ATOM 1 N GLY A 140 6.170 0.397 17.875 1.00127.32 ATOM 2 CA GLY A 140 4.886 -0.087 18.322 1.00127.09 ATOM 3 C GLY A 140 3.727 0.719 17.814 1.00126.80 ATOM 4 O GLY A 140 3.857 1.463 16.839 1.00127.16 ATOM 5 N ALA A 141 2.584 0.591 18.476 1.00122.00 ATOM 6 CA ALA A 141 1.385 1.331 18.096 1.00121.09 ATOM 7 C ALA A 141 1.554 2.822 18.361 1.00120.71 ATOM 8 O ALA A 141 1.034 3.655 17.614 1.00120.00 ATOM 9 CB ALA A 141 0.197 0.802 18.865 1.00119.37 ATOM 10 N LEU A 142 2.282 3.148 19.422 1.00127.35 ATOM 11 CA LEU A 142 2.530 4.539 19.801 1.00126.93 ATOM 12 C LEU A 142 3.699 5.150 19.027 1.00127.03 ATOM 13 O LEU A 142 3.780 6.369 18.889 1.00127.07 ATOM 14 CB LEU A 142 2.786 4.637 21.311 1.00119.15 ATOM 15 CG LEU A 142 3.798 3.695 21.977 1.00118.30 ATOM 16 CD1 LEU A 142 4.121 4.197 23.376 1.00117.71 ATOM 17 CD2 LEU A 142 3.251 2.272 22.030 1.00117.05 ATOM 18 N GLU A 143 4.592 4.294 18.531 1.00126.19 ATOM 19 CA GLU A 143 5.754 4.751 17.775 1.00125.60 ATOM 20 C GLU A 143 5.423 5.112 16.329 1.00124.28 ATOM 21 O GLU A 143 5.955 6.076 15.783 1.00124.10 ATOM 22 CB GLU A 143 6.848 3.678 17.782 1.00129.12 ATOM 23 CG GLU A 143 7.624 3.553 19.079 1.00131.12 ATOM 24 CD GLU A 143 6.777 3.059 20.237 1.00132.20 ATOM 25 OE1 GLU A 143 6.242 1.935 20.140 1.00132.49 ATOM 26 OE2 GLU A 143 6.652 3.797 21.239 1.00133.14 ATOM 27 N SER A 144 4.549 4.331 15.704 1.00123.67 ATOM 28 CA SER A 144 4.162 4.563 14.320 1.00121.31 ATOM 29 C SER A 144 3.134 5.685 14.196 1.00119.55 ATOM 30 O SER A 144 2.861 6.169 13.093 1.00119.44 ATOM 31 CB SER A 144 3.609 3.279 13.702 1.00115.90 ATOM 32 OG SER A 144 3.352 3.445 12.315 1.00115.73 ATOM 33 N LEU A 145 2.558 6.092 15.324 1.00111.57 ATOM 34 CA LEU A 145 1.563 7.156 15.339 1.00108.21 ATOM 35 C LEU A 145 2.293 8.484 15.483 1.00106.25 ATOM 36 O LEU A 145 1.916 9.494 14.875 1.00105.88 ATOM 37 CB LEU A 145 0.602 6.971 16.517 1.00100.42 ATOM 38 CG LEU A 145 -0.787 7.575 16.422 1.00 99.45 ATOM 39 CD1 LEU A 145 -1.522 7.324 17.730 1.00 98.74 ATOM 40 CD2 LEU A 145 -0.711 9.066 16.129 1.00 98.14 ATOM 41 N ARG A 146 3.351 8.482 16.287 1.00100.89 ATOM 42 CA ARG A 146 4.158 9.671 16.529 1.00 98.77 ATOM 43 C ARG A 146 4.901 10.082 15.268 1.00 97.33 ATOM 44 O ARG A 146 5.113 11.267 15.025 1.00 96.80 ATOM 45 CB ARG A 146 5.170 9.400 17.642 1.00100.37 ATOM 46 CG ARG A 146 4.567 9.178 19.013 1.00101.08 ATOM 47 CD ARG A 146 5.612 8.649 19.988 1.00101.88 ATOM 48 NE ARG A 146 5.767 9.508 21.159 1.00101.90 ATOM 49 CZ ARG A 146 6.281 10.734 21.129 1.00101.96 ATOM 50 NH1 ARG A 146 6.687 11.254 19.980 1.00101.06 ATOM 51 NH2 ARG A 146 6.385 11.438 22.245 1.00102.43 ATOM 52 N GLY A 147 5.314 9.098 14.482 1.00102.69 ATOM 53 CA GLY A 147 6.040 9.386 13.269 1.00100.67 ATOM 54 C GLY A 147 5.172 9.605 12.044 1.00 98.88 ATOM 55 O GLY A 147 5.523 10.396 11.168 1.00 99.78 ATOM 56 N ASN A 148 4.042 8.921 11.984 1.00 86.38 ATOM 57 CA ASN A 148 3.126 9.040 10.853 1.00 83.82 ATOM 58 C ASN A 148 2.879 10.506 10.489 1.00 82.20 ATOM 59 O ASN A 148 2.077 11.186 11.124 1.00 81.17 ATOM 60 CB ASN A 148 1.803 8.357 11.187 1.00 87.20 ATOM 61 CG ASN A 148 1.002 8.028 9.945 1.00 87.97 ATOM 62 OD1 ASN A 148 0.761 8.888 9.093 1.00 87.37 ATOM 63 ND2 ASN A 148 0.565 6.778 9.836 1.00 88.41 ATOM 64 N ALA A 149 3.576 10.978 9.462 1.00 87.32 ATOM 65 CA ALA A 149 3.451 12.363 9.007 1.00 85.17 ATOM 66 C ALA A 149 2.045 12.704 8.568 1.00 83.25 ATOM 67 O ALA A 149 1.721 13.870 8.329 1.00 83.23 ATOM 68 CB ALA A 149 4.423 12.618 7.867 1.00 76.55 ATOM 69 N ASP A 150 1.208 11.691 8.442 1.00 78.05 ATOM 70 CA ASP A 150 -0.142 11.918 8.038 1.00 75.37 ATOM 71 C ASP A 150 -1.027 12.063 9.270 1.00 71.34 ATOM 72 O ASP A 150 -2.068 12.720 9.218 1.00 71.34 ATOM 73 CB ASP A 150 -0.644 10.755 7.175 1.00 92.77 ATOM 74 CG ASP A 150 0.063 10.676 5.844 1.00 95.31 ATOM 75 OD1 ASP A 150 -0.040 11.644 5.061 1.00 96.08 ATOM 76 OD2 ASP A 150 0.703 9.651 5.588 1.00 96.38 ATOM 77 N LEU A 151 -0.594 11.472 10.382 1.00 62.26 ATOM 78 CA LEU A 151 -1.367 11.518 11.617 1.00 58.36 ATOM 79 C LEU A 151 -0.843 12.467 12.691 1.00 54.69 ATOM 80 O LEU A 151 -1.609 12.931 13.529 1.00 53.83 ATOM 81 CB LEU A 151 -1.479 10.104 12.196 1.00 65.40 ATOM 82 CG LEU A 151 -2.023 9.059 11.224 1.00 67.11 ATOM 83 CD1 LEU A 151 -2.105 7.708 11.914 1.00 67.59 ATOM 84 CD2 LEU A 151 -3.391 9.486 10.718 1.00 66.73 ATOM 85 N ALA A 152 0.431 12.755 12.662 1.00 53.69 ATOM 86 CA ALA A 152 1.026 13.634 13.659 1.00 50.08 ATOM 87 C ALA A 152 1.877 14.727 13.038 1.00 48.47 ATOM 88 O ALA A 152 2.551 14.493 12.045 1.00 48.67 ATOM 89 CB ALA A 152 1.861 12.818 14.635 1.00 31.29 ATOM 90 N TYR A 153 1.833 15.920 13.621 1.00 40.16 ATOM 91 CA TYR A 153 2.634 17.016 13.130 1.00 39.26 ATOM 92 C TYR A 153 4.068 16.619 13.396 1.00 40.09 ATOM 93 O TYR A 153 4.362 15.988 14.410 1.00 39.19 ATOM 94 CB TYR A 153 2.336 18.310 13.898 1.00 39.90 ATOM 95 CG TYR A 153 0.984 18.905 13.639 1.00 37.22 ATOM 96 CD1 TYR A 153 0.685 19.524 12.427 1.00 36.84 ATOM 97 CD2 TYR A 153 0.009 18.847 14.609 1.00 34.92 ATOM 98 CE1 TYR A 153 -0.546 20.076 12.188 1.00 34.85 ATOM 99 CE2 TYR A 153 -1.239 19.387 14.382 1.00 34.88 ATOM 100 CZ TYR A 153 -1.521 20.002 13.166 1.00 35.36 ATOM 101 OH TYR A 153 -2.775 20.524 12.950 1.00 33.45 ATOM 102 N ILE A 154 4.970 16.975 12.489 1.00 46.72 ATOM 103 CA ILE A 154 6.364 16.632 12.692 1.00 49.35 ATOM 104 C ILE A 154 7.037 17.752 13.467 1.00 50.34 ATOM 105 O ILE A 154 7.130 18.881 12.991 1.00 48.58 ATOM 106 CB ILE A 154 7.108 16.434 11.364 1.00 61.26 ATOM 107 CG1 ILE A 154 6.436 15.339 10.544 1.00 62.57 ATOM 108 CG2 ILE A 154 8.560 16.061 11.640 1.00 62.19 ATOM 109 CD1 ILE A 154 6.397 13.988 11.240 1.00 64.28 ATOM 110 N LEU A 155 7.480 17.430 14.679 1.00 67.46 ATOM 111 CA LEU A 155 8.178 18.385 15.534 1.00 68.65 ATOM 112 C LEU A 155 9.587 17.836 15.722 1.00 70.78 ATOM 113 O LEU A 155 9.889 17.205 16.733 1.00 72.98 ATOM 114 CB LEU A 155 7.472 18.527 16.887 1.00 43.54 ATOM 115 CG LEU A 155 6.470 19.691 16.991 1.00 42.52 ATOM 116 CD1 LEU A 155 5.314 19.503 16.032 1.00 37.48 ATOM 117 CD2 LEU A 155 5.970 19.786 18.417 1.00 40.55 ATOM 118 N SER A 156 10.444 18.086 14.737 1.00 62.47 ATOM 119 CA SER A 156 11.818 17.605 14.762 1.00 62.49 ATOM 120 C SER A 156 12.859 18.710 14.893 1.00 62.37 ATOM 121 O SER A 156 13.990 18.453 15.320 1.00 64.89 ATOM 122 CB SER A 156 12.108 16.809 13.489 1.00 55.97 ATOM 123 OG SER A 156 12.002 17.651 12.350 1.00 56.48 ATOM 124 N MET A 156A 12.489 19.927 14.534 1.00 46.92 ATOM 125 CA MET A 156A 13.419 21.050 14.601 1.00 47.35 ATOM 126 C MET A 156A 13.847 21.449 16.013 1.00 47.67 ATOM 127 O MET A 156A 13.114 21.252 16.989 1.00 47.12 ATOM 128 CB MET A 156A 12.830 22.261 13.881 1.00 57.23 ATOM 129 CG MET A 156A 12.621 22.047 12.399 1.00 58.57 ATOM 130 SD MET A 156A 14.151 21.550 11.577 1.00 58.59 ATOM 131 CE MET A 156A 15.002 23.128 11.467 1.00 57.23 ATOM 132 N GLU A 161 15.042 22.024 16.101 1.00 54.22 ATOM 133 CA GLU A 161 15.605 22.462 17.368 1.00 55.50 ATOM 134 C GLU A 161 16.194 23.863 17.177 1.00 51.69 ATOM 135 O GLU A 161 17.195 24.023 16.489 1.00 52.28 ATOM 136 CB GLU A 161 16.710 21.498 17.794 1.00 89.49 ATOM 137 CG GLU A 161 17.223 21.722 19.195 1.00 98.01 ATOM 138 CD GLU A 161 16.147 21.462 20.225 1.00103.22 ATOM 139 OE1 GLU A 161 15.609 20.339 20.243 1.00106.45 ATOM 140 OE2 GLU A 161 15.853 22.396 21.011 1.00105.46 ATOM 141 N PRO A 162 15.582 24.896 17.795 1.00 48.80 ATOM 142 CA PRO A 162 14.397 24.892 18.652 1.00 45.33 ATOM 143 C PRO A 162 13.090 24.535 17.933 1.00 41.56 ATOM 144 O PRO A 162 13.014 24.588 16.713 1.00 41.46 ATOM 145 CB PRO A 162 14.389 26.325 19.207 1.00 47.43 ATOM 146 CG PRO A 162 14.931 27.109 18.074 1.00 47.29 ATOM 147 CD PRO A 162 16.108 26.261 17.636 1.00 49.24 ATOM 148 N CYS A 162A 12.074 24.177 18.714 1.00 39.29 ATOM 149 CA CYS A 162A 10.768 23.795 18.178 1.00 34.91 ATOM 150 C CYS A 162A 9.978 24.983 17.640 1.00 30.97 ATOM 151 O CYS A 162A 9.297 24.872 16.620 1.00 27.77 ATOM 152 CB CYS A 162A 9.939 23.089 19.253 1.00 37.34 ATOM 153 SG CYS A 162A 8.355 22.441 18.662 1.00 39.57 ATOM 154 N GLY A 163 10.063 26.115 18.331 1.00 30.23 ATOM 155 CA GLY A 163 9.357 27.295 17.879 1.00 30.52 ATOM 156 C GLY A 163 9.384 28.354 18.953 1.00 29.72 ATOM 157 O GLY A 163 10.080 28.200 19.956 1.00 32.47 ATOM 158 N HIS A 164 8.648 29.433 18.730 1.00 29.16 ATOM 159 CA HIS A 164 8.572 30.510 19.707 1.00 30.34 ATOM 160 C HIS A 164 7.467 30.209 20.703 1.00 29.50 ATOM 161 O HIS A 164 6.521 29.478 20.407 1.00 30.76 ATOM 162 CB HIS A 164 8.229 31.845 19.025 1.00 33.91 ATOM 163 CG HIS A 164 9.332 32.406 18.198 1.00 37.26 ATOM 164 ND1 HIS A 164 10.472 32.950 18.746 1.00 37.82 ATOM 165 CD2 HIS A 164 9.466 32.527 16.858 1.00 35.94 ATOM 166 CE1 HIS A 164 11.263 33.371 17.774 1.00 38.43 ATOM 167 NE2 HIS A 164 10.675 33.127 16.619 1.00 38.58 ATOM 168 N CYS A 165 7.605 30.773 21.893 1.00 28.59 ATOM 169 CA CYS A 165 6.608 30.622 22.928 1.00 27.68 ATOM 170 C CYS A 165 6.526 31.977 23.573 1.00 26.86 ATOM 171 O CYS A 165 7.487 32.441 24.188 1.00 28.25 ATOM 172 CB CYS A 165 7.021 29.595 23.977 1.00 33.29 ATOM 173 SG CYS A 165 5.856 29.545 25.365 1.00 36.21 ATOM 174 N LEU A 166 5.390 32.636 23.416 1.00 31.72 ATOM 175 CA LEU A 166 5.226 33.937 24.015 1.00 30.79 ATOM 176 C LEU A 166 4.325 33.786 25.230 1.00 32.46 ATOM 177 O LEU A 166 3.280 33.145 25.154 1.00 32.33 ATOM 178 CB LEU A 166 4.603 34.919 23.017 1.00 25.32 ATOM 179 CG LEU A 166 4.153 36.252 23.622 1.00 25.92 ATOM 180 CD1 LEU A 166 5.338 36.949 24.282 1.00 26.88 ATOM 181 CD2 LEU A 166 3.547 37.127 22.546 1.00 26.00 ATOM 182 N ILE A 167 4.752 34.358 26.350 1.00 32.72 ATOM 183 CA ILE A 167 3.957 34.311 27.562 1.00 29.77 ATOM 184 C ILE A 167 3.660 35.726 28.008 1.00 31.00 ATOM 185 O ILE A 167 4.565 36.472 28.368 1.00 30.74 ATOM 186 CB ILE A 167 4.679 33.592 28.724 1.00 25.01 ATOM 187 CG1 ILE A 167 4.930 32.125 28.377 1.00 24.08 ATOM 188 CG2 ILE A 167 3.819 33.692 29.990 1.00 21.19 ATOM 189 CD1 ILE A 167 5.566 31.306 29.514 1.00 20.01 ATOM 190 N ILE A 168 2.391 36.098 27.951 1.00 29.87 ATOM 191 CA ILE A 168 1.953 37.405 28.388 1.00 29.84 ATOM 192 C ILE A 168 1.580 37.155 29.851 1.00 30.20 ATOM 193 O ILE A 168 0.701 36.350 30.138 1.00 29.05 ATOM 194 CB ILE A 168 0.704 37.891 27.616 1.00 35.15 ATOM 195 CG1 ILE A 168 0.969 37.870 26.111 1.00 37.32 ATOM 196 CG2 ILE A 168 0.336 39.295 28.057 1.00 33.53 ATOM 197 CD1 ILE A 168 1.999 38.844 25.662 1.00 42.91 ATOM 198 N ASN A 169 2.252 37.821 30.775 1.00 31.34 ATOM 199 CA ASN A 169 1.978 37.634 32.186 1.00 30.87 ATOM 200 C ASN A 169 1.493 38.927 32.826 1.00 31.58 ATOM 201 O ASN A 169 2.298 39.791 33.166 1.00 31.35 ATOM 202 CB ASN A 169 3.249 37.144 32.886 1.00 30.44 ATOM 203 CG ASN A 169 3.036 36.853 34.358 1.00 30.08 ATOM 204 OD1 ASN A 169 3.914 37.097 35.174 1.00 34.79 ATOM 205 ND2 ASN A 169 1.879 36.315 34.701 1.00 29.89 ATOM 206 N ASN A 170 0.209 39.070 32.964 1.00 29.27 ATOM 207 CA ASN A 170 -0.333 40.275 33.569 1.00 30.70 ATOM 208 C ASN A 170 -0.583 40.053 35.060 1.00 31.65 ATOM 209 O ASN A 170 -1.430 39.247 35.453 1.00 32.23 ATOM 210 CB ASN A 170 -1.639 40.673 32.881 1.00 30.55 ATOM 211 CG ASN A 170 -1.421 41.132 31.449 1.00 30.25 ATOM 212 OD1 ASN A 170 -0.303 41.461 31.059 1.00 28.44 ATOM 213 ND2 ASN A 170 -2.497 41.172 30.666 1.00 28.36 ATOM 214 N VAL A 171 0.140 40.784 35.876 1.00 34.62 ATOM 215 CA VAL A 171 0.052 40.676 37.321 1.00 34.40 ATOM 216 C VAL A 171 -0.536 41.923 37.961 1.00 35.17 ATOM 217 O VAL A 171 -1.478 41.840 38.745 1.00 35.41 ATOM 218 CB VAL A 171 1.420 40.429 37.912 1.00 35.04 ATOM 219 CG1 VAL A 171 1.391 40.576 39.427 1.00 35.04 ATOM 220 CG2 VAL A 171 1.903 39.036 37.524 1.00 36.28 ATOM 221 N ASN A 172 -0.001 43.077 37.603 1.00 34.12 ATOM 222 CA ASN A 172 -0.432 44.352 38.151 1.00 35.60 ATOM 223 C ASN A 172 -1.359 45.091 37.194 1.00 36.06 ATOM 224 O ASN A 172 -1.029 45.321 36.034 1.00 37.27 ATOM 225 CB ASN A 172 0.742 45.204 38.475 1.00 36.78 ATOM 226 CG ASN A 172 1.787 44.442 39.266 1.00 37.39 ATOM 227 OD1 ASN A 172 1.612 44.189 40.455 1.00 39.53 ATOM 228 ND2 ASN A 172 2.875 44.055 38.601 1.00 35.66 ATOM 229 N PHE A 173 -2.529 45.461 37.696 1.00 29.57 ATOM 230 CA PHE A 173 -3.508 46.174 36.893 1.00 30.89 ATOM 231 C PHE A 173 -3.683 47.556 37.479 1.00 33.63 ATOM 232 O PHE A 173 -3.429 47.767 38.665 1.00 34.12 ATOM 233 CB PHE A 173 -4.837 45.411 36.895 1.00 32.09 ATOM 234 CG PHE A 173 -4.748 44.047 36.277 1.00 30.12 ATOM 235 CD1 PHE A 173 -4.023 43.036 36.892 1.00 26.68 ATOM 236 CD2 PHE A 173 -5.342 43.785 35.044 1.00 28.75 ATOM 237 CE1 PHE A 173 -3.892 41.784 36.289 1.00 29.79 ATOM 238 CE2 PHE A 173 -5.214 42.539 34.439 1.00 29.25 ATOM 239 CZ PHE A 173 -4.486 41.537 35.059 1.00 27.15 ATOM 240 N CYS A 174 -4.105 48.513 36.657 1.00 38.77 ATOM 241 CA CYS A 174 -4.302 49.865 37.150 1.00 43.39 ATOM 242 C CYS A 174 -5.379 49.864 38.229 1.00 42.73 ATOM 243 O CYS A 174 -6.359 49.116 38.145 1.00 42.68 ATOM 244 CB CYS A 174 -4.707 50.800 36.021 1.00 67.96 ATOM 245 SG CYS A 174 -6.144 50.268 35.095 1.00 80.84 ATOM 246 N ARG A 175 -5.176 50.695 39.239 1.00 45.26 ATOM 247 CA ARG A 175 -6.104 50.811 40.352 1.00 46.11 ATOM 248 C ARG A 175 -7.513 51.066 39.841 1.00 43.79 ATOM 249 O ARG A 175 -8.487 50.474 40.313 1.00 43.28 ATOM 250 CB ARG A 175 -5.647 51.964 41.267 1.00 64.87 ATOM 251 CG ARG A 175 -6.582 52.302 42.425 1.00 69.34 ATOM 252 CD ARG A 175 -6.075 53.528 43.169 0.00 71.88 ATOM 253 NE ARG A 175 -7.045 54.038 44.136 0.00 74.20 ATOM 254 CZ ARG A 175 -8.238 54.527 43.811 0.00 75.20 ATOM 255 NH1 ARG A 175 -8.615 54.577 42.541 0.00 75.80 ATOM 256 NH2 ARG A 175 -9.053 54.972 44.759 0.00 75.80 ATOM 257 N GLU A 175A -7.609 51.943 38.852 1.00 42.64 ATOM 258 CA GLU A 175A -8.869 52.343 38.240 1.00 41.87 ATOM 259 C GLU A 175A -9.725 51.201 37.669 1.00 41.07 ATOM 260 O GLU A 175A -10.954 51.253 37.736 1.00 41.32 ATOM 261 CB GLU A 175A -8.567 53.362 37.148 1.00 44.22 ATOM 262 CG GLU A 175A -9.749 53.818 36.359 0.00 44.41 ATOM 263 CD GLU A 175A -9.379 54.143 34.927 0.00 44.60 ATOM 264 OE1 GLU A 175A -8.402 54.889 34.723 0.00 44.60 ATOM 265 OE2 GLU A 175A -10.075 53.670 34.014 0.00 44.60 ATOM 266 N SER A 175B -9.082 50.174 37.109 1.00 37.80 ATOM 267 CA SER A 175B -9.815 49.048 36.534 1.00 37.69 ATOM 268 C SER A 175B -10.578 48.263 37.600 1.00 37.95 ATOM 269 O SER A 175B -11.630 47.688 37.321 1.00 38.09 ATOM 270 CB SER A 175B -8.858 48.088 35.825 1.00 40.67 ATOM 271 OG SER A 175B -8.002 47.445 36.761 1.00 40.45 ATOM 272 N GLY A 175C -10.051 48.244 38.813 1.00 42.84 ATOM 273 CA GLY A 175C -10.699 47.517 39.886 1.00 43.37 ATOM 274 C GLY A 175C -10.286 46.050 39.901 1.00 44.24 ATOM 275 O GLY A 175C -10.798 45.268 40.702 1.00 45.36 ATOM 276 N LEU A 176 -9.374 45.676 39.004 1.00 35.92 ATOM 277 CA LEU A 176 -8.908 44.304 38.924 1.00 34.66 ATOM 278 C LEU A 176 -7.809 44.046 39.962 1.00 35.70 ATOM 279 O LEU A 176 -6.876 44.831 40.114 1.00 36.64 ATOM 280 CB LEU A 176 -8.395 44.015 37.509 1.00 31.92 ATOM 281 CG LEU A 176 -9.454 44.200 36.412 1.00 29.44 ATOM 282 CD1 LEU A 176 -8.822 43.978 35.052 1.00 26.16 ATOM 283 CD2 LEU A 176 -10.606 43.207 36.632 1.00 28.60 ATOM 284 N ARG A 177 -7.931 42.938 40.676 1.00 38.20 ATOM 285 CA ARG A 177 -6.955 42.621 41.707 1.00 41.19 ATOM 286 C ARG A 177 -5.612 42.152 41.164 1.00 37.65 ATOM 287 O ARG A 177 -5.537 41.516 40.120 1.00 35.96 ATOM 288 CB ARG A 177 -7.533 41.567 42.653 1.00 69.88 ATOM 289 CG ARG A 177 -8.725 42.067 43.453 1.00 80.56 ATOM 290 CD ARG A 177 -9.311 40.985 44.350 1.00 90.70 ATOM 291 NE ARG A 177 -10.352 41.506 45.233 1.00 97.43 ATOM 292 CZ ARG A 177 -10.143 42.437 46.168 1.00100.70 ATOM 293 NH1 ARG A 177 -8.927 42.938 46.346 1.00101.96 ATOM 294 NH2 ARG A 177 -11.148 42.852 46.927 1.00102.55 ATOM 295 N THR A 178 -4.555 42.493 41.891 1.00 37.30 ATOM 296 CA THR A 178 -3.208 42.093 41.521 1.00 37.22 ATOM 297 C THR A 178 -3.238 40.581 41.468 1.00 36.39 ATOM 298 O THR A 178 -3.743 39.937 42.379 1.00 37.59 ATOM 299 CB THR A 178 -2.196 42.530 42.589 1.00 35.38 ATOM 300 OG1 THR A 178 -2.217 43.957 42.701 1.00 34.30 ATOM 301 CG2 THR A 178 -0.790 42.055 42.226 1.00 34.32 ATOM 302 N ARG A 179 -2.716 39.999 40.399 1.00 37.13 ATOM 303 CA ARG A 179 -2.725 38.554 40.299 1.00 38.14 ATOM 304 C ARG A 179 -1.444 37.981 40.867 1.00 40.47 ATOM 305 O ARG A 179 -0.503 37.649 40.136 1.00 40.26 ATOM 306 CB ARG A 179 -2.929 38.125 38.841 1.00 34.74 ATOM 307 CG ARG A 179 -4.275 38.605 38.301 1.00 32.13 ATOM 308 CD ARG A 179 -4.540 38.203 36.864 1.00 26.44 ATOM 309 NE ARG A 179 -4.571 36.757 36.683 1.00 23.42 ATOM 310 CZ ARG A 179 -3.532 36.042 36.261 1.00 26.31 ATOM 311 NH1 ARG A 179 -3.646 34.732 36.118 1.00 25.80 ATOM 312 NH2 ARG A 179 -2.383 36.635 35.961 1.00 28.93 ATOM 313 N THR A 180 -1.408 37.882 42.194 1.00 52.12 ATOM 314 CA THR A 180 -0.249 37.324 42.865 1.00 56.54 ATOM 315 C THR A 180 -0.294 35.834 42.553 1.00 55.77 ATOM 316 O THR A 180 -1.367 35.277 42.318 1.00 58.22 ATOM 317 CB THR A 180 -0.328 37.528 44.380 1.00 76.01 ATOM 318 OG1 THR A 180 -0.653 38.894 44.663 1.00 78.74 ATOM 319 CG2 THR A 180 0.990 37.194 45.013 1.00 78.47 ATOM 320 N GLY A 181 0.836 35.188 42.544 1.00 49.02 ATOM 321 CA GLY A 181 0.851 33.772 42.232 1.00 47.83 ATOM 322 C GLY A 181 0.967 33.573 40.737 1.00 44.81 ATOM 323 O GLY A 181 1.296 32.482 40.270 1.00 45.30 ATOM 324 N SER A 182 0.702 34.621 39.967 1.00 38.97 ATOM 325 CA SER A 182 0.804 34.534 38.521 1.00 36.65 ATOM 326 C SER A 182 2.260 34.406 38.149 1.00 34.15 ATOM 327 O SER A 182 2.604 33.690 37.215 1.00 35.18 ATOM 328 CB SER A 182 0.197 35.772 37.854 1.00 35.48 ATOM 329 OG SER A 182 0.088 35.561 36.461 1.00 31.96 ATOM 330 N ASN A 183 3.124 35.082 38.890 1.00 35.78 ATOM 331 CA ASN A 183 4.553 34.991 38.617 1.00 37.48 ATOM 332 C ASN A 183 5.062 33.556 38.728 1.00 37.44 ATOM 333 O ASN A 183 5.955 33.155 37.975 1.00 38.94 ATOM 334 CB ASN A 183 5.358 35.892 39.551 1.00 39.28 ATOM 335 CG ASN A 183 5.233 37.354 39.198 1.00 42.62 ATOM 336 OD1 ASN A 183 5.217 37.705 38.011 1.00 45.79 ATOM 337 ND2 ASN A 183 5.150 38.206 40.208 1.00 41.65 ATOM 338 N ILE A 184 4.490 32.773 39.642 1.00 39.79 ATOM 339 CA ILE A 184 4.931 31.386 39.767 1.00 41.47 ATOM 340 C ILE A 184 4.286 30.557 38.656 1.00 41.27 ATOM 341 O ILE A 184 4.868 29.576 38.174 1.00 41.67 ATOM 342 CB ILE A 184 4.636 30.783 41.173 1.00 49.48 ATOM 343 CG1 ILE A 184 3.186 30.376 41.294 1.00 48.94 ATOM 344 CG2 ILE A 184 5.014 31.765 42.269 1.00 49.38 ATOM 345 CD1 ILE A 184 2.968 28.932 40.966 1.00 50.43 ATOM 346 N ASP A 185 3.081 30.936 38.247 1.00 37.92 ATOM 347 CA ASP A 185 2.417 30.232 37.155 1.00 37.43 ATOM 348 C ASP A 185 3.257 30.423 35.907 1.00 35.77 ATOM 349 O ASP A 185 3.549 29.483 35.170 1.00 33.28 ATOM 350 CB ASP A 185 1.029 30.808 36.892 1.00 46.59 ATOM 351 CG ASP A 185 0.065 30.527 38.018 1.00 49.82 ATOM 352 OD1 ASP A 185 0.186 29.463 38.649 1.00 51.73 ATOM 353 OD2 ASP A 185 -0.816 31.369 38.253 1.00 49.86 ATOM 354 N CYS A 186 3.654 31.670 35.699 1.00 35.44 ATOM 355 CA CYS A 186 4.471 32.027 34.558 1.00 36.68 ATOM 356 C CYS A 186 5.779 31.243 34.555 1.00 37.07 ATOM 357 O CYS A 186 6.164 30.668 33.530 1.00 36.62 ATOM 358 CB CYS A 186 4.758 33.535 34.587 1.00 38.67 ATOM 359 SG CYS A 186 5.799 34.099 33.245 1.00 37.98 ATOM 360 N GLU A 187 6.455 31.205 35.700 1.00 39.22 ATOM 361 CA GLU A 187 7.717 30.483 35.803 1.00 38.49 ATOM 362 C GLU A 187 7.543 29.001 35.516 1.00 37.20 ATOM 363 O GLU A 187 8.408 28.376 34.909 1.00 39.29 ATOM 364 CB GLU A 187 8.347 30.671 37.185 1.00 50.54 ATOM 365 CG GLU A 187 9.642 29.899 37.380 1.00 54.47 ATOM 366 CD GLU A 187 10.729 30.287 36.372 1.00 58.35 ATOM 367 OE1 GLU A 187 11.703 29.513 36.226 1.00 61.99 ATOM 368 OE2 GLU A 187 10.629 31.367 35.742 1.00 58.92 ATOM 369 N LYS A 188 6.431 28.430 35.949 1.00 32.61 ATOM 370 CA LYS A 188 6.190 27.016 35.681 1.00 32.32 ATOM 371 C LYS A 188 6.035 26.779 34.181 1.00 32.77 ATOM 372 O LYS A 188 6.614 25.849 33.621 1.00 32.98 ATOM 373 CB LYS A 188 4.932 26.528 36.398 1.00 32.89 ATOM 374 CG LYS A 188 5.028 26.475 37.908 1.00 34.35 ATOM 375 CD LYS A 188 3.738 25.954 38.496 1.00 34.64 ATOM 376 CE LYS A 188 3.794 25.873 40.013 1.00 34.04 ATOM 377 NZ LYS A 188 2.472 25.464 40.564 1.00 32.68 ATOM 378 N LEU A 189 5.250 27.631 33.522 1.00 31.42 ATOM 379 CA LEU A 189 5.033 27.482 32.088 1.00 30.65 ATOM 380 C LEU A 189 6.291 27.826 31.290 1.00 31.43 ATOM 381 O LEU A 189 6.604 27.169 30.302 1.00 29.18 ATOM 382 CB LEU A 189 3.837 28.313 31.656 1.00 31.01 ATOM 383 CG LEU A 189 2.572 27.789 32.312 1.00 29.09 ATOM 384 CD1 LEU A 189 1.388 28.639 31.937 1.00 28.49 ATOM 385 CD2 LEU A 189 2.367 26.347 31.866 1.00 28.46 ATOM 386 N ARG A 190 7.013 28.850 31.741 1.00 34.17 ATOM 387 CA ARG A 190 8.250 29.239 31.077 1.00 37.98 ATOM 388 C ARG A 190 9.212 28.056 31.099 1.00 40.40 ATOM 389 O ARG A 190 9.832 27.737 30.082 1.00 40.39 ATOM 390 CB ARG A 190 8.893 30.424 31.794 1.00 45.08 ATOM 391 CG ARG A 190 10.128 30.967 31.094 1.00 47.64 ATOM 392 CD ARG A 190 11.072 31.653 32.066 1.00 50.56 ATOM 393 NE ARG A 190 12.253 30.835 32.340 1.00 55.90 ATOM 394 CZ ARG A 190 12.214 29.618 32.884 1.00 58.89 ATOM 395 NH1 ARG A 190 11.054 29.075 33.221 1.00 61.79 ATOM 396 NH2 ARG A 190 13.335 28.935 33.068 1.00 59.74 ATOM 397 N ARG A 191 9.323 27.398 32.252 1.00 46.55 ATOM 398 CA ARG A 191 10.208 26.239 32.390 1.00 48.00 ATOM 399 C ARG A 191 9.688 25.071 31.579 1.00 45.72 ATOM 400 O ARG A 191 10.465 24.331 30.976 1.00 44.99 ATOM 401 CB ARG A 191 10.330 25.801 33.853 1.00 66.63 ATOM 402 CG ARG A 191 11.436 26.485 34.640 1.00 76.24 ATOM 403 CD ARG A 191 11.719 25.753 35.950 1.00 82.37 ATOM 404 NE ARG A 191 10.580 25.788 36.860 1.00 87.79 ATOM 405 CZ ARG A 191 10.458 26.628 37.887 1.00 89.87 ATOM 406 NH1 ARG A 191 11.415 27.514 38.142 1.00 89.76 ATOM 407 NH2 ARG A 191 9.372 26.590 38.651 1.00 89.93 ATOM 408 N ARG A 192 8.368 24.900 31.569 1.00 41.60 ATOM 409 CA ARG A 192 7.745 23.815 30.830 1.00 39.17 ATOM 410 C ARG A 192 8.053 23.867 29.343 1.00 38.08 ATOM 411 O ARG A 192 8.548 22.893 28.773 1.00 38.92 ATOM 412 CB ARG A 192 6.224 23.826 31.020 1.00 35.13 ATOM 413 CG ARG A 192 5.470 22.787 30.176 1.00 33.84 ATOM 414 CD ARG A 192 5.998 21.383 30.463 1.00 36.08 ATOM 415 NE ARG A 192 6.085 21.155 31.904 1.00 37.19 ATOM 416 CZ ARG A 192 6.799 20.196 32.479 1.00 38.22 ATOM 417 NH1 ARG A 192 6.804 20.088 33.796 1.00 35.99 ATOM 418 NH2 ARG A 192 7.513 19.358 31.741 1.00 39.33 ATOM 419 N PHE A 193 7.758 25.000 28.708 1.00 33.28 ATOM 420 CA PHE A 193 7.982 25.120 27.269 1.00 34.52 ATOM 421 C PHE A 193 9.451 25.201 26.889 1.00 34.49 ATOM 422 O PHE A 193 9.813 24.849 25.775 1.00 35.13 ATOM 423 CB PHE A 193 7.172 26.294 26.691 1.00 33.34 ATOM 424 CG PHE A 193 5.682 26.049 26.705 1.00 32.80 ATOM 425 CD1 PHE A 193 4.864 26.711 27.613 1.00 33.10 ATOM 426 CD2 PHE A 193 5.120 25.074 25.898 1.00 31.87 ATOM 427 CE1 PHE A 193 3.510 26.394 27.722 1.00 32.78 ATOM 428 CE2 PHE A 193 3.770 24.747 26.001 1.00 33.73 ATOM 429 CZ PHE A 193 2.973 25.412 26.912 1.00 30.85 ATOM 430 N SER A 194 10.297 25.657 27.806 1.00 41.17 ATOM 431 CA SER A 194 11.727 25.716 27.512 1.00 42.67 ATOM 432 C SER A 194 12.187 24.281 27.338 1.00 42.83 ATOM 433 O SER A 194 12.883 23.965 26.382 1.00 44.05 ATOM 434 CB SER A 194 12.509 26.346 28.660 1.00 49.29 ATOM 435 OG SER A 194 12.444 27.757 28.613 1.00 55.71 ATOM 436 N SER A 195 11.776 23.424 28.261 1.00 37.49 ATOM 437 CA SER A 195 12.172 22.028 28.199 1.00 38.91 ATOM 438 C SER A 195 11.523 21.306 27.017 1.00 39.50 ATOM 439 O SER A 195 11.936 20.201 26.654 1.00 39.52 ATOM 440 CB SER A 195 11.831 21.316 29.518 1.00 37.03 ATOM 441 OG SER A 195 10.434 21.194 29.691 1.00 39.47 ATOM 442 N LEU A 196 10.509 21.924 26.429 1.00 42.84 ATOM 443 CA LEU A 196 9.840 21.341 25.274 1.00 41.95 ATOM 444 C LEU A 196 10.475 21.933 24.013 1.00 41.06 ATOM 445 O LEU A 196 9.954 21.786 22.916 1.00 39.85 ATOM 446 CB LEU A 196 8.337 21.619 25.325 1.00 41.14 ATOM 447 CG LEU A 196 7.588 20.945 26.479 1.00 41.97 ATOM 448 CD1 LEU A 196 6.141 21.412 26.518 1.00 41.52 ATOM 449 CD2 LEU A 196 7.655 19.437 26.316 1.00 41.75 ATOM 450 N HIS A 197 11.600 22.613 24.222 1.00 41.32 ATOM 451 CA HIS A 197 12.392 23.220 23.148 1.00 40.80 ATOM 452 C HIS A 197 11.882 24.490 22.467 1.00 40.47 ATOM 453 O HIS A 197 12.245 24.764 21.322 1.00 39.96 ATOM 454 CB HIS A 197 12.693 22.164 22.084 1.00 45.20 ATOM 455 CG HIS A 197 13.503 21.016 22.595 1.00 49.34 ATOM 456 ND1 HIS A 197 13.074 19.710 22.522 1.00 52.35 ATOM 457 CD2 HIS A 197 14.711 20.978 23.207 1.00 50.55 ATOM 458 CE1 HIS A 197 13.981 18.920 23.063 1.00 51.49 ATOM 459 NE2 HIS A 197 14.987 19.659 23.488 1.00 51.42 ATOM 460 N PHE A 198 11.063 25.274 23.167 1.00 38.25 ATOM 461 CA PHE A 198 10.557 26.508 22.587 1.00 37.20 ATOM 462 C PHE A 198 11.399 27.682 23.076 1.00 37.01 ATOM 463 O PHE A 198 11.937 27.642 24.182 1.00 38.49 ATOM 464 CB PHE A 198 9.090 26.748 22.980 1.00 32.96 ATOM 465 CG PHE A 198 8.106 25.816 22.309 1.00 32.02 ATOM 466 CD1 PHE A 198 7.808 24.575 22.871 1.00 29.27 ATOM 467 CD2 PHE A 198 7.485 26.178 21.121 1.00 31.74 ATOM 468 CE1 PHE A 198 6.892 23.708 22.254 1.00 29.68 ATOM 469 CE2 PHE A 198 6.576 25.318 20.495 1.00 31.47 ATOM 470 CZ PHE A 198 6.279 24.085 21.066 1.00 29.26 ATOM 471 N MET A 199 11.539 28.709 22.251 1.00 35.34 ATOM 472 CA MET A 199 12.300 29.881 22.666 1.00 35.01 ATOM 473 C MET A 199 11.260 30.716 23.397 1.00 34.83 ATOM 474 O MET A 199 10.420 31.379 22.782 1.00 36.86 ATOM 475 CB MET A 199 12.844 30.637 21.455 1.00 36.38 ATOM 476 CG MET A 199 13.842 29.827 20.643 1.00 39.45 ATOM 477 SD MET A 199 14.272 30.648 19.100 1.00 43.22 ATOM 478 CE MET A 199 12.870 30.173 18.085 1.00 39.83 ATOM 479 N VAL A 200 11.301 30.652 24.721 1.00 36.25 ATOM 480 CA VAL A 200 10.320 31.352 25.516 1.00 35.34 ATOM 481 C VAL A 200 10.658 32.788 25.831 1.00 36.77 ATOM 482 O VAL A 200 11.761 33.102 26.266 1.00 39.15 ATOM 483 CB VAL A 200 10.063 30.621 26.845 1.00 30.48 ATOM 484 CG1 VAL A 200 9.026 31.379 27.655 1.00 30.11 ATOM 485 CG2 VAL A 200 9.592 29.198 26.576 1.00 30.14 ATOM 486 N GLU A 201 9.694 33.656 25.598 1.00 32.82 ATOM 487 CA GLU A 201 9.849 35.059 25.909 1.00 33.65 ATOM 488 C GLU A 201 8.696 35.455 26.816 1.00 32.62 ATOM 489 O GLU A 201 7.530 35.204 26.514 1.00 32.44 ATOM 490 CB GLU A 201 9.854 35.916 24.650 1.00 44.66 ATOM 491 CG GLU A 201 9.714 37.388 24.976 1.00 49.29 ATOM 492 CD GLU A 201 9.969 38.298 23.797 1.00 52.88 ATOM 493 OE1 GLU A 201 9.587 37.940 22.661 1.00 56.21 ATOM 494 OE2 GLU A 201 10.542 39.387 24.019 1.00 54.29 ATOM 495 N VAL A 202 9.023 36.067 27.942 1.00 33.99 ATOM 496 CA VAL A 202 8.005 36.507 28.867 1.00 33.72 ATOM 497 C VAL A 202 7.855 38.010 28.751 1.00 34.05 ATOM 498 O VAL A 202 8.828 38.742 28.793 1.00 35.06 ATOM 499 CB VAL A 202 8.370 36.167 30.338 1.00 26.79 ATOM 500 CG1 VAL A 202 7.319 36.738 31.285 1.00 24.21 ATOM 501 CG2 VAL A 202 8.480 34.666 30.510 1.00 22.11 ATOM 502 N LYS A 203 6.619 38.461 28.584 1.00 36.75 ATOM 503 CA LYS A 203 6.342 39.888 28.511 1.00 37.27 ATOM 504 C LYS A 203 5.284 40.118 29.561 1.00 37.10 ATOM 505 O LYS A 203 4.176 39.607 29.452 1.00 37.62 ATOM 506 CB LYS A 203 5.827 40.282 27.125 1.00 39.21 ATOM 507 CG LYS A 203 6.888 40.207 26.050 1.00 40.22 ATOM 508 CD LYS A 203 6.425 40.851 24.754 1.00 44.74 ATOM 509 CE LYS A 203 7.568 40.890 23.743 1.00 47.22 ATOM 510 NZ LYS A 203 7.148 41.462 22.436 1.00 51.23 ATOM 511 N GLY A 204 5.627 40.885 30.586 1.00 32.54 ATOM 512 CA GLY A 204 4.671 41.114 31.651 1.00 31.76 ATOM 513 C GLY A 204 3.979 42.454 31.614 1.00 32.06 ATOM 514 O GLY A 204 4.460 43.395 31.004 1.00 32.10 ATOM 515 N ASP A 205 2.835 42.511 32.286 1.00 36.96 ATOM 516 CA ASP A 205 2.023 43.713 32.413 1.00 37.87 ATOM 517 C ASP A 205 1.775 44.479 31.128 1.00 36.59 ATOM 518 O ASP A 205 2.188 45.629 30.985 1.00 37.76 ATOM 519 CB ASP A 205 2.643 44.647 33.466 1.00 38.27 ATOM 520 CG ASP A 205 2.582 44.059 34.874 1.00 41.16 ATOM 521 OD1 ASP A 205 1.710 43.196 35.120 1.00 41.98 ATOM 522 OD2 ASP A 205 3.387 44.467 35.736 1.00 42.40 ATOM 523 N LEU A 206 1.067 43.848 30.198 1.00 32.65 ATOM 524 CA LEU A 206 0.749 44.483 28.935 1.00 30.92 ATOM 525 C LEU A 206 -0.652 45.013 28.882 1.00 32.16 ATOM 526 O LEU A 206 -1.570 44.364 29.344 1.00 31.92 ATOM 527 CB LEU A 206 0.933 43.504 27.774 1.00 25.97 ATOM 528 CG LEU A 206 2.323 42.937 27.523 1.00 24.27 ATOM 529 CD1 LEU A 206 2.301 42.164 26.205 1.00 21.96 ATOM 530 CD2 LEU A 206 3.356 44.065 27.471 1.00 21.29 ATOM 531 N THR A 207 -0.802 46.202 28.308 1.00 30.68 ATOM 532 CA THR A 207 -2.106 46.803 28.130 1.00 28.78 ATOM 533 C THR A 207 -2.712 45.993 26.993 1.00 28.28 ATOM 534 O THR A 207 -2.034 45.200 26.347 1.00 28.02 ATOM 535 CB THR A 207 -2.001 48.259 27.654 1.00 36.08 ATOM 536 OG1 THR A 207 -1.332 48.291 26.396 1.00 41.05 ATOM 537 CG2 THR A 207 -1.215 49.083 28.625 1.00 37.04 ATOM 538 N ALA A 208 -4.005 46.178 26.753 1.00 31.51 ATOM 539 CA ALA A 208 -4.682 45.464 25.686 1.00 31.91 ATOM 540 C ALA A 208 -3.945 45.704 24.359 1.00 33.55 ATOM 541 O ALA A 208 -3.580 44.760 23.654 1.00 33.11 ATOM 542 CB ALA A 208 -6.125 45.942 25.576 1.00 28.34 ATOM 543 N LYS A 209 -3.708 46.976 24.041 1.00 31.36 ATOM 544 CA LYS A 209 -3.041 47.324 22.808 1.00 33.08 ATOM 545 C LYS A 209 -1.659 46.712 22.687 1.00 31.78 ATOM 546 O LYS A 209 -1.282 46.245 21.606 1.00 33.84 ATOM 547 CB LYS A 209 -2.984 48.852 22.644 1.00 35.02 ATOM 548 CG LYS A 209 -4.285 49.424 22.112 1.00 38.30 ATOM 549 CD LYS A 209 -4.404 50.926 22.295 1.00 41.43 ATOM 550 CE LYS A 209 -5.757 51.401 21.809 1.00 44.27 ATOM 551 NZ LYS A 209 -5.942 52.868 21.952 1.00 46.44 ATOM 552 N LYS A 210 -0.905 46.695 23.774 1.00 27.13 ATOM 553 CA LYS A 210 0.414 46.125 23.718 1.00 28.49 ATOM 554 C LYS A 210 0.393 44.588 23.613 1.00 27.08 ATOM 555 O LYS A 210 1.337 43.981 23.109 1.00 27.16 ATOM 556 CB LYS A 210 1.240 46.589 24.912 1.00 32.02 ATOM 557 CG LYS A 210 1.554 48.078 24.831 1.00 36.52 ATOM 558 CD LYS A 210 2.448 48.555 25.953 1.00 40.53 ATOM 559 CE LYS A 210 2.770 50.042 25.785 1.00 43.21 ATOM 560 NZ LYS A 210 3.598 50.575 26.902 1.00 46.48 ATOM 561 N MET A 211 -0.655 43.961 24.082 1.00 27.96 ATOM 562 CA MET A 211 -0.771 42.512 23.965 1.00 28.19 ATOM 563 C MET A 211 -0.943 42.228 22.473 1.00 25.91 ATOM 564 O MET A 211 -0.336 41.323 21.926 1.00 25.59 ATOM 565 CB MET A 211 -1.978 42.010 24.722 1.00 32.55 ATOM 566 CG MET A 211 -1.878 42.092 26.228 1.00 38.42 ATOM 567 SD MET A 211 -3.432 41.588 27.033 1.00 44.52 ATOM 568 CE MET A 211 -3.400 39.834 26.696 1.00 39.04 ATOM 569 N VAL A 212 -1.794 43.018 21.828 1.00 26.18 ATOM 570 CA VAL A 212 -2.048 42.861 20.397 1.00 27.59 ATOM 571 C VAL A 212 -0.762 43.085 19.628 1.00 28.37 ATOM 572 O VAL A 212 -0.399 42.280 18.774 1.00 28.97 ATOM 573 CB VAL A 212 -3.139 43.862 19.921 1.00 27.04 ATOM 574 CG1 VAL A 212 -3.289 43.808 18.404 1.00 22.09 ATOM 575 CG2 VAL A 212 -4.457 43.516 20.592 1.00 22.55 ATOM 576 N LEU A 213 -0.080 44.174 19.938 1.00 27.92 ATOM 577 CA LEU A 213 1.179 44.465 19.282 1.00 29.90 ATOM 578 C LEU A 213 2.146 43.296 19.457 1.00 30.94 ATOM 579 O LEU A 213 2.768 42.841 18.486 1.00 31.21 ATOM 580 CB LEU A 213 1.812 45.736 19.857 1.00 31.79 ATOM 581 CG LEU A 213 1.055 47.049 19.601 1.00 35.54 ATOM 582 CD1 LEU A 213 1.847 48.211 20.204 1.00 37.02 ATOM 583 CD2 LEU A 213 0.865 47.264 18.095 1.00 33.64 ATOM 584 N ALA A 214 2.268 42.796 20.688 1.00 30.62 ATOM 585 CA ALA A 214 3.164 41.679 20.955 1.00 30.36 ATOM 586 C ALA A 214 2.758 40.433 20.162 1.00 31.02 ATOM 587 O ALA A 214 3.613 39.655 19.755 1.00 34.19 ATOM 588 CB ALA A 214 3.188 41.368 22.449 1.00 24.01 ATOM 589 N LEU A 215 1.461 40.250 19.944 1.00 30.35 ATOM 590 CA LEU A 215 1.002 39.090 19.188 1.00 28.47 ATOM 591 C LEU A 215 1.217 39.315 17.683 1.00 29.74 ATOM 592 O LEU A 215 1.543 38.380 16.950 1.00 27.18 ATOM 593 CB LEU A 215 -0.456 38.817 19.486 1.00 24.39 ATOM 594 CG LEU A 215 -0.758 38.407 20.923 1.00 24.13 ATOM 595 CD1 LEU A 215 -2.244 38.451 21.139 1.00 24.55 ATOM 596 CD2 LEU A 215 -0.215 37.019 21.200 1.00 22.73 ATOM 597 N LEU A 216 1.016 40.551 17.229 1.00 29.92 ATOM 598 CA LEU A 216 1.227 40.869 15.822 1.00 33.62 ATOM 599 C LEU A 216 2.713 40.681 15.539 1.00 34.64 ATOM 600 O LEU A 216 3.108 40.164 14.493 1.00 36.80 ATOM 601 CB LEU A 216 0.829 42.318 15.524 1.00 36.15 ATOM 602 CG LEU A 216 -0.647 42.604 15.491 1.00 39.12 ATOM 603 CD1 LEU A 216 -0.888 44.109 15.416 1.00 39.53 ATOM 604 CD2 LEU A 216 -1.266 41.890 14.300 1.00 39.47 ATOM 605 N GLU A 217 3.532 41.094 16.496 1.00 37.47 ATOM 606 CA GLU A 217 4.978 40.975 16.370 1.00 39.34 ATOM 607 C GLU A 217 5.352 39.503 16.204 1.00 38.14 ATOM 608 O GLU A 217 6.108 39.145 15.296 1.00 37.72 ATOM 609 CB GLU A 217 5.634 41.553 17.624 1.00 64.86 ATOM 610 CG GLU A 217 7.055 42.034 17.431 1.00 74.84 ATOM 611 CD GLU A 217 7.555 42.841 18.626 1.00 81.19 ATOM 612 OE1 GLU A 217 6.886 43.840 18.982 1.00 80.70 ATOM 613 OE2 GLU A 217 8.608 42.478 19.201 1.00 83.44 ATOM 614 N LEU A 218 4.819 38.642 17.070 1.00 34.35 ATOM 615 CA LEU A 218 5.129 37.227 16.983 1.00 32.50 ATOM 616 C LEU A 218 4.666 36.640 15.646 1.00 32.41 ATOM 617 O LEU A 218 5.357 35.803 15.054 1.00 30.74 ATOM 618 CB LEU A 218 4.483 36.468 18.142 1.00 27.94 ATOM 619 CG LEU A 218 4.599 34.946 18.107 1.00 29.27 ATOM 620 CD1 LEU A 218 6.049 34.520 17.960 1.00 27.27 ATOM 621 CD2 LEU A 218 4.005 34.359 19.380 1.00 27.95 ATOM 622 N ALA A 219 3.508 37.092 15.181 1.00 33.66 ATOM 623 CA ALA A 219 2.956 36.591 13.923 1.00 37.04 ATOM 624 C ALA A 219 3.727 37.113 12.719 1.00 39.02 ATOM 625 O ALA A 219 3.734 36.483 11.663 1.00 39.32 ATOM 626 CB ALA A 219 1.491 36.993 13.800 1.00 21.81 ATOM 627 N ARG A 220 4.369 38.264 12.884 1.00 38.54 ATOM 628 CA ARG A 220 5.123 38.894 11.813 1.00 43.11 ATOM 629 C ARG A 220 6.516 38.293 11.621 1.00 42.04 ATOM 630 O ARG A 220 7.187 38.583 10.633 1.00 41.72 ATOM 631 CB ARG A 220 5.268 40.392 12.096 1.00 65.35 ATOM 632 CG ARG A 220 5.452 41.247 10.858 1.00 72.81 ATOM 633 CD ARG A 220 6.004 42.623 11.223 1.00 78.78 ATOM 634 NE ARG A 220 5.528 43.102 12.518 1.00 84.14 ATOM 635 CZ ARG A 220 4.253 43.304 12.835 1.00 86.07 ATOM 636 NH1 ARG A 220 3.942 43.748 14.048 1.00 86.65 ATOM 637 NH2 ARG A 220 3.289 43.062 11.955 1.00 87.41 ATOM 638 N GLN A 221 6.947 37.460 12.567 1.00 35.72 ATOM 639 CA GLN A 221 8.259 36.848 12.462 1.00 35.43 ATOM 640 C GLN A 221 8.269 35.675 11.494 1.00 33.81 ATOM 641 O GLN A 221 7.214 35.215 11.054 1.00 29.88 ATOM 642 CB GLN A 221 8.738 36.401 13.846 1.00 67.52 ATOM 643 CG GLN A 221 8.954 37.575 14.781 1.00 75.76 ATOM 644 CD GLN A 221 10.104 37.344 15.728 1.00 81.16 ATOM 645 OE1 GLN A 221 11.246 37.146 15.299 1.00 84.34 ATOM 646 NE2 GLN A 221 9.822 37.376 17.029 1.00 85.25 ATOM 647 N ASP A 222 9.473 35.213 11.161 1.00 42.18 ATOM 648 CA ASP A 222 9.640 34.104 10.228 1.00 42.68 ATOM 649 C ASP A 222 9.745 32.803 10.984 1.00 39.39 ATOM 650 O ASP A 222 10.725 32.544 11.689 1.00 39.71 ATOM 651 CB ASP A 222 10.900 34.319 9.375 1.00 59.24 ATOM 652 CG ASP A 222 11.036 33.281 8.253 1.00 62.98 ATOM 653 OD1 ASP A 222 11.977 33.413 7.441 1.00 66.10 ATOM 654 OD2 ASP A 222 10.214 32.348 8.185 1.00 64.25 ATOM 655 N HIS A 224 8.723 31.975 10.830 1.00 30.44 ATOM 656 CA HIS A 224 8.650 30.686 11.489 1.00 28.98 ATOM 657 C HIS A 224 9.052 29.589 10.519 1.00 28.25 ATOM 658 O HIS A 224 8.752 28.409 10.734 1.00 28.46 ATOM 659 CB HIS A 224 7.223 30.477 11.992 1.00 33.51 ATOM 660 CG HIS A 224 6.767 31.540 12.947 1.00 31.89 ATOM 661 ND1 HIS A 224 6.866 31.396 14.316 1.00 31.85 ATOM 662 CD2 HIS A 224 6.274 32.780 12.732 1.00 31.27 ATOM 663 CE1 HIS A 224 6.454 32.508 14.903 1.00 33.75 ATOM 664 NE2 HIS A 224 6.089 33.363 13.961 1.00 29.58 ATOM 665 N GLY A 225 9.737 29.981 9.456 1.00 33.91 ATOM 666 CA GLY A 225 10.168 29.029 8.449 1.00 33.40 ATOM 667 C GLY A 225 10.938 27.833 8.970 1.00 34.55 ATOM 668 O GLY A 225 10.733 26.709 8.487 1.00 35.53 ATOM 669 N ALA A 226 11.806 28.042 9.954 1.00 40.71 ATOM 670 CA ALA A 226 12.588 26.940 10.504 1.00 43.35 ATOM 671 C ALA A 226 11.992 26.346 11.785 1.00 43.97 ATOM 672 O ALA A 226 12.649 25.559 12.469 1.00 46.06 ATOM 673 CB ALA A 226 14.020 27.413 10.761 1.00 33.47 ATOM 674 N LEU A 227 10.749 26.707 12.108 1.00 36.95 ATOM 675 CA LEU A 227 10.097 26.206 13.316 1.00 36.12 ATOM 676 C LEU A 227 8.908 25.297 12.994 1.00 36.22 ATOM 677 O LEU A 227 8.312 25.395 11.921 1.00 36.29 ATOM 678 CB LEU A 227 9.656 27.387 14.181 1.00 34.67 ATOM 679 CG LEU A 227 10.785 28.405 14.427 1.00 33.82 ATOM 680 CD1 LEU A 227 10.250 29.631 15.146 1.00 31.97 ATOM 681 CD2 LEU A 227 11.891 27.747 15.242 1.00 31.99 ATOM 682 N ASP A 228 8.562 24.411 13.927 1.00 39.21 ATOM 683 CA ASP A 228 7.460 23.476 13.724 1.00 38.72 ATOM 684 C ASP A 228 6.185 23.800 14.480 1.00 38.43 ATOM 685 O ASP A 228 5.149 23.196 14.232 1.00 38.12 ATOM 686 CB ASP A 228 7.865 22.062 14.141 1.00 41.86 ATOM 687 CG ASP A 228 9.160 21.630 13.525 1.00 43.98 ATOM 688 OD1 ASP A 228 9.327 21.823 12.307 1.00 45.63 ATOM 689 OD2 ASP A 228 10.007 21.081 14.271 1.00 43.63 ATOM 690 N CYS A 229 6.259 24.747 15.408 1.00 35.30 ATOM 691 CA CYS A 229 5.080 25.034 16.211 1.00 33.44 ATOM 692 C CYS A 229 5.172 26.411 16.832 1.00 32.33 ATOM 693 O CYS A 229 6.251 26.983 16.928 1.00 32.93 ATOM 694 CB CYS A 229 4.982 23.953 17.302 1.00 35.94 ATOM 695 SG CYS A 229 3.587 24.057 18.435 1.00 41.83 ATOM 696 N CYS A 230 4.029 26.951 17.234 1.00 30.00 ATOM 697 CA CYS A 230 4.001 28.244 17.884 1.00 28.58 ATOM 698 C CYS A 230 3.134 28.125 19.133 1.00 29.20 ATOM 699 O CYS A 230 2.126 27.418 19.141 1.00 27.91 ATOM 700 CB CYS A 230 3.423 29.320 16.959 1.00 29.99 ATOM 701 SG CYS A 230 3.596 31.001 17.633 1.00 29.67 ATOM 702 N VAL A 231 3.548 28.801 20.198 1.00 27.60 ATOM 703 CA VAL A 231 2.807 28.751 21.447 1.00 27.35 ATOM 704 C VAL A 231 2.615 30.134 22.025 1.00 27.47 ATOM 705 O VAL A 231 3.544 30.936 22.084 1.00 27.56 ATOM 706 CB VAL A 231 3.538 27.858 22.499 1.00 26.41 ATOM 707 CG1 VAL A 231 2.806 27.926 23.830 1.00 20.98 ATOM 708 CG2 VAL A 231 3.622 26.410 22.007 1.00 22.54 ATOM 709 N VAL A 232 1.384 30.403 22.458 1.00 27.86 ATOM 710 CA VAL A 232 1.041 31.663 23.079 1.00 27.38 ATOM 711 C VAL A 232 0.417 31.324 24.400 1.00 27.37 ATOM 712 O VAL A 232 -0.469 30.485 24.458 1.00 28.62 ATOM 713 CB VAL A 232 0.058 32.482 22.233 1.00 28.37 ATOM 714 CG1 VAL A 232 -0.408 33.700 23.032 1.00 28.35 ATOM 715 CG2 VAL A 232 0.699 32.932 20.950 1.00 31.10 ATOM 716 N VAL A 233 0.869 31.942 25.467 1.00 24.96 ATOM 717 CA VAL A 233 0.321 31.699 26.776 1.00 23.93 ATOM 718 C VAL A 233 -0.065 33.041 27.330 1.00 24.46 ATOM 719 O VAL A 233 0.720 33.965 27.346 1.00 25.21 ATOM 720 CB VAL A 233 1.321 31.055 27.743 1.00 25.32 ATOM 721 CG1 VAL A 233 0.721 30.977 29.160 1.00 26.22 ATOM 722 CG2 VAL A 233 1.696 29.673 27.252 1.00 23.86 ATOM 723 N ILE A 234 -1.293 33.155 27.770 1.00 27.74 ATOM 724 CA ILE A 234 -1.757 34.407 28.338 1.00 28.93 ATOM 725 C ILE A 234 -2.268 34.132 29.737 1.00 29.63 ATOM 726 O ILE A 234 -3.058 33.208 29.957 1.00 30.80 ATOM 727 CB ILE A 234 -2.871 35.056 27.483 1.00 28.35 ATOM 728 CG1 ILE A 234 -2.341 35.310 26.062 1.00 27.91 ATOM 729 CG2 ILE A 234 -3.300 36.401 28.097 1.00 24.62 ATOM 730 CD1 ILE A 234 -3.320 36.034 25.159 1.00 29.87 ATOM 731 N LEU A 235 -1.780 34.927 30.677 1.00 29.98 ATOM 732 CA LEU A 235 -2.157 34.812 32.084 1.00 27.91 ATOM 733 C LEU A 235 -2.661 36.188 32.465 1.00 28.59 ATOM 734 O LEU A 235 -1.900 37.157 32.449 1.00 30.46 ATOM 735 CB LEU A 235 -0.945 34.443 32.937 1.00 26.52 ATOM 736 CG LEU A 235 -0.095 33.257 32.461 1.00 26.57 ATOM 737 CD1 LEU A 235 1.087 33.090 33.398 1.00 26.64 ATOM 738 CD2 LEU A 235 -0.939 31.982 32.432 1.00 24.38 ATOM 739 N SER A 236 -3.942 36.274 32.803 1.00 28.26 ATOM 740 CA SER A 236 -4.511 37.557 33.159 1.00 27.04 ATOM 741 C SER A 236 -5.935 37.341 33.669 1.00 27.83 ATOM 742 O SER A 236 -6.360 36.209 33.851 1.00 27.53 ATOM 743 CB SER A 236 -4.540 38.449 31.908 1.00 24.05 ATOM 744 OG SER A 236 -4.984 39.753 32.202 1.00 24.43 ATOM 745 N HIS A 237 -6.651 38.439 33.903 1.00 28.97 ATOM 746 CA HIS A 237 -8.049 38.354 34.304 1.00 32.44 ATOM 747 C HIS A 237 -8.768 38.228 32.972 1.00 34.27 ATOM 748 O HIS A 237 -8.201 38.563 31.928 1.00 35.67 ATOM 749 CB HIS A 237 -8.509 39.639 34.994 1.00 32.57 ATOM 750 CG HIS A 237 -8.011 39.791 36.400 1.00 36.53 ATOM 751 ND1 HIS A 237 -8.350 38.915 37.405 1.00 36.50 ATOM 752 CD2 HIS A 237 -7.215 40.729 36.967 1.00 36.17 ATOM 753 CE1 HIS A 237 -7.788 39.307 38.536 1.00 35.75 ATOM 754 NE2 HIS A 237 -7.096 40.406 38.302 1.00 36.49 ATOM 755 N GLY A 238 -10.002 37.744 32.984 1.00 33.78 ATOM 756 CA GLY A 238 -10.747 37.598 31.750 1.00 33.16 ATOM 757 C GLY A 238 -12.233 37.856 31.900 1.00 33.88 ATOM 758 O GLY A 238 -12.723 38.126 32.994 1.00 33.37 ATOM 759 N CYS A 239 -12.952 37.781 30.786 1.00 29.85 ATOM 760 CA CYS A 239 -14.386 37.997 30.788 1.00 30.74 ATOM 761 C CYS A 239 -14.963 37.235 29.603 1.00 31.43 ATOM 762 O CYS A 239 -14.224 36.765 28.741 1.00 30.48 ATOM 763 CB CYS A 239 -14.709 39.488 30.662 1.00 36.46 ATOM 764 SG CYS A 239 -14.113 40.285 29.163 1.00 40.52 ATOM 765 N GLN A 240 -16.277 37.094 29.571 1.00 36.99 ATOM 766 CA GLN A 240 -16.926 36.375 28.491 1.00 40.96 ATOM 767 C GLN A 240 -16.957 37.231 27.242 1.00 39.80 ATOM 768 O GLN A 240 -16.998 38.453 27.316 1.00 39.59 ATOM 769 CB GLN A 240 -18.352 35.984 28.878 1.00 69.59 ATOM 770 CG GLN A 240 -18.424 34.934 29.984 1.00 79.08 ATOM 771 CD GLN A 240 -19.847 34.488 30.282 1.00 85.32 ATOM 772 OE1 GLN A 240 -20.560 34.027 29.394 1.00 88.09 ATOM 773 NE2 GLN A 240 -20.258 34.620 31.538 1.00 87.71 ATOM 774 N ALA A 240A -16.907 36.564 26.096 1.00 38.05 ATOM 775 CA ALA A 240A -16.958 37.228 24.797 1.00 37.56 ATOM 776 C ALA A 240A -17.458 36.145 23.866 1.00 37.66 ATOM 777 O ALA A 240A -16.707 35.259 23.467 1.00 38.67 ATOM 778 CB ALA A 240A -15.577 37.691 24.366 1.00 28.10 ATOM 779 N SER A 240B -18.730 36.227 23.537 1.00 37.30 ATOM 780 CA SER A 240B -19.341 35.234 22.673 1.00 38.43 ATOM 781 C SER A 240B -18.721 35.173 21.289 1.00 35.45 ATOM 782 O SER A 240B -18.394 36.186 20.688 1.00 35.29 ATOM 783 CB SER A 240B -20.843 35.502 22.551 1.00 64.27 ATOM 784 OG SER A 240B -21.481 34.514 21.769 1.00 73.03 ATOM 785 N HIS A 240C -18.548 33.951 20.805 1.00 35.85 ATOM 786 CA HIS A 240C -18.016 33.705 19.474 1.00 34.24 ATOM 787 C HIS A 240C -18.245 32.227 19.168 1.00 33.81 ATOM 788 O HIS A 240C -17.979 31.373 20.008 1.00 34.84 ATOM 789 CB HIS A 240C -16.536 34.062 19.385 1.00 32.54 ATOM 790 CG HIS A 240C -16.013 34.014 17.987 1.00 31.73 ATOM 791 ND1 HIS A 240C -15.514 32.858 17.418 1.00 29.69 ATOM 792 CD2 HIS A 240C -16.004 34.951 17.008 1.00 30.45 ATOM 793 CE1 HIS A 240C -15.225 33.083 16.152 1.00 30.70 ATOM 794 NE2 HIS A 240C -15.517 34.347 15.878 1.00 28.51 ATOM 795 N LEU A 240D -18.724 31.932 17.964 1.00 34.51 ATOM 796 CA LEU A 240D -19.045 30.550 17.615 1.00 34.92 ATOM 797 C LEU A 240D -17.879 29.590 17.511 1.00 34.36 ATOM 798 O LEU A 240D -18.081 28.375 17.445 1.00 35.06 ATOM 799 CB LEU A 240D -19.875 30.513 16.324 1.00 39.55 ATOM 800 CG LEU A 240D -19.190 30.506 14.959 1.00 43.32 ATOM 801 CD1 LEU A 240D -20.272 30.490 13.876 1.00 42.78 ATOM 802 CD2 LEU A 240D -18.290 31.714 14.805 1.00 45.03 ATOM 803 N GLN A 240E -16.654 30.104 17.503 1.00 32.02 ATOM 804 CA GLN A 240E -15.509 29.213 17.410 1.00 31.38 ATOM 805 C GLN A 240E -14.461 29.412 18.479 1.00 29.79 ATOM 806 O GLN A 240E -13.903 28.446 18.999 1.00 27.67 ATOM 807 CB GLN A 240E -14.863 29.322 16.034 1.00 37.16 ATOM 808 CG GLN A 240E -15.630 28.551 14.990 1.00 40.82 ATOM 809 CD GLN A 240E -15.183 28.834 13.579 1.00 42.72 ATOM 810 OE1 GLN A 240E -15.467 28.053 12.673 1.00 42.39 ATOM 811 NE2 GLN A 240E -14.492 29.946 13.370 1.00 44.75 ATOM 812 N PHE A 240F -14.207 30.675 18.818 1.00 28.18 ATOM 813 CA PHE A 240F -13.198 31.012 19.801 1.00 26.44 ATOM 814 C PHE A 240F -13.722 32.013 20.810 1.00 26.78 ATOM 815 O PHE A 240F -13.275 33.168 20.851 1.00 27.60 ATOM 816 CB PHE A 240F -11.962 31.595 19.091 1.00 28.92 ATOM 817 CG PHE A 240F -11.338 30.656 18.103 1.00 28.18 ATOM 818 CD1 PHE A 240F -11.360 30.948 16.738 1.00 27.82 ATOM 819 CD2 PHE A 240F -10.731 29.487 18.530 1.00 24.18 ATOM 820 CE1 PHE A 240F -10.780 30.088 15.814 1.00 26.58 ATOM 821 CE2 PHE A 240F -10.137 28.606 17.614 1.00 26.50 ATOM 822 CZ PHE A 240F -10.162 28.912 16.246 1.00 25.60 ATOM 823 N PRO A 240G -14.694 31.594 21.634 1.00 27.31 ATOM 824 CA PRO A 240G -15.272 32.475 22.647 1.00 27.64 ATOM 825 C PRO A 240G -14.276 32.843 23.745 1.00 28.38 ATOM 826 O PRO A 240G -13.263 32.170 23.934 1.00 28.97 ATOM 827 CB PRO A 240G -16.449 31.652 23.168 1.00 22.10 ATOM 828 CG PRO A 240G -15.946 30.260 23.048 1.00 22.49 ATOM 829 CD PRO A 240G -15.299 30.256 21.686 1.00 23.46 ATOM 830 N GLY A 241 -14.569 33.914 24.468 1.00 29.54 ATOM 831 CA GLY A 241 -13.699 34.349 25.543 1.00 29.64 ATOM 832 C GLY A 241 -12.908 35.609 25.236 1.00 30.57 ATOM 833 O GLY A 241 -12.799 36.031 24.085 1.00 30.64 ATOM 834 N ALA A 242 -12.365 36.215 26.281 1.00 29.54 ATOM 835 CA ALA A 242 -11.571 37.420 26.146 1.00 30.46 ATOM 836 C ALA A 242 -10.676 37.512 27.355 1.00 30.69 ATOM 837 O ALA A 242 -10.920 36.867 28.374 1.00 31.84 ATOM 838 CB ALA A 242 -12.474 38.657 26.061 1.00 21.19 ATOM 839 N VAL A 243 -9.619 38.306 27.239 1.00 30.01 ATOM 840 CA VAL A 243 -8.700 38.503 28.335 1.00 30.16 ATOM 841 C VAL A 243 -8.511 40.003 28.466 1.00 30.82 ATOM 842 O VAL A 243 -8.716 40.739 27.498 1.00 30.78 ATOM 843 CB VAL A 243 -7.323 37.833 28.064 1.00 30.23 ATOM 844 CG1 VAL A 243 -7.494 36.330 27.977 1.00 30.90 ATOM 845 CG2 VAL A 243 -6.718 38.377 26.775 1.00 29.07 ATOM 846 N TYR A 244 -8.148 40.457 29.659 1.00 28.10 ATOM 847 CA TYR A 244 -7.938 41.877 29.885 1.00 28.25 ATOM 848 C TYR A 244 -6.467 42.217 29.837 1.00 26.77 ATOM 849 O TYR A 244 -5.618 41.398 30.177 1.00 25.06 ATOM 850 CB TYR A 244 -8.457 42.308 31.261 1.00 30.25 ATOM 851 CG TYR A 244 -9.950 42.340 31.400 1.00 32.11 ATOM 852 CD1 TYR A 244 -10.610 41.442 32.228 1.00 32.66 ATOM 853 CD2 TYR A 244 -10.713 43.296 30.724 1.00 33.85 ATOM 854 CE1 TYR A 244 -11.992 41.488 32.388 1.00 31.27 ATOM 855 CE2 TYR A 244 -12.087 43.355 30.865 1.00 34.00 ATOM 856 CZ TYR A 244 -12.721 42.456 31.703 1.00 33.10 ATOM 857 OH TYR A 244 -14.080 42.522 31.861 1.00 34.88 ATOM 858 N GLY A 245 -6.168 43.442 29.417 1.00 27.86 ATOM 859 CA GLY A 245 -4.795 43.893 29.450 1.00 27.49 ATOM 860 C GLY A 245 -4.695 44.483 30.849 1.00 29.38 ATOM 861 O GLY A 245 -5.711 44.586 31.555 1.00 29.18 ATOM 862 N THR A 246 -3.505 44.879 31.272 1.00 32.18 ATOM 863 CA THR A 246 -3.348 45.453 32.602 1.00 33.64 ATOM 864 C THR A 246 -4.214 46.701 32.792 1.00 35.71 ATOM 865 O THR A 246 -4.421 47.167 33.921 1.00 37.16 ATOM 866 CB THR A 246 -1.882 45.834 32.861 1.00 30.87 ATOM 867 OG1 THR A 246 -1.452 46.700 31.822 1.00 32.45 ATOM 868 CG2 THR A 246 -1.005 44.600 32.882 1.00 28.76 ATOM 869 N ASP A 247 -4.727 47.239 31.689 1.00 31.85 ATOM 870 CA ASP A 247 -5.580 48.431 31.727 1.00 30.03 ATOM 871 C ASP A 247 -7.056 48.083 31.915 1.00 29.86 ATOM 872 O ASP A 247 -7.907 48.967 32.018 1.00 27.48 ATOM 873 CB ASP A 247 -5.424 49.243 30.434 1.00 29.42 ATOM 874 CG ASP A 247 -5.496 48.375 29.176 1.00 32.21 ATOM 875 OD1 ASP A 247 -5.272 48.904 28.065 1.00 29.93 ATOM 876 OD2 ASP A 247 -5.773 47.154 29.301 1.00 33.72 ATOM 877 N GLY A 248 -7.363 46.789 31.955 1.00 29.62 ATOM 878 CA GLY A 248 -8.750 46.399 32.115 1.00 29.12 ATOM 879 C GLY A 248 -9.498 46.494 30.802 1.00 29.55 ATOM 880 O GLY A 248 -10.729 46.486 30.782 1.00 29.41 ATOM 881 N CYS A 254 -8.755 46.601 29.704 1.00 28.30 ATOM 882 CA CYS A 254 -9.355 46.677 28.375 1.00 28.86 ATOM 883 C CYS A 254 -9.333 45.259 27.826 1.00 27.14 ATOM 884 O CYS A 254 -8.310 44.578 27.893 1.00 27.11 ATOM 885 CB CYS A 254 -8.549 47.615 27.458 1.00 32.09 ATOM 886 SG CYS A 254 -8.483 49.334 28.076 1.00 39.21 ATOM 887 N PRO A 255 -10.464 44.783 27.285 1.00 28.57 ATOM 888 CA PRO A 255 -10.560 43.430 26.737 1.00 28.76 ATOM 889 C PRO A 255 -9.951 43.209 25.366 1.00 30.48 ATOM 890 O PRO A 255 -9.927 44.104 24.517 1.00 32.08 ATOM 891 CB PRO A 255 -12.062 43.177 26.729 1.00 29.26 ATOM 892 CG PRO A 255 -12.594 44.521 26.358 1.00 27.92 ATOM 893 CD PRO A 255 -11.781 45.448 27.246 1.00 29.69 ATOM 894 N VAL A 256 -9.485 41.988 25.173 1.00 28.91 ATOM 895 CA VAL A 256 -8.911 41.530 23.919 1.00 28.85 ATOM 896 C VAL A 256 -9.551 40.156 23.775 1.00 30.17 ATOM 897 O VAL A 256 -9.304 39.260 24.584 1.00 30.78 ATOM 898 CB VAL A 256 -7.390 41.364 24.013 1.00 29.66 ATOM 899 CG1 VAL A 256 -6.854 40.854 22.690 1.00 30.75 ATOM 900 CG2 VAL A 256 -6.733 42.698 24.379 1.00 27.10 ATOM 901 N SER A 257 -10.386 39.984 22.753 1.00 28.52 ATOM 902 CA SER A 257 -11.063 38.710 22.557 1.00 28.47 ATOM 903 C SER A 257 -10.115 37.629 22.074 1.00 27.14 ATOM 904 O SER A 257 -9.107 37.922 21.431 1.00 26.52 ATOM 905 CB SER A 257 -12.209 38.856 21.551 1.00 29.32 ATOM 906 OG SER A 257 -11.725 39.143 20.257 1.00 29.59 ATOM 907 N VAL A 258 -10.451 36.385 22.401 1.00 27.39 ATOM 908 CA VAL A 258 -9.646 35.244 22.001 1.00 27.68 ATOM 909 C VAL A 258 -9.690 35.103 20.475 1.00 30.98 ATOM 910 O VAL A 258 -8.749 34.589 19.867 1.00 31.31 ATOM 911 CB VAL A 258 -10.168 33.949 22.672 1.00 25.81 ATOM 912 CG1 VAL A 258 -9.518 32.709 22.025 1.00 19.42 ATOM 913 CG2 VAL A 258 -9.856 33.989 24.161 1.00 22.15 ATOM 914 N GLU A 259 -10.786 35.555 19.866 1.00 28.89 ATOM 915 CA GLU A 259 -10.898 35.481 18.417 1.00 34.35 ATOM 916 C GLU A 259 -9.857 36.370 17.762 1.00 31.14 ATOM 917 O GLU A 259 -9.221 35.958 16.799 1.00 27.76 ATOM 918 CB GLU A 259 -12.279 35.923 17.925 1.00 83.61 ATOM 919 CG GLU A 259 -12.223 36.297 16.442 1.00 98.27 ATOM 920 CD GLU A 259 -13.561 36.668 15.848 1.00107.70 ATOM 921 OE1 GLU A 259 -14.230 37.566 16.397 1.00112.46 ATOM 922 OE2 GLU A 259 -13.929 36.069 14.816 1.00112.27 ATOM 923 N LYS A 260 -9.704 37.596 18.260 1.00 30.69 ATOM 924 CA LYS A 260 -8.718 38.497 17.684 1.00 31.54 ATOM 925 C LYS A 260 -7.324 37.904 17.894 1.00 29.96 ATOM 926 O LYS A 260 -6.511 37.884 16.980 1.00 29.31 ATOM 927 CB LYS A 260 -8.806 39.884 18.323 1.00 42.38 ATOM 928 CG LYS A 260 -7.968 40.920 17.606 1.00 46.32 ATOM 929 CD LYS A 260 -8.104 42.304 18.225 1.00 50.60 ATOM 930 CE LYS A 260 -7.378 43.335 17.367 1.00 55.11 ATOM 931 NZ LYS A 260 -7.370 44.701 17.974 1.00 55.45 ATOM 932 N ILE A 261 -7.071 37.394 19.092 1.00 32.04 ATOM 933 CA ILE A 261 -5.778 36.793 19.413 1.00 31.84 ATOM 934 C ILE A 261 -5.451 35.648 18.457 1.00 32.03 ATOM 935 O ILE A 261 -4.360 35.585 17.888 1.00 31.11 ATOM 936 CB ILE A 261 -5.749 36.271 20.869 1.00 30.22 ATOM 937 CG1 ILE A 261 -5.776 37.459 21.845 1.00 29.44 ATOM 938 CG2 ILE A 261 -4.536 35.401 21.103 1.00 27.78 ATOM 939 CD1 ILE A 261 -6.138 37.065 23.248 1.00 31.49 ATOM 940 N VAL A 262 -6.410 34.757 18.256 1.00 32.52 ATOM 941 CA VAL A 262 -6.227 33.614 17.386 1.00 33.12 ATOM 942 C VAL A 262 -6.039 33.988 15.918 1.00 34.18 ATOM 943 O VAL A 262 -5.141 33.469 15.257 1.00 34.83 ATOM 944 CB VAL A 262 -7.435 32.652 17.499 1.00 34.01 ATOM 945 CG1 VAL A 262 -7.462 31.691 16.323 1.00 32.15 ATOM 946 CG2 VAL A 262 -7.343 31.869 18.806 1.00 33.27 ATOM 947 N ASN A 263 -6.879 34.886 15.404 1.00 33.25 ATOM 948 CA ASN A 263 -6.805 35.269 14.008 1.00 35.76 ATOM 949 C ASN A 263 -5.580 36.093 13.623 1.00 35.22 ATOM 950 O ASN A 263 -5.341 36.329 12.449 1.00 34.30 ATOM 951 CB ASN A 263 -8.089 35.994 13.593 1.00 55.47 ATOM 952 CG ASN A 263 -9.297 35.073 13.613 1.00 60.11 ATOM 953 OD1 ASN A 263 -9.224 33.922 13.163 1.00 61.67 ATOM 954 ND2 ASN A 263 -10.411 35.571 14.129 1.00 62.45 ATOM 955 N ILE A 264 -4.816 36.525 14.609 1.00 35.01 ATOM 956 CA ILE A 264 -3.603 37.281 14.340 1.00 34.88 ATOM 957 C ILE A 264 -2.663 36.350 13.572 1.00 34.34 ATOM 958 O ILE A 264 -1.863 36.788 12.780 1.00 33.67 ATOM 959 CB ILE A 264 -2.890 37.701 15.647 1.00 41.02 ATOM 960 CG1 ILE A 264 -3.755 38.691 16.435 1.00 43.21 ATOM 961 CG2 ILE A 264 -1.543 38.276 15.358 1.00 39.94 ATOM 962 CD1 ILE A 264 -4.005 39.984 15.741 1.00 43.74 ATOM 963 N PHE A 265 -2.796 35.049 13.819 1.00 36.36 ATOM 964 CA PHE A 265 -1.928 34.051 13.204 1.00 37.94 ATOM 965 C PHE A 265 -2.514 33.296 12.013 1.00 40.16 ATOM 966 O PHE A 265 -2.352 32.084 11.914 1.00 41.86 ATOM 967 CB PHE A 265 -1.485 33.047 14.285 1.00 32.01 ATOM 968 CG PHE A 265 -0.868 33.688 15.481 1.00 30.10 ATOM 969 CD1 PHE A 265 0.473 33.608 15.677 1.00 29.49 ATOM 970 CD2 PHE A 265 -1.614 34.438 16.375 1.00 28.95 ATOM 971 CE1 PHE A 265 1.085 34.271 16.751 1.00 28.30 ATOM 972 CE2 PHE A 265 -1.029 35.097 17.448 1.00 26.71 ATOM 973 CZ PHE A 265 0.314 35.016 17.633 1.00 28.67 ATOM 974 N ASN A 266 -3.168 34.005 11.111 1.00 45.70 ATOM 975 CA ASN A 266 -3.787 33.402 9.925 1.00 47.74 ATOM 976 C ASN A 266 -2.778 33.082 8.811 1.00 49.15 ATOM 977 O ASN A 266 -1.642 33.507 8.859 1.00 48.92 ATOM 978 CB ASN A 266 -4.871 34.328 9.380 1.00 42.61 ATOM 979 CG ASN A 266 -4.310 35.656 8.903 1.00 44.84 ATOM 980 OD1 ASN A 266 -3.597 35.708 7.898 1.00 43.45 ATOM 981 ND2 ASN A 266 -4.616 36.734 9.624 1.00 44.47 ATOM 982 N GLY A 267 -3.241 32.338 7.800 1.00 54.58 ATOM 983 CA GLY A 267 -2.400 31.952 6.691 1.00 54.10 ATOM 984 C GLY A 267 -2.115 33.036 5.671 1.00 54.35 ATOM 985 O GLY A 267 -1.626 32.762 4.572 1.00 55.38 ATOM 986 N THR A 268 -2.419 34.278 6.022 1.00 45.88 ATOM 987 CA THR A 268 -2.180 35.415 5.148 1.00 45.06 ATOM 988 C THR A 268 -1.202 36.346 5.826 1.00 44.59 ATOM 989 O THR A 268 -0.356 36.947 5.179 1.00 44.96 ATOM 990 CB THR A 268 -3.468 36.185 4.858 1.00 45.79 ATOM 991 OG1 THR A 268 -4.301 35.403 4.010 1.00 48.76 ATOM 992 CG2 THR A 268 -3.168 37.520 4.190 1.00 46.81 ATOM 993 N SER A 269 -1.330 36.457 7.140 1.00 41.62 ATOM 994 CA SER A 269 -0.473 37.312 7.920 1.00 40.99 ATOM 995 C SER A 269 0.710 36.492 8.383 1.00 39.04 ATOM 996 O SER A 269 1.772 37.028 8.693 1.00 38.86 ATOM 997 CB SER A 269 -1.225 37.867 9.116 1.00 58.26 ATOM 998 OG SER A 269 -0.545 38.968 9.681 1.00 63.70 ATOM 999 N CYS A 270 0.535 35.171 8.409 1.00 41.08 ATOM 1000 CA CYS A 270 1.594 34.283 8.849 1.00 39.86 ATOM 1001 C CYS A 270 1.607 32.954 8.081 1.00 39.46 ATOM 1002 O CYS A 270 1.398 31.891 8.661 1.00 40.60 ATOM 1003 CB CYS A 270 1.448 34.023 10.346 1.00 34.52 ATOM 1004 SG CYS A 270 2.966 33.438 11.137 1.00 40.84 ATOM 1005 N PRO A 271 1.859 33.001 6.761 1.00 39.68 ATOM 1006 CA PRO A 271 1.894 31.770 5.968 1.00 37.85 ATOM 1007 C PRO A 271 3.008 30.862 6.482 1.00 35.90 ATOM 1008 O PRO A 271 3.006 29.653 6.271 1.00 35.79 ATOM 1009 CB PRO A 271 2.173 32.280 4.552 1.00 36.79 ATOM 1010 CG PRO A 271 2.987 33.519 4.805 1.00 36.29 ATOM 1011 CD PRO A 271 2.202 34.166 5.930 1.00 38.41 ATOM 1012 N SER A 272 3.963 31.494 7.156 1.00 34.72 ATOM 1013 CA SER A 272 5.118 30.832 7.741 1.00 33.73 ATOM 1014 C SER A 272 4.703 29.736 8.734 1.00 34.24 ATOM 1015 O SER A 272 5.431 28.760 8.930 1.00 34.63 ATOM 1016 CB SER A 272 5.968 31.892 8.451 1.00 38.10 ATOM 1017 OG SER A 272 7.147 31.356 8.985 1.00 43.63 ATOM 1018 N LEU A 273 3.538 29.909 9.367 1.00 35.08 ATOM 1019 CA LEU A 273 3.014 28.930 10.320 1.00 35.48 ATOM 1020 C LEU A 273 1.873 28.117 9.721 1.00 36.78 ATOM 1021 O LEU A 273 1.141 27.438 10.437 1.00 36.68 ATOM 1022 CB LEU A 273 2.517 29.626 11.595 1.00 27.83 ATOM 1023 CG LEU A 273 3.568 30.122 12.580 1.00 25.46 ATOM 1024 CD1 LEU A 273 2.901 30.956 13.673 1.00 25.10 ATOM 1025 CD2 LEU A 273 4.322 28.938 13.183 1.00 23.11 ATOM 1026 N GLY A 274 1.729 28.189 8.401 1.00 33.83 ATOM 1027 CA GLY A 274 0.678 27.444 7.734 1.00 33.13 ATOM 1028 C GLY A 274 0.908 25.955 7.879 1.00 32.90 ATOM 1029 O GLY A 274 2.017 25.462 7.662 1.00 33.92 ATOM 1030 N GLY A 275 -0.121 25.230 8.252 1.00 32.42 ATOM 1031 CA GLY A 275 -0.002 23.797 8.412 1.00 31.91 ATOM 1032 C GLY A 275 0.752 23.397 9.657 1.00 32.34 ATOM 1033 O GLY A 275 1.010 22.218 9.871 1.00 34.50 ATOM 1034 N LYS A 276 1.123 24.371 10.477 1.00 31.27 ATOM 1035 CA LYS A 276 1.857 24.097 11.705 1.00 30.81 ATOM 1036 C LYS A 276 0.956 24.419 12.894 1.00 30.40 ATOM 1037 O LYS A 276 0.212 25.402 12.862 1.00 29.50 ATOM 1038 CB LYS A 276 3.125 24.950 11.777 1.00 32.81 ATOM 1039 CG LYS A 276 4.120 24.662 10.656 1.00 33.81 ATOM 1040 CD LYS A 276 5.243 25.681 10.648 1.00 35.51 ATOM 1041 CE LYS A 276 6.232 25.407 9.522 1.00 34.69 ATOM 1042 NZ LYS A 276 7.323 26.416 9.534 1.00 34.40 ATOM 1043 N PRO A 277 1.036 23.606 13.955 1.00 32.03 ATOM 1044 CA PRO A 277 0.219 23.838 15.128 1.00 33.10 ATOM 1045 C PRO A 277 0.449 25.187 15.800 1.00 32.76 ATOM 1046 O PRO A 277 1.570 25.575 16.051 1.00 34.72 ATOM 1047 CB PRO A 277 0.570 22.660 16.038 1.00 31.15 ATOM 1048 CG PRO A 277 1.978 22.349 15.659 1.00 31.13 ATOM 1049 CD PRO A 277 1.907 22.436 14.157 1.00 30.90 ATOM 1050 N LYS A 278 -0.614 25.887 16.068 1.00 30.35 ATOM 1051 CA LYS A 278 -0.576 27.188 16.735 1.00 29.72 ATOM 1052 C LYS A 278 -1.352 27.005 18.037 1.00 29.76 ATOM 1053 O LYS A 278 -2.581 26.987 18.053 1.00 29.70 ATOM 1054 CB LYS A 278 -1.199 28.261 15.836 1.00 27.69 ATOM 1055 CG LYS A 278 -0.305 28.615 14.643 1.00 30.03 ATOM 1056 CD LYS A 278 -1.002 29.481 13.610 1.00 29.07 ATOM 1057 CE LYS A 278 -1.947 28.675 12.752 1.00 29.40 ATOM 1058 NZ LYS A 278 -1.251 27.721 11.849 1.00 28.71 ATOM 1059 N LEU A 279 -0.614 26.846 19.127 1.00 29.19 ATOM 1060 CA LEU A 279 -1.206 26.604 20.436 1.00 29.84 ATOM 1061 C LEU A 279 -1.449 27.841 21.279 1.00 30.50 ATOM 1062 O LEU A 279 -0.625 28.745 21.307 1.00 31.13 ATOM 1063 CB LEU A 279 -0.316 25.638 21.206 1.00 26.20 ATOM 1064 CG LEU A 279 0.107 24.432 20.369 1.00 25.77 ATOM 1065 CD1 LEU A 279 0.962 23.515 21.221 1.00 29.49 ATOM 1066 CD2 LEU A 279 -1.087 23.693 19.836 1.00 26.63 ATOM 1067 N PHE A 280 -2.587 27.861 21.958 1.00 33.48 ATOM 1068 CA PHE A 280 -2.920 28.976 22.826 1.00 34.64 ATOM 1069 C PHE A 280 -3.396 28.439 24.171 1.00 34.96 ATOM 1070 O PHE A 280 -4.362 27.690 24.235 1.00 37.08 ATOM 1071 CB PHE A 280 -4.027 29.844 22.213 1.00 27.90 ATOM 1072 CG PHE A 280 -3.668 30.414 20.875 1.00 27.44 ATOM 1073 CD1 PHE A 280 -3.702 29.617 19.733 1.00 25.96 ATOM 1074 CD2 PHE A 280 -3.262 31.732 20.761 1.00 25.12 ATOM 1075 CE1 PHE A 280 -3.343 30.128 18.508 1.00 25.22 ATOM 1076 CE2 PHE A 280 -2.890 32.251 19.532 1.00 23.65 ATOM 1077 CZ PHE A 280 -2.931 31.450 18.404 1.00 25.15 ATOM 1078 N PHE A 281 -2.683 28.809 25.232 1.00 28.98 ATOM 1079 CA PHE A 281 -3.050 28.383 26.574 1.00 29.01 ATOM 1080 C PHE A 281 -3.383 29.651 27.318 1.00 28.95 ATOM 1081 O PHE A 281 -2.501 30.472 27.578 1.00 29.65 ATOM 1082 CB PHE A 281 -1.895 27.646 27.257 1.00 31.93 ATOM 1083 CG PHE A 281 -1.465 26.409 26.537 1.00 33.56 ATOM 1084 CD1 PHE A 281 -0.519 26.468 25.523 1.00 33.39 ATOM 1085 CD2 PHE A 281 -2.036 25.176 26.851 1.00 34.08 ATOM 1086 CE1 PHE A 281 -0.144 25.325 24.818 1.00 33.01 ATOM 1087 CE2 PHE A 281 -1.673 24.026 26.150 1.00 34.66 ATOM 1088 CZ PHE A 281 -0.726 24.100 25.138 1.00 34.22 ATOM 1089 N ILE A 282 -4.660 29.819 27.628 1.00 29.35 ATOM 1090 CA ILE A 282 -5.121 31.003 28.323 1.00 29.61 ATOM 1091 C ILE A 282 -5.671 30.702 29.703 1.00 30.54 ATOM 1092 O ILE A 282 -6.541 29.845 29.862 1.00 29.12 ATOM 1093 CB ILE A 282 -6.250 31.717 27.556 1.00 35.77 ATOM 1094 CG1 ILE A 282 -5.881 31.902 26.083 1.00 36.81 ATOM 1095 CG2 ILE A 282 -6.558 33.036 28.227 1.00 36.74 ATOM 1096 CD1 ILE A 282 -4.556 32.563 25.867 1.00 41.38 ATOM 1097 N GLN A 283 -5.137 31.401 30.699 1.00 30.66 ATOM 1098 CA GLN A 283 -5.629 31.297 32.065 1.00 33.00 ATOM 1099 C GLN A 283 -6.181 32.701 32.278 1.00 34.27 ATOM 1100 O GLN A 283 -5.439 33.656 32.483 1.00 35.04 ATOM 1101 CB GLN A 283 -4.503 30.999 33.066 1.00 38.09 ATOM 1102 CG GLN A 283 -4.950 31.071 34.540 1.00 38.00 ATOM 1103 CD GLN A 283 -6.058 30.082 34.883 1.00 39.27 ATOM 1104 OE1 GLN A 283 -6.884 30.335 35.764 1.00 39.01 ATOM 1105 NE2 GLN A 283 -6.082 28.945 34.201 1.00 38.59 ATOM 1106 N ALA A 284 -7.499 32.832 32.170 1.00 40.88 ATOM 1107 CA ALA A 284 -8.153 34.119 32.330 1.00 44.24 ATOM 1108 C ALA A 284 -9.093 34.068 33.517 1.00 46.55 ATOM 1109 O ALA A 284 -10.290 33.809 33.350 1.00 47.19 ATOM 1110 CB ALA A 284 -8.914 34.466 31.071 1.00 52.11 ATOM 1111 N CYS A 285 -8.557 34.306 34.700 1.00 51.51 ATOM 1112 CA CYS A 285 -9.342 34.280 35.926 1.00 56.72 ATOM 1113 C CYS A 285 -10.612 35.131 35.815 1.00 59.44 ATOM 1114 O CYS A 285 -10.555 36.324 35.496 1.00 60.50 ATOM 1115 CB CYS A 285 -8.487 34.747 37.113 1.00 71.08 ATOM 1116 SG CYS A 285 -7.056 33.682 37.459 1.00 76.05 ATOM 1117 N GLY A 286 -11.756 34.505 36.077 1.00 84.44 ATOM 1118 CA GLY A 286 -13.018 35.209 36.017 1.00 88.26 ATOM 1119 C GLY A 286 -13.529 35.546 37.401 1.00 91.46 ATOM 1120 O GLY A 286 -13.234 34.841 38.367 1.00 92.35 TER ATOM 1121 N ALA B 298 -18.638 16.900 7.655 1.00 45.05 ATOM 1122 CA ALA B 298 -19.094 18.152 7.059 1.00 43.64 ATOM 1123 C ALA B 298 -17.974 19.192 7.096 1.00 43.94 ATOM 1124 O ALA B 298 -16.952 18.997 7.765 1.00 43.91 ATOM 1125 CB ALA B 298 -20.319 18.671 7.798 1.00 46.70 ATOM 1126 N THR B 299 -18.172 20.293 6.393 1.00 41.37 ATOM 1127 CA THR B 299 -17.174 21.356 6.334 1.00 43.10 ATOM 1128 C THR B 299 -17.855 22.716 6.319 1.00 41.27 ATOM 1129 O THR B 299 -18.960 22.857 5.811 1.00 41.23 ATOM 1130 CB THR B 299 -16.312 21.234 5.041 1.00 69.29 ATOM 1131 OG1 THR B 299 -15.641 19.965 5.031 1.00 73.23 ATOM 1132 CG2 THR B 299 -15.278 22.346 4.973 1.00 70.40 ATOM 1133 N PRO B 300 -17.215 23.744 6.908 1.00 45.69 ATOM 1134 CA PRO B 300 -17.797 25.087 6.931 1.00 46.27 ATOM 1135 C PRO B 300 -17.714 25.701 5.531 1.00 47.97 ATOM 1136 O PRO B 300 -17.047 25.149 4.658 1.00 45.06 ATOM 1137 CB PRO B 300 -16.920 25.822 7.931 1.00 50.00 ATOM 1138 CG PRO B 300 -16.489 24.729 8.864 1.00 51.04 ATOM 1139 CD PRO B 300 -16.140 23.630 7.912 1.00 49.90 ATOM 1140 N PHE B 301 -18.386 26.827 5.312 1.00 78.11 ATOM 1141 CA PHE B 301 -18.321 27.475 4.007 1.00 81.24 ATOM 1142 C PHE B 301 -18.387 28.999 4.059 1.00 84.81 ATOM 1143 O PHE B 301 -18.672 29.587 5.101 1.00 89.07 ATOM 1144 CB PHE B 301 -19.413 26.927 3.084 1.00 50.74 ATOM 1145 CG PHE B 301 -20.820 27.152 3.556 1.00 49.12 ATOM 1146 CD1 PHE B 301 -21.387 28.422 3.542 1.00 48.07 ATOM 1147 CD2 PHE B 301 -21.589 26.086 4.018 1.00 46.94 ATOM 1148 CE1 PHE B 301 -22.694 28.623 3.966 1.00 48.61 ATOM 1149 CE2 PHE B 301 -22.888 26.278 4.447 1.00 46.82 ATOM 1150 CZ PHE B 301 -23.444 27.549 4.426 1.00 48.31 ATOM 1151 N GLN B 302 -18.099 29.616 2.909 1.00 99.74 ATOM 1152 CA GLN B 302 -18.090 31.071 2.734 1.00100.88 ATOM 1153 C GLN B 302 -16.728 31.653 3.092 1.00103.85 ATOM 1154 O GLN B 302 -16.134 31.291 4.106 1.00106.55 ATOM 1155 CB GLN B 302 -19.176 31.744 3.582 1.00107.26 ATOM 1156 CG GLN B 302 -19.214 33.264 3.471 1.00108.29 ATOM 1157 CD GLN B 302 -19.448 33.753 2.049 1.00108.43 ATOM 1158 OE1 GLN B 302 -20.432 33.379 1.423 1.00107.57 ATOM 1159 NE2 GLN B 302 -18.551 34.601 1.558 1.00106.48 TER ATOM 1160 N SER B 319 -17.587 29.141 -0.095 1.00 94.82 ATOM 1161 CA SER B 319 -16.280 28.515 -0.253 1.00 97.21 ATOM 1162 C SER B 319 -16.093 27.417 0.770 1.00100.09 ATOM 1163 O SER B 319 -16.104 27.678 1.966 1.00 99.17 ATOM 1164 CB SER B 319 -15.179 29.567 -0.110 1.00 87.85 ATOM 1165 OG SER B 319 -15.290 30.557 -1.116 1.00 89.27 ATOM 1166 N SER B 320 -15.914 26.185 0.302 1.00100.07 ATOM 1167 CA SER B 320 -15.742 25.035 1.174 1.00104.79 ATOM 1168 C SER B 320 -14.289 24.668 1.451 1.00110.70 ATOM 1169 O SER B 320 -13.588 24.143 0.586 1.00107.60 ATOM 1170 CB SER B 320 -16.467 23.815 0.581 1.00 87.36 ATOM 1171 OG SER B 320 -17.842 24.080 0.378 1.00 84.36 ATOM 1172 N LEU B 321 -13.842 24.941 2.671 1.00100.87 ATOM 1173 CA LEU B 321 -12.484 24.624 3.075 1.00101.15 ATOM 1174 C LEU B 321 -12.377 24.690 4.604 1.00101.86 ATOM 1175 O LEU B 321 -12.823 25.652 5.230 1.00 96.68 ATOM 1176 CB LEU B 321 -11.459 25.574 2.435 1.00 95.15 ATOM 1177 CG LEU B 321 -11.524 27.088 2.604 1.00 98.13 ATOM 1178 CD1 LEU B 321 -10.306 27.709 1.942 1.00101.48 ATOM 1179 CD2 LEU B 321 -12.806 27.657 2.016 1.00103.63 ATOM 1180 N PRO B 322 -11.796 23.643 5.219 1.00 92.89 ATOM 1181 CA PRO B 322 -11.596 23.500 6.658 1.00 94.06 ATOM 1182 C PRO B 322 -10.851 24.650 7.320 1.00 94.70 ATOM 1183 O PRO B 322 -9.633 24.775 7.202 1.00 96.74 ATOM 1184 CB PRO B 322 -10.826 22.183 6.761 1.00 92.71 ATOM 1185 CG PRO B 322 -11.390 21.396 5.618 1.00 93.82 ATOM 1186 CD PRO B 322 -11.386 22.416 4.512 1.00 91.58 ATOM 1187 N THR B 323 -11.589 25.496 8.028 1.00109.66 ATOM 1188 CA THR B 323 -10.999 26.642 8.706 1.00105.53 ATOM 1189 C THR B 323 -11.885 26.941 9.905 1.00102.23 ATOM 1190 O THR B 323 -13.109 26.916 9.784 1.00107.16 ATOM 1191 CB THR B 323 -10.970 27.873 7.780 1.00 80.64 ATOM 1192 OG1 THR B 323 -10.398 28.982 8.477 1.00 78.89 ATOM 1193 CG2 THR B 323 -12.384 28.234 7.308 1.00 78.61 ATOM 1194 N PRO B 324 -11.299 27.249 11.078 1.00 67.36 ATOM 1195 CA PRO B 324 -9.876 27.348 11.428 1.00 60.02 ATOM 1196 C PRO B 324 -9.114 26.045 11.232 1.00 54.89 ATOM 1197 O PRO B 324 -9.718 24.968 11.176 1.00 53.62 ATOM 1198 CB PRO B 324 -9.913 27.756 12.898 1.00 61.71 ATOM 1199 CG PRO B 324 -11.197 28.486 13.026 1.00 63.77 ATOM 1200 CD PRO B 324 -12.127 27.615 12.234 1.00 66.48 ATOM 1201 N SER B 325 -7.794 26.148 11.135 1.00 47.80 ATOM 1202 CA SER B 325 -6.953 24.978 10.949 1.00 43.78 ATOM 1203 C SER B 325 -5.628 25.096 11.695 1.00 38.09 ATOM 1204 O SER B 325 -5.004 26.151 11.724 1.00 36.20 ATOM 1205 CB SER B 325 -6.649 24.754 9.463 1.00 61.03 ATOM 1206 OG SER B 325 -7.767 24.214 8.785 1.00 68.32 ATOM 1207 N ASP B 326 -5.216 23.987 12.301 1.00 33.57 ATOM 1208 CA ASP B 326 -3.966 23.941 13.026 1.00 31.97 ATOM 1209 C ASP B 326 -3.934 24.942 14.179 1.00 30.87 ATOM 1210 O ASP B 326 -2.881 25.468 14.528 1.00 30.82 ATOM 1211 CB ASP B 326 -2.819 24.218 12.047 1.00 35.23 ATOM 1212 CG ASP B 326 -2.948 23.394 10.767 1.00 34.49 ATOM 1213 OD1 ASP B 326 -3.004 22.152 10.861 1.00 35.71 ATOM 1214 OD2 ASP B 326 -2.990 24.001 9.672 1.00 33.24 ATOM 1215 N ILE B 327 -5.113 25.190 14.754 1.00 32.84 ATOM 1216 CA ILE B 327 -5.266 26.102 15.888 1.00 32.50 ATOM 1217 C ILE B 327 -5.798 25.296 17.076 1.00 33.75 ATOM 1218 O ILE B 327 -6.755 24.530 16.941 1.00 32.90 ATOM 1219 CB ILE B 327 -6.310 27.229 15.608 1.00 32.05 ATOM 1220 CG1 ILE B 327 -5.810 28.198 14.534 1.00 31.33 ATOM 1221 CG2 ILE B 327 -6.594 27.991 16.910 1.00 29.90 ATOM 1222 CD1 ILE B 327 -4.642 29.062 14.980 1.00 31.89 ATOM 1223 N PHE B 328 -5.173 25.459 18.237 1.00 33.63 ATOM 1224 CA PHE B 328 -5.623 24.771 19.442 1.00 33.23 ATOM 1225 C PHE B 328 -5.665 25.781 20.574 1.00 32.60 ATOM 1226 O PHE B 328 -4.642 26.358 20.936 1.00 32.52 ATOM 1227 CB PHE B 328 -4.681 23.630 19.833 1.00 41.73 ATOM 1228 CG PHE B 328 -5.200 22.797 20.974 1.00 43.58 ATOM 1229 CD1 PHE B 328 -5.849 21.590 20.730 1.00 44.92 ATOM 1230 CD2 PHE B 328 -5.109 23.258 22.286 1.00 44.83 ATOM 1231 CE1 PHE B 328 -6.400 20.853 21.771 1.00 45.81 ATOM 1232 CE2 PHE B 328 -5.661 22.528 23.336 1.00 46.75 ATOM 1233 CZ PHE B 328 -6.310 21.325 23.076 1.00 47.59 ATOM 1234 N VAL B 329 -6.855 25.991 21.131 1.00 33.52 ATOM 1235 CA VAL B 329 -7.014 26.926 22.223 1.00 32.97 ATOM 1236 C VAL B 329 -7.524 26.245 23.495 1.00 34.27 ATOM 1237 O VAL B 329 -8.541 25.547 23.484 1.00 34.75 ATOM 1238 CB VAL B 329 -8.008 28.060 21.859 1.00 30.71 ATOM 1239 CG1 VAL B 329 -8.192 28.996 23.063 1.00 28.15 ATOM 1240 CG2 VAL B 329 -7.487 28.848 20.673 1.00 24.08 ATOM 1241 N SER B 330 -6.789 26.424 24.575 1.00 30.94 ATOM 1242 CA SER B 330 -7.181 25.894 25.870 1.00 30.06 ATOM 1243 C SER B 330 -7.458 27.159 26.665 1.00 29.75 ATOM 1244 O SER B 330 -6.536 27.909 26.992 1.00 30.44 ATOM 1245 CB SER B 330 -6.045 25.102 26.513 1.00 35.70 ATOM 1246 OG SER B 330 -6.420 24.671 27.808 1.00 35.72 ATOM 1247 N TYR B 331 -8.732 27.410 26.945 1.00 29.15 ATOM 1248 CA TYR B 331 -9.141 28.607 27.660 1.00 30.03 ATOM 1249 C TYR B 331 -9.662 28.258 29.035 1.00 29.98 ATOM 1250 O TYR B 331 -10.710 27.640 29.160 1.00 30.27 ATOM 1251 CB TYR B 331 -10.240 29.322 26.871 1.00 28.81 ATOM 1252 CG TYR B 331 -10.690 30.644 27.449 1.00 29.32 ATOM 1253 CD1 TYR B 331 -11.918 30.763 28.107 1.00 30.29 ATOM 1254 CD2 TYR B 331 -9.906 31.794 27.300 1.00 29.62 ATOM 1255 CE1 TYR B 331 -12.354 31.996 28.596 1.00 27.91 ATOM 1256 CE2 TYR B 331 -10.332 33.031 27.783 1.00 28.89 ATOM 1257 CZ TYR B 331 -11.556 33.130 28.434 1.00 30.14 ATOM 1258 OH TYR B 331 -11.961 34.350 28.925 1.00 30.37 ATOM 1259 N SER B 332 -8.953 28.684 30.079 1.00 29.80 ATOM 1260 CA SER B 332 -9.382 28.382 31.436 1.00 30.44 ATOM 1261 C SER B 332 -9.704 29.600 32.283 1.00 31.39 ATOM 1262 O SER B 332 -8.946 30.568 32.314 1.00 29.96 ATOM 1263 CB SER B 332 -8.321 27.558 32.158 1.00 34.04 ATOM 1264 OG SER B 332 -8.519 27.636 33.557 1.00 35.96 ATOM 1265 N THR B 333 -10.832 29.536 32.977 1.00 33.02 ATOM 1266 CA THR B 333 -11.241 30.614 33.859 1.00 35.86 ATOM 1267 C THR B 333 -11.360 30.086 35.297 1.00 37.18 ATOM 1268 O THR B 333 -11.860 30.781 36.170 1.00 37.98 ATOM 1269 CB THR B 333 -12.584 31.238 33.416 1.00 44.84 ATOM 1270 OG1 THR B 333 -13.577 30.209 33.319 1.00 45.48 ATOM 1271 CG2 THR B 333 -12.442 31.910 32.050 1.00 44.87 ATOM 1272 N PHE B 334 -10.910 28.850 35.512 1.00 31.78 ATOM 1273 CA PHE B 334 -10.919 28.211 36.834 1.00 36.57 ATOM 1274 C PHE B 334 -10.050 29.095 37.741 1.00 36.89 ATOM 1275 O PHE B 334 -8.845 29.199 37.532 1.00 34.67 ATOM 1276 CB PHE B 334 -10.292 26.818 36.751 1.00 69.39 ATOM 1277 CG PHE B 334 -10.597 25.943 37.930 1.00 76.32 ATOM 1278 CD1 PHE B 334 -11.746 25.156 37.952 1.00 79.17 ATOM 1279 CD2 PHE B 334 -9.730 25.892 39.019 1.00 78.36 ATOM 1280 CE1 PHE B 334 -12.024 24.332 39.040 1.00 81.42 ATOM 1281 CE2 PHE B 334 -9.997 25.074 40.111 1.00 80.68 ATOM 1282 CZ PHE B 334 -11.151 24.292 40.120 1.00 81.69 ATOM 1283 N PRO B 335 -10.649 29.723 38.767 1.00 46.57 ATOM 1284 CA PRO B 335 -9.876 30.594 39.660 1.00 47.28 ATOM 1285 C PRO B 335 -9.148 29.945 40.832 1.00 45.10 ATOM 1286 O PRO B 335 -8.402 30.632 41.534 1.00 42.96 ATOM 1287 CB PRO B 335 -10.927 31.598 40.160 1.00 64.72 ATOM 1288 CG PRO B 335 -12.115 31.425 39.218 1.00 66.34 ATOM 1289 CD PRO B 335 -12.086 29.940 38.986 1.00 64.49 ATOM 1290 N GLY B 336 -9.356 28.640 41.052 1.00 39.44 ATOM 1291 CA GLY B 336 -8.730 27.955 42.172 1.00 40.12 ATOM 1292 C GLY B 336 -7.221 28.031 42.262 1.00 40.03 ATOM 1293 O GLY B 336 -6.546 28.097 41.222 1.00 40.42 ATOM 1294 N PHE B 337 -6.700 28.027 43.485 1.00 45.47 ATOM 1295 CA PHE B 337 -5.259 28.097 43.729 1.00 48.83 ATOM 1296 C PHE B 337 -4.782 26.711 44.174 1.00 51.36 ATOM 1297 O PHE B 337 -5.580 25.919 44.676 1.00 54.67 ATOM 1298 CB PHE B 337 -4.964 29.121 44.828 1.00 47.98 ATOM 1299 CG PHE B 337 -5.621 30.471 44.634 1.00 49.09 ATOM 1300 CD1 PHE B 337 -5.295 31.272 43.549 1.00 50.06 ATOM 1301 CD2 PHE B 337 -6.521 30.959 45.579 1.00 49.74 ATOM 1302 CE1 PHE B 337 -5.849 32.550 43.407 1.00 49.57 ATOM 1303 CE2 PHE B 337 -7.083 32.223 45.442 1.00 50.83 ATOM 1304 CZ PHE B 337 -6.751 33.022 44.362 1.00 51.01 ATOM 1305 N VAL B 338 -3.497 26.417 43.996 1.00 66.21 ATOM 1306 CA VAL B 338 -2.944 25.143 44.403 1.00 69.05 ATOM 1307 C VAL B 338 -3.284 24.935 45.867 1.00 68.24 ATOM 1308 O VAL B 338 -3.640 23.841 46.297 1.00 72.87 ATOM 1309 CB VAL B 338 -1.390 25.133 44.161 1.00 66.48 ATOM 1310 CG1 VAL B 338 -1.046 25.946 42.902 1.00 67.87 ATOM 1311 CG2 VAL B 338 -0.657 25.635 45.403 1.00 67.43 ATOM 1312 N SER B 339 -3.193 26.022 46.618 1.00 45.79 ATOM 1313 CA SER B 339 -3.533 26.033 48.030 1.00 44.87 ATOM 1314 C SER B 339 -4.748 26.939 48.078 1.00 41.89 ATOM 1315 O SER B 339 -4.613 28.168 48.112 1.00 40.12 ATOM 1316 CB SER B 339 -2.424 26.646 48.875 1.00 56.64 ATOM 1317 OG SER B 339 -2.664 26.355 50.234 1.00 60.45 ATOM 1318 N TRP B 340 -5.927 26.321 48.101 1.00 42.74 ATOM 1319 CA TRP B 340 -7.179 27.045 48.065 1.00 44.44 ATOM 1320 C TRP B 340 -7.345 28.316 48.891 1.00 45.96 ATOM 1321 O TRP B 340 -8.197 29.143 48.567 1.00 46.27 ATOM 1322 CB TRP B 340 -8.340 26.086 48.351 1.00 49.08 ATOM 1323 CG TRP B 340 -8.606 25.822 49.792 1.00 49.80 ATOM 1324 CD1 TRP B 340 -8.085 24.820 50.547 1.00 48.96 ATOM 1325 CD2 TRP B 340 -9.432 26.600 50.662 1.00 48.86 ATOM 1326 NE1 TRP B 340 -8.529 24.919 51.843 1.00 49.28 ATOM 1327 CE2 TRP B 340 -9.355 26.012 51.941 1.00 49.66 ATOM 1328 CE3 TRP B 340 -10.218 27.743 50.491 1.00 50.19 ATOM 1329 CZ2 TRP B 340 -10.041 26.527 53.047 1.00 49.38 ATOM 1330 CZ3 TRP B 340 -10.905 28.259 51.582 1.00 50.15 ATOM 1331 CH2 TRP B 340 -10.807 27.650 52.849 1.00 48.83 ATOM 1332 N ARG B 341 -6.557 28.497 49.951 1.00 47.33 ATOM 1333 CA ARG B 341 -6.687 29.727 50.746 1.00 50.37 ATOM 1334 C ARG B 341 -5.643 30.768 50.397 1.00 50.53 ATOM 1335 O ARG B 341 -5.840 31.940 50.663 1.00 51.54 ATOM 1336 CB ARG B 341 -6.559 29.446 52.248 1.00 72.75 ATOM 1337 CG ARG B 341 -7.759 28.814 52.891 1.00 77.24 ATOM 1338 CD ARG B 341 -7.644 28.839 54.403 1.00 80.59 ATOM 1339 NE ARG B 341 -8.691 28.040 55.014 1.00 83.69 ATOM 1340 CZ ARG B 341 -8.892 27.939 56.324 1.00 84.36 ATOM 1341 NH1 ARG B 341 -8.111 28.593 57.164 1.00 86.65 ATOM 1342 NH2 ARG B 341 -9.879 27.173 56.788 1.00 85.41 ATOM 1343 N ASP B 342 -4.532 30.341 49.817 1.00 46.34 ATOM 1344 CA ASP B 342 -3.463 31.273 49.481 1.00 48.81 ATOM 1345 C ASP B 342 -3.446 31.679 48.007 1.00 48.16 ATOM 1346 O ASP B 342 -3.074 30.897 47.135 1.00 45.88 ATOM 1347 CB ASP B 342 -2.109 30.671 49.884 1.00 79.83 ATOM 1348 CG ASP B 342 -0.958 31.630 49.684 1.00 84.10 ATOM 1349 OD1 ASP B 342 -0.650 31.948 48.522 1.00 89.53 ATOM 1350 OD2 ASP B 342 -0.356 32.072 50.681 1.00 88.58 ATOM 1351 N PRO B 343 -3.855 32.920 47.715 1.00 61.41 ATOM 1352 CA PRO B 343 -3.892 33.454 46.348 1.00 62.76 ATOM 1353 C PRO B 343 -2.501 33.592 45.722 1.00 63.56 ATOM 1354 O PRO B 343 -2.382 33.884 44.544 1.00 65.04 ATOM 1355 CB PRO B 343 -4.571 34.808 46.526 1.00 56.24 ATOM 1356 CG PRO B 343 -5.479 34.570 47.682 1.00 56.12 ATOM 1357 CD PRO B 343 -4.577 33.814 48.636 1.00 55.93 ATOM 1358 N LYS B 344 -1.462 33.382 46.530 1.00 56.42 ATOM 1359 CA LYS B 344 -0.074 33.469 46.065 1.00 55.62 ATOM 1360 C LYS B 344 0.487 32.092 45.759 1.00 51.20 ATOM 1361 O LYS B 344 1.588 31.990 45.240 1.00 51.54 ATOM 1362 CB LYS B 344 0.813 34.104 47.116 1.00 78.65 ATOM 1363 CG LYS B 344 0.448 35.479 47.627 1.00 84.88 ATOM 1364 CD LYS B 344 1.667 36.087 48.314 1.00 90.74 ATOM 1365 CE LYS B 344 1.336 37.340 49.100 1.00 93.80 ATOM 1366 NZ LYS B 344 0.515 37.027 50.299 1.00 96.35 ATOM 1367 N SER B 345 -0.225 31.038 46.108 1.00 49.48 ATOM 1368 CA SER B 345 0.250 29.679 45.890 1.00 46.01 ATOM 1369 C SER B 345 0.349 29.305 44.417 1.00 44.00 ATOM 1370 O SER B 345 1.111 28.408 44.052 1.00 45.31 ATOM 1371 CB SER B 345 -0.611 28.667 46.639 1.00 40.23 ATOM 1372 OG SER B 345 -1.969 28.738 46.227 1.00 35.92 ATOM 1373 N GLY B 346 -0.400 29.984 43.578 1.00 42.72 ATOM 1374 CA GLY B 346 -0.374 29.682 42.158 1.00 39.83 ATOM 1375 C GLY B 346 -1.688 29.091 41.701 1.00 38.54 ATOM 1376 O GLY B 346 -2.457 28.576 42.502 1.00 37.42 ATOM 1377 N SER B 347 -1.944 29.181 40.403 1.00 41.09 ATOM 1378 CA SER B 347 -3.170 28.675 39.813 1.00 40.04 ATOM 1379 C SER B 347 -3.239 27.157 39.791 1.00 40.84 ATOM 1380 O SER B 347 -2.309 26.476 39.345 1.00 40.60 ATOM 1381 CB SER B 347 -3.304 29.217 38.384 1.00 41.64 ATOM 1382 OG SER B 347 -4.277 28.496 37.647 1.00 40.42 ATOM 1383 N TRP B 348 -4.361 26.625 40.281 1.00 35.91 ATOM 1384 CA TRP B 348 -4.584 25.189 40.309 1.00 34.92 ATOM 1385 C TRP B 348 -4.537 24.615 38.896 1.00 34.35 ATOM 1386 O TRP B 348 -3.943 23.563 38.661 1.00 34.33 ATOM 1387 CB TRP B 348 -5.944 24.868 40.915 1.00 39.97 ATOM 1388 CG TRP B 348 -6.147 23.404 41.092 1.00 42.54 ATOM 1389 CD1 TRP B 348 -5.715 22.629 42.132 1.00 43.82 ATOM 1390 CD2 TRP B 348 -6.795 22.514 40.169 1.00 43.49 ATOM 1391 NE1 TRP B 348 -6.046 21.313 41.918 1.00 45.64 ATOM 1392 CE2 TRP B 348 -6.709 21.214 40.723 1.00 45.01 ATOM 1393 CE3 TRP B 348 -7.430 22.689 38.938 1.00 43.80 ATOM 1394 CZ2 TRP B 348 -7.234 20.092 40.079 1.00 46.90 ATOM 1395 CZ3 TRP B 348 -7.959 21.572 38.293 1.00 45.98 ATOM 1396 CH2 TRP B 348 -7.857 20.286 38.871 1.00 46.63 ATOM 1397 N TYR B 349 -5.196 25.295 37.957 1.00 31.56 ATOM 1398 CA TYR B 349 -5.223 24.852 36.570 1.00 31.19 ATOM 1399 C TYR B 349 -3.822 24.807 35.955 1.00 28.89 ATOM 1400 O TYR B 349 -3.479 23.865 35.252 1.00 28.30 ATOM 1401 CB TYR B 349 -6.121 25.766 35.736 1.00 40.95 ATOM 1402 CG TYR B 349 -5.951 25.547 34.254 1.00 43.19 ATOM 1403 CD1 TYR B 349 -6.560 24.469 33.607 1.00 45.16 ATOM 1404 CD2 TYR B 349 -5.118 26.381 33.509 1.00 46.43 ATOM 1405 CE1 TYR B 349 -6.337 24.236 32.252 1.00 47.02 ATOM 1406 CE2 TYR B 349 -4.889 26.159 32.167 1.00 47.60 ATOM 1407 CZ TYR B 349 -5.497 25.081 31.539 1.00 48.98 ATOM 1408 OH TYR B 349 -5.228 24.870 30.204 1.00 52.54 ATOM 1409 N VAL B 350 -3.010 25.823 36.201 1.00 34.68 ATOM 1410 CA VAL B 350 -1.660 25.828 35.650 1.00 35.71 ATOM 1411 C VAL B 350 -0.863 24.643 36.200 1.00 37.05 ATOM 1412 O VAL B 350 -0.214 23.922 35.439 1.00 36.78 ATOM 1413 CB VAL B 350 -0.934 27.139 35.984 1.00 33.00 ATOM 1414 CG1 VAL B 350 0.514 27.046 35.576 1.00 31.45 ATOM 1415 CG2 VAL B 350 -1.600 28.292 35.257 1.00 32.64 ATOM 1416 N GLU B 351 -0.924 24.449 37.515 1.00 34.87 ATOM 1417 CA GLU B 351 -0.218 23.361 38.173 1.00 35.46 ATOM 1418 C GLU B 351 -0.652 22.013 37.614 1.00 34.66 ATOM 1419 O GLU B 351 0.165 21.169 37.268 1.00 32.98 ATOM 1420 CB GLU B 351 -0.482 23.409 39.679 1.00 36.64 ATOM 1421 CG GLU B 351 0.038 22.219 40.474 1.00 42.29 ATOM 1422 CD GLU B 351 1.528 22.020 40.341 1.00 45.78 ATOM 1423 OE1 GLU B 351 2.252 23.022 40.195 1.00 48.25 ATOM 1424 OE2 GLU B 351 1.975 20.859 40.404 1.00 46.39 ATOM 1425 N THR B 352 -1.957 21.816 37.506 1.00 37.48 ATOM 1426 CA THR B 352 -2.474 20.570 36.985 1.00 37.17 ATOM 1427 C THR B 352 -1.967 20.339 35.570 1.00 36.63 ATOM 1428 O THR B 352 -1.613 19.222 35.204 1.00 34.25 ATOM 1429 CB THR B 352 -3.998 20.575 36.960 1.00 36.06 ATOM 1430 OG1 THR B 352 -4.490 20.804 38.293 1.00 38.06 ATOM 1431 CG2 THR B 352 -4.528 19.249 36.451 1.00 34.24 ATOM 1432 N LEU B 353 -1.923 21.401 34.771 1.00 32.15 ATOM 1433 CA LEU B 353 -1.444 21.282 33.408 1.00 32.79 ATOM 1434 C LEU B 353 0.040 20.934 33.428 1.00 31.60 ATOM 1435 O LEU B 353 0.464 19.999 32.748 1.00 30.76 ATOM 1436 CB LEU B 353 -1.696 22.579 32.638 1.00 55.55 ATOM 1437 CG LEU B 353 -1.492 22.537 31.120 1.00 57.39 ATOM 1438 CD1 LEU B 353 -2.210 23.704 30.473 1.00 61.67 ATOM 1439 CD2 LEU B 353 -0.016 22.581 30.791 1.00 59.59 ATOM 1440 N ASP B 354 0.812 21.673 34.207 1.00 33.60 ATOM 1441 CA ASP B 354 2.242 21.400 34.267 1.00 36.20 ATOM 1442 C ASP B 354 2.496 19.962 34.714 1.00 37.81 ATOM 1443 O ASP B 354 3.287 19.238 34.098 1.00 37.87 ATOM 1444 CB ASP B 354 2.937 22.345 35.240 1.00 44.94 ATOM 1445 CG ASP B 354 4.434 22.364 35.054 1.00 48.22 ATOM 1446 OD1 ASP B 354 5.163 22.465 36.065 1.00 49.96 ATOM 1447 OD2 ASP B 354 4.891 22.291 33.895 1.00 47.81 ATOM 1448 N ASP B 355 1.812 19.554 35.769 1.00 38.87 ATOM 1449 CA ASP B 355 1.938 18.208 36.329 1.00 39.14 ATOM 1450 C ASP B 355 1.706 17.144 35.263 1.00 37.54 ATOM 1451 O ASP B 355 2.520 16.246 35.070 1.00 36.59 ATOM 1452 CB ASP B 355 0.934 18.025 37.468 1.00 54.05 ATOM 1453 CG ASP B 355 1.109 16.708 38.202 1.00 55.23 ATOM 1454 OD1 ASP B 355 0.105 16.117 38.616 1.00 58.22 ATOM 1455 OD2 ASP B 355 2.267 16.273 38.383 1.00 58.15 ATOM 1456 N ILE B 356 0.575 17.244 34.577 1.00 34.31 ATOM 1457 CA ILE B 356 0.218 16.294 33.530 1.00 34.15 ATOM 1458 C ILE B 356 1.283 16.249 32.446 1.00 34.82 ATOM 1459 O ILE B 356 1.626 15.174 31.949 1.00 33.39 ATOM 1460 CB ILE B 356 -1.133 16.658 32.889 1.00 35.84 ATOM 1461 CG1 ILE B 356 -2.253 16.467 33.916 1.00 37.17 ATOM 1462 CG2 ILE B 356 -1.386 15.796 31.662 1.00 34.69 ATOM 1463 CD1 ILE B 356 -2.338 15.061 34.464 1.00 39.29 ATOM 1464 N PHE B 357 1.803 17.416 32.072 1.00 37.96 ATOM 1465 CA PHE B 357 2.821 17.483 31.040 1.00 40.82 ATOM 1466 C PHE B 357 4.075 16.763 31.481 1.00 41.76 ATOM 1467 O PHE B 357 4.615 15.934 30.756 1.00 41.99 ATOM 1468 CB PHE B 357 3.155 18.941 30.704 1.00 40.41 ATOM 1469 CG PHE B 357 2.316 19.514 29.605 1.00 40.66 ATOM 1470 CD1 PHE B 357 0.933 19.510 29.697 1.00 39.48 ATOM 1471 CD2 PHE B 357 2.902 20.041 28.463 1.00 39.98 ATOM 1472 CE1 PHE B 357 0.157 20.017 28.679 1.00 40.27 ATOM 1473 CE2 PHE B 357 2.125 20.553 27.435 1.00 41.12 ATOM 1474 CZ PHE B 357 0.743 20.540 27.544 1.00 39.67 ATOM 1475 N GLU B 358 4.524 17.080 32.691 1.00 43.60 ATOM 1476 CA GLU B 358 5.714 16.471 33.252 1.00 46.33 ATOM 1477 C GLU B 358 5.656 14.946 33.212 1.00 46.61 ATOM 1478 O GLU B 358 6.652 14.277 32.958 1.00 45.78 ATOM 1479 CB GLU B 358 5.913 16.924 34.699 1.00 54.33 ATOM 1480 CG GLU B 358 7.100 16.282 35.385 1.00 56.30 ATOM 1481 CD GLU B 358 8.424 16.793 34.867 1.00 56.96 ATOM 1482 OE1 GLU B 358 9.459 16.165 35.162 1.00 58.28 ATOM 1483 OE2 GLU B 358 8.433 17.834 34.174 1.00 57.76 ATOM 1484 N GLN B 359 4.476 14.397 33.450 1.00 45.22 ATOM 1485 CA GLN B 359 4.315 12.952 33.474 1.00 47.29 ATOM 1486 C GLN B 359 3.903 12.316 32.161 1.00 45.22 ATOM 1487 O GLN B 359 4.190 11.142 31.925 1.00 45.11 ATOM 1488 CB GLN B 359 3.299 12.554 34.533 1.00 64.06 ATOM 1489 CG GLN B 359 3.629 13.013 35.941 1.00 73.06 ATOM 1490 CD GLN B 359 2.570 12.626 36.949 1.00 77.94 ATOM 1491 OE1 GLN B 359 2.635 12.996 38.123 1.00 81.56 ATOM 1492 NE2 GLN B 359 1.574 11.870 36.489 1.00 80.65 ATOM 1493 N TRP B 360 3.241 13.057 31.281 1.00 41.81 ATOM 1494 CA TRP B 360 2.795 12.420 30.058 1.00 41.64 ATOM 1495 C TRP B 360 3.160 13.011 28.707 1.00 40.21 ATOM 1496 O TRP B 360 2.902 12.368 27.690 1.00 39.19 ATOM 1497 CB TRP B 360 1.279 12.241 30.115 1.00 49.38 ATOM 1498 CG TRP B 360 0.810 11.595 31.369 1.00 51.50 ATOM 1499 CD1 TRP B 360 0.337 12.215 32.493 1.00 52.64 ATOM 1500 CD2 TRP B 360 0.771 10.187 31.646 1.00 52.29 ATOM 1501 NE1 TRP B 360 0.008 11.282 33.449 1.00 51.99 ATOM 1502 CE2 TRP B 360 0.264 10.032 32.951 1.00 52.38 ATOM 1503 CE3 TRP B 360 1.127 9.045 30.912 1.00 51.98 ATOM 1504 CZ2 TRP B 360 0.090 8.780 33.544 1.00 53.27 ATOM 1505 CZ3 TRP B 360 0.950 7.794 31.501 1.00 53.05 ATOM 1506 CH2 TRP B 360 0.435 7.674 32.805 1.00 53.56 ATOM 1507 N ALA B 361 3.744 14.194 28.664 1.00 39.68 ATOM 1508 CA ALA B 361 4.079 14.802 27.378 1.00 40.85 ATOM 1509 C ALA B 361 4.987 13.898 26.553 1.00 42.61 ATOM 1510 O ALA B 361 4.866 13.829 25.327 1.00 43.06 ATOM 1511 CB ALA B 361 4.731 16.167 27.577 1.00 21.25 ATOM 1512 N HIS B 362 5.897 13.200 27.219 1.00 45.53 ATOM 1513 CA HIS B 362 6.834 12.324 26.536 1.00 48.11 ATOM 1514 C HIS B 362 6.154 11.214 25.745 1.00 46.02 ATOM 1515 O HIS B 362 6.707 10.729 24.762 1.00 44.99 ATOM 1516 CB HIS B 362 7.806 11.697 27.546 1.00 81.39 ATOM 1517 CG HIS B 362 7.214 10.600 28.362 1.00 88.99 ATOM 1518 ND1 HIS B 362 6.176 10.801 29.242 1.00 92.20 ATOM 1519 CD2 HIS B 362 7.495 9.270 28.416 1.00 91.91 ATOM 1520 CE1 HIS B 362 5.845 9.652 29.799 1.00 93.33 ATOM 1521 NE2 HIS B 362 6.627 8.710 29.311 1.00 93.61 ATOM 1522 N SER B 363 4.966 10.795 26.160 1.00 44.47 ATOM 1523 CA SER B 363 4.304 9.710 25.457 1.00 44.40 ATOM 1524 C SER B 363 2.891 9.974 24.960 1.00 44.07 ATOM 1525 O SER B 363 2.325 9.139 24.259 1.00 43.71 ATOM 1526 CB SER B 363 4.304 8.454 26.332 1.00 54.87 ATOM 1527 OG SER B 363 3.566 8.659 27.522 1.00 55.59 ATOM 1528 N GLU B 364 2.313 11.108 25.332 1.00 46.15 ATOM 1529 CA GLU B 364 0.958 11.412 24.899 1.00 44.92 ATOM 1530 C GLU B 364 0.857 12.750 24.175 1.00 42.82 ATOM 1531 O GLU B 364 1.560 13.696 24.513 1.00 43.44 ATOM 1532 CB GLU B 364 0.017 11.398 26.093 1.00 49.46 ATOM 1533 CG GLU B 364 0.067 10.126 26.917 1.00 51.78 ATOM 1534 CD GLU B 364 -1.090 10.001 27.892 1.00 52.13 ATOM 1535 OE1 GLU B 364 -1.585 11.044 28.370 1.00 51.96 ATOM 1536 OE2 GLU B 364 -1.500 8.863 28.187 1.00 53.61 ATOM 1537 N ASP B 365 -0.018 12.811 23.206 1.00 41.98 ATOM 1538 CA ASP B 365 -0.223 14.031 22.427 1.00 42.13 ATOM 1539 C ASP B 365 -1.032 15.064 23.223 1.00 41.03 ATOM 1540 O ASP B 365 -1.621 14.745 24.256 1.00 40.78 ATOM 1541 CB ASP B 365 -0.943 13.687 21.130 1.00 52.23 ATOM 1542 CG ASP B 365 -2.222 12.921 21.364 1.00 54.97 ATOM 1543 OD1 ASP B 365 -3.287 13.557 21.473 1.00 56.89 ATOM 1544 OD2 ASP B 365 -2.153 11.681 21.455 1.00 59.97 ATOM 1545 N LEU B 366 -1.048 16.297 22.724 1.00 41.88 ATOM 1546 CA LEU B 366 -1.743 17.403 23.373 1.00 40.94 ATOM 1547 C LEU B 366 -3.192 17.089 23.750 1.00 40.87 ATOM 1548 O LEU B 366 -3.617 17.381 24.864 1.00 41.33 ATOM 1549 CB LEU B 366 -1.697 18.656 22.479 1.00 33.60 ATOM 1550 CG LEU B 366 -2.204 19.952 23.125 1.00 32.00 ATOM 1551 CD1 LEU B 366 -1.387 20.259 24.386 1.00 30.69 ATOM 1552 CD2 LEU B 366 -2.091 21.109 22.136 1.00 30.96 ATOM 1553 N GLN B 367 -3.956 16.497 22.833 1.00 41.38 ATOM 1554 CA GLN B 367 -5.354 16.155 23.117 1.00 42.90 ATOM 1555 C GLN B 367 -5.495 15.279 24.356 1.00 42.10 ATOM 1556 O GLN B 367 -6.363 15.533 25.198 1.00 41.68 ATOM 1557 CB GLN B 367 -5.996 15.417 21.941 1.00 46.25 ATOM 1558 CG GLN B 367 -6.482 16.308 20.832 1.00 48.63 ATOM 1559 CD GLN B 367 -7.255 15.524 19.786 1.00 51.07 ATOM 1560 OE1 GLN B 367 -8.301 14.952 20.072 1.00 51.81 ATOM 1561 NE2 GLN B 367 -6.726 15.486 18.569 1.00 52.52 ATOM 1562 N SER B 368 -4.653 14.260 24.456 1.00 38.99 ATOM 1563 CA SER B 368 -4.691 13.351 25.595 1.00 39.31 ATOM 1564 C SER B 368 -4.267 14.059 26.874 1.00 38.21 ATOM 1565 O SER B 368 -4.800 13.794 27.945 1.00 39.23 ATOM 1566 CB SER B 368 -3.785 12.149 25.353 1.00 43.23 ATOM 1567 OG SER B 368 -4.216 11.438 24.212 1.00 46.25 ATOM 1568 N LEU B 369 -3.293 14.962 26.758 1.00 37.58 ATOM 1569 CA LEU B 369 -2.830 15.708 27.916 1.00 35.68 ATOM 1570 C LEU B 369 -3.962 16.559 28.483 1.00 35.59 ATOM 1571 O LEU B 369 -4.203 16.553 29.691 1.00 35.22 ATOM 1572 CB LEU B 369 -1.649 16.598 27.536 1.00 30.70 ATOM 1573 CG LEU B 369 -0.372 15.887 27.079 1.00 31.89 ATOM 1574 CD1 LEU B 369 0.671 16.931 26.774 1.00 27.81 ATOM 1575 CD2 LEU B 369 0.124 14.907 28.159 1.00 28.71 ATOM 1576 N LEU B 370 -4.663 17.281 27.608 1.00 34.98 ATOM 1577 CA LEU B 370 -5.762 18.144 28.034 1.00 36.05 ATOM 1578 C LEU B 370 -6.999 17.353 28.456 1.00 36.15 ATOM 1579 O LEU B 370 -7.832 17.850 29.210 1.00 36.80 ATOM 1580 CB LEU B 370 -6.113 19.149 26.939 1.00 38.01 ATOM 1581 CG LEU B 370 -5.251 20.417 26.919 1.00 37.69 ATOM 1582 CD1 LEU B 370 -5.466 21.195 28.185 1.00 37.37 ATOM 1583 CD2 LEU B 370 -3.781 20.048 26.796 1.00 37.85 ATOM 1584 N LEU B 371 -7.120 16.120 27.972 1.00 36.79 ATOM 1585 CA LEU B 371 -8.249 15.294 28.368 1.00 39.21 ATOM 1586 C LEU B 371 -7.975 14.909 29.826 1.00 39.72 ATOM 1587 O LEU B 371 -8.892 14.884 30.652 1.00 39.37 ATOM 1588 CB LEU B 371 -8.336 14.034 27.494 1.00 48.47 ATOM 1589 CG LEU B 371 -9.741 13.430 27.392 1.00 50.47 ATOM 1590 CD1 LEU B 371 -9.691 12.179 26.534 1.00 51.14 ATOM 1591 CD2 LEU B 371 -10.280 13.103 28.776 1.00 52.37 ATOM 1592 N ARG B 372 -6.717 14.631 30.148 1.00 44.53 ATOM 1593 CA ARG B 372 -6.348 14.292 31.515 1.00 45.25 ATOM 1594 C ARG B 372 -6.595 15.503 32.401 1.00 46.35 ATOM 1595 O ARG B 372 -7.030 15.365 33.543 1.00 47.24 ATOM 1596 CB ARG B 372 -4.872 13.901 31.604 1.00 38.74 ATOM 1597 CG ARG B 372 -4.545 12.483 31.164 1.00 38.78 ATOM 1598 CD ARG B 372 -3.036 12.271 31.204 1.00 41.30 ATOM 1599 NE ARG B 372 -2.652 10.926 30.798 1.00 42.54 ATOM 1600 CZ ARG B 372 -2.727 9.857 31.577 1.00 43.97 ATOM 1601 NH1 ARG B 372 -3.183 9.967 32.822 1.00 42.80 ATOM 1602 NH2 ARG B 372 -2.367 8.669 31.112 1.00 42.23 ATOM 1603 N VAL B 373 -6.312 16.695 31.878 1.00 40.30 ATOM 1604 CA VAL B 373 -6.526 17.906 32.652 1.00 40.11 ATOM 1605 C VAL B 373 -8.020 18.076 32.892 1.00 41.47 ATOM 1606 O VAL B 373 -8.446 18.346 34.012 1.00 42.32 ATOM 1607 CB VAL B 373 -5.973 19.162 31.917 1.00 38.30 ATOM 1608 CG1 VAL B 373 -6.376 20.432 32.661 1.00 35.71 ATOM 1609 CG2 VAL B 373 -4.459 19.085 31.833 1.00 36.70 ATOM 1610 N ALA B 374 -8.820 17.897 31.846 1.00 41.77 ATOM 1611 CA ALA B 374 -10.264 18.037 31.977 1.00 43.29 ATOM 1612 C ALA B 374 -10.772 17.026 32.986 1.00 45.30 ATOM 1613 O ALA B 374 -11.667 17.319 33.779 1.00 44.57 ATOM 1614 CB ALA B 374 -10.925 17.814 30.642 1.00 22.28 ATOM 1615 N ASN B 375 -10.195 15.831 32.954 1.00 45.51 ATOM 1616 CA ASN B 375 -10.573 14.755 33.858 1.00 48.24 ATOM 1617 C ASN B 375 -10.309 15.216 35.297 1.00 46.46 ATOM 1618 O ASN B 375 -11.144 15.036 36.188 1.00 45.77 ATOM 1619 CB ASN B 375 -9.763 13.500 33.536 1.00 85.93 ATOM 1620 CG ASN B 375 -10.483 12.224 33.918 1.00 92.80 ATOM 1621 OD1 ASN B 375 -11.605 11.987 33.480 1.00 95.63 ATOM 1622 ND2 ASN B 375 -9.837 11.390 34.727 1.00 95.13 ATOM 1623 N ALA B 376 -9.146 15.823 35.513 1.00 39.21 ATOM 1624 CA ALA B 376 -8.778 16.335 36.829 1.00 41.17 ATOM 1625 C ALA B 376 -9.714 17.468 37.247 1.00 44.19 ATOM 1626 O ALA B 376 -10.301 17.440 38.317 1.00 42.20 ATOM 1627 CB ALA B 376 -7.344 16.821 36.814 1.00 30.57 ATOM 1628 N VAL B 377 -9.835 18.479 36.391 1.00 66.94 ATOM 1629 CA VAL B 377 -10.704 19.603 36.706 1.00 71.83 ATOM 1630 C VAL B 377 -12.081 19.093 37.121 1.00 74.55 ATOM 1631 O VAL B 377 -12.719 19.650 38.014 1.00 75.01 ATOM 1632 CB VAL B 377 -10.866 20.548 35.495 1.00 64.84 ATOM 1633 CG1 VAL B 377 -11.703 21.743 35.883 1.00 64.23 ATOM 1634 CG2 VAL B 377 -9.496 21.007 35.004 1.00 65.87 ATOM 1635 N SER B 378 -12.511 18.014 36.476 1.00 67.16 ATOM 1636 CA SER B 378 -13.810 17.413 36.743 1.00 68.42 ATOM 1637 C SER B 378 -14.053 16.934 38.179 1.00 70.27 ATOM 1638 O SER B 378 -15.144 17.122 38.723 1.00 70.08 ATOM 1639 CB SER B 378 -14.040 16.247 35.780 1.00 72.44 ATOM 1640 OG SER B 378 -15.335 15.717 35.938 1.00 72.61 ATOM 1641 N VAL B 379 -13.053 16.318 38.800 1.00 77.83 ATOM 1642 CA VAL B 379 -13.197 15.824 40.165 1.00 78.19 ATOM 1643 C VAL B 379 -12.777 16.873 41.191 1.00 80.55 ATOM 1644 O VAL B 379 -12.557 16.566 42.360 1.00 82.25 ATOM 1645 CB VAL B 379 -12.365 14.533 40.398 1.00 59.94 ATOM 1646 CG1 VAL B 379 -12.665 13.525 39.295 1.00 58.19 ATOM 1647 CG2 VAL B 379 -10.878 14.864 40.439 1.00 58.85 ATOM 1648 N LYS B 380 -12.663 18.117 40.739 1.00 73.65 ATOM 1649 CA LYS B 380 -12.256 19.231 41.595 1.00 75.03 ATOM 1650 C LYS B 380 -13.456 20.126 41.909 1.00 78.35 ATOM 1651 O LYS B 380 -13.448 20.863 42.901 1.00 78.58 ATOM 1652 CB LYS B 380 -11.161 20.038 40.893 1.00 66.62 ATOM 1653 CG LYS B 380 -10.671 21.269 41.647 1.00 63.83 ATOM 1654 CD LYS B 380 -9.811 20.900 42.837 1.00 61.56 ATOM 1655 CE LYS B 380 -9.245 22.148 43.494 1.00 60.87 ATOM 1656 NZ LYS B 380 -8.424 21.835 44.700 1.00 60.52 ATOM 1657 N GLY B 381 -14.469 20.054 41.055 1.00 83.17 ATOM 1658 CA GLY B 381 -15.676 20.853 41.212 1.00 88.56 ATOM 1659 C GLY B 381 -16.504 20.682 39.951 1.00 92.59 ATOM 1660 O GLY B 381 -17.163 19.655 39.786 1.00 92.66 ATOM 1661 N ILE B 382 -16.472 21.690 39.084 1.00 98.16 ATOM 1662 CA ILE B 382 -17.158 21.685 37.784 1.00103.75 ATOM 1663 C ILE B 382 -18.519 22.345 37.586 1.00106.43 ATOM 1664 O ILE B 382 -19.574 21.796 37.906 1.00106.02 ATOM 1665 CB ILE B 382 -17.247 20.265 37.192 1.00118.06 ATOM 1666 CG1 ILE B 382 -15.851 19.660 37.116 1.00119.82 ATOM 1667 CG2 ILE B 382 -17.872 20.302 35.804 1.00118.94 ATOM 1668 CD1 ILE B 382 -14.803 20.627 36.613 1.00120.62 ATOM 1669 N TYR B 383 -18.438 23.540 37.007 1.00121.46 ATOM 1670 CA TYR B 383 -19.547 24.417 36.633 1.00125.49 ATOM 1671 C TYR B 383 -18.755 25.252 35.659 1.00125.42 ATOM 1672 O TYR B 383 -19.249 25.757 34.654 1.00126.34 ATOM 1673 CB TYR B 383 -20.006 25.292 37.796 1.00134.73 ATOM 1674 CG TYR B 383 -21.255 24.785 38.484 1.00139.13 ATOM 1675 CD1 TYR B 383 -21.216 23.631 39.274 1.00140.88 ATOM 1676 CD2 TYR B 383 -22.473 25.445 38.342 1.00141.00 ATOM 1677 CE1 TYR B 383 -22.362 23.148 39.890 1.00142.19 ATOM 1678 CE2 TYR B 383 -23.626 24.967 38.956 1.00142.41 ATOM 1679 CZ TYR B 383 -23.564 23.822 39.731 1.00142.78 ATOM 1680 OH TYR B 383 -24.702 23.345 40.347 1.00143.07 ATOM 1681 N LYS B 384 -17.478 25.352 36.002 1.00116.48 ATOM 1682 CA LYS B 384 -16.492 26.058 35.220 1.00116.08 ATOM 1683 C LYS B 384 -16.037 24.997 34.230 1.00116.53 ATOM 1684 O LYS B 384 -16.541 24.945 33.107 1.00115.89 ATOM 1685 CB LYS B 384 -15.331 26.486 36.114 1.00118.30 ATOM 1686 CG LYS B 384 -14.791 27.861 35.800 1.00117.52 ATOM 1687 CD LYS B 384 -14.301 27.943 34.372 1.00117.09 ATOM 1688 CE LYS B 384 -13.064 27.081 34.148 1.00116.26 ATOM 1689 NZ LYS B 384 -12.472 27.332 32.806 1.00115.44 ATOM 1690 N GLN B 385 -15.121 24.130 34.666 1.00130.86 ATOM 1691 CA GLN B 385 -14.589 23.046 33.831 1.00130.11 ATOM 1692 C GLN B 385 -14.572 23.576 32.426 1.00128.47 ATOM 1693 O GLN B 385 -14.805 22.850 31.458 1.00130.09 ATOM 1694 CB GLN B 385 -15.498 21.813 33.896 1.00121.98 ATOM 1695 CG GLN B 385 -14.895 20.519 33.324 1.00122.68 ATOM 1696 CD GLN B 385 -15.367 20.212 31.913 1.00122.98 ATOM 1697 OE1 GLN B 385 -16.570 20.221 31.634 1.00122.55 ATOM 1698 NE2 GLN B 385 -14.427 19.911 31.026 1.00122.32 ATOM 1699 N MET B 386 -14.275 24.862 32.306 1.00113.08 ATOM 1700 CA MET B 386 -14.287 25.491 31.011 1.00109.83 ATOM 1701 C MET B 386 -12.952 25.588 30.308 1.00105.56 ATOM 1702 O MET B 386 -12.754 26.491 29.487 1.00105.77 ATOM 1703 CB MET B 386 -14.944 26.868 31.101 1.00123.47 ATOM 1704 CG MET B 386 -15.676 27.282 29.838 1.00126.53 ATOM 1705 SD MET B 386 -17.099 28.337 30.183 1.00129.69 ATOM 1706 CE MET B 386 -18.371 27.101 30.574 1.00129.39 ATOM 1707 N PRO B 387 -11.999 24.685 30.620 1.00106.51 ATOM 1708 CA PRO B 387 -10.752 24.832 29.875 1.00103.34 ATOM 1709 C PRO B 387 -11.166 24.696 28.413 1.00100.25 ATOM 1710 O PRO B 387 -10.346 24.741 27.490 1.00100.87 ATOM 1711 CB PRO B 387 -9.925 23.657 30.369 1.00 87.20 ATOM 1712 CG PRO B 387 -10.310 23.581 31.801 1.00 87.30 ATOM 1713 CD PRO B 387 -11.818 23.740 31.741 1.00 89.08 ATOM 1714 N GLY B 388 -12.479 24.524 28.249 1.00 93.14 ATOM 1715 CA GLY B 388 -13.116 24.392 26.955 1.00 84.83 ATOM 1716 C GLY B 388 -12.148 24.584 25.832 1.00 78.04 ATOM 1717 O GLY B 388 -12.033 25.665 25.269 1.00 81.19 ATOM 1718 N CYS B 389 -11.423 23.524 25.511 1.00 55.21 ATOM 1719 CA CYS B 389 -10.467 23.618 24.439 1.00 49.22 ATOM 1720 C CYS B 389 -11.203 23.718 23.106 1.00 43.24 ATOM 1721 O CYS B 389 -12.285 23.148 22.925 1.00 40.52 ATOM 1722 CB CYS B 389 -9.522 22.418 24.455 1.00 73.05 ATOM 1723 SG CYS B 389 -10.105 20.989 23.557 1.00 78.82 ATOM 1724 N PHE B 390 -10.623 24.480 22.196 1.00 42.39 ATOM 1725 CA PHE B 390 -11.168 24.671 20.867 1.00 37.86 ATOM 1726 C PHE B 390 -10.077 24.097 20.005 1.00 35.55 ATOM 1727 O PHE B 390 -9.071 24.745 19.709 1.00 33.73 ATOM 1728 CB PHE B 390 -11.398 26.153 20.628 1.00 38.33 ATOM 1729 CG PHE B 390 -12.185 26.798 21.718 1.00 38.16 ATOM 1730 CD1 PHE B 390 -11.562 27.609 22.663 1.00 39.63 ATOM 1731 CD2 PHE B 390 -13.540 26.512 21.871 1.00 37.93 ATOM 1732 CE1 PHE B 390 -12.279 28.124 23.737 1.00 40.74 ATOM 1733 CE2 PHE B 390 -14.260 27.018 22.938 1.00 37.80 ATOM 1734 CZ PHE B 390 -13.627 27.823 23.877 1.00 39.63 ATOM 1735 N ASN B 392 -10.283 22.835 19.649 1.00 38.22 ATOM 1736 CA ASN B 392 -9.326 22.065 18.880 1.00 36.90 ATOM 1737 C ASN B 392 -9.606 22.024 17.399 1.00 36.24 ATOM 1738 O ASN B 392 -10.572 21.399 16.953 1.00 34.54 ATOM 1739 CB ASN B 392 -9.274 20.653 19.451 1.00 37.53 ATOM 1740 CG ASN B 392 -8.321 19.754 18.700 1.00 39.17 ATOM 1741 OD1 ASN B 392 -7.508 20.221 17.899 1.00 38.55 ATOM 1742 ND2 ASN B 392 -8.402 18.455 18.966 1.00 38.22 ATOM 1743 N PHE B 393 -8.743 22.684 16.632 1.00 33.57 ATOM 1744 CA PHE B 393 -8.869 22.702 15.189 1.00 32.86 ATOM 1745 C PHE B 393 -7.577 22.200 14.560 1.00 34.02 ATOM 1746 O PHE B 393 -7.227 22.583 13.445 1.00 37.17 ATOM 1747 CB PHE B 393 -9.220 24.105 14.708 1.00 30.99 ATOM 1748 CG PHE B 393 -10.603 24.538 15.104 1.00 31.11 ATOM 1749 CD1 PHE B 393 -11.717 24.108 14.382 1.00 30.39 ATOM 1750 CD2 PHE B 393 -10.804 25.343 16.220 1.00 29.56 ATOM 1751 CE1 PHE B 393 -13.015 24.474 14.763 1.00 28.88 ATOM 1752 CE2 PHE B 393 -12.097 25.715 16.622 1.00 30.94 ATOM 1753 CZ PHE B 393 -13.203 25.277 15.887 1.00 28.96 ATOM 1754 N LEU B 394 -6.873 21.344 15.291 1.00 34.10 ATOM 1755 CA LEU B 394 -5.640 20.749 14.796 1.00 35.11 ATOM 1756 C LEU B 394 -6.090 19.677 13.809 1.00 36.97 ATOM 1757 O LEU B 394 -7.186 19.124 13.948 1.00 36.32 ATOM 1758 CB LEU B 394 -4.838 20.105 15.935 1.00 30.10 ATOM 1759 CG LEU B 394 -4.299 21.008 17.051 1.00 29.66 ATOM 1760 CD1 LEU B 394 -3.479 20.167 18.022 1.00 29.73 ATOM 1761 CD2 LEU B 394 -3.443 22.127 16.476 1.00 28.96 ATOM 1762 N ARG B 395 -5.262 19.382 12.816 1.00 40.21 ATOM 1763 CA ARG B 395 -5.611 18.384 11.811 1.00 41.91 ATOM 1764 C ARG B 395 -4.878 17.076 12.052 1.00 40.68 ATOM 1765 O ARG B 395 -5.206 16.048 11.448 1.00 42.43 ATOM 1766 CB ARG B 395 -5.283 18.917 10.410 1.00 51.73 ATOM 1767 CG ARG B 395 -6.048 20.176 10.018 1.00 57.19 ATOM 1768 CD ARG B 395 -5.486 20.777 8.735 1.00 62.79 ATOM 1769 NE ARG B 395 -4.635 19.826 8.015 1.00 66.38 ATOM 1770 CZ ARG B 395 -3.306 19.790 8.091 1.00 66.78 ATOM 1771 NH1 ARG B 395 -2.629 18.878 7.403 1.00 67.30 ATOM 1772 NH2 ARG B 395 -2.644 20.685 8.818 1.00 64.93 ATOM 1773 N LYS B 396 -3.888 17.120 12.930 1.00 34.66 ATOM 1774 CA LYS B 396 -3.084 15.946 13.258 1.00 34.82 ATOM 1775 C LYS B 396 -2.810 15.921 14.755 1.00 34.04 ATOM 1776 O LYS B 396 -3.075 16.894 15.457 1.00 31.92 ATOM 1777 CB LYS B 396 -1.752 15.997 12.493 1.00 43.22 ATOM 1778 CG LYS B 396 -1.882 16.089 10.983 1.00 46.12 ATOM 1779 CD LYS B 396 -0.525 16.329 10.336 1.00 48.48 ATOM 1780 CE LYS B 396 -0.638 16.497 8.829 1.00 48.78 ATOM 1781 NZ LYS B 396 0.615 16.981 8.227 1.00 51.55 ATOM 1782 N LYS B 397 -2.276 14.808 15.243 1.00 40.56 ATOM 1783 CA LYS B 397 -1.954 14.703 16.656 1.00 42.64 ATOM 1784 C LYS B 397 -0.662 15.463 16.920 1.00 42.15 ATOM 1785 O LYS B 397 0.216 15.501 16.074 1.00 42.43 ATOM 1786 CB LYS B 397 -1.804 13.240 17.071 1.00 61.72 ATOM 1787 CG LYS B 397 -3.117 12.483 17.140 1.00 68.04 ATOM 1788 CD LYS B 397 -2.937 11.152 17.849 1.00 74.50 ATOM 1789 CE LYS B 397 -4.274 10.475 18.111 1.00 78.46 ATOM 1790 NZ LYS B 397 -4.114 9.207 18.893 1.00 80.35 ATOM 1791 N LEU B 398 -0.580 16.084 18.084 1.00 39.12 ATOM 1792 CA LEU B 398 0.582 16.850 18.434 1.00 38.98 ATOM 1793 C LEU B 398 1.360 16.237 19.583 1.00 39.05 ATOM 1794 O LEU B 398 0.903 16.217 20.724 1.00 39.83 ATOM 1795 CB LEU B 398 0.193 18.299 18.759 1.00 38.69 ATOM 1796 CG LEU B 398 1.223 19.241 19.361 1.00 39.70 ATOM 1797 CD1 LEU B 398 2.531 19.156 18.631 1.00 41.18 ATOM 1798 CD2 LEU B 398 0.685 20.652 19.302 1.00 39.64 ATOM 1799 N PHE B 399 2.528 15.713 19.270 1.00 40.84 ATOM 1800 CA PHE B 399 3.406 15.126 20.267 1.00 41.25 ATOM 1801 C PHE B 399 4.547 16.110 20.399 1.00 42.24 ATOM 1802 O PHE B 399 5.210 16.400 19.417 1.00 44.15 ATOM 1803 CB PHE B 399 3.938 13.783 19.789 1.00 36.87 ATOM 1804 CG PHE B 399 2.908 12.700 19.747 1.00 34.76 ATOM 1805 CD1 PHE B 399 2.628 11.946 20.879 1.00 33.72 ATOM 1806 CD2 PHE B 399 2.206 12.447 18.580 1.00 33.33 ATOM 1807 CE1 PHE B 399 1.670 10.944 20.846 1.00 33.44 ATOM 1808 CE2 PHE B 399 1.235 11.449 18.537 1.00 33.27 ATOM 1809 CZ PHE B 399 0.970 10.691 19.668 1.00 33.86 ATOM 1810 N PHE B 400 4.753 16.626 21.601 1.00 39.74 ATOM 1811 CA PHE B 400 5.824 17.579 21.820 1.00 42.13 ATOM 1812 C PHE B 400 7.189 16.917 21.714 1.00 45.46 ATOM 1813 O PHE B 400 7.314 15.695 21.806 1.00 45.57 ATOM 1814 CB PHE B 400 5.675 18.226 23.199 1.00 36.66 ATOM 1815 CG PHE B 400 4.563 19.227 23.287 1.00 33.60 ATOM 1816 CD1 PHE B 400 4.693 20.495 22.727 1.00 32.61 ATOM 1817 CD2 PHE B 400 3.372 18.900 23.926 1.00 31.17 ATOM 1818 CE1 PHE B 400 3.665 21.435 22.806 1.00 30.11 ATOM 1819 CE2 PHE B 400 2.338 19.827 24.021 1.00 31.18 ATOM 1820 CZ PHE B 400 2.485 21.099 23.458 1.00 31.03 ATOM 1821 N LYS B 401 8.217 17.728 21.504 1.00 48.01 ATOM 1822 CA LYS B 401 9.583 17.214 21.421 1.00 53.52 ATOM 1823 C LYS B 401 10.115 17.307 22.847 1.00 56.13 ATOM 1824 O LYS B 401 10.453 18.393 23.318 1.00 55.08 ATOM 1825 CB LYS B 401 10.431 18.081 20.493 1.00 78.67 ATOM 1826 CG LYS B 401 11.915 17.739 20.514 1.00 82.76 ATOM 1827 CD LYS B 401 12.249 16.535 19.664 1.00 86.29 ATOM 1828 CE LYS B 401 12.623 16.960 18.256 1.00 86.83 ATOM 1829 NZ LYS B 401 13.770 17.914 18.285 1.00 86.75 ATOM 1830 N THR B 402 10.177 16.165 23.529 1.00 65.25 ATOM 1831 CA THR B 402 10.652 16.138 24.909 1.00 70.48 ATOM 1832 C THR B 402 12.173 16.108 25.042 1.00 74.46 ATOM 1833 O THR B 402 12.880 15.557 24.195 1.00 72.75 ATOM 1834 CB THR B 402 10.041 14.935 25.674 1.00 70.58 ATOM 1835 OG1 THR B 402 10.024 13.777 24.827 1.00 72.43 ATOM 1836 CG2 THR B 402 8.616 15.257 26.106 1.00 72.22 ATOM 1837 N SER B 403 12.657 16.723 26.118 1.00 99.46 ATOM 1838 CA SER B 403 14.084 16.823 26.432 1.00104.43 ATOM 1839 C SER B 403 14.931 15.677 25.881 1.00109.16 ATOM 1840 O SER B 403 15.935 15.965 25.187 1.00110.74 ATOM 1841 CB SER B 403 14.285 16.922 27.949 1.00102.41 ATOM 1842 OG SER B 403 13.741 15.798 28.617 1.00104.10 ATOM 1843 OXT SER B 403 14.590 14.500 26.148 1.00107.18 TER ATOM 1844 N LEU I 256 -28.650 35.920 21.788 1.00 63.77 ATOM 1845 CA LEU I 256 -29.719 35.987 20.751 1.00 63.95 ATOM 1846 C LEU I 256 -29.273 35.298 19.461 1.00 60.91 ATOM 1847 O LEU I 256 -28.148 35.494 18.999 1.00 61.28 ATOM 1848 CB LEU I 256 -30.082 37.446 20.453 1.00 84.50 ATOM 1849 CG LEU I 256 -30.737 38.245 21.578 1.00 86.29 ATOM 1850 CD1 LEU I 256 -30.884 39.696 21.153 1.00 87.03 ATOM 1851 CD2 LEU I 256 -32.086 37.642 21.933 1.00 86.94 ATOM 1852 N PRO I 257 -30.157 34.488 18.874 1.00 49.38 ATOM 1853 CA PRO I 257 -29.871 33.758 17.628 1.00 48.16 ATOM 1854 C PRO I 257 -29.752 34.667 16.406 1.00 47.64 ATOM 1855 O PRO I 257 -30.389 35.716 16.342 1.00 48.15 ATOM 1856 CB PRO I 257 -31.048 32.790 17.521 1.00 50.53 ATOM 1857 CG PRO I 257 -32.164 33.570 18.131 1.00 50.28 ATOM 1858 CD PRO I 257 -31.516 34.166 19.359 1.00 50.98 ATOM 1859 N ARG I 258 -28.929 34.266 15.452 1.00 56.56 ATOM 1860 CA ARG I 258 -28.759 35.062 14.245 1.00 56.68 ATOM 1861 C ARG I 258 -29.995 34.947 13.366 1.00 55.48 ATOM 1862 O ARG I 258 -30.225 35.785 12.500 1.00 56.23 ATOM 1863 CB ARG I 258 -27.527 34.614 13.469 1.00 69.98 ATOM 1864 CG ARG I 258 -26.206 34.908 14.172 1.00 73.74 ATOM 1865 CD ARG I 258 -25.030 34.690 13.235 1.00 76.61 ATOM 1866 NE ARG I 258 -25.020 35.642 12.126 1.00 80.22 ATOM 1867 CZ ARG I 258 -24.169 35.599 11.103 1.00 81.60 ATOM 1868 NH1 ARG I 258 -23.247 34.644 11.040 1.00 82.26 ATOM 1869 NH2 ARG I 258 -24.230 36.512 10.144 1.00 81.99 ATOM 1870 N ASN I 259 -30.796 33.913 13.594 1.00 56.43 ATOM 1871 CA ASN I 259 -32.005 33.711 12.805 1.00 54.29 ATOM 1872 C ASN I 259 -33.181 33.293 13.684 1.00 54.53 ATOM 1873 O ASN I 259 -33.547 32.121 13.734 1.00 53.99 ATOM 1874 CB ASN I 259 -31.768 32.641 11.742 1.00 44.83 ATOM 1875 CG ASN I 259 -32.864 32.609 10.708 1.00 43.43 ATOM 1876 OD1 ASN I 259 -34.024 32.904 11.008 1.00 41.15 ATOM 1877 ND2 ASN I 259 -32.515 32.235 9.481 1.00 39.84 ATOM 1878 N PRO I 260 -33.801 34.253 14.385 1.00 60.29 ATOM 1879 CA PRO I 260 -34.931 33.993 15.274 1.00 60.63 ATOM 1880 C PRO I 260 -36.097 33.226 14.649 1.00 60.27 ATOM 1881 O PRO I 260 -36.814 32.504 15.340 1.00 60.56 ATOM 1882 CB PRO I 260 -35.352 35.390 15.714 1.00 54.80 ATOM 1883 CG PRO I 260 -34.060 36.143 15.701 1.00 55.26 ATOM 1884 CD PRO I 260 -33.447 35.680 14.398 1.00 54.86 ATOM 1885 N SER I 261 -36.272 33.370 13.340 1.00 54.22 ATOM 1886 CA SER I 261 -37.371 32.699 12.651 1.00 54.04 ATOM 1887 C SER I 261 -37.187 31.193 12.560 1.00 54.01 ATOM 1888 O SER I 261 -38.138 30.466 12.266 1.00 54.24 ATOM 1889 CB SER I 261 -37.541 33.277 11.242 1.00 57.64 ATOM 1890 OG SER I 261 -36.481 32.894 10.392 1.00 58.48 ATOM 1891 N MET I 262 -35.968 30.727 12.815 1.00 52.20 ATOM 1892 CA MET I 262 -35.649 29.307 12.749 1.00 50.81 ATOM 1893 C MET I 262 -35.351 28.733 14.135 1.00 49.82 ATOM 1894 O MET I 262 -34.751 27.658 14.258 1.00 49.59 ATOM 1895 CB MET I 262 -34.454 29.089 11.823 1.00 52.60 ATOM 1896 CG MET I 262 -34.727 29.477 10.385 1.00 53.44 ATOM 1897 SD MET I 262 -35.924 28.358 9.634 1.00 57.49 ATOM 1898 CE MET I 262 -35.096 27.953 8.153 1.00 59.13 ATOM 1899 N ALA I 263 -35.775 29.438 15.174 1.00 47.68 ATOM 1900 CA ALA I 263 -35.544 28.998 16.540 1.00 47.82 ATOM 1901 C ALA I 263 -36.358 27.751 16.882 1.00 48.16 ATOM 1902 O ALA I 263 -36.002 26.999 17.791 1.00 48.06 ATOM 1903 CB ALA I 263 -35.887 30.119 17.513 1.00 44.04 ATOM 1904 N ASP I 264 -37.439 27.520 16.140 1.00 49.80 ATOM 1905 CA ASP I 264 -38.290 26.359 16.394 1.00 49.74 ATOM 1906 C ASP I 264 -38.038 25.218 15.419 1.00 47.22 ATOM 1907 O ASP I 264 -37.992 25.404 14.206 1.00 48.21 ATOM 1908 CB ASP I 264 -39.767 26.773 16.351 1.00 61.94 ATOM 1909 CG ASP I 264 -40.703 25.640 16.744 1.00 64.26 ATOM 1910 OD1 ASP I 264 -40.938 24.725 15.922 1.00 63.42 ATOM 1911 OD2 ASP I 264 -41.196 25.652 17.891 1.00 68.67 ATOM 1912 N TYR I 265 -37.878 24.016 15.974 1.00 38.80 ATOM 1913 CA TYR I 265 -37.635 22.810 15.186 1.00 37.89 ATOM 1914 C TYR I 265 -38.553 22.690 13.970 1.00 38.41 ATOM 1915 O TYR I 265 -38.108 22.345 12.879 1.00 37.25 ATOM 1916 CB TYR I 265 -37.824 21.575 16.072 1.00 39.90 ATOM 1917 CG TYR I 265 -37.821 20.282 15.286 1.00 37.98 ATOM 1918 CD1 TYR I 265 -36.622 19.675 14.911 1.00 37.03 ATOM 1919 CD2 TYR I 265 -39.018 19.694 14.868 1.00 37.75 ATOM 1920 CE1 TYR I 265 -36.609 18.523 14.140 1.00 36.37 ATOM 1921 CE2 TYR I 265 -39.015 18.541 14.091 1.00 35.78 ATOM 1922 CZ TYR I 265 -37.805 17.961 13.721 1.00 36.36 ATOM 1923 OH TYR I 265 -37.781 16.837 12.939 1.00 37.74 ATOM 1924 N GLU I 266 -39.844 22.949 14.171 1.00 46.16 ATOM 1925 CA GLU I 266 -40.828 22.853 13.099 1.00 48.46 ATOM 1926 C GLU I 266 -40.516 23.736 11.898 1.00 47.54 ATOM 1927 O GLU I 266 -40.713 23.322 10.754 1.00 47.19 ATOM 1928 CB GLU I 266 -42.223 23.182 13.628 1.00 62.51 ATOM 1929 CG GLU I 266 -42.830 22.078 14.471 1.00 67.51 ATOM 1930 CD GLU I 266 -42.818 20.739 13.754 1.00 71.51 ATOM 1931 OE1 GLU I 266 -43.298 20.673 12.595 1.00 72.76 ATOM 1932 OE2 GLU I 266 -42.344 19.748 14.354 1.00 72.12 ATOM 1933 N ALA I 267 -40.040 24.946 12.156 1.00 49.22 ATOM 1934 CA ALA I 267 -39.697 25.859 11.077 1.00 47.92 ATOM 1935 C ALA I 267 -38.470 25.345 10.326 1.00 47.59 ATOM 1936 O ALA I 267 -38.385 25.464 9.107 1.00 48.01 ATOM 1937 CB ALA I 267 -39.420 27.250 11.633 1.00 50.01 ATOM 1938 N ARG I 268 -37.541 24.751 11.066 1.00 40.35 ATOM 1939 CA ARG I 268 -36.317 24.231 10.464 1.00 39.71 ATOM 1940 C ARG I 268 -36.524 22.989 9.603 1.00 39.33 ATOM 1941 O ARG I 268 -36.017 22.919 8.482 1.00 38.35 ATOM 1942 CB ARG I 268 -35.274 23.920 11.550 1.00 39.61 ATOM 1943 CG ARG I 268 -34.844 25.119 12.393 1.00 38.53 ATOM 1944 CD ARG I 268 -33.533 24.842 13.133 1.00 38.83 ATOM 1945 NE ARG I 268 -33.639 23.809 14.159 1.00 35.49 ATOM 1946 CZ ARG I 268 -34.125 24.004 15.380 1.00 36.18 ATOM 1947 NH1 ARG I 268 -34.567 25.199 15.758 1.00 35.43 ATOM 1948 NH2 ARG I 268 -34.162 22.999 16.253 1.00 37.81 ATOM 1949 N ILE I 269 -37.258 22.004 10.113 1.00 40.69 ATOM 1950 CA ILE I 269 -37.476 20.782 9.351 1.00 41.92 ATOM 1951 C ILE I 269 -38.228 21.095 8.057 1.00 43.77 ATOM 1952 O ILE I 269 -38.066 20.408 7.058 1.00 42.63 ATOM 1953 CB ILE I 269 -38.278 19.720 10.169 1.00 41.07 ATOM 1954 CG1 ILE I 269 -38.352 18.405 9.395 1.00 38.05 ATOM 1955 CG2 ILE I 269 -39.697 20.217 10.445 1.00 40.12 ATOM 1956 CD1 ILE I 269 -37.017 17.762 9.148 1.00 35.60 ATOM 1957 N PHE I 270 -39.029 22.155 8.087 1.00 48.58 ATOM 1958 CA PHE I 270 -39.796 22.562 6.924 1.00 51.77 ATOM 1959 C PHE I 270 -38.898 22.829 5.729 1.00 51.75 ATOM 1960 O PHE I 270 -39.216 22.422 4.627 1.00 52.64 ATOM 1961 CB PHE I 270 -40.597 23.828 7.235 1.00 67.02 ATOM 1962 CG PHE I 270 -41.529 24.251 6.145 1.00 72.00 ATOM 1963 CD1 PHE I 270 -42.642 23.488 5.836 1.00 74.81 ATOM 1964 CD2 PHE I 270 -41.299 25.432 5.438 1.00 74.04 ATOM 1965 CE1 PHE I 270 -43.516 23.879 4.826 1.00 75.77 ATOM 1966 CE2 PHE I 270 -42.165 25.835 4.437 1.00 76.24 ATOM 1967 CZ PHE I 270 -43.279 25.059 4.128 1.00 76.43 ATOM 1968 N THR I 271 -37.768 23.491 5.948 1.00 45.87 ATOM 1969 CA THR I 271 -36.828 23.820 4.881 1.00 44.54 ATOM 1970 C THR I 271 -36.169 22.614 4.229 1.00 45.77 ATOM 1971 O THR I 271 -35.493 22.758 3.214 1.00 45.11 ATOM 1972 CB THR I 271 -35.695 24.743 5.359 1.00 47.56 ATOM 1973 OG1 THR I 271 -34.878 24.037 6.290 1.00 46.50 ATOM 1974 CG2 THR I 271 -36.273 25.975 6.003 1.00 45.34 ATOM 1975 N PHE I 272 -36.346 21.428 4.803 1.00 54.81 ATOM 1976 CA PHE I 272 -35.740 20.233 4.220 1.00 56.99 ATOM 1977 C PHE I 272 -36.754 19.498 3.358 1.00 60.56 ATOM 1978 O PHE I 272 -36.621 18.290 3.143 1.00 61.33 ATOM 1979 CB PHE I 272 -35.231 19.277 5.305 1.00 48.57 ATOM 1980 CG PHE I 272 -34.087 19.809 6.105 1.00 46.60 ATOM 1981 CD1 PHE I 272 -34.319 20.593 7.215 1.00 44.66 ATOM 1982 CD2 PHE I 272 -32.771 19.496 5.769 1.00 45.13 ATOM 1983 CE1 PHE I 272 -33.245 21.058 8.000 1.00 43.62 ATOM 1984 CE2 PHE I 272 -31.700 19.956 6.522 1.00 43.47 ATOM 1985 CZ PHE I 272 -31.948 20.736 7.648 1.00 42.07 ATOM 1986 N GLY I 273 -37.762 20.220 2.876 1.00 67.77 ATOM 1987 CA GLY I 273 -38.789 19.619 2.038 1.00 72.67 ATOM 1988 C GLY I 273 -38.282 18.443 1.242 1.00 76.00 ATOM 1989 O GLY I 273 -38.449 17.285 1.646 1.00 76.55 ATOM 1990 N THR I 274 -37.661 18.721 0.112 1.00 90.42 ATOM 1991 CA THR I 274 -37.116 17.665 -0.715 1.00 92.28 ATOM 1992 C THR I 274 -35.634 17.525 -0.393 1.00 92.21 ATOM 1993 O THR I 274 -34.790 18.158 -1.029 1.00 94.83 ATOM 1994 CB THR I 274 -37.283 17.986 -2.208 1.00 87.55 ATOM 1995 OG1 THR I 274 -38.671 18.239 -2.487 1.00 89.12 ATOM 1996 CG2 THR I 274 -36.815 16.808 -3.054 1.00 87.65 ATOM 1997 N TRP I 275 -35.330 16.709 0.589 1.00 72.48 ATOM 1998 CA TRP I 275 -33.950 16.479 1.001 1.00 68.85 ATOM 1999 C TRP I 275 -33.508 15.135 0.439 1.00 68.22 ATOM 2000 O TRP I 275 -34.011 14.090 0.850 1.00 68.60 ATOM 2001 CB TRP I 275 -33.866 16.486 2.530 1.00 56.97 ATOM 2002 CG TRP I 275 -32.467 16.462 3.057 1.00 52.79 ATOM 2003 CD1 TRP I 275 -31.817 15.399 3.606 1.00 52.05 ATOM 2004 CD2 TRP I 275 -31.540 17.551 3.064 1.00 51.41 ATOM 2005 NE1 TRP I 275 -30.539 15.763 3.968 1.00 50.50 ATOM 2006 CE2 TRP I 275 -30.343 17.078 3.637 1.00 50.80 ATOM 2007 CE3 TRP I 275 -31.607 18.886 2.638 1.00 51.13 ATOM 2008 CZ2 TRP I 275 -29.214 17.888 3.799 1.00 49.66 ATOM 2009 CZ3 TRP I 275 -30.478 19.697 2.801 1.00 50.10 ATOM 2010 CH2 TRP I 275 -29.305 19.192 3.373 1.00 48.56 ATOM 2011 N ILE I 276 -32.564 15.159 -0.477 1.00 65.94 ATOM 2012 CA ILE I 276 -32.096 13.935 -1.111 1.00 66.28 ATOM 2013 C ILE I 276 -30.783 13.369 -0.589 1.00 65.63 ATOM 2014 O ILE I 276 -30.283 12.374 -1.123 1.00 65.32 ATOM 2015 CB ILE I 276 -31.978 14.132 -2.640 1.00 78.50 ATOM 2016 CG1 ILE I 276 -31.015 15.273 -2.965 1.00 79.60 ATOM 2017 CG2 ILE I 276 -33.348 14.449 -3.224 1.00 79.81 ATOM 2018 CD1 ILE I 276 -29.548 14.896 -2.882 1.00 79.62 ATOM 2019 N TYR I 277 -30.229 13.970 0.448 1.00 64.67 ATOM 2020 CA TYR I 277 -28.957 13.500 0.993 1.00 63.20 ATOM 2021 C TYR I 277 -29.113 12.430 2.059 1.00 62.65 ATOM 2022 O TYR I 277 -30.181 12.281 2.647 1.00 62.81 ATOM 2023 CB TYR I 277 -28.157 14.697 1.527 1.00 61.59 ATOM 2024 CG TYR I 277 -28.039 15.778 0.481 1.00 60.11 ATOM 2025 CD1 TYR I 277 -28.988 16.792 0.395 1.00 59.13 ATOM 2026 CD2 TYR I 277 -27.023 15.735 -0.457 1.00 59.73 ATOM 2027 CE1 TYR I 277 -28.937 17.734 -0.611 1.00 58.94 ATOM 2028 CE2 TYR I 277 -26.969 16.670 -1.486 1.00 58.75 ATOM 2029 CZ TYR I 277 -27.926 17.670 -1.556 1.00 59.43 ATOM 2030 OH TYR I 277 -27.881 18.583 -2.582 1.00 60.64 ATOM 2031 N SER I 278 -28.040 11.682 2.298 1.00 69.60 ATOM 2032 CA SER I 278 -28.054 10.605 3.280 1.00 69.19 ATOM 2033 C SER I 278 -28.179 11.087 4.717 1.00 67.47 ATOM 2034 O SER I 278 -28.794 10.421 5.549 1.00 68.28 ATOM 2035 CB SER I 278 -26.797 9.735 3.132 1.00 74.64 ATOM 2036 OG SER I 278 -25.616 10.486 3.376 1.00 78.09 ATOM 2037 N VAL I 279 -27.594 12.250 5.015 1.00 50.60 ATOM 2038 CA VAL I 279 -27.668 12.804 6.363 1.00 48.20 ATOM 2039 C VAL I 279 -29.118 13.110 6.716 1.00 43.59 ATOM 2040 O VAL I 279 -29.768 13.947 6.082 1.00 41.34 ATOM 2041 CB VAL I 279 -26.830 14.092 6.463 1.00 71.13 ATOM 2042 CG1 VAL I 279 -26.903 14.649 7.855 1.00 73.37 ATOM 2043 CG2 VAL I 279 -25.404 13.791 6.104 1.00 74.77 ATOM 2044 N ASN I 280 -29.616 12.416 7.725 1.00 46.48 ATOM 2045 CA ASN I 280 -30.991 12.567 8.161 1.00 44.98 ATOM 2046 C ASN I 280 -31.381 14.019 8.433 1.00 44.96 ATOM 2047 O ASN I 280 -30.723 14.714 9.204 1.00 44.47 ATOM 2048 CB ASN I 280 -31.241 11.709 9.391 1.00 44.51 ATOM 2049 CG ASN I 280 -32.687 11.744 9.837 1.00 44.21 ATOM 2050 OD1 ASN I 280 -33.035 12.454 10.779 1.00 41.74 ATOM 2051 ND2 ASN I 280 -33.525 10.992 9.153 1.00 44.17 ATOM 2052 N LYS I 281 -32.454 14.459 7.803 1.00 48.36 ATOM 2053 CA LYS I 281 -32.929 15.824 7.952 1.00 48.20 ATOM 2054 C LYS I 281 -33.522 16.103 9.322 1.00 47.09 ATOM 2055 O LYS I 281 -33.457 17.231 9.814 1.00 46.77 ATOM 2056 CB LYS I 281 -33.951 16.146 6.868 1.00 50.95 ATOM 2057 CG LYS I 281 -35.089 15.155 6.759 1.00 53.06 ATOM 2058 CD LYS I 281 -36.113 15.654 5.758 1.00 55.30 ATOM 2059 CE LYS I 281 -37.336 14.762 5.699 1.00 56.17 ATOM 2060 NZ LYS I 281 -38.394 15.365 4.844 1.00 58.04 ATOM 2061 N GLU I 282 -34.105 15.087 9.953 1.00 40.89 ATOM 2062 CA GLU I 282 -34.671 15.263 11.282 1.00 40.05 ATOM 2063 C GLU I 282 -33.550 15.554 12.275 1.00 37.46 ATOM 2064 O GLU I 282 -33.660 16.461 13.109 1.00 36.30 ATOM 2065 CB GLU I 282 -35.449 14.020 11.723 1.00 50.51 ATOM 2066 CG GLU I 282 -36.836 13.875 11.116 1.00 52.65 ATOM 2067 CD GLU I 282 -36.815 13.529 9.637 1.00 54.35 ATOM 2068 OE1 GLU I 282 -36.031 12.638 9.244 1.00 54.87 ATOM 2069 OE2 GLU I 282 -37.596 14.141 8.882 1.00 55.21 ATOM 2070 N GLN I 283 -32.460 14.792 12.178 1.00 35.16 ATOM 2071 CA GLN I 283 -31.314 14.993 13.062 1.00 35.51 ATOM 2072 C GLN I 283 -30.750 16.395 12.852 1.00 32.55 ATOM 2073 O GLN I 283 -30.488 17.115 13.824 1.00 29.73 ATOM 2074 CB GLN I 283 -30.204 13.974 12.764 1.00 53.98 ATOM 2075 CG GLN I 283 -30.537 12.559 13.133 1.00 60.08 ATOM 2076 CD GLN I 283 -29.325 11.653 13.045 1.00 64.96 ATOM 2077 OE1 GLN I 283 -28.694 11.529 11.987 1.00 65.94 ATOM 2078 NE2 GLN I 283 -28.981 11.011 14.156 1.00 68.73 ATOM 2079 N LEU I 284 -30.587 16.782 11.594 1.00 31.15 ATOM 2080 CA LEU I 284 -30.058 18.095 11.270 1.00 30.53 ATOM 2081 C LEU I 284 -30.886 19.186 11.924 1.00 30.73 ATOM 2082 O LEU I 284 -30.341 20.060 12.591 1.00 29.80 ATOM 2083 CB LEU I 284 -30.032 18.320 9.758 1.00 32.02 ATOM 2084 CG LEU I 284 -28.938 17.557 9.004 1.00 34.22 ATOM 2085 CD1 LEU I 284 -29.111 17.774 7.506 1.00 35.16 ATOM 2086 CD2 LEU I 284 -27.560 18.040 9.459 1.00 34.30 ATOM 2087 N ALA I 285 -32.203 19.117 11.744 1.00 30.89 ATOM 2088 CA ALA I 285 -33.093 20.114 12.323 1.00 31.76 ATOM 2089 C ALA I 285 -33.015 20.105 13.845 1.00 31.39 ATOM 2090 O ALA I 285 -33.022 21.161 14.473 1.00 30.01 ATOM 2091 CB ALA I 285 -34.531 19.870 11.863 1.00 37.08 ATOM 2092 N ARG I 286 -32.945 18.913 14.445 1.00 37.43 ATOM 2093 CA ARG I 286 -32.837 18.830 15.903 1.00 38.12 ATOM 2094 C ARG I 286 -31.542 19.490 16.369 1.00 37.09 ATOM 2095 O ARG I 286 -31.503 20.122 17.420 1.00 36.91 ATOM 2096 CB ARG I 286 -32.816 17.375 16.381 1.00 35.76 ATOM 2097 CG ARG I 286 -34.117 16.628 16.227 1.00 40.58 ATOM 2098 CD ARG I 286 -33.957 15.202 16.741 1.00 41.19 ATOM 2099 NE ARG I 286 -34.735 14.267 15.947 1.00 44.82 ATOM 2100 CZ ARG I 286 -34.221 13.222 15.313 1.00 44.68 ATOM 2101 NH1 ARG I 286 -32.926 12.975 15.382 1.00 47.03 ATOM 2102 NH2 ARG I 286 -35.003 12.426 14.608 1.00 48.97 ATOM 2103 N ALA I 287 -30.483 19.330 15.576 1.00 30.56 ATOM 2104 CA ALA I 287 -29.190 19.909 15.904 1.00 30.26 ATOM 2105 C ALA I 287 -29.137 21.420 15.636 1.00 30.77 ATOM 2106 O ALA I 287 -28.080 22.033 15.706 1.00 31.44 ATOM 2107 CB ALA I 287 -28.095 19.192 15.141 1.00 19.11 ATOM 2108 N GLY I 288 -30.292 22.008 15.314 1.00 28.53 ATOM 2109 CA GLY I 288 -30.371 23.442 15.082 1.00 28.00 ATOM 2110 C GLY I 288 -30.155 23.901 13.661 1.00 29.86 ATOM 2111 O GLY I 288 -30.159 25.102 13.379 1.00 31.17 ATOM 2112 N PHE I 289 -29.974 22.961 12.751 1.00 31.90 ATOM 2113 CA PHE I 289 -29.728 23.303 11.355 1.00 34.68 ATOM 2114 C PHE I 289 -30.988 23.428 10.517 1.00 36.37 ATOM 2115 O PHE I 289 -32.037 22.892 10.855 1.00 38.46 ATOM 2116 CB PHE I 289 -28.825 22.250 10.713 1.00 35.54 ATOM 2117 CG PHE I 289 -27.457 22.168 11.326 1.00 34.79 ATOM 2118 CD1 PHE I 289 -26.564 23.229 11.214 1.00 34.34 ATOM 2119 CD2 PHE I 289 -27.057 21.024 12.014 1.00 36.15 ATOM 2120 CE1 PHE I 289 -25.293 23.150 11.769 1.00 33.30 ATOM 2121 CE2 PHE I 289 -25.784 20.935 12.576 1.00 35.55 ATOM 2122 CZ PHE I 289 -24.896 22.006 12.455 1.00 35.46 ATOM 2123 N TYR I 290 -30.869 24.173 9.428 1.00 36.04 ATOM 2124 CA TYR I 290 -31.962 24.362 8.481 1.00 39.44 ATOM 2125 C TYR I 290 -31.300 24.459 7.110 1.00 39.92 ATOM 2126 O TYR I 290 -30.250 25.075 6.975 1.00 41.23 ATOM 2127 CB TYR I 290 -32.786 25.614 8.814 1.00 44.09 ATOM 2128 CG TYR I 290 -32.041 26.930 8.759 1.00 47.29 ATOM 2129 CD1 TYR I 290 -31.814 27.571 7.541 1.00 47.33 ATOM 2130 CD2 TYR I 290 -31.610 27.559 9.931 1.00 46.13 ATOM 2131 CE1 TYR I 290 -31.168 28.804 7.490 1.00 48.80 ATOM 2132 CE2 TYR I 290 -30.966 28.791 9.892 1.00 47.01 ATOM 2133 CZ TYR I 290 -30.742 29.414 8.672 1.00 49.80 ATOM 2134 OH TYR I 290 -30.102 30.634 8.623 1.00 49.36 ATOM 2135 N ALA I 291 -31.904 23.816 6.106 1.00 38.55 ATOM 2136 CA ALA I 291 -31.357 23.814 4.771 1.00 39.87 ATOM 2137 C ALA I 291 -31.463 25.182 4.121 1.00 42.19 ATOM 2138 O ALA I 291 -32.460 25.877 4.288 1.00 40.37 ATOM 2139 CB ALA I 291 -32.073 22.778 3.924 1.00 42.14 ATOM 2140 N LEU I 292 -30.427 25.547 3.367 1.00 59.68 ATOM 2141 CA LEU I 292 -30.382 26.840 2.686 1.00 63.93 ATOM 2142 C LEU I 292 -30.997 26.812 1.291 1.00 66.44 ATOM 2143 O LEU I 292 -31.286 27.860 0.721 1.00 66.85 ATOM 2144 CB LEU I 292 -28.935 27.332 2.594 1.00 58.81 ATOM 2145 CG LEU I 292 -28.233 27.584 3.916 1.00 60.68 ATOM 2146 CD1 LEU I 292 -26.814 28.054 3.651 1.00 61.04 ATOM 2147 CD2 LEU I 292 -28.997 28.629 4.707 1.00 60.14 ATOM 2148 N GLY I 293 -31.185 25.619 0.751 1.00 66.43 ATOM 2149 CA GLY I 293 -31.775 25.504 -0.556 1.00 67.84 ATOM 2150 C GLY I 293 -30.787 25.190 -1.656 1.00 68.98 ATOM 2151 O GLY I 293 -31.186 24.961 -2.801 1.00 70.31 ATOM 2152 N GLU I 294 -29.496 25.186 -1.331 1.00 57.28 ATOM 2153 CA GLU I 294 -28.479 24.876 -2.316 1.00 57.60 ATOM 2154 C GLU I 294 -27.558 23.789 -1.795 1.00 55.93 ATOM 2155 O GLU I 294 -26.860 23.976 -0.801 1.00 56.19 ATOM 2156 CB GLU I 294 -27.672 26.132 -2.670 1.00 78.27 ATOM 2157 CG GLU I 294 -27.064 26.857 -1.484 1.00 83.40 ATOM 2158 CD GLU I 294 -26.261 28.065 -1.902 1.00 86.79 ATOM 2159 OE1 GLU I 294 -25.299 27.896 -2.685 1.00 88.78 ATOM 2160 OE2 GLU I 294 -26.589 29.191 -1.458 1.00 87.46 ATOM 2161 N GLY I 295 -27.556 22.651 -2.479 1.00 58.98 ATOM 2162 CA GLY I 295 -26.731 21.535 -2.057 1.00 57.16 ATOM 2163 C GLY I 295 -27.163 21.085 -0.677 1.00 55.86 ATOM 2164 O GLY I 295 -28.264 21.412 -0.229 1.00 56.67 ATOM 2165 N ASP I 296 -26.309 20.333 0.000 1.00 53.03 ATOM 2166 CA ASP I 296 -26.618 19.855 1.324 1.00 51.24 ATOM 2167 C ASP I 296 -26.157 20.894 2.341 1.00 49.97 ATOM 2168 O ASP I 296 -25.750 20.550 3.456 1.00 50.02 ATOM 2169 CB ASP I 296 -25.911 18.520 1.581 1.00 50.41 ATOM 2170 CG ASP I 296 -24.403 18.659 1.653 1.00 50.01 ATOM 2171 OD1 ASP I 296 -23.884 19.731 1.285 1.00 48.84 ATOM 2172 OD2 ASP I 296 -23.734 17.693 2.084 1.00 49.81 ATOM 2173 N LYS I 297 -26.233 22.163 1.967 1.00 46.14 ATOM 2174 CA LYS I 297 -25.809 23.247 2.850 1.00 45.61 ATOM 2175 C LYS I 297 -26.853 23.609 3.884 1.00 43.89 ATOM 2176 O LYS I 297 -28.023 23.835 3.566 1.00 43.28 ATOM 2177 CB LYS I 297 -25.447 24.496 2.041 1.00 60.37 ATOM 2178 CG LYS I 297 -24.182 24.337 1.220 1.00 63.12 ATOM 2179 CD LYS I 297 -23.676 25.666 0.693 1.00 66.57 ATOM 2180 CE LYS I 297 -22.385 25.469 -0.070 1.00 67.82 ATOM 2181 NZ LYS I 297 -21.843 26.752 -0.592 1.00 69.33 ATOM 2182 N VAL I 298 -26.412 23.674 5.107 1.00 46.72 ATOM 2183 CA VAL I 298 -27.284 24.028 6.220 1.00 45.08 ATOM 2184 C VAL I 298 -26.573 25.013 7.146 1.00 44.49 ATOM 2185 O VAL I 298 -25.342 25.085 7.161 1.00 44.10 ATOM 2186 CB VAL I 298 -27.687 22.771 7.036 1.00 38.39 ATOM 2187 CG1 VAL I 298 -28.430 21.792 6.150 1.00 37.44 ATOM 2188 CG2 VAL I 298 -26.448 22.101 7.621 1.00 36.24 ATOM 2189 N LYS I 299 -27.359 25.768 7.901 1.00 43.01 ATOM 2190 CA LYS I 299 -26.811 26.728 8.851 1.00 42.26 ATOM 2191 C LYS I 299 -27.561 26.593 10.162 1.00 40.60 ATOM 2192 O LYS I 299 -28.717 26.172 10.190 1.00 38.11 ATOM 2193 CB LYS I 299 -26.972 28.162 8.326 1.00 57.34 ATOM 2194 CG LYS I 299 -26.288 28.404 6.998 1.00 62.67 ATOM 2195 CD LYS I 299 -26.372 29.855 6.575 1.00 64.44 ATOM 2196 CE LYS I 299 -25.538 30.741 7.468 1.00 63.74 ATOM 2197 NZ LYS I 299 -25.484 32.125 6.951 1.00 66.64 ATOM 2198 N CYS I 300 -26.886 26.934 11.251 1.00 45.06 ATOM 2199 CA CYS I 300 -27.499 26.883 12.565 1.00 43.71 ATOM 2200 C CYS I 300 -28.276 28.181 12.755 1.00 43.80 ATOM 2201 O CYS I 300 -27.767 29.258 12.465 1.00 45.36 ATOM 2202 CB CYS I 300 -26.440 26.749 13.644 1.00 38.40 ATOM 2203 SG CYS I 300 -27.095 26.921 15.304 1.00 34.70 ATOM 2204 N PHE I 301 -29.508 28.078 13.240 1.00 41.55 ATOM 2205 CA PHE I 301 -30.361 29.248 13.446 1.00 41.05 ATOM 2206 C PHE I 301 -29.798 30.185 14.517 1.00 42.48 ATOM 2207 O PHE I 301 -30.120 31.374 14.541 1.00 43.29 ATOM 2208 CB PHE I 301 -31.760 28.815 13.871 1.00 33.74 ATOM 2209 CG PHE I 301 -31.857 28.411 15.321 1.00 31.51 ATOM 2210 CD1 PHE I 301 -32.146 29.355 16.294 1.00 32.65 ATOM 2211 CD2 PHE I 301 -31.589 27.109 15.715 1.00 31.46 ATOM 2212 CE1 PHE I 301 -32.170 29.011 17.645 1.00 31.64 ATOM 2213 CE2 PHE I 301 -31.610 26.750 17.057 1.00 32.11 ATOM 2214 CZ PHE I 301 -31.900 27.704 18.028 1.00 32.93 ATOM 2215 N HIS I 302 -28.976 29.642 15.399 1.00 44.22 ATOM 2216 CA HIS I 302 -28.433 30.437 16.487 1.00 44.77 ATOM 2217 C HIS I 302 -27.040 31.035 16.248 1.00 43.38 ATOM 2218 O HIS I 302 -26.875 32.248 16.283 1.00 45.53 ATOM 2219 CB HIS I 302 -28.431 29.599 17.770 1.00 41.28 ATOM 2220 CG HIS I 302 -28.520 30.417 19.017 1.00 44.77 ATOM 2221 ND1 HIS I 302 -27.546 31.324 19.374 1.00 44.99 ATOM 2222 CD2 HIS I 302 -29.475 30.487 19.972 1.00 44.67 ATOM 2223 CE1 HIS I 302 -27.899 31.918 20.505 1.00 46.70 ATOM 2224 NE2 HIS I 302 -29.066 31.426 20.885 1.00 45.47 ATOM 2225 N CYS I 303 -26.046 30.183 16.013 1.00 39.76 ATOM 2226 CA CYS I 303 -24.686 30.673 15.801 1.00 40.44 ATOM 2227 C CYS I 303 -24.445 31.133 14.372 1.00 39.55 ATOM 2228 O CYS I 303 -23.559 31.937 14.122 1.00 40.71 ATOM 2229 CB CYS I 303 -23.663 29.598 16.174 1.00 39.68 ATOM 2230 SG CYS I 303 -23.566 28.202 15.031 1.00 39.58 ATOM 2231 N GLY I 304 -25.234 30.610 13.434 1.00 36.62 ATOM 2232 CA GLY I 304 -25.094 31.001 12.046 1.00 35.95 ATOM 2233 C GLY I 304 -24.081 30.161 11.295 1.00 37.83 ATOM 2234 O GLY I 304 -23.926 30.317 10.086 1.00 38.27 ATOM 2235 N GLY I 305 -23.393 29.275 12.004 1.00 40.21 ATOM 2236 CA GLY I 305 -22.406 28.429 11.354 1.00 40.31 ATOM 2237 C GLY I 305 -23.015 27.564 10.269 1.00 40.75 ATOM 2238 O GLY I 305 -24.098 26.999 10.449 1.00 40.85 ATOM 2239 N GLY I 306 -22.321 27.449 9.138 1.00 35.81 ATOM 2240 CA GLY I 306 -22.828 26.632 8.048 1.00 34.31 ATOM 2241 C GLY I 306 -21.969 25.408 7.816 1.00 35.71 ATOM 2242 O GLY I 306 -20.766 25.442 8.061 1.00 36.57 ATOM 2243 N LEU I 307 -22.594 24.312 7.373 1.00 37.33 ATOM 2244 CA LEU I 307 -21.878 23.073 7.091 1.00 40.07 ATOM 2245 C LEU I 307 -22.346 22.531 5.742 1.00 41.21 ATOM 2246 O LEU I 307 -23.514 22.674 5.386 1.00 41.08 ATOM 2247 CB LEU I 307 -22.133 22.007 8.171 1.00 43.63 ATOM 2248 CG LEU I 307 -21.516 22.103 9.576 1.00 43.99 ATOM 2249 CD1 LEU I 307 -20.043 22.472 9.470 1.00 42.27 ATOM 2250 CD2 LEU I 307 -22.254 23.126 10.381 1.00 45.71 ATOM 2251 N THR I 308 -21.435 21.901 5.001 1.00 42.99 ATOM 2252 CA THR I 308 -21.747 21.349 3.716 1.00 48.29 ATOM 2253 C THR I 308 -20.953 20.067 3.508 1.00 47.58 ATOM 2254 O THR I 308 -20.091 19.727 4.324 1.00 46.53 ATOM 2255 CB THR I 308 -21.359 22.326 2.588 1.00 72.90 ATOM 2256 OG1 THR I 308 -21.933 23.609 2.860 1.00 79.48 ATOM 2257 CG2 THR I 308 -21.881 21.841 1.252 1.00 75.12 ATOM 2258 N ASP I 309 -21.244 19.360 2.418 1.00 46.94 ATOM 2259 CA ASP I 309 -20.547 18.119 2.097 1.00 49.86 ATOM 2260 C ASP I 309 -20.587 17.143 3.259 1.00 48.09 ATOM 2261 O ASP I 309 -19.543 16.732 3.775 1.00 46.93 ATOM 2262 CB ASP I 309 -19.088 18.406 1.721 1.00 79.97 ATOM 2263 CG ASP I 309 -18.971 19.289 0.497 1.00 83.92 ATOM 2264 OD1 ASP I 309 -17.835 19.713 0.188 1.00 87.18 ATOM 2265 OD2 ASP I 309 -20.000 19.545 -0.145 1.00 85.80 ATOM 2266 N TRP I 310 -21.794 16.777 3.669 1.00 46.16 ATOM 2267 CA TRP I 310 -21.966 15.838 4.764 1.00 46.51 ATOM 2268 C TRP I 310 -21.641 14.410 4.329 1.00 49.37 ATOM 2269 O TRP I 310 -21.871 14.032 3.179 1.00 48.61 ATOM 2270 CB TRP I 310 -23.410 15.891 5.269 1.00 45.64 ATOM 2271 CG TRP I 310 -23.780 17.175 5.933 1.00 41.70 ATOM 2272 CD1 TRP I 310 -24.143 18.350 5.340 1.00 39.97 ATOM 2273 CD2 TRP I 310 -23.789 17.426 7.332 1.00 38.45 ATOM 2274 NE1 TRP I 310 -24.386 19.310 6.274 1.00 38.00 ATOM 2275 CE2 TRP I 310 -24.171 18.770 7.515 1.00 36.40 ATOM 2276 CE3 TRP I 310 -23.503 16.641 8.458 1.00 37.04 ATOM 2277 CZ2 TRP I 310 -24.277 19.355 8.784 1.00 36.98 ATOM 2278 CZ3 TRP I 310 -23.610 17.222 9.716 1.00 37.20 ATOM 2279 CH2 TRP I 310 -23.988 18.564 9.869 1.00 35.83 ATOM 2280 N LYS I 311 -21.096 13.620 5.240 1.00 55.51 ATOM 2281 CA LYS I 311 -20.748 12.235 4.944 1.00 61.69 ATOM 2282 C LYS I 311 -21.894 11.319 5.374 1.00 65.58 ATOM 2283 O LYS I 311 -22.734 11.697 6.190 1.00 64.50 ATOM 2284 CB LYS I 311 -19.462 11.839 5.663 1.00 79.38 ATOM 2285 CG LYS I 311 -18.250 12.680 5.296 1.00 82.21 ATOM 2286 CD LYS I 311 -17.949 12.603 3.816 1.00 84.24 ATOM 2287 CE LYS I 311 -16.729 13.443 3.464 1.00 85.67 ATOM 2288 NZ LYS I 311 -16.404 13.381 2.019 1.00 85.75 ATOM 2289 N PRO I 312 -21.939 10.098 4.825 1.00 95.05 ATOM 2290 CA PRO I 312 -22.976 9.112 5.136 1.00 98.32 ATOM 2291 C PRO I 312 -23.417 9.035 6.598 1.00 99.52 ATOM 2292 O PRO I 312 -24.464 9.571 6.963 1.00101.14 ATOM 2293 CB PRO I 312 -22.356 7.805 4.637 1.00 86.34 ATOM 2294 CG PRO I 312 -21.647 8.264 3.403 1.00 85.77 ATOM 2295 CD PRO I 312 -20.959 9.537 3.873 1.00 84.46 ATOM 2296 N SER I 313 -22.613 8.379 7.426 1.00 85.92 ATOM 2297 CA SER I 313 -22.934 8.225 8.837 1.00 83.77 ATOM 2298 C SER I 313 -22.270 9.294 9.686 1.00 80.58 ATOM 2299 O SER I 313 -21.501 8.990 10.601 1.00 81.38 ATOM 2300 CB SER I 313 -22.501 6.837 9.330 1.00 96.52 ATOM 2301 OG SER I 313 -23.195 5.819 8.645 1.00 99.94 ATOM 2302 N GLU I 314 -22.580 10.547 9.385 1.00 65.98 ATOM 2303 CA GLU I 314 -22.013 11.677 10.113 1.00 60.08 ATOM 2304 C GLU I 314 -23.092 12.281 11.018 1.00 56.44 ATOM 2305 O GLU I 314 -24.192 12.596 10.565 1.00 55.82 ATOM 2306 CB GLU I 314 -21.520 12.713 9.108 1.00 55.55 ATOM 2307 CG GLU I 314 -20.234 13.411 9.488 1.00 55.49 ATOM 2308 CD GLU I 314 -19.719 14.277 8.359 1.00 55.22 ATOM 2309 OE1 GLU I 314 -20.508 15.072 7.821 1.00 55.35 ATOM 2310 OE2 GLU I 314 -18.524 14.164 8.022 1.00 56.05 ATOM 2311 N ASP I 315 -22.764 12.431 12.296 1.00 50.51 ATOM 2312 CA ASP I 315 -23.698 12.984 13.274 1.00 46.41 ATOM 2313 C ASP I 315 -23.726 14.516 13.302 1.00 42.13 ATOM 2314 O ASP I 315 -22.715 15.161 13.557 1.00 41.25 ATOM 2315 CB ASP I 315 -23.338 12.452 14.668 1.00 53.05 ATOM 2316 CG ASP I 315 -24.206 13.036 15.762 1.00 54.37 ATOM 2317 OD1 ASP I 315 -23.893 12.781 16.943 1.00 57.20 ATOM 2318 OD2 ASP I 315 -25.187 13.740 15.462 1.00 57.36 ATOM 2319 N PRO I 316 -24.895 15.111 13.033 1.00 39.85 ATOM 2320 CA PRO I 316 -25.062 16.565 13.027 1.00 36.32 ATOM 2321 C PRO I 316 -24.599 17.262 14.314 1.00 36.11 ATOM 2322 O PRO I 316 -24.016 18.343 14.263 1.00 35.70 ATOM 2323 CB PRO I 316 -26.563 16.743 12.794 1.00 29.18 ATOM 2324 CG PRO I 316 -26.878 15.592 11.899 1.00 30.19 ATOM 2325 CD PRO I 316 -26.121 14.450 12.560 1.00 31.11 ATOM 2326 N TRP I 317 -24.863 16.657 15.464 1.00 37.22 ATOM 2327 CA TRP I 317 -24.446 17.269 16.718 1.00 36.71 ATOM 2328 C TRP I 317 -22.927 17.296 16.861 1.00 36.96 ATOM 2329 O TRP I 317 -22.367 18.305 17.282 1.00 37.93 ATOM 2330 CB TRP I 317 -25.053 16.531 17.912 1.00 34.48 ATOM 2331 CG TRP I 317 -26.377 17.074 18.344 1.00 35.89 ATOM 2332 CD1 TRP I 317 -27.546 16.367 18.519 1.00 34.84 ATOM 2333 CD2 TRP I 317 -26.682 18.429 18.702 1.00 35.59 ATOM 2334 NE1 TRP I 317 -28.537 17.203 18.965 1.00 35.80 ATOM 2335 CE2 TRP I 317 -28.042 18.472 19.090 1.00 35.20 ATOM 2336 CE3 TRP I 317 -25.930 19.615 18.744 1.00 35.13 ATOM 2337 CZ2 TRP I 317 -28.667 19.651 19.511 1.00 34.35 ATOM 2338 CZ3 TRP I 317 -26.550 20.791 19.160 1.00 35.56 ATOM 2339 CH2 TRP I 317 -27.910 20.794 19.535 1.00 35.52 ATOM 2340 N GLU I 318 -22.262 16.193 16.520 1.00 38.30 ATOM 2341 CA GLU I 318 -20.802 16.125 16.617 1.00 38.61 ATOM 2342 C GLU I 318 -20.181 17.167 15.702 1.00 36.56 ATOM 2343 O GLU I 318 -19.279 17.895 16.099 1.00 35.45 ATOM 2344 CB GLU I 318 -20.287 14.749 16.195 1.00 53.31 ATOM 2345 CG GLU I 318 -20.755 13.594 17.044 1.00 59.79 ATOM 2346 CD GLU I 318 -20.162 12.269 16.585 1.00 64.83 ATOM 2347 OE1 GLU I 318 -20.297 11.944 15.386 1.00 68.49 ATOM 2348 OE2 GLU I 318 -19.557 11.570 17.415 1.00 68.06 ATOM 2349 N GLN I 319 -20.660 17.220 14.465 1.00 32.91 ATOM 2350 CA GLN I 319 -20.156 18.173 13.492 1.00 32.96 ATOM 2351 C GLN I 319 -20.402 19.603 13.970 1.00 32.39 ATOM 2352 O GLN I 319 -19.562 20.485 13.791 1.00 33.11 ATOM 2353 CB GLN I 319 -20.831 17.953 12.140 1.00 36.30 ATOM 2354 CG GLN I 319 -20.441 16.641 11.464 1.00 38.74 ATOM 2355 CD GLN I 319 -18.937 16.463 11.397 1.00 41.52 ATOM 2356 OE1 GLN I 319 -18.221 17.348 10.925 1.00 43.63 ATOM 2357 NE2 GLN I 319 -18.451 15.322 11.867 1.00 42.04 ATOM 2358 N HIS I 320 -21.558 19.815 14.577 1.00 30.69 ATOM 2359 CA HIS I 320 -21.913 21.126 15.085 1.00 29.47 ATOM 2360 C HIS I 320 -20.972 21.557 16.207 1.00 30.95 ATOM 2361 O HIS I 320 -20.548 22.709 16.270 1.00 28.69 ATOM 2362 CB HIS I 320 -23.355 21.100 15.580 1.00 27.74 ATOM 2363 CG HIS I 320 -23.962 22.453 15.759 1.00 27.45 ATOM 2364 ND1 HIS I 320 -25.325 22.663 15.745 1.00 28.17 ATOM 2365 CD2 HIS I 320 -23.399 23.668 15.966 1.00 27.56 ATOM 2366 CE1 HIS I 320 -25.573 23.947 15.935 1.00 27.59 ATOM 2367 NE2 HIS I 320 -24.420 24.572 16.072 1.00 24.99 ATOM 2368 N ALA I 321 -20.640 20.617 17.096 1.00 33.83 ATOM 2369 CA ALA I 321 -19.756 20.910 18.214 1.00 35.63 ATOM 2370 C ALA I 321 -18.302 21.020 17.756 1.00 35.96 ATOM 2371 O ALA I 321 -17.542 21.847 18.262 1.00 36.66 ATOM 2372 CB ALA I 321 -19.890 19.832 19.279 1.00 33.93 ATOM 2373 N LYS I 322 -17.927 20.176 16.799 1.00 34.38 ATOM 2374 CA LYS I 322 -16.569 20.168 16.269 1.00 36.38 ATOM 2375 C LYS I 322 -16.191 21.500 15.617 1.00 36.78 ATOM 2376 O LYS I 322 -15.105 22.047 15.851 1.00 35.64 ATOM 2377 CB LYS I 322 -16.444 19.038 15.244 1.00 54.28 ATOM 2378 CG LYS I 322 -15.096 18.934 14.565 1.00 60.85 ATOM 2379 CD LYS I 322 -15.056 17.732 13.633 1.00 66.45 ATOM 2380 CE LYS I 322 -13.681 17.537 13.020 1.00 70.25 ATOM 2381 NZ LYS I 322 -13.260 18.709 12.220 1.00 70.69 ATOM 2382 N TRP I 323 -17.100 22.033 14.805 1.00 36.37 ATOM 2383 CA TRP I 323 -16.839 23.279 14.101 1.00 35.98 ATOM 2384 C TRP I 323 -17.286 24.558 14.789 1.00 35.24 ATOM 2385 O TRP I 323 -16.690 25.613 14.568 1.00 35.09 ATOM 2386 CB TRP I 323 -17.470 23.220 12.707 1.00 37.37 ATOM 2387 CG TRP I 323 -16.870 22.170 11.838 1.00 39.03 ATOM 2388 CD1 TRP I 323 -17.432 20.984 11.465 1.00 39.75 ATOM 2389 CD2 TRP I 323 -15.567 22.195 11.242 1.00 41.68 ATOM 2390 NE1 TRP I 323 -16.569 20.271 10.674 1.00 40.58 ATOM 2391 CE2 TRP I 323 -15.415 20.991 10.517 1.00 41.65 ATOM 2392 CE3 TRP I 323 -14.508 23.120 11.250 1.00 42.16 ATOM 2393 CZ2 TRP I 323 -14.248 20.685 9.806 1.00 43.06 ATOM 2394 CZ3 TRP I 323 -13.352 22.819 10.536 1.00 43.36 ATOM 2395 CH2 TRP I 323 -13.228 21.610 9.824 1.00 43.17 ATOM 2396 N TYR I 324 -18.330 24.481 15.607 1.00 33.97 ATOM 2397 CA TYR I 324 -18.821 25.678 16.281 1.00 33.04 ATOM 2398 C TYR I 324 -19.022 25.483 17.769 1.00 31.95 ATOM 2399 O TYR I 324 -20.126 25.650 18.287 1.00 34.20 ATOM 2400 CB TYR I 324 -20.112 26.140 15.617 1.00 33.86 ATOM 2401 CG TYR I 324 -19.962 26.259 14.122 1.00 36.04 ATOM 2402 CD1 TYR I 324 -20.449 25.262 13.272 1.00 37.17 ATOM 2403 CD2 TYR I 324 -19.287 27.336 13.552 1.00 37.45 ATOM 2404 CE1 TYR I 324 -20.265 25.338 11.891 1.00 38.24 ATOM 2405 CE2 TYR I 324 -19.094 27.431 12.175 1.00 37.18 ATOM 2406 CZ TYR I 324 -19.584 26.432 11.348 1.00 39.76 ATOM 2407 OH TYR I 324 -19.372 26.518 9.986 1.00 40.65 ATOM 2408 N PRO I 325 -17.941 25.166 18.487 1.00 30.86 ATOM 2409 CA PRO I 325 -17.946 24.939 19.929 1.00 31.06 ATOM 2410 C PRO I 325 -18.491 26.093 20.756 1.00 32.40 ATOM 2411 O PRO I 325 -18.811 25.922 21.934 1.00 32.68 ATOM 2412 CB PRO I 325 -16.478 24.652 20.235 1.00 29.67 ATOM 2413 CG PRO I 325 -15.767 25.497 19.225 1.00 29.72 ATOM 2414 CD PRO I 325 -16.555 25.231 17.976 1.00 28.74 ATOM 2415 N GLY I 326 -18.603 27.270 20.148 1.00 34.17 ATOM 2416 CA GLY I 326 -19.092 28.423 20.874 1.00 32.69 ATOM 2417 C GLY I 326 -20.568 28.692 20.706 1.00 32.61 ATOM 2418 O GLY I 326 -21.087 29.668 21.254 1.00 30.07 ATOM 2419 N CYS I 327 -21.257 27.841 19.947 1.00 27.22 ATOM 2420 CA CYS I 327 -22.686 28.025 19.736 1.00 29.61 ATOM 2421 C CYS I 327 -23.450 27.917 21.058 1.00 30.04 ATOM 2422 O CYS I 327 -23.254 26.970 21.814 1.00 29.04 ATOM 2423 CB CYS I 327 -23.219 26.992 18.751 1.00 32.28 ATOM 2424 SG CYS I 327 -24.992 27.170 18.441 1.00 36.07 ATOM 2425 N LYS I 328 -24.322 28.883 21.339 1.00 37.55 ATOM 2426 CA LYS I 328 -25.077 28.862 22.584 1.00 40.79 ATOM 2427 C LYS I 328 -26.192 27.808 22.547 1.00 39.50 ATOM 2428 O LYS I 328 -26.471 27.150 23.546 1.00 37.78 ATOM 2429 CB LYS I 328 -25.654 30.247 22.893 1.00 62.76 ATOM 2430 CG LYS I 328 -24.642 31.398 22.767 1.00 70.21 ATOM 2431 CD LYS I 328 -23.225 31.009 23.218 1.00 75.11 ATOM 2432 CE LYS I 328 -23.103 30.788 24.719 1.00 75.96 ATOM 2433 NZ LYS I 328 -23.173 32.054 25.484 1.00 79.25 ATOM 2434 N TYR I 329 -26.821 27.646 21.387 1.00 35.18 ATOM 2435 CA TYR I 329 -27.853 26.635 21.261 1.00 35.40 ATOM 2436 C TYR I 329 -27.189 25.293 21.570 1.00 35.93 ATOM 2437 O TYR I 329 -27.737 24.469 22.311 1.00 36.35 ATOM 2438 CB TYR I 329 -28.430 26.628 19.849 1.00 33.19 ATOM 2439 CG TYR I 329 -29.370 25.478 19.589 1.00 33.07 ATOM 2440 CD1 TYR I 329 -30.620 25.414 20.216 1.00 33.97 ATOM 2441 CD2 TYR I 329 -29.008 24.454 18.727 1.00 31.13 ATOM 2442 CE1 TYR I 329 -31.478 24.336 19.995 1.00 31.65 ATOM 2443 CE2 TYR I 329 -29.843 23.378 18.498 1.00 31.44 ATOM 2444 CZ TYR I 329 -31.078 23.321 19.132 1.00 32.44 ATOM 2445 OH TYR I 329 -31.883 22.236 18.913 1.00 28.02 ATOM 2446 N LEU I 330 -26.004 25.081 21.007 1.00 38.32 ATOM 2447 CA LEU I 330 -25.237 23.856 21.236 1.00 38.43 ATOM 2448 C LEU I 330 -25.000 23.634 22.735 1.00 38.44 ATOM 2449 O LEU I 330 -25.229 22.543 23.265 1.00 38.01 ATOM 2450 CB LEU I 330 -23.890 23.947 20.512 1.00 35.01 ATOM 2451 CG LEU I 330 -22.836 22.887 20.816 1.00 35.51 ATOM 2452 CD1 LEU I 330 -23.300 21.538 20.278 1.00 35.77 ATOM 2453 CD2 LEU I 330 -21.505 23.279 20.190 1.00 32.18 ATOM 2454 N LEU I 331 -24.543 24.676 23.420 1.00 34.78 ATOM 2455 CA LEU I 331 -24.281 24.606 24.851 1.00 36.05 ATOM 2456 C LEU I 331 -25.565 24.314 25.637 1.00 37.28 ATOM 2457 O LEU I 331 -25.574 23.487 26.548 1.00 36.81 ATOM 2458 CB LEU I 331 -23.663 25.919 25.337 1.00 32.90 ATOM 2459 CG LEU I 331 -23.362 26.029 26.831 1.00 36.12 ATOM 2460 CD1 LEU I 331 -22.338 24.969 27.220 1.00 33.64 ATOM 2461 CD2 LEU I 331 -22.848 27.427 27.164 1.00 33.74 ATOM 2462 N GLU I 332 -26.635 25.003 25.265 1.00 39.09 ATOM 2463 CA GLU I 332 -27.941 24.868 25.889 1.00 43.12 ATOM 2464 C GLU I 332 -28.433 23.424 25.819 1.00 40.83 ATOM 2465 O GLU I 332 -28.852 22.842 26.820 1.00 38.60 ATOM 2466 CB GLU I 332 -28.926 25.784 25.158 1.00 78.79 ATOM 2467 CG GLU I 332 -30.298 25.936 25.784 1.00 88.41 ATOM 2468 CD GLU I 332 -31.269 26.656 24.845 1.00 95.47 ATOM 2469 OE1 GLU I 332 -31.820 25.992 23.934 1.00 97.63 ATOM 2470 OE2 GLU I 332 -31.480 27.872 25.012 1.00 98.28 ATOM 2471 N GLN I 333 -28.362 22.852 24.622 1.00 42.34 ATOM 2472 CA GLN I 333 -28.805 21.493 24.356 1.00 40.91 ATOM 2473 C GLN I 333 -27.887 20.362 24.785 1.00 40.85 ATOM 2474 O GLN I 333 -28.366 19.308 25.216 1.00 41.83 ATOM 2475 CB GLN I 333 -29.103 21.327 22.868 1.00 40.09 ATOM 2476 CG GLN I 333 -30.249 22.163 22.345 1.00 41.33 ATOM 2477 CD GLN I 333 -31.528 21.924 23.115 1.00 42.99 ATOM 2478 OE1 GLN I 333 -31.808 20.792 23.517 1.00 42.96 ATOM 2479 NE2 GLN I 333 -32.309 22.971 23.318 1.00 43.16 ATOM 2480 N LYS I 334 -26.576 20.550 24.677 1.00 35.38 ATOM 2481 CA LYS I 334 -25.649 19.479 25.006 1.00 32.34 ATOM 2482 C LYS I 334 -24.763 19.682 26.227 1.00 32.50 ATOM 2483 O LYS I 334 -24.213 18.713 26.748 1.00 31.74 ATOM 2484 CB LYS I 334 -24.762 19.167 23.804 1.00 38.31 ATOM 2485 CG LYS I 334 -25.502 19.071 22.473 1.00 40.52 ATOM 2486 CD LYS I 334 -26.504 17.911 22.432 1.00 43.11 ATOM 2487 CE LYS I 334 -25.811 16.572 22.504 1.00 42.74 ATOM 2488 NZ LYS I 334 -26.764 15.444 22.336 1.00 43.56 ATOM 2489 N GLY I 335 -24.611 20.922 26.690 1.00 36.40 ATOM 2490 CA GLY I 335 -23.757 21.159 27.845 1.00 39.15 ATOM 2491 C GLY I 335 -22.275 21.262 27.493 1.00 40.52 ATOM 2492 O GLY I 335 -21.815 20.677 26.502 1.00 40.11 ATOM 2493 N GLN I 336 -21.525 21.994 28.302 1.00 42.53 ATOM 2494 CA GLN I 336 -20.091 22.200 28.077 1.00 44.89 ATOM 2495 C GLN I 336 -19.258 20.914 28.062 1.00 45.93 ATOM 2496 O GLN I 336 -18.327 20.787 27.272 1.00 46.19 ATOM 2497 CB GLN I 336 -19.535 23.151 29.146 1.00 51.62 ATOM 2498 CG GLN I 336 -18.132 23.663 28.863 1.00 55.05 ATOM 2499 CD GLN I 336 -18.057 24.478 27.578 1.00 56.70 ATOM 2500 OE1 GLN I 336 -18.771 25.474 27.423 1.00 56.15 ATOM 2501 NE2 GLN I 336 -17.201 24.061 26.656 1.00 57.55 ATOM 2502 N GLU I 337 -19.590 19.975 28.933 1.00 47.56 ATOM 2503 CA GLU I 337 -18.860 18.711 29.011 1.00 49.17 ATOM 2504 C GLU I 337 -18.854 18.034 27.651 1.00 46.87 ATOM 2505 O GLU I 337 -17.844 17.488 27.215 1.00 46.75 ATOM 2506 CB GLU I 337 -19.502 17.769 30.035 1.00 83.13 ATOM 2507 CG GLU I 337 -19.567 18.302 31.467 1.00 94.50 ATOM 2508 CD GLU I 337 -20.442 19.542 31.602 1.00100.15 ATOM 2509 OE1 GLU I 337 -21.610 19.508 31.152 1.00101.36 ATOM 2510 OE2 GLU I 337 -19.963 20.551 32.170 1.00103.42 ATOM 2511 N TYR I 338 -20.013 18.069 26.990 1.00 47.04 ATOM 2512 CA TYR I 338 -20.169 17.455 25.681 1.00 44.77 ATOM 2513 C TYR I 338 -19.250 18.099 24.639 1.00 43.16 ATOM 2514 O TYR I 338 -18.522 17.400 23.939 1.00 44.14 ATOM 2515 CB TYR I 338 -21.623 17.565 25.224 1.00 38.62 ATOM 2516 CG TYR I 338 -21.855 17.035 23.827 1.00 36.71 ATOM 2517 CD1 TYR I 338 -22.035 15.667 23.593 1.00 36.57 ATOM 2518 CD2 TYR I 338 -21.883 17.897 22.738 1.00 34.47 ATOM 2519 CE1 TYR I 338 -22.228 15.179 22.288 1.00 35.07 ATOM 2520 CE2 TYR I 338 -22.071 17.428 21.438 1.00 35.39 ATOM 2521 CZ TYR I 338 -22.241 16.070 21.217 1.00 35.58 ATOM 2522 OH TYR I 338 -22.407 15.621 19.931 1.00 35.53 ATOM 2523 N ILE I 339 -19.301 19.427 24.540 1.00 36.86 ATOM 2524 CA ILE I 339 -18.482 20.154 23.567 1.00 35.86 ATOM 2525 C ILE I 339 -16.992 19.842 23.726 1.00 34.82 ATOM 2526 O ILE I 339 -16.343 19.415 22.765 1.00 32.35 ATOM 2527 CB ILE I 339 -18.650 21.693 23.697 1.00 40.46 ATOM 2528 CG1 ILE I 339 -20.128 22.066 23.876 1.00 38.45 ATOM 2529 CG2 ILE I 339 -18.076 22.384 22.458 1.00 38.02 ATOM 2530 CD1 ILE I 339 -21.030 21.428 22.886 1.00 42.79 ATOM 2531 N ASN I 340 -16.473 20.068 24.930 1.00 36.95 ATOM 2532 CA ASN I 340 -15.058 19.824 25.226 1.00 38.62 ATOM 2533 C ASN I 340 -14.641 18.417 24.881 1.00 38.62 ATOM 2534 O ASN I 340 -13.586 18.188 24.286 1.00 40.38 ATOM 2535 CB ASN I 340 -14.760 20.079 26.708 1.00 38.81 ATOM 2536 CG ASN I 340 -14.923 21.533 27.096 1.00 39.30 ATOM 2537 OD1 ASN I 340 -14.741 22.430 26.276 1.00 38.21 ATOM 2538 ND2 ASN I 340 -15.245 21.771 28.363 1.00 41.31 ATOM 2539 N ASN I 341 -15.478 17.461 25.259 1.00 38.12 ATOM 2540 CA ASN I 341 -15.160 16.075 24.988 1.00 38.90 ATOM 2541 C ASN I 341 -15.092 15.821 23.480 1.00 38.38 ATOM 2542 O ASN I 341 -14.263 15.037 23.017 1.00 38.38 ATOM 2543 CB ASN I 341 -16.202 15.172 25.651 1.00 49.55 ATOM 2544 CG ASN I 341 -15.761 13.728 25.704 1.00 50.95 ATOM 2545 OD1 ASN I 341 -16.071 12.947 24.806 1.00 53.64 ATOM 2546 ND2 ASN I 341 -15.022 13.378 26.745 1.00 52.99 ATOM 2547 N ILE I 342 -15.945 16.491 22.712 1.00 39.38 ATOM 2548 CA ILE I 342 -15.923 16.321 21.265 1.00 39.32 ATOM 2549 C ILE I 342 -14.550 16.774 20.773 1.00 40.78 ATOM 2550 O ILE I 342 -13.893 16.070 20.008 1.00 39.46 ATOM 2551 CB ILE I 342 -17.007 17.182 20.565 1.00 38.08 ATOM 2552 CG1 ILE I 342 -18.405 16.618 20.857 1.00 37.15 ATOM 2553 CG2 ILE I 342 -16.746 17.223 19.057 1.00 34.91 ATOM 2554 CD1 ILE I 342 -18.646 15.247 20.258 1.00 34.73 ATOM 2555 N HIS I 343 -14.120 17.939 21.244 1.00 37.80 ATOM 2556 CA HIS I 343 -12.829 18.491 20.862 1.00 39.68 ATOM 2557 C HIS I 343 -11.621 17.761 21.440 1.00 41.60 ATOM 2558 O HIS I 343 -10.537 17.819 20.872 1.00 38.59 ATOM 2559 CB HIS I 343 -12.762 19.972 21.237 1.00 34.32 ATOM 2560 CG HIS I 343 -13.531 20.848 20.300 1.00 32.79 ATOM 2561 ND1 HIS I 343 -12.923 21.709 19.415 1.00 31.51 ATOM 2562 CD2 HIS I 343 -14.860 20.926 20.045 1.00 31.39 ATOM 2563 CE1 HIS I 343 -13.844 22.284 18.659 1.00 32.03 ATOM 2564 NE2 HIS I 343 -15.027 21.826 19.023 1.00 31.82 ATOM 2565 N LEU I 344 -11.809 17.075 22.561 1.00 51.37 ATOM 2566 CA LEU I 344 -10.701 16.362 23.181 1.00 54.28 ATOM 2567 C LEU I 344 -10.598 14.903 22.740 1.00 56.93 ATOM 2568 O LEU I 344 -9.828 14.140 23.310 1.00 58.38 ATOM 2569 CB LEU I 344 -10.823 16.437 24.702 1.00 46.05 ATOM 2570 CG LEU I 344 -10.580 17.825 25.311 1.00 45.61 ATOM 2571 CD1 LEU I 344 -11.064 17.856 26.751 1.00 46.40 ATOM 2572 CD2 LEU I 344 -9.103 18.169 25.228 1.00 45.06 ATOM 2573 N THR I 345 -11.353 14.510 21.714 1.00 71.83 ATOM 2574 CA THR I 345 -11.292 13.131 21.244 1.00 76.18 ATOM 2575 C THR I 345 -11.414 12.951 19.728 1.00 78.39 ATOM 2576 O THR I 345 -12.069 12.024 19.268 1.00 79.69 ATOM 2577 CB THR I 345 -12.369 12.257 21.934 1.00104.30 ATOM 2578 OG1 THR I 345 -13.661 12.824 21.725 1.00 69.74 ATOM 2579 CG2 THR I 345 -12.096 12.163 23.423 1.00 69.55 ATOM 2580 N HIS I 346 -10.761 13.817 18.967 1.00 95.63 ATOM 2581 CA HIS I 346 -10.786 13.735 17.504 1.00 96.47 ATOM 2582 C HIS I 346 -9.964 12.544 17.018 1.00 98.04 ATOM 2583 O HIS I 346 -10.306 11.914 16.012 1.00 99.72 ATOM 2584 CB HIS I 346 -10.235 15.020 16.895 1.00110.98 ATOM 2585 CG HIS I 346 -11.185 16.171 16.950 1.00110.11 ATOM 2586 ND1 HIS I 346 -12.350 16.212 16.212 1.00 74.52 ATOM 2587 CD2 HIS I 346 -11.138 17.330 17.649 1.00111.37 ATOM 2588 CE1 HIS I 346 -12.979 17.345 16.449 1.00 73.92 ATOM 2589 NE2 HIS I 346 -12.269 18.045 17.320 1.00 74.10 ATOM 2590 N ZN 501 -24.958 26.636 16.285 1.00 35.55 END