CRYST1 51.415 80.863 89.869 90.00 96.94 90.00 I 1 2 1 4 ATOM 1 N SER A 1 -33.148 -19.064 15.292 1.00 22.25 A N ANISOU 1 N SER A 1 1949 3720 2783 196 928 760 A N ATOM 2 CA SER A 1 -32.395 -20.191 14.762 1.00 20.63 A C ANISOU 2 CA SER A 1 1769 3482 2588 114 831 801 A C ATOM 3 C SER A 1 -32.378 -20.228 13.236 1.00 20.02 A C ANISOU 3 C SER A 1 1647 3345 2616 71 727 802 A C ATOM 4 O SER A 1 -32.890 -19.325 12.568 1.00 20.02 A O ANISOU 4 O SER A 1 1597 3332 2676 109 722 776 A O ATOM 5 CB SER A 1 -32.959 -21.488 15.325 1.00 25.59 A C ANISOU 5 CB SER A 1 2363 4130 3231 52 843 905 A C ATOM 6 OG SER A 1 -34.176 -21.825 14.696 1.00 26.42 A O ANISOU 6 OG SER A 1 2359 4225 3456 13 824 972 A O ATOM 7 N GLY A 2 -31.761 -21.267 12.687 1.00 20.28 A N ANISOU 7 N GLY A 2 1702 3336 2668 -8 644 831 A N ATOM 8 CA GLY A 2 -31.489 -21.339 11.269 1.00 19.95 A C ANISOU 8 CA GLY A 2 1644 3238 2697 -56 542 812 A C ATOM 9 C GLY A 2 -30.029 -21.049 10.977 1.00 18.72 A C ANISOU 9 C GLY A 2 1574 3057 2481 -43 505 744 A C ATOM 10 O GLY A 2 -29.329 -20.387 11.742 1.00 19.89 A O ANISOU 10 O GLY A 2 1785 3236 2536 22 557 692 A O ATOM 11 N PHE A 3 -29.560 -21.567 9.841 1.00 18.36 A N ANISOU 11 N PHE A 3 1535 2957 2486 -110 412 738 A N ATOM 12 CA PHE A 3 -28.177 -21.361 9.427 1.00 20.10 A C ANISOU 12 CA PHE A 3 1847 3132 2656 -100 358 663 A C ATOM 13 C PHE A 3 -28.105 -21.256 7.915 1.00 20.87 A C ANISOU 13 C PHE A 3 1937 3175 2816 -143 260 623 A C ATOM 14 O PHE A 3 -28.462 -22.200 7.208 1.00 23.73 A O ANISOU 14 O PHE A 3 2273 3503 3240 -230 204 658 A O ATOM 15 CB PHE A 3 -27.262 -22.475 9.928 1.00 21.09 A C ANISOU 15 CB PHE A 3 2050 3222 2740 -133 342 682 A C ATOM 16 CG PHE A 3 -25.821 -22.058 9.983 1.00 16.61 A C ANISOU 16 CG PHE A 3 1587 2628 2097 -90 308 599 A C ATOM 17 CD1 PHE A 3 -25.364 -21.253 11.010 1.00 19.92 A C ANISOU 17 CD1 PHE A 3 2048 3105 2416 -22 359 563 A C ATOM 18 CD2 PHE A 3 -24.931 -22.444 8.992 1.00 20.04 A C ANISOU 18 CD2 PHE A 3 2074 2984 2558 -121 226 554 A C ATOM 19 CE1 PHE A 3 -24.047 -20.839 11.055 1.00 21.21 A C ANISOU 19 CE1 PHE A 3 2294 3250 2516 5 318 491 A C ATOM 20 CE2 PHE A 3 -23.610 -22.042 9.036 1.00 19.99 A C ANISOU 20 CE2 PHE A 3 2144 2959 2490 -82 197 490 A C ATOM 21 CZ PHE A 3 -23.166 -21.238 10.071 1.00 19.61 A C ANISOU 21 CZ PHE A 3 2127 2972 2351 -23 237 462 A C ATOM 22 N ARG A 4 -27.623 -20.118 7.429 1.00 18.67 A N ANISOU 22 N ARG A 4 1689 2887 2517 -87 239 549 A N ATOM 23 CA ARG A 4 -27.585 -19.820 6.009 1.00 17.38 A C ANISOU 23 CA ARG A 4 1517 2690 2397 -117 153 519 A C ATOM 24 C ARG A 4 -26.198 -19.332 5.641 1.00 14.54 A C ANISOU 24 C ARG A 4 1259 2284 1983 -87 116 432 A C ATOM 25 O ARG A 4 -25.506 -18.726 6.457 1.00 16.63 A O ANISOU 25 O ARG A 4 1575 2554 2188 -26 159 390 A O ATOM 26 CB ARG A 4 -28.609 -18.751 5.635 1.00 19.57 A C ANISOU 26 CB ARG A 4 1697 3011 2728 -76 169 547 A C ATOM 27 CG ARG A 4 -30.010 -19.275 5.587 1.00 17.26 A C ANISOU 27 CG ARG A 4 1302 2754 2503 -121 172 631 A C ATOM 28 CD ARG A 4 -30.248 -19.858 4.205 1.00 23.57 A C ANISOU 28 CD ARG A 4 2094 3526 3337 -215 58 634 A C ATOM 29 NE ARG A 4 -31.672 -20.002 3.903 1.00 25.60 A N ANISOU 29 NE ARG A 4 2270 3808 3648 -244 39 694 A N ATOM 30 CZ ARG A 4 -32.136 -20.669 2.850 1.00 25.19 A C ANISOU 30 CZ ARG A 4 2208 3745 3618 -336 -53 703 A C ATOM 31 NH1 ARG A 4 -33.438 -20.779 2.645 1.00 22.28 A N ANISOU 31 NH1 ARG A 4 1758 3411 3298 -363 -69 764 A N ATOM 32 NH2 ARG A 4 -31.280 -21.194 1.982 1.00 28.94 A N ANISOU 32 NH2 ARG A 4 2756 4178 4063 -401 -127 646 A N ATOM 33 N LYS A 5 -25.804 -19.593 4.400 1.00 17.08 A N ANISOU 33 N LYS A 5 1606 2564 2319 -135 36 404 A N ATOM 34 CA LYS A 5 -24.622 -18.940 3.865 1.00 15.99 A C ANISOU 34 CA LYS A 5 1541 2392 2141 -104 4 333 A C ATOM 35 C LYS A 5 -24.953 -17.460 3.715 1.00 16.23 A C ANISOU 35 C LYS A 5 1536 2445 2186 -40 22 324 A C ATOM 36 O LYS A 5 -25.841 -17.079 2.945 1.00 18.98 A O ANISOU 36 O LYS A 5 1814 2815 2584 -50 -5 363 A O ATOM 37 CB LYS A 5 -24.182 -19.587 2.554 1.00 20.72 A C ANISOU 37 CB LYS A 5 2178 2950 2746 -169 -71 307 A C ATOM 38 CG LYS A 5 -22.685 -19.519 2.341 1.00 21.64 A C ANISOU 38 CG LYS A 5 2383 3023 2816 -146 -83 244 A C ATOM 39 CD LYS A 5 -22.169 -20.608 1.409 1.00 22.73 A C ANISOU 39 CD LYS A 5 2573 3110 2954 -206 -126 217 A C ATOM 40 CE LYS A 5 -21.743 -21.846 2.173 1.00 23.35 A C ANISOU 40 CE LYS A 5 2688 3145 3040 -219 -98 230 A C ATOM 41 NZ LYS A 5 -20.888 -22.759 1.356 1.00 30.04 A N ANISOU 41 NZ LYS A 5 3604 3922 3889 -249 -120 186 A N ATOM 42 N MET A 6 -24.299 -16.642 4.521 1.00 11.50 A N ANISOU 42 N MET A 6 981 1839 1547 24 69 279 A N ATOM 43 CA MET A 6 -24.697 -15.265 4.749 1.00 14.36 A C ANISOU 43 CA MET A 6 1317 2207 1931 94 115 267 A C ATOM 44 C MET A 6 -23.568 -14.339 4.344 1.00 13.55 A C ANISOU 44 C MET A 6 1280 2058 1809 118 89 202 A C ATOM 45 O MET A 6 -22.452 -14.473 4.849 1.00 15.78 A O ANISOU 45 O MET A 6 1635 2326 2035 115 86 151 A O ATOM 46 CB MET A 6 -24.997 -15.020 6.222 1.00 14.86 A C ANISOU 46 CB MET A 6 1383 2301 1961 145 208 256 A C ATOM 47 CG MET A 6 -25.711 -13.745 6.435 1.00 19.70 A C ANISOU 47 CG MET A 6 1956 2913 2617 220 273 250 A C ATOM 48 SD MET A 6 -26.376 -13.706 8.092 1.00 24.67 A S ANISOU 48 SD MET A 6 2577 3596 3202 273 399 248 A S ATOM 49 CE MET A 6 -27.604 -15.013 8.042 1.00 21.72 A C ANISOU 49 CE MET A 6 2093 3285 2874 220 404 366 A C ATOM 50 N ALA A 7 -23.859 -13.395 3.468 1.00 13.16 A N ANISOU 50 N ALA A 7 1200 1990 1811 141 70 215 A N ATOM 51 CA ALA A 7 -22.855 -12.414 3.089 1.00 10.64 A C ANISOU 51 CA ALA A 7 936 1621 1486 162 54 166 A C ATOM 52 C ALA A 7 -23.026 -11.157 3.926 1.00 13.21 A C ANISOU 52 C ALA A 7 1272 1916 1833 234 127 128 A C ATOM 53 O ALA A 7 -24.045 -10.960 4.591 1.00 12.49 A O ANISOU 53 O ALA A 7 1133 1845 1769 278 194 148 A O ATOM 54 CB ALA A 7 -22.940 -12.071 1.605 1.00 13.07 A C ANISOU 54 CB ALA A 7 1216 1919 1831 143 -9 207 A C ATOM 55 N PHE A 8 -21.999 -10.311 3.908 1.00 10.04 A N ANISOU 55 N PHE A 8 934 1461 1421 242 120 69 A N ATOM 56 CA PHE A 8 -22.134 -9.016 4.553 1.00 10.50 A C ANISOU 56 CA PHE A 8 1012 1465 1511 304 187 21 A C ATOM 57 C PHE A 8 -23.019 -8.110 3.711 1.00 10.54 A C ANISOU 57 C PHE A 8 952 1434 1619 353 199 84 A C ATOM 58 O PHE A 8 -23.058 -8.239 2.490 1.00 10.49 A O ANISOU 58 O PHE A 8 908 1437 1642 327 133 150 A O ATOM 59 CB PHE A 8 -20.767 -8.361 4.733 1.00 9.94 A C ANISOU 59 CB PHE A 8 1026 1341 1411 283 166 -58 A C ATOM 60 CG PHE A 8 -19.960 -8.992 5.842 1.00 12.72 A C ANISOU 60 CG PHE A 8 1438 1733 1664 249 164 -120 A C ATOM 61 CD1 PHE A 8 -20.244 -8.727 7.166 1.00 18.09 A C ANISOU 61 CD1 PHE A 8 2152 2427 2294 278 232 -180 A C ATOM 62 CD2 PHE A 8 -18.977 -9.911 5.549 1.00 15.51 A C ANISOU 62 CD2 PHE A 8 1807 2117 1969 194 98 -109 A C ATOM 63 CE1 PHE A 8 -19.518 -9.334 8.183 1.00 23.45 A C ANISOU 63 CE1 PHE A 8 2882 3160 2868 243 221 -222 A C ATOM 64 CE2 PHE A 8 -18.239 -10.525 6.569 1.00 18.03 A C ANISOU 64 CE2 PHE A 8 2168 2480 2201 168 90 -145 A C ATOM 65 CZ PHE A 8 -18.515 -10.233 7.881 1.00 18.90 A C ANISOU 65 CZ PHE A 8 2312 2615 2255 189 144 -196 A C ATOM 66 N PRO A 9 -23.752 -7.198 4.348 1.00 11.05 A N ANISOU 66 N PRO A 9 1001 1460 1738 429 286 68 A N ATOM 67 CA PRO A 9 -24.456 -6.162 3.586 1.00 11.82 A C ANISOU 67 CA PRO A 9 1038 1504 1951 490 303 134 A C ATOM 68 C PRO A 9 -23.478 -5.475 2.645 1.00 14.13 A C ANISOU 68 C PRO A 9 1373 1730 2267 463 242 134 A C ATOM 69 O PRO A 9 -22.339 -5.167 3.020 1.00 12.36 A O ANISOU 69 O PRO A 9 1237 1459 2002 432 236 48 A O ATOM 70 CB PRO A 9 -24.969 -5.208 4.672 1.00 15.03 A C ANISOU 70 CB PRO A 9 1461 1849 2398 578 424 74 A C ATOM 71 CG PRO A 9 -24.943 -6.004 5.941 1.00 13.21 A C ANISOU 71 CG PRO A 9 1271 1685 2065 561 470 6 A C ATOM 72 CD PRO A 9 -23.770 -6.942 5.797 1.00 12.37 A C ANISOU 72 CD PRO A 9 1222 1620 1858 464 376 -21 A C ATOM 73 N SER A 10 -23.910 -5.266 1.401 1.00 11.45 A N ANISOU 73 N SER A 10 965 1397 1988 468 191 240 A N ATOM 74 CA SER A 10 -22.975 -4.894 0.341 1.00 11.42 A C ANISOU 74 CA SER A 10 993 1361 1984 425 123 263 A C ATOM 75 C SER A 10 -22.956 -3.406 0.061 1.00 12.31 A C ANISOU 75 C SER A 10 1111 1363 2205 484 159 288 A C ATOM 76 O SER A 10 -22.151 -2.962 -0.765 1.00 11.74 A O ANISOU 76 O SER A 10 1066 1254 2141 451 114 314 A O ATOM 77 CB SER A 10 -23.296 -5.649 -0.955 1.00 10.71 A C ANISOU 77 CB SER A 10 841 1358 1868 377 34 364 A C ATOM 78 OG SER A 10 -24.642 -5.480 -1.337 1.00 12.94 A O ANISOU 78 OG SER A 10 1019 1676 2222 422 36 468 A O ATOM 79 N GLY A 11 -23.812 -2.635 0.730 1.00 13.21 A N ANISOU 79 N GLY A 11 1199 1416 2406 573 248 284 A N ATOM 80 CA GLY A 11 -23.987 -1.232 0.372 1.00 14.08 A C ANISOU 80 CA GLY A 11 1303 1407 2639 639 287 326 A C ATOM 81 C GLY A 11 -22.689 -0.446 0.334 1.00 14.72 A C ANISOU 81 C GLY A 11 1481 1380 2733 602 281 259 A C ATOM 82 O GLY A 11 -22.480 0.380 -0.563 1.00 17.29 A O ANISOU 82 O GLY A 11 1796 1639 3136 610 259 338 A O ATOM 83 N LYS A 12 -21.819 -0.664 1.329 1.00 13.57 A N ANISOU 83 N LYS A 12 1427 1220 2507 555 297 119 A N ATOM 84 CA LYS A 12 -20.593 0.121 1.416 1.00 14.01 A C ANISOU 84 CA LYS A 12 1571 1175 2578 507 289 46 A C ATOM 85 C LYS A 12 -19.682 -0.152 0.239 1.00 15.53 A C ANISOU 85 C LYS A 12 1754 1406 2740 432 196 119 A C ATOM 86 O LYS A 12 -18.926 0.734 -0.180 1.00 18.36 A O ANISOU 86 O LYS A 12 2145 1672 3158 407 187 128 A O ATOM 87 CB LYS A 12 -19.852 -0.175 2.717 1.00 17.91 A C ANISOU 87 CB LYS A 12 2154 1675 2975 459 306 -109 A C ATOM 88 CG LYS A 12 -20.604 0.192 3.984 1.00 21.30 A C ANISOU 88 CG LYS A 12 2618 2063 3412 527 411 -204 A C ATOM 89 CD LYS A 12 -19.685 0.076 5.193 1.00 25.32 A C ANISOU 89 CD LYS A 12 3230 2578 3814 462 413 -358 A C ATOM 90 CE LYS A 12 -20.127 0.987 6.321 1.00 28.92 A C ANISOU 90 CE LYS A 12 3757 2934 4296 519 524 -480 A C ATOM 91 NZ LYS A 12 -21.471 0.584 6.821 1.00 37.19 A N ANISOU 91 NZ LYS A 12 4752 4042 5338 612 613 -456 A N ATOM 92 N VAL A 13 -19.723 -1.366 -0.296 1.00 13.91 A N ANISOU 92 N VAL A 13 1508 1334 2445 393 133 167 A N ATOM 93 CA VAL A 13 -18.885 -1.677 -1.450 1.00 13.13 A C ANISOU 93 CA VAL A 13 1403 1280 2306 327 59 231 A C ATOM 94 C VAL A 13 -19.572 -1.249 -2.741 1.00 12.29 A C ANISOU 94 C VAL A 13 1227 1181 2260 359 34 378 A C ATOM 95 O VAL A 13 -18.908 -0.832 -3.686 1.00 12.33 A O ANISOU 95 O VAL A 13 1238 1171 2277 326 1 441 A O ATOM 96 CB VAL A 13 -18.563 -3.177 -1.454 1.00 10.11 A C ANISOU 96 CB VAL A 13 1021 1023 1799 271 10 205 A C ATOM 97 CG1 VAL A 13 -17.672 -3.546 -2.655 1.00 13.04 A C ANISOU 97 CG1 VAL A 13 1391 1442 2120 210 -50 258 A C ATOM 98 CG2 VAL A 13 -17.916 -3.569 -0.140 1.00 10.45 A C ANISOU 98 CG2 VAL A 13 1123 1065 1783 246 31 80 A C ATOM 99 N GLU A 14 -20.913 -1.343 -2.802 1.00 12.25 A N ANISOU 99 N GLU A 14 1150 1211 2295 421 48 445 A N ATOM 100 CA GLU A 14 -21.632 -0.917 -3.997 1.00 12.97 A C ANISOU 100 CA GLU A 14 1163 1322 2441 453 13 600 A C ATOM 101 C GLU A 14 -21.263 0.504 -4.370 1.00 13.92 A C ANISOU 101 C GLU A 14 1310 1321 2660 474 42 642 A C ATOM 102 O GLU A 14 -21.120 0.822 -5.555 1.00 15.30 A O ANISOU 102 O GLU A 14 1464 1527 2821 443 -2 744 A O ATOM 103 CB GLU A 14 -23.144 -1.010 -3.777 1.00 13.66 A C ANISOU 103 CB GLU A 14 1181 1459 2551 501 38 638 A C ATOM 104 CG GLU A 14 -23.662 -2.430 -3.570 1.00 12.93 A C ANISOU 104 CG GLU A 14 1051 1492 2370 467 3 620 A C ATOM 105 CD GLU A 14 -25.120 -2.431 -3.139 1.00 14.08 A C ANISOU 105 CD GLU A 14 1132 1667 2551 512 43 647 A C ATOM 106 OE1 GLU A 14 -25.963 -1.714 -3.727 1.00 16.56 A O ANISOU 106 OE1 GLU A 14 1397 1976 2920 539 45 737 A O ATOM 107 OE2 GLU A 14 -25.402 -3.104 -2.147 1.00 13.98 A O ANISOU 107 OE2 GLU A 14 1115 1680 2517 523 81 582 A O ATOM 108 N GLY A 15 -21.102 1.376 -3.369 1.00 14.52 A N ANISOU 108 N GLY A 15 1436 1261 2821 516 121 555 A N ATOM 109 CA GLY A 15 -20.809 2.765 -3.663 1.00 15.65 A C ANISOU 109 CA GLY A 15 1608 1279 3058 526 152 584 A C ATOM 110 C GLY A 15 -19.417 3.008 -4.187 1.00 15.85 A C ANISOU 110 C GLY A 15 1682 1259 3081 455 116 591 A C ATOM 111 O GLY A 15 -19.083 4.138 -4.562 1.00 16.27 A O ANISOU 111 O GLY A 15 1755 1217 3210 449 135 628 A O ATOM 112 N CYS A 16 -18.589 1.974 -4.207 1.00 14.04 A N ANISOU 112 N CYS A 16 1475 1117 2745 386 67 544 A N ATOM 113 CA CYS A 16 -17.236 2.083 -4.717 1.00 13.73 A C ANISOU 113 CA CYS A 16 1474 1071 2672 302 34 544 A C ATOM 114 C CYS A 16 -17.073 1.542 -6.122 1.00 13.38 A C ANISOU 114 C CYS A 16 1386 1148 2549 266 -29 668 A C ATOM 115 O CYS A 16 -15.975 1.653 -6.688 1.00 13.27 A O ANISOU 115 O CYS A 16 1394 1139 2508 203 -47 689 A O ATOM 116 CB CYS A 16 -16.249 1.347 -3.796 1.00 12.79 A C ANISOU 116 CB CYS A 16 1412 986 2461 234 25 395 A C ATOM 117 SG CYS A 16 -16.271 1.957 -2.100 1.00 15.97 A S ANISOU 117 SG CYS A 16 1885 1265 2918 254 91 230 A S ATOM 118 N MET A 17 -18.095 0.931 -6.690 1.00 13.30 A N ANISOU 118 N MET A 17 1318 1244 2493 297 -63 746 A N ATOM 119 CA MET A 17 -17.841 0.155 -7.876 1.00 12.99 A C ANISOU 119 CA MET A 17 1259 1340 2335 244 -125 818 A C ATOM 120 C MET A 17 -18.013 1.061 -9.086 1.00 14.65 A C ANISOU 120 C MET A 17 1439 1553 2574 245 -135 955 A C ATOM 121 O MET A 17 -18.970 1.834 -9.145 1.00 16.46 A O ANISOU 121 O MET A 17 1630 1747 2876 294 -113 1003 A O ATOM 122 CB MET A 17 -18.772 -1.032 -8.009 1.00 14.73 A C ANISOU 122 CB MET A 17 1440 1693 2464 244 -168 817 A C ATOM 123 CG MET A 17 -18.606 -2.028 -6.857 1.00 12.10 A C ANISOU 123 CG MET A 17 1142 1378 2076 227 -150 667 A C ATOM 124 SD MET A 17 -16.942 -2.630 -6.680 1.00 11.03 A S ANISOU 124 SD MET A 17 1080 1256 1857 151 -149 564 A S ATOM 125 CE MET A 17 -16.710 -3.570 -8.183 1.00 19.36 A C ANISOU 125 CE MET A 17 2127 2448 2780 95 -205 631 A C ATOM 126 N VAL A 18 -17.068 0.987 -10.031 1.00 15.78 A N ANISOU 126 N VAL A 18 1600 1747 2650 187 -158 1005 A N ATOM 127 CA VAL A 18 -17.079 1.784 -11.255 1.00 17.84 A C ANISOU 127 CA VAL A 18 1836 2032 2909 174 -163 1121 A C ATOM 128 C VAL A 18 -16.740 0.890 -12.445 1.00 15.60 A C ANISOU 128 C VAL A 18 1556 1907 2465 115 -209 1158 A C ATOM 129 O VAL A 18 -16.293 -0.240 -12.296 1.00 15.06 A O ANISOU 129 O VAL A 18 1516 1907 2298 80 -227 1091 A O ATOM 130 CB VAL A 18 -16.094 2.975 -11.206 1.00 15.73 A C ANISOU 130 CB VAL A 18 1595 1636 2745 161 -119 1143 A C ATOM 131 CG1 VAL A 18 -16.307 3.814 -9.958 1.00 17.14 A C ANISOU 131 CG1 VAL A 18 1794 1646 3072 208 -68 1070 A C ATOM 132 CG2 VAL A 18 -14.663 2.479 -11.261 1.00 16.30 A C ANISOU 132 CG2 VAL A 18 1708 1725 2759 93 -119 1108 A C ATOM 133 N GLN A 19 -16.933 1.435 -13.638 1.00 21.97 A N ANISOU 133 N GLN A 19 2336 2767 3246 104 -222 1263 A N ATOM 134 CA GLN A 19 -16.666 0.728 -14.879 1.00 20.21 A C ANISOU 134 CA GLN A 19 2121 2690 2866 49 -258 1296 A C ATOM 135 C GLN A 19 -15.367 1.272 -15.465 1.00 18.35 A C ANISOU 135 C GLN A 19 1910 2438 2624 16 -224 1341 A C ATOM 136 O GLN A 19 -15.175 2.490 -15.545 1.00 19.65 A O ANISOU 136 O GLN A 19 2058 2510 2899 34 -195 1411 A O ATOM 137 CB GLN A 19 -17.837 0.903 -15.844 1.00 20.64 A C ANISOU 137 CB GLN A 19 2127 2832 2885 56 -300 1384 A C ATOM 138 CG GLN A 19 -17.689 0.259 -17.203 1.00 23.79 A C ANISOU 138 CG GLN A 19 2540 3381 3119 -2 -339 1415 A C ATOM 139 CD GLN A 19 -18.996 0.300 -17.981 1.00 28.54 A C ANISOU 139 CD GLN A 19 3088 4067 3688 -2 -393 1490 A C ATOM 140 NE2 GLN A 19 -19.811 1.314 -17.714 1.00 28.94 A N ANISOU 140 NE2 GLN A 19 3077 4047 3871 52 -385 1571 A N ATOM 141 OE1 GLN A 19 -19.279 -0.580 -18.798 1.00 33.67 A O ANISOU 141 OE1 GLN A 19 3752 4843 4198 -52 -440 1474 A O ATOM 142 N VAL A 20 -14.455 0.379 -15.821 1.00 17.39 A N ANISOU 142 N VAL A 20 1828 2397 2381 -32 -219 1296 A N ATOM 143 CA VAL A 20 -13.192 0.775 -16.428 1.00 19.22 A C ANISOU 143 CA VAL A 20 2076 2632 2594 -67 -179 1337 A C ATOM 144 C VAL A 20 -13.129 0.156 -17.812 1.00 17.16 A C ANISOU 144 C VAL A 20 1830 2526 2164 -102 -194 1367 A C ATOM 145 O VAL A 20 -13.241 -1.065 -17.955 1.00 21.29 A O ANISOU 145 O VAL A 20 2386 3142 2561 -124 -212 1289 A O ATOM 146 CB VAL A 20 -11.981 0.353 -15.581 1.00 17.47 A C ANISOU 146 CB VAL A 20 1885 2360 2392 -93 -138 1257 A C ATOM 147 CG1 VAL A 20 -10.688 0.747 -16.299 1.00 16.58 A C ANISOU 147 CG1 VAL A 20 1774 2264 2260 -133 -90 1306 A C ATOM 148 CG2 VAL A 20 -12.026 0.994 -14.212 1.00 17.82 A C ANISOU 148 CG2 VAL A 20 1925 2245 2601 -68 -126 1216 A C ATOM 149 N THR A 21 -12.957 0.993 -18.830 1.00 23.10 A N ANISOU 149 N THR A 21 2565 3302 2912 -109 -185 1475 A N ATOM 150 CA THR A 21 -12.842 0.531 -20.205 1.00 22.47 A C ANISOU 150 CA THR A 21 2505 3364 2668 -143 -194 1508 A C ATOM 151 C THR A 21 -11.533 1.035 -20.780 1.00 24.81 A C ANISOU 151 C THR A 21 2810 3660 2956 -166 -132 1560 A C ATOM 152 O THR A 21 -11.181 2.207 -20.605 1.00 25.31 A O ANISOU 152 O THR A 21 2841 3624 3150 -155 -108 1637 A O ATOM 153 CB THR A 21 -14.009 1.004 -21.077 1.00 24.29 A C ANISOU 153 CB THR A 21 2699 3653 2877 -132 -249 1606 A C ATOM 154 CG2 THR A 21 -13.883 0.433 -22.486 1.00 23.40 A C ANISOU 154 CG2 THR A 21 2619 3693 2577 -174 -262 1626 A C ATOM 155 OG1 THR A 21 -15.246 0.569 -20.500 1.00 24.18 A O ANISOU 155 OG1 THR A 21 2663 3638 2887 -112 -301 1562 A O ATOM 156 N CYS A 22 -10.814 0.147 -21.452 1.00 23.46 A N ANISOU 156 N CYS A 22 2684 3594 2637 -198 -102 1513 A N ATOM 157 CA CYS A 22 -9.589 0.528 -22.134 1.00 25.78 A C ANISOU 157 CA CYS A 22 2983 3909 2905 -220 -35 1565 A C ATOM 158 C CYS A 22 -9.488 -0.326 -23.384 1.00 29.12 A C ANISOU 158 C CYS A 22 3457 4483 3126 -244 -24 1546 A C ATOM 159 O CYS A 22 -9.518 -1.558 -23.292 1.00 25.65 A O ANISOU 159 O CYS A 22 3065 4100 2581 -253 -22 1431 A O ATOM 160 CB CYS A 22 -8.369 0.338 -21.235 1.00 25.79 A C ANISOU 160 CB CYS A 22 2983 3840 2977 -229 28 1500 A C ATOM 161 SG CYS A 22 -6.855 0.790 -22.078 1.00 35.31 A S ANISOU 161 SG CYS A 22 4178 5077 4161 -258 115 1567 A S ATOM 162 N GLY A 23 -9.382 0.323 -24.536 1.00 28.04 A N ANISOU 162 N GLY A 23 3314 4405 2936 -256 -15 1656 A N ATOM 163 CA GLY A 23 -9.487 -0.402 -25.792 1.00 27.85 A C ANISOU 163 CA GLY A 23 3346 4525 2711 -280 -15 1643 A C ATOM 164 C GLY A 23 -10.872 -1.013 -25.890 1.00 31.30 A C ANISOU 164 C GLY A 23 3797 5016 3080 -284 -105 1600 A C ATOM 165 O GLY A 23 -11.889 -0.324 -25.757 1.00 34.91 A O ANISOU 165 O GLY A 23 4201 5444 3620 -268 -172 1677 A O ATOM 166 N THR A 24 -10.932 -2.327 -26.097 1.00 31.25 A N ANISOU 166 N THR A 24 3859 5083 2932 -305 -105 1474 A N ATOM 167 CA THR A 24 -12.202 -3.035 -26.198 1.00 32.64 A C ANISOU 167 CA THR A 24 4051 5311 3040 -321 -192 1419 A C ATOM 168 C THR A 24 -12.504 -3.859 -24.959 1.00 32.44 A C ANISOU 168 C THR A 24 4029 5218 3078 -311 -208 1295 A C ATOM 169 O THR A 24 -13.448 -4.655 -24.970 1.00 36.13 A O ANISOU 169 O THR A 24 4516 5724 3487 -332 -271 1226 A O ATOM 170 CB THR A 24 -12.211 -3.959 -27.411 1.00 34.51 A C ANISOU 170 CB THR A 24 4372 5676 3064 -362 -191 1361 A C ATOM 171 CG2 THR A 24 -12.136 -3.146 -28.693 1.00 34.26 A C ANISOU 171 CG2 THR A 24 4335 5728 2953 -375 -191 1495 A C ATOM 172 OG1 THR A 24 -11.083 -4.837 -27.332 1.00 35.81 A O ANISOU 172 OG1 THR A 24 4606 5839 3161 -361 -98 1247 A O ATOM 173 N THR A 25 -11.718 -3.710 -23.904 1.00 28.12 A N ANISOU 173 N THR A 25 3464 4575 2646 -285 -155 1266 A N ATOM 174 CA THR A 25 -11.921 -4.457 -22.675 1.00 29.31 A C ANISOU 174 CA THR A 25 3618 4663 2856 -274 -166 1158 A C ATOM 175 C THR A 25 -12.701 -3.591 -21.700 1.00 27.45 A C ANISOU 175 C THR A 25 3310 4332 2789 -242 -214 1217 A C ATOM 176 O THR A 25 -12.313 -2.454 -21.423 1.00 25.76 A O ANISOU 176 O THR A 25 3051 4040 2695 -219 -189 1305 A O ATOM 177 CB THR A 25 -10.589 -4.876 -22.057 1.00 30.75 A C ANISOU 177 CB THR A 25 3821 4803 3058 -265 -78 1089 A C ATOM 178 CG2 THR A 25 -10.830 -5.549 -20.714 1.00 27.09 A C ANISOU 178 CG2 THR A 25 3354 4274 2664 -251 -95 994 A C ATOM 179 OG1 THR A 25 -9.935 -5.806 -22.927 1.00 34.46 A O ANISOU 179 OG1 THR A 25 4363 5357 3374 -284 -21 1018 A O ATOM 180 N THR A 26 -13.810 -4.117 -21.200 1.00 23.05 A N ANISOU 180 N THR A 26 2742 3771 2244 -241 -276 1166 A N ATOM 181 CA THR A 26 -14.544 -3.469 -20.127 1.00 23.14 A C ANISOU 181 CA THR A 26 2692 3685 2414 -203 -305 1198 A C ATOM 182 C THR A 26 -14.553 -4.395 -18.918 1.00 20.94 A C ANISOU 182 C THR A 26 2433 3361 2163 -196 -303 1079 A C ATOM 183 O THR A 26 -14.782 -5.601 -19.048 1.00 20.36 A O ANISOU 183 O THR A 26 2402 3346 1987 -226 -321 983 A O ATOM 184 CB THR A 26 -15.963 -3.095 -20.564 1.00 23.80 A C ANISOU 184 CB THR A 26 2727 3804 2513 -200 -376 1269 A C ATOM 185 CG2 THR A 26 -16.789 -2.638 -19.382 1.00 26.10 A C ANISOU 185 CG2 THR A 26 2961 3997 2960 -153 -392 1277 A C ATOM 186 OG1 THR A 26 -15.891 -2.027 -21.511 1.00 27.39 A O ANISOU 186 OG1 THR A 26 3153 4281 2973 -195 -374 1400 A O ATOM 187 N LEU A 27 -14.247 -3.830 -17.761 1.00 19.72 A N ANISOU 187 N LEU A 27 2252 3097 2145 -160 -278 1084 A N ATOM 188 CA LEU A 27 -14.273 -4.532 -16.488 1.00 20.03 A C ANISOU 188 CA LEU A 27 2300 3084 2226 -147 -278 989 A C ATOM 189 C LEU A 27 -14.577 -3.538 -15.371 1.00 19.17 A C ANISOU 189 C LEU A 27 2147 2850 2289 -99 -275 1026 A C ATOM 190 O LEU A 27 -14.867 -2.359 -15.616 1.00 18.06 A O ANISOU 190 O LEU A 27 1968 2659 2236 -75 -272 1118 A O ATOM 191 CB LEU A 27 -12.983 -5.349 -16.306 1.00 19.85 A C ANISOU 191 CB LEU A 27 2327 3079 2135 -169 -225 914 A C ATOM 192 CG LEU A 27 -11.657 -4.564 -16.341 1.00 18.20 A C ANISOU 192 CG LEU A 27 2110 2825 1979 -169 -158 969 A C ATOM 193 CD1 LEU A 27 -11.263 -3.886 -15.070 1.00 19.84 A C ANISOU 193 CD1 LEU A 27 2289 2900 2348 -146 -138 952 A C ATOM 194 CD2 LEU A 27 -10.621 -5.653 -16.626 1.00 20.36 A C ANISOU 194 CD2 LEU A 27 2429 3166 2140 -192 -102 889 A C ATOM 195 N ASN A 28 -14.557 -4.036 -14.146 1.00 18.09 A N ANISOU 195 N ASN A 28 2015 2659 2198 -82 -274 949 A N ATOM 196 CA ASN A 28 -14.934 -3.248 -12.986 1.00 16.94 A C ANISOU 196 CA ASN A 28 1839 2389 2207 -33 -263 944 A C ATOM 197 C ASN A 28 -13.711 -2.661 -12.318 1.00 12.46 A C ANISOU 197 C ASN A 28 1291 1719 1726 -38 -206 899 A C ATOM 198 O ASN A 28 -12.623 -3.237 -12.361 1.00 14.03 A O ANISOU 198 O ASN A 28 1516 1946 1867 -72 -177 837 A O ATOM 199 CB ASN A 28 -15.700 -4.105 -11.979 1.00 15.82 A C ANISOU 199 CB ASN A 28 1695 2243 2073 -16 -279 837 A C ATOM 200 CG ASN A 28 -16.888 -4.758 -12.606 1.00 15.85 A C ANISOU 200 CG ASN A 28 1676 2347 2000 -29 -336 864 A C ATOM 201 ND2 ASN A 28 -16.783 -6.057 -12.906 1.00 15.25 A N ANISOU 201 ND2 ASN A 28 1637 2354 1803 -76 -356 790 A N ATOM 202 OD1 ASN A 28 -17.904 -4.098 -12.833 1.00 14.19 A O ANISOU 202 OD1 ASN A 28 1419 2127 1846 -4 -350 927 A O ATOM 203 N GLY A 29 -13.896 -1.498 -11.693 1.00 13.24 A N ANISOU 203 N GLY A 29 1370 1694 1967 -4 -189 930 A N ATOM 204 CA GLY A 29 -12.867 -0.930 -10.856 1.00 12.52 A C ANISOU 204 CA GLY A 29 1298 1494 1966 -19 -147 867 A C ATOM 205 C GLY A 29 -13.422 -0.624 -9.474 1.00 12.97 A C ANISOU 205 C GLY A 29 1360 1446 2121 19 -136 777 A C ATOM 206 O GLY A 29 -14.626 -0.481 -9.285 1.00 12.03 A O ANISOU 206 O GLY A 29 1218 1314 2037 71 -147 801 A O ATOM 207 N LEU A 30 -12.517 -0.522 -8.517 1.00 14.10 A N ANISOU 207 N LEU A 30 1530 1523 2303 -8 -112 676 A N ATOM 208 CA LEU A 30 -12.868 -0.174 -7.144 1.00 14.13 A C ANISOU 208 CA LEU A 30 1555 1430 2383 18 -95 576 A C ATOM 209 C LEU A 30 -12.363 1.237 -6.867 1.00 12.57 A C ANISOU 209 C LEU A 30 1373 1084 2317 3 -67 589 A C ATOM 210 O LEU A 30 -11.158 1.493 -6.946 1.00 13.83 A O ANISOU 210 O LEU A 30 1540 1224 2491 -60 -65 582 A O ATOM 211 CB LEU A 30 -12.284 -1.201 -6.167 1.00 12.40 A C ANISOU 211 CB LEU A 30 1360 1259 2094 -9 -101 445 A C ATOM 212 CG LEU A 30 -12.597 -0.954 -4.700 1.00 10.49 A C ANISOU 212 CG LEU A 30 1148 941 1897 10 -84 333 A C ATOM 213 CD1 LEU A 30 -14.007 -1.469 -4.431 1.00 13.15 A C ANISOU 213 CD1 LEU A 30 1470 1315 2211 73 -80 329 A C ATOM 214 CD2 LEU A 30 -11.636 -1.699 -3.785 1.00 9.89 A C ANISOU 214 CD2 LEU A 30 1093 903 1760 -35 -96 228 A C ATOM 215 N TRP A 31 -13.288 2.154 -6.555 1.00 13.17 A N ANISOU 215 N TRP A 31 1451 1052 2501 61 -42 610 A N ATOM 216 CA TRP A 31 -12.990 3.584 -6.443 1.00 14.38 A C ANISOU 216 CA TRP A 31 1624 1040 2801 55 -8 637 A C ATOM 217 C TRP A 31 -12.968 3.943 -4.958 1.00 16.37 A C ANISOU 217 C TRP A 31 1930 1181 3106 56 22 479 A C ATOM 218 O TRP A 31 -14.012 3.940 -4.299 1.00 14.70 A O ANISOU 218 O TRP A 31 1727 943 2916 126 50 432 A O ATOM 219 CB TRP A 31 -14.029 4.400 -7.206 1.00 15.41 A C ANISOU 219 CB TRP A 31 1718 1118 3018 127 7 779 A C ATOM 220 CG TRP A 31 -13.870 5.910 -7.204 1.00 16.89 A C ANISOU 220 CG TRP A 31 1925 1168 3325 127 48 792 A C ATOM 221 CD1 TRP A 31 -12.717 6.619 -7.023 1.00 17.45 A C ANISOU 221 CD1 TRP A 31 2032 1147 3452 54 59 756 A C ATOM 222 CD2 TRP A 31 -14.906 6.880 -7.426 1.00 20.64 A C ANISOU 222 CD2 TRP A 31 2380 1585 3879 201 81 851 A C ATOM 223 CE2 TRP A 31 -14.305 8.155 -7.364 1.00 20.83 A C ANISOU 223 CE2 TRP A 31 2438 1471 4007 172 113 847 A C ATOM 224 CE3 TRP A 31 -16.282 6.791 -7.663 1.00 20.41 A C ANISOU 224 CE3 TRP A 31 2300 1609 3845 283 85 909 A C ATOM 225 NE1 TRP A 31 -12.969 7.967 -7.118 1.00 18.99 A N ANISOU 225 NE1 TRP A 31 2239 1223 3754 78 96 786 A N ATOM 226 CZ2 TRP A 31 -15.035 9.332 -7.528 1.00 22.25 A C ANISOU 226 CZ2 TRP A 31 2610 1555 4290 231 153 901 A C ATOM 227 CZ3 TRP A 31 -17.004 7.947 -7.822 1.00 22.66 A C ANISOU 227 CZ3 TRP A 31 2569 1809 4233 340 124 966 A C ATOM 228 CH2 TRP A 31 -16.383 9.208 -7.749 1.00 22.71 A C ANISOU 228 CH2 TRP A 31 2615 1667 4346 319 161 962 A C ATOM 229 N LEU A 32 -11.780 4.232 -4.431 1.00 14.76 A N ANISOU 229 N LEU A 32 1762 926 2919 -27 16 399 A N ATOM 230 CA LEU A 32 -11.604 4.600 -3.034 1.00 15.16 A C ANISOU 230 CA LEU A 32 1876 883 3001 -48 34 239 A C ATOM 231 C LEU A 32 -10.771 5.861 -3.009 1.00 19.50 A C ANISOU 231 C LEU A 32 2457 1274 3677 -117 45 236 A C ATOM 232 O LEU A 32 -9.692 5.890 -3.608 1.00 17.69 A O ANISOU 232 O LEU A 32 2200 1073 3447 -196 15 294 A O ATOM 233 CB LEU A 32 -10.909 3.490 -2.236 1.00 15.06 A C ANISOU 233 CB LEU A 32 1874 991 2857 -101 -6 128 A C ATOM 234 CG LEU A 32 -11.551 2.113 -2.220 1.00 12.97 A C ANISOU 234 CG LEU A 32 1581 880 2467 -52 -21 127 A C ATOM 235 CD1 LEU A 32 -10.577 1.062 -1.732 1.00 12.64 A C ANISOU 235 CD1 LEU A 32 1537 951 2317 -112 -63 60 A C ATOM 236 CD2 LEU A 32 -12.773 2.150 -1.329 1.00 15.07 A C ANISOU 236 CD2 LEU A 32 1874 1112 2740 24 21 57 A C ATOM 237 N ASP A 33 -11.275 6.897 -2.340 1.00 18.30 A N ANISOU 237 N ASP A 33 2362 981 3608 -85 92 165 A N ATOM 238 CA ASP A 33 -10.676 8.228 -2.392 1.00 21.54 A C ANISOU 238 CA ASP A 33 2810 1273 4101 -137 106 163 A C ATOM 239 C ASP A 33 -10.504 8.567 -3.875 1.00 23.51 A C ANISOU 239 C ASP A 33 2995 1551 4388 -133 100 349 A C ATOM 240 O ASP A 33 -11.443 8.363 -4.657 1.00 21.21 A O ANISOU 240 O ASP A 33 2656 1312 4090 -48 112 463 A O ATOM 241 CB ASP A 33 -9.418 8.230 -1.540 1.00 24.02 A C ANISOU 241 CB ASP A 33 3166 1577 4382 -259 66 37 A C ATOM 242 CG ASP A 33 -9.719 7.932 -0.076 1.00 25.85 A C ANISOU 242 CG ASP A 33 3469 1802 4552 -256 72 -145 A C ATOM 243 OD1 ASP A 33 -10.671 8.529 0.465 1.00 28.56 A O ANISOU 243 OD1 ASP A 33 3867 2061 4925 -181 130 -203 A O ATOM 244 OD2 ASP A 33 -9.039 7.076 0.521 1.00 25.84 A O ANISOU 244 OD2 ASP A 33 3463 1892 4463 -322 21 -224 A O ATOM 245 N ASP A 34 -9.340 9.044 -4.321 1.00 20.66 A N ANISOU 245 N ASP A 34 2624 1174 4051 -225 80 390 A N ATOM 246 CA ASP A 34 -9.204 9.411 -5.725 1.00 20.83 A C ANISOU 246 CA ASP A 34 2588 1230 4095 -217 83 565 A C ATOM 247 C ASP A 34 -8.445 8.366 -6.541 1.00 20.35 A C ANISOU 247 C ASP A 34 2464 1329 3940 -261 46 646 A C ATOM 248 O ASP A 34 -7.777 8.715 -7.519 1.00 22.06 A O ANISOU 248 O ASP A 34 2642 1577 4161 -298 47 757 A O ATOM 249 CB ASP A 34 -8.531 10.779 -5.857 1.00 22.20 A C ANISOU 249 CB ASP A 34 2789 1276 4369 -276 100 583 A C ATOM 250 CG ASP A 34 -7.114 10.794 -5.319 1.00 28.71 A C ANISOU 250 CG ASP A 34 3630 2095 5184 -404 67 500 A C ATOM 251 OD1 ASP A 34 -6.745 9.884 -4.541 1.00 25.59 A O ANISOU 251 OD1 ASP A 34 3239 1769 4713 -442 34 395 A O ATOM 252 OD2 ASP A 34 -6.371 11.741 -5.665 1.00 28.02 A O ANISOU 252 OD2 ASP A 34 3544 1935 5165 -468 73 545 A O ATOM 253 N VAL A 35 -8.554 7.087 -6.190 1.00 17.85 A N ANISOU 253 N VAL A 35 2134 1114 3533 -254 21 597 A N ATOM 254 CA VAL A 35 -7.881 6.029 -6.932 1.00 16.81 A C ANISOU 254 CA VAL A 35 1949 1134 3304 -289 -5 667 A C ATOM 255 C VAL A 35 -8.912 4.992 -7.359 1.00 17.12 A C ANISOU 255 C VAL A 35 1970 1284 3253 -210 -13 713 A C ATOM 256 O VAL A 35 -9.807 4.630 -6.583 1.00 16.90 A O ANISOU 256 O VAL A 35 1967 1254 3200 -152 -13 623 A O ATOM 257 CB VAL A 35 -6.757 5.379 -6.099 1.00 16.24 A C ANISOU 257 CB VAL A 35 1873 1100 3197 -376 -37 560 A C ATOM 258 CG1 VAL A 35 -6.171 4.178 -6.823 1.00 17.12 A C ANISOU 258 CG1 VAL A 35 1930 1395 3181 -384 -49 612 A C ATOM 259 CG2 VAL A 35 -5.667 6.397 -5.794 1.00 20.28 A C ANISOU 259 CG2 VAL A 35 2394 1532 3778 -464 -40 525 A C ATOM 260 N VAL A 36 -8.783 4.513 -8.592 1.00 15.51 A N ANISOU 260 N VAL A 36 1724 1203 2967 -206 -17 836 A N ATOM 261 CA VAL A 36 -9.571 3.391 -9.090 1.00 14.58 A C ANISOU 261 CA VAL A 36 1592 1235 2714 -150 -35 854 A C ATOM 262 C VAL A 36 -8.626 2.223 -9.287 1.00 15.71 A C ANISOU 262 C VAL A 36 1721 1519 2730 -193 -44 812 A C ATOM 263 O VAL A 36 -7.607 2.343 -9.983 1.00 15.07 A O ANISOU 263 O VAL A 36 1613 1472 2640 -245 -28 880 A O ATOM 264 CB VAL A 36 -10.311 3.733 -10.392 1.00 15.25 A C ANISOU 264 CB VAL A 36 1649 1364 2782 -107 -36 1014 A C ATOM 265 CG1 VAL A 36 -10.983 2.483 -10.943 1.00 17.37 A C ANISOU 265 CG1 VAL A 36 1905 1794 2900 -76 -66 1028 A C ATOM 266 CG2 VAL A 36 -11.355 4.819 -10.127 1.00 17.20 A C ANISOU 266 CG2 VAL A 36 1899 1498 3138 -43 -22 1026 A C ATOM 267 N TYR A 37 -8.948 1.103 -8.653 1.00 12.64 A N ANISOU 267 N TYR A 37 1346 1205 2254 -169 -63 704 A N ATOM 268 CA TYR A 37 -8.119 -0.091 -8.686 1.00 15.36 A C ANISOU 268 CA TYR A 37 1679 1665 2491 -195 -65 653 A C ATOM 269 C TYR A 37 -8.784 -1.091 -9.617 1.00 11.43 A C ANISOU 269 C TYR A 37 1181 1292 1868 -159 -71 691 A C ATOM 270 O TYR A 37 -10.000 -1.290 -9.552 1.00 12.71 A O ANISOU 270 O TYR A 37 1354 1463 2013 -113 -92 688 A O ATOM 271 CB TYR A 37 -7.996 -0.718 -7.292 1.00 11.63 A C ANISOU 271 CB TYR A 37 1225 1186 2007 -197 -83 510 A C ATOM 272 CG TYR A 37 -7.377 0.164 -6.250 1.00 13.07 A C ANISOU 272 CG TYR A 37 1419 1259 2289 -244 -90 446 A C ATOM 273 CD1 TYR A 37 -8.123 1.147 -5.615 1.00 12.57 A C ANISOU 273 CD1 TYR A 37 1391 1069 2316 -225 -85 413 A C ATOM 274 CD2 TYR A 37 -6.021 0.041 -5.910 1.00 14.82 A C ANISOU 274 CD2 TYR A 37 1614 1501 2517 -311 -99 417 A C ATOM 275 CE1 TYR A 37 -7.550 1.960 -4.648 1.00 15.03 A C ANISOU 275 CE1 TYR A 37 1727 1273 2709 -280 -91 335 A C ATOM 276 CE2 TYR A 37 -5.453 0.850 -4.952 1.00 12.47 A C ANISOU 276 CE2 TYR A 37 1327 1109 2302 -372 -119 352 A C ATOM 277 CZ TYR A 37 -6.220 1.804 -4.320 1.00 17.06 A C ANISOU 277 CZ TYR A 37 1961 1561 2961 -360 -115 303 A C ATOM 278 OH TYR A 37 -5.657 2.630 -3.370 1.00 19.21 A O ANISOU 278 OH TYR A 37 2259 1731 3308 -431 -134 221 A O ATOM 279 N CYS A 38 -7.998 -1.741 -10.465 1.00 11.41 A N ANISOU 279 N CYS A 38 1167 1389 1780 -182 -51 723 A N ATOM 280 CA CYS A 38 -8.591 -2.717 -11.367 1.00 11.61 A C ANISOU 280 CA CYS A 38 1207 1530 1675 -159 -56 741 A C ATOM 281 C CYS A 38 -7.502 -3.673 -11.825 1.00 13.84 A C ANISOU 281 C CYS A 38 1487 1902 1870 -179 -17 714 A C ATOM 282 O CYS A 38 -6.314 -3.378 -11.669 1.00 13.75 A O ANISOU 282 O CYS A 38 1445 1871 1907 -209 14 723 A O ATOM 283 CB CYS A 38 -9.266 -2.040 -12.572 1.00 12.07 A C ANISOU 283 CB CYS A 38 1259 1615 1711 -152 -65 877 A C ATOM 284 SG CYS A 38 -8.141 -1.311 -13.792 1.00 18.24 A S ANISOU 284 SG CYS A 38 2018 2429 2484 -195 -16 1013 A S ATOM 285 N PRO A 39 -7.879 -4.830 -12.379 1.00 11.07 A N ANISOU 285 N PRO A 39 1164 1644 1396 -163 -16 680 A N ATOM 286 CA PRO A 39 -6.871 -5.788 -12.855 1.00 13.73 A C ANISOU 286 CA PRO A 39 1507 2058 1654 -169 37 648 A C ATOM 287 C PRO A 39 -6.036 -5.182 -13.974 1.00 14.79 A C ANISOU 287 C PRO A 39 1620 2237 1764 -194 90 753 A C ATOM 288 O PRO A 39 -6.556 -4.500 -14.858 1.00 14.69 A O ANISOU 288 O PRO A 39 1614 2249 1720 -203 79 852 A O ATOM 289 CB PRO A 39 -7.722 -6.963 -13.357 1.00 13.20 A C ANISOU 289 CB PRO A 39 1490 2063 1462 -154 22 595 A C ATOM 290 CG PRO A 39 -8.997 -6.852 -12.591 1.00 11.67 A C ANISOU 290 CG PRO A 39 1300 1821 1312 -140 -44 568 A C ATOM 291 CD PRO A 39 -9.236 -5.392 -12.431 1.00 12.21 A C ANISOU 291 CD PRO A 39 1336 1819 1482 -141 -63 654 A C ATOM 292 N ARG A 40 -4.722 -5.416 -13.930 1.00 13.85 A N ANISOU 292 N ARG A 40 1466 2134 1662 -203 149 744 A N ATOM 293 CA ARG A 40 -3.895 -4.796 -14.959 1.00 14.32 A C ANISOU 293 CA ARG A 40 1497 2240 1706 -228 210 855 A C ATOM 294 C ARG A 40 -4.098 -5.427 -16.334 1.00 15.88 A C ANISOU 294 C ARG A 40 1740 2555 1736 -218 254 880 A C ATOM 295 O ARG A 40 -3.723 -4.809 -17.336 1.00 17.31 A O ANISOU 295 O ARG A 40 1913 2781 1884 -235 292 976 A O ATOM 296 CB ARG A 40 -2.415 -4.848 -14.577 1.00 13.90 A C ANISOU 296 CB ARG A 40 1377 2181 1723 -243 266 852 A C ATOM 297 CG ARG A 40 -1.838 -6.242 -14.577 1.00 15.71 A C ANISOU 297 CG ARG A 40 1611 2475 1884 -203 320 767 A C ATOM 298 CD ARG A 40 -0.346 -6.222 -14.251 1.00 14.86 A C ANISOU 298 CD ARG A 40 1415 2373 1859 -213 376 791 A C ATOM 299 NE ARG A 40 0.200 -7.575 -14.266 1.00 16.31 A N ANISOU 299 NE ARG A 40 1598 2609 1990 -159 438 719 A N ATOM 300 CZ ARG A 40 1.497 -7.854 -14.157 1.00 20.77 A C ANISOU 300 CZ ARG A 40 2081 3204 2608 -147 505 742 A C ATOM 301 NH1 ARG A 40 2.381 -6.879 -13.986 1.00 18.16 A N ANISOU 301 NH1 ARG A 40 1669 2851 2379 -193 497 816 A N ATOM 302 NH2 ARG A 40 1.908 -9.108 -14.209 1.00 16.57 A N ANISOU 302 NH2 ARG A 40 1553 2708 2035 -85 569 680 A N ATOM 303 N HIS A 41 -4.678 -6.636 -16.414 1.00 17.59 A N ANISOU 303 N HIS A 41 2016 2817 1850 -193 245 779 A N ATOM 304 CA HIS A 41 -4.861 -7.207 -17.746 1.00 20.65 A C ANISOU 304 CA HIS A 41 2461 3320 2067 -196 284 789 A C ATOM 305 C HIS A 41 -5.906 -6.461 -18.565 1.00 20.57 A C ANISOU 305 C HIS A 41 2476 3335 2006 -216 219 868 A C ATOM 306 O HIS A 41 -6.113 -6.828 -19.720 1.00 21.23 A O ANISOU 306 O HIS A 41 2612 3495 1958 -222 230 855 A O ATOM 307 CB HIS A 41 -5.172 -8.722 -17.676 1.00 17.87 A C ANISOU 307 CB HIS A 41 2173 2992 1623 -173 293 647 A C ATOM 308 CG HIS A 41 -6.519 -9.094 -17.111 1.00 16.41 A C ANISOU 308 CG HIS A 41 2022 2772 1441 -176 196 586 A C ATOM 309 CD2 HIS A 41 -6.845 -9.856 -16.039 1.00 19.73 A C ANISOU 309 CD2 HIS A 41 2448 3127 1920 -157 165 485 A C ATOM 310 ND1 HIS A 41 -7.715 -8.763 -17.718 1.00 20.87 A N ANISOU 310 ND1 HIS A 41 2614 3382 1933 -203 123 635 A N ATOM 311 CE1 HIS A 41 -8.719 -9.266 -17.016 1.00 20.82 A C ANISOU 311 CE1 HIS A 41 2621 3336 1952 -201 53 567 A C ATOM 312 NE2 HIS A 41 -8.218 -9.931 -15.991 1.00 17.35 A N ANISOU 312 NE2 HIS A 41 2173 2828 1590 -174 80 475 A N ATOM 313 N VAL A 42 -6.519 -5.401 -18.018 1.00 19.04 A N ANISOU 313 N VAL A 42 2243 3065 1925 -221 153 941 A N ATOM 314 CA VAL A 42 -7.352 -4.510 -18.823 1.00 19.97 A C ANISOU 314 CA VAL A 42 2363 3193 2033 -227 100 1029 A C ATOM 315 C VAL A 42 -6.561 -3.840 -19.941 1.00 24.58 A C ANISOU 315 C VAL A 42 2936 3816 2588 -239 154 1113 A C ATOM 316 O VAL A 42 -7.149 -3.417 -20.942 1.00 27.95 A O ANISOU 316 O VAL A 42 3377 4292 2951 -245 124 1177 A O ATOM 317 CB VAL A 42 -8.021 -3.435 -17.941 1.00 20.51 A C ANISOU 317 CB VAL A 42 2387 3149 2256 -217 41 1088 A C ATOM 318 CG1 VAL A 42 -6.994 -2.421 -17.445 1.00 17.71 A C ANISOU 318 CG1 VAL A 42 1983 2700 2045 -229 82 1141 A C ATOM 319 CG2 VAL A 42 -9.162 -2.741 -18.699 1.00 22.16 A C ANISOU 319 CG2 VAL A 42 2592 3377 2453 -209 -20 1166 A C ATOM 320 N ILE A 43 -5.236 -3.718 -19.810 1.00 22.80 A N ANISOU 320 N ILE A 43 2678 3573 2410 -245 231 1120 A N ATOM 321 CA ILE A 43 -4.488 -3.019 -20.852 1.00 27.82 A C ANISOU 321 CA ILE A 43 3300 4245 3028 -258 283 1208 A C ATOM 322 C ILE A 43 -4.119 -3.944 -21.996 1.00 28.10 A C ANISOU 322 C ILE A 43 3392 4397 2889 -255 348 1164 A C ATOM 323 O ILE A 43 -3.515 -3.497 -22.980 1.00 33.90 A O ANISOU 323 O ILE A 43 4124 5178 3580 -266 400 1234 A O ATOM 324 CB ILE A 43 -3.250 -2.315 -20.266 1.00 31.35 A C ANISOU 324 CB ILE A 43 3676 4617 3619 -273 331 1247 A C ATOM 325 CG1 ILE A 43 -2.291 -3.310 -19.621 1.00 30.65 A C ANISOU 325 CG1 ILE A 43 3570 4539 3537 -264 391 1155 A C ATOM 326 CG2 ILE A 43 -3.692 -1.292 -19.233 1.00 30.09 A C ANISOU 326 CG2 ILE A 43 3478 4327 3626 -284 266 1283 A C ATOM 327 CD1 ILE A 43 -1.063 -2.638 -19.015 1.00 28.45 A C ANISOU 327 CD1 ILE A 43 3210 4194 3407 -287 423 1190 A C ATOM 328 N CYS A 44 -4.544 -5.194 -21.930 1.00 34.05 A N ANISOU 328 N CYS A 44 4204 5193 3540 -243 345 1050 A N ATOM 329 CA CYS A 44 -4.155 -6.253 -22.840 1.00 39.90 A C ANISOU 329 CA CYS A 44 5015 6020 4125 -237 417 972 A C ATOM 330 C CYS A 44 -5.188 -6.456 -23.937 1.00 46.05 A C ANISOU 330 C CYS A 44 5869 6876 4753 -255 364 970 A C ATOM 331 O CYS A 44 -6.395 -6.426 -23.685 1.00 46.78 A O ANISOU 331 O CYS A 44 5969 6958 4848 -265 264 965 A O ATOM 332 CB CYS A 44 -4.004 -7.551 -22.063 1.00 41.05 A C ANISOU 332 CB CYS A 44 5187 6150 4261 -213 446 836 A C ATOM 333 SG CYS A 44 -2.608 -7.522 -20.934 1.00 44.29 A S ANISOU 333 SG CYS A 44 5504 6495 4829 -188 521 834 A S ATOM 334 N THR A 45 -4.701 -6.687 -25.147 1.00 52.85 A N ANISOU 334 N THR A 45 6784 7815 5484 -261 434 971 A N ATOM 335 CA THR A 45 -5.523 -7.204 -26.227 1.00 57.30 A C ANISOU 335 CA THR A 45 7436 8460 5875 -281 398 935 A C ATOM 336 C THR A 45 -5.441 -8.731 -26.241 1.00 62.05 A C ANISOU 336 C THR A 45 8127 9073 6376 -269 446 770 A C ATOM 337 O THR A 45 -4.633 -9.340 -25.535 1.00 61.42 A O ANISOU 337 O THR A 45 8036 8946 6356 -240 523 697 A O ATOM 338 CB THR A 45 -5.074 -6.603 -27.559 1.00 59.22 A C ANISOU 338 CB THR A 45 7699 8782 6020 -296 449 1028 A C ATOM 339 CG2 THR A 45 -4.968 -5.086 -27.439 1.00 52.32 A C ANISOU 339 CG2 THR A 45 6729 7874 5275 -302 418 1192 A C ATOM 340 OG1 THR A 45 -3.794 -7.139 -27.922 1.00 61.37 A O ANISOU 340 OG1 THR A 45 8000 9073 6244 -278 589 979 A O ATOM 341 N SER A 46 -6.299 -9.357 -27.056 1.00 65.30 A N ANISOU 341 N SER A 46 8626 9544 6640 -292 398 711 A N ATOM 342 CA SER A 46 -6.360 -10.818 -27.095 1.00 67.32 A C ANISOU 342 CA SER A 46 8976 9795 6806 -282 433 547 A C ATOM 343 C SER A 46 -5.067 -11.453 -27.602 1.00 68.56 A C ANISOU 343 C SER A 46 9190 9961 6899 -246 593 484 A C ATOM 344 O SER A 46 -4.822 -12.635 -27.333 1.00 67.57 A O ANISOU 344 O SER A 46 9123 9797 6755 -215 652 350 A O ATOM 345 CB SER A 46 -7.542 -11.280 -27.947 1.00 66.47 A C ANISOU 345 CB SER A 46 8944 9753 6558 -323 339 502 A C ATOM 346 OG SER A 46 -8.760 -11.110 -27.244 1.00 68.58 A O ANISOU 346 OG SER A 46 9159 9993 6904 -350 204 516 A O ATOM 347 N GLU A 47 -4.233 -10.707 -28.322 1.00 66.59 A N ANISOU 347 N GLU A 47 8922 9756 6625 -245 672 579 A N ATOM 348 CA GLU A 47 -2.898 -11.177 -28.658 1.00 65.08 A C ANISOU 348 CA GLU A 47 8756 9562 6409 -210 838 536 A C ATOM 349 C GLU A 47 -1.824 -10.653 -27.713 1.00 65.13 A C ANISOU 349 C GLU A 47 8638 9512 6597 -190 898 595 A C ATOM 350 O GLU A 47 -0.745 -11.253 -27.647 1.00 64.28 A O ANISOU 350 O GLU A 47 8525 9386 6512 -158 1028 536 A O ATOM 351 CB GLU A 47 -2.533 -10.786 -30.089 1.00 67.41 A C ANISOU 351 CB GLU A 47 9106 9948 6557 -225 905 597 A C ATOM 352 CG GLU A 47 -2.325 -9.300 -30.267 1.00 68.20 A C ANISOU 352 CG GLU A 47 9107 10079 6727 -253 873 776 A C ATOM 353 CD GLU A 47 -3.580 -8.622 -30.775 1.00 69.49 A C ANISOU 353 CD GLU A 47 9278 10296 6827 -292 731 858 A C ATOM 354 OE1 GLU A 47 -4.532 -9.350 -31.146 1.00 69.14 A O ANISOU 354 OE1 GLU A 47 9319 10285 6664 -305 663 774 A O ATOM 355 OE2 GLU A 47 -3.612 -7.374 -30.814 1.00 67.69 A O ANISOU 355 OE2 GLU A 47 8968 10076 6678 -309 686 1008 A O ATOM 356 N ASP A 48 -2.086 -9.556 -26.988 1.00 64.67 A N ANISOU 356 N ASP A 48 8472 9424 6673 -206 806 707 A N ATOM 357 CA ASP A 48 -1.240 -9.196 -25.856 1.00 62.29 A C ANISOU 357 CA ASP A 48 8054 9057 6556 -185 833 742 A C ATOM 358 C ASP A 48 -1.252 -10.297 -24.822 1.00 62.90 A C ANISOU 358 C ASP A 48 8137 9075 6687 -151 842 617 A C ATOM 359 O ASP A 48 -0.275 -10.487 -24.093 1.00 59.09 A O ANISOU 359 O ASP A 48 7578 8553 6319 -119 906 605 A O ATOM 360 CB ASP A 48 -1.738 -7.917 -25.194 1.00 57.06 A C ANISOU 360 CB ASP A 48 7304 8354 6024 -208 722 863 A C ATOM 361 CG ASP A 48 -1.373 -6.702 -25.961 1.00 54.32 A C ANISOU 361 CG ASP A 48 6916 8038 5685 -232 733 1005 A C ATOM 362 OD1 ASP A 48 -0.252 -6.684 -26.541 1.00 55.33 A O ANISOU 362 OD1 ASP A 48 7028 8200 5793 -225 845 1027 A O ATOM 363 OD2 ASP A 48 -2.200 -5.762 -25.968 1.00 51.34 A O ANISOU 363 OD2 ASP A 48 6517 7648 5343 -254 634 1096 A O ATOM 364 N MET A 49 -2.379 -11.001 -24.707 1.00 65.27 A N ANISOU 364 N MET A 49 8516 9367 6916 -159 766 530 A N ATOM 365 CA MET A 49 -2.623 -11.876 -23.567 1.00 62.56 A C ANISOU 365 CA MET A 49 8168 8960 6643 -134 744 431 A C ATOM 366 C MET A 49 -1.972 -13.244 -23.732 1.00 61.47 A C ANISOU 366 C MET A 49 8096 8802 6457 -92 864 296 A C ATOM 367 O MET A 49 -2.494 -14.251 -23.254 1.00 61.72 A O ANISOU 367 O MET A 49 8181 8789 6480 -75 843 187 A O ATOM 368 CB MET A 49 -4.136 -11.875 -23.308 1.00 62.88 A C ANISOU 368 CB MET A 49 8243 8996 6654 -169 599 415 A C ATOM 369 CG MET A 49 -5.022 -12.428 -24.398 1.00 68.10 A C ANISOU 369 CG MET A 49 9015 9708 7150 -196 559 355 A C ATOM 370 SD MET A 49 -6.746 -12.316 -23.880 1.00 79.23 A S ANISOU 370 SD MET A 49 10417 11107 8580 -242 380 354 A S ATOM 371 CE MET A 49 -6.655 -13.644 -22.674 1.00 56.18 A C ANISOU 371 CE MET A 49 7514 8104 5726 -214 406 209 A C ATOM 372 N LEU A 50 -0.735 -13.247 -24.254 1.00 56.77 A N ANISOU 372 N LEU A 50 7477 8227 5865 -71 994 310 A N ATOM 373 CA LEU A 50 -0.041 -14.463 -24.692 1.00 56.99 A C ANISOU 373 CA LEU A 50 7569 8245 5839 -42 1129 185 A C ATOM 374 C LEU A 50 1.387 -14.567 -24.128 1.00 53.30 A C ANISOU 374 C LEU A 50 6966 7772 5515 4 1224 199 A C ATOM 375 O LEU A 50 1.905 -15.679 -23.983 1.00 52.12 A O ANISOU 375 O LEU A 50 6810 7609 5383 48 1300 89 A O ATOM 376 CB LEU A 50 -0.032 -14.485 -26.233 1.00 63.10 A C ANISOU 376 CB LEU A 50 8459 9082 6434 -63 1197 177 A C ATOM 377 CG LEU A 50 -1.454 -14.609 -26.833 1.00 61.28 A C ANISOU 377 CG LEU A 50 8350 8874 6058 -69 1082 159 A C ATOM 378 CD1 LEU A 50 -1.382 -14.510 -28.355 1.00 62.62 A C ANISOU 378 CD1 LEU A 50 8618 9128 6049 -76 1138 174 A C ATOM 379 CD2 LEU A 50 -2.209 -15.838 -26.343 1.00 56.25 A C ANISOU 379 CD2 LEU A 50 7776 8189 5406 -20 1031 30 A C ATOM 380 N ASN A 51 2.040 -13.428 -23.808 1.00 52.60 A N ANISOU 380 N ASN A 51 6755 7692 5537 7 1208 338 A N ATOM 381 CA ASN A 51 3.202 -13.414 -22.914 1.00 45.45 A C ANISOU 381 CA ASN A 51 5711 6752 4804 60 1248 376 A C ATOM 382 C ASN A 51 3.599 -11.967 -22.619 1.00 42.33 A C ANISOU 382 C ASN A 51 5207 6361 4514 29 1195 531 A C ATOM 383 O ASN A 51 4.646 -11.496 -23.078 1.00 44.81 A O ANISOU 383 O ASN A 51 5453 6709 4862 31 1266 601 A O ATOM 384 CB ASN A 51 4.376 -14.177 -23.518 1.00 49.58 A C ANISOU 384 CB ASN A 51 6215 7307 5317 109 1392 324 A C ATOM 385 CG ASN A 51 5.277 -14.803 -22.441 1.00 50.21 A C ANISOU 385 CG ASN A 51 6188 7326 5565 188 1419 310 A C ATOM 386 ND2 ASN A 51 5.852 -15.963 -22.751 1.00 47.54 A N ANISOU 386 ND2 ASN A 51 5866 6984 5212 253 1522 215 A N ATOM 387 OD1 ASN A 51 5.428 -14.261 -21.337 1.00 46.08 A O ANISOU 387 OD1 ASN A 51 5570 6756 5183 191 1343 385 A O ATOM 388 N PRO A 52 2.806 -11.248 -21.831 1.00 42.72 A N ANISOU 388 N PRO A 52 5235 6373 4624 -2 1073 583 A N ATOM 389 CA PRO A 52 2.874 -9.782 -21.842 1.00 37.80 A C ANISOU 389 CA PRO A 52 4545 5751 4065 -52 1013 720 A C ATOM 390 C PRO A 52 4.073 -9.262 -21.074 1.00 36.80 A C ANISOU 390 C PRO A 52 4282 5590 4110 -45 1026 789 A C ATOM 391 O PRO A 52 4.425 -9.785 -20.015 1.00 34.78 A O ANISOU 391 O PRO A 52 3969 5289 3956 -12 1013 748 A O ATOM 392 CB PRO A 52 1.604 -9.382 -21.098 1.00 38.04 A C ANISOU 392 CB PRO A 52 4598 5739 4117 -80 882 727 A C ATOM 393 CG PRO A 52 0.701 -10.521 -21.262 1.00 41.65 A C ANISOU 393 CG PRO A 52 5164 6208 4454 -63 875 608 A C ATOM 394 CD PRO A 52 1.539 -11.743 -21.272 1.00 39.79 A C ANISOU 394 CD PRO A 52 4935 5969 4214 -7 985 510 A C ATOM 395 N ASN A 53 4.670 -8.195 -21.591 1.00 33.37 A N ANISOU 395 N ASN A 53 3794 5177 3710 -81 1040 898 A N ATOM 396 CA ASN A 53 5.524 -7.345 -20.773 1.00 33.22 A C ANISOU 396 CA ASN A 53 3651 5111 3862 -105 1005 979 A C ATOM 397 C ASN A 53 4.647 -6.168 -20.355 1.00 30.42 A C ANISOU 397 C ASN A 53 3300 4701 3558 -164 888 1044 A C ATOM 398 O ASN A 53 4.487 -5.198 -21.104 1.00 27.12 A O ANISOU 398 O ASN A 53 2893 4296 3117 -203 880 1131 A O ATOM 399 CB ASN A 53 6.767 -6.897 -21.527 1.00 32.09 A C ANISOU 399 CB ASN A 53 3440 5014 3741 -113 1093 1058 A C ATOM 400 CG ASN A 53 7.747 -6.189 -20.623 1.00 33.24 A C ANISOU 400 CG ASN A 53 3455 5112 4063 -141 1055 1127 A C ATOM 401 ND2 ASN A 53 9.005 -6.602 -20.680 1.00 36.02 A N ANISOU 401 ND2 ASN A 53 3726 5496 4465 -109 1135 1137 A N ATOM 402 OD1 ASN A 53 7.379 -5.285 -19.871 1.00 32.00 A O ANISOU 402 OD1 ASN A 53 3273 4888 3998 -193 953 1166 A O ATOM 403 N TYR A 54 4.054 -6.270 -19.163 1.00 28.27 A N ANISOU 403 N TYR A 54 3021 4364 3357 -168 802 1000 A N ATOM 404 CA TYR A 54 3.077 -5.271 -18.740 1.00 25.33 A C ANISOU 404 CA TYR A 54 2665 3930 3029 -215 697 1044 A C ATOM 405 C TYR A 54 3.686 -3.888 -18.596 1.00 25.19 A C ANISOU 405 C TYR A 54 2575 3858 3137 -271 668 1144 A C ATOM 406 O TYR A 54 3.005 -2.883 -18.824 1.00 23.90 A O ANISOU 406 O TYR A 54 2437 3655 2990 -306 615 1207 A O ATOM 407 CB TYR A 54 2.424 -5.681 -17.424 1.00 22.49 A C ANISOU 407 CB TYR A 54 2307 3512 2726 -210 622 973 A C ATOM 408 CG TYR A 54 1.345 -6.692 -17.608 1.00 24.40 A C ANISOU 408 CG TYR A 54 2641 3789 2842 -173 618 893 A C ATOM 409 CD1 TYR A 54 0.068 -6.288 -17.970 1.00 22.83 A C ANISOU 409 CD1 TYR A 54 2511 3589 2575 -193 554 912 A C ATOM 410 CD2 TYR A 54 1.579 -8.049 -17.392 1.00 23.79 A C ANISOU 410 CD2 TYR A 54 2579 3739 2720 -119 671 797 A C ATOM 411 CE1 TYR A 54 -0.940 -7.192 -18.129 1.00 23.10 A C ANISOU 411 CE1 TYR A 54 2627 3658 2492 -170 535 837 A C ATOM 412 CE2 TYR A 54 0.568 -8.972 -17.552 1.00 21.06 A C ANISOU 412 CE2 TYR A 54 2325 3417 2259 -94 662 715 A C ATOM 413 CZ TYR A 54 -0.696 -8.528 -17.920 1.00 24.26 A C ANISOU 413 CZ TYR A 54 2797 3830 2590 -126 588 734 A C ATOM 414 OH TYR A 54 -1.722 -9.417 -18.092 1.00 22.54 A O ANISOU 414 OH TYR A 54 2667 3638 2257 -114 563 651 A O ATOM 415 N GLU A 55 4.950 -3.809 -18.203 1.00 28.08 A N ANISOU 415 N GLU A 55 2851 4218 3601 -281 698 1160 A N ATOM 416 CA GLU A 55 5.582 -2.504 -18.098 1.00 27.00 A C ANISOU 416 CA GLU A 55 2650 4029 3582 -344 670 1250 A C ATOM 417 C GLU A 55 5.677 -1.846 -19.468 1.00 27.13 A C ANISOU 417 C GLU A 55 2684 4090 3532 -355 726 1346 A C ATOM 418 O GLU A 55 5.385 -0.653 -19.610 1.00 25.22 A O ANISOU 418 O GLU A 55 2444 3791 3347 -402 682 1423 A O ATOM 419 CB GLU A 55 6.942 -2.663 -17.429 1.00 28.93 A C ANISOU 419 CB GLU A 55 2790 4273 3931 -354 685 1246 A C ATOM 420 CG GLU A 55 6.779 -3.006 -15.953 1.00 33.94 A C ANISOU 420 CG GLU A 55 3405 4849 4643 -362 602 1167 A C ATOM 421 CD GLU A 55 6.814 -4.508 -15.701 1.00 40.15 A C ANISOU 421 CD GLU A 55 4198 5688 5368 -286 641 1083 A C ATOM 422 OE1 GLU A 55 7.057 -4.921 -14.544 1.00 41.58 A O ANISOU 422 OE1 GLU A 55 4338 5844 5616 -284 589 1032 A O ATOM 423 OE2 GLU A 55 6.576 -5.279 -16.661 1.00 37.55 A O ANISOU 423 OE2 GLU A 55 3923 5425 4920 -230 723 1064 A O ATOM 424 N ASP A 56 6.049 -2.615 -20.496 1.00 29.47 A N ANISOU 424 N ASP A 56 3003 4487 3709 -312 825 1339 A N ATOM 425 CA ASP A 56 6.036 -2.073 -21.853 1.00 29.73 A C ANISOU 425 CA ASP A 56 3066 4577 3653 -324 878 1426 A C ATOM 426 C ASP A 56 4.622 -1.708 -22.287 1.00 28.18 A C ANISOU 426 C ASP A 56 2961 4372 3373 -329 816 1442 A C ATOM 427 O ASP A 56 4.402 -0.655 -22.895 1.00 25.02 A O ANISOU 427 O ASP A 56 2564 3959 2982 -361 798 1544 A O ATOM 428 CB ASP A 56 6.648 -3.063 -22.849 1.00 33.64 A C ANISOU 428 CB ASP A 56 3582 5180 4018 -277 1002 1394 A C ATOM 429 CG ASP A 56 8.138 -3.236 -22.670 1.00 35.26 A C ANISOU 429 CG ASP A 56 3682 5405 4312 -269 1076 1413 A C ATOM 430 OD1 ASP A 56 8.797 -2.289 -22.200 1.00 34.82 A O ANISOU 430 OD1 ASP A 56 3537 5297 4394 -318 1040 1490 A O ATOM 431 OD2 ASP A 56 8.656 -4.315 -23.024 1.00 42.68 A O ANISOU 431 OD2 ASP A 56 4627 6406 5182 -215 1170 1351 A O ATOM 432 N LEU A 57 3.647 -2.565 -21.983 1.00 25.83 A N ANISOU 432 N LEU A 57 2734 4081 2998 -297 780 1348 A N ATOM 433 CA LEU A 57 2.278 -2.264 -22.373 1.00 25.68 A C ANISOU 433 CA LEU A 57 2793 4062 2903 -301 711 1366 A C ATOM 434 C LEU A 57 1.795 -0.977 -21.723 1.00 25.62 A C ANISOU 434 C LEU A 57 2753 3946 3037 -338 620 1437 A C ATOM 435 O LEU A 57 1.090 -0.184 -22.357 1.00 23.47 A O ANISOU 435 O LEU A 57 2508 3669 2741 -349 584 1517 A O ATOM 436 CB LEU A 57 1.358 -3.431 -22.014 1.00 26.86 A C ANISOU 436 CB LEU A 57 3013 4231 2963 -267 681 1248 A C ATOM 437 CG LEU A 57 1.668 -4.715 -22.784 1.00 31.43 A C ANISOU 437 CG LEU A 57 3650 4904 3389 -231 774 1164 A C ATOM 438 CD1 LEU A 57 0.603 -5.753 -22.522 1.00 30.00 A C ANISOU 438 CD1 LEU A 57 3550 4732 3115 -207 732 1053 A C ATOM 439 CD2 LEU A 57 1.762 -4.428 -24.276 1.00 29.87 A C ANISOU 439 CD2 LEU A 57 3498 4791 3061 -242 829 1227 A C ATOM 440 N LEU A 58 2.191 -0.736 -20.470 1.00 24.42 A N ANISOU 440 N LEU A 58 2542 3702 3033 -357 583 1407 A N ATOM 441 CA LEU A 58 1.629 0.389 -19.733 1.00 23.10 A C ANISOU 441 CA LEU A 58 2364 3414 2999 -390 499 1444 A C ATOM 442 C LEU A 58 2.276 1.710 -20.143 1.00 22.60 A C ANISOU 442 C LEU A 58 2254 3302 3030 -435 512 1558 A C ATOM 443 O LEU A 58 1.602 2.745 -20.180 1.00 22.95 A O ANISOU 443 O LEU A 58 2314 3270 3138 -450 463 1620 A O ATOM 444 CB LEU A 58 1.776 0.164 -18.225 1.00 23.93 A C ANISOU 444 CB LEU A 58 2439 3437 3217 -403 452 1357 A C ATOM 445 CG LEU A 58 1.062 1.232 -17.379 1.00 26.89 A C ANISOU 445 CG LEU A 58 2822 3674 3720 -433 370 1366 A C ATOM 446 CD1 LEU A 58 -0.398 1.316 -17.778 1.00 23.26 A C ANISOU 446 CD1 LEU A 58 2429 3215 3194 -399 329 1385 A C ATOM 447 CD2 LEU A 58 1.197 0.979 -15.888 1.00 25.71 A C ANISOU 447 CD2 LEU A 58 2652 3451 3664 -453 322 1269 A C ATOM 448 N ILE A 59 3.576 1.702 -20.455 1.00 23.58 A N ANISOU 448 N ILE A 59 2318 3467 3173 -454 580 1589 A N ATOM 449 CA ILE A 59 4.225 2.933 -20.899 1.00 25.13 A C ANISOU 449 CA ILE A 59 2467 3623 3457 -502 596 1703 A C ATOM 450 C ILE A 59 3.644 3.434 -22.218 1.00 26.27 A C ANISOU 450 C ILE A 59 2654 3819 3508 -490 616 1807 A C ATOM 451 O ILE A 59 3.719 4.634 -22.512 1.00 27.44 A O ANISOU 451 O ILE A 59 2781 3905 3739 -525 605 1911 A O ATOM 452 CB ILE A 59 5.763 2.749 -20.996 1.00 26.50 A C ANISOU 452 CB ILE A 59 2558 3844 3666 -524 668 1721 A C ATOM 453 CG1 ILE A 59 6.442 4.102 -21.175 1.00 27.64 A C ANISOU 453 CG1 ILE A 59 2647 3923 3933 -589 669 1832 A C ATOM 454 CG2 ILE A 59 6.148 1.863 -22.153 1.00 26.81 A C ANISOU 454 CG2 ILE A 59 2611 4025 3549 -480 768 1730 A C ATOM 455 CD1 ILE A 59 6.225 5.030 -20.022 1.00 29.87 A C ANISOU 455 CD1 ILE A 59 2919 4052 4377 -642 582 1809 A C ATOM 456 N ARG A 60 3.055 2.550 -23.020 1.00 26.10 A N ANISOU 456 N ARG A 60 2695 3908 3314 -445 642 1780 A N ATOM 457 CA ARG A 60 2.411 2.961 -24.262 1.00 27.25 A C ANISOU 457 CA ARG A 60 2886 4115 3353 -437 647 1873 A C ATOM 458 C ARG A 60 1.000 3.490 -24.066 1.00 26.72 A C ANISOU 458 C ARG A 60 2860 3985 3308 -424 553 1893 A C ATOM 459 O ARG A 60 0.386 3.931 -25.043 1.00 27.78 A O ANISOU 459 O ARG A 60 3022 4165 3367 -418 542 1982 A O ATOM 460 CB ARG A 60 2.417 1.797 -25.254 1.00 27.59 A C ANISOU 460 CB ARG A 60 2987 4306 3192 -403 715 1827 A C ATOM 461 CG ARG A 60 3.795 1.176 -25.404 1.00 28.17 A C ANISOU 461 CG ARG A 60 3017 4437 3249 -402 820 1797 A C ATOM 462 CD ARG A 60 3.768 -0.097 -26.205 1.00 28.42 A C ANISOU 462 CD ARG A 60 3119 4591 3089 -364 893 1717 A C ATOM 463 NE ARG A 60 5.099 -0.688 -26.243 1.00 29.02 A N ANISOU 463 NE ARG A 60 3144 4708 3173 -352 1000 1685 A N ATOM 464 CZ ARG A 60 5.356 -1.935 -26.618 1.00 35.56 A C ANISOU 464 CZ ARG A 60 4018 5615 3879 -313 1082 1585 A C ATOM 465 NH1 ARG A 60 4.356 -2.755 -26.920 1.00 33.49 A N ANISOU 465 NH1 ARG A 60 3861 5391 3472 -290 1060 1498 A N ATOM 466 NH2 ARG A 60 6.612 -2.378 -26.626 1.00 35.44 A N ANISOU 466 NH2 ARG A 60 3940 5629 3895 -297 1182 1569 A N ATOM 467 N LYS A 61 0.488 3.484 -22.840 1.00 25.66 A N ANISOU 467 N LYS A 61 2725 3749 3276 -420 488 1819 A N ATOM 468 CA LYS A 61 -0.854 3.953 -22.553 1.00 26.51 A C ANISOU 468 CA LYS A 61 2864 3791 3419 -401 405 1831 A C ATOM 469 C LYS A 61 -0.821 5.430 -22.175 1.00 28.31 A C ANISOU 469 C LYS A 61 3056 3875 3826 -428 378 1914 A C ATOM 470 O LYS A 61 0.216 5.974 -21.787 1.00 27.36 A O ANISOU 470 O LYS A 61 2890 3689 3818 -472 406 1928 A O ATOM 471 CB LYS A 61 -1.480 3.139 -21.418 1.00 24.57 A C ANISOU 471 CB LYS A 61 2642 3508 3185 -379 357 1703 A C ATOM 472 CG LYS A 61 -1.400 1.652 -21.645 1.00 24.80 A C ANISOU 472 CG LYS A 61 2706 3658 3057 -355 390 1609 A C ATOM 473 CD LYS A 61 -2.267 1.206 -22.773 1.00 28.15 A C ANISOU 473 CD LYS A 61 3189 4194 3312 -332 380 1628 A C ATOM 474 CE LYS A 61 -3.696 1.506 -22.491 1.00 32.40 A C ANISOU 474 CE LYS A 61 3748 4689 3872 -313 290 1637 A C ATOM 475 NZ LYS A 61 -4.586 0.675 -23.352 1.00 34.07 A N ANISOU 475 NZ LYS A 61 4019 5021 3904 -296 265 1610 A N ATOM 476 N SER A 62 -1.979 6.073 -22.303 1.00 33.01 A N ANISOU 476 N SER A 62 3672 4422 4450 -403 323 1967 A N ATOM 477 CA SER A 62 -2.207 7.454 -21.902 1.00 31.17 A C ANISOU 477 CA SER A 62 3418 4035 4391 -416 297 2033 A C ATOM 478 C SER A 62 -3.357 7.480 -20.902 1.00 27.70 A C ANISOU 478 C SER A 62 3004 3499 4022 -380 234 1960 A C ATOM 479 O SER A 62 -4.193 6.577 -20.900 1.00 30.29 A O ANISOU 479 O SER A 62 3360 3903 4245 -342 203 1904 A O ATOM 480 CB SER A 62 -2.567 8.339 -23.109 1.00 31.75 A C ANISOU 480 CB SER A 62 3482 4136 4444 -407 302 2190 A C ATOM 481 OG SER A 62 -1.707 8.119 -24.223 1.00 39.31 A O ANISOU 481 OG SER A 62 4428 5220 5290 -430 363 2259 A O ATOM 482 N ASN A 63 -3.402 8.516 -20.054 1.00 28.04 A N ANISOU 482 N ASN A 63 3040 3372 4243 -395 218 1955 A N ATOM 483 CA ASN A 63 -4.547 8.681 -19.152 1.00 27.69 A C ANISOU 483 CA ASN A 63 3021 3226 4274 -353 170 1893 A C ATOM 484 C ASN A 63 -5.868 8.582 -19.908 1.00 28.22 A C ANISOU 484 C ASN A 63 3095 3366 4261 -291 137 1961 A C ATOM 485 O ASN A 63 -6.807 7.908 -19.463 1.00 25.76 A O ANISOU 485 O ASN A 63 2803 3079 3908 -252 100 1892 A O ATOM 486 CB ASN A 63 -4.459 10.022 -18.416 1.00 27.91 A C ANISOU 486 CB ASN A 63 3050 3057 4499 -373 171 1898 A C ATOM 487 CG ASN A 63 -3.373 10.037 -17.346 1.00 27.48 A C ANISOU 487 CG ASN A 63 2995 2917 4527 -440 182 1793 A C ATOM 488 ND2 ASN A 63 -2.862 11.228 -17.024 1.00 26.92 A N ANISOU 488 ND2 ASN A 63 2923 2701 4604 -488 194 1813 A N ATOM 489 OD1 ASN A 63 -2.985 8.993 -16.834 1.00 27.89 A O ANISOU 489 OD1 ASN A 63 3048 3037 4512 -453 177 1696 A O ATOM 490 N HIS A 64 -5.954 9.245 -21.064 1.00 29.16 A N ANISOU 490 N HIS A 64 3194 3529 4357 -287 147 2101 A N ATOM 491 CA HIS A 64 -7.194 9.274 -21.827 1.00 30.26 A C ANISOU 491 CA HIS A 64 3328 3741 4428 -237 109 2180 A C ATOM 492 C HIS A 64 -7.545 7.929 -22.450 1.00 27.75 A C ANISOU 492 C HIS A 64 3031 3608 3904 -229 87 2140 A C ATOM 493 O HIS A 64 -8.692 7.750 -22.873 1.00 28.57 A O ANISOU 493 O HIS A 64 3133 3778 3947 -193 40 2173 A O ATOM 494 CB HIS A 64 -7.123 10.369 -22.896 1.00 31.47 A C ANISOU 494 CB HIS A 64 3453 3893 4613 -240 124 2350 A C ATOM 495 CG HIS A 64 -6.410 9.965 -24.151 1.00 34.12 A C ANISOU 495 CG HIS A 64 3786 4388 4791 -273 154 2421 A C ATOM 496 CD2 HIS A 64 -6.864 9.403 -25.297 1.00 33.86 A C ANISOU 496 CD2 HIS A 64 3762 4525 4580 -263 137 2477 A C ATOM 497 ND1 HIS A 64 -5.060 10.186 -24.342 1.00 36.42 A N ANISOU 497 ND1 HIS A 64 4067 4673 5099 -325 214 2442 A N ATOM 498 CE1 HIS A 64 -4.709 9.750 -25.540 1.00 34.18 A C ANISOU 498 CE1 HIS A 64 3787 4547 4652 -338 240 2506 A C ATOM 499 NE2 HIS A 64 -5.786 9.273 -26.142 1.00 37.69 A N ANISOU 499 NE2 HIS A 64 4250 5100 4972 -303 193 2524 A N ATOM 500 N ASN A 65 -6.615 6.973 -22.489 1.00 27.31 A N ANISOU 500 N ASN A 65 2995 3636 3744 -262 121 2064 A N ATOM 501 CA ASN A 65 -6.985 5.632 -22.931 1.00 25.70 A C ANISOU 501 CA ASN A 65 2825 3586 3353 -255 104 1998 A C ATOM 502 C ASN A 65 -7.906 4.925 -21.945 1.00 28.10 A C ANISOU 502 C ASN A 65 3146 3862 3667 -225 55 1886 A C ATOM 503 O ASN A 65 -8.499 3.906 -22.304 1.00 29.50 A O ANISOU 503 O ASN A 65 3351 4154 3702 -218 26 1837 A O ATOM 504 CB ASN A 65 -5.747 4.765 -23.154 1.00 28.59 A C ANISOU 504 CB ASN A 65 3210 4036 3618 -289 167 1937 A C ATOM 505 CG ASN A 65 -4.844 5.298 -24.228 1.00 32.50 A C ANISOU 505 CG ASN A 65 3690 4585 4076 -316 224 2044 A C ATOM 506 ND2 ASN A 65 -5.438 5.893 -25.256 1.00 31.44 A N ANISOU 506 ND2 ASN A 65 3551 4501 3894 -308 203 2165 A N ATOM 507 OD1 ASN A 65 -3.624 5.160 -24.152 1.00 30.80 A O ANISOU 507 OD1 ASN A 65 3460 4371 3871 -346 287 2024 A O ATOM 508 N PHE A 66 -8.027 5.426 -20.717 1.00 27.01 A N ANISOU 508 N PHE A 66 2997 3574 3692 -213 47 1841 A N ATOM 509 CA PHE A 66 -8.812 4.779 -19.671 1.00 25.87 A C ANISOU 509 CA PHE A 66 2867 3394 3567 -185 10 1734 A C ATOM 510 C PHE A 66 -10.119 5.540 -19.482 1.00 27.29 A C ANISOU 510 C PHE A 66 3026 3503 3841 -137 -31 1784 A C ATOM 511 O PHE A 66 -10.125 6.660 -18.962 1.00 26.20 A O ANISOU 511 O PHE A 66 2873 3219 3864 -123 -17 1815 A O ATOM 512 CB PHE A 66 -8.030 4.725 -18.363 1.00 22.24 A C ANISOU 512 CB PHE A 66 2415 2821 3213 -206 34 1634 A C ATOM 513 CG PHE A 66 -6.774 3.910 -18.439 1.00 21.73 A C ANISOU 513 CG PHE A 66 2357 2829 3069 -249 77 1582 A C ATOM 514 CD1 PHE A 66 -6.814 2.539 -18.274 1.00 24.11 A C ANISOU 514 CD1 PHE A 66 2684 3226 3249 -246 74 1491 A C ATOM 515 CD2 PHE A 66 -5.559 4.517 -18.693 1.00 25.20 A C ANISOU 515 CD2 PHE A 66 2773 3241 3561 -290 125 1628 A C ATOM 516 CE1 PHE A 66 -5.669 1.788 -18.347 1.00 24.72 A C ANISOU 516 CE1 PHE A 66 2761 3367 3263 -274 124 1445 A C ATOM 517 CE2 PHE A 66 -4.405 3.768 -18.766 1.00 26.94 A C ANISOU 517 CE2 PHE A 66 2986 3533 3717 -322 171 1584 A C ATOM 518 CZ PHE A 66 -4.463 2.402 -18.589 1.00 24.45 A C ANISOU 518 CZ PHE A 66 2695 3310 3286 -309 174 1492 A C ATOM 519 N LEU A 67 -11.221 4.926 -19.900 1.00 25.38 A N ANISOU 519 N LEU A 67 2781 3361 3501 -112 -80 1787 A N ATOM 520 CA LEU A 67 -12.551 5.476 -19.678 1.00 28.21 A C ANISOU 520 CA LEU A 67 3107 3670 3943 -61 -117 1829 A C ATOM 521 C LEU A 67 -13.077 4.910 -18.367 1.00 23.35 A C ANISOU 521 C LEU A 67 2504 2991 3378 -35 -130 1708 A C ATOM 522 O LEU A 67 -13.280 3.699 -18.256 1.00 24.62 A O ANISOU 522 O LEU A 67 2686 3244 3423 -47 -155 1627 A O ATOM 523 CB LEU A 67 -13.493 5.116 -20.828 1.00 28.92 A C ANISOU 523 CB LEU A 67 3177 3909 3903 -57 -169 1901 A C ATOM 524 CG LEU A 67 -13.547 5.982 -22.093 1.00 34.07 A C ANISOU 524 CG LEU A 67 3798 4610 4536 -61 -172 2057 A C ATOM 525 CD1 LEU A 67 -14.142 7.367 -21.810 1.00 34.58 A C ANISOU 525 CD1 LEU A 67 3813 4539 4785 -12 -165 2155 A C ATOM 526 CD2 LEU A 67 -12.181 6.090 -22.739 1.00 32.81 A C ANISOU 526 CD2 LEU A 67 3665 4483 4319 -106 -123 2086 A C ATOM 527 N VAL A 68 -13.274 5.771 -17.373 1.00 25.48 A N ANISOU 527 N VAL A 68 2767 3099 3816 -0 -108 1689 A N ATOM 528 CA VAL A 68 -13.798 5.365 -16.072 1.00 22.84 A C ANISOU 528 CA VAL A 68 2446 2692 3539 31 -111 1577 A C ATOM 529 C VAL A 68 -15.174 5.996 -15.891 1.00 24.69 A C ANISOU 529 C VAL A 68 2640 2876 3864 97 -122 1622 A C ATOM 530 O VAL A 68 -15.313 7.226 -15.936 1.00 23.31 A O ANISOU 530 O VAL A 68 2448 2594 3816 126 -94 1691 A O ATOM 531 CB VAL A 68 -12.850 5.759 -14.927 1.00 24.89 A C ANISOU 531 CB VAL A 68 2741 2801 3913 12 -68 1490 A C ATOM 532 CG1 VAL A 68 -13.434 5.328 -13.593 1.00 24.70 A C ANISOU 532 CG1 VAL A 68 2736 2710 3938 46 -70 1373 A C ATOM 533 CG2 VAL A 68 -11.483 5.112 -15.124 1.00 22.26 A C ANISOU 533 CG2 VAL A 68 2431 2529 3496 -56 -55 1457 A C ATOM 534 N GLN A 69 -16.182 5.148 -15.676 1.00 22.64 A N ANISOU 534 N GLN A 69 2365 2693 3544 121 -157 1582 A N ATOM 535 CA GLN A 69 -17.586 5.528 -15.552 1.00 27.40 A C ANISOU 535 CA GLN A 69 2917 3282 4213 181 -169 1625 A C ATOM 536 C GLN A 69 -18.042 5.191 -14.138 1.00 24.90 A C ANISOU 536 C GLN A 69 2614 2883 3961 221 -148 1507 A C ATOM 537 O GLN A 69 -18.007 4.023 -13.740 1.00 22.46 A O ANISOU 537 O GLN A 69 2327 2645 3563 199 -171 1419 A O ATOM 538 CB GLN A 69 -18.443 4.754 -16.559 1.00 28.33 A C ANISOU 538 CB GLN A 69 2996 3575 4195 163 -232 1682 A C ATOM 539 CG GLN A 69 -18.254 5.019 -18.047 1.00 32.30 A C ANISOU 539 CG GLN A 69 3480 4182 4612 128 -260 1804 A C ATOM 540 CD GLN A 69 -19.211 6.070 -18.577 1.00 38.10 A C ANISOU 540 CD GLN A 69 4145 4898 5434 174 -268 1943 A C ATOM 541 NE2 GLN A 69 -20.223 5.617 -19.319 1.00 44.17 A N ANISOU 541 NE2 GLN A 69 4866 5799 6117 165 -327 2002 A N ATOM 542 OE1 GLN A 69 -19.077 7.261 -18.296 1.00 41.40 A O ANISOU 542 OE1 GLN A 69 4551 5181 5999 214 -222 1995 A O ATOM 543 N ALA A 70 -18.469 6.197 -13.381 1.00 26.17 A N ANISOU 543 N ALA A 70 2768 2899 4276 280 -100 1500 A N ATOM 544 CA ALA A 70 -19.064 5.971 -12.063 1.00 27.55 A C ANISOU 544 CA ALA A 70 2955 3002 4512 328 -70 1392 A C ATOM 545 C ALA A 70 -20.555 6.255 -12.202 1.00 32.26 A C ANISOU 545 C ALA A 70 3481 3624 5153 392 -71 1462 A C ATOM 546 O ALA A 70 -20.981 7.412 -12.170 1.00 30.12 A O ANISOU 546 O ALA A 70 3187 3250 5007 445 -29 1521 A O ATOM 547 CB ALA A 70 -18.415 6.837 -10.986 1.00 26.09 A C ANISOU 547 CB ALA A 70 2828 2630 4457 344 -5 1305 A C ATOM 548 N GLY A 71 -21.343 5.197 -12.351 1.00 32.55 A N ANISOU 548 N GLY A 71 3481 3793 5092 383 -117 1457 A N ATOM 549 CA GLY A 71 -22.724 5.394 -12.750 1.00 35.93 A C ANISOU 549 CA GLY A 71 3829 4277 5548 424 -133 1550 A C ATOM 550 C GLY A 71 -22.744 6.035 -14.120 1.00 39.01 A C ANISOU 550 C GLY A 71 4178 4720 5924 406 -165 1700 A C ATOM 551 O GLY A 71 -22.030 5.615 -15.038 1.00 40.27 A O ANISOU 551 O GLY A 71 4359 4974 5969 340 -210 1727 A O ATOM 552 N ASN A 72 -23.548 7.088 -14.265 1.00 41.15 A N ANISOU 552 N ASN A 72 4391 4930 6315 469 -137 1801 A N ATOM 553 CA ASN A 72 -23.603 7.855 -15.502 1.00 43.95 A C ANISOU 553 CA ASN A 72 4701 5321 6679 463 -162 1958 A C ATOM 554 C ASN A 72 -22.751 9.118 -15.428 1.00 43.64 A C ANISOU 554 C ASN A 72 4698 5124 6759 485 -103 1985 A C ATOM 555 O ASN A 72 -23.097 10.141 -16.033 1.00 43.09 A O ANISOU 555 O ASN A 72 4581 5017 6776 520 -91 2118 A O ATOM 556 CB ASN A 72 -25.054 8.190 -15.856 1.00 44.12 A C ANISOU 556 CB ASN A 72 4622 5388 6755 514 -177 2079 A C ATOM 557 CG ASN A 72 -25.803 8.858 -14.711 1.00 51.09 A C ANISOU 557 CG ASN A 72 5484 6129 7799 608 -98 2046 A C ATOM 558 ND2 ASN A 72 -27.133 8.824 -14.771 1.00 47.57 A N ANISOU 558 ND2 ASN A 72 4949 5738 7388 650 -107 2122 A N ATOM 559 OD1 ASN A 72 -25.194 9.404 -13.789 1.00 55.31 A O ANISOU 559 OD1 ASN A 72 6083 6508 8425 639 -27 1952 A O ATOM 560 N VAL A 73 -21.640 9.063 -14.695 1.00 38.82 A N ANISOU 560 N VAL A 73 4171 4421 6160 459 -68 1865 A N ATOM 561 CA VAL A 73 -20.727 10.192 -14.535 1.00 39.34 A C ANISOU 561 CA VAL A 73 4281 4329 6337 462 -15 1869 A C ATOM 562 C VAL A 73 -19.329 9.717 -14.915 1.00 34.71 A C ANISOU 562 C VAL A 73 3750 3788 5649 377 -37 1833 A C ATOM 563 O VAL A 73 -18.841 8.722 -14.369 1.00 32.91 A O ANISOU 563 O VAL A 73 3566 3602 5338 340 -50 1716 A O ATOM 564 CB VAL A 73 -20.753 10.742 -13.098 1.00 39.53 A C ANISOU 564 CB VAL A 73 4356 4169 6496 513 61 1744 A C ATOM 565 CG1 VAL A 73 -19.619 11.727 -12.872 1.00 37.64 A C ANISOU 565 CG1 VAL A 73 4180 3769 6350 487 106 1717 A C ATOM 566 CG2 VAL A 73 -22.093 11.386 -12.799 1.00 42.50 A C ANISOU 566 CG2 VAL A 73 4673 4488 6985 606 100 1795 A C ATOM 567 N GLN A 74 -18.691 10.416 -15.851 1.00 36.90 A N ANISOU 567 N GLN A 74 4022 4062 5936 348 -39 1941 A N ATOM 568 CA GLN A 74 -17.338 10.054 -16.255 1.00 35.90 A C ANISOU 568 CA GLN A 74 3942 3979 5721 270 -49 1919 A C ATOM 569 C GLN A 74 -16.309 10.630 -15.291 1.00 34.25 A C ANISOU 569 C GLN A 74 3797 3597 5619 249 5 1821 A C ATOM 570 O GLN A 74 -16.393 11.795 -14.895 1.00 35.99 A O ANISOU 570 O GLN A 74 4027 3657 5992 283 51 1834 A O ATOM 571 CB GLN A 74 -17.015 10.551 -17.664 1.00 39.39 A C ANISOU 571 CB GLN A 74 4351 4495 6120 242 -68 2075 A C ATOM 572 CG GLN A 74 -15.622 10.096 -18.084 1.00 39.30 A C ANISOU 572 CG GLN A 74 4383 4541 6007 163 -69 2050 A C ATOM 573 CD GLN A 74 -15.221 10.517 -19.480 1.00 44.25 A C ANISOU 573 CD GLN A 74 4985 5254 6575 133 -80 2198 A C ATOM 574 NE2 GLN A 74 -14.008 10.144 -19.873 1.00 41.42 A N ANISOU 574 NE2 GLN A 74 4660 4951 6128 68 -69 2181 A N ATOM 575 OE1 GLN A 74 -15.965 11.207 -20.182 1.00 48.20 A O ANISOU 575 OE1 GLN A 74 5434 5769 7112 168 -93 2332 A O ATOM 576 N LEU A 75 -15.312 9.816 -14.951 1.00 28.34 A N ANISOU 576 N LEU A 75 3094 2884 4790 188 -2 1722 A N ATOM 577 CA LEU A 75 -14.219 10.218 -14.076 1.00 27.73 A C ANISOU 577 CA LEU A 75 3075 2666 4794 147 36 1624 A C ATOM 578 C LEU A 75 -12.967 10.450 -14.914 1.00 31.29 A C ANISOU 578 C LEU A 75 3529 3150 5209 74 38 1692 A C ATOM 579 O LEU A 75 -12.480 9.526 -15.575 1.00 33.17 A O ANISOU 579 O LEU A 75 3759 3538 5306 33 12 1708 A O ATOM 580 CB LEU A 75 -13.952 9.146 -13.021 1.00 28.00 A C ANISOU 580 CB LEU A 75 3150 2716 4773 127 28 1470 A C ATOM 581 CG LEU A 75 -14.950 9.026 -11.871 1.00 27.98 A C ANISOU 581 CG LEU A 75 3160 2644 4826 191 45 1371 A C ATOM 582 CD1 LEU A 75 -14.411 8.043 -10.852 1.00 27.43 A C ANISOU 582 CD1 LEU A 75 3136 2582 4705 157 38 1225 A C ATOM 583 CD2 LEU A 75 -15.231 10.375 -11.226 1.00 32.97 A C ANISOU 583 CD2 LEU A 75 3816 3086 5623 232 100 1349 A C ATOM 584 N ARG A 76 -12.439 11.670 -14.872 1.00 28.14 A N ANISOU 584 N ARG A 76 3144 2610 4939 58 74 1726 A N ATOM 585 CA ARG A 76 -11.204 11.979 -15.584 1.00 31.26 A C ANISOU 585 CA ARG A 76 3537 3023 5317 -14 83 1791 A C ATOM 586 C ARG A 76 -10.016 11.318 -14.897 1.00 28.78 A C ANISOU 586 C ARG A 76 3259 2712 4966 -89 86 1669 A C ATOM 587 O ARG A 76 -9.739 11.595 -13.725 1.00 26.45 A O ANISOU 587 O ARG A 76 3007 2283 4761 -108 102 1548 A O ATOM 588 CB ARG A 76 -10.984 13.488 -15.653 1.00 32.84 A C ANISOU 588 CB ARG A 76 3742 3057 5677 -17 121 1859 A C ATOM 589 CG ARG A 76 -9.898 13.897 -16.636 1.00 33.78 A C ANISOU 589 CG ARG A 76 3843 3214 5779 -82 131 1968 A C ATOM 590 CD ARG A 76 -9.901 15.390 -16.857 1.00 40.33 A C ANISOU 590 CD ARG A 76 4670 3887 6766 -75 164 2063 A C ATOM 591 NE ARG A 76 -9.556 16.096 -15.626 1.00 42.72 A N ANISOU 591 NE ARG A 76 5033 3987 7214 -101 193 1938 A N ATOM 592 CZ ARG A 76 -8.418 16.760 -15.442 1.00 46.58 A C ANISOU 592 CZ ARG A 76 5547 4373 7778 -184 214 1922 A C ATOM 593 NH1 ARG A 76 -7.515 16.818 -16.416 1.00 47.62 A N ANISOU 593 NH1 ARG A 76 5641 4586 7864 -242 217 2032 A N ATOM 594 NH2 ARG A 76 -8.181 17.373 -14.286 1.00 48.70 A N ANISOU 594 NH2 ARG A 76 5878 4460 8164 -215 234 1793 A N ATOM 595 N VAL A 77 -9.304 10.467 -15.632 1.00 29.02 A N ANISOU 595 N VAL A 77 3271 2896 4861 -132 74 1700 A N ATOM 596 CA VAL A 77 -8.073 9.855 -15.139 1.00 25.68 A C ANISOU 596 CA VAL A 77 2864 2491 4402 -204 81 1609 A C ATOM 597 C VAL A 77 -6.934 10.857 -15.289 1.00 26.83 A C ANISOU 597 C VAL A 77 3006 2548 4642 -271 111 1650 A C ATOM 598 O VAL A 77 -6.734 11.430 -16.367 1.00 26.07 A O ANISOU 598 O VAL A 77 2880 2484 4541 -276 126 1783 A O ATOM 599 CB VAL A 77 -7.772 8.555 -15.898 1.00 24.47 A C ANISOU 599 CB VAL A 77 2693 2535 4068 -216 69 1625 A C ATOM 600 CG1 VAL A 77 -6.474 7.932 -15.401 1.00 24.31 A C ANISOU 600 CG1 VAL A 77 2677 2538 4022 -284 83 1541 A C ATOM 601 CG2 VAL A 77 -8.923 7.557 -15.735 1.00 24.89 A C ANISOU 601 CG2 VAL A 77 2754 2674 4031 -160 33 1581 A C ATOM 602 N ILE A 78 -6.188 11.079 -14.208 1.00 26.41 A N ANISOU 602 N ILE A 78 2980 2384 4671 -328 117 1537 A N ATOM 603 CA ILE A 78 -5.100 12.051 -14.189 1.00 26.00 A C ANISOU 603 CA ILE A 78 2926 2235 4719 -405 139 1559 A C ATOM 604 C ILE A 78 -3.751 11.411 -13.909 1.00 26.95 A C ANISOU 604 C ILE A 78 3026 2422 4793 -489 138 1498 A C ATOM 605 O ILE A 78 -2.730 12.106 -13.921 1.00 30.38 A O ANISOU 605 O ILE A 78 3447 2798 5300 -564 152 1518 A O ATOM 606 CB ILE A 78 -5.381 13.183 -13.181 1.00 27.02 A C ANISOU 606 CB ILE A 78 3108 2153 5007 -413 147 1482 A C ATOM 607 CG1 ILE A 78 -5.487 12.626 -11.755 1.00 26.90 A C ANISOU 607 CG1 ILE A 78 3140 2091 4992 -424 127 1301 A C ATOM 608 CG2 ILE A 78 -6.636 13.949 -13.580 1.00 29.63 A C ANISOU 608 CG2 ILE A 78 3444 2414 5401 -324 160 1566 A C ATOM 609 CD1 ILE A 78 -5.292 13.691 -10.684 1.00 32.34 A C ANISOU 609 CD1 ILE A 78 3892 2582 5814 -470 136 1195 A C ATOM 610 N GLY A 79 -3.716 10.106 -13.671 1.00 25.62 A N ANISOU 610 N GLY A 79 2850 2375 4510 -478 121 1431 A N ATOM 611 CA GLY A 79 -2.471 9.391 -13.492 1.00 23.22 A C ANISOU 611 CA GLY A 79 2512 2155 4155 -544 124 1387 A C ATOM 612 C GLY A 79 -2.758 7.910 -13.535 1.00 22.80 A C ANISOU 612 C GLY A 79 2453 2249 3963 -503 114 1346 A C ATOM 613 O GLY A 79 -3.902 7.479 -13.359 1.00 23.80 A O ANISOU 613 O GLY A 79 2608 2384 4050 -439 95 1320 A O ATOM 614 N HIS A 80 -1.710 7.135 -13.798 1.00 21.96 A N ANISOU 614 N HIS A 80 2305 2258 3782 -538 132 1345 A N ATOM 615 CA HIS A 80 -1.849 5.686 -13.817 1.00 20.82 A C ANISOU 615 CA HIS A 80 2156 2247 3507 -504 131 1299 A C ATOM 616 C HIS A 80 -0.513 5.072 -13.425 1.00 21.36 A C ANISOU 616 C HIS A 80 2176 2376 3564 -556 144 1248 A C ATOM 617 O HIS A 80 0.547 5.589 -13.800 1.00 21.01 A O ANISOU 617 O HIS A 80 2088 2336 3559 -605 170 1300 A O ATOM 618 CB HIS A 80 -2.279 5.197 -15.207 1.00 21.75 A C ANISOU 618 CB HIS A 80 2273 2500 3490 -453 159 1395 A C ATOM 619 CG HIS A 80 -1.342 5.613 -16.303 1.00 22.96 A C ANISOU 619 CG HIS A 80 2389 2713 3623 -480 207 1499 A C ATOM 620 CD2 HIS A 80 -0.241 5.006 -16.805 1.00 24.04 A C ANISOU 620 CD2 HIS A 80 2486 2957 3690 -501 254 1512 A C ATOM 621 ND1 HIS A 80 -1.497 6.781 -17.020 1.00 26.10 A N ANISOU 621 ND1 HIS A 80 2783 3056 4076 -484 215 1609 A N ATOM 622 CE1 HIS A 80 -0.525 6.879 -17.911 1.00 29.52 A C ANISOU 622 CE1 HIS A 80 3179 3565 4473 -512 264 1687 A C ATOM 623 NE2 HIS A 80 0.252 5.816 -17.799 1.00 27.18 A N ANISOU 623 NE2 HIS A 80 2860 3367 4101 -520 291 1628 A N ATOM 624 N SER A 81 -0.566 3.981 -12.664 1.00 18.94 A N ANISOU 624 N SER A 81 1872 2118 3209 -545 125 1151 A N ATOM 625 CA SER A 81 0.630 3.227 -12.303 1.00 19.13 A C ANISOU 625 CA SER A 81 1840 2218 3211 -578 136 1106 A C ATOM 626 C SER A 81 0.213 1.788 -12.068 1.00 19.17 A C ANISOU 626 C SER A 81 1853 2317 3112 -528 137 1044 A C ATOM 627 O SER A 81 -0.965 1.503 -11.862 1.00 21.76 A O ANISOU 627 O SER A 81 2232 2626 3409 -489 114 1016 A O ATOM 628 CB SER A 81 1.309 3.767 -11.038 1.00 18.47 A C ANISOU 628 CB SER A 81 1739 2042 3238 -650 89 1023 A C ATOM 629 OG SER A 81 0.346 3.981 -10.015 1.00 22.84 A O ANISOU 629 OG SER A 81 2352 2493 3832 -646 39 933 A O ATOM 630 N MET A 82 1.181 0.879 -12.087 1.00 16.61 A N ANISOU 630 N MET A 82 1478 2093 2741 -527 166 1025 A N ATOM 631 CA MET A 82 0.916 -0.488 -11.650 1.00 18.13 A C ANISOU 631 CA MET A 82 1673 2359 2855 -485 166 952 A C ATOM 632 C MET A 82 1.436 -0.730 -10.249 1.00 17.02 A C ANISOU 632 C MET A 82 1499 2189 2778 -519 111 860 A C ATOM 633 O MET A 82 2.539 -0.294 -9.896 1.00 17.01 A O ANISOU 633 O MET A 82 1445 2175 2842 -568 99 860 A O ATOM 634 CB MET A 82 1.549 -1.549 -12.545 1.00 23.95 A C ANISOU 634 CB MET A 82 2382 3229 3488 -439 242 977 A C ATOM 635 CG MET A 82 0.700 -2.048 -13.650 1.00 28.74 A C ANISOU 635 CG MET A 82 3047 3905 3967 -387 283 1009 A C ATOM 636 SD MET A 82 1.682 -3.216 -14.569 1.00 24.16 A S ANISOU 636 SD MET A 82 2441 3459 3280 -340 383 1008 A S ATOM 637 CE MET A 82 3.249 -2.357 -14.738 1.00 26.68 A C ANISOU 637 CE MET A 82 2671 3765 3699 -386 412 1076 A C ATOM 638 N GLN A 83 0.670 -1.495 -9.485 1.00 16.42 A N ANISOU 638 N GLN A 83 1453 2115 2669 -491 77 780 A N ATOM 639 CA GLN A 83 1.162 -2.141 -8.271 1.00 21.33 A C ANISOU 639 CA GLN A 83 2047 2755 3301 -498 30 688 A C ATOM 640 C GLN A 83 0.944 -3.635 -8.478 1.00 14.67 A C ANISOU 640 C GLN A 83 1220 2008 2346 -411 63 648 A C ATOM 641 O GLN A 83 -0.191 -4.114 -8.405 1.00 13.83 A O ANISOU 641 O GLN A 83 1190 1893 2172 -359 49 591 A O ATOM 642 CB GLN A 83 0.455 -1.642 -7.022 1.00 21.50 A C ANISOU 642 CB GLN A 83 2126 2681 3361 -521 -48 590 A C ATOM 643 CG GLN A 83 0.869 -2.422 -5.790 1.00 24.22 A C ANISOU 643 CG GLN A 83 2449 3067 3687 -523 -99 502 A C ATOM 644 CD GLN A 83 0.693 -1.644 -4.496 1.00 34.31 A C ANISOU 644 CD GLN A 83 3761 4257 5017 -587 -176 415 A C ATOM 645 NE2 GLN A 83 1.199 -2.208 -3.396 1.00 33.22 A N ANISOU 645 NE2 GLN A 83 3596 4168 4859 -606 -231 354 A N ATOM 646 OE1 GLN A 83 0.107 -0.554 -4.478 1.00 37.22 A O ANISOU 646 OE1 GLN A 83 4183 4515 5443 -616 -182 404 A O ATOM 647 N ASN A 84 2.033 -4.358 -8.766 1.00 14.25 A N ANISOU 647 N ASN A 84 1090 2039 2284 -397 112 683 A N ATOM 648 CA ASN A 84 1.954 -5.792 -9.033 1.00 16.20 A C ANISOU 648 CA ASN A 84 1354 2362 2441 -313 159 647 A C ATOM 649 C ASN A 84 0.931 -6.092 -10.118 1.00 13.29 A C ANISOU 649 C ASN A 84 1071 2010 1968 -265 203 647 A C ATOM 650 O ASN A 84 1.068 -5.586 -11.233 1.00 14.39 A O ANISOU 650 O ASN A 84 1207 2174 2085 -279 257 727 A O ATOM 651 CB ASN A 84 1.683 -6.525 -7.734 1.00 13.25 A C ANISOU 651 CB ASN A 84 996 1975 2064 -290 95 555 A C ATOM 652 CG ASN A 84 2.723 -6.179 -6.690 1.00 14.93 A C ANISOU 652 CG ASN A 84 1120 2189 2365 -349 38 562 A C ATOM 653 ND2 ASN A 84 2.277 -5.642 -5.558 1.00 14.15 A N ANISOU 653 ND2 ASN A 84 1055 2031 2290 -395 -49 498 A N ATOM 654 OD1 ASN A 84 3.939 -6.308 -6.946 1.00 13.76 A O ANISOU 654 OD1 ASN A 84 889 2089 2251 -352 73 616 A O ATOM 655 N CYS A 85 -0.120 -6.863 -9.824 1.00 12.97 A N ANISOU 655 N CYS A 85 1107 1960 1860 -219 176 567 A N ATOM 656 CA CYS A 85 -1.058 -7.212 -10.872 1.00 12.10 A C ANISOU 656 CA CYS A 85 1072 1880 1646 -186 206 567 A C ATOM 657 C CYS A 85 -2.304 -6.325 -10.894 1.00 14.92 A C ANISOU 657 C CYS A 85 1482 2181 2005 -206 149 578 A C ATOM 658 O CYS A 85 -3.236 -6.608 -11.658 1.00 12.34 A O ANISOU 658 O CYS A 85 1213 1885 1592 -185 152 580 A O ATOM 659 CB CYS A 85 -1.456 -8.680 -10.749 1.00 12.23 A C ANISOU 659 CB CYS A 85 1135 1925 1586 -128 221 482 A C ATOM 660 SG CYS A 85 -0.052 -9.737 -11.097 1.00 13.77 A S ANISOU 660 SG CYS A 85 1273 2183 1775 -83 320 487 A S ATOM 661 N VAL A 86 -2.329 -5.240 -10.120 1.00 11.06 A N ANISOU 661 N VAL A 86 973 1612 1616 -247 98 588 A N ATOM 662 CA VAL A 86 -3.418 -4.283 -10.242 1.00 13.20 A C ANISOU 662 CA VAL A 86 1285 1819 1910 -256 62 616 A C ATOM 663 C VAL A 86 -2.895 -2.977 -10.808 1.00 12.90 A C ANISOU 663 C VAL A 86 1213 1740 1949 -305 80 722 A C ATOM 664 O VAL A 86 -1.701 -2.637 -10.733 1.00 13.46 A O ANISOU 664 O VAL A 86 1223 1810 2082 -350 102 757 A O ATOM 665 CB VAL A 86 -4.192 -4.049 -8.927 1.00 15.92 A C ANISOU 665 CB VAL A 86 1658 2083 2307 -251 -0 534 A C ATOM 666 CG1 VAL A 86 -4.741 -5.382 -8.403 1.00 14.54 A C ANISOU 666 CG1 VAL A 86 1514 1952 2058 -205 -14 446 A C ATOM 667 CG2 VAL A 86 -3.325 -3.407 -7.905 1.00 16.09 A C ANISOU 667 CG2 VAL A 86 1643 2044 2426 -303 -26 506 A C ATOM 668 N LEU A 87 -3.816 -2.280 -11.441 1.00 12.39 A N ANISOU 668 N LEU A 87 1181 1647 1881 -297 71 787 A N ATOM 669 CA LEU A 87 -3.626 -0.940 -11.962 1.00 13.42 A C ANISOU 669 CA LEU A 87 1290 1714 2095 -337 83 901 A C ATOM 670 C LEU A 87 -4.245 0.050 -10.993 1.00 13.46 A C ANISOU 670 C LEU A 87 1317 1578 2221 -347 36 868 A C ATOM 671 O LEU A 87 -5.305 -0.214 -10.420 1.00 15.51 A O ANISOU 671 O LEU A 87 1616 1813 2464 -303 2 798 A O ATOM 672 CB LEU A 87 -4.282 -0.823 -13.333 1.00 14.32 A C ANISOU 672 CB LEU A 87 1425 1892 2122 -314 103 1011 A C ATOM 673 CG LEU A 87 -3.823 0.206 -14.340 1.00 21.01 A C ANISOU 673 CG LEU A 87 2250 2735 2998 -338 135 1135 A C ATOM 674 CD1 LEU A 87 -2.353 0.032 -14.664 1.00 22.13 A C ANISOU 674 CD1 LEU A 87 2344 2931 3132 -368 190 1143 A C ATOM 675 CD2 LEU A 87 -4.707 0.061 -15.586 1.00 21.15 A C ANISOU 675 CD2 LEU A 87 2303 2842 2892 -299 132 1199 A C ATOM 676 N LYS A 88 -3.569 1.179 -10.791 1.00 15.81 A N ANISOU 676 N LYS A 88 1587 1779 2643 -408 39 912 A N ATOM 677 CA LYS A 88 -4.081 2.270 -9.969 1.00 20.45 A C ANISOU 677 CA LYS A 88 2204 2210 3356 -422 9 880 A C ATOM 678 C LYS A 88 -4.254 3.494 -10.858 1.00 17.85 A C ANISOU 678 C LYS A 88 1877 1819 3085 -418 30 992 A C ATOM 679 O LYS A 88 -3.276 4.117 -11.291 1.00 20.36 A O ANISOU 679 O LYS A 88 2165 2132 3439 -463 50 1040 A O ATOM 680 CB LYS A 88 -3.174 2.555 -8.768 1.00 14.97 A C ANISOU 680 CB LYS A 88 1496 1446 2745 -493 -18 783 A C ATOM 681 CG LYS A 88 -2.980 1.351 -7.869 1.00 16.33 A C ANISOU 681 CG LYS A 88 1668 1704 2833 -476 -46 659 A C ATOM 682 CD LYS A 88 -2.014 1.599 -6.725 1.00 17.26 A C ANISOU 682 CD LYS A 88 1763 1781 3015 -555 -86 578 A C ATOM 683 CE LYS A 88 -2.231 2.938 -6.047 1.00 23.24 A C ANISOU 683 CE LYS A 88 2563 2372 3896 -608 -108 537 A C ATOM 684 NZ LYS A 88 -1.466 3.000 -4.755 1.00 31.73 A N ANISOU 684 NZ LYS A 88 3637 3433 4986 -679 -161 419 A N ATOM 685 N LEU A 89 -5.500 3.819 -11.146 1.00 16.06 A N ANISOU 685 N LEU A 89 1682 1558 2862 -357 22 1032 A N ATOM 686 CA LEU A 89 -5.836 4.970 -11.973 1.00 17.31 A C ANISOU 686 CA LEU A 89 1840 1666 3070 -336 36 1134 A C ATOM 687 C LEU A 89 -6.165 6.127 -11.048 1.00 18.58 A C ANISOU 687 C LEU A 89 2033 1648 3379 -338 31 1079 A C ATOM 688 O LEU A 89 -7.157 6.081 -10.320 1.00 19.35 A O ANISOU 688 O LEU A 89 2163 1685 3506 -290 18 1016 A O ATOM 689 CB LEU A 89 -7.031 4.672 -12.870 1.00 17.56 A C ANISOU 689 CB LEU A 89 1875 1780 3016 -265 26 1212 A C ATOM 690 CG LEU A 89 -6.878 3.436 -13.741 1.00 18.39 A C ANISOU 690 CG LEU A 89 1970 2064 2954 -261 30 1238 A C ATOM 691 CD1 LEU A 89 -8.129 3.149 -14.563 1.00 20.63 A C ANISOU 691 CD1 LEU A 89 2260 2433 3145 -204 4 1296 A C ATOM 692 CD2 LEU A 89 -5.670 3.619 -14.643 1.00 19.39 A C ANISOU 692 CD2 LEU A 89 2068 2254 3045 -305 70 1302 A C ATOM 693 N LYS A 90 -5.338 7.151 -11.036 1.00 19.20 A N ANISOU 693 N LYS A 90 2107 1642 3548 -394 45 1094 A N ATOM 694 CA LYS A 90 -5.710 8.320 -10.255 1.00 20.48 A C ANISOU 694 CA LYS A 90 2312 1628 3842 -394 48 1039 A C ATOM 695 C LYS A 90 -6.701 9.178 -11.008 1.00 23.10 A C ANISOU 695 C LYS A 90 2647 1912 4220 -325 67 1146 A C ATOM 696 O LYS A 90 -6.495 9.500 -12.176 1.00 27.15 A O ANISOU 696 O LYS A 90 3124 2481 4712 -324 80 1276 A O ATOM 697 CB LYS A 90 -4.498 9.150 -9.828 1.00 25.18 A C ANISOU 697 CB LYS A 90 2910 2134 4522 -490 51 1001 A C ATOM 698 CG LYS A 90 -4.981 10.269 -8.930 1.00 28.79 A C ANISOU 698 CG LYS A 90 3433 2407 5099 -489 57 919 A C ATOM 699 CD LYS A 90 -3.914 11.145 -8.413 1.00 32.88 A C ANISOU 699 CD LYS A 90 3970 2825 5699 -592 54 866 A C ATOM 700 CE LYS A 90 -3.132 10.346 -7.405 1.00 39.24 A C ANISOU 700 CE LYS A 90 4773 3686 6450 -662 14 736 A C ATOM 701 NZ LYS A 90 -3.962 10.013 -6.196 1.00 40.91 A N ANISOU 701 NZ LYS A 90 5048 3848 6646 -626 -1 589 A N ATOM 702 N VAL A 91 -7.797 9.507 -10.340 1.00 21.28 A N ANISOU 702 N VAL A 91 2452 1587 4047 -262 71 1091 A N ATOM 703 CA VAL A 91 -8.853 10.304 -10.927 1.00 24.55 A C ANISOU 703 CA VAL A 91 2858 1955 4515 -185 88 1187 A C ATOM 704 C VAL A 91 -8.902 11.652 -10.220 1.00 25.92 A C ANISOU 704 C VAL A 91 3080 1930 4839 -191 118 1135 A C ATOM 705 O VAL A 91 -8.348 11.839 -9.133 1.00 27.20 A O ANISOU 705 O VAL A 91 3292 1997 5044 -246 120 1000 A O ATOM 706 CB VAL A 91 -10.201 9.571 -10.865 1.00 23.65 A C ANISOU 706 CB VAL A 91 2734 1911 4342 -95 75 1184 A C ATOM 707 CG1 VAL A 91 -10.060 8.256 -11.606 1.00 24.19 A C ANISOU 707 CG1 VAL A 91 2767 2171 4254 -104 44 1228 A C ATOM 708 CG2 VAL A 91 -10.607 9.317 -9.425 1.00 22.28 A C ANISOU 708 CG2 VAL A 91 2609 1655 4202 -76 81 1025 A C ATOM 709 N ASP A 92 -9.541 12.609 -10.875 1.00 27.52 A N ANISOU 709 N ASP A 92 3268 2073 5115 -139 141 1245 A N ATOM 710 CA ASP A 92 -9.569 13.966 -10.351 1.00 30.66 A C ANISOU 710 CA ASP A 92 3715 2275 5661 -143 177 1213 A C ATOM 711 C ASP A 92 -10.603 14.153 -9.251 1.00 31.28 A C ANISOU 711 C ASP A 92 3843 2250 5793 -71 202 1095 A C ATOM 712 O ASP A 92 -10.759 15.270 -8.751 1.00 33.22 A O ANISOU 712 O ASP A 92 4139 2324 6158 -62 240 1054 A O ATOM 713 CB ASP A 92 -9.822 14.966 -11.486 1.00 33.19 A C ANISOU 713 CB ASP A 92 3996 2563 6052 -112 197 1385 A C ATOM 714 CG ASP A 92 -11.190 14.791 -12.142 1.00 35.30 A C ANISOU 714 CG ASP A 92 4212 2909 6292 -4 195 1490 A C ATOM 715 OD1 ASP A 92 -12.037 14.021 -11.637 1.00 33.77 A O ANISOU 715 OD1 ASP A 92 4016 2771 6044 53 185 1424 A O ATOM 716 OD2 ASP A 92 -11.428 15.456 -13.169 1.00 40.32 A O ANISOU 716 OD2 ASP A 92 4805 3553 6963 21 201 1646 A O ATOM 717 N THR A 93 -11.321 13.098 -8.876 1.00 28.84 A N ANISOU 717 N THR A 93 3522 2038 5398 -18 188 1041 A N ATOM 718 CA THR A 93 -12.401 13.193 -7.903 1.00 30.00 A C ANISOU 718 CA THR A 93 3704 2111 5583 62 220 942 A C ATOM 719 C THR A 93 -12.269 12.090 -6.865 1.00 25.72 A C ANISOU 719 C THR A 93 3194 1625 4954 41 202 790 A C ATOM 720 O THR A 93 -12.198 10.909 -7.216 1.00 23.46 A O ANISOU 720 O THR A 93 2865 1489 4558 34 163 817 A O ATOM 721 CB THR A 93 -13.770 13.093 -8.587 1.00 28.82 A C ANISOU 721 CB THR A 93 3488 2033 5429 170 227 1061 A C ATOM 722 CG2 THR A 93 -14.889 13.452 -7.615 1.00 29.86 A C ANISOU 722 CG2 THR A 93 3649 2069 5627 259 278 974 A C ATOM 723 OG1 THR A 93 -13.804 13.964 -9.725 1.00 34.00 A O ANISOU 723 OG1 THR A 93 4100 2672 6145 181 232 1225 A O ATOM 724 N ALA A 94 -12.238 12.473 -5.591 1.00 26.01 A N ANISOU 724 N ALA A 94 3310 1541 5032 30 229 628 A N ATOM 725 CA ALA A 94 -12.313 11.484 -4.527 1.00 23.23 A C ANISOU 725 CA ALA A 94 2989 1241 4597 26 218 483 A C ATOM 726 C ALA A 94 -13.748 10.979 -4.391 1.00 25.21 A C ANISOU 726 C ALA A 94 3208 1547 4823 144 244 496 A C ATOM 727 O ALA A 94 -14.703 11.759 -4.464 1.00 25.48 A O ANISOU 727 O ALA A 94 3235 1510 4935 227 291 537 A O ATOM 728 CB ALA A 94 -11.831 12.082 -3.210 1.00 24.15 A C ANISOU 728 CB ALA A 94 3206 1227 4742 -30 236 301 A C ATOM 729 N ASN A 95 -13.895 9.674 -4.211 1.00 23.44 A N ANISOU 729 N ASN A 95 2957 1452 4496 149 214 468 A N ATOM 730 CA ASN A 95 -15.217 9.053 -4.075 1.00 22.28 A C ANISOU 730 CA ASN A 95 2771 1379 4316 250 232 484 A C ATOM 731 C ASN A 95 -15.885 9.534 -2.795 1.00 23.02 A C ANISOU 731 C ASN A 95 2926 1372 4449 304 298 344 A C ATOM 732 O ASN A 95 -15.419 9.184 -1.703 1.00 24.06 A O ANISOU 732 O ASN A 95 3123 1487 4532 262 301 189 A O ATOM 733 CB ASN A 95 -15.088 7.529 -4.058 1.00 18.72 A C ANISOU 733 CB ASN A 95 2289 1074 3748 230 184 470 A C ATOM 734 CG ASN A 95 -16.443 6.811 -4.041 1.00 18.23 A C ANISOU 734 CG ASN A 95 2174 1107 3645 323 193 504 A C ATOM 735 ND2 ASN A 95 -16.402 5.479 -4.138 1.00 17.16 A N ANISOU 735 ND2 ASN A 95 2010 1101 3411 309 148 507 A N ATOM 736 OD1 ASN A 95 -17.506 7.435 -3.924 1.00 19.26 A O ANISOU 736 OD1 ASN A 95 2287 1198 3834 403 240 527 A O ATOM 737 N PRO A 96 -16.973 10.306 -2.865 1.00 26.01 A N ANISOU 737 N PRO A 96 3285 1692 4905 397 352 392 A N ATOM 738 CA PRO A 96 -17.611 10.775 -1.626 1.00 25.11 A C ANISOU 738 CA PRO A 96 3234 1486 4821 454 424 256 A C ATOM 739 C PRO A 96 -18.222 9.651 -0.815 1.00 22.63 A C ANISOU 739 C PRO A 96 2912 1276 4411 492 436 173 A C ATOM 740 O PRO A 96 -18.530 9.850 0.366 1.00 26.36 A O ANISOU 740 O PRO A 96 3448 1695 4871 519 493 33 A O ATOM 741 CB PRO A 96 -18.673 11.758 -2.131 1.00 25.43 A C ANISOU 741 CB PRO A 96 3230 1461 4974 549 476 366 A C ATOM 742 CG PRO A 96 -19.004 11.267 -3.505 1.00 26.17 A C ANISOU 742 CG PRO A 96 3212 1684 5045 562 421 555 A C ATOM 743 CD PRO A 96 -17.703 10.747 -4.069 1.00 23.48 A C ANISOU 743 CD PRO A 96 2881 1400 4640 454 349 575 A C ATOM 744 N LYS A 97 -18.370 8.466 -1.393 1.00 21.05 A N ANISOU 744 N LYS A 97 2638 1226 4134 489 383 252 A N ATOM 745 CA LYS A 97 -18.901 7.322 -0.676 1.00 23.04 A C ANISOU 745 CA LYS A 97 2876 1582 4296 518 390 184 A C ATOM 746 C LYS A 97 -17.811 6.393 -0.159 1.00 20.00 A C ANISOU 746 C LYS A 97 2537 1243 3819 431 346 79 A C ATOM 747 O LYS A 97 -18.115 5.259 0.217 1.00 19.20 A O ANISOU 747 O LYS A 97 2412 1246 3637 445 337 48 A O ATOM 748 CB LYS A 97 -19.873 6.550 -1.565 1.00 19.60 A C ANISOU 748 CB LYS A 97 2329 1286 3832 569 358 331 A C ATOM 749 CG LYS A 97 -21.160 7.300 -1.864 1.00 22.45 A C ANISOU 749 CG LYS A 97 2632 1626 4274 660 404 423 A C ATOM 750 CD LYS A 97 -22.037 6.491 -2.811 1.00 27.03 A C ANISOU 750 CD LYS A 97 3100 2362 4808 681 352 567 A C ATOM 751 CE LYS A 97 -22.702 7.348 -3.866 1.00 28.74 A C ANISOU 751 CE LYS A 97 3248 2567 5104 719 347 723 A C ATOM 752 NZ LYS A 97 -23.292 6.477 -4.930 1.00 33.96 A N ANISOU 752 NZ LYS A 97 3813 3397 5691 703 271 856 A N ATOM 753 N THR A 98 -16.557 6.847 -0.114 1.00 19.67 A N ANISOU 753 N THR A 98 2555 1129 3791 337 317 26 A N ATOM 754 CA THR A 98 -15.485 5.965 0.346 1.00 17.73 A C ANISOU 754 CA THR A 98 2340 936 3461 245 266 -67 A C ATOM 755 C THR A 98 -15.745 5.534 1.787 1.00 20.91 A C ANISOU 755 C THR A 98 2802 1359 3783 256 303 -235 A C ATOM 756 O THR A 98 -15.836 6.396 2.681 1.00 20.38 A O ANISOU 756 O THR A 98 2813 1206 3726 259 351 -345 A O ATOM 757 CB THR A 98 -14.121 6.643 0.236 1.00 18.33 A C ANISOU 757 CB THR A 98 2461 938 3566 132 227 -96 A C ATOM 758 CG2 THR A 98 -12.999 5.668 0.608 1.00 17.00 A C ANISOU 758 CG2 THR A 98 2299 870 3292 30 158 -168 A C ATOM 759 OG1 THR A 98 -13.914 7.059 -1.113 1.00 18.29 A O ANISOU 759 OG1 THR A 98 2398 926 3623 126 203 69 A O ATOM 760 N PRO A 99 -15.910 4.246 2.054 1.00 20.11 A N ANISOU 760 N PRO A 99 2670 1418 3555 255 273 -248 A N ATOM 761 CA PRO A 99 -16.077 3.798 3.433 1.00 19.43 A C ANISOU 761 CA PRO A 99 2640 1377 3367 256 303 -395 A C ATOM 762 C PRO A 99 -14.723 3.795 4.112 1.00 20.15 A C ANISOU 762 C PRO A 99 2799 1474 3383 135 247 -511 A C ATOM 763 O PRO A 99 -13.672 3.864 3.461 1.00 17.95 A O ANISOU 763 O PRO A 99 2502 1197 3119 54 179 -463 A O ATOM 764 CB PRO A 99 -16.598 2.367 3.276 1.00 17.09 A C ANISOU 764 CB PRO A 99 2273 1263 2958 280 272 -331 A C ATOM 765 CG PRO A 99 -15.839 1.888 2.094 1.00 17.72 A C ANISOU 765 CG PRO A 99 2299 1411 3022 222 188 -221 A C ATOM 766 CD PRO A 99 -15.753 3.096 1.144 1.00 18.89 A C ANISOU 766 CD PRO A 99 2438 1425 3315 233 200 -136 A C ATOM 767 N LYS A 100 -14.748 3.679 5.431 1.00 17.90 A N ANISOU 767 N LYS A 100 2586 1206 3010 122 273 -657 A N ATOM 768 CA LYS A 100 -13.509 3.343 6.105 1.00 18.80 A C ANISOU 768 CA LYS A 100 2742 1384 3016 4 197 -747 A C ATOM 769 C LYS A 100 -13.074 1.970 5.613 1.00 20.01 A C ANISOU 769 C LYS A 100 2816 1713 3075 -21 119 -650 A C ATOM 770 O LYS A 100 -13.890 1.054 5.522 1.00 16.12 A O ANISOU 770 O LYS A 100 2277 1318 2530 46 137 -593 A O ATOM 771 CB LYS A 100 -13.702 3.354 7.615 1.00 25.47 A C ANISOU 771 CB LYS A 100 3678 2245 3756 -3 236 -911 A C ATOM 772 CG LYS A 100 -12.397 3.105 8.345 1.00 28.81 A C ANISOU 772 CG LYS A 100 4141 2740 4064 -132 142 -995 A C ATOM 773 CD LYS A 100 -12.525 3.160 9.864 1.00 36.55 A C ANISOU 773 CD LYS A 100 5214 3776 4899 -141 154 -1116 A C ATOM 774 CE LYS A 100 -11.130 3.005 10.488 1.00 31.27 A C ANISOU 774 CE LYS A 100 4570 3184 4127 -273 37 -1163 A C ATOM 775 NZ LYS A 100 -10.566 1.640 10.251 1.00 34.29 A N ANISOU 775 NZ LYS A 100 4870 3725 4434 -311 -34 -1097 A N ATOM 776 N TYR A 101 -11.809 1.827 5.222 1.00 14.77 A N ANISOU 776 N TYR A 101 2131 1082 2401 -115 37 -622 A N ATOM 777 CA TYR A 101 -11.444 0.554 4.622 1.00 14.42 A C ANISOU 777 CA TYR A 101 2010 1184 2286 -122 -19 -523 A C ATOM 778 C TYR A 101 -10.014 0.185 4.977 1.00 15.74 A C ANISOU 778 C TYR A 101 2170 1421 2389 -225 -101 -551 A C ATOM 779 O TYR A 101 -9.215 1.013 5.426 1.00 14.62 A O ANISOU 779 O TYR A 101 2069 1211 2274 -308 -129 -625 A O ATOM 780 CB TYR A 101 -11.585 0.568 3.091 1.00 13.45 A C ANISOU 780 CB TYR A 101 1818 1050 2245 -91 -21 -380 A C ATOM 781 CG TYR A 101 -10.559 1.423 2.388 1.00 15.97 A C ANISOU 781 CG TYR A 101 2127 1288 2651 -162 -49 -341 A C ATOM 782 CD1 TYR A 101 -10.785 2.770 2.152 1.00 16.32 A C ANISOU 782 CD1 TYR A 101 2205 1173 2824 -156 -9 -342 A C ATOM 783 CD2 TYR A 101 -9.374 0.858 1.911 1.00 17.42 A C ANISOU 783 CD2 TYR A 101 2263 1556 2800 -230 -110 -290 A C ATOM 784 CE1 TYR A 101 -9.843 3.545 1.498 1.00 18.46 A C ANISOU 784 CE1 TYR A 101 2464 1368 3184 -228 -33 -293 A C ATOM 785 CE2 TYR A 101 -8.436 1.629 1.253 1.00 15.51 A C ANISOU 785 CE2 TYR A 101 2001 1249 2641 -298 -129 -243 A C ATOM 786 CZ TYR A 101 -8.676 2.964 1.055 1.00 17.22 A C ANISOU 786 CZ TYR A 101 2253 1307 2982 -302 -94 -243 A C ATOM 787 OH TYR A 101 -7.736 3.742 0.407 1.00 21.20 A O ANISOU 787 OH TYR A 101 2736 1742 3578 -377 -111 -185 A O ATOM 788 N LYS A 102 -9.705 -1.087 4.723 1.00 16.18 A N ANISOU 788 N LYS A 102 2168 1611 2369 -221 -140 -485 A N ATOM 789 CA LYS A 102 -8.362 -1.645 4.814 1.00 13.55 A C ANISOU 789 CA LYS A 102 1797 1363 1990 -298 -215 -469 A C ATOM 790 C LYS A 102 -8.178 -2.645 3.685 1.00 12.99 A C ANISOU 790 C LYS A 102 1650 1369 1917 -266 -223 -349 A C ATOM 791 O LYS A 102 -9.126 -3.297 3.258 1.00 11.91 A O ANISOU 791 O LYS A 102 1500 1262 1762 -194 -188 -304 A O ATOM 792 CB LYS A 102 -8.136 -2.386 6.128 1.00 15.70 A C ANISOU 792 CB LYS A 102 2091 1735 2137 -321 -250 -537 A C ATOM 793 CG LYS A 102 -8.301 -1.550 7.373 1.00 22.28 A C ANISOU 793 CG LYS A 102 3014 2519 2933 -358 -243 -674 A C ATOM 794 CD LYS A 102 -7.868 -2.371 8.565 1.00 24.92 A C ANISOU 794 CD LYS A 102 3359 2983 3127 -394 -296 -716 A C ATOM 795 CE LYS A 102 -8.861 -3.476 8.808 1.00 24.63 A C ANISOU 795 CE LYS A 102 3314 3028 3017 -306 -251 -677 A C ATOM 796 NZ LYS A 102 -8.249 -4.591 9.589 1.00 33.53 A N ANISOU 796 NZ LYS A 102 4416 4297 4027 -332 -313 -653 A N ATOM 797 N PHE A 103 -6.939 -2.786 3.232 1.00 12.82 A N ANISOU 797 N PHE A 103 1577 1383 1912 -324 -267 -301 A N ATOM 798 CA PHE A 103 -6.552 -3.865 2.331 1.00 9.93 A C ANISOU 798 CA PHE A 103 1145 1102 1525 -298 -270 -207 A C ATOM 799 C PHE A 103 -5.907 -4.971 3.168 1.00 11.57 A C ANISOU 799 C PHE A 103 1328 1417 1650 -310 -313 -219 A C ATOM 800 O PHE A 103 -4.815 -4.784 3.723 1.00 11.97 A O ANISOU 800 O PHE A 103 1354 1496 1698 -379 -366 -236 A O ATOM 801 CB PHE A 103 -5.553 -3.374 1.283 1.00 10.34 A C ANISOU 801 CB PHE A 103 1145 1133 1650 -343 -276 -135 A C ATOM 802 CG PHE A 103 -6.122 -2.439 0.277 1.00 10.80 A C ANISOU 802 CG PHE A 103 1216 1101 1788 -325 -235 -88 A C ATOM 803 CD1 PHE A 103 -7.490 -2.318 0.116 1.00 10.14 A C ANISOU 803 CD1 PHE A 103 1170 978 1706 -256 -195 -90 A C ATOM 804 CD2 PHE A 103 -5.286 -1.719 -0.560 1.00 11.26 A C ANISOU 804 CD2 PHE A 103 1237 1121 1920 -375 -234 -22 A C ATOM 805 CE1 PHE A 103 -8.012 -1.474 -0.835 1.00 11.70 A C ANISOU 805 CE1 PHE A 103 1368 1099 1979 -234 -163 -26 A C ATOM 806 CE2 PHE A 103 -5.810 -0.872 -1.522 1.00 12.06 A C ANISOU 806 CE2 PHE A 103 1347 1143 2093 -356 -196 42 A C ATOM 807 CZ PHE A 103 -7.168 -0.743 -1.655 1.00 11.02 A C ANISOU 807 CZ PHE A 103 1253 972 1963 -284 -164 42 A C ATOM 808 N VAL A 104 -6.563 -6.118 3.243 1.00 8.99 A N ANISOU 808 N VAL A 104 1001 1150 1264 -248 -294 -200 A N ATOM 809 CA VAL A 104 -6.084 -7.226 4.056 1.00 11.11 A C ANISOU 809 CA VAL A 104 1249 1513 1461 -247 -328 -195 A C ATOM 810 C VAL A 104 -5.951 -8.405 3.117 1.00 12.25 A C ANISOU 810 C VAL A 104 1349 1699 1608 -199 -304 -116 A C ATOM 811 O VAL A 104 -6.711 -8.540 2.156 1.00 18.81 A O ANISOU 811 O VAL A 104 2189 2500 2457 -159 -261 -91 A O ATOM 812 CB VAL A 104 -7.030 -7.575 5.225 1.00 9.76 A C ANISOU 812 CB VAL A 104 1131 1367 1212 -220 -320 -251 A C ATOM 813 CG1 VAL A 104 -7.257 -6.333 6.125 1.00 13.65 A C ANISOU 813 CG1 VAL A 104 1686 1805 1694 -263 -325 -350 A C ATOM 814 CG2 VAL A 104 -8.318 -8.120 4.713 1.00 15.68 A C ANISOU 814 CG2 VAL A 104 1894 2102 1961 -151 -264 -226 A C ATOM 815 N ARG A 105 -4.977 -9.259 3.381 1.00 9.85 A N ANISOU 815 N ARG A 105 994 1463 1285 -203 -332 -78 A N ATOM 816 CA ARG A 105 -4.866 -10.506 2.643 1.00 7.74 A C ANISOU 816 CA ARG A 105 697 1225 1020 -150 -299 -17 A C ATOM 817 C ARG A 105 -5.362 -11.609 3.556 1.00 8.95 A C ANISOU 817 C ARG A 105 867 1419 1114 -115 -305 -17 A C ATOM 818 O ARG A 105 -4.962 -11.660 4.716 1.00 11.07 A O ANISOU 818 O ARG A 105 1129 1736 1343 -138 -351 -26 A O ATOM 819 CB ARG A 105 -3.412 -10.766 2.241 1.00 8.46 A C ANISOU 819 CB ARG A 105 709 1355 1150 -163 -310 41 A C ATOM 820 CG ARG A 105 -3.266 -11.968 1.316 1.00 7.81 A C ANISOU 820 CG ARG A 105 604 1284 1077 -100 -256 93 A C ATOM 821 CD ARG A 105 -1.786 -12.075 0.896 1.00 8.41 A C ANISOU 821 CD ARG A 105 593 1398 1204 -106 -251 154 A C ATOM 822 NE ARG A 105 -1.542 -13.311 0.160 1.00 9.31 A N ANISOU 822 NE ARG A 105 689 1520 1328 -38 -189 193 A N ATOM 823 CZ ARG A 105 -1.556 -13.399 -1.159 1.00 8.21 A C ANISOU 823 CZ ARG A 105 561 1360 1200 -14 -122 202 A C ATOM 824 NH1 ARG A 105 -1.801 -12.312 -1.871 1.00 8.15 A N ANISOU 824 NH1 ARG A 105 570 1329 1196 -54 -115 192 A N ATOM 825 NH2 ARG A 105 -1.326 -14.563 -1.772 1.00 8.32 A N ANISOU 825 NH2 ARG A 105 571 1373 1217 48 -58 221 A N ATOM 826 N ILE A 106 -6.242 -12.473 3.046 1.00 10.27 A N ANISOU 826 N ILE A 106 1058 1570 1273 -66 -261 -4 A N ATOM 827 CA ILE A 106 -6.729 -13.563 3.880 1.00 11.47 A C ANISOU 827 CA ILE A 106 1224 1753 1382 -37 -261 9 A C ATOM 828 C ILE A 106 -5.926 -14.835 3.659 1.00 9.80 A C ANISOU 828 C ILE A 106 972 1562 1190 -2 -251 71 A C ATOM 829 O ILE A 106 -5.149 -14.951 2.706 1.00 12.47 A O ANISOU 829 O ILE A 106 1276 1890 1573 9 -230 97 A O ATOM 830 CB ILE A 106 -8.228 -13.820 3.644 1.00 10.96 A C ANISOU 830 CB ILE A 106 1205 1657 1304 -14 -224 -10 A C ATOM 831 CG1 ILE A 106 -8.468 -14.197 2.183 1.00 8.92 A C ANISOU 831 CG1 ILE A 106 947 1362 1080 3 -188 7 A C ATOM 832 CG2 ILE A 106 -9.071 -12.645 4.143 1.00 15.36 A C ANISOU 832 CG2 ILE A 106 1796 2194 1845 -31 -224 -65 A C ATOM 833 CD1 ILE A 106 -9.895 -14.698 1.894 1.00 14.30 A C ANISOU 833 CD1 ILE A 106 1658 2023 1751 17 -164 1 A C ATOM 834 N GLN A 107 -6.100 -15.786 4.557 1.00 9.06 A N ANISOU 834 N GLN A 107 880 1497 1066 20 -260 101 A N ATOM 835 CA GLN A 107 -5.601 -17.149 4.656 1.00 11.38 A C ANISOU 835 CA GLN A 107 1144 1797 1381 65 -246 168 A C ATOM 836 C GLN A 107 -6.577 -18.104 3.989 1.00 10.46 A C ANISOU 836 C GLN A 107 1071 1621 1282 95 -191 164 A C ATOM 837 O GLN A 107 -7.784 -17.938 4.128 1.00 11.91 A O ANISOU 837 O GLN A 107 1297 1790 1437 80 -183 131 A O ATOM 838 CB GLN A 107 -5.439 -17.556 6.116 1.00 12.81 A C ANISOU 838 CB GLN A 107 1313 2042 1513 63 -291 211 A C ATOM 839 CG GLN A 107 -4.298 -16.867 6.803 1.00 12.70 A C ANISOU 839 CG GLN A 107 1247 2100 1478 27 -359 226 A C ATOM 840 CD GLN A 107 -2.992 -17.311 6.236 1.00 15.69 A C ANISOU 840 CD GLN A 107 1546 2486 1929 55 -357 293 A C ATOM 841 NE2 GLN A 107 -2.074 -16.372 6.016 1.00 13.26 A N ANISOU 841 NE2 GLN A 107 1190 2204 1643 12 -392 282 A N ATOM 842 OE1 GLN A 107 -2.820 -18.492 5.944 1.00 13.40 A O ANISOU 842 OE1 GLN A 107 1237 2169 1685 116 -316 353 A O ATOM 843 N PRO A 108 -6.076 -19.112 3.275 1.00 11.23 A N ANISOU 843 N PRO A 108 1156 1681 1430 136 -150 196 A N ATOM 844 CA PRO A 108 -6.934 -20.237 2.903 1.00 12.17 A C ANISOU 844 CA PRO A 108 1320 1739 1565 155 -107 193 A C ATOM 845 C PRO A 108 -7.685 -20.709 4.137 1.00 11.95 A C ANISOU 845 C PRO A 108 1305 1729 1506 150 -127 226 A C ATOM 846 O PRO A 108 -7.158 -20.691 5.251 1.00 15.45 A O ANISOU 846 O PRO A 108 1716 2229 1924 156 -164 275 A O ATOM 847 CB PRO A 108 -5.951 -21.299 2.383 1.00 11.58 A C ANISOU 847 CB PRO A 108 1223 1624 1554 209 -62 233 A C ATOM 848 CG PRO A 108 -4.594 -20.772 2.650 1.00 14.95 A C ANISOU 848 CG PRO A 108 1576 2108 1998 223 -87 275 A C ATOM 849 CD PRO A 108 -4.665 -19.309 2.900 1.00 10.63 A C ANISOU 849 CD PRO A 108 1019 1617 1404 166 -140 238 A C ATOM 850 N GLY A 109 -8.931 -21.092 3.936 1.00 9.60 A N ANISOU 850 N GLY A 109 1051 1393 1204 133 -105 203 A N ATOM 851 CA GLY A 109 -9.816 -21.433 5.022 1.00 14.02 A C ANISOU 851 CA GLY A 109 1621 1973 1731 122 -113 234 A C ATOM 852 C GLY A 109 -10.705 -20.305 5.491 1.00 16.48 A C ANISOU 852 C GLY A 109 1943 2332 1986 90 -129 192 A C ATOM 853 O GLY A 109 -11.758 -20.579 6.080 1.00 17.20 A O ANISOU 853 O GLY A 109 2046 2432 2056 79 -115 207 A O ATOM 854 N GLN A 110 -10.319 -19.052 5.258 1.00 12.95 A N ANISOU 854 N GLN A 110 1489 1910 1520 77 -150 144 A N ATOM 855 CA GLN A 110 -11.150 -17.914 5.639 1.00 12.82 A C ANISOU 855 CA GLN A 110 1488 1919 1465 56 -154 97 A C ATOM 856 C GLN A 110 -12.198 -17.590 4.579 1.00 11.00 A C ANISOU 856 C GLN A 110 1268 1646 1264 46 -132 66 A C ATOM 857 O GLN A 110 -12.077 -17.932 3.397 1.00 9.60 A O ANISOU 857 O GLN A 110 1094 1431 1124 44 -125 62 A O ATOM 858 CB GLN A 110 -10.327 -16.643 5.906 1.00 12.31 A C ANISOU 858 CB GLN A 110 1416 1883 1378 40 -187 58 A C ATOM 859 CG GLN A 110 -9.304 -16.719 7.009 1.00 16.67 A C ANISOU 859 CG GLN A 110 1951 2497 1886 34 -229 85 A C ATOM 860 CD GLN A 110 -8.732 -15.326 7.316 1.00 23.59 A C ANISOU 860 CD GLN A 110 2830 3395 2738 -3 -265 27 A C ATOM 861 NE2 GLN A 110 -9.446 -14.581 8.168 1.00 26.48 A N ANISOU 861 NE2 GLN A 110 3235 3781 3045 -19 -260 -26 A N ATOM 862 OE1 GLN A 110 -7.701 -14.911 6.785 1.00 13.14 A O ANISOU 862 OE1 GLN A 110 1475 2066 1451 -19 -291 28 A O ATOM 863 N THR A 111 -13.260 -16.937 5.025 1.00 9.13 A N ANISOU 863 N THR A 111 1037 1424 1008 41 -118 45 A N ATOM 864 CA THR A 111 -14.368 -16.626 4.137 1.00 8.92 A C ANISOU 864 CA THR A 111 1005 1371 1013 34 -104 34 A C ATOM 865 C THR A 111 -14.420 -15.130 3.887 1.00 11.48 A C ANISOU 865 C THR A 111 1329 1688 1345 38 -107 -5 A C ATOM 866 O THR A 111 -13.843 -14.333 4.635 1.00 10.32 A O ANISOU 866 O THR A 111 1194 1553 1174 40 -113 -36 A O ATOM 867 CB THR A 111 -15.705 -17.074 4.737 1.00 10.45 A C ANISOU 867 CB THR A 111 1187 1582 1202 34 -76 59 A C ATOM 868 CG2 THR A 111 -15.733 -18.576 4.863 1.00 12.02 A C ANISOU 868 CG2 THR A 111 1388 1769 1410 22 -71 105 A C ATOM 869 OG1 THR A 111 -15.828 -16.481 6.033 1.00 11.88 A O ANISOU 869 OG1 THR A 111 1374 1804 1334 50 -57 45 A O ATOM 870 N PHE A 112 -15.157 -14.770 2.837 1.00 9.63 A N ANISOU 870 N PHE A 112 1081 1431 1145 34 -105 0 A N ATOM 871 CA PHE A 112 -15.427 -13.376 2.531 1.00 10.31 A C ANISOU 871 CA PHE A 112 1162 1498 1258 46 -101 -18 A C ATOM 872 C PHE A 112 -16.644 -13.302 1.625 1.00 10.67 A C ANISOU 872 C PHE A 112 1178 1541 1337 46 -100 15 A C ATOM 873 O PHE A 112 -17.038 -14.284 0.985 1.00 11.82 A O ANISOU 873 O PHE A 112 1313 1698 1479 23 -114 41 A O ATOM 874 CB PHE A 112 -14.249 -12.707 1.840 1.00 9.96 A C ANISOU 874 CB PHE A 112 1127 1431 1226 34 -122 -30 A C ATOM 875 CG PHE A 112 -13.744 -13.446 0.630 1.00 12.21 A C ANISOU 875 CG PHE A 112 1411 1717 1512 17 -137 -7 A C ATOM 876 CD1 PHE A 112 -12.975 -14.595 0.758 1.00 12.17 A C ANISOU 876 CD1 PHE A 112 1413 1722 1488 14 -137 -3 A C ATOM 877 CD2 PHE A 112 -14.013 -12.969 -0.644 1.00 7.33 A C ANISOU 877 CD2 PHE A 112 786 1090 911 9 -144 14 A C ATOM 878 CE1 PHE A 112 -12.498 -15.255 -0.385 1.00 13.61 A C ANISOU 878 CE1 PHE A 112 1604 1898 1671 6 -135 6 A C ATOM 879 CE2 PHE A 112 -13.527 -13.614 -1.788 1.00 9.49 A C ANISOU 879 CE2 PHE A 112 1069 1372 1166 -8 -149 25 A C ATOM 880 CZ PHE A 112 -12.743 -14.744 -1.655 1.00 10.07 A C ANISOU 880 CZ PHE A 112 1157 1447 1222 -8 -138 13 A C ATOM 881 N SER A 113 -17.221 -12.108 1.567 1.00 9.88 A N ANISOU 881 N SER A 113 1062 1421 1273 71 -85 16 A N ATOM 882 CA SER A 113 -18.335 -11.835 0.690 1.00 10.05 A C ANISOU 882 CA SER A 113 1039 1446 1333 77 -91 65 A C ATOM 883 C SER A 113 -17.813 -11.309 -0.634 1.00 9.23 A C ANISOU 883 C SER A 113 938 1327 1240 62 -124 87 A C ATOM 884 O SER A 113 -16.867 -10.520 -0.669 1.00 12.32 A O ANISOU 884 O SER A 113 1355 1685 1642 66 -122 67 A O ATOM 885 CB SER A 113 -19.273 -10.805 1.327 1.00 10.41 A C ANISOU 885 CB SER A 113 1058 1474 1425 127 -47 68 A C ATOM 886 OG SER A 113 -19.690 -11.205 2.627 1.00 11.19 A O ANISOU 886 OG SER A 113 1159 1594 1498 144 -3 43 A O ATOM 887 N VAL A 114 -18.450 -11.721 -1.721 1.00 8.42 A N ANISOU 887 N VAL A 114 810 1256 1134 39 -157 134 A N ATOM 888 CA VAL A 114 -18.106 -11.250 -3.056 1.00 11.35 A C ANISOU 888 CA VAL A 114 1183 1631 1499 22 -188 168 A C ATOM 889 C VAL A 114 -19.284 -10.454 -3.587 1.00 11.87 A C ANISOU 889 C VAL A 114 1192 1709 1610 43 -203 240 A C ATOM 890 O VAL A 114 -20.424 -10.934 -3.548 1.00 10.50 A O ANISOU 890 O VAL A 114 972 1573 1446 37 -216 271 A O ATOM 891 CB VAL A 114 -17.763 -12.417 -3.997 1.00 10.04 A C ANISOU 891 CB VAL A 114 1045 1502 1270 -29 -218 160 A C ATOM 892 CG1 VAL A 114 -17.631 -11.900 -5.453 1.00 12.46 A C ANISOU 892 CG1 VAL A 114 1351 1834 1549 -48 -248 206 A C ATOM 893 CG2 VAL A 114 -16.512 -13.159 -3.528 1.00 13.59 A C ANISOU 893 CG2 VAL A 114 1540 1932 1691 -34 -195 104 A C ATOM 894 N LEU A 115 -19.019 -9.238 -4.074 1.00 9.93 A N ANISOU 894 N LEU A 115 941 1430 1403 67 -200 277 A N ATOM 895 CA LEU A 115 -20.028 -8.443 -4.772 1.00 11.22 A C ANISOU 895 CA LEU A 115 1044 1604 1614 92 -220 369 A C ATOM 896 C LEU A 115 -19.748 -8.573 -6.264 1.00 11.51 A C ANISOU 896 C LEU A 115 1087 1694 1592 47 -273 423 A C ATOM 897 O LEU A 115 -18.891 -7.883 -6.821 1.00 11.93 A O ANISOU 897 O LEU A 115 1167 1723 1644 46 -268 443 A O ATOM 898 CB LEU A 115 -20.014 -6.990 -4.313 1.00 8.81 A C ANISOU 898 CB LEU A 115 731 1216 1402 154 -174 385 A C ATOM 899 CG LEU A 115 -20.976 -6.076 -5.060 1.00 10.22 A C ANISOU 899 CG LEU A 115 841 1392 1648 194 -189 499 A C ATOM 900 CD1 LEU A 115 -22.441 -6.473 -4.777 1.00 14.49 A C ANISOU 900 CD1 LEU A 115 1302 1983 2220 219 -193 542 A C ATOM 901 CD2 LEU A 115 -20.726 -4.631 -4.635 1.00 11.11 A C ANISOU 901 CD2 LEU A 115 965 1392 1863 254 -134 503 A C ATOM 902 N ALA A 116 -20.425 -9.516 -6.901 1.00 11.02 A N ANISOU 902 N ALA A 116 1006 1709 1472 0 -324 443 A N ATOM 903 CA ALA A 116 -20.246 -9.722 -8.328 1.00 10.73 A C ANISOU 903 CA ALA A 116 983 1738 1354 -51 -377 484 A C ATOM 904 C ALA A 116 -20.781 -8.517 -9.083 1.00 14.69 A C ANISOU 904 C ALA A 116 1442 2243 1895 -24 -390 588 A C ATOM 905 O ALA A 116 -21.899 -8.054 -8.827 1.00 15.39 A O ANISOU 905 O ALA A 116 1471 2322 2052 9 -385 636 A O ATOM 906 CB ALA A 116 -20.957 -10.993 -8.790 1.00 13.57 A C ANISOU 906 CB ALA A 116 1350 2160 1645 -117 -418 455 A C ATOM 907 N CYS A 117 -19.989 -8.022 -10.026 1.00 10.24 A N ANISOU 907 N CYS A 117 909 1692 1290 -37 -396 626 A N ATOM 908 CA CYS A 117 -20.303 -6.803 -10.740 1.00 11.90 A C ANISOU 908 CA CYS A 117 1086 1892 1542 -12 -397 728 A C ATOM 909 C CYS A 117 -20.060 -6.987 -12.230 1.00 14.87 A C ANISOU 909 C CYS A 117 1491 2349 1809 -69 -430 762 A C ATOM 910 O CYS A 117 -19.184 -7.743 -12.652 1.00 14.51 A O ANISOU 910 O CYS A 117 1506 2342 1667 -112 -431 706 A O ATOM 911 CB CYS A 117 -19.458 -5.650 -10.270 1.00 15.64 A C ANISOU 911 CB CYS A 117 1565 2273 2104 41 -355 757 A C ATOM 912 SG CYS A 117 -19.835 -5.079 -8.637 1.00 20.42 A S ANISOU 912 SG CYS A 117 2141 2767 2849 118 -301 717 A S ATOM 913 N TYR A 118 -20.836 -6.257 -13.016 1.00 17.47 A N ANISOU 913 N TYR A 118 1777 2706 2157 -63 -452 856 A N ATOM 914 CA TYR A 118 -20.673 -6.197 -14.460 1.00 17.29 A C ANISOU 914 CA TYR A 118 1771 2763 2036 -110 -482 906 A C ATOM 915 C TYR A 118 -20.888 -4.753 -14.881 1.00 20.66 A C ANISOU 915 C TYR A 118 2148 3160 2542 -67 -472 1030 A C ATOM 916 O TYR A 118 -21.842 -4.111 -14.430 1.00 19.00 A O ANISOU 916 O TYR A 118 1874 2909 2435 -21 -468 1084 A O ATOM 917 CB TYR A 118 -21.646 -7.149 -15.176 1.00 17.88 A C ANISOU 917 CB TYR A 118 1840 2930 2024 -171 -540 890 A C ATOM 918 CG TYR A 118 -21.404 -8.574 -14.740 1.00 18.90 A C ANISOU 918 CG TYR A 118 2024 3068 2091 -214 -542 764 A C ATOM 919 CD1 TYR A 118 -22.061 -9.107 -13.636 1.00 18.41 A C ANISOU 919 CD1 TYR A 118 1934 2968 2094 -201 -539 719 A C ATOM 920 CD2 TYR A 118 -20.458 -9.369 -15.387 1.00 18.51 A C ANISOU 920 CD2 TYR A 118 2054 3055 1923 -261 -536 692 A C ATOM 921 CE1 TYR A 118 -21.793 -10.394 -13.195 1.00 16.67 A C ANISOU 921 CE1 TYR A 118 1762 2744 1828 -239 -537 611 A C ATOM 922 CE2 TYR A 118 -20.191 -10.651 -14.964 1.00 18.20 A C ANISOU 922 CE2 TYR A 118 2068 3007 1840 -294 -529 578 A C ATOM 923 CZ TYR A 118 -20.860 -11.164 -13.875 1.00 20.54 A C ANISOU 923 CZ TYR A 118 2333 3262 2207 -285 -533 540 A C ATOM 924 OH TYR A 118 -20.579 -12.440 -13.446 1.00 16.83 A O ANISOU 924 OH TYR A 118 1915 2776 1703 -319 -524 434 A O ATOM 925 N ASN A 119 -19.971 -4.239 -15.706 1.00 23.14 A N ANISOU 925 N ASN A 119 2491 3487 2812 -80 -459 1076 A N ATOM 926 CA ASN A 119 -20.071 -2.880 -16.246 1.00 22.04 A C ANISOU 926 CA ASN A 119 2310 3320 2744 -47 -448 1200 A C ATOM 927 C ASN A 119 -20.160 -1.840 -15.133 1.00 22.01 A C ANISOU 927 C ASN A 119 2273 3180 2909 27 -400 1222 A C ATOM 928 O ASN A 119 -20.850 -0.824 -15.267 1.00 20.71 A O ANISOU 928 O ASN A 119 2053 2978 2838 69 -394 1315 A O ATOM 929 CB ASN A 119 -21.259 -2.757 -17.198 1.00 25.08 A C ANISOU 929 CB ASN A 119 2641 3792 3096 -65 -503 1286 A C ATOM 930 CG ASN A 119 -21.234 -3.808 -18.269 1.00 25.38 A C ANISOU 930 CG ASN A 119 2721 3957 2966 -143 -553 1248 A C ATOM 931 ND2 ASN A 119 -20.229 -3.749 -19.124 1.00 25.29 A N ANISOU 931 ND2 ASN A 119 2760 3985 2862 -170 -538 1257 A N ATOM 932 OD1 ASN A 119 -22.104 -4.671 -18.326 1.00 27.41 A O ANISOU 932 OD1 ASN A 119 2968 4272 3176 -179 -599 1209 A O ATOM 933 N GLY A 120 -19.468 -2.106 -14.023 1.00 17.42 A N ANISOU 933 N GLY A 120 1728 2523 2367 44 -364 1134 A N ATOM 934 CA GLY A 120 -19.532 -1.257 -12.851 1.00 18.03 A C ANISOU 934 CA GLY A 120 1789 2465 2596 110 -316 1125 A C ATOM 935 C GLY A 120 -20.832 -1.312 -12.073 1.00 23.43 A C ANISOU 935 C GLY A 120 2424 3129 3350 156 -313 1110 A C ATOM 936 O GLY A 120 -20.998 -0.539 -11.125 1.00 21.88 A O ANISOU 936 O GLY A 120 2218 2818 3279 218 -262 1097 A O ATOM 937 N SER A 121 -21.759 -2.208 -12.423 1.00 21.65 A N ANISOU 937 N SER A 121 2171 3007 3049 125 -360 1105 A N ATOM 938 CA SER A 121 -23.047 -2.288 -11.728 1.00 16.82 A C ANISOU 938 CA SER A 121 1501 2386 2502 164 -353 1103 A C ATOM 939 C SER A 121 -23.149 -3.566 -10.902 1.00 22.10 A C ANISOU 939 C SER A 121 2189 3085 3122 141 -360 995 A C ATOM 940 O SER A 121 -23.078 -4.666 -11.473 1.00 18.94 A O ANISOU 940 O SER A 121 1814 2776 2607 71 -408 959 A O ATOM 941 CB SER A 121 -24.191 -2.224 -12.732 1.00 27.36 A C ANISOU 941 CB SER A 121 2772 3811 3813 143 -401 1202 A C ATOM 942 OG SER A 121 -24.237 -0.956 -13.348 1.00 30.82 A O ANISOU 942 OG SER A 121 3179 4214 4318 178 -388 1313 A O ATOM 943 N PRO A 122 -23.318 -3.474 -9.580 1.00 21.01 A N ANISOU 943 N PRO A 122 2044 2870 3067 196 -309 938 A N ATOM 944 CA PRO A 122 -23.464 -4.686 -8.755 1.00 17.61 A C ANISOU 944 CA PRO A 122 1624 2472 2595 174 -313 845 A C ATOM 945 C PRO A 122 -24.623 -5.560 -9.205 1.00 18.56 A C ANISOU 945 C PRO A 122 1701 2689 2663 127 -360 867 A C ATOM 946 O PRO A 122 -25.735 -5.082 -9.434 1.00 21.66 A O ANISOU 946 O PRO A 122 2026 3097 3107 151 -363 945 A O ATOM 947 CB PRO A 122 -23.699 -4.119 -7.353 1.00 20.85 A C ANISOU 947 CB PRO A 122 2018 2786 3117 256 -239 807 A C ATOM 948 CG PRO A 122 -22.851 -2.860 -7.358 1.00 24.58 A C ANISOU 948 CG PRO A 122 2522 3152 3663 297 -200 825 A C ATOM 949 CD PRO A 122 -23.076 -2.279 -8.747 1.00 20.57 A C ANISOU 949 CD PRO A 122 1992 2685 3140 274 -239 937 A C ATOM 950 N SER A 123 -24.351 -6.857 -9.300 1.00 19.79 A N ANISOU 950 N SER A 123 1894 2902 2722 59 -395 796 A N ATOM 951 CA SER A 123 -25.297 -7.877 -9.732 1.00 18.37 A C ANISOU 951 CA SER A 123 1690 2803 2487 -4 -445 797 A C ATOM 952 C SER A 123 -25.776 -8.787 -8.607 1.00 17.79 A C ANISOU 952 C SER A 123 1601 2724 2435 -7 -425 735 A C ATOM 953 O SER A 123 -26.962 -9.132 -8.559 1.00 16.70 A O ANISOU 953 O SER A 123 1404 2624 2319 -22 -441 771 A O ATOM 954 CB SER A 123 -24.647 -8.731 -10.827 1.00 23.84 A C ANISOU 954 CB SER A 123 2448 3559 3053 -89 -497 759 A C ATOM 955 OG SER A 123 -25.468 -9.821 -11.190 1.00 32.34 A O ANISOU 955 OG SER A 123 3514 4698 4075 -159 -545 741 A O ATOM 956 N GLY A 124 -24.890 -9.205 -7.711 1.00 13.82 A N ANISOU 956 N GLY A 124 1145 2180 1928 4 -391 652 A N ATOM 957 CA GLY A 124 -25.268 -10.129 -6.662 1.00 12.13 A C ANISOU 957 CA GLY A 124 918 1966 1727 -4 -370 599 A C ATOM 958 C GLY A 124 -24.177 -10.201 -5.626 1.00 15.47 A C ANISOU 958 C GLY A 124 1382 2338 2157 28 -325 526 A C ATOM 959 O GLY A 124 -23.040 -9.771 -5.851 1.00 13.12 A O ANISOU 959 O GLY A 124 1132 2011 1840 37 -323 507 A O ATOM 960 N VAL A 125 -24.536 -10.754 -4.477 1.00 11.93 A N ANISOU 960 N VAL A 125 911 1885 1737 41 -288 494 A N ATOM 961 CA VAL A 125 -23.584 -10.889 -3.390 1.00 12.62 A C ANISOU 961 CA VAL A 125 1055 1923 1818 66 -232 412 A C ATOM 962 C VAL A 125 -23.687 -12.307 -2.853 1.00 13.39 A C ANISOU 962 C VAL A 125 1169 2044 1874 13 -234 367 A C ATOM 963 O VAL A 125 -24.785 -12.879 -2.756 1.00 13.74 A O ANISOU 963 O VAL A 125 1146 2134 1941 -12 -248 410 A O ATOM 964 CB VAL A 125 -23.813 -9.827 -2.289 1.00 12.72 A C ANISOU 964 CB VAL A 125 1051 1878 1905 154 -151 404 A C ATOM 965 CG1 VAL A 125 -25.153 -9.998 -1.673 1.00 19.37 A C ANISOU 965 CG1 VAL A 125 1805 2755 2801 183 -119 450 A C ATOM 966 CG2 VAL A 125 -22.733 -9.883 -1.241 1.00 13.58 A C ANISOU 966 CG2 VAL A 125 1243 1936 1979 164 -101 304 A C ATOM 967 N TYR A 126 -22.536 -12.898 -2.562 1.00 12.64 A N ANISOU 967 N TYR A 126 1158 1919 1726 -8 -221 292 A N ATOM 968 CA TYR A 126 -22.510 -14.244 -2.012 1.00 11.84 A C ANISOU 968 CA TYR A 126 1080 1823 1596 -51 -216 257 A C ATOM 969 C TYR A 126 -21.219 -14.477 -1.239 1.00 14.11 A C ANISOU 969 C TYR A 126 1442 2068 1851 -33 -179 190 A C ATOM 970 O TYR A 126 -20.225 -13.752 -1.381 1.00 10.41 A O ANISOU 970 O TYR A 126 1012 1572 1372 -9 -172 163 A O ATOM 971 CB TYR A 126 -22.668 -15.298 -3.109 1.00 9.64 A C ANISOU 971 CB TYR A 126 814 1572 1277 -133 -280 258 A C ATOM 972 CG TYR A 126 -21.606 -15.212 -4.177 1.00 11.66 A C ANISOU 972 CG TYR A 126 1136 1820 1476 -152 -306 226 A C ATOM 973 CD1 TYR A 126 -20.412 -15.899 -4.063 1.00 16.16 A C ANISOU 973 CD1 TYR A 126 1781 2351 2008 -159 -283 161 A C ATOM 974 CD2 TYR A 126 -21.813 -14.441 -5.306 1.00 14.37 A C ANISOU 974 CD2 TYR A 126 1457 2199 1804 -159 -350 271 A C ATOM 975 CE1 TYR A 126 -19.451 -15.798 -5.046 1.00 15.96 A C ANISOU 975 CE1 TYR A 126 1807 2324 1934 -170 -293 136 A C ATOM 976 CE2 TYR A 126 -20.854 -14.334 -6.293 1.00 17.93 A C ANISOU 976 CE2 TYR A 126 1966 2652 2194 -176 -364 249 A C ATOM 977 CZ TYR A 126 -19.684 -15.016 -6.162 1.00 16.29 A C ANISOU 977 CZ TYR A 126 1832 2406 1951 -181 -331 178 A C ATOM 978 OH TYR A 126 -18.726 -14.929 -7.157 1.00 17.09 A O ANISOU 978 OH TYR A 126 1985 2516 1992 -193 -331 159 A O ATOM 979 N GLN A 127 -21.247 -15.534 -0.444 1.00 11.76 A N ANISOU 979 N GLN A 127 1158 1769 1542 -51 -159 174 A N ATOM 980 CA GLN A 127 -20.148 -15.886 0.436 1.00 15.09 A C ANISOU 980 CA GLN A 127 1634 2164 1934 -34 -130 131 A C ATOM 981 C GLN A 127 -19.265 -16.920 -0.251 1.00 14.51 A C ANISOU 981 C GLN A 127 1612 2068 1832 -74 -154 105 A C ATOM 982 O GLN A 127 -19.770 -17.830 -0.920 1.00 16.81 A O ANISOU 982 O GLN A 127 1904 2359 2125 -125 -180 112 A O ATOM 983 CB GLN A 127 -20.723 -16.412 1.757 1.00 16.44 A C ANISOU 983 CB GLN A 127 1786 2350 2108 -24 -87 147 A C ATOM 984 CG GLN A 127 -19.773 -16.456 2.856 1.00 19.12 A C ANISOU 984 CG GLN A 127 2169 2684 2412 3 -59 117 A C ATOM 985 CD GLN A 127 -19.550 -15.095 3.479 1.00 16.13 A C ANISOU 985 CD GLN A 127 1798 2306 2025 52 -30 85 A C ATOM 986 NE2 GLN A 127 -18.968 -15.093 4.674 1.00 16.85 A N ANISOU 986 NE2 GLN A 127 1921 2412 2071 69 -6 59 A N ATOM 987 OE1 GLN A 127 -19.891 -14.054 2.893 1.00 16.67 A O ANISOU 987 OE1 GLN A 127 1846 2361 2127 71 -32 84 A O ATOM 988 N CYS A 128 -17.946 -16.724 -0.150 1.00 11.51 A N ANISOU 988 N CYS A 128 1274 1668 1433 -51 -145 73 A N ATOM 989 CA CYS A 128 -16.906 -17.612 -0.664 1.00 13.27 A C ANISOU 989 CA CYS A 128 1541 1863 1636 -66 -148 48 A C ATOM 990 C CYS A 128 -15.896 -17.928 0.429 1.00 13.32 A C ANISOU 990 C CYS A 128 1564 1859 1639 -35 -125 43 A C ATOM 991 O CYS A 128 -15.708 -17.159 1.365 1.00 12.27 A O ANISOU 991 O CYS A 128 1420 1745 1499 -9 -116 43 A O ATOM 992 CB CYS A 128 -16.112 -17.000 -1.849 1.00 12.75 A C ANISOU 992 CB CYS A 128 1495 1798 1553 -67 -161 32 A C ATOM 993 SG CYS A 128 -16.908 -16.917 -3.415 1.00 24.12 A S ANISOU 993 SG CYS A 128 2933 3262 2970 -113 -198 41 A S ATOM 994 N ALA A 129 -15.195 -19.050 0.271 1.00 14.58 A N ANISOU 994 N ALA A 129 1751 1988 1801 -39 -116 38 A N ATOM 995 CA ALA A 129 -14.033 -19.354 1.087 1.00 13.00 A C ANISOU 995 CA ALA A 129 1556 1782 1600 -6 -102 48 A C ATOM 996 C ALA A 129 -12.814 -19.431 0.181 1.00 12.18 A C ANISOU 996 C ALA A 129 1467 1659 1500 7 -94 29 A C ATOM 997 O ALA A 129 -12.907 -19.928 -0.947 1.00 12.27 A O ANISOU 997 O ALA A 129 1507 1644 1513 -11 -85 5 A O ATOM 998 CB ALA A 129 -14.195 -20.673 1.837 1.00 12.91 A C ANISOU 998 CB ALA A 129 1552 1746 1606 -5 -86 82 A C ATOM 999 N MET A 130 -11.681 -18.941 0.679 1.00 11.53 A N ANISOU 999 N MET A 130 1367 1598 1418 35 -96 39 A N ATOM 1000 CA MET A 130 -10.388 -19.216 0.048 1.00 7.77 A C ANISOU 1000 CA MET A 130 888 1108 958 57 -77 39 A C ATOM 1001 C MET A 130 -10.057 -20.687 0.251 1.00 11.04 A C ANISOU 1001 C MET A 130 1314 1477 1403 82 -48 60 A C ATOM 1002 O MET A 130 -9.829 -21.131 1.380 1.00 11.79 A O ANISOU 1002 O MET A 130 1391 1581 1509 102 -55 104 A O ATOM 1003 CB MET A 130 -9.314 -18.300 0.639 1.00 10.90 A C ANISOU 1003 CB MET A 130 1244 1543 1354 69 -96 54 A C ATOM 1004 CG MET A 130 -7.923 -18.246 -0.050 1.00 14.91 A C ANISOU 1004 CG MET A 130 1725 2053 1886 89 -76 65 A C ATOM 1005 SD MET A 130 -7.907 -17.964 -1.806 1.00 16.17 A S ANISOU 1005 SD MET A 130 1910 2198 2036 79 -40 35 A S ATOM 1006 CE MET A 130 -8.406 -16.249 -1.903 1.00 8.06 A C ANISOU 1006 CE MET A 130 873 1196 993 40 -78 29 A C ATOM 1007 N ARG A 131 -10.071 -21.453 -0.835 1.00 9.81 A N ANISOU 1007 N ARG A 131 1197 1272 1259 80 -13 29 A N ATOM 1008 CA ARG A 131 -9.724 -22.861 -0.760 1.00 11.99 A C ANISOU 1008 CA ARG A 131 1495 1481 1581 109 27 41 A C ATOM 1009 C ARG A 131 -8.270 -23.021 -0.313 1.00 11.47 A C ANISOU 1009 C ARG A 131 1383 1422 1552 171 48 89 A C ATOM 1010 O ARG A 131 -7.448 -22.110 -0.488 1.00 10.95 A O ANISOU 1010 O ARG A 131 1278 1408 1475 181 40 94 A O ATOM 1011 CB ARG A 131 -9.936 -23.522 -2.124 1.00 11.04 A C ANISOU 1011 CB ARG A 131 1436 1303 1456 90 66 -23 A C ATOM 1012 CG ARG A 131 -11.386 -23.574 -2.667 1.00 13.96 A C ANISOU 1012 CG ARG A 131 1845 1666 1791 17 36 -65 A C ATOM 1013 CD ARG A 131 -12.377 -23.997 -1.610 1.00 11.92 A C ANISOU 1013 CD ARG A 131 1573 1397 1558 -8 9 -26 A C ATOM 1014 NE ARG A 131 -12.011 -25.273 -1.008 1.00 12.79 A N ANISOU 1014 NE ARG A 131 1699 1431 1731 22 45 5 A N ATOM 1015 CZ ARG A 131 -12.680 -25.825 -0.003 1.00 14.29 A C ANISOU 1015 CZ ARG A 131 1876 1604 1951 7 35 58 A C ATOM 1016 NH1 ARG A 131 -13.751 -25.212 0.470 1.00 12.49 A N ANISOU 1016 NH1 ARG A 131 1619 1435 1692 -33 -3 75 A N ATOM 1017 NH2 ARG A 131 -12.283 -26.980 0.519 1.00 15.34 A N ANISOU 1017 NH2 ARG A 131 2020 1660 2148 39 70 101 A N ATOM 1018 N PRO A 132 -7.929 -24.169 0.286 1.00 10.16 A N ANISOU 1018 N PRO A 132 1213 1206 1440 211 73 136 A N ATOM 1019 CA PRO A 132 -6.516 -24.467 0.557 1.00 11.84 A C ANISOU 1019 CA PRO A 132 1373 1422 1704 280 98 194 A C ATOM 1020 C PRO A 132 -5.617 -24.344 -0.659 1.00 12.24 A C ANISOU 1020 C PRO A 132 1421 1460 1769 310 155 156 A C ATOM 1021 O PRO A 132 -4.433 -24.016 -0.492 1.00 11.49 A O ANISOU 1021 O PRO A 132 1256 1409 1702 352 161 204 A O ATOM 1022 CB PRO A 132 -6.576 -25.905 1.089 1.00 13.77 A C ANISOU 1022 CB PRO A 132 1633 1583 2015 318 131 245 A C ATOM 1023 CG PRO A 132 -7.904 -25.933 1.825 1.00 13.56 A C ANISOU 1023 CG PRO A 132 1634 1566 1953 260 88 251 A C ATOM 1024 CD PRO A 132 -8.821 -25.189 0.878 1.00 12.56 A C ANISOU 1024 CD PRO A 132 1549 1453 1770 196 75 160 A C ATOM 1025 N ASN A 133 -6.131 -24.548 -1.883 1.00 10.82 A N ANISOU 1025 N ASN A 133 1312 1233 1565 285 197 73 A N ATOM 1026 CA ASN A 133 -5.287 -24.377 -3.062 1.00 10.03 A C ANISOU 1026 CA ASN A 133 1216 1136 1461 313 260 36 A C ATOM 1027 C ASN A 133 -5.327 -22.963 -3.625 1.00 9.15 A C ANISOU 1027 C ASN A 133 1087 1109 1282 268 226 17 A C ATOM 1028 O ASN A 133 -4.910 -22.767 -4.772 1.00 11.04 A O ANISOU 1028 O ASN A 133 1345 1357 1494 273 279 -20 A O ATOM 1029 CB ASN A 133 -5.652 -25.391 -4.150 1.00 14.20 A C ANISOU 1029 CB ASN A 133 1839 1573 1985 313 332 -47 A C ATOM 1030 CG ASN A 133 -7.070 -25.241 -4.651 1.00 10.99 A C ANISOU 1030 CG ASN A 133 1504 1165 1507 224 287 -116 A C ATOM 1031 ND2 ASN A 133 -7.483 -26.171 -5.502 1.00 15.14 A N ANISOU 1031 ND2 ASN A 133 2118 1611 2023 204 333 -196 A N ATOM 1032 OD1 ASN A 133 -7.793 -24.320 -4.271 1.00 12.35 A O ANISOU 1032 OD1 ASN A 133 1651 1403 1638 173 212 -98 A O ATOM 1033 N PHE A 134 -5.829 -21.989 -2.854 1.00 10.57 A N ANISOU 1033 N PHE A 134 1236 1346 1435 225 148 42 A N ATOM 1034 CA PHE A 134 -5.809 -20.569 -3.223 1.00 9.88 A C ANISOU 1034 CA PHE A 134 1125 1324 1306 186 114 38 A C ATOM 1035 C PHE A 134 -6.696 -20.250 -4.416 1.00 12.30 A C ANISOU 1035 C PHE A 134 1492 1630 1549 141 119 -18 A C ATOM 1036 O PHE A 134 -6.466 -19.262 -5.121 1.00 13.53 A O ANISOU 1036 O PHE A 134 1636 1829 1675 122 118 -15 A O ATOM 1037 CB PHE A 134 -4.391 -20.084 -3.509 1.00 9.84 A C ANISOU 1037 CB PHE A 134 1053 1356 1329 218 145 75 A C ATOM 1038 CG PHE A 134 -3.558 -19.947 -2.303 1.00 9.27 A C ANISOU 1038 CG PHE A 134 901 1317 1304 238 108 141 A C ATOM 1039 CD1 PHE A 134 -3.723 -18.874 -1.466 1.00 10.24 A C ANISOU 1039 CD1 PHE A 134 995 1487 1409 192 33 155 A C ATOM 1040 CD2 PHE A 134 -2.589 -20.896 -1.997 1.00 12.86 A C ANISOU 1040 CD2 PHE A 134 1310 1756 1822 304 148 190 A C ATOM 1041 CE1 PHE A 134 -2.912 -18.743 -0.317 1.00 12.36 A C ANISOU 1041 CE1 PHE A 134 1191 1799 1705 199 -14 212 A C ATOM 1042 CE2 PHE A 134 -1.795 -20.772 -0.858 1.00 16.73 A C ANISOU 1042 CE2 PHE A 134 1714 2293 2348 318 99 265 A C ATOM 1043 CZ PHE A 134 -1.963 -19.691 -0.024 1.00 14.18 A C ANISOU 1043 CZ PHE A 134 1367 2029 1990 258 12 272 A C ATOM 1044 N THR A 135 -7.698 -21.080 -4.671 1.00 12.77 A N ANISOU 1044 N THR A 135 1615 1646 1590 118 119 -60 A N ATOM 1045 CA THR A 135 -8.759 -20.742 -5.599 1.00 9.61 A C ANISOU 1045 CA THR A 135 1263 1263 1125 61 95 -102 A C ATOM 1046 C THR A 135 -10.007 -20.479 -4.782 1.00 12.18 A C ANISOU 1046 C THR A 135 1578 1596 1453 23 29 -86 A C ATOM 1047 O THR A 135 -10.068 -20.795 -3.593 1.00 10.60 A O ANISOU 1047 O THR A 135 1353 1380 1295 41 16 -57 A O ATOM 1048 CB THR A 135 -9.013 -21.870 -6.607 1.00 9.38 A C ANISOU 1048 CB THR A 135 1313 1186 1066 46 140 -170 A C ATOM 1049 CG2 THR A 135 -7.730 -22.245 -7.323 1.00 10.53 A C ANISOU 1049 CG2 THR A 135 1470 1317 1215 100 228 -189 A C ATOM 1050 OG1 THR A 135 -9.483 -23.040 -5.924 1.00 13.46 A O ANISOU 1050 OG1 THR A 135 1855 1628 1631 46 141 -181 A O ATOM 1051 N ILE A 136 -10.996 -19.899 -5.434 1.00 9.49 A N ANISOU 1051 N ILE A 136 1251 1287 1067 -25 -8 -98 A N ATOM 1052 CA ILE A 136 -12.311 -19.734 -4.837 1.00 11.68 A C ANISOU 1052 CA ILE A 136 1514 1573 1350 -59 -60 -83 A C ATOM 1053 C ILE A 136 -13.357 -20.299 -5.785 1.00 11.39 A C ANISOU 1053 C ILE A 136 1520 1535 1273 -119 -82 -118 A C ATOM 1054 O ILE A 136 -13.242 -20.196 -7.012 1.00 12.25 A O ANISOU 1054 O ILE A 136 1664 1668 1323 -143 -78 -146 A O ATOM 1055 CB ILE A 136 -12.610 -18.264 -4.470 1.00 12.94 A C ANISOU 1055 CB ILE A 136 1626 1779 1514 -56 -95 -44 A C ATOM 1056 CG1 ILE A 136 -12.841 -17.419 -5.714 1.00 12.30 A C ANISOU 1056 CG1 ILE A 136 1549 1737 1388 -81 -111 -37 A C ATOM 1057 CG2 ILE A 136 -11.500 -17.672 -3.557 1.00 10.95 A C ANISOU 1057 CG2 ILE A 136 1338 1530 1294 -14 -82 -22 A C ATOM 1058 CD1 ILE A 136 -13.414 -16.055 -5.414 1.00 12.43 A C ANISOU 1058 CD1 ILE A 136 1522 1778 1424 -78 -144 6 A C ATOM 1059 N LYS A 137 -14.365 -20.940 -5.210 1.00 13.30 A N ANISOU 1059 N LYS A 137 1759 1755 1541 -150 -106 -114 A N ATOM 1060 CA LYS A 137 -15.442 -21.519 -6.000 1.00 17.05 A C ANISOU 1060 CA LYS A 137 2263 2231 1985 -224 -141 -144 A C ATOM 1061 C LYS A 137 -16.486 -20.415 -6.116 1.00 14.91 A C ANISOU 1061 C LYS A 137 1935 2032 1699 -248 -200 -95 A C ATOM 1062 O LYS A 137 -17.406 -20.303 -5.304 1.00 17.74 A O ANISOU 1062 O LYS A 137 2243 2400 2098 -256 -222 -56 A O ATOM 1063 CB LYS A 137 -15.951 -22.786 -5.328 1.00 16.41 A C ANISOU 1063 CB LYS A 137 2198 2082 1955 -250 -134 -153 A C ATOM 1064 CG LYS A 137 -14.899 -23.897 -5.261 1.00 16.90 A C ANISOU 1064 CG LYS A 137 2317 2058 2048 -215 -70 -191 A C ATOM 1065 CD LYS A 137 -15.423 -25.139 -4.525 1.00 19.87 A C ANISOU 1065 CD LYS A 137 2707 2354 2490 -240 -61 -183 A C ATOM 1066 CE LYS A 137 -14.463 -26.325 -4.654 1.00 23.31 A C ANISOU 1066 CE LYS A 137 3206 2684 2968 -205 8 -223 A C ATOM 1067 NZ LYS A 137 -14.512 -26.952 -6.006 1.00 28.87 A N ANISOU 1067 NZ LYS A 137 3998 3343 3629 -257 24 -323 A N ATOM 1068 N GLY A 138 -16.292 -19.538 -7.101 1.00 15.02 A N ANISOU 1068 N GLY A 138 1949 2097 1658 -251 -216 -88 A N ATOM 1069 CA GLY A 138 -17.125 -18.372 -7.266 1.00 14.26 A C ANISOU 1069 CA GLY A 138 1795 2063 1561 -257 -264 -27 A C ATOM 1070 C GLY A 138 -18.184 -18.561 -8.332 1.00 17.29 A C ANISOU 1070 C GLY A 138 2179 2500 1890 -333 -328 -22 A C ATOM 1071 O GLY A 138 -18.405 -19.655 -8.854 1.00 17.04 A O ANISOU 1071 O GLY A 138 2200 2455 1821 -395 -341 -78 A O ATOM 1072 N SER A 139 -18.845 -17.454 -8.663 1.00 12.28 A N ANISOU 1072 N SER A 139 1487 1927 1253 -330 -372 49 A N ATOM 1073 CA SER A 139 -19.806 -17.400 -9.756 1.00 14.41 A C ANISOU 1073 CA SER A 139 1740 2272 1462 -399 -447 79 A C ATOM 1074 C SER A 139 -19.486 -16.130 -10.530 1.00 14.43 A C ANISOU 1074 C SER A 139 1728 2319 1437 -363 -450 141 A C ATOM 1075 O SER A 139 -19.869 -15.035 -10.113 1.00 14.20 A O ANISOU 1075 O SER A 139 1629 2293 1471 -314 -453 217 A O ATOM 1076 CB SER A 139 -21.242 -17.405 -9.248 1.00 16.46 A C ANISOU 1076 CB SER A 139 1921 2541 1792 -411 -480 132 A C ATOM 1077 OG SER A 139 -22.170 -17.361 -10.314 1.00 17.05 A O ANISOU 1077 OG SER A 139 1980 2666 1831 -455 -529 162 A O ATOM 1078 N PHE A 140 -18.804 -16.288 -11.658 1.00 16.04 A N ANISOU 1078 N PHE A 140 1997 2551 1546 -387 -441 109 A N ATOM 1079 CA PHE A 140 -18.220 -15.180 -12.403 1.00 15.61 A C ANISOU 1079 CA PHE A 140 1940 2536 1456 -358 -431 167 A C ATOM 1080 C PHE A 140 -18.396 -15.438 -13.893 1.00 17.94 A C ANISOU 1080 C PHE A 140 2281 2889 1647 -408 -452 157 A C ATOM 1081 O PHE A 140 -18.115 -16.539 -14.369 1.00 18.21 A O ANISOU 1081 O PHE A 140 2390 2917 1610 -450 -437 66 A O ATOM 1082 CB PHE A 140 -16.729 -15.033 -12.061 1.00 15.41 A C ANISOU 1082 CB PHE A 140 1951 2469 1436 -309 -355 135 A C ATOM 1083 CG PHE A 140 -16.436 -14.458 -10.689 1.00 11.81 A C ANISOU 1083 CG PHE A 140 1446 1940 1099 -242 -319 152 A C ATOM 1084 CD1 PHE A 140 -16.783 -13.154 -10.364 1.00 14.65 A C ANISOU 1084 CD1 PHE A 140 1743 2296 1525 -204 -333 234 A C ATOM 1085 CD2 PHE A 140 -15.784 -15.215 -9.730 1.00 14.71 A C ANISOU 1085 CD2 PHE A 140 1836 2243 1510 -217 -270 86 A C ATOM 1086 CE1 PHE A 140 -16.475 -12.627 -9.116 1.00 14.11 A C ANISOU 1086 CE1 PHE A 140 1647 2162 1552 -151 -298 230 A C ATOM 1087 CE2 PHE A 140 -15.493 -14.692 -8.467 1.00 14.24 A C ANISOU 1087 CE2 PHE A 140 1739 2133 1538 -165 -245 97 A C ATOM 1088 CZ PHE A 140 -15.836 -13.388 -8.167 1.00 10.92 A C ANISOU 1088 CZ PHE A 140 1268 1711 1171 -137 -258 160 A C ATOM 1089 N LEU A 141 -18.878 -14.439 -14.625 1.00 15.43 A N ANISOU 1089 N LEU A 141 1919 2623 1320 -403 -484 248 A N ATOM 1090 CA LEU A 141 -18.968 -14.497 -16.075 1.00 19.88 A C ANISOU 1090 CA LEU A 141 2522 3257 1776 -446 -506 253 A C ATOM 1091 C LEU A 141 -18.031 -13.458 -16.675 1.00 17.55 A C ANISOU 1091 C LEU A 141 2232 2990 1445 -411 -470 317 A C ATOM 1092 O LEU A 141 -17.392 -12.686 -15.962 1.00 16.69 A O ANISOU 1092 O LEU A 141 2093 2843 1405 -358 -435 360 A O ATOM 1093 CB LEU A 141 -20.413 -14.277 -16.533 1.00 16.13 A C ANISOU 1093 CB LEU A 141 1986 2830 1312 -481 -581 319 A C ATOM 1094 CG LEU A 141 -21.373 -15.209 -15.793 1.00 21.74 A C ANISOU 1094 CG LEU A 141 2674 3508 2078 -515 -611 275 A C ATOM 1095 CD1 LEU A 141 -22.809 -14.741 -15.943 1.00 25.81 A C ANISOU 1095 CD1 LEU A 141 3100 4068 2637 -531 -674 367 A C ATOM 1096 CD2 LEU A 141 -21.221 -16.652 -16.264 1.00 21.28 A C ANISOU 1096 CD2 LEU A 141 2704 3443 1937 -583 -613 155 A C ATOM 1097 N ASN A 142 -17.959 -13.429 -18.002 1.00 21.34 A N ANISOU 1097 N ASN A 142 2751 3540 1818 -444 -481 327 A N ATOM 1098 CA ASN A 142 -17.126 -12.418 -18.628 1.00 20.79 A C ANISOU 1098 CA ASN A 142 2681 3502 1717 -414 -444 403 A C ATOM 1099 C ASN A 142 -17.603 -11.041 -18.187 1.00 20.51 A C ANISOU 1099 C ASN A 142 2551 3448 1794 -371 -468 532 A C ATOM 1100 O ASN A 142 -18.806 -10.789 -18.046 1.00 19.32 A O ANISOU 1100 O ASN A 142 2339 3303 1699 -376 -525 582 A O ATOM 1101 CB ASN A 142 -17.148 -12.540 -20.146 1.00 23.53 A C ANISOU 1101 CB ASN A 142 3077 3936 1928 -457 -459 407 A C ATOM 1102 CG ASN A 142 -16.067 -11.692 -20.800 1.00 33.77 A C ANISOU 1102 CG ASN A 142 4387 5263 3180 -428 -400 471 A C ATOM 1103 ND2 ASN A 142 -16.251 -11.377 -22.082 1.00 35.10 A N ANISOU 1103 ND2 ASN A 142 4573 5515 3249 -455 -423 521 A N ATOM 1104 OD1 ASN A 142 -15.069 -11.317 -20.148 1.00 33.35 A O ANISOU 1104 OD1 ASN A 142 4327 5161 3183 -384 -335 481 A O ATOM 1105 N GLY A 143 -16.651 -10.159 -17.929 1.00 18.94 A N ANISOU 1105 N GLY A 143 2339 3219 1638 -326 -418 586 A N ATOM 1106 CA GLY A 143 -16.958 -8.832 -17.450 1.00 20.79 A C ANISOU 1106 CA GLY A 143 2496 3410 1994 -279 -426 698 A C ATOM 1107 C GLY A 143 -16.925 -8.688 -15.945 1.00 17.10 A C ANISOU 1107 C GLY A 143 1995 2853 1650 -235 -411 678 A C ATOM 1108 O GLY A 143 -17.025 -7.563 -15.445 1.00 17.68 A O ANISOU 1108 O GLY A 143 2015 2868 1833 -189 -403 757 A O ATOM 1109 N SER A 144 -16.785 -9.787 -15.210 1.00 13.72 A N ANISOU 1109 N SER A 144 1599 2405 1208 -246 -403 573 A N ATOM 1110 CA SER A 144 -16.798 -9.735 -13.758 1.00 15.53 A C ANISOU 1110 CA SER A 144 1798 2559 1542 -206 -393 549 A C ATOM 1111 C SER A 144 -15.452 -9.332 -13.171 1.00 13.87 A C ANISOU 1111 C SER A 144 1604 2284 1382 -172 -325 528 A C ATOM 1112 O SER A 144 -15.373 -9.107 -11.962 1.00 14.46 A O ANISOU 1112 O SER A 144 1657 2275 1561 -135 -301 494 A O ATOM 1113 CB SER A 144 -17.197 -11.100 -13.191 1.00 14.37 A C ANISOU 1113 CB SER A 144 1676 2409 1373 -235 -405 444 A C ATOM 1114 OG SER A 144 -16.231 -12.077 -13.576 1.00 14.88 A O ANISOU 1114 OG SER A 144 1818 2493 1344 -265 -369 358 A O ATOM 1115 N CYS A 145 -14.387 -9.261 -13.979 1.00 12.66 A N ANISOU 1115 N CYS A 145 1487 2161 1161 -186 -283 537 A N ATOM 1116 CA CYS A 145 -13.091 -8.911 -13.420 1.00 14.10 A C ANISOU 1116 CA CYS A 145 1671 2277 1410 -160 -214 513 A C ATOM 1117 C CYS A 145 -13.156 -7.563 -12.722 1.00 11.54 A C ANISOU 1117 C CYS A 145 1296 1870 1218 -126 -214 579 A C ATOM 1118 O CYS A 145 -13.855 -6.643 -13.159 1.00 14.37 A O ANISOU 1118 O CYS A 145 1622 2234 1605 -117 -247 681 A O ATOM 1119 CB CYS A 145 -12.012 -8.909 -14.495 1.00 16.29 A C ANISOU 1119 CB CYS A 145 1979 2611 1601 -178 -162 536 A C ATOM 1120 SG CYS A 145 -11.711 -10.586 -15.088 1.00 19.55 A S ANISOU 1120 SG CYS A 145 2468 3086 1873 -206 -132 419 A S ATOM 1121 N GLY A 146 -12.418 -7.456 -11.622 1.00 13.58 A N ANISOU 1121 N GLY A 146 1549 2049 1560 -107 -179 519 A N ATOM 1122 CA GLY A 146 -12.461 -6.279 -10.800 1.00 12.66 A C ANISOU 1122 CA GLY A 146 1401 1841 1569 -82 -176 548 A C ATOM 1123 C GLY A 146 -13.501 -6.300 -9.719 1.00 12.58 A C ANISOU 1123 C GLY A 146 1376 1783 1620 -51 -198 507 A C ATOM 1124 O GLY A 146 -13.466 -5.421 -8.849 1.00 12.46 A O ANISOU 1124 O GLY A 146 1349 1681 1705 -28 -183 499 A O ATOM 1125 N SER A 147 -14.428 -7.265 -9.748 1.00 10.82 A N ANISOU 1125 N SER A 147 1155 1615 1341 -54 -229 479 A N ATOM 1126 CA SER A 147 -15.290 -7.521 -8.602 1.00 10.84 A C ANISOU 1126 CA SER A 147 1141 1583 1393 -28 -236 430 A C ATOM 1127 C SER A 147 -14.417 -7.879 -7.410 1.00 11.24 A C ANISOU 1127 C SER A 147 1215 1586 1467 -23 -201 337 A C ATOM 1128 O SER A 147 -13.366 -8.532 -7.556 1.00 8.89 A O ANISOU 1128 O SER A 147 944 1309 1125 -45 -184 298 A O ATOM 1129 CB SER A 147 -16.246 -8.672 -8.904 1.00 9.28 A C ANISOU 1129 CB SER A 147 941 1458 1126 -50 -274 415 A C ATOM 1130 OG SER A 147 -17.048 -8.394 -10.048 1.00 12.51 A O ANISOU 1130 OG SER A 147 1323 1931 1498 -66 -321 506 A O ATOM 1131 N VAL A 148 -14.820 -7.421 -6.229 1.00 9.00 A N ANISOU 1131 N VAL A 148 922 1244 1254 7 -189 305 A N ATOM 1132 CA VAL A 148 -13.984 -7.578 -5.055 1.00 8.08 A C ANISOU 1132 CA VAL A 148 827 1090 1152 6 -166 226 A C ATOM 1133 C VAL A 148 -14.673 -8.470 -4.037 1.00 10.41 A C ANISOU 1133 C VAL A 148 1124 1401 1429 20 -164 172 A C ATOM 1134 O VAL A 148 -15.902 -8.626 -4.009 1.00 10.24 A O ANISOU 1134 O VAL A 148 1079 1397 1416 38 -171 194 A O ATOM 1135 CB VAL A 148 -13.601 -6.230 -4.405 1.00 9.06 A C ANISOU 1135 CB VAL A 148 954 1129 1360 16 -146 217 A C ATOM 1136 CG1 VAL A 148 -12.683 -5.429 -5.343 1.00 9.11 A C ANISOU 1136 CG1 VAL A 148 957 1114 1391 -10 -144 275 A C ATOM 1137 CG2 VAL A 148 -14.843 -5.437 -4.067 1.00 10.35 A C ANISOU 1137 CG2 VAL A 148 1100 1244 1589 62 -134 239 A C ATOM 1138 N GLY A 149 -13.837 -9.062 -3.199 1.00 10.50 A N ANISOU 1138 N GLY A 149 1157 1414 1419 10 -155 113 A N ATOM 1139 CA GLY A 149 -14.278 -9.797 -2.036 1.00 8.00 A C ANISOU 1139 CA GLY A 149 846 1109 1086 22 -148 67 A C ATOM 1140 C GLY A 149 -13.872 -9.011 -0.806 1.00 8.84 A C ANISOU 1140 C GLY A 149 966 1172 1218 30 -132 18 A C ATOM 1141 O GLY A 149 -12.885 -8.280 -0.818 1.00 8.07 A O ANISOU 1141 O GLY A 149 878 1045 1144 11 -136 7 A O ATOM 1142 N PHE A 150 -14.633 -9.171 0.271 1.00 8.37 A N ANISOU 1142 N PHE A 150 911 1117 1152 53 -114 -13 A N ATOM 1143 CA PHE A 150 -14.456 -8.287 1.404 1.00 8.17 A C ANISOU 1143 CA PHE A 150 911 1051 1140 61 -93 -71 A C ATOM 1144 C PHE A 150 -15.121 -8.880 2.633 1.00 11.30 A C ANISOU 1144 C PHE A 150 1317 1482 1493 80 -68 -104 A C ATOM 1145 O PHE A 150 -16.016 -9.720 2.537 1.00 10.27 A O ANISOU 1145 O PHE A 150 1161 1389 1350 94 -60 -70 A O ATOM 1146 CB PHE A 150 -15.058 -6.911 1.105 1.00 11.05 A C ANISOU 1146 CB PHE A 150 1273 1344 1581 89 -68 -60 A C ATOM 1147 CG PHE A 150 -16.550 -6.942 0.938 1.00 10.76 A C ANISOU 1147 CG PHE A 150 1200 1314 1573 137 -41 -18 A C ATOM 1148 CD1 PHE A 150 -17.111 -7.229 -0.311 1.00 9.42 A C ANISOU 1148 CD1 PHE A 150 987 1174 1417 138 -66 64 A C ATOM 1149 CD2 PHE A 150 -17.398 -6.693 2.019 1.00 9.56 A C ANISOU 1149 CD2 PHE A 150 1053 1150 1428 178 11 -58 A C ATOM 1150 CE1 PHE A 150 -18.510 -7.274 -0.491 1.00 11.28 A C ANISOU 1150 CE1 PHE A 150 1172 1430 1684 175 -53 116 A C ATOM 1151 CE2 PHE A 150 -18.790 -6.735 1.852 1.00 11.41 A C ANISOU 1151 CE2 PHE A 150 1235 1399 1701 226 40 -5 A C ATOM 1152 CZ PHE A 150 -19.346 -7.020 0.595 1.00 13.16 A C ANISOU 1152 CZ PHE A 150 1400 1652 1946 222 2 86 A C ATOM 1153 N ASN A 151 -14.709 -8.367 3.781 1.00 10.87 A N ANISOU 1153 N ASN A 151 1300 1416 1415 74 -57 -171 A N ATOM 1154 CA ASN A 151 -15.378 -8.585 5.054 1.00 13.93 A C ANISOU 1154 CA ASN A 151 1707 1833 1754 96 -18 -210 A C ATOM 1155 C ASN A 151 -15.667 -7.216 5.647 1.00 13.38 A C ANISOU 1155 C ASN A 151 1675 1696 1713 117 26 -279 A C ATOM 1156 O ASN A 151 -15.057 -6.224 5.264 1.00 13.22 A O ANISOU 1156 O ASN A 151 1673 1607 1743 98 12 -303 A O ATOM 1157 CB ASN A 151 -14.502 -9.413 5.987 1.00 12.94 A C ANISOU 1157 CB ASN A 151 1602 1772 1543 63 -49 -231 A C ATOM 1158 CG ASN A 151 -14.450 -10.870 5.606 1.00 14.79 A C ANISOU 1158 CG ASN A 151 1805 2058 1758 58 -70 -166 A C ATOM 1159 ND2 ASN A 151 -15.463 -11.617 6.011 1.00 15.11 A N ANISOU 1159 ND2 ASN A 151 1831 2132 1777 80 -38 -138 A N ATOM 1160 OD1 ASN A 151 -13.459 -11.346 5.060 1.00 14.35 A O ANISOU 1160 OD1 ASN A 151 1739 2010 1705 34 -110 -141 A O ATOM 1161 N ILE A 152 -16.616 -7.145 6.571 1.00 12.67 A N ANISOU 1161 N ILE A 152 1597 1619 1597 157 88 -312 A N ATOM 1162 CA ILE A 152 -16.937 -5.887 7.232 1.00 16.54 A C ANISOU 1162 CA ILE A 152 2135 2037 2112 186 148 -393 A C ATOM 1163 C ILE A 152 -16.784 -6.095 8.726 1.00 24.40 A C ANISOU 1163 C ILE A 152 3189 3089 2994 172 172 -476 A C ATOM 1164 O ILE A 152 -17.288 -7.081 9.273 1.00 21.48 A O ANISOU 1164 O ILE A 152 2800 2805 2556 185 190 -443 A O ATOM 1165 CB ILE A 152 -18.348 -5.383 6.882 1.00 17.72 A C ANISOU 1165 CB ILE A 152 2243 2143 2348 265 222 -355 A C ATOM 1166 CG1 ILE A 152 -18.462 -5.101 5.377 1.00 13.84 A C ANISOU 1166 CG1 ILE A 152 1695 1606 1957 272 186 -264 A C ATOM 1167 CG2 ILE A 152 -18.640 -4.110 7.662 1.00 20.75 A C ANISOU 1167 CG2 ILE A 152 2686 2438 2760 304 302 -452 A C ATOM 1168 CD1 ILE A 152 -19.746 -4.346 4.978 1.00 20.28 A C ANISOU 1168 CD1 ILE A 152 2462 2367 2878 353 250 -215 A C ATOM 1169 N ASP A 153 -16.071 -5.177 9.375 1.00 26.72 A N ANISOU 1169 N ASP A 153 3555 3336 3261 137 168 -579 A N ATOM 1170 CA ASP A 153 -15.773 -5.246 10.803 1.00 32.39 A C ANISOU 1170 CA ASP A 153 4342 4114 3849 107 177 -670 A C ATOM 1171 C ASP A 153 -16.194 -3.911 11.395 1.00 35.97 A C ANISOU 1171 C ASP A 153 4871 4472 4322 133 257 -790 A C ATOM 1172 O ASP A 153 -15.568 -2.882 11.120 1.00 33.75 A O ANISOU 1172 O ASP A 153 4630 4090 4105 97 235 -850 A O ATOM 1173 CB ASP A 153 -14.289 -5.521 11.047 1.00 32.49 A C ANISOU 1173 CB ASP A 153 4374 4177 3795 16 73 -686 A C ATOM 1174 CG ASP A 153 -14.006 -6.023 12.444 1.00 44.69 A C ANISOU 1174 CG ASP A 153 5966 5831 5181 -17 60 -735 A C ATOM 1175 OD1 ASP A 153 -14.961 -6.445 13.132 1.00 43.96 A O ANISOU 1175 OD1 ASP A 153 5884 5794 5025 32 132 -733 A O ATOM 1176 OD2 ASP A 153 -12.819 -6.004 12.852 1.00 48.67 A O ANISOU 1176 OD2 ASP A 153 6492 6376 5623 -95 -25 -766 A O ATOM 1177 N TYR A 154 -17.247 -3.943 12.208 1.00 38.50 A N ANISOU 1177 N TYR A 154 5212 4821 4595 195 356 -824 A N ATOM 1178 CA TYR A 154 -18.058 -2.780 12.538 1.00 44.42 A C ANISOU 1178 CA TYR A 154 6011 5466 5401 261 470 -912 A C ATOM 1179 C TYR A 154 -18.364 -1.948 11.296 1.00 43.65 A C ANISOU 1179 C TYR A 154 5868 5232 5486 306 483 -860 A C ATOM 1180 O TYR A 154 -19.240 -2.315 10.509 1.00 44.79 A O ANISOU 1180 O TYR A 154 5919 5386 5713 369 506 -744 A O ATOM 1181 CB TYR A 154 -17.407 -1.907 13.609 1.00 44.42 A C ANISOU 1181 CB TYR A 154 6135 5429 5314 209 475 -1071 A C ATOM 1182 CG TYR A 154 -18.388 -0.851 14.076 1.00 54.15 A C ANISOU 1182 CG TYR A 154 7409 6571 6596 298 582 -1123 A C ATOM 1183 CD1 TYR A 154 -19.715 -1.189 14.326 1.00 53.60 A C ANISOU 1183 CD1 TYR A 154 7287 6547 6530 399 688 -1076 A C ATOM 1184 CD2 TYR A 154 -18.010 0.480 14.228 1.00 52.41 A C ANISOU 1184 CD2 TYR A 154 7264 6221 6428 282 577 -1212 A C ATOM 1185 CE1 TYR A 154 -20.632 -0.244 14.733 1.00 58.19 A C ANISOU 1185 CE1 TYR A 154 7886 7059 7165 485 784 -1119 A C ATOM 1186 CE2 TYR A 154 -18.928 1.441 14.637 1.00 54.65 A C ANISOU 1186 CE2 TYR A 154 7578 6423 6763 369 676 -1262 A C ATOM 1187 CZ TYR A 154 -20.238 1.071 14.888 1.00 60.28 A C ANISOU 1187 CZ TYR A 154 8233 7193 7479 473 780 -1216 A C ATOM 1188 OH TYR A 154 -21.159 2.013 15.299 1.00 60.82 A O ANISOU 1188 OH TYR A 154 8318 7187 7602 562 881 -1264 A O ATOM 1189 N ASP A 155 -17.666 -0.827 11.112 1.00 39.16 A N ANISOU 1189 N ASP A 155 5360 4539 4982 268 465 -936 A N ATOM 1190 CA ASP A 155 -17.939 0.084 10.006 1.00 38.41 A C ANISOU 1190 CA ASP A 155 5229 4304 5062 311 485 -882 A C ATOM 1191 C ASP A 155 -16.885 0.011 8.912 1.00 32.73 A C ANISOU 1191 C ASP A 155 4472 3572 4394 236 370 -804 A C ATOM 1192 O ASP A 155 -16.961 0.770 7.937 1.00 27.08 A O ANISOU 1192 O ASP A 155 3728 2747 3814 259 374 -746 A O ATOM 1193 CB ASP A 155 -18.011 1.525 10.514 1.00 42.35 A C ANISOU 1193 CB ASP A 155 5819 4658 5615 329 547 -990 A C ATOM 1194 CG ASP A 155 -16.793 1.905 11.339 1.00 43.22 A C ANISOU 1194 CG ASP A 155 6029 4768 5624 218 474 -1108 A C ATOM 1195 OD1 ASP A 155 -16.030 0.988 11.726 1.00 43.19 A O ANISOU 1195 OD1 ASP A 155 6029 4887 5495 140 400 -1123 A O ATOM 1196 OD2 ASP A 155 -16.592 3.114 11.591 1.00 46.72 A O ANISOU 1196 OD2 ASP A 155 6543 5093 6116 208 484 -1176 A O ATOM 1197 N CYS A 156 -15.891 -0.853 9.066 1.00 29.54 A N ANISOU 1197 N CYS A 156 4063 3276 3885 152 275 -797 A N ATOM 1198 CA CYS A 156 -14.698 -0.818 8.235 1.00 24.30 A C ANISOU 1198 CA CYS A 156 3375 2600 3258 73 178 -750 A C ATOM 1199 C CYS A 156 -14.728 -1.983 7.260 1.00 19.79 A C ANISOU 1199 C CYS A 156 2710 2126 2682 84 129 -611 A C ATOM 1200 O CYS A 156 -14.932 -3.137 7.662 1.00 18.99 A O ANISOU 1200 O CYS A 156 2586 2142 2488 91 117 -586 A O ATOM 1201 CB CYS A 156 -13.443 -0.871 9.101 1.00 24.78 A C ANISOU 1201 CB CYS A 156 3492 2706 3217 -32 106 -841 A C ATOM 1202 SG CYS A 156 -11.928 -1.036 8.165 1.00 22.23 A S ANISOU 1202 SG CYS A 156 3114 2399 2931 -127 -9 -767 A S ATOM 1203 N VAL A 157 -14.542 -1.678 5.980 1.00 16.22 A N ANISOU 1203 N VAL A 157 2210 1623 2329 84 103 -522 A N ATOM 1204 CA VAL A 157 -14.547 -2.700 4.942 1.00 11.20 A C ANISOU 1204 CA VAL A 157 1498 1070 1686 88 60 -404 A C ATOM 1205 C VAL A 157 -13.124 -3.192 4.752 1.00 14.34 A C ANISOU 1205 C VAL A 157 1889 1521 2038 7 -19 -396 A C ATOM 1206 O VAL A 157 -12.259 -2.413 4.360 1.00 11.60 A O ANISOU 1206 O VAL A 157 1550 1110 1747 -42 -45 -400 A O ATOM 1207 CB VAL A 157 -15.102 -2.152 3.619 1.00 12.39 A C ANISOU 1207 CB VAL A 157 1602 1159 1948 130 74 -304 A C ATOM 1208 CG1 VAL A 157 -15.050 -3.235 2.560 1.00 9.90 A C ANISOU 1208 CG1 VAL A 157 1223 938 1602 122 25 -202 A C ATOM 1209 CG2 VAL A 157 -16.526 -1.607 3.806 1.00 14.05 A C ANISOU 1209 CG2 VAL A 157 1801 1314 2222 221 154 -298 A C ATOM 1210 N SER A 158 -12.879 -4.482 5.000 1.00 14.24 A N ANISOU 1210 N SER A 158 1852 1620 1937 -4 -52 -373 A N ATOM 1211 CA SER A 158 -11.565 -5.082 4.742 1.00 10.02 A C ANISOU 1211 CA SER A 158 1294 1143 1371 -64 -118 -346 A C ATOM 1212 C SER A 158 -11.642 -5.785 3.397 1.00 9.99 A C ANISOU 1212 C SER A 158 1235 1168 1394 -43 -126 -246 A C ATOM 1213 O SER A 158 -12.213 -6.869 3.293 1.00 10.95 A O ANISOU 1213 O SER A 158 1336 1351 1475 -13 -120 -210 A O ATOM 1214 CB SER A 158 -11.168 -6.063 5.842 1.00 11.54 A C ANISOU 1214 CB SER A 158 1496 1433 1458 -83 -146 -375 A C ATOM 1215 OG SER A 158 -10.975 -5.382 7.084 1.00 15.85 A O ANISOU 1215 OG SER A 158 2100 1966 1955 -117 -148 -475 A O ATOM 1216 N PHE A 159 -11.083 -5.153 2.364 1.00 9.70 A N ANISOU 1216 N PHE A 159 1177 1085 1422 -66 -137 -202 A N ATOM 1217 CA PHE A 159 -11.058 -5.748 1.031 1.00 9.06 A C ANISOU 1217 CA PHE A 159 1055 1039 1350 -54 -143 -114 A C ATOM 1218 C PHE A 159 -9.959 -6.790 1.003 1.00 9.07 A C ANISOU 1218 C PHE A 159 1033 1114 1300 -83 -174 -101 A C ATOM 1219 O PHE A 159 -8.830 -6.510 1.409 1.00 9.71 A O ANISOU 1219 O PHE A 159 1107 1197 1386 -129 -201 -122 A O ATOM 1220 CB PHE A 159 -10.783 -4.694 -0.045 1.00 9.33 A C ANISOU 1220 CB PHE A 159 1076 1007 1461 -68 -138 -61 A C ATOM 1221 CG PHE A 159 -11.874 -3.664 -0.181 1.00 8.83 A C ANISOU 1221 CG PHE A 159 1027 862 1468 -27 -104 -50 A C ATOM 1222 CD1 PHE A 159 -13.049 -3.966 -0.869 1.00 9.15 A C ANISOU 1222 CD1 PHE A 159 1041 925 1509 25 -89 13 A C ATOM 1223 CD2 PHE A 159 -11.725 -2.396 0.384 1.00 11.91 A C ANISOU 1223 CD2 PHE A 159 1452 1147 1927 -41 -87 -101 A C ATOM 1224 CE1 PHE A 159 -14.055 -3.026 -0.996 1.00 9.26 A C ANISOU 1224 CE1 PHE A 159 1051 868 1600 74 -57 40 A C ATOM 1225 CE2 PHE A 159 -12.727 -1.449 0.267 1.00 10.40 A C ANISOU 1225 CE2 PHE A 159 1270 864 1816 11 -43 -86 A C ATOM 1226 CZ PHE A 159 -13.904 -1.766 -0.424 1.00 13.88 A C ANISOU 1226 CZ PHE A 159 1672 1338 2265 74 -27 -7 A C ATOM 1227 N CYS A 160 -10.277 -7.989 0.536 1.00 8.94 A N ANISOU 1227 N CYS A 160 1000 1154 1243 -57 -169 -65 A N ATOM 1228 CA CYS A 160 -9.266 -9.014 0.487 1.00 8.22 A C ANISOU 1228 CA CYS A 160 886 1118 1118 -69 -185 -49 A C ATOM 1229 C CYS A 160 -9.059 -9.626 -0.879 1.00 8.05 A C ANISOU 1229 C CYS A 160 846 1118 1094 -60 -169 4 A C ATOM 1230 O CYS A 160 -8.077 -10.355 -1.041 1.00 10.91 A O ANISOU 1230 O CYS A 160 1186 1516 1445 -63 -168 19 A O ATOM 1231 CB CYS A 160 -9.571 -10.153 1.465 1.00 6.43 A C ANISOU 1231 CB CYS A 160 668 938 837 -50 -189 -68 A C ATOM 1232 SG CYS A 160 -11.250 -10.850 1.253 1.00 12.53 A S ANISOU 1232 SG CYS A 160 1455 1715 1592 -11 -161 -57 A S ATOM 1233 N TYR A 161 -9.904 -9.347 -1.865 1.00 7.22 A N ANISOU 1233 N TYR A 161 748 1000 997 -48 -155 34 A N ATOM 1234 CA TYR A 161 -9.843 -10.116 -3.105 1.00 6.75 A C ANISOU 1234 CA TYR A 161 685 975 904 -43 -141 70 A C ATOM 1235 C TYR A 161 -10.273 -9.243 -4.258 1.00 8.96 A C ANISOU 1235 C TYR A 161 964 1243 1199 -49 -138 120 A C ATOM 1236 O TYR A 161 -11.239 -8.490 -4.147 1.00 9.76 A O ANISOU 1236 O TYR A 161 1066 1312 1330 -37 -146 133 A O ATOM 1237 CB TYR A 161 -10.737 -11.344 -3.068 1.00 7.76 A C ANISOU 1237 CB TYR A 161 830 1128 989 -26 -140 55 A C ATOM 1238 CG TYR A 161 -10.787 -12.155 -4.347 1.00 5.97 A C ANISOU 1238 CG TYR A 161 617 930 719 -31 -127 72 A C ATOM 1239 CD1 TYR A 161 -9.780 -13.064 -4.624 1.00 9.23 A C ANISOU 1239 CD1 TYR A 161 1035 1358 1113 -26 -101 61 A C ATOM 1240 CD2 TYR A 161 -11.873 -12.056 -5.241 1.00 6.09 A C ANISOU 1240 CD2 TYR A 161 642 962 710 -41 -142 96 A C ATOM 1241 CE1 TYR A 161 -9.820 -13.831 -5.760 1.00 8.79 A C ANISOU 1241 CE1 TYR A 161 1008 1324 1010 -30 -78 57 A C ATOM 1242 CE2 TYR A 161 -11.928 -12.827 -6.400 1.00 7.28 A C ANISOU 1242 CE2 TYR A 161 818 1147 801 -58 -135 96 A C ATOM 1243 CZ TYR A 161 -10.863 -13.696 -6.644 1.00 6.40 A C ANISOU 1243 CZ TYR A 161 725 1040 667 -52 -98 68 A C ATOM 1244 OH TYR A 161 -10.890 -14.475 -7.754 1.00 9.39 A O ANISOU 1244 OH TYR A 161 1142 1445 981 -67 -80 51 A O ATOM 1245 N MET A 162 -9.541 -9.340 -5.356 1.00 7.83 A N ANISOU 1245 N MET A 162 813 1127 1034 -62 -120 157 A N ATOM 1246 CA MET A 162 -9.980 -8.780 -6.617 1.00 7.07 A C ANISOU 1246 CA MET A 162 720 1045 923 -68 -118 219 A C ATOM 1247 C MET A 162 -9.960 -9.897 -7.644 1.00 9.08 A C ANISOU 1247 C MET A 162 995 1361 1092 -71 -103 218 A C ATOM 1248 O MET A 162 -8.952 -10.602 -7.775 1.00 7.15 A O ANISOU 1248 O MET A 162 752 1137 826 -69 -69 196 A O ATOM 1249 CB MET A 162 -9.092 -7.614 -7.084 1.00 9.66 A C ANISOU 1249 CB MET A 162 1025 1348 1298 -90 -103 274 A C ATOM 1250 CG MET A 162 -9.688 -6.926 -8.296 1.00 10.41 A C ANISOU 1250 CG MET A 162 1120 1455 1379 -93 -106 357 A C ATOM 1251 SD MET A 162 -9.011 -5.298 -8.738 1.00 15.02 A S ANISOU 1251 SD MET A 162 1677 1981 2047 -118 -91 445 A S ATOM 1252 CE MET A 162 -10.012 -4.215 -7.704 1.00 17.80 A C ANISOU 1252 CE MET A 162 2033 2226 2503 -95 -114 429 A C ATOM 1253 N HIS A 163 -11.054 -10.026 -8.382 1.00 10.32 A N ANISOU 1253 N HIS A 163 1167 1549 1204 -76 -126 241 A N ATOM 1254 CA HIS A 163 -11.190 -11.094 -9.361 1.00 12.24 A C ANISOU 1254 CA HIS A 163 1447 1851 1355 -92 -118 223 A C ATOM 1255 C HIS A 163 -10.444 -10.808 -10.657 1.00 9.48 A C ANISOU 1255 C HIS A 163 1107 1548 946 -107 -86 267 A C ATOM 1256 O HIS A 163 -10.587 -9.734 -11.247 1.00 10.10 A O ANISOU 1256 O HIS A 163 1167 1638 1032 -116 -98 346 A O ATOM 1257 CB HIS A 163 -12.648 -11.330 -9.714 1.00 13.08 A C ANISOU 1257 CB HIS A 163 1559 1986 1424 -108 -168 235 A C ATOM 1258 CG HIS A 163 -12.826 -12.560 -10.528 1.00 9.34 A C ANISOU 1258 CG HIS A 163 1133 1560 854 -138 -168 190 A C ATOM 1259 CD2 HIS A 163 -13.391 -12.763 -11.737 1.00 13.66 A C ANISOU 1259 CD2 HIS A 163 1707 2175 1308 -177 -196 208 A C ATOM 1260 ND1 HIS A 163 -12.259 -13.758 -10.154 1.00 10.75 A N ANISOU 1260 ND1 HIS A 163 1345 1715 1023 -132 -132 112 A N ATOM 1261 CE1 HIS A 163 -12.528 -14.666 -11.074 1.00 11.20 A C ANISOU 1261 CE1 HIS A 163 1454 1808 992 -166 -132 72 A C ATOM 1262 NE2 HIS A 163 -13.214 -14.090 -12.042 1.00 11.56 A N ANISOU 1262 NE2 HIS A 163 1499 1916 976 -200 -175 125 A N ATOM 1263 N HIS A 164 -9.722 -11.832 -11.149 1.00 13.38 A N ANISOU 1263 N HIS A 164 1635 2072 1378 -107 -39 220 A N ATOM 1264 CA HIS A 164 -8.967 -11.758 -12.390 1.00 9.71 A C ANISOU 1264 CA HIS A 164 1187 1662 838 -116 12 249 A C ATOM 1265 C HIS A 164 -9.333 -12.800 -13.429 1.00 13.12 A C ANISOU 1265 C HIS A 164 1687 2152 1145 -137 25 199 A C ATOM 1266 O HIS A 164 -9.302 -12.480 -14.610 1.00 12.29 A O ANISOU 1266 O HIS A 164 1605 2116 949 -160 37 241 A O ATOM 1267 CB HIS A 164 -7.451 -11.876 -12.113 1.00 9.21 A C ANISOU 1267 CB HIS A 164 1095 1584 820 -90 83 242 A C ATOM 1268 CG HIS A 164 -6.868 -10.658 -11.464 1.00 10.06 A C ANISOU 1268 CG HIS A 164 1138 1653 1030 -92 73 302 A C ATOM 1269 CD2 HIS A 164 -7.079 -10.126 -10.237 1.00 11.19 A C ANISOU 1269 CD2 HIS A 164 1252 1735 1266 -91 28 295 A C ATOM 1270 ND1 HIS A 164 -5.911 -9.867 -12.068 1.00 11.02 A N ANISOU 1270 ND1 HIS A 164 1225 1796 1166 -104 116 373 A N ATOM 1271 CE1 HIS A 164 -5.576 -8.887 -11.246 1.00 11.17 A C ANISOU 1271 CE1 HIS A 164 1194 1759 1289 -116 90 405 A C ATOM 1272 NE2 HIS A 164 -6.263 -9.028 -10.126 1.00 11.40 A N ANISOU 1272 NE2 HIS A 164 1231 1739 1362 -108 37 352 A N ATOM 1273 N MET A 165 -9.652 -14.040 -13.045 1.00 12.18 A N ANISOU 1273 N MET A 165 1608 2005 1015 -136 25 110 A N ATOM 1274 CA MET A 165 -9.709 -15.029 -14.118 1.00 12.83 A C ANISOU 1274 CA MET A 165 1768 2131 978 -160 56 46 A C ATOM 1275 C MET A 165 -10.365 -16.318 -13.628 1.00 12.18 A C ANISOU 1275 C MET A 165 1729 1999 901 -173 36 -46 A C ATOM 1276 O MET A 165 -10.490 -16.562 -12.422 1.00 12.13 A O ANISOU 1276 O MET A 165 1689 1928 993 -149 20 -55 A O ATOM 1277 CB MET A 165 -8.291 -15.298 -14.639 1.00 13.44 A C ANISOU 1277 CB MET A 165 1857 2219 1029 -124 163 30 A C ATOM 1278 CG MET A 165 -7.420 -15.952 -13.586 1.00 14.72 A C ANISOU 1278 CG MET A 165 1989 2306 1296 -69 214 -9 A C ATOM 1279 SD MET A 165 -5.764 -16.168 -14.262 1.00 25.14 A S ANISOU 1279 SD MET A 165 3301 3652 2601 -19 347 -6 A S ATOM 1280 CE MET A 165 -4.935 -16.914 -12.891 1.00 21.20 A C ANISOU 1280 CE MET A 165 2747 3068 2240 45 378 -28 A C ATOM 1281 N GLU A 166 -10.776 -17.153 -14.586 1.00 14.92 A N ANISOU 1281 N GLU A 166 2156 2378 1137 -217 38 -113 A N ATOM 1282 CA GLU A 166 -11.362 -18.450 -14.287 1.00 14.15 A C ANISOU 1282 CA GLU A 166 2111 2223 1042 -243 26 -206 A C ATOM 1283 C GLU A 166 -10.412 -19.538 -14.781 1.00 16.35 A C ANISOU 1283 C GLU A 166 2466 2463 1281 -216 131 -302 A C ATOM 1284 O GLU A 166 -9.805 -19.406 -15.848 1.00 17.84 A O ANISOU 1284 O GLU A 166 2696 2710 1371 -215 190 -315 A O ATOM 1285 CB GLU A 166 -12.761 -18.573 -14.917 1.00 13.35 A C ANISOU 1285 CB GLU A 166 2039 2177 856 -330 -70 -216 A C ATOM 1286 CG GLU A 166 -13.290 -20.002 -14.903 1.00 20.00 A C ANISOU 1286 CG GLU A 166 2955 2962 1682 -378 -77 -326 A C ATOM 1287 CD GLU A 166 -14.753 -20.066 -15.275 1.00 19.60 A C ANISOU 1287 CD GLU A 166 2893 2952 1603 -457 -186 -311 A C ATOM 1288 OE1 GLU A 166 -15.528 -19.215 -14.789 1.00 18.98 A O ANISOU 1288 OE1 GLU A 166 2729 2907 1575 -460 -257 -218 A O ATOM 1289 OE2 GLU A 166 -15.125 -20.973 -16.032 1.00 22.76 A O ANISOU 1289 OE2 GLU A 166 3355 3338 1953 -502 -193 -385 A O ATOM 1290 N LEU A 167 -10.221 -20.562 -13.959 1.00 17.31 A N ANISOU 1290 N LEU A 167 2601 2487 1489 -186 164 -357 A N ATOM 1291 CA LEU A 167 -9.331 -21.671 -14.272 1.00 17.72 A C ANISOU 1291 CA LEU A 167 2720 2476 1537 -144 273 -445 A C ATOM 1292 C LEU A 167 -10.120 -22.761 -14.970 1.00 18.88 A C ANISOU 1292 C LEU A 167 2979 2593 1602 -216 261 -560 A C ATOM 1293 O LEU A 167 -11.351 -22.755 -14.941 1.00 22.82 A O ANISOU 1293 O LEU A 167 3483 3112 2076 -297 159 -560 A O ATOM 1294 CB LEU A 167 -8.688 -22.176 -12.983 1.00 18.09 A C ANISOU 1294 CB LEU A 167 2714 2427 1731 -70 312 -426 A C ATOM 1295 CG LEU A 167 -7.756 -21.192 -12.261 1.00 14.03 A C ANISOU 1295 CG LEU A 167 2093 1941 1297 -7 324 -325 A C ATOM 1296 CD1 LEU A 167 -7.383 -21.748 -10.913 1.00 17.54 A C ANISOU 1296 CD1 LEU A 167 2488 2307 1869 47 331 -303 A C ATOM 1297 CD2 LEU A 167 -6.494 -20.973 -13.088 1.00 17.51 A C ANISOU 1297 CD2 LEU A 167 2530 2421 1702 42 428 -320 A C ATOM 1298 N PRO A 168 -9.448 -23.731 -15.598 1.00 20.25 A N ANISOU 1298 N PRO A 168 3243 2715 1738 -191 367 -662 A N ATOM 1299 CA PRO A 168 -10.176 -24.695 -16.439 1.00 20.95 A C ANISOU 1299 CA PRO A 168 3411 2776 1773 -252 331 -750 A C ATOM 1300 C PRO A 168 -11.186 -25.559 -15.697 1.00 22.93 A C ANISOU 1300 C PRO A 168 3678 2934 2099 -308 265 -786 A C ATOM 1301 O PRO A 168 -12.103 -26.074 -16.347 1.00 24.92 A O ANISOU 1301 O PRO A 168 3973 3192 2301 -387 198 -834 A O ATOM 1302 CB PRO A 168 -9.056 -25.547 -17.053 1.00 20.34 A C ANISOU 1302 CB PRO A 168 3390 2642 1695 -178 462 -826 A C ATOM 1303 CG PRO A 168 -7.847 -24.682 -16.986 1.00 23.53 A C ANISOU 1303 CG PRO A 168 3730 3101 2107 -94 547 -754 A C ATOM 1304 CD PRO A 168 -7.986 -23.893 -15.729 1.00 20.60 A C ANISOU 1304 CD PRO A 168 3278 2733 1816 -89 505 -666 A C ATOM 1305 N THR A 169 -11.059 -25.755 -14.382 1.00 15.90 A N ANISOU 1305 N THR A 169 2753 1962 1329 -274 281 -759 A N ATOM 1306 CA THR A 169 -12.090 -26.497 -13.666 1.00 19.05 A C ANISOU 1306 CA THR A 169 3158 2281 1798 -336 213 -775 A C ATOM 1307 C THR A 169 -13.297 -25.632 -13.325 1.00 19.02 A C ANISOU 1307 C THR A 169 3081 2368 1779 -409 82 -695 A C ATOM 1308 O THR A 169 -14.210 -26.111 -12.647 1.00 21.72 A O ANISOU 1308 O THR A 169 3404 2662 2188 -459 22 -685 A O ATOM 1309 CB THR A 169 -11.538 -27.116 -12.374 1.00 17.52 A C ANISOU 1309 CB THR A 169 2926 1968 1762 -254 269 -739 A C ATOM 1310 CG2 THR A 169 -10.649 -28.303 -12.693 1.00 18.41 A C ANISOU 1310 CG2 THR A 169 3124 1957 1913 -196 393 -830 A C ATOM 1311 OG1 THR A 169 -10.771 -26.137 -11.665 1.00 18.86 A O ANISOU 1311 OG1 THR A 169 2988 2194 1984 -167 279 -629 A O ATOM 1312 N GLY A 170 -13.323 -24.381 -13.766 1.00 17.91 A N ANISOU 1312 N GLY A 170 2888 2351 1566 -408 41 -626 A N ATOM 1313 CA GLY A 170 -14.431 -23.516 -13.438 1.00 16.78 A C ANISOU 1313 CA GLY A 170 2661 2286 1428 -456 -73 -537 A C ATOM 1314 C GLY A 170 -14.311 -22.787 -12.122 1.00 20.02 A C ANISOU 1314 C GLY A 170 2964 2687 1957 -386 -81 -433 A C ATOM 1315 O GLY A 170 -15.268 -22.112 -11.726 1.00 18.90 A O ANISOU 1315 O GLY A 170 2751 2594 1836 -414 -161 -362 A O ATOM 1316 N VAL A 171 -13.169 -22.891 -11.431 1.00 15.56 A N ANISOU 1316 N VAL A 171 2382 2064 1468 -295 -0 -421 A N ATOM 1317 CA VAL A 171 -12.929 -22.124 -10.214 1.00 12.16 A C ANISOU 1317 CA VAL A 171 1857 1636 1129 -234 -10 -332 A C ATOM 1318 C VAL A 171 -12.157 -20.864 -10.568 1.00 12.47 A C ANISOU 1318 C VAL A 171 1854 1745 1139 -193 6 -277 A C ATOM 1319 O VAL A 171 -11.732 -20.678 -11.713 1.00 14.51 A O ANISOU 1319 O VAL A 171 2153 2049 1310 -202 36 -301 A O ATOM 1320 CB VAL A 171 -12.181 -22.944 -9.146 1.00 14.52 A C ANISOU 1320 CB VAL A 171 2148 1841 1528 -169 49 -333 A C ATOM 1321 CG1 VAL A 171 -12.984 -24.196 -8.777 1.00 14.56 A C ANISOU 1321 CG1 VAL A 171 2194 1764 1574 -215 36 -374 A C ATOM 1322 CG2 VAL A 171 -10.795 -23.316 -9.615 1.00 14.19 A C ANISOU 1322 CG2 VAL A 171 2138 1770 1485 -104 147 -367 A C ATOM 1323 N HIS A 172 -11.959 -19.993 -9.590 1.00 10.45 A N ANISOU 1323 N HIS A 172 1520 1497 952 -152 -11 -205 A N ATOM 1324 CA HIS A 172 -11.598 -18.621 -9.894 1.00 10.29 A C ANISOU 1324 CA HIS A 172 1455 1540 916 -137 -20 -143 A C ATOM 1325 C HIS A 172 -10.337 -18.233 -9.147 1.00 10.18 A C ANISOU 1325 C HIS A 172 1393 1505 970 -74 26 -112 A C ATOM 1326 O HIS A 172 -10.066 -18.718 -8.041 1.00 8.88 A O ANISOU 1326 O HIS A 172 1207 1294 875 -42 35 -112 A O ATOM 1327 CB HIS A 172 -12.783 -17.722 -9.561 1.00 13.07 A C ANISOU 1327 CB HIS A 172 1760 1926 1283 -166 -99 -88 A C ATOM 1328 CG HIS A 172 -13.995 -18.068 -10.373 1.00 12.68 A C ANISOU 1328 CG HIS A 172 1738 1913 1165 -235 -155 -104 A C ATOM 1329 CD2 HIS A 172 -14.258 -17.916 -11.692 1.00 13.40 A C ANISOU 1329 CD2 HIS A 172 1866 2071 1155 -281 -178 -106 A C ATOM 1330 ND1 HIS A 172 -15.087 -18.718 -9.837 1.00 11.76 A N ANISOU 1330 ND1 HIS A 172 1614 1775 1078 -271 -200 -117 A N ATOM 1331 CE1 HIS A 172 -15.986 -18.923 -10.784 1.00 14.94 A C ANISOU 1331 CE1 HIS A 172 2039 2228 1408 -342 -255 -127 A C ATOM 1332 NE2 HIS A 172 -15.510 -18.444 -11.921 1.00 11.78 A N ANISOU 1332 NE2 HIS A 172 1669 1886 921 -350 -247 -122 A N ATOM 1333 N ALA A 173 -9.567 -17.360 -9.769 1.00 10.86 A N ANISOU 1333 N ALA A 173 1459 1633 1034 -62 52 -76 A N ATOM 1334 CA ALA A 173 -8.293 -16.938 -9.221 1.00 8.24 A C ANISOU 1334 CA ALA A 173 1073 1293 765 -16 92 -41 A C ATOM 1335 C ALA A 173 -8.197 -15.427 -9.304 1.00 10.00 A C ANISOU 1335 C ALA A 173 1248 1550 1001 -30 63 26 A C ATOM 1336 O ALA A 173 -8.713 -14.813 -10.248 1.00 9.15 A O ANISOU 1336 O ALA A 173 1156 1484 835 -61 45 52 A O ATOM 1337 CB ALA A 173 -7.134 -17.607 -9.970 1.00 11.34 A C ANISOU 1337 CB ALA A 173 1487 1688 1136 19 183 -66 A C ATOM 1338 N GLY A 174 -7.562 -14.830 -8.306 1.00 8.65 A N ANISOU 1338 N GLY A 174 1020 1361 907 -13 53 57 A N ATOM 1339 CA GLY A 174 -7.385 -13.396 -8.305 1.00 8.48 A C ANISOU 1339 CA GLY A 174 957 1350 916 -30 30 113 A C ATOM 1340 C GLY A 174 -6.330 -12.975 -7.324 1.00 8.56 A C ANISOU 1340 C GLY A 174 909 1341 1001 -20 30 131 A C ATOM 1341 O GLY A 174 -5.543 -13.790 -6.836 1.00 8.31 A O ANISOU 1341 O GLY A 174 858 1308 993 8 56 116 A O ATOM 1342 N THR A 175 -6.341 -11.690 -6.992 1.00 8.55 A N ANISOU 1342 N THR A 175 879 1325 1044 -45 -3 165 A N ATOM 1343 CA THR A 175 -5.292 -11.104 -6.181 1.00 7.79 A C ANISOU 1343 CA THR A 175 728 1218 1015 -57 -12 181 A C ATOM 1344 C THR A 175 -5.871 -10.505 -4.910 1.00 8.28 A C ANISOU 1344 C THR A 175 793 1240 1113 -72 -69 153 A C ATOM 1345 O THR A 175 -7.087 -10.313 -4.776 1.00 8.21 A O ANISOU 1345 O THR A 175 820 1210 1090 -68 -90 135 A O ATOM 1346 CB THR A 175 -4.558 -9.995 -6.950 1.00 10.08 A C ANISOU 1346 CB THR A 175 982 1513 1334 -87 8 243 A C ATOM 1347 CG2 THR A 175 -4.097 -10.511 -8.278 1.00 9.11 A C ANISOU 1347 CG2 THR A 175 864 1439 1156 -71 75 271 A C ATOM 1348 OG1 THR A 175 -5.475 -8.904 -7.167 1.00 9.34 A O ANISOU 1348 OG1 THR A 175 913 1385 1253 -110 -22 264 A O ATOM 1349 N ASP A 176 -4.972 -10.144 -4.004 1.00 10.35 A N ANISOU 1349 N ASP A 176 1014 1498 1421 -92 -91 151 A N ATOM 1350 CA ASP A 176 -5.363 -9.217 -2.958 1.00 8.26 A C ANISOU 1350 CA ASP A 176 760 1192 1186 -120 -138 119 A C ATOM 1351 C ASP A 176 -5.364 -7.815 -3.572 1.00 8.54 A C ANISOU 1351 C ASP A 176 794 1182 1270 -155 -135 152 A C ATOM 1352 O ASP A 176 -5.081 -7.637 -4.756 1.00 9.30 A O ANISOU 1352 O ASP A 176 876 1292 1366 -158 -102 207 A O ATOM 1353 CB ASP A 176 -4.474 -9.392 -1.722 1.00 10.08 A C ANISOU 1353 CB ASP A 176 957 1444 1431 -141 -175 98 A C ATOM 1354 CG ASP A 176 -3.014 -9.042 -1.961 1.00 11.89 A C ANISOU 1354 CG ASP A 176 1115 1697 1707 -176 -176 143 A C ATOM 1355 OD1 ASP A 176 -2.703 -8.216 -2.832 1.00 10.32 A O ANISOU 1355 OD1 ASP A 176 899 1477 1544 -203 -154 182 A O ATOM 1356 OD2 ASP A 176 -2.163 -9.595 -1.225 1.00 13.31 A O ANISOU 1356 OD2 ASP A 176 1248 1921 1891 -179 -201 150 A O ATOM 1357 N LEU A 177 -5.726 -6.814 -2.788 1.00 9.68 A N ANISOU 1357 N LEU A 177 957 1267 1454 -181 -164 118 A N ATOM 1358 CA LEU A 177 -5.850 -5.468 -3.335 1.00 8.65 A C ANISOU 1358 CA LEU A 177 831 1069 1386 -208 -157 152 A C ATOM 1359 C LEU A 177 -4.505 -4.772 -3.470 1.00 12.06 A C ANISOU 1359 C LEU A 177 1215 1488 1877 -270 -163 186 A C ATOM 1360 O LEU A 177 -4.454 -3.633 -3.953 1.00 12.97 A O ANISOU 1360 O LEU A 177 1329 1539 2058 -302 -154 227 A O ATOM 1361 CB LEU A 177 -6.831 -4.631 -2.496 1.00 8.82 A C ANISOU 1361 CB LEU A 177 899 1012 1440 -203 -171 98 A C ATOM 1362 CG LEU A 177 -8.311 -4.713 -2.921 1.00 9.95 A C ANISOU 1362 CG LEU A 177 1070 1145 1568 -146 -152 114 A C ATOM 1363 CD1 LEU A 177 -8.443 -4.101 -4.305 1.00 9.94 A C ANISOU 1363 CD1 LEU A 177 1054 1127 1595 -144 -133 208 A C ATOM 1364 CD2 LEU A 177 -8.780 -6.160 -2.976 1.00 10.90 A C ANISOU 1364 CD2 LEU A 177 1191 1345 1605 -110 -151 104 A C ATOM 1365 N GLU A 178 -3.428 -5.417 -3.046 1.00 10.48 A N ANISOU 1365 N GLU A 178 968 1348 1667 -289 -177 181 A N ATOM 1366 CA GLU A 178 -2.098 -4.978 -3.441 1.00 12.48 A C ANISOU 1366 CA GLU A 178 1151 1615 1974 -342 -173 238 A C ATOM 1367 C GLU A 178 -1.667 -5.565 -4.781 1.00 12.86 A C ANISOU 1367 C GLU A 178 1163 1724 1998 -309 -110 316 A C ATOM 1368 O GLU A 178 -0.558 -5.274 -5.225 1.00 13.46 A O ANISOU 1368 O GLU A 178 1172 1824 2118 -345 -90 377 A O ATOM 1369 CB GLU A 178 -1.073 -5.351 -2.363 1.00 10.95 A C ANISOU 1369 CB GLU A 178 905 1467 1787 -379 -222 211 A C ATOM 1370 N GLY A 179 -2.503 -6.375 -5.429 1.00 10.49 A N ANISOU 1370 N GLY A 179 907 1453 1626 -246 -76 314 A N ATOM 1371 CA GLY A 179 -2.190 -6.953 -6.722 1.00 10.10 A C ANISOU 1371 CA GLY A 179 844 1463 1532 -216 -10 369 A C ATOM 1372 C GLY A 179 -1.356 -8.214 -6.686 1.00 11.76 A C ANISOU 1372 C GLY A 179 1015 1738 1716 -178 24 362 A C ATOM 1373 O GLY A 179 -0.801 -8.610 -7.730 1.00 10.84 A O ANISOU 1373 O GLY A 179 877 1669 1572 -156 94 405 A O ATOM 1374 N ASN A 180 -1.242 -8.855 -5.524 1.00 10.37 A N ANISOU 1374 N ASN A 180 829 1565 1546 -165 -15 314 A N ATOM 1375 CA ASN A 180 -0.454 -10.073 -5.382 1.00 9.54 A C ANISOU 1375 CA ASN A 180 680 1511 1434 -119 16 319 A C ATOM 1376 C ASN A 180 -1.402 -11.248 -5.478 1.00 9.80 A C ANISOU 1376 C ASN A 180 784 1540 1401 -61 36 268 A C ATOM 1377 O ASN A 180 -2.385 -11.296 -4.742 1.00 8.23 A O ANISOU 1377 O ASN A 180 634 1310 1181 -63 -13 221 A O ATOM 1378 CB ASN A 180 0.292 -10.069 -4.044 1.00 9.85 A C ANISOU 1378 CB ASN A 180 657 1564 1522 -145 -47 316 A C ATOM 1379 CG ASN A 180 1.170 -8.862 -3.901 1.00 13.42 A C ANISOU 1379 CG ASN A 180 1042 2013 2044 -223 -79 356 A C ATOM 1380 ND2 ASN A 180 2.166 -8.781 -4.753 1.00 11.26 A N ANISOU 1380 ND2 ASN A 180 694 1776 1807 -225 -22 428 A N ATOM 1381 OD1 ASN A 180 0.950 -7.991 -3.032 1.00 16.47 A O ANISOU 1381 OD1 ASN A 180 1445 2361 2452 -284 -150 320 A O ATOM 1382 N PHE A 181 -1.144 -12.166 -6.410 1.00 9.00 A N ANISOU 1382 N PHE A 181 690 1463 1264 -13 111 275 A N ATOM 1383 CA PHE A 181 -2.079 -13.257 -6.612 1.00 10.27 A C ANISOU 1383 CA PHE A 181 928 1609 1365 27 129 220 A C ATOM 1384 C PHE A 181 -2.187 -14.134 -5.382 1.00 9.12 A C ANISOU 1384 C PHE A 181 778 1445 1240 54 94 193 A C ATOM 1385 O PHE A 181 -1.209 -14.372 -4.668 1.00 8.62 A O ANISOU 1385 O PHE A 181 646 1401 1229 69 86 225 A O ATOM 1386 CB PHE A 181 -1.691 -14.126 -7.814 1.00 9.16 A C ANISOU 1386 CB PHE A 181 808 1490 1181 71 224 215 A C ATOM 1387 CG PHE A 181 -2.417 -13.768 -9.056 1.00 9.70 A C ANISOU 1387 CG PHE A 181 941 1574 1169 48 246 208 A C ATOM 1388 CD1 PHE A 181 -3.668 -14.335 -9.304 1.00 12.34 A C ANISOU 1388 CD1 PHE A 181 1360 1892 1438 44 224 151 A C ATOM 1389 CD2 PHE A 181 -1.901 -12.854 -9.957 1.00 9.83 A C ANISOU 1389 CD2 PHE A 181 930 1629 1175 23 280 267 A C ATOM 1390 CE1 PHE A 181 -4.369 -14.021 -10.443 1.00 10.79 A C ANISOU 1390 CE1 PHE A 181 1218 1724 1157 17 229 152 A C ATOM 1391 CE2 PHE A 181 -2.599 -12.541 -11.116 1.00 12.22 A C ANISOU 1391 CE2 PHE A 181 1294 1960 1391 2 294 273 A C ATOM 1392 CZ PHE A 181 -3.844 -13.122 -11.347 1.00 13.23 A C ANISOU 1392 CZ PHE A 181 1504 2078 1445 -2 262 214 A C ATOM 1393 N TYR A 182 -3.396 -14.624 -5.153 1.00 8.18 A N ANISOU 1393 N TYR A 182 728 1297 1081 58 70 146 A N ATOM 1394 CA TYR A 182 -3.563 -15.760 -4.275 1.00 7.60 A C ANISOU 1394 CA TYR A 182 664 1205 1018 93 61 128 A C ATOM 1395 C TYR A 182 -3.165 -17.007 -5.040 1.00 8.68 A C ANISOU 1395 C TYR A 182 820 1327 1150 146 142 117 A C ATOM 1396 O TYR A 182 -3.747 -17.309 -6.089 1.00 10.20 A O ANISOU 1396 O TYR A 182 1078 1508 1290 142 180 77 A O ATOM 1397 CB TYR A 182 -5.001 -15.849 -3.782 1.00 7.00 A C ANISOU 1397 CB TYR A 182 648 1103 908 74 16 89 A C ATOM 1398 CG TYR A 182 -5.362 -14.786 -2.779 1.00 6.68 A C ANISOU 1398 CG TYR A 182 593 1068 877 37 -49 90 A C ATOM 1399 CD1 TYR A 182 -4.996 -14.938 -1.443 1.00 9.19 A C ANISOU 1399 CD1 TYR A 182 880 1399 1212 40 -88 99 A C ATOM 1400 CD2 TYR A 182 -6.119 -13.681 -3.137 1.00 8.96 A C ANISOU 1400 CD2 TYR A 182 904 1347 1155 4 -69 81 A C ATOM 1401 CE1 TYR A 182 -5.348 -14.005 -0.503 1.00 7.82 A C ANISOU 1401 CE1 TYR A 182 708 1229 1033 5 -140 82 A C ATOM 1402 CE2 TYR A 182 -6.499 -12.730 -2.190 1.00 7.98 A C ANISOU 1402 CE2 TYR A 182 776 1210 1044 -22 -115 68 A C ATOM 1403 CZ TYR A 182 -6.102 -12.902 -0.879 1.00 8.03 A C ANISOU 1403 CZ TYR A 182 764 1231 1057 -24 -147 59 A C ATOM 1404 OH TYR A 182 -6.441 -11.986 0.091 1.00 8.66 A O ANISOU 1404 OH TYR A 182 853 1300 1136 -52 -186 30 A O ATOM 1405 N GLY A 183 -2.138 -17.690 -4.551 1.00 9.82 A N ANISOU 1405 N GLY A 183 907 1473 1350 194 168 152 A N ATOM 1406 CA GLY A 183 -1.723 -18.950 -5.117 1.00 9.71 A C ANISOU 1406 CA GLY A 183 911 1426 1351 259 255 140 A C ATOM 1407 C GLY A 183 -0.821 -18.799 -6.318 1.00 10.49 A C ANISOU 1407 C GLY A 183 988 1552 1447 284 345 150 A C ATOM 1408 O GLY A 183 -0.446 -17.693 -6.712 1.00 10.00 A O ANISOU 1408 O GLY A 183 886 1539 1376 246 336 181 A O ATOM 1409 N PRO A 184 -0.473 -19.916 -6.924 1.00 10.75 A N ANISOU 1409 N PRO A 184 1049 1546 1488 348 441 123 A N ATOM 1410 CA PRO A 184 0.564 -19.944 -7.971 1.00 11.90 A C ANISOU 1410 CA PRO A 184 1164 1720 1638 391 551 137 A C ATOM 1411 C PRO A 184 -0.031 -19.694 -9.353 1.00 15.76 A C ANISOU 1411 C PRO A 184 1747 2224 2017 356 596 73 A C ATOM 1412 O PRO A 184 0.039 -20.536 -10.252 1.00 16.95 A O ANISOU 1412 O PRO A 184 1965 2347 2128 395 695 12 A O ATOM 1413 CB PRO A 184 1.109 -21.369 -7.851 1.00 16.45 A C ANISOU 1413 CB PRO A 184 1738 2231 2279 486 638 129 A C ATOM 1414 CG PRO A 184 -0.101 -22.158 -7.412 1.00 13.99 A C ANISOU 1414 CG PRO A 184 1525 1843 1946 468 591 66 A C ATOM 1415 CD PRO A 184 -0.946 -21.261 -6.562 1.00 11.78 A C ANISOU 1415 CD PRO A 184 1238 1597 1640 389 460 84 A C ATOM 1416 N PHE A 185 -0.648 -18.544 -9.513 1.00 12.02 A N ANISOU 1416 N PHE A 185 1283 1793 1492 281 523 85 A N ATOM 1417 CA PHE A 185 -1.332 -18.187 -10.748 1.00 12.54 A C ANISOU 1417 CA PHE A 185 1431 1888 1445 237 540 45 A C ATOM 1418 C PHE A 185 -0.795 -16.860 -11.244 1.00 15.74 A C ANISOU 1418 C PHE A 185 1776 2364 1842 203 542 119 A C ATOM 1419 O PHE A 185 -0.301 -16.043 -10.459 1.00 13.63 A O ANISOU 1419 O PHE A 185 1419 2108 1652 185 490 186 A O ATOM 1420 CB PHE A 185 -2.846 -18.124 -10.535 1.00 13.04 A C ANISOU 1420 CB PHE A 185 1569 1928 1456 179 445 -1 A C ATOM 1421 CG PHE A 185 -3.385 -19.356 -9.917 1.00 12.47 A C ANISOU 1421 CG PHE A 185 1545 1783 1410 201 435 -58 A C ATOM 1422 CD1 PHE A 185 -3.293 -20.557 -10.586 1.00 11.69 A C ANISOU 1422 CD1 PHE A 185 1519 1641 1283 235 520 -131 A C ATOM 1423 CD2 PHE A 185 -3.965 -19.332 -8.665 1.00 13.81 A C ANISOU 1423 CD2 PHE A 185 1691 1923 1633 186 350 -42 A C ATOM 1424 CE1 PHE A 185 -3.764 -21.715 -10.013 1.00 14.62 A C ANISOU 1424 CE1 PHE A 185 1934 1927 1693 252 516 -177 A C ATOM 1425 CE2 PHE A 185 -4.433 -20.483 -8.100 1.00 12.94 A C ANISOU 1425 CE2 PHE A 185 1620 1745 1550 204 348 -80 A C ATOM 1426 CZ PHE A 185 -4.324 -21.687 -8.786 1.00 11.93 A C ANISOU 1426 CZ PHE A 185 1562 1562 1409 236 429 -145 A C ATOM 1427 N VAL A 186 -0.871 -16.665 -12.557 1.00 15.70 A N ANISOU 1427 N VAL A 186 1822 2406 1738 188 601 108 A N ATOM 1428 CA VAL A 186 -0.286 -15.503 -13.210 1.00 15.91 A C ANISOU 1428 CA VAL A 186 1795 2499 1750 159 625 191 A C ATOM 1429 C VAL A 186 -1.296 -14.934 -14.193 1.00 16.73 A C ANISOU 1429 C VAL A 186 1980 2644 1734 101 593 186 A C ATOM 1430 O VAL A 186 -2.173 -15.645 -14.696 1.00 17.42 A O ANISOU 1430 O VAL A 186 2166 2727 1726 92 587 109 A O ATOM 1431 CB VAL A 186 1.037 -15.853 -13.923 1.00 19.52 A C ANISOU 1431 CB VAL A 186 2206 2999 2213 216 766 217 A C ATOM 1432 CG1 VAL A 186 2.119 -16.196 -12.888 1.00 21.75 A C ANISOU 1432 CG1 VAL A 186 2374 3255 2636 270 781 258 A C ATOM 1433 CG2 VAL A 186 0.829 -17.019 -14.861 1.00 16.73 A C ANISOU 1433 CG2 VAL A 186 1960 2641 1756 258 864 120 A C ATOM 1434 N ASP A 187 -1.182 -13.640 -14.461 1.00 16.88 A N ANISOU 1434 N ASP A 187 1952 2701 1760 57 565 277 A N ATOM 1435 CA ASP A 187 -2.089 -12.997 -15.410 1.00 20.84 A C ANISOU 1435 CA ASP A 187 2515 3250 2155 6 531 302 A C ATOM 1436 C ASP A 187 -1.450 -12.962 -16.798 1.00 20.53 A C ANISOU 1436 C ASP A 187 2495 3297 2007 12 640 334 A C ATOM 1437 O ASP A 187 -1.266 -11.927 -17.440 1.00 18.32 A O ANISOU 1437 O ASP A 187 2188 3070 1704 -22 648 433 A O ATOM 1438 CB ASP A 187 -2.518 -11.619 -14.894 1.00 16.75 A C ANISOU 1438 CB ASP A 187 1948 2707 1709 -41 436 385 A C ATOM 1439 CG ASP A 187 -1.356 -10.703 -14.558 1.00 19.04 A C ANISOU 1439 CG ASP A 187 2136 2992 2108 -50 461 472 A C ATOM 1440 OD1 ASP A 187 -0.179 -11.127 -14.615 1.00 16.19 A O ANISOU 1440 OD1 ASP A 187 1720 2653 1777 -17 546 481 A O ATOM 1441 OD2 ASP A 187 -1.654 -9.552 -14.158 1.00 16.83 A O ANISOU 1441 OD2 ASP A 187 1824 2676 1895 -92 392 532 A O ATOM 1442 N ARG A 188 -1.080 -14.161 -17.245 1.00 22.27 A N ANISOU 1442 N ARG A 188 2768 3527 2165 59 736 248 A N ATOM 1443 CA ARG A 188 -0.677 -14.407 -18.617 1.00 22.73 A C ANISOU 1443 CA ARG A 188 2883 3662 2092 65 844 236 A C ATOM 1444 C ARG A 188 -1.197 -15.784 -19.005 1.00 25.00 A C ANISOU 1444 C ARG A 188 3291 3928 2280 82 878 92 A C ATOM 1445 O ARG A 188 -1.508 -16.611 -18.138 1.00 24.49 A O ANISOU 1445 O ARG A 188 3240 3785 2280 111 850 19 A O ATOM 1446 CB ARG A 188 0.846 -14.329 -18.806 1.00 24.58 A C ANISOU 1446 CB ARG A 188 3033 3898 2407 104 949 278 A C ATOM 1447 CG ARG A 188 1.625 -15.279 -17.920 1.00 25.18 A C ANISOU 1447 CG ARG A 188 3054 3911 2601 178 999 231 A C ATOM 1448 CD ARG A 188 3.128 -15.147 -18.118 1.00 26.98 A C ANISOU 1448 CD ARG A 188 3183 4154 2914 212 1083 285 A C ATOM 1449 NE ARG A 188 3.810 -15.856 -17.044 1.00 26.20 A N ANISOU 1449 NE ARG A 188 3007 3994 2954 277 1091 274 A N ATOM 1450 CZ ARG A 188 4.137 -17.142 -17.106 1.00 28.96 A C ANISOU 1450 CZ ARG A 188 3390 4303 3311 347 1164 189 A C ATOM 1451 NH1 ARG A 188 3.858 -17.840 -18.206 1.00 30.22 A N ANISOU 1451 NH1 ARG A 188 3659 4479 3345 353 1235 93 A N ATOM 1452 NH2 ARG A 188 4.737 -17.732 -16.074 1.00 28.31 A N ANISOU 1452 NH2 ARG A 188 3232 4162 3362 405 1156 200 A N ATOM 1453 N GLN A 189 -1.303 -16.020 -20.315 1.00 28.18 A N ANISOU 1453 N GLN A 189 3788 4375 2544 50 925 45 A N ATOM 1454 CA GLN A 189 -1.977 -17.213 -20.824 1.00 30.45 A C ANISOU 1454 CA GLN A 189 4206 4638 2723 36 934 -97 A C ATOM 1455 C GLN A 189 -1.065 -18.425 -20.692 1.00 26.72 A C ANISOU 1455 C GLN A 189 3698 4150 2307 122 1027 -190 A C ATOM 1456 O GLN A 189 -0.012 -18.504 -21.339 1.00 26.52 A O ANISOU 1456 O GLN A 189 3640 4159 2277 151 1132 -186 A O ATOM 1457 CB GLN A 189 -2.410 -17.031 -22.274 1.00 34.21 A C ANISOU 1457 CB GLN A 189 4791 5176 3032 40 930 -79 A C ATOM 1458 CG GLN A 189 -3.016 -18.281 -22.876 1.00 33.12 A C ANISOU 1458 CG GLN A 189 4737 5065 2784 59 905 -219 A C ATOM 1459 CD GLN A 189 -4.293 -18.672 -22.160 1.00 33.14 A C ANISOU 1459 CD GLN A 189 4776 4999 2817 -6 776 -280 A C ATOM 1460 NE2 GLN A 189 -4.350 -19.914 -21.692 1.00 34.53 A N ANISOU 1460 NE2 GLN A 189 4984 5091 3045 14 793 -403 A N ATOM 1461 OE1 GLN A 189 -5.219 -17.867 -22.021 1.00 37.63 A O ANISOU 1461 OE1 GLN A 189 5333 5587 3376 -75 660 -212 A O ATOM 1462 N THR A 190 -1.478 -19.369 -19.850 1.00 25.40 A N ANISOU 1462 N THR A 190 3565 3875 2211 157 999 -267 A N ATOM 1463 CA THR A 190 -0.795 -20.636 -19.643 1.00 24.79 A C ANISOU 1463 CA THR A 190 3497 3709 2215 233 1083 -353 A C ATOM 1464 C THR A 190 -1.851 -21.697 -19.394 1.00 27.08 A C ANISOU 1464 C THR A 190 3893 3907 2490 213 1023 -466 A C ATOM 1465 O THR A 190 -3.038 -21.399 -19.249 1.00 24.47 A O ANISOU 1465 O THR A 190 3609 3582 2105 140 912 -470 A O ATOM 1466 CB THR A 190 0.154 -20.602 -18.442 1.00 25.73 A C ANISOU 1466 CB THR A 190 3498 3759 2519 302 1118 -281 A C ATOM 1467 CG2 THR A 190 1.065 -19.384 -18.488 1.00 26.92 A C ANISOU 1467 CG2 THR A 190 3531 3987 2712 300 1142 -149 A C ATOM 1468 OG1 THR A 190 -0.624 -20.555 -17.244 1.00 21.68 A O ANISOU 1468 OG1 THR A 190 2981 3180 2077 288 1029 -266 A O ATOM 1469 N ALA A 191 -1.400 -22.944 -19.305 1.00 28.04 A N ANISOU 1469 N ALA A 191 4044 3933 2677 274 1093 -551 A N ATOM 1470 CA ALA A 191 -2.299 -24.034 -18.955 1.00 25.42 A C ANISOU 1470 CA ALA A 191 3803 3490 2365 251 1043 -651 A C ATOM 1471 C ALA A 191 -2.439 -24.178 -17.442 1.00 26.01 A C ANISOU 1471 C ALA A 191 3822 3467 2591 274 1003 -607 A C ATOM 1472 O ALA A 191 -2.700 -25.281 -16.952 1.00 27.69 A O ANISOU 1472 O ALA A 191 4079 3563 2879 291 1004 -670 A O ATOM 1473 CB ALA A 191 -1.799 -25.343 -19.581 1.00 28.35 A C ANISOU 1473 CB ALA A 191 4243 3791 2740 304 1138 -759 A C ATOM 1474 N GLN A 192 -2.282 -23.081 -16.695 1.00 23.31 A N ANISOU 1474 N GLN A 192 3386 3173 2298 273 969 -496 A N ATOM 1475 CA GLN A 192 -2.332 -23.162 -15.238 1.00 21.30 A C ANISOU 1475 CA GLN A 192 3070 2842 2181 305 935 -447 A C ATOM 1476 C GLN A 192 -3.655 -23.760 -14.779 1.00 27.32 A C ANISOU 1476 C GLN A 192 3909 3532 2937 240 839 -513 A C ATOM 1477 O GLN A 192 -4.714 -23.497 -15.361 1.00 26.31 A O ANISOU 1477 O GLN A 192 3851 3450 2695 148 761 -554 A O ATOM 1478 CB GLN A 192 -2.146 -21.783 -14.587 1.00 18.78 A C ANISOU 1478 CB GLN A 192 2627 2598 1911 287 854 -315 A C ATOM 1479 CG GLN A 192 -3.060 -20.688 -15.100 1.00 22.46 A C ANISOU 1479 CG GLN A 192 3112 3152 2269 193 754 -287 A C ATOM 1480 CD GLN A 192 -2.575 -19.289 -14.733 1.00 19.12 A C ANISOU 1480 CD GLN A 192 2572 2795 1897 185 711 -160 A C ATOM 1481 NE2 GLN A 192 -2.969 -18.304 -15.530 1.00 20.08 A N ANISOU 1481 NE2 GLN A 192 2707 3000 1923 126 676 -119 A N ATOM 1482 OE1 GLN A 192 -1.860 -19.097 -13.740 1.00 19.01 A O ANISOU 1482 OE1 GLN A 192 2459 2756 2009 226 704 -97 A O ATOM 1483 N ALA A 193 -3.585 -24.559 -13.716 1.00 23.44 A N ANISOU 1483 N ALA A 193 3393 2935 2577 286 835 -508 A N ATOM 1484 CA ALA A 193 -4.746 -25.244 -13.179 1.00 21.93 A C ANISOU 1484 CA ALA A 193 3260 2666 2406 229 751 -556 A C ATOM 1485 C ALA A 193 -4.682 -25.207 -11.659 1.00 20.35 A C ANISOU 1485 C ALA A 193 2961 2427 2345 262 689 -461 A C ATOM 1486 O ALA A 193 -3.619 -25.026 -11.065 1.00 21.03 A O ANISOU 1486 O ALA A 193 2951 2520 2521 341 728 -382 A O ATOM 1487 CB ALA A 193 -4.836 -26.696 -13.670 1.00 22.38 A C ANISOU 1487 CB ALA A 193 3428 2609 2467 239 822 -674 A C ATOM 1488 N ALA A 194 -5.844 -25.410 -11.040 1.00 19.50 A N ANISOU 1488 N ALA A 194 2874 2286 2248 197 589 -468 A N ATOM 1489 CA ALA A 194 -5.969 -25.274 -9.592 1.00 20.87 A C ANISOU 1489 CA ALA A 194 2963 2443 2525 214 520 -378 A C ATOM 1490 C ALA A 194 -4.940 -26.108 -8.832 1.00 24.39 A C ANISOU 1490 C ALA A 194 3363 2809 3094 315 593 -336 A C ATOM 1491 O ALA A 194 -4.248 -25.602 -7.941 1.00 30.14 A O ANISOU 1491 O ALA A 194 3986 3579 3888 360 570 -238 A O ATOM 1492 CB ALA A 194 -7.383 -25.664 -9.170 1.00 19.14 A C ANISOU 1492 CB ALA A 194 2788 2185 2300 135 433 -404 A C ATOM 1493 N GLY A 195 -4.833 -27.386 -9.141 1.00 25.62 A N ANISOU 1493 N GLY A 195 3596 2850 3290 349 676 -404 A N ATOM 1494 CA GLY A 195 -4.042 -28.237 -8.277 1.00 29.36 A C ANISOU 1494 CA GLY A 195 4020 3236 3899 446 731 -343 A C ATOM 1495 C GLY A 195 -4.829 -28.716 -7.066 1.00 28.55 A C ANISOU 1495 C GLY A 195 3907 3079 3863 418 652 -291 A C ATOM 1496 O GLY A 195 -5.911 -28.223 -6.750 1.00 24.43 A O ANISOU 1496 O GLY A 195 3392 2603 3289 330 551 -290 A O ATOM 1497 N THR A 196 -4.268 -29.713 -6.382 1.00 24.48 A N ANISOU 1497 N THR A 196 3369 2463 3470 500 705 -240 A N ATOM 1498 CA THR A 196 -5.068 -30.503 -5.455 1.00 25.91 A C ANISOU 1498 CA THR A 196 3572 2559 3715 473 659 -206 A C ATOM 1499 C THR A 196 -5.534 -29.672 -4.261 1.00 21.74 A C ANISOU 1499 C THR A 196 2958 2134 3168 432 539 -106 A C ATOM 1500 O THR A 196 -4.805 -28.821 -3.740 1.00 22.69 A O ANISOU 1500 O THR A 196 2979 2356 3284 467 507 -26 A O ATOM 1501 CB THR A 196 -4.272 -31.716 -4.987 1.00 27.61 A C ANISOU 1501 CB THR A 196 3774 2643 4073 581 747 -152 A C ATOM 1502 CG2 THR A 196 -3.861 -32.572 -6.197 1.00 26.28 A C ANISOU 1502 CG2 THR A 196 3686 2404 3895 593 838 -258 A C ATOM 1503 OG1 THR A 196 -3.093 -31.265 -4.316 1.00 33.46 A O ANISOU 1503 OG1 THR A 196 4383 3472 4860 663 741 -27 A O ATOM 1504 N ASP A 197 -6.777 -29.904 -3.852 1.00 19.03 A N ANISOU 1504 N ASP A 197 2655 1766 2810 351 474 -116 A N ATOM 1505 CA ASP A 197 -7.396 -29.224 -2.725 1.00 18.95 A C ANISOU 1505 CA ASP A 197 2581 1843 2775 310 376 -35 A C ATOM 1506 C ASP A 197 -7.515 -30.188 -1.542 1.00 19.51 A C ANISOU 1506 C ASP A 197 2634 1842 2938 338 374 58 A C ATOM 1507 O ASP A 197 -7.279 -31.389 -1.670 1.00 19.98 A O ANISOU 1507 O ASP A 197 2737 1768 3086 379 444 55 A O ATOM 1508 CB ASP A 197 -8.782 -28.697 -3.107 1.00 14.49 A C ANISOU 1508 CB ASP A 197 2059 1321 2126 199 308 -98 A C ATOM 1509 CG ASP A 197 -9.177 -27.460 -2.316 1.00 16.58 A C ANISOU 1509 CG ASP A 197 2251 1712 2336 171 224 -40 A C ATOM 1510 OD1 ASP A 197 -10.380 -27.097 -2.335 1.00 16.80 A O ANISOU 1510 OD1 ASP A 197 2293 1772 2319 94 169 -61 A O ATOM 1511 OD2 ASP A 197 -8.275 -26.811 -1.726 1.00 17.43 A O ANISOU 1511 OD2 ASP A 197 2287 1887 2447 223 214 23 A O ATOM 1512 N THR A 198 -7.891 -29.645 -0.382 1.00 17.12 A N ANISOU 1512 N THR A 198 2270 1626 2611 317 299 143 A N ATOM 1513 CA THR A 198 -8.189 -30.435 0.806 1.00 15.19 A C ANISOU 1513 CA THR A 198 2007 1338 2426 328 286 243 A C ATOM 1514 C THR A 198 -9.417 -29.832 1.465 1.00 15.32 A C ANISOU 1514 C THR A 198 2014 1435 2373 246 213 257 A C ATOM 1515 O THR A 198 -9.852 -28.735 1.111 1.00 15.89 A O ANISOU 1515 O THR A 198 2079 1596 2362 199 170 201 A O ATOM 1516 CB THR A 198 -7.023 -30.468 1.815 1.00 19.55 A C ANISOU 1516 CB THR A 198 2471 1937 3021 418 282 371 A C ATOM 1517 CG2 THR A 198 -5.847 -31.179 1.220 1.00 23.95 A C ANISOU 1517 CG2 THR A 198 3024 2406 3670 512 368 375 A C ATOM 1518 OG1 THR A 198 -6.598 -29.131 2.120 1.00 19.89 A O ANISOU 1518 OG1 THR A 198 2447 2128 2982 411 222 382 A O ATOM 1519 N THR A 199 -9.992 -30.560 2.420 1.00 15.85 A N ANISOU 1519 N THR A 199 2077 1465 2479 233 205 337 A N ATOM 1520 CA THR A 199 -11.157 -30.051 3.130 1.00 16.98 A C ANISOU 1520 CA THR A 199 2204 1687 2561 164 151 361 A C ATOM 1521 C THR A 199 -10.704 -29.315 4.382 1.00 14.61 A C ANISOU 1521 C THR A 199 1833 1513 2204 199 109 451 A C ATOM 1522 O THR A 199 -9.770 -29.741 5.070 1.00 14.79 A O ANISOU 1522 O THR A 199 1819 1537 2262 265 116 543 A O ATOM 1523 CB THR A 199 -12.111 -31.196 3.478 1.00 16.82 A C ANISOU 1523 CB THR A 199 2216 1568 2606 118 170 402 A C ATOM 1524 CG2 THR A 199 -13.305 -30.684 4.273 1.00 16.29 A C ANISOU 1524 CG2 THR A 199 2117 1592 2479 54 127 440 A C ATOM 1525 OG1 THR A 199 -12.593 -31.761 2.257 1.00 17.85 A O ANISOU 1525 OG1 THR A 199 2419 1589 2773 64 196 296 A O ATOM 1526 N ILE A 200 -11.360 -28.194 4.664 1.00 14.40 A N ANISOU 1526 N ILE A 200 1788 1595 2089 155 64 423 A N ATOM 1527 CA ILE A 200 -10.971 -27.337 5.773 1.00 12.65 A C ANISOU 1527 CA ILE A 200 1516 1497 1795 175 23 476 A C ATOM 1528 C ILE A 200 -11.568 -27.887 7.067 1.00 14.62 A C ANISOU 1528 C ILE A 200 1752 1772 2030 166 20 578 A C ATOM 1529 O ILE A 200 -12.710 -27.585 7.426 1.00 13.08 A O ANISOU 1529 O ILE A 200 1562 1617 1792 117 17 570 A O ATOM 1530 CB ILE A 200 -11.389 -25.882 5.508 1.00 13.66 A C ANISOU 1530 CB ILE A 200 1637 1711 1842 139 -11 395 A C ATOM 1531 CG1 ILE A 200 -10.999 -25.479 4.080 1.00 13.89 A C ANISOU 1531 CG1 ILE A 200 1686 1704 1889 137 -0 305 A C ATOM 1532 CG2 ILE A 200 -10.716 -24.960 6.537 1.00 11.99 A C ANISOU 1532 CG2 ILE A 200 1384 1612 1558 158 -52 428 A C ATOM 1533 CD1 ILE A 200 -11.731 -24.240 3.577 1.00 11.27 A C ANISOU 1533 CD1 ILE A 200 1357 1425 1500 93 -25 233 A C ATOM 1534 N THR A 201 -10.773 -28.684 7.777 1.00 14.16 A N ANISOU 1534 N THR A 201 1671 1700 2009 218 25 685 A N ATOM 1535 CA THR A 201 -11.262 -29.478 8.912 1.00 13.77 A C ANISOU 1535 CA THR A 201 1614 1657 1962 214 33 806 A C ATOM 1536 C THR A 201 -11.874 -28.607 9.999 1.00 12.86 A C ANISOU 1536 C THR A 201 1481 1684 1722 181 2 824 A C ATOM 1537 O THR A 201 -12.956 -28.921 10.527 1.00 14.87 A O ANISOU 1537 O THR A 201 1743 1945 1961 143 25 864 A O ATOM 1538 CB THR A 201 -10.100 -30.295 9.455 1.00 16.09 A C ANISOU 1538 CB THR A 201 1874 1928 2310 287 34 929 A C ATOM 1539 CG2 THR A 201 -10.533 -31.199 10.611 1.00 16.01 A C ANISOU 1539 CG2 THR A 201 1855 1921 2305 284 44 1064 A C ATOM 1540 OG1 THR A 201 -9.578 -31.082 8.381 1.00 16.31 A O ANISOU 1540 OG1 THR A 201 1925 1810 2461 325 82 896 A O ATOM 1541 N VAL A 202 -11.201 -27.510 10.361 1.00 11.47 A N ANISOU 1541 N VAL A 202 1281 1620 1455 193 -44 793 A N ATOM 1542 CA VAL A 202 -11.702 -26.720 11.485 1.00 12.10 A C ANISOU 1542 CA VAL A 202 1357 1832 1408 167 -66 802 A C ATOM 1543 C VAL A 202 -13.054 -26.121 11.131 1.00 10.91 A C ANISOU 1543 C VAL A 202 1230 1679 1237 119 -36 715 A C ATOM 1544 O VAL A 202 -13.912 -25.951 12.002 1.00 11.25 A O ANISOU 1544 O VAL A 202 1273 1790 1210 98 -16 743 A O ATOM 1545 CB VAL A 202 -10.697 -25.630 11.904 1.00 12.71 A C ANISOU 1545 CB VAL A 202 1413 2019 1397 176 -126 769 A C ATOM 1546 CG1 VAL A 202 -10.442 -24.635 10.753 1.00 15.97 A C ANISOU 1546 CG1 VAL A 202 1833 2402 1834 165 -135 639 A C ATOM 1547 CG2 VAL A 202 -11.170 -24.910 13.173 1.00 13.79 A C ANISOU 1547 CG2 VAL A 202 1561 2289 1390 148 -142 772 A C ATOM 1548 N ASN A 203 -13.277 -25.822 9.847 1.00 14.32 A N ANISOU 1548 N ASN A 203 1675 2037 1729 104 -28 618 A N ATOM 1549 CA ASN A 203 -14.557 -25.250 9.437 1.00 12.33 A C ANISOU 1549 CA ASN A 203 1431 1787 1468 62 -7 550 A C ATOM 1550 C ASN A 203 -15.675 -26.279 9.517 1.00 10.34 A C ANISOU 1550 C ASN A 203 1177 1480 1270 27 32 609 A C ATOM 1551 O ASN A 203 -16.792 -25.957 9.947 1.00 11.07 A O ANISOU 1551 O ASN A 203 1254 1622 1330 -1 55 614 A O ATOM 1552 CB ASN A 203 -14.470 -24.687 8.018 1.00 13.46 A C ANISOU 1552 CB ASN A 203 1585 1877 1652 51 -19 447 A C ATOM 1553 CG ASN A 203 -13.688 -23.384 7.943 1.00 11.22 A C ANISOU 1553 CG ASN A 203 1297 1654 1313 69 -51 384 A C ATOM 1554 ND2 ASN A 203 -13.629 -22.822 6.740 1.00 10.10 A N ANISOU 1554 ND2 ASN A 203 1163 1476 1200 60 -58 308 A N ATOM 1555 OD1 ASN A 203 -13.175 -22.875 8.951 1.00 10.81 A O ANISOU 1555 OD1 ASN A 203 1236 1682 1190 84 -72 403 A O ATOM 1556 N VAL A 204 -15.407 -27.514 9.081 1.00 11.79 A N ANISOU 1556 N VAL A 204 1376 1557 1547 27 44 652 A N ATOM 1557 CA VAL A 204 -16.390 -28.582 9.234 1.00 14.02 A C ANISOU 1557 CA VAL A 204 1658 1774 1893 -17 78 718 A C ATOM 1558 C VAL A 204 -16.784 -28.736 10.696 1.00 14.72 A C ANISOU 1558 C VAL A 204 1722 1951 1920 -13 99 830 A C ATOM 1559 O VAL A 204 -17.966 -28.905 11.013 1.00 13.21 A O ANISOU 1559 O VAL A 204 1511 1776 1733 -58 131 865 A O ATOM 1560 CB VAL A 204 -15.860 -29.910 8.658 1.00 13.58 A C ANISOU 1560 CB VAL A 204 1634 1573 1954 -10 94 747 A C ATOM 1561 CG1 VAL A 204 -16.899 -31.003 8.822 1.00 14.33 A C ANISOU 1561 CG1 VAL A 204 1732 1587 2126 -70 127 814 A C ATOM 1562 CG2 VAL A 204 -15.541 -29.768 7.179 1.00 13.52 A C ANISOU 1562 CG2 VAL A 204 1661 1487 1989 -19 84 625 A C ATOM 1563 N LEU A 205 -15.800 -28.726 11.606 1.00 12.46 A N ANISOU 1563 N LEU A 205 1431 1728 1574 38 82 899 A N ATOM 1564 CA LEU A 205 -16.136 -28.830 13.023 1.00 14.17 A C ANISOU 1564 CA LEU A 205 1630 2048 1704 40 100 1007 A C ATOM 1565 C LEU A 205 -17.002 -27.659 13.458 1.00 13.43 A C ANISOU 1565 C LEU A 205 1528 2070 1504 20 117 943 A C ATOM 1566 O LEU A 205 -17.991 -27.851 14.165 1.00 15.21 A O ANISOU 1566 O LEU A 205 1737 2344 1699 -4 165 1005 A O ATOM 1567 CB LEU A 205 -14.870 -28.921 13.887 1.00 13.83 A C ANISOU 1567 CB LEU A 205 1582 2072 1602 91 62 1075 A C ATOM 1568 CG LEU A 205 -13.975 -30.128 13.653 1.00 14.46 A C ANISOU 1568 CG LEU A 205 1658 2042 1795 126 56 1140 A C ATOM 1569 CD1 LEU A 205 -12.633 -29.997 14.381 1.00 14.96 A C ANISOU 1569 CD1 LEU A 205 1697 2183 1804 173 6 1168 A C ATOM 1570 CD2 LEU A 205 -14.693 -31.369 14.114 1.00 15.54 A C ANISOU 1570 CD2 LEU A 205 1793 2111 2000 104 99 1229 A C ATOM 1571 N ALA A 206 -16.673 -26.441 13.000 1.00 12.99 A N ANISOU 1571 N ALA A 206 1482 2052 1402 32 88 821 A N ATOM 1572 CA ALA A 206 -17.495 -25.284 13.344 1.00 12.03 A C ANISOU 1572 CA ALA A 206 1356 2018 1198 24 114 752 A C ATOM 1573 C ALA A 206 -18.936 -25.479 12.889 1.00 12.90 A C ANISOU 1573 C ALA A 206 1436 2089 1375 -14 163 752 A C ATOM 1574 O ALA A 206 -19.879 -25.143 13.614 1.00 13.83 A O ANISOU 1574 O ALA A 206 1532 2283 1438 -19 216 773 A O ATOM 1575 CB ALA A 206 -16.913 -24.017 12.718 1.00 14.15 A C ANISOU 1575 CB ALA A 206 1639 2295 1441 39 76 624 A C ATOM 1576 N TRP A 207 -19.109 -26.028 11.693 1.00 12.61 A N ANISOU 1576 N TRP A 207 1396 1942 1454 -44 146 728 A N ATOM 1577 CA TRP A 207 -20.423 -26.232 11.101 1.00 13.74 A C ANISOU 1577 CA TRP A 207 1502 2048 1670 -95 171 726 A C ATOM 1578 C TRP A 207 -21.175 -27.339 11.830 1.00 14.82 A C ANISOU 1578 C TRP A 207 1613 2178 1840 -131 217 850 A C ATOM 1579 O TRP A 207 -22.397 -27.258 12.028 1.00 16.28 A O ANISOU 1579 O TRP A 207 1747 2400 2037 -163 259 880 A O ATOM 1580 CB TRP A 207 -20.221 -26.556 9.628 1.00 12.69 A C ANISOU 1580 CB TRP A 207 1387 1804 1630 -125 129 659 A C ATOM 1581 CG TRP A 207 -21.416 -26.988 8.863 1.00 13.70 A C ANISOU 1581 CG TRP A 207 1482 1882 1841 -196 132 659 A C ATOM 1582 CD1 TRP A 207 -22.399 -26.194 8.314 1.00 14.31 A C ANISOU 1582 CD1 TRP A 207 1514 2000 1924 -220 126 614 A C ATOM 1583 CD2 TRP A 207 -21.714 -28.320 8.476 1.00 13.81 A C ANISOU 1583 CD2 TRP A 207 1505 1791 1951 -258 131 703 A C ATOM 1584 CE2 TRP A 207 -22.911 -28.284 7.724 1.00 14.21 A C ANISOU 1584 CE2 TRP A 207 1512 1832 2053 -330 117 680 A C ATOM 1585 CE3 TRP A 207 -21.094 -29.551 8.705 1.00 14.04 A C ANISOU 1585 CE3 TRP A 207 1573 1726 2036 -259 141 764 A C ATOM 1586 NE1 TRP A 207 -23.308 -26.976 7.639 1.00 15.77 A N ANISOU 1586 NE1 TRP A 207 1671 2126 2194 -301 114 634 A N ATOM 1587 CZ2 TRP A 207 -23.487 -29.429 7.197 1.00 18.25 A C ANISOU 1587 CZ2 TRP A 207 2025 2247 2663 -418 107 703 A C ATOM 1588 CZ3 TRP A 207 -21.682 -30.691 8.189 1.00 17.50 A C ANISOU 1588 CZ3 TRP A 207 2018 2051 2581 -337 143 787 A C ATOM 1589 CH2 TRP A 207 -22.858 -30.619 7.435 1.00 15.57 A C ANISOU 1589 CH2 TRP A 207 1737 1802 2378 -422 123 750 A C ATOM 1590 N LEU A 208 -20.449 -28.356 12.289 1.00 14.69 A N ANISOU 1590 N LEU A 208 1622 2118 1843 -121 214 937 A N ATOM 1591 CA LEU A 208 -21.086 -29.365 13.133 1.00 14.44 A C ANISOU 1591 CA LEU A 208 1566 2085 1835 -151 262 1075 A C ATOM 1592 C LEU A 208 -21.599 -28.745 14.431 1.00 15.42 A C ANISOU 1592 C LEU A 208 1669 2353 1838 -124 304 1096 A C ATOM 1593 O LEU A 208 -22.677 -29.107 14.917 1.00 17.85 A O ANISOU 1593 O LEU A 208 1939 2679 2163 -153 348 1142 A O ATOM 1594 CB LEU A 208 -20.110 -30.503 13.418 1.00 15.93 A C ANISOU 1594 CB LEU A 208 1789 2194 2071 -127 243 1147 A C ATOM 1595 CG LEU A 208 -19.855 -31.427 12.225 1.00 17.53 A C ANISOU 1595 CG LEU A 208 2018 2223 2419 -159 226 1132 A C ATOM 1596 CD1 LEU A 208 -18.877 -32.524 12.605 1.00 16.56 A C ANISOU 1596 CD1 LEU A 208 1924 2022 2346 -116 220 1199 A C ATOM 1597 CD2 LEU A 208 -21.144 -32.038 11.708 1.00 18.15 A C ANISOU 1597 CD2 LEU A 208 2075 2227 2595 -247 246 1128 A C ATOM 1598 N TYR A 209 -20.846 -27.797 14.999 1.00 15.75 A N ANISOU 1598 N TYR A 209 1737 2494 1754 -72 290 1052 A N ATOM 1599 CA TYR A 209 -21.345 -27.062 16.156 1.00 17.36 A C ANISOU 1599 CA TYR A 209 1936 2824 1835 -49 333 1037 A C ATOM 1600 C TYR A 209 -22.555 -26.206 15.799 1.00 16.77 A C ANISOU 1600 C TYR A 209 1821 2782 1769 -60 385 978 A C ATOM 1601 O TYR A 209 -23.512 -26.139 16.576 1.00 15.93 A O ANISOU 1601 O TYR A 209 1687 2733 1632 -59 446 1001 A O ATOM 1602 CB TYR A 209 -20.244 -26.192 16.752 1.00 16.92 A C ANISOU 1602 CB TYR A 209 1927 2852 1648 -5 296 978 A C ATOM 1603 CG TYR A 209 -19.300 -26.972 17.627 1.00 17.10 A C ANISOU 1603 CG TYR A 209 1971 2891 1636 9 258 1053 A C ATOM 1604 CD1 TYR A 209 -19.707 -27.473 18.860 1.00 17.25 A C ANISOU 1604 CD1 TYR A 209 1986 2970 1598 7 293 1128 A C ATOM 1605 CD2 TYR A 209 -17.990 -27.192 17.228 1.00 15.82 A C ANISOU 1605 CD2 TYR A 209 1824 2687 1500 29 189 1055 A C ATOM 1606 CE1 TYR A 209 -18.832 -28.187 19.659 1.00 20.82 A C ANISOU 1606 CE1 TYR A 209 2449 3442 2019 20 255 1208 A C ATOM 1607 CE2 TYR A 209 -17.110 -27.900 18.019 1.00 19.33 A C ANISOU 1607 CE2 TYR A 209 2272 3148 1924 46 154 1132 A C ATOM 1608 CZ TYR A 209 -17.535 -28.396 19.233 1.00 18.58 A C ANISOU 1608 CZ TYR A 209 2173 3115 1771 40 184 1210 A C ATOM 1609 OH TYR A 209 -16.660 -29.106 20.020 1.00 21.18 A O ANISOU 1609 OH TYR A 209 2500 3467 2080 57 147 1297 A O ATOM 1610 N ALA A 210 -22.509 -25.504 14.658 1.00 16.71 A N ANISOU 1610 N ALA A 210 1805 2738 1805 -63 362 897 A N ATOM 1611 CA ALA A 210 -23.692 -24.795 14.180 1.00 16.54 A C ANISOU 1611 CA ALA A 210 1729 2730 1826 -71 400 848 A C ATOM 1612 C ALA A 210 -24.899 -25.726 14.129 1.00 16.53 A C ANISOU 1612 C ALA A 210 1663 2697 1921 -125 434 936 A C ATOM 1613 O ALA A 210 -26.003 -25.369 14.567 1.00 16.03 A O ANISOU 1613 O ALA A 210 1550 2686 1854 -116 490 941 A O ATOM 1614 CB ALA A 210 -23.421 -24.191 12.799 1.00 17.33 A C ANISOU 1614 CB ALA A 210 1837 2754 1995 -73 335 738 A C ATOM 1615 N ALA A 211 -24.698 -26.940 13.617 1.00 14.77 A N ANISOU 1615 N ALA A 211 1445 2373 1793 -179 394 992 A N ATOM 1616 CA ALA A 211 -25.782 -27.907 13.540 1.00 16.65 A C ANISOU 1616 CA ALA A 211 1634 2561 2131 -240 408 1055 A C ATOM 1617 C ALA A 211 -26.333 -28.217 14.923 1.00 17.40 A C ANISOU 1617 C ALA A 211 1716 2728 2169 -221 469 1128 A C ATOM 1618 O ALA A 211 -27.550 -28.161 15.152 1.00 17.70 A O ANISOU 1618 O ALA A 211 1690 2801 2233 -238 514 1152 A O ATOM 1619 CB ALA A 211 -25.287 -29.180 12.864 1.00 15.74 A C ANISOU 1619 CB ALA A 211 1552 2311 2118 -296 358 1087 A C ATOM 1620 N VAL A 212 -25.446 -28.537 15.866 1.00 17.27 A N ANISOU 1620 N VAL A 212 1752 2738 2070 -184 470 1168 A N ATOM 1621 CA VAL A 212 -25.900 -28.846 17.222 1.00 18.60 A C ANISOU 1621 CA VAL A 212 1913 2983 2172 -170 526 1240 A C ATOM 1622 C VAL A 212 -26.657 -27.666 17.811 1.00 18.89 A C ANISOU 1622 C VAL A 212 1926 3132 2118 -130 593 1189 A C ATOM 1623 O VAL A 212 -27.713 -27.838 18.431 1.00 21.20 A O ANISOU 1623 O VAL A 212 2173 3468 2415 -139 655 1239 A O ATOM 1624 CB VAL A 212 -24.712 -29.249 18.116 1.00 20.54 A C ANISOU 1624 CB VAL A 212 2220 3253 2332 -135 502 1284 A C ATOM 1625 CG1 VAL A 212 -25.183 -29.395 19.553 1.00 20.44 A C ANISOU 1625 CG1 VAL A 212 2202 3339 2225 -121 562 1351 A C ATOM 1626 CG2 VAL A 212 -24.081 -30.561 17.635 1.00 19.06 A C ANISOU 1626 CG2 VAL A 212 2049 2939 2254 -164 454 1351 A C ATOM 1627 N ILE A 213 -26.133 -26.448 17.626 1.00 18.66 A N ANISOU 1627 N ILE A 213 1929 3147 2014 -85 585 1087 A N ATOM 1628 CA ILE A 213 -26.821 -25.267 18.148 1.00 18.94 A C ANISOU 1628 CA ILE A 213 1952 3269 1974 -40 656 1022 A C ATOM 1629 C ILE A 213 -28.225 -25.181 17.575 1.00 20.97 A C ANISOU 1629 C ILE A 213 2119 3508 2340 -60 695 1035 A C ATOM 1630 O ILE A 213 -29.177 -24.803 18.277 1.00 23.36 A O ANISOU 1630 O ILE A 213 2388 3874 2616 -37 775 1043 A O ATOM 1631 CB ILE A 213 -25.990 -24.002 17.847 1.00 22.68 A C ANISOU 1631 CB ILE A 213 2478 3765 2374 5 633 901 A C ATOM 1632 CG1 ILE A 213 -24.687 -24.041 18.659 1.00 22.28 A C ANISOU 1632 CG1 ILE A 213 2511 3755 2199 22 592 891 A C ATOM 1633 CG2 ILE A 213 -26.789 -22.737 18.157 1.00 23.38 A C ANISOU 1633 CG2 ILE A 213 2553 3910 2422 53 712 820 A C ATOM 1634 CD1 ILE A 213 -23.740 -22.901 18.388 1.00 22.77 A C ANISOU 1634 CD1 ILE A 213 2629 3834 2190 53 554 774 A C ATOM 1635 N ASN A 214 -28.393 -25.606 16.327 1.00 20.27 A N ANISOU 1635 N ASN A 214 1989 3334 2379 -110 638 1043 A N ATOM 1636 CA ASN A 214 -29.660 -25.532 15.621 1.00 20.55 A C ANISOU 1636 CA ASN A 214 1934 3351 2524 -140 647 1053 A C ATOM 1637 C ASN A 214 -30.508 -26.796 15.744 1.00 21.54 A C ANISOU 1637 C ASN A 214 2006 3441 2736 -209 650 1156 A C ATOM 1638 O ASN A 214 -31.560 -26.888 15.095 1.00 23.61 A O ANISOU 1638 O ASN A 214 2189 3685 3097 -250 641 1172 A O ATOM 1639 CB ASN A 214 -29.395 -25.201 14.163 1.00 24.46 A C ANISOU 1639 CB ASN A 214 2416 3782 3097 -165 573 994 A C ATOM 1640 CG ASN A 214 -29.395 -23.707 13.919 1.00 25.82 A C ANISOU 1640 CG ASN A 214 2582 3998 3230 -96 595 903 A C ATOM 1641 ND2 ASN A 214 -28.212 -23.106 13.851 1.00 23.81 A N ANISOU 1641 ND2 ASN A 214 2400 3747 2901 -59 574 834 A N ATOM 1642 OD1 ASN A 214 -30.464 -23.094 13.848 1.00 26.06 A O ANISOU 1642 OD1 ASN A 214 2544 4057 3299 -73 634 898 A O ATOM 1643 N GLY A 215 -30.090 -27.765 16.556 1.00 21.36 A N ANISOU 1643 N GLY A 215 2024 3411 2682 -225 659 1228 A N ATOM 1644 CA GLY A 215 -30.940 -28.884 16.911 1.00 21.38 A C ANISOU 1644 CA GLY A 215 1979 3391 2755 -282 681 1331 A C ATOM 1645 C GLY A 215 -30.646 -30.184 16.196 1.00 24.06 A C ANISOU 1645 C GLY A 215 2333 3606 3204 -362 613 1372 A C ATOM 1646 O GLY A 215 -31.355 -31.169 16.431 1.00 25.02 A O ANISOU 1646 O GLY A 215 2416 3694 3395 -418 628 1454 A O ATOM 1647 N ASP A 216 -29.642 -30.220 15.327 1.00 20.16 A N ANISOU 1647 N ASP A 216 1893 3035 2731 -369 545 1314 A N ATOM 1648 CA ASP A 216 -29.219 -31.443 14.650 1.00 21.56 A C ANISOU 1648 CA ASP A 216 2105 3077 3009 -437 489 1336 A C ATOM 1649 C ASP A 216 -28.218 -32.152 15.555 1.00 22.93 A C ANISOU 1649 C ASP A 216 2344 3232 3134 -402 499 1401 A C ATOM 1650 O ASP A 216 -27.090 -31.679 15.726 1.00 24.03 A O ANISOU 1650 O ASP A 216 2540 3397 3195 -342 482 1367 A O ATOM 1651 CB ASP A 216 -28.586 -31.126 13.295 1.00 22.51 A C ANISOU 1651 CB ASP A 216 2258 3124 3171 -456 419 1240 A C ATOM 1652 CG ASP A 216 -29.613 -30.947 12.200 1.00 26.34 A C ANISOU 1652 CG ASP A 216 2680 3588 3740 -524 383 1195 A C ATOM 1653 OD1 ASP A 216 -30.773 -31.325 12.431 1.00 29.11 A O ANISOU 1653 OD1 ASP A 216 2964 3958 4139 -568 405 1247 A O ATOM 1654 OD2 ASP A 216 -29.272 -30.384 11.132 1.00 23.48 A O ANISOU 1654 OD2 ASP A 216 2330 3202 3389 -533 330 1111 A O ATOM 1655 N ARG A 217 -28.621 -33.296 16.126 1.00 22.02 A N ANISOU 1655 N ARG A 217 2218 3077 3072 -441 523 1498 A N ATOM 1656 CA ARG A 217 -27.794 -33.993 17.106 1.00 22.71 A C ANISOU 1656 CA ARG A 217 2354 3161 3115 -404 535 1580 A C ATOM 1657 C ARG A 217 -27.518 -35.452 16.766 1.00 23.91 A C ANISOU 1657 C ARG A 217 2535 3158 3389 -456 510 1637 A C ATOM 1658 O ARG A 217 -26.843 -36.127 17.546 1.00 24.26 A O ANISOU 1658 O ARG A 217 2614 3190 3415 -423 518 1717 A O ATOM 1659 CB ARG A 217 -28.455 -33.939 18.497 1.00 24.04 A C ANISOU 1659 CB ARG A 217 2486 3450 3197 -381 606 1666 A C ATOM 1660 CG ARG A 217 -28.800 -32.538 18.971 1.00 25.55 A C ANISOU 1660 CG ARG A 217 2658 3787 3264 -325 649 1606 A C ATOM 1661 CD ARG A 217 -29.325 -32.547 20.405 1.00 26.08 A C ANISOU 1661 CD ARG A 217 2706 3969 3234 -300 726 1686 A C ATOM 1662 NE ARG A 217 -28.387 -33.177 21.332 1.00 25.82 A N ANISOU 1662 NE ARG A 217 2728 3950 3133 -274 717 1762 A N ATOM 1663 CZ ARG A 217 -27.475 -32.519 22.037 1.00 25.57 A C ANISOU 1663 CZ ARG A 217 2751 4007 2956 -213 709 1730 A C ATOM 1664 NH1 ARG A 217 -27.343 -31.204 21.906 1.00 24.59 A N ANISOU 1664 NH1 ARG A 217 2645 3954 2743 -173 714 1615 A N ATOM 1665 NH2 ARG A 217 -26.672 -33.178 22.854 1.00 26.40 A N ANISOU 1665 NH2 ARG A 217 2894 4128 3010 -196 691 1812 A N ATOM 1666 N TRP A 218 -28.022 -35.961 15.641 1.00 23.53 A N ANISOU 1666 N TRP A 218 2480 2993 3467 -537 480 1594 A N ATOM 1667 CA TRP A 218 -28.002 -37.399 15.404 1.00 24.71 A C ANISOU 1667 CA TRP A 218 2659 2989 3738 -598 472 1644 A C ATOM 1668 C TRP A 218 -26.596 -37.957 15.234 1.00 24.43 A C ANISOU 1668 C TRP A 218 2706 2850 3726 -551 445 1640 A C ATOM 1669 O TRP A 218 -26.388 -39.157 15.448 1.00 25.68 A O ANISOU 1669 O TRP A 218 2894 2898 3964 -570 455 1710 A O ATOM 1670 CB TRP A 218 -28.841 -37.738 14.175 1.00 25.25 A C ANISOU 1670 CB TRP A 218 2711 2960 3921 -705 438 1575 A C ATOM 1671 CG TRP A 218 -28.363 -37.105 12.880 1.00 23.41 A C ANISOU 1671 CG TRP A 218 2513 2685 3695 -711 382 1441 A C ATOM 1672 CD1 TRP A 218 -28.854 -35.979 12.288 1.00 25.19 A C ANISOU 1672 CD1 TRP A 218 2692 2997 3881 -716 359 1365 A C ATOM 1673 CD2 TRP A 218 -27.327 -37.590 12.020 1.00 22.97 A C ANISOU 1673 CD2 TRP A 218 2546 2489 3693 -712 345 1374 A C ATOM 1674 CE2 TRP A 218 -27.244 -36.708 10.925 1.00 23.36 A C ANISOU 1674 CE2 TRP A 218 2599 2553 3725 -724 300 1257 A C ATOM 1675 CE3 TRP A 218 -26.461 -38.687 12.069 1.00 24.57 A C ANISOU 1675 CE3 TRP A 218 2823 2552 3959 -697 351 1403 A C ATOM 1676 NE1 TRP A 218 -28.182 -35.728 11.112 1.00 22.84 A N ANISOU 1676 NE1 TRP A 218 2447 2628 3603 -726 306 1257 A N ATOM 1677 CZ2 TRP A 218 -26.325 -36.885 9.896 1.00 23.01 A C ANISOU 1677 CZ2 TRP A 218 2634 2393 3717 -725 263 1164 A C ATOM 1678 CZ3 TRP A 218 -25.554 -38.862 11.042 1.00 24.89 A C ANISOU 1678 CZ3 TRP A 218 2941 2472 4042 -691 320 1308 A C ATOM 1679 CH2 TRP A 218 -25.495 -37.964 9.971 1.00 24.24 A C ANISOU 1679 CH2 TRP A 218 2864 2411 3934 -706 278 1188 A C ATOM 1680 N PHE A 219 -25.646 -37.125 14.828 1.00 22.96 A N ANISOU 1680 N PHE A 219 2553 2691 3479 -490 415 1563 A N ATOM 1681 CA PHE A 219 -24.259 -37.517 14.629 1.00 25.00 A C ANISOU 1681 CA PHE A 219 2879 2865 3756 -433 390 1556 A C ATOM 1682 C PHE A 219 -23.425 -37.447 15.904 1.00 23.01 A C ANISOU 1682 C PHE A 219 2627 2710 3406 -344 402 1647 A C ATOM 1683 O PHE A 219 -22.232 -37.769 15.865 1.00 24.64 A O ANISOU 1683 O PHE A 219 2874 2863 3625 -287 381 1656 A O ATOM 1684 CB PHE A 219 -23.633 -36.628 13.553 1.00 23.38 A C ANISOU 1684 CB PHE A 219 2702 2649 3533 -413 350 1434 A C ATOM 1685 CG PHE A 219 -23.805 -35.159 13.818 1.00 19.88 A C ANISOU 1685 CG PHE A 219 2220 2372 2963 -377 349 1393 A C ATOM 1686 CD1 PHE A 219 -22.948 -34.484 14.675 1.00 19.47 A C ANISOU 1686 CD1 PHE A 219 2175 2433 2790 -292 349 1416 A C ATOM 1687 CD2 PHE A 219 -24.846 -34.455 13.223 1.00 20.71 A C ANISOU 1687 CD2 PHE A 219 2279 2521 3071 -431 347 1330 A C ATOM 1688 CE1 PHE A 219 -23.115 -33.127 14.923 1.00 19.94 A C ANISOU 1688 CE1 PHE A 219 2211 2635 2731 -262 354 1364 A C ATOM 1689 CE2 PHE A 219 -25.021 -33.101 13.466 1.00 19.46 A C ANISOU 1689 CE2 PHE A 219 2086 2503 2804 -390 355 1291 A C ATOM 1690 CZ PHE A 219 -24.154 -32.433 14.318 1.00 18.12 A C ANISOU 1690 CZ PHE A 219 1937 2434 2512 -306 364 1303 A C ATOM 1691 N LEU A 220 -24.004 -36.999 17.013 1.00 23.48 A N ANISOU 1691 N LEU A 220 2643 2917 3363 -331 435 1707 A N ATOM 1692 CA LEU A 220 -23.278 -36.951 18.271 1.00 24.07 A C ANISOU 1692 CA LEU A 220 2722 3095 3330 -261 441 1789 A C ATOM 1693 C LEU A 220 -23.097 -38.354 18.835 1.00 25.77 A C ANISOU 1693 C LEU A 220 2944 3225 3624 -266 456 1916 A C ATOM 1694 O LEU A 220 -23.813 -39.296 18.487 1.00 28.73 A O ANISOU 1694 O LEU A 220 3314 3483 4121 -331 476 1948 A O ATOM 1695 CB LEU A 220 -24.011 -36.084 19.295 1.00 24.33 A C ANISOU 1695 CB LEU A 220 2716 3304 3223 -251 481 1805 A C ATOM 1696 CG LEU A 220 -24.080 -34.603 18.930 1.00 22.84 A C ANISOU 1696 CG LEU A 220 2525 3212 2941 -230 473 1685 A C ATOM 1697 CD1 LEU A 220 -24.740 -33.838 20.032 1.00 23.41 A C ANISOU 1697 CD1 LEU A 220 2573 3446 2878 -212 525 1698 A C ATOM 1698 CD2 LEU A 220 -22.663 -34.077 18.683 1.00 21.77 A C ANISOU 1698 CD2 LEU A 220 2434 3085 2752 -171 418 1628 A C ATOM 1699 N ASN A 221 -22.130 -38.476 19.734 1.00 26.32 A N ANISOU 1699 N ASN A 221 3022 3357 3622 -199 442 1988 A N ATOM 1700 CA ASN A 221 -21.844 -39.744 20.375 1.00 28.12 A C ANISOU 1700 CA ASN A 221 3251 3519 3916 -190 455 2123 A C ATOM 1701 C ASN A 221 -21.117 -39.476 21.680 1.00 30.87 A C ANISOU 1701 C ASN A 221 3588 4018 4122 -127 442 2206 A C ATOM 1702 O ASN A 221 -20.664 -38.359 21.941 1.00 27.80 A O ANISOU 1702 O ASN A 221 3204 3762 3598 -92 416 2141 A O ATOM 1703 CB ASN A 221 -21.053 -40.655 19.431 1.00 34.47 A C ANISOU 1703 CB ASN A 221 4094 4131 4872 -178 433 2107 A C ATOM 1704 CG ASN A 221 -19.855 -39.949 18.781 1.00 38.14 A C ANISOU 1704 CG ASN A 221 4583 4600 5308 -116 386 2012 A C ATOM 1705 ND2 ASN A 221 -19.793 -40.033 17.454 1.00 35.39 A N ANISOU 1705 ND2 ASN A 221 4270 4113 5062 -139 377 1907 A N ATOM 1706 OD1 ASN A 221 -19.029 -39.298 19.446 1.00 38.76 A O ANISOU 1706 OD1 ASN A 221 4650 4808 5268 -56 357 2027 A O ATOM 1707 N ARG A 222 -21.059 -40.506 22.520 1.00 30.60 A N ANISOU 1707 N ARG A 222 3542 3968 4118 -121 461 2351 A N ATOM 1708 CA ARG A 222 -20.278 -40.440 23.745 1.00 32.95 A C ANISOU 1708 CA ARG A 222 3829 4398 4292 -67 441 2446 A C ATOM 1709 C ARG A 222 -18.825 -40.834 23.533 1.00 34.97 A C ANISOU 1709 C ARG A 222 4093 4594 4599 -2 389 2470 A C ATOM 1710 O ARG A 222 -18.002 -40.588 24.418 1.00 41.56 A O ANISOU 1710 O ARG A 222 4915 5552 5322 43 354 2527 A O ATOM 1711 CB ARG A 222 -20.915 -41.323 24.824 1.00 35.72 A C ANISOU 1711 CB ARG A 222 4155 4777 4641 -89 487 2606 A C ATOM 1712 CG ARG A 222 -22.050 -40.626 25.524 1.00 36.29 A C ANISOU 1712 CG ARG A 222 4209 4993 4586 -126 535 2599 A C ATOM 1713 CD ARG A 222 -21.553 -39.823 26.711 1.00 39.75 A C ANISOU 1713 CD ARG A 222 4654 5633 4815 -85 519 2617 A C ATOM 1714 NE ARG A 222 -21.539 -40.629 27.930 1.00 43.71 A N ANISOU 1714 NE ARG A 222 5139 6194 5273 -80 539 2789 A N ATOM 1715 CZ ARG A 222 -22.386 -40.462 28.941 1.00 42.40 A C ANISOU 1715 CZ ARG A 222 4963 6155 4992 -102 596 2848 A C ATOM 1716 NH1 ARG A 222 -23.321 -39.519 28.874 1.00 44.81 A N ANISOU 1716 NH1 ARG A 222 5269 6536 5220 -128 642 2746 A N ATOM 1717 NH2 ARG A 222 -22.305 -41.240 30.013 1.00 45.96 A N ANISOU 1717 NH2 ARG A 222 5399 6657 5405 -97 611 3014 A N ATOM 1718 N PHE A 223 -18.500 -41.417 22.378 1.00 39.17 A N ANISOU 1718 N PHE A 223 4646 4944 5292 0 385 2423 A N ATOM 1719 CA PHE A 223 -17.118 -41.688 22.005 1.00 39.25 A C ANISOU 1719 CA PHE A 223 4660 4891 5361 69 345 2424 A C ATOM 1720 C PHE A 223 -16.291 -40.413 22.102 1.00 36.33 A C ANISOU 1720 C PHE A 223 4286 4669 4850 108 291 2342 A C ATOM 1721 O PHE A 223 -16.799 -39.297 21.941 1.00 33.24 A O ANISOU 1721 O PHE A 223 3905 4368 4358 80 287 2236 A O ATOM 1722 CB PHE A 223 -17.026 -42.191 20.558 1.00 38.81 A C ANISOU 1722 CB PHE A 223 4642 4627 5476 60 357 2334 A C ATOM 1723 CG PHE A 223 -17.874 -43.397 20.263 1.00 42.21 A C ANISOU 1723 CG PHE A 223 5092 4889 6056 5 406 2381 A C ATOM 1724 CD1 PHE A 223 -17.496 -44.664 20.672 1.00 46.61 A C ANISOU 1724 CD1 PHE A 223 5645 5343 6719 32 426 2512 A C ATOM 1725 CD2 PHE A 223 -19.036 -43.257 19.520 1.00 43.44 A C ANISOU 1725 CD2 PHE A 223 5270 4983 6253 -79 430 2291 A C ATOM 1726 CE1 PHE A 223 -18.290 -45.769 20.374 1.00 48.39 A C ANISOU 1726 CE1 PHE A 223 5896 5402 7087 -28 471 2547 A C ATOM 1727 CE2 PHE A 223 -19.836 -44.342 19.219 1.00 44.03 A C ANISOU 1727 CE2 PHE A 223 5364 4901 6463 -146 468 2324 A C ATOM 1728 CZ PHE A 223 -19.464 -45.605 19.645 1.00 51.25 A C ANISOU 1728 CZ PHE A 223 6283 5708 7483 -122 489 2449 A C ATOM 1729 N THR A 224 -14.994 -40.585 22.331 1.00 32.97 A N ANISOU 1729 N THR A 224 3841 4262 4426 172 249 2391 A N ATOM 1730 CA THR A 224 -14.051 -39.504 22.106 1.00 34.12 A C ANISOU 1730 CA THR A 224 3982 4500 4483 205 193 2298 A C ATOM 1731 C THR A 224 -12.868 -40.073 21.336 1.00 33.43 A C ANISOU 1731 C THR A 224 3884 4289 4530 266 178 2301 A C ATOM 1732 O THR A 224 -12.789 -41.277 21.081 1.00 34.22 A O ANISOU 1732 O THR A 224 3984 4238 4779 285 213 2374 A O ATOM 1733 CB THR A 224 -13.597 -38.854 23.422 1.00 36.89 A C ANISOU 1733 CB THR A 224 4307 5058 4649 215 147 2351 A C ATOM 1734 CG2 THR A 224 -12.681 -39.799 24.202 1.00 33.95 A C ANISOU 1734 CG2 THR A 224 3893 4695 4310 263 125 2512 A C ATOM 1735 OG1 THR A 224 -12.897 -37.632 23.136 1.00 34.21 A O ANISOU 1735 OG1 THR A 224 3974 4810 4217 226 94 2234 A O ATOM 1736 N THR A 225 -11.947 -39.198 20.955 1.00 29.00 A N ANISOU 1736 N THR A 225 3313 3787 3919 296 131 2218 A N ATOM 1737 CA THR A 225 -10.734 -39.620 20.270 1.00 33.21 A C ANISOU 1737 CA THR A 225 3826 4226 4566 360 121 2219 A C ATOM 1738 C THR A 225 -9.607 -38.689 20.691 1.00 32.71 A C ANISOU 1738 C THR A 225 3722 4318 4388 387 50 2206 A C ATOM 1739 O THR A 225 -9.838 -37.641 21.298 1.00 34.06 A O ANISOU 1739 O THR A 225 3898 4645 4397 351 12 2161 A O ATOM 1740 CB THR A 225 -10.911 -39.599 18.744 1.00 33.71 A C ANISOU 1740 CB THR A 225 3934 4128 4745 357 154 2088 A C ATOM 1741 CG2 THR A 225 -11.110 -38.180 18.261 1.00 31.19 A C ANISOU 1741 CG2 THR A 225 3634 3899 4319 326 125 1948 A C ATOM 1742 OG1 THR A 225 -9.740 -40.132 18.113 1.00 34.71 A O ANISOU 1742 OG1 THR A 225 4042 4155 4990 427 160 2096 A O ATOM 1743 N THR A 226 -8.377 -39.082 20.376 1.00 33.27 A N ANISOU 1743 N THR A 226 3753 4343 4547 450 37 2242 A N ATOM 1744 CA THR A 226 -7.242 -38.205 20.611 1.00 31.98 A C ANISOU 1744 CA THR A 226 3544 4313 4295 469 -32 2221 A C ATOM 1745 C THR A 226 -7.016 -37.344 19.380 1.00 30.86 A C ANISOU 1745 C THR A 226 3426 4129 4172 468 -33 2065 A C ATOM 1746 O THR A 226 -7.478 -37.661 18.280 1.00 27.34 A O ANISOU 1746 O THR A 226 3022 3531 3835 472 21 1993 A O ATOM 1747 CB THR A 226 -5.963 -38.988 20.929 1.00 35.54 A C ANISOU 1747 CB THR A 226 3923 4755 4826 536 -48 2349 A C ATOM 1748 CG2 THR A 226 -6.213 -39.995 22.039 1.00 31.93 A C ANISOU 1748 CG2 THR A 226 3442 4314 4374 543 -38 2519 A C ATOM 1749 OG1 THR A 226 -5.534 -39.692 19.761 1.00 35.33 A O ANISOU 1749 OG1 THR A 226 3898 4547 4979 592 8 2323 A O ATOM 1750 N LEU A 227 -6.306 -36.236 19.578 1.00 29.65 A N ANISOU 1750 N LEU A 227 3247 4110 3910 458 -98 2012 A N ATOM 1751 CA LEU A 227 -5.965 -35.370 18.458 1.00 28.20 A C ANISOU 1751 CA LEU A 227 3076 3898 3742 459 -105 1876 A C ATOM 1752 C LEU A 227 -5.161 -36.117 17.404 1.00 30.57 A C ANISOU 1752 C LEU A 227 3355 4051 4211 526 -61 1881 A C ATOM 1753 O LEU A 227 -5.433 -36.016 16.205 1.00 29.03 A O ANISOU 1753 O LEU A 227 3201 3743 4088 532 -19 1779 A O ATOM 1754 CB LEU A 227 -5.215 -34.132 18.960 1.00 30.71 A C ANISOU 1754 CB LEU A 227 3364 4382 3922 433 -186 1833 A C ATOM 1755 CG LEU A 227 -5.096 -32.978 17.964 1.00 26.37 A C ANISOU 1755 CG LEU A 227 2837 3831 3353 415 -199 1683 A C ATOM 1756 CD1 LEU A 227 -6.440 -32.630 17.307 1.00 26.81 A C ANISOU 1756 CD1 LEU A 227 2964 3824 3399 380 -154 1584 A C ATOM 1757 CD2 LEU A 227 -4.519 -31.744 18.650 1.00 27.38 A C ANISOU 1757 CD2 LEU A 227 2946 4123 3334 371 -281 1639 A C ATOM 1758 N ASN A 228 -4.164 -36.884 17.835 1.00 30.48 A N ANISOU 1758 N ASN A 228 3279 4038 4264 580 -66 2001 A N ATOM 1759 CA ASN A 228 -3.347 -37.632 16.870 1.00 32.67 A C ANISOU 1759 CA ASN A 228 3533 4175 4706 653 -12 2007 A C ATOM 1760 C ASN A 228 -4.179 -38.667 16.113 1.00 33.23 A C ANISOU 1760 C ASN A 228 3669 4047 4909 667 75 1984 A C ATOM 1761 O ASN A 228 -4.095 -38.769 14.879 1.00 33.75 A O ANISOU 1761 O ASN A 228 3771 3985 5067 692 127 1887 A O ATOM 1762 CB ASN A 228 -2.184 -38.333 17.576 1.00 34.78 A C ANISOU 1762 CB ASN A 228 3712 4480 5024 711 -29 2159 A C ATOM 1763 CG ASN A 228 -1.233 -37.363 18.195 1.00 40.28 A C ANISOU 1763 CG ASN A 228 4340 5357 5606 692 -117 2176 A C ATOM 1764 ND2 ASN A 228 -0.623 -36.528 17.359 1.00 40.28 A N ANISOU 1764 ND2 ASN A 228 4329 5369 5607 693 -128 2074 A N ATOM 1765 OD1 ASN A 228 -1.087 -37.317 19.424 1.00 45.41 A O ANISOU 1765 OD1 ASN A 228 4953 6140 6160 668 -177 2276 A O ATOM 1766 N ASP A 229 -5.006 -39.423 16.831 1.00 33.79 A N ANISOU 1766 N ASP A 229 3762 4090 4986 645 92 2068 A N ATOM 1767 CA ASP A 229 -5.812 -40.434 16.168 1.00 32.32 A C ANISOU 1767 CA ASP A 229 3641 3711 4929 645 169 2047 A C ATOM 1768 C ASP A 229 -6.799 -39.787 15.207 1.00 30.49 A C ANISOU 1768 C ASP A 229 3485 3427 4672 587 185 1891 A C ATOM 1769 O ASP A 229 -7.034 -40.313 14.115 1.00 29.54 A O ANISOU 1769 O ASP A 229 3421 3138 4665 594 244 1812 A O ATOM 1770 CB ASP A 229 -6.524 -41.304 17.204 1.00 33.84 A C ANISOU 1770 CB ASP A 229 3835 3898 5127 623 178 2176 A C ATOM 1771 CG ASP A 229 -5.547 -42.120 18.054 1.00 38.74 A C ANISOU 1771 CG ASP A 229 4380 4544 5797 687 170 2344 A C ATOM 1772 OD1 ASP A 229 -4.327 -42.030 17.811 1.00 43.00 A O ANISOU 1772 OD1 ASP A 229 4863 5101 6374 748 160 2358 A O ATOM 1773 OD2 ASP A 229 -5.996 -42.875 18.941 1.00 43.07 A O ANISOU 1773 OD2 ASP A 229 4920 5091 6353 678 178 2469 A O ATOM 1774 N PHE A 230 -7.356 -38.623 15.563 1.00 28.76 A N ANISOU 1774 N PHE A 230 3272 3350 4305 528 134 1840 A N ATOM 1775 CA PHE A 230 -8.224 -37.948 14.607 1.00 29.93 A C ANISOU 1775 CA PHE A 230 3483 3455 4435 478 148 1701 A C ATOM 1776 C PHE A 230 -7.437 -37.521 13.377 1.00 27.64 A C ANISOU 1776 C PHE A 230 3199 3108 4195 516 160 1594 A C ATOM 1777 O PHE A 230 -7.903 -37.687 12.245 1.00 24.44 A O ANISOU 1777 O PHE A 230 2854 2571 3862 503 205 1496 A O ATOM 1778 CB PHE A 230 -8.911 -36.730 15.223 1.00 27.21 A C ANISOU 1778 CB PHE A 230 3140 3275 3925 417 98 1667 A C ATOM 1779 CG PHE A 230 -9.670 -35.916 14.211 1.00 26.41 A C ANISOU 1779 CG PHE A 230 3088 3142 3805 372 107 1532 A C ATOM 1780 CD1 PHE A 230 -10.927 -36.326 13.772 1.00 24.08 A C ANISOU 1780 CD1 PHE A 230 2845 2746 3559 318 149 1501 A C ATOM 1781 CD2 PHE A 230 -9.097 -34.786 13.634 1.00 23.56 A C ANISOU 1781 CD2 PHE A 230 2718 2844 3389 382 73 1441 A C ATOM 1782 CE1 PHE A 230 -11.610 -35.600 12.810 1.00 24.02 A C ANISOU 1782 CE1 PHE A 230 2876 2709 3540 274 155 1386 A C ATOM 1783 CE2 PHE A 230 -9.779 -34.059 12.676 1.00 25.94 A C ANISOU 1783 CE2 PHE A 230 3062 3113 3679 346 82 1328 A C ATOM 1784 CZ PHE A 230 -11.038 -34.463 12.264 1.00 20.54 A C ANISOU 1784 CZ PHE A 230 2428 2335 3041 292 122 1303 A C ATOM 1785 N ASN A 231 -6.233 -36.985 13.579 1.00 27.28 A N ANISOU 1785 N ASN A 231 3090 3164 4111 560 120 1613 A N ATOM 1786 CA ASN A 231 -5.459 -36.466 12.460 1.00 27.36 A C ANISOU 1786 CA ASN A 231 3097 3142 4156 594 132 1517 A C ATOM 1787 C ASN A 231 -5.006 -37.564 11.509 1.00 27.31 A C ANISOU 1787 C ASN A 231 3113 2954 4310 655 213 1501 A C ATOM 1788 O ASN A 231 -4.760 -37.281 10.332 1.00 26.95 A O ANISOU 1788 O ASN A 231 3096 2842 4303 671 248 1392 A O ATOM 1789 CB ASN A 231 -4.272 -35.654 12.981 1.00 26.62 A C ANISOU 1789 CB ASN A 231 2923 3204 3987 614 68 1550 A C ATOM 1790 CG ASN A 231 -4.645 -34.208 13.227 1.00 24.85 A C ANISOU 1790 CG ASN A 231 2705 3123 3613 551 2 1477 A C ATOM 1791 ND2 ASN A 231 -4.142 -33.614 14.302 1.00 25.91 A N ANISOU 1791 ND2 ASN A 231 2790 3416 3640 530 -70 1528 A N ATOM 1792 OD1 ASN A 231 -5.397 -33.642 12.460 1.00 29.04 A O ANISOU 1792 OD1 ASN A 231 3289 3618 4127 519 15 1374 A O ATOM 1793 N LEU A 232 -4.924 -38.810 11.982 1.00 29.60 A N ANISOU 1793 N LEU A 232 3395 3161 4691 687 249 1602 A N ATOM 1794 CA LEU A 232 -4.666 -39.924 11.076 1.00 28.82 A C ANISOU 1794 CA LEU A 232 3335 2869 4745 738 336 1572 A C ATOM 1795 C LEU A 232 -5.862 -40.169 10.166 1.00 30.96 A C ANISOU 1795 C LEU A 232 3713 2999 5052 679 378 1452 A C ATOM 1796 O LEU A 232 -5.693 -40.502 8.988 1.00 29.60 A O ANISOU 1796 O LEU A 232 3596 2694 4958 700 439 1345 A O ATOM 1797 CB LEU A 232 -4.331 -41.185 11.870 1.00 30.77 A C ANISOU 1797 CB LEU A 232 3548 3059 5084 784 361 1717 A C ATOM 1798 CG LEU A 232 -2.941 -41.256 12.515 1.00 36.71 A C ANISOU 1798 CG LEU A 232 4193 3905 5848 858 340 1839 A C ATOM 1799 CD1 LEU A 232 -2.817 -42.500 13.380 1.00 36.11 A C ANISOU 1799 CD1 LEU A 232 4087 3775 5859 895 361 1996 A C ATOM 1800 CD2 LEU A 232 -1.831 -41.200 11.478 1.00 33.96 A C ANISOU 1800 CD2 LEU A 232 3824 3505 5574 928 389 1775 A C ATOM 1801 N VAL A 233 -7.082 -40.009 10.694 1.00 27.83 A N ANISOU 1801 N VAL A 233 3346 2634 4594 599 347 1464 A N ATOM 1802 CA VAL A 233 -8.269 -40.146 9.855 1.00 27.87 A C ANISOU 1802 CA VAL A 233 3444 2522 4626 526 375 1354 A C ATOM 1803 C VAL A 233 -8.372 -38.975 8.889 1.00 29.23 A C ANISOU 1803 C VAL A 233 3640 2734 4731 501 360 1217 A C ATOM 1804 O VAL A 233 -8.684 -39.151 7.703 1.00 28.55 A O ANISOU 1804 O VAL A 233 3628 2524 4696 477 401 1092 A O ATOM 1805 CB VAL A 233 -9.527 -40.275 10.732 1.00 30.20 A C ANISOU 1805 CB VAL A 233 3747 2853 4874 445 349 1419 A C ATOM 1806 CG1 VAL A 233 -10.797 -40.239 9.876 1.00 29.65 A C ANISOU 1806 CG1 VAL A 233 3757 2689 4820 351 365 1305 A C ATOM 1807 CG2 VAL A 233 -9.463 -41.542 11.558 1.00 30.43 A C ANISOU 1807 CG2 VAL A 233 3759 2817 4984 469 375 1551 A C ATOM 1808 N ALA A 234 -8.118 -37.760 9.385 1.00 27.60 A N ANISOU 1808 N ALA A 234 3377 2703 4406 501 298 1236 A N ATOM 1809 CA ALA A 234 -8.133 -36.575 8.540 1.00 25.11 A C ANISOU 1809 CA ALA A 234 3076 2436 4028 484 280 1122 A C ATOM 1810 C ALA A 234 -7.258 -36.771 7.307 1.00 27.09 A C ANISOU 1810 C ALA A 234 3349 2588 4354 541 335 1030 A C ATOM 1811 O ALA A 234 -7.702 -36.557 6.172 1.00 25.75 A O ANISOU 1811 O ALA A 234 3248 2340 4198 509 365 904 A O ATOM 1812 CB ALA A 234 -7.670 -35.363 9.350 1.00 24.88 A C ANISOU 1812 CB ALA A 234 2975 2607 3872 490 206 1166 A C ATOM 1813 N MET A 235 -6.006 -37.184 7.520 1.00 27.99 A N ANISOU 1813 N MET A 235 3406 2713 4516 622 353 1092 A N ATOM 1814 CA MET A 235 -5.104 -37.468 6.411 1.00 28.77 A C ANISOU 1814 CA MET A 235 3519 2725 4688 684 421 1016 A C ATOM 1815 C MET A 235 -5.726 -38.440 5.416 1.00 28.45 A C ANISOU 1815 C MET A 235 3584 2492 4734 662 496 913 A C ATOM 1816 O MET A 235 -5.658 -38.229 4.199 1.00 27.96 A O ANISOU 1816 O MET A 235 3578 2370 4675 661 539 780 A O ATOM 1817 CB MET A 235 -3.801 -38.046 6.952 1.00 28.47 A C ANISOU 1817 CB MET A 235 3398 2709 4708 769 437 1126 A C ATOM 1818 CG MET A 235 -2.671 -38.146 5.953 1.00 36.40 A C ANISOU 1818 CG MET A 235 4389 3667 5772 842 504 1069 A C ATOM 1819 SD MET A 235 -1.125 -37.655 6.733 1.00 50.22 A S ANISOU 1819 SD MET A 235 5997 5581 7504 904 460 1196 A S ATOM 1820 CE MET A 235 -1.047 -38.864 8.059 1.00 37.65 A C ANISOU 1820 CE MET A 235 4362 3966 5978 931 451 1368 A C ATOM 1821 N LYS A 236 -6.345 -39.510 5.921 1.00 28.26 A N ANISOU 1821 N LYS A 236 3592 2372 4773 638 509 969 A N ATOM 1822 CA LYS A 236 -6.850 -40.557 5.043 1.00 27.77 A C ANISOU 1822 CA LYS A 236 3632 2119 4800 612 575 873 A C ATOM 1823 C LYS A 236 -7.976 -40.055 4.146 1.00 27.86 A C ANISOU 1823 C LYS A 236 3730 2096 4760 511 562 729 A C ATOM 1824 O LYS A 236 -8.116 -40.526 3.011 1.00 30.62 A O ANISOU 1824 O LYS A 236 4167 2322 5145 490 613 595 A O ATOM 1825 CB LYS A 236 -7.305 -41.755 5.877 1.00 28.61 A C ANISOU 1825 CB LYS A 236 3746 2139 4986 598 584 978 A C ATOM 1826 CG LYS A 236 -7.990 -42.832 5.068 1.00 32.50 A C ANISOU 1826 CG LYS A 236 4350 2433 5565 548 637 879 A C ATOM 1827 CD LYS A 236 -8.492 -43.969 5.933 1.00 34.81 A C ANISOU 1827 CD LYS A 236 4647 2640 5939 528 641 992 A C ATOM 1828 CE LYS A 236 -9.453 -44.850 5.149 1.00 32.28 A C ANISOU 1828 CE LYS A 236 4445 2138 5683 440 670 881 A C ATOM 1829 NZ LYS A 236 -9.362 -46.275 5.565 1.00 36.09 A N ANISOU 1829 NZ LYS A 236 4948 2471 6295 466 716 962 A N ATOM 1830 N TYR A 237 -8.774 -39.097 4.620 1.00 25.95 A N ANISOU 1830 N TYR A 237 3464 1968 4427 445 495 751 A N ATOM 1831 CA TYR A 237 -9.896 -38.554 3.861 1.00 23.34 A C ANISOU 1831 CA TYR A 237 3200 1621 4049 342 475 632 A C ATOM 1832 C TYR A 237 -9.589 -37.191 3.271 1.00 23.16 A C ANISOU 1832 C TYR A 237 3158 1701 3939 353 455 560 A C ATOM 1833 O TYR A 237 -10.514 -36.439 2.947 1.00 21.68 A O ANISOU 1833 O TYR A 237 2995 1547 3694 270 421 500 A O ATOM 1834 CB TYR A 237 -11.140 -38.479 4.741 1.00 23.92 A C ANISOU 1834 CB TYR A 237 3258 1738 4093 253 424 708 A C ATOM 1835 CG TYR A 237 -11.683 -39.845 5.056 1.00 26.64 A C ANISOU 1835 CG TYR A 237 3640 1956 4527 216 448 750 A C ATOM 1836 CD1 TYR A 237 -12.608 -40.458 4.216 1.00 27.22 A C ANISOU 1836 CD1 TYR A 237 3802 1901 4641 117 459 641 A C ATOM 1837 CD2 TYR A 237 -11.236 -40.544 6.166 1.00 28.10 A C ANISOU 1837 CD2 TYR A 237 3773 2151 4753 275 455 896 A C ATOM 1838 CE1 TYR A 237 -13.089 -41.719 4.494 1.00 26.09 A C ANISOU 1838 CE1 TYR A 237 3695 1634 4584 79 478 680 A C ATOM 1839 CE2 TYR A 237 -11.711 -41.805 6.450 1.00 28.74 A C ANISOU 1839 CE2 TYR A 237 3889 2107 4924 243 481 941 A C ATOM 1840 CZ TYR A 237 -12.636 -42.384 5.611 1.00 28.28 A C ANISOU 1840 CZ TYR A 237 3921 1914 4911 146 494 833 A C ATOM 1841 OH TYR A 237 -13.103 -43.638 5.905 1.00 31.16 A O ANISOU 1841 OH TYR A 237 4322 2150 5369 109 516 880 A O ATOM 1842 N ASN A 238 -8.308 -36.855 3.143 1.00 22.28 A N ANISOU 1842 N ASN A 238 2998 1646 3823 450 475 573 A N ATOM 1843 CA ASN A 238 -7.892 -35.623 2.480 1.00 23.01 A C ANISOU 1843 CA ASN A 238 3073 1827 3842 466 465 502 A C ATOM 1844 C ASN A 238 -8.438 -34.401 3.226 1.00 20.28 A C ANISOU 1844 C ASN A 238 2673 1634 3399 423 382 556 A C ATOM 1845 O ASN A 238 -8.883 -33.419 2.631 1.00 19.43 A O ANISOU 1845 O ASN A 238 2577 1615 3189 360 344 453 A O ATOM 1846 CB ASN A 238 -8.330 -35.635 1.015 1.00 20.57 A C ANISOU 1846 CB ASN A 238 2865 1427 3521 413 509 327 A C ATOM 1847 CG ASN A 238 -7.726 -34.516 0.230 1.00 24.98 A C ANISOU 1847 CG ASN A 238 3407 2079 4004 439 513 251 A C ATOM 1848 ND2 ASN A 238 -6.591 -34.038 0.701 1.00 25.52 A N ANISOU 1848 ND2 ASN A 238 3383 2239 4076 530 510 339 A N ATOM 1849 OD1 ASN A 238 -8.252 -34.089 -0.797 1.00 29.60 A O ANISOU 1849 OD1 ASN A 238 4054 2682 4512 368 506 118 A O ATOM 1850 N TYR A 239 -8.423 -34.472 4.547 1.00 20.75 A N ANISOU 1850 N TYR A 239 2668 1766 3449 438 339 698 A N ATOM 1851 CA TYR A 239 -8.781 -33.348 5.393 1.00 19.98 A C ANISOU 1851 CA TYR A 239 2516 1845 3231 400 258 741 A C ATOM 1852 C TYR A 239 -7.512 -32.713 5.934 1.00 21.10 A C ANISOU 1852 C TYR A 239 2571 2106 3339 477 225 815 A C ATOM 1853 O TYR A 239 -6.501 -33.383 6.135 1.00 20.70 A O ANISOU 1853 O TYR A 239 2483 2038 3344 539 249 866 A O ATOM 1854 CB TYR A 239 -9.665 -33.777 6.567 1.00 18.32 A C ANISOU 1854 CB TYR A 239 2295 1651 3013 359 234 853 A C ATOM 1855 CG TYR A 239 -11.156 -33.742 6.312 1.00 16.97 A C ANISOU 1855 CG TYR A 239 2174 1462 2814 250 226 783 A C ATOM 1856 CD1 TYR A 239 -11.715 -34.370 5.203 1.00 18.90 A C ANISOU 1856 CD1 TYR A 239 2493 1564 3126 198 266 677 A C ATOM 1857 CD2 TYR A 239 -12.002 -33.094 7.198 1.00 16.79 A C ANISOU 1857 CD2 TYR A 239 2118 1566 2694 197 181 825 A C ATOM 1858 CE1 TYR A 239 -13.089 -34.342 4.984 1.00 18.34 A C ANISOU 1858 CE1 TYR A 239 2449 1486 3033 90 247 625 A C ATOM 1859 CE2 TYR A 239 -13.371 -33.064 7.000 1.00 15.39 A C ANISOU 1859 CE2 TYR A 239 1965 1380 2503 103 177 777 A C ATOM 1860 CZ TYR A 239 -13.909 -33.687 5.892 1.00 17.57 A C ANISOU 1860 CZ TYR A 239 2301 1521 2852 47 204 684 A C ATOM 1861 OH TYR A 239 -15.259 -33.651 5.689 1.00 16.63 A O ANISOU 1861 OH TYR A 239 2191 1404 2723 -54 189 647 A O ATOM 1862 N GLU A 240 -7.590 -31.416 6.188 1.00 20.53 A N ANISOU 1862 N GLU A 240 2465 2188 3146 438 160 779 A N ATOM 1863 CA GLU A 240 -6.449 -30.689 6.701 1.00 20.71 A C ANISOU 1863 CA GLU A 240 2407 2336 3128 485 113 836 A C ATOM 1864 C GLU A 240 -6.164 -31.145 8.130 1.00 21.05 A C ANISOU 1864 C GLU A 240 2401 2451 3144 492 76 961 A C ATOM 1865 O GLU A 240 -7.085 -31.519 8.860 1.00 21.96 A O ANISOU 1865 O GLU A 240 2542 2569 3234 453 69 1008 A O ATOM 1866 CB GLU A 240 -6.753 -29.201 6.669 1.00 19.85 A C ANISOU 1866 CB GLU A 240 2292 2358 2894 421 54 748 A C ATOM 1867 CG GLU A 240 -6.455 -28.603 5.335 1.00 22.91 A C ANISOU 1867 CG GLU A 240 2697 2721 3286 416 80 627 A C ATOM 1868 CD GLU A 240 -6.507 -27.104 5.358 1.00 29.10 A C ANISOU 1868 CD GLU A 240 3462 3627 3968 366 22 564 A C ATOM 1869 OE1 GLU A 240 -5.606 -26.484 4.754 1.00 34.30 A O ANISOU 1869 OE1 GLU A 240 4087 4315 4631 386 23 532 A O ATOM 1870 OE2 GLU A 240 -7.433 -26.547 6.000 1.00 26.39 A O ANISOU 1870 OE2 GLU A 240 3135 3345 3547 311 -17 551 A O ATOM 1871 N PRO A 241 -4.897 -31.171 8.543 1.00 23.10 A N ANISOU 1871 N PRO A 241 2592 2776 3410 532 56 1013 A N ATOM 1872 CA PRO A 241 -4.601 -31.502 9.941 1.00 23.07 A C ANISOU 1872 CA PRO A 241 2542 2859 3363 527 13 1123 A C ATOM 1873 C PRO A 241 -5.270 -30.514 10.883 1.00 23.42 A C ANISOU 1873 C PRO A 241 2592 3043 3264 459 -57 1116 A C ATOM 1874 O PRO A 241 -5.421 -29.330 10.574 1.00 25.76 A O ANISOU 1874 O PRO A 241 2894 3405 3487 426 -91 1035 A O ATOM 1875 CB PRO A 241 -3.071 -31.413 10.015 1.00 24.69 A C ANISOU 1875 CB PRO A 241 2669 3120 3594 571 -3 1162 A C ATOM 1876 CG PRO A 241 -2.615 -31.543 8.596 1.00 25.38 A C ANISOU 1876 CG PRO A 241 2767 3102 3774 617 65 1089 A C ATOM 1877 CD PRO A 241 -3.672 -30.902 7.768 1.00 22.37 A C ANISOU 1877 CD PRO A 241 2455 2683 3361 579 76 980 A C ATOM 1878 N LEU A 242 -5.714 -31.018 12.028 1.00 25.37 A N ANISOU 1878 N LEU A 242 2839 3331 3470 441 -70 1198 A N ATOM 1879 CA LEU A 242 -6.286 -30.167 13.062 1.00 25.07 A C ANISOU 1879 CA LEU A 242 2809 3430 3286 382 -124 1191 A C ATOM 1880 C LEU A 242 -5.192 -29.828 14.063 1.00 22.62 A C ANISOU 1880 C LEU A 242 2440 3247 2908 380 -188 1241 A C ATOM 1881 O LEU A 242 -4.515 -30.721 14.565 1.00 21.36 A O ANISOU 1881 O LEU A 242 2238 3079 2798 416 -185 1344 A O ATOM 1882 CB LEU A 242 -7.454 -30.857 13.765 1.00 23.32 A C ANISOU 1882 CB LEU A 242 2623 3192 3048 356 -95 1249 A C ATOM 1883 CG LEU A 242 -8.386 -29.914 14.522 1.00 20.84 A C ANISOU 1883 CG LEU A 242 2335 2994 2588 296 -121 1209 A C ATOM 1884 CD1 LEU A 242 -9.210 -29.105 13.527 1.00 21.93 A C ANISOU 1884 CD1 LEU A 242 2514 3100 2719 269 -104 1102 A C ATOM 1885 CD2 LEU A 242 -9.276 -30.699 15.500 1.00 22.45 A C ANISOU 1885 CD2 LEU A 242 2552 3208 2769 277 -93 1296 A C ATOM 1886 N THR A 243 -4.998 -28.544 14.321 1.00 23.83 A N ANISOU 1886 N THR A 243 2591 3509 2953 335 -245 1168 A N ATOM 1887 CA THR A 243 -3.974 -28.104 15.252 1.00 24.76 A C ANISOU 1887 CA THR A 243 2661 3746 3000 317 -314 1201 A C ATOM 1888 C THR A 243 -4.591 -27.779 16.602 1.00 23.27 A C ANISOU 1888 C THR A 243 2503 3669 2671 267 -348 1214 A C ATOM 1889 O THR A 243 -5.808 -27.620 16.742 1.00 22.99 A O ANISOU 1889 O THR A 243 2524 3631 2582 243 -318 1177 A O ATOM 1890 CB THR A 243 -3.249 -26.870 14.721 1.00 22.57 A C ANISOU 1890 CB THR A 243 2367 3512 2699 290 -357 1106 A C ATOM 1891 CG2 THR A 243 -2.716 -27.129 13.319 1.00 23.65 A C ANISOU 1891 CG2 THR A 243 2478 3543 2965 340 -312 1086 A C ATOM 1892 OG1 THR A 243 -4.175 -25.781 14.695 1.00 22.28 A O ANISOU 1892 OG1 THR A 243 2389 3509 2568 237 -367 997 A O ATOM 1893 N GLN A 244 -3.722 -27.651 17.605 1.00 22.10 A N ANISOU 1893 N GLN A 244 2314 3625 2457 251 -410 1268 A N ATOM 1894 CA GLN A 244 -4.198 -27.224 18.914 1.00 22.61 A C ANISOU 1894 CA GLN A 244 2414 3807 2371 201 -446 1267 A C ATOM 1895 C GLN A 244 -4.771 -25.820 18.862 1.00 21.87 A C ANISOU 1895 C GLN A 244 2380 3756 2173 145 -461 1121 A C ATOM 1896 O GLN A 244 -5.691 -25.499 19.625 1.00 23.12 A O ANISOU 1896 O GLN A 244 2593 3969 2221 114 -449 1091 A O ATOM 1897 CB GLN A 244 -3.087 -27.303 19.959 1.00 25.74 A C ANISOU 1897 CB GLN A 244 2756 4311 2712 189 -519 1349 A C ATOM 1898 CG GLN A 244 -3.584 -26.945 21.355 1.00 25.53 A C ANISOU 1898 CG GLN A 244 2774 4408 2519 139 -553 1351 A C ATOM 1899 CD GLN A 244 -4.701 -27.859 21.823 1.00 26.94 A C ANISOU 1899 CD GLN A 244 2984 4564 2689 158 -490 1425 A C ATOM 1900 NE2 GLN A 244 -5.727 -27.279 22.435 1.00 30.15 A N ANISOU 1900 NE2 GLN A 244 3459 5026 2969 119 -472 1359 A N ATOM 1901 OE1 GLN A 244 -4.648 -29.072 21.624 1.00 28.52 A O ANISOU 1901 OE1 GLN A 244 3146 4691 3000 209 -453 1538 A O ATOM 1902 N ASP A 245 -4.264 -24.971 17.958 1.00 22.71 A N ANISOU 1902 N ASP A 245 2477 3834 2317 135 -480 1030 A N ATOM 1903 CA ASP A 245 -4.861 -23.647 17.829 1.00 23.56 A C ANISOU 1903 CA ASP A 245 2645 3965 2344 86 -487 891 A C ATOM 1904 C ASP A 245 -6.286 -23.729 17.295 1.00 22.42 A C ANISOU 1904 C ASP A 245 2552 3757 2210 97 -413 850 A C ATOM 1905 O ASP A 245 -7.159 -22.981 17.751 1.00 22.44 A O ANISOU 1905 O ASP A 245 2611 3801 2113 63 -399 774 A O ATOM 1906 CB ASP A 245 -4.021 -22.734 16.941 1.00 22.52 A C ANISOU 1906 CB ASP A 245 2488 3809 2260 70 -520 811 A C ATOM 1907 CG ASP A 245 -4.408 -21.284 17.110 1.00 23.28 A C ANISOU 1907 CG ASP A 245 2642 3940 2262 10 -542 675 A C ATOM 1908 OD1 ASP A 245 -4.383 -20.814 18.269 1.00 26.73 A O ANISOU 1908 OD1 ASP A 245 3111 4463 2580 -33 -582 653 A O ATOM 1909 OD2 ASP A 245 -4.770 -20.620 16.116 1.00 27.25 A O ANISOU 1909 OD2 ASP A 245 3164 4383 2806 7 -518 589 A O ATOM 1910 N HIS A 246 -6.537 -24.623 16.328 1.00 22.81 A N ANISOU 1910 N HIS A 246 2583 3703 2380 144 -362 897 A N ATOM 1911 CA HIS A 246 -7.909 -24.893 15.895 1.00 21.54 A C ANISOU 1911 CA HIS A 246 2463 3485 2236 150 -296 883 A C ATOM 1912 C HIS A 246 -8.778 -25.339 17.061 1.00 21.02 A C ANISOU 1912 C HIS A 246 2423 3473 2089 136 -270 939 A C ATOM 1913 O HIS A 246 -9.930 -24.910 17.192 1.00 22.38 A O ANISOU 1913 O HIS A 246 2638 3662 2205 115 -229 889 A O ATOM 1914 CB HIS A 246 -7.935 -25.969 14.808 1.00 22.10 A C ANISOU 1914 CB HIS A 246 2515 3429 2454 198 -251 938 A C ATOM 1915 CG HIS A 246 -7.293 -25.557 13.521 1.00 19.67 A C ANISOU 1915 CG HIS A 246 2189 3061 2225 217 -258 878 A C ATOM 1916 CD2 HIS A 246 -7.230 -24.358 12.897 1.00 23.90 A C ANISOU 1916 CD2 HIS A 246 2735 3615 2733 192 -279 772 A C ATOM 1917 ND1 HIS A 246 -6.591 -26.441 12.728 1.00 23.34 A N ANISOU 1917 ND1 HIS A 246 2621 3431 2817 269 -233 927 A N ATOM 1918 CE1 HIS A 246 -6.138 -25.806 11.660 1.00 24.62 A C ANISOU 1918 CE1 HIS A 246 2772 3563 3018 276 -237 855 A C ATOM 1919 NE2 HIS A 246 -6.515 -24.541 11.736 1.00 23.27 A N ANISOU 1919 NE2 HIS A 246 2623 3460 2757 227 -269 765 A N ATOM 1920 N VAL A 247 -8.265 -26.252 17.884 1.00 24.67 A N ANISOU 1920 N VAL A 247 2856 3962 2556 152 -284 1050 A N ATOM 1921 CA VAL A 247 -9.021 -26.698 19.054 1.00 22.17 A C ANISOU 1921 CA VAL A 247 2560 3706 2158 139 -260 1114 A C ATOM 1922 C VAL A 247 -9.345 -25.512 19.951 1.00 25.19 A C ANISOU 1922 C VAL A 247 2989 4202 2378 93 -280 1025 A C ATOM 1923 O VAL A 247 -10.481 -25.362 20.430 1.00 23.26 A O ANISOU 1923 O VAL A 247 2786 3988 2065 78 -228 1007 A O ATOM 1924 CB VAL A 247 -8.246 -27.794 19.808 1.00 25.70 A C ANISOU 1924 CB VAL A 247 2961 4171 2631 164 -284 1254 A C ATOM 1925 CG1 VAL A 247 -8.956 -28.159 21.098 1.00 26.78 A C ANISOU 1925 CG1 VAL A 247 3119 4388 2668 146 -265 1322 A C ATOM 1926 CG2 VAL A 247 -8.089 -29.018 18.924 1.00 26.16 A C ANISOU 1926 CG2 VAL A 247 2986 4094 2859 214 -245 1333 A C ATOM 1927 N ASP A 248 -8.359 -24.641 20.177 1.00 22.17 A N ANISOU 1927 N ASP A 248 2604 3880 1939 69 -349 965 A N ATOM 1928 CA ASP A 248 -8.587 -23.475 21.022 1.00 27.31 A C ANISOU 1928 CA ASP A 248 3312 4624 2440 23 -368 865 A C ATOM 1929 C ASP A 248 -9.627 -22.548 20.405 1.00 23.64 A C ANISOU 1929 C ASP A 248 2898 4123 1963 12 -314 741 A C ATOM 1930 O ASP A 248 -10.524 -22.061 21.103 1.00 25.17 A O ANISOU 1930 O ASP A 248 3145 4365 2053 -5 -271 691 A O ATOM 1931 CB ASP A 248 -7.268 -22.733 21.260 1.00 26.16 A C ANISOU 1931 CB ASP A 248 3152 4531 2258 -9 -459 823 A C ATOM 1932 CG ASP A 248 -6.270 -23.553 22.061 1.00 26.08 A C ANISOU 1932 CG ASP A 248 3088 4583 2238 -2 -516 950 A C ATOM 1933 OD1 ASP A 248 -6.694 -24.486 22.778 1.00 26.57 A O ANISOU 1933 OD1 ASP A 248 3146 4674 2274 16 -489 1055 A O ATOM 1934 OD2 ASP A 248 -5.051 -23.265 21.978 1.00 27.01 A O ANISOU 1934 OD2 ASP A 248 3161 4724 2377 -16 -587 951 A O ATOM 1935 N ILE A 249 -9.534 -22.308 19.091 1.00 19.81 A N ANISOU 1935 N ILE A 249 2393 3552 1583 26 -309 695 A N ATOM 1936 CA ILE A 249 -10.490 -21.439 18.409 1.00 21.94 A C ANISOU 1936 CA ILE A 249 2700 3786 1851 20 -259 587 A C ATOM 1937 C ILE A 249 -11.906 -21.990 18.545 1.00 21.87 A C ANISOU 1937 C ILE A 249 2705 3768 1839 36 -174 627 A C ATOM 1938 O ILE A 249 -12.876 -21.229 18.646 1.00 22.37 A O ANISOU 1938 O ILE A 249 2806 3848 1846 28 -120 547 A O ATOM 1939 CB ILE A 249 -10.068 -21.259 16.933 1.00 20.44 A C ANISOU 1939 CB ILE A 249 2478 3509 1778 35 -274 554 A C ATOM 1940 CG1 ILE A 249 -8.850 -20.336 16.844 1.00 24.08 A C ANISOU 1940 CG1 ILE A 249 2932 3988 2231 6 -347 486 A C ATOM 1941 CG2 ILE A 249 -11.206 -20.734 16.078 1.00 22.47 A C ANISOU 1941 CG2 ILE A 249 2758 3722 2057 40 -216 483 A C ATOM 1942 CD1 ILE A 249 -7.975 -20.580 15.595 1.00 21.81 A C ANISOU 1942 CD1 ILE A 249 2588 3627 2070 28 -371 506 A C ATOM 1943 N LEU A 250 -12.043 -23.310 18.600 1.00 20.95 A N ANISOU 1943 N LEU A 250 2555 3620 1787 58 -154 753 A N ATOM 1944 CA LEU A 250 -13.348 -23.943 18.736 1.00 23.79 A C ANISOU 1944 CA LEU A 250 2917 3962 2160 64 -75 806 A C ATOM 1945 C LEU A 250 -13.852 -23.982 20.177 1.00 21.26 A C ANISOU 1945 C LEU A 250 2623 3736 1718 51 -46 835 A C ATOM 1946 O LEU A 250 -14.955 -24.489 20.414 1.00 24.07 A O ANISOU 1946 O LEU A 250 2976 4087 2084 52 25 885 A O ATOM 1947 CB LEU A 250 -13.293 -25.360 18.161 1.00 20.77 A C ANISOU 1947 CB LEU A 250 2494 3485 1912 86 -64 925 A C ATOM 1948 CG LEU A 250 -13.082 -25.495 16.653 1.00 18.23 A C ANISOU 1948 CG LEU A 250 2156 3053 1718 101 -69 902 A C ATOM 1949 CD1 LEU A 250 -12.847 -26.960 16.340 1.00 17.42 A C ANISOU 1949 CD1 LEU A 250 2027 2851 1741 124 -58 1016 A C ATOM 1950 CD2 LEU A 250 -14.289 -24.974 15.894 1.00 15.89 A C ANISOU 1950 CD2 LEU A 250 1874 2728 1437 86 -16 840 A C ATOM 1951 N GLY A 251 -13.083 -23.465 21.138 1.00 22.65 A N ANISOU 1951 N GLY A 251 2826 3999 1782 33 -98 807 A N ATOM 1952 CA GLY A 251 -13.460 -23.450 22.537 1.00 22.60 A C ANISOU 1952 CA GLY A 251 2856 4091 1642 19 -75 829 A C ATOM 1953 C GLY A 251 -14.836 -22.878 22.840 1.00 24.84 A C ANISOU 1953 C GLY A 251 3180 4397 1862 17 21 765 A C ATOM 1954 O GLY A 251 -15.669 -23.535 23.476 1.00 26.11 A O ANISOU 1954 O GLY A 251 3336 4585 2000 21 83 844 A O ATOM 1955 N PRO A 252 -15.091 -21.630 22.419 1.00 26.43 A N ANISOU 1955 N PRO A 252 3417 4586 2038 12 39 625 A N ATOM 1956 CA PRO A 252 -16.402 -21.019 22.706 1.00 27.14 A C ANISOU 1956 CA PRO A 252 3541 4694 2078 20 143 560 A C ATOM 1957 C PRO A 252 -17.572 -21.840 22.207 1.00 24.48 A C ANISOU 1957 C PRO A 252 3149 4310 1842 39 222 644 A C ATOM 1958 O PRO A 252 -18.586 -21.972 22.907 1.00 26.22 A O ANISOU 1958 O PRO A 252 3376 4571 2018 44 305 670 A O ATOM 1959 CB PRO A 252 -16.317 -19.666 21.982 1.00 27.72 A C ANISOU 1959 CB PRO A 252 3644 4728 2161 20 141 408 A C ATOM 1960 CG PRO A 252 -14.864 -19.347 21.969 1.00 27.18 A C ANISOU 1960 CG PRO A 252 3589 4666 2073 -7 29 376 A C ATOM 1961 CD PRO A 252 -14.176 -20.672 21.767 1.00 26.28 A C ANISOU 1961 CD PRO A 252 3411 4539 2034 -1 -29 519 A C ATOM 1962 N LEU A 253 -17.457 -22.401 21.006 1.00 23.77 A N ANISOU 1962 N LEU A 253 3007 4135 1890 46 197 687 A N ATOM 1963 CA LEU A 253 -18.530 -23.232 20.476 1.00 22.15 A C ANISOU 1963 CA LEU A 253 2750 3874 1793 50 260 768 A C ATOM 1964 C LEU A 253 -18.655 -24.525 21.267 1.00 21.84 A C ANISOU 1964 C LEU A 253 2690 3849 1760 43 270 908 A C ATOM 1965 O LEU A 253 -19.765 -24.956 21.598 1.00 23.42 A O ANISOU 1965 O LEU A 253 2867 4055 1976 38 344 963 A O ATOM 1966 CB LEU A 253 -18.264 -23.521 19.010 1.00 18.71 A C ANISOU 1966 CB LEU A 253 2278 3338 1494 52 225 774 A C ATOM 1967 CG LEU A 253 -18.589 -22.355 18.081 1.00 18.84 A C ANISOU 1967 CG LEU A 253 2298 3334 1528 60 242 656 A C ATOM 1968 CD1 LEU A 253 -18.199 -22.713 16.665 1.00 19.45 A C ANISOU 1968 CD1 LEU A 253 2347 3320 1724 56 200 672 A C ATOM 1969 CD2 LEU A 253 -20.072 -22.019 18.181 1.00 21.27 A C ANISOU 1969 CD2 LEU A 253 2582 3655 1846 67 342 640 A C ATOM 1970 N SER A 254 -17.521 -25.152 21.582 1.00 20.63 A N ANISOU 1970 N SER A 254 2538 3701 1601 43 196 973 A N ATOM 1971 CA SER A 254 -17.525 -26.304 22.472 1.00 23.31 A C ANISOU 1971 CA SER A 254 2861 4063 1932 40 202 1107 A C ATOM 1972 C SER A 254 -18.210 -25.979 23.793 1.00 25.20 A C ANISOU 1972 C SER A 254 3134 4412 2029 32 260 1107 A C ATOM 1973 O SER A 254 -19.007 -26.776 24.309 1.00 27.79 A O ANISOU 1973 O SER A 254 3440 4748 2370 26 317 1204 A O ATOM 1974 CB SER A 254 -16.084 -26.761 22.703 1.00 23.68 A C ANISOU 1974 CB SER A 254 2903 4117 1976 48 111 1161 A C ATOM 1975 OG SER A 254 -16.008 -27.766 23.679 1.00 26.84 A O ANISOU 1975 OG SER A 254 3290 4555 2354 49 113 1292 A O ATOM 1976 N ALA A 255 -17.915 -24.807 24.358 1.00 25.13 A N ANISOU 1976 N ALA A 255 3183 4482 1883 28 249 995 A N ATOM 1977 CA ALA A 255 -18.482 -24.439 25.651 1.00 28.35 A C ANISOU 1977 CA ALA A 255 3638 4993 2139 21 309 982 A C ATOM 1978 C ALA A 255 -19.983 -24.204 25.552 1.00 28.96 A C ANISOU 1978 C ALA A 255 3703 5060 2241 30 427 958 A C ATOM 1979 O ALA A 255 -20.746 -24.628 26.432 1.00 28.47 A O ANISOU 1979 O ALA A 255 3641 5052 2124 26 497 1026 A O ATOM 1980 CB ALA A 255 -17.781 -23.193 26.188 1.00 30.07 A C ANISOU 1980 CB ALA A 255 3933 5277 2214 10 269 850 A C ATOM 1981 N GLN A 256 -20.421 -23.524 24.491 1.00 26.10 A N ANISOU 1981 N GLN A 256 3323 4632 1963 41 452 869 A N ATOM 1982 CA GLN A 256 -21.840 -23.237 24.317 1.00 28.00 A C ANISOU 1982 CA GLN A 256 3534 4860 2244 54 562 847 A C ATOM 1983 C GLN A 256 -22.652 -24.519 24.183 1.00 28.59 A C ANISOU 1983 C GLN A 256 3535 4898 2428 41 598 990 A C ATOM 1984 O GLN A 256 -23.752 -24.629 24.740 1.00 30.76 A O ANISOU 1984 O GLN A 256 3790 5210 2688 42 690 1024 A O ATOM 1985 CB GLN A 256 -22.036 -22.342 23.095 1.00 25.82 A C ANISOU 1985 CB GLN A 256 3241 4516 2053 70 566 740 A C ATOM 1986 CG GLN A 256 -23.488 -22.138 22.701 1.00 26.75 A C ANISOU 1986 CG GLN A 256 3302 4609 2252 86 667 735 A C ATOM 1987 CD GLN A 256 -23.640 -21.228 21.508 1.00 26.85 A C ANISOU 1987 CD GLN A 256 3293 4559 2348 106 666 638 A C ATOM 1988 NE2 GLN A 256 -24.876 -20.862 21.194 1.00 30.49 A N ANISOU 1988 NE2 GLN A 256 3701 5004 2880 126 751 624 A N ATOM 1989 OE1 GLN A 256 -22.656 -20.866 20.862 1.00 31.53 A O ANISOU 1989 OE1 GLN A 256 3913 5120 2949 104 587 582 A O ATOM 1990 N THR A 257 -22.129 -25.498 23.448 1.00 26.94 A N ANISOU 1990 N THR A 257 3289 4611 2336 28 530 1072 A N ATOM 1991 CA THR A 257 -22.832 -26.753 23.232 1.00 24.84 A C ANISOU 1991 CA THR A 257 2962 4286 2192 7 556 1199 A C ATOM 1992 C THR A 257 -22.536 -27.792 24.300 1.00 26.12 A C ANISOU 1992 C THR A 257 3129 4487 2306 -3 548 1327 A C ATOM 1993 O THR A 257 -23.294 -28.757 24.431 1.00 30.39 A O ANISOU 1993 O THR A 257 3626 4998 2923 -23 589 1434 A O ATOM 1994 CB THR A 257 -22.471 -27.323 21.861 1.00 25.37 A C ANISOU 1994 CB THR A 257 2995 4227 2418 -7 498 1215 A C ATOM 1995 CG2 THR A 257 -22.886 -26.346 20.773 1.00 21.61 A C ANISOU 1995 CG2 THR A 257 2504 3716 1991 -1 510 1104 A C ATOM 1996 OG1 THR A 257 -21.050 -27.509 21.777 1.00 22.29 A O ANISOU 1996 OG1 THR A 257 2636 3821 2011 5 410 1218 A O ATOM 1997 N GLY A 258 -21.463 -27.622 25.064 1.00 26.89 A N ANISOU 1997 N GLY A 258 3277 4654 2285 8 492 1324 A N ATOM 1998 CA GLY A 258 -21.073 -28.644 26.012 1.00 27.25 A C ANISOU 1998 CA GLY A 258 3322 4738 2295 2 473 1458 A C ATOM 1999 C GLY A 258 -20.517 -29.902 25.389 1.00 27.45 A C ANISOU 1999 C GLY A 258 3305 4653 2471 -0 419 1566 A C ATOM 2000 O GLY A 258 -20.436 -30.934 26.061 1.00 28.94 A O ANISOU 2000 O GLY A 258 3478 4848 2670 -4 420 1698 A O ATOM 2001 N ILE A 259 -20.130 -29.855 24.123 1.00 23.95 A N ANISOU 2001 N ILE A 259 2847 4104 2147 4 378 1513 A N ATOM 2002 CA ILE A 259 -19.543 -30.997 23.436 1.00 25.08 A C ANISOU 2002 CA ILE A 259 2962 4126 2440 6 334 1596 A C ATOM 2003 C ILE A 259 -18.055 -30.713 23.272 1.00 24.50 A C ANISOU 2003 C ILE A 259 2907 4060 2341 33 247 1563 A C ATOM 2004 O ILE A 259 -17.668 -29.787 22.550 1.00 23.92 A O ANISOU 2004 O ILE A 259 2849 3979 2259 40 217 1447 A O ATOM 2005 CB ILE A 259 -20.225 -31.256 22.088 1.00 24.35 A C ANISOU 2005 CB ILE A 259 2843 3900 2508 -16 357 1565 A C ATOM 2006 CG1 ILE A 259 -21.690 -31.630 22.315 1.00 27.24 A C ANISOU 2006 CG1 ILE A 259 3177 4262 2910 -51 437 1612 A C ATOM 2007 CG2 ILE A 259 -19.500 -32.357 21.318 1.00 25.87 A C ANISOU 2007 CG2 ILE A 259 3026 3952 2851 -11 315 1624 A C ATOM 2008 CD1 ILE A 259 -22.534 -31.358 21.129 1.00 27.26 A C ANISOU 2008 CD1 ILE A 259 3154 4186 3019 -80 459 1543 A C ATOM 2009 N ALA A 260 -17.220 -31.487 23.967 1.00 24.16 A N ANISOU 2009 N ALA A 260 2855 4037 2288 49 207 1669 A N ATOM 2010 CA ALA A 260 -15.780 -31.281 23.896 1.00 25.17 A C ANISOU 2010 CA ALA A 260 2984 4182 2398 75 123 1653 A C ATOM 2011 C ALA A 260 -15.320 -31.310 22.446 1.00 24.21 A C ANISOU 2011 C ALA A 260 2850 3930 2418 89 99 1595 A C ATOM 2012 O ALA A 260 -15.868 -32.046 21.623 1.00 24.62 A O ANISOU 2012 O ALA A 260 2889 3856 2610 84 137 1621 A O ATOM 2013 CB ALA A 260 -15.046 -32.350 24.712 1.00 25.60 A C ANISOU 2013 CB ALA A 260 3012 4253 2462 94 92 1803 A C ATOM 2014 N VAL A 261 -14.323 -30.484 22.121 1.00 23.77 A N ANISOU 2014 N VAL A 261 2802 3905 2324 103 38 1512 A N ATOM 2015 CA VAL A 261 -13.852 -30.446 20.741 1.00 20.29 A C ANISOU 2015 CA VAL A 261 2353 3350 2007 119 19 1455 A C ATOM 2016 C VAL A 261 -13.481 -31.848 20.280 1.00 21.53 A C ANISOU 2016 C VAL A 261 2481 3376 2324 145 27 1560 A C ATOM 2017 O VAL A 261 -13.935 -32.318 19.230 1.00 22.31 A O ANISOU 2017 O VAL A 261 2585 3343 2550 142 62 1544 A O ATOM 2018 CB VAL A 261 -12.675 -29.464 20.591 1.00 23.79 A C ANISOU 2018 CB VAL A 261 2797 3850 2390 129 -52 1372 A C ATOM 2019 CG1 VAL A 261 -12.032 -29.623 19.211 1.00 20.03 A C ANISOU 2019 CG1 VAL A 261 2305 3255 2051 155 -68 1339 A C ATOM 2020 CG2 VAL A 261 -13.138 -28.032 20.808 1.00 22.30 A C ANISOU 2020 CG2 VAL A 261 2650 3755 2070 100 -50 1244 A C ATOM 2021 N LEU A 262 -12.716 -32.566 21.096 1.00 22.51 A N ANISOU 2021 N LEU A 262 2579 3532 2443 170 -0 1670 A N ATOM 2022 CA LEU A 262 -12.288 -33.899 20.704 1.00 25.05 A C ANISOU 2022 CA LEU A 262 2874 3722 2921 203 14 1768 A C ATOM 2023 C LEU A 262 -13.457 -34.876 20.598 1.00 24.80 A C ANISOU 2023 C LEU A 262 2853 3589 2981 180 82 1827 A C ATOM 2024 O LEU A 262 -13.357 -35.863 19.859 1.00 25.58 A O ANISOU 2024 O LEU A 262 2951 3533 3237 196 107 1860 A O ATOM 2025 CB LEU A 262 -11.247 -34.417 21.692 1.00 28.38 A C ANISOU 2025 CB LEU A 262 3257 4214 3313 235 -30 1885 A C ATOM 2026 CG LEU A 262 -9.832 -33.867 21.445 1.00 25.02 A C ANISOU 2026 CG LEU A 262 2802 3828 2876 265 -97 1848 A C ATOM 2027 CD1 LEU A 262 -8.864 -34.529 22.409 1.00 32.24 A C ANISOU 2027 CD1 LEU A 262 3666 4806 3778 294 -138 1985 A C ATOM 2028 CD2 LEU A 262 -9.377 -34.004 19.999 1.00 27.82 A C ANISOU 2028 CD2 LEU A 262 3153 4040 3376 297 -83 1784 A C ATOM 2029 N ASP A 263 -14.562 -34.637 21.311 1.00 24.37 A N ANISOU 2029 N ASP A 263 2810 3612 2838 139 117 1838 A N ATOM 2030 CA ASP A 263 -15.746 -35.463 21.085 1.00 24.45 A C ANISOU 2030 CA ASP A 263 2824 3522 2943 105 181 1881 A C ATOM 2031 C ASP A 263 -16.328 -35.191 19.705 1.00 22.56 A C ANISOU 2031 C ASP A 263 2605 3171 2798 77 202 1772 A C ATOM 2032 O ASP A 263 -16.723 -36.119 18.987 1.00 22.77 A O ANISOU 2032 O ASP A 263 2637 3045 2969 58 232 1791 A O ATOM 2033 CB ASP A 263 -16.817 -35.211 22.154 1.00 24.85 A C ANISOU 2033 CB ASP A 263 2874 3692 2878 69 221 1917 A C ATOM 2034 CG ASP A 263 -16.434 -35.750 23.528 1.00 30.89 A C ANISOU 2034 CG ASP A 263 3623 4550 3564 86 210 2049 A C ATOM 2035 OD1 ASP A 263 -15.303 -36.248 23.698 1.00 29.21 A O ANISOU 2035 OD1 ASP A 263 3393 4324 3382 126 165 2115 A O ATOM 2036 OD2 ASP A 263 -17.292 -35.702 24.438 1.00 28.60 A O ANISOU 2036 OD2 ASP A 263 3334 4350 3184 60 251 2094 A O ATOM 2037 N MET A 264 -16.383 -33.921 19.316 1.00 22.07 A N ANISOU 2037 N MET A 264 2554 3178 2652 71 185 1655 A N ATOM 2038 CA MET A 264 -16.895 -33.592 17.997 1.00 19.88 A C ANISOU 2038 CA MET A 264 2292 2807 2455 44 200 1557 A C ATOM 2039 C MET A 264 -15.980 -34.155 16.913 1.00 20.67 A C ANISOU 2039 C MET A 264 2405 2764 2686 73 179 1538 A C ATOM 2040 O MET A 264 -16.454 -34.535 15.837 1.00 21.58 A O ANISOU 2040 O MET A 264 2539 2746 2914 43 201 1494 A O ATOM 2041 CB MET A 264 -17.049 -32.073 17.864 1.00 18.67 A C ANISOU 2041 CB MET A 264 2147 2765 2183 40 186 1443 A C ATOM 2042 CG MET A 264 -17.814 -31.642 16.633 1.00 17.50 A C ANISOU 2042 CG MET A 264 2004 2546 2100 4 206 1355 A C ATOM 2043 SD MET A 264 -19.537 -32.220 16.743 1.00 19.52 A S ANISOU 2043 SD MET A 264 2235 2769 2413 -62 273 1398 A S ATOM 2044 CE MET A 264 -20.313 -30.811 17.546 1.00 18.03 A C ANISOU 2044 CE MET A 264 2031 2756 2061 -60 305 1341 A C ATOM 2045 N CYS A 265 -14.674 -34.232 17.187 1.00 21.45 A N ANISOU 2045 N CYS A 265 2492 2887 2770 129 138 1567 A N ATOM 2046 CA CYS A 265 -13.754 -34.902 16.270 1.00 23.46 A C ANISOU 2046 CA CYS A 265 2753 3004 3157 170 132 1561 A C ATOM 2047 C CYS A 265 -14.114 -36.372 16.101 1.00 24.87 A C ANISOU 2047 C CYS A 265 2944 3027 3480 161 178 1634 A C ATOM 2048 O CYS A 265 -14.140 -36.887 14.977 1.00 22.19 A O ANISOU 2048 O CYS A 265 2637 2530 3266 156 202 1580 A O ATOM 2049 CB CYS A 265 -12.315 -34.766 16.768 1.00 22.69 A C ANISOU 2049 CB CYS A 265 2623 2979 3020 230 84 1599 A C ATOM 2050 SG CYS A 265 -11.620 -33.118 16.584 1.00 21.77 A S ANISOU 2050 SG CYS A 265 2500 2995 2777 236 24 1488 A S ATOM 2051 N ALA A 266 -14.386 -37.067 17.214 1.00 23.49 A N ANISOU 2051 N ALA A 266 2748 2890 3289 158 191 1752 A N ATOM 2052 CA ALA A 266 -14.858 -38.444 17.132 1.00 23.67 A C ANISOU 2052 CA ALA A 266 2783 2765 3446 140 236 1824 A C ATOM 2053 C ALA A 266 -16.091 -38.551 16.243 1.00 25.71 A C ANISOU 2053 C ALA A 266 3076 2919 3772 63 270 1748 A C ATOM 2054 O ALA A 266 -16.184 -39.456 15.406 1.00 26.17 A O ANISOU 2054 O ALA A 266 3170 2803 3972 47 296 1725 A O ATOM 2055 CB ALA A 266 -15.154 -38.990 18.532 1.00 27.58 A C ANISOU 2055 CB ALA A 266 3248 3343 3890 136 245 1965 A C ATOM 2056 N SER A 267 -17.041 -37.616 16.394 1.00 25.04 A N ANISOU 2056 N SER A 267 2981 2942 3590 14 271 1701 A N ATOM 2057 CA SER A 267 -18.242 -37.620 15.562 1.00 23.20 A C ANISOU 2057 CA SER A 267 2764 2633 3418 -66 296 1632 A C ATOM 2058 C SER A 267 -17.894 -37.430 14.094 1.00 24.07 A C ANISOU 2058 C SER A 267 2915 2627 3605 -72 283 1511 A C ATOM 2059 O SER A 267 -18.427 -38.123 13.218 1.00 23.91 A O ANISOU 2059 O SER A 267 2928 2459 3699 -130 301 1466 A O ATOM 2060 CB SER A 267 -19.200 -36.524 16.029 1.00 24.09 A C ANISOU 2060 CB SER A 267 2846 2901 3407 -101 302 1606 A C ATOM 2061 OG SER A 267 -19.710 -36.842 17.305 1.00 26.99 A O ANISOU 2061 OG SER A 267 3184 3357 3716 -107 328 1712 A O ATOM 2062 N LEU A 268 -17.013 -36.473 13.806 1.00 21.82 A N ANISOU 2062 N LEU A 268 2630 2408 3253 -20 251 1451 A N ATOM 2063 CA LEU A 268 -16.556 -36.282 12.435 1.00 20.73 A C ANISOU 2063 CA LEU A 268 2530 2164 3182 -16 242 1342 A C ATOM 2064 C LEU A 268 -15.871 -37.534 11.901 1.00 21.64 A C ANISOU 2064 C LEU A 268 2684 2103 3435 15 265 1348 A C ATOM 2065 O LEU A 268 -16.074 -37.906 10.741 1.00 22.65 A O ANISOU 2065 O LEU A 268 2863 2090 3655 -22 281 1256 A O ATOM 2066 CB LEU A 268 -15.639 -35.061 12.354 1.00 21.41 A C ANISOU 2066 CB LEU A 268 2602 2361 3170 42 204 1295 A C ATOM 2067 CG LEU A 268 -15.076 -34.701 10.978 1.00 16.63 A C ANISOU 2067 CG LEU A 268 2031 1668 2619 56 198 1186 A C ATOM 2068 CD1 LEU A 268 -16.172 -34.532 9.932 1.00 17.49 A C ANISOU 2068 CD1 LEU A 268 2169 1704 2773 -31 209 1097 A C ATOM 2069 CD2 LEU A 268 -14.263 -33.407 11.071 1.00 17.79 A C ANISOU 2069 CD2 LEU A 268 2154 1949 2656 106 156 1154 A C ATOM 2070 N LYS A 269 -15.084 -38.216 12.740 1.00 22.21 A N ANISOU 2070 N LYS A 269 2734 2182 3521 79 269 1451 A N ATOM 2071 CA LYS A 269 -14.454 -39.465 12.321 1.00 23.28 A C ANISOU 2071 CA LYS A 269 2901 2149 3794 116 301 1467 A C ATOM 2072 C LYS A 269 -15.495 -40.473 11.856 1.00 25.07 A C ANISOU 2072 C LYS A 269 3178 2220 4128 34 336 1446 A C ATOM 2073 O LYS A 269 -15.357 -41.080 10.788 1.00 24.22 A O ANISOU 2073 O LYS A 269 3131 1949 4122 22 360 1359 A O ATOM 2074 CB LYS A 269 -13.633 -40.041 13.472 1.00 26.09 A C ANISOU 2074 CB LYS A 269 3210 2556 4145 187 298 1607 A C ATOM 2075 CG LYS A 269 -13.023 -41.397 13.202 1.00 29.33 A C ANISOU 2075 CG LYS A 269 3644 2796 4703 232 339 1646 A C ATOM 2076 CD LYS A 269 -11.989 -41.738 14.269 1.00 29.69 A C ANISOU 2076 CD LYS A 269 3626 2919 4735 314 326 1785 A C ATOM 2077 CE LYS A 269 -11.695 -43.231 14.270 1.00 36.09 A C ANISOU 2077 CE LYS A 269 4453 3561 5698 348 375 1860 A C ATOM 2078 NZ LYS A 269 -10.951 -43.651 15.486 1.00 36.53 A N ANISOU 2078 NZ LYS A 269 4438 3701 5740 411 360 2025 A N ATOM 2079 N GLU A 270 -16.554 -40.660 12.651 1.00 27.53 A N ANISOU 2079 N GLU A 270 3465 2584 4411 -29 340 1521 A N ATOM 2080 CA GLU A 270 -17.610 -41.596 12.272 1.00 26.64 A C ANISOU 2080 CA GLU A 270 3390 2335 4397 -122 367 1508 A C ATOM 2081 C GLU A 270 -18.326 -41.153 11.007 1.00 25.74 A C ANISOU 2081 C GLU A 270 3317 2166 4298 -207 356 1360 A C ATOM 2082 O GLU A 270 -18.661 -41.987 10.159 1.00 30.30 A O ANISOU 2082 O GLU A 270 3957 2580 4977 -269 370 1291 A O ATOM 2083 CB GLU A 270 -18.599 -41.774 13.424 1.00 27.11 A C ANISOU 2083 CB GLU A 270 3401 2485 4415 -169 377 1625 A C ATOM 2084 CG GLU A 270 -17.903 -42.221 14.681 1.00 29.04 A C ANISOU 2084 CG GLU A 270 3607 2792 4635 -92 383 1773 A C ATOM 2085 CD GLU A 270 -17.357 -43.624 14.538 1.00 31.83 A C ANISOU 2085 CD GLU A 270 3995 2965 5132 -63 413 1824 A C ATOM 2086 OE1 GLU A 270 -18.089 -44.485 14.005 1.00 37.44 A O ANISOU 2086 OE1 GLU A 270 4751 3523 5950 -138 438 1797 A O ATOM 2087 OE2 GLU A 270 -16.180 -43.854 14.906 1.00 37.71 A O ANISOU 2087 OE2 GLU A 270 4723 3719 5887 32 410 1886 A O ATOM 2088 N LEU A 271 -18.566 -39.847 10.853 1.00 23.91 A N ANISOU 2088 N LEU A 271 3052 2068 3963 -217 327 1307 A N ATOM 2089 CA LEU A 271 -19.216 -39.369 9.636 1.00 24.96 A C ANISOU 2089 CA LEU A 271 3215 2162 4108 -299 310 1172 A C ATOM 2090 C LEU A 271 -18.344 -39.618 8.414 1.00 25.88 A C ANISOU 2090 C LEU A 271 3404 2141 4287 -271 313 1055 A C ATOM 2091 O LEU A 271 -18.851 -39.941 7.333 1.00 26.90 A O ANISOU 2091 O LEU A 271 3590 2162 4469 -353 308 943 A O ATOM 2092 CB LEU A 271 -19.550 -37.885 9.760 1.00 24.27 A C ANISOU 2092 CB LEU A 271 3072 2248 3902 -301 281 1150 A C ATOM 2093 CG LEU A 271 -20.672 -37.540 10.735 1.00 23.80 A C ANISOU 2093 CG LEU A 271 2944 2324 3776 -344 287 1228 A C ATOM 2094 CD1 LEU A 271 -20.651 -36.045 11.019 1.00 18.51 A C ANISOU 2094 CD1 LEU A 271 2228 1829 2977 -309 269 1211 A C ATOM 2095 CD2 LEU A 271 -22.002 -37.971 10.148 1.00 24.32 A C ANISOU 2095 CD2 LEU A 271 3006 2328 3908 -465 286 1187 A C ATOM 2096 N LEU A 272 -17.026 -39.485 8.575 1.00 24.52 A N ANISOU 2096 N LEU A 272 3231 1981 4104 -157 322 1076 A N ATOM 2097 CA LEU A 272 -16.109 -39.739 7.470 1.00 25.86 A C ANISOU 2097 CA LEU A 272 3464 2030 4331 -112 340 969 A C ATOM 2098 C LEU A 272 -16.076 -41.220 7.111 1.00 26.98 A C ANISOU 2098 C LEU A 272 3674 1983 4594 -127 378 952 A C ATOM 2099 O LEU A 272 -16.080 -41.576 5.927 1.00 28.78 A O ANISOU 2099 O LEU A 272 3979 2086 4869 -164 391 818 A O ATOM 2100 CB LEU A 272 -14.716 -39.239 7.841 1.00 23.83 A C ANISOU 2100 CB LEU A 272 3168 1853 4035 16 340 1012 A C ATOM 2101 CG LEU A 272 -14.563 -37.722 7.828 1.00 22.99 A C ANISOU 2101 CG LEU A 272 3019 1902 3815 32 302 986 A C ATOM 2102 CD1 LEU A 272 -13.200 -37.330 8.370 1.00 25.03 A C ANISOU 2102 CD1 LEU A 272 3228 2251 4031 146 292 1046 A C ATOM 2103 CD2 LEU A 272 -14.758 -37.176 6.417 1.00 21.77 A C ANISOU 2103 CD2 LEU A 272 2916 1692 3666 -13 301 832 A C ATOM 2104 N GLN A 273 -16.067 -42.097 8.117 1.00 28.19 A N ANISOU 2104 N GLN A 273 3803 2113 4794 -104 397 1083 A N ATOM 2105 CA GLN A 273 -15.938 -43.527 7.860 1.00 30.25 A C ANISOU 2105 CA GLN A 273 4126 2187 5179 -108 438 1082 A C ATOM 2106 C GLN A 273 -17.260 -44.171 7.476 1.00 30.28 A C ANISOU 2106 C GLN A 273 4182 2092 5231 -249 431 1036 A C ATOM 2107 O GLN A 273 -17.257 -45.195 6.789 1.00 30.92 A O ANISOU 2107 O GLN A 273 4345 1997 5405 -280 456 969 A O ATOM 2108 CB GLN A 273 -15.378 -44.244 9.090 1.00 29.41 A C ANISOU 2108 CB GLN A 273 3970 2092 5113 -28 460 1252 A C ATOM 2109 CG GLN A 273 -13.925 -43.937 9.375 1.00 31.77 A C ANISOU 2109 CG GLN A 273 4223 2456 5394 109 467 1297 A C ATOM 2110 CD GLN A 273 -13.474 -44.459 10.720 1.00 32.25 A C ANISOU 2110 CD GLN A 273 4215 2572 5465 174 471 1479 A C ATOM 2111 NE2 GLN A 273 -12.170 -44.419 10.959 1.00 35.08 A N ANISOU 2111 NE2 GLN A 273 4529 2970 5830 286 477 1528 A N ATOM 2112 OE1 GLN A 273 -14.290 -44.873 11.550 1.00 38.00 A O ANISOU 2112 OE1 GLN A 273 4926 3319 6194 120 468 1576 A O ATOM 2113 N ASN A 274 -18.383 -43.587 7.889 1.00 29.64 A N ANISOU 2113 N ASN A 274 4052 2125 5086 -336 400 1068 A N ATOM 2114 CA ASN A 274 -19.684 -44.210 7.715 1.00 32.02 A C ANISOU 2114 CA ASN A 274 4377 2358 5431 -475 392 1054 A C ATOM 2115 C ASN A 274 -20.568 -43.495 6.707 1.00 29.80 A C ANISOU 2115 C ASN A 274 4110 2112 5100 -588 349 920 A C ATOM 2116 O ASN A 274 -21.526 -44.097 6.214 1.00 32.34 A O ANISOU 2116 O ASN A 274 4470 2353 5465 -715 335 869 A O ATOM 2117 CB ASN A 274 -20.425 -44.248 9.058 1.00 33.67 A C ANISOU 2117 CB ASN A 274 4503 2676 5616 -494 397 1213 A C ATOM 2118 CG ASN A 274 -19.703 -45.083 10.092 1.00 38.53 A C ANISOU 2118 CG ASN A 274 5102 3257 6281 -402 433 1358 A C ATOM 2119 ND2 ASN A 274 -19.954 -44.788 11.367 1.00 38.43 A N ANISOU 2119 ND2 ASN A 274 5007 3390 6203 -376 434 1498 A N ATOM 2120 OD1 ASN A 274 -18.910 -45.967 9.757 1.00 39.23 A O ANISOU 2120 OD1 ASN A 274 5249 3196 6461 -351 460 1344 A O ATOM 2121 N GLY A 275 -20.279 -42.241 6.394 1.00 31.09 A N ANISOU 2121 N GLY A 275 4241 2398 5175 -551 324 865 A N ATOM 2122 CA GLY A 275 -21.239 -41.431 5.686 1.00 30.05 A C ANISOU 2122 CA GLY A 275 4089 2341 4987 -656 278 775 A C ATOM 2123 C GLY A 275 -22.362 -41.005 6.625 1.00 33.07 A C ANISOU 2123 C GLY A 275 4370 2865 5329 -706 269 880 A C ATOM 2124 O GLY A 275 -22.270 -41.093 7.847 1.00 34.44 A O ANISOU 2124 O GLY A 275 4489 3106 5489 -646 295 1016 A O ATOM 2125 N MET A 276 -23.445 -40.532 6.019 1.00 34.73 A N ANISOU 2125 N MET A 276 4550 3133 5515 -815 230 813 A N ATOM 2126 CA MET A 276 -24.576 -40.028 6.784 1.00 34.05 A C ANISOU 2126 CA MET A 276 4356 3193 5390 -856 224 899 A C ATOM 2127 C MET A 276 -25.754 -40.991 6.840 1.00 37.76 A C ANISOU 2127 C MET A 276 4814 3602 5930 -976 228 925 A C ATOM 2128 O MET A 276 -26.658 -40.786 7.658 1.00 37.63 A O ANISOU 2128 O MET A 276 4705 3695 5896 -996 239 1020 A O ATOM 2129 CB MET A 276 -25.038 -38.681 6.221 1.00 35.04 A C ANISOU 2129 CB MET A 276 4421 3457 5437 -876 177 830 A C ATOM 2130 CG MET A 276 -23.964 -37.612 6.259 1.00 33.68 A C ANISOU 2130 CG MET A 276 4247 3357 5191 -765 174 817 A C ATOM 2131 SD MET A 276 -24.713 -35.982 6.132 1.00 33.40 A S ANISOU 2131 SD MET A 276 4110 3520 5059 -775 132 798 A S ATOM 2132 CE MET A 276 -23.278 -34.979 5.796 1.00 24.05 A C ANISOU 2132 CE MET A 276 2963 2359 3816 -670 123 748 A C ATOM 2133 N ASN A 277 -25.754 -42.039 6.016 1.00 37.53 A N ANISOU 2133 N ASN A 277 4881 3404 5976 -1057 224 843 A N ATOM 2134 CA ASN A 277 -26.823 -43.030 6.006 1.00 39.23 A C ANISOU 2134 CA ASN A 277 5096 3545 6266 -1184 228 861 A C ATOM 2135 C ASN A 277 -28.176 -42.379 5.727 1.00 38.87 A C ANISOU 2135 C ASN A 277 4948 3631 6191 -1283 188 840 A C ATOM 2136 O ASN A 277 -29.173 -42.638 6.409 1.00 39.74 A O ANISOU 2136 O ASN A 277 4976 3791 6331 -1333 202 935 A O ATOM 2137 CB ASN A 277 -26.858 -43.819 7.316 1.00 40.43 A C ANISOU 2137 CB ASN A 277 5221 3671 6469 -1146 280 1024 A C ATOM 2138 CG ASN A 277 -27.719 -45.052 7.219 1.00 45.38 A C ANISOU 2138 CG ASN A 277 5877 4173 7194 -1276 290 1037 A C ATOM 2139 ND2 ASN A 277 -28.325 -45.442 8.339 1.00 48.57 A N ANISOU 2139 ND2 ASN A 277 6207 4618 7628 -1282 324 1185 A N ATOM 2140 OD1 ASN A 277 -27.869 -45.635 6.142 1.00 48.47 A O ANISOU 2140 OD1 ASN A 277 6356 4435 7626 -1378 267 913 A O ATOM 2141 N GLY A 278 -28.206 -41.527 4.707 1.00 37.65 A N ANISOU 2141 N GLY A 278 4789 3536 5979 -1304 138 719 A N ATOM 2142 CA GLY A 278 -29.455 -40.954 4.252 1.00 34.02 A C ANISOU 2142 CA GLY A 278 4230 3195 5502 -1392 87 689 A C ATOM 2143 C GLY A 278 -29.948 -39.769 5.047 1.00 37.45 A C ANISOU 2143 C GLY A 278 4532 3826 5870 -1321 83 786 A C ATOM 2144 O GLY A 278 -31.066 -39.301 4.805 1.00 36.65 A O ANISOU 2144 O GLY A 278 4334 3831 5760 -1380 44 787 A O ATOM 2145 N ARG A 279 -29.156 -39.260 5.980 1.00 36.32 A N ANISOU 2145 N ARG A 279 4383 3738 5680 -1195 124 866 A N ATOM 2146 CA ARG A 279 -29.568 -38.137 6.802 1.00 30.56 A C ANISOU 2146 CA ARG A 279 3543 3190 4877 -1123 135 949 A C ATOM 2147 C ARG A 279 -28.868 -36.873 6.330 1.00 29.61 A C ANISOU 2147 C ARG A 279 3427 3150 4674 -1048 105 881 A C ATOM 2148 O ARG A 279 -27.937 -36.908 5.521 1.00 28.88 A O ANISOU 2148 O ARG A 279 3421 2973 4578 -1037 82 788 A O ATOM 2149 CB ARG A 279 -29.256 -38.422 8.271 1.00 30.31 A C ANISOU 2149 CB ARG A 279 3497 3183 4835 -1041 204 1086 A C ATOM 2150 CG ARG A 279 -30.183 -39.465 8.856 1.00 32.49 A C ANISOU 2150 CG ARG A 279 3741 3419 5186 -1116 235 1175 A C ATOM 2151 CD ARG A 279 -29.715 -39.875 10.223 1.00 33.27 A C ANISOU 2151 CD ARG A 279 3844 3528 5271 -1035 298 1307 A C ATOM 2152 NE ARG A 279 -28.458 -40.618 10.145 1.00 35.48 A N ANISOU 2152 NE ARG A 279 4231 3667 5583 -989 308 1296 A N ATOM 2153 CZ ARG A 279 -27.977 -41.376 11.124 1.00 34.29 A C ANISOU 2153 CZ ARG A 279 4102 3474 5452 -938 352 1406 A C ATOM 2154 NH1 ARG A 279 -28.662 -41.513 12.258 1.00 32.41 A N ANISOU 2154 NH1 ARG A 279 3794 3324 5198 -935 392 1532 A N ATOM 2155 NH2 ARG A 279 -26.809 -41.993 10.967 1.00 33.36 A N ANISOU 2155 NH2 ARG A 279 4074 3231 5371 -886 356 1393 A N ATOM 2156 N THR A 280 -29.333 -35.738 6.837 1.00 27.68 A N ANISOU 2156 N THR A 280 3090 3066 4362 -994 111 926 A N ATOM 2157 CA THR A 280 -28.743 -34.463 6.478 1.00 24.71 A C ANISOU 2157 CA THR A 280 2709 2773 3906 -923 88 872 A C ATOM 2158 C THR A 280 -28.348 -33.717 7.742 1.00 22.14 A C ANISOU 2158 C THR A 280 2351 2556 3506 -809 147 957 A C ATOM 2159 O THR A 280 -28.816 -34.012 8.845 1.00 21.58 A O ANISOU 2159 O THR A 280 2239 2529 3431 -790 200 1054 A O ATOM 2160 CB THR A 280 -29.693 -33.596 5.637 1.00 24.44 A C ANISOU 2160 CB THR A 280 2600 2835 3851 -966 30 818 A C ATOM 2161 CG2 THR A 280 -29.980 -34.279 4.306 1.00 25.94 A C ANISOU 2161 CG2 THR A 280 2835 2933 4089 -1080 -39 718 A C ATOM 2162 OG1 THR A 280 -30.930 -33.415 6.332 1.00 23.51 A O ANISOU 2162 OG1 THR A 280 2376 2815 3742 -973 57 902 A O ATOM 2163 N ILE A 281 -27.452 -32.759 7.558 1.00 18.56 A N ANISOU 2163 N ILE A 281 1920 2145 2986 -738 138 914 A N ATOM 2164 CA ILE A 281 -27.010 -31.849 8.602 1.00 18.95 A C ANISOU 2164 CA ILE A 281 1948 2310 2944 -633 187 964 A C ATOM 2165 C ILE A 281 -27.179 -30.434 8.082 1.00 19.21 A C ANISOU 2165 C ILE A 281 1936 2443 2920 -605 163 903 A C ATOM 2166 O ILE A 281 -26.569 -30.067 7.072 1.00 17.80 A O ANISOU 2166 O ILE A 281 1796 2228 2738 -613 113 819 A O ATOM 2167 CB ILE A 281 -25.548 -32.100 9.002 1.00 18.97 A C ANISOU 2167 CB ILE A 281 2030 2259 2918 -563 202 980 A C ATOM 2168 CG1 ILE A 281 -25.328 -33.568 9.394 1.00 17.43 A C ANISOU 2168 CG1 ILE A 281 1883 1945 2795 -584 222 1040 A C ATOM 2169 CG2 ILE A 281 -25.125 -31.110 10.063 1.00 16.86 A C ANISOU 2169 CG2 ILE A 281 1746 2127 2534 -465 243 1018 A C ATOM 2170 CD1 ILE A 281 -23.887 -33.884 9.866 1.00 19.63 A C ANISOU 2170 CD1 ILE A 281 2229 2178 3053 -498 236 1072 A C ATOM 2171 N LEU A 282 -27.987 -29.635 8.777 1.00 19.64 A N ANISOU 2171 N LEU A 282 1914 2619 2927 -564 205 938 A N ATOM 2172 CA LEU A 282 -28.273 -28.263 8.365 1.00 20.10 A C ANISOU 2172 CA LEU A 282 1923 2770 2943 -525 194 886 A C ATOM 2173 C LEU A 282 -28.655 -28.216 6.886 1.00 20.75 A C ANISOU 2173 C LEU A 282 1992 2813 3080 -598 109 816 A C ATOM 2174 O LEU A 282 -28.170 -27.380 6.114 1.00 22.72 A O ANISOU 2174 O LEU A 282 2255 3079 3300 -578 70 748 A O ATOM 2175 CB LEU A 282 -27.092 -27.331 8.668 1.00 17.15 A C ANISOU 2175 CB LEU A 282 1603 2436 2476 -430 210 841 A C ATOM 2176 CG LEU A 282 -26.933 -26.998 10.155 1.00 17.48 A C ANISOU 2176 CG LEU A 282 1643 2566 2431 -355 293 901 A C ATOM 2177 CD1 LEU A 282 -25.665 -26.167 10.410 1.00 18.20 A C ANISOU 2177 CD1 LEU A 282 1814 2680 2421 -265 283 822 A C ATOM 2178 CD2 LEU A 282 -28.182 -26.339 10.752 1.00 19.42 A C ANISOU 2178 CD2 LEU A 282 1810 2906 2661 -325 349 923 A C ATOM 2179 N GLY A 283 -29.519 -29.156 6.490 1.00 21.31 A N ANISOU 2179 N GLY A 283 2042 2832 3221 -688 78 829 A N ATOM 2180 CA GLY A 283 -30.013 -29.211 5.128 1.00 24.91 A C ANISOU 2180 CA GLY A 283 2490 3264 3712 -767 -8 762 A C ATOM 2181 C GLY A 283 -29.000 -29.640 4.089 1.00 25.35 A C ANISOU 2181 C GLY A 283 2646 3218 3768 -811 -65 671 A C ATOM 2182 O GLY A 283 -29.236 -29.454 2.893 1.00 24.68 A O ANISOU 2182 O GLY A 283 2568 3133 3677 -861 -138 598 A O ATOM 2183 N SER A 284 -27.879 -30.225 4.503 1.00 22.17 A N ANISOU 2183 N SER A 284 2325 2730 3370 -788 -32 675 A N ATOM 2184 CA SER A 284 -26.858 -30.669 3.565 1.00 19.86 A C ANISOU 2184 CA SER A 284 2137 2325 3082 -814 -71 585 A C ATOM 2185 C SER A 284 -26.600 -32.156 3.745 1.00 21.23 A C ANISOU 2185 C SER A 284 2381 2353 3331 -860 -47 597 A C ATOM 2186 O SER A 284 -26.593 -32.665 4.871 1.00 18.58 A O ANISOU 2186 O SER A 284 2034 2007 3020 -826 14 691 A O ATOM 2187 CB SER A 284 -25.555 -29.882 3.749 1.00 20.48 A C ANISOU 2187 CB SER A 284 2276 2430 3076 -683 -48 536 A C ATOM 2188 OG SER A 284 -24.554 -30.368 2.866 1.00 19.94 A O ANISOU 2188 OG SER A 284 2313 2257 3007 -684 -69 441 A O ATOM 2189 N ALA A 285 -26.410 -32.853 2.628 1.00 21.43 A N ANISOU 2189 N ALA A 285 2485 2271 3385 -932 -90 497 A N ATOM 2190 CA ALA A 285 -26.002 -34.245 2.634 1.00 20.53 A C ANISOU 2190 CA ALA A 285 2459 1994 3346 -964 -58 483 A C ATOM 2191 C ALA A 285 -24.489 -34.398 2.527 1.00 22.71 A C ANISOU 2191 C ALA A 285 2832 2168 3627 -887 -31 448 A C ATOM 2192 O ALA A 285 -24.001 -35.520 2.365 1.00 23.31 A O ANISOU 2192 O ALA A 285 2995 2094 3768 -896 1 418 A O ATOM 2193 CB ALA A 285 -26.683 -35.002 1.497 1.00 24.39 A C ANISOU 2193 CB ALA A 285 2986 2414 3866 -1083 -104 381 A C ATOM 2194 N LEU A 286 -23.751 -33.295 2.608 1.00 18.37 A N ANISOU 2194 N LEU A 286 2277 1723 2982 -775 -27 424 A N ATOM 2195 CA LEU A 286 -22.296 -33.282 2.558 1.00 22.99 A C ANISOU 2195 CA LEU A 286 2936 2259 3540 -666 7 383 A C ATOM 2196 C LEU A 286 -21.762 -32.559 3.786 1.00 21.26 A C ANISOU 2196 C LEU A 286 2667 2145 3265 -551 42 474 A C ATOM 2197 O LEU A 286 -22.445 -31.709 4.362 1.00 18.84 A O ANISOU 2197 O LEU A 286 2283 1968 2908 -545 35 522 A O ATOM 2198 CB LEU A 286 -21.788 -32.562 1.304 1.00 22.58 A C ANISOU 2198 CB LEU A 286 2929 2236 3412 -651 -30 251 A C ATOM 2199 CG LEU A 286 -21.974 -33.202 -0.062 1.00 24.18 A C ANISOU 2199 CG LEU A 286 3211 2343 3633 -748 -62 130 A C ATOM 2200 CD1 LEU A 286 -21.237 -32.379 -1.099 1.00 24.92 A C ANISOU 2200 CD1 LEU A 286 3348 2489 3632 -702 -81 24 A C ATOM 2201 CD2 LEU A 286 -21.471 -34.650 -0.044 1.00 28.45 A C ANISOU 2201 CD2 LEU A 286 3841 2691 4277 -761 -10 116 A C ATOM 2202 N LEU A 287 -20.533 -32.889 4.185 1.00 19.96 A N ANISOU 2202 N LEU A 287 2547 1928 3109 -460 79 496 A N ATOM 2203 CA LEU A 287 -19.868 -32.136 5.245 1.00 18.23 A C ANISOU 2203 CA LEU A 287 2289 1819 2819 -359 96 565 A C ATOM 2204 C LEU A 287 -19.389 -30.798 4.682 1.00 18.52 A C ANISOU 2204 C LEU A 287 2320 1954 2761 -312 65 475 A C ATOM 2205 O LEU A 287 -18.542 -30.765 3.786 1.00 20.59 A O ANISOU 2205 O LEU A 287 2633 2168 3022 -285 59 392 A O ATOM 2206 CB LEU A 287 -18.712 -32.953 5.831 1.00 17.41 A C ANISOU 2206 CB LEU A 287 2220 1635 2761 -282 135 633 A C ATOM 2207 CG LEU A 287 -19.186 -34.311 6.365 1.00 19.88 A C ANISOU 2207 CG LEU A 287 2541 1830 3181 -329 170 735 A C ATOM 2208 CD1 LEU A 287 -18.045 -35.220 6.826 1.00 22.19 A C ANISOU 2208 CD1 LEU A 287 2867 2020 3542 -248 211 814 A C ATOM 2209 CD2 LEU A 287 -20.183 -34.104 7.479 1.00 19.81 A C ANISOU 2209 CD2 LEU A 287 2460 1927 3139 -361 179 848 A C ATOM 2210 N GLU A 288 -19.938 -29.698 5.200 1.00 15.05 A N ANISOU 2210 N GLU A 288 1821 1647 2249 -301 53 493 A N ATOM 2211 CA GLU A 288 -19.685 -28.347 4.703 1.00 15.76 A C ANISOU 2211 CA GLU A 288 1900 1825 2264 -267 24 417 A C ATOM 2212 C GLU A 288 -18.456 -27.737 5.349 1.00 13.01 A C ANISOU 2212 C GLU A 288 1558 1528 1857 -176 32 427 A C ATOM 2213 O GLU A 288 -18.342 -27.710 6.578 1.00 14.08 A O ANISOU 2213 O GLU A 288 1671 1719 1961 -141 52 505 A O ATOM 2214 CB GLU A 288 -20.883 -27.442 4.989 1.00 17.71 A C ANISOU 2214 CB GLU A 288 2078 2176 2476 -291 17 433 A C ATOM 2215 CG GLU A 288 -22.182 -27.933 4.355 1.00 18.99 A C ANISOU 2215 CG GLU A 288 2209 2311 2695 -390 -4 435 A C ATOM 2216 CD GLU A 288 -22.158 -27.847 2.837 1.00 27.07 A C ANISOU 2216 CD GLU A 288 3268 3297 3722 -438 -56 338 A C ATOM 2217 OE1 GLU A 288 -23.076 -28.406 2.193 1.00 29.37 A O ANISOU 2217 OE1 GLU A 288 3546 3556 4058 -534 -87 328 A O ATOM 2218 OE2 GLU A 288 -21.268 -27.154 2.288 1.00 26.24 A O ANISOU 2218 OE2 GLU A 288 3197 3206 3567 -386 -68 274 A O ATOM 2219 N ASP A 289 -17.560 -27.185 4.528 1.00 14.67 A N ANISOU 2219 N ASP A 289 1796 1733 2045 -143 14 351 A N ATOM 2220 CA ASP A 289 -16.325 -26.657 5.088 1.00 13.25 A C ANISOU 2220 CA ASP A 289 1613 1598 1821 -69 14 364 A C ATOM 2221 C ASP A 289 -16.100 -25.178 4.768 1.00 15.09 A C ANISOU 2221 C ASP A 289 1832 1912 1990 -50 -12 301 A C ATOM 2222 O ASP A 289 -14.972 -24.701 4.907 1.00 13.36 A O ANISOU 2222 O ASP A 289 1613 1718 1744 -3 -21 292 A O ATOM 2223 CB ASP A 289 -15.131 -27.507 4.632 1.00 12.32 A C ANISOU 2223 CB ASP A 289 1533 1391 1757 -31 30 361 A C ATOM 2224 CG ASP A 289 -14.639 -27.177 3.205 1.00 15.77 A C ANISOU 2224 CG ASP A 289 2003 1795 2195 -32 25 261 A C ATOM 2225 OD1 ASP A 289 -15.395 -26.604 2.392 1.00 13.91 A O ANISOU 2225 OD1 ASP A 289 1772 1582 1933 -81 3 199 A O ATOM 2226 OD2 ASP A 289 -13.470 -27.543 2.907 1.00 13.37 A O ANISOU 2226 OD2 ASP A 289 1716 1444 1919 20 47 256 A O ATOM 2227 N GLU A 290 -17.140 -24.426 4.365 1.00 12.40 A N ANISOU 2227 N GLU A 290 1470 1609 1632 -86 -25 267 A N ATOM 2228 CA GLU A 290 -16.948 -23.017 4.045 1.00 14.79 A C ANISOU 2228 CA GLU A 290 1761 1970 1890 -65 -44 216 A C ATOM 2229 C GLU A 290 -17.614 -22.077 5.042 1.00 13.89 A C ANISOU 2229 C GLU A 290 1611 1933 1732 -50 -32 233 A C ATOM 2230 O GLU A 290 -17.936 -20.941 4.695 1.00 13.68 A O ANISOU 2230 O GLU A 290 1570 1938 1691 -43 -40 195 A O ATOM 2231 CB GLU A 290 -17.382 -22.691 2.612 1.00 16.39 A C ANISOU 2231 CB GLU A 290 1969 2153 2104 -102 -68 160 A C ATOM 2232 CG GLU A 290 -16.524 -23.454 1.578 1.00 14.81 A C ANISOU 2232 CG GLU A 290 1819 1882 1925 -108 -68 121 A C ATOM 2233 CD GLU A 290 -16.399 -22.771 0.210 1.00 20.66 A C ANISOU 2233 CD GLU A 290 2576 2633 2641 -123 -90 61 A C ATOM 2234 OE1 GLU A 290 -17.158 -21.810 -0.081 1.00 16.07 A O ANISOU 2234 OE1 GLU A 290 1963 2103 2040 -139 -116 59 A O ATOM 2235 OE2 GLU A 290 -15.545 -23.240 -0.597 1.00 17.84 A O ANISOU 2235 OE2 GLU A 290 2261 2230 2286 -116 -77 23 A O ATOM 2236 N PHE A 291 -17.744 -22.504 6.299 1.00 14.28 A N ANISOU 2236 N PHE A 291 1653 2015 1760 -38 -6 291 A N ATOM 2237 CA PHE A 291 -18.110 -21.626 7.409 1.00 13.38 A C ANISOU 2237 CA PHE A 291 1521 1980 1582 -14 17 297 A C ATOM 2238 C PHE A 291 -16.993 -21.654 8.445 1.00 13.00 A C ANISOU 2238 C PHE A 291 1495 1972 1471 18 10 318 A C ATOM 2239 O PHE A 291 -16.664 -22.722 8.977 1.00 11.77 A O ANISOU 2239 O PHE A 291 1344 1806 1321 19 14 389 A O ATOM 2240 CB PHE A 291 -19.421 -22.068 8.076 1.00 14.78 A C ANISOU 2240 CB PHE A 291 1664 2187 1766 -34 61 357 A C ATOM 2241 CG PHE A 291 -20.592 -22.094 7.162 1.00 15.14 A C ANISOU 2241 CG PHE A 291 1669 2209 1876 -73 59 353 A C ATOM 2242 CD1 PHE A 291 -21.252 -20.920 6.833 1.00 19.41 A C ANISOU 2242 CD1 PHE A 291 2178 2783 2416 -58 65 316 A C ATOM 2243 CD2 PHE A 291 -21.018 -23.280 6.598 1.00 14.78 A C ANISOU 2243 CD2 PHE A 291 1618 2104 1895 -129 47 387 A C ATOM 2244 CE1 PHE A 291 -22.352 -20.934 5.988 1.00 17.85 A C ANISOU 2244 CE1 PHE A 291 1928 2578 2276 -95 52 329 A C ATOM 2245 CE2 PHE A 291 -22.097 -23.300 5.737 1.00 17.88 A C ANISOU 2245 CE2 PHE A 291 1968 2486 2339 -180 30 384 A C ATOM 2246 CZ PHE A 291 -22.770 -22.123 5.436 1.00 19.25 A C ANISOU 2246 CZ PHE A 291 2095 2711 2506 -162 29 362 A C ATOM 2247 N THR A 292 -16.430 -20.489 8.759 1.00 11.37 A N ANISOU 2247 N THR A 292 1301 1810 1209 38 -4 263 A N ATOM 2248 CA THR A 292 -15.413 -20.441 9.795 1.00 15.70 A C ANISOU 2248 CA THR A 292 1865 2414 1685 54 -25 282 A C ATOM 2249 C THR A 292 -16.044 -20.460 11.184 1.00 12.97 A C ANISOU 2249 C THR A 292 1523 2149 1255 57 12 319 A C ATOM 2250 O THR A 292 -17.243 -20.183 11.338 1.00 13.60 A O ANISOU 2250 O THR A 292 1591 2243 1333 56 62 311 A O ATOM 2251 CB THR A 292 -14.582 -19.175 9.671 1.00 15.10 A C ANISOU 2251 CB THR A 292 1803 2357 1578 59 -59 204 A C ATOM 2252 CG2 THR A 292 -13.995 -19.028 8.304 1.00 12.82 A C ANISOU 2252 CG2 THR A 292 1508 2002 1362 56 -84 172 A C ATOM 2253 OG1 THR A 292 -15.421 -18.060 9.993 1.00 16.38 A O ANISOU 2253 OG1 THR A 292 1975 2542 1704 61 -26 144 A O ATOM 2254 N PRO A 293 -15.256 -20.759 12.221 1.00 16.48 A N ANISOU 2254 N PRO A 293 1980 2659 1624 63 -11 366 A N ATOM 2255 CA PRO A 293 -15.770 -20.585 13.587 1.00 14.75 A C ANISOU 2255 CA PRO A 293 1776 2536 1292 64 25 388 A C ATOM 2256 C PRO A 293 -16.362 -19.202 13.799 1.00 17.61 A C ANISOU 2256 C PRO A 293 2161 2927 1602 69 60 282 A C ATOM 2257 O PRO A 293 -17.415 -19.072 14.431 1.00 16.43 A O ANISOU 2257 O PRO A 293 2011 2820 1409 77 129 287 A O ATOM 2258 CB PRO A 293 -14.527 -20.829 14.452 1.00 15.86 A C ANISOU 2258 CB PRO A 293 1927 2748 1349 63 -33 434 A C ATOM 2259 CG PRO A 293 -13.781 -21.879 13.699 1.00 16.96 A C ANISOU 2259 CG PRO A 293 2038 2813 1593 74 -68 505 A C ATOM 2260 CD PRO A 293 -13.949 -21.455 12.224 1.00 15.43 A C ANISOU 2260 CD PRO A 293 1839 2519 1505 72 -64 422 A C ATOM 2261 N PHE A 294 -15.729 -18.168 13.228 1.00 17.40 A N ANISOU 2261 N PHE A 294 2151 2869 1592 66 23 189 A N ATOM 2262 CA PHE A 294 -16.269 -16.815 13.324 1.00 19.12 A C ANISOU 2262 CA PHE A 294 2394 3085 1785 75 61 86 A C ATOM 2263 C PHE A 294 -17.650 -16.734 12.702 1.00 18.78 A C ANISOU 2263 C PHE A 294 2316 2997 1822 96 127 91 A C ATOM 2264 O PHE A 294 -18.578 -16.171 13.300 1.00 19.53 A O ANISOU 2264 O PHE A 294 2417 3123 1881 119 199 61 A O ATOM 2265 CB PHE A 294 -15.339 -15.806 12.639 1.00 20.30 A C ANISOU 2265 CB PHE A 294 2560 3186 1968 62 7 3 A C ATOM 2266 CG PHE A 294 -15.928 -14.415 12.551 1.00 25.02 A C ANISOU 2266 CG PHE A 294 3184 3749 2575 77 51 -97 A C ATOM 2267 CD1 PHE A 294 -15.646 -13.472 13.523 1.00 27.23 A C ANISOU 2267 CD1 PHE A 294 3522 4066 2758 66 59 -184 A C ATOM 2268 CD2 PHE A 294 -16.759 -14.053 11.491 1.00 26.65 A C ANISOU 2268 CD2 PHE A 294 3359 3882 2887 100 84 -102 A C ATOM 2269 CE1 PHE A 294 -16.199 -12.202 13.459 1.00 30.28 A C ANISOU 2269 CE1 PHE A 294 3939 4400 3168 86 112 -279 A C ATOM 2270 CE2 PHE A 294 -17.318 -12.786 11.427 1.00 30.06 A C ANISOU 2270 CE2 PHE A 294 3808 4272 3342 125 131 -178 A C ATOM 2271 CZ PHE A 294 -17.027 -11.858 12.412 1.00 30.32 A C ANISOU 2271 CZ PHE A 294 3904 4325 3293 122 150 -270 A C ATOM 2272 N ASP A 295 -17.783 -17.250 11.473 1.00 14.95 A N ANISOU 2272 N ASP A 295 1793 2441 1445 88 103 124 A N ATOM 2273 CA ASP A 295 -19.061 -17.226 10.769 1.00 16.84 A C ANISOU 2273 CA ASP A 295 1987 2646 1764 96 145 140 A C ATOM 2274 C ASP A 295 -20.155 -17.882 11.597 1.00 17.61 A C ANISOU 2274 C ASP A 295 2055 2796 1839 99 211 207 A C ATOM 2275 O ASP A 295 -21.286 -17.391 11.649 1.00 19.55 A O ANISOU 2275 O ASP A 295 2266 3054 2110 121 273 203 A O ATOM 2276 CB ASP A 295 -18.938 -17.941 9.427 1.00 15.64 A C ANISOU 2276 CB ASP A 295 1809 2427 1705 70 98 171 A C ATOM 2277 CG ASP A 295 -17.934 -17.283 8.509 1.00 17.44 A C ANISOU 2277 CG ASP A 295 2058 2609 1958 68 45 114 A C ATOM 2278 OD1 ASP A 295 -17.601 -16.113 8.768 1.00 17.81 A O ANISOU 2278 OD1 ASP A 295 2129 2662 1977 84 47 51 A O ATOM 2279 OD2 ASP A 295 -17.469 -17.939 7.550 1.00 18.59 A O ANISOU 2279 OD2 ASP A 295 2201 2711 2152 49 7 131 A O ATOM 2280 N VAL A 296 -19.833 -19.001 12.255 1.00 14.70 A N ANISOU 2280 N VAL A 296 1694 2461 1432 81 204 282 A N ATOM 2281 CA VAL A 296 -20.847 -19.702 13.038 1.00 17.49 A C ANISOU 2281 CA VAL A 296 2015 2864 1766 77 271 364 A C ATOM 2282 C VAL A 296 -21.233 -18.877 14.253 1.00 19.23 A C ANISOU 2282 C VAL A 296 2259 3172 1875 111 344 327 A C ATOM 2283 O VAL A 296 -22.416 -18.724 14.569 1.00 21.12 A O ANISOU 2283 O VAL A 296 2459 3444 2123 129 426 349 A O ATOM 2284 CB VAL A 296 -20.342 -21.100 13.435 1.00 15.64 A C ANISOU 2284 CB VAL A 296 1786 2633 1524 51 246 466 A C ATOM 2285 CG1 VAL A 296 -21.283 -21.746 14.427 1.00 16.08 A C ANISOU 2285 CG1 VAL A 296 1813 2752 1543 45 319 560 A C ATOM 2286 CG2 VAL A 296 -20.149 -21.977 12.189 1.00 14.84 A C ANISOU 2286 CG2 VAL A 296 1666 2428 1544 20 195 491 A C ATOM 2287 N VAL A 297 -20.248 -18.312 14.941 1.00 19.66 A N ANISOU 2287 N VAL A 297 2377 3268 1823 117 317 268 A N ATOM 2288 CA VAL A 297 -20.560 -17.470 16.087 1.00 23.73 A C ANISOU 2288 CA VAL A 297 2935 3865 2217 143 387 208 A C ATOM 2289 C VAL A 297 -21.312 -16.214 15.642 1.00 25.89 A C ANISOU 2289 C VAL A 297 3201 4092 2545 183 445 114 A C ATOM 2290 O VAL A 297 -22.229 -15.759 16.333 1.00 27.09 A O ANISOU 2290 O VAL A 297 3350 4289 2654 219 547 94 A O ATOM 2291 CB VAL A 297 -19.271 -17.133 16.858 1.00 22.28 A C ANISOU 2291 CB VAL A 297 2824 3736 1903 125 326 157 A C ATOM 2292 CG1 VAL A 297 -19.541 -16.094 17.931 1.00 22.45 A C ANISOU 2292 CG1 VAL A 297 2911 3814 1807 141 390 57 A C ATOM 2293 CG2 VAL A 297 -18.645 -18.402 17.452 1.00 23.45 A C ANISOU 2293 CG2 VAL A 297 2969 3941 1999 98 278 275 A C ATOM 2294 N ARG A 298 -20.957 -15.649 14.474 1.00 24.31 A N ANISOU 2294 N ARG A 298 2992 3800 2444 181 389 63 A N ATOM 2295 CA ARG A 298 -21.663 -14.469 13.959 1.00 28.63 A C ANISOU 2295 CA ARG A 298 3523 4292 3063 224 439 -5 A C ATOM 2296 C ARG A 298 -23.140 -14.751 13.774 1.00 30.37 A C ANISOU 2296 C ARG A 298 3658 4522 3359 253 518 66 A C ATOM 2297 O ARG A 298 -23.988 -13.928 14.138 1.00 34.95 A O ANISOU 2297 O ARG A 298 4226 5110 3945 307 613 29 A O ATOM 2298 CB ARG A 298 -21.045 -13.965 12.631 1.00 27.67 A C ANISOU 2298 CB ARG A 298 3396 4076 3039 212 360 -40 A C ATOM 2299 CG ARG A 298 -22.012 -13.101 11.695 1.00 32.32 A C ANISOU 2299 CG ARG A 298 3932 4600 3749 254 397 -50 A C ATOM 2300 CD ARG A 298 -21.310 -12.292 10.506 1.00 30.29 A C ANISOU 2300 CD ARG A 298 3688 4255 3568 246 329 -93 A C ATOM 2301 NE ARG A 298 -20.968 -12.886 9.199 1.00 32.15 A N ANISOU 2301 NE ARG A 298 3887 4455 3872 209 246 -40 A N ATOM 2302 CZ ARG A 298 -21.540 -12.589 8.019 1.00 25.54 A C ANISOU 2302 CZ ARG A 298 2997 3576 3130 217 230 -7 A C ATOM 2303 NH1 ARG A 298 -22.541 -11.691 7.915 1.00 20.47 A N ANISOU 2303 NH1 ARG A 298 2313 2914 2549 270 289 -5 A N ATOM 2304 NH2 ARG A 298 -21.082 -13.172 6.910 1.00 23.66 A N ANISOU 2304 NH2 ARG A 298 2747 3318 2925 176 156 26 A N ATOM 2305 N GLN A 299 -23.468 -15.919 13.236 1.00 28.74 A N ANISOU 2305 N GLN A 299 3390 4314 3215 215 484 168 A N ATOM 2306 CA GLN A 299 -24.835 -16.211 12.845 1.00 29.73 A C ANISOU 2306 CA GLN A 299 3418 4443 3433 224 535 243 A C ATOM 2307 C GLN A 299 -25.615 -16.863 13.968 1.00 28.51 A C ANISOU 2307 C GLN A 299 3234 4375 3222 228 625 316 A C ATOM 2308 O GLN A 299 -26.798 -16.564 14.153 1.00 34.35 A O ANISOU 2308 O GLN A 299 3904 5145 4002 265 715 347 A O ATOM 2309 CB GLN A 299 -24.841 -17.110 11.611 1.00 28.39 A C ANISOU 2309 CB GLN A 299 3201 4221 3363 166 448 305 A C ATOM 2310 CG GLN A 299 -26.081 -16.979 10.812 1.00 22.86 A C ANISOU 2310 CG GLN A 299 2401 3510 2774 169 463 353 A C ATOM 2311 CD GLN A 299 -26.043 -17.806 9.571 1.00 20.95 A C ANISOU 2311 CD GLN A 299 2129 3221 2611 100 370 395 A C ATOM 2312 NE2 GLN A 299 -24.866 -17.890 8.928 1.00 17.40 A N ANISOU 2312 NE2 GLN A 299 1747 2718 2146 78 290 344 A N ATOM 2313 OE1 GLN A 299 -27.052 -18.392 9.193 1.00 20.24 A O ANISOU 2313 OE1 GLN A 299 1954 3143 2592 63 370 469 A O ATOM 2314 N CYS A 300 -24.982 -17.745 14.734 1.00 29.47 A N ANISOU 2314 N CYS A 300 3401 4541 3253 194 607 358 A N ATOM 2315 CA CYS A 300 -25.609 -18.329 15.906 1.00 29.71 A C ANISOU 2315 CA CYS A 300 3422 4649 3219 194 685 426 A C ATOM 2316 C CYS A 300 -25.449 -17.443 17.153 1.00 36.65 A C ANISOU 2316 C CYS A 300 4381 5575 3967 233 746 335 A C ATOM 2317 O CYS A 300 -25.487 -17.962 18.278 1.00 43.02 A O ANISOU 2317 O CYS A 300 5221 6439 4687 217 773 372 A O ATOM 2318 CB CYS A 300 -25.056 -19.743 16.150 1.00 27.22 A C ANISOU 2318 CB CYS A 300 3118 4341 2885 137 628 526 A C ATOM 2319 SG CYS A 300 -25.099 -20.889 14.689 1.00 28.00 A S ANISOU 2319 SG CYS A 300 3151 4346 3140 71 545 608 A S ATOM 2320 N SER A 301 -25.265 -16.120 16.965 1.00 38.15 A N ANISOU 2320 N SER A 301 4609 5738 4148 278 767 216 A N ATOM 2321 CA SER A 301 -25.264 -15.133 18.050 1.00 41.43 A C ANISOU 2321 CA SER A 301 5106 6175 4459 309 836 108 A C ATOM 2322 C SER A 301 -25.823 -13.770 17.620 1.00 43.16 A C ANISOU 2322 C SER A 301 5316 6330 4754 371 901 12 A C ATOM 2323 O SER A 301 -26.616 -13.171 18.355 1.00 41.48 A O ANISOU 2323 O SER A 301 5111 6125 4525 406 1003 -32 A O ATOM 2324 CB SER A 301 -23.857 -14.954 18.631 1.00 43.99 A C ANISOU 2324 CB SER A 301 5540 6525 4649 275 764 37 A C ATOM 2325 OG SER A 301 -23.844 -13.943 19.627 1.00 49.27 A O ANISOU 2325 OG SER A 301 6298 7204 5220 290 827 -80 A O ATOM 2326 N GLY A 302 -25.403 -13.246 16.464 1.00 44.40 A N ANISOU 2326 N GLY A 302 5457 6420 4992 387 846 -21 A N ATOM 2327 CA GLY A 302 -26.132 -12.143 15.848 1.00 45.87 A C ANISOU 2327 CA GLY A 302 5604 6531 5296 450 901 -66 A C ATOM 2328 C GLY A 302 -25.505 -10.759 15.775 1.00 51.62 A C ANISOU 2328 C GLY A 302 6415 7182 6017 485 907 -207 A C ATOM 2329 O GLY A 302 -26.181 -9.762 16.056 1.00 50.29 A O ANISOU 2329 O GLY A 302 6250 6965 5892 536 993 -271 A O ATOM 2330 N VAL A 303 -24.240 -10.665 15.357 1.00 51.90 A N ANISOU 2330 N VAL A 303 6512 7187 6022 441 801 -254 A N ATOM 2331 CA VAL A 303 -23.544 -9.380 15.337 1.00 54.32 A C ANISOU 2331 CA VAL A 303 6906 7409 6325 451 792 -388 A C ATOM 2332 C VAL A 303 -23.920 -8.606 14.074 1.00 52.20 A C ANISOU 2332 C VAL A 303 6580 7025 6230 491 782 -375 A C ATOM 2333 O VAL A 303 -24.265 -9.192 13.040 1.00 47.83 A O ANISOU 2333 O VAL A 303 5934 6464 5776 480 728 -268 A O ATOM 2334 CB VAL A 303 -22.020 -9.593 15.444 1.00 53.42 A C ANISOU 2334 CB VAL A 303 6869 7306 6123 367 667 -432 A C ATOM 2335 CG1 VAL A 303 -21.298 -8.263 15.652 1.00 56.75 A C ANISOU 2335 CG1 VAL A 303 7389 7650 6524 361 662 -580 A C ATOM 2336 CG2 VAL A 303 -21.697 -10.578 16.566 1.00 51.38 A C ANISOU 2336 CG2 VAL A 303 6643 7176 5704 327 658 -399 A C ATOM 2337 N THR A 304 -23.860 -7.272 14.162 1.00 49.89 A N ANISOU 2337 N THR A 304 6345 6640 5970 535 835 -484 A N ATOM 2338 CA THR A 304 -24.240 -6.356 13.089 1.00 45.84 A C ANISOU 2338 CA THR A 304 5785 6010 5622 585 841 -469 A C ATOM 2339 C THR A 304 -23.082 -5.407 12.799 1.00 53.57 A C ANISOU 2339 C THR A 304 6855 6886 6614 546 776 -569 A C ATOM 2340 O THR A 304 -22.010 -5.488 13.412 1.00 55.83 A O ANISOU 2340 O THR A 304 7230 7199 6783 476 720 -648 A O ATOM 2341 CB THR A 304 -25.495 -5.547 13.448 1.00 42.29 A C ANISOU 2341 CB THR A 304 5295 5526 5246 675 963 -482 A C ATOM 2342 CG2 THR A 304 -26.704 -6.446 13.521 1.00 33.44 A C ANISOU 2342 CG2 THR A 304 4057 4497 4150 693 1001 -361 A C ATOM 2343 OG1 THR A 304 -25.313 -4.922 14.725 1.00 50.12 A O ANISOU 2343 OG1 THR A 304 6388 6524 6132 675 1018 -617 A O ATOM 2344 N PHE A 305 -23.312 -4.485 11.858 1.00 51.50 A N ANISOU 2344 N PHE A 305 6562 6508 6499 589 781 -554 A N ATOM 2345 CA PHE A 305 -22.245 -3.644 11.326 1.00 56.40 A C ANISOU 2345 CA PHE A 305 7246 7024 7162 544 710 -614 A C ATOM 2346 C PHE A 305 -22.793 -2.270 10.970 1.00 55.78 A C ANISOU 2346 C PHE A 305 7169 6798 7225 626 791 -644 A C ATOM 2347 O PHE A 305 -23.880 -2.152 10.397 1.00 52.26 A O ANISOU 2347 O PHE A 305 6625 6343 6888 700 830 -542 A O ATOM 2348 CB PHE A 305 -21.590 -4.309 10.104 1.00 51.36 A C ANISOU 2348 CB PHE A 305 6549 6404 6560 480 576 -512 A C ATOM 2349 CG PHE A 305 -21.368 -5.773 10.298 1.00 49.54 A C ANISOU 2349 CG PHE A 305 6291 6304 6230 426 516 -453 A C ATOM 2350 CD1 PHE A 305 -20.209 -6.228 10.905 1.00 46.17 A C ANISOU 2350 CD1 PHE A 305 5930 5927 5684 351 450 -505 A C ATOM 2351 CD2 PHE A 305 -22.341 -6.695 9.926 1.00 45.04 A C ANISOU 2351 CD2 PHE A 305 5624 5801 5689 450 527 -340 A C ATOM 2352 CE1 PHE A 305 -20.019 -7.572 11.129 1.00 47.62 A C ANISOU 2352 CE1 PHE A 305 6087 6217 5788 311 404 -441 A C ATOM 2353 CE2 PHE A 305 -22.154 -8.042 10.145 1.00 44.10 A C ANISOU 2353 CE2 PHE A 305 5486 5781 5490 399 480 -287 A C ATOM 2354 CZ PHE A 305 -20.998 -8.483 10.755 1.00 46.64 A C ANISOU 2354 CZ PHE A 305 5878 6143 5701 336 424 -335 A C ATOM 2355 N GLN A 306 -22.029 -1.238 11.318 1.00 57.48 A N ANISOU 2355 N GLN A 306 7489 6916 7434 596 783 -761 A N ATOM 2356 CA GLN A 306 -22.442 0.144 11.096 1.00 60.16 A C ANISOU 2356 CA GLN A 306 7842 7121 7895 653 823 -778 A C ATOM 2357 C GLN A 306 -21.313 0.967 10.487 1.00 54.69 A C ANISOU 2357 C GLN A 306 7209 6305 7265 590 753 -817 A C ATOM 2358 O GLN A 306 -21.252 1.151 9.274 1.00 51.64 A O ANISOU 2358 O GLN A 306 6761 5859 7002 598 715 -720 A O ATOM 2359 CB GLN A 306 -22.901 0.783 12.407 1.00 62.10 A C ANISOU 2359 CB GLN A 306 8161 7363 8072 691 905 -890 A C ATOM 2360 CG GLN A 306 -24.170 0.191 12.980 1.00 58.80 A C ANISOU 2360 CG GLN A 306 7669 7051 7620 763 990 -842 A C ATOM 2361 CD GLN A 306 -25.025 1.228 13.680 1.00 62.86 A C ANISOU 2361 CD GLN A 306 8209 7505 8171 845 1093 -906 A C ATOM 2362 NE2 GLN A 306 -25.512 2.212 12.925 1.00 62.10 A N ANISOU 2362 NE2 GLN A 306 8076 7284 8234 906 1118 -858 A N ATOM 2363 OE1 GLN A 306 -25.247 1.146 14.890 1.00 66.95 A O ANISOU 2363 OE1 GLN A 306 8778 8090 8570 854 1152 -994 A O TER HETATM 2364 C1 A1AQA 401 -10.486 -18.505 -18.862 1.00 24.25 B C ANISOU 2364 C1 A1AQA 401 3594 3735 1885 -310 137 -274 B C HETATM 2365 C3 A1AQA 401 -11.927 -18.378 -19.296 1.00 25.06 B C ANISOU 2365 C3 A1AQA 401 3692 3876 1953 -380 10 -250 B C HETATM 2366 O3 A1AQA 401 -6.473 -14.261 -18.420 1.00 26.89 B O ANISOU 2366 O3 A1AQA 401 3633 4177 2408 -148 360 138 B O HETATM 2367 C4 A1AQA 401 -12.850 -19.325 -18.873 1.00 25.17 B C ANISOU 2367 C4 A1AQA 401 3727 3833 2003 -424 -49 -322 B C HETATM 2368 C5 A1AQA 401 -14.176 -19.209 -19.278 1.00 25.66 B C ANISOU 2368 C5 A1AQA 401 3768 3937 2043 -489 -160 -291 B C HETATM 2369 C6 A1AQA 401 -14.577 -18.155 -20.094 1.00 25.54 B C ANISOU 2369 C6 A1AQA 401 3715 4017 1972 -504 -214 -190 B C HETATM 2370 C7 A1AQA 401 -13.650 -17.208 -20.520 1.00 26.60 B C ANISOU 2370 C7 A1AQA 401 3837 4200 2070 -459 -157 -118 B C HETATM 2371 C8 A1AQA 401 -12.548 -10.802 -16.680 1.00 18.83 B C ANISOU 2371 C8 A1AQA 401 2421 3125 1606 -263 -183 460 B C HETATM 2372 C9 A1AQA 401 -12.326 -17.322 -20.115 1.00 26.84 B C ANISOU 2372 C9 A1AQA 401 3885 4191 2122 -400 -45 -148 B C HETATM 2373 O9 A1AQA 401 -13.822 -10.168 -16.613 1.00 17.95 B O ANISOU 2373 O9 A1AQA 401 2260 3007 1554 -265 -264 526 B O HETATM 2374 C10 A1AQA 401 -5.102 -13.939 -18.638 1.00 27.91 B C ANISOU 2374 C10 A1AQA 401 3716 4324 2566 -106 469 185 B C HETATM 2375 C11 A1AQA 401 -4.340 -14.538 -17.468 1.00 25.68 B C ANISOU 2375 C11 A1AQA 401 3383 3946 2427 -48 508 138 B C HETATM 2376 O11 A1AQA 401 -9.812 -17.286 -19.160 1.00 23.63 B O ANISOU 2376 O11 A1AQA 401 3462 3722 1793 -282 168 -164 B O HETATM 2377 C12 A1AQA 401 -9.920 -16.137 -18.295 1.00 23.36 B C ANISOU 2377 C12 A1AQA 401 3331 3699 1847 -276 122 -50 B C HETATM 2378 C13 A1AQA 401 -8.276 -14.967 -19.764 1.00 24.77 B C ANISOU 2378 C13 A1AQA 401 3495 3972 1944 -232 251 62 B C HETATM 2379 N13 A1AQA 401 -9.236 -15.058 -18.663 1.00 24.43 B N ANISOU 2379 N13 A1AQA 401 3420 3883 1980 -254 157 52 B N HETATM 2380 C14 A1AQA 401 -9.403 -13.804 -17.946 1.00 21.61 B C ANISOU 2380 C14 A1AQA 401 2968 3510 1735 -242 103 171 B C HETATM 2381 C15 A1AQA 401 -10.811 -13.306 -18.075 1.00 21.17 B C ANISOU 2381 C15 A1AQA 401 2894 3482 1667 -285 -16 227 B C HETATM 2382 C16 A1AQA 401 -7.422 -13.784 -19.359 1.00 27.74 B C ANISOU 2382 C16 A1AQA 401 3778 4360 2403 -203 288 183 B C HETATM 2383 N16 A1AQA 401 -11.347 -12.842 -16.966 1.00 20.48 B N ANISOU 2383 N16 A1AQA 401 2743 3334 1705 -269 -72 263 B N HETATM 2384 C17 A1AQA 401 -12.680 -12.287 -16.993 1.00 20.22 B C ANISOU 2384 C17 A1AQA 401 2673 3322 1688 -295 -174 330 B C HETATM 2385 C18 A1AQA 401 -4.914 -12.425 -18.698 1.00 28.21 B C ANISOU 2385 C18 A1AQA 401 3675 4389 2656 -125 439 332 B C HETATM 2386 C19 A1AQA 401 -13.567 -13.056 -16.002 1.00 16.82 B C ANISOU 2386 C19 A1AQA 401 2235 2841 1315 -304 -225 262 B C HETATM 2387 C20 A1AQA 401 -13.569 -14.528 -16.396 1.00 17.22 B C ANISOU 2387 C20 A1AQA 401 2368 2892 1282 -340 -204 134 B C HETATM 2388 C21 A1AQA 401 -14.341 -14.781 -17.686 1.00 22.16 B C ANISOU 2388 C21 A1AQA 401 3030 3574 1817 -388 -250 126 B C HETATM 2389 C22 A1AQA 401 -15.163 -16.047 -17.418 1.00 21.82 B C ANISOU 2389 C22 A1AQA 401 3020 3493 1776 -430 -287 27 B C HETATM 2390 C23 A1AQA 401 -4.592 -14.582 -19.921 1.00 30.23 B C ANISOU 2390 C23 A1AQA 401 4091 4676 2719 -98 573 131 B C HETATM 2391 N23 A1AQA 401 -15.155 -16.207 -15.979 1.00 20.60 B N ANISOU 2391 N23 A1AQA 401 2829 3270 1729 -405 -283 15 B N HETATM 2392 C24 A1AQA 401 -14.292 -15.377 -15.386 1.00 18.28 B C ANISOU 2392 C24 A1AQA 401 2497 2966 1481 -353 -241 69 B C HETATM 2393 O26 A1AQA 401 -14.089 -15.311 -14.190 1.00 15.57 B O ANISOU 2393 O26 A1AQA 401 2112 2545 1260 -306 -221 66 B O HETATM 2394 O33 A1AQA 401 -10.608 -16.199 -17.283 1.00 20.57 B O ANISOU 2394 O33 A1AQA 401 2939 3291 1585 -281 56 -50 B O HETATM 2395 C34 A1AQA 401 -8.422 -12.883 -18.658 1.00 26.03 B C ANISOU 2395 C34 A1AQA 401 3499 4126 2266 -227 171 267 B C HETATM 2396 O38 A1AQA 401 -11.412 -13.356 -19.144 1.00 25.36 B O ANISOU 2396 O38 A1AQA 401 3460 4060 2116 -316 -54 230 B O HETATM 2397 O HOH A 501 -7.656 5.892 -0.060 1.00 25.44 C O HETATM 2398 O HOH A 502 -18.926 -13.376 -8.381 1.00 34.10 C O HETATM 2399 O HOH A 503 -3.497 -24.282 -6.478 1.00 19.17 C O HETATM 2400 O HOH A 504 -13.663 -22.272 -16.977 1.00 24.30 C O HETATM 2401 O HOH A 505 -7.335 -6.533 9.988 1.00 28.36 C O HETATM 2402 O HOH A 506 -16.550 -7.862 13.692 1.00 38.73 C O HETATM 2403 O HOH A 507 -1.982 -3.277 -24.583 1.00 36.88 C O HETATM 2404 O HOH A 508 -26.853 -4.559 16.294 1.00 36.18 C O HETATM 2405 O HOH A 509 -24.713 -2.384 8.298 1.00 35.31 C O HETATM 2406 O HOH A 510 3.080 -10.273 -6.200 1.00 17.22 C O HETATM 2407 O HOH A 511 -4.349 -36.685 3.114 1.00 32.86 C O HETATM 2408 O HOH A 512 -5.117 -24.295 4.167 1.00 23.92 C O HETATM 2409 O HOH A 513 0.334 1.093 -2.854 1.00 31.42 C O HETATM 2410 O HOH A 514 -19.508 -24.186 0.138 1.00 27.88 C O HETATM 2411 O HOH A 515 -2.377 8.216 -5.866 1.00 34.45 C O HETATM 2412 O HOH A 516 -0.342 -14.243 -21.672 1.00 41.12 C O HETATM 2413 O HOH A 517 -29.759 -19.414 1.289 1.00 39.25 C O HETATM 2414 O HOH A 518 -4.287 -26.943 -17.778 1.00 33.68 C O HETATM 2415 O HOH A 519 -12.901 -4.847 8.524 1.00 23.53 C O HETATM 2416 O HOH A 520 -16.086 -34.695 3.616 1.00 23.61 C O HETATM 2417 O HOH A 521 -29.548 -19.392 13.998 1.00 29.64 C O HETATM 2418 O HOH A 522 -19.139 -20.509 0.638 1.00 22.37 C O HETATM 2419 O HOH A 523 -3.351 -21.696 20.349 1.00 26.49 C O HETATM 2420 O HOH A 524 -8.515 -25.616 24.033 1.00 32.13 C O HETATM 2421 O HOH A 525 2.298 -17.457 -25.681 1.00 44.51 C O HETATM 2422 O HOH A 526 -17.789 -37.506 26.085 1.00 36.97 C O HETATM 2423 O HOH A 527 -7.201 13.611 -7.088 1.00 29.03 C O HETATM 2424 O HOH A 528 -4.249 -34.072 7.005 1.00 27.39 C O HETATM 2425 O HOH A 529 -1.769 -34.612 16.205 1.00 34.89 C O HETATM 2426 O HOH A 530 -12.640 8.614 -17.916 1.00 30.09 C O HETATM 2427 O HOH A 531 -11.565 -45.409 6.822 1.00 38.83 C O HETATM 2428 O HOH A 532 -10.131 9.193 -18.686 1.00 28.78 C O HETATM 2429 O HOH A 533 -18.315 -33.646 25.543 1.00 27.89 C O HETATM 2430 O HOH A 534 -11.140 -33.323 0.851 1.00 24.33 C O HETATM 2431 O HOH A 535 -7.452 -24.050 5.433 1.00 24.16 C O HETATM 2432 O HOH A 536 -17.349 -5.880 -6.406 1.00 13.28 C O HETATM 2433 O HOH A 537 -3.268 -36.858 20.691 1.00 33.68 C O HETATM 2434 O HOH A 538 -1.406 6.023 -25.676 1.00 42.84 C O HETATM 2435 O HOH A 539 -19.852 -25.054 2.731 1.00 20.84 C O HETATM 2436 O HOH A 540 -16.847 -13.785 6.038 1.00 18.65 C O HETATM 2437 O HOH A 541 -2.442 -27.925 -4.229 1.00 29.27 C O HETATM 2438 O HOH A 542 -3.830 -22.420 -22.001 1.00 35.72 C O HETATM 2439 O HOH A 543 -18.702 -13.722 8.292 1.00 36.74 C O HETATM 2440 O HOH A 544 -15.593 14.100 -3.845 1.00 34.30 C O HETATM 2441 O HOH A 545 -3.751 -41.836 7.931 1.00 32.26 C O HETATM 2442 O HOH A 546 1.313 7.792 -20.310 1.00 29.92 C O HETATM 2443 O HOH A 547 -1.741 5.772 -10.029 1.00 22.53 C O HETATM 2444 O HOH A 548 -10.997 -21.485 9.074 1.00 17.91 C O HETATM 2445 O HOH A 549 -25.378 -22.910 25.806 1.00 34.94 C O HETATM 2446 O HOH A 550 -29.536 -24.543 6.883 1.00 29.95 C O HETATM 2447 O HOH A 551 -18.000 -25.260 7.372 1.00 9.37 C O HETATM 2448 O HOH A 552 -5.521 -1.054 -25.062 1.00 27.55 C O HETATM 2449 O HOH A 553 -20.020 -36.347 19.847 1.00 27.21 C O HETATM 2450 O HOH A 554 -21.872 -13.308 -11.349 1.00 20.57 C O HETATM 2451 O HOH A 555 -19.853 3.318 -0.001 1.00 22.04 C O HETATM 2452 O HOH A 556 -10.442 -44.269 8.999 1.00 31.95 C O HETATM 2453 O HOH A 557 -3.553 -23.757 13.151 1.00 21.80 C O HETATM 2454 O HOH A 558 3.467 -11.575 -18.353 1.00 32.89 C O HETATM 2455 O HOH A 559 -28.833 -29.281 20.319 1.00 23.88 C O HETATM 2456 O HOH A 560 -32.337 -29.111 13.927 1.00 30.10 C O HETATM 2457 O HOH A 561 -3.319 -24.418 23.585 1.00 30.83 C O HETATM 2458 O HOH A 562 -11.249 -13.961 -21.701 1.00 29.86 C O HETATM 2459 O HOH A 563 -9.061 1.741 8.093 1.00 28.04 C O HETATM 2460 O HOH A 564 4.683 -14.595 -14.902 1.00 30.31 C O HETATM 2461 O HOH A 565 2.144 5.370 -19.579 1.00 27.08 C O HETATM 2462 O HOH A 566 -30.858 -40.396 13.234 1.00 46.39 C O HETATM 2463 O HOH A 567 -17.444 -8.531 11.488 1.00 35.93 C O HETATM 2464 O HOH A 568 -29.151 -16.419 12.935 1.00 24.53 C O HETATM 2465 O HOH A 569 -0.262 -1.171 -24.422 1.00 29.40 C O HETATM 2466 O HOH A 570 -23.381 -0.205 -15.809 1.00 35.44 C O HETATM 2467 O HOH A 571 -1.933 -24.810 -8.986 1.00 23.85 C O HETATM 2468 O HOH A 572 -9.521 -6.808 8.847 1.00 27.61 C O HETATM 2469 O HOH A 573 -15.836 2.550 -18.820 1.00 24.30 C O HETATM 2470 O HOH A 574 3.555 -4.838 -11.831 1.00 24.60 C O HETATM 2471 O HOH A 575 -21.211 -11.598 -18.879 1.00 27.02 C O HETATM 2472 O HOH A 576 -12.549 -18.601 18.990 1.00 33.45 C O HETATM 2473 O HOH A 577 -6.476 -17.075 -6.658 1.00 10.56 C O HETATM 2474 O HOH A 578 -29.009 -24.361 20.912 1.00 34.65 C O HETATM 2475 O HOH A 579 -20.878 -39.238 14.080 1.00 25.77 C O HETATM 2476 O HOH A 580 -13.482 1.109 12.555 1.00 38.16 C O HETATM 2477 O HOH A 581 -11.402 -27.094 -4.814 1.00 21.72 C O HETATM 2478 O HOH A 582 -8.762 2.958 -24.802 1.00 33.02 C O HETATM 2479 O HOH A 583 -24.629 -26.502 3.276 1.00 30.42 C O HETATM 2480 O HOH A 584 -10.767 -26.891 -9.088 1.00 17.47 C O HETATM 2481 O HOH A 585 -1.938 -24.547 -1.359 1.00 21.93 C O HETATM 2482 O HOH A 586 -15.566 -21.288 18.802 1.00 23.92 C O HETATM 2483 O HOH A 587 -14.821 -21.090 -2.450 1.00 12.92 C O HETATM 2484 O HOH A 588 -19.851 7.694 -5.245 1.00 25.71 C O HETATM 2485 O HOH A 589 -8.658 -8.484 -20.244 1.00 32.25 C O HETATM 2486 O HOH A 590 -17.320 3.246 6.885 1.00 28.81 C O HETATM 2487 O HOH A 591 -6.763 2.160 5.622 1.00 31.68 C O HETATM 2488 O HOH A 592 -4.851 -21.450 13.530 1.00 27.70 C O HETATM 2489 O HOH A 593 -23.966 -29.120 -0.275 1.00 29.43 C O HETATM 2490 O HOH A 594 -12.912 -14.568 7.180 1.00 18.64 C O HETATM 2491 O HOH A 595 -0.000 -8.492 0.000 0.50 16.21 C O HETATM 2492 O HOH A 596 -6.338 -19.858 19.904 1.00 31.42 C O HETATM 2493 O HOH A 597 -23.738 -43.658 4.681 1.00 34.17 C O HETATM 2494 O HOH A 598 -5.363 -22.152 -17.649 1.00 25.82 C O HETATM 2495 O HOH A 599 -7.082 -15.971 9.226 1.00 32.86 C O HETATM 2496 O HOH A 600 0.577 -20.200 -12.913 1.00 21.48 C O HETATM 2497 O HOH A 601 -3.816 -34.785 9.717 1.00 27.32 C O HETATM 2498 O HOH A 602 -19.903 -25.908 28.706 1.00 35.65 C O HETATM 2499 O HOH A 603 -2.234 14.368 -15.391 1.00 38.85 C O HETATM 2500 O HOH A 604 -13.124 -29.630 24.436 1.00 33.86 C O HETATM 2501 O HOH A 605 -6.211 -6.838 0.063 1.00 15.06 C O HETATM 2502 O HOH A 606 4.083 -9.954 -12.749 1.00 49.17 C O HETATM 2503 O HOH A 607 -7.040 -25.543 8.535 1.00 31.90 C O HETATM 2504 O HOH A 608 -7.399 -3.649 -23.676 1.00 35.44 C O HETATM 2505 O HOH A 609 -24.910 -37.939 1.403 1.00 34.93 C O HETATM 2506 O HOH A 610 -15.302 -46.737 5.606 1.00 34.94 C O HETATM 2507 O HOH A 611 1.292 -21.160 -15.350 1.00 24.07 C O HETATM 2508 O HOH A 612 -32.870 -18.402 17.961 1.00 23.65 C O HETATM 2509 O HOH A 613 -16.409 -22.119 -9.205 1.00 17.00 C O HETATM 2510 O HOH A 614 -10.083 -25.611 -6.755 1.00 16.24 C O HETATM 2511 O HOH A 615 -17.528 -31.826 1.436 1.00 33.36 C O HETATM 2512 O HOH A 616 5.283 1.283 -17.628 1.00 28.53 C O HETATM 2513 O HOH A 617 -28.641 -2.356 -3.412 1.00 18.79 C O HETATM 2514 O HOH A 618 -31.012 -31.065 7.836 1.00 24.97 C O HETATM 2515 O HOH A 619 -8.266 -25.810 -12.823 1.00 21.90 C O HETATM 2516 O HOH A 620 -15.028 -32.978 1.684 1.00 26.89 C O HETATM 2517 O HOH A 621 -1.650 -38.035 13.764 1.00 33.09 C O HETATM 2518 O HOH A 622 -11.087 -25.496 23.146 1.00 26.76 C O HETATM 2519 O HOH A 623 -19.365 -18.125 5.514 1.00 18.77 C O HETATM 2520 O HOH A 624 -12.864 -37.265 1.693 1.00 25.94 C O HETATM 2521 O HOH A 625 -2.439 -30.764 21.431 1.00 37.13 C O HETATM 2522 O HOH A 626 -15.044 -41.758 16.504 1.00 30.54 C O HETATM 2523 O HOH A 627 -9.568 -21.724 -17.538 1.00 25.14 C O HETATM 2524 O HOH A 628 -7.159 -18.743 -16.450 1.00 32.97 C O HETATM 2525 O HOH A 629 -7.784 -20.064 7.902 1.00 23.71 C O HETATM 2526 O HOH A 630 -28.855 -25.718 3.970 1.00 34.04 C O HETATM 2527 O HOH A 631 -15.989 -28.418 0.346 1.00 28.61 C O HETATM 2528 O HOH A 632 1.112 -12.656 -12.660 1.00 17.09 C O HETATM 2529 O HOH A 633 -17.778 -5.354 -17.040 1.00 21.41 C O HETATM 2530 O HOH A 634 -14.779 -15.489 9.082 1.00 21.53 C O HETATM 2531 O HOH A 635 -10.097 -21.556 23.838 1.00 36.92 C O HETATM 2532 O HOH A 636 -13.633 -8.264 -18.681 1.00 21.75 C O HETATM 2533 O HOH A 637 -14.739 7.493 5.033 1.00 34.15 C O HETATM 2534 O HOH A 638 -2.369 -15.332 2.440 1.00 11.29 C O HETATM 2535 O HOH A 639 -1.165 -19.635 3.970 1.00 12.27 C O HETATM 2536 O HOH A 640 -12.038 -29.345 -1.956 1.00 23.74 C O HETATM 2537 O HOH A 641 -25.857 -17.103 20.937 1.00 38.34 C O HETATM 2538 O HOH A 642 1.108 -11.906 -8.086 1.00 13.73 C O HETATM 2539 O HOH A 643 -17.208 -6.462 -20.200 1.00 29.57 C O HETATM 2540 O HOH A 644 -31.055 -23.909 9.342 1.00 26.35 C O HETATM 2541 O HOH A 645 -23.716 -16.889 -0.248 1.00 19.61 C O HETATM 2542 O HOH A 646 2.457 -17.197 -20.931 1.00 33.40 C O HETATM 2543 O HOH A 647 -7.361 4.661 -2.400 1.00 22.35 C O HETATM 2544 O HOH A 648 -16.135 -39.913 3.643 1.00 29.50 C O HETATM 2545 O HOH A 649 -19.205 -6.385 -19.129 1.00 31.91 C O HETATM 2546 O HOH A 650 -23.761 -39.853 3.290 1.00 39.09 C O HETATM 2547 O HOH A 651 -18.134 -14.248 15.331 1.00 31.35 C O HETATM 2548 O HOH A 652 -26.072 -29.140 23.376 1.00 32.36 C O HETATM 2549 O HOH A 653 -22.112 0.791 -8.211 1.00 34.49 C O HETATM 2550 O HOH A 654 -18.757 -39.179 4.603 1.00 32.01 C O HETATM 2551 O HOH A 655 -3.000 -23.933 1.956 1.00 21.06 C O HETATM 2552 O HOH A 656 -2.448 -5.341 2.249 1.00 15.89 C O HETATM 2553 O HOH A 657 -20.720 2.494 -11.716 1.00 25.56 C O HETATM 2554 O HOH A 658 1.692 -20.639 -22.144 1.00 30.39 C O HETATM 2555 O HOH A 659 -5.830 9.149 -1.946 1.00 42.09 C O HETATM 2556 O HOH A 660 -25.078 -31.671 24.676 1.00 33.08 C O HETATM 2557 O HOH A 661 4.495 -7.376 -24.321 1.00 38.47 C O HETATM 2558 O HOH A 662 -25.571 -26.196 5.862 1.00 21.15 C O HETATM 2559 O HOH A 663 -0.055 -23.378 -10.621 1.00 22.83 C O HETATM 2560 O HOH A 664 5.648 -16.824 -13.509 1.00 28.82 C O HETATM 2561 O HOH A 665 -19.078 -19.866 24.793 1.00 32.39 C O HETATM 2562 O HOH A 666 -34.021 -25.473 14.649 1.00 31.34 C O HETATM 2563 O HOH A 667 -11.310 -9.559 4.372 1.00 16.21 C O HETATM 2564 O HOH A 668 -2.127 -9.455 -22.144 1.00 45.88 C O HETATM 2565 O HOH A 669 -11.059 -7.577 -24.901 1.00 38.01 C O HETATM 2566 O HOH A 670 -2.912 -1.198 -4.051 1.00 23.49 C O HETATM 2567 O HOH A 671 -5.528 -35.819 22.323 1.00 33.51 C O HETATM 2568 O HOH A 672 1.353 -23.758 -19.622 1.00 27.53 C O HETATM 2569 O HOH A 673 1.471 -13.367 -4.251 1.00 9.17 C O HETATM 2570 O HOH A 674 -4.384 -8.591 -14.248 1.00 15.23 C O HETATM 2571 O HOH A 675 2.036 -12.222 -16.133 1.00 23.65 C O HETATM 2572 O HOH A 676 4.571 -3.006 -9.160 1.00 23.12 C O HETATM 2573 O HOH A 677 -22.189 -2.158 6.191 1.00 29.99 C O HETATM 2574 O HOH A 678 -25.736 -1.150 -6.569 1.00 26.66 C O HETATM 2575 O HOH A 679 -22.191 -16.418 9.052 1.00 15.35 C O HETATM 2576 O HOH A 680 -9.421 -37.381 24.179 1.00 34.84 C O HETATM 2577 O HOH A 681 -20.065 -35.714 23.495 1.00 31.85 C O HETATM 2578 O HOH A 682 -25.099 -1.386 -16.118 1.00 37.74 C O HETATM 2579 O HOH A 683 1.391 -13.651 -10.182 1.00 13.86 C O HETATM 2580 O HOH A 684 -4.963 -0.935 4.416 1.00 21.46 C O HETATM 2581 O HOH A 685 -27.655 -14.254 12.495 1.00 36.37 C O HETATM 2582 O HOH A 686 -3.575 6.416 -27.510 1.00 35.75 C O HETATM 2583 O HOH A 687 3.894 2.014 -12.560 1.00 25.70 C O HETATM 2584 O HOH A 688 -10.146 4.200 5.914 1.00 21.93 C O HETATM 2585 O HOH A 689 0.590 8.772 -14.762 1.00 26.45 C O HETATM 2586 O HOH A 690 -14.999 -11.850 8.949 1.00 25.44 C O HETATM 2587 O HOH A 691 -18.721 6.713 3.395 1.00 34.70 C O HETATM 2588 O HOH A 692 -24.407 -12.597 -11.518 1.00 35.04 C O HETATM 2589 O HOH A 693 -12.832 -18.173 12.476 1.00 21.24 C O HETATM 2590 O HOH A 694 -18.795 -34.829 2.708 1.00 24.24 C O HETATM 2591 O HOH A 695 -31.509 -28.491 10.507 1.00 33.61 C O HETATM 2592 O HOH A 696 -31.447 -34.015 10.283 1.00 35.21 C O HETATM 2593 O HOH A 697 -0.698 -24.901 -12.952 1.00 23.54 C O HETATM 2594 O HOH A 698 -26.235 -12.127 13.266 1.00 50.68 C O HETATM 2595 O HOH A 699 -8.266 -27.418 9.686 1.00 19.04 C O HETATM 2596 O HOH A 700 1.362 -2.343 -26.897 1.00 30.07 C O HETATM 2597 O HOH A 701 -14.294 -24.890 25.802 1.00 29.86 C O HETATM 2598 O HOH A 702 -0.000 -16.625 0.000 0.50 10.64 C O HETATM 2599 O HOH A 703 -25.860 1.188 -2.879 1.00 35.38 C O HETATM 2600 O HOH A 704 -4.042 8.712 -3.459 1.00 35.25 C O HETATM 2601 O HOH A 705 -4.080 11.579 -21.555 1.00 29.28 C O HETATM 2602 O HOH A 706 -6.697 -31.312 21.636 1.00 28.44 C O HETATM 2603 O HOH A 707 -1.307 -24.945 17.248 1.00 22.37 C O HETATM 2604 O HOH A 708 -19.618 -22.098 -7.503 1.00 27.36 C O HETATM 2605 O HOH A 709 -18.709 -16.032 -19.392 1.00 26.22 C O HETATM 2606 O HOH A 710 -21.892 -17.192 6.304 1.00 12.98 C O HETATM 2607 O HOH A 711 -13.537 -29.985 -0.033 1.00 32.74 C O HETATM 2608 O HOH A 712 -4.332 -21.074 6.525 1.00 19.90 C O HETATM 2609 O HOH A 713 -11.403 -36.022 25.251 1.00 33.95 C O HETATM 2610 O HOH A 714 -25.226 -26.598 0.991 1.00 34.42 C O HETATM 2611 O HOH A 715 -2.929 -13.474 6.536 1.00 17.25 C O HETATM 2612 O HOH A 716 0.327 -17.282 -2.757 1.00 12.19 C O HETATM 2613 O HOH A 717 -31.071 -34.787 15.012 1.00 24.67 C O HETATM 2614 O HOH A 718 -25.708 -31.414 0.000 0.50 20.16 C O HETATM 2615 O HOH A 719 -11.869 6.205 4.349 1.00 26.12 C O HETATM 2616 O HOH A 720 -14.871 -6.620 -22.669 1.00 34.12 C O HETATM 2617 O HOH A 721 -4.466 -28.280 -0.697 1.00 22.07 C O HETATM 2618 O HOH A 722 4.749 -3.301 -6.736 1.00 21.11 C O HETATM 2619 O HOH A 723 -0.637 -27.869 17.111 1.00 23.90 C O HETATM 2620 O HOH A 724 -31.699 -36.311 8.815 1.00 31.91 C O HETATM 2621 O HOH A 725 -1.316 -30.023 -7.407 1.00 28.87 C O HETATM 2622 O HOH A 726 -4.502 -18.778 -18.327 1.00 28.59 C O HETATM 2623 O HOH A 727 -5.246 -13.463 8.119 1.00 24.39 C O HETATM 2624 O HOH A 728 2.415 -17.130 -9.292 1.00 19.53 C O HETATM 2625 O HOH A 729 -7.854 -28.496 24.422 1.00 29.35 C O HETATM 2626 O HOH A 730 -8.232 -3.929 -25.772 1.00 38.11 C O HETATM 2627 O HOH A 731 -32.321 -25.199 18.372 1.00 33.55 C O HETATM 2628 O HOH A 732 -22.686 -43.170 11.095 1.00 37.44 C O HETATM 2629 O HOH A 733 -27.828 -20.775 2.211 1.00 23.93 C O HETATM 2630 O HOH A 734 -17.544 -8.504 -21.473 1.00 38.45 C O HETATM 2631 O HOH A 735 -15.224 -25.253 -16.321 1.00 29.28 C O HETATM 2632 O HOH A 736 0.139 10.897 -15.878 1.00 31.93 C O HETATM 2633 O HOH A 737 -21.523 -26.200 -0.816 1.00 44.23 C O HETATM 2634 O HOH A 738 -22.212 -37.705 0.736 1.00 48.70 C O HETATM 2635 O HOH A 739 -24.254 2.810 -1.833 1.00 36.77 C O HETATM 2636 O HOH A 740 -20.983 -34.089 25.361 1.00 32.07 C O HETATM 2637 O HOH A 741 -19.709 4.500 3.067 1.00 31.22 C O HETATM 2638 O HOH A 742 -13.106 -42.216 17.873 1.00 35.75 C O HETATM 2639 O HOH A 743 -23.994 2.742 -4.440 1.00 33.93 C O HETATM 2640 O HOH A 744 5.642 -5.660 -25.772 1.00 35.97 C O HETATM 2641 O HOH A 745 -5.335 -20.302 23.588 1.00 37.26 C O HETATM 2642 O HOH A 746 -23.982 2.445 1.677 1.00 32.19 C O HETATM 2643 O HOH A 747 -3.560 -7.337 0.895 1.00 17.25 C O HETATM 2644 O HOH A 748 -22.435 3.742 0.038 1.00 26.22 C O HETATM 2645 O HOH A 749 4.700 -19.097 -21.839 1.00 36.18 C O HETATM 2646 O HOH A 750 -20.413 -7.765 -18.828 1.00 31.38 C O HETATM 2647 O HOH A 751 4.104 3.693 -17.592 1.00 26.65 C O HETATM 2648 O HOH A 752 -6.011 7.319 -29.106 1.00 38.69 C O HETATM 2649 O HOH A 753 -15.098 -9.844 9.862 1.00 38.74 C O HETATM 2650 O HOH A 754 -7.469 -21.105 12.167 1.00 26.23 C O HETATM 2651 O HOH A 755 -24.307 1.004 -7.207 1.00 29.58 C O HETATM 2652 O HOH A 756 -3.757 -19.361 12.893 1.00 33.64 C O HETATM 2653 O HOH A 757 -1.040 -24.000 14.592 1.00 22.11 C O HETATM 2654 O HOH A 758 -15.233 -16.612 16.445 1.00 28.42 C O HETATM 2655 O HOH A 759 -12.747 -26.751 24.871 1.00 35.52 C O HETATM 2656 O HOH A 760 -23.289 -33.255 26.218 1.00 40.13 C O HETATM 2657 O HOH A 761 -13.798 -29.775 -3.749 1.00 36.18 C O HETATM 2658 O HOH A 762 -5.436 -37.725 0.486 1.00 36.19 C O HETATM 2659 O HOH A 763 -2.984 -24.097 10.483 1.00 25.06 C O HETATM 2660 O HOH A 764 7.072 -14.238 -16.025 1.00 38.50 C O HETATM 2661 O HOH A 765 -10.762 -9.712 7.169 1.00 20.58 C O HETATM 2662 O HOH A 766 -29.147 -27.059 21.863 1.00 36.23 C O HETATM 2663 O HOH A 767 3.384 -12.648 -14.298 1.00 28.38 C O HETATM 2664 O HOH A 768 -0.961 -27.353 -12.600 1.00 26.48 C O HETATM 2665 O HOH A 769 2.775 -9.969 -8.375 1.00 27.13 C O HETATM 2666 O HOH A 770 -15.465 13.524 -1.081 1.00 35.89 C O HETATM 2667 O HOH A 771 -11.314 -9.442 -19.515 1.00 29.95 C O HETATM 2668 O HOH A 772 -4.086 -24.462 -21.756 1.00 36.65 C O HETATM 2669 O HOH A 773 -33.507 -28.792 11.151 1.00 43.03 C O HETATM 2670 O HOH A 774 -7.908 -28.152 -14.548 1.00 29.22 C O HETATM 2671 O HOH A 775 -34.457 -29.198 13.658 1.00 35.06 C O HETATM 2672 O HOH A 776 -1.251 -25.205 -5.352 1.00 30.77 C O HETATM 2673 O HOH A 777 -28.622 -18.250 20.735 1.00 45.83 C O HETATM 2674 O HOH A 778 -8.538 -21.879 8.810 1.00 32.57 C O HETATM 2675 O HOH A 779 -2.518 -24.603 6.460 1.00 28.61 C O HETATM 2676 O HOH A 780 4.018 -9.624 -10.841 1.00 34.79 C O HETATM 2677 O HOH A 781 0.901 -24.943 -21.916 1.00 29.71 C O HETATM 2678 O HOH A 782 -12.481 -16.761 15.131 1.00 29.38 C O HETATM 2679 O HOH A 783 -26.352 -26.401 21.931 1.00 35.48 C O HETATM 2680 O HOH A 784 -2.409 -26.146 2.310 1.00 24.19 C O HETATM 2681 O HOH A 785 -17.506 -33.042 27.877 1.00 36.38 C O HETATM 2682 O HOH A 786 -0.348 -26.722 -7.851 1.00 31.40 C O HETATM 2683 O HOH A 787 -29.356 -38.072 1.322 1.00 37.80 C O HETATM 2684 O HOH A 788 -3.482 -23.059 5.446 1.00 22.26 C O HETATM 2685 O HOH A 789 -15.141 -17.770 18.740 1.00 32.71 C O HETATM 2686 O HOH A 790 -18.785 -25.224 -2.292 1.00 35.53 C O HETATM 2687 O HOH A 791 -29.095 -20.006 18.625 1.00 37.60 C O HETATM 2688 O HOH A 792 -1.847 6.506 -7.508 1.00 32.76 C O HETATM 2689 O HOH A 793 -1.330 -34.880 10.549 1.00 31.70 C O HETATM 2690 O HOH A 794 4.820 0.609 -6.483 1.00 28.20 C O HETATM 2691 O HOH A 795 -9.036 -40.167 24.633 1.00 36.78 C O HETATM 2692 O HOH A 796 -32.016 -25.401 10.595 1.00 34.32 C O HETATM 2693 O HOH A 797 -11.202 -17.839 21.308 1.00 35.30 C O HETATM 2694 O HOH A 798 -6.721 -37.015 24.229 1.00 39.86 C O HETATM 2695 O HOH A 799 -22.526 -41.079 13.069 1.00 36.12 C O HETATM 2696 O HOH A 800 -0.802 -23.674 -3.691 1.00 23.73 C O HETATM 2697 O HOH A 801 -18.092 14.372 -5.372 1.00 32.89 C O HETATM 2698 O HOH A 802 -19.949 -37.151 3.010 1.00 34.02 C O HETATM 2699 O HOH A 803 -19.359 4.078 4.829 1.00 30.30 C O HETATM 2700 O HOH A 804 -23.622 -25.342 -1.020 1.00 39.57 C O HETATM 2701 O HOH A 805 -0.000 -23.786 0.000 0.50 25.23 C O HETATM 2702 O HOH A 806 -4.451 -21.099 9.218 1.00 23.85 C O HETATM 2703 O HOH A 807 -6.654 -18.206 9.714 1.00 28.24 C O HETATM 2704 O HOH A 808 -2.901 -29.138 -19.358 1.00 36.98 C O HETATM 2705 O HOH A 809 1.515 -22.181 -3.498 1.00 18.37 C O HETATM 2706 O HOH A 810 -18.545 12.262 -6.878 1.00 34.10 C O HETATM 2707 O HOH A 811 5.117 -15.332 -12.205 1.00 32.22 C O HETATM 2708 O HOH A 812 4.020 -14.656 -9.817 1.00 20.41 C O HETATM 2709 O HOH A 813 -13.756 -13.316 10.033 1.00 33.32 C O HETATM 2710 O HOH A 814 -11.210 -33.322 25.496 1.00 33.72 C O HETATM 2711 O HOH A 815 -11.087 -16.909 17.861 1.00 31.51 C O HETATM 2712 O HOH A 816 0.484 -28.581 19.686 1.00 31.25 C O HETATM 2713 O HOH A 817 -10.294 -20.527 11.975 1.00 27.08 C O HETATM 2714 O HOH A 818 -1.177 -25.925 6.496 1.00 32.95 C O HETATM 2715 O HOH A 819 -15.225 -37.498 2.820 1.00 28.45 C O HETATM 2716 O HOH A 820 0.017 -27.828 21.733 1.00 34.31 C O HETATM 2717 O HOH A 821 -25.708 -21.651 0.000 0.50 28.05 C O HETATM 2718 O HOH A 822 -15.279 7.901 7.847 1.00 41.36 C O HETATM 2719 O HOH A 823 -16.152 -31.201 -4.010 1.00 37.18 C O HETATM 2720 O HOH A 824 -0.209 -29.465 10.993 1.00 35.55 C O HETATM 2721 O HOH A 825 -16.873 -16.467 20.397 1.00 30.69 C O HETATM 2722 O HOH A 826 -16.479 -14.342 19.491 1.00 31.87 C O CONECT 1120 2371 CONECT 2364 2365 2376 CONECT 2365 2364 2367 2372 CONECT 2366 2374 2382 CONECT 2367 2365 2368 CONECT 2368 2367 2369 CONECT 2369 2368 2370 CONECT 2370 2369 2372 CONECT 2371 1120 2373 2384 CONECT 2372 2365 2370 CONECT 2373 2371 CONECT 2374 2366 2375 2385 2390 CONECT 2375 2374 CONECT 2376 2364 2377 CONECT 2377 2376 2379 2394 CONECT 2378 2379 2382 CONECT 2379 2377 2378 2380 CONECT 2380 2379 2381 2395 CONECT 2381 2380 2383 2396 CONECT 2382 2366 2378 2395 CONECT 2383 2381 2384 CONECT 2384 2371 2383 2386 CONECT 2385 2374 CONECT 2386 2384 2387 CONECT 2387 2386 2388 2392 CONECT 2388 2387 2389 CONECT 2389 2388 2391 CONECT 2390 2374 CONECT 2391 2389 2392 CONECT 2392 2387 2391 2393 CONECT 2393 2392 CONECT 2394 2377 CONECT 2395 2380 2382 CONECT 2396 2381 END