Files
RFdiffusion/examples/input_pdbs/7zkr_GABARAP.pdb
2025-06-22 17:56:19 -07:00

2629 lines
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CRYST1 99.030 99.030 99.030 90.00 90.00 90.00 I 2 3 24
ATOM 1 N AMET A 3 -31.883 -45.522 2.304 0.61 35.86 A N
ANISOU 1 N AMET A 3 5093 4593 3939 -144 285 397 A N
ATOM 2 N BMET A 3 -31.896 -45.710 2.124 0.39 35.31 A N
ANISOU 2 N BMET A 3 5004 4403 4008 -56 310 184 A N
ATOM 3 CA AMET A 3 -31.011 -45.197 3.427 0.61 34.83 A C
ANISOU 3 CA AMET A 3 4968 4470 3794 -103 376 344 A C
ATOM 4 CA BMET A 3 -31.088 -45.398 3.297 0.39 34.76 A C
ANISOU 4 CA BMET A 3 4941 4335 3932 -11 338 140 A C
ATOM 5 C AMET A 3 -31.542 -45.800 4.728 0.61 33.69 A C
ANISOU 5 C AMET A 3 4916 4248 3638 48 481 6 A C
ATOM 6 C BMET A 3 -31.655 -46.083 4.532 0.39 33.35 A C
ANISOU 6 C BMET A 3 4846 4112 3714 90 499 -95 A C
ATOM 7 O AMET A 3 -32.614 -45.424 5.205 0.61 35.36 A O
ANISOU 7 O AMET A 3 5152 4392 3893 103 441 65 A O
ATOM 8 O BMET A 3 -32.857 -46.019 4.790 0.39 34.52 A O
ANISOU 8 O BMET A 3 4946 4199 3972 62 490 79 A O
ATOM 9 CB AMET A 3 -30.855 -43.678 3.571 0.61 34.20 A C
ANISOU 9 CB AMET A 3 4738 4568 3691 -120 385 669 A C
ATOM 10 CB BMET A 3 -31.045 -43.890 3.533 0.39 35.17 A C
ANISOU 10 CB BMET A 3 4909 4470 3984 22 240 322 A C
ATOM 11 CG AMET A 3 -30.760 -42.927 2.247 0.61 33.33 A C
ANISOU 11 CG AMET A 3 4356 4807 3503 -30 435 852 A C
ATOM 12 CG BMET A 3 -31.205 -43.055 2.281 0.39 35.24 A C
ANISOU 12 CG BMET A 3 4822 4634 3936 115 156 403 A C
ATOM 13 SD AMET A 3 -29.715 -41.450 2.295 0.61 31.81 A S
ANISOU 13 SD AMET A 3 3824 5017 3244 58 627 1088 A S
ATOM 14 SD BMET A 3 -31.003 -41.303 2.640 0.39 34.59 A S
ANISOU 14 SD BMET A 3 4678 4701 3762 258 114 415 A S
ATOM 15 CE AMET A 3 -30.242 -40.673 3.816 0.61 31.50 A C
ANISOU 15 CE AMET A 3 3754 4986 3229 -114 628 1156 A C
ATOM 16 CE BMET A 3 -29.239 -41.220 2.909 0.39 34.83 A C
ANISOU 16 CE BMET A 3 4616 4767 3850 81 164 382 A C
ATOM 17 N LYS A 4 -30.786 -46.735 5.296 1.00 30.72 A N
ANISOU 17 N LYS A 4 4643 3812 3218 149 556 -513 A N
ATOM 18 CA LYS A 4 -31.172 -47.413 6.528 1.00 27.20 A C
ANISOU 18 CA LYS A 4 4245 3179 2911 221 449 -747 A C
ATOM 19 C LYS A 4 -30.637 -46.627 7.718 1.00 23.07 A C
ANISOU 19 C LYS A 4 3371 2901 2491 226 283 -711 A C
ATOM 20 O LYS A 4 -29.420 -46.468 7.869 1.00 26.59 A O
ANISOU 20 O LYS A 4 3417 3654 3033 325 389 -800 A O
ATOM 21 CB LYS A 4 -30.618 -48.837 6.549 1.00 29.66 A C
ANISOU 21 CB LYS A 4 4655 3191 3423 510 493 -643 A C
ATOM 22 CG LYS A 4 -30.939 -49.609 7.820 1.00 31.56 A C
ANISOU 22 CG LYS A 4 4935 3328 3727 534 421 -420 A C
ATOM 23 N PHE A 5 -31.540 -46.136 8.558 1.00 16.20 A N
ANISOU 23 N PHE A 5 2605 1645 1904 212 227 -232 A N
ATOM 24 CA PHE A 5 -31.152 -45.413 9.760 1.00 13.51 A C
ANISOU 24 CA PHE A 5 1964 1355 1815 226 174 -132 A C
ATOM 25 C PHE A 5 -31.314 -46.311 10.979 1.00 13.58 A C
ANISOU 25 C PHE A 5 1771 1389 1999 20 149 -33 A C
ATOM 26 O PHE A 5 -32.410 -46.820 11.250 1.00 14.37 A O
ANISOU 26 O PHE A 5 1718 1704 2038 -20 -44 -44 A O
ATOM 27 CB PHE A 5 -31.944 -44.118 9.905 1.00 13.90 A C
ANISOU 27 CB PHE A 5 1868 1484 1929 225 76 -38 A C
ATOM 28 CG PHE A 5 -31.464 -43.021 9.001 1.00 13.42 A C
ANISOU 28 CG PHE A 5 1748 1477 1874 317 63 -141 A C
ATOM 29 CD1 PHE A 5 -31.821 -42.996 7.661 1.00 14.97 A C
ANISOU 29 CD1 PHE A 5 2246 1611 1832 95 43 -118 A C
ATOM 30 CD2 PHE A 5 -30.630 -42.025 9.489 1.00 13.45 A C
ANISOU 30 CD2 PHE A 5 1662 1397 2050 349 -147 -136 A C
ATOM 31 CE1 PHE A 5 -31.367 -41.981 6.835 1.00 16.46 A C
ANISOU 31 CE1 PHE A 5 2482 1827 1945 212 25 -0 A C
ATOM 32 CE2 PHE A 5 -30.177 -41.004 8.668 1.00 13.92 A C
ANISOU 32 CE2 PHE A 5 1605 1468 2215 305 -74 130 A C
ATOM 33 CZ PHE A 5 -30.536 -40.988 7.340 1.00 15.06 A C
ANISOU 33 CZ PHE A 5 1988 1616 2120 312 88 174 A C
ATOM 34 N VAL A 6 -30.211 -46.508 11.703 1.00 13.38 A N
ANISOU 34 N VAL A 6 1774 1434 1875 245 24 65 A N
ATOM 35 CA VAL A 6 -30.229 -47.294 12.931 1.00 14.06 A C
ANISOU 35 CA VAL A 6 1746 1664 1933 256 -49 398 A C
ATOM 36 C VAL A 6 -31.199 -46.702 13.948 1.00 13.74 A C
ANISOU 36 C VAL A 6 1558 1606 2056 202 -24 449 A C
ATOM 37 O VAL A 6 -31.793 -47.434 14.751 1.00 15.03 A O
ANISOU 37 O VAL A 6 1568 1881 2261 -20 140 439 A O
ATOM 38 CB VAL A 6 -28.791 -47.395 13.477 1.00 15.31 A C
ANISOU 38 CB VAL A 6 1740 1855 2221 346 -32 298 A C
ATOM 39 CG1 VAL A 6 -28.772 -48.026 14.858 1.00 16.75 A C
ANISOU 39 CG1 VAL A 6 2016 2193 2155 283 -122 516 A C
ATOM 40 CG2 VAL A 6 -27.912 -48.177 12.507 1.00 16.59 A C
ANISOU 40 CG2 VAL A 6 1867 1843 2592 464 336 10 A C
ATOM 41 N TYR A 7 -31.387 -45.380 13.923 1.00 13.58 A N
ANISOU 41 N TYR A 7 1595 1652 1912 173 35 151 A N
ATOM 42 CA TYR A 7 -32.300 -44.729 14.859 1.00 13.92 A C
ANISOU 42 CA TYR A 7 1619 1698 1972 84 176 63 A C
ATOM 43 C TYR A 7 -33.685 -45.367 14.840 1.00 14.05 A C
ANISOU 43 C TYR A 7 1573 1725 2040 27 162 -32 A C
ATOM 44 O TYR A 7 -34.331 -45.497 15.885 1.00 15.56 A O
ANISOU 44 O TYR A 7 1878 1821 2214 -126 503 -196 A O
ATOM 45 CB TYR A 7 -32.404 -43.238 14.532 1.00 13.81 A C
ANISOU 45 CB TYR A 7 1701 1616 1929 56 70 139 A C
ATOM 46 CG TYR A 7 -33.169 -42.471 15.580 1.00 13.37 A C
ANISOU 46 CG TYR A 7 1675 1541 1863 66 28 127 A C
ATOM 47 CD1 TYR A 7 -32.554 -42.081 16.766 1.00 13.80 A C
ANISOU 47 CD1 TYR A 7 1775 1770 1697 65 -82 -57 A C
ATOM 48 CD2 TYR A 7 -34.513 -42.157 15.400 1.00 13.35 A C
ANISOU 48 CD2 TYR A 7 1500 1614 1957 14 93 109 A C
ATOM 49 CE1 TYR A 7 -33.247 -41.400 17.734 1.00 14.98 A C
ANISOU 49 CE1 TYR A 7 1892 1905 1895 163 -148 -117 A C
ATOM 50 CE2 TYR A 7 -35.219 -41.476 16.368 1.00 14.32 A C
ANISOU 50 CE2 TYR A 7 1566 1781 2094 37 -156 -78 A C
ATOM 51 CZ TYR A 7 -34.578 -41.099 17.534 1.00 14.74 A C
ANISOU 51 CZ TYR A 7 1721 1877 2002 119 62 -49 A C
ATOM 52 OH TYR A 7 -35.262 -40.422 18.518 1.00 16.24 A O
ANISOU 52 OH TYR A 7 1960 2087 2125 122 267 -319 A O
ATOM 53 N LYS A 8 -34.158 -45.780 13.663 1.00 15.42 A N
ANISOU 53 N LYS A 8 1474 1924 2462 -12 -81 -202 A N
ATOM 54 CA LYS A 8 -35.496 -46.359 13.584 1.00 17.79 A C
ANISOU 54 CA LYS A 8 1537 2233 2991 52 -217 -351 A C
ATOM 55 C LYS A 8 -35.571 -47.729 14.238 1.00 19.62 A C
ANISOU 55 C LYS A 8 1591 2273 3591 -155 45 -290 A C
ATOM 56 O LYS A 8 -36.645 -48.133 14.702 1.00 21.31 A O
ANISOU 56 O LYS A 8 1722 2469 3906 -31 81 -268 A O
ATOM 57 CB LYS A 8 -35.954 -46.454 12.138 1.00 19.18 A C
ANISOU 57 CB LYS A 8 1920 2570 2796 251 -564 -599 A C
ATOM 58 CG LYS A 8 -36.114 -45.125 11.474 1.00 19.26 A C
ANISOU 58 CG LYS A 8 2027 2705 2584 420 -470 -745 A C
ATOM 59 CD LYS A 8 -36.784 -45.337 10.148 1.00 20.85 A C
ANISOU 59 CD LYS A 8 2597 2494 2833 376 -453 -576 A C
ATOM 60 CE LYS A 8 -37.053 -44.030 9.447 1.00 21.50 A C
ANISOU 60 CE LYS A 8 2980 2233 2955 444 -553 -280 A C
ATOM 61 NZ LYS A 8 -37.777 -44.269 8.160 1.00 22.69 A N
ANISOU 61 NZ LYS A 8 3154 2523 2945 137 -692 -322 A N
ATOM 62 N GLU A 9 -34.461 -48.465 14.267 1.00 20.68 A N
ANISOU 62 N GLU A 9 1884 2203 3771 128 -200 -414 A N
ATOM 63 CA GLU A 9 -34.452 -49.715 15.015 1.00 23.09 A C
ANISOU 63 CA GLU A 9 2352 2477 3943 315 -242 -179 A C
ATOM 64 C GLU A 9 -34.603 -49.437 16.499 1.00 24.20 A C
ANISOU 64 C GLU A 9 2670 2614 3909 430 -253 259 A C
ATOM 65 O GLU A 9 -35.254 -50.199 17.220 1.00 26.54 A O
ANISOU 65 O GLU A 9 3153 2963 3969 173 148 581 A O
ATOM 66 CB GLU A 9 -33.142 -50.465 14.778 1.00 24.92 A C
ANISOU 66 CB GLU A 9 2620 2691 4159 457 -60 -556 A C
ATOM 67 CG GLU A 9 -32.817 -50.757 13.330 1.00 28.92 A C
ANISOU 67 CG GLU A 9 3184 3258 4546 628 243 -882 A C
ATOM 68 CD GLU A 9 -31.488 -51.476 13.173 1.00 33.47 A C
ANISOU 68 CD GLU A 9 3686 4003 5029 765 361 -1041 A C
ATOM 69 OE1 GLU A 9 -30.841 -51.772 14.204 1.00 33.70 A O
ANISOU 69 OE1 GLU A 9 3558 4100 5146 967 475 -1197 A O
ATOM 70 OE2 GLU A 9 -31.088 -51.741 12.021 1.00 35.33 A O
ANISOU 70 OE2 GLU A 9 3924 4328 5172 808 443 -1205 A O
ATOM 71 N GLU A 10 -34.012 -48.340 16.964 1.00 22.92 A N
ANISOU 71 N GLU A 10 2601 2467 3639 525 -325 58 A N
ATOM 72 CA GLU A 10 -33.950 -48.018 18.379 1.00 22.68 A C
ANISOU 72 CA GLU A 10 2673 2516 3429 532 -30 389 A C
ATOM 73 C GLU A 10 -35.225 -47.367 18.904 1.00 22.90 A C
ANISOU 73 C GLU A 10 2969 2437 3297 751 33 604 A C
ATOM 74 O GLU A 10 -35.416 -47.329 20.124 1.00 24.90 A O
ANISOU 74 O GLU A 10 3488 2834 3138 672 133 1216 A O
ATOM 75 CB GLU A 10 -32.718 -47.138 18.644 1.00 22.96 A C
ANISOU 75 CB GLU A 10 2410 2679 3633 421 272 498 A C
ATOM 76 CG GLU A 10 -31.413 -47.778 18.164 1.00 23.95 A C
ANISOU 76 CG GLU A 10 2399 2740 3959 512 654 589 A C
ATOM 77 CD GLU A 10 -30.186 -46.880 18.316 1.00 26.44 A C
ANISOU 77 CD GLU A 10 2747 2938 4362 584 271 339 A C
ATOM 78 OE1 GLU A 10 -30.339 -45.638 18.335 1.00 27.92 A O
ANISOU 78 OE1 GLU A 10 2989 2873 4747 377 315 68 A O
ATOM 79 OE2 GLU A 10 -29.060 -47.423 18.404 1.00 26.94 A O
ANISOU 79 OE2 GLU A 10 3038 3091 4105 466 53 376 A O
ATOM 80 N HIS A 11 -36.111 -46.882 18.023 1.00 20.36 A N
ANISOU 80 N HIS A 11 2470 2101 3167 875 63 709 A N
ATOM 81 CA HIS A 11 -37.269 -46.096 18.438 1.00 18.81 A C
ANISOU 81 CA HIS A 11 2189 1992 2965 310 160 670 A C
ATOM 82 C HIS A 11 -38.463 -46.350 17.527 1.00 18.32 A C
ANISOU 82 C HIS A 11 2207 1773 2981 275 108 610 A C
ATOM 83 O HIS A 11 -38.420 -45.998 16.340 1.00 19.00 A O
ANISOU 83 O HIS A 11 2337 2104 2778 203 -126 328 A O
ATOM 84 CB HIS A 11 -36.906 -44.612 18.422 1.00 18.82 A C
ANISOU 84 CB HIS A 11 2170 2077 2905 263 126 515 A C
ATOM 85 CG HIS A 11 -35.705 -44.289 19.250 1.00 20.12 A C
ANISOU 85 CG HIS A 11 2480 2388 2779 218 -135 531 A C
ATOM 86 CD2 HIS A 11 -34.400 -44.167 18.915 1.00 21.64 A C
ANISOU 86 CD2 HIS A 11 2582 2725 2915 -14 -347 610 A C
ATOM 87 ND1 HIS A 11 -35.771 -44.095 20.614 1.00 23.32 A N
ANISOU 87 ND1 HIS A 11 3049 2745 3067 -17 -136 203 A N
ATOM 88 CE1 HIS A 11 -34.559 -43.851 21.079 1.00 24.28 A C
ANISOU 88 CE1 HIS A 11 3112 2867 3246 -153 -412 322 A C
ATOM 89 NE2 HIS A 11 -33.709 -43.888 20.069 1.00 22.85 A N
ANISOU 89 NE2 HIS A 11 2839 2769 3075 -275 -456 401 A N
ATOM 90 N PRO A 12 -39.547 -46.932 18.042 1.00 20.11 A N
ANISOU 90 N PRO A 12 2270 1860 3511 -65 163 599 A N
ATOM 91 CA PRO A 12 -40.686 -47.259 17.179 1.00 20.86 A C
ANISOU 91 CA PRO A 12 2321 1831 3773 -124 48 413 A C
ATOM 92 C PRO A 12 -41.357 -46.013 16.630 1.00 18.50 A C
ANISOU 92 C PRO A 12 1987 1484 3556 26 426 162 A C
ATOM 93 O PRO A 12 -41.307 -44.934 17.229 1.00 17.99 A O
ANISOU 93 O PRO A 12 1925 1563 3348 52 334 291 A O
ATOM 94 CB PRO A 12 -41.631 -48.028 18.111 1.00 23.01 A C
ANISOU 94 CB PRO A 12 2507 2275 3961 -423 -110 503 A C
ATOM 95 CG PRO A 12 -41.262 -47.592 19.474 1.00 23.93 A C
ANISOU 95 CG PRO A 12 2617 2583 3893 -477 158 403 A C
ATOM 96 CD PRO A 12 -39.780 -47.337 19.439 1.00 21.88 A C
ANISOU 96 CD PRO A 12 2398 2247 3668 -373 430 694 A C
ATOM 97 N PHE A 13 -42.013 -46.197 15.480 1.00 18.71 A N
ANISOU 97 N PHE A 13 1977 1462 3670 -90 369 -6 A N
ATOM 98 CA PHE A 13 -42.589 -45.084 14.733 1.00 18.50 A C
ANISOU 98 CA PHE A 13 1976 1544 3510 -112 -26 -170 A C
ATOM 99 C PHE A 13 -43.473 -44.199 15.603 1.00 16.83 A C
ANISOU 99 C PHE A 13 1655 1400 3341 -211 17 -2 A C
ATOM 100 O PHE A 13 -43.370 -42.971 15.556 1.00 16.46 A O
ANISOU 100 O PHE A 13 1755 1416 3083 -262 135 33 A O
ATOM 101 CB PHE A 13 -43.388 -45.600 13.534 1.00 19.07 A C
ANISOU 101 CB PHE A 13 1967 1715 3564 -104 -139 -292 A C
ATOM 102 CG PHE A 13 -44.177 -44.526 12.841 1.00 18.88 A C
ANISOU 102 CG PHE A 13 1770 1770 3634 -275 -212 -291 A C
ATOM 103 CD1 PHE A 13 -43.560 -43.665 11.949 1.00 19.09 A C
ANISOU 103 CD1 PHE A 13 1850 1838 3566 -362 -95 -161 A C
ATOM 104 CD2 PHE A 13 -45.529 -44.359 13.101 1.00 20.08 A C
ANISOU 104 CD2 PHE A 13 1713 2038 3879 -214 -175 -27 A C
ATOM 105 CE1 PHE A 13 -44.277 -42.662 11.321 1.00 20.90 A C
ANISOU 105 CE1 PHE A 13 2020 2193 3728 -255 -94 -106 A C
ATOM 106 CE2 PHE A 13 -46.253 -43.357 12.476 1.00 21.12 A C
ANISOU 106 CE2 PHE A 13 1773 2311 3941 -214 -121 62 A C
ATOM 107 CZ PHE A 13 -45.626 -42.507 11.582 1.00 21.64 A C
ANISOU 107 CZ PHE A 13 2032 2282 3909 -256 -227 -62 A C
ATOM 108 N GLU A 14 -44.376 -44.799 16.379 1.00 17.84 A N
ANISOU 108 N GLU A 14 1820 1482 3478 -237 279 125 A N
ATOM 109 CA GLU A 14 -45.324 -43.975 17.125 1.00 19.32 A C
ANISOU 109 CA GLU A 14 1949 1840 3553 -246 586 305 A C
ATOM 110 C GLU A 14 -44.624 -43.114 18.168 1.00 18.88 A C
ANISOU 110 C GLU A 14 2125 1801 3248 -242 566 352 A C
ATOM 111 O GLU A 14 -45.042 -41.976 18.418 1.00 19.61 A O
ANISOU 111 O GLU A 14 2253 1785 3414 -42 725 334 A O
ATOM 112 CB GLU A 14 -46.435 -44.821 17.748 1.00 22.43 A C
ANISOU 112 CB GLU A 14 2178 2160 4183 -33 557 266 A C
ATOM 113 CG GLU A 14 -47.415 -44.016 18.610 1.00 24.62 A C
ANISOU 113 CG GLU A 14 2393 2308 4655 159 596 301 A C
ATOM 114 CD GLU A 14 -48.032 -42.817 17.887 1.00 26.64 A C
ANISOU 114 CD GLU A 14 2515 2535 5070 241 676 298 A C
ATOM 115 OE1 GLU A 14 -48.159 -42.853 16.642 1.00 27.65 A O
ANISOU 115 OE1 GLU A 14 2226 2903 5376 248 488 470 A O
ATOM 116 OE2 GLU A 14 -48.395 -41.831 18.570 1.00 27.99 A O
ANISOU 116 OE2 GLU A 14 2962 2454 5218 424 802 587 A O
ATOM 117 N ALYS A 15 -43.548 -43.622 18.773 0.52 19.15 A N
ANISOU 117 N ALYS A 15 2207 1967 3103 -366 425 338 A N
ATOM 118 N BLYS A 15 -43.562 -43.638 18.786 0.48 18.81 A N
ANISOU 118 N BLYS A 15 2242 1914 2991 -286 479 492 A N
ATOM 119 CA ALYS A 15 -42.804 -42.808 19.728 0.52 19.12 A C
ANISOU 119 CA ALYS A 15 2345 2015 2906 -287 243 286 A C
ATOM 120 CA BLYS A 15 -42.782 -42.833 19.720 0.48 18.28 A C
ANISOU 120 CA BLYS A 15 2379 1885 2681 -92 363 613 A C
ATOM 121 C ALYS A 15 -42.067 -41.672 19.028 0.52 17.12 A C
ANISOU 121 C ALYS A 15 2203 1770 2533 -133 364 249 A C
ATOM 122 C BLYS A 15 -42.116 -41.667 19.002 0.48 16.50 A C
ANISOU 122 C BLYS A 15 2237 1680 2354 49 459 465 A C
ATOM 123 O ALYS A 15 -42.009 -40.552 19.550 0.52 17.96 A O
ANISOU 123 O ALYS A 15 2353 1887 2582 -332 506 124 A O
ATOM 124 O BLYS A 15 -42.154 -40.527 19.479 0.48 17.01 A O
ANISOU 124 O BLYS A 15 2401 1778 2283 56 655 398 A O
ATOM 125 CB ALYS A 15 -41.847 -43.677 20.544 0.52 21.38 A C
ANISOU 125 CB ALYS A 15 2725 2264 3133 -319 69 391 A C
ATOM 126 CB BLYS A 15 -41.737 -43.703 20.420 0.48 19.43 A C
ANISOU 126 CB BLYS A 15 2744 1902 2737 -1 322 1026 A C
ATOM 127 CG ALYS A 15 -42.552 -44.656 21.473 0.52 24.30 A C
ANISOU 127 CG ALYS A 15 3118 2691 3422 -249 14 269 A C
ATOM 128 CG BLYS A 15 -42.317 -44.734 21.373 0.48 21.80 A C
ANISOU 128 CG BLYS A 15 3099 2277 2907 106 486 905 A C
ATOM 129 CD ALYS A 15 -41.566 -45.368 22.384 0.52 25.32 A C
ANISOU 129 CD ALYS A 15 3239 2912 3468 -304 -32 294 A C
ATOM 130 CD BLYS A 15 -43.025 -44.069 22.541 0.48 22.38 A C
ANISOU 130 CD BLYS A 15 3232 2489 2780 5 771 1002 A C
ATOM 131 N ARG A 16 -41.504 -41.938 17.846 1.00 15.23 A N
ANISOU 131 N ARG A 16 1946 1521 2320 83 191 335 A N
ATOM 132 CA ARG A 16 -40.866 -40.873 17.076 1.00 13.66 A C
ANISOU 132 CA ARG A 16 1669 1287 2235 52 256 209 A C
ATOM 133 C ARG A 16 -41.884 -39.821 16.666 1.00 13.36 A C
ANISOU 133 C ARG A 16 1475 1459 2142 -43 378 98 A C
ATOM 134 O ARG A 16 -41.649 -38.618 16.820 1.00 12.92 A O
ANISOU 134 O ARG A 16 1467 1446 1994 -28 195 19 A O
ATOM 135 CB ARG A 16 -40.189 -41.443 15.826 1.00 13.94 A C
ANISOU 135 CB ARG A 16 1552 1522 2222 192 182 -55 A C
ATOM 136 CG ARG A 16 -39.149 -42.522 16.097 1.00 14.86 A C
ANISOU 136 CG ARG A 16 1706 1499 2441 159 342 -119 A C
ATOM 137 CD ARG A 16 -38.321 -42.869 14.859 1.00 14.90 A C
ANISOU 137 CD ARG A 16 1664 1463 2535 18 11 -291 A C
ATOM 138 NE ARG A 16 -39.101 -43.072 13.639 1.00 16.16 A N
ANISOU 138 NE ARG A 16 1796 1669 2673 -131 80 -140 A N
ATOM 139 CZ ARG A 16 -39.382 -44.251 13.098 1.00 16.21 A C
ANISOU 139 CZ ARG A 16 1790 1678 2690 -96 50 -86 A C
ATOM 140 NH1 ARG A 16 -39.078 -45.390 13.707 1.00 17.93 A N
ANISOU 140 NH1 ARG A 16 2124 1793 2897 -34 345 -70 A N
ATOM 141 NH2 ARG A 16 -39.965 -44.291 11.903 1.00 18.54 A N
ANISOU 141 NH2 ARG A 16 1979 2243 2823 -159 82 -66 A N
ATOM 142 N ARG A 17 -43.023 -40.265 16.132 1.00 13.78 A N
ANISOU 142 N ARG A 17 1468 1408 2359 -85 303 33 A N
ATOM 143 CA ARG A 17 -44.028 -39.340 15.626 1.00 13.40 A C
ANISOU 143 CA ARG A 17 1365 1492 2235 -16 202 -182 A C
ATOM 144 C ARG A 17 -44.561 -38.448 16.736 1.00 13.56 A C
ANISOU 144 C ARG A 17 1357 1542 2254 -38 247 142 A C
ATOM 145 O ARG A 17 -44.716 -37.235 16.546 1.00 13.85 A O
ANISOU 145 O ARG A 17 1436 1592 2234 55 284 75 A O
ATOM 146 CB ARG A 17 -45.164 -40.127 14.976 1.00 14.86 A C
ANISOU 146 CB ARG A 17 1399 1694 2554 -126 75 -68 A C
ATOM 147 CG ARG A 17 -46.211 -39.269 14.290 1.00 15.94 A C
ANISOU 147 CG ARG A 17 1390 1863 2803 -47 247 -31 A C
ATOM 148 CD ARG A 17 -47.569 -39.960 14.323 1.00 19.05 A C
ANISOU 148 CD ARG A 17 1788 2095 3354 -51 204 -144 A C
ATOM 149 NE ARG A 17 -48.066 -40.056 15.691 1.00 19.69 A N
ANISOU 149 NE ARG A 17 1607 2163 3712 81 268 -24 A N
ATOM 150 CZ ARG A 17 -48.580 -39.038 16.368 1.00 20.41 A C
ANISOU 150 CZ ARG A 17 1865 2328 3564 479 388 280 A C
ATOM 151 NH1 ARG A 17 -48.750 -37.848 15.809 1.00 20.20 A N
ANISOU 151 NH1 ARG A 17 1775 2463 3435 447 344 351 A N
ATOM 152 NH2 ARG A 17 -48.921 -39.213 17.641 1.00 22.79 A N
ANISOU 152 NH2 ARG A 17 2192 2747 3719 517 609 478 A N
ATOM 153 N ASER A 18 -44.861 -39.034 17.898 0.52 14.56 A N
ANISOU 153 N ASER A 18 1631 1602 2297 22 445 248 A N
ATOM 154 N BSER A 18 -44.855 -39.034 17.902 0.37 14.02 A N
ANISOU 154 N BSER A 18 1476 1551 2302 4 340 184 A N
ATOM 155 N CSER A 18 -44.840 -39.025 17.908 0.11 13.76 A N
ANISOU 155 N CSER A 18 1404 1607 2216 4 162 134 A N
ATOM 156 CA ASER A 18 -45.352 -38.238 19.017 0.52 16.00 A C
ANISOU 156 CA ASER A 18 1870 1829 2380 -171 602 161 A C
ATOM 157 CA BSER A 18 -45.353 -38.244 19.024 0.37 14.86 A C
ANISOU 157 CA BSER A 18 1621 1667 2358 -174 445 101 A C
ATOM 158 CA CSER A 18 -45.363 -38.226 19.012 0.11 14.20 A C
ANISOU 158 CA CSER A 18 1507 1710 2178 -5 91 82 A C
ATOM 159 C ASER A 18 -44.330 -37.189 19.427 0.52 14.52 A C
ANISOU 159 C ASER A 18 1697 1674 2146 90 410 33 A C
ATOM 160 C BSER A 18 -44.334 -37.198 19.448 0.37 14.34 A C
ANISOU 160 C BSER A 18 1581 1628 2238 75 328 7 A C
ATOM 161 C CSER A 18 -44.338 -37.205 19.491 0.11 14.19 A C
ANISOU 161 C CSER A 18 1524 1696 2170 97 181 86 A C
ATOM 162 O ASER A 18 -44.678 -36.025 19.654 0.52 14.61 A O
ANISOU 162 O ASER A 18 1712 1747 2092 194 401 105 A O
ATOM 163 O BSER A 18 -44.688 -36.044 19.715 0.37 14.94 A O
ANISOU 163 O BSER A 18 1603 1714 2359 176 302 -1 A O
ATOM 164 O CSER A 18 -44.695 -36.076 19.846 0.11 14.67 A O
ANISOU 164 O CSER A 18 1547 1747 2279 157 152 70 A O
ATOM 165 CB ASER A 18 -45.688 -39.149 20.199 0.52 18.61 A C
ANISOU 165 CB ASER A 18 2264 2122 2684 -179 677 257 A C
ATOM 166 CB BSER A 18 -45.696 -39.162 20.199 0.37 15.88 A C
ANISOU 166 CB BSER A 18 1762 1761 2509 -262 495 171 A C
ATOM 167 CB CSER A 18 -45.804 -39.134 20.159 0.11 14.40 A C
ANISOU 167 CB CSER A 18 1552 1785 2134 37 -161 71 A C
ATOM 168 OG ASER A 18 -46.084 -38.388 21.326 0.52 20.92 A O
ANISOU 168 OG ASER A 18 2539 2503 2905 34 661 329 A O
ATOM 169 OG BSER A 18 -46.765 -40.034 19.877 0.37 16.65 A O
ANISOU 169 OG BSER A 18 1770 1964 2592 -190 475 195 A O
ATOM 170 OG CSER A 18 -44.707 -39.856 20.689 0.11 14.37 A O
ANISOU 170 OG CSER A 18 1515 1865 2078 122 -370 39 A O
ATOM 171 N GLU A 19 -43.058 -37.583 19.504 1.00 13.80 A N
ANISOU 171 N GLU A 19 1518 1651 2076 91 304 176 A N
ATOM 172 CA GLU A 19 -42.012 -36.642 19.880 1.00 13.53 A C
ANISOU 172 CA GLU A 19 1496 1594 2051 10 97 256 A C
ATOM 173 C GLU A 19 -41.848 -35.548 18.832 1.00 12.00 A C
ANISOU 173 C GLU A 19 1258 1509 1794 114 138 -39 A C
ATOM 174 O GLU A 19 -41.645 -34.380 19.180 1.00 12.28 A O
ANISOU 174 O GLU A 19 1414 1534 1718 92 8 11 A O
ATOM 175 CB GLU A 19 -40.690 -37.384 20.074 1.00 13.61 A C
ANISOU 175 CB GLU A 19 1592 1551 2028 129 -63 193 A C
ATOM 176 CG GLU A 19 -39.543 -36.452 20.447 1.00 15.92 A C
ANISOU 176 CG GLU A 19 1762 2000 2285 284 -143 -48 A C
ATOM 177 CD GLU A 19 -38.256 -37.175 20.798 1.00 17.58 A C
ANISOU 177 CD GLU A 19 2174 2299 2208 294 -180 40 A C
ATOM 178 OE1 GLU A 19 -37.866 -38.112 20.075 1.00 21.73 A O
ANISOU 178 OE1 GLU A 19 2436 2977 2845 816 51 -150 A O
ATOM 179 OE2 GLU A 19 -37.612 -36.789 21.793 1.00 20.41 A O
ANISOU 179 OE2 GLU A 19 2508 2622 2625 445 -424 -118 A O
ATOM 180 N GLY A 20 -41.913 -35.915 17.548 1.00 11.83 A N
ANISOU 180 N GLY A 20 1186 1541 1769 107 127 60 A N
ATOM 181 CA GLY A 20 -41.746 -34.932 16.492 1.00 11.91 A C
ANISOU 181 CA GLY A 20 1326 1428 1771 44 102 117 A C
ATOM 182 C GLY A 20 -42.861 -33.907 16.469 1.00 11.60 A C
ANISOU 182 C GLY A 20 1340 1374 1693 -85 -33 136 A C
ATOM 183 O GLY A 20 -42.614 -32.716 16.265 1.00 11.61 A O
ANISOU 183 O GLY A 20 1242 1412 1758 34 4 -74 A O
ATOM 184 N GLU A 21 -44.107 -34.352 16.663 1.00 12.01 A N
ANISOU 184 N GLU A 21 1269 1479 1815 54 -70 56 A N
ATOM 185 CA GLU A 21 -45.222 -33.408 16.739 1.00 12.57 A C
ANISOU 185 CA GLU A 21 1283 1472 2022 6 -71 43 A C
ATOM 186 C GLU A 21 -45.007 -32.405 17.868 1.00 11.97 A C
ANISOU 186 C GLU A 21 1159 1396 1992 84 119 111 A C
ATOM 187 O GLU A 21 -45.156 -31.189 17.685 1.00 12.58 A O
ANISOU 187 O GLU A 21 1236 1555 1988 99 66 3 A O
ATOM 188 CB GLU A 21 -46.538 -34.161 16.950 1.00 13.63 A C
ANISOU 188 CB GLU A 21 1210 1760 2209 -141 -29 158 A C
ATOM 189 CG GLU A 21 -47.721 -33.233 17.217 1.00 14.49 A C
ANISOU 189 CG GLU A 21 1247 1812 2445 -63 151 170 A C
ATOM 190 CD GLU A 21 -49.037 -33.963 17.471 1.00 15.76 A C
ANISOU 190 CD GLU A 21 1339 1842 2808 40 202 139 A C
ATOM 191 OE1 GLU A 21 -49.027 -35.204 17.644 1.00 16.56 A O
ANISOU 191 OE1 GLU A 21 1414 1738 3141 -27 244 271 A O
ATOM 192 OE2 GLU A 21 -50.090 -33.287 17.494 1.00 16.07 A O
ANISOU 192 OE2 GLU A 21 1439 1974 2693 72 287 71 A O
ATOM 193 N LYS A 22 -44.643 -32.903 19.050 1.00 12.00 A N
ANISOU 193 N LYS A 22 1113 1619 1828 -6 52 114 A N
ATOM 194 CA LYS A 22 -44.461 -32.023 20.198 1.00 12.16 A C
ANISOU 194 CA LYS A 22 1300 1768 1552 -65 144 105 A C
ATOM 195 C LYS A 22 -43.312 -31.041 19.993 1.00 11.25 A C
ANISOU 195 C LYS A 22 1308 1444 1524 139 89 157 A C
ATOM 196 O LYS A 22 -43.413 -29.874 20.393 1.00 11.86 A O
ANISOU 196 O LYS A 22 1212 1521 1775 280 246 143 A O
ATOM 197 CB LYS A 22 -44.231 -32.854 21.457 1.00 13.76 A C
ANISOU 197 CB LYS A 22 1656 1915 1659 -94 363 285 A C
ATOM 198 CG LYS A 22 -45.439 -33.664 21.897 1.00 16.57 A C
ANISOU 198 CG LYS A 22 2384 2066 1845 -65 478 233 A C
ATOM 199 CD LYS A 22 -45.093 -34.577 23.064 1.00 22.56 A C
ANISOU 199 CD LYS A 22 3341 2794 2437 -307 644 525 A C
ATOM 200 CE LYS A 22 -46.238 -35.524 23.390 1.00 27.51 A C
ANISOU 200 CE LYS A 22 4106 3382 2965 -248 630 675 A C
ATOM 201 NZ LYS A 22 -45.828 -36.565 24.373 1.00 31.03 A N
ANISOU 201 NZ LYS A 22 4648 3795 3348 -71 586 568 A N
ATOM 202 N ILE A 23 -42.196 -31.498 19.415 1.00 10.52 A N
ANISOU 202 N ILE A 23 1253 1359 1385 187 104 49 A N
ATOM 203 CA ILE A 23 -41.028 -30.627 19.307 1.00 10.17 A C
ANISOU 203 CA ILE A 23 1190 1319 1357 141 28 144 A C
ATOM 204 C ILE A 23 -41.271 -29.520 18.289 1.00 10.02 A C
ANISOU 204 C ILE A 23 1081 1379 1347 82 28 -62 A C
ATOM 205 O ILE A 23 -40.750 -28.409 18.439 1.00 10.04 A O
ANISOU 205 O ILE A 23 1179 1373 1264 66 -35 -14 A O
ATOM 206 CB ILE A 23 -39.745 -31.440 19.020 1.00 10.56 A C
ANISOU 206 CB ILE A 23 1188 1407 1418 149 -61 -6 A C
ATOM 207 CG1 ILE A 23 -38.494 -30.698 19.520 1.00 11.14 A C
ANISOU 207 CG1 ILE A 23 1253 1517 1461 -73 -144 7 A C
ATOM 208 CG2 ILE A 23 -39.612 -31.774 17.534 1.00 11.43 A C
ANISOU 208 CG2 ILE A 23 1326 1519 1498 239 -21 -176 A C
ATOM 209 CD1 ILE A 23 -38.357 -30.664 21.029 1.00 11.67 A C
ANISOU 209 CD1 ILE A 23 1547 1518 1368 85 -152 63 A C
ATOM 210 N ARG A 24 -42.070 -29.792 17.248 1.00 10.13 A N
ANISOU 210 N ARG A 24 1067 1417 1363 193 50 -15 A N
ATOM 211 CA ARG A 24 -42.405 -28.756 16.276 1.00 10.91 A C
ANISOU 211 CA ARG A 24 1113 1546 1486 260 -19 7 A C
ATOM 212 C ARG A 24 -43.279 -27.680 16.906 1.00 10.23 A C
ANISOU 212 C ARG A 24 939 1499 1450 58 -12 1 A C
ATOM 213 O ARG A 24 -43.120 -26.493 16.608 1.00 11.27 A O
ANISOU 213 O ARG A 24 1174 1544 1565 80 103 65 A O
ATOM 214 CB ARG A 24 -43.091 -29.385 15.062 1.00 11.39 A C
ANISOU 214 CB ARG A 24 1161 1618 1547 33 34 -60 A C
ATOM 215 CG ARG A 24 -42.137 -30.159 14.123 1.00 12.46 A C
ANISOU 215 CG ARG A 24 1245 1910 1578 173 46 -47 A C
ATOM 216 CD ARG A 24 -41.237 -29.203 13.333 1.00 13.61 A C
ANISOU 216 CD ARG A 24 1191 2530 1452 -16 29 68 A C
ATOM 217 NE ARG A 24 -42.038 -28.375 12.445 1.00 15.27 A N
ANISOU 217 NE ARG A 24 1314 2925 1562 -408 -321 450 A N
ATOM 218 CZ ARG A 24 -41.785 -27.108 12.146 1.00 16.10 A C
ANISOU 218 CZ ARG A 24 1299 3002 1817 -385 -329 408 A C
ATOM 219 NH1 ARG A 24 -40.699 -26.491 12.587 1.00 15.84 A N
ANISOU 219 NH1 ARG A 24 1407 2633 1979 -241 -367 -14 A N
ATOM 220 NH2 ARG A 24 -42.663 -26.432 11.410 1.00 19.26 A N
ANISOU 220 NH2 ARG A 24 1777 3160 2381 -579 -731 912 A N
ATOM 221 N LYS A 25 -44.201 -28.072 17.791 1.00 10.56 A N
ANISOU 221 N LYS A 25 974 1485 1551 144 31 -41 A N
ATOM 222 CA LYS A 25 -45.023 -27.079 18.477 1.00 10.85 A C
ANISOU 222 CA LYS A 25 1049 1436 1638 135 76 -104 A C
ATOM 223 C LYS A 25 -44.210 -26.244 19.455 1.00 10.66 A C
ANISOU 223 C LYS A 25 1099 1475 1477 99 38 -35 A C
ATOM 224 O LYS A 25 -44.476 -25.048 19.629 1.00 11.54 A O
ANISOU 224 O LYS A 25 1279 1305 1801 81 -99 -126 A O
ATOM 225 CB LYS A 25 -46.153 -27.769 19.229 1.00 11.95 A C
ANISOU 225 CB LYS A 25 1162 1563 1814 -89 212 -133 A C
ATOM 226 CG LYS A 25 -47.211 -28.354 18.335 1.00 12.32 A C
ANISOU 226 CG LYS A 25 1126 1609 1946 -124 139 -158 A C
ATOM 227 CD LYS A 25 -48.185 -29.192 19.135 1.00 13.36 A C
ANISOU 227 CD LYS A 25 1257 1970 1849 -112 -37 -180 A C
ATOM 228 CE LYS A 25 -49.298 -29.678 18.254 1.00 13.94 A C
ANISOU 228 CE LYS A 25 1408 1929 1960 -365 -108 275 A C
ATOM 229 NZ LYS A 25 -50.233 -30.582 18.980 1.00 14.81 A N
ANISOU 229 NZ LYS A 25 1505 2119 2004 -263 -99 201 A N
ATOM 230 N ALYS A 26 -43.240 -26.859 20.130 0.51 10.23 A N
ANISOU 230 N ALYS A 26 1071 1434 1383 64 104 -40 A N
ATOM 231 N BLYS A 26 -43.238 -26.859 20.128 0.49 10.64 A N
ANISOU 231 N BLYS A 26 1121 1482 1438 60 110 -47 A N
ATOM 232 CA ALYS A 26 -42.468 -26.129 21.126 0.51 11.21 A C
ANISOU 232 CA ALYS A 26 1269 1694 1295 193 -102 -133 A C
ATOM 233 CA BLYS A 26 -42.464 -26.137 21.128 0.49 12.05 A C
ANISOU 233 CA BLYS A 26 1386 1759 1432 149 -39 -183 A C
ATOM 234 C ALYS A 26 -41.455 -25.201 20.470 0.51 10.58 A C
ANISOU 234 C ALYS A 26 1071 1577 1373 132 -71 -313 A C
ATOM 235 C BLYS A 26 -41.428 -25.224 20.491 0.49 11.18 A C
ANISOU 235 C BLYS A 26 1213 1609 1425 58 -63 -399 A C
ATOM 236 O ALYS A 26 -41.221 -24.089 20.957 0.51 11.70 A O
ANISOU 236 O ALYS A 26 1193 1704 1548 258 29 -312 A O
ATOM 237 O BLYS A 26 -41.150 -24.142 21.023 0.49 12.09 A O
ANISOU 237 O BLYS A 26 1383 1684 1525 88 -7 -553 A O
ATOM 238 CB ALYS A 26 -41.775 -27.113 22.071 0.51 16.79 A C
ANISOU 238 CB ALYS A 26 2025 2377 1978 299 -279 -27 A C
ATOM 239 CB BLYS A 26 -41.789 -27.127 22.080 0.49 17.15 A C
ANISOU 239 CB BLYS A 26 2064 2430 2023 272 -235 -57 A C
ATOM 240 CG ALYS A 26 -41.222 -26.480 23.341 0.51 23.29 A C
ANISOU 240 CG ALYS A 26 2927 3148 2772 209 -254 84 A C
ATOM 241 CG BLYS A 26 -41.218 -26.490 23.338 0.49 23.48 A C
ANISOU 241 CG BLYS A 26 2958 3166 2797 190 -243 76 A C
ATOM 242 CD ALYS A 26 -40.661 -27.532 24.294 0.51 27.50 A C
ANISOU 242 CD ALYS A 26 3476 3587 3385 124 -64 108 A C
ATOM 243 CD BLYS A 26 -40.831 -27.538 24.376 0.49 27.32 A C
ANISOU 243 CD BLYS A 26 3467 3584 3329 100 -122 144 A C
ATOM 244 CE ALYS A 26 -41.756 -28.329 24.979 0.51 29.50 A C
ANISOU 244 CE ALYS A 26 3715 3773 3722 74 42 -96 A C
ATOM 245 CE BLYS A 26 -40.323 -26.882 25.653 0.49 29.00 A C
ANISOU 245 CE BLYS A 26 3694 3745 3581 20 -140 8 A C
ATOM 246 NZ ALYS A 26 -42.194 -27.702 26.257 0.51 30.90 A N
ANISOU 246 NZ ALYS A 26 3937 3922 3883 15 50 -202 A N
ATOM 247 NZ BLYS A 26 -39.971 -27.881 26.703 0.49 29.41 A N
ANISOU 247 NZ BLYS A 26 3746 3775 3655 -18 -130 30 A N
ATOM 248 N TYR A 27 -40.857 -25.634 19.362 1.00 10.01 A N
ANISOU 248 N TYR A 27 1132 1356 1316 129 -45 -207 A N
ATOM 249 CA TYR A 27 -39.777 -24.902 18.706 1.00 9.64 A C
ANISOU 249 CA TYR A 27 996 1318 1348 50 12 -50 A C
ATOM 250 C TYR A 27 -40.076 -24.802 17.216 1.00 9.92 A C
ANISOU 250 C TYR A 27 1136 1303 1330 -47 -89 -180 A C
ATOM 251 O TYR A 27 -39.412 -25.452 16.394 1.00 10.26 A O
ANISOU 251 O TYR A 27 1185 1384 1330 26 -10 -209 A O
ATOM 252 CB TYR A 27 -38.438 -25.599 18.944 1.00 10.24 A C
ANISOU 252 CB TYR A 27 1052 1431 1409 193 -125 -34 A C
ATOM 253 CG TYR A 27 -38.076 -25.792 20.399 1.00 10.47 A C
ANISOU 253 CG TYR A 27 1041 1426 1512 111 -102 -131 A C
ATOM 254 CD1 TYR A 27 -37.576 -24.739 21.155 1.00 11.25 A C
ANISOU 254 CD1 TYR A 27 1330 1473 1471 7 -66 -154 A C
ATOM 255 CD2 TYR A 27 -38.236 -27.020 21.017 1.00 10.98 A C
ANISOU 255 CD2 TYR A 27 1309 1431 1432 244 73 -144 A C
ATOM 256 CE1 TYR A 27 -37.231 -24.917 22.490 1.00 12.71 A C
ANISOU 256 CE1 TYR A 27 1718 1684 1429 206 -254 -130 A C
ATOM 257 CE2 TYR A 27 -37.892 -27.206 22.343 1.00 12.26 A C
ANISOU 257 CE2 TYR A 27 1528 1729 1402 282 -40 -145 A C
ATOM 258 CZ TYR A 27 -37.386 -26.155 23.074 1.00 12.86 A C
ANISOU 258 CZ TYR A 27 1765 1863 1258 351 -264 -164 A C
ATOM 259 OH TYR A 27 -37.043 -26.326 24.398 1.00 15.11 A O
ANISOU 259 OH TYR A 27 2144 2037 1560 169 -319 -68 A O
ATOM 260 N PRO A 28 -41.056 -23.975 16.822 1.00 10.55 A N
ANISOU 260 N PRO A 28 1047 1496 1466 104 -86 -17 A N
ATOM 261 CA PRO A 28 -41.476 -23.971 15.404 1.00 11.73 A C
ANISOU 261 CA PRO A 28 1124 1718 1615 32 -276 -22 A C
ATOM 262 C PRO A 28 -40.450 -23.377 14.453 1.00 10.96 A C
ANISOU 262 C PRO A 28 1232 1561 1373 204 -253 -35 A C
ATOM 263 O PRO A 28 -40.552 -23.573 13.230 1.00 12.35 A O
ANISOU 263 O PRO A 28 1446 1684 1562 -19 -246 -7 A O
ATOM 264 CB PRO A 28 -42.777 -23.157 15.422 1.00 13.33 A C
ANISOU 264 CB PRO A 28 1214 1819 2032 147 -245 -10 A C
ATOM 265 CG PRO A 28 -42.626 -22.279 16.619 1.00 13.18 A C
ANISOU 265 CG PRO A 28 1296 1756 1955 314 44 251 A C
ATOM 266 CD PRO A 28 -41.932 -23.123 17.648 1.00 11.57 A C
ANISOU 266 CD PRO A 28 1108 1593 1696 268 161 48 A C
ATOM 267 N ASP A 29 -39.477 -22.645 14.978 1.00 10.28 A N
ANISOU 267 N ASP A 29 1116 1294 1494 220 -143 -50 A N
ATOM 268 CA ASP A 29 -38.382 -22.075 14.213 1.00 9.99 A C
ANISOU 268 CA ASP A 29 1131 1276 1390 142 -23 -34 A C
ATOM 269 C ASP A 29 -37.166 -22.991 14.181 1.00 9.44 A C
ANISOU 269 C ASP A 29 1116 1291 1178 103 -60 -62 A C
ATOM 270 O ASP A 29 -36.085 -22.560 13.769 1.00 10.14 A O
ANISOU 270 O ASP A 29 1240 1247 1365 72 17 -128 A O
ATOM 271 CB ASP A 29 -38.022 -20.687 14.762 1.00 10.76 A C
ANISOU 271 CB ASP A 29 1245 1382 1462 156 13 -119 A C
ATOM 272 CG ASP A 29 -37.747 -20.683 16.261 1.00 11.02 A C
ANISOU 272 CG ASP A 29 1245 1182 1762 172 -202 -223 A C
ATOM 273 OD1 ASP A 29 -37.843 -21.747 16.902 1.00 11.22 A O
ANISOU 273 OD1 ASP A 29 1499 1256 1509 137 -109 -231 A O
ATOM 274 OD2 ASP A 29 -37.434 -19.601 16.799 1.00 13.53 A O
ANISOU 274 OD2 ASP A 29 1719 1347 2075 146 -540 -216 A O
ATOM 275 N ARG A 30 -37.328 -24.241 14.604 1.00 9.07 A N
ANISOU 275 N ARG A 30 1064 1208 1174 90 -99 -143 A N
ATOM 276 CA ARG A 30 -36.303 -25.264 14.516 1.00 9.15 A C
ANISOU 276 CA ARG A 30 1064 1212 1199 129 -97 -194 A C
ATOM 277 C ARG A 30 -36.899 -26.494 13.853 1.00 9.06 A C
ANISOU 277 C ARG A 30 1045 1220 1177 9 -140 -100 A C
ATOM 278 O ARG A 30 -38.122 -26.661 13.797 1.00 9.88 A O
ANISOU 278 O ARG A 30 1084 1354 1315 9 -205 -150 A O
ATOM 279 CB ARG A 30 -35.768 -25.637 15.904 1.00 9.52 A C
ANISOU 279 CB ARG A 30 1187 1357 1071 38 -262 -181 A C
ATOM 280 CG ARG A 30 -35.041 -24.496 16.616 1.00 10.00 A C
ANISOU 280 CG ARG A 30 1261 1405 1134 73 -216 -229 A C
ATOM 281 CD ARG A 30 -34.587 -24.943 17.992 1.00 9.84 A C
ANISOU 281 CD ARG A 30 1180 1256 1302 95 -208 -248 A C
ATOM 282 NE ARG A 30 -33.599 -24.083 18.632 1.00 10.06 A N
ANISOU 282 NE ARG A 30 1247 1335 1239 132 -179 -341 A N
ATOM 283 CZ ARG A 30 -33.879 -23.177 19.561 1.00 10.16 A C
ANISOU 283 CZ ARG A 30 1291 1281 1287 105 -80 -290 A C
ATOM 284 NH1 ARG A 30 -35.118 -22.764 19.770 1.00 10.80 A N
ANISOU 284 NH1 ARG A 30 1121 1435 1549 147 56 -377 A N
ATOM 285 NH2 ARG A 30 -32.899 -22.710 20.331 1.00 10.69 A N
ANISOU 285 NH2 ARG A 30 1363 1332 1365 47 -248 -379 A N
ATOM 286 N VAL A 31 -36.031 -27.356 13.338 1.00 9.17 A N
ANISOU 286 N VAL A 31 1231 1119 1133 109 -174 -152 A N
ATOM 287 CA VAL A 31 -36.500 -28.626 12.792 1.00 10.80 A C
ANISOU 287 CA VAL A 31 1642 1290 1171 180 -355 -184 A C
ATOM 288 C VAL A 31 -35.731 -29.790 13.396 1.00 9.55 A C
ANISOU 288 C VAL A 31 1175 1364 1088 215 -205 -129 A C
ATOM 289 O VAL A 31 -34.501 -29.728 13.585 1.00 9.69 A O
ANISOU 289 O VAL A 31 1286 1315 1080 102 -97 -130 A O
ATOM 290 CB VAL A 31 -36.511 -28.662 11.259 1.00 12.78 A C
ANISOU 290 CB VAL A 31 1935 1495 1428 183 -380 -126 A C
ATOM 291 CG1 VAL A 31 -37.530 -27.671 10.704 1.00 13.81 A C
ANISOU 291 CG1 VAL A 31 2160 1559 1528 173 -419 -101 A C
ATOM 292 CG2 VAL A 31 -35.143 -28.400 10.743 1.00 12.23 A C
ANISOU 292 CG2 VAL A 31 1532 1528 1589 99 -341 -150 A C
ATOM 293 N PRO A 32 -36.434 -30.873 13.706 1.00 9.26 A N
ANISOU 293 N PRO A 32 1120 1193 1205 102 -120 -89 A N
ATOM 294 CA PRO A 32 -35.793 -32.032 14.320 1.00 9.42 A C
ANISOU 294 CA PRO A 32 1195 1202 1181 120 -84 -67 A C
ATOM 295 C PRO A 32 -35.192 -32.911 13.234 1.00 9.41 A C
ANISOU 295 C PRO A 32 1117 1224 1234 2 -239 37 A C
ATOM 296 O PRO A 32 -35.834 -33.194 12.219 1.00 9.79 A O
ANISOU 296 O PRO A 32 1188 1266 1267 134 -197 -174 A O
ATOM 297 CB PRO A 32 -36.958 -32.725 15.031 1.00 10.35 A C
ANISOU 297 CB PRO A 32 1256 1354 1322 88 -89 -62 A C
ATOM 298 CG PRO A 32 -38.156 -32.396 14.179 1.00 10.83 A C
ANISOU 298 CG PRO A 32 1185 1412 1519 19 -132 -199 A C
ATOM 299 CD PRO A 32 -37.907 -30.995 13.675 1.00 10.58 A C
ANISOU 299 CD PRO A 32 1098 1534 1386 73 -124 -181 A C
ATOM 300 N AVAL A 33 -33.958 -33.357 13.467 0.62 9.86 A N
ANISOU 300 N AVAL A 33 1206 1246 1293 338 -288 -251 A N
ATOM 301 N BVAL A 33 -33.940 -33.307 13.433 0.38 9.49 A N
ANISOU 301 N BVAL A 33 1152 1158 1294 -166 -57 354 A N
ATOM 302 CA AVAL A 33 -33.167 -34.060 12.464 0.62 9.95 A C
ANISOU 302 CA AVAL A 33 1244 1289 1248 419 -174 -387 A C
ATOM 303 CA BVAL A 33 -33.214 -34.087 12.444 0.38 9.98 A C
ANISOU 303 CA BVAL A 33 1407 1257 1129 -169 -11 313 A C
ATOM 304 C AVAL A 33 -32.506 -35.272 13.103 0.62 10.18 A C
ANISOU 304 C AVAL A 33 1157 1462 1250 398 -385 -374 A C
ATOM 305 C BVAL A 33 -32.560 -35.283 13.114 0.38 10.38 A C
ANISOU 305 C BVAL A 33 1462 1384 1098 -6 -113 214 A C
ATOM 306 O AVAL A 33 -31.964 -35.184 14.209 0.62 12.16 A O
ANISOU 306 O AVAL A 33 1696 1419 1506 678 -535 -579 A O
ATOM 307 O BVAL A 33 -32.110 -35.203 14.262 0.38 12.92 A O
ANISOU 307 O BVAL A 33 2010 1483 1417 171 -512 236 A O
ATOM 308 CB AVAL A 33 -32.080 -33.143 11.865 0.62 10.80 A C
ANISOU 308 CB AVAL A 33 1513 1199 1393 259 -14 -54 A C
ATOM 309 CB BVAL A 33 -32.170 -33.246 11.674 0.38 11.02 A C
ANISOU 309 CB BVAL A 33 1566 1470 1150 -276 -15 120 A C
ATOM 310 CG1AVAL A 33 -31.406 -33.821 10.686 0.62 11.91 A C
ANISOU 310 CG1AVAL A 33 1676 1285 1562 177 432 -208 A C
ATOM 311 CG1BVAL A 33 -32.841 -32.086 10.953 0.38 11.68 A C
ANISOU 311 CG1BVAL A 33 1596 1841 999 -154 -5 -55 A C
ATOM 312 CG2AVAL A 33 -32.659 -31.797 11.453 0.62 11.35 A C
ANISOU 312 CG2AVAL A 33 1667 1331 1315 101 -353 -79 A C
ATOM 313 CG2BVAL A 33 -31.081 -32.743 12.604 0.38 11.21 A C
ANISOU 313 CG2BVAL A 33 1515 1655 1089 -333 -191 2 A C
ATOM 314 N ILE A 34 -32.515 -36.392 12.386 1.00 9.70 A N
ANISOU 314 N ILE A 34 1231 1298 1157 226 -164 -122 A N
ATOM 315 CA ILE A 34 -31.722 -37.560 12.740 1.00 9.97 A C
ANISOU 315 CA ILE A 34 1300 1251 1236 273 -154 -22 A C
ATOM 316 C ILE A 34 -30.529 -37.554 11.799 1.00 10.27 A C
ANISOU 316 C ILE A 34 1440 1361 1100 310 -120 -63 A C
ATOM 317 O ILE A 34 -30.711 -37.520 10.575 1.00 10.64 A O
ANISOU 317 O ILE A 34 1345 1535 1162 208 -166 4 A O
ATOM 318 CB ILE A 34 -32.532 -38.856 12.572 1.00 10.97 A C
ANISOU 318 CB ILE A 34 1507 1351 1312 140 -155 30 A C
ATOM 319 CG1 ILE A 34 -33.804 -38.839 13.424 1.00 11.00 A C
ANISOU 319 CG1 ILE A 34 1446 1296 1436 79 -201 -14 A C
ATOM 320 CG2 ILE A 34 -31.659 -40.083 12.851 1.00 11.58 A C
ANISOU 320 CG2 ILE A 34 1622 1250 1527 167 -213 45 A C
ATOM 321 CD1 ILE A 34 -33.571 -38.568 14.897 1.00 11.46 A C
ANISOU 321 CD1 ILE A 34 1498 1461 1394 91 -41 -40 A C
ATOM 322 N VAL A 35 -29.319 -37.577 12.357 1.00 10.01 A N
ANISOU 322 N VAL A 35 1297 1356 1151 203 -159 -12 A N
ATOM 323 CA VAL A 35 -28.073 -37.503 11.601 1.00 9.97 A C
ANISOU 323 CA VAL A 35 1238 1279 1270 200 -95 -8 A C
ATOM 324 C VAL A 35 -27.299 -38.785 11.864 1.00 10.63 A C
ANISOU 324 C VAL A 35 1364 1448 1228 217 -138 -37 A C
ATOM 325 O VAL A 35 -26.993 -39.100 13.023 1.00 11.45 A O
ANISOU 325 O VAL A 35 1499 1664 1188 349 -211 133 A O
ATOM 326 CB VAL A 35 -27.227 -36.287 12.019 1.00 11.11 A C
ANISOU 326 CB VAL A 35 1393 1374 1453 69 -106 -49 A C
ATOM 327 CG1 VAL A 35 -25.902 -36.257 11.248 1.00 12.59 A C
ANISOU 327 CG1 VAL A 35 1297 1796 1691 65 22 -119 A C
ATOM 328 CG2 VAL A 35 -28.005 -34.987 11.836 1.00 11.98 A C
ANISOU 328 CG2 VAL A 35 1557 1415 1581 22 -115 16 A C
ATOM 329 N GLU A 36 -26.971 -39.521 10.802 1.00 10.35 A N
ANISOU 329 N GLU A 36 1241 1382 1309 282 -112 -22 A N
ATOM 330 CA GLU A 36 -26.175 -40.734 10.921 1.00 11.00 A C
ANISOU 330 CA GLU A 36 1321 1462 1395 241 4 93 A C
ATOM 331 C GLU A 36 -25.076 -40.748 9.872 1.00 11.01 A C
ANISOU 331 C GLU A 36 1311 1479 1392 316 27 247 A C
ATOM 332 O GLU A 36 -25.209 -40.158 8.798 1.00 11.67 A O
ANISOU 332 O GLU A 36 1356 1831 1248 319 77 287 A O
ATOM 333 CB GLU A 36 -27.038 -41.989 10.782 1.00 11.57 A C
ANISOU 333 CB GLU A 36 1535 1294 1568 161 126 115 A C
ATOM 334 CG GLU A 36 -27.944 -42.190 11.979 1.00 12.17 A C
ANISOU 334 CG GLU A 36 1606 1519 1498 106 259 64 A C
ATOM 335 CD GLU A 36 -28.703 -43.505 11.984 1.00 13.26 A C
ANISOU 335 CD GLU A 36 1763 1642 1631 229 164 43 A C
ATOM 336 OE1 GLU A 36 -28.222 -44.501 11.394 1.00 14.22 A O
ANISOU 336 OE1 GLU A 36 1826 1557 2019 194 53 -2 A O
ATOM 337 OE2 GLU A 36 -29.791 -43.536 12.599 1.00 13.84 A O
ANISOU 337 OE2 GLU A 36 1848 1677 1733 2 171 116 A O
ATOM 338 N ALYS A 37 -23.977 -41.413 10.208 0.52 11.87 A N
ANISOU 338 N ALYS A 37 1602 1531 1378 394 138 317 A N
ATOM 339 N BLYS A 37 -23.988 -41.440 10.194 0.48 11.94 A N
ANISOU 339 N BLYS A 37 1478 1583 1474 281 140 249 A N
ATOM 340 CA ALYS A 37 -22.899 -41.620 9.257 0.52 12.10 A C
ANISOU 340 CA ALYS A 37 1694 1560 1345 414 128 333 A C
ATOM 341 CA BLYS A 37 -22.883 -41.611 9.264 0.48 11.86 A C
ANISOU 341 CA BLYS A 37 1377 1594 1536 206 194 277 A C
ATOM 342 C ALYS A 37 -23.315 -42.690 8.254 0.52 13.61 A C
ANISOU 342 C ALYS A 37 2202 1634 1335 162 91 325 A C
ATOM 343 C BLYS A 37 -23.062 -42.893 8.462 0.48 13.08 A C
ANISOU 343 C BLYS A 37 1606 1865 1498 -167 354 267 A C
ATOM 344 O ALYS A 37 -23.807 -43.755 8.641 0.52 15.63 A O
ANISOU 344 O ALYS A 37 2714 1719 1505 -277 278 145 A O
ATOM 345 O BLYS A 37 -23.488 -43.922 8.995 0.48 15.18 A O
ANISOU 345 O BLYS A 37 2175 2060 1531 -338 75 109 A O
ATOM 346 CB ALYS A 37 -21.632 -42.050 9.996 0.52 12.25 A C
ANISOU 346 CB ALYS A 37 1681 1503 1469 639 248 202 A C
ATOM 347 CB BLYS A 37 -21.553 -41.673 10.017 0.48 12.04 A C
ANISOU 347 CB BLYS A 37 1399 1356 1818 429 164 229 A C
ATOM 348 CG ALYS A 37 -20.381 -42.019 9.127 0.52 14.20 A C
ANISOU 348 CG ALYS A 37 1988 1745 1662 811 296 299 A C
ATOM 349 CG BLYS A 37 -20.340 -41.581 9.095 0.48 12.91 A C
ANISOU 349 CG BLYS A 37 1469 1444 1994 237 285 140 A C
ATOM 350 CD ALYS A 37 -19.140 -42.371 9.920 0.52 17.76 A C
ANISOU 350 CD ALYS A 37 2302 2222 2222 828 224 612 A C
ATOM 351 CD BLYS A 37 -19.043 -41.829 9.836 0.48 12.65 A C
ANISOU 351 CD BLYS A 37 1439 1331 2035 154 171 346 A C
ATOM 352 CE ALYS A 37 -19.130 -43.841 10.292 0.52 20.77 A C
ANISOU 352 CE ALYS A 37 2902 2322 2666 832 213 945 A C
ATOM 353 CE BLYS A 37 -18.866 -43.307 10.139 0.48 13.86 A C
ANISOU 353 CE BLYS A 37 1489 1718 2060 -94 173 407 A C
ATOM 354 NZ ALYS A 37 -19.160 -44.706 9.087 0.52 23.05 A N
ANISOU 354 NZ ALYS A 37 3219 2163 3376 1059 501 803 A N
ATOM 355 NZ BLYS A 37 -17.583 -43.597 10.837 0.48 15.06 A N
ANISOU 355 NZ BLYS A 37 1620 2043 2057 96 -219 119 A N
ATOM 356 N AALA A 38 -23.137 -42.400 6.966 0.52 14.66 A N
ANISOU 356 N AALA A 38 2672 1561 1337 285 55 258 A N
ATOM 357 N BALA A 38 -22.734 -42.824 7.177 0.48 13.41 A N
ANISOU 357 N BALA A 38 1725 1879 1492 -169 253 82 A N
ATOM 358 CA AALA A 38 -23.469 -43.377 5.943 0.52 17.78 A C
ANISOU 358 CA AALA A 38 3505 1714 1534 108 -108 154 A C
ATOM 359 CA BALA A 38 -22.666 -44.029 6.366 0.48 13.74 A C
ANISOU 359 CA BALA A 38 2007 1843 1370 332 82 289 A C
ATOM 360 C AALA A 38 -22.643 -44.645 6.153 0.52 19.67 A C
ANISOU 360 C AALA A 38 4290 1635 1548 61 88 -59 A C
ATOM 361 C BALA A 38 -21.645 -44.981 6.987 0.48 13.44 A C
ANISOU 361 C BALA A 38 2137 1581 1389 107 77 134 A C
ATOM 362 O AALA A 38 -21.505 -44.584 6.628 0.52 18.39 A O
ANISOU 362 O AALA A 38 4279 1293 1417 303 137 -62 A O
ATOM 363 O BALA A 38 -20.543 -44.545 7.354 0.48 13.63 A O
ANISOU 363 O BALA A 38 2021 1585 1573 57 -47 58 A O
ATOM 364 CB AALA A 38 -23.184 -42.807 4.556 0.52 17.45 A C
ANISOU 364 CB AALA A 38 3580 1749 1301 184 -354 319 A C
ATOM 365 CB BALA A 38 -22.253 -43.669 4.941 0.48 14.87 A C
ANISOU 365 CB BALA A 38 1988 2130 1531 608 98 298 A C
ATOM 366 N APRO A 39 -23.195 -45.811 5.824 0.52 24.65 A N
ANISOU 366 N APRO A 39 5012 1988 2366 -105 95 112 A N
ATOM 367 N BPRO A 39 -21.966 -46.271 7.130 0.48 15.99 A N
ANISOU 367 N BPRO A 39 2672 1639 1767 3 -31 227 A N
ATOM 368 CA APRO A 39 -22.454 -47.059 6.045 0.52 26.76 A C
ANISOU 368 CA APRO A 39 5351 2061 2755 -86 315 144 A C
ATOM 369 CA BPRO A 39 -21.100 -47.152 7.936 0.48 17.37 A C
ANISOU 369 CA BPRO A 39 3094 1665 1843 159 22 370 A C
ATOM 370 C APRO A 39 -21.146 -47.080 5.266 0.52 27.00 A C
ANISOU 370 C APRO A 39 5441 2072 2745 152 554 -115 A C
ATOM 371 C BPRO A 39 -19.681 -47.268 7.410 0.48 18.32 A C
ANISOU 371 C BPRO A 39 3346 1570 2045 403 64 541 A C
ATOM 372 O APRO A 39 -21.112 -46.795 4.067 0.52 23.87 A O
ANISOU 372 O APRO A 39 5286 1744 2039 -97 486 -200 A O
ATOM 373 O BPRO A 39 -18.731 -47.336 8.200 0.48 18.09 A O
ANISOU 373 O BPRO A 39 3085 1753 2035 332 -225 829 A O
ATOM 374 CB APRO A 39 -23.426 -48.141 5.557 0.52 27.77 A C
ANISOU 374 CB APRO A 39 5442 2185 2923 -347 294 296 A C
ATOM 375 CB BPRO A 39 -21.844 -48.495 7.898 0.48 18.26 A C
ANISOU 375 CB BPRO A 39 3145 1909 1885 -79 -59 138 A C
ATOM 376 CG APRO A 39 -24.394 -47.427 4.672 0.52 28.72 A C
ANISOU 376 CG APRO A 39 5434 2401 3077 -298 245 149 A C
ATOM 377 CG BPRO A 39 -22.637 -48.440 6.634 0.48 18.44 A C
ANISOU 377 CG BPRO A 39 3038 1859 2109 -60 -196 129 A C
ATOM 378 CD APRO A 39 -24.530 -46.055 5.255 0.52 27.29 A C
ANISOU 378 CD APRO A 39 5281 2243 2844 -256 175 159 A C
ATOM 379 CD BPRO A 39 -23.079 -47.009 6.511 0.48 17.08 A C
ANISOU 379 CD BPRO A 39 2735 1660 2095 -29 -204 248 A C
ATOM 380 N ALYS A 40 -20.064 -47.397 5.978 0.52 29.00 A N
ANISOU 380 N ALYS A 40 5515 2330 3175 717 799 -88 A N
ATOM 381 N BLYS A 40 -19.509 -47.285 6.091 0.48 21.48 A N
ANISOU 381 N BLYS A 40 3958 1787 2414 597 616 483 A N
ATOM 382 CA ALYS A 40 -18.685 -47.561 5.503 0.52 30.90 A C
ANISOU 382 CA ALYS A 40 5485 2730 3525 1073 1208 -182 A C
ATOM 383 CA BLYS A 40 -18.188 -47.437 5.497 0.48 26.07 A C
ANISOU 383 CA BLYS A 40 4487 2347 3070 808 1069 204 A C
ATOM 384 C ALYS A 40 -17.898 -46.260 5.346 0.52 30.02 A C
ANISOU 384 C ALYS A 40 5312 2760 3334 1349 1534 33 A C
ATOM 385 C BLYS A 40 -17.389 -46.141 5.471 0.48 25.91 A C
ANISOU 385 C BLYS A 40 4525 2417 2901 1167 1440 179 A C
ATOM 386 O ALYS A 40 -16.748 -46.317 4.897 0.52 31.72 A O
ANISOU 386 O ALYS A 40 5374 3027 3652 1607 1595 -169 A O
ATOM 387 O BLYS A 40 -16.190 -46.180 5.176 0.48 27.36 A O
ANISOU 387 O BLYS A 40 4646 2543 3209 1230 1431 -262 A O
ATOM 388 CB ALYS A 40 -18.536 -48.420 4.233 0.52 32.56 A C
ANISOU 388 CB ALYS A 40 5482 2954 3934 1113 1203 -245 A C
ATOM 389 CB BLYS A 40 -18.302 -48.004 4.077 0.48 29.90 A C
ANISOU 389 CB BLYS A 40 4846 2775 3739 563 1124 120 A C
ATOM 390 CG ALYS A 40 -18.575 -49.927 4.469 0.52 34.42 A C
ANISOU 390 CG ALYS A 40 5519 3279 4280 881 1063 16 A C
ATOM 391 CG BLYS A 40 -18.492 -49.517 4.004 0.48 32.76 A C
ANISOU 391 CG BLYS A 40 5094 3147 4205 335 1083 291 A C
ATOM 392 CD ALYS A 40 -19.975 -50.420 4.802 0.52 34.75 A C
ANISOU 392 CD ALYS A 40 5498 3314 4393 797 1041 209 A C
ATOM 393 CD BLYS A 40 -19.877 -49.956 4.466 0.48 33.98 A C
ANISOU 393 CD BLYS A 40 5178 3388 4345 295 1140 342 A C
ATOM 394 N AALA A 41 -18.456 -45.103 5.696 0.52 26.75 A N
ANISOU 394 N AALA A 41 4895 2418 2853 1354 1680 361 A N
ATOM 395 N BALA A 41 -18.012 -45.003 5.770 0.48 23.57 A N
ANISOU 395 N BALA A 41 4311 2159 2486 1332 1548 605 A N
ATOM 396 CA AALA A 41 -17.705 -43.861 5.568 0.52 26.30 A C
ANISOU 396 CA AALA A 41 4678 2400 2916 1224 1757 522 A C
ATOM 397 CA BALA A 41 -17.295 -43.737 5.734 0.48 24.45 A C
ANISOU 397 CA BALA A 41 4306 2256 2727 1261 1601 613 A C
ATOM 398 C AALA A 41 -16.547 -43.844 6.559 0.52 25.63 A C
ANISOU 398 C AALA A 41 4064 2472 3203 1234 1921 698 A C
ATOM 399 C BALA A 41 -16.242 -43.706 6.833 0.48 25.32 A C
ANISOU 399 C BALA A 41 3954 2509 3157 1267 1833 671 A C
ATOM 400 O AALA A 41 -16.683 -44.294 7.700 0.52 26.42 A O
ANISOU 400 O AALA A 41 3883 2980 3174 1521 1847 1073 A O
ATOM 401 O BALA A 41 -16.556 -43.868 8.016 0.48 26.61 A O
ANISOU 401 O BALA A 41 3906 2995 3210 1422 1836 947 A O
ATOM 402 CB AALA A 41 -18.622 -42.663 5.811 0.52 25.46 A C
ANISOU 402 CB AALA A 41 4795 2133 2747 1255 1603 695 A C
ATOM 403 CB BALA A 41 -18.274 -42.577 5.909 0.48 24.42 A C
ANISOU 403 CB BALA A 41 4460 2142 2674 1244 1531 592 A C
ATOM 404 N AARG A 42 -15.399 -43.328 6.116 0.52 25.14 A N
ANISOU 404 N AARG A 42 3994 2132 3428 894 2091 583 A N
ATOM 405 N BARG A 42 -14.988 -43.496 6.440 0.48 25.84 A N
ANISOU 405 N BARG A 42 3969 2318 3531 1155 1775 441 A N
ATOM 406 CA AARG A 42 -14.182 -43.394 6.918 0.52 25.36 A C
ANISOU 406 CA AARG A 42 3821 2021 3796 589 1981 99 A C
ATOM 407 CA BARG A 42 -13.876 -43.528 7.381 0.48 27.90 A C
ANISOU 407 CA BARG A 42 4203 2433 3966 923 1632 14 A C
ATOM 408 C AARG A 42 -13.820 -42.054 7.551 0.52 24.51 A C
ANISOU 408 C AARG A 42 3266 2354 3691 643 1732 -125 A C
ATOM 409 C BARG A 42 -13.722 -42.235 8.168 0.48 28.48 A C
ANISOU 409 C BARG A 42 4212 2740 3869 721 1410 -100 A C
ATOM 410 O AARG A 42 -12.681 -41.589 7.435 0.52 26.19 A O
ANISOU 410 O AARG A 42 3260 2833 3860 712 1752 -181 A O
ATOM 411 O BARG A 42 -12.664 -42.015 8.766 0.48 30.83 A O
ANISOU 411 O BARG A 42 4564 3049 4100 603 1112 -255 A O
ATOM 412 CB AARG A 42 -13.023 -43.952 6.092 0.52 26.05 A C
ANISOU 412 CB AARG A 42 3933 1913 4052 361 2102 127 A C
ATOM 413 CB BARG A 42 -12.572 -43.879 6.657 0.48 29.21 A C
ANISOU 413 CB BARG A 42 4357 2370 4371 814 1795 -123 A C
ATOM 414 CG AARG A 42 -13.267 -45.356 5.564 0.52 25.58 A C
ANISOU 414 CG AARG A 42 3926 1725 4069 133 2069 443 A C
ATOM 415 CG BARG A 42 -12.635 -45.197 5.904 0.48 30.08 A C
ANISOU 415 CG BARG A 42 4546 2270 4615 617 1836 -53 A C
ATOM 416 CD AARG A 42 -13.471 -46.353 6.699 0.52 27.20 A C
ANISOU 416 CD AARG A 42 4163 1821 4350 16 1661 753 A C
ATOM 417 CD BARG A 42 -13.285 -46.273 6.759 0.48 31.56 A C
ANISOU 417 CD BARG A 42 4809 2262 4919 450 1711 159 A C
ATOM 418 NE AARG A 42 -13.771 -47.690 6.198 0.52 29.69 A N
ANISOU 418 NE AARG A 42 4553 2091 4638 15 1362 941 A N
ATOM 419 NE BARG A 42 -13.538 -47.497 6.010 0.48 33.01 A N
ANISOU 419 NE BARG A 42 5023 2395 5124 256 1640 367 A N
ATOM 420 CZ AARG A 42 -14.767 -48.453 6.631 0.52 31.18 A C
ANISOU 420 CZ AARG A 42 4774 2469 4604 23 1246 1106 A C
ATOM 421 CZ BARG A 42 -14.257 -48.515 6.465 0.48 34.24 A C
ANISOU 421 CZ BARG A 42 5171 2596 5243 131 1548 470 A C
ATOM 422 NH1AARG A 42 -15.569 -48.057 7.607 0.52 31.66 A N
ANISOU 422 NH1AARG A 42 4863 2652 4513 -61 1274 1315 A N
ATOM 423 NH1BARG A 42 -14.821 -48.482 7.662 0.48 34.14 A N
ANISOU 423 NH1BARG A 42 5196 2560 5214 97 1550 661 A N
ATOM 424 NH2AARG A 42 -14.956 -49.648 6.080 0.52 32.15 A N
ANISOU 424 NH2AARG A 42 4881 2742 4592 -32 1180 1034 A N
ATOM 425 NH2BARG A 42 -14.415 -49.591 5.700 0.48 35.10 A N
ANISOU 425 NH2BARG A 42 5233 2794 5309 24 1475 407 A N
ATOM 426 N AILE A 43 -14.782 -41.435 8.232 0.52 20.46 A N
ANISOU 426 N AILE A 43 2556 2064 3153 840 1270 90 A N
ATOM 427 N BILE A 43 -14.745 -41.383 8.181 0.48 26.44 A N
ANISOU 427 N BILE A 43 3845 2591 3612 889 1455 121 A N
ATOM 428 CA AILE A 43 -14.577 -40.198 8.974 0.52 17.86 A C
ANISOU 428 CA AILE A 43 1936 1938 2912 443 999 154 A C
ATOM 429 CA BILE A 43 -14.701 -40.126 8.920 0.48 24.37 A C
ANISOU 429 CA BILE A 43 3429 2444 3386 902 1296 350 A C
ATOM 430 C AILE A 43 -15.258 -40.333 10.331 0.52 18.10 A C
ANISOU 430 C AILE A 43 1760 1914 3203 477 984 371 A C
ATOM 431 C BILE A 43 -15.232 -40.335 10.331 0.48 21.59 A C
ANISOU 431 C BILE A 43 2681 2195 3329 829 1082 535 A C
ATOM 432 O AILE A 43 -15.902 -41.342 10.627 0.52 18.46 A O
ANISOU 432 O AILE A 43 1840 1789 3386 344 860 155 A O
ATOM 433 O BILE A 43 -15.745 -41.410 10.666 0.48 21.40 A O
ANISOU 433 O BILE A 43 2768 2039 3323 869 1012 600 A O
ATOM 434 CB AILE A 43 -15.077 -38.956 8.208 0.52 14.93 A C
ANISOU 434 CB AILE A 43 1346 2067 2260 51 482 -113 A C
ATOM 435 CB BILE A 43 -15.463 -39.004 8.191 0.48 25.85 A C
ANISOU 435 CB BILE A 43 3663 2900 3258 720 1146 292 A C
ATOM 436 CG1AILE A 43 -16.488 -39.198 7.674 0.52 14.39 A C
ANISOU 436 CG1AILE A 43 924 2598 1944 90 165 -158 A C
ATOM 437 CG1BILE A 43 -16.891 -39.446 7.870 0.48 26.14 A C
ANISOU 437 CG1BILE A 43 3762 3056 3113 709 821 186 A C
ATOM 438 CG2AILE A 43 -14.134 -38.605 7.071 0.52 14.66 A C
ANISOU 438 CG2AILE A 43 1342 2217 2009 151 215 -384 A C
ATOM 439 CG2BILE A 43 -14.721 -38.587 6.930 0.48 26.21 A C
ANISOU 439 CG2BILE A 43 3641 3068 3252 648 1222 306 A C
ATOM 440 CD1AILE A 43 -17.156 -37.967 7.058 0.52 14.67 A C
ANISOU 440 CD1AILE A 43 914 2761 1899 428 -143 -646 A C
ATOM 441 CD1BILE A 43 -17.685 -38.412 7.105 0.48 25.73 A C
ANISOU 441 CD1BILE A 43 3715 3017 3043 781 768 23 A C
ATOM 442 N GLY A 44 -15.115 -39.302 11.160 1.00 19.84 A N
ANISOU 442 N GLY A 44 2005 2259 3273 749 979 384 A N
ATOM 443 CA GLY A 44 -15.472 -39.424 12.558 1.00 18.59 A C
ANISOU 443 CA GLY A 44 1797 2328 2936 665 324 512 A C
ATOM 444 C GLY A 44 -16.956 -39.602 12.815 1.00 14.75 A C
ANISOU 444 C GLY A 44 1586 1784 2236 664 118 236 A C
ATOM 445 O GLY A 44 -17.826 -39.268 12.004 1.00 15.65 A O
ANISOU 445 O GLY A 44 1823 2008 2116 625 251 462 A O
ATOM 446 N ASP A 45 -17.227 -40.108 14.014 1.00 13.96 A N
ANISOU 446 N ASP A 45 1646 1762 1895 465 -17 100 A N
ATOM 447 CA ASP A 45 -18.568 -40.368 14.511 1.00 13.10 A C
ANISOU 447 CA ASP A 45 1667 1601 1708 369 -26 0 A C
ATOM 448 C ASP A 45 -18.997 -39.308 15.514 1.00 12.46 A C
ANISOU 448 C ASP A 45 1501 1577 1657 270 -91 -218 A C
ATOM 449 O ASP A 45 -18.200 -38.845 16.332 1.00 13.91 A O
ANISOU 449 O ASP A 45 1507 1909 1868 363 -112 -453 A O
ATOM 450 CB ASP A 45 -18.585 -41.700 15.256 1.00 15.07 A C
ANISOU 450 CB ASP A 45 2081 1692 1951 585 44 29 A C
ATOM 451 CG ASP A 45 -18.160 -42.851 14.389 1.00 18.69 A C
ANISOU 451 CG ASP A 45 2443 2264 2392 835 -301 -265 A C
ATOM 452 OD1 ASP A 45 -18.758 -43.020 13.315 1.00 19.30 A O
ANISOU 452 OD1 ASP A 45 2527 2340 2465 529 -306 -632 A O
ATOM 453 OD2 ASP A 45 -17.227 -43.588 14.772 1.00 23.18 A O
ANISOU 453 OD2 ASP A 45 3233 2652 2921 1192 -660 -567 A O
ATOM 454 N LEU A 46 -20.280 -38.971 15.477 1.00 11.64 A N
ANISOU 454 N LEU A 46 1449 1493 1481 318 -59 -104 A N
ATOM 455 CA LEU A 46 -20.911 -38.192 16.529 1.00 10.74 A C
ANISOU 455 CA LEU A 46 1421 1320 1338 317 -73 -87 A C
ATOM 456 C LEU A 46 -21.343 -39.128 17.660 1.00 11.07 A C
ANISOU 456 C LEU A 46 1511 1303 1392 185 -217 -208 A C
ATOM 457 O LEU A 46 -21.413 -40.348 17.494 1.00 13.15 A O
ANISOU 457 O LEU A 46 2255 1220 1521 215 -90 -166 A O
ATOM 458 CB LEU A 46 -22.129 -37.460 15.966 1.00 10.87 A C
ANISOU 458 CB LEU A 46 1479 1271 1382 202 -184 -79 A C
ATOM 459 CG LEU A 46 -21.838 -36.530 14.789 1.00 10.99 A C
ANISOU 459 CG LEU A 46 1539 1276 1361 182 -167 -167 A C
ATOM 460 CD1 LEU A 46 -23.123 -35.978 14.200 1.00 12.41 A C
ANISOU 460 CD1 LEU A 46 1701 1505 1509 261 -263 -76 A C
ATOM 461 CD2 LEU A 46 -20.884 -35.415 15.196 1.00 12.46 A C
ANISOU 461 CD2 LEU A 46 1584 1398 1752 -34 -233 -16 A C
ATOM 462 N ASP A 47 -21.643 -38.548 18.824 1.00 10.57 A N
ANISOU 462 N ASP A 47 1419 1263 1335 153 -218 -138 A N
ATOM 463 CA ASP A 47 -22.099 -39.332 19.967 1.00 10.89 A C
ANISOU 463 CA ASP A 47 1416 1311 1409 139 -196 -55 A C
ATOM 464 C ASP A 47 -23.610 -39.381 20.089 1.00 11.90 A C
ANISOU 464 C ASP A 47 1388 1680 1454 -4 -386 112 A C
ATOM 465 O ASP A 47 -24.123 -40.116 20.940 1.00 14.47 A O
ANISOU 465 O ASP A 47 1488 2181 1829 -64 -519 519 A O
ATOM 466 CB ASP A 47 -21.512 -38.775 21.266 1.00 10.81 A C
ANISOU 466 CB ASP A 47 1430 1344 1332 154 -311 -190 A C
ATOM 467 CG ASP A 47 -20.007 -38.821 21.276 1.00 10.71 A C
ANISOU 467 CG ASP A 47 1437 1264 1369 242 -360 -88 A C
ATOM 468 OD1 ASP A 47 -19.425 -39.855 20.878 1.00 12.68 A O
ANISOU 468 OD1 ASP A 47 1494 1551 1773 277 -384 -321 A O
ATOM 469 OD2 ASP A 47 -19.406 -37.806 21.689 1.00 10.71 A O
ANISOU 469 OD2 ASP A 47 1316 1279 1473 130 -210 -132 A O
ATOM 470 N LYS A 48 -24.322 -38.612 19.273 1.00 10.99 A N
ANISOU 470 N LYS A 48 1293 1540 1344 123 -365 -20 A N
ATOM 471 CA LYS A 48 -25.772 -38.568 19.262 1.00 11.48 A C
ANISOU 471 CA LYS A 48 1411 1634 1315 130 -381 -139 A C
ATOM 472 C LYS A 48 -26.233 -38.709 17.820 1.00 11.03 A C
ANISOU 472 C LYS A 48 1387 1390 1413 110 -304 -59 A C
ATOM 473 O LYS A 48 -25.451 -38.535 16.882 1.00 11.41 A O
ANISOU 473 O LYS A 48 1455 1516 1365 145 -341 -250 A O
ATOM 474 CB LYS A 48 -26.276 -37.233 19.829 1.00 12.83 A C
ANISOU 474 CB LYS A 48 1519 2057 1298 302 -367 -459 A C
ATOM 475 CG LYS A 48 -25.876 -36.990 21.266 1.00 16.28 A C
ANISOU 475 CG LYS A 48 1861 2746 1577 63 -189 -461 A C
ATOM 476 CD LYS A 48 -26.577 -37.953 22.199 1.00 19.27 A C
ANISOU 476 CD LYS A 48 2342 3171 1809 26 -363 -204 A C
ATOM 477 CE LYS A 48 -26.151 -37.733 23.632 1.00 23.85 A C
ANISOU 477 CE LYS A 48 2995 3518 2549 221 -138 -190 A C
ATOM 478 NZ LYS A 48 -26.319 -36.307 23.985 1.00 25.12 A N
ANISOU 478 NZ LYS A 48 3110 3602 2831 637 163 -370 A N
ATOM 479 N LYS A 49 -27.524 -39.005 17.662 1.00 10.81 A N
ANISOU 479 N LYS A 49 1409 1341 1357 163 -340 -42 A N
ATOM 480 CA LYS A 49 -28.191 -39.020 16.368 1.00 11.14 A C
ANISOU 480 CA LYS A 49 1559 1359 1313 171 -445 -106 A C
ATOM 481 C LYS A 49 -29.242 -37.931 16.237 1.00 11.00 A C
ANISOU 481 C LYS A 49 1366 1508 1307 112 -258 -77 A C
ATOM 482 O LYS A 49 -29.469 -37.427 15.138 1.00 11.56 A O
ANISOU 482 O LYS A 49 1499 1662 1232 283 -275 -47 A O
ATOM 483 CB LYS A 49 -28.869 -40.377 16.130 1.00 12.79 A C
ANISOU 483 CB LYS A 49 1670 1427 1762 138 -332 -188 A C
ATOM 484 CG LYS A 49 -27.892 -41.526 15.953 1.00 13.46 A C
ANISOU 484 CG LYS A 49 1658 1240 2217 142 -296 -212 A C
ATOM 485 CD LYS A 49 -28.626 -42.856 15.841 1.00 15.47 A C
ANISOU 485 CD LYS A 49 1800 1492 2587 131 -355 -429 A C
ATOM 486 CE LYS A 49 -27.693 -43.994 15.458 1.00 16.66 A C
ANISOU 486 CE LYS A 49 1923 1678 2729 211 -510 -311 A C
ATOM 487 NZ LYS A 49 -26.604 -44.146 16.456 1.00 16.99 A N
ANISOU 487 NZ LYS A 49 2251 1573 2632 340 -229 -38 A N
ATOM 488 N LYS A 50 -29.874 -37.541 17.328 1.00 10.73 A N
ANISOU 488 N LYS A 50 1411 1288 1377 139 -175 6 A N
ATOM 489 CA LYS A 50 -31.003 -36.629 17.288 1.00 10.92 A C
ANISOU 489 CA LYS A 50 1286 1442 1422 113 11 42 A C
ATOM 490 C LYS A 50 -30.527 -35.214 17.608 1.00 10.35 A C
ANISOU 490 C LYS A 50 1367 1356 1211 337 -215 -110 A C
ATOM 491 O LYS A 50 -29.928 -34.979 18.665 1.00 11.90 A O
ANISOU 491 O LYS A 50 1715 1529 1276 408 -400 -122 A O
ATOM 492 CB LYS A 50 -32.036 -37.125 18.298 1.00 15.10 A C
ANISOU 492 CB LYS A 50 1645 2202 1889 407 45 237 A C
ATOM 493 CG LYS A 50 -33.342 -36.400 18.283 1.00 15.81 A C
ANISOU 493 CG LYS A 50 1957 2098 1953 244 283 153 A C
ATOM 494 CD LYS A 50 -34.394 -37.071 19.176 1.00 16.91 A C
ANISOU 494 CD LYS A 50 1953 2213 2258 250 513 242 A C
ATOM 495 CE LYS A 50 -33.989 -37.102 20.645 1.00 17.70 A C
ANISOU 495 CE LYS A 50 1862 2395 2470 403 721 879 A C
ATOM 496 NZ LYS A 50 -34.987 -37.796 21.518 1.00 18.69 A N
ANISOU 496 NZ LYS A 50 2015 2405 2682 339 547 776 A N
ATOM 497 N TYR A 51 -30.809 -34.280 16.696 1.00 9.98 A N
ANISOU 497 N TYR A 51 1309 1222 1261 314 -113 -187 A N
ATOM 498 CA TYR A 51 -30.438 -32.876 16.800 1.00 9.52 A C
ANISOU 498 CA TYR A 51 1238 1203 1176 332 -228 -232 A C
ATOM 499 C TYR A 51 -31.664 -32.019 16.520 1.00 10.04 A C
ANISOU 499 C TYR A 51 1230 1314 1270 170 -269 -263 A C
ATOM 500 O TYR A 51 -32.631 -32.465 15.898 1.00 10.60 A O
ANISOU 500 O TYR A 51 1203 1294 1530 206 -369 -378 A O
ATOM 501 CB TYR A 51 -29.299 -32.541 15.813 1.00 9.99 A C
ANISOU 501 CB TYR A 51 1303 1283 1211 307 -170 -211 A C
ATOM 502 CG TYR A 51 -28.031 -33.277 16.177 1.00 9.56 A C
ANISOU 502 CG TYR A 51 1065 1299 1268 233 -73 -212 A C
ATOM 503 CD1 TYR A 51 -27.119 -32.704 17.052 1.00 10.18 A C
ANISOU 503 CD1 TYR A 51 1100 1360 1409 75 -209 -183 A C
ATOM 504 CD2 TYR A 51 -27.773 -34.568 15.711 1.00 9.86 A C
ANISOU 504 CD2 TYR A 51 1149 1257 1340 208 -130 -168 A C
ATOM 505 CE1 TYR A 51 -25.965 -33.377 17.438 1.00 10.26 A C
ANISOU 505 CE1 TYR A 51 1161 1317 1421 128 -215 -256 A C
ATOM 506 CE2 TYR A 51 -26.625 -35.251 16.092 1.00 9.68 A C
ANISOU 506 CE2 TYR A 51 1276 1191 1213 132 -144 -109 A C
ATOM 507 CZ TYR A 51 -25.728 -34.657 16.962 1.00 10.31 A C
ANISOU 507 CZ TYR A 51 1252 1345 1319 274 -201 -216 A C
ATOM 508 OH TYR A 51 -24.599 -35.347 17.340 1.00 10.90 A O
ANISOU 508 OH TYR A 51 1214 1426 1500 366 -344 -222 A O
ATOM 509 N LEU A 52 -31.629 -30.779 16.996 1.00 9.22 A N
ANISOU 509 N LEU A 52 1149 1214 1139 189 -212 -134 A N
ATOM 510 CA LEU A 52 -32.728 -29.837 16.789 1.00 9.26 A C
ANISOU 510 CA LEU A 52 1018 1226 1275 240 -44 -79 A C
ATOM 511 C LEU A 52 -32.101 -28.543 16.283 1.00 9.00 A C
ANISOU 511 C LEU A 52 1054 1160 1204 61 -74 -40 A C
ATOM 512 O LEU A 52 -31.485 -27.802 17.058 1.00 10.03 A O
ANISOU 512 O LEU A 52 1321 1216 1273 -29 -187 -128 A O
ATOM 513 CB LEU A 52 -33.519 -29.635 18.074 1.00 9.47 A C
ANISOU 513 CB LEU A 52 1164 1262 1170 190 -12 -105 A C
ATOM 514 CG LEU A 52 -34.778 -28.777 17.896 1.00 10.01 A C
ANISOU 514 CG LEU A 52 1216 1405 1183 154 20 -162 A C
ATOM 515 CD1 LEU A 52 -35.805 -29.457 16.983 1.00 10.69 A C
ANISOU 515 CD1 LEU A 52 1107 1634 1319 74 -8 -259 A C
ATOM 516 CD2 LEU A 52 -35.396 -28.461 19.239 1.00 10.85 A C
ANISOU 516 CD2 LEU A 52 1253 1520 1348 129 63 -17 A C
ATOM 517 N VAL A 53 -32.238 -28.289 14.985 1.00 9.13 A N
ANISOU 517 N VAL A 53 1066 1268 1135 134 -94 -29 A N
ATOM 518 CA VAL A 53 -31.420 -27.279 14.318 1.00 9.45 A C
ANISOU 518 CA VAL A 53 1045 1329 1218 114 -117 -68 A C
ATOM 519 C VAL A 53 -32.273 -26.090 13.896 1.00 9.31 A C
ANISOU 519 C VAL A 53 1017 1400 1122 51 -73 -113 A C
ATOM 520 O VAL A 53 -33.482 -26.240 13.660 1.00 9.62 A O
ANISOU 520 O VAL A 53 1104 1338 1213 81 -65 -69 A O
ATOM 521 CB VAL A 53 -30.667 -27.880 13.120 1.00 10.43 A C
ANISOU 521 CB VAL A 53 1272 1306 1386 279 -31 -150 A C
ATOM 522 CG1 VAL A 53 -29.894 -29.119 13.555 1.00 11.23 A C
ANISOU 522 CG1 VAL A 53 1319 1463 1485 381 -126 -195 A C
ATOM 523 CG2 VAL A 53 -31.621 -28.214 11.977 1.00 11.15 A C
ANISOU 523 CG2 VAL A 53 1427 1489 1320 60 -146 -195 A C
ATOM 524 N PRO A 54 -31.693 -24.900 13.771 1.00 9.27 A N
ANISOU 524 N PRO A 54 1133 1230 1158 62 -111 -165 A N
ATOM 525 CA PRO A 54 -32.482 -23.756 13.302 1.00 9.61 A C
ANISOU 525 CA PRO A 54 1246 1231 1173 234 -218 -139 A C
ATOM 526 C PRO A 54 -33.005 -23.994 11.898 1.00 9.42 A C
ANISOU 526 C PRO A 54 1221 1166 1194 198 -113 -63 A C
ATOM 527 O PRO A 54 -32.293 -24.492 11.029 1.00 9.60 A O
ANISOU 527 O PRO A 54 1198 1247 1202 194 -10 -80 A O
ATOM 528 CB PRO A 54 -31.479 -22.596 13.330 1.00 10.12 A C
ANISOU 528 CB PRO A 54 1249 1243 1355 53 -191 -225 A C
ATOM 529 CG PRO A 54 -30.442 -23.027 14.326 1.00 10.34 A C
ANISOU 529 CG PRO A 54 1260 1215 1455 8 -234 -162 A C
ATOM 530 CD PRO A 54 -30.320 -24.507 14.138 1.00 10.05 A C
ANISOU 530 CD PRO A 54 1181 1230 1407 -51 -126 -167 A C
ATOM 531 N ASER A 55 -34.257 -23.602 11.665 0.56 9.25 A N
ANISOU 531 N ASER A 55 1160 1219 1136 219 -255 -110 A N
ATOM 532 N BSER A 55 -34.272 -23.632 11.690 0.44 10.37 A N
ANISOU 532 N BSER A 55 1346 1336 1258 180 -175 -75 A N
ATOM 533 CA ASER A 55 -34.806 -23.721 10.320 0.56 9.42 A C
ANISOU 533 CA ASER A 55 1152 1294 1133 302 -189 -86 A C
ATOM 534 CA BSER A 55 -34.854 -23.674 10.358 0.44 12.24 A C
ANISOU 534 CA BSER A 55 1607 1630 1414 375 -166 -144 A C
ATOM 535 C ASER A 55 -33.984 -22.945 9.299 0.56 9.47 A C
ANISOU 535 C ASER A 55 1309 1102 1186 298 -331 -47 A C
ATOM 536 C BSER A 55 -34.089 -22.807 9.369 0.44 11.58 A C
ANISOU 536 C BSER A 55 1658 1385 1356 266 -125 -3 A C
ATOM 537 O ASER A 55 -33.848 -23.385 8.152 0.56 9.11 A O
ANISOU 537 O ASER A 55 1260 1088 1112 211 -182 -85 A O
ATOM 538 O BSER A 55 -34.158 -23.054 8.160 0.44 12.09 A O
ANISOU 538 O BSER A 55 1931 1350 1311 498 -190 74 A O
ATOM 539 CB ASER A 55 -36.264 -23.276 10.314 0.56 9.56 A C
ANISOU 539 CB ASER A 55 929 1457 1245 110 -108 102 A C
ATOM 540 CB BSER A 55 -36.305 -23.208 10.434 0.44 15.17 A C
ANISOU 540 CB BSER A 55 1911 2125 1727 575 -344 -254 A C
ATOM 541 OG ASER A 55 -37.018 -24.137 11.146 0.56 10.23 A O
ANISOU 541 OG ASER A 55 972 1570 1344 -41 -161 -25 A O
ATOM 542 OG BSER A 55 -36.893 -23.174 9.152 0.44 18.15 A O
ANISOU 542 OG BSER A 55 2392 2433 2070 677 -340 -495 A O
ATOM 543 N AASP A 56 -33.414 -21.807 9.685 0.56 10.05 A N
ANISOU 543 N AASP A 56 1397 1187 1235 418 -419 -67 A N
ATOM 544 N BASP A 56 -33.364 -21.801 9.849 0.44 10.46 A N
ANISOU 544 N BASP A 56 1335 1361 1276 -120 101 -57 A N
ATOM 545 CA AASP A 56 -32.667 -21.010 8.722 0.56 12.21 A C
ANISOU 545 CA AASP A 56 1727 1196 1717 474 -325 -142 A C
ATOM 546 CA BASP A 56 -32.633 -20.889 8.979 0.44 10.66 A C
ANISOU 546 CA BASP A 56 1429 1431 1191 -124 21 -38 A C
ATOM 547 C AASP A 56 -31.194 -21.394 8.601 0.56 12.43 A C
ANISOU 547 C AASP A 56 1654 1266 1802 344 -243 -11 A C
ATOM 548 C BASP A 56 -31.186 -21.308 8.731 0.44 10.89 A C
ANISOU 548 C BASP A 56 1427 1460 1251 -18 -15 101 A C
ATOM 549 O AASP A 56 -30.481 -20.770 7.808 0.56 13.90 A O
ANISOU 549 O AASP A 56 1815 1446 2020 197 -269 70 A O
ATOM 550 O BASP A 56 -30.493 -20.636 7.961 0.44 11.45 A O
ANISOU 550 O BASP A 56 1444 1659 1249 -68 59 415 A O
ATOM 551 CB AASP A 56 -32.842 -19.505 8.970 0.56 14.18 A C
ANISOU 551 CB AASP A 56 2199 1281 1907 589 -531 -302 A C
ATOM 552 CB BASP A 56 -32.685 -19.461 9.535 0.44 12.65 A C
ANISOU 552 CB BASP A 56 1659 1536 1610 -16 111 120 A C
ATOM 553 CG AASP A 56 -32.283 -19.050 10.302 0.56 15.37 A C
ANISOU 553 CG AASP A 56 2373 1371 2094 212 -531 -226 A C
ATOM 554 CG BASP A 56 -34.075 -18.847 9.446 0.44 15.85 A C
ANISOU 554 CG BASP A 56 2169 1779 2073 221 -25 43 A C
ATOM 555 OD1AASP A 56 -31.598 -19.840 10.982 0.56 15.40 A O
ANISOU 555 OD1AASP A 56 2220 1531 2099 148 -557 -239 A O
ATOM 556 OD1BASP A 56 -34.908 -19.346 8.659 0.44 17.40 A O
ANISOU 556 OD1BASP A 56 2083 2176 2352 481 -24 46 A O
ATOM 557 OD2AASP A 56 -32.522 -17.877 10.661 0.56 17.18 A O
ANISOU 557 OD2AASP A 56 2892 1460 2175 243 -623 -377 A O
ATOM 558 OD2BASP A 56 -34.331 -17.856 10.160 0.44 18.04 A O
ANISOU 558 OD2BASP A 56 2515 1891 2450 228 -5 -86 A O
ATOM 559 N LEU A 57 -30.722 -22.391 9.351 1.00 10.99 A N
ANISOU 559 N LEU A 57 1328 1439 1409 207 -81 16 A N
ATOM 560 CA LEU A 57 -29.369 -22.891 9.134 1.00 10.82 A C
ANISOU 560 CA LEU A 57 1317 1514 1281 230 -19 123 A C
ATOM 561 C LEU A 57 -29.260 -23.475 7.726 1.00 10.55 A C
ANISOU 561 C LEU A 57 1300 1583 1124 238 -53 134 A C
ATOM 562 O LEU A 57 -30.132 -24.230 7.291 1.00 11.92 A O
ANISOU 562 O LEU A 57 1314 1928 1285 -0 -141 -78 A O
ATOM 563 CB LEU A 57 -29.095 -24.005 10.148 1.00 11.04 A C
ANISOU 563 CB LEU A 57 1362 1583 1248 317 51 101 A C
ATOM 564 CG LEU A 57 -27.669 -24.571 10.186 1.00 10.74 A C
ANISOU 564 CG LEU A 57 1274 1587 1221 236 -26 -10 A C
ATOM 565 CD1 LEU A 57 -26.741 -23.656 10.977 1.00 11.87 A C
ANISOU 565 CD1 LEU A 57 1393 1849 1266 132 -135 -211 A C
ATOM 566 CD2 LEU A 57 -27.670 -25.980 10.759 1.00 11.85 A C
ANISOU 566 CD2 LEU A 57 1385 1622 1495 371 -102 58 A C
ATOM 567 N THR A 58 -28.173 -23.168 7.021 1.00 10.97 A N
ANISOU 567 N THR A 58 1329 1649 1190 153 -30 129 A N
ATOM 568 CA THR A 58 -27.991 -23.763 5.702 1.00 11.11 A C
ANISOU 568 CA THR A 58 1447 1570 1204 129 11 98 A C
ATOM 569 C THR A 58 -27.213 -25.070 5.791 1.00 10.42 A C
ANISOU 569 C THR A 58 1310 1516 1134 121 -69 5 A C
ATOM 570 O THR A 58 -26.504 -25.337 6.766 1.00 10.73 A O
ANISOU 570 O THR A 58 1405 1600 1072 177 11 13 A O
ATOM 571 CB THR A 58 -27.246 -22.827 4.754 1.00 11.76 A C
ANISOU 571 CB THR A 58 1608 1571 1290 100 -58 134 A C
ATOM 572 CG2 THR A 58 -27.973 -21.494 4.593 1.00 14.30 A C
ANISOU 572 CG2 THR A 58 1801 1860 1772 197 50 324 A C
ATOM 573 OG1 THR A 58 -25.920 -22.623 5.254 1.00 12.28 A O
ANISOU 573 OG1 THR A 58 1540 1691 1436 -4 50 152 A O
ATOM 574 N VAL A 59 -27.336 -25.877 4.732 1.00 11.05 A N
ANISOU 574 N VAL A 59 1473 1593 1134 36 -117 81 A N
ATOM 575 CA VAL A 59 -26.496 -27.064 4.591 1.00 11.26 A C
ANISOU 575 CA VAL A 59 1428 1666 1183 21 -134 -65 A C
ATOM 576 C VAL A 59 -25.029 -26.682 4.735 1.00 10.30 A C
ANISOU 576 C VAL A 59 1449 1442 1023 -22 -3 -118 A C
ATOM 577 O VAL A 59 -24.266 -27.344 5.441 1.00 10.99 A O
ANISOU 577 O VAL A 59 1534 1410 1231 112 -23 -123 A O
ATOM 578 CB VAL A 59 -26.794 -27.782 3.260 1.00 11.43 A C
ANISOU 578 CB VAL A 59 1557 1590 1197 -87 -143 -25 A C
ATOM 579 CG1 VAL A 59 -25.733 -28.851 2.965 1.00 12.39 A C
ANISOU 579 CG1 VAL A 59 1751 1703 1253 41 27 -110 A C
ATOM 580 CG2 VAL A 59 -28.192 -28.383 3.280 1.00 12.15 A C
ANISOU 580 CG2 VAL A 59 1759 1498 1359 -320 -332 98 A C
ATOM 581 N GLY A 60 -24.617 -25.595 4.072 1.00 10.85 A N
ANISOU 581 N GLY A 60 1458 1611 1054 -129 -2 -20 A N
ATOM 582 CA GLY A 60 -23.227 -25.167 4.164 1.00 11.70 A C
ANISOU 582 CA GLY A 60 1612 1637 1195 -31 1 13 A C
ATOM 583 C GLY A 60 -22.789 -24.855 5.585 1.00 10.78 A C
ANISOU 583 C GLY A 60 1414 1422 1261 -73 84 8 A C
ATOM 584 O GLY A 60 -21.679 -25.209 5.996 1.00 10.97 A O
ANISOU 584 O GLY A 60 1393 1537 1238 -35 34 -85 A O
ATOM 585 N GLN A 61 -23.653 -24.191 6.359 1.00 10.33 A N
ANISOU 585 N GLN A 61 1435 1314 1177 -12 20 -8 A N
ATOM 586 CA GLN A 61 -23.302 -23.934 7.754 1.00 10.39 A C
ANISOU 586 CA GLN A 61 1521 1249 1177 48 -29 -57 A C
ATOM 587 C GLN A 61 -23.220 -25.230 8.547 1.00 9.72 A C
ANISOU 587 C GLN A 61 1270 1306 1115 41 -22 -145 A C
ATOM 588 O GLN A 61 -22.364 -25.367 9.430 1.00 10.22 A O
ANISOU 588 O GLN A 61 1344 1440 1101 -22 -131 -83 A O
ATOM 589 CB GLN A 61 -24.333 -23.021 8.399 1.00 10.88 A C
ANISOU 589 CB GLN A 61 1655 1236 1241 94 71 -179 A C
ATOM 590 CG GLN A 61 -24.275 -21.590 7.951 1.00 12.32 A C
ANISOU 590 CG GLN A 61 1716 1205 1760 34 75 -77 A C
ATOM 591 CD GLN A 61 -25.411 -20.792 8.546 1.00 13.91 A C
ANISOU 591 CD GLN A 61 1946 1523 1817 160 -117 -261 A C
ATOM 592 NE2 GLN A 61 -25.073 -19.814 9.371 1.00 18.67 A N
ANISOU 592 NE2 GLN A 61 2449 2114 2530 358 -286 -831 A N
ATOM 593 OE1 GLN A 61 -26.583 -21.069 8.294 1.00 13.31 A O
ANISOU 593 OE1 GLN A 61 1712 1495 1850 220 55 -245 A O
ATOM 594 N PHE A 62 -24.112 -26.184 8.258 1.00 9.38 A N
ANISOU 594 N PHE A 62 1330 1174 1059 31 62 -37 A N
ATOM 595 CA PHE A 62 -24.063 -27.480 8.930 1.00 9.86 A C
ANISOU 595 CA PHE A 62 1294 1292 1160 45 37 -92 A C
ATOM 596 C PHE A 62 -22.782 -28.231 8.573 1.00 10.36 A C
ANISOU 596 C PHE A 62 1430 1271 1237 95 -166 -120 A C
ATOM 597 O PHE A 62 -22.144 -28.834 9.445 1.00 10.63 A O
ANISOU 597 O PHE A 62 1374 1378 1287 34 -6 -90 A O
ATOM 598 CB PHE A 62 -25.319 -28.282 8.569 1.00 10.47 A C
ANISOU 598 CB PHE A 62 1301 1442 1233 -53 15 9 A C
ATOM 599 CG PHE A 62 -25.805 -29.260 9.631 1.00 10.87 A C
ANISOU 599 CG PHE A 62 1478 1287 1366 -64 -33 -63 A C
ATOM 600 CD1 PHE A 62 -24.991 -29.733 10.654 1.00 11.51 A C
ANISOU 600 CD1 PHE A 62 1899 1274 1200 -2 125 -4 A C
ATOM 601 CD2 PHE A 62 -27.126 -29.693 9.592 1.00 12.06 A C
ANISOU 601 CD2 PHE A 62 1620 1580 1382 77 187 -20 A C
ATOM 602 CE1 PHE A 62 -25.489 -30.633 11.597 1.00 11.74 A C
ANISOU 602 CE1 PHE A 62 1661 1434 1366 70 63 -202 A C
ATOM 603 CE2 PHE A 62 -27.617 -30.587 10.534 1.00 13.59 A C
ANISOU 603 CE2 PHE A 62 1890 1656 1619 138 113 -124 A C
ATOM 604 CZ PHE A 62 -26.792 -31.055 11.532 1.00 13.39 A C
ANISOU 604 CZ PHE A 62 1962 1553 1572 18 123 -67 A C
ATOM 605 N TYR A 63 -22.370 -28.185 7.299 1.00 10.03 A N
ANISOU 605 N TYR A 63 1303 1359 1150 77 62 -133 A N
ATOM 606 CA TYR A 63 -21.090 -28.776 6.910 1.00 10.64 A C
ANISOU 606 CA TYR A 63 1336 1537 1170 99 3 -37 A C
ATOM 607 C TYR A 63 -19.945 -28.181 7.718 1.00 10.85 A C
ANISOU 607 C TYR A 63 1443 1503 1177 97 12 -70 A C
ATOM 608 O TYR A 63 -19.061 -28.906 8.190 1.00 11.43 A O
ANISOU 608 O TYR A 63 1487 1581 1276 256 -18 -94 A O
ATOM 609 CB TYR A 63 -20.818 -28.502 5.431 1.00 11.59 A C
ANISOU 609 CB TYR A 63 1591 1615 1200 6 39 -68 A C
ATOM 610 CG TYR A 63 -21.528 -29.346 4.386 1.00 11.57 A C
ANISOU 610 CG TYR A 63 1609 1362 1426 154 -1 -158 A C
ATOM 611 CD1 TYR A 63 -22.027 -30.611 4.673 1.00 12.54 A C
ANISOU 611 CD1 TYR A 63 1771 1592 1403 91 -218 -41 A C
ATOM 612 CD2 TYR A 63 -21.663 -28.868 3.092 1.00 12.30 A C
ANISOU 612 CD2 TYR A 63 1892 1600 1183 194 -37 -25 A C
ATOM 613 CE1 TYR A 63 -22.658 -31.371 3.681 1.00 12.95 A C
ANISOU 613 CE1 TYR A 63 1907 1583 1431 76 -199 -13 A C
ATOM 614 CE2 TYR A 63 -22.282 -29.613 2.105 1.00 11.62 A C
ANISOU 614 CE2 TYR A 63 1836 1525 1055 134 -70 -177 A C
ATOM 615 CZ TYR A 63 -22.766 -30.872 2.390 1.00 11.49 A C
ANISOU 615 CZ TYR A 63 1732 1386 1247 107 -50 -38 A C
ATOM 616 OH TYR A 63 -23.378 -31.632 1.411 1.00 11.69 A O
ANISOU 616 OH TYR A 63 1807 1353 1283 74 -269 -59 A O
ATOM 617 N PHE A 64 -19.912 -26.849 7.830 1.00 10.68 A N
ANISOU 617 N PHE A 64 1386 1547 1123 76 -11 -98 A N
ATOM 618 CA PHE A 64 -18.824 -26.190 8.549 1.00 12.62 A C
ANISOU 618 CA PHE A 64 1599 1790 1406 -187 -38 -29 A C
ATOM 619 C PHE A 64 -18.763 -26.674 9.990 1.00 11.37 A C
ANISOU 619 C PHE A 64 1413 1583 1326 207 -44 -159 A C
ATOM 620 O PHE A 64 -17.688 -26.994 10.512 1.00 12.87 A O
ANISOU 620 O PHE A 64 1464 2025 1400 244 -127 -227 A O
ATOM 621 CB PHE A 64 -19.030 -24.671 8.485 1.00 14.82 A C
ANISOU 621 CB PHE A 64 1967 1920 1745 -567 -130 47 A C
ATOM 622 CG PHE A 64 -18.006 -23.882 9.240 1.00 18.97 A C
ANISOU 622 CG PHE A 64 2432 2418 2357 -741 -47 -147 A C
ATOM 623 CD1 PHE A 64 -16.826 -23.495 8.629 1.00 23.51 A C
ANISOU 623 CD1 PHE A 64 2784 3056 3092 -1126 161 -40 A C
ATOM 624 CD2 PHE A 64 -18.221 -23.521 10.559 1.00 19.92 A C
ANISOU 624 CD2 PHE A 64 2788 2391 2389 -686 -296 -477 A C
ATOM 625 CE1 PHE A 64 -15.876 -22.768 9.321 1.00 25.46 A C
ANISOU 625 CE1 PHE A 64 3125 3269 3278 -1345 5 -212 A C
ATOM 626 CE2 PHE A 64 -17.276 -22.789 11.254 1.00 22.65 A C
ANISOU 626 CE2 PHE A 64 3270 2612 2722 -957 -371 -365 A C
ATOM 627 CZ PHE A 64 -16.105 -22.416 10.632 1.00 25.13 A C
ANISOU 627 CZ PHE A 64 3336 3174 3036 -1065 -271 -264 A C
ATOM 628 N LEU A 65 -19.922 -26.747 10.645 1.00 10.27 A N
ANISOU 628 N LEU A 65 1395 1306 1201 158 -4 -153 A N
ATOM 629 CA LEU A 65 -19.971 -27.178 12.039 1.00 10.41 A C
ANISOU 629 CA LEU A 65 1469 1397 1088 341 5 -104 A C
ATOM 630 C LEU A 65 -19.543 -28.637 12.197 1.00 10.76 A C
ANISOU 630 C LEU A 65 1490 1478 1122 381 -8 -109 A C
ATOM 631 O LEU A 65 -18.754 -28.962 13.088 1.00 11.69 A O
ANISOU 631 O LEU A 65 1664 1560 1216 407 -160 -114 A O
ATOM 632 CB LEU A 65 -21.370 -26.934 12.599 1.00 10.96 A C
ANISOU 632 CB LEU A 65 1548 1335 1281 271 54 -118 A C
ATOM 633 CG LEU A 65 -21.691 -25.461 12.846 1.00 10.99 A C
ANISOU 633 CG LEU A 65 1498 1408 1269 201 20 -247 A C
ATOM 634 CD1 LEU A 65 -23.171 -25.290 13.155 1.00 13.24 A C
ANISOU 634 CD1 LEU A 65 1569 1733 1730 184 27 -198 A C
ATOM 635 CD2 LEU A 65 -20.843 -24.888 13.976 1.00 13.01 A C
ANISOU 635 CD2 LEU A 65 1793 1695 1455 310 -299 -427 A C
ATOM 636 N AILE A 66 -19.999 -29.531 11.315 0.56 10.25 A N
ANISOU 636 N AILE A 66 1496 1396 1001 166 -204 -85 A N
ATOM 637 N BILE A 66 -20.095 -29.530 11.367 0.44 10.63 A N
ANISOU 637 N BILE A 66 1424 1448 1167 470 123 -79 A N
ATOM 638 CA AILE A 66 -19.574 -30.927 11.423 0.56 10.92 A C
ANISOU 638 CA AILE A 66 1537 1356 1257 162 -169 -253 A C
ATOM 639 CA BILE A 66 -19.750 -30.949 11.441 0.44 11.85 A C
ANISOU 639 CA BILE A 66 1608 1490 1405 578 84 -3 A C
ATOM 640 C AILE A 66 -18.075 -31.067 11.173 0.56 11.21 A C
ANISOU 640 C AILE A 66 1667 1450 1144 145 -129 -99 A C
ATOM 641 C BILE A 66 -18.262 -31.145 11.189 0.44 10.95 A C
ANISOU 641 C BILE A 66 1433 1561 1167 523 7 -251 A C
ATOM 642 O AILE A 66 -17.380 -31.779 11.908 0.56 12.14 A O
ANISOU 642 O AILE A 66 1790 1453 1370 257 -329 -1 A O
ATOM 643 O BILE A 66 -17.582 -31.880 11.915 0.44 11.03 A O
ANISOU 643 O BILE A 66 1384 1611 1196 516 198 -332 A O
ATOM 644 CB AILE A 66 -20.412 -31.848 10.514 0.56 11.04 A C
ANISOU 644 CB AILE A 66 1465 1399 1331 280 -150 -424 A C
ATOM 645 CB BILE A 66 -20.600 -31.765 10.448 0.44 13.83 A C
ANISOU 645 CB BILE A 66 1902 1679 1675 466 131 258 A C
ATOM 646 CG1AILE A 66 -21.823 -32.001 11.084 0.56 11.57 A C
ANISOU 646 CG1AILE A 66 1412 1448 1537 303 -234 -493 A C
ATOM 647 CG1BILE A 66 -22.066 -31.808 10.883 0.44 14.80 A C
ANISOU 647 CG1BILE A 66 2183 1793 1649 470 339 310 A C
ATOM 648 CG2AILE A 66 -19.740 -33.231 10.336 0.56 11.39 A C
ANISOU 648 CG2AILE A 66 1357 1555 1417 577 -110 -515 A C
ATOM 649 CG2BILE A 66 -20.038 -33.181 10.283 0.44 14.92 A C
ANISOU 649 CG2BILE A 66 1886 1936 1847 320 95 389 A C
ATOM 650 CD1AILE A 66 -22.787 -32.670 10.148 0.56 11.39 A C
ANISOU 650 CD1AILE A 66 1391 1503 1434 342 -439 -400 A C
ATOM 651 CD1BILE A 66 -22.369 -32.880 11.906 0.44 14.96 A C
ANISOU 651 CD1BILE A 66 2362 1722 1598 670 538 176 A C
ATOM 652 N AARG A 67 -17.551 -30.398 10.139 0.56 11.97 A N
ANISOU 652 N AARG A 67 1558 1655 1333 207 -56 -194 A N
ATOM 653 N BARG A 67 -17.738 -30.492 10.148 0.44 11.03 A N
ANISOU 653 N BARG A 67 1311 1623 1257 404 -62 -323 A N
ATOM 654 CA AARG A 67 -16.121 -30.494 9.849 0.56 12.65 A C
ANISOU 654 CA AARG A 67 1445 1935 1426 292 -3 -269 A C
ATOM 655 CA BARG A 67 -16.326 -30.624 9.805 0.44 11.88 A C
ANISOU 655 CA BARG A 67 1410 1847 1258 205 -43 -297 A C
ATOM 656 C AARG A 67 -15.277 -30.145 11.068 0.56 13.72 A C
ANISOU 656 C AARG A 67 1682 1930 1600 418 -40 -422 A C
ATOM 657 C BARG A 67 -15.433 -30.333 11.004 0.44 11.12 A C
ANISOU 657 C BARG A 67 1289 1697 1238 132 -38 -184 A C
ATOM 658 O AARG A 67 -14.268 -30.806 11.345 0.56 14.35 A O
ANISOU 658 O AARG A 67 1737 1983 1732 424 -204 -584 A O
ATOM 659 O BARG A 67 -14.499 -31.089 11.296 0.44 12.25 A O
ANISOU 659 O BARG A 67 1333 1953 1370 216 -56 -83 A O
ATOM 660 CB AARG A 67 -15.748 -29.588 8.673 0.56 13.76 A C
ANISOU 660 CB AARG A 67 1792 2159 1278 -55 93 -151 A C
ATOM 661 CB BARG A 67 -15.995 -29.685 8.643 0.44 13.25 A C
ANISOU 661 CB BARG A 67 1693 2039 1303 89 44 -267 A C
ATOM 662 CG AARG A 67 -16.251 -30.073 7.320 0.56 15.76 A C
ANISOU 662 CG AARG A 67 2024 2419 1546 -292 234 -174 A C
ATOM 663 CG BARG A 67 -14.513 -29.474 8.401 0.44 14.44 A C
ANISOU 663 CG BARG A 67 1735 2214 1539 -71 1 -193 A C
ATOM 664 CD AARG A 67 -15.691 -29.241 6.172 0.56 19.42 A C
ANISOU 664 CD AARG A 67 2287 2877 2214 -115 280 -16 A C
ATOM 665 CD BARG A 67 -14.267 -28.743 7.087 0.44 15.33 A C
ANISOU 665 CD BARG A 67 1947 2434 1443 -287 308 -289 A C
ATOM 666 NE AARG A 67 -14.253 -29.430 6.030 0.56 21.25 A N
ANISOU 666 NE AARG A 67 2449 3108 2517 42 247 -119 A N
ATOM 667 NE BARG A 67 -14.750 -29.508 5.943 0.44 16.02 A N
ANISOU 667 NE BARG A 67 2027 2459 1601 -361 467 -160 A N
ATOM 668 CZ AARG A 67 -13.693 -30.426 5.357 0.56 22.54 A C
ANISOU 668 CZ AARG A 67 2543 3313 2709 202 334 -100 A C
ATOM 669 CZ BARG A 67 -14.059 -30.464 5.337 0.44 16.88 A C
ANISOU 669 CZ BARG A 67 2314 2419 1682 -399 650 -79 A C
ATOM 670 NH1AARG A 67 -14.424 -31.329 4.723 0.56 22.78 A N
ANISOU 670 NH1AARG A 67 2560 3381 2713 339 178 -57 A N
ATOM 671 NH1BARG A 67 -12.836 -30.786 5.726 0.44 17.88 A N
ANISOU 671 NH1BARG A 67 2554 2414 1826 -347 802 -26 A N
ATOM 672 NH2AARG A 67 -12.367 -30.521 5.324 0.56 23.66 A N
ANISOU 672 NH2AARG A 67 2645 3474 2872 240 571 26 A N
ATOM 673 NH2BARG A 67 -14.611 -31.117 4.318 0.44 17.53 A N
ANISOU 673 NH2BARG A 67 2324 2513 1822 -190 302 -113 A N
ATOM 674 N ALYS A 68 -15.672 -29.108 11.808 0.56 12.99 A N
ANISOU 674 N ALYS A 68 1587 1744 1604 116 90 -287 A N
ATOM 675 N BLYS A 68 -15.708 -29.238 11.713 0.44 10.66 A N
ANISOU 675 N BLYS A 68 1303 1666 1082 -31 -15 -185 A N
ATOM 676 CA ALYS A 68 -14.927 -28.711 12.998 0.56 12.68 A C
ANISOU 676 CA ALYS A 68 1585 1807 1426 -47 154 -222 A C
ATOM 677 CA BLYS A 68 -14.891 -28.886 12.870 0.44 11.10 A C
ANISOU 677 CA BLYS A 68 1536 1637 1045 -115 -19 -334 A C
ATOM 678 C ALYS A 68 -15.218 -29.619 14.188 0.56 12.08 A C
ANISOU 678 C ALYS A 68 1511 1795 1285 73 38 -178 A C
ATOM 679 C BLYS A 68 -15.174 -29.803 14.055 0.44 10.77 A C
ANISOU 679 C BLYS A 68 1359 1671 1063 -90 62 -314 A C
ATOM 680 O ALYS A 68 -14.325 -29.871 15.005 0.56 13.21 A O
ANISOU 680 O ALYS A 68 1487 2121 1411 104 -85 94 A O
ATOM 681 O BLYS A 68 -14.245 -30.226 14.754 0.44 10.52 A O
ANISOU 681 O BLYS A 68 1165 1725 1104 65 0 -387 A O
ATOM 682 CB ALYS A 68 -15.236 -27.252 13.344 0.56 13.55 A C
ANISOU 682 CB ALYS A 68 1795 1917 1438 -194 215 12 A C
ATOM 683 CB BLYS A 68 -15.110 -27.420 13.244 0.44 12.62 A C
ANISOU 683 CB BLYS A 68 1820 1730 1247 -145 177 -99 A C
ATOM 684 CG ALYS A 68 -14.880 -26.261 12.242 0.56 16.72 A C
ANISOU 684 CG ALYS A 68 1945 2490 1917 -382 120 227 A C
ATOM 685 CG BLYS A 68 -14.528 -26.441 12.238 0.44 14.87 A C
ANISOU 685 CG BLYS A 68 2041 1899 1711 56 345 -204 A C
ATOM 686 CD ALYS A 68 -13.414 -26.364 11.851 0.56 18.46 A C
ANISOU 686 CD ALYS A 68 2170 2715 2130 -270 33 402 A C
ATOM 687 CD BLYS A 68 -14.695 -25.008 12.707 0.44 16.82 A C
ANISOU 687 CD BLYS A 68 2441 1970 1981 125 482 -112 A C
ATOM 688 N ARG A 69 -16.450 -30.117 14.298 1.00 10.61 A N
ANISOU 688 N ARG A 69 1435 1517 1078 92 129 -189 A N
ATOM 689 CA ARG A 69 -16.813 -31.013 15.396 1.00 10.67 A C
ANISOU 689 CA ARG A 69 1272 1595 1188 233 -190 -160 A C
ATOM 690 C ARG A 69 -16.076 -32.350 15.332 1.00 10.94 A C
ANISOU 690 C ARG A 69 1317 1619 1219 293 -94 -173 A C
ATOM 691 O ARG A 69 -15.643 -32.872 16.368 1.00 11.27 A O
ANISOU 691 O ARG A 69 1302 1681 1300 288 -123 -30 A O
ATOM 692 CB ARG A 69 -18.330 -31.230 15.387 1.00 10.44 A C
ANISOU 692 CB ARG A 69 1423 1402 1141 251 -111 -37 A C
ATOM 693 CG ARG A 69 -18.861 -32.411 16.209 1.00 10.50 A C
ANISOU 693 CG ARG A 69 1476 1348 1163 107 -55 -6 A C
ATOM 694 CD ARG A 69 -18.686 -32.246 17.715 1.00 10.07 A C
ANISOU 694 CD ARG A 69 1538 1220 1069 63 -93 -33 A C
ATOM 695 NE ARG A 69 -19.140 -33.434 18.430 1.00 10.14 A N
ANISOU 695 NE ARG A 69 1415 1252 1185 235 -179 -200 A N
ATOM 696 CZ ARG A 69 -18.437 -34.559 18.521 1.00 10.42 A C
ANISOU 696 CZ ARG A 69 1510 1242 1207 218 -145 -78 A C
ATOM 697 NH1 ARG A 69 -17.213 -34.651 18.019 1.00 11.13 A N
ANISOU 697 NH1 ARG A 69 1486 1358 1383 331 -134 -159 A N
ATOM 698 NH2 ARG A 69 -18.983 -35.624 19.103 1.00 11.11 A N
ANISOU 698 NH2 ARG A 69 1636 1283 1303 176 -98 -30 A N
ATOM 699 N ILE A 70 -15.934 -32.927 14.134 1.00 11.97 A N
ANISOU 699 N ILE A 70 1588 1655 1307 340 -57 -224 A N
ATOM 700 CA ILE A 70 -15.261 -34.214 13.976 1.00 13.44 A C
ANISOU 700 CA ILE A 70 1818 1907 1380 592 -43 -220 A C
ATOM 701 C ILE A 70 -13.824 -34.060 13.488 1.00 14.91 A C
ANISOU 701 C ILE A 70 1830 2292 1542 782 -131 -302 A C
ATOM 702 O ILE A 70 -13.194 -35.049 13.100 1.00 16.56 A O
ANISOU 702 O ILE A 70 1896 2189 2209 828 -216 -528 A O
ATOM 703 CB ILE A 70 -16.073 -35.241 13.165 1.00 12.96 A C
ANISOU 703 CB ILE A 70 1868 1707 1348 438 9 -147 A C
ATOM 704 CG1 ILE A 70 -16.217 -34.823 11.699 1.00 12.73 A C
ANISOU 704 CG1 ILE A 70 1724 1655 1459 353 -166 -182 A C
ATOM 705 CG2 ILE A 70 -17.422 -35.488 13.837 1.00 14.98 A C
ANISOU 705 CG2 ILE A 70 2160 1715 1817 122 420 -276 A C
ATOM 706 CD1 ILE A 70 -16.936 -35.848 10.833 1.00 13.70 A C
ANISOU 706 CD1 ILE A 70 1800 1708 1699 413 -91 -316 A C
ATOM 707 N AHIS A 71 -13.291 -32.839 13.501 0.80 14.18 A N
ANISOU 707 N AHIS A 71 1573 2294 1520 531 -215 -355 A N
ATOM 708 N BHIS A 71 -13.295 -32.835 13.495 0.20 16.65 A N
ANISOU 708 N BHIS A 71 1910 2757 1659 657 -113 -320 A N
ATOM 709 CA AHIS A 71 -11.871 -32.592 13.257 0.80 16.56 A C
ANISOU 709 CA AHIS A 71 1265 3320 1706 454 -389 -511 A C
ATOM 710 CA BHIS A 71 -11.878 -32.575 13.245 0.20 19.06 A C
ANISOU 710 CA BHIS A 71 1936 3421 1887 554 -113 -404 A C
ATOM 711 C AHIS A 71 -11.432 -33.108 11.887 0.80 17.16 A C
ANISOU 711 C AHIS A 71 1416 3463 1642 681 -311 -620 A C
ATOM 712 C BHIS A 71 -11.434 -33.115 11.885 0.20 18.54 A C
ANISOU 712 C BHIS A 71 1804 3496 1744 660 -47 -582 A C
ATOM 713 O AHIS A 71 -10.384 -33.742 11.755 0.80 19.10 A O
ANISOU 713 O AHIS A 71 1628 3794 1835 1069 -449 -646 A O
ATOM 714 O BHIS A 71 -10.396 -33.770 11.760 0.20 19.59 A O
ANISOU 714 O BHIS A 71 1961 3627 1855 732 -5 -720 A O
ATOM 715 CB AHIS A 71 -11.004 -33.182 14.375 0.80 20.37 A C
ANISOU 715 CB AHIS A 71 1553 4303 1886 247 -469 -709 A C
ATOM 716 CB BHIS A 71 -11.005 -33.117 14.382 0.20 22.25 A C
ANISOU 716 CB BHIS A 71 2180 4013 2260 367 -180 -344 A C
ATOM 717 CG AHIS A 71 -9.705 -32.467 14.580 0.80 25.66 A C
ANISOU 717 CG AHIS A 71 2164 5081 2506 -159 -75 -680 A C
ATOM 718 CG BHIS A 71 -9.625 -32.536 14.421 0.20 25.41 A C
ANISOU 718 CG BHIS A 71 2467 4514 2675 174 -179 -217 A C
ATOM 719 CD2AHIS A 71 -8.888 -31.825 13.711 0.80 28.80 A C
ANISOU 719 CD2AHIS A 71 2538 5430 2976 -357 50 -666 A C
ATOM 720 CD2BHIS A 71 -8.495 -32.966 15.029 0.20 26.67 A C
ANISOU 720 CD2BHIS A 71 2554 4717 2864 155 -153 -161 A C
ATOM 721 ND1AHIS A 71 -9.104 -32.365 15.815 0.80 27.16 A N
ANISOU 721 ND1AHIS A 71 2347 5296 2676 -403 94 -944 A N
ATOM 722 ND1BHIS A 71 -9.291 -31.364 13.777 0.20 26.80 A N
ANISOU 722 ND1BHIS A 71 2606 4707 2870 93 -213 -191 A N
ATOM 723 CE1AHIS A 71 -7.975 -31.689 15.701 0.80 28.72 A C
ANISOU 723 CE1AHIS A 71 2432 5479 3002 -527 77 -842 A C
ATOM 724 CE1BHIS A 71 -8.014 -31.097 13.987 0.20 27.38 A C
ANISOU 724 CE1BHIS A 71 2649 4817 2937 60 -246 -155 A C
ATOM 725 NE2AHIS A 71 -7.821 -31.348 14.434 0.80 30.32 A N
ANISOU 725 NE2AHIS A 71 2737 5564 3220 -456 74 -683 A N
ATOM 726 NE2BHIS A 71 -7.508 -32.054 14.744 0.20 27.30 A N
ANISOU 726 NE2BHIS A 71 2616 4830 2928 66 -238 -166 A N
ATOM 727 N LEU A 72 -12.235 -32.845 10.857 1.00 17.33 A N
ANISOU 727 N LEU A 72 1550 3484 1552 708 -88 -598 A N
ATOM 728 CA LEU A 72 -11.855 -33.267 9.516 1.00 19.56 A C
ANISOU 728 CA LEU A 72 1670 3963 1799 461 -68 -628 A C
ATOM 729 C LEU A 72 -10.604 -32.529 9.065 1.00 23.98 A C
ANISOU 729 C LEU A 72 1974 4985 2154 105 161 -877 A C
ATOM 730 O LEU A 72 -10.373 -31.371 9.423 1.00 25.94 A O
ANISOU 730 O LEU A 72 2254 5096 2507 -384 239 -682 A O
ATOM 731 CB LEU A 72 -12.968 -32.992 8.513 1.00 17.24 A C
ANISOU 731 CB LEU A 72 1614 3236 1699 247 -10 -352 A C
ATOM 732 CG LEU A 72 -14.201 -33.876 8.650 1.00 18.41 A C
ANISOU 732 CG LEU A 72 2010 2877 2108 306 80 -228 A C
ATOM 733 CD1 LEU A 72 -15.136 -33.617 7.492 1.00 18.65 A C
ANISOU 733 CD1 LEU A 72 1932 3092 2062 48 -303 -252 A C
ATOM 734 CD2 LEU A 72 -13.823 -35.342 8.733 1.00 20.76 A C
ANISOU 734 CD2 LEU A 72 2399 2894 2594 616 -43 -24 A C
ATOM 735 N ARG A 73 -9.786 -33.225 8.285 1.00 25.90 A N
ANISOU 735 N ARG A 73 1880 5657 2305 288 383 -894 A N
ATOM 736 CA ARG A 73 -8.648 -32.605 7.635 1.00 28.50 A C
ANISOU 736 CA ARG A 73 1979 6265 2586 167 227 -672 A C
ATOM 737 C ARG A 73 -9.116 -31.891 6.372 1.00 29.75 A C
ANISOU 737 C ARG A 73 2141 6471 2691 -311 -66 -533 A C
ATOM 738 O ARG A 73 -10.189 -32.172 5.835 1.00 27.83 A O
ANISOU 738 O ARG A 73 1705 6230 2638 -494 -97 -516 A O
ATOM 739 CB ARG A 73 -7.610 -33.663 7.266 1.00 30.51 A C
ANISOU 739 CB ARG A 73 2141 6515 2936 595 575 -417 A C
ATOM 740 CG ARG A 73 -7.218 -34.576 8.417 1.00 35.25 A C
ANISOU 740 CG ARG A 73 3007 6836 3551 728 586 -403 A C
ATOM 741 CD ARG A 73 -6.118 -35.540 8.002 1.00 39.88 A C
ANISOU 741 CD ARG A 73 3859 7077 4215 606 357 -367 A C
ATOM 742 NE ARG A 73 -6.534 -36.418 6.914 1.00 43.95 A N
ANISOU 742 NE ARG A 73 4616 7298 4785 347 80 -249 A N
ATOM 743 CZ ARG A 73 -7.008 -37.645 7.081 1.00 46.85 A C
ANISOU 743 CZ ARG A 73 5144 7495 5163 156 -29 -198 A C
ATOM 744 NH1 ARG A 73 -7.147 -38.175 8.286 1.00 48.08 A N
ANISOU 744 NH1 ARG A 73 5327 7577 5364 52 35 -110 A N
ATOM 745 NH2 ARG A 73 -7.347 -38.361 6.013 1.00 47.68 A N
ANISOU 745 NH2 ARG A 73 5312 7531 5274 150 -68 -281 A N
ATOM 746 N ALA A 74 -8.293 -30.952 5.897 1.00 32.02 A N
ANISOU 746 N ALA A 74 2377 6738 3052 -606 -226 -415 A N
ATOM 747 CA ALA A 74 -8.647 -30.207 4.691 1.00 33.50 A C
ANISOU 747 CA ALA A 74 2584 6914 3230 -610 -417 -324 A C
ATOM 748 C ALA A 74 -8.872 -31.143 3.509 1.00 32.55 A C
ANISOU 748 C ALA A 74 2342 7068 2958 -557 -414 -203 A C
ATOM 749 O ALA A 74 -9.761 -30.908 2.678 1.00 34.50 A O
ANISOU 749 O ALA A 74 2560 7223 3325 -566 -649 -77 A O
ATOM 750 CB ALA A 74 -7.560 -29.181 4.370 1.00 35.23 A C
ANISOU 750 CB ALA A 74 2956 6924 3506 -728 -384 -493 A C
ATOM 751 N GLU A 75 -8.090 -32.217 3.426 1.00 30.97 A N
ANISOU 751 N GLU A 75 2187 7046 2534 -341 65 -236 A N
ATOM 752 CA GLU A 75 -8.205 -33.159 2.321 1.00 30.59 A C
ANISOU 752 CA GLU A 75 2184 7029 2410 -80 232 -448 A C
ATOM 753 C GLU A 75 -9.363 -34.134 2.483 1.00 28.15 A C
ANISOU 753 C GLU A 75 2029 6592 2075 154 100 -683 A C
ATOM 754 O GLU A 75 -9.576 -34.967 1.594 1.00 29.55 A O
ANISOU 754 O GLU A 75 2318 6831 2078 211 270 -850 A O
ATOM 755 CB GLU A 75 -6.896 -33.932 2.134 1.00 33.17 A C
ANISOU 755 CB GLU A 75 2259 7364 2982 319 162 -374 A C
ATOM 756 CG GLU A 75 -6.580 -34.905 3.258 1.00 35.46 A C
ANISOU 756 CG GLU A 75 2490 7692 3292 656 -320 -359 A C
ATOM 757 CD GLU A 75 -5.672 -34.312 4.322 1.00 39.40 A C
ANISOU 757 CD GLU A 75 3085 8050 3835 812 -544 -288 A C
ATOM 758 OE1 GLU A 75 -5.699 -33.078 4.525 1.00 40.32 A O
ANISOU 758 OE1 GLU A 75 3211 8216 3892 875 -517 -273 A O
ATOM 759 OE2 GLU A 75 -4.922 -35.086 4.953 1.00 41.33 A O
ANISOU 759 OE2 GLU A 75 3340 8180 4185 859 -656 -309 A O
ATOM 760 N ASP A 76 -10.104 -34.060 3.584 1.00 24.52 A N
ANISOU 760 N ASP A 76 1735 5655 1927 525 220 -504 A N
ATOM 761 CA ASP A 76 -11.262 -34.913 3.796 1.00 22.86 A C
ANISOU 761 CA ASP A 76 1982 5052 1653 753 104 -603 A C
ATOM 762 C ASP A 76 -12.491 -34.245 3.199 1.00 19.56 A C
ANISOU 762 C ASP A 76 1881 4025 1525 434 105 -499 A C
ATOM 763 O ASP A 76 -12.711 -33.048 3.400 1.00 19.53 A O
ANISOU 763 O ASP A 76 1963 3627 1829 18 -56 -604 A O
ATOM 764 CB ASP A 76 -11.496 -35.120 5.291 1.00 25.42 A C
ANISOU 764 CB ASP A 76 2427 5484 1748 1428 -118 -682 A C
ATOM 765 CG ASP A 76 -10.418 -35.958 5.945 1.00 29.87 A C
ANISOU 765 CG ASP A 76 3262 5885 2203 2000 -300 -650 A C
ATOM 766 OD1 ASP A 76 -9.759 -36.746 5.236 1.00 33.04 A O
ANISOU 766 OD1 ASP A 76 3880 5866 2809 2392 -393 -764 A O
ATOM 767 OD2 ASP A 76 -10.233 -35.830 7.175 1.00 31.20 A O
ANISOU 767 OD2 ASP A 76 3453 6228 2173 1978 -467 -475 A O
ATOM 768 N ALA A 77 -13.285 -35.019 2.472 1.00 17.87 A N
ANISOU 768 N ALA A 77 1892 3448 1449 326 -70 -357 A N
ATOM 769 CA ALA A 77 -14.546 -34.535 1.941 1.00 15.99 A C
ANISOU 769 CA ALA A 77 1817 2873 1386 121 -9 -410 A C
ATOM 770 C ALA A 77 -15.658 -34.764 2.958 1.00 14.66 A C
ANISOU 770 C ALA A 77 1747 2576 1246 313 -0 -201 A C
ATOM 771 O ALA A 77 -15.543 -35.596 3.860 1.00 16.28 A O
ANISOU 771 O ALA A 77 1878 2829 1478 721 -26 -61 A O
ATOM 772 CB ALA A 77 -14.885 -35.266 0.644 1.00 16.60 A C
ANISOU 772 CB ALA A 77 2066 2821 1420 1 110 -473 A C
ATOM 773 N LEU A 78 -16.753 -34.028 2.784 1.00 13.09 A N
ANISOU 773 N LEU A 78 1531 2175 1267 110 -28 -150 A N
ATOM 774 CA LEU A 78 -17.942 -34.211 3.610 1.00 12.25 A C
ANISOU 774 CA LEU A 78 1597 1864 1194 73 31 17 A C
ATOM 775 C LEU A 78 -19.158 -33.954 2.740 1.00 11.84 A C
ANISOU 775 C LEU A 78 1704 1687 1109 94 -152 31 A C
ATOM 776 O LEU A 78 -19.281 -32.870 2.165 1.00 13.12 A O
ANISOU 776 O LEU A 78 1691 1762 1533 -89 -220 101 A O
ATOM 777 CB LEU A 78 -17.936 -33.239 4.789 1.00 13.00 A C
ANISOU 777 CB LEU A 78 1781 1815 1342 -27 -59 -200 A C
ATOM 778 CG LEU A 78 -19.176 -33.313 5.687 1.00 12.52 A C
ANISOU 778 CG LEU A 78 1751 1744 1262 7 49 -199 A C
ATOM 779 CD1 LEU A 78 -19.306 -34.676 6.361 1.00 13.34 A C
ANISOU 779 CD1 LEU A 78 1978 1788 1302 -200 138 90 A C
ATOM 780 CD2 LEU A 78 -19.137 -32.203 6.712 1.00 13.18 A C
ANISOU 780 CD2 LEU A 78 1752 1767 1490 10 84 -286 A C
ATOM 781 N PHE A 79 -20.053 -34.937 2.656 1.00 11.12 A N
ANISOU 781 N PHE A 79 1571 1586 1068 -37 -55 -112 A N
ATOM 782 CA PHE A 79 -21.285 -34.844 1.887 1.00 11.03 A C
ANISOU 782 CA PHE A 79 1574 1483 1133 -127 -43 -9 A C
ATOM 783 C PHE A 79 -22.458 -35.199 2.788 1.00 10.74 A C
ANISOU 783 C PHE A 79 1573 1394 1115 38 -145 93 A C
ATOM 784 O PHE A 79 -22.344 -36.060 3.671 1.00 11.44 A O
ANISOU 784 O PHE A 79 1647 1515 1184 219 -40 281 A O
ATOM 785 CB PHE A 79 -21.303 -35.856 0.727 1.00 11.61 A C
ANISOU 785 CB PHE A 79 1782 1532 1098 -141 26 -197 A C
ATOM 786 CG PHE A 79 -20.171 -35.699 -0.251 1.00 12.72 A C
ANISOU 786 CG PHE A 79 2083 1699 1052 -182 -12 -22 A C
ATOM 787 CD1 PHE A 79 -18.965 -36.356 -0.051 1.00 12.67 A C
ANISOU 787 CD1 PHE A 79 1854 1923 1038 -172 133 -191 A C
ATOM 788 CD2 PHE A 79 -20.307 -34.903 -1.380 1.00 14.10 A C
ANISOU 788 CD2 PHE A 79 2609 1712 1036 -262 3 55 A C
ATOM 789 CE1 PHE A 79 -17.923 -36.229 -0.961 1.00 14.63 A C
ANISOU 789 CE1 PHE A 79 2230 2140 1186 -264 157 -167 A C
ATOM 790 CE2 PHE A 79 -19.260 -34.772 -2.288 1.00 14.66 A C
ANISOU 790 CE2 PHE A 79 2568 1779 1224 -350 -116 54 A C
ATOM 791 CZ PHE A 79 -18.077 -35.441 -2.078 1.00 15.30 A C
ANISOU 791 CZ PHE A 79 2515 1939 1358 -366 84 -166 A C
ATOM 792 N PHE A 80 -23.591 -34.542 2.546 1.00 10.60 A N
ANISOU 792 N PHE A 80 1617 1364 1044 116 -178 8 A N
ATOM 793 CA PHE A 80 -24.875 -34.953 3.096 1.00 10.48 A C
ANISOU 793 CA PHE A 80 1627 1297 1056 159 -25 -111 A C
ATOM 794 C PHE A 80 -25.686 -35.665 2.020 1.00 10.18 A C
ANISOU 794 C PHE A 80 1574 1257 1036 347 -10 24 A C
ATOM 795 O PHE A 80 -25.564 -35.370 0.828 1.00 10.94 A O
ANISOU 795 O PHE A 80 1709 1365 1085 171 -129 21 A O
ATOM 796 CB PHE A 80 -25.720 -33.746 3.522 1.00 11.47 A C
ANISOU 796 CB PHE A 80 1980 1305 1073 300 -61 -208 A C
ATOM 797 CG PHE A 80 -25.437 -33.188 4.892 1.00 12.58 A C
ANISOU 797 CG PHE A 80 2162 1385 1233 251 -172 -114 A C
ATOM 798 CD1 PHE A 80 -24.486 -33.728 5.746 1.00 12.61 A C
ANISOU 798 CD1 PHE A 80 2264 1318 1211 142 -191 -204 A C
ATOM 799 CD2 PHE A 80 -26.190 -32.104 5.332 1.00 13.11 A C
ANISOU 799 CD2 PHE A 80 2086 1525 1369 25 94 -126 A C
ATOM 800 CE1 PHE A 80 -24.288 -33.167 7.011 1.00 14.36 A C
ANISOU 800 CE1 PHE A 80 2636 1308 1512 334 -284 -74 A C
ATOM 801 CE2 PHE A 80 -25.997 -31.548 6.576 1.00 14.66 A C
ANISOU 801 CE2 PHE A 80 2311 1556 1703 237 5 -26 A C
ATOM 802 CZ PHE A 80 -25.052 -32.079 7.420 1.00 14.71 A C
ANISOU 802 CZ PHE A 80 2460 1655 1475 178 -167 -78 A C
ATOM 803 N PHE A 81 -26.567 -36.559 2.467 1.00 10.41 A N
ANISOU 803 N PHE A 81 1547 1318 1092 192 -66 59 A N
ATOM 804 CA PHE A 81 -27.571 -37.189 1.620 1.00 11.20 A C
ANISOU 804 CA PHE A 81 1758 1314 1184 51 -200 -30 A C
ATOM 805 C PHE A 81 -28.907 -37.146 2.338 1.00 12.02 A C
ANISOU 805 C PHE A 81 1765 1519 1283 1 -333 121 A C
ATOM 806 O PHE A 81 -28.992 -37.473 3.527 1.00 12.65 A O
ANISOU 806 O PHE A 81 1774 1784 1248 -61 -352 163 A O
ATOM 807 CB PHE A 81 -27.209 -38.646 1.308 1.00 12.73 A C
ANISOU 807 CB PHE A 81 2078 1167 1593 26 -405 -70 A C
ATOM 808 CG PHE A 81 -25.907 -38.792 0.592 1.00 13.51 A C
ANISOU 808 CG PHE A 81 1938 1426 1769 365 -465 -197 A C
ATOM 809 CD1 PHE A 81 -24.728 -38.916 1.303 1.00 15.91 A C
ANISOU 809 CD1 PHE A 81 2260 1567 2217 725 -609 -490 A C
ATOM 810 CD2 PHE A 81 -25.851 -38.768 -0.789 1.00 13.22 A C
ANISOU 810 CD2 PHE A 81 1881 1463 1678 369 -230 -147 A C
ATOM 811 CE1 PHE A 81 -23.516 -39.034 0.652 1.00 17.90 A C
ANISOU 811 CE1 PHE A 81 2346 1931 2523 776 -528 -602 A C
ATOM 812 CE2 PHE A 81 -24.646 -38.878 -1.444 1.00 15.40 A C
ANISOU 812 CE2 PHE A 81 2072 1585 2194 559 -171 -338 A C
ATOM 813 CZ PHE A 81 -23.477 -39.016 -0.722 1.00 16.59 A C
ANISOU 813 CZ PHE A 81 2072 1791 2441 664 -391 -497 A C
ATOM 814 N VAL A 82 -29.947 -36.749 1.615 1.00 11.98 A N
ANISOU 814 N VAL A 82 1687 1530 1333 -58 -219 27 A N
ATOM 815 CA VAL A 82 -31.327 -36.919 2.044 1.00 13.03 A C
ANISOU 815 CA VAL A 82 1762 1787 1402 22 -255 -64 A C
ATOM 816 C VAL A 82 -31.987 -37.758 0.964 1.00 14.54 A C
ANISOU 816 C VAL A 82 1774 2137 1613 -19 -361 22 A C
ATOM 817 O VAL A 82 -31.951 -37.392 -0.217 1.00 14.71 A O
ANISOU 817 O VAL A 82 2011 2154 1425 -5 -407 17 A O
ATOM 818 CB VAL A 82 -32.041 -35.569 2.215 1.00 14.41 A C
ANISOU 818 CB VAL A 82 1815 2057 1605 245 -199 -194 A C
ATOM 819 CG1 VAL A 82 -33.495 -35.779 2.626 1.00 15.84 A C
ANISOU 819 CG1 VAL A 82 1789 2391 1839 442 -90 -149 A C
ATOM 820 CG2 VAL A 82 -31.314 -34.696 3.232 1.00 15.31 A C
ANISOU 820 CG2 VAL A 82 2028 1842 1948 301 -122 -309 A C
ATOM 821 N ASN A 83 -32.539 -38.904 1.351 1.00 16.01 A N
ANISOU 821 N ASN A 83 2095 2508 1479 -273 -240 -246 A N
ATOM 822 CA ASN A 83 -33.107 -39.842 0.381 1.00 18.72 A C
ANISOU 822 CA ASN A 83 2495 2901 1717 -683 -150 -404 A C
ATOM 823 C ASN A 83 -32.130 -40.128 -0.759 1.00 18.63 A C
ANISOU 823 C ASN A 83 2878 2536 1664 -887 -80 -490 A C
ATOM 824 O ASN A 83 -32.491 -40.114 -1.938 1.00 21.19 A O
ANISOU 824 O ASN A 83 3167 3162 1724 -1238 -104 -574 A O
ATOM 825 CB ASN A 83 -34.458 -39.363 -0.148 1.00 20.86 A C
ANISOU 825 CB ASN A 83 2595 3454 1875 -668 -161 -364 A C
ATOM 826 CG ASN A 83 -35.495 -39.254 0.941 1.00 20.99 A C
ANISOU 826 CG ASN A 83 2759 3406 1811 -758 -262 -356 A C
ATOM 827 ND2 ASN A 83 -36.399 -38.292 0.805 1.00 21.90 A N
ANISOU 827 ND2 ASN A 83 2814 3336 2172 -505 -459 -259 A N
ATOM 828 OD1 ASN A 83 -35.476 -40.018 1.907 1.00 21.81 A O
ANISOU 828 OD1 ASN A 83 2990 3461 1836 -1070 -43 -296 A O
ATOM 829 N AASN A 84 -30.870 -40.364 -0.394 0.43 17.90 A N
ANISOU 829 N AASN A 84 3023 2011 1768 -612 54 -406 A N
ATOM 830 N BASN A 84 -30.868 -40.363 -0.394 0.57 17.43 A N
ANISOU 830 N BASN A 84 3052 1840 1731 -546 71 -474 A N
ATOM 831 CA AASN A 84 -29.812 -40.777 -1.314 0.43 18.51 A C
ANISOU 831 CA AASN A 84 3159 1892 1981 -323 270 -416 A C
ATOM 832 CA BASN A 84 -29.795 -40.768 -1.300 0.57 18.26 A C
ANISOU 832 CA BASN A 84 3206 1747 1984 -218 333 -461 A C
ATOM 833 C AASN A 84 -29.379 -39.686 -2.288 0.43 16.01 A C
ANISOU 833 C AASN A 84 2674 1672 1736 -201 106 -307 A C
ATOM 834 C BASN A 84 -29.348 -39.677 -2.267 0.57 15.71 A C
ANISOU 834 C BASN A 84 2674 1605 1690 -37 152 -315 A C
ATOM 835 O AASN A 84 -28.688 -39.990 -3.267 0.43 16.95 A O
ANISOU 835 O AASN A 84 2650 1777 2016 -246 150 -400 A O
ATOM 836 O BASN A 84 -28.603 -39.972 -3.209 0.57 16.42 A O
ANISOU 836 O BASN A 84 2602 1807 1830 77 105 -358 A O
ATOM 837 CB AASN A 84 -30.171 -42.059 -2.081 0.43 22.56 A C
ANISOU 837 CB AASN A 84 3639 2303 2629 -415 437 -382 A C
ATOM 838 CB BASN A 84 -30.106 -42.075 -2.043 0.57 22.57 A C
ANISOU 838 CB BASN A 84 3727 2151 2698 -394 461 -462 A C
ATOM 839 CG AASN A 84 -29.013 -43.027 -2.177 0.43 26.42 A C
ANISOU 839 CG AASN A 84 3981 2930 3127 -303 394 -246 A C
ATOM 840 CG BASN A 84 -29.941 -43.297 -1.164 0.57 26.24 A C
ANISOU 840 CG BASN A 84 4116 2653 3202 -416 254 -427 A C
ATOM 841 ND2AASN A 84 -29.056 -44.078 -1.368 0.43 27.95 A N
ANISOU 841 ND2AASN A 84 4030 3304 3286 -20 463 -173 A N
ATOM 842 ND2BASN A 84 -30.754 -44.319 -1.408 0.57 28.23 A N
ANISOU 842 ND2BASN A 84 4224 3078 3426 -700 157 -240 A N
ATOM 843 OD1AASN A 84 -28.097 -42.841 -2.976 0.43 28.85 A O
ANISOU 843 OD1AASN A 84 4275 3269 3418 -336 212 -173 A O
ATOM 844 OD1BASN A 84 -29.089 -43.325 -0.276 0.57 27.61 A O
ANISOU 844 OD1BASN A 84 4391 2712 3387 -255 261 -477 A O
ATOM 845 N VAL A 85 -29.753 -38.428 -2.052 1.00 14.05 A N
ANISOU 845 N VAL A 85 2367 1548 1424 -213 -57 -180 A N
ATOM 846 CA VAL A 85 -29.413 -37.325 -2.942 1.00 14.42 A C
ANISOU 846 CA VAL A 85 2487 1620 1370 -88 -350 -184 A C
ATOM 847 C VAL A 85 -28.754 -36.217 -2.133 1.00 12.48 A C
ANISOU 847 C VAL A 85 2157 1466 1119 53 -261 1 A C
ATOM 848 O VAL A 85 -29.218 -35.872 -1.039 1.00 12.09 A O
ANISOU 848 O VAL A 85 1916 1525 1152 -26 -256 -101 A O
ATOM 849 CB VAL A 85 -30.663 -36.790 -3.667 1.00 18.50 A C
ANISOU 849 CB VAL A 85 2866 2242 1922 -235 -998 -84 A C
ATOM 850 CG1 VAL A 85 -30.302 -35.620 -4.567 1.00 20.99 A C
ANISOU 850 CG1 VAL A 85 3384 2295 2296 -57 -1345 191 A C
ATOM 851 CG2 VAL A 85 -31.326 -37.901 -4.480 1.00 20.89 A C
ANISOU 851 CG2 VAL A 85 2992 2637 2308 -397 -982 -309 A C
ATOM 852 N ILE A 86 -27.683 -35.646 -2.675 1.00 12.71 A N
ANISOU 852 N ILE A 86 2162 1505 1163 218 -170 -64 A N
ATOM 853 CA ILE A 86 -26.992 -34.545 -2.004 1.00 11.46 A C
ANISOU 853 CA ILE A 86 1840 1384 1130 115 -33 -98 A C
ATOM 854 C ILE A 86 -27.857 -33.289 -2.052 1.00 10.72 A C
ANISOU 854 C ILE A 86 1679 1267 1125 75 -186 15 A C
ATOM 855 O ILE A 86 -28.173 -32.802 -3.147 1.00 11.17 A O
ANISOU 855 O ILE A 86 1551 1513 1182 218 -108 40 A O
ATOM 856 CB ILE A 86 -25.627 -34.263 -2.652 1.00 11.74 A C
ANISOU 856 CB ILE A 86 1815 1463 1184 378 35 -44 A C
ATOM 857 CG1 ILE A 86 -24.739 -35.509 -2.635 1.00 13.04 A C
ANISOU 857 CG1 ILE A 86 2057 1674 1225 458 128 -128 A C
ATOM 858 CG2 ILE A 86 -24.950 -33.093 -1.955 1.00 11.61 A C
ANISOU 858 CG2 ILE A 86 1468 1654 1289 228 44 63 A C
ATOM 859 CD1 ILE A 86 -23.506 -35.398 -3.515 1.00 14.63 A C
ANISOU 859 CD1 ILE A 86 2260 1812 1485 687 177 103 A C
ATOM 860 N PRO A 87 -28.242 -32.718 -0.915 1.00 10.97 A N
ANISOU 860 N PRO A 87 1735 1299 1132 57 -55 -75 A N
ATOM 861 CA PRO A 87 -29.041 -31.487 -0.933 1.00 11.32 A C
ANISOU 861 CA PRO A 87 1676 1384 1242 226 147 -96 A C
ATOM 862 C PRO A 87 -28.170 -30.300 -1.292 1.00 11.08 A C
ANISOU 862 C PRO A 87 1626 1414 1169 297 -62 1 A C
ATOM 863 O PRO A 87 -26.963 -30.303 -1.014 1.00 11.37 A O
ANISOU 863 O PRO A 87 1572 1381 1366 241 18 -36 A O
ATOM 864 CB PRO A 87 -29.530 -31.373 0.518 1.00 11.97 A C
ANISOU 864 CB PRO A 87 1839 1480 1230 245 196 -100 A C
ATOM 865 CG PRO A 87 -28.417 -32.002 1.316 1.00 11.91 A C
ANISOU 865 CG PRO A 87 1893 1510 1124 321 115 -77 A C
ATOM 866 CD PRO A 87 -27.937 -33.161 0.461 1.00 11.44 A C
ANISOU 866 CD PRO A 87 1971 1367 1009 112 -18 -121 A C
ATOM 867 N PRO A 88 -28.752 -29.244 -1.860 1.00 11.30 A N
ANISOU 867 N PRO A 88 1620 1454 1218 105 -56 28 A N
ATOM 868 CA PRO A 88 -27.950 -28.063 -2.197 1.00 11.62 A C
ANISOU 868 CA PRO A 88 1808 1504 1102 107 -87 73 A C
ATOM 869 C PRO A 88 -27.317 -27.432 -0.968 1.00 10.95 A C
ANISOU 869 C PRO A 88 1689 1355 1117 163 -49 -12 A C
ATOM 870 O PRO A 88 -27.949 -27.289 0.080 1.00 11.19 A O
ANISOU 870 O PRO A 88 1718 1457 1076 214 75 -1 A O
ATOM 871 CB PRO A 88 -28.969 -27.116 -2.840 1.00 12.98 A C
ANISOU 871 CB PRO A 88 1966 1690 1277 136 -157 62 A C
ATOM 872 CG PRO A 88 -30.088 -28.004 -3.297 1.00 14.17 A C
ANISOU 872 CG PRO A 88 1965 1808 1610 49 -291 331 A C
ATOM 873 CD PRO A 88 -30.160 -29.096 -2.272 1.00 13.20 A C
ANISOU 873 CD PRO A 88 1861 1662 1494 261 -237 178 A C
ATOM 874 N THR A 89 -26.063 -27.013 -1.121 1.00 11.31 A N
ANISOU 874 N THR A 89 1823 1382 1094 203 8 40 A N
ATOM 875 CA THR A 89 -25.343 -26.375 -0.025 1.00 11.74 A C
ANISOU 875 CA THR A 89 1734 1554 1174 117 46 -38 A C
ATOM 876 C THR A 89 -26.052 -25.112 0.448 1.00 11.18 A C
ANISOU 876 C THR A 89 1647 1401 1201 47 28 22 A C
ATOM 877 O THR A 89 -26.017 -24.789 1.642 1.00 11.49 A O
ANISOU 877 O THR A 89 1608 1569 1188 105 20 10 A O
ATOM 878 CB THR A 89 -23.906 -26.101 -0.473 1.00 12.81 A C
ANISOU 878 CB THR A 89 1704 1718 1446 67 192 -31 A C
ATOM 879 CG2 THR A 89 -23.060 -25.527 0.657 1.00 14.52 A C
ANISOU 879 CG2 THR A 89 1628 2290 1598 24 -13 -263 A C
ATOM 880 OG1 THR A 89 -23.323 -27.333 -0.900 1.00 13.16 A O
ANISOU 880 OG1 THR A 89 1748 1729 1524 165 254 11 A O
ATOM 881 N SER A 90 -26.732 -24.412 -0.462 1.00 11.38 A N
ANISOU 881 N SER A 90 1732 1423 1170 112 10 159 A N
ATOM 882 CA SER A 90 -27.444 -23.190 -0.119 1.00 12.60 A C
ANISOU 882 CA SER A 90 1946 1386 1457 180 153 185 A C
ATOM 883 C SER A 90 -28.792 -23.432 0.548 1.00 12.36 A C
ANISOU 883 C SER A 90 1771 1619 1304 216 -31 115 A C
ATOM 884 O SER A 90 -29.386 -22.470 1.047 1.00 12.74 A O
ANISOU 884 O SER A 90 1648 1637 1555 352 -15 -19 A O
ATOM 885 CB SER A 90 -27.691 -22.379 -1.390 1.00 16.08 A C
ANISOU 885 CB SER A 90 2509 1844 1758 158 174 377 A C
ATOM 886 OG SER A 90 -28.476 -23.133 -2.301 1.00 18.47 A O
ANISOU 886 OG SER A 90 2897 2506 1617 238 37 683 A O
ATOM 887 N ALA A 91 -29.306 -24.662 0.548 1.00 11.62 A N
ANISOU 887 N ALA A 91 1724 1606 1083 54 -27 126 A N
ATOM 888 CA ALA A 91 -30.636 -24.904 1.098 1.00 11.56 A C
ANISOU 888 CA ALA A 91 1575 1626 1193 62 -29 36 A C
ATOM 889 C ALA A 91 -30.653 -24.721 2.610 1.00 10.98 A C
ANISOU 889 C ALA A 91 1503 1676 992 119 -106 18 A C
ATOM 890 O ALA A 91 -29.691 -25.065 3.302 1.00 11.86 A O
ANISOU 890 O ALA A 91 1504 1879 1121 228 -106 -5 A O
ATOM 891 CB ALA A 91 -31.087 -26.328 0.789 1.00 12.27 A C
ANISOU 891 CB ALA A 91 1669 1813 1182 -51 -63 -73 A C
ATOM 892 N THR A 92 -31.764 -24.188 3.126 1.00 11.15 A N
ANISOU 892 N THR A 92 1465 1688 1085 170 -35 1 A N
ATOM 893 CA THR A 92 -31.939 -24.162 4.570 1.00 10.95 A C
ANISOU 893 CA THR A 92 1373 1620 1167 166 -95 22 A C
ATOM 894 C THR A 92 -32.525 -25.477 5.073 1.00 10.47 A C
ANISOU 894 C THR A 92 1245 1686 1048 153 -83 -98 A C
ATOM 895 O THR A 92 -33.189 -26.222 4.345 1.00 10.95 A O
ANISOU 895 O THR A 92 1400 1645 1114 171 -93 -82 A O
ATOM 896 CB THR A 92 -32.853 -23.025 5.037 1.00 11.78 A C
ANISOU 896 CB THR A 92 1496 1563 1419 134 -41 25 A C
ATOM 897 CG2 THR A 92 -32.375 -21.681 4.518 1.00 13.24 A C
ANISOU 897 CG2 THR A 92 1861 1614 1557 69 -111 18 A C
ATOM 898 OG1 THR A 92 -34.201 -23.283 4.614 1.00 11.72 A O
ANISOU 898 OG1 THR A 92 1323 1725 1404 215 -124 -51 A O
ATOM 899 N AMET A 93 -32.266 -25.752 6.354 0.58 10.44 A N
ANISOU 899 N AMET A 93 1345 1548 1073 380 -93 -34 A N
ATOM 900 N BMET A 93 -32.309 -25.735 6.361 0.41 10.95 A N
ANISOU 900 N BMET A 93 1410 1733 1019 -53 25 37 A N
ATOM 901 CA AMET A 93 -32.851 -26.920 7.002 0.58 10.42 A C
ANISOU 901 CA AMET A 93 1471 1474 1014 295 -260 -88 A C
ATOM 902 CA BMET A 93 -32.848 -26.947 6.961 0.41 11.67 A C
ANISOU 902 CA BMET A 93 1532 1826 1076 -157 -120 -23 A C
ATOM 903 C AMET A 93 -34.370 -26.884 6.934 0.58 10.43 A C
ANISOU 903 C AMET A 93 1438 1489 1035 220 -213 -85 A C
ATOM 904 C BMET A 93 -34.372 -26.902 7.060 0.41 11.51 A C
ANISOU 904 C BMET A 93 1443 1774 1157 -39 -57 -178 A C
ATOM 905 O AMET A 93 -35.013 -27.914 6.698 0.58 9.68 A O
ANISOU 905 O AMET A 93 1451 1411 816 134 -88 -146 A O
ATOM 906 O BMET A 93 -35.020 -27.955 7.053 0.41 12.02 A O
ANISOU 906 O BMET A 93 1437 1937 1193 -26 -1 -159 A O
ATOM 907 CB AMET A 93 -32.389 -26.992 8.456 0.58 11.23 A C
ANISOU 907 CB AMET A 93 1664 1503 1101 375 -166 -45 A C
ATOM 908 CB BMET A 93 -32.177 -27.204 8.311 0.41 12.98 A C
ANISOU 908 CB BMET A 93 1836 1930 1167 -83 -304 -195 A C
ATOM 909 CG AMET A 93 -30.920 -27.326 8.614 0.58 11.80 A C
ANISOU 909 CG AMET A 93 1712 1397 1375 103 -180 24 A C
ATOM 910 CG BMET A 93 -30.638 -27.186 8.252 0.41 12.88 A C
ANISOU 910 CG BMET A 93 1751 2132 1011 26 -371 -173 A C
ATOM 911 SD AMET A 93 -30.537 -28.978 8.019 0.58 11.42 A S
ANISOU 911 SD AMET A 93 1367 1582 1388 164 -60 -34 A S
ATOM 912 SD BMET A 93 -29.909 -28.401 7.129 0.41 14.41 A S
ANISOU 912 SD BMET A 93 1792 2268 1415 182 -40 -341 A S
ATOM 913 CE AMET A 93 -29.528 -28.579 6.602 0.58 11.95 A C
ANISOU 913 CE AMET A 93 1435 1758 1346 224 -52 -211 A C
ATOM 914 CE BMET A 93 -30.814 -29.836 7.666 0.41 17.56 A C
ANISOU 914 CE BMET A 93 2359 2478 1834 60 23 -338 A C
ATOM 915 N GLY A 94 -34.962 -25.703 7.133 1.00 11.25 A N
ANISOU 915 N GLY A 94 1413 1630 1232 116 41 -167 A N
ATOM 916 CA GLY A 94 -36.409 -25.593 7.060 1.00 11.85 A C
ANISOU 916 CA GLY A 94 1268 1686 1549 114 -32 -295 A C
ATOM 917 C GLY A 94 -36.946 -25.960 5.689 1.00 11.76 A C
ANISOU 917 C GLY A 94 1277 1545 1647 89 -12 -142 A C
ATOM 918 O GLY A 94 -37.992 -26.614 5.578 1.00 12.40 A O
ANISOU 918 O GLY A 94 1341 1665 1706 -14 -16 -266 A O
ATOM 919 N AGLN A 95 -36.242 -25.551 4.632 0.52 11.89 A N
ANISOU 919 N AGLN A 95 1383 1579 1556 76 -268 -184 A N
ATOM 920 N BGLN A 95 -36.253 -25.538 4.625 0.48 11.24 A N
ANISOU 920 N BGLN A 95 1401 1274 1597 54 -98 -75 A N
ATOM 921 CA AGLN A 95 -36.666 -25.917 3.286 0.52 12.55 A C
ANISOU 921 CA AGLN A 95 1525 1763 1480 199 -314 -97 A C
ATOM 922 CA BGLN A 95 -36.668 -25.923 3.278 0.48 11.48 A C
ANISOU 922 CA BGLN A 95 1494 1327 1540 -6 22 -32 A C
ATOM 923 C AGLN A 95 -36.534 -27.419 3.055 0.52 11.76 A C
ANISOU 923 C AGLN A 95 1413 1627 1426 186 -324 51 A C
ATOM 924 C BGLN A 95 -36.551 -27.430 3.079 0.48 10.96 A C
ANISOU 924 C BGLN A 95 1423 1328 1416 -47 3 -122 A C
ATOM 925 O AGLN A 95 -37.431 -28.046 2.480 0.52 12.99 A O
ANISOU 925 O AGLN A 95 1464 1937 1536 253 -575 159 A O
ATOM 926 O BGLN A 95 -37.463 -28.069 2.542 0.48 12.10 A O
ANISOU 926 O BGLN A 95 1558 1508 1533 -168 -10 -405 A O
ATOM 927 CB AGLN A 95 -35.875 -25.111 2.255 0.52 14.48 A C
ANISOU 927 CB AGLN A 95 1832 2105 1564 248 -489 16 A C
ATOM 928 CB BGLN A 95 -35.856 -25.164 2.223 0.48 12.78 A C
ANISOU 928 CB BGLN A 95 1719 1444 1692 -85 -26 160 A C
ATOM 929 CG AGLN A 95 -36.497 -25.080 0.874 0.52 16.16 A C
ANISOU 929 CG AGLN A 95 2238 2258 1646 473 -731 178 A C
ATOM 930 CG BGLN A 95 -36.114 -25.590 0.767 0.48 14.71 A C
ANISOU 930 CG BGLN A 95 2048 1713 1829 -57 -173 375 A C
ATOM 931 CD AGLN A 95 -36.070 -26.254 0.034 0.52 17.27 A C
ANISOU 931 CD AGLN A 95 2427 2461 1674 391 -377 -82 A C
ATOM 932 CD BGLN A 95 -37.463 -25.132 0.220 0.48 15.48 A C
ANISOU 932 CD BGLN A 95 2054 2087 1742 -208 -245 300 A C
ATOM 933 NE2AGLN A 95 -36.872 -26.587 -0.970 0.52 18.37 A N
ANISOU 933 NE2AGLN A 95 2667 2624 1691 212 -307 -383 A N
ATOM 934 NE2BGLN A 95 -37.911 -25.775 -0.854 0.48 16.07 A N
ANISOU 934 NE2BGLN A 95 2106 2374 1625 -220 -505 494 A N
ATOM 935 OE1AGLN A 95 -35.026 -26.859 0.282 0.52 17.81 A O
ANISOU 935 OE1AGLN A 95 2569 2441 1757 338 -288 -39 A O
ATOM 936 OE1BGLN A 95 -38.087 -24.210 0.746 0.48 16.71 A O
ANISOU 936 OE1BGLN A 95 2171 2220 1958 -45 -234 343 A O
ATOM 937 N LEU A 96 -35.429 -28.018 3.508 1.00 11.36 A N
ANISOU 937 N LEU A 96 1489 1430 1399 146 -114 -76 A N
ATOM 938 CA LEU A 96 -35.273 -29.467 3.385 1.00 11.48 A C
ANISOU 938 CA LEU A 96 1481 1543 1338 154 -158 -189 A C
ATOM 939 C LEU A 96 -36.326 -30.204 4.195 1.00 11.14 A C
ANISOU 939 C LEU A 96 1330 1543 1358 30 -232 -203 A C
ATOM 940 O LEU A 96 -36.844 -31.238 3.756 1.00 12.27 A O
ANISOU 940 O LEU A 96 1581 1593 1486 56 -272 -251 A O
ATOM 941 CB LEU A 96 -33.880 -29.903 3.827 1.00 12.11 A C
ANISOU 941 CB LEU A 96 1428 1720 1452 113 -154 -183 A C
ATOM 942 CG LEU A 96 -32.706 -29.424 2.983 1.00 13.09 A C
ANISOU 942 CG LEU A 96 1514 1881 1578 54 -82 -168 A C
ATOM 943 CD1 LEU A 96 -31.426 -29.995 3.564 1.00 15.08 A C
ANISOU 943 CD1 LEU A 96 1586 2305 1840 -52 -320 -407 A C
ATOM 944 CD2 LEU A 96 -32.870 -29.821 1.524 1.00 13.67 A C
ANISOU 944 CD2 LEU A 96 1699 1954 1540 208 15 77 A C
ATOM 945 N TYR A 97 -36.649 -29.686 5.382 1.00 11.73 A N
ANISOU 945 N TYR A 97 1498 1662 1297 -3 -108 -159 A N
ATOM 946 CA TYR A 97 -37.666 -30.303 6.218 1.00 12.57 A C
ANISOU 946 CA TYR A 97 1511 1672 1594 -69 -21 -159 A C
ATOM 947 C TYR A 97 -39.015 -30.286 5.517 1.00 13.53 A C
ANISOU 947 C TYR A 97 1648 1608 1883 6 -26 -203 A C
ATOM 948 O TYR A 97 -39.718 -31.302 5.474 1.00 14.47 A O
ANISOU 948 O TYR A 97 1696 1716 2088 -281 -121 -229 A O
ATOM 949 CB TYR A 97 -37.748 -29.550 7.547 1.00 13.04 A C
ANISOU 949 CB TYR A 97 1660 1721 1572 -210 274 -360 A C
ATOM 950 CG TYR A 97 -38.742 -30.155 8.499 1.00 12.77 A C
ANISOU 950 CG TYR A 97 1560 1680 1613 -228 182 -349 A C
ATOM 951 CD1 TYR A 97 -38.381 -31.210 9.324 1.00 12.42 A C
ANISOU 951 CD1 TYR A 97 1644 1625 1450 -248 99 -351 A C
ATOM 952 CD2 TYR A 97 -40.047 -29.687 8.564 1.00 13.52 A C
ANISOU 952 CD2 TYR A 97 1620 1733 1783 -63 43 -154 A C
ATOM 953 CE1 TYR A 97 -39.284 -31.781 10.183 1.00 11.89 A C
ANISOU 953 CE1 TYR A 97 1546 1375 1595 -124 87 -319 A C
ATOM 954 CE2 TYR A 97 -40.954 -30.257 9.428 1.00 13.08 A C
ANISOU 954 CE2 TYR A 97 1442 1626 1901 41 -47 -23 A C
ATOM 955 CZ TYR A 97 -40.571 -31.300 10.231 1.00 12.18 A C
ANISOU 955 CZ TYR A 97 1366 1521 1743 -9 1 -205 A C
ATOM 956 OH TYR A 97 -41.488 -31.858 11.088 1.00 12.40 A O
ANISOU 956 OH TYR A 97 1230 1667 1814 0 -55 19 A O
ATOM 957 N AGLN A 98 -39.421 -29.125 5.002 0.55 13.81 A N
ANISOU 957 N AGLN A 98 1546 1567 2135 77 -58 -202 A N
ATOM 958 N BGLN A 98 -39.361 -29.143 4.919 0.45 15.12 A N
ANISOU 958 N BGLN A 98 1638 1734 2375 24 -91 -157 A N
ATOM 959 CA AGLN A 98 -40.715 -29.029 4.336 0.55 14.07 A C
ANISOU 959 CA AGLN A 98 1530 1607 2210 171 -216 -49 A C
ATOM 960 CA BGLN A 98 -40.601 -28.987 4.167 0.45 17.48 A C
ANISOU 960 CA BGLN A 98 1749 2037 2856 60 -303 -12 A C
ATOM 961 C AGLN A 98 -40.853 -30.085 3.250 0.55 12.68 A C
ANISOU 961 C AGLN A 98 1482 1634 1704 -80 -172 -93 A C
ATOM 962 C BGLN A 98 -40.631 -29.870 2.924 0.45 18.36 A C
ANISOU 962 C BGLN A 98 1679 2232 3065 -174 -663 17 A C
ATOM 963 O AGLN A 98 -41.886 -30.754 3.147 0.55 13.77 A O
ANISOU 963 O AGLN A 98 1609 1831 1791 -253 -183 -31 A O
ATOM 964 O BGLN A 98 -41.710 -30.277 2.478 0.45 20.66 A O
ANISOU 964 O BGLN A 98 1845 2475 3531 -479 -771 186 A O
ATOM 965 CB AGLN A 98 -40.864 -27.635 3.733 0.55 16.96 A C
ANISOU 965 CB AGLN A 98 1760 1937 2746 407 -585 -64 A C
ATOM 966 CB BGLN A 98 -40.729 -27.509 3.794 0.45 19.70 A C
ANISOU 966 CB BGLN A 98 2038 2406 3041 144 -427 47 A C
ATOM 967 CG AGLN A 98 -42.165 -27.385 3.012 0.55 20.36 A C
ANISOU 967 CG AGLN A 98 2263 2462 3011 32 -675 30 A C
ATOM 968 CG BGLN A 98 -41.816 -27.126 2.819 0.45 22.48 A C
ANISOU 968 CG BGLN A 98 2521 2839 3183 128 -515 55 A C
ATOM 969 CD AGLN A 98 -42.139 -26.073 2.256 0.55 23.34 A C
ANISOU 969 CD AGLN A 98 2860 2712 3294 -145 -507 119 A C
ATOM 970 CD BGLN A 98 -41.814 -25.630 2.560 0.45 24.80 A C
ANISOU 970 CD BGLN A 98 2912 3045 3464 -52 -436 246 A C
ATOM 971 NE2AGLN A 98 -41.555 -26.090 1.062 0.55 24.15 A N
ANISOU 971 NE2AGLN A 98 3076 2630 3469 -114 -470 417 A N
ATOM 972 NE2BGLN A 98 -41.548 -25.239 1.321 0.45 26.52 A N
ANISOU 972 NE2BGLN A 98 3198 3124 3755 -290 -355 326 A N
ATOM 973 OE1AGLN A 98 -42.618 -25.052 2.745 0.55 25.26 A O
ANISOU 973 OE1AGLN A 98 3201 2919 3478 -184 -516 -195 A O
ATOM 974 OE1BGLN A 98 -42.021 -24.835 3.474 0.45 26.41 A O
ANISOU 974 OE1BGLN A 98 3153 3220 3663 -100 -449 339 A O
ATOM 975 N AGLU A 99 -39.804 -30.260 2.444 0.52 12.67 A N
ANISOU 975 N AGLU A 99 1689 1494 1632 2 -486 -147 A N
ATOM 976 N BGLU A 99 -39.466 -30.177 2.352 0.48 16.65 A N
ANISOU 976 N BGLU A 99 1713 1973 2641 -74 -793 96 A N
ATOM 977 CA AGLU A 99 -39.854 -31.147 1.289 0.52 13.81 A C
ANISOU 977 CA AGLU A 99 1955 1696 1594 -18 -491 -127 A C
ATOM 978 CA BGLU A 99 -39.401 -31.009 1.156 0.48 16.47 A C
ANISOU 978 CA BGLU A 99 1916 1920 2421 -196 -1003 250 A C
ATOM 979 C AGLU A 99 -39.709 -32.614 1.676 0.52 13.49 A C
ANISOU 979 C AGLU A 99 1819 1700 1606 -120 -529 -168 A C
ATOM 980 C BGLU A 99 -39.308 -32.500 1.460 0.48 15.29 A C
ANISOU 980 C BGLU A 99 1933 1742 2136 -314 -953 -3 A C
ATOM 981 O AGLU A 99 -40.372 -33.479 1.090 0.52 14.58 A O
ANISOU 981 O AGLU A 99 1926 1783 1831 -347 -628 -53 A O
ATOM 982 O BGLU A 99 -39.742 -33.314 0.633 0.48 15.41 A O
ANISOU 982 O BGLU A 99 1975 1786 2095 -275 -999 255 A O
ATOM 983 CB AGLU A 99 -38.737 -30.768 0.317 0.52 15.39 A C
ANISOU 983 CB AGLU A 99 2508 1983 1356 -123 -644 -217 A C
ATOM 984 CB BGLU A 99 -38.191 -30.620 0.297 0.48 17.31 A C
ANISOU 984 CB BGLU A 99 2255 1935 2387 -344 -1159 448 A C
ATOM 985 CG AGLU A 99 -38.862 -29.377 -0.260 0.52 19.24 A C
ANISOU 985 CG AGLU A 99 2926 2429 1956 -296 -657 -50 A C
ATOM 986 CG BGLU A 99 -38.262 -29.253 -0.372 0.48 19.43 A C
ANISOU 986 CG BGLU A 99 2640 2291 2450 -195 -1303 554 A C
ATOM 987 CD AGLU A 99 -40.149 -29.202 -1.023 0.52 21.15 A C
ANISOU 987 CD AGLU A 99 3088 2725 2224 -36 -680 95 A C
ATOM 988 CD BGLU A 99 -36.967 -28.894 -1.089 0.48 23.00 A C
ANISOU 988 CD BGLU A 99 3273 2710 2757 -38 -1112 523 A C
ATOM 989 OE1AGLU A 99 -40.482 -30.099 -1.826 0.52 21.35 A O
ANISOU 989 OE1AGLU A 99 3079 3033 2002 188 -884 31 A O
ATOM 990 OE1BGLU A 99 -35.987 -29.659 -0.964 0.48 25.52 A O
ANISOU 990 OE1BGLU A 99 3469 2906 3321 9 -859 559 A O
ATOM 991 OE2AGLU A 99 -40.834 -28.182 -0.805 0.52 22.42 A O
ANISOU 991 OE2AGLU A 99 3081 2833 2604 235 -927 -5 A O
ATOM 992 OE2BGLU A 99 -36.924 -27.851 -1.776 0.48 23.46 A O
ANISOU 992 OE2BGLU A 99 3575 2837 2501 -284 -838 239 A O
ATOM 993 N AHIS A 100 -38.842 -32.917 2.647 0.55 12.63 A N
ANISOU 993 N AHIS A 100 1756 1615 1429 46 -519 -215 A N
ATOM 994 N BHIS A 100 -38.753 -32.886 2.622 0.45 13.72 A N
ANISOU 994 N BHIS A 100 1837 1582 1794 -86 -726 -107 A N
ATOM 995 CA AHIS A 100 -38.364 -34.279 2.841 0.55 12.38 A C
ANISOU 995 CA AHIS A 100 1649 1618 1436 -11 -189 -121 A C
ATOM 996 CA BHIS A 100 -38.361 -34.276 2.827 0.45 12.81 A C
ANISOU 996 CA BHIS A 100 1703 1604 1561 -105 -332 -91 A C
ATOM 997 C AHIS A 100 -38.678 -34.891 4.196 0.55 12.67 A C
ANISOU 997 C AHIS A 100 1604 1676 1534 -57 -314 -145 A C
ATOM 998 C BHIS A 100 -38.677 -34.883 4.189 0.45 12.79 A C
ANISOU 998 C BHIS A 100 1645 1652 1564 -68 -333 -131 A C
ATOM 999 O AHIS A 100 -38.311 -36.050 4.418 0.55 12.79 A O
ANISOU 999 O AHIS A 100 1757 1554 1547 -121 -379 -96 A O
ATOM 1000 O BHIS A 100 -38.305 -36.040 4.407 0.45 13.03 A O
ANISOU 1000 O BHIS A 100 1816 1535 1598 -68 -352 -126 A O
ATOM 1001 CB AHIS A 100 -36.848 -34.363 2.629 0.55 13.11 A C
ANISOU 1001 CB AHIS A 100 1734 1751 1497 -15 -39 -74 A C
ATOM 1002 CB BHIS A 100 -36.856 -34.468 2.573 0.45 13.14 A C
ANISOU 1002 CB BHIS A 100 1728 1725 1541 -250 -256 -99 A C
ATOM 1003 CG AHIS A 100 -36.384 -33.830 1.312 0.55 15.39 A C
ANISOU 1003 CG AHIS A 100 2113 2175 1561 95 -139 30 A C
ATOM 1004 CG BHIS A 100 -36.370 -33.883 1.286 0.45 15.30 A C
ANISOU 1004 CG BHIS A 100 2098 2134 1583 14 -176 27 A C
ATOM 1005 CD2AHIS A 100 -35.580 -32.783 1.015 0.55 16.93 A C
ANISOU 1005 CD2AHIS A 100 2237 2346 1848 69 152 137 A C
ATOM 1006 CD2BHIS A 100 -35.553 -32.831 1.044 0.45 16.55 A C
ANISOU 1006 CD2BHIS A 100 2214 2297 1776 3 131 165 A C
ATOM 1007 ND1AHIS A 100 -36.731 -34.403 0.107 0.55 18.16 A N
ANISOU 1007 ND1AHIS A 100 2601 2513 1788 -26 71 -56 A N
ATOM 1008 ND1BHIS A 100 -36.700 -34.404 0.054 0.45 18.02 A N
ANISOU 1008 ND1BHIS A 100 2577 2483 1787 -32 26 -68 A N
ATOM 1009 CE1AHIS A 100 -36.168 -33.723 -0.877 0.55 19.11 A C
ANISOU 1009 CE1AHIS A 100 2600 2559 2103 -126 117 67 A C
ATOM 1010 CE1BHIS A 100 -36.119 -33.689 -0.893 0.45 18.79 A C
ANISOU 1010 CE1BHIS A 100 2573 2534 2034 -111 85 52 A C
ATOM 1011 NE2AHIS A 100 -35.463 -32.736 -0.353 0.55 18.66 A N
ANISOU 1011 NE2AHIS A 100 2500 2542 2047 -41 198 131 A N
ATOM 1012 NE2BHIS A 100 -35.415 -32.729 -0.318 0.45 18.10 A N
ANISOU 1012 NE2BHIS A 100 2444 2503 1930 -63 147 142 A N
ATOM 1013 N HIS A 101 -39.315 -34.168 5.116 1.00 12.46 A N
ANISOU 1013 N HIS A 101 1554 1646 1534 -137 -275 -139 A N
ATOM 1014 CA HIS A 101 -39.597 -34.774 6.416 1.00 12.74 A C
ANISOU 1014 CA HIS A 101 1709 1649 1482 -142 -273 -214 A C
ATOM 1015 C HIS A 101 -40.438 -36.037 6.257 1.00 12.59 A C
ANISOU 1015 C HIS A 101 1567 1698 1520 -12 -383 -190 A C
ATOM 1016 O HIS A 101 -41.279 -36.147 5.362 1.00 13.84 A O
ANISOU 1016 O HIS A 101 1563 1897 1798 15 -509 -306 A O
ATOM 1017 CB HIS A 101 -40.285 -33.802 7.377 1.00 13.87 A C
ANISOU 1017 CB HIS A 101 1787 1667 1816 -229 -132 -391 A C
ATOM 1018 CG HIS A 101 -41.729 -33.559 7.071 1.00 16.49 A C
ANISOU 1018 CG HIS A 101 1747 1974 2543 -54 12 -203 A C
ATOM 1019 CD2 HIS A 101 -42.335 -32.553 6.400 1.00 21.33 A C
ANISOU 1019 CD2 HIS A 101 2088 2398 3616 377 -414 279 A C
ATOM 1020 ND1 HIS A 101 -42.735 -34.413 7.473 1.00 19.09 A N
ANISOU 1020 ND1 HIS A 101 1744 2394 3117 17 -47 -261 A N
ATOM 1021 CE1 HIS A 101 -43.898 -33.945 7.059 1.00 23.77 A C
ANISOU 1021 CE1 HIS A 101 2154 2913 3965 222 -202 -64 A C
ATOM 1022 NE2 HIS A 101 -43.684 -32.816 6.408 1.00 23.99 A N
ANISOU 1022 NE2 HIS A 101 2006 2906 4201 457 -509 203 A N
ATOM 1023 N GLU A 102 -40.183 -37.006 7.125 1.00 12.64 A N
ANISOU 1023 N GLU A 102 1517 1568 1719 -166 -282 -178 A N
ATOM 1024 CA GLU A 102 -40.936 -38.245 7.129 1.00 12.79 A C
ANISOU 1024 CA GLU A 102 1518 1628 1714 -132 -90 -227 A C
ATOM 1025 C GLU A 102 -42.215 -38.081 7.950 1.00 13.36 A C
ANISOU 1025 C GLU A 102 1528 1744 1803 -9 -166 -171 A C
ATOM 1026 O GLU A 102 -42.471 -37.041 8.568 1.00 13.67 A O
ANISOU 1026 O GLU A 102 1650 1715 1831 61 -74 -147 A O
ATOM 1027 CB GLU A 102 -40.060 -39.399 7.613 1.00 13.67 A C
ANISOU 1027 CB GLU A 102 1548 1661 1987 127 -41 -243 A C
ATOM 1028 CG GLU A 102 -38.898 -39.673 6.671 1.00 14.53 A C
ANISOU 1028 CG GLU A 102 1748 1750 2021 98 -240 -176 A C
ATOM 1029 CD GLU A 102 -38.233 -41.015 6.887 1.00 16.01 A C
ANISOU 1029 CD GLU A 102 1849 1971 2263 28 -35 -168 A C
ATOM 1030 OE1 GLU A 102 -38.689 -41.780 7.762 1.00 16.61 A O
ANISOU 1030 OE1 GLU A 102 2038 1963 2312 -19 -112 -139 A O
ATOM 1031 OE2 GLU A 102 -37.252 -41.302 6.169 1.00 17.04 A O
ANISOU 1031 OE2 GLU A 102 2070 2159 2244 45 -27 -362 A O
ATOM 1032 N GLU A 103 -43.029 -39.135 7.960 1.00 14.34 A N
ANISOU 1032 N GLU A 103 1444 1943 2060 -251 -105 -156 A N
ATOM 1033 CA GLU A 103 -44.309 -39.081 8.651 1.00 16.60 A C
ANISOU 1033 CA GLU A 103 1655 2343 2309 -374 -52 -234 A C
ATOM 1034 C GLU A 103 -44.167 -39.029 10.166 1.00 14.76 A C
ANISOU 1034 C GLU A 103 1451 1963 2192 -265 -6 -77 A C
ATOM 1035 O GLU A 103 -45.156 -38.745 10.853 1.00 16.57 A O
ANISOU 1035 O GLU A 103 1492 2380 2422 -147 -55 -138 A O
ATOM 1036 CB GLU A 103 -45.195 -40.242 8.201 1.00 20.67 A C
ANISOU 1036 CB GLU A 103 2113 2977 2764 -843 -243 -414 A C
ATOM 1037 CG GLU A 103 -45.610 -40.121 6.735 1.00 25.29 A C
ANISOU 1037 CG GLU A 103 2871 3568 3169 -920 -672 -424 A C
ATOM 1038 CD GLU A 103 -46.587 -41.193 6.288 1.00 32.41 A C
ANISOU 1038 CD GLU A 103 4043 4214 4057 -581 -637 -54 A C
ATOM 1039 OE1 GLU A 103 -46.850 -42.133 7.067 1.00 34.88 A O
ANISOU 1039 OE1 GLU A 103 4401 4282 4572 -738 -307 165 A O
ATOM 1040 OE2 GLU A 103 -47.097 -41.090 5.150 1.00 36.37 A O
ANISOU 1040 OE2 GLU A 103 4533 4684 4603 -348 -686 -88 A O
ATOM 1041 N ASP A 104 -42.973 -39.273 10.701 1.00 13.47 A N
ANISOU 1041 N ASP A 104 1435 1713 1972 -170 -65 -51 A N
ATOM 1042 CA ASP A 104 -42.720 -39.075 12.121 1.00 13.31 A C
ANISOU 1042 CA ASP A 104 1409 1627 2022 -210 84 12 A C
ATOM 1043 C ASP A 104 -42.331 -37.643 12.459 1.00 12.37 A C
ANISOU 1043 C ASP A 104 1192 1651 1858 -71 3 -1 A C
ATOM 1044 O ASP A 104 -41.978 -37.366 13.609 1.00 13.40 A O
ANISOU 1044 O ASP A 104 1259 1919 1914 -29 15 146 A O
ATOM 1045 CB ASP A 104 -41.665 -40.059 12.643 1.00 14.75 A C
ANISOU 1045 CB ASP A 104 1482 1748 2373 42 119 261 A C
ATOM 1046 CG ASP A 104 -40.315 -39.902 11.966 1.00 14.28 A C
ANISOU 1046 CG ASP A 104 1556 1622 2246 138 -12 233 A C
ATOM 1047 OD1 ASP A 104 -40.150 -38.985 11.131 1.00 13.29 A O
ANISOU 1047 OD1 ASP A 104 1397 1612 2041 83 -25 47 A O
ATOM 1048 OD2 ASP A 104 -39.418 -40.713 12.275 1.00 15.17 A O
ANISOU 1048 OD2 ASP A 104 1624 1800 2339 229 188 420 A O
ATOM 1049 N PHE A 105 -42.383 -36.735 11.485 1.00 11.76 A N
ANISOU 1049 N PHE A 105 1124 1576 1769 -22 8 -55 A N
ATOM 1050 CA PHE A 105 -42.046 -35.325 11.648 1.00 12.34 A C
ANISOU 1050 CA PHE A 105 1362 1609 1718 -66 87 -158 A C
ATOM 1051 C PHE A 105 -40.552 -35.055 11.801 1.00 11.23 A C
ANISOU 1051 C PHE A 105 1276 1494 1495 68 -42 -72 A C
ATOM 1052 O PHE A 105 -40.178 -33.928 12.151 1.00 12.02 A O
ANISOU 1052 O PHE A 105 1330 1540 1698 81 -180 -163 A O
ATOM 1053 CB PHE A 105 -42.862 -34.637 12.750 1.00 14.21 A C
ANISOU 1053 CB PHE A 105 1444 1839 2117 60 342 -14 A C
ATOM 1054 CG PHE A 105 -44.340 -34.734 12.543 1.00 15.60 A C
ANISOU 1054 CG PHE A 105 1556 1906 2465 284 506 337 A C
ATOM 1055 CD1 PHE A 105 -44.953 -34.042 11.515 1.00 19.41 A C
ANISOU 1055 CD1 PHE A 105 1556 2816 3004 662 560 899 A C
ATOM 1056 CD2 PHE A 105 -45.115 -35.526 13.363 1.00 16.26 A C
ANISOU 1056 CD2 PHE A 105 1702 1948 2528 -195 546 80 A C
ATOM 1057 CE1 PHE A 105 -46.314 -34.124 11.315 1.00 21.60 A C
ANISOU 1057 CE1 PHE A 105 1751 3123 3332 652 411 920 A C
ATOM 1058 CE2 PHE A 105 -46.481 -35.616 13.169 1.00 16.59 A C
ANISOU 1058 CE2 PHE A 105 1584 2001 2717 8 521 38 A C
ATOM 1059 CZ PHE A 105 -47.081 -34.911 12.142 1.00 19.45 A C
ANISOU 1059 CZ PHE A 105 1661 2659 3069 437 612 571 A C
ATOM 1060 N PHE A 106 -39.690 -36.036 11.524 1.00 11.29 A N
ANISOU 1060 N PHE A 106 1247 1586 1457 -8 -8 50 A N
ATOM 1061 CA PHE A 106 -38.248 -35.827 11.512 1.00 11.29 A C
ANISOU 1061 CA PHE A 106 1143 1666 1480 10 -193 -39 A C
ATOM 1062 C PHE A 106 -37.718 -35.760 10.083 1.00 10.76 A C
ANISOU 1062 C PHE A 106 1150 1533 1404 35 -291 -50 A C
ATOM 1063 O PHE A 106 -38.268 -36.379 9.166 1.00 11.99 A O
ANISOU 1063 O PHE A 106 1298 1684 1574 -104 -272 -111 A O
ATOM 1064 CB PHE A 106 -37.518 -36.962 12.238 1.00 12.04 A C
ANISOU 1064 CB PHE A 106 1418 1788 1368 121 -91 116 A C
ATOM 1065 CG PHE A 106 -37.547 -36.852 13.740 1.00 11.59 A C
ANISOU 1065 CG PHE A 106 1299 1601 1502 128 -131 228 A C
ATOM 1066 CD1 PHE A 106 -38.660 -37.256 14.462 1.00 13.29 A C
ANISOU 1066 CD1 PHE A 106 1467 2053 1529 -113 -28 49 A C
ATOM 1067 CD2 PHE A 106 -36.448 -36.364 14.438 1.00 11.23 A C
ANISOU 1067 CD2 PHE A 106 1263 1512 1493 145 -107 53 A C
ATOM 1068 CE1 PHE A 106 -38.679 -37.167 15.844 1.00 14.02 A C
ANISOU 1068 CE1 PHE A 106 1425 2323 1580 13 81 58 A C
ATOM 1069 CE2 PHE A 106 -36.468 -36.275 15.833 1.00 11.81 A C
ANISOU 1069 CE2 PHE A 106 1440 1468 1578 250 -188 74 A C
ATOM 1070 CZ PHE A 106 -37.587 -36.674 16.532 1.00 12.79 A C
ANISOU 1070 CZ PHE A 106 1459 1848 1551 123 10 110 A C
ATOM 1071 N LEU A 107 -36.641 -34.991 9.908 1.00 10.65 A N
ANISOU 1071 N LEU A 107 1282 1423 1341 -74 -69 -59 A N
ATOM 1072 CA LEU A 107 -35.815 -35.015 8.707 1.00 10.38 A C
ANISOU 1072 CA LEU A 107 1260 1312 1373 124 -142 -43 A C
ATOM 1073 C LEU A 107 -34.621 -35.925 8.965 1.00 10.46 A C
ANISOU 1073 C LEU A 107 1406 1274 1296 49 -199 -134 A C
ATOM 1074 O LEU A 107 -34.026 -35.875 10.041 1.00 12.06 A O
ANISOU 1074 O LEU A 107 1718 1562 1300 341 -447 -239 A O
ATOM 1075 CB LEU A 107 -35.305 -33.602 8.420 1.00 10.77 A C
ANISOU 1075 CB LEU A 107 1297 1408 1385 153 -114 -73 A C
ATOM 1076 CG LEU A 107 -34.315 -33.414 7.265 1.00 10.95 A C
ANISOU 1076 CG LEU A 107 1361 1564 1236 -18 -82 -12 A C
ATOM 1077 CD1 LEU A 107 -34.925 -33.805 5.918 1.00 12.04 A C
ANISOU 1077 CD1 LEU A 107 1648 1748 1177 19 -121 -11 A C
ATOM 1078 CD2 LEU A 107 -33.778 -31.983 7.242 1.00 12.54 A C
ANISOU 1078 CD2 LEU A 107 1597 1726 1442 -25 -178 89 A C
ATOM 1079 N TYR A 108 -34.271 -36.751 7.978 1.00 10.37 A N
ANISOU 1079 N TYR A 108 1290 1305 1345 88 -169 -138 A N
ATOM 1080 CA TYR A 108 -33.201 -37.740 8.103 1.00 10.61 A C
ANISOU 1080 CA TYR A 108 1477 1344 1212 104 -151 -88 A C
ATOM 1081 C TYR A 108 -32.057 -37.364 7.168 1.00 10.57 A C
ANISOU 1081 C TYR A 108 1539 1315 1163 160 -228 -48 A C
ATOM 1082 O TYR A 108 -32.260 -37.237 5.957 1.00 12.03 A O
ANISOU 1082 O TYR A 108 1554 1756 1262 66 -268 -61 A O
ATOM 1083 CB TYR A 108 -33.733 -39.144 7.781 1.00 11.05 A C
ANISOU 1083 CB TYR A 108 1570 1311 1319 -31 -145 -79 A C
ATOM 1084 CG TYR A 108 -34.597 -39.721 8.882 1.00 11.27 A C
ANISOU 1084 CG TYR A 108 1444 1384 1454 126 -93 -173 A C
ATOM 1085 CD1 TYR A 108 -35.923 -39.336 9.034 1.00 11.58 A C
ANISOU 1085 CD1 TYR A 108 1312 1377 1712 31 -28 -186 A C
ATOM 1086 CD2 TYR A 108 -34.074 -40.629 9.789 1.00 11.54 A C
ANISOU 1086 CD2 TYR A 108 1565 1372 1448 103 -161 -191 A C
ATOM 1087 CE1 TYR A 108 -36.699 -39.842 10.063 1.00 12.39 A C
ANISOU 1087 CE1 TYR A 108 1428 1432 1849 -68 21 -111 A C
ATOM 1088 CE2 TYR A 108 -34.836 -41.143 10.809 1.00 11.90 A C
ANISOU 1088 CE2 TYR A 108 1567 1422 1532 75 -3 -192 A C
ATOM 1089 CZ TYR A 108 -36.149 -40.744 10.948 1.00 12.42 A C
ANISOU 1089 CZ TYR A 108 1572 1406 1743 86 -71 -113 A C
ATOM 1090 OH TYR A 108 -36.910 -41.259 11.975 1.00 13.21 A O
ANISOU 1090 OH TYR A 108 1633 1586 1800 55 94 46 A O
ATOM 1091 N ILE A 109 -30.858 -37.207 7.728 1.00 10.47 A N
ANISOU 1091 N ILE A 109 1460 1351 1166 178 -150 25 A N
ATOM 1092 CA ILE A 109 -29.668 -36.823 6.976 1.00 10.62 A C
ANISOU 1092 CA ILE A 109 1353 1403 1281 148 -115 17 A C
ATOM 1093 C ILE A 109 -28.574 -37.848 7.237 1.00 10.10 A C
ANISOU 1093 C ILE A 109 1307 1398 1134 210 -164 -44 A C
ATOM 1094 O ILE A 109 -28.267 -38.151 8.397 1.00 11.03 A O
ANISOU 1094 O ILE A 109 1498 1514 1178 322 -103 -20 A O
ATOM 1095 CB ILE A 109 -29.159 -35.432 7.408 1.00 11.84 A C
ANISOU 1095 CB ILE A 109 1470 1396 1634 226 -26 -48 A C
ATOM 1096 CG1 ILE A 109 -30.200 -34.356 7.148 1.00 14.48 A C
ANISOU 1096 CG1 ILE A 109 1740 1663 2098 426 -382 -236 A C
ATOM 1097 CG2 ILE A 109 -27.850 -35.094 6.712 1.00 14.16 A C
ANISOU 1097 CG2 ILE A 109 1646 1552 2181 -50 179 -143 A C
ATOM 1098 CD1 ILE A 109 -29.742 -33.016 7.625 1.00 18.08 A C
ANISOU 1098 CD1 ILE A 109 2035 2037 2797 381 -421 -419 A C
ATOM 1099 N ALA A 110 -27.959 -38.347 6.170 1.00 10.47 A N
ANISOU 1099 N ALA A 110 1431 1375 1171 229 -60 11 A N
ATOM 1100 CA ALA A 110 -26.750 -39.147 6.286 1.00 11.06 A C
ANISOU 1100 CA ALA A 110 1481 1502 1217 343 5 9 A C
ATOM 1101 C ALA A 110 -25.554 -38.304 5.870 1.00 10.62 A C
ANISOU 1101 C ALA A 110 1396 1666 972 259 31 60 A C
ATOM 1102 O ALA A 110 -25.652 -37.465 4.973 1.00 11.79 A O
ANISOU 1102 O ALA A 110 1541 1805 1135 129 -74 340 A O
ATOM 1103 CB ALA A 110 -26.837 -40.397 5.408 1.00 13.15 A C
ANISOU 1103 CB ALA A 110 1751 1487 1757 399 80 -37 A C
ATOM 1104 N TYR A 111 -24.411 -38.533 6.511 1.00 11.04 A N
ANISOU 1104 N TYR A 111 1484 1593 1117 372 -2 151 A N
ATOM 1105 CA TYR A 111 -23.183 -37.874 6.089 1.00 10.90 A C
ANISOU 1105 CA TYR A 111 1366 1550 1226 200 112 204 A C
ATOM 1106 C TYR A 111 -22.108 -38.898 5.746 1.00 10.64 A C
ANISOU 1106 C TYR A 111 1349 1566 1128 361 63 153 A C
ATOM 1107 O TYR A 111 -22.089 -40.011 6.282 1.00 11.67 A O
ANISOU 1107 O TYR A 111 1553 1562 1319 477 103 168 A O
ATOM 1108 CB TYR A 111 -22.684 -36.817 7.103 1.00 11.42 A C
ANISOU 1108 CB TYR A 111 1461 1590 1287 200 -76 143 A C
ATOM 1109 CG TYR A 111 -22.096 -37.358 8.378 1.00 11.21 A C
ANISOU 1109 CG TYR A 111 1465 1510 1284 279 91 121 A C
ATOM 1110 CD1 TYR A 111 -22.905 -37.646 9.467 1.00 11.53 A C
ANISOU 1110 CD1 TYR A 111 1463 1642 1277 144 82 138 A C
ATOM 1111 CD2 TYR A 111 -20.724 -37.547 8.510 1.00 11.35 A C
ANISOU 1111 CD2 TYR A 111 1477 1465 1370 258 -43 131 A C
ATOM 1112 CE1 TYR A 111 -22.369 -38.132 10.651 1.00 11.84 A C
ANISOU 1112 CE1 TYR A 111 1402 1808 1287 226 -23 -23 A C
ATOM 1113 CE2 TYR A 111 -20.175 -38.039 9.686 1.00 11.25 A C
ANISOU 1113 CE2 TYR A 111 1433 1481 1362 214 -46 -10 A C
ATOM 1114 CZ TYR A 111 -21.005 -38.331 10.759 1.00 11.12 A C
ANISOU 1114 CZ TYR A 111 1465 1476 1285 211 -14 111 A C
ATOM 1115 OH TYR A 111 -20.497 -38.815 11.945 1.00 12.00 A O
ANISOU 1115 OH TYR A 111 1510 1726 1324 267 48 177 A O
ATOM 1116 N SER A 112 -21.199 -38.500 4.862 1.00 11.49 A N
ANISOU 1116 N SER A 112 1480 1718 1167 305 165 155 A N
ATOM 1117 CA SER A 112 -20.225 -39.436 4.331 1.00 11.97 A C
ANISOU 1117 CA SER A 112 1619 1661 1267 263 126 21 A C
ATOM 1118 C SER A 112 -19.015 -38.688 3.789 1.00 12.03 A C
ANISOU 1118 C SER A 112 1568 1842 1161 379 7 30 A C
ATOM 1119 O SER A 112 -19.060 -37.475 3.554 1.00 13.10 A O
ANISOU 1119 O SER A 112 1670 1847 1460 360 84 166 A O
ATOM 1120 CB SER A 112 -20.847 -40.272 3.208 1.00 13.62 A C
ANISOU 1120 CB SER A 112 1705 1987 1484 197 143 -51 A C
ATOM 1121 OG SER A 112 -19.937 -41.253 2.756 1.00 14.56 A O
ANISOU 1121 OG SER A 112 1863 2183 1485 150 253 -214 A O
ATOM 1122 N ASP A 113 -17.933 -39.443 3.582 1.00 11.90 A N
ANISOU 1122 N ASP A 113 1538 1852 1132 381 26 -32 A N
ATOM 1123 CA ASP A 113 -16.775 -38.969 2.842 1.00 13.92 A C
ANISOU 1123 CA ASP A 113 1671 2357 1261 318 131 149 A C
ATOM 1124 C ASP A 113 -16.845 -39.320 1.360 1.00 14.81 A C
ANISOU 1124 C ASP A 113 1816 2508 1305 602 304 222 A C
ATOM 1125 O ASP A 113 -15.921 -38.980 0.613 1.00 18.00 A O
ANISOU 1125 O ASP A 113 1952 3105 1780 356 625 293 A O
ATOM 1126 CB ASP A 113 -15.471 -39.503 3.454 1.00 16.99 A C
ANISOU 1126 CB ASP A 113 1693 2919 1842 480 -152 -6 A C
ATOM 1127 CG ASP A 113 -15.433 -41.020 3.564 1.00 20.33 A C
ANISOU 1127 CG ASP A 113 1953 3526 2245 1204 30 198 A C
ATOM 1128 OD1 ASP A 113 -16.429 -41.704 3.261 1.00 19.10 A O
ANISOU 1128 OD1 ASP A 113 2404 2976 1876 1223 140 539 A O
ATOM 1129 OD2 ASP A 113 -14.376 -41.540 3.974 1.00 26.79 A O
ANISOU 1129 OD2 ASP A 113 2451 4270 3458 1247 -264 84 A O
ATOM 1130 N AGLU A 114 -17.931 -39.943 0.904 0.54 14.36 A N
ANISOU 1130 N AGLU A 114 1802 2470 1182 712 -27 153 A N
ATOM 1131 N BGLU A 114 -17.893 -40.023 0.939 0.46 15.05 A N
ANISOU 1131 N BGLU A 114 1911 2578 1231 617 251 -11 A N
ATOM 1132 CA AGLU A 114 -18.125 -40.274 -0.501 0.54 15.12 A C
ANISOU 1132 CA AGLU A 114 2158 2456 1132 850 -140 122 A C
ATOM 1133 CA BGLU A 114 -18.051 -40.498 -0.426 0.46 16.33 A C
ANISOU 1133 CA BGLU A 114 2367 2603 1236 674 89 -257 A C
ATOM 1134 C AGLU A 114 -19.384 -39.589 -1.024 0.54 12.40 A C
ANISOU 1134 C AGLU A 114 1786 1849 1078 382 -78 84 A C
ATOM 1135 C BGLU A 114 -19.087 -39.650 -1.152 0.46 14.84 A C
ANISOU 1135 C BGLU A 114 1943 2408 1288 589 -55 -187 A C
ATOM 1136 O AGLU A 114 -20.292 -39.251 -0.262 0.54 12.25 A O
ANISOU 1136 O AGLU A 114 1755 1697 1201 13 -3 190 A O
ATOM 1137 O BGLU A 114 -20.056 -39.174 -0.554 0.46 13.93 A O
ANISOU 1137 O BGLU A 114 1824 2231 1239 629 -18 -253 A O
ATOM 1138 CB AGLU A 114 -18.225 -41.795 -0.697 0.54 20.03 A C
ANISOU 1138 CB AGLU A 114 2841 2967 1802 1200 -275 25 A C
ATOM 1139 CB BGLU A 114 -18.494 -41.966 -0.447 0.46 18.33 A C
ANISOU 1139 CB BGLU A 114 3026 2594 1344 814 63 -633 A C
ATOM 1140 CG AGLU A 114 -17.827 -42.284 -2.082 0.54 26.19 A C
ANISOU 1140 CG AGLU A 114 3590 3743 2617 948 -234 170 A C
ATOM 1141 CG BGLU A 114 -17.630 -42.882 -1.307 0.46 21.30 A C
ANISOU 1141 CG BGLU A 114 3585 2816 1692 758 212 -656 A C
ATOM 1142 CD AGLU A 114 -17.715 -43.797 -2.161 0.54 30.59 A C
ANISOU 1142 CD AGLU A 114 4052 4351 3221 732 53 7 A C
ATOM 1143 CD BGLU A 114 -17.574 -42.453 -2.765 0.46 22.99 A C
ANISOU 1143 CD BGLU A 114 3692 3093 1952 583 599 -732 A C
ATOM 1144 OE1AGLU A 114 -18.151 -44.479 -1.210 0.54 32.19 A O
ANISOU 1144 OE1AGLU A 114 4195 4526 3508 551 -10 65 A O
ATOM 1145 OE1BGLU A 114 -16.808 -41.520 -3.082 0.46 23.83 A O
ANISOU 1145 OE1BGLU A 114 3733 3015 2306 476 450 -938 A O
ATOM 1146 OE2AGLU A 114 -17.189 -44.304 -3.174 0.54 32.73 A O
ANISOU 1146 OE2AGLU A 114 4288 4626 3523 696 259 -19 A O
ATOM 1147 OE2BGLU A 114 -18.301 -43.043 -3.592 0.46 24.73 A O
ANISOU 1147 OE2BGLU A 114 3633 3410 2354 318 798 -269 A O
ATOM 1148 N ASER A 115 -19.432 -39.386 -2.344 0.54 11.90 A N
ANISOU 1148 N ASER A 115 1884 1565 1073 299 -74 95 A N
ATOM 1149 N BSER A 115 -18.882 -39.485 -2.455 0.46 14.11 A N
ANISOU 1149 N BSER A 115 1898 2229 1232 540 -188 80 A N
ATOM 1150 CA ASER A 115 -20.519 -38.645 -2.981 0.54 11.36 A C
ANISOU 1150 CA ASER A 115 1770 1336 1209 181 -75 -19 A C
ATOM 1151 CA BSER A 115 -19.682 -38.574 -3.262 0.46 14.16 A C
ANISOU 1151 CA BSER A 115 1992 2045 1341 421 -200 32 A C
ATOM 1152 C ASER A 115 -21.673 -39.536 -3.416 0.54 11.17 A C
ANISOU 1152 C ASER A 115 1797 1482 966 66 12 -74 A C
ATOM 1153 C BSER A 115 -20.928 -39.224 -3.851 0.46 14.31 A C
ANISOU 1153 C BSER A 115 2112 1903 1423 650 -290 -161 A C
ATOM 1154 O ASER A 115 -22.657 -39.032 -3.966 0.54 11.50 A O
ANISOU 1154 O ASER A 115 1643 1566 1160 -51 292 216 A O
ATOM 1155 O BSER A 115 -21.726 -38.529 -4.491 0.46 15.52 A O
ANISOU 1155 O BSER A 115 2209 2053 1634 611 -498 -330 A O
ATOM 1156 CB ASER A 115 -20.003 -37.840 -4.182 0.54 10.71 A C
ANISOU 1156 CB ASER A 115 1479 1376 1215 239 -55 -155 A C
ATOM 1157 CB BSER A 115 -18.830 -38.005 -4.394 0.46 13.06 A C
ANISOU 1157 CB BSER A 115 1777 1932 1254 267 -125 -110 A C
ATOM 1158 OG ASER A 115 -19.837 -38.660 -5.323 0.54 11.07 A O
ANISOU 1158 OG ASER A 115 1626 1591 988 81 112 68 A O
ATOM 1159 OG BSER A 115 -18.468 -39.028 -5.307 0.46 13.52 A O
ANISOU 1159 OG BSER A 115 1890 1948 1299 302 121 30 A O
ATOM 1160 N AVAL A 116 -21.576 -40.839 -3.187 0.54 12.51 A N
ANISOU 1160 N AVAL A 116 2007 1459 1287 262 220 -136 A N
ATOM 1161 N BVAL A 116 -21.094 -40.535 -3.664 0.46 15.78 A N
ANISOU 1161 N BVAL A 116 2468 1824 1705 305 166 -326 A N
ATOM 1162 CA AVAL A 116 -22.656 -41.781 -3.446 0.54 13.91 A C
ANISOU 1162 CA AVAL A 116 2444 1644 1199 286 274 390 A C
ATOM 1163 CA BVAL A 116 -22.234 -41.295 -4.167 0.46 21.26 A C
ANISOU 1163 CA BVAL A 116 3068 2596 2415 208 749 -297 A C
ATOM 1164 C AVAL A 116 -22.952 -42.492 -2.136 0.54 15.58 A C
ANISOU 1164 C AVAL A 116 2716 1831 1374 253 249 177 A C
ATOM 1165 C BVAL A 116 -22.587 -42.385 -3.164 0.46 24.66 A C
ANISOU 1165 C BVAL A 116 3453 2869 3049 -145 776 -260 A C
ATOM 1166 O AVAL A 116 -22.034 -42.985 -1.471 0.54 15.83 A O
ANISOU 1166 O AVAL A 116 2732 1709 1573 299 290 26 A O
ATOM 1167 O BVAL A 116 -21.997 -43.470 -3.186 0.46 25.51 A O
ANISOU 1167 O BVAL A 116 3449 2935 3307 -303 626 -495 A O
ATOM 1168 CB AVAL A 116 -22.266 -42.791 -4.539 0.54 17.46 A C
ANISOU 1168 CB AVAL A 116 3076 2064 1496 -362 -66 -251 A C
ATOM 1169 CB BVAL A 116 -21.936 -41.924 -5.541 0.46 23.17 A C
ANISOU 1169 CB BVAL A 116 3284 2930 2591 540 1085 -478 A C
ATOM 1170 CG1AVAL A 116 -23.376 -43.810 -4.737 0.54 18.13 A C
ANISOU 1170 CG1AVAL A 116 3258 1977 1656 -706 108 -534 A C
ATOM 1171 CG1BVAL A 116 -22.595 -41.138 -6.622 0.46 23.43 A C
ANISOU 1171 CG1BVAL A 116 3337 3010 2553 777 1359 -468 A C
ATOM 1172 CG2AVAL A 116 -21.943 -42.070 -5.850 0.54 19.17 A C
ANISOU 1172 CG2AVAL A 116 3304 2624 1357 -399 -202 -352 A C
ATOM 1173 CG2BVAL A 116 -20.435 -42.023 -5.785 0.46 23.86 A C
ANISOU 1173 CG2BVAL A 116 3397 2988 2681 591 1169 -436 A C
ATOM 1174 N ATYR A 117 -24.225 -42.533 -1.760 0.54 16.55 A N
ANISOU 1174 N ATYR A 117 2783 1848 1660 67 402 414 A N
ATOM 1175 N BTYR A 117 -23.550 -42.115 -2.290 0.46 26.45 A N
ANISOU 1175 N BTYR A 117 3900 2917 3235 -88 759 -337 A N
ATOM 1176 CA ATYR A 117 -24.604 -43.079 -0.464 0.54 19.62 A C
ANISOU 1176 CA ATYR A 117 3202 2151 2102 414 623 430 A C
ATOM 1177 CA BTYR A 117 -23.934 -43.090 -1.272 0.46 27.09 A C
ANISOU 1177 CA BTYR A 117 4076 2777 3442 -115 720 -349 A C
ATOM 1178 C ATYR A 117 -24.225 -44.548 -0.322 0.54 21.54 A C
ANISOU 1178 C ATYR A 117 3665 2209 2310 701 416 807 A C
ATOM 1179 C BTYR A 117 -25.160 -43.898 -1.686 0.46 26.09 A C
ANISOU 1179 C BTYR A 117 4131 2310 3472 -193 1013 -403 A C
ATOM 1180 O ATYR A 117 -23.634 -44.942 0.683 0.54 23.35 A O
ANISOU 1180 O ATYR A 117 4057 2357 2457 1145 343 607 A O
ATOM 1181 O BTYR A 117 -25.172 -45.126 -1.566 0.46 24.58 A O
ANISOU 1181 O BTYR A 117 4139 1740 3459 -241 1294 -619 A O
ATOM 1182 CB ATYR A 117 -26.101 -42.880 -0.208 0.54 21.49 A C
ANISOU 1182 CB ATYR A 117 3375 2436 2353 217 1009 227 A C
ATOM 1183 CB BTYR A 117 -24.183 -42.400 0.070 0.46 27.85 A C
ANISOU 1183 CB BTYR A 117 4114 2907 3562 -117 519 -373 A C
ATOM 1184 CG ATYR A 117 -26.593 -43.486 1.088 0.54 22.84 A C
ANISOU 1184 CG ATYR A 117 3569 2645 2466 -30 1284 142 A C
ATOM 1185 CD1ATYR A 117 -26.494 -42.790 2.287 0.54 23.10 A C
ANISOU 1185 CD1ATYR A 117 3630 2673 2474 -289 1528 34 A C
ATOM 1186 CD2ATYR A 117 -27.166 -44.751 1.111 0.54 23.52 A C
ANISOU 1186 CD2ATYR A 117 3779 2754 2403 -179 1342 181 A C
ATOM 1187 CE1ATYR A 117 -26.948 -43.342 3.474 0.54 24.00 A C
ANISOU 1187 CE1ATYR A 117 3981 2602 2535 -385 1381 -105 A C
ATOM 1188 CE2ATYR A 117 -27.620 -45.309 2.289 0.54 24.12 A C
ANISOU 1188 CE2ATYR A 117 3998 2756 2410 -114 1391 -6 A C
ATOM 1189 CZ ATYR A 117 -27.510 -44.601 3.467 0.54 24.88 A C
ANISOU 1189 CZ ATYR A 117 4120 2806 2528 -275 1370 -57 A C
ATOM 1190 OH ATYR A 117 -27.964 -45.154 4.643 0.54 26.43 A O
ANISOU 1190 OH ATYR A 117 4322 2999 2723 -357 1317 174 A O
TER
ATOM 1191 N AASP B 1 -18.961 -17.548 14.614 0.48 23.48 B N
ANISOU 1191 N AASP B 1 2514 3589 2818 -75 904 -345 B N
ATOM 1192 N BASP B 1 -21.193 -19.145 14.261 0.52 24.03 B N
ANISOU 1192 N BASP B 1 3011 3406 2712 512 679 82 B N
ATOM 1193 CA AASP B 1 -20.346 -17.106 14.730 0.48 22.35 B C
ANISOU 1193 CA AASP B 1 2596 3324 2571 -167 635 -163 B C
ATOM 1194 CA BASP B 1 -20.746 -17.862 14.788 0.52 22.73 B C
ANISOU 1194 CA BASP B 1 3045 3257 2334 389 631 -95 B C
ATOM 1195 C AASP B 1 -20.863 -17.397 16.141 0.48 19.47 B C
ANISOU 1195 C AASP B 1 2239 2855 2302 -240 279 -255 B C
ATOM 1196 C BASP B 1 -21.118 -17.721 16.265 0.52 22.34 B C
ANISOU 1196 C BASP B 1 2999 3092 2396 471 626 138 B C
ATOM 1197 O AASP B 1 -20.628 -18.479 16.681 0.48 21.24 B O
ANISOU 1197 O AASP B 1 2378 2936 2757 -432 37 -337 B O
ATOM 1198 O BASP B 1 -20.956 -18.665 17.036 0.52 23.88 B O
ANISOU 1198 O BASP B 1 3316 3147 2611 585 785 231 B O
ATOM 1199 CB AASP B 1 -21.209 -17.790 13.664 0.48 23.01 B C
ANISOU 1199 CB AASP B 1 2944 3360 2440 -193 463 183 B C
ATOM 1200 CB BASP B 1 -21.318 -16.707 13.956 0.52 21.31 B C
ANISOU 1200 CB BASP B 1 2993 3111 1992 335 356 -272 B C
ATOM 1201 CG AASP B 1 -22.614 -17.228 13.596 0.48 21.40 B C
ANISOU 1201 CG AASP B 1 2930 3085 2114 -384 492 346 B C
ATOM 1202 CG BASP B 1 -22.825 -16.780 13.806 0.52 22.02 B C
ANISOU 1202 CG BASP B 1 3153 3030 2184 522 121 -509 B C
ATOM 1203 OD1AASP B 1 -23.393 -17.476 14.534 0.48 16.32 B O
ANISOU 1203 OD1AASP B 1 2347 2452 1401 -772 382 534 B O
ATOM 1204 OD1BASP B 1 -23.445 -17.665 14.426 0.52 19.62 B O
ANISOU 1204 OD1BASP B 1 2950 2625 1879 433 122 -806 B O
ATOM 1205 OD2AASP B 1 -22.940 -16.536 12.607 0.48 24.24 B O
ANISOU 1205 OD2AASP B 1 3294 3595 2322 -196 763 268 B O
ATOM 1206 OD2BASP B 1 -23.392 -15.946 13.065 0.52 25.24 B O
ANISOU 1206 OD2BASP B 1 3480 3474 2638 494 -3 -69 B O
ATOM 1207 N AALA B 2 -21.562 -16.432 16.737 0.48 15.15 B N
ANISOU 1207 N AALA B 2 1640 2440 1676 -307 -14 -103 B N
ATOM 1208 N BALA B 2 -21.614 -16.552 16.660 0.52 20.23 B N
ANISOU 1208 N BALA B 2 2544 2903 2238 235 366 130 B N
ATOM 1209 CA AALA B 2 -21.931 -16.536 18.146 0.48 11.53 B C
ANISOU 1209 CA AALA B 2 1435 1725 1221 -229 -51 22 B C
ATOM 1210 CA BALA B 2 -22.002 -16.340 18.050 0.52 17.03 B C
ANISOU 1210 CA BALA B 2 2189 2367 1914 35 275 -2 B C
ATOM 1211 C AALA B 2 -23.363 -17.006 18.384 0.48 10.31 B C
ANISOU 1211 C AALA B 2 1451 1253 1211 3 -133 115 B C
ATOM 1212 C BALA B 2 -23.309 -17.057 18.363 0.52 12.56 B C
ANISOU 1212 C BALA B 2 1631 1747 1394 89 6 101 B C
ATOM 1213 O AALA B 2 -23.825 -17.018 19.523 0.48 11.58 B O
ANISOU 1213 O AALA B 2 1618 1400 1382 156 -218 -27 B O
ATOM 1214 O BALA B 2 -23.618 -17.312 19.522 0.52 11.22 B O
ANISOU 1214 O BALA B 2 1320 1752 1193 211 -69 86 B O
ATOM 1215 CB AALA B 2 -21.671 -15.220 18.872 0.48 11.07 B C
ANISOU 1215 CB AALA B 2 1251 1521 1434 -388 -170 -412 B C
ATOM 1216 CB BALA B 2 -22.119 -14.854 18.360 0.52 18.91 B C
ANISOU 1216 CB BALA B 2 2524 2520 2140 -196 276 -317 B C
HETATM 1217 N LE1 B 3 -24.066 -17.396 17.323 1.00 10.69 B N
ANISOU 1217 N LE1 B 3 1442 1277 1344 35 -99 -18 B N
HETATM 1218 CA LE1 B 3 -25.382 -18.066 17.499 1.00 10.13 B C
ANISOU 1218 CA LE1 B 3 1528 1128 1193 193 -167 -45 B C
HETATM 1219 C LE1 B 3 -25.310 -19.487 16.925 1.00 9.37 B C
ANISOU 1219 C LE1 B 3 1295 1166 1100 188 -180 -2 B C
HETATM 1220 O LE1 B 3 -25.669 -20.431 17.657 1.00 9.69 B O
ANISOU 1220 O LE1 B 3 1311 1195 1176 172 -138 -100 B O
HETATM 1221 CB LE1 B 3 -26.584 -17.209 17.019 1.00 10.44 B C
ANISOU 1221 CB LE1 B 3 1614 1194 1161 142 -102 -150 B C
HETATM 1222 SG LE1 B 3 -28.164 -18.046 17.471 1.00 10.40 B S
ANISOU 1222 SG LE1 B 3 1476 1230 1244 182 -213 -155 B S
HETATM 1223 C8 LE1 B 3 -26.580 -15.903 17.804 1.00 11.19 B C
ANISOU 1223 C8 LE1 B 3 1671 1262 1318 73 -8 -102 B C
HETATM 1224 C9 LE1 B 3 -26.534 -16.916 15.524 1.00 11.81 B C
ANISOU 1224 C9 LE1 B 3 1808 1323 1355 325 -230 -77 B C
ATOM 1225 N TYR B 4 -24.856 -19.639 15.686 1.00 9.94 B N
ANISOU 1225 N TYR B 4 1432 1223 1122 226 -63 -79 B N
ATOM 1226 CA TYR B 4 -24.805 -20.950 15.053 1.00 10.28 B C
ANISOU 1226 CA TYR B 4 1443 1190 1271 254 -108 -149 B C
ATOM 1227 C TYR B 4 -23.556 -21.705 15.499 1.00 10.20 B C
ANISOU 1227 C TYR B 4 1377 1250 1250 160 -59 -170 B C
ATOM 1228 O TYR B 4 -22.549 -21.762 14.790 1.00 12.57 B O
ANISOU 1228 O TYR B 4 1687 1678 1410 386 44 77 B O
ATOM 1229 CB TYR B 4 -24.855 -20.814 13.530 1.00 11.18 B C
ANISOU 1229 CB TYR B 4 1636 1529 1082 272 -172 0 B C
ATOM 1230 CG TYR B 4 -26.122 -20.165 13.018 1.00 11.21 B C
ANISOU 1230 CG TYR B 4 1605 1457 1197 187 -173 -17 B C
ATOM 1231 CD1 TYR B 4 -27.348 -20.817 13.103 1.00 12.25 B C
ANISOU 1231 CD1 TYR B 4 1707 1618 1331 208 -236 29 B C
ATOM 1232 CD2 TYR B 4 -26.093 -18.903 12.440 1.00 13.39 B C
ANISOU 1232 CD2 TYR B 4 1735 1789 1564 203 -186 116 B C
ATOM 1233 CE1 TYR B 4 -28.512 -20.221 12.630 1.00 12.64 B C
ANISOU 1233 CE1 TYR B 4 1764 1590 1447 217 -349 -18 B C
ATOM 1234 CE2 TYR B 4 -27.247 -18.301 11.962 1.00 13.99 B C
ANISOU 1234 CE2 TYR B 4 1883 1913 1522 264 -184 232 B C
ATOM 1235 CZ TYR B 4 -28.452 -18.966 12.053 1.00 13.35 B C
ANISOU 1235 CZ TYR B 4 1781 1900 1391 409 -315 84 B C
ATOM 1236 OH TYR B 4 -29.602 -18.368 11.581 1.00 16.33 B O
ANISOU 1236 OH TYR B 4 2078 2233 1894 605 -329 307 B O
ATOM 1237 N THR B 5 -23.635 -22.298 16.680 1.00 10.31 B N
ANISOU 1237 N THR B 5 1311 1274 1334 238 -177 -74 B N
ATOM 1238 CA THR B 5 -22.556 -23.077 17.266 1.00 10.03 B C
ANISOU 1238 CA THR B 5 1181 1226 1403 292 -228 -117 B C
ATOM 1239 C THR B 5 -22.956 -24.546 17.308 1.00 9.65 B C
ANISOU 1239 C THR B 5 1254 1258 1153 310 -204 -107 B C
ATOM 1240 O THR B 5 -24.107 -24.913 17.073 1.00 9.98 B O
ANISOU 1240 O THR B 5 1242 1204 1349 125 -244 -80 B O
ATOM 1241 CB THR B 5 -22.257 -22.605 18.691 1.00 10.12 B C
ANISOU 1241 CB THR B 5 1301 1176 1367 214 -142 -169 B C
ATOM 1242 CG2 THR B 5 -21.944 -21.116 18.728 1.00 11.07 B C
ANISOU 1242 CG2 THR B 5 1387 1273 1546 227 -152 -53 B C
ATOM 1243 OG1 THR B 5 -23.391 -22.887 19.519 1.00 10.19 B O
ANISOU 1243 OG1 THR B 5 1272 1197 1403 265 -122 -65 B O
ATOM 1244 N TRP B 6 -21.999 -25.407 17.655 1.00 9.62 B N
ANISOU 1244 N TRP B 6 1324 1154 1175 161 -120 -103 B N
ATOM 1245 CA TRP B 6 -22.338 -26.816 17.809 1.00 9.43 B C
ANISOU 1245 CA TRP B 6 1201 1195 1186 138 -159 -130 B C
ATOM 1246 C TRP B 6 -23.430 -27.005 18.860 1.00 9.42 B C
ANISOU 1246 C TRP B 6 1295 1066 1219 134 -233 -280 B C
ATOM 1247 O TRP B 6 -24.406 -27.732 18.634 1.00 9.56 B O
ANISOU 1247 O TRP B 6 1218 1093 1321 147 -217 -246 B O
ATOM 1248 CB TRP B 6 -21.094 -27.651 18.129 1.00 9.90 B C
ANISOU 1248 CB TRP B 6 1261 1198 1303 260 -227 -194 B C
ATOM 1249 CG TRP B 6 -21.431 -29.111 18.178 1.00 9.54 B C
ANISOU 1249 CG TRP B 6 1214 1218 1191 257 -61 -149 B C
ATOM 1250 CD1 TRP B 6 -21.502 -29.911 19.286 1.00 10.07 B C
ANISOU 1250 CD1 TRP B 6 1230 1096 1501 380 23 -108 B C
ATOM 1251 CD2 TRP B 6 -21.813 -29.925 17.069 1.00 9.69 B C
ANISOU 1251 CD2 TRP B 6 1224 1133 1325 340 -142 -177 B C
ATOM 1252 CE2 TRP B 6 -22.095 -31.212 17.568 1.00 9.69 B C
ANISOU 1252 CE2 TRP B 6 1206 1178 1297 332 -12 -242 B C
ATOM 1253 CE3 TRP B 6 -21.930 -29.693 15.694 1.00 11.34 B C
ANISOU 1253 CE3 TRP B 6 1661 1398 1249 461 -266 -288 B C
ATOM 1254 NE1 TRP B 6 -21.911 -31.175 18.929 1.00 10.54 B N
ANISOU 1254 NE1 TRP B 6 1308 1317 1381 322 -47 -221 B N
ATOM 1255 CZ2 TRP B 6 -22.510 -32.257 16.738 1.00 11.22 B C
ANISOU 1255 CZ2 TRP B 6 1436 1345 1480 370 -134 -179 B C
ATOM 1256 CZ3 TRP B 6 -22.329 -30.730 14.877 1.00 12.55 B C
ANISOU 1256 CZ3 TRP B 6 1824 1481 1463 397 -346 -409 B C
ATOM 1257 CH2 TRP B 6 -22.613 -31.995 15.399 1.00 12.07 B C
ANISOU 1257 CH2 TRP B 6 1601 1258 1727 331 -377 -388 B C
ATOM 1258 N GLU B 7 -23.303 -26.328 20.008 1.00 9.32 B N
ANISOU 1258 N GLU B 7 1167 1233 1141 102 -174 -113 B N
ATOM 1259 CA GLU B 7 -24.291 -26.516 21.065 1.00 9.14 B C
ANISOU 1259 CA GLU B 7 1158 1272 1043 121 -214 -58 B C
ATOM 1260 C GLU B 7 -25.668 -25.992 20.668 1.00 9.66 B C
ANISOU 1260 C GLU B 7 1226 1294 1150 106 -90 -274 B C
ATOM 1261 O GLU B 7 -26.682 -26.477 21.187 1.00 9.83 B O
ANISOU 1261 O GLU B 7 1229 1356 1151 7 -116 -161 B O
ATOM 1262 CB GLU B 7 -23.814 -25.887 22.373 1.00 10.20 B C
ANISOU 1262 CB GLU B 7 1253 1376 1248 240 -325 -98 B C
ATOM 1263 CG GLU B 7 -22.567 -26.537 22.935 1.00 11.94 B C
ANISOU 1263 CG GLU B 7 1504 1487 1546 147 -264 3 B C
ATOM 1264 CD GLU B 7 -22.699 -28.030 23.086 1.00 15.30 B C
ANISOU 1264 CD GLU B 7 1927 1867 2021 231 -520 95 B C
ATOM 1265 OE1 GLU B 7 -23.733 -28.480 23.614 1.00 19.03 B O
ANISOU 1265 OE1 GLU B 7 2409 1897 2927 129 -265 782 B O
ATOM 1266 OE2 GLU B 7 -21.766 -28.751 22.666 1.00 17.15 B O
ANISOU 1266 OE2 GLU B 7 2331 2053 2134 723 -820 -367 B O
ATOM 1267 N CYS B 8 -25.732 -25.008 19.762 1.00 9.37 B N
ANISOU 1267 N CYS B 8 1113 1225 1223 186 -226 -266 B N
ATOM 1268 CA CYS B 8 -27.018 -24.545 19.242 1.00 10.07 B C
ANISOU 1268 CA CYS B 8 1168 1295 1364 175 -229 -216 B C
ATOM 1269 C CYS B 8 -27.834 -25.701 18.674 1.00 9.76 B C
ANISOU 1269 C CYS B 8 1099 1346 1264 212 -190 -191 B C
ATOM 1270 O CYS B 8 -29.067 -25.702 18.777 1.00 10.05 B O
ANISOU 1270 O CYS B 8 1109 1291 1418 168 -207 -263 B O
ATOM 1271 CB CYS B 8 -26.769 -23.464 18.177 1.00 10.64 B C
ANISOU 1271 CB CYS B 8 1403 1269 1371 272 -268 -33 B C
ATOM 1272 SG CYS B 8 -28.178 -22.909 17.188 1.00 11.14 B S
ANISOU 1272 SG CYS B 8 1464 1350 1417 210 -324 -180 B S
ATOM 1273 N LEU B 9 -27.167 -26.698 18.085 1.00 9.59 B N
ANISOU 1273 N LEU B 9 1144 1268 1231 194 -283 -279 B N
ATOM 1274 CA LEU B 9 -27.856 -27.789 17.407 1.00 10.25 B C
ANISOU 1274 CA LEU B 9 1195 1386 1312 248 -313 -425 B C
ATOM 1275 C LEU B 9 -28.321 -28.889 18.351 1.00 10.21 B C
ANISOU 1275 C LEU B 9 1161 1228 1491 225 -244 -286 B C
ATOM 1276 O LEU B 9 -29.015 -29.814 17.914 1.00 11.03 B O
ANISOU 1276 O LEU B 9 1243 1310 1640 120 -290 -294 B O
ATOM 1277 CB LEU B 9 -26.937 -28.405 16.354 1.00 11.70 B C
ANISOU 1277 CB LEU B 9 1358 1575 1512 68 -265 -504 B C
ATOM 1278 CG LEU B 9 -26.195 -27.468 15.402 1.00 13.04 B C
ANISOU 1278 CG LEU B 9 1538 1816 1602 15 49 -496 B C
ATOM 1279 CD1 LEU B 9 -25.454 -28.286 14.356 1.00 14.97 B C
ANISOU 1279 CD1 LEU B 9 1811 2071 1807 -178 332 -676 B C
ATOM 1280 CD2 LEU B 9 -27.119 -26.456 14.746 1.00 13.48 B C
ANISOU 1280 CD2 LEU B 9 1563 2067 1491 197 -190 -138 B C
ATOM 1281 N ALA B 10 -27.933 -28.842 19.619 1.00 10.51 B N
ANISOU 1281 N ALA B 10 1457 1255 1280 188 -227 -186 B N
ATOM 1282 CA ALA B 10 -28.180 -29.963 20.511 1.00 11.80 B C
ANISOU 1282 CA ALA B 10 1511 1437 1534 174 -330 -151 B C
ATOM 1283 C ALA B 10 -29.664 -30.105 20.813 1.00 11.31 B C
ANISOU 1283 C ALA B 10 1479 1326 1494 209 -139 -123 B C
ATOM 1284 O ALA B 10 -30.378 -29.113 20.995 1.00 12.52 B O
ANISOU 1284 O ALA B 10 1622 1461 1673 366 15 -91 B O
ATOM 1285 CB ALA B 10 -27.409 -29.765 21.817 1.00 12.95 B C
ANISOU 1285 CB ALA B 10 1772 1487 1662 12 -489 -32 B C
ATOM 1286 N TRP B 11 -30.120 -31.353 20.873 1.00 11.46 B N
ANISOU 1286 N TRP B 11 1496 1414 1444 129 -138 -75 B N
ATOM 1287 CA TRP B 11 -31.478 -31.620 21.303 1.00 11.77 B C
ANISOU 1287 CA TRP B 11 1647 1381 1445 122 -128 -18 B C
ATOM 1288 C TRP B 11 -31.668 -31.063 22.710 1.00 13.48 B C
ANISOU 1288 C TRP B 11 1837 1804 1480 401 -181 -68 B C
ATOM 1289 O TRP B 11 -30.787 -31.224 23.562 1.00 15.87 B O
ANISOU 1289 O TRP B 11 1998 2481 1551 516 -380 -33 B O
ATOM 1290 CB TRP B 11 -31.717 -33.127 21.338 1.00 13.70 B C
ANISOU 1290 CB TRP B 11 1700 1701 1805 -183 -77 227 B C
ATOM 1291 CG TRP B 11 -33.163 -33.471 21.440 1.00 14.07 B C
ANISOU 1291 CG TRP B 11 1880 1948 1519 -194 -127 58 B C
ATOM 1292 CD1 TRP B 11 -33.868 -33.794 22.564 1.00 17.07 B C
ANISOU 1292 CD1 TRP B 11 1992 2659 1836 -267 -103 84 B C
ATOM 1293 CD2 TRP B 11 -34.094 -33.504 20.359 1.00 13.90 B C
ANISOU 1293 CD2 TRP B 11 1820 1638 1825 -127 -320 -71 B C
ATOM 1294 CE2 TRP B 11 -35.346 -33.865 20.890 1.00 15.56 B C
ANISOU 1294 CE2 TRP B 11 1854 2015 2045 -273 -162 -97 B C
ATOM 1295 CE3 TRP B 11 -33.986 -33.268 18.987 1.00 14.13 B C
ANISOU 1295 CE3 TRP B 11 2254 1390 1725 7 -481 -49 B C
ATOM 1296 NE1 TRP B 11 -35.184 -34.033 22.241 1.00 17.31 B N
ANISOU 1296 NE1 TRP B 11 1915 2742 1922 -462 93 19 B N
ATOM 1297 CZ2 TRP B 11 -36.484 -33.997 20.092 1.00 16.23 B C
ANISOU 1297 CZ2 TRP B 11 2007 1671 2490 -99 -288 36 B C
ATOM 1298 CZ3 TRP B 11 -35.103 -33.408 18.202 1.00 16.04 B C
ANISOU 1298 CZ3 TRP B 11 2484 1380 2230 -30 -656 -4 B C
ATOM 1299 CH2 TRP B 11 -36.336 -33.767 18.755 1.00 16.02 B C
ANISOU 1299 CH2 TRP B 11 2112 1350 2625 238 -566 185 B C
ATOM 1300 N PRO B 12 -32.794 -30.402 22.995 1.00 15.14 B N
ANISOU 1300 N PRO B 12 2073 2340 1342 408 36 -166 B N
ATOM 1301 CA PRO B 12 -32.969 -29.803 24.324 1.00 18.51 B C
ANISOU 1301 CA PRO B 12 2522 2908 1602 542 -59 -304 B C
ATOM 1302 C PRO B 12 -33.070 -30.836 25.445 1.00 23.19 B C
ANISOU 1302 C PRO B 12 3623 3513 1674 188 139 -254 B C
ATOM 1303 O PRO B 12 -33.542 -31.950 25.220 1.00 26.39 B O
ANISOU 1303 O PRO B 12 4321 3901 1806 -91 514 10 B O
ATOM 1304 CB PRO B 12 -34.268 -28.993 24.191 1.00 19.70 B C
ANISOU 1304 CB PRO B 12 2497 3008 1981 700 66 -478 B C
ATOM 1305 CG PRO B 12 -34.929 -29.482 22.961 1.00 18.14 B C
ANISOU 1305 CG PRO B 12 2269 2735 1887 618 99 -307 B C
ATOM 1306 CD PRO B 12 -33.882 -30.060 22.066 1.00 14.89 B C
ANISOU 1306 CD PRO B 12 1889 2285 1484 506 -42 -183 B C
TER
CONECT 1211 1217 1217
CONECT 1212 1217 1217
CONECT 1217 1211 1212 1218 1211
CONECT 1217 1212
CONECT 1218 1217 1219 1221
CONECT 1219 1218 1220 1225 1225
CONECT 1220 1219
CONECT 1221 1218 1222 1223 1224
CONECT 1222 1221
CONECT 1223 1221
CONECT 1224 1221
CONECT 1225 1219 1219
END