ATOM 1 N GLU A 1 41.386 11.870 27.422 0.50 19.34 ATOM 2 CA GLU A 1 41.961 12.710 28.498 0.50 18.64 ATOM 3 C GLU A 1 41.800 12.051 29.848 0.50 17.30 ATOM 4 O GLU A 1 40.778 11.452 30.188 0.50 17.74 ATOM 5 CB GLU A 1 41.304 14.087 28.598 0.50 20.16 ATOM 6 CG GLU A 1 40.982 14.790 27.321 0.50 22.85 ATOM 7 CD GLU A 1 39.641 15.483 27.427 0.50 26.44 ATOM 8 OE1 GLU A 1 38.633 14.898 26.968 0.50 28.82 ATOM 9 OE2 GLU A 1 39.586 16.578 28.025 0.50 27.81 ATOM 10 N ARG A 2 42.841 12.228 30.653 0.16 16.07 ATOM 11 CA ARG A 2 42.866 11.726 32.014 0.16 15.04 ATOM 12 C ARG A 2 43.431 12.769 32.971 0.16 14.48 ATOM 13 O ARG A 2 44.050 13.744 32.543 0.16 14.76 ATOM 14 CB ARG A 2 43.672 10.433 32.064 0.16 14.74 ATOM 15 CG ARG A 2 42.998 9.311 31.286 0.16 13.98 ATOM 16 CD ARG A 2 43.963 8.230 30.892 0.16 13.00 ATOM 17 NE ARG A 2 44.590 7.639 32.057 0.16 11.99 ATOM 18 CZ ARG A 2 44.124 6.596 32.733 0.16 10.44 ATOM 19 NH1 ARG A 2 42.993 5.963 32.394 0.16 10.31 ATOM 20 NH2 ARG A 2 44.815 6.194 33.775 0.16 9.43 ATOM 21 N ASP A 3 43.189 12.572 34.264 1.00 13.76 ATOM 22 CA ASP A 3 43.614 13.512 35.279 1.00 14.93 ATOM 23 C ASP A 3 44.248 12.817 36.458 1.00 13.95 ATOM 24 O ASP A 3 44.469 11.617 36.436 1.00 13.76 ATOM 25 CB ASP A 3 42.467 14.435 35.680 1.00 15.66 ATOM 26 CG ASP A 3 41.327 13.713 36.361 1.00 16.04 ATOM 27 OD1 ASP A 3 41.526 12.577 36.854 1.00 15.19 ATOM 28 OD2 ASP A 3 40.209 14.296 36.358 1.00 18.05 ATOM 29 N ALA A 4 44.563 13.576 37.507 1.00 15.53 ATOM 30 CA ALA A 4 45.285 13.036 38.635 1.00 15.11 ATOM 31 C ALA A 4 44.461 11.952 39.341 1.00 14.00 ATOM 32 O ALA A 4 45.032 11.072 39.978 1.00 15.35 ATOM 33 CB ALA A 4 45.649 14.151 39.607 1.00 17.80 ATOM 34 N PHE A 5 43.129 11.984 39.226 1.00 13.88 ATOM 35 CA PHE A 5 42.324 10.977 39.866 1.00 12.70 ATOM 36 C PHE A 5 42.464 9.686 39.079 1.00 12.18 ATOM 37 O PHE A 5 42.563 8.620 39.670 1.00 12.38 ATOM 38 CB PHE A 5 40.834 11.406 39.943 1.00 13.65 ATOM 39 CG PHE A 5 40.016 10.534 40.841 1.00 12.32 ATOM 40 CD1 PHE A 5 40.007 10.799 42.197 1.00 12.96 ATOM 41 CD2 PHE A 5 39.316 9.413 40.351 1.00 11.24 ATOM 42 CE1 PHE A 5 39.297 10.002 43.048 1.00 12.95 ATOM 43 CE2 PHE A 5 38.662 8.590 41.234 1.00 11.47 ATOM 44 CZ PHE A 5 38.672 8.882 42.572 1.00 12.09 ATOM 45 N ASP A 6 42.492 9.756 37.734 1.00 11.87 ATOM 46 CA ASP A 6 42.817 8.572 36.962 1.00 11.53 ATOM 47 C ASP A 6 44.167 8.021 37.381 1.00 11.56 ATOM 48 O ASP A 6 44.332 6.833 37.535 1.00 12.70 ATOM 49 CB ASP A 6 42.838 8.878 35.481 1.00 11.09 ATOM 50 CG ASP A 6 41.495 9.243 34.965 1.00 11.94 ATOM 51 OD1 ASP A 6 40.588 8.371 34.965 1.00 13.59 ATOM 52 OD2 ASP A 6 41.308 10.391 34.581 1.00 13.81 ATOM 53 N THR A 7 45.162 8.896 37.518 1.00 12.35 ATOM 54 CA THR A 7 46.502 8.425 37.846 1.00 12.88 ATOM 55 C THR A 7 46.542 7.722 39.175 1.00 12.57 ATOM 56 O THR A 7 47.107 6.646 39.296 1.00 14.29 ATOM 57 CB THR A 7 47.510 9.567 37.817 1.00 13.22 ATOM 58 OG1 THR A 7 47.420 10.184 36.521 1.00 15.15 ATOM 59 CG2 THR A 7 48.936 9.075 38.078 1.00 14.21 ATOM 60 N LEU A 8 45.886 8.240 40.200 0.54 12.88 ATOM 61 CA LEU A 8 45.984 7.556 41.483 0.54 13.59 ATOM 62 C LEU A 8 45.163 6.277 41.427 0.54 12.44 ATOM 63 O LEU A 8 45.621 5.206 41.920 0.54 11.55 ATOM 64 CB LEU A 8 45.601 8.470 42.649 0.54 13.94 ATOM 65 CG LEU A 8 44.123 8.750 42.918 0.54 15.62 ATOM 66 CD1 LEU A 8 43.503 7.674 43.737 0.54 15.30 ATOM 67 CD2 LEU A 8 43.963 10.078 43.616 0.54 15.31 ATOM 68 N PHE A 9 43.961 6.338 40.812 1.00 12.92 ATOM 69 CA PHE A 9 43.171 5.112 40.803 1.00 12.21 ATOM 70 C PHE A 9 43.938 4.002 40.071 1.00 12.58 ATOM 71 O PHE A 9 43.989 2.867 40.530 1.00 13.58 ATOM 72 CB PHE A 9 41.855 5.348 40.094 1.00 11.96 ATOM 73 CG PHE A 9 40.928 4.141 40.137 1.00 11.42 ATOM 74 CD1 PHE A 9 39.992 4.002 41.125 1.00 10.39 ATOM 75 CD2 PHE A 9 41.061 3.123 39.210 1.00 12.22 ATOM 76 CE1 PHE A 9 39.226 2.852 41.198 1.00 11.22 ATOM 77 CE2 PHE A 9 40.266 1.988 39.253 1.00 13.13 ATOM 78 CZ PHE A 9 39.349 1.852 40.250 1.00 12.14 ATOM 79 N ASP A 10 44.543 4.357 38.938 1.00 12.76 ATOM 80 CA ASP A 10 45.135 3.368 38.067 1.00 13.60 ATOM 81 C ASP A 10 46.503 2.903 38.543 1.00 14.32 ATOM 82 O ASP A 10 46.884 1.765 38.261 1.00 15.46 ATOM 83 CB ASP A 10 45.287 3.933 36.659 1.00 14.50 ATOM 84 CG ASP A 10 43.981 4.244 35.990 1.00 17.22 ATOM 85 OD1 ASP A 10 42.934 3.734 36.400 1.00 19.21 ATOM 86 OD2 ASP A 10 44.009 5.021 35.017 1.00 20.91 ATOM 87 N HSD A 11 47.215 3.770 39.271 1.00 13.71 ATOM 88 CA HSD A 11 48.646 3.508 39.564 1.00 14.32 ATOM 89 C HSD A 11 49.044 3.594 41.018 1.00 13.93 ATOM 90 O HSD A 11 50.215 3.268 41.290 1.00 15.60 ATOM 91 CB HSD A 11 49.543 4.429 38.712 1.00 15.43 ATOM 92 CG HSD A 11 49.218 4.357 37.263 1.00 14.87 ATOM 93 ND1 HSD A 11 49.490 3.247 36.491 1.00 14.64 ATOM 94 CD2 HSD A 11 48.630 5.259 36.441 1.00 15.72 ATOM 95 CE1 HSD A 11 49.009 3.454 35.271 1.00 13.66 ATOM 96 NE2 HSD A 11 48.479 4.666 35.215 1.00 14.79 ATOM 97 N ALA A 12 48.202 4.031 41.955 1.00 15.33 ATOM 98 CA ALA A 12 48.675 4.332 43.307 1.00 15.63 ATOM 99 C ALA A 12 47.797 3.651 44.331 1.00 15.90 ATOM 100 O ALA A 12 46.954 4.294 44.985 1.00 15.69 ATOM 101 CB ALA A 12 48.737 5.824 43.538 1.00 16.06 ATOM 102 N PRO A 13 47.986 2.334 44.531 1.00 17.69 ATOM 103 CA PRO A 13 47.158 1.627 45.517 1.00 17.82 ATOM 104 C PRO A 13 47.106 2.251 46.928 1.00 18.06 ATOM 105 O PRO A 13 46.033 2.264 47.525 1.00 17.65 ATOM 106 CB PRO A 13 47.763 0.212 45.558 1.00 19.76 ATOM 107 CG PRO A 13 48.499 0.047 44.266 1.00 19.90 ATOM 108 CD PRO A 13 48.877 1.428 43.779 1.00 17.71 ATOM 109 N ASP A 14 48.223 2.755 47.471 1.00 17.61 ATOM 110 CA ASP A 14 48.184 3.330 48.830 1.00 17.09 ATOM 111 C ASP A 14 47.375 4.618 48.869 1.00 16.78 ATOM 112 O ASP A 14 46.666 4.903 49.851 1.00 17.40 ATOM 113 CB ASP A 14 49.576 3.642 49.359 1.00 18.13 ATOM 114 CG ASP A 14 50.460 2.405 49.500 0.50 16.74 ATOM 115 OD1 ASP A 14 49.888 1.334 49.806 0.50 19.76 ATOM 116 OD2 ASP A 14 51.698 2.506 49.315 0.50 21.86 ATOM 117 N LYS A 15 47.504 5.454 47.851 1.00 16.38 ATOM 118 CA LYS A 15 46.750 6.695 47.845 1.00 17.13 ATOM 119 C LYS A 15 45.259 6.369 47.635 1.00 14.45 ATOM 120 O LYS A 15 44.362 6.967 48.262 1.00 16.90 ATOM 121 CB LYS A 15 47.299 7.620 46.775 1.00 18.86 ATOM 122 CG LYS A 15 46.780 9.036 46.859 1.00 21.76 ATOM 123 CD LYS A 15 47.709 10.125 46.403 1.00 23.52 ATOM 124 CE LYS A 15 48.230 9.937 45.013 1.00 26.85 ATOM 125 NZ LYS A 15 49.352 10.897 44.801 1.00 28.38 ATOM 126 N LEU A 16 44.988 5.425 46.722 1.00 14.22 ATOM 127 CA LEU A 16 43.604 5.011 46.511 1.00 13.33 ATOM 128 C LEU A 16 42.994 4.512 47.825 1.00 13.30 ATOM 129 O LEU A 16 41.810 4.763 48.132 1.00 12.97 ATOM 130 CB LEU A 16 43.535 3.932 45.431 1.00 13.28 ATOM 131 CG LEU A 16 42.132 3.431 45.103 1.00 13.96 ATOM 132 CD1 LEU A 16 41.238 4.626 44.724 1.00 14.05 ATOM 133 CD2 LEU A 16 42.193 2.348 44.017 1.00 15.31 ATOM 134 N ASN A 17 43.790 3.812 48.634 0.57 13.19 ATOM 135 CA ASN A 17 43.261 3.277 49.879 0.57 14.01 ATOM 136 C ASN A 17 42.847 4.387 50.841 0.57 12.68 ATOM 137 O ASN A 17 41.791 4.315 51.472 0.57 11.90 ATOM 138 CB ASN A 17 44.260 2.324 50.534 0.57 14.81 ATOM 139 CG ASN A 17 44.290 0.967 49.860 0.57 17.71 ATOM 140 OD1 ASN A 17 43.318 0.546 49.220 0.57 22.74 ATOM 141 ND2 ASN A 17 45.394 0.256 50.025 0.57 20.97 ATOM 142 N VAL A 18 43.616 5.450 50.954 1.00 13.81 ATOM 143 CA VAL A 18 43.200 6.518 51.858 1.00 12.20 ATOM 144 C VAL A 18 42.047 7.285 51.273 1.00 11.51 ATOM 145 O VAL A 18 41.176 7.749 52.017 1.00 12.55 ATOM 146 CB VAL A 18 44.377 7.424 52.322 1.00 13.37 ATOM 147 CG1 VAL A 18 45.062 8.147 51.185 1.00 16.27 ATOM 148 CG2 VAL A 18 43.922 8.407 53.356 1.00 15.10 ATOM 149 N VAL A 19 41.996 7.419 49.957 1.00 12.20 ATOM 150 CA VAL A 19 40.783 7.997 49.339 1.00 11.13 ATOM 151 C VAL A 19 39.539 7.203 49.738 1.00 9.79 ATOM 152 O VAL A 19 38.525 7.776 50.151 1.00 9.65 ATOM 153 CB VAL A 19 40.938 8.118 47.831 1.00 12.13 ATOM 154 CG1 VAL A 19 39.621 8.435 47.159 1.00 12.13 ATOM 155 CG2 VAL A 19 41.998 9.208 47.486 1.00 14.10 ATOM 156 N LYS A 20 39.552 5.903 49.532 0.45 9.54 ATOM 157 CA LYS A 20 38.382 5.116 49.848 0.45 9.71 ATOM 158 C LYS A 20 38.045 5.271 51.305 0.45 8.71 ATOM 159 O LYS A 20 36.867 5.432 51.690 0.45 8.15 ATOM 160 CB LYS A 20 38.591 3.658 49.489 0.45 9.96 ATOM 161 CG LYS A 20 38.780 3.421 47.996 0.45 9.98 ATOM 162 CD LYS A 20 39.031 1.963 47.660 0.45 12.00 ATOM 163 CE LYS A 20 37.734 1.138 47.662 0.45 13.76 ATOM 164 NZ LYS A 20 38.052 -0.312 47.513 0.45 13.60 ATOM 165 N LYS A 21 39.087 5.224 52.140 0.45 9.32 ATOM 166 CA LYS A 21 38.888 5.291 53.570 0.45 9.83 ATOM 167 C LYS A 21 38.138 6.537 53.952 0.45 9.15 ATOM 168 O LYS A 21 37.146 6.485 54.686 0.45 10.51 ATOM 169 CB LYS A 21 40.234 5.292 54.279 0.45 9.66 ATOM 170 CG LYS A 21 40.172 5.296 55.787 0.45 11.21 ATOM 171 CD LYS A 21 41.599 5.265 56.347 0.45 12.10 ATOM 172 CE LYS A 21 41.631 5.431 57.842 0.45 14.35 ATOM 173 NZ LYS A 21 41.358 4.158 58.527 0.45 17.25 ATOM 174 N THR A 22 38.607 7.644 53.423 1.00 9.29 ATOM 175 CA THR A 22 38.106 8.995 53.667 1.00 8.74 ATOM 176 C THR A 22 36.667 9.085 53.165 1.00 8.33 ATOM 177 O THR A 22 35.815 9.674 53.808 1.00 8.48 ATOM 178 CB THR A 22 38.978 10.005 52.900 1.00 9.15 ATOM 179 OG1 THR A 22 40.329 9.926 53.450 1.00 10.47 ATOM 180 CG2 THR A 22 38.512 11.412 53.081 1.00 10.52 ATOM 181 N LEU A 23 36.407 8.503 51.980 0.62 8.03 ATOM 182 CA LEU A 23 35.064 8.567 51.397 0.62 7.80 ATOM 183 C LEU A 23 34.064 7.831 52.254 0.62 8.17 ATOM 184 O LEU A 23 32.940 8.306 52.448 0.62 8.90 ATOM 185 CB LEU A 23 35.068 8.053 49.975 0.62 7.92 ATOM 186 CG LEU A 23 35.823 9.008 49.022 0.62 6.19 ATOM 187 CD1 LEU A 23 35.816 8.346 47.613 0.62 7.79 ATOM 188 CD2 LEU A 23 35.234 10.389 48.981 0.62 9.22 ATOM 189 N ILE A 24 34.430 6.664 52.772 1.00 9.19 ATOM 190 CA ILE A 24 33.518 5.938 53.653 1.00 10.29 ATOM 191 C ILE A 24 33.209 6.818 54.886 1.00 9.90 ATOM 192 O ILE A 24 32.034 6.936 55.283 1.00 10.22 ATOM 193 CB ILE A 24 34.089 4.562 54.041 1.00 12.30 ATOM 194 CG1 ILE A 24 34.099 3.663 52.811 1.00 14.20 ATOM 195 CG2 ILE A 24 33.297 3.899 55.170 1.00 14.01 ATOM 196 CD ILE A 24 34.768 2.310 52.971 1.00 16.35 ATOM 197 N THR A 25 34.217 7.445 55.500 1.00 9.89 ATOM 198 CA THR A 25 33.979 8.295 56.636 1.00 10.03 ATOM 199 C THR A 25 33.022 9.438 56.283 1.00 8.89 ATOM 200 O THR A 25 32.078 9.733 57.024 1.00 9.63 ATOM 201 CB THR A 25 35.315 8.839 57.183 1.00 11.07 ATOM 202 OG1 THR A 25 36.179 7.737 57.540 1.00 13.63 ATOM 203 CG2 THR A 25 35.078 9.726 58.358 1.00 12.60 ATOM 204 N PHE A 26 33.280 10.073 55.155 1.00 8.47 ATOM 205 CA PHE A 26 32.489 11.226 54.716 1.00 8.32 ATOM 206 C PHE A 26 31.038 10.814 54.458 1.00 7.86 ATOM 207 O PHE A 26 30.101 11.492 54.900 1.00 8.99 ATOM 208 CB PHE A 26 33.155 11.775 53.464 1.00 8.28 ATOM 209 CG PHE A 26 32.292 12.764 52.686 1.00 8.25 ATOM 210 CD1 PHE A 26 31.978 14.007 53.217 1.00 8.92 ATOM 211 CD2 PHE A 26 31.822 12.447 51.419 1.00 8.44 ATOM 212 CE1 PHE A 26 31.206 14.918 52.467 1.00 9.44 ATOM 213 CE2 PHE A 26 31.034 13.326 50.692 1.00 9.49 ATOM 214 CZ PHE A 26 30.746 14.568 51.193 1.00 9.20 ATOM 215 N VAL A 27 30.824 9.775 53.658 1.00 7.97 ATOM 216 CA VAL A 27 29.435 9.436 53.332 1.00 8.27 ATOM 217 C VAL A 27 28.686 9.015 54.602 1.00 8.46 ATOM 218 O VAL A 27 27.502 9.331 54.750 1.00 9.36 ATOM 219 CB VAL A 27 29.286 8.419 52.189 1.00 8.76 ATOM 220 CG1 VAL A 27 29.940 8.929 50.936 1.00 9.26 ATOM 221 CG2 VAL A 27 29.722 7.036 52.554 1.00 10.32 ATOM 222 N ASN A 28 29.353 8.395 55.581 0.58 8.72 ATOM 223 CA ASN A 28 28.639 8.046 56.805 0.58 8.50 ATOM 224 C ASN A 28 28.382 9.246 57.720 0.58 8.42 ATOM 225 O ASN A 28 27.380 9.272 58.427 0.58 8.31 ATOM 226 CB ASN A 28 29.377 6.890 57.510 0.58 9.20 ATOM 227 CG ASN A 28 29.220 5.581 56.738 0.58 10.77 ATOM 228 OD1 ASN A 28 28.213 5.389 56.016 0.58 12.78 ATOM 229 ND2 ASN A 28 30.179 4.680 56.862 0.58 11.70 ATOM 230 N LYS A 29 29.247 10.259 57.698 0.58 8.70 ATOM 231 CA LYS A 29 28.987 11.474 58.474 0.58 9.42 ATOM 232 C LYS A 29 27.589 11.986 58.176 0.58 8.74 ATOM 233 O LYS A 29 26.892 12.528 59.050 0.58 8.89 ATOM 234 CB LYS A 29 30.048 12.504 58.095 0.58 9.26 ATOM 235 CG LYS A 29 29.881 13.854 58.616 0.58 10.57 ATOM 236 CD LYS A 29 31.033 14.707 58.114 0.58 11.32 ATOM 237 CE LYS A 29 30.946 16.126 58.561 0.58 12.76 ATOM 238 NZ LYS A 29 32.018 16.888 57.842 0.58 12.77 ATOM 239 N HSD A 30 27.196 11.780 56.932 1.00 8.75 ATOM 240 CA HSD A 30 25.872 12.239 56.500 1.00 9.05 ATOM 241 C HSD A 30 24.815 11.173 56.566 1.00 8.78 ATOM 242 O HSD A 30 23.746 11.399 57.135 1.00 9.57 ATOM 243 CB HSD A 30 25.995 12.892 55.148 1.00 8.94 ATOM 244 CG HSD A 30 26.916 14.053 55.212 1.00 9.79 ATOM 245 ND1 HSD A 30 26.555 15.210 55.859 1.00 11.22 ATOM 246 CD2 HSD A 30 28.210 14.184 54.828 1.00 10.10 ATOM 247 CE1 HSD A 30 27.602 16.020 55.845 1.00 11.46 ATOM 248 NE2 HSD A 30 28.619 15.425 55.238 1.00 11.08 ATOM 249 N LEU A 31 25.067 10.008 55.991 1.00 8.54 ATOM 250 CA LEU A 31 24.046 8.968 55.931 1.00 8.99 ATOM 251 C LEU A 31 23.689 8.435 57.309 1.00 9.75 ATOM 252 O LEU A 31 22.544 7.980 57.512 1.00 10.19 ATOM 253 CB LEU A 31 24.496 7.829 54.995 1.00 9.86 ATOM 254 CG LEU A 31 24.528 8.232 53.498 1.00 9.62 ATOM 255 CD1 LEU A 31 25.242 7.201 52.650 1.00 11.80 ATOM 256 CD2 LEU A 31 23.097 8.473 52.946 1.00 11.51 ATOM 257 N ASN A 32 24.590 8.513 58.288 1.00 10.60 ATOM 258 CA ASN A 32 24.248 8.127 59.646 1.00 12.04 ATOM 259 C ASN A 32 23.105 8.996 60.218 1.00 12.12 ATOM 260 O ASN A 32 22.390 8.554 61.131 1.00 13.81 ATOM 261 CB ASN A 32 25.468 8.155 60.571 1.00 13.41 ATOM 262 CG ASN A 32 26.566 7.068 60.255 1.00 15.40 ATOM 263 OD1 ASN A 32 27.623 7.154 60.872 1.00 19.45 ATOM 264 ND2 ASN A 32 26.386 6.152 59.312 1.00 15.61 ATOM 265 N LYS A 33 22.910 10.212 59.691 1.00 11.99 ATOM 266 CA LYS A 33 21.776 11.063 60.099 1.00 13.05 ATOM 267 C LYS A 33 20.430 10.395 59.803 1.00 12.68 ATOM 268 O LYS A 33 19.405 10.736 60.416 1.00 14.78 ATOM 269 CB LYS A 33 21.808 12.406 59.377 1.00 13.01 ATOM 270 CG LYS A 33 23.039 13.280 59.662 1.00 14.26 ATOM 271 CD LYS A 33 23.188 14.445 58.675 1.00 13.89 ATOM 272 CE LYS A 33 24.351 15.376 59.005 1.00 14.95 ATOM 273 NZ LYS A 33 24.717 16.334 57.904 1.00 14.73 ATOM 274 N LEU A 34 20.433 9.472 58.845 0.90 11.55 ATOM 275 CA LEU A 34 19.252 8.677 58.428 0.90 11.34 ATOM 276 C LEU A 34 19.343 7.232 58.950 0.90 11.71 ATOM 277 O LEU A 34 18.606 6.361 58.510 0.90 13.38 ATOM 278 CB LEU A 34 19.158 8.678 56.920 0.90 12.18 ATOM 279 CG LEU A 34 19.117 10.090 56.307 0.90 13.39 ATOM 280 CD1 LEU A 34 18.944 10.047 54.812 0.90 13.44 ATOM 281 CD2 LEU A 34 18.102 10.995 56.967 0.90 16.72 ATOM 282 N ASN A 35 20.254 6.972 59.874 1.00 11.84 ATOM 283 CA ASN A 35 20.473 5.606 60.384 1.00 12.40 ATOM 284 C ASN A 35 20.885 4.619 59.327 1.00 12.49 ATOM 285 O ASN A 35 20.547 3.452 59.390 1.00 15.16 ATOM 286 CB ASN A 35 19.301 5.109 61.227 1.00 13.83 ATOM 287 CG ASN A 35 18.982 6.071 62.297 1.00 14.82 ATOM 288 OD1 ASN A 35 19.822 6.398 63.119 1.00 17.52 ATOM 289 ND2 ASN A 35 17.772 6.612 62.261 1.00 16.70 ATOM 290 N LEU A 36 21.660 5.105 58.357 1.00 12.25 ATOM 291 CA LEU A 36 22.169 4.279 57.254 1.00 12.55 ATOM 292 C LEU A 36 23.689 4.235 57.328 1.00 12.92 ATOM 293 O LEU A 36 24.308 5.245 57.643 1.00 14.37 ATOM 294 CB LEU A 36 21.730 4.866 55.910 1.00 12.95 ATOM 295 CG LEU A 36 20.228 4.924 55.674 1.00 14.58 ATOM 296 CD1 LEU A 36 19.938 5.739 54.424 1.00 16.08 ATOM 297 CD2 LEU A 36 19.659 3.511 55.572 1.00 17.82 ATOM 298 N GLU A 37 24.271 3.057 57.100 1.00 13.76 ATOM 299 CA GLU A 37 25.738 2.816 57.126 1.00 13.89 ATOM 300 C GLU A 37 26.221 2.278 55.787 1.00 12.61 ATOM 301 O GLU A 37 25.636 1.353 55.233 1.00 15.92 ATOM 302 CB GLU A 37 26.139 1.789 58.211 1.00 15.02 ATOM 303 CG GLU A 37 27.658 1.548 58.280 1.00 16.24 ATOM 304 CD GLU A 37 28.105 0.445 59.255 1.00 16.98 ATOM 305 OE1 GLU A 37 27.265 -0.312 59.788 1.00 21.84 ATOM 306 OE2 GLU A 37 29.331 0.284 59.474 1.00 21.55 ATOM 307 N VAL A 38 27.290 2.845 55.264 1.00 11.45 ATOM 308 CA VAL A 38 27.987 2.273 54.132 1.00 11.40 ATOM 309 C VAL A 38 29.251 1.577 54.618 1.00 11.49 ATOM 310 O VAL A 38 30.047 2.141 55.396 1.00 12.95 ATOM 311 CB VAL A 38 28.333 3.377 53.116 1.00 12.28 ATOM 312 CG1 VAL A 38 29.318 2.899 52.085 1.00 14.10 ATOM 313 CG2 VAL A 38 27.055 3.904 52.461 1.00 14.15 ATOM 314 N THR A 39 29.410 0.337 54.188 1.00 11.08 ATOM 315 CA THR A 39 30.629 -0.430 54.422 1.00 12.48 ATOM 316 C THR A 39 31.405 -0.758 53.153 1.00 12.25 ATOM 317 O THR A 39 32.572 -1.130 53.256 1.00 15.70 ATOM 318 CB THR A 39 30.346 -1.732 55.170 1.00 14.08 ATOM 319 OG1 THR A 39 29.361 -2.481 54.446 1.00 15.89 ATOM 320 CG2 THR A 39 29.868 -1.453 56.585 1.00 16.70 ATOM 321 N GLU A 40 30.705 -0.781 51.991 0.63 12.20 ATOM 322 CA GLU A 40 31.236 -1.273 50.684 0.63 11.24 ATOM 323 C GLU A 40 30.959 -0.284 49.548 0.63 10.10 ATOM 324 O GLU A 40 29.854 -0.246 48.951 0.63 9.45 ATOM 325 CB GLU A 40 30.664 -2.655 50.354 0.63 10.78 ATOM 326 CG GLU A 40 31.190 -3.336 49.113 0.63 14.62 ATOM 327 CD GLU A 40 30.735 -4.756 49.018 0.63 16.72 ATOM 328 OE1 GLU A 40 31.280 -5.611 49.731 0.63 22.10 ATOM 329 OE2 GLU A 40 29.834 -5.022 48.214 0.63 22.51 ATOM 330 N LEU A 41 31.961 0.523 49.219 0.63 9.20 ATOM 331 CA LEU A 41 31.800 1.514 48.139 0.63 9.63 ATOM 332 C LEU A 41 31.553 0.876 46.779 0.63 9.70 ATOM 333 O LEU A 41 30.939 1.523 45.918 0.63 9.73 ATOM 334 CB LEU A 41 33.027 2.407 48.038 0.63 9.82 ATOM 335 CG LEU A 41 33.413 3.212 49.297 0.63 10.77 ATOM 336 CD1 LEU A 41 34.788 3.879 49.122 0.63 12.30 ATOM 337 CD2 LEU A 41 32.344 4.248 49.698 0.63 13.30 ATOM 338 N GLU A 42 32.052 -0.347 46.588 1.00 10.44 ATOM 339 CA GLU A 42 31.965 -1.090 45.326 1.00 10.87 ATOM 340 C GLU A 42 30.530 -1.315 44.837 1.00 10.37 ATOM 341 O GLU A 42 30.312 -1.436 43.657 1.00 12.75 ATOM 342 CB GLU A 42 32.688 -2.446 45.466 1.00 12.36 ATOM 343 CG GLU A 42 34.216 -2.380 45.481 1.00 14.57 ATOM 344 CD GLU A 42 34.850 -1.969 46.781 1.00 16.38 ATOM 345 OE1 GLU A 42 34.168 -1.830 47.821 1.00 15.47 ATOM 346 OE2 GLU A 42 36.078 -1.779 46.739 1.00 19.39 ATOM 347 N THR A 43 29.601 -1.438 45.775 1.00 9.87 ATOM 348 CA THR A 43 28.226 -1.752 45.401 1.00 10.71 ATOM 349 C THR A 43 27.142 -0.919 46.048 1.00 9.40 ATOM 350 O THR A 43 26.027 -0.889 45.509 1.00 9.93 ATOM 351 CB THR A 43 27.890 -3.216 45.684 1.00 14.05 ATOM 352 OG1 THR A 43 27.870 -3.413 47.101 1.00 17.76 ATOM 353 CG2 THR A 43 28.852 -4.176 44.975 1.00 15.70 ATOM 354 N GLN A 44 27.379 -0.290 47.185 1.00 8.77 ATOM 355 CA GLN A 44 26.288 0.291 47.954 1.00 9.51 ATOM 356 C GLN A 44 25.768 1.623 47.403 1.00 8.73 ATOM 357 O GLN A 44 24.780 2.139 47.954 1.00 9.97 ATOM 358 CB GLN A 44 26.633 0.391 49.432 1.00 10.24 ATOM 359 CG GLN A 44 26.657 -0.967 50.096 1.00 12.05 ATOM 360 CD GLN A 44 26.837 -0.840 51.588 1.00 13.63 ATOM 361 OE1 GLN A 44 27.815 -0.350 52.064 1.00 12.80 ATOM 362 NE2 GLN A 44 25.806 -1.175 52.327 1.00 19.84 ATOM 363 N PHE A 45 26.388 2.170 46.372 1.00 8.21 ATOM 364 CA PHE A 45 25.874 3.342 45.671 1.00 7.92 ATOM 365 C PHE A 45 25.224 3.018 44.339 1.00 7.77 ATOM 366 O PHE A 45 24.673 3.913 43.692 1.00 8.31 ATOM 367 CB PHE A 45 26.960 4.421 45.506 1.00 8.34 ATOM 368 CG PHE A 45 27.242 5.139 46.831 1.00 8.93 ATOM 369 CD1 PHE A 45 26.405 6.162 47.243 1.00 10.07 ATOM 370 CD2 PHE A 45 28.221 4.721 47.694 1.00 10.47 ATOM 371 CE1 PHE A 45 26.587 6.821 48.461 1.00 10.36 ATOM 372 CE2 PHE A 45 28.405 5.428 48.950 1.00 10.32 ATOM 373 CZ PHE A 45 27.534 6.433 49.301 1.00 10.93 ATOM 374 N ALA A 46 25.267 1.761 43.919 1.00 8.28 ATOM 375 CA ALA A 46 24.851 1.407 42.562 1.00 8.56 ATOM 376 C ALA A 46 23.377 1.672 42.313 1.00 8.39 ATOM 377 O ALA A 46 23.004 1.938 41.178 1.00 9.74 ATOM 378 CB ALA A 46 25.165 -0.035 42.278 1.00 10.29 ATOM 379 N ASP A 47 22.517 1.513 43.322 1.00 8.16 ATOM 380 CA ASP A 47 21.067 1.649 43.072 1.00 8.29 ATOM 381 C ASP A 47 20.577 3.078 43.115 1.00 7.90 ATOM 382 O ASP A 47 19.380 3.336 42.921 1.00 8.39 ATOM 383 CB ASP A 47 20.252 0.701 43.943 1.00 8.86 ATOM 384 CG ASP A 47 20.241 1.042 45.395 1.00 10.41 ATOM 385 OD1 ASP A 47 20.582 2.164 45.793 1.00 9.72 ATOM 386 OD2 ASP A 47 19.787 0.154 46.162 1.00 14.50 ATOM 387 N GLY A 48 21.482 4.031 43.363 1.00 7.56 ATOM 388 CA GLY A 48 21.188 5.426 43.347 1.00 7.59 ATOM 389 C GLY A 48 20.566 5.996 44.607 1.00 7.60 ATOM 390 O GLY A 48 20.477 7.212 44.726 1.00 7.90 ATOM 391 N VAL A 49 20.071 5.150 45.514 1.00 7.43 ATOM 392 CA VAL A 49 19.289 5.639 46.656 1.00 8.00 ATOM 393 C VAL A 49 20.148 6.467 47.590 1.00 7.91 ATOM 394 O VAL A 49 19.790 7.589 47.957 1.00 8.35 ATOM 395 CB VAL A 49 18.648 4.446 47.387 1.00 8.59 ATOM 396 CG1 VAL A 49 17.991 4.852 48.688 1.00 9.60 ATOM 397 CG2 VAL A 49 17.636 3.765 46.438 1.00 10.18 ATOM 398 N TYR A 50 21.290 5.914 48.006 1.00 8.09 ATOM 399 CA TYR A 50 22.154 6.654 48.895 1.00 8.30 ATOM 400 C TYR A 50 22.696 7.910 48.278 1.00 7.96 ATOM 401 O TYR A 50 22.925 8.908 48.987 1.00 8.43 ATOM 402 CB TYR A 50 23.282 5.757 49.440 1.00 9.56 ATOM 403 CG TYR A 50 22.830 4.637 50.360 1.00 10.65 ATOM 404 CD1 TYR A 50 21.495 4.437 50.739 1.00 12.57 ATOM 405 CD2 TYR A 50 23.759 3.766 50.868 1.00 13.35 ATOM 406 CE1 TYR A 50 21.102 3.407 51.572 1.00 13.99 ATOM 407 CE2 TYR A 50 23.373 2.733 51.761 1.00 14.59 ATOM 408 CZ TYR A 50 22.053 2.564 52.094 1.00 15.31 ATOM 409 OH TYR A 50 21.682 1.532 52.942 1.00 18.02 ATOM 410 N LEU A 51 22.967 7.867 46.985 0.51 7.67 ATOM 411 CA LEU A 51 23.482 9.022 46.337 0.51 7.31 ATOM 412 C LEU A 51 22.478 10.202 46.300 0.51 7.21 ATOM 413 O LEU A 51 22.841 11.356 46.456 0.51 7.13 ATOM 414 CB LEU A 51 23.958 8.623 44.944 0.51 7.24 ATOM 415 CG LEU A 51 24.841 9.687 44.279 0.51 6.58 ATOM 416 CD1 LEU A 51 26.153 9.961 45.049 0.51 7.19 ATOM 417 CD2 LEU A 51 25.109 9.258 42.836 0.51 6.59 ATOM 418 N VAL A 52 21.198 9.905 46.056 1.00 7.09 ATOM 419 CA VAL A 52 20.135 10.919 46.145 1.00 7.41 ATOM 420 C VAL A 52 20.037 11.457 47.570 1.00 7.27 ATOM 421 O VAL A 52 20.000 12.655 47.794 1.00 7.97 ATOM 422 CB VAL A 52 18.780 10.338 45.663 1.00 7.58 ATOM 423 CG1 VAL A 52 17.659 11.337 46.000 1.00 8.62 ATOM 424 CG2 VAL A 52 18.853 10.060 44.161 1.00 7.92 ATOM 425 N LEU A 53 19.937 10.553 48.532 1.00 7.68 ATOM 426 CA LEU A 53 19.762 10.985 49.924 1.00 8.01 ATOM 427 C LEU A 53 20.967 11.825 50.372 1.00 7.78 ATOM 428 O LEU A 53 20.770 12.857 51.035 1.00 8.48 ATOM 429 CB LEU A 53 19.605 9.779 50.840 1.00 8.96 ATOM 430 CG LEU A 53 18.271 9.044 50.635 1.00 10.23 ATOM 431 CD1 LEU A 53 18.323 7.733 51.399 1.00 12.95 ATOM 432 CD2 LEU A 53 17.093 9.937 51.024 1.00 12.62 ATOM 433 N LEU A 54 22.160 11.383 50.010 1.00 7.93 ATOM 434 CA LEU A 54 23.368 12.148 50.339 1.00 8.14 ATOM 435 C LEU A 54 23.321 13.540 49.760 1.00 8.27 ATOM 436 O LEU A 54 23.669 14.513 50.455 1.00 8.50 ATOM 437 CB LEU A 54 24.612 11.382 49.851 1.00 8.17 ATOM 438 CG LEU A 54 25.935 12.037 50.085 1.00 8.56 ATOM 439 CD1 LEU A 54 26.235 12.210 51.589 1.00 10.39 ATOM 440 CD2 LEU A 54 27.031 11.150 49.433 1.00 9.29 ATOM 441 N MET A 55 22.884 13.681 48.504 1.00 8.61 ATOM 442 CA MET A 55 22.834 15.007 47.894 1.00 8.96 ATOM 443 C MET A 55 21.898 15.932 48.620 1.00 9.33 ATOM 444 O MET A 55 22.208 17.127 48.778 1.00 11.35 ATOM 445 CB MET A 55 22.437 14.943 46.420 1.00 9.56 ATOM 446 CG MET A 55 23.548 14.445 45.542 1.00 10.13 ATOM 447 SD MET A 55 25.103 15.250 45.809 1.00 11.57 ATOM 448 CE MET A 55 24.731 16.904 45.774 1.00 9.14 ATOM 449 N GLY A 56 20.746 15.449 49.087 1.00 9.35 ATOM 450 CA GLY A 56 19.910 16.327 49.871 1.00 9.36 ATOM 451 C GLY A 56 20.599 16.747 51.145 1.00 9.57 ATOM 452 O GLY A 56 20.656 17.933 51.490 1.00 10.85 ATOM 453 N LEU A 57 21.180 15.784 51.861 1.00 8.74 ATOM 454 CA LEU A 57 21.839 16.088 53.119 1.00 9.59 ATOM 455 C LEU A 57 22.969 17.094 52.978 1.00 9.44 ATOM 456 O LEU A 57 23.141 17.962 53.839 1.00 11.15 ATOM 457 CB LEU A 57 22.360 14.822 53.765 1.00 10.00 ATOM 458 CG LEU A 57 21.283 13.823 54.200 1.00 11.02 ATOM 459 CD1 LEU A 57 21.945 12.465 54.517 1.00 13.75 ATOM 460 CD2 LEU A 57 20.382 14.411 55.285 1.00 14.69 ATOM 461 N LEU A 58 23.746 16.977 51.924 1.00 9.34 ATOM 462 CA LEU A 58 24.855 17.896 51.690 1.00 9.71 ATOM 463 C LEU A 58 24.382 19.312 51.424 1.00 10.86 ATOM 464 O LEU A 58 25.108 20.259 51.717 1.00 12.62 ATOM 465 CB LEU A 58 25.742 17.401 50.551 1.00 9.32 ATOM 466 CG LEU A 58 26.470 16.084 50.836 1.00 8.54 ATOM 467 CD1 LEU A 58 27.272 15.631 49.641 1.00 9.81 ATOM 468 CD2 LEU A 58 27.400 16.203 52.081 1.00 9.78 ATOM 469 N GLU A 59 23.156 19.452 50.885 1.00 10.78 ATOM 470 CA GLU A 59 22.530 20.743 50.647 1.00 12.33 ATOM 471 C GLU A 59 21.520 21.105 51.774 1.00 12.73 ATOM 472 O GLU A 59 20.752 22.055 51.631 1.00 15.16 ATOM 473 CB GLU A 59 21.831 20.717 49.278 1.00 13.16 ATOM 474 CG GLU A 59 22.832 20.745 48.123 1.00 14.74 ATOM 475 CD GLU A 59 23.499 22.070 47.903 0.85 15.68 ATOM 476 OE1 GLU A 59 22.958 23.121 48.327 0.85 19.75 ATOM 477 OE2 GLU A 59 24.540 22.091 47.218 0.85 15.27 ATOM 478 N GLY A 60 21.551 20.399 52.904 1.00 11.75 ATOM 479 CA GLY A 60 20.771 20.768 54.061 1.00 12.31 ATOM 480 C GLY A 60 19.315 20.375 54.057 1.00 12.18 ATOM 481 O GLY A 60 18.549 20.999 54.791 1.00 14.68 ATOM 482 N TYR A 61 18.931 19.391 53.213 0.45 12.72 ATOM 483 CA TYR A 61 17.532 19.064 52.821 0.45 13.02 ATOM 484 C TYR A 61 17.271 17.555 52.869 0.45 12.66 ATOM 485 O TYR A 61 18.050 16.773 52.305 0.45 13.51 ATOM 486 CB TYR A 61 17.288 19.575 51.381 0.45 14.25 ATOM 487 CG TYR A 61 15.937 19.300 50.730 0.45 13.86 ATOM 488 CD1 TYR A 61 15.833 18.518 49.573 0.45 14.56 ATOM 489 CD2 TYR A 61 14.774 19.865 51.238 0.45 13.85 ATOM 490 CE1 TYR A 61 14.598 18.290 48.973 0.45 15.84 ATOM 491 CE2 TYR A 61 13.545 19.644 50.646 0.45 15.00 ATOM 492 CZ TYR A 61 13.465 18.859 49.518 0.45 15.03 ATOM 493 OH TYR A 61 12.244 18.636 48.920 0.45 16.00 ATOM 494 N PHE A 62 16.188 17.133 53.531 0.45 12.01 ATOM 495 CA PHE A 62 15.742 15.738 53.396 0.45 10.94 ATOM 496 C PHE A 62 14.945 15.645 52.108 0.45 10.31 ATOM 497 O PHE A 62 13.932 16.361 51.932 0.45 10.42 ATOM 498 CB PHE A 62 14.881 15.228 54.578 0.45 11.51 ATOM 499 CG PHE A 62 15.653 14.970 55.870 0.45 10.83 ATOM 500 CD1 PHE A 62 16.800 14.176 55.904 0.45 11.80 ATOM 501 CD2 PHE A 62 15.200 15.505 57.058 0.45 9.91 ATOM 502 CE1 PHE A 62 17.489 13.953 57.127 0.45 11.95 ATOM 503 CE2 PHE A 62 15.854 15.303 58.235 0.45 9.78 ATOM 504 CZ PHE A 62 16.993 14.516 58.296 0.45 12.27 ATOM 505 N VAL A 63 15.389 14.776 51.201 1.00 9.41 ATOM 506 CA VAL A 63 14.694 14.580 49.957 1.00 9.48 ATOM 507 C VAL A 63 13.427 13.739 50.217 1.00 9.35 ATOM 508 O VAL A 63 13.508 12.689 50.804 1.00 10.60 ATOM 509 CB VAL A 63 15.592 13.814 48.950 1.00 9.83 ATOM 510 CG1 VAL A 63 14.822 13.546 47.659 1.00 10.87 ATOM 511 CG2 VAL A 63 16.866 14.607 48.611 1.00 11.85 ATOM 512 N PRO A 64 12.261 14.176 49.736 1.00 9.69 ATOM 513 CA PRO A 64 11.050 13.373 49.937 1.00 9.68 ATOM 514 C PRO A 64 11.249 11.970 49.384 1.00 9.93 ATOM 515 O PRO A 64 11.716 11.775 48.244 1.00 10.46 ATOM 516 CB PRO A 64 9.988 14.145 49.173 1.00 10.65 ATOM 517 CG PRO A 64 10.484 15.544 49.185 1.00 11.62 ATOM 518 CD PRO A 64 11.982 15.454 49.087 1.00 10.93 ATOM 519 N LEU A 65 10.875 10.967 50.174 1.00 10.08 ATOM 520 CA LEU A 65 11.195 9.567 49.807 1.00 11.20 ATOM 521 C LEU A 65 10.372 9.061 48.614 1.00 11.92 ATOM 522 O LEU A 65 10.777 8.088 47.978 1.00 15.75 ATOM 523 CB LEU A 65 11.051 8.644 51.011 1.00 12.00 ATOM 524 CG LEU A 65 11.968 8.974 52.196 1.00 12.43 ATOM 525 CD1 LEU A 65 11.804 7.943 53.316 1.00 15.15 ATOM 526 CD2 LEU A 65 13.441 9.106 51.793 1.00 13.35 ATOM 527 N HSD A 66 9.286 9.737 48.297 1.00 12.07 ATOM 528 CA HSD A 66 8.473 9.362 47.167 1.00 12.34 ATOM 529 C HSD A 66 8.889 10.104 45.900 1.00 12.11 ATOM 530 O HSD A 66 8.281 9.886 44.861 1.00 14.17 ATOM 531 CB HSD A 66 7.014 9.638 47.481 1.00 12.78 ATOM 532 CG HSD A 66 6.783 11.029 47.937 1.00 12.75 ATOM 533 ND1 HSD A 66 6.762 12.090 47.066 1.00 14.58 ATOM 534 CD2 HSD A 66 6.611 11.548 49.187 1.00 13.72 ATOM 535 CE1 HSD A 66 6.555 13.202 47.752 1.00 15.94 ATOM 536 NE2 HSD A 66 6.479 12.902 49.037 1.00 14.81 ATOM 537 N SER A 67 9.920 10.928 45.978 0.56 11.13 ATOM 538 CA SER A 67 10.268 11.705 44.823 0.56 10.41 ATOM 539 C SER A 67 11.245 10.936 43.907 0.56 9.94 ATOM 540 O SER A 67 11.492 11.369 42.799 0.56 11.14 ATOM 541 CB SER A 67 10.765 13.094 45.178 0.56 11.53 ATOM 542 OG SER A 67 12.039 13.036 45.843 0.56 9.69 ATOM 543 N PHE A 68 11.775 9.808 44.378 1.00 9.47 ATOM 544 CA PHE A 68 12.665 8.959 43.593 1.00 8.82 ATOM 545 C PHE A 68 12.300 7.522 43.944 1.00 9.19 ATOM 546 O PHE A 68 11.317 7.306 44.664 1.00 10.97 ATOM 547 CB PHE A 68 14.144 9.297 43.875 1.00 8.96 ATOM 548 CG PHE A 68 14.562 9.053 45.299 1.00 8.42 ATOM 549 CD1 PHE A 68 15.251 7.923 45.630 1.00 9.90 ATOM 550 CD2 PHE A 68 14.209 9.930 46.336 1.00 8.92 ATOM 551 CE1 PHE A 68 15.648 7.681 46.934 1.00 10.81 ATOM 552 CE2 PHE A 68 14.586 9.696 47.645 1.00 9.52 ATOM 553 CZ PHE A 68 15.278 8.561 47.933 1.00 10.44 ATOM 554 N PHE A 69 13.025 6.556 43.394 1.00 9.24 ATOM 555 CA PHE A 69 12.706 5.146 43.634 1.00 10.16 ATOM 556 C PHE A 69 13.447 4.633 44.844 1.00 9.96 ATOM 557 O PHE A 69 14.618 4.297 44.759 1.00 10.21 ATOM 558 CB PHE A 69 13.027 4.333 42.386 1.00 9.82 ATOM 559 CG PHE A 69 12.275 4.791 41.145 1.00 10.13 ATOM 560 CD1 PHE A 69 10.954 4.447 40.953 1.00 11.45 ATOM 561 CD2 PHE A 69 12.920 5.586 40.186 1.00 9.47 ATOM 562 CE1 PHE A 69 10.289 4.868 39.821 1.00 11.90 ATOM 563 CE2 PHE A 69 12.236 6.025 39.047 1.00 10.64 ATOM 564 CZ PHE A 69 10.915 5.668 38.876 1.00 11.72 ATOM 565 N LEU A 70 12.789 4.649 46.003 1.00 11.28 ATOM 566 CA LEU A 70 13.452 4.287 47.260 1.00 11.44 ATOM 567 C LEU A 70 13.868 2.834 47.270 1.00 10.57 ATOM 568 O LEU A 70 14.869 2.469 47.905 1.00 12.39 ATOM 569 CB LEU A 70 12.498 4.566 48.437 1.00 12.37 ATOM 570 CG LEU A 70 13.056 4.320 49.832 1.00 13.68 ATOM 571 CD1 LEU A 70 14.219 5.279 50.099 1.00 16.01 ATOM 572 CD2 LEU A 70 11.933 4.485 50.852 1.00 15.07 ATOM 573 N THR A 71 13.044 2.023 46.609 0.13 10.79 ATOM 574 CA THR A 71 13.266 0.604 46.426 0.13 10.66 ATOM 575 C THR A 71 13.206 0.355 44.926 0.13 10.57 ATOM 576 O THR A 71 12.147 0.021 44.389 0.13 10.67 ATOM 577 CB THR A 71 12.165 -0.217 47.124 0.13 10.73 ATOM 578 OG1 THR A 71 11.891 0.349 48.412 0.13 9.79 ATOM 579 CG2 THR A 71 12.605 -1.670 47.264 0.13 10.67 ATOM 580 N PRO A 72 14.319 0.603 44.219 1.00 10.59 ATOM 581 CA PRO A 72 14.240 0.461 42.759 1.00 10.40 ATOM 582 C PRO A 72 14.112 -0.990 42.347 1.00 11.16 ATOM 583 O PRO A 72 14.781 -1.868 42.906 1.00 13.15 ATOM 584 CB PRO A 72 15.556 1.097 42.275 1.00 10.93 ATOM 585 CG PRO A 72 16.448 1.094 43.433 1.00 11.71 ATOM 586 CD PRO A 72 15.609 1.158 44.673 1.00 10.41 ATOM 587 N ASP A 73 13.252 -1.229 41.356 0.99 10.83 ATOM 588 CA ASP A 73 12.877 -2.575 40.977 0.99 12.11 ATOM 589 C ASP A 73 13.583 -3.057 39.703 0.99 11.43 ATOM 590 O ASP A 73 13.295 -4.153 39.197 0.99 13.93 ATOM 591 CB ASP A 73 11.359 -2.719 40.899 0.99 13.89 ATOM 592 CG ASP A 73 10.747 -1.998 39.752 0.99 14.65 ATOM 593 OD1 ASP A 73 11.454 -1.497 38.888 0.99 14.74 ATOM 594 OD2 ASP A 73 9.483 -1.996 39.669 0.99 19.99 ATOM 595 N SER A 74 14.478 -2.239 39.158 1.00 10.05 ATOM 596 CA SER A 74 15.026 -2.469 37.828 1.00 9.12 ATOM 597 C SER A 74 16.261 -1.624 37.628 1.00 8.29 ATOM 598 O SER A 74 16.456 -0.605 38.304 1.00 8.21 ATOM 599 CB SER A 74 14.005 -2.099 36.764 1.00 8.92 ATOM 600 OG SER A 74 13.737 -0.707 36.819 1.00 9.87 ATOM 601 N PHE A 75 17.081 -2.023 36.672 1.00 8.36 ATOM 602 CA PHE A 75 18.182 -1.226 36.145 1.00 7.84 ATOM 603 C PHE A 75 17.715 0.194 35.858 1.00 7.65 ATOM 604 O PHE A 75 18.363 1.171 36.248 1.00 7.67 ATOM 605 CB PHE A 75 18.722 -1.911 34.893 1.00 9.07 ATOM 606 CG PHE A 75 19.705 -1.102 34.100 1.00 9.22 ATOM 607 CD1 PHE A 75 20.970 -0.828 34.603 1.00 10.02 ATOM 608 CD2 PHE A 75 19.363 -0.600 32.855 1.00 10.89 ATOM 609 CE1 PHE A 75 21.870 -0.117 33.860 1.00 10.76 ATOM 610 CE2 PHE A 75 20.266 0.111 32.108 1.00 11.55 ATOM 611 CZ PHE A 75 21.522 0.360 32.611 1.00 11.51 ATOM 612 N GLU A 76 16.592 0.324 35.158 1.00 7.68 ATOM 613 CA GLU A 76 16.144 1.623 34.714 1.00 7.57 ATOM 614 C GLU A 76 15.816 2.532 35.887 1.00 7.21 ATOM 615 O GLU A 76 16.110 3.717 35.827 1.00 7.45 ATOM 616 CB GLU A 76 14.898 1.449 33.796 1.00 7.57 ATOM 617 CG GLU A 76 15.205 0.754 32.480 1.00 9.11 ATOM 618 CD GLU A 76 15.198 -0.759 32.480 1.00 9.25 ATOM 619 OE1 GLU A 76 15.222 -1.428 33.527 1.00 10.23 ATOM 620 OE2 GLU A 76 15.234 -1.310 31.365 1.00 13.17 ATOM 621 N GLN A 77 15.149 2.001 36.912 1.00 7.08 ATOM 622 CA GLN A 77 14.868 2.841 38.087 1.00 7.20 ATOM 623 C GLN A 77 16.154 3.274 38.791 1.00 7.15 ATOM 624 O GLN A 77 16.252 4.410 39.284 1.00 7.58 ATOM 625 CB GLN A 77 13.947 2.138 39.066 1.00 7.67 ATOM 626 CG GLN A 77 12.506 2.077 38.510 1.00 8.17 ATOM 627 CD GLN A 77 11.472 1.556 39.480 1.00 9.46 ATOM 628 OE1 GLN A 77 11.787 1.163 40.612 1.00 10.75 ATOM 629 NE2 GLN A 77 10.213 1.562 39.036 1.00 11.95 ATOM 630 N LYS A 78 17.156 2.385 38.836 1.00 7.01 ATOM 631 CA LYS A 78 18.468 2.769 39.407 1.00 7.06 ATOM 632 C LYS A 78 19.121 3.889 38.609 1.00 6.90 ATOM 633 O LYS A 78 19.659 4.839 39.179 1.00 7.00 ATOM 634 CB LYS A 78 19.379 1.540 39.492 1.00 7.19 ATOM 635 CG LYS A 78 18.779 0.472 40.411 1.00 8.00 ATOM 636 CD LYS A 78 19.570 -0.784 40.457 1.00 9.79 ATOM 637 CE LYS A 78 18.862 -1.867 41.250 1.00 12.25 ATOM 638 NZ LYS A 78 19.651 -3.130 41.194 1.00 17.60 ATOM 639 N VAL A 79 19.087 3.796 37.280 1.00 6.69 ATOM 640 CA VAL A 79 19.684 4.817 36.448 1.00 6.99 ATOM 641 C VAL A 79 18.957 6.127 36.643 1.00 6.64 ATOM 642 O VAL A 79 19.580 7.184 36.734 1.00 7.14 ATOM 643 CB VAL A 79 19.746 4.428 34.961 1.00 7.11 ATOM 644 CG1 VAL A 79 20.340 5.522 34.119 1.00 8.16 ATOM 645 CG2 VAL A 79 20.517 3.126 34.748 1.00 8.43 ATOM 646 N LEU A 80 17.614 6.087 36.743 1.00 6.71 ATOM 647 CA LEU A 80 16.869 7.295 36.995 1.00 6.93 ATOM 648 C LEU A 80 17.284 7.893 38.349 1.00 6.49 ATOM 649 O LEU A 80 17.412 9.123 38.450 1.00 7.20 ATOM 650 CB LEU A 80 15.367 7.044 36.951 1.00 7.37 ATOM 651 CG LEU A 80 14.821 6.868 35.519 1.00 8.47 ATOM 652 CD1 LEU A 80 13.415 6.269 35.527 1.00 10.28 ATOM 653 CD2 LEU A 80 14.841 8.250 34.795 1.00 9.49 ATOM 654 N ASN A 81 17.449 7.083 39.386 1.00 6.42 ATOM 655 CA ASN A 81 17.917 7.629 40.660 1.00 6.57 ATOM 656 C ASN A 81 19.267 8.302 40.534 1.00 6.45 ATOM 657 O ASN A 81 19.468 9.401 41.041 1.00 6.88 ATOM 658 CB ASN A 81 18.035 6.535 41.711 1.00 6.72 ATOM 659 CG ASN A 81 16.714 6.074 42.290 1.00 7.74 ATOM 660 OD1 ASN A 81 15.683 6.731 42.162 1.00 7.97 ATOM 661 ND2 ASN A 81 16.806 4.952 43.014 1.00 8.38 ATOM 662 N VAL A 82 20.229 7.642 39.903 0.88 6.40 ATOM 663 CA VAL A 82 21.561 8.237 39.750 0.88 7.01 ATOM 664 C VAL A 82 21.460 9.539 38.971 0.88 6.58 ATOM 665 O VAL A 82 22.084 10.541 39.348 0.88 7.04 ATOM 666 CB VAL A 82 22.565 7.257 39.097 0.88 6.82 ATOM 667 CG1 VAL A 82 23.912 7.927 38.883 0.88 7.31 ATOM 668 CG2 VAL A 82 22.757 6.011 40.002 0.88 6.89 ATOM 669 N SER A 83 20.690 9.544 37.880 0.88 7.10 ATOM 670 CA SER A 83 20.494 10.761 37.091 0.88 7.59 ATOM 671 C SER A 83 19.939 11.857 37.953 0.88 7.28 ATOM 672 O SER A 83 20.343 13.017 37.810 0.88 7.74 ATOM 673 CB SER A 83 19.561 10.485 35.923 0.88 8.62 ATOM 674 OG SER A 83 20.119 9.572 35.026 0.88 12.10 ATOM 675 N PHE A 84 18.992 11.559 38.835 1.00 7.21 ATOM 676 CA PHE A 84 18.424 12.570 39.712 1.00 7.40 ATOM 677 C PHE A 84 19.504 13.113 40.658 1.00 7.45 ATOM 678 O PHE A 84 19.602 14.309 40.869 1.00 7.89 ATOM 679 CB PHE A 84 17.252 11.979 40.499 1.00 7.93 ATOM 680 CG PHE A 84 16.537 12.945 41.371 1.00 8.57 ATOM 681 CD1 PHE A 84 16.214 14.232 40.924 1.00 11.59 ATOM 682 CD2 PHE A 84 16.192 12.590 42.654 1.00 10.37 ATOM 683 CE1 PHE A 84 15.514 15.115 41.771 1.00 13.79 ATOM 684 CE2 PHE A 84 15.472 13.465 43.468 1.00 12.08 ATOM 685 CZ PHE A 84 15.157 14.709 43.020 1.00 13.31 ATOM 686 N ALA A 85 20.327 12.224 41.232 1.00 6.92 ATOM 687 CA ALA A 85 21.433 12.707 42.071 1.00 7.33 ATOM 688 C ALA A 85 22.348 13.618 41.260 1.00 7.23 ATOM 689 O ALA A 85 22.803 14.652 41.781 1.00 7.80 ATOM 690 CB ALA A 85 22.206 11.543 42.649 1.00 7.69 ATOM 691 N PHE A 86 22.667 13.254 40.016 1.00 7.32 ATOM 692 CA PHE A 86 23.518 14.113 39.200 1.00 7.73 ATOM 693 C PHE A 86 22.855 15.450 38.915 1.00 8.12 ATOM 694 O PHE A 86 23.539 16.482 38.861 1.00 9.04 ATOM 695 CB PHE A 86 23.832 13.426 37.859 1.00 8.05 ATOM 696 CG PHE A 86 24.840 12.302 37.908 1.00 8.07 ATOM 697 CD1 PHE A 86 25.320 11.749 39.097 1.00 7.85 ATOM 698 CD2 PHE A 86 25.316 11.774 36.724 1.00 9.27 ATOM 699 CE1 PHE A 86 26.264 10.734 39.052 1.00 8.77 ATOM 700 CE2 PHE A 86 26.260 10.753 36.695 1.00 9.37 ATOM 701 CZ PHE A 86 26.743 10.244 37.856 1.00 9.15 ATOM 702 N GLU A 87 21.537 15.451 38.722 1.00 8.31 ATOM 703 CA GLU A 87 20.784 16.697 38.539 1.00 8.60 ATOM 704 C GLU A 87 20.932 17.569 39.778 1.00 8.91 ATOM 705 O GLU A 87 21.183 18.772 39.665 1.00 10.15 ATOM 706 CB GLU A 87 19.318 16.376 38.257 1.00 8.96 ATOM 707 CG GLU A 87 18.444 17.583 38.111 1.00 10.44 ATOM 708 CD GLU A 87 16.991 17.230 37.905 1.00 11.61 ATOM 709 OE1 GLU A 87 16.611 16.035 37.817 1.00 12.33 ATOM 710 OE2 GLU A 87 16.198 18.192 37.855 1.00 13.81 ATOM 711 N LEU A 88 20.769 16.987 40.955 1.00 8.50 ATOM 712 CA LEU A 88 20.899 17.770 42.190 1.00 8.82 ATOM 713 C LEU A 88 22.327 18.333 42.311 1.00 8.82 ATOM 714 O LEU A 88 22.521 19.457 42.759 1.00 9.86 ATOM 715 CB LEU A 88 20.596 16.886 43.396 1.00 9.01 ATOM 716 CG LEU A 88 19.125 16.432 43.487 1.00 10.23 ATOM 717 CD1 LEU A 88 18.945 15.515 44.671 1.00 11.39 ATOM 718 CD2 LEU A 88 18.158 17.644 43.504 1.00 12.24 ATOM 719 N MET A 89 23.334 17.558 41.915 1.00 8.69 ATOM 720 CA MET A 89 24.699 18.074 41.918 1.00 8.97 ATOM 721 C MET A 89 24.813 19.312 41.061 1.00 9.15 ATOM 722 O MET A 89 25.382 20.321 41.493 1.00 10.55 ATOM 723 CB MET A 89 25.673 17.020 41.394 1.00 8.74 ATOM 724 CG MET A 89 25.800 15.819 42.347 1.00 8.78 ATOM 725 SD MET A 89 26.765 14.486 41.640 1.00 8.61 ATOM 726 CE MET A 89 26.164 13.104 42.631 1.00 8.76 ATOM 727 N GLN A 90 24.312 19.238 39.840 1.00 9.74 ATOM 728 CA GLN A 90 24.381 20.365 38.916 1.00 10.48 ATOM 729 C GLN A 90 23.532 21.530 39.354 1.00 10.98 ATOM 730 O GLN A 90 23.987 22.686 39.222 1.00 12.59 ATOM 731 CB GLN A 90 24.031 19.903 37.502 1.00 10.60 ATOM 732 CG GLN A 90 25.075 18.949 36.944 1.00 12.09 ATOM 733 CD GLN A 90 24.605 18.217 35.714 1.00 13.81 ATOM 734 OE1 GLN A 90 24.621 18.735 34.588 1.00 17.26 ATOM 735 NE2 GLN A 90 24.153 17.000 35.922 1.00 15.07 ATOM 736 N ASP A 91 22.377 21.271 39.955 1.00 10.98 ATOM 737 CA ASP A 91 21.537 22.333 40.459 1.00 11.33 ATOM 738 C ASP A 91 22.322 23.139 41.505 1.00 12.29 ATOM 739 O ASP A 91 22.132 24.356 41.623 1.00 14.27 ATOM 740 CB ASP A 91 20.263 21.802 41.111 1.00 11.96 ATOM 741 CG ASP A 91 19.251 21.237 40.114 0.96 11.68 ATOM 742 OD1 ASP A 91 19.370 21.450 38.885 0.96 13.18 ATOM 743 OD2 ASP A 91 18.309 20.604 40.622 0.96 14.95 ATOM 744 N GLY A 92 23.191 22.470 42.261 1.00 11.73 ATOM 745 CA GLY A 92 23.989 23.097 43.300 1.00 12.49 ATOM 746 C GLY A 92 25.239 23.744 42.793 1.00 12.90 ATOM 747 O GLY A 92 25.987 24.354 43.587 1.00 14.65 ATOM 748 N GLY A 93 25.526 23.626 41.510 1.00 13.18 ATOM 749 CA GLY A 93 26.658 24.326 40.942 1.00 13.61 ATOM 750 C GLY A 93 27.801 23.462 40.472 1.00 13.02 ATOM 751 O GLY A 93 28.754 23.971 39.871 1.00 15.67 ATOM 752 N LEU A 94 27.777 22.148 40.736 0.72 12.73 ATOM 753 CA LEU A 94 28.827 21.289 40.185 0.72 12.73 ATOM 754 C LEU A 94 28.693 21.161 38.681 0.72 12.21 ATOM 755 O LEU A 94 27.587 21.178 38.144 0.72 12.42 ATOM 756 CB LEU A 94 28.785 19.877 40.805 0.72 12.66 ATOM 757 CG LEU A 94 29.496 19.736 42.163 0.72 15.20 ATOM 758 CD1 LEU A 94 29.126 18.424 42.823 0.72 16.59 ATOM 759 CD2 LEU A 94 31.000 19.883 42.054 0.72 16.05 ATOM 760 N GLU A 95 29.829 20.975 38.011 0.72 12.56 ATOM 761 CA GLU A 95 29.810 20.581 36.607 0.72 13.74 ATOM 762 C GLU A 95 29.166 19.189 36.434 0.72 12.67 ATOM 763 O GLU A 95 29.216 18.347 37.358 0.72 13.24 ATOM 764 CB GLU A 95 31.243 20.554 36.088 0.72 15.05 ATOM 765 CG GLU A 95 31.994 21.901 36.228 0.72 19.45 ATOM 766 CD GLU A 95 32.699 22.129 37.586 0.36 20.92 ATOM 767 OE1 GLU A 95 32.442 21.408 38.585 0.36 20.73 ATOM 768 OE2 GLU A 95 33.531 23.065 37.651 0.36 23.46 ATOM 769 N LYS A 96 28.592 18.914 35.265 0.72 12.34 ATOM 770 CA LYS A 96 28.043 17.592 35.018 0.72 11.94 ATOM 771 C LYS A 96 29.169 16.603 35.312 0.72 11.19 ATOM 772 O LYS A 96 30.289 16.788 34.855 0.72 11.49 ATOM 773 CB LYS A 96 27.544 17.433 33.570 0.72 11.38 ATOM 774 CG LYS A 96 26.786 16.148 33.300 0.72 11.90 ATOM 775 CD LYS A 96 26.404 15.941 31.850 0.72 10.82 ATOM 776 CE LYS A 96 27.608 15.630 30.987 0.72 12.23 ATOM 777 NZ LYS A 96 27.079 15.133 29.643 0.72 12.60 ATOM 778 N PRO A 97 28.890 15.571 36.086 1.00 10.88 ATOM 779 CA PRO A 97 29.854 14.470 36.297 1.00 10.06 ATOM 780 C PRO A 97 30.351 13.858 35.008 1.00 10.80 ATOM 781 O PRO A 97 29.653 13.851 33.981 1.00 11.57 ATOM 782 CB PRO A 97 29.040 13.475 37.106 1.00 10.20 ATOM 783 CG PRO A 97 28.083 14.305 37.870 1.00 10.35 ATOM 784 CD PRO A 97 27.666 15.362 36.868 1.00 11.01 ATOM 785 N LYS A 98 31.602 13.403 35.065 0.40 10.21 ATOM 786 CA LYS A 98 32.233 12.670 33.974 0.40 10.78 ATOM 787 C LYS A 98 31.496 11.381 33.652 0.40 9.89 ATOM 788 O LYS A 98 31.062 11.207 32.525 0.40 10.45 ATOM 789 CB LYS A 98 33.731 12.414 34.229 0.40 11.11 ATOM 790 CG LYS A 98 34.606 13.614 33.903 0.40 12.40 ATOM 791 CD LYS A 98 36.084 13.407 34.181 0.40 11.66 ATOM 792 CE LYS A 98 36.886 14.602 33.713 0.40 13.78 ATOM 793 NZ LYS A 98 38.337 14.454 34.038 0.40 16.30 ATOM 794 N PRO A 99 31.314 10.483 34.630 1.00 9.40 ATOM 795 CA PRO A 99 30.703 9.196 34.317 1.00 9.63 ATOM 796 C PRO A 99 29.260 9.324 33.841 1.00 9.38 ATOM 797 O PRO A 99 28.558 10.237 34.232 1.00 11.08 ATOM 798 CB PRO A 99 30.736 8.433 35.641 1.00 10.31 ATOM 799 CG PRO A 99 31.811 9.144 36.468 1.00 11.00 ATOM 800 CD PRO A 99 31.679 10.592 36.054 1.00 10.29 ATOM 801 N ARG A 100 28.882 8.397 32.960 0.52 8.26 ATOM 802 CA ARG A 100 27.458 8.117 32.651 0.52 8.53 ATOM 803 C ARG A 100 26.743 7.679 33.919 0.52 7.50 ATOM 804 O ARG A 100 27.363 7.064 34.791 0.52 7.49 ATOM 805 CB ARG A 100 27.284 7.028 31.565 0.52 7.91 ATOM 806 CG ARG A 100 28.034 7.319 30.287 0.52 9.51 ATOM 807 CD ARG A 100 27.853 8.704 29.893 0.52 11.66 ATOM 808 NE ARG A 100 26.445 8.869 29.564 0.52 11.00 ATOM 809 CZ ARG A 100 25.771 9.995 29.680 0.52 12.16 ATOM 810 NH1 ARG A 100 26.418 11.084 30.064 0.52 12.14 ATOM 811 NH2 ARG A 100 24.445 10.000 29.441 0.52 12.57 ATOM 812 N PRO A 101 25.425 7.939 34.050 0.52 8.34 ATOM 813 CA PRO A 101 24.728 7.507 35.270 0.52 8.00 ATOM 814 C PRO A 101 24.721 5.984 35.411 0.52 7.95 ATOM 815 O PRO A 101 24.848 5.442 36.516 0.52 8.03 ATOM 816 CB PRO A 101 23.338 8.124 35.124 0.52 8.22 ATOM 817 CG PRO A 101 23.156 8.321 33.655 0.52 8.19 ATOM 818 CD PRO A 101 24.539 8.677 33.134 0.52 8.09 ATOM 819 N GLU A 102 24.622 5.297 34.278 1.00 8.57 ATOM 820 CA GLU A 102 24.661 3.845 34.277 1.00 8.93 ATOM 821 C GLU A 102 26.010 3.291 34.707 1.00 8.45 ATOM 822 O GLU A 102 26.080 2.135 35.107 1.00 8.83 ATOM 823 CB GLU A 102 24.261 3.254 32.952 1.00 9.99 ATOM 824 CG GLU A 102 25.134 3.527 31.773 1.00 11.93 ATOM 825 CD GLU A 102 24.876 4.814 31.036 0.89 13.90 ATOM 826 OE1 GLU A 102 24.161 5.718 31.554 0.89 12.87 ATOM 827 OE2 GLU A 102 25.426 4.908 29.901 0.89 17.31 ATOM 828 N ASP A 103 27.081 4.090 34.615 1.00 8.55 ATOM 829 CA ASP A 103 28.385 3.610 35.083 1.00 8.65 ATOM 830 C ASP A 103 28.359 3.327 36.598 1.00 7.83 ATOM 831 O ASP A 103 29.043 2.442 37.077 1.00 9.08 ATOM 832 CB ASP A 103 29.489 4.613 34.718 1.00 8.52 ATOM 833 CG ASP A 103 29.676 4.798 33.220 1.00 10.32 ATOM 834 OD1 ASP A 103 29.236 3.925 32.408 1.00 13.37 ATOM 835 OD2 ASP A 103 30.264 5.846 32.857 1.00 11.10 ATOM 836 N ILE A 104 27.629 4.165 37.320 0.89 7.57 ATOM 837 CA ILE A 104 27.438 3.990 38.753 0.89 7.80 ATOM 838 C ILE A 104 26.568 2.735 38.983 0.89 7.26 ATOM 839 O ILE A 104 26.876 1.883 39.829 0.89 7.64 ATOM 840 CB ILE A 104 26.736 5.243 39.371 0.89 8.79 ATOM 841 CG1 ILE A 104 27.500 6.537 39.080 0.89 10.30 ATOM 842 CG2 ILE A 104 26.436 5.015 40.846 0.89 9.25 ATOM 843 CD ILE A 104 28.805 6.491 39.590 0.89 12.97 ATOM 844 N VAL A 105 25.471 2.599 38.229 0.89 7.45 ATOM 845 CA VAL A 105 24.592 1.439 38.380 0.89 7.62 ATOM 846 C VAL A 105 25.340 0.144 38.089 0.89 7.63 ATOM 847 O VAL A 105 25.109 -0.866 38.737 0.89 8.21 ATOM 848 CB VAL A 105 23.337 1.601 37.487 0.89 7.21 ATOM 849 CG1 VAL A 105 22.435 0.366 37.674 0.89 8.24 ATOM 850 CG2 VAL A 105 22.616 2.884 37.947 0.89 7.71 ATOM 851 N ASN A 106 26.234 0.184 37.111 1.00 7.80 ATOM 852 CA ASN A 106 27.041 -0.958 36.702 1.00 8.00 ATOM 853 C ASN A 106 28.265 -1.163 37.587 1.00 8.48 ATOM 854 O ASN A 106 29.114 -1.990 37.268 1.00 9.79 ATOM 855 CB ASN A 106 27.431 -0.828 35.239 1.00 8.72 ATOM 856 CG ASN A 106 26.242 -1.040 34.318 1.00 8.98 ATOM 857 OD1 ASN A 106 25.375 -1.876 34.587 1.00 11.33 ATOM 858 ND2 ASN A 106 26.221 -0.315 33.232 1.00 9.91 ATOM 859 N CYS A 107 28.335 -0.464 38.707 1.00 8.13 ATOM 860 CA CYS A 107 29.360 -0.717 39.714 1.00 8.74 ATOM 861 C CYS A 107 30.767 -0.496 39.166 1.00 8.39 ATOM 862 O CYS A 107 31.718 -1.177 39.586 1.00 9.98 ATOM 863 CB CYS A 107 29.229 -2.138 40.341 1.00 9.87 ATOM 864 SG CYS A 107 27.700 -2.387 41.210 1.00 11.23 ATOM 865 N ASP A 108 30.958 0.502 38.319 1.00 8.91 ATOM 866 CA ASP A 108 32.323 0.888 37.941 1.00 8.48 ATOM 867 C ASP A 108 32.948 1.652 39.100 1.00 7.98 ATOM 868 O ASP A 108 32.480 2.743 39.470 1.00 8.17 ATOM 869 CB ASP A 108 32.336 1.734 36.684 1.00 9.14 ATOM 870 CG ASP A 108 33.760 2.067 36.301 0.98 9.64 ATOM 871 OD1 ASP A 108 34.539 1.123 36.061 0.98 11.32 ATOM 872 OD2 ASP A 108 34.153 3.259 36.343 0.98 9.77 ATOM 873 N LEU A 109 34.004 1.094 39.713 1.00 8.31 ATOM 874 CA LEU A 109 34.536 1.683 40.927 1.00 8.06 ATOM 875 C LEU A 109 35.136 3.053 40.690 1.00 8.09 ATOM 876 O LEU A 109 34.882 3.975 41.468 1.00 8.14 ATOM 877 CB LEU A 109 35.551 0.763 41.593 1.00 9.28 ATOM 878 CG LEU A 109 36.076 1.251 42.949 1.00 9.41 ATOM 879 CD1 LEU A 109 34.957 1.386 43.973 1.00 10.10 ATOM 880 CD2 LEU A 109 37.175 0.278 43.443 1.00 11.69 ATOM 881 N LYS A 110 35.943 3.256 39.643 0.44 8.55 ATOM 882 CA LYS A 110 36.536 4.591 39.455 0.44 8.56 ATOM 883 C LYS A 110 35.422 5.617 39.324 0.44 7.74 ATOM 884 O LYS A 110 35.465 6.662 39.952 0.44 7.90 ATOM 885 CB LYS A 110 37.469 4.691 38.241 0.44 9.22 ATOM 886 CG LYS A 110 38.065 6.104 38.063 0.44 10.40 ATOM 887 CD LYS A 110 39.129 6.177 37.004 0.44 10.61 ATOM 888 CE LYS A 110 38.638 5.914 35.674 0.44 11.76 ATOM 889 NZ LYS A 110 39.750 5.982 34.671 0.44 14.60 ATOM 890 N SER A 111 34.414 5.311 38.513 1.00 8.03 ATOM 891 CA SER A 111 33.319 6.273 38.335 1.00 8.00 ATOM 892 C SER A 111 32.684 6.655 39.658 1.00 7.66 ATOM 893 O SER A 111 32.392 7.802 39.924 1.00 7.88 ATOM 894 CB SER A 111 32.230 5.687 37.430 1.00 8.29 ATOM 895 OG SER A 111 32.680 5.440 36.116 1.00 9.94 ATOM 896 N THR A 112 32.417 5.637 40.464 1.00 7.61 ATOM 897 CA THR A 112 31.738 5.828 41.750 1.00 7.56 ATOM 898 C THR A 112 32.621 6.689 42.662 1.00 6.77 ATOM 899 O THR A 112 32.170 7.634 43.283 1.00 7.61 ATOM 900 CB THR A 112 31.444 4.486 42.390 1.00 8.03 ATOM 901 OG1 THR A 112 30.653 3.706 41.467 1.00 8.74 ATOM 902 CG2 THR A 112 30.700 4.602 43.715 1.00 9.45 ATOM 903 N LEU A 113 33.902 6.313 42.751 1.00 7.36 ATOM 904 CA LEU A 113 34.822 7.059 43.618 1.00 7.54 ATOM 905 C LEU A 113 35.017 8.481 43.125 1.00 7.37 ATOM 906 O LEU A 113 35.149 9.401 43.931 1.00 8.00 ATOM 907 CB LEU A 113 36.156 6.359 43.770 1.00 7.85 ATOM 908 CG LEU A 113 36.069 4.966 44.350 1.00 8.98 ATOM 909 CD1 LEU A 113 37.516 4.383 44.500 1.00 10.41 ATOM 910 CD2 LEU A 113 35.339 4.881 45.716 1.00 10.13 ATOM 911 N ARG A 114 35.087 8.731 41.813 0.55 7.44 ATOM 912 CA ARG A 114 35.275 10.105 41.327 0.55 7.48 ATOM 913 C ARG A 114 34.085 10.946 41.751 0.55 7.21 ATOM 914 O ARG A 114 34.219 12.069 42.248 0.55 7.58 ATOM 915 CB ARG A 114 35.423 10.155 39.800 0.55 7.90 ATOM 916 CG ARG A 114 35.562 11.546 39.238 0.55 8.46 ATOM 917 CD ARG A 114 35.674 11.529 37.734 0.55 8.77 ATOM 918 NE ARG A 114 36.906 10.919 37.209 0.55 8.32 ATOM 919 CZ ARG A 114 38.074 11.545 37.138 0.55 10.20 ATOM 920 NH1 ARG A 114 38.180 12.807 37.605 0.55 10.11 ATOM 921 NH2 ARG A 114 39.098 10.879 36.583 0.55 11.23 ATOM 922 N VAL A 115 32.878 10.411 41.526 1.00 7.25 ATOM 923 CA VAL A 115 31.709 11.177 41.894 1.00 7.64 ATOM 924 C VAL A 115 31.718 11.495 43.372 1.00 7.09 ATOM 925 O VAL A 115 31.449 12.635 43.769 1.00 7.55 ATOM 926 CB VAL A 115 30.421 10.421 41.439 1.00 8.22 ATOM 927 CG1 VAL A 115 29.201 10.963 42.119 1.00 9.00 ATOM 928 CG2 VAL A 115 30.317 10.511 39.920 1.00 9.69 ATOM 929 N LEU A 116 31.985 10.505 44.211 1.00 6.98 ATOM 930 CA LEU A 116 32.012 10.744 45.634 1.00 7.36 ATOM 931 C LEU A 116 33.127 11.703 46.042 1.00 7.14 ATOM 932 O LEU A 116 32.944 12.532 46.934 1.00 8.05 ATOM 933 CB LEU A 116 32.114 9.429 46.398 1.00 7.45 ATOM 934 CG LEU A 116 30.909 8.494 46.296 1.00 8.02 ATOM 935 CD1 LEU A 116 31.230 7.181 46.988 1.00 9.54 ATOM 936 CD2 LEU A 116 29.661 9.128 46.864 1.00 9.23 ATOM 937 N TYR A 117 34.286 11.572 45.413 1.00 7.67 ATOM 938 CA TYR A 117 35.426 12.445 45.731 1.00 8.05 ATOM 939 C TYR A 117 35.093 13.900 45.419 1.00 8.09 ATOM 940 O TYR A 117 35.455 14.803 46.178 1.00 8.68 ATOM 941 CB TYR A 117 36.669 11.959 44.970 1.00 8.79 ATOM 942 CG TYR A 117 37.903 12.678 45.437 1.00 10.36 ATOM 943 CD1 TYR A 117 38.461 12.399 46.692 1.00 16.62 ATOM 944 CD2 TYR A 117 38.446 13.727 44.719 1.00 13.34 ATOM 945 CE1 TYR A 117 39.582 13.110 47.172 1.00 17.69 ATOM 946 CE2 TYR A 117 39.608 14.412 45.178 1.00 14.70 ATOM 947 CZ TYR A 117 40.153 14.079 46.394 1.00 15.04 ATOM 948 OH TYR A 117 41.255 14.776 46.879 1.00 17.05 ATOM 949 N ASN A 118 34.408 14.157 44.289 1.00 8.07 ATOM 950 CA ASN A 118 34.061 15.520 43.977 1.00 8.32 ATOM 951 C ASN A 118 33.045 16.075 44.974 1.00 8.28 ATOM 952 O ASN A 118 33.064 17.291 45.276 1.00 9.83 ATOM 953 CB ASN A 118 33.556 15.652 42.557 1.00 9.01 ATOM 954 CG ASN A 118 34.649 15.425 41.539 1.00 9.71 ATOM 955 OD1 ASN A 118 35.826 15.649 41.809 1.00 12.54 ATOM 956 ND2 ASN A 118 34.280 15.025 40.339 1.00 10.49 ATOM 957 N LEU A 119 32.174 15.228 45.529 1.00 7.84 ATOM 958 CA LEU A 119 31.328 15.674 46.598 1.00 7.70 ATOM 959 C LEU A 119 32.130 15.999 47.836 1.00 8.01 ATOM 960 O LEU A 119 31.870 16.989 48.509 1.00 8.87 ATOM 961 CB LEU A 119 30.256 14.614 46.961 1.00 7.46 ATOM 962 CG LEU A 119 29.282 14.278 45.812 1.00 7.86 ATOM 963 CD1 LEU A 119 28.258 13.261 46.336 1.00 8.65 ATOM 964 CD2 LEU A 119 28.617 15.520 45.266 1.00 9.89 ATOM 965 N PHE A 120 33.076 15.139 48.199 1.00 7.88 ATOM 966 CA PHE A 120 33.915 15.387 49.377 1.00 8.22 ATOM 967 C PHE A 120 34.663 16.709 49.249 1.00 8.67 ATOM 968 O PHE A 120 34.691 17.496 50.182 1.00 9.25 ATOM 969 CB PHE A 120 34.911 14.204 49.527 1.00 7.84 ATOM 970 CG PHE A 120 35.914 14.399 50.633 1.00 8.00 ATOM 971 CD1 PHE A 120 35.528 14.399 51.962 1.00 8.72 ATOM 972 CD2 PHE A 120 37.251 14.644 50.344 1.00 8.77 ATOM 973 CE1 PHE A 120 36.441 14.594 52.984 1.00 8.91 ATOM 974 CE2 PHE A 120 38.162 14.857 51.369 1.00 9.71 ATOM 975 CZ PHE A 120 37.750 14.815 52.656 1.00 9.88 ATOM 976 N THR A 121 35.259 16.973 48.113 0.48 9.07 ATOM 977 CA THR A 121 36.084 18.163 48.052 0.48 10.49 ATOM 978 C THR A 121 35.228 19.439 48.100 0.48 10.80 ATOM 979 O THR A 121 35.700 20.470 48.587 0.48 10.75 ATOM 980 CB THR A 121 37.015 18.135 46.854 0.48 11.90 ATOM 981 OG1 THR A 121 36.251 18.266 45.657 0.48 14.21 ATOM 982 CG2 THR A 121 37.774 16.826 46.783 0.48 12.32 ATOM 983 N LYS A 122 33.982 19.382 47.616 1.00 10.20 ATOM 984 CA LYS A 122 33.082 20.525 47.726 1.00 10.47 ATOM 985 C LYS A 122 32.459 20.665 49.117 1.00 10.23 ATOM 986 O LYS A 122 32.301 21.780 49.618 1.00 11.31 ATOM 987 CB LYS A 122 31.985 20.452 46.643 1.00 10.34 ATOM 988 CG LYS A 122 30.978 21.577 46.753 1.00 11.43 ATOM 989 CD LYS A 122 30.096 21.695 45.531 1.00 12.13 ATOM 990 CE LYS A 122 29.076 22.804 45.746 1.00 14.36 ATOM 991 NZ LYS A 122 28.257 23.062 44.507 1.00 17.20 ATOM 992 N TYR A 123 32.034 19.543 49.690 1.00 9.06 ATOM 993 CA TYR A 123 31.138 19.540 50.828 1.00 8.96 ATOM 994 C TYR A 123 31.771 19.062 52.134 1.00 8.66 ATOM 995 O TYR A 123 31.065 18.817 53.099 1.00 9.35 ATOM 996 CB TYR A 123 29.903 18.684 50.495 1.00 9.24 ATOM 997 CG TYR A 123 29.003 19.230 49.420 1.00 9.13 ATOM 998 CD1 TYR A 123 28.092 20.234 49.678 1.00 10.31 ATOM 999 CD2 TYR A 123 28.939 18.616 48.171 1.00 9.65 ATOM 1000 CE1 TYR A 123 27.177 20.642 48.691 1.00 11.04 ATOM 1001 CE2 TYR A 123 28.037 19.013 47.199 1.00 9.77 ATOM 1002 CZ TYR A 123 27.126 19.997 47.480 1.00 11.91 ATOM 1003 OH TYR A 123 26.211 20.323 46.513 1.00 13.32 ATOM 1004 N ARG A 124 33.109 18.917 52.165 1.00 8.89 ATOM 1005 CA ARG A 124 33.751 18.388 53.364 1.00 9.11 ATOM 1006 C ARG A 124 33.469 19.200 54.617 1.00 9.97 ATOM 1007 O ARG A 124 33.588 18.658 55.705 1.00 11.61 ATOM 1008 CB ARG A 124 35.264 18.204 53.173 1.00 9.31 ATOM 1009 CG ARG A 124 36.055 19.484 52.882 1.00 10.04 ATOM 1010 CD ARG A 124 37.563 19.186 52.665 1.00 10.20 ATOM 1011 NE ARG A 124 38.119 18.659 53.906 1.00 10.38 ATOM 1012 CZ ARG A 124 39.157 17.819 53.990 1.00 9.69 ATOM 1013 NH1 ARG A 124 39.845 17.478 52.902 1.00 11.02 ATOM 1014 NH2 ARG A 124 39.521 17.296 55.169 1.00 10.36 ATOM 1015 N ASN A 125 33.091 20.474 54.499 1.00 10.11 ATOM 1016 CA ASN A 125 32.788 21.294 55.694 1.00 11.40 ATOM 1017 C ASN A 125 31.328 21.334 56.110 1.00 11.64 ATOM 1018 O ASN A 125 30.998 21.976 57.108 1.00 14.26 ATOM 1019 CB ASN A 125 33.305 22.708 55.510 1.00 11.08 ATOM 1020 CG ASN A 125 34.787 22.726 55.378 1.00 12.48 ATOM 1021 OD1 ASN A 125 35.331 23.355 54.470 1.00 16.06 ATOM 1022 ND2 ASN A 125 35.446 22.014 56.244 1.00 11.00 ATOM 1023 N VAL A 126 30.446 20.645 55.391 1.00 11.51 ATOM 1024 CA VAL A 126 29.058 20.529 55.826 1.00 12.47 ATOM 1025 C VAL A 126 29.026 19.696 57.105 1.00 12.58 ATOM 1026 O VAL A 126 29.554 18.593 57.171 1.00 14.05 ATOM 1027 CB VAL A 126 28.208 19.916 54.746 1.00 12.34 ATOM 1028 CG1 VAL A 126 26.761 19.696 55.281 1.00 14.01 ATOM 1029 CG2 VAL A 126 28.222 20.828 53.536 1.00 13.76 ATOM 1030 N GLU A 127 28.386 20.232 58.145 1.00 14.65 ATOM 1031 CA GLU A 127 28.350 19.511 59.409 1.00 16.36 ATOM 1032 C GLU A 127 27.434 18.296 59.408 1.00 18.11 ATOM 1033 O GLU A 127 26.450 18.317 58.669 1.00 17.73 ATOM 1034 CB GLU A 127 27.910 20.450 60.526 1.00 18.38 ATOM 1035 CG GLU A 127 28.826 21.611 60.772 1.00 21.84 ATOM 1036 CD GLU A 127 30.099 21.241 61.526 0.50 24.83 ATOM 1037 OE1 GLU A 127 30.164 20.141 62.115 0.50 27.43 ATOM 1038 OE2 GLU A 127 31.045 22.061 61.530 0.50 27.18 ATOM 1039 OT2 GLU A 127 27.689 17.313 60.144 1.00 20.97 TER END