HEADER 3.30.30.10 1npiA00 ATOM 1 N LYS A 1 10.428 -8.772 12.768 1.00 12.10 N ANISOU 1 N LYS A 1 1728 1181 1686 134 278 116 N ATOM 2 CA LYS A 1 11.030 -7.868 11.763 1.00 13.59 C ANISOU 2 CA LYS A 1 1880 1134 2149 151 589 265 C ATOM 3 C LYS A 1 10.382 -6.501 11.902 1.00 10.85 C ANISOU 3 C LYS A 1 1531 1141 1453 39 221 16 C ATOM 4 O LYS A 1 9.221 -6.390 12.245 1.00 12.44 O ANISOU 4 O LYS A 1 1591 1342 1795 48 427 118 O ATOM 5 CB LYS A 1 10.857 -8.474 10.370 1.00 22.52 C ANISOU 5 CB LYS A 1 4996 1322 2238 454 1802 -138 C ATOM 6 CG LYS A 1 10.898 -7.821 9.086 1.00 22.81 C ANISOU 6 CG LYS A 1 4284 2189 2194 589 431 -76 C ATOM 7 CD LYS A 1 10.617 -8.646 7.860 1.00 25.17 C ANISOU 7 CD LYS A 1 4438 2746 2381 -114 1644 -681 C ATOM 8 CE LYS A 1 10.963 -7.931 6.572 1.00 32.64 C ANISOU 8 CE LYS A 1 5779 4312 2310 -1358 525 -131 C ATOM 9 NZ LYS A 1 10.623 -9.011 5.586 1.00 30.72 N ANISOU 9 NZ LYS A 1 2942 6107 2623 231 66 -1566 N ATOM 10 N GLU A 2 11.136 -5.475 11.576 1.00 11.69 N ANISOU 10 N GLU A 2 1457 1196 1789 99 284 182 N ATOM 11 CA GLU A 2 10.665 -4.116 11.606 1.00 10.57 C ANISOU 11 CA GLU A 2 1571 1110 1337 64 166 110 C ATOM 12 C GLU A 2 10.770 -3.473 10.248 1.00 11.09 C ANISOU 12 C GLU A 2 1420 1478 1313 215 292 199 C ATOM 13 O GLU A 2 11.518 -3.917 9.375 1.00 15.74 O ANISOU 13 O GLU A 2 2441 1831 1709 721 819 267 O ATOM 14 CB AGLU A 2 11.372 -3.357 12.719 0.55 12.85 C ANISOU 14 CB AGLU A 2 1588 1676 1620 88 -144 -89 C ATOM 15 CB BGLU A 2 11.644 -3.251 12.417 0.45 12.03 C ANISOU 15 CB BGLU A 2 1817 1220 1535 128 -217 293 C ATOM 16 CG AGLU A 2 12.879 -3.340 12.601 0.55 17.24 C ANISOU 16 CG AGLU A 2 1524 2251 2775 255 -472 10 C ATOM 17 CG BGLU A 2 11.687 -3.642 13.867 0.45 12.23 C ANISOU 17 CG BGLU A 2 1536 1580 1530 101 -227 475 C ATOM 18 CD AGLU A 2 13.418 -2.636 13.841 0.55 16.81 C ANISOU 18 CD AGLU A 2 1677 1710 3001 352 -839 176 C ATOM 19 CD BGLU A 2 12.681 -2.790 14.631 0.45 13.54 C ANISOU 19 CD BGLU A 2 1863 1623 1659 264 -233 -39 C ATOM 20 OE1AGLU A 2 13.693 -3.410 14.778 0.55 28.58 O ANISOU 20 OE1AGLU A 2 5192 2040 3626 234 -2256 436 O ATOM 21 OE1BGLU A 2 13.129 -3.311 15.669 0.45 16.04 O ANISOU 21 OE1BGLU A 2 2289 2077 1727 -390 -541 224 O ATOM 22 OE2AGLU A 2 13.566 -1.408 13.843 0.55 20.62 O ANISOU 22 OE2AGLU A 2 2291 1730 3814 57 -848 261 O ATOM 23 OE2BGLU A 2 13.042 -1.667 14.198 0.45 12.11 O ANISOU 23 OE2BGLU A 2 985 1928 1689 107 -411 138 O ATOM 24 N GLY A 3 10.009 -2.417 10.021 1.00 10.53 N ANISOU 24 N GLY A 3 1437 1303 1261 119 226 169 N ATOM 25 CA GLY A 3 10.162 -1.628 8.821 1.00 11.13 C ANISOU 25 CA GLY A 3 1511 1320 1399 135 339 275 C ATOM 26 C GLY A 3 8.945 -0.818 8.527 1.00 10.32 C ANISOU 26 C GLY A 3 1350 1516 1057 127 247 138 C ATOM 27 O GLY A 3 7.954 -0.793 9.237 1.00 11.34 O ANISOU 27 O GLY A 3 1482 1569 1256 91 408 187 O ATOM 28 N TYR A 4 9.044 -0.070 7.434 1.00 10.20 N ANISOU 28 N TYR A 4 1272 1430 1172 80 246 105 N ATOM 29 CA TYR A 4 7.930 0.716 6.918 1.00 10.62 C ANISOU 29 CA TYR A 4 1380 1518 1139 159 287 258 C ATOM 30 C TYR A 4 6.992 -0.120 6.073 1.00 11.55 C ANISOU 30 C TYR A 4 1333 1766 1289 32 244 286 C ATOM 31 O TYR A 4 7.437 -0.842 5.187 1.00 13.45 O ANISOU 31 O TYR A 4 1681 1950 1480 -32 270 -113 O ATOM 32 CB TYR A 4 8.421 1.868 6.086 1.00 11.74 C ANISOU 32 CB TYR A 4 1696 1590 1174 -25 214 252 C ATOM 33 CG TYR A 4 9.229 2.908 6.826 1.00 12.29 C ANISOU 33 CG TYR A 4 1677 1652 1340 -85 218 163 C ATOM 34 CD1 TYR A 4 8.614 3.957 7.483 1.00 12.95 C ANISOU 34 CD1 TYR A 4 1901 1759 1261 4 184 107 C ATOM 35 CD2 TYR A 4 10.586 2.841 6.830 1.00 14.12 C ANISOU 35 CD2 TYR A 4 1711 1611 2045 -144 264 49 C ATOM 36 CE1 TYR A 4 9.359 4.919 8.147 1.00 14.68 C ANISOU 36 CE1 TYR A 4 2208 1663 1708 -321 583 -1 C ATOM 37 CE2 TYR A 4 11.362 3.778 7.469 1.00 16.07 C ANISOU 37 CE2 TYR A 4 1808 1928 2371 -357 292 -100 C ATOM 38 CZ TYR A 4 10.715 4.818 8.127 1.00 16.07 C ANISOU 38 CZ TYR A 4 2168 2123 1816 -495 351 -278 C ATOM 39 OH TYR A 4 11.467 5.764 8.770 1.00 21.31 O ANISOU 39 OH TYR A 4 2800 2456 2842 -555 -241 -590 O ATOM 40 N LEU A 5 5.715 -0.035 6.338 1.00 12.89 N ANISOU 40 N LEU A 5 1413 2159 1327 -39 234 252 N ATOM 41 CA LEU A 5 4.687 -0.639 5.519 1.00 14.90 C ANISOU 41 CA LEU A 5 1514 2573 1575 -372 34 541 C ATOM 42 C LEU A 5 4.607 0.129 4.200 1.00 14.07 C ANISOU 42 C LEU A 5 1608 2221 1516 -191 -16 324 C ATOM 43 O LEU A 5 4.879 1.293 4.118 1.00 16.06 O ANISOU 43 O LEU A 5 2370 2191 1542 -260 -288 308 O ATOM 44 CB LEU A 5 3.332 -0.558 6.162 1.00 18.38 C ANISOU 44 CB LEU A 5 1471 3909 1606 -250 55 493 C ATOM 45 CG LEU A 5 3.162 -1.537 7.296 1.00 24.60 C ANISOU 45 CG LEU A 5 2172 5431 1743 -618 292 1117 C ATOM 46 CD1 LEU A 5 1.715 -1.440 7.807 1.00 36.58 C ANISOU 46 CD1 LEU A 5 2105 9478 2314 -1543 559 1237 C ATOM 47 CD2 LEU A 5 3.434 -2.989 6.961 1.00 31.27 C ANISOU 47 CD2 LEU A 5 4407 4506 2970 -1527 -582 1799 C ATOM 48 N MET A 6 4.189 -0.629 3.171 1.00 15.25 N ANISOU 48 N MET A 6 1958 2261 1575 -603 -88 410 N ATOM 49 CA MET A 6 3.931 -0.079 1.881 1.00 15.89 C ANISOU 49 CA MET A 6 2181 2269 1587 -561 -162 450 C ATOM 50 C MET A 6 2.482 -0.222 1.460 1.00 17.26 C ANISOU 50 C MET A 6 2186 2848 1523 -628 -186 410 C ATOM 51 O MET A 6 1.837 -1.157 1.913 1.00 23.60 O ANISOU 51 O MET A 6 2498 3812 2658 -1222 -635 1343 O ATOM 52 CB MET A 6 4.701 -0.856 0.824 1.00 20.53 C ANISOU 52 CB MET A 6 2420 3654 1729 -596 258 135 C ATOM 53 CG MET A 6 6.170 -0.564 0.952 1.00 20.97 C ANISOU 53 CG MET A 6 2284 3560 2126 -209 -17 614 C ATOM 54 SD MET A 6 7.042 -1.357 -0.386 1.00 24.87 S ANISOU 54 SD MET A 6 2853 3598 2998 376 779 873 S ATOM 55 CE MET A 6 7.009 -3.080 0.049 1.00 34.19 C ANISOU 55 CE MET A 6 4144 3533 5313 591 1729 1124 C ATOM 56 N ASP A 7 2.067 0.677 0.614 1.00 19.00 N ANISOU 56 N ASP A 7 2171 3365 1684 -647 -325 709 N ATOM 57 CA ASP A 7 0.743 0.516 0.001 1.00 17.87 C ANISOU 57 CA ASP A 7 1814 3159 1815 -243 -58 74 C ATOM 58 C ASP A 7 0.885 -0.312 -1.252 1.00 16.11 C ANISOU 58 C ASP A 7 1732 2591 1798 -108 -80 261 C ATOM 59 O ASP A 7 1.906 -0.859 -1.589 1.00 17.38 O ANISOU 59 O ASP A 7 1975 2467 2164 181 -103 387 O ATOM 60 CB ASP A 7 0.119 1.872 -0.256 1.00 20.43 C ANISOU 60 CB ASP A 7 2353 3499 1911 510 343 -235 C ATOM 61 CG ASP A 7 0.785 2.743 -1.283 1.00 19.49 C ANISOU 61 CG ASP A 7 2450 2922 2033 676 88 -79 C ATOM 62 OD1 ASP A 7 1.628 2.240 -2.051 1.00 16.85 O ANISOU 62 OD1 ASP A 7 2091 2577 1734 290 23 81 O ATOM 63 OD2 ASP A 7 0.442 3.965 -1.363 1.00 27.71 O ANISOU 63 OD2 ASP A 7 4098 3215 3216 1389 461 67 O ATOM 64 N HIS A 8 -0.189 -0.399 -2.018 1.00 15.31 N ANISOU 64 N HIS A 8 1851 2250 1714 -117 -92 325 N ATOM 65 CA HIS A 8 -0.320 -1.219 -3.205 1.00 15.01 C ANISOU 65 CA HIS A 8 1653 2025 2026 39 -148 101 C ATOM 66 C HIS A 8 0.548 -0.709 -4.373 1.00 15.68 C ANISOU 66 C HIS A 8 1678 2387 1893 -94 -54 -267 C ATOM 67 O HIS A 8 0.799 -1.499 -5.285 1.00 21.44 O ANISOU 67 O HIS A 8 2606 2969 2571 -251 440 -845 O ATOM 68 CB HIS A 8 -1.741 -1.345 -3.669 1.00 16.36 C ANISOU 68 CB HIS A 8 1668 2084 2465 -128 -256 258 C ATOM 69 CG HIS A 8 -2.312 -0.062 -4.186 1.00 16.53 C ANISOU 69 CG HIS A 8 1665 2023 2593 -115 -407 270 C ATOM 70 ND1 HIS A 8 -2.581 1.057 -3.414 1.00 21.99 N ANISOU 70 ND1 HIS A 8 2534 2270 3553 86 -670 -268 N ATOM 71 CD2 HIS A 8 -2.601 0.257 -5.458 1.00 20.59 C ANISOU 71 CD2 HIS A 8 2414 2680 2731 -442 -655 670 C ATOM 72 CE1 HIS A 8 -3.056 2.001 -4.210 1.00 27.48 C ANISOU 72 CE1 HIS A 8 2551 2524 5368 777 -823 199 C ATOM 73 NE2 HIS A 8 -3.077 1.527 -5.432 1.00 27.10 N ANISOU 73 NE2 HIS A 8 3141 2751 4404 -212 -911 1428 N ATOM 74 N GLU A 9 0.978 0.545 -4.321 1.00 15.19 N ANISOU 74 N GLU A 9 1844 2345 1581 -86 -138 113 N ATOM 75 CA GLU A 9 1.827 1.181 -5.296 1.00 16.83 C ANISOU 75 CA GLU A 9 2077 2785 1534 -124 -142 263 C ATOM 76 C GLU A 9 3.301 1.095 -4.928 1.00 16.24 C ANISOU 76 C GLU A 9 1956 2872 1342 -349 28 -183 C ATOM 77 O GLU A 9 4.136 1.547 -5.679 1.00 19.76 O ANISOU 77 O GLU A 9 2355 3579 1573 -632 77 97 O ATOM 78 CB GLU A 9 1.520 2.685 -5.410 1.00 22.32 C ANISOU 78 CB GLU A 9 3114 2856 2510 -169 -465 1035 C ATOM 79 CG GLU A 9 0.134 3.052 -5.865 1.00 28.44 C ANISOU 79 CG GLU A 9 3128 4319 3360 986 396 1536 C ATOM 80 CD GLU A 9 0.118 4.491 -6.366 1.00 41.45 C ANISOU 80 CD GLU A 9 6135 4894 4719 1396 -1017 2510 C ATOM 81 OE1 GLU A 9 0.122 5.444 -5.571 1.00 65.62 O ANISOU 81 OE1 GLU A 9 9675 4528 10731 3251 -1433 185 O ATOM 82 OE2 GLU A 9 0.118 4.580 -7.609 1.00 62.03 O ANISOU 82 OE2 GLU A 9 7402 11065 5102 -3728 -2782 5508 O ATOM 83 N GLY A 10 3.631 0.539 -3.774 1.00 14.42 N ANISOU 83 N GLY A 10 1780 2151 1550 -45 -41 -190 N ATOM 84 CA GLY A 10 4.989 0.491 -3.334 1.00 15.00 C ANISOU 84 CA GLY A 10 1759 1983 1957 -86 -73 -318 C ATOM 85 C GLY A 10 5.459 1.714 -2.579 1.00 13.85 C ANISOU 85 C GLY A 10 1991 1916 1355 -126 -164 -67 C ATOM 86 O GLY A 10 6.669 1.865 -2.334 1.00 16.81 O ANISOU 86 O GLY A 10 1948 2363 2078 -168 -286 -385 O ATOM 87 N CYS A 11 4.531 2.600 -2.210 1.00 15.37 N ANISOU 87 N CYS A 11 2110 2322 1409 20 -45 -314 N ATOM 88 CA CYS A 11 4.859 3.799 -1.455 1.00 15.82 C ANISOU 88 CA CYS A 11 2468 2147 1396 51 -50 -175 C ATOM 89 C CYS A 11 4.711 3.526 0.033 1.00 14.87 C ANISOU 89 C CYS A 11 2201 2044 1406 144 62 -263 C ATOM 90 O CYS A 11 3.896 2.727 0.452 1.00 18.13 O ANISOU 90 O CYS A 11 3192 2292 1405 -555 -159 -162 O ATOM 91 CB CYS A 11 3.901 4.936 -1.818 1.00 18.34 C ANISOU 91 CB CYS A 11 2905 2355 1708 275 -176 -44 C ATOM 92 SG CYS A 11 4.021 5.449 -3.541 1.00 21.53 S ANISOU 92 SG CYS A 11 3203 3067 1911 827 0 399 S ATOM 93 N LYS A 12 5.478 4.262 0.824 1.00 14.66 N ANISOU 93 N LYS A 12 2431 1821 1320 -123 166 -57 N ATOM 94 CA LYS A 12 5.280 4.146 2.261 1.00 14.87 C ANISOU 94 CA LYS A 12 2714 1592 1346 30 220 -332 C ATOM 95 C LYS A 12 3.881 4.625 2.619 1.00 14.64 C ANISOU 95 C LYS A 12 2463 1854 1247 -149 90 -140 C ATOM 96 O LYS A 12 3.316 5.495 1.980 1.00 17.77 O ANISOU 96 O LYS A 12 2712 2235 1804 251 434 323 O ATOM 97 CB LYS A 12 6.295 5.005 3.014 1.00 15.15 C ANISOU 97 CB LYS A 12 2413 1964 1379 -64 289 -336 C ATOM 98 CG LYS A 12 7.710 4.537 2.943 1.00 16.02 C ANISOU 98 CG LYS A 12 2553 2219 1317 145 458 -225 C ATOM 99 CD LYS A 12 8.601 5.448 3.758 1.00 19.07 C ANISOU 99 CD LYS A 12 2505 3017 1721 99 185 -546 C ATOM 100 CE ALYS A 12 10.029 5.028 3.831 0.39 14.48 C ANISOU 100 CE ALYS A 12 2525 1966 1011 68 541 151 C ATOM 101 CE BLYS A 12 9.979 5.558 3.207 0.61 20.85 C ANISOU 101 CE BLYS A 12 2294 3224 2404 399 137 -985 C ATOM 102 NZ ALYS A 12 10.850 5.690 4.870 0.39 25.59 N ANISOU 102 NZ ALYS A 12 2932 4477 2315 -588 -197 -455 N ATOM 103 NZ BLYS A 12 10.914 6.333 4.037 0.61 23.28 N ANISOU 103 NZ BLYS A 12 2643 2833 3367 24 399 -1435 N ATOM 104 N LEU A 13 3.346 4.013 3.648 1.00 15.04 N ANISOU 104 N LEU A 13 2151 1947 1615 -639 -212 133 N ATOM 105 CA LEU A 13 2.037 4.354 4.103 1.00 15.31 C ANISOU 105 CA LEU A 13 2061 2284 1471 -556 -304 318 C ATOM 106 C LEU A 13 2.096 5.647 4.888 1.00 14.20 C ANISOU 106 C LEU A 13 1483 2438 1475 -387 -236 300 C ATOM 107 O LEU A 13 2.740 5.688 5.922 1.00 16.24 O ANISOU 107 O LEU A 13 2098 2419 1654 -381 -573 116 O ATOM 108 CB LEU A 13 1.487 3.239 4.998 1.00 19.49 C ANISOU 108 CB LEU A 13 2607 2875 1924 -1081 -275 683 C ATOM 109 CG LEU A 13 0.024 3.173 5.207 1.00 25.30 C ANISOU 109 CG LEU A 13 2642 3971 2999 -1460 -342 1090 C ATOM 110 CD1 LEU A 13 -0.758 3.078 3.917 1.00 32.12 C ANISOU 110 CD1 LEU A 13 2631 6400 3173 -1130 -546 820 C ATOM 111 CD2 LEU A 13 -0.203 1.963 6.126 1.00 31.25 C ANISOU 111 CD2 LEU A 13 3606 4423 3844 -2477 -325 1512 C ATOM 112 N SER A 14 1.463 6.701 4.416 1.00 14.89 N ANISOU 112 N SER A 14 1564 2551 1544 -129 -320 -17 N ATOM 113 CA SER A 14 1.525 8.025 4.977 1.00 15.17 C ANISOU 113 CA SER A 14 1832 2470 1463 -362 62 49 C ATOM 114 C SER A 14 0.747 8.137 6.251 1.00 13.66 C ANISOU 114 C SER A 14 1531 2212 1447 -45 -107 229 C ATOM 115 O SER A 14 -0.365 7.558 6.401 1.00 17.06 O ANISOU 115 O SER A 14 1759 2959 1766 -469 6 139 O ATOM 116 CB SER A 14 0.779 8.907 3.937 1.00 22.47 C ANISOU 116 CB SER A 14 4322 2592 1625 152 224 621 C ATOM 117 OG SER A 14 0.785 10.202 4.387 1.00 28.88 O ANISOU 117 OG SER A 14 5138 2574 3262 150 191 400 O ATOM 118 N CYS A 15 1.239 8.887 7.205 1.00 12.69 N ANISOU 118 N CYS A 15 1516 2100 1207 38 -31 335 N ATOM 119 CA CYS A 15 0.464 9.178 8.383 1.00 11.93 C ANISOU 119 CA CYS A 15 1265 1895 1371 109 -27 293 C ATOM 120 C CYS A 15 0.411 10.667 8.655 1.00 14.43 C ANISOU 120 C CYS A 15 1640 1913 1928 391 270 421 C ATOM 121 O CYS A 15 0.151 11.081 9.760 1.00 19.72 O ANISOU 121 O CYS A 15 3379 2043 2073 1115 311 193 O ATOM 122 CB CYS A 15 0.993 8.392 9.585 1.00 11.62 C ANISOU 122 CB CYS A 15 1409 1734 1273 67 58 255 C ATOM 123 SG CYS A 15 2.742 8.537 9.918 1.00 11.60 S ANISOU 123 SG CYS A 15 1413 1732 1261 166 80 221 S ATOM 124 N PHE A 16 0.578 11.488 7.624 1.00 17.73 N ANISOU 124 N PHE A 16 1991 2123 2623 429 594 890 N ATOM 125 CA PHE A 16 0.224 12.873 7.629 1.00 21.60 C ANISOU 125 CA PHE A 16 2576 2290 3339 744 1039 1133 C ATOM 126 C PHE A 16 -1.266 12.926 8.024 1.00 22.70 C ANISOU 126 C PHE A 16 2525 2516 3583 845 1075 1373 C ATOM 127 O PHE A 16 -2.138 12.207 7.457 1.00 24.85 O ANISOU 127 O PHE A 16 2466 3245 3732 752 679 1431 O ATOM 128 CB PHE A 16 0.294 13.588 6.288 1.00 22.24 C ANISOU 128 CB PHE A 16 2315 2591 3545 285 746 1491 C ATOM 129 CG PHE A 16 1.669 13.779 5.719 1.00 18.23 C ANISOU 129 CG PHE A 16 2090 1965 2871 304 526 577 C ATOM 130 CD1 PHE A 16 1.896 13.228 4.467 1.00 21.75 C ANISOU 130 CD1 PHE A 16 2425 3107 2730 17 128 246 C ATOM 131 CD2 PHE A 16 2.669 14.470 6.352 1.00 20.29 C ANISOU 131 CD2 PHE A 16 2335 2627 2748 398 388 60 C ATOM 132 CE1 PHE A 16 3.116 13.372 3.854 1.00 20.60 C ANISOU 132 CE1 PHE A 16 2349 3034 2445 324 120 -353 C ATOM 133 CE2 PHE A 16 3.890 14.660 5.731 1.00 18.86 C ANISOU 133 CE2 PHE A 16 2331 2264 2573 -122 177 -69 C ATOM 134 CZ PHE A 16 4.055 14.150 4.460 1.00 18.66 C ANISOU 134 CZ PHE A 16 2533 2246 2312 60 280 380 C ATOM 135 N ILE A 17 -1.517 13.803 8.941 1.00 23.36 N ANISOU 135 N ILE A 17 2817 2401 3656 776 1507 1484 N ATOM 136 CA ILE A 17 -2.841 14.134 9.438 1.00 24.67 C ANISOU 136 CA ILE A 17 2725 2602 4048 636 1590 1336 C ATOM 137 C ILE A 17 -3.759 12.933 9.606 1.00 22.91 C ANISOU 137 C ILE A 17 2317 2626 3760 710 979 1164 C ATOM 138 O ILE A 17 -4.947 12.944 9.297 1.00 29.81 O ANISOU 138 O ILE A 17 2382 3598 5348 680 718 2186 O ATOM 139 CB ILE A 17 -3.507 15.198 8.559 1.00 31.98 C ANISOU 139 CB ILE A 17 2674 3440 6036 815 1386 2461 C ATOM 140 CG1 ILE A 17 -3.722 14.871 7.087 1.00 38.49 C ANISOU 140 CG1 ILE A 17 3304 5934 5387 2233 1426 3305 C ATOM 141 CG2 ILE A 17 -2.671 16.469 8.716 1.00 50.41 C ANISOU 141 CG2 ILE A 17 5814 3212 10128 -273 1970 2948 C ATOM 142 CD1 ILE A 17 -4.538 15.944 6.349 1.00 54.34 C ANISOU 142 CD1 ILE A 17 5055 7618 7973 2582 1048 5481 C ATOM 143 N ARG A 18 -3.247 11.885 10.193 1.00 20.34 N ANISOU 143 N ARG A 18 2082 2306 3340 369 719 865 N ATOM 144 CA ARG A 18 -4.013 10.759 10.695 1.00 17.11 C ANISOU 144 CA ARG A 18 1747 2384 2370 207 570 461 C ATOM 145 C ARG A 18 -4.188 10.825 12.210 1.00 15.02 C ANISOU 145 C ARG A 18 1420 2006 2279 340 148 225 C ATOM 146 O ARG A 18 -3.328 11.334 12.925 1.00 17.69 O ANISOU 146 O ARG A 18 1784 1996 2940 2 38 24 O ATOM 147 CB ARG A 18 -3.298 9.477 10.309 1.00 17.04 C ANISOU 147 CB ARG A 18 1967 2266 2242 216 550 336 C ATOM 148 CG ARG A 18 -3.245 9.174 8.848 1.00 18.05 C ANISOU 148 CG ARG A 18 2204 2449 2205 -53 522 422 C ATOM 149 CD ARG A 18 -4.546 8.644 8.307 1.00 21.92 C ANISOU 149 CD ARG A 18 2363 3614 2352 -291 344 376 C ATOM 150 NE ARG A 18 -4.427 8.253 6.907 1.00 24.63 N ANISOU 150 NE ARG A 18 2640 4232 2485 525 -117 23 N ATOM 151 CZ ARG A 18 -5.452 7.764 6.189 1.00 27.41 C ANISOU 151 CZ ARG A 18 2942 4326 3146 815 -661 -238 C ATOM 152 NH1 ARG A 18 -6.627 7.620 6.796 1.00 32.77 N ANISOU 152 NH1 ARG A 18 3019 5699 3733 -246 -791 891 N ATOM 153 NH2 ARG A 18 -5.321 7.433 4.924 1.00 39.23 N ANISOU 153 NH2 ARG A 18 4132 7945 2827 357 -1214 -339 N ATOM 154 N PRO A 19 -5.251 10.199 12.739 1.00 14.67 N ANISOU 154 N PRO A 19 1757 1872 1947 138 326 -2 N ATOM 155 CA PRO A 19 -5.374 10.126 14.182 1.00 15.20 C ANISOU 155 CA PRO A 19 1789 2020 1965 468 298 -105 C ATOM 156 C PRO A 19 -4.244 9.308 14.775 1.00 14.67 C ANISOU 156 C PRO A 19 1996 1603 1974 332 95 -321 C ATOM 157 O PRO A 19 -3.637 8.425 14.156 1.00 15.22 O ANISOU 157 O PRO A 19 1969 1923 1890 551 185 -276 O ATOM 158 CB PRO A 19 -6.731 9.457 14.359 1.00 18.97 C ANISOU 158 CB PRO A 19 1801 3233 2173 238 668 14 C ATOM 159 CG PRO A 19 -7.448 9.466 13.053 1.00 25.01 C ANISOU 159 CG PRO A 19 2452 4954 2097 -1302 579 -456 C ATOM 160 CD PRO A 19 -6.334 9.547 12.029 1.00 16.83 C ANISOU 160 CD PRO A 19 1773 2569 2053 -82 248 59 C ATOM 161 N SER A 20 -3.948 9.540 16.024 1.00 15.33 N ANISOU 161 N SER A 20 2086 1633 2104 643 -18 -469 N ATOM 162 CA SER A 20 -3.005 8.724 16.757 1.00 15.32 C ANISOU 162 CA SER A 20 2071 1633 2119 428 -16 -197 C ATOM 163 C SER A 20 -3.519 7.284 16.752 1.00 14.11 C ANISOU 163 C SER A 20 1707 1762 1895 317 143 -118 C ATOM 164 O SER A 20 -4.697 7.004 16.794 1.00 16.20 O ANISOU 164 O SER A 20 1839 2138 2179 279 634 -152 O ATOM 165 CB SER A 20 -2.884 9.263 18.172 1.00 19.00 C ANISOU 165 CB SER A 20 2884 1972 2363 892 -473 -529 C ATOM 166 OG ASER A 20 -1.718 8.681 18.723 0.67 19.76 O ANISOU 166 OG ASER A 20 2635 2845 2028 902 -209 -321 O ATOM 167 OG BSER A 20 -2.304 10.517 18.299 0.33 23.93 O ANISOU 167 OG BSER A 20 2828 1982 4284 1054 -1732 -968 O ATOM 168 N GLY A 21 -2.587 6.355 16.647 1.00 13.86 N ANISOU 168 N GLY A 21 1953 1647 1665 409 39 -304 N ATOM 169 CA GLY A 21 -2.861 4.953 16.642 1.00 13.27 C ANISOU 169 CA GLY A 21 1838 1670 1535 262 285 -6 C ATOM 170 C GLY A 21 -3.170 4.349 15.303 1.00 12.10 C ANISOU 170 C GLY A 21 1640 1478 1477 262 506 16 C ATOM 171 O GLY A 21 -3.317 3.121 15.179 1.00 13.69 O ANISOU 171 O GLY A 21 2026 1463 1714 51 561 11 O ATOM 172 N TYR A 22 -3.245 5.203 14.276 1.00 11.50 N ANISOU 172 N TYR A 22 1471 1342 1557 54 193 35 N ATOM 173 CA TYR A 22 -3.473 4.708 12.922 1.00 11.09 C ANISOU 173 CA TYR A 22 1208 1475 1529 151 224 -67 C ATOM 174 C TYR A 22 -2.433 3.693 12.513 1.00 10.20 C ANISOU 174 C TYR A 22 1116 1250 1509 44 238 71 C ATOM 175 O TYR A 22 -2.729 2.627 11.990 1.00 11.15 O ANISOU 175 O TYR A 22 1223 1296 1718 -85 85 0 O ATOM 176 CB TYR A 22 -3.506 5.936 11.983 1.00 12.25 C ANISOU 176 CB TYR A 22 1368 1658 1629 417 40 65 C ATOM 177 CG TYR A 22 -3.524 5.562 10.526 1.00 12.85 C ANISOU 177 CG TYR A 22 1366 1975 1540 247 -16 5 C ATOM 178 CD1 TYR A 22 -4.705 5.166 9.917 1.00 16.32 C ANISOU 178 CD1 TYR A 22 1435 3040 1727 23 -219 395 C ATOM 179 CD2 TYR A 22 -2.361 5.595 9.781 1.00 13.08 C ANISOU 179 CD2 TYR A 22 1563 1921 1486 -38 41 307 C ATOM 180 CE1 TYR A 22 -4.660 4.822 8.569 1.00 17.76 C ANISOU 180 CE1 TYR A 22 1810 3079 1858 -414 -352 183 C ATOM 181 CE2 TYR A 22 -2.341 5.245 8.448 1.00 14.43 C ANISOU 181 CE2 TYR A 22 1683 2174 1628 203 95 53 C ATOM 182 CZ TYR A 22 -3.509 4.866 7.843 1.00 14.83 C ANISOU 182 CZ TYR A 22 2031 2018 1586 -7 -198 309 C ATOM 183 OH TYR A 22 -3.495 4.517 6.530 1.00 19.70 O ANISOU 183 OH TYR A 22 2979 2816 1689 -371 -204 70 O ATOM 184 N CYS A 23 -1.174 4.036 12.730 1.00 9.69 N ANISOU 184 N CYS A 23 1117 1136 1429 -24 227 73 N ATOM 185 CA CYS A 23 -0.114 3.121 12.273 1.00 9.70 C ANISOU 185 CA CYS A 23 1112 1289 1286 72 154 -117 C ATOM 186 C CYS A 23 -0.112 1.877 13.097 1.00 9.94 C ANISOU 186 C CYS A 23 1110 1190 1477 -47 311 -135 C ATOM 187 O CYS A 23 0.160 0.814 12.566 1.00 11.70 O ANISOU 187 O CYS A 23 1475 1163 1806 -23 339 -155 O ATOM 188 CB CYS A 23 1.216 3.855 12.356 1.00 9.86 C ANISOU 188 CB CYS A 23 1225 1197 1326 -27 239 -10 C ATOM 189 SG CYS A 23 1.404 5.202 11.190 1.00 10.24 S ANISOU 189 SG CYS A 23 1291 1213 1389 -45 223 -34 S ATOM 190 N GLY A 24 -0.375 1.944 14.404 1.00 10.69 N ANISOU 190 N GLY A 24 1416 1256 1390 78 166 -19 N ATOM 191 CA GLY A 24 -0.459 0.707 15.186 1.00 11.98 C ANISOU 191 CA GLY A 24 1774 1334 1446 -46 131 -6 C ATOM 192 C GLY A 24 -1.521 -0.201 14.644 1.00 11.80 C ANISOU 192 C GLY A 24 1570 1422 1490 -19 227 40 C ATOM 193 O GLY A 24 -1.363 -1.415 14.543 1.00 12.67 O ANISOU 193 O GLY A 24 1711 1369 1733 -182 32 157 O ATOM 194 N ARG A 25 -2.649 0.333 14.211 1.00 11.81 N ANISOU 194 N ARG A 25 1521 1404 1560 -112 254 147 N ATOM 195 CA ARG A 25 -3.716 -0.481 13.630 1.00 12.69 C ANISOU 195 CA ARG A 25 1347 1421 2055 -246 437 23 C ATOM 196 C ARG A 25 -3.279 -1.133 12.323 1.00 11.83 C ANISOU 196 C ARG A 25 1293 1322 1879 8 192 113 C ATOM 197 O ARG A 25 -3.450 -2.317 12.069 1.00 12.59 O ANISOU 197 O ARG A 25 1472 1455 1857 -223 100 37 O ATOM 198 CB ARG A 25 -4.952 0.391 13.427 1.00 16.28 C ANISOU 198 CB ARG A 25 1206 2385 2596 57 425 -492 C ATOM 199 CG ARG A 25 -6.097 -0.393 12.819 1.00 20.06 C ANISOU 199 CG ARG A 25 1577 2630 3413 -504 -12 70 C ATOM 200 CD ARG A 25 -7.296 0.573 12.597 1.00 31.54 C ANISOU 200 CD ARG A 25 1644 5234 5107 333 -558 658 C ATOM 201 NE ARG A 25 -7.110 1.191 11.298 1.00 44.68 N ANISOU 201 NE ARG A 25 4605 6514 5859 616 -1632 2090 N ATOM 202 CZ ARG A 25 -7.734 2.187 10.722 1.00 52.18 C ANISOU 202 CZ ARG A 25 4629 7302 7896 891 -1644 2915 C ATOM 203 NH1 ARG A 25 -8.723 2.866 11.282 1.00 73.98 N ANISOU 203 NH1 ARG A 25 2603 10748 14758 1870 -1445 2624 N ATOM 204 NH2 ARG A 25 -7.352 2.549 9.495 1.00 58.76 N ANISOU 204 NH2 ARG A 25 5136 7959 9230 -3299 -2634 5196 N ATOM 205 N GLU A 26 -2.705 -0.310 11.430 1.00 11.33 N ANISOU 205 N GLU A 26 1202 1425 1678 -256 -16 -3 N ATOM 206 CA GLU A 26 -2.297 -0.827 10.130 1.00 11.90 C ANISOU 206 CA GLU A 26 1419 1581 1522 -108 -180 73 C ATOM 207 C GLU A 26 -1.212 -1.865 10.289 1.00 11.11 C ANISOU 207 C GLU A 26 1458 1323 1442 -187 -105 72 C ATOM 208 O GLU A 26 -1.208 -2.885 9.587 1.00 12.84 O ANISOU 208 O GLU A 26 1704 1525 1651 -159 -91 -117 O ATOM 209 CB GLU A 26 -1.822 0.341 9.255 1.00 13.17 C ANISOU 209 CB GLU A 26 1796 1635 1572 -36 -189 248 C ATOM 210 CG GLU A 26 -2.966 1.248 8.804 1.00 15.21 C ANISOU 210 CG GLU A 26 2127 1753 1899 271 -202 193 C ATOM 211 CD GLU A 26 -3.943 0.566 7.876 1.00 19.11 C ANISOU 211 CD GLU A 26 2341 2471 2450 496 -781 -12 C ATOM 212 OE1 GLU A 26 -3.507 -0.244 7.039 1.00 24.45 O ANISOU 212 OE1 GLU A 26 3454 3408 2430 829 -1217 -687 O ATOM 213 OE2 GLU A 26 -5.118 0.894 7.982 1.00 27.95 O ANISOU 213 OE2 GLU A 26 2234 3671 4713 497 -879 -488 O ATOM 214 N CYS A 27 -0.287 -1.683 11.205 1.00 10.03 N ANISOU 214 N CYS A 27 1245 1150 1417 -189 121 110 N ATOM 215 CA CYS A 27 0.707 -2.687 11.492 1.00 10.33 C ANISOU 215 CA CYS A 27 1268 1243 1415 -75 163 119 C ATOM 216 C CYS A 27 0.088 -3.973 11.991 1.00 10.78 C ANISOU 216 C CYS A 27 1406 1136 1553 -112 84 117 C ATOM 217 O CYS A 27 0.512 -5.061 11.611 1.00 12.14 O ANISOU 217 O CYS A 27 1693 1219 1702 -162 182 13 O ATOM 218 CB CYS A 27 1.706 -2.147 12.502 1.00 11.26 C ANISOU 218 CB CYS A 27 1356 1372 1550 -181 131 5 C ATOM 219 SG CYS A 27 2.746 -0.809 11.867 1.00 11.26 S ANISOU 219 SG CYS A 27 1309 1261 1708 -98 115 -47 S ATOM 220 N GLY A 28 -0.916 -3.863 12.849 1.00 11.72 N ANISOU 220 N GLY A 28 1513 1304 1635 -278 150 152 N ATOM 221 CA GLY A 28 -1.619 -5.034 13.392 1.00 11.92 C ANISOU 221 CA GLY A 28 1694 1247 1589 -337 123 137 C ATOM 222 C GLY A 28 -2.374 -5.813 12.339 1.00 11.80 C ANISOU 222 C GLY A 28 1605 1246 1631 -272 37 98 C ATOM 223 O GLY A 28 -2.477 -7.020 12.451 1.00 12.67 O ANISOU 223 O GLY A 28 1603 1226 1985 -279 112 164 O ATOM 224 N ILE A 29 -2.927 -5.136 11.354 1.00 12.99 N ANISOU 224 N ILE A 29 1570 1284 2083 -390 -246 232 N ATOM 225 CA ILE A 29 -3.577 -5.858 10.241 1.00 13.77 C ANISOU 225 CA ILE A 29 1758 1439 2036 -458 -328 277 C ATOM 226 C ILE A 29 -2.583 -6.739 9.510 1.00 14.89 C ANISOU 226 C ILE A 29 1956 1899 1804 -431 -349 75 C ATOM 227 O ILE A 29 -2.965 -7.802 9.008 1.00 16.85 O ANISOU 227 O ILE A 29 1999 1945 2460 -300 -216 -270 O ATOM 228 CB ILE A 29 -4.273 -4.846 9.342 1.00 19.61 C ANISOU 228 CB ILE A 29 2511 1617 3323 -446 -1436 333 C ATOM 229 CG1 ILE A 29 -5.451 -4.216 10.064 1.00 25.63 C ANISOU 229 CG1 ILE A 29 2852 2476 4410 550 -1946 -490 C ATOM 230 CG2 ILE A 29 -4.722 -5.514 8.046 1.00 22.85 C ANISOU 230 CG2 ILE A 29 3155 2684 2844 -593 -1439 523 C ATOM 231 CD1 ILE A 29 -6.005 -2.986 9.379 1.00 28.91 C ANISOU 231 CD1 ILE A 29 3129 2171 5684 102 -2224 -118 C ATOM 232 N LYS A 30 -1.313 -6.341 9.422 1.00 14.06 N ANISOU 232 N LYS A 30 1811 1818 1714 -233 -395 126 N ATOM 233 CA LYS A 30 -0.268 -7.151 8.815 1.00 14.77 C ANISOU 233 CA LYS A 30 2224 1944 1446 -347 -40 -52 C ATOM 234 C LYS A 30 0.426 -8.064 9.802 1.00 13.14 C ANISOU 234 C LYS A 30 1858 1704 1433 -94 102 -323 C ATOM 235 O LYS A 30 1.475 -8.627 9.535 1.00 17.15 O ANISOU 235 O LYS A 30 2198 2330 1988 169 498 -261 O ATOM 236 CB LYS A 30 0.768 -6.252 8.109 1.00 20.00 C ANISOU 236 CB LYS A 30 2812 2959 1828 -649 405 363 C ATOM 237 CG LYS A 30 0.284 -5.626 6.797 1.00 29.81 C ANISOU 237 CG LYS A 30 4667 3918 2742 -619 175 1530 C ATOM 238 CD LYS A 30 -0.128 -6.625 5.757 1.00 44.10 C ANISOU 238 CD LYS A 30 7242 6788 2727 -1539 -1884 1150 C ATOM 239 CE LYS A 30 -0.211 -6.166 4.314 1.00 57.05 C ANISOU 239 CE LYS A 30 9192 9229 3257 -1874 -2582 2219 C ATOM 240 NZ LYS A 30 -0.509 -4.731 4.066 1.00 76.53 N ANISOU 240 NZ LYS A 30 13154 10015 5909 -1128 -4087 3967 N ATOM 241 N LYS A 31 -0.158 -8.225 10.980 1.00 12.50 N ANISOU 241 N LYS A 31 1751 1643 1355 -22 12 -151 N ATOM 242 CA LYS A 31 0.237 -9.137 12.056 1.00 12.93 C ANISOU 242 CA LYS A 31 1809 1693 1412 -10 39 -238 C ATOM 243 C LYS A 31 1.441 -8.685 12.831 1.00 11.88 C ANISOU 243 C LYS A 31 1731 1396 1388 45 34 -95 C ATOM 244 O LYS A 31 2.018 -9.409 13.585 1.00 14.34 O ANISOU 244 O LYS A 31 1801 1532 2114 65 -116 238 O ATOM 245 CB LYS A 31 0.466 -10.572 11.506 1.00 15.01 C ANISOU 245 CB LYS A 31 2220 1470 2014 -182 67 -223 C ATOM 246 CG LYS A 31 -0.888 -11.093 10.970 1.00 18.49 C ANISOU 246 CG LYS A 31 2354 2187 2484 -544 364 -768 C ATOM 247 CD LYS A 31 -0.868 -12.583 10.753 1.00 23.86 C ANISOU 247 CD LYS A 31 3047 2262 3757 -845 344 -1001 C ATOM 248 CE LYS A 31 -2.276 -13.055 10.323 1.00 28.06 C ANISOU 248 CE LYS A 31 3380 2915 4366 -1343 -16 -827 C ATOM 249 NZ LYS A 31 -2.224 -13.392 8.902 1.00 46.11 N ANISOU 249 NZ LYS A 31 4394 8005 5122 -198 -843 -3027 N ATOM 250 N GLY A 32 1.747 -7.385 12.740 1.00 11.35 N ANISOU 250 N GLY A 32 1682 1466 1164 -78 -11 -3 N ATOM 251 CA GLY A 32 2.738 -6.806 13.581 1.00 10.70 C ANISOU 251 CA GLY A 32 1394 1393 1278 -41 79 32 C ATOM 252 C GLY A 32 2.253 -6.549 14.992 1.00 10.65 C ANISOU 252 C GLY A 32 1417 1370 1261 -41 -9 23 C ATOM 253 O GLY A 32 1.057 -6.410 15.236 1.00 15.49 O ANISOU 253 O GLY A 32 1384 2944 1557 50 47 -507 O ATOM 254 N SER A 33 3.158 -6.428 15.900 1.00 10.79 N ANISOU 254 N SER A 33 1402 1480 1217 -59 108 51 N ATOM 255 CA SER A 33 2.807 -6.260 17.313 1.00 11.74 C ANISOU 255 CA SER A 33 1947 1344 1170 -190 124 23 C ATOM 256 C SER A 33 2.735 -4.828 17.770 1.00 10.91 C ANISOU 256 C SER A 33 1758 1327 1061 -132 284 164 C ATOM 257 O SER A 33 2.145 -4.565 18.786 1.00 14.63 O ANISOU 257 O SER A 33 2607 1509 1442 -265 864 22 O ATOM 258 CB SER A 33 3.845 -7.016 18.148 1.00 13.53 C ANISOU 258 CB SER A 33 2237 1426 1476 -43 63 180 C ATOM 259 OG SER A 33 5.097 -6.486 17.976 1.00 16.39 O ANISOU 259 OG SER A 33 1981 2714 1533 -10 90 407 O ATOM 260 N SER A 34 3.328 -3.901 17.047 1.00 10.32 N ANISOU 260 N SER A 34 1635 1233 1053 -79 257 162 N ATOM 261 CA SER A 34 3.351 -2.498 17.452 1.00 11.51 C ANISOU 261 CA SER A 34 1808 1220 1346 48 268 202 C ATOM 262 C SER A 34 3.625 -1.665 16.235 1.00 11.13 C ANISOU 262 C SER A 34 1760 1181 1288 -117 368 187 C ATOM 263 O SER A 34 4.181 -2.135 15.235 1.00 12.36 O ANISOU 263 O SER A 34 1859 1301 1535 102 574 151 O ATOM 264 CB SER A 34 4.468 -2.309 18.501 1.00 13.97 C ANISOU 264 CB SER A 34 2650 1345 1312 -358 -48 205 C ATOM 265 OG SER A 34 4.242 -1.055 19.100 1.00 22.18 O ANISOU 265 OG SER A 34 4378 1811 2237 -80 -494 -403 O ATOM 266 N GLY A 35 3.251 -0.396 16.261 1.00 11.56 N ANISOU 266 N GLY A 35 1835 1214 1345 -111 606 165 N ATOM 267 CA GLY A 35 3.676 0.520 15.231 1.00 11.69 C ANISOU 267 CA GLY A 35 1851 1085 1508 -123 411 211 C ATOM 268 C GLY A 35 3.422 1.941 15.676 1.00 10.34 C ANISOU 268 C GLY A 35 1582 1175 1170 6 258 159 C ATOM 269 O GLY A 35 2.733 2.186 16.658 1.00 12.37 O ANISOU 269 O GLY A 35 1889 1494 1316 -131 505 36 O ATOM 270 N TYR A 36 3.984 2.872 14.928 1.00 9.92 N ANISOU 270 N TYR A 36 1576 1010 1183 -127 216 30 N ATOM 271 CA TYR A 36 3.829 4.274 15.241 1.00 9.32 C ANISOU 271 CA TYR A 36 1442 1042 1057 -11 220 34 C ATOM 272 C TYR A 36 4.043 5.069 13.954 1.00 8.75 C ANISOU 272 C TYR A 36 1271 997 1055 -129 183 -56 C ATOM 273 O TYR A 36 4.537 4.591 12.953 1.00 9.48 O ANISOU 273 O TYR A 36 1537 971 1096 -41 175 -18 O ATOM 274 CB TYR A 36 4.768 4.728 16.312 1.00 10.26 C ANISOU 274 CB TYR A 36 1747 1014 1139 -6 31 38 C ATOM 275 CG TYR A 36 6.217 4.915 15.947 1.00 10.23 C ANISOU 275 CG TYR A 36 1679 1004 1204 -32 -2 -125 C ATOM 276 CD1 TYR A 36 7.032 3.823 15.702 1.00 12.54 C ANISOU 276 CD1 TYR A 36 1684 1001 2082 -69 7 -218 C ATOM 277 CD2 TYR A 36 6.796 6.165 15.810 1.00 10.98 C ANISOU 277 CD2 TYR A 36 1795 1014 1360 -12 160 -89 C ATOM 278 CE1 TYR A 36 8.369 4.002 15.361 1.00 14.38 C ANISOU 278 CE1 TYR A 36 1646 1253 2564 124 -9 -17 C ATOM 279 CE2 TYR A 36 8.089 6.348 15.469 1.00 11.50 C ANISOU 279 CE2 TYR A 36 1832 1135 1403 -213 116 -233 C ATOM 280 CZ TYR A 36 8.873 5.255 15.242 1.00 11.59 C ANISOU 280 CZ TYR A 36 1526 1325 1551 -69 -208 -213 C ATOM 281 OH TYR A 36 10.192 5.427 14.891 1.00 14.71 O ANISOU 281 OH TYR A 36 1718 1531 2341 -83 35 -97 O ATOM 282 N CYS A 37 3.618 6.310 14.017 1.00 9.21 N ANISOU 282 N CYS A 37 1397 989 1112 -34 220 67 N ATOM 283 CA CYS A 37 3.840 7.254 12.902 1.00 8.69 C ANISOU 283 CA CYS A 37 1296 990 1016 -99 88 -50 C ATOM 284 C CYS A 37 5.237 7.846 13.018 1.00 8.68 C ANISOU 284 C CYS A 37 1354 1051 895 -79 13 106 C ATOM 285 O CYS A 37 5.485 8.796 13.740 1.00 10.27 O ANISOU 285 O CYS A 37 1438 1192 1271 -171 148 -249 O ATOM 286 CB CYS A 37 2.747 8.320 12.927 1.00 9.52 C ANISOU 286 CB CYS A 37 1325 1103 1189 -47 178 101 C ATOM 287 SG CYS A 37 2.915 9.573 11.645 1.00 11.30 S ANISOU 287 SG CYS A 37 1608 1190 1496 9 67 180 S ATOM 288 N ALA A 38 6.155 7.245 12.253 1.00 9.10 N ANISOU 288 N ALA A 38 1382 967 1108 -204 180 -20 N ATOM 289 CA ALA A 38 7.498 7.711 12.097 1.00 9.33 C ANISOU 289 CA ALA A 38 1430 993 1124 -304 178 -95 C ATOM 290 C ALA A 38 7.460 8.775 10.992 1.00 9.56 C ANISOU 290 C ALA A 38 1294 1073 1265 -253 368 3 C ATOM 291 O ALA A 38 7.881 8.558 9.878 1.00 10.64 O ANISOU 291 O ALA A 38 1546 1340 1157 -110 188 7 O ATOM 292 CB ALA A 38 8.434 6.554 11.749 1.00 10.59 C ANISOU 292 CB ALA A 38 1401 1239 1385 -156 176 -81 C ATOM 293 N TRP A 39 6.871 9.895 11.368 1.00 10.78 N ANISOU 293 N TRP A 39 1719 1193 1183 -98 339 17 N ATOM 294 CA TRP A 39 6.363 10.914 10.464 1.00 10.52 C ANISOU 294 CA TRP A 39 1703 1072 1221 -177 194 -43 C ATOM 295 C TRP A 39 7.343 11.191 9.337 1.00 10.06 C ANISOU 295 C TRP A 39 1614 1080 1130 -89 59 -45 C ATOM 296 O TRP A 39 8.513 11.497 9.620 1.00 11.96 O ANISOU 296 O TRP A 39 1676 1484 1384 -343 105 28 O ATOM 297 CB TRP A 39 6.134 12.144 11.290 1.00 11.43 C ANISOU 297 CB TRP A 39 1750 1222 1370 -52 258 -128 C ATOM 298 CG TRP A 39 5.392 13.266 10.674 1.00 12.20 C ANISOU 298 CG TRP A 39 1964 1188 1482 -48 217 -27 C ATOM 299 CD1 TRP A 39 4.039 13.472 10.738 1.00 13.79 C ANISOU 299 CD1 TRP A 39 1925 1448 1867 58 53 183 C ATOM 300 CD2 TRP A 39 5.913 14.359 9.921 1.00 14.20 C ANISOU 300 CD2 TRP A 39 2595 1406 1397 -47 591 46 C ATOM 301 NE1 TRP A 39 3.668 14.597 10.071 1.00 17.55 N ANISOU 301 NE1 TRP A 39 2654 1747 2266 572 338 386 N ATOM 302 CE2 TRP A 39 4.824 15.166 9.567 1.00 16.36 C ANISOU 302 CE2 TRP A 39 3079 1430 1706 236 449 187 C ATOM 303 CE3 TRP A 39 7.201 14.702 9.529 1.00 16.14 C ANISOU 303 CE3 TRP A 39 2855 1640 1636 -374 733 30 C ATOM 304 CZ2 TRP A 39 4.973 16.320 8.830 1.00 20.30 C ANISOU 304 CZ2 TRP A 39 4335 1385 1994 104 332 230 C ATOM 305 CZ3 TRP A 39 7.351 15.860 8.797 1.00 20.95 C ANISOU 305 CZ3 TRP A 39 3973 1883 2104 -795 708 286 C ATOM 306 CH2 TRP A 39 6.246 16.631 8.464 1.00 22.61 C ANISOU 306 CH2 TRP A 39 4753 1776 2061 -356 641 588 C ATOM 307 N PRO A 40 6.931 11.081 8.097 1.00 10.59 N ANISOU 307 N PRO A 40 1710 1161 1153 -108 65 110 N ATOM 308 CA PRO A 40 5.562 10.988 7.608 1.00 12.17 C ANISOU 308 CA PRO A 40 1909 1202 1513 13 -290 163 C ATOM 309 C PRO A 40 4.977 9.616 7.355 1.00 9.99 C ANISOU 309 C PRO A 40 1402 1290 1102 -116 96 270 C ATOM 310 O PRO A 40 3.941 9.570 6.729 1.00 11.85 O ANISOU 310 O PRO A 40 1433 1550 1518 -45 -58 303 O ATOM 311 CB PRO A 40 5.722 11.725 6.258 1.00 18.37 C ANISOU 311 CB PRO A 40 3466 1450 2064 -495 -855 846 C ATOM 312 CG PRO A 40 7.034 11.250 5.789 1.00 20.65 C ANISOU 312 CG PRO A 40 3303 3242 1301 -1397 -103 563 C ATOM 313 CD PRO A 40 7.907 11.287 6.989 1.00 14.44 C ANISOU 313 CD PRO A 40 2486 1807 1194 -738 304 8 C ATOM 314 N ALA A 41 5.612 8.544 7.809 1.00 9.76 N ANISOU 314 N ALA A 41 1452 1222 1034 -22 96 84 N ATOM 315 CA ALA A 41 5.181 7.212 7.410 1.00 9.55 C ANISOU 315 CA ALA A 41 1277 1248 1105 -29 23 65 C ATOM 316 C ALA A 41 5.077 6.261 8.596 1.00 8.58 C ANISOU 316 C ALA A 41 1084 1106 1068 28 172 -39 C ATOM 317 O ALA A 41 5.729 6.386 9.591 1.00 10.15 O ANISOU 317 O ALA A 41 1433 1340 1084 -204 -61 61 O ATOM 318 CB ALA A 41 6.210 6.621 6.406 1.00 13.82 C ANISOU 318 CB ALA A 41 2715 1231 1306 -256 793 -21 C ATOM 319 N CYS A 42 4.233 5.240 8.403 1.00 9.31 N ANISOU 319 N CYS A 42 1282 1238 1017 -55 -14 74 N ATOM 320 CA CYS A 42 4.065 4.235 9.441 1.00 9.14 C ANISOU 320 CA CYS A 42 1140 1242 1091 0 79 76 C ATOM 321 C CYS A 42 5.226 3.273 9.482 1.00 9.16 C ANISOU 321 C CYS A 42 1211 1158 1112 54 182 56 C ATOM 322 O CYS A 42 5.633 2.720 8.460 1.00 11.12 O ANISOU 322 O CYS A 42 1494 1675 1057 297 182 62 O ATOM 323 CB CYS A 42 2.790 3.436 9.183 1.00 9.95 C ANISOU 323 CB CYS A 42 1248 1109 1424 -17 58 -94 C ATOM 324 SG CYS A 42 1.231 4.317 9.371 1.00 10.66 S ANISOU 324 SG CYS A 42 1226 1482 1342 -8 83 -6 S ATOM 325 N TYR A 43 5.669 2.983 10.698 1.00 8.93 N ANISOU 325 N TYR A 43 1261 1057 1073 139 254 68 N ATOM 326 CA TYR A 43 6.740 2.072 10.976 1.00 8.72 C ANISOU 326 CA TYR A 43 1256 1043 1015 54 170 104 C ATOM 327 C TYR A 43 6.223 1.004 11.923 1.00 8.80 C ANISOU 327 C TYR A 43 1301 964 1078 29 198 41 C ATOM 328 O TYR A 43 5.570 1.321 12.927 1.00 10.66 O ANISOU 328 O TYR A 43 1833 1005 1213 24 501 71 O ATOM 329 CB TYR A 43 7.921 2.808 11.568 1.00 10.60 C ANISOU 329 CB TYR A 43 1337 1107 1582 -75 7 259 C ATOM 330 CG TYR A 43 9.184 1.999 11.701 1.00 10.00 C ANISOU 330 CG TYR A 43 1286 919 1596 -102 25 103 C ATOM 331 CD1 TYR A 43 9.473 1.261 12.810 1.00 11.67 C ANISOU 331 CD1 TYR A 43 1656 1103 1676 -43 -78 223 C ATOM 332 CD2 TYR A 43 10.108 2.006 10.654 1.00 11.92 C ANISOU 332 CD2 TYR A 43 1343 1406 1779 -104 127 233 C ATOM 333 CE1 TYR A 43 10.649 0.519 12.932 1.00 12.82 C ANISOU 333 CE1 TYR A 43 1647 1281 1945 -71 -234 373 C ATOM 334 CE2 TYR A 43 11.270 1.303 10.760 1.00 13.09 C ANISOU 334 CE2 TYR A 43 1289 1774 1910 -25 161 93 C ATOM 335 CZ TYR A 43 11.529 0.562 11.886 1.00 12.87 C ANISOU 335 CZ TYR A 43 1402 1376 2114 -90 -172 85 C ATOM 336 OH TYR A 43 12.729 -0.129 11.900 1.00 16.79 O ANISOU 336 OH TYR A 43 1543 1828 3007 52 -114 444 O ATOM 337 N CYS A 44 6.532 -0.251 11.669 1.00 8.39 N ANISOU 337 N CYS A 44 1143 978 1069 -38 172 15 N ATOM 338 CA CYS A 44 6.057 -1.371 12.454 1.00 8.98 C ANISOU 338 CA CYS A 44 1219 1020 1174 -95 192 104 C ATOM 339 C CYS A 44 7.180 -2.127 13.094 1.00 9.15 C ANISOU 339 C CYS A 44 1450 1048 979 129 233 -53 C ATOM 340 O CYS A 44 8.274 -2.265 12.552 1.00 10.58 O ANISOU 340 O CYS A 44 1355 1345 1322 171 300 176 O ATOM 341 CB CYS A 44 5.318 -2.355 11.561 1.00 10.89 C ANISOU 341 CB CYS A 44 1328 1108 1701 -127 88 -126 C ATOM 342 SG CYS A 44 3.997 -1.733 10.584 1.00 11.44 S ANISOU 342 SG CYS A 44 1416 1538 1393 -100 78 -30 S ATOM 343 N TYR A 45 6.852 -2.708 14.241 1.00 9.80 N ANISOU 343 N TYR A 45 1361 1216 1148 119 266 151 N ATOM 344 CA TYR A 45 7.662 -3.702 14.935 1.00 9.98 C ANISOU 344 CA TYR A 45 1538 1090 1165 172 182 126 C ATOM 345 C TYR A 45 6.923 -5.051 14.972 1.00 9.93 C ANISOU 345 C TYR A 45 1537 1161 1076 113 174 64 C ATOM 346 O TYR A 45 5.701 -5.085 14.943 1.00 10.79 O ANISOU 346 O TYR A 45 1545 1109 1445 177 170 148 O ATOM 347 CB ATYR A 45 8.003 -3.339 16.366 0.40 11.48 C ANISOU 347 CB ATYR A 45 2188 936 1239 173 -38 94 C ATOM 348 CB BTYR A 45 7.950 -3.284 16.374 0.61 11.63 C ANISOU 348 CB BTYR A 45 2303 951 1165 37 23 174 C ATOM 349 CG ATYR A 45 8.456 -1.933 16.638 0.40 11.96 C ANISOU 349 CG ATYR A 45 2423 1013 1109 -88 -21 348 C ATOM 350 CG BTYR A 45 8.796 -2.038 16.452 0.61 13.14 C ANISOU 350 CG BTYR A 45 2226 1157 1608 -30 122 -85 C ATOM 351 CD1ATYR A 45 9.812 -1.661 16.807 0.40 15.17 C ANISOU 351 CD1ATYR A 45 2420 1682 1662 -294 442 -575 C ATOM 352 CD1BTYR A 45 10.180 -2.160 16.474 0.61 16.34 C ANISOU 352 CD1BTYR A 45 2233 1604 2371 -37 -245 -547 C ATOM 353 CD2ATYR A 45 7.559 -0.873 16.720 0.40 14.65 C ANISOU 353 CD2ATYR A 45 2659 663 2245 -203 251 384 C ATOM 354 CD2BTYR A 45 8.237 -0.759 16.492 0.61 12.80 C ANISOU 354 CD2BTYR A 45 2348 945 1572 -190 255 177 C ATOM 355 CE1ATYR A 45 10.233 -0.362 17.053 0.40 16.68 C ANISOU 355 CE1ATYR A 45 2980 1633 1725 -651 101 -40 C ATOM 356 CE1BTYR A 45 10.993 -1.032 16.544 0.61 18.46 C ANISOU 356 CE1BTYR A 45 2537 2076 2402 -591 305 -246 C ATOM 357 CE2ATYR A 45 7.957 0.414 16.971 0.40 17.03 C ANISOU 357 CE2ATYR A 45 3187 866 2416 -478 132 185 C ATOM 358 CE2BTYR A 45 9.051 0.346 16.563 0.61 16.55 C ANISOU 358 CE2BTYR A 45 2944 1262 2084 -587 265 66 C ATOM 359 CZ ATYR A 45 9.311 0.656 17.139 0.40 18.00 C ANISOU 359 CZ ATYR A 45 3386 1290 2162 -582 -552 37 C ATOM 360 CZ BTYR A 45 10.418 0.214 16.587 0.61 17.32 C ANISOU 360 CZ BTYR A 45 2876 1723 1984 -892 -178 51 C ATOM 361 OH ATYR A 45 9.671 1.965 17.383 0.40 22.69 O ANISOU 361 OH ATYR A 45 3892 1336 3392 -784 -1045 125 O ATOM 362 OH BTYR A 45 11.219 1.336 16.648 0.61 23.83 O ANISOU 362 OH BTYR A 45 3726 2268 3062 -1589 158 -369 O ATOM 363 N GLY A 46 7.686 -6.127 15.053 1.00 10.09 N ANISOU 363 N GLY A 46 1470 1133 1231 111 234 -3 N ATOM 364 CA GLY A 46 7.073 -7.412 15.290 1.00 10.57 C ANISOU 364 CA GLY A 46 1549 1207 1262 32 152 201 C ATOM 365 C GLY A 46 6.340 -7.973 14.108 1.00 9.99 C ANISOU 365 C GLY A 46 1489 1071 1234 58 235 89 C ATOM 366 O GLY A 46 5.438 -8.784 14.263 1.00 11.31 O ANISOU 366 O GLY A 46 1425 1354 1517 -35 183 154 O ATOM 367 N LEU A 47 6.722 -7.600 12.899 1.00 10.15 N ANISOU 367 N LEU A 47 1437 1144 1277 -181 204 -159 N ATOM 368 CA LEU A 47 6.155 -8.221 11.721 1.00 9.63 C ANISOU 368 CA LEU A 47 1374 1038 1246 -91 200 -116 C ATOM 369 C LEU A 47 6.765 -9.618 11.557 1.00 10.29 C ANISOU 369 C LEU A 47 1637 1099 1173 -56 281 -76 C ATOM 370 O LEU A 47 7.964 -9.795 11.731 1.00 11.36 O ANISOU 370 O LEU A 47 1589 1080 1648 95 142 -91 O ATOM 371 CB LEU A 47 6.484 -7.423 10.457 1.00 11.03 C ANISOU 371 CB LEU A 47 1929 1052 1209 48 426 -149 C ATOM 372 CG LEU A 47 5.866 -6.020 10.388 1.00 11.45 C ANISOU 372 CG LEU A 47 2107 1105 1139 125 222 -112 C ATOM 373 CD1 LEU A 47 6.554 -5.203 9.309 1.00 14.05 C ANISOU 373 CD1 LEU A 47 2460 1406 1472 -25 237 176 C ATOM 374 CD2 LEU A 47 4.372 -6.110 10.203 1.00 14.69 C ANISOU 374 CD2 LEU A 47 2078 1691 1812 417 363 54 C ATOM 375 N PRO A 48 5.983 -10.597 11.139 1.00 10.85 N ANISOU 375 N PRO A 48 1684 1051 1388 -30 190 -123 N ATOM 376 CA PRO A 48 6.550 -11.876 10.717 1.00 11.10 C ANISOU 376 CA PRO A 48 1843 1062 1313 42 261 -98 C ATOM 377 C PRO A 48 7.463 -11.670 9.543 1.00 10.71 C ANISOU 377 C PRO A 48 1624 1104 1341 -76 139 -203 C ATOM 378 O PRO A 48 7.426 -10.727 8.784 1.00 12.02 O ANISOU 378 O PRO A 48 1948 1212 1406 60 397 14 O ATOM 379 CB PRO A 48 5.325 -12.705 10.329 1.00 14.71 C ANISOU 379 CB PRO A 48 1953 1374 2262 -365 625 -499 C ATOM 380 CG PRO A 48 4.159 -12.026 10.906 1.00 19.14 C ANISOU 380 CG PRO A 48 1866 1505 3902 -197 347 -909 C ATOM 381 CD PRO A 48 4.533 -10.571 11.050 1.00 12.29 C ANISOU 381 CD PRO A 48 1685 1345 1638 -5 9 -336 C ATOM 382 N ASN A 49 8.304 -12.716 9.371 1.00 12.38 N ANISOU 382 N ASN A 49 1985 1274 1444 166 312 -155 N ATOM 383 CA ASN A 49 9.403 -12.593 8.394 1.00 13.19 C ANISOU 383 CA ASN A 49 1722 1663 1625 232 222 -221 C ATOM 384 C ASN A 49 8.925 -12.594 6.987 1.00 11.98 C ANISOU 384 C ASN A 49 1660 1403 1487 101 395 -216 C ATOM 385 O ASN A 49 9.627 -12.164 6.061 1.00 15.04 O ANISOU 385 O ASN A 49 1984 1952 1780 -115 572 -31 O ATOM 386 CB ASN A 49 10.391 -13.725 8.631 1.00 16.08 C ANISOU 386 CB ASN A 49 1869 2185 2056 552 132 -223 C ATOM 387 CG ASN A 49 11.317 -13.441 9.792 1.00 23.23 C ANISOU 387 CG ASN A 49 2713 3657 2457 1391 -545 -777 C ATOM 388 OD1 ASN A 49 11.507 -12.258 10.119 1.00 28.97 O ANISOU 388 OD1 ASN A 49 3325 4254 3427 1399 -1349 -1876 O ATOM 389 ND2 ASN A 49 11.868 -14.457 10.410 1.00 33.51 N ANISOU 389 ND2 ASN A 49 5135 5089 2509 2897 -833 -422 N ATOM 390 N TRP A 50 7.719 -13.049 6.692 1.00 11.91 N ANISOU 390 N TRP A 50 1716 1468 1340 56 446 -306 N ATOM 391 CA TRP A 50 7.170 -13.092 5.371 1.00 12.51 C ANISOU 391 CA TRP A 50 1823 1542 1390 -64 290 -192 C ATOM 392 C TRP A 50 6.609 -11.763 4.898 1.00 12.43 C ANISOU 392 C TRP A 50 1810 1574 1340 -181 281 -226 C ATOM 393 O TRP A 50 6.272 -11.651 3.725 1.00 16.21 O ANISOU 393 O TRP A 50 2990 1791 1378 418 6 -210 O ATOM 394 CB TRP A 50 6.104 -14.165 5.266 1.00 14.51 C ANISOU 394 CB TRP A 50 2180 1528 1805 -199 315 -378 C ATOM 395 CG TRP A 50 4.913 -14.014 6.174 1.00 13.61 C ANISOU 395 CG TRP A 50 1814 1551 1806 -313 133 -435 C ATOM 396 CD1 TRP A 50 3.861 -13.160 6.060 1.00 16.56 C ANISOU 396 CD1 TRP A 50 1864 2055 2374 -117 154 -73 C ATOM 397 CD2 TRP A 50 4.681 -14.793 7.346 1.00 14.25 C ANISOU 397 CD2 TRP A 50 1978 1675 1760 -240 168 -464 C ATOM 398 NE1 TRP A 50 3.005 -13.363 7.086 1.00 17.40 N ANISOU 398 NE1 TRP A 50 1747 2300 2565 -120 170 -225 N ATOM 399 CE2 TRP A 50 3.478 -14.362 7.893 1.00 15.85 C ANISOU 399 CE2 TRP A 50 2194 1723 2105 -354 441 -522 C ATOM 400 CE3 TRP A 50 5.343 -15.812 7.997 1.00 16.23 C ANISOU 400 CE3 TRP A 50 2559 1961 1646 -62 312 -280 C ATOM 401 CZ2 TRP A 50 2.922 -14.882 9.031 1.00 18.88 C ANISOU 401 CZ2 TRP A 50 2436 2427 2310 -524 678 -381 C ATOM 402 CZ3 TRP A 50 4.816 -16.354 9.142 1.00 17.78 C ANISOU 402 CZ3 TRP A 50 2866 2093 1798 -424 435 -231 C ATOM 403 CH2 TRP A 50 3.616 -15.885 9.649 1.00 19.53 C ANISOU 403 CH2 TRP A 50 3044 2182 2196 -519 825 -236 C ATOM 404 N VAL A 51 6.481 -10.780 5.761 1.00 12.15 N ANISOU 404 N VAL A 51 1906 1423 1286 -168 234 -96 N ATOM 405 CA VAL A 51 5.915 -9.505 5.366 1.00 11.84 C ANISOU 405 CA VAL A 51 1827 1448 1226 -135 42 -176 C ATOM 406 C VAL A 51 6.934 -8.661 4.616 1.00 13.26 C ANISOU 406 C VAL A 51 1988 1635 1414 -91 184 94 C ATOM 407 O VAL A 51 8.036 -8.471 5.072 1.00 15.62 O ANISOU 407 O VAL A 51 2046 2074 1814 -315 91 295 O ATOM 408 CB VAL A 51 5.374 -8.732 6.591 1.00 13.30 C ANISOU 408 CB VAL A 51 2171 1576 1308 57 202 -93 C ATOM 409 CG1 VAL A 51 4.820 -7.373 6.125 1.00 16.54 C ANISOU 409 CG1 VAL A 51 2613 1857 1813 586 341 33 C ATOM 410 CG2 VAL A 51 4.323 -9.552 7.298 1.00 17.52 C ANISOU 410 CG2 VAL A 51 2628 1910 2120 45 892 -83 C ATOM 411 N LYS A 52 6.536 -8.135 3.471 1.00 13.81 N ANISOU 411 N LYS A 52 2240 1437 1569 -51 167 141 N ATOM 412 CA LYS A 52 7.377 -7.243 2.696 1.00 15.79 C ANISOU 412 CA LYS A 52 2433 1903 1664 -226 212 352 C ATOM 413 C LYS A 52 7.351 -5.838 3.267 1.00 17.93 C ANISOU 413 C LYS A 52 2505 1427 2882 129 369 625 C ATOM 414 O LYS A 52 6.281 -5.280 3.564 1.00 23.91 O ANISOU 414 O LYS A 52 2586 1759 4741 365 478 767 O ATOM 415 CB LYS A 52 6.773 -7.227 1.273 1.00 23.83 C ANISOU 415 CB LYS A 52 3146 4082 1827 -843 -34 972 C ATOM 416 CG LYS A 52 5.341 -6.671 1.335 1.00 31.58 C ATOM 417 CD LYS A 52 4.771 -5.953 0.128 1.00 31.58 C ATOM 418 CE LYS A 52 3.795 -4.854 0.520 1.00 31.58 C ATOM 419 NZ LYS A 52 2.395 -5.065 0.070 1.00 31.58 N ATOM 420 N VAL A 53 8.504 -5.241 3.496 1.00 16.29 N ANISOU 420 N VAL A 53 2614 1564 2010 -23 840 102 N ATOM 421 CA VAL A 53 8.549 -3.871 3.969 1.00 15.60 C ANISOU 421 CA VAL A 53 2754 1575 1600 83 806 226 C ATOM 422 C VAL A 53 9.253 -3.013 2.914 1.00 14.30 C ANISOU 422 C VAL A 53 2166 1629 1640 31 653 245 C ATOM 423 O VAL A 53 9.911 -3.559 2.004 1.00 17.02 O ANISOU 423 O VAL A 53 2800 1841 1825 195 977 168 O ATOM 424 CB VAL A 53 9.253 -3.719 5.342 1.00 16.47 C ANISOU 424 CB VAL A 53 2946 1742 1569 8 820 212 C ATOM 425 CG1 VAL A 53 8.401 -4.380 6.403 1.00 20.03 C ANISOU 425 CG1 VAL A 53 3807 2098 1704 -589 904 351 C ATOM 426 CG2 VAL A 53 10.677 -4.245 5.318 1.00 18.81 C ANISOU 426 CG2 VAL A 53 3087 1945 2115 219 387 308 C ATOM 427 N TRP A 54 9.138 -1.718 3.026 1.00 14.40 N ANISOU 427 N TRP A 54 2427 1606 1438 85 733 266 N ATOM 428 CA TRP A 54 9.760 -0.797 2.068 1.00 13.54 C ANISOU 428 CA TRP A 54 2253 1550 1340 98 585 251 C ATOM 429 C TRP A 54 11.269 -0.980 2.049 1.00 13.49 C ANISOU 429 C TRP A 54 2310 1497 1319 235 606 224 C ATOM 430 O TRP A 54 11.919 -1.169 3.084 1.00 15.77 O ANISOU 430 O TRP A 54 2332 2350 1309 153 534 228 O ATOM 431 CB ATRP A 54 9.199 0.580 2.326 0.39 15.00 C ANISOU 431 CB ATRP A 54 2312 1675 1713 293 999 465 C ATOM 432 CB BTRP A 54 9.566 0.639 2.557 0.61 17.12 C ANISOU 432 CB BTRP A 54 2794 1537 2175 403 1131 270 C ATOM 433 CG ATRP A 54 9.550 1.539 1.227 0.39 11.77 C ANISOU 433 CG ATRP A 54 2190 1190 1093 -110 665 -139 C ATOM 434 CG BTRP A 54 10.544 1.723 2.162 0.61 16.03 C ANISOU 434 CG BTRP A 54 2898 1574 1618 18 403 -74 C ATOM 435 CD1ATRP A 54 8.927 1.775 0.043 0.39 13.25 C ANISOU 435 CD1ATRP A 54 2573 957 1504 -300 216 -12 C ATOM 436 CD1BTRP A 54 11.729 2.202 2.679 0.61 17.52 C ANISOU 436 CD1BTRP A 54 2536 1968 2155 464 253 -69 C ATOM 437 CD2ATRP A 54 10.686 2.418 1.266 0.39 12.75 C ANISOU 437 CD2ATRP A 54 1843 1548 1455 -12 583 -34 C ATOM 438 CD2BTRP A 54 10.321 2.527 1.002 0.61 14.16 C ANISOU 438 CD2BTRP A 54 2554 1379 1446 -129 504 -194 C ATOM 439 NE1ATRP A 54 9.601 2.759 -0.672 0.39 13.78 N ANISOU 439 NE1ATRP A 54 2811 984 1441 -215 333 107 N ATOM 440 NE1BTRP A 54 12.241 3.243 1.914 0.61 17.11 N ANISOU 440 NE1BTRP A 54 2251 2248 2004 49 491 -396 N ATOM 441 CE2ATRP A 54 10.680 3.162 0.068 0.39 13.71 C ANISOU 441 CE2ATRP A 54 2650 1242 1317 -448 762 -260 C ATOM 442 CE2BTRP A 54 11.376 3.445 0.890 0.61 14.88 C ANISOU 442 CE2BTRP A 54 2401 1552 1702 -69 648 -320 C ATOM 443 CE3ATRP A 54 11.693 2.638 2.209 0.39 15.16 C ANISOU 443 CE3ATRP A 54 1819 2168 1773 29 526 -301 C ATOM 444 CE3BTRP A 54 9.281 2.545 0.045 0.61 15.40 C ANISOU 444 CE3BTRP A 54 2453 1686 1714 -22 428 -100 C ATOM 445 CZ2ATRP A 54 11.675 4.113 -0.182 0.39 16.97 C ANISOU 445 CZ2ATRP A 54 2788 1705 1955 -646 895 -135 C ATOM 446 CZ2BTRP A 54 11.454 4.385 -0.142 0.61 15.34 C ANISOU 446 CZ2BTRP A 54 2454 1398 1977 -77 974 -253 C ATOM 447 CZ3ATRP A 54 12.673 3.583 1.957 0.39 16.29 C ANISOU 447 CZ3ATRP A 54 1909 1978 2304 -42 563 -682 C ATOM 448 CZ3BTRP A 54 9.354 3.465 -0.971 0.61 17.34 C ANISOU 448 CZ3BTRP A 54 3024 1516 2047 -39 60 62 C ATOM 449 CH2ATRP A 54 12.636 4.292 0.771 0.39 17.60 C ANISOU 449 CH2ATRP A 54 2398 1772 2518 -427 826 -544 C ATOM 450 CH2BTRP A 54 10.430 4.362 -1.047 0.61 17.53 C ANISOU 450 CH2BTRP A 54 3452 1564 1644 -289 515 -176 C ATOM 451 N ASP A 55 11.819 -0.841 0.849 1.00 13.44 N ANISOU 451 N ASP A 55 2060 1791 1254 -68 532 153 N ATOM 452 CA ASP A 55 13.256 -0.867 0.578 1.00 15.26 C ANISOU 452 CA ASP A 55 1996 2119 1682 104 405 346 C ATOM 453 C ASP A 55 13.549 0.239 -0.427 1.00 13.87 C ANISOU 453 C ASP A 55 1750 2025 1497 -35 526 160 C ATOM 454 O ASP A 55 12.981 0.247 -1.523 1.00 14.89 O ANISOU 454 O ASP A 55 2011 2024 1621 -221 203 250 O ATOM 455 CB ASP A 55 13.654 -2.233 0.044 1.00 20.98 C ANISOU 455 CB ASP A 55 3074 2161 2737 758 1007 706 C ATOM 456 CG ASP A 55 15.066 -2.279 -0.494 1.00 25.55 C ANISOU 456 CG ASP A 55 3145 3286 3275 971 1120 36 C ATOM 457 OD1 ASP A 55 15.956 -2.007 0.322 1.00 43.51 O ANISOU 457 OD1 ASP A 55 3066 8405 5060 1798 -138 -330 O ATOM 458 OD2 ASP A 55 15.251 -2.541 -1.713 1.00 36.85 O ANISOU 458 OD2 ASP A 55 4905 5824 3274 990 2020 356 O ATOM 459 N ARG A 56 14.440 1.159 -0.084 1.00 14.14 N ANISOU 459 N ARG A 56 2032 2087 1256 -27 441 -103 N ATOM 460 CA ARG A 56 14.697 2.266 -0.982 1.00 14.93 C ANISOU 460 CA ARG A 56 2449 1770 1454 -175 624 -230 C ATOM 461 C ARG A 56 15.294 1.775 -2.304 1.00 13.42 C ANISOU 461 C ARG A 56 1819 1930 1351 8 442 -23 C ATOM 462 O ARG A 56 14.955 2.317 -3.357 1.00 14.36 O ANISOU 462 O ARG A 56 2376 1676 1405 -56 406 92 O ATOM 463 CB ARG A 56 15.683 3.252 -0.345 1.00 17.50 C ANISOU 463 CB ARG A 56 2877 2284 1489 -438 491 -226 C ATOM 464 CG ARG A 56 16.061 4.398 -1.238 1.00 21.11 C ANISOU 464 CG ARG A 56 3774 2111 2136 -939 757 -368 C ATOM 465 CD ARG A 56 16.580 5.615 -0.529 1.00 20.67 C ANISOU 465 CD ARG A 56 3690 2089 2074 -339 83 -541 C ATOM 466 NE ARG A 56 15.438 6.272 0.107 1.00 24.97 N ANISOU 466 NE ARG A 56 4371 2843 2272 195 359 -620 N ATOM 467 CZ ARG A 56 14.559 7.022 -0.560 1.00 28.34 C ANISOU 467 CZ ARG A 56 4149 3563 3056 559 1067 266 C ATOM 468 NH1 ARG A 56 14.686 7.244 -1.878 1.00 25.81 N ANISOU 468 NH1 ARG A 56 3749 3097 2959 -10 413 181 N ATOM 469 NH2 ARG A 56 13.564 7.541 0.166 1.00 29.55 N ANISOU 469 NH2 ARG A 56 3878 3084 4267 -164 1494 -406 N ATOM 470 N ALA A 57 16.169 0.764 -2.267 1.00 14.34 N ANISOU 470 N ALA A 57 1708 2250 1491 117 486 123 N ATOM 471 CA ALA A 57 16.829 0.357 -3.483 1.00 15.62 C ANISOU 471 CA ALA A 57 1626 2432 1876 182 623 -74 C ATOM 472 C ALA A 57 15.875 -0.006 -4.588 1.00 14.25 C ANISOU 472 C ALA A 57 2234 1606 1573 27 673 -117 C ATOM 473 O ALA A 57 16.068 0.345 -5.753 1.00 17.31 O ANISOU 473 O ALA A 57 2839 2141 1599 2 862 -4 O ATOM 474 CB ALA A 57 17.741 -0.833 -3.175 1.00 19.48 C ANISOU 474 CB ALA A 57 2302 2816 2282 634 654 45 C ATOM 475 N THR A 58 14.832 -0.750 -4.209 1.00 14.39 N ANISOU 475 N THR A 58 2270 1650 1548 -38 631 -275 N ATOM 476 CA THR A 58 13.928 -1.322 -5.139 1.00 15.54 C ANISOU 476 CA THR A 58 2620 1768 1517 -146 489 -304 C ATOM 477 C THR A 58 12.607 -0.586 -5.194 1.00 15.45 C ANISOU 477 C THR A 58 2417 1889 1565 -297 388 -11 C ATOM 478 O THR A 58 11.631 -1.059 -5.802 1.00 19.91 O ANISOU 478 O THR A 58 2766 2722 2077 -701 74 -383 O ATOM 479 CB THR A 58 13.667 -2.821 -4.888 1.00 18.34 C ANISOU 479 CB THR A 58 3232 1719 2019 -209 329 -272 C ATOM 480 OG1 THR A 58 13.171 -2.963 -3.563 1.00 21.69 O ANISOU 480 OG1 THR A 58 3956 1947 2339 -573 723 66 O ATOM 481 CG2 THR A 58 14.964 -3.603 -4.974 1.00 24.76 C ANISOU 481 CG2 THR A 58 4316 2492 2600 948 319 -288 C ATOM 482 N ASN A 59 12.569 0.595 -4.627 1.00 14.44 N ANISOU 482 N ASN A 59 2214 1854 1416 -44 179 28 N ATOM 483 CA ASN A 59 11.275 1.233 -4.565 1.00 16.92 C ANISOU 483 CA ASN A 59 2388 2600 1443 284 82 -216 C ATOM 484 C ASN A 59 10.718 1.576 -5.926 1.00 17.09 C ANISOU 484 C ASN A 59 2240 2791 1462 121 240 175 C ATOM 485 O ASN A 59 11.404 1.905 -6.891 1.00 18.28 O ANISOU 485 O ASN A 59 2766 2611 1568 -196 492 25 O ATOM 486 CB AASN A 59 11.101 2.292 -3.513 0.57 14.94 C ANISOU 486 CB AASN A 59 2305 1978 1394 -151 616 143 C ATOM 487 CB BASN A 59 11.708 2.643 -4.035 0.43 14.48 C ANISOU 487 CB BASN A 59 1965 2353 1185 397 591 98 C ATOM 488 CG AASN A 59 11.412 3.596 -4.225 0.57 16.06 C ANISOU 488 CG AASN A 59 2193 2397 1511 -905 -221 576 C ATOM 489 CG BASN A 59 10.790 3.805 -4.066 0.43 16.08 C ANISOU 489 CG BASN A 59 1750 2232 2128 162 335 586 C ATOM 490 OD1AASN A 59 10.456 4.166 -4.747 0.57 17.46 O ANISOU 490 OD1AASN A 59 2229 2463 1942 -474 -77 542 O ATOM 491 OD1BASN A 59 9.691 3.710 -3.551 0.43 15.05 O ANISOU 491 OD1BASN A 59 1923 1849 1946 461 585 753 O ATOM 492 ND2AASN A 59 12.676 3.885 -4.246 0.57 14.95 N ANISOU 492 ND2AASN A 59 1936 2070 1676 14 554 116 N ATOM 493 ND2BASN A 59 11.116 4.969 -4.613 0.43 20.66 N ANISOU 493 ND2BASN A 59 2076 2668 3106 461 1208 1167 N ATOM 494 N LYS A 60 9.401 1.467 -5.948 1.00 17.50 N ANISOU 494 N LYS A 60 2270 2858 1522 30 101 176 N ATOM 495 CA LYS A 60 8.600 1.639 -7.121 1.00 19.60 C ANISOU 495 CA LYS A 60 2551 3300 1597 49 -101 142 C ATOM 496 C LYS A 60 7.686 2.844 -6.998 1.00 20.61 C ANISOU 496 C LYS A 60 2937 3375 1520 318 -57 518 C ATOM 497 O LYS A 60 6.887 3.109 -7.903 1.00 29.87 O ANISOU 497 O LYS A 60 4752 3862 2736 1055 -1548 -98 O ATOM 498 CB LYS A 60 7.749 0.382 -7.337 1.00 23.51 C ANISOU 498 CB LYS A 60 2923 3596 2412 -171 -298 -308 C ATOM 499 CG LYS A 60 8.555 -0.832 -7.766 1.00 25.72 C ANISOU 499 CG LYS A 60 3022 3736 3014 -677 654 -926 C ATOM 500 CD LYS A 60 7.706 -1.935 -8.340 1.00 35.36 C ANISOU 500 CD LYS A 60 4293 5289 3855 -1064 303 -2539 C ATOM 501 CE LYS A 60 8.510 -2.739 -9.378 1.00 43.09 C ANISOU 501 CE LYS A 60 5422 6470 4479 -1924 1636 -3172 C ATOM 502 NZ LYS A 60 8.098 -2.381 -10.799 1.00 48.78 N ANISOU 502 NZ LYS A 60 6422 7571 4540 38 1486 -3564 N ATOM 503 N CYS A 61 7.775 3.596 -5.923 1.00 21.14 N ANISOU 503 N CYS A 61 2794 3539 1698 675 -178 361 N ATOM 504 CA CYS A 61 6.906 4.697 -5.648 1.00 23.01 C ANISOU 504 CA CYS A 61 3319 3364 2060 733 -95 449 C ATOM 505 C CYS A 61 7.307 5.853 -6.552 1.00 29.56 C ANISOU 505 C CYS A 61 5583 3563 2087 587 173 690 C ATOM 506 O ACYS A 61 8.298 6.485 -6.218 1.00 40.29 O ANISOU 506 O ACYS A 61 3559 4519 7232 530 1081 1823 O ATOM 507 O BCYS A 61 6.419 6.576 -7.005 1.00 49.88 O ANISOU 507 O BCYS A 61 10785 4665 3501 2931 -1973 822 O ATOM 508 CB CYS A 61 7.008 5.099 -4.181 1.00 19.54 C ANISOU 508 CB CYS A 61 3112 2263 2051 265 33 638 C ATOM 509 SG CYS A 61 5.813 6.347 -3.694 1.00 23.54 S ANISOU 509 SG CYS A 61 3739 2468 2737 473 431 586 S TER 510 CYS A 61 END