HEADER 3.10.20.30 1n62A01 ATOM 1 N LYS A 3 100.596 177.191 114.688 1.00 35.77 N ANISOU 1 N LYS A 3 3499 7265 2824 -1532 -753 239 N ATOM 2 CA LYS A 3 99.368 176.691 115.354 1.00 22.41 C ANISOU 2 CA LYS A 3 2605 2489 3420 -463 -220 394 C ATOM 3 C LYS A 3 98.122 177.124 114.618 1.00 21.14 C ANISOU 3 C LYS A 3 2958 2342 2730 -184 487 346 C ATOM 4 O LYS A 3 98.106 178.115 113.923 1.00 29.87 O ANISOU 4 O LYS A 3 3167 2919 5263 -948 -610 1627 O ATOM 5 CB LYS A 3 99.304 177.168 116.804 1.00 27.35 C ANISOU 5 CB LYS A 3 3149 3513 3727 -833 -498 326 C ATOM 6 CG LYS A 3 100.279 176.457 117.734 1.00 33.62 C ANISOU 6 CG LYS A 3 2664 4090 6018 -505 -1677 606 C ATOM 7 CD LYS A 3 100.056 176.868 119.175 1.00 36.62 C ANISOU 7 CD LYS A 3 2917 3057 7939 -30 -922 480 C ATOM 8 CE LYS A 3 100.985 176.132 120.120 1.00 33.91 C ANISOU 8 CE LYS A 3 3294 4697 4893 1451 -913 -1853 C ATOM 9 NZ LYS A 3 100.670 176.481 121.536 1.00 55.18 N ANISOU 9 NZ LYS A 3 3574 10607 6783 155 -802 -3226 N ATOM 10 N ALA A 4 97.094 176.313 114.721 1.00 16.79 N ANISOU 10 N ALA A 4 2316 1798 2265 -227 51 419 N ATOM 11 CA ALA A 4 95.811 176.545 114.105 1.00 16.64 C ANISOU 11 CA ALA A 4 2477 1712 2131 27 199 679 C ATOM 12 C ALA A 4 94.913 177.226 115.094 1.00 15.04 C ANISOU 12 C ALA A 4 2432 1300 1981 -159 313 186 C ATOM 13 O ALA A 4 94.819 176.836 116.241 1.00 17.05 O ANISOU 13 O ALA A 4 2725 1532 2220 38 126 361 O ATOM 14 CB ALA A 4 95.189 175.230 113.722 1.00 16.97 C ANISOU 14 CB ALA A 4 2635 1763 2049 173 133 562 C ATOM 15 N HIS A 5 94.093 178.121 114.574 1.00 16.36 N ANISOU 15 N HIS A 5 2355 1622 2239 175 86 535 N ATOM 16 CA HIS A 5 93.129 178.834 115.381 1.00 16.77 C ANISOU 16 CA HIS A 5 2141 1631 2599 66 -322 568 C ATOM 17 C HIS A 5 91.810 178.104 115.319 1.00 15.22 C ANISOU 17 C HIS A 5 2368 1456 1958 -10 -186 326 C ATOM 18 O HIS A 5 91.322 177.797 114.241 1.00 17.05 O ANISOU 18 O HIS A 5 2658 2097 1722 -70 -43 236 O ATOM 19 CB HIS A 5 92.960 180.223 114.806 1.00 18.82 C ANISOU 19 CB HIS A 5 2630 1846 2671 109 -340 370 C ATOM 20 CG HIS A 5 91.841 180.996 115.409 1.00 17.98 C ANISOU 20 CG HIS A 5 2383 1718 2730 -132 -299 518 C ATOM 21 ND1 HIS A 5 90.811 181.514 114.655 1.00 19.74 N ANISOU 21 ND1 HIS A 5 2494 2038 2967 236 -379 -127 N ATOM 22 CD2 HIS A 5 91.671 181.478 116.661 1.00 17.67 C ANISOU 22 CD2 HIS A 5 2561 2216 1932 96 -153 -32 C ATOM 23 CE1 HIS A 5 90.016 182.227 115.434 1.00 18.79 C ANISOU 23 CE1 HIS A 5 2570 1852 2714 269 -403 165 C ATOM 24 NE2 HIS A 5 90.512 182.216 116.659 1.00 18.82 N ANISOU 24 NE2 HIS A 5 2615 1981 2552 -110 -447 797 N ATOM 25 N ILE A 6 91.260 177.753 116.470 1.00 14.59 N ANISOU 25 N ILE A 6 2123 1611 1808 -20 -32 474 N ATOM 26 CA ILE A 6 89.964 177.088 116.488 1.00 13.50 C ANISOU 26 CA ILE A 6 2291 1191 1647 -164 -3 186 C ATOM 27 C ILE A 6 89.026 177.824 117.409 1.00 13.76 C ANISOU 27 C ILE A 6 2283 1564 1379 -100 -285 59 C ATOM 28 O ILE A 6 89.439 178.453 118.365 1.00 14.65 O ANISOU 28 O ILE A 6 2295 1462 1808 -157 -240 -125 O ATOM 29 CB ILE A 6 90.060 175.642 116.880 1.00 14.11 C ANISOU 29 CB ILE A 6 2363 1536 1463 -184 -38 -197 C ATOM 30 CG1 ILE A 6 90.620 175.449 118.297 1.00 15.16 C ANISOU 30 CG1 ILE A 6 2310 1515 1935 -91 49 309 C ATOM 31 CG2 ILE A 6 90.885 174.892 115.866 1.00 15.77 C ANISOU 31 CG2 ILE A 6 2352 1484 2154 -51 -315 -241 C ATOM 32 CD1 ILE A 6 90.613 173.982 118.763 1.00 16.72 C ANISOU 32 CD1 ILE A 6 2136 1867 2348 -31 -89 463 C ATOM 33 N GLU A 7 87.762 177.775 117.058 1.00 13.83 N ANISOU 33 N GLU A 7 2542 1174 1536 8 5 182 N ATOM 34 CA GLU A 7 86.704 178.265 117.890 1.00 13.41 C ANISOU 34 CA GLU A 7 2431 1292 1369 -241 -276 163 C ATOM 35 C GLU A 7 85.641 177.198 117.906 1.00 13.25 C ANISOU 35 C GLU A 7 2319 1231 1484 -52 -89 142 C ATOM 36 O GLU A 7 85.259 176.667 116.870 1.00 13.29 O ANISOU 36 O GLU A 7 2416 1282 1349 -148 -116 103 O ATOM 37 CB GLU A 7 86.138 179.579 117.332 1.00 14.59 C ANISOU 37 CB GLU A 7 2676 1250 1615 -211 -250 172 C ATOM 38 CG GLU A 7 87.045 180.771 117.519 1.00 16.49 C ANISOU 38 CG GLU A 7 2842 1420 2002 -127 -562 399 C ATOM 39 CD GLU A 7 86.435 182.047 116.978 1.00 18.27 C ANISOU 39 CD GLU A 7 3138 1685 2118 -93 254 278 C ATOM 40 OE1 GLU A 7 85.597 182.696 117.682 1.00 17.99 O ANISOU 40 OE1 GLU A 7 3458 1412 1965 -55 -299 320 O ATOM 41 OE2 GLU A 7 86.743 182.363 115.822 1.00 17.45 O ANISOU 41 OE2 GLU A 7 2615 1560 2453 78 -313 328 O ATOM 42 N LEU A 8 85.140 176.920 119.094 1.00 12.55 N ANISOU 42 N LEU A 8 2493 935 1341 15 -137 35 N ATOM 43 CA LEU A 8 84.178 175.870 119.235 1.00 13.24 C ANISOU 43 CA LEU A 8 2655 1071 1304 63 8 13 C ATOM 44 C LEU A 8 83.363 176.132 120.466 1.00 11.23 C ANISOU 44 C LEU A 8 2164 762 1341 76 -240 189 C ATOM 45 O LEU A 8 83.467 177.201 121.039 1.00 12.24 O ANISOU 45 O LEU A 8 2277 988 1386 -94 -115 60 O ATOM 46 CB LEU A 8 84.860 174.486 119.207 1.00 12.77 C ANISOU 46 CB LEU A 8 2097 1130 1624 -91 -93 115 C ATOM 47 CG LEU A 8 85.801 174.155 120.353 1.00 13.19 C ANISOU 47 CG LEU A 8 2233 1123 1653 15 -144 251 C ATOM 48 CD1 LEU A 8 85.913 172.639 120.442 1.00 16.22 C ANISOU 48 CD1 LEU A 8 3138 1115 1908 304 -68 414 C ATOM 49 CD2 LEU A 8 87.164 174.784 120.190 1.00 15.64 C ANISOU 49 CD2 LEU A 8 2612 1439 1889 20 -515 113 C ATOM 50 N THR A 9 82.549 175.177 120.864 1.00 12.75 N ANISOU 50 N THR A 9 2642 816 1387 -100 -49 236 N ATOM 51 CA THR A 9 81.744 175.322 122.052 1.00 12.91 C ANISOU 51 CA THR A 9 2451 1009 1444 -7 -261 211 C ATOM 52 C THR A 9 81.956 174.084 122.852 1.00 13.11 C ANISOU 52 C THR A 9 2531 1010 1439 -173 -174 209 C ATOM 53 O THR A 9 81.896 172.986 122.308 1.00 14.55 O ANISOU 53 O THR A 9 3260 991 1278 -165 -203 162 O ATOM 54 CB THR A 9 80.265 175.444 121.669 1.00 14.30 C ANISOU 54 CB THR A 9 2594 1050 1785 93 148 306 C ATOM 55 OG1 THR A 9 80.085 176.383 120.604 1.00 14.83 O ANISOU 55 OG1 THR A 9 2825 1096 1712 -46 -273 148 O ATOM 56 CG2 THR A 9 79.439 175.905 122.848 1.00 15.32 C ANISOU 56 CG2 THR A 9 2540 1544 1733 -46 229 204 C ATOM 57 N ILE A 10 82.281 174.254 124.119 1.00 11.97 N ANISOU 57 N ILE A 10 2386 903 1260 -93 -199 238 N ATOM 58 CA ILE A 10 82.471 173.127 124.973 1.00 12.03 C ANISOU 58 CA ILE A 10 2099 1098 1371 -32 -163 96 C ATOM 59 C ILE A 10 81.656 173.311 126.188 1.00 12.38 C ANISOU 59 C ILE A 10 2388 1013 1300 -52 -227 115 C ATOM 60 O ILE A 10 81.762 174.343 126.829 1.00 12.93 O ANISOU 60 O ILE A 10 2485 1177 1251 -60 17 89 O ATOM 61 CB ILE A 10 83.942 172.904 125.348 1.00 12.56 C ANISOU 61 CB ILE A 10 2459 1171 1142 -63 63 223 C ATOM 62 CG1 ILE A 10 84.828 172.753 124.103 1.00 13.51 C ANISOU 62 CG1 ILE A 10 2362 1300 1472 8 -127 230 C ATOM 63 CG2 ILE A 10 84.047 171.672 126.215 1.00 14.27 C ANISOU 63 CG2 ILE A 10 2486 1280 1652 48 -173 248 C ATOM 64 CD1 ILE A 10 86.275 172.547 124.425 1.00 16.04 C ANISOU 64 CD1 ILE A 10 2495 1650 1946 214 35 368 C ATOM 65 N ASN A 11 80.791 172.350 126.459 1.00 12.00 N ANISOU 65 N ASN A 11 2307 1026 1226 -74 -115 293 N ATOM 66 CA ASN A 11 79.865 172.437 127.556 1.00 12.70 C ANISOU 66 CA ASN A 11 2383 948 1491 -156 -89 250 C ATOM 67 C ASN A 11 79.040 173.712 127.546 1.00 13.51 C ANISOU 67 C ASN A 11 2511 1085 1536 -241 89 351 C ATOM 68 O ASN A 11 78.785 174.315 128.559 1.00 14.21 O ANISOU 68 O ASN A 11 2642 1264 1492 122 62 185 O ATOM 69 CB ASN A 11 80.616 172.246 128.845 1.00 13.85 C ANISOU 69 CB ASN A 11 2716 1118 1429 -27 -210 78 C ATOM 70 CG ASN A 11 81.286 170.919 128.877 1.00 12.83 C ANISOU 70 CG ASN A 11 2628 1041 1203 -219 -188 137 C ATOM 71 OD1 ASN A 11 80.751 169.968 128.345 1.00 13.43 O ANISOU 71 OD1 ASN A 11 2876 932 1292 -60 -263 157 O ATOM 72 ND2 ASN A 11 82.436 170.836 129.524 1.00 13.87 N ANISOU 72 ND2 ASN A 11 2348 1548 1370 -48 -296 65 N ATOM 73 N GLY A 12 78.695 174.141 126.351 1.00 13.49 N ANISOU 73 N GLY A 12 2433 1199 1491 -98 89 208 N ATOM 74 CA GLY A 12 77.824 175.280 126.175 1.00 14.66 C ANISOU 74 CA GLY A 12 2131 1164 2273 31 -23 480 C ATOM 75 C GLY A 12 78.564 176.599 126.167 1.00 14.16 C ANISOU 75 C GLY A 12 2825 1107 1448 263 52 163 C ATOM 76 O GLY A 12 77.927 177.631 125.967 1.00 16.45 O ANISOU 76 O GLY A 12 2818 1112 2318 109 -298 434 O ATOM 77 N HIS A 13 79.881 176.612 126.361 1.00 14.04 N ANISOU 77 N HIS A 13 2714 987 1634 104 215 199 N ATOM 78 CA HIS A 13 80.670 177.828 126.414 1.00 13.70 C ANISOU 78 CA HIS A 13 2870 1128 1206 -15 60 -17 C ATOM 79 C HIS A 13 81.511 177.967 125.206 1.00 13.20 C ANISOU 79 C HIS A 13 2700 863 1453 -161 -94 -49 C ATOM 80 O HIS A 13 82.182 177.035 124.825 1.00 13.29 O ANISOU 80 O HIS A 13 2547 927 1571 70 -65 63 O ATOM 81 CB HIS A 13 81.598 177.794 127.615 1.00 17.35 C ANISOU 81 CB HIS A 13 3833 1270 1490 -724 -73 -131 C ATOM 82 CG HIS A 13 80.884 177.582 128.894 1.00 22.78 C ANISOU 82 CG HIS A 13 4932 1800 1923 -579 570 -339 C ATOM 83 ND1 HIS A 13 79.996 178.499 129.406 1.00 38.78 N ANISOU 83 ND1 HIS A 13 9715 2720 2296 976 1736 130 N ATOM 84 CD2 HIS A 13 80.913 176.554 129.770 1.00 24.78 C ANISOU 84 CD2 HIS A 13 5569 1903 1941 -220 120 348 C ATOM 85 CE1 HIS A 13 79.677 178.135 130.635 1.00 57.26 C ANISOU 85 CE1 HIS A 13 13194 6717 1844 2380 1886 668 C ATOM 86 NE2 HIS A 13 80.087 176.892 130.810 1.00 36.38 N ANISOU 86 NE2 HIS A 13 7192 4507 2122 -2082 1446 -177 N ATOM 87 N PRO A 14 81.579 179.155 124.655 1.00 13.21 N ANISOU 87 N PRO A 14 2795 956 1268 -46 -346 192 N ATOM 88 CA PRO A 14 82.548 179.395 123.600 1.00 13.28 C ANISOU 88 CA PRO A 14 2883 975 1184 -19 -93 207 C ATOM 89 C PRO A 14 83.971 179.145 124.069 1.00 13.20 C ANISOU 89 C PRO A 14 2439 1074 1503 136 -249 217 C ATOM 90 O PRO A 14 84.365 179.521 125.154 1.00 14.40 O ANISOU 90 O PRO A 14 2809 1317 1343 -81 -403 -21 O ATOM 91 CB PRO A 14 82.309 180.861 123.242 1.00 14.15 C ANISOU 91 CB PRO A 14 2705 1097 1576 -57 -353 263 C ATOM 92 CG PRO A 14 80.940 181.119 123.665 1.00 14.15 C ANISOU 92 CG PRO A 14 2504 1116 1756 174 -82 274 C ATOM 93 CD PRO A 14 80.776 180.350 124.951 1.00 13.54 C ANISOU 93 CD PRO A 14 2345 995 1802 109 -187 65 C ATOM 94 N VAL A 15 84.748 178.584 123.167 1.00 12.70 N ANISOU 94 N VAL A 15 2363 1141 1322 -80 -293 242 N ATOM 95 CA VAL A 15 86.156 178.300 123.351 1.00 13.25 C ANISOU 95 CA VAL A 15 2436 1266 1332 -119 -283 166 C ATOM 96 C VAL A 15 86.860 178.788 122.115 1.00 13.10 C ANISOU 96 C VAL A 15 2073 1275 1627 10 -242 127 C ATOM 97 O VAL A 15 86.465 178.458 121.030 1.00 14.45 O ANISOU 97 O VAL A 15 2463 1617 1410 -297 -196 205 O ATOM 98 CB VAL A 15 86.383 176.805 123.562 1.00 14.08 C ANISOU 98 CB VAL A 15 2371 1339 1640 147 -168 256 C ATOM 99 CG1 VAL A 15 87.858 176.518 123.516 1.00 14.78 C ANISOU 99 CG1 VAL A 15 2036 1533 2046 93 -251 248 C ATOM 100 CG2 VAL A 15 85.765 176.394 124.885 1.00 16.68 C ANISOU 100 CG2 VAL A 15 2922 1280 2133 -23 -593 406 C ATOM 101 N GLU A 16 87.969 179.464 122.303 1.00 13.55 N ANISOU 101 N GLU A 16 2091 1467 1589 -89 -131 17 N ATOM 102 CA GLU A 16 88.787 179.910 121.211 1.00 14.03 C ANISOU 102 CA GLU A 16 2064 1495 1770 -218 -412 34 C ATOM 103 C GLU A 16 90.191 179.553 121.619 1.00 14.55 C ANISOU 103 C GLU A 16 2696 1429 1404 -461 -104 -57 C ATOM 104 O GLU A 16 90.586 179.768 122.752 1.00 16.64 O ANISOU 104 O GLU A 16 2588 2100 1632 -405 -135 -57 O ATOM 105 CB GLU A 16 88.599 181.418 121.016 1.00 15.70 C ANISOU 105 CB GLU A 16 2682 1506 1775 -113 -152 281 C ATOM 106 CG GLU A 16 89.476 181.985 119.923 1.00 17.17 C ANISOU 106 CG GLU A 16 2940 1212 2371 -12 -436 140 C ATOM 107 CD GLU A 16 89.062 183.374 119.452 1.00 16.67 C ANISOU 107 CD GLU A 16 2892 1367 2073 1 -228 196 C ATOM 108 OE1 GLU A 16 88.367 184.110 120.193 1.00 19.12 O ANISOU 108 OE1 GLU A 16 3623 1456 2184 49 -333 285 O ATOM 109 OE2 GLU A 16 89.551 183.802 118.388 1.00 22.32 O ANISOU 109 OE2 GLU A 16 4945 1237 2298 159 44 381 O ATOM 110 N ALA A 17 90.954 178.969 120.715 1.00 14.20 N ANISOU 110 N ALA A 17 2456 1412 1528 -81 -186 35 N ATOM 111 CA ALA A 17 92.250 178.475 121.082 1.00 15.47 C ANISOU 111 CA ALA A 17 2662 1387 1826 249 -164 38 C ATOM 112 C ALA A 17 93.136 178.394 119.865 1.00 15.39 C ANISOU 112 C ALA A 17 2233 1464 2151 -346 -423 348 C ATOM 113 O ALA A 17 92.674 178.399 118.726 1.00 15.45 O ANISOU 113 O ALA A 17 2064 1842 1966 -97 -97 -52 O ATOM 114 CB ALA A 17 92.129 177.074 121.742 1.00 16.97 C ANISOU 114 CB ALA A 17 2415 1480 2554 -164 -185 52 C ATOM 115 N LEU A 18 94.416 178.251 120.152 1.00 16.58 N ANISOU 115 N LEU A 18 2201 1700 2398 -76 -264 -223 N ATOM 116 CA LEU A 18 95.412 177.920 119.154 1.00 19.17 C ANISOU 116 CA LEU A 18 2248 1638 3398 -162 -241 -135 C ATOM 117 C LEU A 18 95.927 176.547 119.489 1.00 21.48 C ANISOU 117 C LEU A 18 2294 3161 2703 133 -636 -394 C ATOM 118 O LEU A 18 96.272 176.297 120.645 1.00 23.20 O ANISOU 118 O LEU A 18 3327 3005 2481 861 -838 -702 O ATOM 119 CB LEU A 18 96.578 178.871 119.243 1.00 22.59 C ANISOU 119 CB LEU A 18 2458 2381 3743 -210 -182 -1054 C ATOM 120 CG LEU A 18 96.247 180.289 118.832 1.00 25.34 C ANISOU 120 CG LEU A 18 3657 2331 3639 -1044 623 -355 C ATOM 121 CD1 LEU A 18 97.485 181.126 118.967 1.00 30.89 C ANISOU 121 CD1 LEU A 18 5426 2781 3528 -2140 -129 -359 C ATOM 122 CD2 LEU A 18 95.745 180.347 117.410 1.00 33.76 C ANISOU 122 CD2 LEU A 18 6054 2213 4557 -1225 -2788 469 C ATOM 123 N VAL A 19 95.962 175.664 118.505 1.00 16.78 N ANISOU 123 N VAL A 19 2490 1810 2072 12 122 -220 N ATOM 124 CA VAL A 19 96.434 174.306 118.747 1.00 17.90 C ANISOU 124 CA VAL A 19 2282 1914 2606 329 -621 -28 C ATOM 125 C VAL A 19 97.372 173.904 117.629 1.00 15.53 C ANISOU 125 C VAL A 19 2199 1597 2100 20 -328 87 C ATOM 126 O VAL A 19 97.201 174.289 116.477 1.00 16.97 O ANISOU 126 O VAL A 19 2842 1797 1806 285 0 250 O ATOM 127 CB VAL A 19 95.273 173.272 118.799 1.00 16.38 C ANISOU 127 CB VAL A 19 2255 2071 1897 -285 -198 456 C ATOM 128 CG1 VAL A 19 94.398 173.507 119.975 1.00 20.29 C ANISOU 128 CG1 VAL A 19 2651 3199 1861 -115 -63 215 C ATOM 129 CG2 VAL A 19 94.456 173.345 117.548 1.00 16.33 C ANISOU 129 CG2 VAL A 19 2705 1360 2135 -211 -156 144 C ATOM 130 N GLU A 20 98.278 173.001 117.917 1.00 14.90 N ANISOU 130 N GLU A 20 2284 1774 1601 164 -155 167 N ATOM 131 CA GLU A 20 99.011 172.326 116.859 1.00 16.04 C ANISOU 131 CA GLU A 20 2039 1958 2094 -328 306 59 C ATOM 132 C GLU A 20 98.077 171.361 116.213 1.00 14.01 C ANISOU 132 C GLU A 20 2208 1357 1756 -82 30 167 C ATOM 133 O GLU A 20 97.265 170.735 116.879 1.00 14.70 O ANISOU 133 O GLU A 20 2154 1510 1921 -225 249 216 O ATOM 134 CB GLU A 20 100.226 171.588 117.397 1.00 20.67 C ANISOU 134 CB GLU A 20 2790 2204 2858 366 -83 -241 C ATOM 135 CG GLU A 20 101.207 172.525 118.060 1.00 25.30 C ANISOU 135 CG GLU A 20 2509 2958 4144 274 -623 -1402 C ATOM 136 CD GLU A 20 102.056 173.282 117.057 1.00 58.31 C ANISOU 136 CD GLU A 20 1976 4119 16059 -1288 1958 -3445 C ATOM 137 OE1 GLU A 20 101.922 173.012 115.845 1.00 35.72 O ANISOU 137 OE1 GLU A 20 3596 2648 7326 38 120 -670 O ATOM 138 OE2 GLU A 20 102.751 174.237 117.462 1.00 23.12 O ANISOU 138 OE2 GLU A 20 5929 1842 1013 -195 -1239 1063 O ATOM 139 N PRO A 21 98.224 171.161 114.924 1.00 14.86 N ANISOU 139 N PRO A 21 2310 1448 1887 -174 -93 130 N ATOM 140 CA PRO A 21 97.330 170.212 114.260 1.00 14.55 C ANISOU 140 CA PRO A 21 2222 1475 1828 83 -91 331 C ATOM 141 C PRO A 21 97.384 168.824 114.855 1.00 15.08 C ANISOU 141 C PRO A 21 2422 1773 1532 -124 331 282 C ATOM 142 O PRO A 21 96.349 168.149 114.923 1.00 15.18 O ANISOU 142 O PRO A 21 2067 1780 1920 -27 285 219 O ATOM 143 CB PRO A 21 97.822 170.212 112.838 1.00 16.76 C ANISOU 143 CB PRO A 21 3003 1723 1641 -222 326 182 C ATOM 144 CG PRO A 21 98.284 171.661 112.640 1.00 18.74 C ANISOU 144 CG PRO A 21 2915 2076 2127 -351 -88 557 C ATOM 145 CD PRO A 21 98.946 172.019 113.965 1.00 16.35 C ANISOU 145 CD PRO A 21 2617 1421 2176 -329 80 322 C ATOM 146 N ARG A 22 98.561 168.389 115.267 1.00 14.96 N ANISOU 146 N ARG A 22 2163 1639 1882 -241 74 487 N ATOM 147 CA ARG A 22 98.656 167.033 115.731 1.00 14.24 C ANISOU 147 CA ARG A 22 2243 1598 1565 -96 103 590 C ATOM 148 C ARG A 22 98.114 166.823 117.111 1.00 13.43 C ANISOU 148 C ARG A 22 1873 1592 1636 -243 0 186 C ATOM 149 O ARG A 22 98.154 165.719 117.615 1.00 14.87 O ANISOU 149 O ARG A 22 2467 1476 1705 -132 204 293 O ATOM 150 CB ARG A 22 100.076 166.520 115.635 1.00 14.44 C ANISOU 150 CB ARG A 22 1978 1745 1763 -223 93 294 C ATOM 151 CG ARG A 22 101.045 167.172 116.581 1.00 15.07 C ANISOU 151 CG ARG A 22 2381 1462 1881 -63 253 151 C ATOM 152 CD ARG A 22 102.277 166.339 116.775 1.00 15.07 C ANISOU 152 CD ARG A 22 2161 1876 1688 -54 63 357 C ATOM 153 NE ARG A 22 103.303 167.059 117.492 1.00 15.47 N ANISOU 153 NE ARG A 22 2502 2055 1318 -254 -98 187 N ATOM 154 CZ ARG A 22 104.500 166.577 117.721 1.00 16.91 C ANISOU 154 CZ ARG A 22 2163 2720 1541 135 -140 278 C ATOM 155 NH1 ARG A 22 104.764 165.316 117.414 1.00 18.71 N ANISOU 155 NH1 ARG A 22 2816 2373 1918 296 -24 234 N ATOM 156 NH2 ARG A 22 105.393 167.325 118.339 1.00 18.47 N ANISOU 156 NH2 ARG A 22 2669 2524 1821 -423 -335 175 N ATOM 157 N THR A 23 97.763 167.896 117.788 1.00 13.20 N ANISOU 157 N THR A 23 2146 1515 1353 -148 215 141 N ATOM 158 CA THR A 23 97.213 167.717 119.118 1.00 12.96 C ANISOU 158 CA THR A 23 1772 1393 1757 -254 -113 207 C ATOM 159 C THR A 23 95.946 166.948 119.073 1.00 13.07 C ANISOU 159 C THR A 23 2032 1609 1322 -173 -32 241 C ATOM 160 O THR A 23 94.983 167.339 118.446 1.00 13.31 O ANISOU 160 O THR A 23 2039 1586 1432 -207 -130 311 O ATOM 161 CB THR A 23 96.984 169.045 119.760 1.00 14.84 C ANISOU 161 CB THR A 23 2025 1879 1735 -507 76 307 C ATOM 162 OG1 THR A 23 98.218 169.746 119.789 1.00 16.70 O ANISOU 162 OG1 THR A 23 2248 2125 1973 -626 164 3 O ATOM 163 CG2 THR A 23 96.490 168.946 121.178 1.00 15.89 C ANISOU 163 CG2 THR A 23 2364 2127 1545 -375 24 236 C ATOM 164 N LEU A 24 95.950 165.831 119.763 1.00 12.66 N ANISOU 164 N LEU A 24 1826 1403 1580 -195 -70 335 N ATOM 165 CA LEU A 24 94.747 165.037 119.866 1.00 13.30 C ANISOU 165 CA LEU A 24 2115 1465 1472 -76 -92 340 C ATOM 166 C LEU A 24 93.698 165.790 120.652 1.00 12.31 C ANISOU 166 C LEU A 24 2124 1324 1230 -189 -99 472 C ATOM 167 O LEU A 24 94.007 166.468 121.607 1.00 12.33 O ANISOU 167 O LEU A 24 1962 1459 1263 -189 -17 308 O ATOM 168 CB LEU A 24 95.032 163.696 120.493 1.00 12.76 C ANISOU 168 CB LEU A 24 1882 1458 1508 54 92 392 C ATOM 169 CG LEU A 24 95.979 162.798 119.719 1.00 14.77 C ANISOU 169 CG LEU A 24 2222 1657 1731 -83 225 463 C ATOM 170 CD1 LEU A 24 96.400 161.580 120.489 1.00 16.36 C ANISOU 170 CD1 LEU A 24 2612 1587 2016 151 -269 82 C ATOM 171 CD2 LEU A 24 95.381 162.334 118.422 1.00 14.61 C ANISOU 171 CD2 LEU A 24 2433 1601 1513 152 216 164 C ATOM 172 N LEU A 25 92.437 165.596 120.268 1.00 11.52 N ANISOU 172 N LEU A 25 1943 1229 1203 -173 -122 375 N ATOM 173 CA LEU A 25 91.369 166.288 120.951 1.00 11.70 C ANISOU 173 CA LEU A 25 2046 1147 1253 -274 -142 168 C ATOM 174 C LEU A 25 91.366 165.990 122.437 1.00 11.00 C ANISOU 174 C LEU A 25 1738 1165 1273 -162 -131 313 C ATOM 175 O LEU A 25 91.149 166.887 123.245 1.00 11.83 O ANISOU 175 O LEU A 25 1969 1105 1418 -161 -311 284 O ATOM 176 CB LEU A 25 90.059 165.962 120.326 1.00 11.75 C ANISOU 176 CB LEU A 25 1990 1171 1305 -177 -46 299 C ATOM 177 CG LEU A 25 88.827 166.576 120.941 1.00 11.63 C ANISOU 177 CG LEU A 25 2038 1057 1324 21 -102 294 C ATOM 178 CD1 LEU A 25 88.869 168.083 120.909 1.00 12.62 C ANISOU 178 CD1 LEU A 25 2303 1256 1233 -160 -121 259 C ATOM 179 CD2 LEU A 25 87.574 166.059 120.325 1.00 12.45 C ANISOU 179 CD2 LEU A 25 2154 1180 1395 -6 -284 357 C ATOM 180 N ILE A 26 91.652 164.739 122.789 1.00 11.22 N ANISOU 180 N ILE A 26 2003 1083 1174 10 -181 373 N ATOM 181 CA ILE A 26 91.703 164.405 124.179 1.00 11.54 C ANISOU 181 CA ILE A 26 2083 1036 1262 -252 -195 114 C ATOM 182 C ILE A 26 92.709 165.270 124.916 1.00 11.14 C ANISOU 182 C ILE A 26 1731 1118 1380 -162 -109 212 C ATOM 183 O ILE A 26 92.468 165.675 126.032 1.00 12.09 O ANISOU 183 O ILE A 26 2099 1163 1332 -242 -140 81 O ATOM 184 CB ILE A 26 91.981 162.886 124.367 1.00 11.33 C ANISOU 184 CB ILE A 26 2101 1067 1133 -160 -54 241 C ATOM 185 CG1 ILE A 26 91.914 162.493 125.830 1.00 12.28 C ANISOU 185 CG1 ILE A 26 2116 1220 1331 -138 -151 311 C ATOM 186 CG2 ILE A 26 93.337 162.495 123.839 1.00 12.41 C ANISOU 186 CG2 ILE A 26 2065 1088 1561 -172 -231 173 C ATOM 187 CD1 ILE A 26 90.652 162.816 126.494 1.00 12.27 C ANISOU 187 CD1 ILE A 26 2162 1296 1203 -174 -155 200 C ATOM 188 N HIS A 27 93.861 165.510 124.322 1.00 11.78 N ANISOU 188 N HIS A 27 1873 1304 1298 -135 -263 258 N ATOM 189 CA HIS A 27 94.874 166.321 124.961 1.00 12.38 C ANISOU 189 CA HIS A 27 1902 1184 1615 -288 -430 298 C ATOM 190 C HIS A 27 94.507 167.793 124.953 1.00 13.95 C ANISOU 190 C HIS A 27 1977 1406 1915 -419 -452 659 C ATOM 191 O HIS A 27 94.774 168.505 125.907 1.00 14.28 O ANISOU 191 O HIS A 27 2594 1318 1509 -310 -549 204 O ATOM 192 CB HIS A 27 96.249 166.113 124.341 1.00 13.64 C ANISOU 192 CB HIS A 27 2143 1368 1668 -421 -331 573 C ATOM 193 CG HIS A 27 96.809 164.753 124.571 1.00 14.02 C ANISOU 193 CG HIS A 27 1826 1782 1719 -401 -240 670 C ATOM 194 ND1 HIS A 27 97.301 163.987 123.541 1.00 14.96 N ANISOU 194 ND1 HIS A 27 2337 1379 1967 -144 -109 460 N ATOM 195 CD2 HIS A 27 96.875 163.992 125.683 1.00 16.94 C ANISOU 195 CD2 HIS A 27 2554 1528 2352 -568 -515 518 C ATOM 196 CE1 HIS A 27 97.736 162.840 124.030 1.00 15.39 C ANISOU 196 CE1 HIS A 27 1956 1685 2205 -49 -160 305 C ATOM 197 NE2 HIS A 27 97.465 162.813 125.319 1.00 14.20 N ANISOU 197 NE2 HIS A 27 2137 1475 1782 -37 13 262 N ATOM 198 N PHE A 28 93.873 168.269 123.904 1.00 12.78 N ANISOU 198 N PHE A 28 2304 1147 1401 -324 -303 381 N ATOM 199 CA PHE A 28 93.385 169.639 123.965 1.00 12.05 C ANISOU 199 CA PHE A 28 1911 1378 1289 -228 -147 375 C ATOM 200 C PHE A 28 92.399 169.817 125.095 1.00 12.86 C ANISOU 200 C PHE A 28 2246 1230 1411 -280 -463 208 C ATOM 201 O PHE A 28 92.479 170.768 125.857 1.00 13.92 O ANISOU 201 O PHE A 28 2660 1230 1397 -310 -195 93 O ATOM 202 CB PHE A 28 92.676 169.964 122.679 1.00 13.06 C ANISOU 202 CB PHE A 28 2304 1351 1305 -346 -175 309 C ATOM 203 CG PHE A 28 91.991 171.297 122.695 1.00 12.58 C ANISOU 203 CG PHE A 28 2092 1240 1447 -211 -144 355 C ATOM 204 CD1 PHE A 28 92.720 172.447 122.723 1.00 13.85 C ANISOU 204 CD1 PHE A 28 1993 1270 1996 -115 -236 335 C ATOM 205 CD2 PHE A 28 90.622 171.366 122.655 1.00 14.14 C ANISOU 205 CD2 PHE A 28 2493 1484 1393 -244 40 104 C ATOM 206 CE1 PHE A 28 92.073 173.688 122.749 1.00 15.90 C ANISOU 206 CE1 PHE A 28 2545 1316 2178 -175 -194 307 C ATOM 207 CE2 PHE A 28 89.973 172.558 122.642 1.00 13.75 C ANISOU 207 CE2 PHE A 28 1856 1745 1622 -126 -12 430 C ATOM 208 CZ PHE A 28 90.686 173.740 122.710 1.00 14.76 C ANISOU 208 CZ PHE A 28 2581 1396 1631 207 -168 88 C ATOM 209 N ILE A 29 91.467 168.876 125.219 1.00 11.85 N ANISOU 209 N ILE A 29 2261 1045 1195 -102 -94 233 N ATOM 210 CA ILE A 29 90.471 168.956 126.270 1.00 13.46 C ANISOU 210 CA ILE A 29 2664 1212 1239 -292 -489 228 C ATOM 211 C ILE A 29 91.134 168.888 127.628 1.00 12.93 C ANISOU 211 C ILE A 29 2567 1237 1108 -546 -340 194 C ATOM 212 O ILE A 29 90.847 169.699 128.478 1.00 13.42 O ANISOU 212 O ILE A 29 2777 1102 1218 -216 -231 93 O ATOM 213 CB ILE A 29 89.469 167.831 126.076 1.00 12.43 C ANISOU 213 CB ILE A 29 2057 1504 1158 -267 -165 346 C ATOM 214 CG1 ILE A 29 88.622 168.117 124.835 1.00 12.15 C ANISOU 214 CG1 ILE A 29 2152 1168 1295 24 34 19 C ATOM 215 CG2 ILE A 29 88.586 167.635 127.274 1.00 13.69 C ANISOU 215 CG2 ILE A 29 2432 1306 1462 -148 -287 157 C ATOM 216 CD1 ILE A 29 87.655 167.018 124.489 1.00 13.84 C ANISOU 216 CD1 ILE A 29 2372 1632 1252 -305 -230 -38 C ATOM 217 N ARG A 30 92.012 167.911 127.815 1.00 12.23 N ANISOU 217 N ARG A 30 2260 1204 1178 -151 -226 196 N ATOM 218 CA ARG A 30 92.630 167.701 129.109 1.00 12.22 C ANISOU 218 CA ARG A 30 2498 966 1177 -34 -300 170 C ATOM 219 C ARG A 30 93.702 168.730 129.433 1.00 14.17 C ANISOU 219 C ARG A 30 2962 1094 1326 -357 -452 119 C ATOM 220 O ARG A 30 93.809 169.191 130.557 1.00 15.51 O ANISOU 220 O ARG A 30 2824 1562 1506 -214 -504 -120 O ATOM 221 CB ARG A 30 93.251 166.334 129.204 1.00 12.80 C ANISOU 221 CB ARG A 30 2486 1274 1103 -249 -379 214 C ATOM 222 CG ARG A 30 92.253 165.223 129.264 1.00 12.35 C ANISOU 222 CG ARG A 30 2396 1066 1229 -184 -296 234 C ATOM 223 CD ARG A 30 92.927 163.878 129.325 1.00 11.47 C ANISOU 223 CD ARG A 30 1790 1216 1351 -230 -206 208 C ATOM 224 NE ARG A 30 93.899 163.801 130.410 1.00 11.14 N ANISOU 224 NE ARG A 30 1723 1199 1309 -81 -186 196 N ATOM 225 CZ ARG A 30 93.603 163.783 131.681 1.00 11.04 C ANISOU 225 CZ ARG A 30 1869 1128 1198 -130 -195 200 C ATOM 226 NH1 ARG A 30 92.356 163.626 132.071 1.00 10.70 N ANISOU 226 NH1 ARG A 30 1768 1171 1127 -195 -133 208 N ATOM 227 NH2 ARG A 30 94.553 164.056 132.544 1.00 12.22 N ANISOU 227 NH2 ARG A 30 1668 1720 1253 -441 -185 340 N ATOM 228 N GLU A 31 94.605 168.951 128.482 1.00 14.18 N ANISOU 228 N GLU A 31 2474 1536 1377 -537 -256 206 N ATOM 229 CA GLU A 31 95.851 169.690 128.725 1.00 13.21 C ANISOU 229 CA GLU A 31 2060 1679 1280 -373 -258 215 C ATOM 230 C GLU A 31 95.715 171.157 128.507 1.00 16.57 C ANISOU 230 C GLU A 31 2994 1650 1651 -465 -588 227 C ATOM 231 O GLU A 31 96.384 171.896 129.195 1.00 21.17 O ANISOU 231 O GLU A 31 4140 1812 2090 -913 -813 216 O ATOM 232 CB GLU A 31 96.985 169.170 127.859 1.00 16.50 C ANISOU 232 CB GLU A 31 2770 1886 1611 -700 -103 243 C ATOM 233 CG GLU A 31 97.302 167.691 127.977 1.00 16.05 C ANISOU 233 CG GLU A 31 2556 1688 1853 -111 -140 566 C ATOM 234 CD GLU A 31 97.945 167.297 129.272 1.00 16.89 C ANISOU 234 CD GLU A 31 1967 2363 2087 -410 -197 549 C ATOM 235 OE1 GLU A 31 99.072 167.737 129.522 1.00 23.58 O ANISOU 235 OE1 GLU A 31 2757 3702 2500 -1110 -659 1307 O ATOM 236 OE2 GLU A 31 97.233 166.719 130.101 1.00 16.70 O ANISOU 236 OE2 GLU A 31 2795 1926 1623 -307 -209 254 O ATOM 237 N GLN A 32 94.897 171.588 127.561 1.00 15.39 N ANISOU 237 N GLN A 32 2572 1501 1772 -522 -162 48 N ATOM 238 CA GLN A 32 94.720 172.994 127.278 1.00 16.05 C ANISOU 238 CA GLN A 32 2881 1587 1631 -430 -155 98 C ATOM 239 C GLN A 32 93.455 173.576 127.882 1.00 14.90 C ANISOU 239 C GLN A 32 2921 938 1801 -233 -439 68 C ATOM 240 O GLN A 32 93.508 174.625 128.500 1.00 19.22 O ANISOU 240 O GLN A 32 3131 1553 2617 -586 71 38 O ATOM 241 CB GLN A 32 94.726 173.224 125.773 1.00 18.14 C ANISOU 241 CB GLN A 32 3819 1394 1678 -900 -271 441 C ATOM 242 CG GLN A 32 96.076 172.955 125.176 1.00 22.40 C ANISOU 242 CG GLN A 32 2953 3127 2428 -863 142 355 C ATOM 243 CD GLN A 32 96.115 173.192 123.693 1.00 21.48 C ANISOU 243 CD GLN A 32 4273 2113 1773 -401 439 272 C ATOM 244 OE1 GLN A 32 96.349 172.265 122.915 1.00 26.11 O ANISOU 244 OE1 GLN A 32 3625 2870 3425 215 606 153 O ATOM 245 NE2 GLN A 32 95.789 174.413 123.277 1.00 20.61 N ANISOU 245 NE2 GLN A 32 2773 2421 2635 -368 -152 493 N ATOM 246 N GLN A 33 92.366 172.810 127.877 1.00 15.93 N ANISOU 246 N GLN A 33 3138 1319 1591 -467 -274 172 N ATOM 247 CA GLN A 33 91.121 173.265 128.471 1.00 15.24 C ANISOU 247 CA GLN A 33 3027 1221 1542 -333 -318 219 C ATOM 248 C GLN A 33 90.984 172.877 129.926 1.00 13.89 C ANISOU 248 C GLN A 33 2581 1079 1615 -20 -239 59 C ATOM 249 O GLN A 33 90.018 173.252 130.569 1.00 14.79 O ANISOU 249 O GLN A 33 2675 1094 1850 140 -346 114 O ATOM 250 CB GLN A 33 89.900 172.809 127.673 1.00 15.99 C ANISOU 250 CB GLN A 33 3420 1119 1536 -182 -375 -129 C ATOM 251 CG GLN A 33 89.909 173.311 126.288 1.00 15.92 C ANISOU 251 CG GLN A 33 3012 1481 1553 74 -564 116 C ATOM 252 CD GLN A 33 89.961 174.810 126.205 1.00 17.94 C ANISOU 252 CD GLN A 33 2874 1687 2254 -370 -878 643 C ATOM 253 OE1 GLN A 33 90.946 175.378 125.717 1.00 22.16 O ANISOU 253 OE1 GLN A 33 3664 2205 2549 -491 331 377 O ATOM 254 NE2 GLN A 33 88.910 175.458 126.664 1.00 18.75 N ANISOU 254 NE2 GLN A 33 3280 1729 2117 304 -551 670 N ATOM 255 N ASN A 34 91.859 172.001 130.400 1.00 15.03 N ANISOU 255 N ASN A 34 3231 1279 1199 -262 -86 142 N ATOM 256 CA ASN A 34 91.832 171.542 131.765 1.00 15.93 C ANISOU 256 CA ASN A 34 3140 1383 1528 -247 -627 293 C ATOM 257 C ASN A 34 90.532 170.843 132.121 1.00 14.80 C ANISOU 257 C ASN A 34 2644 1358 1620 -185 -223 159 C ATOM 258 O ASN A 34 90.149 170.805 133.276 1.00 17.32 O ANISOU 258 O ASN A 34 2892 2336 1351 -141 -189 -57 O ATOM 259 CB ASN A 34 92.107 172.694 132.713 1.00 18.78 C ANISOU 259 CB ASN A 34 3675 1891 1568 -762 -595 231 C ATOM 260 CG ASN A 34 93.537 173.209 132.624 1.00 22.76 C ANISOU 260 CG ASN A 34 3580 2612 2454 -1143 -381 -542 C ATOM 261 OD1 ASN A 34 93.849 174.260 133.174 0.50 40.89 O ANISOU 261 OD1 ASN A 34 5078 3050 7404 -2283 1794 -2910 O ATOM 262 ND2 ASN A 34 94.361 172.560 131.819 1.00 28.59 N ANISOU 262 ND2 ASN A 34 4365 2302 4192 -120 -1689 -115 N ATOM 263 N LEU A 35 89.908 170.187 131.159 1.00 12.99 N ANISOU 263 N LEU A 35 2346 1186 1402 -214 -340 228 N ATOM 264 CA LEU A 35 88.729 169.358 131.402 1.00 12.32 C ANISOU 264 CA LEU A 35 2172 1177 1331 147 -311 216 C ATOM 265 C LEU A 35 89.182 167.927 131.520 1.00 12.78 C ANISOU 265 C LEU A 35 2250 1132 1471 13 -153 82 C ATOM 266 O LEU A 35 89.271 167.187 130.579 1.00 13.10 O ANISOU 266 O LEU A 35 2587 1186 1203 146 -236 115 O ATOM 267 CB LEU A 35 87.723 169.548 130.279 1.00 14.30 C ANISOU 267 CB LEU A 35 2588 1314 1529 78 -261 146 C ATOM 268 CG LEU A 35 87.086 170.926 130.210 1.00 14.99 C ANISOU 268 CG LEU A 35 2685 1257 1749 76 -546 329 C ATOM 269 CD1 LEU A 35 86.342 171.064 128.929 1.00 16.57 C ANISOU 269 CD1 LEU A 35 2901 1352 2040 -70 -621 496 C ATOM 270 CD2 LEU A 35 86.154 171.125 131.365 1.00 17.11 C ANISOU 270 CD2 LEU A 35 2727 1448 2326 368 -77 291 C ATOM 271 N THR A 36 89.663 167.618 132.703 1.00 12.13 N ANISOU 271 N THR A 36 2348 1068 1189 -34 -318 216 N ATOM 272 CA THR A 36 90.404 166.387 132.906 1.00 11.36 C ANISOU 272 CA THR A 36 1960 1234 1120 57 -94 156 C ATOM 273 C THR A 36 89.502 165.216 133.283 1.00 11.34 C ANISOU 273 C THR A 36 1888 1115 1304 -92 -59 132 C ATOM 274 O THR A 36 89.990 164.160 133.628 1.00 11.22 O ANISOU 274 O THR A 36 1844 1018 1402 -71 -131 278 O ATOM 275 CB THR A 36 91.493 166.573 133.951 1.00 12.75 C ANISOU 275 CB THR A 36 2145 1116 1580 -218 -310 289 C ATOM 276 OG1 THR A 36 90.965 167.299 135.061 1.00 13.18 O ANISOU 276 OG1 THR A 36 2377 1209 1421 -141 -255 138 O ATOM 277 CG2 THR A 36 92.684 167.369 133.397 1.00 14.46 C ANISOU 277 CG2 THR A 36 2223 1508 1762 -6 -141 104 C ATOM 278 N GLY A 37 88.201 165.335 133.124 1.00 12.00 N ANISOU 278 N GLY A 37 2225 913 1421 -35 -100 70 N ATOM 279 CA GLY A 37 87.329 164.195 133.311 1.00 10.82 C ANISOU 279 CA GLY A 37 1784 1137 1190 27 -37 -102 C ATOM 280 C GLY A 37 87.601 163.097 132.301 1.00 11.29 C ANISOU 280 C GLY A 37 1715 1194 1379 -21 82 188 C ATOM 281 O GLY A 37 87.679 161.930 132.624 1.00 12.06 O ANISOU 281 O GLY A 37 2160 1053 1369 0 34 186 O ATOM 282 N ALA A 38 87.637 163.476 131.041 1.00 11.33 N ANISOU 282 N ALA A 38 1932 1076 1298 51 -24 -24 N ATOM 283 CA ALA A 38 87.935 162.553 129.997 1.00 11.83 C ANISOU 283 CA ALA A 38 1932 1363 1199 -132 -231 254 C ATOM 284 C ALA A 38 89.294 161.958 130.223 1.00 10.69 C ANISOU 284 C ALA A 38 1718 1146 1199 6 -108 10 C ATOM 285 O ALA A 38 90.240 162.640 130.621 1.00 11.65 O ANISOU 285 O ALA A 38 1898 1027 1499 -93 -168 92 O ATOM 286 CB ALA A 38 87.921 163.267 128.686 1.00 12.61 C ANISOU 286 CB ALA A 38 2009 1377 1405 178 -57 -87 C ATOM 287 N HIS A 39 89.419 160.671 129.956 1.00 10.05 N ANISOU 287 N HIS A 39 1683 978 1156 -80 -119 55 N ATOM 288 CA HIS A 39 90.632 159.959 130.256 1.00 10.46 C ANISOU 288 CA HIS A 39 1833 1010 1130 -153 -49 89 C ATOM 289 C HIS A 39 91.162 159.221 129.080 1.00 10.13 C ANISOU 289 C HIS A 39 1853 935 1059 -52 -147 136 C ATOM 290 O HIS A 39 90.435 158.914 128.157 1.00 11.62 O ANISOU 290 O HIS A 39 1986 1208 1221 -13 -252 17 O ATOM 291 CB HIS A 39 90.392 158.935 131.356 1.00 11.36 C ANISOU 291 CB HIS A 39 2260 756 1298 -28 -20 74 C ATOM 292 CG HIS A 39 90.004 159.570 132.628 1.00 12.01 C ANISOU 292 CG HIS A 39 2509 822 1230 -20 6 116 C ATOM 293 ND1 HIS A 39 89.052 159.039 133.461 1.00 11.24 N ANISOU 293 ND1 HIS A 39 1912 1057 1300 -88 40 192 N ATOM 294 CD2 HIS A 39 90.543 160.619 133.281 1.00 11.61 C ANISOU 294 CD2 HIS A 39 2239 996 1174 -242 -76 115 C ATOM 295 CE1 HIS A 39 88.943 159.816 134.520 1.00 11.68 C ANISOU 295 CE1 HIS A 39 2208 1040 1189 -152 6 -57 C ATOM 296 NE2 HIS A 39 89.872 160.749 134.455 1.00 11.83 N ANISOU 296 NE2 HIS A 39 2282 1154 1058 -71 -46 74 N ATOM 297 N ILE A 40 92.421 158.845 129.189 1.00 10.68 N ANISOU 297 N ILE A 40 1757 1115 1185 -8 -160 8 N ATOM 298 CA ILE A 40 93.054 157.995 128.223 1.00 10.50 C ANISOU 298 CA ILE A 40 1710 1194 1084 89 77 63 C ATOM 299 C ILE A 40 93.307 156.665 128.841 1.00 9.96 C ANISOU 299 C ILE A 40 1727 967 1089 78 -87 88 C ATOM 300 O ILE A 40 93.976 156.567 129.844 1.00 11.59 O ANISOU 300 O ILE A 40 2076 1165 1159 70 -252 74 O ATOM 301 CB ILE A 40 94.375 158.619 127.779 1.00 10.95 C ANISOU 301 CB ILE A 40 1714 1098 1348 -20 -3 -10 C ATOM 302 CG1 ILE A 40 94.076 159.905 127.013 1.00 12.54 C ANISOU 302 CG1 ILE A 40 2046 1128 1588 -138 111 286 C ATOM 303 CG2 ILE A 40 95.176 157.648 126.902 1.00 12.94 C ANISOU 303 CG2 ILE A 40 2126 1472 1317 -203 -94 220 C ATOM 304 CD1 ILE A 40 95.253 160.844 126.880 1.00 16.14 C ANISOU 304 CD1 ILE A 40 2396 1596 2141 -355 -253 416 C ATOM 305 N GLY A 41 92.822 155.626 128.208 1.00 10.46 N ANISOU 305 N GLY A 41 1862 1177 934 -115 -99 143 N ATOM 306 CA GLY A 41 92.991 154.276 128.692 1.00 10.48 C ANISOU 306 CA GLY A 41 2000 929 1053 87 13 30 C ATOM 307 C GLY A 41 93.727 153.386 127.731 1.00 11.49 C ANISOU 307 C GLY A 41 2152 1049 1162 -120 -333 181 C ATOM 308 O GLY A 41 93.964 152.214 128.040 1.00 12.32 O ANISOU 308 O GLY A 41 2366 1101 1213 126 -120 144 O ATOM 309 N CYS A 42 94.030 153.861 126.547 1.00 10.84 N ANISOU 309 N CYS A 42 1984 1097 1036 15 -70 77 N ATOM 310 CA CYS A 42 94.611 153.001 125.557 1.00 10.74 C ANISOU 310 CA CYS A 42 1879 1079 1123 27 -93 113 C ATOM 311 C CYS A 42 95.252 153.845 124.504 1.00 10.99 C ANISOU 311 C CYS A 42 1757 1154 1263 -93 -221 206 C ATOM 312 O CYS A 42 95.096 155.040 124.474 1.00 11.97 O ANISOU 312 O CYS A 42 2017 1323 1208 -119 93 119 O ATOM 313 CB CYS A 42 93.583 152.023 125.008 1.00 11.28 C ANISOU 313 CB CYS A 42 1842 1261 1184 -17 -181 133 C ATOM 314 SG CYS A 42 92.480 152.779 123.806 1.00 10.09 S ANISOU 314 SG CYS A 42 1801 1023 1008 -38 -66 121 S ATOM 315 N ASP A 43 95.924 153.156 123.613 1.00 11.87 N ANISOU 315 N ASP A 43 2037 1257 1212 68 189 40 N ATOM 316 CA ASP A 43 96.611 153.793 122.544 1.00 11.76 C ANISOU 316 CA ASP A 43 1653 1342 1471 1 -59 120 C ATOM 317 C ASP A 43 96.150 153.250 121.220 1.00 13.15 C ANISOU 317 C ASP A 43 1951 1404 1639 -80 142 54 C ATOM 318 O ASP A 43 96.700 153.622 120.203 1.00 16.97 O ANISOU 318 O ASP A 43 2759 2407 1281 -698 335 38 O ATOM 319 CB ASP A 43 98.123 153.671 122.705 1.00 13.65 C ANISOU 319 CB ASP A 43 2321 1512 1352 348 130 284 C ATOM 320 CG ASP A 43 98.577 152.310 123.167 1.00 13.46 C ANISOU 320 CG ASP A 43 1820 1981 1313 -54 121 -99 C ATOM 321 OD1 ASP A 43 97.825 151.322 123.026 1.00 14.08 O ANISOU 321 OD1 ASP A 43 2177 1699 1474 174 -115 49 O ATOM 322 OD2 ASP A 43 99.753 152.134 123.546 1.00 14.79 O ANISOU 322 OD2 ASP A 43 2170 1967 1482 131 -65 255 O ATOM 323 N THR A 44 95.063 152.506 121.209 1.00 11.88 N ANISOU 323 N THR A 44 2159 1315 1040 93 -57 -19 N ATOM 324 CA THR A 44 94.575 151.856 120.013 1.00 12.09 C ANISOU 324 CA THR A 44 2285 1119 1186 44 238 205 C ATOM 325 C THR A 44 93.104 152.104 119.745 1.00 11.17 C ANISOU 325 C THR A 44 2045 996 1203 -175 -103 165 C ATOM 326 O THR A 44 92.549 151.498 118.858 1.00 12.42 O ANISOU 326 O THR A 44 2322 1256 1140 118 -6 -76 O ATOM 327 CB THR A 44 94.789 150.368 120.108 1.00 12.69 C ANISOU 327 CB THR A 44 2163 1365 1292 166 214 204 C ATOM 328 OG1 THR A 44 94.235 149.893 121.336 1.00 12.73 O ANISOU 328 OG1 THR A 44 2207 1479 1147 132 81 249 O ATOM 329 CG2 THR A 44 96.270 150.011 120.109 1.00 14.05 C ANISOU 329 CG2 THR A 44 2443 1468 1424 140 198 15 C ATOM 330 N SER A 45 92.500 153.023 120.467 1.00 10.62 N ANISOU 330 N SER A 45 1939 1018 1076 89 -17 77 N ATOM 331 CA SER A 45 91.133 153.460 120.231 1.00 11.00 C ANISOU 331 CA SER A 45 2063 1125 988 0 -121 184 C ATOM 332 C SER A 45 90.071 152.459 120.654 1.00 10.85 C ANISOU 332 C SER A 45 2004 1033 1084 -54 13 15 C ATOM 333 O SER A 45 88.928 152.575 120.242 1.00 12.07 O ANISOU 333 O SER A 45 2123 1242 1221 -10 -164 238 O ATOM 334 CB SER A 45 90.911 153.874 118.785 1.00 11.88 C ANISOU 334 CB SER A 45 2258 1013 1239 -68 131 237 C ATOM 335 OG SER A 45 91.901 154.790 118.404 1.00 12.13 O ANISOU 335 OG SER A 45 2020 1298 1288 -127 12 227 O ATOM 336 N HIS A 46 90.400 151.547 121.557 1.00 10.65 N ANISOU 336 N HIS A 46 1902 1046 1098 -94 -156 35 N ATOM 337 CA HIS A 46 89.440 150.560 122.003 1.00 10.74 C ANISOU 337 CA HIS A 46 1976 1058 1046 -93 -94 66 C ATOM 338 C HIS A 46 88.639 150.977 123.200 1.00 10.74 C ANISOU 338 C HIS A 46 1983 996 1099 104 -17 138 C ATOM 339 O HIS A 46 87.482 150.579 123.337 1.00 12.03 O ANISOU 339 O HIS A 46 1949 1347 1272 -66 -10 143 O ATOM 340 CB HIS A 46 90.137 149.262 122.360 1.00 11.74 C ANISOU 340 CB HIS A 46 2065 1207 1186 -20 -300 31 C ATOM 341 CG HIS A 46 90.639 148.567 121.176 1.00 11.45 C ANISOU 341 CG HIS A 46 1983 1112 1255 41 -82 104 C ATOM 342 ND1 HIS A 46 91.911 148.752 120.699 1.00 12.30 N ANISOU 342 ND1 HIS A 46 1986 1178 1506 74 -41 131 N ATOM 343 CD2 HIS A 46 90.024 147.707 120.340 1.00 13.49 C ANISOU 343 CD2 HIS A 46 2116 1362 1644 -43 -428 -216 C ATOM 344 CE1 HIS A 46 92.051 148.038 119.603 1.00 13.45 C ANISOU 344 CE1 HIS A 46 2452 1280 1377 88 -54 54 C ATOM 345 NE2 HIS A 46 90.919 147.406 119.359 1.00 14.55 N ANISOU 345 NE2 HIS A 46 2746 1518 1264 297 161 -204 N ATOM 346 N CYS A 47 89.247 151.681 124.138 1.00 10.11 N ANISOU 346 N CYS A 47 1952 803 1084 -30 -68 74 N ATOM 347 CA CYS A 47 88.650 151.750 125.446 1.00 10.24 C ANISOU 347 CA CYS A 47 1796 917 1177 -120 -80 59 C ATOM 348 C CYS A 47 87.499 152.675 125.651 1.00 10.61 C ANISOU 348 C CYS A 47 1882 984 1164 -170 -131 -151 C ATOM 349 O CYS A 47 86.739 152.472 126.578 1.00 9.83 O ANISOU 349 O CYS A 47 1638 1031 1067 -162 0 97 O ATOM 350 CB CYS A 47 89.715 151.976 126.481 1.00 10.95 C ANISOU 350 CB CYS A 47 1729 1146 1282 -208 -115 214 C ATOM 351 SG CYS A 47 90.246 153.706 126.607 1.00 9.70 S ANISOU 351 SG CYS A 47 1731 954 1000 -48 -65 137 S ATOM 352 N GLY A 48 87.425 153.753 124.890 1.00 10.32 N ANISOU 352 N GLY A 48 1912 1023 986 -54 -133 148 N ATOM 353 CA GLY A 48 86.351 154.713 125.074 1.00 10.18 C ANISOU 353 CA GLY A 48 1776 1022 1068 -111 -131 80 C ATOM 354 C GLY A 48 86.441 155.612 126.263 1.00 10.36 C ANISOU 354 C GLY A 48 1808 917 1209 38 -15 232 C ATOM 355 O GLY A 48 85.549 156.410 126.468 1.00 10.03 O ANISOU 355 O GLY A 48 1749 939 1120 -19 -82 107 O ATOM 356 N ALA A 49 87.523 155.586 127.018 1.00 9.84 N ANISOU 356 N ALA A 49 1731 869 1136 74 -142 249 N ATOM 357 CA ALA A 49 87.577 156.435 128.200 1.00 9.84 C ANISOU 357 CA ALA A 49 1673 1001 1063 -62 65 174 C ATOM 358 C ALA A 49 87.606 157.920 127.864 1.00 10.25 C ANISOU 358 C ALA A 49 1629 1042 1221 -161 -166 266 C ATOM 359 O ALA A 49 87.329 158.753 128.709 1.00 10.44 O ANISOU 359 O ALA A 49 1870 962 1133 -92 -52 35 O ATOM 360 CB ALA A 49 88.778 156.070 129.018 1.00 10.85 C ANISOU 360 CB ALA A 49 2208 886 1024 -17 -110 141 C ATOM 361 N CYS A 50 87.964 158.201 126.631 1.00 9.49 N ANISOU 361 N CYS A 50 1712 848 1042 1 38 129 N ATOM 362 CA CYS A 50 88.105 159.527 126.094 1.00 9.95 C ANISOU 362 CA CYS A 50 1617 976 1184 -121 -51 137 C ATOM 363 C CYS A 50 86.846 160.009 125.406 1.00 10.42 C ANISOU 363 C CYS A 50 1990 872 1098 -31 -13 142 C ATOM 364 O CYS A 50 86.867 161.022 124.731 1.00 11.10 O ANISOU 364 O CYS A 50 1985 988 1243 -87 -44 137 O ATOM 365 CB CYS A 50 89.260 159.498 125.125 1.00 10.03 C ANISOU 365 CB CYS A 50 1779 839 1191 -73 -10 93 C ATOM 366 SG CYS A 50 88.846 158.361 123.801 1.00 9.81 S ANISOU 366 SG CYS A 50 1770 988 969 -15 -87 127 S ATOM 367 N THR A 51 85.744 159.301 125.556 1.00 9.92 N ANISOU 367 N THR A 51 1762 1040 969 -66 10 154 N ATOM 368 CA THR A 51 84.551 159.610 124.787 1.00 10.07 C ANISOU 368 CA THR A 51 1557 1146 1120 -51 -24 144 C ATOM 369 C THR A 51 83.994 160.946 125.226 1.00 10.24 C ANISOU 369 C THR A 51 1595 943 1351 -162 -105 198 C ATOM 370 O THR A 51 83.791 161.200 126.388 1.00 11.02 O ANISOU 370 O THR A 51 1859 1193 1133 -38 -87 80 O ATOM 371 CB THR A 51 83.506 158.562 125.003 1.00 10.75 C ANISOU 371 CB THR A 51 1855 1067 1159 37 -65 125 C ATOM 372 OG1 THR A 51 83.968 157.303 124.504 1.00 10.62 O ANISOU 372 OG1 THR A 51 1852 873 1307 -77 -142 24 O ATOM 373 CG2 THR A 51 82.222 158.884 124.276 1.00 10.96 C ANISOU 373 CG2 THR A 51 1620 1265 1278 -227 -109 208 C ATOM 374 N VAL A 52 83.697 161.761 124.232 1.00 10.44 N ANISOU 374 N VAL A 52 1974 944 1048 -88 -130 182 N ATOM 375 CA VAL A 52 82.950 162.983 124.441 1.00 10.83 C ANISOU 375 CA VAL A 52 1808 922 1385 -110 -109 149 C ATOM 376 C VAL A 52 81.787 162.986 123.469 1.00 10.73 C ANISOU 376 C VAL A 52 1639 1098 1340 -80 -57 82 C ATOM 377 O VAL A 52 81.779 162.273 122.500 1.00 11.50 O ANISOU 377 O VAL A 52 2006 1128 1234 -3 -38 126 O ATOM 378 CB VAL A 52 83.826 164.208 124.270 1.00 12.10 C ANISOU 378 CB VAL A 52 2011 844 1740 15 -239 109 C ATOM 379 CG1 VAL A 52 84.958 164.133 125.241 1.00 12.58 C ANISOU 379 CG1 VAL A 52 1967 1212 1598 -24 -228 -87 C ATOM 380 CG2 VAL A 52 84.355 164.312 122.864 1.00 12.80 C ANISOU 380 CG2 VAL A 52 1743 1262 1856 -280 -127 326 C ATOM 381 N ASP A 53 80.833 163.859 123.731 1.00 10.48 N ANISOU 381 N ASP A 53 1582 1127 1272 63 -181 116 N ATOM 382 CA ASP A 53 79.714 164.041 122.835 1.00 10.27 C ANISOU 382 CA ASP A 53 1828 980 1092 -98 -156 86 C ATOM 383 C ASP A 53 79.996 165.237 121.975 1.00 11.85 C ANISOU 383 C ASP A 53 2223 926 1352 -31 -163 148 C ATOM 384 O ASP A 53 80.322 166.283 122.468 1.00 14.17 O ANISOU 384 O ASP A 53 3064 961 1358 -198 -204 137 O ATOM 385 CB ASP A 53 78.429 164.226 123.624 1.00 11.90 C ANISOU 385 CB ASP A 53 2061 1142 1318 -46 -215 -8 C ATOM 386 CG ASP A 53 77.209 163.959 122.847 1.00 12.79 C ANISOU 386 CG ASP A 53 2076 1111 1669 104 -186 135 C ATOM 387 OD1 ASP A 53 76.985 162.801 122.457 1.00 12.00 O ANISOU 387 OD1 ASP A 53 1944 1106 1509 70 -144 244 O ATOM 388 OD2 ASP A 53 76.403 164.873 122.605 1.00 15.67 O ANISOU 388 OD2 ASP A 53 2467 1312 2175 98 -551 -65 O ATOM 389 N LEU A 54 80.043 165.032 120.684 1.00 11.17 N ANISOU 389 N LEU A 54 2274 815 1155 -30 -241 43 N ATOM 390 CA LEU A 54 80.557 166.033 119.788 1.00 11.49 C ANISOU 390 CA LEU A 54 2030 1022 1314 -49 -239 285 C ATOM 391 C LEU A 54 79.623 166.089 118.611 1.00 12.33 C ANISOU 391 C LEU A 54 2477 1050 1155 -124 -57 188 C ATOM 392 O LEU A 54 79.395 165.091 117.942 1.00 12.20 O ANISOU 392 O LEU A 54 2434 996 1203 -76 -102 166 O ATOM 393 CB LEU A 54 81.959 165.648 119.354 1.00 12.89 C ANISOU 393 CB LEU A 54 2583 1096 1220 -133 -362 232 C ATOM 394 CG LEU A 54 82.682 166.672 118.515 1.00 12.93 C ANISOU 394 CG LEU A 54 1855 1412 1641 -55 -119 447 C ATOM 395 CD1 LEU A 54 84.156 166.455 118.693 1.00 14.95 C ANISOU 395 CD1 LEU A 54 2424 1649 1607 -171 51 -155 C ATOM 396 CD2 LEU A 54 82.292 166.599 117.072 1.00 14.52 C ANISOU 396 CD2 LEU A 54 2730 1211 1577 59 136 55 C ATOM 397 N ASP A 55 78.968 167.230 118.463 1.00 12.16 N ANISOU 397 N ASP A 55 2425 922 1272 109 -318 197 N ATOM 398 CA ASP A 55 77.955 167.393 117.442 1.00 12.86 C ANISOU 398 CA ASP A 55 2430 1077 1378 -26 -348 120 C ATOM 399 C ASP A 55 77.015 166.202 117.358 1.00 13.29 C ANISOU 399 C ASP A 55 2347 1351 1351 121 -401 231 C ATOM 400 O ASP A 55 76.692 165.730 116.299 1.00 13.68 O ANISOU 400 O ASP A 55 2500 1159 1537 -73 -399 255 O ATOM 401 CB ASP A 55 78.598 167.677 116.108 1.00 13.50 C ANISOU 401 CB ASP A 55 2314 1398 1414 -166 -344 98 C ATOM 402 CG ASP A 55 79.321 168.985 116.077 1.00 15.30 C ANISOU 402 CG ASP A 55 2599 1642 1571 -350 -136 597 C ATOM 403 OD1 ASP A 55 78.984 169.904 116.864 1.00 18.17 O ANISOU 403 OD1 ASP A 55 3635 1631 1638 -729 -192 138 O ATOM 404 OD2 ASP A 55 80.238 169.160 115.272 1.00 22.68 O ANISOU 404 OD2 ASP A 55 4273 1704 2639 -533 98 732 O ATOM 405 N GLY A 56 76.514 165.788 118.496 1.00 12.66 N ANISOU 405 N GLY A 56 1993 1322 1494 38 -153 124 N ATOM 406 CA GLY A 56 75.482 164.786 118.544 1.00 13.25 C ANISOU 406 CA GLY A 56 2100 1312 1621 247 -19 196 C ATOM 407 C GLY A 56 76.008 163.374 118.348 1.00 12.16 C ANISOU 407 C GLY A 56 1858 1330 1430 -70 15 355 C ATOM 408 O GLY A 56 75.213 162.463 118.118 1.00 14.28 O ANISOU 408 O GLY A 56 2146 1500 1779 -126 -186 487 O ATOM 409 N MET A 57 77.323 163.186 118.441 1.00 11.38 N ANISOU 409 N MET A 57 1967 1168 1186 -164 -206 126 N ATOM 410 CA MET A 57 77.948 161.877 118.231 1.00 11.37 C ANISOU 410 CA MET A 57 1961 1049 1307 -88 -184 120 C ATOM 411 C MET A 57 78.765 161.542 119.431 1.00 11.58 C ANISOU 411 C MET A 57 2169 970 1257 -272 -228 57 C ATOM 412 O MET A 57 79.357 162.423 120.031 1.00 13.29 O ANISOU 412 O MET A 57 2639 996 1412 -122 -384 226 O ATOM 413 CB MET A 57 78.907 161.952 117.082 1.00 12.28 C ANISOU 413 CB MET A 57 2676 932 1054 6 -76 27 C ATOM 414 CG MET A 57 78.249 162.417 115.829 1.00 13.97 C ANISOU 414 CG MET A 57 2811 1206 1290 -87 -76 120 C ATOM 415 SD MET A 57 79.324 162.372 114.403 1.00 13.72 S ANISOU 415 SD MET A 57 2752 1303 1155 27 -65 82 S ATOM 416 CE MET A 57 80.508 163.653 114.853 1.00 16.19 C ANISOU 416 CE MET A 57 2678 1609 1863 68 313 -46 C ATOM 417 N SER A 58 78.945 160.263 119.691 1.00 11.01 N ANISOU 417 N SER A 58 1929 952 1299 -73 -219 237 N ATOM 418 CA SER A 58 79.941 159.820 120.653 1.00 10.79 C ANISOU 418 CA SER A 58 1942 966 1191 -38 -131 164 C ATOM 419 C SER A 58 81.239 159.629 119.938 1.00 10.41 C ANISOU 419 C SER A 58 1791 1045 1116 -148 -122 212 C ATOM 420 O SER A 58 81.318 158.819 119.041 1.00 11.85 O ANISOU 420 O SER A 58 2161 1050 1291 -175 -115 -20 O ATOM 421 CB SER A 58 79.526 158.497 121.263 1.00 11.32 C ANISOU 421 CB SER A 58 1962 992 1344 -111 -68 258 C ATOM 422 OG SER A 58 78.275 158.594 121.907 1.00 11.98 O ANISOU 422 OG SER A 58 1975 1204 1372 -43 -81 248 O ATOM 423 N VAL A 59 82.260 160.351 120.373 1.00 10.72 N ANISOU 423 N VAL A 59 1987 1088 996 -71 -161 127 N ATOM 424 CA VAL A 59 83.542 160.333 119.719 1.00 11.39 C ANISOU 424 CA VAL A 59 1826 1243 1260 34 23 215 C ATOM 425 C VAL A 59 84.619 160.005 120.719 1.00 10.68 C ANISOU 425 C VAL A 59 1791 967 1298 82 82 120 C ATOM 426 O VAL A 59 84.682 160.560 121.816 1.00 11.19 O ANISOU 426 O VAL A 59 1967 1252 1032 130 -76 118 O ATOM 427 CB VAL A 59 83.835 161.697 119.091 1.00 13.20 C ANISOU 427 CB VAL A 59 1868 1774 1370 125 76 698 C ATOM 428 CG1 VAL A 59 85.252 161.813 118.605 1.00 17.38 C ANISOU 428 CG1 VAL A 59 2658 1605 2339 74 -231 681 C ATOM 429 CG2 VAL A 59 82.793 161.960 118.026 1.00 13.26 C ANISOU 429 CG2 VAL A 59 2171 1439 1429 -131 -197 394 C ATOM 430 N LYS A 60 85.485 159.099 120.303 1.00 10.36 N ANISOU 430 N LYS A 60 1740 1059 1137 -115 -167 225 N ATOM 431 CA LYS A 60 86.694 158.822 121.039 1.00 10.58 C ANISOU 431 CA LYS A 60 1712 1040 1266 -32 20 186 C ATOM 432 C LYS A 60 87.705 159.915 120.742 1.00 10.95 C ANISOU 432 C LYS A 60 1880 961 1316 87 -98 167 C ATOM 433 O LYS A 60 88.314 159.949 119.678 1.00 11.50 O ANISOU 433 O LYS A 60 1983 1168 1217 -91 31 131 O ATOM 434 CB LYS A 60 87.228 157.459 120.662 1.00 10.53 C ANISOU 434 CB LYS A 60 1771 912 1317 -60 -41 171 C ATOM 435 CG LYS A 60 86.348 156.351 121.258 1.00 10.45 C ANISOU 435 CG LYS A 60 1921 939 1111 -76 -98 98 C ATOM 436 CD LYS A 60 86.781 154.966 120.852 1.00 11.94 C ANISOU 436 CD LYS A 60 1949 1080 1509 -142 -270 306 C ATOM 437 CE LYS A 60 85.952 153.951 121.568 1.00 12.39 C ANISOU 437 CE LYS A 60 2295 883 1528 -55 0 48 C ATOM 438 NZ LYS A 60 86.340 152.557 121.261 1.00 12.02 N ANISOU 438 NZ LYS A 60 2270 967 1326 -89 -133 -15 N ATOM 439 N SER A 61 87.841 160.843 121.668 1.00 10.17 N ANISOU 439 N SER A 61 1754 996 1111 -108 -59 234 N ATOM 440 CA SER A 61 88.614 162.035 121.435 1.00 11.12 C ANISOU 440 CA SER A 61 2017 1023 1185 -110 -164 273 C ATOM 441 C SER A 61 90.097 161.771 121.350 1.00 10.17 C ANISOU 441 C SER A 61 1800 1057 1009 -142 -34 -15 C ATOM 442 O SER A 61 90.829 162.687 120.951 1.00 11.43 O ANISOU 442 O SER A 61 1932 1067 1343 -189 -48 211 O ATOM 443 CB SER A 61 88.294 163.086 122.475 1.00 11.19 C ANISOU 443 CB SER A 61 2313 936 1001 -230 -171 153 C ATOM 444 OG SER A 61 88.751 162.715 123.746 1.00 11.32 O ANISOU 444 OG SER A 61 1903 1180 1218 -225 -152 247 O ATOM 445 N CYS A 62 90.557 160.566 121.652 1.00 10.31 N ANISOU 445 N CYS A 62 1808 917 1190 -98 -71 174 N ATOM 446 CA CYS A 62 91.926 160.220 121.389 1.00 10.10 C ANISOU 446 CA CYS A 62 1574 1004 1260 -149 -219 228 C ATOM 447 C CYS A 62 92.170 159.859 119.951 1.00 11.25 C ANISOU 447 C CYS A 62 1925 1041 1306 -115 -99 233 C ATOM 448 O CYS A 62 93.310 159.627 119.566 1.00 11.80 O ANISOU 448 O CYS A 62 1900 1273 1307 -57 -111 289 O ATOM 449 CB CYS A 62 92.370 159.037 122.208 1.00 11.41 C ANISOU 449 CB CYS A 62 1889 1196 1250 -238 -104 231 C ATOM 450 SG CYS A 62 91.578 157.500 121.646 1.00 10.16 S ANISOU 450 SG CYS A 62 1805 1001 1054 -63 -20 189 S ATOM 451 N THR A 63 91.105 159.841 119.165 1.00 10.61 N ANISOU 451 N THR A 63 1730 1067 1234 -120 -182 331 N ATOM 452 CA THR A 63 91.204 159.417 117.785 1.00 10.98 C ANISOU 452 CA THR A 63 2002 1013 1156 0 -44 241 C ATOM 453 C THR A 63 90.699 160.529 116.877 1.00 11.37 C ANISOU 453 C THR A 63 1710 1198 1411 -335 0 184 C ATOM 454 O THR A 63 90.062 160.273 115.875 1.00 12.37 O ANISOU 454 O THR A 63 2337 1076 1286 -121 -91 189 O ATOM 455 CB THR A 63 90.450 158.117 117.586 1.00 11.05 C ANISOU 455 CB THR A 63 2035 1124 1040 -89 -237 103 C ATOM 456 OG1 THR A 63 90.851 157.191 118.598 1.00 12.83 O ANISOU 456 OG1 THR A 63 2535 1045 1295 -122 -152 210 O ATOM 457 CG2 THR A 63 90.885 157.443 116.334 1.00 12.74 C ANISOU 457 CG2 THR A 63 2337 1218 1284 -118 -307 126 C ATOM 458 N MET A 64 90.926 161.752 117.300 1.00 11.41 N ANISOU 458 N MET A 64 1911 1190 1233 -120 -81 197 N ATOM 459 CA MET A 64 90.553 162.948 116.574 1.00 12.23 C ANISOU 459 CA MET A 64 2316 1127 1203 -296 -161 211 C ATOM 460 C MET A 64 91.539 164.004 116.990 1.00 12.99 C ANISOU 460 C MET A 64 2264 1279 1391 -155 -99 113 C ATOM 461 O MET A 64 91.951 164.039 118.135 1.00 14.29 O ANISOU 461 O MET A 64 2709 1357 1362 -328 -362 259 O ATOM 462 CB MET A 64 89.144 163.363 116.957 1.00 13.76 C ANISOU 462 CB MET A 64 2131 1416 1679 -162 -155 346 C ATOM 463 CG AMET A 64 88.638 164.543 116.174 0.50 16.73 C ANISOU 463 CG AMET A 64 2635 1169 2549 318 163 434 C ATOM 464 CG BMET A 64 88.626 164.577 116.240 0.50 15.11 C ANISOU 464 CG BMET A 64 2325 1720 1695 109 -27 331 C ATOM 465 SD AMET A 64 86.960 164.968 116.575 0.50 15.07 S ANISOU 465 SD AMET A 64 2142 1871 1711 104 114 5 S ATOM 466 SD BMET A 64 86.955 165.024 116.719 0.50 15.39 S ANISOU 466 SD BMET A 64 2472 1948 1428 -122 -273 322 S ATOM 467 CE AMET A 64 86.428 163.424 117.028 0.50 13.79 C ANISOU 467 CE AMET A 64 1691 1626 1921 340 247 614 C ATOM 468 CE BMET A 64 86.059 164.012 115.618 0.50 13.88 C ANISOU 468 CE BMET A 64 2351 1519 1402 85 12 260 C ATOM 469 N PHE A 65 91.898 164.861 116.064 1.00 12.06 N ANISOU 469 N PHE A 65 2289 1118 1173 -273 -30 234 N ATOM 470 CA PHE A 65 92.713 166.004 116.385 1.00 12.09 C ANISOU 470 CA PHE A 65 2197 1150 1243 -377 146 253 C ATOM 471 C PHE A 65 91.830 167.158 116.750 1.00 13.29 C ANISOU 471 C PHE A 65 2261 1259 1529 -331 74 359 C ATOM 472 O PHE A 65 90.732 167.277 116.247 1.00 12.81 O ANISOU 472 O PHE A 65 2222 1199 1447 -115 3 186 O ATOM 473 CB PHE A 65 93.560 166.374 115.181 1.00 13.16 C ANISOU 473 CB PHE A 65 2380 1280 1337 -44 -196 76 C ATOM 474 CG PHE A 65 94.482 165.279 114.783 1.00 13.12 C ANISOU 474 CG PHE A 65 2073 1299 1612 -239 305 255 C ATOM 475 CD1 PHE A 65 95.569 164.963 115.570 1.00 14.23 C ANISOU 475 CD1 PHE A 65 2257 1351 1798 -171 225 436 C ATOM 476 CD2 PHE A 65 94.264 164.562 113.626 1.00 13.78 C ANISOU 476 CD2 PHE A 65 2263 1097 1876 -265 474 115 C ATOM 477 CE1 PHE A 65 96.434 163.961 115.219 1.00 15.87 C ANISOU 477 CE1 PHE A 65 2208 1436 2383 -212 645 102 C ATOM 478 CE2 PHE A 65 95.104 163.546 113.279 1.00 16.08 C ANISOU 478 CE2 PHE A 65 2282 1530 2298 -476 417 87 C ATOM 479 CZ PHE A 65 96.197 163.241 114.083 1.00 15.83 C ANISOU 479 CZ PHE A 65 2705 1001 2305 -148 1111 57 C ATOM 480 N ALA A 66 92.298 167.999 117.656 1.00 11.88 N ANISOU 480 N ALA A 66 2041 1240 1230 -222 -31 166 N ATOM 481 CA ALA A 66 91.545 169.160 118.046 1.00 12.75 C ANISOU 481 CA ALA A 66 2226 1394 1225 -98 170 197 C ATOM 482 C ALA A 66 91.117 169.997 116.874 1.00 12.93 C ANISOU 482 C ALA A 66 2256 1248 1409 -147 126 120 C ATOM 483 O ALA A 66 90.013 170.505 116.849 1.00 13.26 O ANISOU 483 O ALA A 66 2267 1281 1490 -43 -31 148 O ATOM 484 CB ALA A 66 92.299 170.008 119.039 1.00 14.14 C ANISOU 484 CB ALA A 66 2399 1583 1389 -82 -154 10 C ATOM 485 N VAL A 67 91.969 170.106 115.866 1.00 12.27 N ANISOU 485 N VAL A 67 1985 1290 1386 -19 3 320 N ATOM 486 CA VAL A 67 91.591 170.901 114.727 1.00 13.31 C ANISOU 486 CA VAL A 67 2413 1050 1594 -27 214 148 C ATOM 487 C VAL A 67 90.331 170.372 114.056 1.00 13.55 C ANISOU 487 C VAL A 67 2109 1562 1475 -76 -24 198 C ATOM 488 O VAL A 67 89.605 171.129 113.415 1.00 14.10 O ANISOU 488 O VAL A 67 2319 1286 1753 65 -54 544 O ATOM 489 CB VAL A 67 92.735 171.024 113.707 1.00 13.70 C ANISOU 489 CB VAL A 67 2169 1377 1659 -71 52 416 C ATOM 490 CG1 VAL A 67 93.771 171.964 114.227 1.00 15.11 C ANISOU 490 CG1 VAL A 67 2419 1517 1806 -98 74 149 C ATOM 491 CG2 VAL A 67 93.349 169.699 113.346 1.00 14.39 C ANISOU 491 CG2 VAL A 67 2275 1700 1491 -177 333 348 C ATOM 492 N GLN A 68 90.103 169.075 114.138 1.00 13.16 N ANISOU 492 N GLN A 68 2452 1107 1440 -82 10 239 N ATOM 493 CA GLN A 68 88.927 168.502 113.507 1.00 13.07 C ANISOU 493 CA GLN A 68 2283 1168 1513 -1 -51 198 C ATOM 494 C GLN A 68 87.675 168.960 114.208 1.00 13.64 C ANISOU 494 C GLN A 68 1988 1234 1959 88 -174 351 C ATOM 495 O GLN A 68 86.606 168.845 113.651 1.00 14.45 O ANISOU 495 O GLN A 68 2125 1451 1911 -15 -109 278 O ATOM 496 CB GLN A 68 88.962 166.984 113.541 1.00 14.20 C ANISOU 496 CB GLN A 68 2319 1349 1724 -51 276 93 C ATOM 497 CG GLN A 68 90.003 166.368 112.691 1.00 13.93 C ANISOU 497 CG GLN A 68 2479 1307 1506 -133 78 194 C ATOM 498 CD GLN A 68 90.077 164.876 112.965 1.00 13.29 C ANISOU 498 CD GLN A 68 2035 1416 1597 8 57 -81 C ATOM 499 OE1 GLN A 68 90.957 164.399 113.629 1.00 14.89 O ANISOU 499 OE1 GLN A 68 2649 1451 1553 -41 -37 210 O ATOM 500 NE2 GLN A 68 89.117 164.138 112.436 1.00 16.10 N ANISOU 500 NE2 GLN A 68 2635 1370 2109 -285 -179 361 N ATOM 501 N ALA A 69 87.800 169.457 115.433 1.00 13.01 N ANISOU 501 N ALA A 69 2196 1350 1397 115 -93 219 N ATOM 502 CA ALA A 69 86.633 169.858 116.209 1.00 13.80 C ANISOU 502 CA ALA A 69 2113 1234 1895 -142 -88 454 C ATOM 503 C ALA A 69 86.382 171.358 116.077 1.00 13.52 C ANISOU 503 C ALA A 69 2462 1229 1444 -23 -119 355 C ATOM 504 O ALA A 69 85.593 171.939 116.817 1.00 13.93 O ANISOU 504 O ALA A 69 2266 1500 1523 -62 -6 205 O ATOM 505 CB ALA A 69 86.837 169.483 117.665 1.00 15.73 C ANISOU 505 CB ALA A 69 2266 1598 2111 78 17 810 C ATOM 506 N ASN A 70 87.089 172.025 115.187 1.00 12.94 N ANISOU 506 N ASN A 70 2171 1275 1469 19 35 302 N ATOM 507 CA ASN A 70 86.810 173.432 114.973 1.00 12.03 C ANISOU 507 CA ASN A 70 1911 1108 1552 -59 -107 288 C ATOM 508 C ASN A 70 85.348 173.586 114.657 1.00 12.41 C ANISOU 508 C ASN A 70 2437 1071 1206 -206 -120 173 C ATOM 509 O ASN A 70 84.830 172.873 113.810 1.00 13.33 O ANISOU 509 O ASN A 70 2368 1348 1350 -131 -138 -57 O ATOM 510 CB ASN A 70 87.682 173.941 113.855 1.00 13.48 C ANISOU 510 CB ASN A 70 2198 1300 1621 -148 130 59 C ATOM 511 CG ASN A 70 87.726 175.437 113.803 1.00 14.88 C ANISOU 511 CG ASN A 70 2621 1297 1736 -110 74 208 C ATOM 512 OD1 ASN A 70 87.394 176.102 114.766 1.00 14.21 O ANISOU 512 OD1 ASN A 70 2527 1248 1624 1 -60 165 O ATOM 513 ND2 ASN A 70 88.222 175.979 112.706 1.00 16.97 N ANISOU 513 ND2 ASN A 70 3181 1414 1849 -362 483 86 N ATOM 514 N GLY A 71 84.685 174.508 115.328 1.00 12.13 N ANISOU 514 N GLY A 71 2021 1142 1442 -233 -38 23 N ATOM 515 CA GLY A 71 83.287 174.771 115.065 1.00 12.81 C ANISOU 515 CA GLY A 71 2017 1212 1638 -99 -31 175 C ATOM 516 C GLY A 71 82.334 173.791 115.732 1.00 12.54 C ANISOU 516 C GLY A 71 2196 1168 1400 -51 -187 129 C ATOM 517 O GLY A 71 81.128 173.968 115.652 1.00 15.81 O ANISOU 517 O GLY A 71 2173 1375 2457 35 -8 511 O ATOM 518 N ALA A 72 82.841 172.774 116.415 1.00 13.00 N ANISOU 518 N ALA A 72 2289 1216 1433 -173 -13 130 N ATOM 519 CA ALA A 72 82.005 171.736 116.994 1.00 12.58 C ANISOU 519 CA ALA A 72 1997 1221 1562 80 -87 63 C ATOM 520 C ALA A 72 81.435 172.190 118.302 1.00 12.73 C ANISOU 520 C ALA A 72 2406 1080 1351 -32 -403 28 C ATOM 521 O ALA A 72 81.899 173.148 118.916 1.00 14.44 O ANISOU 521 O ALA A 72 2594 1539 1350 -264 -24 57 O ATOM 522 CB ALA A 72 82.805 170.450 117.198 1.00 15.10 C ANISOU 522 CB ALA A 72 2642 1057 2037 -328 -105 0 C ATOM 523 N SER A 73 80.395 171.488 118.701 1.00 12.39 N ANISOU 523 N SER A 73 2243 1017 1446 -161 -238 203 N ATOM 524 CA SER A 73 79.888 171.563 120.043 1.00 11.54 C ANISOU 524 CA SER A 73 2242 923 1218 63 -40 204 C ATOM 525 C SER A 73 80.214 170.266 120.718 1.00 12.68 C ANISOU 525 C SER A 73 2481 1010 1324 77 -220 167 C ATOM 526 O SER A 73 79.762 169.228 120.315 1.00 14.21 O ANISOU 526 O SER A 73 2624 1033 1739 -99 -588 242 O ATOM 527 CB ASER A 73 78.379 171.780 120.013 0.50 16.18 C ANISOU 527 CB ASER A 73 3483 1130 1534 71 31 326 C ATOM 528 CB BSER A 73 78.381 171.786 120.038 0.50 15.75 C ANISOU 528 CB BSER A 73 3231 1238 1515 31 -73 370 C ATOM 529 OG ASER A 73 78.068 173.029 119.425 0.50 17.98 O ANISOU 529 OG ASER A 73 2196 1621 3012 350 -68 680 O ATOM 530 OG BSER A 73 77.901 171.911 121.366 0.50 19.05 O ANISOU 530 OG BSER A 73 2847 2937 1455 305 -98 553 O ATOM 531 N ILE A 74 80.933 170.384 121.810 1.00 11.49 N ANISOU 531 N ILE A 74 2219 988 1159 -46 -171 125 N ATOM 532 CA ILE A 74 81.366 169.233 122.557 1.00 11.42 C ANISOU 532 CA ILE A 74 2187 1077 1072 -34 -143 131 C ATOM 533 C ILE A 74 80.731 169.327 123.915 1.00 11.78 C ANISOU 533 C ILE A 74 2298 1022 1155 31 -20 129 C ATOM 534 O ILE A 74 80.709 170.385 124.519 1.00 13.00 O ANISOU 534 O ILE A 74 2736 1024 1176 -54 -46 31 O ATOM 535 CB ILE A 74 82.878 169.234 122.715 1.00 12.05 C ANISOU 535 CB ILE A 74 2304 1106 1167 -83 -125 199 C ATOM 536 CG1 ILE A 74 83.529 169.099 121.356 1.00 13.91 C ANISOU 536 CG1 ILE A 74 2333 1263 1688 10 -215 255 C ATOM 537 CG2 ILE A 74 83.338 168.093 123.599 1.00 15.40 C ANISOU 537 CG2 ILE A 74 3204 1097 1551 -125 -456 430 C ATOM 538 CD1 ILE A 74 85.006 169.167 121.340 1.00 14.40 C ANISOU 538 CD1 ILE A 74 2290 1538 1641 -115 -74 174 C ATOM 539 N THR A 75 80.344 168.177 124.445 1.00 11.14 N ANISOU 539 N THR A 75 2186 888 1158 -6 -252 68 N ATOM 540 CA THR A 75 79.995 168.047 125.835 1.00 11.17 C ANISOU 540 CA THR A 75 1946 1133 1164 -78 -60 137 C ATOM 541 C THR A 75 80.947 167.023 126.416 1.00 11.73 C ANISOU 541 C THR A 75 2247 892 1315 19 -93 91 C ATOM 542 O THR A 75 81.146 165.947 125.849 1.00 12.26 O ANISOU 542 O THR A 75 2266 1046 1347 -109 -320 88 O ATOM 543 CB THR A 75 78.582 167.562 125.995 1.00 12.33 C ANISOU 543 CB THR A 75 2232 1182 1268 167 -193 340 C ATOM 544 OG1 THR A 75 77.652 168.361 125.256 1.00 13.77 O ANISOU 544 OG1 THR A 75 2360 1259 1613 -23 -294 284 O ATOM 545 CG2 THR A 75 78.141 167.600 127.438 1.00 13.75 C ANISOU 545 CG2 THR A 75 2161 1492 1570 -74 -168 48 C ATOM 546 N THR A 76 81.537 167.390 127.526 1.00 11.80 N ANISOU 546 N THR A 76 2356 973 1152 0 -295 68 N ATOM 547 CA THR A 76 82.351 166.483 128.283 1.00 11.81 C ANISOU 547 CA THR A 76 2260 1013 1212 140 -144 153 C ATOM 548 C THR A 76 81.653 166.198 129.581 1.00 12.19 C ANISOU 548 C THR A 76 2061 1221 1350 -32 -304 -143 C ATOM 549 O THR A 76 80.588 166.761 129.852 1.00 11.38 O ANISOU 549 O THR A 76 2154 1116 1050 -15 -151 147 O ATOM 550 CB THR A 76 83.726 167.068 128.571 1.00 11.72 C ANISOU 550 CB THR A 76 2010 1254 1187 -31 -164 248 C ATOM 551 OG1 THR A 76 83.588 168.189 129.439 1.00 13.16 O ANISOU 551 OG1 THR A 76 2518 1067 1412 -99 -322 23 O ATOM 552 CG2 THR A 76 84.421 167.540 127.319 1.00 13.11 C ANISOU 552 CG2 THR A 76 2260 1202 1519 -194 -76 174 C ATOM 553 N ILE A 77 82.219 165.309 130.397 1.00 10.57 N ANISOU 553 N ILE A 77 1928 921 1168 231 -241 179 N ATOM 554 CA ILE A 77 81.496 164.945 131.574 1.00 10.82 C ANISOU 554 CA ILE A 77 2109 1040 961 -120 -83 174 C ATOM 555 C ILE A 77 81.208 166.137 132.461 1.00 10.61 C ANISOU 555 C ILE A 77 1932 1005 1093 3 -87 182 C ATOM 556 O ILE A 77 80.183 166.160 133.118 1.00 11.28 O ANISOU 556 O ILE A 77 1941 1080 1263 6 24 104 O ATOM 557 CB ILE A 77 82.267 163.863 132.302 1.00 11.12 C ANISOU 557 CB ILE A 77 2207 939 1077 -71 -285 137 C ATOM 558 CG1 ILE A 77 81.428 163.244 133.395 1.00 11.76 C ANISOU 558 CG1 ILE A 77 2157 1061 1250 96 -229 313 C ATOM 559 CG2 ILE A 77 83.557 164.378 132.844 1.00 11.79 C ANISOU 559 CG2 ILE A 77 2028 1143 1307 27 -153 170 C ATOM 560 CD1 ILE A 77 80.179 162.612 132.928 1.00 11.94 C ANISOU 560 CD1 ILE A 77 2036 1178 1319 -262 -215 255 C ATOM 561 N GLU A 78 82.087 167.131 132.439 1.00 11.34 N ANISOU 561 N GLU A 78 1943 1054 1310 -102 -86 -38 N ATOM 562 CA GLU A 78 81.928 168.320 133.234 1.00 12.03 C ANISOU 562 CA GLU A 78 2272 948 1349 -57 -164 -7 C ATOM 563 C GLU A 78 80.673 169.071 132.845 1.00 12.44 C ANISOU 563 C GLU A 78 2190 1042 1493 -142 -8 142 C ATOM 564 O GLU A 78 80.191 169.880 133.619 1.00 14.03 O ANISOU 564 O GLU A 78 2427 1208 1693 113 -258 -68 O ATOM 565 CB GLU A 78 83.161 169.204 133.066 1.00 13.62 C ANISOU 565 CB GLU A 78 2590 961 1623 20 -322 -153 C ATOM 566 CG GLU A 78 84.418 168.601 133.665 1.00 13.08 C ANISOU 566 CG GLU A 78 2136 1324 1507 -24 -173 43 C ATOM 567 CD GLU A 78 85.265 167.769 132.721 1.00 13.01 C ANISOU 567 CD GLU A 78 2685 1014 1242 -46 -86 57 C ATOM 568 OE1 GLU A 78 84.785 167.372 131.640 1.00 12.28 O ANISOU 568 OE1 GLU A 78 2141 1194 1328 15 -130 73 O ATOM 569 OE2 GLU A 78 86.461 167.573 133.023 1.00 13.78 O ANISOU 569 OE2 GLU A 78 2300 1270 1665 107 -296 -3 O ATOM 570 N GLY A 79 80.201 168.855 131.629 1.00 12.25 N ANISOU 570 N GLY A 79 2113 1155 1385 209 -44 203 N ATOM 571 CA GLY A 79 79.035 169.527 131.138 1.00 12.59 C ANISOU 571 CA GLY A 79 2123 1272 1388 48 -120 156 C ATOM 572 C GLY A 79 77.721 168.856 131.433 1.00 13.19 C ANISOU 572 C GLY A 79 2093 1363 1552 88 -434 221 C ATOM 573 O GLY A 79 76.693 169.360 131.054 1.00 15.86 O ANISOU 573 O GLY A 79 2596 1228 2203 76 -564 414 O TER END