ATOM 1 N ALA A 2 33.763 52.112 -44.090 1.00 25.34 ATOM 2 CA ALA A 2 33.403 52.722 -42.739 1.00 25.11 ATOM 3 C ALA A 2 31.960 53.249 -42.614 1.00 24.76 ATOM 4 O ALA A 2 31.694 54.512 -42.582 1.00 23.96 ATOM 5 CB ALA A 2 34.416 53.856 -42.420 1.00 25.90 ATOM 6 N ALA A 3 31.006 52.310 -42.598 1.00 22.94 ATOM 7 CA ALA A 3 29.599 52.628 -42.417 1.00 20.08 ATOM 8 C ALA A 3 29.149 54.015 -41.825 1.00 19.99 ATOM 9 O ALA A 3 28.776 54.906 -42.573 1.00 20.00 ATOM 10 CB ALA A 3 28.955 51.482 -41.644 1.00 23.26 ATOM 11 N VAL A 4 29.035 54.170 -40.506 1.00 18.40 ATOM 12 CA VAL A 4 28.549 55.423 -39.964 1.00 18.10 ATOM 13 C VAL A 4 29.576 56.081 -38.981 1.00 20.17 ATOM 14 O VAL A 4 30.137 55.401 -38.110 1.00 23.21 ATOM 15 CB VAL A 4 27.169 55.298 -39.311 1.00 17.65 ATOM 16 CG1 VAL A 4 26.698 56.664 -38.801 1.00 15.66 ATOM 17 CG2 VAL A 4 26.087 54.720 -40.311 1.00 13.28 ATOM 18 N THR A 5 29.873 57.358 -39.124 1.00 20.40 ATOM 19 CA THR A 5 30.874 57.978 -38.197 1.00 20.85 ATOM 20 C THR A 5 30.306 59.193 -37.579 1.00 20.88 ATOM 21 O THR A 5 29.679 59.984 -38.291 1.00 23.01 ATOM 22 CB THR A 5 32.105 58.415 -38.935 1.00 19.13 ATOM 23 OG1 THR A 5 31.701 59.319 -39.976 1.00 20.17 ATOM 24 CG2 THR A 5 32.793 57.235 -39.515 1.00 19.09 ATOM 25 N GLN A 6 30.516 59.359 -36.266 1.00 22.20 ATOM 26 CA GLN A 6 30.067 60.585 -35.579 1.00 23.92 ATOM 27 C GLN A 6 31.183 61.576 -35.350 1.00 24.16 ATOM 28 O GLN A 6 32.319 61.255 -35.567 1.00 24.44 ATOM 29 CB GLN A 6 29.374 60.216 -34.293 1.00 24.31 ATOM 30 CG GLN A 6 28.414 59.048 -34.567 1.00 26.83 ATOM 31 CD GLN A 6 27.650 58.653 -33.341 1.00 33.51 ATOM 32 OE1 GLN A 6 27.159 57.489 -33.222 1.00 29.01 ATOM 33 NE2 GLN A 6 27.551 59.606 -32.387 1.00 30.50 ATOM 34 N SER A 7 30.858 62.793 -34.915 1.00 24.73 ATOM 35 CA SER A 7 31.873 63.763 -34.592 1.00 24.61 ATOM 36 C SER A 7 31.252 64.844 -33.743 1.00 22.89 ATOM 37 O SER A 7 30.226 65.374 -34.175 1.00 23.88 ATOM 38 CB SER A 7 32.492 64.358 -35.868 1.00 24.52 ATOM 39 OG SER A 7 32.873 65.718 -35.598 1.00 29.35 ATOM 40 N PRO A 8 31.876 65.196 -32.575 1.00 21.61 ATOM 41 CA PRO A 8 33.116 64.595 -32.127 1.00 23.90 ATOM 42 C PRO A 8 32.855 63.370 -31.324 1.00 25.23 ATOM 43 O PRO A 8 31.723 63.054 -31.034 1.00 26.87 ATOM 44 CB PRO A 8 33.746 65.663 -31.273 1.00 21.34 ATOM 45 CG PRO A 8 32.608 66.338 -30.689 1.00 20.62 ATOM 46 CD PRO A 8 31.440 66.196 -31.594 1.00 21.05 ATOM 47 N ARG A 9 33.912 62.635 -31.030 1.00 30.32 ATOM 48 CA ARG A 9 33.769 61.344 -30.318 1.00 32.66 ATOM 49 C ARG A 9 33.547 61.556 -28.814 1.00 34.51 ATOM 50 O ARG A 9 32.676 60.886 -28.211 1.00 34.65 ATOM 51 CB ARG A 9 34.960 60.411 -30.594 1.00 33.97 ATOM 52 CG ARG A 9 34.579 58.965 -31.203 1.00 37.59 ATOM 53 CD ARG A 9 34.574 57.847 -30.146 1.00 41.10 ATOM 54 NE ARG A 9 33.525 57.998 -29.122 1.00 41.96 ATOM 55 CZ ARG A 9 33.148 57.018 -28.288 1.00 46.33 ATOM 56 NH1 ARG A 9 33.734 55.823 -28.351 1.00 46.04 ATOM 57 NH2 ARG A 9 32.191 57.226 -27.381 1.00 45.03 ATOM 58 N ASN A 10 34.255 62.538 -28.252 1.00 34.63 ATOM 59 CA ASN A 10 34.322 62.770 -26.841 1.00 36.87 ATOM 60 C ASN A 10 34.176 64.301 -26.619 1.00 37.49 ATOM 61 O ASN A 10 34.952 65.100 -27.222 1.00 37.87 ATOM 62 CB ASN A 10 35.728 62.350 -26.344 1.00 38.51 ATOM 63 CG ASN A 10 35.808 60.909 -25.778 1.00 40.50 ATOM 64 OD1 ASN A 10 35.289 60.621 -24.690 1.00 42.89 ATOM 65 ND2 ASN A 10 36.562 60.024 -26.478 1.00 45.07 ATOM 66 N LYS A 11 33.234 64.711 -25.756 1.00 37.13 ATOM 67 CA LYS A 11 32.988 66.146 -25.513 1.00 37.05 ATOM 68 C LYS A 11 32.611 66.551 -24.094 1.00 37.79 ATOM 69 O LYS A 11 31.611 66.081 -23.547 1.00 38.26 ATOM 70 CB LYS A 11 31.917 66.640 -26.461 1.00 36.57 ATOM 71 CG LYS A 11 31.671 68.085 -26.434 1.00 34.46 ATOM 72 CD LYS A 11 32.930 68.874 -26.804 1.00 34.83 ATOM 73 CE LYS A 11 32.640 70.397 -26.761 1.00 30.64 ATOM 74 NZ LYS A 11 31.514 70.805 -27.599 1.00 22.67 ATOM 75 N VAL A 12 33.386 67.505 -23.554 1.00 38.60 ATOM 76 CA VAL A 12 33.166 68.115 -22.222 1.00 38.63 ATOM 77 C VAL A 12 32.833 69.600 -22.304 1.00 37.84 ATOM 78 O VAL A 12 33.705 70.410 -22.575 1.00 37.68 ATOM 79 CB VAL A 12 34.436 68.044 -21.367 1.00 38.68 ATOM 80 CG1 VAL A 12 34.455 66.783 -20.594 1.00 36.81 ATOM 81 CG2 VAL A 12 35.698 68.267 -22.244 1.00 39.25 ATOM 82 N ALA A 13 31.582 69.958 -22.048 1.00 38.24 ATOM 83 CA ALA A 13 31.154 71.334 -22.244 1.00 37.91 ATOM 84 C ALA A 13 30.518 71.865 -20.969 1.00 38.80 ATOM 85 O ALA A 13 29.977 71.078 -20.172 1.00 40.28 ATOM 86 CB ALA A 13 30.206 71.429 -23.445 1.00 36.72 ATOM 87 N VAL A 14 30.572 73.184 -20.774 1.00 38.57 ATOM 88 CA VAL A 14 30.029 73.826 -19.562 1.00 37.61 ATOM 89 C VAL A 14 28.509 74.033 -19.608 1.00 37.37 ATOM 90 O VAL A 14 27.928 74.222 -20.657 1.00 37.41 ATOM 91 CB VAL A 14 30.786 75.122 -19.224 1.00 37.15 ATOM 92 CG1 VAL A 14 32.258 74.813 -18.990 1.00 39.31 ATOM 93 CG2 VAL A 14 30.659 76.145 -20.333 1.00 36.96 ATOM 94 N THR A 15 27.833 73.972 -18.484 1.00 37.50 ATOM 95 CA THR A 15 26.374 74.084 -18.570 1.00 38.08 ATOM 96 C THR A 15 26.081 75.446 -19.119 1.00 38.88 ATOM 97 O THR A 15 26.546 76.448 -18.589 1.00 38.13 ATOM 98 CB THR A 15 25.740 73.917 -17.219 1.00 38.28 ATOM 99 OG1 THR A 15 26.179 72.659 -16.708 1.00 37.16 ATOM 100 CG2 THR A 15 24.211 73.945 -17.270 1.00 33.98 ATOM 101 N GLY A 16 25.378 75.454 -20.243 1.00 40.38 ATOM 102 CA GLY A 16 25.006 76.708 -20.944 1.00 40.95 ATOM 103 C GLY A 16 25.235 76.682 -22.453 1.00 41.28 ATOM 104 O GLY A 16 24.284 76.759 -23.237 1.00 41.72 ATOM 105 N GLU A 17 26.507 76.545 -22.845 1.00 40.82 ATOM 106 CA GLU A 17 26.917 76.561 -24.222 1.00 39.97 ATOM 107 C GLU A 17 26.090 75.713 -25.162 1.00 39.45 ATOM 108 O GLU A 17 25.424 74.709 -24.773 1.00 41.25 ATOM 109 CB GLU A 17 28.383 76.194 -24.313 1.00 39.94 ATOM 110 CG GLU A 17 28.705 74.768 -24.699 1.00 42.31 ATOM 111 CD GLU A 17 30.173 74.663 -25.044 1.00 46.41 ATOM 112 OE1 GLU A 17 30.997 74.973 -24.160 1.00 50.97 ATOM 113 OE2 GLU A 17 30.528 74.333 -26.192 1.00 47.31 ATOM 114 N LYS A 18 26.162 76.106 -26.423 1.00 38.14 ATOM 115 CA LYS A 18 25.390 75.490 -27.489 1.00 36.59 ATOM 116 C LYS A 18 26.189 74.336 -28.077 1.00 35.70 ATOM 117 O LYS A 18 27.186 74.553 -28.726 1.00 35.80 ATOM 118 CB LYS A 18 25.078 76.547 -28.555 1.00 35.73 ATOM 119 CG LYS A 18 24.642 75.967 -29.873 1.00 35.86 ATOM 120 CD LYS A 18 24.304 77.030 -30.889 1.00 32.18 ATOM 121 CE LYS A 18 23.847 76.454 -32.203 1.00 30.56 ATOM 122 NZ LYS A 18 23.525 77.616 -33.110 1.00 28.09 ATOM 123 N VAL A 19 25.740 73.104 -27.883 1.00 34.54 ATOM 124 CA VAL A 19 26.489 72.024 -28.480 1.00 33.14 ATOM 125 C VAL A 19 25.814 71.336 -29.702 1.00 31.93 ATOM 126 O VAL A 19 24.659 70.939 -29.621 1.00 30.42 ATOM 127 CB VAL A 19 26.948 71.030 -27.399 1.00 32.22 ATOM 128 CG1 VAL A 19 27.930 70.120 -27.985 1.00 33.61 ATOM 129 CG2 VAL A 19 27.634 71.795 -26.270 1.00 32.41 ATOM 130 N THR A 20 26.586 71.154 -30.793 1.00 30.75 ATOM 131 CA THR A 20 26.129 70.433 -32.017 1.00 30.63 ATOM 132 C THR A 20 26.803 69.064 -32.325 1.00 29.61 ATOM 133 O THR A 20 28.002 68.986 -32.412 1.00 28.29 ATOM 134 CB THR A 20 26.358 71.321 -33.227 1.00 30.22 ATOM 135 OG1 THR A 20 26.098 72.665 -32.851 1.00 33.58 ATOM 136 CG2 THR A 20 25.454 70.942 -34.404 1.00 33.21 ATOM 137 N LEU A 21 26.040 67.994 -32.533 1.00 29.29 ATOM 138 CA LEU A 21 26.700 66.703 -32.864 1.00 27.84 ATOM 139 C LEU A 21 26.557 66.244 -34.315 1.00 27.04 ATOM 140 O LEU A 21 25.477 65.992 -34.733 1.00 27.86 ATOM 141 CB LEU A 21 26.195 65.601 -31.949 1.00 27.07 ATOM 142 CG LEU A 21 26.733 65.616 -30.538 1.00 26.22 ATOM 143 CD1 LEU A 21 26.467 64.263 -30.005 1.00 22.98 ATOM 144 CD2 LEU A 21 28.210 65.836 -30.545 1.00 24.93 ATOM 145 N SER A 22 27.666 66.097 -35.041 1.00 26.93 ATOM 146 CA SER A 22 27.686 65.831 -36.452 1.00 25.10 ATOM 147 C SER A 22 27.878 64.323 -36.752 1.00 25.45 ATOM 148 O SER A 22 28.824 63.705 -36.279 1.00 25.57 ATOM 149 CB SER A 22 28.845 66.590 -37.029 1.00 25.68 ATOM 150 OG SER A 22 30.064 66.188 -36.403 1.00 23.64 ATOM 151 N CYS A 23 26.991 63.763 -37.572 1.00 24.02 ATOM 152 CA CYS A 23 27.004 62.372 -37.923 1.00 22.83 ATOM 153 C CYS A 23 26.979 62.271 -39.446 1.00 23.31 ATOM 154 O CYS A 23 26.279 63.033 -40.098 1.00 23.51 ATOM 155 CB CYS A 23 25.766 61.690 -37.327 1.00 21.98 ATOM 156 SG CYS A 23 25.500 60.064 -38.017 1.00 27.28 ATOM 157 N GLN A 24 27.724 61.334 -40.069 1.00 24.11 ATOM 158 CA GLN A 24 27.667 61.306 -41.533 1.00 22.59 ATOM 159 C GLN A 24 27.779 59.925 -42.002 1.00 21.63 ATOM 160 O GLN A 24 28.489 59.172 -41.354 1.00 24.40 ATOM 161 CB GLN A 24 28.770 62.176 -42.143 1.00 21.88 ATOM 162 CG GLN A 24 30.159 61.762 -41.757 1.00 21.77 ATOM 163 CD GLN A 24 31.178 62.618 -42.429 1.00 26.24 ATOM 164 OE1 GLN A 24 31.091 63.863 -42.343 1.00 29.92 ATOM 165 NE2 GLN A 24 32.140 61.991 -43.145 1.00 24.42 ATOM 166 N GLN A 25 27.160 59.595 -43.134 1.00 20.02 ATOM 167 CA GLN A 25 27.124 58.224 -43.673 1.00 21.13 ATOM 168 C GLN A 25 27.819 58.088 -45.004 1.00 20.72 ATOM 169 O GLN A 25 28.362 59.074 -45.564 1.00 22.35 ATOM 170 CB GLN A 25 25.756 57.546 -43.767 1.00 19.39 ATOM 171 CG GLN A 25 24.519 58.524 -43.955 1.00 20.36 ATOM 172 CD GLN A 25 23.359 57.917 -44.753 1.00 23.09 ATOM 173 OE1 GLN A 25 22.679 56.907 -44.328 1.00 19.57 ATOM 174 NE2 GLN A 25 23.099 58.545 -45.937 1.00 16.66 ATOM 175 N THR A 26 27.877 56.829 -45.457 1.00 18.37 ATOM 176 CA THR A 26 28.528 56.500 -46.708 1.00 16.35 ATOM 177 C THR A 26 27.721 55.440 -47.431 1.00 17.39 ATOM 178 O THR A 26 27.938 55.242 -48.615 1.00 17.50 ATOM 179 CB THR A 26 29.959 56.011 -46.482 1.00 16.16 ATOM 180 OG1 THR A 26 29.910 54.845 -45.647 1.00 11.99 ATOM 181 CG2 THR A 26 30.757 57.080 -45.751 1.00 13.64 ATOM 182 N ASN A 27 26.734 54.815 -46.773 1.00 17.97 ATOM 183 CA ASN A 27 25.938 53.826 -47.485 1.00 18.36 ATOM 184 C ASN A 27 24.715 54.509 -47.983 1.00 18.04 ATOM 185 O ASN A 27 23.783 53.876 -48.453 1.00 18.57 ATOM 186 CB ASN A 27 25.558 52.683 -46.505 1.00 20.73 ATOM 187 CG ASN A 27 25.725 51.289 -47.098 1.00 24.04 ATOM 188 OD1 ASN A 27 26.831 50.715 -47.091 1.00 29.48 ATOM 189 ND2 ASN A 27 24.608 50.706 -47.571 1.00 30.58 ATOM 190 N ASN A 28 24.671 55.826 -47.792 1.00 20.40 ATOM 191 CA ASN A 28 23.537 56.642 -48.189 1.00 19.02 ATOM 192 C ASN A 28 22.188 55.904 -47.921 1.00 19.71 ATOM 193 O ASN A 28 21.534 55.410 -48.886 1.00 19.66 ATOM 194 CB ASN A 28 23.680 56.862 -49.657 1.00 20.31 ATOM 195 CG ASN A 28 24.155 58.217 -50.032 1.00 20.99 ATOM 196 OD1 ASN A 28 23.445 59.211 -49.917 1.00 27.80 ATOM 197 ND2 ASN A 28 25.368 58.270 -50.570 1.00 24.27 ATOM 198 N HIS A 29 21.795 55.744 -46.648 1.00 18.69 ATOM 199 CA HIS A 29 20.457 55.153 -46.346 1.00 18.06 ATOM 200 C HIS A 29 19.444 56.308 -46.121 1.00 16.73 ATOM 201 O HIS A 29 19.811 57.331 -45.565 1.00 20.04 ATOM 202 CB HIS A 29 20.507 54.337 -45.095 1.00 17.41 ATOM 203 CG HIS A 29 21.021 52.959 -45.269 1.00 19.31 ATOM 204 ND1 HIS A 29 20.203 51.888 -45.553 1.00 16.65 ATOM 205 CD2 HIS A 29 22.258 52.452 -45.058 1.00 21.43 ATOM 206 CE1 HIS A 29 20.941 50.796 -45.604 1.00 25.33 ATOM 207 NE2 HIS A 29 22.191 51.109 -45.304 1.00 22.12 ATOM 208 N ASN A 30 18.211 56.170 -46.565 1.00 16.43 ATOM 209 CA ASN A 30 17.159 57.197 -46.310 1.00 17.97 ATOM 210 C ASN A 30 17.031 57.559 -44.839 1.00 16.70 ATOM 211 O ASN A 30 17.239 58.757 -44.450 1.00 17.12 ATOM 212 CB ASN A 30 15.761 56.739 -46.736 1.00 17.02 ATOM 213 CG ASN A 30 15.515 56.891 -48.242 1.00 22.50 ATOM 214 OD1 ASN A 30 15.136 57.977 -48.709 1.00 18.29 ATOM 215 ND2 ASN A 30 15.689 55.759 -49.011 1.00 22.63 ATOM 216 N ASN A 31 16.761 56.515 -44.054 1.00 11.02 ATOM 217 CA ASN A 31 16.530 56.652 -42.671 1.00 9.90 ATOM 218 C ASN A 31 17.818 56.798 -41.902 1.00 6.58 ATOM 219 O ASN A 31 18.694 55.898 -41.955 1.00 4.85 ATOM 220 CB ASN A 31 15.760 55.424 -42.145 1.00 6.98 ATOM 221 CG ASN A 31 14.467 55.180 -42.966 1.00 14.28 ATOM 222 OD1 ASN A 31 13.762 56.123 -43.321 1.00 7.84 ATOM 223 ND2 ASN A 31 14.218 53.914 -43.341 1.00 16.55 ATOM 224 N MET A 32 17.807 57.813 -41.093 1.00 5.23 ATOM 225 CA MET A 32 18.898 58.140 -40.201 1.00 7.27 ATOM 226 C MET A 32 18.254 58.442 -38.836 1.00 8.07 ATOM 227 O MET A 32 17.211 58.997 -38.766 1.00 8.99 ATOM 228 CB MET A 32 19.672 59.387 -40.702 1.00 3.95 ATOM 229 CG MET A 32 20.577 59.136 -41.919 1.00 5.49 ATOM 230 SD MET A 32 21.698 60.644 -42.175 1.00 5.77 ATOM 231 CE MET A 32 22.930 60.281 -40.924 1.00 2.69 ATOM 232 N TYR A 33 18.939 58.049 -37.781 1.00 10.23 ATOM 233 CA TYR A 33 18.485 58.134 -36.453 1.00 11.65 ATOM 234 C TYR A 33 19.529 58.685 -35.519 1.00 13.00 ATOM 235 O TYR A 33 20.745 58.482 -35.738 1.00 14.80 ATOM 236 CB TYR A 33 18.183 56.755 -35.952 1.00 8.27 ATOM 237 CG TYR A 33 17.172 55.995 -36.797 1.00 9.16 ATOM 238 CD1 TYR A 33 17.567 55.372 -37.947 1.00 9.60 ATOM 239 CD2 TYR A 33 15.875 55.813 -36.394 1.00 8.35 ATOM 240 CE1 TYR A 33 16.726 54.629 -38.655 1.00 8.48 ATOM 241 CE2 TYR A 33 14.994 55.044 -37.161 1.00 4.06 ATOM 242 CZ TYR A 33 15.412 54.492 -38.272 1.00 2.00 ATOM 243 OH TYR A 33 14.651 53.753 -39.062 1.00 2.00 ATOM 244 N TRP A 34 19.017 59.313 -34.456 1.00 12.47 ATOM 245 CA TRP A 34 19.789 59.833 -33.397 1.00 14.01 ATOM 246 C TRP A 34 19.380 59.348 -32.091 1.00 14.80 ATOM 247 O TRP A 34 18.295 59.679 -31.673 1.00 13.65 ATOM 248 CB TRP A 34 19.719 61.354 -33.312 1.00 14.33 ATOM 249 CG TRP A 34 21.039 62.043 -33.708 1.00 14.58 ATOM 250 CD1 TRP A 34 21.164 63.184 -34.489 1.00 21.03 ATOM 251 CD2 TRP A 34 22.393 61.706 -33.337 1.00 21.37 ATOM 252 NE1 TRP A 34 22.489 63.581 -34.609 1.00 18.93 ATOM 253 CE2 TRP A 34 23.268 62.656 -33.967 1.00 22.46 ATOM 254 CE3 TRP A 34 22.966 60.679 -32.611 1.00 22.42 ATOM 255 CZ2 TRP A 34 24.640 62.626 -33.817 1.00 16.69 ATOM 256 CZ3 TRP A 34 24.360 60.669 -32.487 1.00 19.46 ATOM 257 CH2 TRP A 34 25.156 61.624 -33.089 1.00 16.75 ATOM 258 N TYR A 35 20.318 58.700 -31.373 1.00 16.59 ATOM 259 CA TYR A 35 20.025 58.048 -30.110 1.00 19.53 ATOM 260 C TYR A 35 20.770 58.434 -28.838 1.00 23.24 ATOM 261 O TYR A 35 21.798 59.136 -28.807 1.00 23.03 ATOM 262 CB TYR A 35 20.165 56.517 -30.238 1.00 19.62 ATOM 263 CG TYR A 35 19.116 55.815 -31.007 1.00 17.41 ATOM 264 CD1 TYR A 35 19.385 55.211 -32.233 1.00 24.24 ATOM 265 CD2 TYR A 35 17.824 55.757 -30.540 1.00 26.35 ATOM 266 CE1 TYR A 35 18.329 54.539 -32.996 1.00 23.20 ATOM 267 CE2 TYR A 35 16.774 55.105 -31.289 1.00 23.93 ATOM 268 CZ TYR A 35 17.047 54.502 -32.502 1.00 18.60 ATOM 269 OH TYR A 35 16.022 53.857 -33.132 1.00 18.41 ATOM 270 N ARG A 36 20.215 57.924 -27.745 1.00 26.23 ATOM 271 CA ARG A 36 20.751 58.211 -26.419 1.00 28.69 ATOM 272 C ARG A 36 20.212 57.170 -25.494 1.00 28.15 ATOM 273 O ARG A 36 19.027 56.836 -25.571 1.00 28.01 ATOM 274 CB ARG A 36 20.285 59.583 -25.939 1.00 27.85 ATOM 275 CG ARG A 36 20.493 59.755 -24.462 1.00 31.16 ATOM 276 CD ARG A 36 19.602 60.811 -23.864 1.00 33.89 ATOM 277 NE ARG A 36 20.211 61.355 -22.672 1.00 36.37 ATOM 278 CZ ARG A 36 19.768 62.446 -22.062 1.00 41.06 ATOM 279 NH1 ARG A 36 18.687 63.103 -22.518 1.00 39.15 ATOM 280 NH2 ARG A 36 20.414 62.881 -20.979 1.00 45.24 ATOM 281 N GLN A 37 21.052 56.654 -24.618 1.00 27.73 ATOM 282 CA GLN A 37 20.513 55.667 -23.666 1.00 29.93 ATOM 283 C GLN A 37 20.937 55.839 -22.220 1.00 32.10 ATOM 284 O GLN A 37 22.045 56.329 -21.956 1.00 31.45 ATOM 285 CB GLN A 37 20.940 54.259 -24.103 1.00 28.84 ATOM 286 CG GLN A 37 22.207 53.757 -23.477 1.00 28.69 ATOM 287 CD GLN A 37 23.398 54.608 -23.778 1.00 28.99 ATOM 288 OE1 GLN A 37 23.312 55.848 -23.782 1.00 31.15 ATOM 289 NE2 GLN A 37 24.542 53.954 -23.997 1.00 31.03 ATOM 290 N ASP A 38 20.091 55.359 -21.292 1.00 35.15 ATOM 291 CA ASP A 38 20.347 55.510 -19.830 1.00 37.59 ATOM 292 C ASP A 38 21.750 54.926 -19.513 1.00 39.77 ATOM 293 O ASP A 38 22.144 53.892 -20.107 1.00 39.61 ATOM 294 CB ASP A 38 19.246 54.830 -18.980 1.00 37.64 ATOM 295 CG ASP A 38 17.786 55.219 -19.403 1.00 40.45 ATOM 296 OD1 ASP A 38 16.827 54.657 -18.785 1.00 43.63 ATOM 297 OD2 ASP A 38 17.596 56.075 -20.341 1.00 42.66 ATOM 298 N THR A 39 22.522 55.610 -18.641 1.00 40.55 ATOM 299 CA THR A 39 23.847 55.118 -18.192 1.00 40.95 ATOM 300 C THR A 39 23.898 53.578 -18.042 1.00 40.92 ATOM 301 O THR A 39 23.483 53.036 -17.009 1.00 41.40 ATOM 302 CB THR A 39 24.208 55.719 -16.803 1.00 41.28 ATOM 303 OG1 THR A 39 23.294 55.208 -15.795 1.00 40.20 ATOM 304 CG2 THR A 39 24.172 57.241 -16.865 1.00 38.52 ATOM 305 N GLY A 40 24.365 52.867 -19.061 1.00 40.84 ATOM 306 CA GLY A 40 24.301 51.382 -19.003 1.00 39.24 ATOM 307 C GLY A 40 22.895 50.808 -18.952 1.00 39.07 ATOM 308 O GLY A 40 22.571 49.886 -18.168 1.00 38.71 ATOM 309 N HIS A 41 22.035 51.322 -19.806 1.00 38.93 ATOM 310 CA HIS A 41 20.732 50.721 -19.935 1.00 39.45 ATOM 311 C HIS A 41 20.433 50.476 -21.375 1.00 38.06 ATOM 312 O HIS A 41 21.288 49.913 -22.066 1.00 39.00 ATOM 313 CB HIS A 41 19.656 51.558 -19.295 1.00 40.24 ATOM 314 CG HIS A 41 19.886 51.795 -17.843 1.00 44.06 ATOM 315 ND1 HIS A 41 20.900 52.611 -17.378 1.00 44.73 ATOM 316 CD2 HIS A 41 19.210 51.352 -16.751 1.00 44.64 ATOM 317 CE1 HIS A 41 20.838 52.657 -16.056 1.00 48.20 ATOM 318 NE2 HIS A 41 19.828 51.897 -15.653 1.00 46.58 ATOM 319 N GLY A 42 19.234 50.901 -21.798 1.00 36.92 ATOM 320 CA GLY A 42 18.756 50.882 -23.205 1.00 33.98 ATOM 321 C GLY A 42 18.650 52.260 -23.892 1.00 32.32 ATOM 322 O GLY A 42 18.530 53.325 -23.203 1.00 30.64 ATOM 323 N LEU A 43 18.686 52.201 -25.244 1.00 30.24 ATOM 324 CA LEU A 43 18.813 53.349 -26.156 1.00 28.39 ATOM 325 C LEU A 43 17.429 53.821 -26.436 1.00 26.43 ATOM 326 O LEU A 43 16.610 53.017 -26.821 1.00 27.01 ATOM 327 CB LEU A 43 19.447 52.940 -27.507 1.00 26.17 ATOM 328 CG LEU A 43 20.808 52.296 -27.686 1.00 27.83 ATOM 329 CD1 LEU A 43 20.850 51.996 -29.120 1.00 20.60 ATOM 330 CD2 LEU A 43 22.063 53.200 -27.360 1.00 26.64 ATOM 331 N ARG A 44 17.190 55.112 -26.282 1.00 25.05 ATOM 332 CA ARG A 44 15.838 55.669 -26.456 1.00 21.42 ATOM 333 C ARG A 44 15.875 56.773 -27.502 1.00 18.53 ATOM 334 O ARG A 44 16.653 57.707 -27.355 1.00 15.20 ATOM 335 CB ARG A 44 15.350 56.296 -25.153 1.00 21.90 ATOM 336 CG ARG A 44 14.698 55.388 -24.124 1.00 25.18 ATOM 337 CD ARG A 44 14.147 56.223 -22.980 1.00 25.46 ATOM 338 NE ARG A 44 12.690 56.439 -23.148 1.00 32.69 ATOM 339 CZ ARG A 44 11.874 57.006 -22.248 1.00 31.77 ATOM 340 NH1 ARG A 44 12.363 57.448 -21.079 1.00 32.00 ATOM 341 NH2 ARG A 44 10.555 57.108 -22.503 1.00 30.75 ATOM 342 N LEU A 45 14.957 56.707 -28.469 1.00 16.07 ATOM 343 CA LEU A 45 14.820 57.706 -29.550 1.00 16.26 ATOM 344 C LEU A 45 14.482 59.159 -29.299 1.00 17.44 ATOM 345 O LEU A 45 13.280 59.517 -29.108 1.00 17.07 ATOM 346 CB LEU A 45 13.762 57.206 -30.568 1.00 16.13 ATOM 347 CG LEU A 45 13.630 57.726 -32.009 1.00 13.95 ATOM 348 CD1 LEU A 45 14.927 58.143 -32.676 1.00 9.54 ATOM 349 CD2 LEU A 45 12.942 56.649 -32.893 1.00 15.48 ATOM 350 N ILE A 46 15.475 60.026 -29.511 1.00 17.03 ATOM 351 CA ILE A 46 15.239 61.497 -29.465 1.00 17.15 ATOM 352 C ILE A 46 14.645 62.029 -30.738 1.00 17.84 ATOM 353 O ILE A 46 13.578 62.589 -30.728 1.00 16.66 ATOM 354 CB ILE A 46 16.535 62.247 -29.258 1.00 17.70 ATOM 355 CG1 ILE A 46 17.534 61.249 -28.731 1.00 17.56 ATOM 356 CG2 ILE A 46 16.338 63.315 -28.213 1.00 15.51 ATOM 357 CD1 ILE A 46 18.843 61.663 -29.077 1.00 31.46 ATOM 358 N HIS A 47 15.366 61.844 -31.845 1.00 18.47 ATOM 359 CA HIS A 47 14.915 62.350 -33.169 1.00 19.88 ATOM 360 C HIS A 47 15.342 61.473 -34.313 1.00 19.68 ATOM 361 O HIS A 47 16.442 60.924 -34.283 1.00 20.02 ATOM 362 CB HIS A 47 15.493 63.749 -33.415 1.00 18.60 ATOM 363 CG HIS A 47 14.717 64.794 -32.719 1.00 20.12 ATOM 364 ND1 HIS A 47 13.370 64.973 -32.962 1.00 19.16 ATOM 365 CD2 HIS A 47 15.052 65.676 -31.756 1.00 18.63 ATOM 366 CE1 HIS A 47 12.922 65.972 -32.223 1.00 21.23 ATOM 367 NE2 HIS A 47 13.925 66.433 -31.500 1.00 23.41 ATOM 368 N TYR A 48 14.499 61.385 -35.333 1.00 21.16 ATOM 369 CA TYR A 48 14.814 60.597 -36.549 1.00 20.65 ATOM 370 C TYR A 48 14.527 61.357 -37.816 1.00 21.75 ATOM 371 O TYR A 48 14.028 62.495 -37.743 1.00 23.47 ATOM 372 CB TYR A 48 14.078 59.310 -36.601 1.00 19.65 ATOM 373 CG TYR A 48 12.582 59.339 -36.698 1.00 15.57 ATOM 374 CD1 TYR A 48 11.852 59.965 -35.756 1.00 12.80 ATOM 375 CD2 TYR A 48 11.909 58.546 -37.644 1.00 13.82 ATOM 376 CE1 TYR A 48 10.495 59.958 -35.784 1.00 20.40 ATOM 377 CE2 TYR A 48 10.548 58.489 -37.674 1.00 20.23 ATOM 378 CZ TYR A 48 9.848 59.245 -36.721 1.00 21.09 ATOM 379 OH TYR A 48 8.507 59.262 -36.650 1.00 26.85 ATOM 380 N SER A 49 14.874 60.783 -38.965 1.00 21.01 ATOM 381 CA SER A 49 14.604 61.422 -40.248 1.00 21.90 ATOM 382 C SER A 49 14.467 60.424 -41.392 1.00 23.43 ATOM 383 O SER A 49 15.316 59.524 -41.525 1.00 25.88 ATOM 384 CB SER A 49 15.683 62.458 -40.535 1.00 20.33 ATOM 385 OG SER A 49 15.677 62.884 -41.871 1.00 20.71 ATOM 386 N TYR A 50 13.399 60.596 -42.210 1.00 25.27 ATOM 387 CA TYR A 50 13.154 59.850 -43.486 1.00 24.55 ATOM 388 C TYR A 50 13.955 60.321 -44.693 1.00 23.16 ATOM 389 O TYR A 50 14.199 59.547 -45.605 1.00 21.41 ATOM 390 CB TYR A 50 11.662 59.878 -43.843 1.00 25.93 ATOM 391 CG TYR A 50 10.801 59.254 -42.771 1.00 27.76 ATOM 392 CD1 TYR A 50 11.001 57.919 -42.349 1.00 23.84 ATOM 393 CD2 TYR A 50 9.786 60.020 -42.177 1.00 26.69 ATOM 394 CE1 TYR A 50 10.201 57.382 -41.364 1.00 29.67 ATOM 395 CE2 TYR A 50 9.017 59.535 -41.212 1.00 26.58 ATOM 396 CZ TYR A 50 9.186 58.226 -40.810 1.00 31.34 ATOM 397 OH TYR A 50 8.312 57.826 -39.836 1.00 30.53 ATOM 398 N GLY A 51 14.382 61.599 -44.667 1.00 24.09 ATOM 399 CA GLY A 51 15.044 62.217 -45.809 1.00 22.40 ATOM 400 C GLY A 51 15.515 63.611 -45.560 1.00 23.82 ATOM 401 O GLY A 51 14.961 64.313 -44.716 1.00 26.06 ATOM 402 N ALA A 52 16.553 64.051 -46.281 1.00 23.19 ATOM 403 CA ALA A 52 17.007 65.436 -46.141 1.00 23.91 ATOM 404 C ALA A 52 15.881 66.444 -46.162 1.00 24.25 ATOM 405 O ALA A 52 14.943 66.314 -46.916 1.00 25.89 ATOM 406 CB ALA A 52 18.151 65.807 -47.227 1.00 22.66 ATOM 407 N GLY A 53 16.015 67.459 -45.311 1.00 24.18 ATOM 408 CA GLY A 53 15.035 68.450 -45.106 1.00 22.02 ATOM 409 C GLY A 53 13.803 67.916 -44.403 1.00 22.81 ATOM 410 O GLY A 53 12.703 68.347 -44.689 1.00 21.34 ATOM 411 N SER A 54 13.971 66.935 -43.509 1.00 22.17 ATOM 412 CA SER A 54 12.877 66.527 -42.671 1.00 21.55 ATOM 413 C SER A 54 13.201 65.595 -41.507 1.00 21.71 ATOM 414 O SER A 54 13.686 64.487 -41.696 1.00 20.84 ATOM 415 CB SER A 54 11.802 65.882 -43.505 1.00 20.87 ATOM 416 OG SER A 54 10.948 65.235 -42.602 1.00 23.65 ATOM 417 N THR A 55 12.833 66.054 -40.303 1.00 22.12 ATOM 418 CA THR A 55 12.933 65.303 -39.070 1.00 21.61 ATOM 419 C THR A 55 11.540 65.066 -38.392 1.00 21.37 ATOM 420 O THR A 55 10.504 65.776 -38.677 1.00 18.29 ATOM 421 CB THR A 55 13.918 65.965 -38.099 1.00 21.00 ATOM 422 OG1 THR A 55 13.268 67.027 -37.418 1.00 22.30 ATOM 423 CG2 THR A 55 15.184 66.550 -38.840 1.00 24.47 ATOM 424 N GLU A 56 11.513 64.052 -37.523 1.00 21.59 ATOM 425 CA GLU A 56 10.357 63.828 -36.597 1.00 23.73 ATOM 426 C GLU A 56 10.811 63.516 -35.181 1.00 23.29 ATOM 427 O GLU A 56 11.898 62.891 -34.967 1.00 24.24 ATOM 428 CB GLU A 56 9.366 62.757 -37.097 1.00 22.89 ATOM 429 CG GLU A 56 8.972 62.899 -38.593 1.00 23.30 ATOM 430 CD GLU A 56 7.966 63.975 -38.767 1.00 24.59 ATOM 431 OE1 GLU A 56 6.975 63.962 -38.004 1.00 24.30 ATOM 432 OE2 GLU A 56 8.173 64.864 -39.630 1.00 22.90 ATOM 433 N LYS A 57 9.977 63.983 -34.260 1.00 21.97 ATOM 434 CA LYS A 57 10.125 63.815 -32.851 1.00 21.74 ATOM 435 C LYS A 57 10.046 62.357 -32.520 1.00 23.50 ATOM 436 O LYS A 57 9.113 61.660 -33.019 1.00 24.08 ATOM 437 CB LYS A 57 9.004 64.498 -32.131 1.00 21.29 ATOM 438 CG LYS A 57 9.092 66.030 -32.143 1.00 22.47 ATOM 439 CD LYS A 57 8.106 66.668 -31.228 1.00 17.06 ATOM 440 CE LYS A 57 6.736 66.528 -31.850 1.00 19.31 ATOM 441 NZ LYS A 57 5.969 67.741 -31.538 1.00 13.09 ATOM 442 N GLY A 58 11.013 61.945 -31.675 1.00 22.52 ATOM 443 CA GLY A 58 11.141 60.601 -31.144 1.00 23.14 ATOM 444 C GLY A 58 10.491 60.439 -29.804 1.00 23.00 ATOM 445 O GLY A 58 9.500 61.107 -29.477 1.00 25.96 ATOM 446 N ASP A 59 11.057 59.544 -29.011 1.00 22.81 ATOM 447 CA ASP A 59 10.479 59.219 -27.734 1.00 21.67 ATOM 448 C ASP A 59 10.615 60.410 -26.766 1.00 20.59 ATOM 449 O ASP A 59 9.570 60.910 -26.239 1.00 16.51 ATOM 450 CB ASP A 59 11.204 58.085 -27.102 1.00 21.61 ATOM 451 CG ASP A 59 10.902 56.820 -27.730 1.00 24.79 ATOM 452 OD1 ASP A 59 9.737 56.567 -28.095 1.00 31.31 ATOM 453 OD2 ASP A 59 11.864 56.042 -27.866 1.00 35.15 ATOM 454 N ILE A 60 11.906 60.748 -26.535 1.00 14.01 ATOM 455 CA ILE A 60 12.349 61.815 -25.704 1.00 12.85 ATOM 456 C ILE A 60 12.806 63.151 -26.431 1.00 13.38 ATOM 457 O ILE A 60 13.811 63.676 -26.085 1.00 7.88 ATOM 458 CB ILE A 60 13.442 61.322 -24.741 1.00 11.10 ATOM 459 CG1 ILE A 60 14.791 61.088 -25.491 1.00 7.48 ATOM 460 CG2 ILE A 60 12.981 60.093 -24.170 1.00 7.33 ATOM 461 CD1 ILE A 60 15.782 60.438 -24.619 1.00 6.63 ATOM 462 N PRO A 61 11.927 63.770 -27.291 1.00 15.12 ATOM 463 CA PRO A 61 12.273 64.920 -28.126 1.00 15.69 ATOM 464 C PRO A 61 12.844 66.019 -27.261 1.00 18.53 ATOM 465 O PRO A 61 14.033 66.465 -27.424 1.00 17.03 ATOM 466 CB PRO A 61 10.909 65.320 -28.776 1.00 18.22 ATOM 467 CG PRO A 61 9.837 64.631 -28.044 1.00 14.90 ATOM 468 CD PRO A 61 10.511 63.389 -27.425 1.00 15.95 ATOM 469 N ASP A 62 12.055 66.359 -26.241 1.00 19.16 ATOM 470 CA ASP A 62 12.335 67.506 -25.360 1.00 22.26 ATOM 471 C ASP A 62 13.779 67.849 -25.121 1.00 22.45 ATOM 472 O ASP A 62 14.600 66.976 -24.835 1.00 21.75 ATOM 473 CB ASP A 62 11.652 67.288 -24.035 1.00 22.99 ATOM 474 CG ASP A 62 10.145 67.026 -24.200 1.00 26.95 ATOM 475 OD1 ASP A 62 9.379 68.031 -24.343 1.00 27.55 ATOM 476 OD2 ASP A 62 9.751 65.812 -24.217 1.00 23.92 ATOM 477 N GLY A 63 14.084 69.127 -25.257 1.00 23.31 ATOM 478 CA GLY A 63 15.418 69.672 -24.964 1.00 23.00 ATOM 479 C GLY A 63 16.459 69.321 -26.028 1.00 25.36 ATOM 480 O GLY A 63 17.703 69.460 -25.831 1.00 24.68 ATOM 481 N TYR A 65 15.959 68.720 -27.420 1.00 19.63 ATOM 482 CA TYR A 65 16.878 68.607 -28.527 1.00 20.06 ATOM 483 C TYR A 65 16.368 69.227 -29.784 1.00 20.64 ATOM 484 O TYR A 65 15.126 69.419 -29.965 1.00 23.12 ATOM 485 CB TYR A 65 17.234 67.148 -28.747 1.00 19.26 ATOM 486 CG TYR A 65 18.014 66.628 -27.603 1.00 18.44 ATOM 487 CD1 TYR A 65 19.403 66.906 -27.457 1.00 16.23 ATOM 488 CD2 TYR A 65 17.393 65.948 -26.599 1.00 14.82 ATOM 489 CE1 TYR A 65 20.115 66.405 -26.338 1.00 17.23 ATOM 490 CE2 TYR A 65 18.076 65.465 -25.489 1.00 17.56 ATOM 491 CZ TYR A 65 19.409 65.684 -25.339 1.00 20.74 ATOM 492 OH TYR A 65 20.037 65.156 -24.211 1.00 24.31 ATOM 493 N LYS A 66 17.332 69.545 -30.665 1.00 20.59 ATOM 494 CA LYS A 66 17.100 70.052 -32.030 1.00 18.57 ATOM 495 C LYS A 66 17.852 69.194 -32.963 1.00 17.77 ATOM 496 O LYS A 66 18.948 68.800 -32.639 1.00 20.25 ATOM 497 CB LYS A 66 17.584 71.478 -32.191 1.00 18.01 ATOM 498 CG LYS A 66 16.390 72.410 -32.349 1.00 14.95 ATOM 499 CD LYS A 66 15.674 72.462 -31.017 1.00 14.01 ATOM 500 CE LYS A 66 14.751 73.705 -30.789 1.00 21.17 ATOM 501 NZ LYS A 66 15.542 75.062 -30.712 1.00 20.26 ATOM 502 N ALA A 67 17.283 68.861 -34.109 1.00 16.92 ATOM 503 CA ALA A 67 18.016 68.067 -35.075 1.00 16.23 ATOM 504 C ALA A 67 18.008 68.801 -36.409 1.00 15.26 ATOM 505 O ALA A 67 17.425 69.935 -36.527 1.00 15.93 ATOM 506 CB ALA A 67 17.514 66.589 -35.160 1.00 13.96 ATOM 507 N SER A 68 18.698 68.217 -37.398 1.00 12.50 ATOM 508 CA SER A 68 18.651 68.734 -38.754 1.00 10.06 ATOM 509 C SER A 68 19.205 67.806 -39.812 1.00 9.01 ATOM 510 O SER A 68 20.371 67.363 -39.695 1.00 9.10 ATOM 511 CB SER A 68 19.462 70.011 -38.820 1.00 8.25 ATOM 512 OG SER A 68 19.426 70.358 -40.171 1.00 9.36 ATOM 513 N ARG A 69 18.460 67.575 -40.888 1.00 7.32 ATOM 514 CA ARG A 69 18.987 66.675 -42.042 1.00 6.51 ATOM 515 C ARG A 69 19.050 67.470 -43.266 1.00 6.32 ATOM 516 O ARG A 69 18.025 67.776 -43.877 1.00 7.29 ATOM 517 CB ARG A 69 18.025 65.512 -42.346 1.00 7.56 ATOM 518 CG ARG A 69 18.425 64.404 -43.244 1.00 2.00 ATOM 519 CD ARG A 69 19.062 63.260 -42.459 1.00 7.87 ATOM 520 NE ARG A 69 19.565 62.159 -43.299 1.00 2.00 ATOM 521 CZ ARG A 69 18.724 61.367 -43.970 1.00 9.88 ATOM 522 NH1 ARG A 69 19.189 60.339 -44.719 1.00 2.65 ATOM 523 NH2 ARG A 69 17.380 61.594 -43.841 1.00 6.65 ATOM 524 N PRO A 70 20.233 67.879 -43.615 1.00 8.98 ATOM 525 CA PRO A 70 20.571 68.724 -44.742 1.00 8.76 ATOM 526 C PRO A 70 20.981 68.046 -45.986 1.00 8.00 ATOM 527 O PRO A 70 21.057 68.718 -47.017 1.00 8.50 ATOM 528 CB PRO A 70 21.709 69.611 -44.185 1.00 10.30 ATOM 529 CG PRO A 70 22.478 68.558 -43.262 1.00 10.69 ATOM 530 CD PRO A 70 21.396 67.681 -42.695 1.00 11.50 ATOM 531 N SER A 71 21.092 66.704 -45.949 1.00 10.22 ATOM 532 CA SER A 71 21.519 65.934 -47.038 1.00 7.07 ATOM 533 C SER A 71 21.439 64.413 -46.663 1.00 10.49 ATOM 534 O SER A 71 22.057 64.013 -45.654 1.00 12.31 ATOM 535 CB SER A 71 22.961 66.344 -47.335 1.00 9.69 ATOM 536 OG SER A 71 23.860 66.173 -46.280 1.00 6.34 ATOM 537 N GLN A 72 20.687 63.610 -47.418 1.00 7.39 ATOM 538 CA GLN A 72 20.667 62.122 -47.333 1.00 10.10 ATOM 539 C GLN A 72 21.697 61.453 -46.511 1.00 10.83 ATOM 540 O GLN A 72 21.357 60.718 -45.696 1.00 15.05 ATOM 541 CB GLN A 72 20.553 61.480 -48.729 1.00 8.55 ATOM 542 CG GLN A 72 19.132 60.903 -48.997 1.00 6.16 ATOM 543 CD GLN A 72 18.945 59.442 -48.739 1.00 4.96 ATOM 544 OE1 GLN A 72 19.928 58.648 -48.743 1.00 7.54 ATOM 545 NE2 GLN A 72 17.665 59.032 -48.424 1.00 4.14 ATOM 546 N GLU A 73 22.967 61.840 -46.616 1.00 18.10 ATOM 547 CA GLU A 73 24.014 61.227 -45.813 1.00 20.45 ATOM 548 C GLU A 73 24.460 62.009 -44.574 1.00 21.25 ATOM 549 O GLU A 73 25.455 61.657 -43.906 1.00 22.74 ATOM 550 CB GLU A 73 25.204 60.777 -46.715 1.00 21.37 ATOM 551 CG GLU A 73 26.107 61.919 -47.214 1.00 25.91 ATOM 552 CD GLU A 73 25.471 62.696 -48.296 1.00 30.33 ATOM 553 OE1 GLU A 73 25.819 63.890 -48.434 1.00 36.07 ATOM 554 OE2 GLU A 73 24.575 62.130 -48.985 1.00 37.75 ATOM 555 N GLN A 74 23.753 63.069 -44.218 1.00 21.10 ATOM 556 CA GLN A 74 24.223 63.914 -43.050 1.00 18.96 ATOM 557 C GLN A 74 23.063 64.248 -42.126 1.00 19.32 ATOM 558 O GLN A 74 21.965 64.539 -42.642 1.00 20.50 ATOM 559 CB GLN A 74 24.840 65.155 -43.538 1.00 16.28 ATOM 560 CG GLN A 74 25.188 66.134 -42.337 1.00 20.77 ATOM 561 CD GLN A 74 26.198 65.514 -41.271 1.00 18.29 ATOM 562 OE1 GLN A 74 26.127 65.828 -40.078 1.00 18.61 ATOM 563 NE2 GLN A 74 27.109 64.603 -41.728 1.00 22.03 ATOM 564 N PHE A 75 23.271 64.195 -40.802 1.00 20.12 ATOM 565 CA PHE A 75 22.225 64.478 -39.692 1.00 20.28 ATOM 566 C PHE A 75 23.044 65.020 -38.500 1.00 20.22 ATOM 567 O PHE A 75 24.233 64.606 -38.304 1.00 21.49 ATOM 568 CB PHE A 75 21.526 63.178 -39.228 1.00 19.63 ATOM 569 CG PHE A 75 20.143 63.339 -38.633 1.00 19.51 ATOM 570 CD1 PHE A 75 19.429 64.541 -38.725 1.00 17.91 ATOM 571 CD2 PHE A 75 19.501 62.247 -38.086 1.00 15.80 ATOM 572 CE1 PHE A 75 18.126 64.640 -38.263 1.00 18.24 ATOM 573 CE2 PHE A 75 18.170 62.395 -37.596 1.00 18.85 ATOM 574 CZ PHE A 75 17.509 63.600 -37.706 1.00 13.17 ATOM 575 N SER A 76 22.438 65.895 -37.724 1.00 18.33 ATOM 576 CA SER A 76 23.094 66.642 -36.635 1.00 19.06 ATOM 577 C SER A 76 22.195 66.909 -35.418 1.00 19.81 ATOM 578 O SER A 76 20.976 67.121 -35.561 1.00 21.88 ATOM 579 CB SER A 76 23.724 67.957 -37.150 1.00 17.55 ATOM 580 OG SER A 76 24.248 67.727 -38.459 1.00 15.12 ATOM 581 N LEU A 77 22.764 66.836 -34.218 1.00 19.96 ATOM 582 CA LEU A 77 21.937 66.978 -32.984 1.00 21.04 ATOM 583 C LEU A 77 22.306 68.335 -32.408 1.00 22.72 ATOM 584 O LEU A 77 23.515 68.564 -32.114 1.00 23.84 ATOM 585 CB LEU A 77 22.267 65.859 -31.972 1.00 19.71 ATOM 586 CG LEU A 77 21.254 65.468 -30.936 1.00 16.37 ATOM 587 CD1 LEU A 77 20.058 65.094 -31.704 1.00 23.34 ATOM 588 CD2 LEU A 77 21.653 64.259 -30.036 1.00 19.34 ATOM 589 N ILE A 78 21.331 69.241 -32.370 1.00 24.76 ATOM 590 CA ILE A 78 21.572 70.568 -31.829 1.00 28.07 ATOM 591 C ILE A 78 21.116 70.641 -30.376 1.00 29.24 ATOM 592 O ILE A 78 20.137 70.001 -29.992 1.00 29.48 ATOM 593 CB ILE A 78 21.083 71.747 -32.771 1.00 28.37 ATOM 594 CG1 ILE A 78 21.845 71.695 -34.109 1.00 30.48 ATOM 595 CG2 ILE A 78 21.437 73.125 -32.176 1.00 25.48 ATOM 596 CD1 ILE A 78 21.085 72.241 -35.308 1.00 32.11 ATOM 597 N LEU A 79 21.894 71.361 -29.572 1.00 31.09 ATOM 598 CA LEU A 79 21.646 71.560 -28.153 1.00 33.06 ATOM 599 C LEU A 79 21.943 72.998 -27.807 1.00 33.59 ATOM 600 O LEU A 79 23.115 73.408 -27.776 1.00 34.79 ATOM 601 CB LEU A 79 22.576 70.648 -27.361 1.00 33.63 ATOM 602 CG LEU A 79 22.018 69.218 -27.316 1.00 33.58 ATOM 603 CD1 LEU A 79 22.503 68.427 -28.455 1.00 35.82 ATOM 604 CD2 LEU A 79 22.473 68.540 -26.077 1.00 32.36 ATOM 605 N GLU A 80 20.890 73.777 -27.589 1.00 34.47 ATOM 606 CA GLU A 80 21.055 75.212 -27.578 1.00 34.81 ATOM 607 C GLU A 80 21.702 75.589 -26.248 1.00 35.80 ATOM 608 O GLU A 80 22.928 75.889 -26.179 1.00 37.02 ATOM 609 CB GLU A 80 19.721 75.882 -27.786 1.00 34.59 ATOM 610 CG GLU A 80 19.770 77.292 -28.411 1.00 34.90 ATOM 611 CD GLU A 80 19.674 77.291 -29.941 1.00 35.81 ATOM 612 OE1 GLU A 80 18.613 76.862 -30.493 1.00 33.77 ATOM 613 OE2 GLU A 80 20.666 77.723 -30.575 1.00 33.25 ATOM 614 N SER A 81 20.928 75.517 -25.170 1.00 34.67 ATOM 615 CA SER A 81 21.519 75.649 -23.834 1.00 33.28 ATOM 616 C SER A 81 21.590 74.271 -23.172 1.00 32.90 ATOM 617 O SER A 81 20.570 73.728 -22.759 1.00 32.83 ATOM 618 CB SER A 81 20.715 76.626 -22.949 1.00 34.47 ATOM 619 OG SER A 81 20.274 77.805 -23.635 1.00 33.38 ATOM 620 N ALA A 82 22.800 73.708 -23.122 1.00 32.67 ATOM 621 CA ALA A 82 23.068 72.434 -22.458 1.00 32.37 ATOM 622 C ALA A 82 22.717 72.504 -21.007 1.00 32.22 ATOM 623 O ALA A 82 22.595 73.598 -20.430 1.00 34.49 ATOM 624 CB ALA A 82 24.509 72.063 -22.586 1.00 31.35 ATOM 625 N THR A 83 22.610 71.333 -20.405 1.00 31.68 ATOM 626 CA THR A 83 22.424 71.174 -18.960 1.00 31.76 ATOM 627 C THR A 83 22.860 69.746 -18.549 1.00 31.96 ATOM 628 O THR A 83 22.633 68.790 -19.318 1.00 32.23 ATOM 629 CB THR A 83 20.925 71.301 -18.557 1.00 30.60 ATOM 630 OG1 THR A 83 20.235 70.118 -18.976 1.00 28.00 ATOM 631 CG2 THR A 83 20.285 72.495 -19.217 1.00 33.27 ATOM 632 N PRO A 84 23.476 69.604 -17.357 1.00 31.47 ATOM 633 CA PRO A 84 24.094 68.370 -16.921 1.00 30.69 ATOM 634 C PRO A 84 23.235 67.208 -17.192 1.00 30.90 ATOM 635 O PRO A 84 23.740 66.259 -17.733 1.00 32.14 ATOM 636 CB PRO A 84 24.305 68.597 -15.458 1.00 31.44 ATOM 637 CG PRO A 84 24.748 70.155 -15.443 1.00 30.69 ATOM 638 CD PRO A 84 23.703 70.712 -16.399 1.00 32.64 ATOM 639 N SER A 85 21.940 67.289 -16.909 1.00 30.74 ATOM 640 CA SER A 85 20.986 66.254 -17.312 1.00 30.68 ATOM 641 C SER A 85 21.299 65.585 -18.671 1.00 29.82 ATOM 642 O SER A 85 21.387 64.336 -18.758 1.00 29.59 ATOM 643 CB SER A 85 19.586 66.850 -17.402 1.00 31.56 ATOM 644 OG SER A 85 19.367 67.736 -16.333 1.00 34.84 ATOM 645 N GLN A 86 21.439 66.414 -19.717 1.00 27.94 ATOM 646 CA GLN A 86 21.732 65.966 -21.084 1.00 26.08 ATOM 647 C GLN A 86 23.091 65.288 -21.160 1.00 26.67 ATOM 648 O GLN A 86 23.608 64.988 -22.240 1.00 28.23 ATOM 649 CB GLN A 86 21.691 67.140 -22.047 1.00 25.17 ATOM 650 CG GLN A 86 20.319 67.829 -22.172 1.00 20.93 ATOM 651 CD GLN A 86 20.368 69.002 -23.076 1.00 21.62 ATOM 652 OE1 GLN A 86 21.401 69.744 -23.136 1.00 23.80 ATOM 653 NE2 GLN A 86 19.287 69.208 -23.820 1.00 23.26 ATOM 654 N THR A 87 23.683 64.999 -20.023 1.00 26.64 ATOM 655 CA THR A 87 25.012 64.384 -20.074 1.00 25.84 ATOM 656 C THR A 87 24.914 62.912 -20.298 1.00 24.76 ATOM 657 O THR A 87 24.318 62.224 -19.474 1.00 24.67 ATOM 658 CB THR A 87 25.758 64.614 -18.804 1.00 25.33 ATOM 659 OG1 THR A 87 26.164 65.997 -18.742 1.00 28.64 ATOM 660 CG2 THR A 87 26.982 63.731 -18.783 1.00 27.86 ATOM 661 N SER A 88 25.501 62.395 -21.391 1.00 24.36 ATOM 662 CA SER A 88 25.407 60.952 -21.684 1.00 21.73 ATOM 663 C SER A 88 26.274 60.418 -22.863 1.00 22.18 ATOM 664 O SER A 88 27.319 61.007 -23.207 1.00 19.63 ATOM 665 CB SER A 88 23.940 60.567 -21.884 1.00 20.91 ATOM 666 OG SER A 88 23.838 59.253 -22.405 1.00 24.54 ATOM 667 N VAL A 89 25.808 59.310 -23.478 1.00 21.23 ATOM 668 CA VAL A 89 26.430 58.712 -24.647 1.00 20.48 ATOM 669 C VAL A 89 25.371 58.628 -25.771 1.00 20.61 ATOM 670 O VAL A 89 24.345 57.912 -25.598 1.00 19.43 ATOM 671 CB VAL A 89 26.952 57.283 -24.320 1.00 19.60 ATOM 672 CG1 VAL A 89 27.430 56.704 -25.530 1.00 22.57 ATOM 673 CG2 VAL A 89 28.099 57.282 -23.399 1.00 17.69 ATOM 674 N TYR A 90 25.614 59.411 -26.856 1.00 20.59 ATOM 675 CA TYR A 90 24.821 59.476 -28.078 1.00 19.75 ATOM 676 C TYR A 90 25.227 58.495 -29.234 1.00 19.70 ATOM 677 O TYR A 90 26.435 58.282 -29.492 1.00 20.90 ATOM 678 CB TYR A 90 24.762 60.934 -28.553 1.00 21.37 ATOM 679 CG TYR A 90 24.112 61.839 -27.490 1.00 20.56 ATOM 680 CD1 TYR A 90 24.860 62.303 -26.407 1.00 19.91 ATOM 681 CD2 TYR A 90 22.802 62.251 -27.588 1.00 16.94 ATOM 682 CE1 TYR A 90 24.305 63.093 -25.447 1.00 17.31 ATOM 683 CE2 TYR A 90 22.245 63.063 -26.606 1.00 12.46 ATOM 684 CZ TYR A 90 22.998 63.423 -25.533 1.00 17.07 ATOM 685 OH TYR A 90 22.497 64.165 -24.526 1.00 18.29 ATOM 686 N PHE A 91 24.268 57.943 -29.983 1.00 18.99 ATOM 687 CA PHE A 91 24.676 56.971 -31.084 1.00 18.42 ATOM 688 C PHE A 91 23.810 57.255 -32.288 1.00 17.15 ATOM 689 O PHE A 91 22.624 57.554 -32.137 1.00 16.37 ATOM 690 CB PHE A 91 24.418 55.526 -30.739 1.00 16.98 ATOM 691 CG PHE A 91 25.403 54.914 -29.845 1.00 16.49 ATOM 692 CD1 PHE A 91 26.490 54.188 -30.362 1.00 19.19 ATOM 693 CD2 PHE A 91 25.190 54.910 -28.510 1.00 17.43 ATOM 694 CE1 PHE A 91 27.372 53.597 -29.593 1.00 15.02 ATOM 695 CE2 PHE A 91 26.066 54.366 -27.712 1.00 15.69 ATOM 696 CZ PHE A 91 27.241 53.687 -28.268 1.00 17.74 ATOM 697 N CYS A 92 24.399 57.129 -33.464 1.00 16.41 ATOM 698 CA CYS A 92 23.771 57.517 -34.705 1.00 16.96 ATOM 699 C CYS A 92 23.599 56.269 -35.504 1.00 15.72 ATOM 700 O CYS A 92 24.488 55.435 -35.526 1.00 16.29 ATOM 701 CB CYS A 92 24.678 58.472 -35.489 1.00 18.61 ATOM 702 SG CYS A 92 23.944 59.212 -37.011 1.00 23.63 ATOM 703 N ALA A 93 22.458 56.140 -36.165 1.00 13.99 ATOM 704 CA ALA A 93 22.243 55.027 -37.068 1.00 11.57 ATOM 705 C ALA A 93 21.548 55.415 -38.349 1.00 12.39 ATOM 706 O ALA A 93 20.745 56.401 -38.424 1.00 11.49 ATOM 707 CB ALA A 93 21.489 53.930 -36.413 1.00 10.15 ATOM 708 N SER A 94 21.759 54.539 -39.329 1.00 12.18 ATOM 709 CA SER A 94 21.044 54.576 -40.607 1.00 9.60 ATOM 710 C SER A 94 20.648 53.183 -40.926 1.00 9.12 ATOM 711 O SER A 94 21.406 52.166 -40.720 1.00 6.58 ATOM 712 CB SER A 94 22.023 55.019 -41.649 1.00 7.65 ATOM 713 OG SER A 94 23.207 54.268 -41.355 1.00 12.05 ATOM 714 N GLY A 95 19.505 53.169 -41.543 1.00 11.63 ATOM 715 CA GLY A 95 18.600 52.030 -41.608 1.00 12.49 ATOM 716 C GLY A 95 17.878 52.015 -42.984 1.00 14.87 ATOM 717 O GLY A 95 17.472 53.076 -43.480 1.00 14.59 ATOM 718 N GLY A 96 17.720 50.808 -43.601 1.00 15.93 ATOM 719 CA GLY A 96 17.256 50.745 -45.014 1.00 16.18 ATOM 720 C GLY A 96 17.464 49.438 -45.734 1.00 17.00 ATOM 721 O GLY A 96 18.383 48.692 -45.438 1.00 17.51 ATOM 722 N GLY A 97 16.588 49.132 -46.678 1.00 18.28 ATOM 723 CA GLY A 97 16.631 47.827 -47.309 1.00 17.77 ATOM 724 C GLY A 97 17.089 46.726 -46.412 1.00 18.83 ATOM 725 O GLY A 97 17.969 46.009 -46.752 1.00 20.47 ATOM 726 N GLY A 98 16.462 46.553 -45.261 1.00 21.86 ATOM 727 CA GLY A 98 16.840 45.474 -44.308 1.00 23.33 ATOM 728 C GLY A 98 18.162 45.786 -43.608 1.00 25.81 ATOM 729 O GLY A 98 19.022 44.886 -43.439 1.00 25.35 ATOM 730 N THR A 99 18.368 47.057 -43.204 1.00 24.75 ATOM 731 CA THR A 99 19.680 47.437 -42.682 1.00 25.00 ATOM 732 C THR A 99 19.548 48.550 -41.602 1.00 24.87 ATOM 733 O THR A 99 18.457 49.170 -41.491 1.00 24.41 ATOM 734 CB THR A 99 20.609 47.780 -43.897 1.00 26.72 ATOM 735 OG1 THR A 99 20.607 46.656 -44.794 1.00 29.51 ATOM 736 CG2 THR A 99 22.060 48.119 -43.519 1.00 24.08 ATOM 737 N LEU A 100 20.603 48.685 -40.770 1.00 22.07 ATOM 738 CA LEU A 100 20.668 49.552 -39.620 1.00 21.67 ATOM 739 C LEU A 100 22.149 49.677 -39.220 1.00 22.92 ATOM 740 O LEU A 100 22.780 48.691 -38.892 1.00 22.85 ATOM 741 CB LEU A 100 19.827 49.030 -38.442 1.00 22.58 ATOM 742 CG LEU A 100 19.595 49.844 -37.168 1.00 21.21 ATOM 743 CD1 LEU A 100 19.535 51.364 -37.409 1.00 25.83 ATOM 744 CD2 LEU A 100 18.396 49.373 -36.361 1.00 20.40 ATOM 745 N TYR A 101 22.715 50.878 -39.273 1.00 21.83 ATOM 746 CA TYR A 101 24.121 50.939 -38.988 1.00 21.69 ATOM 747 C TYR A 101 24.314 51.712 -37.736 1.00 20.75 ATOM 748 O TYR A 101 23.656 52.703 -37.532 1.00 19.76 ATOM 749 CB TYR A 101 24.890 51.480 -40.186 1.00 22.03 ATOM 750 CG TYR A 101 25.320 50.372 -41.087 1.00 22.85 ATOM 751 CD1 TYR A 101 25.923 50.635 -42.288 1.00 25.76 ATOM 752 CD2 TYR A 101 25.099 49.037 -40.731 1.00 28.10 ATOM 753 CE1 TYR A 101 26.322 49.615 -43.147 1.00 29.14 ATOM 754 CE2 TYR A 101 25.478 47.958 -41.570 1.00 27.04 ATOM 755 CZ TYR A 101 26.097 48.266 -42.799 1.00 28.81 ATOM 756 OH TYR A 101 26.508 47.282 -43.689 1.00 25.17 ATOM 757 N PHE A 108 25.796 51.509 -36.846 1.00 23.14 ATOM 758 CA PHE A 108 25.593 52.538 -35.802 1.00 22.74 ATOM 759 C PHE A 108 26.853 53.325 -35.788 1.00 23.97 ATOM 760 O PHE A 108 27.890 52.816 -36.196 1.00 25.37 ATOM 761 CB PHE A 108 25.475 51.881 -34.427 1.00 22.25 ATOM 762 CG PHE A 108 24.058 51.459 -34.040 1.00 16.70 ATOM 763 CD1 PHE A 108 23.678 50.130 -34.142 1.00 15.08 ATOM 764 CD2 PHE A 108 23.131 52.378 -33.574 1.00 18.12 ATOM 765 CE1 PHE A 108 22.438 49.732 -33.768 1.00 16.12 ATOM 766 CE2 PHE A 108 21.855 51.997 -33.209 1.00 7.42 ATOM 767 CZ PHE A 108 21.483 50.736 -33.298 1.00 12.82 ATOM 768 N GLY A 109 26.807 54.533 -35.273 1.00 23.99 ATOM 769 CA GLY A 109 28.025 55.292 -35.101 1.00 24.15 ATOM 770 C GLY A 109 28.791 54.785 -33.905 1.00 24.01 ATOM 771 O GLY A 109 28.454 53.768 -33.315 1.00 23.80 ATOM 772 N ALA A 110 29.861 55.467 -33.547 1.00 25.49 ATOM 773 CA ALA A 110 30.728 54.861 -32.550 1.00 25.77 ATOM 774 C ALA A 110 30.348 55.522 -31.280 1.00 26.56 ATOM 775 O ALA A 110 30.881 55.249 -30.243 1.00 28.13 ATOM 776 CB ALA A 110 32.212 55.059 -32.896 1.00 26.23 ATOM 777 N GLY A 111 29.351 56.381 -31.346 1.00 27.71 ATOM 778 CA GLY A 111 28.863 56.987 -30.135 1.00 27.86 ATOM 779 C GLY A 111 29.637 58.278 -29.814 1.00 27.73 ATOM 780 O GLY A 111 30.829 58.413 -30.117 1.00 26.03 ATOM 781 N THR A 112 28.935 59.222 -29.182 1.00 28.75 ATOM 782 CA THR A 112 29.537 60.467 -28.644 1.00 28.28 ATOM 783 C THR A 112 29.319 60.549 -27.147 1.00 28.92 ATOM 784 O THR A 112 28.196 60.439 -26.702 1.00 30.00 ATOM 785 CB THR A 112 28.947 61.626 -29.319 1.00 28.48 ATOM 786 OG1 THR A 112 29.185 61.457 -30.712 1.00 28.68 ATOM 787 CG2 THR A 112 29.594 62.918 -28.838 1.00 31.20 ATOM 788 N ARG A 113 30.403 60.636 -26.377 1.00 30.74 ATOM 789 CA ARG A 113 30.387 60.678 -24.924 1.00 32.03 ATOM 790 C ARG A 113 30.446 62.132 -24.544 1.00 31.11 ATOM 791 O ARG A 113 31.453 62.776 -24.809 1.00 32.54 ATOM 792 CB ARG A 113 31.630 59.986 -24.374 1.00 32.00 ATOM 793 CG ARG A 113 31.649 58.473 -24.550 1.00 35.71 ATOM 794 CD ARG A 113 32.988 57.842 -24.112 1.00 37.55 ATOM 795 NE ARG A 113 33.135 56.454 -24.554 1.00 44.07 ATOM 796 CZ ARG A 113 34.213 55.711 -24.329 1.00 48.18 ATOM 797 NH1 ARG A 113 34.232 54.447 -24.748 1.00 49.96 ATOM 798 NH2 ARG A 113 35.280 56.233 -23.702 1.00 51.15 ATOM 799 N LEU A 114 29.386 62.644 -23.908 1.00 30.65 ATOM 800 CA LEU A 114 29.223 64.073 -23.619 1.00 29.44 ATOM 801 C LEU A 114 29.274 64.390 -22.127 1.00 29.99 ATOM 802 O LEU A 114 29.050 63.498 -21.318 1.00 29.03 ATOM 803 CB LEU A 114 27.924 64.575 -24.216 1.00 29.38 ATOM 804 CG LEU A 114 27.736 66.059 -23.995 1.00 27.56 ATOM 805 CD1 LEU A 114 28.957 66.681 -24.544 1.00 27.56 ATOM 806 CD2 LEU A 114 26.492 66.543 -24.706 1.00 25.50 ATOM 807 N SER A 115 29.539 65.670 -21.765 1.00 30.00 ATOM 808 CA SER A 115 29.621 66.072 -20.353 1.00 27.94 ATOM 809 C SER A 115 29.199 67.512 -20.170 1.00 27.64 ATOM 810 O SER A 115 29.829 68.465 -20.669 1.00 25.16 ATOM 811 CB SER A 115 31.035 65.824 -19.800 1.00 27.42 ATOM 812 OG SER A 115 31.646 64.723 -20.470 1.00 27.25 ATOM 813 N VAL A 116 28.123 67.651 -19.401 1.00 28.68 ATOM 814 CA VAL A 116 27.453 68.912 -19.238 1.00 29.51 ATOM 815 C VAL A 116 27.605 69.348 -17.817 1.00 30.12 ATOM 816 O VAL A 116 26.847 68.922 -16.934 1.00 30.98 ATOM 817 CB VAL A 116 25.946 68.867 -19.510 1.00 29.62 ATOM 818 CG1 VAL A 116 25.479 70.293 -19.652 1.00 29.79 ATOM 819 CG2 VAL A 116 25.636 68.102 -20.793 1.00 30.72 ATOM 820 N LEU A 117 28.600 70.205 -17.611 1.00 30.29 ATOM 821 CA LEU A 117 29.021 70.664 -16.285 1.00 30.02 ATOM 822 C LEU A 117 28.991 72.211 -16.238 1.00 31.55 ATOM 823 O LEU A 117 28.115 72.739 -15.535 1.00 32.99 ATOM 824 CB LEU A 117 30.402 70.080 -15.927 1.00 27.75 ATOM 825 CG LEU A 117 31.582 70.437 -16.806 1.00 25.62 ATOM 826 CD1 LEU A 117 32.102 71.840 -16.433 1.00 25.56 ATOM 827 CD2 LEU A 117 32.699 69.428 -16.689 1.00 25.18 ATOM 828 OXT LEU A 117 29.765 72.971 -16.897 1.00 32.42 ATOM 830 N SER B 2 -12.922 87.868 -57.323 1.00 49.46 ATOM 831 CA SER B 2 -11.806 87.540 -56.402 1.00 48.79 ATOM 832 C SER B 2 -12.055 86.351 -55.422 1.00 49.31 ATOM 833 O SER B 2 -13.190 85.844 -55.322 1.00 48.83 ATOM 834 CB SER B 2 -11.469 88.790 -55.623 1.00 48.77 ATOM 835 OG SER B 2 -10.170 88.647 -55.125 1.00 48.31 ATOM 836 N GLN B 3 -10.986 85.888 -54.740 1.00 49.19 ATOM 837 CA GLN B 3 -11.064 84.920 -53.596 1.00 48.86 ATOM 838 C GLN B 3 -11.487 85.698 -52.298 1.00 49.55 ATOM 839 O GLN B 3 -10.695 86.513 -51.788 1.00 50.05 ATOM 840 CB GLN B 3 -9.707 84.192 -53.388 1.00 48.33 ATOM 841 CG GLN B 3 -9.746 82.913 -52.500 1.00 47.69 ATOM 842 CD GLN B 3 -8.367 82.248 -52.242 1.00 46.58 ATOM 843 OE1 GLN B 3 -8.265 81.026 -52.113 1.00 42.58 ATOM 844 NE2 GLN B 3 -7.321 83.060 -52.145 1.00 42.62 ATOM 845 N PRO B 4 -12.730 85.463 -51.772 1.00 49.48 ATOM 846 CA PRO B 4 -13.194 86.135 -50.554 1.00 49.75 ATOM 847 C PRO B 4 -12.220 85.975 -49.369 1.00 49.79 ATOM 848 O PRO B 4 -11.565 84.909 -49.257 1.00 50.72 ATOM 849 CB PRO B 4 -14.531 85.438 -50.253 1.00 49.38 ATOM 850 CG PRO B 4 -14.546 84.264 -51.047 1.00 49.06 ATOM 851 CD PRO B 4 -13.771 84.553 -52.267 1.00 49.45 ATOM 852 N ASP B 5 -12.093 87.039 -48.555 1.00 48.69 ATOM 853 CA ASP B 5 -11.260 87.080 -47.343 1.00 47.45 ATOM 854 C ASP B 5 -11.474 85.845 -46.457 1.00 47.10 ATOM 855 O ASP B 5 -12.635 85.374 -46.332 1.00 48.05 ATOM 856 CB ASP B 5 -11.551 88.375 -46.572 1.00 48.22 ATOM 857 CG ASP B 5 -10.393 89.390 -46.650 1.00 47.87 ATOM 858 OD1 ASP B 5 -10.500 90.526 -46.098 1.00 46.94 ATOM 859 OD2 ASP B 5 -9.356 89.014 -47.235 1.00 47.90 ATOM 860 N PRO B 6 -10.389 85.287 -45.865 1.00 45.35 ATOM 861 CA PRO B 6 -10.480 83.963 -45.209 1.00 44.40 ATOM 862 C PRO B 6 -11.416 84.024 -44.032 1.00 43.68 ATOM 863 O PRO B 6 -11.791 85.140 -43.617 1.00 43.26 ATOM 864 CB PRO B 6 -9.066 83.745 -44.672 1.00 44.87 ATOM 865 CG PRO B 6 -8.463 85.182 -44.538 1.00 45.39 ATOM 866 CD PRO B 6 -9.042 85.878 -45.734 1.00 45.51 ATOM 867 N MET B 7 -11.766 82.859 -43.482 1.00 43.29 ATOM 868 CA MET B 7 -12.558 82.791 -42.235 1.00 43.42 ATOM 869 C MET B 7 -11.817 82.205 -41.022 1.00 41.64 ATOM 870 O MET B 7 -11.003 81.338 -41.176 1.00 41.74 ATOM 871 CB MET B 7 -13.867 82.057 -42.472 1.00 43.12 ATOM 872 CG MET B 7 -14.881 82.876 -43.309 1.00 44.63 ATOM 873 SD MET B 7 -16.391 82.001 -43.780 1.00 46.00 ATOM 874 CE MET B 7 -16.086 81.536 -45.474 1.00 45.38 ATOM 875 N PRO B 8 -12.075 82.739 -39.824 1.00 40.58 ATOM 876 CA PRO B 8 -11.602 82.269 -38.537 1.00 39.41 ATOM 877 C PRO B 8 -11.354 80.759 -38.486 1.00 39.14 ATOM 878 O PRO B 8 -10.205 80.297 -38.461 1.00 35.97 ATOM 879 CB PRO B 8 -12.769 82.608 -37.614 1.00 40.15 ATOM 880 CG PRO B 8 -13.805 83.511 -38.512 1.00 41.93 ATOM 881 CD PRO B 8 -12.897 83.954 -39.673 1.00 40.17 ATOM 882 N ASP B 9 -12.459 80.012 -38.473 1.00 37.97 ATOM 883 CA ASP B 9 -12.404 78.567 -38.416 1.00 37.87 ATOM 884 C ASP B 9 -12.072 78.072 -39.838 1.00 35.74 ATOM 885 O ASP B 9 -12.058 76.906 -40.113 1.00 36.24 ATOM 886 CB ASP B 9 -13.761 78.077 -37.934 1.00 37.93 ATOM 887 CG ASP B 9 -14.883 78.722 -38.711 1.00 41.67 ATOM 888 OD1 ASP B 9 -15.393 79.807 -38.263 1.00 38.95 ATOM 889 OD2 ASP B 9 -15.217 78.135 -39.790 1.00 43.48 ATOM 890 N ASP B 10 -11.808 78.983 -40.757 1.00 34.01 ATOM 891 CA ASP B 10 -11.432 78.587 -42.104 1.00 31.00 ATOM 892 C ASP B 10 -9.941 78.590 -42.281 1.00 28.13 ATOM 893 O ASP B 10 -9.442 78.366 -43.405 1.00 27.56 ATOM 894 CB ASP B 10 -12.089 79.467 -43.162 1.00 31.03 ATOM 895 CG ASP B 10 -13.537 79.031 -43.497 1.00 34.41 ATOM 896 OD1 ASP B 10 -14.481 79.227 -42.651 1.00 34.30 ATOM 897 OD2 ASP B 10 -13.741 78.495 -44.632 1.00 35.04 ATOM 898 N LEU B 11 -9.251 78.865 -41.178 1.00 25.86 ATOM 899 CA LEU B 11 -7.741 78.964 -41.092 1.00 23.56 ATOM 900 C LEU B 11 -7.166 77.868 -40.181 1.00 23.57 ATOM 901 O LEU B 11 -7.882 77.367 -39.268 1.00 26.01 ATOM 902 CB LEU B 11 -7.290 80.355 -40.609 1.00 20.63 ATOM 903 CG LEU B 11 -7.653 81.528 -41.534 1.00 18.00 ATOM 904 CD1 LEU B 11 -7.544 82.846 -40.865 1.00 12.99 ATOM 905 CD2 LEU B 11 -6.781 81.594 -42.784 1.00 13.84 ATOM 906 N HIS B 12 -5.936 77.438 -40.442 1.00 21.48 ATOM 907 CA HIS B 12 -5.348 76.332 -39.727 1.00 20.33 ATOM 908 C HIS B 12 -4.675 76.904 -38.512 1.00 21.48 ATOM 909 O HIS B 12 -4.085 78.055 -38.515 1.00 25.05 ATOM 910 CB HIS B 12 -4.281 75.644 -40.576 1.00 20.41 ATOM 911 CG HIS B 12 -4.804 74.672 -41.605 1.00 17.84 ATOM 912 ND1 HIS B 12 -3.961 73.932 -42.413 1.00 16.88 ATOM 913 CD2 HIS B 12 -6.056 74.271 -41.914 1.00 14.19 ATOM 914 CE1 HIS B 12 -4.680 73.127 -43.182 1.00 19.53 ATOM 915 NE2 HIS B 12 -5.958 73.341 -42.930 1.00 11.77 ATOM 916 N LYS B 13 -4.684 76.094 -37.478 1.00 19.87 ATOM 917 CA LYS B 13 -4.274 76.539 -36.217 1.00 15.64 ATOM 918 C LYS B 13 -3.105 75.722 -35.836 1.00 14.91 ATOM 919 O LYS B 13 -3.162 74.456 -35.690 1.00 12.68 ATOM 920 CB LYS B 13 -5.357 76.258 -35.218 1.00 16.55 ATOM 921 CG LYS B 13 -6.629 77.068 -35.451 1.00 18.23 ATOM 922 CD LYS B 13 -7.676 76.703 -34.429 1.00 17.83 ATOM 923 CE LYS B 13 -9.096 77.253 -34.794 1.00 17.38 ATOM 924 NZ LYS B 13 -9.703 76.685 -36.027 1.00 19.74 ATOM 925 N SER B 14 -2.080 76.493 -35.533 1.00 9.93 ATOM 926 CA SER B 14 -0.873 76.010 -34.961 1.00 7.98 ATOM 927 C SER B 14 -1.060 75.122 -33.772 1.00 8.16 ATOM 928 O SER B 14 -0.506 74.034 -33.780 1.00 7.79 ATOM 929 CB SER B 14 -0.015 77.203 -34.554 1.00 7.92 ATOM 930 OG SER B 14 1.229 76.758 -34.063 1.00 11.22 ATOM 931 N SER B 15 -1.772 75.606 -32.717 1.00 9.50 ATOM 932 CA SER B 15 -2.182 74.794 -31.569 1.00 8.75 ATOM 933 C SER B 15 -2.690 73.367 -31.957 1.00 7.50 ATOM 934 O SER B 15 -2.784 72.491 -31.119 1.00 2.00 ATOM 935 CB SER B 15 -3.361 75.457 -30.840 1.00 10.06 ATOM 936 OG SER B 15 -4.501 75.523 -31.686 1.00 11.48 ATOM 937 N GLU B 16 -3.118 73.202 -33.202 1.00 8.28 ATOM 938 CA GLU B 16 -3.663 71.873 -33.584 1.00 8.32 ATOM 939 C GLU B 16 -2.693 70.973 -34.283 1.00 7.34 ATOM 940 O GLU B 16 -3.077 69.906 -34.819 1.00 9.72 ATOM 941 CB GLU B 16 -4.940 71.972 -34.384 1.00 6.90 ATOM 942 CG GLU B 16 -6.110 72.774 -33.611 1.00 13.03 ATOM 943 CD GLU B 16 -7.082 73.426 -34.592 1.00 15.44 ATOM 944 OE1 GLU B 16 -8.246 73.802 -34.204 1.00 14.49 ATOM 945 OE2 GLU B 16 -6.693 73.489 -35.802 1.00 15.33 ATOM 946 N PHE B 17 -1.447 71.346 -34.309 1.00 5.54 ATOM 947 CA PHE B 17 -0.477 70.537 -35.005 1.00 8.01 ATOM 948 C PHE B 17 0.634 70.002 -34.046 1.00 8.60 ATOM 949 O PHE B 17 1.639 70.697 -33.698 1.00 10.83 ATOM 950 CB PHE B 17 0.093 71.335 -36.173 1.00 9.38 ATOM 951 CG PHE B 17 1.388 70.796 -36.738 1.00 8.94 ATOM 952 CD1 PHE B 17 1.406 69.702 -37.581 1.00 8.04 ATOM 953 CD2 PHE B 17 2.592 71.437 -36.481 1.00 13.11 ATOM 954 CE1 PHE B 17 2.597 69.272 -38.139 1.00 3.89 ATOM 955 CE2 PHE B 17 3.797 70.956 -37.026 1.00 4.66 ATOM 956 CZ PHE B 17 3.789 69.927 -37.838 1.00 6.54 ATOM 957 N THR B 18 0.463 68.752 -33.636 1.00 5.37 ATOM 958 CA THR B 18 1.315 68.198 -32.667 1.00 5.33 ATOM 959 C THR B 18 2.629 67.818 -33.297 1.00 4.69 ATOM 960 O THR B 18 3.511 67.445 -32.597 1.00 4.77 ATOM 961 CB THR B 18 0.720 66.955 -32.010 1.00 6.54 ATOM 962 OG1 THR B 18 1.465 65.775 -32.431 1.00 3.09 ATOM 963 CG2 THR B 18 -0.787 66.747 -32.453 1.00 6.57 ATOM 964 N GLY B 19 2.715 68.028 -34.598 1.00 5.78 ATOM 965 CA GLY B 19 3.820 67.641 -35.507 1.00 6.84 ATOM 966 C GLY B 19 5.073 68.363 -35.118 1.00 8.48 ATOM 967 O GLY B 19 5.154 68.776 -33.959 1.00 10.21 ATOM 968 N THR B 20 6.004 68.575 -36.076 1.00 8.52 ATOM 969 CA THR B 20 7.187 69.354 -35.838 1.00 6.10 ATOM 970 C THR B 20 7.286 70.595 -36.787 1.00 4.47 ATOM 971 O THR B 20 7.777 70.493 -37.870 1.00 7.92 ATOM 972 CB THR B 20 8.422 68.486 -36.181 1.00 7.30 ATOM 973 OG1 THR B 20 8.455 67.268 -35.411 1.00 4.45 ATOM 974 CG2 THR B 20 9.736 69.308 -35.881 1.00 5.58 ATOM 975 N MET B 21 6.923 71.806 -36.425 1.00 7.84 ATOM 976 CA MET B 21 6.991 72.951 -37.374 1.00 6.25 ATOM 977 C MET B 21 8.347 73.215 -38.035 1.00 6.67 ATOM 978 O MET B 21 8.460 74.145 -38.823 1.00 9.47 ATOM 979 CB MET B 21 6.533 74.221 -36.666 1.00 9.03 ATOM 980 CG MET B 21 6.240 75.448 -37.531 1.00 2.99 ATOM 981 SD MET B 21 4.679 75.068 -38.286 1.00 12.32 ATOM 982 CE MET B 21 3.576 75.454 -36.948 1.00 2.00 ATOM 983 N GLY B 22 9.354 72.348 -37.848 1.00 5.67 ATOM 984 CA GLY B 22 10.657 72.569 -38.394 1.00 5.46 ATOM 985 C GLY B 22 10.691 72.137 -39.819 1.00 5.45 ATOM 986 O GLY B 22 11.374 72.766 -40.666 1.00 4.30 ATOM 987 N ASN B 23 9.894 71.108 -40.152 1.00 4.03 ATOM 988 CA ASN B 23 9.755 70.722 -41.544 1.00 2.32 ATOM 989 C ASN B 23 9.094 71.790 -42.450 1.00 3.97 ATOM 990 O ASN B 23 9.135 71.699 -43.717 1.00 4.25 ATOM 991 CB ASN B 23 8.988 69.480 -41.632 1.00 3.48 ATOM 992 CG ASN B 23 9.503 68.445 -40.683 1.00 4.51 ATOM 993 OD1 ASN B 23 8.951 67.398 -40.603 1.00 2.00 ATOM 994 ND2 ASN B 23 10.684 68.724 -40.048 1.00 8.89 ATOM 995 N MET B 24 8.413 72.746 -41.824 1.00 4.15 ATOM 996 CA MET B 24 7.869 73.871 -42.604 1.00 6.07 ATOM 997 C MET B 24 8.935 74.946 -42.606 1.00 8.10 ATOM 998 O MET B 24 9.056 75.652 -43.569 1.00 11.97 ATOM 999 CB MET B 24 6.585 74.375 -41.946 1.00 5.93 ATOM 1000 CG MET B 24 6.282 75.875 -42.155 1.00 6.16 ATOM 1001 SD MET B 24 5.399 76.020 -43.732 1.00 11.88 ATOM 1002 CE MET B 24 4.033 74.884 -43.653 1.00 12.63 ATOM 1003 N LYS B 25 9.591 75.196 -41.477 1.00 9.51 ATOM 1004 CA LYS B 25 10.632 76.225 -41.474 1.00 12.64 ATOM 1005 C LYS B 25 11.555 75.823 -42.623 1.00 12.16 ATOM 1006 O LYS B 25 11.972 76.666 -43.399 1.00 10.17 ATOM 1007 CB LYS B 25 11.449 76.210 -40.172 1.00 11.58 ATOM 1008 CG LYS B 25 12.314 77.417 -39.928 1.00 13.23 ATOM 1009 CD LYS B 25 13.033 77.369 -38.536 1.00 12.03 ATOM 1010 CE LYS B 25 14.389 78.062 -38.522 1.00 11.09 ATOM 1011 NZ LYS B 25 14.975 78.650 -37.246 1.00 9.14 ATOM 1012 N TYR B 26 11.729 74.508 -42.790 1.00 12.78 ATOM 1013 CA TYR B 26 12.779 73.942 -43.671 1.00 13.08 ATOM 1014 C TYR B 26 12.727 74.501 -45.052 1.00 14.82 ATOM 1015 O TYR B 26 13.768 74.870 -45.606 1.00 16.26 ATOM 1016 CB TYR B 26 12.662 72.412 -43.825 1.00 15.17 ATOM 1017 CG TYR B 26 13.626 71.883 -44.844 1.00 16.72 ATOM 1018 CD1 TYR B 26 14.993 72.051 -44.706 1.00 16.69 ATOM 1019 CD2 TYR B 26 13.154 71.284 -45.989 1.00 22.97 ATOM 1020 CE1 TYR B 26 15.922 71.599 -45.696 1.00 17.03 ATOM 1021 CE2 TYR B 26 14.042 70.807 -46.984 1.00 21.75 ATOM 1022 CZ TYR B 26 15.423 71.017 -46.822 1.00 20.28 ATOM 1023 OH TYR B 26 16.212 70.601 -47.826 1.00 22.50 ATOM 1024 N LEU B 27 11.513 74.577 -45.606 1.00 15.13 ATOM 1025 CA LEU B 27 11.258 74.998 -46.969 1.00 11.75 ATOM 1026 C LEU B 27 11.462 76.511 -47.238 1.00 12.61 ATOM 1027 O LEU B 27 11.363 76.924 -48.416 1.00 13.55 ATOM 1028 CB LEU B 27 9.793 74.655 -47.240 1.00 11.96 ATOM 1029 CG LEU B 27 9.249 73.293 -46.797 1.00 10.71 ATOM 1030 CD1 LEU B 27 7.846 73.236 -47.184 1.00 8.09 ATOM 1031 CD2 LEU B 27 10.048 72.234 -47.482 1.00 10.20 ATOM 1032 N TYR B 28 11.605 77.351 -46.192 1.00 10.51 ATOM 1033 CA TYR B 28 11.910 78.786 -46.430 1.00 12.26 ATOM 1034 C TYR B 28 13.061 79.521 -45.738 1.00 9.88 ATOM 1035 O TYR B 28 13.247 80.680 -45.994 1.00 9.05 ATOM 1036 CB TYR B 28 10.688 79.632 -46.251 1.00 12.47 ATOM 1037 CG TYR B 28 9.486 79.043 -46.815 1.00 16.52 ATOM 1038 CD1 TYR B 28 9.009 77.837 -46.342 1.00 17.14 ATOM 1039 CD2 TYR B 28 8.708 79.739 -47.700 1.00 17.99 ATOM 1040 CE1 TYR B 28 7.896 77.325 -46.807 1.00 19.39 ATOM 1041 CE2 TYR B 28 7.536 79.196 -48.149 1.00 18.75 ATOM 1042 CZ TYR B 28 7.138 78.013 -47.697 1.00 14.71 ATOM 1043 OH TYR B 28 5.988 77.435 -48.151 1.00 18.96 ATOM 1044 N ASP B 29 13.834 78.889 -44.865 1.00 11.42 ATOM 1045 CA ASP B 29 15.039 79.582 -44.329 1.00 12.07 ATOM 1046 C ASP B 29 16.120 79.506 -45.382 1.00 12.70 ATOM 1047 O ASP B 29 16.874 78.462 -45.477 1.00 13.45 ATOM 1048 CB ASP B 29 15.478 79.013 -42.972 1.00 12.05 ATOM 1049 CG ASP B 29 16.523 79.893 -42.233 1.00 20.40 ATOM 1050 OD1 ASP B 29 16.977 79.436 -41.118 1.00 25.56 ATOM 1051 OD2 ASP B 29 16.891 81.035 -42.722 1.00 21.98 ATOM 1052 N ASP B 30 16.145 80.510 -46.279 1.00 10.97 ATOM 1053 CA ASP B 30 17.227 80.571 -47.304 1.00 12.51 ATOM 1054 C ASP B 30 17.311 79.226 -48.096 1.00 13.06 ATOM 1055 O ASP B 30 18.435 78.724 -48.297 1.00 12.50 ATOM 1056 CB ASP B 30 18.607 80.840 -46.658 1.00 12.06 ATOM 1057 CG ASP B 30 19.697 81.234 -47.696 1.00 17.11 ATOM 1058 OD1 ASP B 30 19.489 82.195 -48.463 1.00 15.72 ATOM 1059 OD2 ASP B 30 20.774 80.600 -47.724 1.00 14.13 ATOM 1060 N HIS B 31 16.132 78.730 -48.546 1.00 9.50 ATOM 1061 CA HIS B 31 15.966 77.483 -49.319 1.00 11.12 ATOM 1062 C HIS B 31 15.071 77.866 -50.454 1.00 11.29 ATOM 1063 O HIS B 31 13.974 78.366 -50.185 1.00 16.56 ATOM 1064 CB HIS B 31 15.131 76.527 -48.447 1.00 9.99 ATOM 1065 CG HIS B 31 14.696 75.288 -49.095 1.00 7.73 ATOM 1066 ND1 HIS B 31 15.545 74.224 -49.295 1.00 2.00 ATOM 1067 CD2 HIS B 31 13.465 74.898 -49.547 1.00 14.99 ATOM 1068 CE1 HIS B 31 14.855 73.229 -49.825 1.00 11.39 ATOM 1069 NE2 HIS B 31 13.587 73.591 -49.959 1.00 5.47 ATOM 1070 N TYR B 32 15.557 77.760 -51.681 1.00 11.92 ATOM 1071 CA TYR B 32 14.771 77.896 -52.927 1.00 12.20 ATOM 1072 C TYR B 32 15.646 77.342 -54.070 1.00 12.61 ATOM 1073 O TYR B 32 16.857 77.145 -53.874 1.00 10.79 ATOM 1074 CB TYR B 32 14.534 79.343 -53.236 1.00 12.35 ATOM 1075 CG TYR B 32 15.805 80.063 -53.151 1.00 12.45 ATOM 1076 CD1 TYR B 32 16.803 79.780 -54.022 1.00 7.96 ATOM 1077 CD2 TYR B 32 16.029 81.005 -52.146 1.00 10.10 ATOM 1078 CE1 TYR B 32 18.015 80.430 -53.913 1.00 11.27 ATOM 1079 CE2 TYR B 32 17.196 81.659 -52.046 1.00 11.49 ATOM 1080 CZ TYR B 32 18.206 81.364 -52.904 1.00 13.57 ATOM 1081 OH TYR B 32 19.445 81.985 -52.705 1.00 15.12 ATOM 1082 N VAL B 33 15.053 77.207 -55.268 1.00 9.92 ATOM 1083 CA VAL B 33 15.792 76.815 -56.413 1.00 7.41 ATOM 1084 C VAL B 33 15.738 77.982 -57.313 1.00 9.49 ATOM 1085 O VAL B 33 14.617 78.528 -57.530 1.00 7.51 ATOM 1086 CB VAL B 33 15.069 75.631 -57.030 1.00 7.08 ATOM 1087 CG1 VAL B 33 15.556 75.285 -58.414 1.00 2.45 ATOM 1088 CG2 VAL B 33 15.150 74.529 -56.135 1.00 5.59 ATOM 1089 N SER B 34 16.898 78.390 -57.879 1.00 8.50 ATOM 1090 CA SER B 34 16.866 79.564 -58.721 1.00 9.28 ATOM 1091 C SER B 34 17.727 79.393 -59.896 1.00 10.37 ATOM 1092 O SER B 34 18.939 79.451 -59.788 1.00 14.13 ATOM 1093 CB SER B 34 17.181 80.861 -58.005 1.00 10.40 ATOM 1094 OG SER B 34 16.973 81.971 -58.909 1.00 9.49 ATOM 1095 N ALA B 35 17.098 79.261 -61.062 1.00 11.32 ATOM 1096 CA ALA B 35 17.828 79.044 -62.324 1.00 9.78 ATOM 1097 C ALA B 35 17.370 80.112 -63.260 1.00 8.82 ATOM 1098 O ALA B 35 16.275 80.511 -63.151 1.00 6.77 ATOM 1099 CB ALA B 35 17.474 77.737 -62.932 1.00 9.96 ATOM 1100 N THR B 36 18.220 80.489 -64.208 1.00 10.12 ATOM 1101 CA THR B 36 18.011 81.657 -65.118 1.00 11.05 ATOM 1102 C THR B 36 18.294 81.320 -66.544 1.00 12.61 ATOM 1103 O THR B 36 19.354 80.861 -66.853 1.00 10.92 ATOM 1104 CB THR B 36 18.942 82.743 -64.777 1.00 11.66 ATOM 1105 OG1 THR B 36 18.747 82.955 -63.382 1.00 15.75 ATOM 1106 CG2 THR B 36 18.594 84.074 -65.630 1.00 11.27 ATOM 1107 N LYS B 37 17.296 81.531 -67.430 1.00 14.89 ATOM 1108 CA LYS B 37 17.543 81.310 -68.814 1.00 13.99 ATOM 1109 C LYS B 37 17.984 79.844 -68.958 1.00 14.22 ATOM 1110 O LYS B 37 19.196 79.574 -69.047 1.00 11.92 ATOM 1111 CB LYS B 37 18.653 82.324 -69.197 1.00 14.69 ATOM 1112 CG LYS B 37 19.098 82.350 -70.666 1.00 14.92 ATOM 1113 CD LYS B 37 20.481 83.023 -70.818 1.00 15.90 ATOM 1114 CE LYS B 37 21.493 82.531 -69.826 1.00 18.89 ATOM 1115 NZ LYS B 37 22.701 83.497 -70.086 1.00 25.94 ATOM 1116 N VAL B 38 17.018 78.889 -68.941 1.00 14.33 ATOM 1117 CA VAL B 38 17.333 77.460 -69.217 1.00 8.47 ATOM 1118 C VAL B 38 16.156 76.741 -69.917 1.00 11.64 ATOM 1119 O VAL B 38 15.036 77.291 -70.018 1.00 11.70 ATOM 1120 CB VAL B 38 17.549 76.692 -67.969 1.00 9.41 ATOM 1121 CG1 VAL B 38 18.761 77.135 -67.216 1.00 5.49 ATOM 1122 CG2 VAL B 38 16.192 76.623 -66.976 1.00 3.34 ATOM 1123 N LYS B 39 16.348 75.481 -70.341 1.00 8.26 ATOM 1124 CA LYS B 39 15.260 74.869 -70.996 1.00 7.03 ATOM 1125 C LYS B 39 15.158 73.459 -70.546 1.00 7.23 ATOM 1126 O LYS B 39 16.188 72.769 -70.251 1.00 4.87 ATOM 1127 CB LYS B 39 15.431 74.849 -72.513 1.00 8.92 ATOM 1128 CG LYS B 39 14.042 74.528 -73.349 1.00 8.95 ATOM 1129 CD LYS B 39 14.417 74.176 -74.848 1.00 5.73 ATOM 1130 CE LYS B 39 15.312 75.405 -75.341 1.00 11.99 ATOM 1131 NZ LYS B 39 15.446 75.446 -76.803 1.00 16.06 ATOM 1132 N SER B 40 13.887 73.080 -70.432 1.00 4.91 ATOM 1133 CA SER B 40 13.521 71.755 -69.977 1.00 6.31 ATOM 1134 C SER B 40 14.456 70.798 -70.680 1.00 4.19 ATOM 1135 O SER B 40 14.844 71.105 -71.730 1.00 7.46 ATOM 1136 CB SER B 40 12.115 71.366 -70.441 1.00 3.16 ATOM 1137 OG SER B 40 12.137 69.930 -70.572 1.00 4.42 ATOM 1138 N VAL B 41 14.734 69.669 -70.124 1.00 4.68 ATOM 1139 CA VAL B 41 15.584 68.637 -70.775 1.00 5.16 ATOM 1140 C VAL B 41 15.081 67.212 -70.608 1.00 6.17 ATOM 1141 O VAL B 41 15.809 66.230 -70.835 1.00 8.77 ATOM 1142 CB VAL B 41 16.973 68.667 -70.217 1.00 3.62 ATOM 1143 CG1 VAL B 41 17.543 70.203 -70.141 1.00 2.00 ATOM 1144 CG2 VAL B 41 16.981 68.059 -68.909 1.00 2.37 ATOM 1145 N ASP B 42 13.868 67.049 -70.145 1.00 7.39 ATOM 1146 CA ASP B 42 13.306 65.666 -70.092 1.00 9.19 ATOM 1147 C ASP B 42 11.941 65.741 -69.522 1.00 8.29 ATOM 1148 O ASP B 42 11.325 66.848 -69.425 1.00 9.02 ATOM 1149 CB ASP B 42 14.161 64.741 -69.201 1.00 8.49 ATOM 1150 CG ASP B 42 13.714 63.283 -69.281 1.00 12.22 ATOM 1151 OD1 ASP B 42 14.480 62.410 -68.854 1.00 9.11 ATOM 1152 OD2 ASP B 42 12.595 62.983 -69.819 1.00 14.09 ATOM 1153 N LYS B 43 11.473 64.586 -69.038 1.00 8.95 ATOM 1154 CA LYS B 43 10.139 64.519 -68.495 1.00 7.59 ATOM 1155 C LYS B 43 9.684 63.146 -68.063 1.00 10.74 ATOM 1156 O LYS B 43 10.015 62.135 -68.714 1.00 10.33 ATOM 1157 CB LYS B 43 9.253 65.059 -69.569 1.00 5.57 ATOM 1158 CG LYS B 43 7.828 64.484 -69.586 1.00 10.36 ATOM 1159 CD LYS B 43 6.985 64.859 -70.881 1.00 3.92 ATOM 1160 CE LYS B 43 6.779 66.394 -71.226 1.00 11.54 ATOM 1161 NZ LYS B 43 5.771 67.268 -70.464 1.00 12.95 ATOM 1162 N PHE B 44 8.899 63.089 -66.973 1.00 13.77 ATOM 1163 CA PHE B 44 8.231 61.846 -66.431 1.00 13.20 ATOM 1164 C PHE B 44 6.713 61.771 -66.767 1.00 13.65 ATOM 1165 O PHE B 44 6.333 61.164 -67.764 1.00 14.30 ATOM 1166 CB PHE B 44 8.265 61.820 -64.913 1.00 15.36 ATOM 1167 CG PHE B 44 7.633 60.568 -64.303 1.00 18.19 ATOM 1168 CD1 PHE B 44 7.180 60.562 -63.004 1.00 25.22 ATOM 1169 CD2 PHE B 44 7.398 59.431 -65.070 1.00 23.88 ATOM 1170 CE1 PHE B 44 6.605 59.390 -62.409 1.00 26.02 ATOM 1171 CE2 PHE B 44 6.800 58.257 -64.475 1.00 24.48 ATOM 1172 CZ PHE B 44 6.431 58.275 -63.141 1.00 25.14 ATOM 1173 N LEU B 45 5.846 62.308 -65.937 1.00 10.95 ATOM 1174 CA LEU B 45 4.420 62.211 -66.290 1.00 13.95 ATOM 1175 C LEU B 45 4.007 63.403 -67.129 1.00 13.43 ATOM 1176 O LEU B 45 4.714 64.387 -67.080 1.00 13.44 ATOM 1177 CB LEU B 45 3.533 62.034 -65.052 1.00 12.98 ATOM 1178 CG LEU B 45 3.491 60.557 -64.573 1.00 17.93 ATOM 1179 CD1 LEU B 45 2.605 60.444 -63.348 1.00 15.62 ATOM 1180 CD2 LEU B 45 2.989 59.653 -65.701 1.00 18.26 ATOM 1181 N ALA B 46 2.807 63.332 -67.766 1.00 15.53 ATOM 1182 CA ALA B 46 2.294 64.222 -68.816 1.00 13.36 ATOM 1183 C ALA B 46 2.261 65.697 -68.384 1.00 14.37 ATOM 1184 O ALA B 46 1.548 66.560 -68.990 1.00 16.33 ATOM 1185 CB ALA B 46 0.974 63.805 -69.171 1.00 15.72 ATOM 1186 N HIS B 47 2.986 65.981 -67.335 1.00 11.62 ATOM 1187 CA HIS B 47 2.946 67.269 -66.763 1.00 12.15 ATOM 1188 C HIS B 47 4.089 67.604 -65.841 1.00 12.13 ATOM 1189 O HIS B 47 3.843 68.485 -65.023 1.00 16.78 ATOM 1190 CB HIS B 47 1.627 67.475 -65.997 1.00 11.30 ATOM 1191 CG HIS B 47 1.524 66.644 -64.769 1.00 8.04 ATOM 1192 ND1 HIS B 47 1.415 65.265 -64.818 1.00 11.28 ATOM 1193 CD2 HIS B 47 1.572 66.966 -63.462 1.00 9.91 ATOM 1194 CE1 HIS B 47 1.331 64.779 -63.591 1.00 12.14 ATOM 1195 NE2 HIS B 47 1.447 65.780 -62.744 1.00 11.10 ATOM 1196 N ASP B 48 5.329 67.095 -66.039 1.00 10.44 ATOM 1197 CA ASP B 48 6.482 67.608 -65.281 1.00 10.07 ATOM 1198 C ASP B 48 7.732 67.723 -66.130 1.00 11.73 ATOM 1199 O ASP B 48 8.044 66.806 -66.774 1.00 12.14 ATOM 1200 CB ASP B 48 6.804 66.628 -64.196 1.00 10.01 ATOM 1201 CG ASP B 48 7.151 65.308 -64.774 1.00 12.06 ATOM 1202 OD1 ASP B 48 6.255 64.716 -65.450 1.00 16.00 ATOM 1203 OD2 ASP B 48 8.334 64.933 -64.674 1.00 10.05 ATOM 1204 N LEU B 49 8.419 68.874 -66.147 1.00 14.01 ATOM 1205 CA LEU B 49 9.622 69.109 -66.936 1.00 11.39 ATOM 1206 C LEU B 49 10.864 69.134 -66.050 1.00 10.43 ATOM 1207 O LEU B 49 10.920 69.975 -65.207 1.00 8.63 ATOM 1208 CB LEU B 49 9.471 70.402 -67.733 1.00 14.66 ATOM 1209 CG LEU B 49 7.996 70.851 -67.931 1.00 11.19 ATOM 1210 CD1 LEU B 49 8.099 72.163 -68.333 1.00 10.92 ATOM 1211 CD2 LEU B 49 7.245 70.080 -68.995 1.00 11.02 ATOM 1212 N ILE B 50 11.770 68.146 -66.209 1.00 8.25 ATOM 1213 CA ILE B 50 13.045 68.051 -65.544 1.00 9.33 ATOM 1214 C ILE B 50 14.068 69.010 -66.171 1.00 10.09 ATOM 1215 O ILE B 50 14.155 69.097 -67.364 1.00 11.32 ATOM 1216 CB ILE B 50 13.693 66.661 -65.734 1.00 10.94 ATOM 1217 CG1 ILE B 50 12.772 65.492 -65.444 1.00 7.35 ATOM 1218 CG2 ILE B 50 15.055 66.522 -64.894 1.00 15.10 ATOM 1219 CD1 ILE B 50 12.196 65.557 -64.237 1.00 19.03 ATOM 1220 N TYR B 51 14.861 69.697 -65.394 1.00 10.16 ATOM 1221 CA TYR B 51 15.858 70.595 -65.925 1.00 10.62 ATOM 1222 C TYR B 51 17.190 70.100 -65.383 1.00 13.67 ATOM 1223 O TYR B 51 17.173 69.256 -64.457 1.00 13.15 ATOM 1224 CB TYR B 51 15.580 71.985 -65.381 1.00 9.74 ATOM 1225 CG TYR B 51 14.372 72.680 -66.007 1.00 4.41 ATOM 1226 CD1 TYR B 51 13.066 72.166 -65.865 1.00 9.42 ATOM 1227 CD2 TYR B 51 14.534 73.789 -66.752 1.00 2.00 ATOM 1228 CE1 TYR B 51 11.920 72.867 -66.435 1.00 3.76 ATOM 1229 CE2 TYR B 51 13.431 74.465 -67.376 1.00 3.37 ATOM 1230 CZ TYR B 51 12.132 73.991 -67.193 1.00 2.47 ATOM 1231 OH TYR B 51 11.103 74.610 -67.833 1.00 2.40 ATOM 1232 N ASN B 52 18.309 70.669 -65.826 1.00 11.97 ATOM 1233 CA ASN B 52 19.512 70.170 -65.302 1.00 16.18 ATOM 1234 C ASN B 52 20.011 71.357 -64.563 1.00 18.09 ATOM 1235 O ASN B 52 20.932 72.001 -65.058 1.00 16.56 ATOM 1236 CB ASN B 52 20.539 69.722 -66.381 1.00 14.82 ATOM 1237 CG ASN B 52 20.068 68.591 -67.201 1.00 18.24 ATOM 1238 OD1 ASN B 52 19.771 67.528 -66.662 1.00 22.02 ATOM 1239 ND2 ASN B 52 19.954 68.790 -68.538 1.00 15.48 ATOM 1240 N ILE B 53 19.397 71.620 -63.404 1.00 19.01 ATOM 1241 CA ILE B 53 19.784 72.713 -62.507 1.00 18.95 ATOM 1242 C ILE B 53 20.574 72.138 -61.328 1.00 19.83 ATOM 1243 O ILE B 53 20.063 71.356 -60.587 1.00 18.44 ATOM 1244 CB ILE B 53 18.514 73.413 -61.941 1.00 18.10 ATOM 1245 CG1 ILE B 53 17.650 74.111 -63.022 1.00 20.40 ATOM 1246 CG2 ILE B 53 18.850 74.429 -60.893 1.00 15.21 ATOM 1247 CD1 ILE B 53 18.495 74.743 -64.053 1.00 28.21 ATOM 1248 N SER B 54 21.773 72.639 -61.067 1.00 20.41 ATOM 1249 CA SER B 54 22.556 72.066 -59.997 1.00 19.93 ATOM 1250 C SER B 54 22.663 72.786 -58.690 1.00 21.74 ATOM 1251 O SER B 54 23.084 73.939 -58.644 1.00 22.49 ATOM 1252 CB SER B 54 24.016 71.951 -60.412 1.00 19.12 ATOM 1253 OG SER B 54 24.117 71.236 -61.577 1.00 19.90 ATOM 1254 N ASP B 55 22.484 72.032 -57.619 1.00 24.40 ATOM 1255 CA ASP B 55 22.631 72.525 -56.276 1.00 27.39 ATOM 1256 C ASP B 55 23.850 73.400 -56.170 1.00 28.79 ATOM 1257 O ASP B 55 24.937 72.900 -56.246 1.00 29.60 ATOM 1258 CB ASP B 55 22.775 71.310 -55.333 1.00 28.70 ATOM 1259 CG ASP B 55 22.622 71.670 -53.853 1.00 28.72 ATOM 1260 OD1 ASP B 55 22.728 70.776 -52.983 1.00 21.42 ATOM 1261 OD2 ASP B 55 22.423 72.871 -53.570 1.00 29.02 ATOM 1262 N LYS B 56 23.689 74.715 -55.947 1.00 30.83 ATOM 1263 CA LYS B 56 24.874 75.548 -55.684 1.00 30.73 ATOM 1264 C LYS B 56 25.373 75.552 -54.230 1.00 30.90 ATOM 1265 O LYS B 56 26.582 75.461 -53.950 1.00 32.61 ATOM 1266 CB LYS B 56 24.687 76.960 -56.247 1.00 31.60 ATOM 1267 CG LYS B 56 25.160 77.072 -57.720 1.00 32.82 ATOM 1268 CD LYS B 56 26.585 76.462 -57.886 1.00 37.24 ATOM 1269 CE LYS B 56 26.706 75.575 -59.119 1.00 35.70 ATOM 1270 NZ LYS B 56 26.428 76.315 -60.371 1.00 35.95 ATOM 1271 N LYS B 57 24.428 75.645 -53.310 1.00 31.60 ATOM 1272 CA LYS B 57 24.639 75.634 -51.870 1.00 31.24 ATOM 1273 C LYS B 57 25.322 74.360 -51.418 1.00 30.68 ATOM 1274 O LYS B 57 26.396 74.421 -50.916 1.00 28.36 ATOM 1275 CB LYS B 57 23.295 75.785 -51.152 1.00 31.97 ATOM 1276 CG LYS B 57 22.915 77.245 -50.724 1.00 33.43 ATOM 1277 CD LYS B 57 22.763 78.189 -51.967 1.00 38.46 ATOM 1278 CE LYS B 57 21.830 79.384 -51.702 1.00 38.33 ATOM 1279 NZ LYS B 57 20.614 78.991 -50.937 1.00 33.85 ATOM 1280 N LEU B 58 24.698 73.204 -51.613 1.00 31.37 ATOM 1281 CA LEU B 58 25.336 71.948 -51.168 1.00 31.93 ATOM 1282 C LEU B 58 25.752 71.059 -52.354 1.00 31.95 ATOM 1283 O LEU B 58 26.643 71.387 -53.145 1.00 32.26 ATOM 1284 CB LEU B 58 24.392 71.172 -50.259 1.00 32.96 ATOM 1285 CG LEU B 58 23.395 71.988 -49.404 1.00 32.02 ATOM 1286 CD1 LEU B 58 22.251 71.121 -48.917 1.00 36.53 ATOM 1287 CD2 LEU B 58 24.084 72.609 -48.210 1.00 34.80 ATOM 1288 N LYS B 59 25.098 69.921 -52.485 1.00 31.56 ATOM 1289 CA LYS B 59 25.498 68.925 -53.512 1.00 30.11 ATOM 1290 C LYS B 59 24.412 67.847 -53.648 1.00 27.60 ATOM 1291 O LYS B 59 24.633 66.702 -54.165 1.00 25.06 ATOM 1292 CB LYS B 59 26.889 68.313 -53.230 1.00 30.42 ATOM 1293 CG LYS B 59 27.120 67.821 -51.786 1.00 33.62 ATOM 1294 CD LYS B 59 28.487 67.027 -51.655 1.00 32.10 ATOM 1295 CE LYS B 59 28.596 66.317 -50.318 1.00 35.13 ATOM 1296 NZ LYS B 59 29.742 65.287 -50.286 1.00 37.19 ATOM 1297 N ASN B 60 23.215 68.265 -53.235 1.00 25.43 ATOM 1298 CA ASN B 60 22.065 67.375 -53.182 1.00 25.07 ATOM 1299 C ASN B 60 21.634 66.986 -54.603 1.00 23.02 ATOM 1300 O ASN B 60 21.571 65.851 -54.845 1.00 23.53 ATOM 1301 CB ASN B 60 20.943 67.975 -52.301 1.00 24.37 ATOM 1302 CG ASN B 60 21.513 68.539 -51.004 1.00 29.91 ATOM 1303 OD1 ASN B 60 22.355 67.865 -50.312 1.00 22.22 ATOM 1304 ND2 ASN B 60 21.158 69.825 -50.702 1.00 26.60 ATOM 1305 N TYR B 61 21.386 67.925 -55.539 1.00 22.28 ATOM 1306 CA TYR B 61 20.766 67.595 -56.850 1.00 21.25 ATOM 1307 C TYR B 61 21.603 68.088 -57.992 1.00 19.95 ATOM 1308 O TYR B 61 22.388 68.957 -57.803 1.00 22.42 ATOM 1309 CB TYR B 61 19.317 68.143 -56.927 1.00 20.47 ATOM 1310 CG TYR B 61 19.231 69.645 -56.725 1.00 22.50 ATOM 1311 CD1 TYR B 61 19.603 70.503 -57.744 1.00 17.96 ATOM 1312 CD2 TYR B 61 18.819 70.185 -55.508 1.00 22.53 ATOM 1313 CE1 TYR B 61 19.552 71.866 -57.543 1.00 21.42 ATOM 1314 CE2 TYR B 61 18.791 71.524 -55.288 1.00 18.08 ATOM 1315 CZ TYR B 61 19.175 72.338 -56.311 1.00 18.98 ATOM 1316 OH TYR B 61 19.158 73.620 -56.151 1.00 23.27 ATOM 1317 N ASP B 62 21.453 67.527 -59.165 1.00 18.98 ATOM 1318 CA ASP B 62 21.948 68.124 -60.410 1.00 18.61 ATOM 1319 C ASP B 62 20.707 68.334 -61.325 1.00 17.80 ATOM 1320 O ASP B 62 20.795 68.945 -62.349 1.00 17.30 ATOM 1321 CB ASP B 62 22.852 67.123 -61.091 1.00 19.51 ATOM 1322 CG ASP B 62 22.099 65.851 -61.414 1.00 18.23 ATOM 1323 OD1 ASP B 62 22.010 64.964 -60.565 1.00 16.70 ATOM 1324 OD2 ASP B 62 21.558 65.780 -62.505 1.00 24.79 ATOM 1325 N LYS B 63 19.526 67.848 -60.930 1.00 18.24 ATOM 1326 CA LYS B 63 18.277 67.989 -61.726 1.00 17.27 ATOM 1327 C LYS B 63 17.025 68.255 -60.877 1.00 16.44 ATOM 1328 O LYS B 63 17.022 68.000 -59.702 1.00 16.35 ATOM 1329 CB LYS B 63 18.004 66.723 -62.471 1.00 17.43 ATOM 1330 CG LYS B 63 18.989 66.354 -63.557 1.00 18.56 ATOM 1331 CD LYS B 63 18.273 65.328 -64.583 1.00 19.04 ATOM 1332 CE LYS B 63 19.232 64.535 -65.499 1.00 22.68 ATOM 1333 NZ LYS B 63 20.351 63.925 -64.725 1.00 20.82 ATOM 1334 N VAL B 64 15.956 68.762 -61.466 1.00 14.94 ATOM 1335 CA VAL B 64 14.918 69.428 -60.687 1.00 13.39 ATOM 1336 C VAL B 64 13.690 69.204 -61.470 1.00 14.07 ATOM 1337 O VAL B 64 13.659 69.610 -62.662 1.00 13.58 ATOM 1338 CB VAL B 64 15.129 70.881 -60.563 1.00 13.23 ATOM 1339 CG1 VAL B 64 14.106 71.459 -59.685 1.00 13.27 ATOM 1340 CG2 VAL B 64 16.539 71.163 -59.937 1.00 14.70 ATOM 1341 N LYS B 65 12.758 68.457 -60.862 1.00 11.22 ATOM 1342 CA LYS B 65 11.479 68.023 -61.513 1.00 10.59 ATOM 1343 C LYS B 65 10.399 68.943 -61.018 1.00 9.34 ATOM 1344 O LYS B 65 10.124 68.893 -59.864 1.00 10.41 ATOM 1345 CB LYS B 65 11.075 66.669 -61.027 1.00 9.02 ATOM 1346 CG LYS B 65 9.850 66.003 -61.721 1.00 12.54 ATOM 1347 CD LYS B 65 9.549 64.629 -60.972 1.00 10.08 ATOM 1348 CE LYS B 65 8.240 64.021 -61.369 1.00 15.90 ATOM 1349 NZ LYS B 65 6.934 64.371 -60.782 1.00 11.30 ATOM 1350 N THR B 66 9.829 69.785 -61.846 1.00 5.88 ATOM 1351 CA THR B 66 8.816 70.634 -61.359 1.00 7.32 ATOM 1352 C THR B 66 7.519 70.173 -61.946 1.00 6.50 ATOM 1353 O THR B 66 7.553 69.747 -63.109 1.00 7.78 ATOM 1354 CB THR B 66 8.992 72.105 -61.878 1.00 7.09 ATOM 1355 OG1 THR B 66 7.855 72.831 -61.412 1.00 8.11 ATOM 1356 CG2 THR B 66 8.875 72.163 -63.350 1.00 2.38 ATOM 1357 N GLU B 67 6.431 70.214 -61.200 1.00 4.69 ATOM 1358 CA GLU B 67 5.170 69.577 -61.684 1.00 7.90 ATOM 1359 C GLU B 67 4.184 70.675 -61.809 1.00 7.23 ATOM 1360 O GLU B 67 4.206 71.534 -60.958 1.00 10.86 ATOM 1361 CB GLU B 67 4.580 68.526 -60.696 1.00 7.73 ATOM 1362 CG GLU B 67 5.458 67.338 -60.426 1.00 8.95 ATOM 1363 CD GLU B 67 4.690 66.177 -59.888 1.00 11.55 ATOM 1364 OE1 GLU B 67 4.324 66.244 -58.729 1.00 16.77 ATOM 1365 OE2 GLU B 67 4.470 65.142 -60.591 1.00 16.26 ATOM 1366 N LEU B 68 3.365 70.693 -62.850 1.00 8.84 ATOM 1367 CA LEU B 68 2.462 71.833 -63.143 1.00 9.86 ATOM 1368 C LEU B 68 1.027 71.385 -62.992 1.00 10.53 ATOM 1369 O LEU B 68 0.791 70.184 -62.825 1.00 10.30 ATOM 1370 CB LEU B 68 2.716 72.295 -64.551 1.00 9.24 ATOM 1371 CG LEU B 68 4.027 73.070 -64.676 1.00 7.01 ATOM 1372 CD1 LEU B 68 5.248 72.234 -64.901 1.00 17.00 ATOM 1373 CD2 LEU B 68 4.025 74.132 -65.788 1.00 14.31 ATOM 1374 N LEU B 69 0.099 72.328 -63.029 1.00 11.18 ATOM 1375 CA LEU B 69 -1.315 72.050 -62.810 1.00 11.28 ATOM 1376 C LEU B 69 -1.819 70.892 -63.672 1.00 10.82 ATOM 1377 O LEU B 69 -2.476 69.979 -63.156 1.00 8.92 ATOM 1378 CB LEU B 69 -2.130 73.341 -62.923 1.00 12.67 ATOM 1379 CG LEU B 69 -3.627 73.149 -62.920 1.00 15.85 ATOM 1380 CD1 LEU B 69 -4.010 72.221 -61.839 1.00 18.69 ATOM 1381 CD2 LEU B 69 -4.286 74.471 -62.738 1.00 17.52 ATOM 1382 N ASN B 70 -1.508 70.919 -64.968 1.00 9.53 ATOM 1383 CA ASN B 70 -2.003 69.907 -65.903 1.00 9.06 ATOM 1384 C ASN B 70 -1.073 69.825 -67.089 1.00 9.38 ATOM 1385 O ASN B 70 -0.050 70.521 -67.152 1.00 10.04 ATOM 1386 CB ASN B 70 -3.409 70.182 -66.411 1.00 6.28 ATOM 1387 CG ASN B 70 -3.501 71.506 -66.983 1.00 13.91 ATOM 1388 OD1 ASN B 70 -2.579 71.916 -67.741 1.00 16.29 ATOM 1389 ND2 ASN B 70 -4.504 72.305 -66.529 1.00 11.11 ATOM 1390 N GLU B 71 -1.424 68.960 -68.016 1.00 7.89 ATOM 1391 CA GLU B 71 -0.676 68.737 -69.198 1.00 7.99 ATOM 1392 C GLU B 71 -0.468 69.933 -70.108 1.00 9.63 ATOM 1393 O GLU B 71 0.627 70.112 -70.552 1.00 8.93 ATOM 1394 CB GLU B 71 -1.268 67.546 -69.978 1.00 7.88 ATOM 1395 CG GLU B 71 -0.765 67.327 -71.345 1.00 8.94 ATOM 1396 CD GLU B 71 -1.738 66.502 -72.194 1.00 19.55 ATOM 1397 OE1 GLU B 71 -2.182 65.417 -71.711 1.00 21.09 ATOM 1398 OE2 GLU B 71 -2.064 66.942 -73.327 1.00 22.55 ATOM 1399 N ASP B 72 -1.517 70.679 -70.516 1.00 14.68 ATOM 1400 CA ASP B 72 -1.301 71.873 -71.390 1.00 13.93 ATOM 1401 C ASP B 72 -0.493 72.928 -70.793 1.00 14.66 ATOM 1402 O ASP B 72 0.170 73.716 -71.506 1.00 17.22 ATOM 1403 CB ASP B 72 -2.611 72.412 -71.915 1.00 17.39 ATOM 1404 CG ASP B 72 -3.429 71.314 -72.501 1.00 19.78 ATOM 1405 OD1 ASP B 72 -2.947 70.643 -73.464 1.00 21.01 ATOM 1406 OD2 ASP B 72 -4.467 71.078 -71.921 1.00 18.49 ATOM 1407 N LEU B 73 -0.450 72.988 -69.489 1.00 15.50 ATOM 1408 CA LEU B 73 0.356 74.077 -68.854 1.00 16.88 ATOM 1409 C LEU B 73 1.795 73.598 -68.994 1.00 17.13 ATOM 1410 O LEU B 73 2.713 74.421 -68.993 1.00 14.55 ATOM 1411 CB LEU B 73 0.041 74.280 -67.349 1.00 15.61 ATOM 1412 CG LEU B 73 0.738 75.289 -66.451 1.00 14.47 ATOM 1413 CD1 LEU B 73 0.660 76.606 -67.087 1.00 15.56 ATOM 1414 CD2 LEU B 73 -0.027 75.293 -65.170 1.00 12.77 ATOM 1415 N ALA B 74 1.958 72.262 -69.083 1.00 17.65 ATOM 1416 CA ALA B 74 3.328 71.583 -69.197 1.00 18.93 ATOM 1417 C ALA B 74 3.979 72.020 -70.515 1.00 17.88 ATOM 1418 O ALA B 74 5.065 72.519 -70.526 1.00 19.26 ATOM 1419 CB ALA B 74 3.180 70.088 -69.191 1.00 17.35 ATOM 1420 N LYS B 75 3.242 71.878 -71.613 1.00 16.67 ATOM 1421 CA LYS B 75 3.692 72.225 -72.929 1.00 14.00 ATOM 1422 C LYS B 75 3.926 73.707 -73.032 1.00 14.30 ATOM 1423 O LYS B 75 5.026 74.104 -73.441 1.00 15.59 ATOM 1424 CB LYS B 75 2.679 71.749 -73.934 1.00 14.96 ATOM 1425 CG LYS B 75 1.968 70.381 -73.562 1.00 14.40 ATOM 1426 CD LYS B 75 2.272 69.253 -74.608 1.00 12.43 ATOM 1427 CE LYS B 75 1.170 68.249 -74.842 1.00 15.68 ATOM 1428 NZ LYS B 75 -0.199 68.762 -75.093 1.00 13.37 ATOM 1429 N LYS B 76 2.984 74.553 -72.617 1.00 12.03 ATOM 1430 CA LYS B 76 3.311 75.984 -72.654 1.00 10.80 ATOM 1431 C LYS B 76 4.841 76.225 -72.391 1.00 10.78 ATOM 1432 O LYS B 76 5.448 77.124 -72.943 1.00 9.45 ATOM 1433 CB LYS B 76 2.462 76.752 -71.698 1.00 8.57 ATOM 1434 CG LYS B 76 2.749 78.209 -71.763 1.00 8.38 ATOM 1435 CD LYS B 76 1.966 78.906 -70.687 1.00 4.09 ATOM 1436 CE LYS B 76 2.484 80.347 -70.386 1.00 2.00 ATOM 1437 NZ LYS B 76 1.287 81.228 -69.885 1.00 6.42 ATOM 1438 N TYR B 77 5.491 75.393 -71.582 1.00 10.61 ATOM 1439 CA TYR B 77 6.872 75.670 -71.324 1.00 12.40 ATOM 1440 C TYR B 77 7.830 74.629 -71.793 1.00 12.88 ATOM 1441 O TYR B 77 9.057 74.842 -71.636 1.00 11.52 ATOM 1442 CB TYR B 77 7.130 75.839 -69.871 1.00 12.86 ATOM 1443 CG TYR B 77 6.508 77.058 -69.301 1.00 15.12 ATOM 1444 CD1 TYR B 77 5.163 77.019 -68.837 1.00 14.99 ATOM 1445 CD2 TYR B 77 7.157 78.239 -69.376 1.00 6.11 ATOM 1446 CE1 TYR B 77 4.582 78.144 -68.372 1.00 18.57 ATOM 1447 CE2 TYR B 77 6.584 79.388 -68.847 1.00 16.06 ATOM 1448 CZ TYR B 77 5.311 79.335 -68.345 1.00 7.39 ATOM 1449 OH TYR B 77 4.699 80.458 -67.889 1.00 14.02 ATOM 1450 N LYS B 78 7.263 73.504 -72.250 1.00 14.19 ATOM 1451 CA LYS B 78 8.003 72.249 -72.535 1.00 15.10 ATOM 1452 C LYS B 78 9.323 72.472 -73.139 1.00 15.39 ATOM 1453 O LYS B 78 10.278 71.866 -72.682 1.00 16.90 ATOM 1454 CB LYS B 78 7.264 71.344 -73.514 1.00 15.32 ATOM 1455 CG LYS B 78 7.999 69.995 -73.797 1.00 11.68 ATOM 1456 CD LYS B 78 7.232 69.281 -74.934 1.00 16.61 ATOM 1457 CE LYS B 78 8.095 68.285 -75.666 1.00 20.76 ATOM 1458 NZ LYS B 78 9.032 67.580 -74.703 1.00 11.20 ATOM 1459 N ASP B 79 9.423 73.322 -74.163 1.00 16.73 ATOM 1460 CA ASP B 79 10.788 73.702 -74.750 1.00 18.74 ATOM 1461 C ASP B 79 11.135 75.217 -74.946 1.00 20.66 ATOM 1462 O ASP B 79 11.712 75.641 -76.009 1.00 20.48 ATOM 1463 CB ASP B 79 10.968 73.054 -76.098 1.00 18.72 ATOM 1464 CG ASP B 79 9.662 72.840 -76.800 1.00 21.57 ATOM 1465 OD1 ASP B 79 9.419 71.711 -77.346 1.00 25.37 ATOM 1466 OD2 ASP B 79 8.851 73.809 -76.783 1.00 24.82 ATOM 1467 N GLU B 80 10.863 76.019 -73.924 1.00 19.44 ATOM 1468 CA GLU B 80 11.144 77.436 -73.999 1.00 19.33 ATOM 1469 C GLU B 80 12.226 77.796 -73.009 1.00 18.09 ATOM 1470 O GLU B 80 12.434 77.108 -72.022 1.00 16.55 ATOM 1471 CB GLU B 80 9.828 78.244 -73.719 1.00 20.36 ATOM 1472 CG GLU B 80 8.704 78.003 -74.707 1.00 21.54 ATOM 1473 CD GLU B 80 9.206 78.011 -76.179 1.00 30.53 ATOM 1474 OE1 GLU B 80 9.469 79.116 -76.782 1.00 31.76 ATOM 1475 OE2 GLU B 80 9.326 76.886 -76.746 1.00 31.31 ATOM 1476 N VAL B 81 12.878 78.937 -73.238 1.00 17.57 ATOM 1477 CA VAL B 81 13.940 79.359 -72.343 1.00 16.47 ATOM 1478 C VAL B 81 13.323 80.074 -71.207 1.00 15.80 ATOM 1479 O VAL B 81 12.771 81.152 -71.433 1.00 16.92 ATOM 1480 CB VAL B 81 15.086 80.195 -73.045 1.00 17.46 ATOM 1481 CG1 VAL B 81 16.185 80.500 -72.069 1.00 13.61 ATOM 1482 CG2 VAL B 81 15.671 79.426 -74.271 1.00 17.65 ATOM 1483 N VAL B 82 13.346 79.476 -69.990 1.00 14.23 ATOM 1484 CA VAL B 82 12.610 80.098 -68.904 1.00 13.60 ATOM 1485 C VAL B 82 13.534 80.375 -67.765 1.00 12.40 ATOM 1486 O VAL B 82 14.676 79.967 -67.895 1.00 14.07 ATOM 1487 CB VAL B 82 11.490 79.249 -68.382 1.00 12.61 ATOM 1488 CG1 VAL B 82 10.354 79.315 -69.282 1.00 10.09 ATOM 1489 CG2 VAL B 82 11.999 77.805 -68.150 1.00 11.70 ATOM 1490 N ASP B 83 13.039 81.043 -66.689 1.00 10.60 ATOM 1491 CA ASP B 83 13.762 81.172 -65.403 1.00 11.28 ATOM 1492 C ASP B 83 13.062 80.297 -64.387 1.00 9.47 ATOM 1493 O ASP B 83 11.936 79.906 -64.585 1.00 9.22 ATOM 1494 CB ASP B 83 13.768 82.602 -64.944 1.00 9.92 ATOM 1495 CG ASP B 83 14.390 83.537 -65.985 1.00 11.34 ATOM 1496 OD1 ASP B 83 15.623 83.444 -66.297 1.00 17.16 ATOM 1497 OD2 ASP B 83 13.664 84.379 -66.431 1.00 6.06 ATOM 1498 N VAL B 84 13.691 80.060 -63.267 1.00 8.77 ATOM 1499 CA VAL B 84 13.023 79.298 -62.188 1.00 10.37 ATOM 1500 C VAL B 84 13.117 79.876 -60.767 1.00 11.30 ATOM 1501 O VAL B 84 14.126 80.482 -60.456 1.00 13.92 ATOM 1502 CB VAL B 84 13.628 77.883 -62.165 1.00 10.76 ATOM 1503 CG1 VAL B 84 12.884 77.064 -61.176 1.00 5.69 ATOM 1504 CG2 VAL B 84 13.564 77.266 -63.594 1.00 4.66 ATOM 1505 N TYR B 85 12.108 79.666 -59.896 1.00 8.83 ATOM 1506 CA TYR B 85 12.136 80.156 -58.546 1.00 9.12 ATOM 1507 C TYR B 85 11.096 79.343 -57.815 1.00 10.75 ATOM 1508 O TYR B 85 9.841 79.621 -57.969 1.00 10.81 ATOM 1509 CB TYR B 85 11.767 81.683 -58.387 1.00 11.31 ATOM 1510 CG TYR B 85 12.501 82.121 -57.168 1.00 9.98 ATOM 1511 CD1 TYR B 85 13.853 82.362 -57.238 1.00 8.95 ATOM 1512 CD2 TYR B 85 11.896 82.151 -55.943 1.00 5.62 ATOM 1513 CE1 TYR B 85 14.571 82.620 -56.105 1.00 9.81 ATOM 1514 CE2 TYR B 85 12.609 82.444 -54.793 1.00 5.27 ATOM 1515 CZ TYR B 85 13.965 82.664 -54.887 1.00 10.35 ATOM 1516 OH TYR B 85 14.728 83.004 -53.767 1.00 11.66 ATOM 1517 N GLY B 86 11.541 78.354 -57.052 1.00 7.23 ATOM 1518 CA GLY B 86 10.644 77.587 -56.266 1.00 7.38 ATOM 1519 C GLY B 86 11.231 76.949 -55.037 1.00 6.94 ATOM 1520 O GLY B 86 12.435 76.891 -54.965 1.00 8.25 ATOM 1521 N SER B 87 10.382 76.472 -54.097 1.00 7.72 ATOM 1522 CA SER B 87 10.844 75.599 -52.995 1.00 8.44 ATOM 1523 C SER B 87 10.802 74.121 -53.322 1.00 8.90 ATOM 1524 O SER B 87 9.713 73.546 -53.513 1.00 9.26 ATOM 1525 CB SER B 87 9.983 75.747 -51.747 1.00 8.80 ATOM 1526 OG SER B 87 10.728 75.763 -50.525 1.00 7.70 ATOM 1527 N ASN B 88 11.982 73.491 -53.252 1.00 8.69 ATOM 1528 CA ASN B 88 12.165 72.144 -53.582 1.00 7.11 ATOM 1529 C ASN B 88 12.002 71.279 -52.338 1.00 8.13 ATOM 1530 O ASN B 88 12.130 71.771 -51.217 1.00 4.36 ATOM 1531 CB ASN B 88 13.499 71.970 -54.194 1.00 7.12 ATOM 1532 CG ASN B 88 14.642 72.413 -53.287 1.00 10.18 ATOM 1533 OD1 ASN B 88 14.774 73.557 -53.002 1.00 11.23 ATOM 1534 ND2 ASN B 88 15.541 71.479 -52.920 1.00 14.47 ATOM 1535 N TYR B 89 11.690 69.987 -52.544 1.00 6.65 ATOM 1536 CA TYR B 89 11.737 69.031 -51.411 1.00 8.82 ATOM 1537 C TYR B 89 12.318 67.674 -51.833 1.00 7.44 ATOM 1538 O TYR B 89 12.585 67.502 -52.994 1.00 11.07 ATOM 1539 CB TYR B 89 10.314 68.813 -50.904 1.00 8.27 ATOM 1540 CG TYR B 89 9.512 68.177 -51.942 1.00 11.68 ATOM 1541 CD1 TYR B 89 8.875 68.985 -52.869 1.00 15.37 ATOM 1542 CD2 TYR B 89 9.322 66.799 -51.994 1.00 12.69 ATOM 1543 CE1 TYR B 89 8.097 68.485 -53.860 1.00 17.48 ATOM 1544 CE2 TYR B 89 8.426 66.252 -52.973 1.00 17.91 ATOM 1545 CZ TYR B 89 7.807 67.121 -53.924 1.00 17.27 ATOM 1546 OH TYR B 89 6.978 66.738 -55.040 1.00 15.30 ATOM 1547 N TYR B 90 12.379 66.694 -50.953 1.00 6.70 ATOM 1548 CA TYR B 90 12.874 65.401 -51.307 1.00 9.56 ATOM 1549 C TYR B 90 11.972 64.287 -50.795 1.00 10.66 ATOM 1550 O TYR B 90 11.441 63.521 -51.556 1.00 9.30 ATOM 1551 CB TYR B 90 14.355 65.180 -50.866 1.00 11.84 ATOM 1552 CG TYR B 90 15.304 66.388 -51.055 1.00 6.94 ATOM 1553 CD1 TYR B 90 15.061 67.617 -50.466 1.00 11.94 ATOM 1554 CD2 TYR B 90 16.488 66.267 -51.848 1.00 13.00 ATOM 1555 CE1 TYR B 90 16.035 68.788 -50.710 1.00 13.14 ATOM 1556 CE2 TYR B 90 17.361 67.346 -52.107 1.00 6.85 ATOM 1557 CZ TYR B 90 17.158 68.564 -51.548 1.00 11.37 ATOM 1558 OH TYR B 90 18.112 69.535 -51.834 1.00 13.49 ATOM 1559 N VAL B 91 11.758 64.193 -49.511 1.00 12.20 ATOM 1560 CA VAL B 91 10.935 63.129 -49.007 1.00 12.35 ATOM 1561 C VAL B 91 9.624 63.043 -49.868 1.00 14.60 ATOM 1562 O VAL B 91 8.783 63.939 -49.828 1.00 15.23 ATOM 1563 CB VAL B 91 10.650 63.404 -47.531 1.00 11.92 ATOM 1564 CG1 VAL B 91 9.584 62.436 -46.988 1.00 15.42 ATOM 1565 CG2 VAL B 91 11.821 63.307 -46.758 1.00 10.19 ATOM 1566 N ASN B 92 9.518 61.970 -50.668 1.00 17.21 ATOM 1567 CA ASN B 92 8.487 61.746 -51.714 1.00 19.48 ATOM 1568 C ASN B 92 8.707 62.480 -53.062 1.00 18.45 ATOM 1569 O ASN B 92 7.691 62.951 -53.670 1.00 21.19 ATOM 1570 CB ASN B 92 7.082 62.037 -51.126 1.00 19.37 ATOM 1571 CG ASN B 92 7.038 61.674 -49.672 1.00 22.66 ATOM 1572 OD1 ASN B 92 7.620 60.637 -49.265 1.00 20.81 ATOM 1573 ND2 ASN B 92 6.391 62.518 -48.864 1.00 18.75 ATOM 1574 N CYS B 93 9.980 62.605 -53.491 1.00 15.78 ATOM 1575 CA CYS B 93 10.367 63.139 -54.805 1.00 13.75 ATOM 1576 C CYS B 93 10.644 61.980 -55.647 1.00 13.70 ATOM 1577 O CYS B 93 11.751 61.344 -55.527 1.00 10.79 ATOM 1578 CB CYS B 93 11.636 63.954 -54.782 1.00 13.51 ATOM 1579 SG CYS B 93 11.861 64.897 -56.272 1.00 14.61 ATOM 1580 N TYR B 94 9.653 61.678 -56.486 1.00 13.67 ATOM 1581 CA TYR B 94 9.621 60.421 -57.328 1.00 15.69 ATOM 1582 C TYR B 94 9.675 60.669 -58.829 1.00 15.27 ATOM 1583 O TYR B 94 9.286 61.762 -59.331 1.00 19.56 ATOM 1584 CB TYR B 94 8.305 59.659 -57.057 1.00 15.20 ATOM 1585 CG TYR B 94 7.031 60.478 -57.059 1.00 18.01 ATOM 1586 CD1 TYR B 94 7.022 61.873 -56.649 1.00 15.82 ATOM 1587 CD2 TYR B 94 5.785 59.875 -57.383 1.00 23.47 ATOM 1588 CE1 TYR B 94 5.877 62.615 -56.650 1.00 17.23 ATOM 1589 CE2 TYR B 94 4.621 60.606 -57.388 1.00 19.56 ATOM 1590 CZ TYR B 94 4.679 62.004 -56.987 1.00 19.32 ATOM 1591 OH TYR B 94 3.547 62.769 -56.927 1.00 17.22 ATOM 1592 N PHE B 95 9.970 59.607 -59.527 1.00 17.97 ATOM 1593 CA PHE B 95 10.083 59.509 -60.982 1.00 19.11 ATOM 1594 C PHE B 95 9.652 58.228 -61.591 1.00 21.85 ATOM 1595 O PHE B 95 10.132 57.878 -62.688 1.00 22.70 ATOM 1596 CB PHE B 95 11.560 59.673 -61.375 1.00 17.11 ATOM 1597 CG PHE B 95 12.114 61.023 -61.058 1.00 14.83 ATOM 1598 CD1 PHE B 95 12.667 61.299 -59.805 1.00 13.75 ATOM 1599 CD2 PHE B 95 12.203 61.974 -62.026 1.00 14.84 ATOM 1600 CE1 PHE B 95 13.252 62.604 -59.528 1.00 8.51 ATOM 1601 CE2 PHE B 95 12.822 63.262 -61.725 1.00 12.52 ATOM 1602 CZ PHE B 95 13.338 63.488 -60.464 1.00 6.47 ATOM 1603 N SER B 96 8.810 57.482 -60.875 1.00 25.99 ATOM 1604 CA SER B 96 8.347 56.176 -61.296 1.00 28.59 ATOM 1605 C SER B 96 7.024 55.902 -60.597 1.00 31.56 ATOM 1606 O SER B 96 6.234 56.815 -60.366 1.00 33.73 ATOM 1607 CB SER B 96 9.379 55.077 -60.951 1.00 29.62 ATOM 1608 OG SER B 96 9.536 54.957 -59.559 1.00 28.29 ATOM 1609 N SER B 97 6.788 54.675 -60.185 1.00 33.99 ATOM 1610 CA SER B 97 5.468 54.366 -59.653 1.00 38.04 ATOM 1611 C SER B 97 5.525 54.185 -58.124 1.00 39.63 ATOM 1612 O SER B 97 4.625 54.625 -57.400 1.00 40.35 ATOM 1613 CB SER B 97 4.880 53.118 -60.369 1.00 37.97 ATOM 1614 OG SER B 97 5.813 52.017 -60.388 1.00 40.53 ATOM 1615 N LYS B 98 6.578 53.505 -57.648 1.00 41.07 ATOM 1616 CA LYS B 98 6.788 53.287 -56.228 1.00 41.19 ATOM 1617 C LYS B 98 6.946 54.657 -55.566 1.00 40.42 ATOM 1618 O LYS B 98 7.752 55.497 -56.014 1.00 40.75 ATOM 1619 CB LYS B 98 8.019 52.418 -55.969 1.00 41.81 ATOM 1620 CG LYS B 98 8.231 52.130 -54.448 1.00 46.39 ATOM 1621 CD LYS B 98 8.799 50.694 -54.215 1.00 47.24 ATOM 1622 CE LYS B 98 9.540 50.525 -52.875 1.00 44.71 ATOM 1623 NZ LYS B 98 10.104 49.134 -52.858 1.00 43.05 ATOM 1624 N ASP B 99 6.189 54.810 -54.474 1.00 38.39 ATOM 1625 CA ASP B 99 5.901 56.066 -53.718 1.00 34.76 ATOM 1626 C ASP B 99 7.036 56.611 -52.805 1.00 32.59 ATOM 1627 O ASP B 99 7.281 57.835 -52.828 1.00 31.60 ATOM 1628 CB ASP B 99 4.584 55.829 -52.926 1.00 34.67 ATOM 1629 CG ASP B 99 4.399 54.356 -52.600 1.00 35.24 ATOM 1630 OD1 ASP B 99 5.420 53.669 -52.353 1.00 32.71 ATOM 1631 OD2 ASP B 99 3.253 53.869 -52.686 1.00 40.51 ATOM 1632 N ASN B 100 7.685 55.702 -52.026 1.00 31.93 ATOM 1633 CA ASN B 100 8.939 55.992 -51.232 1.00 30.10 ATOM 1634 C ASN B 100 10.162 55.208 -51.702 1.00 27.75 ATOM 1635 O ASN B 100 10.419 54.047 -51.296 1.00 26.05 ATOM 1636 CB ASN B 100 8.766 55.841 -49.718 1.00 30.15 ATOM 1637 CG ASN B 100 9.343 57.037 -48.930 1.00 33.53 ATOM 1638 OD1 ASN B 100 9.026 57.182 -47.760 1.00 37.67 ATOM 1639 ND2 ASN B 100 10.181 57.898 -49.571 1.00 36.67 ATOM 1640 N VAL B 101 10.896 55.889 -52.579 1.00 23.52 ATOM 1641 CA VAL B 101 12.030 55.317 -53.305 1.00 19.42 ATOM 1642 C VAL B 101 13.074 56.460 -53.430 1.00 17.45 ATOM 1643 O VAL B 101 12.697 57.638 -53.560 1.00 17.04 ATOM 1644 CB VAL B 101 11.655 54.932 -54.680 1.00 19.06 ATOM 1645 CG1 VAL B 101 12.769 55.233 -55.580 1.00 16.25 ATOM 1646 CG2 VAL B 101 11.246 53.482 -54.761 1.00 16.36 ATOM 1647 N TRP B 102 14.352 56.134 -53.434 1.00 13.17 ATOM 1648 CA TRP B 102 15.408 57.181 -53.580 1.00 11.54 ATOM 1649 C TRP B 102 16.058 57.307 -55.003 1.00 13.46 ATOM 1650 O TRP B 102 15.952 56.363 -55.838 1.00 12.67 ATOM 1651 CB TRP B 102 16.497 57.028 -52.477 1.00 10.48 ATOM 1652 CG TRP B 102 17.507 58.185 -52.433 1.00 5.07 ATOM 1653 CD1 TRP B 102 17.217 59.462 -52.217 1.00 7.38 ATOM 1654 CD2 TRP B 102 18.941 58.100 -52.532 1.00 6.91 ATOM 1655 NE1 TRP B 102 18.339 60.232 -52.206 1.00 12.31 ATOM 1656 CE2 TRP B 102 19.437 59.423 -52.400 1.00 11.59 ATOM 1657 CE3 TRP B 102 19.844 57.047 -52.618 1.00 2.04 ATOM 1658 CZ2 TRP B 102 20.804 59.745 -52.437 1.00 9.18 ATOM 1659 CZ3 TRP B 102 21.225 57.372 -52.720 1.00 12.39 ATOM 1660 CH2 TRP B 102 21.678 58.744 -52.650 1.00 5.74 ATOM 1661 N TRP B 103 16.737 58.440 -55.275 1.00 10.67 ATOM 1662 CA TRP B 103 17.389 58.659 -56.531 1.00 11.92 ATOM 1663 C TRP B 103 18.728 59.316 -56.402 1.00 12.65 ATOM 1664 O TRP B 103 19.762 58.621 -56.390 1.00 9.75 ATOM 1665 CB TRP B 103 16.594 59.594 -57.349 1.00 12.69 ATOM 1666 CG TRP B 103 15.126 59.184 -57.268 1.00 16.33 ATOM 1667 CD1 TRP B 103 14.267 59.483 -56.223 1.00 18.14 ATOM 1668 CD2 TRP B 103 14.374 58.378 -58.206 1.00 10.68 ATOM 1669 NE1 TRP B 103 12.989 58.940 -56.488 1.00 21.88 ATOM 1670 CE2 TRP B 103 13.016 58.269 -57.681 1.00 16.85 ATOM 1671 CE3 TRP B 103 14.674 57.779 -59.411 1.00 9.65 ATOM 1672 CZ2 TRP B 103 12.003 57.597 -58.327 1.00 5.83 ATOM 1673 CZ3 TRP B 103 13.686 57.072 -60.073 1.00 14.50 ATOM 1674 CH2 TRP B 103 12.327 56.970 -59.508 1.00 16.82 ATOM 1675 N HIS B 104 18.665 60.638 -56.254 1.00 12.02 ATOM 1676 CA HIS B 104 19.857 61.491 -56.132 1.00 16.75 ATOM 1677 C HIS B 104 20.012 62.383 -57.314 1.00 16.77 ATOM 1678 O HIS B 104 19.530 62.037 -58.414 1.00 18.99 ATOM 1679 CB HIS B 104 21.213 60.746 -55.925 1.00 16.62 ATOM 1680 CG HIS B 104 22.336 61.642 -55.459 1.00 25.28 ATOM 1681 ND1 HIS B 104 23.120 62.390 -56.337 1.00 29.30 ATOM 1682 CD2 HIS B 104 22.773 61.953 -54.208 1.00 29.34 ATOM 1683 CE1 HIS B 104 23.952 63.152 -55.647 1.00 29.76 ATOM 1684 NE2 HIS B 104 23.782 62.891 -54.358 1.00 36.11 ATOM 1685 N GLY B 105 20.739 63.493 -57.095 1.00 18.38 ATOM 1686 CA GLY B 105 20.819 64.653 -58.034 1.00 16.22 ATOM 1687 C GLY B 105 19.465 65.145 -58.513 1.00 16.19 ATOM 1688 O GLY B 105 19.368 65.887 -59.512 1.00 19.12 ATOM 1689 N LYS B 106 18.393 64.787 -57.799 1.00 14.02 ATOM 1690 CA LYS B 106 17.084 65.062 -58.255 1.00 12.47 ATOM 1691 C LYS B 106 16.345 65.731 -57.120 1.00 12.17 ATOM 1692 O LYS B 106 16.776 65.679 -56.013 1.00 11.55 ATOM 1693 CB LYS B 106 16.360 63.756 -58.710 1.00 13.14 ATOM 1694 CG LYS B 106 16.797 63.278 -60.111 1.00 8.35 ATOM 1695 CD LYS B 106 16.382 61.820 -60.425 1.00 11.82 ATOM 1696 CE LYS B 106 17.092 61.326 -61.692 1.00 15.57 ATOM 1697 NZ LYS B 106 18.235 60.490 -61.370 1.00 7.61 ATOM 1698 N THR B 107 15.234 66.428 -57.401 1.00 13.15 ATOM 1699 CA THR B 107 14.476 67.159 -56.381 1.00 8.49 ATOM 1700 C THR B 107 13.231 67.590 -57.055 1.00 6.30 ATOM 1701 O THR B 107 13.235 67.728 -58.277 1.00 5.01 ATOM 1702 CB THR B 107 15.275 68.272 -55.782 1.00 8.54 ATOM 1703 OG1 THR B 107 14.660 68.602 -54.511 1.00 14.67 ATOM 1704 CG2 THR B 107 15.330 69.521 -56.648 1.00 9.67 ATOM 1705 N CYS B 108 12.188 67.807 -56.306 1.00 4.27 ATOM 1706 CA CYS B 108 10.876 68.141 -56.923 1.00 6.58 ATOM 1707 C CYS B 108 10.353 69.553 -56.567 1.00 5.36 ATOM 1708 O CYS B 108 10.907 70.226 -55.725 1.00 5.29 ATOM 1709 CB CYS B 108 9.803 67.187 -56.465 1.00 6.72 ATOM 1710 SG CYS B 108 10.094 65.385 -57.069 1.00 9.90 ATOM 1711 N MET B 109 9.316 70.008 -57.246 1.00 5.12 ATOM 1712 CA MET B 109 8.679 71.251 -56.801 1.00 7.91 ATOM 1713 C MET B 109 7.433 71.379 -57.550 1.00 9.35 ATOM 1714 O MET B 109 6.863 70.371 -58.066 1.00 8.73 ATOM 1715 CB MET B 109 9.568 72.495 -57.063 1.00 4.69 ATOM 1716 CG MET B 109 10.500 72.430 -58.287 1.00 4.57 ATOM 1717 SD MET B 109 11.353 73.955 -58.699 1.00 14.05 ATOM 1718 CE MET B 109 10.059 75.050 -58.966 1.00 5.69 ATOM 1719 N TYR B 110 6.937 72.604 -57.591 1.00 9.58 ATOM 1720 CA TYR B 110 5.757 72.850 -58.404 1.00 10.15 ATOM 1721 C TYR B 110 5.902 74.323 -58.882 1.00 9.39 ATOM 1722 O TYR B 110 6.311 75.097 -58.125 1.00 9.09 ATOM 1723 CB TYR B 110 4.550 72.741 -57.565 1.00 7.44 ATOM 1724 CG TYR B 110 4.372 71.414 -56.868 1.00 9.66 ATOM 1725 CD1 TYR B 110 4.965 71.150 -55.616 1.00 6.00 ATOM 1726 CD2 TYR B 110 3.577 70.425 -57.453 1.00 3.96 ATOM 1727 CE1 TYR B 110 4.778 69.920 -54.962 1.00 12.85 ATOM 1728 CE2 TYR B 110 3.408 69.212 -56.844 1.00 15.12 ATOM 1729 CZ TYR B 110 3.977 68.950 -55.612 1.00 12.80 ATOM 1730 OH TYR B 110 3.699 67.763 -55.123 1.00 5.30 ATOM 1731 N GLY B 111 5.582 74.631 -60.131 1.00 8.70 ATOM 1732 CA GLY B 111 5.484 75.996 -60.610 1.00 9.13 ATOM 1733 C GLY B 111 6.866 76.655 -60.607 1.00 9.52 ATOM 1734 O GLY B 111 7.889 75.991 -60.731 1.00 8.14 ATOM 1735 N GLY B 112 6.873 77.960 -60.434 1.00 10.77 ATOM 1736 CA GLY B 112 8.144 78.748 -60.544 1.00 13.18 ATOM 1737 C GLY B 112 8.996 78.739 -61.797 1.00 11.17 ATOM 1738 O GLY B 112 10.105 78.204 -61.791 1.00 13.11 ATOM 1739 N ILE B 113 8.467 79.310 -62.878 1.00 11.24 ATOM 1740 CA ILE B 113 9.169 79.449 -64.171 1.00 9.56 ATOM 1741 C ILE B 113 8.519 80.518 -64.952 1.00 10.23 ATOM 1742 O ILE B 113 7.281 80.661 -64.867 1.00 10.06 ATOM 1743 CB ILE B 113 9.006 78.156 -64.984 1.00 8.61 ATOM 1744 CG1 ILE B 113 7.580 77.622 -64.832 1.00 8.65 ATOM 1745 CG2 ILE B 113 9.994 77.192 -64.406 1.00 6.90 ATOM 1746 CD1 ILE B 113 7.313 76.166 -65.516 1.00 12.96 ATOM 1747 N THR B 114 9.325 81.256 -65.725 1.00 10.16 ATOM 1748 CA THR B 114 8.774 82.257 -66.629 1.00 11.15 ATOM 1749 C THR B 114 9.670 82.465 -67.835 1.00 10.54 ATOM 1750 O THR B 114 10.912 82.234 -67.805 1.00 11.15 ATOM 1751 CB THR B 114 8.550 83.601 -65.914 1.00 13.35 ATOM 1752 OG1 THR B 114 9.843 84.078 -65.478 1.00 16.18 ATOM 1753 CG2 THR B 114 7.606 83.380 -64.728 1.00 7.66 ATOM 1754 N LYS B 115 9.050 82.879 -68.928 1.00 9.49 ATOM 1755 CA LYS B 115 9.785 83.011 -70.168 1.00 9.70 ATOM 1756 C LYS B 115 10.811 84.122 -69.895 1.00 9.23 ATOM 1757 O LYS B 115 10.503 85.183 -69.354 1.00 9.06 ATOM 1758 CB LYS B 115 8.908 83.301 -71.387 1.00 10.49 ATOM 1759 CG LYS B 115 8.038 82.187 -72.012 1.00 19.64 ATOM 1760 CD LYS B 115 8.699 80.880 -72.386 1.00 19.57 ATOM 1761 CE LYS B 115 9.221 80.970 -73.805 1.00 21.13 ATOM 1762 NZ LYS B 115 8.195 80.572 -74.876 1.00 17.94 ATOM 1763 N HIS B 116 12.071 83.790 -70.094 1.00 10.99 ATOM 1764 CA HIS B 116 13.201 84.707 -69.864 1.00 10.07 ATOM 1765 C HIS B 116 13.223 85.943 -70.791 1.00 12.52 ATOM 1766 O HIS B 116 13.477 87.033 -70.303 1.00 9.87 ATOM 1767 CB HIS B 116 14.447 83.988 -70.149 1.00 9.39 ATOM 1768 CG HIS B 116 15.634 84.874 -70.122 1.00 10.83 ATOM 1769 ND1 HIS B 116 15.658 86.065 -70.805 1.00 10.40 ATOM 1770 CD2 HIS B 116 16.854 84.727 -69.554 1.00 7.08 ATOM 1771 CE1 HIS B 116 16.851 86.627 -70.630 1.00 16.48 ATOM 1772 NE2 HIS B 116 17.600 85.809 -69.915 1.00 13.80 ATOM 1773 N GLU B 117 12.954 85.711 -72.095 1.00 14.09 ATOM 1774 CA GLU B 117 13.008 86.715 -73.119 1.00 18.84 ATOM 1775 C GLU B 117 12.160 87.878 -72.715 1.00 20.59 ATOM 1776 O GLU B 117 10.973 87.724 -72.412 1.00 18.17 ATOM 1777 CB GLU B 117 12.507 86.212 -74.453 1.00 19.37 ATOM 1778 CG GLU B 117 13.333 85.008 -74.997 1.00 25.78 ATOM 1779 CD GLU B 117 13.310 83.843 -74.035 1.00 27.77 ATOM 1780 OE1 GLU B 117 12.223 83.466 -73.482 1.00 32.69 ATOM 1781 OE2 GLU B 117 14.401 83.336 -73.758 1.00 33.27 ATOM 1782 N GLY B 118 12.817 89.041 -72.711 1.00 22.37 ATOM 1783 CA GLY B 118 12.149 90.322 -72.498 1.00 24.73 ATOM 1784 C GLY B 118 11.132 90.259 -71.360 1.00 26.71 ATOM 1785 O GLY B 118 9.886 90.422 -71.592 1.00 27.33 ATOM 1786 N ASN B 119 11.679 89.909 -70.183 1.00 27.51 ATOM 1787 CA ASN B 119 10.988 89.869 -68.887 1.00 29.14 ATOM 1788 C ASN B 119 11.884 90.374 -67.752 1.00 29.31 ATOM 1789 O ASN B 119 11.366 90.684 -66.681 1.00 30.05 ATOM 1790 CB ASN B 119 10.432 88.477 -68.527 1.00 28.85 ATOM 1791 CG ASN B 119 9.737 88.451 -67.164 1.00 29.52 ATOM 1792 OD1 ASN B 119 8.930 89.342 -66.828 1.00 26.52 ATOM 1793 ND2 ASN B 119 10.089 87.441 -66.339 1.00 26.90 ATOM 1794 N HIS B 120 13.196 90.450 -67.971 1.00 28.78 ATOM 1795 CA HIS B 120 14.067 91.078 -66.995 1.00 29.01 ATOM 1796 C HIS B 120 14.113 92.632 -67.214 1.00 29.57 ATOM 1797 O HIS B 120 13.477 93.145 -68.150 1.00 28.35 ATOM 1798 CB HIS B 120 15.447 90.446 -66.999 1.00 27.87 ATOM 1799 CG HIS B 120 15.452 88.993 -66.670 1.00 27.03 ATOM 1800 ND1 HIS B 120 16.619 88.308 -66.412 1.00 24.92 ATOM 1801 CD2 HIS B 120 14.451 88.070 -66.614 1.00 27.21 ATOM 1802 CE1 HIS B 120 16.339 87.035 -66.170 1.00 25.59 ATOM 1803 NE2 HIS B 120 15.024 86.861 -66.280 1.00 24.73 ATOM 1804 N PHE B 121 14.850 93.346 -66.342 1.00 30.72 ATOM 1805 CA PHE B 121 14.986 94.839 -66.354 1.00 30.52 ATOM 1806 C PHE B 121 16.146 95.390 -67.176 1.00 31.96 ATOM 1807 O PHE B 121 17.125 94.668 -67.533 1.00 28.89 ATOM 1808 CB PHE B 121 15.031 95.395 -64.915 1.00 30.37 ATOM 1809 CG PHE B 121 13.773 95.020 -64.070 1.00 32.98 ATOM 1810 CD1 PHE B 121 13.731 93.846 -63.346 1.00 29.42 ATOM 1811 CD2 PHE B 121 12.650 95.835 -64.060 1.00 31.22 ATOM 1812 CE1 PHE B 121 12.612 93.474 -62.648 1.00 29.11 ATOM 1813 CE2 PHE B 121 11.490 95.513 -63.325 1.00 31.61 ATOM 1814 CZ PHE B 121 11.449 94.340 -62.621 1.00 33.06 ATOM 1815 N ASP B 122 16.012 96.696 -67.433 1.00 33.06 ATOM 1816 CA ASP B 122 17.021 97.532 -68.102 1.00 35.47 ATOM 1817 C ASP B 122 18.478 97.100 -67.971 1.00 36.30 ATOM 1818 O ASP B 122 19.023 96.501 -68.922 1.00 36.41 ATOM 1819 CB ASP B 122 16.832 98.948 -67.623 1.00 35.80 ATOM 1820 CG ASP B 122 15.368 99.286 -67.473 1.00 37.96 ATOM 1821 OD1 ASP B 122 14.704 99.441 -68.516 1.00 33.41 ATOM 1822 OD2 ASP B 122 14.876 99.334 -66.319 1.00 41.53 ATOM 1823 N ASN B 123 19.109 97.411 -66.826 1.00 36.90 ATOM 1824 CA ASN B 123 20.581 97.164 -66.654 1.00 38.14 ATOM 1825 C ASN B 123 20.949 96.369 -65.397 1.00 37.63 ATOM 1826 O ASN B 123 21.938 96.646 -64.728 1.00 37.21 ATOM 1827 CB ASN B 123 21.380 98.488 -66.751 1.00 38.59 ATOM 1828 CG ASN B 123 20.858 99.394 -67.885 1.00 40.63 ATOM 1829 OD1 ASN B 123 20.748 98.955 -69.059 1.00 38.53 ATOM 1830 ND2 ASN B 123 20.479 100.644 -67.525 1.00 41.94 ATOM 1831 N GLY B 124 20.147 95.340 -65.127 1.00 38.07 ATOM 1832 CA GLY B 124 20.142 94.651 -63.830 1.00 36.81 ATOM 1833 C GLY B 124 19.411 95.286 -62.633 1.00 35.66 ATOM 1834 O GLY B 124 19.419 94.723 -61.534 1.00 36.43 ATOM 1835 N ASN B 125 18.789 96.454 -62.805 1.00 34.47 ATOM 1836 CA ASN B 125 17.963 97.006 -61.726 1.00 31.69 ATOM 1837 C ASN B 125 16.999 95.950 -61.192 1.00 30.35 ATOM 1838 O ASN B 125 16.532 95.069 -61.946 1.00 29.46 ATOM 1839 CB ASN B 125 17.196 98.203 -62.233 1.00 31.89 ATOM 1840 CG ASN B 125 18.067 99.117 -63.058 1.00 30.31 ATOM 1841 OD1 ASN B 125 19.126 99.578 -62.604 1.00 32.28 ATOM 1842 ND2 ASN B 125 17.651 99.357 -64.282 1.00 27.13 ATOM 1843 N LEU B 126 16.716 96.038 -59.894 1.00 28.25 ATOM 1844 CA LEU B 126 15.776 95.134 -59.194 1.00 25.70 ATOM 1845 C LEU B 126 14.576 95.936 -58.726 1.00 25.19 ATOM 1846 O LEU B 126 14.705 97.120 -58.351 1.00 24.59 ATOM 1847 CB LEU B 126 16.428 94.546 -57.965 1.00 22.39 ATOM 1848 CG LEU B 126 17.691 93.714 -58.205 1.00 25.21 ATOM 1849 CD1 LEU B 126 18.909 94.566 -57.829 1.00 21.63 ATOM 1850 CD2 LEU B 126 17.725 92.365 -57.395 1.00 14.86 ATOM 1851 N GLN B 127 13.438 95.266 -58.681 1.00 24.03 ATOM 1852 CA GLN B 127 12.162 95.869 -58.291 1.00 23.82 ATOM 1853 C GLN B 127 11.867 95.662 -56.816 1.00 21.33 ATOM 1854 O GLN B 127 12.310 94.690 -56.213 1.00 23.19 ATOM 1855 CB GLN B 127 11.088 95.236 -59.159 1.00 24.51 ATOM 1856 CG GLN B 127 9.693 95.720 -59.004 1.00 23.80 ATOM 1857 CD GLN B 127 9.518 97.090 -59.486 1.00 19.47 ATOM 1858 OE1 GLN B 127 9.931 97.432 -60.602 1.00 16.64 ATOM 1859 NE2 GLN B 127 8.884 97.934 -58.638 1.00 18.42 ATOM 1860 N ASN B 128 11.174 96.586 -56.197 1.00 18.24 ATOM 1861 CA ASN B 128 10.876 96.414 -54.808 1.00 16.74 ATOM 1862 C ASN B 128 9.400 96.250 -54.537 1.00 14.86 ATOM 1863 O ASN B 128 8.579 96.911 -55.087 1.00 13.35 ATOM 1864 CB ASN B 128 11.460 97.541 -54.027 1.00 17.06 ATOM 1865 CG ASN B 128 12.946 97.437 -53.892 1.00 22.92 ATOM 1866 OD1 ASN B 128 13.540 96.484 -53.243 1.00 27.41 ATOM 1867 ND2 ASN B 128 13.598 98.411 -54.478 1.00 23.80 ATOM 1868 N VAL B 129 9.079 95.342 -53.647 1.00 15.83 ATOM 1869 CA VAL B 129 7.672 94.996 -53.374 1.00 12.49 ATOM 1870 C VAL B 129 7.427 95.137 -51.888 1.00 12.76 ATOM 1871 O VAL B 129 8.068 94.511 -51.012 1.00 12.57 ATOM 1872 CB VAL B 129 7.312 93.651 -53.890 1.00 11.86 ATOM 1873 CG1 VAL B 129 5.859 93.312 -53.630 1.00 13.98 ATOM 1874 CG2 VAL B 129 7.557 93.552 -55.345 1.00 12.23 ATOM 1875 N LEU B 130 6.505 96.028 -51.600 1.00 12.53 ATOM 1876 CA LEU B 130 6.116 96.238 -50.255 1.00 14.17 ATOM 1877 C LEU B 130 5.396 95.053 -49.567 1.00 15.01 ATOM 1878 O LEU B 130 4.605 94.357 -50.183 1.00 12.94 ATOM 1879 CB LEU B 130 5.234 97.449 -50.208 1.00 13.01 ATOM 1880 CG LEU B 130 4.670 97.861 -48.845 1.00 13.37 ATOM 1881 CD1 LEU B 130 5.718 98.086 -47.935 1.00 17.50 ATOM 1882 CD2 LEU B 130 3.956 99.214 -49.054 1.00 14.42 ATOM 1883 N VAL B 131 5.654 94.887 -48.273 1.00 15.72 ATOM 1884 CA VAL B 131 4.900 93.944 -47.502 1.00 17.44 ATOM 1885 C VAL B 131 4.422 94.588 -46.227 1.00 17.65 ATOM 1886 O VAL B 131 5.232 94.875 -45.390 1.00 18.45 ATOM 1887 CB VAL B 131 5.732 92.787 -47.129 1.00 17.83 ATOM 1888 CG1 VAL B 131 4.857 91.621 -46.696 1.00 20.26 ATOM 1889 CG2 VAL B 131 6.479 92.304 -48.370 1.00 21.52 ATOM 1890 N ARG B 132 3.096 94.764 -46.065 1.00 17.10 ATOM 1891 CA ARG B 132 2.514 95.230 -44.837 1.00 16.49 ATOM 1892 C ARG B 132 2.250 94.041 -43.951 1.00 16.38 ATOM 1893 O ARG B 132 1.486 93.128 -44.288 1.00 17.66 ATOM 1894 CB ARG B 132 1.233 96.053 -45.158 1.00 17.64 ATOM 1895 CG ARG B 132 1.533 97.451 -45.817 1.00 19.05 ATOM 1896 CD ARG B 132 0.175 98.171 -46.138 1.00 22.16 ATOM 1897 NE ARG B 132 0.272 99.465 -46.820 1.00 26.61 ATOM 1898 CZ ARG B 132 1.090 100.473 -46.477 1.00 28.63 ATOM 1899 NH1 ARG B 132 1.978 100.343 -45.482 1.00 24.59 ATOM 1900 NH2 ARG B 132 1.025 101.621 -47.167 1.00 26.04 ATOM 1901 N VAL B 133 2.899 93.957 -42.793 1.00 17.40 ATOM 1902 CA VAL B 133 2.578 92.864 -41.856 1.00 17.03 ATOM 1903 C VAL B 133 1.515 93.263 -40.800 1.00 18.71 ATOM 1904 O VAL B 133 1.548 94.406 -40.251 1.00 20.36 ATOM 1905 CB VAL B 133 3.822 92.297 -41.244 1.00 16.70 ATOM 1906 CG1 VAL B 133 3.556 90.928 -40.665 1.00 16.96 ATOM 1907 CG2 VAL B 133 4.932 92.191 -42.356 1.00 16.40 ATOM 1908 N TYR B 134 0.524 92.392 -40.573 1.00 15.25 ATOM 1909 CA TYR B 134 -0.435 92.626 -39.494 1.00 14.39 ATOM 1910 C TYR B 134 -0.391 91.550 -38.377 1.00 14.65 ATOM 1911 O TYR B 134 -0.665 90.379 -38.641 1.00 16.82 ATOM 1912 CB TYR B 134 -1.813 92.708 -40.093 1.00 12.80 ATOM 1913 CG TYR B 134 -1.924 93.732 -41.220 1.00 11.35 ATOM 1914 CD1 TYR B 134 -1.179 93.601 -42.391 1.00 13.80 ATOM 1915 CD2 TYR B 134 -2.725 94.806 -41.095 1.00 9.74 ATOM 1916 CE1 TYR B 134 -1.221 94.530 -43.377 1.00 12.88 ATOM 1917 CE2 TYR B 134 -2.824 95.757 -42.071 1.00 12.15 ATOM 1918 CZ TYR B 134 -2.126 95.645 -43.251 1.00 15.95 ATOM 1919 OH TYR B 134 -2.229 96.681 -44.278 1.00 10.49 ATOM 1920 N GLU B 135 -0.109 91.959 -37.145 1.00 12.49 ATOM 1921 CA GLU B 135 -0.117 91.142 -35.939 1.00 11.29 ATOM 1922 C GLU B 135 -1.349 91.598 -35.210 1.00 11.63 ATOM 1923 O GLU B 135 -1.486 92.793 -34.824 1.00 11.38 ATOM 1924 CB GLU B 135 1.158 91.467 -35.102 1.00 6.45 ATOM 1925 CG GLU B 135 2.327 91.503 -35.961 1.00 9.85 ATOM 1926 CD GLU B 135 3.631 91.477 -35.138 1.00 15.83 ATOM 1927 OE1 GLU B 135 3.927 90.356 -34.611 1.00 17.06 ATOM 1928 OE2 GLU B 135 4.251 92.551 -34.974 1.00 8.29 ATOM 1929 N ASN B 136 -2.278 90.671 -35.064 1.00 13.39 ATOM 1930 CA ASN B 136 -3.520 90.942 -34.395 1.00 14.33 ATOM 1931 C ASN B 136 -4.244 92.175 -34.980 1.00 15.19 ATOM 1932 O ASN B 136 -4.798 92.970 -34.222 1.00 15.12 ATOM 1933 CB ASN B 136 -3.238 91.057 -32.887 1.00 13.00 ATOM 1934 CG ASN B 136 -2.793 89.706 -32.317 1.00 15.23 ATOM 1935 OD1 ASN B 136 -3.528 88.730 -32.438 1.00 16.81 ATOM 1936 ND2 ASN B 136 -1.577 89.630 -31.783 1.00 8.97 ATOM 1937 N LYS B 137 -4.207 92.305 -36.305 1.00 15.54 ATOM 1938 CA LYS B 137 -4.813 93.461 -36.993 1.00 16.83 ATOM 1939 C LYS B 137 -4.002 94.796 -36.861 1.00 17.35 ATOM 1940 O LYS B 137 -4.584 95.859 -36.880 1.00 17.81 ATOM 1941 CB LYS B 137 -6.211 93.705 -36.484 1.00 16.90 ATOM 1942 CG LYS B 137 -7.126 92.573 -36.869 1.00 17.32 ATOM 1943 CD LYS B 137 -8.365 92.709 -36.102 1.00 16.98 ATOM 1944 CE LYS B 137 -9.354 91.606 -36.404 1.00 13.15 ATOM 1945 NZ LYS B 137 -9.922 91.819 -37.745 1.00 15.50 ATOM 1946 N ARG B 138 -2.684 94.771 -36.745 1.00 16.45 ATOM 1947 CA ARG B 138 -2.027 96.073 -36.683 1.00 16.54 ATOM 1948 C ARG B 138 -0.818 96.168 -37.593 1.00 15.22 ATOM 1949 O ARG B 138 -0.110 95.183 -37.825 1.00 11.80 ATOM 1950 CB ARG B 138 -1.701 96.347 -35.235 1.00 18.53 ATOM 1951 CG ARG B 138 -2.889 96.118 -34.246 1.00 17.08 ATOM 1952 CD ARG B 138 -2.777 97.008 -32.987 1.00 23.06 ATOM 1953 NE ARG B 138 -3.823 96.655 -32.002 1.00 22.86 ATOM 1954 CZ ARG B 138 -4.245 97.403 -31.003 1.00 20.73 ATOM 1955 NH1 ARG B 138 -3.748 98.619 -30.789 1.00 28.49 ATOM 1956 NH2 ARG B 138 -5.168 96.938 -30.191 1.00 21.56 ATOM 1957 N ASN B 139 -0.613 97.325 -38.231 1.00 14.96 ATOM 1958 CA ASN B 139 0.519 97.337 -39.218 1.00 12.56 ATOM 1959 C ASN B 139 1.790 97.520 -38.443 1.00 12.18 ATOM 1960 O ASN B 139 2.277 98.658 -38.204 1.00 12.06 ATOM 1961 CB ASN B 139 0.269 98.289 -40.419 1.00 12.40 ATOM 1962 CG ASN B 139 1.417 98.285 -41.448 1.00 12.13 ATOM 1963 OD1 ASN B 139 1.525 99.198 -42.291 1.00 5.69 ATOM 1964 ND2 ASN B 139 2.212 97.187 -41.462 1.00 8.79 ATOM 1965 N THR B 140 2.331 96.396 -37.975 1.00 9.99 ATOM 1966 CA THR B 140 3.434 96.455 -37.026 1.00 10.22 ATOM 1967 C THR B 140 4.735 96.731 -37.764 1.00 10.78 ATOM 1968 O THR B 140 5.424 97.718 -37.508 1.00 10.37 ATOM 1969 CB THR B 140 3.592 95.116 -36.234 1.00 11.20 ATOM 1970 OG1 THR B 140 3.922 94.053 -37.120 1.00 10.26 ATOM 1971 CG2 THR B 140 2.394 94.746 -35.594 1.00 2.00 ATOM 1972 N ILE B 141 4.992 95.880 -38.747 1.00 11.81 ATOM 1973 CA ILE B 141 6.255 95.790 -39.452 1.00 10.72 ATOM 1974 C ILE B 141 5.875 95.830 -40.951 1.00 12.42 ATOM 1975 O ILE B 141 4.781 95.385 -41.355 1.00 7.30 ATOM 1976 CB ILE B 141 7.065 94.510 -39.006 1.00 11.91 ATOM 1977 CG1 ILE B 141 8.147 94.211 -40.039 1.00 8.86 ATOM 1978 CG2 ILE B 141 6.128 93.292 -38.739 1.00 12.28 ATOM 1979 CD1 ILE B 141 9.167 95.493 -40.257 1.00 3.62 ATOM 1980 N SER B 142 6.709 96.523 -41.742 1.00 14.48 ATOM 1981 CA SER B 142 6.628 96.591 -43.249 1.00 13.70 ATOM 1982 C SER B 142 8.025 96.659 -43.904 1.00 13.12 ATOM 1983 O SER B 142 8.828 97.511 -43.611 1.00 11.14 ATOM 1984 CB SER B 142 5.924 97.861 -43.653 1.00 15.53 ATOM 1985 OG SER B 142 4.702 98.005 -42.923 1.00 14.03 ATOM 1986 N PHE B 143 8.274 95.801 -44.875 1.00 11.99 ATOM 1987 CA PHE B 143 9.587 95.706 -45.468 1.00 11.37 ATOM 1988 C PHE B 143 9.326 95.531 -46.924 1.00 11.45 ATOM 1989 O PHE B 143 8.239 95.761 -47.315 1.00 12.79 ATOM 1990 CB PHE B 143 10.301 94.526 -44.890 1.00 10.71 ATOM 1991 CG PHE B 143 9.560 93.219 -45.002 1.00 9.49 ATOM 1992 CD1 PHE B 143 10.106 92.186 -45.648 1.00 18.65 ATOM 1993 CD2 PHE B 143 8.331 93.022 -44.396 1.00 19.43 ATOM 1994 CE1 PHE B 143 9.481 90.991 -45.773 1.00 12.40 ATOM 1995 CE2 PHE B 143 7.697 91.820 -44.463 1.00 19.98 ATOM 1996 CZ PHE B 143 8.272 90.796 -45.184 1.00 14.91 ATOM 1997 N GLU B 144 10.294 95.092 -47.693 1.00 13.00 ATOM 1998 CA GLU B 144 10.170 94.924 -49.116 1.00 14.00 ATOM 1999 C GLU B 144 10.976 93.757 -49.637 1.00 15.25 ATOM 2000 O GLU B 144 11.881 93.239 -49.002 1.00 15.56 ATOM 2001 CB GLU B 144 10.675 96.141 -49.862 1.00 15.88 ATOM 2002 CG GLU B 144 9.759 97.382 -49.850 1.00 16.61 ATOM 2003 CD GLU B 144 10.582 98.650 -50.076 1.00 25.88 ATOM 2004 OE1 GLU B 144 10.004 99.734 -50.402 1.00 24.45 ATOM 2005 OE2 GLU B 144 11.836 98.527 -49.921 1.00 27.33 ATOM 2006 N VAL B 145 10.655 93.342 -50.842 1.00 16.09 ATOM 2007 CA VAL B 145 11.274 92.161 -51.363 1.00 16.73 ATOM 2008 C VAL B 145 11.813 92.517 -52.690 1.00 16.25 ATOM 2009 O VAL B 145 11.346 93.406 -53.306 1.00 17.89 ATOM 2010 CB VAL B 145 10.275 91.022 -51.474 1.00 14.60 ATOM 2011 CG1 VAL B 145 9.897 90.667 -50.134 1.00 16.65 ATOM 2012 CG2 VAL B 145 8.988 91.435 -52.283 1.00 15.99 ATOM 2013 N GLN B 146 12.814 91.803 -53.152 1.00 17.11 ATOM 2014 CA GLN B 146 13.408 92.204 -54.403 1.00 15.52 ATOM 2015 C GLN B 146 13.434 91.066 -55.360 1.00 14.76 ATOM 2016 O GLN B 146 13.734 89.925 -54.991 1.00 12.62 ATOM 2017 CB GLN B 146 14.852 92.695 -54.164 1.00 15.29 ATOM 2018 CG GLN B 146 14.915 93.883 -53.203 1.00 15.56 ATOM 2019 CD GLN B 146 16.273 94.492 -53.179 1.00 18.50 ATOM 2020 OE1 GLN B 146 17.342 93.781 -53.079 1.00 18.79 ATOM 2021 NE2 GLN B 146 16.291 95.800 -53.332 1.00 18.71 ATOM 2022 N THR B 147 13.218 91.384 -56.629 1.00 14.53 ATOM 2023 CA THR B 147 13.246 90.289 -57.663 1.00 12.61 ATOM 2024 C THR B 147 13.786 90.853 -59.005 1.00 11.23 ATOM 2025 O THR B 147 13.910 92.079 -59.168 1.00 10.99 ATOM 2026 CB THR B 147 11.877 89.794 -57.949 1.00 11.13 ATOM 2027 OG1 THR B 147 11.982 88.639 -58.863 1.00 11.61 ATOM 2028 CG2 THR B 147 11.081 90.946 -58.616 1.00 5.83 ATOM 2029 N ASP B 148 14.115 89.978 -59.937 1.00 10.18 ATOM 2030 CA ASP B 148 14.563 90.373 -61.257 1.00 10.48 ATOM 2031 C ASP B 148 13.474 90.219 -62.298 1.00 11.60 ATOM 2032 O ASP B 148 13.622 90.804 -63.393 1.00 12.41 ATOM 2033 CB ASP B 148 15.841 89.592 -61.685 1.00 9.84 ATOM 2034 CG ASP B 148 15.558 88.075 -61.807 1.00 11.48 ATOM 2035 OD1 ASP B 148 16.421 87.265 -62.192 1.00 4.81 ATOM 2036 OD2 ASP B 148 14.466 87.683 -61.423 1.00 7.10 ATOM 2037 N LYS B 149 12.332 89.534 -61.997 1.00 11.88 ATOM 2038 CA LYS B 149 11.258 89.381 -62.974 1.00 10.08 ATOM 2039 C LYS B 149 10.382 90.661 -63.193 1.00 11.09 ATOM 2040 O LYS B 149 10.161 91.470 -62.235 1.00 12.10 ATOM 2041 CB LYS B 149 10.389 88.174 -62.594 1.00 11.55 ATOM 2042 CG LYS B 149 11.188 87.045 -61.819 1.00 7.50 ATOM 2043 CD LYS B 149 12.368 86.532 -62.637 1.00 2.00 ATOM 2044 CE LYS B 149 12.881 85.112 -62.243 1.00 3.24 ATOM 2045 NZ LYS B 149 13.152 84.927 -60.827 1.00 2.00 ATOM 2046 N LYS B 150 9.764 90.813 -64.379 1.00 10.58 ATOM 2047 CA LYS B 150 8.923 92.106 -64.677 1.00 9.53 ATOM 2048 C LYS B 150 7.539 91.632 -64.457 1.00 11.23 ATOM 2049 O LYS B 150 6.500 92.418 -64.529 1.00 10.14 ATOM 2050 CB LYS B 150 9.052 92.532 -66.136 1.00 4.52 ATOM 2051 CG LYS B 150 8.851 94.008 -66.451 1.00 13.20 ATOM 2052 CD LYS B 150 9.400 94.300 -67.839 1.00 9.55 ATOM 2053 CE LYS B 150 10.997 94.288 -67.822 1.00 4.98 ATOM 2054 NZ LYS B 150 11.424 94.556 -69.223 1.00 4.30 ATOM 2055 N SER B 151 7.503 90.300 -64.323 1.00 9.23 ATOM 2056 CA SER B 151 6.316 89.645 -63.928 1.00 10.30 ATOM 2057 C SER B 151 6.768 88.289 -63.338 1.00 11.72 ATOM 2058 O SER B 151 7.337 87.448 -64.084 1.00 8.10 ATOM 2059 CB SER B 151 5.377 89.450 -65.116 1.00 10.96 ATOM 2060 OG SER B 151 4.585 88.212 -64.909 1.00 14.65 ATOM 2061 N VAL B 152 6.455 88.057 -62.037 1.00 11.10 ATOM 2062 CA VAL B 152 7.048 86.941 -61.284 1.00 9.74 ATOM 2063 C VAL B 152 6.031 86.059 -60.641 1.00 10.99 ATOM 2064 O VAL B 152 4.885 86.505 -60.445 1.00 6.61 ATOM 2065 CB VAL B 152 7.801 87.481 -60.116 1.00 9.35 ATOM 2066 CG1 VAL B 152 6.878 88.376 -59.353 1.00 11.35 ATOM 2067 CG2 VAL B 152 8.253 86.384 -59.300 1.00 13.03 ATOM 2068 N THR B 153 6.510 84.848 -60.248 1.00 11.20 ATOM 2069 CA THR B 153 5.698 83.768 -59.709 1.00 11.26 ATOM 2070 C THR B 153 5.340 84.185 -58.299 1.00 12.21 ATOM 2071 O THR B 153 6.251 84.416 -57.503 1.00 12.96 ATOM 2072 CB THR B 153 6.433 82.432 -59.655 1.00 11.29 ATOM 2073 OG1 THR B 153 7.814 82.597 -59.311 1.00 11.34 ATOM 2074 CG2 THR B 153 6.466 81.805 -60.952 1.00 12.78 ATOM 2075 N ALA B 154 4.019 84.290 -57.955 1.00 12.08 ATOM 2076 CA ALA B 154 3.649 84.533 -56.565 1.00 9.26 ATOM 2077 C ALA B 154 4.533 83.702 -55.618 1.00 11.16 ATOM 2078 O ALA B 154 4.940 84.181 -54.553 1.00 12.36 ATOM 2079 CB ALA B 154 2.205 84.209 -56.320 1.00 9.88 ATOM 2080 N GLN B 155 4.785 82.440 -55.964 1.00 12.24 ATOM 2081 CA GLN B 155 5.619 81.588 -55.156 1.00 11.20 ATOM 2082 C GLN B 155 6.899 82.299 -54.858 1.00 11.78 ATOM 2083 O GLN B 155 7.191 82.525 -53.686 1.00 12.77 ATOM 2084 CB GLN B 155 5.908 80.251 -55.863 1.00 11.22 ATOM 2085 CG GLN B 155 6.855 79.389 -55.121 1.00 9.44 ATOM 2086 CD GLN B 155 6.851 78.024 -55.598 1.00 12.25 ATOM 2087 OE1 GLN B 155 7.563 77.137 -55.072 1.00 14.74 ATOM 2088 NE2 GLN B 155 6.021 77.785 -56.576 1.00 12.35 ATOM 2089 N GLU B 156 7.640 82.714 -55.879 1.00 12.68 ATOM 2090 CA GLU B 156 8.891 83.439 -55.654 1.00 11.50 ATOM 2091 C GLU B 156 8.637 84.443 -54.618 1.00 10.38 ATOM 2092 O GLU B 156 9.384 84.522 -53.634 1.00 12.43 ATOM 2093 CB GLU B 156 9.405 84.209 -56.862 1.00 11.73 ATOM 2094 CG GLU B 156 10.798 84.824 -56.532 1.00 10.22 ATOM 2095 CD GLU B 156 11.506 85.410 -57.710 1.00 10.70 ATOM 2096 OE1 GLU B 156 12.296 86.337 -57.499 1.00 10.68 ATOM 2097 OE2 GLU B 156 11.198 85.056 -58.862 1.00 10.69 ATOM 2098 N LEU B 157 7.605 85.247 -54.803 1.00 9.38 ATOM 2099 CA LEU B 157 7.452 86.402 -53.926 1.00 6.92 ATOM 2100 C LEU B 157 7.151 85.981 -52.523 1.00 9.33 ATOM 2101 O LEU B 157 7.821 86.443 -51.555 1.00 7.71 ATOM 2102 CB LEU B 157 6.296 87.275 -54.392 1.00 7.19 ATOM 2103 CG LEU B 157 6.432 88.273 -55.528 1.00 4.70 ATOM 2104 CD1 LEU B 157 5.233 89.109 -55.484 1.00 9.57 ATOM 2105 CD2 LEU B 157 7.750 89.060 -55.364 1.00 2.23 ATOM 2106 N ASP B 158 6.125 85.108 -52.393 1.00 6.81 ATOM 2107 CA ASP B 158 5.819 84.524 -51.116 1.00 9.26 ATOM 2108 C ASP B 158 7.054 84.005 -50.379 1.00 9.19 ATOM 2109 O ASP B 158 7.252 84.374 -49.231 1.00 8.82 ATOM 2110 CB ASP B 158 4.784 83.418 -51.365 1.00 11.98 ATOM 2111 CG ASP B 158 4.422 82.679 -50.145 1.00 16.30 ATOM 2112 OD1 ASP B 158 3.748 83.262 -49.219 1.00 14.32 ATOM 2113 OD2 ASP B 158 4.880 81.525 -50.123 1.00 19.46 ATOM 2114 N ILE B 159 7.863 83.122 -51.007 1.00 9.30 ATOM 2115 CA ILE B 159 8.998 82.477 -50.346 1.00 8.37 ATOM 2116 C ILE B 159 9.803 83.588 -49.644 1.00 10.33 ATOM 2117 O ILE B 159 9.997 83.623 -48.443 1.00 7.57 ATOM 2118 CB ILE B 159 9.929 81.735 -51.351 1.00 11.06 ATOM 2119 CG1 ILE B 159 9.363 80.388 -51.909 1.00 7.96 ATOM 2120 CG2 ILE B 159 11.177 81.314 -50.633 1.00 9.39 ATOM 2121 CD1 ILE B 159 7.844 80.183 -51.454 1.00 17.04 ATOM 2122 N LYS B 160 10.165 84.572 -50.452 1.00 11.82 ATOM 2123 CA LYS B 160 11.039 85.659 -50.114 1.00 11.64 ATOM 2124 C LYS B 160 10.470 86.359 -48.872 1.00 11.98 ATOM 2125 O LYS B 160 11.216 86.627 -47.920 1.00 12.74 ATOM 2126 CB LYS B 160 11.194 86.610 -51.340 1.00 12.67 ATOM 2127 CG LYS B 160 12.181 86.122 -52.431 1.00 9.61 ATOM 2128 CD LYS B 160 12.580 87.203 -53.487 1.00 11.23 ATOM 2129 CE LYS B 160 13.616 86.635 -54.541 1.00 9.99 ATOM 2130 NZ LYS B 160 14.115 87.376 -55.820 1.00 5.35 ATOM 2131 N ALA B 161 9.146 86.534 -48.838 1.00 12.01 ATOM 2132 CA ALA B 161 8.426 87.120 -47.715 1.00 11.13 ATOM 2133 C ALA B 161 8.716 86.295 -46.441 1.00 11.55 ATOM 2134 O ALA B 161 9.305 86.799 -45.452 1.00 9.66 ATOM 2135 CB ALA B 161 6.886 87.065 -48.056 1.00 12.32 ATOM 2136 N ARG B 162 8.197 85.055 -46.442 1.00 11.54 ATOM 2137 CA ARG B 162 8.422 84.079 -45.400 1.00 9.79 ATOM 2138 C ARG B 162 9.892 83.993 -44.978 1.00 9.42 ATOM 2139 O ARG B 162 10.168 84.068 -43.811 1.00 10.61 ATOM 2140 CB ARG B 162 7.896 82.740 -45.885 1.00 10.88 ATOM 2141 CG ARG B 162 6.352 82.681 -45.804 1.00 13.06 ATOM 2142 CD ARG B 162 5.850 81.273 -46.220 1.00 10.66 ATOM 2143 NE ARG B 162 4.394 81.194 -46.520 1.00 10.75 ATOM 2144 CZ ARG B 162 3.785 80.040 -46.788 1.00 9.56 ATOM 2145 NH1 ARG B 162 4.494 78.951 -46.798 1.00 8.33 ATOM 2146 NH2 ARG B 162 2.508 79.945 -47.064 1.00 10.35 ATOM 2147 N ASN B 163 10.835 83.795 -45.876 1.00 10.21 ATOM 2148 CA ASN B 163 12.235 83.716 -45.525 1.00 12.67 ATOM 2149 C ASN B 163 12.604 84.864 -44.587 1.00 15.05 ATOM 2150 O ASN B 163 13.316 84.622 -43.558 1.00 17.57 ATOM 2151 CB ASN B 163 13.070 83.786 -46.788 1.00 14.36 ATOM 2152 CG ASN B 163 14.512 83.980 -46.551 1.00 14.15 ATOM 2153 OD1 ASN B 163 15.211 83.055 -46.280 1.00 11.96 ATOM 2154 ND2 ASN B 163 15.004 85.206 -46.822 1.00 24.48 ATOM 2155 N PHE B 164 12.080 86.093 -44.849 1.00 15.44 ATOM 2156 CA PHE B 164 12.399 87.286 -44.019 1.00 15.88 ATOM 2157 C PHE B 164 11.749 87.102 -42.681 1.00 16.37 ATOM 2158 O PHE B 164 12.455 87.126 -41.657 1.00 16.67 ATOM 2159 CB PHE B 164 11.861 88.609 -44.588 1.00 17.00 ATOM 2160 CG PHE B 164 12.462 89.877 -43.968 1.00 14.90 ATOM 2161 CD1 PHE B 164 13.725 90.325 -44.338 1.00 13.56 ATOM 2162 CD2 PHE B 164 11.668 90.727 -43.203 1.00 15.63 ATOM 2163 CE1 PHE B 164 14.224 91.559 -43.866 1.00 13.87 ATOM 2164 CE2 PHE B 164 12.157 91.868 -42.730 1.00 19.60 ATOM 2165 CZ PHE B 164 13.479 92.294 -43.064 1.00 18.93 ATOM 2166 N LEU B 165 10.410 86.953 -42.669 1.00 15.37 ATOM 2167 CA LEU B 165 9.702 86.666 -41.401 1.00 13.55 ATOM 2168 C LEU B 165 10.424 85.562 -40.539 1.00 13.06 ATOM 2169 O LEU B 165 10.520 85.713 -39.307 1.00 11.08 ATOM 2170 CB LEU B 165 8.245 86.377 -41.674 1.00 13.17 ATOM 2171 CG LEU B 165 7.361 87.729 -41.740 1.00 13.02 ATOM 2172 CD1 LEU B 165 8.178 89.013 -41.878 1.00 11.78 ATOM 2173 CD2 LEU B 165 6.474 87.628 -42.851 1.00 6.61 ATOM 2174 N ILE B 166 10.884 84.469 -41.152 1.00 11.42 ATOM 2175 CA ILE B 166 11.692 83.493 -40.416 1.00 11.67 ATOM 2176 C ILE B 166 12.885 84.313 -39.938 1.00 10.13 ATOM 2177 O ILE B 166 13.040 84.607 -38.744 1.00 10.32 ATOM 2178 CB ILE B 166 12.252 82.345 -41.291 1.00 11.20 ATOM 2179 CG1 ILE B 166 11.249 81.284 -41.675 1.00 11.84 ATOM 2180 CG2 ILE B 166 13.248 81.641 -40.507 1.00 11.60 ATOM 2181 CD1 ILE B 166 9.884 81.831 -42.041 1.00 22.91 ATOM 2182 N ASN B 167 13.770 84.714 -40.837 1.00 11.87 ATOM 2183 CA ASN B 167 14.978 85.474 -40.340 1.00 14.05 ATOM 2184 C ASN B 167 14.829 86.695 -39.391 1.00 12.90 ATOM 2185 O ASN B 167 15.831 87.273 -38.896 1.00 13.51 ATOM 2186 CB ASN B 167 15.834 85.843 -41.520 1.00 14.78 ATOM 2187 CG ASN B 167 16.375 84.558 -42.230 1.00 19.05 ATOM 2188 OD1 ASN B 167 15.645 83.560 -42.347 1.00 14.46 ATOM 2189 ND2 ASN B 167 17.676 84.566 -42.610 1.00 19.30 ATOM 2190 N LYS B 168 13.615 87.148 -39.125 1.00 11.26 ATOM 2191 CA LYS B 168 13.500 88.395 -38.258 1.00 11.77 ATOM 2192 C LYS B 168 12.337 88.450 -37.256 1.00 12.15 ATOM 2193 O LYS B 168 12.322 89.311 -36.316 1.00 12.84 ATOM 2194 CB LYS B 168 13.505 89.680 -39.095 1.00 9.20 ATOM 2195 CG LYS B 168 14.681 89.812 -40.078 1.00 10.37 ATOM 2196 CD LYS B 168 15.794 90.757 -39.535 1.00 8.01 ATOM 2197 CE LYS B 168 17.213 90.346 -40.138 1.00 15.79 ATOM 2198 NZ LYS B 168 17.281 88.821 -40.091 1.00 16.18 ATOM 2199 N LYS B 169 11.339 87.613 -37.467 1.00 13.05 ATOM 2200 CA LYS B 169 10.094 87.567 -36.613 1.00 12.54 ATOM 2201 C LYS B 169 9.630 86.120 -36.246 1.00 13.48 ATOM 2202 O LYS B 169 8.418 85.868 -35.965 1.00 10.89 ATOM 2203 CB LYS B 169 8.916 88.327 -37.262 1.00 13.42 ATOM 2204 CG LYS B 169 8.749 89.804 -36.680 1.00 17.03 ATOM 2205 CD LYS B 169 7.947 89.896 -35.456 1.00 14.89 ATOM 2206 CE LYS B 169 7.454 91.335 -35.199 1.00 16.37 ATOM 2207 NZ LYS B 169 6.425 91.315 -34.085 1.00 15.63 ATOM 2208 N ASN B 170 10.593 85.201 -36.191 1.00 12.08 ATOM 2209 CA ASN B 170 10.322 83.812 -35.828 1.00 12.48 ATOM 2210 C ASN B 170 9.004 83.244 -36.324 1.00 12.71 ATOM 2211 O ASN B 170 8.240 82.589 -35.537 1.00 14.21 ATOM 2212 CB ASN B 170 10.468 83.548 -34.334 1.00 11.37 ATOM 2213 CG ASN B 170 11.920 83.693 -33.827 1.00 17.78 ATOM 2214 OD1 ASN B 170 12.516 84.844 -33.851 1.00 15.93 ATOM 2215 ND2 ASN B 170 12.530 82.540 -33.361 1.00 15.97 ATOM 2216 N LEU B 171 8.770 83.362 -37.618 1.00 12.00 ATOM 2217 CA LEU B 171 7.446 82.934 -38.152 1.00 13.94 ATOM 2218 C LEU B 171 7.249 81.443 -37.909 1.00 12.54 ATOM 2219 O LEU B 171 6.137 81.008 -37.725 1.00 12.15 ATOM 2220 CB LEU B 171 7.261 83.317 -39.637 1.00 13.40 ATOM 2221 CG LEU B 171 6.274 82.567 -40.512 1.00 14.34 ATOM 2222 CD1 LEU B 171 4.844 83.009 -40.145 1.00 7.49 ATOM 2223 CD2 LEU B 171 6.735 82.999 -41.949 1.00 8.00 ATOM 2224 N TYR B 172 8.341 80.728 -37.855 1.00 10.81 ATOM 2225 CA TYR B 172 8.365 79.256 -37.737 1.00 11.68 ATOM 2226 C TYR B 172 9.645 79.034 -36.906 1.00 12.20 ATOM 2227 O TYR B 172 10.677 79.740 -37.096 1.00 10.17 ATOM 2228 CB TYR B 172 8.570 78.541 -39.088 1.00 11.85 ATOM 2229 CG TYR B 172 7.468 78.762 -40.131 1.00 9.76 ATOM 2230 CD1 TYR B 172 7.741 79.149 -41.451 1.00 7.06 ATOM 2231 CD2 TYR B 172 6.145 78.621 -39.779 1.00 10.34 ATOM 2232 CE1 TYR B 172 6.648 79.451 -42.338 1.00 9.66 ATOM 2233 CE2 TYR B 172 5.073 78.813 -40.713 1.00 4.52 ATOM 2234 CZ TYR B 172 5.331 79.239 -41.922 1.00 7.82 ATOM 2235 OH TYR B 172 4.253 79.404 -42.710 1.00 8.43 ATOM 2236 N GLU B 173 9.500 78.171 -35.925 1.00 10.42 ATOM 2237 CA GLU B 173 10.576 77.696 -35.098 1.00 10.75 ATOM 2238 C GLU B 173 10.569 76.151 -35.102 1.00 8.85 ATOM 2239 O GLU B 173 9.491 75.561 -35.281 1.00 8.01 ATOM 2240 CB GLU B 173 10.446 78.222 -33.678 1.00 10.73 ATOM 2241 CG GLU B 173 11.265 79.448 -33.450 1.00 12.19 ATOM 2242 CD GLU B 173 11.168 80.039 -32.022 1.00 15.69 ATOM 2243 OE1 GLU B 173 10.013 80.268 -31.509 1.00 15.58 ATOM 2244 OE2 GLU B 173 12.274 80.389 -31.525 1.00 12.51 ATOM 2245 N PHE B 174 11.758 75.549 -34.925 1.00 6.15 ATOM 2246 CA PHE B 174 11.932 74.151 -34.929 1.00 8.07 ATOM 2247 C PHE B 174 10.870 73.308 -34.207 1.00 9.68 ATOM 2248 O PHE B 174 10.626 72.209 -34.646 1.00 9.78 ATOM 2249 CB PHE B 174 13.303 73.732 -34.570 1.00 7.52 ATOM 2250 CG PHE B 174 13.510 72.266 -34.568 1.00 5.79 ATOM 2251 CD1 PHE B 174 14.065 71.623 -35.663 1.00 14.25 ATOM 2252 CD2 PHE B 174 13.263 71.536 -33.446 1.00 9.44 ATOM 2253 CE1 PHE B 174 14.391 70.235 -35.653 1.00 10.77 ATOM 2254 CE2 PHE B 174 13.485 70.101 -33.390 1.00 10.57 ATOM 2255 CZ PHE B 174 14.040 69.450 -34.497 1.00 12.18 ATOM 2256 N ASN B 175 10.204 73.806 -33.170 1.00 12.47 ATOM 2257 CA ASN B 175 9.083 73.005 -32.528 1.00 13.00 ATOM 2258 C ASN B 175 7.697 73.473 -32.777 1.00 12.75 ATOM 2259 O ASN B 175 6.675 72.740 -32.556 1.00 16.51 ATOM 2260 CB ASN B 175 9.316 72.909 -31.030 1.00 12.93 ATOM 2261 CG ASN B 175 10.835 72.902 -30.648 1.00 19.64 ATOM 2262 OD1 ASN B 175 11.562 73.894 -30.895 1.00 24.36 ATOM 2263 ND2 ASN B 175 11.309 71.787 -30.048 1.00 18.24 ATOM 2264 N SER B 176 7.597 74.751 -33.083 1.00 12.74 ATOM 2265 CA SER B 176 6.358 75.376 -33.393 1.00 12.21 ATOM 2266 C SER B 176 6.504 76.858 -33.733 1.00 12.97 ATOM 2267 O SER B 176 7.577 77.313 -34.215 1.00 13.11 ATOM 2268 CB SER B 176 5.358 75.164 -32.278 1.00 14.14 ATOM 2269 OG SER B 176 4.137 75.662 -32.658 1.00 7.94 ATOM 2270 N SER B 177 5.427 77.594 -33.519 1.00 10.45 ATOM 2271 CA SER B 177 5.393 79.010 -33.915 1.00 12.73 ATOM 2272 C SER B 177 4.541 79.885 -32.965 1.00 12.63 ATOM 2273 O SER B 177 3.448 79.464 -32.507 1.00 11.87 ATOM 2274 CB SER B 177 4.833 79.114 -35.350 1.00 12.31 ATOM 2275 OG SER B 177 5.052 80.370 -35.936 1.00 11.70 ATOM 2276 N PRO B 178 5.080 81.076 -32.644 1.00 12.02 ATOM 2277 CA PRO B 178 4.547 82.091 -31.802 1.00 9.04 ATOM 2278 C PRO B 178 3.199 82.494 -32.270 1.00 8.64 ATOM 2279 O PRO B 178 2.496 83.197 -31.526 1.00 10.15 ATOM 2280 CB PRO B 178 5.504 83.279 -32.044 1.00 6.82 ATOM 2281 CG PRO B 178 6.732 82.693 -32.542 1.00 10.75 ATOM 2282 CD PRO B 178 6.362 81.497 -33.266 1.00 10.69 ATOM 2283 N TYR B 179 2.828 82.127 -33.485 1.00 8.35 ATOM 2284 CA TYR B 179 1.535 82.531 -34.083 1.00 7.55 ATOM 2285 C TYR B 179 0.545 81.338 -34.147 1.00 9.22 ATOM 2286 O TYR B 179 0.978 80.119 -34.091 1.00 7.45 ATOM 2287 CB TYR B 179 1.749 83.185 -35.439 1.00 7.94 ATOM 2288 CG TYR B 179 2.835 84.308 -35.407 1.00 9.55 ATOM 2289 CD1 TYR B 179 4.125 84.015 -35.696 1.00 4.63 ATOM 2290 CD2 TYR B 179 2.489 85.691 -35.052 1.00 5.68 ATOM 2291 CE1 TYR B 179 5.148 85.040 -35.661 1.00 9.84 ATOM 2292 CE2 TYR B 179 3.437 86.672 -35.060 1.00 10.92 ATOM 2293 CZ TYR B 179 4.731 86.347 -35.363 1.00 7.69 ATOM 2294 OH TYR B 179 5.601 87.296 -35.362 1.00 11.82 ATOM 2295 N GLU B 180 -0.758 81.659 -34.154 1.00 7.58 ATOM 2296 CA GLU B 180 -1.771 80.611 -34.103 1.00 8.20 ATOM 2297 C GLU B 180 -2.225 80.392 -35.524 1.00 9.69 ATOM 2298 O GLU B 180 -2.495 79.213 -35.937 1.00 12.55 ATOM 2299 CB GLU B 180 -2.968 81.073 -33.226 1.00 9.88 ATOM 2300 CG GLU B 180 -4.214 80.055 -33.074 1.00 7.74 ATOM 2301 CD GLU B 180 -3.815 78.698 -32.652 1.00 14.00 ATOM 2302 OE1 GLU B 180 -4.718 77.859 -32.381 1.00 13.19 ATOM 2303 OE2 GLU B 180 -2.594 78.441 -32.539 1.00 14.28 ATOM 2304 N THR B 181 -2.340 81.495 -36.291 1.00 7.35 ATOM 2305 CA THR B 181 -2.758 81.443 -37.668 1.00 5.80 ATOM 2306 C THR B 181 -2.063 82.479 -38.501 1.00 8.40 ATOM 2307 O THR B 181 -1.553 83.505 -37.992 1.00 8.91 ATOM 2308 CB THR B 181 -4.217 81.805 -37.857 1.00 6.75 ATOM 2309 OG1 THR B 181 -4.375 83.227 -37.709 1.00 3.57 ATOM 2310 CG2 THR B 181 -5.036 81.183 -36.781 1.00 9.08 ATOM 2311 N GLY B 182 -2.142 82.311 -39.822 1.00 10.56 ATOM 2312 CA GLY B 182 -1.544 83.286 -40.758 1.00 10.08 ATOM 2313 C GLY B 182 -1.610 82.947 -42.226 1.00 9.33 ATOM 2314 O GLY B 182 -1.493 81.779 -42.637 1.00 11.90 ATOM 2315 N TYR B 183 -1.868 83.965 -43.020 1.00 10.65 ATOM 2316 CA TYR B 183 -2.120 83.795 -44.454 1.00 9.89 ATOM 2317 C TYR B 183 -1.543 84.942 -45.226 1.00 8.57 ATOM 2318 O TYR B 183 -1.530 86.077 -44.750 1.00 9.83 ATOM 2319 CB TYR B 183 -3.624 83.631 -44.720 1.00 9.39 ATOM 2320 CG TYR B 183 -4.399 84.770 -44.286 1.00 8.52 ATOM 2321 CD1 TYR B 183 -4.479 85.875 -45.086 1.00 11.80 ATOM 2322 CD2 TYR B 183 -5.080 84.771 -43.095 1.00 10.88 ATOM 2323 CE1 TYR B 183 -5.115 86.953 -44.720 1.00 6.52 ATOM 2324 CE2 TYR B 183 -5.779 85.899 -42.704 1.00 12.75 ATOM 2325 CZ TYR B 183 -5.731 87.021 -43.535 1.00 11.06 ATOM 2326 OH TYR B 183 -6.374 88.211 -43.253 1.00 7.67 ATOM 2327 N ILE B 184 -1.031 84.654 -46.405 1.00 9.90 ATOM 2328 CA ILE B 184 -0.388 85.700 -47.205 1.00 10.65 ATOM 2329 C ILE B 184 -1.317 86.012 -48.368 1.00 11.31 ATOM 2330 O ILE B 184 -1.555 85.121 -49.199 1.00 11.43 ATOM 2331 CB ILE B 184 1.035 85.376 -47.623 1.00 9.55 ATOM 2332 CG1 ILE B 184 1.540 86.523 -48.481 1.00 11.59 ATOM 2333 CG2 ILE B 184 1.133 84.079 -48.420 1.00 7.45 ATOM 2334 CD1 ILE B 184 3.055 86.502 -48.734 1.00 2.00 ATOM 2335 N LYS B 185 -1.922 87.214 -48.352 1.00 11.47 ATOM 2336 CA LYS B 185 -2.835 87.668 -49.404 1.00 10.17 ATOM 2337 C LYS B 185 -2.159 88.672 -50.310 1.00 10.31 ATOM 2338 O LYS B 185 -1.532 89.563 -49.758 1.00 9.95 ATOM 2339 CB LYS B 185 -4.051 88.357 -48.798 1.00 9.79 ATOM 2340 CG LYS B 185 -4.768 89.267 -49.747 1.00 6.30 ATOM 2341 CD LYS B 185 -5.563 90.327 -48.982 1.00 10.91 ATOM 2342 CE LYS B 185 -6.862 89.796 -48.284 1.00 7.86 ATOM 2343 NZ LYS B 185 -7.989 89.703 -49.318 1.00 5.30 ATOM 2344 N PHE B 186 -2.414 88.522 -51.635 1.00 9.12 ATOM 2345 CA PHE B 186 -1.964 89.335 -52.784 1.00 10.62 ATOM 2346 C PHE B 186 -3.098 90.156 -53.455 1.00 12.24 ATOM 2347 O PHE B 186 -4.298 89.748 -53.549 1.00 10.76 ATOM 2348 CB PHE B 186 -1.213 88.516 -53.906 1.00 9.75 ATOM 2349 CG PHE B 186 0.022 87.762 -53.438 1.00 9.80 ATOM 2350 CD1 PHE B 186 -0.134 86.622 -52.682 1.00 11.65 ATOM 2351 CD2 PHE B 186 1.306 88.160 -53.817 1.00 3.11 ATOM 2352 CE1 PHE B 186 0.994 85.877 -52.255 1.00 16.27 ATOM 2353 CE2 PHE B 186 2.389 87.450 -53.410 1.00 15.26 ATOM 2354 CZ PHE B 186 2.244 86.292 -52.600 1.00 6.63 ATOM 2355 N ILE B 187 -2.700 91.335 -53.942 1.00 11.90 ATOM 2356 CA ILE B 187 -3.582 92.250 -54.580 1.00 12.57 ATOM 2357 C ILE B 187 -3.041 92.600 -55.941 1.00 14.79 ATOM 2358 O ILE B 187 -1.846 93.039 -56.077 1.00 16.42 ATOM 2359 CB ILE B 187 -3.715 93.431 -53.735 1.00 13.01 ATOM 2360 CG1 ILE B 187 -4.226 93.007 -52.311 1.00 16.00 ATOM 2361 CG2 ILE B 187 -4.758 94.386 -54.373 1.00 15.42 ATOM 2362 CD1 ILE B 187 -4.528 94.141 -51.308 1.00 10.51 ATOM 2363 N GLU B 188 -3.836 92.355 -56.982 1.00 15.05 ATOM 2364 CA GLU B 188 -3.408 92.707 -58.334 1.00 14.95 ATOM 2365 C GLU B 188 -4.027 94.071 -58.816 1.00 19.36 ATOM 2366 O GLU B 188 -5.206 94.374 -58.606 1.00 18.43 ATOM 2367 CB GLU B 188 -3.804 91.576 -59.273 1.00 17.01 ATOM 2368 CG GLU B 188 -2.806 90.476 -59.373 1.00 12.13 ATOM 2369 CD GLU B 188 -3.221 89.365 -60.378 1.00 13.05 ATOM 2370 OE1 GLU B 188 -4.321 88.737 -60.229 1.00 10.21 ATOM 2371 OE2 GLU B 188 -2.443 89.176 -61.327 1.00 10.67 ATOM 2372 N ASN B 189 -3.182 94.892 -59.418 1.00 19.45 ATOM 2373 CA ASN B 189 -3.527 96.195 -59.949 1.00 20.35 ATOM 2374 C ASN B 189 -4.976 96.278 -60.436 1.00 20.82 ATOM 2375 O ASN B 189 -5.691 97.232 -60.105 1.00 20.40 ATOM 2376 CB ASN B 189 -2.462 96.539 -61.019 1.00 20.40 ATOM 2377 CG ASN B 189 -2.371 97.982 -61.313 1.00 22.90 ATOM 2378 OD1 ASN B 189 -1.446 98.399 -62.053 1.00 19.48 ATOM 2379 ND2 ASN B 189 -3.348 98.783 -60.807 1.00 20.53 ATOM 2380 N ASN B 190 -5.448 95.201 -61.065 1.00 22.20 ATOM 2381 CA ASN B 190 -6.825 95.098 -61.558 1.00 24.24 ATOM 2382 C ASN B 190 -7.914 95.023 -60.459 1.00 24.69 ATOM 2383 O ASN B 190 -9.077 95.542 -60.629 1.00 25.12 ATOM 2384 CB ASN B 190 -6.974 93.922 -62.575 1.00 22.98 ATOM 2385 CG ASN B 190 -6.899 92.603 -61.943 1.00 24.78 ATOM 2386 OD1 ASN B 190 -7.526 92.379 -60.912 1.00 22.45 ATOM 2387 ND2 ASN B 190 -6.111 91.662 -62.565 1.00 29.35 ATOM 2388 N GLY B 191 -7.535 94.384 -59.353 1.00 23.82 ATOM 2389 CA GLY B 191 -8.432 94.063 -58.212 1.00 23.15 ATOM 2390 C GLY B 191 -8.493 92.564 -57.899 1.00 22.31 ATOM 2391 O GLY B 191 -9.385 92.085 -57.250 1.00 22.97 ATOM 2392 N ASN B 192 -7.533 91.811 -58.346 1.00 21.65 ATOM 2393 CA ASN B 192 -7.634 90.412 -58.000 1.00 22.72 ATOM 2394 C ASN B 192 -6.888 90.259 -56.722 1.00 21.77 ATOM 2395 O ASN B 192 -5.828 90.871 -56.502 1.00 22.82 ATOM 2396 CB ASN B 192 -7.213 89.485 -59.140 1.00 22.16 ATOM 2397 CG ASN B 192 -7.340 88.019 -58.780 1.00 23.83 ATOM 2398 OD1 ASN B 192 -8.445 87.499 -58.582 1.00 28.16 ATOM 2399 ND2 ASN B 192 -6.202 87.341 -58.688 1.00 15.99 ATOM 2400 N THR B 193 -7.516 89.556 -55.813 1.00 22.25 ATOM 2401 CA THR B 193 -6.939 89.344 -54.528 1.00 23.00 ATOM 2402 C THR B 193 -7.088 87.890 -54.172 1.00 22.98 ATOM 2403 O THR B 193 -8.237 87.347 -54.187 1.00 23.92 ATOM 2404 CB THR B 193 -7.653 90.154 -53.441 1.00 24.01 ATOM 2405 OG1 THR B 193 -9.071 89.922 -53.495 1.00 27.20 ATOM 2406 CG2 THR B 193 -7.330 91.673 -53.524 1.00 25.14 ATOM 2407 N PHE B 194 -5.977 87.264 -53.775 1.00 20.38 ATOM 2408 CA PHE B 194 -6.001 85.844 -53.397 1.00 19.18 ATOM 2409 C PHE B 194 -5.067 85.592 -52.208 1.00 18.89 ATOM 2410 O PHE B 194 -4.134 86.334 -51.997 1.00 21.99 ATOM 2411 CB PHE B 194 -5.628 84.944 -54.586 1.00 17.29 ATOM 2412 CG PHE B 194 -4.247 85.218 -55.194 1.00 18.77 ATOM 2413 CD1 PHE B 194 -3.169 84.380 -54.924 1.00 12.76 ATOM 2414 CD2 PHE B 194 -4.047 86.286 -56.084 1.00 13.96 ATOM 2415 CE1 PHE B 194 -1.951 84.623 -55.515 1.00 11.06 ATOM 2416 CE2 PHE B 194 -2.787 86.529 -56.635 1.00 12.71 ATOM 2417 CZ PHE B 194 -1.763 85.671 -56.366 1.00 8.39 ATOM 2418 N TRP B 195 -5.338 84.619 -51.381 1.00 17.64 ATOM 2419 CA TRP B 195 -4.539 84.404 -50.150 1.00 16.18 ATOM 2420 C TRP B 195 -4.153 82.918 -50.037 1.00 15.37 ATOM 2421 O TRP B 195 -4.823 82.064 -50.592 1.00 17.63 ATOM 2422 CB TRP B 195 -5.301 84.892 -48.904 1.00 15.52 ATOM 2423 CG TRP B 195 -6.663 84.153 -48.565 1.00 13.57 ATOM 2424 CD1 TRP B 195 -7.938 84.485 -48.996 1.00 16.11 ATOM 2425 CD2 TRP B 195 -6.810 83.005 -47.748 1.00 13.94 ATOM 2426 NE1 TRP B 195 -8.883 83.587 -48.487 1.00 12.09 ATOM 2427 CE2 TRP B 195 -8.210 82.663 -47.730 1.00 11.99 ATOM 2428 CE3 TRP B 195 -5.912 82.179 -47.097 1.00 11.60 ATOM 2429 CZ2 TRP B 195 -8.672 81.627 -47.067 1.00 11.51 ATOM 2430 CZ3 TRP B 195 -6.395 81.122 -46.421 1.00 17.58 ATOM 2431 CH2 TRP B 195 -7.790 80.877 -46.369 1.00 14.64 ATOM 2432 N TYR B 196 -3.187 82.614 -49.215 1.00 14.57 ATOM 2433 CA TYR B 196 -2.660 81.260 -49.076 1.00 12.19 ATOM 2434 C TYR B 196 -2.391 81.016 -47.588 1.00 13.35 ATOM 2435 O TYR B 196 -1.703 81.832 -46.938 1.00 13.23 ATOM 2436 CB TYR B 196 -1.325 81.064 -49.838 1.00 12.78 ATOM 2437 CG TYR B 196 -1.362 81.122 -51.385 1.00 11.28 ATOM 2438 CD1 TYR B 196 -0.232 81.508 -52.105 1.00 7.94 ATOM 2439 CD2 TYR B 196 -2.517 80.777 -52.105 1.00 10.80 ATOM 2440 CE1 TYR B 196 -0.243 81.564 -53.451 1.00 9.77 ATOM 2441 CE2 TYR B 196 -2.571 80.869 -53.487 1.00 8.96 ATOM 2442 CZ TYR B 196 -1.388 81.261 -54.156 1.00 14.65 ATOM 2443 OH TYR B 196 -1.393 81.334 -55.542 1.00 12.98 ATOM 2444 N ASP B 197 -2.894 79.903 -47.033 1.00 11.14 ATOM 2445 CA ASP B 197 -2.708 79.655 -45.619 1.00 11.60 ATOM 2446 C ASP B 197 -1.246 79.357 -45.326 1.00 11.07 ATOM 2447 O ASP B 197 -0.588 78.761 -46.133 1.00 12.24 ATOM 2448 CB ASP B 197 -3.616 78.517 -45.132 1.00 10.08 ATOM 2449 CG ASP B 197 -3.393 78.176 -43.664 1.00 14.64 ATOM 2450 OD1 ASP B 197 -2.209 78.129 -43.204 1.00 19.92 ATOM 2451 OD2 ASP B 197 -4.376 77.867 -42.955 1.00 18.48 ATOM 2452 N MET B 198 -0.742 79.757 -44.170 1.00 12.07 ATOM 2453 CA MET B 198 0.727 79.527 -43.850 1.00 11.16 ATOM 2454 C MET B 198 0.926 78.434 -42.884 1.00 11.82 ATOM 2455 O MET B 198 2.065 77.960 -42.729 1.00 9.95 ATOM 2456 CB MET B 198 1.388 80.779 -43.383 1.00 7.16 ATOM 2457 CG MET B 198 0.996 81.883 -44.351 1.00 8.30 ATOM 2458 SD MET B 198 1.492 83.513 -43.744 1.00 9.06 ATOM 2459 CE MET B 198 3.287 83.563 -43.783 1.00 2.00 ATOM 2460 N MET B 199 -0.184 78.031 -42.249 1.00 12.91 ATOM 2461 CA MET B 199 -0.064 77.067 -41.224 1.00 15.02 ATOM 2462 C MET B 199 -0.478 75.681 -41.652 1.00 16.65 ATOM 2463 O MET B 199 -1.454 75.492 -42.412 1.00 19.44 ATOM 2464 CB MET B 199 -0.720 77.528 -39.935 1.00 13.49 ATOM 2465 CG MET B 199 -0.201 78.796 -39.427 1.00 11.97 ATOM 2466 SD MET B 199 1.350 78.591 -38.589 1.00 13.57 ATOM 2467 CE MET B 199 1.680 80.312 -38.301 1.00 8.73 ATOM 2468 N PRO B 200 0.288 74.679 -41.195 1.00 17.16 ATOM 2469 CA PRO B 200 0.032 73.273 -41.338 1.00 16.01 ATOM 2470 C PRO B 200 -1.377 72.760 -41.071 1.00 17.27 ATOM 2471 O PRO B 200 -2.319 73.473 -40.633 1.00 17.12 ATOM 2472 CB PRO B 200 1.001 72.626 -40.355 1.00 16.46 ATOM 2473 CG PRO B 200 2.214 73.558 -40.387 1.00 14.67 ATOM 2474 CD PRO B 200 1.551 74.971 -40.464 1.00 17.02 ATOM 2475 N ALA B 201 -1.540 71.493 -41.378 1.00 15.58 ATOM 2476 CA ALA B 201 -2.863 70.939 -41.396 1.00 17.17 ATOM 2477 C ALA B 201 -3.114 70.473 -39.966 1.00 18.46 ATOM 2478 O ALA B 201 -2.181 69.919 -39.361 1.00 20.88 ATOM 2479 CB ALA B 201 -2.815 69.737 -42.273 1.00 17.09 ATOM 2480 N PRO B 202 -4.355 70.567 -39.454 1.00 16.86 ATOM 2481 CA PRO B 202 -4.566 70.282 -38.124 1.00 16.02 ATOM 2482 C PRO B 202 -4.383 68.790 -37.988 1.00 16.82 ATOM 2483 O PRO B 202 -5.291 68.064 -38.297 1.00 17.69 ATOM 2484 CB PRO B 202 -6.027 70.705 -37.918 1.00 12.96 ATOM 2485 CG PRO B 202 -6.672 70.356 -39.075 1.00 13.52 ATOM 2486 CD PRO B 202 -5.649 70.868 -40.091 1.00 20.01 ATOM 2487 N GLY B 203 -3.168 68.355 -37.621 1.00 18.95 ATOM 2488 CA GLY B 203 -2.881 66.987 -37.126 1.00 19.31 ATOM 2489 C GLY B 203 -1.470 66.626 -36.655 1.00 20.74 ATOM 2490 O GLY B 203 -0.637 67.490 -36.252 1.00 21.35 ATOM 2491 N ASP B 204 -1.169 65.332 -36.660 1.00 21.37 ATOM 2492 CA ASP B 204 0.117 64.865 -36.115 1.00 22.31 ATOM 2493 C ASP B 204 1.356 65.057 -36.952 1.00 21.10 ATOM 2494 O ASP B 204 2.421 65.302 -36.395 1.00 20.39 ATOM 2495 CB ASP B 204 0.038 63.364 -35.820 1.00 23.43 ATOM 2496 CG ASP B 204 1.406 62.788 -35.466 1.00 29.29 ATOM 2497 OD1 ASP B 204 2.103 63.400 -34.634 1.00 25.43 ATOM 2498 OD2 ASP B 204 1.788 61.713 -36.016 1.00 35.50 ATOM 2499 N LYS B 205 1.253 64.780 -38.266 1.00 21.26 ATOM 2500 CA LYS B 205 2.385 64.893 -39.228 1.00 19.07 ATOM 2501 C LYS B 205 2.184 65.936 -40.311 1.00 16.65 ATOM 2502 O LYS B 205 1.121 66.441 -40.483 1.00 14.45 ATOM 2503 CB LYS B 205 2.831 63.549 -39.839 1.00 20.05 ATOM 2504 CG LYS B 205 1.670 62.561 -40.116 1.00 24.18 ATOM 2505 CD LYS B 205 1.331 61.766 -38.850 1.00 21.21 ATOM 2506 CE LYS B 205 0.100 60.838 -39.050 1.00 23.66 ATOM 2507 NZ LYS B 205 0.010 59.948 -37.824 1.00 18.16 ATOM 2508 N PHE B 206 3.242 66.235 -41.061 1.00 14.82 ATOM 2509 CA PHE B 206 3.137 67.215 -42.131 1.00 13.57 ATOM 2510 C PHE B 206 3.690 66.705 -43.463 1.00 13.13 ATOM 2511 O PHE B 206 4.897 66.556 -43.586 1.00 14.61 ATOM 2512 CB PHE B 206 3.972 68.471 -41.702 1.00 11.00 ATOM 2513 CG PHE B 206 4.048 69.531 -42.709 1.00 10.52 ATOM 2514 CD1 PHE B 206 2.886 70.012 -43.328 1.00 5.52 ATOM 2515 CD2 PHE B 206 5.278 70.093 -43.038 1.00 8.57 ATOM 2516 CE1 PHE B 206 2.972 71.070 -44.134 1.00 9.40 ATOM 2517 CE2 PHE B 206 5.354 71.122 -43.857 1.00 5.77 ATOM 2518 CZ PHE B 206 4.172 71.631 -44.437 1.00 4.76 ATOM 2519 N ASP B 207 2.852 66.444 -44.474 1.00 14.31 ATOM 2520 CA ASP B 207 3.382 66.066 -45.781 1.00 12.10 ATOM 2521 C ASP B 207 3.919 67.366 -46.431 1.00 13.28 ATOM 2522 O ASP B 207 3.152 68.192 -46.951 1.00 11.62 ATOM 2523 CB ASP B 207 2.239 65.477 -46.568 1.00 11.84 ATOM 2524 CG ASP B 207 2.604 65.072 -47.969 1.00 14.12 ATOM 2525 OD1 ASP B 207 3.819 65.021 -48.280 1.00 20.54 ATOM 2526 OD2 ASP B 207 1.653 64.838 -48.794 1.00 16.80 ATOM 2527 N GLN B 208 5.249 67.519 -46.462 1.00 12.94 ATOM 2528 CA GLN B 208 5.846 68.678 -47.079 1.00 12.07 ATOM 2529 C GLN B 208 5.292 68.909 -48.441 1.00 14.28 ATOM 2530 O GLN B 208 4.488 69.855 -48.699 1.00 16.38 ATOM 2531 CB GLN B 208 7.343 68.518 -47.118 1.00 13.83 ATOM 2532 CG GLN B 208 8.076 69.250 -45.963 1.00 8.93 ATOM 2533 CD GLN B 208 9.522 68.700 -45.880 1.00 7.81 ATOM 2534 OE1 GLN B 208 10.449 69.331 -45.329 1.00 2.00 ATOM 2535 NE2 GLN B 208 9.706 67.572 -46.534 1.00 7.76 ATOM 2536 N SER B 209 5.549 67.949 -49.281 1.00 13.28 ATOM 2537 CA SER B 209 4.976 67.974 -50.609 1.00 14.95 ATOM 2538 C SER B 209 3.596 68.558 -50.733 1.00 15.05 ATOM 2539 O SER B 209 3.413 69.708 -51.100 1.00 15.66 ATOM 2540 CB SER B 209 4.884 66.623 -51.212 1.00 14.51 ATOM 2541 OG SER B 209 4.184 66.790 -52.450 1.00 20.02 ATOM 2542 N LYS B 210 2.629 67.688 -50.540 1.00 13.77 ATOM 2543 CA LYS B 210 1.213 68.094 -50.713 1.00 12.46 ATOM 2544 C LYS B 210 0.881 69.486 -50.315 1.00 8.67 ATOM 2545 O LYS B 210 -0.174 69.981 -50.687 1.00 8.86 ATOM 2546 CB LYS B 210 0.316 67.149 -49.895 1.00 10.27 ATOM 2547 CG LYS B 210 -1.092 67.083 -50.390 1.00 10.90 ATOM 2548 CD LYS B 210 -2.095 66.676 -49.232 1.00 11.44 ATOM 2549 CE LYS B 210 -3.580 66.439 -49.764 1.00 14.70 ATOM 2550 NZ LYS B 210 -4.473 66.155 -48.636 1.00 13.56 ATOM 2551 N TYR B 211 1.706 70.096 -49.468 1.00 10.54 ATOM 2552 CA TYR B 211 1.443 71.515 -49.057 1.00 7.88 ATOM 2553 C TYR B 211 1.711 72.318 -50.290 1.00 8.59 ATOM 2554 O TYR B 211 0.925 73.263 -50.746 1.00 11.87 ATOM 2555 CB TYR B 211 2.347 71.974 -47.907 1.00 7.91 ATOM 2556 CG TYR B 211 2.248 73.541 -47.516 1.00 9.48 ATOM 2557 CD1 TYR B 211 1.033 74.114 -47.060 1.00 2.42 ATOM 2558 CD2 TYR B 211 3.315 74.389 -47.688 1.00 5.30 ATOM 2559 CE1 TYR B 211 0.899 75.421 -46.669 1.00 2.05 ATOM 2560 CE2 TYR B 211 3.187 75.795 -47.393 1.00 7.64 ATOM 2561 CZ TYR B 211 1.964 76.276 -46.875 1.00 8.61 ATOM 2562 OH TYR B 211 1.790 77.577 -46.600 1.00 7.48 ATOM 2563 N LEU B 212 2.870 72.048 -50.850 1.00 7.58 ATOM 2564 CA LEU B 212 3.405 72.839 -51.971 1.00 5.40 ATOM 2565 C LEU B 212 2.632 72.655 -53.177 1.00 8.42 ATOM 2566 O LEU B 212 2.670 73.494 -54.063 1.00 12.22 ATOM 2567 CB LEU B 212 4.817 72.454 -52.247 1.00 4.90 ATOM 2568 CG LEU B 212 5.906 72.763 -51.202 1.00 2.14 ATOM 2569 CD1 LEU B 212 7.193 72.208 -51.542 1.00 10.84 ATOM 2570 CD2 LEU B 212 6.169 74.388 -51.135 1.00 5.79 ATOM 2571 N MET B 213 1.842 71.572 -53.271 1.00 9.17 ATOM 2572 CA MET B 213 1.198 71.298 -54.517 1.00 5.98 ATOM 2573 C MET B 213 0.358 72.535 -54.882 1.00 6.67 ATOM 2574 O MET B 213 -0.136 72.676 -55.997 1.00 8.57 ATOM 2575 CB MET B 213 0.327 70.158 -54.313 1.00 2.70 ATOM 2576 CG MET B 213 -0.485 69.890 -55.450 1.00 5.38 ATOM 2577 SD MET B 213 -1.040 68.218 -55.292 1.00 10.00 ATOM 2578 CE MET B 213 0.675 67.411 -55.231 1.00 7.05 ATOM 2579 N MET B 214 0.114 73.410 -53.931 1.00 6.76 ATOM 2580 CA MET B 214 -0.600 74.596 -54.245 1.00 5.62 ATOM 2581 C MET B 214 0.100 75.546 -55.204 1.00 8.62 ATOM 2582 O MET B 214 -0.545 76.605 -55.666 1.00 7.46 ATOM 2583 CB MET B 214 -0.940 75.403 -53.004 1.00 7.43 ATOM 2584 CG MET B 214 0.189 75.926 -52.127 1.00 5.09 ATOM 2585 SD MET B 214 -0.177 76.922 -50.685 1.00 3.90 ATOM 2586 CE MET B 214 0.893 78.406 -51.057 1.00 7.67 ATOM 2587 N TYR B 215 1.355 75.241 -55.536 1.00 6.55 ATOM 2588 CA TYR B 215 2.067 76.214 -56.352 1.00 8.24 ATOM 2589 C TYR B 215 2.055 75.738 -57.767 1.00 10.44 ATOM 2590 O TYR B 215 2.719 76.301 -58.669 1.00 9.45 ATOM 2591 CB TYR B 215 3.489 76.556 -55.873 1.00 9.46 ATOM 2592 CG TYR B 215 3.640 77.347 -54.574 1.00 9.98 ATOM 2593 CD1 TYR B 215 4.463 76.871 -53.521 1.00 13.26 ATOM 2594 CD2 TYR B 215 2.891 78.498 -54.349 1.00 12.80 ATOM 2595 CE1 TYR B 215 4.586 77.611 -52.313 1.00 11.10 ATOM 2596 CE2 TYR B 215 3.009 79.237 -53.144 1.00 7.24 ATOM 2597 CZ TYR B 215 3.863 78.800 -52.158 1.00 6.83 ATOM 2598 OH TYR B 215 3.966 79.535 -50.972 1.00 6.01 ATOM 2599 N ASN B 216 1.207 74.743 -58.027 1.00 10.11 ATOM 2600 CA ASN B 216 1.243 74.184 -59.366 1.00 10.42 ATOM 2601 C ASN B 216 0.340 74.921 -60.396 1.00 11.37 ATOM 2602 O ASN B 216 0.157 74.494 -61.556 1.00 12.14 ATOM 2603 CB ASN B 216 1.003 72.660 -59.234 1.00 10.99 ATOM 2604 CG ASN B 216 -0.493 72.295 -58.845 1.00 7.94 ATOM 2605 OD1 ASN B 216 -0.880 71.187 -59.046 1.00 8.88 ATOM 2606 ND2 ASN B 216 -1.276 73.223 -58.348 1.00 7.90 ATOM 2607 N ASP B 217 -0.208 76.049 -59.971 1.00 13.41 ATOM 2608 CA ASP B 217 -1.109 76.814 -60.818 1.00 13.47 ATOM 2609 C ASP B 217 -0.190 77.876 -61.500 1.00 13.44 ATOM 2610 O ASP B 217 -0.605 78.774 -62.232 1.00 8.95 ATOM 2611 CB ASP B 217 -2.173 77.474 -59.928 1.00 14.77 ATOM 2612 CG ASP B 217 -1.604 78.561 -59.073 1.00 18.29 ATOM 2613 OD1 ASP B 217 -0.357 78.599 -59.004 1.00 25.18 ATOM 2614 OD2 ASP B 217 -2.360 79.387 -58.522 1.00 15.38 ATOM 2615 N ASN B 218 1.119 77.716 -61.246 1.00 13.79 ATOM 2616 CA ASN B 218 2.083 78.640 -61.731 1.00 11.63 ATOM 2617 C ASN B 218 1.623 80.062 -61.868 1.00 14.18 ATOM 2618 O ASN B 218 1.977 80.681 -62.792 1.00 16.15 ATOM 2619 CB ASN B 218 2.554 78.205 -63.054 1.00 12.01 ATOM 2620 CG ASN B 218 3.987 78.680 -63.272 1.00 13.18 ATOM 2621 OD1 ASN B 218 4.903 78.223 -62.578 1.00 10.21 ATOM 2622 ND2 ASN B 218 4.161 79.674 -64.107 1.00 7.20 ATOM 2623 N LYS B 219 0.784 80.555 -60.967 1.00 13.83 ATOM 2624 CA LYS B 219 0.125 81.773 -61.130 1.00 13.39 ATOM 2625 C LYS B 219 1.207 82.778 -60.997 1.00 14.08 ATOM 2626 O LYS B 219 2.116 82.609 -60.161 1.00 16.86 ATOM 2627 CB LYS B 219 -0.855 82.027 -59.962 1.00 13.32 ATOM 2628 CG LYS B 219 -1.266 83.523 -59.806 1.00 10.67 ATOM 2629 CD LYS B 219 -1.971 84.122 -61.071 1.00 2.64 ATOM 2630 CE LYS B 219 -2.428 85.720 -60.820 1.00 6.33 ATOM 2631 NZ LYS B 219 -3.811 85.804 -60.273 1.00 9.10 ATOM 2632 N THR B 220 1.132 83.796 -61.845 1.00 12.34 ATOM 2633 CA THR B 220 2.051 84.948 -61.885 1.00 13.14 ATOM 2634 C THR B 220 1.331 86.328 -61.557 1.00 11.83 ATOM 2635 O THR B 220 0.035 86.521 -61.610 1.00 6.57 ATOM 2636 CB THR B 220 2.628 85.189 -63.283 1.00 11.29 ATOM 2637 OG1 THR B 220 1.735 84.675 -64.246 1.00 16.36 ATOM 2638 CG2 THR B 220 4.031 84.648 -63.482 1.00 15.28 ATOM 2639 N VAL B 221 2.205 87.279 -61.336 1.00 9.47 ATOM 2640 CA VAL B 221 1.804 88.642 -60.939 1.00 8.96 ATOM 2641 C VAL B 221 2.805 89.735 -61.425 1.00 9.26 ATOM 2642 O VAL B 221 3.969 89.454 -61.744 1.00 7.29 ATOM 2643 CB VAL B 221 1.740 88.729 -59.432 1.00 8.07 ATOM 2644 CG1 VAL B 221 0.413 88.178 -58.892 1.00 6.23 ATOM 2645 CG2 VAL B 221 2.885 88.058 -58.844 1.00 8.07 ATOM 2646 N ASP B 222 2.354 90.999 -61.458 1.00 11.10 ATOM 2647 CA ASP B 222 3.230 92.030 -62.042 1.00 11.38 ATOM 2648 C ASP B 222 3.928 92.799 -60.967 1.00 10.59 ATOM 2649 O ASP B 222 3.290 93.658 -60.236 1.00 10.88 ATOM 2650 CB ASP B 222 2.458 92.942 -62.994 1.00 11.31 ATOM 2651 CG ASP B 222 3.159 94.290 -63.216 1.00 18.61 ATOM 2652 OD1 ASP B 222 4.402 94.328 -63.651 1.00 12.76 ATOM 2653 OD2 ASP B 222 2.437 95.315 -62.949 1.00 20.55 ATOM 2654 N SER B 223 5.202 92.484 -60.775 1.00 11.01 ATOM 2655 CA SER B 223 6.008 93.167 -59.706 1.00 10.81 ATOM 2656 C SER B 223 5.680 94.662 -59.588 1.00 13.01 ATOM 2657 O SER B 223 4.861 95.098 -58.779 1.00 12.28 ATOM 2658 CB SER B 223 7.431 92.954 -60.035 1.00 12.80 ATOM 2659 OG SER B 223 7.714 93.692 -61.198 1.00 17.99 ATOM 2660 N LYS B 224 6.293 95.493 -60.391 1.00 16.57 ATOM 2661 CA LYS B 224 6.027 96.970 -60.347 1.00 18.61 ATOM 2662 C LYS B 224 4.662 97.474 -59.806 1.00 17.45 ATOM 2663 O LYS B 224 4.496 98.671 -59.496 1.00 22.39 ATOM 2664 CB LYS B 224 6.328 97.627 -61.715 1.00 17.57 ATOM 2665 CG LYS B 224 5.840 99.108 -61.832 1.00 22.56 ATOM 2666 CD LYS B 224 6.607 100.035 -60.888 1.00 30.04 ATOM 2667 CE LYS B 224 8.134 99.942 -61.100 1.00 30.69 ATOM 2668 NZ LYS B 224 8.574 100.785 -62.276 1.00 30.96 ATOM 2669 N SER B 225 3.700 96.620 -59.636 1.00 15.93 ATOM 2670 CA SER B 225 2.383 97.129 -59.155 1.00 16.39 ATOM 2671 C SER B 225 1.743 96.430 -58.047 1.00 13.02 ATOM 2672 O SER B 225 1.368 97.084 -57.074 1.00 16.98 ATOM 2673 CB SER B 225 1.304 97.240 -60.229 1.00 15.75 ATOM 2674 OG SER B 225 0.888 95.949 -60.640 1.00 23.80 ATOM 2675 N VAL B 226 1.532 95.163 -58.206 1.00 12.07 ATOM 2676 CA VAL B 226 1.080 94.194 -57.144 1.00 12.12 ATOM 2677 C VAL B 226 1.634 94.647 -55.829 1.00 13.26 ATOM 2678 O VAL B 226 2.795 95.206 -55.740 1.00 15.27 ATOM 2679 CB VAL B 226 1.664 92.740 -57.401 1.00 10.62 ATOM 2680 CG1 VAL B 226 3.105 92.644 -57.014 1.00 12.40 ATOM 2681 CG2 VAL B 226 0.975 91.629 -56.666 1.00 12.97 ATOM 2682 N LYS B 227 0.829 94.417 -54.801 1.00 14.79 ATOM 2683 CA LYS B 227 1.127 94.757 -53.375 1.00 13.32 ATOM 2684 C LYS B 227 0.797 93.482 -52.514 1.00 11.92 ATOM 2685 O LYS B 227 -0.144 92.773 -52.855 1.00 9.07 ATOM 2686 CB LYS B 227 0.244 95.971 -52.941 1.00 10.36 ATOM 2687 CG LYS B 227 -1.236 95.816 -53.245 1.00 12.29 ATOM 2688 CD LYS B 227 -2.001 97.269 -53.303 1.00 16.29 ATOM 2689 CE LYS B 227 -1.117 98.384 -54.076 1.00 17.98 ATOM 2690 NZ LYS B 227 -1.848 99.652 -54.281 1.00 21.46 ATOM 2691 N ILE B 228 1.511 93.278 -51.387 1.00 12.84 ATOM 2692 CA ILE B 228 1.363 92.065 -50.474 1.00 12.66 ATOM 2693 C ILE B 228 0.868 92.391 -49.090 1.00 11.62 ATOM 2694 O ILE B 228 1.163 93.494 -48.570 1.00 9.82 ATOM 2695 CB ILE B 228 2.649 91.385 -50.356 1.00 11.44 ATOM 2696 CG1 ILE B 228 3.085 91.087 -51.804 1.00 17.05 ATOM 2697 CG2 ILE B 228 2.432 90.020 -49.796 1.00 14.63 ATOM 2698 CD1 ILE B 228 4.582 90.906 -51.983 1.00 27.71 ATOM 2699 N GLU B 229 0.051 91.488 -48.552 1.00 8.09 ATOM 2700 CA GLU B 229 -0.319 91.548 -47.203 1.00 8.55 ATOM 2701 C GLU B 229 -0.230 90.210 -46.470 1.00 10.16 ATOM 2702 O GLU B 229 -0.815 89.166 -46.918 1.00 8.76 ATOM 2703 CB GLU B 229 -1.793 92.008 -47.080 1.00 8.11 ATOM 2704 CG GLU B 229 -1.987 93.457 -47.591 1.00 5.95 ATOM 2705 CD GLU B 229 -3.473 94.015 -47.374 1.00 9.38 ATOM 2706 OE1 GLU B 229 -4.138 93.522 -46.464 1.00 4.16 ATOM 2707 OE2 GLU B 229 -3.928 94.948 -48.149 1.00 5.72 ATOM 2708 N VAL B 230 0.441 90.271 -45.317 1.00 9.23 ATOM 2709 CA VAL B 230 0.472 89.129 -44.411 1.00 10.18 ATOM 2710 C VAL B 230 -0.299 89.382 -43.165 1.00 10.18 ATOM 2711 O VAL B 230 -0.392 90.540 -42.669 1.00 7.88 ATOM 2712 CB VAL B 230 1.900 88.713 -44.098 1.00 9.33 ATOM 2713 CG1 VAL B 230 1.911 87.345 -43.637 1.00 11.38 ATOM 2714 CG2 VAL B 230 2.678 88.721 -45.378 1.00 6.10 ATOM 2715 N HIS B 231 -0.999 88.328 -42.715 1.00 10.47 ATOM 2716 CA HIS B 231 -1.878 88.492 -41.562 1.00 7.93 ATOM 2717 C HIS B 231 -1.788 87.438 -40.479 1.00 9.90 ATOM 2718 O HIS B 231 -2.104 86.235 -40.706 1.00 7.96 ATOM 2719 CB HIS B 231 -3.308 88.687 -42.003 1.00 10.05 ATOM 2720 CG HIS B 231 -3.514 89.873 -42.884 1.00 4.45 ATOM 2721 ND1 HIS B 231 -3.540 91.167 -42.386 1.00 14.17 ATOM 2722 CD2 HIS B 231 -3.743 89.978 -44.205 1.00 8.07 ATOM 2723 CE1 HIS B 231 -3.814 92.023 -43.367 1.00 11.46 ATOM 2724 NE2 HIS B 231 -3.921 91.338 -44.496 1.00 9.52 ATOM 2725 N LEU B 232 -1.347 87.908 -39.281 1.00 9.33 ATOM 2726 CA LEU B 232 -1.211 87.048 -38.168 1.00 10.79 ATOM 2727 C LEU B 232 -1.990 87.322 -36.867 1.00 11.53 ATOM 2728 O LEU B 232 -2.351 88.432 -36.581 1.00 9.61 ATOM 2729 CB LEU B 232 0.289 86.905 -37.838 1.00 6.58 ATOM 2730 CG LEU B 232 1.204 87.014 -39.059 1.00 6.26 ATOM 2731 CD1 LEU B 232 2.639 87.509 -38.690 1.00 2.00 ATOM 2732 CD2 LEU B 232 1.300 85.699 -39.770 1.00 8.32 ATOM 2733 N THR B 233 -2.050 86.274 -36.041 1.00 13.55 ATOM 2734 CA THR B 233 -2.766 86.244 -34.802 1.00 17.69 ATOM 2735 C THR B 233 -1.963 85.429 -33.839 1.00 18.51 ATOM 2736 O THR B 233 -1.586 84.272 -34.110 1.00 18.86 ATOM 2737 CB THR B 233 -4.114 85.683 -34.921 1.00 15.29 ATOM 2738 OG1 THR B 233 -4.012 84.454 -35.648 1.00 22.65 ATOM 2739 CG2 THR B 233 -5.033 86.635 -35.675 1.00 16.54 ATOM 2740 N THR B 234 -1.686 86.088 -32.721 1.00 21.39 ATOM 2741 CA THR B 234 -0.809 85.565 -31.717 1.00 24.25 ATOM 2742 C THR B 234 -1.483 84.491 -30.955 1.00 24.47 ATOM 2743 O THR B 234 -2.715 84.347 -30.992 1.00 26.05 ATOM 2744 CB THR B 234 -0.389 86.652 -30.788 1.00 24.84 ATOM 2745 OG1 THR B 234 0.167 87.710 -31.570 1.00 25.92 ATOM 2746 CG2 THR B 234 0.698 86.127 -29.884 1.00 31.82 ATOM 2747 N LYS B 235 -0.671 83.665 -30.317 1.00 26.23 ATOM 2748 CA LYS B 235 -1.160 82.497 -29.579 1.00 25.36 ATOM 2749 C LYS B 235 -1.798 83.077 -28.343 1.00 26.05 ATOM 2750 O LYS B 235 -2.684 83.934 -28.437 1.00 26.41 ATOM 2751 CB LYS B 235 0.022 81.665 -29.110 1.00 24.60 ATOM 2752 CG LYS B 235 0.453 80.518 -30.001 1.00 28.91 ATOM 2753 CD LYS B 235 -0.485 79.259 -29.947 1.00 27.15 ATOM 2754 CE LYS B 235 0.151 78.062 -30.780 1.00 23.19 ATOM 2755 NZ LYS B 235 1.588 77.709 -30.374 1.00 24.48