.425   1.00 34.88 ? 243  ASN A C   1 
ATOM   1708 O O   . ASN A 1 243 ? 27.592 25.050 0.118   1.00 34.47 ? 243  ASN A O   1 
ATOM   1709 C CB  . ASN A 1 243 ? 25.673 26.371 1.740   1.00 36.69 ? 243  ASN A CB  1 
ATOM   1710 C CG  . ASN A 1 243 ? 24.867 26.960 0.603   1.00 38.25 ? 243  ASN A CG  1 
ATOM   1711 O OD1 . ASN A 1 243 ? 25.159 26.725 -0.568  1.00 39.86 ? 243  ASN A OD1 1 
ATOM   1712 N ND2 . ASN A 1 243 ? 23.847 27.736 0.945   1.00 40.27 ? 243  ASN A ND2 1 
ATOM   1713 N N   . HIS A 1 244 ? 26.096 23.418 -0.275  1.00 36.87 ? 244  HIS A N   1 
ATOM   1714 C CA  . HIS A 1 244 ? 26.774 22.928 -1.470  1.00 39.01 ? 244  HIS A CA  1 
ATOM   1715 C C   . HIS A 1 244 ? 26.811 23.940 -2.606  1.00 39.99 ? 244  HIS A C   1 
ATOM   1716 O O   . HIS A 1 244 ? 27.601 23.801 -3.541  1.00 40.60 ? 244  HIS A O   1 
ATOM   1717 C CB  . HIS A 1 244 ? 26.121 21.629 -1.946  1.00 40.75 ? 244  HIS A CB  1 
ATOM   1718 C CG  . HIS A 1 244 ? 26.446 20.447 -1.086  1.00 43.46 ? 244  HIS A CG  1 
ATOM   1719 N ND1 . HIS A 1 244 ? 27.693 19.859 -1.071  1.00 44.33 ? 244  HIS A ND1 1 
ATOM   1720 C CD2 . HIS A 1 244 ? 25.701 19.773 -0.177  1.00 43.96 ? 244  HIS A CD2 1 
ATOM   1721 C CE1 . HIS A 1 244 ? 27.704 18.875 -0.189  1.00 43.63 ? 244  HIS A CE1 1 
ATOM   1722 N NE2 . HIS A 1 244 ? 26.508 18.802 0.367   1.00 44.80 ? 244  HIS A NE2 1 
ATOM   1723 N N   . ALA A 1 245 ? 25.964 24.962 -2.521  1.00 40.31 ? 245  ALA A N   1 
ATOM   1724 C CA  . ALA A 1 245 ? 25.920 25.996 -3.548  1.00 40.76 ? 245  ALA A CA  1 
ATOM   1725 C C   . ALA A 1 245 ? 27.051 26.995 -3.342  1.00 40.72 ? 245  ALA A C   1 
ATOM   1726 O O   . ALA A 1 245 ? 27.770 27.331 -4.283  1.00 42.14 ? 245  ALA A O   1 
ATOM   1727 C CB  . ALA A 1 245 ? 24.578 26.715 -3.513  1.00 39.73 ? 245  ALA A CB  1 
ATOM   1728 N N   . LEU A 1 246 ? 27.206 27.465 -2.107  1.00 40.68 ? 246  LEU A N   1 
ATOM   1729 C CA  . LEU A 1 246 ? 28.250 28.431 -1.781  1.00 39.69 ? 246  LEU A CA  1 
ATOM   1730 C C   . LEU A 1 246 ? 29.569 27.747 -1.440  1.00 38.16 ? 246  LEU A C   1 
ATOM   1731 O O   . LEU A 1 246 ? 30.569 28.414 -1.168  1.00 38.41 ? 246  LEU A O   1 
ATOM   1732 C CB  . LEU A 1 246 ? 27.811 29.313 -0.608  1.00 41.13 ? 246  LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 246 ? 26.574 30.191 -0.833  1.00 43.12 ? 246  LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 246 ? 26.280 30.986 0.431   1.00 43.56 ? 246  LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 246 ? 26.809 31.129 -2.008  1.00 42.71 ? 246  LEU A CD2 1 
ATOM   1736 N N   . LYS A 1 247 ? 29.562 26.417 -1.457  1.00 35.46 ? 247  LYS A N   1 
ATOM   1737 C CA  . LYS A 1 247 ? 30.754 25.624 -1.159  1.00 35.02 ? 247  LYS A CA  1 
ATOM   1738 C C   . LYS A 1 247 ? 31.363 25.996 0.201   1.00 31.03 ? 247  LYS A C   1 
ATOM   1739 O O   . LYS A 1 247 ? 32.581 26.138 0.324   1.00 29.51 ? 247  LYS A O   1 
ATOM   1740 C CB  . LYS A 1 247 ? 31.809 25.821 -2.258  1.00 38.44 ? 247  LYS A CB  1 
ATOM   1741 C CG  . LYS A 1 247 ? 31.251 26.113 -3.651  1.00 44.27 ? 247  LYS A CG  1 
ATOM   1742 C CD  . LYS A 1 247 ? 30.394 24.976 -4.191  1.00 47.38 ? 247  LYS A CD  1 
ATOM   1743 C CE  . LYS A 1 247 ? 29.744 25.357 -5.522  1.00 48.81 ? 247  LYS A CE  1 
ATOM   1744 N NZ  . LYS A 1 247 ? 30.744 25.701 -6.579  1.00 49.63 ? 247  LYS A NZ  1 
ATOM   1745 N N   . ASP A 1 248 ? 30.514 26.154 1.212   1.00 27.61 ? 248  ASP A N   1 
ATOM   1746 C CA  . ASP A 1 248 ? 30.968 26.506 2.557   1.00 27.30 ? 248  ASP A CA  1 
ATOM   1747 C C   . ASP A 1 248 ? 29.944 26.155 3.629   1.00 27.99 ? 248  ASP A C   1 
ATOM   1748 O O   . ASP A 1 248 ? 28.763 25.957 3.339   1.00 26.56 ? 248  ASP A O   1 
ATOM   1749 C CB  . ASP A 1 248 ? 31.278 28.006 2.660   1.00 26.39 ? 248  ASP A CB  1 
ATOM   1750 C CG  . ASP A 1 248 ? 32.721 28.337 2.322   1.00 27.37 ? 248  ASP A CG  1 
ATOM   1751 O OD1 . ASP A 1 248 ? 33.624 27.567 2.707   1.00 25.05 ? 248  ASP A OD1 1 
ATOM   1752 O OD2 . ASP A 1 248 ? 32.957 29.381 1.686   1.00 29.68 ? 248  ASP A OD2 1 
ATOM   1753 N N   . PRO A 1 249 ? 30.391 26.073 4.894   1.00 28.87 ? 249  PRO A N   1 
ATOM   1754 C CA  . PRO A 1 249 ? 29.485 25.748 5.998   1.00 30.53 ? 249  PRO A CA  1 
ATOM   1755 C C   . PRO A 1 249 ? 28.527 26.904 6.276   1.00 31.86 ? 249  PRO A C   1 
ATOM   1756 O O   . PRO A 1 249 ? 28.855 28.066 6.037   1.00 32.04 ? 249  PRO A O   1 
ATOM   1757 C CB  . PRO A 1 249 ? 30.440 25.489 7.161   1.00 29.00 ? 249  PRO A CB  1 
ATOM   1758 C CG  . PRO A 1 249 ? 31.576 26.405 6.868   1.00 29.93 ? 249  PRO A CG  1 
ATOM   1759 C CD  . PRO A 1 249 ? 31.775 26.220 5.379   1.00 28.99 ? 249  PRO A CD  1 
ATOM   1760 N N   . THR A 1 250 ? 27.337 26.574 6.766   1.00 31.43 ? 250  THR A N   1 
ATOM   1761 C CA  . THR A 1 250 ? 26.336 27.580 7.079   1.00 32.89 ? 250  THR A CA  1 
ATOM   1762 C C   . THR A 1 250 ? 25.792 27.306 8.483   1.00 32.59 ? 250  THR A C   1 
ATOM   1763 O O   . THR A 1 250 ? 25.544 26.158 8.858   1.00 32.12 ? 250  THR A O   1 
ATOM   1764 C CB  . THR A 1 250 ? 25.202 27.575 6.026   1.00 33.63 ? 250  THR A CB  1 
ATOM   1765 O OG1 . THR A 1 250 ? 24.220 28.555 6.375   1.00 36.44 ? 250  THR A OG1 1 
ATOM   1766 C CG2 . THR A 1 250 ? 24.557 26.207 5.932   1.00 33.68 ? 250  THR A CG2 1 
ATOM   1767 N N   . PRO A 1 251 ? 25.603 28.366 9.279   1.00 32.35 ? 251  PRO A N   1 
ATOM   1768 C CA  . PRO A 1 251 ? 25.105 28.277 10.653  1.00 31.12 ? 251  PRO A CA  1 
ATOM   1769 C C   . PRO A 1 251 ? 23.738 27.667 10.934  1.00 30.49 ? 251  PRO A C   1 
ATOM   1770 O O   . PRO A 1 251 ? 22.836 27.677 10.099  1.00 30.54 ? 251  PRO A O   1 
ATOM   1771 C CB  . PRO A 1 251 ? 25.198 29.723 11.141  1.00 31.27 ? 251  PRO A CB  1 
ATOM   1772 C CG  . PRO A 1 251 ? 24.936 30.506 9.902   1.00 31.77 ? 251  PRO A CG  1 
ATOM   1773 C CD  . PRO A 1 251 ? 25.775 29.776 8.879   1.00 32.10 ? 251  PRO A CD  1 
ATOM   1774 N N   . ASP A 1 252 ? 23.630 27.129 12.147  1.00 31.08 ? 252  ASP A N   1 
ATOM   1775 C CA  . ASP A 1 252 ? 22.425 26.518 12.698  1.00 30.61 ? 252  ASP A CA  1 
ATOM   1776 C C   . ASP A 1 252 ? 21.475 25.802 11.750  1.00 30.03 ? 252  ASP A C   1 
ATOM   1777 O O   . ASP A 1 252 ? 20.279 26.097 11.737  1.00 32.53 ? 252  ASP A O   1 
ATOM   1778 C CB  . ASP A 1 252 ? 21.639 27.581 13.463  1.00 31.53 ? 252  ASP A CB  1 
ATOM   1779 C CG  . ASP A 1 252 ? 22.539 28.553 14.191  1.00 32.49 ? 252  ASP A CG  1 
ATOM   1780 O OD1 . ASP A 1 252 ? 23.562 28.111 14.753  1.00 33.91 ? 252  ASP A OD1 1 
ATOM   1781 O OD2 . ASP A 1 252 ? 22.220 29.758 14.210  1.00 34.23 ? 252  ASP A OD2 1 
ATOM   1782 N N   . GLN A 1 253 ? 21.985 24.846 10.984  1.00 27.54 ? 253  GLN A N   1 
ATOM   1783 C CA  . GLN A 1 253 ? 21.147 24.109 10.045  1.00 26.51 ? 253  GLN A CA  1 
ATOM   1784 C C   . GLN A 1 253 ? 20.445 22.938 10.709  1.00 27.05 ? 253  GLN A C   1 
ATOM   1785 O O   . GLN A 1 253 ? 19.439 22.443 10.211  1.00 25.66 ? 253  GLN A O   1 
ATOM   1786 C CB  . GLN A 1 253 ? 21.990 23.599 8.878   1.00 27.76 ? 253  GLN A CB  1 
ATOM   1787 C CG  . GLN A 1 253 ? 22.688 24.711 8.118   1.00 31.63 ? 253  GLN A CG  1 
ATOM   1788 C CD  . GLN A 1 253 ? 21.705 25.617 7.407   1.00 32.74 ? 253  GLN A CD  1 
ATOM   1789 O OE1 . GLN A 1 253 ? 21.828 26.842 7.444   1.00 34.22 ? 253  GLN A OE1 1 
ATOM   1790 N NE2 . GLN A 1 253 ? 20.724 25.015 6.748   1.00 34.39 ? 253  GLN A NE2 1 
ATOM   1791 N N   . TYR A 1 254 ? 20.975 22.490 11.840  1.00 25.53 ? 254  TYR A N   1 
ATOM   1792 C CA  . TYR A 1 254 ? 20.375 21.362 12.534  1.00 25.45 ? 254  TYR A CA  1 
ATOM   1793 C C   . TYR A 1 254 ? 20.245 21.674 14.013  1.00 25.13 ? 254  TYR A C   1 
ATOM   1794 O O   . TYR A 1 254 ? 21.210 22.078 14.656  1.00 23.48 ? 254  TYR A O   1 
ATOM   1795 C CB  . TYR A 1 254 ? 21.235 20.112 12.329  1.00 26.35 ? 254  TYR A CB  1 
ATOM   1796 C CG  . TYR A 1 254 ? 21.503 19.804 10.867  1.00 29.94 ? 254  TYR A CG  1 
ATOM   1797 C CD1 . TYR A 1 254 ? 20.563 19.125 10.091  1.00 31.38 ? 254  TYR A CD1 1 
ATOM   1798 C CD2 . TYR A 1 254 ? 22.682 20.229 10.251  1.00 29.86 ? 254  TYR A CD2 1 
ATOM   1799 C CE1 . TYR A 1 254 ? 20.791 18.878 8.736   1.00 32.61 ? 254  TYR A CE1 1 
ATOM   1800 C CE2 . TYR A 1 254 ? 22.919 19.988 8.902   1.00 31.83 ? 254  TYR A CE2 1 
ATOM   1801 C CZ  . TYR A 1 254 ? 21.970 19.312 8.151   1.00 33.74 ? 254  TYR A CZ  1 
ATOM   1802 O OH  . TYR A 1 254 ? 22.204 19.069 6.817   1.00 36.90 ? 254  TYR A OH  1 
ATOM   1803 N N   . CYS A 1 255 ? 19.043 21.486 14.546  1.00 23.20 ? 255  CYS A N   1 
ATOM   1804 C CA  . CYS A 1 255 ? 18.787 21.747 15.951  1.00 23.50 ? 255  CYS A CA  1 
ATOM   1805 C C   . CYS A 1 255 ? 18.546 20.460 16.726  1.00 21.24 ? 255  CYS A C   1 
ATOM   1806 O O   . CYS A 1 255 ? 17.689 19.660 16.363  1.00 21.51 ? 255  CYS A O   1 
ATOM   1807 C CB  . CYS A 1 255 ? 17.568 22.662 16.114  1.00 24.13 ? 255  CYS A CB  1 
ATOM   1808 S SG  . CYS A 1 255 ? 17.128 23.003 17.851  1.00 29.72 ? 255  CYS A SG  1 
ATOM   1809 N N   . ILE A 1 256 ? 19.321 20.268 17.787  1.00 20.26 ? 256  ILE A N   1 
ATOM   1810 C CA  . ILE A 1 256 ? 19.184 19.108 18.656  1.00 18.19 ? 256  ILE A CA  1 
ATOM   1811 C C   . ILE A 1 256 ? 18.590 19.676 19.942  1.00 19.79 ? 256  ILE A C   1 
ATOM   1812 O O   . ILE A 1 256 ? 19.245 20.460 20.635  1.00 17.52 ? 256  ILE A O   1 
ATOM   1813 C CB  . ILE A 1 256 ? 20.554 18.478 18.965  1.00 17.49 ? 256  ILE A CB  1 
ATOM   1814 C CG1 . ILE A 1 256 ? 21.208 18.003 17.667  1.00 17.77 ? 256  ILE A CG1 1 
ATOM   1815 C CG2 . ILE A 1 256 ? 20.387 17.321 19.945  1.00 17.39 ? 256  ILE A CG2 1 
ATOM   1816 C CD1 . ILE A 1 256 ? 22.672 17.681 17.808  1.00 19.84 ? 256  ILE A CD1 1 
ATOM   1817 N N   . SER A 1 257 ? 17.353 19.295 20.252  1.00 20.25 ? 257  SER A N   1 
ATOM   1818 C CA  . SER A 1 257 ? 16.681 19.806 21.446  1.00 20.79 ? 257  SER A CA  1 
ATOM   1819 C C   . SER A 1 257 ? 16.391 18.735 22.488  1.00 20.96 ? 257  SER A C   1 
ATOM   1820 O O   . SER A 1 257 ? 16.754 17.569 22.320  1.00 21.34 ? 257  SER A O   1 
ATOM   1821 C CB  . SER A 1 257 ? 15.358 20.471 21.056  1.00 21.34 ? 257  SER A CB  1 
ATOM   1822 O OG  . SER A 1 257 ? 14.394 19.492 20.689  1.00 22.80 ? 257  SER A OG  1 
ATOM   1823 N N   . LYS A 1 258 ? 15.726 19.147 23.565  1.00 19.68 ? 258  LYS A N   1 
ATOM   1824 C CA  . LYS A 1 258 ? 15.348 18.237 24.642  1.00 20.02 ? 258  LYS A CA  1 
ATOM   1825 C C   . LYS A 1 258 ? 14.495 17.095 24.097  1.00 20.91 ? 258  LYS A C   1 
ATOM   1826 O O   . LYS A 1 258 ? 14.424 16.026 24.698  1.00 22.30 ? 258  LYS A O   1 
ATOM   1827 C CB  . LYS A 1 258 ? 14.531 18.974 25.709  1.00 20.62 ? 258  LYS A CB  1 
ATOM   1828 C CG  . LYS A 1 258 ? 13.163 19.449 25.202  1.00 21.61 ? 258  LYS A CG  1 
ATOM   1829 C CD  . LYS A 1 258 ? 12.259 19.991 26.317  1.00 21.59 ? 258  LYS A CD  1 
ATOM   1830 C CE  . LYS A 1 258 ? 12.860 21.210 26.995  1.00 21.17 ? 258  LYS A CE  1 
ATOM   1831 N NZ  . LYS A 1 258 ? 13.163 22.301 26.035  1.00 23.49 ? 258  LYS A NZ  1 
ATOM   1832 N N   . PHE A 1 259 ? 13.832 17.320 22.968  1.00 20.33 ? 259  PHE A N   1 
ATOM   1833 C CA  . PHE A 1 259 ? 12.980 16.278 22.402  1.00 20.13 ? 259  PHE A CA  1 
ATOM   1834 C C   . PHE A 1 259 ? 13.782 15.262 21.607  1.00 19.06 ? 259  PHE A C   1 
ATOM   1835 O O   . PHE A 1 259 ? 13.333 14.142 21.379  1.00 19.03 ? 259  PHE A O   1 
ATOM   1836 C CB  . PHE A 1 259 ? 11.882 16.902 21.532  1.00 21.99 ? 259  PHE A CB  1 
ATOM   1837 C CG  . PHE A 1 259 ? 10.906 17.737 22.312  1.00 23.10 ? 259  PHE A CG  1 
ATOM   1838 C CD1 . PHE A 1 259 ? 10.097 17.156 23.283  1.00 24.29 ? 259  PHE A CD1 1 
ATOM   1839 C CD2 . PHE A 1 259 ? 10.827 19.109 22.111  1.00 25.78 ? 259  PHE A CD2 1 
ATOM   1840 C CE1 . PHE A 1 259 ? 9.226  17.930 24.048  1.00 23.61 ? 259  PHE A CE1 1 
ATOM   1841 C CE2 . PHE A 1 259 ? 9.963  19.891 22.867  1.00 25.41 ? 259  PHE A CE2 1 
ATOM   1842 C CZ  . PHE A 1 259 ? 9.161  19.299 23.839  1.00 25.31 ? 259  PHE A CZ  1 
ATOM   1843 N N   . THR A 1 260 ? 14.983 15.648 21.195  1.00 19.69 ? 260  THR A N   1 
ATOM   1844 C CA  . THR A 1 260 ? 15.826 14.735 20.447  1.00 17.09 ? 260  THR A CA  1 
ATOM   1845 C C   . THR A 1 260 ? 16.401 13.693 21.402  1.00 16.60 ? 260  THR A C   1 
ATOM   1846 O O   . THR A 1 260 ? 17.222 14.015 22.260  1.00 17.61 ? 260  THR A O   1 
ATOM   1847 C CB  . THR A 1 260 ? 16.988 15.469 19.776  1.00 18.15 ? 260  THR A CB  1 
ATOM   1848 O OG1 . THR A 1 260 ? 16.503 16.660 19.139  1.00 18.28 ? 260  THR A OG1 1 
ATOM   1849 C CG2 . THR A 1 260 ? 17.638 14.555 18.740  1.00 14.37 ? 260  THR A CG2 1 
ATOM   1850 N N   . ARG A 1 261 ? 15.965 12.447 21.248  1.00 14.12 ? 261  ARG A N   1 
ATOM   1851 C CA  . ARG A 1 261 ? 16.440 11.369 22.102  1.00 15.91 ? 261  ARG A CA  1 
ATOM   1852 C C   . ARG A 1 261 ? 17.307 10.396 21.298  1.00 14.08 ? 261  ARG A C   1 
ATOM   1853 O O   . ARG A 1 261 ? 17.865 9.450  21.844  1.00 12.61 ? 261  ARG A O   1 
ATOM   1854 C CB  . ARG A 1 261 ? 15.244 10.648 22.733  1.00 17.17 ? 261  ARG A CB  1 
ATOM   1855 C CG  . ARG A 1 261 ? 14.303 11.580 23.507  1.00 15.15 ? 261  ARG A CG  1 
ATOM   1856 C CD  . ARG A 1 261 ? 14.988 12.221 24.723  1.00 15.80 ? 261  ARG A CD  1 
ATOM   1857 N NE  . ARG A 1 261 ? 15.055 11.316 25.872  1.00 15.44 ? 261  ARG A NE  1 
ATOM   1858 C CZ  . ARG A 1 261 ? 14.008 11.005 26.637  1.00 16.25 ? 261  ARG A CZ  1 
ATOM   1859 N NH1 . ARG A 1 261 ? 12.815 11.530 26.379  1.00 15.79 ? 261  ARG A NH1 1 
ATOM   1860 N NH2 . ARG A 1 261 ? 14.148 10.156 27.647  1.00 14.65 ? 261  ARG A NH2 1 
ATOM   1861 N N   . ILE A 1 262 ? 17.416 10.654 19.997  1.00 13.63 ? 262  ILE A N   1 
ATOM   1862 C CA  . ILE A 1 262 ? 18.210 9.834  19.092  1.00 15.13 ? 262  ILE A CA  1 
ATOM   1863 C C   . ILE A 1 262 ? 18.993 10.756 18.174  1.00 15.45 ? 262  ILE A C   1 
ATOM   1864 O O   . ILE A 1 262 ? 18.410 11.567 17.450  1.00 15.50 ? 262  ILE A O   1 
ATOM   1865 C CB  . ILE A 1 262 ? 17.313 8.911  18.230  1.00 17.15 ? 262  ILE A CB  1 
ATOM   1866 C CG1 . ILE A 1 262 ? 16.570 7.929  19.138  1.00 17.87 ? 262  ILE A CG1 1 
ATOM   1867 C CG2 . ILE A 1 262 ? 18.158 8.149  17.212  1.00 13.48 ? 262  ILE A CG2 1 
ATOM   1868 C CD1 . ILE A 1 262 ? 15.521 7.130  18.433  1.00 20.24 ? 262  ILE A CD1 1 
ATOM   1869 N N   . VAL A 1 263 ? 20.316 10.646 18.214  1.00 15.37 ? 263  VAL A N   1 
ATOM   1870 C CA  . VAL A 1 263 ? 21.157 11.490 17.382  1.00 15.49 ? 263  VAL A CA  1 
ATOM   1871 C C   . VAL A 1 263 ? 21.932 10.634 16.403  1.00 15.83 ? 263  VAL A C   1 
ATOM   1872 O O   . VAL A 1 263 ? 22.704 9.753  16.789  1.00 16.54 ? 263  VAL A O   1 
ATOM   1873 C CB  . VAL A 1 263 ? 22.138 12.320 18.231  1.00 15.50 ? 263  VAL A CB  1 
ATOM   1874 C CG1 . VAL A 1 263 ? 22.959 13.233 17.334  1.00 16.70 ? 263  VAL A CG1 1 
ATOM   1875 C CG2 . VAL A 1 263 ? 21.365 13.148 19.243  1.00 16.06 ? 263  VAL A CG2 1 
ATOM   1876 N N   . ILE A 1 264 ? 21.714 10.897 15.124  1.00 16.23 ? 264  ILE A N   1 
ATOM   1877 C CA  . ILE A 1 264 ? 22.372 10.136 14.087  1.00 15.06 ? 264  ILE A CA  1 
ATOM   1878 C C   . ILE A 1 264 ? 23.480 10.974 13.461  1.00 15.02 ? 264  ILE A C   1 
ATOM   1879 O O   . ILE A 1 264 ? 23.221 11.893 12.691  1.00 15.65 ? 264  ILE A O   1 
ATOM   1880 C CB  . ILE A 1 264 ? 21.346 9.700  13.018  1.00 15.29 ? 264  ILE A CB  1 
ATOM   1881 C CG1 . ILE A 1 264 ? 20.211 8.929  13.701  1.00 15.63 ? 264  ILE A CG1 1 
ATOM   1882 C CG2 . ILE A 1 264 ? 22.019 8.827  11.961  1.00 13.23 ? 264  ILE A CG2 1 
ATOM   1883 C CD1 . ILE A 1 264 ? 18.936 8.861  12.895  1.00 18.53 ? 264  ILE A CD1 1 
ATOM   1884 N N   . LEU A 1 265 ? 24.715 10.666 13.833  1.00 13.59 ? 265  LEU A N   1 
ATOM   1885 C CA  . LEU A 1 265 ? 25.869 11.367 13.295  1.00 15.29 ? 265  LEU A CA  1 
ATOM   1886 C C   . LEU A 1 265 ? 26.384 10.578 12.103  1.00 14.74 ? 265  LEU A C   1 
ATOM   1887 O O   . LEU A 1 265 ? 26.658 9.381  12.213  1.00 14.35 ? 265  LEU A O   1 
ATOM   1888 C CB  . LEU A 1 265 ? 26.971 11.480 14.348  1.00 15.41 ? 265  LEU A CB  1 
ATOM   1889 C CG  . LEU A 1 265 ? 26.570 12.222 15.623  1.00 14.88 ? 265  LEU A CG  1 
ATOM   1890 C CD1 . LEU A 1 265 ? 26.069 11.233 16.660  1.00 18.61 ? 265  LEU A CD1 1 
ATOM   1891 C CD2 . LEU A 1 265 ? 27.766 12.978 16.161  1.00 17.64 ? 265  LEU A CD2 1 
ATOM   1892 N N   . GLU A 1 266 ? 26.513 11.248 10.964  1.00 14.57 ? 266  GLU A N   1 
ATOM   1893 C CA  . GLU A 1 266 ? 26.995 10.587 9.763   1.00 14.78 ? 266  GLU A CA  1 
ATOM   1894 C C   . GLU A 1 266 ? 28.126 11.388 9.143   1.00 15.34 ? 266  GLU A C   1 
ATOM   1895 O O   . GLU A 1 266 ? 28.084 12.617 9.106   1.00 13.75 ? 266  GLU A O   1