HEADER 3.10.20.30 1wriA00 ATOM 1 N ALA A 1 24.979 13.166 -13.450 1.00 20.99 N ANISOU 1 N ALA A 1 2352 3652 1972 -993 493 -1600 N ATOM 2 CA ALA A 1 26.159 13.388 -12.610 1.00 18.27 C ANISOU 2 CA ALA A 1 2430 2870 1642 -785 434 -1069 C ATOM 3 C ALA A 1 26.142 14.842 -12.151 1.00 15.32 C ANISOU 3 C ALA A 1 1839 2541 1441 -762 78 -476 C ATOM 4 O ALA A 1 25.425 15.659 -12.718 1.00 19.82 O ANISOU 4 O ALA A 1 2097 3226 2209 -384 -666 -718 O ATOM 5 CB ALA A 1 27.458 13.111 -13.337 1.00 27.41 C ANISOU 5 CB ALA A 1 2346 4446 3623 -907 697 -2544 C ATOM 6 N TYR A 2 26.931 15.088 -11.123 1.00 13.72 N ANISOU 6 N TYR A 2 1582 2293 1336 -229 162 -676 N ATOM 7 CA TYR A 2 27.131 16.458 -10.674 1.00 12.75 C ANISOU 7 CA TYR A 2 1328 2229 1288 -305 268 -555 C ATOM 8 C TYR A 2 28.291 17.147 -11.386 1.00 12.94 C ANISOU 8 C TYR A 2 1015 2616 1285 -282 37 -345 C ATOM 9 O TYR A 2 29.385 16.587 -11.478 1.00 16.15 O ANISOU 9 O TYR A 2 1269 2831 2037 -130 421 -57 O ATOM 10 CB TYR A 2 27.411 16.419 -9.173 1.00 12.55 C ANISOU 10 CB TYR A 2 1321 2176 1271 -198 227 -507 C ATOM 11 CG TYR A 2 26.305 15.939 -8.293 1.00 10.30 C ANISOU 11 CG TYR A 2 1065 1615 1235 -159 -14 -569 C ATOM 12 CD1 TYR A 2 25.035 16.525 -8.328 1.00 10.57 C ANISOU 12 CD1 TYR A 2 996 1734 1288 -186 -56 -456 C ATOM 13 CD2 TYR A 2 26.557 14.925 -7.403 1.00 11.51 C ANISOU 13 CD2 TYR A 2 1134 1717 1521 -50 158 -424 C ATOM 14 CE1 TYR A 2 24.033 16.077 -7.480 1.00 10.63 C ANISOU 14 CE1 TYR A 2 1075 1622 1341 -285 -75 -297 C ATOM 15 CE2 TYR A 2 25.576 14.473 -6.550 1.00 11.37 C ANISOU 15 CE2 TYR A 2 1078 1877 1364 -27 91 -373 C ATOM 16 CZ TYR A 2 24.316 15.050 -6.604 1.00 10.23 C ANISOU 16 CZ TYR A 2 938 1485 1462 -246 -162 -369 C ATOM 17 OH TYR A 2 23.379 14.566 -5.724 1.00 11.44 O ANISOU 17 OH TYR A 2 973 1651 1724 -306 -74 -140 O ATOM 18 N LYS A 3 28.061 18.363 -11.847 1.00 13.70 N ANISOU 18 N LYS A 3 1446 2496 1263 -439 -36 -383 N ATOM 19 CA LYS A 3 29.125 19.159 -12.450 1.00 13.81 C ANISOU 19 CA LYS A 3 1384 2807 1056 -539 71 -534 C ATOM 20 C LYS A 3 29.905 19.876 -11.345 1.00 13.54 C ANISOU 20 C LYS A 3 1135 2792 1217 -327 101 -714 C ATOM 21 O LYS A 3 29.314 20.614 -10.565 1.00 16.37 O ANISOU 21 O LYS A 3 1135 3284 1800 -234 58 -1235 O ATOM 22 CB LYS A 3 28.508 20.163 -13.392 1.00 16.94 C ANISOU 22 CB LYS A 3 1863 3130 1445 -922 -222 28 C ATOM 23 CG LYS A 3 29.369 21.065 -14.207 1.00 22.45 C ANISOU 23 CG LYS A 3 2634 4157 1738 -1597 29 257 C ATOM 24 CD LYS A 3 28.609 21.789 -15.304 1.00 28.49 C ANISOU 24 CD LYS A 3 3689 4505 2630 -917 395 1263 C ATOM 25 CE LYS A 3 27.621 22.788 -14.718 1.00 36.69 C ANISOU 25 CE LYS A 3 5564 5762 2616 578 -191 542 C ATOM 26 NZ LYS A 3 27.009 23.640 -15.792 1.00 46.76 N ANISOU 26 NZ LYS A 3 7864 6924 2977 2243 -884 237 N ATOM 27 N VAL A 4 31.213 19.638 -11.281 1.00 12.08 N ANISOU 27 N VAL A 4 1082 2409 1100 -357 164 -359 N ATOM 28 CA VAL A 4 32.071 20.280 -10.259 1.00 11.18 C ANISOU 28 CA VAL A 4 976 2100 1173 -279 214 -380 C ATOM 29 C VAL A 4 33.010 21.207 -10.993 1.00 11.18 C ANISOU 29 C VAL A 4 943 2322 984 -250 161 -229 C ATOM 30 O VAL A 4 33.724 20.759 -11.908 1.00 13.73 O ANISOU 30 O VAL A 4 1569 2488 1161 -303 519 -416 O ATOM 31 CB VAL A 4 32.829 19.219 -9.444 1.00 12.17 C ANISOU 31 CB VAL A 4 1085 2340 1200 -242 190 -164 C ATOM 32 CG1 VAL A 4 33.811 19.834 -8.453 1.00 13.41 C ANISOU 32 CG1 VAL A 4 1118 2740 1238 -192 164 -383 C ATOM 33 CG2 VAL A 4 31.854 18.289 -8.747 1.00 15.06 C ANISOU 33 CG2 VAL A 4 1667 2352 1705 -416 435 -59 C ATOM 34 N THR A 5 33.035 22.462 -10.595 1.00 10.63 N ANISOU 34 N THR A 5 957 2294 786 -307 161 -171 N ATOM 35 CA THR A 5 34.046 23.387 -11.090 1.00 10.88 C ANISOU 35 CA THR A 5 1004 2289 840 -312 -33 17 C ATOM 36 C THR A 5 34.970 23.757 -9.931 1.00 9.89 C ANISOU 36 C THR A 5 873 2274 612 -292 176 -53 C ATOM 37 O THR A 5 34.488 24.264 -8.915 1.00 10.86 O ANISOU 37 O THR A 5 870 2437 820 -24 165 -212 O ATOM 38 CB THR A 5 33.416 24.680 -11.674 1.00 12.59 C ANISOU 38 CB THR A 5 1188 2282 1315 -247 -280 23 C ATOM 39 OG1 THR A 5 32.551 24.298 -12.736 1.00 13.93 O ANISOU 39 OG1 THR A 5 1168 2968 1159 -144 -254 53 O ATOM 40 CG2 THR A 5 34.528 25.604 -12.172 1.00 13.59 C ANISOU 40 CG2 THR A 5 1512 2266 1387 -229 -88 213 C ATOM 41 N LEU A 6 36.250 23.495 -10.118 1.00 9.97 N ANISOU 41 N LEU A 6 826 2227 736 -249 210 -50 N ATOM 42 CA LEU A 6 37.280 23.941 -9.166 1.00 9.92 C ANISOU 42 CA LEU A 6 875 2023 872 -211 51 -32 C ATOM 43 C LEU A 6 37.951 25.176 -9.721 1.00 10.12 C ANISOU 43 C LEU A 6 975 2187 683 -288 219 20 C ATOM 44 O LEU A 6 38.537 25.119 -10.811 1.00 12.04 O ANISOU 44 O LEU A 6 1099 2792 684 -325 288 -108 O ATOM 45 CB LEU A 6 38.292 22.836 -8.863 1.00 10.88 C ANISOU 45 CB LEU A 6 1057 2183 895 40 174 -123 C ATOM 46 CG LEU A 6 37.655 21.561 -8.273 1.00 11.83 C ANISOU 46 CG LEU A 6 1338 1960 1196 -15 -69 -149 C ATOM 47 CD1 LEU A 6 38.765 20.526 -7.991 1.00 13.28 C ANISOU 47 CD1 LEU A 6 1467 2179 1400 163 -172 -126 C ATOM 48 CD2 LEU A 6 36.856 21.854 -7.012 1.00 12.19 C ANISOU 48 CD2 LEU A 6 1401 1978 1254 -177 190 171 C ATOM 49 N LYS A 7 37.834 26.298 -9.029 1.00 9.69 N ANISOU 49 N LYS A 7 859 2112 711 -332 161 79 N ATOM 50 CA LYS A 7 38.446 27.592 -9.400 1.00 10.55 C ANISOU 50 CA LYS A 7 934 2045 1031 -220 -48 353 C ATOM 51 C LYS A 7 39.758 27.647 -8.647 1.00 9.62 C ANISOU 51 C LYS A 7 933 2021 702 -365 60 304 C ATOM 52 O LYS A 7 39.763 27.938 -7.440 1.00 10.50 O ANISOU 52 O LYS A 7 1057 2158 773 -239 128 186 O ATOM 53 CB LYS A 7 37.529 28.725 -9.074 1.00 10.89 C ANISOU 53 CB LYS A 7 1029 2178 932 -198 69 215 C ATOM 54 CG LYS A 7 36.213 28.692 -9.824 1.00 12.56 C ANISOU 54 CG LYS A 7 862 2587 1323 -135 116 280 C ATOM 55 CD LYS A 7 35.354 29.933 -9.580 1.00 16.50 C ANISOU 55 CD LYS A 7 1225 2491 2554 49 -173 428 C ATOM 56 CE LYS A 7 35.935 31.100 -10.339 1.00 21.08 C ANISOU 56 CE LYS A 7 2661 2718 2629 441 938 553 C ATOM 57 NZ LYS A 7 35.734 30.961 -11.814 1.00 34.23 N ANISOU 57 NZ LYS A 7 5597 4657 2753 461 -272 1359 N ATOM 58 N THR A 8 40.866 27.302 -9.341 1.00 11.97 N ANISOU 58 N THR A 8 813 3011 724 -394 154 285 N ATOM 59 CA THR A 8 42.175 27.226 -8.715 1.00 11.46 C ANISOU 59 CA THR A 8 874 2699 782 -284 149 222 C ATOM 60 C THR A 8 42.929 28.506 -8.978 1.00 12.34 C ANISOU 60 C THR A 8 858 2784 1045 -334 59 402 C ATOM 61 O THR A 8 42.576 29.255 -9.889 1.00 15.13 O ANISOU 61 O THR A 8 1405 3219 1124 -533 -153 711 O ATOM 62 CB THR A 8 43.006 26.004 -9.159 1.00 12.61 C ANISOU 62 CB THR A 8 1006 2799 985 -251 248 105 C ATOM 63 OG1 THR A 8 43.642 26.353 -10.388 1.00 13.44 O ANISOU 63 OG1 THR A 8 967 3233 907 -182 260 154 O ATOM 64 CG2 THR A 8 42.185 24.756 -9.340 1.00 13.34 C ANISOU 64 CG2 THR A 8 1510 2702 858 -291 170 89 C ATOM 65 N PRO A 9 44.016 28.786 -8.277 1.00 12.84 N ANISOU 65 N PRO A 9 1118 2805 954 -435 -34 261 N ATOM 66 CA PRO A 9 44.805 29.966 -8.577 1.00 15.88 C ANISOU 66 CA PRO A 9 1794 3013 1226 -938 -340 281 C ATOM 67 C PRO A 9 45.363 29.999 -9.997 1.00 20.66 C ANISOU 67 C PRO A 9 2557 3941 1352 -1651 -138 655 C ATOM 68 O PRO A 9 45.661 31.091 -10.450 1.00 31.19 O ANISOU 68 O PRO A 9 5080 4865 1904 -3080 -574 1241 O ATOM 69 CB PRO A 9 45.964 29.886 -7.549 1.00 18.73 C ANISOU 69 CB PRO A 9 1839 3707 1571 -1151 -493 829 C ATOM 70 CG PRO A 9 45.328 29.157 -6.398 1.00 16.47 C ANISOU 70 CG PRO A 9 1682 3314 1261 -914 -375 443 C ATOM 71 CD PRO A 9 44.506 28.059 -7.067 1.00 13.85 C ANISOU 71 CD PRO A 9 1211 3036 1016 -531 -192 291 C ATOM 72 N ASP A 10 45.455 28.839 -10.622 1.00 19.03 N ANISOU 72 N ASP A 10 1195 4786 1249 -1127 62 -47 N ATOM 73 CA ASP A 10 46.015 28.743 -11.982 1.00 23.18 C ANISOU 73 CA ASP A 10 1116 6382 1311 -1238 255 392 C ATOM 74 C ASP A 10 44.952 28.403 -13.007 1.00 21.79 C ANISOU 74 C ASP A 10 1246 6019 1014 -810 184 362 C ATOM 75 O ASP A 10 45.295 27.930 -14.092 1.00 33.25 O ANISOU 75 O ASP A 10 1900 9194 1539 -378 297 -710 O ATOM 76 CB ASP A 10 47.113 27.674 -11.985 1.00 32.68 C ANISOU 76 CB ASP A 10 1149 9395 1871 254 169 -486 C ATOM 77 CG ASP A 10 48.379 28.028 -11.230 1.00 42.74 C ANISOU 77 CG ASP A 10 2098 10070 4072 -328 -1255 363 C ATOM 78 OD1 ASP A 10 48.923 27.144 -10.514 1.00 53.33 O ANISOU 78 OD1 ASP A 10 3208 13357 3697 619 -1212 1830 O ATOM 79 OD2 ASP A 10 48.854 29.189 -11.341 1.00 62.59 O ANISOU 79 OD2 ASP A 10 3223 11094 9463 -1958 -1351 210 O ATOM 80 N GLY A 11 43.689 28.633 -12.772 1.00 17.09 N ANISOU 80 N GLY A 11 1264 3707 1521 -684 -146 166 N ATOM 81 CA GLY A 11 42.649 28.347 -13.763 1.00 15.63 C ANISOU 81 CA GLY A 11 1199 3605 1135 -773 8 507 C ATOM 82 C GLY A 11 41.539 27.511 -13.194 1.00 13.27 C ANISOU 82 C GLY A 11 1124 3152 764 -501 -43 465 C ATOM 83 O GLY A 11 41.690 26.923 -12.133 1.00 14.86 O ANISOU 83 O GLY A 11 1237 3613 796 -443 86 547 O ATOM 84 N ASP A 12 40.446 27.490 -13.931 1.00 12.04 N ANISOU 84 N ASP A 12 932 2729 912 -294 57 201 N ATOM 85 CA ASP A 12 39.279 26.720 -13.526 1.00 12.47 C ANISOU 85 CA ASP A 12 1099 2835 803 -394 -19 266 C ATOM 86 C ASP A 12 39.241 25.396 -14.277 1.00 12.87 C ANISOU 86 C ASP A 12 1151 3149 590 -650 -33 91 C ATOM 87 O ASP A 12 39.609 25.332 -15.444 1.00 14.64 O ANISOU 87 O ASP A 12 1342 3631 590 -552 101 73 O ATOM 88 CB ASP A 12 37.998 27.506 -13.820 1.00 16.10 C ANISOU 88 CB ASP A 12 948 3869 1299 -89 152 415 C ATOM 89 CG ASP A 12 37.863 28.848 -13.138 1.00 21.45 C ANISOU 89 CG ASP A 12 2813 4274 1062 1221 380 390 C ATOM 90 OD1 ASP A 12 38.664 29.155 -12.234 1.00 19.71 O ANISOU 90 OD1 ASP A 12 3131 2952 1406 -75 484 512 O ATOM 91 OD2 ASP A 12 36.940 29.613 -13.526 1.00 32.22 O ANISOU 91 OD2 ASP A 12 4552 5981 1708 2886 297 662 O ATOM 92 N ILE A 13 38.784 24.340 -13.607 1.00 13.02 N ANISOU 92 N ILE A 13 1152 2948 845 -590 165 22 N ATOM 93 CA ILE A 13 38.545 23.093 -14.315 1.00 14.29 C ANISOU 93 CA ILE A 13 1215 3051 1164 -451 504 -279 C ATOM 94 C ILE A 13 37.194 22.536 -13.884 1.00 13.85 C ANISOU 94 C ILE A 13 1384 2915 965 -646 430 -328 C ATOM 95 O ILE A 13 36.844 22.546 -12.728 1.00 14.94 O ANISOU 95 O ILE A 13 1533 3211 932 -744 523 -586 O ATOM 96 CB ILE A 13 39.671 22.054 -14.181 1.00 18.25 C ANISOU 96 CB ILE A 13 1660 3478 1796 -29 118 -384 C ATOM 97 CG1 ILE A 13 39.498 20.936 -15.211 1.00 20.65 C ANISOU 97 CG1 ILE A 13 2616 3314 1917 175 301 -474 C ATOM 98 CG2 ILE A 13 39.802 21.623 -12.726 1.00 21.54 C ANISOU 98 CG2 ILE A 13 2609 3661 1913 305 -188 -270 C ATOM 99 CD1 ILE A 13 39.452 21.391 -16.648 1.00 25.36 C ANISOU 99 CD1 ILE A 13 3329 4571 1737 1333 69 -688 C ATOM 100 N THR A 14 36.473 22.018 -14.851 1.00 15.81 N ANISOU 100 N THR A 14 1362 3560 1084 -727 498 -619 N ATOM 101 CA THR A 14 35.137 21.460 -14.617 1.00 15.12 C ANISOU 101 CA THR A 14 1429 3319 998 -682 463 -435 C ATOM 102 C THR A 14 35.146 19.996 -14.978 1.00 15.64 C ANISOU 102 C THR A 14 1315 3396 1233 -610 366 -722 C ATOM 103 O THR A 14 35.725 19.633 -16.021 1.00 20.59 O ANISOU 103 O THR A 14 2752 3845 1226 -964 839 -917 O ATOM 104 CB THR A 14 34.099 22.226 -15.450 1.00 17.89 C ANISOU 104 CB THR A 14 1593 3416 1788 -622 -56 -570 C ATOM 105 OG1 THR A 14 34.050 23.581 -14.978 1.00 18.04 O ANISOU 105 OG1 THR A 14 1700 3320 1836 -603 194 -510 O ATOM 106 CG2 THR A 14 32.687 21.702 -15.269 1.00 18.37 C ANISOU 106 CG2 THR A 14 1677 3259 2044 -677 32 -173 C ATOM 107 N PHE A 15 34.540 19.186 -14.126 1.00 15.56 N ANISOU 107 N PHE A 15 1401 3258 1253 -662 337 -669 N ATOM 108 CA PHE A 15 34.452 17.759 -14.377 1.00 16.02 C ANISOU 108 CA PHE A 15 1505 3321 1259 -600 456 -726 C ATOM 109 C PHE A 15 33.186 17.201 -13.750 1.00 15.93 C ANISOU 109 C PHE A 15 2036 3083 934 -757 615 -748 C ATOM 110 O PHE A 15 32.606 17.794 -12.845 1.00 18.06 O ANISOU 110 O PHE A 15 1715 3255 1894 -593 828 -1214 O ATOM 111 CB PHE A 15 35.684 17.013 -13.848 1.00 18.99 C ANISOU 111 CB PHE A 15 2098 3600 1520 -70 224 -1016 C ATOM 112 CG PHE A 15 35.955 17.240 -12.374 1.00 16.80 C ANISOU 112 CG PHE A 15 1454 3531 1399 -196 392 -930 C ATOM 113 CD1 PHE A 15 35.472 16.408 -11.366 1.00 17.37 C ANISOU 113 CD1 PHE A 15 1348 3557 1695 -237 475 -853 C ATOM 114 CD2 PHE A 15 36.743 18.344 -12.004 1.00 16.86 C ANISOU 114 CD2 PHE A 15 1483 3194 1731 -46 -13 -633 C ATOM 115 CE1 PHE A 15 35.768 16.672 -10.023 1.00 16.85 C ANISOU 115 CE1 PHE A 15 1168 3604 1629 -248 236 -437 C ATOM 116 CE2 PHE A 15 36.995 18.580 -10.673 1.00 16.18 C ANISOU 116 CE2 PHE A 15 1214 3160 1775 -103 77 -722 C ATOM 117 CZ PHE A 15 36.545 17.760 -9.648 1.00 15.74 C ANISOU 117 CZ PHE A 15 881 3417 1684 71 315 -748 C ATOM 118 N ASP A 16 32.686 16.036 -14.130 1.00 16.11 N ANISOU 118 N ASP A 16 1880 2933 1307 -604 504 -824 N ATOM 119 CA ASP A 16 31.558 15.386 -13.539 1.00 17.19 C ANISOU 119 CA ASP A 16 1852 3059 1622 -653 371 -592 C ATOM 120 C ASP A 16 31.931 14.378 -12.477 1.00 15.38 C ANISOU 120 C ASP A 16 1580 2492 1772 -533 563 -781 C ATOM 121 O ASP A 16 32.958 13.683 -12.522 1.00 18.72 O ANISOU 121 O ASP A 16 1851 3109 2153 -139 537 -901 O ATOM 122 CB ASP A 16 30.811 14.694 -14.685 1.00 21.56 C ANISOU 122 CB ASP A 16 2822 3406 1963 -1308 -59 -466 C ATOM 123 CG ASP A 16 29.888 15.604 -15.475 1.00 29.55 C ANISOU 123 CG ASP A 16 4930 3566 2731 -915 -1506 -583 C ATOM 124 OD1 ASP A 16 29.372 15.152 -16.514 1.00 34.94 O ANISOU 124 OD1 ASP A 16 5089 5009 3176 -377 -1783 -1353 O ATOM 125 OD2 ASP A 16 29.636 16.772 -15.099 1.00 40.51 O ANISOU 125 OD2 ASP A 16 8559 3520 3313 -126 -2488 -586 O ATOM 126 N VAL A 17 31.074 14.316 -11.454 1.00 15.58 N ANISOU 126 N VAL A 17 1681 2732 1506 -421 440 -694 N ATOM 127 CA VAL A 17 31.203 13.376 -10.329 1.00 15.55 C ANISOU 127 CA VAL A 17 1331 2699 1879 -220 596 -514 C ATOM 128 C VAL A 17 29.918 12.567 -10.232 1.00 15.77 C ANISOU 128 C VAL A 17 1445 2541 2006 -299 437 -618 C ATOM 129 O VAL A 17 28.825 13.131 -10.216 1.00 17.75 O ANISOU 129 O VAL A 17 1375 2628 2741 -313 459 -434 O ATOM 130 CB VAL A 17 31.544 14.155 -9.038 1.00 16.10 C ANISOU 130 CB VAL A 17 1612 2661 1843 -365 -264 -128 C ATOM 131 CG1 VAL A 17 31.599 13.293 -7.786 1.00 17.42 C ANISOU 131 CG1 VAL A 17 1690 2744 2185 -427 -208 181 C ATOM 132 CG2 VAL A 17 32.878 14.898 -9.220 1.00 17.22 C ANISOU 132 CG2 VAL A 17 1611 3115 1818 -435 241 -172 C ATOM 133 N GLU A 18 30.026 11.243 -10.136 1.00 17.41 N ANISOU 133 N GLU A 18 1899 2505 2212 -209 807 -705 N ATOM 134 CA GLU A 18 28.852 10.388 -9.961 1.00 16.95 C ANISOU 134 CA GLU A 18 1934 2323 2185 -231 465 -765 C ATOM 135 C GLU A 18 28.277 10.614 -8.558 1.00 13.55 C ANISOU 135 C GLU A 18 1358 1862 1930 -300 212 -477 C ATOM 136 O GLU A 18 29.014 10.768 -7.597 1.00 14.94 O ANISOU 136 O GLU A 18 1361 2110 2204 -351 126 -672 O ATOM 137 CB GLU A 18 29.217 8.918 -10.174 1.00 21.13 C ANISOU 137 CB GLU A 18 2759 2469 2800 -172 630 -1155 C ATOM 138 CG GLU A 18 29.591 8.665 -11.643 1.00 30.34 C ANISOU 138 CG GLU A 18 3955 4452 3121 -721 477 -2744 C ATOM 139 CD GLU A 18 28.324 8.742 -12.491 1.00 32.46 C ANISOU 139 CD GLU A 18 4363 4774 3196 -1807 102 -2310 C ATOM 140 OE1 GLU A 18 27.256 8.287 -12.018 1.00 38.78 O ANISOU 140 OE1 GLU A 18 4880 5552 4304 -2918 -884 -201 O ATOM 141 OE2 GLU A 18 28.383 9.224 -13.631 1.00 38.17 O ANISOU 141 OE2 GLU A 18 4168 7027 3308 -2599 44 -1713 O ATOM 142 N PRO A 19 26.953 10.661 -8.463 1.00 15.17 N ANISOU 142 N PRO A 19 1396 2277 2093 -257 43 -674 N ATOM 143 CA PRO A 19 26.348 11.038 -7.181 1.00 13.47 C ANISOU 143 CA PRO A 19 1111 1914 2093 -178 97 -393 C ATOM 144 C PRO A 19 26.738 10.104 -6.073 1.00 13.13 C ANISOU 144 C PRO A 19 1043 1615 2331 -385 111 -304 C ATOM 145 O PRO A 19 26.633 8.877 -6.149 1.00 15.24 O ANISOU 145 O PRO A 19 1465 1710 2615 -463 72 -417 O ATOM 146 CB PRO A 19 24.830 10.955 -7.412 1.00 17.13 C ANISOU 146 CB PRO A 19 1209 3206 2096 -323 -13 -140 C ATOM 147 CG PRO A 19 24.709 11.151 -8.889 1.00 24.83 C ANISOU 147 CG PRO A 19 1798 5589 2046 699 -112 -223 C ATOM 148 CD PRO A 19 25.922 10.514 -9.497 1.00 18.96 C ANISOU 148 CD PRO A 19 1553 3427 2224 -267 -113 -696 C ATOM 149 N GLY A 20 27.213 10.722 -5.003 1.00 12.37 N ANISOU 149 N GLY A 20 944 1700 2055 -120 230 -317 N ATOM 150 CA GLY A 20 27.677 9.966 -3.845 1.00 13.46 C ANISOU 150 CA GLY A 20 994 1793 2325 -438 220 65 C ATOM 151 C GLY A 20 29.169 9.877 -3.744 1.00 12.05 C ANISOU 151 C GLY A 20 1008 1343 2227 -143 275 -226 C ATOM 152 O GLY A 20 29.692 9.564 -2.671 1.00 13.43 O ANISOU 152 O GLY A 20 1158 1660 2284 31 272 -9 O ATOM 153 N GLU A 21 29.900 10.150 -4.829 1.00 12.43 N ANISOU 153 N GLU A 21 1026 1381 2315 -135 266 -37 N ATOM 154 CA GLU A 21 31.344 10.118 -4.792 1.00 12.83 C ANISOU 154 CA GLU A 21 977 1448 2450 -142 385 -366 C ATOM 155 C GLU A 21 31.922 11.397 -4.208 1.00 11.60 C ANISOU 155 C GLU A 21 890 1405 2112 -175 516 -246 C ATOM 156 O GLU A 21 31.321 12.494 -4.346 1.00 13.27 O ANISOU 156 O GLU A 21 930 1477 2636 -89 251 -443 O ATOM 157 CB GLU A 21 31.826 9.927 -6.261 1.00 16.62 C ANISOU 157 CB GLU A 21 1298 2427 2591 -110 381 -998 C ATOM 158 CG GLU A 21 31.488 8.527 -6.750 1.00 19.94 C ANISOU 158 CG GLU A 21 1761 2339 3477 87 577 -1290 C ATOM 159 CD GLU A 21 31.992 7.491 -5.775 1.00 24.25 C ANISOU 159 CD GLU A 21 2224 2461 4529 -142 -92 -858 C ATOM 160 OE1 GLU A 21 33.215 7.390 -5.513 1.00 29.64 O ANISOU 160 OE1 GLU A 21 2428 3384 5449 618 -570 -1616 O ATOM 161 OE2 GLU A 21 31.138 6.725 -5.265 1.00 46.39 O ANISOU 161 OE2 GLU A 21 3986 5355 8286 -2072 -1384 2442 O ATOM 162 N ARG A 22 33.088 11.317 -3.591 1.00 13.65 N ANISOU 162 N ARG A 22 943 1475 2767 -84 283 -341 N ATOM 163 CA ARG A 22 33.901 12.473 -3.215 1.00 13.32 C ANISOU 163 CA ARG A 22 1090 1589 2381 -272 374 -356 C ATOM 164 C ARG A 22 34.433 13.184 -4.442 1.00 14.14 C ANISOU 164 C ARG A 22 1282 1731 2360 -362 753 -671 C ATOM 165 O ARG A 22 34.902 12.560 -5.411 1.00 17.58 O ANISOU 165 O ARG A 22 2030 1952 2699 -307 1092 -830 O ATOM 166 CB ARG A 22 35.101 12.024 -2.373 1.00 15.61 C ANISOU 166 CB ARG A 22 848 2164 2921 96 310 -510 C ATOM 167 CG ARG A 22 34.691 11.561 -0.953 1.00 18.30 C ANISOU 167 CG ARG A 22 1560 2818 2575 294 120 -432 C ATOM 168 CD AARG A 22 35.838 11.314 0.028 0.50 32.18 C ANISOU 168 CD AARG A 22 3824 4405 3999 1707 -1376 -175 C ATOM 169 CD BARG A 22 35.986 10.946 -0.367 0.50 29.97 C ANISOU 169 CD BARG A 22 3113 4569 3706 2478 266 112 C ATOM 170 NE AARG A 22 35.550 10.346 1.076 0.50 40.03 N ANISOU 170 NE AARG A 22 5924 4446 4840 2410 -1460 526 N ATOM 171 NE BARG A 22 35.791 9.514 -0.350 0.50 51.27 N ANISOU 171 NE BARG A 22 8055 4476 6947 2665 -2173 581 N ATOM 172 CZ AARG A 22 35.846 9.808 2.216 0.50 48.87 C ANISOU 172 CZ AARG A 22 8533 4684 5351 1310 -2511 915 C ATOM 173 CZ BARG A 22 35.681 8.496 0.457 0.50 59.55 C ANISOU 173 CZ BARG A 22 10456 4483 7688 1553 -2769 884 C ATOM 174 NH1AARG A 22 36.893 10.158 2.980 0.50 60.23 N ANISOU 174 NH1AARG A 22 13015 3936 5935 1537 -5191 -1778 N ATOM 175 NH1BARG A 22 35.743 8.525 1.780 0.50 60.56 N ANISOU 175 NH1BARG A 22 10602 4843 7564 847 -1092 1217 N ATOM 176 NH2AARG A 22 35.125 8.806 2.781 0.50 53.95 N ANISOU 176 NH2AARG A 22 11801 3675 5022 1607 438 -275 N ATOM 177 NH2BARG A 22 35.489 7.325 -0.167 0.50 73.98 N ANISOU 177 NH2BARG A 22 14698 4602 8810 1623 -2241 307 N ATOM 178 N LEU A 23 34.417 14.520 -4.435 1.00 10.57 N ANISOU 178 N LEU A 23 795 1692 1527 -65 170 -328 N ATOM 179 CA LEU A 23 34.969 15.242 -5.573 1.00 11.76 C ANISOU 179 CA LEU A 23 818 2100 1549 91 217 -212 C ATOM 180 C LEU A 23 36.479 15.154 -5.654 1.00 11.30 C ANISOU 180 C LEU A 23 836 1965 1493 -222 188 -310 C ATOM 181 O LEU A 23 37.028 15.402 -6.755 1.00 12.54 O ANISOU 181 O LEU A 23 1060 2287 1416 -184 333 -443 O ATOM 182 CB LEU A 23 34.480 16.679 -5.532 1.00 11.79 C ANISOU 182 CB LEU A 23 946 1880 1655 -161 144 -257 C ATOM 183 CG LEU A 23 34.931 17.559 -4.385 1.00 11.95 C ANISOU 183 CG LEU A 23 1141 2190 1209 -177 217 -174 C ATOM 184 CD1 LEU A 23 36.282 18.232 -4.574 1.00 13.20 C ANISOU 184 CD1 LEU A 23 1302 1804 1910 -350 -124 35 C ATOM 185 CD2 LEU A 23 33.886 18.642 -4.121 1.00 14.26 C ANISOU 185 CD2 LEU A 23 1529 2036 1851 -50 177 -282 C ATOM 186 N ILE A 24 37.165 14.815 -4.549 1.00 10.85 N ANISOU 186 N ILE A 24 678 1980 1464 -237 127 -462 N ATOM 187 CA ILE A 24 38.618 14.861 -4.590 1.00 11.16 C ANISOU 187 CA ILE A 24 743 2135 1363 -153 237 -423 C ATOM 188 C ILE A 24 39.214 13.786 -5.460 1.00 11.89 C ANISOU 188 C ILE A 24 945 1937 1637 112 56 -376 C ATOM 189 O ILE A 24 40.340 13.931 -5.936 1.00 13.59 O ANISOU 189 O ILE A 24 1012 2493 1659 179 211 -446 O ATOM 190 CB ILE A 24 39.229 14.787 -3.158 1.00 11.50 C ANISOU 190 CB ILE A 24 711 2197 1460 23 223 -198 C ATOM 191 CG1 ILE A 24 40.634 15.380 -3.173 1.00 12.61 C ANISOU 191 CG1 ILE A 24 700 2660 1432 -40 146 -267 C ATOM 192 CG2 ILE A 24 39.150 13.399 -2.579 1.00 13.87 C ANISOU 192 CG2 ILE A 24 1086 2342 1843 282 498 40 C ATOM 193 CD1 ILE A 24 40.706 16.894 -3.334 1.00 16.49 C ANISOU 193 CD1 ILE A 24 1492 2745 2027 -617 55 -58 C ATOM 194 N ASP A 25 38.443 12.691 -5.682 1.00 13.47 N ANISOU 194 N ASP A 25 1352 1919 1846 31 18 -516 N ATOM 195 CA ASP A 25 39.068 11.592 -6.435 1.00 17.71 C ANISOU 195 CA ASP A 25 2438 1879 2412 131 273 -602 C ATOM 196 C ASP A 25 39.396 12.014 -7.834 1.00 18.39 C ANISOU 196 C ASP A 25 1998 2612 2378 631 556 -676 C ATOM 197 O ASP A 25 40.519 11.839 -8.277 1.00 23.14 O ANISOU 197 O ASP A 25 1993 3632 3167 684 651 -1060 O ATOM 198 CB ASP A 25 38.083 10.415 -6.426 1.00 23.65 C ANISOU 198 CB ASP A 25 3022 1952 4012 -192 838 -983 C ATOM 199 CG ASP A 25 37.943 9.839 -5.023 1.00 27.61 C ANISOU 199 CG ASP A 25 3047 2371 5074 -11 859 395 C ATOM 200 OD1 ASP A 25 38.752 10.192 -4.143 1.00 42.69 O ANISOU 200 OD1 ASP A 25 5204 6567 4450 -2622 392 1487 O ATOM 201 OD2 ASP A 25 37.055 8.990 -4.767 1.00 39.48 O ANISOU 201 OD2 ASP A 25 4750 3309 6941 -1317 316 1317 O ATOM 202 N ILE A 26 38.432 12.549 -8.565 1.00 16.02 N ANISOU 202 N ILE A 26 1696 2259 2131 -166 305 -692 N ATOM 203 CA ILE A 26 38.719 13.039 -9.928 1.00 16.40 C ANISOU 203 CA ILE A 26 1378 2907 1946 -429 280 -898 C ATOM 204 C ILE A 26 39.372 14.395 -9.825 1.00 14.89 C ANISOU 204 C ILE A 26 1153 2753 1753 -254 555 -814 C ATOM 205 O ILE A 26 40.262 14.700 -10.630 1.00 16.16 O ANISOU 205 O ILE A 26 1541 2908 1692 -209 670 -611 O ATOM 206 CB ILE A 26 37.433 13.093 -10.767 1.00 17.18 C ANISOU 206 CB ILE A 26 1543 2841 2146 -331 98 -870 C ATOM 207 CG1 ILE A 26 36.902 11.659 -10.946 1.00 18.47 C ANISOU 207 CG1 ILE A 26 1763 2770 2486 -226 -52 -1202 C ATOM 208 CG2 ILE A 26 37.645 13.814 -12.083 1.00 19.18 C ANISOU 208 CG2 ILE A 26 1638 3569 2079 -544 3 -764 C ATOM 209 CD1 ILE A 26 35.497 11.642 -11.524 1.00 24.84 C ANISOU 209 CD1 ILE A 26 2012 4021 3406 -855 -447 -1042 C ATOM 210 N GLY A 27 39.043 15.224 -8.830 1.00 13.89 N ANISOU 210 N GLY A 27 973 2633 1672 -260 372 -732 N ATOM 211 CA GLY A 27 39.680 16.534 -8.721 1.00 13.44 C ANISOU 211 CA GLY A 27 966 2451 1691 -173 208 -396 C ATOM 212 C GLY A 27 41.191 16.454 -8.700 1.00 12.66 C ANISOU 212 C GLY A 27 944 2560 1307 -199 322 -417 C ATOM 213 O GLY A 27 41.867 17.225 -9.392 1.00 15.25 O ANISOU 213 O GLY A 27 1205 3056 1532 -422 423 -221 O ATOM 214 N SER A 28 41.736 15.535 -7.860 1.00 13.55 N ANISOU 214 N SER A 28 992 2469 1687 -121 196 -456 N ATOM 215 CA SER A 28 43.201 15.377 -7.798 1.00 15.52 C ANISOU 215 CA SER A 28 879 2570 2447 -29 178 -738 C ATOM 216 C SER A 28 43.816 14.891 -9.084 1.00 17.79 C ANISOU 216 C SER A 28 1090 3169 2499 -10 420 -675 C ATOM 217 O SER A 28 45.033 14.971 -9.284 1.00 21.54 O ANISOU 217 O SER A 28 1189 3986 3007 -114 700 -646 O ATOM 218 CB SER A 28 43.537 14.365 -6.696 1.00 17.48 C ANISOU 218 CB SER A 28 1140 3074 2426 544 122 -673 C ATOM 219 OG ASER A 28 43.367 14.979 -5.438 0.50 17.89 O ANISOU 219 OG ASER A 28 1361 2892 2545 120 546 -572 O ATOM 220 OG BSER A 28 42.767 13.175 -6.761 0.50 38.52 O ANISOU 220 OG BSER A 28 5164 3245 6225 -959 455 547 O ATOM 221 N GLU A 29 42.996 14.282 -9.951 1.00 20.29 N ANISOU 221 N GLU A 29 1506 3808 2395 20 427 -1070 N ATOM 222 CA GLU A 29 43.457 13.827 -11.278 1.00 23.99 C ANISOU 222 CA GLU A 29 2502 3690 2922 250 851 -1519 C ATOM 223 C GLU A 29 43.553 15.005 -12.237 1.00 22.82 C ANISOU 223 C GLU A 29 1919 4368 2382 -164 924 -1400 C ATOM 224 O GLU A 29 44.389 15.118 -13.128 1.00 35.01 O ANISOU 224 O GLU A 29 3771 6191 3342 414 2269 -1041 O ATOM 225 CB GLU A 29 42.480 12.811 -11.827 1.00 30.98 C ANISOU 225 CB GLU A 29 3615 4851 3304 -1231 2222 -2365 C ATOM 226 CG GLU A 29 42.623 11.373 -11.400 1.00 41.52 C ANISOU 226 CG GLU A 29 5889 4778 5108 -1943 2871 -1901 C ATOM 227 CD GLU A 29 41.506 10.519 -11.989 1.00 52.02 C ANISOU 227 CD GLU A 29 7697 5660 6410 -3181 2332 -2093 C ATOM 228 OE1 GLU A 29 41.338 9.395 -11.481 1.00 63.08 O ANISOU 228 OE1 GLU A 29 9605 5442 8921 -3726 3686 -1969 O ATOM 229 OE2 GLU A 29 40.832 10.981 -12.940 1.00 57.16 O ANISOU 229 OE2 GLU A 29 8723 6020 6974 -1492 870 -4284 O ATOM 230 N LYS A 30 42.693 16.014 -12.030 1.00 18.21 N ANISOU 230 N LYS A 30 1182 3992 1744 -433 -8 -1075 N ATOM 231 CA LYS A 30 42.538 17.084 -13.003 1.00 19.49 C ANISOU 231 CA LYS A 30 1627 4686 1092 -796 121 -863 C ATOM 232 C LYS A 30 43.271 18.357 -12.606 1.00 18.31 C ANISOU 232 C LYS A 30 1388 4469 1099 -728 64 -511 C ATOM 233 O LYS A 30 43.486 19.233 -13.464 1.00 25.60 O ANISOU 233 O LYS A 30 3070 5648 1007 -1916 203 -271 O ATOM 234 CB LYS A 30 41.069 17.473 -13.187 1.00 22.04 C ANISOU 234 CB LYS A 30 1666 4404 2303 -979 -303 183 C ATOM 235 CG LYS A 30 40.067 16.404 -13.531 1.00 28.81 C ANISOU 235 CG LYS A 30 2616 5231 3101 -1692 -1408 539 C ATOM 236 CD LYS A 30 40.330 15.853 -14.909 1.00 38.61 C ANISOU 236 CD LYS A 30 5723 6201 2747 -2725 -1844 138 C ATOM 237 CE LYS A 30 39.185 14.884 -15.282 1.00 40.19 C ANISOU 237 CE LYS A 30 6133 5863 3276 -3102 -1477 385 C ATOM 238 NZ LYS A 30 39.660 14.012 -16.398 1.00 53.58 N ANISOU 238 NZ LYS A 30 8408 5843 6106 -2725 -1331 -1629 N ATOM 239 N ALA A 31 43.662 18.436 -11.336 1.00 16.60 N ANISOU 239 N ALA A 31 1258 3863 1187 -513 -54 -589 N ATOM 240 CA ALA A 31 44.367 19.622 -10.830 1.00 16.93 C ANISOU 240 CA ALA A 31 1456 3543 1431 -375 -206 -481 C ATOM 241 C ALA A 31 45.292 19.187 -9.686 1.00 15.26 C ANISOU 241 C ALA A 31 1324 3490 985 -717 5 -337 C ATOM 242 O ALA A 31 45.082 18.156 -9.075 1.00 17.50 O ANISOU 242 O ALA A 31 1494 3450 1706 -733 -45 -209 O ATOM 243 CB ALA A 31 43.409 20.681 -10.370 1.00 19.26 C ANISOU 243 CB ALA A 31 1586 3928 1802 -190 -106 -718 C ATOM 244 N ASP A 32 46.308 20.010 -9.434 1.00 15.77 N ANISOU 244 N ASP A 32 1409 3594 990 -820 59 -286 N ATOM 245 CA ASP A 32 47.187 19.742 -8.283 1.00 16.11 C ANISOU 245 CA ASP A 32 1107 4072 942 -705 170 -441 C ATOM 246 C ASP A 32 46.521 20.447 -7.111 1.00 14.47 C ANISOU 246 C ASP A 32 1690 2822 984 -953 373 -299 C ATOM 247 O ASP A 32 46.426 21.689 -7.043 1.00 23.17 O ANISOU 247 O ASP A 32 4404 2697 1702 -1518 807 -237 O ATOM 248 CB ASP A 32 48.581 20.253 -8.519 1.00 22.04 C ANISOU 248 CB ASP A 32 1244 5607 1524 -1170 271 -530 C ATOM 249 CG ASP A 32 49.269 19.761 -9.769 1.00 26.36 C ANISOU 249 CG ASP A 32 1385 6651 1978 -1138 713 -768 C ATOM 250 OD1 ASP A 32 49.261 18.561 -10.012 1.00 28.52 O ANISOU 250 OD1 ASP A 32 1849 6745 2241 -32 129 -1062 O ATOM 251 OD2 ASP A 32 49.853 20.645 -10.420 1.00 34.00 O ANISOU 251 OD2 ASP A 32 2111 8096 2711 -1085 1149 498 O ATOM 252 N LEU A 33 46.016 19.649 -6.202 1.00 10.95 N ANISOU 252 N LEU A 33 962 2366 831 -73 72 -52 N ATOM 253 CA LEU A 33 45.249 20.130 -5.072 1.00 10.51 C ANISOU 253 CA LEU A 33 913 2204 874 -28 170 40 C ATOM 254 C LEU A 33 45.956 19.806 -3.782 1.00 9.77 C ANISOU 254 C LEU A 33 895 1923 895 278 183 -80 C ATOM 255 O LEU A 33 46.400 18.700 -3.598 1.00 11.45 O ANISOU 255 O LEU A 33 1121 1945 1285 206 121 -78 O ATOM 256 CB LEU A 33 43.864 19.487 -5.090 1.00 11.06 C ANISOU 256 CB LEU A 33 1005 2143 1052 -60 101 162 C ATOM 257 CG LEU A 33 43.028 19.811 -6.332 1.00 11.70 C ANISOU 257 CG LEU A 33 1026 2251 1170 -36 -67 -26 C ATOM 258 CD1 LEU A 33 41.728 18.991 -6.269 1.00 13.55 C ANISOU 258 CD1 LEU A 33 994 2626 1528 -140 68 -253 C ATOM 259 CD2 LEU A 33 42.689 21.278 -6.477 1.00 14.30 C ANISOU 259 CD2 LEU A 33 1594 2277 1561 146 -491 11 C ATOM 260 N PRO A 34 46.083 20.734 -2.832 1.00 9.33 N ANISOU 260 N PRO A 34 844 1760 941 9 80 161 N ATOM 261 CA PRO A 34 46.841 20.428 -1.610 1.00 9.14 C ANISOU 261 CA PRO A 34 767 1814 892 -120 106 70 C ATOM 262 C PRO A 34 46.100 19.529 -0.670 1.00 8.04 C ANISOU 262 C PRO A 34 632 1531 892 110 174 -31 C ATOM 263 O PRO A 34 44.910 19.747 -0.392 1.00 9.25 O ANISOU 263 O PRO A 34 619 1863 1034 41 107 154 O ATOM 264 CB PRO A 34 47.038 21.805 -0.977 1.00 10.28 C ANISOU 264 CB PRO A 34 916 1653 1338 -109 120 75 C ATOM 265 CG PRO A 34 45.860 22.619 -1.492 1.00 11.34 C ANISOU 265 CG PRO A 34 1387 1940 980 161 18 136 C ATOM 266 CD PRO A 34 45.595 22.125 -2.886 1.00 9.52 C ANISOU 266 CD PRO A 34 958 1616 1045 -89 227 107 C ATOM 267 N LEU A 35 46.804 18.552 -0.140 1.00 9.11 N ANISOU 267 N LEU A 35 811 1603 1048 60 -2 136 N ATOM 268 CA LEU A 35 46.277 17.609 0.796 1.00 9.55 C ANISOU 268 CA LEU A 35 686 1716 1226 -26 34 196 C ATOM 269 C LEU A 35 47.331 17.326 1.864 1.00 8.87 C ANISOU 269 C LEU A 35 577 1654 1141 144 161 265 C ATOM 270 O LEU A 35 48.514 17.360 1.587 1.00 9.93 O ANISOU 270 O LEU A 35 564 1914 1295 -21 108 265 O ATOM 271 CB LEU A 35 45.910 16.272 0.159 1.00 10.83 C ANISOU 271 CB LEU A 35 900 1730 1486 -100 186 57 C ATOM 272 CG LEU A 35 44.816 16.332 -0.929 1.00 12.34 C ANISOU 272 CG LEU A 35 816 2152 1719 -79 -25 -360 C ATOM 273 CD1ALEU A 35 44.800 15.043 -1.750 0.50 14.42 C ANISOU 273 CD1ALEU A 35 1490 2046 1945 -89 -37 -394 C ATOM 274 CD1BLEU A 35 43.668 17.274 -0.582 0.50 39.71 C ANISOU 274 CD1BLEU A 35 3239 7075 4774 3442 -1682 -2353 C ATOM 275 CD2ALEU A 35 43.473 16.584 -0.286 0.50 15.20 C ANISOU 275 CD2ALEU A 35 753 2602 2419 -493 346 -523 C ATOM 276 CD2BLEU A 35 45.488 16.468 -2.242 0.50 40.11 C ANISOU 276 CD2BLEU A 35 3999 9619 1623 765 489 1028 C ATOM 277 N SER A 36 46.893 16.906 3.041 1.00 10.72 N ANISOU 277 N SER A 36 636 2163 1274 168 269 436 N ATOM 278 CA SER A 36 47.770 16.454 4.108 1.00 12.13 C ANISOU 278 CA SER A 36 814 2419 1375 351 265 727 C ATOM 279 C SER A 36 47.154 15.206 4.759 1.00 11.78 C ANISOU 279 C SER A 36 668 2274 1535 292 86 561 C ATOM 280 O SER A 36 47.583 14.084 4.475 1.00 15.17 O ANISOU 280 O SER A 36 1299 2308 2158 372 586 531 O ATOM 281 CB SER A 36 48.010 17.524 5.204 1.00 15.59 C ANISOU 281 CB SER A 36 1448 2641 1834 -141 -414 490 C ATOM 282 OG ASER A 36 48.884 17.005 6.202 0.50 20.96 O ANISOU 282 OG ASER A 36 1969 3843 2150 302 -657 455 O ATOM 283 OG BSER A 36 48.479 18.756 4.724 0.50 36.47 O ANISOU 283 OG BSER A 36 5650 3110 5097 -1568 1487 34 O ATOM 284 N CYS A 37 46.180 15.368 5.633 1.00 12.03 N ANISOU 284 N CYS A 37 659 2253 1659 200 230 647 N ATOM 285 CA CYS A 37 45.607 14.245 6.363 1.00 12.97 C ANISOU 285 CA CYS A 37 926 2252 1750 232 228 751 C ATOM 286 C CYS A 37 44.644 13.387 5.542 1.00 12.85 C ANISOU 286 C CYS A 37 856 1912 2113 290 266 766 C ATOM 287 O CYS A 37 44.471 12.218 5.833 1.00 15.03 O ANISOU 287 O CYS A 37 1435 1849 2427 418 505 579 O ATOM 288 CB CYS A 37 44.933 14.731 7.659 1.00 13.27 C ANISOU 288 CB CYS A 37 940 2355 1745 269 355 908 C ATOM 289 SG CYS A 37 43.320 15.519 7.387 1.00 12.13 S ANISOU 289 SG CYS A 37 945 2217 1446 209 240 545 S ATOM 290 N GLN A 38 44.011 13.972 4.520 1.00 12.36 N ANISOU 290 N GLN A 38 994 1941 1761 269 174 373 N ATOM 291 CA GLN A 38 43.000 13.350 3.680 1.00 13.23 C ANISOU 291 CA GLN A 38 980 1947 2102 175 270 -16 C ATOM 292 C GLN A 38 41.803 12.802 4.454 1.00 14.73 C ANISOU 292 C GLN A 38 1223 1701 2674 180 479 172 C ATOM 293 O GLN A 38 41.069 11.939 3.924 1.00 18.26 O ANISOU 293 O GLN A 38 1474 1977 3488 -155 584 -139 O ATOM 294 CB GLN A 38 43.574 12.205 2.824 1.00 16.34 C ANISOU 294 CB GLN A 38 1855 1973 2382 3 707 -67 C ATOM 295 CG GLN A 38 44.762 12.652 1.958 1.00 18.76 C ANISOU 295 CG GLN A 38 1581 3129 2420 98 765 -129 C ATOM 296 CD GLN A 38 45.215 11.435 1.157 1.00 23.08 C ANISOU 296 CD GLN A 38 2100 3911 2758 681 591 -609 C ATOM 297 OE1 GLN A 38 44.774 11.225 0.029 1.00 22.70 O ANISOU 297 OE1 GLN A 38 2598 3004 3025 0 366 -505 O ATOM 298 NE2 GLN A 38 46.104 10.616 1.736 1.00 26.89 N ANISOU 298 NE2 GLN A 38 2761 3662 3793 949 -234 -1202 N ATOM 299 N ALA A 39 41.564 13.313 5.653 1.00 13.38 N ANISOU 299 N ALA A 39 1103 1826 2153 366 347 704 N ATOM 300 CA ALA A 39 40.584 12.719 6.555 1.00 15.53 C ANISOU 300 CA ALA A 39 1134 1856 2911 177 605 801 C ATOM 301 C ALA A 39 39.684 13.749 7.217 1.00 14.14 C ANISOU 301 C ALA A 39 1059 2052 2260 110 372 603 C ATOM 302 O ALA A 39 38.894 13.425 8.092 1.00 20.17 O ANISOU 302 O ALA A 39 2001 2600 3062 301 1240 988 O ATOM 303 CB ALA A 39 41.335 11.974 7.653 1.00 22.55 C ANISOU 303 CB ALA A 39 1849 3218 3501 1016 1278 2032 C ATOM 304 N GLY A 40 39.758 14.993 6.810 1.00 12.44 N ANISOU 304 N GLY A 40 940 1962 1826 236 201 362 N ATOM 305 CA GLY A 40 38.862 15.989 7.378 1.00 12.36 C ANISOU 305 CA GLY A 40 709 2248 1741 319 29 186 C ATOM 306 C GLY A 40 39.306 16.561 8.713 1.00 11.65 C ANISOU 306 C GLY A 40 787 2411 1228 160 347 561 C ATOM 307 O GLY A 40 38.476 17.192 9.360 1.00 13.45 O ANISOU 307 O GLY A 40 954 2660 1498 271 314 285 O ATOM 308 N ALA A 41 40.577 16.393 9.068 1.00 12.30 N ANISOU 308 N ALA A 41 864 2421 1388 216 120 500 N ATOM 309 CA ALA A 41 41.047 16.795 10.391 1.00 13.09 C ANISOU 309 CA ALA A 41 932 2789 1253 290 198 693 C ATOM 310 C ALA A 41 42.072 17.878 10.371 1.00 12.25 C ANISOU 310 C ALA A 41 1071 2516 1067 315 71 425 C ATOM 311 O ALA A 41 42.755 18.126 11.378 1.00 21.41 O ANISOU 311 O ALA A 41 2365 4427 1342 -934 -521 1026 O ATOM 312 CB ALA A 41 41.626 15.510 11.063 1.00 16.66 C ANISOU 312 CB ALA A 41 1989 2662 1681 424 97 855 C ATOM 313 N CYS A 42 42.258 18.577 9.264 1.00 11.95 N ANISOU 313 N CYS A 42 1009 2545 988 239 209 327 N ATOM 314 CA CYS A 42 43.193 19.689 9.203 1.00 12.30 C ANISOU 314 CA CYS A 42 1366 2339 970 193 61 233 C ATOM 315 C CYS A 42 42.560 20.734 8.277 1.00 13.19 C ANISOU 315 C CYS A 42 1559 2158 1295 556 83 50 C ATOM 316 O CYS A 42 41.351 20.711 7.992 1.00 16.81 O ANISOU 316 O CYS A 42 1792 2805 1790 558 -280 406 O ATOM 317 CB CYS A 42 44.601 19.222 8.817 1.00 11.58 C ANISOU 317 CB CYS A 42 1090 2226 1084 27 -173 193 C ATOM 318 SG CYS A 42 44.907 18.889 7.049 1.00 11.01 S ANISOU 318 SG CYS A 42 912 2086 1186 124 145 256 S ATOM 319 N SER A 43 43.297 21.701 7.842 1.00 14.92 N ANISOU 319 N SER A 43 1886 2457 1325 697 329 450 N ATOM 320 CA SER A 43 42.724 22.688 6.935 1.00 12.73 C ANISOU 320 CA SER A 43 1462 2407 969 755 193 182 C ATOM 321 C SER A 43 43.558 22.743 5.664 1.00 10.59 C ANISOU 321 C SER A 43 1065 2107 853 515 -8 -15 C ATOM 322 O SER A 43 43.375 23.690 4.888 1.00 10.73 O ANISOU 322 O SER A 43 954 2159 963 478 -61 40 O ATOM 323 CB SER A 43 42.669 24.077 7.594 1.00 15.39 C ANISOU 323 CB SER A 43 2209 2499 1139 898 504 45 C ATOM 324 OG SER A 43 44.009 24.386 8.065 1.00 18.05 O ANISOU 324 OG SER A 43 2934 2682 1242 -27 -51 211 O ATOM 325 N THR A 44 44.464 21.785 5.419 1.00 9.43 N ANISOU 325 N THR A 44 839 1801 942 240 63 114 N ATOM 326 CA THR A 44 45.363 21.908 4.267 1.00 9.48 C ANISOU 326 CA THR A 44 706 1977 919 169 -4 124 C ATOM 327 C THR A 44 44.612 22.034 2.953 1.00 7.88 C ANISOU 327 C THR A 44 546 1546 904 76 65 28 C ATOM 328 O THR A 44 45.018 22.786 2.056 1.00 8.82 O ANISOU 328 O THR A 44 634 1739 978 -16 50 206 O ATOM 329 CB THR A 44 46.297 20.680 4.234 1.00 9.86 C ANISOU 329 CB THR A 44 682 2131 932 279 75 266 C ATOM 330 OG1 THR A 44 47.148 20.799 5.387 1.00 10.70 O ANISOU 330 OG1 THR A 44 685 2234 1145 198 -55 171 O ATOM 331 CG2 THR A 44 47.190 20.666 3.004 1.00 11.32 C ANISOU 331 CG2 THR A 44 1012 2068 1223 88 468 277 C ATOM 332 N CYS A 45 43.524 21.304 2.835 1.00 8.04 N ANISOU 332 N CYS A 45 613 1575 865 33 75 65 N ATOM 333 CA CYS A 45 42.740 21.218 1.590 1.00 7.51 C ANISOU 333 CA CYS A 45 577 1427 849 28 58 72 C ATOM 334 C CYS A 45 41.636 22.238 1.543 1.00 7.36 C ANISOU 334 C CYS A 45 588 1446 764 49 134 102 C ATOM 335 O CYS A 45 40.731 22.151 0.687 1.00 8.25 O ANISOU 335 O CYS A 45 726 1563 845 107 19 117 O ATOM 336 CB CYS A 45 42.161 19.790 1.496 1.00 8.10 C ANISOU 336 CB CYS A 45 641 1450 988 -51 268 -6 C ATOM 337 SG CYS A 45 40.889 19.542 2.788 1.00 8.50 S ANISOU 337 SG CYS A 45 607 1613 1009 70 114 161 S ATOM 338 N LEU A 46 41.656 23.263 2.403 1.00 7.58 N ANISOU 338 N LEU A 46 624 1443 815 29 181 147 N ATOM 339 CA LEU A 46 40.523 24.190 2.492 1.00 7.61 C ANISOU 339 CA LEU A 46 725 1496 671 129 98 57 C ATOM 340 C LEU A 46 40.188 24.825 1.145 1.00 7.08 C ANISOU 340 C LEU A 46 591 1416 682 -134 66 82 C ATOM 341 O LEU A 46 41.075 25.258 0.396 1.00 7.68 O ANISOU 341 O LEU A 46 583 1564 771 -115 113 110 O ATOM 342 CB LEU A 46 40.899 25.303 3.480 1.00 8.48 C ANISOU 342 CB LEU A 46 795 1682 744 77 -34 -83 C ATOM 343 CG LEU A 46 39.690 26.145 3.963 1.00 8.88 C ANISOU 343 CG LEU A 46 840 1497 1035 187 17 33 C ATOM 344 CD1 LEU A 46 38.780 25.317 4.856 1.00 9.91 C ANISOU 344 CD1 LEU A 46 858 1903 1005 -28 100 -103 C ATOM 345 CD2 LEU A 46 40.198 27.387 4.693 1.00 10.78 C ANISOU 345 CD2 LEU A 46 967 1721 1410 115 150 -202 C ATOM 346 N GLY A 47 38.894 24.907 0.907 1.00 7.49 N ANISOU 346 N GLY A 47 558 1608 680 -59 30 44 N ATOM 347 CA GLY A 47 38.353 25.676 -0.218 1.00 7.74 C ANISOU 347 CA GLY A 47 659 1439 842 83 20 44 C ATOM 348 C GLY A 47 37.162 26.479 0.257 1.00 7.19 C ANISOU 348 C GLY A 47 645 1445 643 -89 8 4 C ATOM 349 O GLY A 47 36.805 26.434 1.449 1.00 7.75 O ANISOU 349 O GLY A 47 745 1576 625 -41 140 87 O ATOM 350 N LYS A 48 36.520 27.189 -0.663 1.00 7.71 N ANISOU 350 N LYS A 48 509 1650 769 -17 69 208 N ATOM 351 CA LYS A 48 35.328 27.974 -0.362 1.00 8.30 C ANISOU 351 CA LYS A 48 628 1773 751 -4 57 11 C ATOM 352 C LYS A 48 34.295 27.685 -1.413 1.00 7.24 C ANISOU 352 C LYS A 48 628 1410 714 118 40 -29 C ATOM 353 O LYS A 48 34.559 27.797 -2.597 1.00 8.74 O ANISOU 353 O LYS A 48 759 1904 656 20 106 182 O ATOM 354 CB LYS A 48 35.637 29.483 -0.333 1.00 12.67 C ANISOU 354 CB LYS A 48 1021 1715 2078 -90 -135 -436 C ATOM 355 CG LYS A 48 34.533 30.193 0.479 1.00 27.59 C ANISOU 355 CG LYS A 48 2066 2294 6123 -275 1592 -1554 C ATOM 356 CD LYS A 48 34.917 31.644 0.741 1.00 36.49 C ANISOU 356 CD LYS A 48 3234 2651 7978 -624 1829 -2679 C ATOM 357 CE LYS A 48 34.115 32.294 1.828 1.00 37.80 C ANISOU 357 CE LYS A 48 3699 2876 7789 26 1697 -2444 C ATOM 358 NZ LYS A 48 34.811 33.277 2.691 1.00 39.03 N ANISOU 358 NZ LYS A 48 3889 5091 5850 -734 1815 -2375 N ATOM 359 N ILE A 49 33.093 27.303 -0.993 1.00 7.58 N ANISOU 359 N ILE A 49 548 1649 685 109 70 31 N ATOM 360 CA ILE A 49 32.015 27.017 -1.939 1.00 7.34 C ANISOU 360 CA ILE A 49 541 1553 695 37 40 39 C ATOM 361 C ILE A 49 31.423 28.331 -2.420 1.00 7.82 C ANISOU 361 C ILE A 49 629 1503 840 116 63 -27 C ATOM 362 O ILE A 49 30.979 29.131 -1.627 1.00 10.38 O ANISOU 362 O ILE A 49 1072 1669 1201 252 3 -217 O ATOM 363 CB ILE A 49 30.965 26.152 -1.301 1.00 8.81 C ANISOU 363 CB ILE A 49 513 1910 925 -79 -20 223 C ATOM 364 CG1 ILE A 49 31.483 24.847 -0.756 1.00 10.30 C ANISOU 364 CG1 ILE A 49 851 1808 1256 -104 58 298 C ATOM 365 CG2 ILE A 49 29.827 25.893 -2.320 1.00 10.15 C ANISOU 365 CG2 ILE A 49 674 2043 1140 -160 -105 -74 C ATOM 366 CD1 ILE A 49 30.565 24.209 0.290 1.00 11.99 C ANISOU 366 CD1 ILE A 49 1212 1839 1503 -114 265 409 C ATOM 367 N VAL A 50 31.386 28.492 -3.740 1.00 8.43 N ANISOU 367 N VAL A 50 742 1558 904 76 -132 145 N ATOM 368 CA VAL A 50 30.792 29.656 -4.383 1.00 9.77 C ANISOU 368 CA VAL A 50 890 1554 1267 -39 -334 288 C ATOM 369 C VAL A 50 29.330 29.393 -4.713 1.00 9.88 C ANISOU 369 C VAL A 50 918 1479 1356 110 -311 72 C ATOM 370 O VAL A 50 28.503 30.303 -4.628 1.00 15.54 O ANISOU 370 O VAL A 50 1155 1491 3257 281 -525 -35 O ATOM 371 CB VAL A 50 31.540 29.979 -5.712 1.00 14.15 C ANISOU 371 CB VAL A 50 1294 2460 1624 -212 -292 1029 C ATOM 372 CG1 VAL A 50 30.829 31.119 -6.417 1.00 17.26 C ANISOU 372 CG1 VAL A 50 1606 2690 2261 33 -22 1367 C ATOM 373 CG2 VAL A 50 32.998 30.301 -5.445 1.00 16.98 C ANISOU 373 CG2 VAL A 50 1206 2743 2504 -162 97 1267 C ATOM 374 N SER A 51 28.972 28.181 -5.103 1.00 8.81 N ANISOU 374 N SER A 51 842 1476 1031 -94 9 122 N ATOM 375 CA SER A 51 27.571 27.842 -5.410 1.00 9.97 C ANISOU 375 CA SER A 51 847 1551 1388 -75 -251 331 C ATOM 376 C SER A 51 27.409 26.339 -5.229 1.00 8.41 C ANISOU 376 C SER A 51 611 1558 1025 -23 -132 -48 C ATOM 377 O SER A 51 28.386 25.579 -5.383 1.00 8.91 O ANISOU 377 O SER A 51 687 1574 1125 -9 65 -62 O ATOM 378 CB SER A 51 27.179 28.307 -6.834 1.00 12.82 C ANISOU 378 CB SER A 51 1441 2282 1147 10 -143 324 C ATOM 379 OG SER A 51 27.948 27.665 -7.783 1.00 14.47 O ANISOU 379 OG SER A 51 1435 2567 1495 238 -204 74 O ATOM 380 N GLY A 52 26.185 25.936 -4.929 1.00 8.62 N ANISOU 380 N GLY A 52 689 1535 1052 -29 -13 101 N ATOM 381 CA GLY A 52 25.868 24.537 -4.754 1.00 9.22 C ANISOU 381 CA GLY A 52 940 1563 999 -122 5 75 C ATOM 382 C GLY A 52 26.074 24.051 -3.321 1.00 8.00 C ANISOU 382 C GLY A 52 676 1326 1038 61 -9 -67 C ATOM 383 O GLY A 52 26.325 24.818 -2.412 1.00 9.21 O ANISOU 383 O GLY A 52 1086 1362 1054 -114 -183 -104 O ATOM 384 N THR A 53 25.959 22.749 -3.164 1.00 9.64 N ANISOU 384 N THR A 53 1224 1307 1132 183 -122 -84 N ATOM 385 CA THR A 53 25.958 22.140 -1.839 1.00 12.18 C ANISOU 385 CA THR A 53 1743 1544 1343 333 -484 199 C ATOM 386 C THR A 53 26.828 20.906 -1.795 1.00 8.41 C ANISOU 386 C THR A 53 800 1397 999 -146 -5 118 C ATOM 387 O THR A 53 26.884 20.145 -2.794 1.00 9.91 O ANISOU 387 O THR A 53 1248 1512 1006 -158 -352 -50 O ATOM 388 CB THR A 53 24.495 21.745 -1.496 1.00 19.33 C ANISOU 388 CB THR A 53 1646 3320 2377 1153 1003 783 C ATOM 389 OG1ATHR A 53 24.448 21.174 -0.196 0.50 51.08 O ANISOU 389 OG1ATHR A 53 5667 10308 3435 -947 1134 3215 O ATOM 390 OG1BTHR A 53 23.584 22.814 -1.548 0.50 26.77 O ANISOU 390 OG1BTHR A 53 2626 3325 4222 1578 512 -76 O ATOM 391 CG2ATHR A 53 24.017 20.706 -2.472 0.50 22.62 C ANISOU 391 CG2ATHR A 53 1144 2517 4934 -355 219 1161 C ATOM 392 CG2BTHR A 53 24.462 21.146 -0.097 0.50 49.69 C ANISOU 392 CG2BTHR A 53 3691 10389 4802 1287 1214 4989 C ATOM 393 N VAL A 54 27.476 20.669 -0.689 1.00 8.57 N ANISOU 393 N VAL A 54 835 1494 926 32 -120 -26 N ATOM 394 CA VAL A 54 28.200 19.422 -0.438 1.00 8.74 C ANISOU 394 CA VAL A 54 563 1566 1191 29 54 182 C ATOM 395 C VAL A 54 27.786 18.848 0.905 1.00 9.10 C ANISOU 395 C VAL A 54 632 1601 1224 101 179 166 C ATOM 396 O VAL A 54 27.348 19.554 1.811 1.00 11.97 O ANISOU 396 O VAL A 54 1356 1924 1269 436 299 199 O ATOM 397 CB VAL A 54 29.746 19.560 -0.433 1.00 9.95 C ANISOU 397 CB VAL A 54 541 2161 1078 -86 156 34 C ATOM 398 CG1 VAL A 54 30.206 20.264 -1.718 1.00 10.37 C ANISOU 398 CG1 VAL A 54 818 1944 1180 -244 -19 232 C ATOM 399 CG2 VAL A 54 30.225 20.352 0.765 1.00 11.93 C ANISOU 399 CG2 VAL A 54 1040 2176 1316 -327 -102 -19 C ATOM 400 N ASP A 55 28.004 17.557 1.063 1.00 9.40 N ANISOU 400 N ASP A 55 646 1593 1334 -125 -79 213 N ATOM 401 CA ASP A 55 28.056 16.905 2.352 1.00 9.49 C ANISOU 401 CA ASP A 55 607 1657 1342 -126 10 274 C ATOM 402 C ASP A 55 29.528 16.801 2.758 1.00 8.80 C ANISOU 402 C ASP A 55 589 1767 987 -52 162 247 C ATOM 403 O ASP A 55 30.306 16.087 2.151 1.00 10.41 O ANISOU 403 O ASP A 55 695 2021 1240 94 131 75 O ATOM 404 CB ASP A 55 27.394 15.528 2.248 1.00 10.73 C ANISOU 404 CB ASP A 55 875 1715 1487 -231 -53 213 C ATOM 405 CG ASP A 55 27.458 14.742 3.525 1.00 11.08 C ANISOU 405 CG ASP A 55 942 1823 1444 -251 192 285 C ATOM 406 OD1 ASP A 55 27.991 15.234 4.525 1.00 13.34 O ANISOU 406 OD1 ASP A 55 1409 2161 1500 -404 -55 349 O ATOM 407 OD2 ASP A 55 26.910 13.605 3.521 1.00 12.96 O ANISOU 407 OD2 ASP A 55 1418 1742 1763 -244 196 253 O ATOM 408 N GLN A 56 29.900 17.524 3.817 1.00 9.17 N ANISOU 408 N GLN A 56 694 1657 1132 -62 7 260 N ATOM 409 CA GLN A 56 31.270 17.423 4.356 1.00 9.00 C ANISOU 409 CA GLN A 56 606 1587 1227 -41 85 174 C ATOM 410 C GLN A 56 31.182 17.042 5.838 1.00 10.24 C ANISOU 410 C GLN A 56 638 1959 1295 -140 -55 378 C ATOM 411 O GLN A 56 32.033 17.373 6.658 1.00 10.64 O ANISOU 411 O GLN A 56 906 1839 1297 -176 -69 458 O ATOM 412 CB GLN A 56 32.068 18.713 4.128 1.00 9.09 C ANISOU 412 CB GLN A 56 702 1565 1188 -48 209 105 C ATOM 413 CG GLN A 56 31.371 19.959 4.733 1.00 9.29 C ANISOU 413 CG GLN A 56 721 1598 1212 -54 162 12 C ATOM 414 CD GLN A 56 32.248 21.184 4.607 1.00 8.29 C ANISOU 414 CD GLN A 56 722 1513 914 48 219 208 C ATOM 415 OE1 GLN A 56 33.480 21.119 4.757 1.00 8.99 O ANISOU 415 OE1 GLN A 56 738 1535 1141 -5 141 318 O ATOM 416 NE2 GLN A 56 31.633 22.313 4.265 1.00 9.28 N ANISOU 416 NE2 GLN A 56 769 1670 1086 136 259 300 N ATOM 417 N SER A 57 30.133 16.275 6.169 1.00 10.93 N ANISOU 417 N SER A 57 862 2015 1275 -216 61 405 N ATOM 418 CA SER A 57 29.946 15.911 7.583 1.00 13.53 C ANISOU 418 CA SER A 57 930 2867 1343 -390 112 521 C ATOM 419 C SER A 57 31.019 14.948 8.105 1.00 14.74 C ANISOU 419 C SER A 57 1589 2363 1647 -531 -116 907 C ATOM 420 O SER A 57 31.111 14.835 9.323 1.00 19.45 O ANISOU 420 O SER A 57 1505 4063 1821 -500 -29 1388 O ATOM 421 CB SER A 57 28.514 15.326 7.688 1.00 17.25 C ANISOU 421 CB SER A 57 1294 3576 1683 -869 526 89 C ATOM 422 OG SER A 57 28.443 14.108 6.974 1.00 17.20 O ANISOU 422 OG SER A 57 1697 2887 1951 -963 153 691 O ATOM 423 N GLU A 58 31.821 14.348 7.237 1.00 14.96 N ANISOU 423 N GLU A 58 1372 2164 2148 -382 -247 709 N ATOM 424 CA GLU A 58 32.977 13.524 7.641 1.00 15.84 C ANISOU 424 CA GLU A 58 1733 2208 2077 -342 -563 702 C ATOM 425 C GLU A 58 34.058 14.411 8.289 1.00 14.53 C ANISOU 425 C GLU A 58 1395 2111 2015 -135 -294 559 C ATOM 426 O GLU A 58 34.860 13.887 9.036 1.00 17.62 O ANISOU 426 O GLU A 58 1834 2428 2432 -171 -757 606 O ATOM 427 CB GLU A 58 33.590 12.696 6.480 1.00 19.48 C ANISOU 427 CB GLU A 58 2599 1907 2894 -22 -494 212 C ATOM 428 CG AGLU A 58 34.727 11.803 6.931 0.50 34.17 C ANISOU 428 CG AGLU A 58 3385 4239 5358 1516 -1039 -333 C ATOM 429 CG BGLU A 58 32.562 11.708 5.851 0.50 36.31 C ANISOU 429 CG BGLU A 58 4755 3526 5513 -1188 -704 -1470 C ATOM 430 CD AGLU A 58 35.160 10.621 6.138 0.50 47.59 C ANISOU 430 CD AGLU A 58 5303 4688 8089 2685 -1452 -1270 C ATOM 431 CD BGLU A 58 33.167 10.789 4.815 0.50 42.92 C ANISOU 431 CD BGLU A 58 5225 4379 6702 -1087 -606 -2509 C ATOM 432 OE1AGLU A 58 34.457 9.988 5.297 0.50 61.34 O ANISOU 432 OE1AGLU A 58 8094 5895 9317 2245 -1972 -2975 O ATOM 433 OE1BGLU A 58 34.441 10.880 4.659 0.50 46.15 O ANISOU 433 OE1BGLU A 58 4955 4843 7739 1146 -311 670 O ATOM 434 OE2AGLU A 58 36.311 10.117 6.275 0.50 59.40 O ANISOU 434 OE2AGLU A 58 6189 4908 11471 3746 -917 -3 O ATOM 435 OE2BGLU A 58 32.568 9.992 4.024 0.50 49.38 O ANISOU 435 OE2BGLU A 58 9195 3907 5660 -274 -2778 -1715 O ATOM 436 N GLY A 59 34.068 15.719 7.982 1.00 13.05 N ANISOU 436 N GLY A 59 959 2150 1849 -265 -67 479 N ATOM 437 CA GLY A 59 35.079 16.617 8.542 1.00 12.02 C ANISOU 437 CA GLY A 59 916 2251 1398 -127 -68 421 C ATOM 438 C GLY A 59 34.914 16.939 10.002 1.00 11.57 C ANISOU 438 C GLY A 59 897 1882 1615 229 212 278 C ATOM 439 O GLY A 59 33.815 16.952 10.556 1.00 16.23 O ANISOU 439 O GLY A 59 992 2970 2203 41 505 166 O ATOM 440 N SER A 60 36.046 17.162 10.677 1.00 12.07 N ANISOU 440 N SER A 60 1126 2141 1318 -134 88 392 N ATOM 441 CA SER A 60 36.060 17.466 12.108 1.00 14.84 C ANISOU 441 CA SER A 60 1556 2785 1296 -235 259 495 C ATOM 442 C SER A 60 36.782 18.774 12.398 1.00 13.85 C ANISOU 442 C SER A 60 1420 2914 928 -156 -94 310 C ATOM 443 O SER A 60 36.821 19.252 13.538 1.00 21.00 O ANISOU 443 O SER A 60 1924 4947 1110 -1094 225 -299 O ATOM 444 CB SER A 60 36.661 16.278 12.896 1.00 18.09 C ANISOU 444 CB SER A 60 2349 3068 1455 30 -50 639 C ATOM 445 OG SER A 60 38.025 16.037 12.487 1.00 24.05 O ANISOU 445 OG SER A 60 2271 4122 2745 388 54 1837 O ATOM 446 N PHE A 61 37.406 19.439 11.438 1.00 11.59 N ANISOU 446 N PHE A 61 1082 2206 1117 273 -28 347 N ATOM 447 CA PHE A 61 38.254 20.598 11.725 1.00 11.39 C ANISOU 447 CA PHE A 61 962 2273 1092 316 213 133 C ATOM 448 C PHE A 61 37.492 21.892 11.794 1.00 10.75 C ANISOU 448 C PHE A 61 1068 2223 793 235 144 204 C ATOM 449 O PHE A 61 37.834 22.758 12.628 1.00 12.82 O ANISOU 449 O PHE A 61 1455 2448 968 404 -71 -13 O ATOM 450 CB PHE A 61 39.373 20.689 10.656 1.00 12.61 C ANISOU 450 CB PHE A 61 902 2669 1220 125 201 -169 C ATOM 451 CG PHE A 61 40.318 21.878 10.883 1.00 17.33 C ANISOU 451 CG PHE A 61 1402 3450 1733 -492 851 -715 C ATOM 452 CD1 PHE A 61 41.446 21.719 11.683 1.00 23.17 C ANISOU 452 CD1 PHE A 61 887 4662 3255 -633 597 -1503 C ATOM 453 CD2 PHE A 61 40.086 23.124 10.288 1.00 22.51 C ANISOU 453 CD2 PHE A 61 2818 3375 2360 -1291 1441 -200 C ATOM 454 CE1 PHE A 61 42.275 22.804 11.900 1.00 27.76 C ANISOU 454 CE1 PHE A 61 1841 5615 3090 -1736 1089 -1585 C ATOM 455 CE2 PHE A 61 40.871 24.235 10.524 1.00 26.11 C ANISOU 455 CE2 PHE A 61 3691 3743 2487 -1615 1855 -1287 C ATOM 456 CZ PHE A 61 41.990 24.028 11.326 1.00 31.46 C ANISOU 456 CZ PHE A 61 4219 5135 2598 -2102 1196 -1872 C ATOM 457 N LEU A 62 36.563 22.126 10.862 1.00 10.47 N ANISOU 457 N LEU A 62 907 2244 825 262 228 272 N ATOM 458 CA LEU A 62 35.925 23.452 10.785 1.00 10.01 C ANISOU 458 CA LEU A 62 1013 2055 736 182 193 139 C ATOM 459 C LEU A 62 34.934 23.670 11.915 1.00 9.52 C ANISOU 459 C LEU A 62 744 2075 797 150 95 178 C ATOM 460 O LEU A 62 34.242 22.766 12.376 1.00 13.14 O ANISOU 460 O LEU A 62 1406 2254 1333 3 726 125 O ATOM 461 CB LEU A 62 35.215 23.569 9.435 1.00 10.66 C ANISOU 461 CB LEU A 62 1025 2285 742 232 145 166 C ATOM 462 CG LEU A 62 36.157 23.584 8.249 1.00 11.63 C ANISOU 462 CG LEU A 62 1262 2439 717 85 276 -131 C ATOM 463 CD1 LEU A 62 35.341 23.708 6.934 1.00 12.49 C ANISOU 463 CD1 LEU A 62 1409 2613 724 466 314 2 C ATOM 464 CD2 LEU A 62 37.141 24.750 8.280 1.00 15.84 C ANISOU 464 CD2 LEU A 62 2007 2878 1132 -555 568 -37 C ATOM 465 N ASP A 63 34.838 24.920 12.355 1.00 9.89 N ANISOU 465 N ASP A 63 908 2141 709 187 78 80 N ATOM 466 CA ASP A 63 33.824 25.286 13.350 1.00 10.54 C ANISOU 466 CA ASP A 63 922 2369 714 301 46 -39 C ATOM 467 C ASP A 63 32.529 25.682 12.617 1.00 9.53 C ANISOU 467 C ASP A 63 873 2075 674 127 121 121 C ATOM 468 O ASP A 63 32.452 25.828 11.379 1.00 9.76 O ANISOU 468 O ASP A 63 956 2112 641 259 114 95 O ATOM 469 CB ASP A 63 34.361 26.354 14.272 1.00 12.64 C ANISOU 469 CB ASP A 63 1465 2524 815 266 -250 -128 C ATOM 470 CG ASP A 63 34.678 27.690 13.691 1.00 12.98 C ANISOU 470 CG ASP A 63 1585 2546 799 83 41 -265 C ATOM 471 OD1 ASP A 63 35.678 28.314 14.107 1.00 19.58 O ANISOU 471 OD1 ASP A 63 1868 3103 2470 -269 -585 204 O ATOM 472 OD2 ASP A 63 33.929 28.185 12.836 1.00 16.00 O ANISOU 472 OD2 ASP A 63 2304 2327 1450 -133 -512 81 O ATOM 473 N ASP A 64 31.453 25.855 13.379 1.00 11.13 N ANISOU 473 N ASP A 64 834 2561 832 182 140 41 N ATOM 474 CA ASP A 64 30.134 26.120 12.773 1.00 11.05 C ANISOU 474 CA ASP A 64 850 2516 831 285 82 73 C ATOM 475 C ASP A 64 30.185 27.380 11.947 1.00 11.13 C ANISOU 475 C ASP A 64 1013 2483 733 297 140 -13 C ATOM 476 O ASP A 64 29.578 27.438 10.868 1.00 12.63 O ANISOU 476 O ASP A 64 1132 2920 748 398 20 79 O ATOM 477 CB ASP A 64 29.078 26.273 13.863 1.00 13.42 C ANISOU 477 CB ASP A 64 964 3242 894 293 242 237 C ATOM 478 CG ASP A 64 28.686 25.030 14.602 1.00 13.66 C ANISOU 478 CG ASP A 64 1177 2967 1045 13 210 2 C ATOM 479 OD1 ASP A 64 29.073 23.897 14.226 1.00 16.51 O ANISOU 479 OD1 ASP A 64 1641 3043 1589 -139 306 -390 O ATOM 480 OD2 ASP A 64 27.977 25.199 15.634 1.00 15.78 O ANISOU 480 OD2 ASP A 64 1612 3017 1368 -114 627 16 O ATOM 481 N GLU A 65 30.849 28.444 12.426 1.00 11.96 N ANISOU 481 N GLU A 65 1489 2194 860 496 39 9 N ATOM 482 CA GLU A 65 30.876 29.719 11.662 1.00 13.19 C ANISOU 482 CA GLU A 65 2129 2067 816 790 205 -50 C ATOM 483 C GLU A 65 31.587 29.504 10.354 1.00 10.53 C ANISOU 483 C GLU A 65 1315 1823 863 424 17 -4 C ATOM 484 O GLU A 65 31.149 30.013 9.315 1.00 11.35 O ANISOU 484 O GLU A 65 1410 2148 754 549 5 -31 O ATOM 485 CB GLU A 65 31.597 30.806 12.492 1.00 16.84 C ANISOU 485 CB GLU A 65 3348 2105 945 397 181 -113 C ATOM 486 CG GLU A 65 31.609 32.148 11.686 1.00 20.60 C ANISOU 486 CG GLU A 65 4008 2275 1545 39 221 223 C ATOM 487 CD GLU A 65 32.099 33.308 12.503 1.00 31.45 C ANISOU 487 CD GLU A 65 7331 2525 2095 -808 -594 262 C ATOM 488 OE1 GLU A 65 33.065 33.135 13.290 1.00 44.45 O ANISOU 488 OE1 GLU A 65 8493 3896 4498 -1470 -2552 -190 O ATOM 489 OE2 GLU A 65 31.568 34.449 12.374 1.00 51.12 O ANISOU 489 OE2 GLU A 65 12606 2454 4364 207 -2869 -525 O ATOM 490 N GLN A 66 32.708 28.788 10.361 1.00 9.86 N ANISOU 490 N GLN A 66 912 1991 844 115 16 42 N ATOM 491 CA GLN A 66 33.427 28.561 9.094 1.00 9.22 C ANISOU 491 CA GLN A 66 960 1724 820 66 63 -110 C ATOM 492 C GLN A 66 32.560 27.776 8.119 1.00 8.77 C ANISOU 492 C GLN A 66 1013 1492 827 135 -121 134 C ATOM 493 O GLN A 66 32.528 28.075 6.932 1.00 9.11 O ANISOU 493 O GLN A 66 933 1808 721 333 -36 86 O ATOM 494 CB GLN A 66 34.716 27.798 9.434 1.00 10.05 C ANISOU 494 CB GLN A 66 788 2155 875 -20 -24 79 C ATOM 495 CG GLN A 66 35.721 28.681 10.143 1.00 12.50 C ANISOU 495 CG GLN A 66 1327 1937 1485 52 -459 -64 C ATOM 496 CD GLN A 66 36.852 27.936 10.797 1.00 11.19 C ANISOU 496 CD GLN A 66 874 2192 1188 -111 -112 203 C ATOM 497 OE1 GLN A 66 36.708 26.763 11.168 1.00 11.05 O ANISOU 497 OE1 GLN A 66 814 2256 1129 -12 -91 276 O ATOM 498 NE2 GLN A 66 37.991 28.596 10.987 1.00 16.83 N ANISOU 498 NE2 GLN A 66 1299 2605 2490 -445 -580 183 N ATOM 499 N ILE A 67 31.870 26.743 8.581 1.00 8.53 N ANISOU 499 N ILE A 67 937 1485 821 156 10 -59 N ATOM 500 CA ILE A 67 30.955 26.017 7.688 1.00 9.56 C ANISOU 500 CA ILE A 67 810 1671 1150 119 -234 -7 C ATOM 501 C ILE A 67 29.861 26.936 7.182 1.00 8.80 C ANISOU 501 C ILE A 67 962 1703 681 164 7 13 C ATOM 502 O ILE A 67 29.488 26.880 5.996 1.00 9.04 O ANISOU 502 O ILE A 67 790 1875 769 99 -85 11 O ATOM 503 CB ILE A 67 30.381 24.782 8.395 1.00 13.15 C ANISOU 503 CB ILE A 67 1100 1934 1962 -245 -610 483 C ATOM 504 CG1 ILE A 67 31.492 23.784 8.683 1.00 15.76 C ANISOU 504 CG1 ILE A 67 1902 1923 2162 293 -778 251 C ATOM 505 CG2 ILE A 67 29.279 24.149 7.521 1.00 14.42 C ANISOU 505 CG2 ILE A 67 1618 1924 1936 -411 -634 386 C ATOM 506 CD1AILE A 67 31.196 22.502 9.360 0.50 22.41 C ANISOU 506 CD1AILE A 67 2742 2310 3461 341 -102 897 C ATOM 507 CD1BILE A 67 31.877 22.987 7.463 0.50 31.22 C ANISOU 507 CD1BILE A 67 2777 5307 3778 1495 -1167 -1897 C ATOM 508 N GLU A 68 29.345 27.792 8.041 1.00 8.99 N ANISOU 508 N GLU A 68 918 1774 722 243 23 122 N ATOM 509 CA GLU A 68 28.252 28.709 7.673 1.00 9.82 C ANISOU 509 CA GLU A 68 962 2062 708 450 66 214 C ATOM 510 C GLU A 68 28.714 29.744 6.664 1.00 8.39 C ANISOU 510 C GLU A 68 930 1551 706 299 -9 -135 C ATOM 511 O GLU A 68 27.891 30.263 5.927 1.00 10.06 O ANISOU 511 O GLU A 68 939 1831 1052 412 -40 141 O ATOM 512 CB GLU A 68 27.680 29.382 8.942 1.00 11.79 C ANISOU 512 CB GLU A 68 1146 2461 872 571 181 170 C ATOM 513 CG GLU A 68 26.777 28.411 9.685 1.00 14.87 C ANISOU 513 CG GLU A 68 1278 3244 1130 490 349 628 C ATOM 514 CD GLU A 68 26.548 28.773 11.125 1.00 18.59 C ANISOU 514 CD GLU A 68 2070 3846 1146 1139 543 789 C ATOM 515 OE1 GLU A 68 26.890 29.900 11.526 1.00 24.83 O ANISOU 515 OE1 GLU A 68 2961 4855 1620 537 760 -439 O ATOM 516 OE2 GLU A 68 25.963 27.923 11.818 1.00 24.49 O ANISOU 516 OE2 GLU A 68 2899 4544 1864 1515 1125 1551 O ATOM 517 N GLN A 69 30.004 30.035 6.633 1.00 9.30 N ANISOU 517 N GLN A 69 898 1821 816 257 2 63 N ATOM 518 CA GLN A 69 30.543 30.984 5.667 1.00 9.58 C ANISOU 518 CA GLN A 69 991 1681 970 251 95 -7 C ATOM 519 C GLN A 69 30.850 30.335 4.320 1.00 8.73 C ANISOU 519 C GLN A 69 771 1685 860 344 87 116 C ATOM 520 O GLN A 69 31.252 31.012 3.385 1.00 11.41 O ANISOU 520 O GLN A 69 1502 1844 990 279 191 308 O ATOM 521 CB GLN A 69 31.834 31.597 6.233 1.00 12.21 C ANISOU 521 CB GLN A 69 1317 2068 1254 -97 -6 -118 C ATOM 522 CG GLN A 69 31.577 32.578 7.345 1.00 15.57 C ANISOU 522 CG GLN A 69 2185 2122 1610 -178 -88 -392 C ATOM 523 CD GLN A 69 32.831 32.970 8.098 1.00 22.19 C ANISOU 523 CD GLN A 69 2630 3434 2368 -446 -609 -888 C ATOM 524 OE1 GLN A 69 33.874 32.318 8.095 1.00 29.33 O ANISOU 524 OE1 GLN A 69 1554 5540 4051 -626 191 -2559 O ATOM 525 NE2 GLN A 69 32.678 34.094 8.770 1.00 28.64 N ANISOU 525 NE2 GLN A 69 3536 3075 4272 -379 -1565 -1228 N ATOM 526 N GLY A 70 30.708 29.008 4.220 1.00 8.75 N ANISOU 526 N GLY A 70 926 1675 725 360 -3 30 N ATOM 527 CA GLY A 70 30.919 28.320 2.947 1.00 9.92 C ANISOU 527 CA GLY A 70 1197 1787 786 555 16 22 C ATOM 528 C GLY A 70 32.307 27.684 2.835 1.00 8.02 C ANISOU 528 C GLY A 70 844 1564 641 149 100 146 C ATOM 529 O GLY A 70 32.615 27.148 1.772 1.00 9.18 O ANISOU 529 O GLY A 70 965 1904 618 166 188 149 O ATOM 530 N TYR A 71 33.109 27.658 3.884 1.00 7.57 N ANISOU 530 N TYR A 71 818 1346 714 240 135 -19 N ATOM 531 CA TYR A 71 34.380 26.911 3.788 1.00 7.21 C ANISOU 531 CA TYR A 71 681 1353 704 101 148 29 C ATOM 532 C TYR A 71 34.130 25.430 3.675 1.00 6.97 C ANISOU 532 C TYR A 71 661 1294 693 129 169 176 C ATOM 533 O TYR A 71 33.122 24.902 4.184 1.00 8.02 O ANISOU 533 O TYR A 71 772 1439 837 89 301 165 O ATOM 534 CB TYR A 71 35.273 27.250 4.986 1.00 8.85 C ANISOU 534 CB TYR A 71 761 1590 1010 89 -27 -48 C ATOM 535 CG TYR A 71 35.873 28.631 4.906 1.00 9.49 C ANISOU 535 CG TYR A 71 545 1689 1370 100 -50 -186 C ATOM 536 CD1 TYR A 71 35.517 29.632 5.795 1.00 12.34 C ANISOU 536 CD1 TYR A 71 1232 1591 1866 124 26 -358 C ATOM 537 CD2 TYR A 71 36.843 28.920 3.966 1.00 11.00 C ANISOU 537 CD2 TYR A 71 720 1821 1640 -78 29 1 C ATOM 538 CE1 TYR A 71 36.105 30.859 5.673 1.00 16.28 C ANISOU 538 CE1 TYR A 71 1688 1935 2564 -333 488 -658 C ATOM 539 CE2 TYR A 71 37.448 30.137 3.841 1.00 13.48 C ANISOU 539 CE2 TYR A 71 1104 1929 2090 -253 201 -134 C ATOM 540 CZ TYR A 71 37.058 31.125 4.726 1.00 15.71 C ANISOU 540 CZ TYR A 71 1690 1940 2341 -262 262 -289 C ATOM 541 OH TYR A 71 37.629 32.372 4.667 1.00 21.25 O ANISOU 541 OH TYR A 71 2319 2210 3546 -808 809 -711 O ATOM 542 N VAL A 72 35.050 24.712 3.062 1.00 7.14 N ANISOU 542 N VAL A 72 599 1410 705 47 131 -48 N ATOM 543 CA VAL A 72 34.874 23.294 2.777 1.00 7.49 C ANISOU 543 CA VAL A 72 590 1431 825 139 70 23 C ATOM 544 C VAL A 72 36.230 22.609 2.855 1.00 7.40 C ANISOU 544 C VAL A 72 550 1391 869 53 180 101 C ATOM 545 O VAL A 72 37.252 23.128 2.385 1.00 7.92 O ANISOU 545 O VAL A 72 546 1548 915 36 144 173 O ATOM 546 CB VAL A 72 34.189 23.085 1.396 1.00 7.92 C ANISOU 546 CB VAL A 72 709 1482 819 1 75 -81 C ATOM 547 CG1 VAL A 72 34.944 23.736 0.223 1.00 9.15 C ANISOU 547 CG1 VAL A 72 867 1736 872 30 151 106 C ATOM 548 CG2 VAL A 72 33.969 21.609 1.081 1.00 9.76 C ANISOU 548 CG2 VAL A 72 1093 1413 1201 -1 -31 -35 C ATOM 549 N LEU A 73 36.195 21.422 3.436 1.00 7.35 N ANISOU 549 N LEU A 73 597 1377 818 39 112 88 N ATOM 550 CA LEU A 73 37.358 20.505 3.395 1.00 7.99 C ANISOU 550 CA LEU A 73 662 1507 866 182 70 100 C ATOM 551 C LEU A 73 37.197 19.691 2.134 1.00 7.30 C ANISOU 551 C LEU A 73 462 1314 998 55 140 163 C ATOM 552 O LEU A 73 36.363 18.799 2.010 1.00 8.52 O ANISOU 552 O LEU A 73 634 1597 1005 -86 99 81 O ATOM 553 CB LEU A 73 37.467 19.658 4.642 1.00 9.14 C ANISOU 553 CB LEU A 73 859 1548 1067 90 142 247 C ATOM 554 CG LEU A 73 37.524 20.470 5.956 1.00 9.65 C ANISOU 554 CG LEU A 73 1051 1650 965 -7 99 93 C ATOM 555 CD1ALEU A 73 37.546 19.507 7.119 0.50 12.02 C ANISOU 555 CD1ALEU A 73 924 2385 1259 130 308 595 C ATOM 556 CD1BLEU A 73 36.192 20.688 6.304 0.50 41.95 C ANISOU 556 CD1BLEU A 73 2111 9522 4305 1701 1131 -2639 C ATOM 557 CD2ALEU A 73 38.689 21.412 5.934 0.50 10.26 C ANISOU 557 CD2ALEU A 73 745 1964 1190 -23 43 177 C ATOM 558 CD2BLEU A 73 38.136 19.639 7.107 0.50 37.01 C ANISOU 558 CD2BLEU A 73 7365 4517 2180 665 -2356 973 C ATOM 559 N THR A 74 37.991 20.045 1.112 1.00 7.60 N ANISOU 559 N THR A 74 592 1430 866 46 103 94 N ATOM 560 CA THR A 74 37.822 19.419 -0.213 1.00 8.08 C ANISOU 560 CA THR A 74 717 1480 871 32 13 45 C ATOM 561 C THR A 74 38.174 17.935 -0.184 1.00 8.24 C ANISOU 561 C THR A 74 655 1451 1023 65 99 50 C ATOM 562 O THR A 74 37.677 17.222 -1.080 1.00 9.88 O ANISOU 562 O THR A 74 944 1580 1230 -115 68 -120 O ATOM 563 CB THR A 74 38.630 20.139 -1.320 1.00 8.30 C ANISOU 563 CB THR A 74 662 1538 953 8 24 128 C ATOM 564 OG1 THR A 74 40.018 20.141 -1.014 1.00 8.55 O ANISOU 564 OG1 THR A 74 628 1536 1086 -20 129 7 O ATOM 565 CG2 THR A 74 38.126 21.576 -1.501 1.00 9.34 C ANISOU 565 CG2 THR A 74 878 1539 1134 82 54 194 C ATOM 566 N CYS A 75 38.981 17.454 0.778 1.00 8.32 N ANISOU 566 N CYS A 75 644 1460 1056 58 191 120 N ATOM 567 CA CYS A 75 39.377 16.033 0.730 1.00 9.54 C ANISOU 567 CA CYS A 75 713 1518 1392 128 133 183 C ATOM 568 C CYS A 75 38.227 15.095 1.080 1.00 9.28 C ANISOU 568 C CYS A 75 799 1260 1466 158 101 185 C ATOM 569 O CYS A 75 38.301 13.932 0.737 1.00 10.89 O ANISOU 569 O CYS A 75 816 1402 1921 154 223 -17 O ATOM 570 CB CYS A 75 40.539 15.780 1.677 1.00 10.91 C ANISOU 570 CB CYS A 75 714 1843 1588 296 30 87 C ATOM 571 SG CYS A 75 40.119 16.001 3.426 1.00 10.77 S ANISOU 571 SG CYS A 75 776 1886 1431 -64 -13 464 S ATOM 572 N ILE A 76 37.177 15.583 1.746 1.00 9.01 N ANISOU 572 N ILE A 76 729 1290 1405 20 77 103 N ATOM 573 CA ILE A 76 36.078 14.696 2.140 1.00 9.59 C ANISOU 573 CA ILE A 76 804 1412 1428 -32 146 237 C ATOM 574 C ILE A 76 34.739 15.148 1.587 1.00 10.36 C ANISOU 574 C ILE A 76 788 1617 1531 -91 113 283 C ATOM 575 O ILE A 76 33.710 14.518 1.800 1.00 12.86 O ANISOU 575 O ILE A 76 884 1749 2254 -235 -39 440 O ATOM 576 CB ILE A 76 36.055 14.403 3.676 1.00 11.20 C ANISOU 576 CB ILE A 76 970 1781 1504 5 144 325 C ATOM 577 CG1 ILE A 76 36.139 15.600 4.573 1.00 12.41 C ANISOU 577 CG1 ILE A 76 1024 2225 1468 -84 137 52 C ATOM 578 CG2 ILE A 76 37.215 13.468 3.960 1.00 13.50 C ANISOU 578 CG2 ILE A 76 1022 2179 1928 135 -103 609 C ATOM 579 CD1 ILE A 76 34.958 16.555 4.518 1.00 13.07 C ANISOU 579 CD1 ILE A 76 1167 1960 1839 -28 113 53 C ATOM 580 N ALA A 77 34.681 16.297 0.884 1.00 8.81 N ANISOU 580 N ALA A 77 667 1446 1235 -29 97 79 N ATOM 581 CA ALA A 77 33.417 16.809 0.421 1.00 8.71 C ANISOU 581 CA ALA A 77 613 1430 1266 -45 -1 -49 C ATOM 582 C ALA A 77 32.777 15.945 -0.638 1.00 8.40 C ANISOU 582 C ALA A 77 620 1281 1293 55 41 -22 C ATOM 583 O ALA A 77 33.413 15.565 -1.636 1.00 9.58 O ANISOU 583 O ALA A 77 744 1534 1360 -42 55 -112 O ATOM 584 CB ALA A 77 33.629 18.210 -0.174 1.00 10.10 C ANISOU 584 CB ALA A 77 845 1358 1636 -89 -169 16 C ATOM 585 N ILE A 78 31.459 15.696 -0.473 1.00 8.90 N ANISOU 585 N ILE A 78 600 1434 1346 15 -49 -5 N ATOM 586 CA ILE A 78 30.665 14.915 -1.418 1.00 9.38 C ANISOU 586 CA ILE A 78 671 1308 1584 -83 -54 -22 C ATOM 587 C ILE A 78 29.612 15.836 -2.046 1.00 8.45 C ANISOU 587 C ILE A 78 595 1352 1264 -122 48 -76 C ATOM 588 O ILE A 78 28.717 16.294 -1.335 1.00 9.04 O ANISOU 588 O ILE A 78 636 1494 1305 -48 115 -83 O ATOM 589 CB ILE A 78 29.978 13.733 -0.725 1.00 9.81 C ANISOU 589 CB ILE A 78 685 1392 1650 -13 102 39 C ATOM 590 CG1 ILE A 78 31.064 12.800 -0.129 1.00 10.92 C ANISOU 590 CG1 ILE A 78 902 1370 1878 -21 -55 154 C ATOM 591 CG2 ILE A 78 29.048 12.983 -1.669 1.00 10.80 C ANISOU 591 CG2 ILE A 78 781 1564 1758 -222 113 -86 C ATOM 592 CD1 ILE A 78 30.429 11.806 0.869 1.00 14.38 C ANISOU 592 CD1 ILE A 78 1311 1769 2384 -187 -40 620 C ATOM 593 N PRO A 79 29.694 16.162 -3.337 1.00 9.00 N ANISOU 593 N PRO A 79 756 1322 1340 -2 118 -49 N ATOM 594 CA PRO A 79 28.658 17.067 -3.895 1.00 9.24 C ANISOU 594 CA PRO A 79 727 1519 1263 -115 -59 36 C ATOM 595 C PRO A 79 27.274 16.495 -3.745 1.00 8.73 C ANISOU 595 C PRO A 79 783 1317 1217 -120 73 -103 C ATOM 596 O PRO A 79 27.042 15.305 -3.858 1.00 9.84 O ANISOU 596 O PRO A 79 809 1358 1572 -64 14 -308 O ATOM 597 CB PRO A 79 29.041 17.095 -5.403 1.00 11.31 C ANISOU 597 CB PRO A 79 883 2099 1314 -209 112 169 C ATOM 598 CG PRO A 79 30.523 16.847 -5.457 1.00 13.28 C ANISOU 598 CG PRO A 79 1058 2261 1726 224 323 433 C ATOM 599 CD PRO A 79 30.814 15.867 -4.282 1.00 10.45 C ANISOU 599 CD PRO A 79 907 1681 1382 -94 340 42 C ATOM 600 N GLU A 80 26.305 17.421 -3.540 1.00 8.60 N ANISOU 600 N GLU A 80 688 1278 1302 -192 7 -178 N ATOM 601 CA GLU A 80 24.880 17.109 -3.564 1.00 9.54 C ANISOU 601 CA GLU A 80 690 1422 1514 -195 -49 -111 C ATOM 602 C GLU A 80 24.156 17.954 -4.599 1.00 9.87 C ANISOU 602 C GLU A 80 779 1271 1701 -118 -87 -128 C ATOM 603 O GLU A 80 22.919 17.911 -4.652 1.00 10.82 O ANISOU 603 O GLU A 80 701 1815 1595 -106 -119 -79 O ATOM 604 CB GLU A 80 24.284 17.316 -2.164 1.00 10.20 C ANISOU 604 CB GLU A 80 876 1309 1692 -124 201 -109 C ATOM 605 CG GLU A 80 24.803 16.260 -1.196 1.00 11.18 C ANISOU 605 CG GLU A 80 1187 1419 1643 -130 -104 -62 C ATOM 606 CD GLU A 80 24.207 16.304 0.192 1.00 11.92 C ANISOU 606 CD GLU A 80 1262 1572 1696 -118 -142 -206 C ATOM 607 OE1 GLU A 80 23.665 17.374 0.572 1.00 15.03 O ANISOU 607 OE1 GLU A 80 1781 1767 2165 120 101 -326 O ATOM 608 OE2 GLU A 80 24.275 15.300 0.918 1.00 12.57 O ANISOU 608 OE2 GLU A 80 1154 1884 1738 -162 -40 6 O ATOM 609 N SER A 81 24.897 18.645 -5.413 1.00 9.96 N ANISOU 609 N SER A 81 948 1473 1364 -255 -210 -141 N ATOM 610 CA SER A 81 24.374 19.443 -6.560 1.00 9.97 C ANISOU 610 CA SER A 81 878 1546 1364 -226 -235 -91 C ATOM 611 C SER A 81 25.580 19.712 -7.430 1.00 9.88 C ANISOU 611 C SER A 81 959 1603 1190 -127 -228 -279 C ATOM 612 O SER A 81 26.723 19.436 -7.078 1.00 11.06 O ANISOU 612 O SER A 81 854 2021 1327 -75 -109 -298 O ATOM 613 CB SER A 81 23.730 20.743 -6.073 1.00 10.44 C ANISOU 613 CB SER A 81 851 1552 1562 -197 -143 -162 C ATOM 614 OG SER A 81 24.736 21.623 -5.551 1.00 11.59 O ANISOU 614 OG SER A 81 1351 1691 1362 -173 -283 -378 O ATOM 615 N ASP A 82 25.345 20.362 -8.577 1.00 10.99 N ANISOU 615 N ASP A 82 1043 2033 1101 -309 -202 -177 N ATOM 616 CA ASP A 82 26.465 21.007 -9.260 1.00 11.03 C ANISOU 616 CA ASP A 82 979 1997 1215 -243 -205 -157 C ATOM 617 C ASP A 82 27.076 21.993 -8.282 1.00 9.58 C ANISOU 617 C ASP A 82 856 1699 1083 -182 -62 -113 C ATOM 618 O ASP A 82 26.367 22.702 -7.554 1.00 10.44 O ANISOU 618 O ASP A 82 731 1861 1375 -112 -58 -126 O ATOM 619 CB ASP A 82 26.001 21.754 -10.516 1.00 12.79 C ANISOU 619 CB ASP A 82 1092 2789 981 -140 -57 0 C ATOM 620 CG ASP A 82 25.422 20.857 -11.564 1.00 14.32 C ANISOU 620 CG ASP A 82 1028 3172 1241 -222 -106 -249 C ATOM 621 OD1 ASP A 82 25.547 19.630 -11.503 1.00 16.57 O ANISOU 621 OD1 ASP A 82 1461 3221 1614 -142 -198 -513 O ATOM 622 OD2 ASP A 82 24.834 21.448 -12.501 1.00 19.90 O ANISOU 622 OD2 ASP A 82 2294 3807 1461 -182 -715 -184 O ATOM 623 N VAL A 83 28.406 22.047 -8.244 1.00 9.57 N ANISOU 623 N VAL A 83 788 1852 998 -257 28 -158 N ATOM 624 CA VAL A 83 29.054 22.893 -7.224 1.00 9.86 C ANISOU 624 CA VAL A 83 822 1995 930 -323 -11 -199 C ATOM 625 C VAL A 83 30.215 23.628 -7.865 1.00 9.63 C ANISOU 625 C VAL A 83 759 2009 890 -314 -30 -291 C ATOM 626 O VAL A 83 30.905 23.083 -8.756 1.00 12.48 O ANISOU 626 O VAL A 83 1159 2388 1193 -389 259 -453 O ATOM 627 CB VAL A 83 29.540 22.018 -6.052 1.00 11.97 C ANISOU 627 CB VAL A 83 1306 2057 1185 -99 -277 -2 C ATOM 628 CG1AVAL A 83 28.505 21.546 -5.112 0.50 16.90 C ANISOU 628 CG1AVAL A 83 1938 2555 1929 -382 2 673 C ATOM 629 CG1BVAL A 83 30.703 21.146 -6.475 0.50 25.06 C ANISOU 629 CG1BVAL A 83 3004 3860 2660 1704 -667 -632 C ATOM 630 CG2AVAL A 83 30.224 20.765 -6.596 0.50 24.54 C ANISOU 630 CG2AVAL A 83 3585 2207 3531 720 698 107 C ATOM 631 CG2BVAL A 83 29.913 22.792 -4.810 0.50 19.34 C ANISOU 631 CG2BVAL A 83 3501 2379 1467 118 -945 -110 C ATOM 632 N VAL A 84 30.480 24.834 -7.388 1.00 8.65 N ANISOU 632 N VAL A 84 615 1862 809 -204 -8 -32 N ATOM 633 CA VAL A 84 31.667 25.626 -7.773 1.00 8.64 C ANISOU 633 CA VAL A 84 801 1619 862 -248 -31 -61 C ATOM 634 C VAL A 84 32.431 25.890 -6.489 1.00 8.16 C ANISOU 634 C VAL A 84 707 1608 787 -282 60 -68 C ATOM 635 O VAL A 84 31.824 26.420 -5.531 1.00 8.64 O ANISOU 635 O VAL A 84 839 1666 778 -31 -33 -21 O ATOM 636 CB VAL A 84 31.265 26.921 -8.478 1.00 9.82 C ANISOU 636 CB VAL A 84 863 1875 993 -146 -46 117 C ATOM 637 CG1 VAL A 84 32.508 27.731 -8.836 1.00 11.61 C ANISOU 637 CG1 VAL A 84 1155 2075 1184 -340 154 424 C ATOM 638 CG2 VAL A 84 30.454 26.651 -9.749 1.00 11.49 C ANISOU 638 CG2 VAL A 84 1005 2348 1012 80 -66 18 C ATOM 639 N ILE A 85 33.717 25.531 -6.442 1.00 8.38 N ANISOU 639 N ILE A 85 705 1718 759 -217 33 38 N ATOM 640 CA ILE A 85 34.527 25.691 -5.234 1.00 7.97 C ANISOU 640 CA ILE A 85 676 1672 679 -72 147 52 C ATOM 641 C ILE A 85 35.832 26.399 -5.621 1.00 8.11 C ANISOU 641 C ILE A 85 599 1737 746 -47 108 68 C ATOM 642 O ILE A 85 36.467 25.952 -6.570 1.00 9.18 O ANISOU 642 O ILE A 85 832 1869 788 -111 278 -13 O ATOM 643 CB ILE A 85 34.836 24.332 -4.606 1.00 9.13 C ANISOU 643 CB ILE A 85 812 1645 1011 -48 67 136 C ATOM 644 CG1 ILE A 85 33.551 23.731 -4.055 1.00 10.49 C ANISOU 644 CG1 ILE A 85 971 1528 1486 1 350 154 C ATOM 645 CG2 ILE A 85 35.890 24.427 -3.510 1.00 11.24 C ANISOU 645 CG2 ILE A 85 1104 1955 1213 80 -211 143 C ATOM 646 CD1 ILE A 85 33.740 22.283 -3.649 1.00 12.29 C ANISOU 646 CD1 ILE A 85 1415 1531 1722 -45 425 214 C ATOM 647 N GLU A 86 36.189 27.433 -4.876 1.00 8.18 N ANISOU 647 N GLU A 86 649 1775 685 -107 -51 157 N ATOM 648 CA GLU A 86 37.507 28.022 -4.960 1.00 8.34 C ANISOU 648 CA GLU A 86 637 1794 736 -173 -22 161 C ATOM 649 C GLU A 86 38.487 27.242 -4.107 1.00 7.64 C ANISOU 649 C GLU A 86 506 1862 535 -182 97 144 C ATOM 650 O GLU A 86 38.216 27.050 -2.916 1.00 9.82 O ANISOU 650 O GLU A 86 664 2399 669 80 158 153 O ATOM 651 CB GLU A 86 37.471 29.479 -4.456 1.00 10.85 C ANISOU 651 CB GLU A 86 1046 1750 1326 -175 205 43 C ATOM 652 CG GLU A 86 36.590 30.379 -5.309 1.00 14.62 C ANISOU 652 CG GLU A 86 1490 1808 2259 -20 -82 223 C ATOM 653 CD GLU A 86 36.290 31.709 -4.647 1.00 22.64 C ANISOU 653 CD GLU A 86 3502 1847 3255 430 -798 -143 C ATOM 654 OE1 GLU A 86 35.973 32.648 -5.364 1.00 27.69 O ANISOU 654 OE1 GLU A 86 3205 2224 5092 626 792 1211 O ATOM 655 OE2 GLU A 86 36.370 31.761 -3.388 1.00 37.28 O ANISOU 655 OE2 GLU A 86 7102 3748 3313 1515 -818 -1217 O ATOM 656 N THR A 87 39.586 26.783 -4.672 1.00 8.44 N ANISOU 656 N THR A 87 578 1944 685 -106 84 128 N ATOM 657 CA THR A 87 40.521 25.936 -3.945 1.00 8.34 C ANISOU 657 CA THR A 87 529 1845 794 -126 15 104 C ATOM 658 C THR A 87 41.637 26.783 -3.349 1.00 8.00 C ANISOU 658 C THR A 87 558 1608 874 -102 106 177 C ATOM 659 O THR A 87 41.730 27.991 -3.572 1.00 9.53 O ANISOU 659 O THR A 87 974 1750 898 -211 -62 223 O ATOM 660 CB THR A 87 41.113 24.880 -4.865 1.00 9.02 C ANISOU 660 CB THR A 87 739 1812 877 -102 127 112 C ATOM 661 OG1 THR A 87 41.824 25.540 -5.917 1.00 10.45 O ANISOU 661 OG1 THR A 87 988 2273 711 23 142 142 O ATOM 662 CG2 THR A 87 40.015 24.023 -5.533 1.00 11.36 C ANISOU 662 CG2 THR A 87 1027 2015 1276 -110 -44 -210 C ATOM 663 N HIS A 88 42.509 26.138 -2.577 1.00 8.49 N ANISOU 663 N HIS A 88 587 1922 715 -94 -34 168 N ATOM 664 CA HIS A 88 43.746 26.804 -2.129 1.00 9.20 C ANISOU 664 CA HIS A 88 800 1842 852 -253 -43 108 C ATOM 665 C HIS A 88 43.430 27.986 -1.225 1.00 8.92 C ANISOU 665 C HIS A 88 667 1633 1091 -117 -32 175 C ATOM 666 O HIS A 88 44.051 29.061 -1.323 1.00 11.02 O ANISOU 666 O HIS A 88 1088 1906 1194 -447 -57 206 O ATOM 667 CB HIS A 88 44.692 27.223 -3.248 1.00 9.79 C ANISOU 667 CB HIS A 88 707 1999 1012 -198 11 186 C ATOM 668 CG HIS A 88 45.177 26.106 -4.104 1.00 9.98 C ANISOU 668 CG HIS A 88 748 2044 999 -135 145 340 C ATOM 669 ND1 HIS A 88 44.393 25.474 -5.063 1.00 10.25 N ANISOU 669 ND1 HIS A 88 878 1967 1050 -22 101 172 N ATOM 670 CD2 HIS A 88 46.424 25.530 -4.171 1.00 11.23 C ANISOU 670 CD2 HIS A 88 699 2363 1204 -140 335 346 C ATOM 671 CE1 HIS A 88 45.156 24.562 -5.647 1.00 11.09 C ANISOU 671 CE1 HIS A 88 909 2074 1231 67 241 242 C ATOM 672 NE2 HIS A 88 46.370 24.572 -5.146 1.00 11.49 N ANISOU 672 NE2 HIS A 88 892 2250 1225 51 239 322 N ATOM 673 N LYS A 89 42.483 27.786 -0.289 1.00 9.14 N ANISOU 673 N LYS A 89 747 1724 1001 -124 -9 91 N ATOM 674 CA LYS A 89 42.035 28.877 0.567 1.00 9.89 C ANISOU 674 CA LYS A 89 825 1768 1166 -8 -47 -21 C ATOM 675 C LYS A 89 42.577 28.834 1.993 1.00 9.78 C ANISOU 675 C LYS A 89 776 1719 1221 -7 -43 -119 C ATOM 676 O LYS A 89 42.187 29.679 2.805 1.00 11.38 O ANISOU 676 O LYS A 89 1146 1913 1267 -114 79 -212 O ATOM 677 CB LYS A 89 40.494 28.925 0.616 1.00 11.10 C ANISOU 677 CB LYS A 89 840 1845 1533 32 -90 -97 C ATOM 678 CG LYS A 89 39.869 29.292 -0.720 1.00 14.25 C ANISOU 678 CG LYS A 89 1222 2262 1930 209 -576 -290 C ATOM 679 CD LYS A 89 40.091 30.764 -1.046 1.00 24.70 C ANISOU 679 CD LYS A 89 3813 2825 2748 -399 -1251 956 C ATOM 680 CE LYS A 89 40.565 31.078 -2.418 1.00 31.26 C ANISOU 680 CE LYS A 89 5517 2839 3519 -661 486 245 C ATOM 681 NZ LYS A 89 40.727 32.563 -2.571 1.00 34.65 N ANISOU 681 NZ LYS A 89 6543 2855 3766 -200 1323 732 N ATOM 682 N GLU A 90 43.471 27.902 2.350 1.00 9.87 N ANISOU 682 N GLU A 90 790 1964 998 -58 -15 100 N ATOM 683 CA GLU A 90 43.910 27.840 3.751 1.00 11.03 C ANISOU 683 CA GLU A 90 1119 1893 1180 45 -281 -44 C ATOM 684 C GLU A 90 44.513 29.140 4.257 1.00 13.00 C ANISOU 684 C GLU A 90 1691 1908 1342 54 -196 -174 C ATOM 685 O GLU A 90 44.319 29.433 5.456 1.00 16.48 O ANISOU 685 O GLU A 90 2708 2348 1205 -77 -580 -251 O ATOM 686 CB GLU A 90 44.928 26.684 3.845 1.00 10.59 C ANISOU 686 CB GLU A 90 1060 1954 1009 147 -69 -82 C ATOM 687 CG GLU A 90 45.261 26.460 5.351 1.00 13.20 C ANISOU 687 CG GLU A 90 1854 1907 1253 12 -551 32 C ATOM 688 CD GLU A 90 46.279 25.383 5.549 1.00 15.17 C ANISOU 688 CD GLU A 90 1673 2208 1885 61 -619 244 C ATOM 689 OE1 GLU A 90 47.145 25.130 4.705 1.00 17.55 O ANISOU 689 OE1 GLU A 90 1653 2662 2352 114 -520 -258 O ATOM 690 OE2 GLU A 90 46.217 24.707 6.610 1.00 20.62 O ANISOU 690 OE2 GLU A 90 2858 2757 2219 274 -755 737 O ATOM 691 N ASP A 91 45.132 29.935 3.407 1.00 12.72 N ANISOU 691 N ASP A 91 1274 1902 1656 -117 -311 -142 N ATOM 692 CA ASP A 91 45.694 31.215 3.893 1.00 16.43 C ANISOU 692 CA ASP A 91 1444 2180 2618 -281 -210 -663 C ATOM 693 C ASP A 91 44.640 32.191 4.325 1.00 16.64 C ANISOU 693 C ASP A 91 1832 2464 2028 16 -608 -930 C ATOM 694 O ASP A 91 45.047 33.207 4.865 1.00 23.47 O ANISOU 694 O ASP A 91 2864 2294 3761 -212 -548 -1229 O ATOM 695 CB ASP A 91 46.587 31.802 2.801 1.00 21.29 C ANISOU 695 CB ASP A 91 2568 1936 3586 -523 622 -436 C ATOM 696 CG ASP A 91 45.962 32.256 1.509 1.00 28.61 C ANISOU 696 CG ASP A 91 4164 3486 3221 -903 572 19 C ATOM 697 OD1 ASP A 91 44.744 32.032 1.261 1.00 23.00 O ANISOU 697 OD1 ASP A 91 3609 2624 2508 508 737 397 O ATOM 698 OD2 ASP A 91 46.681 32.884 0.676 1.00 41.31 O ANISOU 698 OD2 ASP A 91 5427 5367 4903 -2670 -114 1725 O ATOM 699 N GLU A 92 43.342 31.950 4.135 1.00 14.71 N ANISOU 699 N GLU A 92 1612 2124 1852 84 -75 -21 N ATOM 700 CA GLU A 92 42.406 32.889 4.691 1.00 18.08 C ANISOU 700 CA GLU A 92 2203 2388 2280 268 432 -108 C ATOM 701 C GLU A 92 42.106 32.662 6.160 1.00 21.51 C ANISOU 701 C GLU A 92 3180 2762 2232 256 560 -161 C ATOM 702 O GLU A 92 41.470 33.488 6.786 1.00 25.40 O ANISOU 702 O GLU A 92 4537 2491 2623 -31 1093 -592 O ATOM 703 CB GLU A 92 41.020 32.703 4.029 1.00 20.09 C ANISOU 703 CB GLU A 92 2060 2880 2693 883 348 2 C ATOM 704 CG GLU A 92 41.190 33.102 2.611 1.00 18.14 C ANISOU 704 CG GLU A 92 2089 2125 2678 313 149 0 C ATOM 705 CD GLU A 92 39.868 33.261 1.877 1.00 19.11 C ANISOU 705 CD GLU A 92 2072 2198 2990 68 125 533 C ATOM 706 OE1 GLU A 92 40.061 33.789 0.773 1.00 21.14 O ANISOU 706 OE1 GLU A 92 3310 2338 2384 167 10 111 O ATOM 707 OE2 GLU A 92 38.824 32.854 2.402 1.00 24.04 O ANISOU 707 OE2 GLU A 92 2139 2945 4049 -379 180 491 O ATOM 708 N LEU A 93 42.494 31.506 6.690 1.00 26.61 N ANISOU 708 N LEU A 93 5223 2767 2122 508 592 -118 N ATOM 709 CA LEU A 93 42.108 31.327 8.109 1.00 38.86 C ANISOU 709 CA LEU A 93 8501 3946 2319 -936 945 365 C ATOM 710 C LEU A 93 42.979 32.143 9.035 1.00 44.53 C ANISOU 710 C LEU A 93 10359 4489 2070 -1122 1479 -996 C ATOM 711 O LEU A 93 43.757 33.015 8.677 1.00 54.01 O ANISOU 711 O LEU A 93 11525 5805 3190 -2831 186 -570 O ATOM 712 CB LEU A 93 42.190 29.849 8.457 1.00 41.59 C ANISOU 712 CB LEU A 93 10396 3785 1620 -601 949 -124 C ATOM 713 CG LEU A 93 41.254 28.852 7.818 1.00 38.66 C ANISOU 713 CG LEU A 93 9578 3426 1684 -110 1333 -407 C ATOM 714 CD1 LEU A 93 41.740 27.451 8.192 1.00 49.69 C ANISOU 714 CD1 LEU A 93 12699 3738 2441 -1230 -2230 1291 C ATOM 715 CD2 LEU A 93 39.793 28.998 8.216 1.00 48.38 C ANISOU 715 CD2 LEU A 93 10970 3968 3444 -2416 4911 -1596 C ATOM 716 OXT LEU A 93 43.273 32.305 10.124 1.00 50.02 O ANISOU 716 OXT LEU A 93 10486 6362 2157 -781 1480 -1534 O TER 717 LEU A 93 END