ATOM 1 N ALA A 1 15.594 -3.052 50.617 1.00 30.16 ATOM 2 CA ALA A 1 16.100 -1.758 50.076 1.00 30.13 ATOM 3 C ALA A 1 15.034 -0.677 50.183 1.00 28.41 ATOM 4 O ALA A 1 13.851 -0.931 49.956 1.00 30.18 ATOM 5 CB ALA A 1 16.519 -1.931 48.621 1.00 30.23 ATOM 6 N PRO A 2 15.439 0.551 50.540 1.00 26.83 ATOM 7 CA PRO A 2 14.473 1.645 50.662 1.00 24.55 ATOM 8 C PRO A 2 13.865 1.992 49.304 1.00 23.02 ATOM 9 O PRO A 2 14.561 1.986 48.289 1.00 23.13 ATOM 10 CB PRO A 2 15.317 2.795 51.216 1.00 26.29 ATOM 11 CG PRO A 2 16.429 2.094 51.942 1.00 25.97 ATOM 12 CD PRO A 2 16.772 0.976 50.997 1.00 26.19 ATOM 13 N ARG A 3 12.566 2.272 49.286 1.00 21.20 ATOM 14 CA ARG A 3 11.889 2.660 48.052 1.00 19.95 ATOM 15 C ARG A 3 11.787 4.174 48.121 1.00 17.46 ATOM 16 O ARG A 3 11.094 4.719 48.981 1.00 18.32 ATOM 17 CB ARG A 3 10.487 2.055 47.977 1.00 20.90 ATOM 18 CG ARG A 3 10.456 0.544 47.830 1.00 21.72 ATOM 19 CD ARG A 3 9.023 0.035 47.866 1.00 23.53 ATOM 20 NE ARG A 3 8.940 -1.419 47.748 1.00 25.18 ATOM 21 CZ ARG A 3 9.254 -2.104 46.652 1.00 26.73 ATOM 22 NH1 ARG A 3 9.678 -1.471 45.566 1.00 25.73 ATOM 23 NH2 ARG A 3 9.135 -3.425 46.643 1.00 27.77 ATOM 24 N ILE A 4 12.483 4.850 47.218 1.00 16.08 ATOM 25 CA ILE A 4 12.491 6.304 47.207 1.00 15.52 ATOM 26 C ILE A 4 11.607 6.890 46.120 1.00 14.84 ATOM 27 O ILE A 4 11.471 6.323 45.037 1.00 14.91 ATOM 28 CB ILE A 4 13.931 6.831 47.011 1.00 16.15 ATOM 29 CG1 ILE A 4 14.832 6.295 48.126 1.00 18.88 ATOM 30 CG2 ILE A 4 13.947 8.357 47.005 1.00 17.05 ATOM 31 CD ILE A 4 14.375 6.678 49.525 1.00 23.80 ATOM 32 N LYS A 5 10.999 8.028 46.429 1.00 15.07 ATOM 33 CA LYS A 5 10.151 8.733 45.483 1.00 15.65 ATOM 34 C LYS A 5 11.014 9.836 44.878 1.00 14.47 ATOM 35 O LYS A 5 11.575 10.658 45.605 1.00 15.68 ATOM 36 CB LYS A 5 8.950 9.340 46.212 1.00 17.78 ATOM 37 CG LYS A 5 8.028 8.306 46.848 1.00 21.26 ATOM 38 CD LYS A 5 7.298 8.877 48.057 1.00 25.97 ATOM 39 CE LYS A 5 8.273 9.134 49.203 1.00 28.57 ATOM 40 NZ LYS A 5 7.618 9.699 50.416 1.00 30.72 ATOM 41 N LEU A 6 11.150 9.834 43.556 1.00 12.32 ATOM 42 CA LEU A 6 11.950 10.851 42.882 1.00 14.36 ATOM 43 C LEU A 6 11.083 11.707 41.977 1.00 12.84 ATOM 44 O LEU A 6 10.316 11.195 41.161 1.00 16.68 ATOM 45 CB LEU A 6 13.075 10.214 42.060 1.00 16.51 ATOM 46 CG LEU A 6 14.135 9.439 42.847 1.00 18.28 ATOM 47 CD1 LEU A 6 13.678 7.999 43.034 1.00 24.44 ATOM 48 CD2 LEU A 6 15.458 9.479 42.092 1.00 21.09 ATOM 49 N LYS A 7 11.222 13.019 42.114 1.00 9.34 ATOM 50 CA LYS A 7 10.439 13.958 41.326 1.00 8.01 ATOM 51 C LYS A 7 11.331 14.686 40.334 1.00 9.07 ATOM 52 O LYS A 7 12.285 15.361 40.717 1.00 7.55 ATOM 53 CB LYS A 7 9.769 14.964 42.262 1.00 10.98 ATOM 54 CG LYS A 7 8.926 16.013 41.575 1.00 14.23 ATOM 55 CD LYS A 7 8.367 17.000 42.585 1.00 18.22 ATOM 56 CE LYS A 7 7.476 18.028 41.906 1.00 21.96 ATOM 57 NZ LYS A 7 6.929 19.015 42.879 1.00 23.57 ATOM 58 N ILE A 8 11.016 14.558 39.052 1.00 7.90 ATOM 59 CA ILE A 8 11.824 15.217 38.045 1.00 9.25 ATOM 60 C ILE A 8 11.558 16.718 38.060 1.00 10.75 ATOM 61 O ILE A 8 10.457 17.163 38.398 1.00 11.16 ATOM 62 CB ILE A 8 11.519 14.637 36.636 1.00 8.85 ATOM 63 CG1 ILE A 8 12.643 14.998 35.664 1.00 12.54 ATOM 64 CG2 ILE A 8 10.195 15.191 36.113 1.00 11.06 ATOM 65 CD ILE A 8 12.539 14.296 34.326 1.00 16.79 ATOM 66 N LEU A 9 12.588 17.496 37.743 1.00 10.01 ATOM 67 CA LEU A 9 12.452 18.944 37.654 1.00 11.82 ATOM 68 C LEU A 9 12.457 19.304 36.176 1.00 11.57 ATOM 69 O LEU A 9 13.063 18.608 35.356 1.00 13.14 ATOM 70 CB LEU A 9 13.615 19.674 38.349 1.00 13.74 ATOM 71 CG LEU A 9 13.657 19.765 39.875 1.00 16.01 ATOM 72 CD1 LEU A 9 13.844 18.379 40.478 1.00 21.51 ATOM 73 CD2 LEU A 9 14.809 20.676 40.286 1.00 17.26 ATOM 74 N ASN A 10 11.772 20.393 35.850 1.00 14.61 ATOM 75 CA ASN A 10 11.710 20.880 34.484 1.00 17.36 ATOM 76 C ASN A 10 13.018 21.596 34.161 1.00 16.28 ATOM 77 O ASN A 10 13.712 22.058 35.071 1.00 17.41 ATOM 78 CB ASN A 10 10.547 21.868 34.318 1.00 22.22 ATOM 79 CG ASN A 10 10.419 22.369 32.899 1.00 23.95 ATOM 80 OD1 ASN A 10 10.278 21.576 31.971 1.00 27.64 ATOM 81 ND2 ASN A 10 10.482 23.682 32.717 1.00 29.43 ATOM 82 N GLY A 11 13.364 21.666 32.877 1.00 16.71 ATOM 83 CA GLY A 11 14.566 22.379 32.478 1.00 16.23 ATOM 84 C GLY A 11 15.834 21.578 32.263 1.00 16.67 ATOM 85 O GLY A 11 16.003 20.468 32.773 1.00 15.88 ATOM 86 N SER A 12 16.739 22.169 31.493 1.00 15.00 ATOM 87 CA SER A 12 18.018 21.563 31.186 1.00 15.27 ATOM 88 C SER A 12 19.064 22.228 32.072 1.00 13.06 ATOM 89 O SER A 12 19.140 23.457 32.143 1.00 14.70 ATOM 90 CB SER A 12 18.346 21.771 29.705 1.00 14.62 ATOM 91 OG SER A 12 19.608 21.224 29.390 1.00 24.74 ATOM 92 N TYR A 13 19.854 21.409 32.757 1.00 10.78 ATOM 93 CA TYR A 13 20.889 21.916 33.646 1.00 9.87 ATOM 94 C TYR A 13 22.310 21.726 33.136 1.00 9.59 ATOM 95 O TYR A 13 22.578 20.904 32.258 1.00 10.58 ATOM 96 CB TYR A 13 20.764 21.267 35.028 1.00 9.33 ATOM 97 CG TYR A 13 19.592 21.784 35.816 1.00 7.62 ATOM 98 CD1 TYR A 13 18.305 21.295 35.594 1.00 9.21 ATOM 99 CD2 TYR A 13 19.753 22.826 36.725 1.00 10.36 ATOM 100 CE1 TYR A 13 17.208 21.842 36.255 1.00 10.10 ATOM 101 CE2 TYR A 13 18.665 23.376 37.387 1.00 9.53 ATOM 102 CZ TYR A 13 17.397 22.883 37.145 1.00 11.82 ATOM 103 OH TYR A 13 16.322 23.457 37.774 1.00 12.07 ATOM 104 N GLY A 14 23.224 22.510 33.697 1.00 10.08 ATOM 105 CA GLY A 14 24.618 22.410 33.316 1.00 10.16 ATOM 106 C GLY A 14 25.479 22.605 34.545 1.00 8.40 ATOM 107 O GLY A 14 25.025 23.192 35.528 1.00 8.25 ATOM 108 N ILE A 15 26.709 22.100 34.496 1.00 8.95 ATOM 109 CA ILE A 15 27.652 22.234 35.603 1.00 9.58 ATOM 110 C ILE A 15 28.768 23.159 35.130 1.00 9.19 ATOM 111 O ILE A 15 29.595 22.769 34.300 1.00 9.98 ATOM 112 CB ILE A 15 28.300 20.889 35.973 1.00 10.40 ATOM 113 CG1 ILE A 15 27.249 19.775 36.002 1.00 15.37 ATOM 114 CG2 ILE A 15 28.999 21.017 37.315 1.00 13.47 ATOM 115 CD ILE A 15 26.164 19.966 37.004 1.00 18.63 ATOM 116 N ALA A 16 28.787 24.380 35.647 1.00 7.84 ATOM 117 CA ALA A 16 29.814 25.327 35.244 1.00 9.73 ATOM 118 C ALA A 16 31.027 25.314 36.152 1.00 10.62 ATOM 119 O ALA A 16 30.922 25.037 37.345 1.00 9.39 ATOM 120 CB ALA A 16 29.235 26.734 35.178 1.00 10.44 ATOM 121 N ARG A 17 32.197 25.589 35.584 1.00 10.28 ATOM 122 CA ARG A 17 33.391 25.646 36.407 1.00 11.77 ATOM 123 C ARG A 17 34.020 27.027 36.300 1.00 11.62 ATOM 124 O ARG A 17 34.383 27.473 35.212 1.00 12.33 ATOM 125 CB ARG A 17 34.429 24.584 36.034 1.00 14.25 ATOM 126 CG ARG A 17 35.509 24.534 37.112 1.00 20.28 ATOM 127 CD ARG A 17 36.809 23.840 36.775 1.00 24.25 ATOM 128 NE ARG A 17 37.725 24.027 37.902 1.00 28.16 ATOM 129 CZ ARG A 17 38.957 23.531 37.981 1.00 30.76 ATOM 130 NH1 ARG A 17 39.451 22.800 36.991 1.00 32.32 ATOM 131 NH2 ARG A 17 39.695 23.764 39.060 1.00 32.03 ATOM 132 N LEU A 18 34.137 27.693 37.446 1.00 10.41 ATOM 133 CA LEU A 18 34.719 29.032 37.535 1.00 13.60 ATOM 134 C LEU A 18 35.974 28.987 38.387 1.00 13.35 ATOM 135 O LEU A 18 36.262 27.967 39.012 1.00 15.89 ATOM 136 CB LEU A 18 33.734 30.009 38.182 1.00 12.67 ATOM 137 CG LEU A 18 32.620 30.540 37.282 1.00 15.19 ATOM 138 CD1 LEU A 18 31.718 29.373 36.973 1.00 16.77 ATOM 139 CD2 LEU A 18 31.823 31.682 37.937 1.00 15.31 ATOM 140 N SER A 19 36.700 30.104 38.420 1.00 14.00 ATOM 141 CA SER A 19 37.926 30.228 39.204 1.00 15.81 ATOM 142 C SER A 19 37.645 30.093 40.700 1.00 14.25 ATOM 143 O SER A 19 36.675 30.650 41.219 1.00 12.90 ATOM 144 CB SER A 19 38.596 31.585 38.922 1.00 18.04 ATOM 145 OG SER A 19 39.777 31.753 39.692 1.00 26.13 ATOM 146 N ALA A 20 38.514 29.368 41.393 1.00 14.13 ATOM 147 CA ALA A 20 38.367 29.153 42.826 1.00 14.43 ATOM 148 C ALA A 20 38.182 30.431 43.645 1.00 14.63 ATOM 149 O ALA A 20 37.533 30.406 44.688 1.00 16.37 ATOM 150 CB ALA A 20 39.564 28.370 43.358 1.00 16.26 ATOM 151 N SER A 21 38.739 31.548 43.185 1.00 15.22 ATOM 152 CA SER A 21 38.622 32.796 43.937 1.00 15.52 ATOM 153 C SER A 21 37.637 33.812 43.383 1.00 14.56 ATOM 154 O SER A 21 37.452 34.882 43.961 1.00 15.44 ATOM 155 CB SER A 21 39.991 33.455 44.075 1.00 16.75 ATOM 156 OG SER A 21 40.783 32.747 45.007 1.00 21.59 ATOM 157 N GLU A 22 36.996 33.469 42.275 1.00 13.33 ATOM 158 CA GLU A 22 36.043 34.359 41.633 1.00 13.07 ATOM 159 C GLU A 22 34.797 34.583 42.486 1.00 12.58 ATOM 160 O GLU A 22 34.361 33.689 43.207 1.00 13.55 ATOM 161 CB GLU A 22 35.644 33.767 40.282 1.00 17.81 ATOM 162 CG GLU A 22 34.897 34.712 39.377 1.00 21.95 ATOM 163 CD GLU A 22 34.638 34.105 38.012 1.00 19.14 ATOM 164 OE1 GLU A 22 35.256 33.061 37.690 1.00 20.37 ATOM 165 OE2 GLU A 22 33.828 34.682 37.262 1.00 22.99 ATOM 166 N ALA A 23 34.225 35.779 42.406 1.00 12.21 ATOM 167 CA ALA A 23 33.015 36.069 43.167 1.00 11.20 ATOM 168 C ALA A 23 31.875 35.276 42.539 1.00 11.84 ATOM 169 O ALA A 23 31.956 34.876 41.375 1.00 12.38 ATOM 170 CB ALA A 23 32.704 37.561 43.118 1.00 13.75 ATOM 171 N ILE A 24 30.824 35.027 43.309 1.00 11.79 ATOM 172 CA ILE A 24 29.680 34.304 42.773 1.00 11.44 ATOM 173 C ILE A 24 29.082 35.205 41.697 1.00 12.04 ATOM 174 O ILE A 24 28.748 36.360 41.965 1.00 12.64 ATOM 175 CB ILE A 24 28.625 34.033 43.868 1.00 10.72 ATOM 176 CG1 ILE A 24 29.228 33.147 44.961 1.00 12.75 ATOM 177 CG2 ILE A 24 27.391 33.372 43.249 1.00 9.58 ATOM 178 CD ILE A 24 28.281 32.847 46.121 1.00 12.61 ATOM 179 N PRO A 25 28.951 34.694 40.462 1.00 13.14 ATOM 180 CA PRO A 25 28.391 35.491 39.369 1.00 12.70 ATOM 181 C PRO A 25 26.917 35.818 39.568 1.00 12.39 ATOM 182 O PRO A 25 26.190 35.086 40.246 1.00 13.07 ATOM 183 CB PRO A 25 28.636 34.612 38.145 1.00 13.55 ATOM 184 CG PRO A 25 28.491 33.231 38.712 1.00 15.49 ATOM 185 CD PRO A 25 29.289 33.336 39.997 1.00 12.39 ATOM 186 N ALA A 26 26.488 36.925 38.968 1.00 13.26 ATOM 187 CA ALA A 26 25.109 37.377 39.074 1.00 14.63 ATOM 188 C ALA A 26 24.130 36.412 38.421 1.00 14.17 ATOM 189 O ALA A 26 22.952 36.395 38.765 1.00 14.82 ATOM 190 CB ALA A 26 24.968 38.757 38.446 1.00 16.79 ATOM 191 N TRP A 27 24.617 35.611 37.479 1.00 12.38 ATOM 192 CA TRP A 27 23.755 34.666 36.780 1.00 12.42 ATOM 193 C TRP A 27 23.559 33.337 37.500 1.00 12.12 ATOM 194 O TRP A 27 22.734 32.527 37.085 1.00 13.16 ATOM 195 CB TRP A 27 24.302 34.385 35.374 1.00 11.25 ATOM 196 CG TRP A 27 25.728 33.910 35.333 1.00 11.40 ATOM 197 CD1 TRP A 27 26.830 34.657 35.041 1.00 10.89 ATOM 198 CD2 TRP A 27 26.201 32.579 35.581 1.00 11.06 ATOM 199 NE1 TRP A 27 27.962 33.879 35.087 1.00 11.48 ATOM 200 CE2 TRP A 27 27.605 32.598 35.416 1.00 11.13 ATOM 201 CE3 TRP A 27 25.575 31.371 35.927 1.00 10.80 ATOM 202 CZ2 TRP A 27 28.398 31.455 35.584 1.00 11.60 ATOM 203 CZ3 TRP A 27 26.362 30.237 36.096 1.00 12.06 ATOM 204 CH2 TRP A 27 27.760 30.288 35.923 1.00 12.08 ATOM 205 N ALA A 28 24.304 33.115 38.577 1.00 13.30 ATOM 206 CA ALA A 28 24.223 31.852 39.305 1.00 15.55 ATOM 207 C ALA A 28 22.894 31.598 39.997 1.00 17.42 ATOM 208 O ALA A 28 22.227 30.594 39.732 1.00 16.18 ATOM 209 CB ALA A 28 25.356 31.761 40.318 1.00 14.01 ATOM 210 N ASP A 29 22.511 32.500 40.891 1.00 20.24 ATOM 211 CA ASP A 29 21.266 32.335 41.616 1.00 26.53 ATOM 212 C ASP A 29 20.096 32.846 40.783 1.00 27.78 ATOM 213 O ASP A 29 20.133 33.951 40.236 1.00 30.68 ATOM 214 CB ASP A 29 21.343 33.070 42.956 1.00 29.85 ATOM 215 CG ASP A 29 20.332 32.556 43.956 1.00 33.48 ATOM 216 OD1 ASP A 29 19.294 32.016 43.520 1.00 36.45 ATOM 217 OD2 ASP A 29 20.566 32.700 45.173 1.00 36.39 ATOM 218 N GLY A 30 19.055 32.030 40.695 1.00 28.87 ATOM 219 CA GLY A 30 17.878 32.401 39.935 1.00 24.89 ATOM 220 C GLY A 30 16.828 31.353 40.211 1.00 23.23 ATOM 221 O GLY A 30 16.820 30.744 41.284 1.00 23.85 ATOM 222 N GLY A 31 15.941 31.132 39.252 1.00 19.96 ATOM 223 CA GLY A 31 14.908 30.135 39.443 1.00 17.67 ATOM 224 C GLY A 31 15.442 28.734 39.220 1.00 16.00 ATOM 225 O GLY A 31 16.510 28.553 38.630 1.00 16.63 ATOM 226 N GLY A 32 14.696 27.741 39.692 1.00 14.70 ATOM 227 CA GLY A 32 15.106 26.360 39.528 1.00 12.96 ATOM 228 C GLY A 32 16.093 25.897 40.581 1.00 11.47 ATOM 229 O GLY A 32 16.252 26.531 41.624 1.00 14.71 ATOM 230 N PHE A 33 16.757 24.782 40.300 1.00 10.21 ATOM 231 CA PHE A 33 17.742 24.214 41.211 1.00 9.13 ATOM 232 C PHE A 33 19.069 24.939 41.031 1.00 8.49 ATOM 233 O PHE A 33 19.533 25.123 39.908 1.00 8.94 ATOM 234 CB PHE A 33 17.928 22.724 40.919 1.00 10.21 ATOM 235 CG PHE A 33 18.959 22.055 41.784 1.00 10.29 ATOM 236 CD1 PHE A 33 18.659 21.672 43.088 1.00 10.92 ATOM 237 CD2 PHE A 33 20.235 21.807 41.292 1.00 9.87 ATOM 238 CE1 PHE A 33 19.613 21.052 43.884 1.00 9.60 ATOM 239 CE2 PHE A 33 21.202 21.185 42.087 1.00 9.99 ATOM 240 CZ PHE A 33 20.889 20.809 43.381 1.00 10.27 ATOM 241 N VAL A 34 19.669 25.353 42.143 1.00 6.60 ATOM 242 CA VAL A 34 20.948 26.056 42.119 1.00 7.91 ATOM 243 C VAL A 34 21.891 25.492 43.174 1.00 8.36 ATOM 244 O VAL A 34 21.523 25.376 44.340 1.00 10.40 ATOM 245 CB VAL A 34 20.762 27.560 42.410 1.00 8.04 ATOM 246 CG1 VAL A 34 22.111 28.272 42.406 1.00 11.61 ATOM 247 CG2 VAL A 34 19.824 28.169 41.387 1.00 8.19 ATOM 248 N SER A 35 23.103 25.131 42.767 1.00 7.27 ATOM 249 CA SER A 35 24.084 24.628 43.716 1.00 5.98 ATOM 250 C SER A 35 25.418 25.284 43.413 1.00 8.17 ATOM 251 O SER A 35 26.023 25.028 42.375 1.00 7.54 ATOM 252 CB SER A 35 24.219 23.105 43.630 1.00 6.78 ATOM 253 OG SER A 35 25.036 22.632 44.690 1.00 7.53 ATOM 254 N ILE A 36 25.851 26.144 44.327 1.00 6.83 ATOM 255 CA ILE A 36 27.106 26.882 44.214 1.00 6.44 ATOM 256 C ILE A 36 28.074 26.322 45.254 1.00 6.22 ATOM 257 O ILE A 36 27.866 26.493 46.463 1.00 6.01 ATOM 258 CB ILE A 36 26.867 28.375 44.496 1.00 7.64 ATOM 259 CG1 ILE A 36 25.823 28.926 43.519 1.00 8.18 ATOM 260 CG2 ILE A 36 28.185 29.145 44.403 1.00 8.75 ATOM 261 CD ILE A 36 25.133 30.197 44.004 1.00 7.66 ATOM 262 N THR A 37 29.130 25.656 44.798 1.00 5.92 ATOM 263 CA THR A 37 30.089 25.056 45.712 1.00 5.47 ATOM 264 C THR A 37 31.512 25.553 45.485 1.00 6.33 ATOM 265 O THR A 37 32.049 25.459 44.379 1.00 7.84 ATOM 266 CB THR A 37 30.032 23.513 45.593 1.00 5.85 ATOM 267 OG1 THR A 37 28.714 23.077 45.947 1.00 7.93 ATOM 268 CG2 THR A 37 31.038 22.843 46.525 1.00 7.50 ATOM 269 N ARG A 38 32.113 26.100 46.537 1.00 6.54 ATOM 270 CA ARG A 38 33.478 26.590 46.442 1.00 7.84 ATOM 271 C ARG A 38 34.396 25.680 47.250 1.00 11.13 ATOM 272 O ARG A 38 34.107 25.346 48.403 1.00 10.54 ATOM 273 CB ARG A 38 33.578 28.031 46.954 1.00 7.49 ATOM 274 CG ARG A 38 34.908 28.705 46.609 1.00 7.68 ATOM 275 CD ARG A 38 35.067 30.048 47.298 1.00 8.43 ATOM 276 NE ARG A 38 34.064 31.030 46.890 1.00 8.65 ATOM 277 CZ ARG A 38 34.066 31.681 45.732 1.00 8.85 ATOM 278 NH1 ARG A 38 35.025 31.461 44.838 1.00 9.99 ATOM 279 NH2 ARG A 38 33.111 32.564 45.469 1.00 10.09 ATOM 280 N THR A 39 35.492 25.263 46.621 1.00 12.70 ATOM 281 CA THR A 39 36.472 24.398 47.261 1.00 14.46 ATOM 282 C THR A 39 37.830 25.071 47.128 1.00 17.55 ATOM 283 O THR A 39 37.926 26.186 46.617 1.00 16.90 ATOM 284 CB THR A 39 36.525 22.998 46.596 1.00 14.36 ATOM 285 OG1 THR A 39 37.164 23.091 45.319 1.00 15.67 ATOM 286 CG2 THR A 39 35.116 22.447 46.406 1.00 14.31 ATOM 287 N ASP A 40 38.878 24.393 47.573 1.00 21.55 ATOM 288 CA ASP A 40 40.214 24.965 47.506 1.00 24.37 ATOM 289 C ASP A 40 40.757 24.992 46.080 1.00 24.55 ATOM 290 O ASP A 40 41.819 25.564 45.827 1.00 26.49 ATOM 291 CB ASP A 40 41.159 24.178 48.420 1.00 27.89 ATOM 292 CG ASP A 40 41.436 22.776 47.910 1.00 32.15 ATOM 293 OD1 ASP A 40 40.556 22.196 47.237 1.00 35.66 ATOM 294 OD2 ASP A 40 42.534 22.250 48.196 1.00 35.21 ATOM 295 N ASP A 41 40.021 24.395 45.148 1.00 23.09 ATOM 296 CA ASP A 41 40.462 24.345 43.758 1.00 22.29 ATOM 297 C ASP A 41 39.462 24.824 42.716 1.00 19.64 ATOM 298 O ASP A 41 39.836 25.020 41.563 1.00 17.60 ATOM 299 CB ASP A 41 40.871 22.917 43.379 1.00 27.07 ATOM 300 CG ASP A 41 42.096 22.434 44.129 1.00 30.04 ATOM 301 OD1 ASP A 41 42.791 23.268 44.748 1.00 32.89 ATOM 302 OD2 ASP A 41 42.369 21.216 44.089 1.00 32.53 ATOM 303 N GLU A 42 38.200 25.013 43.096 1.00 16.89 ATOM 304 CA GLU A 42 37.200 25.423 42.112 1.00 14.31 ATOM 305 C GLU A 42 35.982 26.124 42.703 1.00 12.06 ATOM 306 O GLU A 42 35.754 26.110 43.917 1.00 10.37 ATOM 307 CB GLU A 42 36.684 24.182 41.354 1.00 15.82 ATOM 308 CG GLU A 42 35.546 23.461 42.113 1.00 14.13 ATOM 309 CD GLU A 42 35.186 22.075 41.580 1.00 12.12 ATOM 310 OE1 GLU A 42 34.751 21.953 40.410 1.00 10.68 ATOM 311 OE2 GLU A 42 35.327 21.104 42.354 1.00 11.90 ATOM 312 N LEU A 43 35.212 26.743 41.813 1.00 11.10 ATOM 313 CA LEU A 43 33.937 27.362 42.155 1.00 10.74 ATOM 314 C LEU A 43 33.033 26.679 41.132 1.00 10.28 ATOM 315 O LEU A 43 33.070 26.985 39.936 1.00 13.32 ATOM 316 CB LEU A 43 33.931 28.875 41.941 1.00 11.08 ATOM 317 CG LEU A 43 32.532 29.477 42.141 1.00 11.13 ATOM 318 CD1 LEU A 43 32.045 29.207 43.555 1.00 11.25 ATOM 319 CD2 LEU A 43 32.554 30.969 41.870 1.00 13.11 ATOM 320 N SER A 44 32.251 25.720 41.611 1.00 8.58 ATOM 321 CA SER A 44 31.363 24.934 40.766 1.00 7.79 ATOM 322 C SER A 44 29.936 25.441 40.882 1.00 9.61 ATOM 323 O SER A 44 29.465 25.703 41.979 1.00 8.88 ATOM 324 CB SER A 44 31.447 23.467 41.201 1.00 8.39 ATOM 325 OG SER A 44 30.594 22.638 40.439 1.00 8.47 ATOM 326 N ILE A 45 29.250 25.580 39.753 1.00 7.16 ATOM 327 CA ILE A 45 27.874 26.064 39.770 1.00 7.57 ATOM 328 C ILE A 45 26.925 25.230 38.922 1.00 6.98 ATOM 329 O ILE A 45 27.119 25.080 37.717 1.00 6.98 ATOM 330 CB ILE A 45 27.793 27.533 39.284 1.00 7.69 ATOM 331 CG1 ILE A 45 28.600 28.431 40.229 1.00 10.37 ATOM 332 CG2 ILE A 45 26.331 27.979 39.192 1.00 9.83 ATOM 333 CD ILE A 45 28.695 29.877 39.786 1.00 14.03 ATOM 334 N VAL A 46 25.899 24.677 39.560 1.00 6.69 ATOM 335 CA VAL A 46 24.887 23.920 38.841 1.00 7.66 ATOM 336 C VAL A 46 23.661 24.818 38.778 1.00 8.22 ATOM 337 O VAL A 46 23.212 25.327 39.802 1.00 7.75 ATOM 338 CB VAL A 46 24.489 22.629 39.579 1.00 8.18 ATOM 339 CG1 VAL A 46 23.384 21.907 38.808 1.00 6.55 ATOM 340 CG2 VAL A 46 25.703 21.735 39.745 1.00 9.02 ATOM 341 N CYS A 47 23.135 25.033 37.578 1.00 6.28 ATOM 342 CA CYS A 47 21.941 25.851 37.407 1.00 8.34 ATOM 343 C CYS A 47 21.409 25.649 36.001 1.00 9.48 ATOM 344 O CYS A 47 22.017 24.943 35.197 1.00 8.26 ATOM 345 CB CYS A 47 22.250 27.335 37.650 1.00 9.81 ATOM 346 SG CYS A 47 23.325 28.146 36.447 1.00 9.89 ATOM 347 N LEU A 48 20.264 26.252 35.710 1.00 10.37 ATOM 348 CA LEU A 48 19.676 26.124 34.385 1.00 10.97 ATOM 349 C LEU A 48 20.678 26.611 33.345 1.00 11.98 ATOM 350 O LEU A 48 21.251 27.692 33.476 1.00 10.25 ATOM 351 CB LEU A 48 18.372 26.924 34.314 1.00 10.76 ATOM 352 CG LEU A 48 17.224 26.308 35.121 1.00 12.44 ATOM 353 CD1 LEU A 48 16.040 27.258 35.175 1.00 13.06 ATOM 354 CD2 LEU A 48 16.818 24.988 34.482 1.00 13.34 ATOM 355 N ILE A 49 20.898 25.786 32.324 1.00 12.82 ATOM 356 CA ILE A 49 21.836 26.090 31.248 1.00 15.26 ATOM 357 C ILE A 49 21.607 27.462 30.627 1.00 16.07 ATOM 358 O ILE A 49 22.556 28.133 30.219 1.00 16.20 ATOM 359 CB ILE A 49 21.747 25.038 30.126 1.00 17.23 ATOM 360 CG1 ILE A 49 22.074 23.653 30.685 1.00 15.86 ATOM 361 CG2 ILE A 49 22.705 25.392 29.004 1.00 18.86 ATOM 362 CD ILE A 49 22.083 22.544 29.629 1.00 18.48 ATOM 363 N ASP A 50 20.346 27.868 30.557 1.00 17.24 ATOM 364 CA ASP A 50 19.981 29.156 29.978 1.00 18.60 ATOM 365 C ASP A 50 20.738 30.327 30.593 1.00 17.83 ATOM 366 O ASP A 50 20.999 31.325 29.918 1.00 17.75 ATOM 367 CB ASP A 50 18.479 29.399 30.136 1.00 21.82 ATOM 368 CG ASP A 50 17.643 28.327 29.473 1.00 26.17 ATOM 369 OD1 ASP A 50 17.907 28.011 28.293 1.00 29.36 ATOM 370 OD2 ASP A 50 16.710 27.810 30.127 1.00 29.68 ATOM 371 N ARG A 51 21.086 30.207 31.870 1.00 14.75 ATOM 372 CA ARG A 51 21.797 31.276 32.568 1.00 14.35 ATOM 373 C ARG A 51 23.317 31.193 32.490 1.00 13.71 ATOM 374 O ARG A 51 24.005 32.123 32.904 1.00 13.34 ATOM 375 CB ARG A 51 21.387 31.313 34.045 1.00 12.68 ATOM 376 CG ARG A 51 19.919 31.605 34.289 1.00 14.54 ATOM 377 CD ARG A 51 19.720 32.341 35.603 1.00 14.23 ATOM 378 NE ARG A 51 20.079 31.555 36.783 1.00 15.04 ATOM 379 CZ ARG A 51 19.355 30.550 37.272 1.00 16.43 ATOM 380 NH1 ARG A 51 18.222 30.192 36.682 1.00 15.01 ATOM 381 NH2 ARG A 51 19.752 29.918 38.368 1.00 15.23 ATOM 382 N ILE A 52 23.848 30.088 31.979 1.00 14.07 ATOM 383 CA ILE A 52 25.296 29.937 31.896 1.00 15.09 ATOM 384 C ILE A 52 25.839 30.602 30.633 1.00 15.50 ATOM 385 O ILE A 52 25.468 30.230 29.519 1.00 15.32 ATOM 386 CB ILE A 52 25.694 28.450 31.920 1.00 15.35 ATOM 387 CG1 ILE A 52 25.119 27.790 33.179 1.00 17.01 ATOM 388 CG2 ILE A 52 27.212 28.315 31.911 1.00 20.61 ATOM 389 CD ILE A 52 25.270 26.282 33.223 1.00 21.42 ATOM 390 N PRO A 53 26.713 31.613 30.799 1.00 16.63 ATOM 391 CA PRO A 53 27.334 32.367 29.703 1.00 18.39 ATOM 392 C PRO A 53 28.254 31.526 28.818 1.00 18.20 ATOM 393 O PRO A 53 28.730 30.465 29.224 1.00 19.18 ATOM 394 CB PRO A 53 28.101 33.471 30.433 1.00 18.47 ATOM 395 CG PRO A 53 27.320 33.659 31.690 1.00 19.83 ATOM 396 CD PRO A 53 27.038 32.235 32.094 1.00 18.26 ATOM 397 N GLN A 54 28.520 32.028 27.614 1.00 20.07 ATOM 398 CA GLN A 54 29.369 31.334 26.644 1.00 21.32 ATOM 399 C GLN A 54 30.869 31.445 26.929 1.00 21.35 ATOM 400 O GLN A 54 31.674 30.773 26.284 1.00 21.94 ATOM 401 CB GLN A 54 29.095 31.868 25.236 1.00 24.35 ATOM 402 CG GLN A 54 27.672 31.648 24.748 1.00 27.93 ATOM 403 CD GLN A 54 27.288 30.173 24.713 1.00 30.12 ATOM 404 OE1 GLN A 54 28.111 29.298 24.986 1.00 31.98 ATOM 405 NE2 GLN A 54 26.037 29.893 24.375 1.00 30.50 ATOM 406 N ASP A 55 31.246 32.301 27.876 1.00 20.18 ATOM 407 CA ASP A 55 32.654 32.485 28.234 1.00 22.12 ATOM 408 C ASP A 55 33.022 31.656 29.469 1.00 20.63 ATOM 409 O ASP A 55 34.097 31.838 30.042 1.00 19.94 ATOM 410 CB ASP A 55 32.942 33.974 28.488 1.00 25.28 ATOM 411 CG ASP A 55 32.299 34.488 29.764 1.00 29.91 ATOM 412 OD1 ASP A 55 31.231 33.964 30.131 1.00 32.97 ATOM 413 OD2 ASP A 55 32.847 35.426 30.391 1.00 32.89 ATOM 414 N VAL A 56 32.131 30.747 29.875 1.00 19.85 ATOM 415 CA VAL A 56 32.379 29.896 31.045 1.00 19.11 ATOM 416 C VAL A 56 32.431 28.404 30.694 1.00 17.79 ATOM 417 O VAL A 56 31.612 27.903 29.918 1.00 17.63 ATOM 418 CB VAL A 56 31.291 30.124 32.151 1.00 20.03 ATOM 419 CG1 VAL A 56 31.509 29.180 33.322 1.00 20.84 ATOM 420 CG2 VAL A 56 31.334 31.570 32.640 1.00 19.26 ATOM 421 N ARG A 57 33.415 27.705 31.256 1.00 16.63 ATOM 422 CA ARG A 57 33.554 26.273 31.025 1.00 14.78 ATOM 423 C ARG A 57 32.336 25.594 31.618 1.00 12.98 ATOM 424 O ARG A 57 31.908 25.922 32.727 1.00 11.66 ATOM 425 CB ARG A 57 34.833 25.734 31.673 1.00 17.71 ATOM 426 CG ARG A 57 36.094 26.086 30.896 1.00 22.06 ATOM 427 CD ARG A 57 37.248 25.161 31.259 1.00 24.89 ATOM 428 NE ARG A 57 37.669 25.313 32.648 1.00 25.09 ATOM 429 CZ ARG A 57 38.141 26.444 33.164 1.00 25.06 ATOM 430 NH1 ARG A 57 38.252 27.528 32.404 1.00 24.97 ATOM 431 NH2 ARG A 57 38.508 26.492 34.437 1.00 23.71 ATOM 432 N VAL A 58 31.775 24.642 30.888 1.00 11.17 ATOM 433 CA VAL A 58 30.581 23.978 31.368 1.00 11.12 ATOM 434 C VAL A 58 30.408 22.569 30.835 1.00 11.63 ATOM 435 O VAL A 58 30.827 22.247 29.726 1.00 12.85 ATOM 436 CB VAL A 58 29.316 24.812 31.003 1.00 10.30 ATOM 437 CG1 VAL A 58 29.143 24.874 29.495 1.00 13.57 ATOM 438 CG2 VAL A 58 28.083 24.217 31.665 1.00 11.26 ATOM 439 N ASP A 59 29.803 21.730 31.666 1.00 11.89 ATOM 440 CA ASP A 59 29.495 20.347 31.326 1.00 12.16 ATOM 441 C ASP A 59 27.971 20.436 31.226 1.00 13.61 ATOM 442 O ASP A 59 27.269 20.340 32.232 1.00 11.95 ATOM 443 CB ASP A 59 29.912 19.425 32.474 1.00 13.12 ATOM 444 CG ASP A 59 29.772 17.958 32.126 1.00 12.39 ATOM 445 OD1 ASP A 59 28.872 17.629 31.335 1.00 14.91 ATOM 446 OD2 ASP A 59 30.549 17.134 32.657 1.00 15.38 ATOM 447 N PRO A 60 27.438 20.644 30.010 1.00 14.32 ATOM 448 CA PRO A 60 25.987 20.759 29.845 1.00 13.39 ATOM 449 C PRO A 60 25.200 19.485 29.573 1.00 12.88 ATOM 450 O PRO A 60 25.762 18.397 29.455 1.00 13.46 ATOM 451 CB PRO A 60 25.866 21.736 28.686 1.00 17.77 ATOM 452 CG PRO A 60 26.963 21.263 27.803 1.00 16.37 ATOM 453 CD PRO A 60 28.127 21.043 28.767 1.00 17.57 ATOM 454 N GLY A 61 23.884 19.657 29.490 1.00 12.24 ATOM 455 CA GLY A 61 22.989 18.556 29.189 1.00 12.48 ATOM 456 C GLY A 61 22.610 17.650 30.338 1.00 11.98 ATOM 457 O GLY A 61 22.716 16.429 30.216 1.00 13.05 ATOM 458 N TRP A 62 22.158 18.229 31.446 1.00 10.87 ATOM 459 CA TRP A 62 21.767 17.427 32.602 1.00 11.32 ATOM 460 C TRP A 62 20.314 17.629 33.011 1.00 11.70 ATOM 461 O TRP A 62 19.720 18.681 32.768 1.00 11.98 ATOM 462 CB TRP A 62 22.665 17.737 33.805 1.00 8.21 ATOM 463 CG TRP A 62 24.102 17.404 33.597 1.00 9.26 ATOM 464 CD1 TRP A 62 25.000 18.079 32.821 1.00 8.48 ATOM 465 CD2 TRP A 62 24.814 16.308 34.175 1.00 9.56 ATOM 466 NE1 TRP A 62 26.230 17.471 32.880 1.00 9.77 ATOM 467 CE2 TRP A 62 26.145 16.379 33.704 1.00 10.37 ATOM 468 CE3 TRP A 62 24.457 15.268 35.045 1.00 11.14 ATOM 469 CZ2 TRP A 62 27.121 15.451 34.075 1.00 9.33 ATOM 470 CZ3 TRP A 62 25.427 14.345 35.415 1.00 8.36 ATOM 471 CH2 TRP A 62 26.746 14.443 34.930 1.00 10.55 ATOM 472 N SER A 63 19.755 16.601 33.643 1.00 11.61 ATOM 473 CA SER A 63 18.380 16.613 34.137 1.00 9.96 ATOM 474 C SER A 63 18.467 16.408 35.645 1.00 10.12 ATOM 475 O SER A 63 19.327 15.663 36.124 1.00 9.52 ATOM 476 CB SER A 63 17.564 15.484 33.502 1.00 12.04 ATOM 477 OG SER A 63 17.437 15.677 32.101 1.00 11.14 ATOM 478 N CYS A 64 17.571 17.056 36.383 1.00 10.06 ATOM 479 CA CYS A 64 17.579 16.989 37.839 1.00 11.01 ATOM 480 C CYS A 64 16.345 16.346 38.462 1.00 11.08 ATOM 481 O CYS A 64 15.221 16.540 37.992 1.00 10.96 ATOM 482 CB CYS A 64 17.755 18.406 38.391 1.00 11.23 ATOM 483 SG CYS A 64 18.038 18.516 40.163 1.00 11.32 ATOM 484 N PHE A 65 16.578 15.581 39.527 1.00 10.51 ATOM 485 CA PHE A 65 15.519 14.905 40.282 1.00 10.91 ATOM 486 C PHE A 65 15.647 15.272 41.749 1.00 10.56 ATOM 487 O PHE A 65 16.753 15.384 42.273 1.00 10.10 ATOM 488 CB PHE A 65 15.638 13.379 40.210 1.00 10.70 ATOM 489 CG PHE A 65 15.265 12.792 38.891 1.00 12.43 ATOM 490 CD1 PHE A 65 16.202 12.689 37.873 1.00 13.38 ATOM 491 CD2 PHE A 65 13.976 12.311 38.676 1.00 13.08 ATOM 492 CE1 PHE A 65 15.865 12.106 36.653 1.00 14.21 ATOM 493 CE2 PHE A 65 13.628 11.727 37.460 1.00 12.91 ATOM 494 CZ PHE A 65 14.572 11.623 36.449 1.00 15.08 ATOM 495 N LYS A 66 14.511 15.436 42.414 1.00 9.71 ATOM 496 CA LYS A 66 14.510 15.736 43.835 1.00 9.38 ATOM 497 C LYS A 66 14.084 14.480 44.586 1.00 10.12 ATOM 498 O LYS A 66 13.139 13.805 44.172 1.00 9.61 ATOM 499 CB LYS A 66 13.513 16.854 44.143 1.00 10.08 ATOM 500 CG LYS A 66 13.410 17.190 45.627 1.00 12.15 ATOM 501 CD LYS A 66 12.327 18.226 45.864 1.00 15.93 ATOM 502 CE LYS A 66 10.954 17.590 45.828 1.00 20.77 ATOM 503 NZ LYS A 66 10.756 16.692 47.001 1.00 25.28 ATOM 504 N PHE A 67 14.797 14.142 45.660 1.00 9.01 ATOM 505 CA PHE A 67 14.406 12.997 46.486 1.00 11.20 ATOM 506 C PHE A 67 13.241 13.581 47.294 1.00 13.68 ATOM 507 O PHE A 67 13.411 14.586 47.991 1.00 13.36 ATOM 508 CB PHE A 67 15.530 12.581 47.443 1.00 9.42 ATOM 509 CG PHE A 67 16.621 11.753 46.807 1.00 11.27 ATOM 510 CD1 PHE A 67 17.241 12.156 45.631 1.00 12.35 ATOM 511 CD2 PHE A 67 17.072 10.594 47.432 1.00 10.08 ATOM 512 CE1 PHE A 67 18.296 11.418 45.094 1.00 12.30 ATOM 513 CE2 PHE A 67 18.121 9.852 46.905 1.00 12.51 ATOM 514 CZ PHE A 67 18.738 10.264 45.732 1.00 11.69 ATOM 515 N GLN A 68 12.076 12.943 47.209 1.00 16.14 ATOM 516 CA GLN A 68 10.854 13.427 47.862 1.00 21.60 ATOM 517 C GLN A 68 10.386 12.989 49.248 1.00 24.54 ATOM 518 O GLN A 68 10.811 11.969 49.809 1.00 26.86 ATOM 519 CB GLN A 68 9.675 13.202 46.927 1.00 21.82 ATOM 520 CG GLN A 68 9.600 14.128 45.750 1.00 25.10 ATOM 521 CD GLN A 68 8.395 13.821 44.896 1.00 27.61 ATOM 522 OE1 GLN A 68 8.289 12.737 44.332 1.00 30.38 ATOM 523 NE2 GLN A 68 7.472 14.767 44.805 1.00 28.39 ATOM 524 N GLY A 69 9.461 13.812 49.749 1.00 29.19 ATOM 525 CA GLY A 69 8.808 13.627 51.034 1.00 31.61 ATOM 526 C GLY A 69 9.669 13.452 52.268 1.00 33.66 ATOM 527 O GLY A 69 10.904 13.473 52.189 1.00 34.28 ATOM 528 N PRO A 70 9.025 13.279 53.450 1.00 34.51 ATOM 529 CA PRO A 70 9.724 13.090 54.724 1.00 34.96 ATOM 530 C PRO A 70 10.629 11.870 54.639 1.00 35.08 ATOM 531 O PRO A 70 10.337 10.931 53.895 1.00 36.86 ATOM 532 CB PRO A 70 8.583 12.833 55.713 1.00 34.53 ATOM 533 CG PRO A 70 7.457 13.578 55.168 1.00 34.49 ATOM 534 CD PRO A 70 7.566 13.240 53.687 1.00 34.74 ATOM 535 N PHE A 71 11.715 11.865 55.402 1.00 34.98 ATOM 536 CA PHE A 71 12.611 10.719 55.375 1.00 33.66 ATOM 537 C PHE A 71 12.718 10.010 56.722 1.00 34.46 ATOM 538 O PHE A 71 13.727 10.126 57.423 1.00 34.08 ATOM 539 CB PHE A 71 14.011 11.132 54.903 1.00 31.58 ATOM 540 CG PHE A 71 14.068 11.563 53.466 1.00 29.98 ATOM 541 CD1 PHE A 71 13.795 10.661 52.443 1.00 28.89 ATOM 542 CD2 PHE A 71 14.396 12.874 53.135 1.00 28.67 ATOM 543 CE1 PHE A 71 13.841 11.059 51.110 1.00 28.32 ATOM 544 CE2 PHE A 71 14.445 13.283 51.805 1.00 27.24 ATOM 545 CZ PHE A 71 14.169 12.374 50.791 1.00 27.92 ATOM 546 N ALA A 72 11.670 9.290 57.098 1.00 35.85 ATOM 547 CA ALA A 72 11.721 8.541 58.339 1.00 36.85 ATOM 548 C ALA A 72 12.345 7.217 57.936 1.00 37.73 ATOM 549 O ALA A 72 11.675 6.371 57.339 1.00 37.96 ATOM 550 CB ALA A 72 10.323 8.321 58.898 1.00 37.07 ATOM 551 N PHE A 73 13.637 7.060 58.218 1.00 38.37 ATOM 552 CA PHE A 73 14.340 5.822 57.889 1.00 39.03 ATOM 553 C PHE A 73 14.992 5.243 59.141 1.00 39.25 ATOM 554 O PHE A 73 14.943 5.843 60.217 1.00 39.93 ATOM 555 CB PHE A 73 15.399 6.070 56.808 1.00 38.87 ATOM 556 N ASP A 74 15.595 4.068 59.003 1.00 39.35 ATOM 557 CA ASP A 74 16.246 3.429 60.136 1.00 39.07 ATOM 558 C ASP A 74 17.639 2.945 59.755 1.00 39.18 ATOM 559 O ASP A 74 17.870 1.746 59.586 1.00 39.58 ATOM 560 CB ASP A 74 15.398 2.264 60.635 1.00 38.53 ATOM 561 N GLU A 75 18.564 3.892 59.619 1.00 38.95 ATOM 562 CA GLU A 75 19.944 3.585 59.261 1.00 38.22 ATOM 563 C GLU A 75 20.051 2.875 57.910 1.00 37.77 ATOM 564 O GLU A 75 20.789 1.897 57.773 1.00 38.56 ATOM 565 CB GLU A 75 20.591 2.732 60.358 1.00 38.43 ATOM 566 N THR A 76 19.315 3.369 56.918 1.00 35.86 ATOM 567 CA THR A 76 19.338 2.789 55.576 1.00 33.95 ATOM 568 C THR A 76 19.936 3.793 54.591 1.00 31.24 ATOM 569 O THR A 76 19.762 4.999 54.743 1.00 33.03 ATOM 570 CB THR A 76 17.926 2.401 55.143 1.00 33.66 ATOM 571 N GLY A 77 20.641 3.291 53.583 1.00 27.98 ATOM 572 CA GLY A 77 21.256 4.174 52.610 1.00 20.16 ATOM 573 C GLY A 77 20.305 4.684 51.544 1.00 15.83 ATOM 574 O GLY A 77 20.145 4.053 50.503 1.00 13.37 ATOM 575 N ILE A 78 19.673 5.825 51.804 1.00 13.59 ATOM 576 CA ILE A 78 18.744 6.425 50.850 1.00 11.45 ATOM 577 C ILE A 78 19.454 6.770 49.540 1.00 9.12 ATOM 578 O ILE A 78 18.987 6.405 48.459 1.00 8.91 ATOM 579 CB ILE A 78 18.090 7.697 51.447 1.00 11.99 ATOM 580 CG1 ILE A 78 17.056 7.292 52.503 1.00 14.44 ATOM 581 CG2 ILE A 78 17.430 8.524 50.355 1.00 12.58 ATOM 582 CD ILE A 78 16.406 8.467 53.216 1.00 12.70 ATOM 583 N VAL A 79 20.579 7.472 49.625 1.00 8.24 ATOM 584 CA VAL A 79 21.314 7.825 48.417 1.00 8.54 ATOM 585 C VAL A 79 21.847 6.558 47.753 1.00 8.22 ATOM 586 O VAL A 79 21.739 6.389 46.540 1.00 6.49 ATOM 587 CB VAL A 79 22.481 8.790 48.738 1.00 9.04 ATOM 588 CG1 VAL A 79 23.360 8.988 47.509 1.00 8.60 ATOM 589 CG2 VAL A 79 21.925 10.137 49.181 1.00 9.87 ATOM 590 N LEU A 80 22.416 5.661 48.552 1.00 8.65 ATOM 591 CA LEU A 80 22.949 4.414 48.022 1.00 9.32 ATOM 592 C LEU A 80 21.903 3.640 47.219 1.00 7.79 ATOM 593 O LEU A 80 22.184 3.166 46.117 1.00 7.88 ATOM 594 CB LEU A 80 23.465 3.533 49.168 1.00 10.92 ATOM 595 CG LEU A 80 23.930 2.119 48.800 1.00 11.56 ATOM 596 CD1 LEU A 80 25.175 2.182 47.933 1.00 12.48 ATOM 597 CD2 LEU A 80 24.216 1.337 50.078 1.00 12.69 ATOM 598 N SER A 81 20.698 3.529 47.771 1.00 9.17 ATOM 599 CA SER A 81 19.625 2.780 47.122 1.00 9.31 ATOM 600 C SER A 81 19.288 3.324 45.741 1.00 9.20 ATOM 601 O SER A 81 18.852 2.580 44.859 1.00 10.79 ATOM 602 CB SER A 81 18.358 2.788 47.992 1.00 10.98 ATOM 603 OG SER A 81 17.670 4.026 47.911 1.00 12.54 ATOM 604 N VAL A 82 19.506 4.619 45.549 1.00 8.77 ATOM 605 CA VAL A 82 19.207 5.248 44.274 1.00 8.47 ATOM 606 C VAL A 82 20.376 5.201 43.291 1.00 8.23 ATOM 607 O VAL A 82 20.200 4.835 42.134 1.00 10.12 ATOM 608 CB VAL A 82 18.751 6.719 44.483 1.00 6.27 ATOM 609 CG1 VAL A 82 18.658 7.442 43.150 1.00 9.42 ATOM 610 CG2 VAL A 82 17.393 6.735 45.163 1.00 9.96 ATOM 611 N ILE A 83 21.577 5.539 43.747 1.00 7.29 ATOM 612 CA ILE A 83 22.709 5.535 42.828 1.00 9.59 ATOM 613 C ILE A 83 23.284 4.163 42.491 1.00 8.14 ATOM 614 O ILE A 83 23.908 3.999 41.444 1.00 10.83 ATOM 615 CB ILE A 83 23.851 6.457 43.320 1.00 9.77 ATOM 616 CG1 ILE A 83 24.481 5.902 44.595 1.00 10.04 ATOM 617 CG2 ILE A 83 23.309 7.869 43.544 1.00 10.94 ATOM 618 CD ILE A 83 25.806 6.561 44.944 1.00 13.02 ATOM 619 N SER A 84 23.067 3.168 43.347 1.00 9.39 ATOM 620 CA SER A 84 23.609 1.837 43.066 1.00 10.32 ATOM 621 C SER A 84 23.148 1.286 41.712 1.00 10.28 ATOM 622 O SER A 84 23.970 0.856 40.899 1.00 9.49 ATOM 623 CB SER A 84 23.230 0.855 44.176 1.00 14.52 ATOM 624 OG SER A 84 23.824 -0.414 43.938 1.00 21.32 ATOM 625 N PRO A 85 21.830 1.284 41.449 1.00 10.14 ATOM 626 CA PRO A 85 21.380 0.759 40.152 1.00 10.30 ATOM 627 C PRO A 85 21.845 1.575 38.950 1.00 10.79 ATOM 628 O PRO A 85 21.931 1.061 37.835 1.00 12.08 ATOM 629 CB PRO A 85 19.857 0.724 40.292 1.00 12.13 ATOM 630 CG PRO A 85 19.568 1.753 41.346 1.00 11.20 ATOM 631 CD PRO A 85 20.687 1.574 42.331 1.00 10.24 ATOM 632 N LEU A 86 22.155 2.846 39.171 1.00 9.02 ATOM 633 CA LEU A 86 22.615 3.694 38.080 1.00 8.69 ATOM 634 C LEU A 86 24.110 3.508 37.817 1.00 9.30 ATOM 635 O LEU A 86 24.529 3.224 36.692 1.00 10.62 ATOM 636 CB LEU A 86 22.315 5.166 38.395 1.00 8.40 ATOM 637 CG LEU A 86 20.837 5.505 38.624 1.00 7.45 ATOM 638 CD1 LEU A 86 20.679 6.994 38.909 1.00 10.32 ATOM 639 CD2 LEU A 86 20.024 5.099 37.390 1.00 9.51 ATOM 640 N SER A 87 24.912 3.649 38.868 1.00 10.05 ATOM 641 CA SER A 87 26.359 3.519 38.752 1.00 11.05 ATOM 642 C SER A 87 26.823 2.143 38.292 1.00 12.12 ATOM 643 O SER A 87 27.791 2.037 37.536 1.00 16.05 ATOM 644 CB SER A 87 27.023 3.871 40.084 1.00 9.43 ATOM 645 OG SER A 87 26.804 5.233 40.405 1.00 12.60 ATOM 646 N THR A 88 26.137 1.097 38.741 1.00 11.08 ATOM 647 CA THR A 88 26.499 -0.265 38.359 1.00 14.52 ATOM 648 C THR A 88 26.098 -0.544 36.916 1.00 14.74 ATOM 649 O THR A 88 26.523 -1.539 36.330 1.00 16.50 ATOM 650 CB THR A 88 25.822 -1.312 39.269 1.00 16.36 ATOM 651 OG1 THR A 88 24.400 -1.170 39.193 1.00 20.05 ATOM 652 CG2 THR A 88 26.271 -1.133 40.714 1.00 20.19 ATOM 653 N ASN A 89 25.297 0.341 36.334 1.00 13.39 ATOM 654 CA ASN A 89 24.859 0.148 34.957 1.00 15.15 ATOM 655 C ASN A 89 25.289 1.234 33.968 1.00 15.78 ATOM 656 O ASN A 89 24.574 1.547 33.016 1.00 18.43 ATOM 657 CB ASN A 89 23.340 -0.057 34.928 1.00 13.82 ATOM 658 CG ASN A 89 22.931 -1.403 35.512 1.00 15.30 ATOM 659 OD1 ASN A 89 23.266 -2.459 34.964 1.00 18.32 ATOM 660 ND2 ASN A 89 22.224 -1.376 36.631 1.00 14.60 ATOM 661 N GLY A 90 26.467 1.804 34.204 1.00 15.31 ATOM 662 CA GLY A 90 27.013 2.809 33.307 1.00 15.12 ATOM 663 C GLY A 90 26.402 4.197 33.270 1.00 16.72 ATOM 664 O GLY A 90 26.639 4.947 32.320 1.00 18.28 ATOM 665 N ILE A 91 25.622 4.557 34.282 1.00 13.49 ATOM 666 CA ILE A 91 25.016 5.882 34.301 1.00 13.59 ATOM 667 C ILE A 91 25.760 6.792 35.274 1.00 13.05 ATOM 668 O ILE A 91 25.835 6.509 36.466 1.00 12.54 ATOM 669 CB ILE A 91 23.524 5.815 34.708 1.00 11.79 ATOM 670 CG1 ILE A 91 22.771 4.870 33.762 1.00 14.98 ATOM 671 CG2 ILE A 91 22.909 7.215 34.676 1.00 13.34 ATOM 672 CD ILE A 91 21.280 4.845 33.972 1.00 18.63 ATOM 673 N GLY A 92 26.325 7.875 34.753 1.00 12.56 ATOM 674 CA GLY A 92 27.040 8.806 35.604 1.00 12.59 ATOM 675 C GLY A 92 26.058 9.540 36.490 1.00 12.60 ATOM 676 O GLY A 92 24.949 9.874 36.059 1.00 12.27 ATOM 677 N ILE A 93 26.458 9.785 37.733 1.00 11.38 ATOM 678 CA ILE A 93 25.602 10.482 38.686 1.00 11.66 ATOM 679 C ILE A 93 26.262 11.715 39.292 1.00 10.72 ATOM 680 O ILE A 93 27.484 11.788 39.422 1.00 12.84 ATOM 681 CB ILE A 93 25.155 9.535 39.828 1.00 10.71 ATOM 682 CG1 ILE A 93 26.367 9.004 40.607 1.00 13.81 ATOM 683 CG2 ILE A 93 24.360 8.381 39.255 1.00 11.33 ATOM 684 CD ILE A 93 26.788 9.880 41.783 1.00 14.20 ATOM 685 N PHE A 94 25.429 12.681 39.660 1.00 8.61 ATOM 686 CA PHE A 94 25.884 13.932 40.259 1.00 9.21 ATOM 687 C PHE A 94 24.909 14.145 41.410 1.00 7.65 ATOM 688 O PHE A 94 23.724 14.379 41.194 1.00 9.68 ATOM 689 CB PHE A 94 25.787 15.063 39.227 1.00 8.74 ATOM 690 CG PHE A 94 26.455 16.339 39.653 1.00 7.67 ATOM 691 CD1 PHE A 94 25.836 17.195 40.559 1.00 8.74 ATOM 692 CD2 PHE A 94 27.706 16.687 39.146 1.00 10.51 ATOM 693 CE1 PHE A 94 26.450 18.382 40.954 1.00 8.74 ATOM 694 CE2 PHE A 94 28.329 17.874 39.538 1.00 8.81 ATOM 695 CZ PHE A 94 27.698 18.720 40.441 1.00 10.58 ATOM 696 N VAL A 95 25.409 14.053 42.636 1.00 7.55 ATOM 697 CA VAL A 95 24.554 14.181 43.806 1.00 8.71 ATOM 698 C VAL A 95 24.795 15.428 44.621 1.00 8.81 ATOM 699 O VAL A 95 25.931 15.792 44.889 1.00 8.59 ATOM 700 CB VAL A 95 24.730 12.967 44.752 1.00 10.26 ATOM 701 CG1 VAL A 95 23.849 13.125 45.990 1.00 13.54 ATOM 702 CG2 VAL A 95 24.392 11.684 44.007 1.00 17.29 ATOM 703 N VAL A 96 23.713 16.084 45.013 1.00 6.59 ATOM 704 CA VAL A 96 23.823 17.262 45.853 1.00 7.91 ATOM 705 C VAL A 96 22.919 17.080 47.062 1.00 6.95 ATOM 706 O VAL A 96 21.695 17.215 46.972 1.00 7.49 ATOM 707 CB VAL A 96 23.420 18.552 45.108 1.00 9.80 ATOM 708 CG1 VAL A 96 23.515 19.743 46.047 1.00 15.38 ATOM 709 CG2 VAL A 96 24.333 18.770 43.921 1.00 10.02 ATOM 710 N SER A 97 23.523 16.744 48.195 1.00 7.59 ATOM 711 CA SER A 97 22.773 16.587 49.430 1.00 7.47 ATOM 712 C SER A 97 22.501 17.988 49.961 1.00 7.17 ATOM 713 O SER A 97 23.261 18.921 49.702 1.00 8.18 ATOM 714 CB SER A 97 23.585 15.798 50.464 1.00 7.48 ATOM 715 OG SER A 97 23.836 14.477 50.017 1.00 7.35 ATOM 716 N THR A 98 21.396 18.131 50.676 1.00 5.58 ATOM 717 CA THR A 98 21.024 19.403 51.275 1.00 7.74 ATOM 718 C THR A 98 20.506 19.099 52.669 1.00 7.74 ATOM 719 O THR A 98 20.330 17.937 53.041 1.00 8.05 ATOM 720 CB THR A 98 19.893 20.104 50.494 1.00 8.64 ATOM 721 OG1 THR A 98 18.724 19.281 50.510 1.00 9.16 ATOM 722 CG2 THR A 98 20.310 20.355 49.054 1.00 11.02 ATOM 723 N PHE A 99 20.253 20.146 53.438 1.00 7.11 ATOM 724 CA PHE A 99 19.729 19.965 54.783 1.00 8.65 ATOM 725 C PHE A 99 18.493 19.049 54.753 1.00 10.01 ATOM 726 O PHE A 99 18.430 18.059 55.486 1.00 11.74 ATOM 727 CB PHE A 99 19.391 21.341 55.374 1.00 9.42 ATOM 728 CG PHE A 99 18.840 21.296 56.774 1.00 9.98 ATOM 729 CD1 PHE A 99 17.493 21.029 56.994 1.00 10.76 ATOM 730 CD2 PHE A 99 19.668 21.531 57.869 1.00 10.84 ATOM 731 CE1 PHE A 99 16.975 20.999 58.282 1.00 13.42 ATOM 732 CE2 PHE A 99 19.158 21.502 59.169 1.00 11.13 ATOM 733 CZ PHE A 99 17.807 21.235 59.371 1.00 12.25 ATOM 734 N ASP A 100 17.531 19.362 53.885 1.00 9.41 ATOM 735 CA ASP A 100 16.301 18.568 53.780 1.00 10.26 ATOM 736 C ASP A 100 16.466 17.166 53.210 1.00 11.50 ATOM 737 O ASP A 100 15.779 16.236 53.633 1.00 12.91 ATOM 738 CB ASP A 100 15.260 19.293 52.924 1.00 10.82 ATOM 739 CG ASP A 100 14.577 20.428 53.657 1.00 11.97 ATOM 740 OD1 ASP A 100 14.861 20.640 54.860 1.00 12.42 ATOM 741 OD2 ASP A 100 13.742 21.109 53.023 1.00 15.66 ATOM 742 N GLY A 101 17.351 17.007 52.236 1.00 9.32 ATOM 743 CA GLY A 101 17.517 15.693 51.644 1.00 10.22 ATOM 744 C GLY A 101 18.574 15.643 50.565 1.00 7.75 ATOM 745 O GLY A 101 19.744 15.909 50.828 1.00 10.44 ATOM 746 N ASP A 102 18.166 15.304 49.346 1.00 8.69 ATOM 747 CA ASP A 102 19.112 15.205 48.242 1.00 9.06 ATOM 748 C ASP A 102 18.469 15.454 46.894 1.00 8.56 ATOM 749 O ASP A 102 17.263 15.284 46.716 1.00 8.00 ATOM 750 CB ASP A 102 19.721 13.797 48.159 1.00 9.41 ATOM 751 CG ASP A 102 20.185 13.266 49.494 1.00 9.82 ATOM 752 OD1 ASP A 102 21.381 13.425 49.813 1.00 12.58 ATOM 753 OD2 ASP A 102 19.353 12.684 50.220 1.00 11.61 ATOM 754 N HSD A 103 19.312 15.852 45.949 1.00 8.02 ATOM 755 CA HSD A 103 18.914 16.036 44.564 1.00 8.59 ATOM 756 C HSD A 103 19.920 15.219 43.766 1.00 7.86 ATOM 757 O HSD A 103 21.063 15.041 44.187 1.00 6.53 ATOM 758 CB HSD A 103 18.966 17.504 44.139 1.00 8.97 ATOM 759 CG HSD A 103 17.728 18.272 44.485 1.00 8.36 ATOM 760 ND1 HSD A 103 16.805 18.674 43.542 1.00 12.28 ATOM 761 CD2 HSD A 103 17.272 18.725 45.674 1.00 7.35 ATOM 762 CE1 HSD A 103 15.836 19.349 44.139 1.00 10.03 ATOM 763 NE2 HSD A 103 16.096 19.393 45.432 1.00 11.96 ATOM 764 N LEU A 104 19.485 14.702 42.626 1.00 6.74 ATOM 765 CA LEU A 104 20.337 13.887 41.770 1.00 8.34 ATOM 766 C LEU A 104 20.245 14.382 40.342 1.00 8.65 ATOM 767 O LEU A 104 19.153 14.654 39.855 1.00 7.25 ATOM 768 CB LEU A 104 19.867 12.422 41.798 1.00 9.79 ATOM 769 CG LEU A 104 20.363 11.542 40.640 1.00 11.68 ATOM 770 CD1 LEU A 104 21.817 11.198 40.873 1.00 11.62 ATOM 771 CD2 LEU A 104 19.533 10.275 40.526 1.00 10.51 ATOM 772 N LEU A 105 21.384 14.519 39.678 1.00 7.35 ATOM 773 CA LEU A 105 21.361 14.900 38.280 1.00 7.11 ATOM 774 C LEU A 105 22.042 13.799 37.477 1.00 7.97 ATOM 775 O LEU A 105 22.993 13.167 37.938 1.00 7.61 ATOM 776 CB LEU A 105 22.078 16.238 38.044 1.00 9.31 ATOM 777 CG LEU A 105 21.412 17.479 38.647 1.00 6.85 ATOM 778 CD1 LEU A 105 22.063 17.797 39.983 1.00 8.79 ATOM 779 CD2 LEU A 105 21.540 18.670 37.698 1.00 10.28 ATOM 780 N VAL A 106 21.508 13.547 36.291 1.00 8.15 ATOM 781 CA VAL A 106 22.070 12.569 35.377 1.00 9.63 ATOM 782 C VAL A 106 22.031 13.270 34.032 1.00 9.29 ATOM 783 O VAL A 106 21.287 14.237 33.860 1.00 9.69 ATOM 784 CB VAL A 106 21.230 11.262 35.293 1.00 9.81 ATOM 785 CG1 VAL A 106 21.247 10.546 36.643 1.00 10.85 ATOM 786 CG2 VAL A 106 19.808 11.571 34.860 1.00 11.25 ATOM 787 N ARG A 107 22.838 12.808 33.085 1.00 11.47 ATOM 788 CA ARG A 107 22.828 13.425 31.770 1.00 11.49 ATOM 789 C ARG A 107 21.448 13.202 31.178 1.00 12.07 ATOM 790 O ARG A 107 20.845 12.136 31.355 1.00 11.99 ATOM 791 CB ARG A 107 23.916 12.815 30.885 1.00 13.81 ATOM 792 CG ARG A 107 25.313 13.134 31.379 1.00 15.31 ATOM 793 CD ARG A 107 26.399 12.575 30.473 1.00 18.80 ATOM 794 NE ARG A 107 27.736 12.927 30.952 1.00 21.76 ATOM 795 CZ ARG A 107 28.226 14.165 30.971 1.00 23.26 ATOM 796 NH1 ARG A 107 27.493 15.180 30.535 1.00 23.00 ATOM 797 NH2 ARG A 107 29.448 14.389 31.436 1.00 24.14 ATOM 798 N SER A 108 20.940 14.211 30.484 1.00 11.04 ATOM 799 CA SER A 108 19.620 14.116 29.892 1.00 12.91 ATOM 800 C SER A 108 19.464 12.962 28.921 1.00 12.91 ATOM 801 O SER A 108 18.381 12.405 28.797 1.00 13.61 ATOM 802 CB SER A 108 19.262 15.433 29.211 1.00 13.59 ATOM 803 OG SER A 108 19.250 16.476 30.174 1.00 15.49 ATOM 804 N ASN A 109 20.538 12.597 28.237 1.00 13.93 ATOM 805 CA ASN A 109 20.464 11.490 27.297 1.00 16.44 ATOM 806 C ASN A 109 20.323 10.154 28.027 1.00 16.68 ATOM 807 O ASN A 109 20.018 9.134 27.405 1.00 18.47 ATOM 808 CB ASN A 109 21.699 11.468 26.381 1.00 19.49 ATOM 809 CG ASN A 109 23.002 11.399 27.149 1.00 25.53 ATOM 810 OD1 ASN A 109 23.017 11.101 28.338 1.00 28.50 ATOM 811 ND2 ASN A 109 24.108 11.657 26.462 1.00 28.10 ATOM 812 N ASP A 110 20.534 10.164 29.344 1.00 13.51 ATOM 813 CA ASP A 110 20.407 8.956 30.165 1.00 12.86 ATOM 814 C ASP A 110 19.073 8.908 30.910 1.00 12.10 ATOM 815 O ASP A 110 18.835 8.002 31.710 1.00 11.29 ATOM 816 CB ASP A 110 21.536 8.871 31.207 1.00 12.79 ATOM 817 CG ASP A 110 22.885 8.570 30.594 1.00 13.28 ATOM 818 OD1 ASP A 110 22.936 7.743 29.658 1.00 16.61 ATOM 819 OD2 ASP A 110 23.898 9.141 31.064 1.00 15.43 ATOM 820 N LEU A 111 18.201 9.870 30.632 1.00 12.96 ATOM 821 CA LEU A 111 16.915 9.958 31.314 1.00 12.29 ATOM 822 C LEU A 111 16.030 8.717 31.203 1.00 11.83 ATOM 823 O LEU A 111 15.495 8.236 32.209 1.00 11.81 ATOM 824 CB LEU A 111 16.157 11.199 30.824 1.00 15.62 ATOM 825 CG LEU A 111 15.029 11.741 31.707 1.00 18.24 ATOM 826 CD1 LEU A 111 15.489 11.805 33.159 1.00 17.15 ATOM 827 CD2 LEU A 111 14.621 13.127 31.211 1.00 18.18 ATOM 828 N GLU A 112 15.877 8.192 29.993 1.00 13.16 ATOM 829 CA GLU A 112 15.040 7.015 29.779 1.00 12.74 ATOM 830 C GLU A 112 15.600 5.771 30.464 1.00 11.66 ATOM 831 O GLU A 112 14.861 5.014 31.091 1.00 11.14 ATOM 832 CB GLU A 112 14.864 6.762 28.278 1.00 15.04 ATOM 833 CG GLU A 112 14.197 7.921 27.541 1.00 20.79 ATOM 834 CD GLU A 112 12.739 8.124 27.934 1.00 21.66 ATOM 835 OE1 GLU A 112 12.294 7.528 28.939 1.00 25.41 ATOM 836 OE2 GLU A 112 12.032 8.890 27.236 1.00 15.32 ATOM 837 N LYS A 113 16.908 5.561 30.351 1.00 9.90 ATOM 838 CA LYS A 113 17.532 4.408 30.993 1.00 9.55 ATOM 839 C LYS A 113 17.476 4.559 32.511 1.00 8.63 ATOM 840 O LYS A 113 17.240 3.592 33.230 1.00 8.62 ATOM 841 CB LYS A 113 18.983 4.261 30.525 1.00 11.80 ATOM 842 CG LYS A 113 19.101 3.927 29.047 1.00 15.20 ATOM 843 CD LYS A 113 20.545 3.799 28.569 1.00 18.08 ATOM 844 CE LYS A 113 21.265 5.139 28.531 1.00 20.35 ATOM 845 NZ LYS A 113 22.569 5.030 27.813 1.00 24.78 ATOM 846 N THR A 114 17.668 5.784 32.991 1.00 9.28 ATOM 847 CA THR A 114 17.634 6.040 34.423 1.00 8.96 ATOM 848 C THR A 114 16.266 5.686 34.994 1.00 8.47 ATOM 849 O THR A 114 16.163 5.028 36.033 1.00 7.68 ATOM 850 CB THR A 114 17.956 7.519 34.716 1.00 10.08 ATOM 851 OG1 THR A 114 19.328 7.771 34.395 1.00 11.17 ATOM 852 CG2 THR A 114 17.695 7.854 36.182 1.00 8.68 ATOM 853 N ALA A 115 15.212 6.112 34.309 1.00 7.80 ATOM 854 CA ALA A 115 13.863 5.814 34.773 1.00 8.72 ATOM 855 C ALA A 115 13.586 4.311 34.799 1.00 9.07 ATOM 856 O ALA A 115 12.984 3.810 35.753 1.00 8.82 ATOM 857 CB ALA A 115 12.839 6.525 33.906 1.00 10.55 ATOM 858 N ASP A 116 14.035 3.583 33.773 1.00 7.46 ATOM 859 CA ASP A 116 13.814 2.137 33.733 1.00 6.42 ATOM 860 C ASP A 116 14.549 1.450 34.879 1.00 6.36 ATOM 861 O ASP A 116 13.988 0.592 35.557 1.00 8.51 ATOM 862 CB ASP A 116 14.292 1.524 32.409 1.00 7.91 ATOM 863 CG ASP A 116 13.397 1.875 31.239 1.00 12.32 ATOM 864 OD1 ASP A 116 12.201 2.166 31.462 1.00 14.46 ATOM 865 OD2 ASP A 116 13.889 1.838 30.093 1.00 12.27 ATOM 866 N LEU A 117 15.803 1.837 35.092 1.00 7.69 ATOM 867 CA LEU A 117 16.612 1.240 36.144 1.00 9.08 ATOM 868 C LEU A 117 16.087 1.534 37.540 1.00 9.13 ATOM 869 O LEU A 117 16.075 0.651 38.392 1.00 8.69 ATOM 870 CB LEU A 117 18.061 1.715 36.027 1.00 9.34 ATOM 871 CG LEU A 117 18.807 1.240 34.775 1.00 12.10 ATOM 872 CD1 LEU A 117 20.130 1.972 34.676 1.00 14.42 ATOM 873 CD2 LEU A 117 19.025 -0.268 34.825 1.00 19.15 ATOM 874 N LEU A 118 15.645 2.763 37.777 1.00 9.25 ATOM 875 CA LEU A 118 15.135 3.110 39.096 1.00 8.57 ATOM 876 C LEU A 118 13.808 2.414 39.392 1.00 8.68 ATOM 877 O LEU A 118 13.570 1.979 40.518 1.00 8.63 ATOM 878 CB LEU A 118 14.987 4.626 39.231 1.00 9.15 ATOM 879 CG LEU A 118 16.325 5.372 39.224 1.00 10.66 ATOM 880 CD1 LEU A 118 16.083 6.869 39.301 1.00 12.60 ATOM 881 CD2 LEU A 118 17.177 4.906 40.399 1.00 12.55 ATOM 882 N ALA A 119 12.945 2.300 38.390 1.00 7.88 ATOM 883 CA ALA A 119 11.667 1.626 38.602 1.00 8.85 ATOM 884 C ALA A 119 11.905 0.151 38.918 1.00 10.83 ATOM 885 O ALA A 119 11.307 -0.403 39.840 1.00 9.68 ATOM 886 CB ALA A 119 10.783 1.764 37.373 1.00 9.89 ATOM 887 N ASN A 120 12.790 -0.489 38.161 1.00 9.83 ATOM 888 CA ASN A 120 13.081 -1.899 38.398 1.00 10.58 ATOM 889 C ASN A 120 13.639 -2.101 39.807 1.00 10.47 ATOM 890 O ASN A 120 13.421 -3.143 40.430 1.00 11.26 ATOM 891 CB ASN A 120 14.070 -2.424 37.349 1.00 12.86 ATOM 892 CG ASN A 120 13.426 -2.606 35.973 1.00 15.89 ATOM 893 OD1 ASN A 120 14.099 -2.955 34.998 1.00 19.91 ATOM 894 ND2 ASN A 120 12.120 -2.377 35.893 1.00 17.89 ATOM 895 N ALA A 121 14.339 -1.085 40.312 1.00 9.79 ATOM 896 CA ALA A 121 14.928 -1.135 41.649 1.00 10.27 ATOM 897 C ALA A 121 13.892 -0.880 42.751 1.00 10.98 ATOM 898 O ALA A 121 14.213 -0.912 43.941 1.00 13.31 ATOM 899 CB ALA A 121 16.073 -0.125 41.747 1.00 10.19 ATOM 900 N GLY A 122 12.653 -0.618 42.346 1.00 11.17 ATOM 901 CA GLY A 122 11.585 -0.401 43.305 1.00 10.45 ATOM 902 C GLY A 122 11.249 1.032 43.663 1.00 9.97 ATOM 903 O GLY A 122 10.378 1.274 44.501 1.00 11.66 ATOM 904 N HSD A 123 11.932 1.990 43.050 1.00 7.29 ATOM 905 CA HSD A 123 11.663 3.388 43.345 1.00 9.45 ATOM 906 C HSD A 123 10.471 3.912 42.563 1.00 11.86 ATOM 907 O HSD A 123 10.111 3.366 41.520 1.00 12.48 ATOM 908 CB HSD A 123 12.898 4.229 43.048 1.00 8.15 ATOM 909 CG HSD A 123 14.106 3.807 43.822 1.00 9.94 ATOM 910 ND1 HSD A 123 14.158 3.844 45.199 1.00 10.97 ATOM 911 CD2 HSD A 123 15.301 3.321 43.412 1.00 11.30 ATOM 912 CE1 HSD A 123 15.333 3.397 45.604 1.00 11.51 ATOM 913 NE2 HSD A 123 16.045 3.072 44.539 1.00 10.97 ATOM 914 N SER A 124 9.857 4.966 43.089 1.00 14.10 ATOM 915 CA SER A 124 8.703 5.592 42.457 1.00 16.72 ATOM 916 C SER A 124 9.175 6.867 41.773 1.00 16.76 ATOM 917 O SER A 124 9.982 7.609 42.327 1.00 19.36 ATOM 918 CB SER A 124 7.643 5.929 43.509 1.00 18.00 ATOM 919 OG SER A 124 6.521 6.557 42.914 1.00 24.90 ATOM 920 N LEU A 125 8.678 7.127 40.573 1.00 15.57 ATOM 921 CA LEU A 125 9.094 8.324 39.866 1.00 16.06 ATOM 922 C LEU A 125 7.932 9.206 39.438 1.00 14.84 ATOM 923 O LEU A 125 6.982 8.742 38.809 1.00 17.07 ATOM 924 CB LEU A 125 9.922 7.953 38.634 1.00 18.47 ATOM 925 CG LEU A 125 11.134 7.047 38.864 1.00 18.85 ATOM 926 CD1 LEU A 125 11.868 6.866 37.546 1.00 20.97 ATOM 927 CD2 LEU A 125 12.056 7.648 39.913 1.00 21.51 ATOM 928 N LEU A 126 8.005 10.479 39.805 1.00 13.36 ATOM 929 CA LEU A 126 6.990 11.447 39.411 1.00 13.41 ATOM 930 C LEU A 126 7.645 12.167 38.240 1.00 13.43 ATOM 931 O LEU A 126 8.558 12.974 38.429 1.00 14.46 ATOM 932 CB LEU A 126 6.694 12.423 40.553 1.00 16.45 ATOM 933 CG LEU A 126 6.057 11.858 41.829 1.00 21.57 ATOM 934 CD1 LEU A 126 5.611 13.018 42.704 1.00 23.86 ATOM 935 CD2 LEU A 126 4.861 10.975 41.491 1.00 23.43 ATOM 936 N LEU A 127 7.186 11.868 37.027 1.00 14.06 ATOM 937 CA LEU A 127 7.789 12.448 35.833 1.00 13.21 ATOM 938 C LEU A 127 7.007 13.588 35.175 1.00 15.60 ATOM 939 O LEU A 127 7.158 13.834 33.974 1.00 16.38 ATOM 940 CB LEU A 127 8.044 11.329 34.816 1.00 12.76 ATOM 941 CG LEU A 127 8.849 10.123 35.323 1.00 13.41 ATOM 942 CD1 LEU A 127 8.912 9.062 34.238 1.00 15.61 ATOM 943 CD2 LEU A 127 10.249 10.556 35.719 1.00 14.41 ATOM 944 N GLU A 128 6.194 14.290 35.958 1.00 17.06 ATOM 945 CA GLU A 128 5.409 15.400 35.433 1.00 19.82 ATOM 946 C GLU A 128 6.125 16.732 35.608 1.00 21.81 ATOM 947 O GLU A 128 6.673 17.035 36.666 1.00 21.11 ATOM 948 CB GLU A 128 4.053 15.490 36.140 1.00 20.58 ATOM 949 CG GLU A 128 3.225 14.210 36.138 1.00 22.88 ATOM 950 CD GLU A 128 1.810 14.433 36.658 1.00 26.72 ATOM 951 OE1 GLU A 128 1.653 15.109 37.699 1.00 26.47 ATOM 952 OE2 GLU A 128 0.856 13.929 36.025 1.00 29.78 TER END