ATOM 1 N ALA A 1 26.646 20.523 20.885 0.50 30.87 ATOM 2 CA ALA A 1 26.812 21.196 19.569 0.50 22.24 ATOM 3 C ALA A 1 26.984 22.728 19.737 0.50 18.49 ATOM 4 O ALA A 1 26.416 23.328 20.657 0.50 20.91 ATOM 5 CB ALA A 1 25.642 20.845 18.591 0.50 29.19 ATOM 6 N ASP A 2 27.696 23.329 18.781 1.00 19.56 ATOM 7 CA ASP A 2 28.132 24.718 18.730 1.00 13.71 ATOM 8 C ASP A 2 27.414 25.447 17.559 1.00 11.35 ATOM 9 O ASP A 2 27.880 25.424 16.431 1.00 12.19 ATOM 10 CB ASP A 2 29.668 24.922 18.794 1.00 15.15 ATOM 11 CG ASP A 2 30.090 26.390 18.824 1.00 9.60 ATOM 12 OD1 ASP A 2 31.324 26.637 18.958 1.00 18.64 ATOM 13 OD2 ASP A 2 29.296 27.326 18.749 1.00 13.34 ATOM 14 N GLY A 3 26.263 26.066 17.882 1.00 10.04 ATOM 15 CA GLY A 3 25.472 26.743 16.859 1.00 8.72 ATOM 16 C GLY A 3 26.233 27.855 16.158 1.00 7.59 ATOM 17 O GLY A 3 26.050 28.089 14.965 1.00 8.78 ATOM 18 N LYS A 4 27.070 28.563 16.907 1.00 8.64 ATOM 19 CA LYS A 4 27.869 29.639 16.333 1.00 10.23 ATOM 20 C LYS A 4 28.824 29.116 15.259 1.00 8.93 ATOM 21 O LYS A 4 28.931 29.692 14.178 1.00 9.40 ATOM 22 CB LYS A 4 28.643 30.377 17.426 1.00 11.46 ATOM 23 CG LYS A 4 29.421 31.580 16.929 1.00 14.50 ATOM 24 CD LYS A 4 30.124 32.281 18.078 1.00 19.67 ATOM 25 CE LYS A 4 31.180 33.249 17.574 1.00 23.42 ATOM 26 NZ LYS A 4 31.838 33.970 18.697 1.00 28.37 ATOM 27 N ALA A 5 29.490 28.002 15.547 1.00 9.73 ATOM 28 CA ALA A 5 30.429 27.411 14.597 1.00 10.16 ATOM 29 C ALA A 5 29.730 26.896 13.341 1.00 8.86 ATOM 30 O ALA A 5 30.242 27.042 12.228 1.00 9.89 ATOM 31 CB ALA A 5 31.222 26.296 15.256 1.00 11.88 ATOM 32 N ILE A 6 28.547 26.319 13.518 1.00 8.94 ATOM 33 CA ILE A 6 27.758 25.860 12.381 1.00 9.14 ATOM 34 C ILE A 6 27.362 27.041 11.496 1.00 7.67 ATOM 35 O ILE A 6 27.541 27.011 10.278 1.00 8.81 ATOM 36 CB ILE A 6 26.500 25.098 12.845 1.00 9.54 ATOM 37 CG1 ILE A 6 26.893 23.814 13.581 1.00 12.80 ATOM 38 CG2 ILE A 6 25.594 24.789 11.665 1.00 10.70 ATOM 39 CD ILE A 6 25.754 23.176 14.350 1.00 14.86 ATOM 40 N PHE A 7 26.852 28.094 12.124 1.00 7.56 ATOM 41 CA PHE A 7 26.473 29.309 11.417 1.00 8.11 ATOM 42 C PHE A 7 27.647 29.866 10.609 1.00 8.34 ATOM 43 O PHE A 7 27.486 30.250 9.449 1.00 10.33 ATOM 44 CB PHE A 7 25.970 30.349 12.422 1.00 8.56 ATOM 45 CG PHE A 7 25.427 31.595 11.789 1.00 8.29 ATOM 46 CD1 PHE A 7 24.075 31.715 11.519 1.00 7.56 ATOM 47 CD2 PHE A 7 26.240 32.702 11.613 1.00 8.76 ATOM 48 CE1 PHE A 7 23.558 32.894 11.010 1.00 7.31 ATOM 49 CE2 PHE A 7 25.727 33.880 11.114 1.00 7.50 ATOM 50 CZ PHE A 7 24.386 33.974 10.811 1.00 7.52 ATOM 51 N GLN A 8 28.788 30.025 11.272 0.50 8.35 ATOM 52 CA GLN A 8 29.998 30.513 10.619 0.50 11.02 ATOM 53 C GLN A 8 30.323 29.688 9.378 0.50 9.57 ATOM 54 O GLN A 8 30.581 30.237 8.305 0.50 11.70 ATOM 55 CB GLN A 8 31.180 30.482 11.590 0.50 14.26 ATOM 56 CG GLN A 8 30.844 30.960 12.993 0.50 20.05 ATOM 57 CD GLN A 8 32.078 31.170 13.848 0.50 17.18 ATOM 58 OE1 GLN A 8 32.562 32.293 13.993 0.50 16.89 ATOM 59 NE2 GLN A 8 32.577 30.093 14.445 0.50 15.15 ATOM 60 N GLN A 9 30.311 28.368 9.531 0.50 8.94 ATOM 61 CA GLN A 9 30.996 27.480 8.599 0.50 9.94 ATOM 62 C GLN A 9 30.104 27.120 7.413 0.50 9.03 ATOM 63 O GLN A 9 30.593 26.733 6.351 0.50 9.54 ATOM 64 CB GLN A 9 31.462 26.210 9.316 0.50 9.99 ATOM 65 CG GLN A 9 32.602 26.435 10.298 0.50 14.21 ATOM 66 CD GLN A 9 32.946 25.188 11.091 0.50 12.20 ATOM 67 OE1 GLN A 9 32.575 24.077 10.713 0.50 16.13 ATOM 68 NE2 GLN A 9 33.752 25.357 12.134 0.50 13.49 ATOM 69 N LYS A 10 28.798 27.299 7.585 1.00 8.67 ATOM 70 CA LYS A 10 27.847 27.146 6.492 1.00 9.99 ATOM 71 C LYS A 10 27.656 28.443 5.708 1.00 9.81 ATOM 72 O LYS A 10 26.959 28.465 4.693 1.00 12.88 ATOM 73 CB LYS A 10 26.505 26.614 7.009 1.00 10.41 ATOM 74 CG LYS A 10 26.604 25.301 7.785 1.00 12.49 ATOM 75 CD LYS A 10 27.159 24.176 6.923 1.00 12.53 ATOM 76 CE LYS A 10 27.083 22.830 7.636 1.00 15.00 ATOM 77 NZ LYS A 10 27.858 21.772 6.925 1.00 17.63 ATOM 78 N GLY A 11 28.328 29.507 6.141 1.00 8.17 ATOM 79 CA GLY A 11 28.388 30.748 5.372 1.00 9.38 ATOM 80 C GLY A 11 27.193 31.666 5.562 1.00 8.58 ATOM 81 O GLY A 11 27.007 32.609 4.795 1.00 8.84 ATOM 82 N CYS A 12 26.420 31.434 6.621 1.00 7.03 ATOM 83 CA CYS A 12 25.138 32.113 6.808 1.00 7.04 ATOM 84 C CYS A 12 25.314 33.616 6.982 1.00 7.13 ATOM 85 O CYS A 12 24.396 34.392 6.712 1.00 7.54 ATOM 86 CB CYS A 12 24.404 31.543 8.023 1.00 6.78 ATOM 87 SG CYS A 12 24.198 29.749 8.026 1.00 6.05 ATOM 88 N GLY A 13 26.421 34.001 7.606 1.00 7.60 ATOM 89 CA GLY A 13 26.617 35.382 8.017 1.00 8.71 ATOM 90 C GLY A 13 26.704 36.332 6.842 1.00 8.53 ATOM 91 O GLY A 13 26.547 37.539 7.000 1.00 11.40 ATOM 92 N SER A 14 26.978 35.786 5.661 1.00 9.40 ATOM 93 CA SER A 14 27.106 36.595 4.457 1.00 10.65 ATOM 94 C SER A 14 25.839 37.403 4.176 1.00 9.92 ATOM 95 O SER A 14 25.908 38.490 3.600 1.00 12.03 ATOM 96 CB SER A 14 27.462 35.718 3.254 1.00 12.36 ATOM 97 OG SER A 14 26.502 34.692 3.067 1.00 23.50 ATOM 98 N CYS A 15 24.687 36.861 4.569 1.00 7.01 ATOM 99 CA CYS A 15 23.399 37.516 4.340 1.00 6.32 ATOM 100 C CYS A 15 22.665 37.889 5.623 1.00 6.00 ATOM 101 O CYS A 15 21.564 38.433 5.573 1.00 7.77 ATOM 102 CB CYS A 15 22.496 36.627 3.491 1.00 5.47 ATOM 103 SG CYS A 15 23.179 36.270 1.872 1.00 5.85 ATOM 104 N HSD A 16 23.227 37.490 6.760 1.00 5.66 ATOM 105 CA HSD A 16 22.581 37.670 8.055 1.00 5.04 ATOM 106 C HSD A 16 23.550 38.264 9.061 1.00 6.14 ATOM 107 O HSD A 16 24.235 37.542 9.783 1.00 9.11 ATOM 108 CB HSD A 16 22.050 36.340 8.583 1.00 4.93 ATOM 109 CG HSD A 16 20.944 35.762 7.759 1.00 3.86 ATOM 110 ND1 HSD A 16 19.679 36.310 7.720 1.00 4.04 ATOM 111 CD2 HSD A 16 20.891 34.638 7.003 1.00 3.94 ATOM 112 CE1 HSD A 16 18.902 35.557 6.961 1.00 3.45 ATOM 113 NE2 HSD A 16 19.616 34.545 6.502 1.00 3.31 ATOM 114 N GLN A 17 23.560 39.586 9.142 1.00 5.72 ATOM 115 CA GLN A 17 24.299 40.277 10.181 1.00 6.50 ATOM 116 C GLN A 17 23.473 40.345 11.458 1.00 5.75 ATOM 117 O GLN A 17 22.264 40.104 11.436 1.00 5.89 ATOM 118 CB GLN A 17 24.699 41.668 9.696 1.00 7.53 ATOM 119 CG GLN A 17 25.733 41.616 8.573 1.00 11.89 ATOM 120 CD GLN A 17 25.839 42.907 7.794 1.00 13.70 ATOM 121 OE1 GLN A 17 25.535 43.979 8.312 1.00 14.76 ATOM 122 NE2 GLN A 17 26.409 42.826 6.596 1.00 16.61 ATOM 123 N ALA A 18 24.148 40.517 12.588 1.00 6.43 ATOM 124 CA ALA A 18 23.481 40.413 13.879 1.00 5.97 ATOM 125 C ALA A 18 22.336 41.415 14.003 1.00 5.89 ATOM 126 O ALA A 18 21.242 41.055 14.434 1.00 6.70 ATOM 127 CB ALA A 18 24.474 40.587 15.013 1.00 7.94 ATOM 128 N ASN A 19 22.594 42.669 13.628 1.00 5.81 ATOM 129 CA ASN A 19 21.738 43.784 14.028 1.00 7.24 ATOM 130 C ASN A 19 21.295 44.674 12.870 1.00 6.60 ATOM 131 O ASN A 19 20.733 45.745 13.096 1.00 8.53 ATOM 132 CB ASN A 19 22.431 44.642 15.086 1.00 8.81 ATOM 133 CG ASN A 19 22.774 43.859 16.332 1.00 11.02 ATOM 134 OD1 ASN A 19 23.888 43.953 16.849 1.00 18.70 ATOM 135 ND2 ASN A 19 21.791 43.151 16.873 1.00 12.67 ATOM 136 N VAL A 20 21.583 44.253 11.641 1.00 6.32 ATOM 137 CA VAL A 20 21.219 45.026 10.454 1.00 6.68 ATOM 138 C VAL A 20 20.621 44.102 9.400 1.00 6.22 ATOM 139 O VAL A 20 21.185 43.046 9.111 1.00 6.91 ATOM 140 CB VAL A 20 22.453 45.728 9.834 1.00 8.91 ATOM 141 CG1 VAL A 20 22.026 46.666 8.715 1.00 11.58 ATOM 142 CG2 VAL A 20 23.242 46.475 10.901 1.00 9.64 ATOM 143 N ASP A 21 19.472 44.489 8.849 1.00 6.58 ATOM 144 CA ASP A 21 18.900 43.795 7.695 1.00 6.45 ATOM 145 C ASP A 21 19.770 44.087 6.480 1.00 6.59 ATOM 146 O ASP A 21 20.089 45.239 6.205 1.00 9.23 ATOM 147 CB ASP A 21 17.480 44.292 7.401 1.00 7.85 ATOM 148 CG ASP A 21 16.486 43.963 8.505 1.00 7.83 ATOM 149 OD1 ASP A 21 16.747 43.066 9.333 1.00 7.71 ATOM 150 OD2 ASP A 21 15.425 44.621 8.537 1.00 10.72 ATOM 151 N THR A 22 20.136 43.044 5.744 1.00 6.54 ATOM 152 CA THR A 22 20.884 43.212 4.507 1.00 7.40 ATOM 153 C THR A 22 20.229 42.418 3.380 1.00 6.75 ATOM 154 O THR A 22 19.044 42.603 3.102 1.00 8.89 ATOM 155 CB THR A 22 22.379 42.864 4.683 1.00 8.68 ATOM 156 OG1 THR A 22 22.522 41.502 5.109 1.00 9.37 ATOM 157 CG2 THR A 22 23.011 43.778 5.726 1.00 11.52 ATOM 158 N VAL A 23 20.950 41.464 2.805 1.00 8.09 ATOM 159 CA VAL A 23 20.323 40.547 1.866 1.00 7.86 ATOM 160 C VAL A 23 19.201 39.773 2.557 1.00 7.93 ATOM 161 O VAL A 23 18.073 39.725 2.066 1.00 8.01 ATOM 162 CB VAL A 23 21.348 39.571 1.253 1.00 9.01 ATOM 163 CG1 VAL A 23 20.647 38.523 0.402 1.00 9.83 ATOM 164 CG2 VAL A 23 22.378 40.338 0.431 1.00 14.78 ATOM 165 N GLY A 24 19.489 39.269 3.753 1.00 6.39 ATOM 166 CA GLY A 24 18.467 38.678 4.607 1.00 5.61 ATOM 167 C GLY A 24 18.238 39.497 5.864 1.00 5.04 ATOM 168 O GLY A 24 19.009 40.404 6.179 1.00 5.23 ATOM 169 N PRO A 25 17.201 39.142 6.628 1.00 4.59 ATOM 170 CA PRO A 25 16.910 39.852 7.865 1.00 4.61 ATOM 171 C PRO A 25 18.024 39.676 8.887 1.00 4.22 ATOM 172 O PRO A 25 18.727 38.664 8.883 1.00 4.62 ATOM 173 CB PRO A 25 15.626 39.181 8.361 1.00 5.84 ATOM 174 CG PRO A 25 15.582 37.860 7.649 1.00 9.24 ATOM 175 CD PRO A 25 16.180 38.135 6.313 1.00 4.82 ATOM 176 N SER A 26 18.161 40.647 9.779 1.00 4.55 ATOM 177 CA SER A 26 19.124 40.533 10.860 1.00 4.84 ATOM 178 C SER A 26 18.804 39.326 11.734 1.00 4.28 ATOM 179 O SER A 26 17.651 38.898 11.841 1.00 4.48 ATOM 180 CB SER A 26 19.141 41.803 11.708 1.00 6.30 ATOM 181 OG SER A 26 17.988 41.881 12.524 1.00 6.20 ATOM 182 N LEU A 27 19.817 38.831 12.434 1.00 4.66 ATOM 183 CA LEU A 27 19.584 37.796 13.427 1.00 4.95 ATOM 184 C LEU A 27 18.659 38.275 14.537 1.00 4.89 ATOM 185 O LEU A 27 17.845 37.508 15.046 1.00 4.81 ATOM 186 CB LEU A 27 20.902 37.284 14.003 1.00 5.09 ATOM 187 CG LEU A 27 21.837 36.649 12.978 1.00 5.25 ATOM 188 CD1 LEU A 27 23.110 36.173 13.651 1.00 8.60 ATOM 189 CD2 LEU A 27 21.143 35.508 12.249 1.00 7.42 ATOM 190 N LYS A 28 18.789 39.540 14.917 1.00 4.92 ATOM 191 CA LYS A 28 17.910 40.115 15.927 1.00 5.75 ATOM 192 C LYS A 28 16.445 40.013 15.505 1.00 5.30 ATOM 193 O LYS A 28 15.581 39.612 16.291 1.00 6.02 ATOM 194 CB LYS A 28 18.287 41.573 16.186 1.00 7.57 ATOM 195 CG LYS A 28 17.461 42.246 17.263 1.00 11.93 ATOM 196 CD LYS A 28 17.883 43.695 17.440 1.00 18.36 ATOM 197 CE LYS A 28 18.999 43.825 18.462 1.00 29.25 ATOM 198 NZ LYS A 28 18.473 43.808 19.855 1.00 28.76 ATOM 199 N LYS A 29 16.171 40.351 14.249 1.00 5.10 ATOM 200 CA LYS A 29 14.807 40.318 13.740 1.00 5.80 ATOM 201 C LYS A 29 14.269 38.890 13.691 1.00 4.68 ATOM 202 O LYS A 29 13.117 38.636 14.054 1.00 5.58 ATOM 203 CB LYS A 29 14.743 40.953 12.353 1.00 6.81 ATOM 204 CG LYS A 29 13.363 40.921 11.725 1.00 9.30 ATOM 205 CD LYS A 29 13.323 41.736 10.443 1.00 10.26 ATOM 206 CE LYS A 29 13.122 43.213 10.737 1.00 12.24 ATOM 207 NZ LYS A 29 13.017 44.017 9.487 1.00 14.25 ATOM 208 N ILE A 30 15.100 37.959 13.233 1.00 4.32 ATOM 209 CA ILE A 30 14.705 36.557 13.192 1.00 4.73 ATOM 210 C ILE A 30 14.461 36.018 14.602 1.00 4.05 ATOM 211 O ILE A 30 13.466 35.334 14.856 1.00 4.63 ATOM 212 CB ILE A 30 15.757 35.691 12.469 1.00 4.46 ATOM 213 CG1 ILE A 30 15.910 36.124 11.008 1.00 5.26 ATOM 214 CG2 ILE A 30 15.377 34.224 12.546 1.00 5.29 ATOM 215 CD ILE A 30 17.172 35.594 10.347 1.00 7.09 ATOM 216 N ALA A 31 15.357 36.359 15.523 1.00 4.19 ATOM 217 CA ALA A 31 15.248 35.910 16.906 1.00 4.90 ATOM 218 C ALA A 31 13.961 36.403 17.549 1.00 4.61 ATOM 219 O ALA A 31 13.333 35.686 18.325 1.00 6.41 ATOM 220 CB ALA A 31 16.452 36.378 17.703 1.00 5.51 ATOM 221 N GLN A 32 13.590 37.642 17.253 1.00 5.04 ATOM 222 CA GLN A 32 12.342 38.196 17.756 1.00 6.05 ATOM 223 C GLN A 32 11.127 37.477 17.179 1.00 5.43 ATOM 224 O GLN A 32 10.200 37.127 17.907 1.00 6.82 ATOM 225 CB GLN A 32 12.264 39.687 17.450 1.00 7.37 ATOM 226 CG GLN A 32 13.160 40.543 18.325 1.00 14.88 ATOM 227 CD GLN A 32 12.554 40.819 19.688 1.00 22.81 ATOM 228 OE1 GLN A 32 11.374 40.551 19.919 1.00 25.59 ATOM 229 NE2 GLN A 32 13.393 41.221 20.634 1.00 28.80 ATOM 230 N ALA A 33 11.149 37.225 15.873 1.00 5.50 ATOM 231 CA ALA A 33 10.037 36.547 15.215 1.00 5.76 ATOM 232 C ALA A 33 9.811 35.155 15.791 1.00 6.28 ATOM 233 O ALA A 33 8.674 34.687 15.881 1.00 7.32 ATOM 234 CB ALA A 33 10.272 36.469 13.717 1.00 7.12 ATOM 235 N TYR A 34 10.902 34.474 16.127 1.00 4.89 ATOM 236 CA TYR A 34 10.825 33.090 16.569 1.00 4.99 ATOM 237 C TYR A 34 10.921 32.945 18.089 1.00 5.46 ATOM 238 O TYR A 34 11.061 31.839 18.601 1.00 5.70 ATOM 239 CB TYR A 34 11.905 32.255 15.881 1.00 4.63 ATOM 240 CG TYR A 34 11.553 31.853 14.462 1.00 4.49 ATOM 241 CD1 TYR A 34 10.808 30.706 14.215 1.00 4.85 ATOM 242 CD2 TYR A 34 11.979 32.605 13.373 1.00 4.73 ATOM 243 CE1 TYR A 34 10.520 30.304 12.925 1.00 4.99 ATOM 244 CE2 TYR A 34 11.693 32.209 12.071 1.00 4.52 ATOM 245 CZ TYR A 34 10.984 31.041 11.857 1.00 4.24 ATOM 246 OH TYR A 34 10.758 30.576 10.581 1.00 4.97 ATOM 247 N ALA A 35 10.732 34.042 18.812 1.00 5.77 ATOM 248 CA ALA A 35 10.740 33.988 20.270 1.00 6.43 ATOM 249 C ALA A 35 9.645 33.060 20.778 1.00 7.27 ATOM 250 O ALA A 35 8.477 33.207 20.421 1.00 8.29 ATOM 251 CB ALA A 35 10.568 35.378 20.855 1.00 9.31 ATOM 252 N GLY A 36 10.048 32.039 21.527 1.00 7.20 ATOM 253 CA GLY A 36 9.119 31.036 22.031 1.00 9.46 ATOM 254 C GLY A 36 8.660 30.049 20.973 1.00 7.73 ATOM 255 O GLY A 36 7.761 29.245 21.220 1.00 10.32 ATOM 256 N LYS A 37 9.317 30.077 19.815 1.00 7.92 ATOM 257 CA LYS A 37 8.962 29.210 18.695 1.00 8.10 ATOM 258 C LYS A 37 10.164 28.417 18.197 1.00 7.42 ATOM 259 O LYS A 37 10.356 28.259 16.988 1.00 8.10 ATOM 260 CB LYS A 37 8.394 30.038 17.542 1.00 9.77 ATOM 261 CG LYS A 37 7.128 30.795 17.883 1.00 11.75 ATOM 262 CD LYS A 37 6.602 31.540 16.667 1.00 14.91 ATOM 263 CE LYS A 37 5.213 32.102 16.919 1.00 19.29 ATOM 264 NZ LYS A 37 5.181 32.994 18.108 1.00 25.41 ATOM 265 N GLU A 38 10.974 27.916 19.124 1.00 7.84 ATOM 266 CA GLU A 38 12.177 27.192 18.735 1.00 8.98 ATOM 267 C GLU A 38 11.856 26.009 17.827 1.00 7.31 ATOM 268 O GLU A 38 12.566 25.754 16.856 1.00 7.71 ATOM 269 CB GLU A 38 12.965 26.721 19.954 1.00 11.04 ATOM 270 CG GLU A 38 14.182 25.884 19.590 1.00 17.15 ATOM 271 CD GLU A 38 15.433 26.324 20.316 1.00 12.40 ATOM 272 OE1 GLU A 38 15.381 26.386 21.562 1.00 23.49 ATOM 273 OE2 GLU A 38 16.516 26.264 19.695 1.00 13.92 ATOM 274 N ASP A 39 10.807 25.267 18.160 1.00 8.11 ATOM 275 CA ASP A 39 10.451 24.104 17.359 1.00 7.57 ATOM 276 C ASP A 39 10.149 24.501 15.920 1.00 6.50 ATOM 277 O ASP A 39 10.523 23.796 14.984 1.00 6.61 ATOM 278 CB ASP A 39 9.254 23.371 17.962 1.00 9.38 ATOM 279 CG ASP A 39 9.642 22.480 19.130 1.00 12.80 ATOM 280 OD1 ASP A 39 10.851 22.285 19.370 1.00 16.23 ATOM 281 OD2 ASP A 39 8.730 21.924 19.775 1.00 17.44 ATOM 282 N GLN A 40 9.423 25.599 15.743 1.00 6.84 ATOM 283 CA GLN A 40 9.115 26.073 14.405 1.00 6.22 ATOM 284 C GLN A 40 10.355 26.556 13.656 1.00 5.02 ATOM 285 O GLN A 40 10.459 26.385 12.444 1.00 5.88 ATOM 286 CB GLN A 40 8.044 27.161 14.425 1.00 7.01 ATOM 287 CG GLN A 40 7.482 27.446 13.043 1.00 9.71 ATOM 288 CD GLN A 40 6.363 28.467 13.050 1.00 11.29 ATOM 289 OE1 GLN A 40 5.549 28.502 13.975 1.00 16.05 ATOM 290 NE2 GLN A 40 6.210 29.179 11.935 1.00 12.48 ATOM 291 N LEU A 41 11.298 27.159 14.374 1.00 5.14 ATOM 292 CA LEU A 41 12.550 27.573 13.749 1.00 4.61 ATOM 293 C LEU A 41 13.334 26.360 13.252 1.00 4.08 ATOM 294 O LEU A 41 13.838 26.351 12.129 1.00 4.79 ATOM 295 CB LEU A 41 13.394 28.410 14.711 1.00 4.60 ATOM 296 CG LEU A 41 14.736 28.925 14.177 1.00 4.85 ATOM 297 CD1 LEU A 41 14.564 29.626 12.839 1.00 5.18 ATOM 298 CD2 LEU A 41 15.366 29.859 15.199 1.00 4.90 ATOM 299 N ILE A 42 13.364 25.304 14.057 1.00 4.98 ATOM 300 CA ILE A 42 13.994 24.065 13.622 1.00 5.46 ATOM 301 C ILE A 42 13.293 23.486 12.391 1.00 4.91 ATOM 302 O ILE A 42 13.945 23.096 11.419 1.00 5.26 ATOM 303 CB ILE A 42 14.056 23.029 14.760 1.00 6.02 ATOM 304 CG1 ILE A 42 14.995 23.523 15.866 1.00 8.05 ATOM 305 CG2 ILE A 42 14.502 21.673 14.228 1.00 6.94 ATOM 306 CD ILE A 42 14.807 22.819 17.191 1.00 9.36 ATOM 307 N LYS A 43 11.963 23.486 12.406 1.00 5.37 ATOM 308 CA LYS A 43 11.201 23.058 11.237 1.00 6.03 ATOM 309 C LYS A 43 11.539 23.899 10.007 1.00 4.33 ATOM 310 O LYS A 43 11.719 23.365 8.910 1.00 6.26 ATOM 311 CB LYS A 43 9.699 23.098 11.516 1.00 6.92 ATOM 312 CG LYS A 43 9.196 21.957 12.381 1.00 11.06 ATOM 313 CD LYS A 43 7.691 22.045 12.577 1.00 19.51 ATOM 314 CE LYS A 43 6.946 21.609 11.328 1.00 26.23 ATOM 315 NZ LYS A 43 6.423 20.220 11.456 1.00 36.26 ATOM 316 N PHE A 44 11.614 25.215 10.181 1.00 4.75 ATOM 317 CA PHE A 44 11.982 26.080 9.073 1.00 4.64 ATOM 318 C PHE A 44 13.335 25.673 8.502 1.00 3.57 ATOM 319 O PHE A 44 13.509 25.586 7.284 1.00 4.65 ATOM 320 CB PHE A 44 12.013 27.548 9.489 1.00 4.63 ATOM 321 CG PHE A 44 12.517 28.458 8.409 1.00 3.94 ATOM 322 CD1 PHE A 44 11.678 28.833 7.370 1.00 4.87 ATOM 323 CD2 PHE A 44 13.878 28.707 8.284 1.00 4.27 ATOM 324 CE1 PHE A 44 12.179 29.463 6.244 1.00 5.04 ATOM 325 CE2 PHE A 44 14.386 29.319 7.153 1.00 4.52 ATOM 326 CZ PHE A 44 13.535 29.699 6.135 1.00 5.16 ATOM 327 N LEU A 45 14.297 25.435 9.387 1.00 3.96 ATOM 328 CA LEU A 45 15.651 25.096 8.973 1.00 4.72 ATOM 329 C LEU A 45 15.714 23.768 8.227 1.00 4.37 ATOM 330 O LEU A 45 16.634 23.538 7.443 1.00 5.35 ATOM 331 CB LEU A 45 16.592 25.081 10.174 1.00 4.51 ATOM 332 CG LEU A 45 16.822 26.443 10.829 1.00 4.87 ATOM 333 CD1 LEU A 45 17.544 26.280 12.158 1.00 6.79 ATOM 334 CD2 LEU A 45 17.589 27.372 9.892 1.00 5.85 ATOM 335 N LYS A 46 14.708 22.923 8.436 1.00 4.99 ATOM 336 CA LYS A 46 14.605 21.642 7.742 1.00 6.22 ATOM 337 C LYS A 46 13.846 21.735 6.421 1.00 6.40 ATOM 338 O LYS A 46 13.716 20.741 5.710 1.00 8.53 ATOM 339 CB LYS A 46 13.936 20.608 8.645 1.00 6.21 ATOM 340 CG LYS A 46 14.788 20.181 9.822 1.00 8.99 ATOM 341 CD LYS A 46 14.069 19.144 10.668 1.00 15.59 ATOM 342 CE LYS A 46 14.093 17.775 10.003 1.00 24.76 ATOM 343 NZ LYS A 46 14.966 16.814 10.732 1.00 21.58 ATOM 344 N GLY A 47 13.303 22.910 6.117 1.00 6.05 ATOM 345 CA GLY A 47 12.433 23.068 4.955 1.00 7.91 ATOM 346 C GLY A 47 10.984 22.695 5.222 1.00 9.64 ATOM 347 O GLY A 47 10.202 22.531 4.289 1.00 14.19 ATOM 348 N GLU A 48 10.597 22.748 6.494 0.50 10.95 ATOM 349 CA GLU A 48 9.381 22.096 6.969 0.50 11.93 ATOM 350 C GLU A 48 8.307 23.118 7.340 0.50 11.09 ATOM 351 O GLU A 48 7.208 22.746 7.750 0.50 11.33 ATOM 352 CB GLU A 48 9.688 21.208 8.180 0.50 12.59 ATOM 353 CG GLU A 48 10.089 19.785 7.832 0.50 10.81 ATOM 354 CD GLU A 48 10.456 18.966 9.056 0.50 16.03 ATOM 355 OE1 GLU A 48 11.204 17.978 8.907 0.50 13.25 ATOM 356 OE2 GLU A 48 10.048 19.345 10.174 0.50 19.63 ATOM 357 N ALA A 49 8.696 24.389 7.380 1.00 7.25 ATOM 358 CA ALA A 49 7.804 25.450 7.838 1.00 7.28 ATOM 359 C ALA A 49 7.981 26.670 6.946 1.00 6.99 ATOM 360 O ALA A 49 9.051 26.866 6.364 1.00 7.59 ATOM 361 CB ALA A 49 8.101 25.807 9.291 1.00 7.81 ATOM 362 N PRO A 50 6.932 27.500 6.839 1.00 7.62 ATOM 363 CA PRO A 50 6.950 28.629 5.917 1.00 8.56 ATOM 364 C PRO A 50 7.797 29.772 6.459 1.00 6.92 ATOM 365 O PRO A 50 7.900 29.947 7.673 1.00 7.64 ATOM 366 CB PRO A 50 5.480 29.050 5.859 1.00 11.58 ATOM 367 CG PRO A 50 4.941 28.665 7.189 1.00 11.52 ATOM 368 CD PRO A 50 5.646 27.386 7.549 1.00 9.60 ATOM 369 N ALA A 51 8.280 30.627 5.566 1.00 6.63 ATOM 370 CA ALA A 51 8.882 31.885 5.985 1.00 5.65 ATOM 371 C ALA A 51 7.861 32.752 6.708 1.00 5.78 ATOM 372 O ALA A 51 6.752 32.953 6.212 1.00 8.19 ATOM 373 CB ALA A 51 9.444 32.626 4.784 1.00 6.24 ATOM 374 N ILE A 52 8.251 33.285 7.864 1.00 5.67 ATOM 375 CA ILE A 52 7.399 34.197 8.614 1.00 5.84 ATOM 376 C ILE A 52 7.999 35.592 8.755 1.00 6.33 ATOM 377 O ILE A 52 7.323 36.511 9.209 1.00 9.60 ATOM 378 CB ILE A 52 7.039 33.644 10.012 1.00 6.34 ATOM 379 CG1 ILE A 52 8.289 33.459 10.878 1.00 7.03 ATOM 380 CG2 ILE A 52 6.267 32.350 9.881 1.00 8.63 ATOM 381 CD ILE A 52 7.987 33.103 12.330 1.00 8.26 ATOM 382 N VAL A 53 9.253 35.760 8.340 1.00 4.73 ATOM 383 CA VAL A 53 9.930 37.044 8.495 1.00 5.69 ATOM 384 C VAL A 53 9.859 37.900 7.231 1.00 5.16 ATOM 385 O VAL A 53 9.348 39.016 7.263 1.00 8.16 ATOM 386 CB VAL A 53 11.401 36.880 8.941 1.00 5.59 ATOM 387 CG1 VAL A 53 12.032 38.244 9.182 1.00 7.83 ATOM 388 CG2 VAL A 53 11.488 36.018 10.195 1.00 7.17 ATOM 389 N ASP A 54 10.303 37.343 6.109 1.00 6.14 ATOM 390 CA ASP A 54 10.309 38.069 4.843 1.00 6.32 ATOM 391 C ASP A 54 9.813 37.179 3.706 1.00 6.72 ATOM 392 O ASP A 54 10.594 36.741 2.863 1.00 7.42 ATOM 393 CB ASP A 54 11.712 38.597 4.540 1.00 7.46 ATOM 394 CG ASP A 54 11.756 39.479 3.311 1.00 10.33 ATOM 395 OD1 ASP A 54 10.682 39.823 2.779 1.00 15.84 ATOM 396 OD2 ASP A 54 12.875 39.817 2.871 1.00 11.16 ATOM 397 N PRO A 55 8.502 36.903 3.682 1.00 6.75 ATOM 398 CA PRO A 55 7.962 35.977 2.689 1.00 6.63 ATOM 399 C PRO A 55 8.226 36.412 1.245 1.00 6.23 ATOM 400 O PRO A 55 8.288 35.567 0.356 1.00 7.16 ATOM 401 CB PRO A 55 6.461 35.972 2.989 1.00 7.99 ATOM 402 CG PRO A 55 6.358 36.344 4.425 1.00 12.55 ATOM 403 CD PRO A 55 7.506 37.275 4.703 1.00 7.40 ATOM 404 N ALA A 56 8.391 37.711 1.012 1.00 6.05 ATOM 405 CA ALA A 56 8.676 38.208 -0.336 1.00 6.75 ATOM 406 C ALA A 56 9.920 37.556 -0.938 1.00 5.74 ATOM 407 O ALA A 56 10.040 37.444 -2.158 1.00 7.65 ATOM 408 CB ALA A 56 8.821 39.723 -0.331 1.00 6.61 ATOM 409 N LYS A 57 10.861 37.173 -0.080 0.50 5.81 ATOM 410 CA LYS A 57 12.136 36.624 -0.533 0.50 6.52 ATOM 411 C LYS A 57 12.362 35.207 -0.015 0.50 6.30 ATOM 412 O LYS A 57 13.490 34.714 0.006 0.50 6.04 ATOM 413 CB LYS A 57 13.289 37.539 -0.118 0.50 7.41 ATOM 414 CG LYS A 57 13.090 38.992 -0.522 0.50 9.60 ATOM 415 CD LYS A 57 14.409 39.747 -0.564 0.50 9.85 ATOM 416 CE LYS A 57 14.343 40.915 -1.537 0.50 11.24 ATOM 417 NZ LYS A 57 15.444 41.895 -1.314 0.50 13.50 ATOM 418 N GLU A 58 11.265 34.509 0.255 1.00 5.34 ATOM 419 CA GLU A 58 11.317 33.124 0.702 1.00 6.50 ATOM 420 C GLU A 58 12.116 32.222 -0.235 1.00 5.37 ATOM 421 O GLU A 58 12.896 31.382 0.216 1.00 6.02 ATOM 422 CB GLU A 58 9.891 32.600 0.873 1.00 7.56 ATOM 423 CG GLU A 58 9.783 31.209 1.469 1.00 8.91 ATOM 424 CD GLU A 58 8.391 30.915 2.000 1.00 8.73 ATOM 425 OE1 GLU A 58 7.479 31.738 1.768 1.00 10.73 ATOM 426 OE2 GLU A 58 8.218 29.888 2.694 1.00 8.62 ATOM 427 N ALA A 59 11.938 32.407 -1.538 1.00 6.60 ATOM 428 CA ALA A 59 12.539 31.508 -2.516 1.00 6.96 ATOM 429 C ALA A 59 14.049 31.716 -2.635 1.00 7.66 ATOM 430 O ALA A 59 14.761 30.844 -3.128 1.00 8.15 ATOM 431 CB ALA A 59 11.864 31.667 -3.875 1.00 10.04 ATOM 432 N ILE A 60 14.532 32.880 -2.210 1.00 7.10 ATOM 433 CA ILE A 60 15.970 33.152 -2.205 1.00 7.77 ATOM 434 C ILE A 60 16.660 32.379 -1.087 1.00 6.01 ATOM 435 O ILE A 60 17.765 31.861 -1.253 1.00 7.17 ATOM 436 CB ILE A 60 16.259 34.649 -2.012 1.00 9.30 ATOM 437 CG1 ILE A 60 15.748 35.452 -3.207 1.00 16.97 ATOM 438 CG2 ILE A 60 17.750 34.885 -1.803 1.00 14.94 ATOM 439 CD ILE A 60 15.868 36.949 -3.029 1.00 26.56 ATOM 440 N MET A 61 16.024 32.353 0.076 1.00 5.49 ATOM 441 CA MET A 61 16.593 31.688 1.239 1.00 5.25 ATOM 442 C MET A 61 16.494 30.166 1.147 1.00 4.99 ATOM 443 O MET A 61 17.360 29.451 1.648 1.00 5.65 ATOM 444 CB MET A 61 15.924 32.207 2.511 1.00 4.85 ATOM 445 CG MET A 61 16.289 31.450 3.768 1.00 4.21 ATOM 446 SD MET A 61 18.067 31.362 4.065 1.00 3.47 ATOM 447 CE MET A 61 18.139 29.821 4.973 1.00 4.90 ATOM 448 N LYS A 62 15.430 29.668 0.528 1.00 5.05 ATOM 449 CA LYS A 62 15.151 28.241 0.563 1.00 5.63 ATOM 450 C LYS A 62 16.340 27.358 0.172 1.00 4.82 ATOM 451 O LYS A 62 16.647 26.398 0.874 1.00 5.51 ATOM 452 CB LYS A 62 13.914 27.889 -0.257 1.00 7.75 ATOM 453 CG LYS A 62 13.603 26.405 -0.234 1.00 7.99 ATOM 454 CD LYS A 62 12.235 26.103 -0.807 1.00 10.00 ATOM 455 CE LYS A 62 12.136 26.580 -2.243 1.00 11.74 ATOM 456 NZ LYS A 62 10.818 26.239 -2.836 1.00 15.45 ATOM 457 N PRO A 63 17.024 27.674 -0.945 1.00 5.28 ATOM 458 CA PRO A 63 18.092 26.758 -1.351 1.00 6.11 ATOM 459 C PRO A 63 19.224 26.669 -0.326 1.00 5.47 ATOM 460 O PRO A 63 19.917 25.655 -0.269 1.00 6.06 ATOM 461 CB PRO A 63 18.600 27.343 -2.679 1.00 8.01 ATOM 462 CG PRO A 63 17.966 28.681 -2.809 1.00 12.16 ATOM 463 CD PRO A 63 16.717 28.666 -1.987 1.00 6.26 ATOM 464 N GLN A 64 19.417 27.716 0.473 1.00 5.38 ATOM 465 CA GLN A 64 20.454 27.700 1.505 1.00 5.56 ATOM 466 C GLN A 64 20.229 26.584 2.521 1.00 5.47 ATOM 467 O GLN A 64 21.168 26.121 3.171 1.00 6.76 ATOM 468 CB GLN A 64 20.534 29.051 2.217 1.00 6.51 ATOM 469 CG GLN A 64 20.944 30.200 1.316 1.00 5.71 ATOM 470 CD GLN A 64 22.347 30.028 0.757 1.00 6.06 ATOM 471 OE1 GLN A 64 23.258 29.592 1.461 1.00 7.34 ATOM 472 NE2 GLN A 64 22.538 30.424 -0.495 1.00 7.68 ATOM 473 N LEU A 65 18.983 26.144 2.649 1.00 5.20 ATOM 474 CA LEU A 65 18.650 25.095 3.602 1.00 5.64 ATOM 475 C LEU A 65 19.296 23.759 3.244 1.00 5.76 ATOM 476 O LEU A 65 19.477 22.897 4.103 1.00 6.89 ATOM 477 CB LEU A 65 17.137 24.946 3.720 1.00 5.84 ATOM 478 CG LEU A 65 16.421 26.192 4.246 1.00 5.93 ATOM 479 CD1 LEU A 65 14.914 25.980 4.279 1.00 6.89 ATOM 480 CD2 LEU A 65 16.953 26.572 5.626 1.00 6.58 ATOM 481 N THR A 66 19.653 23.592 1.976 0.50 6.50 ATOM 482 CA THR A 66 20.237 22.337 1.520 0.50 7.00 ATOM 483 C THR A 66 21.573 22.056 2.205 0.50 9.05 ATOM 484 O THR A 66 21.945 20.900 2.406 0.50 10.20 ATOM 485 CB THR A 66 20.428 22.324 -0.007 0.50 7.36 ATOM 486 OG1 THR A 66 21.491 23.215 -0.369 0.50 5.67 ATOM 487 CG2 THR A 66 19.147 22.753 -0.707 0.50 10.57 ATOM 488 N MET A 67 22.251 23.117 2.632 0.50 8.27 ATOM 489 CA MET A 67 23.512 22.990 3.357 0.50 8.81 ATOM 490 C MET A 67 23.348 22.180 4.634 0.50 11.44 ATOM 491 O MET A 67 24.335 21.712 5.201 0.50 15.48 ATOM 492 CB MET A 67 24.059 24.369 3.711 0.50 10.32 ATOM 493 CG MET A 67 24.469 25.193 2.518 0.50 11.71 ATOM 494 SD MET A 67 25.477 26.586 3.032 0.50 10.54 ATOM 495 CE MET A 67 25.932 27.257 1.439 0.50 9.24 ATOM 496 N LEU A 68 22.178 22.324 5.243 1.00 7.07 ATOM 497 CA LEU A 68 21.960 21.865 6.607 1.00 7.20 ATOM 498 C LEU A 68 21.558 20.390 6.686 1.00 7.31 ATOM 499 O LEU A 68 21.236 19.890 7.762 1.00 8.18 ATOM 500 CB LEU A 68 20.908 22.739 7.300 1.00 6.11 ATOM 501 CG LEU A 68 21.195 24.242 7.316 1.00 7.13 ATOM 502 CD1 LEU A 68 20.075 24.985 8.020 1.00 6.99 ATOM 503 CD2 LEU A 68 22.540 24.537 7.969 1.00 8.07 ATOM 504 N LYS A 69 21.571 19.702 5.547 0.50 9.03 ATOM 505 CA LYS A 69 21.027 18.346 5.467 0.50 8.74 ATOM 506 C LYS A 69 21.980 17.287 6.023 0.50 7.68 ATOM 507 O LYS A 69 21.619 16.115 6.134 0.50 10.29 ATOM 508 CB LYS A 69 20.637 18.001 4.027 0.50 9.17 ATOM 509 CG LYS A 69 19.607 18.941 3.418 0.50 8.38 ATOM 510 CD LYS A 69 18.243 18.779 4.071 0.50 7.74 ATOM 511 CE LYS A 69 17.163 19.463 3.252 0.50 6.40 ATOM 512 NZ LYS A 69 16.054 19.953 4.108 0.50 6.72 ATOM 513 N GLY A 70 23.165 17.719 6.444 1.00 7.74 ATOM 514 CA GLY A 70 24.106 16.841 7.130 1.00 7.73 ATOM 515 C GLY A 70 24.066 16.968 8.640 1.00 6.87 ATOM 516 O GLY A 70 24.836 16.312 9.340 1.00 8.67 ATOM 517 N LEU A 71 23.202 17.847 9.140 1.00 6.70 ATOM 518 CA LEU A 71 23.122 18.126 10.573 1.00 6.58 ATOM 519 C LEU A 71 22.121 17.210 11.261 1.00 6.64 ATOM 520 O LEU A 71 21.025 16.977 10.752 1.00 7.67 ATOM 521 CB LEU A 71 22.729 19.581 10.822 1.00 7.00 ATOM 522 CG LEU A 71 23.686 20.636 10.275 1.00 7.87 ATOM 523 CD1 LEU A 71 23.212 22.023 10.667 1.00 10.63 ATOM 524 CD2 LEU A 71 25.104 20.398 10.764 1.00 9.23 ATOM 525 N SER A 72 22.454 16.795 12.476 1.00 6.26 ATOM 526 CA SER A 72 21.494 16.119 13.336 1.00 6.91 ATOM 527 C SER A 72 20.440 17.104 13.828 1.00 7.40 ATOM 528 O SER A 72 20.648 18.319 13.798 1.00 6.01 ATOM 529 CB SER A 72 22.215 15.508 14.530 1.00 7.87 ATOM 530 OG SER A 72 22.670 16.536 15.392 1.00 7.35 ATOM 531 N ASP A 73 19.375 16.576 14.419 1.00 7.74 ATOM 532 CA ASP A 73 18.366 17.432 15.023 1.00 9.06 ATOM 533 C ASP A 73 18.925 18.242 16.193 1.00 8.01 ATOM 534 O ASP A 73 18.584 19.411 16.365 1.00 7.68 ATOM 535 CB ASP A 73 17.153 16.610 15.462 1.00 11.15 ATOM 536 CG ASP A 73 16.281 16.188 14.293 1.00 15.99 ATOM 537 OD1 ASP A 73 16.532 16.650 13.159 1.00 14.44 ATOM 538 OD2 ASP A 73 15.372 15.359 14.500 1.00 22.22 ATOM 539 N ALA A 74 19.861 17.657 16.933 1.00 7.69 ATOM 540 CA ALA A 74 20.523 18.384 18.015 1.00 8.14 ATOM 541 C ALA A 74 21.363 19.544 17.482 1.00 6.61 ATOM 542 O ALA A 74 21.421 20.615 18.087 1.00 6.72 ATOM 543 CB ALA A 74 21.378 17.444 18.845 1.00 10.21 ATOM 544 N GLU A 75 22.026 19.322 16.355 1.00 5.60 ATOM 545 CA GLU A 75 22.818 20.374 15.728 1.00 5.00 ATOM 546 C GLU A 75 21.948 21.482 15.148 1.00 5.01 ATOM 547 O GLU A 75 22.256 22.667 15.295 1.00 5.66 ATOM 548 CB GLU A 75 23.745 19.792 14.664 1.00 5.66 ATOM 549 CG GLU A 75 24.882 19.000 15.269 1.00 7.59 ATOM 550 CD GLU A 75 25.686 18.236 14.244 1.00 9.25 ATOM 551 OE1 GLU A 75 25.099 17.712 13.276 1.00 8.03 ATOM 552 OE2 GLU A 75 26.897 18.054 14.482 1.00 17.42 ATOM 553 N LEU A 76 20.820 21.102 14.561 1.00 5.37 ATOM 554 CA LEU A 76 19.857 22.089 14.098 1.00 5.16 ATOM 555 C LEU A 76 19.316 22.917 15.255 1.00 5.17 ATOM 556 O LEU A 76 19.149 24.129 15.136 1.00 5.62 ATOM 557 CB LEU A 76 18.708 21.415 13.352 1.00 6.21 ATOM 558 CG LEU A 76 19.085 20.837 11.989 1.00 6.33 ATOM 559 CD1 LEU A 76 18.030 19.851 11.519 1.00 10.98 ATOM 560 CD2 LEU A 76 19.279 21.946 10.966 1.00 9.05 ATOM 561 N LYS A 77 19.063 22.262 16.382 1.00 5.12 ATOM 562 CA LYS A 77 18.628 22.969 17.577 1.00 6.38 ATOM 563 C LYS A 77 19.689 23.950 18.072 1.00 5.65 ATOM 564 O LYS A 77 19.374 25.082 18.438 1.00 5.94 ATOM 565 CB LYS A 77 18.243 21.991 18.685 1.00 6.51 ATOM 566 CG LYS A 77 17.742 22.679 19.936 1.00 9.13 ATOM 567 CD LYS A 77 17.404 21.661 21.007 1.00 13.20 ATOM 568 CE LYS A 77 16.879 22.333 22.265 1.00 20.32 ATOM 569 NZ LYS A 77 17.836 23.341 22.802 1.00 25.39 ATOM 570 N ALA A 78 20.949 23.529 18.056 1.00 5.61 ATOM 571 CA ALA A 78 22.037 24.415 18.461 1.00 6.32 ATOM 572 C ALA A 78 22.128 25.642 17.550 1.00 5.27 ATOM 573 O ALA A 78 22.335 26.759 18.016 1.00 5.34 ATOM 574 CB ALA A 78 23.358 23.661 18.486 1.00 7.82 ATOM 575 N LEU A 79 21.980 25.425 16.248 1.00 5.31 ATOM 576 CA LEU A 79 21.947 26.518 15.283 1.00 4.92 ATOM 577 C LEU A 79 20.770 27.461 15.544 1.00 4.60 ATOM 578 O LEU A 79 20.938 28.681 15.603 1.00 4.94 ATOM 579 CB LEU A 79 21.871 25.948 13.865 1.00 5.20 ATOM 580 CG LEU A 79 21.743 26.944 12.716 1.00 5.35 ATOM 581 CD1 LEU A 79 22.898 27.928 12.708 1.00 6.67 ATOM 582 CD2 LEU A 79 21.661 26.200 11.395 1.00 6.26 ATOM 583 N ALA A 80 19.601 26.885 15.803 1.00 4.82 ATOM 584 CA ALA A 80 18.431 27.673 16.164 1.00 4.61 ATOM 585 C ALA A 80 18.664 28.486 17.434 1.00 4.73 ATOM 586 O ALA A 80 18.339 29.671 17.482 1.00 5.75 ATOM 587 CB ALA A 80 17.217 26.779 16.322 1.00 5.43 ATOM 588 N ASP A 81 19.339 27.896 18.411 0.50 4.36 ATOM 589 CA ASP A 81 19.498 28.562 19.696 0.50 6.25 ATOM 590 C ASP A 81 20.557 29.657 19.633 0.50 5.09 ATOM 591 O ASP A 81 20.394 30.714 20.244 0.50 4.54 ATOM 592 CB ASP A 81 19.819 27.554 20.797 0.50 5.68 ATOM 593 CG ASP A 81 18.622 26.702 21.175 0.50 8.29 ATOM 594 OD1 ASP A 81 18.832 25.574 21.658 0.50 6.52 ATOM 595 OD2 ASP A 81 17.481 27.087 20.838 0.50 7.75 ATOM 596 N PHE A 82 21.496 29.510 18.702 1.00 5.20 ATOM 597 CA PHE A 82 22.420 30.594 18.396 1.00 6.45 ATOM 598 C PHE A 82 21.694 31.776 17.760 1.00 4.79 ATOM 599 O PHE A 82 21.879 32.924 18.159 1.00 5.65 ATOM 600 CB PHE A 82 23.553 30.112 17.484 1.00 6.07 ATOM 601 CG PHE A 82 24.430 31.222 16.974 1.00 7.04 ATOM 602 CD1 PHE A 82 25.301 31.879 17.827 1.00 9.34 ATOM 603 CD2 PHE A 82 24.307 31.674 15.672 1.00 8.51 ATOM 604 CE1 PHE A 82 26.060 32.945 17.378 1.00 11.50 ATOM 605 CE2 PHE A 82 25.082 32.719 15.211 1.00 10.40 ATOM 606 CZ PHE A 82 25.961 33.350 16.065 1.00 12.56 ATOM 607 N ILE A 83 20.842 31.495 16.784 1.00 4.91 ATOM 608 CA ILE A 83 20.047 32.551 16.176 1.00 4.72 ATOM 609 C ILE A 83 19.190 33.249 17.231 1.00 4.17 ATOM 610 O ILE A 83 19.235 34.471 17.369 1.00 4.73 ATOM 611 CB ILE A 83 19.163 32.007 15.036 1.00 5.38 ATOM 612 CG1 ILE A 83 20.039 31.497 13.887 1.00 5.60 ATOM 613 CG2 ILE A 83 18.201 33.080 14.550 1.00 7.12 ATOM 614 CD ILE A 83 19.294 30.650 12.872 1.00 7.94 ATOM 615 N LEU A 84 18.481 32.461 18.029 1.00 4.27 ATOM 616 CA LEU A 84 17.550 32.972 19.026 1.00 4.31 ATOM 617 C LEU A 84 18.218 33.814 20.100 1.00 4.82 ATOM 618 O LEU A 84 17.578 34.674 20.702 1.00 6.09 ATOM 619 CB LEU A 84 16.771 31.825 19.661 1.00 4.80 ATOM 620 CG LEU A 84 15.738 31.173 18.741 1.00 5.25 ATOM 621 CD1 LEU A 84 15.347 29.802 19.251 1.00 7.06 ATOM 622 CD2 LEU A 84 14.513 32.066 18.603 1.00 7.15 ATOM 623 N SER A 85 19.514 33.606 20.299 1.00 5.26 ATOM 624 CA SER A 85 20.252 34.319 21.335 1.00 6.08 ATOM 625 C SER A 85 20.428 35.803 21.020 1.00 7.18 ATOM 626 O SER A 85 20.895 36.560 21.865 1.00 8.90 ATOM 627 CB SER A 85 21.612 33.666 21.574 1.00 7.15 ATOM 628 OG SER A 85 22.519 33.978 20.531 1.00 8.20 ATOM 629 N HSD A 86 20.090 36.204 19.796 1.00 6.46 ATOM 630 CA HSD A 86 20.295 37.580 19.342 1.00 8.05 ATOM 631 C HSD A 86 19.090 38.475 19.617 1.00 10.44 ATOM 632 O HSD A 86 19.022 39.595 19.105 1.00 16.05 ATOM 633 CB HSD A 86 20.602 37.609 17.845 1.00 8.51 ATOM 634 CG HSD A 86 21.920 37.000 17.488 1.00 7.14 ATOM 635 ND1 HSD A 86 22.097 35.640 17.350 1.00 7.70 ATOM 636 CD2 HSD A 86 23.141 37.558 17.312 1.00 8.97 ATOM 637 CE1 HSD A 86 23.380 35.383 17.169 1.00 9.68 ATOM 638 NE2 HSD A 86 24.028 36.531 17.098 1.00 10.12 TER END