ATOM 1 N VAL A 1 8.234 26.669 22.509 1.00 15.90 ATOM 2 CA VAL A 1 7.771 26.928 21.151 1.00 15.50 ATOM 3 C VAL A 1 8.817 26.610 20.079 1.00 14.71 ATOM 4 O VAL A 1 8.448 26.375 18.933 1.00 15.47 ATOM 5 CB VAL A 1 7.261 28.389 20.944 1.00 14.65 ATOM 6 CG1 VAL A 1 5.886 28.625 21.628 1.00 16.64 ATOM 7 CG2 VAL A 1 8.307 29.402 21.380 1.00 14.98 ATOM 8 N ALA A 2 10.107 26.626 20.437 1.00 13.76 ATOM 9 CA ALA A 2 11.159 26.308 19.463 1.00 13.23 ATOM 10 C ALA A 2 11.626 24.871 19.603 1.00 12.59 ATOM 11 O ALA A 2 12.215 24.503 20.616 1.00 13.24 ATOM 12 CB ALA A 2 12.330 27.274 19.597 1.00 13.83 ATOM 13 N ILE A 3 11.344 24.075 18.576 1.00 11.66 ATOM 14 CA ILE A 3 11.581 22.631 18.580 1.00 11.72 ATOM 15 C ILE A 3 12.783 22.267 17.701 1.00 11.25 ATOM 16 O ILE A 3 12.866 22.672 16.543 1.00 10.43 ATOM 17 CB ILE A 3 10.347 21.866 18.079 1.00 12.44 ATOM 18 CG1 ILE A 3 9.109 22.214 18.907 1.00 13.81 ATOM 19 CG2 ILE A 3 10.618 20.347 18.033 1.00 13.22 ATOM 20 CD ILE A 3 7.797 21.867 18.223 1.00 17.38 ATOM 21 N LYS A 4 13.707 21.477 18.243 1.00 11.29 ATOM 22 CA LYS A 4 14.914 21.110 17.501 1.00 11.97 ATOM 23 C LYS A 4 14.668 20.094 16.385 1.00 12.30 ATOM 24 O LYS A 4 13.999 19.078 16.593 1.00 13.74 ATOM 25 CB LYS A 4 15.997 20.585 18.447 1.00 12.54 ATOM 26 CG LYS A 4 17.379 20.560 17.796 1.00 16.00 ATOM 27 CD LYS A 4 18.471 20.253 18.799 1.00 21.41 ATOM 28 CE LYS A 4 18.377 18.841 19.294 1.00 25.37 ATOM 29 NZ LYS A 4 19.217 18.705 20.523 1.00 28.70 ATOM 30 N LEU A 5 15.218 20.388 15.205 1.00 12.34 ATOM 31 CA LEU A 5 15.275 19.429 14.087 1.00 12.59 ATOM 32 C LEU A 5 16.635 18.760 14.045 1.00 13.37 ATOM 33 O LEU A 5 17.667 19.416 14.198 1.00 13.81 ATOM 34 CB LEU A 5 15.061 20.148 12.754 1.00 13.12 ATOM 35 CG LEU A 5 13.753 20.910 12.557 1.00 13.38 ATOM 36 CD1 LEU A 5 13.890 21.864 11.384 1.00 16.18 ATOM 37 CD2 LEU A 5 12.593 19.953 12.345 1.00 16.05 ATOM 38 N SER A 6 16.629 17.445 13.834 1.00 14.80 ATOM 39 CA SER A 6 17.888 16.696 13.776 1.00 16.00 ATOM 40 C SER A 6 18.119 15.953 12.469 1.00 15.95 ATOM 41 O SER A 6 19.113 15.232 12.347 1.00 17.16 ATOM 42 CB SER A 6 17.959 15.690 14.925 1.00 16.89 ATOM 43 OG SER A 6 16.897 14.755 14.841 1.00 21.34 ATOM 44 N SER A 7 17.206 16.091 11.507 1.00 14.57 ATOM 45 CA SER A 7 17.399 15.434 10.218 1.00 14.30 ATOM 46 C SER A 7 16.676 16.098 9.080 1.00 13.84 ATOM 47 O SER A 7 15.696 16.825 9.273 1.00 13.35 ATOM 48 CB SER A 7 16.969 13.963 10.294 1.00 14.61 ATOM 49 OG SER A 7 15.560 13.827 10.454 1.00 14.96 ATOM 50 N ILE A 8 17.152 15.795 7.876 1.00 13.90 ATOM 51 CA ILE A 8 16.445 16.168 6.658 1.00 13.88 ATOM 52 C ILE A 8 15.014 15.565 6.631 1.00 13.81 ATOM 53 O ILE A 8 14.063 16.260 6.279 1.00 13.61 ATOM 54 CB ILE A 8 17.269 15.774 5.403 1.00 13.82 ATOM 55 CG1 ILE A 8 18.562 16.575 5.370 1.00 14.25 ATOM 56 CG2 ILE A 8 16.473 16.022 4.119 1.00 14.19 ATOM 57 CD ILE A 8 19.594 16.030 4.447 1.00 15.85 ATOM 58 N ASP A 9 14.851 14.306 7.058 1.00 13.98 ATOM 59 CA ASP A 9 13.527 13.680 7.154 1.00 14.51 ATOM 60 C ASP A 9 12.544 14.532 7.979 1.00 15.05 ATOM 61 O ASP A 9 11.403 14.762 7.570 1.00 15.74 ATOM 62 CB ASP A 9 13.627 12.311 7.855 1.00 15.19 ATOM 63 CG ASP A 9 14.009 11.175 6.936 1.00 16.46 ATOM 64 OD1 ASP A 9 13.813 11.257 5.720 1.00 18.49 ATOM 65 OD2 ASP A 9 14.478 10.149 7.467 1.00 17.41 ATOM 66 N GLN A 10 12.984 14.987 9.151 0.50 14.93 ATOM 67 CA GLN A 10 12.120 15.786 10.025 0.50 14.56 ATOM 68 C GLN A 10 11.808 17.150 9.443 0.50 14.31 ATOM 69 O GLN A 10 10.677 17.627 9.569 0.50 14.68 ATOM 70 CB GLN A 10 12.746 15.963 11.403 0.50 14.74 ATOM 71 CG GLN A 10 12.916 14.687 12.156 0.50 15.19 ATOM 72 CD GLN A 10 13.566 14.914 13.504 0.50 16.07 ATOM 73 OE1 GLN A 10 13.947 16.044 13.851 0.50 15.65 ATOM 74 NE2 GLN A 10 13.675 13.847 14.287 0.50 17.51 ATOM 75 N PHE A 11 12.811 17.775 8.821 1.00 14.06 ATOM 76 CA PHE A 11 12.604 19.066 8.143 1.00 13.43 ATOM 77 C PHE A 11 11.530 18.948 7.065 1.00 13.80 ATOM 78 O PHE A 11 10.560 19.723 7.064 1.00 13.82 ATOM 79 CB PHE A 11 13.914 19.632 7.594 1.00 13.67 ATOM 80 CG PHE A 11 13.727 20.803 6.691 1.00 13.61 ATOM 81 CD1 PHE A 11 13.438 22.063 7.209 1.00 13.14 ATOM 82 CD2 PHE A 11 13.807 20.649 5.309 1.00 13.94 ATOM 83 CE1 PHE A 11 13.252 23.140 6.369 1.00 12.60 ATOM 84 CE2 PHE A 11 13.616 21.730 4.457 1.00 14.51 ATOM 85 CZ PHE A 11 13.330 22.990 4.994 1.00 13.87 ATOM 86 N GLU A 12 11.666 17.962 6.183 1.00 14.71 ATOM 87 CA GLU A 12 10.639 17.760 5.158 1.00 15.74 ATOM 88 C GLU A 12 9.281 17.428 5.770 1.00 16.17 ATOM 89 O GLU A 12 8.241 17.880 5.265 1.00 16.14 ATOM 90 CB GLU A 12 11.080 16.758 4.066 1.00 16.22 ATOM 91 CG GLU A 12 12.132 17.346 3.123 1.00 16.80 ATOM 92 CD GLU A 12 11.568 18.280 2.034 1.00 17.89 ATOM 93 OE1 GLU A 12 10.343 18.283 1.812 1.00 18.13 ATOM 94 OE2 GLU A 12 12.362 18.991 1.376 1.00 19.21 ATOM 95 N GLN A 13 9.278 16.647 6.849 0.50 16.18 ATOM 96 CA GLN A 13 8.032 16.294 7.522 0.50 16.18 ATOM 97 C GLN A 13 7.341 17.532 8.077 0.50 16.19 ATOM 98 O GLN A 13 6.134 17.709 7.930 0.50 15.81 ATOM 99 CB GLN A 13 8.286 15.289 8.647 0.50 17.11 ATOM 100 CG GLN A 13 7.020 14.810 9.323 0.50 17.66 ATOM 101 CD GLN A 13 6.255 13.787 8.496 0.50 19.53 ATOM 102 OE1 GLN A 13 6.728 13.333 7.455 0.50 19.55 ATOM 103 NE2 GLN A 13 5.071 13.413 8.965 0.50 20.55 ATOM 104 N VAL A 14 8.119 18.397 8.707 0.50 15.28 ATOM 105 CA VAL A 14 7.549 19.568 9.348 0.50 15.12 ATOM 106 C VAL A 14 6.887 20.526 8.341 0.50 15.03 ATOM 107 O VAL A 14 5.752 20.962 8.549 0.50 15.01 ATOM 108 CB VAL A 14 8.607 20.291 10.203 0.50 14.61 ATOM 109 CG1 VAL A 14 8.106 21.636 10.597 0.50 14.47 ATOM 110 CG2 VAL A 14 8.964 19.450 11.440 0.50 14.55 ATOM 111 N ILE A 15 7.580 20.820 7.240 1.00 15.43 ATOM 112 CA ILE A 15 7.126 21.826 6.253 1.00 15.62 ATOM 113 C ILE A 15 5.955 21.288 5.440 1.00 16.49 ATOM 114 O ILE A 15 5.178 22.052 4.891 1.00 16.46 ATOM 115 CB ILE A 15 8.259 22.397 5.340 1.00 15.46 ATOM 116 CG1 ILE A 15 8.770 21.318 4.371 1.00 15.30 ATOM 117 CG2 ILE A 15 9.364 23.047 6.172 1.00 15.69 ATOM 118 CD ILE A 15 9.800 21.811 3.378 1.00 16.66 ATOM 119 N GLU A 16 5.824 19.967 5.400 1.00 17.38 ATOM 120 CA GLU A 16 4.668 19.315 4.801 1.00 19.31 ATOM 121 C GLU A 16 3.438 19.329 5.715 1.00 19.98 ATOM 122 O GLU A 16 2.327 19.644 5.267 1.00 19.99 ATOM 123 CB GLU A 16 5.042 17.875 4.409 1.00 19.81 ATOM 124 CG GLU A 16 3.853 16.950 4.084 1.00 22.99 ATOM 125 CD GLU A 16 3.123 17.362 2.816 1.00 27.40 ATOM 126 OE1 GLU A 16 3.764 17.972 1.922 1.00 29.92 ATOM 127 OE2 GLU A 16 1.906 17.074 2.709 1.00 30.18 ATOM 128 N GLU A 17 3.647 19.005 6.988 1.00 20.12 ATOM 129 CA GLU A 17 2.550 18.830 7.942 1.00 21.35 ATOM 130 C GLU A 17 1.956 20.143 8.429 1.00 21.38 ATOM 131 O GLU A 17 0.803 20.181 8.857 1.00 22.36 ATOM 132 CB GLU A 17 3.018 18.044 9.162 1.00 22.46 ATOM 133 CG GLU A 17 3.189 16.559 8.937 1.00 26.84 ATOM 134 CD GLU A 17 3.392 15.813 10.251 1.00 31.90 ATOM 135 OE1 GLU A 17 4.213 16.254 11.095 1.00 34.41 ATOM 136 OE2 GLU A 17 2.720 14.781 10.446 1.00 34.93 ATOM 137 N ASN A 18 2.746 21.211 8.377 1.00 19.98 ATOM 138 CA ASN A 18 2.311 22.514 8.867 1.00 19.46 ATOM 139 C ASN A 18 2.239 23.507 7.725 1.00 18.04 ATOM 140 O ASN A 18 3.215 23.673 6.988 1.00 18.70 ATOM 141 CB ASN A 18 3.298 23.047 9.906 1.00 19.95 ATOM 142 CG ASN A 18 3.476 22.115 11.084 1.00 22.67 ATOM 143 OD1 ASN A 18 2.770 22.241 12.077 1.00 26.29 ATOM 144 ND2 ASN A 18 4.422 21.172 10.984 1.00 23.04 ATOM 145 N LYS A 19 1.095 24.170 7.581 0.50 17.34 ATOM 146 CA LYS A 19 0.909 25.166 6.525 0.50 16.55 ATOM 147 C LYS A 19 1.945 26.277 6.654 0.50 15.78 ATOM 148 O LYS A 19 2.592 26.655 5.680 0.50 15.11 ATOM 149 CB LYS A 19 -0.501 25.769 6.565 0.50 17.13 ATOM 150 CG LYS A 19 -0.675 26.962 5.629 0.50 18.90 ATOM 151 CD LYS A 19 -2.123 27.435 5.583 0.50 21.57 ATOM 152 CE LYS A 19 -2.392 28.280 4.345 0.50 23.34 ATOM 153 NZ LYS A 19 -2.500 27.447 3.118 0.50 24.42 ATOM 154 N TYR A 20 2.109 26.765 7.876 1.00 14.72 ATOM 155 CA TYR A 20 2.962 27.918 8.161 1.00 14.07 ATOM 156 C TYR A 20 4.050 27.503 9.122 1.00 12.93 ATOM 157 O TYR A 20 3.757 27.119 10.260 1.00 13.94 ATOM 158 CB TYR A 20 2.112 29.010 8.819 1.00 15.12 ATOM 159 CG TYR A 20 1.087 29.615 7.897 1.00 19.08 ATOM 160 CD1 TYR A 20 1.492 30.201 6.703 1.00 23.57 ATOM 161 CD2 TYR A 20 -0.269 29.616 8.212 1.00 21.87 ATOM 162 CE1 TYR A 20 0.601 30.767 5.840 1.00 26.63 ATOM 163 CE2 TYR A 20 -1.199 30.205 7.327 1.00 24.71 ATOM 164 CZ TYR A 20 -0.733 30.772 6.142 1.00 26.56 ATOM 165 OH TYR A 20 -1.569 31.364 5.217 1.00 30.90 ATOM 166 N VAL A 21 5.308 27.586 8.677 0.50 11.72 ATOM 167 CA VAL A 21 6.460 27.074 9.442 0.50 11.21 ATOM 168 C VAL A 21 7.648 28.035 9.423 0.50 10.13 ATOM 169 O VAL A 21 8.130 28.397 8.346 0.50 9.47 ATOM 170 CB VAL A 21 6.942 25.726 8.848 0.50 11.40 ATOM 171 CG1 VAL A 21 8.254 25.272 9.486 0.50 11.14 ATOM 172 CG2 VAL A 21 5.892 24.662 9.019 0.50 12.21 ATOM 173 N PHE A 22 8.132 28.439 10.602 1.00 9.72 ATOM 174 CA PHE A 22 9.387 29.166 10.689 1.00 9.45 ATOM 175 C PHE A 22 10.469 28.200 11.128 1.00 9.08 ATOM 176 O PHE A 22 10.230 27.359 12.001 1.00 9.69 ATOM 177 CB PHE A 22 9.289 30.300 11.724 1.00 10.01 ATOM 178 CG PHE A 22 8.521 31.505 11.252 1.00 10.05 ATOM 179 CD1 PHE A 22 9.167 32.528 10.556 1.00 10.56 ATOM 180 CD2 PHE A 22 7.158 31.635 11.529 1.00 12.28 ATOM 181 CE1 PHE A 22 8.467 33.677 10.129 1.00 11.75 ATOM 182 CE2 PHE A 22 6.446 32.774 11.098 1.00 12.07 ATOM 183 CZ PHE A 22 7.109 33.794 10.412 1.00 12.29 ATOM 184 N VAL A 23 11.650 28.334 10.532 1.00 9.01 ATOM 185 CA VAL A 23 12.814 27.491 10.841 1.00 9.45 ATOM 186 C VAL A 23 14.030 28.400 11.036 1.00 9.04 ATOM 187 O VAL A 23 14.304 29.254 10.188 1.00 9.81 ATOM 188 CB VAL A 23 13.115 26.494 9.691 1.00 9.79 ATOM 189 CG1 VAL A 23 14.353 25.651 10.016 1.00 10.82 ATOM 190 CG2 VAL A 23 11.901 25.588 9.437 1.00 11.63 ATOM 191 N LEU A 24 14.767 28.190 12.124 1.00 8.72 ATOM 192 CA LEU A 24 15.943 28.982 12.433 1.00 8.53 ATOM 193 C LEU A 24 17.206 28.129 12.419 1.00 8.96 ATOM 194 O LEU A 24 17.275 27.138 13.137 1.00 9.15 ATOM 195 CB LEU A 24 15.782 29.588 13.830 1.00 8.84 ATOM 196 CG LEU A 24 16.968 30.363 14.386 1.00 7.91 ATOM 197 CD1 LEU A 24 17.184 31.668 13.627 1.00 9.89 ATOM 198 CD2 LEU A 24 16.825 30.594 15.890 1.00 9.29 ATOM 199 N LYS A 25 18.197 28.543 11.638 1.00 9.15 ATOM 200 CA LYS A 25 19.554 28.034 11.770 1.00 10.01 ATOM 201 C LYS A 25 20.230 28.776 12.917 1.00 10.26 ATOM 202 O LYS A 25 20.335 30.011 12.888 1.00 10.44 ATOM 203 CB LYS A 25 20.361 28.264 10.488 1.00 10.07 ATOM 204 CG LYS A 25 19.894 27.488 9.286 1.00 10.55 ATOM 205 CD LYS A 25 20.945 27.621 8.179 1.00 11.21 ATOM 206 CE LYS A 25 20.588 26.790 6.948 1.00 11.99 ATOM 207 NZ LYS A 25 21.739 26.817 5.975 1.00 12.38 ATOM 208 N HSD A 26 20.716 28.026 13.899 1.00 10.79 ATOM 209 CA HSD A 26 21.286 28.602 15.121 1.00 11.60 ATOM 210 C HSD A 26 22.711 28.086 15.356 1.00 12.47 ATOM 211 O HSD A 26 22.979 26.904 15.147 1.00 12.17 ATOM 212 CB HSD A 26 20.357 28.245 16.296 1.00 11.71 ATOM 213 CG HSD A 26 20.864 28.656 17.645 1.00 12.77 ATOM 214 ND1 HSD A 26 21.187 29.960 17.963 1.00 12.63 ATOM 215 CD2 HSD A 26 21.052 27.936 18.778 1.00 14.79 ATOM 216 CE1 HSD A 26 21.569 30.021 19.230 1.00 13.96 ATOM 217 NE2 HSD A 26 21.492 28.807 19.746 1.00 16.40 ATOM 218 N SER A 27 23.614 28.974 15.776 0.50 12.89 ATOM 219 CA SER A 27 24.966 28.573 16.209 0.50 13.58 ATOM 220 C SER A 27 25.043 28.584 17.729 0.50 14.31 ATOM 221 O SER A 27 24.525 29.499 18.366 0.50 13.53 ATOM 222 CB SER A 27 26.032 29.509 15.633 0.50 14.09 ATOM 223 OG SER A 27 26.173 29.336 14.236 0.50 15.30 ATOM 224 N GLU A 28 25.693 27.580 18.317 0.50 15.23 ATOM 225 CA GLU A 28 25.703 27.457 19.778 0.50 16.75 ATOM 226 C GLU A 28 26.805 28.262 20.482 0.50 17.38 ATOM 227 O GLU A 28 26.860 28.302 21.710 0.50 18.47 ATOM 228 CB GLU A 28 25.767 25.982 20.202 0.50 16.52 ATOM 229 CG GLU A 28 26.894 25.213 19.547 0.50 17.27 ATOM 230 CD GLU A 28 26.818 23.707 19.788 0.50 18.38 ATOM 231 OE1 GLU A 28 25.899 23.232 20.484 0.50 19.33 ATOM 232 OE2 GLU A 28 27.690 22.995 19.268 0.50 20.85 ATOM 233 N THR A 29 27.662 28.913 19.706 0.50 18.02 ATOM 234 CA THR A 29 28.792 29.633 20.271 0.50 18.72 ATOM 235 C THR A 29 28.798 31.106 19.886 0.50 18.34 ATOM 236 O THR A 29 29.852 31.739 19.897 0.50 19.62 ATOM 237 CB THR A 29 30.113 29.041 19.769 0.50 18.79 ATOM 238 OG1 THR A 29 30.153 29.128 18.338 0.50 20.96 ATOM 239 CG2 THR A 29 30.245 27.587 20.197 0.50 19.53 ATOM 240 N CYS A 30 27.632 31.660 19.566 0.50 17.78 ATOM 241 CA CYS A 30 27.551 32.995 18.971 0.50 17.09 ATOM 242 C CYS A 30 26.487 33.887 19.645 0.50 16.37 ATOM 243 O CYS A 30 25.299 33.577 19.556 0.50 15.74 ATOM 244 CB CYS A 30 27.252 32.830 17.470 0.50 17.14 ATOM 245 SG CYS A 30 26.950 34.305 16.512 0.50 18.76 ATOM 246 N PRO A 31 26.903 34.990 20.325 1.00 16.10 ATOM 247 CA PRO A 31 25.942 35.971 20.855 1.00 14.97 ATOM 248 C PRO A 31 24.960 36.506 19.824 1.00 13.84 ATOM 249 O PRO A 31 23.807 36.728 20.164 1.00 13.46 ATOM 250 CB PRO A 31 26.818 37.113 21.394 1.00 15.11 ATOM 251 CG PRO A 31 28.178 36.598 21.459 1.00 16.89 ATOM 252 CD PRO A 31 28.308 35.394 20.575 1.00 16.47 ATOM 253 N ILE A 32 25.388 36.680 18.579 1.00 13.33 ATOM 254 CA ILE A 32 24.459 37.169 17.552 1.00 13.48 ATOM 255 C ILE A 32 23.356 36.129 17.316 1.00 12.50 ATOM 256 O ILE A 32 22.164 36.457 17.211 1.00 12.19 ATOM 257 CB ILE A 32 25.183 37.532 16.218 1.00 14.27 ATOM 258 CG1 ILE A 32 26.164 38.679 16.442 1.00 16.65 ATOM 259 CG2 ILE A 32 24.153 37.896 15.130 1.00 15.06 ATOM 260 CD ILE A 32 27.231 38.834 15.364 1.00 20.04 ATOM 261 N SER A 33 23.743 34.863 17.259 1.00 11.69 ATOM 262 CA SER A 33 22.765 33.794 17.114 1.00 11.27 ATOM 263 C SER A 33 21.841 33.676 18.330 1.00 10.86 ATOM 264 O SER A 33 20.618 33.503 18.184 1.00 10.87 ATOM 265 CB SER A 33 23.459 32.456 16.827 1.00 11.15 ATOM 266 OG SER A 33 22.532 31.557 16.240 1.00 12.33 ATOM 267 N ALA A 34 22.405 33.782 19.533 1.00 10.63 ATOM 268 CA ALA A 34 21.567 33.767 20.733 1.00 10.87 ATOM 269 C ALA A 34 20.551 34.904 20.744 1.00 11.38 ATOM 270 O ALA A 34 19.422 34.701 21.174 1.00 12.23 ATOM 271 CB ALA A 34 22.446 33.857 21.987 1.00 10.98 ATOM 272 N ASN A 35 20.954 36.092 20.292 1.00 11.49 ATOM 273 CA ASN A 35 20.014 37.222 20.191 1.00 12.93 ATOM 274 C ASN A 35 18.872 36.878 19.230 1.00 12.23 ATOM 275 O ASN A 35 17.691 37.120 19.526 1.00 12.79 ATOM 276 CB ASN A 35 20.750 38.478 19.697 1.00 14.05 ATOM 277 CG ASN A 35 21.662 39.089 20.749 1.00 18.57 ATOM 278 OD1 ASN A 35 21.514 38.835 21.940 1.00 22.91 ATOM 279 ND2 ASN A 35 22.612 39.915 20.303 1.00 22.46 ATOM 280 N ALA A 36 19.217 36.307 18.075 1.00 11.75 ATOM 281 CA ALA A 36 18.195 35.862 17.115 1.00 11.13 ATOM 282 C ALA A 36 17.267 34.769 17.665 1.00 10.90 ATOM 283 O ALA A 36 16.064 34.802 17.437 1.00 11.05 ATOM 284 CB ALA A 36 18.849 35.412 15.816 1.00 11.26 ATOM 285 N TYR A 37 17.838 33.794 18.370 1.00 10.70 ATOM 286 CA TYR A 37 17.066 32.724 18.973 1.00 11.73 ATOM 287 C TYR A 37 16.081 33.308 19.998 1.00 11.86 ATOM 288 O TYR A 37 14.917 32.905 20.062 1.00 11.83 ATOM 289 CB TYR A 37 18.012 31.716 19.640 1.00 11.78 ATOM 290 CG TYR A 37 17.361 30.458 20.183 1.00 14.32 ATOM 291 CD1 TYR A 37 17.311 29.304 19.424 1.00 17.93 ATOM 292 CD2 TYR A 37 16.844 30.417 21.475 1.00 18.20 ATOM 293 CE1 TYR A 37 16.739 28.141 19.914 1.00 20.15 ATOM 294 CE2 TYR A 37 16.266 29.238 21.980 1.00 20.88 ATOM 295 CZ TYR A 37 16.222 28.116 21.180 1.00 21.69 ATOM 296 OH TYR A 37 15.660 26.950 21.653 1.00 25.29 ATOM 297 N ASP A 38 16.558 34.266 20.794 1.00 12.34 ATOM 298 CA ASP A 38 15.683 34.962 21.740 1.00 12.94 ATOM 299 C ASP A 38 14.510 35.676 21.032 1.00 12.22 ATOM 300 O ASP A 38 13.356 35.548 21.460 1.00 12.43 ATOM 301 CB ASP A 38 16.517 35.952 22.551 1.00 14.22 ATOM 302 CG ASP A 38 15.738 36.589 23.688 1.00 17.84 ATOM 303 OD1 ASP A 38 15.659 37.820 23.677 1.00 22.21 ATOM 304 OD2 ASP A 38 15.220 35.863 24.548 1.00 23.51 ATOM 305 N GLN A 39 14.800 36.404 19.945 1.00 11.83 ATOM 306 CA GLN A 39 13.746 37.046 19.134 1.00 11.86 ATOM 307 C GLN A 39 12.764 36.014 18.591 1.00 11.26 ATOM 308 O GLN A 39 11.553 36.218 18.619 1.00 11.06 ATOM 309 CB GLN A 39 14.345 37.859 17.982 1.00 12.06 ATOM 310 CG GLN A 39 15.155 39.060 18.486 1.00 13.11 ATOM 311 CD GLN A 39 14.284 40.107 19.143 1.00 14.16 ATOM 312 OE1 GLN A 39 13.423 40.721 18.500 1.00 13.82 ATOM 313 NE2 GLN A 39 14.479 40.295 20.437 1.00 14.94 ATOM 314 N PHE A 40 13.306 34.896 18.122 1.00 10.34 ATOM 315 CA PHE A 40 12.532 33.806 17.544 1.00 10.35 ATOM 316 C PHE A 40 11.563 33.267 18.593 1.00 10.53 ATOM 317 O PHE A 40 10.358 33.159 18.319 1.00 10.39 ATOM 318 CB PHE A 40 13.516 32.738 17.038 1.00 10.03 ATOM 319 CG PHE A 40 12.932 31.693 16.117 1.00 10.87 ATOM 320 CD1 PHE A 40 12.531 32.016 14.826 1.00 12.83 ATOM 321 CD2 PHE A 40 12.885 30.356 16.517 1.00 10.43 ATOM 322 CE1 PHE A 40 12.029 31.008 13.957 1.00 12.54 ATOM 323 CE2 PHE A 40 12.410 29.359 15.671 1.00 10.14 ATOM 324 CZ PHE A 40 11.971 29.688 14.390 1.00 10.86 ATOM 325 N ASN A 41 12.068 32.967 19.790 0.50 10.99 ATOM 326 CA ASN A 41 11.219 32.495 20.885 0.50 11.60 ATOM 327 C ASN A 41 10.177 33.508 21.325 0.50 11.36 ATOM 328 O ASN A 41 9.061 33.126 21.643 0.50 11.54 ATOM 329 CB ASN A 41 12.049 32.121 22.114 0.50 12.39 ATOM 330 CG ASN A 41 12.550 30.707 22.074 0.50 13.79 ATOM 331 OD1 ASN A 41 11.774 29.757 22.106 0.50 14.23 ATOM 332 ND2 ASN A 41 13.865 30.556 22.019 0.50 16.41 ATOM 333 N LYS A 42 10.551 34.788 21.389 1.00 11.19 ATOM 334 CA LYS A 42 9.602 35.848 21.776 1.00 11.08 ATOM 335 C LYS A 42 8.476 35.958 20.766 1.00 11.08 ATOM 336 O LYS A 42 7.300 36.044 21.121 1.00 12.18 ATOM 337 CB LYS A 42 10.328 37.189 21.908 1.00 11.12 ATOM 338 CG LYS A 42 11.012 37.375 23.251 1.00 11.68 ATOM 339 CD LYS A 42 12.050 38.456 23.119 1.00 13.32 ATOM 340 CE LYS A 42 12.583 38.874 24.459 1.00 15.20 ATOM 341 NZ LYS A 42 13.513 40.016 24.191 1.00 19.25 ATOM 342 N PHE A 43 8.824 35.904 19.491 1.00 10.74 ATOM 343 CA PHE A 43 7.820 35.970 18.446 1.00 10.83 ATOM 344 C PHE A 43 6.868 34.763 18.501 1.00 11.21 ATOM 345 O PHE A 43 5.631 34.919 18.500 1.00 13.09 ATOM 346 CB PHE A 43 8.543 36.034 17.098 1.00 10.50 ATOM 347 CG PHE A 43 7.638 35.814 15.921 1.00 11.88 ATOM 348 CD1 PHE A 43 6.766 36.820 15.504 1.00 11.98 ATOM 349 CD2 PHE A 43 7.659 34.599 15.232 1.00 11.17 ATOM 350 CE1 PHE A 43 5.928 36.620 14.419 1.00 13.54 ATOM 351 CE2 PHE A 43 6.829 34.392 14.149 1.00 12.23 ATOM 352 CZ PHE A 43 5.969 35.407 13.740 1.00 13.02 ATOM 353 N LEU A 44 7.433 33.555 18.540 1.00 11.66 ATOM 354 CA LEU A 44 6.600 32.356 18.528 1.00 11.67 ATOM 355 C LEU A 44 5.700 32.258 19.752 1.00 11.97 ATOM 356 O LEU A 44 4.516 31.883 19.641 1.00 12.29 ATOM 357 CB LEU A 44 7.477 31.112 18.429 1.00 11.47 ATOM 358 CG LEU A 44 8.249 30.942 17.124 1.00 10.79 ATOM 359 CD1 LEU A 44 9.321 29.869 17.307 1.00 11.57 ATOM 360 CD2 LEU A 44 7.311 30.653 15.956 1.00 10.62 ATOM 361 N TYR A 45 6.268 32.588 20.909 1.00 12.59 ATOM 362 CA TYR A 45 5.520 32.589 22.173 1.00 13.65 ATOM 363 C TYR A 45 4.347 33.572 22.137 1.00 14.22 ATOM 364 O TYR A 45 3.234 33.236 22.520 1.00 14.42 ATOM 365 CB TYR A 45 6.473 32.891 23.325 1.00 13.42 ATOM 366 CG TYR A 45 5.858 32.933 24.689 1.00 15.40 ATOM 367 CD1 TYR A 45 5.354 31.788 25.285 1.00 17.71 ATOM 368 CD2 TYR A 45 5.827 34.122 25.399 1.00 16.72 ATOM 369 CE1 TYR A 45 4.803 31.841 26.574 1.00 18.80 ATOM 370 CE2 TYR A 45 5.293 34.187 26.664 1.00 18.42 ATOM 371 CZ TYR A 45 4.774 33.052 27.239 1.00 18.61 ATOM 372 OH TYR A 45 4.248 33.133 28.512 1.00 21.99 ATOM 373 N GLU A 46 4.592 34.769 21.618 1.00 14.58 ATOM 374 CA GLU A 46 3.525 35.768 21.496 1.00 16.51 ATOM 375 C GLU A 46 2.441 35.299 20.514 1.00 16.64 ATOM 376 O GLU A 46 1.250 35.600 20.695 1.00 17.51 ATOM 377 CB GLU A 46 4.132 37.120 21.075 1.00 17.59 ATOM 378 CG GLU A 46 3.290 38.370 21.333 1.00 21.92 ATOM 379 CD GLU A 46 2.725 38.463 22.749 1.00 23.96 ATOM 380 OE1 GLU A 46 1.591 37.977 22.945 1.00 27.28 ATOM 381 OE2 GLU A 46 3.397 39.002 23.664 1.00 23.25 ATOM 382 N ARG A 47 2.856 34.561 19.484 0.50 17.01 ATOM 383 CA ARG A 47 1.949 34.031 18.467 0.50 17.48 ATOM 384 C ARG A 47 1.253 32.743 18.900 0.50 17.59 ATOM 385 O ARG A 47 0.286 32.320 18.275 0.50 17.70 ATOM 386 CB ARG A 47 2.710 33.764 17.162 0.50 17.80 ATOM 387 CG ARG A 47 3.184 35.006 16.420 0.50 18.93 ATOM 388 CD ARG A 47 2.027 35.740 15.777 0.50 20.16 ATOM 389 NE ARG A 47 2.479 36.943 15.081 0.50 20.58 ATOM 390 CZ ARG A 47 2.461 38.163 15.609 0.50 21.29 ATOM 391 NH1 ARG A 47 2.018 38.351 16.846 0.50 22.95 ATOM 392 NH2 ARG A 47 2.897 39.195 14.903 0.50 20.58 ATOM 393 N ASP A 48 1.756 32.102 19.950 0.50 17.53 ATOM 394 CA ASP A 48 1.223 30.799 20.352 0.50 17.46 ATOM 395 C ASP A 48 1.374 29.832 19.179 0.50 17.05 ATOM 396 O ASP A 48 0.420 29.168 18.759 0.50 17.64 ATOM 397 CB ASP A 48 -0.250 30.939 20.747 0.50 17.56 ATOM 398 CG ASP A 48 -0.776 29.736 21.512 0.50 19.61 ATOM 399 OD1 ASP A 48 0.026 28.950 22.053 0.50 20.09 ATOM 400 OD2 ASP A 48 -2.014 29.587 21.572 0.50 22.17 ATOM 401 N MET A 49 2.593 29.765 18.652 0.50 16.44 ATOM 402 CA MET A 49 2.876 29.020 17.437 0.50 15.94 ATOM 403 C MET A 49 4.183 28.261 17.605 0.50 15.11 ATOM 404 O MET A 49 5.173 28.840 18.042 0.50 15.44 ATOM 405 CB MET A 49 2.975 30.002 16.263 0.50 16.43 ATOM 406 CG MET A 49 3.885 29.587 15.116 0.50 18.31 ATOM 407 S MET A 49 4.028 30.975 13.738 0.50 23.44 ATOM 408 CE MET A 49 2.723 30.224 12.538 0.50 22.84 ATOM 409 N ASP A 50 4.198 26.969 17.278 1.00 14.14 ATOM 410 CA ASP A 50 5.471 26.265 17.299 1.00 14.14 ATOM 411 C ASP A 50 6.304 26.621 16.094 1.00 13.33 ATOM 412 O ASP A 50 5.779 26.810 14.998 1.00 14.21 ATOM 413 CB ASP A 50 5.282 24.760 17.330 1.00 14.78 ATOM 414 CG ASP A 50 4.689 24.262 18.638 1.00 16.01 ATOM 415 OD1 ASP A 50 4.699 24.985 19.652 1.00 17.56 ATOM 416 OD2 ASP A 50 4.216 23.131 18.623 1.00 19.78 ATOM 417 N GLY A 51 7.607 26.686 16.310 1.00 11.63 ATOM 418 CA GLY A 51 8.562 26.808 15.225 1.00 10.91 ATOM 419 C GLY A 51 9.702 25.868 15.489 1.00 10.97 ATOM 420 O GLY A 51 9.697 25.137 16.482 1.00 12.07 ATOM 421 N TYR A 52 10.675 25.880 14.582 1.00 10.01 ATOM 422 CA TYR A 52 11.725 24.877 14.592 1.00 9.83 ATOM 423 C TYR A 52 13.096 25.495 14.464 1.00 9.69 ATOM 424 O TYR A 52 13.242 26.572 13.907 1.00 10.53 ATOM 425 CB TYR A 52 11.471 23.848 13.466 1.00 9.96 ATOM 426 CG TYR A 52 10.162 23.164 13.665 1.00 12.18 ATOM 427 CD1 TYR A 52 10.083 21.976 14.395 1.00 13.93 ATOM 428 CD2 TYR A 52 8.988 23.741 13.197 1.00 14.38 ATOM 429 CE1 TYR A 52 8.841 21.355 14.618 1.00 16.17 ATOM 430 CE2 TYR A 52 7.756 23.136 13.427 1.00 17.05 ATOM 431 CZ TYR A 52 7.701 21.951 14.122 1.00 17.59 ATOM 432 OH TYR A 52 6.453 21.384 14.315 1.00 22.73 ATOM 433 N TYR A 53 14.100 24.814 14.999 1.00 9.38 ATOM 434 CA TYR A 53 15.461 25.306 14.850 1.00 9.06 ATOM 435 C TYR A 53 16.401 24.129 14.689 1.00 9.21 ATOM 436 O TYR A 53 16.033 22.979 14.965 1.00 10.33 ATOM 437 CB TYR A 53 15.862 26.197 16.045 1.00 9.97 ATOM 438 CG TYR A 53 16.188 25.449 17.320 1.00 8.91 ATOM 439 CD1 TYR A 53 17.520 25.165 17.663 1.00 12.59 ATOM 440 CD2 TYR A 53 15.174 25.008 18.168 1.00 11.20 ATOM 441 CE1 TYR A 53 17.829 24.462 18.823 1.00 13.27 ATOM 442 CE2 TYR A 53 15.476 24.309 19.336 1.00 12.00 ATOM 443 CZ TYR A 53 16.804 24.033 19.643 1.00 13.79 ATOM 444 OH TYR A 53 17.092 23.343 20.797 1.00 15.71 ATOM 445 N LEU A 54 17.600 24.417 14.212 1.00 9.20 ATOM 446 CA LEU A 54 18.655 23.401 14.185 1.00 9.54 ATOM 447 C LEU A 54 19.935 24.040 14.668 1.00 10.49 ATOM 448 O LEU A 54 20.145 25.244 14.498 1.00 9.94 ATOM 449 CB LEU A 54 18.848 22.804 12.782 1.00 10.31 ATOM 450 CG LEU A 54 19.149 23.777 11.646 1.00 10.05 ATOM 451 CD1 LEU A 54 20.172 23.211 10.662 1.00 11.70 ATOM 452 CD2 LEU A 54 17.846 24.206 10.951 1.00 11.31 ATOM 453 N ILE A 55 20.776 23.225 15.291 0.50 10.77 ATOM 454 CA ILE A 55 22.126 23.641 15.637 0.50 11.29 ATOM 455 C ILE A 55 23.035 23.326 14.444 0.50 11.96 ATOM 456 O ILE A 55 23.395 22.171 14.206 0.50 11.76 ATOM 457 CB ILE A 55 22.622 22.950 16.917 0.50 11.52 ATOM 458 CG1 ILE A 55 21.768 23.395 18.111 0.50 10.99 ATOM 459 CG2 ILE A 55 24.091 23.268 17.139 0.50 11.70 ATOM 460 CD ILE A 55 21.872 22.467 19.315 0.50 11.80 ATOM 461 N VAL A 56 23.388 24.365 13.696 0.50 12.57 ATOM 462 CA VAL A 56 24.129 24.217 12.440 0.50 13.41 ATOM 463 C VAL A 56 25.275 23.206 12.543 0.50 14.16 ATOM 464 O VAL A 56 25.318 22.205 11.814 0.50 13.61 ATOM 465 CB VAL A 56 24.701 25.581 11.975 0.50 13.45 ATOM 466 CG1 VAL A 56 25.653 25.388 10.784 0.50 13.93 ATOM 467 CG2 VAL A 56 23.561 26.561 11.643 0.50 13.80 ATOM 468 N GLN A 57 26.190 23.494 13.464 0.50 14.83 ATOM 469 CA GLN A 57 27.397 22.699 13.677 0.50 15.93 ATOM 470 C GLN A 57 27.075 21.209 13.860 0.50 16.41 ATOM 471 O GLN A 57 27.728 20.335 13.270 0.50 17.11 ATOM 472 CB GLN A 57 28.178 23.263 14.876 0.50 16.26 ATOM 473 CG GLN A 57 28.657 24.724 14.718 0.50 17.38 ATOM 474 CD GLN A 57 27.905 25.753 15.588 0.50 17.63 ATOM 475 OE1 GLN A 57 26.720 25.601 15.898 0.50 16.76 ATOM 476 NE2 GLN A 57 28.610 26.809 15.975 0.50 19.36 ATOM 477 N GLN A 58 26.053 20.911 14.655 1.00 16.25 ATOM 478 CA GLN A 58 25.710 19.524 14.925 1.00 16.95 ATOM 479 C GLN A 58 24.971 18.842 13.788 1.00 17.11 ATOM 480 O GLN A 58 24.906 17.613 13.726 1.00 17.98 ATOM 481 CB GLN A 58 24.891 19.407 16.224 1.00 17.00 ATOM 482 CG GLN A 58 25.598 19.943 17.502 1.00 20.35 ATOM 483 CD GLN A 58 26.996 19.360 17.762 1.00 25.31 ATOM 484 OE1 GLN A 58 27.221 18.163 17.595 1.00 27.65 ATOM 485 NE2 GLN A 58 27.929 20.217 18.206 1.00 28.33 ATOM 486 N GLU A 59 24.389 19.635 12.894 1.00 17.24 ATOM 487 CA GLU A 59 23.529 19.088 11.843 1.00 17.86 ATOM 488 C GLU A 59 23.882 19.736 10.512 1.00 17.83 ATOM 489 O GLU A 59 23.035 20.387 9.865 1.00 17.27 ATOM 490 CB GLU A 59 22.048 19.337 12.182 1.00 18.24 ATOM 491 CG GLU A 59 21.600 18.780 13.542 1.00 19.98 ATOM 492 CD GLU A 59 21.697 17.261 13.642 1.00 22.89 ATOM 493 OE1 GLU A 59 21.815 16.588 12.604 1.00 24.23 ATOM 494 OE2 GLU A 59 21.662 16.727 14.770 1.00 24.65 ATOM 495 N ARG A 60 25.131 19.574 10.078 0.50 17.94 ATOM 496 CA ARG A 60 25.579 20.168 8.814 0.50 17.83 ATOM 497 C ARG A 60 24.823 19.614 7.596 0.50 17.43 ATOM 498 O ARG A 60 24.459 20.373 6.684 0.50 17.18 ATOM 499 CB ARG A 60 27.097 20.015 8.642 0.50 18.10 ATOM 500 CG ARG A 60 27.926 20.841 9.616 0.50 18.82 ATOM 501 CD ARG A 60 28.577 22.036 8.939 0.50 21.68 ATOM 502 NE ARG A 60 27.790 23.265 9.006 0.50 23.48 ATOM 503 CZ ARG A 60 28.152 24.344 9.698 0.50 25.25 ATOM 504 NH1 ARG A 60 27.383 25.425 9.704 0.50 25.58 ATOM 505 NH2 ARG A 60 29.292 24.350 10.378 0.50 26.42 ATOM 506 N ASP A 61 24.555 18.311 7.569 0.50 17.13 ATOM 507 CA ASP A 61 23.773 17.779 6.448 0.50 16.70 ATOM 508 C ASP A 61 22.514 18.601 6.267 0.50 16.19 ATOM 509 O ASP A 61 22.230 19.086 5.165 0.50 15.88 ATOM 510 CB ASP A 61 23.399 16.316 6.645 0.50 16.80 ATOM 511 CG ASP A 61 24.492 15.383 6.201 0.50 17.74 ATOM 512 OD1 ASP A 61 25.436 15.863 5.542 0.50 19.84 ATOM 513 OD2 ASP A 61 24.398 14.184 6.503 0.50 17.29 ATOM 514 N LEU A 62 21.775 18.759 7.363 1.00 15.81 ATOM 515 CA LEU A 62 20.487 19.451 7.346 1.00 14.82 ATOM 516 C LEU A 62 20.687 20.923 6.977 1.00 13.96 ATOM 517 O LEU A 62 19.908 21.479 6.189 1.00 13.17 ATOM 518 CB LEU A 62 19.753 19.313 8.693 1.00 14.16 ATOM 519 CG LEU A 62 18.450 20.129 8.797 1.00 13.94 ATOM 520 CD1 LEU A 62 17.461 19.844 7.664 1.00 14.33 ATOM 521 CD2 LEU A 62 17.796 19.928 10.157 1.00 15.06 ATOM 522 N SER A 63 21.718 21.552 7.536 1.00 13.29 ATOM 523 CA SER A 63 22.000 22.958 7.237 1.00 13.02 ATOM 524 C SER A 63 22.253 23.150 5.724 1.00 13.46 ATOM 525 O SER A 63 21.707 24.078 5.099 1.00 13.73 ATOM 526 CB SER A 63 23.175 23.483 8.067 1.00 12.83 ATOM 527 OG SER A 63 23.354 24.858 7.820 1.00 13.33 ATOM 528 N ASP A 64 23.076 22.282 5.135 0.50 13.18 ATOM 529 CA ASP A 64 23.338 22.384 3.698 0.50 13.04 ATOM 530 C ASP A 64 22.080 22.033 2.882 0.50 12.50 ATOM 531 O ASP A 64 21.838 22.643 1.836 0.50 12.24 ATOM 532 CB ASP A 64 24.568 21.561 3.275 0.50 13.47 ATOM 533 CG ASP A 64 25.121 21.979 1.915 0.50 14.48 ATOM 534 OD1 ASP A 64 25.404 23.172 1.706 0.50 16.19 ATOM 535 OD2 ASP A 64 25.288 21.108 1.048 0.50 17.04 ATOM 536 N TYR A 65 21.268 21.095 3.379 1.00 12.56 ATOM 537 CA TYR A 65 20.021 20.760 2.731 1.00 12.34 ATOM 538 C TYR A 65 19.091 21.977 2.644 1.00 12.24 ATOM 539 O TYR A 65 18.481 22.220 1.600 1.00 12.68 ATOM 540 CB TYR A 65 19.301 19.597 3.418 1.00 12.47 ATOM 541 CG TYR A 65 18.047 19.240 2.677 1.00 12.99 ATOM 542 CD1 TYR A 65 18.105 18.444 1.537 1.00 13.62 ATOM 543 CD2 TYR A 65 16.807 19.747 3.067 1.00 12.79 ATOM 544 CE1 TYR A 65 16.974 18.147 0.834 1.00 14.84 ATOM 545 CE2 TYR A 65 15.651 19.448 2.364 1.00 14.28 ATOM 546 CZ TYR A 65 15.744 18.647 1.229 1.00 14.30 ATOM 547 OH TYR A 65 14.618 18.338 0.513 1.00 16.79 ATOM 548 N ILE A 66 18.982 22.740 3.731 1.00 12.10 ATOM 549 CA ILE A 66 18.133 23.934 3.725 1.00 11.70 ATOM 550 C ILE A 66 18.654 24.996 2.745 1.00 11.37 ATOM 551 O ILE A 66 17.862 25.634 2.046 1.00 11.59 ATOM 552 CB ILE A 66 17.945 24.467 5.160 1.00 10.79 ATOM 553 CG1 ILE A 66 17.132 23.444 5.960 1.00 11.25 ATOM 554 CG2 ILE A 66 17.249 25.842 5.165 1.00 12.37 ATOM 555 CD ILE A 66 17.152 23.682 7.459 1.00 11.76 ATOM 556 N ALA A 67 19.978 25.134 2.644 1.00 11.27 ATOM 557 CA ALA A 67 20.568 26.031 1.666 1.00 11.20 ATOM 558 C ALA A 67 20.180 25.618 0.236 1.00 11.38 ATOM 559 O ALA A 67 19.825 26.474 -0.585 1.00 12.00 ATOM 560 CB ALA A 67 22.068 26.089 1.836 1.00 11.56 ATOM 561 N LYS A 68 20.234 24.319 -0.061 0.50 11.44 ATOM 562 CA LYS A 68 19.867 23.827 -1.395 0.50 11.52 ATOM 563 C LYS A 68 18.356 23.811 -1.609 0.50 11.39 ATOM 564 O LYS A 68 17.875 23.808 -2.739 0.50 11.18 ATOM 565 CB LYS A 68 20.430 22.424 -1.649 0.50 12.69 ATOM 566 CG LYS A 68 21.443 22.350 -2.771 0.50 13.61 ATOM 567 CD LYS A 68 22.811 22.811 -2.323 0.50 16.77 ATOM 568 CE LYS A 68 23.889 22.164 -3.170 0.50 17.70 ATOM 569 NZ LYS A 68 24.074 20.701 -2.917 0.50 19.23 ATOM 570 N LYS A 69 17.609 23.778 -0.516 0.50 10.77 ATOM 571 CA LYS A 69 16.157 23.743 -0.577 0.50 10.35 ATOM 572 C LYS A 69 15.607 25.093 -1.027 0.50 10.67 ATOM 573 O LYS A 69 14.566 25.173 -1.677 0.50 10.55 ATOM 574 CB LYS A 69 15.627 23.408 0.817 0.50 9.90 ATOM 575 CG LYS A 69 14.128 23.508 0.990 0.50 9.60 ATOM 576 CD LYS A 69 13.412 22.477 0.159 0.50 8.03 ATOM 577 CE LYS A 69 11.889 22.597 0.295 0.50 10.35 ATOM 578 NZ LYS A 69 11.236 21.313 -0.101 0.50 10.16 ATOM 579 N THR A 70 16.334 26.145 -0.666 1.00 11.20 ATOM 580 CA THR A 70 15.887 27.535 -0.782 1.00 11.80 ATOM 581 C THR A 70 16.733 28.322 -1.768 1.00 12.38 ATOM 582 O THR A 70 16.388 29.455 -2.135 1.00 13.23 ATOM 583 CB THR A 70 16.014 28.225 0.614 1.00 11.13 ATOM 584 OG1 THR A 70 17.393 28.200 1.032 1.00 10.83 ATOM 585 CG2 THR A 70 15.140 27.520 1.667 1.00 13.68 ATOM 586 N ASN A 71 17.837 27.727 -2.219 1.00 12.52 ATOM 587 CA ASN A 71 18.866 28.464 -2.949 1.00 13.74 ATOM 588 C ASN A 71 19.374 29.740 -2.274 1.00 13.30 ATOM 589 O ASN A 71 19.783 30.697 -2.935 1.00 13.38 ATOM 590 CB ASN A 71 18.456 28.733 -4.397 1.00 14.83 ATOM 591 CG ASN A 71 19.660 28.862 -5.296 1.00 17.99 ATOM 592 OD1 ASN A 71 20.729 28.300 -5.006 1.00 21.38 ATOM 593 ND2 ASN A 71 19.518 29.619 -6.371 1.00 18.17 ATOM 594 N VAL A 72 19.367 29.723 -0.939 1.00 12.36 ATOM 595 CA VAL A 72 19.892 30.813 -0.145 1.00 12.74 ATOM 596 C VAL A 72 21.179 30.339 0.528 1.00 12.91 ATOM 597 O VAL A 72 21.169 29.366 1.280 1.00 13.79 ATOM 598 CB VAL A 72 18.862 31.289 0.907 1.00 12.32 ATOM 599 CG1 VAL A 72 19.466 32.360 1.796 1.00 13.12 ATOM 600 CG2 VAL A 72 17.607 31.837 0.205 1.00 12.49 ATOM 601 N LYS A 73 22.295 31.006 0.248 1.00 14.32 ATOM 602 CA LYS A 73 23.564 30.546 0.804 1.00 15.36 ATOM 603 C LYS A 73 23.554 30.634 2.324 1.00 14.92 ATOM 604 O LYS A 73 22.921 31.508 2.928 1.00 14.65 ATOM 605 CB LYS A 73 24.764 31.276 0.198 1.00 16.90 ATOM 606 CG LYS A 73 25.017 30.942 -1.286 1.00 21.67 ATOM 607 CD LYS A 73 25.600 29.552 -1.528 1.00 26.30 ATOM 608 CE LYS A 73 25.461 29.154 -2.989 1.00 28.64 ATOM 609 NZ LYS A 73 24.014 28.900 -3.325 1.00 30.81 ATOM 610 N HSD A 74 24.234 29.673 2.918 1.00 14.24 ATOM 611 CA HSD A 74 24.214 29.507 4.349 1.00 14.12 ATOM 612 C HSD A 74 24.694 30.734 5.134 1.00 14.02 ATOM 613 O HSD A 74 25.729 31.320 4.816 1.00 15.03 ATOM 614 CB HSD A 74 25.069 28.307 4.733 1.00 14.23 ATOM 615 CG HSD A 74 25.256 28.189 6.204 1.00 14.42 ATOM 616 ND1 HSD A 74 24.255 27.726 7.027 1.00 14.89 ATOM 617 CD2 HSD A 74 26.284 28.540 7.013 1.00 15.97 ATOM 618 CE1 HSD A 74 24.671 27.757 8.280 1.00 15.08 ATOM 619 NE2 HSD A 74 25.896 28.253 8.300 1.00 15.66 ATOM 620 N GLU A 75 23.943 31.105 6.172 1.00 13.45 ATOM 621 CA GLU A 75 24.403 32.055 7.192 1.00 13.38 ATOM 622 C GLU A 75 23.963 31.489 8.518 1.00 13.15 ATOM 623 O GLU A 75 23.076 30.633 8.577 1.00 12.73 ATOM 624 CB GLU A 75 23.764 33.443 7.047 1.00 13.57 ATOM 625 CG GLU A 75 23.953 34.109 5.696 1.00 15.97 ATOM 626 CD GLU A 75 25.325 34.721 5.500 1.00 19.72 ATOM 627 OE1 GLU A 75 26.152 34.752 6.444 1.00 21.60 ATOM 628 OE2 GLU A 75 25.564 35.187 4.369 1.00 23.31 ATOM 629 N SER A 76 24.555 32.004 9.591 1.00 12.65 ATOM 630 CA SER A 76 24.036 31.723 10.917 1.00 13.34 ATOM 631 C SER A 76 24.194 32.961 11.798 1.00 12.41 ATOM 632 O SER A 76 25.267 33.573 11.829 1.00 13.24 ATOM 633 CB SER A 76 24.702 30.499 11.525 1.00 14.42 ATOM 634 OG SER A 76 23.991 30.105 12.678 1.00 17.40 ATOM 635 N PRO A 77 23.122 33.366 12.491 1.00 10.70 ATOM 636 CA PRO A 77 21.788 32.785 12.483 1.00 10.29 ATOM 637 C PRO A 77 21.060 33.144 11.186 1.00 10.10 ATOM 638 O PRO A 77 21.334 34.176 10.588 1.00 10.75 ATOM 639 CB PRO A 77 21.115 33.467 13.672 1.00 9.95 ATOM 640 CG PRO A 77 21.747 34.806 13.735 1.00 10.27 ATOM 641 CD PRO A 77 23.185 34.575 13.337 1.00 10.27 ATOM 642 N GLN A 78 20.095 32.320 10.797 1.00 9.83 ATOM 643 CA GLN A 78 19.361 32.544 9.555 1.00 9.33 ATOM 644 C GLN A 78 17.974 31.983 9.731 1.00 9.42 ATOM 645 O GLN A 78 17.819 30.832 10.126 1.00 10.15 ATOM 646 CB GLN A 78 20.087 31.856 8.405 1.00 9.69 ATOM 647 CG GLN A 78 19.510 32.154 7.039 1.00 9.70 ATOM 648 CD GLN A 78 20.406 31.565 5.941 1.00 9.83 ATOM 649 OE1 GLN A 78 20.789 30.389 6.003 1.00 11.76 ATOM 650 NE2 GLN A 78 20.775 32.393 4.960 1.00 12.65 ATOM 651 N ALA A 79 16.954 32.776 9.427 1.00 8.64 ATOM 652 CA ALA A 79 15.590 32.320 9.654 1.00 8.58 ATOM 653 C ALA A 79 14.842 32.266 8.341 1.00 8.54 ATOM 654 O ALA A 79 15.088 33.087 7.450 1.00 8.63 ATOM 655 CB ALA A 79 14.873 33.248 10.645 1.00 8.63 ATOM 656 N PHE A 80 13.947 31.287 8.234 1.00 8.41 ATOM 657 CA PHE A 80 13.171 31.053 7.021 1.00 8.50 ATOM 658 C PHE A 80 11.710 30.902 7.402 1.00 9.19 ATOM 659 O PHE A 80 11.387 30.410 8.476 1.00 8.68 ATOM 660 CB PHE A 80 13.591 29.725 6.382 1.00 8.81 ATOM 661 CG PHE A 80 14.967 29.725 5.833 1.00 8.92 ATOM 662 CD1 PHE A 80 15.190 30.113 4.512 1.00 10.17 ATOM 663 CD2 PHE A 80 16.066 29.351 6.625 1.00 10.56 ATOM 664 CE1 PHE A 80 16.479 30.126 3.981 1.00 11.47 ATOM 665 CE2 PHE A 80 17.343 29.359 6.098 1.00 10.93 ATOM 666 CZ PHE A 80 17.549 29.751 4.778 1.00 11.36 ATOM 667 N TYR A 81 10.844 31.311 6.486 1.00 8.46 ATOM 668 CA TYR A 81 9.405 31.128 6.633 1.00 8.80 ATOM 669 C TYR A 81 8.905 30.349 5.440 1.00 8.99 ATOM 670 O TYR A 81 9.110 30.765 4.281 1.00 10.10 ATOM 671 CB TYR A 81 8.710 32.478 6.712 1.00 9.28 ATOM 672 CG TYR A 81 7.213 32.447 6.963 1.00 10.09 ATOM 673 CD1 TYR A 81 6.645 31.584 7.907 1.00 11.03 ATOM 674 CD2 TYR A 81 6.376 33.316 6.273 1.00 12.40 ATOM 675 CE1 TYR A 81 5.254 31.584 8.144 1.00 13.27 ATOM 676 CE2 TYR A 81 4.998 33.335 6.505 1.00 12.81 ATOM 677 CZ TYR A 81 4.444 32.465 7.437 1.00 13.81 ATOM 678 OH TYR A 81 3.064 32.499 7.650 1.00 17.67 ATOM 679 N PHE A 82 8.283 29.210 5.737 1.00 9.09 ATOM 680 CA PHE A 82 7.681 28.331 4.718 1.00 9.10 ATOM 681 C PHE A 82 6.167 28.346 4.783 1.00 10.62 ATOM 682 O PHE A 82 5.574 28.201 5.854 1.00 10.91 ATOM 683 CB PHE A 82 8.165 26.881 4.881 1.00 10.14 ATOM 684 CG PHE A 82 9.635 26.717 4.678 1.00 9.58 ATOM 685 CD1 PHE A 82 10.154 26.417 3.416 1.00 10.49 ATOM 686 CD2 PHE A 82 10.520 26.914 5.742 1.00 9.94 ATOM 687 CE1 PHE A 82 11.538 26.289 3.224 1.00 10.82 ATOM 688 CE2 PHE A 82 11.906 26.786 5.556 1.00 10.90 ATOM 689 CZ PHE A 82 12.417 26.473 4.312 1.00 10.40 ATOM 690 N VAL A 83 5.559 28.553 3.620 1.00 11.15 ATOM 691 CA VAL A 83 4.104 28.535 3.507 1.00 12.96 ATOM 692 C VAL A 83 3.770 27.412 2.538 1.00 13.42 ATOM 693 O VAL A 83 4.203 27.434 1.397 1.00 13.98 ATOM 694 CB VAL A 83 3.548 29.886 2.995 1.00 13.32 ATOM 695 CG1 VAL A 83 2.051 29.774 2.719 1.00 15.67 ATOM 696 CG2 VAL A 83 3.833 30.994 4.004 1.00 14.65 ATOM 697 N ASN A 84 3.010 26.418 3.010 1.00 14.74 ATOM 698 CA ASN A 84 2.753 25.199 2.228 1.00 16.17 ATOM 699 C ASN A 84 4.015 24.609 1.588 1.00 15.68 ATOM 700 O ASN A 84 4.017 24.222 0.408 1.00 17.02 ATOM 701 CB ASN A 84 1.707 25.469 1.147 1.00 17.22 ATOM 702 CG ASN A 84 0.322 25.658 1.712 1.00 19.46 ATOM 703 OD1 ASN A 84 -0.228 26.754 1.679 1.00 23.16 ATOM 704 ND2 ASN A 84 -0.245 24.591 2.233 1.00 24.18 ATOM 705 N GLY A 85 5.090 24.548 2.366 1.00 14.76 ATOM 706 CA GLY A 85 6.314 23.909 1.934 1.00 14.46 ATOM 707 C GLY A 85 7.266 24.749 1.112 1.00 14.17 ATOM 708 O GLY A 85 8.340 24.271 0.746 1.00 15.29 ATOM 709 N GLU A 86 6.855 25.967 0.773 0.50 14.06 ATOM 710 CA GLU A 86 7.633 26.809 -0.123 0.50 13.62 ATOM 711 C GLU A 86 8.157 28.002 0.631 0.50 12.66 ATOM 712 O GLU A 86 7.433 28.639 1.390 0.50 12.39 ATOM 713 CB GLU A 86 6.787 27.288 -1.303 0.50 14.19 ATOM 714 CG GLU A 86 7.515 28.261 -2.207 0.50 15.48 ATOM 715 CD GLU A 86 6.821 28.469 -3.549 0.50 17.16 ATOM 716 OE1 GLU A 86 6.147 27.528 -4.034 0.50 18.97 ATOM 717 OE2 GLU A 86 6.972 29.568 -4.130 0.50 15.47 ATOM 718 N MET A 87 9.421 28.323 0.423 0.50 12.10 ATOM 719 CA MET A 87 9.925 29.474 1.109 0.50 12.02 ATOM 720 C MET A 87 9.283 30.752 0.618 0.50 11.72 ATOM 721 O MET A 87 9.001 30.944 -0.569 0.50 11.31 ATOM 722 CB MET A 87 11.415 29.612 0.980 0.50 12.38 ATOM 723 CG MET A 87 11.768 30.792 1.774 0.50 12.56 ATOM 724 S MET A 87 13.237 31.791 1.276 0.50 13.09 ATOM 725 CE MET A 87 13.591 31.346 -0.593 0.50 8.23 ATOM 726 N VAL A 88 9.069 31.661 1.542 1.00 11.58 ATOM 727 CA VAL A 88 8.528 32.963 1.141 1.00 12.12 ATOM 728 C VAL A 88 9.289 34.144 1.744 1.00 10.93 ATOM 729 O VAL A 88 9.027 35.294 1.380 1.00 10.29 ATOM 730 CB VAL A 88 7.020 33.107 1.456 1.00 13.90 ATOM 731 CG1 VAL A 88 6.182 32.023 0.747 1.00 15.55 ATOM 732 CG2 VAL A 88 6.783 33.062 2.907 1.00 14.27 ATOM 733 N TRP A 89 10.216 33.863 2.668 1.00 9.78 ATOM 734 CA TRP A 89 10.962 34.917 3.371 1.00 8.93 ATOM 735 C TRP A 89 12.178 34.304 4.036 1.00 8.66 ATOM 736 O TRP A 89 12.139 33.153 4.501 1.00 8.45 ATOM 737 CB TRP A 89 10.050 35.544 4.441 1.00 9.21 ATOM 738 CG TRP A 89 10.644 36.505 5.468 1.00 8.99 ATOM 739 CD1 TRP A 89 10.599 37.883 5.445 1.00 10.40 ATOM 740 CD2 TRP A 89 11.259 36.153 6.723 1.00 9.00 ATOM 741 NE1 TRP A 89 11.156 38.394 6.598 1.00 10.55 ATOM 742 CE2 TRP A 89 11.552 37.354 7.400 1.00 9.57 ATOM 743 CE3 TRP A 89 11.570 34.927 7.346 1.00 9.10 ATOM 744 CZ2 TRP A 89 12.177 37.375 8.640 1.00 9.35 ATOM 745 CZ3 TRP A 89 12.172 34.948 8.582 1.00 8.86 ATOM 746 CH2 TRP A 89 12.467 36.167 9.221 1.00 9.70 ATOM 747 N ASN A 90 13.257 35.077 4.093 1.00 8.80 ATOM 748 CA ASN A 90 14.375 34.735 4.969 1.00 9.25 ATOM 749 C ASN A 90 15.056 36.021 5.453 1.00 9.15 ATOM 750 O ASN A 90 14.966 37.067 4.792 1.00 10.03 ATOM 751 CB ASN A 90 15.376 33.827 4.250 1.00 9.32 ATOM 752 CG ASN A 90 16.160 34.548 3.174 1.00 12.15 ATOM 753 OD1 ASN A 90 17.157 35.196 3.458 1.00 14.58 ATOM 754 ND2 ASN A 90 15.716 34.427 1.925 1.00 13.93 ATOM 755 N ARG A 91 15.738 35.921 6.590 1.00 9.26 ATOM 756 CA ARG A 91 16.588 36.990 7.095 1.00 8.83 ATOM 757 C ARG A 91 17.732 36.363 7.846 1.00 9.03 ATOM 758 O ARG A 91 17.643 35.205 8.284 1.00 9.30 ATOM 759 CB ARG A 91 15.835 37.939 8.045 1.00 9.50 ATOM 760 CG ARG A 91 14.860 38.911 7.396 1.00 8.73 ATOM 761 CD ARG A 91 15.498 39.849 6.372 1.00 8.93 ATOM 762 NE ARG A 91 14.557 40.881 5.937 1.00 10.27 ATOM 763 CZ ARG A 91 13.623 40.710 4.997 1.00 9.81 ATOM 764 NH1 ARG A 91 13.514 39.547 4.357 1.00 9.09 ATOM 765 NH2 ARG A 91 12.800 41.712 4.688 1.00 11.86 ATOM 766 N ASP A 92 18.803 37.123 8.035 1.00 9.88 ATOM 767 CA ASP A 92 19.919 36.589 8.797 1.00 10.35 ATOM 768 C ASP A 92 20.469 37.628 9.752 1.00 10.70 ATOM 769 O ASP A 92 20.126 38.813 9.661 1.00 10.76 ATOM 770 CB ASP A 92 21.021 36.047 7.873 1.00 10.47 ATOM 771 CG ASP A 92 21.529 37.092 6.916 1.00 12.49 ATOM 772 OD1 ASP A 92 22.308 37.973 7.346 1.00 15.61 ATOM 773 OD2 ASP A 92 21.168 37.031 5.713 1.00 13.99 ATOM 774 N HSD A 93 21.296 37.154 10.687 1.00 11.28 ATOM 775 CA HSD A 93 21.932 38.016 11.697 1.00 11.89 ATOM 776 C HSD A 93 20.935 38.916 12.401 1.00 12.55 ATOM 777 O HSD A 93 19.841 38.458 12.747 1.00 12.00 ATOM 778 CB HSD A 93 23.142 38.760 11.105 1.00 12.74 ATOM 779 CG HSD A 93 24.191 37.838 10.571 1.00 13.41 ATOM 780 ND1 HSD A 93 24.169 37.359 9.281 1.00 15.34 ATOM 781 CD2 HSD A 93 25.290 37.296 11.154 1.00 15.07 ATOM 782 CE1 HSD A 93 25.190 36.538 9.100 1.00 14.92 ATOM 783 NE2 HSD A 93 25.894 36.495 10.218 1.00 15.71 ATOM 784 N GLY A 94 21.283 40.184 12.616 1.00 12.85 ATOM 785 CA GLY A 94 20.394 41.093 13.330 1.00 12.99 ATOM 786 C GLY A 94 19.065 41.431 12.687 1.00 12.55 ATOM 787 O GLY A 94 18.197 42.016 13.333 1.00 13.50 ATOM 788 N ASP A 95 18.896 41.062 11.417 1.00 12.41 ATOM 789 CA ASP A 95 17.605 41.241 10.750 1.00 13.42 ATOM 790 C ASP A 95 16.553 40.238 11.199 1.00 12.10 ATOM 791 O ASP A 95 15.391 40.344 10.794 1.00 13.87 ATOM 792 CB ASP A 95 17.742 41.113 9.239 1.00 13.15 ATOM 793 CG ASP A 95 18.164 42.398 8.557 1.00 17.70 ATOM 794 OD1 ASP A 95 18.099 43.508 9.151 1.00 20.52 ATOM 795 OD2 ASP A 95 18.545 42.280 7.378 1.00 20.57 ATOM 796 N ILE A 96 16.947 39.257 12.017 1.00 10.84 ATOM 797 CA ILE A 96 15.981 38.340 12.630 1.00 10.90 ATOM 798 C ILE A 96 15.526 38.973 13.937 1.00 11.34 ATOM 799 O ILE A 96 16.266 38.986 14.937 1.00 11.61 ATOM 800 CB ILE A 96 16.589 36.947 12.930 1.00 10.04 ATOM 801 CG1 ILE A 96 17.145 36.285 11.657 1.00 9.61 ATOM 802 CG2 ILE A 96 15.515 35.998 13.562 1.00 10.29 ATOM 803 CD ILE A 96 18.138 35.150 11.939 1.00 8.85 ATOM 804 N ASN A 97 14.309 39.494 13.948 1.00 11.76 ATOM 805 CA ASN A 97 13.770 40.090 15.169 1.00 12.26 ATOM 806 C ASN A 97 12.257 39.961 15.126 1.00 12.45 ATOM 807 O ASN A 97 11.688 39.594 14.086 1.00 12.23 ATOM 808 CB ASN A 97 14.245 41.550 15.331 1.00 13.63 ATOM 809 CG ASN A 97 14.029 42.374 14.083 1.00 14.02 ATOM 810 OD1 ASN A 97 12.912 42.487 13.584 1.00 15.43 ATOM 811 ND2 ASN A 97 15.110 42.930 13.547 1.00 18.61 ATOM 812 N VAL A 98 11.599 40.262 16.246 0.50 12.45 ATOM 813 CA VAL A 98 10.166 40.026 16.354 0.50 12.41 ATOM 814 C VAL A 98 9.369 40.770 15.285 0.50 13.19 ATOM 815 O VAL A 98 8.368 40.256 14.781 0.50 13.41 ATOM 816 CB VAL A 98 9.631 40.394 17.742 0.50 12.12 ATOM 817 CG1 VAL A 98 8.129 40.209 17.761 0.50 9.97 ATOM 818 CG2 VAL A 98 10.312 39.543 18.819 0.50 11.73 ATOM 819 N SER A 99 9.817 41.966 14.920 0.50 13.66 ATOM 820 CA SER A 99 9.129 42.726 13.874 0.50 14.27 ATOM 821 C SER A 99 9.337 42.167 12.462 0.50 13.62 ATOM 822 O SER A 99 8.397 42.154 11.664 0.50 13.86 ATOM 823 CB SER A 99 9.464 44.217 13.942 0.50 14.93 ATOM 824 OG SER A 99 10.860 44.456 14.012 0.50 16.86 ATOM 825 N SER A 100 10.544 41.703 12.137 1.00 13.24 ATOM 826 CA SER A 100 10.752 41.124 10.812 1.00 13.15 ATOM 827 C SER A 100 10.040 39.786 10.646 1.00 12.81 ATOM 828 O SER A 100 9.497 39.490 9.578 1.00 12.30 ATOM 829 CB SER A 100 12.227 41.027 10.457 1.00 12.89 ATOM 830 OG SER A 100 12.870 39.983 11.170 1.00 12.95 ATOM 831 N LEU A 101 10.030 38.985 11.710 1.00 11.80 ATOM 832 CA LEU A 101 9.278 37.738 11.710 1.00 11.70 ATOM 833 C LEU A 101 7.798 38.025 11.498 1.00 12.46 ATOM 834 O LEU A 101 7.126 37.335 10.733 1.00 12.56 ATOM 835 CB LEU A 101 9.531 36.960 13.009 1.00 10.95 ATOM 836 CG LEU A 101 10.956 36.383 13.160 1.00 9.90 ATOM 837 CD1 LEU A 101 11.322 36.165 14.621 1.00 11.15 ATOM 838 CD2 LEU A 101 11.104 35.073 12.393 1.00 11.18 ATOM 839 N ALA A 102 7.299 39.070 12.152 1.00 12.98 ATOM 840 CA ALA A 102 5.896 39.446 11.978 1.00 13.71 ATOM 841 C ALA A 102 5.586 39.916 10.546 1.00 14.57 ATOM 842 O ALA A 102 4.553 39.562 9.975 1.00 15.23 ATOM 843 CB ALA A 102 5.515 40.493 12.990 1.00 13.93 ATOM 844 N GLN A 103 6.508 40.665 9.953 1.00 15.31 ATOM 845 CA GLN A 103 6.363 41.113 8.568 1.00 16.47 ATOM 846 C GLN A 103 6.334 39.952 7.591 1.00 16.27 ATOM 847 O GLN A 103 5.644 40.019 6.569 1.00 16.38 ATOM 848 CB GLN A 103 7.504 42.046 8.192 1.00 18.05 ATOM 849 CG GLN A 103 7.421 43.424 8.807 1.00 21.88 ATOM 850 CD GLN A 103 8.808 44.041 9.092 1.00 27.05 ATOM 851 OE1 GLN A 103 9.811 43.699 8.456 1.00 28.57 ATOM 852 NE2 GLN A 103 8.859 44.942 10.056 1.00 29.12 ATOM 853 N ALA A 104 7.060 38.879 7.914 1.00 15.16 ATOM 854 CA ALA A 104 7.102 37.702 7.050 1.00 15.24 ATOM 855 C ALA A 104 5.722 37.116 6.815 1.00 16.05 ATOM 856 O ALA A 104 5.458 36.542 5.757 1.00 15.84 ATOM 857 CB ALA A 104 8.030 36.636 7.651 1.00 14.57 ATOM 858 N GLU A 105 4.842 37.261 7.801 1.00 17.46 ATOM 859 CA GLU A 105 3.511 36.665 7.739 1.00 18.96 ATOM 860 C GLU A 105 2.504 37.453 6.906 1.00 20.76 ATOM 861 O GLU A 105 1.461 36.900 6.533 1.00 22.14 ATOM 862 CB GLU A 105 2.938 36.495 9.145 1.00 18.24 ATOM 863 CG GLU A 105 3.800 35.677 10.078 1.00 18.38 ATOM 864 CD GLU A 105 3.113 35.429 11.405 1.00 18.75 ATOM 865 OE1 GLU A 105 2.912 36.388 12.180 1.00 19.70 ATOM 866 OE2 GLU A 105 2.782 34.263 11.669 1.00 21.60 ATOM 867 N GLU A 106 2.810 38.718 6.622 1.00 22.42 ATOM 868 CA GLU A 106 1.846 39.661 6.018 1.00 24.57 ATOM 869 C GLU A 106 1.456 39.305 4.593 1.00 25.34 ATOM 870 O GLU A 106 2.188 38.621 3.877 1.00 25.67 ATOM 871 CB GLU A 106 2.386 41.088 6.040 1.00 25.00 ATOM 872 CG GLU A 106 2.476 41.709 7.420 1.00 28.07 ATOM 873 CD GLU A 106 2.882 43.177 7.379 1.00 32.56 ATOM 874 OE1 GLU A 106 2.184 43.969 6.698 1.00 35.27 ATOM 875 OE2 GLU A 106 3.897 43.542 8.023 1.00 32.72 TER END