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*** ***elNémo ID: EXAMPLE2Input data for this run:HEADER Maltodextrin bp HEADER Maltodextrin binding protein ATOM 1 N LYS A 1 -12.621 27.691 51.154 1.00 87.40 ATOM 2 CA LYS A 1 -12.341 26.198 51.153 1.00 87.46 ATOM 3 C LYS A 1 -12.865 25.547 49.864 1.00 86.45 ATOM 4 O LYS A 1 -12.310 24.601 49.210 1.00 86.78 ATOM 5 CB LYS A 1 -12.846 25.664 52.487 1.00 87.70 ATOM 6 N ILE A 2 -13.989 26.145 49.466 1.00 85.10 ATOM 7 CA ILE A 2 -14.831 25.957 48.307 1.00 82.24 ATOM 8 C ILE A 2 -15.288 24.505 48.119 1.00 80.03 ATOM 9 O ILE A 2 -16.020 23.932 48.985 1.00 79.86 ATOM 10 CB ILE A 2 -14.071 26.497 47.059 1.00 81.04 ATOM 11 N GLU A 3 -14.808 24.006 46.994 1.00 75.95 ATOM 12 CA GLU A 3 -15.046 22.628 46.522 1.00 72.52 ATOM 13 C GLU A 3 -16.516 22.334 46.292 1.00 69.04 ATOM 14 O GLU A 3 -17.058 22.773 45.193 1.00 69.11 ATOM 15 CB GLU A 3 -14.129 21.719 47.409 1.00 71.61 ATOM 16 N GLU A 4 -17.299 21.618 47.069 1.00 65.36 ATOM 17 CA GLU A 4 -18.714 21.389 46.782 1.00 61.45 ATOM 18 C GLU A 4 -19.341 20.296 47.651 1.00 59.14 ATOM 19 O GLU A 4 -19.659 20.537 48.853 1.00 58.76 ATOM 20 CB GLU A 4 -18.813 20.983 45.297 1.00 63.88 ATOM 21 N GLY A 5 -19.530 19.202 46.959 1.00 55.20 ATOM 22 CA GLY A 5 -19.972 17.870 47.059 1.00 52.46 ATOM 23 C GLY A 5 -19.601 16.960 45.855 1.00 51.64 ATOM 24 O GLY A 5 -20.237 16.004 45.374 1.00 51.78 ATOM 25 N LYS A 6 -18.451 17.258 45.287 1.00 50.87 ATOM 26 CA LYS A 6 -17.744 16.609 44.186 1.00 47.41 ATOM 27 C LYS A 6 -16.265 16.450 44.595 1.00 44.94 ATOM 28 O LYS A 6 -15.984 16.785 45.788 1.00 43.59 ATOM 29 CB LYS A 6 -17.920 17.463 42.947 1.00 49.52 ATOM 30 CG LYS A 6 -16.885 18.598 42.990 1.00 52.46 ATOM 31 CD LYS A 6 -16.480 18.938 41.561 1.00 55.20 ATOM 32 CE LYS A 6 -17.132 20.225 41.086 1.00 56.45 ATOM 33 NZ LYS A 6 -16.020 21.174 40.677 1.00 58.97 ATOM 34 N LEU A 7 -15.433 15.892 43.728 1.00 42.30 ATOM 35 CA LEU A 7 -13.991 15.630 43.823 1.00 39.10 ATOM 36 C LEU A 7 -13.205 16.243 42.650 1.00 36.75 ATOM 37 O LEU A 7 -13.505 16.057 41.481 1.00 36.60 ATOM 38 CB LEU A 7 -13.634 14.136 43.943 1.00 37.45 ATOM 39 CG LEU A 7 -14.166 13.362 45.106 1.00 39.28 ATOM 40 CD1 LEU A 7 -13.737 11.918 45.219 1.00 38.12 ATOM 41 CD2 LEU A 7 -13.664 14.066 46.403 1.00 41.04 ATOM 42 N VAL A 8 -12.187 17.031 42.859 1.00 34.90 ATOM 43 CA VAL A 8 -11.288 17.626 41.815 1.00 31.67 ATOM 44 C VAL A 8 -9.882 17.091 42.169 1.00 31.15 ATOM 45 O VAL A 8 -9.462 17.109 43.371 1.00 28.51 ATOM 46 CB VAL A 8 -11.578 19.114 41.813 1.00 31.66 ATOM 47 CG1 VAL A 8 -10.646 20.020 41.013 1.00 29.62 ATOM 48 CG2 VAL A 8 -13.007 19.352 41.412 1.00 33.16 ATOM 49 N ILE A 9 -9.209 16.495 41.229 1.00 29.62 ATOM 50 CA ILE A 9 -7.899 15.891 41.393 1.00 28.07 ATOM 51 C ILE A 9 -6.925 16.579 40.475 1.00 25.92 ATOM 52 O ILE A 9 -7.226 16.877 39.358 1.00 25.70 ATOM 53 CB ILE A 9 -7.856 14.357 41.062 1.00 29.29 ATOM 54 CG1 ILE A 9 -8.904 13.659 41.998 1.00 31.89 ATOM 55 CG2 ILE A 9 -6.440 13.757 41.181 1.00 25.82 ATOM 56 CD1 ILE A 9 -9.486 12.274 41.659 1.00 29.23 ATOM 57 N TRP A 10 -5.764 16.816 41.028 1.00 24.98 ATOM 58 CA TRP A 10 -4.622 17.406 40.266 1.00 26.18 ATOM 59 C TRP A 10 -3.477 16.376 40.225 1.00 25.37 ATOM 60 O TRP A 10 -3.146 15.838 41.332 1.00 22.91 ATOM 61 CB TRP A 10 -4.127 18.682 40.851 1.00 27.81 ATOM 62 CG TRP A 10 -5.026 19.871 40.629 1.00 31.09 ATOM 63 CD1 TRP A 10 -6.343 20.013 40.219 1.00 29.15 ATOM 64 CD2 TRP A 10 -4.518 21.183 40.962 1.00 30.43 ATOM 65 NE1 TRP A 10 -6.664 21.356 40.229 1.00 32.09 ATOM 66 CE2 TRP A 10 -5.578 22.077 40.648 1.00 32.07 ATOM 67 CE3 TRP A 10 -3.311 21.602 41.524 1.00 30.41 ATOM 68 CZ2 TRP A 10 -5.379 23.434 40.869 1.00 34.46 ATOM 69 CZ3 TRP A 10 -3.101 22.952 41.739 1.00 28.99 ATOM 70 CH2 TRP A 10 -4.088 23.834 41.363 1.00 31.93 ATOM 71 N ILE A 11 -3.012 16.060 39.014 1.00 22.92 ATOM 72 CA ILE A 11 -1.912 15.068 38.860 1.00 20.90 ATOM 73 C ILE A 11 -1.049 15.651 37.758 1.00 21.05 ATOM 74 O ILE A 11 -1.514 16.506 37.026 1.00 23.35 ATOM 75 CB ILE A 11 -2.545 13.679 38.583 1.00 19.59 ATOM 76 CG1 ILE A 11 -1.444 12.650 38.426 1.00 21.24 ATOM 77 CG2 ILE A 11 -3.380 13.755 37.310 1.00 24.06 ATOM 78 CD1 ILE A 11 -1.834 11.172 38.530 1.00 23.01 ATOM 79 N ASN A 12 0.207 15.395 37.691 1.00 22.27 ATOM 80 CA ASN A 12 1.192 15.821 36.714 1.00 21.93 ATOM 81 C ASN A 12 0.771 15.179 35.360 1.00 23.41 ATOM 82 O ASN A 12 0.235 14.074 35.194 1.00 24.07 ATOM 83 CB ASN A 12 2.636 15.476 37.061 1.00 20.71 ATOM 84 CG ASN A 12 3.544 16.517 36.370 1.00 23.03 ATOM 85 OD1 ASN A 12 3.174 17.701 36.311 1.00 26.41 ATOM 86 ND2 ASN A 12 4.723 16.170 35.940 1.00 23.71 ATOM 87 N GLY A 13 1.121 15.974 34.373 1.00 22.90 ATOM 88 CA GLY A 13 0.873 15.748 32.971 1.00 25.54 ATOM 89 C GLY A 13 1.610 14.531 32.429 1.00 25.45 ATOM 90 O GLY A 13 1.055 14.041 31.415 1.00 25.69 ATOM 91 N ASP A 14 2.724 14.120 33.075 1.00 22.83 ATOM 92 CA ASP A 14 3.387 12.920 32.595 1.00 22.35 ATOM 93 C ASP A 14 2.817 11.618 33.199 1.00 22.69 ATOM 94 O ASP A 14 3.325 10.556 32.783 1.00 24.80 ATOM 95 CB ASP A 14 4.919 13.055 32.811 1.00 23.85 ATOM 96 CG ASP A 14 5.269 13.270 34.283 1.00 25.78 ATOM 97 OD1 ASP A 14 4.326 13.325 35.094 1.00 21.27 ATOM 98 OD2 ASP A 14 6.468 13.454 34.625 1.00 27.63 ATOM 99 N LYS A 15 1.748 11.621 33.974 1.00 20.08 ATOM 100 CA LYS A 15 1.187 10.437 34.615 1.00 21.33 ATOM 101 C LYS A 15 -0.058 9.987 33.887 1.00 20.90 ATOM 102 O LYS A 15 -0.584 10.797 33.113 1.00 19.17 ATOM 103 CB LYS A 15 0.916 10.766 36.160 1.00 16.97 ATOM 104 CG LYS A 15 2.112 11.574 36.829 1.00 16.21 ATOM 105 CD LYS A 15 3.294 10.615 36.574 1.00 18.66 ATOM 106 CE LYS A 15 4.338 10.472 37.605 1.00 19.34 ATOM 107 NZ LYS A 15 5.097 11.684 37.729 1.00 23.84 ATOM 108 N GLY A 16 -0.632 8.797 34.189 1.00 22.97 ATOM 109 CA GLY A 16 -1.825 8.421 33.448 1.00 24.44 ATOM 110 C GLY A 16 -3.110 8.966 34.013 1.00 26.25 ATOM 111 O GLY A 16 -3.995 8.283 34.640 1.00 26.82 ATOM 112 N TYR A 17 -3.301 10.272 33.730 1.00 28.41 ATOM 113 CA TYR A 17 -4.499 11.014 34.121 1.00 27.27 ATOM 114 C TYR A 17 -5.729 10.473 33.399 1.00 29.24 ATOM 115 O TYR A 17 -6.861 10.615 33.954 1.00 32.36 ATOM 116 CB TYR A 17 -4.311 12.515 33.900 1.00 28.29 ATOM 117 CG TYR A 17 -3.775 12.958 32.579 1.00 26.73 ATOM 118 CD1 TYR A 17 -4.721 13.135 31.554 1.00 30.37 ATOM 119 CD2 TYR A 17 -2.488 13.347 32.321 1.00 29.24 ATOM 120 CE1 TYR A 17 -4.357 13.643 30.309 1.00 27.34 ATOM 121 CE2 TYR A 17 -2.074 13.825 31.060 1.00 30.71 ATOM 122 CZ TYR A 17 -3.031 13.938 30.057 1.00 30.99 ATOM 123 OH TYR A 17 -2.749 14.415 28.771 1.00 33.39 ATOM 124 N ASN A 18 -5.581 9.852 32.216 1.00 28.96 ATOM 125 CA ASN A 18 -6.817 9.297 31.595 1.00 29.37 ATOM 126 C ASN A 18 -7.081 8.001 32.377 1.00 29.76 ATOM 127 O ASN A 18 -8.272 7.779 32.633 1.00 31.92 ATOM 128 CB ASN A 18 -6.738 9.196 30.080 1.00 29.90 ATOM 129 CG ASN A 18 -6.781 10.499 29.351 1.00 30.67 ATOM 130 OD1 ASN A 18 -6.031 10.844 28.439 1.00 33.03 ATOM 131 ND2 ASN A 18 -7.597 11.464 29.807 1.00 35.38 ATOM 132 N GLY A 19 -6.146 7.157 32.816 1.00 27.54 ATOM 133 CA GLY A 19 -6.523 6.007 33.584 1.00 26.01 ATOM 134 C GLY A 19 -7.258 6.452 34.844 1.00 25.64 ATOM 135 O GLY A 19 -8.164 5.768 35.373 1.00 25.49 ATOM 136 N LEU A 20 -6.754 7.525 35.399 1.00 25.51 ATOM 137 CA LEU A 20 -7.281 8.121 36.667 1.00 27.47 ATOM 138 C LEU A 20 -8.708 8.566 36.419 1.00 28.32 ATOM 139 O LEU A 20 -9.512 8.237 37.285 1.00 30.79 ATOM 140 CB LEU A 20 -6.335 9.204 37.314 1.00 25.82 ATOM 141 CG LEU A 20 -6.772 9.764 38.717 1.00 27.48 ATOM 142 CD1 LEU A 20 -6.867 8.694 39.754 1.00 24.39 ATOM 143 CD2 LEU A 20 -5.797 10.844 39.144 1.00 26.48 ATOM 144 N ALA A 21 -8.985 9.269 35.378 1.00 31.50 ATOM 145 CA ALA A 21 -10.320 9.674 34.936 1.00 33.85 ATOM 146 C ALA A 21 -11.226 8.452 34.762 1.00 37.10 ATOM 147 O ALA A 21 -12.414 8.612 35.224 1.00 38.89 ATOM 148 CB ALA A 21 -10.253 10.485 33.655 1.00 34.38 ATOM 149 N GLU A 22 -10.835 7.290 34.265 1.00 37.84 ATOM 150 CA GLU A 22 -11.620 6.057 34.117 1.00 38.63 ATOM 151 C GLU A 22 -11.995 5.543 35.496 1.00 39.37 ATOM 152 O GLU A 22 -13.028 4.851 35.781 1.00 38.99 ATOM 153 CB GLU A 22 -10.933 4.924 33.358 1.00 44.36 ATOM 154 CG GLU A 22 -10.322 5.082 31.972 1.00 52.64 ATOM 155 CD GLU A 22 -9.165 4.213 31.486 1.00 57.81 ATOM 156 OE1 GLU A 22 -9.075 3.012 31.846 1.00 61.61 ATOM 157 OE2 GLU A 22 -8.277 4.705 30.656 1.00 56.89 ATOM 158 N VAL A 23 -11.077 5.791 36.448 1.00 37.01 ATOM 159 CA VAL A 23 -11.375 5.411 37.822 1.00 37.32 ATOM 160 C VAL A 23 -12.341 6.425 38.421 1.00 38.16 ATOM 161 O VAL A 23 -13.289 6.027 39.139 1.00 40.42 ATOM 162 CB VAL A 23 -10.088 5.170 38.645 1.00 36.43 ATOM 163 CG1 VAL A 23 -10.510 4.728 40.081 1.00 34.87 ATOM 164 CG2 VAL A 23 -9.195 4.304 37.828 1.00 31.98 ATOM 165 N GLY A 24 -12.275 7.706 38.171 1.00 38.13 ATOM 166 CA GLY A 24 -13.301 8.585 38.731 1.00 39.86 ATOM 167 C GLY A 24 -14.716 8.186 38.304 1.00 41.89 ATOM 168 O GLY A 24 -15.716 8.293 39.023 1.00 41.79 ATOM 169 N LYS A 25 -14.778 7.749 37.062 1.00 44.67 ATOM 170 CA LYS A 25 -15.980 7.351 36.343 1.00 46.41 ATOM 171 C LYS A 25 -16.765 6.249 37.009 1.00 45.92 ATOM 172 O LYS A 25 -17.992 6.367 36.983 1.00 46.99 ATOM 173 CB LYS A 25 -15.739 6.897 34.879 1.00 47.96 ATOM 174 CG LYS A 25 -15.733 8.202 34.069 1.00 50.20 ATOM 175 CD LYS A 25 -15.846 7.994 32.583 1.00 55.40 ATOM 176 CE LYS A 25 -16.630 6.820 32.052 1.00 57.98 ATOM 177 NZ LYS A 25 -16.646 6.784 30.534 1.00 58.56 ATOM 178 N LYS A 26 -16.096 5.278 37.536 1.00 45.84 ATOM 179 CA LYS A 26 -16.853 4.214 38.198 1.00 47.97 ATOM 180 C LYS A 26 -16.894 4.634 39.649 1.00 50.69 ATOM 181 O LYS A 26 -17.203 3.780 40.539 1.00 54.70 ATOM 182 CB LYS A 26 -16.322 2.822 37.883 1.00 46.57 ATOM 183 CG LYS A 26 -15.234 2.281 38.738 1.00 47.35 ATOM 184 CD LYS A 26 -15.127 0.818 38.861 1.00 51.79 ATOM 185 CE LYS A 26 -16.078 0.118 39.827 1.00 54.95 ATOM 186 NZ LYS A 26 -17.525 0.505 39.603 1.00 58.04 ATOM 187 N PHE A 27 -16.518 5.884 39.968 1.00 49.17 ATOM 188 CA PHE A 27 -16.617 6.193 41.436 1.00 47.47 ATOM 189 C PHE A 27 -18.061 6.734 41.520 1.00 49.79 ATOM 190 O PHE A 27 -18.953 6.417 42.314 1.00 48.83 ATOM 191 CB PHE A 27 -15.540 7.136 41.940 1.00 42.14 ATOM 192 CG PHE A 27 -15.792 7.593 43.366 1.00 37.02 ATOM 193 CD1 PHE A 27 -15.649 6.690 44.410 1.00 36.81 ATOM 194 CD2 PHE A 27 -16.157 8.897 43.633 1.00 35.18 ATOM 195 CE1 PHE A 27 -15.929 7.034 45.743 1.00 36.23 ATOM 196 CE2 PHE A 27 -16.366 9.281 44.953 1.00 32.89 ATOM 197 CZ PHE A 27 -16.274 8.381 45.982 1.00 31.41 ATOM 198 N GLU A 28 -18.199 7.594 40.510 1.00 51.63 ATOM 199 CA GLU A 28 -19.358 8.408 40.199 1.00 55.22 ATOM 200 C GLU A 28 -20.653 7.741 39.722 1.00 56.05 ATOM 201 O GLU A 28 -21.822 8.128 39.972 1.00 54.35 ATOM 202 CB GLU A 28 -18.945 9.386 39.104 1.00 54.62 ATOM 203 CG GLU A 28 -20.074 9.733 38.122 1.00 59.09 ATOM 204 CD GLU A 28 -19.576 10.855 37.273 1.00 62.34 ATOM 205 OE1 GLU A 28 -18.358 11.034 37.600 1.00 68.34 ATOM 206 OE2 GLU A 28 -20.132 11.497 36.445 1.00 65.27 ATOM 207 N LYS A 29 -20.411 6.693 38.990 1.00 57.70 ATOM 208 CA LYS A 29 -21.423 5.799 38.394 1.00 59.47 ATOM 209 C LYS A 29 -21.898 4.951 39.573 1.00 59.49 ATOM 210 O LYS A 29 -23.021 4.392 39.530 1.00 61.64 ATOM 211 CB LYS A 29 -20.793 5.003 37.267 1.00 59.69 ATOM 212 CG LYS A 29 -21.508 4.249 36.202 1.00 60.83 ATOM 213 CD LYS A 29 -20.691 3.104 35.571 1.00 62.02 ATOM 214 CE LYS A 29 -21.596 2.158 34.772 1.00 62.52 ATOM 215 NZ LYS A 29 -20.805 1.224 33.938 1.00 62.32 ATOM 216 N ASP A 30 -21.071 4.947 40.613 1.00 58.71 ATOM 217 CA ASP A 30 -21.409 4.047 41.801 1.00 58.37 ATOM 218 C ASP A 30 -21.657 4.907 43.016 1.00 57.60 ATOM 219 O ASP A 30 -21.922 4.458 44.175 1.00 58.59 ATOM 220 CB ASP A 30 -20.373 2.947 41.776 1.00 59.61 ATOM 221 CG ASP A 30 -19.648 2.188 42.790 1.00 59.90 ATOM 222 OD1 ASP A 30 -19.749 2.631 43.971 1.00 63.11 ATOM 223 OD2 ASP A 30 -18.905 1.165 42.629 1.00 59.45 ATOM 224 N THR A 31 -21.696 6.212 42.735 1.00 54.82 ATOM 225 CA THR A 31 -21.886 7.060 43.910 1.00 53.63 ATOM 226 C THR A 31 -22.646 8.330 43.732 1.00 53.55 ATOM 227 O THR A 31 -23.122 8.854 44.778 1.00 56.25 ATOM 228 CB THR A 31 -20.358 7.462 44.317 1.00 51.55 ATOM 229 OG1 THR A 31 -20.272 7.452 45.740 1.00 49.91 ATOM 230 CG2 THR A 31 -20.003 8.781 43.626 1.00 47.77 ATOM 231 N GLY A 32 -22.666 8.868 42.542 1.00 51.51 ATOM 232 CA GLY A 32 -23.250 10.163 42.263 1.00 51.98 ATOM 233 C GLY A 32 -22.287 11.347 42.432 1.00 52.91 ATOM 234 O GLY A 32 -22.644 12.559 42.128 1.00 54.34 ATOM 235 N ILE A 33 -21.061 11.065 42.966 1.00 50.58 ATOM 236 CA ILE A 33 -20.121 12.160 43.122 1.00 48.58 ATOM 237 C ILE A 33 -19.304 12.135 41.824 1.00 46.88 ATOM 238 O ILE A 33 -18.671 11.081 41.699 1.00 48.28 ATOM 239 CB ILE A 33 -19.039 12.115 44.221 1.00 50.17 ATOM 240 CG1 ILE A 33 -19.630 12.085 45.653 1.00 50.93 ATOM 241 CG2 ILE A 33 -18.071 13.314 44.021 1.00 51.02 ATOM 242 CD1 ILE A 33 -20.086 10.599 45.995 1.00 51.53 ATOM 243 N LYS A 34 -19.361 13.185 41.080 1.00 45.92 ATOM 244 CA LYS A 34 -18.547 13.180 39.865 1.00 45.89 ATOM 245 C LYS A 34 -17.117 13.674 40.216 1.00 44.95 ATOM 246 O LYS A 34 -16.806 14.678 40.920 1.00 41.15 ATOM 247 CB LYS A 34 -19.117 14.059 38.767 1.00 49.13 ATOM 248 CG LYS A 34 -18.367 15.403 38.760 1.00 56.49 ATOM 249 CD LYS A 34 -19.062 16.564 38.093 1.00 61.90 ATOM 250 CE LYS A 34 -20.029 17.360 38.985 1.00 65.71 ATOM 251 NZ LYS A 34 -21.411 16.740 39.074 1.00 66.82 ATOM 252 N VAL A 35 -16.205 12.938 39.551 1.00 43.61 ATOM 253 CA VAL A 35 -14.776 13.307 39.734 1.00 42.37 ATOM 254 C VAL A 35 -14.243 14.043 38.531 1.00 42.66 ATOM 255 O VAL A 35 -14.602 13.449 37.468 1.00 47.18 ATOM 256 CB VAL A 35 -14.016 12.007 40.007 1.00 40.92 ATOM 257 CG1 VAL A 35 -12.548 12.383 40.292 1.00 40.88 ATOM 258 CG2 VAL A 35 -14.746 11.250 41.091 1.00 37.39 ATOM 259 N THR A 36 -13.519 15.116 38.629 1.00 39.49 ATOM 260 CA THR A 36 -12.892 15.922 37.634 1.00 38.66 ATOM 261 C THR A 36 -11.333 15.794 37.753 1.00 39.37 ATOM 262 O THR A 36 -10.790 16.204 38.801 1.00 39.74 ATOM 263 CB THR A 36 -13.203 17.469 37.696 1.00 39.53 ATOM 264 OG1 THR A 36 -14.639 17.672 37.533 1.00 41.87 ATOM 265 CG2 THR A 36 -12.385 18.279 36.675 1.00 38.81 ATOM 266 N VAL A 37 -10.588 15.348 36.773 1.00 38.11 ATOM 267 CA VAL A 37 -9.151 15.159 36.795 1.00 37.21 ATOM 268 C VAL A 37 -8.405 16.224 36.071 1.00 37.58 ATOM 269 O VAL A 37 -8.695 16.308 34.862 1.00 40.64 ATOM 270 CB VAL A 37 -8.803 13.772 36.187 1.00 36.33 ATOM 271 CG1 VAL A 37 -7.342 13.628 35.835 1.00 34.76 ATOM 272 CG2 VAL A 37 -9.260 12.703 37.160 1.00 35.47 ATOM 273 N GLU A 38 -7.536 17.008 36.705 1.00 37.81 ATOM 274 CA GLU A 38 -6.822 18.046 35.929 1.00 37.54 ATOM 275 C GLU A 38 -5.322 17.851 36.109 1.00 36.54 ATOM 276 O GLU A 38 -5.004 17.236 37.161 1.00 35.30 ATOM 277 CB GLU A 38 -7.100 19.475 36.410 1.00 42.10 ATOM 278 CG GLU A 38 -8.606 19.621 36.652 1.00 48.97 ATOM 279 CD GLU A 38 -9.090 21.021 36.748 1.00 54.04 ATOM 280 OE1 GLU A 38 -8.351 21.948 37.040 1.00 58.98 ATOM 281 OE2 GLU A 38 -10.310 21.134 36.486 1.00 57.77 ATOM 282 N HIS A 39 -4.620 18.377 35.132 1.00 32.21 ATOM 283 CA HIS A 39 -3.146 18.326 35.153 1.00 31.14 ATOM 284 C HIS A 39 -2.525 19.664 34.788 1.00 31.86 ATOM 285 O HIS A 39 -1.823 19.795 33.737 1.00 31.29 ATOM 286 CB HIS A 39 -2.518 17.196 34.289 1.00 30.01 ATOM 287 CG HIS A 39 -3.069 17.208 32.920 1.00 31.38 ATOM 288 ND1 HIS A 39 -2.422 17.787 31.844 1.00 32.40 ATOM 289 CD2 HIS A 39 -4.303 16.792 32.483 1.00 32.92 ATOM 290 CE1 HIS A 39 -3.228 17.663 30.781 1.00 33.89 ATOM 291 NE2 HIS A 39 -4.353 17.064 31.106 1.00 31.74 ATOM 292 N PRO A 40 -2.695 20.635 35.698 1.00 32.50 ATOM 293 CA PRO A 40 -2.128 21.967 35.495 1.00 32.60 ATOM 294 C PRO A 40 -0.641 21.868 35.449 1.00 33.22 ATOM 295 O PRO A 40 -0.036 21.008 36.085 1.00 32.04 ATOM 296 CB PRO A 40 -2.633 22.838 36.644 1.00 33.52 ATOM 297 CG PRO A 40 -3.333 21.912 37.615 1.00 32.90 ATOM 298 CD PRO A 40 -3.486 20.572 36.954 1.00 33.56 ATOM 299 N ASP A 41 -0.059 22.802 34.710 1.00 36.01 ATOM 300 CA ASP A 41 1.436 22.944 34.589 1.00 38.31 ATOM 301 C ASP A 41 2.053 23.408 35.910 1.00 35.17 ATOM 302 O ASP A 41 1.324 24.217 36.593 1.00 35.53 ATOM 303 CB ASP A 41 1.641 23.960 33.450 1.00 47.84 ATOM 304 CG ASP A 41 1.500 23.440 32.047 1.00 54.62 ATOM 305 OD1 ASP A 41 0.434 23.106 31.476 1.00 59.16 ATOM 306 OD2 ASP A 41 2.641 23.384 31.484 1.00 58.65 ATOM 307 N LYS A 42 3.232 23.082 36.370 1.00 33.34 ATOM 308 CA LYS A 42 3.651 23.612 37.691 1.00 32.73 ATOM 309 C LYS A 42 2.669 23.350 38.796 1.00 32.19 ATOM 310 O LYS A 42 2.411 24.250 39.676 1.00 32.46 ATOM 311 CB LYS A 42 3.597 25.175 37.666 1.00 33.24 ATOM 312 CG LYS A 42 5.012 25.630 37.477 1.00 36.74 ATOM 313 CD LYS A 42 5.446 25.265 36.082 1.00 39.35 ATOM 314 CE LYS A 42 6.976 25.289 36.013 1.00 43.17 ATOM 315 NZ LYS A 42 7.392 25.944 34.660 1.00 49.31 ATOM 316 N LEU A 43 1.997 22.222 38.782 1.00 31.74 ATOM 317 CA LEU A 43 0.944 22.136 39.861 1.00 31.34 ATOM 318 C LEU A 43 1.543 22.124 41.272 1.00 31.59 ATOM 319 O LEU A 43 0.815 22.450 42.205 1.00 31.22 ATOM 320 CB LEU A 43 0.128 20.886 39.547 1.00 31.10 ATOM 321 CG LEU A 43 0.703 19.526 39.869 1.00 27.90 ATOM 322 CD1 LEU A 43 0.281 19.177 41.272 1.00 29.18 ATOM 323 CD2 LEU A 43 0.048 18.543 38.915 1.00 29.24 ATOM 324 N GLU A 44 2.776 21.635 41.296 1.00 32.19 ATOM 325 CA GLU A 44 3.448 21.420 42.587 1.00 33.24 ATOM 326 C GLU A 44 3.793 22.736 43.264 1.00 34.27 ATOM 327 O GLU A 44 4.055 22.890 44.405 1.00 30.98 ATOM 328 CB GLU A 44 4.752 20.666 42.401 1.00 33.70 ATOM 329 CG GLU A 44 5.962 21.332 41.808 1.00 33.18 ATOM 330 CD GLU A 44 6.067 21.554 40.329 1.00 35.04 ATOM 331 OE1 GLU A 44 4.969 21.525 39.685 1.00 34.36 ATOM 332 OE2 GLU A 44 7.190 21.792 39.879 1.00 37.69 ATOM 333 N GLU A 45 3.796 23.692 42.374 1.00 35.93 ATOM 334 CA GLU A 45 4.027 25.119 42.646 1.00 36.94 ATOM 335 C GLU A 45 2.709 25.833 42.796 1.00 36.65 ATOM 336 O GLU A 45 2.489 26.624 43.737 1.00 36.65 ATOM 337 CB GLU A 45 4.782 25.472 41.402 1.00 41.66 ATOM 338 CG GLU A 45 4.826 26.869 40.956 1.00 46.66 ATOM 339 CD GLU A 45 6.322 27.206 40.772 1.00 51.81 ATOM 340 OE1 GLU A 45 7.034 26.156 40.908 1.00 50.62 ATOM 341 OE2 GLU A 45 6.426 28.432 40.554 1.00 54.95 ATOM 342 N LYS A 46 1.758 25.547 41.913 1.00 36.02 ATOM 343 CA LYS A 46 0.466 26.160 41.953 1.00 35.83 ATOM 344 C LYS A 46 -0.230 25.690 43.197 1.00 36.24 ATOM 345 O LYS A 46 -0.981 26.527 43.707 1.00 38.78 ATOM 346 CB LYS A 46 -0.459 25.800 40.789 1.00 41.42 ATOM 347 CG LYS A 46 -0.207 26.535 39.472 1.00 48.85 ATOM 348 CD LYS A 46 1.097 27.346 39.521 1.00 55.09 ATOM 349 CE LYS A 46 1.573 28.134 38.286 1.00 56.83 ATOM 350 NZ LYS A 46 2.666 29.121 38.737 1.00 56.90 ATOM 351 N PHE A 47 -0.127 24.451 43.673 1.00 34.63 ATOM 352 CA PHE A 47 -0.920 24.037 44.822 1.00 32.93 ATOM 353 C PHE A 47 -0.864 24.921 46.075 1.00 35.37 ATOM 354 O PHE A 47 -1.919 25.259 46.679 1.00 33.33 ATOM 355 CB PHE A 47 -0.636 22.545 45.199 1.00 30.79 ATOM 356 CG PHE A 47 -1.468 22.035 46.357 1.00 26.75 ATOM 357 CD1 PHE A 47 -2.843 21.842 46.245 1.00 27.45 ATOM 358 CD2 PHE A 47 -0.892 21.852 47.596 1.00 26.34 ATOM 359 CE1 PHE A 47 -3.539 21.447 47.382 1.00 28.71 ATOM 360 CE2 PHE A 47 -1.587 21.417 48.716 1.00 26.08 ATOM 361 CZ PHE A 47 -2.950 21.244 48.641 1.00 26.87 ATOM 362 N PRO A 48 0.366 25.197 46.525 1.00 37.90 ATOM 363 CA PRO A 48 0.557 25.929 47.799 1.00 39.27 ATOM 364 C PRO A 48 -0.070 27.308 47.664 1.00 41.00 ATOM 365 O PRO A 48 -0.597 27.836 48.650 1.00 39.75 ATOM 366 CB PRO A 48 2.056 25.901 48.093 1.00 38.29 ATOM 367 CG PRO A 48 2.745 25.218 46.947 1.00 37.27 ATOM 368 CD PRO A 48 1.675 24.829 45.930 1.00 37.84 ATOM 369 N GLN A 49 0.040 27.797 46.397 1.00 42.28 ATOM 370 CA GLN A 49 -0.524 29.123 46.160 1.00 44.96 ATOM 371 C GLN A 49 -2.040 29.116 46.316 1.00 45.74 ATOM 372 O GLN A 49 -2.540 29.957 47.116 1.00 48.98 ATOM 373 CB GLN A 49 -0.176 29.734 44.839 1.00 48.52 ATOM 374 CG GLN A 49 1.298 29.811 44.468 1.00 55.95 ATOM 375 CD GLN A 49 1.394 30.293 43.003 1.00 61.29 ATOM 376 OE1 GLN A 49 2.474 30.719 42.552 1.00 65.13 ATOM 377 NE2 GLN A 49 0.248 30.249 42.275 1.00 61.81 ATOM 378 N VAL A 50 -2.797 28.357 45.579 1.00 45.27 ATOM 379 CA VAL A 50 -4.250 28.352 45.668 1.00 43.59 ATOM 380 C VAL A 50 -4.740 27.665 46.926 1.00 43.02 ATOM 381 O VAL A 50 -5.836 28.142 47.309 1.00 43.66 ATOM 382 CB VAL A 50 -4.903 27.652 44.448 1.00 44.15 ATOM 383 CG1 VAL A 50 -4.205 27.955 43.145 1.00 44.46 ATOM 384 CG2 VAL A 50 -4.979 26.143 44.744 1.00 46.50 ATOM 385 N ALA A 51 -4.031 26.669 47.469 1.00 41.85 ATOM 386 CA ALA A 51 -4.557 25.966 48.663 1.00 41.49 ATOM 387 C ALA A 51 -4.499 26.832 49.931 1.00 43.35 ATOM 388 O ALA A 51 -5.193 26.649 50.964 1.00 41.26 ATOM 389 CB ALA A 51 -3.825 24.629 48.879 1.00 39.05 ATOM 390 N ALA A 52 -3.510 27.721 49.817 1.00 44.99 ATOM 391 CA ALA A 52 -3.177 28.647 50.913 1.00 48.40 ATOM 392 C ALA A 52 -4.415 29.494 51.168 1.00 51.82 ATOM 393 O ALA A 52 -4.794 29.746 52.330 1.00 54.18 ATOM 394 CB ALA A 52 -1.914 29.364 50.473 1.00 48.76 ATOM 395 N THR A 53 -5.111 29.848 50.063 1.00 53.18 ATOM 396 CA THR A 53 -6.349 30.628 50.036 1.00 51.99 ATOM 397 C THR A 53 -7.531 29.712 50.391 1.00 51.61 ATOM 398 O THR A 53 -8.669 30.191 50.286 1.00 53.19 ATOM 399 CB THR A 53 -6.767 31.313 48.685 1.00 48.21 ATOM 400 OG1 THR A 53 -7.591 30.242 48.096 1.00 48.17 ATOM 401 CG2 THR A 53 -5.718 31.667 47.652 1.00 50.73 ATOM 402 N GLY A 54 -7.262 28.490 50.767 1.00 51.76 ATOM 403 CA GLY A 54 -8.430 27.652 51.115 1.00 52.79 ATOM 404 C GLY A 54 -9.058 27.081 49.864 1.00 54.12 ATOM 405 O GLY A 54 -10.132 26.463 50.058 1.00 54.17 ATOM 406 N ASP A 55 -8.423 27.250 48.662 1.00 53.96 ATOM 407 CA ASP A 55 -9.126 26.518 47.503 1.00 52.44 ATOM 408 C ASP A 55 -8.201 25.438 46.912 1.00 50.08 ATOM 409 O ASP A 55 -7.499 24.726 47.732 1.00 49.50 ATOM 410 CB ASP A 55 -9.852 27.522 46.690 1.00 56.84 ATOM 411 CG ASP A 55 -9.174 28.495 45.803 1.00 59.58 ATOM 412 OD1 ASP A 55 -8.186 28.203 45.105 1.00 63.13 ATOM 413 OD2 ASP A 55 -9.687 29.644 45.769 1.00 62.01 ATOM 414 N GLY A 56 -8.221 25.180 45.595 1.00 46.98 ATOM 415 CA GLY A 56 -7.368 24.152 44.925 1.00 42.30 ATOM 416 C GLY A 56 -8.096 22.848 44.742 1.00 38.39 ATOM 417 O GLY A 56 -9.339 22.935 44.812 1.00 39.81 ATOM 418 N PRO A 57 -7.415 21.707 44.517 1.00 35.33 ATOM 419 CA PRO A 57 -8.074 20.424 44.333 1.00 32.90 ATOM 420 C PRO A 57 -8.468 19.832 45.643 1.00 31.43 ATOM 421 O PRO A 57 -7.997 20.229 46.732 1.00 32.83 ATOM 422 CB PRO A 57 -6.988 19.527 43.613 1.00 31.23 ATOM 423 CG PRO A 57 -5.701 20.038 44.158 1.00 29.61 ATOM 424 CD PRO A 57 -5.945 21.517 44.373 1.00 33.32 ATOM 425 N ASP A 58 -9.340 18.884 45.696 1.00 30.53 ATOM 426 CA ASP A 58 -9.684 18.125 46.900 1.00 31.94 ATOM 427 C ASP A 58 -8.448 17.222 47.212 1.00 30.94 ATOM 428 O ASP A 58 -8.072 16.970 48.366 1.00 28.83 ATOM 429 CB ASP A 58 -10.971 17.287 46.759 1.00 35.52 ATOM 430 CG ASP A 58 -12.234 18.155 46.643 1.00 36.53 ATOM 431 OD1 ASP A 58 -12.636 18.580 45.549 1.00 38.16 ATOM 432 OD2 ASP A 58 -12.712 18.421 47.788 1.00 40.41 ATOM 433 N ILE A 59 -7.895 16.663 46.090 1.00 30.61 ATOM 434 CA ILE A 59 -6.739 15.737 46.132 1.00 29.60 ATOM 435 C ILE A 59 -5.663 16.128 45.108 1.00 27.63 ATOM 436 O ILE A 59 -5.849 16.574 43.998 1.00 27.14 ATOM 437 CB ILE A 59 -7.159 14.233 46.233 1.00 30.99 ATOM 438 CG1 ILE A 59 -6.049 13.418 45.499 1.00 27.52 ATOM 439 CG2 ILE A 59 -8.547 13.567 45.913 1.00 30.80 ATOM 440 CD1 ILE A 59 -6.401 11.914 45.668 1.00 32.51 ATOM 441 N ILE A 60 -4.409 16.076 45.613 1.00 26.46 ATOM 442 CA ILE A 60 -3.167 16.380 44.990 1.00 24.02 ATOM 443 C ILE A 60 -2.205 15.196 45.019 1.00 22.46 ATOM 444 O ILE A 60 -1.895 14.549 45.997 1.00 21.01 ATOM 445 CB ILE A 60 -2.509 17.640 45.680 1.00 27.12 ATOM 446 CG1 ILE A 60 -1.269 18.093 44.857 1.00 27.26 ATOM 447 CG2 ILE A 60 -2.139 17.412 47.152 1.00 24.57 ATOM 448 CD1 ILE A 60 -1.800 18.935 43.613 1.00 32.92 ATOM 449 N PHE A 61 -1.676 14.951 43.817 1.00 21.00 ATOM 450 CA PHE A 61 -0.695 13.891 43.581 1.00 22.36 ATOM 451 C PHE A 61 0.680 14.554 43.161 1.00 21.10 ATOM 452 O PHE A 61 0.655 15.414 42.242 1.00 21.30 ATOM 453 CB PHE A 61 -1.009 12.930 42.438 1.00 20.87 ATOM 454 CG PHE A 61 -2.182 12.051 42.634 1.00 19.64 ATOM 455 CD1 PHE A 61 -3.472 12.472 42.634 1.00 18.74 ATOM 456 CD2 PHE A 61 -1.883 10.653 42.762 1.00 25.39 ATOM 457 CE1 PHE A 61 -4.523 11.573 42.824 1.00 21.61 ATOM 458 CE2 PHE A 61 -2.985 9.743 42.957 1.00 26.29 ATOM 459 CZ PHE A 61 -4.304 10.189 42.993 1.00 21.81 ATOM 460 N TRP A 62 1.697 14.114 43.902 1.00 18.91 ATOM 461 CA TRP A 62 3.065 14.518 43.584 1.00 16.85 ATOM 462 C TRP A 62 3.960 13.459 44.244 1.00 18.31 ATOM 463 O TRP A 62 3.397 12.618 45.002 1.00 18.36 ATOM 464 CB TRP A 62 3.347 16.007 43.934 1.00 17.63 ATOM 465 CG TRP A 62 4.719 16.469 43.306 1.00 17.52 ATOM 466 CD1 TRP A 62 5.937 16.436 43.813 1.00 15.19 ATOM 467 CD2 TRP A 62 4.888 16.968 41.952 1.00 16.34 ATOM 468 NE1 TRP A 62 6.865 16.898 42.917 1.00 17.65 ATOM 469 CE2 TRP A 62 6.236 17.202 41.761 1.00 18.48 ATOM 470 CE3 TRP A 62 3.946 17.170 40.925 1.00 20.09 ATOM 471 CZ2 TRP A 62 6.790 17.735 40.576 1.00 18.35 ATOM 472 CZ3 TRP A 62 4.463 17.729 39.753 1.00 19.41 ATOM 473 CH2 TRP A 62 5.852 17.938 39.606 1.00 20.02 ATOM 474 N ALA A 63 5.291 13.431 43.885 1.00 16.89 ATOM 475 CA ALA A 63 6.322 12.663 44.574 1.00 14.19 ATOM 476 C ALA A 63 6.303 13.135 46.061 1.00 15.79 ATOM 477 O ALA A 63 5.928 14.359 46.283 1.00 14.46 ATOM 478 CB ALA A 63 7.692 12.709 43.993 1.00 15.58 ATOM 479 N HIS A 64 6.698 12.342 47.008 1.00 15.17 ATOM 480 CA HIS A 64 6.574 12.744 48.441 1.00 16.39 ATOM 481 C HIS A 64 7.488 13.836 48.860 1.00 18.44 ATOM 482 O HIS A 64 7.202 14.477 49.952 1.00 17.46 ATOM 483 CB HIS A 64 6.767 11.437 49.343 1.00 13.90 ATOM 484 CG HIS A 64 8.221 11.007 49.194 1.00 16.61 ATOM 485 ND1 HIS A 64 9.264 11.216 50.076 1.00 17.21 ATOM 486 CD2 HIS A 64 8.795 10.378 48.140 1.00 12.50 ATOM 487 CE1 HIS A 64 10.399 10.741 49.657 1.00 14.10 ATOM 488 NE2 HIS A 64 10.077 10.260 48.424 1.00 17.83 ATOM 489 N ASP A 65 8.622 14.139 48.128 1.00 17.03 ATOM 490 CA ASP A 65 9.569 15.208 48.572 1.00 16.25 ATOM 491 C ASP A 65 8.892 16.576 48.792 1.00 18.46 ATOM 492 O ASP A 65 9.390 17.402 49.581 1.00 17.41 ATOM 493 CB ASP A 65 10.795 15.320 47.622 1.00 16.52 ATOM 494 CG ASP A 65 10.426 15.767 46.252 1.00 14.74 ATOM 495 OD1 ASP A 65 9.470 15.193 45.559 1.00 14.91 ATOM 496 OD2 ASP A 65 10.911 16.789 45.762 1.00 17.68 ATOM 497 N ARG A 66 7.788 16.876 48.117 1.00 18.75 ATOM 498 CA ARG A 66 7.104 18.181 48.226 1.00 17.77 ATOM 499 C ARG A 66 6.153 18.168 49.444 1.00 18.83 ATOM 500 O ARG A 66 5.840 19.328 49.880 1.00 18.58 ATOM 501 CB ARG A 66 6.281 18.501 47.015 1.00 18.07 ATOM 502 CG ARG A 66 7.025 18.710 45.705 1.00 18.34 ATOM 503 CD ARG A 66 7.571 20.107 45.776 1.00 25.02 ATOM 504 NE ARG A 66 8.625 20.265 44.789 1.00 28.36 ATOM 505 CZ ARG A 66 9.183 21.434 44.466 1.00 30.88 ATOM 506 NH1 ARG A 66 8.715 22.643 44.971 1.00 30.46 ATOM 507 NH2 ARG A 66 10.222 21.471 43.589 1.00 29.38 ATOM 508 N PHE A 67 5.746 17.028 49.959 1.00 19.04 ATOM 509 CA PHE A 67 4.720 16.943 51.044 1.00 20.67 ATOM 510 C PHE A 67 5.144 17.518 52.410 1.00 21.00 ATOM 511 O PHE A 67 4.171 18.084 53.030 1.00 22.00 ATOM 512 CB PHE A 67 4.141 15.523 51.113 1.00 18.36 ATOM 513 CG PHE A 67 3.156 15.301 49.944 1.00 25.38 ATOM 514 CD1 PHE A 67 3.558 15.486 48.644 1.00 28.86 ATOM 515 CD2 PHE A 67 1.858 14.925 50.140 1.00 30.02 ATOM 516 CE1 PHE A 67 2.715 15.238 47.550 1.00 31.55 ATOM 517 CE2 PHE A 67 0.926 14.766 49.113 1.00 33.42 ATOM 518 CZ PHE A 67 1.361 14.935 47.788 1.00 32.81 ATOM 519 N GLY A 68 6.324 17.425 52.920 1.00 20.33 ATOM 520 CA GLY A 68 6.770 18.004 54.198 1.00 21.17 ATOM 521 C GLY A 68 6.485 19.494 54.187 1.00 22.44 ATOM 522 O GLY A 68 6.000 20.150 55.116 1.00 22.77 ATOM 523 N GLY A 69 6.738 20.187 53.112 1.00 20.54 ATOM 524 CA GLY A 69 6.556 21.613 52.999 1.00 19.84 ATOM 525 C GLY A 69 5.093 21.939 52.985 1.00 21.77 ATOM 526 O GLY A 69 4.747 22.902 53.622 1.00 23.06 ATOM 527 N TYR A 70 4.241 21.181 52.312 1.00 20.33 ATOM 528 CA TYR A 70 2.831 21.430 52.245 1.00 19.86 ATOM 529 C TYR A 70 2.291 21.298 53.663 1.00 20.89 ATOM 530 O TYR A 70 1.468 22.121 53.999 1.00 22.64 ATOM 531 CB TYR A 70 2.097 20.449 51.302 1.00 20.32 ATOM 532 CG TYR A 70 2.386 20.531 49.821 1.00 22.15 ATOM 533 CD1 TYR A 70 2.986 21.674 49.250 1.00 19.96 ATOM 534 CD2 TYR A 70 2.152 19.373 49.004 1.00 19.73 ATOM 535 CE1 TYR A 70 3.286 21.768 47.893 1.00 20.82 ATOM 536 CE2 TYR A 70 2.474 19.453 47.625 1.00 20.55 ATOM 537 CZ TYR A 70 3.058 20.620 47.126 1.00 21.69 ATOM 538 OH TYR A 70 3.345 20.694 45.775 1.00 27.96 ATOM 539 N ALA A 71 2.611 20.267 54.362 1.00 21.93 ATOM 540 CA ALA A 71 2.203 19.924 55.711 1.00 23.56 ATOM 541 C ALA A 71 2.621 21.041 56.691 1.00 25.83 ATOM 542 O ALA A 71 1.766 21.468 57.457 1.00 27.05 ATOM 543 CB ALA A 71 2.841 18.597 56.147 1.00 21.93 ATOM 544 N GLN A 72 3.849 21.505 56.665 1.00 26.16 ATOM 545 CA GLN A 72 4.324 22.585 57.526 1.00 29.69 ATOM 546 C GLN A 72 3.581 23.915 57.325 1.00 31.89 ATOM 547 O GLN A 72 3.529 24.731 58.266 1.00 33.87 ATOM 548 CB GLN A 72 5.799 22.891 57.299 1.00 30.81 ATOM 549 CG GLN A 72 6.335 24.087 58.014 1.00 28.04 ATOM 550 CD GLN A 72 7.666 24.544 57.541 1.00 28.24 ATOM 551 OE1 GLN A 72 8.688 24.420 58.263 1.00 31.26 ATOM 552 NE2 GLN A 72 7.787 25.220 56.406 1.00 27.87 ATOM 553 N SER A 73 3.125 24.182 56.132 1.00 30.29 ATOM 554 CA SER A 73 2.352 25.347 55.800 1.00 30.44 ATOM 555 C SER A 73 0.858 25.159 56.164 1.00 30.34 ATOM 556 O SER A 73 0.023 26.082 55.871 1.00 32.61 ATOM 557 CB SER A 73 2.461 25.609 54.288 1.00 30.38 ATOM 558 OG SER A 73 3.816 25.858 54.030 1.00 32.28 ATOM 559 N GLY A 74 0.540 24.016 56.679 1.00 28.77 ATOM 560 CA GLY A 74 -0.750 23.452 57.039 1.00 30.04 ATOM 561 C GLY A 74 -1.695 23.126 55.876 1.00 30.20 ATOM 562 O GLY A 74 -2.925 23.338 56.115 1.00 31.87 ATOM 563 N LEU A 75 -1.351 22.593 54.725 1.00 27.25 ATOM 564 CA LEU A 75 -2.211 22.448 53.532 1.00 25.25 ATOM 565 C LEU A 75 -2.814 21.088 53.298 1.00 25.97 ATOM 566 O LEU A 75 -3.709 20.888 52.431 1.00 25.21 ATOM 567 CB LEU A 75 -1.440 23.007 52.308 1.00 22.09 ATOM 568 CG LEU A 75 -0.908 24.426 52.310 1.00 24.87 ATOM 569 CD1 LEU A 75 0.044 24.670 51.156 1.00 24.34 ATOM 570 CD2 LEU A 75 -2.032 25.491 52.287 1.00 22.85 ATOM 571 N LEU A 76 -2.380 20.196 54.193 1.00 26.85 ATOM 572 CA LEU A 76 -2.867 18.844 54.069 1.00 30.07 ATOM 573 C LEU A 76 -3.517 18.346 55.355 1.00 32.12 ATOM 574 O LEU A 76 -2.967 18.629 56.442 1.00 33.59 ATOM 575 CB LEU A 76 -1.603 17.915 53.801 1.00 26.99 ATOM 576 CG LEU A 76 -0.826 18.255 52.507 1.00 24.65 ATOM 577 CD1 LEU A 76 0.412 17.426 52.545 1.00 24.67 ATOM 578 CD2 LEU A 76 -1.736 17.975 51.314 1.00 25.03 ATOM 579 N ALA A 77 -4.477 17.498 55.197 1.00 32.30 ATOM 580 CA ALA A 77 -5.144 16.805 56.272 1.00 32.92 ATOM 581 C ALA A 77 -4.357 15.537 56.609 1.00 34.17 ATOM 582 O ALA A 77 -3.839 14.863 55.730 1.00 31.63 ATOM 583 CB ALA A 77 -6.604 16.393 55.908 1.00 31.57 ATOM 584 N GLU A 78 -4.388 15.224 57.907 1.00 35.96 ATOM 585 CA GLU A 78 -3.802 14.005 58.469 1.00 38.34 ATOM 586 C GLU A 78 -4.831 12.913 58.065 1.00 37.65 ATOM 587 O GLU A 78 -6.035 13.018 58.167 1.00 37.24 ATOM 588 CB GLU A 78 -3.524 14.013 59.946 1.00 40.69 ATOM 589 CG GLU A 78 -3.506 12.672 60.714 1.00 47.32 ATOM 590 CD GLU A 78 -3.186 12.745 62.197 1.00 51.54 ATOM 591 OE1 GLU A 78 -3.437 13.814 62.818 1.00 55.15 ATOM 592 OE2 GLU A 78 -2.630 11.729 62.729 1.00 51.80 ATOM 593 N ILE A 79 -4.274 11.857 57.515 1.00 38.37 ATOM 594 CA ILE A 79 -5.082 10.730 57.083 1.00 39.14 ATOM 595 C ILE A 79 -4.895 9.711 58.212 1.00 41.86 ATOM 596 O ILE A 79 -3.893 9.659 58.961 1.00 39.15 ATOM 597 CB ILE A 79 -4.646 10.246 55.654 1.00 37.05 ATOM 598 CG1 ILE A 79 -3.221 9.669 55.737 1.00 33.87 ATOM 599 CG2 ILE A 79 -4.665 11.286 54.489 1.00 35.74 ATOM 600 CD1 ILE A 79 -2.836 8.543 54.811 1.00 33.96 ATOM 601 N THR A 80 -5.870 8.815 58.253 1.00 48.00 ATOM 602 CA THR A 80 -5.966 7.696 59.217 1.00 52.57 ATOM 603 C THR A 80 -6.479 6.372 58.681 1.00 53.84 ATOM 604 O THR A 80 -7.673 5.962 58.756 1.00 54.91 ATOM 605 CB THR A 80 -6.917 8.170 60.409 1.00 55.23 ATOM 606 OG1 THR A 80 -8.044 8.810 59.662 1.00 58.54 ATOM 607 CG2 THR A 80 -6.330 9.099 61.448 1.00 55.39 ATOM 608 N PRO A 81 -5.583 5.595 58.139 1.00 54.92 ATOM 609 CA PRO A 81 -5.991 4.260 57.629 1.00 56.00 ATOM 610 C PRO A 81 -5.798 3.336 58.818 1.00 55.47 ATOM 611 O PRO A 81 -4.863 3.577 59.635 1.00 56.08 ATOM 612 CB PRO A 81 -5.069 4.062 56.456 1.00 55.59 ATOM 613 CG PRO A 81 -4.109 5.231 56.475 1.00 55.50 ATOM 614 CD PRO A 81 -4.136 5.757 57.920 1.00 55.00 ATOM 615 N ASP A 82 -6.608 2.319 58.946 1.00 55.71 ATOM 616 CA ASP A 82 -6.325 1.423 60.098 1.00 56.52 ATOM 617 C ASP A 82 -5.334 0.378 59.580 1.00 54.60 ATOM 618 O ASP A 82 -5.275 0.112 58.398 1.00 54.20 ATOM 619 CB ASP A 82 -7.533 0.779 60.713 1.00 62.77 ATOM 620 CG ASP A 82 -8.510 0.203 59.684 1.00 66.06 ATOM 621 OD1 ASP A 82 -8.551 0.728 58.551 1.00 67.70 ATOM 622 OD2 ASP A 82 -9.232 -0.756 60.123 1.00 68.32 ATOM 623 N LYS A 83 -4.683 -0.133 60.566 1.00 54.31 ATOM 624 CA LYS A 83 -3.648 -1.162 60.479 1.00 54.60 ATOM 625 C LYS A 83 -4.000 -2.220 59.437 1.00 51.81 ATOM 626 O LYS A 83 -3.114 -2.932 58.965 1.00 50.29 ATOM 627 CB LYS A 83 -3.361 -1.858 61.832 1.00 58.99 ATOM 628 CG LYS A 83 -4.129 -3.155 62.039 1.00 63.00 ATOM 629 CD LYS A 83 -3.495 -4.192 62.931 1.00 67.55 ATOM 630 CE LYS A 83 -2.110 -4.711 62.605 1.00 70.95 ATOM 631 NZ LYS A 83 -1.943 -6.219 62.769 1.00 72.56 ATOM 632 N ALA A 84 -5.313 -2.323 59.170 1.00 50.22 ATOM 633 CA ALA A 84 -5.685 -3.361 58.194 1.00 48.69 ATOM 634 C ALA A 84 -5.360 -2.663 56.859 1.00 46.75 ATOM 635 O ALA A 84 -4.632 -3.329 56.150 1.00 48.64 ATOM 636 CB ALA A 84 -7.075 -3.972 58.102 1.00 47.82 ATOM 637 N PHE A 85 -5.893 -1.498 56.680 1.00 44.73 ATOM 638 CA PHE A 85 -5.592 -0.877 55.383 1.00 42.93 ATOM 639 C PHE A 85 -4.103 -0.652 55.251 1.00 43.08 ATOM 640 O PHE A 85 -3.555 -0.878 54.129 1.00 44.12 ATOM 641 CB PHE A 85 -6.298 0.407 55.166 1.00 42.44 ATOM 642 CG PHE A 85 -5.926 0.984 53.819 1.00 42.40 ATOM 643 CD1 PHE A 85 -4.763 1.697 53.693 1.00 40.81 ATOM 644 CD2 PHE A 85 -6.785 0.724 52.723 1.00 43.10 ATOM 645 CE1 PHE A 85 -4.413 2.219 52.454 1.00 40.45 ATOM 646 CE2 PHE A 85 -6.448 1.220 51.476 1.00 43.41 ATOM 647 CZ PHE A 85 -5.229 1.961 51.384 1.00 41.49 ATOM 648 N GLN A 86 -3.486 -0.239 56.338 1.00 41.40 ATOM 649 CA GLN A 86 -2.055 0.037 56.321 1.00 40.67 ATOM 650 C GLN A 86 -1.199 -1.130 55.858 1.00 41.37 ATOM 651 O GLN A 86 -0.095 -0.987 55.275 1.00 41.02 ATOM 652 CB GLN A 86 -1.576 0.502 57.733 1.00 42.75 ATOM 653 CG GLN A 86 -1.367 1.945 57.878 1.00 44.12 ATOM 654 CD GLN A 86 -0.889 2.594 59.145 1.00 45.08 ATOM 655 OE1 GLN A 86 0.263 2.976 59.394 1.00 45.97 ATOM 656 NE2 GLN A 86 -1.976 2.843 59.916 1.00 46.63 ATOM 657 N ASP A 87 -1.659 -2.305 56.203 1.00 40.74 ATOM 658 CA ASP A 87 -1.148 -3.659 56.041 1.00 40.77 ATOM 659 C ASP A 87 -1.014 -4.095 54.581 1.00 36.12 ATOM 660 O ASP A 87 -0.106 -4.841 54.178 1.00 36.45 ATOM 661 CB ASP A 87 -2.078 -4.539 56.904 1.00 45.46 ATOM 662 CG ASP A 87 -1.348 -5.368 57.935 1.00 50.80 ATOM 663 OD1 ASP A 87 -0.195 -5.011 58.289 1.00 52.85 ATOM 664 OD2 ASP A 87 -2.095 -6.334 58.365 1.00 54.43 ATOM 665 N LYS A 88 -1.855 -3.553 53.783 1.00 34.25 ATOM 666 CA LYS A 88 -1.866 -3.768 52.329 1.00 32.57 ATOM 667 C LYS A 88 -0.695 -3.118 51.592 1.00 32.53 ATOM 668 O LYS A 88 -0.388 -3.479 50.417 1.00 36.26 ATOM 669 CB LYS A 88 -3.158 -3.208 51.839 1.00 31.00 ATOM 670 CG LYS A 88 -4.348 -4.082 52.148 1.00 33.05 ATOM 671 CD LYS A 88 -5.585 -3.624 51.509 1.00 36.47 ATOM 672 CE LYS A 88 -6.801 -3.153 52.223 1.00 40.72 ATOM 673 NZ LYS A 88 -8.041 -3.430 51.410 1.00 39.71 ATOM 674 N LEU A 89 -0.001 -2.180 52.182 1.00 31.86 ATOM 675 CA LEU A 89 1.078 -1.438 51.592 1.00 30.68 ATOM 676 C LEU A 89 2.424 -1.743 52.188 1.00 31.20 ATOM 677 O LEU A 89 2.580 -2.021 53.398 1.00 33.15 ATOM 678 CB LEU A 89 0.754 0.058 51.818 1.00 28.91 ATOM 679 CG LEU A 89 -0.396 0.724 51.217 1.00 28.89 ATOM 680 CD1 LEU A 89 0.033 2.105 50.669 1.00 31.33 ATOM 681 CD2 LEU A 89 -0.967 -0.023 50.028 1.00 28.02 ATOM 682 N TYR A 90 3.420 -1.623 51.328 1.00 28.21 ATOM 683 CA TYR A 90 4.762 -1.772 51.877 1.00 30.92 ATOM 684 C TYR A 90 4.976 -0.644 52.893 1.00 34.34 ATOM 685 O TYR A 90 4.765 0.612 52.670 1.00 34.67 ATOM 686 CB TYR A 90 5.778 -1.665 50.766 1.00 30.58 ATOM 687 CG TYR A 90 5.730 -2.788 49.775 1.00 33.53 ATOM 688 CD1 TYR A 90 6.343 -3.997 50.125 1.00 32.52 ATOM 689 CD2 TYR A 90 5.136 -2.674 48.483 1.00 32.65 ATOM 690 CE1 TYR A 90 6.375 -5.034 49.184 1.00 32.72 ATOM 691 CE2 TYR A 90 5.194 -3.704 47.543 1.00 31.58 ATOM 692 CZ TYR A 90 5.806 -4.873 47.909 1.00 33.65 ATOM 693 OH TYR A 90 5.894 -6.027 47.128 1.00 38.81 ATOM 694 N PRO A 91 5.472 -1.021 54.054 1.00 35.71 ATOM 695 CA PRO A 91 5.743 -0.054 55.147 1.00 34.70 ATOM 696 C PRO A 91 6.789 0.986 54.825 1.00 31.44 ATOM 697 O PRO A 91 6.625 2.093 55.315 1.00 29.86 ATOM 698 CB PRO A 91 6.145 -0.898 56.366 1.00 36.66 ATOM 699 CG PRO A 91 6.858 -2.068 55.646 1.00 39.29 ATOM 700 CD PRO A 91 5.751 -2.407 54.507 1.00 37.31 ATOM 701 N PHE A 92 7.812 0.692 54.062 1.00 31.09 ATOM 702 CA PHE A 92 8.761 1.798 53.816 1.00 30.13 ATOM 703 C PHE A 92 7.980 2.873 53.054 1.00 29.72 ATOM 704 O PHE A 92 8.452 4.065 53.135 1.00 31.00 ATOM 705 CB PHE A 92 9.994 1.312 53.066 1.00 32.57 ATOM 706 CG PHE A 92 9.795 1.229 51.575 1.00 35.45 ATOM 707 CD1 PHE A 92 9.274 0.051 51.017 1.00 34.58 ATOM 708 CD2 PHE A 92 10.154 2.353 50.737 1.00 35.83 ATOM 709 CE1 PHE A 92 9.068 -0.024 49.621 1.00 35.83 ATOM 710 CE2 PHE A 92 9.954 2.238 49.346 1.00 34.23 ATOM 711 CZ PHE A 92 9.423 1.049 48.762 1.00 32.68 ATOM 712 N THR A 93 6.878 2.550 52.376 1.00 26.97 ATOM 713 CA THR A 93 6.114 3.577 51.626 1.00 25.83 ATOM 714 C THR A 93 5.303 4.485 52.544 1.00 26.16 ATOM 715 O THR A 93 5.187 5.711 52.244 1.00 22.40 ATOM 716 CB THR A 93 5.312 3.002 50.376 1.00 23.01 ATOM 717 OG1 THR A 93 4.140 2.345 50.911 1.00 24.85 ATOM 718 CG2 THR A 93 6.136 2.118 49.477 1.00 23.30 ATOM 719 N TRP A 94 4.851 3.960 53.741 1.00 26.08 ATOM 720 CA TRP A 94 4.115 4.857 54.703 1.00 23.12 ATOM 721 C TRP A 94 5.129 5.776 55.365 1.00 21.53 ATOM 722 O TRP A 94 4.807 6.960 55.720 1.00 24.87 ATOM 723 CB TRP A 94 3.406 4.023 55.736 1.00 22.26 ATOM 724 CG TRP A 94 2.208 3.297 55.299 1.00 18.12 ATOM 725 CD1 TRP A 94 2.068 1.941 55.159 1.00 19.30 ATOM 726 CD2 TRP A 94 0.951 3.873 54.963 1.00 21.74 ATOM 727 NE1 TRP A 94 0.792 1.662 54.712 1.00 23.67 ATOM 728 CE2 TRP A 94 0.060 2.833 54.640 1.00 21.25 ATOM 729 CE3 TRP A 94 0.467 5.175 54.836 1.00 22.59 ATOM 730 CZ2 TRP A 94 -1.244 3.066 54.237 1.00 24.60 ATOM 731 CZ3 TRP A 94 -0.838 5.426 54.475 1.00 23.57 ATOM 732 CH2 TRP A 94 -1.705 4.370 54.147 1.00 24.10 ATOM 733 N ASP A 95 6.337 5.471 55.555 1.00 21.02 ATOM 734 CA ASP A 95 7.382 6.192 56.184 1.00 24.72 ATOM 735 C ASP A 95 7.741 7.457 55.390 1.00 27.52 ATOM 736 O ASP A 95 8.259 8.423 55.970 1.00 29.97 ATOM 737 CB ASP A 95 8.645 5.336 56.324 1.00 31.58 ATOM 738 CG ASP A 95 8.676 4.295 57.449 1.00 37.85 ATOM 739 OD1 ASP A 95 7.891 4.520 58.384 1.00 38.66 ATOM 740 OD2 ASP A 95 9.482 3.292 57.276 1.00 41.90 ATOM 741 N ALA A 96 7.610 7.281 54.071 1.00 24.95 ATOM 742 CA ALA A 96 7.892 8.354 53.110 1.00 22.68 ATOM 743 C ALA A 96 6.867 9.442 53.266 1.00 21.80 ATOM 744 O ALA A 96 7.222 10.619 52.975 1.00 22.63 ATOM 745 CB ALA A 96 7.917 7.754 51.666 1.00 22.45 ATOM 746 N VAL A 97 5.668 9.140 53.809 1.00 21.20 ATOM 747 CA VAL A 97 4.588 10.128 53.863 1.00 21.68 ATOM 748 C VAL A 97 4.260 10.533 55.320 1.00 20.10 ATOM 749 O VAL A 97 3.113 10.963 55.469 1.00 23.68 ATOM 750 CB VAL A 97 3.406 9.711 52.984 1.00 20.81 ATOM 751 CG1 VAL A 97 3.849 9.699 51.476 1.00 22.95 ATOM 752 CG2 VAL A 97 2.806 8.361 53.305 1.00 22.42 ATOM 753 N ARG A 98 5.221 10.425 56.118 1.00 20.47 ATOM 754 CA ARG A 98 5.092 10.782 57.541 1.00 24.25 ATOM 755 C ARG A 98 5.812 12.070 57.734 1.00 25.01 ATOM 756 O ARG A 98 6.961 12.267 57.356 1.00 28.96 ATOM 757 CB ARG A 98 5.688 9.779 58.522 1.00 28.60 ATOM 758 CG ARG A 98 4.894 9.002 59.504 1.00 28.40 ATOM 759 CD ARG A 98 5.836 7.995 60.108 1.00 31.71 ATOM 760 NE ARG A 98 5.260 6.648 59.970 1.00 37.22 ATOM 761 CZ ARG A 98 4.000 6.314 60.322 1.00 38.13 ATOM 762 NH1 ARG A 98 3.127 7.156 60.885 1.00 39.75 ATOM 763 NH2 ARG A 98 3.559 5.083 59.956 1.00 41.00 ATOM 764 N TYR A 99 5.160 13.006 58.346 1.00 26.30 ATOM 765 CA TYR A 99 5.801 14.269 58.627 1.00 26.67 ATOM 766 C TYR A 99 5.519 14.525 60.134 1.00 27.16 ATOM 767 O TYR A 99 4.373 14.753 60.435 1.00 26.89 ATOM 768 CB TYR A 99 5.307 15.360 57.701 1.00 24.28 ATOM 769 CG TYR A 99 5.961 16.706 57.982 1.00 25.20 ATOM 770 CD1 TYR A 99 7.269 17.038 57.673 1.00 24.46 ATOM 771 CD2 TYR A 99 5.163 17.655 58.601 1.00 25.88 ATOM 772 CE1 TYR A 99 7.777 18.288 57.850 1.00 26.00 ATOM 773 CE2 TYR A 99 5.666 18.875 58.900 1.00 26.79 ATOM 774 CZ TYR A 99 6.935 19.203 58.489 1.00 26.99 ATOM 775 OH TYR A 99 7.299 20.493 58.794 1.00 28.07 ATOM 776 N ASN A 100 6.581 14.571 60.907 1.00 28.54 ATOM 777 CA ASN A 100 6.527 14.796 62.348 1.00 32.41 ATOM 778 C ASN A 100 5.685 13.700 62.989 1.00 31.57 ATOM 779 O ASN A 100 4.853 13.941 63.858 1.00 33.49 ATOM 780 CB ASN A 100 6.140 16.247 62.680 1.00 36.49 ATOM 781 CG ASN A 100 7.183 17.309 62.280 1.00 41.17 ATOM 782 OD1 ASN A 100 6.758 18.431 61.850 1.00 41.34 ATOM 783 ND2 ASN A 100 8.541 17.155 62.334 1.00 39.92 ATOM 784 N GLY A 101 5.851 12.476 62.548 1.00 30.13 ATOM 785 CA GLY A 101 5.180 11.273 62.933 1.00 29.61 ATOM 786 C GLY A 101 3.781 11.076 62.418 1.00 31.93 ATOM 787 O GLY A 101 3.243 9.899 62.509 1.00 35.22 ATOM 788 N LYS A 102 3.051 12.005 61.854 1.00 32.67 ATOM 789 CA LYS A 102 1.670 11.907 61.342 1.00 32.94 ATOM 790 C LYS A 102 1.656 11.447 59.839 1.00 32.17 ATOM 791 O LYS A 102 2.573 11.834 59.150 1.00 28.00 ATOM 792 CB LYS A 102 0.934 13.256 61.235 1.00 37.09 ATOM 793 CG LYS A 102 0.784 14.097 62.538 1.00 40.86 ATOM 794 CD LYS A 102 0.394 13.064 63.638 1.00 44.14 ATOM 795 CE LYS A 102 -0.338 13.701 64.823 1.00 46.57 ATOM 796 NZ LYS A 102 -0.755 12.588 65.782 1.00 46.78 ATOM 797 N LEU A 103 0.651 10.772 59.416 1.00 29.20 ATOM 798 CA LEU A 103 0.647 10.414 57.981 1.00 29.95 ATOM 799 C LEU A 103 -0.024 11.544 57.260 1.00 28.33 ATOM 800 O LEU A 103 -1.064 11.961 57.805 1.00 26.73 ATOM 801 CB LEU A 103 0.057 9.038 57.935 1.00 27.56 ATOM 802 CG LEU A 103 0.944 7.980 58.543 1.00 28.99 ATOM 803 CD1 LEU A 103 -0.150 6.846 58.571 1.00 31.26 ATOM 804 CD2 LEU A 103 2.117 7.496 57.758 1.00 27.09 ATOM 805 N ILE A 104 0.541 12.052 56.160 1.00 25.90 ATOM 806 CA ILE A 104 -0.093 13.204 55.454 1.00 24.57 ATOM 807 C ILE A 104 -0.491 12.985 53.991 1.00 23.58 ATOM 808 O ILE A 104 -0.848 13.939 53.305 1.00 22.61 ATOM 809 CB ILE A 104 0.911 14.399 55.422 1.00 26.59 ATOM 810 CG1 ILE A 104 2.225 13.846 54.747 1.00 25.94 ATOM 811 CG2 ILE A 104 1.146 14.944 56.807 1.00 30.88 ATOM 812 CD1 ILE A 104 3.358 14.822 54.795 1.00 30.36 ATOM 813 N ALA A 105 -0.335 11.666 53.675 1.00 23.69 ATOM 814 CA ALA A 105 -0.716 11.218 52.310 1.00 20.89 ATOM 815 C ALA A 105 -0.708 9.698 52.197 1.00 20.42 ATOM 816 O ALA A 105 -0.234 8.960 53.070 1.00 20.81 ATOM 817 CB ALA A 105 0.229 11.869 51.295 1.00 21.61 ATOM 818 N TYR A 106 -1.336 9.241 51.108 1.00 20.25 ATOM 819 CA TYR A 106 -1.406 7.840 50.689 1.00 21.08 ATOM 820 C TYR A 106 -0.307 7.633 49.587 1.00 20.59 ATOM 821 O TYR A 106 -0.359 8.425 48.619 1.00 19.76 ATOM 822 CB TYR A 106 -2.718 7.479 50.009 1.00 23.92 ATOM 823 CG TYR A 106 -3.876 7.430 51.002 1.00 28.83 ATOM 824 CD1 TYR A 106 -4.573 8.611 51.259 1.00 26.50 ATOM 825 CD2 TYR A 106 -4.262 6.222 51.592 1.00 29.20 ATOM 826 CE1 TYR A 106 -5.639 8.582 52.167 1.00 29.58 ATOM 827 CE2 TYR A 106 -5.306 6.180 52.510 1.00 30.48 ATOM 828 CZ TYR A 106 -5.965 7.379 52.777 1.00 31.74 ATOM 829 OH TYR A 106 -7.020 7.383 53.717 1.00 38.89 ATOM 830 N PRO A 107 0.534 6.704 49.826 1.00 22.27 ATOM 831 CA PRO A 107 1.638 6.329 48.917 1.00 21.19 ATOM 832 C PRO A 107 1.011 5.510 47.810 1.00 23.25 ATOM 833 O PRO A 107 0.141 4.688 48.173 1.00 23.73 ATOM 834 CB PRO A 107 2.586 5.492 49.685 1.00 23.35 ATOM 835 CG PRO A 107 1.966 5.419 51.123 1.00 25.03 ATOM 836 CD PRO A 107 0.528 5.833 51.049 1.00 21.59 ATOM 837 N ILE A 108 1.388 5.744 46.566 1.00 20.48 ATOM 838 CA ILE A 108 0.812 5.081 45.397 1.00 19.11 ATOM 839 C ILE A 108 1.842 4.209 44.688 1.00 20.39 ATOM 840 O ILE A 108 1.619 2.986 44.489 1.00 20.35 ATOM 841 CB ILE A 108 0.203 6.157 44.376 1.00 17.76 ATOM 842 CG1 ILE A 108 -0.820 7.134 44.985 1.00 19.36 ATOM 843 CG2 ILE A 108 -0.363 5.481 43.115 1.00 22.68 ATOM 844 CD1 ILE A 108 -2.163 6.666 45.614 1.00 20.72 ATOM 845 N ALA A 109 3.045 4.788 44.414 1.00 17.12 ATOM 846 CA ALA A 109 4.029 3.991 43.618 1.00 18.16 ATOM 847 C ALA A 109 5.391 4.510 43.851 1.00 16.34 ATOM 848 O ALA A 109 5.536 5.681 44.292 1.00 19.36 ATOM 849 CB ALA A 109 3.693 4.114 42.090 1.00 19.32 ATOM 850 N VAL A 110 6.392 3.757 43.616 1.00 16.63 ATOM 851 CA VAL A 110 7.815 3.914 43.813 1.00 19.47 ATOM 852 C VAL A 110 8.466 4.093 42.441 1.00 19.31 ATOM 853 O VAL A 110 8.361 3.235 41.575 1.00 19.56 ATOM 854 CB VAL A 110 8.432 2.783 44.667 1.00 19.26 ATOM 855 CG1 VAL A 110 9.900 3.053 44.739 1.00 18.84 ATOM 856 CG2 VAL A 110 7.627 2.709 45.946 1.00 24.54 ATOM 857 N GLU A 111 8.946 5.363 42.375 1.00 19.12 ATOM 858 CA GLU A 111 9.575 5.813 41.060 1.00 18.05 ATOM 859 C GLU A 111 11.055 5.901 41.097 1.00 17.63 ATOM 860 O GLU A 111 11.665 6.478 42.044 1.00 17.48 ATOM 861 CB GLU A 111 8.944 7.213 40.782 1.00 15.13 ATOM 862 CG GLU A 111 7.445 7.353 40.682 1.00 15.53 ATOM 863 CD GLU A 111 7.095 8.754 40.327 1.00 14.88 ATOM 864 OE1 GLU A 111 7.896 9.661 40.337 1.00 20.98 ATOM 865 OE2 GLU A 111 5.939 8.935 39.907 1.00 17.19 ATOM 866 N ALA A 112 11.859 5.306 40.131 1.00 16.11 ATOM 867 CA ALA A 112 13.287 5.450 40.066 1.00 16.29 ATOM 868 C ALA A 112 13.596 5.540 38.535 1.00 16.18 ATOM 869 O ALA A 112 12.853 4.921 37.758 1.00 17.75 ATOM 870 CB ALA A 112 14.104 4.403 40.727 1.00 17.57 ATOM 871 N LEU A 113 14.524 6.373 38.197 1.00 15.81 ATOM 872 CA LEU A 113 14.992 6.475 36.795 1.00 16.31 ATOM 873 C LEU A 113 15.779 5.207 36.435 1.00 17.37 ATOM 874 O LEU A 113 16.563 4.592 37.259 1.00 16.95 ATOM 875 CB LEU A 113 15.948 7.690 36.724 1.00 12.97 ATOM 876 CG LEU A 113 15.269 9.058 36.830 1.00 16.08 ATOM 877 CD1 LEU A 113 16.309 10.173 36.962 1.00 15.89 ATOM 878 CD2 LEU A 113 14.344 9.371 35.594 1.00 14.66 ATOM 879 N SER A 114 15.751 4.800 35.164 1.00 17.56 ATOM 880 CA SER A 114 16.506 3.673 34.557 1.00 16.88 ATOM 881 C SER A 114 17.190 4.079 33.203 1.00 16.45 ATOM 882 O SER A 114 16.855 5.167 32.777 1.00 15.05 ATOM 883 CB SER A 114 15.566 2.522 34.240 1.00 17.43 ATOM 884 OG SER A 114 15.273 1.908 35.456 1.00 18.50 ATOM 885 N LEU A 115 18.155 3.274 32.804 1.00 16.59 ATOM 886 CA LEU A 115 18.773 3.520 31.496 1.00 18.16 ATOM 887 C LEU A 115 17.830 2.804 30.543 1.00 15.78 ATOM 888 O LEU A 115 17.542 1.609 30.725 1.00 17.76 ATOM 889 CB LEU A 115 20.123 2.905 31.515 1.00 21.46 ATOM 890 CG LEU A 115 21.367 3.289 30.653 1.00 25.25 ATOM 891 CD1 LEU A 115 22.063 2.092 30.030 1.00 26.37 ATOM 892 CD2 LEU A 115 21.141 4.471 29.735 1.00 23.62 ATOM 893 N ILE A 116 17.356 3.439 29.514 1.00 18.00 ATOM 894 CA ILE A 116 16.518 2.842 28.423 1.00 17.85 ATOM 895 C ILE A 116 17.381 2.852 27.162 1.00 19.11 ATOM 896 O ILE A 116 17.993 3.907 26.830 1.00 19.58 ATOM 897 CB ILE A 116 15.229 3.671 28.236 1.00 18.14 ATOM 898 CG1 ILE A 116 14.512 3.780 29.674 1.00 15.11 ATOM 899 CG2 ILE A 116 14.332 3.194 27.070 1.00 17.15 ATOM 900 CD1 ILE A 116 13.363 4.821 29.656 1.00 15.93 ATOM 901 N TYR A 117 17.464 1.703 26.513 1.00 21.13 ATOM 902 CA TYR A 117 18.417 1.714 25.319 1.00 21.95 ATOM 903 C TYR A 117 17.671 1.037 24.174 1.00 25.23 ATOM 904 O TYR A 117 16.705 0.223 24.470 1.00 23.97 ATOM 905 CB TYR A 117 19.736 1.067 25.685 1.00 18.27 ATOM 906 CG TYR A 117 19.578 -0.360 26.080 1.00 18.45 ATOM 907 CD1 TYR A 117 19.042 -0.837 27.268 1.00 17.53 ATOM 908 CD2 TYR A 117 19.981 -1.387 25.125 1.00 21.09 ATOM 909 CE1 TYR A 117 18.933 -2.183 27.549 1.00 19.38 ATOM 910 CE2 TYR A 117 19.920 -2.741 25.387 1.00 21.48 ATOM 911 CZ TYR A 117 19.408 -3.113 26.584 1.00 22.33 ATOM 912 OH TYR A 117 19.323 -4.438 26.903 1.00 26.17 ATOM 913 N ASN A 118 18.170 1.426 22.968 1.00 24.59 ATOM 914 CA ASN A 118 17.557 0.905 21.693 1.00 25.44 ATOM 915 C ASN A 118 18.289 -0.377 21.386 1.00 26.69 ATOM 916 O ASN A 118 19.506 -0.222 21.069 1.00 27.32 ATOM 917 CB ASN A 118 17.711 1.981 20.627 1.00 26.59 ATOM 918 CG ASN A 118 17.049 1.629 19.274 1.00 27.12 ATOM 919 OD1 ASN A 118 17.115 0.418 19.004 1.00 29.87 ATOM 920 ND2 ASN A 118 16.462 2.559 18.601 1.00 21.35 ATOM 921 N LYS A 119 17.635 -1.513 21.540 1.00 29.38 ATOM 922 CA LYS A 119 18.309 -2.819 21.311 1.00 32.47 ATOM 923 C LYS A 119 18.879 -3.061 19.880 1.00 33.14 ATOM 924 O LYS A 119 19.770 -3.886 19.725 1.00 32.70 ATOM 925 CB LYS A 119 17.404 -4.007 21.582 1.00 31.77 ATOM 926 CG LYS A 119 17.518 -4.488 22.999 1.00 35.09 ATOM 927 CD LYS A 119 16.296 -5.225 23.514 1.00 35.12 ATOM 928 CE LYS A 119 16.359 -5.642 24.965 1.00 34.21 ATOM 929 NZ LYS A 119 15.217 -6.488 25.378 1.00 35.24 ATOM 930 N ASP A 120 18.318 -2.288 19.006 1.00 35.33 ATOM 931 CA ASP A 120 18.693 -2.341 17.588 1.00 39.15 ATOM 932 C ASP A 120 19.923 -1.476 17.348 1.00 39.04 ATOM 933 O ASP A 120 20.636 -1.927 16.409 1.00 40.70 ATOM 934 CB ASP A 120 17.515 -2.047 16.656 1.00 41.65 ATOM 935 CG ASP A 120 16.435 -3.096 16.637 1.00 43.82 ATOM 936 OD1 ASP A 120 16.684 -4.294 16.979 1.00 45.34 ATOM 937 OD2 ASP A 120 15.294 -2.709 16.301 1.00 45.82 ATOM 938 N LEU A 121 20.172 -0.364 17.982 1.00 38.50 ATOM 939 CA LEU A 121 21.423 0.389 17.801 1.00 36.34 ATOM 940 C LEU A 121 22.451 -0.169 18.791 1.00 37.77 ATOM 941 O LEU A 121 23.648 -0.044 18.491 1.00 38.65 ATOM 942 CB LEU A 121 21.275 1.875 18.047 1.00 36.56 ATOM 943 CG LEU A 121 20.402 2.698 17.131 1.00 39.79 ATOM 944 CD1 LEU A 121 20.271 4.197 17.459 1.00 38.11 ATOM 945 CD2 LEU A 121 21.197 2.503 15.817 1.00 40.75 ATOM 946 N LEU A 122 22.036 -0.712 19.908 1.00 39.02 ATOM 947 CA LEU A 122 22.901 -1.158 21.038 1.00 40.84 ATOM 948 C LEU A 122 22.415 -2.372 21.784 1.00 40.90 ATOM 949 O LEU A 122 21.783 -2.245 22.858 1.00 40.10 ATOM 950 CB LEU A 122 22.843 0.074 22.038 1.00 37.41 ATOM 951 CG LEU A 122 24.045 0.545 22.773 1.00 36.20 ATOM 952 CD1 LEU A 122 25.172 1.133 21.918 1.00 31.92 ATOM 953 CD2 LEU A 122 23.560 1.681 23.729 1.00 35.75 ATOM 954 N PRO A 123 22.602 -3.527 21.227 1.00 42.48 ATOM 955 CA PRO A 123 22.122 -4.771 21.828 1.00 42.51 ATOM 956 C PRO A 123 22.633 -4.856 23.250 1.00 42.49 ATOM 957 O PRO A 123 21.889 -5.396 24.116 1.00 44.14 ATOM 958 CB PRO A 123 22.697 -5.851 20.907 1.00 43.39 ATOM 959 CG PRO A 123 23.921 -5.160 20.290 1.00 43.08 ATOM 960 CD PRO A 123 23.281 -3.797 19.929 1.00 43.36 ATOM 961 N ASN A 124 23.848 -4.411 23.500 1.00 40.11 ATOM 962 CA ASN A 124 24.436 -4.430 24.893 1.00 39.28 ATOM 963 C ASN A 124 24.699 -2.983 25.408 1.00 35.36 ATOM 964 O ASN A 124 25.544 -2.200 24.866 1.00 35.83 ATOM 965 CB ASN A 124 25.688 -5.242 24.919 1.00 43.22 ATOM 966 CG ASN A 124 25.888 -6.630 24.398 1.00 45.68 ATOM 967 OD1 ASN A 124 25.135 -7.621 24.520 1.00 46.42 ATOM 968 ND2 ASN A 124 27.121 -6.708 23.831 1.00 48.20 ATOM 969 N PRO A 125 24.023 -2.653 26.478 1.00 32.94 ATOM 970 CA PRO A 125 24.146 -1.284 27.048 1.00 32.58 ATOM 971 C PRO A 125 25.483 -1.158 27.717 1.00 32.47 ATOM 972 O PRO A 125 26.119 -2.126 28.132 1.00 32.68 ATOM 973 CB PRO A 125 22.934 -1.129 27.895 1.00 31.36 ATOM 974 CG PRO A 125 22.571 -2.546 28.323 1.00 33.73 ATOM 975 CD PRO A 125 23.048 -3.488 27.189 1.00 32.55 ATOM 976 N PRO A 126 26.015 0.050 27.726 1.00 32.55 ATOM 977 CA PRO A 126 27.316 0.333 28.373 1.00 33.12 ATOM 978 C PRO A 126 27.197 0.107 29.898 1.00 32.17 ATOM 979 O PRO A 126 26.114 0.402 30.493 1.00 32.16 ATOM 980 CB PRO A 126 27.654 1.792 27.990 1.00 33.63 ATOM 981 CG PRO A 126 26.534 2.218 27.065 1.00 34.70 ATOM 982 CD PRO A 126 25.313 1.286 27.272 1.00 33.73 ATOM 983 N LYS A 127 28.244 -0.322 30.560 1.00 29.30 ATOM 984 CA LYS A 127 28.123 -0.543 32.003 1.00 30.59 ATOM 985 C LYS A 127 28.671 0.640 32.807 1.00 29.38 ATOM 986 O LYS A 127 28.465 0.821 34.026 1.00 27.74 ATOM 987 CB LYS A 127 28.815 -1.906 32.256 1.00 35.30 ATOM 988 CG LYS A 127 27.672 -2.976 32.501 1.00 41.24 ATOM 989 CD LYS A 127 27.409 -3.916 31.380 1.00 47.13 ATOM 990 CE LYS A 127 25.965 -4.441 31.151 1.00 48.12 ATOM 991 NZ LYS A 127 25.942 -4.992 29.743 1.00 49.46 ATOM 992 N THR A 128 29.275 1.560 32.043 1.00 26.29 ATOM 993 CA THR A 128 30.002 2.696 32.648 1.00 26.05 ATOM 994 C THR A 128 29.751 3.992 31.985 1.00 25.56 ATOM 995 O THR A 128 29.543 4.077 30.763 1.00 24.55 ATOM 996 CB THR A 128 31.509 2.123 32.488 1.00 25.96 ATOM 997 OG1 THR A 128 31.980 1.657 33.780 1.00 29.55 ATOM 998 CG2 THR A 128 32.328 2.998 31.601 1.00 25.62 ATOM 999 N TRP A 129 29.686 5.095 32.775 1.00 22.57 ATOM 1000 CA TRP A 129 29.465 6.386 32.176 1.00 21.86 ATOM 1001 C TRP A 129 30.691 6.689 31.289 1.00 21.46 ATOM 1002 O TRP A 129 30.647 7.383 30.271 1.00 21.15 ATOM 1003 CB TRP A 129 29.350 7.436 33.317 1.00 23.76 ATOM 1004 CG TRP A 129 27.973 7.644 33.848 1.00 24.64 ATOM 1005 CD1 TRP A 129 27.344 7.148 34.971 1.00 21.70 ATOM 1006 CD2 TRP A 129 26.994 8.467 33.156 1.00 23.36 ATOM 1007 NE1 TRP A 129 25.993 7.569 35.025 1.00 19.15 ATOM 1008 CE2 TRP A 129 25.784 8.394 33.975 1.00 22.69 ATOM 1009 CE3 TRP A 129 27.112 9.224 31.981 1.00 20.23 ATOM 1010 CZ2 TRP A 129 24.633 9.125 33.644 1.00 19.81 ATOM 1011 CZ3 TRP A 129 25.978 9.965 31.693 1.00 22.64 ATOM 1012 CH2 TRP A 129 24.821 9.925 32.549 1.00 22.50 ATOM 1013 N GLU A 130 31.842 6.199 31.802 1.00 22.82 ATOM 1014 CA GLU A 130 33.126 6.541 31.119 1.00 24.25 ATOM 1015 C GLU A 130 33.219 6.034 29.700 1.00 25.21 ATOM 1016 O GLU A 130 33.899 6.714 28.877 1.00 26.38 ATOM 1017 CB GLU A 130 34.312 5.985 31.893 1.00 23.64 ATOM 1018 CG GLU A 130 34.639 6.512 33.275 1.00 23.29 ATOM 1019 CD GLU A 130 33.820 6.110 34.451 1.00 23.53 ATOM 1020 OE1 GLU A 130 32.810 5.417 34.290 1.00 25.25 ATOM 1021 OE2 GLU A 130 34.245 6.492 35.507 1.00 22.59 ATOM 1022 N GLU A 131 32.555 4.966 29.351 1.00 26.58 ATOM 1023 CA GLU A 131 32.687 4.538 27.900 1.00 28.26 ATOM 1024 C GLU A 131 31.685 5.175 27.016 1.00 29.45 ATOM 1025 O GLU A 131 31.565 4.850 25.804 1.00 31.04 ATOM 1026 CB GLU A 131 32.585 3.038 27.821 1.00 29.03 ATOM 1027 CG GLU A 131 31.257 2.417 28.043 1.00 32.54 ATOM 1028 CD GLU A 131 31.238 1.034 28.644 1.00 37.41 ATOM 1029 OE1 GLU A 131 31.296 0.638 29.811 1.00 34.16 ATOM 1030 OE2 GLU A 131 31.135 0.166 27.697 1.00 40.94 ATOM 1031 N ILE A 132 30.963 6.168 27.483 1.00 27.99 ATOM 1032 CA ILE A 132 29.934 6.793 26.670 1.00 29.27 ATOM 1033 C ILE A 132 30.536 7.669 25.596 1.00 28.86 ATOM 1034 O ILE A 132 30.010 7.680 24.485 1.00 26.35 ATOM 1035 CB ILE A 132 28.836 7.449 27.638 1.00 31.57 ATOM 1036 CG1 ILE A 132 28.032 6.218 28.228 1.00 31.14 ATOM 1037 CG2 ILE A 132 27.918 8.499 27.031 1.00 32.36 ATOM 1038 CD1 ILE A 132 26.841 6.685 29.152 1.00 31.26 ATOM 1039 N PRO A 133 31.564 8.425 25.897 1.00 28.91 ATOM 1040 CA PRO A 133 32.157 9.342 24.872 1.00 31.07 ATOM 1041 C PRO A 133 32.598 8.567 23.602 1.00 31.73 ATOM 1042 O PRO A 133 32.226 9.090 22.506 1.00 29.60 ATOM 1043 CB PRO A 133 33.235 10.139 25.597 1.00 28.81 ATOM 1044 CG PRO A 133 32.754 10.004 27.071 1.00 28.14 ATOM 1045 CD PRO A 133 32.302 8.503 27.152 1.00 28.79 ATOM 1046 N ALA A 134 33.318 7.463 23.823 1.00 31.30 ATOM 1047 CA ALA A 134 33.800 6.605 22.741 1.00 33.72 ATOM 1048 C ALA A 134 32.622 6.102 21.890 1.00 36.08 ATOM 1049 O ALA A 134 32.423 6.103 20.647 1.00 35.96 ATOM 1050 CB ALA A 134 34.529 5.397 23.285 1.00 31.65 ATOM 1051 N LEU A 135 31.656 5.661 22.700 1.00 34.15 ATOM 1052 CA LEU A 135 30.445 5.131 22.063 1.00 34.93 ATOM 1053 C LEU A 135 29.796 6.160 21.167 1.00 33.16 ATOM 1054 O LEU A 135 29.376 5.743 20.043 1.00 33.26 ATOM 1055 CB LEU A 135 29.680 4.547 23.238 1.00 39.50 ATOM 1056 CG LEU A 135 28.564 3.612 23.005 1.00 41.83 ATOM 1057 CD1 LEU A 135 28.801 2.802 21.706 1.00 47.69 ATOM 1058 CD2 LEU A 135 28.560 2.584 24.177 1.00 45.01 ATOM 1059 N ASP A 136 29.671 7.398 21.520 1.00 30.98 ATOM 1060 CA ASP A 136 29.034 8.489 20.776 1.00 32.77 ATOM 1061 C ASP A 136 29.795 8.762 19.419 1.00 33.00 ATOM 1062 O ASP A 136 29.090 9.043 18.463 1.00 32.16 ATOM 1063 CB ASP A 136 28.971 9.772 21.588 1.00 28.33 ATOM 1064 CG ASP A 136 28.260 10.882 20.962 1.00 25.93 ATOM 1065 OD1 ASP A 136 27.068 10.763 20.778 1.00 27.43 ATOM 1066 OD2 ASP A 136 28.822 11.936 20.566 1.00 26.00 ATOM 1067 N LYS A 137 31.093 8.708 19.609 1.00 34.67 ATOM 1068 CA LYS A 137 32.082 8.878 18.517 1.00 37.30 ATOM 1069 C LYS A 137 31.658 7.898 17.382 1.00 37.40 ATOM 1070 O LYS A 137 31.547 8.337 16.212 1.00 39.63 ATOM 1071 CB LYS A 137 33.465 8.503 18.836 1.00 39.09 ATOM 1072 CG LYS A 137 34.584 8.924 19.662 1.00 46.92 ATOM 1073 CD LYS A 137 35.710 9.768 19.032 1.00 49.26 ATOM 1074 CE LYS A 137 36.352 9.060 17.851 1.00 52.78 ATOM 1075 NZ LYS A 137 36.712 9.901 16.659 1.00 51.95 ATOM 1076 N GLU A 138 31.506 6.657 17.706 1.00 36.37 ATOM 1077 CA GLU A 138 31.131 5.567 16.792 1.00 38.49 ATOM 1078 C GLU A 138 29.771 5.708 16.157 1.00 38.52 ATOM 1079 O GLU A 138 29.541 5.565 14.852 1.00 39.03 ATOM 1080 CB GLU A 138 31.322 4.250 17.584 1.00 44.58 ATOM 1081 CG GLU A 138 31.231 2.942 16.852 1.00 55.47 ATOM 1082 CD GLU A 138 30.385 1.813 17.385 1.00 62.97 ATOM 1083 OE1 GLU A 138 30.769 1.052 18.312 1.00 67.50 ATOM 1084 OE2 GLU A 138 29.205 1.648 16.863 1.00 65.91 ATOM 1085 N LEU A 139 28.747 6.087 16.923 1.00 34.54 ATOM 1086 CA LEU A 139 27.379 6.218 16.456 1.00 31.46 ATOM 1087 C LEU A 139 27.255 7.428 15.568 1.00 30.26 ATOM 1088 O LEU A 139 26.443 7.412 14.653 1.00 28.42 ATOM 1089 CB LEU A 139 26.496 6.315 17.760 1.00 29.40 ATOM 1090 CG LEU A 139 26.319 4.913 18.331 1.00 31.35 ATOM 1091 CD1 LEU A 139 25.802 4.838 19.755 1.00 30.17 ATOM 1092 CD2 LEU A 139 25.261 4.245 17.425 1.00 31.91 ATOM 1093 N LYS A 140 27.915 8.488 15.908 1.00 30.18 ATOM 1094 CA LYS A 140 27.885 9.780 15.257 1.00 32.84 ATOM 1095 C LYS A 140 28.353 9.786 13.782 1.00 34.06 ATOM 1096 O LYS A 140 27.988 10.749 13.069 1.00 34.27 ATOM 1097 CB LYS A 140 28.795 10.733 16.063 1.00 34.78 ATOM 1098 CG LYS A 140 28.098 12.024 16.486 1.00 37.71 ATOM 1099 CD LYS A 140 27.192 11.899 17.633 1.00 40.28 ATOM 1100 CE LYS A 140 26.706 13.215 18.238 1.00 41.69 ATOM 1101 NZ LYS A 140 27.399 13.479 19.505 1.00 41.23 ATOM 1102 N ALA A 141 29.199 8.859 13.488 1.00 33.89 ATOM 1103 CA ALA A 141 29.829 8.499 12.246 1.00 37.28 ATOM 1104 C ALA A 141 28.768 7.876 11.334 1.00 39.10 ATOM 1105 O ALA A 141 28.751 7.767 10.058 1.00 39.46 ATOM 1106 CB ALA A 141 30.962 7.471 12.526 1.00 32.82 ATOM 1107 N LYS A 142 27.733 7.409 12.009 1.00 40.23 ATOM 1108 CA LYS A 142 26.545 6.718 11.422 1.00 39.72 ATOM 1109 C LYS A 142 25.279 7.568 11.480 1.00 37.42 ATOM 1110 O LYS A 142 24.146 7.027 11.255 1.00 38.80 ATOM 1111 CB LYS A 142 26.519 5.416 12.193 1.00 45.85 ATOM 1112 CG LYS A 142 25.419 4.444 12.319 1.00 52.15 ATOM 1113 CD LYS A 142 25.357 3.596 13.589 1.00 55.05 ATOM 1114 CE LYS A 142 26.666 3.127 14.222 1.00 56.87 ATOM 1115 NZ LYS A 142 26.426 1.746 14.801 1.00 58.67 ATOM 1116 N GLY A 143 25.377 8.849 11.717 1.00 33.77 ATOM 1117 CA GLY A 143 24.403 9.876 11.883 1.00 33.48 ATOM 1118 C GLY A 143 23.620 9.839 13.225 1.00 35.29 ATOM 1119 O GLY A 143 22.631 10.619 13.312 1.00 35.98 ATOM 1120 N LYS A 144 23.921 9.000 14.194 1.00 35.17 ATOM 1121 CA LYS A 144 23.218 8.844 15.491 1.00 35.16 ATOM 1122 C LYS A 144 24.012 9.459 16.644 1.00 35.75 ATOM 1123 O LYS A 144 24.980 10.225 16.415 1.00 38.19 ATOM 1124 CB LYS A 144 22.949 7.395 15.876 1.00 35.87 ATOM 1125 CG LYS A 144 22.443 6.460 14.823 1.00 35.99 ATOM 1126 CD LYS A 144 21.036 6.075 14.663 1.00 33.97 ATOM 1127 CE LYS A 144 20.180 7.068 13.925 1.00 38.75 ATOM 1128 NZ LYS A 144 19.044 6.314 13.281 1.00 38.43 ATOM 1129 N SER A 145 23.500 9.239 17.888 1.00 34.06 ATOM 1130 CA SER A 145 24.133 9.702 19.163 1.00 28.65 ATOM 1131 C SER A 145 23.901 8.582 20.223 1.00 23.82 ATOM 1132 O SER A 145 23.001 7.780 20.078 1.00 22.93 ATOM 1133 CB SER A 145 23.728 11.013 19.723 1.00 31.63 ATOM 1134 OG SER A 145 22.383 11.199 19.917 1.00 27.82 ATOM 1135 N ALA A 146 24.792 8.593 21.155 1.00 20.93 ATOM 1136 CA ALA A 146 24.775 7.628 22.196 1.00 19.86 ATOM 1137 C ALA A 146 23.649 7.892 23.204 1.00 19.94 ATOM 1138 O ALA A 146 23.000 6.951 23.609 1.00 21.08 ATOM 1139 CB ALA A 146 26.157 7.671 22.899 1.00 21.37 ATOM 1140 N LEU A 147 23.475 9.108 23.689 1.00 21.36 ATOM 1141 CA LEU A 147 22.561 9.427 24.770 1.00 21.37 ATOM 1142 C LEU A 147 21.951 10.756 24.782 1.00 22.34 ATOM 1143 O LEU A 147 22.687 11.779 24.540 1.00 25.69 ATOM 1144 CB LEU A 147 23.510 9.166 26.075 1.00 21.18 ATOM 1145 CG LEU A 147 22.834 9.704 27.401 1.00 19.46 ATOM 1146 CD1 LEU A 147 21.742 8.728 27.775 1.00 18.99 ATOM 1147 CD2 LEU A 147 23.874 9.666 28.476 1.00 22.26 ATOM 1148 N MET A 148 20.646 10.871 25.127 1.00 21.41 ATOM 1149 CA MET A 148 20.095 12.204 25.251 1.00 20.17 ATOM 1150 C MET A 148 19.099 12.118 26.386 1.00 19.47 ATOM 1151 O MET A 148 18.278 11.150 26.345 1.00 20.53 ATOM 1152 CB MET A 148 19.465 12.546 23.893 1.00 27.47 ATOM 1153 CG MET A 148 20.633 13.059 22.976 1.00 35.08 ATOM 1154 SD MET A 148 19.904 14.717 22.457 1.00 46.75 ATOM 1155 CE MET A 148 18.929 13.863 21.182 1.00 42.98 ATOM 1156 N PHE A 149 19.129 13.060 27.285 1.00 18.88 ATOM 1157 CA PHE A 149 18.078 12.987 28.421 1.00 19.68 ATOM 1158 C PHE A 149 17.851 14.415 28.854 1.00 18.60 ATOM 1159 O PHE A 149 18.684 15.375 28.532 1.00 19.25 ATOM 1160 CB PHE A 149 18.515 12.014 29.546 1.00 19.01 ATOM 1161 CG PHE A 149 19.710 12.438 30.282 1.00 20.43 ATOM 1162 CD1 PHE A 149 21.015 12.177 29.802 1.00 21.31 ATOM 1163 CD2 PHE A 149 19.544 13.190 31.466 1.00 20.80 ATOM 1164 CE1 PHE A 149 22.206 12.535 30.425 1.00 21.32 ATOM 1165 CE2 PHE A 149 20.727 13.522 32.140 1.00 21.42 ATOM 1166 CZ PHE A 149 22.064 13.274 31.626 1.00 23.43 ATOM 1167 N ASN A 150 16.797 14.626 29.603 1.00 19.32 ATOM 1168 CA ASN A 150 16.416 15.963 30.070 1.00 20.03 ATOM 1169 C ASN A 150 17.490 16.600 30.962 1.00 22.66 ATOM 1170 O ASN A 150 17.538 16.189 32.149 1.00 24.25 ATOM 1171 CB ASN A 150 15.083 15.914 30.815 1.00 19.28 ATOM 1172 CG ASN A 150 14.534 17.258 31.189 1.00 18.73 ATOM 1173 OD1 ASN A 150 15.109 18.351 30.884 1.00 20.25 ATOM 1174 ND2 ASN A 150 13.400 17.371 31.846 1.00 16.14 ATOM 1175 N LEU A 151 18.162 17.657 30.553 1.00 20.81 ATOM 1176 CA LEU A 151 19.160 18.367 31.294 1.00 21.48 ATOM 1177 C LEU A 151 18.607 19.600 32.032 1.00 19.34 ATOM 1178 O LEU A 151 19.390 20.171 32.835 1.00 22.89 ATOM 1179 CB LEU A 151 20.364 18.788 30.381 1.00 25.44 ATOM 1180 CG LEU A 151 21.236 17.826 29.682 1.00 23.21 ATOM 1181 CD1 LEU A 151 22.403 18.619 29.067 1.00 26.52 ATOM 1182 CD2 LEU A 151 21.863 16.771 30.613 1.00 26.43 ATOM 1183 N GLN A 152 17.396 19.936 31.792 1.00 19.02 ATOM 1184 CA GLN A 152 16.756 21.068 32.351 1.00 18.15 ATOM 1185 C GLN A 152 16.245 20.741 33.763 1.00 19.90 ATOM 1186 O GLN A 152 16.090 21.729 34.538 1.00 21.14 ATOM 1187 CB GLN A 152 15.589 21.588 31.512 1.00 19.90 ATOM 1188 CG GLN A 152 16.003 21.983 30.072 1.00 22.68 ATOM 1189 CD GLN A 152 17.369 22.594 29.985 1.00 29.43 ATOM 1190 OE1 GLN A 152 17.703 23.649 30.614 1.00 32.52 ATOM 1191 NE2 GLN A 152 18.280 21.940 29.258 1.00 29.24 ATOM 1192 N GLU A 153 15.950 19.566 34.152 1.00 19.66 ATOM 1193 CA GLU A 153 15.435 19.056 35.492 1.00 18.94 ATOM 1194 C GLU A 153 16.489 18.289 36.268 1.00 15.92 ATOM 1195 O GLU A 153 16.988 17.255 35.745 1.00 14.78 ATOM 1196 CB GLU A 153 14.168 18.215 35.200 1.00 17.08 ATOM 1197 CG GLU A 153 12.916 19.120 35.085 1.00 19.50 ATOM 1198 CD GLU A 153 12.481 19.954 36.237 1.00 23.65 ATOM 1199 OE1 GLU A 153 12.974 19.921 37.378 1.00 26.26 ATOM 1200 OE2 GLU A 153 11.689 20.876 36.066 1.00 28.40 ATOM 1201 N PRO A 154 16.875 18.840 37.451 1.00 16.54 ATOM 1202 CA PRO A 154 17.996 18.313 38.233 1.00 17.66 ATOM 1203 C PRO A 154 17.848 16.878 38.632 1.00 17.05 ATOM 1204 O PRO A 154 18.799 16.177 38.912 1.00 15.56 ATOM 1205 CB PRO A 154 18.201 19.321 39.422 1.00 16.88 ATOM 1206 CG PRO A 154 16.893 20.069 39.596 1.00 14.65 ATOM 1207 CD PRO A 154 16.372 20.097 38.096 1.00 16.95 ATOM 1208 N TYR A 155 16.560 16.473 38.633 1.00 17.84 ATOM 1209 CA TYR A 155 16.161 15.098 38.967 1.00 17.52 ATOM 1210 C TYR A 155 16.866 14.065 38.016 1.00 17.68 ATOM 1211 O TYR A 155 17.290 13.006 38.534 1.00 15.47 ATOM 1212 CB TYR A 155 14.683 14.891 38.778 1.00 15.96 ATOM 1213 CG TYR A 155 14.044 13.567 39.058 1.00 17.22 ATOM 1214 CD1 TYR A 155 13.805 13.113 40.408 1.00 15.10 ATOM 1215 CD2 TYR A 155 13.636 12.713 38.019 1.00 15.47 ATOM 1216 CE1 TYR A 155 13.150 11.942 40.613 1.00 12.71 ATOM 1217 CE2 TYR A 155 12.912 11.556 38.245 1.00 18.63 ATOM 1218 CZ TYR A 155 12.684 11.121 39.606 1.00 16.35 ATOM 1219 OH TYR A 155 12.033 9.935 39.696 1.00 14.77 ATOM 1220 N PHE A 156 17.083 14.498 36.771 1.00 17.87 ATOM 1221 CA PHE A 156 17.662 13.542 35.740 1.00 18.74 ATOM 1222 C PHE A 156 19.169 13.375 35.796 1.00 15.96 ATOM 1223 O PHE A 156 19.715 12.297 35.517 1.00 16.44 ATOM 1224 CB PHE A 156 17.109 14.011 34.371 1.00 16.91 ATOM 1225 CG PHE A 156 15.678 13.760 34.189 1.00 14.20 ATOM 1226 CD1 PHE A 156 15.292 12.566 33.622 1.00 15.82 ATOM 1227 CD2 PHE A 156 14.751 14.773 34.473 1.00 14.97 ATOM 1228 CE1 PHE A 156 13.947 12.297 33.394 1.00 16.32 ATOM 1229 CE2 PHE A 156 13.385 14.475 34.326 1.00 17.43 ATOM 1230 CZ PHE A 156 13.018 13.251 33.761 1.00 15.10 ATOM 1231 N THR A 157 19.730 14.511 36.248 1.00 16.55 ATOM 1232 CA THR A 157 21.187 14.607 36.451 1.00 19.13 ATOM 1233 C THR A 157 21.685 14.160 37.857 1.00 18.04 ATOM 1234 O THR A 157 22.863 13.801 37.917 1.00 16.39 ATOM 1235 CB THR A 157 21.713 16.042 36.071 1.00 19.65 ATOM 1236 OG1 THR A 157 20.925 17.040 36.805 1.00 24.06 ATOM 1237 CG2 THR A 157 21.573 16.240 34.565 1.00 18.96 ATOM 1238 N TRP A 158 20.879 14.247 38.927 1.00 15.63 ATOM 1239 CA TRP A 158 21.282 13.853 40.256 1.00 13.96 ATOM 1240 C TRP A 158 21.878 12.517 40.319 1.00 12.85 ATOM 1241 O TRP A 158 22.886 12.381 41.060 1.00 14.31 ATOM 1242 CB TRP A 158 19.973 13.879 41.152 1.00 16.97 ATOM 1243 CG TRP A 158 20.410 13.643 42.566 1.00 17.27 ATOM 1244 CD1 TRP A 158 20.221 12.506 43.308 1.00 17.36 ATOM 1245 CD2 TRP A 158 21.188 14.562 43.352 1.00 17.58 ATOM 1246 NE1 TRP A 158 20.794 12.674 44.560 1.00 18.30 ATOM 1247 CE2 TRP A 158 21.418 13.919 44.600 1.00 17.36 ATOM 1248 CE3 TRP A 158 21.714 15.844 43.096 1.00 15.95 ATOM 1249 CZ2 TRP A 158 22.097 14.537 45.619 1.00 16.45 ATOM 1250 CZ3 TRP A 158 22.511 16.413 44.081 1.00 16.21 ATOM 1251 CH2 TRP A 158 22.637 15.773 45.353 1.00 18.62 ATOM 1252 N PRO A 159 21.496 11.456 39.651 1.00 14.65 ATOM 1253 CA PRO A 159 22.179 10.139 39.824 1.00 15.35 ATOM 1254 C PRO A 159 23.664 10.138 39.596 1.00 17.00 ATOM 1255 O PRO A 159 24.461 9.407 40.229 1.00 15.38 ATOM 1256 CB PRO A 159 21.464 9.187 38.852 1.00 17.35 ATOM 1257 CG PRO A 159 20.227 9.897 38.347 1.00 14.75 ATOM 1258 CD PRO A 159 20.306 11.344 38.763 1.00 13.38 ATOM 1259 N LEU A 160 24.125 10.963 38.636 1.00 16.15 ATOM 1260 CA LEU A 160 25.553 11.047 38.332 1.00 17.64 ATOM 1261 C LEU A 160 26.295 11.886 39.399 1.00 19.03 ATOM 1262 O LEU A 160 27.464 11.657 39.732 1.00 17.80 ATOM 1263 CB LEU A 160 25.708 11.732 36.951 1.00 19.59 ATOM 1264 CG LEU A 160 26.820 11.568 35.979 1.00 24.01 ATOM 1265 CD1 LEU A 160 27.009 12.822 35.144 1.00 23.52 ATOM 1266 CD2 LEU A 160 28.131 11.016 36.464 1.00 21.49 ATOM 1267 N ILE A 161 25.607 12.985 39.831 1.00 17.61 ATOM 1268 CA ILE A 161 26.181 13.856 40.870 1.00 19.06 ATOM 1269 C ILE A 161 26.339 13.119 42.200 1.00 15.48 ATOM 1270 O ILE A 161 27.359 13.193 42.932 1.00 17.73 ATOM 1271 CB ILE A 161 25.277 15.153 41.048 1.00 19.32 ATOM 1272 CG1 ILE A 161 25.427 15.948 39.723 1.00 17.80 ATOM 1273 CG2 ILE A 161 25.638 15.949 42.317 1.00 17.58 ATOM 1274 CD1 ILE A 161 24.445 17.147 39.579 1.00 26.58 ATOM 1275 N ALA A 162 25.351 12.363 42.506 1.00 16.22 ATOM 1276 CA ALA A 162 25.404 11.598 43.751 1.00 15.36 ATOM 1277 C ALA A 162 26.294 10.402 43.617 1.00 18.02 ATOM 1278 O ALA A 162 26.746 9.939 44.710 1.00 18.02 ATOM 1279 CB ALA A 162 23.991 11.152 44.030 1.00 13.85 ATOM 1280 N ALA A 163 26.625 9.758 42.465 1.00 15.72 ATOM 1281 CA ALA A 163 27.381 8.530 42.375 1.00 14.97 ATOM 1282 C ALA A 163 28.645 8.449 43.163 1.00 16.66 ATOM 1283 O ALA A 163 28.884 7.475 43.916 1.00 16.94 ATOM 1284 CB ALA A 163 27.709 8.320 40.824 1.00 16.08 ATOM 1285 N ASP A 164 29.545 9.407 43.027 1.00 18.03 ATOM 1286 CA ASP A 164 30.852 9.452 43.690 1.00 20.53 ATOM 1287 C ASP A 164 30.766 10.218 45.023 1.00 22.27 ATOM 1288 O ASP A 164 31.848 10.567 45.554 1.00 21.20 ATOM 1289 CB ASP A 164 31.915 10.029 42.724 1.00 21.07 ATOM 1290 CG ASP A 164 33.364 9.854 43.220 1.00 25.94 ATOM 1291 OD1 ASP A 164 33.696 8.790 43.729 1.00 26.99 ATOM 1292 OD2 ASP A 164 34.043 10.944 43.108 1.00 28.83 ATOM 1293 N GLY A 165 29.579 10.475 45.565 1.00 23.05 ATOM 1294 CA GLY A 165 29.453 11.145 46.880 1.00 20.68 ATOM 1295 C GLY A 165 28.612 12.336 46.997 1.00 21.01 ATOM 1296 O GLY A 165 28.681 12.788 48.176 1.00 21.59 ATOM 1297 N GLY A 166 28.003 12.989 46.016 1.00 18.67 ATOM 1298 CA GLY A 166 27.192 14.211 46.280 1.00 18.91 ATOM 1299 C GLY A 166 26.043 13.782 47.120 1.00 18.36 ATOM 1300 O GLY A 166 25.593 12.616 47.113 1.00 17.37 ATOM 1301 N TYR A 167 25.458 14.694 47.900 1.00 19.38 ATOM 1302 CA TYR A 167 24.266 14.299 48.741 1.00 18.48 ATOM 1303 C TYR A 167 23.469 15.565 49.068 1.00 18.17 ATOM 1304 O TYR A 167 24.098 16.657 48.969 1.00 19.60 ATOM 1305 CB TYR A 167 24.541 13.501 50.036 1.00 17.22 ATOM 1306 CG TYR A 167 25.450 14.158 51.046 1.00 18.37 ATOM 1307 CD1 TYR A 167 24.844 15.002 52.014 1.00 14.44 ATOM 1308 CD2 TYR A 167 26.834 13.891 51.017 1.00 16.39 ATOM 1309 CE1 TYR A 167 25.681 15.613 52.940 1.00 16.23 ATOM 1310 CE2 TYR A 167 27.662 14.520 51.975 1.00 18.28 ATOM 1311 CZ TYR A 167 27.009 15.305 52.965 1.00 16.57 ATOM 1312 OH TYR A 167 27.859 15.955 53.867 1.00 17.88 ATOM 1313 N ALA A 168 22.184 15.399 49.329 1.00 16.38 ATOM 1314 CA ALA A 168 21.333 16.559 49.663 1.00 17.55 ATOM 1315 C ALA A 168 21.587 17.005 51.112 1.00 16.43 ATOM 1316 O ALA A 168 22.267 17.998 51.343 1.00 16.71 ATOM 1317 CB ALA A 168 19.851 16.252 49.280 1.00 15.16 ATOM 1318 N PHE A 169 21.019 16.376 52.087 1.00 16.65 ATOM 1319 CA PHE A 169 21.056 16.599 53.545 1.00 18.18 ATOM 1320 C PHE A 169 21.531 15.291 54.210 1.00 18.73 ATOM 1321 O PHE A 169 21.146 14.178 53.787 1.00 20.00 ATOM 1322 CB PHE A 169 19.641 17.044 54.041 1.00 17.00 ATOM 1323 CG PHE A 169 19.187 18.317 53.366 1.00 21.24 ATOM 1324 CD1 PHE A 169 19.772 19.566 53.711 1.00 19.53 ATOM 1325 CD2 PHE A 169 18.146 18.304 52.397 1.00 20.17 ATOM 1326 CE1 PHE A 169 19.346 20.727 53.120 1.00 20.94 ATOM 1327 CE2 PHE A 169 17.771 19.465 51.706 1.00 18.36 ATOM 1328 CZ PHE A 169 18.322 20.665 52.128 1.00 21.41 ATOM 1329 N LYS A 170 22.466 15.432 55.067 1.00 16.42 ATOM 1330 CA LYS A 170 23.008 14.346 55.852 1.00 19.52 ATOM 1331 C LYS A 170 21.893 13.922 56.854 1.00 25.16 ATOM 1332 O LYS A 170 21.265 14.817 57.443 1.00 23.27 ATOM 1333 CB LYS A 170 24.218 14.756 56.642 1.00 18.39 ATOM 1334 CG LYS A 170 24.945 13.675 57.369 1.00 24.00 ATOM 1335 CD LYS A 170 25.676 12.689 56.481 1.00 28.25 ATOM 1336 CE LYS A 170 26.993 13.220 55.939 1.00 32.53 ATOM 1337 NZ LYS A 170 27.822 14.096 56.841 1.00 30.72 ATOM 1338 N TYR A 171 21.622 12.627 56.863 1.00 27.38 ATOM 1339 CA TYR A 171 20.700 11.975 57.710 1.00 34.77 ATOM 1340 C TYR A 171 21.521 11.621 58.989 1.00 39.14 ATOM 1341 O TYR A 171 22.473 10.809 58.911 1.00 41.35 ATOM 1342 CB TYR A 171 20.113 10.697 57.096 1.00 40.41 ATOM 1343 CG TYR A 171 19.030 10.240 58.058 1.00 48.20 ATOM 1344 CD1 TYR A 171 17.815 10.947 58.096 1.00 50.76 ATOM 1345 CD2 TYR A 171 19.231 9.224 58.990 1.00 52.69 ATOM 1346 CE1 TYR A 171 16.764 10.560 58.916 1.00 54.59 ATOM 1347 CE2 TYR A 171 18.202 8.852 59.897 1.00 55.71 ATOM 1348 CZ TYR A 171 16.972 9.509 59.842 1.00 57.07 ATOM 1349 OH TYR A 171 15.972 9.199 60.751 1.00 59.64 ATOM 1350 N GLU A 172 21.286 12.262 60.119 1.00 41.29 ATOM 1351 CA GLU A 172 22.138 11.971 61.270 1.00 44.84 ATOM 1352 C GLU A 172 21.301 11.846 62.516 1.00 49.78 ATOM 1353 O GLU A 172 20.620 12.859 62.879 1.00 50.32 ATOM 1354 CB GLU A 172 23.021 13.212 61.453 1.00 44.88 ATOM 1355 CG GLU A 172 23.795 13.137 62.802 1.00 47.17 ATOM 1356 CD GLU A 172 24.821 12.015 62.751 1.00 49.17 ATOM 1357 OE1 GLU A 172 25.156 11.364 61.748 1.00 49.86 ATOM 1358 OE2 GLU A 172 25.274 11.902 63.912 1.00 49.72 ATOM 1359 N ASN A 173 21.279 10.674 63.123 1.00 54.43 ATOM 1360 CA ASN A 173 20.508 10.338 64.364 1.00 56.20 ATOM 1361 C ASN A 173 19.044 10.803 64.308 1.00 54.73 ATOM 1362 O ASN A 173 18.562 11.819 64.886 1.00 53.96 ATOM 1363 CB ASN A 173 21.273 10.719 65.605 1.00 61.89 ATOM 1364 CG ASN A 173 20.796 11.858 66.455 1.00 66.68 ATOM 1365 OD1 ASN A 173 20.584 11.689 67.707 1.00 69.43 ATOM 1366 ND2 ASN A 173 20.627 13.056 65.859 1.00 68.20 ATOM 1367 N GLY A 174 18.315 9.956 63.541 1.00 53.11 ATOM 1368 CA GLY A 174 16.875 10.139 63.369 1.00 51.08 ATOM 1369 C GLY A 174 16.386 11.368 62.602 1.00 48.26 ATOM 1370 O GLY A 174 15.144 11.513 62.392 1.00 47.86 ATOM 1371 N LYS A 175 17.379 12.205 62.204 1.00 43.97 ATOM 1372 CA LYS A 175 16.866 13.341 61.398 1.00 39.57 ATOM 1373 C LYS A 175 17.946 13.869 60.487 1.00 34.32 ATOM 1374 O LYS A 175 19.106 13.543 60.446 1.00 32.03 ATOM 1375 CB LYS A 175 16.086 14.224 62.334 1.00 45.04 ATOM 1376 CG LYS A 175 16.595 15.514 62.855 1.00 48.29 ATOM 1377 CD LYS A 175 17.353 15.337 64.160 1.00 53.19 ATOM 1378 CE LYS A 175 18.181 16.637 64.329 1.00 57.90 ATOM 1379 NZ LYS A 175 17.122 17.755 64.454 1.00 60.97 ATOM 1380 N TYR A 176 17.443 14.712 59.567 1.00 32.03 ATOM 1381 CA TYR A 176 18.196 15.411 58.561 1.00 27.31 ATOM 1382 C TYR A 176 18.776 16.704 59.166 1.00 26.63 ATOM 1383 O TYR A 176 17.971 17.515 59.661 1.00 24.94 ATOM 1384 CB TYR A 176 17.288 15.832 57.367 1.00 26.98 ATOM 1385 CG TYR A 176 17.036 14.617 56.476 1.00 25.30 ATOM 1386 CD1 TYR A 176 18.012 14.074 55.674 1.00 24.47 ATOM 1387 CD2 TYR A 176 15.766 14.021 56.564 1.00 26.58 ATOM 1388 CE1 TYR A 176 17.762 12.921 54.942 1.00 26.71 ATOM 1389 CE2 TYR A 176 15.481 12.848 55.834 1.00 24.27 ATOM 1390 CZ TYR A 176 16.495 12.337 55.048 1.00 26.88 ATOM 1391 OH TYR A 176 16.194 11.177 54.359 1.00 30.46 ATOM 1392 N ASP A 177 20.082 16.824 58.975 1.00 22.24 ATOM 1393 CA ASP A 177 20.814 18.013 59.325 1.00 21.72 ATOM 1394 C ASP A 177 20.753 18.954 58.071 1.00 22.98 ATOM 1395 O ASP A 177 21.354 18.758 56.974 1.00 22.36 ATOM 1396 CB ASP A 177 22.220 17.695 59.810 1.00 20.48 ATOM 1397 CG ASP A 177 23.032 18.858 60.287 1.00 20.00 ATOM 1398 OD1 ASP A 177 22.716 20.037 59.984 1.00 21.11 ATOM 1399 OD2 ASP A 177 24.135 18.666 60.930 1.00 23.61 ATOM 1400 N ILE A 178 19.989 20.013 58.268 1.00 20.56 ATOM 1401 CA ILE A 178 19.766 21.042 57.269 1.00 21.01 ATOM 1402 C ILE A 178 20.967 21.920 56.971 1.00 22.14 ATOM 1403 O ILE A 178 21.050 22.651 55.914 1.00 21.96 ATOM 1404 CB ILE A 178 18.445 21.830 57.588 1.00 25.30 ATOM 1405 CG1 ILE A 178 18.564 22.717 58.859 1.00 26.02 ATOM 1406 CG2 ILE A 178 17.192 20.878 57.640 1.00 25.59 ATOM 1407 CD1 ILE A 178 17.646 24.020 58.690 1.00 28.97 ATOM 1408 N LYS A 179 21.992 21.788 57.825 1.00 21.35 ATOM 1409 CA LYS A 179 23.180 22.617 57.631 1.00 20.35 ATOM 1410 C LYS A 179 24.258 21.738 57.060 1.00 20.36 ATOM 1411 O LYS A 179 25.280 22.337 56.786 1.00 21.95 ATOM 1412 CB LYS A 179 23.638 23.216 58.950 1.00 25.32 ATOM 1413 CG LYS A 179 22.688 24.299 59.603 1.00 23.83 ATOM 1414 CD LYS A 179 22.345 25.314 58.528 1.00 29.38 ATOM 1415 CE LYS A 179 21.955 26.665 59.042 1.00 34.12 ATOM 1416 NZ LYS A 179 20.908 27.283 58.140 1.00 39.01 ATOM 1417 N ASP A 180 24.072 20.437 56.978 1.00 19.40 ATOM 1418 CA ASP A 180 25.063 19.533 56.391 1.00 18.28 ATOM 1419 C ASP A 180 24.538 19.080 54.989 1.00 18.53 ATOM 1420 O ASP A 180 23.811 18.154 54.817 1.00 19.18 ATOM 1421 CB ASP A 180 25.449 18.394 57.364 1.00 19.14 ATOM 1422 CG ASP A 180 26.481 17.392 56.828 1.00 18.04 ATOM 1423 OD1 ASP A 180 26.880 17.564 55.617 1.00 20.66 ATOM 1424 OD2 ASP A 180 26.948 16.443 57.488 1.00 19.45 ATOM 1425 N VAL A 181 25.057 19.779 53.930 1.00 18.25 ATOM 1426 CA VAL A 181 24.697 19.586 52.544 1.00 19.42 ATOM 1427 C VAL A 181 25.834 19.026 51.699 1.00 20.26 ATOM 1428 O VAL A 181 27.009 19.418 51.956 1.00 22.09 ATOM 1429 CB VAL A 181 24.099 20.952 52.017 1.00 19.84 ATOM 1430 CG1 VAL A 181 23.872 21.080 50.545 1.00 23.06 ATOM 1431 CG2 VAL A 181 22.789 21.337 52.784 1.00 22.24 ATOM 1432 N GLY A 182 25.633 18.200 50.654 1.00 19.30 ATOM 1433 CA GLY A 182 26.819 17.629 49.970 1.00 17.47 ATOM 1434 C GLY A 182 26.757 17.866 48.524 1.00 18.58 ATOM 1435 O GLY A 182 27.109 17.019 47.727 1.00 17.93 ATOM 1436 N VAL A 183 26.403 19.155 48.304 1.00 18.41 ATOM 1437 CA VAL A 183 26.238 19.575 46.845 1.00 19.05 ATOM 1438 C VAL A 183 27.515 20.123 46.325 1.00 21.56 ATOM 1439 O VAL A 183 27.725 20.097 45.088 1.00 23.71 ATOM 1440 CB VAL A 183 25.042 20.465 46.499 1.00 18.11 ATOM 1441 CG1 VAL A 183 23.680 20.025 47.026 1.00 16.33 ATOM 1442 CG2 VAL A 183 25.180 21.883 46.833 1.00 21.20 ATOM 1443 N ASP A 184 28.429 20.500 47.148 1.00 22.46 ATOM 1444 CA ASP A 184 29.700 21.035 46.686 1.00 21.61 ATOM 1445 C ASP A 184 30.872 20.210 47.112 1.00 21.88 ATOM 1446 O ASP A 184 32.024 20.769 47.251 1.00 25.88 ATOM 1447 CB ASP A 184 29.676 22.474 47.278 1.00 24.20 ATOM 1448 CG ASP A 184 30.870 23.211 46.797 1.00 28.76 ATOM 1449 OD1 ASP A 184 31.254 22.939 45.588 1.00 34.87 ATOM 1450 OD2 ASP A 184 31.463 24.010 47.498 1.00 31.18 ATOM 1451 N ASN A 185 30.674 18.972 47.483 1.00 20.12 ATOM 1452 CA ASN A 185 31.863 18.174 47.932 1.00 18.13 ATOM 1453 C ASN A 185 32.600 17.575 46.686 1.00 19.20 ATOM 1454 O ASN A 185 32.236 17.820 45.491 1.00 18.29 ATOM 1455 CB ASN A 185 31.324 17.188 48.976 1.00 20.37 ATOM 1456 CG ASN A 185 30.421 16.095 48.566 1.00 22.20 ATOM 1457 OD1 ASN A 185 30.299 15.777 47.303 1.00 22.18 ATOM 1458 ND2 ASN A 185 29.713 15.385 49.419 1.00 21.74 ATOM 1459 N ALA A 186 33.662 16.836 46.929 1.00 17.44 ATOM 1460 CA ALA A 186 34.482 16.287 45.862 1.00 19.37 ATOM 1461 C ALA A 186 33.638 15.350 45.002 1.00 19.66 ATOM 1462 O ALA A 186 33.935 15.386 43.754 1.00 22.04 ATOM 1463 CB ALA A 186 35.744 15.595 46.440 1.00 18.22 ATOM 1464 N GLY A 187 32.725 14.550 45.439 1.00 17.85 ATOM 1465 CA GLY A 187 31.970 13.637 44.538 1.00 18.40 ATOM 1466 C GLY A 187 31.026 14.327 43.632 1.00 16.98 ATOM 1467 O GLY A 187 30.782 13.974 42.446 1.00 16.61 ATOM 1468 N ALA A 188 30.375 15.325 44.210 1.00 16.28 ATOM 1469 CA ALA A 188 29.435 16.165 43.476 1.00 16.04 ATOM 1470 C ALA A 188 30.194 16.946 42.364 1.00 18.67 ATOM 1471 O ALA A 188 29.673 16.980 41.173 1.00 18.92 ATOM 1472 CB ALA A 188 28.704 17.121 44.403 1.00 16.65 ATOM 1473 N LYS A 189 31.341 17.500 42.716 1.00 18.63 ATOM 1474 CA LYS A 189 32.166 18.215 41.705 1.00 20.48 ATOM 1475 C LYS A 189 32.641 17.227 40.572 1.00 20.71 ATOM 1476 O LYS A 189 32.599 17.614 39.310 1.00 18.91 ATOM 1477 CB LYS A 189 33.410 18.941 42.250 1.00 17.18 ATOM 1478 CG LYS A 189 32.930 20.175 43.085 1.00 17.51 ATOM 1479 CD LYS A 189 34.120 20.844 43.813 1.00 18.61 ATOM 1480 CE LYS A 189 35.007 19.843 44.441 1.00 20.99 ATOM 1481 NZ LYS A 189 35.885 20.437 45.591 1.00 22.95 ATOM 1482 N ALA A 190 33.056 16.039 40.884 1.00 18.62 ATOM 1483 CA ALA A 190 33.535 15.067 39.872 1.00 19.71 ATOM 1484 C ALA A 190 32.420 14.717 38.862 1.00 19.64 ATOM 1485 O ALA A 190 32.689 14.678 37.660 1.00 18.88 ATOM 1486 CB ALA A 190 33.954 13.820 40.570 1.00 16.94 ATOM 1487 N GLY A 191 31.202 14.521 39.422 1.00 16.97 ATOM 1488 CA GLY A 191 29.984 14.197 38.709 1.00 18.06 ATOM 1489 C GLY A 191 29.537 15.241 37.725 1.00 18.40 ATOM 1490 O GLY A 191 29.368 14.940 36.515 1.00 15.97 ATOM 1491 N LEU A 192 29.409 16.502 38.241 1.00 19.22 ATOM 1492 CA LEU A 192 29.016 17.585 37.313 1.00 20.21 ATOM 1493 C LEU A 192 30.080 17.875 36.236 1.00 20.74 ATOM 1494 O LEU A 192 29.798 18.302 35.086 1.00 20.92 ATOM 1495 CB LEU A 192 28.551 18.781 38.210 1.00 22.81 ATOM 1496 CG LEU A 192 27.905 19.929 37.362 1.00 22.73 ATOM 1497 CD1 LEU A 192 26.677 19.397 36.587 1.00 22.91 ATOM 1498 CD2 LEU A 192 27.515 21.049 38.291 1.00 24.30 ATOM 1499 N THR A 193 31.343 17.751 36.611 1.00 21.29 ATOM 1500 CA THR A 193 32.469 17.989 35.683 1.00 22.73 ATOM 1501 C THR A 193 32.364 17.037 34.485 1.00 23.30 ATOM 1502 O THR A 193 32.483 17.439 33.377 1.00 22.21 ATOM 1503 CB THR A 193 33.882 17.713 36.317 1.00 24.68 ATOM 1504 OG1 THR A 193 34.002 18.881 37.214 1.00 23.91 ATOM 1505 CG2 THR A 193 35.033 17.631 35.297 1.00 23.78 ATOM 1506 N PHE A 194 32.163 15.808 34.779 1.00 22.25 ATOM 1507 CA PHE A 194 31.954 14.732 33.813 1.00 22.42 ATOM 1508 C PHE A 194 30.786 15.145 32.925 1.00 22.56 ATOM 1509 O PHE A 194 30.917 14.861 31.695 1.00 21.88 ATOM 1510 CB PHE A 194 31.707 13.338 34.398 1.00 23.49 ATOM 1511 CG PHE A 194 31.635 12.266 33.337 1.00 25.80 ATOM 1512 CD1 PHE A 194 32.827 11.713 32.864 1.00 26.27 ATOM 1513 CD2 PHE A 194 30.350 11.921 32.828 1.00 27.23 ATOM 1514 CE1 PHE A 194 32.760 10.780 31.789 1.00 27.24 ATOM 1515 CE2 PHE A 194 30.293 10.979 31.792 1.00 26.67 ATOM 1516 CZ PHE A 194 31.510 10.442 31.297 1.00 25.95 ATOM 1517 N LEU A 195 29.702 15.575 33.412 1.00 20.76 ATOM 1518 CA LEU A 195 28.586 15.967 32.585 1.00 22.60 ATOM 1519 C LEU A 195 28.960 17.140 31.633 1.00 20.42 ATOM 1520 O LEU A 195 28.503 17.178 30.488 1.00 21.34 ATOM 1521 CB LEU A 195 27.386 16.367 33.515 1.00 23.97 ATOM 1522 CG LEU A 195 26.119 16.795 32.681 1.00 27.45 ATOM 1523 CD1 LEU A 195 25.491 15.631 31.968 1.00 26.97 ATOM 1524 CD2 LEU A 195 25.180 17.545 33.634 1.00 25.98 ATOM 1525 N VAL A 196 29.548 18.157 32.147 1.00 21.83 ATOM 1526 CA VAL A 196 29.912 19.390 31.456 1.00 24.71 ATOM 1527 C VAL A 196 30.907 19.006 30.345 1.00 25.11 ATOM 1528 O VAL A 196 30.929 19.557 29.242 1.00 23.53 ATOM 1529 CB VAL A 196 30.409 20.458 32.492 1.00 24.75 ATOM 1530 CG1 VAL A 196 30.932 21.698 31.722 1.00 23.63 ATOM 1531 CG2 VAL A 196 29.360 20.860 33.452 1.00 24.70 ATOM 1532 N ASP A 197 31.781 18.037 30.615 1.00 25.17 ATOM 1533 CA ASP A 197 32.770 17.598 29.661 1.00 27.74 ATOM 1534 C ASP A 197 32.070 16.931 28.453 1.00 29.03 ATOM 1535 O ASP A 197 32.583 17.017 27.334 1.00 25.83 ATOM 1536 CB ASP A 197 33.779 16.716 30.284 1.00 32.08 ATOM 1537 CG ASP A 197 35.024 17.351 30.856 1.00 38.43 ATOM 1538 OD1 ASP A 197 35.246 18.586 30.967 1.00 40.92 ATOM 1539 OD2 ASP A 197 35.808 16.442 31.331 1.00 43.30 ATOM 1540 N LEU A 198 30.954 16.270 28.677 1.00 28.16 ATOM 1541 CA LEU A 198 30.153 15.593 27.671 1.00 28.86 ATOM 1542 C LEU A 198 29.652 16.639 26.676 1.00 29.29 ATOM 1543 O LEU A 198 29.659 16.376 25.486 1.00 32.61 ATOM 1544 CB LEU A 198 28.990 14.847 28.282 1.00 26.82 ATOM 1545 CG LEU A 198 29.213 13.467 28.867 1.00 27.84 ATOM 1546 CD1 LEU A 198 27.845 12.946 29.346 1.00 28.48 ATOM 1547 CD2 LEU A 198 29.798 12.467 27.855 1.00 27.80 ATOM 1548 N ILE A 199 29.230 17.720 27.240 1.00 29.17 ATOM 1549 CA ILE A 199 28.727 18.831 26.457 1.00 30.02 ATOM 1550 C ILE A 199 29.897 19.530 25.768 1.00 33.01 ATOM 1551 O ILE A 199 29.855 19.744 24.550 1.00 33.16 ATOM 1552 CB ILE A 199 27.920 19.791 27.357 1.00 29.00 ATOM 1553 CG1 ILE A 199 26.656 19.061 27.891 1.00 26.86 ATOM 1554 CG2 ILE A 199 27.606 21.079 26.561 1.00 28.03 ATOM 1555 CD1 ILE A 199 26.021 19.861 29.111 1.00 29.10 ATOM 1556 N LYS A 200 30.876 19.915 26.508 1.00 33.49 ATOM 1557 CA LYS A 200 32.057 20.580 25.999 1.00 37.48 ATOM 1558 C LYS A 200 32.506 19.948 24.684 1.00 37.91 ATOM 1559 O LYS A 200 32.868 20.683 23.724 1.00 39.27 ATOM 1560 CB LYS A 200 33.303 20.311 26.886 1.00 41.99 ATOM 1561 CG LYS A 200 34.113 21.505 27.353 1.00 46.64 ATOM 1562 CD LYS A 200 33.313 22.176 28.472 1.00 51.19 ATOM 1563 CE LYS A 200 33.962 23.218 29.357 1.00 52.17 ATOM 1564 NZ LYS A 200 32.947 24.291 29.752 1.00 52.63 ATOM 1565 N ASN A 201 32.614 18.643 24.753 1.00 35.61 ATOM 1566 CA ASN A 201 33.138 17.756 23.696 1.00 34.84 ATOM 1567 C ASN A 201 32.106 17.295 22.691 1.00 33.01 ATOM 1568 O ASN A 201 32.260 16.264 22.003 1.00 34.31 ATOM 1569 CB ASN A 201 33.916 16.597 24.358 1.00 35.80 ATOM 1570 CG ASN A 201 35.257 17.049 24.941 1.00 40.07 ATOM 1571 OD1 ASN A 201 35.648 16.599 26.047 1.00 41.68 ATOM 1572 ND2 ASN A 201 36.032 17.947 24.290 1.00 42.48 ATOM 1573 N LYS A 202 31.010 17.968 22.682 1.00 34.25 ATOM 1574 CA LYS A 202 29.899 17.747 21.740 1.00 36.87 ATOM 1575 C LYS A 202 29.230 16.427 21.749 1.00 36.56 ATOM 1576 O LYS A 202 28.578 16.007 20.776 1.00 38.53 ATOM 1577 CB LYS A 202 30.478 18.088 20.341 1.00 41.88 ATOM 1578 CG LYS A 202 31.034 19.548 20.328 1.00 45.39 ATOM 1579 CD LYS A 202 30.017 20.620 20.015 1.00 51.30 ATOM 1580 CE LYS A 202 28.743 20.720 20.851 1.00 55.52 ATOM 1581 NZ LYS A 202 27.643 21.431 20.034 1.00 59.01 ATOM 1582 N HIS A 203 29.198 15.739 22.903 1.00 34.71 ATOM 1583 CA HIS A 203 28.488 14.446 22.954 1.00 32.46 ATOM 1584 C HIS A 203 27.045 14.665 23.310 1.00 32.87 ATOM 1585 O HIS A 203 26.219 13.791 23.077 1.00 35.43 ATOM 1586 CB HIS A 203 29.159 13.479 23.956 1.00 30.54 ATOM 1587 CG HIS A 203 30.482 13.091 23.327 1.00 31.41 ATOM 1588 ND1 HIS A 203 31.691 13.478 23.781 1.00 32.60 ATOM 1589 CD2 HIS A 203 30.728 12.345 22.228 1.00 27.60 ATOM 1590 CE1 HIS A 203 32.669 13.003 23.005 1.00 29.94 ATOM 1591 NE2 HIS A 203 32.067 12.298 22.072 1.00 30.92 ATOM 1592 N MET A 204 26.792 15.826 23.884 1.00 33.05 ATOM 1593 CA MET A 204 25.506 16.242 24.401 1.00 32.72 ATOM 1594 C MET A 204 25.269 17.687 24.248 1.00 32.20 ATOM 1595 O MET A 204 26.313 18.397 24.242 1.00 34.16 ATOM 1596 CB MET A 204 25.692 15.936 25.928 1.00 37.49 ATOM 1597 CG MET A 204 24.383 15.853 26.612 1.00 40.20 ATOM 1598 SD MET A 204 24.634 14.331 27.663 1.00 42.49 ATOM 1599 CE MET A 204 22.920 13.813 27.680 1.00 40.99 ATOM 1600 N ASN A 205 24.033 18.147 24.199 1.00 32.12 ATOM 1601 CA ASN A 205 23.814 19.596 24.129 1.00 33.25 ATOM 1602 C ASN A 205 23.101 20.073 25.387 1.00 29.24 ATOM 1603 O ASN A 205 22.200 19.424 25.808 1.00 31.21 ATOM 1604 CB ASN A 205 23.126 20.035 22.840 1.00 43.50 ATOM 1605 CG ASN A 205 24.048 19.676 21.626 1.00 49.48 ATOM 1606 OD1 ASN A 205 25.218 20.138 21.505 1.00 53.34 ATOM 1607 ND2 ASN A 205 23.422 18.779 20.837 1.00 50.34 ATOM 1608 N ALA A 206 23.534 21.206 25.816 1.00 27.45 ATOM 1609 CA ALA A 206 23.115 21.963 26.938 1.00 25.46 ATOM 1610 C ALA A 206 21.642 22.279 26.906 1.00 28.06 ATOM 1611 O ALA A 206 21.030 22.550 27.999 1.00 31.20 ATOM 1612 CB ALA A 206 23.881 23.278 26.999 1.00 27.06 ATOM 1613 N ASP A 207 21.068 22.268 25.705 1.00 26.97 ATOM 1614 CA ASP A 207 19.626 22.646 25.680 1.00 28.54 ATOM 1615 C ASP A 207 18.697 21.447 25.788 1.00 26.90 ATOM 1616 O ASP A 207 17.447 21.673 25.884 1.00 29.09 ATOM 1617 CB ASP A 207 19.369 23.599 24.473 1.00 33.37 ATOM 1618 CG ASP A 207 19.203 22.834 23.139 1.00 37.58 ATOM 1619 OD1 ASP A 207 20.120 22.053 22.771 1.00 39.99 ATOM 1620 OD2 ASP A 207 18.089 23.029 22.455 1.00 41.97 ATOM 1621 N THR A 208 19.162 20.188 25.663 1.00 25.79 ATOM 1622 CA THR A 208 18.184 19.095 25.701 1.00 24.04 ATOM 1623 C THR A 208 17.213 19.164 26.881 1.00 25.38 ATOM 1624 O THR A 208 17.700 19.349 28.033 1.00 24.32 ATOM 1625 CB THR A 208 18.960 17.760 25.629 1.00 24.81 ATOM 1626 OG1 THR A 208 19.907 18.035 24.545 1.00 28.11 ATOM 1627 CG2 THR A 208 17.991 16.609 25.458 1.00 22.67 ATOM 1628 N ASP A 209 15.938 19.076 26.460 1.00 24.12 ATOM 1629 CA ASP A 209 14.887 19.039 27.458 1.00 23.13 ATOM 1630 C ASP A 209 14.147 17.679 27.353 1.00 22.24 ATOM 1631 O ASP A 209 14.492 16.767 26.569 1.00 22.67 ATOM 1632 CB ASP A 209 14.049 20.283 27.421 1.00 23.94 ATOM 1633 CG ASP A 209 13.138 20.443 26.221 1.00 27.38 ATOM 1634 OD1 ASP A 209 13.159 19.507 25.436 1.00 28.04 ATOM 1635 OD2 ASP A 209 12.397 21.438 26.018 1.00 31.42 ATOM 1636 N TYR A 210 13.043 17.572 28.052 1.00 22.22 ATOM 1637 CA TYR A 210 12.192 16.374 28.101 1.00 23.62 ATOM 1638 C TYR A 210 11.657 15.957 26.728 1.00 23.94 ATOM 1639 O TYR A 210 11.837 14.814 26.290 1.00 25.04 ATOM 1640 CB TYR A 210 11.009 16.413 29.107 1.00 20.91 ATOM 1641 CG TYR A 210 10.425 15.015 29.346 1.00 23.15 ATOM 1642 CD1 TYR A 210 9.439 14.483 28.492 1.00 20.22 ATOM 1643 CD2 TYR A 210 10.792 14.261 30.519 1.00 20.57 ATOM 1644 CE1 TYR A 210 8.850 13.297 28.773 1.00 22.17 ATOM 1645 CE2 TYR A 210 10.169 13.047 30.804 1.00 21.11 ATOM 1646 CZ TYR A 210 9.208 12.569 29.953 1.00 23.40 ATOM 1647 OH TYR A 210 8.644 11.365 30.145 1.00 24.29 ATOM 1648 N SER A 211 11.063 16.873 26.053 1.00 24.99 ATOM 1649 CA SER A 211 10.557 16.662 24.680 1.00 26.76 ATOM 1650 C SER A 211 11.642 16.354 23.699 1.00 26.16 ATOM 1651 O SER A 211 11.502 15.370 22.928 1.00 30.42 ATOM 1652 CB SER A 211 9.894 17.971 24.168 1.00 27.38 ATOM 1653 OG SER A 211 8.592 17.811 24.686 1.00 36.62 ATOM 1654 N ILE A 212 12.708 17.115 23.585 1.00 27.99 ATOM 1655 CA ILE A 212 13.786 16.864 22.619 1.00 25.10 ATOM 1656 C ILE A 212 14.321 15.462 22.827 1.00 26.40 ATOM 1657 O ILE A 212 14.517 14.703 21.848 1.00 24.51 ATOM 1658 CB ILE A 212 14.983 17.862 22.836 1.00 25.59 ATOM 1659 CG1 ILE A 212 14.684 19.376 22.618 1.00 29.88 ATOM 1660 CG2 ILE A 212 16.201 17.352 22.035 1.00 27.13 ATOM 1661 CD1 ILE A 212 13.403 19.407 21.786 1.00 33.25 ATOM 1662 N ALA A 213 14.582 15.107 24.182 1.00 26.23 ATOM 1663 CA ALA A 213 15.132 13.735 24.501 1.00 23.83 ATOM 1664 C ALA A 213 14.174 12.643 24.142 1.00 23.00 ATOM 1665 O ALA A 213 14.480 11.597 23.484 1.00 23.58 ATOM 1666 CB ALA A 213 15.503 13.617 25.972 1.00 22.66 ATOM 1667 N GLU A 214 12.929 12.899 24.527 1.00 22.85 ATOM 1668 CA GLU A 214 11.895 11.901 24.171 1.00 23.45 ATOM 1669 C GLU A 214 11.758 11.742 22.672 1.00 25.44 ATOM 1670 O GLU A 214 11.858 10.553 22.263 1.00 25.00 ATOM 1671 CB GLU A 214 10.545 12.232 24.790 1.00 26.21 ATOM 1672 CG GLU A 214 9.475 11.084 24.721 1.00 26.88 ATOM 1673 CD GLU A 214 8.185 11.453 25.324 1.00 25.98 ATOM 1674 OE1 GLU A 214 7.812 12.582 25.360 1.00 28.16 ATOM 1675 OE2 GLU A 214 7.653 10.534 25.945 1.00 27.05 ATOM 1676 N ALA A 215 11.588 12.760 21.865 1.00 25.50 ATOM 1677 CA ALA A 215 11.457 12.611 20.406 1.00 27.59 ATOM 1678 C ALA A 215 12.666 11.950 19.791 1.00 27.85 ATOM 1679 O ALA A 215 12.485 11.049 18.884 1.00 29.34 ATOM 1680 CB ALA A 215 11.261 13.983 19.725 1.00 28.31 ATOM 1681 N ALA A 216 13.830 12.337 20.316 1.00 28.03 ATOM 1682 CA ALA A 216 15.065 11.739 19.797 1.00 27.69 ATOM 1683 C ALA A 216 15.028 10.254 19.960 1.00 28.51 ATOM 1684 O ALA A 216 15.271 9.517 18.991 1.00 29.54 ATOM 1685 CB ALA A 216 16.364 12.290 20.430 1.00 26.91 ATOM 1686 N PHE A 217 14.760 9.723 21.195 1.00 23.57 ATOM 1687 CA PHE A 217 14.869 8.241 21.303 1.00 22.55 ATOM 1688 C PHE A 217 13.774 7.519 20.563 1.00 23.16 ATOM 1689 O PHE A 217 13.983 6.405 20.051 1.00 24.95 ATOM 1690 CB PHE A 217 14.903 7.941 22.814 1.00 21.93 ATOM 1691 CG PHE A 217 15.003 6.486 23.093 1.00 18.47 ATOM 1692 CD1 PHE A 217 13.877 5.687 23.137 1.00 21.23 ATOM 1693 CD2 PHE A 217 16.236 5.944 23.302 1.00 18.03 ATOM 1694 CE1 PHE A 217 13.970 4.322 23.416 1.00 22.62 ATOM 1695 CE2 PHE A 217 16.360 4.623 23.578 1.00 20.24 ATOM 1696 CZ PHE A 217 15.237 3.779 23.668 1.00 18.05 ATOM 1697 N ASN A 218 12.580 8.071 20.592 1.00 23.23 ATOM 1698 CA ASN A 218 11.372 7.503 20.023 1.00 26.21 ATOM 1699 C ASN A 218 11.478 7.458 18.452 1.00 29.15 ATOM 1700 O ASN A 218 10.909 6.530 17.866 1.00 27.83 ATOM 1701 CB ASN A 218 10.097 8.180 20.497 1.00 24.62 ATOM 1702 CG ASN A 218 9.739 7.703 21.927 1.00 25.68 ATOM 1703 OD1 ASN A 218 8.679 8.008 22.461 1.00 27.23 ATOM 1704 ND2 ASN A 218 10.683 7.028 22.601 1.00 24.93 ATOM 1705 N LYS A 219 12.268 8.374 17.884 1.00 30.33 ATOM 1706 CA LYS A 219 12.450 8.360 16.400 1.00 32.01 ATOM 1707 C LYS A 219 13.635 7.572 15.931 1.00 32.49 ATOM 1708 O LYS A 219 13.913 7.548 14.675 1.00 35.24 ATOM 1709 CB LYS A 219 12.640 9.795 15.851 1.00 35.74 ATOM 1710 CG LYS A 219 11.371 10.605 16.311 1.00 42.88 ATOM 1711 CD LYS A 219 11.638 12.099 16.269 1.00 50.01 ATOM 1712 CE LYS A 219 12.563 12.511 15.118 1.00 53.18 ATOM 1713 NZ LYS A 219 13.347 13.716 15.638 1.00 59.32 ATOM 1714 N GLY A 220 14.359 7.000 16.843 1.00 28.38 ATOM 1715 CA GLY A 220 15.536 6.196 16.576 1.00 27.11 ATOM 1716 C GLY A 220 16.789 6.956 16.410 1.00 26.76 ATOM 1717 O GLY A 220 17.845 6.338 15.945 1.00 29.32 ATOM 1718 N GLU A 221 16.797 8.226 16.773 1.00 28.48 ATOM 1719 CA GLU A 221 18.104 8.951 16.563 1.00 29.37 ATOM 1720 C GLU A 221 19.132 8.827 17.636 1.00 29.96 ATOM 1721 O GLU A 221 20.330 9.095 17.315 1.00 30.49 ATOM 1722 CB GLU A 221 17.750 10.405 16.332 1.00 34.70 ATOM 1723 CG GLU A 221 16.455 10.570 15.443 1.00 40.91 ATOM 1724 CD GLU A 221 16.248 12.062 15.240 1.00 46.03 ATOM 1725 OE1 GLU A 221 16.766 12.919 15.964 1.00 48.55 ATOM 1726 OE2 GLU A 221 15.529 12.264 14.211 1.00 53.44 ATOM 1727 N THR A 222 18.741 8.496 18.890 1.00 26.81 ATOM 1728 CA THR A 222 19.747 8.375 19.941 1.00 24.33 ATOM 1729 C THR A 222 19.671 6.948 20.419 1.00 23.39 ATOM 1730 O THR A 222 18.573 6.410 20.422 1.00 21.99 ATOM 1731 CB THR A 222 19.494 9.444 21.057 1.00 26.01 ATOM 1732 OG1 THR A 222 20.759 9.419 21.820 1.00 27.75 ATOM 1733 CG2 THR A 222 18.273 9.141 21.923 1.00 25.07 ATOM 1734 N ALA A 223 20.807 6.331 20.836 1.00 22.81 ATOM 1735 CA ALA A 223 20.704 4.946 21.276 1.00 21.91 ATOM 1736 C ALA A 223 20.210 4.799 22.740 1.00 22.26 ATOM 1737 O ALA A 223 19.747 3.668 22.992 1.00 21.98 ATOM 1738 CB ALA A 223 22.061 4.236 21.141 1.00 23.51 ATOM 1739 N MET A 224 20.262 5.798 23.597 1.00 22.50 ATOM 1740 CA MET A 224 19.839 5.626 25.051 1.00 19.70 ATOM 1741 C MET A 224 19.245 6.906 25.542 1.00 19.08 ATOM 1742 O MET A 224 19.479 8.000 25.057 1.00 17.71 ATOM 1743 CB MET A 224 21.160 5.405 25.845 1.00 19.25 ATOM 1744 CG MET A 224 21.816 4.118 25.666 1.00 21.55 ATOM 1745 SD MET A 224 23.356 4.003 26.581 1.00 27.08 ATOM 1746 CE MET A 224 24.477 5.155 25.828 1.00 25.34 ATOM 1747 N THR A 225 18.427 6.751 26.602 1.00 19.19 ATOM 1748 CA THR A 225 17.826 7.969 27.267 1.00 17.61 ATOM 1749 C THR A 225 17.701 7.557 28.747 1.00 19.51 ATOM 1750 O THR A 225 17.925 6.345 29.095 1.00 18.99 ATOM 1751 CB THR A 225 16.507 8.438 26.597 1.00 13.98 ATOM 1752 OG1 THR A 225 16.119 9.697 27.154 1.00 21.69 ATOM 1753 CG2 THR A 225 15.375 7.356 26.691 1.00 17.53 ATOM 1754 N ILE A 226 17.453 8.460 29.635 1.00 18.10 ATOM 1755 CA ILE A 226 17.275 8.098 31.065 1.00 15.93 ATOM 1756 C ILE A 226 15.896 8.592 31.358 1.00 15.68 ATOM 1757 O ILE A 226 15.651 9.779 31.030 1.00 17.30 ATOM 1758 CB ILE A 226 18.355 8.783 31.904 1.00 16.97 ATOM 1759 CG1 ILE A 226 19.762 8.038 31.620 1.00 16.31 ATOM 1760 CG2 ILE A 226 17.951 8.769 33.387 1.00 18.79 ATOM 1761 CD1 ILE A 226 20.871 9.057 32.213 1.00 18.28 ATOM 1762 N ASN A 227 14.976 7.811 31.841 1.00 15.21 ATOM 1763 CA ASN A 227 13.636 8.274 32.174 1.00 15.29 ATOM 1764 C ASN A 227 12.964 7.273 33.210 1.00 16.75 ATOM 1765 O ASN A 227 13.586 6.241 33.548 1.00 17.04 ATOM 1766 CB ASN A 227 12.813 8.442 30.891 1.00 19.15 ATOM 1767 CG ASN A 227 11.891 9.636 30.922 1.00 20.59 ATOM 1768 OD1 ASN A 227 11.240 10.061 31.945 1.00 25.03 ATOM 1769 ND2 ASN A 227 11.622 10.280 29.798 1.00 21.39 ATOM 1770 N GLY A 228 11.781 7.660 33.692 1.00 16.86 ATOM 1771 CA GLY A 228 11.007 6.887 34.639 1.00 16.25 ATOM 1772 C GLY A 228 9.944 6.086 33.921 1.00 19.00 ATOM 1773 O GLY A 228 9.735 6.143 32.663 1.00 19.13 ATOM 1774 N PRO A 229 9.217 5.241 34.698 1.00 19.24 ATOM 1775 CA PRO A 229 8.236 4.320 34.188 1.00 17.81 ATOM 1776 C PRO A 229 7.187 4.927 33.306 1.00 18.56 ATOM 1777 O PRO A 229 6.679 4.230 32.384 1.00 17.71 ATOM 1778 CB PRO A 229 7.664 3.576 35.420 1.00 17.05 ATOM 1779 CG PRO A 229 8.576 3.886 36.515 1.00 19.44 ATOM 1780 CD PRO A 229 9.450 5.068 36.164 1.00 18.37 ATOM 1781 N TRP A 230 6.712 6.176 33.592 1.00 17.59 ATOM 1782 CA TRP A 230 5.734 6.924 32.919 1.00 16.85 ATOM 1783 C TRP A 230 6.125 7.127 31.419 1.00 17.44 ATOM 1784 O TRP A 230 5.195 7.207 30.608 1.00 19.47 ATOM 1785 CB TRP A 230 5.448 8.289 33.641 1.00 16.91 ATOM 1786 CG TRP A 230 6.722 9.099 33.695 1.00 19.47 ATOM 1787 CD1 TRP A 230 7.315 9.800 32.695 1.00 19.47 ATOM 1788 CD2 TRP A 230 7.657 9.193 34.820 1.00 20.47 ATOM 1789 NE1 TRP A 230 8.517 10.366 33.132 1.00 19.66 ATOM 1790 CE2 TRP A 230 8.754 9.942 34.435 1.00 20.33 ATOM 1791 CE3 TRP A 230 7.606 8.669 36.114 1.00 21.16 ATOM 1792 CZ2 TRP A 230 9.767 10.285 35.265 1.00 19.60 ATOM 1793 CZ3 TRP A 230 8.710 8.936 36.918 1.00 18.79 ATOM 1794 CH2 TRP A 230 9.764 9.710 36.511 1.00 22.05 ATOM 1795 N ALA A 231 7.345 7.152 30.995 1.00 19.60 ATOM 1796 CA ALA A 231 7.736 7.302 29.569 1.00 18.83 ATOM 1797 C ALA A 231 7.559 6.024 28.762 1.00 18.79 ATOM 1798 O ALA A 231 7.526 6.031 27.481 1.00 19.11 ATOM 1799 CB ALA A 231 9.236 7.533 29.685 1.00 17.18 ATOM 1800 N TRP A 232 7.379 4.839 29.339 1.00 18.62 ATOM 1801 CA TRP A 232 7.403 3.562 28.628 1.00 21.07 ATOM 1802 C TRP A 232 6.290 3.520 27.578 1.00 23.97 ATOM 1803 O TRP A 232 6.453 2.846 26.547 1.00 21.87 ATOM 1804 CB TRP A 232 7.365 2.280 29.496 1.00 19.90 ATOM 1805 CG TRP A 232 8.497 2.191 30.506 1.00 18.81 ATOM 1806 CD1 TRP A 232 9.737 2.784 30.520 1.00 18.39 ATOM 1807 CD2 TRP A 232 8.439 1.419 31.740 1.00 17.55 ATOM 1808 NE1 TRP A 232 10.436 2.444 31.640 1.00 16.62 ATOM 1809 CE2 TRP A 232 9.631 1.582 32.382 1.00 15.06 ATOM 1810 CE3 TRP A 232 7.393 0.611 32.250 1.00 18.32 ATOM 1811 CZ2 TRP A 232 9.928 0.955 33.637 1.00 20.58 ATOM 1812 CZ3 TRP A 232 7.649 0.008 33.482 1.00 18.91 ATOM 1813 CH2 TRP A 232 8.864 0.129 34.122 1.00 17.77 ATOM 1814 N SER A 233 5.169 4.099 27.961 1.00 24.57 ATOM 1815 CA SER A 233 3.982 4.097 27.045 1.00 28.37 ATOM 1816 C SER A 233 4.225 4.642 25.657 1.00 27.00 ATOM 1817 O SER A 233 3.783 3.982 24.697 1.00 28.52 ATOM 1818 CB SER A 233 2.800 4.945 27.646 1.00 28.20 ATOM 1819 OG SER A 233 2.281 3.856 28.405 1.00 35.62 ATOM 1820 N ASN A 234 4.864 5.778 25.596 1.00 25.65 ATOM 1821 CA ASN A 234 5.124 6.389 24.262 1.00 27.45 ATOM 1822 C ASN A 234 6.170 5.578 23.435 1.00 25.88 ATOM 1823 O ASN A 234 6.134 5.672 22.197 1.00 26.65 ATOM 1824 CB ASN A 234 5.560 7.830 24.376 1.00 27.20 ATOM 1825 CG ASN A 234 4.515 8.800 24.825 1.00 32.73 ATOM 1826 OD1 ASN A 234 3.313 8.548 24.569 1.00 34.93 ATOM 1827 ND2 ASN A 234 4.849 9.872 25.578 1.00 34.92 ATOM 1828 N ILE A 235 7.114 5.014 24.183 1.00 25.01 ATOM 1829 CA ILE A 235 8.115 4.183 23.586 1.00 23.56 ATOM 1830 C ILE A 235 7.370 3.000 22.931 1.00 25.58 ATOM 1831 O ILE A 235 7.666 2.590 21.770 1.00 26.71 ATOM 1832 CB ILE A 235 9.203 3.650 24.561 1.00 19.34 ATOM 1833 CG1 ILE A 235 9.903 4.834 25.272 1.00 18.44 ATOM 1834 CG2 ILE A 235 10.227 2.842 23.723 1.00 22.65 ATOM 1835 CD1 ILE A 235 10.920 4.384 26.351 1.00 19.01 ATOM 1836 N ASP A 236 6.432 2.424 23.663 1.00 25.62 ATOM 1837 CA ASP A 236 5.804 1.190 23.133 1.00 28.44 ATOM 1838 C ASP A 236 5.118 1.466 21.765 1.00 32.41 ATOM 1839 O ASP A 236 5.125 0.567 20.923 1.00 31.56 ATOM 1840 CB ASP A 236 4.757 0.546 23.983 1.00 26.70 ATOM 1841 CG ASP A 236 5.359 -0.147 25.240 1.00 28.31 ATOM 1842 OD1 ASP A 236 6.526 -0.472 25.341 1.00 25.76 ATOM 1843 OD2 ASP A 236 4.469 -0.256 26.130 1.00 30.38 ATOM 1844 N THR A 237 4.511 2.638 21.851 1.00 33.40 ATOM 1845 CA THR A 237 3.729 3.212 20.797 1.00 34.18 ATOM 1846 C THR A 237 4.572 3.527 19.540 1.00 34.60 ATOM 1847 O THR A 237 3.966 3.522 18.437 1.00 34.43 ATOM 1848 CB THR A 237 2.950 4.540 21.105 1.00 33.57 ATOM 1849 OG1 THR A 237 1.917 4.214 22.004 1.00 35.33 ATOM 1850 CG2 THR A 237 2.218 4.888 19.792 1.00 39.52 ATOM 1851 N SER A 238 5.808 3.839 19.781 1.00 33.33 ATOM 1852 CA SER A 238 6.705 4.126 18.641 1.00 34.83 ATOM 1853 C SER A 238 7.301 2.795 18.137 1.00 35.05 ATOM 1854 O SER A 238 8.054 2.728 17.178 1.00 31.67 ATOM 1855 CB SER A 238 7.763 5.118 19.204 1.00 35.96 ATOM 1856 OG SER A 238 8.945 4.225 19.502 1.00 36.71 ATOM 1857 N LYS A 239 7.038 1.688 18.865 1.00 37.42 ATOM 1858 CA LYS A 239 7.578 0.364 18.581 1.00 42.05 ATOM 1859 C LYS A 239 9.099 0.345 18.606 1.00 41.41 ATOM 1860 O LYS A 239 9.633 -0.615 17.967 1.00 40.74 ATOM 1861 CB LYS A 239 7.140 -0.328 17.252 1.00 43.06 ATOM 1862 CG LYS A 239 7.870 -1.647 16.984 1.00 49.69 ATOM 1863 CD LYS A 239 9.199 -1.966 16.362 1.00 50.19 ATOM 1864 CE LYS A 239 10.514 -2.223 17.004 1.00 49.43 ATOM 1865 NZ LYS A 239 11.091 -3.522 17.406 1.00 46.73 ATOM 1866 N VAL A 240 9.862 1.286 19.207 1.00 40.43 ATOM 1867 CA VAL A 240 11.363 1.074 19.164 1.00 36.57 ATOM 1868 C VAL A 240 11.579 -0.273 19.838 1.00 35.68 ATOM 1869 O VAL A 240 10.662 -0.682 20.650 1.00 37.66 ATOM 1870 CB VAL A 240 12.054 2.246 19.895 1.00 34.25 ATOM 1871 CG1 VAL A 240 13.309 1.759 20.671 1.00 28.26 ATOM 1872 CG2 VAL A 240 12.285 3.439 18.995 1.00 31.90 ATOM 1873 N ASN A 241 12.656 -0.992 19.610 1.00 35.28 ATOM 1874 CA ASN A 241 13.007 -2.255 20.317 1.00 32.94 ATOM 1875 C ASN A 241 13.969 -1.847 21.492 1.00 29.39 ATOM 1876 O ASN A 241 15.157 -1.821 21.450 1.00 28.65 ATOM 1877 CB ASN A 241 13.602 -3.255 19.386 1.00 33.85 ATOM 1878 CG ASN A 241 13.964 -4.582 20.044 1.00 39.23 ATOM 1879 OD1 ASN A 241 13.334 -5.159 20.978 1.00 36.88 ATOM 1880 ND2 ASN A 241 15.073 -5.173 19.489 1.00 41.90 ATOM 1881 N TYR A 242 13.353 -1.585 22.649 1.00 29.99 ATOM 1882 CA TYR A 242 14.068 -1.075 23.831 1.00 25.45 ATOM 1883 C TYR A 242 14.222 -1.987 25.011 1.00 26.26 ATOM 1884 O TYR A 242 13.368 -2.874 25.265 1.00 27.76 ATOM 1885 CB TYR A 242 13.302 0.210 24.323 1.00 24.55 ATOM 1886 CG TYR A 242 12.015 0.045 25.060 1.00 25.49 ATOM 1887 CD1 TYR A 242 10.808 -0.155 24.328 1.00 25.96 ATOM 1888 CD2 TYR A 242 11.889 0.115 26.483 1.00 22.24 ATOM 1889 CE1 TYR A 242 9.560 -0.279 24.992 1.00 27.59 ATOM 1890 CE2 TYR A 242 10.700 -0.001 27.134 1.00 22.93 ATOM 1891 CZ TYR A 242 9.510 -0.178 26.404 1.00 24.82 ATOM 1892 OH TYR A 242 8.249 -0.306 26.967 1.00 25.64 ATOM 1893 N GLY A 243 15.306 -1.723 25.788 1.00 22.77 ATOM 1894 CA GLY A 243 15.435 -2.522 27.027 1.00 20.02 ATOM 1895 C GLY A 243 15.438 -1.406 28.118 1.00 20.94 ATOM 1896 O GLY A 243 15.609 -0.212 27.820 1.00 19.26 ATOM 1897 N VAL A 244 15.257 -1.872 29.344 1.00 21.00 ATOM 1898 CA VAL A 244 15.265 -0.945 30.529 1.00 21.23 ATOM 1899 C VAL A 244 16.321 -1.547 31.443 1.00 22.15 ATOM 1900 O VAL A 244 16.118 -2.749 31.763 1.00 23.13 ATOM 1901 CB VAL A 244 13.865 -0.754 31.172 1.00 17.16 ATOM 1902 CG1 VAL A 244 14.074 0.039 32.487 1.00 17.47 ATOM 1903 CG2 VAL A 244 12.818 -0.154 30.312 1.00 16.45 ATOM 1904 N THR A 245 17.372 -0.834 31.864 1.00 19.82 ATOM 1905 CA THR A 245 18.281 -1.551 32.783 1.00 21.22 ATOM 1906 C THR A 245 18.868 -0.660 33.876 1.00 20.99 ATOM 1907 O THR A 245 18.514 0.520 34.014 1.00 19.84 ATOM 1908 CB THR A 245 19.372 -2.181 31.812 1.00 24.12 ATOM 1909 OG1 THR A 245 20.338 -3.041 32.488 1.00 26.10 ATOM 1910 CG2 THR A 245 20.087 -1.059 30.997 1.00 25.89 ATOM 1911 N VAL A 246 19.840 -1.180 34.614 1.00 19.99 ATOM 1912 CA VAL A 246 20.504 -0.379 35.632 1.00 23.38 ATOM 1913 C VAL A 246 21.231 0.821 35.002 1.00 23.21 ATOM 1914 O VAL A 246 21.884 0.624 33.975 1.00 23.62 ATOM 1915 CB VAL A 246 21.613 -1.178 36.409 1.00 27.54 ATOM 1916 CG1 VAL A 246 22.003 -0.676 37.842 1.00 25.50 ATOM 1917 CG2 VAL A 246 21.055 -2.562 36.470 1.00 34.17 ATOM 1918 N LEU A 247 21.298 1.941 35.653 1.00 21.06 ATOM 1919 CA LEU A 247 22.122 3.062 35.218 1.00 20.17 ATOM 1920 C LEU A 247 23.606 2.700 35.257 1.00 21.20 ATOM 1921 O LEU A 247 24.156 1.851 36.033 1.00 22.52 ATOM 1922 CB LEU A 247 21.778 4.220 36.197 1.00 18.74 ATOM 1923 CG LEU A 247 20.331 4.741 36.069 1.00 18.60 ATOM 1924 CD1 LEU A 247 20.063 5.655 37.318 1.00 18.93 ATOM 1925 CD2 LEU A 247 20.173 5.533 34.790 1.00 18.94 ATOM 1926 N PRO A 248 24.418 3.348 34.393 1.00 21.31 ATOM 1927 CA PRO A 248 25.872 3.063 34.428 1.00 22.85 ATOM 1928 C PRO A 248 26.540 3.588 35.725 1.00 23.34 ATOM 1929 O PRO A 248 25.998 4.524 36.453 1.00 22.85 ATOM 1930 CB PRO A 248 26.407 3.729 33.155 1.00 20.22 ATOM 1931 CG PRO A 248 25.328 4.585 32.689 1.00 20.59 ATOM 1932 CD PRO A 248 24.051 4.378 33.459 1.00 21.09 ATOM 1933 N THR A 249 27.701 3.032 36.019 1.00 22.52 ATOM 1934 CA THR A 249 28.516 3.403 37.153 1.00 19.87 ATOM 1935 C THR A 249 29.391 4.560 36.746 1.00 21.30 ATOM 1936 O THR A 249 29.750 4.854 35.596 1.00 21.30 ATOM 1937 CB THR A 249 29.429 2.224 37.692 1.00 21.47 ATOM 1938 OG1 THR A 249 30.453 1.932 36.622 1.00 25.49 ATOM 1939 CG2 THR A 249 28.677 1.020 38.212 1.00 19.39 ATOM 1940 N PHE A 250 29.857 5.256 37.780 1.00 19.36 ATOM 1941 CA PHE A 250 30.726 6.367 37.541 1.00 21.37 ATOM 1942 C PHE A 250 31.854 6.106 38.569 1.00 23.36 ATOM 1943 O PHE A 250 31.484 6.076 39.767 1.00 22.78 ATOM 1944 CB PHE A 250 30.011 7.717 37.768 1.00 20.48 ATOM 1945 CG PHE A 250 30.888 8.925 37.652 1.00 18.81 ATOM 1946 CD1 PHE A 250 31.561 9.180 36.456 1.00 18.62 ATOM 1947 CD2 PHE A 250 31.072 9.815 38.701 1.00 18.64 ATOM 1948 CE1 PHE A 250 32.433 10.286 36.415 1.00 19.05 ATOM 1949 CE2 PHE A 250 31.892 10.929 38.665 1.00 18.50 ATOM 1950 CZ PHE A 250 32.602 11.166 37.464 1.00 17.78 ATOM 1951 N LYS A 251 33.080 6.005 38.174 1.00 23.69 ATOM 1952 CA LYS A 251 34.241 5.881 39.108 1.00 25.44 ATOM 1953 C LYS A 251 34.035 4.583 39.851 1.00 24.99 ATOM 1954 O LYS A 251 34.381 4.474 41.046 1.00 27.25 ATOM 1955 CB LYS A 251 34.442 7.078 40.078 1.00 29.26 ATOM 1956 CG LYS A 251 34.977 8.357 39.374 1.00 31.89 ATOM 1957 CD LYS A 251 35.517 9.482 40.150 1.00 34.06 ATOM 1958 CE LYS A 251 36.510 10.481 39.758 1.00 37.64 ATOM 1959 NZ LYS A 251 36.647 10.955 38.354 1.00 37.78 ATOM 1960 N GLY A 252 33.350 3.689 39.179 1.00 22.07 ATOM 1961 CA GLY A 252 33.122 2.355 39.770 1.00 22.28 ATOM 1962 C GLY A 252 31.967 2.314 40.749 1.00 25.31 ATOM 1963 O GLY A 252 31.670 1.166 41.309 1.00 27.62 ATOM 1964 N GLN A 253 31.288 3.444 41.032 1.00 21.35 ATOM 1965 CA GLN A 253 30.180 3.388 41.997 1.00 20.46 ATOM 1966 C GLN A 253 28.895 3.450 41.189 1.00 21.04 ATOM 1967 O GLN A 253 28.839 4.046 40.056 1.00 19.95 ATOM 1968 CB GLN A 253 30.185 4.632 42.914 1.00 21.38 ATOM 1969 CG GLN A 253 31.516 5.372 43.039 1.00 28.07 ATOM 1970 CD GLN A 253 31.934 5.006 44.427 1.00 33.68 ATOM 1971 OE1 GLN A 253 31.690 3.811 44.691 1.00 37.58 ATOM 1972 NE2 GLN A 253 32.301 5.934 45.302 1.00 40.06 ATOM 1973 N PRO A 254 27.820 2.894 41.741 1.00 20.25 ATOM 1974 CA PRO A 254 26.553 2.943 41.095 1.00 19.81 ATOM 1975 C PRO A 254 26.064 4.382 40.945 1.00 19.71 ATOM 1976 O PRO A 254 26.356 5.208 41.900 1.00 20.39 ATOM 1977 CB PRO A 254 25.567 2.132 42.003 1.00 19.11 ATOM 1978 CG PRO A 254 26.426 1.528 43.039 1.00 21.38 ATOM 1979 CD PRO A 254 27.847 2.138 43.026 1.00 19.37 ATOM 1980 N SER A 255 25.363 4.719 39.887 1.00 18.71 ATOM 1981 CA SER A 255 24.591 5.984 39.748 1.00 18.55 ATOM 1982 C SER A 255 23.502 5.835 40.862 1.00 20.09 ATOM 1983 O SER A 255 23.006 4.688 41.192 1.00 18.06 ATOM 1984 CB SER A 255 23.859 6.161 38.391 1.00 17.14 ATOM 1985 OG SER A 255 24.976 6.478 37.502 1.00 19.50 ATOM 1986 N LYS A 256 23.154 6.899 41.532 1.00 19.40 ATOM 1987 CA LYS A 256 22.191 6.790 42.697 1.00 20.71 ATOM 1988 C LYS A 256 21.040 7.709 42.505 1.00 18.36 ATOM 1989 O LYS A 256 21.163 8.904 42.911 1.00 17.16 ATOM 1990 CB LYS A 256 22.896 7.379 43.920 1.00 23.96 ATOM 1991 CG LYS A 256 23.676 6.616 44.926 1.00 32.07 ATOM 1992 CD LYS A 256 24.965 6.107 44.226 1.00 36.18 ATOM 1993 CE LYS A 256 25.924 5.277 45.080 1.00 36.75 ATOM 1994 NZ LYS A 256 27.328 5.509 44.700 1.00 31.97 ATOM 1995 N PRO A 257 19.961 7.231 41.903 1.00 19.72 ATOM 1996 CA PRO A 257 18.802 8.109 41.671 1.00 20.42 ATOM 1997 C PRO A 257 18.139 8.484 43.020 1.00 19.31 ATOM 1998 O PRO A 257 18.198 7.711 43.932 1.00 15.36 ATOM 1999 CB PRO A 257 17.854 7.276 40.802 1.00 20.91 ATOM 2000 CG PRO A 257 18.276 5.795 40.928 1.00 18.43 ATOM 2001 CD PRO A 257 19.712 5.880 41.401 1.00 18.52 ATOM 2002 N PHE A 258 17.527 9.629 43.097 1.00 17.43 ATOM 2003 CA PHE A 258 16.724 10.012 44.224 1.00 17.73 ATOM 2004 C PHE A 258 15.451 9.202 43.982 1.00 20.84 ATOM 2005 O PHE A 258 14.926 9.202 42.799 1.00 24.35 ATOM 2006 CB PHE A 258 16.450 11.532 44.284 1.00 17.12 ATOM 2007 CG PHE A 258 17.117 12.246 45.393 1.00 19.14 ATOM 2008 CD1 PHE A 258 17.260 11.589 46.659 1.00 22.37 ATOM 2009 CD2 PHE A 258 17.615 13.557 45.175 1.00 22.12 ATOM 2010 CE1 PHE A 258 17.794 12.241 47.761 1.00 24.66 ATOM 2011 CE2 PHE A 258 18.224 14.198 46.285 1.00 25.08 ATOM 2012 CZ PHE A 258 18.255 13.567 47.582 1.00 26.99 ATOM 2013 N VAL A 259 14.890 8.515 44.931 1.00 15.41 ATOM 2014 CA VAL A 259 13.641 7.775 44.694 1.00 15.38 ATOM 2015 C VAL A 259 12.464 8.530 45.220 1.00 17.28 ATOM 2016 O VAL A 259 12.382 9.099 46.371 1.00 18.07 ATOM 2017 CB VAL A 259 13.868 6.353 45.321 1.00 18.40 ATOM 2018 CG1 VAL A 259 12.631 5.501 45.282 1.00 16.65 ATOM 2019 CG2 VAL A 259 15.135 5.681 44.693 1.00 18.04 ATOM 2020 N GLY A 260 11.379 8.588 44.417 1.00 17.42 ATOM 2021 CA GLY A 260 10.154 9.295 44.722 1.00 15.41 ATOM 2022 C GLY A 260 9.065 8.249 44.890 1.00 16.34 ATOM 2023 O GLY A 260 8.972 7.222 44.230 1.00 16.77 ATOM 2024 N VAL A 261 8.198 8.527 45.849 1.00 16.08 ATOM 2025 CA VAL A 261 7.011 7.768 46.207 1.00 16.15 ATOM 2026 C VAL A 261 5.894 8.647 45.709 1.00 16.66 ATOM 2027 O VAL A 261 5.670 9.701 46.432 1.00 18.50 ATOM 2028 CB VAL A 261 6.853 7.383 47.753 1.00 17.05 ATOM 2029 CG1 VAL A 261 5.522 6.727 47.972 1.00 17.45 ATOM 2030 CG2 VAL A 261 7.967 6.538 48.302 1.00 18.27 ATOM 2031 N LEU A 262 5.222 8.357 44.563 1.00 16.02 ATOM 2032 CA LEU A 262 4.088 9.038 44.032 1.00 17.63 ATOM 2033 C LEU A 262 3.027 8.972 45.233 1.00 16.69 ATOM 2034 O LEU A 262 2.792 7.826 45.656 1.00 18.15 ATOM 2035 CB LEU A 262 3.482 8.532 42.743 1.00 16.65 ATOM 2036 CG LEU A 262 2.251 9.132 42.152 1.00 17.06 ATOM 2037 CD1 LEU A 262 2.438 10.613 41.715 1.00 16.98 ATOM 2038 CD2 LEU A 262 1.729 8.339 40.925 1.00 20.38 ATOM 2039 N SER A 263 2.513 10.139 45.544 1.00 18.04 ATOM 2040 CA SER A 263 1.602 10.254 46.689 1.00 20.14 ATOM 2041 C SER A 263 0.370 11.147 46.400 1.00 18.92 ATOM 2042 O SER A 263 0.437 12.063 45.646 1.00 17.51 ATOM 2043 CB SER A 263 2.376 10.786 47.904 1.00 20.36 ATOM 2044 OG SER A 263 3.477 9.968 48.225 1.00 24.42 ATOM 2045 N ALA A 264 -0.745 10.811 47.174 1.00 19.84 ATOM 2046 CA ALA A 264 -2.046 11.537 47.004 1.00 18.06 ATOM 2047 C ALA A 264 -2.398 12.176 48.360 1.00 19.68 ATOM 2048 O ALA A 264 -2.533 11.410 49.348 1.00 21.06 ATOM 2049 CB ALA A 264 -3.227 10.763 46.504 1.00 15.61 ATOM 2050 N GLY A 265 -2.476 13.487 48.336 1.00 20.86 ATOM 2051 CA GLY A 265 -2.779 14.207 49.625 1.00 21.38 ATOM 2052 C GLY A 265 -4.113 14.860 49.549 1.00 23.25 ATOM 2053 O GLY A 265 -4.620 15.117 48.466 1.00 23.67 ATOM 2054 N ILE A 266 -4.710 15.070 50.781 1.00 26.12 ATOM 2055 CA ILE A 266 -6.077 15.713 50.789 1.00 24.73 ATOM 2056 C ILE A 266 -5.964 17.126 51.317 1.00 26.51 ATOM 2057 O ILE A 266 -5.261 17.455 52.322 1.00 26.58 ATOM 2058 CB ILE A 266 -7.046 14.784 51.588 1.00 26.71 ATOM 2059 CG1 ILE A 266 -7.108 13.338 50.966 1.00 26.96 ATOM 2060 CG2 ILE A 266 -8.434 15.402 51.761 1.00 23.77 ATOM 2061 CD1 ILE A 266 -7.802 12.407 52.011 1.00 28.14 ATOM 2062 N ASN A 267 -6.517 18.009 50.513 1.00 27.81 ATOM 2063 CA ASN A 267 -6.501 19.448 50.776 1.00 30.65 ATOM 2064 C ASN A 267 -7.229 19.579 52.095 1.00 33.63 ATOM 2065 O ASN A 267 -8.367 19.092 52.238 1.00 33.06 ATOM 2066 CB ASN A 267 -7.103 20.177 49.595 1.00 28.39 ATOM 2067 CG ASN A 267 -6.958 21.653 49.552 1.00 29.79 ATOM 2068 OD1 ASN A 267 -6.844 22.222 50.696 1.00 30.71 ATOM 2069 ND2 ASN A 267 -6.981 22.288 48.391 1.00 24.61 ATOM 2070 N ALA A 268 -6.468 20.240 52.979 1.00 38.69 ATOM 2071 CA ALA A 268 -6.978 20.528 54.386 1.00 40.84 ATOM 2072 C ALA A 268 -8.323 21.325 54.275 1.00 41.69 ATOM 2073 O ALA A 268 -9.245 21.114 55.111 1.00 41.47 ATOM 2074 CB ALA A 268 -5.956 21.212 55.283 1.00 33.60 ATOM 2075 N ALA A 269 -8.386 22.153 53.224 1.00 42.17 ATOM 2076 CA ALA A 269 -9.457 23.017 52.782 1.00 43.82 ATOM 2077 C ALA A 269 -10.642 22.286 52.101 1.00 43.91 ATOM 2078 O ALA A 269 -11.540 23.089 51.782 1.00 45.62 ATOM 2079 CB ALA A 269 -9.026 24.146 51.777 1.00 42.37 ATOM 2080 N SER A 270 -10.674 20.984 51.889 1.00 43.22 ATOM 2081 CA SER A 270 -11.768 20.302 51.298 1.00 42.91 ATOM 2082 C SER A 270 -12.849 19.923 52.343 1.00 43.35 ATOM 2083 O SER A 270 -12.496 19.429 53.423 1.00 43.05 ATOM 2084 CB SER A 270 -11.465 18.915 50.632 1.00 40.62 ATOM 2085 N PRO A 271 -14.078 20.065 51.859 1.00 43.58 ATOM 2086 CA PRO A 271 -15.322 19.656 52.469 1.00 44.93 ATOM 2087 C PRO A 271 -15.608 18.135 52.272 1.00 46.11 ATOM 2088 O PRO A 271 -16.396 17.416 52.957 1.00 45.88 ATOM 2089 CB PRO A 271 -16.409 20.403 51.701 1.00 44.76 ATOM 2090 CG PRO A 271 -15.740 21.277 50.673 1.00 44.50 ATOM 2091 CD PRO A 271 -14.364 20.644 50.508 1.00 45.24 ATOM 2092 N ASN A 272 -14.931 17.669 51.192 1.00 45.16 ATOM 2093 CA ASN A 272 -15.043 16.289 50.724 1.00 42.93 ATOM 2094 C ASN A 272 -14.045 15.401 51.386 1.00 42.70 ATOM 2095 O ASN A 272 -13.704 14.487 50.584 1.00 45.22 ATOM 2096 CB ASN A 272 -14.848 16.392 49.181 1.00 42.30 ATOM 2097 CG ASN A 272 -15.725 17.476 48.559 1.00 44.10 ATOM 2098 OD1 ASN A 272 -16.959 17.144 48.563 1.00 47.06 ATOM 2099 ND2 ASN A 272 -15.391 18.648 48.007 1.00 39.66 ATOM 2100 N LYS A 273 -13.520 15.407 52.562 1.00 41.00 ATOM 2101 CA LYS A 273 -12.469 14.490 52.986 1.00 42.06 ATOM 2102 C LYS A 273 -12.782 13.002 52.998 1.00 43.32 ATOM 2103 O LYS A 273 -11.857 12.142 52.841 1.00 42.20 ATOM 2104 CB LYS A 273 -11.900 14.710 54.439 1.00 43.03 ATOM 2105 CG LYS A 273 -11.513 16.145 54.722 1.00 45.48 ATOM 2106 CD LYS A 273 -10.383 16.409 55.668 1.00 48.86 ATOM 2107 CE LYS A 273 -9.622 17.733 55.521 1.00 50.21 ATOM 2108 NZ LYS A 273 -10.427 18.974 55.546 1.00 49.62 ATOM 2109 N GLU A 274 -14.037 12.756 53.387 1.00 43.25 ATOM 2110 CA GLU A 274 -14.614 11.429 53.561 1.00 42.62 ATOM 2111 C GLU A 274 -14.795 10.793 52.185 1.00 40.74 ATOM 2112 O GLU A 274 -14.399 9.598 52.123 1.00 41.76 ATOM 2113 CB GLU A 274 -15.877 11.346 54.394 1.00 48.11 ATOM 2114 CG GLU A 274 -16.042 10.283 55.493 1.00 54.86 ATOM 2115 CD GLU A 274 -14.965 9.645 56.302 1.00 58.92 ATOM 2116 OE1 GLU A 274 -14.268 10.182 57.198 1.00 60.51 ATOM 2117 OE2 GLU A 274 -14.739 8.388 56.039 1.00 60.94 ATOM 2118 N LEU A 275 -15.257 11.520 51.219 1.00 39.62 ATOM 2119 CA LEU A 275 -15.412 11.112 49.825 1.00 39.50 ATOM 2120 C LEU A 275 -14.028 10.689 49.243 1.00 39.07 ATOM 2121 O LEU A 275 -13.788 9.699 48.572 1.00 38.33 ATOM 2122 CB LEU A 275 -15.907 12.298 48.955 1.00 38.16 ATOM 2123 CG LEU A 275 -17.327 12.817 49.256 1.00 39.52 ATOM 2124 CD1 LEU A 275 -17.909 13.672 48.135 1.00 38.49 ATOM 2125 CD2 LEU A 275 -18.154 11.563 49.498 1.00 37.75 ATOM 2126 N ALA A 276 -13.120 11.633 49.513 1.00 38.83 ATOM 2127 CA ALA A 276 -11.702 11.588 49.132 1.00 36.98 ATOM 2128 C ALA A 276 -11.144 10.306 49.704 1.00 36.67 ATOM 2129 O ALA A 276 -10.607 9.457 48.947 1.00 33.27 ATOM 2130 CB ALA A 276 -11.019 12.876 49.554 1.00 38.64 ATOM 2131 N LYS A 277 -11.309 10.147 51.027 1.00 35.90 ATOM 2132 CA LYS A 277 -10.777 8.868 51.586 1.00 37.91 ATOM 2133 C LYS A 277 -11.454 7.676 50.949 1.00 38.29 ATOM 2134 O LYS A 277 -10.809 6.623 50.629 1.00 37.92 ATOM 2135 CB LYS A 277 -10.741 8.899 53.126 1.00 38.85 ATOM 2136 CG LYS A 277 -11.789 8.234 53.903 1.00 45.72 ATOM 2137 CD LYS A 277 -11.668 7.757 55.368 1.00 48.11 ATOM 2138 CE LYS A 277 -10.603 6.716 55.618 1.00 51.36 ATOM 2139 NZ LYS A 277 -10.590 5.849 56.824 1.00 52.97 ATOM 2140 N GLU A 278 -12.758 7.680 50.686 1.00 40.78 ATOM 2141 CA GLU A 278 -13.426 6.473 50.118 1.00 42.39 ATOM 2142 C GLU A 278 -12.737 6.072 48.794 1.00 40.26 ATOM 2143 O GLU A 278 -12.314 4.902 48.625 1.00 40.14 ATOM 2144 CB GLU A 278 -14.910 6.551 49.925 1.00 49.14 ATOM 2145 CG GLU A 278 -15.988 6.804 50.903 1.00 55.93 ATOM 2146 CD GLU A 278 -16.030 6.404 52.323 1.00 62.04 ATOM 2147 OE1 GLU A 278 -15.439 5.323 52.676 1.00 63.86 ATOM 2148 OE2 GLU A 278 -16.639 7.166 53.133 1.00 64.36 ATOM 2149 N PHE A 279 -12.649 7.017 47.919 1.00 38.70 ATOM 2150 CA PHE A 279 -11.991 7.033 46.593 1.00 37.81 ATOM 2151 C PHE A 279 -10.583 6.454 46.585 1.00 36.25 ATOM 2152 O PHE A 279 -10.178 5.561 45.830 1.00 37.28 ATOM 2153 CB PHE A 279 -11.948 8.508 46.041 1.00 37.03 ATOM 2154 CG PHE A 279 -11.338 8.534 44.654 1.00 38.73 ATOM 2155 CD1 PHE A 279 -9.957 8.655 44.503 1.00 38.71 ATOM 2156 CD2 PHE A 279 -12.142 8.363 43.535 1.00 41.56 ATOM 2157 CE1 PHE A 279 -9.404 8.683 43.240 1.00 39.71 ATOM 2158 CE2 PHE A 279 -11.602 8.360 42.230 1.00 43.00 ATOM 2159 CZ PHE A 279 -10.201 8.513 42.107 1.00 41.76 ATOM 2160 N LEU A 280 -9.746 7.010 47.461 1.00 34.49 ATOM 2161 CA LEU A 280 -8.387 6.578 47.511 1.00 33.06 ATOM 2162 C LEU A 280 -8.330 5.157 48.001 1.00 36.38 ATOM 2163 O LEU A 280 -7.788 4.329 47.233 1.00 37.77 ATOM 2164 CB LEU A 280 -7.572 7.588 48.339 1.00 30.09 ATOM 2165 CG LEU A 280 -7.410 8.935 47.632 1.00 29.88 ATOM 2166 CD1 LEU A 280 -6.724 9.939 48.558 1.00 27.36 ATOM 2167 CD2 LEU A 280 -6.569 8.781 46.324 1.00 29.42 ATOM 2168 N GLU A 281 -8.780 4.935 49.242 1.00 37.69 ATOM 2169 CA GLU A 281 -8.660 3.587 49.864 1.00 36.83 ATOM 2170 C GLU A 281 -9.485 2.456 49.285 1.00 36.15 ATOM 2171 O GLU A 281 -9.044 1.295 49.327 1.00 35.94 ATOM 2172 CB GLU A 281 -9.027 3.693 51.337 1.00 39.75 ATOM 2173 CG GLU A 281 -8.690 5.011 52.086 1.00 40.65 ATOM 2174 CD GLU A 281 -8.877 4.652 53.550 1.00 44.73 ATOM 2175 OE1 GLU A 281 -9.538 3.637 53.834 1.00 47.00 ATOM 2176 OE2 GLU A 281 -8.357 5.377 54.389 1.00 46.11 ATOM 2177 N ASN A 282 -10.677 2.777 48.764 1.00 36.66 ATOM 2178 CA ASN A 282 -11.578 1.802 48.175 1.00 37.18 ATOM 2179 C ASN A 282 -11.711 1.751 46.640 1.00 35.96 ATOM 2180 O ASN A 282 -12.282 0.683 46.271 1.00 34.56 ATOM 2181 CB ASN A 282 -13.022 1.930 48.739 1.00 38.18 ATOM 2182 CG ASN A 282 -13.017 1.779 50.257 1.00 38.66 ATOM 2183 OD1 ASN A 282 -12.149 1.147 50.924 1.00 40.16 ATOM 2184 ND2 ASN A 282 -14.022 2.539 50.740 1.00 40.19 ATOM 2185 N TYR A 283 -11.283 2.730 45.876 1.00 35.92 ATOM 2186 CA TYR A 283 -11.367 2.738 44.404 1.00 35.40 ATOM 2187 C TYR A 283 -9.988 2.624 43.743 1.00 34.40 ATOM 2188 O TYR A 283 -9.666 1.634 43.014 1.00 33.01 ATOM 2189 CB TYR A 283 -12.176 3.951 43.817 1.00 40.10 ATOM 2190 CG TYR A 283 -13.662 3.660 44.006 1.00 44.33 ATOM 2191 CD1 TYR A 283 -14.239 3.840 45.281 1.00 46.92 ATOM 2192 CD2 TYR A 283 -14.428 3.062 43.009 1.00 46.04 ATOM 2193 CE1 TYR A 283 -15.582 3.495 45.510 1.00 49.80 ATOM 2194 CE2 TYR A 283 -15.772 2.706 43.214 1.00 47.35 ATOM 2195 CZ TYR A 283 -16.335 2.941 44.458 1.00 48.23 ATOM 2196 OH TYR A 283 -17.624 2.610 44.675 1.00 49.84 ATOM 2197 N LEU A 284 -9.165 3.656 44.047 1.00 32.87 ATOM 2198 CA LEU A 284 -7.787 3.707 43.461 1.00 29.50 ATOM 2199 C LEU A 284 -6.847 2.731 44.094 1.00 26.56 ATOM 2200 O LEU A 284 -6.220 1.955 43.393 1.00 28.11 ATOM 2201 CB LEU A 284 -7.256 5.122 43.620 1.00 26.55 ATOM 2202 CG LEU A 284 -5.918 5.225 42.843 1.00 26.19 ATOM 2203 CD1 LEU A 284 -6.078 5.279 41.343 1.00 27.65 ATOM 2204 CD2 LEU A 284 -5.355 6.544 43.320 1.00 24.64 ATOM 2205 N LEU A 285 -6.735 2.718 45.364 1.00 26.19 ATOM 2206 CA LEU A 285 -5.788 1.822 46.006 1.00 28.57 ATOM 2207 C LEU A 285 -6.254 0.361 46.076 1.00 30.35 ATOM 2208 O LEU A 285 -6.161 -0.462 47.034 1.00 31.83 ATOM 2209 CB LEU A 285 -5.302 2.512 47.291 1.00 29.05 ATOM 2210 CG LEU A 285 -4.241 3.615 47.262 1.00 29.33 ATOM 2211 CD1 LEU A 285 -3.926 4.306 48.595 1.00 23.75 ATOM 2212 CD2 LEU A 285 -2.987 2.897 46.646 1.00 30.26 ATOM 2213 N THR A 286 -6.686 -0.172 44.956 1.00 31.16 ATOM 2214 CA THR A 286 -7.062 -1.573 44.761 1.00 33.00 ATOM 2215 C THR A 286 -6.247 -2.173 43.628 1.00 32.28 ATOM 2216 O THR A 286 -5.546 -1.422 42.915 1.00 35.56 ATOM 2217 CB THR A 286 -8.610 -1.626 44.457 1.00 35.25 ATOM 2218 OG1 THR A 286 -8.940 -0.770 43.247 1.00 36.89 ATOM 2219 CG2 THR A 286 -9.424 -1.310 45.717 1.00 34.72 ATOM 2220 N ASP A 287 -6.335 -3.394 43.257 1.00 31.15 ATOM 2221 CA ASP A 287 -5.615 -3.992 42.090 1.00 29.63 ATOM 2222 C ASP A 287 -6.251 -3.449 40.830 1.00 30.14 ATOM 2223 O ASP A 287 -5.604 -3.231 39.826 1.00 32.00 ATOM 2224 CB ASP A 287 -5.783 -5.474 42.093 1.00 28.32 ATOM 2225 CG ASP A 287 -4.857 -6.257 42.894 1.00 29.50 ATOM 2226 OD1 ASP A 287 -3.964 -5.869 43.651 1.00 34.03 ATOM 2227 OD2 ASP A 287 -4.943 -7.510 42.795 1.00 37.41 ATOM 2228 N GLU A 288 -7.527 -3.207 40.859 1.00 29.72 ATOM 2229 CA GLU A 288 -8.272 -2.773 39.704 1.00 29.98 ATOM 2230 C GLU A 288 -8.070 -1.349 39.360 1.00 28.84 ATOM 2231 O GLU A 288 -7.990 -0.979 38.214 1.00 28.48 ATOM 2232 CB GLU A 288 -9.763 -3.091 40.042 1.00 37.35 ATOM 2233 CG GLU A 288 -9.850 -4.526 40.748 1.00 44.73 ATOM 2234 CD GLU A 288 -9.924 -4.639 42.230 1.00 46.60 ATOM 2235 OE1 GLU A 288 -10.822 -4.088 42.914 1.00 49.73 ATOM 2236 OE2 GLU A 288 -9.005 -5.284 42.811 1.00 49.22 ATOM 2237 N GLY A 289 -8.018 -0.494 40.387 1.00 29.56 ATOM 2238 CA GLY A 289 -7.837 0.952 40.193 1.00 25.68 ATOM 2239 C GLY A 289 -6.412 1.242 39.721 1.00 23.46 ATOM 2240 O GLY A 289 -6.266 2.082 38.842 1.00 21.86 ATOM 2241 N LEU A 290 -5.467 0.581 40.333 1.00 24.53 ATOM 2242 CA LEU A 290 -4.048 0.766 39.984 1.00 25.64 ATOM 2243 C LEU A 290 -3.820 0.327 38.525 1.00 27.65 ATOM 2244 O LEU A 290 -3.054 1.002 37.827 1.00 25.48 ATOM 2245 CB LEU A 290 -3.097 0.061 40.939 1.00 25.31 ATOM 2246 CG LEU A 290 -3.065 0.710 42.320 1.00 21.12 ATOM 2247 CD1 LEU A 290 -2.060 0.014 43.162 1.00 25.13 ATOM 2248 CD2 LEU A 290 -2.700 2.175 42.059 1.00 23.36 ATOM 2249 N GLU A 291 -4.522 -0.760 38.197 1.00 28.25 ATOM 2250 CA GLU A 291 -4.331 -1.223 36.809 1.00 30.34 ATOM 2251 C GLU A 291 -4.958 -0.340 35.773 1.00 26.80 ATOM 2252 O GLU A 291 -4.244 -0.277 34.741 1.00 27.44 ATOM 2253 CB GLU A 291 -4.723 -2.660 36.673 1.00 37.38 ATOM 2254 CG GLU A 291 -6.119 -3.025 36.307 1.00 48.46 ATOM 2255 CD GLU A 291 -6.107 -4.144 35.238 1.00 51.59 ATOM 2256 OE1 GLU A 291 -5.251 -4.041 34.367 1.00 52.16 ATOM 2257 OE2 GLU A 291 -7.013 -4.937 35.596 1.00 55.82 ATOM 2258 N ALA A 292 -6.011 0.381 35.919 1.00 26.00 ATOM 2259 CA ALA A 292 -6.599 1.309 34.980 1.00 24.71 ATOM 2260 C ALA A 292 -5.612 2.429 34.710 1.00 24.42 ATOM 2261 O ALA A 292 -5.495 3.014 33.671 1.00 25.84 ATOM 2262 CB ALA A 292 -7.849 2.025 35.525 1.00 22.58 ATOM 2263 N VAL A 293 -4.947 2.863 35.804 1.00 24.74 ATOM 2264 CA VAL A 293 -3.960 3.949 35.776 1.00 24.38 ATOM 2265 C VAL A 293 -2.691 3.445 35.028 1.00 24.89 ATOM 2266 O VAL A 293 -2.315 4.198 34.145 1.00 24.06 ATOM 2267 CB VAL A 293 -3.603 4.576 37.173 1.00 25.65 ATOM 2268 CG1 VAL A 293 -2.513 5.659 37.025 1.00 23.87 ATOM 2269 CG2 VAL A 293 -4.805 5.145 37.936 1.00 23.92 ATOM 2270 N ASN A 294 -2.102 2.329 35.426 1.00 25.24 ATOM 2271 CA ASN A 294 -0.915 1.724 34.907 1.00 26.72 ATOM 2272 C ASN A 294 -1.022 1.378 33.429 1.00 27.44 ATOM 2273 O ASN A 294 -0.039 1.442 32.707 1.00 30.55 ATOM 2274 CB ASN A 294 -0.467 0.549 35.769 1.00 28.51 ATOM 2275 CG ASN A 294 0.957 0.042 35.487 1.00 29.07 ATOM 2276 OD1 ASN A 294 1.941 0.567 36.010 1.00 27.38 ATOM 2277 ND2 ASN A 294 1.076 -1.064 34.709 1.00 26.93 ATOM 2278 N LYS A 295 -2.147 1.095 32.877 1.00 31.09 ATOM 2279 CA LYS A 295 -2.392 0.796 31.438 1.00 32.69 ATOM 2280 C LYS A 295 -2.311 2.118 30.687 1.00 32.30 ATOM 2281 O LYS A 295 -1.805 2.078 29.521 1.00 35.27 ATOM 2282 CB LYS A 295 -3.620 -0.007 31.173 1.00 38.08 ATOM 2283 CG LYS A 295 -5.010 0.545 31.222 1.00 45.95 ATOM 2284 CD LYS A 295 -5.207 1.810 30.430 1.00 53.62 ATOM 2285 CE LYS A 295 -5.866 1.701 29.042 1.00 58.68 ATOM 2286 NZ LYS A 295 -5.791 3.031 28.290 1.00 60.11 ATOM 2287 N ASP A 296 -2.655 3.230 31.299 1.00 27.71 ATOM 2288 CA ASP A 296 -2.508 4.559 30.693 1.00 26.59 ATOM 2289 C ASP A 296 -1.019 4.914 30.677 1.00 26.02 ATOM 2290 O ASP A 296 -0.379 4.858 29.537 1.00 26.93 ATOM 2291 CB ASP A 296 -3.521 5.513 31.323 1.00 25.58 ATOM 2292 CG ASP A 296 -3.400 6.903 30.810 1.00 25.34 ATOM 2293 OD1 ASP A 296 -2.797 7.103 29.709 1.00 28.67 ATOM 2294 OD2 ASP A 296 -3.876 7.876 31.403 1.00 28.14 ATOM 2295 N LYS A 297 -0.406 5.212 31.797 1.00 22.68 ATOM 2296 CA LYS A 297 1.080 5.467 31.890 1.00 21.42 ATOM 2297 C LYS A 297 1.601 4.594 32.970 1.00 19.90 ATOM 2298 O LYS A 297 1.072 4.664 34.082 1.00 22.20 ATOM 2299 CB LYS A 297 1.387 6.934 32.106 1.00 20.77 ATOM 2300 CG LYS A 297 1.156 7.719 30.830 1.00 27.53 ATOM 2301 CD LYS A 297 0.924 9.146 31.231 1.00 37.26 ATOM 2302 CE LYS A 297 1.243 10.145 30.095 1.00 40.57 ATOM 2303 NZ LYS A 297 0.298 11.370 30.255 1.00 40.85 ATOM 2304 N PRO A 298 2.541 3.703 32.818 1.00 20.53 ATOM 2305 CA PRO A 298 3.008 2.820 33.878 1.00 19.54 ATOM 2306 C PRO A 298 3.414 3.560 35.118 1.00 19.85 ATOM 2307 O PRO A 298 4.078 4.613 35.073 1.00 17.94 ATOM 2308 CB PRO A 298 4.232 2.071 33.279 1.00 20.51 ATOM 2309 CG PRO A 298 3.950 2.193 31.754 1.00 21.20 ATOM 2310 CD PRO A 298 3.236 3.493 31.541 1.00 19.27 ATOM 2311 N LEU A 299 3.063 2.999 36.294 1.00 21.08 ATOM 2312 CA LEU A 299 3.416 3.623 37.573 1.00 20.11 ATOM 2313 C LEU A 299 4.800 3.335 38.103 1.00 18.73 ATOM 2314 O LEU A 299 5.328 4.166 38.931 1.00 21.38 ATOM 2315 CB LEU A 299 2.293 3.221 38.595 1.00 21.52 ATOM 2316 CG LEU A 299 0.905 3.759 38.505 1.00 23.94 ATOM 2317 CD1 LEU A 299 -0.003 2.900 39.450 1.00 23.54 ATOM 2318 CD2 LEU A 299 0.775 5.218 38.927 1.00 23.25 ATOM 2319 N GLY A 300 5.415 2.227 37.820 1.00 18.95 ATOM 2320 CA GLY A 300 6.682 1.825 38.400 1.00 18.40 ATOM 2321 C GLY A 300 6.217 0.644 39.370 1.00 21.72 ATOM 2322 O GLY A 300 5.184 -0.025 39.094 1.00 21.48 ATOM 2323 N ALA A 301 6.969 0.573 40.435 1.00 20.58 ATOM 2324 CA ALA A 301 6.747 -0.450 41.501 1.00 22.75 ATOM 2325 C ALA A 301 5.612 0.062 42.332 1.00 24.25 ATOM 2326 O ALA A 301 5.787 1.241 42.731 1.00 27.75 ATOM 2327 CB ALA A 301 8.096 -0.623 42.262 1.00 19.62 ATOM 2328 N VAL A 302 4.447 -0.486 42.576 1.00 22.94 ATOM 2329 CA VAL A 302 3.308 0.029 43.321 1.00 22.51 ATOM 2330 C VAL A 302 3.453 -0.272 44.814 1.00 24.21 ATOM 2331 O VAL A 302 4.165 -1.226 45.222 1.00 25.58 ATOM 2332 CB VAL A 302 1.965 -0.486 42.789 1.00 22.57 ATOM 2333 CG1 VAL A 302 1.630 0.027 41.392 1.00 21.36 ATOM 2334 CG2 VAL A 302 1.834 -2.009 42.858 1.00 22.06 ATOM 2335 N ALA A 303 2.851 0.594 45.621 1.00 24.53 ATOM 2336 CA ALA A 303 2.990 0.304 47.105 1.00 25.60 ATOM 2337 C ALA A 303 2.036 -0.790 47.559 1.00 25.64 ATOM 2338 O ALA A 303 2.251 -1.349 48.674 1.00 28.64 ATOM 2339 CB ALA A 303 2.774 1.599 47.836 1.00 23.88 ATOM 2340 N LEU A 304 1.004 -1.086 46.781 1.00 27.46 ATOM 2341 CA LEU A 304 -0.010 -2.147 47.065 1.00 27.72 ATOM 2342 C LEU A 304 0.647 -3.500 46.766 1.00 27.24 ATOM 2343 O LEU A 304 1.040 -3.874 45.640 1.00 23.14 ATOM 2344 CB LEU A 304 -1.264 -1.817 46.297 1.00 29.54 ATOM 2345 CG LEU A 304 -2.545 -2.572 46.617 1.00 30.50 ATOM 2346 CD1 LEU A 304 -2.974 -2.027 48.009 1.00 29.34 ATOM 2347 CD2 LEU A 304 -3.611 -2.399 45.497 1.00 27.41 ATOM 2348 N LYS A 305 0.812 -4.212 47.913 1.00 26.72 ATOM 2349 CA LYS A 305 1.515 -5.508 47.763 1.00 28.47 ATOM 2350 C LYS A 305 0.967 -6.501 46.763 1.00 26.16 ATOM 2351 O LYS A 305 1.744 -7.252 46.111 1.00 26.59 ATOM 2352 CB LYS A 305 1.663 -6.173 49.180 1.00 28.60 ATOM 2353 CG LYS A 305 2.661 -5.297 49.928 1.00 30.41 ATOM 2354 CD LYS A 305 3.182 -5.810 51.200 1.00 33.73 ATOM 2355 CE LYS A 305 2.175 -5.714 52.341 1.00 37.16 ATOM 2356 NZ LYS A 305 2.999 -5.859 53.618 1.00 41.24 ATOM 2357 N SER A 306 -0.312 -6.605 46.670 1.00 28.46 ATOM 2358 CA SER A 306 -1.097 -7.541 45.872 1.00 29.48 ATOM 2359 C SER A 306 -0.832 -7.318 44.395 1.00 31.28 ATOM 2360 O SER A 306 -0.484 -8.285 43.702 1.00 33.56 ATOM 2361 CB SER A 306 -2.552 -7.435 46.223 1.00 28.01 ATOM 2362 OG SER A 306 -3.118 -6.173 45.893 1.00 32.04 ATOM 2363 N TYR A 307 -1.015 -6.083 43.949 1.00 31.97 ATOM 2364 CA TYR A 307 -0.698 -5.624 42.578 1.00 30.91 ATOM 2365 C TYR A 307 0.791 -5.683 42.253 1.00 29.77 ATOM 2366 O TYR A 307 1.277 -6.132 41.143 1.00 28.61 ATOM 2367 CB TYR A 307 -1.365 -4.238 42.325 1.00 32.07 ATOM 2368 CG TYR A 307 -1.352 -3.935 40.844 1.00 32.85 ATOM 2369 CD1 TYR A 307 -1.994 -4.847 39.981 1.00 36.61 ATOM 2370 CD2 TYR A 307 -0.686 -2.860 40.277 1.00 35.39 ATOM 2371 CE1 TYR A 307 -2.067 -4.621 38.568 1.00 35.89 ATOM 2372 CE2 TYR A 307 -0.669 -2.645 38.872 1.00 35.31 ATOM 2373 CZ TYR A 307 -1.361 -3.507 38.040 1.00 37.14 ATOM 2374 OH TYR A 307 -1.375 -3.355 36.667 1.00 37.46 ATOM 2375 N GLU A 308 1.649 -5.278 43.239 1.00 29.32 ATOM 2376 CA GLU A 308 3.065 -5.247 43.026 1.00 28.64 ATOM 2377 C GLU A 308 3.610 -6.617 42.657 1.00 33.09 ATOM 2378 O GLU A 308 4.621 -6.864 41.933 1.00 32.77 ATOM 2379 CB GLU A 308 3.891 -4.787 44.221 1.00 26.96 ATOM 2380 CG GLU A 308 5.383 -4.841 43.820 1.00 24.83 ATOM 2381 CD GLU A 308 5.774 -4.031 42.630 1.00 25.19 ATOM 2382 OE1 GLU A 308 4.991 -3.310 42.009 1.00 23.32 ATOM 2383 OE2 GLU A 308 6.919 -4.141 42.238 1.00 27.76 ATOM 2384 N GLU A 309 2.893 -7.543 43.308 1.00 35.06 ATOM 2385 CA GLU A 309 3.155 -8.995 43.123 1.00 37.44 ATOM 2386 C GLU A 309 2.998 -9.439 41.661 1.00 37.07 ATOM 2387 O GLU A 309 3.728 -10.263 41.128 1.00 34.96 ATOM 2388 CB GLU A 309 2.189 -9.793 44.025 1.00 37.46 ATOM 2389 CG GLU A 309 2.880 -10.925 44.714 1.00 44.63 ATOM 2390 CD GLU A 309 2.068 -12.118 45.138 1.00 48.24 ATOM 2391 OE1 GLU A 309 1.735 -12.801 44.112 1.00 53.82 ATOM 2392 OE2 GLU A 309 1.823 -12.321 46.298 1.00 49.26 ATOM 2393 N GLU A 310 2.017 -8.864 40.962 1.00 39.26 ATOM 2394 CA GLU A 310 1.764 -9.191 39.578 1.00 41.74 ATOM 2395 C GLU A 310 2.656 -8.346 38.653 1.00 42.96 ATOM 2396 O GLU A 310 2.921 -8.757 37.461 1.00 44.07 ATOM 2397 CB GLU A 310 0.309 -8.931 39.241 1.00 45.99 ATOM 2398 CG GLU A 310 -0.789 -9.197 40.255 1.00 53.78 ATOM 2399 CD GLU A 310 -2.179 -8.698 39.844 1.00 59.50 ATOM 2400 OE1 GLU A 310 -2.717 -8.676 38.705 1.00 60.18 ATOM 2401 OE2 GLU A 310 -2.827 -8.282 40.881 1.00 62.13 ATOM 2402 N LEU A 311 3.084 -7.207 39.223 1.00 40.62 ATOM 2403 CA LEU A 311 3.889 -6.214 38.434 1.00 39.00 ATOM 2404 C LEU A 311 5.326 -6.610 38.299 1.00 39.37 ATOM 2405 O LEU A 311 6.065 -6.264 37.292 1.00 34.71 ATOM 2406 CB LEU A 311 3.657 -4.868 39.117 1.00 33.62 ATOM 2407 CG LEU A 311 3.140 -3.751 38.278 1.00 33.27 ATOM 2408 CD1 LEU A 311 2.114 -4.208 37.284 1.00 27.90 ATOM 2409 CD2 LEU A 311 2.629 -2.765 39.332 1.00 32.20 ATOM 2410 N ALA A 312 5.986 -7.363 39.288 1.00 41.27 ATOM 2411 CA ALA A 312 7.269 -7.450 38.545 1.00 44.77 ATOM 2412 C ALA A 312 8.251 -8.500 38.936 1.00 44.68 ATOM 2413 O ALA A 312 8.734 -8.336 39.979 1.00 46.80 ATOM 2414 CB ALA A 312 7.777 -6.068 38.273 1.00 48.19 ATOM 2415 N LYS A 313 8.156 -9.396 38.067 1.00 43.40 ATOM 2416 CA LYS A 313 8.227 -10.300 37.018 1.00 42.92 ATOM 2417 C LYS A 313 8.569 -9.603 35.665 1.00 39.72 ATOM 2418 O LYS A 313 9.305 -10.134 34.786 1.00 41.92 ATOM 2419 CB LYS A 313 6.891 -11.060 36.777 1.00 44.36 ATOM 2420 CG LYS A 313 5.952 -10.884 37.952 1.00 49.80 ATOM 2421 CD LYS A 313 5.825 -12.118 38.858 1.00 52.47 ATOM 2422 CE LYS A 313 4.562 -12.114 39.716 1.00 55.24 ATOM 2423 NZ LYS A 313 3.415 -12.979 39.329 1.00 56.79 ATOM 2424 N ASP A 314 8.024 -8.387 35.642 1.00 35.61 ATOM 2425 CA ASP A 314 8.286 -7.512 34.442 1.00 33.24 ATOM 2426 C ASP A 314 9.745 -7.066 34.563 1.00 29.14 ATOM 2427 O ASP A 314 10.013 -6.527 35.645 1.00 30.71 ATOM 2428 CB ASP A 314 7.254 -6.424 34.302 1.00 32.83 ATOM 2429 CG ASP A 314 7.333 -5.527 33.083 1.00 31.36 ATOM 2430 OD1 ASP A 314 8.328 -5.335 32.400 1.00 32.19 ATOM 2431 OD2 ASP A 314 6.273 -4.868 32.813 1.00 36.91 ATOM 2432 N PRO A 315 10.593 -7.339 33.620 1.00 26.01 ATOM 2433 CA PRO A 315 11.969 -6.984 33.705 1.00 26.03 ATOM 2434 C PRO A 315 12.179 -5.436 33.819 1.00 23.11 ATOM 2435 O PRO A 315 13.263 -5.094 34.330 1.00 22.58 ATOM 2436 CB PRO A 315 12.623 -7.677 32.498 1.00 27.67 ATOM 2437 CG PRO A 315 11.515 -7.875 31.498 1.00 27.58 ATOM 2438 CD PRO A 315 10.271 -8.078 32.357 1.00 28.10 ATOM 2439 N ARG A 316 11.332 -4.648 33.311 1.00 22.71 ATOM 2440 CA ARG A 316 11.319 -3.160 33.354 1.00 22.46 ATOM 2441 C ARG A 316 11.155 -2.735 34.803 1.00 22.51 ATOM 2442 O ARG A 316 11.915 -1.871 35.253 1.00 21.69 ATOM 2443 CB ARG A 316 10.260 -2.542 32.458 1.00 24.55 ATOM 2444 CG ARG A 316 10.691 -2.863 30.985 1.00 21.61 ATOM 2445 CD ARG A 316 9.735 -2.366 30.018 1.00 24.42 ATOM 2446 NE ARG A 316 8.379 -2.720 30.358 1.00 25.62 ATOM 2447 CZ ARG A 316 7.185 -2.364 30.006 1.00 25.75 ATOM 2448 NH1 ARG A 316 6.836 -1.422 29.045 1.00 30.76 ATOM 2449 NH2 ARG A 316 6.105 -2.832 30.689 1.00 28.63 ATOM 2450 N ILE A 317 10.236 -3.380 35.444 1.00 22.14 ATOM 2451 CA ILE A 317 9.955 -3.207 36.885 1.00 24.72 ATOM 2452 C ILE A 317 11.108 -3.712 37.706 1.00 25.68 ATOM 2453 O ILE A 317 11.542 -3.141 38.744 1.00 23.31 ATOM 2454 CB ILE A 317 8.545 -3.721 37.276 1.00 24.64 ATOM 2455 CG1 ILE A 317 7.602 -2.632 36.661 1.00 27.94 ATOM 2456 CG2 ILE A 317 8.331 -3.748 38.821 1.00 26.99 ATOM 2457 CD1 ILE A 317 6.287 -2.506 37.381 1.00 32.96 ATOM 2458 N ALA A 318 11.694 -4.866 37.333 1.00 25.13 ATOM 2459 CA ALA A 318 12.849 -5.339 38.102 1.00 23.36 ATOM 2460 C ALA A 318 14.007 -4.370 38.042 1.00 23.40 ATOM 2461 O ALA A 318 14.815 -4.145 38.957 1.00 23.37 ATOM 2462 CB ALA A 318 13.251 -6.661 37.512 1.00 23.30 ATOM 2463 N ALA A 319 14.153 -3.736 36.877 1.00 22.32 ATOM 2464 CA ALA A 319 15.273 -2.783 36.728 1.00 20.47 ATOM 2465 C ALA A 319 15.031 -1.506 37.532 1.00 19.03 ATOM 2466 O ALA A 319 15.988 -0.886 38.018 1.00 18.75 ATOM 2467 CB ALA A 319 15.401 -2.551 35.186 1.00 20.41 ATOM 2468 N THR A 320 13.767 -1.139 37.572 1.00 18.38 ATOM 2469 CA THR A 320 13.277 0.029 38.327 1.00 21.40 ATOM 2470 C THR A 320 13.670 -0.163 39.815 1.00 22.53 ATOM 2471 O THR A 320 14.363 0.726 40.400 1.00 21.62 ATOM 2472 CB THR A 320 11.768 0.283 38.248 1.00 19.28 ATOM 2473 OG1 THR A 320 11.460 0.518 36.868 1.00 20.77 ATOM 2474 CG2 THR A 320 11.245 1.451 39.179 1.00 18.05 ATOM 2475 N MET A 321 13.266 -1.368 40.292 1.00 20.96 ATOM 2476 CA MET A 321 13.683 -1.771 41.680 1.00 24.11 ATOM 2477 C MET A 321 15.161 -1.849 41.922 1.00 21.99 ATOM 2478 O MET A 321 15.682 -1.460 43.030 1.00 21.03 ATOM 2479 CB MET A 321 12.995 -3.090 42.079 1.00 30.25 ATOM 2480 CG MET A 321 11.764 -2.723 42.942 1.00 38.08 ATOM 2481 SD MET A 321 10.835 -4.318 42.838 1.00 48.07 ATOM 2482 CE MET A 321 12.266 -5.373 43.270 1.00 43.91 ATOM 2483 N GLU A 322 15.956 -2.271 40.973 1.00 21.26 ATOM 2484 CA GLU A 322 17.376 -2.312 41.190 1.00 23.29 ATOM 2485 C GLU A 322 17.976 -0.899 41.271 1.00 22.41 ATOM 2486 O GLU A 322 18.891 -0.688 42.088 1.00 19.92 ATOM 2487 CB GLU A 322 18.023 -3.095 40.035 1.00 30.03 ATOM 2488 CG GLU A 322 19.541 -3.060 39.921 1.00 37.69 ATOM 2489 CD GLU A 322 20.162 -4.415 39.567 1.00 45.45 ATOM 2490 OE1 GLU A 322 19.203 -5.296 39.522 1.00 48.17 ATOM 2491 OE2 GLU A 322 21.410 -4.494 39.454 1.00 46.30 ATOM 2492 N ASN A 323 17.514 -0.002 40.380 1.00 19.96 ATOM 2493 CA ASN A 323 18.078 1.401 40.441 1.00 17.98 ATOM 2494 C ASN A 323 17.568 2.020 41.753 1.00 15.90 ATOM 2495 O ASN A 323 18.351 2.771 42.310 1.00 16.18 ATOM 2496 CB ASN A 323 17.536 2.106 39.181 1.00 17.12 ATOM 2497 CG ASN A 323 18.364 1.762 37.917 1.00 16.19 ATOM 2498 OD1 ASN A 323 19.605 1.915 37.947 1.00 18.44 ATOM 2499 ND2 ASN A 323 17.701 1.335 36.935 1.00 16.14 ATOM 2500 N ALA A 324 16.332 1.739 42.068 1.00 14.92 ATOM 2501 CA ALA A 324 15.781 2.283 43.340 1.00 17.28 ATOM 2502 C ALA A 324 16.592 1.898 44.556 1.00 19.22 ATOM 2503 O ALA A 324 16.921 2.638 45.484 1.00 19.87 ATOM 2504 CB ALA A 324 14.293 1.871 43.505 1.00 14.71 ATOM 2505 N GLN A 325 16.981 0.615 44.627 1.00 23.76 ATOM 2506 CA GLN A 325 17.836 -0.011 45.657 1.00 25.61 ATOM 2507 C GLN A 325 19.201 0.627 45.715 1.00 23.27 ATOM 2508 O GLN A 325 19.775 0.765 46.812 1.00 25.60 ATOM 2509 CB GLN A 325 17.900 -1.554 45.454 1.00 32.46 ATOM 2510 CG GLN A 325 16.660 -2.226 46.040 1.00 43.75 ATOM 2511 CD GLN A 325 16.714 -2.166 47.580 1.00 53.35 ATOM 2512 OE1 GLN A 325 15.653 -1.973 48.245 1.00 59.01 ATOM 2513 NE2 GLN A 325 17.880 -2.305 48.272 1.00 54.67 ATOM 2514 N LYS A 326 19.828 1.126 44.689 1.00 20.42 ATOM 2515 CA LYS A 326 21.067 1.790 44.632 1.00 19.27 ATOM 2516 C LYS A 326 20.910 3.291 44.881 1.00 20.63 ATOM 2517 O LYS A 326 21.901 3.981 45.005 1.00 23.89 ATOM 2518 CB LYS A 326 21.653 1.575 43.241 1.00 23.16 ATOM 2519 CG LYS A 326 21.650 0.073 43.090 1.00 26.63 ATOM 2520 CD LYS A 326 22.762 -0.662 42.509 1.00 35.11 ATOM 2521 CE LYS A 326 22.424 -1.084 41.014 1.00 36.66 ATOM 2522 NZ LYS A 326 23.461 -2.223 40.908 1.00 42.18 ATOM 2523 N GLY A 327 19.697 3.721 44.902 1.00 19.85 ATOM 2524 CA GLY A 327 19.441 5.115 45.103 1.00 20.10 ATOM 2525 C GLY A 327 19.154 5.384 46.581 1.00 21.75 ATOM 2526 O GLY A 327 19.465 4.636 47.514 1.00 24.65 ATOM 2527 N GLU A 328 18.465 6.465 46.792 1.00 21.74 ATOM 2528 CA GLU A 328 18.044 6.930 48.109 1.00 23.60 ATOM 2529 C GLU A 328 16.715 7.634 47.986 1.00 20.20 ATOM 2530 O GLU A 328 16.476 8.416 47.022 1.00 21.38 ATOM 2531 CB GLU A 328 19.183 7.684 48.695 1.00 26.99 ATOM 2532 CG GLU A 328 19.396 9.115 48.815 1.00 39.78 ATOM 2533 CD GLU A 328 20.252 9.452 50.039 1.00 46.04 ATOM 2534 OE1 GLU A 328 21.435 9.049 50.012 1.00 50.45 ATOM 2535 OE2 GLU A 328 19.593 10.113 50.924 1.00 51.26 ATOM 2536 N ILE A 329 15.835 7.278 48.865 1.00 18.47 ATOM 2537 CA ILE A 329 14.512 7.850 48.978 1.00 22.81 ATOM 2538 C ILE A 329 14.716 9.319 49.323 1.00 21.18 ATOM 2539 O ILE A 329 15.558 9.632 50.177 1.00 22.50 ATOM 2540 CB ILE A 329 13.705 7.175 50.148 1.00 26.47 ATOM 2541 CG1 ILE A 329 12.323 7.830 50.256 1.00 29.54 ATOM 2542 CG2 ILE A 329 14.590 7.436 51.445 1.00 32.85 ATOM 2543 CD1 ILE A 329 11.238 6.811 49.727 1.00 36.55 ATOM 2544 N MET A 330 14.004 10.230 48.720 1.00 20.31 ATOM 2545 CA MET A 330 14.214 11.676 48.984 1.00 16.70 ATOM 2546 C MET A 330 13.681 11.962 50.407 1.00 16.98 ATOM 2547 O MET A 330 12.640 11.384 50.844 1.00 16.93 ATOM 2548 CB MET A 330 13.283 12.426 47.958 1.00 17.18 ATOM 2549 CG MET A 330 13.995 12.330 46.582 1.00 15.84 ATOM 2550 SD MET A 330 13.001 13.363 45.444 1.00 20.01 ATOM 2551 CE MET A 330 11.719 12.344 44.943 1.00 12.57 ATOM 2552 N PRO A 331 14.291 12.952 50.977 1.00 18.16 ATOM 2553 CA PRO A 331 13.770 13.618 52.206 1.00 18.32 ATOM 2554 C PRO A 331 12.455 14.279 51.832 1.00 19.51 ATOM 2555 O PRO A 331 12.209 14.639 50.660 1.00 20.22 ATOM 2556 CB PRO A 331 14.789 14.752 52.417 1.00 19.06 ATOM 2557 CG PRO A 331 16.075 14.125 51.792 1.00 18.27 ATOM 2558 CD PRO A 331 15.469 13.674 50.428 1.00 16.86 ATOM 2559 N ASN A 332 11.459 14.570 52.699 1.00 19.62 ATOM 2560 CA ASN A 332 10.258 15.282 52.456 1.00 17.83 ATOM 2561 C ASN A 332 10.290 16.608 53.302 1.00 18.03 ATOM 2562 O ASN A 332 9.232 17.222 53.316 1.00 22.06 ATOM 2563 CB ASN A 332 9.029 14.515 52.841 1.00 20.22 ATOM 2564 CG ASN A 332 8.854 14.227 54.338 1.00 22.63 ATOM 2565 OD1 ASN A 332 9.548 14.684 55.223 1.00 23.08 ATOM 2566 ND2 ASN A 332 7.942 13.296 54.563 1.00 24.29 ATOM 2567 N ILE A 333 11.379 16.927 53.894 1.00 18.29 ATOM 2568 CA ILE A 333 11.546 18.150 54.734 1.00 19.45 ATOM 2569 C ILE A 333 11.199 19.379 53.956 1.00 20.34 ATOM 2570 O ILE A 333 11.411 19.316 52.688 1.00 22.12 ATOM 2571 CB ILE A 333 12.992 18.159 55.330 1.00 19.92 ATOM 2572 CG1 ILE A 333 14.137 18.246 54.262 1.00 19.00 ATOM 2573 CG2 ILE A 333 13.258 16.958 56.270 1.00 20.24 ATOM 2574 CD1 ILE A 333 15.557 18.449 54.905 1.00 20.32 ATOM 2575 N PRO A 334 10.742 20.494 54.504 1.00 21.00 ATOM 2576 CA PRO A 334 10.381 21.727 53.790 1.00 19.32 ATOM 2577 C PRO A 334 11.540 22.259 52.966 1.00 20.33 ATOM 2578 O PRO A 334 11.331 22.939 51.910 1.00 21.17 ATOM 2579 CB PRO A 334 9.952 22.723 54.843 1.00 19.72 ATOM 2580 CG PRO A 334 9.422 21.727 55.895 1.00 20.09 ATOM 2581 CD PRO A 334 10.437 20.620 55.966 1.00 21.23 ATOM 2582 N GLN A 335 12.756 22.002 53.423 1.00 18.96 ATOM 2583 CA GLN A 335 13.949 22.471 52.725 1.00 20.55 ATOM 2584 C GLN A 335 14.166 21.791 51.347 1.00 22.35 ATOM 2585 O GLN A 335 15.045 22.355 50.651 1.00 20.15 ATOM 2586 CB GLN A 335 15.223 22.199 53.498 1.00 20.40 ATOM 2587 CG GLN A 335 15.280 23.111 54.677 1.00 23.71 ATOM 2588 CD GLN A 335 14.291 22.720 55.746 1.00 25.17 ATOM 2589 OE1 GLN A 335 13.994 23.690 56.476 1.00 32.46 ATOM 2590 NE2 GLN A 335 13.784 21.532 56.025 1.00 20.49 ATOM 2591 N MET A 336 13.451 20.729 50.982 1.00 22.07 ATOM 2592 CA MET A 336 13.616 20.128 49.599 1.00 20.90 ATOM 2593 C MET A 336 13.366 21.087 48.465 1.00 21.36 ATOM 2594 O MET A 336 14.124 21.061 47.422 1.00 20.28 ATOM 2595 CB MET A 336 12.756 18.876 49.491 1.00 21.12 ATOM 2596 CG MET A 336 13.469 17.755 50.231 1.00 20.43 ATOM 2597 SD MET A 336 15.148 17.364 49.709 1.00 21.75 ATOM 2598 CE MET A 336 14.873 16.592 48.118 1.00 19.22 ATOM 2599 N SER A 337 12.454 22.007 48.642 1.00 23.07 ATOM 2600 CA SER A 337 12.275 23.030 47.555 1.00 26.38 ATOM 2601 C SER A 337 13.459 23.994 47.358 1.00 24.84 ATOM 2602 O SER A 337 13.716 24.310 46.188 1.00 24.32 ATOM 2603 CB SER A 337 10.966 23.745 47.760 1.00 31.40 ATOM 2604 OG SER A 337 11.064 25.006 48.268 1.00 38.53 ATOM 2605 N ALA A 338 14.205 24.386 48.368 1.00 24.19 ATOM 2606 CA ALA A 338 15.379 25.239 48.263 1.00 23.24 ATOM 2607 C ALA A 338 16.494 24.444 47.576 1.00 21.74 ATOM 2608 O ALA A 338 17.150 25.014 46.682 1.00 23.09 ATOM 2609 CB ALA A 338 15.906 25.792 49.564 1.00 20.70 ATOM 2610 N PHE A 339 16.683 23.241 48.055 1.00 19.84 ATOM 2611 CA PHE A 339 17.666 22.328 47.454 1.00 18.27 ATOM 2612 C PHE A 339 17.401 22.246 45.941 1.00 16.85 ATOM 2613 O PHE A 339 18.367 22.430 45.171 1.00 18.64 ATOM 2614 CB PHE A 339 17.469 20.940 48.142 1.00 18.85 ATOM 2615 CG PHE A 339 18.221 19.836 47.385 1.00 20.26 ATOM 2616 CD1 PHE A 339 19.582 19.619 47.576 1.00 19.47 ATOM 2617 CD2 PHE A 339 17.458 19.027 46.477 1.00 18.45 ATOM 2618 CE1 PHE A 339 20.257 18.697 46.782 1.00 17.20 ATOM 2619 CE2 PHE A 339 18.192 18.002 45.816 1.00 19.23 ATOM 2620 CZ PHE A 339 19.569 17.878 45.945 1.00 17.43 ATOM 2621 N TRP A 340 16.183 21.910 45.546 1.00 15.64 ATOM 2622 CA TRP A 340 15.949 21.735 44.090 1.00 19.80 ATOM 2623 C TRP A 340 16.186 22.962 43.216 1.00 20.80 ATOM 2624 O TRP A 340 16.697 22.936 42.098 1.00 20.98 ATOM 2625 CB TRP A 340 14.495 21.162 43.854 1.00 17.62 ATOM 2626 CG TRP A 340 14.291 19.742 44.201 1.00 15.81 ATOM 2627 CD1 TRP A 340 13.279 19.189 44.932 1.00 14.78 ATOM 2628 CD2 TRP A 340 15.068 18.632 43.651 1.00 18.26 ATOM 2629 NE1 TRP A 340 13.440 17.803 44.912 1.00 17.80 ATOM 2630 CE2 TRP A 340 14.502 17.393 44.179 1.00 16.28 ATOM 2631 CE3 TRP A 340 16.170 18.505 42.762 1.00 17.79 ATOM 2632 CZ2 TRP A 340 14.979 16.167 43.781 1.00 15.58 ATOM 2633 CZ3 TRP A 340 16.668 17.262 42.442 1.00 17.99 ATOM 2634 CH2 TRP A 340 16.122 16.060 42.991 1.00 18.45 ATOM 2635 N TYR A 341 15.740 24.089 43.762 1.00 22.30 ATOM 2636 CA TYR A 341 15.927 25.330 42.894 1.00 25.19 ATOM 2637 C TYR A 341 17.370 25.692 42.838 1.00 21.63 ATOM 2638 O TYR A 341 17.865 26.038 41.768 1.00 19.50 ATOM 2639 CB TYR A 341 14.896 26.281 43.356 1.00 35.36 ATOM 2640 CG TYR A 341 14.871 27.314 44.362 1.00 45.18 ATOM 2641 CD1 TYR A 341 15.594 28.518 44.442 1.00 49.31 ATOM 2642 CD2 TYR A 341 13.886 27.066 45.347 1.00 51.69 ATOM 2643 CE1 TYR A 341 15.417 29.424 45.516 1.00 53.83 ATOM 2644 CE2 TYR A 341 13.678 27.934 46.430 1.00 55.99 ATOM 2645 CZ TYR A 341 14.456 29.107 46.487 1.00 56.86 ATOM 2646 OH TYR A 341 14.093 29.844 47.609 1.00 61.27 ATOM 2647 N ALA A 342 18.100 25.512 43.965 1.00 20.33 ATOM 2648 CA ALA A 342 19.563 25.805 43.940 1.00 16.66 ATOM 2649 C ALA A 342 20.297 24.884 43.000 1.00 18.51 ATOM 2650 O ALA A 342 21.172 25.300 42.165 1.00 16.46 ATOM 2651 CB ALA A 342 20.120 25.753 45.349 1.00 15.25 ATOM 2652 N VAL A 343 19.953 23.578 43.026 1.00 17.57 ATOM 2653 CA VAL A 343 20.668 22.598 42.167 1.00 17.31 ATOM 2654 C VAL A 343 20.255 22.793 40.710 1.00 16.83 ATOM 2655 O VAL A 343 21.038 22.608 39.807 1.00 15.53 ATOM 2656 CB VAL A 343 20.470 21.200 42.822 1.00 18.41 ATOM 2657 CG1 VAL A 343 20.916 20.136 41.843 1.00 20.17 ATOM 2658 CG2 VAL A 343 21.226 21.170 44.160 1.00 18.69 ATOM 2659 N ARG A 344 19.046 23.217 40.455 1.00 18.04 ATOM 2660 CA ARG A 344 18.563 23.495 39.101 1.00 21.04 ATOM 2661 C ARG A 344 19.387 24.631 38.497 1.00 20.30 ATOM 2662 O ARG A 344 19.953 24.397 37.377 1.00 22.22 ATOM 2663 CB ARG A 344 17.055 23.780 38.999 1.00 21.05 ATOM 2664 CG ARG A 344 16.604 23.919 37.501 1.00 26.33 ATOM 2665 CD ARG A 344 15.266 24.682 37.384 1.00 33.39 ATOM 2666 NE ARG A 344 14.475 24.564 38.574 1.00 41.20 ATOM 2667 CZ ARG A 344 13.872 23.412 38.933 1.00 44.60 ATOM 2668 NH1 ARG A 344 13.723 22.447 38.030 1.00 47.84 ATOM 2669 NH2 ARG A 344 13.311 23.204 40.149 1.00 50.39 ATOM 2670 N THR A 345 19.483 25.723 39.236 1.00 19.84 ATOM 2671 CA THR A 345 20.359 26.797 38.636 1.00 20.59 ATOM 2672 C THR A 345 21.767 26.382 38.316 1.00 23.30 ATOM 2673 O THR A 345 22.303 26.499 37.137 1.00 22.88 ATOM 2674 CB THR A 345 20.279 27.978 39.708 1.00 20.73 ATOM 2675 OG1 THR A 345 18.891 28.297 39.857 1.00 21.65 ATOM 2676 CG2 THR A 345 21.189 29.142 39.397 1.00 21.30 ATOM 2677 N ALA A 346 22.398 25.718 39.366 1.00 21.33 ATOM 2678 CA ALA A 346 23.787 25.284 39.285 1.00 20.71 ATOM 2679 C ALA A 346 24.077 24.516 38.043 1.00 19.84 ATOM 2680 O ALA A 346 25.096 24.591 37.351 1.00 23.05 ATOM 2681 CB ALA A 346 24.257 24.472 40.516 1.00 18.83 ATOM 2682 N VAL A 347 23.254 23.566 37.693 1.00 22.85 ATOM 2683 CA VAL A 347 23.544 22.641 36.539 1.00 22.00 ATOM 2684 C VAL A 347 23.417 23.380 35.178 1.00 23.30 ATOM 2685 O VAL A 347 24.231 23.104 34.280 1.00 23.48 ATOM 2686 CB VAL A 347 22.648 21.386 36.603 1.00 22.26 ATOM 2687 CG1 VAL A 347 22.591 20.635 35.267 1.00 23.03 ATOM 2688 CG2 VAL A 347 22.960 20.375 37.731 1.00 18.05 ATOM 2689 N ILE A 348 22.339 24.167 35.192 1.00 22.71 ATOM 2690 CA ILE A 348 22.082 24.896 33.927 1.00 25.23 ATOM 2691 C ILE A 348 23.239 25.872 33.717 1.00 24.58 ATOM 2692 O ILE A 348 23.804 25.850 32.649 1.00 24.59 ATOM 2693 CB ILE A 348 20.675 25.483 34.050 1.00 25.22 ATOM 2694 CG1 ILE A 348 19.588 24.485 33.594 1.00 23.57 ATOM 2695 CG2 ILE A 348 20.586 26.820 33.292 1.00 27.98 ATOM 2696 CD1 ILE A 348 18.254 25.174 34.094 1.00 28.81 ATOM 2697 N ASN A 349 23.564 26.626 34.727 1.00 26.89 ATOM 2698 CA ASN A 349 24.688 27.604 34.621 1.00 25.49 ATOM 2699 C ASN A 349 25.976 26.878 34.270 1.00 24.40 ATOM 2700 O ASN A 349 26.799 27.445 33.541 1.00 24.15 ATOM 2701 CB ASN A 349 24.773 28.497 35.867 1.00 25.19 ATOM 2702 CG ASN A 349 23.702 29.503 36.138 1.00 25.07 ATOM 2703 OD1 ASN A 349 22.858 29.843 35.320 1.00 31.75 ATOM 2704 ND2 ASN A 349 23.717 30.062 37.377 1.00 27.28 ATOM 2705 N ALA A 350 26.266 25.694 34.801 1.00 22.84 ATOM 2706 CA ALA A 350 27.471 24.994 34.532 1.00 22.87 ATOM 2707 C ALA A 350 27.422 24.356 33.142 1.00 25.48 ATOM 2708 O ALA A 350 28.527 24.329 32.461 1.00 25.91 ATOM 2709 CB ALA A 350 27.832 23.864 35.536 1.00 19.82 ATOM 2710 N ALA A 351 26.272 23.835 32.764 1.00 25.14 ATOM 2711 CA ALA A 351 26.210 23.144 31.417 1.00 26.99 ATOM 2712 C ALA A 351 26.326 24.136 30.244 1.00 27.64 ATOM 2713 O ALA A 351 26.984 23.909 29.202 1.00 29.35 ATOM 2714 CB ALA A 351 24.920 22.328 31.361 1.00 27.22 ATOM 2715 N SER A 352 25.730 25.296 30.445 1.00 29.27 ATOM 2716 CA SER A 352 25.669 26.460 29.551 1.00 30.40 ATOM 2717 C SER A 352 27.006 27.206 29.527 1.00 31.95 ATOM 2718 O SER A 352 27.151 28.066 28.645 1.00 35.02 ATOM 2719 CB SER A 352 24.485 27.329 29.958 1.00 26.61 ATOM 2720 OG SER A 352 24.845 28.101 31.104 1.00 30.58 ATOM 2721 N GLY A 353 27.961 26.932 30.405 1.00 30.84 ATOM 2722 CA GLY A 353 29.266 27.459 30.548 1.00 29.04 ATOM 2723 C GLY A 353 29.268 28.848 31.129 1.00 31.84 ATOM 2724 O GLY A 353 30.413 29.380 31.015 1.00 33.36 ATOM 2725 N ARG A 354 28.153 29.274 31.755 1.00 30.68 ATOM 2726 CA ARG A 354 28.007 30.580 32.361 1.00 33.29 ATOM 2727 C ARG A 354 28.873 30.642 33.652 1.00 35.02 ATOM 2728 O ARG A 354 29.288 31.748 34.106 1.00 38.74 ATOM 2729 CB ARG A 354 26.651 31.135 32.730 1.00 31.66 ATOM 2730 CG ARG A 354 25.479 31.278 31.822 1.00 35.91 ATOM 2731 CD ARG A 354 24.595 32.491 32.152 1.00 36.12 ATOM 2732 NE ARG A 354 23.232 32.034 32.132 1.00 41.26 ATOM 2733 CZ ARG A 354 22.622 31.293 31.186 1.00 42.90 ATOM 2734 NH1 ARG A 354 22.834 30.810 29.969 1.00 40.51 ATOM 2735 NH2 ARG A 354 21.485 30.649 31.647 1.00 45.01 ATOM 2736 N GLN A 355 29.058 29.487 34.291 1.00 32.88 ATOM 2737 CA GLN A 355 29.822 29.377 35.518 1.00 28.32 ATOM 2738 C GLN A 355 30.580 28.048 35.350 1.00 26.91 ATOM 2739 O GLN A 355 30.151 27.187 34.610 1.00 25.60 ATOM 2740 CB GLN A 355 28.991 29.277 36.789 1.00 27.33 ATOM 2741 CG GLN A 355 28.299 30.515 37.289 1.00 27.67 ATOM 2742 CD GLN A 355 27.496 30.260 38.538 1.00 30.61 ATOM 2743 OE1 GLN A 355 26.484 29.544 38.554 1.00 31.20 ATOM 2744 NE2 GLN A 355 27.887 30.907 39.650 1.00 28.51 ATOM 2745 N THR A 356 31.662 28.005 36.075 1.00 26.36 ATOM 2746 CA THR A 356 32.500 26.809 36.200 1.00 26.12 ATOM 2747 C THR A 356 31.708 25.926 37.222 1.00 24.97 ATOM 2748 O THR A 356 30.895 26.455 37.991 1.00 24.65 ATOM 2749 CB THR A 356 33.957 26.965 36.739 1.00 26.48 ATOM 2750 OG1 THR A 356 33.944 27.558 38.085 1.00 25.11 ATOM 2751 CG2 THR A 356 34.885 27.801 35.806 1.00 29.29 ATOM 2752 N VAL A 357 32.062 24.653 37.202 1.00 25.60 ATOM 2753 CA VAL A 357 31.501 23.707 38.180 1.00 24.62 ATOM 2754 C VAL A 357 31.734 24.166 39.593 1.00 24.29 ATOM 2755 O VAL A 357 30.714 24.229 40.344 1.00 26.92 ATOM 2756 CB VAL A 357 32.093 22.304 37.884 1.00 24.42 ATOM 2757 CG1 VAL A 357 31.678 21.268 38.931 1.00 22.52 ATOM 2758 CG2 VAL A 357 31.644 22.012 36.448 1.00 24.91 ATOM 2759 N ASP A 358 32.953 24.484 39.942 1.00 25.19 ATOM 2760 CA ASP A 358 33.344 24.926 41.334 1.00 27.18 ATOM 2761 C ASP A 358 32.514 26.130 41.776 1.00 26.89 ATOM 2762 O ASP A 358 31.905 26.093 42.883 1.00 25.43 ATOM 2763 CB ASP A 358 34.843 25.101 41.393 1.00 34.51 ATOM 2764 CG ASP A 358 35.802 23.967 41.224 1.00 39.72 ATOM 2765 OD1 ASP A 358 36.057 23.123 42.114 1.00 47.15 ATOM 2766 OD2 ASP A 358 36.537 23.785 40.200 1.00 49.39 ATOM 2767 N GLU A 359 32.434 27.152 40.953 1.00 25.66 ATOM 2768 CA GLU A 359 31.614 28.319 41.176 1.00 25.86 ATOM 2769 C GLU A 359 30.142 27.927 41.252 1.00 23.65 ATOM 2770 O GLU A 359 29.452 28.446 42.150 1.00 24.02 ATOM 2771 CB GLU A 359 31.637 29.360 40.044 1.00 32.11 ATOM 2772 CG GLU A 359 32.839 30.305 40.004 1.00 38.99 ATOM 2773 CD GLU A 359 33.205 30.920 38.658 1.00 42.40 ATOM 2774 OE1 GLU A 359 32.254 31.002 37.852 1.00 41.52 ATOM 2775 OE2 GLU A 359 34.387 31.244 38.381 1.00 45.30 ATOM 2776 N ALA A 360 29.610 27.138 40.378 1.00 20.82 ATOM 2777 CA ALA A 360 28.185 26.769 40.421 1.00 19.55 ATOM 2778 C ALA A 360 27.774 26.025 41.702 1.00 17.14 ATOM 2779 O ALA A 360 26.691 26.412 42.251 1.00 18.13 ATOM 2780 CB ALA A 360 27.877 25.907 39.169 1.00 18.90 ATOM 2781 N LEU A 361 28.602 25.101 42.105 1.00 18.86 ATOM 2782 CA LEU A 361 28.243 24.220 43.260 1.00 18.39 ATOM 2783 C LEU A 361 28.434 24.944 44.549 1.00 22.29 ATOM 2784 O LEU A 361 27.709 24.653 45.479 1.00 23.42 ATOM 2785 CB LEU A 361 28.953 22.871 43.227 1.00 18.88 ATOM 2786 CG LEU A 361 28.475 22.040 41.972 1.00 19.71 ATOM 2787 CD1 LEU A 361 29.335 20.843 41.840 1.00 17.72 ATOM 2788 CD2 LEU A 361 26.950 21.759 42.071 1.00 14.79 ATOM 2789 N LYS A 362 29.337 25.906 44.408 1.00 23.80 ATOM 2790 CA LYS A 362 29.568 26.661 45.693 1.00 23.44 ATOM 2791 C LYS A 362 28.428 27.564 45.901 1.00 22.81 ATOM 2792 O LYS A 362 27.987 27.787 47.084 1.00 25.51 ATOM 2793 CB LYS A 362 30.873 27.335 45.512 1.00 29.64 ATOM 2794 CG LYS A 362 31.402 27.999 46.763 1.00 37.21 ATOM 2795 CD LYS A 362 31.527 29.478 46.318 1.00 45.09 ATOM 2796 CE LYS A 362 30.144 30.127 46.682 1.00 50.12 ATOM 2797 NZ LYS A 362 30.261 31.646 46.496 1.00 55.02 ATOM 2798 N ASP A 363 27.921 28.164 44.894 1.00 22.46 ATOM 2799 CA ASP A 363 26.787 29.099 45.077 1.00 23.70 ATOM 2800 C ASP A 363 25.553 28.384 45.590 1.00 21.93 ATOM 2801 O ASP A 363 24.697 28.907 46.258 1.00 22.41 ATOM 2802 CB ASP A 363 26.390 29.666 43.703 1.00 30.99 ATOM 2803 CG ASP A 363 27.041 31.019 43.435 1.00 41.33 ATOM 2804 OD1 ASP A 363 28.007 31.449 44.182 1.00 44.85 ATOM 2805 OD2 ASP A 363 26.525 31.627 42.421 1.00 46.02 ATOM 2806 N ALA A 364 25.470 27.167 45.036 1.00 20.83 ATOM 2807 CA ALA A 364 24.307 26.334 45.367 1.00 20.13 ATOM 2808 C ALA A 364 24.311 26.015 46.839 1.00 19.47 ATOM 2809 O ALA A 364 23.307 26.000 47.581 1.00 19.07 ATOM 2810 CB ALA A 364 24.253 25.102 44.416 1.00 17.22 ATOM 2811 N GLN A 365 25.545 25.630 47.270 1.00 20.72 ATOM 2812 CA GLN A 365 25.793 25.252 48.697 1.00 23.13 ATOM 2813 C GLN A 365 25.404 26.367 49.621 1.00 23.99 ATOM 2814 O GLN A 365 24.720 26.209 50.643 1.00 25.68 ATOM 2815 CB GLN A 365 27.245 24.855 48.775 1.00 27.82 ATOM 2816 CG GLN A 365 27.764 24.633 50.172 1.00 33.30 ATOM 2817 CD GLN A 365 27.336 23.322 50.734 1.00 39.43 ATOM 2818 OE1 GLN A 365 26.887 22.383 50.047 1.00 42.04 ATOM 2819 NE2 GLN A 365 27.543 23.272 52.061 1.00 41.78 ATOM 2820 N THR A 366 25.836 27.614 49.306 1.00 25.64 ATOM 2821 CA THR A 366 25.506 28.835 50.016 1.00 24.71 ATOM 2822 C THR A 366 24.047 29.111 50.003 1.00 24.90 ATOM 2823 O THR A 366 23.480 29.386 51.063 1.00 28.95 ATOM 2824 CB THR A 366 26.193 30.108 49.303 1.00 26.56 ATOM 2825 OG1 THR A 366 27.536 29.683 49.314 1.00 29.29 ATOM 2826 CG2 THR A 366 25.759 31.337 50.087 1.00 28.25 ATOM 2827 N ARG A 367 23.435 29.037 48.826 1.00 24.37 ATOM 2828 CA ARG A 367 22.036 29.255 48.726 1.00 24.44 ATOM 2829 C ARG A 367 21.287 28.297 49.628 1.00 27.44 ATOM 2830 O ARG A 367 20.266 28.742 50.263 1.00 29.58 ATOM 2831 CB ARG A 367 21.594 29.026 47.278 1.00 28.34 ATOM 2832 CG ARG A 367 22.056 30.239 46.447 1.00 36.19 ATOM 2833 CD ARG A 367 21.230 30.366 45.229 1.00 43.32 ATOM 2834 NE ARG A 367 19.791 30.044 45.283 1.00 49.69 ATOM 2835 CZ ARG A 367 19.145 29.885 44.063 1.00 56.63 ATOM 2836 NH1 ARG A 367 19.863 29.735 42.909 1.00 54.14 ATOM 2837 NH2 ARG A 367 17.777 29.752 43.897 1.00 60.31 ATOM 2838 N ILE A 368 21.608 27.014 49.638 1.00 24.54 ATOM 2839 CA ILE A 368 20.863 26.051 50.451 1.00 26.05 ATOM 2840 C ILE A 368 21.022 26.211 51.945 1.00 25.93 ATOM 2841 O ILE A 368 20.040 26.039 52.673 1.00 24.75 ATOM 2842 CB ILE A 368 21.163 24.512 50.072 1.00 25.20 ATOM 2843 CG1 ILE A 368 20.838 24.255 48.583 1.00 21.49 ATOM 2844 CG2 ILE A 368 20.339 23.585 51.067 1.00 23.97 ATOM 2845 CD1 ILE A 368 21.697 23.122 47.907 1.00 22.00 ATOM 2846 N THR A 369 22.235 26.464 52.387 1.00 29.61 ATOM 2847 CA THR A 369 22.448 26.552 53.846 1.00 32.75 ATOM 2848 C THR A 369 22.232 27.917 54.471 1.00 36.83 ATOM 2849 O THR A 369 22.330 27.894 55.744 1.00 37.14 ATOM 2850 CB THR A 369 23.892 26.042 54.237 1.00 30.83 ATOM 2851 OG1 THR A 369 24.789 27.010 53.631 1.00 27.79 ATOM 2852 CG2 THR A 369 24.040 24.561 53.813 1.00 31.27 ATOM 2853 N LYS A 370 21.926 28.945 53.779 1.00 39.60 ATOM 2854 CA LYS A 370 21.731 30.315 54.234 1.00 44.78 ATOM 2855 C LYS A 370 20.879 30.604 55.430 1.00 47.81 ATOM 2856 CB LYS A 370 21.177 31.156 53.033 1.00 49.22 ATOM 2857 CG LYS A 370 22.370 31.851 52.305 1.00 54.39 ATOM 2858 CD LYS A 370 21.942 33.223 51.814 1.00 59.84 ATOM 2859 CE LYS A 370 22.219 34.389 52.766 1.00 64.71 ATOM 2860 NZ LYS A 370 21.328 35.617 52.564 1.00 67.45 END A second structure was input as follows:ATOM 1 N LYS A 1 -20.828 26.293 49.639 1.00 56.81 ATOM 2 CA LYS A 1 -19.852 25.381 49.023 1.00 57.02 ATOM 3 C LYS A 1 -18.680 24.991 49.921 1.00 56.60 ATOM 4 O LYS A 1 -17.690 25.740 50.118 1.00 57.52 ATOM 5 CB LYS A 1 -19.373 26.032 47.713 1.00 57.07 ATOM 6 N ILE A 2 -18.752 23.782 50.476 1.00 54.94 ATOM 7 CA ILE A 2 -17.735 23.195 51.347 1.00 52.17 ATOM 8 C ILE A 2 -18.054 21.729 51.663 1.00 50.14 ATOM 9 O ILE A 2 -18.175 21.296 52.806 1.00 48.68 ATOM 10 CB ILE A 2 -17.417 24.030 52.569 1.00 52.43 ATOM 11 N GLU A 3 -18.211 20.994 50.579 1.00 48.65 ATOM 12 CA GLU A 3 -18.423 19.552 50.497 1.00 47.01 ATOM 13 C GLU A 3 -19.657 19.032 51.204 1.00 44.31 ATOM 14 O GLU A 3 -20.749 19.529 50.926 1.00 44.45 ATOM 15 CB GLU A 3 -17.133 18.920 51.117 1.00 48.31 ATOM 16 N GLU A 4 -19.459 18.030 52.024 1.00 40.81 ATOM 17 CA GLU A 4 -20.408 17.397 52.905 1.00 38.78 ATOM 18 C GLU A 4 -21.314 16.326 52.351 1.00 37.13 ATOM 19 O GLU A 4 -22.318 16.661 51.704 1.00 37.52 ATOM 20 CB GLU A 4 -21.238 18.505 53.562 1.00 39.35 ATOM 21 N GLY A 5 -21.002 15.071 52.625 1.00 35.06 ATOM 22 CA GLY A 5 -21.777 13.915 52.156 1.00 33.11 ATOM 23 C GLY A 5 -21.456 13.379 50.767 1.00 30.69 ATOM 24 O GLY A 5 -22.195 12.549 50.200 1.00 30.13 ATOM 25 N LYS A 6 -20.365 13.858 50.198 1.00 28.47 ATOM 26 CA LYS A 6 -19.895 13.409 48.896 1.00 26.55 ATOM 27 C LYS A 6 -18.387 13.551 48.861 1.00 25.71 ATOM 28 O LYS A 6 -17.762 13.880 49.878 1.00 25.21 ATOM 29 CB LYS A 6 -20.579 14.092 47.766 1.00 26.80 ATOM 30 CG LYS A 6 -20.330 15.573 47.618 1.00 27.86 ATOM 31 CD LYS A 6 -20.887 16.072 46.297 1.00 31.02 ATOM 32 CE LYS A 6 -20.660 15.174 45.097 1.00 32.98 ATOM 33 NZ LYS A 6 -19.284 14.609 45.022 1.00 32.95 ATOM 34 N LEU A 7 -17.806 13.217 47.727 1.00 24.11 ATOM 35 CA LEU A 7 -16.334 13.347 47.586 1.00 22.29 ATOM 36 C LEU A 7 -16.053 14.090 46.291 1.00 21.35 ATOM 37 O LEU A 7 -16.673 13.907 45.261 1.00 21.91 ATOM 38 CB LEU A 7 -15.688 11.989 47.731 1.00 20.78 ATOM 39 CG LEU A 7 -15.416 11.328 49.048 1.00 18.45 ATOM 40 CD1 LEU A 7 -14.939 9.890 48.865 1.00 18.81 ATOM 41 CD2 LEU A 7 -14.348 12.052 49.845 1.00 17.75 ATOM 42 N VAL A 8 -15.150 15.043 46.373 1.00 21.25 ATOM 43 CA VAL A 8 -14.683 15.767 45.191 1.00 20.48 ATOM 44 C VAL A 8 -13.160 15.546 45.204 1.00 19.02 ATOM 45 O VAL A 8 -12.477 15.601 46.215 1.00 18.19 ATOM 46 CB VAL A 8 -15.272 17.065 44.796 1.00 22.06 ATOM 47 CG1 VAL A 8 -16.046 17.859 45.824 1.00 24.15 ATOM 48 CG2 VAL A 8 -14.262 17.968 44.082 1.00 21.85 ATOM 49 N ILE A 9 -12.719 15.124 44.029 1.00 18.66 ATOM 50 CA ILE A 9 -11.298 14.822 43.799 1.00 17.11 ATOM 51 C ILE A 9 -10.766 15.646 42.630 1.00 16.86 ATOM 52 O ILE A 9 -11.488 15.868 41.658 1.00 16.70 ATOM 53 CB ILE A 9 -11.133 13.301 43.479 1.00 17.88 ATOM 54 CG1 ILE A 9 -11.821 12.466 44.582 1.00 18.31 ATOM 55 CG2 ILE A 9 -9.643 12.948 43.286 1.00 17.04 ATOM 56 CD1 ILE A 9 -11.799 10.947 44.253 1.00 19.61 ATOM 57 N TRP A 10 -9.535 16.053 42.803 1.00 17.03 ATOM 58 CA TRP A 10 -8.753 16.827 41.841 1.00 17.32 ATOM 59 C TRP A 10 -7.511 16.030 41.451 1.00 16.61 ATOM 60 O TRP A 10 -6.733 15.575 42.292 1.00 17.95 ATOM 61 CB TRP A 10 -8.356 18.155 42.450 1.00 18.38 ATOM 62 CG TRP A 10 -9.430 19.185 42.393 1.00 19.67 ATOM 63 CD1 TRP A 10 -10.752 19.031 42.131 1.00 19.53 ATOM 64 CD2 TRP A 10 -9.217 20.582 42.668 1.00 19.64 ATOM 65 NE1 TRP A 10 -11.389 20.233 42.183 1.00 21.28 ATOM 66 CE2 TRP A 10 -10.465 21.209 42.509 1.00 21.17 ATOM 67 CE3 TRP A 10 -8.095 21.332 43.015 1.00 19.18 ATOM 68 CZ2 TRP A 10 -10.620 22.575 42.710 1.00 20.58 ATOM 69 CZ3 TRP A 10 -8.248 22.681 43.225 1.00 20.22 ATOM 70 CH2 TRP A 10 -9.489 23.294 43.068 1.00 20.58 ATOM 71 N ILE A 11 -7.359 15.873 40.157 1.00 16.81 ATOM 72 CA ILE A 11 -6.234 15.138 39.568 1.00 15.52 ATOM 73 C ILE A 11 -5.911 15.837 38.260 1.00 16.75 ATOM 74 O ILE A 11 -6.815 16.415 37.656 1.00 17.99 ATOM 75 CB ILE A 11 -6.648 13.622 39.392 1.00 14.80 ATOM 76 CG1 ILE A 11 -5.429 12.776 39.002 1.00 14.29 ATOM 77 CG2 ILE A 11 -7.837 13.411 38.428 1.00 12.82 ATOM 78 CD1 ILE A 11 -5.541 11.244 39.280 1.00 13.21 ATOM 79 N ASN A 12 -4.686 15.809 37.839 1.00 18.72 ATOM 80 CA ASN A 12 -4.270 16.436 36.565 1.00 19.92 ATOM 81 C ASN A 12 -4.921 15.710 35.373 1.00 20.42 ATOM 82 O ASN A 12 -5.111 14.497 35.384 1.00 18.72 ATOM 83 CB ASN A 12 -2.744 16.450 36.481 1.00 20.56 ATOM 84 CG ASN A 12 -2.214 17.610 35.663 1.00 22.28 ATOM 85 OD1 ASN A 12 -2.920 18.586 35.361 1.00 24.84 ATOM 86 ND2 ASN A 12 -0.951 17.533 35.304 1.00 24.20 ATOM 87 N GLY A 13 -5.199 16.494 34.348 1.00 21.73 ATOM 88 CA GLY A 13 -5.779 16.081 33.091 1.00 23.78 ATOM 89 C GLY A 13 -5.010 15.031 32.302 1.00 24.20 ATOM 90 O GLY A 13 -5.632 14.294 31.500 1.00 25.75 ATOM 91 N ASP A 14 -3.755 14.875 32.539 1.00 24.92 ATOM 92 CA ASP A 14 -2.818 13.944 31.909 1.00 26.74 ATOM 93 C ASP A 14 -2.758 12.573 32.590 1.00 27.18 ATOM 94 O ASP A 14 -1.863 11.738 32.310 1.00 27.74 ATOM 95 CB ASP A 14 -1.446 14.613 31.796 1.00 28.05 ATOM 96 CG ASP A 14 -0.634 14.719 33.056 1.00 30.88 ATOM 97 OD1 ASP A 14 -1.187 14.560 34.167 1.00 32.40 ATOM 98 OD2 ASP A 14 0.594 14.960 33.028 1.00 32.97 ATOM 99 N LYS A 15 -3.670 12.341 33.507 1.00 26.37 ATOM 100 CA LYS A 15 -3.807 11.131 34.306 1.00 25.09 ATOM 101 C LYS A 15 -5.122 10.432 33.976 1.00 23.32 ATOM 102 O LYS A 15 -5.998 11.006 33.356 1.00 22.97 ATOM 103 CB LYS A 15 -3.856 11.438 35.816 1.00 26.22 ATOM 104 CG LYS A 15 -2.789 12.405 36.300 1.00 25.46 ATOM 105 CD LYS A 15 -1.530 11.715 36.700 1.00 25.02 ATOM 106 CE LYS A 15 -0.368 12.130 35.831 1.00 27.99 ATOM 107 NZ LYS A 15 0.795 11.287 36.211 1.00 31.92 ATOM 108 N GLY A 16 -5.225 9.223 34.473 1.00 22.74 ATOM 109 CA GLY A 16 -6.395 8.401 34.221 1.00 22.42 ATOM 110 C GLY A 16 -7.558 8.774 35.115 1.00 22.81 ATOM 111 O GLY A 16 -7.972 7.941 35.934 1.00 22.76 ATOM 112 N TYR A 17 -8.062 9.973 34.909 1.00 22.81 ATOM 113 CA TYR A 17 -9.218 10.437 35.699 1.00 23.16 ATOM 114 C TYR A 17 -10.526 9.784 35.318 1.00 23.48 ATOM 115 O TYR A 17 -11.551 9.925 36.020 1.00 23.84 ATOM 116 CB TYR A 17 -9.249 11.955 35.617 1.00 23.34 ATOM 117 CG TYR A 17 -9.383 12.493 34.219 1.00 23.32 ATOM 118 CD1 TYR A 17 -10.645 12.570 33.669 1.00 23.63 ATOM 119 CD2 TYR A 17 -8.302 12.937 33.469 1.00 23.65 ATOM 120 CE1 TYR A 17 -10.837 13.061 32.389 1.00 25.13 ATOM 121 CE2 TYR A 17 -8.469 13.467 32.198 1.00 24.05 ATOM 122 CZ TYR A 17 -9.744 13.507 31.660 1.00 25.35 ATOM 123 OH TYR A 17 -10.034 14.005 30.415 1.00 27.46 ATOM 124 N ASN A 18 -10.572 9.076 34.198 1.00 23.47 ATOM 125 CA ASN A 18 -11.778 8.368 33.736 1.00 22.16 ATOM 126 C ASN A 18 -11.788 7.033 34.487 1.00 21.54 ATOM 127 O ASN A 18 -12.854 6.519 34.835 1.00 22.57 ATOM 128 CB ASN A 18 -11.861 8.214 32.235 1.00 23.69 ATOM 129 CG ASN A 18 -12.191 9.495 31.520 1.00 25.61 ATOM 130 OD1 ASN A 18 -11.489 9.952 30.608 1.00 27.94 ATOM 131 ND2 ASN A 18 -13.278 10.110 31.987 1.00 28.44 ATOM 132 N GLY A 19 -10.613 6.516 34.684 1.00 20.85 ATOM 133 CA GLY A 19 -10.453 5.235 35.425 1.00 20.66 ATOM 134 C GLY A 19 -10.734 5.518 36.900 1.00 21.38 ATOM 135 O GLY A 19 -11.322 4.687 37.602 1.00 22.22 ATOM 136 N LEU A 20 -10.251 6.671 37.359 1.00 21.27 ATOM 137 CA LEU A 20 -10.496 7.060 38.758 1.00 21.30 ATOM 138 C LEU A 20 -12.002 7.294 38.954 1.00 21.47 ATOM 139 O LEU A 20 -12.505 6.891 40.025 1.00 22.74 ATOM 140 CB LEU A 20 -9.577 8.200 39.172 1.00 19.91 ATOM 141 CG LEU A 20 -9.672 8.570 40.664 1.00 18.70 ATOM 142 CD1 LEU A 20 -9.209 7.421 41.526 1.00 17.68 ATOM 143 CD2 LEU A 20 -8.887 9.845 40.872 1.00 18.90 ATOM 144 N ALA A 21 -12.694 7.890 38.005 1.00 21.25 ATOM 145 CA ALA A 21 -14.127 8.107 38.036 1.00 22.73 ATOM 146 C ALA A 21 -14.871 6.765 38.073 1.00 24.89 ATOM 147 O ALA A 21 -16.011 6.770 38.559 1.00 26.80 ATOM 148 CB ALA A 21 -14.648 8.934 36.879 1.00 21.24 ATOM 149 N GLU A 22 -14.309 5.687 37.587 1.00 25.46 ATOM 150 CA GLU A 22 -14.841 4.344 37.573 1.00 26.32 ATOM 151 C GLU A 22 -14.711 3.628 38.912 1.00 25.87 ATOM 152 O GLU A 22 -15.506 2.722 39.257 1.00 25.29 ATOM 153 CB GLU A 22 -14.129 3.438 36.544 1.00 29.83 ATOM 154 CG GLU A 22 -14.557 3.657 35.083 1.00 34.89 ATOM 155 CD GLU A 22 -16.006 3.335 34.822 1.00 37.82 ATOM 156 OE1 GLU A 22 -16.137 2.090 34.752 1.00 40.28 ATOM 157 OE2 GLU A 22 -16.909 4.151 34.726 1.00 39.64 ATOM 158 N VAL A 23 -13.679 3.992 39.669 1.00 23.94 ATOM 159 CA VAL A 23 -13.476 3.425 41.011 1.00 22.02 ATOM 160 C VAL A 23 -14.555 4.076 41.902 1.00 22.46 ATOM 161 O VAL A 23 -15.083 3.465 42.827 1.00 22.30 ATOM 162 CB VAL A 23 -12.072 3.649 41.536 1.00 20.89 ATOM 163 CG1 VAL A 23 -11.904 3.169 42.960 1.00 19.19 ATOM 164 CG2 VAL A 23 -11.060 2.920 40.634 1.00 21.79 ATOM 165 N GLY A 24 -14.837 5.298 41.546 1.00 22.72 ATOM 166 CA GLY A 24 -15.812 6.147 42.192 1.00 24.83 ATOM 167 C GLY A 24 -17.248 5.676 42.044 1.00 26.20 ATOM 168 O GLY A 24 -18.054 5.881 42.954 1.00 25.15 ATOM 169 N LYS A 25 -17.570 5.092 40.898 1.00 27.54 ATOM 170 CA LYS A 25 -18.908 4.576 40.607 1.00 29.31 ATOM 171 C LYS A 25 -19.128 3.336 41.454 1.00 28.97 ATOM 172 O LYS A 25 -20.202 3.103 42.037 1.00 29.82 ATOM 173 CB LYS A 25 -19.165 4.405 39.122 1.00 32.02 ATOM 174 CG LYS A 25 -20.590 3.858 38.826 1.00 36.78 ATOM 175 CD LYS A 25 -21.676 4.852 39.244 1.00 38.24 ATOM 176 CE LYS A 25 -22.921 4.241 39.838 1.00 37.20 ATOM 177 NZ LYS A 25 -22.589 3.291 40.927 1.00 36.59 ATOM 178 N LYS A 26 -18.102 2.546 41.585 1.00 28.68 ATOM 179 CA LYS A 26 -18.063 1.347 42.421 1.00 29.88 ATOM 180 C LYS A 26 -18.250 1.749 43.885 1.00 31.25 ATOM 181 O LYS A 26 -18.954 1.060 44.665 1.00 32.91 ATOM 182 CB LYS A 26 -16.779 0.608 42.215 1.00 30.20 ATOM 183 CG LYS A 26 -16.259 -0.361 43.235 1.00 33.13 ATOM 184 CD LYS A 26 -17.180 -1.490 43.613 1.00 36.34 ATOM 185 CE LYS A 26 -16.490 -2.797 43.926 1.00 37.97 ATOM 186 NZ LYS A 26 -16.346 -3.061 45.386 1.00 39.59 ATOM 187 N PHE A 27 -17.623 2.856 44.299 1.00 30.47 ATOM 188 CA PHE A 27 -17.741 3.331 45.688 1.00 28.50 ATOM 189 C PHE A 27 -19.190 3.777 45.917 1.00 28.75 ATOM 190 O PHE A 27 -19.764 3.425 46.959 1.00 28.79 ATOM 191 CB PHE A 27 -16.742 4.401 46.057 1.00 25.98 ATOM 192 CG PHE A 27 -16.717 4.947 47.457 1.00 22.90 ATOM 193 CD1 PHE A 27 -16.102 4.239 48.482 1.00 20.15 ATOM 194 CD2 PHE A 27 -17.277 6.208 47.724 1.00 21.50 ATOM 195 CE1 PHE A 27 -16.041 4.727 49.782 1.00 18.40 ATOM 196 CE2 PHE A 27 -17.218 6.726 49.011 1.00 20.03 ATOM 197 CZ PHE A 27 -16.615 5.982 50.022 1.00 18.01 ATOM 198 N GLU A 28 -19.732 4.511 44.998 1.00 29.58 ATOM 199 CA GLU A 28 -21.089 5.040 45.061 1.00 32.41 ATOM 200 C GLU A 28 -22.133 3.929 45.098 1.00 34.42 ATOM 201 O GLU A 28 -23.273 4.157 45.505 1.00 34.56 ATOM 202 CB GLU A 28 -21.404 5.988 43.943 1.00 31.57 ATOM 203 CG GLU A 28 -22.790 6.330 43.508 1.00 33.54 ATOM 204 CD GLU A 28 -22.928 7.498 42.583 1.00 36.49 ATOM 205 OE1 GLU A 28 -21.942 7.683 41.841 1.00 37.19 ATOM 206 OE2 GLU A 28 -23.885 8.262 42.523 1.00 39.08 ATOM 207 N LYS A 29 -21.724 2.749 44.684 1.00 36.98 ATOM 208 CA LYS A 29 -22.565 1.551 44.629 1.00 38.62 ATOM 209 C LYS A 29 -22.764 0.936 46.002 1.00 38.12 ATOM 210 O LYS A 29 -23.921 0.624 46.371 1.00 38.99 ATOM 211 CB LYS A 29 -21.967 0.480 43.704 1.00 41.39 ATOM 212 CG LYS A 29 -22.892 0.070 42.556 1.00 44.19 ATOM 213 CD LYS A 29 -22.088 -0.143 41.273 1.00 47.51 ATOM 214 CE LYS A 29 -22.862 0.228 40.022 1.00 49.62 ATOM 215 NZ LYS A 29 -23.657 -0.920 39.483 1.00 50.86 ATOM 216 N ASP A 30 -21.680 0.753 46.736 1.00 36.99 ATOM 217 CA ASP A 30 -21.797 0.147 48.068 1.00 37.15 ATOM 218 C ASP A 30 -21.922 1.204 49.170 1.00 37.07 ATOM 219 O ASP A 30 -21.824 0.802 50.350 1.00 38.75 ATOM 220 CB ASP A 30 -20.633 -0.784 48.386 1.00 37.18 ATOM 221 CG ASP A 30 -19.768 -1.187 47.229 1.00 36.17 ATOM 222 OD1 ASP A 30 -20.247 -1.234 46.098 1.00 37.27 ATOM 223 OD2 ASP A 30 -18.585 -1.470 47.518 1.00 35.82 ATOM 224 N THR A 31 -22.123 2.453 48.808 1.00 36.02 ATOM 225 CA THR A 31 -22.175 3.520 49.826 1.00 34.45 ATOM 226 C THR A 31 -23.267 4.520 49.595 1.00 33.84 ATOM 227 O THR A 31 -23.893 5.018 50.569 1.00 35.75 ATOM 228 CB THR A 31 -20.716 4.195 49.885 1.00 33.09 ATOM 229 OG1 THR A 31 -19.869 3.205 50.554 1.00 31.71 ATOM 230 CG2 THR A 31 -20.652 5.532 50.550 1.00 31.90 ATOM 231 N GLY A 32 -23.516 4.858 48.362 1.00 32.51 ATOM 232 CA GLY A 32 -24.519 5.843 47.968 1.00 32.46 ATOM 233 C GLY A 32 -23.910 7.231 47.868 1.00 32.55 ATOM 234 O GLY A 32 -24.554 8.204 47.463 1.00 32.42 ATOM 235 N ILE A 33 -22.636 7.278 48.278 1.00 33.39 ATOM 236 CA ILE A 33 -21.873 8.532 48.246 1.00 32.26 ATOM 237 C ILE A 33 -21.319 8.702 46.817 1.00 31.42 ATOM 238 O ILE A 33 -20.616 7.805 46.344 1.00 30.22 ATOM 239 CB ILE A 33 -20.744 8.546 49.324 1.00 32.63 ATOM 240 CG1 ILE A 33 -21.363 8.520 50.746 1.00 32.86 ATOM 241 CG2 ILE A 33 -19.780 9.747 49.147 1.00 32.23 ATOM 242 CD1 ILE A 33 -22.356 9.655 51.070 1.00 33.46 ATOM 243 N LYS A 34 -21.684 9.823 46.251 1.00 30.65 ATOM 244 CA LYS A 34 -21.245 10.208 44.920 1.00 32.14 ATOM 245 C LYS A 34 -19.831 10.788 45.000 1.00 31.72 ATOM 246 O LYS A 34 -19.556 11.621 45.893 1.00 32.45 ATOM 247 CB LYS A 34 -22.143 11.293 44.329 1.00 34.72 ATOM 248 CG LYS A 34 -22.706 12.233 45.400 1.00 39.86 ATOM 249 CD LYS A 34 -23.720 13.190 44.780 1.00 44.39 ATOM 250 CE LYS A 34 -24.892 13.491 45.712 1.00 47.08 ATOM 251 NZ LYS A 34 -26.166 13.613 44.910 1.00 49.25 ATOM 252 N VAL A 35 -18.985 10.362 44.091 1.00 30.33 ATOM 253 CA VAL A 35 -17.586 10.841 43.977 1.00 28.49 ATOM 254 C VAL A 35 -17.570 11.728 42.734 1.00 28.33 ATOM 255 O VAL A 35 -18.322 11.419 41.807 1.00 30.32 ATOM 256 CB VAL A 35 -16.587 9.686 43.975 1.00 27.11 ATOM 257 CG1 VAL A 35 -15.142 10.120 43.798 1.00 25.37 ATOM 258 CG2 VAL A 35 -16.711 8.818 45.219 1.00 25.98 ATOM 259 N THR A 36 -16.866 12.814 42.726 1.00 28.12 ATOM 260 CA THR A 36 -16.748 13.747 41.624 1.00 27.76 ATOM 261 C THR A 36 -15.282 13.962 41.287 1.00 26.79 ATOM 262 O THR A 36 -14.520 14.449 42.148 1.00 27.30 ATOM 263 CB THR A 36 -17.393 15.156 41.948 1.00 28.80 ATOM 264 OG1 THR A 36 -18.703 14.843 42.526 1.00 31.82 ATOM 265 CG2 THR A 36 -17.494 16.079 40.742 1.00 29.32 ATOM 266 N VAL A 37 -14.928 13.603 40.071 1.00 25.57 ATOM 267 CA VAL A 37 -13.526 13.777 39.642 1.00 24.48 ATOM 268 C VAL A 37 -13.495 14.962 38.683 1.00 24.44 ATOM 269 O VAL A 37 -14.325 15.104 37.796 1.00 24.50 ATOM 270 CB VAL A 37 -12.886 12.514 39.064 1.00 23.84 ATOM 271 CG1 VAL A 37 -11.431 12.802 38.672 1.00 23.67 ATOM 272 CG2 VAL A 37 -12.927 11.287 39.953 1.00 22.67 ATOM 273 N GLU A 38 -12.523 15.806 38.917 1.00 25.96 ATOM 274 CA GLU A 38 -12.285 16.997 38.090 1.00 26.85 ATOM 275 C GLU A 38 -10.777 17.138 37.900 1.00 26.29 ATOM 276 O GLU A 38 -10.014 16.576 38.683 1.00 25.12 ATOM 277 CB GLU A 38 -12.870 18.251 38.673 1.00 29.22 ATOM 278 CG GLU A 38 -13.577 18.133 40.010 1.00 34.00 ATOM 279 CD GLU A 38 -14.622 19.142 40.347 1.00 37.52 ATOM 280 OE1 GLU A 38 -15.381 19.439 39.393 1.00 39.95 ATOM 281 OE2 GLU A 38 -14.728 19.613 41.470 1.00 39.62 ATOM 282 N HIS A 39 -10.443 17.851 36.852 1.00 26.46 ATOM 283 CA HIS A 39 -9.026 18.082 36.504 1.00 28.40 ATOM 284 C HIS A 39 -8.842 19.524 36.051 1.00 29.85 ATOM 285 O HIS A 39 -8.591 19.776 34.855 1.00 30.75 ATOM 286 CB HIS A 39 -8.553 17.073 35.433 1.00 27.69 ATOM 287 CG HIS A 39 -9.537 16.926 34.307 1.00 27.20 ATOM 288 ND1 HIS A 39 -9.383 17.492 33.078 1.00 27.08 ATOM 289 CD2 HIS A 39 -10.724 16.284 34.277 1.00 26.65 ATOM 290 CE1 HIS A 39 -10.423 17.202 32.321 1.00 26.84 ATOM 291 NE2 HIS A 39 -11.249 16.486 33.049 1.00 27.56 ATOM 292 N PRO A 40 -8.968 20.454 36.991 1.00 30.72 ATOM 293 CA PRO A 40 -8.844 21.886 36.703 1.00 31.77 ATOM 294 C PRO A 40 -7.429 22.248 36.308 1.00 33.01 ATOM 295 O PRO A 40 -6.458 21.583 36.651 1.00 32.47 ATOM 296 CB PRO A 40 -9.352 22.568 37.971 1.00 31.40 ATOM 297 CG PRO A 40 -9.040 21.588 39.064 1.00 30.44 ATOM 298 CD PRO A 40 -9.235 20.233 38.419 1.00 30.66 ATOM 299 N ASP A 41 -7.353 23.350 35.588 1.00 35.82 ATOM 300 CA ASP A 41 -6.114 23.934 35.066 1.00 38.09 ATOM 301 C ASP A 41 -5.270 24.444 36.232 1.00 37.66 ATOM 302 O ASP A 41 -5.850 25.129 37.097 1.00 37.78 ATOM 303 CB ASP A 41 -6.467 25.095 34.094 1.00 41.23 ATOM 304 CG ASP A 41 -5.778 24.914 32.746 1.00 43.71 ATOM 305 OD1 ASP A 41 -4.556 25.175 32.631 1.00 44.20 ATOM 306 OD2 ASP A 41 -6.500 24.484 31.822 1.00 46.24 ATOM 307 N LYS A 42 -3.991 24.155 36.186 1.00 36.80 ATOM 308 CA LYS A 42 -3.033 24.579 37.226 1.00 35.88 ATOM 309 C LYS A 42 -3.646 24.329 38.609 1.00 34.26 ATOM 310 O LYS A 42 -3.611 25.244 39.436 1.00 34.24 ATOM 311 CB LYS A 42 -2.666 26.051 37.133 1.00 36.01 ATOM 312 CG LYS A 42 -2.163 26.617 35.828 1.00 37.86 ATOM 313 CD LYS A 42 -1.216 25.724 35.062 1.00 39.47 ATOM 314 CE LYS A 42 0.248 25.934 35.370 1.00 41.22 ATOM 315 NZ LYS A 42 0.854 26.876 34.379 1.00 41.72 ATOM 316 N LEU A 43 -4.187 23.140 38.804 1.00 31.86 ATOM 317 CA LEU A 43 -4.870 22.814 40.070 1.00 29.59 ATOM 318 C LEU A 43 -3.918 22.882 41.254 1.00 28.14 ATOM 319 O LEU A 43 -4.386 23.090 42.401 1.00 28.24 ATOM 320 CB LEU A 43 -5.641 21.485 39.903 1.00 27.54 ATOM 321 CG LEU A 43 -4.776 20.226 39.818 1.00 25.53 ATOM 322 CD1 LEU A 43 -4.334 19.710 41.168 1.00 23.34 ATOM 323 CD2 LEU A 43 -5.550 19.155 39.076 1.00 24.55 ATOM 324 N GLU A 44 -2.631 22.696 41.002 1.00 26.46 ATOM 325 CA GLU A 44 -1.634 22.713 42.091 1.00 25.30 ATOM 326 C GLU A 44 -1.369 24.153 42.543 1.00 24.95 ATOM 327 O GLU A 44 -0.802 24.397 43.607 1.00 23.99 ATOM 328 CB GLU A 44 -0.343 22.044 41.715 1.00 24.76 ATOM 329 CG GLU A 44 0.602 22.814 40.809 1.00 25.54 ATOM 330 CD GLU A 44 0.245 22.979 39.375 1.00 25.17 ATOM 331 OE1 GLU A 44 -0.945 22.801 39.057 1.00 26.33 ATOM 332 OE2 GLU A 44 1.091 23.227 38.541 1.00 26.29 ATOM 333 N GLU A 45 -1.803 25.090 41.729 1.00 25.25 ATOM 334 CA GLU A 45 -1.690 26.526 42.015 1.00 26.44 ATOM 335 C GLU A 45 -2.988 26.976 42.686 1.00 25.54 ATOM 336 O GLU A 45 -2.975 27.763 43.633 1.00 25.39 ATOM 337 CB GLU A 45 -1.505 27.372 40.767 1.00 28.86 ATOM 338 CG GLU A 45 -0.164 28.018 40.524 1.00 34.28 ATOM 339 CD GLU A 45 1.052 27.163 40.635 1.00 38.38 ATOM 340 OE1 GLU A 45 1.438 26.933 41.800 1.00 38.83 ATOM 341 OE2 GLU A 45 1.660 26.732 39.653 1.00 43.01 ATOM 342 N LYS A 46 -4.069 26.444 42.153 1.00 24.20 ATOM 343 CA LYS A 46 -5.394 26.726 42.640 1.00 24.74 ATOM 344 C LYS A 46 -5.643 26.120 44.010 1.00 24.31 ATOM 345 O LYS A 46 -6.395 26.755 44.770 1.00 25.04 ATOM 346 CB LYS A 46 -6.497 26.247 41.710 1.00 27.22 ATOM 347 CG LYS A 46 -6.695 27.172 40.501 1.00 32.06 ATOM 348 CD LYS A 46 -7.516 26.508 39.418 1.00 35.02 ATOM 349 CE LYS A 46 -7.802 27.423 38.234 1.00 37.03 ATOM 350 NZ LYS A 46 -6.609 28.215 37.852 1.00 38.04 ATOM 351 N PHE A 47 -5.107 24.958 44.296 1.00 22.73 ATOM 352 CA PHE A 47 -5.309 24.284 45.561 1.00 21.62 ATOM 353 C PHE A 47 -5.014 25.216 46.753 1.00 22.32 ATOM 354 O PHE A 47 -5.867 25.429 47.616 1.00 22.53 ATOM 355 CB PHE A 47 -4.591 22.941 45.742 1.00 19.25 ATOM 356 CG PHE A 47 -4.898 22.216 47.040 1.00 18.20 ATOM 357 CD1 PHE A 47 -6.149 21.628 47.267 1.00 16.60 ATOM 358 CD2 PHE A 47 -3.938 22.106 48.040 1.00 16.08 ATOM 359 CE1 PHE A 47 -6.409 20.956 48.461 1.00 16.25 ATOM 360 CE2 PHE A 47 -4.189 21.466 49.242 1.00 16.95 ATOM 361 CZ PHE A 47 -5.438 20.886 49.460 1.00 15.37 ATOM 362 N PRO A 48 -3.787 25.688 46.840 1.00 23.24 ATOM 363 CA PRO A 48 -3.378 26.533 47.968 1.00 23.85 ATOM 364 C PRO A 48 -4.295 27.702 48.201 1.00 24.74 ATOM 365 O PRO A 48 -4.565 28.058 49.381 1.00 25.29 ATOM 366 CB PRO A 48 -1.909 26.807 47.747 1.00 24.41 ATOM 367 CG PRO A 48 -1.491 26.063 46.516 1.00 24.54 ATOM 368 CD PRO A 48 -2.710 25.487 45.866 1.00 22.26 ATOM 369 N GLN A 49 -4.860 28.287 47.184 1.00 25.21 ATOM 370 CA GLN A 49 -5.764 29.408 47.225 1.00 26.43 ATOM 371 C GLN A 49 -7.123 29.047 47.827 1.00 25.73 ATOM 372 O GLN A 49 -7.567 29.766 48.741 1.00 26.93 ATOM 373 CB GLN A 49 -6.036 30.058 45.871 1.00 30.09 ATOM 374 CG GLN A 49 -5.069 31.136 45.495 1.00 37.69 ATOM 375 CD GLN A 49 -3.943 30.752 44.568 1.00 41.73 ATOM 376 OE1 GLN A 49 -2.833 30.414 45.022 1.00 43.63 ATOM 377 NE2 GLN A 49 -4.264 30.836 43.258 1.00 42.64 ATOM 378 N VAL A 50 -7.788 28.068 47.270 1.00 23.70 ATOM 379 CA VAL A 50 -9.100 27.653 47.742 1.00 21.98 ATOM 380 C VAL A 50 -9.033 26.952 49.074 1.00 21.22 ATOM 381 O VAL A 50 -10.011 27.115 49.837 1.00 21.47 ATOM 382 CB VAL A 50 -9.891 26.894 46.656 1.00 21.44 ATOM 383 CG1 VAL A 50 -10.072 27.710 45.384 1.00 22.19 ATOM 384 CG2 VAL A 50 -9.270 25.546 46.320 1.00 22.28 ATOM 385 N ALA A 51 -8.021 26.174 49.369 1.00 20.96 ATOM 386 CA ALA A 51 -7.899 25.442 50.618 1.00 21.83 ATOM 387 C ALA A 51 -7.666 26.427 51.785 1.00 23.44 ATOM 388 O ALA A 51 -8.181 26.148 52.879 1.00 24.21 ATOM 389 CB ALA A 51 -6.854 24.345 50.634 1.00 18.68 ATOM 390 N ALA A 52 -6.903 27.490 51.517 1.00 24.37 ATOM 391 CA ALA A 52 -6.619 28.517 52.521 1.00 25.44 ATOM 392 C ALA A 52 -7.919 29.162 53.027 1.00 26.20 ATOM 393 O ALA A 52 -7.979 29.722 54.133 1.00 26.69 ATOM 394 CB ALA A 52 -5.641 29.562 51.988 1.00 25.38 ATOM 395 N THR A 53 -8.991 29.077 52.252 1.00 27.22 ATOM 396 CA THR A 53 -10.284 29.619 52.610 1.00 27.91 ATOM 397 C THR A 53 -11.315 28.542 52.975 1.00 27.95 ATOM 398 O THR A 53 -12.517 28.843 52.993 1.00 28.42 ATOM 399 CB THR A 53 -10.858 30.654 51.579 1.00 28.01 ATOM 400 OG1 THR A 53 -11.602 29.934 50.556 1.00 29.68 ATOM 401 CG2 THR A 53 -9.809 31.599 50.983 1.00 27.99 ATOM 402 N GLY A 54 -10.852 27.345 53.253 1.00 27.95 ATOM 403 CA GLY A 54 -11.629 26.176 53.601 1.00 27.32 ATOM 404 C GLY A 54 -12.509 25.682 52.465 1.00 27.87 ATOM 405 O GLY A 54 -13.630 25.170 52.646 1.00 28.48 ATOM 406 N ASP A 55 -12.027 25.829 51.249 1.00 27.91 ATOM 407 CA ASP A 55 -12.707 25.376 50.038 1.00 28.08 ATOM 408 C ASP A 55 -11.785 24.333 49.363 1.00 26.74 ATOM 409 O ASP A 55 -10.792 23.891 49.954 1.00 25.62 ATOM 410 CB ASP A 55 -13.114 26.560 49.169 1.00 31.13 ATOM 411 CG ASP A 55 -14.492 27.092 49.522 1.00 35.48 ATOM 412 OD1 ASP A 55 -15.192 26.352 50.254 1.00 37.40 ATOM 413 OD2 ASP A 55 -14.932 28.199 49.140 1.00 37.79 ATOM 414 N GLY A 56 -12.165 23.984 48.152 1.00 25.46 ATOM 415 CA GLY A 56 -11.427 23.019 47.323 1.00 24.66 ATOM 416 C GLY A 56 -12.019 21.606 47.407 1.00 22.69 ATOM 417 O GLY A 56 -13.153 21.426 47.896 1.00 23.58 ATOM 418 N PRO A 57 -11.243 20.651 46.897 1.00 20.29 ATOM 419 CA PRO A 57 -11.647 19.246 46.864 1.00 16.41 ATOM 420 C PRO A 57 -11.305 18.587 48.173 1.00 14.29 ATOM 421 O PRO A 57 -10.447 19.101 48.907 1.00 13.73 ATOM 422 CB PRO A 57 -10.755 18.725 45.700 1.00 15.86 ATOM 423 CG PRO A 57 -9.446 19.412 45.953 1.00 15.73 ATOM 424 CD PRO A 57 -9.885 20.833 46.306 1.00 19.16 ATOM 425 N ASP A 58 -11.908 17.462 48.444 1.00 12.04 ATOM 426 CA ASP A 58 -11.675 16.634 49.604 1.00 13.38 ATOM 427 C ASP A 58 -10.299 15.990 49.513 1.00 13.03 ATOM 428 O ASP A 58 -9.544 15.801 50.476 1.00 13.17 ATOM 429 CB ASP A 58 -12.762 15.526 49.698 1.00 15.11 ATOM 430 CG ASP A 58 -14.122 16.115 49.993 1.00 16.59 ATOM 431 OD1 ASP A 58 -14.271 16.438 51.204 1.00 19.08 ATOM 432 OD2 ASP A 58 -14.917 16.266 49.065 1.00 17.09 ATOM 433 N ILE A 59 -10.032 15.648 48.230 1.00 14.82 ATOM 434 CA ILE A 59 -8.747 14.980 47.932 1.00 15.10 ATOM 435 C ILE A 59 -8.097 15.513 46.683 1.00 14.13 ATOM 436 O ILE A 59 -8.729 15.855 45.702 1.00 15.25 ATOM 437 CB ILE A 59 -8.853 13.439 48.106 1.00 17.81 ATOM 438 CG1 ILE A 59 -8.298 12.705 46.848 1.00 18.86 ATOM 439 CG2 ILE A 59 -10.167 12.843 48.614 1.00 16.16 ATOM 440 CD1 ILE A 59 -6.955 12.028 47.217 1.00 20.85 ATOM 441 N ILE A 60 -6.784 15.608 46.767 1.00 14.27 ATOM 442 CA ILE A 60 -5.936 16.138 45.693 1.00 13.49 ATOM 443 C ILE A 60 -4.836 15.148 45.352 1.00 12.23 ATOM 444 O ILE A 60 -4.202 14.599 46.241 1.00 12.11 ATOM 445 CB ILE A 60 -5.332 17.527 46.144 1.00 15.55 ATOM 446 CG1 ILE A 60 -4.368 18.101 45.050 1.00 14.36 ATOM 447 CG2 ILE A 60 -4.560 17.497 47.489 1.00 14.79 ATOM 448 CD1 ILE A 60 -5.182 19.082 44.165 1.00 18.68 ATOM 449 N PHE A 61 -4.570 15.008 44.054 1.00 12.01 ATOM 450 CA PHE A 61 -3.493 14.095 43.602 1.00 11.22 ATOM 451 C PHE A 61 -2.379 14.977 42.998 1.00 8.85 ATOM 452 O PHE A 61 -2.750 15.797 42.172 1.00 10.85 ATOM 453 CB PHE A 61 -4.025 13.175 42.477 1.00 10.53 ATOM 454 CG PHE A 61 -4.813 12.002 42.972 1.00 12.71 ATOM 455 CD1 PHE A 61 -6.168 12.138 43.262 1.00 13.92 ATOM 456 CD2 PHE A 61 -4.190 10.769 43.126 1.00 12.40 ATOM 457 CE1 PHE A 61 -6.896 11.027 43.719 1.00 14.76 ATOM 458 CE2 PHE A 61 -4.904 9.664 43.560 1.00 13.22 ATOM 459 CZ PHE A 61 -6.253 9.795 43.855 1.00 12.91 ATOM 460 N TRP A 62 -1.192 14.804 43.409 1.00 9.99 ATOM 461 CA TRP A 62 -0.020 15.543 42.840 1.00 10.38 ATOM 462 C TRP A 62 1.216 14.847 43.285 1.00 9.86 ATOM 463 O TRP A 62 1.252 14.035 44.227 1.00 10.43 ATOM 464 CB TRP A 62 -0.076 17.048 43.162 1.00 10.76 ATOM 465 CG TRP A 62 0.709 17.851 42.171 1.00 14.47 ATOM 466 CD1 TRP A 62 2.010 18.294 42.282 1.00 15.37 ATOM 467 CD2 TRP A 62 0.246 18.305 40.886 1.00 14.45 ATOM 468 NE1 TRP A 62 2.391 18.985 41.141 1.00 15.36 ATOM 469 CE2 TRP A 62 1.324 19.019 40.288 1.00 15.60 ATOM 470 CE3 TRP A 62 -0.954 18.183 40.204 1.00 15.53 ATOM 471 CZ2 TRP A 62 1.205 19.582 39.021 1.00 14.99 ATOM 472 CZ3 TRP A 62 -1.096 18.772 38.953 1.00 15.58 ATOM 473 CH2 TRP A 62 -0.017 19.443 38.368 1.00 15.84 ATOM 474 N ALA A 63 2.332 15.150 42.602 1.00 11.31 ATOM 475 CA ALA A 63 3.638 14.634 42.989 1.00 11.16 ATOM 476 C ALA A 63 3.855 15.090 44.456 1.00 11.79 ATOM 477 O ALA A 63 3.505 16.234 44.792 1.00 11.50 ATOM 478 CB ALA A 63 4.718 15.265 42.104 1.00 13.27 ATOM 479 N HIS A 64 4.494 14.278 45.240 1.00 12.29 ATOM 480 CA HIS A 64 4.761 14.479 46.644 1.00 12.96 ATOM 481 C HIS A 64 5.513 15.757 47.014 1.00 15.58 ATOM 482 O HIS A 64 5.320 16.288 48.130 1.00 15.35 ATOM 483 CB HIS A 64 5.521 13.303 47.303 1.00 11.65 ATOM 484 CG HIS A 64 6.951 13.241 46.894 1.00 13.29 ATOM 485 ND1 HIS A 64 8.028 13.569 47.686 1.00 15.69 ATOM 486 CD2 HIS A 64 7.491 12.896 45.693 1.00 13.42 ATOM 487 CE1 HIS A 64 9.166 13.445 46.978 1.00 13.78 ATOM 488 NE2 HIS A 64 8.837 13.029 45.758 1.00 14.23 ATOM 489 N ASP A 65 6.416 16.184 46.145 1.00 16.58 ATOM 490 CA ASP A 65 7.285 17.328 46.446 1.00 18.33 ATOM 491 C ASP A 65 6.502 18.589 46.759 1.00 18.94 ATOM 492 O ASP A 65 6.889 19.398 47.618 1.00 20.18 ATOM 493 CB ASP A 65 8.438 17.409 45.465 1.00 19.31 ATOM 494 CG ASP A 65 7.974 17.869 44.109 1.00 21.94 ATOM 495 OD1 ASP A 65 7.149 17.331 43.392 1.00 24.89 ATOM 496 OD2 ASP A 65 8.471 18.936 43.750 1.00 26.14 ATOM 497 N ARG A 66 5.395 18.812 46.138 1.00 18.97 ATOM 498 CA ARG A 66 4.529 19.939 46.300 1.00 20.66 ATOM 499 C ARG A 66 3.773 19.905 47.633 1.00 20.38 ATOM 500 O ARG A 66 3.367 20.996 48.033 1.00 21.15 ATOM 501 CB ARG A 66 3.484 19.991 45.187 1.00 23.21 ATOM 502 CG ARG A 66 2.990 21.336 44.764 1.00 29.13 ATOM 503 CD ARG A 66 4.116 22.215 44.328 1.00 33.64 ATOM 504 NE ARG A 66 3.743 23.228 43.394 1.00 38.88 ATOM 505 CZ ARG A 66 2.986 24.307 43.509 1.00 40.55 ATOM 506 NH1 ARG A 66 2.381 24.671 44.648 1.00 40.54 ATOM 507 NH2 ARG A 66 2.830 25.073 42.409 1.00 42.28 ATOM 508 N PHE A 67 3.607 18.746 48.216 1.00 19.97 ATOM 509 CA PHE A 67 2.863 18.480 49.438 1.00 18.34 ATOM 510 C PHE A 67 3.527 19.094 50.662 1.00 18.64 ATOM 511 O PHE A 67 2.824 19.406 51.625 1.00 17.31 ATOM 512 CB PHE A 67 2.479 17.016 49.664 1.00 16.59 ATOM 513 CG PHE A 67 1.311 16.511 48.881 1.00 17.36 ATOM 514 CD1 PHE A 67 0.836 17.174 47.762 1.00 18.42 ATOM 515 CD2 PHE A 67 0.661 15.339 49.259 1.00 18.42 ATOM 516 CE1 PHE A 67 -0.253 16.726 47.004 1.00 19.10 ATOM 517 CE2 PHE A 67 -0.416 14.859 48.529 1.00 17.63 ATOM 518 CZ PHE A 67 -0.874 15.539 47.418 1.00 17.63 ATOM 519 N GLY A 68 4.821 19.265 50.583 1.00 19.12 ATOM 520 CA GLY A 68 5.611 19.869 51.674 1.00 20.86 ATOM 521 C GLY A 68 5.143 21.306 51.977 1.00 20.99 ATOM 522 O GLY A 68 4.958 21.643 53.161 1.00 22.15 ATOM 523 N GLY A 69 4.983 22.107 50.973 1.00 20.48 ATOM 524 CA GLY A 69 4.534 23.484 51.018 1.00 20.74 ATOM 525 C GLY A 69 3.088 23.574 51.463 1.00 20.84 ATOM 526 O GLY A 69 2.696 24.462 52.204 1.00 21.01 ATOM 527 N TYR A 70 2.256 22.644 50.997 1.00 20.79 ATOM 528 CA TYR A 70 0.842 22.541 51.365 1.00 19.63 ATOM 529 C TYR A 70 0.691 22.217 52.876 1.00 19.33 ATOM 530 O TYR A 70 -0.145 22.827 53.568 1.00 19.61 ATOM 531 CB TYR A 70 0.137 21.445 50.557 1.00 19.13 ATOM 532 CG TYR A 70 -0.082 21.647 49.094 1.00 19.71 ATOM 533 CD1 TYR A 70 0.187 22.860 48.444 1.00 18.90 ATOM 534 CD2 TYR A 70 -0.568 20.575 48.322 1.00 18.93 ATOM 535 CE1 TYR A 70 -0.048 23.016 47.083 1.00 19.01 ATOM 536 CE2 TYR A 70 -0.799 20.727 46.954 1.00 18.43 ATOM 537 CZ TYR A 70 -0.541 21.939 46.335 1.00 18.95 ATOM 538 OH TYR A 70 -0.770 22.107 44.996 1.00 19.45 ATOM 539 N ALA A 71 1.417 21.259 53.374 1.00 17.60 ATOM 540 CA ALA A 71 1.487 20.775 54.717 1.00 19.31 ATOM 541 C ALA A 71 1.971 21.896 55.678 1.00 21.08 ATOM 542 O ALA A 71 1.506 22.006 56.817 1.00 20.66 ATOM 543 CB ALA A 71 2.388 19.559 54.872 1.00 17.00 ATOM 544 N GLN A 72 2.919 22.644 55.184 1.00 21.79 ATOM 545 CA GLN A 72 3.533 23.754 55.922 1.00 23.26 ATOM 546 C GLN A 72 2.397 24.714 56.296 1.00 22.22 ATOM 547 O GLN A 72 2.408 25.074 57.468 1.00 24.64 ATOM 548 CB GLN A 72 4.571 24.495 55.102 1.00 25.94 ATOM 549 CG GLN A 72 5.723 25.080 55.919 1.00 30.41 ATOM 550 CD GLN A 72 6.500 26.012 54.998 1.00 33.63 ATOM 551 OE1 GLN A 72 7.714 26.005 54.891 1.00 35.86 ATOM 552 NE2 GLN A 72 5.702 26.840 54.304 1.00 36.33 ATOM 553 N SER A 73 1.547 25.067 55.372 1.00 19.13 ATOM 554 CA SER A 73 0.426 25.944 55.583 1.00 17.59 ATOM 555 C SER A 73 -0.811 25.309 56.200 1.00 17.54 ATOM 556 O SER A 73 -1.862 25.981 56.170 1.00 17.41 ATOM 557 CB SER A 73 -0.026 26.623 54.298 1.00 17.11 ATOM 558 OG SER A 73 1.051 27.370 53.792 1.00 20.15 ATOM 559 N GLY A 74 -0.702 24.081 56.625 1.00 16.86 ATOM 560 CA GLY A 74 -1.689 23.259 57.269 1.00 16.76 ATOM 561 C GLY A 74 -2.887 22.913 56.408 1.00 16.50 ATOM 562 O GLY A 74 -4.000 22.774 56.921 1.00 16.03 ATOM 563 N LEU A 75 -2.638 22.730 55.121 1.00 14.95 ATOM 564 CA LEU A 75 -3.702 22.435 54.165 1.00 15.00 ATOM 565 C LEU A 75 -4.070 20.956 54.070 1.00 13.66 ATOM 566 O LEU A 75 -5.134 20.652 53.519 1.00 14.09 ATOM 567 CB LEU A 75 -3.264 23.027 52.823 1.00 15.18 ATOM 568 CG LEU A 75 -2.936 24.517 52.806 1.00 15.38 ATOM 569 CD1 LEU A 75 -2.530 24.889 51.376 1.00 16.20 ATOM 570 CD2 LEU A 75 -4.194 25.279 53.185 1.00 13.76 ATOM 571 N LEU A 76 -3.278 20.080 54.584 1.00 13.94 ATOM 572 CA LEU A 76 -3.476 18.654 54.550 1.00 15.37 ATOM 573 C LEU A 76 -3.726 18.002 55.910 1.00 16.40 ATOM 574 O LEU A 76 -2.992 18.260 56.886 1.00 17.73 ATOM 575 CB LEU A 76 -2.239 18.016 53.863 1.00 14.72 ATOM 576 CG LEU A 76 -1.937 18.418 52.437 1.00 14.46 ATOM 577 CD1 LEU A 76 -0.760 17.584 51.895 1.00 15.08 ATOM 578 CD2 LEU A 76 -3.128 18.194 51.529 1.00 14.61 ATOM 579 N ALA A 77 -4.685 17.076 55.890 1.00 14.92 ATOM 580 CA ALA A 77 -4.988 16.290 57.075 1.00 15.54 ATOM 581 C ALA A 77 -3.904 15.232 57.232 1.00 17.53 ATOM 582 O ALA A 77 -3.307 14.691 56.269 1.00 16.81 ATOM 583 CB ALA A 77 -6.363 15.678 56.977 1.00 15.24 ATOM 584 N GLU A 78 -3.639 14.978 58.502 1.00 18.63 ATOM 585 CA GLU A 78 -2.685 13.957 58.908 1.00 20.54 ATOM 586 C GLU A 78 -3.424 12.626 58.643 1.00 19.76 ATOM 587 O GLU A 78 -4.649 12.568 58.842 1.00 19.46 ATOM 588 CB GLU A 78 -2.296 13.952 60.367 1.00 22.78 ATOM 589 CG GLU A 78 -1.302 12.895 60.841 1.00 25.81 ATOM 590 CD GLU A 78 -0.913 12.906 62.282 1.00 26.33 ATOM 591 OE1 GLU A 78 -1.173 13.809 63.028 1.00 28.96 ATOM 592 OE2 GLU A 78 -0.320 11.896 62.689 1.00 28.58 ATOM 593 N ILE A 79 -2.685 11.672 58.141 1.00 20.01 ATOM 594 CA ILE A 79 -3.283 10.349 57.827 1.00 19.96 ATOM 595 C ILE A 79 -2.756 9.330 58.794 1.00 20.56 ATOM 596 O ILE A 79 -1.661 9.369 59.333 1.00 19.44 ATOM 597 CB ILE A 79 -3.175 9.952 56.308 1.00 19.32 ATOM 598 CG1 ILE A 79 -1.695 9.781 55.892 1.00 18.76 ATOM 599 CG2 ILE A 79 -3.914 10.932 55.364 1.00 17.46 ATOM 600 CD1 ILE A 79 -1.404 8.575 54.980 1.00 18.13 ATOM 601 N THR A 80 -3.615 8.320 59.002 1.00 24.30 ATOM 602 CA THR A 80 -3.208 7.252 59.917 1.00 28.10 ATOM 603 C THR A 80 -3.562 5.857 59.475 1.00 29.43 ATOM 604 O THR A 80 -4.400 5.202 60.125 1.00 30.84 ATOM 605 CB THR A 80 -3.819 7.576 61.359 1.00 29.96 ATOM 606 OG1 THR A 80 -5.193 8.006 61.034 1.00 32.20 ATOM 607 CG2 THR A 80 -2.924 8.560 62.110 1.00 28.97 ATOM 608 N PRO A 81 -2.903 5.409 58.417 1.00 29.73 ATOM 609 CA PRO A 81 -3.131 4.031 57.950 1.00 29.63 ATOM 610 C PRO A 81 -2.543 3.178 59.059 1.00 30.69 ATOM 611 O PRO A 81 -1.521 3.611 59.647 1.00 31.05 ATOM 612 CB PRO A 81 -2.274 3.931 56.690 1.00 29.65 ATOM 613 CG PRO A 81 -1.314 5.067 56.727 1.00 28.01 ATOM 614 CD PRO A 81 -1.886 6.121 57.634 1.00 28.77 ATOM 615 N ASP A 82 -3.085 2.018 59.314 1.00 32.66 ATOM 616 CA ASP A 82 -2.476 1.155 60.374 1.00 34.02 ATOM 617 C ASP A 82 -1.329 0.367 59.729 1.00 33.44 ATOM 618 O ASP A 82 -1.173 0.352 58.492 1.00 32.42 ATOM 619 CB ASP A 82 -3.542 0.373 61.101 1.00 37.77 ATOM 620 CG ASP A 82 -3.845 -0.950 60.433 1.00 40.64 ATOM 621 OD1 ASP A 82 -4.412 -0.956 59.336 1.00 42.96 ATOM 622 OD2 ASP A 82 -3.437 -1.969 61.063 1.00 44.36 ATOM 623 N LYS A 83 -0.549 -0.234 60.589 1.00 32.64 ATOM 624 CA LYS A 83 0.644 -1.012 60.250 1.00 31.86 ATOM 625 C LYS A 83 0.447 -1.921 59.052 1.00 30.36 ATOM 626 O LYS A 83 1.276 -2.000 58.146 1.00 30.14 ATOM 627 CB LYS A 83 1.127 -1.856 61.417 1.00 33.78 ATOM 628 CG LYS A 83 2.503 -1.534 61.962 1.00 36.39 ATOM 629 CD LYS A 83 3.566 -2.503 61.467 1.00 39.44 ATOM 630 CE LYS A 83 4.969 -2.030 61.817 1.00 42.64 ATOM 631 NZ LYS A 83 5.915 -3.166 62.035 1.00 43.96 ATOM 632 N ALA A 84 -0.654 -2.602 59.097 1.00 29.04 ATOM 633 CA ALA A 84 -1.117 -3.583 58.134 1.00 27.89 ATOM 634 C ALA A 84 -1.328 -2.995 56.748 1.00 26.41 ATOM 635 O ALA A 84 -1.010 -3.666 55.761 1.00 26.74 ATOM 636 CB ALA A 84 -2.407 -4.224 58.650 1.00 28.50 ATOM 637 N PHE A 85 -1.907 -1.799 56.724 1.00 24.31 ATOM 638 CA PHE A 85 -2.139 -1.142 55.447 1.00 21.71 ATOM 639 C PHE A 85 -0.753 -0.685 54.929 1.00 21.75 ATOM 640 O PHE A 85 -0.476 -0.767 53.751 1.00 21.20 ATOM 641 CB PHE A 85 -3.143 -0.026 55.447 1.00 20.41 ATOM 642 CG PHE A 85 -3.252 0.686 54.121 1.00 19.75 ATOM 643 CD1 PHE A 85 -4.096 0.193 53.135 1.00 18.99 ATOM 644 CD2 PHE A 85 -2.484 1.817 53.866 1.00 18.44 ATOM 645 CE1 PHE A 85 -4.206 0.834 51.889 1.00 19.39 ATOM 646 CE2 PHE A 85 -2.596 2.474 52.640 1.00 18.24 ATOM 647 CZ PHE A 85 -3.427 1.978 51.666 1.00 18.02 ATOM 648 N GLN A 86 0.058 -0.234 55.837 1.00 21.73 ATOM 649 CA GLN A 86 1.372 0.297 55.536 1.00 23.26 ATOM 650 C GLN A 86 2.287 -0.712 54.876 1.00 24.08 ATOM 651 O GLN A 86 3.149 -0.334 54.056 1.00 23.52 ATOM 652 CB GLN A 86 2.020 0.919 56.783 1.00 24.05 ATOM 653 CG GLN A 86 1.533 2.360 56.983 1.00 26.55 ATOM 654 CD GLN A 86 2.039 2.904 58.288 1.00 28.41 ATOM 655 OE1 GLN A 86 1.295 3.031 59.258 1.00 31.73 ATOM 656 NE2 GLN A 86 3.316 3.227 58.320 1.00 28.84 ATOM 657 N ASP A 87 2.133 -1.949 55.275 1.00 25.01 ATOM 658 CA ASP A 87 2.956 -3.063 54.766 1.00 26.41 ATOM 659 C ASP A 87 2.557 -3.479 53.365 1.00 24.18 ATOM 660 O ASP A 87 3.302 -4.244 52.723 1.00 25.02 ATOM 661 CB ASP A 87 3.061 -4.150 55.838 1.00 30.14 ATOM 662 CG ASP A 87 4.039 -3.829 56.944 1.00 34.56 ATOM 663 OD1 ASP A 87 4.558 -2.702 57.140 1.00 37.91 ATOM 664 OD2 ASP A 87 4.346 -4.762 57.727 1.00 37.48 ATOM 665 N LYS A 88 1.472 -2.992 52.842 1.00 22.96 ATOM 666 CA LYS A 88 0.995 -3.273 51.495 1.00 23.05 ATOM 667 C LYS A 88 1.757 -2.476 50.417 1.00 21.82 ATOM 668 O LYS A 88 1.645 -2.814 49.245 1.00 21.29 ATOM 669 CB LYS A 88 -0.479 -3.026 51.255 1.00 22.96 ATOM 670 CG LYS A 88 -1.416 -3.633 52.285 1.00 26.15 ATOM 671 CD LYS A 88 -2.133 -4.869 51.840 1.00 29.40 ATOM 672 CE LYS A 88 -3.379 -5.133 52.679 1.00 30.84 ATOM 673 NZ LYS A 88 -4.376 -4.089 52.275 1.00 33.19 ATOM 674 N LEU A 89 2.459 -1.444 50.793 1.00 21.18 ATOM 675 CA LEU A 89 3.230 -0.568 49.933 1.00 19.72 ATOM 676 C LEU A 89 4.724 -0.656 50.250 1.00 20.17 ATOM 677 O LEU A 89 5.152 -1.038 51.337 1.00 20.60 ATOM 678 CB LEU A 89 2.708 0.849 49.983 1.00 18.10 ATOM 679 CG LEU A 89 1.296 1.254 50.171 1.00 17.19 ATOM 680 CD1 LEU A 89 1.184 2.770 49.915 1.00 17.94 ATOM 681 CD2 LEU A 89 0.379 0.501 49.235 1.00 18.18 ATOM 682 N TYR A 90 5.520 -0.310 49.226 1.00 20.59 ATOM 683 CA TYR A 90 6.995 -0.296 49.369 1.00 20.03 ATOM 684 C TYR A 90 7.327 0.719 50.456 1.00 19.86 ATOM 685 O TYR A 90 6.814 1.858 50.386 1.00 20.24 ATOM 686 CB TYR A 90 7.621 0.112 48.004 1.00 20.39 ATOM 687 CG TYR A 90 7.426 -0.988 46.980 1.00 19.43 ATOM 688 CD1 TYR A 90 8.247 -2.109 47.033 1.00 20.30 ATOM 689 CD2 TYR A 90 6.437 -0.929 46.025 1.00 18.88 ATOM 690 CE1 TYR A 90 8.087 -3.166 46.120 1.00 21.37 ATOM 691 CE2 TYR A 90 6.265 -1.977 45.119 1.00 19.72 ATOM 692 CZ TYR A 90 7.083 -3.078 45.166 1.00 20.24 ATOM 693 OH TYR A 90 6.947 -4.135 44.309 1.00 23.22 ATOM 694 N PRO A 91 8.130 0.296 51.409 1.00 19.81 ATOM 695 CA PRO A 91 8.506 1.130 52.558 1.00 19.85 ATOM 696 C PRO A 91 9.011 2.519 52.217 1.00 18.84 ATOM 697 O PRO A 91 8.595 3.547 52.790 1.00 18.99 ATOM 698 CB PRO A 91 9.492 0.255 53.339 1.00 20.27 ATOM 699 CG PRO A 91 9.030 -1.158 53.027 1.00 20.27 ATOM 700 CD PRO A 91 8.700 -1.066 51.527 1.00 20.59 ATOM 701 N PHE A 92 9.883 2.571 51.211 1.00 17.93 ATOM 702 CA PHE A 92 10.517 3.781 50.721 1.00 15.97 ATOM 703 C PHE A 92 9.481 4.773 50.257 1.00 14.65 ATOM 704 O PHE A 92 9.768 5.985 50.278 1.00 15.44 ATOM 705 CB PHE A 92 11.617 3.449 49.673 1.00 15.70 ATOM 706 CG PHE A 92 11.102 3.310 48.268 1.00 16.10 ATOM 707 CD1 PHE A 92 11.050 4.413 47.425 1.00 15.91 ATOM 708 CD2 PHE A 92 10.693 2.061 47.783 1.00 15.61 ATOM 709 CE1 PHE A 92 10.542 4.304 46.119 1.00 15.33 ATOM 710 CE2 PHE A 92 10.202 1.946 46.502 1.00 15.03 ATOM 711 CZ PHE A 92 10.131 3.063 45.662 1.00 14.74 ATOM 712 N THR A 93 8.313 4.344 49.847 1.00 13.77 ATOM 713 CA THR A 93 7.288 5.249 49.367 1.00 13.93 ATOM 714 C THR A 93 6.665 6.067 50.518 1.00 13.93 ATOM 715 O THR A 93 6.250 7.205 50.233 1.00 13.19 ATOM 716 CB THR A 93 6.211 4.629 48.419 1.00 13.63 ATOM 717 OG1 THR A 93 5.455 3.666 49.208 1.00 15.78 ATOM 718 CG2 THR A 93 6.826 3.949 47.173 1.00 15.12 ATOM 719 N TRP A 94 6.672 5.513 51.697 1.00 14.10 ATOM 720 CA TRP A 94 6.117 6.224 52.880 1.00 14.60 ATOM 721 C TRP A 94 7.015 7.393 53.260 1.00 15.32 ATOM 722 O TRP A 94 6.523 8.386 53.820 1.00 16.10 ATOM 723 CB TRP A 94 5.862 5.242 54.021 1.00 13.64 ATOM 724 CG TRP A 94 4.685 4.338 53.802 1.00 13.98 ATOM 725 CD1 TRP A 94 4.741 2.956 53.713 1.00 14.15 ATOM 726 CD2 TRP A 94 3.315 4.698 53.664 1.00 13.12 ATOM 727 NE1 TRP A 94 3.490 2.454 53.509 1.00 13.70 ATOM 728 CE2 TRP A 94 2.589 3.479 53.473 1.00 13.92 ATOM 729 CE3 TRP A 94 2.607 5.878 53.730 1.00 11.40 ATOM 730 CZ2 TRP A 94 1.201 3.455 53.328 1.00 13.44 ATOM 731 CZ3 TRP A 94 1.232 5.876 53.558 1.00 12.27 ATOM 732 CH2 TRP A 94 0.533 4.683 53.361 1.00 13.85 ATOM 733 N ASP A 95 8.282 7.350 52.946 1.00 14.96 ATOM 734 CA ASP A 95 9.241 8.405 53.202 1.00 15.85 ATOM 735 C ASP A 95 8.972 9.667 52.408 1.00 16.08 ATOM 736 O ASP A 95 9.390 10.774 52.844 1.00 17.71 ATOM 737 CB ASP A 95 10.689 7.932 52.990 1.00 18.52 ATOM 738 CG ASP A 95 11.104 6.961 54.036 1.00 21.33 ATOM 739 OD1 ASP A 95 10.691 7.070 55.203 1.00 26.28 ATOM 740 OD2 ASP A 95 11.843 6.009 53.754 1.00 25.72 ATOM 741 N ALA A 96 8.309 9.573 51.282 1.00 13.99 ATOM 742 CA ALA A 96 7.996 10.647 50.391 1.00 13.76 ATOM 743 C ALA A 96 6.831 11.543 50.851 1.00 14.49 ATOM 744 O ALA A 96 6.652 12.662 50.351 1.00 14.33 ATOM 745 CB ALA A 96 7.621 10.137 48.988 1.00 9.79 ATOM 746 N VAL A 97 5.980 10.945 51.669 1.00 15.40 ATOM 747 CA VAL A 97 4.755 11.608 52.139 1.00 15.52 ATOM 748 C VAL A 97 4.765 11.930 53.645 1.00 17.45 ATOM 749 O VAL A 97 3.705 11.996 54.255 1.00 15.65 ATOM 750 CB VAL A 97 3.553 10.692 51.787 1.00 13.85 ATOM 751 CG1 VAL A 97 3.255 10.722 50.303 1.00 13.01 ATOM 752 CG2 VAL A 97 3.694 9.322 52.362 1.00 12.36 ATOM 753 N ARG A 98 5.922 12.062 54.196 1.00 19.71 ATOM 754 CA ARG A 98 6.186 12.426 55.585 1.00 23.97 ATOM 755 C ARG A 98 6.613 13.905 55.583 1.00 26.39 ATOM 756 O ARG A 98 7.496 14.315 54.804 1.00 26.81 ATOM 757 CB ARG A 98 7.262 11.559 56.189 1.00 24.88 ATOM 758 CG ARG A 98 6.910 10.854 57.461 1.00 28.34 ATOM 759 CD ARG A 98 7.864 9.781 57.803 1.00 31.29 ATOM 760 NE ARG A 98 7.652 8.571 57.026 1.00 36.32 ATOM 761 CZ ARG A 98 8.135 7.380 57.385 1.00 37.39 ATOM 762 NH1 ARG A 98 8.801 7.332 58.560 1.00 41.21 ATOM 763 NH2 ARG A 98 8.025 6.261 56.703 1.00 36.66 ATOM 764 N TYR A 99 5.963 14.711 56.400 1.00 28.66 ATOM 765 CA TYR A 99 6.285 16.134 56.536 1.00 31.21 ATOM 766 C TYR A 99 6.511 16.366 58.045 1.00 34.00 ATOM 767 O TYR A 99 5.547 16.426 58.810 1.00 34.53 ATOM 768 CB TYR A 99 5.288 17.128 55.977 1.00 30.84 ATOM 769 CG TYR A 99 5.811 18.550 55.973 1.00 31.78 ATOM 770 CD1 TYR A 99 6.861 18.876 55.110 1.00 32.60 ATOM 771 CD2 TYR A 99 5.309 19.535 56.820 1.00 32.48 ATOM 772 CE1 TYR A 99 7.385 20.158 55.077 1.00 34.93 ATOM 773 CE2 TYR A 99 5.812 20.835 56.793 1.00 33.79 ATOM 774 CZ TYR A 99 6.851 21.139 55.923 1.00 35.22 ATOM 775 OH TYR A 99 7.367 22.405 55.886 1.00 37.38 ATOM 776 N ASN A 100 7.781 16.390 58.361 1.00 37.03 ATOM 777 CA ASN A 100 8.310 16.567 59.708 1.00 39.43 ATOM 778 C ASN A 100 7.727 15.531 60.651 1.00 39.36 ATOM 779 O ASN A 100 7.149 15.861 61.677 1.00 39.65 ATOM 780 CB ASN A 100 8.139 18.009 60.187 1.00 43.24 ATOM 781 CG ASN A 100 9.270 18.889 59.654 1.00 45.78 ATOM 782 OD1 ASN A 100 10.287 18.399 59.148 1.00 47.06 ATOM 783 ND2 ASN A 100 9.063 20.204 59.754 1.00 48.97 ATOM 784 N GLY A 101 7.870 14.290 60.213 1.00 39.48 ATOM 785 CA GLY A 101 7.412 13.128 60.941 1.00 37.94 ATOM 786 C GLY A 101 5.975 12.726 60.703 1.00 36.41 ATOM 787 O GLY A 101 5.693 11.515 60.856 1.00 37.65 ATOM 788 N LYS A 102 5.110 13.644 60.354 1.00 34.19 ATOM 789 CA LYS A 102 3.688 13.384 60.115 1.00 31.24 ATOM 790 C LYS A 102 3.433 12.880 58.681 1.00 27.73 ATOM 791 O LYS A 102 3.981 13.478 57.754 1.00 26.10 ATOM 792 CB LYS A 102 2.874 14.668 60.295 1.00 34.22 ATOM 793 CG LYS A 102 1.996 14.755 61.531 1.00 37.28 ATOM 794 CD LYS A 102 2.719 15.450 62.671 1.00 42.03 ATOM 795 CE LYS A 102 2.032 15.307 64.021 1.00 44.71 ATOM 796 NZ LYS A 102 2.415 14.053 64.729 1.00 46.03 ATOM 797 N LEU A 103 2.639 11.842 58.572 1.00 23.77 ATOM 798 CA LEU A 103 2.205 11.263 57.285 1.00 20.24 ATOM 799 C LEU A 103 1.105 12.196 56.761 1.00 17.94 ATOM 800 O LEU A 103 0.046 12.328 57.424 1.00 16.66 ATOM 801 CB LEU A 103 1.681 9.856 57.519 1.00 21.15 ATOM 802 CG LEU A 103 2.444 8.599 57.297 1.00 20.40 ATOM 803 CD1 LEU A 103 3.507 8.377 58.349 1.00 23.86 ATOM 804 CD2 LEU A 103 1.493 7.402 57.419 1.00 22.19 ATOM 805 N ILE A 104 1.298 12.788 55.608 1.00 14.54 ATOM 806 CA ILE A 104 0.349 13.720 55.018 1.00 12.61 ATOM 807 C ILE A 104 -0.231 13.331 53.676 1.00 11.57 ATOM 808 O ILE A 104 -0.931 14.152 53.045 1.00 11.38 ATOM 809 CB ILE A 104 0.959 15.184 55.060 1.00 12.62 ATOM 810 CG1 ILE A 104 2.373 15.211 54.462 1.00 12.72 ATOM 811 CG2 ILE A 104 0.997 15.697 56.526 1.00 14.33 ATOM 812 CD1 ILE A 104 2.496 15.347 52.951 1.00 12.83 ATOM 813 N ALA A 105 -0.021 12.086 53.254 1.00 11.27 ATOM 814 CA ALA A 105 -0.602 11.635 51.960 1.00 11.68 ATOM 815 C ALA A 105 -0.340 10.148 51.740 1.00 10.24 ATOM 816 O ALA A 105 0.502 9.579 52.379 1.00 10.59 ATOM 817 CB ALA A 105 -0.008 12.453 50.808 1.00 11.31 ATOM 818 N TYR A 106 -1.111 9.596 50.813 1.00 11.34 ATOM 819 CA TYR A 106 -0.894 8.151 50.452 1.00 11.25 ATOM 820 C TYR A 106 -0.119 8.134 49.096 1.00 10.46 ATOM 821 O TYR A 106 -0.560 8.835 48.207 1.00 8.70 ATOM 822 CB TYR A 106 -2.253 7.479 50.163 1.00 11.77 ATOM 823 CG TYR A 106 -3.158 7.305 51.374 1.00 13.95 ATOM 824 CD1 TYR A 106 -3.087 6.159 52.172 1.00 13.42 ATOM 825 CD2 TYR A 106 -4.114 8.288 51.681 1.00 15.69 ATOM 826 CE1 TYR A 106 -3.959 5.961 53.261 1.00 12.56 ATOM 827 CE2 TYR A 106 -4.980 8.094 52.794 1.00 15.81 ATOM 828 CZ TYR A 106 -4.880 6.947 53.553 1.00 13.75 ATOM 829 OH TYR A 106 -5.715 6.752 54.621 1.00 15.88 ATOM 830 N PRO A 107 0.896 7.308 49.071 1.00 11.78 ATOM 831 CA PRO A 107 1.752 7.135 47.856 1.00 11.74 ATOM 832 C PRO A 107 0.944 6.372 46.817 1.00 11.24 ATOM 833 O PRO A 107 0.202 5.465 47.222 1.00 12.61 ATOM 834 CB PRO A 107 2.947 6.408 48.382 1.00 12.46 ATOM 835 CG PRO A 107 2.853 6.192 49.848 1.00 11.42 ATOM 836 CD PRO A 107 1.388 6.460 50.165 1.00 11.82 ATOM 837 N ILE A 108 0.948 6.729 45.574 1.00 11.76 ATOM 838 CA ILE A 108 0.188 6.059 44.510 1.00 12.69 ATOM 839 C ILE A 108 1.105 5.387 43.456 1.00 13.42 ATOM 840 O ILE A 108 1.137 4.157 43.325 1.00 12.05 ATOM 841 CB ILE A 108 -0.824 7.010 43.820 1.00 11.64 ATOM 842 CG1 ILE A 108 -1.714 7.792 44.819 1.00 12.32 ATOM 843 CG2 ILE A 108 -1.698 6.292 42.746 1.00 13.13 ATOM 844 CD1 ILE A 108 -2.594 7.014 45.766 1.00 12.38 ATOM 845 N ALA A 109 1.865 6.238 42.769 1.00 14.28 ATOM 846 CA ALA A 109 2.805 5.777 41.690 1.00 13.47 ATOM 847 C ALA A 109 4.197 6.286 41.939 1.00 14.11 ATOM 848 O ALA A 109 4.373 7.215 42.743 1.00 12.94 ATOM 849 CB ALA A 109 2.205 6.320 40.388 1.00 12.95 ATOM 850 N VAL A 110 5.213 5.720 41.340 1.00 14.52 ATOM 851 CA VAL A 110 6.634 6.073 41.482 1.00 14.87 ATOM 852 C VAL A 110 7.260 6.333 40.095 1.00 16.14 ATOM 853 O VAL A 110 6.959 5.649 39.094 1.00 16.24 ATOM 854 CB VAL A 110 7.314 4.939 42.266 1.00 15.78 ATOM 855 CG1 VAL A 110 8.798 5.159 42.543 1.00 15.44 ATOM 856 CG2 VAL A 110 6.569 4.575 43.554 1.00 16.08 ATOM 857 N GLU A 111 8.091 7.354 39.992 1.00 15.12 ATOM 858 CA GLU A 111 8.752 7.728 38.725 1.00 14.98 ATOM 859 C GLU A 111 10.204 8.031 38.977 1.00 14.19 ATOM 860 O GLU A 111 10.542 8.625 40.031 1.00 14.54 ATOM 861 CB GLU A 111 8.151 8.965 38.105 1.00 17.47 ATOM 862 CG GLU A 111 7.344 8.796 36.844 1.00 22.67 ATOM 863 CD GLU A 111 6.721 10.066 36.316 1.00 26.09 ATOM 864 OE1 GLU A 111 7.008 11.154 36.821 1.00 27.17 ATOM 865 OE2 GLU A 111 5.960 9.774 35.366 1.00 27.04 ATOM 866 N ALA A 112 11.075 7.565 38.079 1.00 12.07 ATOM 867 CA ALA A 112 12.511 7.787 38.188 1.00 9.91 ATOM 868 C ALA A 112 13.073 7.618 36.764 1.00 10.79 ATOM 869 O ALA A 112 12.398 6.936 35.948 1.00 12.57 ATOM 870 CB ALA A 112 13.198 6.862 39.166 1.00 7.95 ATOM 871 N LEU A 113 14.199 8.254 36.526 1.00 9.85 ATOM 872 CA LEU A 113 14.878 8.132 35.201 1.00 8.62 ATOM 873 C LEU A 113 15.414 6.722 35.082 1.00 6.99 ATOM 874 O LEU A 113 15.746 6.051 36.034 1.00 5.87 ATOM 875 CB LEU A 113 16.031 9.159 35.200 1.00 8.28 ATOM 876 CG LEU A 113 15.660 10.604 34.974 1.00 7.20 ATOM 877 CD1 LEU A 113 16.906 11.497 35.124 1.00 8.03 ATOM 878 CD2 LEU A 113 14.950 10.837 33.669 1.00 5.88 ATOM 879 N SER A 114 15.612 6.319 33.814 1.00 8.98 ATOM 880 CA SER A 114 16.185 4.985 33.536 1.00 7.65 ATOM 881 C SER A 114 17.146 5.161 32.305 1.00 6.31 ATOM 882 O SER A 114 17.043 6.210 31.712 1.00 6.74 ATOM 883 CB SER A 114 15.064 4.021 33.134 1.00 8.73 ATOM 884 OG SER A 114 14.386 3.468 34.235 1.00 8.45 ATOM 885 N LEU A 115 17.932 4.171 32.119 1.00 7.32 ATOM 886 CA LEU A 115 18.852 4.126 30.922 1.00 8.45 ATOM 887 C LEU A 115 18.026 3.529 29.765 1.00 7.94 ATOM 888 O LEU A 115 17.506 2.433 29.999 1.00 8.70 ATOM 889 CB LEU A 115 20.047 3.300 31.242 1.00 8.88 ATOM 890 CG LEU A 115 21.374 3.571 30.551 1.00 13.50 ATOM 891 CD1 LEU A 115 22.037 2.305 30.052 1.00 13.68 ATOM 892 CD2 LEU A 115 21.384 4.680 29.550 1.00 13.97 ATOM 893 N ILE A 116 17.870 4.226 28.695 1.00 8.36 ATOM 894 CA ILE A 116 17.104 3.793 27.502 1.00 9.63 ATOM 895 C ILE A 116 18.151 3.472 26.424 1.00 11.47 ATOM 896 O ILE A 116 18.968 4.378 26.239 1.00 12.88 ATOM 897 CB ILE A 116 16.077 4.826 27.037 1.00 8.42 ATOM 898 CG1 ILE A 116 15.073 5.164 28.208 1.00 7.94 ATOM 899 CG2 ILE A 116 15.257 4.405 25.776 1.00 8.26 ATOM 900 CD1 ILE A 116 14.096 6.282 27.844 1.00 7.74 ATOM 901 N TYR A 117 18.108 2.344 25.749 1.00 11.46 ATOM 902 CA TYR A 117 19.182 2.074 24.754 1.00 10.41 ATOM 903 C TYR A 117 18.590 1.439 23.507 1.00 11.01 ATOM 904 O TYR A 117 17.491 0.921 23.575 1.00 11.37 ATOM 905 CB TYR A 117 20.268 1.236 25.397 1.00 12.64 ATOM 906 CG TYR A 117 19.821 -0.173 25.727 1.00 15.52 ATOM 907 CD1 TYR A 117 19.050 -0.477 26.853 1.00 16.31 ATOM 908 CD2 TYR A 117 20.174 -1.198 24.856 1.00 17.27 ATOM 909 CE1 TYR A 117 18.654 -1.791 27.115 1.00 18.13 ATOM 910 CE2 TYR A 117 19.765 -2.503 25.089 1.00 18.79 ATOM 911 CZ TYR A 117 19.017 -2.797 26.205 1.00 19.16 ATOM 912 OH TYR A 117 18.671 -4.089 26.460 1.00 21.49 ATOM 913 N ASN A 118 19.313 1.547 22.439 1.00 10.95 ATOM 914 CA ASN A 118 18.931 1.080 21.084 1.00 12.04 ATOM 915 C ASN A 118 19.488 -0.340 20.962 1.00 12.91 ATOM 916 O ASN A 118 20.692 -0.447 20.914 1.00 12.41 ATOM 917 CB ASN A 118 19.482 2.100 20.087 1.00 12.21 ATOM 918 CG ASN A 118 19.040 1.784 18.659 1.00 12.82 ATOM 919 OD1 ASN A 118 18.946 0.573 18.362 1.00 16.81 ATOM 920 ND2 ASN A 118 18.710 2.771 17.890 1.00 11.52 ATOM 921 N LYS A 119 18.589 -1.320 20.988 1.00 14.83 ATOM 922 CA LYS A 119 18.954 -2.743 20.960 1.00 16.85 ATOM 923 C LYS A 119 19.655 -3.148 19.668 1.00 17.35 ATOM 924 O LYS A 119 20.415 -4.144 19.722 1.00 18.35 ATOM 925 CB LYS A 119 17.788 -3.658 21.230 1.00 17.35 ATOM 926 CG LYS A 119 17.517 -3.870 22.700 1.00 21.76 ATOM 927 CD LYS A 119 16.084 -3.946 23.122 1.00 23.76 ATOM 928 CE LYS A 119 15.259 -5.055 22.664 1.00 26.95 ATOM 929 NZ LYS A 119 14.674 -5.918 23.716 1.00 30.33 ATOM 930 N ASP A 120 19.423 -2.383 18.632 1.00 18.01 ATOM 931 CA ASP A 120 20.078 -2.627 17.322 1.00 19.92 ATOM 932 C ASP A 120 21.504 -2.097 17.283 1.00 20.62 ATOM 933 O ASP A 120 22.324 -2.612 16.466 1.00 23.24 ATOM 934 CB ASP A 120 19.227 -2.085 16.172 1.00 19.84 ATOM 935 CG ASP A 120 17.912 -2.751 15.925 1.00 19.41 ATOM 936 OD1 ASP A 120 17.791 -3.925 16.298 1.00 20.54 ATOM 937 OD2 ASP A 120 17.000 -2.146 15.352 1.00 21.55 ATOM 938 N LEU A 121 21.908 -1.117 18.060 1.00 19.62 ATOM 939 CA LEU A 121 23.270 -0.574 18.047 1.00 18.15 ATOM 940 C LEU A 121 24.117 -1.146 19.163 1.00 19.58 ATOM 941 O LEU A 121 25.341 -1.222 19.045 1.00 19.17 ATOM 942 CB LEU A 121 23.168 0.955 18.223 1.00 15.91 ATOM 943 CG LEU A 121 22.536 1.702 17.078 1.00 17.00 ATOM 944 CD1 LEU A 121 22.378 3.200 17.349 1.00 15.81 ATOM 945 CD2 LEU A 121 23.404 1.465 15.819 1.00 15.96 ATOM 946 N LEU A 122 23.397 -1.503 20.223 1.00 20.54 ATOM 947 CA LEU A 122 24.024 -1.976 21.455 1.00 22.99 ATOM 948 C LEU A 122 23.323 -3.239 21.937 1.00 26.02 ATOM 949 O LEU A 122 22.178 -3.150 22.363 1.00 26.24 ATOM 950 CB LEU A 122 23.921 -0.746 22.391 1.00 21.89 ATOM 951 CG LEU A 122 24.971 -0.520 23.425 1.00 21.81 ATOM 952 CD1 LEU A 122 26.349 -0.377 22.809 1.00 21.80 ATOM 953 CD2 LEU A 122 24.657 0.733 24.254 1.00 21.68 ATOM 954 N PRO A 123 24.062 -4.337 21.874 1.00 29.42 ATOM 955 CA PRO A 123 23.614 -5.663 22.283 1.00 31.26 ATOM 956 C PRO A 123 23.207 -5.699 23.747 1.00 31.53 ATOM 957 O PRO A 123 22.105 -6.099 24.158 1.00 32.70 ATOM 958 CB PRO A 123 24.825 -6.582 22.031 1.00 31.73 ATOM 959 CG PRO A 123 26.020 -5.649 22.111 1.00 32.31 ATOM 960 CD PRO A 123 25.483 -4.387 21.406 1.00 31.27 ATOM 961 N ASN A 124 24.185 -5.290 24.538 1.00 31.60 ATOM 962 CA ASN A 124 24.006 -5.225 26.002 1.00 31.41 ATOM 963 C ASN A 124 24.447 -3.822 26.438 1.00 28.48 ATOM 964 O ASN A 124 25.508 -3.371 26.013 1.00 28.20 ATOM 965 CB ASN A 124 24.723 -6.368 26.692 1.00 34.71 ATOM 966 CG ASN A 124 23.943 -7.674 26.585 1.00 38.69 ATOM 967 OD1 ASN A 124 23.677 -8.362 27.582 1.00 41.25 ATOM 968 ND2 ASN A 124 23.571 -8.027 25.350 1.00 40.58 ATOM 969 N PRO A 125 23.590 -3.228 27.238 1.00 26.02 ATOM 970 CA PRO A 125 23.887 -1.872 27.767 1.00 23.80 ATOM 971 C PRO A 125 25.088 -1.981 28.683 1.00 20.47 ATOM 972 O PRO A 125 25.289 -3.036 29.287 1.00 18.62 ATOM 973 CB PRO A 125 22.610 -1.500 28.514 1.00 25.24 ATOM 974 CG PRO A 125 21.939 -2.793 28.864 1.00 25.15 ATOM 975 CD PRO A 125 22.317 -3.749 27.721 1.00 25.12 ATOM 976 N PRO A 126 25.828 -0.886 28.821 1.00 18.83 ATOM 977 CA PRO A 126 27.005 -0.854 29.700 1.00 16.79 ATOM 978 C PRO A 126 26.524 -0.920 31.150 1.00 15.65 ATOM 979 O PRO A 126 25.458 -0.360 31.394 1.00 15.04 ATOM 980 CB PRO A 126 27.658 0.496 29.411 1.00 17.74 ATOM 981 CG PRO A 126 26.538 1.357 28.905 1.00 18.12 ATOM 982 CD PRO A 126 25.626 0.394 28.140 1.00 18.46 ATOM 983 N LYS A 127 27.276 -1.572 31.988 1.00 13.46 ATOM 984 CA LYS A 127 26.924 -1.696 33.366 1.00 15.42 ATOM 985 C LYS A 127 27.477 -0.551 34.205 1.00 14.21 ATOM 986 O LYS A 127 26.993 -0.243 35.279 1.00 12.96 ATOM 987 CB LYS A 127 27.355 -3.042 33.942 1.00 18.50 ATOM 988 CG LYS A 127 26.372 -4.141 33.421 1.00 23.79 ATOM 989 CD LYS A 127 24.914 -3.770 33.718 1.00 28.78 ATOM 990 CE LYS A 127 23.987 -3.716 32.513 1.00 29.77 ATOM 991 NZ LYS A 127 22.568 -3.406 32.874 1.00 29.36 ATOM 992 N THR A 128 28.447 0.078 33.632 1.00 13.90 ATOM 993 CA THR A 128 29.266 1.149 34.216 1.00 14.12 ATOM 994 C THR A 128 29.324 2.410 33.408 1.00 13.69 ATOM 995 O THR A 128 29.245 2.387 32.165 1.00 13.97 ATOM 996 CB THR A 128 30.708 0.444 34.230 1.00 16.06 ATOM 997 OG1 THR A 128 30.945 -0.151 35.527 1.00 20.05 ATOM 998 CG2 THR A 128 31.828 1.194 33.616 1.00 16.06 ATOM 999 N TRP A 129 29.495 3.548 34.115 1.00 12.44 ATOM 1000 CA TRP A 129 29.677 4.841 33.478 1.00 11.36 ATOM 1001 C TRP A 129 31.144 4.897 32.924 1.00 10.70 ATOM 1002 O TRP A 129 31.360 5.566 31.942 1.00 11.31 ATOM 1003 CB TRP A 129 29.514 6.046 34.415 1.00 11.74 ATOM 1004 CG TRP A 129 28.114 6.514 34.653 1.00 12.02 ATOM 1005 CD1 TRP A 129 27.253 6.204 35.672 1.00 9.63 ATOM 1006 CD2 TRP A 129 27.413 7.429 33.795 1.00 12.45 ATOM 1007 NE1 TRP A 129 26.039 6.873 35.481 1.00 9.70 ATOM 1008 CE2 TRP A 129 26.145 7.656 34.376 1.00 10.62 ATOM 1009 CE3 TRP A 129 27.794 8.121 32.639 1.00 11.23 ATOM 1010 CZ2 TRP A 129 25.223 8.500 33.781 1.00 9.89 ATOM 1011 CZ3 TRP A 129 26.888 8.997 32.119 1.00 10.80 ATOM 1012 CH2 TRP A 129 25.615 9.169 32.644 1.00 10.60 ATOM 1013 N GLU A 130 32.056 4.265 33.612 1.00 12.18 ATOM 1014 CA GLU A 130 33.476 4.269 33.315 1.00 14.00 ATOM 1015 C GLU A 130 33.813 3.706 31.951 1.00 15.44 ATOM 1016 O GLU A 130 34.824 4.099 31.346 1.00 16.46 ATOM 1017 CB GLU A 130 34.355 3.617 34.370 1.00 13.21 ATOM 1018 CG GLU A 130 34.424 4.370 35.720 1.00 14.39 ATOM 1019 CD GLU A 130 33.429 4.036 36.764 1.00 14.62 ATOM 1020 OE1 GLU A 130 32.380 3.466 36.429 1.00 14.60 ATOM 1021 OE2 GLU A 130 33.602 4.291 37.948 1.00 18.25 ATOM 1022 N GLU A 131 32.926 2.884 31.438 1.00 16.68 ATOM 1023 CA GLU A 131 33.139 2.258 30.123 1.00 17.26 ATOM 1024 C GLU A 131 32.481 3.003 29.015 1.00 17.84 ATOM 1025 O GLU A 131 32.626 2.554 27.851 1.00 18.95 ATOM 1026 CB GLU A 131 32.673 0.815 30.182 1.00 18.53 ATOM 1027 CG GLU A 131 31.203 0.504 30.269 1.00 20.87 ATOM 1028 CD GLU A 131 30.824 -0.931 30.509 1.00 23.18 ATOM 1029 OE1 GLU A 131 30.813 -1.454 31.610 1.00 23.74 ATOM 1030 OE2 GLU A 131 30.485 -1.520 29.456 1.00 24.27 ATOM 1031 N ILE A 132 31.819 4.130 29.230 1.00 16.49 ATOM 1032 CA ILE A 132 31.172 4.888 28.184 1.00 16.00 ATOM 1033 C ILE A 132 32.118 5.556 27.198 1.00 17.03 ATOM 1034 O ILE A 132 31.868 5.518 25.970 1.00 15.59 ATOM 1035 CB ILE A 132 30.005 5.770 28.721 1.00 15.57 ATOM 1036 CG1 ILE A 132 28.919 4.796 29.253 1.00 16.27 ATOM 1037 CG2 ILE A 132 29.474 6.769 27.683 1.00 15.85 ATOM 1038 CD1 ILE A 132 27.638 5.509 29.760 1.00 16.98 ATOM 1039 N PRO A 133 33.159 6.197 27.668 1.00 17.55 ATOM 1040 CA PRO A 133 34.143 6.833 26.791 1.00 18.55 ATOM 1041 C PRO A 133 34.665 5.902 25.687 1.00 17.75 ATOM 1042 O PRO A 133 34.684 6.328 24.525 1.00 19.00 ATOM 1043 CB PRO A 133 35.249 7.257 27.772 1.00 18.73 ATOM 1044 CG PRO A 133 34.480 7.524 29.051 1.00 17.84 ATOM 1045 CD PRO A 133 33.536 6.323 29.097 1.00 18.09 ATOM 1046 N ALA A 134 35.085 4.718 25.992 1.00 16.95 ATOM 1047 CA ALA A 134 35.598 3.663 25.134 1.00 17.06 ATOM 1048 C ALA A 134 34.563 3.186 24.125 1.00 18.94 ATOM 1049 O ALA A 134 34.813 2.908 22.918 1.00 19.68 ATOM 1050 CB ALA A 134 36.161 2.553 25.990 1.00 15.81 ATOM 1051 N LEU A 135 33.339 3.059 24.577 1.00 18.37 ATOM 1052 CA LEU A 135 32.182 2.662 23.793 1.00 18.66 ATOM 1053 C LEU A 135 31.862 3.748 22.765 1.00 17.37 ATOM 1054 O LEU A 135 31.484 3.442 21.637 1.00 17.30 ATOM 1055 CB LEU A 135 31.003 2.454 24.758 1.00 18.76 ATOM 1056 CG LEU A 135 29.839 1.657 24.282 1.00 20.62 ATOM 1057 CD1 LEU A 135 30.300 0.183 24.283 1.00 22.01 ATOM 1058 CD2 LEU A 135 28.670 1.817 25.259 1.00 20.31 ATOM 1059 N ASP A 136 31.995 4.991 23.210 1.00 16.21 ATOM 1060 CA ASP A 136 31.732 6.133 22.344 1.00 16.74 ATOM 1061 C ASP A 136 32.764 6.141 21.174 1.00 17.81 ATOM 1062 O ASP A 136 32.324 6.479 20.082 1.00 17.70 ATOM 1063 CB ASP A 136 31.759 7.454 23.083 1.00 15.14 ATOM 1064 CG ASP A 136 31.242 8.560 22.214 1.00 14.79 ATOM 1065 OD1 ASP A 136 30.128 8.575 21.719 1.00 16.04 ATOM 1066 OD2 ASP A 136 32.059 9.476 22.002 1.00 16.11 ATOM 1067 N LYS A 137 33.994 5.829 21.469 1.00 19.72 ATOM 1068 CA LYS A 137 35.051 5.799 20.418 1.00 22.31 ATOM 1069 C LYS A 137 34.754 4.665 19.430 1.00 21.35 ATOM 1070 O LYS A 137 34.843 4.876 18.202 1.00 20.15 ATOM 1071 CB LYS A 137 36.417 5.800 21.013 1.00 25.50 ATOM 1072 CG LYS A 137 37.111 4.463 21.187 1.00 32.24 ATOM 1073 CD LYS A 137 37.834 3.978 19.944 1.00 36.76 ATOM 1074 CE LYS A 137 38.015 2.459 19.926 1.00 39.32 ATOM 1075 NZ LYS A 137 38.283 2.012 18.520 1.00 41.28 ATOM 1076 N GLU A 138 34.243 3.536 19.874 1.00 21.30 ATOM 1077 CA GLU A 138 33.875 2.427 18.997 1.00 21.19 ATOM 1078 C GLU A 138 32.680 2.739 18.128 1.00 20.77 ATOM 1079 O GLU A 138 32.642 2.341 16.941 1.00 20.19 ATOM 1080 CB GLU A 138 33.553 1.124 19.692 1.00 23.72 ATOM 1081 CG GLU A 138 34.734 0.382 20.321 1.00 29.27 ATOM 1082 CD GLU A 138 34.353 -0.888 21.051 1.00 33.60 ATOM 1083 OE1 GLU A 138 33.540 -1.547 20.348 1.00 33.80 ATOM 1084 OE2 GLU A 138 34.784 -1.156 22.179 1.00 35.57 ATOM 1085 N LEU A 139 31.705 3.453 18.687 1.00 18.91 ATOM 1086 CA LEU A 139 30.507 3.845 17.965 1.00 17.16 ATOM 1087 C LEU A 139 30.743 4.964 16.974 1.00 16.16 ATOM 1088 O LEU A 139 30.064 5.085 15.952 1.00 15.64 ATOM 1089 CB LEU A 139 29.382 4.105 18.966 1.00 16.97 ATOM 1090 CG LEU A 139 28.670 2.873 19.523 1.00 19.22 ATOM 1091 CD1 LEU A 139 27.882 3.233 20.783 1.00 16.35 ATOM 1092 CD2 LEU A 139 27.691 2.390 18.428 1.00 19.09 ATOM 1093 N LYS A 140 31.679 5.820 17.283 1.00 16.25 ATOM 1094 CA LYS A 140 32.093 6.971 16.496 1.00 17.13 ATOM 1095 C LYS A 140 32.734 6.480 15.166 1.00 17.38 ATOM 1096 O LYS A 140 32.635 7.152 14.149 1.00 17.86 ATOM 1097 CB LYS A 140 33.054 7.858 17.259 1.00 17.56 ATOM 1098 CG LYS A 140 32.473 8.726 18.387 1.00 19.44 ATOM 1099 CD LYS A 140 31.435 9.693 17.903 1.00 21.41 ATOM 1100 CE LYS A 140 30.676 10.421 18.973 1.00 24.09 ATOM 1101 NZ LYS A 140 31.618 11.056 19.969 1.00 25.43 ATOM 1102 N ALA A 141 33.354 5.345 15.252 1.00 18.18 ATOM 1103 CA ALA A 141 33.963 4.633 14.111 1.00 19.99 ATOM 1104 C ALA A 141 32.913 4.361 13.034 1.00 20.94 ATOM 1105 O ALA A 141 33.303 4.207 11.872 1.00 22.05 ATOM 1106 CB ALA A 141 34.603 3.342 14.585 1.00 18.72 ATOM 1107 N LYS A 142 31.641 4.299 13.371 1.00 21.60 ATOM 1108 CA LYS A 142 30.516 4.075 12.491 1.00 22.35 ATOM 1109 C LYS A 142 29.588 5.277 12.328 1.00 21.22 ATOM 1110 O LYS A 142 28.476 5.154 11.729 1.00 20.91 ATOM 1111 CB LYS A 142 29.590 2.955 12.926 1.00 25.58 ATOM 1112 CG LYS A 142 30.182 1.565 12.925 1.00 31.58 ATOM 1113 CD LYS A 142 29.816 0.806 14.192 1.00 34.48 ATOM 1114 CE LYS A 142 28.338 0.555 14.423 1.00 35.00 ATOM 1115 NZ LYS A 142 28.234 -0.435 15.560 1.00 37.58 ATOM 1116 N GLY A 143 30.004 6.407 12.857 1.00 20.45 ATOM 1117 CA GLY A 143 29.243 7.643 12.752 1.00 20.28 ATOM 1118 C GLY A 143 28.120 7.734 13.811 1.00 19.91 ATOM 1119 O GLY A 143 27.248 8.567 13.626 1.00 20.59 ATOM 1120 N LYS A 144 28.188 6.947 14.848 1.00 19.56 ATOM 1121 CA LYS A 144 27.175 6.965 15.925 1.00 19.04 ATOM 1122 C LYS A 144 27.861 7.377 17.228 1.00 18.45 ATOM 1123 O LYS A 144 29.081 7.178 17.367 1.00 19.05 ATOM 1124 CB LYS A 144 26.574 5.572 16.111 1.00 18.97 ATOM 1125 CG LYS A 144 25.961 4.850 14.923 1.00 17.82 ATOM 1126 CD LYS A 144 24.878 5.648 14.270 1.00 18.60 ATOM 1127 CE LYS A 144 24.096 4.973 13.169 1.00 20.08 ATOM 1128 NZ LYS A 144 22.939 5.827 12.775 1.00 20.45 ATOM 1129 N SER A 145 27.089 7.894 18.193 1.00 17.85 ATOM 1130 CA SER A 145 27.637 8.243 19.519 1.00 15.94 ATOM 1131 C SER A 145 27.017 7.264 20.544 1.00 14.84 ATOM 1132 O SER A 145 25.967 6.665 20.315 1.00 14.65 ATOM 1133 CB SER A 145 27.345 9.673 19.903 1.00 15.93 ATOM 1134 OG SER A 145 25.960 9.877 20.065 1.00 19.00 ATOM 1135 N ALA A 146 27.668 7.117 21.679 1.00 13.30 ATOM 1136 CA ALA A 146 27.242 6.238 22.747 1.00 11.58 ATOM 1137 C ALA A 146 26.015 6.761 23.493 1.00 13.16 ATOM 1138 O ALA A 146 24.993 6.054 23.582 1.00 13.34 ATOM 1139 CB ALA A 146 28.420 6.008 23.669 1.00 8.58 ATOM 1140 N LEU A 147 26.080 7.983 24.007 1.00 13.63 ATOM 1141 CA LEU A 147 25.001 8.549 24.825 1.00 12.68 ATOM 1142 C LEU A 147 24.771 10.018 24.639 1.00 13.47 ATOM 1143 O LEU A 147 25.764 10.761 24.436 1.00 15.31 ATOM 1144 CB LEU A 147 25.544 8.295 26.288 1.00 11.85 ATOM 1145 CG LEU A 147 24.750 8.972 27.423 1.00 11.88 ATOM 1146 CD1 LEU A 147 23.399 8.345 27.666 1.00 11.84 ATOM 1147 CD2 LEU A 147 25.596 8.867 28.693 1.00 11.12 ATOM 1148 N MET A 148 23.536 10.451 24.700 1.00 12.27 ATOM 1149 CA MET A 148 23.141 11.837 24.643 1.00 13.66 ATOM 1150 C MET A 148 21.954 12.039 25.617 1.00 14.59 ATOM 1151 O MET A 148 20.948 11.328 25.456 1.00 15.43 ATOM 1152 CB MET A 148 22.766 12.309 23.246 1.00 16.42 ATOM 1153 CG MET A 148 24.014 12.893 22.550 1.00 19.53 ATOM 1154 SD MET A 148 23.496 13.372 20.918 1.00 28.20 ATOM 1155 CE MET A 148 22.577 14.859 21.144 1.00 21.45 ATOM 1156 N PHE A 149 22.062 12.982 26.527 1.00 13.52 ATOM 1157 CA PHE A 149 20.968 13.298 27.464 1.00 14.03 ATOM 1158 C PHE A 149 21.030 14.811 27.774 1.00 14.70 ATOM 1159 O PHE A 149 21.993 15.497 27.436 1.00 14.65 ATOM 1160 CB PHE A 149 20.994 12.443 28.705 1.00 13.14 ATOM 1161 CG PHE A 149 22.111 12.564 29.672 1.00 13.09 ATOM 1162 CD1 PHE A 149 23.359 12.064 29.437 1.00 13.64 ATOM 1163 CD2 PHE A 149 21.904 13.248 30.886 1.00 14.21 ATOM 1164 CE1 PHE A 149 24.379 12.161 30.392 1.00 16.15 ATOM 1165 CE2 PHE A 149 22.868 13.334 31.851 1.00 13.77 ATOM 1166 CZ PHE A 149 24.135 12.831 31.613 1.00 14.41 ATOM 1167 N ASN A 150 19.965 15.283 28.404 1.00 15.14 ATOM 1168 CA ASN A 150 19.823 16.686 28.789 1.00 14.34 ATOM 1169 C ASN A 150 20.874 17.054 29.841 1.00 15.12 ATOM 1170 O ASN A 150 20.798 16.596 30.959 1.00 15.41 ATOM 1171 CB ASN A 150 18.416 16.909 29.343 1.00 15.40 ATOM 1172 CG ASN A 150 18.124 18.389 29.562 1.00 15.30 ATOM 1173 OD1 ASN A 150 18.956 19.242 29.307 1.00 14.10 ATOM 1174 ND2 ASN A 150 16.911 18.628 30.035 1.00 17.17 ATOM 1175 N LEU A 151 21.827 17.876 29.471 1.00 15.04 ATOM 1176 CA LEU A 151 22.873 18.333 30.357 1.00 15.73 ATOM 1177 C LEU A 151 22.514 19.660 31.048 1.00 15.23 ATOM 1178 O LEU A 151 23.235 19.989 31.988 1.00 15.77 ATOM 1179 CB LEU A 151 24.181 18.442 29.546 1.00 14.38 ATOM 1180 CG LEU A 151 24.741 17.134 28.985 1.00 14.13 ATOM 1181 CD1 LEU A 151 26.042 17.424 28.227 1.00 14.97 ATOM 1182 CD2 LEU A 151 25.117 16.164 30.067 1.00 13.19 ATOM 1183 N GLN A 152 21.501 20.323 30.641 1.00 15.70 ATOM 1184 CA GLN A 152 21.075 21.636 31.100 1.00 17.70 ATOM 1185 C GLN A 152 20.405 21.695 32.460 1.00 18.95 ATOM 1186 O GLN A 152 20.583 22.677 33.208 1.00 19.24 ATOM 1187 CB GLN A 152 20.136 22.295 30.080 1.00 16.95 ATOM 1188 CG GLN A 152 20.736 22.615 28.745 1.00 22.33 ATOM 1189 CD GLN A 152 22.187 22.977 28.714 1.00 24.80 ATOM 1190 OE1 GLN A 152 22.556 24.079 29.094 1.00 26.78 ATOM 1191 NE2 GLN A 152 23.056 22.048 28.233 1.00 26.75 ATOM 1192 N GLU A 153 19.609 20.682 32.753 1.00 18.48 ATOM 1193 CA GLU A 153 18.878 20.616 34.016 1.00 18.52 ATOM 1194 C GLU A 153 19.440 19.597 34.937 1.00 16.69 ATOM 1195 O GLU A 153 19.720 18.433 34.570 1.00 15.14 ATOM 1196 CB GLU A 153 17.399 20.474 33.718 1.00 23.25 ATOM 1197 CG GLU A 153 16.509 19.941 34.847 1.00 30.02 ATOM 1198 CD GLU A 153 16.189 20.941 35.932 1.00 33.02 ATOM 1199 OE1 GLU A 153 16.027 22.136 35.658 1.00 34.38 ATOM 1200 OE2 GLU A 153 16.142 20.378 37.053 1.00 32.94 ATOM 1201 N PRO A 154 19.648 20.000 36.217 1.00 14.75 ATOM 1202 CA PRO A 154 20.199 19.123 37.227 1.00 13.27 ATOM 1203 C PRO A 154 19.383 17.846 37.498 1.00 10.29 ATOM 1204 O PRO A 154 19.961 16.916 38.020 1.00 8.84 ATOM 1205 CB PRO A 154 20.385 19.962 38.472 1.00 13.30 ATOM 1206 CG PRO A 154 19.982 21.340 38.101 1.00 14.81 ATOM 1207 CD PRO A 154 19.392 21.353 36.719 1.00 13.92 ATOM 1208 N TYR A 155 18.114 17.869 37.231 1.00 11.01 ATOM 1209 CA TYR A 155 17.248 16.682 37.404 1.00 11.58 ATOM 1210 C TYR A 155 17.890 15.514 36.604 1.00 11.98 ATOM 1211 O TYR A 155 17.998 14.381 37.072 1.00 12.84 ATOM 1212 CB TYR A 155 15.828 16.994 36.901 1.00 11.85 ATOM 1213 CG TYR A 155 14.891 15.800 37.045 1.00 13.39 ATOM 1214 CD1 TYR A 155 14.278 15.448 38.249 1.00 15.25 ATOM 1215 CD2 TYR A 155 14.666 14.963 35.943 1.00 15.05 ATOM 1216 CE1 TYR A 155 13.444 14.344 38.365 1.00 15.47 ATOM 1217 CE2 TYR A 155 13.887 13.829 36.039 1.00 15.58 ATOM 1218 CZ TYR A 155 13.222 13.538 37.219 1.00 16.89 ATOM 1219 OH TYR A 155 12.449 12.408 37.264 1.00 16.58 ATOM 1220 N PHE A 156 18.358 15.822 35.402 1.00 11.48 ATOM 1221 CA PHE A 156 19.025 14.850 34.531 1.00 10.40 ATOM 1222 C PHE A 156 20.451 14.535 34.896 1.00 10.54 ATOM 1223 O PHE A 156 20.873 13.357 34.786 1.00 11.46 ATOM 1224 CB PHE A 156 18.871 15.323 33.083 1.00 10.84 ATOM 1225 CG PHE A 156 17.477 15.280 32.580 1.00 11.62 ATOM 1226 CD1 PHE A 156 16.629 16.372 32.760 1.00 11.61 ATOM 1227 CD2 PHE A 156 17.009 14.123 31.935 1.00 12.00 ATOM 1228 CE1 PHE A 156 15.320 16.342 32.308 1.00 12.35 ATOM 1229 CE2 PHE A 156 15.691 14.089 31.467 1.00 12.25 ATOM 1230 CZ PHE A 156 14.836 15.186 31.654 1.00 13.11 ATOM 1231 N THR A 157 21.264 15.451 35.414 1.00 9.12 ATOM 1232 CA THR A 157 22.645 15.131 35.740 1.00 9.94 ATOM 1233 C THR A 157 22.852 14.609 37.127 1.00 10.41 ATOM 1234 O THR A 157 23.850 13.951 37.406 1.00 9.74 ATOM 1235 CB THR A 157 23.583 16.361 35.400 1.00 11.30 ATOM 1236 OG1 THR A 157 22.973 17.433 36.183 1.00 12.39 ATOM 1237 CG2 THR A 157 23.492 16.716 33.880 1.00 12.16 ATOM 1238 N TRP A 158 21.905 14.842 38.023 1.00 11.61 ATOM 1239 CA TRP A 158 22.009 14.365 39.408 1.00 11.36 ATOM 1240 C TRP A 158 22.340 12.912 39.581 1.00 11.12 ATOM 1241 O TRP A 158 23.160 12.605 40.479 1.00 11.34 ATOM 1242 CB TRP A 158 20.747 14.759 40.209 1.00 13.32 ATOM 1243 CG TRP A 158 20.935 14.567 41.690 1.00 13.13 ATOM 1244 CD1 TRP A 158 20.348 13.655 42.493 1.00 12.10 ATOM 1245 CD2 TRP A 158 21.806 15.347 42.533 1.00 14.71 ATOM 1246 NE1 TRP A 158 20.770 13.802 43.773 1.00 11.99 ATOM 1247 CE2 TRP A 158 21.645 14.848 43.840 1.00 13.38 ATOM 1248 CE3 TRP A 158 22.694 16.397 42.296 1.00 14.89 ATOM 1249 CZ2 TRP A 158 22.356 15.373 44.930 1.00 13.88 ATOM 1250 CZ3 TRP A 158 23.395 16.916 43.394 1.00 15.67 ATOM 1251 CH2 TRP A 158 23.232 16.418 44.690 1.00 12.99 ATOM 1252 N PRO A 159 21.734 11.976 38.808 1.00 9.40 ATOM 1253 CA PRO A 159 22.059 10.552 38.991 1.00 8.77 ATOM 1254 C PRO A 159 23.529 10.242 39.061 1.00 8.60 ATOM 1255 O PRO A 159 23.954 9.423 39.896 1.00 8.88 ATOM 1256 CB PRO A 159 21.293 9.844 37.894 1.00 6.62 ATOM 1257 CG PRO A 159 20.332 10.803 37.328 1.00 6.54 ATOM 1258 CD PRO A 159 20.743 12.198 37.775 1.00 7.59 ATOM 1259 N LEU A 160 24.321 10.862 38.186 1.00 8.72 ATOM 1260 CA LEU A 160 25.774 10.682 38.116 1.00 10.81 ATOM 1261 C LEU A 160 26.506 11.425 39.254 1.00 10.33 ATOM 1262 O LEU A 160 27.379 10.850 39.879 1.00 11.51 ATOM 1263 CB LEU A 160 26.268 11.162 36.739 1.00 9.76 ATOM 1264 CG LEU A 160 27.529 10.668 36.108 1.00 12.95 ATOM 1265 CD1 LEU A 160 28.180 11.767 35.264 1.00 12.88 ATOM 1266 CD2 LEU A 160 28.532 9.939 36.951 1.00 9.49 ATOM 1267 N ILE A 161 26.121 12.677 39.459 1.00 12.49 ATOM 1268 CA ILE A 161 26.722 13.532 40.504 1.00 13.21 ATOM 1269 C ILE A 161 26.560 12.922 41.881 1.00 12.93 ATOM 1270 O ILE A 161 27.507 12.853 42.659 1.00 14.88 ATOM 1271 CB ILE A 161 26.212 15.015 40.370 1.00 12.87 ATOM 1272 CG1 ILE A 161 26.782 15.617 39.056 1.00 12.94 ATOM 1273 CG2 ILE A 161 26.606 15.917 41.575 1.00 13.89 ATOM 1274 CD1 ILE A 161 25.928 16.825 38.572 1.00 13.89 ATOM 1275 N ALA A 162 25.392 12.410 42.199 1.00 12.95 ATOM 1276 CA ALA A 162 25.059 11.771 43.458 1.00 11.99 ATOM 1277 C ALA A 162 25.578 10.381 43.671 1.00 12.88 ATOM 1278 O ALA A 162 25.777 9.943 44.829 1.00 13.80 ATOM 1279 CB ALA A 162 23.513 11.719 43.520 1.00 13.02 ATOM 1280 N ALA A 163 25.764 9.576 42.641 1.00 13.69 ATOM 1281 CA ALA A 163 26.220 8.196 42.665 1.00 13.24 ATOM 1282 C ALA A 163 27.209 7.852 43.764 1.00 14.22 ATOM 1283 O ALA A 163 26.941 6.944 44.566 1.00 14.26 ATOM 1284 CB ALA A 163 26.824 7.791 41.282 1.00 12.70 ATOM 1285 N ASP A 164 28.355 8.523 43.774 1.00 14.59 ATOM 1286 CA ASP A 164 29.408 8.286 44.739 1.00 15.31 ATOM 1287 C ASP A 164 29.343 9.067 46.040 1.00 15.74 ATOM 1288 O ASP A 164 30.369 9.236 46.728 1.00 16.28 ATOM 1289 CB ASP A 164 30.756 8.500 44.038 1.00 16.25 ATOM 1290 CG ASP A 164 31.857 7.790 44.810 1.00 17.84 ATOM 1291 OD1 ASP A 164 31.686 6.670 45.288 1.00 18.33 ATOM 1292 OD2 ASP A 164 32.881 8.481 44.921 1.00 19.58 ATOM 1293 N GLY A 165 28.192 9.499 46.483 1.00 17.37 ATOM 1294 CA GLY A 165 28.092 10.216 47.770 1.00 16.75 ATOM 1295 C GLY A 165 27.330 11.485 47.823 1.00 15.61 ATOM 1296 O GLY A 165 27.112 11.934 48.959 1.00 17.11 ATOM 1297 N GLY A 166 26.879 12.104 46.784 1.00 15.17 ATOM 1298 CA GLY A 166 26.118 13.362 46.841 1.00 16.21 ATOM 1299 C GLY A 166 24.698 13.126 47.284 1.00 16.59 ATOM 1300 O GLY A 166 24.145 12.045 47.091 1.00 17.18 ATOM 1301 N TYR A 167 24.088 14.148 47.853 1.00 17.49 ATOM 1302 CA TYR A 167 22.679 14.144 48.311 1.00 17.71 ATOM 1303 C TYR A 167 22.265 15.618 48.446 1.00 17.10 ATOM 1304 O TYR A 167 23.190 16.423 48.586 1.00 17.29 ATOM 1305 CB TYR A 167 22.453 13.414 49.618 1.00 18.10 ATOM 1306 CG TYR A 167 23.342 13.851 50.773 1.00 19.82 ATOM 1307 CD1 TYR A 167 22.967 14.898 51.624 1.00 19.06 ATOM 1308 CD2 TYR A 167 24.558 13.205 50.994 1.00 20.68 ATOM 1309 CE1 TYR A 167 23.801 15.278 52.668 1.00 19.02 ATOM 1310 CE2 TYR A 167 25.400 13.566 52.041 1.00 21.32 ATOM 1311 CZ TYR A 167 24.977 14.629 52.872 1.00 20.28 ATOM 1312 OH TYR A 167 25.811 15.006 53.876 1.00 22.70 ATOM 1313 N ALA A 168 21.001 15.924 48.373 1.00 16.91 ATOM 1314 CA ALA A 168 20.500 17.293 48.465 1.00 17.80 ATOM 1315 C ALA A 168 20.563 17.715 49.951 1.00 19.84 ATOM 1316 O ALA A 168 21.390 18.563 50.290 1.00 20.16 ATOM 1317 CB ALA A 168 19.149 17.499 47.843 1.00 15.78 ATOM 1318 N PHE A 169 19.780 17.034 50.764 1.00 21.06 ATOM 1319 CA PHE A 169 19.661 17.254 52.213 1.00 21.29 ATOM 1320 C PHE A 169 19.641 15.945 52.974 1.00 22.35 ATOM 1321 O PHE A 169 18.880 15.009 52.623 1.00 23.65 ATOM 1322 CB PHE A 169 18.421 18.093 52.508 1.00 19.40 ATOM 1323 CG PHE A 169 18.300 19.428 51.888 1.00 18.77 ATOM 1324 CD1 PHE A 169 18.895 20.550 52.510 1.00 18.71 ATOM 1325 CD2 PHE A 169 17.581 19.625 50.722 1.00 18.67 ATOM 1326 CE1 PHE A 169 18.770 21.799 51.949 1.00 18.12 ATOM 1327 CE2 PHE A 169 17.466 20.881 50.128 1.00 19.05 ATOM 1328 CZ PHE A 169 18.058 21.993 50.767 1.00 18.92 ATOM 1329 N LYS A 170 20.435 15.833 54.003 1.00 23.99 ATOM 1330 CA LYS A 170 20.480 14.613 54.809 1.00 26.97 ATOM 1331 C LYS A 170 19.116 14.325 55.427 1.00 29.79 ATOM 1332 O LYS A 170 18.500 15.169 56.069 1.00 29.89 ATOM 1333 CB LYS A 170 21.549 14.668 55.868 1.00 26.11 ATOM 1334 CG LYS A 170 21.599 13.400 56.693 1.00 28.09 ATOM 1335 CD LYS A 170 21.849 12.165 55.846 1.00 28.21 ATOM 1336 CE LYS A 170 23.230 11.616 56.127 1.00 29.44 ATOM 1337 NZ LYS A 170 24.215 12.559 55.567 1.00 29.99 ATOM 1338 N TYR A 171 18.628 13.110 55.198 1.00 32.90 ATOM 1339 CA TYR A 171 17.315 12.696 55.736 1.00 36.04 ATOM 1340 C TYR A 171 17.578 11.536 56.693 1.00 39.48 ATOM 1341 O TYR A 171 18.366 10.633 56.341 1.00 39.88 ATOM 1342 CB TYR A 171 16.339 12.332 54.642 1.00 34.78 ATOM 1343 CG TYR A 171 14.984 11.783 55.031 1.00 34.43 ATOM 1344 CD1 TYR A 171 14.834 10.489 55.495 1.00 34.21 ATOM 1345 CD2 TYR A 171 13.825 12.545 54.881 1.00 34.87 ATOM 1346 CE1 TYR A 171 13.599 9.972 55.840 1.00 35.22 ATOM 1347 CE2 TYR A 171 12.562 12.056 55.177 1.00 35.73 ATOM 1348 CZ TYR A 171 12.462 10.756 55.670 1.00 36.09 ATOM 1349 OH TYR A 171 11.254 10.211 56.006 1.00 36.60 ATOM 1350 N GLU A 172 16.934 11.604 57.857 1.00 44.47 ATOM 1351 CA GLU A 172 17.167 10.498 58.813 1.00 49.21 ATOM 1352 C GLU A 172 16.096 10.267 59.829 1.00 49.97 ATOM 1353 O GLU A 172 16.414 9.656 60.892 1.00 51.76 ATOM 1354 CB GLU A 172 18.527 10.706 59.528 1.00 51.46 ATOM 1355 CG GLU A 172 19.280 9.402 59.833 1.00 55.40 ATOM 1356 CD GLU A 172 20.753 9.359 59.580 1.00 57.33 ATOM 1357 OE1 GLU A 172 21.312 10.460 59.810 1.00 58.65 ATOM 1358 OE2 GLU A 172 21.374 8.357 59.209 1.00 58.52 ATOM 1359 N ASN A 173 14.847 10.636 59.550 1.00 50.35 ATOM 1360 CA ASN A 173 13.779 10.455 60.550 1.00 50.40 ATOM 1361 C ASN A 173 12.470 11.095 60.128 1.00 49.22 ATOM 1362 O ASN A 173 11.776 11.661 61.019 1.00 50.26 ATOM 1363 CB ASN A 173 14.276 11.172 61.856 1.00 52.78 ATOM 1364 CG ASN A 173 14.520 12.658 61.536 1.00 54.80 ATOM 1365 OD1 ASN A 173 15.110 13.009 60.491 1.00 55.59 ATOM 1366 ND2 ASN A 173 14.037 13.533 62.424 1.00 55.58 ATOM 1367 N GLY A 174 12.142 11.045 58.862 1.00 47.20 ATOM 1368 CA GLY A 174 10.890 11.684 58.383 1.00 44.55 ATOM 1369 C GLY A 174 11.131 13.200 58.325 1.00 42.58 ATOM 1370 O GLY A 174 10.224 13.992 58.000 1.00 43.00 ATOM 1371 N LYS A 175 12.380 13.510 58.624 1.00 39.94 ATOM 1372 CA LYS A 175 12.883 14.878 58.694 1.00 37.51 ATOM 1373 C LYS A 175 14.243 15.041 58.013 1.00 34.72 ATOM 1374 O LYS A 175 15.184 14.249 58.101 1.00 32.35 ATOM 1375 CB LYS A 175 12.930 15.308 60.165 1.00 38.27 ATOM 1376 CG LYS A 175 13.652 16.584 60.497 1.00 40.52 ATOM 1377 CD LYS A 175 12.840 17.831 60.261 1.00 42.96 ATOM 1378 CE LYS A 175 13.484 19.101 60.792 1.00 44.35 ATOM 1379 NZ LYS A 175 13.641 19.053 62.268 1.00 44.31 ATOM 1380 N TYR A 176 14.292 16.169 57.325 1.00 33.09 ATOM 1381 CA TYR A 176 15.429 16.655 56.568 1.00 32.62 ATOM 1382 C TYR A 176 16.222 17.683 57.393 1.00 33.52 ATOM 1383 O TYR A 176 15.596 18.648 57.868 1.00 34.94 ATOM 1384 CB TYR A 176 14.958 17.346 55.258 1.00 29.73 ATOM 1385 CG TYR A 176 14.541 16.361 54.188 1.00 28.21 ATOM 1386 CD1 TYR A 176 15.502 15.582 53.528 1.00 26.14 ATOM 1387 CD2 TYR A 176 13.193 16.193 53.849 1.00 26.42 ATOM 1388 CE1 TYR A 176 15.103 14.687 52.538 1.00 25.94 ATOM 1389 CE2 TYR A 176 12.779 15.280 52.896 1.00 25.03 ATOM 1390 CZ TYR A 176 13.754 14.541 52.221 1.00 25.69 ATOM 1391 OH TYR A 176 13.343 13.626 51.286 1.00 24.31 ATOM 1392 N ASP A 177 17.511 17.461 57.500 1.00 33.51 ATOM 1393 CA ASP A 177 18.452 18.371 58.188 1.00 32.65 ATOM 1394 C ASP A 177 18.921 19.366 57.112 1.00 33.06 ATOM 1395 O ASP A 177 19.780 18.993 56.293 1.00 33.42 ATOM 1396 CB ASP A 177 19.584 17.601 58.835 1.00 31.30 ATOM 1397 CG ASP A 177 20.617 18.566 59.440 1.00 31.75 ATOM 1398 OD1 ASP A 177 20.392 19.789 59.378 1.00 28.83 ATOM 1399 OD2 ASP A 177 21.626 18.005 59.938 1.00 31.17 ATOM 1400 N ILE A 178 18.369 20.561 57.114 1.00 32.64 ATOM 1401 CA ILE A 178 18.697 21.543 56.088 1.00 34.13 ATOM 1402 C ILE A 178 20.066 22.174 56.129 1.00 33.35 ATOM 1403 O ILE A 178 20.410 23.015 55.264 1.00 33.56 ATOM 1404 CB ILE A 178 17.515 22.566 55.974 1.00 36.18 ATOM 1405 CG1 ILE A 178 17.614 23.630 57.100 1.00 37.48 ATOM 1406 CG2 ILE A 178 16.137 21.850 55.959 1.00 36.92 ATOM 1407 CD1 ILE A 178 16.997 25.002 56.664 1.00 37.41 ATOM 1408 N LYS A 179 20.874 21.790 57.079 1.00 33.40 ATOM 1409 CA LYS A 179 22.233 22.288 57.234 1.00 33.83 ATOM 1410 C LYS A 179 23.204 21.156 56.912 1.00 33.07 ATOM 1411 O LYS A 179 24.403 21.311 57.101 1.00 33.75 ATOM 1412 CB LYS A 179 22.562 22.902 58.576 1.00 36.08 ATOM 1413 CG LYS A 179 22.001 24.312 58.774 1.00 38.64 ATOM 1414 CD LYS A 179 22.914 25.423 58.294 1.00 41.63 ATOM 1415 CE LYS A 179 22.485 26.054 56.989 1.00 43.18 ATOM 1416 NZ LYS A 179 21.351 26.997 57.156 1.00 43.84 ATOM 1417 N ASP A 180 22.632 20.066 56.439 1.00 31.51 ATOM 1418 CA ASP A 180 23.388 18.880 56.006 1.00 29.61 ATOM 1419 C ASP A 180 23.036 18.746 54.505 1.00 28.20 ATOM 1420 O ASP A 180 22.020 18.179 54.112 1.00 26.92 ATOM 1421 CB ASP A 180 23.121 17.663 56.851 1.00 30.30 ATOM 1422 CG ASP A 180 24.228 16.639 56.827 1.00 32.26 ATOM 1423 OD1 ASP A 180 25.213 16.776 56.077 1.00 33.77 ATOM 1424 OD2 ASP A 180 24.159 15.646 57.590 1.00 34.09 ATOM 1425 N VAL A 181 23.874 19.401 53.748 1.00 27.89 ATOM 1426 CA VAL A 181 23.793 19.476 52.260 1.00 26.79 ATOM 1427 C VAL A 181 24.955 18.696 51.687 1.00 26.07 ATOM 1428 O VAL A 181 26.070 18.786 52.261 1.00 25.59 ATOM 1429 CB VAL A 181 23.713 20.947 51.824 1.00 26.44 ATOM 1430 CG1 VAL A 181 23.787 21.136 50.326 1.00 25.18 ATOM 1431 CG2 VAL A 181 22.421 21.547 52.385 1.00 26.79 ATOM 1432 N GLY A 182 24.698 17.939 50.623 1.00 24.89 ATOM 1433 CA GLY A 182 25.758 17.117 50.025 1.00 24.23 ATOM 1434 C GLY A 182 26.172 17.399 48.599 1.00 24.46 ATOM 1435 O GLY A 182 26.406 16.454 47.809 1.00 21.84 ATOM 1436 N VAL A 183 26.292 18.667 48.219 1.00 25.37 ATOM 1437 CA VAL A 183 26.681 19.000 46.850 1.00 27.16 ATOM 1438 C VAL A 183 28.173 19.288 46.730 1.00 28.39 ATOM 1439 O VAL A 183 28.689 19.317 45.601 1.00 28.59 ATOM 1440 CB VAL A 183 25.770 20.080 46.236 1.00 26.62 ATOM 1441 CG1 VAL A 183 24.320 19.941 46.663 1.00 26.36 ATOM 1442 CG2 VAL A 183 26.293 21.465 46.358 1.00 26.86 ATOM 1443 N ASP A 184 28.851 19.462 47.851 1.00 29.34 ATOM 1444 CA ASP A 184 30.276 19.802 47.814 1.00 30.76 ATOM 1445 C ASP A 184 31.147 18.688 48.305 1.00 29.86 ATOM 1446 O ASP A 184 32.380 18.900 48.459 1.00 32.09 ATOM 1447 CB ASP A 184 30.481 21.108 48.601 1.00 34.92 ATOM 1448 CG ASP A 184 31.896 21.624 48.532 1.00 39.95 ATOM 1449 OD1 ASP A 184 32.569 21.276 47.521 1.00 43.41 ATOM 1450 OD2 ASP A 184 32.383 22.319 49.443 1.00 42.82 ATOM 1451 N ASN A 185 30.589 17.533 48.595 1.00 28.38 ATOM 1452 CA ASN A 185 31.494 16.449 49.088 1.00 26.79 ATOM 1453 C ASN A 185 32.298 15.858 47.914 1.00 26.26 ATOM 1454 O ASN A 185 32.169 16.210 46.736 1.00 25.59 ATOM 1455 CB ASN A 185 30.770 15.515 50.007 1.00 26.35 ATOM 1456 CG ASN A 185 29.614 14.740 49.407 1.00 25.21 ATOM 1457 OD1 ASN A 185 29.674 14.367 48.237 1.00 24.07 ATOM 1458 ND2 ASN A 185 28.634 14.499 50.260 1.00 24.38 ATOM 1459 N ALA A 186 33.200 14.970 48.291 1.00 24.85 ATOM 1460 CA ALA A 186 34.111 14.294 47.379 1.00 24.54 ATOM 1461 C ALA A 186 33.280 13.489 46.374 1.00 24.70 ATOM 1462 O ALA A 186 33.599 13.434 45.170 1.00 25.94 ATOM 1463 CB ALA A 186 35.051 13.424 48.193 1.00 23.63 ATOM 1464 N GLY A 187 32.198 12.939 46.890 1.00 23.83 ATOM 1465 CA GLY A 187 31.234 12.136 46.139 1.00 21.47 ATOM 1466 C GLY A 187 30.754 12.901 44.917 1.00 20.59 ATOM 1467 O GLY A 187 30.965 12.443 43.787 1.00 19.50 ATOM 1468 N ALA A 188 30.109 14.037 45.168 1.00 19.03 ATOM 1469 CA ALA A 188 29.578 14.903 44.125 1.00 17.39 ATOM 1470 C ALA A 188 30.715 15.401 43.226 1.00 18.21 ATOM 1471 O ALA A 188 30.568 15.554 42.012 1.00 16.91 ATOM 1472 CB ALA A 188 28.858 16.090 44.738 1.00 17.36 ATOM 1473 N LYS A 189 31.842 15.680 43.873 1.00 18.95 ATOM 1474 CA LYS A 189 33.031 16.151 43.173 1.00 20.84 ATOM 1475 C LYS A 189 33.491 15.080 42.176 1.00 20.74 ATOM 1476 O LYS A 189 33.781 15.429 41.012 1.00 21.86 ATOM 1477 CB LYS A 189 34.179 16.437 44.125 1.00 24.23 ATOM 1478 CG LYS A 189 34.897 17.750 43.858 1.00 29.09 ATOM 1479 CD LYS A 189 34.344 18.892 44.710 1.00 31.68 ATOM 1480 CE LYS A 189 34.794 18.814 46.156 1.00 33.18 ATOM 1481 NZ LYS A 189 35.921 17.848 46.291 1.00 34.01 ATOM 1482 N ALA A 190 33.558 13.835 42.625 1.00 19.77 ATOM 1483 CA ALA A 190 33.971 12.738 41.717 1.00 19.19 ATOM 1484 C ALA A 190 33.048 12.685 40.500 1.00 18.44 ATOM 1485 O ALA A 190 33.534 12.631 39.362 1.00 18.71 ATOM 1486 CB ALA A 190 34.070 11.399 42.406 1.00 17.71 ATOM 1487 N GLY A 191 31.753 12.718 40.706 1.00 17.24 ATOM 1488 CA GLY A 191 30.731 12.670 39.682 1.00 15.61 ATOM 1489 C GLY A 191 30.708 13.735 38.624 1.00 15.65 ATOM 1490 O GLY A 191 30.599 13.486 37.414 1.00 12.88 ATOM 1491 N LEU A 192 30.772 15.003 39.065 1.00 15.56 ATOM 1492 CA LEU A 192 30.775 16.173 38.204 1.00 15.55 ATOM 1493 C LEU A 192 32.065 16.191 37.389 1.00 14.85 ATOM 1494 O LEU A 192 32.057 16.600 36.247 1.00 14.73 ATOM 1495 CB LEU A 192 30.604 17.468 39.048 1.00 15.57 ATOM 1496 CG LEU A 192 30.428 18.735 38.253 1.00 17.18 ATOM 1497 CD1 LEU A 192 29.222 18.648 37.306 1.00 16.10 ATOM 1498 CD2 LEU A 192 30.191 19.968 39.124 1.00 17.95 ATOM 1499 N THR A 193 33.132 15.779 38.020 1.00 16.89 ATOM 1500 CA THR A 193 34.437 15.716 37.345 1.00 18.99 ATOM 1501 C THR A 193 34.296 14.726 36.183 1.00 19.55 ATOM 1502 O THR A 193 34.701 15.066 35.081 1.00 22.12 ATOM 1503 CB THR A 193 35.642 15.319 38.241 1.00 19.96 ATOM 1504 OG1 THR A 193 35.860 16.381 39.198 1.00 20.48 ATOM 1505 CG2 THR A 193 36.939 15.039 37.428 1.00 22.45 ATOM 1506 N PHE A 194 33.750 13.560 36.476 1.00 19.50 ATOM 1507 CA PHE A 194 33.561 12.550 35.390 1.00 18.96 ATOM 1508 C PHE A 194 32.741 13.145 34.255 1.00 18.83 ATOM 1509 O PHE A 194 33.042 12.922 33.046 1.00 18.51 ATOM 1510 CB PHE A 194 32.955 11.255 35.926 1.00 19.76 ATOM 1511 CG PHE A 194 32.937 10.153 34.891 1.00 20.43 ATOM 1512 CD1 PHE A 194 34.054 9.342 34.735 1.00 21.47 ATOM 1513 CD2 PHE A 194 31.819 9.979 34.083 1.00 20.94 ATOM 1514 CE1 PHE A 194 34.042 8.327 33.756 1.00 22.96 ATOM 1515 CE2 PHE A 194 31.789 8.975 33.120 1.00 21.95 ATOM 1516 CZ PHE A 194 32.906 8.159 32.956 1.00 22.09 ATOM 1517 N LEU A 195 31.699 13.889 34.602 1.00 17.66 ATOM 1518 CA LEU A 195 30.828 14.497 33.598 1.00 17.44 ATOM 1519 C LEU A 195 31.576 15.507 32.733 1.00 17.92 ATOM 1520 O LEU A 195 31.414 15.547 31.507 1.00 16.60 ATOM 1521 CB LEU A 195 29.581 15.053 34.290 1.00 17.61 ATOM 1522 CG LEU A 195 28.659 15.943 33.487 1.00 18.81 ATOM 1523 CD1 LEU A 195 27.996 15.108 32.390 1.00 21.32 ATOM 1524 CD2 LEU A 195 27.554 16.518 34.387 1.00 18.35 ATOM 1525 N VAL A 196 32.349 16.344 33.402 1.00 18.31 ATOM 1526 CA VAL A 196 33.113 17.413 32.762 1.00 18.00 ATOM 1527 C VAL A 196 34.112 16.791 31.787 1.00 18.30 ATOM 1528 O VAL A 196 34.187 17.331 30.677 1.00 18.71 ATOM 1529 CB VAL A 196 33.711 18.372 33.786 1.00 19.94 ATOM 1530 CG1 VAL A 196 34.687 19.374 33.151 1.00 19.22 ATOM 1531 CG2 VAL A 196 32.604 19.138 34.530 1.00 18.06 ATOM 1532 N ASP A 197 34.766 15.754 32.200 1.00 19.58 ATOM 1533 CA ASP A 197 35.744 15.007 31.397 1.00 23.20 ATOM 1534 C ASP A 197 35.075 14.448 30.116 1.00 23.84 ATOM 1535 O ASP A 197 35.772 14.241 29.107 1.00 24.40 ATOM 1536 CB ASP A 197 36.486 13.923 32.150 1.00 25.66 ATOM 1537 CG ASP A 197 37.531 14.396 33.132 1.00 30.57 ATOM 1538 OD1 ASP A 197 37.860 15.591 33.213 1.00 33.33 ATOM 1539 OD2 ASP A 197 38.073 13.541 33.879 1.00 32.79 ATOM 1540 N LEU A 198 33.793 14.169 30.180 1.00 23.64 ATOM 1541 CA LEU A 198 33.050 13.637 29.065 1.00 23.94 ATOM 1542 C LEU A 198 32.940 14.694 27.977 1.00 24.01 ATOM 1543 O LEU A 198 33.112 14.337 26.820 1.00 24.28 ATOM 1544 CB LEU A 198 31.659 13.144 29.452 1.00 24.54 ATOM 1545 CG LEU A 198 31.557 11.789 30.120 1.00 25.14 ATOM 1546 CD1 LEU A 198 30.158 11.622 30.708 1.00 25.81 ATOM 1547 CD2 LEU A 198 31.811 10.721 29.056 1.00 25.27 ATOM 1548 N ILE A 199 32.612 15.894 28.419 1.00 24.14 ATOM 1549 CA ILE A 199 32.411 17.022 27.534 1.00 25.03 ATOM 1550 C ILE A 199 33.716 17.521 26.900 1.00 26.00 ATOM 1551 O ILE A 199 33.716 17.852 25.712 1.00 25.25 ATOM 1552 CB ILE A 199 31.624 18.181 28.224 1.00 24.36 ATOM 1553 CG1 ILE A 199 30.273 17.685 28.769 1.00 24.42 ATOM 1554 CG2 ILE A 199 31.408 19.376 27.240 1.00 25.31 ATOM 1555 CD1 ILE A 199 29.541 18.723 29.686 1.00 23.39 ATOM 1556 N LYS A 200 34.756 17.589 27.703 1.00 27.71 ATOM 1557 CA LYS A 200 36.046 18.099 27.196 1.00 30.12 ATOM 1558 C LYS A 200 36.733 17.089 26.288 1.00 30.61 ATOM 1559 O LYS A 200 37.479 17.481 25.361 1.00 31.70 ATOM 1560 CB LYS A 200 36.904 18.674 28.253 1.00 30.62 ATOM 1561 CG LYS A 200 37.654 17.758 29.193 1.00 34.30 ATOM 1562 CD LYS A 200 38.465 18.631 30.167 1.00 37.95 ATOM 1563 CE LYS A 200 39.174 17.818 31.234 1.00 40.14 ATOM 1564 NZ LYS A 200 38.577 18.129 32.583 1.00 42.09 ATOM 1565 N ASN A 201 36.460 15.817 26.501 1.00 29.69 ATOM 1566 CA ASN A 201 37.005 14.719 25.700 1.00 27.91 ATOM 1567 C ASN A 201 36.082 14.428 24.499 1.00 26.86 ATOM 1568 O ASN A 201 36.252 13.408 23.819 1.00 26.25 ATOM 1569 CB ASN A 201 37.303 13.498 26.512 1.00 27.82 ATOM 1570 CG ASN A 201 38.464 13.697 27.450 1.00 27.49 ATOM 1571 OD1 ASN A 201 38.336 13.294 28.608 1.00 30.62 ATOM 1572 ND2 ASN A 201 39.519 14.275 26.934 1.00 28.47 ATOM 1573 N LYS A 202 35.166 15.318 24.313 1.00 25.76 ATOM 1574 CA LYS A 202 34.225 15.366 23.237 1.00 26.75 ATOM 1575 C LYS A 202 33.302 14.196 23.055 1.00 26.02 ATOM 1576 O LYS A 202 32.704 14.062 21.972 1.00 26.47 ATOM 1577 CB LYS A 202 34.978 15.712 21.925 1.00 29.12 ATOM 1578 CG LYS A 202 35.529 17.171 21.991 1.00 29.69 ATOM 1579 CD LYS A 202 34.377 18.153 21.853 1.00 34.06 ATOM 1580 CE LYS A 202 33.823 18.835 23.065 1.00 35.49 ATOM 1581 NZ LYS A 202 32.539 18.306 23.601 1.00 32.86 ATOM 1582 N HIS A 203 33.097 13.432 24.102 1.00 25.13 ATOM 1583 CA HIS A 203 32.189 12.285 24.116 1.00 24.08 ATOM 1584 C HIS A 203 30.761 12.784 24.276 1.00 25.02 ATOM 1585 O HIS A 203 29.835 12.005 24.053 1.00 26.32 ATOM 1586 CB HIS A 203 32.440 11.281 25.247 1.00 21.66 ATOM 1587 CG HIS A 203 33.762 10.624 25.066 1.00 19.73 ATOM 1588 ND1 HIS A 203 34.782 10.645 25.960 1.00 20.47 ATOM 1589 CD2 HIS A 203 34.210 9.932 23.992 1.00 19.78 ATOM 1590 CE1 HIS A 203 35.822 9.971 25.478 1.00 19.81 ATOM 1591 NE2 HIS A 203 35.481 9.523 24.281 1.00 21.23 ATOM 1592 N MET A 204 30.676 14.035 24.616 1.00 26.30 ATOM 1593 CA MET A 204 29.427 14.794 24.886 1.00 26.93 ATOM 1594 C MET A 204 29.619 16.287 24.645 1.00 26.67 ATOM 1595 O MET A 204 30.701 16.812 24.884 1.00 26.10 ATOM 1596 CB MET A 204 29.161 14.466 26.374 1.00 26.96 ATOM 1597 CG MET A 204 27.744 14.531 26.709 1.00 28.62 ATOM 1598 SD MET A 204 27.273 13.176 27.890 1.00 29.02 ATOM 1599 CE MET A 204 25.601 13.008 27.191 1.00 29.70 ATOM 1600 N ASN A 205 28.629 16.974 24.146 1.00 27.75 ATOM 1601 CA ASN A 205 28.534 18.390 23.852 1.00 28.54 ATOM 1602 C ASN A 205 27.842 19.102 25.031 1.00 28.13 ATOM 1603 O ASN A 205 26.777 18.651 25.460 1.00 26.56 ATOM 1604 CB ASN A 205 27.721 18.730 22.600 1.00 31.75 ATOM 1605 CG ASN A 205 28.517 18.519 21.327 1.00 35.31 ATOM 1606 OD1 ASN A 205 28.511 17.385 20.811 1.00 38.29 ATOM 1607 ND2 ASN A 205 29.186 19.570 20.869 1.00 37.63 ATOM 1608 N ALA A 206 28.450 20.218 25.421 1.00 27.72 ATOM 1609 CA ALA A 206 27.896 20.958 26.568 1.00 27.13 ATOM 1610 C ALA A 206 26.552 21.573 26.301 1.00 26.67 ATOM 1611 O ALA A 206 25.858 21.976 27.257 1.00 27.91 ATOM 1612 CB ALA A 206 28.898 21.960 27.092 1.00 27.16 ATOM 1613 N ASP A 207 26.123 21.657 25.055 1.00 26.81 ATOM 1614 CA ASP A 207 24.828 22.286 24.762 1.00 26.50 ATOM 1615 C ASP A 207 23.681 21.324 24.512 1.00 24.09 ATOM 1616 O ASP A 207 22.626 21.782 24.075 1.00 22.02 ATOM 1617 CB ASP A 207 25.015 23.334 23.667 1.00 30.17 ATOM 1618 CG ASP A 207 25.252 22.760 22.293 1.00 33.03 ATOM 1619 OD1 ASP A 207 26.003 21.794 22.065 1.00 35.15 ATOM 1620 OD2 ASP A 207 24.617 23.347 21.382 1.00 35.71 ATOM 1621 N THR A 208 23.874 20.065 24.834 1.00 22.68 ATOM 1622 CA THR A 208 22.788 19.064 24.652 1.00 21.08 ATOM 1623 C THR A 208 21.660 19.325 25.658 1.00 19.11 ATOM 1624 O THR A 208 21.864 19.329 26.864 1.00 18.04 ATOM 1625 CB THR A 208 23.370 17.593 24.746 1.00 20.07 ATOM 1626 OG1 THR A 208 24.476 17.523 23.799 1.00 18.62 ATOM 1627 CG2 THR A 208 22.325 16.510 24.444 1.00 19.58 ATOM 1628 N ASP A 209 20.478 19.548 25.156 1.00 18.88 ATOM 1629 CA ASP A 209 19.281 19.796 25.961 1.00 18.71 ATOM 1630 C ASP A 209 18.307 18.638 25.779 1.00 17.98 ATOM 1631 O ASP A 209 18.676 17.607 25.207 1.00 18.33 ATOM 1632 CB ASP A 209 18.667 21.152 25.706 1.00 21.00 ATOM 1633 CG ASP A 209 18.243 21.399 24.287 1.00 22.77 ATOM 1634 OD1 ASP A 209 18.153 20.424 23.522 1.00 25.04 ATOM 1635 OD2 ASP A 209 17.987 22.527 23.865 1.00 26.54 ATOM 1636 N TYR A 210 17.092 18.820 26.248 1.00 16.94 ATOM 1637 CA TYR A 210 16.043 17.801 26.188 1.00 15.78 ATOM 1638 C TYR A 210 15.679 17.412 24.758 1.00 15.91 ATOM 1639 O TYR A 210 15.613 16.225 24.448 1.00 14.92 ATOM 1640 CB TYR A 210 14.794 18.181 26.976 1.00 13.93 ATOM 1641 CG TYR A 210 13.799 17.055 27.169 1.00 13.30 ATOM 1642 CD1 TYR A 210 13.891 16.202 28.256 1.00 12.88 ATOM 1643 CD2 TYR A 210 12.761 16.839 26.253 1.00 13.39 ATOM 1644 CE1 TYR A 210 12.964 15.171 28.442 1.00 12.97 ATOM 1645 CE2 TYR A 210 11.856 15.791 26.417 1.00 13.10 ATOM 1646 CZ TYR A 210 11.954 14.962 27.525 1.00 11.84 ATOM 1647 OH TYR A 210 11.100 13.948 27.724 1.00 13.43 ATOM 1648 N SER A 211 15.415 18.411 23.964 1.00 17.20 ATOM 1649 CA SER A 211 15.032 18.279 22.584 1.00 19.75 ATOM 1650 C SER A 211 16.090 17.618 21.707 1.00 20.33 ATOM 1651 O SER A 211 15.731 16.778 20.881 1.00 21.55 ATOM 1652 CB SER A 211 14.673 19.640 21.996 1.00 22.40 ATOM 1653 OG SER A 211 13.444 20.051 22.588 1.00 29.57 ATOM 1654 N ILE A 212 17.312 18.050 21.860 1.00 20.28 ATOM 1655 CA ILE A 212 18.440 17.548 21.092 1.00 20.40 ATOM 1656 C ILE A 212 18.681 16.075 21.393 1.00 20.05 ATOM 1657 O ILE A 212 18.827 15.317 20.411 1.00 20.90 ATOM 1658 CB ILE A 212 19.730 18.404 21.296 1.00 21.44 ATOM 1659 CG1 ILE A 212 19.540 19.787 20.608 1.00 22.27 ATOM 1660 CG2 ILE A 212 21.058 17.725 20.877 1.00 20.55 ATOM 1661 CD1 ILE A 212 20.734 20.763 20.876 1.00 22.87 ATOM 1662 N ALA A 213 18.783 15.675 22.644 1.00 17.66 ATOM 1663 CA ALA A 213 19.040 14.267 22.971 1.00 16.04 ATOM 1664 C ALA A 213 17.917 13.341 22.518 1.00 16.20 ATOM 1665 O ALA A 213 18.148 12.171 22.141 1.00 16.81 ATOM 1666 CB ALA A 213 19.335 14.115 24.441 1.00 14.50 ATOM 1667 N GLU A 214 16.708 13.822 22.628 1.00 15.92 ATOM 1668 CA GLU A 214 15.512 13.113 22.293 1.00 17.90 ATOM 1669 C GLU A 214 15.426 12.826 20.780 1.00 18.84 ATOM 1670 O GLU A 214 15.063 11.718 20.418 1.00 19.35 ATOM 1671 CB GLU A 214 14.208 13.860 22.600 1.00 18.19 ATOM 1672 CG GLU A 214 12.975 12.960 22.647 1.00 20.89 ATOM 1673 CD GLU A 214 11.678 13.721 22.761 1.00 22.89 ATOM 1674 OE1 GLU A 214 11.552 14.859 22.407 1.00 23.94 ATOM 1675 OE2 GLU A 214 10.784 13.050 23.309 1.00 26.56 ATOM 1676 N ALA A 215 15.705 13.814 19.986 1.00 18.47 ATOM 1677 CA ALA A 215 15.662 13.715 18.528 1.00 17.70 ATOM 1678 C ALA A 215 16.776 12.765 18.080 1.00 17.27 ATOM 1679 O ALA A 215 16.514 11.956 17.160 1.00 17.64 ATOM 1680 CB ALA A 215 15.781 15.068 17.883 1.00 17.64 ATOM 1681 N ALA A 216 17.896 12.867 18.721 1.00 15.71 ATOM 1682 CA ALA A 216 19.080 12.067 18.429 1.00 15.25 ATOM 1683 C ALA A 216 18.832 10.596 18.667 1.00 14.88 ATOM 1684 O ALA A 216 19.206 9.745 17.821 1.00 14.32 ATOM 1685 CB ALA A 216 20.312 12.616 19.123 1.00 14.26 ATOM 1686 N PHE A 217 18.236 10.281 19.820 1.00 14.13 ATOM 1687 CA PHE A 217 17.906 8.884 20.120 1.00 13.17 ATOM 1688 C PHE A 217 16.837 8.362 19.144 1.00 13.17 ATOM 1689 O PHE A 217 16.913 7.206 18.678 1.00 14.91 ATOM 1690 CB PHE A 217 17.367 8.714 21.561 1.00 14.03 ATOM 1691 CG PHE A 217 17.271 7.249 21.912 1.00 11.92 ATOM 1692 CD1 PHE A 217 18.396 6.498 22.200 1.00 8.72 ATOM 1693 CD2 PHE A 217 15.995 6.651 21.910 1.00 12.51 ATOM 1694 CE1 PHE A 217 18.304 5.166 22.477 1.00 8.35 ATOM 1695 CE2 PHE A 217 15.887 5.298 22.236 1.00 10.76 ATOM 1696 CZ PHE A 217 17.039 4.572 22.514 1.00 8.61 ATOM 1697 N ASN A 218 15.839 9.148 18.886 1.00 13.25 ATOM 1698 CA ASN A 218 14.719 8.807 18.029 1.00 15.13 ATOM 1699 C ASN A 218 15.074 8.684 16.556 1.00 16.55 ATOM 1700 O ASN A 218 14.333 8.018 15.796 1.00 17.27 ATOM 1701 CB ASN A 218 13.520 9.658 18.358 1.00 16.37 ATOM 1702 CG ASN A 218 12.913 9.433 19.745 1.00 17.31 ATOM 1703 OD1 ASN A 218 11.943 10.149 20.064 1.00 20.49 ATOM 1704 ND2 ASN A 218 13.403 8.564 20.587 1.00 17.07 ATOM 1705 N LYS A 219 16.168 9.254 16.143 1.00 17.40 ATOM 1706 CA LYS A 219 16.693 9.199 14.788 1.00 17.52 ATOM 1707 C LYS A 219 17.741 8.112 14.651 1.00 18.41 ATOM 1708 O LYS A 219 18.372 7.912 13.598 1.00 19.19 ATOM 1709 CB LYS A 219 17.278 10.550 14.337 1.00 17.67 ATOM 1710 CG LYS A 219 16.130 11.496 13.996 1.00 19.09 ATOM 1711 CD LYS A 219 16.530 12.840 13.478 1.00 22.26 ATOM 1712 CE LYS A 219 17.505 13.587 14.331 1.00 23.69 ATOM 1713 NZ LYS A 219 18.330 14.568 13.597 1.00 23.85 ATOM 1714 N GLY A 220 17.941 7.372 15.722 1.00 18.43 ATOM 1715 CA GLY A 220 18.925 6.286 15.770 1.00 18.89 ATOM 1716 C GLY A 220 20.352 6.740 15.642 1.00 19.15 ATOM 1717 O GLY A 220 21.241 5.926 15.340 1.00 18.82 ATOM 1718 N GLU A 221 20.616 8.021 15.897 1.00 18.90 ATOM 1719 CA GLU A 221 21.966 8.582 15.825 1.00 17.37 ATOM 1720 C GLU A 221 22.804 8.282 17.043 1.00 16.08 ATOM 1721 O GLU A 221 24.028 8.184 16.977 1.00 16.54 ATOM 1722 CB GLU A 221 21.971 10.088 15.625 1.00 18.30 ATOM 1723 CG GLU A 221 21.061 10.596 14.512 1.00 22.53 ATOM 1724 CD GLU A 221 20.974 12.099 14.397 1.00 26.02 ATOM 1725 OE1 GLU A 221 21.214 12.892 15.294 1.00 26.16 ATOM 1726 OE2 GLU A 221 20.545 12.404 13.257 1.00 28.51 ATOM 1727 N THR A 222 22.192 8.100 18.200 1.00 14.69 ATOM 1728 CA THR A 222 22.928 7.818 19.430 1.00 12.32 ATOM 1729 C THR A 222 22.439 6.511 20.030 1.00 12.04 ATOM 1730 O THR A 222 21.240 6.231 19.928 1.00 14.34 ATOM 1731 CB THR A 222 22.767 9.091 20.373 1.00 11.24 ATOM 1732 OG1 THR A 222 23.751 8.857 21.432 1.00 12.42 ATOM 1733 CG2 THR A 222 21.366 9.212 20.929 1.00 9.90 ATOM 1734 N ALA A 223 23.288 5.740 20.687 1.00 10.91 ATOM 1735 CA ALA A 223 22.906 4.459 21.225 1.00 11.93 ATOM 1736 C ALA A 223 22.077 4.483 22.518 1.00 12.53 ATOM 1737 O ALA A 223 21.310 3.538 22.732 1.00 12.71 ATOM 1738 CB ALA A 223 24.088 3.532 21.462 1.00 11.93 ATOM 1739 N MET A 224 22.275 5.490 23.325 1.00 11.85 ATOM 1740 CA MET A 224 21.580 5.562 24.626 1.00 10.36 ATOM 1741 C MET A 224 21.110 6.989 24.899 1.00 11.34 ATOM 1742 O MET A 224 21.648 7.944 24.354 1.00 12.37 ATOM 1743 CB MET A 224 22.558 5.137 25.708 1.00 9.53 ATOM 1744 CG MET A 224 23.118 3.792 25.541 1.00 10.70 ATOM 1745 SD MET A 224 24.200 3.254 26.862 1.00 12.87 ATOM 1746 CE MET A 224 25.772 4.003 26.493 1.00 12.23 ATOM 1747 N THR A 225 20.212 7.050 25.856 1.00 10.21 ATOM 1748 CA THR A 225 19.621 8.248 26.416 1.00 9.87 ATOM 1749 C THR A 225 19.186 7.944 27.853 1.00 9.35 ATOM 1750 O THR A 225 19.232 6.827 28.320 1.00 8.84 ATOM 1751 CB THR A 225 18.521 8.872 25.531 1.00 9.68 ATOM 1752 OG1 THR A 225 18.463 10.282 25.915 1.00 10.00 ATOM 1753 CG2 THR A 225 17.119 8.302 25.583 1.00 9.55 ATOM 1754 N ILE A 226 18.952 9.035 28.586 1.00 11.69 ATOM 1755 CA ILE A 226 18.486 8.977 30.000 1.00 9.40 ATOM 1756 C ILE A 226 17.187 9.733 29.999 1.00 8.83 ATOM 1757 O ILE A 226 17.190 10.918 29.609 1.00 8.98 ATOM 1758 CB ILE A 226 19.533 9.474 31.028 1.00 9.39 ATOM 1759 CG1 ILE A 226 20.752 8.564 30.938 1.00 6.44 ATOM 1760 CG2 ILE A 226 18.979 9.415 32.497 1.00 8.90 ATOM 1761 CD1 ILE A 226 21.824 8.907 31.980 1.00 8.46 ATOM 1762 N ASN A 227 16.094 9.018 30.297 1.00 8.04 ATOM 1763 CA ASN A 227 14.789 9.673 30.266 1.00 7.73 ATOM 1764 C ASN A 227 13.821 8.868 31.162 1.00 7.74 ATOM 1765 O ASN A 227 14.220 7.853 31.739 1.00 7.33 ATOM 1766 CB ASN A 227 14.303 9.944 28.839 1.00 10.16 ATOM 1767 CG ASN A 227 13.678 11.311 28.670 1.00 10.87 ATOM 1768 OD1 ASN A 227 13.082 11.852 29.634 1.00 12.34 ATOM 1769 ND2 ASN A 227 13.820 11.904 27.509 1.00 13.11 ATOM 1770 N GLY A 228 12.639 9.403 31.286 1.00 9.23 ATOM 1771 CA GLY A 228 11.612 8.832 32.176 1.00 10.70 ATOM 1772 C GLY A 228 10.467 8.267 31.386 1.00 10.95 ATOM 1773 O GLY A 228 10.465 8.419 30.166 1.00 10.82 ATOM 1774 N PRO A 229 9.487 7.715 32.120 1.00 12.61 ATOM 1775 CA PRO A 229 8.328 7.050 31.518 1.00 12.76 ATOM 1776 C PRO A 229 7.521 7.894 30.618 1.00 13.96 ATOM 1777 O PRO A 229 6.856 7.419 29.660 1.00 16.10 ATOM 1778 CB PRO A 229 7.577 6.417 32.671 1.00 12.55 ATOM 1779 CG PRO A 229 8.596 6.318 33.775 1.00 12.50 ATOM 1780 CD PRO A 229 9.508 7.515 33.571 1.00 11.91 ATOM 1781 N TRP A 230 7.541 9.215 30.841 1.00 14.04 ATOM 1782 CA TRP A 230 6.815 10.115 29.970 1.00 14.05 ATOM 1783 C TRP A 230 7.332 10.136 28.538 1.00 15.33 ATOM 1784 O TRP A 230 6.632 10.654 27.630 1.00 16.54 ATOM 1785 CB TRP A 230 6.857 11.519 30.636 1.00 15.28 ATOM 1786 CG TRP A 230 8.270 12.004 30.762 1.00 13.83 ATOM 1787 CD1 TRP A 230 9.034 12.596 29.787 1.00 12.60 ATOM 1788 CD2 TRP A 230 9.086 11.893 31.934 1.00 13.57 ATOM 1789 NE1 TRP A 230 10.275 12.826 30.281 1.00 15.21 ATOM 1790 CE2 TRP A 230 10.341 12.435 31.600 1.00 13.36 ATOM 1791 CE3 TRP A 230 8.866 11.391 33.219 1.00 11.85 ATOM 1792 CZ2 TRP A 230 11.396 12.498 32.508 1.00 12.12 ATOM 1793 CZ3 TRP A 230 9.927 11.436 34.102 1.00 12.17 ATOM 1794 CH2 TRP A 230 11.165 11.948 33.751 1.00 11.54 ATOM 1795 N ALA A 231 8.539 9.680 28.288 1.00 15.92 ATOM 1796 CA ALA A 231 9.192 9.692 26.990 1.00 16.41 ATOM 1797 C ALA A 231 8.927 8.471 26.105 1.00 15.93 ATOM 1798 O ALA A 231 9.163 8.590 24.878 1.00 17.29 ATOM 1799 CB ALA A 231 10.720 9.784 27.209 1.00 15.63 ATOM 1800 N TRP A 232 8.468 7.402 26.675 1.00 15.86 ATOM 1801 CA TRP A 232 8.183 6.146 26.003 1.00 16.35 ATOM 1802 C TRP A 232 7.286 6.316 24.796 1.00 19.92 ATOM 1803 O TRP A 232 7.722 5.802 23.729 1.00 20.77 ATOM 1804 CB TRP A 232 7.712 5.066 26.935 1.00 12.21 ATOM 1805 CG TRP A 232 8.646 4.819 28.066 1.00 12.42 ATOM 1806 CD1 TRP A 232 9.936 5.215 28.210 1.00 11.43 ATOM 1807 CD2 TRP A 232 8.354 4.071 29.269 1.00 11.92 ATOM 1808 NE1 TRP A 232 10.479 4.740 29.355 1.00 11.22 ATOM 1809 CE2 TRP A 232 9.505 4.080 30.062 1.00 12.03 ATOM 1810 CE3 TRP A 232 7.196 3.419 29.709 1.00 11.83 ATOM 1811 CZ2 TRP A 232 9.585 3.405 31.276 1.00 11.49 ATOM 1812 CZ3 TRP A 232 7.269 2.820 30.934 1.00 11.59 ATOM 1813 CH2 TRP A 232 8.392 2.802 31.702 1.00 11.27 ATOM 1814 N SER A 233 6.167 6.977 24.882 1.00 21.98 ATOM 1815 CA SER A 233 5.257 7.123 23.736 1.00 25.35 ATOM 1816 C SER A 233 5.898 7.696 22.475 1.00 25.94 ATOM 1817 O SER A 233 5.471 7.383 21.331 1.00 25.67 ATOM 1818 CB SER A 233 3.956 7.808 24.112 1.00 26.97 ATOM 1819 OG SER A 233 4.113 8.998 24.865 1.00 30.61 ATOM 1820 N ASN A 234 6.907 8.523 22.619 1.00 26.63 ATOM 1821 CA ASN A 234 7.652 9.187 21.563 1.00 26.39 ATOM 1822 C ASN A 234 8.615 8.217 20.870 1.00 24.58 ATOM 1823 O ASN A 234 8.803 8.408 19.676 1.00 25.08 ATOM 1824 CB ASN A 234 8.398 10.419 22.033 1.00 29.53 ATOM 1825 CG ASN A 234 7.564 11.598 22.444 1.00 32.59 ATOM 1826 OD1 ASN A 234 7.645 12.616 21.754 1.00 33.42 ATOM 1827 ND2 ASN A 234 6.813 11.469 23.562 1.00 35.70 ATOM 1828 N ILE A 235 9.195 7.312 21.605 1.00 23.21 ATOM 1829 CA ILE A 235 10.137 6.322 21.102 1.00 22.44 ATOM 1830 C ILE A 235 9.411 5.263 20.277 1.00 23.95 ATOM 1831 O ILE A 235 9.868 4.879 19.206 1.00 25.14 ATOM 1832 CB ILE A 235 11.022 5.690 22.234 1.00 19.78 ATOM 1833 CG1 ILE A 235 11.614 6.789 23.145 1.00 17.10 ATOM 1834 CG2 ILE A 235 12.134 4.807 21.592 1.00 19.49 ATOM 1835 CD1 ILE A 235 12.193 6.283 24.488 1.00 13.67 ATOM 1836 N ASP A 236 8.266 4.840 20.779 1.00 25.72 ATOM 1837 CA ASP A 236 7.377 3.869 20.149 1.00 26.92 ATOM 1838 C ASP A 236 7.157 4.331 18.696 1.00 28.03 ATOM 1839 O ASP A 236 7.392 3.592 17.744 1.00 29.42 ATOM 1840 CB ASP A 236 6.063 3.752 20.892 1.00 27.04 ATOM 1841 CG ASP A 236 6.170 3.360 22.331 1.00 28.89 ATOM 1842 OD1 ASP A 236 7.031 2.527 22.683 1.00 28.16 ATOM 1843 OD2 ASP A 236 5.362 3.912 23.122 1.00 31.28 ATOM 1844 N THR A 237 6.687 5.541 18.559 1.00 28.38 ATOM 1845 CA THR A 237 6.411 6.221 17.316 1.00 29.75 ATOM 1846 C THR A 237 7.598 6.178 16.344 1.00 31.03 ATOM 1847 O THR A 237 7.459 5.933 15.113 1.00 30.98 ATOM 1848 CB THR A 237 6.007 7.717 17.646 1.00 29.82 ATOM 1849 OG1 THR A 237 4.791 7.604 18.434 1.00 30.27 ATOM 1850 CG2 THR A 237 5.785 8.604 16.435 1.00 31.88 ATOM 1851 N SER A 238 8.752 6.429 16.923 1.00 30.85 ATOM 1852 CA SER A 238 10.030 6.501 16.235 1.00 31.83 ATOM 1853 C SER A 238 10.351 5.195 15.523 1.00 33.02 ATOM 1854 O SER A 238 11.017 5.201 14.464 1.00 34.62 ATOM 1855 CB SER A 238 11.138 6.942 17.184 1.00 31.02 ATOM 1856 OG SER A 238 11.635 5.875 17.978 1.00 30.06 ATOM 1857 N LYS A 239 9.920 4.092 16.082 1.00 33.62 ATOM 1858 CA LYS A 239 10.160 2.755 15.538 1.00 34.33 ATOM 1859 C LYS A 239 11.550 2.215 15.864 1.00 32.93 ATOM 1860 O LYS A 239 12.055 1.279 15.210 1.00 34.29 ATOM 1861 CB LYS A 239 9.881 2.656 14.041 1.00 36.40 ATOM 1862 CG LYS A 239 8.517 2.061 13.710 1.00 39.39 ATOM 1863 CD LYS A 239 7.357 2.952 14.131 1.00 42.31 ATOM 1864 CE LYS A 239 6.052 2.156 14.267 1.00 43.20 ATOM 1865 NZ LYS A 239 6.397 0.820 14.843 1.00 44.09 ATOM 1866 N VAL A 240 12.165 2.776 16.886 1.00 29.31 ATOM 1867 CA VAL A 240 13.474 2.354 17.377 1.00 25.46 ATOM 1868 C VAL A 240 13.171 1.120 18.243 1.00 23.89 ATOM 1869 O VAL A 240 12.137 1.106 18.919 1.00 23.32 ATOM 1870 CB VAL A 240 14.162 3.507 18.150 1.00 24.48 ATOM 1871 CG1 VAL A 240 15.376 3.061 18.934 1.00 22.88 ATOM 1872 CG2 VAL A 240 14.539 4.663 17.253 1.00 23.31 ATOM 1873 N ASN A 241 14.036 0.146 18.177 1.00 22.56 ATOM 1874 CA ASN A 241 13.932 -1.095 18.952 1.00 21.94 ATOM 1875 C ASN A 241 14.757 -0.832 20.235 1.00 19.28 ATOM 1876 O ASN A 241 15.957 -1.084 20.287 1.00 17.76 ATOM 1877 CB ASN A 241 14.336 -2.331 18.183 1.00 24.22 ATOM 1878 CG ASN A 241 14.256 -3.604 18.996 1.00 27.64 ATOM 1879 OD1 ASN A 241 13.258 -3.853 19.713 1.00 29.45 ATOM 1880 ND2 ASN A 241 15.299 -4.437 18.876 1.00 29.26 ATOM 1881 N TYR A 242 13.976 -0.313 21.181 1.00 17.15 ATOM 1882 CA TYR A 242 14.577 0.112 22.474 1.00 14.72 ATOM 1883 C TYR A 242 14.338 -0.767 23.653 1.00 13.92 ATOM 1884 O TYR A 242 13.350 -1.518 23.676 1.00 15.89 ATOM 1885 CB TYR A 242 14.043 1.532 22.726 1.00 13.22 ATOM 1886 CG TYR A 242 12.670 1.708 23.299 1.00 15.26 ATOM 1887 CD1 TYR A 242 11.560 1.798 22.453 1.00 13.25 ATOM 1888 CD2 TYR A 242 12.442 1.809 24.693 1.00 15.09 ATOM 1889 CE1 TYR A 242 10.307 2.011 22.943 1.00 16.85 ATOM 1890 CE2 TYR A 242 11.152 2.010 25.189 1.00 17.03 ATOM 1891 CZ TYR A 242 10.085 2.123 24.318 1.00 18.27 ATOM 1892 OH TYR A 242 8.775 2.312 24.730 1.00 18.74 ATOM 1893 N GLY A 243 15.140 -0.650 24.683 1.00 12.16 ATOM 1894 CA GLY A 243 15.067 -1.352 25.954 1.00 11.08 ATOM 1895 C GLY A 243 15.295 -0.241 27.058 1.00 12.41 ATOM 1896 O GLY A 243 15.897 0.771 26.727 1.00 11.63 ATOM 1897 N VAL A 244 14.766 -0.523 28.203 1.00 12.82 ATOM 1898 CA VAL A 244 14.814 0.311 29.424 1.00 12.02 ATOM 1899 C VAL A 244 15.494 -0.509 30.473 1.00 11.50 ATOM 1900 O VAL A 244 15.071 -1.692 30.681 1.00 13.55 ATOM 1901 CB VAL A 244 13.417 0.809 29.831 1.00 12.66 ATOM 1902 CG1 VAL A 244 13.454 1.768 31.033 1.00 11.92 ATOM 1903 CG2 VAL A 244 12.642 1.436 28.685 1.00 12.52 ATOM 1904 N THR A 245 16.526 0.010 31.118 1.00 10.05 ATOM 1905 CA THR A 245 17.229 -0.813 32.112 1.00 10.13 ATOM 1906 C THR A 245 17.772 0.010 33.282 1.00 10.45 ATOM 1907 O THR A 245 17.605 1.243 33.310 1.00 12.34 ATOM 1908 CB THR A 245 18.348 -1.643 31.371 1.00 9.42 ATOM 1909 OG1 THR A 245 18.934 -2.578 32.301 1.00 12.33 ATOM 1910 CG2 THR A 245 19.501 -0.770 30.803 1.00 9.79 ATOM 1911 N VAL A 246 18.434 -0.633 34.190 1.00 11.00 ATOM 1912 CA VAL A 246 19.053 0.045 35.338 1.00 12.51 ATOM 1913 C VAL A 246 20.150 0.998 34.846 1.00 12.90 ATOM 1914 O VAL A 246 20.911 0.661 33.935 1.00 13.41 ATOM 1915 CB VAL A 246 19.523 -0.963 36.368 1.00 13.64 ATOM 1916 CG1 VAL A 246 20.718 -1.821 35.897 1.00 15.34 ATOM 1917 CG2 VAL A 246 19.922 -0.296 37.691 1.00 13.68 ATOM 1918 N LEU A 247 20.245 2.181 35.455 1.00 12.13 ATOM 1919 CA LEU A 247 21.304 3.148 35.125 1.00 11.52 ATOM 1920 C LEU A 247 22.647 2.519 35.480 1.00 10.55 ATOM 1921 O LEU A 247 22.769 1.665 36.377 1.00 11.18 ATOM 1922 CB LEU A 247 21.074 4.426 35.993 1.00 10.11 ATOM 1923 CG LEU A 247 19.870 5.250 35.626 1.00 11.25 ATOM 1924 CD1 LEU A 247 19.586 6.250 36.756 1.00 10.31 ATOM 1925 CD2 LEU A 247 20.137 5.960 34.305 1.00 9.83 ATOM 1926 N PRO A 248 23.710 3.016 34.851 1.00 11.07 ATOM 1927 CA PRO A 248 25.039 2.501 35.093 1.00 11.70 ATOM 1928 C PRO A 248 25.552 2.881 36.487 1.00 13.03 ATOM 1929 O PRO A 248 25.078 3.879 37.042 1.00 14.00 ATOM 1930 CB PRO A 248 25.893 3.105 33.956 1.00 9.62 ATOM 1931 CG PRO A 248 24.976 3.804 33.032 1.00 10.74 ATOM 1932 CD PRO A 248 23.657 4.049 33.790 1.00 9.70 ATOM 1933 N THR A 249 26.494 2.128 37.010 1.00 13.82 ATOM 1934 CA THR A 249 27.114 2.410 38.294 1.00 13.87 ATOM 1935 C THR A 249 28.288 3.356 38.069 1.00 14.80 ATOM 1936 O THR A 249 28.738 3.517 36.944 1.00 14.70 ATOM 1937 CB THR A 249 27.594 1.132 39.069 1.00 12.52 ATOM 1938 OG1 THR A 249 28.629 0.511 38.237 1.00 13.82 ATOM 1939 CG2 THR A 249 26.476 0.167 39.426 1.00 13.20 ATOM 1940 N PHE A 250 28.719 4.035 39.125 1.00 16.01 ATOM 1941 CA PHE A 250 29.882 4.941 39.056 1.00 16.02 ATOM 1942 C PHE A 250 30.685 4.678 40.350 1.00 17.32 ATOM 1943 O PHE A 250 30.135 4.688 41.456 1.00 17.46 ATOM 1944 CB PHE A 250 29.570 6.360 38.739 1.00 17.09 ATOM 1945 CG PHE A 250 30.732 7.310 38.854 1.00 18.12 ATOM 1946 CD1 PHE A 250 31.731 7.301 37.882 1.00 17.44 ATOM 1947 CD2 PHE A 250 30.833 8.189 39.939 1.00 18.09 ATOM 1948 CE1 PHE A 250 32.802 8.188 37.921 1.00 17.68 ATOM 1949 CE2 PHE A 250 31.923 9.060 40.011 1.00 18.05 ATOM 1950 CZ PHE A 250 32.890 9.073 39.010 1.00 18.43 ATOM 1951 N LYS A 251 31.948 4.335 40.166 1.00 17.71 ATOM 1952 CA LYS A 251 32.837 3.985 41.272 1.00 18.65 ATOM 1953 C LYS A 251 32.244 2.849 42.078 1.00 19.15 ATOM 1954 O LYS A 251 32.438 2.716 43.275 1.00 20.28 ATOM 1955 CB LYS A 251 33.106 5.204 42.162 1.00 19.12 ATOM 1956 CG LYS A 251 33.880 6.214 41.314 1.00 20.14 ATOM 1957 CD LYS A 251 34.232 7.481 42.027 1.00 22.62 ATOM 1958 CE LYS A 251 35.599 7.345 42.667 1.00 23.46 ATOM 1959 NZ LYS A 251 35.521 6.132 43.523 1.00 27.44 ATOM 1960 N GLY A 252 31.537 2.010 41.332 1.00 19.58 ATOM 1961 CA GLY A 252 30.844 0.829 41.796 1.00 18.67 ATOM 1962 C GLY A 252 29.547 1.156 42.530 1.00 18.35 ATOM 1963 O GLY A 252 28.908 0.220 43.058 1.00 19.84 ATOM 1964 N GLN A 253 29.145 2.399 42.552 1.00 16.14 ATOM 1965 CA GLN A 253 27.921 2.814 43.239 1.00 14.94 ATOM 1966 C GLN A 253 26.809 3.072 42.244 1.00 14.00 ATOM 1967 O GLN A 253 27.034 3.663 41.193 1.00 14.58 ATOM 1968 CB GLN A 253 28.219 4.110 44.035 1.00 17.07 ATOM 1969 CG GLN A 253 29.385 3.997 45.001 1.00 16.94 ATOM 1970 CD GLN A 253 29.293 2.860 45.969 1.00 18.13 ATOM 1971 OE1 GLN A 253 28.259 2.435 46.457 1.00 17.36 ATOM 1972 NE2 GLN A 253 30.479 2.309 46.306 1.00 20.54 ATOM 1973 N PRO A 254 25.587 2.719 42.644 1.00 12.80 ATOM 1974 CA PRO A 254 24.431 2.936 41.790 1.00 12.90 ATOM 1975 C PRO A 254 24.205 4.405 41.525 1.00 13.34 ATOM 1976 O PRO A 254 24.520 5.212 42.398 1.00 14.67 ATOM 1977 CB PRO A 254 23.282 2.247 42.499 1.00 12.08 ATOM 1978 CG PRO A 254 23.806 1.674 43.768 1.00 12.35 ATOM 1979 CD PRO A 254 25.255 2.034 43.902 1.00 11.83 ATOM 1980 N SER A 255 23.702 4.761 40.365 1.00 13.30 ATOM 1981 CA SER A 255 23.315 6.135 39.987 1.00 13.32 ATOM 1982 C SER A 255 22.112 6.433 40.919 1.00 14.57 ATOM 1983 O SER A 255 21.415 5.453 41.243 1.00 13.75 ATOM 1984 CB SER A 255 22.855 6.251 38.550 1.00 13.60 ATOM 1985 OG SER A 255 23.937 6.049 37.656 1.00 14.05 ATOM 1986 N LYS A 256 21.940 7.672 41.292 1.00 14.19 ATOM 1987 CA LYS A 256 20.867 8.046 42.226 1.00 14.27 ATOM 1988 C LYS A 256 19.951 9.094 41.654 1.00 12.63 ATOM 1989 O LYS A 256 20.129 10.284 41.929 1.00 13.54 ATOM 1990 CB LYS A 256 21.470 8.668 43.487 1.00 17.17 ATOM 1991 CG LYS A 256 21.349 7.982 44.819 1.00 19.71 ATOM 1992 CD LYS A 256 22.649 7.472 45.371 1.00 23.14 ATOM 1993 CE LYS A 256 23.055 6.132 44.774 1.00 26.75 ATOM 1994 NZ LYS A 256 24.400 5.649 45.230 1.00 25.87 ATOM 1995 N PRO A 257 18.980 8.680 40.866 1.00 11.90 ATOM 1996 CA PRO A 257 18.035 9.603 40.293 1.00 11.40 ATOM 1997 C PRO A 257 17.045 10.018 41.415 1.00 12.47 ATOM 1998 O PRO A 257 16.920 9.249 42.350 1.00 13.26 ATOM 1999 CB PRO A 257 17.343 8.807 39.176 1.00 10.63 ATOM 2000 CG PRO A 257 17.396 7.397 39.701 1.00 11.06 ATOM 2001 CD PRO A 257 18.645 7.277 40.530 1.00 11.20 ATOM 2002 N PHE A 258 16.507 11.182 41.262 1.00 12.82 ATOM 2003 CA PHE A 258 15.487 11.703 42.207 1.00 13.06 ATOM 2004 C PHE A 258 14.236 10.876 41.860 1.00 13.09 ATOM 2005 O PHE A 258 13.988 10.571 40.672 1.00 13.27 ATOM 2006 CB PHE A 258 15.203 13.187 41.984 1.00 12.31 ATOM 2007 CG PHE A 258 16.177 14.165 42.565 1.00 13.41 ATOM 2008 CD1 PHE A 258 16.400 14.194 43.940 1.00 11.61 ATOM 2009 CD2 PHE A 258 16.871 15.040 41.703 1.00 13.41 ATOM 2010 CE1 PHE A 258 17.297 15.095 44.492 1.00 14.30 ATOM 2011 CE2 PHE A 258 17.800 15.946 42.237 1.00 13.74 ATOM 2012 CZ PHE A 258 17.994 15.974 43.635 1.00 13.54 ATOM 2013 N VAL A 259 13.468 10.575 42.874 1.00 14.04 ATOM 2014 CA VAL A 259 12.202 9.790 42.783 1.00 12.16 ATOM 2015 C VAL A 259 11.017 10.731 43.022 1.00 12.28 ATOM 2016 O VAL A 259 11.112 11.497 44.026 1.00 13.39 ATOM 2017 CB VAL A 259 12.268 8.674 43.826 1.00 10.95 ATOM 2018 CG1 VAL A 259 11.057 7.759 43.812 1.00 12.44 ATOM 2019 CG2 VAL A 259 13.537 7.891 43.822 1.00 9.13 ATOM 2020 N GLY A 260 10.046 10.746 42.170 1.00 9.92 ATOM 2021 CA GLY A 260 8.825 11.564 42.326 1.00 10.31 ATOM 2022 C GLY A 260 7.726 10.533 42.663 1.00 10.92 ATOM 2023 O GLY A 260 7.755 9.438 42.097 1.00 10.85 ATOM 2024 N VAL A 261 6.824 10.816 43.573 1.00 10.28 ATOM 2025 CA VAL A 261 5.767 9.873 43.970 1.00 10.83 ATOM 2026 C VAL A 261 4.425 10.532 43.821 1.00 11.05 ATOM 2027 O VAL A 261 4.256 11.583 44.491 1.00 13.20 ATOM 2028 CB VAL A 261 6.022 9.397 45.403 1.00 10.64 ATOM 2029 CG1 VAL A 261 4.888 8.534 45.986 1.00 10.29 ATOM 2030 CG2 VAL A 261 7.325 8.681 45.626 1.00 10.52 ATOM 2031 N LEU A 262 3.536 10.081 42.969 1.00 10.45 ATOM 2032 CA LEU A 262 2.201 10.545 42.750 1.00 9.46 ATOM 2033 C LEU A 262 1.467 10.217 44.098 1.00 8.81 ATOM 2034 O LEU A 262 1.568 9.082 44.548 1.00 9.97 ATOM 2035 CB LEU A 262 1.484 9.942 41.542 1.00 9.45 ATOM 2036 CG LEU A 262 0.046 10.445 41.417 1.00 10.02 ATOM 2037 CD1 LEU A 262 -0.014 11.891 40.964 1.00 10.09 ATOM 2038 CD2 LEU A 262 -0.764 9.566 40.460 1.00 13.30 ATOM 2039 N SER A 263 0.952 11.284 44.695 1.00 8.84 ATOM 2040 CA SER A 263 0.379 11.165 46.041 1.00 8.57 ATOM 2041 C SER A 263 -1.028 11.667 46.137 1.00 7.83 ATOM 2042 O SER A 263 -1.482 12.460 45.338 1.00 8.28 ATOM 2043 CB SER A 263 1.345 11.868 47.033 1.00 7.35 ATOM 2044 OG SER A 263 2.518 11.102 47.170 1.00 10.27 ATOM 2045 N ALA A 264 -1.734 11.110 47.154 1.00 8.47 ATOM 2046 CA ALA A 264 -3.148 11.529 47.350 1.00 8.02 ATOM 2047 C ALA A 264 -3.241 12.084 48.788 1.00 6.82 ATOM 2048 O ALA A 264 -2.906 11.401 49.730 1.00 8.66 ATOM 2049 CB ALA A 264 -4.078 10.357 47.138 1.00 7.51 ATOM 2050 N GLY A 265 -3.656 13.343 48.839 1.00 9.27 ATOM 2051 CA GLY A 265 -3.748 14.000 50.185 1.00 9.53 ATOM 2052 C GLY A 265 -5.178 14.440 50.384 1.00 9.80 ATOM 2053 O GLY A 265 -5.894 14.715 49.453 1.00 10.90 ATOM 2054 N ILE A 266 -5.557 14.523 51.675 1.00 12.08 ATOM 2055 CA ILE A 266 -6.930 14.926 52.086 1.00 10.40 ATOM 2056 C ILE A 266 -6.932 16.377 52.590 1.00 8.46 ATOM 2057 O ILE A 266 -6.086 16.691 53.436 1.00 9.80 ATOM 2058 CB ILE A 266 -7.378 13.958 53.267 1.00 12.05 ATOM 2059 CG1 ILE A 266 -7.417 12.494 52.768 1.00 12.99 ATOM 2060 CG2 ILE A 266 -8.761 14.347 53.859 1.00 12.23 ATOM 2061 CD1 ILE A 266 -7.344 11.420 53.870 1.00 13.90 ATOM 2062 N ASN A 267 -7.804 17.158 52.113 1.00 9.54 ATOM 2063 CA ASN A 267 -7.970 18.584 52.500 1.00 11.59 ATOM 2064 C ASN A 267 -8.280 18.626 54.016 1.00 12.46 ATOM 2065 O ASN A 267 -9.176 17.941 54.493 1.00 11.46 ATOM 2066 CB ASN A 267 -9.001 19.216 51.616 1.00 12.61 ATOM 2067 CG ASN A 267 -9.068 20.718 51.687 1.00 15.49 ATOM 2068 OD1 ASN A 267 -8.686 21.275 52.731 1.00 18.04 ATOM 2069 ND2 ASN A 267 -9.538 21.385 50.659 1.00 16.32 ATOM 2070 N ALA A 268 -7.457 19.372 54.742 1.00 13.70 ATOM 2071 CA ALA A 268 -7.631 19.537 56.195 1.00 13.59 ATOM 2072 C ALA A 268 -9.016 20.127 56.468 1.00 14.79 ATOM 2073 O ALA A 268 -9.531 19.906 57.568 1.00 15.46 ATOM 2074 CB ALA A 268 -6.562 20.506 56.733 1.00 15.28 ATOM 2075 N ALA A 269 -9.567 20.883 55.542 1.00 15.98 ATOM 2076 CA ALA A 269 -10.866 21.508 55.622 1.00 17.18 ATOM 2077 C ALA A 269 -12.018 20.592 55.250 1.00 18.26 ATOM 2078 O ALA A 269 -13.184 20.965 55.457 1.00 19.88 ATOM 2079 CB ALA A 269 -10.989 22.811 54.831 1.00 16.25 ATOM 2080 N SER A 270 -11.764 19.379 54.762 1.00 19.03 ATOM 2081 CA SER A 270 -12.900 18.527 54.404 1.00 18.81 ATOM 2082 C SER A 270 -13.644 17.944 55.605 1.00 17.41 ATOM 2083 O SER A 270 -13.044 17.385 56.531 1.00 17.21 ATOM 2084 CB SER A 270 -12.409 17.334 53.549 1.00 19.08 ATOM 2085 N PRO A 271 -14.952 17.948 55.479 1.00 18.21 ATOM 2086 CA PRO A 271 -15.847 17.323 56.472 1.00 19.41 ATOM 2087 C PRO A 271 -15.990 15.821 56.272 1.00 19.52 ATOM 2088 O PRO A 271 -16.593 15.067 57.038 1.00 20.25 ATOM 2089 CB PRO A 271 -17.205 17.990 56.210 1.00 18.98 ATOM 2090 CG PRO A 271 -17.123 18.715 54.940 1.00 18.49 ATOM 2091 CD PRO A 271 -15.724 18.574 54.395 1.00 17.66 ATOM 2092 N ASN A 272 -15.380 15.315 55.198 1.00 19.99 ATOM 2093 CA ASN A 272 -15.452 13.916 54.772 1.00 17.53 ATOM 2094 C ASN A 272 -14.183 13.134 54.879 1.00 17.15 ATOM 2095 O ASN A 272 -14.004 12.283 53.978 1.00 17.40 ATOM 2096 CB ASN A 272 -15.887 13.950 53.269 1.00 17.28 ATOM 2097 CG ASN A 272 -17.055 14.853 53.057 1.00 17.75 ATOM 2098 OD1 ASN A 272 -18.124 14.603 53.684 1.00 21.09 ATOM 2099 ND2 ASN A 272 -16.989 15.872 52.238 1.00 16.61 ATOM 2100 N LYS A 273 -13.349 13.292 55.861 1.00 15.89 ATOM 2101 CA LYS A 273 -12.101 12.585 55.942 1.00 15.61 ATOM 2102 C LYS A 273 -12.181 11.085 56.086 1.00 14.89 ATOM 2103 O LYS A 273 -11.247 10.367 55.670 1.00 13.04 ATOM 2104 CB LYS A 273 -11.178 13.152 57.017 1.00 16.44 ATOM 2105 CG LYS A 273 -10.878 14.663 56.850 1.00 18.29 ATOM 2106 CD LYS A 273 -10.006 15.042 58.077 1.00 19.08 ATOM 2107 CE LYS A 273 -9.589 16.473 58.065 1.00 20.51 ATOM 2108 NZ LYS A 273 -10.776 17.366 57.924 1.00 22.24 ATOM 2109 N GLU A 274 -13.190 10.594 56.761 1.00 14.68 ATOM 2110 CA GLU A 274 -13.396 9.166 56.989 1.00 15.40 ATOM 2111 C GLU A 274 -13.817 8.554 55.662 1.00 14.46 ATOM 2112 O GLU A 274 -13.277 7.489 55.304 1.00 16.55 ATOM 2113 CB GLU A 274 -14.416 8.899 58.085 1.00 18.96 ATOM 2114 CG GLU A 274 -13.862 8.993 59.519 1.00 25.13 ATOM 2115 CD GLU A 274 -12.783 7.984 59.828 1.00 32.33 ATOM 2116 OE1 GLU A 274 -13.115 6.770 59.564 1.00 35.64 ATOM 2117 OE2 GLU A 274 -11.662 8.263 60.298 1.00 34.56 ATOM 2118 N LEU A 275 -14.644 9.235 54.931 1.00 13.59 ATOM 2119 CA LEU A 275 -15.060 8.765 53.605 1.00 14.16 ATOM 2120 C LEU A 275 -13.831 8.682 52.667 1.00 15.21 ATOM 2121 O LEU A 275 -13.685 7.691 51.932 1.00 14.68 ATOM 2122 CB LEU A 275 -16.153 9.625 53.063 1.00 14.20 ATOM 2123 CG LEU A 275 -17.592 9.421 53.463 1.00 12.87 ATOM 2124 CD1 LEU A 275 -18.442 10.528 52.870 1.00 14.03 ATOM 2125 CD2 LEU A 275 -18.046 8.042 52.989 1.00 13.72 ATOM 2126 N ALA A 276 -13.005 9.704 52.708 1.00 14.79 ATOM 2127 CA ALA A 276 -11.778 9.796 51.891 1.00 13.92 ATOM 2128 C ALA A 276 -10.820 8.676 52.133 1.00 14.41 ATOM 2129 O ALA A 276 -10.279 8.010 51.225 1.00 14.14 ATOM 2130 CB ALA A 276 -11.105 11.171 52.081 1.00 13.30 ATOM 2131 N LYS A 277 -10.549 8.388 53.393 1.00 14.69 ATOM 2132 CA LYS A 277 -9.642 7.342 53.808 1.00 16.42 ATOM 2133 C LYS A 277 -10.166 5.971 53.436 1.00 17.59 ATOM 2134 O LYS A 277 -9.415 5.028 53.157 1.00 18.77 ATOM 2135 CB LYS A 277 -9.307 7.499 55.256 1.00 17.87 ATOM 2136 CG LYS A 277 -9.816 6.496 56.235 1.00 19.84 ATOM 2137 CD LYS A 277 -8.763 5.568 56.694 1.00 20.70 ATOM 2138 CE LYS A 277 -8.834 5.221 58.163 1.00 18.89 ATOM 2139 NZ LYS A 277 -7.496 4.804 58.607 1.00 20.29 ATOM 2140 N GLU A 278 -11.471 5.832 53.431 1.00 18.83 ATOM 2141 CA GLU A 278 -12.086 4.553 53.077 1.00 19.98 ATOM 2142 C GLU A 278 -12.012 4.362 51.566 1.00 19.03 ATOM 2143 O GLU A 278 -11.665 3.251 51.157 1.00 18.64 ATOM 2144 CB GLU A 278 -13.438 4.382 53.707 1.00 23.47 ATOM 2145 CG GLU A 278 -13.380 3.639 55.074 1.00 29.80 ATOM 2146 CD GLU A 278 -12.475 4.004 56.197 1.00 31.85 ATOM 2147 OE1 GLU A 278 -12.504 5.074 56.858 1.00 33.25 ATOM 2148 OE2 GLU A 278 -11.666 3.066 56.472 1.00 30.71 ATOM 2149 N PHE A 279 -12.305 5.384 50.809 1.00 17.34 ATOM 2150 CA PHE A 279 -12.206 5.373 49.355 1.00 17.26 ATOM 2151 C PHE A 279 -10.754 5.031 48.976 1.00 17.36 ATOM 2152 O PHE A 279 -10.454 4.061 48.276 1.00 17.91 ATOM 2153 CB PHE A 279 -12.669 6.682 48.730 1.00 17.16 ATOM 2154 CG PHE A 279 -12.413 6.784 47.257 1.00 19.28 ATOM 2155 CD1 PHE A 279 -13.307 6.247 46.340 1.00 18.39 ATOM 2156 CD2 PHE A 279 -11.231 7.378 46.773 1.00 19.29 ATOM 2157 CE1 PHE A 279 -13.080 6.327 44.979 1.00 17.31 ATOM 2158 CE2 PHE A 279 -10.968 7.442 45.412 1.00 18.78 ATOM 2159 CZ PHE A 279 -11.908 6.932 44.519 1.00 18.26 ATOM 2160 N LEU A 280 -9.814 5.816 49.499 1.00 16.13 ATOM 2161 CA LEU A 280 -8.414 5.624 49.237 1.00 15.36 ATOM 2162 C LEU A 280 -7.892 4.279 49.666 1.00 16.20 ATOM 2163 O LEU A 280 -7.222 3.583 48.874 1.00 15.77 ATOM 2164 CB LEU A 280 -7.616 6.815 49.839 1.00 14.09 ATOM 2165 CG LEU A 280 -7.796 8.180 49.215 1.00 11.92 ATOM 2166 CD1 LEU A 280 -7.073 9.249 50.026 1.00 11.72 ATOM 2167 CD2 LEU A 280 -7.253 8.198 47.787 1.00 11.52 ATOM 2168 N GLU A 281 -8.070 3.872 50.932 1.00 15.88 ATOM 2169 CA GLU A 281 -7.474 2.628 51.354 1.00 16.94 ATOM 2170 C GLU A 281 -8.133 1.351 50.848 1.00 17.58 ATOM 2171 O GLU A 281 -7.416 0.335 50.615 1.00 16.71 ATOM 2172 CB GLU A 281 -7.296 2.527 52.858 1.00 17.10 ATOM 2173 CG GLU A 281 -6.789 3.734 53.621 1.00 18.57 ATOM 2174 CD GLU A 281 -6.481 3.466 55.078 1.00 19.82 ATOM 2175 OE1 GLU A 281 -6.800 2.430 55.648 1.00 20.89 ATOM 2176 OE2 GLU A 281 -5.862 4.395 55.626 1.00 18.79 ATOM 2177 N ASN A 282 -9.423 1.378 50.646 1.00 19.14 ATOM 2178 CA ASN A 282 -10.149 0.143 50.278 1.00 19.67 ATOM 2179 C ASN A 282 -10.717 0.093 48.912 1.00 20.17 ATOM 2180 O ASN A 282 -11.276 -0.974 48.566 1.00 21.65 ATOM 2181 CB ASN A 282 -11.199 -0.148 51.389 1.00 20.76 ATOM 2182 CG ASN A 282 -10.519 -0.346 52.719 1.00 20.63 ATOM 2183 OD1 ASN A 282 -9.558 -1.088 52.887 1.00 21.70 ATOM 2184 ND2 ASN A 282 -11.006 0.377 53.734 1.00 24.21 ATOM 2185 N TYR A 283 -10.639 1.148 48.127 1.00 20.76 ATOM 2186 CA TYR A 283 -11.191 1.104 46.764 1.00 20.53 ATOM 2187 C TYR A 283 -10.076 1.341 45.751 1.00 20.01 ATOM 2188 O TYR A 283 -9.872 0.530 44.841 1.00 19.89 ATOM 2189 CB TYR A 283 -12.325 2.133 46.589 1.00 22.76 ATOM 2190 CG TYR A 283 -13.583 1.616 47.273 1.00 26.36 ATOM 2191 CD1 TYR A 283 -13.603 1.487 48.674 1.00 27.19 ATOM 2192 CD2 TYR A 283 -14.682 1.234 46.523 1.00 26.98 ATOM 2193 CE1 TYR A 283 -14.711 0.962 49.319 1.00 28.54 ATOM 2194 CE2 TYR A 283 -15.816 0.713 47.152 1.00 29.62 ATOM 2195 CZ TYR A 283 -15.814 0.590 48.538 1.00 30.73 ATOM 2196 OH TYR A 283 -16.941 0.078 49.128 1.00 33.63 ATOM 2197 N LEU A 284 -9.398 2.466 45.988 1.00 18.07 ATOM 2198 CA LEU A 284 -8.320 2.872 45.102 1.00 17.43 ATOM 2199 C LEU A 284 -7.060 2.070 45.258 1.00 16.74 ATOM 2200 O LEU A 284 -6.587 1.501 44.236 1.00 18.11 ATOM 2201 CB LEU A 284 -8.181 4.407 45.085 1.00 16.91 ATOM 2202 CG LEU A 284 -6.990 4.823 44.197 1.00 15.79 ATOM 2203 CD1 LEU A 284 -7.421 4.726 42.757 1.00 16.40 ATOM 2204 CD2 LEU A 284 -6.530 6.211 44.580 1.00 15.61 ATOM 2205 N LEU A 285 -6.480 1.934 46.421 1.00 15.30 ATOM 2206 CA LEU A 285 -5.266 1.228 46.662 1.00 13.87 ATOM 2207 C LEU A 285 -5.457 -0.282 46.799 1.00 14.06 ATOM 2208 O LEU A 285 -4.995 -0.869 47.755 1.00 13.53 ATOM 2209 CB LEU A 285 -4.433 1.871 47.778 1.00 15.14 ATOM 2210 CG LEU A 285 -3.798 3.224 47.362 1.00 15.18 ATOM 2211 CD1 LEU A 285 -3.617 4.096 48.570 1.00 15.89 ATOM 2212 CD2 LEU A 285 -2.511 2.882 46.637 1.00 13.93 ATOM 2213 N THR A 286 -6.033 -0.780 45.727 1.00 15.17 ATOM 2214 CA THR A 286 -6.295 -2.221 45.549 1.00 16.23 ATOM 2215 C THR A 286 -5.901 -2.581 44.098 1.00 17.25 ATOM 2216 O THR A 286 -5.905 -1.703 43.235 1.00 17.63 ATOM 2217 CB THR A 286 -7.821 -2.531 45.753 1.00 12.87 ATOM 2218 OG1 THR A 286 -8.521 -1.885 44.654 1.00 15.23 ATOM 2219 CG2 THR A 286 -8.388 -2.003 47.084 1.00 16.42 ATOM 2220 N ASP A 287 -5.694 -3.856 43.863 1.00 19.34 ATOM 2221 CA ASP A 287 -5.349 -4.299 42.478 1.00 21.26 ATOM 2222 C ASP A 287 -6.394 -3.822 41.487 1.00 21.51 ATOM 2223 O ASP A 287 -6.080 -3.409 40.353 1.00 22.59 ATOM 2224 CB ASP A 287 -5.128 -5.799 42.439 1.00 22.60 ATOM 2225 CG ASP A 287 -3.908 -6.291 43.132 1.00 23.50 ATOM 2226 OD1 ASP A 287 -2.980 -5.537 43.409 1.00 25.65 ATOM 2227 OD2 ASP A 287 -3.850 -7.509 43.413 1.00 26.77 ATOM 2228 N GLU A 288 -7.657 -3.879 41.866 1.00 21.60 ATOM 2229 CA GLU A 288 -8.744 -3.485 40.969 1.00 22.44 ATOM 2230 C GLU A 288 -8.855 -1.993 40.777 1.00 20.74 ATOM 2231 O GLU A 288 -9.266 -1.514 39.718 1.00 19.77 ATOM 2232 CB GLU A 288 -10.089 -4.063 41.430 1.00 26.83 ATOM 2233 CG GLU A 288 -10.076 -5.467 42.027 1.00 33.37 ATOM 2234 CD GLU A 288 -10.029 -5.638 43.516 1.00 37.04 ATOM 2235 OE1 GLU A 288 -11.043 -5.703 44.231 1.00 39.18 ATOM 2236 OE2 GLU A 288 -8.863 -5.749 43.974 1.00 37.24 ATOM 2237 N GLY A 289 -8.511 -1.241 41.822 1.00 20.80 ATOM 2238 CA GLY A 289 -8.590 0.238 41.737 1.00 19.14 ATOM 2239 C GLY A 289 -7.456 0.755 40.815 1.00 17.83 ATOM 2240 O GLY A 289 -7.738 1.572 39.953 1.00 17.06 ATOM 2241 N LEU A 290 -6.247 0.310 41.056 1.00 17.52 ATOM 2242 CA LEU A 290 -5.071 0.761 40.258 1.00 17.86 ATOM 2243 C LEU A 290 -5.267 0.333 38.811 1.00 19.83 ATOM 2244 O LEU A 290 -4.923 1.053 37.868 1.00 19.73 ATOM 2245 CB LEU A 290 -3.792 0.293 40.932 1.00 16.15 ATOM 2246 CG LEU A 290 -3.465 0.880 42.316 1.00 15.84 ATOM 2247 CD1 LEU A 290 -2.206 0.294 42.904 1.00 14.48 ATOM 2248 CD2 LEU A 290 -3.318 2.399 42.190 1.00 16.11 ATOM 2249 N GLU A 291 -5.858 -0.847 38.651 1.00 21.59 ATOM 2250 CA GLU A 291 -6.122 -1.400 37.322 1.00 24.23 ATOM 2251 C GLU A 291 -7.093 -0.576 36.514 1.00 24.40 ATOM 2252 O GLU A 291 -6.811 -0.333 35.317 1.00 26.19 ATOM 2253 CB GLU A 291 -6.632 -2.824 37.407 1.00 27.33 ATOM 2254 CG GLU A 291 -7.194 -3.411 36.123 1.00 33.79 ATOM 2255 CD GLU A 291 -6.948 -4.878 35.929 1.00 37.57 ATOM 2256 OE1 GLU A 291 -7.055 -5.548 36.990 1.00 39.76 ATOM 2257 OE2 GLU A 291 -6.647 -5.304 34.819 1.00 40.97 ATOM 2258 N ALA A 292 -8.209 -0.144 37.078 1.00 23.01 ATOM 2259 CA ALA A 292 -9.185 0.694 36.378 1.00 21.51 ATOM 2260 C ALA A 292 -8.543 2.012 35.962 1.00 21.20 ATOM 2261 O ALA A 292 -8.827 2.523 34.861 1.00 22.23 ATOM 2262 CB ALA A 292 -10.403 0.960 37.235 1.00 20.96 ATOM 2263 N VAL A 293 -7.691 2.566 36.831 1.00 20.89 ATOM 2264 CA VAL A 293 -7.021 3.834 36.522 1.00 20.46 ATOM 2265 C VAL A 293 -5.969 3.636 35.392 1.00 20.47 ATOM 2266 O VAL A 293 -5.995 4.403 34.433 1.00 19.67 ATOM 2267 CB VAL A 293 -6.411 4.503 37.758 1.00 20.38 ATOM 2268 CG1 VAL A 293 -5.539 5.678 37.308 1.00 18.59 ATOM 2269 CG2 VAL A 293 -7.444 4.936 38.806 1.00 19.15 ATOM 2270 N ASN A 294 -5.142 2.664 35.598 1.00 21.02 ATOM 2271 CA ASN A 294 -4.060 2.257 34.679 1.00 23.28 ATOM 2272 C ASN A 294 -4.598 1.998 33.277 1.00 24.79 ATOM 2273 O ASN A 294 -3.968 2.422 32.286 1.00 25.95 ATOM 2274 CB ASN A 294 -3.258 1.110 35.279 1.00 22.23 ATOM 2275 CG ASN A 294 -1.922 0.876 34.604 1.00 23.27 ATOM 2276 OD1 ASN A 294 -0.913 1.561 34.815 1.00 22.58 ATOM 2277 ND2 ASN A 294 -1.884 -0.153 33.772 1.00 23.57 ATOM 2278 N LYS A 295 -5.738 1.367 33.165 1.00 26.46 ATOM 2279 CA LYS A 295 -6.422 1.076 31.904 1.00 27.92 ATOM 2280 C LYS A 295 -6.736 2.340 31.127 1.00 28.43 ATOM 2281 O LYS A 295 -6.681 2.384 29.873 1.00 29.46 ATOM 2282 CB LYS A 295 -7.706 0.281 32.135 1.00 29.87 ATOM 2283 CG LYS A 295 -7.554 -1.207 31.876 1.00 33.18 ATOM 2284 CD LYS A 295 -8.545 -2.099 32.540 1.00 37.49 ATOM 2285 CE LYS A 295 -9.821 -1.505 33.065 1.00 40.61 ATOM 2286 NZ LYS A 295 -10.079 -1.995 34.476 1.00 43.43 ATOM 2287 N ASP A 296 -7.039 3.406 31.845 1.00 28.17 ATOM 2288 CA ASP A 296 -7.353 4.711 31.275 1.00 27.63 ATOM 2289 C ASP A 296 -6.066 5.399 30.808 1.00 27.36 ATOM 2290 O ASP A 296 -6.008 5.886 29.669 1.00 27.70 ATOM 2291 CB ASP A 296 -8.199 5.553 32.224 1.00 28.58 ATOM 2292 CG ASP A 296 -8.654 6.848 31.604 1.00 29.92 ATOM 2293 OD1 ASP A 296 -8.756 6.895 30.355 1.00 32.53 ATOM 2294 OD2 ASP A 296 -8.910 7.852 32.273 1.00 31.67 ATOM 2295 N LYS A 297 -5.081 5.446 31.673 1.00 26.82 ATOM 2296 CA LYS A 297 -3.757 6.058 31.431 1.00 25.88 ATOM 2297 C LYS A 297 -2.776 5.353 32.346 1.00 24.82 ATOM 2298 O LYS A 297 -3.013 5.283 33.566 1.00 25.04 ATOM 2299 CB LYS A 297 -3.797 7.515 31.856 1.00 29.35 ATOM 2300 CG LYS A 297 -3.508 8.579 30.837 1.00 33.36 ATOM 2301 CD LYS A 297 -4.757 8.927 30.019 1.00 38.20 ATOM 2302 CE LYS A 297 -5.724 9.821 30.737 1.00 40.38 ATOM 2303 NZ LYS A 297 -7.104 9.832 30.178 1.00 42.45 ATOM 2304 N PRO A 298 -1.692 4.832 31.819 1.00 23.64 ATOM 2305 CA PRO A 298 -0.702 4.105 32.636 1.00 23.56 ATOM 2306 C PRO A 298 -0.142 4.944 33.763 1.00 20.96 ATOM 2307 O PRO A 298 0.143 6.138 33.551 1.00 22.34 ATOM 2308 CB PRO A 298 0.356 3.601 31.640 1.00 22.05 ATOM 2309 CG PRO A 298 0.246 4.648 30.538 1.00 23.79 ATOM 2310 CD PRO A 298 -1.289 4.832 30.399 1.00 24.54 ATOM 2311 N LEU A 299 0.047 4.317 34.897 1.00 19.38 ATOM 2312 CA LEU A 299 0.607 4.967 36.090 1.00 18.86 ATOM 2313 C LEU A 299 2.126 4.854 36.211 1.00 18.42 ATOM 2314 O LEU A 299 2.765 5.577 36.989 1.00 17.48 ATOM 2315 CB LEU A 299 -0.052 4.275 37.304 1.00 17.47 ATOM 2316 CG LEU A 299 -1.498 4.629 37.563 1.00 18.29 ATOM 2317 CD1 LEU A 299 -2.079 3.678 38.621 1.00 16.21 ATOM 2318 CD2 LEU A 299 -1.542 6.069 38.079 1.00 18.30 ATOM 2319 N GLY A 300 2.650 3.865 35.467 1.00 16.79 ATOM 2320 CA GLY A 300 4.076 3.542 35.510 1.00 15.11 ATOM 2321 C GLY A 300 4.194 2.543 36.650 1.00 14.69 ATOM 2322 O GLY A 300 3.285 1.709 36.727 1.00 16.11 ATOM 2323 N ALA A 301 5.224 2.610 37.445 1.00 12.77 ATOM 2324 CA ALA A 301 5.433 1.718 38.560 1.00 13.31 ATOM 2325 C ALA A 301 4.441 2.210 39.664 1.00 13.01 ATOM 2326 O ALA A 301 4.184 3.408 39.694 1.00 13.82 ATOM 2327 CB ALA A 301 6.867 1.726 39.037 1.00 12.96 ATOM 2328 N VAL A 302 3.955 1.310 40.453 1.00 12.65 ATOM 2329 CA VAL A 302 2.971 1.702 41.507 1.00 12.38 ATOM 2330 C VAL A 302 3.532 1.365 42.870 1.00 12.45 ATOM 2331 O VAL A 302 4.430 0.534 42.958 1.00 13.74 ATOM 2332 CB VAL A 302 1.594 1.106 41.212 1.00 11.06 ATOM 2333 CG1 VAL A 302 0.919 1.702 40.023 1.00 8.40 ATOM 2334 CG2 VAL A 302 1.679 -0.420 41.248 1.00 11.78 ATOM 2335 N ALA A 303 2.976 2.028 43.921 1.00 11.78 ATOM 2336 CA ALA A 303 3.468 1.795 45.270 1.00 10.28 ATOM 2337 C ALA A 303 2.943 0.514 45.910 1.00 8.94 ATOM 2338 O ALA A 303 3.636 -0.039 46.773 1.00 8.91 ATOM 2339 CB ALA A 303 3.183 3.068 46.081 1.00 11.49 ATOM 2340 N LEU A 304 1.802 0.050 45.485 1.00 9.94 ATOM 2341 CA LEU A 304 1.160 -1.188 46.000 1.00 9.82 ATOM 2342 C LEU A 304 1.935 -2.416 45.506 1.00 11.25 ATOM 2343 O LEU A 304 1.837 -2.623 44.291 1.00 13.27 ATOM 2344 CB LEU A 304 -0.268 -1.193 45.487 1.00 8.98 ATOM 2345 CG LEU A 304 -1.160 -2.304 46.057 1.00 8.95 ATOM 2346 CD1 LEU A 304 -1.380 -2.105 47.557 1.00 11.14 ATOM 2347 CD2 LEU A 304 -2.459 -2.336 45.282 1.00 8.20 ATOM 2348 N LYS A 305 2.615 -3.113 46.332 1.00 12.00 ATOM 2349 CA LYS A 305 3.426 -4.265 46.034 1.00 14.15 ATOM 2350 C LYS A 305 2.770 -5.329 45.166 1.00 15.89 ATOM 2351 O LYS A 305 3.399 -5.868 44.258 1.00 16.83 ATOM 2352 CB LYS A 305 3.968 -5.000 47.232 1.00 14.13 ATOM 2353 CG LYS A 305 5.004 -4.292 48.085 1.00 17.16 ATOM 2354 CD LYS A 305 4.850 -4.775 49.523 1.00 18.41 ATOM 2355 CE LYS A 305 6.156 -4.867 50.244 1.00 21.63 ATOM 2356 NZ LYS A 305 5.845 -5.235 51.663 1.00 22.97 ATOM 2357 N SER A 306 1.540 -5.650 45.452 1.00 16.87 ATOM 2358 CA SER A 306 0.773 -6.692 44.767 1.00 17.39 ATOM 2359 C SER A 306 0.544 -6.394 43.298 1.00 17.81 ATOM 2360 O SER A 306 0.701 -7.269 42.408 1.00 17.25 ATOM 2361 CB SER A 306 -0.493 -6.966 45.570 1.00 15.61 ATOM 2362 OG SER A 306 -1.459 -5.960 45.393 1.00 17.47 ATOM 2363 N TYR A 307 0.141 -5.162 43.002 1.00 16.77 ATOM 2364 CA TYR A 307 -0.135 -4.769 41.638 1.00 16.79 ATOM 2365 C TYR A 307 1.188 -4.483 40.898 1.00 16.58 ATOM 2366 O TYR A 307 1.257 -4.706 39.692 1.00 17.27 ATOM 2367 CB TYR A 307 -1.129 -3.621 41.516 1.00 15.73 ATOM 2368 CG TYR A 307 -1.645 -3.375 40.120 1.00 16.86 ATOM 2369 CD1 TYR A 307 -2.163 -4.443 39.360 1.00 17.69 ATOM 2370 CD2 TYR A 307 -1.617 -2.116 39.542 1.00 17.22 ATOM 2371 CE1 TYR A 307 -2.660 -4.221 38.087 1.00 18.08 ATOM 2372 CE2 TYR A 307 -2.120 -1.873 38.274 1.00 19.05 ATOM 2373 CZ TYR A 307 -2.624 -2.962 37.541 1.00 18.92 ATOM 2374 OH TYR A 307 -3.114 -2.700 36.305 1.00 21.10 ATOM 2375 N GLU A 308 2.167 -4.023 41.629 1.00 16.87 ATOM 2376 CA GLU A 308 3.453 -3.707 40.993 1.00 18.28 ATOM 2377 C GLU A 308 4.025 -5.014 40.411 1.00 20.86 ATOM 2378 O GLU A 308 4.605 -5.033 39.317 1.00 21.33 ATOM 2379 CB GLU A 308 4.453 -3.131 41.973 1.00 15.12 ATOM 2380 CG GLU A 308 5.845 -2.872 41.473 1.00 13.23 ATOM 2381 CD GLU A 308 6.094 -2.122 40.220 1.00 12.23 ATOM 2382 OE1 GLU A 308 5.144 -1.506 39.762 1.00 12.48 ATOM 2383 OE2 GLU A 308 7.210 -2.139 39.665 1.00 14.79 ATOM 2384 N GLU A 309 3.846 -6.086 41.169 1.00 23.34 ATOM 2385 CA GLU A 309 4.323 -7.412 40.752 1.00 25.28 ATOM 2386 C GLU A 309 3.663 -7.838 39.458 1.00 23.96 ATOM 2387 O GLU A 309 4.337 -8.525 38.666 1.00 24.41 ATOM 2388 CB GLU A 309 4.268 -8.466 41.825 1.00 28.64 ATOM 2389 CG GLU A 309 5.494 -8.546 42.756 1.00 34.63 ATOM 2390 CD GLU A 309 5.297 -9.275 44.046 1.00 39.46 ATOM 2391 OE1 GLU A 309 4.491 -10.233 43.943 1.00 42.21 ATOM 2392 OE2 GLU A 309 5.851 -8.982 45.108 1.00 42.37 ATOM 2393 N GLU A 310 2.464 -7.415 39.178 1.00 23.15 ATOM 2394 CA GLU A 310 1.799 -7.753 37.923 1.00 23.31 ATOM 2395 C GLU A 310 2.373 -6.896 36.800 1.00 21.42 ATOM 2396 O GLU A 310 2.702 -7.315 35.681 1.00 20.02 ATOM 2397 CB GLU A 310 0.291 -7.579 37.980 1.00 27.65 ATOM 2398 CG GLU A 310 -0.507 -7.972 36.744 1.00 36.32 ATOM 2399 CD GLU A 310 -1.973 -7.674 36.644 1.00 41.10 ATOM 2400 OE1 GLU A 310 -2.654 -8.322 37.488 1.00 42.60 ATOM 2401 OE2 GLU A 310 -2.487 -6.900 35.813 1.00 43.11 ATOM 2402 N LEU A 311 2.518 -5.614 37.118 1.00 19.32 ATOM 2403 CA LEU A 311 3.017 -4.609 36.184 1.00 17.23 ATOM 2404 C LEU A 311 4.461 -4.822 35.749 1.00 15.25 ATOM 2405 O LEU A 311 4.834 -4.436 34.626 1.00 14.94 ATOM 2406 CB LEU A 311 2.784 -3.228 36.852 1.00 18.37 ATOM 2407 CG LEU A 311 1.433 -2.584 36.900 1.00 18.05 ATOM 2408 CD1 LEU A 311 1.554 -1.142 37.459 1.00 16.89 ATOM 2409 CD2 LEU A 311 0.811 -2.512 35.525 1.00 17.02 ATOM 2410 N ALA A 312 5.262 -5.319 36.636 1.00 14.32 ATOM 2411 CA ALA A 312 6.667 -5.577 36.465 1.00 14.24 ATOM 2412 C ALA A 312 6.978 -6.632 35.385 1.00 15.09 ATOM 2413 O ALA A 312 8.174 -6.860 35.122 1.00 15.93 ATOM 2414 CB ALA A 312 7.298 -5.886 37.795 1.00 13.86 ATOM 2415 N LYS A 313 6.013 -7.224 34.753 1.00 15.62 ATOM 2416 CA LYS A 313 6.161 -8.173 33.623 1.00 15.61 ATOM 2417 C LYS A 313 6.559 -7.394 32.368 1.00 15.60 ATOM 2418 O LYS A 313 6.910 -7.905 31.296 1.00 16.09 ATOM 2419 CB LYS A 313 4.875 -8.941 33.331 1.00 15.73 ATOM 2420 CG LYS A 313 4.576 -9.921 34.484 1.00 18.36 ATOM 2421 CD LYS A 313 3.321 -10.757 34.123 1.00 20.05 ATOM 2422 CE LYS A 313 3.219 -11.865 35.172 1.00 22.83 ATOM 2423 NZ LYS A 313 1.996 -12.685 35.001 1.00 26.20 ATOM 2424 N ASP A 314 6.414 -6.078 32.453 1.00 14.85 ATOM 2425 CA ASP A 314 6.845 -5.119 31.442 1.00 13.62 ATOM 2426 C ASP A 314 8.235 -4.744 31.981 1.00 14.54 ATOM 2427 O ASP A 314 8.280 -4.206 33.112 1.00 14.79 ATOM 2428 CB ASP A 314 5.900 -3.949 31.343 1.00 14.31 ATOM 2429 CG ASP A 314 6.319 -2.929 30.325 1.00 14.22 ATOM 2430 OD1 ASP A 314 7.505 -2.865 29.968 1.00 15.63 ATOM 2431 OD2 ASP A 314 5.460 -2.196 29.824 1.00 17.39 ATOM 2432 N PRO A 315 9.296 -5.089 31.285 1.00 13.58 ATOM 2433 CA PRO A 315 10.629 -4.811 31.771 1.00 13.06 ATOM 2434 C PRO A 315 10.896 -3.318 31.888 1.00 10.05 ATOM 2435 O PRO A 315 11.790 -2.997 32.704 1.00 12.24 ATOM 2436 CB PRO A 315 11.553 -5.614 30.841 1.00 14.11 ATOM 2437 CG PRO A 315 10.793 -5.594 29.540 1.00 13.96 ATOM 2438 CD PRO A 315 9.331 -5.740 29.965 1.00 14.82 ATOM 2439 N ARG A 316 10.199 -2.480 31.231 1.00 9.18 ATOM 2440 CA ARG A 316 10.373 -0.996 31.334 1.00 9.27 ATOM 2441 C ARG A 316 9.900 -0.516 32.720 1.00 11.04 ATOM 2442 O ARG A 316 10.507 0.376 33.368 1.00 10.27 ATOM 2443 CB ARG A 316 9.560 -0.299 30.272 1.00 8.36 ATOM 2444 CG ARG A 316 9.966 -0.644 28.841 1.00 9.10 ATOM 2445 CD ARG A 316 9.082 0.033 27.882 1.00 10.22 ATOM 2446 NE ARG A 316 7.702 -0.373 27.918 1.00 11.51 ATOM 2447 CZ ARG A 316 6.654 0.126 27.364 1.00 11.88 ATOM 2448 NH1 ARG A 316 6.641 1.198 26.580 1.00 14.42 ATOM 2449 NH2 ARG A 316 5.443 -0.451 27.536 1.00 16.24 ATOM 2450 N ILE A 317 8.812 -1.159 33.146 1.00 11.07 ATOM 2451 CA ILE A 317 8.251 -0.836 34.486 1.00 10.52 ATOM 2452 C ILE A 317 9.127 -1.393 35.576 1.00 10.62 ATOM 2453 O ILE A 317 9.384 -0.685 36.604 1.00 11.02 ATOM 2454 CB ILE A 317 6.739 -1.162 34.585 1.00 10.52 ATOM 2455 CG1 ILE A 317 5.942 -0.170 33.761 1.00 12.18 ATOM 2456 CG2 ILE A 317 6.320 -1.207 36.095 1.00 8.98 ATOM 2457 CD1 ILE A 317 4.492 -0.558 33.381 1.00 16.80 ATOM 2458 N ALA A 318 9.678 -2.588 35.415 1.00 9.51 ATOM 2459 CA ALA A 318 10.551 -3.204 36.371 1.00 9.00 ATOM 2460 C ALA A 318 11.819 -2.350 36.566 1.00 10.36 ATOM 2461 O ALA A 318 12.382 -2.329 37.682 1.00 10.91 ATOM 2462 CB ALA A 318 10.999 -4.612 36.001 1.00 8.79 ATOM 2463 N ALA A 319 12.307 -1.842 35.441 1.00 10.51 ATOM 2464 CA ALA A 319 13.530 -1.039 35.461 1.00 11.00 ATOM 2465 C ALA A 319 13.287 0.297 36.218 1.00 11.27 ATOM 2466 O ALA A 319 14.177 0.665 36.987 1.00 11.44 ATOM 2467 CB ALA A 319 13.947 -0.759 34.021 1.00 10.89 ATOM 2468 N THR A 320 12.180 0.905 35.966 1.00 12.52 ATOM 2469 CA THR A 320 11.718 2.163 36.572 1.00 13.21 ATOM 2470 C THR A 320 11.759 1.972 38.094 1.00 13.30 ATOM 2471 O THR A 320 12.385 2.760 38.813 1.00 12.64 ATOM 2472 CB THR A 320 10.324 2.658 36.080 1.00 13.16 ATOM 2473 OG1 THR A 320 10.385 2.890 34.658 1.00 12.06 ATOM 2474 CG2 THR A 320 9.787 3.944 36.801 1.00 12.92 ATOM 2475 N MET A 321 11.071 0.949 38.563 1.00 12.91 ATOM 2476 CA MET A 321 11.060 0.622 40.007 1.00 11.31 ATOM 2477 C MET A 321 12.415 0.370 40.553 1.00 11.45 ATOM 2478 O MET A 321 12.786 0.830 41.656 1.00 10.75 ATOM 2479 CB MET A 321 10.006 -0.434 40.321 1.00 12.72 ATOM 2480 CG MET A 321 10.078 -0.909 41.746 1.00 13.26 ATOM 2481 SD MET A 321 9.532 0.455 42.833 1.00 17.65 ATOM 2482 CE MET A 321 7.784 0.436 42.590 1.00 12.84 ATOM 2483 N GLU A 322 13.296 -0.374 39.867 1.00 11.40 ATOM 2484 CA GLU A 322 14.635 -0.666 40.312 1.00 12.26 ATOM 2485 C GLU A 322 15.523 0.577 40.532 1.00 10.44 ATOM 2486 O GLU A 322 16.267 0.646 41.506 1.00 10.09 ATOM 2487 CB GLU A 322 15.421 -1.530 39.265 1.00 15.44 ATOM 2488 CG GLU A 322 16.608 -2.214 39.897 1.00 22.41 ATOM 2489 CD GLU A 322 17.376 -3.187 39.076 1.00 27.16 ATOM 2490 OE1 GLU A 322 16.819 -3.426 37.975 1.00 31.40 ATOM 2491 OE2 GLU A 322 18.451 -3.645 39.433 1.00 29.95 ATOM 2492 N ASN A 323 15.416 1.477 39.593 1.00 9.72 ATOM 2493 CA ASN A 323 16.144 2.743 39.578 1.00 9.90 ATOM 2494 C ASN A 323 15.618 3.625 40.770 1.00 9.84 ATOM 2495 O ASN A 323 16.446 4.241 41.399 1.00 9.18 ATOM 2496 CB ASN A 323 16.050 3.450 38.247 1.00 8.18 ATOM 2497 CG ASN A 323 17.101 2.872 37.247 1.00 6.70 ATOM 2498 OD1 ASN A 323 18.232 2.591 37.581 1.00 10.74 ATOM 2499 ND2 ASN A 323 16.607 2.692 36.054 1.00 9.12 ATOM 2500 N ALA A 324 14.326 3.615 40.899 1.00 9.59 ATOM 2501 CA ALA A 324 13.622 4.353 41.954 1.00 11.72 ATOM 2502 C ALA A 324 14.037 3.823 43.314 1.00 12.19 ATOM 2503 O ALA A 324 14.273 4.622 44.229 1.00 13.37 ATOM 2504 CB ALA A 324 12.153 4.431 41.701 1.00 11.56 ATOM 2505 N GLN A 325 14.213 2.544 43.502 1.00 12.59 ATOM 2506 CA GLN A 325 14.627 1.964 44.762 1.00 14.50 ATOM 2507 C GLN A 325 16.045 2.323 45.104 1.00 15.10 ATOM 2508 O GLN A 325 16.442 2.253 46.275 1.00 16.84 ATOM 2509 CB GLN A 325 14.419 0.452 44.892 1.00 16.38 ATOM 2510 CG GLN A 325 12.952 0.074 44.965 1.00 20.18 ATOM 2511 CD GLN A 325 12.713 -1.402 44.867 1.00 24.80 ATOM 2512 OE1 GLN A 325 11.649 -1.836 44.412 1.00 29.73 ATOM 2513 NE2 GLN A 325 13.657 -2.232 45.283 1.00 25.88 ATOM 2514 N LYS A 326 16.856 2.630 44.134 1.00 16.51 ATOM 2515 CA LYS A 326 18.248 3.025 44.297 1.00 16.13 ATOM 2516 C LYS A 326 18.435 4.550 44.316 1.00 14.56 ATOM 2517 O LYS A 326 19.539 4.990 44.661 1.00 15.48 ATOM 2518 CB LYS A 326 19.095 2.429 43.157 1.00 18.50 ATOM 2519 CG LYS A 326 19.399 0.949 43.300 1.00 19.09 ATOM 2520 CD LYS A 326 19.620 0.308 41.920 1.00 22.93 ATOM 2521 CE LYS A 326 19.708 -1.204 42.094 1.00 25.58 ATOM 2522 NZ LYS A 326 20.215 -1.846 40.858 1.00 30.23 ATOM 2523 N GLY A 327 17.474 5.332 43.960 1.00 13.56 ATOM 2524 CA GLY A 327 17.490 6.778 43.865 1.00 12.09 ATOM 2525 C GLY A 327 17.313 7.498 45.200 1.00 12.11 ATOM 2526 O GLY A 327 17.349 6.917 46.271 1.00 13.08 ATOM 2527 N GLU A 328 17.178 8.780 45.119 1.00 12.62 ATOM 2528 CA GLU A 328 17.008 9.744 46.208 1.00 12.63 ATOM 2529 C GLU A 328 15.647 10.350 46.192 1.00 11.11 ATOM 2530 O GLU A 328 15.249 11.051 45.207 1.00 11.61 ATOM 2531 CB GLU A 328 18.078 10.868 46.043 1.00 13.55 ATOM 2532 CG GLU A 328 17.988 11.953 47.151 1.00 15.48 ATOM 2533 CD GLU A 328 19.084 12.949 47.333 1.00 18.39 ATOM 2534 OE1 GLU A 328 19.960 12.955 46.435 1.00 16.83 ATOM 2535 OE2 GLU A 328 19.133 13.728 48.281 1.00 17.93 ATOM 2536 N ILE A 329 14.829 10.100 47.233 1.00 11.59 ATOM 2537 CA ILE A 329 13.483 10.739 47.222 1.00 12.02 ATOM 2538 C ILE A 329 13.698 12.265 47.146 1.00 12.33 ATOM 2539 O ILE A 329 14.534 12.759 47.904 1.00 13.98 ATOM 2540 CB ILE A 329 12.602 10.381 48.437 1.00 13.31 ATOM 2541 CG1 ILE A 329 12.109 8.917 48.377 1.00 14.53 ATOM 2542 CG2 ILE A 329 11.375 11.326 48.590 1.00 12.62 ATOM 2543 CD1 ILE A 329 12.091 8.253 49.794 1.00 17.67 ATOM 2544 N MET A 330 13.018 12.959 46.301 1.00 12.42 ATOM 2545 CA MET A 330 13.182 14.410 46.191 1.00 14.72 ATOM 2546 C MET A 330 12.626 15.083 47.482 1.00 15.57 ATOM 2547 O MET A 330 11.437 14.894 47.753 1.00 14.78 ATOM 2548 CB MET A 330 12.358 14.888 44.997 1.00 15.11 ATOM 2549 CG MET A 330 12.866 16.192 44.452 1.00 17.96 ATOM 2550 SD MET A 330 11.737 16.625 43.101 1.00 27.27 ATOM 2551 CE MET A 330 11.931 15.238 42.005 1.00 20.93 ATOM 2552 N PRO A 331 13.452 15.836 48.175 1.00 16.28 ATOM 2553 CA PRO A 331 13.037 16.584 49.392 1.00 16.35 ATOM 2554 C PRO A 331 11.841 17.458 49.129 1.00 16.07 ATOM 2555 O PRO A 331 11.667 18.125 48.121 1.00 15.60 ATOM 2556 CB PRO A 331 14.300 17.362 49.781 1.00 15.51 ATOM 2557 CG PRO A 331 15.418 16.448 49.273 1.00 16.41 ATOM 2558 CD PRO A 331 14.887 16.075 47.883 1.00 15.66 ATOM 2559 N ASN A 332 10.860 17.425 50.061 1.00 17.52 ATOM 2560 CA ASN A 332 9.617 18.188 49.916 1.00 19.60 ATOM 2561 C ASN A 332 9.600 19.572 50.596 1.00 21.69 ATOM 2562 O ASN A 332 8.551 20.250 50.582 1.00 21.90 ATOM 2563 CB ASN A 332 8.421 17.332 50.337 1.00 19.05 ATOM 2564 CG ASN A 332 8.460 16.936 51.801 1.00 19.14 ATOM 2565 OD1 ASN A 332 9.452 17.186 52.492 1.00 19.49 ATOM 2566 ND2 ASN A 332 7.426 16.249 52.275 1.00 18.42 ATOM 2567 N ILE A 333 10.724 19.968 51.143 1.00 23.54 ATOM 2568 CA ILE A 333 10.950 21.225 51.863 1.00 23.73 ATOM 2569 C ILE A 333 11.223 22.366 50.893 1.00 26.41 ATOM 2570 O ILE A 333 11.666 22.169 49.756 1.00 26.88 ATOM 2571 CB ILE A 333 12.096 21.072 52.891 1.00 22.71 ATOM 2572 CG1 ILE A 333 13.423 20.826 52.124 1.00 20.87 ATOM 2573 CG2 ILE A 333 11.792 19.973 53.960 1.00 22.55 ATOM 2574 CD1 ILE A 333 14.655 20.520 52.983 1.00 22.28 ATOM 2575 N PRO A 334 10.921 23.564 51.411 1.00 28.09 ATOM 2576 CA PRO A 334 11.079 24.813 50.685 1.00 27.09 ATOM 2577 C PRO A 334 12.487 25.152 50.276 1.00 26.07 ATOM 2578 O PRO A 334 12.670 25.767 49.220 1.00 25.78 ATOM 2579 CB PRO A 334 10.439 25.850 51.622 1.00 28.87 ATOM 2580 CG PRO A 334 10.505 25.246 52.989 1.00 29.02 ATOM 2581 CD PRO A 334 10.401 23.751 52.790 1.00 28.33 ATOM 2582 N GLN A 335 13.504 24.798 51.001 1.00 26.10 ATOM 2583 CA GLN A 335 14.902 25.036 50.680 1.00 27.64 ATOM 2584 C GLN A 335 15.357 24.348 49.387 1.00 27.88 ATOM 2585 O GLN A 335 16.495 24.544 48.922 1.00 28.37 ATOM 2586 CB GLN A 335 15.796 24.539 51.827 1.00 30.20 ATOM 2587 CG GLN A 335 15.580 25.211 53.138 1.00 35.26 ATOM 2588 CD GLN A 335 14.533 24.674 54.064 1.00 36.99 ATOM 2589 OE1 GLN A 335 14.416 23.482 54.330 1.00 39.83 ATOM 2590 NE2 GLN A 335 13.774 25.585 54.673 1.00 39.04 ATOM 2591 N MET A 336 14.522 23.482 48.849 1.00 27.07 ATOM 2592 CA MET A 336 14.777 22.722 47.612 1.00 25.43 ATOM 2593 C MET A 336 14.834 23.708 46.457 1.00 25.18 ATOM 2594 O MET A 336 15.507 23.433 45.453 1.00 25.17 ATOM 2595 CB MET A 336 13.741 21.635 47.453 1.00 25.09 ATOM 2596 CG MET A 336 14.017 20.503 46.565 1.00 22.74 ATOM 2597 SD MET A 336 15.603 19.686 46.839 1.00 21.02 ATOM 2598 CE MET A 336 15.740 18.937 45.203 1.00 20.76 ATOM 2599 N SER A 337 14.160 24.842 46.593 1.00 24.45 ATOM 2600 CA SER A 337 14.202 25.835 45.507 1.00 25.72 ATOM 2601 C SER A 337 15.627 26.385 45.362 1.00 24.95 ATOM 2602 O SER A 337 16.102 26.713 44.259 1.00 26.91 ATOM 2603 CB SER A 337 13.237 26.971 45.770 1.00 27.38 ATOM 2604 OG SER A 337 12.071 26.442 46.376 1.00 33.01 ATOM 2605 N ALA A 338 16.308 26.519 46.465 1.00 24.10 ATOM 2606 CA ALA A 338 17.684 27.013 46.480 1.00 22.50 ATOM 2607 C ALA A 338 18.587 26.013 45.757 1.00 21.10 ATOM 2608 O ALA A 338 19.499 26.398 45.022 1.00 19.75 ATOM 2609 CB ALA A 338 18.148 27.204 47.914 1.00 23.74 ATOM 2610 N PHE A 339 18.340 24.748 46.050 1.00 19.37 ATOM 2611 CA PHE A 339 19.104 23.639 45.450 1.00 17.84 ATOM 2612 C PHE A 339 18.950 23.668 43.932 1.00 17.13 ATOM 2613 O PHE A 339 19.970 23.613 43.223 1.00 16.70 ATOM 2614 CB PHE A 339 18.773 22.289 46.085 1.00 17.26 ATOM 2615 CG PHE A 339 19.355 21.052 45.438 1.00 16.13 ATOM 2616 CD1 PHE A 339 18.783 20.531 44.274 1.00 16.92 ATOM 2617 CD2 PHE A 339 20.445 20.412 45.998 1.00 15.34 ATOM 2618 CE1 PHE A 339 19.308 19.402 43.657 1.00 14.62 ATOM 2619 CE2 PHE A 339 20.980 19.278 45.417 1.00 15.91 ATOM 2620 CZ PHE A 339 20.391 18.788 44.258 1.00 14.44 ATOM 2621 N TRP A 340 17.761 23.791 43.407 1.00 17.90 ATOM 2622 CA TRP A 340 17.582 23.779 41.960 1.00 20.03 ATOM 2623 C TRP A 340 18.450 24.815 41.272 1.00 21.91 ATOM 2624 O TRP A 340 19.239 24.493 40.373 1.00 20.60 ATOM 2625 CB TRP A 340 16.143 23.754 41.488 1.00 21.10 ATOM 2626 CG TRP A 340 15.367 22.538 41.862 1.00 22.51 ATOM 2627 CD1 TRP A 340 14.250 22.498 42.647 1.00 23.59 ATOM 2628 CD2 TRP A 340 15.652 21.171 41.518 1.00 23.76 ATOM 2629 NE1 TRP A 340 13.824 21.206 42.807 1.00 24.52 ATOM 2630 CE2 TRP A 340 14.670 20.374 42.128 1.00 23.86 ATOM 2631 CE3 TRP A 340 16.624 20.556 40.738 1.00 24.45 ATOM 2632 CZ2 TRP A 340 14.646 18.989 41.989 1.00 24.36 ATOM 2633 CZ3 TRP A 340 16.598 19.191 40.590 1.00 23.78 ATOM 2634 CH2 TRP A 340 15.629 18.409 41.219 1.00 23.96 ATOM 2635 N TYR A 341 18.256 26.072 41.694 1.00 23.83 ATOM 2636 CA TYR A 341 19.008 27.187 41.075 1.00 24.81 ATOM 2637 C TYR A 341 20.492 27.047 41.285 1.00 21.76 ATOM 2638 O TYR A 341 21.225 27.222 40.295 1.00 21.78 ATOM 2639 CB TYR A 341 18.450 28.588 41.443 1.00 30.63 ATOM 2640 CG TYR A 341 19.407 29.334 42.345 1.00 38.04 ATOM 2641 CD1 TYR A 341 19.385 29.099 43.725 1.00 41.29 ATOM 2642 CD2 TYR A 341 20.402 30.182 41.834 1.00 41.27 ATOM 2643 CE1 TYR A 341 20.293 29.698 44.602 1.00 43.58 ATOM 2644 CE2 TYR A 341 21.309 30.812 42.696 1.00 44.43 ATOM 2645 CZ TYR A 341 21.251 30.565 44.078 1.00 45.41 ATOM 2646 OH TYR A 341 22.122 31.163 44.966 1.00 47.19 ATOM 2647 N ALA A 342 20.965 26.770 42.471 1.00 19.43 ATOM 2648 CA ALA A 342 22.374 26.643 42.755 1.00 19.79 ATOM 2649 C ALA A 342 23.101 25.567 41.949 1.00 20.42 ATOM 2650 O ALA A 342 24.182 25.798 41.365 1.00 20.16 ATOM 2651 CB ALA A 342 22.647 26.443 44.223 1.00 18.12 ATOM 2652 N VAL A 343 22.588 24.364 42.057 1.00 20.75 ATOM 2653 CA VAL A 343 23.160 23.194 41.342 1.00 20.41 ATOM 2654 C VAL A 343 23.007 23.404 39.834 1.00 19.97 ATOM 2655 O VAL A 343 23.914 23.049 39.040 1.00 19.84 ATOM 2656 CB VAL A 343 22.561 21.902 41.946 1.00 20.57 ATOM 2657 CG1 VAL A 343 22.929 20.692 41.067 1.00 20.75 ATOM 2658 CG2 VAL A 343 23.032 21.662 43.376 1.00 18.69 ATOM 2659 N ARG A 344 21.956 24.046 39.388 1.00 20.27 ATOM 2660 CA ARG A 344 21.791 24.300 37.943 1.00 22.58 ATOM 2661 C ARG A 344 22.985 25.102 37.428 1.00 22.64 ATOM 2662 O ARG A 344 23.685 24.786 36.453 1.00 22.17 ATOM 2663 CB ARG A 344 20.455 24.910 37.606 1.00 23.90 ATOM 2664 CG ARG A 344 20.373 25.411 36.166 1.00 28.13 ATOM 2665 CD ARG A 344 19.232 24.897 35.445 1.00 32.95 ATOM 2666 NE ARG A 344 18.003 25.610 35.419 1.00 37.83 ATOM 2667 CZ ARG A 344 16.891 25.375 36.109 1.00 41.52 ATOM 2668 NH1 ARG A 344 16.807 24.412 37.030 1.00 42.62 ATOM 2669 NH2 ARG A 344 15.784 26.120 35.914 1.00 44.05 ATOM 2670 N THR A 345 23.264 26.156 38.189 1.00 23.16 ATOM 2671 CA THR A 345 24.385 27.065 37.912 1.00 22.26 ATOM 2672 C THR A 345 25.700 26.361 38.047 1.00 20.53 ATOM 2673 O THR A 345 26.521 26.476 37.116 1.00 22.20 ATOM 2674 CB THR A 345 24.307 28.380 38.791 1.00 22.83 ATOM 2675 OG1 THR A 345 23.066 29.030 38.371 1.00 23.69 ATOM 2676 CG2 THR A 345 25.498 29.317 38.591 1.00 22.50 ATOM 2677 N ALA A 346 25.968 25.634 39.085 1.00 19.87 ATOM 2678 CA ALA A 346 27.226 24.929 39.264 1.00 19.65 ATOM 2679 C ALA A 346 27.578 24.040 38.076 1.00 21.10 ATOM 2680 O ALA A 346 28.752 23.969 37.670 1.00 21.76 ATOM 2681 CB ALA A 346 27.250 24.100 40.555 1.00 18.82 ATOM 2682 N VAL A 347 26.585 23.339 37.545 1.00 21.80 ATOM 2683 CA VAL A 347 26.855 22.396 36.448 1.00 22.46 ATOM 2684 C VAL A 347 27.133 23.104 35.136 1.00 22.77 ATOM 2685 O VAL A 347 28.075 22.689 34.422 1.00 22.41 ATOM 2686 CB VAL A 347 25.806 21.265 36.379 1.00 22.19 ATOM 2687 CG1 VAL A 347 26.015 20.373 35.149 1.00 21.50 ATOM 2688 CG2 VAL A 347 25.828 20.370 37.611 1.00 21.25 ATOM 2689 N ILE A 348 26.348 24.103 34.809 1.00 23.64 ATOM 2690 CA ILE A 348 26.550 24.832 33.534 1.00 24.52 ATOM 2691 C ILE A 348 27.912 25.527 33.568 1.00 24.40 ATOM 2692 O ILE A 348 28.555 25.620 32.535 1.00 25.73 ATOM 2693 CB ILE A 348 25.388 25.813 33.216 1.00 25.06 ATOM 2694 CG1 ILE A 348 24.091 25.143 32.727 1.00 25.20 ATOM 2695 CG2 ILE A 348 25.832 26.880 32.177 1.00 26.57 ATOM 2696 CD1 ILE A 348 23.896 23.651 33.085 1.00 27.84 ATOM 2697 N ASN A 349 28.340 25.976 34.718 1.00 24.62 ATOM 2698 CA ASN A 349 29.576 26.689 34.942 1.00 23.42 ATOM 2699 C ASN A 349 30.758 25.767 34.823 1.00 23.43 ATOM 2700 O ASN A 349 31.693 26.193 34.139 1.00 23.96 ATOM 2701 CB ASN A 349 29.614 27.498 36.238 1.00 24.50 ATOM 2702 CG ASN A 349 28.824 28.799 36.135 1.00 24.78 ATOM 2703 OD1 ASN A 349 28.183 29.136 35.130 1.00 23.45 ATOM 2704 ND2 ASN A 349 28.831 29.508 37.270 1.00 25.68 ATOM 2705 N ALA A 350 30.707 24.643 35.491 1.00 23.54 ATOM 2706 CA ALA A 350 31.783 23.665 35.434 1.00 24.91 ATOM 2707 C ALA A 350 31.925 23.086 34.023 1.00 26.39 ATOM 2708 O ALA A 350 33.042 22.743 33.617 1.00 27.53 ATOM 2709 CB ALA A 350 31.623 22.536 36.447 1.00 23.50 ATOM 2710 N ALA A 351 30.839 22.938 33.333 1.00 28.87 ATOM 2711 CA ALA A 351 30.709 22.362 32.007 1.00 31.67 ATOM 2712 C ALA A 351 31.255 23.252 30.893 1.00 33.28 ATOM 2713 O ALA A 351 31.778 22.721 29.895 1.00 34.67 ATOM 2714 CB ALA A 351 29.240 22.040 31.660 1.00 31.04 ATOM 2715 N SER A 352 31.050 24.526 31.063 1.00 34.40 ATOM 2716 CA SER A 352 31.481 25.553 30.131 1.00 36.03 ATOM 2717 C SER A 352 32.855 26.094 30.471 1.00 37.23 ATOM 2718 O SER A 352 33.262 27.075 29.818 1.00 39.13 ATOM 2719 CB SER A 352 30.449 26.692 30.095 1.00 37.12 ATOM 2720 OG SER A 352 30.419 27.401 31.322 1.00 37.75 ATOM 2721 N GLY A 353 33.573 25.574 31.438 1.00 37.48 ATOM 2722 CA GLY A 353 34.890 26.009 31.841 1.00 37.54 ATOM 2723 C GLY A 353 34.917 27.302 32.648 1.00 38.10 ATOM 2724 O GLY A 353 35.974 27.678 33.209 1.00 38.07 ATOM 2725 N ARG A 354 33.795 27.972 32.713 1.00 38.98 ATOM 2726 CA ARG A 354 33.611 29.239 33.450 1.00 39.67 ATOM 2727 C ARG A 354 34.072 29.114 34.897 1.00 38.66 ATOM 2728 O ARG A 354 34.449 30.148 35.508 1.00 39.18 ATOM 2729 CB ARG A 354 32.195 29.764 33.314 1.00 42.62 ATOM 2730 CG ARG A 354 31.885 31.234 33.444 1.00 47.62 ATOM 2731 CD ARG A 354 30.705 31.694 32.640 1.00 51.53 ATOM 2732 NE ARG A 354 30.911 31.703 31.197 1.00 56.21 ATOM 2733 CZ ARG A 354 30.154 32.107 30.175 1.00 56.98 ATOM 2734 NH1 ARG A 354 28.920 32.613 30.325 1.00 56.73 ATOM 2735 NH2 ARG A 354 30.602 32.017 28.908 1.00 56.65 ATOM 2736 N GLN A 355 34.101 27.907 35.451 1.00 35.98 ATOM 2737 CA GLN A 355 34.562 27.709 36.851 1.00 33.67 ATOM 2738 C GLN A 355 35.064 26.277 36.960 1.00 32.55 ATOM 2739 O GLN A 355 34.690 25.477 36.088 1.00 33.69 ATOM 2740 CB GLN A 355 33.431 27.964 37.822 1.00 33.47 ATOM 2741 CG GLN A 355 33.728 28.783 39.045 1.00 34.10 ATOM 2742 CD GLN A 355 32.471 29.047 39.842 1.00 35.38 ATOM 2743 OE1 GLN A 355 31.372 29.003 39.271 1.00 37.00 ATOM 2744 NE2 GLN A 355 32.612 29.281 41.146 1.00 35.44 ATOM 2745 N THR A 356 35.886 25.958 37.924 1.00 31.00 ATOM 2746 CA THR A 356 36.388 24.599 38.127 1.00 30.03 ATOM 2747 C THR A 356 35.322 23.831 38.933 1.00 29.61 ATOM 2748 O THR A 356 34.370 24.457 39.436 1.00 29.53 ATOM 2749 CB THR A 356 37.780 24.521 38.838 1.00 30.02 ATOM 2750 OG1 THR A 356 37.577 24.886 40.234 1.00 28.90 ATOM 2751 CG2 THR A 356 38.859 25.380 38.170 1.00 30.64 ATOM 2752 N VAL A 357 35.504 22.532 39.033 1.00 28.81 ATOM 2753 CA VAL A 357 34.573 21.648 39.739 1.00 27.35 ATOM 2754 C VAL A 357 34.544 21.997 41.227 1.00 28.04 ATOM 2755 O VAL A 357 33.483 22.172 41.834 1.00 26.74 ATOM 2756 CB VAL A 357 34.813 20.178 39.377 1.00 24.47 ATOM 2757 CG1 VAL A 357 34.065 19.219 40.288 1.00 21.91 ATOM 2758 CG2 VAL A 357 34.379 19.962 37.921 1.00 23.58 ATOM 2759 N ASP A 358 35.728 22.094 41.765 1.00 30.09 ATOM 2760 CA ASP A 358 35.932 22.455 43.170 1.00 32.42 ATOM 2761 C ASP A 358 35.256 23.797 43.499 1.00 31.97 ATOM 2762 O ASP A 358 34.682 23.914 44.590 1.00 31.98 ATOM 2763 CB ASP A 358 37.435 22.467 43.462 1.00 35.92 ATOM 2764 CG ASP A 358 38.072 21.155 43.061 1.00 40.70 ATOM 2765 OD1 ASP A 358 37.867 20.213 43.859 1.00 43.43 ATOM 2766 OD2 ASP A 358 38.711 21.018 41.994 1.00 44.57 ATOM 2767 N GLU A 359 35.353 24.750 42.618 1.00 31.20 ATOM 2768 CA GLU A 359 34.826 26.097 42.725 1.00 31.07 ATOM 2769 C GLU A 359 33.318 26.144 42.572 1.00 28.90 ATOM 2770 O GLU A 359 32.589 26.728 43.387 1.00 27.68 ATOM 2771 CB GLU A 359 35.366 27.030 41.629 1.00 34.64 ATOM 2772 CG GLU A 359 36.789 27.514 41.598 1.00 40.11 ATOM 2773 CD GLU A 359 37.382 28.173 40.374 1.00 42.50 ATOM 2774 OE1 GLU A 359 36.550 28.622 39.541 1.00 42.59 ATOM 2775 OE2 GLU A 359 38.607 28.288 40.188 1.00 42.58 ATOM 2776 N ALA A 360 32.877 25.567 41.466 1.00 26.69 ATOM 2777 CA ALA A 360 31.455 25.488 41.111 1.00 25.03 ATOM 2778 C ALA A 360 30.618 24.869 42.234 1.00 23.30 ATOM 2779 O ALA A 360 29.540 25.396 42.528 1.00 23.17 ATOM 2780 CB ALA A 360 31.250 24.688 39.819 1.00 23.72 ATOM 2781 N LEU A 361 31.113 23.788 42.822 1.00 22.80 ATOM 2782 CA LEU A 361 30.366 23.109 43.876 1.00 22.41 ATOM 2783 C LEU A 361 30.506 23.817 45.205 1.00 23.41 ATOM 2784 O LEU A 361 29.509 23.822 45.944 1.00 23.56 ATOM 2785 CB LEU A 361 30.636 21.616 43.964 1.00 20.85 ATOM 2786 CG LEU A 361 30.227 20.754 42.758 1.00 19.58 ATOM 2787 CD1 LEU A 361 30.864 19.396 42.913 1.00 18.89 ATOM 2788 CD2 LEU A 361 28.719 20.679 42.635 1.00 16.98 ATOM 2789 N LYS A 362 31.678 24.341 45.473 1.00 24.79 ATOM 2790 CA LYS A 362 31.886 25.077 46.752 1.00 26.64 ATOM 2791 C LYS A 362 30.858 26.205 46.808 1.00 26.64 ATOM 2792 O LYS A 362 30.185 26.340 47.848 1.00 27.30 ATOM 2793 CB LYS A 362 33.297 25.593 46.852 1.00 29.03 ATOM 2794 CG LYS A 362 33.733 26.341 48.099 1.00 32.39 ATOM 2795 CD LYS A 362 34.223 27.747 47.721 1.00 35.21 ATOM 2796 CE LYS A 362 33.060 28.737 47.710 1.00 36.66 ATOM 2797 NZ LYS A 362 33.407 29.912 46.869 1.00 37.14 ATOM 2798 N ASP A 363 30.670 26.953 45.746 1.00 25.98 ATOM 2799 CA ASP A 363 29.737 28.041 45.623 1.00 26.50 ATOM 2800 C ASP A 363 28.280 27.614 45.849 1.00 26.21 ATOM 2801 O ASP A 363 27.530 28.290 46.550 1.00 26.75 ATOM 2802 CB ASP A 363 29.814 28.739 44.267 1.00 29.33 ATOM 2803 CG ASP A 363 30.967 29.698 44.123 1.00 33.10 ATOM 2804 OD1 ASP A 363 31.874 29.677 44.978 1.00 35.62 ATOM 2805 OD2 ASP A 363 30.953 30.454 43.128 1.00 34.54 ATOM 2806 N ALA A 364 27.891 26.570 45.156 1.00 25.29 ATOM 2807 CA ALA A 364 26.522 26.040 45.240 1.00 24.17 ATOM 2808 C ALA A 364 26.222 25.625 46.675 1.00 23.18 ATOM 2809 O ALA A 364 25.158 25.967 47.173 1.00 21.49 ATOM 2810 CB ALA A 364 26.346 24.908 44.240 1.00 24.44 ATOM 2811 N GLN A 365 27.135 24.918 47.290 1.00 24.21 ATOM 2812 CA GLN A 365 27.014 24.475 48.683 1.00 26.18 ATOM 2813 C GLN A 365 26.720 25.712 49.559 1.00 27.66 ATOM 2814 O GLN A 365 25.850 25.711 50.430 1.00 28.07 ATOM 2815 CB GLN A 365 28.240 23.761 49.224 1.00 27.09 ATOM 2816 CG GLN A 365 28.193 23.317 50.663 1.00 27.84 ATOM 2817 CD GLN A 365 27.507 22.007 50.951 1.00 28.82 ATOM 2818 OE1 GLN A 365 27.416 21.106 50.120 1.00 27.93 ATOM 2819 NE2 GLN A 365 27.004 21.867 52.190 1.00 28.93 ATOM 2820 N THR A 366 27.484 26.751 49.305 1.00 28.28 ATOM 2821 CA THR A 366 27.378 28.034 49.990 1.00 29.21 ATOM 2822 C THR A 366 26.004 28.644 49.842 1.00 29.72 ATOM 2823 O THR A 366 25.438 29.001 50.890 1.00 30.59 ATOM 2824 CB THR A 366 28.551 28.982 49.530 1.00 29.08 ATOM 2825 OG1 THR A 366 29.709 28.452 50.245 1.00 31.00 ATOM 2826 CG2 THR A 366 28.323 30.451 49.757 1.00 30.59 ATOM 2827 N ARG A 367 25.452 28.763 48.665 1.00 30.18 ATOM 2828 CA ARG A 367 24.144 29.342 48.445 1.00 32.31 ATOM 2829 C ARG A 367 22.970 28.560 49.004 1.00 33.57 ATOM 2830 O ARG A 367 21.875 29.168 49.124 1.00 34.04 ATOM 2831 CB ARG A 367 23.904 29.520 46.929 1.00 34.56 ATOM 2832 CG ARG A 367 24.939 30.433 46.300 1.00 39.11 ATOM 2833 CD ARG A 367 24.882 30.434 44.819 1.00 43.21 ATOM 2834 NE ARG A 367 26.213 30.447 44.224 1.00 48.22 ATOM 2835 CZ ARG A 367 26.782 31.468 43.583 1.00 49.51 ATOM 2836 NH1 ARG A 367 26.121 32.612 43.412 1.00 49.79 ATOM 2837 NH2 ARG A 367 28.026 31.345 43.092 1.00 50.57 ATOM 2838 N ILE A 368 23.146 27.260 49.259 1.00 33.93 ATOM 2839 CA ILE A 368 22.087 26.383 49.756 1.00 33.32 ATOM 2840 C ILE A 368 21.963 26.480 51.292 1.00 34.06 ATOM 2841 O ILE A 368 20.846 26.516 51.810 1.00 33.94 ATOM 2842 CB ILE A 368 22.232 24.863 49.375 1.00 31.69 ATOM 2843 CG1 ILE A 368 22.510 24.607 47.879 1.00 29.79 ATOM 2844 CG2 ILE A 368 20.981 24.041 49.821 1.00 29.88 ATOM 2845 CD1 ILE A 368 21.507 25.316 46.962 1.00 29.73 ATOM 2846 N THR A 369 23.100 26.434 51.939 1.00 34.81 ATOM 2847 CA THR A 369 23.238 26.478 53.389 1.00 36.71 ATOM 2848 C THR A 369 23.331 27.926 53.900 1.00 39.41 ATOM 2849 O THR A 369 23.637 28.118 55.084 1.00 40.66 ATOM 2850 CB THR A 369 24.496 25.654 53.869 1.00 34.83 ATOM 2851 OG1 THR A 369 25.637 26.332 53.254 1.00 32.76 ATOM 2852 CG2 THR A 369 24.475 24.170 53.525 1.00 34.14 ATOM 2853 N LYS A 370 23.128 28.870 53.013 1.00 42.01 ATOM 2854 CA LYS A 370 23.141 30.325 53.240 1.00 44.26 ATOM 2855 C LYS A 370 21.843 30.688 53.979 1.00 46.19 ATOM 2857 CB LYS A 370 23.182 31.093 51.932 1.00 43.89 ATOM 2858 CG LYS A 370 23.436 32.581 51.905 1.00 44.72 ATOM 2859 CD LYS A 370 24.906 32.927 52.118 1.00 47.02 ATOM 2860 CE LYS A 370 25.210 34.328 52.582 1.00 46.79 ATOM 2861 NZ LYS A 370 24.794 34.569 53.990 1.00 46.84 TER If you find results from this site helpful for your research, please cite one of our papers:
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