HETATM 1 N 8VS A1205 2.595 10.036 21.369 0.82 59.17 N HETATM 2 CA 8VS A1205 2.839 10.230 19.965 0.82 57.99 C HETATM 3 C 8VS A1205 1.536 10.431 19.215 0.82 64.58 C HETATM 4 O 8VS A1205 0.468 10.243 19.780 0.82 63.70 O HETATM 5 CB 8VS A1205 3.584 9.029 19.401 0.82 56.04 C HETATM 6 CG 8VS A1205 5.056 9.016 19.901 0.82 57.41 C HETATM 7 CD1 8VS A1205 6.096 9.482 19.067 0.82 59.36 C HETATM 8 CD2 8VS A1205 5.356 8.541 21.182 0.82 57.08 C HETATM 9 CE1 8VS A1205 7.438 9.467 19.526 0.82 59.23 C HETATM 10 CE2 8VS A1205 6.698 8.529 21.638 0.82 55.20 C HETATM 11 CZ 8VS A1205 7.732 8.993 20.809 0.82 53.41 C HETATM 12 CAA 8VS A1205 6.486 9.405 24.839 0.82 56.12 C HETATM 13 CAB 8VS A1205 6.215 8.166 25.391 0.82 55.81 C HETATM 14 CAC 8VS A1205 4.882 7.699 25.453 0.82 58.27 C HETATM 15 CAD 8VS A1205 3.838 8.479 24.958 0.82 58.52 C HETATM 16 CAE 8VS A1205 4.097 9.719 24.419 0.82 57.87 C HETATM 17 CAF 8VS A1205 5.446 10.179 24.336 0.82 55.56 C HETATM 18 CAG 8VS A1205 2.915 10.542 23.862 0.82 62.02 C HETATM 19 CAH 8VS A1205 2.422 11.715 24.735 0.82 59.23 C HETATM 20 CAI 8VS A1205 3.248 10.879 22.408 0.82 62.10 C HETATM 21 CAJ 8VS A1205 3.463 12.353 25.635 0.82 58.80 C HETATM 22 CAK 8VS A1205 2.758 13.249 26.672 0.82 60.96 C HETATM 23 CAL 8VS A1205 1.806 14.241 26.075 0.82 60.81 C HETATM 24 CAM 8VS A1205 1.013 13.739 24.864 0.82 60.24 C HETATM 25 CAN 8VS A1205 1.825 12.828 23.920 0.82 60.40 C HETATM 26 CBB 8VS A1205 9.198 8.978 21.317 0.82 53.43 C HETATM 27 CBE 8VS A1205 0.303 11.031 17.107 0.82 62.49 C HETATM 28 CBF 8VS A1205 -0.160 9.677 16.655 0.82 62.53 C HETATM 29 CBH 8VS A1205 -1.964 8.170 15.764 0.82 53.04 C HETATM 30 CBJ 8VS A1205 0.460 11.911 15.858 0.82 72.65 C HETATM 31 CBK 8VS A1205 1.172 13.242 16.101 0.82 73.94 C HETATM 32 CBL 8VS A1205 2.433 13.448 15.567 0.82 75.87 C HETATM 33 CBM 8VS A1205 3.088 14.662 15.767 0.82 71.20 C HETATM 34 CBN 8VS A1205 2.478 15.670 16.496 0.82 73.25 C HETATM 35 CBO 8VS A1205 1.205 15.472 17.027 0.82 79.53 C HETATM 36 CBP 8VS A1205 0.555 14.268 16.829 0.82 74.80 C HETATM 37 NAS 8VS A1205 1.558 10.853 17.814 0.82 64.04 N HETATM 38 NBC 8VS A1205 10.289 9.063 20.375 0.82 56.41 N HETATM 39 NBG 8VS A1205 -1.520 9.488 16.206 0.82 60.19 N HETATM 40 OAQ 8VS A1205 4.018 11.749 22.104 0.82 61.07 O HETATM 41 OBD 8VS A1205 9.429 8.894 22.518 0.82 55.50 O HETATM 42 OBI 8VS A1205 0.606 8.743 16.658 0.82 52.46 O HETATM 43 BR1 8VS A1205 0.355 16.863 18.029 0.82104.06 BR TER 44 8VS A1205 ATOM 170 N VAL A 54 0.730 17.997 30.176 1.00 57.82 N ATOM 171 CA VAL A 54 0.564 16.736 29.461 1.00 53.27 C ATOM 172 C VAL A 54 -0.912 16.450 29.228 1.00 51.86 C ATOM 173 O VAL A 54 -1.310 15.988 28.152 1.00 61.60 O ATOM 174 CB VAL A 54 1.246 15.594 30.237 1.00 48.61 C ATOM 175 CG1 VAL A 54 0.873 14.246 29.648 1.00 50.01 C ATOM 176 CG2 VAL A 54 2.754 15.781 30.240 1.00 50.74 C ATOM 192 N ALA A 57 -2.366 18.700 26.427 1.00 55.08 N ATOM 193 CA ALA A 57 -1.900 18.332 25.094 1.00 52.75 C ATOM 194 C ALA A 57 -2.729 17.192 24.516 1.00 60.42 C ATOM 195 O ALA A 57 -3.046 17.190 23.321 1.00 62.09 O ATOM 196 CB ALA A 57 -0.423 17.948 25.141 1.00 53.00 C ATOM 197 N ILE A 58 -3.091 16.214 25.349 1.00 60.14 N ATOM 198 CA ILE A 58 -3.909 15.101 24.879 1.00 57.15 C ATOM 199 C ILE A 58 -5.357 15.537 24.690 1.00 59.40 C ATOM 200 O ILE A 58 -6.074 14.990 23.843 1.00 66.52 O ATOM 201 CB ILE A 58 -3.786 13.915 25.853 1.00 54.87 C ATOM 202 CG1 ILE A 58 -2.338 13.433 25.900 1.00 53.03 C ATOM 203 CG2 ILE A 58 -4.707 12.774 25.453 1.00 53.39 C ATOM 204 CD1 ILE A 58 -2.083 12.355 26.917 1.00 59.69 C ATOM 219 N PHE A 61 -5.301 18.314 21.186 1.00 64.46 N ATOM 220 CA PHE A 61 -4.840 17.854 19.882 1.00 60.87 C ATOM 221 C PHE A 61 -5.514 16.534 19.525 1.00 68.04 C ATOM 222 O PHE A 61 -5.416 15.552 20.271 1.00 67.64 O ATOM 223 CB PHE A 61 -3.319 17.711 19.873 1.00 56.42 C ATOM 224 CG PHE A 61 -2.589 19.024 19.868 1.00 60.51 C ATOM 225 CD1 PHE A 61 -2.580 19.818 18.735 1.00 66.55 C ATOM 226 CD2 PHE A 61 -1.905 19.462 20.991 1.00 66.89 C ATOM 227 CE1 PHE A 61 -1.907 21.026 18.719 1.00 68.66 C ATOM 228 CE2 PHE A 61 -1.228 20.671 20.982 1.00 63.34 C ATOM 229 CZ PHE A 61 -1.229 21.452 19.844 1.00 61.86 C ATOM 239 N ARG A 63 -4.745 14.488 17.161 1.00 69.59 N ATOM 240 CA ARG A 63 -3.831 13.423 16.768 1.00 69.53 C ATOM 241 C ARG A 63 -3.332 12.636 17.973 1.00 63.70 C ATOM 242 O ARG A 63 -2.987 11.456 17.841 1.00 64.38 O ATOM 243 CB ARG A 63 -2.655 14.001 15.988 1.00 67.77 C ATOM 244 CG ARG A 63 -3.043 14.804 14.762 1.00 81.60 C ATOM 245 CD ARG A 63 -1.805 15.254 14.000 1.00 86.77 C ATOM 246 NE ARG A 63 -1.063 14.114 13.469 1.00 89.07 N ATOM 247 CZ ARG A 63 0.108 14.202 12.846 1.00 91.13 C ATOM 248 NH1 ARG A 63 0.685 15.384 12.673 1.00 86.59 N1+ ATOM 249 NH2 ARG A 63 0.704 13.105 12.397 1.00 87.42 N ATOM 250 N LEU A 64 -3.292 13.263 19.147 1.00 66.30 N ATOM 251 CA LEU A 64 -2.802 12.606 20.351 1.00 61.83 C ATOM 252 C LEU A 64 -3.846 11.721 21.018 1.00 64.28 C ATOM 253 O LEU A 64 -3.515 11.030 21.986 1.00 60.41 O ATOM 254 CB LEU A 64 -2.299 13.650 21.349 1.00 58.27 C ATOM 255 CG LEU A 64 -1.053 14.428 20.915 1.00 62.26 C ATOM 256 CD1 LEU A 64 -0.632 15.439 21.971 1.00 55.86 C ATOM 257 CD2 LEU A 64 0.088 13.473 20.596 1.00 61.08 C ATOM 267 N THR A 66 -5.102 8.678 21.494 1.00 62.92 N ATOM 268 CA THR A 66 -4.806 7.283 21.212 1.00 62.49 C ATOM 269 C THR A 66 -4.912 6.486 22.504 1.00 65.71 C ATOM 270 O THR A 66 -5.033 7.045 23.598 1.00 69.70 O ATOM 271 CB THR A 66 -3.420 7.119 20.574 1.00 63.94 C ATOM 272 OG1 THR A 66 -3.063 5.735 20.545 1.00 74.90 O ATOM 273 CG2 THR A 66 -2.377 7.872 21.359 1.00 60.46 C ATOM 281 N THR A 68 -2.706 4.598 24.077 1.00 62.74 N ATOM 282 CA THR A 68 -1.596 4.812 24.999 1.00 54.56 C ATOM 283 C THR A 68 -1.718 6.154 25.710 1.00 56.81 C ATOM 284 O THR A 68 -1.532 6.234 26.930 1.00 58.61 O ATOM 285 CB THR A 68 -0.268 4.710 24.248 1.00 51.17 C ATOM 286 OG1 THR A 68 -0.159 3.415 23.644 1.00 60.26 O ATOM 287 CG2 THR A 68 0.899 4.910 25.194 1.00 54.24 C ATOM 288 N ASN A 69 -2.045 7.219 24.974 1.00 60.90 N ATOM 289 CA ASN A 69 -2.150 8.532 25.599 1.00 58.70 C ATOM 290 C ASN A 69 -3.338 8.629 26.548 1.00 61.05 C ATOM 291 O ASN A 69 -3.321 9.465 27.457 1.00 64.54 O ATOM 292 CB ASN A 69 -2.235 9.626 24.535 1.00 61.53 C ATOM 293 CG ASN A 69 -0.967 9.736 23.707 1.00 61.47 C ATOM 294 OD1 ASN A 69 0.037 9.088 24.003 1.00 59.46 O ATOM 295 ND2 ASN A 69 -1.008 10.555 22.662 1.00 62.81 N ATOM 319 N ILE A 72 -1.728 7.442 29.493 1.00 57.94 N ATOM 320 CA ILE A 72 -0.835 8.509 29.938 1.00 54.31 C ATOM 321 C ILE A 72 -1.612 9.548 30.735 1.00 55.33 C ATOM 322 O ILE A 72 -1.125 10.070 31.746 1.00 55.77 O ATOM 323 CB ILE A 72 -0.114 9.147 28.734 1.00 59.02 C ATOM 324 CG1 ILE A 72 0.781 8.124 28.029 1.00 57.73 C ATOM 325 CG2 ILE A 72 0.710 10.347 29.176 1.00 58.35 C ATOM 326 CD1 ILE A 72 1.985 7.703 28.838 1.00 59.62 C ATOM 2901 N LYS A 267 11.007 4.589 14.621 1.00 56.67 N ATOM 2902 CA LYS A 267 10.282 5.548 15.449 1.00 56.21 C ATOM 2903 C LYS A 267 9.412 4.845 16.484 1.00 62.39 C ATOM 2904 O LYS A 267 9.367 5.256 17.649 1.00 62.43 O ATOM 2905 CB LYS A 267 9.435 6.475 14.579 1.00 57.31 C ATOM 2906 CG LYS A 267 8.482 7.341 15.391 1.00 68.78 C ATOM 2907 CD LYS A 267 8.233 8.692 14.746 1.00 65.98 C ATOM 2908 CE LYS A 267 7.372 9.562 15.652 1.00 73.44 C ATOM 2909 NZ LYS A 267 7.294 10.972 15.183 1.00 77.44 N1+ ATOM 2929 N LYS A 270 11.554 3.754 19.147 1.00 55.24 N ATOM 2930 CA LYS A 270 11.865 4.889 20.008 1.00 56.05 C ATOM 2931 C LYS A 270 10.720 5.163 20.974 1.00 54.14 C ATOM 2932 O LYS A 270 10.949 5.449 22.155 1.00 53.35 O ATOM 2933 CB LYS A 270 12.166 6.127 19.164 1.00 59.43 C ATOM 2934 CG LYS A 270 13.422 6.021 18.314 1.00 56.36 C ATOM 2935 CD LYS A 270 13.675 7.310 17.552 1.00 55.64 C ATOM 2936 CE LYS A 270 14.992 7.258 16.798 1.00 65.48 C ATOM 2937 NZ LYS A 270 16.143 7.043 17.719 1.00 75.55 N1+ ATOM 2938 N ALA A 271 9.478 5.067 20.489 1.00 51.62 N ATOM 2939 CA ALA A 271 8.321 5.280 21.352 1.00 47.95 C ATOM 2940 C ALA A 271 8.261 4.242 22.465 1.00 49.09 C ATOM 2941 O ALA A 271 7.863 4.555 23.593 1.00 57.05 O ATOM 2942 CB ALA A 271 7.039 5.252 20.522 1.00 50.74 C ATOM 2960 N THR A 274 10.870 5.130 25.371 1.00 52.99 N ATOM 2961 CA THR A 274 10.439 6.153 26.319 1.00 55.34 C ATOM 2962 C THR A 274 9.451 5.581 27.327 1.00 54.14 C ATOM 2963 O THR A 274 9.499 5.920 28.516 1.00 56.28 O ATOM 2964 CB THR A 274 9.828 7.340 25.574 1.00 50.67 C ATOM 2965 OG1 THR A 274 10.747 7.802 24.576 1.00 52.74 O ATOM 2966 CG2 THR A 274 9.536 8.479 26.536 1.00 53.11 C ATOM 2967 N LEU A 275 8.550 4.705 26.874 1.00 51.42 N ATOM 2968 CA LEU A 275 7.667 4.015 27.808 1.00 48.92 C ATOM 2969 C LEU A 275 8.455 3.136 28.766 1.00 51.35 C ATOM 2970 O LEU A 275 8.040 2.942 29.914 1.00 60.08 O ATOM 2971 CB LEU A 275 6.638 3.180 27.049 1.00 53.84 C ATOM 2972 CG LEU A 275 5.524 3.953 26.344 1.00 49.50 C ATOM 2973 CD1 LEU A 275 4.590 2.993 25.624 1.00 43.57 C ATOM 2974 CD2 LEU A 275 4.761 4.802 27.346 1.00 48.90 C ATOM 3380 N TYR A 326 8.654 12.740 28.615 1.00 59.00 N ATOM 3381 CA TYR A 326 7.855 12.814 27.397 1.00 56.94 C ATOM 3382 C TYR A 326 8.449 13.764 26.366 1.00 60.80 C ATOM 3383 O TYR A 326 8.068 13.699 25.193 1.00 62.48 O ATOM 3384 CB TYR A 326 6.423 13.239 27.726 1.00 51.79 C ATOM 3385 CG TYR A 326 5.681 12.253 28.597 1.00 59.42 C ATOM 3386 CD1 TYR A 326 5.929 10.889 28.505 1.00 56.83 C ATOM 3387 CD2 TYR A 326 4.737 12.688 29.519 1.00 60.94 C ATOM 3388 CE1 TYR A 326 5.252 9.985 29.303 1.00 58.28 C ATOM 3389 CE2 TYR A 326 4.057 11.793 30.323 1.00 56.79 C ATOM 3390 CZ TYR A 326 4.317 10.444 30.210 1.00 61.98 C ATOM 3391 OH TYR A 326 3.637 9.555 31.012 1.00 63.82 O ATOM 3398 N ARG A 328 11.208 13.479 25.110 1.00 54.48 N ATOM 3399 CA ARG A 328 11.896 12.650 24.129 1.00 59.35 C ATOM 3400 C ARG A 328 11.061 12.443 22.873 1.00 63.60 C ATOM 3401 O ARG A 328 11.607 12.067 21.830 1.00 66.02 O ATOM 3402 CB ARG A 328 12.249 11.291 24.737 1.00 61.52 C ATOM 3403 CG ARG A 328 13.222 11.347 25.898 1.00 67.63 C ATOM 3404 CD ARG A 328 13.368 9.976 26.531 1.00 69.37 C ATOM 3405 NE ARG A 328 13.618 8.946 25.527 1.00 65.91 N ATOM 3406 CZ ARG A 328 14.826 8.514 25.183 1.00 70.74 C ATOM 3407 NH1 ARG A 328 15.904 9.019 25.770 1.00 65.56 N1+ ATOM 3408 NH2 ARG A 328 14.958 7.574 24.255 1.00 73.57 N ATOM 3409 N SER A 329 9.752 12.672 22.953 1.00 63.16 N ATOM 3410 CA SER A 329 8.867 12.495 21.812 1.00 60.09 C ATOM 3411 C SER A 329 8.800 13.785 21.009 1.00 66.68 C ATOM 3412 O SER A 329 8.474 14.836 21.578 1.00 63.72 O ATOM 3413 CB SER A 329 7.475 12.102 22.271 1.00 59.14 C ATOM 3414 OG SER A 329 6.547 12.182 21.203 1.00 62.51 O ATOM 3415 N PRO A 330 9.100 13.763 19.709 1.00 69.98 N ATOM 3416 CA PRO A 330 8.887 14.968 18.893 1.00 65.08 C ATOM 3417 C PRO A 330 7.425 15.356 18.776 1.00 63.74 C ATOM 3418 O PRO A 330 7.130 16.505 18.426 1.00 61.95 O ATOM 3419 CB PRO A 330 9.475 14.580 17.529 1.00 61.60 C ATOM 3420 CG PRO A 330 10.388 13.425 17.814 1.00 65.38 C ATOM 3421 CD PRO A 330 9.749 12.686 18.943 1.00 64.01 C ATOM 3422 N ASP A 331 6.500 14.439 19.071 1.00 63.53 N ATOM 3423 CA ASP A 331 5.079 14.735 18.930 1.00 65.54 C ATOM 3424 C ASP A 331 4.546 15.528 20.118 1.00 64.64 C ATOM 3425 O ASP A 331 3.783 16.483 19.936 1.00 68.77 O ATOM 3426 CB ASP A 331 4.295 13.436 18.746 1.00 68.72 C ATOM 3427 CG ASP A 331 4.845 12.584 17.617 1.00 73.16 C ATOM 3428 OD1 ASP A 331 4.313 11.479 17.383 1.00 71.09 O ATOM 3429 OD2 ASP A 331 5.819 13.018 16.967 1.00 74.65 O1- ATOM 3430 N PHE A 332 4.925 15.149 21.340 1.00 63.66 N ATOM 3431 CA PHE A 332 4.607 15.992 22.488 1.00 66.75 C ATOM 3432 C PHE A 332 5.425 17.276 22.469 1.00 65.34 C ATOM 3433 O PHE A 332 4.942 18.324 22.910 1.00 68.08 O ATOM 3434 CB PHE A 332 4.837 15.226 23.793 1.00 62.75 C ATOM 3435 CG PHE A 332 4.941 16.107 25.012 1.00 64.84 C ATOM 3436 CD1 PHE A 332 6.128 16.188 25.724 1.00 68.46 C ATOM 3437 CD2 PHE A 332 3.856 16.857 25.445 1.00 69.14 C ATOM 3438 CE1 PHE A 332 6.231 16.994 26.848 1.00 65.09 C ATOM 3439 CE2 PHE A 332 3.953 17.666 26.568 1.00 63.89 C ATOM 3440 CZ PHE A 332 5.143 17.734 27.268 1.00 63.78 C ATOM 3452 N ILE A 334 6.394 19.133 19.861 1.00 60.15 N ATOM 3453 CA ILE A 334 5.635 20.078 19.050 1.00 65.50 C ATOM 3454 C ILE A 334 4.354 20.482 19.764 1.00 65.37 C ATOM 3455 O ILE A 334 3.913 21.635 19.667 1.00 66.13 O ATOM 3456 CB ILE A 334 5.347 19.468 17.663 1.00 67.88 C ATOM 3457 CG1 ILE A 334 6.649 19.269 16.886 1.00 58.46 C ATOM 3458 CG2 ILE A 334 4.376 20.330 16.874 1.00 60.39 C ATOM 3459 CD1 ILE A 334 6.458 18.587 15.556 1.00 62.05 C ATOM 3460 N ALA A 335 3.751 19.557 20.512 1.00 66.81 N ATOM 3461 CA ALA A 335 2.470 19.835 21.151 1.00 66.45 C ATOM 3462 C ALA A 335 2.604 20.900 22.234 1.00 66.05 C ATOM 3463 O ALA A 335 1.797 21.835 22.297 1.00 64.53 O ATOM 3464 CB ALA A 335 1.879 18.550 21.727 1.00 61.43 C END