HEADER OXYGEN STORAGE/TRANSPORT 15-FEB-01 1I3D COMPND HEMOGLOBIN GAMMA CHAINS; EXPDTA X-RAY DIFFRACTION ATOM 1 N GLY B 1 2.431 46.628 -4.604 1.00 32.97 ATOM 2 CA GLY B 1 3.776 47.088 -4.248 1.00 28.98 ATOM 3 C GLY B 1 4.523 47.460 -5.428 1.00 30.45 ATOM 4 O GLY B 1 4.115 47.364 -6.559 1.00 28.18 ATOM 5 N HIS B 2 5.818 48.079 -5.245 1.00 25.80 ATOM 6 CA HIS B 2 6.538 48.515 -6.202 1.00 25.78 ATOM 7 C HIS B 2 8.067 48.823 -5.751 1.00 26.67 ATOM 8 O HIS B 2 8.239 49.688 -4.903 1.00 26.49 ATOM 9 CB HIS B 2 6.020 49.931 -6.813 1.00 31.55 ATOM 10 CG HIS B 2 6.899 50.536 -7.678 1.00 27.84 ATOM 11 ND1 HIS B 2 7.273 50.104 -8.982 1.00 29.50 ATOM 12 CD2 HIS B 2 7.613 51.848 -7.446 1.00 32.90 ATOM 13 CE1 HIS B 2 8.089 50.979 -9.564 1.00 30.90 ATOM 14 NE2 HIS B 2 8.253 52.075 -8.642 1.00 29.67 ATOM 15 N PHE B 3 8.943 48.147 -6.359 1.00 22.57 ATOM 16 CA PHE B 3 10.439 48.435 -5.974 1.00 21.05 ATOM 17 C PHE B 3 10.821 49.506 -6.803 1.00 22.18 ATOM 18 O PHE B 3 10.671 49.531 -8.059 1.00 25.15 ATOM 19 CB PHE B 3 11.263 47.148 -6.306 1.00 19.26 ATOM 20 CG PHE B 3 10.949 45.986 -5.354 1.00 16.76 ATOM 21 CD1 PHE B 3 10.205 44.977 -5.727 1.00 16.03 ATOM 22 CD2 PHE B 3 11.480 45.991 -4.072 1.00 16.08 ATOM 23 CE1 PHE B 3 9.960 43.873 -4.857 1.00 17.12 ATOM 24 CE2 PHE B 3 11.210 44.966 -3.195 1.00 15.74 ATOM 25 CZ PHE B 3 10.441 43.897 -3.600 1.00 14.55 ATOM 26 N THR B 4 11.578 50.548 -6.236 1.00 20.26 ATOM 27 CA THR B 4 12.182 51.526 -6.942 1.00 21.01 ATOM 28 C THR B 4 13.421 51.219 -7.499 1.00 22.26 ATOM 29 O THR B 4 14.026 50.106 -7.147 1.00 21.53 ATOM 30 CB THR B 4 12.330 52.820 -6.060 1.00 20.13 ATOM 31 OG1 THR B 4 13.397 52.525 -5.078 1.00 18.14 ATOM 32 CG2 THR B 4 11.085 53.191 -5.313 1.00 18.55 ATOM 33 N GLU B 5 14.078 51.985 -8.389 1.00 20.74 ATOM 34 CA GLU B 5 15.291 51.666 -8.918 1.00 19.97 ATOM 35 C GLU B 5 16.295 51.583 -7.730 1.00 19.20 ATOM 36 O GLU B 5 17.264 50.751 -7.749 1.00 17.18 ATOM 37 CB GLU B 5 15.808 52.712 -9.973 1.00 24.12 ATOM 38 CG GLU B 5 15.107 52.675 -11.275 1.00 22.46 ATOM 39 CD GLU B 5 15.347 51.314 -12.064 1.00 24.22 ATOM 40 OE1 GLU B 5 14.670 51.080 -13.174 1.00 28.33 ATOM 41 OE2 GLU B 5 16.256 50.421 -11.798 1.00 30.00 ATOM 42 N GLU B 6 16.126 52.478 -6.764 1.00 17.30 ATOM 43 CA GLU B 6 17.028 52.566 -5.662 1.00 17.37 ATOM 44 C GLU B 6 16.840 51.224 -4.777 1.00 17.74 ATOM 45 O GLU B 6 17.852 50.695 -4.321 1.00 14.79 ATOM 46 CB GLU B 6 16.787 53.694 -4.736 1.00 18.44 ATOM 47 CG GLU B 6 17.210 55.045 -5.363 1.00 19.37 ATOM 48 CD GLU B 6 16.240 55.641 -6.317 1.00 22.87 ATOM 49 OE1 GLU B 6 16.427 56.808 -6.703 1.00 24.34 ATOM 50 OE2 GLU B 6 15.232 54.943 -6.746 1.00 23.21 ATOM 51 N ASP B 7 15.589 50.851 -4.604 1.00 16.16 ATOM 52 CA ASP B 7 15.321 49.618 -3.852 1.00 14.89 ATOM 53 C ASP B 7 16.112 48.419 -4.482 1.00 15.69 ATOM 54 O ASP B 7 16.756 47.658 -3.859 1.00 13.74 ATOM 55 CB ASP B 7 13.844 49.251 -3.859 1.00 14.69 ATOM 56 CG ASP B 7 12.986 50.206 -3.028 1.00 15.34 ATOM 57 OD1 ASP B 7 13.510 50.735 -1.964 1.00 14.93 ATOM 58 OD2 ASP B 7 11.813 50.386 -3.340 1.00 15.08 ATOM 59 N LYS B 8 15.882 48.344 -5.852 1.00 15.62 ATOM 60 CA LYS B 8 16.577 47.185 -6.524 1.00 15.10 ATOM 61 C LYS B 8 17.983 47.170 -6.436 1.00 14.11 ATOM 62 O LYS B 8 18.651 46.111 -6.246 1.00 15.90 ATOM 63 CB LYS B 8 16.180 47.229 -8.066 1.00 15.39 ATOM 64 CG LYS B 8 14.617 46.983 -8.224 1.00 19.47 ATOM 65 CD LYS B 8 14.323 47.072 -9.729 1.00 19.59 ATOM 66 CE LYS B 8 12.987 46.872 -10.010 1.00 21.22 ATOM 67 NZ LYS B 8 12.769 47.000 -11.549 1.00 22.79 ATOM 68 N ALA B 9 18.690 48.376 -6.557 1.00 14.90 ATOM 69 CA ALA B 9 20.083 48.414 -6.473 1.00 13.16 ATOM 70 C ALA B 9 20.615 48.065 -5.064 1.00 12.83 ATOM 71 O ALA B 9 21.604 47.422 -4.925 1.00 14.46 ATOM 72 CB ALA B 9 20.626 49.842 -6.885 1.00 16.38 ATOM 73 N THR B 10 19.854 48.522 -4.065 1.00 12.64 ATOM 74 CA THR B 10 20.236 48.275 -2.653 1.00 12.91 ATOM 75 C THR B 10 20.073 46.798 -2.374 1.00 11.82 ATOM 76 O THR B 10 20.988 46.204 -1.723 1.00 11.58 ATOM 77 CB THR B 10 19.272 49.090 -1.761 1.00 13.42 ATOM 78 OG1 THR B 10 19.705 50.463 -1.745 1.00 12.88 ATOM 79 CG2 THR B 10 19.411 48.539 -0.305 1.00 13.68 ATOM 80 N ILE B 11 18.983 46.184 -2.792 1.00 11.25 ATOM 81 CA ILE B 11 18.759 44.745 -2.526 1.00 10.98 ATOM 82 C ILE B 11 19.800 43.917 -3.230 1.00 12.83 ATOM 83 O ILE B 11 20.401 43.011 -2.646 1.00 12.08 ATOM 84 CB ILE B 11 17.347 44.341 -2.961 1.00 10.02 ATOM 85 CG1 ILE B 11 16.342 44.960 -1.971 1.00 11.04 ATOM 86 CG2 ILE B 11 17.203 42.815 -2.885 1.00 11.58 ATOM 87 CD1 ILE B 11 14.897 44.990 -2.526 1.00 10.00 ATOM 88 N THR B 12 20.019 44.213 -4.510 1.00 11.91 ATOM 89 CA THR B 12 20.955 43.423 -5.321 1.00 13.08 ATOM 90 C THR B 12 22.385 43.591 -4.798 1.00 13.44 ATOM 91 O THR B 12 23.116 42.612 -4.711 1.00 12.87 ATOM 92 CB THR B 12 20.924 43.864 -6.760 1.00 13.57 ATOM 93 OG1 THR B 12 19.601 43.605 -7.346 1.00 15.73 ATOM 94 CG2 THR B 12 21.966 43.087 -7.457 1.00 18.98 ATOM 95 N SER B 13 22.783 44.849 -4.541 1.00 13.69 ATOM 96 CA SER B 13 24.176 45.118 -4.053 1.00 14.79 ATOM 97 C SER B 13 24.459 44.500 -2.728 1.00 16.17 ATOM 98 O SER B 13 25.471 43.749 -2.596 1.00 16.32 ATOM 99 CB SER B 13 24.365 46.604 -3.927 1.00 17.24 ATOM 100 OG SER B 13 25.627 46.942 -3.576 1.00 22.38 ATOM 101 N LEU B 14 23.597 44.654 -1.753 1.00 14.11 ATOM 102 CA LEU B 14 23.850 44.040 -0.386 1.00 12.85 ATOM 103 C LEU B 14 23.789 42.569 -0.466 1.00 14.76 ATOM 104 O LEU B 14 24.569 41.877 0.193 1.00 15.60 ATOM 105 CB LEU B 14 22.812 44.588 0.610 1.00 14.39 ATOM 106 CG LEU B 14 23.196 44.369 2.080 1.00 15.16 ATOM 107 CD1 LEU B 14 24.426 45.163 2.413 1.00 15.83 ATOM 108 CD2 LEU B 14 22.019 44.750 3.092 1.00 18.34 ATOM 109 N TRP B 15 22.886 42.028 -1.280 1.00 14.21 ATOM 110 CA TRP B 15 22.799 40.561 -1.327 1.00 14.30 ATOM 111 C TRP B 15 24.079 39.955 -1.952 1.00 15.06 ATOM 112 O TRP B 15 24.452 38.862 -1.571 1.00 13.32 ATOM 113 CB TRP B 15 21.567 40.190 -2.249 1.00 15.47 ATOM 114 CG TRP B 15 21.426 38.647 -2.222 1.00 16.06 ATOM 115 CD1 TRP B 15 21.712 37.870 -3.358 1.00 16.84 ATOM 116 CD2 TRP B 15 20.891 37.893 -1.195 1.00 13.37 ATOM 117 NE1 TRP B 15 21.408 36.556 -2.979 1.00 17.01 ATOM 118 CE2 TRP B 15 20.878 36.512 -1.709 1.00 17.29 ATOM 119 CE3 TRP B 15 20.434 38.116 0.030 1.00 17.33 ATOM 120 CZ2 TRP B 15 20.489 35.522 -0.917 1.00 17.36 ATOM 121 CZ3 TRP B 15 19.937 37.030 0.839 1.00 17.57 ATOM 122 CH2 TRP B 15 20.089 35.764 0.328 1.00 15.21 ATOM 123 N GLY B 16 24.670 40.686 -2.862 1.00 15.50 ATOM 124 CA GLY B 16 25.917 40.155 -3.530 1.00 15.88 ATOM 125 C GLY B 16 27.040 40.023 -2.468 1.00 18.14 ATOM 126 O GLY B 16 27.963 39.208 -2.793 1.00 19.04 ATOM 127 N LYS B 17 26.933 40.538 -1.338 1.00 15.66 ATOM 128 CA LYS B 17 27.947 40.481 -0.318 1.00 16.19 ATOM 129 C LYS B 17 27.607 39.469 0.806 1.00 17.99 ATOM 130 O LYS B 17 28.303 39.264 1.738 1.00 17.55 ATOM 131 CB LYS B 17 28.201 41.807 0.285 1.00 18.41 ATOM 132 CG LYS B 17 28.568 42.898 -0.732 1.00 19.36 ATOM 133 CD LYS B 17 28.648 44.238 -0.038 1.00 20.73 ATOM 134 CE LYS B 17 28.852 45.304 -1.051 1.00 21.57 ATOM 135 NZ LYS B 17 29.003 46.671 -0.456 1.00 20.64 ATOM 136 N VAL B 18 26.312 38.769 0.599 1.00 16.14 ATOM 137 CA VAL B 18 26.081 37.794 1.564 1.00 16.27 ATOM 138 C VAL B 18 26.624 36.393 1.271 1.00 17.79 ATOM 139 O VAL B 18 26.443 35.939 0.119 1.00 19.47 ATOM 140 CB VAL B 18 24.443 37.731 1.623 1.00 15.95 ATOM 141 CG1 VAL B 18 23.955 36.564 2.517 1.00 16.50 ATOM 142 CG2 VAL B 18 23.939 39.051 2.136 1.00 16.79 ATOM 143 N ASN B 19 27.035 35.716 2.301 1.00 19.50 ATOM 144 CA ASN B 19 27.563 34.357 2.139 1.00 18.98 ATOM 145 C ASN B 19 26.261 33.401 2.356 1.00 21.04 ATOM 146 O ASN B 19 25.904 33.187 3.481 1.00 23.78 ATOM 147 CB ASN B 19 28.537 34.146 3.200 1.00 24.64 ATOM 148 CG ASN B 19 28.934 32.524 3.133 1.00 28.76 ATOM 149 OD1 ASN B 19 29.770 32.276 2.032 1.00 31.01 ATOM 150 ND2 ASN B 19 28.765 31.843 3.930 1.00 30.80 ATOM 151 N VAL B 20 25.774 32.886 1.279 1.00 24.04 ATOM 152 CA VAL B 20 24.532 31.962 1.342 1.00 26.85 ATOM 153 C VAL B 20 25.168 30.556 1.664 1.00 23.95 ATOM 154 O VAL B 20 24.702 29.561 1.098 1.00 29.87 ATOM 155 CB VAL B 20 23.631 31.996 -0.006 1.00 25.14 ATOM 156 CG1 VAL B 20 22.803 31.209 0.155 1.00 21.25 ATOM 157 CG2 VAL B 20 23.655 33.347 -0.531 1.00 24.62 ATOM 158 N GLU B 21 26.178 30.529 2.534 1.00 25.46 ATOM 159 CA GLU B 21 26.609 28.970 3.095 1.00 22.93 ATOM 160 C GLU B 21 26.534 29.244 4.492 1.00 21.17 ATOM 161 O GLU B 21 26.375 28.039 5.124 1.00 18.29 ATOM 162 CB GLU B 21 28.083 28.933 2.794 1.00 24.50 ATOM 163 CG GLU B 21 28.786 27.813 2.958 1.00 25.56 ATOM 164 CD GLU B 21 28.113 26.578 2.401 1.00 20.59 ATOM 165 OE1 GLU B 21 28.163 26.475 1.172 1.00 24.67 ATOM 166 OE2 GLU B 21 27.598 25.765 3.119 1.00 25.67 ATOM 167 N ASP B 22 26.568 30.394 5.077 1.00 19.82 ATOM 168 CA ASP B 22 26.473 30.517 6.558 1.00 21.35 ATOM 169 C ASP B 22 25.246 31.365 6.891 1.00 19.62 ATOM 170 O ASP B 22 24.637 31.091 7.997 1.00 19.16 ATOM 171 CB ASP B 22 27.734 31.200 7.144 1.00 21.17 ATOM 172 CG ASP B 22 28.920 30.319 6.791 1.00 20.36 ATOM 173 OD1 ASP B 22 29.010 29.260 7.023 1.00 19.87 ATOM 174 OD2 ASP B 22 29.997 31.110 6.329 1.00 20.09 ATOM 175 N ALA B 23 24.915 32.347 6.124 1.00 16.25 ATOM 176 CA ALA B 23 23.822 33.285 6.424 1.00 14.97 ATOM 177 C ALA B 23 22.492 32.468 6.573 1.00 14.91 ATOM 178 O ALA B 23 21.622 32.831 7.374 1.00 12.76 ATOM 179 CB ALA B 23 23.682 34.380 5.468 1.00 15.08 ATOM 180 N GLY B 24 22.311 31.522 5.656 1.00 13.95 ATOM 181 CA GLY B 24 21.055 30.755 5.692 1.00 14.91 ATOM 182 C GLY B 24 20.891 29.997 7.001 1.00 13.22 ATOM 183 O GLY B 24 19.864 30.128 7.667 1.00 14.13 ATOM 184 N GLY B 25 21.944 29.291 7.429 1.00 13.89 ATOM 185 CA GLY B 25 21.865 28.549 8.696 1.00 13.34 ATOM 186 C GLY B 25 21.674 29.523 9.881 1.00 14.24 ATOM 187 O GLY B 25 20.938 29.250 10.831 1.00 13.49 ATOM 188 N GLU B 26 22.328 30.698 9.801 1.00 13.03 ATOM 189 CA GLU B 26 22.258 31.658 10.825 1.00 11.74 ATOM 190 C GLU B 26 20.846 32.245 10.947 1.00 12.82 ATOM 191 O GLU B 26 20.357 32.517 12.043 1.00 11.48 ATOM 192 CB GLU B 26 23.213 32.844 10.573 1.00 15.47 ATOM 193 CG GLU B 26 24.640 32.396 10.779 1.00 17.80 ATOM 194 CD GLU B 26 25.640 33.584 10.262 1.00 16.40 ATOM 195 OE1 GLU B 26 25.430 34.789 11.127 1.00 21.46 ATOM 196 OE2 GLU B 26 26.409 33.441 9.597 1.00 16.87 ATOM 197 N THR B 27 20.194 32.451 9.783 1.00 10.29 ATOM 198 CA THR B 27 18.876 33.039 9.785 1.00 9.66 ATOM 199 C THR B 27 17.815 32.049 10.280 1.00 11.77 ATOM 200 O THR B 27 16.974 32.402 11.104 1.00 9.76 ATOM 201 CB THR B 27 18.510 33.549 8.371 1.00 10.95 ATOM 202 OG1 THR B 27 19.446 34.545 7.990 1.00 10.28 ATOM 203 CG2 THR B 27 17.131 34.155 8.381 1.00 13.94 ATOM 204 N LEU B 28 17.870 30.814 9.739 1.00 9.07 ATOM 205 CA LEU B 28 16.845 29.848 10.188 1.00 8.83 ATOM 206 C LEU B 28 17.083 29.476 11.664 1.00 8.57 ATOM 207 O LEU B 28 16.155 29.359 12.414 1.00 9.12 ATOM 208 CB LEU B 28 16.992 28.559 9.325 1.00 9.96 ATOM 209 CG LEU B 28 16.033 27.432 9.725 1.00 10.28 ATOM 210 CD1 LEU B 28 14.600 27.885 9.732 1.00 11.40 ATOM 211 CD2 LEU B 28 16.229 26.277 8.647 1.00 12.31 ATOM 212 N GLY B 29 18.409 29.362 12.048 1.00 9.62 ATOM 213 CA GLY B 29 18.624 29.049 13.445 1.00 8.48 ATOM 214 C GLY B 29 18.112 30.124 14.347 1.00 9.21 ATOM 215 O GLY B 29 17.561 29.859 15.450 1.00 8.55 ATOM 216 N ARG B 30 18.327 31.405 13.972 1.00 9.20 ATOM 217 CA ARG B 30 17.899 32.496 14.826 1.00 9.61 ATOM 218 C ARG B 30 16.370 32.500 14.897 1.00 9.55 ATOM 219 O ARG B 30 15.816 32.773 15.992 1.00 10.73 ATOM 220 CB ARG B 30 18.446 33.848 14.201 1.00 11.63 ATOM 221 CG ARG B 30 18.229 35.010 15.032 1.00 11.40 ATOM 222 CD ARG B 30 19.116 36.221 14.494 1.00 13.08 ATOM 223 NE ARG B 30 20.502 36.112 14.772 1.00 12.47 ATOM 224 CZ ARG B 30 21.113 36.662 15.832 1.00 12.12 ATOM 225 NH1 ARG B 30 20.465 37.378 16.733 1.00 13.19 ATOM 226 NH2 ARG B 30 22.439 36.492 15.986 1.00 11.75 ATOM 227 N LEU B 31 15.714 32.223 13.820 1.00 8.68 ATOM 228 CA LEU B 31 14.256 32.152 13.852 1.00 9.47 ATOM 229 C LEU B 31 13.833 31.105 14.868 1.00 9.14 ATOM 230 O LEU B 31 12.942 31.373 15.725 1.00 8.51 ATOM 231 CB LEU B 31 13.691 31.704 12.455 1.00 10.38 ATOM 232 CG LEU B 31 12.171 31.482 12.457 1.00 10.39 ATOM 233 CD1 LEU B 31 11.473 32.872 12.377 1.00 11.13 ATOM 234 CD2 LEU B 31 11.818 30.708 11.120 1.00 10.83 ATOM 235 N LEU B 32 14.428 29.929 14.852 1.00 9.66 ATOM 236 CA LEU B 32 14.036 28.866 15.743 1.00 8.50 ATOM 237 C LEU B 32 14.290 29.172 17.271 1.00 10.05 ATOM 238 O LEU B 32 13.546 28.705 18.080 1.00 10.05 ATOM 239 CB LEU B 32 14.739 27.558 15.391 1.00 10.73 ATOM 240 CG LEU B 32 14.374 27.065 13.969 1.00 12.00 ATOM 241 CD1 LEU B 32 15.397 25.970 13.490 1.00 11.81 ATOM 242 CD2 LEU B 32 12.986 26.486 13.961 1.00 12.06 ATOM 243 N VAL B 33 15.333 29.918 17.496 1.00 9.69 ATOM 244 CA VAL B 33 15.671 30.322 18.890 1.00 9.72 ATOM 245 C VAL B 33 14.772 31.418 19.381 1.00 11.62 ATOM 246 O VAL B 33 14.138 31.306 20.475 1.00 11.28 ATOM 247 CB VAL B 33 17.121 30.715 18.952 1.00 10.35 ATOM 248 CG1 VAL B 33 17.468 31.271 20.393 1.00 10.55 ATOM 249 CG2 VAL B 33 18.015 29.521 18.618 1.00 11.25 ATOM 250 N VAL B 34 14.723 32.501 18.656 1.00 11.86 ATOM 251 CA VAL B 34 13.959 33.696 19.049 1.00 12.32 ATOM 252 C VAL B 34 12.448 33.503 19.102 1.00 11.63 ATOM 253 O VAL B 34 11.757 33.992 19.973 1.00 12.88 ATOM 254 CB VAL B 34 14.289 34.872 18.121 1.00 11.44 ATOM 255 CG1 VAL B 34 13.580 36.141 18.570 1.00 13.78 ATOM 256 CG2 VAL B 34 15.864 35.093 18.193 1.00 13.31 ATOM 257 N TYR B 35 11.909 32.727 18.115 1.00 11.57 ATOM 258 CA TYR B 35 10.466 32.461 18.074 1.00 10.86 ATOM 259 C TYR B 35 10.255 30.932 18.053 1.00 12.99 ATOM 260 O TYR B 35 9.968 30.328 17.049 1.00 10.81 ATOM 261 CB TYR B 35 9.942 33.089 16.752 1.00 12.84 ATOM 262 CG TYR B 35 10.314 34.523 16.619 1.00 12.43 ATOM 263 CD1 TYR B 35 9.682 35.566 17.363 1.00 14.28 ATOM 264 CD2 TYR B 35 11.270 34.936 15.698 1.00 13.18 ATOM 265 CE1 TYR B 35 9.998 36.877 17.249 1.00 14.26 ATOM 266 CE2 TYR B 35 11.645 36.250 15.607 1.00 14.52 ATOM 267 CZ TYR B 35 11.044 37.204 16.349 1.00 15.09 ATOM 268 OH TYR B 35 11.331 38.578 16.164 1.00 16.29 ATOM 269 N PRO B 36 10.395 30.323 19.255 1.00 12.12 ATOM 270 CA PRO B 36 10.300 28.893 19.511 1.00 14.02 ATOM 271 C PRO B 36 9.169 28.116 18.860 1.00 11.82 ATOM 272 O PRO B 36 9.318 26.936 18.570 1.00 11.00 ATOM 273 CB PRO B 36 10.262 28.850 21.046 1.00 15.08 ATOM 274 CG PRO B 36 10.973 30.059 21.485 1.00 16.91 ATOM 275 CD PRO B 36 10.486 31.129 20.485 1.00 14.62 ATOM 276 N TRP B 37 8.010 28.749 18.739 1.00 11.35 ATOM 277 CA TRP B 37 6.916 28.007 18.098 1.00 13.80 ATOM 278 C TRP B 37 7.168 27.488 16.710 1.00 13.22 ATOM 279 O TRP B 37 6.589 26.607 16.220 1.00 12.95 ATOM 280 CB TRP B 37 5.617 28.892 18.160 1.00 12.85 ATOM 281 CG TRP B 37 5.791 30.266 17.646 1.00 15.44 ATOM 282 CD1 TRP B 37 5.502 30.703 16.351 1.00 17.28 ATOM 283 CD2 TRP B 37 6.214 31.386 18.407 1.00 17.46 ATOM 284 NE1 TRP B 37 5.706 32.073 16.318 1.00 16.12 ATOM 285 CE2 TRP B 37 6.123 32.525 17.481 1.00 17.32 ATOM 286 CE3 TRP B 37 6.563 31.599 19.683 1.00 16.39 ATOM 287 CZ2 TRP B 37 6.401 33.851 17.927 1.00 18.14 ATOM 288 CZ3 TRP B 37 6.936 32.928 20.137 1.00 17.81 ATOM 289 CH2 TRP B 37 6.846 33.974 19.219 1.00 16.74 ATOM 290 N THR B 38 8.153 28.259 16.028 1.00 12.27 ATOM 291 CA THR B 38 8.457 27.819 14.659 1.00 11.37 ATOM 292 C THR B 38 9.081 26.455 14.585 1.00 12.25 ATOM 293 O THR B 38 9.112 25.810 13.545 1.00 11.89 ATOM 294 CB THR B 38 9.356 28.854 13.956 1.00 11.31 ATOM 295 OG1 THR B 38 10.576 29.050 14.675 1.00 9.68 ATOM 296 CG2 THR B 38 8.607 30.205 13.848 1.00 11.59 ATOM 297 N GLN B 39 9.664 25.985 15.710 1.00 11.53 ATOM 298 CA GLN B 39 10.323 24.685 15.748 1.00 15.28 ATOM 299 C GLN B 39 9.320 23.532 15.384 1.00 15.46 ATOM 300 O GLN B 39 9.731 22.493 14.959 1.00 15.47 ATOM 301 CB GLN B 39 10.915 24.411 17.133 1.00 13.84 ATOM 302 CG GLN B 39 11.869 25.532 17.626 1.00 14.63 ATOM 303 CD GLN B 39 12.365 25.330 19.009 1.00 14.47 ATOM 304 OE1 GLN B 39 13.071 26.240 19.597 1.00 15.94 ATOM 305 NE2 GLN B 39 12.045 24.225 19.659 1.00 15.77 ATOM 306 N ARG B 40 8.047 23.832 15.635 1.00 15.82 ATOM 307 CA ARG B 40 7.040 22.782 15.339 1.00 18.94 ATOM 308 C ARG B 40 7.070 22.253 13.899 1.00 19.11 ATOM 309 O ARG B 40 6.786 21.149 13.607 1.00 20.23 ATOM 310 CB ARG B 40 5.636 23.360 15.683 1.00 20.61 ATOM 311 CG ARG B 40 4.515 22.532 15.032 1.00 26.17 ATOM 312 CD ARG B 40 4.554 21.149 15.732 1.00 29.24 ATOM 313 NE ARG B 40 3.498 21.088 16.685 1.00 32.36 ATOM 314 CZ ARG B 40 2.154 20.481 16.542 1.00 30.10 ATOM 315 NH1 ARG B 40 1.910 19.936 15.558 1.00 37.55 ATOM 316 NH2 ARG B 40 1.425 20.559 17.622 1.00 27.65 ATOM 317 N PHE B 41 7.487 23.192 12.946 1.00 19.75 ATOM 318 CA PHE B 41 7.505 22.707 11.525 1.00 20.30 ATOM 319 C PHE B 41 8.700 21.860 11.293 1.00 20.69 ATOM 320 O PHE B 41 8.717 21.338 10.096 1.00 22.58 ATOM 321 CB PHE B 41 7.532 24.052 10.678 1.00 19.83 ATOM 322 CG PHE B 41 6.349 24.782 10.698 1.00 20.98 ATOM 323 CD1 PHE B 41 5.159 24.386 10.021 1.00 21.43 ATOM 324 CD2 PHE B 41 6.258 25.950 11.615 1.00 20.71 ATOM 325 CE1 PHE B 41 3.971 25.228 10.244 1.00 22.48 ATOM 326 CE2 PHE B 41 5.036 26.674 11.665 1.00 24.96 ATOM 327 CZ PHE B 41 3.985 26.295 10.970 1.00 22.66 ATOM 328 N PHE B 42 9.701 21.880 11.997 1.00 19.89 ATOM 329 CA PHE B 42 10.901 21.198 11.798 1.00 21.37 ATOM 330 C PHE B 42 11.309 20.104 12.792 1.00 24.04 ATOM 331 O PHE B 42 12.395 19.815 13.138 1.00 22.19 ATOM 332 CB PHE B 42 12.123 22.308 11.771 1.00 20.08 ATOM 333 CG PHE B 42 11.849 23.364 10.896 1.00 19.32 ATOM 334 CD1 PHE B 42 12.164 23.269 9.479 1.00 19.97 ATOM 335 CD2 PHE B 42 11.303 24.547 11.244 1.00 19.41 ATOM 336 CE1 PHE B 42 11.977 24.344 8.655 1.00 20.42 ATOM 337 CE2 PHE B 42 11.105 25.603 10.406 1.00 18.61 ATOM 338 CZ PHE B 42 11.421 25.493 9.103 1.00 17.83 ATOM 339 N ASP B 43 10.148 19.364 13.183 1.00 24.20 ATOM 340 CA ASP B 43 10.322 18.245 14.226 1.00 29.37 ATOM 341 C ASP B 43 11.142 17.144 13.556 1.00 27.45 ATOM 342 O ASP B 43 11.297 16.057 14.244 1.00 30.94 ATOM 343 CB ASP B 43 8.942 17.712 14.690 1.00 23.10 ATOM 344 CG ASP B 43 8.685 18.362 16.063 1.00 30.50 ATOM 345 OD1 ASP B 43 7.821 19.002 16.469 1.00 32.67 ATOM 346 OD2 ASP B 43 9.413 17.987 17.117 1.00 29.83 ATOM 347 N SER B 44 11.517 17.149 12.297 1.00 27.58 ATOM 348 CA SER B 44 12.240 16.155 11.608 1.00 28.76 ATOM 349 C SER B 44 13.715 16.459 11.558 1.00 28.03 ATOM 350 O SER B 44 14.540 15.636 11.179 1.00 28.24 ATOM 351 CB SER B 44 11.743 15.811 10.357 1.00 33.40 ATOM 352 OG SER B 44 12.140 16.993 9.457 1.00 30.93 ATOM 353 N PHE B 45 14.078 17.669 12.059 1.00 25.78 ATOM 354 CA PHE B 45 15.431 18.036 11.999 1.00 24.95 ATOM 355 C PHE B 45 16.303 17.586 13.233 1.00 25.73 ATOM 356 O PHE B 45 17.460 17.717 13.209 1.00 27.50 ATOM 357 CB PHE B 45 15.540 19.661 11.899 1.00 24.61 ATOM 358 CG PHE B 45 15.217 20.089 10.488 1.00 27.75 ATOM 359 CD1 PHE B 45 14.383 19.398 9.673 1.00 27.51 ATOM 360 CD2 PHE B 45 15.782 21.396 10.065 1.00 26.99 ATOM 361 CE1 PHE B 45 14.006 19.851 8.384 1.00 28.78 ATOM 362 CE2 PHE B 45 15.443 21.770 8.879 1.00 27.04 ATOM 363 CZ PHE B 45 14.707 21.221 7.906 1.00 28.71 ATOM 364 N GLY B 46 15.644 16.956 14.200 1.00 25.37 ATOM 365 CA GLY B 46 16.350 16.561 15.329 1.00 23.61 ATOM 366 C GLY B 46 16.138 17.352 16.578 1.00 25.76 ATOM 367 O GLY B 46 15.062 17.984 16.829 1.00 26.06 ATOM 368 N ASN B 47 17.128 17.413 17.499 1.00 26.95 ATOM 369 CA ASN B 47 16.974 18.032 18.735 1.00 27.78 ATOM 370 C ASN B 47 17.195 19.624 18.501 1.00 23.31 ATOM 371 O ASN B 47 18.187 20.015 18.009 1.00 25.50 ATOM 372 CB ASN B 47 18.248 17.648 19.789 1.00 19.36 ATOM 373 CG ASN B 47 18.266 18.389 20.943 1.00 25.68 ATOM 374 OD1 ASN B 47 17.198 18.606 21.775 1.00 23.46 ATOM 375 ND2 ASN B 47 19.271 18.999 21.306 1.00 31.39 ATOM 376 N LEU B 48 16.180 20.339 18.935 1.00 24.41 ATOM 377 CA LEU B 48 16.123 21.792 18.858 1.00 21.66 ATOM 378 C LEU B 48 15.733 22.270 20.238 1.00 21.09 ATOM 379 O LEU B 48 15.122 23.406 20.371 1.00 22.25 ATOM 380 CB LEU B 48 15.104 22.188 17.834 1.00 18.89 ATOM 381 CG LEU B 48 15.163 21.556 16.442 1.00 22.09 ATOM 382 CD1 LEU B 48 13.922 21.956 15.646 1.00 19.22 ATOM 383 CD2 LEU B 48 16.418 22.069 15.725 1.00 20.25 ATOM 384 N SER B 49 16.153 21.620 21.333 1.00 22.35 ATOM 385 CA SER B 49 15.773 22.066 22.657 1.00 23.51 ATOM 386 C SER B 49 16.498 23.160 23.252 1.00 25.69 ATOM 387 O SER B 49 16.249 23.746 24.293 1.00 22.12 ATOM 388 CB SER B 49 16.051 20.753 23.666 1.00 26.93 ATOM 389 OG SER B 49 17.338 20.242 23.422 1.00 26.93 ATOM 390 N SER B 50 17.733 23.592 22.556 1.00 21.94 ATOM 391 CA SER B 50 18.393 24.686 23.073 1.00 21.00 ATOM 392 C SER B 50 19.105 25.510 21.928 1.00 17.56 ATOM 393 O SER B 50 19.208 24.934 20.806 1.00 20.93 ATOM 394 CB SER B 50 19.574 24.292 23.971 1.00 18.78 ATOM 395 OG SER B 50 20.529 23.538 23.297 1.00 20.13 ATOM 396 N ALA B 51 19.508 26.661 22.216 1.00 18.87 ATOM 397 CA ALA B 51 20.193 27.478 21.198 1.00 17.02 ATOM 398 C ALA B 51 21.325 26.779 20.650 1.00 18.18 ATOM 399 O ALA B 51 21.622 26.731 19.436 1.00 19.02 ATOM 400 CB ALA B 51 20.573 28.895 21.816 1.00 18.89 ATOM 401 N SER B 52 22.218 26.212 21.621 1.00 17.92 ATOM 402 CA SER B 52 23.380 25.502 21.064 1.00 18.40 ATOM 403 C SER B 52 23.035 24.366 20.170 1.00 18.17 ATOM 404 O SER B 52 23.658 24.113 19.209 1.00 18.16 ATOM 405 CB SER B 52 24.186 25.034 22.411 1.00 20.40 ATOM 406 OG SER B 52 25.549 24.711 22.053 1.00 26.85 ATOM 407 N ALA B 53 21.990 23.557 20.598 1.00 18.37 ATOM 408 CA ALA B 53 21.614 22.403 19.723 1.00 16.26 ATOM 409 C ALA B 53 21.123 22.876 18.355 1.00 18.65 ATOM 410 O ALA B 53 21.517 22.332 17.320 1.00 17.09 ATOM 411 CB ALA B 53 20.434 21.687 20.445 1.00 18.49 ATOM 412 N ILE B 54 20.370 23.977 18.375 1.00 17.53 ATOM 413 CA ILE B 54 19.789 24.518 17.023 1.00 15.02 ATOM 414 C ILE B 54 20.885 25.061 16.224 1.00 17.57 ATOM 415 O ILE B 54 21.009 24.659 15.005 1.00 16.13 ATOM 416 CB ILE B 54 18.799 25.669 17.402 1.00 14.92 ATOM 417 CG1 ILE B 54 17.491 25.029 18.153 1.00 16.78 ATOM 418 CG2 ILE B 54 18.362 26.386 16.077 1.00 17.45 ATOM 419 CD1 ILE B 54 16.642 26.117 18.655 1.00 16.84 ATOM 420 N MET B 55 21.629 25.997 16.734 1.00 18.30 ATOM 421 CA MET B 55 22.690 26.682 15.885 1.00 19.25 ATOM 422 C MET B 55 23.732 25.740 15.461 1.00 21.34 ATOM 423 O MET B 55 24.414 25.981 14.383 1.00 22.27 ATOM 424 CB MET B 55 23.330 27.804 16.684 1.00 17.57 ATOM 425 CG MET B 55 22.395 28.864 17.245 1.00 17.63 ATOM 426 SD MET B 55 21.267 29.566 15.948 1.00 15.84 ATOM 427 CE MET B 55 22.384 30.464 14.834 1.00 19.65 ATOM 428 N GLY B 56 23.897 24.499 16.086 1.00 19.49 ATOM 429 CA GLY B 56 24.891 23.594 15.738 1.00 22.43 ATOM 430 C GLY B 56 24.278 22.363 14.843 1.00 23.61 ATOM 431 O GLY B 56 25.036 21.546 14.411 1.00 22.56 ATOM 432 N ASN B 57 22.960 22.423 14.592 1.00 20.62 ATOM 433 CA ASN B 57 22.356 21.368 13.928 1.00 18.90 ATOM 434 C ASN B 57 22.631 21.413 12.431 1.00 17.89 ATOM 435 O ASN B 57 22.384 22.403 11.751 1.00 17.67 ATOM 436 CB ASN B 57 20.769 21.498 14.148 1.00 20.05 ATOM 437 CG ASN B 57 20.035 20.335 13.629 1.00 19.58 ATOM 438 OD1 ASN B 57 20.035 20.061 12.371 1.00 20.72 ATOM 439 ND2 ASN B 57 19.244 19.700 14.420 1.00 18.93 ATOM 440 N PRO B 58 23.226 20.383 11.908 1.00 18.76 ATOM 441 CA PRO B 58 23.606 20.373 10.436 1.00 17.20 ATOM 442 C PRO B 58 22.432 20.378 9.525 1.00 16.58 ATOM 443 O PRO B 58 22.564 20.936 8.398 1.00 16.33 ATOM 444 CB PRO B 58 24.425 19.039 10.319 1.00 21.76 ATOM 445 CG PRO B 58 23.744 18.109 11.431 1.00 18.85 ATOM 446 CD PRO B 58 23.586 19.029 12.569 1.00 19.85 ATOM 447 N LYS B 59 21.242 19.952 9.921 1.00 17.03 ATOM 448 CA LYS B 59 20.115 19.936 9.053 1.00 16.29 ATOM 449 C LYS B 59 19.548 21.406 8.998 1.00 16.67 ATOM 450 O LYS B 59 18.996 21.802 7.920 1.00 17.16 ATOM 451 CB LYS B 59 18.972 19.038 9.471 1.00 18.92 ATOM 452 CG LYS B 59 19.499 17.461 9.408 1.00 19.22 ATOM 453 CD LYS B 59 18.424 16.543 9.949 1.00 23.53 ATOM 454 CE LYS B 59 17.464 16.353 8.897 1.00 24.27 ATOM 455 NZ LYS B 59 16.445 15.092 9.255 1.00 23.02 ATOM 456 N VAL B 60 19.705 22.106 10.037 1.00 15.77 ATOM 457 CA VAL B 60 19.257 23.553 10.106 1.00 15.92 ATOM 458 C VAL B 60 20.149 24.315 9.128 1.00 15.10 ATOM 459 O VAL B 60 19.661 25.129 8.360 1.00 15.14 ATOM 460 CB VAL B 60 19.373 24.103 11.525 1.00 14.07 ATOM 461 CG1 VAL B 60 19.151 25.598 11.543 1.00 14.45 ATOM 462 CG2 VAL B 60 18.310 23.448 12.418 1.00 14.70 ATOM 463 N LYS B 61 21.450 24.064 9.202 1.00 15.07 ATOM 464 CA LYS B 61 22.380 24.784 8.387 1.00 13.25 ATOM 465 C LYS B 61 22.123 24.430 6.906 1.00 13.89 ATOM 466 O LYS B 61 22.070 25.375 6.038 1.00 13.77 ATOM 467 CB LYS B 61 23.837 24.428 8.762 1.00 15.81 ATOM 468 CG LYS B 61 24.844 25.193 7.905 1.00 19.90 ATOM 469 CD LYS B 61 26.332 24.760 8.346 1.00 23.83 ATOM 470 CE LYS B 61 26.253 24.173 9.798 1.00 23.68 ATOM 471 NZ LYS B 61 25.203 24.730 10.605 1.00 28.14 ATOM 472 N ALA B 62 21.890 23.195 6.597 1.00 12.90 ATOM 473 CA ALA B 62 21.692 22.745 5.291 1.00 14.92 ATOM 474 C ALA B 62 20.369 23.277 4.690 1.00 13.87 ATOM 475 O ALA B 62 20.241 23.598 3.490 1.00 14.51 ATOM 476 CB ALA B 62 21.720 21.209 5.121 1.00 17.65 ATOM 477 N HIS B 63 19.320 23.319 5.550 1.00 13.56 ATOM 478 CA HIS B 63 18.034 23.755 5.034 1.00 11.99 ATOM 479 C HIS B 63 18.063 25.327 4.848 1.00 14.57 ATOM 480 O HIS B 63 17.536 25.828 3.880 1.00 13.72 ATOM 481 CB HIS B 63 16.931 23.450 6.075 1.00 13.60 ATOM 482 CG HIS B 63 15.558 23.760 5.519 1.00 11.88 ATOM 483 ND1 HIS B 63 15.055 22.970 4.528 1.00 14.43 ATOM 484 CD2 HIS B 63 14.728 24.805 5.729 1.00 13.68 ATOM 485 CE1 HIS B 63 13.873 23.525 4.092 1.00 12.61 ATOM 486 NE2 HIS B 63 13.669 24.633 4.905 1.00 13.22 ATOM 487 N GLY B 64 18.732 25.989 5.810 1.00 12.35 ATOM 488 CA GLY B 64 18.794 27.508 5.673 1.00 13.33 ATOM 489 C GLY B 64 19.505 27.828 4.331 1.00 12.19 ATOM 490 O GLY B 64 19.229 28.857 3.767 1.00 12.43 ATOM 491 N LYS B 65 20.417 26.970 3.923 1.00 12.04 ATOM 492 CA LYS B 65 21.122 27.285 2.630 1.00 11.89 ATOM 493 C LYS B 65 20.168 27.271 1.491 1.00 13.07 ATOM 494 O LYS B 65 20.202 28.122 0.591 1.00 13.37 ATOM 495 CB LYS B 65 22.273 26.218 2.414 1.00 13.73 ATOM 496 CG LYS B 65 22.959 26.418 1.034 1.00 16.22 ATOM 497 CD LYS B 65 24.099 25.392 0.844 1.00 18.56 ATOM 498 CE LYS B 65 24.654 25.604 -0.529 1.00 22.74 ATOM 499 NZ LYS B 65 25.863 24.566 -0.745 1.00 24.84 ATOM 500 N LYS B 66 19.178 26.329 1.516 1.00 12.57 ATOM 501 CA LYS B 66 18.159 26.242 0.475 1.00 12.50 ATOM 502 C LYS B 66 17.355 27.463 0.458 1.00 12.46 ATOM 503 O LYS B 66 16.992 28.034 -0.570 1.00 12.58 ATOM 504 CB LYS B 66 17.280 25.004 0.640 1.00 13.77 ATOM 505 CG LYS B 66 18.084 23.677 0.548 1.00 13.82 ATOM 506 CD LYS B 66 17.071 22.533 0.775 1.00 14.48 ATOM 507 CE LYS B 66 17.899 21.216 0.859 1.00 17.22 ATOM 508 NZ LYS B 66 16.893 20.071 1.024 1.00 18.40 ATOM 509 N VAL B 67 16.862 27.880 1.660 1.00 10.99 ATOM 510 CA VAL B 67 16.033 29.045 1.829 1.00 10.95 ATOM 511 C VAL B 67 16.615 30.303 1.232 1.00 12.65 ATOM 512 O VAL B 67 16.037 30.983 0.424 1.00 10.61 ATOM 513 CB VAL B 67 15.758 29.288 3.341 1.00 12.24 ATOM 514 CG1 VAL B 67 14.865 30.535 3.486 1.00 12.20 ATOM 515 CG2 VAL B 67 15.083 28.052 3.895 1.00 15.27 ATOM 516 N LEU B 68 17.908 30.614 1.629 1.00 11.98 ATOM 517 CA LEU B 68 18.500 31.807 1.106 1.00 12.34 ATOM 518 C LEU B 68 18.926 31.729 -0.368 1.00 12.20 ATOM 519 O LEU B 68 18.957 32.706 -1.063 1.00 11.07 ATOM 520 CB LEU B 68 19.795 32.177 1.946 1.00 12.86 ATOM 521 CG LEU B 68 19.405 33.216 3.051 1.00 17.33 ATOM 522 CD1 LEU B 68 18.396 32.597 3.963 1.00 20.01 ATOM 523 CD2 LEU B 68 20.608 33.633 3.786 1.00 18.52 ATOM 524 N THR B 69 19.174 30.466 -0.856 1.00 13.39 ATOM 525 CA THR B 69 19.517 30.348 -2.264 1.00 11.27 ATOM 526 C THR B 69 18.300 30.643 -3.133 1.00 14.02 ATOM 527 O THR B 69 18.361 31.239 -4.163 1.00 12.81 ATOM 528 CB THR B 69 20.002 28.896 -2.569 1.00 12.53 ATOM 529 OG1 THR B 69 21.199 28.667 -1.831 1.00 13.26 ATOM 530 CG2 THR B 69 20.321 28.794 -4.140 1.00 15.21 ATOM 531 N SER B 70 17.083 30.138 -2.608 1.00 13.61 ATOM 532 CA SER B 70 15.847 30.407 -3.358 1.00 12.43 ATOM 533 C SER B 70 15.516 31.912 -3.280 1.00 11.29 ATOM 534 O SER B 70 15.038 32.474 -4.224 1.00 11.83 ATOM 535 CB SER B 70 14.729 29.654 -2.700 1.00 12.96 ATOM 536 OG SER B 70 14.894 28.242 -2.996 1.00 17.19 ATOM 537 N LEU B 71 15.847 32.542 -2.141 1.00 12.34 ATOM 538 CA LEU B 71 15.624 34.002 -2.040 1.00 12.12 ATOM 539 C LEU B 71 16.618 34.734 -2.948 1.00 13.14 ATOM 540 O LEU B 71 16.184 35.677 -3.642 1.00 13.92 ATOM 541 CB LEU B 71 15.933 34.462 -0.566 1.00 14.70 ATOM 542 CG LEU B 71 15.584 35.948 -0.363 1.00 18.84 ATOM 543 CD1 LEU B 71 14.096 36.076 -0.320 1.00 19.85 ATOM 544 CD2 LEU B 71 16.176 36.361 0.992 1.00 18.06 ATOM 545 N GLY B 72 17.773 34.229 -3.040 1.00 14.90 ATOM 546 CA GLY B 72 18.780 34.911 -3.930 1.00 15.52 ATOM 547 C GLY B 72 18.281 34.848 -5.350 1.00 15.74 ATOM 548 O GLY B 72 18.444 35.726 -6.157 1.00 16.17 ATOM 549 N ASP B 73 17.666 33.671 -5.766 1.00 17.04 ATOM 550 CA ASP B 73 17.176 33.577 -7.083 1.00 15.91 ATOM 551 C ASP B 73 16.008 34.529 -7.310 1.00 16.32 ATOM 552 O ASP B 73 15.895 35.180 -8.389 1.00 15.83 ATOM 553 CB ASP B 73 16.739 32.092 -7.397 1.00 16.44 ATOM 554 CG ASP B 73 16.313 31.915 -8.832 1.00 18.66 ATOM 555 OD1 ASP B 73 17.265 31.819 -9.702 1.00 18.11 ATOM 556 OD2 ASP B 73 15.124 31.816 -9.154 1.00 19.70 ATOM 557 N ALA B 74 15.119 34.690 -6.324 1.00 15.65 ATOM 558 CA ALA B 74 14.054 35.554 -6.431 1.00 15.27 ATOM 559 C ALA B 74 14.459 37.037 -6.622 1.00 17.97 ATOM 560 O ALA B 74 13.685 37.849 -7.161 1.00 15.95 ATOM 561 CB ALA B 74 13.117 35.455 -5.215 1.00 16.62 ATOM 562 N ILE B 75 15.595 37.346 -6.069 1.00 16.20 ATOM 563 CA ILE B 75 16.082 38.754 -6.212 1.00 16.16 ATOM 564 C ILE B 75 16.469 39.061 -7.610 1.00 19.00 ATOM 565 O ILE B 75 16.626 40.270 -7.985 1.00 18.77 ATOM 566 CB ILE B 75 17.422 38.924 -5.286 1.00 16.57 ATOM 567 CG1 ILE B 75 16.795 38.950 -3.814 1.00 14.61 ATOM 568 CG2 ILE B 75 18.169 40.058 -5.616 1.00 20.01 ATOM 569 CD1 ILE B 75 17.900 39.045 -2.686 1.00 16.95 ATOM 570 N LYS B 76 16.512 38.037 -8.518 1.00 18.21 ATOM 571 CA LYS B 76 16.661 38.284 -9.923 1.00 19.29 ATOM 572 C LYS B 76 15.335 38.595 -10.591 1.00 20.15 ATOM 573 O LYS B 76 15.300 38.894 -11.874 1.00 20.69 ATOM 574 CB LYS B 76 17.305 37.035 -10.616 1.00 21.04 ATOM 575 CG LYS B 76 18.713 36.730 -10.056 1.00 20.07 ATOM 576 CD LYS B 76 19.262 35.371 -10.835 1.00 20.91 ATOM 577 CE LYS B 76 20.552 35.035 -10.375 1.00 25.19 ATOM 578 NZ LYS B 76 20.609 34.617 -8.894 1.00 28.11 ATOM 579 N HIS B 77 14.192 38.484 -9.923 1.00 16.58 ATOM 580 CA HIS B 77 12.911 38.592 -10.381 1.00 17.06 ATOM 581 C HIS B 77 12.024 39.525 -9.483 1.00 17.18 ATOM 582 O HIS B 77 10.884 39.222 -9.217 1.00 16.01 ATOM 583 CB HIS B 77 12.143 37.285 -10.559 1.00 17.79 ATOM 584 CG HIS B 77 12.968 36.200 -11.337 1.00 20.65 ATOM 585 ND1 HIS B 77 12.746 35.974 -12.703 1.00 21.35 ATOM 586 CD2 HIS B 77 13.957 35.425 -10.973 1.00 18.90 ATOM 587 CE1 HIS B 77 13.585 35.044 -13.107 1.00 19.76 ATOM 588 NE2 HIS B 77 14.350 34.685 -12.090 1.00 20.21 ATOM 589 N LEU B 78 12.637 40.616 -9.096 1.00 18.83 ATOM 590 CA LEU B 78 11.919 41.513 -8.215 1.00 20.82 ATOM 591 C LEU B 78 10.615 42.041 -8.680 1.00 22.69 ATOM 592 O LEU B 78 9.741 42.387 -7.860 1.00 20.07 ATOM 593 CB LEU B 78 12.874 42.662 -7.730 1.00 18.04 ATOM 594 CG LEU B 78 14.092 42.277 -6.902 1.00 20.14 ATOM 595 CD1 LEU B 78 14.923 43.540 -6.650 1.00 16.52 ATOM 596 CD2 LEU B 78 13.628 41.646 -5.579 1.00 20.78 ATOM 597 N ASP B 79 10.446 42.140 -9.983 1.00 21.52 ATOM 598 CA ASP B 79 9.194 42.652 -10.456 1.00 22.62 ATOM 599 C ASP B 79 8.186 41.492 -10.662 1.00 24.29 ATOM 600 O ASP B 79 7.098 41.803 -11.246 1.00 26.99 ATOM 601 CB ASP B 79 9.421 43.439 -11.845 1.00 25.98 ATOM 602 CG ASP B 79 10.089 44.907 -11.597 1.00 25.76 ATOM 603 OD1 ASP B 79 9.924 45.400 -10.501 1.00 26.62 ATOM 604 OD2 ASP B 79 10.797 45.251 -12.437 1.00 28.26 ATOM 605 N ASP B 80 8.481 40.392 -10.398 1.00 22.27 ATOM 606 CA ASP B 80 7.563 39.202 -10.450 1.00 20.66 ATOM 607 C ASP B 80 7.786 38.059 -9.421 1.00 23.02 ATOM 608 O ASP B 80 8.128 36.992 -9.690 1.00 20.92 ATOM 609 CB ASP B 80 7.726 38.479 -11.776 1.00 27.98 ATOM 610 CG ASP B 80 6.620 37.477 -12.012 1.00 23.94 ATOM 611 OD1 ASP B 80 5.592 37.496 -11.291 1.00 27.39 ATOM 612 OD2 ASP B 80 6.834 36.564 -12.774 1.00 28.03 ATOM 613 N LEU B 81 7.749 38.594 -8.103 1.00 20.23 ATOM 614 CA LEU B 81 7.962 37.595 -6.957 1.00 19.94 ATOM 615 C LEU B 81 6.810 36.595 -6.827 1.00 19.83 ATOM 616 O LEU B 81 7.049 35.418 -6.537 1.00 18.33 ATOM 617 CB LEU B 81 8.080 38.337 -5.736 1.00 19.20 ATOM 618 CG LEU B 81 9.374 39.139 -5.687 1.00 16.35 ATOM 619 CD1 LEU B 81 9.502 39.931 -4.246 1.00 18.72 ATOM 620 CD2 LEU B 81 10.576 38.158 -5.775 1.00 17.53 ATOM 621 N LYS B 82 5.593 36.985 -7.212 1.00 20.80 ATOM 622 CA LYS B 82 4.420 36.022 -7.075 1.00 19.22 ATOM 623 C LYS B 82 4.600 34.814 -7.894 1.00 21.79 ATOM 624 O LYS B 82 4.435 33.701 -7.501 1.00 18.98 ATOM 625 CB LYS B 82 3.089 36.740 -7.414 1.00 23.26 ATOM 626 CG LYS B 82 1.900 35.847 -7.278 1.00 22.76 ATOM 627 CD LYS B 82 0.571 36.644 -7.701 1.00 23.58 ATOM 628 CE LYS B 82 0.545 36.808 -9.232 1.00 22.75 ATOM 629 NZ LYS B 82 1.647 37.654 -9.769 1.00 22.85 ATOM 630 N GLY B 83 4.970 35.070 -9.218 1.00 20.22 ATOM 631 CA GLY B 83 5.175 33.928 -10.113 1.00 20.39 ATOM 632 C GLY B 83 6.408 33.120 -9.792 1.00 19.03 ATOM 633 O GLY B 83 6.382 31.877 -9.898 1.00 19.30 ATOM 634 N THR B 84 7.479 33.801 -9.355 1.00 18.54 ATOM 635 CA THR B 84 8.702 33.148 -9.072 1.00 17.66 ATOM 636 C THR B 84 8.590 32.156 -7.825 1.00 17.33 ATOM 637 O THR B 84 9.303 31.177 -7.712 1.00 15.43 ATOM 638 CB THR B 84 9.818 34.138 -8.717 1.00 16.76 ATOM 639 OG1 THR B 84 9.948 35.042 -9.853 1.00 21.10 ATOM 640 CG2 THR B 84 11.223 33.472 -8.527 1.00 18.18 ATOM 641 N PHE B 85 7.666 32.569 -6.903 1.00 17.93 ATOM 642 CA PHE B 85 7.512 31.720 -5.704 1.00 15.26 ATOM 643 C PHE B 85 6.265 30.864 -5.735 1.00 15.96 ATOM 644 O PHE B 85 5.890 30.233 -4.760 1.00 13.85 ATOM 645 CB PHE B 85 7.399 32.760 -4.463 1.00 14.95 ATOM 646 CG PHE B 85 8.675 33.142 -3.912 1.00 15.03 ATOM 647 CD1 PHE B 85 9.549 32.311 -3.380 1.00 15.92 ATOM 648 CD2 PHE B 85 8.983 34.599 -3.921 1.00 14.64 ATOM 649 CE1 PHE B 85 10.841 32.708 -2.817 1.00 15.88 ATOM 650 CE2 PHE B 85 10.153 35.019 -3.338 1.00 14.54 ATOM 651 CZ PHE B 85 11.126 34.045 -2.804 1.00 18.20 ATOM 652 N ALA B 86 5.582 30.824 -6.925 1.00 14.84 ATOM 653 CA ALA B 86 4.330 30.089 -6.985 1.00 15.67 ATOM 654 C ALA B 86 4.417 28.656 -6.511 1.00 14.40 ATOM 655 O ALA B 86 3.551 28.186 -5.779 1.00 14.70 ATOM 656 CB ALA B 86 3.808 30.124 -8.413 1.00 15.51 ATOM 657 N GLN B 87 5.457 27.950 -6.998 1.00 15.38 ATOM 658 CA GLN B 87 5.591 26.554 -6.585 1.00 16.28 ATOM 659 C GLN B 87 5.864 26.384 -5.127 1.00 14.87 ATOM 660 O GLN B 87 5.269 25.511 -4.456 1.00 14.25 ATOM 661 CB GLN B 87 6.731 25.897 -7.429 1.00 17.57 ATOM 662 CG GLN B 87 7.033 24.409 -6.982 1.00 20.32 ATOM 663 CD GLN B 87 8.031 24.379 -5.943 1.00 16.32 ATOM 664 OE1 GLN B 87 8.043 23.302 -5.161 1.00 20.85 ATOM 665 NE2 GLN B 87 8.967 25.282 -5.896 1.00 20.80 ATOM 666 N LEU B 88 6.770 27.276 -4.560 1.00 14.51 ATOM 667 CA LEU B 88 7.029 27.174 -3.086 1.00 14.02 ATOM 668 C LEU B 88 5.768 27.630 -2.245 1.00 13.76 ATOM 669 O LEU B 88 5.656 27.212 -1.144 1.00 12.59 ATOM 670 CB LEU B 88 8.201 28.046 -2.675 1.00 15.22 ATOM 671 CG LEU B 88 9.604 27.477 -3.114 1.00 13.10 ATOM 672 CD1 LEU B 88 10.694 28.460 -2.710 1.00 12.93 ATOM 673 CD2 LEU B 88 9.812 26.125 -2.386 1.00 12.27 ATOM 674 N SER B 89 4.924 28.435 -2.878 1.00 13.89 ATOM 675 CA SER B 89 3.740 28.829 -2.132 1.00 12.65 ATOM 676 C SER B 89 2.853 27.575 -1.937 1.00 14.97 ATOM 677 O SER B 89 2.279 27.360 -0.895 1.00 14.31 ATOM 678 CB SER B 89 2.997 29.978 -2.918 1.00 12.74 ATOM 679 OG SER B 89 1.830 30.392 -2.168 1.00 12.89 ATOM 680 N GLU B 90 2.738 26.827 -3.057 1.00 14.46 ATOM 681 CA GLU B 90 1.917 25.647 -3.038 1.00 15.18 ATOM 682 C GLU B 90 2.456 24.669 -1.968 1.00 14.50 ATOM 683 O GLU B 90 1.727 24.140 -1.151 1.00 14.79 ATOM 684 CB GLU B 90 1.956 24.979 -4.459 1.00 17.51 ATOM 685 CG GLU B 90 1.050 23.833 -4.622 1.00 23.47 ATOM 686 CD GLU B 90 1.272 23.043 -5.876 1.00 28.82 ATOM 687 OE1 GLU B 90 1.814 23.781 -7.022 1.00 28.69 ATOM 688 OE2 GLU B 90 1.273 21.753 -5.951 1.00 29.95 ATOM 689 N LEU B 91 3.782 24.504 -1.960 1.00 14.25 ATOM 690 CA LEU B 91 4.390 23.601 -0.970 1.00 13.81 ATOM 691 C LEU B 91 4.118 24.058 0.451 1.00 14.17 ATOM 692 O LEU B 91 3.611 23.297 1.272 1.00 12.19 ATOM 693 CB LEU B 91 5.921 23.549 -1.174 1.00 13.64 ATOM 694 CG LEU B 91 6.689 22.840 -0.148 1.00 15.35 ATOM 695 CD1 LEU B 91 6.322 21.279 -0.146 1.00 15.96 ATOM 696 CD2 LEU B 91 8.193 23.026 -0.385 1.00 17.23 ATOM 697 N HIS B 92 4.473 25.304 0.759 1.00 13.25 ATOM 698 CA HIS B 92 4.319 25.830 2.115 1.00 13.23 ATOM 699 C HIS B 92 2.848 25.962 2.612 1.00 11.30 ATOM 700 O HIS B 92 2.597 25.704 3.785 1.00 14.06 ATOM 701 CB HIS B 92 4.952 27.219 2.240 1.00 11.78 ATOM 702 CG HIS B 92 6.465 27.123 2.226 1.00 10.53 ATOM 703 ND1 HIS B 92 7.180 27.032 1.019 1.00 9.41 ATOM 704 CD2 HIS B 92 7.348 27.074 3.205 1.00 9.14 ATOM 705 CE1 HIS B 92 8.423 26.945 1.285 1.00 11.29 ATOM 706 NE2 HIS B 92 8.618 26.970 2.630 1.00 8.83 ATOM 707 N CYS B 93 1.917 26.361 1.731 1.00 13.90 ATOM 708 CA CYS B 93 0.493 26.563 2.129 1.00 13.86 ATOM 709 C CYS B 93 -0.302 25.321 2.029 1.00 16.24 ATOM 710 O CYS B 93 -0.879 24.871 3.021 1.00 16.49 ATOM 711 CB CYS B 93 -0.040 27.697 1.299 1.00 14.09 ATOM 712 SG CYS B 93 0.830 29.283 1.425 1.00 11.87 ATOM 713 N ASP B 94 -0.288 24.761 0.833 1.00 17.14 ATOM 714 CA ASP B 94 -1.304 23.569 0.614 1.00 20.16 ATOM 715 C ASP B 94 -0.844 22.301 1.285 1.00 19.94 ATOM 716 O ASP B 94 -1.481 21.525 1.825 1.00 20.09 ATOM 717 CB ASP B 94 -1.442 23.365 -0.826 1.00 19.34 ATOM 718 CG ASP B 94 -2.162 24.399 -1.544 1.00 24.85 ATOM 719 OD1 ASP B 94 -3.259 24.868 -1.179 1.00 25.10 ATOM 720 OD2 ASP B 94 -1.598 24.994 -2.545 1.00 27.11 ATOM 721 N LYS B 95 0.656 22.092 1.257 1.00 19.52 ATOM 722 CA LYS B 95 1.161 20.879 1.814 1.00 22.34 ATOM 723 C LYS B 95 1.590 20.947 3.195 1.00 19.99 ATOM 724 O LYS B 95 1.207 20.111 4.132 1.00 22.39 ATOM 725 CB LYS B 95 2.331 20.456 0.942 1.00 22.28 ATOM 726 CG LYS B 95 2.021 20.411 -0.516 1.00 23.91 ATOM 727 CD LYS B 95 3.145 20.550 -1.462 1.00 26.55 ATOM 728 CE LYS B 95 2.870 20.769 -2.894 1.00 20.31 ATOM 729 NZ LYS B 95 4.037 21.053 -3.644 1.00 19.76 ATOM 730 N LEU B 96 2.407 21.973 3.612 1.00 19.61 ATOM 731 CA LEU B 96 2.912 22.033 4.983 1.00 17.23 ATOM 732 C LEU B 96 2.082 22.854 5.916 1.00 18.59 ATOM 733 O LEU B 96 2.368 22.817 7.183 1.00 19.23 ATOM 734 CB LEU B 96 4.352 22.669 4.899 1.00 17.57 ATOM 735 CG LEU B 96 5.367 21.846 4.089 1.00 23.59 ATOM 736 CD1 LEU B 96 6.532 22.707 3.740 1.00 19.46 ATOM 737 CD2 LEU B 96 5.771 20.650 4.928 1.00 19.97 ATOM 738 N HIS B 97 1.115 23.648 5.444 1.00 17.25 ATOM 739 CA HIS B 97 0.305 24.450 6.325 1.00 17.52 ATOM 740 C HIS B 97 0.999 25.376 7.233 1.00 18.50 ATOM 741 O HIS B 97 0.761 25.577 8.372 1.00 16.01 ATOM 742 CB HIS B 97 -0.615 23.536 7.252 1.00 18.54 ATOM 743 CG HIS B 97 -1.928 23.177 6.438 1.00 23.14 ATOM 744 ND1 HIS B 97 -2.519 23.879 5.485 1.00 24.68 ATOM 745 CD2 HIS B 97 -2.789 22.169 6.752 1.00 21.92 ATOM 746 CE1 HIS B 97 -3.668 23.462 5.096 1.00 23.50 ATOM 747 NE2 HIS B 97 -3.885 22.321 5.975 1.00 26.32 ATOM 748 N VAL B 98 2.073 26.077 6.641 1.00 16.50 ATOM 749 CA VAL B 98 2.751 27.055 7.439 1.00 15.34 ATOM 750 C VAL B 98 2.007 28.264 7.580 1.00 15.19 ATOM 751 O VAL B 98 1.337 28.758 6.728 1.00 16.71 ATOM 752 CB VAL B 98 4.085 27.482 6.482 1.00 16.50 ATOM 753 CG1 VAL B 98 4.743 28.701 7.116 1.00 17.01 ATOM 754 CG2 VAL B 98 5.061 26.332 6.492 1.00 15.66 ATOM 755 N ASP B 99 1.926 28.763 8.875 1.00 17.80 ATOM 756 CA ASP B 99 1.180 29.954 9.162 1.00 16.69 ATOM 757 C ASP B 99 1.781 31.155 8.358 1.00 18.89 ATOM 758 O ASP B 99 2.964 31.368 8.449 1.00 17.05 ATOM 759 CB ASP B 99 1.190 30.278 10.673 1.00 18.33 ATOM 760 CG ASP B 99 0.568 31.339 11.032 1.00 16.56 ATOM 761 OD1 ASP B 99 0.254 32.359 10.376 1.00 22.11 ATOM 762 OD2 ASP B 99 -0.164 31.295 12.271 1.00 22.26 ATOM 763 N PRO B 100 0.963 31.861 7.638 1.00 20.30 ATOM 764 CA PRO B 100 1.357 32.932 6.877 1.00 17.08 ATOM 765 C PRO B 100 2.142 34.012 7.622 1.00 20.72 ATOM 766 O PRO B 100 3.091 34.629 7.064 1.00 20.61 ATOM 767 CB PRO B 100 0.004 33.601 6.344 1.00 23.60 ATOM 768 CG PRO B 100 -0.903 32.468 6.443 1.00 20.79 ATOM 769 CD PRO B 100 -0.551 31.700 7.568 1.00 19.68 ATOM 770 N GLU B 101 1.915 34.147 8.946 1.00 18.18 ATOM 771 CA GLU B 101 2.568 35.123 9.740 1.00 23.23 ATOM 772 C GLU B 101 4.043 34.786 9.915 1.00 21.47 ATOM 773 O GLU B 101 4.894 35.678 10.025 1.00 19.20 ATOM 774 CB GLU B 101 1.946 35.099 11.202 1.00 21.55 ATOM 775 CG GLU B 101 2.327 36.540 12.008 1.00 20.97 ATOM 776 CD GLU B 101 1.931 37.618 11.400 1.00 22.01 ATOM 777 OE1 GLU B 101 0.648 37.797 10.654 1.00 25.90 ATOM 778 OE2 GLU B 101 2.624 38.565 11.061 1.00 23.56 ATOM 779 N ASN B 102 4.394 33.431 9.799 1.00 18.35 ATOM 780 CA ASN B 102 5.723 33.055 9.849 1.00 15.45 ATOM 781 C ASN B 102 6.635 33.565 8.712 1.00 14.33 ATOM 782 O ASN B 102 7.886 33.653 8.885 1.00 15.51 ATOM 783 CB ASN B 102 5.909 31.525 9.971 1.00 17.26 ATOM 784 CG ASN B 102 5.289 30.963 11.334 1.00 20.75 ATOM 785 OD1 ASN B 102 5.516 31.577 12.353 1.00 24.05 ATOM 786 ND2 ASN B 102 4.515 29.971 11.230 1.00 20.09 ATOM 787 N PHE B 103 6.099 33.856 7.584 1.00 15.58 ATOM 788 CA PHE B 103 6.910 34.264 6.434 1.00 13.23 ATOM 789 C PHE B 103 7.497 35.659 6.738 1.00 13.67 ATOM 790 O PHE B 103 8.553 36.001 6.410 1.00 14.46 ATOM 791 CB PHE B 103 6.102 34.329 5.168 1.00 14.07 ATOM 792 CG PHE B 103 5.547 33.023 4.718 1.00 13.97 ATOM 793 CD1 PHE B 103 6.406 31.937 4.577 1.00 17.27 ATOM 794 CD2 PHE B 103 4.201 32.916 4.389 1.00 14.77 ATOM 795 CE1 PHE B 103 5.884 30.683 4.174 1.00 15.89 ATOM 796 CE2 PHE B 103 3.675 31.683 3.872 1.00 18.89 ATOM 797 CZ PHE B 103 4.525 30.563 3.867 1.00 17.37 ATOM 798 N LYS B 104 6.600 36.481 7.404 1.00 16.35 ATOM 799 CA LYS B 104 7.105 37.878 7.718 1.00 14.67 ATOM 800 C LYS B 104 8.058 37.717 8.897 1.00 16.29 ATOM 801 O LYS B 104 9.095 38.496 8.955 1.00 14.34 ATOM 802 CB LYS B 104 5.855 38.745 8.092 1.00 18.47 ATOM 803 CG LYS B 104 5.837 38.956 9.618 1.00 20.34 ATOM 804 CD LYS B 104 4.876 40.141 9.967 1.00 17.63 ATOM 805 CE LYS B 104 4.883 40.449 11.456 1.00 17.74 ATOM 806 NZ LYS B 104 4.039 41.629 11.789 1.00 17.72 ATOM 807 N LEU B 105 7.855 36.820 9.780 1.00 13.11 ATOM 808 CA LEU B 105 8.742 36.625 10.955 1.00 12.95 ATOM 809 C LEU B 105 10.101 36.252 10.451 1.00 12.19 ATOM 810 O LEU B 105 11.120 36.798 10.974 1.00 13.05 ATOM 811 CB LEU B 105 8.177 35.531 11.847 1.00 16.08 ATOM 812 CG LEU B 105 8.785 35.397 13.121 1.00 16.98 ATOM 813 CD1 LEU B 105 8.801 36.870 13.906 1.00 21.62 ATOM 814 CD2 LEU B 105 7.934 34.444 14.051 1.00 18.16 ATOM 815 N LEU B 106 10.178 35.316 9.490 1.00 9.59 ATOM 816 CA LEU B 106 11.502 34.918 8.960 1.00 9.11 ATOM 817 C LEU B 106 12.143 36.075 8.244 1.00 10.01 ATOM 818 O LEU B 106 13.406 36.303 8.396 1.00 9.08 ATOM 819 CB LEU B 106 11.344 33.710 8.037 1.00 8.60 ATOM 820 CG LEU B 106 12.622 33.222 7.352 1.00 10.63 ATOM 821 CD1 LEU B 106 13.736 32.956 8.375 1.00 12.54 ATOM 822 CD2 LEU B 106 12.290 31.878 6.656 1.00 12.31 ATOM 823 N GLY B 107 11.395 36.832 7.542 1.00 9.39 ATOM 824 CA GLY B 107 11.921 37.986 6.786 1.00 11.41 ATOM 825 C GLY B 107 12.529 38.986 7.779 1.00 12.32 ATOM 826 O GLY B 107 13.645 39.514 7.521 1.00 11.33 ATOM 827 N ASN B 108 11.862 39.229 8.869 1.00 11.98 ATOM 828 CA ASN B 108 12.418 40.177 9.915 1.00 13.02 ATOM 829 C ASN B 108 13.656 39.639 10.572 1.00 11.44 ATOM 830 O ASN B 108 14.467 40.417 11.010 1.00 9.71 ATOM 831 CB ASN B 108 11.327 40.641 10.822 1.00 18.13 ATOM 832 CG ASN B 108 10.333 41.515 9.946 1.00 18.72 ATOM 833 OD1 ASN B 108 10.772 42.461 9.251 1.00 17.91 ATOM 834 ND2 ASN B 108 9.055 41.429 10.285 1.00 19.23 ATOM 835 N VAL B 109 13.796 38.305 10.642 1.00 9.06 ATOM 836 CA VAL B 109 14.983 37.808 11.276 1.00 7.53 ATOM 837 C VAL B 109 16.145 37.944 10.235 1.00 8.14 ATOM 838 O VAL B 109 17.249 38.271 10.626 1.00 8.39 ATOM 839 CB VAL B 109 14.840 36.231 11.553 1.00 8.93 ATOM 840 CG1 VAL B 109 16.249 35.711 11.967 1.00 8.98 ATOM 841 CG2 VAL B 109 13.891 36.066 12.723 1.00 7.38 ATOM 842 N LEU B 110 15.797 37.841 8.951 1.00 8.41 ATOM 843 CA LEU B 110 16.886 38.063 7.935 1.00 8.26 ATOM 844 C LEU B 110 17.347 39.547 8.032 1.00 8.27 ATOM 845 O LEU B 110 18.529 39.803 7.882 1.00 8.36 ATOM 846 CB LEU B 110 16.335 37.812 6.497 1.00 9.42 ATOM 847 CG LEU B 110 17.343 38.115 5.478 1.00 11.43 ATOM 848 CD1 LEU B 110 18.589 37.177 5.566 1.00 10.31 ATOM 849 CD2 LEU B 110 16.727 37.902 4.014 1.00 10.24 ATOM 850 N VAL B 111 16.426 40.441 8.317 1.00 8.39 ATOM 851 CA VAL B 111 16.779 41.851 8.417 1.00 10.05 ATOM 852 C VAL B 111 17.763 41.983 9.639 1.00 10.08 ATOM 853 O VAL B 111 18.795 42.732 9.526 1.00 9.88 ATOM 854 CB VAL B 111 15.578 42.750 8.672 1.00 10.18 ATOM 855 CG1 VAL B 111 15.949 44.177 9.089 1.00 12.09 ATOM 856 CG2 VAL B 111 14.769 42.781 7.281 1.00 10.69 ATOM 857 N THR B 112 17.491 41.312 10.707 1.00 8.40 ATOM 858 CA THR B 112 18.366 41.381 11.941 1.00 8.81 ATOM 859 C THR B 112 19.751 40.845 11.571 1.00 9.30 ATOM 860 O THR B 112 20.771 41.420 11.951 1.00 8.51 ATOM 861 CB THR B 112 17.783 40.547 13.096 1.00 10.05 ATOM 862 OG1 THR B 112 16.495 41.071 13.384 1.00 10.80 ATOM 863 CG2 THR B 112 18.705 40.591 14.233 1.00 10.81 ATOM 864 N VAL B 113 19.797 39.728 10.810 1.00 8.30 ATOM 865 CA VAL B 113 21.067 39.155 10.413 1.00 7.70 ATOM 866 C VAL B 113 21.828 40.097 9.478 1.00 8.23 ATOM 867 O VAL B 113 23.047 40.206 9.597 1.00 9.10 ATOM 868 CB VAL B 113 20.787 37.814 9.682 1.00 7.09 ATOM 869 CG1 VAL B 113 22.051 37.274 9.019 1.00 9.88 ATOM 870 CG2 VAL B 113 20.314 36.773 10.766 1.00 7.84 ATOM 871 N LEU B 114 21.127 40.802 8.550 1.00 8.29 ATOM 872 CA LEU B 114 21.790 41.762 7.743 1.00 8.85 ATOM 873 C LEU B 114 22.316 42.934 8.547 1.00 10.91 ATOM 874 O LEU B 114 23.412 43.462 8.314 1.00 10.92 ATOM 875 CB LEU B 114 20.814 42.312 6.601 1.00 9.10 ATOM 876 CG LEU B 114 20.371 41.256 5.630 1.00 10.47 ATOM 877 CD1 LEU B 114 19.347 41.901 4.655 1.00 10.05 ATOM 878 CD2 LEU B 114 21.559 40.723 4.876 1.00 10.58 ATOM 879 N ALA B 115 21.566 43.347 9.596 1.00 10.27 ATOM 880 CA ALA B 115 22.047 44.449 10.378 1.00 8.74 ATOM 881 C ALA B 115 23.303 44.011 11.155 1.00 11.18 ATOM 882 O ALA B 115 24.211 44.809 11.344 1.00 10.25 ATOM 883 CB ALA B 115 20.873 44.927 11.428 1.00 9.11 ATOM 884 N ILE B 116 23.299 42.794 11.645 1.00 9.72 ATOM 885 CA ILE B 116 24.507 42.286 12.396 1.00 11.37 ATOM 886 C ILE B 116 25.700 42.286 11.494 1.00 10.94 ATOM 887 O ILE B 116 26.763 42.841 11.842 1.00 12.05 ATOM 888 CB ILE B 116 24.233 40.844 12.929 1.00 11.36 ATOM 889 CG1 ILE B 116 23.254 40.859 14.040 1.00 10.63 ATOM 890 CG2 ILE B 116 25.560 40.186 13.225 1.00 11.50 ATOM 891 CD1 ILE B 116 22.822 39.472 14.556 1.00 11.66 ATOM 892 N HIS B 117 25.570 41.728 10.270 1.00 11.74 ATOM 893 CA HIS B 117 26.736 41.638 9.389 1.00 11.49 ATOM 894 C HIS B 117 27.132 42.968 8.734 1.00 12.62 ATOM 895 O HIS B 117 28.360 43.159 8.495 1.00 13.33 ATOM 896 CB HIS B 117 26.467 40.574 8.312 1.00 15.97 ATOM 897 CG HIS B 117 27.369 39.254 8.322 1.00 18.39 ATOM 898 ND1 HIS B 117 28.587 39.411 7.880 1.00 16.00 ATOM 899 CD2 HIS B 117 27.335 38.174 8.959 1.00 17.67 ATOM 900 CE1 HIS B 117 29.266 38.304 8.055 1.00 17.58 ATOM 901 NE2 HIS B 117 28.264 37.421 8.767 1.00 20.47 ATOM 902 N PHE B 118 26.231 43.816 8.389 1.00 12.27 ATOM 903 CA PHE B 118 26.599 45.023 7.682 1.00 13.42 ATOM 904 C PHE B 118 26.671 46.285 8.585 1.00 12.50 ATOM 905 O PHE B 118 27.255 47.342 8.118 1.00 13.48 ATOM 906 CB PHE B 118 25.619 45.283 6.514 1.00 14.16 ATOM 907 CG PHE B 118 25.770 44.180 5.487 1.00 16.32 ATOM 908 CD1 PHE B 118 26.849 44.245 4.545 1.00 18.37 ATOM 909 CD2 PHE B 118 24.845 43.213 5.342 1.00 15.81 ATOM 910 CE1 PHE B 118 26.958 43.307 3.547 1.00 19.60 ATOM 911 CE2 PHE B 118 24.969 42.233 4.439 1.00 19.21 ATOM 912 CZ PHE B 118 26.038 42.188 3.514 1.00 19.93 ATOM 913 N GLY B 119 26.152 46.177 9.753 1.00 12.00 ATOM 914 CA GLY B 119 26.286 47.379 10.714 1.00 12.77 ATOM 915 C GLY B 119 25.812 48.702 10.054 1.00 15.75 ATOM 916 O GLY B 119 24.794 48.862 9.566 1.00 14.71 ATOM 917 N LYS B 120 26.744 49.705 10.282 1.00 16.09 ATOM 918 CA LYS B 120 26.370 51.073 9.860 1.00 18.05 ATOM 919 C LYS B 120 26.019 51.196 8.355 1.00 16.02 ATOM 920 O LYS B 120 25.303 52.130 8.022 1.00 15.10 ATOM 921 CB LYS B 120 27.675 51.947 10.032 1.00 19.45 ATOM 922 CG LYS B 120 28.498 51.551 11.278 1.00 24.23 ATOM 923 CD LYS B 120 29.156 50.116 11.236 1.00 24.85 ATOM 924 CE LYS B 120 29.347 49.475 12.294 1.00 22.91 ATOM 925 NZ LYS B 120 28.063 49.247 13.189 1.00 29.64 ATOM 926 N GLU B 121 26.442 50.203 7.557 1.00 15.78 ATOM 927 CA GLU B 121 26.087 50.223 6.109 1.00 13.49 ATOM 928 C GLU B 121 24.467 50.009 5.993 1.00 13.45 ATOM 929 O GLU B 121 23.948 50.354 4.927 1.00 12.33 ATOM 930 CB GLU B 121 26.752 49.138 5.414 1.00 16.20 ATOM 931 CG GLU B 121 26.778 49.366 3.907 1.00 20.34 ATOM 932 CD GLU B 121 27.463 48.234 3.148 1.00 23.44 ATOM 933 OE1 GLU B 121 28.421 47.577 3.673 1.00 23.30 ATOM 934 OE2 GLU B 121 27.072 47.978 1.988 1.00 24.27 ATOM 935 N PHE B 122 23.915 49.386 6.966 1.00 11.67 ATOM 936 CA PHE B 122 22.478 49.097 6.975 1.00 11.58 ATOM 937 C PHE B 122 21.769 50.347 7.493 1.00 10.95 ATOM 938 O PHE B 122 21.162 50.335 8.573 1.00 10.46 ATOM 939 CB PHE B 122 22.178 47.868 7.898 1.00 12.01 ATOM 940 CG PHE B 122 20.905 47.169 7.513 1.00 9.23 ATOM 941 CD1 PHE B 122 20.808 46.548 6.278 1.00 10.19 ATOM 942 CD2 PHE B 122 19.862 47.173 8.405 1.00 10.25 ATOM 943 CE1 PHE B 122 19.618 45.801 5.999 1.00 10.28 ATOM 944 CE2 PHE B 122 18.663 46.472 8.085 1.00 10.05 ATOM 945 CZ PHE B 122 18.562 45.825 6.850 1.00 9.13 ATOM 946 N THR B 123 21.754 51.351 6.663 1.00 10.42 ATOM 947 CA THR B 123 21.131 52.688 7.055 1.00 10.96 ATOM 948 C THR B 123 19.641 52.556 7.043 1.00 10.76 ATOM 949 O THR B 123 19.064 51.534 6.593 1.00 11.18 ATOM 950 CB THR B 123 21.458 53.767 5.955 1.00 12.34 ATOM 951 OG1 THR B 123 20.987 53.296 4.673 1.00 12.57 ATOM 952 CG2 THR B 123 22.994 53.926 5.845 1.00 15.04 ATOM 953 N PRO B 124 18.919 53.582 7.555 1.00 10.20 ATOM 954 CA PRO B 124 17.468 53.478 7.600 1.00 10.51 ATOM 955 C PRO B 124 16.922 53.261 6.197 1.00 9.90 ATOM 956 O PRO B 124 16.002 52.508 5.992 1.00 9.49 ATOM 957 CB PRO B 124 17.036 54.865 8.145 1.00 11.58 ATOM 958 CG PRO B 124 18.140 55.084 9.194 1.00 9.32 ATOM 959 CD PRO B 124 19.421 54.724 8.368 1.00 12.91 ATOM 960 N GLU B 125 17.535 54.010 5.217 1.00 9.62 ATOM 961 CA GLU B 125 16.991 53.801 3.854 1.00 11.15 ATOM 962 C GLU B 125 17.241 52.381 3.334 1.00 11.23 ATOM 963 O GLU B 125 16.441 51.880 2.564 1.00 10.63 ATOM 964 CB GLU B 125 17.657 54.825 2.876 1.00 12.12 ATOM 965 CG GLU B 125 17.242 56.266 3.316 1.00 16.68 ATOM 966 CD GLU B 125 18.071 57.258 2.534 1.00 18.46 ATOM 967 OE1 GLU B 125 19.274 57.454 2.961 1.00 23.81 ATOM 968 OE2 GLU B 125 17.462 57.885 1.596 1.00 24.17 ATOM 969 N VAL B 126 18.445 51.864 3.632 1.00 8.92 ATOM 970 CA VAL B 126 18.784 50.534 3.178 1.00 10.58 ATOM 971 C VAL B 126 17.769 49.519 3.870 1.00 10.80 ATOM 972 O VAL B 126 17.300 48.633 3.185 1.00 10.56 ATOM 973 CB VAL B 126 20.235 50.152 3.544 1.00 10.49 ATOM 974 CG1 VAL B 126 20.406 48.595 3.458 1.00 9.37 ATOM 975 CG2 VAL B 126 21.139 50.818 2.589 1.00 11.38 ATOM 976 N GLN B 127 17.472 49.791 5.097 1.00 9.47 ATOM 977 CA GLN B 127 16.525 48.879 5.825 1.00 10.30 ATOM 978 C GLN B 127 15.131 49.016 5.241 1.00 11.73 ATOM 979 O GLN B 127 14.441 47.995 5.072 1.00 10.23 ATOM 980 CB GLN B 127 16.484 49.246 7.317 1.00 10.73 ATOM 981 CG GLN B 127 15.641 48.236 8.045 1.00 12.29 ATOM 982 CD GLN B 127 15.412 48.612 9.501 1.00 13.15 ATOM 983 OE1 GLN B 127 16.046 49.382 10.079 1.00 12.61 ATOM 984 NE2 GLN B 127 14.358 47.856 10.050 1.00 16.22 ATOM 985 N ALA B 128 14.784 50.204 4.801 1.00 10.01 ATOM 986 CA ALA B 128 13.454 50.384 4.176 1.00 9.24 ATOM 987 C ALA B 128 13.303 49.551 2.980 1.00 11.29 ATOM 988 O ALA B 128 12.257 48.935 2.752 1.00 11.41 ATOM 989 CB ALA B 128 13.265 51.945 3.845 1.00 11.93 ATOM 990 N SER B 129 14.370 49.522 2.109 1.00 10.04 ATOM 991 CA SER B 129 14.298 48.718 0.891 1.00 11.36 ATOM 992 C SER B 129 14.165 47.246 1.261 1.00 9.44 ATOM 993 O SER B 129 13.374 46.530 0.629 1.00 10.37 ATOM 994 CB SER B 129 15.580 48.879 0.069 1.00 8.85 ATOM 995 OG SER B 129 15.719 50.290 -0.336 1.00 13.43 ATOM 996 N TRP B 130 14.908 46.800 2.276 1.00 10.68 ATOM 997 CA TRP B 130 14.807 45.405 2.682 1.00 8.34 ATOM 998 C TRP B 130 13.496 45.007 3.370 1.00 10.80 ATOM 999 O TRP B 130 13.114 43.868 3.281 1.00 11.35 ATOM 1000 CB TRP B 130 16.040 45.005 3.553 1.00 12.13 ATOM 1001 CG TRP B 130 17.182 44.635 2.667 1.00 8.88 ATOM 1002 CD1 TRP B 130 18.182 45.467 2.256 1.00 10.99 ATOM 1003 CD2 TRP B 130 17.397 43.386 2.001 1.00 11.17 ATOM 1004 NE1 TRP B 130 18.994 44.802 1.371 1.00 9.76 ATOM 1005 CE2 TRP B 130 18.504 43.525 1.201 1.00 9.95 ATOM 1006 CE3 TRP B 130 16.708 42.169 2.005 1.00 9.91 ATOM 1007 CZ2 TRP B 130 19.017 42.505 0.427 1.00 10.51 ATOM 1008 CZ3 TRP B 130 17.205 41.122 1.219 1.00 10.41 ATOM 1009 CH2 TRP B 130 18.353 41.288 0.438 1.00 10.73 ATOM 1010 N GLN B 131 12.867 45.988 4.014 1.00 10.69 ATOM 1011 CA GLN B 131 11.538 45.751 4.612 1.00 12.24 ATOM 1012 C GLN B 131 10.516 45.579 3.550 1.00 14.23 ATOM 1013 O GLN B 131 9.599 44.749 3.651 1.00 12.63 ATOM 1014 CB GLN B 131 11.127 46.910 5.489 1.00 12.52 ATOM 1015 CG GLN B 131 11.827 47.032 6.772 1.00 12.01 ATOM 1016 CD GLN B 131 11.758 45.763 7.706 1.00 14.59 ATOM 1017 OE1 GLN B 131 10.809 44.964 7.570 1.00 13.35 ATOM 1018 NE2 GLN B 131 12.708 45.650 8.607 1.00 11.36 ATOM 1019 N LYS B 132 10.711 46.275 2.452 1.00 11.42 ATOM 1020 CA LYS B 132 9.805 46.151 1.305 1.00 13.78 ATOM 1021 C LYS B 132 10.064 44.746 0.751 1.00 13.88 ATOM 1022 O LYS B 132 9.053 44.078 0.358 1.00 12.75 ATOM 1023 CB LYS B 132 10.175 47.182 0.250 1.00 13.81 ATOM 1024 CG LYS B 132 9.195 47.200 -0.916 1.00 14.52 ATOM 1025 CD LYS B 132 9.544 48.357 -1.938 1.00 17.51 ATOM 1026 CE LYS B 132 9.164 49.743 -1.317 1.00 16.14 ATOM 1027 NZ LYS B 132 9.486 50.822 -2.322 1.00 18.77 ATOM 1028 N MET B 133 11.207 44.284 0.708 1.00 12.21 ATOM 1029 CA MET B 133 11.533 42.954 0.159 1.00 12.73 ATOM 1030 C MET B 133 10.861 41.903 1.080 1.00 13.05 ATOM 1031 O MET B 133 10.240 40.975 0.595 1.00 13.39 ATOM 1032 CB MET B 133 13.058 42.694 0.118 1.00 11.03 ATOM 1033 CG MET B 133 13.403 41.321 -0.362 1.00 14.86 ATOM 1034 SD MET B 133 12.973 41.276 -2.157 1.00 14.59 ATOM 1035 CE MET B 133 13.461 39.594 -2.517 1.00 15.33 ATOM 1036 N VAL B 134 11.054 42.024 2.414 1.00 13.79 ATOM 1037 CA VAL B 134 10.437 41.096 3.384 1.00 15.40 ATOM 1038 C VAL B 134 8.952 40.966 3.158 1.00 15.03 ATOM 1039 O VAL B 134 8.435 39.856 3.027 1.00 16.93 ATOM 1040 CB VAL B 134 10.611 41.616 4.848 1.00 17.40 ATOM 1041 CG1 VAL B 134 9.759 40.783 5.806 1.00 19.32 ATOM 1042 CG2 VAL B 134 12.017 41.540 5.263 1.00 17.24 ATOM 1043 N THR B 135 8.272 42.086 3.037 1.00 15.10 ATOM 1044 CA THR B 135 6.802 42.111 2.798 1.00 16.12 ATOM 1045 C THR B 135 6.464 41.430 1.513 1.00 14.64 ATOM 1046 O THR B 135 5.509 40.652 1.451 1.00 14.46 ATOM 1047 CB THR B 135 6.294 43.505 2.794 1.00 16.79 ATOM 1048 OG1 THR B 135 6.430 44.084 4.124 1.00 19.21 ATOM 1049 CG2 THR B 135 4.781 43.510 2.450 1.00 16.59 ATOM 1050 N ALA B 136 7.199 41.767 0.425 1.00 12.10 ATOM 1051 CA ALA B 136 6.902 41.216 -0.851 1.00 13.61 ATOM 1052 C ALA B 136 7.076 39.677 -0.909 1.00 12.95 ATOM 1053 O ALA B 136 6.331 38.982 -1.557 1.00 12.40 ATOM 1054 CB ALA B 136 7.781 41.891 -1.907 1.00 13.41 ATOM 1055 N VAL B 137 8.142 39.220 -0.232 1.00 13.73 ATOM 1056 CA VAL B 137 8.411 37.750 -0.230 1.00 12.35 ATOM 1057 C VAL B 137 7.241 37.063 0.552 1.00 13.05 ATOM 1058 O VAL B 137 6.791 35.973 0.128 1.00 14.08 ATOM 1059 CB VAL B 137 9.784 37.460 0.407 1.00 13.21 ATOM 1060 CG1 VAL B 137 9.932 35.946 0.607 1.00 13.34 ATOM 1061 CG2 VAL B 137 10.909 37.960 -0.517 1.00 14.05 ATOM 1062 N ALA B 138 6.916 37.615 1.692 1.00 13.71 ATOM 1063 CA ALA B 138 5.850 37.026 2.548 1.00 12.97 ATOM 1064 C ALA B 138 4.548 36.946 1.749 1.00 14.04 ATOM 1065 O ALA B 138 3.797 35.966 1.835 1.00 13.58 ATOM 1066 CB ALA B 138 5.659 37.829 3.802 1.00 13.30 ATOM 1067 N SER B 139 4.280 37.988 0.979 1.00 12.84 ATOM 1068 CA SER B 139 3.013 38.001 0.185 1.00 15.26 ATOM 1069 C SER B 139 3.036 36.962 -0.874 1.00 13.72 ATOM 1070 O SER B 139 2.047 36.247 -1.127 1.00 13.81 ATOM 1071 CB SER B 139 2.817 39.368 -0.394 1.00 14.48 ATOM 1072 OG SER B 139 1.704 39.385 -1.343 1.00 19.47 ATOM 1073 N ALA B 140 4.195 36.824 -1.568 1.00 13.24 ATOM 1074 CA ALA B 140 4.317 35.836 -2.625 1.00 14.04 ATOM 1075 C ALA B 140 4.213 34.436 -2.148 1.00 12.93 ATOM 1076 O ALA B 140 3.622 33.568 -2.777 1.00 13.60 ATOM 1077 CB ALA B 140 5.660 36.083 -3.376 1.00 13.83 ATOM 1078 N LEU B 141 4.803 34.140 -0.925 1.00 13.36 ATOM 1079 CA LEU B 141 4.813 32.802 -0.424 1.00 13.33 ATOM 1080 C LEU B 141 3.392 32.418 0.190 1.00 14.06 ATOM 1081 O LEU B 141 3.089 31.249 0.245 1.00 13.85 ATOM 1082 CB LEU B 141 5.860 32.620 0.627 1.00 13.19 ATOM 1083 CG LEU B 141 7.234 32.471 0.055 1.00 15.25 ATOM 1084 CD1 LEU B 141 8.157 32.412 1.187 1.00 17.18 ATOM 1085 CD2 LEU B 141 7.370 31.095 -0.799 1.00 16.30 ATOM 1086 N SER B 142 2.705 33.409 0.615 1.00 13.81 ATOM 1087 CA SER B 142 1.293 33.144 1.241 1.00 13.63 ATOM 1088 C SER B 142 0.302 33.254 0.179 1.00 15.34 ATOM 1089 O SER B 142 -0.901 33.142 0.525 1.00 15.93 ATOM 1090 CB SER B 142 1.127 34.137 2.426 1.00 15.25 ATOM 1091 OG SER B 142 1.023 35.453 1.875 1.00 15.10 ATOM 1092 N SER B 143 0.686 33.488 -1.038 1.00 13.68 ATOM 1093 CA SER B 143 -0.392 33.717 -2.103 1.00 16.63 ATOM 1094 C SER B 143 -1.392 32.662 -2.125 1.00 17.14 ATOM 1095 O SER B 143 -2.639 32.967 -2.305 1.00 17.46 ATOM 1096 CB SER B 143 0.364 33.733 -3.476 1.00 17.41 ATOM 1097 OG SER B 143 -0.516 34.210 -4.450 1.00 20.06 ATOM 1098 N ARG B 144 -1.055 31.368 -1.988 1.00 17.37 ATOM 1099 CA ARG B 144 -2.003 30.290 -2.050 1.00 16.56 ATOM 1100 C ARG B 144 -3.103 30.336 -0.893 1.00 18.55 ATOM 1101 O ARG B 144 -4.161 29.727 -1.093 1.00 19.53 ATOM 1102 CB ARG B 144 -1.246 28.908 -1.868 1.00 20.95 ATOM 1103 CG ARG B 144 -0.685 28.451 -3.212 1.00 20.37 ATOM 1104 CD ARG B 144 -1.849 27.970 -4.282 1.00 25.29 ATOM 1105 NE ARG B 144 -2.668 27.005 -3.572 1.00 30.00 ATOM 1106 CZ ARG B 144 -3.915 26.739 -3.891 1.00 31.22 ATOM 1107 NH1 ARG B 144 -4.656 25.862 -3.105 1.00 29.96 ATOM 1108 NH2 ARG B 144 -4.526 27.422 -4.957 1.00 35.02 ATOM 1109 N TYR B 145 -2.879 31.119 0.093 1.00 16.24 ATOM 1110 CA TYR B 145 -3.794 31.285 1.167 1.00 18.65 ATOM 1111 C TYR B 145 -4.744 32.439 0.818 1.00 21.67 ATOM 1112 O TYR B 145 -5.836 32.603 1.473 1.00 19.99 ATOM 1113 CB TYR B 145 -3.214 31.589 2.487 1.00 16.58 ATOM 1114 CG TYR B 145 -2.529 30.513 3.153 1.00 18.07 ATOM 1115 CD1 TYR B 145 -3.161 29.262 3.437 1.00 14.52 ATOM 1116 CD2 TYR B 145 -1.168 30.632 3.698 1.00 18.11 ATOM 1117 CE1 TYR B 145 -2.575 28.248 4.048 1.00 20.05 ATOM 1118 CE2 TYR B 145 -0.589 29.715 4.387 1.00 16.46 ATOM 1119 CZ TYR B 145 -1.246 28.386 4.664 1.00 17.73 ATOM 1120 OH TYR B 145 -0.646 27.437 5.275 1.00 16.60 ATOM 1121 N HIS B 146 -4.398 33.186 -0.137 1.00 19.62 ATOM 1122 CA HIS B 146 -5.146 34.437 -0.507 1.00 20.40 ATOM 1123 C HIS B 146 -5.581 34.318 -2.029 1.00 19.49 ATOM 1124 O HIS B 146 -6.181 35.623 -2.055 1.00 21.41 ATOM 1125 CB HIS B 146 -4.196 35.666 -0.279 1.00 19.32 ATOM 1126 CG HIS B 146 -3.591 35.707 1.014 1.00 20.83 ATOM 1127 ND1 HIS B 146 -2.195 36.114 1.184 1.00 19.57 ATOM 1128 CD2 HIS B 146 -3.989 35.407 2.273 1.00 18.56 ATOM 1129 CE1 HIS B 146 -1.855 36.056 2.458 1.00 20.70 ATOM 1130 NE2 HIS B 146 -2.982 35.607 3.212 1.00 22.63 ATOM 1131 OXT HIS B 146 -6.255 33.534 -2.457 1.00 20.93 HETATM 1132 FE HEM B 147 10.365 26.962 3.785 1.00 12.03 HETATM 1133 CHA HEM B 147 10.884 23.726 2.809 1.00 15.05 HETATM 1134 CHB HEM B 147 12.012 28.101 1.010 1.00 12.19 HETATM 1135 CHC HEM B 147 9.818 30.208 4.816 1.00 12.37 HETATM 1136 CHD HEM B 147 8.818 25.829 6.663 1.00 14.29 HETATM 1137 N A HEM B 147 11.300 26.098 2.253 1.00 11.40 HETATM 1138 C1A HEM B 147 11.376 24.759 2.022 1.00 13.84 HETATM 1139 C2A HEM B 147 12.174 24.540 0.779 1.00 13.41 HETATM 1140 C3A HEM B 147 12.457 25.762 0.278 1.00 13.48 HETATM 1141 C4A HEM B 147 11.974 26.728 1.175 1.00 11.92 HETATM 1142 CMA HEM B 147 13.309 26.048 -1.016 1.00 12.40 HETATM 1143 CAA HEM B 147 12.650 23.204 0.158 1.00 16.60 HETATM 1144 CBA HEM B 147 11.682 22.553 -0.728 1.00 21.44 HETATM 1145 CGA HEM B 147 12.505 21.301 -1.465 1.00 21.04 HETATM 1146 O1A HEM B 147 12.035 20.812 -2.473 1.00 26.42 HETATM 1147 O2A HEM B 147 13.506 20.876 -0.824 1.00 25.94 HETATM 1148 N B HEM B 147 10.822 28.748 3.081 1.00 11.40 HETATM 1149 C1B HEM B 147 11.498 29.048 1.885 1.00 11.23 HETATM 1150 C2B HEM B 147 11.596 30.449 1.671 1.00 11.50 HETATM 1151 C3B HEM B 147 11.031 31.048 2.777 1.00 12.01 HETATM 1152 C4B HEM B 147 10.501 29.982 3.581 1.00 12.30 HETATM 1153 CMB HEM B 147 12.372 31.090 0.439 1.00 11.98 HETATM 1154 CAB HEM B 147 10.833 32.536 3.036 1.00 13.75 HETATM 1155 CBB HEM B 147 12.009 33.477 2.936 1.00 13.52 HETATM 1156 N C HEM B 147 9.521 27.837 5.368 1.00 11.64 HETATM 1157 C1C HEM B 147 9.369 29.196 5.582 1.00 11.82 HETATM 1158 C2C HEM B 147 8.717 29.455 6.904 1.00 12.37 HETATM 1159 C3C HEM B 147 8.423 28.228 7.360 1.00 14.53 HETATM 1160 C4C HEM B 147 8.911 27.236 6.462 1.00 13.18 HETATM 1161 CMC HEM B 147 8.413 30.793 7.509 1.00 15.93 HETATM 1162 CAC HEM B 147 7.767 27.921 8.740 1.00 14.80 HETATM 1163 CBC HEM B 147 8.086 28.687 9.887 1.00 14.95 HETATM 1164 N D HEM B 147 9.939 25.194 4.552 1.00 13.19 HETATM 1165 C1D HEM B 147 9.277 24.895 5.803 1.00 14.50 HETATM 1166 C2D HEM B 147 9.189 23.447 5.978 1.00 15.61 HETATM 1167 C3D HEM B 147 9.769 22.882 4.916 1.00 14.27 HETATM 1168 C4D HEM B 147 10.224 23.929 4.039 1.00 14.39 HETATM 1169 CMD HEM B 147 8.504 22.760 7.197 1.00 16.08 HETATM 1170 CAD HEM B 147 9.972 21.310 4.614 1.00 16.54 HETATM 1171 CBD HEM B 147 11.299 20.946 5.099 1.00 19.12 HETATM 1172 CGD HEM B 147 11.526 19.353 5.368 1.00 20.39 HETATM 1173 O1D HEM B 147 12.218 18.955 6.283 1.00 23.02 HETATM 1174 O2D HEM B 147 10.954 18.614 4.660 1.00 25.23 HETATM 1175 C CMO B 148 12.131 27.157 5.187 1.00 14.53 HETATM 1176 O CMO B 148 12.503 28.052 6.233 1.00 19.63 TER 1177 CMO B 148 END