ATOM 1 N PRO A 11 14.215 12.398 36.931 1.00 20.06 N ANISOU 1 N PRO A 11 2231 2999 2390 -98 348 -248 N ATOM 2 CA PRO A 11 13.285 12.391 35.842 1.00 17.93 C ANISOU 2 CA PRO A 11 2048 2587 2175 -39 253 -322 C ATOM 3 C PRO A 11 13.923 12.322 34.472 1.00 14.43 C ANISOU 3 C PRO A 11 1633 2027 1822 -1 227 -388 C ATOM 4 O PRO A 11 13.231 11.990 33.495 1.00 13.66 O ANISOU 4 O PRO A 11 1593 1904 1692 36 172 -624 O ATOM 5 CB PRO A 11 12.563 13.711 35.993 1.00 20.65 C ANISOU 5 CB PRO A 11 2529 3040 2276 86 243 -142 C ATOM 6 CG PRO A 11 13.443 14.548 36.678 1.00 21.71 C ANISOU 6 CG PRO A 11 2533 2675 3038 94 341 -308 C ATOM 7 CD PRO A 11 14.143 13.681 37.646 1.00 22.15 C ANISOU 7 CD PRO A 11 2606 3244 2565 -135 126 -359 C ATOM 8 N LEU A 12 15.200 12.642 34.369 1.00 14.14 N ANISOU 8 N LEU A 12 1598 2043 1729 -97 170 -518 N ATOM 9 CA LEU A 12 15.950 12.596 33.097 1.00 13.73 C ANISOU 9 CA LEU A 12 1578 2008 1630 -9 119 -662 C ATOM 10 C LEU A 12 17.335 12.061 33.337 1.00 14.12 C ANISOU 10 C LEU A 12 1553 2155 1654 -105 54 -587 C ATOM 11 O LEU A 12 18.081 12.565 34.189 1.00 17.23 O ANISOU 11 O LEU A 12 1799 2658 2087 69 -44 -998 O ATOM 12 CB LEU A 12 16.026 13.970 32.478 1.00 13.63 C ANISOU 12 CB LEU A 12 1488 2093 1598 -190 78 -667 C ATOM 13 CG LEU A 12 16.732 14.116 31.151 1.00 14.12 C ANISOU 13 CG LEU A 12 1513 2044 1808 -203 291 -365 C ATOM 14 CD1 LEU A 12 16.094 13.257 30.046 1.00 16.71 C ANISOU 14 CD1 LEU A 12 2183 2432 1733 -184 7 -466 C ATOM 15 CD2 LEU A 12 16.913 15.581 30.702 1.00 17.05 C ANISOU 15 CD2 LEU A 12 1928 2083 2464 -270 238 -385 C ATOM 16 N MET A 13 17.652 10.951 32.687 1.00 13.75 N ANISOU 16 N MET A 13 1571 2058 1595 43 284 -492 N ATOM 17 CA MET A 13 18.978 10.331 32.820 1.00 13.65 C ANISOU 17 CA MET A 13 1559 2150 1478 44 69 -393 C ATOM 18 C MET A 13 19.470 10.046 31.397 1.00 11.69 C ANISOU 18 C MET A 13 1435 1852 1152 65 22 -230 C ATOM 19 O MET A 13 18.705 9.746 30.509 1.00 12.29 O ANISOU 19 O MET A 13 1203 2083 1381 133 109 -479 O ATOM 20 CB MET A 13 18.865 9.008 33.567 1.00 16.44 C ANISOU 20 CB MET A 13 1882 2471 1891 167 232 -223 C ATOM 21 CG MET A 13 20.214 8.359 34.024 1.00 19.45 C ANISOU 21 CG MET A 13 2421 2591 2374 49 205 -185 C ATOM 22 SD MET A 13 20.883 7.194 32.833 1.00 26.59 S ANISOU 22 SD MET A 13 3386 3426 3291 299 295 119 S ATOM 23 CE MET A 13 20.125 5.658 33.387 1.00 26.66 C ANISOU 23 CE MET A 13 3507 3325 3296 59 139 582 C ATOM 24 N VAL A 14 20.771 10.125 31.224 1.00 11.13 N ANISOU 24 N VAL A 14 1326 1734 1166 68 100 -150 N ATOM 25 CA VAL A 14 21.425 9.848 29.950 1.00 10.97 C ANISOU 25 CA VAL A 14 1238 1714 1215 47 14 -124 C ATOM 26 C VAL A 14 22.463 8.770 30.181 1.00 10.90 C ANISOU 26 C VAL A 14 1268 1703 1170 60 144 -180 C ATOM 27 O VAL A 14 23.227 8.880 31.139 1.00 12.70 O ANISOU 27 O VAL A 14 1470 2032 1320 253 -152 -288 O ATOM 28 CB VAL A 14 22.037 11.118 29.313 1.00 11.21 C ANISOU 28 CB VAL A 14 1432 1619 1206 -127 -40 -114 C ATOM 29 CG1 VAL A 14 22.676 10.733 27.981 1.00 12.84 C ANISOU 29 CG1 VAL A 14 1338 2161 1378 35 250 129 C ATOM 30 CG2 VAL A 14 20.958 12.167 29.107 1.00 12.26 C ANISOU 30 CG2 VAL A 14 1461 1656 1538 -91 -149 49 C ATOM 31 N LYS A 15 22.470 7.732 29.318 1.00 10.67 N ANISOU 31 N LYS A 15 1282 1683 1086 155 109 -202 N ATOM 32 CA ALYS A 15 23.464 6.660 29.441 0.50 11.80 C ANISOU 32 CA ALYS A 15 1464 1784 1234 148 78 -95 C ATOM 33 C LYS A 15 24.073 6.419 28.076 1.00 11.63 C ANISOU 33 C LYS A 15 1316 1923 1178 145 62 -171 C ATOM 34 O LYS A 15 23.358 6.348 27.075 1.00 12.34 O ANISOU 34 O LYS A 15 1321 2375 990 263 -56 -351 O ATOM 35 CB ALYS A 15 22.839 5.375 29.950 0.50 12.81 C ANISOU 35 CB ALYS A 15 1621 1877 1369 115 186 -38 C ATOM 36 CG ALYS A 15 23.871 4.321 30.252 0.50 15.07 C ANISOU 36 CG ALYS A 15 2020 2037 1669 63 9 -21 C ATOM 37 CD ALYS A 15 23.275 3.066 30.906 0.50 16.23 C ANISOU 37 CD ALYS A 15 2182 2029 1954 -92 72 103 C ATOM 38 CE ALYS A 15 24.389 2.084 31.375 0.50 18.08 C ANISOU 38 CE ALYS A 15 2258 2143 2469 -128 20 5 C ATOM 39 NZ ALYS A 15 23.994 1.104 32.448 0.50 21.26 N ANISOU 39 NZ ALYS A 15 2877 2439 2761 -43 -9 131 N ATOM 40 N VAL A 16 25.399 6.307 28.043 1.00 10.00 N ANISOU 40 N VAL A 16 1210 1760 827 317 35 -183 N ATOM 41 CA VAL A 16 26.114 6.208 26.774 1.00 9.96 C ANISOU 41 CA VAL A 16 1243 1555 984 243 62 -123 C ATOM 42 C VAL A 16 27.119 5.054 26.868 1.00 10.05 C ANISOU 42 C VAL A 16 1242 1479 1096 343 68 -27 C ATOM 43 O VAL A 16 27.856 4.907 27.831 1.00 10.50 O ANISOU 43 O VAL A 16 1265 1713 1011 373 -41 14 O ATOM 44 CB VAL A 16 26.859 7.530 26.465 1.00 10.66 C ANISOU 44 CB VAL A 16 1413 1609 1027 240 2 -161 C ATOM 45 CG1 VAL A 16 27.404 7.534 25.038 1.00 11.25 C ANISOU 45 CG1 VAL A 16 1456 2025 794 348 100 -81 C ATOM 46 CG2 VAL A 16 25.939 8.773 26.645 1.00 12.16 C ANISOU 46 CG2 VAL A 16 1979 1346 1295 467 -187 -126 C ATOM 47 N LEU A 17 27.099 4.233 25.843 1.00 10.07 N ANISOU 47 N LEU A 17 1391 1454 978 348 -166 -67 N ATOM 48 CA LEU A 17 28.021 3.102 25.653 1.00 9.96 C ANISOU 48 CA LEU A 17 1281 1436 1067 277 44 70 C ATOM 49 C LEU A 17 28.925 3.323 24.429 1.00 9.65 C ANISOU 49 C LEU A 17 1254 1328 1084 295 106 52 C ATOM 50 O LEU A 17 28.499 3.937 23.456 1.00 10.32 O ANISOU 50 O LEU A 17 1333 1498 1090 361 94 142 O ATOM 51 CB LEU A 17 27.234 1.792 25.488 1.00 11.64 C ANISOU 51 CB LEU A 17 1590 1582 1248 216 -43 37 C ATOM 52 CG LEU A 17 26.345 1.401 26.660 1.00 12.89 C ANISOU 52 CG LEU A 17 1711 1790 1394 176 74 128 C ATOM 53 CD1 LEU A 17 25.641 0.051 26.350 1.00 15.73 C ANISOU 53 CD1 LEU A 17 2226 1676 2073 -191 182 227 C ATOM 54 CD2 LEU A 17 27.185 1.296 27.940 1.00 15.89 C ANISOU 54 CD2 LEU A 17 2243 2297 1496 -98 -199 509 C ATOM 55 N ASP A 18 30.103 2.718 24.465 1.00 10.21 N ANISOU 55 N ASP A 18 1397 1324 1156 471 202 292 N ATOM 56 CA ASP A 18 31.096 2.769 23.390 1.00 10.00 C ANISOU 56 CA ASP A 18 1429 1266 1102 253 158 120 C ATOM 57 C ASP A 18 31.161 1.372 22.739 1.00 9.66 C ANISOU 57 C ASP A 18 1321 1254 1094 238 180 91 C ATOM 58 O ASP A 18 31.525 0.372 23.390 1.00 10.53 O ANISOU 58 O ASP A 18 1426 1399 1175 370 42 272 O ATOM 59 CB ASP A 18 32.426 3.189 23.992 1.00 11.18 C ANISOU 59 CB ASP A 18 1674 1407 1165 250 130 -58 C ATOM 60 CG ASP A 18 33.559 3.262 22.990 1.00 10.96 C ANISOU 60 CG ASP A 18 1309 1379 1476 293 72 207 C ATOM 61 OD1 ASP A 18 33.616 2.399 22.104 1.00 11.55 O ANISOU 61 OD1 ASP A 18 1471 1452 1464 357 192 -93 O ATOM 62 OD2 ASP A 18 34.417 4.195 23.137 1.00 13.29 O ANISOU 62 OD2 ASP A 18 1505 2040 1503 70 -137 -116 O ATOM 63 N ALA A 19 30.704 1.302 21.489 1.00 9.91 N ANISOU 63 N ALA A 19 1476 1200 1086 393 -2 210 N ATOM 64 CA ALA A 19 30.612 0.082 20.730 1.00 9.58 C ANISOU 64 CA ALA A 19 1435 1124 1080 258 91 226 C ATOM 65 C ALA A 19 31.959 -0.451 20.217 1.00 9.76 C ANISOU 65 C ALA A 19 1446 1121 1140 232 157 210 C ATOM 66 O ALA A 19 32.018 -1.586 19.731 1.00 11.07 O ANISOU 66 O ALA A 19 1579 1167 1457 324 112 163 O ATOM 67 CB ALA A 19 29.665 0.276 19.567 1.00 11.34 C ANISOU 67 CB ALA A 19 1702 1624 983 379 -138 126 C ATOM 68 N VAL A 20 32.982 0.408 20.272 1.00 9.77 N ANISOU 68 N VAL A 20 1437 1010 1264 307 116 -14 N ATOM 69 CA VAL A 20 34.338 0.032 19.865 1.00 11.67 C ANISOU 69 CA VAL A 20 1588 1429 1414 259 220 15 C ATOM 70 C VAL A 20 35.084 -0.676 20.984 1.00 13.00 C ANISOU 70 C VAL A 20 1736 1477 1725 240 161 30 C ATOM 71 O VAL A 20 35.734 -1.683 20.728 1.00 15.46 O ANISOU 71 O VAL A 20 2124 1849 1902 453 -18 272 O ATOM 72 CB VAL A 20 35.163 1.269 19.362 1.00 11.39 C ANISOU 72 CB VAL A 20 1463 1319 1543 248 274 45 C ATOM 73 CG1 VAL A 20 36.630 0.896 19.143 1.00 15.38 C ANISOU 73 CG1 VAL A 20 1428 2345 2071 320 586 136 C ATOM 74 CG2 VAL A 20 34.543 1.854 18.119 1.00 14.01 C ANISOU 74 CG2 VAL A 20 2151 1749 1420 204 94 164 C ATOM 75 N ARG A 21 34.935 -0.143 22.196 1.00 11.58 N ANISOU 75 N ARG A 21 1347 1700 1353 254 -7 174 N ATOM 76 CA AARG A 21 35.616 -0.619 23.424 0.50 12.91 C ANISOU 76 CA AARG A 21 1589 1694 1621 237 -28 135 C ATOM 77 C ARG A 21 34.817 -1.682 24.155 1.00 12.45 C ANISOU 77 C ARG A 21 1541 1572 1615 218 -12 43 C ATOM 78 O ARG A 21 35.351 -2.411 24.950 1.00 14.70 O ANISOU 78 O ARG A 21 1791 1968 1826 388 -125 291 O ATOM 79 CB AARG A 21 35.807 0.556 24.422 0.50 14.38 C ANISOU 79 CB AARG A 21 1635 1970 1856 192 -45 148 C ATOM 80 CG AARG A 21 36.778 1.621 23.978 0.50 16.99 C ANISOU 80 CG AARG A 21 2251 1976 2228 36 -115 -164 C ATOM 81 CD AARG A 21 36.706 2.853 24.907 0.50 18.69 C ANISOU 81 CD AARG A 21 2441 2187 2472 172 -76 -206 C ATOM 82 NE AARG A 21 37.870 3.701 24.760 0.50 22.38 N ANISOU 82 NE AARG A 21 2784 2697 3022 34 -45 -51 N ATOM 83 CZ AARG A 21 39.079 3.420 25.253 0.50 24.80 C ANISOU 83 CZ AARG A 21 2958 3160 3304 40 -166 55 C ATOM 84 NH1AARG A 21 39.293 2.285 25.921 0.50 28.44 N ANISOU 84 NH1AARG A 21 3659 3516 3629 -18 -41 107 N ATOM 85 NH2AARG A 21 40.087 4.263 25.060 0.50 25.08 N ANISOU 85 NH2AARG A 21 3136 3061 3330 19 43 71 N ATOM 86 N GLY A 22 33.512 -1.714 23.935 1.00 10.60 N ANISOU 86 N GLY A 22 1491 1225 1308 210 -135 91 N ATOM 87 CA GLY A 22 32.644 -2.535 24.790 1.00 11.77 C ANISOU 87 CA GLY A 22 1673 1321 1474 126 -38 43 C ATOM 88 C GLY A 22 32.659 -2.106 26.250 1.00 9.55 C ANISOU 88 C GLY A 22 1322 988 1316 166 -89 127 C ATOM 89 O GLY A 22 32.871 -2.911 27.184 1.00 11.40 O ANISOU 89 O GLY A 22 1876 1076 1379 121 -318 178 O ATOM 90 N SER A 23 32.377 -0.825 26.439 1.00 10.18 N ANISOU 90 N SER A 23 1622 945 1301 163 -175 16 N ATOM 91 CA ASER A 23 32.513 -0.188 27.733 0.50 10.69 C ANISOU 91 CA ASER A 23 1670 1068 1322 152 -199 43 C ATOM 92 C SER A 23 31.548 0.967 27.833 1.00 10.68 C ANISOU 92 C SER A 23 1715 1065 1277 187 -266 -87 C ATOM 93 O SER A 23 31.067 1.461 26.807 1.00 12.46 O ANISOU 93 O SER A 23 2057 1372 1302 349 -224 132 O ATOM 94 CB ASER A 23 33.903 0.415 27.849 0.50 11.50 C ANISOU 94 CB ASER A 23 1767 1149 1450 170 -324 -74 C ATOM 95 OG ASER A 23 34.018 1.514 26.968 0.50 12.41 O ANISOU 95 OG ASER A 23 1613 1308 1795 -124 32 189 O ATOM 96 N PRO A 24 31.303 1.434 29.045 1.00 11.46 N ANISOU 96 N PRO A 24 1774 1266 1312 162 -128 151 N ATOM 97 CA PRO A 24 30.638 2.729 29.165 1.00 11.84 C ANISOU 97 CA PRO A 24 1704 1391 1400 192 0 -50 C ATOM 98 C PRO A 24 31.442 3.823 28.443 1.00 11.74 C ANISOU 98 C PRO A 24 1678 1319 1463 268 3 83 C ATOM 99 O PRO A 24 32.672 3.696 28.300 1.00 12.68 O ANISOU 99 O PRO A 24 1543 1521 1751 319 -201 149 O ATOM 100 CB PRO A 24 30.592 2.981 30.656 1.00 12.78 C ANISOU 100 CB PRO A 24 1932 1484 1437 322 8 -31 C ATOM 101 CG PRO A 24 31.010 1.789 31.267 1.00 17.90 C ANISOU 101 CG PRO A 24 2916 2247 1638 529 -132 76 C ATOM 102 CD PRO A 24 31.656 0.865 30.338 1.00 12.22 C ANISOU 102 CD PRO A 24 2065 1179 1398 148 -194 19 C ATOM 103 N ALA A 25 30.760 4.817 27.891 1.00 10.94 N ANISOU 103 N ALA A 25 1546 1199 1412 302 69 -36 N ATOM 104 CA ALA A 25 31.413 5.965 27.321 1.00 10.75 C ANISOU 104 CA ALA A 25 1521 1207 1354 205 -4 -21 C ATOM 105 C ALA A 25 31.509 6.997 28.437 1.00 10.47 C ANISOU 105 C ALA A 25 1520 1190 1266 187 -41 13 C ATOM 106 O ALA A 25 30.526 7.587 28.855 1.00 11.37 O ANISOU 106 O ALA A 25 1447 1282 1588 214 168 -283 O ATOM 107 CB ALA A 25 30.639 6.506 26.122 1.00 11.47 C ANISOU 107 CB ALA A 25 1573 1347 1436 117 -14 -22 C ATOM 108 N ILE A 26 32.729 7.192 28.903 1.00 10.23 N ANISOU 108 N ILE A 26 1471 1194 1219 180 -191 -98 N ATOM 109 CA ILE A 26 33.031 8.021 30.108 1.00 12.36 C ANISOU 109 CA ILE A 26 1752 1560 1383 150 -248 0 C ATOM 110 C ILE A 26 33.356 9.438 29.708 1.00 11.32 C ANISOU 110 C ILE A 26 1599 1385 1317 156 -202 -34 C ATOM 111 O ILE A 26 33.974 9.661 28.703 1.00 12.05 O ANISOU 111 O ILE A 26 1620 1570 1385 124 -124 -149 O ATOM 112 CB ILE A 26 34.196 7.390 30.926 1.00 13.57 C ANISOU 112 CB ILE A 26 2116 1556 1483 168 -314 146 C ATOM 113 CG1 ILE A 26 33.852 5.941 31.239 1.00 15.32 C ANISOU 113 CG1 ILE A 26 2467 1715 1638 492 -407 80 C ATOM 114 CG2 ILE A 26 34.568 8.171 32.141 1.00 16.67 C ANISOU 114 CG2 ILE A 26 2188 2184 1959 214 -409 -55 C ATOM 115 CD1 ILE A 26 35.110 5.253 31.767 1.00 19.00 C ANISOU 115 CD1 ILE A 26 2381 2570 2267 403 -418 184 C ATOM 116 N ASN A 27 32.954 10.396 30.540 1.00 11.88 N ANISOU 116 N ASN A 27 1621 1568 1325 221 -176 -81 N ATOM 117 CA ASN A 27 33.311 11.796 30.326 1.00 12.76 C ANISOU 117 CA ASN A 27 1722 1557 1569 114 -127 -30 C ATOM 118 C ASN A 27 32.751 12.325 28.999 1.00 11.88 C ANISOU 118 C ASN A 27 1704 1323 1486 101 -111 -91 C ATOM 119 O ASN A 27 33.338 13.192 28.365 1.00 13.35 O ANISOU 119 O ASN A 27 1638 1699 1733 -14 22 92 O ATOM 120 CB ASN A 27 34.849 12.012 30.384 1.00 15.36 C ANISOU 120 CB ASN A 27 1870 1872 2092 -113 -256 -51 C ATOM 121 CG ASN A 27 35.436 11.748 31.747 1.00 21.29 C ANISOU 121 CG ASN A 27 2828 2712 2546 88 -19 94 C ATOM 122 OD1 ASN A 27 34.819 12.038 32.762 1.00 29.05 O ANISOU 122 OD1 ASN A 27 3898 4113 3024 -136 16 -61 O ATOM 123 ND2 ASN A 27 36.653 11.159 31.772 1.00 26.74 N ANISOU 123 ND2 ASN A 27 2879 3604 3677 -176 -38 -1 N ATOM 124 N VAL A 28 31.562 11.883 28.641 1.00 11.08 N ANISOU 124 N VAL A 28 1584 1265 1359 134 -118 27 N ATOM 125 CA VAL A 28 30.861 12.453 27.478 1.00 11.32 C ANISOU 125 CA VAL A 28 1697 1218 1383 136 -48 -21 C ATOM 126 C VAL A 28 30.087 13.677 27.949 1.00 11.11 C ANISOU 126 C VAL A 28 1545 1365 1311 147 8 -52 C ATOM 127 O VAL A 28 29.234 13.547 28.819 1.00 11.66 O ANISOU 127 O VAL A 28 1741 1210 1479 331 195 76 O ATOM 128 CB VAL A 28 29.892 11.438 26.822 1.00 11.51 C ANISOU 128 CB VAL A 28 1722 1185 1464 224 8 -103 C ATOM 129 CG1 VAL A 28 29.167 12.090 25.646 1.00 12.13 C ANISOU 129 CG1 VAL A 28 1897 1529 1183 356 -263 -27 C ATOM 130 CG2 VAL A 28 30.622 10.148 26.390 1.00 12.87 C ANISOU 130 CG2 VAL A 28 2122 1338 1428 443 -42 -25 C ATOM 131 N ALA A 29 30.303 14.814 27.288 1.00 10.12 N ANISOU 131 N ALA A 29 1415 1180 1249 138 -19 -214 N ATOM 132 CA ALA A 29 29.550 16.029 27.620 1.00 9.94 C ANISOU 132 CA ALA A 29 1377 1182 1216 143 -66 -194 C ATOM 133 C ALA A 29 28.179 15.942 26.996 1.00 9.17 C ANISOU 133 C ALA A 29 1294 985 1205 156 51 -209 C ATOM 134 O ALA A 29 28.010 15.469 25.870 1.00 10.78 O ANISOU 134 O ALA A 29 1537 1526 1029 18 97 -247 O ATOM 135 CB ALA A 29 30.275 17.283 27.123 1.00 10.62 C ANISOU 135 CB ALA A 29 1451 1188 1393 -2 -85 -55 C ATOM 136 N VAL A 30 27.189 16.406 27.768 1.00 9.78 N ANISOU 136 N VAL A 30 1403 1326 986 40 63 -328 N ATOM 137 CA VAL A 30 25.789 16.384 27.358 1.00 10.11 C ANISOU 137 CA VAL A 30 1384 1241 1214 91 -87 -342 C ATOM 138 C VAL A 30 25.206 17.760 27.725 1.00 9.36 C ANISOU 138 C VAL A 30 1317 1158 1079 32 -110 -308 C ATOM 139 O VAL A 30 25.311 18.241 28.863 1.00 11.25 O ANISOU 139 O VAL A 30 1455 1497 1322 95 -250 -356 O ATOM 140 CB VAL A 30 25.011 15.267 28.118 1.00 10.67 C ANISOU 140 CB VAL A 30 1401 1529 1122 -52 114 -355 C ATOM 141 CG1 VAL A 30 23.471 15.337 27.794 1.00 14.07 C ANISOU 141 CG1 VAL A 30 1679 1627 2037 -179 -114 -168 C ATOM 142 CG2 VAL A 30 25.607 13.880 27.810 1.00 12.39 C ANISOU 142 CG2 VAL A 30 1971 1413 1320 225 157 -226 C ATOM 143 N HIS A 31 24.569 18.368 26.735 1.00 9.94 N ANISOU 143 N HIS A 31 1337 1325 1113 108 -231 -265 N ATOM 144 CA HIS A 31 23.848 19.621 26.903 1.00 9.88 C ANISOU 144 CA HIS A 31 1258 1315 1181 94 -165 -371 C ATOM 145 C HIS A 31 22.378 19.434 26.580 1.00 9.37 C ANISOU 145 C HIS A 31 1115 1280 1162 82 -89 -545 C ATOM 146 O HIS A 31 22.078 18.911 25.510 1.00 12.95 O ANISOU 146 O HIS A 31 1394 2001 1523 55 -34 -636 O ATOM 147 CB HIS A 31 24.409 20.720 26.009 1.00 10.61 C ANISOU 147 CB HIS A 31 1358 1344 1328 71 -145 -322 C ATOM 148 CG HIS A 31 25.834 21.077 26.324 1.00 12.18 C ANISOU 148 CG HIS A 31 1493 1552 1582 -222 -35 -99 C ATOM 149 ND1 HIS A 31 26.200 22.279 26.875 1.00 13.47 N ANISOU 149 ND1 HIS A 31 1312 1796 2009 -255 -224 -322 N ATOM 150 CD2 HIS A 31 26.976 20.380 26.134 1.00 13.31 C ANISOU 150 CD2 HIS A 31 1485 1642 1929 -10 -163 -148 C ATOM 151 CE1 HIS A 31 27.514 22.290 27.064 1.00 15.18 C ANISOU 151 CE1 HIS A 31 1545 1857 2363 -384 -165 -313 C ATOM 152 NE2 HIS A 31 28.022 21.166 26.568 1.00 15.45 N ANISOU 152 NE2 HIS A 31 1725 1813 2330 -120 -15 19 N ATOM 153 N VAL A 32 21.518 19.857 27.508 1.00 10.14 N ANISOU 153 N VAL A 32 1345 1324 1184 75 -101 -357 N ATOM 154 CA VAL A 32 20.085 19.776 27.312 1.00 10.79 C ANISOU 154 CA VAL A 32 1359 1261 1480 -49 -80 -382 C ATOM 155 C VAL A 32 19.530 21.180 27.121 1.00 11.22 C ANISOU 155 C VAL A 32 1184 1500 1577 61 -148 -250 C ATOM 156 O VAL A 32 19.935 22.119 27.835 1.00 11.59 O ANISOU 156 O VAL A 32 1380 1317 1705 113 -136 -487 O ATOM 157 CB VAL A 32 19.389 19.086 28.502 1.00 11.05 C ANISOU 157 CB VAL A 32 1458 1388 1350 -149 -44 -315 C ATOM 158 CG1 VAL A 32 17.856 18.909 28.239 1.00 12.66 C ANISOU 158 CG1 VAL A 32 1316 1547 1944 -65 -212 -186 C ATOM 159 CG2 VAL A 32 20.067 17.782 28.868 1.00 12.97 C ANISOU 159 CG2 VAL A 32 1659 1402 1866 -48 -76 -71 C ATOM 160 N PHE A 33 18.666 21.320 26.128 1.00 10.21 N ANISOU 160 N PHE A 33 1020 1245 1615 -98 -331 -397 N ATOM 161 CA PHE A 33 17.990 22.553 25.804 1.00 11.21 C ANISOU 161 CA PHE A 33 1251 1242 1763 17 -270 -280 C ATOM 162 C PHE A 33 16.480 22.340 25.857 1.00 11.44 C ANISOU 162 C PHE A 33 1210 1286 1850 30 -110 -404 C ATOM 163 O PHE A 33 15.995 21.241 25.653 1.00 11.46 O ANISOU 163 O PHE A 33 1209 1200 1943 -39 -176 -498 O ATOM 164 CB PHE A 33 18.373 23.072 24.419 1.00 12.43 C ANISOU 164 CB PHE A 33 1401 1326 1993 70 -134 -207 C ATOM 165 CG PHE A 33 19.856 23.180 24.226 1.00 12.65 C ANISOU 165 CG PHE A 33 1562 1499 1744 16 -163 -67 C ATOM 166 CD1 PHE A 33 20.619 22.102 23.872 1.00 12.55 C ANISOU 166 CD1 PHE A 33 1414 1652 1700 9 -171 113 C ATOM 167 CD2 PHE A 33 20.482 24.368 24.438 1.00 14.12 C ANISOU 167 CD2 PHE A 33 1697 1471 2194 19 45 11 C ATOM 168 CE1 PHE A 33 22.036 22.211 23.721 1.00 13.26 C ANISOU 168 CE1 PHE A 33 1513 1597 1928 97 -178 -47 C ATOM 169 CE2 PHE A 33 21.850 24.494 24.280 1.00 14.78 C ANISOU 169 CE2 PHE A 33 1680 1514 2420 -286 -18 -93 C ATOM 170 CZ PHE A 33 22.620 23.423 23.942 1.00 14.80 C ANISOU 170 CZ PHE A 33 1327 1882 2414 -158 -6 -59 C ATOM 171 N ARG A 34 15.749 23.440 26.029 1.00 12.79 N ANISOU 171 N ARG A 34 1349 1338 2171 33 -246 -381 N ATOM 172 CA ARG A 34 14.283 23.407 25.986 1.00 13.01 C ANISOU 172 CA ARG A 34 1472 1400 2068 -43 -309 -232 C ATOM 173 C ARG A 34 13.828 24.495 25.072 1.00 14.25 C ANISOU 173 C ARG A 34 1678 1552 2183 1 -425 -198 C ATOM 174 O ARG A 34 14.295 25.613 25.178 1.00 14.69 O ANISOU 174 O ARG A 34 1626 1328 2625 -46 -585 -258 O ATOM 175 CB ARG A 34 13.709 23.591 27.379 1.00 13.73 C ANISOU 175 CB ARG A 34 1578 1586 2053 53 -252 -123 C ATOM 176 CG ARG A 34 12.202 23.550 27.455 1.00 13.74 C ANISOU 176 CG ARG A 34 1588 1579 2053 97 -167 -131 C ATOM 177 CD ARG A 34 11.691 23.796 28.897 1.00 15.52 C ANISOU 177 CD ARG A 34 2001 1751 2144 101 -77 -224 C ATOM 178 NE ARG A 34 10.213 23.800 28.921 1.00 16.45 N ANISOU 178 NE ARG A 34 2303 1839 2108 209 177 -315 N ATOM 179 CZ ARG A 34 9.441 24.819 28.588 1.00 17.02 C ANISOU 179 CZ ARG A 34 2172 2170 2122 176 0 -67 C ATOM 180 NH1 ARG A 34 9.976 25.975 28.281 1.00 16.80 N ANISOU 180 NH1 ARG A 34 1998 2137 2245 204 71 -411 N ATOM 181 NH2 ARG A 34 8.125 24.670 28.615 1.00 16.95 N ANISOU 181 NH2 ARG A 34 1916 1885 2639 219 151 -227 N ATOM 182 N LYS A 35 12.886 24.209 24.215 1.00 13.88 N ANISOU 182 N LYS A 35 1575 1401 2298 -140 -313 -178 N ATOM 183 CA ALYS A 35 12.395 25.207 23.302 0.50 15.78 C ANISOU 183 CA ALYS A 35 1855 1876 2263 -82 -201 -52 C ATOM 184 C LYS A 35 11.555 26.263 24.050 1.00 16.05 C ANISOU 184 C LYS A 35 1910 1810 2375 -25 -196 18 C ATOM 185 O LYS A 35 10.644 25.945 24.823 1.00 16.37 O ANISOU 185 O LYS A 35 1990 1604 2623 131 -143 183 O ATOM 186 CB ALYS A 35 11.615 24.462 22.218 0.50 15.84 C ANISOU 186 CB ALYS A 35 1919 1862 2234 -119 -259 -41 C ATOM 187 CG ALYS A 35 11.309 25.296 21.000 0.50 16.76 C ANISOU 187 CG ALYS A 35 2050 2183 2136 3 -167 203 C ATOM 188 CD ALYS A 35 10.670 24.348 19.973 0.50 18.46 C ANISOU 188 CD ALYS A 35 2205 2473 2333 -4 -260 -3 C ATOM 189 CE ALYS A 35 10.545 24.894 18.569 0.50 21.90 C ANISOU 189 CE ALYS A 35 2857 2847 2614 9 -62 79 C ATOM 190 NZ ALYS A 35 9.939 23.817 17.713 0.50 23.42 N ANISOU 190 NZ ALYS A 35 3044 3161 2691 -135 -287 -123 N ATOM 191 N ALA A 36 11.907 27.523 23.846 1.00 17.46 N ANISOU 191 N ALA A 36 2162 2053 2419 -27 -27 -49 N ATOM 192 CA ALA A 36 11.259 28.651 24.518 1.00 19.23 C ANISOU 192 CA ALA A 36 2476 2265 2564 73 -27 -25 C ATOM 193 C ALA A 36 10.074 29.107 23.734 1.00 21.00 C ANISOU 193 C ALA A 36 2780 2566 2633 150 20 65 C ATOM 194 O ALA A 36 9.836 28.657 22.605 1.00 21.61 O ANISOU 194 O ALA A 36 2741 2624 2846 385 45 108 O ATOM 195 CB ALA A 36 12.259 29.748 24.656 1.00 20.06 C ANISOU 195 CB ALA A 36 2507 2445 2670 31 -39 -151 C ATOM 196 N ALA A 37 9.348 30.053 24.349 1.00 23.13 N ANISOU 196 N ALA A 37 2987 2889 2912 390 101 190 N ATOM 197 CA ALA A 37 8.134 30.651 23.767 1.00 24.97 C ANISOU 197 CA ALA A 37 3209 3181 3094 248 76 207 C ATOM 198 C ALA A 37 8.418 31.270 22.410 1.00 26.43 C ANISOU 198 C ALA A 37 3458 3362 3221 218 33 246 C ATOM 199 O ALA A 37 7.531 31.298 21.559 1.00 28.93 O ANISOU 199 O ALA A 37 3734 3823 3434 362 6 318 O ATOM 200 CB ALA A 37 7.573 31.732 24.723 1.00 25.92 C ANISOU 200 CB ALA A 37 3260 3203 3384 341 135 164 C ATOM 201 N ASP A 38 9.639 31.767 22.244 1.00 27.55 N ANISOU 201 N ASP A 38 3656 3330 3483 311 61 298 N ATOM 202 CA ASP A 38 10.052 32.412 21.003 1.00 28.62 C ANISOU 202 CA ASP A 38 3769 3524 3579 159 90 208 C ATOM 203 C ASP A 38 10.695 31.466 20.001 1.00 28.89 C ANISOU 203 C ASP A 38 3899 3472 3606 127 82 199 C ATOM 204 O ASP A 38 11.333 31.910 19.043 1.00 29.71 O ANISOU 204 O ASP A 38 4160 3742 3386 113 79 416 O ATOM 205 CB ASP A 38 10.988 33.576 21.337 1.00 29.95 C ANISOU 205 CB ASP A 38 3977 3473 3928 115 108 167 C ATOM 206 CG ASP A 38 12.315 33.154 21.929 1.00 33.23 C ANISOU 206 CG ASP A 38 4417 3811 4397 129 31 145 C ATOM 207 OD1 ASP A 38 12.599 31.937 22.106 1.00 32.03 O ANISOU 207 OD1 ASP A 38 4780 2893 4495 -76 219 304 O ATOM 208 OD2 ASP A 38 13.106 34.080 22.236 1.00 40.03 O ANISOU 208 OD2 ASP A 38 5282 4469 5459 -142 -93 47 O ATOM 209 N ASP A 39 10.561 30.160 20.254 1.00 28.89 N ANISOU 209 N ASP A 39 3895 3516 3565 110 26 164 N ATOM 210 CA ASP A 39 11.056 29.104 19.367 1.00 29.15 C ANISOU 210 CA ASP A 39 3808 3577 3690 69 20 82 C ATOM 211 C ASP A 39 12.563 28.901 19.356 1.00 28.50 C ANISOU 211 C ASP A 39 3756 3451 3621 53 60 70 C ATOM 212 O ASP A 39 13.047 28.091 18.575 1.00 30.72 O ANISOU 212 O ASP A 39 4054 3746 3869 200 184 -94 O ATOM 213 CB ASP A 39 10.517 29.264 17.942 1.00 30.99 C ANISOU 213 CB ASP A 39 4041 3897 3834 82 41 136 C ATOM 214 CG ASP A 39 9.107 28.802 17.829 1.00 36.51 C ANISOU 214 CG ASP A 39 4646 4578 4645 -117 -89 -1 C ATOM 215 OD1 ASP A 39 8.875 27.620 18.181 1.00 41.60 O ANISOU 215 OD1 ASP A 39 5480 4914 5410 -33 -166 239 O ATOM 216 OD2 ASP A 39 8.229 29.614 17.418 1.00 44.58 O ANISOU 216 OD2 ASP A 39 5639 5479 5820 206 -41 144 O ATOM 217 N THR A 40 13.293 29.574 20.238 1.00 26.20 N ANISOU 217 N THR A 40 3487 3028 3440 9 110 176 N ATOM 218 CA THR A 40 14.741 29.384 20.381 1.00 24.88 C ANISOU 218 CA THR A 40 3300 2752 3398 28 53 194 C ATOM 219 C THR A 40 15.018 28.227 21.345 1.00 22.28 C ANISOU 219 C THR A 40 2794 2481 3189 -67 -7 249 C ATOM 220 O THR A 40 14.150 27.884 22.156 1.00 20.59 O ANISOU 220 O THR A 40 2375 2210 3238 105 96 139 O ATOM 221 CB THR A 40 15.444 30.680 20.910 1.00 24.94 C ANISOU 221 CB THR A 40 3442 2647 3388 -62 65 307 C ATOM 222 OG1 THR A 40 15.097 30.946 22.267 1.00 27.60 O ANISOU 222 OG1 THR A 40 3876 2455 4155 -160 86 72 O ATOM 223 CG2 THR A 40 15.086 31.919 20.065 1.00 25.77 C ANISOU 223 CG2 THR A 40 3683 2646 3462 128 -107 299 C ATOM 224 N TRP A 41 16.206 27.639 21.248 1.00 20.76 N ANISOU 224 N TRP A 41 2601 2154 3130 -175 -7 181 N ATOM 225 CA TRP A 41 16.668 26.596 22.182 1.00 19.40 C ANISOU 225 CA TRP A 41 2373 2220 2775 -263 -80 36 C ATOM 226 C TRP A 41 17.364 27.183 23.382 1.00 18.84 C ANISOU 226 C TRP A 41 2287 2068 2803 -338 -138 0 C ATOM 227 O TRP A 41 18.550 27.598 23.307 1.00 22.69 O ANISOU 227 O TRP A 41 2409 2912 3298 -391 -59 -224 O ATOM 228 CB TRP A 41 17.637 25.619 21.488 1.00 18.46 C ANISOU 228 CB TRP A 41 2164 2234 2613 -248 -15 101 C ATOM 229 CG TRP A 41 17.002 24.706 20.535 1.00 19.72 C ANISOU 229 CG TRP A 41 2358 2433 2699 -151 -12 102 C ATOM 230 CD1 TRP A 41 17.243 24.656 19.225 1.00 21.99 C ANISOU 230 CD1 TRP A 41 2658 2849 2847 -348 113 20 C ATOM 231 CD2 TRP A 41 16.054 23.669 20.820 1.00 18.78 C ANISOU 231 CD2 TRP A 41 2168 2390 2577 -59 83 -150 C ATOM 232 NE1 TRP A 41 16.503 23.661 18.637 1.00 23.82 N ANISOU 232 NE1 TRP A 41 2976 3110 2963 -321 274 -107 N ATOM 233 CE2 TRP A 41 15.769 23.034 19.604 1.00 21.91 C ANISOU 233 CE2 TRP A 41 2768 2850 2703 -410 102 16 C ATOM 234 CE3 TRP A 41 15.481 23.173 21.987 1.00 16.63 C ANISOU 234 CE3 TRP A 41 1917 2024 2378 -16 -130 11 C ATOM 235 CZ2 TRP A 41 14.903 21.961 19.520 1.00 21.20 C ANISOU 235 CZ2 TRP A 41 2732 2507 2816 -350 -11 -237 C ATOM 236 CZ3 TRP A 41 14.622 22.117 21.883 1.00 18.16 C ANISOU 236 CZ3 TRP A 41 2112 2029 2759 199 159 15 C ATOM 237 CH2 TRP A 41 14.319 21.559 20.665 1.00 20.24 C ANISOU 237 CH2 TRP A 41 2435 2360 2892 -261 26 -43 C ATOM 238 N GLU A 42 16.695 27.179 24.500 1.00 16.78 N ANISOU 238 N GLU A 42 1908 1847 2620 -105 -315 -88 N ATOM 239 CA AGLU A 42 17.241 27.741 25.728 0.50 17.72 C ANISOU 239 CA AGLU A 42 2158 1936 2636 -136 -252 -126 C ATOM 240 C GLU A 42 18.053 26.685 26.471 1.00 16.66 C ANISOU 240 C GLU A 42 2012 1778 2538 -113 -347 -173 C ATOM 241 O GLU A 42 17.570 25.582 26.644 1.00 15.64 O ANISOU 241 O GLU A 42 1745 1531 2666 -107 -336 -225 O ATOM 242 CB AGLU A 42 16.091 28.166 26.638 0.50 18.55 C ANISOU 242 CB AGLU A 42 2304 2132 2611 -114 -208 -142 C ATOM 243 CG AGLU A 42 16.513 28.933 27.874 0.50 18.94 C ANISOU 243 CG AGLU A 42 2387 2099 2711 -77 -250 -216 C ATOM 244 CD AGLU A 42 15.368 29.225 28.803 0.50 22.60 C ANISOU 244 CD AGLU A 42 2795 2780 3011 -138 -114 -175 C ATOM 245 OE1AGLU A 42 14.315 28.552 28.717 0.50 27.26 O ANISOU 245 OE1AGLU A 42 2961 3835 3560 -174 143 -52 O ATOM 246 OE2AGLU A 42 15.518 30.142 29.628 0.50 27.29 O ANISOU 246 OE2AGLU A 42 3570 3261 3536 -16 -51 -408 O ATOM 247 N PRO A 43 19.262 27.026 26.961 1.00 15.62 N ANISOU 247 N PRO A 43 1902 1508 2522 -152 -349 -186 N ATOM 248 CA PRO A 43 19.985 26.066 27.764 1.00 15.54 C ANISOU 248 CA PRO A 43 1960 1663 2279 -207 -306 -206 C ATOM 249 C PRO A 43 19.194 25.685 28.990 1.00 16.33 C ANISOU 249 C PRO A 43 1953 1852 2397 28 -122 -274 C ATOM 250 O PRO A 43 18.629 26.541 29.685 1.00 18.89 O ANISOU 250 O PRO A 43 2652 2013 2512 211 233 -313 O ATOM 251 CB PRO A 43 21.321 26.798 28.096 1.00 16.20 C ANISOU 251 CB PRO A 43 1923 1856 2374 -224 -390 -229 C ATOM 252 CG PRO A 43 21.449 27.823 27.033 1.00 19.42 C ANISOU 252 CG PRO A 43 2262 2191 2923 -261 -402 -83 C ATOM 253 CD PRO A 43 20.029 28.275 26.799 1.00 18.30 C ANISOU 253 CD PRO A 43 2215 1798 2940 -200 -390 25 C ATOM 254 N PHE A 44 19.113 24.376 29.237 1.00 13.72 N ANISOU 254 N PHE A 44 1626 1568 2015 35 -142 -331 N ATOM 255 CA PHE A 44 18.305 23.836 30.324 1.00 13.24 C ANISOU 255 CA PHE A 44 1531 1698 1801 43 -99 -470 C ATOM 256 C PHE A 44 19.119 23.152 31.420 1.00 13.58 C ANISOU 256 C PHE A 44 1553 1719 1887 52 -10 -448 C ATOM 257 O PHE A 44 18.913 23.339 32.613 1.00 14.73 O ANISOU 257 O PHE A 44 1615 2048 1932 201 40 -799 O ATOM 258 CB PHE A 44 17.250 22.876 29.731 1.00 13.33 C ANISOU 258 CB PHE A 44 1567 1837 1660 12 -33 -457 C ATOM 259 CG PHE A 44 16.344 22.275 30.759 1.00 13.16 C ANISOU 259 CG PHE A 44 1360 1945 1693 -9 -86 -514 C ATOM 260 CD1 PHE A 44 15.263 22.997 31.267 1.00 15.85 C ANISOU 260 CD1 PHE A 44 1581 2325 2115 -247 143 -643 C ATOM 261 CD2 PHE A 44 16.530 21.012 31.225 1.00 13.39 C ANISOU 261 CD2 PHE A 44 1085 2094 1906 -65 -36 -300 C ATOM 262 CE1 PHE A 44 14.443 22.450 32.257 1.00 14.82 C ANISOU 262 CE1 PHE A 44 1617 2554 1459 -92 131 -636 C ATOM 263 CE2 PHE A 44 15.749 20.476 32.187 1.00 15.47 C ANISOU 263 CE2 PHE A 44 1466 2519 1893 5 35 -329 C ATOM 264 CZ PHE A 44 14.676 21.227 32.719 1.00 14.51 C ANISOU 264 CZ PHE A 44 1448 2588 1473 -267 -18 -515 C ATOM 265 N ALA A 45 20.062 22.313 31.031 1.00 12.31 N ANISOU 265 N ALA A 45 1466 1547 1661 113 -40 -546 N ATOM 266 CA ALA A 45 20.960 21.636 31.957 1.00 11.78 C ANISOU 266 CA ALA A 45 1221 1633 1619 167 51 -373 C ATOM 267 C ALA A 45 22.113 21.044 31.166 1.00 10.93 C ANISOU 267 C ALA A 45 1202 1510 1438 103 12 -389 C ATOM 268 O ALA A 45 21.993 20.846 29.966 1.00 12.43 O ANISOU 268 O ALA A 45 1322 1857 1543 120 -230 -503 O ATOM 269 CB ALA A 45 20.258 20.542 32.654 1.00 14.24 C ANISOU 269 CB ALA A 45 1644 1840 1925 98 129 -204 C ATOM 270 N SER A 46 23.213 20.746 31.871 1.00 11.00 N ANISOU 270 N SER A 46 1247 1546 1383 180 -58 -320 N ATOM 271 CA SER A 46 24.312 20.061 31.232 1.00 9.57 C ANISOU 271 CA SER A 46 1058 1272 1304 25 -132 -370 C ATOM 272 C SER A 46 25.079 19.234 32.238 1.00 10.05 C ANISOU 272 C SER A 46 1153 1310 1355 103 -102 -363 C ATOM 273 O SER A 46 24.949 19.452 33.417 1.00 11.59 O ANISOU 273 O SER A 46 1557 1615 1229 51 -203 -437 O ATOM 274 CB SER A 46 25.237 21.019 30.457 1.00 10.82 C ANISOU 274 CB SER A 46 1275 1396 1440 167 -53 -141 C ATOM 275 OG SER A 46 25.913 21.919 31.322 1.00 12.06 O ANISOU 275 OG SER A 46 1379 1541 1659 -121 -358 -623 O ATOM 276 N GLY A 47 25.909 18.323 31.750 1.00 10.03 N ANISOU 276 N GLY A 47 1212 1395 1202 110 -55 -332 N ATOM 277 CA GLY A 47 26.724 17.533 32.624 1.00 10.70 C ANISOU 277 CA GLY A 47 1478 1389 1197 77 58 -208 C ATOM 278 C GLY A 47 27.609 16.606 31.796 1.00 10.47 C ANISOU 278 C GLY A 47 1530 1258 1188 157 7 -227 C ATOM 279 O GLY A 47 27.711 16.745 30.559 1.00 11.01 O ANISOU 279 O GLY A 47 1558 1405 1220 28 -26 -197 O ATOM 280 N LYS A 48 28.258 15.667 32.474 1.00 11.14 N ANISOU 280 N LYS A 48 1749 1275 1208 147 78 -216 N ATOM 281 CA ALYS A 48 29.182 14.685 31.845 0.50 12.15 C ANISOU 281 CA ALYS A 48 1720 1431 1465 152 4 -141 C ATOM 282 C LYS A 48 28.836 13.295 32.316 1.00 11.29 C ANISOU 282 C LYS A 48 1517 1414 1358 188 -93 -27 C ATOM 283 O LYS A 48 28.531 13.120 33.472 1.00 13.26 O ANISOU 283 O LYS A 48 2191 1401 1445 90 -16 -236 O ATOM 284 CB ALYS A 48 30.634 14.845 32.321 0.50 14.61 C ANISOU 284 CB ALYS A 48 1959 1798 1794 112 -7 -36 C ATOM 285 CG ALYS A 48 31.267 16.147 32.166 0.50 17.60 C ANISOU 285 CG ALYS A 48 2408 2072 2204 41 -30 59 C ATOM 286 CD ALYS A 48 32.127 16.236 30.939 0.50 18.46 C ANISOU 286 CD ALYS A 48 2587 2149 2275 -6 92 242 C ATOM 287 CE ALYS A 48 33.156 17.350 31.143 0.50 18.07 C ANISOU 287 CE ALYS A 48 2659 1929 2277 96 -92 -66 C ATOM 288 NZ ALYS A 48 33.915 17.821 30.037 0.50 10.70 N ANISOU 288 NZ ALYS A 48 2019 836 1209 68 -420 -446 N ATOM 289 N THR A 49 28.997 12.292 31.468 1.00 10.91 N ANISOU 289 N THR A 49 1443 1371 1331 224 47 -96 N ATOM 290 CA THR A 49 28.784 10.935 31.945 1.00 10.84 C ANISOU 290 CA THR A 49 1558 1416 1143 201 -40 -59 C ATOM 291 C THR A 49 29.925 10.531 32.889 1.00 11.36 C ANISOU 291 C THR A 49 1704 1489 1124 188 54 -154 C ATOM 292 O THR A 49 31.076 10.928 32.718 1.00 12.36 O ANISOU 292 O THR A 49 1754 1660 1280 135 -75 -194 O ATOM 293 CB THR A 49 28.675 9.947 30.781 1.00 10.32 C ANISOU 293 CB THR A 49 1511 1290 1119 271 -71 -141 C ATOM 294 OG1 THR A 49 29.901 9.958 30.037 1.00 10.78 O ANISOU 294 OG1 THR A 49 1462 1264 1367 288 158 -97 O ATOM 295 CG2 THR A 49 27.468 10.219 29.852 1.00 11.79 C ANISOU 295 CG2 THR A 49 1653 1702 1125 352 -126 -167 C ATOM 296 N SER A 50 29.561 9.710 33.851 1.00 12.41 N ANISOU 296 N SER A 50 1703 1613 1398 126 -222 0 N ATOM 297 CA SER A 50 30.468 9.207 34.826 1.00 13.75 C ANISOU 297 CA SER A 50 1946 1845 1433 241 -251 113 C ATOM 298 C SER A 50 31.221 7.999 34.326 1.00 14.91 C ANISOU 298 C SER A 50 2064 2004 1595 246 -308 72 C ATOM 299 O SER A 50 31.077 7.587 33.189 1.00 13.20 O ANISOU 299 O SER A 50 1968 1661 1385 351 -177 -9 O ATOM 300 CB SER A 50 29.599 8.820 36.044 1.00 15.16 C ANISOU 300 CB SER A 50 2131 2132 1496 354 -198 166 C ATOM 301 OG SER A 50 28.873 7.628 35.732 1.00 17.29 O ANISOU 301 OG SER A 50 2175 2231 2162 358 -41 518 O ATOM 302 N GLU A 51 31.941 7.359 35.247 1.00 14.94 N ANISOU 302 N GLU A 51 2110 2036 1529 345 -363 37 N ATOM 303 CA CGLU A 51 32.669 6.129 34.872 0.62 16.06 C ANISOU 303 CA CGLU A 51 2196 2140 1763 319 -241 112 C ATOM 304 C GLU A 51 31.731 4.969 34.503 1.00 16.23 C ANISOU 304 C GLU A 51 2314 2128 1722 339 -216 235 C ATOM 305 O GLU A 51 32.163 4.040 33.841 1.00 17.82 O ANISOU 305 O GLU A 51 2730 2018 2022 391 -132 48 O ATOM 306 CB CGLU A 51 33.727 5.737 35.929 0.62 17.93 C ANISOU 306 CB CGLU A 51 2284 2486 2043 303 -295 155 C ATOM 307 CG CGLU A 51 34.765 6.856 36.153 0.62 22.53 C ANISOU 307 CG CGLU A 51 2945 2865 2749 165 -235 39 C ATOM 308 CD CGLU A 51 36.037 6.762 35.336 0.62 28.06 C ANISOU 308 CD CGLU A 51 3678 3646 3334 78 -46 72 C ATOM 309 OE1CGLU A 51 36.588 7.843 35.017 0.62 31.03 O ANISOU 309 OE1CGLU A 51 4130 3771 3888 -16 -190 -1 O ATOM 310 OE2CGLU A 51 36.528 5.642 35.048 0.62 32.26 O ANISOU 310 OE2CGLU A 51 4648 3751 3858 139 -12 116 O ATOM 311 N SER A 52 30.470 5.025 34.864 1.00 14.99 N ANISOU 311 N SER A 52 2227 2043 1423 364 -211 269 N ATOM 312 CA SER A 52 29.502 4.053 34.459 1.00 14.88 C ANISOU 312 CA SER A 52 2065 2001 1587 242 -97 119 C ATOM 313 C SER A 52 28.796 4.396 33.135 1.00 12.90 C ANISOU 313 C SER A 52 1876 1670 1352 243 6 -80 C ATOM 314 O SER A 52 27.902 3.673 32.675 1.00 14.54 O ANISOU 314 O SER A 52 1992 1709 1822 111 176 -11 O ATOM 315 CB SER A 52 28.445 3.875 35.545 1.00 17.45 C ANISOU 315 CB SER A 52 2433 2371 1825 27 -202 303 C ATOM 316 OG SER A 52 27.672 5.035 35.604 1.00 21.39 O ANISOU 316 OG SER A 52 3000 3005 2121 40 211 -463 O ATOM 317 N GLY A 53 29.180 5.524 32.539 1.00 11.66 N ANISOU 317 N GLY A 53 1717 1589 1124 152 -23 -75 N ATOM 318 CA GLY A 53 28.521 6.014 31.314 1.00 11.95 C ANISOU 318 CA GLY A 53 1761 1649 1128 218 -23 -90 C ATOM 319 C GLY A 53 27.189 6.673 31.535 1.00 11.19 C ANISOU 319 C GLY A 53 1586 1577 1088 109 -67 -63 C ATOM 320 O GLY A 53 26.498 6.981 30.599 1.00 11.15 O ANISOU 320 O GLY A 53 1550 1563 1123 70 -19 44 O ATOM 321 N GLU A 54 26.850 6.965 32.786 1.00 11.55 N ANISOU 321 N GLU A 54 1632 1640 1116 130 -100 -69 N ATOM 322 CA GLU A 54 25.562 7.555 33.137 1.00 12.33 C ANISOU 322 CA GLU A 54 1723 1724 1235 134 -37 -107 C ATOM 323 C GLU A 54 25.721 8.988 33.602 1.00 10.15 C ANISOU 323 C GLU A 54 1261 1587 1005 119 -54 -197 C ATOM 324 O GLU A 54 26.735 9.384 34.200 1.00 11.96 O ANISOU 324 O GLU A 54 1343 1840 1360 227 -213 -218 O ATOM 325 CB GLU A 54 24.864 6.751 34.269 1.00 14.23 C ANISOU 325 CB GLU A 54 1866 1916 1622 113 82 -21 C ATOM 326 CG GLU A 54 24.594 5.292 33.847 1.00 16.82 C ANISOU 326 CG GLU A 54 2296 2185 1906 13 186 97 C ATOM 327 CD GLU A 54 23.846 4.431 34.835 1.00 21.17 C ANISOU 327 CD GLU A 54 3050 2327 2667 -187 34 85 C ATOM 328 OE1 GLU A 54 23.507 4.923 35.910 1.00 25.49 O ANISOU 328 OE1 GLU A 54 3788 2718 3176 -49 612 385 O ATOM 329 OE2 GLU A 54 23.615 3.257 34.472 1.00 28.65 O ANISOU 329 OE2 GLU A 54 4366 2489 4030 -273 276 -112 O ATOM 330 N LEU A 55 24.674 9.735 33.357 1.00 11.40 N ANISOU 330 N LEU A 55 1390 1576 1364 123 -210 -167 N ATOM 331 CA LEU A 55 24.563 11.105 33.778 1.00 11.14 C ANISOU 331 CA LEU A 55 1329 1616 1288 189 -202 -231 C ATOM 332 C LEU A 55 23.227 11.253 34.443 1.00 11.73 C ANISOU 332 C LEU A 55 1622 1657 1177 174 -106 -125 C ATOM 333 O LEU A 55 22.168 11.151 33.826 1.00 12.76 O ANISOU 333 O LEU A 55 1637 1757 1455 284 -31 -188 O ATOM 334 CB LEU A 55 24.660 12.055 32.590 1.00 11.94 C ANISOU 334 CB LEU A 55 1426 1722 1388 169 -48 -173 C ATOM 335 CG LEU A 55 24.362 13.511 32.819 1.00 11.42 C ANISOU 335 CG LEU A 55 1320 1777 1240 221 -68 -32 C ATOM 336 CD1 LEU A 55 25.157 14.118 33.952 1.00 13.72 C ANISOU 336 CD1 LEU A 55 1789 2041 1382 215 22 -277 C ATOM 337 CD2 LEU A 55 24.685 14.284 31.536 1.00 12.77 C ANISOU 337 CD2 LEU A 55 1758 1894 1197 136 -78 -101 C ATOM 338 N HIS A 56 23.355 11.507 35.742 1.00 14.49 N ANISOU 338 N HIS A 56 2152 1886 1467 153 48 -221 N ATOM 339 CA HIS A 56 22.271 11.703 36.662 1.00 16.87 C ANISOU 339 CA HIS A 56 2424 2119 1864 72 85 -115 C ATOM 340 C HIS A 56 22.283 13.153 37.142 1.00 17.32 C ANISOU 340 C HIS A 56 2433 2269 1878 86 118 -265 C ATOM 341 O HIS A 56 23.247 13.892 37.011 1.00 18.15 O ANISOU 341 O HIS A 56 2519 2338 2037 106 232 -554 O ATOM 342 CB HIS A 56 22.422 10.774 37.916 1.00 18.20 C ANISOU 342 CB HIS A 56 2636 2443 1836 66 205 -18 C ATOM 343 CG HIS A 56 22.383 9.317 37.609 1.00 21.22 C ANISOU 343 CG HIS A 56 2929 2661 2471 8 105 235 C ATOM 344 ND1 HIS A 56 21.196 8.623 37.544 1.00 26.74 N ANISOU 344 ND1 HIS A 56 3264 3279 3615 -231 440 17 N ATOM 345 CD2 HIS A 56 23.338 8.453 37.219 1.00 25.18 C ANISOU 345 CD2 HIS A 56 3157 3371 3036 143 294 135 C ATOM 346 CE1 HIS A 56 21.438 7.363 37.219 1.00 27.66 C ANISOU 346 CE1 HIS A 56 3485 3355 3666 -89 171 -138 C ATOM 347 NE2 HIS A 56 22.736 7.233 37.020 1.00 24.53 N ANISOU 347 NE2 HIS A 56 3166 3326 2825 98 204 101 N ATOM 348 N GLY A 57 21.178 13.536 37.705 1.00 17.32 N ANISOU 348 N GLY A 57 2319 2287 1974 136 -41 -190 N ATOM 349 CA GLY A 57 21.111 14.846 38.345 1.00 16.74 C ANISOU 349 CA GLY A 57 2220 2213 1924 256 -39 -255 C ATOM 350 C GLY A 57 20.944 16.052 37.439 1.00 15.97 C ANISOU 350 C GLY A 57 2000 2025 2040 216 -165 -217 C ATOM 351 O GLY A 57 21.155 17.159 37.881 1.00 18.60 O ANISOU 351 O GLY A 57 2623 2092 2349 364 -167 -329 O ATOM 352 N LEU A 58 20.532 15.858 36.191 1.00 14.36 N ANISOU 352 N LEU A 58 1629 1912 1915 58 -116 -304 N ATOM 353 CA LEU A 58 20.386 16.989 35.296 1.00 14.11 C ANISOU 353 CA LEU A 58 1516 1859 1985 84 -12 -287 C ATOM 354 C LEU A 58 19.280 17.945 35.747 1.00 13.65 C ANISOU 354 C LEU A 58 1530 1844 1809 72 17 -226 C ATOM 355 O LEU A 58 19.435 19.157 35.579 1.00 15.47 O ANISOU 355 O LEU A 58 1912 2002 1960 164 234 -208 O ATOM 356 CB LEU A 58 20.077 16.466 33.899 1.00 13.96 C ANISOU 356 CB LEU A 58 1575 1750 1979 125 -3 -254 C ATOM 357 CG LEU A 58 21.292 15.957 33.125 1.00 13.28 C ANISOU 357 CG LEU A 58 1239 1804 2003 175 195 -427 C ATOM 358 CD1 LEU A 58 20.820 15.176 31.913 1.00 13.71 C ANISOU 358 CD1 LEU A 58 1649 1790 1767 109 69 -420 C ATOM 359 CD2 LEU A 58 22.110 17.167 32.679 1.00 16.19 C ANISOU 359 CD2 LEU A 58 1645 2087 2417 -71 464 -579 C ATOM 360 N THR A 59 18.177 17.404 36.280 1.00 13.39 N ANISOU 360 N THR A 59 1433 1734 1919 151 17 -159 N ATOM 361 CA THR A 59 17.025 18.240 36.586 1.00 14.10 C ANISOU 361 CA THR A 59 1582 1857 1918 192 30 -306 C ATOM 362 C THR A 59 16.215 17.670 37.699 1.00 14.57 C ANISOU 362 C THR A 59 1711 1954 1868 263 5 -205 C ATOM 363 O THR A 59 16.537 16.647 38.243 1.00 18.06 O ANISOU 363 O THR A 59 2143 2465 2251 568 315 -7 O ATOM 364 CB THR A 59 16.171 18.461 35.322 1.00 13.94 C ANISOU 364 CB THR A 59 1393 2006 1895 187 9 -230 C ATOM 365 OG1 THR A 59 15.221 19.507 35.549 1.00 14.44 O ANISOU 365 OG1 THR A 59 1448 2052 1987 349 -48 -635 O ATOM 366 CG2 THR A 59 15.490 17.172 34.805 1.00 15.14 C ANISOU 366 CG2 THR A 59 1835 2066 1850 269 4 -478 C ATOM 367 N THR A 60 15.115 18.338 38.018 1.00 16.45 N ANISOU 367 N THR A 60 2008 2131 2111 250 301 -278 N ATOM 368 CA THR A 60 14.241 17.964 39.130 1.00 16.95 C ANISOU 368 CA THR A 60 2199 2176 2066 185 252 -258 C ATOM 369 C THR A 60 12.863 17.777 38.544 1.00 17.00 C ANISOU 369 C THR A 60 2254 2223 1981 92 262 -232 C ATOM 370 O THR A 60 12.528 18.327 37.483 1.00 16.15 O ANISOU 370 O THR A 60 2095 2199 1841 111 350 -243 O ATOM 371 CB THR A 60 14.180 19.042 40.247 1.00 16.58 C ANISOU 371 CB THR A 60 2205 2330 1764 113 177 -213 C ATOM 372 OG1 THR A 60 13.625 20.259 39.725 1.00 17.00 O ANISOU 372 OG1 THR A 60 2081 2408 1968 172 9 -552 O ATOM 373 CG2 THR A 60 15.605 19.303 40.774 1.00 20.36 C ANISOU 373 CG2 THR A 60 2541 2739 2456 333 -193 -355 C ATOM 374 N GLU A 61 12.002 17.037 39.243 1.00 18.75 N ANISOU 374 N GLU A 61 2431 2480 2213 54 301 -53 N ATOM 375 CA AGLU A 61 10.598 16.927 38.866 0.50 19.09 C ANISOU 375 CA AGLU A 61 2464 2528 2259 -53 193 -82 C ATOM 376 C GLU A 61 9.954 18.318 38.688 1.00 19.39 C ANISOU 376 C GLU A 61 2418 2579 2369 -65 172 -36 C ATOM 377 O GLU A 61 9.180 18.572 37.779 1.00 19.34 O ANISOU 377 O GLU A 61 2423 2554 2371 -101 92 -76 O ATOM 378 CB AGLU A 61 9.842 16.101 39.931 0.50 20.55 C ANISOU 378 CB AGLU A 61 2578 2697 2530 -35 246 12 C ATOM 379 CG AGLU A 61 10.336 14.666 40.005 0.50 20.71 C ANISOU 379 CG AGLU A 61 2733 2518 2615 -70 146 -51 C ATOM 380 CD AGLU A 61 9.671 13.835 41.109 0.50 23.18 C ANISOU 380 CD AGLU A 61 3106 2904 2795 -94 134 46 C ATOM 381 OE1AGLU A 61 9.477 14.340 42.239 0.50 27.78 O ANISOU 381 OE1AGLU A 61 3870 3481 3201 -234 104 -165 O ATOM 382 OE2AGLU A 61 9.341 12.666 40.849 0.50 28.73 O ANISOU 382 OE2AGLU A 61 4065 3389 3462 -301 29 11 O ATOM 383 N GLU A 62 10.239 19.258 39.588 1.00 16.63 N ANISOU 383 N GLU A 62 2038 2448 1831 -18 193 -143 N ATOM 384 CA GLU A 62 9.618 20.594 39.527 1.00 17.53 C ANISOU 384 CA GLU A 62 2036 2451 2170 -39 90 -140 C ATOM 385 C GLU A 62 10.054 21.343 38.286 1.00 13.79 C ANISOU 385 C GLU A 62 1595 2032 1610 -26 -30 -451 C ATOM 386 O GLU A 62 9.261 21.988 37.626 1.00 14.62 O ANISOU 386 O GLU A 62 1557 2308 1687 37 9 -507 O ATOM 387 CB GLU A 62 9.940 21.501 40.748 1.00 19.98 C ANISOU 387 CB GLU A 62 2300 2907 2383 42 -13 -105 C ATOM 388 CG GLU A 62 8.948 21.415 41.859 1.00 24.20 C ANISOU 388 CG GLU A 62 3006 3155 3033 -110 141 -119 C ATOM 389 CD GLU A 62 9.163 22.380 42.999 1.00 20.33 C ANISOU 389 CD GLU A 62 2759 2597 2368 213 321 4 C ATOM 390 OE1 GLU A 62 9.815 23.469 42.856 1.00 20.22 O ANISOU 390 OE1 GLU A 62 2838 2575 2268 106 304 -89 O ATOM 391 OE2 GLU A 62 8.701 22.011 44.096 1.00 26.38 O ANISOU 391 OE2 GLU A 62 3877 3194 2952 137 554 44 O ATOM 392 N GLU A 63 11.354 21.292 37.989 1.00 13.27 N ANISOU 392 N GLU A 63 1479 1941 1619 46 -68 -433 N ATOM 393 CA AGLU A 63 11.937 22.069 36.934 0.50 13.32 C ANISOU 393 CA AGLU A 63 1523 1848 1689 51 -19 -425 C ATOM 394 C GLU A 63 11.622 21.503 35.544 1.00 11.31 C ANISOU 394 C GLU A 63 1250 1577 1469 -10 -35 -424 C ATOM 395 O GLU A 63 11.598 22.239 34.580 1.00 12.42 O ANISOU 395 O GLU A 63 1458 1642 1618 36 -112 -489 O ATOM 396 CB AGLU A 63 13.454 22.058 37.153 0.50 13.31 C ANISOU 396 CB AGLU A 63 1570 1787 1698 -85 -214 -394 C ATOM 397 CG AGLU A 63 14.243 22.923 36.207 0.50 14.93 C ANISOU 397 CG AGLU A 63 1612 2149 1910 -1 -33 -372 C ATOM 398 CD AGLU A 63 15.756 22.877 36.448 0.50 14.78 C ANISOU 398 CD AGLU A 63 1646 2092 1878 2 -119 -268 C ATOM 399 OE1AGLU A 63 16.428 21.908 36.076 0.50 13.24 O ANISOU 399 OE1AGLU A 63 1461 1657 1913 149 -93 -394 O ATOM 400 OE2AGLU A 63 16.247 23.870 37.003 0.50 22.58 O ANISOU 400 OE2AGLU A 63 3145 2367 3065 -186 -121 -376 O ATOM 401 N PHE A 64 11.457 20.178 35.487 1.00 11.86 N ANISOU 401 N PHE A 64 1353 1642 1511 132 15 -395 N ATOM 402 CA PHE A 64 11.292 19.442 34.214 1.00 11.61 C ANISOU 402 CA PHE A 64 1317 1617 1475 187 -35 -467 C ATOM 403 C PHE A 64 9.837 19.460 33.809 1.00 12.38 C ANISOU 403 C PHE A 64 1410 1639 1654 88 -127 -488 C ATOM 404 O PHE A 64 9.125 18.458 33.878 1.00 13.91 O ANISOU 404 O PHE A 64 1401 1799 2085 157 0 -679 O ATOM 405 CB PHE A 64 11.844 18.022 34.368 1.00 12.66 C ANISOU 405 CB PHE A 64 1464 1708 1635 59 -52 -296 C ATOM 406 CG PHE A 64 12.001 17.255 33.085 1.00 13.47 C ANISOU 406 CG PHE A 64 1527 1839 1750 260 -207 -249 C ATOM 407 CD1 PHE A 64 12.492 17.806 31.936 1.00 14.10 C ANISOU 407 CD1 PHE A 64 1766 1751 1837 232 39 -603 C ATOM 408 CD2 PHE A 64 11.793 15.912 33.119 1.00 15.86 C ANISOU 408 CD2 PHE A 64 2336 2089 1601 -306 -145 -454 C ATOM 409 CE1 PHE A 64 12.663 17.019 30.805 1.00 13.62 C ANISOU 409 CE1 PHE A 64 1828 1874 1473 209 13 -299 C ATOM 410 CE2 PHE A 64 11.991 15.139 32.000 1.00 18.97 C ANISOU 410 CE2 PHE A 64 3016 1893 2296 -14 139 -636 C ATOM 411 CZ PHE A 64 12.413 15.701 30.876 1.00 15.16 C ANISOU 411 CZ PHE A 64 1967 1861 1930 329 -9 -543 C ATOM 412 N VAL A 65 9.421 20.653 33.413 1.00 11.78 N ANISOU 412 N VAL A 65 1230 1713 1533 111 -135 -525 N ATOM 413 CA VAL A 65 8.027 20.892 33.003 1.00 12.44 C ANISOU 413 CA VAL A 65 1384 1618 1722 151 -120 -331 C ATOM 414 C VAL A 65 7.768 20.363 31.597 1.00 12.59 C ANISOU 414 C VAL A 65 1345 1740 1697 113 -93 -441 C ATOM 415 O VAL A 65 8.673 19.905 30.877 1.00 11.80 O ANISOU 415 O VAL A 65 1194 1754 1535 178 -81 -856 O ATOM 416 CB VAL A 65 7.711 22.385 33.092 1.00 11.01 C ANISOU 416 CB VAL A 65 1190 1375 1616 210 -179 -486 C ATOM 417 CG1 VAL A 65 7.733 22.855 34.573 1.00 13.44 C ANISOU 417 CG1 VAL A 65 1780 1885 1438 205 -146 -741 C ATOM 418 CG2 VAL A 65 8.606 23.218 32.233 1.00 14.07 C ANISOU 418 CG2 VAL A 65 1482 1639 2224 30 85 -453 C ATOM 419 N GLU A 66 6.527 20.378 31.144 1.00 11.43 N ANISOU 419 N GLU A 66 1198 1799 1346 136 29 -555 N ATOM 420 CA AGLU A 66 6.256 20.012 29.788 0.50 12.67 C ANISOU 420 CA AGLU A 66 1461 1743 1611 43 -90 -399 C ATOM 421 C GLU A 66 7.053 20.936 28.830 1.00 12.24 C ANISOU 421 C GLU A 66 1464 1703 1483 28 -133 -497 C ATOM 422 O GLU A 66 7.299 22.086 29.095 1.00 14.50 O ANISOU 422 O GLU A 66 2180 1570 1756 -21 103 -623 O ATOM 423 CB AGLU A 66 4.732 20.042 29.665 0.50 13.57 C ANISOU 423 CB AGLU A 66 1552 1860 1741 -72 -22 -386 C ATOM 424 CG AGLU A 66 4.115 19.773 28.342 0.50 14.33 C ANISOU 424 CG AGLU A 66 1682 1712 2049 -183 -277 -233 C ATOM 425 CD AGLU A 66 2.612 20.218 28.353 0.50 17.26 C ANISOU 425 CD AGLU A 66 1768 2336 2452 -200 -149 -172 C ATOM 426 OE1AGLU A 66 2.086 20.689 29.387 0.50 20.41 O ANISOU 426 OE1AGLU A 66 2158 3127 2469 7 127 -62 O ATOM 427 OE2AGLU A 66 1.995 20.172 27.304 0.50 22.05 O ANISOU 427 OE2AGLU A 66 2888 3227 2260 93 -295 -30 O ATOM 428 N GLY A 67 7.417 20.398 27.677 1.00 12.01 N ANISOU 428 N GLY A 67 1515 1615 1432 99 -117 -522 N ATOM 429 CA GLY A 67 8.104 21.157 26.681 1.00 13.38 C ANISOU 429 CA GLY A 67 1658 1693 1730 108 -31 -362 C ATOM 430 C GLY A 67 8.731 20.244 25.651 1.00 11.12 C ANISOU 430 C GLY A 67 1368 1448 1406 121 -44 -317 C ATOM 431 O GLY A 67 8.615 19.029 25.753 1.00 11.63 O ANISOU 431 O GLY A 67 1465 1371 1581 1 6 -354 O ATOM 432 N ILE A 68 9.380 20.860 24.699 1.00 11.71 N ANISOU 432 N ILE A 68 1393 1435 1618 42 27 -351 N ATOM 433 CA ILE A 68 10.196 20.156 23.711 1.00 11.90 C ANISOU 433 CA ILE A 68 1474 1493 1551 75 -64 -322 C ATOM 434 C ILE A 68 11.642 20.346 24.105 1.00 11.24 C ANISOU 434 C ILE A 68 1411 1336 1524 57 -53 -434 C ATOM 435 O ILE A 68 12.131 21.457 24.288 1.00 12.61 O ANISOU 435 O ILE A 68 1461 1248 2083 77 -174 -367 O ATOM 436 CB ILE A 68 9.967 20.689 22.303 1.00 13.19 C ANISOU 436 CB ILE A 68 1530 1720 1760 82 -116 -191 C ATOM 437 CG1 ILE A 68 8.475 20.548 21.896 1.00 15.15 C ANISOU 437 CG1 ILE A 68 1756 2099 1901 -22 -345 -113 C ATOM 438 CG2 ILE A 68 10.855 19.963 21.317 1.00 14.51 C ANISOU 438 CG2 ILE A 68 1871 2040 1600 157 11 -283 C ATOM 439 CD1 ILE A 68 8.162 21.145 20.516 1.00 17.11 C ANISOU 439 CD1 ILE A 68 1966 2437 2095 148 -375 154 C ATOM 440 N TYR A 69 12.283 19.223 24.335 1.00 10.46 N ANISOU 440 N TYR A 69 1154 1324 1495 54 -201 -374 N ATOM 441 CA TYR A 69 13.656 19.144 24.820 1.00 10.22 C ANISOU 441 CA TYR A 69 1211 1276 1395 38 -107 -320 C ATOM 442 C TYR A 69 14.576 18.563 23.757 1.00 9.87 C ANISOU 442 C TYR A 69 1184 1265 1298 86 -23 -301 C ATOM 443 O TYR A 69 14.182 17.726 22.955 1.00 11.08 O ANISOU 443 O TYR A 69 1256 1495 1459 -41 57 -457 O ATOM 444 CB TYR A 69 13.713 18.291 26.088 1.00 11.08 C ANISOU 444 CB TYR A 69 1367 1400 1442 127 -77 -305 C ATOM 445 CG TYR A 69 13.028 18.956 27.260 1.00 11.01 C ANISOU 445 CG TYR A 69 1256 1427 1498 3 -138 -500 C ATOM 446 CD1 TYR A 69 11.675 18.832 27.459 1.00 10.74 C ANISOU 446 CD1 TYR A 69 1206 1484 1390 1 -130 -540 C ATOM 447 CD2 TYR A 69 13.753 19.726 28.185 1.00 10.76 C ANISOU 447 CD2 TYR A 69 1021 1476 1591 -91 -18 -540 C ATOM 448 CE1 TYR A 69 11.007 19.433 28.534 1.00 10.72 C ANISOU 448 CE1 TYR A 69 895 1652 1523 11 103 -416 C ATOM 449 CE2 TYR A 69 13.115 20.324 29.242 1.00 11.83 C ANISOU 449 CE2 TYR A 69 1348 1694 1451 -18 -241 -675 C ATOM 450 CZ TYR A 69 11.742 20.194 29.423 1.00 11.61 C ANISOU 450 CZ TYR A 69 1263 1603 1543 116 -30 -571 C ATOM 451 OH TYR A 69 11.170 20.846 30.504 1.00 12.46 O ANISOU 451 OH TYR A 69 1312 1813 1609 68 88 -681 O ATOM 452 N LYS A 70 15.807 19.041 23.792 1.00 10.26 N ANISOU 452 N LYS A 70 1260 1257 1379 -40 2 -432 N ATOM 453 CA LYS A 70 16.877 18.556 22.946 1.00 10.66 C ANISOU 453 CA LYS A 70 1322 1427 1302 11 -51 -351 C ATOM 454 C LYS A 70 18.049 18.154 23.823 1.00 9.83 C ANISOU 454 C LYS A 70 1143 1331 1259 60 -21 -362 C ATOM 455 O LYS A 70 18.557 18.982 24.568 1.00 11.84 O ANISOU 455 O LYS A 70 1435 1485 1575 37 -152 -522 O ATOM 456 CB LYS A 70 17.331 19.638 21.991 1.00 12.21 C ANISOU 456 CB LYS A 70 1677 1618 1344 -65 32 -478 C ATOM 457 CG LYS A 70 18.549 19.221 21.187 1.00 15.74 C ANISOU 457 CG LYS A 70 1886 2133 1961 -70 107 -134 C ATOM 458 CD LYS A 70 18.917 20.150 20.016 1.00 19.03 C ANISOU 458 CD LYS A 70 2204 2695 2330 -148 376 -39 C ATOM 459 CE LYS A 70 19.142 21.532 20.430 1.00 21.37 C ANISOU 459 CE LYS A 70 2653 2826 2640 -137 268 222 C ATOM 460 NZ LYS A 70 19.933 22.279 19.397 1.00 27.31 N ANISOU 460 NZ LYS A 70 3645 3230 3501 -166 493 573 N ATOM 461 N VAL A 71 18.421 16.903 23.756 1.00 10.24 N ANISOU 461 N VAL A 71 1377 1378 1134 55 -108 -416 N ATOM 462 CA VAL A 71 19.579 16.351 24.428 1.00 10.73 C ANISOU 462 CA VAL A 71 1358 1398 1317 -61 -65 -293 C ATOM 463 C VAL A 71 20.676 16.191 23.414 1.00 10.53 C ANISOU 463 C VAL A 71 1470 1358 1171 -50 -163 -330 C ATOM 464 O VAL A 71 20.543 15.403 22.487 1.00 10.96 O ANISOU 464 O VAL A 71 1367 1490 1305 -52 -128 -533 O ATOM 465 CB VAL A 71 19.229 15.019 25.101 1.00 11.55 C ANISOU 465 CB VAL A 71 1439 1572 1374 -80 -94 -229 C ATOM 466 CG1 VAL A 71 20.494 14.370 25.709 1.00 13.53 C ANISOU 466 CG1 VAL A 71 1801 1779 1558 233 -204 -69 C ATOM 467 CG2 VAL A 71 18.140 15.223 26.163 1.00 14.36 C ANISOU 467 CG2 VAL A 71 1839 2017 1598 -276 172 -67 C ATOM 468 N GLU A 72 21.708 17.036 23.560 1.00 11.55 N ANISOU 468 N GLU A 72 1490 1536 1363 8 -32 -153 N ATOM 469 CA AGLU A 72 22.858 17.049 22.672 0.50 11.51 C ANISOU 469 CA AGLU A 72 1584 1497 1290 31 -77 -205 C ATOM 470 C GLU A 72 23.982 16.271 23.372 1.00 9.73 C ANISOU 470 C GLU A 72 1425 1254 1017 6 -167 -384 C ATOM 471 O GLU A 72 24.469 16.672 24.399 1.00 11.60 O ANISOU 471 O GLU A 72 1465 1575 1367 191 -261 -359 O ATOM 472 CB AGLU A 72 23.310 18.482 22.423 0.50 13.04 C ANISOU 472 CB AGLU A 72 1691 1758 1506 59 -112 -176 C ATOM 473 CG AGLU A 72 24.030 18.743 21.132 0.50 14.62 C ANISOU 473 CG AGLU A 72 1856 1930 1766 -27 -101 -130 C ATOM 474 CD AGLU A 72 23.758 20.184 20.685 0.50 16.99 C ANISOU 474 CD AGLU A 72 2373 2079 2002 -86 82 111 C ATOM 475 OE1AGLU A 72 24.334 21.057 21.357 0.50 21.04 O ANISOU 475 OE1AGLU A 72 2773 2373 2848 80 211 -198 O ATOM 476 OE2AGLU A 72 22.919 20.439 19.761 0.50 25.88 O ANISOU 476 OE2AGLU A 72 3402 3381 3047 -291 -14 256 O ATOM 477 N ILE A 73 24.411 15.182 22.705 1.00 10.83 N ANISOU 477 N ILE A 73 1782 1295 1038 177 -27 -201 N ATOM 478 CA ILE A 73 25.489 14.338 23.215 1.00 10.68 C ANISOU 478 CA ILE A 73 1684 1372 1002 53 -85 -236 C ATOM 479 C ILE A 73 26.707 14.628 22.408 1.00 11.66 C ANISOU 479 C ILE A 73 1644 1492 1295 18 -83 -75 C ATOM 480 O ILE A 73 26.669 14.475 21.169 1.00 11.28 O ANISOU 480 O ILE A 73 1690 1666 928 1 174 -100 O ATOM 481 CB ILE A 73 25.101 12.855 23.148 1.00 10.82 C ANISOU 481 CB ILE A 73 1950 1209 949 13 123 -224 C ATOM 482 CG1 ILE A 73 23.749 12.613 23.884 1.00 12.68 C ANISOU 482 CG1 ILE A 73 2008 1647 1161 133 195 -113 C ATOM 483 CG2 ILE A 73 26.223 11.947 23.681 1.00 12.09 C ANISOU 483 CG2 ILE A 73 1771 1751 1070 242 140 14 C ATOM 484 CD1 ILE A 73 23.233 11.177 23.745 1.00 14.84 C ANISOU 484 CD1 ILE A 73 2242 1832 1565 -8 186 -375 C ATOM 485 N ASP A 74 27.754 15.092 23.036 1.00 10.77 N ANISOU 485 N ASP A 74 1718 1534 839 43 -16 -28 N ATOM 486 CA ASP A 74 28.900 15.641 22.313 1.00 12.25 C ANISOU 486 CA ASP A 74 1803 1663 1186 -153 -55 8 C ATOM 487 C ASP A 74 29.874 14.534 21.892 1.00 11.88 C ANISOU 487 C ASP A 74 1572 1919 1021 -263 131 37 C ATOM 488 O ASP A 74 30.972 14.352 22.426 1.00 11.48 O ANISOU 488 O ASP A 74 1488 1868 1005 -215 82 -126 O ATOM 489 CB ASP A 74 29.520 16.746 23.167 1.00 12.63 C ANISOU 489 CB ASP A 74 1853 1615 1331 -167 -95 -52 C ATOM 490 CG ASP A 74 28.596 17.979 23.266 1.00 17.22 C ANISOU 490 CG ASP A 74 2272 2184 2086 56 -77 -160 C ATOM 491 OD1 ASP A 74 27.744 18.225 22.371 1.00 18.51 O ANISOU 491 OD1 ASP A 74 2259 2045 2727 286 -296 -226 O ATOM 492 OD2 ASP A 74 28.746 18.730 24.234 1.00 21.62 O ANISOU 492 OD2 ASP A 74 3198 2713 2301 356 -1 -761 O ATOM 493 N THR A 75 29.448 13.764 20.915 1.00 10.82 N ANISOU 493 N THR A 75 1489 1697 923 -105 67 -75 N ATOM 494 CA THR A 75 30.149 12.591 20.486 1.00 11.38 C ANISOU 494 CA THR A 75 1451 1721 1150 -163 61 82 C ATOM 495 C THR A 75 31.489 12.947 19.807 1.00 11.53 C ANISOU 495 C THR A 75 1335 1728 1317 -183 49 -28 C ATOM 496 O THR A 75 32.476 12.239 19.992 1.00 12.46 O ANISOU 496 O THR A 75 1238 2230 1266 -170 25 101 O ATOM 497 CB THR A 75 29.271 11.782 19.510 1.00 11.46 C ANISOU 497 CB THR A 75 1367 1605 1382 -48 49 10 C ATOM 498 OG1 THR A 75 28.955 12.571 18.369 1.00 10.43 O ANISOU 498 OG1 THR A 75 1158 1663 1140 -7 60 -106 O ATOM 499 CG2 THR A 75 27.983 11.311 20.174 1.00 11.37 C ANISOU 499 CG2 THR A 75 1253 1637 1429 -262 288 -22 C ATOM 500 N LYS A 76 31.523 14.057 19.049 1.00 12.18 N ANISOU 500 N LYS A 76 1315 1927 1383 -163 81 50 N ATOM 501 CA LYS A 76 32.798 14.387 18.400 1.00 13.91 C ANISOU 501 CA LYS A 76 1479 2123 1682 -236 11 119 C ATOM 502 C LYS A 76 33.880 14.705 19.462 1.00 14.82 C ANISOU 502 C LYS A 76 1541 2182 1909 -371 50 185 C ATOM 503 O LYS A 76 35.006 14.229 19.328 1.00 16.72 O ANISOU 503 O LYS A 76 1742 2778 1831 -350 -178 620 O ATOM 504 CB LYS A 76 32.654 15.567 17.458 1.00 13.76 C ANISOU 504 CB LYS A 76 1360 2085 1782 -101 -25 28 C ATOM 505 CG LYS A 76 33.934 15.904 16.750 1.00 16.59 C ANISOU 505 CG LYS A 76 1777 2458 2065 -217 34 284 C ATOM 506 CD LYS A 76 33.707 16.966 15.707 1.00 18.26 C ANISOU 506 CD LYS A 76 2022 2598 2315 -228 -12 377 C ATOM 507 CE LYS A 76 34.888 17.308 14.900 1.00 23.36 C ANISOU 507 CE LYS A 76 2902 3244 2729 35 217 416 C ATOM 508 NZ LYS A 76 34.461 18.257 13.848 1.00 26.89 N ANISOU 508 NZ LYS A 76 3273 3774 3168 70 105 824 N ATOM 509 N SER A 77 33.502 15.529 20.467 1.00 15.13 N ANISOU 509 N SER A 77 1761 2256 1732 -370 -195 298 N ATOM 510 CA SER A 77 34.413 15.915 21.588 1.00 16.95 C ANISOU 510 CA SER A 77 2036 2466 1937 -332 -154 232 C ATOM 511 C SER A 77 34.862 14.660 22.290 1.00 17.34 C ANISOU 511 C SER A 77 2186 2448 1953 -422 -290 173 C ATOM 512 O SER A 77 36.025 14.566 22.681 1.00 17.72 O ANISOU 512 O SER A 77 2148 2643 1940 -486 -65 281 O ATOM 513 CB SER A 77 33.756 16.927 22.550 1.00 18.43 C ANISOU 513 CB SER A 77 2529 2465 2008 -172 -429 229 C ATOM 514 OG SER A 77 33.642 18.237 21.962 1.00 20.68 O ANISOU 514 OG SER A 77 2851 2565 2442 -454 -335 252 O ATOM 515 N TYR A 78 33.947 13.671 22.463 1.00 15.84 N ANISOU 515 N TYR A 78 1947 2422 1649 -504 -203 375 N ATOM 516 CA TYR A 78 34.310 12.396 23.104 1.00 15.93 C ANISOU 516 CA TYR A 78 1858 2369 1825 -296 -181 178 C ATOM 517 C TYR A 78 35.360 11.648 22.304 1.00 14.89 C ANISOU 517 C TYR A 78 1813 2303 1540 -331 -145 212 C ATOM 518 O TYR A 78 36.431 11.301 22.843 1.00 17.10 O ANISOU 518 O TYR A 78 1881 2623 1993 -391 -168 388 O ATOM 519 CB TYR A 78 33.080 11.481 23.214 1.00 14.67 C ANISOU 519 CB TYR A 78 1745 2324 1501 -409 -102 183 C ATOM 520 CG TYR A 78 33.370 10.026 23.629 1.00 14.31 C ANISOU 520 CG TYR A 78 1589 2364 1481 -365 -85 66 C ATOM 521 CD1 TYR A 78 33.621 9.725 24.931 1.00 14.15 C ANISOU 521 CD1 TYR A 78 1934 2054 1387 -247 -203 142 C ATOM 522 CD2 TYR A 78 33.355 8.978 22.742 1.00 12.84 C ANISOU 522 CD2 TYR A 78 1433 2086 1359 -312 196 194 C ATOM 523 CE1 TYR A 78 33.860 8.435 25.344 1.00 14.24 C ANISOU 523 CE1 TYR A 78 1737 2124 1548 -149 -106 58 C ATOM 524 CE2 TYR A 78 33.599 7.697 23.107 1.00 11.88 C ANISOU 524 CE2 TYR A 78 995 2270 1248 -92 0 -46 C ATOM 525 CZ TYR A 78 33.865 7.411 24.445 1.00 13.54 C ANISOU 525 CZ TYR A 78 1673 2181 1288 14 -154 -46 C ATOM 526 OH TYR A 78 34.077 6.119 24.876 1.00 13.56 O ANISOU 526 OH TYR A 78 1574 2201 1377 -245 -4 -51 O ATOM 527 N TRP A 79 35.110 11.435 20.991 1.00 15.71 N ANISOU 527 N TRP A 79 1665 2721 1581 -380 -150 305 N ATOM 528 CA TRP A 79 36.013 10.680 20.138 1.00 15.28 C ANISOU 528 CA TRP A 79 1733 2404 1667 -92 -172 417 C ATOM 529 C TRP A 79 37.355 11.473 19.956 1.00 17.05 C ANISOU 529 C TRP A 79 1685 2521 2269 -197 -93 210 C ATOM 530 O TRP A 79 38.415 10.891 20.075 1.00 17.33 O ANISOU 530 O TRP A 79 1729 2923 1933 -303 -204 338 O ATOM 531 CB TRP A 79 35.423 10.377 18.742 1.00 15.01 C ANISOU 531 CB TRP A 79 1559 2542 1599 -22 39 410 C ATOM 532 CG TRP A 79 34.262 9.395 18.760 1.00 13.80 C ANISOU 532 CG TRP A 79 1610 2283 1349 -48 -305 361 C ATOM 533 CD1 TRP A 79 32.960 9.627 18.421 1.00 13.67 C ANISOU 533 CD1 TRP A 79 1555 2289 1350 242 163 193 C ATOM 534 CD2 TRP A 79 34.338 8.009 19.078 1.00 13.11 C ANISOU 534 CD2 TRP A 79 1444 2166 1369 292 311 499 C ATOM 535 NE1 TRP A 79 32.199 8.474 18.591 1.00 12.06 N ANISOU 535 NE1 TRP A 79 1299 2112 1171 382 169 431 N ATOM 536 CE2 TRP A 79 33.033 7.463 18.978 1.00 13.57 C ANISOU 536 CE2 TRP A 79 1609 2176 1370 75 285 422 C ATOM 537 CE3 TRP A 79 35.372 7.173 19.499 1.00 15.54 C ANISOU 537 CE3 TRP A 79 1604 2504 1793 437 89 378 C ATOM 538 CZ2 TRP A 79 32.729 6.159 19.323 1.00 13.09 C ANISOU 538 CZ2 TRP A 79 1453 2064 1454 551 344 180 C ATOM 539 CZ3 TRP A 79 35.081 5.834 19.763 1.00 16.20 C ANISOU 539 CZ3 TRP A 79 1830 2397 1926 485 53 72 C ATOM 540 CH2 TRP A 79 33.788 5.331 19.693 1.00 14.59 C ANISOU 540 CH2 TRP A 79 1933 2007 1601 223 -62 306 C ATOM 541 N LYS A 80 37.281 12.803 19.831 1.00 17.20 N ANISOU 541 N LYS A 80 1663 2745 2126 -305 109 453 N ATOM 542 CA LYS A 80 38.529 13.632 19.667 1.00 18.80 C ANISOU 542 CA LYS A 80 1894 2755 2493 -246 -79 146 C ATOM 543 C LYS A 80 39.381 13.615 20.950 1.00 19.60 C ANISOU 543 C LYS A 80 2017 2946 2484 -236 -103 156 C ATOM 544 O LYS A 80 40.602 13.577 20.861 1.00 20.41 O ANISOU 544 O LYS A 80 2087 2889 2778 -572 11 37 O ATOM 545 CB LYS A 80 38.168 15.034 19.252 1.00 19.01 C ANISOU 545 CB LYS A 80 1902 2794 2527 -488 -27 209 C ATOM 546 CG LYS A 80 37.779 15.097 17.780 1.00 22.30 C ANISOU 546 CG LYS A 80 2347 3319 2805 -156 -71 322 C ATOM 547 CD LYS A 80 37.452 16.501 17.381 1.00 24.60 C ANISOU 547 CD LYS A 80 2802 3318 3224 -216 -113 198 C ATOM 548 CE LYS A 80 38.731 17.380 17.326 1.00 28.51 C ANISOU 548 CE LYS A 80 3358 3606 3865 -356 -9 230 C ATOM 549 NZ LYS A 80 38.409 18.702 16.693 1.00 30.99 N ANISOU 549 NZ LYS A 80 4042 3647 4086 -212 -128 206 N ATOM 550 N ALA A 81 38.753 13.557 22.135 1.00 17.53 N ANISOU 550 N ALA A 81 1765 2637 2256 -188 -249 -51 N ATOM 551 CA ALA A 81 39.481 13.426 23.402 1.00 18.99 C ANISOU 551 CA ALA A 81 1937 2889 2388 -229 -264 -46 C ATOM 552 C ALA A 81 40.182 12.084 23.466 1.00 18.99 C ANISOU 552 C ALA A 81 1958 2844 2411 -150 -369 39 C ATOM 553 O ALA A 81 41.194 11.938 24.196 1.00 23.42 O ANISOU 553 O ALA A 81 2539 3465 2893 -31 -762 67 O ATOM 554 CB ALA A 81 38.528 13.621 24.599 1.00 17.46 C ANISOU 554 CB ALA A 81 1986 2731 1914 -82 -275 3 C ATOM 555 N LEU A 82 39.716 11.093 22.729 1.00 18.93 N ANISOU 555 N LEU A 82 2176 2871 2142 -95 -298 -40 N ATOM 556 CA LEU A 82 40.348 9.799 22.600 1.00 18.75 C ANISOU 556 CA LEU A 82 2047 2850 2224 -66 -109 37 C ATOM 557 C LEU A 82 41.303 9.720 21.430 1.00 20.46 C ANISOU 557 C LEU A 82 2439 2950 2384 -34 -108 -93 C ATOM 558 O LEU A 82 41.859 8.666 21.154 1.00 22.28 O ANISOU 558 O LEU A 82 2304 3246 2913 358 204 199 O ATOM 559 CB LEU A 82 39.289 8.670 22.501 1.00 19.09 C ANISOU 559 CB LEU A 82 2331 2754 2166 -88 25 -210 C ATOM 560 CG LEU A 82 38.413 8.464 23.769 1.00 19.37 C ANISOU 560 CG LEU A 82 1992 2996 2372 53 -77 205 C ATOM 561 CD1 LEU A 82 37.285 7.469 23.511 1.00 21.38 C ANISOU 561 CD1 LEU A 82 2064 3303 2754 -23 -37 384 C ATOM 562 CD2 LEU A 82 39.298 7.998 24.968 1.00 21.38 C ANISOU 562 CD2 LEU A 82 2421 3372 2330 -307 -154 269 C ATOM 563 N GLY A 83 41.476 10.841 20.728 1.00 19.63 N ANISOU 563 N GLY A 83 2110 2981 2366 -152 -251 -55 N ATOM 564 CA GLY A 83 42.414 10.933 19.590 1.00 19.90 C ANISOU 564 CA GLY A 83 2193 3054 2313 -81 -142 -106 C ATOM 565 C GLY A 83 41.945 10.305 18.296 1.00 19.90 C ANISOU 565 C GLY A 83 2181 3158 2221 -78 -142 -119 C ATOM 566 O GLY A 83 42.763 10.040 17.428 1.00 23.56 O ANISOU 566 O GLY A 83 2621 3728 2601 -29 -23 -179 O ATOM 567 N ILE A 84 40.616 10.132 18.161 1.00 19.72 N ANISOU 567 N ILE A 84 2247 3078 2167 36 -71 3 N ATOM 568 CA ILE A 84 39.909 9.523 16.998 1.00 20.70 C ANISOU 568 CA ILE A 84 2501 3118 2244 61 -116 48 C ATOM 569 C ILE A 84 39.137 10.624 16.245 1.00 20.66 C ANISOU 569 C ILE A 84 2674 2954 2219 351 -18 -21 C ATOM 570 O ILE A 84 38.582 11.517 16.928 1.00 22.67 O ANISOU 570 O ILE A 84 2762 3469 2381 584 -329 77 O ATOM 571 CB ILE A 84 38.847 8.476 17.550 1.00 19.75 C ANISOU 571 CB ILE A 84 2281 2968 2253 101 -172 -7 C ATOM 572 CG1 ILE A 84 39.596 7.480 18.466 1.00 24.17 C ANISOU 572 CG1 ILE A 84 3062 3170 2951 -10 -41 292 C ATOM 573 CG2 ILE A 84 38.118 7.793 16.454 1.00 20.10 C ANISOU 573 CG2 ILE A 84 2414 3115 2106 -60 -225 -95 C ATOM 574 CD1 ILE A 84 38.885 6.253 18.936 1.00 25.58 C ANISOU 574 CD1 ILE A 84 3278 3277 3163 -110 -79 113 C ATOM 575 N SER A 85 39.197 10.596 14.907 1.00 19.70 N ANISOU 575 N SER A 85 2308 2943 2230 169 238 283 N ATOM 576 CA SER A 85 38.457 11.515 14.004 1.00 18.92 C ANISOU 576 CA SER A 85 2225 2811 2150 165 189 253 C ATOM 577 C SER A 85 37.087 10.952 13.619 1.00 18.47 C ANISOU 577 C SER A 85 2265 2567 2184 256 280 436 C ATOM 578 O SER A 85 36.984 10.117 12.739 1.00 19.09 O ANISOU 578 O SER A 85 2203 2753 2294 255 496 156 O ATOM 579 CB ASER A 85 39.271 11.742 12.689 0.65 19.53 C ANISOU 579 CB ASER A 85 2276 2900 2244 10 183 272 C ATOM 580 OG ASER A 85 40.585 12.231 12.963 0.65 21.16 O ANISOU 580 OG ASER A 85 2392 3094 2554 -46 26 105 O ATOM 581 N PRO A 86 35.996 11.376 14.307 1.00 16.48 N ANISOU 581 N PRO A 86 1940 2423 1899 319 311 442 N ATOM 582 CA PRO A 86 34.741 10.710 13.971 1.00 16.29 C ANISOU 582 CA PRO A 86 2039 2400 1746 305 325 364 C ATOM 583 C PRO A 86 33.904 11.431 12.895 1.00 15.22 C ANISOU 583 C PRO A 86 1791 2226 1764 389 343 233 C ATOM 584 O PRO A 86 34.262 12.541 12.472 1.00 15.51 O ANISOU 584 O PRO A 86 2101 2368 1421 271 538 620 O ATOM 585 CB PRO A 86 33.984 10.841 15.285 1.00 15.62 C ANISOU 585 CB PRO A 86 1687 2638 1606 291 362 440 C ATOM 586 CG PRO A 86 34.379 12.202 15.754 1.00 16.81 C ANISOU 586 CG PRO A 86 1861 2587 1936 539 243 274 C ATOM 587 CD PRO A 86 35.848 12.366 15.351 1.00 18.54 C ANISOU 587 CD PRO A 86 2278 2615 2151 256 287 444 C ATOM 588 N PHE A 87 32.759 10.866 12.508 1.00 12.85 N ANISOU 588 N PHE A 87 1740 1750 1392 378 242 375 N ATOM 589 CA PHE A 87 31.934 11.525 11.454 1.00 13.61 C ANISOU 589 CA PHE A 87 1938 1926 1306 346 318 330 C ATOM 590 C PHE A 87 31.017 12.639 11.939 1.00 12.52 C ANISOU 590 C PHE A 87 1933 1608 1215 354 309 307 C ATOM 591 O PHE A 87 30.926 13.698 11.315 1.00 13.64 O ANISOU 591 O PHE A 87 2168 1441 1573 344 270 255 O ATOM 592 CB PHE A 87 31.114 10.490 10.755 1.00 13.19 C ANISOU 592 CB PHE A 87 2073 1723 1213 365 390 327 C ATOM 593 CG PHE A 87 30.348 11.014 9.579 1.00 14.56 C ANISOU 593 CG PHE A 87 2286 1631 1614 263 206 179 C ATOM 594 CD1 PHE A 87 30.990 11.309 8.390 1.00 17.38 C ANISOU 594 CD1 PHE A 87 2550 2058 1994 297 182 133 C ATOM 595 CD2 PHE A 87 28.979 11.199 9.665 1.00 14.60 C ANISOU 595 CD2 PHE A 87 2598 1642 1307 302 -34 198 C ATOM 596 CE1 PHE A 87 30.290 11.819 7.318 1.00 16.73 C ANISOU 596 CE1 PHE A 87 2671 2174 1509 127 120 1 C ATOM 597 CE2 PHE A 87 28.274 11.735 8.575 1.00 16.89 C ANISOU 597 CE2 PHE A 87 2602 1991 1822 149 -213 -148 C ATOM 598 CZ PHE A 87 28.934 11.983 7.414 1.00 16.90 C ANISOU 598 CZ PHE A 87 2577 2106 1736 270 -289 305 C ATOM 599 N HIS A 88 30.245 12.364 12.982 1.00 10.73 N ANISOU 599 N HIS A 88 1573 1436 1064 238 75 221 N ATOM 600 CA HIS A 88 29.192 13.299 13.395 1.00 10.51 C ANISOU 600 CA HIS A 88 1511 1420 1059 233 18 158 C ATOM 601 C HIS A 88 29.753 14.360 14.310 1.00 10.87 C ANISOU 601 C HIS A 88 1494 1642 994 91 -25 71 C ATOM 602 O HIS A 88 30.710 14.164 15.047 1.00 11.43 O ANISOU 602 O HIS A 88 1296 1769 1277 174 -231 15 O ATOM 603 CB HIS A 88 28.056 12.552 14.140 1.00 10.81 C ANISOU 603 CB HIS A 88 1364 1417 1325 298 -79 -15 C ATOM 604 CG HIS A 88 27.457 11.472 13.287 1.00 9.70 C ANISOU 604 CG HIS A 88 1302 1069 1311 170 -285 53 C ATOM 605 ND1 HIS A 88 27.882 10.151 13.350 1.00 11.72 N ANISOU 605 ND1 HIS A 88 1585 1325 1544 221 -10 231 N ATOM 606 CD2 HIS A 88 26.491 11.535 12.340 1.00 12.52 C ANISOU 606 CD2 HIS A 88 1880 1375 1502 195 -219 -46 C ATOM 607 CE1 HIS A 88 27.189 9.455 12.469 1.00 12.24 C ANISOU 607 CE1 HIS A 88 1746 1046 1857 -19 -292 282 C ATOM 608 NE2 HIS A 88 26.338 10.263 11.847 1.00 11.61 N ANISOU 608 NE2 HIS A 88 1899 1177 1334 55 44 86 N ATOM 609 N GLU A 89 29.090 15.494 14.316 1.00 10.15 N ANISOU 609 N GLU A 89 1459 1557 840 109 -17 111 N ATOM 610 CA GLU A 89 29.411 16.548 15.253 1.00 10.61 C ANISOU 610 CA GLU A 89 1258 1609 1161 -86 73 -16 C ATOM 611 C GLU A 89 28.928 16.212 16.659 1.00 11.59 C ANISOU 611 C GLU A 89 1445 1831 1125 -29 -18 -101 C ATOM 612 O GLU A 89 29.624 16.419 17.637 1.00 13.34 O ANISOU 612 O GLU A 89 1544 2353 1171 -106 -169 -199 O ATOM 613 CB GLU A 89 28.780 17.859 14.806 1.00 12.12 C ANISOU 613 CB GLU A 89 1648 1679 1275 -45 -20 -95 C ATOM 614 CG GLU A 89 29.395 18.458 13.560 1.00 14.41 C ANISOU 614 CG GLU A 89 2116 1861 1498 -67 -124 26 C ATOM 615 CD GLU A 89 30.853 18.787 13.763 1.00 18.58 C ANISOU 615 CD GLU A 89 2717 2171 2169 -44 123 433 C ATOM 616 OE1 GLU A 89 31.155 19.525 14.704 1.00 21.95 O ANISOU 616 OE1 GLU A 89 2557 3052 2729 -696 -24 363 O ATOM 617 OE2 GLU A 89 31.664 18.274 13.033 1.00 20.36 O ANISOU 617 OE2 GLU A 89 2505 2938 2292 183 148 1242 O ATOM 618 N HIS A 90 27.723 15.715 16.765 1.00 11.09 N ANISOU 618 N HIS A 90 1398 1854 960 -44 -18 -78 N ATOM 619 CA HIS A 90 27.053 15.371 18.028 1.00 11.81 C ANISOU 619 CA HIS A 90 1670 1837 979 77 254 -175 C ATOM 620 C HIS A 90 25.933 14.543 17.746 1.00 16.80 C ANISOU 620 C HIS A 90 2165 2336 1882 -161 25 -52 C ATOM 621 O HIS A 90 25.617 14.404 16.612 1.00 13.68 O ANISOU 621 O HIS A 90 1796 3002 399 -790 37 -93 O ATOM 622 CB HIS A 90 26.744 16.629 18.851 1.00 15.90 C ANISOU 622 CB HIS A 90 2304 2249 1487 69 343 -388 C ATOM 623 CG HIS A 90 26.030 17.676 18.124 1.00 19.52 C ANISOU 623 CG HIS A 90 2479 2771 2167 363 530 -364 C ATOM 624 ND1 HIS A 90 26.547 18.935 17.892 1.00 23.41 N ANISOU 624 ND1 HIS A 90 3217 2997 2679 74 -93 -202 N ATOM 625 CD2 HIS A 90 24.812 17.648 17.536 1.00 26.46 C ANISOU 625 CD2 HIS A 90 3406 3325 3320 24 -175 -86 C ATOM 626 CE1 HIS A 90 25.652 19.648 17.227 1.00 25.53 C ANISOU 626 CE1 HIS A 90 3550 2917 3231 213 -75 -107 C ATOM 627 NE2 HIS A 90 24.589 18.892 17.001 1.00 29.40 N ANISOU 627 NE2 HIS A 90 3996 3339 3834 296 -198 76 N ATOM 628 N ALA A 91 25.283 13.910 18.632 1.00 11.80 N ANISOU 628 N ALA A 91 1549 2221 713 -289 92 -249 N ATOM 629 CA ALA A 91 24.011 13.264 18.467 1.00 15.51 C ANISOU 629 CA ALA A 91 1923 2645 1324 -262 36 -226 C ATOM 630 C ALA A 91 23.009 14.200 19.277 1.00 12.95 C ANISOU 630 C ALA A 91 1608 2617 692 -418 -196 -719 C ATOM 631 O ALA A 91 23.250 14.645 20.402 1.00 26.97 O ANISOU 631 O ALA A 91 2459 4358 3428 -80 171 -40 O ATOM 632 CB ALA A 91 24.062 11.864 19.122 1.00 16.34 C ANISOU 632 CB ALA A 91 2462 2408 1337 -403 -58 -330 C ATOM 633 N GLU A 92 21.847 14.437 18.542 1.00 18.54 N ANISOU 633 N GLU A 92 2069 3153 1820 -45 132 -181 N ATOM 634 CA GLU A 92 20.802 15.292 19.049 1.00 18.47 C ANISOU 634 CA GLU A 92 2114 2962 1942 -112 31 -161 C ATOM 635 C GLU A 92 19.605 14.397 19.229 1.00 17.49 C ANISOU 635 C GLU A 92 1960 2954 1729 -193 -39 -304 C ATOM 636 O GLU A 92 19.227 13.645 18.298 1.00 21.99 O ANISOU 636 O GLU A 92 2401 3998 1954 -322 281 -697 O ATOM 637 CB GLU A 92 20.451 16.406 18.029 1.00 20.74 C ANISOU 637 CB GLU A 92 2348 3222 2309 -36 82 -67 C ATOM 638 CG GLU A 92 21.522 17.500 17.900 1.00 25.75 C ANISOU 638 CG GLU A 92 3190 3527 3064 -29 0 51 C ATOM 639 CD GLU A 92 21.117 18.668 16.978 1.00 26.42 C ANISOU 639 CD GLU A 92 3176 3594 3268 -58 -11 123 C ATOM 640 OE1 GLU A 92 19.907 18.776 16.618 1.00 35.62 O ANISOU 640 OE1 GLU A 92 4037 4829 4668 179 -173 -84 O ATOM 641 OE2 GLU A 92 21.976 19.534 16.692 1.00 35.10 O ANISOU 641 OE2 GLU A 92 3954 4556 4825 -165 105 133 O ATOM 642 N VAL A 93 18.958 14.451 20.367 1.00 13.48 N ANISOU 642 N VAL A 93 1652 2053 1415 120 57 -364 N ATOM 643 CA VAL A 93 17.745 13.673 20.637 1.00 12.39 C ANISOU 643 CA VAL A 93 1751 1623 1333 74 -118 -275 C ATOM 644 C VAL A 93 16.665 14.694 21.011 1.00 10.68 C ANISOU 644 C VAL A 93 1425 1404 1226 -31 -48 -342 C ATOM 645 O VAL A 93 16.805 15.346 22.046 1.00 11.58 O ANISOU 645 O VAL A 93 1594 1532 1274 22 -148 -478 O ATOM 646 CB VAL A 93 18.032 12.652 21.756 1.00 13.50 C ANISOU 646 CB VAL A 93 2018 1672 1438 230 -67 -249 C ATOM 647 CG1 VAL A 93 16.797 11.856 22.002 1.00 17.08 C ANISOU 647 CG1 VAL A 93 2008 2249 2230 -278 -284 20 C ATOM 648 CG2 VAL A 93 19.270 11.779 21.410 1.00 15.03 C ANISOU 648 CG2 VAL A 93 2034 1943 1732 247 -145 -341 C ATOM 649 N VAL A 94 15.621 14.825 20.213 1.00 10.11 N ANISOU 649 N VAL A 94 1488 1303 1047 53 -17 -189 N ATOM 650 CA VAL A 94 14.615 15.886 20.388 1.00 10.25 C ANISOU 650 CA VAL A 94 1406 1331 1157 -86 -110 -256 C ATOM 651 C VAL A 94 13.250 15.209 20.583 1.00 9.74 C ANISOU 651 C VAL A 94 1331 1189 1181 -25 -23 -247 C ATOM 652 O VAL A 94 12.821 14.367 19.800 1.00 10.34 O ANISOU 652 O VAL A 94 1479 1394 1056 -233 -25 -392 O ATOM 653 CB VAL A 94 14.584 16.866 19.188 1.00 11.51 C ANISOU 653 CB VAL A 94 1519 1413 1438 -240 -30 -35 C ATOM 654 CG1 VAL A 94 13.623 17.989 19.393 1.00 12.87 C ANISOU 654 CG1 VAL A 94 1684 1510 1696 238 -163 21 C ATOM 655 CG2 VAL A 94 16.007 17.364 18.894 1.00 13.71 C ANISOU 655 CG2 VAL A 94 1612 1976 1619 -344 73 167 C ATOM 656 N PHE A 95 12.572 15.620 21.665 1.00 9.84 N ANISOU 656 N PHE A 95 1404 1176 1158 60 32 -348 N ATOM 657 CA PHE A 95 11.331 14.982 22.057 1.00 9.79 C ANISOU 657 CA PHE A 95 1425 1316 978 11 28 -254 C ATOM 658 C PHE A 95 10.486 15.906 22.928 1.00 9.27 C ANISOU 658 C PHE A 95 1334 1154 1034 -5 71 -385 C ATOM 659 O PHE A 95 11.006 16.755 23.638 1.00 11.59 O ANISOU 659 O PHE A 95 1493 1409 1499 12 -73 -498 O ATOM 660 CB PHE A 95 11.620 13.698 22.830 1.00 11.07 C ANISOU 660 CB PHE A 95 1541 1373 1289 59 75 -177 C ATOM 661 CG PHE A 95 12.444 13.885 24.053 1.00 11.89 C ANISOU 661 CG PHE A 95 1759 1288 1472 46 141 108 C ATOM 662 CD1 PHE A 95 13.820 14.018 23.957 1.00 13.09 C ANISOU 662 CD1 PHE A 95 1883 1795 1294 92 -135 0 C ATOM 663 CD2 PHE A 95 11.843 13.910 25.310 1.00 12.99 C ANISOU 663 CD2 PHE A 95 1971 1533 1429 94 -45 -187 C ATOM 664 CE1 PHE A 95 14.629 14.133 25.045 1.00 13.64 C ANISOU 664 CE1 PHE A 95 1918 1757 1508 -82 -175 101 C ATOM 665 CE2 PHE A 95 12.670 14.053 26.470 1.00 13.82 C ANISOU 665 CE2 PHE A 95 2529 1391 1330 307 101 66 C ATOM 666 CZ PHE A 95 14.046 14.213 26.281 1.00 14.03 C ANISOU 666 CZ PHE A 95 2405 1752 1171 23 -429 -475 C ATOM 667 N THR A 96 9.188 15.698 22.845 1.00 11.38 N ANISOU 667 N THR A 96 1532 1396 1393 -1 -17 -553 N ATOM 668 CA THR A 96 8.248 16.308 23.764 1.00 11.70 C ANISOU 668 CA THR A 96 1395 1436 1612 -37 -6 -480 C ATOM 669 C THR A 96 8.231 15.504 25.057 1.00 11.95 C ANISOU 669 C THR A 96 1520 1441 1576 -132 130 -467 C ATOM 670 O THR A 96 8.215 14.288 25.016 1.00 14.73 O ANISOU 670 O THR A 96 2207 1617 1772 -140 305 -347 O ATOM 671 CB THR A 96 6.846 16.350 23.161 1.00 12.82 C ANISOU 671 CB THR A 96 1355 1677 1838 56 -114 -484 C ATOM 672 OG1 THR A 96 6.868 17.148 21.978 1.00 16.25 O ANISOU 672 OG1 THR A 96 1900 2155 2118 319 -169 -366 O ATOM 673 CG2 THR A 96 5.871 16.945 24.136 1.00 15.54 C ANISOU 673 CG2 THR A 96 1729 2292 1883 222 39 -664 C ATOM 674 N ALA A 97 8.309 16.185 26.194 1.00 12.13 N ANISOU 674 N ALA A 97 1603 1345 1660 -44 110 -441 N ATOM 675 CA ALA A 97 8.307 15.513 27.474 1.00 12.15 C ANISOU 675 CA ALA A 97 1464 1545 1606 -4 143 -440 C ATOM 676 C ALA A 97 7.174 16.036 28.343 1.00 11.52 C ANISOU 676 C ALA A 97 1516 1288 1572 -66 195 -582 C ATOM 677 O ALA A 97 6.818 17.197 28.263 1.00 14.96 O ANISOU 677 O ALA A 97 1933 1686 2064 -35 240 -342 O ATOM 678 CB ALA A 97 9.662 15.707 28.232 1.00 13.66 C ANISOU 678 CB ALA A 97 1410 2091 1690 -233 204 -495 C ATOM 679 N ASN A 98 6.651 15.134 29.186 1.00 12.58 N ANISOU 679 N ASN A 98 1671 1449 1659 182 230 -413 N ATOM 680 CA ASN A 98 5.744 15.450 30.268 1.00 14.13 C ANISOU 680 CA ASN A 98 1746 1775 1846 92 173 -298 C ATOM 681 C ASN A 98 4.422 16.013 29.853 1.00 16.98 C ANISOU 681 C ASN A 98 1926 2242 2282 211 242 -150 C ATOM 682 O ASN A 98 3.733 16.683 30.639 1.00 18.22 O ANISOU 682 O ASN A 98 1845 2659 2417 545 336 -241 O ATOM 683 CB ASN A 98 6.407 16.371 31.308 1.00 14.84 C ANISOU 683 CB ASN A 98 2061 1777 1800 142 249 -331 C ATOM 684 CG ASN A 98 7.688 15.831 31.814 1.00 13.93 C ANISOU 684 CG ASN A 98 1904 1854 1532 121 350 -580 C ATOM 685 OD1 ASN A 98 7.745 14.680 32.303 1.00 15.14 O ANISOU 685 OD1 ASN A 98 2021 1893 1835 178 409 -229 O ATOM 686 ND2 ASN A 98 8.764 16.601 31.624 1.00 15.44 N ANISOU 686 ND2 ASN A 98 1934 2096 1833 -229 134 -433 N ATOM 687 N ASP A 99 4.037 15.742 28.626 1.00 17.34 N ANISOU 687 N ASP A 99 1801 2371 2413 292 190 -194 N ATOM 688 CA ASP A 99 2.807 16.349 28.128 1.00 20.22 C ANISOU 688 CA ASP A 99 2220 2753 2708 94 21 -66 C ATOM 689 C ASP A 99 1.533 15.621 28.576 1.00 20.44 C ANISOU 689 C ASP A 99 2039 2894 2831 178 56 -40 C ATOM 690 O ASP A 99 0.425 16.103 28.338 1.00 21.77 O ANISOU 690 O ASP A 99 1801 3294 3176 248 -185 145 O ATOM 691 CB ASP A 99 2.919 16.578 26.628 1.00 21.94 C ANISOU 691 CB ASP A 99 2458 2995 2882 246 -48 -136 C ATOM 692 CG ASP A 99 3.084 15.342 25.900 1.00 24.82 C ANISOU 692 CG ASP A 99 3259 3237 2934 62 -173 -403 C ATOM 693 OD1 ASP A 99 3.787 14.432 26.430 1.00 28.75 O ANISOU 693 OD1 ASP A 99 4225 3959 2736 -92 -439 -351 O ATOM 694 OD2 ASP A 99 2.540 15.285 24.771 1.00 33.98 O ANISOU 694 OD2 ASP A 99 4006 4849 4053 278 -336 -135 O ATOM 695 N SER A 100 1.688 14.464 29.223 1.00 20.87 N ANISOU 695 N SER A 100 1989 2998 2941 -18 155 47 N ATOM 696 CA SER A 100 0.573 13.738 29.869 1.00 22.21 C ANISOU 696 CA SER A 100 2317 2988 3132 -26 205 -27 C ATOM 697 C SER A 100 0.903 13.569 31.323 1.00 21.41 C ANISOU 697 C SER A 100 2241 2801 3091 -142 222 -109 C ATOM 698 O SER A 100 0.523 12.576 31.953 1.00 26.51 O ANISOU 698 O SER A 100 3158 3282 3630 -309 152 -7 O ATOM 699 CB SER A 100 0.411 12.366 29.227 1.00 23.54 C ANISOU 699 CB SER A 100 2430 3209 3303 -47 154 -14 C ATOM 700 OG SER A 100 0.079 12.519 27.858 1.00 30.71 O ANISOU 700 OG SER A 100 3640 4268 3761 -152 -83 123 O ATOM 701 N GLY A 101 1.626 14.525 31.890 1.00 19.67 N ANISOU 701 N GLY A 101 2101 2489 2881 47 348 -246 N ATOM 702 CA GLY A 101 2.007 14.450 33.241 1.00 18.64 C ANISOU 702 CA GLY A 101 2032 2447 2599 78 337 -265 C ATOM 703 C GLY A 101 3.424 13.946 33.371 1.00 17.71 C ANISOU 703 C GLY A 101 1975 2264 2489 102 391 -342 C ATOM 704 O GLY A 101 4.072 13.499 32.360 1.00 17.08 O ANISOU 704 O GLY A 101 1792 2404 2292 139 742 -543 O ATOM 705 N PRO A 102 3.985 13.995 34.579 1.00 17.46 N ANISOU 705 N PRO A 102 2029 2371 2232 164 635 -501 N ATOM 706 CA PRO A 102 5.397 13.685 34.731 1.00 17.53 C ANISOU 706 CA PRO A 102 2075 2244 2341 -15 341 -416 C ATOM 707 C PRO A 102 5.699 12.248 34.316 1.00 17.10 C ANISOU 707 C PRO A 102 1945 2192 2359 1 459 -427 C ATOM 708 O PRO A 102 5.002 11.305 34.680 1.00 17.47 O ANISOU 708 O PRO A 102 2170 2218 2250 53 752 -549 O ATOM 709 CB PRO A 102 5.661 13.896 36.232 1.00 17.91 C ANISOU 709 CB PRO A 102 2109 2436 2258 -165 470 -281 C ATOM 710 CG PRO A 102 4.329 14.171 36.860 1.00 20.03 C ANISOU 710 CG PRO A 102 2403 2852 2355 182 570 -408 C ATOM 711 CD PRO A 102 3.306 14.376 35.842 1.00 18.24 C ANISOU 711 CD PRO A 102 2050 2574 2302 153 656 -578 C ATOM 712 N ARG A 103 6.814 12.079 33.601 1.00 15.99 N ANISOU 712 N ARG A 103 1878 2103 2094 -47 584 -451 N ATOM 713 CA ARG A 103 7.375 10.745 33.317 1.00 15.78 C ANISOU 713 CA ARG A 103 1868 2082 2044 -36 404 -349 C ATOM 714 C ARG A 103 8.860 10.768 33.622 1.00 15.32 C ANISOU 714 C ARG A 103 1793 2057 1969 -150 402 -413 C ATOM 715 O ARG A 103 9.457 11.843 33.783 1.00 15.76 O ANISOU 715 O ARG A 103 1700 2159 2128 -220 439 -498 O ATOM 716 CB ARG A 103 7.150 10.343 31.895 1.00 15.53 C ANISOU 716 CB ARG A 103 1839 1958 2102 -3 270 -256 C ATOM 717 CG ARG A 103 5.724 10.229 31.465 1.00 17.14 C ANISOU 717 CG ARG A 103 1996 2232 2283 -80 330 -324 C ATOM 718 CD ARG A 103 5.010 9.073 32.102 1.00 18.79 C ANISOU 718 CD ARG A 103 2190 2253 2694 -207 8 -109 C ATOM 719 NE ARG A 103 3.648 8.950 31.571 1.00 21.35 N ANISOU 719 NE ARG A 103 2102 2694 3316 -275 212 -199 N ATOM 720 CZ ARG A 103 2.598 9.620 32.034 1.00 22.26 C ANISOU 720 CZ ARG A 103 2204 3031 3223 -237 -97 -105 C ATOM 721 NH1 ARG A 103 2.681 10.407 33.108 1.00 22.93 N ANISOU 721 NH1 ARG A 103 2148 2890 3670 -129 221 -100 N ATOM 722 NH2 ARG A 103 1.418 9.424 31.424 1.00 23.62 N ANISOU 722 NH2 ARG A 103 1834 3295 3842 -433 -377 -243 N ATOM 723 N ARG A 104 9.439 9.579 33.737 1.00 13.88 N ANISOU 723 N ARG A 104 1504 2111 1657 -143 325 -367 N ATOM 724 CA ARG A 104 10.875 9.431 33.839 1.00 15.51 C ANISOU 724 CA ARG A 104 1884 2139 1869 -36 305 -411 C ATOM 725 C ARG A 104 11.452 8.945 32.496 1.00 13.04 C ANISOU 725 C ARG A 104 1778 1677 1497 -61 313 -415 C ATOM 726 O ARG A 104 10.950 7.996 31.928 1.00 14.43 O ANISOU 726 O ARG A 104 1898 1761 1822 -235 494 -520 O ATOM 727 CB ARG A 104 11.259 8.426 34.910 1.00 17.07 C ANISOU 727 CB ARG A 104 1996 2449 2041 -60 222 -320 C ATOM 728 CG ARG A 104 10.682 8.838 36.296 1.00 22.81 C ANISOU 728 CG ARG A 104 3028 3190 2446 164 300 -300 C ATOM 729 CD ARG A 104 11.315 8.114 37.430 1.00 28.42 C ANISOU 729 CD ARG A 104 3633 3820 3343 -23 58 48 C ATOM 730 NE ARG A 104 10.553 8.277 38.670 1.00 32.92 N ANISOU 730 NE ARG A 104 4281 4616 3611 43 257 -110 N ATOM 731 CZ ARG A 104 10.386 9.426 39.333 1.00 37.24 C ANISOU 731 CZ ARG A 104 4829 4764 4554 -42 198 -164 C ATOM 732 NH1 ARG A 104 10.905 10.593 38.891 1.00 39.33 N ANISOU 732 NH1 ARG A 104 5057 5088 4797 -71 133 29 N ATOM 733 NH2 ARG A 104 9.671 9.418 40.462 1.00 39.15 N ANISOU 733 NH2 ARG A 104 5037 5232 4605 -126 239 -78 N ATOM 734 N TYR A 105 12.468 9.673 32.065 1.00 11.48 N ANISOU 734 N TYR A 105 1377 1601 1383 -52 289 -445 N ATOM 735 CA TYR A 105 13.073 9.455 30.772 1.00 11.42 C ANISOU 735 CA TYR A 105 1419 1542 1377 5 165 -303 C ATOM 736 C TYR A 105 14.511 9.019 30.914 1.00 11.08 C ANISOU 736 C TYR A 105 1396 1468 1346 -37 121 -307 C ATOM 737 O TYR A 105 15.280 9.722 31.519 1.00 13.05 O ANISOU 737 O TYR A 105 1476 1722 1758 -1 143 -677 O ATOM 738 CB TYR A 105 13.036 10.739 29.920 1.00 11.46 C ANISOU 738 CB TYR A 105 1521 1445 1386 -23 136 -194 C ATOM 739 CG TYR A 105 11.644 11.236 29.634 1.00 10.72 C ANISOU 739 CG TYR A 105 1466 1222 1384 76 64 -108 C ATOM 740 CD1 TYR A 105 10.953 12.027 30.573 1.00 12.16 C ANISOU 740 CD1 TYR A 105 1762 1327 1529 -50 56 -327 C ATOM 741 CD2 TYR A 105 10.995 10.894 28.476 1.00 12.50 C ANISOU 741 CD2 TYR A 105 1360 1743 1644 -186 225 -39 C ATOM 742 CE1 TYR A 105 9.679 12.477 30.330 1.00 12.57 C ANISOU 742 CE1 TYR A 105 1686 1250 1840 -115 46 -458 C ATOM 743 CE2 TYR A 105 9.674 11.328 28.277 1.00 12.80 C ANISOU 743 CE2 TYR A 105 1692 1595 1577 -152 182 -269 C ATOM 744 CZ TYR A 105 9.028 12.114 29.213 1.00 11.42 C ANISOU 744 CZ TYR A 105 1208 1356 1775 30 113 -256 C ATOM 745 OH TYR A 105 7.725 12.484 29.035 1.00 12.43 O ANISOU 745 OH TYR A 105 1532 1230 1961 138 118 -231 O ATOM 746 N THR A 106 14.873 7.902 30.261 1.00 11.14 N ANISOU 746 N THR A 106 1255 1514 1462 52 272 -363 N ATOM 747 CA THR A 106 16.259 7.524 30.056 1.00 10.97 C ANISOU 747 CA THR A 106 1293 1595 1277 91 69 -257 C ATOM 748 C THR A 106 16.524 7.629 28.569 1.00 10.95 C ANISOU 748 C THR A 106 1260 1562 1336 163 85 -305 C ATOM 749 O THR A 106 15.875 6.981 27.775 1.00 12.00 O ANISOU 749 O THR A 106 1515 1779 1263 -151 291 -455 O ATOM 750 CB THR A 106 16.536 6.115 30.566 1.00 12.71 C ANISOU 750 CB THR A 106 1640 1715 1474 143 113 -242 C ATOM 751 OG1 THR A 106 16.290 6.103 31.965 1.00 16.91 O ANISOU 751 OG1 THR A 106 2664 2359 1401 -220 58 22 O ATOM 752 CG2 THR A 106 17.984 5.723 30.278 1.00 14.77 C ANISOU 752 CG2 THR A 106 1693 1919 1998 315 195 -124 C ATOM 753 N ILE A 107 17.525 8.445 28.237 1.00 10.65 N ANISOU 753 N ILE A 107 1304 1711 1030 -19 177 -437 N ATOM 754 CA ILE A 107 18.019 8.564 26.874 1.00 11.01 C ANISOU 754 CA ILE A 107 1289 1834 1060 57 -32 -285 C ATOM 755 C ILE A 107 19.316 7.788 26.807 1.00 11.47 C ANISOU 755 C ILE A 107 1440 1845 1073 68 34 -164 C ATOM 756 O ILE A 107 20.273 8.142 27.459 1.00 12.40 O ANISOU 756 O ILE A 107 1395 1960 1354 172 -97 -330 O ATOM 757 CB ILE A 107 18.224 10.049 26.455 1.00 12.65 C ANISOU 757 CB ILE A 107 1601 1832 1370 19 -104 -304 C ATOM 758 CG1 ILE A 107 16.938 10.873 26.677 1.00 15.22 C ANISOU 758 CG1 ILE A 107 2006 1908 1869 70 30 -381 C ATOM 759 CG2 ILE A 107 18.796 10.142 25.024 1.00 15.10 C ANISOU 759 CG2 ILE A 107 1842 2575 1318 -209 14 -185 C ATOM 760 CD1 ILE A 107 15.704 10.381 25.906 1.00 16.74 C ANISOU 760 CD1 ILE A 107 2003 2121 2235 51 -389 -15 C ATOM 761 N ALA A 108 19.297 6.676 26.087 1.00 11.31 N ANISOU 761 N ALA A 108 1286 1911 1098 138 4 -173 N ATOM 762 CA ALA A 108 20.443 5.827 25.911 1.00 12.44 C ANISOU 762 CA ALA A 108 1513 2057 1154 290 85 -224 C ATOM 763 C ALA A 108 21.028 6.058 24.503 1.00 13.00 C ANISOU 763 C ALA A 108 1657 2040 1240 270 -34 -148 C ATOM 764 O ALA A 108 20.294 6.318 23.536 1.00 14.07 O ANISOU 764 O ALA A 108 1626 2526 1192 339 -157 -17 O ATOM 765 CB ALA A 108 20.020 4.356 26.071 1.00 15.05 C ANISOU 765 CB ALA A 108 1999 2107 1609 398 132 -347 C ATOM 766 N ALA A 109 22.340 5.945 24.416 1.00 11.32 N ANISOU 766 N ALA A 109 1443 1756 1100 463 -38 -196 N ATOM 767 CA ALA A 109 23.025 6.100 23.115 1.00 10.11 C ANISOU 767 CA ALA A 109 1295 1533 1011 440 53 -214 C ATOM 768 C ALA A 109 24.163 5.111 23.086 1.00 10.13 C ANISOU 768 C ALA A 109 1236 1603 1008 349 -36 -59 C ATOM 769 O ALA A 109 24.842 4.853 24.092 1.00 11.94 O ANISOU 769 O ALA A 109 1445 2057 1034 708 -116 -134 O ATOM 770 CB ALA A 109 23.517 7.469 22.949 1.00 12.28 C ANISOU 770 CB ALA A 109 1312 1802 1551 207 -18 -39 C ATOM 771 N LEU A 110 24.367 4.556 21.906 1.00 9.96 N ANISOU 771 N LEU A 110 1508 1420 855 399 43 43 N ATOM 772 CA LEU A 110 25.453 3.626 21.598 1.00 10.00 C ANISOU 772 CA LEU A 110 1476 1444 879 352 173 20 C ATOM 773 C LEU A 110 26.304 4.197 20.507 1.00 9.66 C ANISOU 773 C LEU A 110 1381 1374 914 291 226 98 C ATOM 774 O LEU A 110 25.775 4.491 19.463 1.00 10.67 O ANISOU 774 O LEU A 110 1406 1863 784 379 -41 260 O ATOM 775 CB LEU A 110 24.833 2.314 21.159 1.00 11.62 C ANISOU 775 CB LEU A 110 1592 1658 1162 271 107 0 C ATOM 776 CG LEU A 110 25.794 1.262 20.706 1.00 12.13 C ANISOU 776 CG LEU A 110 1758 1450 1400 303 346 -109 C ATOM 777 CD1 LEU A 110 26.641 0.747 21.849 1.00 12.73 C ANISOU 777 CD1 LEU A 110 1678 1380 1780 297 142 10 C ATOM 778 CD2 LEU A 110 25.028 0.062 20.087 1.00 15.95 C ANISOU 778 CD2 LEU A 110 2247 2096 1715 145 24 -325 C ATOM 779 N LEU A 111 27.566 4.414 20.758 1.00 9.45 N ANISOU 779 N LEU A 111 1332 1334 922 512 46 324 N ATOM 780 CA LEU A 111 28.441 5.176 19.842 1.00 9.76 C ANISOU 780 CA LEU A 111 1365 1445 896 483 172 188 C ATOM 781 C LEU A 111 29.492 4.348 19.099 1.00 10.72 C ANISOU 781 C LEU A 111 1579 1604 887 469 216 113 C ATOM 782 O LEU A 111 30.201 3.562 19.763 1.00 10.78 O ANISOU 782 O LEU A 111 1529 1637 929 611 170 252 O ATOM 783 CB LEU A 111 29.199 6.226 20.638 1.00 10.35 C ANISOU 783 CB LEU A 111 1525 1410 995 325 81 367 C ATOM 784 CG LEU A 111 28.372 7.211 21.479 1.00 10.84 C ANISOU 784 CG LEU A 111 1526 1558 1034 245 213 183 C ATOM 785 CD1 LEU A 111 29.330 8.265 22.097 1.00 12.77 C ANISOU 785 CD1 LEU A 111 1493 1779 1581 216 -154 -161 C ATOM 786 CD2 LEU A 111 27.211 7.805 20.747 1.00 11.59 C ANISOU 786 CD2 LEU A 111 1376 1616 1411 456 32 36 C ATOM 787 N SER A 112 29.633 4.621 17.833 1.00 11.88 N ANISOU 787 N SER A 112 1602 1731 1180 604 274 276 N ATOM 788 CA SER A 112 30.729 4.209 17.020 1.00 11.24 C ANISOU 788 CA SER A 112 1772 1492 1004 483 291 201 C ATOM 789 C SER A 112 31.214 5.424 16.222 1.00 11.28 C ANISOU 789 C SER A 112 1720 1527 1035 511 486 248 C ATOM 790 O SER A 112 30.479 6.386 16.101 1.00 11.11 O ANISOU 790 O SER A 112 1822 1280 1118 547 444 133 O ATOM 791 CB SER A 112 30.292 3.140 16.032 1.00 11.43 C ANISOU 791 CB SER A 112 1889 1359 1093 444 302 167 C ATOM 792 OG SER A 112 29.825 1.977 16.720 1.00 13.64 O ANISOU 792 OG SER A 112 2339 1480 1363 431 472 140 O ATOM 793 N PRO A 113 32.444 5.384 15.706 1.00 13.01 N ANISOU 793 N PRO A 113 1927 1679 1337 626 408 235 N ATOM 794 CA PRO A 113 32.919 6.599 15.050 1.00 12.32 C ANISOU 794 CA PRO A 113 1767 1764 1149 439 259 421 C ATOM 795 C PRO A 113 32.060 7.113 13.871 1.00 12.23 C ANISOU 795 C PRO A 113 1755 1668 1223 517 416 365 C ATOM 796 O PRO A 113 31.985 8.337 13.717 1.00 14.18 O ANISOU 796 O PRO A 113 2207 1644 1535 540 412 176 O ATOM 797 CB PRO A 113 34.335 6.218 14.574 1.00 13.87 C ANISOU 797 CB PRO A 113 1855 2010 1405 416 389 583 C ATOM 798 CG PRO A 113 34.774 5.252 15.707 1.00 15.35 C ANISOU 798 CG PRO A 113 1864 2401 1566 667 268 585 C ATOM 799 CD PRO A 113 33.536 4.434 15.968 1.00 13.27 C ANISOU 799 CD PRO A 113 1835 1821 1383 719 284 301 C ATOM 800 N TYR A 114 31.434 6.209 13.116 1.00 10.81 N ANISOU 800 N TYR A 114 1517 1519 1071 488 329 319 N ATOM 801 CA TYR A 114 30.600 6.622 11.949 1.00 11.85 C ANISOU 801 CA TYR A 114 1836 1515 1150 520 232 120 C ATOM 802 C TYR A 114 29.129 6.250 12.096 1.00 12.47 C ANISOU 802 C TYR A 114 1867 1552 1319 483 132 240 C ATOM 803 O TYR A 114 28.359 6.298 11.136 1.00 12.17 O ANISOU 803 O TYR A 114 1817 1755 1050 594 272 216 O ATOM 804 CB TYR A 114 31.150 6.057 10.629 1.00 13.03 C ANISOU 804 CB TYR A 114 1887 1726 1337 418 316 176 C ATOM 805 CG TYR A 114 32.333 6.859 10.097 1.00 11.91 C ANISOU 805 CG TYR A 114 1853 1655 1015 388 287 190 C ATOM 806 CD1 TYR A 114 33.556 6.791 10.702 1.00 16.76 C ANISOU 806 CD1 TYR A 114 2177 2769 1422 -3 161 199 C ATOM 807 CD2 TYR A 114 32.231 7.648 8.947 1.00 13.48 C ANISOU 807 CD2 TYR A 114 2348 1372 1400 330 377 194 C ATOM 808 CE1 TYR A 114 34.653 7.513 10.196 1.00 18.81 C ANISOU 808 CE1 TYR A 114 2263 3255 1629 -97 92 435 C ATOM 809 CE2 TYR A 114 33.334 8.322 8.452 1.00 15.31 C ANISOU 809 CE2 TYR A 114 2221 2125 1470 159 567 130 C ATOM 810 CZ TYR A 114 34.525 8.263 9.067 1.00 18.00 C ANISOU 810 CZ TYR A 114 2482 2384 1972 -271 282 93 C ATOM 811 OH TYR A 114 35.649 8.917 8.613 1.00 23.67 O ANISOU 811 OH TYR A 114 2924 3814 2253 -214 297 130 O ATOM 812 N SER A 115 28.699 5.976 13.329 1.00 12.04 N ANISOU 812 N SER A 115 1786 1577 1208 416 213 260 N ATOM 813 CA SER A 115 27.319 5.512 13.527 1.00 11.67 C ANISOU 813 CA SER A 115 1835 1531 1066 312 124 359 C ATOM 814 C SER A 115 26.936 5.672 15.007 1.00 11.29 C ANISOU 814 C SER A 115 1613 1645 1033 434 104 306 C ATOM 815 O SER A 115 27.776 5.479 15.889 1.00 13.30 O ANISOU 815 O SER A 115 1756 2220 1076 605 261 506 O ATOM 816 CB SER A 115 27.198 4.064 13.111 1.00 13.44 C ANISOU 816 CB SER A 115 2250 1567 1288 316 58 504 C ATOM 817 OG SER A 115 25.884 3.558 13.265 1.00 15.57 O ANISOU 817 OG SER A 115 2724 1596 1594 310 160 462 O ATOM 818 N TYR A 116 25.663 5.966 15.258 1.00 10.14 N ANISOU 818 N TYR A 116 1358 1602 889 203 203 349 N ATOM 819 CA TYR A 116 25.149 5.876 16.631 1.00 10.33 C ANISOU 819 CA TYR A 116 1565 1419 941 67 53 208 C ATOM 820 C TYR A 116 23.697 5.460 16.608 1.00 10.66 C ANISOU 820 C TYR A 116 1543 1493 1011 150 184 124 C ATOM 821 O TYR A 116 23.007 5.670 15.611 1.00 10.54 O ANISOU 821 O TYR A 116 1529 1638 836 130 73 71 O ATOM 822 CB TYR A 116 25.393 7.157 17.398 1.00 11.89 C ANISOU 822 CB TYR A 116 1812 1708 995 27 -59 126 C ATOM 823 CG TYR A 116 24.655 8.344 16.895 1.00 11.49 C ANISOU 823 CG TYR A 116 1914 1305 1146 -53 12 -7 C ATOM 824 CD1 TYR A 116 23.332 8.596 17.252 1.00 11.33 C ANISOU 824 CD1 TYR A 116 1813 1322 1168 115 -141 193 C ATOM 825 CD2 TYR A 116 25.258 9.191 15.994 1.00 12.03 C ANISOU 825 CD2 TYR A 116 1818 1474 1278 -172 9 65 C ATOM 826 CE1 TYR A 116 22.632 9.690 16.704 1.00 12.56 C ANISOU 826 CE1 TYR A 116 1892 1628 1249 -65 -16 8 C ATOM 827 CE2 TYR A 116 24.609 10.280 15.504 1.00 13.43 C ANISOU 827 CE2 TYR A 116 2019 1583 1499 -160 -34 128 C ATOM 828 CZ TYR A 116 23.308 10.530 15.822 1.00 11.16 C ANISOU 828 CZ TYR A 116 1814 1192 1233 88 -114 51 C ATOM 829 OH TYR A 116 22.648 11.608 15.296 1.00 14.80 O ANISOU 829 OH TYR A 116 2280 1535 1808 -180 -140 600 O ATOM 830 N SER A 117 23.265 4.933 17.733 1.00 10.01 N ANISOU 830 N SER A 117 1501 1534 766 222 -18 65 N ATOM 831 CA ASER A 117 21.916 4.557 17.999 0.50 10.74 C ANISOU 831 CA ASER A 117 1521 1598 959 66 -22 107 C ATOM 832 C SER A 117 21.464 5.315 19.240 1.00 10.79 C ANISOU 832 C SER A 117 1404 1653 1039 63 -42 166 C ATOM 833 O SER A 117 22.267 5.473 20.156 1.00 12.50 O ANISOU 833 O SER A 117 1587 2110 1050 262 -20 -251 O ATOM 834 CB ASER A 117 21.926 3.051 18.285 0.50 11.32 C ANISOU 834 CB ASER A 117 1630 1606 1062 40 42 -25 C ATOM 835 OG ASER A 117 20.640 2.552 18.520 0.50 14.67 O ANISOU 835 OG ASER A 117 2038 2179 1354 -249 198 -23 O ATOM 836 N THR A 118 20.197 5.648 19.324 1.00 10.14 N ANISOU 836 N THR A 118 1134 1628 1089 30 10 -106 N ATOM 837 CA THR A 118 19.641 6.153 20.545 1.00 11.24 C ANISOU 837 CA THR A 118 1348 1773 1148 122 -30 -81 C ATOM 838 C THR A 118 18.275 5.557 20.759 1.00 11.37 C ANISOU 838 C THR A 118 1322 1898 1099 136 -24 -150 C ATOM 839 O THR A 118 17.491 5.385 19.812 1.00 13.40 O ANISOU 839 O THR A 118 1500 2459 1132 -87 24 -117 O ATOM 840 CB THR A 118 19.627 7.687 20.523 1.00 13.16 C ANISOU 840 CB THR A 118 1673 1934 1393 135 -33 -111 C ATOM 841 OG1 THR A 118 19.181 8.204 21.752 1.00 14.00 O ANISOU 841 OG1 THR A 118 1775 2089 1455 283 -42 -301 O ATOM 842 CG2 THR A 118 18.694 8.270 19.452 1.00 13.49 C ANISOU 842 CG2 THR A 118 1644 1760 1718 271 -353 12 C ATOM 843 N THR A 119 17.962 5.287 22.027 1.00 11.14 N ANISOU 843 N THR A 119 1350 1804 1076 99 108 -315 N ATOM 844 CA THR A 119 16.664 4.769 22.405 1.00 11.47 C ANISOU 844 CA THR A 119 1485 1663 1209 91 281 -223 C ATOM 845 C THR A 119 16.192 5.486 23.633 1.00 11.57 C ANISOU 845 C THR A 119 1533 1527 1336 32 125 -128 C ATOM 846 O THR A 119 16.992 5.930 24.450 1.00 13.19 O ANISOU 846 O THR A 119 1414 2110 1486 -71 26 -599 O ATOM 847 CB THR A 119 16.721 3.281 22.712 1.00 14.40 C ANISOU 847 CB THR A 119 2010 1775 1685 204 446 -492 C ATOM 848 OG1 THR A 119 17.440 2.640 21.677 1.00 18.62 O ANISOU 848 OG1 THR A 119 2983 2304 1788 279 267 -359 O ATOM 849 CG2 THR A 119 15.290 2.704 22.747 1.00 15.13 C ANISOU 849 CG2 THR A 119 2233 1335 2181 -8 525 -414 C ATOM 850 N ALA A 120 14.897 5.645 23.746 1.00 10.42 N ANISOU 850 N ALA A 120 1260 1645 1053 7 191 -337 N ATOM 851 CA ALA A 120 14.269 6.231 24.959 1.00 10.91 C ANISOU 851 CA ALA A 120 1395 1444 1307 -24 348 -365 C ATOM 852 C ALA A 120 13.542 5.145 25.720 1.00 10.14 C ANISOU 852 C ALA A 120 1115 1592 1142 -74 333 -372 C ATOM 853 O ALA A 120 12.842 4.322 25.131 1.00 12.91 O ANISOU 853 O ALA A 120 1427 1970 1507 -312 249 -486 O ATOM 854 CB ALA A 120 13.332 7.336 24.589 1.00 13.34 C ANISOU 854 CB ALA A 120 1616 1595 1857 -45 157 -200 C ATOM 855 N VAL A 121 13.723 5.156 27.027 1.00 10.75 N ANISOU 855 N VAL A 121 1478 1392 1212 -60 162 -200 N ATOM 856 CA VAL A 121 12.918 4.341 27.912 1.00 11.98 C ANISOU 856 CA VAL A 121 1631 1542 1379 -87 276 -300 C ATOM 857 C VAL A 121 12.144 5.336 28.769 1.00 11.57 C ANISOU 857 C VAL A 121 1610 1549 1236 -164 306 -253 C ATOM 858 O VAL A 121 12.750 6.132 29.505 1.00 13.13 O ANISOU 858 O VAL A 121 1711 1775 1502 -270 192 -508 O ATOM 859 CB VAL A 121 13.774 3.387 28.801 1.00 13.84 C ANISOU 859 CB VAL A 121 1822 1829 1607 -103 211 -243 C ATOM 860 CG1 VAL A 121 12.864 2.612 29.784 1.00 18.27 C ANISOU 860 CG1 VAL A 121 2525 2410 2006 -451 -123 118 C ATOM 861 CG2 VAL A 121 14.594 2.448 27.925 1.00 18.15 C ANISOU 861 CG2 VAL A 121 2476 2136 2282 510 202 -350 C ATOM 862 N VAL A 122 10.821 5.251 28.686 1.00 11.82 N ANISOU 862 N VAL A 122 1657 1502 1333 -132 201 -391 N ATOM 863 CA VAL A 122 9.936 6.184 29.354 1.00 12.39 C ANISOU 863 CA VAL A 122 1624 1577 1504 -112 329 -336 C ATOM 864 C VAL A 122 9.079 5.378 30.325 1.00 13.37 C ANISOU 864 C VAL A 122 1741 1652 1687 -196 347 -366 C ATOM 865 O VAL A 122 8.417 4.426 29.936 1.00 14.25 O ANISOU 865 O VAL A 122 1756 1744 1912 -170 475 -312 O ATOM 866 CB VAL A 122 9.034 6.908 28.338 1.00 12.48 C ANISOU 866 CB VAL A 122 1741 1446 1554 -77 355 -430 C ATOM 867 CG1 VAL A 122 8.150 7.953 29.041 1.00 14.99 C ANISOU 867 CG1 VAL A 122 2198 1520 1978 331 389 -274 C ATOM 868 CG2 VAL A 122 9.866 7.526 27.281 1.00 15.17 C ANISOU 868 CG2 VAL A 122 2602 1532 1630 -127 326 -21 C ATOM 869 N THR A 123 9.115 5.786 31.592 1.00 14.44 N ANISOU 869 N THR A 123 1785 1934 1768 -307 471 -133 N ATOM 870 CA THR A 123 8.360 5.078 32.645 1.00 16.61 C ANISOU 870 CA THR A 123 2073 2205 2031 -161 418 -59 C ATOM 871 C THR A 123 7.480 6.055 33.396 1.00 16.78 C ANISOU 871 C THR A 123 2142 2058 2174 -153 489 -143 C ATOM 872 O THR A 123 7.766 7.239 33.502 1.00 16.26 O ANISOU 872 O THR A 123 1822 2308 2047 -393 673 -338 O ATOM 873 CB THR A 123 9.267 4.325 33.603 1.00 20.05 C ANISOU 873 CB THR A 123 2470 2670 2475 -31 354 53 C ATOM 874 OG1 THR A 123 9.958 5.223 34.418 1.00 25.64 O ANISOU 874 OG1 THR A 123 3356 3545 2838 -11 -117 93 O ATOM 875 CG2 THR A 123 10.304 3.545 32.864 1.00 21.04 C ANISOU 875 CG2 THR A 123 2489 2935 2567 400 198 215 C ATOM 876 N ASN A 124 6.372 5.530 33.904 1.00 21.09 N ANISOU 876 N ASN A 124 2566 2551 2895 -105 554 -98 N ATOM 877 CA ASN A 124 5.438 6.362 34.667 1.00 23.15 C ANISOU 877 CA ASN A 124 2945 2832 3016 -44 444 -134 C ATOM 878 C ASN A 124 5.630 6.034 36.104 1.00 26.48 C ANISOU 878 C ASN A 124 3380 3247 3434 23 344 -86 C ATOM 879 O ASN A 124 5.308 4.929 36.512 1.00 27.38 O ANISOU 879 O ASN A 124 3520 3367 3515 -60 514 -3 O ATOM 880 CB ASN A 124 3.987 6.069 34.251 1.00 23.55 C ANISOU 880 CB ASN A 124 2938 2874 3136 -8 423 -154 C ATOM 881 CG ASN A 124 3.009 7.042 34.849 1.00 24.52 C ANISOU 881 CG ASN A 124 2891 3114 3310 -130 540 -42 C ATOM 882 OD1 ASN A 124 3.323 7.701 35.830 1.00 25.79 O ANISOU 882 OD1 ASN A 124 2941 3614 3245 -172 1181 -65 O ATOM 883 ND2 ASN A 124 1.850 7.175 34.240 1.00 27.99 N ANISOU 883 ND2 ASN A 124 3441 3601 3590 -11 290 -4 N ATOM 884 N PRO A 125 6.057 7.023 36.897 1.00 29.88 N ANISOU 884 N PRO A 125 3913 3795 3644 -88 156 -53 N ATOM 885 CA PRO A 125 6.358 6.771 38.314 1.00 31.09 C ANISOU 885 CA PRO A 125 4011 3994 3808 0 146 15 C ATOM 886 C PRO A 125 5.106 6.477 39.109 1.00 33.90 C ANISOU 886 C PRO A 125 4316 4418 4143 62 160 74 C ATOM 887 O PRO A 125 5.210 5.843 40.152 1.00 35.88 O ANISOU 887 O PRO A 125 4561 4737 4335 133 128 254 O ATOM 888 CB PRO A 125 7.001 8.079 38.784 1.00 31.73 C ANISOU 888 CB PRO A 125 4165 4031 3857 -4 52 -41 C ATOM 889 CG PRO A 125 6.630 9.128 37.783 1.00 31.68 C ANISOU 889 CG PRO A 125 4142 4084 3809 -59 104 -23 C ATOM 890 CD PRO A 125 6.227 8.443 36.514 1.00 30.35 C ANISOU 890 CD PRO A 125 3989 3843 3700 -86 192 -9 C TER 891 PRO A 125 ATOM 983 N PRO A 11 26.646 13.585 -4.627 1.00 19.51 N ANISOU 983 N PRO B 11 2223 2738 2450 124 488 420 N ATOM 984 CA PRO A 11 27.580 13.413 -3.523 1.00 19.02 C ANISOU 984 CA PRO B 11 2359 2607 2258 2 249 323 C ATOM 985 C PRO A 11 26.881 13.082 -2.178 1.00 17.91 C ANISOU 985 C PRO B 11 2290 2504 2008 20 153 619 C ATOM 986 O PRO A 11 27.569 12.755 -1.228 1.00 18.25 O ANISOU 986 O PRO B 11 2145 2629 2157 49 15 722 O ATOM 987 CB PRO A 11 28.234 14.801 -3.375 1.00 21.03 C ANISOU 987 CB PRO B 11 2514 2965 2511 -54 251 334 C ATOM 988 CG PRO A 11 27.299 15.704 -3.915 1.00 22.16 C ANISOU 988 CG PRO B 11 2701 2795 2924 -29 226 371 C ATOM 989 CD PRO A 11 26.563 14.996 -5.018 1.00 21.32 C ANISOU 989 CD PRO B 11 2770 2752 2575 74 231 442 C ATOM 990 N LEU A 12 25.563 13.254 -2.095 1.00 16.39 N ANISOU 990 N LEU B 12 2258 2285 1683 12 162 627 N ATOM 991 CA LEU A 12 24.791 13.072 -0.844 1.00 16.62 C ANISOU 991 CA LEU B 12 2257 2229 1827 -26 171 394 C ATOM 992 C LEU A 12 23.512 12.333 -1.130 1.00 17.31 C ANISOU 992 C LEU B 12 2352 2410 1814 -71 46 426 C ATOM 993 O LEU A 12 22.727 12.770 -1.975 1.00 19.30 O ANISOU 993 O LEU B 12 2572 2773 1987 -4 -154 813 O ATOM 994 CB LEU A 12 24.452 14.419 -0.217 1.00 17.00 C ANISOU 994 CB LEU B 12 2209 2345 1902 -6 215 404 C ATOM 995 CG LEU A 12 23.668 14.392 1.095 1.00 16.94 C ANISOU 995 CG LEU B 12 2302 2243 1890 53 179 382 C ATOM 996 CD1 LEU A 12 24.497 13.710 2.176 1.00 16.97 C ANISOU 996 CD1 LEU B 12 2516 2340 1592 287 -37 213 C ATOM 997 CD2 LEU A 12 23.266 15.846 1.508 1.00 18.31 C ANISOU 997 CD2 LEU B 12 2497 2073 2385 121 213 238 C ATOM 998 N MET A 13 23.312 11.202 -0.436 1.00 15.76 N ANISOU 998 N MET B 13 2309 2269 1408 0 174 366 N ATOM 999 CA AMET A 13 22.135 10.366 -0.550 0.50 15.40 C ANISOU 999 CA AMET B 13 2199 2189 1460 -14 85 267 C ATOM 1000 C MET A 13 21.623 10.120 0.874 1.00 13.93 C ANISOU 1000 C MET B 13 1944 2042 1303 13 119 237 C ATOM 1001 O MET A 13 22.439 9.946 1.776 1.00 14.76 O ANISOU 1001 O MET B 13 2032 2299 1274 156 139 382 O ATOM 1002 CB AMET A 13 22.508 9.010 -1.183 0.50 15.29 C ANISOU 1002 CB AMET B 13 2199 2270 1339 -60 162 191 C ATOM 1003 CG AMET A 13 21.282 8.206 -1.675 0.50 17.29 C ANISOU 1003 CG AMET B 13 2453 2223 1894 3 176 133 C ATOM 1004 SD AMET A 13 20.532 7.067 -0.492 0.50 17.20 S ANISOU 1004 SD AMET B 13 2337 2381 1814 -188 154 134 S ATOM 1005 CE AMET A 13 21.247 5.525 -1.022 0.50 19.02 C ANISOU 1005 CE AMET B 13 2388 2435 2400 0 -4 -121 C ATOM 1006 N VAL A 14 20.322 10.087 1.056 1.00 12.52 N ANISOU 1006 N VAL B 14 1851 1955 948 -31 55 127 N ATOM 1007 CA VAL A 14 19.737 9.751 2.359 1.00 12.71 C ANISOU 1007 CA VAL B 14 1829 1945 1055 15 4 259 C ATOM 1008 C VAL A 14 18.838 8.543 2.159 1.00 14.65 C ANISOU 1008 C VAL B 14 2097 2169 1300 -118 -163 111 C ATOM 1009 O VAL A 14 18.053 8.480 1.212 1.00 15.89 O ANISOU 1009 O VAL B 14 2229 2481 1326 -324 -293 434 O ATOM 1010 CB VAL A 14 18.909 10.944 2.950 1.00 12.99 C ANISOU 1010 CB VAL B 14 1804 1935 1195 232 -39 159 C ATOM 1011 CG1 VAL A 14 18.210 10.567 4.256 1.00 14.46 C ANISOU 1011 CG1 VAL B 14 2103 2106 1285 215 169 101 C ATOM 1012 CG2 VAL A 14 19.804 12.150 3.092 1.00 14.01 C ANISOU 1012 CG2 VAL B 14 2128 1749 1445 130 -50 166 C ATOM 1013 N LYS A 15 18.955 7.574 3.046 1.00 13.18 N ANISOU 1013 N LYS B 15 1927 2038 1041 -25 -180 238 N ATOM 1014 CA LYS A 15 18.235 6.325 2.980 1.00 14.34 C ANISOU 1014 CA LYS B 15 2026 2127 1294 -60 -49 114 C ATOM 1015 C LYS A 15 17.575 6.071 4.302 1.00 12.53 C ANISOU 1015 C LYS B 15 1774 1829 1157 -254 5 144 C ATOM 1016 O LYS A 15 18.255 6.176 5.337 1.00 13.15 O ANISOU 1016 O LYS B 15 1730 2318 948 -212 -147 119 O ATOM 1017 CB LYS A 15 19.149 5.124 2.641 1.00 16.26 C ANISOU 1017 CB LYS B 15 2420 2258 1498 -95 126 131 C ATOM 1018 CG LYS A 15 18.344 3.810 2.528 1.00 19.48 C ANISOU 1018 CG LYS B 15 2702 2499 2199 -66 27 -3 C ATOM 1019 CD LYS A 15 18.998 2.690 1.682 1.00 23.37 C ANISOU 1019 CD LYS B 15 3137 2900 2840 -41 178 -50 C ATOM 1020 CE LYS A 15 18.000 1.548 1.329 1.00 24.60 C ANISOU 1020 CE LYS B 15 3221 3089 3037 13 -25 -171 C ATOM 1021 NZ LYS A 15 17.010 1.701 0.158 1.00 29.61 N ANISOU 1021 NZ LYS B 15 3671 3848 3730 95 -259 123 N ATOM 1022 N VAL A 16 16.296 5.741 4.314 1.00 11.86 N ANISOU 1022 N VAL B 16 1807 1755 943 -194 -82 56 N ATOM 1023 CA VAL A 16 15.528 5.566 5.564 1.00 12.09 C ANISOU 1023 CA VAL B 16 1824 1715 1051 -128 -34 -10 C ATOM 1024 C VAL A 16 14.790 4.245 5.555 1.00 11.85 C ANISOU 1024 C VAL B 16 1911 1485 1103 -85 -127 -28 C ATOM 1025 O VAL A 16 14.055 3.916 4.579 1.00 12.80 O ANISOU 1025 O VAL B 16 2031 1852 980 -189 -236 -64 O ATOM 1026 CB VAL A 16 14.530 6.740 5.829 1.00 13.25 C ANISOU 1026 CB VAL B 16 1959 1840 1233 -101 -1 9 C ATOM 1027 CG1 VAL A 16 13.940 6.693 7.248 1.00 12.98 C ANISOU 1027 CG1 VAL B 16 1846 2103 981 -12 237 -58 C ATOM 1028 CG2 VAL A 16 15.209 8.115 5.597 1.00 13.50 C ANISOU 1028 CG2 VAL B 16 1849 1834 1443 -256 92 63 C ATOM 1029 N LEU A 17 14.941 3.474 6.630 1.00 11.22 N ANISOU 1029 N LEU B 17 1536 1638 1085 -34 -100 16 N ATOM 1030 CA LEU A 17 14.324 2.192 6.767 1.00 10.78 C ANISOU 1030 CA LEU B 17 1524 1475 1095 31 0 -182 C ATOM 1031 C LEU A 17 13.427 2.136 8.001 1.00 10.50 C ANISOU 1031 C LEU B 17 1377 1485 1125 95 -143 3 C ATOM 1032 O LEU A 17 13.678 2.858 8.974 1.00 11.50 O ANISOU 1032 O LEU B 17 1626 1596 1145 -151 -129 -125 O ATOM 1033 CB LEU A 17 15.379 1.108 6.884 1.00 12.45 C ANISOU 1033 CB LEU B 17 1725 1577 1427 -61 165 -45 C ATOM 1034 CG LEU A 17 16.310 0.871 5.677 1.00 13.61 C ANISOU 1034 CG LEU B 17 1767 1870 1531 -29 339 -261 C ATOM 1035 CD1 LEU A 17 17.301 -0.223 5.997 1.00 17.10 C ANISOU 1035 CD1 LEU B 17 2164 2355 1977 322 301 -396 C ATOM 1036 CD2 LEU A 17 15.548 0.531 4.392 1.00 17.18 C ANISOU 1036 CD2 LEU B 17 2193 2711 1620 185 247 -703 C ATOM 1037 N ASP A 18 12.430 1.256 7.951 1.00 10.55 N ANISOU 1037 N ASP B 18 1470 1445 1091 -1 -80 -101 N ATOM 1038 CA ASP A 18 11.431 1.085 9.009 1.00 10.40 C ANISOU 1038 CA ASP B 18 1417 1307 1225 9 -58 -220 C ATOM 1039 C ASP A 18 11.650 -0.287 9.644 1.00 9.63 C ANISOU 1039 C ASP B 18 1310 1296 1052 -12 -95 -94 C ATOM 1040 O ASP A 18 11.516 -1.333 9.001 1.00 10.39 O ANISOU 1040 O ASP B 18 1554 1301 1093 -58 -210 -178 O ATOM 1041 CB ASP A 18 10.057 1.224 8.383 1.00 10.57 C ANISOU 1041 CB ASP B 18 1468 1264 1282 23 -154 -195 C ATOM 1042 CG ASP A 18 8.891 0.918 9.302 1.00 12.24 C ANISOU 1042 CG ASP B 18 1645 1474 1531 61 -102 -209 C ATOM 1043 OD1 ASP A 18 9.037 0.168 10.281 1.00 11.90 O ANISOU 1043 OD1 ASP B 18 1498 1591 1432 -19 159 -126 O ATOM 1044 OD2 ASP A 18 7.797 1.455 8.972 1.00 15.26 O ANISOU 1044 OD2 ASP B 18 1551 2153 2093 197 -164 173 O ATOM 1045 N ALA A 19 12.099 -0.260 10.904 1.00 10.01 N ANISOU 1045 N ALA B 19 1631 1226 945 71 -67 -223 N ATOM 1046 CA ALA A 19 12.445 -1.441 11.676 1.00 10.10 C ANISOU 1046 CA ALA B 19 1520 1236 1079 157 -64 -287 C ATOM 1047 C ALA A 19 11.255 -2.217 12.219 1.00 11.36 C ANISOU 1047 C ALA B 19 1825 1322 1168 -39 -219 -220 C ATOM 1048 O ALA A 19 11.425 -3.343 12.689 1.00 12.16 O ANISOU 1048 O ALA B 19 1942 1410 1268 -77 -342 -161 O ATOM 1049 CB ALA A 19 13.324 -1.030 12.818 1.00 11.00 C ANISOU 1049 CB ALA B 19 1599 1598 981 37 -207 -221 C ATOM 1050 N VAL A 20 10.060 -1.619 12.178 1.00 11.61 N ANISOU 1050 N VAL B 20 1703 1380 1327 -122 37 -149 N ATOM 1051 CA VAL A 20 8.823 -2.221 12.641 1.00 12.77 C ANISOU 1051 CA VAL B 20 1717 1580 1552 -216 -4 -279 C ATOM 1052 C VAL A 20 8.227 -3.112 11.565 1.00 13.33 C ANISOU 1052 C VAL B 20 1734 1507 1823 -239 -84 -178 C ATOM 1053 O VAL A 20 7.774 -4.208 11.839 1.00 16.45 O ANISOU 1053 O VAL B 20 2522 1717 2008 -383 -171 -280 O ATOM 1054 CB VAL A 20 7.812 -1.154 13.113 1.00 13.48 C ANISOU 1054 CB VAL B 20 1685 1552 1882 -225 -1 -214 C ATOM 1055 CG1 VAL A 20 6.460 -1.751 13.445 1.00 16.64 C ANISOU 1055 CG1 VAL B 20 1676 2281 2363 -364 293 -602 C ATOM 1056 CG2 VAL A 20 8.331 -0.432 14.328 1.00 14.78 C ANISOU 1056 CG2 VAL B 20 2105 1836 1674 -318 140 -371 C ATOM 1057 N ARG A 21 8.205 -2.590 10.361 1.00 13.74 N ANISOU 1057 N ARG B 21 1855 1779 1586 -234 -172 -420 N ATOM 1058 CA ARG A 21 7.616 -3.317 9.226 1.00 15.17 C ANISOU 1058 CA ARG B 21 2041 1919 1804 -161 -247 -308 C ATOM 1059 C ARG A 21 8.620 -3.989 8.337 1.00 14.59 C ANISOU 1059 C ARG B 21 2128 1816 1596 -89 -312 -212 C ATOM 1060 O ARG A 21 8.247 -4.801 7.470 1.00 16.23 O ANISOU 1060 O ARG B 21 2482 1988 1694 -161 -371 -426 O ATOM 1061 CB ARG A 21 6.794 -2.349 8.410 1.00 16.06 C ANISOU 1061 CB ARG B 21 2076 1982 2042 -64 -218 -455 C ATOM 1062 CG ARG A 21 5.704 -1.705 9.344 1.00 21.23 C ANISOU 1062 CG ARG B 21 2445 2804 2816 95 45 -144 C ATOM 1063 CD ARG A 21 4.643 -1.055 8.612 1.00 23.72 C ANISOU 1063 CD ARG B 21 2913 3038 3059 -2 -91 -88 C ATOM 1064 NE ARG A 21 5.176 0.094 7.922 1.00 26.42 N ANISOU 1064 NE ARG B 21 3317 3093 3626 127 -129 201 N ATOM 1065 CZ ARG A 21 4.556 0.694 6.922 1.00 29.11 C ANISOU 1065 CZ ARG B 21 3543 3808 3709 -43 -225 95 C ATOM 1066 NH1 ARG A 21 3.373 0.244 6.479 1.00 28.24 N ANISOU 1066 NH1 ARG B 21 3246 3617 3865 -189 -147 -178 N ATOM 1067 NH2 ARG A 21 5.140 1.733 6.360 1.00 29.43 N ANISOU 1067 NH2 ARG B 21 3748 3715 3719 17 -186 145 N ATOM 1068 N GLY A 22 9.899 -3.679 8.522 1.00 13.01 N ANISOU 1068 N GLY B 22 1998 1431 1513 160 -383 -115 N ATOM 1069 CA GLY A 22 10.901 -4.336 7.689 1.00 13.08 C ANISOU 1069 CA GLY B 22 1959 1547 1465 106 -210 -107 C ATOM 1070 C GLY A 22 10.805 -3.869 6.236 1.00 12.56 C ANISOU 1070 C GLY B 22 2040 1418 1312 122 -289 -249 C ATOM 1071 O GLY A 22 10.769 -4.650 5.272 1.00 13.91 O ANISOU 1071 O GLY B 22 2330 1584 1371 373 -379 -259 O ATOM 1072 N SER A 23 10.771 -2.543 6.079 1.00 12.95 N ANISOU 1072 N SER B 23 2241 1392 1287 82 -249 -133 N ATOM 1073 CA SER A 23 10.511 -1.954 4.770 1.00 13.79 C ANISOU 1073 CA SER B 23 2151 1716 1370 89 -249 -74 C ATOM 1074 C SER A 23 11.276 -0.670 4.628 1.00 13.24 C ANISOU 1074 C SER B 23 2141 1623 1265 61 -288 67 C ATOM 1075 O SER A 23 11.670 -0.060 5.617 1.00 14.41 O ANISOU 1075 O SER B 23 2310 1840 1323 -109 -438 -160 O ATOM 1076 CB SER A 23 9.026 -1.662 4.639 1.00 16.12 C ANISOU 1076 CB SER B 23 2447 2012 1666 178 -384 -78 C ATOM 1077 OG SER A 23 8.684 -0.562 5.468 1.00 19.24 O ANISOU 1077 OG SER B 23 2674 2414 2221 305 -370 -88 O ATOM 1078 N PRO A 24 11.424 -0.185 3.410 1.00 12.93 N ANISOU 1078 N PRO B 24 2107 1606 1197 156 -245 -226 N ATOM 1079 CA PRO A 24 11.824 1.208 3.262 1.00 14.23 C ANISOU 1079 CA PRO B 24 2114 1865 1425 -49 -70 -66 C ATOM 1080 C PRO A 24 10.809 2.100 3.957 1.00 13.45 C ANISOU 1080 C PRO B 24 2033 1593 1483 1 -92 -18 C ATOM 1081 O PRO A 24 9.646 1.744 4.042 1.00 14.35 O ANISOU 1081 O PRO B 24 2103 1693 1656 -60 -143 -259 O ATOM 1082 CB PRO A 24 11.758 1.429 1.744 1.00 14.74 C ANISOU 1082 CB PRO B 24 2202 1902 1494 22 -12 88 C ATOM 1083 CG PRO A 24 11.843 0.017 1.181 1.00 18.97 C ANISOU 1083 CG PRO B 24 2923 2489 1793 -156 71 -160 C ATOM 1084 CD PRO A 24 11.186 -0.869 2.129 1.00 13.25 C ANISOU 1084 CD PRO B 24 2456 1557 1021 278 -326 -28 C ATOM 1085 N ALA A 25 11.249 3.259 4.425 1.00 12.65 N ANISOU 1085 N ALA B 25 1879 1492 1432 -119 -87 -14 N ATOM 1086 CA ALA A 25 10.348 4.279 4.950 1.00 13.20 C ANISOU 1086 CA ALA B 25 2018 1536 1459 -28 -105 0 C ATOM 1087 C ALA A 25 10.079 5.263 3.818 1.00 12.86 C ANISOU 1087 C ALA B 25 1887 1524 1475 -67 -153 -1 C ATOM 1088 O ALA A 25 10.958 6.018 3.437 1.00 12.97 O ANISOU 1088 O ALA B 25 1933 1495 1500 -55 -286 109 O ATOM 1089 CB ALA A 25 10.971 4.999 6.160 1.00 13.12 C ANISOU 1089 CB ALA B 25 1999 1679 1304 -134 -67 -32 C ATOM 1090 N ILE A 26 8.864 5.183 3.280 1.00 13.40 N ANISOU 1090 N ILE B 26 1968 1656 1468 -88 -149 127 N ATOM 1091 CA ILE A 26 8.471 5.887 2.070 1.00 14.82 C ANISOU 1091 CA ILE B 26 2042 1906 1683 -88 -285 23 C ATOM 1092 C ILE A 26 7.795 7.196 2.415 1.00 14.99 C ANISOU 1092 C ILE B 26 1993 1965 1737 -45 -336 90 C ATOM 1093 O ILE A 26 7.063 7.307 3.382 1.00 14.77 O ANISOU 1093 O ILE B 26 1901 1943 1768 12 -363 144 O ATOM 1094 CB ILE A 26 7.517 4.977 1.199 1.00 16.60 C ANISOU 1094 CB ILE B 26 2494 1987 1822 -222 -358 -132 C ATOM 1095 CG1 ILE A 26 8.201 3.642 0.930 1.00 17.05 C ANISOU 1095 CG1 ILE B 26 2385 2273 1817 -218 -319 -300 C ATOM 1096 CG2 ILE A 26 7.123 5.639 -0.087 1.00 18.69 C ANISOU 1096 CG2 ILE B 26 2582 2417 2103 71 -300 -44 C ATOM 1097 CD1 ILE A 26 7.284 2.547 0.348 1.00 20.34 C ANISOU 1097 CD1 ILE B 26 2938 2529 2259 -347 -279 -253 C ATOM 1098 N ASN A 27 8.033 8.199 1.558 1.00 14.15 N ANISOU 1098 N ASN B 27 1727 1874 1772 -163 -209 147 N ATOM 1099 CA AASN A 27 7.400 9.493 1.678 0.50 14.98 C ANISOU 1099 CA AASN B 27 1835 1905 1948 -97 -165 83 C ATOM 1100 C ASN A 27 7.713 10.205 2.996 1.00 15.09 C ANISOU 1100 C ASN B 27 1842 1872 2018 -106 56 38 C ATOM 1101 O ASN A 27 6.881 10.937 3.535 1.00 17.98 O ANISOU 1101 O ASN B 27 1984 2229 2615 29 -43 -182 O ATOM 1102 CB AASN A 27 5.884 9.352 1.455 0.50 15.62 C ANISOU 1102 CB AASN B 27 1873 1960 2099 -48 -245 212 C ATOM 1103 CG AASN A 27 5.227 10.661 1.095 0.50 16.54 C ANISOU 1103 CG AASN B 27 2028 1968 2285 0 -187 289 C ATOM 1104 OD1AASN A 27 5.810 11.498 0.401 0.50 21.71 O ANISOU 1104 OD1AASN B 27 2377 2628 3242 73 -91 339 O ATOM 1105 ND2AASN A 27 4.025 10.861 1.630 0.50 20.31 N ANISOU 1105 ND2AASN B 27 2183 2394 3138 -90 -126 283 N ATOM 1106 N VAL A 28 8.942 10.011 3.471 1.00 13.40 N ANISOU 1106 N VAL B 28 1632 1692 1765 -114 -31 1 N ATOM 1107 CA VAL A 28 9.462 10.698 4.639 1.00 13.83 C ANISOU 1107 CA VAL B 28 1746 1728 1779 -142 -11 55 C ATOM 1108 C VAL A 28 10.077 12.026 4.182 1.00 13.34 C ANISOU 1108 C VAL B 28 1651 1691 1726 -72 -89 125 C ATOM 1109 O VAL A 28 10.949 12.041 3.319 1.00 12.86 O ANISOU 1109 O VAL B 28 1838 1484 1564 -34 -42 122 O ATOM 1110 CB VAL A 28 10.523 9.849 5.398 1.00 14.30 C ANISOU 1110 CB VAL B 28 2112 1600 1720 -126 -16 47 C ATOM 1111 CG1 VAL A 28 11.061 10.620 6.612 1.00 16.49 C ANISOU 1111 CG1 VAL B 28 2611 1777 1877 -143 -313 -227 C ATOM 1112 CG2 VAL A 28 9.898 8.564 5.877 1.00 15.50 C ANISOU 1112 CG2 VAL B 28 2495 1578 1814 -346 155 173 C ATOM 1113 N ALA A 29 9.684 13.115 4.808 1.00 12.96 N ANISOU 1113 N ALA B 29 1620 1640 1662 -26 184 245 N ATOM 1114 CA ALA A 29 10.290 14.432 4.490 1.00 12.64 C ANISOU 1114 CA ALA B 29 1606 1553 1642 -18 25 177 C ATOM 1115 C ALA A 29 11.663 14.540 5.121 1.00 11.77 C ANISOU 1115 C ALA B 29 1523 1529 1419 -22 56 172 C ATOM 1116 O ALA A 29 11.888 14.113 6.253 1.00 11.68 O ANISOU 1116 O ALA B 29 1549 1660 1228 -119 39 266 O ATOM 1117 CB ALA A 29 9.434 15.608 4.957 1.00 13.60 C ANISOU 1117 CB ALA B 29 1796 1486 1885 163 166 142 C ATOM 1118 N VAL A 30 12.596 15.040 4.327 1.00 11.38 N ANISOU 1118 N VAL B 30 1485 1514 1322 -78 9 361 N ATOM 1119 CA VAL A 30 13.966 15.199 4.697 1.00 11.50 C ANISOU 1119 CA VAL B 30 1438 1596 1333 -77 24 257 C ATOM 1120 C VAL A 30 14.390 16.620 4.278 1.00 10.56 C ANISOU 1120 C VAL B 30 1338 1590 1084 -26 -76 350 C ATOM 1121 O VAL A 30 14.207 17.043 3.127 1.00 12.98 O ANISOU 1121 O VAL B 30 1574 1955 1404 -151 -156 445 O ATOM 1122 CB VAL A 30 14.864 14.165 3.995 1.00 11.82 C ANISOU 1122 CB VAL B 30 1439 1826 1225 109 -126 316 C ATOM 1123 CG1 VAL A 30 16.353 14.454 4.340 1.00 14.11 C ANISOU 1123 CG1 VAL B 30 1236 2032 2092 71 72 162 C ATOM 1124 CG2 VAL A 30 14.466 12.745 4.336 1.00 13.12 C ANISOU 1124 CG2 VAL B 30 1738 1415 1829 -130 -70 -89 C ATOM 1125 N HIS A 31 14.979 17.325 5.276 1.00 11.71 N ANISOU 1125 N HIS B 31 1434 1652 1361 -125 57 275 N ATOM 1126 CA HIS A 31 15.533 18.656 5.037 1.00 12.00 C ANISOU 1126 CA HIS B 31 1459 1656 1443 -68 -184 398 C ATOM 1127 C HIS A 31 16.999 18.693 5.410 1.00 10.53 C ANISOU 1127 C HIS B 31 1296 1455 1247 -99 -242 667 C ATOM 1128 O HIS A 31 17.392 18.210 6.478 1.00 14.81 O ANISOU 1128 O HIS B 31 1631 2243 1752 -299 -198 675 O ATOM 1129 CB HIS A 31 14.810 19.722 5.854 1.00 14.46 C ANISOU 1129 CB HIS B 31 1730 1904 1859 -2 -201 303 C ATOM 1130 CG HIS A 31 13.360 19.883 5.501 1.00 16.79 C ANISOU 1130 CG HIS B 31 2039 1933 2406 189 -173 -45 C ATOM 1131 ND1 HIS A 31 12.876 21.000 4.847 1.00 20.86 N ANISOU 1131 ND1 HIS B 31 2316 2367 3243 422 -633 100 N ATOM 1132 CD2 HIS A 31 12.295 19.067 5.698 1.00 18.91 C ANISOU 1132 CD2 HIS B 31 2220 2065 2899 74 -248 -136 C ATOM 1133 CE1 HIS A 31 11.570 20.846 4.632 1.00 20.61 C ANISOU 1133 CE1 HIS B 31 2232 2460 3137 456 -402 64 C ATOM 1134 NE2 HIS A 31 11.182 19.706 5.176 1.00 20.79 N ANISOU 1134 NE2 HIS B 31 2471 2418 3009 362 -268 -94 N ATOM 1135 N VAL A 32 17.758 19.281 4.478 1.00 11.80 N ANISOU 1135 N VAL B 32 1413 1585 1485 -108 -92 546 N ATOM 1136 CA VAL A 32 19.176 19.451 4.658 1.00 12.17 C ANISOU 1136 CA VAL B 32 1508 1478 1636 36 -93 503 C ATOM 1137 C VAL A 32 19.448 20.928 4.833 1.00 11.86 C ANISOU 1137 C VAL B 32 1600 1409 1494 178 -122 341 C ATOM 1138 O VAL A 32 18.832 21.763 4.126 1.00 13.14 O ANISOU 1138 O VAL B 32 1718 1538 1737 81 -231 669 O ATOM 1139 CB VAL A 32 20.021 18.892 3.492 1.00 11.60 C ANISOU 1139 CB VAL B 32 1446 1500 1458 51 -72 470 C ATOM 1140 CG1 VAL A 32 21.509 18.982 3.799 1.00 13.65 C ANISOU 1140 CG1 VAL B 32 1251 1921 2014 125 -157 295 C ATOM 1141 CG2 VAL A 32 19.615 17.459 3.173 1.00 13.93 C ANISOU 1141 CG2 VAL B 32 1787 1691 1815 -23 -60 250 C ATOM 1142 N PHE A 33 20.284 21.258 5.787 1.00 12.27 N ANISOU 1142 N PHE B 33 1549 1411 1700 34 -240 439 N ATOM 1143 CA PHE A 33 20.704 22.610 6.108 1.00 13.45 C ANISOU 1143 CA PHE B 33 1767 1559 1785 114 -213 357 C ATOM 1144 C PHE A 33 22.239 22.670 6.079 1.00 13.62 C ANISOU 1144 C PHE B 33 1752 1588 1832 -75 -142 329 C ATOM 1145 O PHE A 33 22.920 21.674 6.381 1.00 12.66 O ANISOU 1145 O PHE B 33 1505 1681 1622 121 -139 525 O ATOM 1146 CB PHE A 33 20.214 23.023 7.491 1.00 14.20 C ANISOU 1146 CB PHE B 33 1856 1493 2044 -21 -172 247 C ATOM 1147 CG PHE A 33 18.730 22.903 7.680 1.00 14.80 C ANISOU 1147 CG PHE B 33 1838 1646 2139 50 -156 -42 C ATOM 1148 CD1 PHE A 33 18.154 21.706 8.090 1.00 14.56 C ANISOU 1148 CD1 PHE B 33 1636 1714 2182 31 140 -168 C ATOM 1149 CD2 PHE A 33 17.907 23.980 7.444 1.00 17.00 C ANISOU 1149 CD2 PHE B 33 2014 1853 2592 -68 -226 13 C ATOM 1150 CE1 PHE A 33 16.779 21.549 8.232 1.00 15.29 C ANISOU 1150 CE1 PHE B 33 1782 1944 2084 0 142 -110 C ATOM 1151 CE2 PHE A 33 16.543 23.842 7.579 1.00 17.87 C ANISOU 1151 CE2 PHE B 33 2004 2085 2699 247 -261 236 C ATOM 1152 CZ PHE A 33 15.973 22.655 7.974 1.00 16.56 C ANISOU 1152 CZ PHE B 33 1813 2089 2387 56 -97 52 C ATOM 1153 N ARG A 34 22.773 23.856 5.781 1.00 15.40 N ANISOU 1153 N ARG B 34 2006 1661 2182 -12 -190 414 N ATOM 1154 CA AARG A 34 24.194 24.141 5.863 0.50 16.23 C ANISOU 1154 CA AARG B 34 2097 1891 2176 -23 -72 266 C ATOM 1155 C ARG A 34 24.391 25.189 6.949 1.00 16.09 C ANISOU 1155 C ARG B 34 2111 1728 2274 -75 -17 307 C ATOM 1156 O ARG A 34 23.641 26.171 7.004 1.00 17.50 O ANISOU 1156 O ARG B 34 2191 1788 2670 89 -309 24 O ATOM 1157 CB AARG A 34 24.715 24.654 4.498 0.50 17.23 C ANISOU 1157 CB AARG B 34 2345 2032 2166 -69 -72 306 C ATOM 1158 CG AARG A 34 26.218 24.870 4.445 0.50 17.97 C ANISOU 1158 CG AARG B 34 2286 2229 2311 -55 -29 197 C ATOM 1159 CD AARG A 34 26.908 25.007 3.048 0.50 20.25 C ANISOU 1159 CD AARG B 34 2654 2510 2528 -29 -21 241 C ATOM 1160 NE AARG A 34 28.373 25.002 3.246 0.50 22.63 N ANISOU 1160 NE AARG B 34 2831 2898 2869 -176 254 229 N ATOM 1161 CZ AARG A 34 29.105 26.080 3.537 0.50 24.15 C ANISOU 1161 CZ AARG B 34 3009 3003 3163 -83 87 -18 C ATOM 1162 NH1AARG A 34 28.575 27.298 3.556 0.50 24.09 N ANISOU 1162 NH1AARG B 34 2921 3000 3230 80 175 -34 N ATOM 1163 NH2AARG A 34 30.408 25.963 3.724 0.50 23.40 N ANISOU 1163 NH2AARG B 34 2832 2759 3300 120 -9 55 N ATOM 1164 N LYS A 35 25.416 25.031 7.778 1.00 17.04 N ANISOU 1164 N LYS B 35 2200 1951 2321 -1 -120 193 N ATOM 1165 CA LYS A 35 25.674 26.003 8.831 1.00 19.32 C ANISOU 1165 CA LYS B 35 2507 2287 2546 -89 -47 148 C ATOM 1166 C LYS A 35 26.310 27.256 8.230 1.00 19.54 C ANISOU 1166 C LYS B 35 2546 2205 2671 -145 49 147 C ATOM 1167 O LYS A 35 27.323 27.160 7.525 1.00 19.33 O ANISOU 1167 O LYS B 35 2590 1932 2820 -219 189 165 O ATOM 1168 CB LYS A 35 26.578 25.399 9.912 1.00 19.68 C ANISOU 1168 CB LYS B 35 2393 2495 2588 3 -183 124 C ATOM 1169 CG LYS A 35 26.470 26.136 11.239 1.00 23.47 C ANISOU 1169 CG LYS B 35 3081 2860 2977 -4 -139 -6 C ATOM 1170 CD LYS A 35 27.443 25.608 12.260 1.00 25.13 C ANISOU 1170 CD LYS B 35 3111 3224 3213 -49 -174 -38 C ATOM 1171 CE LYS A 35 26.834 25.436 13.620 1.00 30.54 C ANISOU 1171 CE LYS B 35 3923 3921 3760 100 -97 -31 C ATOM 1172 NZ LYS A 35 27.864 24.877 14.537 1.00 30.60 N ANISOU 1172 NZ LYS B 35 4220 3921 3483 178 -189 140 N ATOM 1173 N ALA A 36 25.681 28.402 8.469 1.00 20.46 N ANISOU 1173 N ALA B 36 2687 2321 2762 -260 279 208 N ATOM 1174 CA ALA A 36 26.145 29.694 7.962 1.00 23.21 C ANISOU 1174 CA ALA B 36 3088 2654 3078 -191 132 79 C ATOM 1175 C ALA A 36 27.200 30.251 8.887 1.00 24.41 C ANISOU 1175 C ALA B 36 3245 2859 3170 -184 96 28 C ATOM 1176 O ALA A 36 27.367 29.780 10.026 1.00 24.53 O ANISOU 1176 O ALA B 36 3244 2996 3078 -495 76 -227 O ATOM 1177 CB ALA A 36 24.962 30.644 7.899 1.00 24.48 C ANISOU 1177 CB ALA B 36 3250 2717 3332 -101 118 -23 C ATOM 1178 N ALA A 37 27.878 31.300 8.404 1.00 26.62 N ANISOU 1178 N ALA B 37 3501 3163 3450 -267 151 2 N ATOM 1179 CA ALA A 37 28.949 31.924 9.194 1.00 28.10 C ANISOU 1179 CA ALA B 37 3744 3376 3554 -229 98 -30 C ATOM 1180 C ALA A 37 28.503 32.454 10.553 1.00 29.91 C ANISOU 1180 C ALA B 37 4000 3634 3730 -184 69 -80 C ATOM 1181 O ALA A 37 29.293 32.407 11.486 1.00 31.79 O ANISOU 1181 O ALA B 37 4251 3784 4043 -292 0 -161 O ATOM 1182 CB ALA A 37 29.591 33.061 8.432 1.00 29.49 C ANISOU 1182 CB ALA B 37 3975 3408 3821 -300 119 25 C ATOM 1183 N ASP A 38 27.260 32.940 10.627 1.00 30.39 N ANISOU 1183 N ASP B 38 4082 3682 3782 -158 113 -130 N ATOM 1184 CA ASP A 38 26.627 33.370 11.889 1.00 30.89 C ANISOU 1184 CA ASP B 38 4097 3779 3859 -134 138 -86 C ATOM 1185 C ASP A 38 26.078 32.231 12.746 1.00 31.45 C ANISOU 1185 C ASP B 38 4180 3819 3950 -110 186 -71 C ATOM 1186 O ASP A 38 25.418 32.492 13.752 1.00 31.84 O ANISOU 1186 O ASP B 38 4320 3881 3897 -159 288 -241 O ATOM 1187 CB ASP A 38 25.509 34.383 11.632 1.00 31.77 C ANISOU 1187 CB ASP B 38 4239 3838 3993 -119 79 -84 C ATOM 1188 CG ASP A 38 24.322 33.818 10.856 1.00 34.29 C ANISOU 1188 CG ASP B 38 4379 4067 4580 -66 71 -72 C ATOM 1189 OD1 ASP A 38 24.252 32.597 10.560 1.00 33.27 O ANISOU 1189 OD1 ASP B 38 4440 3691 4510 99 407 -44 O ATOM 1190 OD2 ASP A 38 23.428 34.639 10.532 1.00 37.17 O ANISOU 1190 OD2 ASP B 38 4960 4015 5147 147 35 112 O ATOM 1191 N ASP A 39 26.360 30.985 12.369 1.00 30.32 N ANISOU 1191 N ASP B 39 4017 3745 3756 -125 172 -126 N ATOM 1192 CA ASP A 39 25.967 29.800 13.159 1.00 30.50 C ANISOU 1192 CA ASP B 39 4021 3817 3749 -36 94 -75 C ATOM 1193 C ASP A 39 24.492 29.424 13.067 1.00 29.57 C ANISOU 1193 C ASP B 39 3901 3721 3611 23 127 -53 C ATOM 1194 O ASP A 39 24.054 28.500 13.758 1.00 32.30 O ANISOU 1194 O ASP B 39 4125 4122 4024 -63 160 59 O ATOM 1195 CB ASP A 39 26.376 29.915 14.647 1.00 32.06 C ANISOU 1195 CB ASP B 39 4185 4119 3877 -63 -39 -89 C ATOM 1196 CG ASP A 39 27.845 29.603 14.884 1.00 35.52 C ANISOU 1196 CG ASP B 39 4501 4692 4301 64 -48 -88 C ATOM 1197 OD1 ASP A 39 28.569 29.183 13.943 1.00 39.34 O ANISOU 1197 OD1 ASP B 39 5020 5148 4779 10 -4 -287 O ATOM 1198 OD2 ASP A 39 28.277 29.792 16.050 1.00 41.39 O ANISOU 1198 OD2 ASP B 39 5404 5529 4792 35 -189 -217 O ATOM 1199 N THR A 40 23.738 30.060 12.189 1.00 27.24 N ANISOU 1199 N THR B 40 3618 3295 3436 164 242 -234 N ATOM 1200 CA THR A 40 22.392 29.612 11.931 1.00 26.69 C ANISOU 1200 CA THR B 40 3570 3168 3402 138 152 -106 C ATOM 1201 C THR A 40 22.388 28.529 10.844 1.00 24.62 C ANISOU 1201 C THR B 40 3176 2927 3251 181 205 -116 C ATOM 1202 O THR A 40 23.365 28.358 10.090 1.00 22.72 O ANISOU 1202 O THR B 40 2882 2601 3150 -48 483 -106 O ATOM 1203 CB THR A 40 21.510 30.778 11.486 1.00 27.40 C ANISOU 1203 CB THR B 40 3626 3245 3538 188 163 -101 C ATOM 1204 OG1 THR A 40 21.980 31.288 10.231 1.00 27.86 O ANISOU 1204 OG1 THR B 40 4025 2893 3666 460 241 170 O ATOM 1205 CG2 THR A 40 21.538 31.920 12.543 1.00 28.55 C ANISOU 1205 CG2 THR B 40 3800 3248 3797 229 270 -215 C ATOM 1206 N TRP A 41 21.291 27.803 10.778 1.00 23.53 N ANISOU 1206 N TRP B 41 3067 2802 3069 242 122 19 N ATOM 1207 CA TRP A 41 21.120 26.736 9.826 1.00 22.73 C ANISOU 1207 CA TRP B 41 2902 2763 2971 223 30 29 C ATOM 1208 C TRP A 41 20.373 27.259 8.619 1.00 23.56 C ANISOU 1208 C TRP B 41 2962 2776 3214 263 -43 49 C ATOM 1209 O TRP A 41 19.191 27.647 8.732 1.00 26.91 O ANISOU 1209 O TRP B 41 3077 3425 3722 358 33 187 O ATOM 1210 CB TRP A 41 20.308 25.606 10.446 1.00 22.01 C ANISOU 1210 CB TRP B 41 2867 2645 2848 216 16 42 C ATOM 1211 CG TRP A 41 21.061 24.870 11.477 1.00 20.46 C ANISOU 1211 CG TRP B 41 2710 2694 2368 192 23 9 C ATOM 1212 CD1 TRP A 41 20.806 24.849 12.805 1.00 22.34 C ANISOU 1212 CD1 TRP B 41 2796 2924 2766 232 192 9 C ATOM 1213 CD2 TRP A 41 22.225 24.043 11.279 1.00 18.98 C ANISOU 1213 CD2 TRP B 41 2450 2381 2379 78 -53 236 C ATOM 1214 NE1 TRP A 41 21.709 24.061 13.444 1.00 23.10 N ANISOU 1214 NE1 TRP B 41 2851 3357 2566 256 175 118 N ATOM 1215 CE2 TRP A 41 22.589 23.539 12.526 1.00 21.14 C ANISOU 1215 CE2 TRP B 41 2661 3025 2345 253 138 82 C ATOM 1216 CE3 TRP A 41 22.960 23.655 10.162 1.00 17.92 C ANISOU 1216 CE3 TRP B 41 2292 2043 2474 -204 95 182 C ATOM 1217 CZ2 TRP A 41 23.682 22.675 12.699 1.00 22.54 C ANISOU 1217 CZ2 TRP B 41 2934 2903 2729 251 99 209 C ATOM 1218 CZ3 TRP A 41 24.042 22.791 10.339 1.00 19.04 C ANISOU 1218 CZ3 TRP B 41 2440 2331 2461 -137 140 254 C ATOM 1219 CH2 TRP A 41 24.400 22.341 11.594 1.00 20.04 C ANISOU 1219 CH2 TRP B 41 2558 2459 2596 134 38 199 C ATOM 1220 N GLU A 42 21.005 27.256 7.461 1.00 22.04 N ANISOU 1220 N GLU B 42 2800 2614 2960 291 -227 61 N ATOM 1221 CA GLU A 42 20.285 27.736 6.288 1.00 23.23 C ANISOU 1221 CA GLU B 42 3043 2680 3101 223 -187 108 C ATOM 1222 C GLU A 42 19.817 26.599 5.396 1.00 20.80 C ANISOU 1222 C GLU B 42 2597 2294 3012 243 -235 153 C ATOM 1223 O GLU A 42 20.573 25.632 5.171 1.00 18.68 O ANISOU 1223 O GLU B 42 2464 1796 2836 403 -330 423 O ATOM 1224 CB GLU A 42 21.078 28.760 5.536 1.00 26.00 C ANISOU 1224 CB GLU B 42 3380 3110 3386 51 -114 143 C ATOM 1225 CG GLU A 42 22.368 28.313 4.977 1.00 28.55 C ANISOU 1225 CG GLU B 42 3723 3420 3704 38 -7 150 C ATOM 1226 CD GLU A 42 22.954 29.334 3.989 1.00 30.29 C ANISOU 1226 CD GLU B 42 4095 3589 3823 -24 -1 191 C ATOM 1227 OE1 GLU A 42 23.100 30.498 4.421 1.00 36.03 O ANISOU 1227 OE1 GLU B 42 4909 3867 4910 -123 -146 66 O ATOM 1228 OE2 GLU A 42 23.276 28.953 2.824 1.00 34.93 O ANISOU 1228 OE2 GLU B 42 4629 4476 4165 -247 400 178 O ATOM 1229 N PRO A 43 18.562 26.682 4.922 1.00 20.31 N ANISOU 1229 N PRO B 43 2645 2114 2955 450 -273 247 N ATOM 1230 CA PRO A 43 18.089 25.655 4.036 1.00 19.02 C ANISOU 1230 CA PRO B 43 2434 2090 2701 351 -233 355 C ATOM 1231 C PRO A 43 19.051 25.429 2.913 1.00 17.10 C ANISOU 1231 C PRO B 43 2229 1850 2418 284 -266 479 C ATOM 1232 O PRO A 43 19.560 26.382 2.303 1.00 18.95 O ANISOU 1232 O PRO B 43 2591 1934 2675 168 -95 524 O ATOM 1233 CB PRO A 43 16.775 26.237 3.539 1.00 19.96 C ANISOU 1233 CB PRO B 43 2523 2233 2825 388 -336 244 C ATOM 1234 CG PRO A 43 16.322 27.053 4.729 1.00 21.19 C ANISOU 1234 CG PRO B 43 2699 2438 2910 345 -45 211 C ATOM 1235 CD PRO A 43 17.503 27.685 5.217 1.00 21.98 C ANISOU 1235 CD PRO B 43 2875 2436 3040 446 -201 153 C ATOM 1236 N PHE A 44 19.243 24.171 2.583 1.00 15.13 N ANISOU 1236 N PHE B 44 1859 1752 2137 96 -243 401 N ATOM 1237 CA PHE A 44 20.164 23.746 1.562 1.00 13.91 C ANISOU 1237 CA PHE B 44 1763 1752 1767 -35 -156 465 C ATOM 1238 C PHE A 44 19.537 22.852 0.495 1.00 13.46 C ANISOU 1238 C PHE B 44 1692 1725 1695 -33 -151 543 C ATOM 1239 O PHE A 44 19.726 23.072 -0.667 1.00 16.17 O ANISOU 1239 O PHE B 44 1986 2209 1949 -173 -62 555 O ATOM 1240 CB PHE A 44 21.386 23.042 2.249 1.00 13.34 C ANISOU 1240 CB PHE B 44 1505 1820 1742 7 -182 375 C ATOM 1241 CG PHE A 44 22.423 22.573 1.292 1.00 14.51 C ANISOU 1241 CG PHE B 44 1561 1916 2034 -39 -117 467 C ATOM 1242 CD1 PHE A 44 23.309 23.476 0.719 1.00 15.13 C ANISOU 1242 CD1 PHE B 44 1888 1968 1890 -17 113 448 C ATOM 1243 CD2 PHE A 44 22.496 21.247 0.910 1.00 15.28 C ANISOU 1243 CD2 PHE B 44 1717 2204 1882 69 -138 150 C ATOM 1244 CE1 PHE A 44 24.268 23.025 -0.189 1.00 16.24 C ANISOU 1244 CE1 PHE B 44 1869 2541 1758 -17 25 427 C ATOM 1245 CE2 PHE A 44 23.424 20.815 0.010 1.00 16.52 C ANISOU 1245 CE2 PHE B 44 1855 2352 2067 10 -281 171 C ATOM 1246 CZ PHE A 44 24.315 21.704 -0.533 1.00 16.72 C ANISOU 1246 CZ PHE B 44 1933 2761 1657 89 98 182 C ATOM 1247 N ALA A 45 18.745 21.865 0.909 1.00 13.69 N ANISOU 1247 N ALA B 45 1598 1748 1854 -123 -157 457 N ATOM 1248 CA ALA A 45 18.064 20.978 -0.017 1.00 13.28 C ANISOU 1248 CA ALA B 45 1607 1834 1603 -57 -125 437 C ATOM 1249 C ALA A 45 17.024 20.185 0.769 1.00 12.63 C ANISOU 1249 C ALA B 45 1608 1732 1456 -73 -138 477 C ATOM 1250 O ALA A 45 17.123 20.067 1.985 1.00 14.17 O ANISOU 1250 O ALA B 45 1753 1959 1670 -187 -168 527 O ATOM 1251 CB ALA A 45 19.039 20.022 -0.701 1.00 14.54 C ANISOU 1251 CB ALA B 45 1631 2059 1833 -53 -105 246 C ATOM 1252 N SER A 46 15.987 19.688 0.063 1.00 12.12 N ANISOU 1252 N SER B 46 1487 1698 1420 -21 -190 435 N ATOM 1253 CA SER A 46 14.985 18.865 0.707 1.00 12.01 C ANISOU 1253 CA SER B 46 1491 1586 1486 131 -195 464 C ATOM 1254 C SER A 46 14.261 17.984 -0.278 1.00 11.89 C ANISOU 1254 C SER B 46 1566 1415 1535 117 -60 464 C ATOM 1255 O SER A 46 14.338 18.179 -1.471 1.00 14.37 O ANISOU 1255 O SER B 46 1931 1849 1678 20 -95 632 O ATOM 1256 CB SER A 46 14.002 19.730 1.533 1.00 13.34 C ANISOU 1256 CB SER B 46 1672 1782 1612 -32 9 232 C ATOM 1257 OG SER A 46 13.313 20.645 0.702 1.00 13.27 O ANISOU 1257 OG SER B 46 1543 1879 1619 129 -381 469 O ATOM 1258 N GLY A 47 13.520 17.027 0.259 1.00 11.99 N ANISOU 1258 N GLY B 47 1441 1539 1575 -78 -33 376 N ATOM 1259 CA GLY A 47 12.714 16.145 -0.583 1.00 12.61 C ANISOU 1259 CA GLY B 47 1524 1576 1689 -6 -100 345 C ATOM 1260 C GLY A 47 11.969 15.142 0.274 1.00 12.87 C ANISOU 1260 C GLY B 47 1612 1632 1646 -26 -203 372 C ATOM 1261 O GLY A 47 11.995 15.256 1.508 1.00 13.51 O ANISOU 1261 O GLY B 47 1787 1674 1671 -54 -170 351 O ATOM 1262 N LYS A 48 11.357 14.170 -0.398 1.00 13.90 N ANISOU 1262 N LYS B 48 2008 1699 1572 -149 -95 346 N ATOM 1263 CA LYS A 48 10.672 13.082 0.297 1.00 14.68 C ANISOU 1263 CA LYS B 48 2089 1768 1719 -156 -30 246 C ATOM 1264 C LYS A 48 11.278 11.777 -0.184 1.00 14.12 C ANISOU 1264 C LYS B 48 2222 1656 1485 -196 -111 168 C ATOM 1265 O LYS A 48 11.567 11.600 -1.371 1.00 14.26 O ANISOU 1265 O LYS B 48 2104 1871 1443 -206 -59 286 O ATOM 1266 CB LYS A 48 9.187 13.064 -0.052 1.00 17.86 C ANISOU 1266 CB LYS B 48 2340 2174 2269 -148 10 207 C ATOM 1267 CG LYS A 48 8.433 14.305 0.363 1.00 24.01 C ANISOU 1267 CG LYS B 48 3121 2691 3309 -50 112 73 C ATOM 1268 CD LYS A 48 8.055 14.337 1.836 1.00 30.07 C ANISOU 1268 CD LYS B 48 3942 3751 3731 -24 -85 6 C ATOM 1269 CE LYS A 48 6.567 14.006 2.127 1.00 31.24 C ANISOU 1269 CE LYS B 48 4106 3801 3962 -73 21 96 C ATOM 1270 NZ LYS A 48 6.235 13.734 3.601 1.00 31.98 N ANISOU 1270 NZ LYS B 48 4168 4048 3934 159 296 -122 N ATOM 1271 N THR A 49 11.470 10.828 0.726 1.00 12.95 N ANISOU 1271 N THR B 49 2060 1587 1272 -175 -213 131 N ATOM 1272 CA THR A 49 12.023 9.555 0.295 1.00 13.08 C ANISOU 1272 CA THR B 49 1929 1663 1375 -129 -167 127 C ATOM 1273 C THR A 49 11.070 8.869 -0.711 1.00 13.76 C ANISOU 1273 C THR B 49 1983 1893 1351 -150 -190 314 C ATOM 1274 O THR A 49 9.863 8.985 -0.612 1.00 14.66 O ANISOU 1274 O THR B 49 1990 2031 1548 -125 -213 181 O ATOM 1275 CB THR A 49 12.289 8.627 1.489 1.00 12.95 C ANISOU 1275 CB THR B 49 1873 1708 1339 21 -250 190 C ATOM 1276 OG1 THR A 49 11.034 8.407 2.172 1.00 12.70 O ANISOU 1276 OG1 THR B 49 1810 1605 1410 -17 -16 49 O ATOM 1277 CG2 THR A 49 13.369 9.195 2.436 1.00 12.59 C ANISOU 1277 CG2 THR B 49 1581 1908 1295 -73 -330 138 C ATOM 1278 N SER A 50 11.667 8.084 -1.592 1.00 14.16 N ANISOU 1278 N SER B 50 2013 1914 1450 -194 -254 110 N ATOM 1279 CA SER A 50 10.984 7.381 -2.662 1.00 16.00 C ANISOU 1279 CA SER B 50 2348 2188 1539 -149 -245 32 C ATOM 1280 C SER A 50 10.432 6.071 -2.145 1.00 17.58 C ANISOU 1280 C SER B 50 2458 2293 1926 -195 -316 -9 C ATOM 1281 O SER A 50 10.575 5.710 -0.964 1.00 16.55 O ANISOU 1281 O SER B 50 2697 2081 1508 -371 -290 79 O ATOM 1282 CB SER A 50 11.979 7.062 -3.780 1.00 16.75 C ANISOU 1282 CB SER B 50 2541 2335 1487 -181 -245 38 C ATOM 1283 OG SER A 50 12.889 6.051 -3.307 1.00 19.50 O ANISOU 1283 OG SER B 50 2968 2467 1971 -93 -250 -283 O ATOM 1284 N GLU A 51 9.845 5.310 -3.032 1.00 18.29 N ANISOU 1284 N GLU B 51 2861 2366 1722 -283 -351 -148 N ATOM 1285 CA GLU A 51 9.412 3.961 -2.728 1.00 18.81 C ANISOU 1285 CA GLU B 51 2792 2415 1940 -221 -276 -93 C ATOM 1286 C GLU A 51 10.510 3.034 -2.226 1.00 17.73 C ANISOU 1286 C GLU B 51 2661 2340 1732 -222 -148 -244 C ATOM 1287 O GLU A 51 10.175 2.035 -1.568 1.00 20.11 O ANISOU 1287 O GLU B 51 3031 2433 2176 -136 -193 -50 O ATOM 1288 CB GLU A 51 8.711 3.320 -3.976 1.00 22.34 C ANISOU 1288 CB GLU B 51 3293 2819 2376 -235 -323 -78 C ATOM 1289 CG GLU A 51 7.343 3.879 -4.179 1.00 28.10 C ANISOU 1289 CG GLU B 51 3682 3557 3436 -53 -174 -82 C ATOM 1290 CD GLU A 51 6.296 3.348 -3.179 1.00 34.43 C ANISOU 1290 CD GLU B 51 4330 4437 4312 -124 -16 7 C ATOM 1291 OE1 GLU A 51 6.432 2.191 -2.719 1.00 42.21 O ANISOU 1291 OE1 GLU B 51 5416 5238 5381 157 -141 123 O ATOM 1292 OE2 GLU A 51 5.323 4.090 -2.868 1.00 41.27 O ANISOU 1292 OE2 GLU B 51 5292 5261 5125 78 45 -147 O ATOM 1293 N SER A 52 11.774 3.317 -2.517 1.00 17.58 N ANISOU 1293 N SER B 52 2829 2244 1606 -178 -260 -219 N ATOM 1294 CA SER A 52 12.857 2.507 -2.018 1.00 18.83 C ANISOU 1294 CA SER B 52 2876 2392 1884 -43 -144 -164 C ATOM 1295 C SER A 52 13.442 3.102 -0.738 1.00 17.30 C ANISOU 1295 C SER B 52 2655 2170 1747 109 -118 -190 C ATOM 1296 O SER A 52 14.443 2.591 -0.216 1.00 19.81 O ANISOU 1296 O SER B 52 3031 2558 1936 356 38 -180 O ATOM 1297 CB SER A 52 13.936 2.427 -3.057 1.00 21.03 C ANISOU 1297 CB SER B 52 3054 2731 2204 58 -143 -260 C ATOM 1298 OG SER A 52 14.495 3.691 -3.262 1.00 25.20 O ANISOU 1298 OG SER B 52 3560 3387 2624 -69 229 -1 O ATOM 1299 N GLY A 53 12.815 4.161 -0.197 1.00 16.04 N ANISOU 1299 N GLY B 53 2616 1963 1513 71 -123 -165 N ATOM 1300 CA GLY A 53 13.289 4.776 1.031 1.00 15.76 C ANISOU 1300 CA GLY B 53 2476 2191 1322 -4 -199 21 C ATOM 1301 C GLY A 53 14.462 5.690 0.843 1.00 15.19 C ANISOU 1301 C GLY B 53 2339 2117 1313 42 -101 -55 C ATOM 1302 O GLY A 53 15.073 6.127 1.778 1.00 14.61 O ANISOU 1302 O GLY B 53 2203 2161 1185 13 -372 -54 O ATOM 1303 N GLU A 54 14.775 6.035 -0.400 1.00 14.87 N ANISOU 1303 N GLU B 54 2212 2282 1154 -73 -122 -12 N ATOM 1304 CA GLU A 54 15.943 6.812 -0.738 1.00 15.74 C ANISOU 1304 CA GLU B 54 2337 2191 1451 -81 -128 16 C ATOM 1305 C GLU A 54 15.535 8.169 -1.256 1.00 15.01 C ANISOU 1305 C GLU B 54 1977 2334 1389 17 -110 11 C ATOM 1306 O GLU A 54 14.434 8.385 -1.826 1.00 15.94 O ANISOU 1306 O GLU B 54 1975 2534 1548 -34 -443 354 O ATOM 1307 CB GLU A 54 16.771 6.062 -1.807 1.00 16.70 C ANISOU 1307 CB GLU B 54 2324 2250 1770 56 -2 59 C ATOM 1308 CG GLU A 54 17.263 4.688 -1.296 1.00 19.62 C ANISOU 1308 CG GLU B 54 2819 2397 2237 55 -108 65 C ATOM 1309 CD GLU A 54 18.154 3.905 -2.249 1.00 22.25 C ANISOU 1309 CD GLU B 54 3049 2648 2756 213 122 113 C ATOM 1310 OE1 GLU A 54 18.415 4.397 -3.354 1.00 27.72 O ANISOU 1310 OE1 GLU B 54 4232 3073 3228 343 693 16 O ATOM 1311 OE2 GLU A 54 18.568 2.778 -1.906 1.00 32.72 O ANISOU 1311 OE2 GLU B 54 4533 3435 4462 257 18 201 O ATOM 1312 N LEU A 55 16.464 9.088 -1.074 1.00 13.87 N ANISOU 1312 N LEU B 55 1971 2005 1291 -41 -275 112 N ATOM 1313 CA LEU A 55 16.324 10.434 -1.561 1.00 14.49 C ANISOU 1313 CA LEU B 55 1960 2101 1444 -28 -178 38 C ATOM 1314 C LEU A 55 17.608 10.791 -2.233 1.00 15.29 C ANISOU 1314 C LEU B 55 2161 2246 1401 21 -94 139 C ATOM 1315 O LEU A 55 18.642 10.931 -1.578 1.00 15.59 O ANISOU 1315 O LEU B 55 2073 2222 1627 -51 -111 8 O ATOM 1316 CB LEU A 55 16.005 11.383 -0.429 1.00 14.65 C ANISOU 1316 CB LEU B 55 1904 2143 1518 28 -217 -105 C ATOM 1317 CG LEU A 55 15.805 12.835 -0.746 1.00 15.34 C ANISOU 1317 CG LEU B 55 1940 2331 1556 49 -98 3 C ATOM 1318 CD1 LEU A 55 14.866 13.056 -1.918 1.00 16.56 C ANISOU 1318 CD1 LEU B 55 2363 2498 1430 90 -305 396 C ATOM 1319 CD2 LEU A 55 15.341 13.581 0.507 1.00 16.52 C ANISOU 1319 CD2 LEU B 55 2415 2477 1384 -2 -25 -4 C ATOM 1320 N HIS A 56 17.511 10.883 -3.560 1.00 16.88 N ANISOU 1320 N HIS B 56 2448 2443 1521 -20 20 271 N ATOM 1321 CA HIS A 56 18.624 11.136 -4.461 1.00 18.95 C ANISOU 1321 CA HIS B 56 2588 2611 2001 -17 82 136 C ATOM 1322 C HIS A 56 18.443 12.563 -4.964 1.00 19.15 C ANISOU 1322 C HIS B 56 2700 2692 1881 -4 226 157 C ATOM 1323 O HIS A 56 17.400 13.177 -4.775 1.00 19.98 O ANISOU 1323 O HIS B 56 2726 2762 2104 18 -202 326 O ATOM 1324 CB HIS A 56 18.603 10.159 -5.661 1.00 21.26 C ANISOU 1324 CB HIS B 56 2961 2972 2145 22 143 150 C ATOM 1325 CG HIS A 56 18.864 8.746 -5.267 1.00 24.28 C ANISOU 1325 CG HIS B 56 3446 3019 2759 124 122 -227 C ATOM 1326 ND1 HIS A 56 20.120 8.170 -5.325 1.00 29.42 N ANISOU 1326 ND1 HIS B 56 3839 3651 3689 238 294 156 N ATOM 1327 CD2 HIS A 56 18.044 7.811 -4.737 1.00 28.56 C ANISOU 1327 CD2 HIS B 56 3818 3499 3531 104 311 66 C ATOM 1328 CE1 HIS A 56 20.046 6.923 -4.886 1.00 28.26 C ANISOU 1328 CE1 HIS B 56 3845 3535 3354 159 99 132 C ATOM 1329 NE2 HIS A 56 18.797 6.679 -4.531 1.00 27.62 N ANISOU 1329 NE2 HIS B 56 3866 3419 3209 287 186 70 N ATOM 1330 N GLY A 57 19.487 13.087 -5.562 1.00 19.40 N ANISOU 1330 N GLY B 57 2520 2608 2243 -218 62 206 N ATOM 1331 CA GLY A 57 19.391 14.364 -6.267 1.00 19.25 C ANISOU 1331 CA GLY B 57 2592 2586 2134 -64 31 253 C ATOM 1332 C GLY A 57 19.347 15.590 -5.398 1.00 19.53 C ANISOU 1332 C GLY B 57 2538 2610 2270 -91 29 301 C ATOM 1333 O GLY A 57 18.958 16.656 -5.834 1.00 20.78 O ANISOU 1333 O GLY B 57 2847 2699 2350 141 -258 515 O ATOM 1334 N LEU A 58 19.746 15.461 -4.144 1.00 18.51 N ANISOU 1334 N LEU B 58 2324 2598 2109 -85 -127 318 N ATOM 1335 CA LEU A 58 19.705 16.604 -3.241 1.00 17.62 C ANISOU 1335 CA LEU B 58 2190 2408 2095 86 -8 329 C ATOM 1336 C LEU A 58 20.612 17.747 -3.637 1.00 17.26 C ANISOU 1336 C LEU B 58 2155 2446 1954 131 -79 355 C ATOM 1337 O LEU A 58 20.224 18.919 -3.529 1.00 18.75 O ANISOU 1337 O LEU B 58 2526 2512 2086 -7 207 438 O ATOM 1338 CB LEU A 58 20.000 16.194 -1.791 1.00 18.15 C ANISOU 1338 CB LEU B 58 2196 2577 2121 11 -112 293 C ATOM 1339 CG LEU A 58 18.836 15.455 -1.130 1.00 16.34 C ANISOU 1339 CG LEU B 58 2135 2261 1810 -78 -100 215 C ATOM 1340 CD1 LEU A 58 19.346 14.681 0.081 1.00 18.71 C ANISOU 1340 CD1 LEU B 58 2472 2791 1844 -233 -184 502 C ATOM 1341 CD2 LEU A 58 17.687 16.382 -0.826 1.00 19.43 C ANISOU 1341 CD2 LEU B 58 2579 2215 2588 -136 340 183 C ATOM 1342 N THR A 59 21.798 17.413 -4.136 1.00 17.26 N ANISOU 1342 N THR B 59 1970 2435 2153 149 -121 486 N ATOM 1343 CA THR A 59 22.792 18.430 -4.422 1.00 18.03 C ANISOU 1343 CA THR B 59 2279 2443 2126 23 -11 351 C ATOM 1344 C THR A 59 23.741 17.959 -5.494 1.00 18.78 C ANISOU 1344 C THR B 59 2303 2579 2254 -97 33 323 C ATOM 1345 O THR A 59 23.593 16.892 -6.057 1.00 18.89 O ANISOU 1345 O THR B 59 2425 2704 2045 -44 257 354 O ATOM 1346 CB THR A 59 23.547 18.829 -3.121 1.00 17.38 C ANISOU 1346 CB THR B 59 2120 2394 2089 -75 83 298 C ATOM 1347 OG1 THR A 59 24.332 20.033 -3.326 1.00 19.05 O ANISOU 1347 OG1 THR B 59 2517 2664 2055 -189 -124 241 O ATOM 1348 CG2 THR A 59 24.406 17.673 -2.581 1.00 18.52 C ANISOU 1348 CG2 THR B 59 2229 2709 2096 105 -97 342 C ATOM 1349 N THR A 60 24.715 18.803 -5.802 1.00 19.28 N ANISOU 1349 N THR B 60 2363 2646 2316 -201 159 266 N ATOM 1350 CA THR A 60 25.710 18.496 -6.824 1.00 20.10 C ANISOU 1350 CA THR B 60 2524 2730 2383 -154 134 303 C ATOM 1351 C THR A 60 27.061 18.636 -6.186 1.00 19.55 C ANISOU 1351 C THR B 60 2513 2596 2316 -159 161 332 C ATOM 1352 O THR A 60 27.201 19.277 -5.133 1.00 18.24 O ANISOU 1352 O THR B 60 2447 2359 2124 -246 135 637 O ATOM 1353 CB THR A 60 25.629 19.444 -7.981 1.00 20.64 C ANISOU 1353 CB THR B 60 2407 2962 2471 -91 -36 300 C ATOM 1354 OG1 THR A 60 25.883 20.786 -7.519 1.00 23.39 O ANISOU 1354 OG1 THR B 60 2856 3094 2937 -140 -25 869 O ATOM 1355 CG2 THR A 60 24.248 19.304 -8.716 1.00 22.58 C ANISOU 1355 CG2 THR B 60 2751 3271 2555 -184 -265 433 C ATOM 1356 N GLU A 61 28.078 18.074 -6.820 1.00 21.22 N ANISOU 1356 N GLU B 61 2629 2824 2609 -100 168 246 N ATOM 1357 CA GLU A 61 29.442 18.236 -6.322 1.00 23.21 C ANISOU 1357 CA GLU B 61 2811 3070 2938 -110 147 173 C ATOM 1358 C GLU A 61 29.834 19.718 -6.215 1.00 21.77 C ANISOU 1358 C GLU B 61 2555 2924 2791 -102 190 160 C ATOM 1359 O GLU A 61 30.457 20.113 -5.259 1.00 20.91 O ANISOU 1359 O GLU B 61 2331 2954 2660 -289 218 268 O ATOM 1360 CB GLU A 61 30.434 17.494 -7.196 1.00 25.25 C ANISOU 1360 CB GLU B 61 3107 3202 3283 -49 209 109 C ATOM 1361 CG GLU A 61 30.327 15.991 -7.059 1.00 28.60 C ANISOU 1361 CG GLU B 61 3549 3606 3710 -51 274 17 C ATOM 1362 CD GLU A 61 31.550 15.271 -7.572 1.00 31.59 C ANISOU 1362 CD GLU B 61 3917 4019 4065 152 187 77 C ATOM 1363 OE1 GLU A 61 32.071 15.702 -8.638 1.00 37.91 O ANISOU 1363 OE1 GLU B 61 4868 5072 4463 -19 281 94 O ATOM 1364 OE2 GLU A 61 31.973 14.291 -6.885 1.00 40.79 O ANISOU 1364 OE2 GLU B 61 5280 5074 5142 289 -13 320 O ATOM 1365 N GLU A 62 29.443 20.540 -7.173 1.00 20.85 N ANISOU 1365 N GLU B 62 2380 2878 2664 -115 163 167 N ATOM 1366 CA GLU A 62 29.827 21.938 -7.139 1.00 23.01 C ANISOU 1366 CA GLU B 62 2732 3039 2970 -101 96 127 C ATOM 1367 C GLU A 62 29.256 22.641 -5.904 1.00 20.81 C ANISOU 1367 C GLU B 62 2334 2854 2716 -116 188 227 C ATOM 1368 O GLU A 62 29.924 23.444 -5.262 1.00 22.10 O ANISOU 1368 O GLU B 62 2305 3112 2979 -287 265 217 O ATOM 1369 CB GLU A 62 29.366 22.626 -8.432 1.00 24.99 C ANISOU 1369 CB GLU B 62 3087 3166 3242 -40 54 157 C ATOM 1370 CG GLU A 62 30.316 22.418 -9.669 1.00 30.56 C ANISOU 1370 CG GLU B 62 3829 3938 3842 -29 168 108 C ATOM 1371 CD GLU A 62 30.353 23.622 -10.631 1.00 31.58 C ANISOU 1371 CD GLU B 62 3982 4120 3898 -82 217 200 C ATOM 1372 OE1 GLU A 62 29.479 24.536 -10.518 1.00 41.25 O ANISOU 1372 OE1 GLU B 62 5224 5064 5385 245 191 140 O ATOM 1373 OE2 GLU A 62 31.242 23.629 -11.534 1.00 36.71 O ANISOU 1373 OE2 GLU B 62 4367 5362 4218 -111 612 180 O ATOM 1374 N GLU A 63 28.002 22.356 -5.566 1.00 20.05 N ANISOU 1374 N GLU B 63 2298 2503 2815 -110 6 429 N ATOM 1375 CA GLU A 63 27.331 23.045 -4.474 1.00 20.16 C ANISOU 1375 CA GLU B 63 2346 2585 2728 -62 32 360 C ATOM 1376 C GLU A 63 27.699 22.516 -3.073 1.00 17.41 C ANISOU 1376 C GLU B 63 1876 2284 2453 -143 88 333 C ATOM 1377 O GLU A 63 27.676 23.237 -2.089 1.00 18.86 O ANISOU 1377 O GLU B 63 2055 2271 2838 -90 416 514 O ATOM 1378 CB GLU A 63 25.804 22.914 -4.671 1.00 20.76 C ANISOU 1378 CB GLU B 63 2329 2794 2765 -1 -26 377 C ATOM 1379 CG GLU A 63 25.226 23.497 -6.008 1.00 23.84 C ANISOU 1379 CG GLU B 63 2803 3196 3058 73 68 384 C ATOM 1380 CD GLU A 63 23.793 23.008 -6.377 1.00 26.41 C ANISOU 1380 CD GLU B 63 3110 3326 3596 -3 -111 289 C ATOM 1381 OE1 GLU A 63 23.512 21.795 -6.613 1.00 32.52 O ANISOU 1381 OE1 GLU B 63 3759 4015 4582 -126 -291 -59 O ATOM 1382 OE2 GLU A 63 22.917 23.892 -6.463 1.00 35.54 O ANISOU 1382 OE2 GLU B 63 4045 4481 4974 372 26 227 O ATOM 1383 N PHE A 64 28.104 21.252 -3.006 1.00 16.31 N ANISOU 1383 N PHE B 64 1772 2173 2252 -133 191 306 N ATOM 1384 CA PHE A 64 28.322 20.563 -1.718 1.00 16.65 C ANISOU 1384 CA PHE B 64 1870 2353 2100 -34 -1 248 C ATOM 1385 C PHE A 64 29.747 20.741 -1.222 1.00 15.17 C ANISOU 1385 C PHE B 64 1807 2130 1825 20 -93 173 C ATOM 1386 O PHE A 64 30.541 19.787 -1.139 1.00 16.79 O ANISOU 1386 O PHE B 64 1989 2236 2151 25 46 405 O ATOM 1387 CB PHE A 64 27.957 19.085 -1.839 1.00 15.97 C ANISOU 1387 CB PHE B 64 1877 2355 1835 -81 48 184 C ATOM 1388 CG PHE A 64 27.825 18.349 -0.520 1.00 15.22 C ANISOU 1388 CG PHE B 64 1875 2025 1881 -42 -174 112 C ATOM 1389 CD1 PHE A 64 26.970 18.790 0.441 1.00 16.93 C ANISOU 1389 CD1 PHE B 64 2184 2068 2180 2 -12 293 C ATOM 1390 CD2 PHE A 64 28.540 17.183 -0.278 1.00 19.21 C ANISOU 1390 CD2 PHE B 64 2590 2333 2374 -67 425 451 C ATOM 1391 CE1 PHE A 64 26.829 18.037 1.620 1.00 16.60 C ANISOU 1391 CE1 PHE B 64 2168 2251 1886 -165 96 124 C ATOM 1392 CE2 PHE A 64 28.396 16.489 0.895 1.00 17.94 C ANISOU 1392 CE2 PHE B 64 2456 2354 2007 348 24 420 C ATOM 1393 CZ PHE A 64 27.528 16.928 1.813 1.00 18.15 C ANISOU 1393 CZ PHE B 64 2391 2438 2067 -159 149 314 C ATOM 1394 N VAL A 65 30.037 21.972 -0.852 1.00 13.34 N ANISOU 1394 N VAL B 65 1418 1731 1919 -74 20 506 N ATOM 1395 CA VAL A 65 31.350 22.353 -0.396 1.00 14.30 C ANISOU 1395 CA VAL B 65 1711 1807 1914 -91 -90 324 C ATOM 1396 C VAL A 65 31.572 21.945 1.043 1.00 13.91 C ANISOU 1396 C VAL B 65 1624 1959 1700 -66 32 342 C ATOM 1397 O VAL A 65 30.640 21.598 1.738 1.00 13.32 O ANISOU 1397 O VAL B 65 1526 2025 1507 -248 277 661 O ATOM 1398 CB VAL A 65 31.583 23.853 -0.542 1.00 13.78 C ANISOU 1398 CB VAL B 65 1538 1736 1961 -278 93 583 C ATOM 1399 CG1 VAL A 65 31.574 24.281 -2.063 1.00 16.79 C ANISOU 1399 CG1 VAL B 65 2308 1821 2250 -341 14 892 C ATOM 1400 CG2 VAL A 65 30.625 24.704 0.312 1.00 17.51 C ANISOU 1400 CG2 VAL B 65 2439 1680 2531 20 106 429 C ATOM 1401 N GLU A 66 32.797 21.949 1.500 1.00 12.41 N ANISOU 1401 N GLU B 66 1478 1740 1496 -51 254 477 N ATOM 1402 CA GLU A 66 33.097 21.622 2.869 1.00 13.05 C ANISOU 1402 CA GLU B 66 1612 1762 1582 -66 86 488 C ATOM 1403 C GLU A 66 32.312 22.518 3.796 1.00 14.13 C ANISOU 1403 C GLU B 66 1762 1863 1741 -150 112 370 C ATOM 1404 O GLU A 66 32.099 23.702 3.568 1.00 15.79 O ANISOU 1404 O GLU B 66 2080 2062 1856 -239 262 580 O ATOM 1405 CB GLU A 66 34.616 21.796 3.175 1.00 13.84 C ANISOU 1405 CB GLU B 66 1803 1845 1609 -19 22 651 C ATOM 1406 CG GLU A 66 35.478 20.799 2.493 1.00 14.45 C ANISOU 1406 CG GLU B 66 1793 2122 1574 24 90 460 C ATOM 1407 CD GLU A 66 36.939 20.869 2.857 1.00 15.27 C ANISOU 1407 CD GLU B 66 1788 2098 1913 88 -12 477 C ATOM 1408 OE1 GLU A 66 37.560 21.968 2.678 1.00 16.05 O ANISOU 1408 OE1 GLU B 66 1946 2280 1870 103 -63 630 O ATOM 1409 OE2 GLU A 66 37.495 19.785 3.209 1.00 20.24 O ANISOU 1409 OE2 GLU B 66 2707 2243 2741 -9 120 489 O ATOM 1410 N GLY A 67 31.972 21.947 4.926 1.00 14.23 N ANISOU 1410 N GLY B 67 1858 1802 1746 -240 323 342 N ATOM 1411 CA GLY A 67 31.226 22.671 5.961 1.00 14.64 C ANISOU 1411 CA GLY B 67 1863 1898 1800 -314 188 176 C ATOM 1412 C GLY A 67 30.419 21.722 6.812 1.00 13.74 C ANISOU 1412 C GLY B 67 1717 1855 1649 -293 201 159 C ATOM 1413 O GLY A 67 30.512 20.550 6.635 1.00 14.28 O ANISOU 1413 O GLY B 67 1902 1901 1622 -47 333 461 O ATOM 1414 N ILE A 68 29.646 22.282 7.716 1.00 14.35 N ANISOU 1414 N ILE B 68 1752 1934 1764 -387 233 98 N ATOM 1415 CA ILE A 68 28.802 21.493 8.613 1.00 13.09 C ANISOU 1415 CA ILE B 68 1687 1655 1631 -187 79 283 C ATOM 1416 C ILE A 68 27.382 21.501 8.047 1.00 12.65 C ANISOU 1416 C ILE B 68 1749 1533 1522 -152 95 287 C ATOM 1417 O ILE A 68 26.830 22.559 7.719 1.00 13.36 O ANISOU 1417 O ILE B 68 1865 1437 1773 -25 -156 273 O ATOM 1418 CB ILE A 68 28.838 22.087 10.028 1.00 14.18 C ANISOU 1418 CB ILE B 68 1739 1932 1717 -190 -108 238 C ATOM 1419 CG1 ILE A 68 30.267 22.037 10.592 1.00 17.27 C ANISOU 1419 CG1 ILE B 68 1842 2694 2023 23 -19 84 C ATOM 1420 CG2 ILE A 68 27.902 21.315 10.959 1.00 14.95 C ANISOU 1420 CG2 ILE B 68 1790 2143 1744 -357 109 316 C ATOM 1421 CD1 ILE A 68 30.441 22.599 12.008 1.00 19.44 C ANISOU 1421 CD1 ILE B 68 2295 2781 2310 -75 -160 -203 C ATOM 1422 N TYR A 69 26.814 20.294 7.926 1.00 11.34 N ANISOU 1422 N TYR B 69 1287 1435 1586 -162 0 542 N ATOM 1423 CA TYR A 69 25.487 20.102 7.406 1.00 11.09 C ANISOU 1423 CA TYR B 69 1330 1425 1455 -163 112 399 C ATOM 1424 C TYR A 69 24.652 19.368 8.480 1.00 10.15 C ANISOU 1424 C TYR B 69 1297 1466 1090 -131 36 518 C ATOM 1425 O TYR A 69 25.149 18.617 9.308 1.00 12.24 O ANISOU 1425 O TYR B 69 1307 1813 1531 88 -8 468 O ATOM 1426 CB TYR A 69 25.526 19.245 6.143 1.00 12.00 C ANISOU 1426 CB TYR B 69 1295 1595 1668 -92 -42 368 C ATOM 1427 CG TYR A 69 26.190 19.963 4.995 1.00 13.22 C ANISOU 1427 CG TYR B 69 1506 1773 1744 -40 -41 351 C ATOM 1428 CD1 TYR A 69 27.565 19.987 4.856 1.00 11.16 C ANISOU 1428 CD1 TYR B 69 1266 1764 1208 -68 341 455 C ATOM 1429 CD2 TYR A 69 25.451 20.656 4.042 1.00 12.72 C ANISOU 1429 CD2 TYR B 69 1400 2195 1237 -149 -42 419 C ATOM 1430 CE1 TYR A 69 28.200 20.677 3.762 1.00 12.30 C ANISOU 1430 CE1 TYR B 69 1059 2038 1575 -83 325 573 C ATOM 1431 CE2 TYR A 69 26.046 21.318 2.975 1.00 13.26 C ANISOU 1431 CE2 TYR B 69 1362 2074 1598 8 195 412 C ATOM 1432 CZ TYR A 69 27.385 21.301 2.861 1.00 12.93 C ANISOU 1432 CZ TYR B 69 1352 1882 1676 -90 155 506 C ATOM 1433 OH TYR A 69 27.992 21.964 1.792 1.00 13.09 O ANISOU 1433 OH TYR B 69 1589 1957 1425 -10 321 755 O ATOM 1434 N LYS A 70 23.348 19.616 8.377 1.00 10.84 N ANISOU 1434 N LYS B 70 1298 1396 1425 27 -56 406 N ATOM 1435 CA ALYS A 70 22.381 18.912 9.189 0.50 11.48 C ANISOU 1435 CA ALYS B 70 1413 1528 1420 -43 -57 269 C ATOM 1436 C LYS A 70 21.292 18.349 8.264 1.00 10.23 C ANISOU 1436 C LYS B 70 1262 1330 1292 45 -85 433 C ATOM 1437 O LYS A 70 20.746 19.050 7.418 1.00 12.29 O ANISOU 1437 O LYS B 70 1535 1570 1565 -52 -215 593 O ATOM 1438 CB ALYS A 70 21.807 19.816 10.296 0.50 12.17 C ANISOU 1438 CB ALYS B 70 1637 1588 1397 -76 180 307 C ATOM 1439 CG ALYS A 70 20.620 19.206 11.102 0.50 12.65 C ANISOU 1439 CG ALYS B 70 1557 1872 1377 48 108 328 C ATOM 1440 CD ALYS A 70 20.065 20.168 12.158 0.50 12.87 C ANISOU 1440 CD ALYS B 70 1630 1791 1466 105 -224 134 C ATOM 1441 CE ALYS A 70 19.608 21.504 11.648 0.50 15.69 C ANISOU 1441 CE ALYS B 70 2100 1897 1964 56 -33 -39 C ATOM 1442 NZ ALYS A 70 18.716 22.173 12.659 0.50 18.95 N ANISOU 1442 NZ ALYS B 70 2504 2330 2363 176 215 47 N ATOM 1443 N VAL A 71 21.039 17.049 8.480 1.00 11.17 N ANISOU 1443 N VAL B 71 1388 1421 1435 -133 -92 343 N ATOM 1444 CA VAL A 71 19.984 16.321 7.828 1.00 11.39 C ANISOU 1444 CA VAL B 71 1462 1679 1183 -114 -195 354 C ATOM 1445 C VAL A 71 18.900 16.080 8.866 1.00 11.23 C ANISOU 1445 C VAL B 71 1297 1644 1324 -45 -248 411 C ATOM 1446 O VAL A 71 19.160 15.402 9.835 1.00 12.53 O ANISOU 1446 O VAL B 71 1322 2007 1431 -154 -156 634 O ATOM 1447 CB VAL A 71 20.480 15.022 7.227 1.00 12.35 C ANISOU 1447 CB VAL B 71 1860 1733 1099 -87 -198 450 C ATOM 1448 CG1 VAL A 71 19.318 14.215 6.575 1.00 15.40 C ANISOU 1448 CG1 VAL B 71 2045 2342 1464 -223 -253 93 C ATOM 1449 CG2 VAL A 71 21.607 15.235 6.181 1.00 14.70 C ANISOU 1449 CG2 VAL B 71 1669 2131 1783 -24 -5 267 C ATOM 1450 N GLU A 72 17.713 16.670 8.654 1.00 11.73 N ANISOU 1450 N GLU B 72 1336 1682 1439 -101 -6 334 N ATOM 1451 CA GLU A 72 16.569 16.470 9.547 1.00 12.33 C ANISOU 1451 CA GLU B 72 1548 1701 1433 -126 -66 231 C ATOM 1452 C GLU A 72 15.545 15.592 8.819 1.00 10.97 C ANISOU 1452 C GLU B 72 1460 1574 1131 -203 -107 290 C ATOM 1453 O GLU A 72 15.121 15.867 7.704 1.00 14.58 O ANISOU 1453 O GLU B 72 1869 1898 1772 -350 -161 478 O ATOM 1454 CB GLU A 72 15.974 17.809 9.851 1.00 15.12 C ANISOU 1454 CB GLU B 72 1938 1935 1871 -132 -39 108 C ATOM 1455 CG GLU A 72 14.848 17.829 10.816 1.00 17.10 C ANISOU 1455 CG GLU B 72 2223 2126 2145 84 44 156 C ATOM 1456 CD GLU A 72 14.725 19.223 11.452 1.00 21.67 C ANISOU 1456 CD GLU B 72 2991 2702 2538 293 -60 0 C ATOM 1457 OE1 GLU A 72 14.313 20.118 10.732 1.00 29.69 O ANISOU 1457 OE1 GLU B 72 3855 3893 3529 452 -15 313 O ATOM 1458 OE2 GLU A 72 15.137 19.406 12.617 1.00 33.75 O ANISOU 1458 OE2 GLU B 72 4889 4407 3526 -82 -282 -176 O ATOM 1459 N ILE A 73 15.201 14.510 9.540 1.00 10.97 N ANISOU 1459 N ILE B 73 1607 1544 1015 -319 47 174 N ATOM 1460 CA ILE A 73 14.309 13.491 8.982 1.00 11.91 C ANISOU 1460 CA ILE B 73 1689 1559 1275 -153 122 142 C ATOM 1461 C ILE A 73 13.018 13.584 9.794 1.00 11.22 C ANISOU 1461 C ILE B 73 1534 1447 1282 -172 143 27 C ATOM 1462 O ILE A 73 13.023 13.444 11.034 1.00 11.93 O ANISOU 1462 O ILE B 73 1737 1692 1103 -257 204 -25 O ATOM 1463 CB ILE A 73 14.917 12.080 9.059 1.00 11.44 C ANISOU 1463 CB ILE B 73 1721 1603 1022 -17 254 163 C ATOM 1464 CG1 ILE A 73 16.256 12.063 8.346 1.00 11.86 C ANISOU 1464 CG1 ILE B 73 1909 1507 1089 -22 199 254 C ATOM 1465 CG2 ILE A 73 13.972 11.039 8.507 1.00 12.99 C ANISOU 1465 CG2 ILE B 73 2107 1682 1145 -114 280 -75 C ATOM 1466 CD1 ILE A 73 17.085 10.796 8.494 1.00 15.00 C ANISOU 1466 CD1 ILE B 73 2177 1902 1618 55 247 214 C ATOM 1467 N ASP A 74 11.902 13.782 9.112 1.00 12.14 N ANISOU 1467 N ASP B 74 1533 1665 1415 -48 166 176 N ATOM 1468 CA AASP A 74 10.600 13.998 9.792 0.50 12.82 C ANISOU 1468 CA AASP B 74 1625 1638 1606 -50 202 128 C ATOM 1469 C ASP A 74 9.972 12.681 10.194 1.00 12.80 C ANISOU 1469 C ASP B 74 1466 1721 1676 -74 214 77 C ATOM 1470 O ASP A 74 8.998 12.248 9.625 1.00 13.71 O ANISOU 1470 O ASP B 74 1705 1911 1590 -67 204 305 O ATOM 1471 CB AASP A 74 9.600 14.778 8.916 0.50 13.85 C ANISOU 1471 CB AASP B 74 1740 1643 1876 1 158 184 C ATOM 1472 CG AASP A 74 8.290 15.094 9.655 0.50 14.20 C ANISOU 1472 CG AASP B 74 1598 1719 2079 -87 29 259 C ATOM 1473 OD1AASP A 74 8.165 14.725 10.841 0.50 14.21 O ANISOU 1473 OD1AASP B 74 1481 1370 2547 -2 499 62 O ATOM 1474 OD2AASP A 74 7.380 15.647 9.001 0.50 18.69 O ANISOU 1474 OD2AASP B 74 1587 2480 3032 122 465 756 O ATOM 1475 N THR A 75 10.571 12.053 11.201 1.00 11.60 N ANISOU 1475 N THR B 75 1529 1505 1372 -144 213 176 N ATOM 1476 CA THR A 75 10.145 10.772 11.689 1.00 11.89 C ANISOU 1476 CA THR B 75 1491 1522 1503 -54 282 19 C ATOM 1477 C THR A 75 8.749 10.809 12.352 1.00 10.81 C ANISOU 1477 C THR B 75 1295 1426 1387 -54 251 -10 C ATOM 1478 O THR A 75 8.002 9.856 12.251 1.00 11.66 O ANISOU 1478 O THR B 75 1637 1621 1172 -80 0 -78 O ATOM 1479 CB THR A 75 11.205 10.229 12.665 1.00 11.34 C ANISOU 1479 CB THR B 75 1548 1215 1546 -178 348 13 C ATOM 1480 OG1 THR A 75 11.342 11.103 13.762 1.00 11.52 O ANISOU 1480 OG1 THR B 75 1559 1387 1430 -91 6 -89 O ATOM 1481 CG2 THR A 75 12.554 10.016 11.985 1.00 13.35 C ANISOU 1481 CG2 THR B 75 1446 1775 1848 210 418 27 C ATOM 1482 N LYS A 76 8.443 11.910 13.010 1.00 12.68 N ANISOU 1482 N LYS B 76 1475 1586 1757 -155 335 -107 N ATOM 1483 CA LYS A 76 7.191 12.010 13.749 1.00 13.52 C ANISOU 1483 CA LYS B 76 1593 1680 1861 -60 307 -89 C ATOM 1484 C LYS A 76 5.998 11.885 12.773 1.00 13.51 C ANISOU 1484 C LYS B 76 1625 1716 1792 -12 320 -44 C ATOM 1485 O LYS A 76 5.039 11.131 13.030 1.00 13.72 O ANISOU 1485 O LYS B 76 1515 1699 1996 -34 253 -82 O ATOM 1486 CB LYS A 76 7.130 13.285 14.560 1.00 13.66 C ANISOU 1486 CB LYS B 76 1600 1683 1906 -260 342 -61 C ATOM 1487 CG LYS A 76 5.904 13.360 15.474 1.00 16.48 C ANISOU 1487 CG LYS B 76 1849 2137 2276 -49 505 -202 C ATOM 1488 CD LYS A 76 5.969 14.628 16.317 1.00 17.88 C ANISOU 1488 CD LYS B 76 2022 2419 2352 138 335 -376 C ATOM 1489 CE LYS A 76 4.885 14.693 17.372 1.00 23.14 C ANISOU 1489 CE LYS B 76 2655 3167 2969 80 356 -268 C ATOM 1490 NZ LYS A 76 5.021 15.885 18.266 1.00 26.36 N ANISOU 1490 NZ LYS B 76 3034 3308 3671 176 254 -647 N ATOM 1491 N SER A 77 6.061 12.591 11.627 1.00 14.65 N ANISOU 1491 N SER B 77 1715 1811 2037 50 212 44 N ATOM 1492 CA SER A 77 4.961 12.509 10.642 1.00 14.70 C ANISOU 1492 CA SER B 77 1665 2058 1860 109 222 140 C ATOM 1493 C SER A 77 4.854 11.138 10.070 1.00 14.81 C ANISOU 1493 C SER B 77 1558 2257 1811 106 167 163 C ATOM 1494 O SER A 77 3.751 10.668 9.765 1.00 15.97 O ANISOU 1494 O SER B 77 1355 2614 2096 96 20 -151 O ATOM 1495 CB SER A 77 5.125 13.514 9.539 1.00 17.97 C ANISOU 1495 CB SER B 77 2063 2495 2267 37 236 168 C ATOM 1496 OG SER A 77 5.090 14.791 10.083 1.00 21.73 O ANISOU 1496 OG SER B 77 2556 2353 3346 380 281 575 O ATOM 1497 N TYR A 78 6.001 10.510 9.833 1.00 14.32 N ANISOU 1497 N TYR B 78 1456 2237 1745 165 255 37 N ATOM 1498 CA TYR A 78 6.012 9.144 9.321 1.00 14.19 C ANISOU 1498 CA TYR B 78 1499 2220 1670 85 95 -129 C ATOM 1499 C TYR A 78 5.206 8.183 10.210 1.00 13.73 C ANISOU 1499 C TYR B 78 1334 2117 1765 35 139 -238 C ATOM 1500 O TYR A 78 4.332 7.440 9.768 1.00 15.65 O ANISOU 1500 O TYR B 78 1583 2424 1936 -77 -3 -320 O ATOM 1501 CB TYR A 78 7.452 8.650 9.159 1.00 13.85 C ANISOU 1501 CB TYR B 78 1368 2198 1693 201 -16 -121 C ATOM 1502 CG TYR A 78 7.532 7.228 8.658 1.00 13.32 C ANISOU 1502 CG TYR B 78 1285 2177 1599 136 -23 -18 C ATOM 1503 CD1 TYR A 78 7.253 6.936 7.356 1.00 13.50 C ANISOU 1503 CD1 TYR B 78 1644 2110 1373 431 -157 99 C ATOM 1504 CD2 TYR A 78 7.852 6.174 9.523 1.00 12.30 C ANISOU 1504 CD2 TYR B 78 1303 2052 1319 -10 -31 94 C ATOM 1505 CE1 TYR A 78 7.304 5.654 6.900 1.00 14.11 C ANISOU 1505 CE1 TYR B 78 1803 2209 1347 441 -19 -53 C ATOM 1506 CE2 TYR A 78 7.903 4.906 9.084 1.00 13.46 C ANISOU 1506 CE2 TYR B 78 1784 1957 1370 389 -102 196 C ATOM 1507 CZ TYR A 78 7.616 4.613 7.753 1.00 13.50 C ANISOU 1507 CZ TYR B 78 1568 1999 1561 233 -48 -7 C ATOM 1508 OH TYR A 78 7.647 3.311 7.251 1.00 15.21 O ANISOU 1508 OH TYR B 78 1638 2457 1680 264 -77 -6 O ATOM 1509 N TRP A 79 5.525 8.175 11.508 1.00 12.41 N ANISOU 1509 N TRP B 79 1367 1825 1522 25 133 -170 N ATOM 1510 CA TRP A 79 4.863 7.263 12.410 1.00 12.62 C ANISOU 1510 CA TRP B 79 1208 1828 1758 18 132 -113 C ATOM 1511 C TRP A 79 3.380 7.619 12.606 1.00 13.90 C ANISOU 1511 C TRP B 79 1259 1918 2101 -74 211 -179 C ATOM 1512 O TRP A 79 2.501 6.755 12.628 1.00 15.24 O ANISOU 1512 O TRP B 79 1332 2162 2294 -126 353 -184 O ATOM 1513 CB TRP A 79 5.577 7.221 13.767 1.00 11.80 C ANISOU 1513 CB TRP B 79 1395 1571 1515 -5 133 -140 C ATOM 1514 CG TRP A 79 6.910 6.611 13.704 1.00 10.84 C ANISOU 1514 CG TRP B 79 1407 1492 1220 -49 122 -139 C ATOM 1515 CD1 TRP A 79 8.106 7.220 13.955 1.00 11.71 C ANISOU 1515 CD1 TRP B 79 1493 1376 1578 0 -82 -117 C ATOM 1516 CD2 TRP A 79 7.215 5.262 13.366 1.00 10.77 C ANISOU 1516 CD2 TRP B 79 1282 1606 1204 -97 -50 -54 C ATOM 1517 NE1 TRP A 79 9.146 6.339 13.776 1.00 11.62 N ANISOU 1517 NE1 TRP B 79 1388 1569 1455 -196 67 188 N ATOM 1518 CE2 TRP A 79 8.624 5.121 13.413 1.00 10.61 C ANISOU 1518 CE2 TRP B 79 1181 1485 1364 -120 -55 26 C ATOM 1519 CE3 TRP A 79 6.442 4.152 13.019 1.00 12.90 C ANISOU 1519 CE3 TRP B 79 1483 1721 1696 -109 -181 -128 C ATOM 1520 CZ2 TRP A 79 9.259 3.929 13.102 1.00 12.51 C ANISOU 1520 CZ2 TRP B 79 1426 1792 1535 49 -185 -192 C ATOM 1521 CZ3 TRP A 79 7.105 2.978 12.686 1.00 13.58 C ANISOU 1521 CZ3 TRP B 79 1775 1599 1787 -204 -187 -233 C ATOM 1522 CH2 TRP A 79 8.485 2.872 12.767 1.00 12.55 C ANISOU 1522 CH2 TRP B 79 1696 1458 1612 280 31 -297 C ATOM 1523 N LYS A 80 3.091 8.899 12.665 1.00 13.44 N ANISOU 1523 N LYS B 80 1138 1954 2011 37 387 -81 N ATOM 1524 CA LYS A 80 1.697 9.305 12.839 1.00 15.87 C ANISOU 1524 CA LYS B 80 1489 2236 2304 85 245 -35 C ATOM 1525 C LYS A 80 0.855 8.880 11.659 1.00 16.27 C ANISOU 1525 C LYS B 80 1275 2403 2504 117 159 -91 C ATOM 1526 O LYS A 80 -0.316 8.502 11.816 1.00 18.71 O ANISOU 1526 O LYS B 80 1482 2469 3157 37 281 -177 O ATOM 1527 CB LYS A 80 1.621 10.793 13.098 1.00 16.36 C ANISOU 1527 CB LYS B 80 1484 2382 2347 130 260 31 C ATOM 1528 CG LYS A 80 2.094 11.130 14.513 1.00 20.34 C ANISOU 1528 CG LYS B 80 2169 2728 2832 -21 4 -127 C ATOM 1529 CD LYS A 80 1.958 12.566 14.859 1.00 23.15 C ANISOU 1529 CD LYS B 80 2601 3044 3148 64 93 -191 C ATOM 1530 CE LYS A 80 2.506 12.826 16.260 1.00 27.28 C ANISOU 1530 CE LYS B 80 3274 3656 3433 14 -48 -194 C ATOM 1531 NZ LYS A 80 2.194 11.893 17.470 1.00 31.61 N ANISOU 1531 NZ LYS B 80 3584 4049 4377 -124 227 65 N ATOM 1532 N ALA A 81 1.424 8.875 10.465 1.00 16.95 N ANISOU 1532 N ALA B 81 1331 2691 2417 25 -134 -241 N ATOM 1533 CA ALA A 81 0.645 8.444 9.291 1.00 19.00 C ANISOU 1533 CA ALA B 81 1810 2782 2628 -28 -153 -224 C ATOM 1534 C ALA A 81 0.343 6.927 9.310 1.00 21.35 C ANISOU 1534 C ALA B 81 2151 3015 2945 -68 -209 -279 C ATOM 1535 O ALA A 81 -0.611 6.444 8.617 1.00 23.28 O ANISOU 1535 O ALA B 81 2249 3333 3262 -137 -566 -469 O ATOM 1536 CB ALA A 81 1.325 8.887 7.997 1.00 20.73 C ANISOU 1536 CB ALA B 81 2159 2977 2741 -126 -123 -199 C ATOM 1537 N LEU A 82 1.110 6.179 10.074 1.00 20.87 N ANISOU 1537 N LEU B 82 2107 2884 2937 -108 -217 -255 N ATOM 1538 CA LEU A 82 0.925 4.780 10.285 1.00 21.41 C ANISOU 1538 CA LEU B 82 2278 2808 3049 -59 -116 -265 C ATOM 1539 C LEU A 82 0.082 4.509 11.519 1.00 21.03 C ANISOU 1539 C LEU B 82 2212 2711 3065 -110 -36 -195 C ATOM 1540 O LEU A 82 -0.127 3.359 11.949 1.00 22.33 O ANISOU 1540 O LEU B 82 2279 2609 3596 -100 130 -394 O ATOM 1541 CB LEU A 82 2.281 4.119 10.422 1.00 22.70 C ANISOU 1541 CB LEU B 82 2375 2920 3329 -147 -236 -263 C ATOM 1542 CG LEU A 82 3.027 4.002 9.124 1.00 24.24 C ANISOU 1542 CG LEU B 82 2673 3226 3310 -59 -312 -251 C ATOM 1543 CD1 LEU A 82 4.466 3.485 9.346 1.00 24.29 C ANISOU 1543 CD1 LEU B 82 2427 3355 3446 166 -203 -363 C ATOM 1544 CD2 LEU A 82 2.245 2.990 8.250 1.00 25.31 C ANISOU 1544 CD2 LEU B 82 2964 3611 3040 9 -309 -559 C ATOM 1545 N GLY A 83 -0.456 5.576 12.088 1.00 19.31 N ANISOU 1545 N GLY B 83 2013 2437 2885 -119 -126 -184 N ATOM 1546 CA GLY A 83 -1.275 5.465 13.295 1.00 19.96 C ANISOU 1546 CA GLY B 83 2213 2459 2911 -257 37 -67 C ATOM 1547 C GLY A 83 -0.518 5.076 14.542 1.00 18.65 C ANISOU 1547 C GLY B 83 2017 2304 2761 -231 96 -15 C ATOM 1548 O GLY A 83 -1.082 4.492 15.464 1.00 22.00 O ANISOU 1548 O GLY B 83 2250 2666 3442 -334 256 53 O ATOM 1549 N ILE A 84 0.793 5.374 14.589 1.00 19.51 N ANISOU 1549 N ILE B 84 2076 2489 2846 -285 59 6 N ATOM 1550 CA ILE A 84 1.646 5.050 15.714 1.00 18.92 C ANISOU 1550 CA ILE B 84 2111 2452 2623 -285 144 17 C ATOM 1551 C ILE A 84 2.132 6.367 16.349 1.00 19.15 C ANISOU 1551 C ILE B 84 2241 2561 2471 -229 208 58 C ATOM 1552 O ILE A 84 2.538 7.263 15.595 1.00 18.83 O ANISOU 1552 O ILE B 84 1996 2679 2479 -322 256 113 O ATOM 1553 CB ILE A 84 2.838 4.173 15.231 1.00 19.55 C ANISOU 1553 CB ILE B 84 2206 2491 2729 -300 -33 19 C ATOM 1554 CG1 ILE A 84 2.334 2.794 14.753 1.00 21.26 C ANISOU 1554 CG1 ILE B 84 2425 2582 3071 -243 -72 49 C ATOM 1555 CG2 ILE A 84 3.875 4.023 16.324 1.00 20.71 C ANISOU 1555 CG2 ILE B 84 2053 2773 3041 -168 -170 175 C ATOM 1556 CD1 ILE A 84 3.313 2.013 13.869 1.00 21.10 C ANISOU 1556 CD1 ILE B 84 2605 2202 3208 -360 50 -24 C ATOM 1557 N SER A 85 2.092 6.494 17.697 1.00 18.16 N ANISOU 1557 N SER B 85 1853 2762 2285 -266 299 32 N ATOM 1558 CA ASER A 85 2.650 7.629 18.414 0.70 18.16 C ANISOU 1558 CA ASER B 85 2013 2674 2213 -96 251 -21 C ATOM 1559 C SER A 85 4.130 7.400 18.676 1.00 18.29 C ANISOU 1559 C SER B 85 2076 2577 2296 -71 178 -6 C ATOM 1560 O SER A 85 4.508 6.528 19.411 1.00 20.88 O ANISOU 1560 O SER B 85 2211 3023 2699 -407 4 384 O ATOM 1561 CB ASER A 85 1.976 7.828 19.808 0.70 18.12 C ANISOU 1561 CB ASER B 85 1825 2852 2204 -62 320 -68 C ATOM 1562 OG ASER A 85 2.318 9.103 20.394 0.70 18.26 O ANISOU 1562 OG ASER B 85 1771 2925 2241 279 113 -306 O ATOM 1563 N PRO A 86 4.974 8.235 18.140 1.00 15.04 N ANISOU 1563 N PRO B 86 1935 2081 1695 -160 168 -163 N ATOM 1564 CA PRO A 86 6.418 8.004 18.362 1.00 14.81 C ANISOU 1564 CA PRO B 86 1872 1961 1790 -199 138 -156 C ATOM 1565 C PRO A 86 7.001 8.947 19.405 1.00 13.92 C ANISOU 1565 C PRO B 86 1845 1698 1745 -248 224 -249 C ATOM 1566 O PRO A 86 6.329 9.892 19.867 1.00 16.09 O ANISOU 1566 O PRO B 86 2002 2085 2023 27 252 -428 O ATOM 1567 CB PRO A 86 7.015 8.435 17.058 1.00 17.40 C ANISOU 1567 CB PRO B 86 2167 2385 2057 -261 156 -139 C ATOM 1568 CG PRO A 86 6.185 9.546 16.653 1.00 16.51 C ANISOU 1568 CG PRO B 86 2365 2066 1841 -249 173 168 C ATOM 1569 CD PRO A 86 4.744 9.314 17.160 1.00 16.83 C ANISOU 1569 CD PRO B 86 2303 2189 1901 199 204 -182 C ATOM 1570 N PHE A 87 8.247 8.688 19.773 1.00 11.96 N ANISOU 1570 N PHE B 87 1755 1382 1408 -218 334 -111 N ATOM 1571 CA PHE A 87 8.899 9.454 20.815 1.00 11.79 C ANISOU 1571 CA PHE B 87 1739 1461 1280 -202 287 -111 C ATOM 1572 C PHE A 87 9.506 10.754 20.323 1.00 11.72 C ANISOU 1572 C PHE B 87 1826 1272 1353 -110 227 -101 C ATOM 1573 O PHE A 87 9.394 11.797 20.946 1.00 11.39 O ANISOU 1573 O PHE B 87 1844 1181 1300 -59 327 -254 O ATOM 1574 CB PHE A 87 10.031 8.613 21.414 1.00 12.34 C ANISOU 1574 CB PHE B 87 1950 1384 1353 -138 340 -71 C ATOM 1575 CG PHE A 87 10.768 9.301 22.490 1.00 12.82 C ANISOU 1575 CG PHE B 87 2181 1086 1604 -4 166 137 C ATOM 1576 CD1 PHE A 87 10.157 9.497 23.699 1.00 14.52 C ANISOU 1576 CD1 PHE B 87 2444 1457 1617 -4 183 -5 C ATOM 1577 CD2 PHE A 87 12.051 9.761 22.313 1.00 13.87 C ANISOU 1577 CD2 PHE B 87 2374 1268 1625 85 29 -171 C ATOM 1578 CE1 PHE A 87 10.844 10.148 24.720 1.00 14.38 C ANISOU 1578 CE1 PHE B 87 2592 1427 1443 119 182 -85 C ATOM 1579 CE2 PHE A 87 12.718 10.424 23.332 1.00 14.92 C ANISOU 1579 CE2 PHE B 87 2258 1364 2046 -92 -88 12 C ATOM 1580 CZ PHE A 87 12.088 10.590 24.544 1.00 14.24 C ANISOU 1580 CZ PHE B 87 2285 1441 1685 222 -241 -271 C ATOM 1581 N HIS A 88 10.236 10.682 19.212 1.00 10.71 N ANISOU 1581 N HIS B 88 1742 1138 1186 -281 192 -184 N ATOM 1582 CA HIS A 88 11.076 11.808 18.793 1.00 10.85 C ANISOU 1582 CA HIS B 88 1617 1356 1148 -193 163 -132 C ATOM 1583 C HIS A 88 10.273 12.778 17.943 1.00 10.53 C ANISOU 1583 C HIS B 88 1589 1423 989 -141 82 -200 C ATOM 1584 O HIS A 88 9.361 12.425 17.225 1.00 12.05 O ANISOU 1584 O HIS B 88 1839 1373 1365 -222 -10 -121 O ATOM 1585 CB HIS A 88 12.319 11.324 18.018 1.00 11.62 C ANISOU 1585 CB HIS B 88 1594 1435 1382 -229 173 -163 C ATOM 1586 CG HIS A 88 13.191 10.372 18.753 1.00 11.53 C ANISOU 1586 CG HIS B 88 1636 1244 1499 -10 361 -134 C ATOM 1587 ND1 HIS A 88 13.080 8.992 18.647 1.00 12.65 N ANISOU 1587 ND1 HIS B 88 1836 1215 1753 55 366 -284 N ATOM 1588 CD2 HIS A 88 14.189 10.611 19.646 1.00 13.56 C ANISOU 1588 CD2 HIS B 88 1854 1284 2012 -25 162 -39 C ATOM 1589 CE1 HIS A 88 13.969 8.439 19.458 1.00 14.00 C ANISOU 1589 CE1 HIS B 88 1784 1241 2291 -119 110 -496 C ATOM 1590 NE2 HIS A 88 14.659 9.393 20.068 1.00 13.84 N ANISOU 1590 NE2 HIS B 88 1715 1164 2379 66 73 -230 N ATOM 1591 N GLU A 89 10.674 14.049 18.010 1.00 10.73 N ANISOU 1591 N GLU B 89 1578 1364 1135 -92 33 -78 N ATOM 1592 CA GLU A 89 10.097 15.046 17.100 1.00 11.80 C ANISOU 1592 CA GLU B 89 1554 1591 1337 -177 2 14 C ATOM 1593 C GLU A 89 10.625 14.874 15.691 1.00 12.69 C ANISOU 1593 C GLU B 89 1727 1767 1327 -192 -135 120 C ATOM 1594 O GLU A 89 9.927 15.136 14.711 1.00 15.90 O ANISOU 1594 O GLU B 89 1542 2685 1812 -272 -230 401 O ATOM 1595 CB GLU A 89 10.492 16.461 17.563 1.00 13.31 C ANISOU 1595 CB GLU B 89 1852 1580 1622 -67 -95 163 C ATOM 1596 CG GLU A 89 9.785 16.912 18.765 1.00 13.90 C ANISOU 1596 CG GLU B 89 1913 1598 1769 -2 -225 -23 C ATOM 1597 CD GLU A 89 8.300 17.059 18.552 1.00 17.24 C ANISOU 1597 CD GLU B 89 2237 2255 2057 287 43 -275 C ATOM 1598 OE1 GLU A 89 7.878 17.900 17.748 1.00 21.84 O ANISOU 1598 OE1 GLU B 89 2629 3021 2645 108 -73 374 O ATOM 1599 OE2 GLU A 89 7.568 16.288 19.177 1.00 19.92 O ANISOU 1599 OE2 GLU B 89 2337 2472 2759 181 149 -450 O ATOM 1600 N HIS A 90 11.872 14.475 15.565 1.00 11.89 N ANISOU 1600 N HIS B 90 1735 1616 1164 -62 93 116 N ATOM 1601 CA HIS A 90 12.541 14.247 14.264 1.00 12.13 C ANISOU 1601 CA HIS B 90 1677 1699 1230 -266 160 222 C ATOM 1602 C HIS A 90 13.834 13.546 14.596 1.00 12.39 C ANISOU 1602 C HIS B 90 1873 1645 1186 -121 39 143 C ATOM 1603 O HIS A 90 14.175 13.424 15.754 1.00 15.01 O ANISOU 1603 O HIS B 90 2023 2486 1194 112 52 84 O ATOM 1604 CB HIS A 90 12.772 15.539 13.460 1.00 15.76 C ANISOU 1604 CB HIS B 90 2275 2192 1521 -118 195 305 C ATOM 1605 CG HIS A 90 13.337 16.660 14.219 1.00 19.89 C ANISOU 1605 CG HIS B 90 2762 2381 2413 -203 378 336 C ATOM 1606 ND1 HIS A 90 12.612 17.795 14.502 1.00 25.87 N ANISOU 1606 ND1 HIS B 90 3958 2697 3174 -151 211 -23 N ATOM 1607 CD2 HIS A 90 14.567 16.848 14.729 1.00 26.97 C ANISOU 1607 CD2 HIS B 90 3663 3153 3429 -88 -192 -22 C ATOM 1608 CE1 HIS A 90 13.381 18.627 15.188 1.00 25.50 C ANISOU 1608 CE1 HIS B 90 3708 2359 3620 -286 -39 72 C ATOM 1609 NE2 HIS A 90 14.581 18.091 15.305 1.00 27.78 N ANISOU 1609 NE2 HIS B 90 4214 3059 3280 -90 -502 76 N ATOM 1610 N ALA A 91 14.531 13.052 13.584 1.00 12.56 N ANISOU 1610 N ALA B 91 1771 2020 980 -96 172 157 N ATOM 1611 CA ALA A 91 15.871 12.583 13.732 1.00 13.20 C ANISOU 1611 CA ALA B 91 1857 2137 1021 -216 207 438 C ATOM 1612 C ALA A 91 16.759 13.615 12.974 1.00 12.61 C ANISOU 1612 C ALA B 91 1823 2188 779 -226 298 372 C ATOM 1613 O ALA A 91 16.473 14.029 11.906 1.00 20.28 O ANISOU 1613 O ALA B 91 2386 3035 2282 -434 -235 236 O ATOM 1614 CB ALA A 91 16.036 11.218 13.087 1.00 15.24 C ANISOU 1614 CB ALA B 91 2084 2217 1487 56 297 289 C ATOM 1615 N GLU A 92 17.845 13.945 13.638 1.00 16.31 N ANISOU 1615 N GLU B 92 1852 2740 1604 -230 163 392 N ATOM 1616 CA GLU A 92 18.810 14.935 13.138 1.00 16.37 C ANISOU 1616 CA GLU B 92 1895 2600 1725 -84 116 231 C ATOM 1617 C GLU A 92 20.178 14.295 13.023 1.00 15.43 C ANISOU 1617 C GLU B 92 1577 2459 1826 -12 43 475 C ATOM 1618 O GLU A 92 20.593 13.531 13.912 1.00 17.99 O ANISOU 1618 O GLU B 92 1847 3533 1454 124 229 828 O ATOM 1619 CB GLU A 92 18.984 16.034 14.211 1.00 19.89 C ANISOU 1619 CB GLU B 92 2223 2827 2505 -9 9 -8 C ATOM 1620 CG GLU A 92 17.785 16.817 14.574 1.00 25.38 C ANISOU 1620 CG GLU B 92 3278 3255 3109 44 30 -372 C ATOM 1621 CD GLU A 92 18.177 18.222 15.058 1.00 25.61 C ANISOU 1621 CD GLU B 92 3217 3275 3238 -270 111 -39 C ATOM 1622 OE1 GLU A 92 19.369 18.608 14.873 1.00 39.14 O ANISOU 1622 OE1 GLU B 92 4200 5319 5351 -194 107 -60 O ATOM 1623 OE2 GLU A 92 17.314 18.932 15.604 1.00 36.86 O ANISOU 1623 OE2 GLU B 92 4403 4580 5020 145 46 -363 O ATOM 1624 N VAL A 93 20.852 14.520 11.908 1.00 11.63 N ANISOU 1624 N VAL B 93 1401 1682 1334 -2 63 433 N ATOM 1625 CA VAL A 93 22.188 14.011 11.670 1.00 11.09 C ANISOU 1625 CA VAL B 93 1322 1576 1315 -45 -83 299 C ATOM 1626 C VAL A 93 23.061 15.200 11.285 1.00 9.59 C ANISOU 1626 C VAL B 93 1249 1342 1053 -39 -85 321 C ATOM 1627 O VAL A 93 22.784 15.857 10.279 1.00 12.43 O ANISOU 1627 O VAL B 93 1549 1875 1296 -126 -155 658 O ATOM 1628 CB VAL A 93 22.188 12.926 10.550 1.00 11.97 C ANISOU 1628 CB VAL B 93 1503 1616 1428 24 -129 282 C ATOM 1629 CG1 VAL A 93 23.563 12.384 10.379 1.00 15.08 C ANISOU 1629 CG1 VAL B 93 1651 1968 2111 202 -185 79 C ATOM 1630 CG2 VAL A 93 21.126 11.852 10.835 1.00 14.55 C ANISOU 1630 CG2 VAL B 93 1787 1771 1969 -291 -100 274 C ATOM 1631 N VAL A 94 24.076 15.479 12.094 1.00 9.72 N ANISOU 1631 N VAL B 94 1283 1288 1121 21 -31 313 N ATOM 1632 CA VAL A 94 24.911 16.675 11.945 1.00 10.46 C ANISOU 1632 CA VAL B 94 1354 1447 1172 22 156 136 C ATOM 1633 C VAL A 94 26.342 16.220 11.738 1.00 10.40 C ANISOU 1633 C VAL B 94 1262 1433 1257 -65 48 211 C ATOM 1634 O VAL A 94 26.866 15.456 12.538 1.00 10.61 O ANISOU 1634 O VAL B 94 1321 1517 1191 36 -78 377 O ATOM 1635 CB VAL A 94 24.806 17.627 13.152 1.00 11.40 C ANISOU 1635 CB VAL B 94 1356 1657 1317 -34 147 -71 C ATOM 1636 CG1 VAL A 94 25.615 18.870 12.887 1.00 13.52 C ANISOU 1636 CG1 VAL B 94 1761 1661 1713 -189 -93 24 C ATOM 1637 CG2 VAL A 94 23.332 17.938 13.469 1.00 15.04 C ANISOU 1637 CG2 VAL B 94 1574 1890 2250 177 94 -143 C ATOM 1638 N PHE A 95 26.975 16.719 10.687 1.00 10.81 N ANISOU 1638 N PHE B 95 1369 1506 1232 -99 -36 218 N ATOM 1639 CA PHE A 95 28.312 16.219 10.288 1.00 11.08 C ANISOU 1639 CA PHE B 95 1317 1581 1311 20 50 271 C ATOM 1640 C PHE A 95 29.051 17.260 9.485 1.00 11.93 C ANISOU 1640 C PHE B 95 1335 1741 1454 -65 69 222 C ATOM 1641 O PHE A 95 28.452 18.183 8.938 1.00 12.29 O ANISOU 1641 O PHE B 95 1428 1643 1599 -73 220 388 O ATOM 1642 CB PHE A 95 28.194 14.941 9.475 1.00 12.75 C ANISOU 1642 CB PHE B 95 1575 1737 1531 115 80 277 C ATOM 1643 CG PHE A 95 27.506 15.108 8.163 1.00 12.04 C ANISOU 1643 CG PHE B 95 1612 1636 1328 53 138 72 C ATOM 1644 CD1 PHE A 95 26.151 15.086 8.040 1.00 12.92 C ANISOU 1644 CD1 PHE B 95 1794 1711 1403 149 -25 201 C ATOM 1645 CD2 PHE A 95 28.254 15.267 7.005 1.00 14.71 C ANISOU 1645 CD2 PHE B 95 2097 2020 1471 221 -43 219 C ATOM 1646 CE1 PHE A 95 25.551 15.247 6.776 1.00 14.96 C ANISOU 1646 CE1 PHE B 95 1668 1915 2098 150 -150 -87 C ATOM 1647 CE2 PHE A 95 27.665 15.460 5.772 1.00 15.82 C ANISOU 1647 CE2 PHE B 95 2463 2004 1542 -108 12 210 C ATOM 1648 CZ PHE A 95 26.311 15.420 5.686 1.00 16.03 C ANISOU 1648 CZ PHE B 95 2460 2129 1503 -52 -455 -87 C ATOM 1649 N THR A 96 30.363 17.092 9.416 1.00 14.15 N ANISOU 1649 N THR B 96 1389 2212 1772 28 77 542 N ATOM 1650 CA THR A 96 31.198 17.908 8.541 1.00 14.29 C ANISOU 1650 CA THR B 96 1555 2127 1744 -2 135 300 C ATOM 1651 C THR A 96 31.536 17.192 7.247 1.00 14.72 C ANISOU 1651 C THR B 96 1649 2107 1834 81 164 310 C ATOM 1652 O THR A 96 31.964 16.050 7.275 1.00 17.41 O ANISOU 1652 O THR B 96 2303 2352 1957 327 384 510 O ATOM 1653 CB THR A 96 32.496 18.340 9.276 1.00 14.51 C ANISOU 1653 CB THR B 96 1345 2235 1933 -104 327 356 C ATOM 1654 OG1 THR A 96 32.189 19.095 10.426 1.00 16.73 O ANISOU 1654 OG1 THR B 96 1712 2997 1645 -237 19 269 O ATOM 1655 CG2 THR A 96 33.380 19.211 8.359 1.00 16.36 C ANISOU 1655 CG2 THR B 96 1482 2866 1867 -491 427 539 C ATOM 1656 N ALA A 97 31.271 17.851 6.126 1.00 14.16 N ANISOU 1656 N ALA B 97 1680 1924 1777 93 254 360 N ATOM 1657 CA ALA A 97 31.754 17.376 4.831 1.00 15.72 C ANISOU 1657 CA ALA B 97 1874 2107 1992 -52 256 312 C ATOM 1658 C ALA A 97 33.222 17.786 4.709 1.00 16.21 C ANISOU 1658 C ALA B 97 1976 2111 2070 -85 371 460 C ATOM 1659 O ALA A 97 33.565 18.944 4.963 1.00 15.12 O ANISOU 1659 O ALA B 97 2022 2038 1685 85 520 400 O ATOM 1660 CB ALA A 97 30.969 17.963 3.661 1.00 16.49 C ANISOU 1660 CB ALA B 97 2109 2128 2026 -136 73 265 C ATOM 1661 N ASN A 98 34.057 16.819 4.333 1.00 18.10 N ANISOU 1661 N ASN B 98 2291 2226 2356 -25 336 446 N ATOM 1662 CA AASN A 98 35.500 16.944 4.315 0.50 19.72 C ANISOU 1662 CA AASN B 98 2383 2523 2586 28 229 306 C ATOM 1663 C ASN A 98 36.013 16.499 2.959 1.00 20.08 C ANISOU 1663 C ASN B 98 2384 2612 2633 5 330 263 C ATOM 1664 O ASN A 98 35.786 15.387 2.579 1.00 21.10 O ANISOU 1664 O ASN B 98 2373 2784 2859 -268 848 389 O ATOM 1665 CB AASN A 98 36.065 16.010 5.391 0.50 21.36 C ANISOU 1665 CB AASN B 98 2594 2734 2785 135 186 315 C ATOM 1666 CG AASN A 98 37.572 16.037 5.468 0.50 21.76 C ANISOU 1666 CG AASN B 98 2544 2811 2913 43 89 360 C ATOM 1667 OD1AASN A 98 38.246 16.990 5.049 0.50 22.58 O ANISOU 1667 OD1AASN B 98 2136 3433 3008 74 67 411 O ATOM 1668 ND2AASN A 98 38.120 14.976 6.048 0.50 25.56 N ANISOU 1668 ND2AASN B 98 3351 2999 3359 318 -143 459 N ATOM 1669 N ASP A 99 36.702 17.364 2.212 1.00 19.75 N ANISOU 1669 N ASP B 99 2412 2451 2641 51 367 329 N ATOM 1670 CA ASP A 99 37.233 16.983 0.881 1.00 21.52 C ANISOU 1670 CA ASP B 99 2712 2675 2789 -43 295 261 C ATOM 1671 C ASP A 99 38.333 15.923 0.892 1.00 24.27 C ANISOU 1671 C ASP B 99 2977 3073 3171 -73 367 206 C ATOM 1672 O ASP A 99 38.482 15.197 -0.073 1.00 27.45 O ANISOU 1672 O ASP B 99 3557 3184 3686 -1 492 315 O ATOM 1673 CB ASP A 99 37.636 18.256 0.098 1.00 18.69 C ANISOU 1673 CB ASP B 99 2112 2414 2575 -70 426 346 C ATOM 1674 CG ASP A 99 36.450 18.998 -0.449 1.00 19.51 C ANISOU 1674 CG ASP B 99 2471 2416 2526 -172 419 525 C ATOM 1675 OD1 ASP A 99 35.288 18.520 -0.338 1.00 23.39 O ANISOU 1675 OD1 ASP B 99 2608 2716 3562 18 78 269 O ATOM 1676 OD2 ASP A 99 36.663 20.123 -0.933 1.00 18.61 O ANISOU 1676 OD2 ASP B 99 2341 2216 2512 -325 188 505 O ATOM 1677 N SER A 100 39.053 15.810 1.985 1.00 27.53 N ANISOU 1677 N SER B 100 3223 3558 3677 156 332 186 N ATOM 1678 CA SER A 100 40.122 14.805 2.101 1.00 29.50 C ANISOU 1678 CA SER B 100 3594 3648 3965 114 154 137 C ATOM 1679 C SER A 100 39.526 13.404 1.950 1.00 31.98 C ANISOU 1679 C SER B 100 3948 3885 4317 65 215 54 C ATOM 1680 O SER A 100 40.014 12.556 1.158 1.00 35.43 O ANISOU 1680 O SER B 100 4355 4200 4906 21 231 -88 O ATOM 1681 CB SER A 100 40.811 14.951 3.460 1.00 31.09 C ANISOU 1681 CB SER B 100 3840 3899 4072 130 106 129 C ATOM 1682 OG SER A 100 41.140 16.308 3.763 1.00 34.51 O ANISOU 1682 OG SER B 100 4134 4365 4612 -51 92 107 O ATOM 1683 N GLY A 101 38.433 13.176 2.664 1.00 31.80 N ANISOU 1683 N GLY B 101 3992 3823 4267 6 145 133 N ATOM 1684 CA GLY A 101 37.787 11.842 2.683 1.00 31.12 C ANISOU 1684 CA GLY B 101 3990 3793 4041 -11 87 197 C ATOM 1685 C GLY A 101 37.118 11.494 1.363 1.00 31.55 C ANISOU 1685 C GLY B 101 4081 3871 4035 -6 9 274 C ATOM 1686 O GLY A 101 37.169 12.284 0.395 1.00 32.22 O ANISOU 1686 O GLY B 101 4201 4074 3965 25 46 467 O ATOM 1687 N PRO A 102 36.535 10.291 1.268 1.00 29.74 N ANISOU 1687 N PRO B 102 3911 3714 3674 0 76 377 N ATOM 1688 CA PRO A 102 35.841 9.863 0.075 1.00 29.12 C ANISOU 1688 CA PRO B 102 3703 3662 3700 29 106 260 C ATOM 1689 C PRO A 102 34.684 10.827 -0.273 1.00 28.30 C ANISOU 1689 C PRO B 102 3646 3613 3493 34 104 214 C ATOM 1690 O PRO A 102 34.218 11.617 0.588 1.00 29.46 O ANISOU 1690 O PRO B 102 3810 3588 3793 106 176 279 O ATOM 1691 CB PRO A 102 35.392 8.427 0.395 1.00 29.46 C ANISOU 1691 CB PRO B 102 3810 3739 3644 28 82 259 C ATOM 1692 CG PRO A 102 36.271 7.973 1.509 1.00 29.98 C ANISOU 1692 CG PRO B 102 3927 3791 3673 71 34 264 C ATOM 1693 CD PRO A 102 36.581 9.222 2.299 1.00 29.84 C ANISOU 1693 CD PRO B 102 4018 3653 3666 24 -30 417 C ATOM 1694 N ARG A 103 34.240 10.742 -1.522 1.00 27.20 N ANISOU 1694 N ARG B 103 3416 3597 3322 -14 225 250 N ATOM 1695 CA AARG A 103 33.445 11.747 -2.229 0.50 26.71 C ANISOU 1695 CA AARG B 103 3481 3457 3209 -8 152 198 C ATOM 1696 C ARG A 103 31.948 11.580 -2.114 1.00 26.10 C ANISOU 1696 C ARG B 103 3429 3364 3124 20 161 222 C ATOM 1697 O ARG A 103 31.200 12.505 -2.432 1.00 28.08 O ANISOU 1697 O ARG B 103 3852 3411 3405 53 17 303 O ATOM 1698 CB AARG A 103 33.717 11.713 -3.760 0.50 26.49 C ANISOU 1698 CB AARG B 103 3465 3403 3196 -76 168 180 C ATOM 1699 CG AARG A 103 35.122 11.406 -4.246 0.50 28.31 C ANISOU 1699 CG AARG B 103 3622 3574 3559 10 42 9 C ATOM 1700 CD AARG A 103 36.194 12.409 -3.844 0.50 28.09 C ANISOU 1700 CD AARG B 103 3619 3593 3460 17 12 41 C ATOM 1701 NE AARG A 103 37.524 11.802 -3.916 0.50 27.87 N ANISOU 1701 NE AARG B 103 3588 3530 3471 25 257 91 N ATOM 1702 CZ AARG A 103 38.160 11.510 -5.051 0.50 28.42 C ANISOU 1702 CZ AARG B 103 3605 3624 3568 14 55 17 C ATOM 1703 NH1AARG A 103 37.628 11.781 -6.233 0.50 29.03 N ANISOU 1703 NH1AARG B 103 3711 3811 3505 8 49 -150 N ATOM 1704 NH2AARG A 103 39.345 10.947 -5.006 0.50 27.70 N ANISOU 1704 NH2AARG B 103 3528 3392 3604 -11 42 13 N ATOM 1705 N ARG A 104 31.480 10.367 -1.788 1.00 22.83 N ANISOU 1705 N ARG B 104 3109 3037 2526 148 298 385 N ATOM 1706 CA ARG A 104 30.054 10.159 -1.754 1.00 22.22 C ANISOU 1706 CA ARG B 104 3079 3049 2315 59 277 436 C ATOM 1707 C ARG A 104 29.625 9.799 -0.330 1.00 19.15 C ANISOU 1707 C ARG B 104 2788 2740 1748 313 344 464 C ATOM 1708 O ARG A 104 30.197 8.919 0.290 1.00 19.01 O ANISOU 1708 O ARG B 104 2667 2845 1709 582 483 430 O ATOM 1709 CB ARG A 104 29.638 9.062 -2.712 1.00 23.11 C ANISOU 1709 CB ARG B 104 3175 3280 2323 32 228 380 C ATOM 1710 CG ARG A 104 30.138 9.154 -4.151 1.00 28.95 C ANISOU 1710 CG ARG B 104 3804 3933 3259 -3 226 239 C ATOM 1711 CD ARG A 104 29.648 7.876 -4.799 1.00 31.65 C ANISOU 1711 CD ARG B 104 4209 4123 3691 -85 59 98 C ATOM 1712 NE ARG A 104 30.425 7.377 -5.930 1.00 38.62 N ANISOU 1712 NE ARG B 104 5113 4833 4727 -37 250 -256 N ATOM 1713 CZ ARG A 104 30.157 6.224 -6.555 1.00 38.73 C ANISOU 1713 CZ ARG B 104 5158 4779 4777 -58 127 -177 C ATOM 1714 NH1 ARG A 104 29.139 5.456 -6.145 1.00 41.59 N ANISOU 1714 NH1 ARG B 104 5257 5298 5245 -167 192 -44 N ATOM 1715 NH2 ARG A 104 30.897 5.834 -7.598 1.00 40.67 N ANISOU 1715 NH2 ARG B 104 5259 5124 5070 -61 237 -119 N ATOM 1716 N TYR A 105 28.598 10.485 0.118 1.00 16.68 N ANISOU 1716 N TYR B 105 2517 2396 1424 238 434 583 N ATOM 1717 CA TYR A 105 28.095 10.314 1.482 1.00 16.44 C ANISOU 1717 CA TYR B 105 2256 2335 1653 182 191 375 C ATOM 1718 C TYR A 105 26.692 9.747 1.392 1.00 14.72 C ANISOU 1718 C TYR B 105 2093 2076 1423 220 108 422 C ATOM 1719 O TYR A 105 25.834 10.333 0.773 1.00 17.68 O ANISOU 1719 O TYR B 105 2077 2636 2003 284 -111 556 O ATOM 1720 CB TYR A 105 28.014 11.665 2.192 1.00 17.20 C ANISOU 1720 CB TYR B 105 2155 2464 1916 205 90 211 C ATOM 1721 CG TYR A 105 29.296 12.407 2.370 1.00 17.35 C ANISOU 1721 CG TYR B 105 2125 2319 2148 135 216 221 C ATOM 1722 CD1 TYR A 105 29.890 13.045 1.280 1.00 20.88 C ANISOU 1722 CD1 TYR B 105 2667 2985 2278 47 214 405 C ATOM 1723 CD2 TYR A 105 29.927 12.503 3.590 1.00 20.63 C ANISOU 1723 CD2 TYR B 105 2479 3165 2193 -146 367 4 C ATOM 1724 CE1 TYR A 105 31.059 13.761 1.432 1.00 22.79 C ANISOU 1724 CE1 TYR B 105 2879 3066 2711 -155 21 65 C ATOM 1725 CE2 TYR A 105 31.137 13.269 3.743 1.00 19.26 C ANISOU 1725 CE2 TYR B 105 2619 2632 2065 -14 -252 225 C ATOM 1726 CZ TYR A 105 31.684 13.859 2.670 1.00 21.42 C ANISOU 1726 CZ TYR B 105 2308 3015 2815 69 180 -125 C ATOM 1727 OH TYR A 105 32.827 14.616 2.820 1.00 22.65 O ANISOU 1727 OH TYR B 105 2385 2874 3346 64 138 -214 O ATOM 1728 N THR A 106 26.467 8.606 2.043 1.00 14.18 N ANISOU 1728 N THR B 106 2126 2105 1156 254 199 323 N ATOM 1729 CA THR A 106 25.159 8.102 2.249 1.00 13.99 C ANISOU 1729 CA THR B 106 2143 2016 1155 155 114 245 C ATOM 1730 C THR A 106 24.909 8.239 3.745 1.00 12.93 C ANISOU 1730 C THR B 106 1957 1913 1040 182 145 265 C ATOM 1731 O THR A 106 25.626 7.699 4.582 1.00 15.05 O ANISOU 1731 O THR B 106 2135 2247 1335 500 227 280 O ATOM 1732 CB THR A 106 25.032 6.638 1.833 1.00 15.53 C ANISOU 1732 CB THR B 106 2296 2232 1372 281 185 144 C ATOM 1733 OG1 THR A 106 25.219 6.559 0.427 1.00 19.16 O ANISOU 1733 OG1 THR B 106 3068 2645 1564 371 291 10 O ATOM 1734 CG2 THR A 106 23.681 6.069 2.225 1.00 17.10 C ANISOU 1734 CG2 THR B 106 2453 2218 1823 61 30 196 C ATOM 1735 N ILE A 107 23.839 8.921 4.071 1.00 13.03 N ANISOU 1735 N ILE B 107 1945 1970 1032 228 228 314 N ATOM 1736 CA ILE A 107 23.322 9.036 5.453 1.00 12.59 C ANISOU 1736 CA ILE B 107 1774 1907 1100 39 70 243 C ATOM 1737 C ILE A 107 22.148 8.071 5.528 1.00 13.04 C ANISOU 1737 C ILE B 107 1866 1921 1166 50 42 157 C ATOM 1738 O ILE A 107 21.124 8.278 4.896 1.00 14.26 O ANISOU 1738 O ILE B 107 1881 2303 1235 -65 -23 324 O ATOM 1739 CB ILE A 107 22.910 10.484 5.772 1.00 12.76 C ANISOU 1739 CB ILE B 107 1731 2037 1081 157 1 214 C ATOM 1740 CG1 ILE A 107 24.092 11.461 5.523 1.00 14.84 C ANISOU 1740 CG1 ILE B 107 2270 1899 1467 31 -67 6 C ATOM 1741 CG2 ILE A 107 22.273 10.566 7.144 1.00 14.44 C ANISOU 1741 CG2 ILE B 107 1978 2187 1322 123 92 69 C ATOM 1742 CD1 ILE A 107 25.315 11.255 6.394 1.00 17.48 C ANISOU 1742 CD1 ILE B 107 2412 2410 1818 59 -252 27 C ATOM 1743 N ALA A 108 22.321 7.005 6.280 1.00 12.66 N ANISOU 1743 N ALA B 108 1953 1906 950 3 108 213 N ATOM 1744 CA ALA A 108 21.295 6.012 6.474 1.00 13.07 C ANISOU 1744 CA ALA B 108 2013 1883 1067 -12 -50 138 C ATOM 1745 C ALA A 108 20.667 6.151 7.857 1.00 12.97 C ANISOU 1745 C ALA B 108 1940 1869 1116 -7 -25 151 C ATOM 1746 O ALA A 108 21.382 6.428 8.795 1.00 12.96 O ANISOU 1746 O ALA B 108 1756 2074 1092 -179 -108 132 O ATOM 1747 CB ALA A 108 21.883 4.623 6.313 1.00 14.94 C ANISOU 1747 CB ALA B 108 2367 1966 1343 140 -100 75 C ATOM 1748 N ALA A 109 19.375 5.947 7.972 1.00 12.56 N ANISOU 1748 N ALA B 109 1963 1839 968 -211 -151 116 N ATOM 1749 CA ALA A 109 18.655 5.944 9.251 1.00 11.72 C ANISOU 1749 CA ALA B 109 1725 1657 1070 -150 -80 -8 C ATOM 1750 C ALA A 109 17.726 4.751 9.346 1.00 11.48 C ANISOU 1750 C ALA B 109 1743 1633 987 -240 -20 -77 C ATOM 1751 O ALA A 109 17.050 4.426 8.351 1.00 13.13 O ANISOU 1751 O ALA B 109 2064 2009 916 -418 -456 5 O ATOM 1752 CB ALA A 109 17.865 7.201 9.447 1.00 13.81 C ANISOU 1752 CB ALA B 109 2098 1734 1414 -81 -133 -73 C ATOM 1753 N LEU A 110 17.670 4.126 10.505 1.00 10.63 N ANISOU 1753 N LEU B 110 1573 1442 1024 29 97 -136 N ATOM 1754 CA LEU A 110 16.810 2.991 10.770 1.00 10.74 C ANISOU 1754 CA LEU B 110 1621 1385 1074 157 62 -107 C ATOM 1755 C LEU A 110 15.871 3.382 11.895 1.00 10.81 C ANISOU 1755 C LEU B 110 1458 1595 1054 93 35 -103 C ATOM 1756 O LEU A 110 16.348 3.717 12.980 1.00 11.28 O ANISOU 1756 O LEU B 110 1513 1790 981 118 -36 -181 O ATOM 1757 CB LEU A 110 17.688 1.804 11.181 1.00 10.58 C ANISOU 1757 CB LEU B 110 1575 1465 978 157 32 -8 C ATOM 1758 CG LEU A 110 16.918 0.526 11.612 1.00 11.97 C ANISOU 1758 CG LEU B 110 1779 1285 1483 199 199 -60 C ATOM 1759 CD1 LEU A 110 16.102 -0.034 10.432 1.00 13.32 C ANISOU 1759 CD1 LEU B 110 1860 1454 1746 -191 277 -301 C ATOM 1760 CD2 LEU A 110 17.914 -0.513 12.184 1.00 15.36 C ANISOU 1760 CD2 LEU B 110 2048 1860 1927 479 38 348 C ATOM 1761 N LEU A 111 14.554 3.399 11.620 1.00 9.93 N ANISOU 1761 N LEU B 111 1398 1480 892 117 43 -228 N ATOM 1762 CA LEU A 111 13.573 3.987 12.486 1.00 10.25 C ANISOU 1762 CA LEU B 111 1440 1380 1073 51 15 -300 C ATOM 1763 C LEU A 111 12.724 2.947 13.232 1.00 10.10 C ANISOU 1763 C LEU B 111 1418 1292 1128 210 90 -239 C ATOM 1764 O LEU A 111 12.175 2.022 12.642 1.00 9.86 O ANISOU 1764 O LEU B 111 1385 1314 1045 200 -165 -300 O ATOM 1765 CB LEU A 111 12.638 4.864 11.696 1.00 9.54 C ANISOU 1765 CB LEU B 111 1369 1243 1010 93 41 -388 C ATOM 1766 CG LEU A 111 13.237 5.909 10.817 1.00 11.02 C ANISOU 1766 CG LEU B 111 1495 1445 1246 197 -13 -232 C ATOM 1767 CD1 LEU A 111 12.091 6.745 10.177 1.00 13.01 C ANISOU 1767 CD1 LEU B 111 1630 1749 1565 125 -474 68 C ATOM 1768 CD2 LEU A 111 14.253 6.780 11.545 1.00 10.58 C ANISOU 1768 CD2 LEU B 111 1247 1470 1301 25 -111 -179 C ATOM 1769 N SER A 112 12.571 3.179 14.535 1.00 11.12 N ANISOU 1769 N SER B 112 1696 1500 1028 -59 -16 -154 N ATOM 1770 CA SER A 112 11.550 2.562 15.370 1.00 9.95 C ANISOU 1770 CA SER B 112 1412 1328 1040 192 18 -218 C ATOM 1771 C SER A 112 10.823 3.659 16.146 1.00 9.47 C ANISOU 1771 C SER B 112 1311 1306 980 95 67 -123 C ATOM 1772 O SER A 112 11.337 4.758 16.271 1.00 10.24 O ANISOU 1772 O SER B 112 1379 1356 1153 -55 130 -129 O ATOM 1773 CB SER A 112 12.168 1.557 16.352 1.00 11.83 C ANISOU 1773 CB SER B 112 1729 1647 1116 263 55 -265 C ATOM 1774 OG SER A 112 12.892 0.518 15.687 1.00 12.59 O ANISOU 1774 OG SER B 112 1988 1510 1284 583 -6 -189 O ATOM 1775 N PRO A 113 9.650 3.347 16.742 1.00 9.91 N ANISOU 1775 N PRO B 113 1477 1102 1185 55 56 -78 N ATOM 1776 CA PRO A 113 8.935 4.434 17.413 1.00 10.28 C ANISOU 1776 CA PRO B 113 1472 1214 1221 148 43 -115 C ATOM 1777 C PRO A 113 9.701 5.165 18.516 1.00 11.06 C ANISOU 1777 C PRO B 113 1624 1262 1316 86 202 -98 C ATOM 1778 O PRO A 113 9.547 6.385 18.654 1.00 10.96 O ANISOU 1778 O PRO B 113 1824 1058 1281 215 184 -79 O ATOM 1779 CB PRO A 113 7.633 3.776 17.865 1.00 11.28 C ANISOU 1779 CB PRO B 113 1401 1396 1489 326 16 -209 C ATOM 1780 CG PRO A 113 7.414 2.723 16.797 1.00 11.47 C ANISOU 1780 CG PRO B 113 1476 1392 1488 -213 24 -174 C ATOM 1781 CD PRO A 113 8.786 2.200 16.485 1.00 11.46 C ANISOU 1781 CD PRO B 113 1814 1363 1176 -44 30 -196 C ATOM 1782 N TYR A 114 10.482 4.425 19.312 1.00 9.63 N ANISOU 1782 N TYR B 114 1417 1161 1080 89 75 -245 N ATOM 1783 CA TYR A 114 11.242 4.983 20.451 1.00 10.26 C ANISOU 1783 CA TYR B 114 1458 1181 1256 -32 7 -178 C ATOM 1784 C TYR A 114 12.732 4.914 20.255 1.00 10.35 C ANISOU 1784 C TYR B 114 1437 1352 1141 -76 104 -167 C ATOM 1785 O TYR A 114 13.486 5.110 21.189 1.00 11.86 O ANISOU 1785 O TYR B 114 1402 1947 1155 -78 70 -577 O ATOM 1786 CB TYR A 114 10.818 4.332 21.773 1.00 10.71 C ANISOU 1786 CB TYR B 114 1488 1276 1304 125 196 -161 C ATOM 1787 CG TYR A 114 9.505 4.844 22.312 1.00 10.23 C ANISOU 1787 CG TYR B 114 1500 1240 1145 33 388 -197 C ATOM 1788 CD1 TYR A 114 8.325 4.452 21.733 1.00 15.39 C ANISOU 1788 CD1 TYR B 114 1551 2611 1683 229 283 -388 C ATOM 1789 CD2 TYR A 114 9.425 5.689 23.391 1.00 9.91 C ANISOU 1789 CD2 TYR B 114 1455 986 1325 268 93 69 C ATOM 1790 CE1 TYR A 114 7.111 4.866 22.235 1.00 18.90 C ANISOU 1790 CE1 TYR B 114 1843 3170 2167 46 141 -278 C ATOM 1791 CE2 TYR A 114 8.223 6.189 23.860 1.00 13.28 C ANISOU 1791 CE2 TYR B 114 1753 1782 1508 290 393 100 C ATOM 1792 CZ TYR A 114 7.064 5.721 23.274 1.00 17.40 C ANISOU 1792 CZ TYR B 114 1844 2483 2282 211 165 -190 C ATOM 1793 OH TYR A 114 5.836 6.116 23.714 1.00 20.67 O ANISOU 1793 OH TYR B 114 1877 3526 2450 318 411 -321 O ATOM 1794 N SER A 115 13.206 4.661 19.051 1.00 11.24 N ANISOU 1794 N SER B 115 1441 1627 1200 -63 37 -350 N ATOM 1795 CA SER A 115 14.628 4.536 18.821 1.00 10.76 C ANISOU 1795 CA SER B 115 1332 1594 1163 -27 72 -216 C ATOM 1796 C SER A 115 14.969 4.779 17.370 1.00 10.74 C ANISOU 1796 C SER B 115 1256 1595 1229 -12 94 -392 C ATOM 1797 O SER A 115 14.174 4.445 16.496 1.00 12.46 O ANISOU 1797 O SER B 115 1214 2238 1282 -42 -11 -583 O ATOM 1798 CB SER A 115 15.051 3.102 19.158 1.00 12.09 C ANISOU 1798 CB SER B 115 1667 1692 1233 -130 161 -242 C ATOM 1799 OG SER A 115 16.390 2.838 19.046 1.00 15.48 O ANISOU 1799 OG SER B 115 2144 1743 1995 203 49 -423 O ATOM 1800 N TYR A 116 16.174 5.270 17.106 1.00 10.23 N ANISOU 1800 N TYR B 116 1167 1701 1018 66 193 -366 N ATOM 1801 CA TYR A 116 16.709 5.272 15.761 1.00 10.54 C ANISOU 1801 CA TYR B 116 1304 1667 1033 84 146 -115 C ATOM 1802 C TYR A 116 18.211 5.152 15.793 1.00 9.98 C ANISOU 1802 C TYR B 116 1262 1597 932 56 73 -113 C ATOM 1803 O TYR A 116 18.860 5.502 16.756 1.00 11.13 O ANISOU 1803 O TYR B 116 1329 1920 978 64 -3 -119 O ATOM 1804 CB TYR A 116 16.239 6.463 14.950 1.00 12.27 C ANISOU 1804 CB TYR B 116 1564 1972 1125 110 68 -124 C ATOM 1805 CG TYR A 116 16.784 7.788 15.413 1.00 12.30 C ANISOU 1805 CG TYR B 116 1819 1670 1184 245 84 -8 C ATOM 1806 CD1 TYR A 116 18.013 8.269 15.022 1.00 12.50 C ANISOU 1806 CD1 TYR B 116 1931 1572 1246 228 -189 139 C ATOM 1807 CD2 TYR A 116 16.006 8.578 16.251 1.00 13.51 C ANISOU 1807 CD2 TYR B 116 1753 2072 1306 511 2 -55 C ATOM 1808 CE1 TYR A 116 18.461 9.506 15.484 1.00 15.44 C ANISOU 1808 CE1 TYR B 116 2026 1825 2015 179 -33 49 C ATOM 1809 CE2 TYR A 116 16.420 9.787 16.636 1.00 16.23 C ANISOU 1809 CE2 TYR B 116 1976 2216 1973 449 -49 -372 C ATOM 1810 CZ TYR A 116 17.647 10.253 16.322 1.00 15.06 C ANISOU 1810 CZ TYR B 116 2145 1790 1787 9 -158 -285 C ATOM 1811 OH TYR A 116 18.029 11.519 16.791 1.00 19.46 O ANISOU 1811 OH TYR B 116 2542 2068 2780 62 -55 -555 O ATOM 1812 N SER A 117 18.706 4.600 14.692 1.00 10.25 N ANISOU 1812 N SER B 117 1336 1659 899 -48 2 -106 N ATOM 1813 CA BSER A 117 20.101 4.407 14.387 0.50 11.52 C ANISOU 1813 CA BSER B 117 1458 1719 1201 11 56 -45 C ATOM 1814 C SER A 117 20.434 5.231 13.148 1.00 10.82 C ANISOU 1814 C SER B 117 1417 1761 931 66 82 -100 C ATOM 1815 O SER A 117 19.600 5.306 12.228 1.00 12.07 O ANISOU 1815 O SER B 117 1620 2066 897 -54 50 -32 O ATOM 1816 CB BSER A 117 20.343 2.933 14.029 0.50 12.28 C ANISOU 1816 CB BSER B 117 1500 1636 1527 172 74 206 C ATOM 1817 OG BSER A 117 21.728 2.708 13.859 0.50 16.88 O ANISOU 1817 OG BSER B 117 1959 2614 1838 102 350 173 O ATOM 1818 N THR A 118 21.619 5.777 13.096 1.00 10.16 N ANISOU 1818 N THR B 118 1368 1673 816 -65 77 13 N ATOM 1819 CA THR A 118 22.081 6.401 11.856 1.00 10.89 C ANISOU 1819 CA THR B 118 1506 1680 952 -55 44 10 C ATOM 1820 C THR A 118 23.545 6.037 11.637 1.00 12.41 C ANISOU 1820 C THR B 118 1625 1824 1267 -96 92 21 C ATOM 1821 O THR A 118 24.344 5.972 12.548 1.00 13.64 O ANISOU 1821 O THR B 118 1569 2483 1128 -66 238 -76 O ATOM 1822 CB THR A 118 21.850 7.904 11.858 1.00 12.68 C ANISOU 1822 CB THR B 118 1844 1808 1165 14 5 -97 C ATOM 1823 OG1 THR A 118 22.163 8.445 10.583 1.00 12.66 O ANISOU 1823 OG1 THR B 118 1799 1852 1156 -167 -263 68 O ATOM 1824 CG2 THR A 118 22.687 8.606 12.939 1.00 13.57 C ANISOU 1824 CG2 THR B 118 2160 1730 1267 -76 -339 -152 C ATOM 1825 N THR A 119 23.871 5.818 10.372 1.00 11.66 N ANISOU 1825 N THR B 119 1680 1777 970 -84 90 51 N ATOM 1826 CA ATHR A 119 25.292 5.552 9.992 0.50 12.69 C ANISOU 1826 CA ATHR B 119 1805 1665 1349 66 152 -71 C ATOM 1827 C THR A 119 25.570 6.317 8.741 1.00 12.71 C ANISOU 1827 C THR B 119 1840 1657 1332 153 87 74 C ATOM 1828 O THR A 119 24.701 6.692 7.973 1.00 13.22 O ANISOU 1828 O THR B 119 1857 2104 1059 164 -80 398 O ATOM 1829 CB ATHR A 119 25.736 3.983 9.900 0.50 10.65 C ANISOU 1829 CB ATHR B 119 1504 1500 1041 129 107 219 C ATOM 1830 OG1ATHR A 119 27.171 3.823 9.942 0.50 12.08 O ANISOU 1830 OG1ATHR B 119 1519 1656 1414 119 143 4 O ATOM 1831 CG2ATHR A 119 25.224 3.326 8.675 0.50 12.55 C ANISOU 1831 CG2ATHR B 119 1855 1562 1349 59 -231 162 C ATOM 1832 N ALA A 120 26.836 6.610 8.590 1.00 12.41 N ANISOU 1832 N ALA B 120 1849 1849 1016 112 96 292 N ATOM 1833 CA ALA A 120 27.389 7.274 7.416 1.00 12.62 C ANISOU 1833 CA ALA B 120 1863 1759 1171 121 239 238 C ATOM 1834 C ALA A 120 28.236 6.271 6.662 1.00 12.99 C ANISOU 1834 C ALA B 120 1921 1801 1214 246 164 408 C ATOM 1835 O ALA A 120 29.101 5.617 7.245 1.00 15.48 O ANISOU 1835 O ALA B 120 2197 2368 1315 594 210 227 O ATOM 1836 CB ALA A 120 28.219 8.463 7.892 1.00 15.51 C ANISOU 1836 CB ALA B 120 2338 1898 1656 -32 201 194 C ATOM 1837 N VAL A 121 27.965 6.147 5.379 1.00 12.85 N ANISOU 1837 N VAL B 121 1687 1816 1379 338 208 166 N ATOM 1838 CA VAL A 121 28.752 5.299 4.498 1.00 14.02 C ANISOU 1838 CA VAL B 121 2053 1887 1385 281 243 230 C ATOM 1839 C VAL A 121 29.389 6.292 3.539 1.00 13.96 C ANISOU 1839 C VAL B 121 1931 1907 1465 378 396 263 C ATOM 1840 O VAL A 121 28.680 6.936 2.736 1.00 16.47 O ANISOU 1840 O VAL B 121 2314 2232 1712 558 312 247 O ATOM 1841 CB VAL A 121 27.912 4.249 3.788 1.00 14.62 C ANISOU 1841 CB VAL B 121 2348 1761 1443 293 291 168 C ATOM 1842 CG1 VAL A 121 28.836 3.312 3.004 1.00 17.89 C ANISOU 1842 CG1 VAL B 121 2734 2198 1865 448 352 -19 C ATOM 1843 CG2 VAL A 121 27.001 3.477 4.790 1.00 17.54 C ANISOU 1843 CG2 VAL B 121 2881 1911 1872 20 333 258 C ATOM 1844 N VAL A 122 30.699 6.442 3.635 1.00 15.16 N ANISOU 1844 N VAL B 122 2246 1950 1563 198 353 344 N ATOM 1845 CA VAL A 122 31.444 7.435 2.834 1.00 17.36 C ANISOU 1845 CA VAL B 122 2467 2345 1783 123 454 288 C ATOM 1846 C VAL A 122 32.408 6.696 1.957 1.00 18.98 C ANISOU 1846 C VAL B 122 2534 2489 2188 266 404 281 C ATOM 1847 O VAL A 122 33.310 6.045 2.458 1.00 18.06 O ANISOU 1847 O VAL B 122 2347 2616 1899 151 543 503 O ATOM 1848 CB VAL A 122 32.180 8.439 3.765 1.00 17.87 C ANISOU 1848 CB VAL B 122 2532 2408 1848 95 342 308 C ATOM 1849 CG1 VAL A 122 32.780 9.590 2.987 1.00 21.53 C ANISOU 1849 CG1 VAL B 122 3272 2434 2474 -447 376 505 C ATOM 1850 CG2 VAL A 122 31.171 9.012 4.807 1.00 19.86 C ANISOU 1850 CG2 VAL B 122 2703 2758 2084 158 618 85 C ATOM 1851 N THR A 123 32.185 6.803 0.642 1.00 19.13 N ANISOU 1851 N THR B 123 2648 2463 2156 205 526 188 N ATOM 1852 CA THR A 123 32.947 6.019 -0.347 1.00 22.13 C ANISOU 1852 CA THR B 123 3152 2749 2507 248 464 116 C ATOM 1853 C THR A 123 33.456 6.876 -1.492 1.00 24.25 C ANISOU 1853 C THR B 123 3554 2934 2725 287 607 179 C ATOM 1854 O THR A 123 33.074 8.028 -1.658 1.00 23.69 O ANISOU 1854 O THR B 123 3625 2855 2520 381 1051 214 O ATOM 1855 CB THR A 123 32.079 4.925 -0.979 1.00 22.76 C ANISOU 1855 CB THR B 123 3134 2740 2771 222 423 178 C ATOM 1856 OG1 THR A 123 30.920 5.497 -1.601 1.00 27.46 O ANISOU 1856 OG1 THR B 123 3907 3577 2947 107 158 105 O ATOM 1857 CG2 THR A 123 31.660 3.903 0.079 1.00 22.15 C ANISOU 1857 CG2 THR B 123 3270 2810 2336 -84 514 182 C ATOM 1858 N ASN A 124 34.355 6.306 -2.285 1.00 26.41 N ANISOU 1858 N ASN B 124 3772 3319 2943 237 684 129 N ATOM 1859 CA ASN A 124 34.854 6.966 -3.513 1.00 29.12 C ANISOU 1859 CA ASN B 124 4096 3602 3365 110 350 234 C ATOM 1860 C ASN A 124 34.350 6.283 -4.757 1.00 32.11 C ANISOU 1860 C ASN B 124 4541 3906 3753 61 269 196 C ATOM 1861 O ASN A 124 34.399 5.059 -4.775 1.00 33.62 O ANISOU 1861 O ASN B 124 4956 3895 3924 120 152 175 O ATOM 1862 CB ASN A 124 36.376 6.961 -3.500 1.00 30.05 C ANISOU 1862 CB ASN B 124 4080 3820 3515 74 481 156 C ATOM 1863 CG ASN A 124 36.955 8.213 -2.877 1.00 33.82 C ANISOU 1863 CG ASN B 124 4470 4419 3960 -23 261 147 C ATOM 1864 OD1 ASN A 124 36.356 9.306 -2.943 1.00 36.43 O ANISOU 1864 OD1 ASN B 124 4575 4935 4329 133 367 348 O ATOM 1865 ND2 ASN A 124 38.116 8.066 -2.237 1.00 37.51 N ANISOU 1865 ND2 ASN B 124 4367 4973 4910 192 59 179 N TER 1866 ASN B 124 ATOM 1 N PRO A 11 28.635 -12.398 36.931 1.00 20.06 N ANISOU 1 N PRO C 11 2231 2999 2390 -98 348 -248 N ATOM 2 CA PRO A 11 29.565 -12.391 35.842 1.00 17.93 C ANISOU 2 CA PRO C 11 2048 2587 2175 -39 253 -322 C ATOM 3 C PRO A 11 28.927 -12.322 34.472 1.00 14.43 C ANISOU 3 C PRO C 11 1633 2027 1822 -1 227 -388 C ATOM 4 O PRO A 11 29.619 -11.990 33.495 1.00 13.66 O ANISOU 4 O PRO C 11 1593 1904 1692 36 172 -624 O ATOM 5 CB PRO A 11 30.287 -13.711 35.993 1.00 20.65 C ANISOU 5 CB PRO C 11 2529 3040 2276 86 243 -142 C ATOM 6 CG PRO A 11 29.407 -14.548 36.678 1.00 21.71 C ANISOU 6 CG PRO C 11 2533 2675 3038 94 341 -308 C ATOM 7 CD PRO A 11 28.707 -13.681 37.646 1.00 22.15 C ANISOU 7 CD PRO C 11 2606 3244 2565 -135 126 -359 C ATOM 8 N LEU A 12 27.650 -12.642 34.369 1.00 14.14 N ANISOU 8 N LEU C 12 1598 2043 1729 -97 170 -518 N ATOM 9 CA LEU A 12 26.900 -12.596 33.097 1.00 13.73 C ANISOU 9 CA LEU C 12 1578 2008 1630 -9 119 -662 C ATOM 10 C LEU A 12 25.515 -12.061 33.337 1.00 14.12 C ANISOU 10 C LEU C 12 1553 2155 1654 -105 54 -587 C ATOM 11 O LEU A 12 24.769 -12.565 34.189 1.00 17.23 O ANISOU 11 O LEU C 12 1799 2658 2087 69 -44 -998 O ATOM 12 CB LEU A 12 26.824 -13.970 32.478 1.00 13.63 C ANISOU 12 CB LEU C 12 1488 2093 1598 -190 78 -667 C ATOM 13 CG LEU A 12 26.118 -14.116 31.151 1.00 14.12 C ANISOU 13 CG LEU C 12 1513 2044 1808 -203 291 -365 C ATOM 14 CD1 LEU A 12 26.756 -13.257 30.046 1.00 16.71 C ANISOU 14 CD1 LEU C 12 2183 2432 1733 -184 7 -466 C ATOM 15 CD2 LEU A 12 25.937 -15.581 30.702 1.00 17.05 C ANISOU 15 CD2 LEU C 12 1928 2083 2464 -270 238 -385 C ATOM 16 N MET A 13 25.198 -10.951 32.687 1.00 13.75 N ANISOU 16 N MET C 13 1571 2058 1595 43 284 -492 N ATOM 17 CA MET A 13 23.872 -10.331 32.820 1.00 13.65 C ANISOU 17 CA MET C 13 1559 2150 1478 44 69 -393 C ATOM 18 C MET A 13 23.380 -10.046 31.397 1.00 11.69 C ANISOU 18 C MET C 13 1435 1852 1152 65 22 -230 C ATOM 19 O MET A 13 24.145 -9.746 30.509 1.00 12.29 O ANISOU 19 O MET C 13 1203 2083 1381 133 109 -479 O ATOM 20 CB MET A 13 23.985 -9.008 33.567 1.00 16.44 C ANISOU 20 CB MET C 13 1882 2471 1891 167 232 -223 C ATOM 21 CG MET A 13 22.636 -8.359 34.024 1.00 19.45 C ANISOU 21 CG MET C 13 2421 2591 2374 49 205 -185 C ATOM 22 SD MET A 13 21.967 -7.194 32.833 1.00 26.59 S ANISOU 22 SD MET C 13 3386 3426 3291 299 295 119 S ATOM 23 CE MET A 13 22.725 -5.658 33.387 1.00 26.66 C ANISOU 23 CE MET C 13 3507 3325 3296 59 139 582 C ATOM 24 N VAL A 14 22.079 -10.125 31.224 1.00 11.13 N ANISOU 24 N VAL C 14 1326 1734 1166 68 100 -150 N ATOM 25 CA VAL A 14 21.425 -9.848 29.950 1.00 10.97 C ANISOU 25 CA VAL C 14 1238 1714 1215 47 14 -124 C ATOM 26 C VAL A 14 20.387 -8.770 30.181 1.00 10.90 C ANISOU 26 C VAL C 14 1268 1703 1170 60 144 -180 C ATOM 27 O VAL A 14 19.623 -8.880 31.139 1.00 12.70 O ANISOU 27 O VAL C 14 1470 2032 1320 253 -152 -288 O ATOM 28 CB VAL A 14 20.813 -11.118 29.313 1.00 11.21 C ANISOU 28 CB VAL C 14 1432 1619 1206 -127 -40 -114 C ATOM 29 CG1 VAL A 14 20.174 -10.733 27.981 1.00 12.84 C ANISOU 29 CG1 VAL C 14 1338 2161 1378 35 250 129 C ATOM 30 CG2 VAL A 14 21.892 -12.167 29.107 1.00 12.26 C ANISOU 30 CG2 VAL C 14 1461 1656 1538 -91 -149 49 C ATOM 31 N LYS A 15 20.380 -7.732 29.318 1.00 10.67 N ANISOU 31 N LYS C 15 1282 1683 1086 155 109 -202 N ATOM 32 CA ALYS A 15 19.386 -6.660 29.441 0.50 11.80 C ANISOU 32 CA ALYS C 15 1464 1784 1234 148 78 -95 C ATOM 33 C LYS A 15 18.777 -6.419 28.076 1.00 11.63 C ANISOU 33 C LYS C 15 1316 1923 1178 145 62 -171 C ATOM 34 O LYS A 15 19.492 -6.348 27.075 1.00 12.34 O ANISOU 34 O LYS C 15 1321 2375 990 263 -56 -351 O ATOM 35 CB ALYS A 15 20.011 -5.375 29.950 0.50 12.81 C ANISOU 35 CB ALYS C 15 1621 1877 1369 115 186 -38 C ATOM 36 CG ALYS A 15 18.979 -4.321 30.252 0.50 15.07 C ANISOU 36 CG ALYS C 15 2020 2037 1669 63 9 -21 C ATOM 37 CD ALYS A 15 19.575 -3.066 30.906 0.50 16.23 C ANISOU 37 CD ALYS C 15 2182 2029 1954 -92 72 103 C ATOM 38 CE ALYS A 15 18.461 -2.084 31.375 0.50 18.08 C ANISOU 38 CE ALYS C 15 2258 2143 2469 -128 20 5 C ATOM 39 NZ ALYS A 15 18.856 -1.104 32.448 0.50 21.26 N ANISOU 39 NZ ALYS C 15 2877 2439 2761 -43 -9 131 N ATOM 40 N VAL A 16 17.451 -6.307 28.043 1.00 10.00 N ANISOU 40 N VAL C 16 1210 1760 827 317 35 -183 N ATOM 41 CA VAL A 16 16.736 -6.208 26.774 1.00 9.96 C ANISOU 41 CA VAL C 16 1243 1555 984 243 62 -123 C ATOM 42 C VAL A 16 15.731 -5.054 26.868 1.00 10.05 C ANISOU 42 C VAL C 16 1242 1479 1096 343 68 -27 C ATOM 43 O VAL A 16 14.994 -4.907 27.831 1.00 10.50 O ANISOU 43 O VAL C 16 1265 1713 1011 373 -41 14 O ATOM 44 CB VAL A 16 15.991 -7.530 26.465 1.00 10.66 C ANISOU 44 CB VAL C 16 1413 1609 1027 240 2 -161 C ATOM 45 CG1 VAL A 16 15.446 -7.534 25.038 1.00 11.25 C ANISOU 45 CG1 VAL C 16 1456 2025 794 348 100 -81 C ATOM 46 CG2 VAL A 16 16.911 -8.773 26.645 1.00 12.16 C ANISOU 46 CG2 VAL C 16 1979 1346 1295 467 -187 -126 C ATOM 47 N LEU A 17 15.751 -4.233 25.843 1.00 10.07 N ANISOU 47 N LEU C 17 1391 1454 978 348 -166 -67 N ATOM 48 CA LEU A 17 14.829 -3.102 25.653 1.00 9.96 C ANISOU 48 CA LEU C 17 1281 1436 1067 277 44 70 C ATOM 49 C LEU A 17 13.925 -3.323 24.429 1.00 9.65 C ANISOU 49 C LEU C 17 1254 1328 1084 295 106 52 C ATOM 50 O LEU A 17 14.351 -3.937 23.456 1.00 10.32 O ANISOU 50 O LEU C 17 1333 1498 1090 361 94 142 O ATOM 51 CB LEU A 17 15.616 -1.792 25.488 1.00 11.64 C ANISOU 51 CB LEU C 17 1590 1582 1248 216 -43 37 C ATOM 52 CG LEU A 17 16.505 -1.401 26.660 1.00 12.89 C ANISOU 52 CG LEU C 17 1711 1790 1394 176 74 128 C ATOM 53 CD1 LEU A 17 17.209 -0.051 26.350 1.00 15.73 C ANISOU 53 CD1 LEU C 17 2226 1676 2073 -191 182 227 C ATOM 54 CD2 LEU A 17 15.665 -1.296 27.940 1.00 15.89 C ANISOU 54 CD2 LEU C 17 2243 2297 1496 -98 -199 509 C ATOM 55 N ASP A 18 12.747 -2.718 24.465 1.00 10.21 N ANISOU 55 N ASP C 18 1397 1324 1156 471 202 292 N ATOM 56 CA ASP A 18 11.754 -2.769 23.390 1.00 10.00 C ANISOU 56 CA ASP C 18 1429 1266 1102 253 158 120 C ATOM 57 C ASP A 18 11.689 -1.372 22.739 1.00 9.66 C ANISOU 57 C ASP C 18 1321 1254 1094 238 180 91 C ATOM 58 O ASP A 18 11.325 -0.372 23.390 1.00 10.53 O ANISOU 58 O ASP C 18 1426 1399 1175 370 42 272 O ATOM 59 CB ASP A 18 10.424 -3.189 23.992 1.00 11.18 C ANISOU 59 CB ASP C 18 1674 1407 1165 250 130 -58 C ATOM 60 CG ASP A 18 9.291 -3.262 22.990 1.00 10.96 C ANISOU 60 CG ASP C 18 1309 1379 1476 293 72 207 C ATOM 61 OD1 ASP A 18 9.234 -2.399 22.104 1.00 11.55 O ANISOU 61 OD1 ASP C 18 1471 1452 1464 357 192 -93 O ATOM 62 OD2 ASP A 18 8.433 -4.195 23.137 1.00 13.29 O ANISOU 62 OD2 ASP C 18 1505 2040 1503 70 -137 -116 O ATOM 63 N ALA A 19 12.146 -1.302 21.489 1.00 9.91 N ANISOU 63 N ALA C 19 1476 1200 1086 393 -2 210 N ATOM 64 CA ALA A 19 12.238 -0.082 20.730 1.00 9.58 C ANISOU 64 CA ALA C 19 1435 1124 1080 258 91 226 C ATOM 65 C ALA A 19 10.891 0.451 20.217 1.00 9.76 C ANISOU 65 C ALA C 19 1446 1121 1140 232 157 210 C ATOM 66 O ALA A 19 10.832 1.586 19.731 1.00 11.07 O ANISOU 66 O ALA C 19 1579 1167 1457 324 112 163 O ATOM 67 CB ALA A 19 13.185 -0.276 19.567 1.00 11.34 C ANISOU 67 CB ALA C 19 1702 1624 983 379 -138 126 C ATOM 68 N VAL A 20 9.868 -0.408 20.272 1.00 9.77 N ANISOU 68 N VAL C 20 1437 1010 1264 307 116 -14 N ATOM 69 CA VAL A 20 8.512 -0.032 19.865 1.00 11.67 C ANISOU 69 CA VAL C 20 1588 1429 1414 259 220 15 C ATOM 70 C VAL A 20 7.766 0.676 20.984 1.00 13.00 C ANISOU 70 C VAL C 20 1736 1477 1725 240 161 30 C ATOM 71 O VAL A 20 7.116 1.683 20.728 1.00 15.46 O ANISOU 71 O VAL C 20 2124 1849 1902 453 -18 272 O ATOM 72 CB VAL A 20 7.687 -1.269 19.362 1.00 11.39 C ANISOU 72 CB VAL C 20 1463 1319 1543 248 274 45 C ATOM 73 CG1 VAL A 20 6.220 -0.896 19.143 1.00 15.38 C ANISOU 73 CG1 VAL C 20 1428 2345 2071 320 586 136 C ATOM 74 CG2 VAL A 20 8.307 -1.854 18.119 1.00 14.01 C ANISOU 74 CG2 VAL C 20 2151 1749 1420 204 94 164 C ATOM 75 N ARG A 21 7.915 0.143 22.196 1.00 11.58 N ANISOU 75 N ARG C 21 1347 1700 1353 254 -7 174 N ATOM 76 CA AARG A 21 7.234 0.619 23.424 0.50 12.91 C ANISOU 76 CA AARG C 21 1589 1694 1621 237 -28 135 C ATOM 77 C ARG A 21 8.033 1.682 24.155 1.00 12.45 C ANISOU 77 C ARG C 21 1541 1572 1615 218 -12 43 C ATOM 78 O ARG A 21 7.499 2.411 24.950 1.00 14.70 O ANISOU 78 O ARG C 21 1791 1968 1826 388 -125 291 O ATOM 79 CB AARG A 21 7.043 -0.556 24.422 0.50 14.38 C ANISOU 79 CB AARG C 21 1635 1970 1856 192 -45 148 C ATOM 80 CG AARG A 21 6.072 -1.621 23.978 0.50 16.99 C ANISOU 80 CG AARG C 21 2251 1976 2228 36 -115 -164 C ATOM 81 CD AARG A 21 6.144 -2.853 24.907 0.50 18.69 C ANISOU 81 CD AARG C 21 2441 2187 2472 172 -76 -206 C ATOM 82 NE AARG A 21 4.980 -3.701 24.760 0.50 22.38 N ANISOU 82 NE AARG C 21 2784 2697 3022 34 -45 -51 N ATOM 83 CZ AARG A 21 3.771 -3.420 25.253 0.50 24.80 C ANISOU 83 CZ AARG C 21 2958 3160 3304 40 -166 55 C ATOM 84 NH1AARG A 21 3.557 -2.285 25.921 0.50 28.44 N ANISOU 84 NH1AARG C 21 3659 3516 3629 -18 -41 107 N ATOM 85 NH2AARG A 21 2.763 -4.263 25.060 0.50 25.08 N ANISOU 85 NH2AARG C 21 3136 3061 3330 19 43 71 N ATOM 86 N GLY A 22 9.338 1.714 23.935 1.00 10.60 N ANISOU 86 N GLY C 22 1491 1225 1308 210 -135 91 N ATOM 87 CA GLY A 22 10.206 2.535 24.790 1.00 11.77 C ANISOU 87 CA GLY C 22 1673 1321 1474 126 -38 43 C ATOM 88 C GLY A 22 10.191 2.106 26.250 1.00 9.55 C ANISOU 88 C GLY C 22 1322 988 1316 166 -89 127 C ATOM 89 O GLY A 22 9.979 2.911 27.184 1.00 11.40 O ANISOU 89 O GLY C 22 1876 1076 1379 121 -318 178 O ATOM 90 N SER A 23 10.473 0.825 26.439 1.00 10.18 N ANISOU 90 N SER C 23 1622 945 1301 163 -175 16 N ATOM 91 CA ASER A 23 10.337 0.188 27.733 0.50 10.69 C ANISOU 91 CA ASER C 23 1670 1068 1322 152 -199 43 C ATOM 92 C SER A 23 11.302 -0.967 27.833 1.00 10.68 C ANISOU 92 C SER C 23 1715 1065 1277 187 -266 -87 C ATOM 93 O SER A 23 11.783 -1.461 26.807 1.00 12.46 O ANISOU 93 O SER C 23 2057 1372 1302 349 -224 132 O ATOM 94 CB ASER A 23 8.947 -0.415 27.849 0.50 11.50 C ANISOU 94 CB ASER C 23 1767 1149 1450 170 -324 -74 C ATOM 95 OG ASER A 23 8.832 -1.514 26.968 0.50 12.41 O ANISOU 95 OG ASER C 23 1613 1308 1795 -124 32 189 O ATOM 96 N PRO A 24 11.547 -1.434 29.045 1.00 11.46 N ANISOU 96 N PRO C 24 1774 1266 1312 162 -128 151 N ATOM 97 CA PRO A 24 12.212 -2.729 29.165 1.00 11.84 C ANISOU 97 CA PRO C 24 1704 1391 1400 192 0 -50 C ATOM 98 C PRO A 24 11.408 -3.823 28.443 1.00 11.74 C ANISOU 98 C PRO C 24 1678 1319 1463 268 3 83 C ATOM 99 O PRO A 24 10.178 -3.696 28.300 1.00 12.68 O ANISOU 99 O PRO C 24 1543 1521 1751 319 -201 149 O ATOM 100 CB PRO A 24 12.258 -2.981 30.656 1.00 12.78 C ANISOU 100 CB PRO C 24 1932 1484 1437 322 8 -31 C ATOM 101 CG PRO A 24 11.840 -1.789 31.267 1.00 17.90 C ANISOU 101 CG PRO C 24 2916 2247 1638 529 -132 76 C ATOM 102 CD PRO A 24 11.194 -0.865 30.338 1.00 12.22 C ANISOU 102 CD PRO C 24 2065 1179 1398 148 -194 19 C ATOM 103 N ALA A 25 12.090 -4.817 27.891 1.00 10.94 N ANISOU 103 N ALA C 25 1546 1199 1412 302 69 -36 N ATOM 104 CA ALA A 25 11.437 -5.965 27.321 1.00 10.75 C ANISOU 104 CA ALA C 25 1521 1207 1354 205 -4 -21 C ATOM 105 C ALA A 25 11.341 -6.997 28.437 1.00 10.47 C ANISOU 105 C ALA C 25 1520 1190 1266 187 -41 13 C ATOM 106 O ALA A 25 12.324 -7.587 28.855 1.00 11.37 O ANISOU 106 O ALA C 25 1447 1282 1588 214 168 -283 O ATOM 107 CB ALA A 25 12.211 -6.506 26.122 1.00 11.47 C ANISOU 107 CB ALA C 25 1573 1347 1436 117 -14 -22 C ATOM 108 N ILE A 26 10.121 -7.192 28.903 1.00 10.23 N ANISOU 108 N ILE C 26 1471 1194 1219 180 -191 -98 N ATOM 109 CA ILE A 26 9.819 -8.021 30.108 1.00 12.36 C ANISOU 109 CA ILE C 26 1752 1560 1383 150 -248 0 C ATOM 110 C ILE A 26 9.494 -9.438 29.708 1.00 11.32 C ANISOU 110 C ILE C 26 1599 1385 1317 156 -202 -34 C ATOM 111 O ILE A 26 8.876 -9.661 28.703 1.00 12.05 O ANISOU 111 O ILE C 26 1620 1570 1385 124 -124 -149 O ATOM 112 CB ILE A 26 8.654 -7.390 30.926 1.00 13.57 C ANISOU 112 CB ILE C 26 2116 1556 1483 168 -314 146 C ATOM 113 CG1 ILE A 26 8.998 -5.941 31.239 1.00 15.32 C ANISOU 113 CG1 ILE C 26 2467 1715 1638 492 -407 80 C ATOM 114 CG2 ILE A 26 8.282 -8.171 32.141 1.00 16.67 C ANISOU 114 CG2 ILE C 26 2188 2184 1959 214 -409 -55 C ATOM 115 CD1 ILE A 26 7.740 -5.253 31.767 1.00 19.00 C ANISOU 115 CD1 ILE C 26 2381 2570 2267 403 -418 184 C ATOM 116 N ASN A 27 9.896 -10.396 30.540 1.00 11.88 N ANISOU 116 N ASN C 27 1621 1568 1325 221 -176 -81 N ATOM 117 CA ASN A 27 9.539 -11.796 30.326 1.00 12.76 C ANISOU 117 CA ASN C 27 1722 1557 1569 114 -127 -30 C ATOM 118 C ASN A 27 10.099 -12.325 28.999 1.00 11.88 C ANISOU 118 C ASN C 27 1704 1323 1486 101 -111 -91 C ATOM 119 O ASN A 27 9.512 -13.192 28.365 1.00 13.35 O ANISOU 119 O ASN C 27 1638 1699 1733 -14 22 92 O ATOM 120 CB ASN A 27 8.001 -12.012 30.384 1.00 15.36 C ANISOU 120 CB ASN C 27 1870 1872 2092 -113 -256 -51 C ATOM 121 CG ASN A 27 7.414 -11.748 31.747 1.00 21.29 C ANISOU 121 CG ASN C 27 2828 2712 2546 88 -19 94 C ATOM 122 OD1 ASN A 27 8.031 -12.038 32.762 1.00 29.05 O ANISOU 122 OD1 ASN C 27 3898 4113 3024 -136 16 -61 O ATOM 123 ND2 ASN A 27 6.197 -11.159 31.772 1.00 26.74 N ANISOU 123 ND2 ASN C 27 2879 3604 3677 -176 -38 -1 N ATOM 124 N VAL A 28 11.288 -11.883 28.641 1.00 11.08 N ANISOU 124 N VAL C 28 1584 1265 1359 134 -118 27 N ATOM 125 CA VAL A 28 11.989 -12.453 27.478 1.00 11.32 C ANISOU 125 CA VAL C 28 1697 1218 1383 136 -48 -21 C ATOM 126 C VAL A 28 12.763 -13.677 27.949 1.00 11.11 C ANISOU 126 C VAL C 28 1545 1365 1311 147 8 -52 C ATOM 127 O VAL A 28 13.616 -13.547 28.819 1.00 11.66 O ANISOU 127 O VAL C 28 1741 1210 1479 331 195 76 O ATOM 128 CB VAL A 28 12.958 -11.438 26.822 1.00 11.51 C ANISOU 128 CB VAL C 28 1722 1185 1464 224 8 -103 C ATOM 129 CG1 VAL A 28 13.683 -12.090 25.646 1.00 12.13 C ANISOU 129 CG1 VAL C 28 1897 1529 1183 356 -263 -27 C ATOM 130 CG2 VAL A 28 12.228 -10.148 26.390 1.00 12.87 C ANISOU 130 CG2 VAL C 28 2122 1338 1428 443 -42 -25 C ATOM 131 N ALA A 29 12.547 -14.814 27.288 1.00 10.12 N ANISOU 131 N ALA C 29 1415 1180 1249 138 -19 -214 N ATOM 132 CA ALA A 29 13.300 -16.029 27.620 1.00 9.94 C ANISOU 132 CA ALA C 29 1377 1182 1216 143 -66 -194 C ATOM 133 C ALA A 29 14.671 -15.942 26.996 1.00 9.17 C ANISOU 133 C ALA C 29 1294 985 1205 156 51 -209 C ATOM 134 O ALA A 29 14.840 -15.469 25.870 1.00 10.78 O ANISOU 134 O ALA C 29 1537 1526 1029 18 97 -247 O ATOM 135 CB ALA A 29 12.575 -17.283 27.123 1.00 10.62 C ANISOU 135 CB ALA C 29 1451 1188 1393 -2 -85 -55 C ATOM 136 N VAL A 30 15.661 -16.406 27.768 1.00 9.78 N ANISOU 136 N VAL C 30 1403 1326 986 40 63 -328 N ATOM 137 CA VAL A 30 17.061 -16.384 27.358 1.00 10.11 C ANISOU 137 CA VAL C 30 1384 1241 1214 91 -87 -342 C ATOM 138 C VAL A 30 17.644 -17.760 27.725 1.00 9.36 C ANISOU 138 C VAL C 30 1317 1158 1079 32 -110 -308 C ATOM 139 O VAL A 30 17.539 -18.241 28.863 1.00 11.25 O ANISOU 139 O VAL C 30 1455 1497 1322 95 -250 -356 O ATOM 140 CB VAL A 30 17.839 -15.267 28.118 1.00 10.67 C ANISOU 140 CB VAL C 30 1401 1529 1122 -52 114 -355 C ATOM 141 CG1 VAL A 30 19.379 -15.337 27.794 1.00 14.07 C ANISOU 141 CG1 VAL C 30 1679 1627 2037 -179 -114 -168 C ATOM 142 CG2 VAL A 30 17.243 -13.880 27.810 1.00 12.39 C ANISOU 142 CG2 VAL C 30 1971 1413 1320 225 157 -226 C ATOM 143 N HIS A 31 18.281 -18.368 26.735 1.00 9.94 N ANISOU 143 N HIS C 31 1337 1325 1113 108 -231 -265 N ATOM 144 CA HIS A 31 19.002 -19.621 26.903 1.00 9.88 C ANISOU 144 CA HIS C 31 1258 1315 1181 94 -165 -371 C ATOM 145 C HIS A 31 20.472 -19.434 26.580 1.00 9.37 C ANISOU 145 C HIS C 31 1115 1280 1162 82 -89 -545 C ATOM 146 O HIS A 31 20.772 -18.911 25.510 1.00 12.95 O ANISOU 146 O HIS C 31 1394 2001 1523 55 -34 -636 O ATOM 147 CB HIS A 31 18.441 -20.720 26.009 1.00 10.61 C ANISOU 147 CB HIS C 31 1358 1344 1328 71 -145 -322 C ATOM 148 CG HIS A 31 17.016 -21.077 26.324 1.00 12.18 C ANISOU 148 CG HIS C 31 1493 1552 1582 -222 -35 -99 C ATOM 149 ND1 HIS A 31 16.650 -22.279 26.875 1.00 13.47 N ANISOU 149 ND1 HIS C 31 1312 1796 2009 -255 -224 -322 N ATOM 150 CD2 HIS A 31 15.874 -20.380 26.134 1.00 13.31 C ANISOU 150 CD2 HIS C 31 1485 1642 1929 -10 -163 -148 C ATOM 151 CE1 HIS A 31 15.336 -22.290 27.064 1.00 15.18 C ANISOU 151 CE1 HIS C 31 1545 1857 2363 -384 -165 -313 C ATOM 152 NE2 HIS A 31 14.828 -21.166 26.568 1.00 15.45 N ANISOU 152 NE2 HIS C 31 1725 1813 2330 -120 -15 19 N ATOM 153 N VAL A 32 21.332 -19.857 27.508 1.00 10.14 N ANISOU 153 N VAL C 32 1345 1324 1184 75 -101 -357 N ATOM 154 CA VAL A 32 22.765 -19.776 27.312 1.00 10.79 C ANISOU 154 CA VAL C 32 1359 1261 1480 -49 -80 -382 C ATOM 155 C VAL A 32 23.320 -21.180 27.121 1.00 11.22 C ANISOU 155 C VAL C 32 1184 1500 1577 61 -148 -250 C ATOM 156 O VAL A 32 22.915 -22.119 27.835 1.00 11.59 O ANISOU 156 O VAL C 32 1380 1317 1705 113 -136 -487 O ATOM 157 CB VAL A 32 23.461 -19.086 28.502 1.00 11.05 C ANISOU 157 CB VAL C 32 1458 1388 1350 -149 -44 -315 C ATOM 158 CG1 VAL A 32 24.994 -18.909 28.239 1.00 12.66 C ANISOU 158 CG1 VAL C 32 1316 1547 1944 -65 -212 -186 C ATOM 159 CG2 VAL A 32 22.783 -17.782 28.868 1.00 12.97 C ANISOU 159 CG2 VAL C 32 1659 1402 1866 -48 -76 -71 C ATOM 160 N PHE A 33 24.184 -21.320 26.128 1.00 10.21 N ANISOU 160 N PHE C 33 1020 1245 1615 -98 -331 -397 N ATOM 161 CA PHE A 33 24.860 -22.553 25.804 1.00 11.21 C ANISOU 161 CA PHE C 33 1251 1242 1763 17 -270 -280 C ATOM 162 C PHE A 33 26.370 -22.340 25.857 1.00 11.44 C ANISOU 162 C PHE C 33 1210 1286 1850 30 -110 -404 C ATOM 163 O PHE A 33 26.855 -21.241 25.653 1.00 11.46 O ANISOU 163 O PHE C 33 1209 1200 1943 -39 -176 -498 O ATOM 164 CB PHE A 33 24.477 -23.072 24.419 1.00 12.43 C ANISOU 164 CB PHE C 33 1401 1326 1993 70 -134 -207 C ATOM 165 CG PHE A 33 22.994 -23.180 24.226 1.00 12.65 C ANISOU 165 CG PHE C 33 1562 1499 1744 16 -163 -67 C ATOM 166 CD1 PHE A 33 22.231 -22.102 23.872 1.00 12.55 C ANISOU 166 CD1 PHE C 33 1414 1652 1700 9 -171 113 C ATOM 167 CD2 PHE A 33 22.368 -24.368 24.438 1.00 14.12 C ANISOU 167 CD2 PHE C 33 1697 1471 2194 19 45 11 C ATOM 168 CE1 PHE A 33 20.814 -22.211 23.721 1.00 13.26 C ANISOU 168 CE1 PHE C 33 1513 1597 1928 97 -178 -47 C ATOM 169 CE2 PHE A 33 21.000 -24.494 24.280 1.00 14.78 C ANISOU 169 CE2 PHE C 33 1680 1514 2420 -286 -18 -93 C ATOM 170 CZ PHE A 33 20.230 -23.423 23.942 1.00 14.80 C ANISOU 170 CZ PHE C 33 1327 1882 2414 -158 -6 -59 C ATOM 171 N ARG A 34 27.101 -23.440 26.029 1.00 12.79 N ANISOU 171 N ARG C 34 1349 1338 2171 33 -246 -381 N ATOM 172 CA ARG A 34 28.567 -23.407 25.986 1.00 13.01 C ANISOU 172 CA ARG C 34 1472 1400 2068 -43 -309 -232 C ATOM 173 C ARG A 34 29.022 -24.495 25.072 1.00 14.25 C ANISOU 173 C ARG C 34 1678 1552 2183 1 -425 -198 C ATOM 174 O ARG A 34 28.555 -25.613 25.178 1.00 14.69 O ANISOU 174 O ARG C 34 1626 1328 2625 -46 -585 -258 O ATOM 175 CB ARG A 34 29.141 -23.591 27.379 1.00 13.73 C ANISOU 175 CB ARG C 34 1578 1586 2053 53 -252 -123 C ATOM 176 CG ARG A 34 30.648 -23.550 27.455 1.00 13.74 C ANISOU 176 CG ARG C 34 1588 1579 2053 97 -167 -131 C ATOM 177 CD ARG A 34 31.159 -23.796 28.897 1.00 15.52 C ANISOU 177 CD ARG C 34 2001 1751 2144 101 -77 -224 C ATOM 178 NE ARG A 34 32.637 -23.800 28.921 1.00 16.45 N ANISOU 178 NE ARG C 34 2303 1839 2108 209 177 -315 N ATOM 179 CZ ARG A 34 33.409 -24.819 28.588 1.00 17.02 C ANISOU 179 CZ ARG C 34 2172 2170 2122 176 0 -67 C ATOM 180 NH1 ARG A 34 32.874 -25.975 28.281 1.00 16.80 N ANISOU 180 NH1 ARG C 34 1998 2137 2245 204 71 -411 N ATOM 181 NH2 ARG A 34 34.725 -24.670 28.615 1.00 16.95 N ANISOU 181 NH2 ARG C 34 1916 1885 2639 219 151 -227 N ATOM 182 N LYS A 35 29.964 -24.209 24.215 1.00 13.88 N ANISOU 182 N LYS C 35 1575 1401 2298 -140 -313 -178 N ATOM 183 CA ALYS A 35 30.455 -25.207 23.302 0.50 15.78 C ANISOU 183 CA ALYS C 35 1855 1876 2263 -82 -201 -52 C ATOM 184 C LYS A 35 31.295 -26.263 24.050 1.00 16.05 C ANISOU 184 C LYS C 35 1910 1810 2375 -25 -196 18 C ATOM 185 O LYS A 35 32.206 -25.945 24.823 1.00 16.37 O ANISOU 185 O LYS C 35 1990 1604 2623 131 -143 183 O ATOM 186 CB ALYS A 35 31.235 -24.462 22.218 0.50 15.84 C ANISOU 186 CB ALYS C 35 1919 1862 2234 -119 -259 -41 C ATOM 187 CG ALYS A 35 31.541 -25.296 21.000 0.50 16.76 C ANISOU 187 CG ALYS C 35 2050 2183 2136 3 -167 203 C ATOM 188 CD ALYS A 35 32.180 -24.348 19.973 0.50 18.46 C ANISOU 188 CD ALYS C 35 2205 2473 2333 -4 -260 -3 C ATOM 189 CE ALYS A 35 32.305 -24.894 18.569 0.50 21.90 C ANISOU 189 CE ALYS C 35 2857 2847 2614 9 -62 79 C ATOM 190 NZ ALYS A 35 32.911 -23.817 17.713 0.50 23.42 N ANISOU 190 NZ ALYS C 35 3044 3161 2691 -135 -287 -123 N ATOM 191 N ALA A 36 30.943 -27.523 23.846 1.00 17.46 N ANISOU 191 N ALA C 36 2162 2053 2419 -27 -27 -49 N ATOM 192 CA ALA A 36 31.591 -28.651 24.518 1.00 19.23 C ANISOU 192 CA ALA C 36 2476 2265 2564 73 -27 -25 C ATOM 193 C ALA A 36 32.776 -29.107 23.734 1.00 21.00 C ANISOU 193 C ALA C 36 2780 2566 2633 150 20 65 C ATOM 194 O ALA A 36 33.014 -28.657 22.605 1.00 21.61 O ANISOU 194 O ALA C 36 2741 2624 2846 385 45 108 O ATOM 195 CB ALA A 36 30.591 -29.748 24.656 1.00 20.06 C ANISOU 195 CB ALA C 36 2507 2445 2670 31 -39 -151 C ATOM 196 N ALA A 37 33.502 -30.053 24.349 1.00 23.13 N ANISOU 196 N ALA C 37 2987 2889 2912 390 101 190 N ATOM 197 CA ALA A 37 34.716 -30.651 23.767 1.00 24.97 C ANISOU 197 CA ALA C 37 3209 3181 3094 248 76 207 C ATOM 198 C ALA A 37 34.432 -31.270 22.410 1.00 26.43 C ANISOU 198 C ALA C 37 3458 3362 3221 218 33 246 C ATOM 199 O ALA A 37 35.319 -31.298 21.559 1.00 28.93 O ANISOU 199 O ALA C 37 3734 3823 3434 362 6 318 O ATOM 200 CB ALA A 37 35.277 -31.732 24.723 1.00 25.92 C ANISOU 200 CB ALA C 37 3260 3203 3384 341 135 164 C ATOM 201 N ASP A 38 33.211 -31.767 22.244 1.00 27.55 N ANISOU 201 N ASP C 38 3656 3330 3483 311 61 298 N ATOM 202 CA ASP A 38 32.798 -32.412 21.003 1.00 28.62 C ANISOU 202 CA ASP C 38 3769 3524 3579 159 90 208 C ATOM 203 C ASP A 38 32.155 -31.466 20.001 1.00 28.89 C ANISOU 203 C ASP C 38 3899 3472 3606 127 82 199 C ATOM 204 O ASP A 38 31.517 -31.910 19.043 1.00 29.71 O ANISOU 204 O ASP C 38 4160 3742 3386 113 79 416 O ATOM 205 CB ASP A 38 31.862 -33.576 21.337 1.00 29.95 C ANISOU 205 CB ASP C 38 3977 3473 3928 115 108 167 C ATOM 206 CG ASP A 38 30.535 -33.154 21.929 1.00 33.23 C ANISOU 206 CG ASP C 38 4417 3811 4397 129 31 145 C ATOM 207 OD1 ASP A 38 30.251 -31.937 22.106 1.00 32.03 O ANISOU 207 OD1 ASP C 38 4780 2893 4495 -76 219 304 O ATOM 208 OD2 ASP A 38 29.744 -34.080 22.236 1.00 40.03 O ANISOU 208 OD2 ASP C 38 5282 4469 5459 -142 -93 47 O ATOM 209 N ASP A 39 32.289 -30.160 20.254 1.00 28.89 N ANISOU 209 N ASP C 39 3895 3516 3565 110 26 164 N ATOM 210 CA ASP A 39 31.794 -29.104 19.367 1.00 29.15 C ANISOU 210 CA ASP C 39 3808 3577 3690 69 20 82 C ATOM 211 C ASP A 39 30.287 -28.901 19.356 1.00 28.50 C ANISOU 211 C ASP C 39 3756 3451 3621 53 60 70 C ATOM 212 O ASP A 39 29.803 -28.091 18.575 1.00 30.72 O ANISOU 212 O ASP C 39 4054 3746 3869 200 184 -94 O ATOM 213 CB ASP A 39 32.333 -29.264 17.942 1.00 30.99 C ANISOU 213 CB ASP C 39 4041 3897 3834 82 41 136 C ATOM 214 CG ASP A 39 33.743 -28.802 17.829 1.00 36.51 C ANISOU 214 CG ASP C 39 4646 4578 4645 -117 -89 -1 C ATOM 215 OD1 ASP A 39 33.975 -27.620 18.181 1.00 41.60 O ANISOU 215 OD1 ASP C 39 5480 4914 5410 -33 -166 239 O ATOM 216 OD2 ASP A 39 34.621 -29.614 17.418 1.00 44.58 O ANISOU 216 OD2 ASP C 39 5639 5479 5820 206 -41 144 O ATOM 217 N THR A 40 29.557 -29.574 20.238 1.00 26.20 N ANISOU 217 N THR C 40 3487 3028 3440 9 110 176 N ATOM 218 CA THR A 40 28.109 -29.384 20.381 1.00 24.88 C ANISOU 218 CA THR C 40 3300 2752 3398 28 53 194 C ATOM 219 C THR A 40 27.832 -28.227 21.345 1.00 22.28 C ANISOU 219 C THR C 40 2794 2481 3189 -67 -7 249 C ATOM 220 O THR A 40 28.700 -27.884 22.156 1.00 20.59 O ANISOU 220 O THR C 40 2375 2210 3238 105 96 139 O ATOM 221 CB THR A 40 27.406 -30.680 20.910 1.00 24.94 C ANISOU 221 CB THR C 40 3442 2647 3388 -62 65 307 C ATOM 222 OG1 THR A 40 27.753 -30.946 22.267 1.00 27.60 O ANISOU 222 OG1 THR C 40 3876 2455 4155 -160 86 72 O ATOM 223 CG2 THR A 40 27.764 -31.919 20.065 1.00 25.77 C ANISOU 223 CG2 THR C 40 3683 2646 3462 128 -107 299 C ATOM 224 N TRP A 41 26.644 -27.639 21.248 1.00 20.76 N ANISOU 224 N TRP C 41 2601 2154 3130 -175 -7 181 N ATOM 225 CA TRP A 41 26.182 -26.596 22.182 1.00 19.40 C ANISOU 225 CA TRP C 41 2373 2220 2775 -263 -80 36 C ATOM 226 C TRP A 41 25.486 -27.183 23.382 1.00 18.84 C ANISOU 226 C TRP C 41 2287 2068 2803 -338 -138 0 C ATOM 227 O TRP A 41 24.300 -27.598 23.307 1.00 22.69 O ANISOU 227 O TRP C 41 2409 2912 3298 -391 -59 -224 O ATOM 228 CB TRP A 41 25.213 -25.619 21.488 1.00 18.46 C ANISOU 228 CB TRP C 41 2164 2234 2613 -248 -15 101 C ATOM 229 CG TRP A 41 25.848 -24.706 20.535 1.00 19.72 C ANISOU 229 CG TRP C 41 2358 2433 2699 -151 -12 102 C ATOM 230 CD1 TRP A 41 25.607 -24.656 19.225 1.00 21.99 C ANISOU 230 CD1 TRP C 41 2658 2849 2847 -348 113 20 C ATOM 231 CD2 TRP A 41 26.796 -23.669 20.820 1.00 18.78 C ANISOU 231 CD2 TRP C 41 2168 2390 2577 -59 83 -150 C ATOM 232 NE1 TRP A 41 26.347 -23.661 18.637 1.00 23.82 N ANISOU 232 NE1 TRP C 41 2976 3110 2963 -321 274 -107 N ATOM 233 CE2 TRP A 41 27.081 -23.034 19.604 1.00 21.91 C ANISOU 233 CE2 TRP C 41 2768 2850 2703 -410 102 16 C ATOM 234 CE3 TRP A 41 27.369 -23.173 21.987 1.00 16.63 C ANISOU 234 CE3 TRP C 41 1917 2024 2378 -16 -130 11 C ATOM 235 CZ2 TRP A 41 27.947 -21.961 19.520 1.00 21.20 C ANISOU 235 CZ2 TRP C 41 2732 2507 2816 -350 -11 -237 C ATOM 236 CZ3 TRP A 41 28.228 -22.117 21.883 1.00 18.16 C ANISOU 236 CZ3 TRP C 41 2112 2029 2759 199 159 15 C ATOM 237 CH2 TRP A 41 28.531 -21.559 20.665 1.00 20.24 C ANISOU 237 CH2 TRP C 41 2435 2360 2892 -261 26 -43 C ATOM 238 N GLU A 42 26.155 -27.179 24.500 1.00 16.78 N ANISOU 238 N GLU C 42 1908 1847 2620 -105 -315 -88 N ATOM 239 CA AGLU A 42 25.609 -27.741 25.728 0.50 17.72 C ANISOU 239 CA AGLU C 42 2158 1936 2636 -136 -252 -126 C ATOM 240 C GLU A 42 24.797 -26.685 26.471 1.00 16.66 C ANISOU 240 C GLU C 42 2012 1778 2538 -113 -347 -173 C ATOM 241 O GLU A 42 25.280 -25.582 26.644 1.00 15.64 O ANISOU 241 O GLU C 42 1745 1531 2666 -107 -336 -225 O ATOM 242 CB AGLU A 42 26.759 -28.166 26.638 0.50 18.55 C ANISOU 242 CB AGLU C 42 2304 2132 2611 -114 -208 -142 C ATOM 243 CG AGLU A 42 26.337 -28.933 27.874 0.50 18.94 C ANISOU 243 CG AGLU C 42 2387 2099 2711 -77 -250 -216 C ATOM 244 CD AGLU A 42 27.482 -29.225 28.803 0.50 22.60 C ANISOU 244 CD AGLU C 42 2795 2780 3011 -138 -114 -175 C ATOM 245 OE1AGLU A 42 28.535 -28.552 28.717 0.50 27.26 O ANISOU 245 OE1AGLU C 42 2961 3835 3560 -174 143 -52 O ATOM 246 OE2AGLU A 42 27.332 -30.142 29.628 0.50 27.29 O ANISOU 246 OE2AGLU C 42 3570 3261 3536 -16 -51 -408 O ATOM 247 N PRO A 43 23.588 -27.026 26.961 1.00 15.62 N ANISOU 247 N PRO C 43 1902 1508 2522 -152 -349 -186 N ATOM 248 CA PRO A 43 22.865 -26.066 27.764 1.00 15.54 C ANISOU 248 CA PRO C 43 1960 1663 2279 -207 -306 -206 C ATOM 249 C PRO A 43 23.656 -25.685 28.990 1.00 16.33 C ANISOU 249 C PRO C 43 1953 1852 2397 28 -122 -274 C ATOM 250 O PRO A 43 24.221 -26.541 29.685 1.00 18.89 O ANISOU 250 O PRO C 43 2652 2013 2512 211 233 -313 O ATOM 251 CB PRO A 43 21.529 -26.798 28.096 1.00 16.20 C ANISOU 251 CB PRO C 43 1923 1856 2374 -224 -390 -229 C ATOM 252 CG PRO A 43 21.401 -27.823 27.033 1.00 19.42 C ANISOU 252 CG PRO C 43 2262 2191 2923 -261 -402 -83 C ATOM 253 CD PRO A 43 22.821 -28.275 26.799 1.00 18.30 C ANISOU 253 CD PRO C 43 2215 1798 2940 -200 -390 25 C ATOM 254 N PHE A 44 23.737 -24.376 29.237 1.00 13.72 N ANISOU 254 N PHE C 44 1626 1568 2015 35 -142 -331 N ATOM 255 CA PHE A 44 24.545 -23.836 30.324 1.00 13.24 C ANISOU 255 CA PHE C 44 1531 1698 1801 43 -99 -470 C ATOM 256 C PHE A 44 23.731 -23.152 31.420 1.00 13.58 C ANISOU 256 C PHE C 44 1553 1719 1887 52 -10 -448 C ATOM 257 O PHE A 44 23.937 -23.339 32.613 1.00 14.73 O ANISOU 257 O PHE C 44 1615 2048 1932 201 40 -799 O ATOM 258 CB PHE A 44 25.600 -22.876 29.731 1.00 13.33 C ANISOU 258 CB PHE C 44 1567 1837 1660 12 -33 -457 C ATOM 259 CG PHE A 44 26.506 -22.275 30.759 1.00 13.16 C ANISOU 259 CG PHE C 44 1360 1945 1693 -9 -86 -514 C ATOM 260 CD1 PHE A 44 27.587 -22.997 31.267 1.00 15.85 C ANISOU 260 CD1 PHE C 44 1581 2325 2115 -247 143 -643 C ATOM 261 CD2 PHE A 44 26.320 -21.012 31.225 1.00 13.39 C ANISOU 261 CD2 PHE C 44 1085 2094 1906 -65 -36 -300 C ATOM 262 CE1 PHE A 44 28.407 -22.450 32.257 1.00 14.82 C ANISOU 262 CE1 PHE C 44 1617 2554 1459 -92 131 -636 C ATOM 263 CE2 PHE A 44 27.101 -20.476 32.187 1.00 15.47 C ANISOU 263 CE2 PHE C 44 1466 2519 1893 5 35 -329 C ATOM 264 CZ PHE A 44 28.174 -21.227 32.719 1.00 14.51 C ANISOU 264 CZ PHE C 44 1448 2588 1473 -267 -18 -515 C ATOM 265 N ALA A 45 22.788 -22.313 31.031 1.00 12.31 N ANISOU 265 N ALA C 45 1466 1547 1661 113 -40 -546 N ATOM 266 CA ALA A 45 21.890 -21.636 31.957 1.00 11.78 C ANISOU 266 CA ALA C 45 1221 1633 1619 167 51 -373 C ATOM 267 C ALA A 45 20.737 -21.044 31.166 1.00 10.93 C ANISOU 267 C ALA C 45 1202 1510 1438 103 12 -389 C ATOM 268 O ALA A 45 20.857 -20.846 29.966 1.00 12.43 O ANISOU 268 O ALA C 45 1322 1857 1543 120 -230 -503 O ATOM 269 CB ALA A 45 22.592 -20.542 32.654 1.00 14.24 C ANISOU 269 CB ALA C 45 1644 1840 1925 98 129 -204 C ATOM 270 N SER A 46 19.637 -20.746 31.871 1.00 11.00 N ANISOU 270 N SER C 46 1247 1546 1383 180 -58 -320 N ATOM 271 CA SER A 46 18.538 -20.061 31.232 1.00 9.57 C ANISOU 271 CA SER C 46 1058 1272 1304 25 -132 -370 C ATOM 272 C SER A 46 17.771 -19.234 32.238 1.00 10.05 C ANISOU 272 C SER C 46 1153 1310 1355 103 -102 -363 C ATOM 273 O SER A 46 17.901 -19.452 33.417 1.00 11.59 O ANISOU 273 O SER C 46 1557 1615 1229 51 -203 -437 O ATOM 274 CB SER A 46 17.613 -21.019 30.457 1.00 10.82 C ANISOU 274 CB SER C 46 1275 1396 1440 167 -53 -141 C ATOM 275 OG SER A 46 16.937 -21.919 31.322 1.00 12.06 O ANISOU 275 OG SER C 46 1379 1541 1659 -121 -358 -623 O ATOM 276 N GLY A 47 16.941 -18.323 31.750 1.00 10.03 N ANISOU 276 N GLY C 47 1212 1395 1202 110 -55 -332 N ATOM 277 CA GLY A 47 16.126 -17.533 32.624 1.00 10.70 C ANISOU 277 CA GLY C 47 1478 1389 1197 77 58 -208 C ATOM 278 C GLY A 47 15.241 -16.606 31.796 1.00 10.47 C ANISOU 278 C GLY C 47 1530 1258 1188 157 7 -227 C ATOM 279 O GLY A 47 15.139 -16.745 30.559 1.00 11.01 O ANISOU 279 O GLY C 47 1558 1405 1220 28 -26 -197 O ATOM 280 N LYS A 48 14.592 -15.667 32.474 1.00 11.14 N ANISOU 280 N LYS C 48 1749 1275 1208 147 78 -216 N ATOM 281 CA ALYS A 48 13.668 -14.685 31.845 0.50 12.15 C ANISOU 281 CA ALYS C 48 1720 1431 1465 152 4 -141 C ATOM 282 C LYS A 48 14.014 -13.295 32.316 1.00 11.29 C ANISOU 282 C LYS C 48 1517 1414 1358 188 -93 -27 C ATOM 283 O LYS A 48 14.319 -13.120 33.472 1.00 13.26 O ANISOU 283 O LYS C 48 2191 1401 1445 90 -16 -236 O ATOM 284 CB ALYS A 48 12.216 -14.845 32.321 0.50 14.61 C ANISOU 284 CB ALYS C 48 1959 1798 1794 112 -7 -36 C ATOM 285 CG ALYS A 48 11.583 -16.147 32.166 0.50 17.60 C ANISOU 285 CG ALYS C 48 2408 2072 2204 41 -30 59 C ATOM 286 CD ALYS A 48 10.723 -16.236 30.939 0.50 18.46 C ANISOU 286 CD ALYS C 48 2587 2149 2275 -6 92 242 C ATOM 287 CE ALYS A 48 9.694 -17.350 31.143 0.50 18.07 C ANISOU 287 CE ALYS C 48 2659 1929 2277 96 -92 -66 C ATOM 288 NZ ALYS A 48 8.935 -17.821 30.037 0.50 10.70 N ANISOU 288 NZ ALYS C 48 2019 836 1209 68 -420 -446 N ATOM 289 N THR A 49 13.853 -12.292 31.468 1.00 10.91 N ANISOU 289 N THR C 49 1443 1371 1331 224 47 -96 N ATOM 290 CA THR A 49 14.066 -10.935 31.945 1.00 10.84 C ANISOU 290 CA THR C 49 1558 1416 1143 201 -40 -59 C ATOM 291 C THR A 49 12.925 -10.531 32.889 1.00 11.36 C ANISOU 291 C THR C 49 1704 1489 1124 188 54 -154 C ATOM 292 O THR A 49 11.774 -10.928 32.718 1.00 12.36 O ANISOU 292 O THR C 49 1754 1660 1280 135 -75 -194 O ATOM 293 CB THR A 49 14.175 -9.947 30.781 1.00 10.32 C ANISOU 293 CB THR C 49 1511 1290 1119 271 -71 -141 C ATOM 294 OG1 THR A 49 12.949 -9.958 30.037 1.00 10.78 O ANISOU 294 OG1 THR C 49 1462 1264 1367 288 158 -97 O ATOM 295 CG2 THR A 49 15.382 -10.219 29.852 1.00 11.79 C ANISOU 295 CG2 THR C 49 1653 1702 1125 352 -126 -167 C ATOM 296 N SER A 50 13.289 -9.710 33.851 1.00 12.41 N ANISOU 296 N SER C 50 1703 1613 1398 126 -222 0 N ATOM 297 CA SER A 50 12.382 -9.207 34.826 1.00 13.75 C ANISOU 297 CA SER C 50 1946 1845 1433 241 -251 113 C ATOM 298 C SER A 50 11.629 -7.999 34.326 1.00 14.91 C ANISOU 298 C SER C 50 2064 2004 1595 246 -308 72 C ATOM 299 O SER A 50 11.773 -7.587 33.189 1.00 13.20 O ANISOU 299 O SER C 50 1968 1661 1385 351 -177 -9 O ATOM 300 CB SER A 50 13.251 -8.820 36.044 1.00 15.16 C ANISOU 300 CB SER C 50 2131 2132 1496 354 -198 166 C ATOM 301 OG SER A 50 13.977 -7.628 35.732 1.00 17.29 O ANISOU 301 OG SER C 50 2175 2231 2162 358 -41 518 O ATOM 302 N GLU A 51 10.909 -7.359 35.247 1.00 14.94 N ANISOU 302 N GLU C 51 2110 2036 1529 345 -363 37 N ATOM 303 CA CGLU A 51 10.181 -6.129 34.872 0.62 16.06 C ANISOU 303 CA CGLU C 51 2196 2140 1763 319 -241 112 C ATOM 304 C GLU A 51 11.119 -4.969 34.503 1.00 16.23 C ANISOU 304 C GLU C 51 2314 2128 1722 339 -216 235 C ATOM 305 O GLU A 51 10.687 -4.040 33.841 1.00 17.82 O ANISOU 305 O GLU C 51 2730 2018 2022 391 -132 48 O ATOM 306 CB CGLU A 51 9.123 -5.737 35.929 0.62 17.93 C ANISOU 306 CB CGLU C 51 2284 2486 2043 303 -295 155 C ATOM 307 CG CGLU A 51 8.085 -6.856 36.153 0.62 22.53 C ANISOU 307 CG CGLU C 51 2945 2865 2749 165 -235 39 C ATOM 308 CD CGLU A 51 6.813 -6.762 35.336 0.62 28.06 C ANISOU 308 CD CGLU C 51 3678 3646 3334 78 -46 72 C ATOM 309 OE1CGLU A 51 6.262 -7.843 35.017 0.62 31.03 O ANISOU 309 OE1CGLU C 51 4130 3771 3888 -16 -190 -1 O ATOM 310 OE2CGLU A 51 6.322 -5.642 35.048 0.62 32.26 O ANISOU 310 OE2CGLU C 51 4648 3751 3858 139 -12 116 O ATOM 311 N SER A 52 12.380 -5.025 34.864 1.00 14.99 N ANISOU 311 N SER C 52 2227 2043 1423 364 -211 269 N ATOM 312 CA SER A 52 13.348 -4.053 34.459 1.00 14.88 C ANISOU 312 CA SER C 52 2065 2001 1587 242 -97 119 C ATOM 313 C SER A 52 14.054 -4.396 33.135 1.00 12.90 C ANISOU 313 C SER C 52 1876 1670 1352 243 6 -80 C ATOM 314 O SER A 52 14.948 -3.673 32.675 1.00 14.54 O ANISOU 314 O SER C 52 1992 1709 1822 111 176 -11 O ATOM 315 CB SER A 52 14.405 -3.875 35.545 1.00 17.45 C ANISOU 315 CB SER C 52 2433 2371 1825 27 -202 303 C ATOM 316 OG SER A 52 15.178 -5.035 35.604 1.00 21.39 O ANISOU 316 OG SER C 52 3000 3005 2121 40 211 -463 O ATOM 317 N GLY A 53 13.670 -5.524 32.539 1.00 11.66 N ANISOU 317 N GLY C 53 1717 1589 1124 152 -23 -75 N ATOM 318 CA GLY A 53 14.329 -6.014 31.314 1.00 11.95 C ANISOU 318 CA GLY C 53 1761 1649 1128 218 -23 -90 C ATOM 319 C GLY A 53 15.661 -6.673 31.535 1.00 11.19 C ANISOU 319 C GLY C 53 1586 1577 1088 109 -67 -63 C ATOM 320 O GLY A 53 16.352 -6.981 30.599 1.00 11.15 O ANISOU 320 O GLY C 53 1550 1563 1123 70 -19 44 O ATOM 321 N GLU A 54 16.000 -6.965 32.786 1.00 11.55 N ANISOU 321 N GLU C 54 1632 1640 1116 130 -100 -69 N ATOM 322 CA GLU A 54 17.288 -7.555 33.137 1.00 12.33 C ANISOU 322 CA GLU C 54 1723 1724 1235 134 -37 -107 C ATOM 323 C GLU A 54 17.129 -8.988 33.602 1.00 10.15 C ANISOU 323 C GLU C 54 1261 1587 1005 119 -54 -197 C ATOM 324 O GLU A 54 16.115 -9.384 34.200 1.00 11.96 O ANISOU 324 O GLU C 54 1343 1840 1360 227 -213 -218 O ATOM 325 CB GLU A 54 17.986 -6.751 34.269 1.00 14.23 C ANISOU 325 CB GLU C 54 1866 1916 1622 113 82 -21 C ATOM 326 CG GLU A 54 18.256 -5.292 33.847 1.00 16.82 C ANISOU 326 CG GLU C 54 2296 2185 1906 13 186 97 C ATOM 327 CD GLU A 54 19.004 -4.431 34.835 1.00 21.17 C ANISOU 327 CD GLU C 54 3050 2327 2667 -187 34 85 C ATOM 328 OE1 GLU A 54 19.343 -4.923 35.910 1.00 25.49 O ANISOU 328 OE1 GLU C 54 3788 2718 3176 -49 612 385 O ATOM 329 OE2 GLU A 54 19.235 -3.257 34.472 1.00 28.65 O ANISOU 329 OE2 GLU C 54 4366 2489 4030 -273 276 -112 O ATOM 330 N LEU A 55 18.176 -9.735 33.357 1.00 11.40 N ANISOU 330 N LEU C 55 1390 1576 1364 123 -210 -167 N ATOM 331 CA LEU A 55 18.287 -11.105 33.778 1.00 11.14 C ANISOU 331 CA LEU C 55 1329 1616 1288 189 -202 -231 C ATOM 332 C LEU A 55 19.623 -11.253 34.443 1.00 11.73 C ANISOU 332 C LEU C 55 1622 1657 1177 174 -106 -125 C ATOM 333 O LEU A 55 20.682 -11.151 33.826 1.00 12.76 O ANISOU 333 O LEU C 55 1637 1757 1455 284 -31 -188 O ATOM 334 CB LEU A 55 18.190 -12.055 32.590 1.00 11.94 C ANISOU 334 CB LEU C 55 1426 1722 1388 169 -48 -173 C ATOM 335 CG LEU A 55 18.488 -13.511 32.819 1.00 11.42 C ANISOU 335 CG LEU C 55 1320 1777 1240 221 -68 -32 C ATOM 336 CD1 LEU A 55 17.693 -14.118 33.952 1.00 13.72 C ANISOU 336 CD1 LEU C 55 1789 2041 1382 215 22 -277 C ATOM 337 CD2 LEU A 55 18.165 -14.284 31.536 1.00 12.77 C ANISOU 337 CD2 LEU C 55 1758 1894 1197 136 -78 -101 C ATOM 338 N HIS A 56 19.495 -11.507 35.742 1.00 14.49 N ANISOU 338 N HIS C 56 2152 1886 1467 153 48 -221 N ATOM 339 CA HIS A 56 20.579 -11.703 36.662 1.00 16.87 C ANISOU 339 CA HIS C 56 2424 2119 1864 72 85 -115 C ATOM 340 C HIS A 56 20.567 -13.153 37.142 1.00 17.32 C ANISOU 340 C HIS C 56 2433 2269 1878 86 118 -265 C ATOM 341 O HIS A 56 19.603 -13.892 37.011 1.00 18.15 O ANISOU 341 O HIS C 56 2519 2338 2037 106 232 -554 O ATOM 342 CB HIS A 56 20.428 -10.774 37.916 1.00 18.20 C ANISOU 342 CB HIS C 56 2636 2443 1836 66 205 -18 C ATOM 343 CG HIS A 56 20.467 -9.317 37.609 1.00 21.22 C ANISOU 343 CG HIS C 56 2929 2661 2471 8 105 235 C ATOM 344 ND1 HIS A 56 21.654 -8.623 37.544 1.00 26.74 N ANISOU 344 ND1 HIS C 56 3264 3279 3615 -231 440 17 N ATOM 345 CD2 HIS A 56 19.512 -8.453 37.219 1.00 25.18 C ANISOU 345 CD2 HIS C 56 3157 3371 3036 143 294 135 C ATOM 346 CE1 HIS A 56 21.412 -7.363 37.219 1.00 27.66 C ANISOU 346 CE1 HIS C 56 3485 3355 3666 -89 171 -138 C ATOM 347 NE2 HIS A 56 20.114 -7.233 37.020 1.00 24.53 N ANISOU 347 NE2 HIS C 56 3166 3326 2825 98 204 101 N ATOM 348 N GLY A 57 21.672 -13.536 37.705 1.00 17.32 N ANISOU 348 N GLY C 57 2319 2287 1974 136 -41 -190 N ATOM 349 CA GLY A 57 21.739 -14.846 38.345 1.00 16.74 C ANISOU 349 CA GLY C 57 2220 2213 1924 256 -39 -255 C ATOM 350 C GLY A 57 21.906 -16.052 37.439 1.00 15.97 C ANISOU 350 C GLY C 57 2000 2025 2040 216 -165 -217 C ATOM 351 O GLY A 57 21.695 -17.159 37.881 1.00 18.60 O ANISOU 351 O GLY C 57 2623 2092 2349 364 -167 -329 O ATOM 352 N LEU A 58 22.318 -15.858 36.191 1.00 14.36 N ANISOU 352 N LEU C 58 1629 1912 1915 58 -116 -304 N ATOM 353 CA LEU A 58 22.464 -16.989 35.296 1.00 14.11 C ANISOU 353 CA LEU C 58 1516 1859 1985 84 -12 -287 C ATOM 354 C LEU A 58 23.570 -17.945 35.747 1.00 13.65 C ANISOU 354 C LEU C 58 1530 1844 1809 72 17 -226 C ATOM 355 O LEU A 58 23.415 -19.157 35.579 1.00 15.47 O ANISOU 355 O LEU C 58 1912 2002 1960 164 234 -208 O ATOM 356 CB LEU A 58 22.773 -16.466 33.899 1.00 13.96 C ANISOU 356 CB LEU C 58 1575 1750 1979 125 -3 -254 C ATOM 357 CG LEU A 58 21.558 -15.957 33.125 1.00 13.28 C ANISOU 357 CG LEU C 58 1239 1804 2003 175 195 -427 C ATOM 358 CD1 LEU A 58 22.030 -15.176 31.913 1.00 13.71 C ANISOU 358 CD1 LEU C 58 1649 1790 1767 109 69 -420 C ATOM 359 CD2 LEU A 58 20.740 -17.167 32.679 1.00 16.19 C ANISOU 359 CD2 LEU C 58 1645 2087 2417 -71 464 -579 C ATOM 360 N THR A 59 24.673 -17.404 36.280 1.00 13.39 N ANISOU 360 N THR C 59 1433 1734 1919 151 17 -159 N ATOM 361 CA THR A 59 25.825 -18.240 36.586 1.00 14.10 C ANISOU 361 CA THR C 59 1582 1857 1918 192 30 -306 C ATOM 362 C THR A 59 26.635 -17.670 37.699 1.00 14.57 C ANISOU 362 C THR C 59 1711 1954 1868 263 5 -205 C ATOM 363 O THR A 59 26.313 -16.647 38.243 1.00 18.06 O ANISOU 363 O THR C 59 2143 2465 2251 568 315 -7 O ATOM 364 CB THR A 59 26.679 -18.461 35.322 1.00 13.94 C ANISOU 364 CB THR C 59 1393 2006 1895 187 9 -230 C ATOM 365 OG1 THR A 59 27.629 -19.507 35.549 1.00 14.44 O ANISOU 365 OG1 THR C 59 1448 2052 1987 349 -48 -635 O ATOM 366 CG2 THR A 59 27.360 -17.172 34.805 1.00 15.14 C ANISOU 366 CG2 THR C 59 1835 2066 1850 269 4 -478 C ATOM 367 N THR A 60 27.735 -18.338 38.018 1.00 16.45 N ANISOU 367 N THR C 60 2008 2131 2111 250 301 -278 N ATOM 368 CA THR A 60 28.609 -17.964 39.130 1.00 16.95 C ANISOU 368 CA THR C 60 2199 2176 2066 185 252 -258 C ATOM 369 C THR A 60 29.987 -17.777 38.544 1.00 17.00 C ANISOU 369 C THR C 60 2254 2223 1981 92 262 -232 C ATOM 370 O THR A 60 30.322 -18.327 37.483 1.00 16.15 O ANISOU 370 O THR C 60 2095 2199 1841 111 350 -243 O ATOM 371 CB THR A 60 28.670 -19.042 40.247 1.00 16.58 C ANISOU 371 CB THR C 60 2205 2330 1764 113 177 -213 C ATOM 372 OG1 THR A 60 29.225 -20.259 39.725 1.00 17.00 O ANISOU 372 OG1 THR C 60 2081 2408 1968 172 9 -552 O ATOM 373 CG2 THR A 60 27.245 -19.303 40.774 1.00 20.36 C ANISOU 373 CG2 THR C 60 2541 2739 2456 333 -193 -355 C ATOM 374 N GLU A 61 30.848 -17.037 39.243 1.00 18.75 N ANISOU 374 N GLU C 61 2431 2480 2213 54 301 -53 N ATOM 375 CA AGLU A 61 32.252 -16.927 38.866 0.50 19.09 C ANISOU 375 CA AGLU C 61 2464 2528 2259 -53 193 -82 C ATOM 376 C GLU A 61 32.896 -18.318 38.688 1.00 19.39 C ANISOU 376 C GLU C 61 2418 2579 2369 -65 172 -36 C ATOM 377 O GLU A 61 33.670 -18.572 37.779 1.00 19.34 O ANISOU 377 O GLU C 61 2423 2554 2371 -101 92 -76 O ATOM 378 CB AGLU A 61 33.008 -16.101 39.931 0.50 20.55 C ANISOU 378 CB AGLU C 61 2578 2697 2530 -35 246 12 C ATOM 379 CG AGLU A 61 32.514 -14.666 40.005 0.50 20.71 C ANISOU 379 CG AGLU C 61 2733 2518 2615 -70 146 -51 C ATOM 380 CD AGLU A 61 33.179 -13.835 41.109 0.50 23.18 C ANISOU 380 CD AGLU C 61 3106 2904 2795 -94 134 46 C ATOM 381 OE1AGLU A 61 33.373 -14.340 42.239 0.50 27.78 O ANISOU 381 OE1AGLU C 61 3870 3481 3201 -234 104 -165 O ATOM 382 OE2AGLU A 61 33.509 -12.666 40.849 0.50 28.73 O ANISOU 382 OE2AGLU C 61 4065 3389 3462 -301 29 11 O ATOM 383 N GLU A 62 32.611 -19.258 39.588 1.00 16.63 N ANISOU 383 N GLU C 62 2038 2448 1831 -18 193 -143 N ATOM 384 CA GLU A 62 33.232 -20.594 39.527 1.00 17.53 C ANISOU 384 CA GLU C 62 2036 2451 2170 -39 90 -140 C ATOM 385 C GLU A 62 32.796 -21.343 38.286 1.00 13.79 C ANISOU 385 C GLU C 62 1595 2032 1610 -26 -30 -451 C ATOM 386 O GLU A 62 33.589 -21.988 37.626 1.00 14.62 O ANISOU 386 O GLU C 62 1557 2308 1687 37 9 -507 O ATOM 387 CB GLU A 62 32.910 -21.501 40.748 1.00 19.98 C ANISOU 387 CB GLU C 62 2300 2907 2383 42 -13 -105 C ATOM 388 CG GLU A 62 33.902 -21.415 41.859 1.00 24.20 C ANISOU 388 CG GLU C 62 3006 3155 3033 -110 141 -119 C ATOM 389 CD GLU A 62 33.687 -22.380 42.999 1.00 20.33 C ANISOU 389 CD GLU C 62 2759 2597 2368 213 321 4 C ATOM 390 OE1 GLU A 62 33.035 -23.469 42.856 1.00 20.22 O ANISOU 390 OE1 GLU C 62 2838 2575 2268 106 304 -89 O ATOM 391 OE2 GLU A 62 34.149 -22.011 44.096 1.00 26.38 O ANISOU 391 OE2 GLU C 62 3877 3194 2952 137 554 44 O ATOM 392 N GLU A 63 31.496 -21.292 37.989 1.00 13.27 N ANISOU 392 N GLU C 63 1479 1941 1619 46 -68 -433 N ATOM 393 CA AGLU A 63 30.913 -22.069 36.934 0.50 13.32 C ANISOU 393 CA AGLU C 63 1523 1848 1689 51 -19 -425 C ATOM 394 C GLU A 63 31.228 -21.503 35.544 1.00 11.31 C ANISOU 394 C GLU C 63 1250 1577 1469 -10 -35 -424 C ATOM 395 O GLU A 63 31.252 -22.239 34.580 1.00 12.42 O ANISOU 395 O GLU C 63 1458 1642 1618 36 -112 -489 O ATOM 396 CB AGLU A 63 29.396 -22.058 37.153 0.50 13.31 C ANISOU 396 CB AGLU C 63 1570 1787 1698 -85 -214 -394 C ATOM 397 CG AGLU A 63 28.607 -22.923 36.207 0.50 14.93 C ANISOU 397 CG AGLU C 63 1612 2149 1910 -1 -33 -372 C ATOM 398 CD AGLU A 63 27.094 -22.877 36.448 0.50 14.78 C ANISOU 398 CD AGLU C 63 1646 2092 1878 2 -119 -268 C ATOM 399 OE1AGLU A 63 26.422 -21.908 36.076 0.50 13.24 O ANISOU 399 OE1AGLU C 63 1461 1657 1913 149 -93 -394 O ATOM 400 OE2AGLU A 63 26.603 -23.870 37.003 0.50 22.58 O ANISOU 400 OE2AGLU C 63 3145 2367 3065 -186 -121 -376 O ATOM 401 N PHE A 64 31.393 -20.178 35.487 1.00 11.86 N ANISOU 401 N PHE C 64 1353 1642 1511 132 15 -395 N ATOM 402 CA PHE A 64 31.558 -19.442 34.214 1.00 11.61 C ANISOU 402 CA PHE C 64 1317 1617 1475 187 -35 -467 C ATOM 403 C PHE A 64 33.013 -19.460 33.809 1.00 12.38 C ANISOU 403 C PHE C 64 1410 1639 1654 88 -127 -488 C ATOM 404 O PHE A 64 33.725 -18.458 33.878 1.00 13.91 O ANISOU 404 O PHE C 64 1401 1799 2085 157 0 -679 O ATOM 405 CB PHE A 64 31.006 -18.022 34.368 1.00 12.66 C ANISOU 405 CB PHE C 64 1464 1708 1635 59 -52 -296 C ATOM 406 CG PHE A 64 30.849 -17.255 33.085 1.00 13.47 C ANISOU 406 CG PHE C 64 1527 1839 1750 260 -207 -249 C ATOM 407 CD1 PHE A 64 30.358 -17.806 31.936 1.00 14.10 C ANISOU 407 CD1 PHE C 64 1766 1751 1837 232 39 -603 C ATOM 408 CD2 PHE A 64 31.057 -15.912 33.119 1.00 15.86 C ANISOU 408 CD2 PHE C 64 2336 2089 1601 -306 -145 -454 C ATOM 409 CE1 PHE A 64 30.187 -17.019 30.805 1.00 13.62 C ANISOU 409 CE1 PHE C 64 1828 1874 1473 209 13 -299 C ATOM 410 CE2 PHE A 64 30.859 -15.139 32.000 1.00 18.97 C ANISOU 410 CE2 PHE C 64 3016 1893 2296 -14 139 -636 C ATOM 411 CZ PHE A 64 30.437 -15.701 30.876 1.00 15.16 C ANISOU 411 CZ PHE C 64 1967 1861 1930 329 -9 -543 C ATOM 412 N VAL A 65 33.429 -20.653 33.413 1.00 11.78 N ANISOU 412 N VAL C 65 1230 1713 1533 111 -135 -525 N ATOM 413 CA VAL A 65 34.823 -20.892 33.003 1.00 12.44 C ANISOU 413 CA VAL C 65 1384 1618 1722 151 -120 -331 C ATOM 414 C VAL A 65 35.082 -20.363 31.597 1.00 12.59 C ANISOU 414 C VAL C 65 1345 1740 1697 113 -93 -441 C ATOM 415 O VAL A 65 34.177 -19.905 30.877 1.00 11.80 O ANISOU 415 O VAL C 65 1194 1754 1535 178 -81 -856 O ATOM 416 CB VAL A 65 35.139 -22.385 33.092 1.00 11.01 C ANISOU 416 CB VAL C 65 1190 1375 1616 210 -179 -486 C ATOM 417 CG1 VAL A 65 35.117 -22.855 34.573 1.00 13.44 C ANISOU 417 CG1 VAL C 65 1780 1885 1438 205 -146 -741 C ATOM 418 CG2 VAL A 65 34.244 -23.218 32.233 1.00 14.07 C ANISOU 418 CG2 VAL C 65 1482 1639 2224 30 85 -453 C ATOM 419 N GLU A 66 36.323 -20.378 31.144 1.00 11.43 N ANISOU 419 N GLU C 66 1198 1799 1346 136 29 -555 N ATOM 420 CA AGLU A 66 36.594 -20.012 29.788 0.50 12.67 C ANISOU 420 CA AGLU C 66 1461 1743 1611 43 -90 -399 C ATOM 421 C GLU A 66 35.797 -20.936 28.830 1.00 12.24 C ANISOU 421 C GLU C 66 1464 1703 1483 28 -133 -497 C ATOM 422 O GLU A 66 35.551 -22.086 29.095 1.00 14.50 O ANISOU 422 O GLU C 66 2180 1570 1756 -21 103 -623 O ATOM 423 CB AGLU A 66 38.118 -20.042 29.665 0.50 13.57 C ANISOU 423 CB AGLU C 66 1552 1860 1741 -72 -22 -386 C ATOM 424 CG AGLU A 66 38.735 -19.773 28.342 0.50 14.33 C ANISOU 424 CG AGLU C 66 1682 1712 2049 -183 -277 -233 C ATOM 425 CD AGLU A 66 40.238 -20.218 28.353 0.50 17.26 C ANISOU 425 CD AGLU C 66 1768 2336 2452 -200 -149 -172 C ATOM 426 OE1AGLU A 66 40.764 -20.689 29.387 0.50 20.41 O ANISOU 426 OE1AGLU C 66 2158 3127 2469 7 127 -62 O ATOM 427 OE2AGLU A 66 40.855 -20.172 27.304 0.50 22.05 O ANISOU 427 OE2AGLU C 66 2888 3227 2260 93 -295 -30 O ATOM 428 N GLY A 67 35.433 -20.398 27.677 1.00 12.01 N ANISOU 428 N GLY C 67 1515 1615 1432 99 -117 -522 N ATOM 429 CA GLY A 67 34.746 -21.157 26.681 1.00 13.38 C ANISOU 429 CA GLY C 67 1658 1693 1730 108 -31 -362 C ATOM 430 C GLY A 67 34.119 -20.244 25.651 1.00 11.12 C ANISOU 430 C GLY C 67 1368 1448 1406 121 -44 -317 C ATOM 431 O GLY A 67 34.235 -19.029 25.753 1.00 11.63 O ANISOU 431 O GLY C 67 1465 1371 1581 1 6 -354 O ATOM 432 N ILE A 68 33.470 -20.860 24.699 1.00 11.71 N ANISOU 432 N ILE C 68 1393 1435 1618 42 27 -351 N ATOM 433 CA ILE A 68 32.654 -20.156 23.711 1.00 11.90 C ANISOU 433 CA ILE C 68 1474 1493 1551 75 -64 -322 C ATOM 434 C ILE A 68 31.208 -20.346 24.105 1.00 11.24 C ANISOU 434 C ILE C 68 1411 1336 1524 57 -53 -434 C ATOM 435 O ILE A 68 30.719 -21.457 24.288 1.00 12.61 O ANISOU 435 O ILE C 68 1461 1248 2083 77 -174 -367 O ATOM 436 CB ILE A 68 32.883 -20.689 22.303 1.00 13.19 C ANISOU 436 CB ILE C 68 1530 1720 1760 82 -116 -191 C ATOM 437 CG1 ILE A 68 34.375 -20.548 21.896 1.00 15.15 C ANISOU 437 CG1 ILE C 68 1756 2099 1901 -22 -345 -113 C ATOM 438 CG2 ILE A 68 31.995 -19.963 21.317 1.00 14.51 C ANISOU 438 CG2 ILE C 68 1871 2040 1600 157 11 -283 C ATOM 439 CD1 ILE A 68 34.688 -21.145 20.516 1.00 17.11 C ANISOU 439 CD1 ILE C 68 1966 2437 2095 148 -375 154 C ATOM 440 N TYR A 69 30.567 -19.223 24.335 1.00 10.46 N ANISOU 440 N TYR C 69 1154 1324 1495 54 -201 -374 N ATOM 441 CA TYR A 69 29.194 -19.144 24.820 1.00 10.22 C ANISOU 441 CA TYR C 69 1211 1276 1395 38 -107 -320 C ATOM 442 C TYR A 69 28.274 -18.563 23.757 1.00 9.87 C ANISOU 442 C TYR C 69 1184 1265 1298 86 -23 -301 C ATOM 443 O TYR A 69 28.668 -17.726 22.955 1.00 11.08 O ANISOU 443 O TYR C 69 1256 1495 1459 -41 57 -457 O ATOM 444 CB TYR A 69 29.137 -18.291 26.088 1.00 11.08 C ANISOU 444 CB TYR C 69 1367 1400 1442 127 -77 -305 C ATOM 445 CG TYR A 69 29.822 -18.956 27.260 1.00 11.01 C ANISOU 445 CG TYR C 69 1256 1427 1498 3 -138 -500 C ATOM 446 CD1 TYR A 69 31.175 -18.832 27.459 1.00 10.74 C ANISOU 446 CD1 TYR C 69 1206 1484 1390 1 -130 -540 C ATOM 447 CD2 TYR A 69 29.097 -19.726 28.185 1.00 10.76 C ANISOU 447 CD2 TYR C 69 1021 1476 1591 -91 -18 -540 C ATOM 448 CE1 TYR A 69 31.843 -19.433 28.534 1.00 10.72 C ANISOU 448 CE1 TYR C 69 895 1652 1523 11 103 -416 C ATOM 449 CE2 TYR A 69 29.735 -20.324 29.242 1.00 11.83 C ANISOU 449 CE2 TYR C 69 1348 1694 1451 -18 -241 -675 C ATOM 450 CZ TYR A 69 31.108 -20.194 29.423 1.00 11.61 C ANISOU 450 CZ TYR C 69 1263 1603 1543 116 -30 -571 C ATOM 451 OH TYR A 69 31.680 -20.846 30.504 1.00 12.46 O ANISOU 451 OH TYR C 69 1312 1813 1609 68 88 -681 O ATOM 452 N LYS A 70 27.043 -19.041 23.792 1.00 10.26 N ANISOU 452 N LYS C 70 1260 1257 1379 -40 2 -432 N ATOM 453 CA LYS A 70 25.973 -18.556 22.946 1.00 10.66 C ANISOU 453 CA LYS C 70 1322 1427 1302 11 -51 -351 C ATOM 454 C LYS A 70 24.801 -18.154 23.823 1.00 9.83 C ANISOU 454 C LYS C 70 1143 1331 1259 60 -21 -362 C ATOM 455 O LYS A 70 24.293 -18.982 24.568 1.00 11.84 O ANISOU 455 O LYS C 70 1435 1485 1575 37 -152 -522 O ATOM 456 CB LYS A 70 25.519 -19.638 21.991 1.00 12.21 C ANISOU 456 CB LYS C 70 1677 1618 1344 -65 32 -478 C ATOM 457 CG LYS A 70 24.301 -19.221 21.187 1.00 15.74 C ANISOU 457 CG LYS C 70 1886 2133 1961 -70 107 -134 C ATOM 458 CD LYS A 70 23.933 -20.150 20.016 1.00 19.03 C ANISOU 458 CD LYS C 70 2204 2695 2330 -148 376 -39 C ATOM 459 CE LYS A 70 23.708 -21.532 20.430 1.00 21.37 C ANISOU 459 CE LYS C 70 2653 2826 2640 -137 268 222 C ATOM 460 NZ LYS A 70 22.917 -22.279 19.397 1.00 27.31 N ANISOU 460 NZ LYS C 70 3645 3230 3501 -166 493 573 N ATOM 461 N VAL A 71 24.429 -16.903 23.756 1.00 10.24 N ANISOU 461 N VAL C 71 1377 1378 1134 55 -108 -416 N ATOM 462 CA VAL A 71 23.271 -16.351 24.428 1.00 10.73 C ANISOU 462 CA VAL C 71 1358 1398 1317 -61 -65 -293 C ATOM 463 C VAL A 71 22.174 -16.191 23.414 1.00 10.53 C ANISOU 463 C VAL C 71 1470 1358 1171 -50 -163 -330 C ATOM 464 O VAL A 71 22.307 -15.403 22.487 1.00 10.96 O ANISOU 464 O VAL C 71 1367 1490 1305 -52 -128 -533 O ATOM 465 CB VAL A 71 23.621 -15.019 25.101 1.00 11.55 C ANISOU 465 CB VAL C 71 1439 1572 1374 -80 -94 -229 C ATOM 466 CG1 VAL A 71 22.356 -14.370 25.709 1.00 13.53 C ANISOU 466 CG1 VAL C 71 1801 1779 1558 233 -204 -69 C ATOM 467 CG2 VAL A 71 24.710 -15.223 26.163 1.00 14.36 C ANISOU 467 CG2 VAL C 71 1839 2017 1598 -276 172 -67 C ATOM 468 N GLU A 72 21.142 -17.036 23.560 1.00 11.55 N ANISOU 468 N GLU C 72 1490 1536 1363 8 -32 -153 N ATOM 469 CA AGLU A 72 19.992 -17.049 22.672 0.50 11.51 C ANISOU 469 CA AGLU C 72 1584 1497 1290 31 -77 -205 C ATOM 470 C GLU A 72 18.868 -16.271 23.372 1.00 9.73 C ANISOU 470 C GLU C 72 1425 1254 1017 6 -167 -384 C ATOM 471 O GLU A 72 18.381 -16.672 24.399 1.00 11.60 O ANISOU 471 O GLU C 72 1465 1575 1367 191 -261 -359 O ATOM 472 CB AGLU A 72 19.540 -18.482 22.423 0.50 13.04 C ANISOU 472 CB AGLU C 72 1691 1758 1506 59 -112 -176 C ATOM 473 CG AGLU A 72 18.820 -18.743 21.132 0.50 14.62 C ANISOU 473 CG AGLU C 72 1856 1930 1766 -27 -101 -130 C ATOM 474 CD AGLU A 72 19.092 -20.184 20.685 0.50 16.99 C ANISOU 474 CD AGLU C 72 2373 2079 2002 -86 82 111 C ATOM 475 OE1AGLU A 72 18.516 -21.057 21.357 0.50 21.04 O ANISOU 475 OE1AGLU C 72 2773 2373 2848 80 211 -198 O ATOM 476 OE2AGLU A 72 19.931 -20.439 19.761 0.50 25.88 O ANISOU 476 OE2AGLU C 72 3402 3381 3047 -291 -14 256 O ATOM 477 N ILE A 73 18.439 -15.182 22.705 1.00 10.83 N ANISOU 477 N ILE C 73 1782 1295 1038 177 -27 -201 N ATOM 478 CA ILE A 73 17.361 -14.338 23.215 1.00 10.68 C ANISOU 478 CA ILE C 73 1684 1372 1002 53 -85 -236 C ATOM 479 C ILE A 73 16.143 -14.628 22.408 1.00 11.66 C ANISOU 479 C ILE C 73 1644 1492 1295 18 -83 -75 C ATOM 480 O ILE A 73 16.181 -14.475 21.169 1.00 11.28 O ANISOU 480 O ILE C 73 1690 1666 928 1 174 -100 O ATOM 481 CB ILE A 73 17.749 -12.855 23.148 1.00 10.82 C ANISOU 481 CB ILE C 73 1950 1209 949 13 123 -224 C ATOM 482 CG1 ILE A 73 19.101 -12.613 23.884 1.00 12.68 C ANISOU 482 CG1 ILE C 73 2008 1647 1161 133 195 -113 C ATOM 483 CG2 ILE A 73 16.627 -11.947 23.681 1.00 12.09 C ANISOU 483 CG2 ILE C 73 1771 1751 1070 242 140 14 C ATOM 484 CD1 ILE A 73 19.617 -11.177 23.745 1.00 14.84 C ANISOU 484 CD1 ILE C 73 2242 1832 1565 -8 186 -375 C ATOM 485 N ASP A 74 15.096 -15.092 23.036 1.00 10.77 N ANISOU 485 N ASP C 74 1718 1534 839 43 -16 -28 N ATOM 486 CA ASP A 74 13.950 -15.641 22.313 1.00 12.25 C ANISOU 486 CA ASP C 74 1803 1663 1186 -153 -55 8 C ATOM 487 C ASP A 74 12.976 -14.534 21.892 1.00 11.88 C ANISOU 487 C ASP C 74 1572 1919 1021 -263 131 37 C ATOM 488 O ASP A 74 11.878 -14.352 22.426 1.00 11.48 O ANISOU 488 O ASP C 74 1488 1868 1005 -215 82 -126 O ATOM 489 CB ASP A 74 13.330 -16.746 23.167 1.00 12.63 C ANISOU 489 CB ASP C 74 1853 1615 1331 -167 -95 -52 C ATOM 490 CG ASP A 74 14.254 -17.979 23.266 1.00 17.22 C ANISOU 490 CG ASP C 74 2272 2184 2086 56 -77 -160 C ATOM 491 OD1 ASP A 74 15.106 -18.225 22.371 1.00 18.51 O ANISOU 491 OD1 ASP C 74 2259 2045 2727 286 -296 -226 O ATOM 492 OD2 ASP A 74 14.104 -18.730 24.234 1.00 21.62 O ANISOU 492 OD2 ASP C 74 3198 2713 2301 356 -1 -761 O ATOM 493 N THR A 75 13.402 -13.764 20.915 1.00 10.82 N ANISOU 493 N THR C 75 1489 1697 923 -105 67 -75 N ATOM 494 CA THR A 75 12.701 -12.591 20.486 1.00 11.38 C ANISOU 494 CA THR C 75 1451 1721 1150 -163 61 82 C ATOM 495 C THR A 75 11.361 -12.947 19.807 1.00 11.53 C ANISOU 495 C THR C 75 1335 1728 1317 -183 49 -28 C ATOM 496 O THR A 75 10.374 -12.239 19.992 1.00 12.46 O ANISOU 496 O THR C 75 1238 2230 1266 -170 25 101 O ATOM 497 CB THR A 75 13.579 -11.782 19.510 1.00 11.46 C ANISOU 497 CB THR C 75 1367 1605 1382 -48 49 10 C ATOM 498 OG1 THR A 75 13.895 -12.571 18.369 1.00 10.43 O ANISOU 498 OG1 THR C 75 1158 1663 1140 -7 60 -106 O ATOM 499 CG2 THR A 75 14.867 -11.311 20.174 1.00 11.37 C ANISOU 499 CG2 THR C 75 1253 1637 1429 -262 288 -22 C ATOM 500 N LYS A 76 11.327 -14.057 19.049 1.00 12.18 N ANISOU 500 N LYS C 76 1315 1927 1383 -163 81 50 N ATOM 501 CA LYS A 76 10.052 -14.387 18.400 1.00 13.91 C ANISOU 501 CA LYS C 76 1479 2123 1682 -236 11 119 C ATOM 502 C LYS A 76 8.970 -14.705 19.462 1.00 14.82 C ANISOU 502 C LYS C 76 1541 2182 1909 -371 50 185 C ATOM 503 O LYS A 76 7.844 -14.229 19.328 1.00 16.72 O ANISOU 503 O LYS C 76 1742 2778 1831 -350 -178 620 O ATOM 504 CB LYS A 76 10.196 -15.567 17.458 1.00 13.76 C ANISOU 504 CB LYS C 76 1360 2085 1782 -101 -25 28 C ATOM 505 CG LYS A 76 8.916 -15.904 16.750 1.00 16.59 C ANISOU 505 CG LYS C 76 1777 2458 2065 -217 34 284 C ATOM 506 CD LYS A 76 9.143 -16.966 15.707 1.00 18.26 C ANISOU 506 CD LYS C 76 2022 2598 2315 -228 -12 377 C ATOM 507 CE LYS A 76 7.962 -17.308 14.900 1.00 23.36 C ANISOU 507 CE LYS C 76 2902 3244 2729 35 217 416 C ATOM 508 NZ LYS A 76 8.389 -18.257 13.848 1.00 26.89 N ANISOU 508 NZ LYS C 76 3273 3774 3168 70 105 824 N ATOM 509 N SER A 77 9.348 -15.529 20.467 1.00 15.13 N ANISOU 509 N SER C 77 1761 2256 1732 -370 -195 298 N ATOM 510 CA SER A 77 8.437 -15.915 21.588 1.00 16.95 C ANISOU 510 CA SER C 77 2036 2466 1937 -332 -154 232 C ATOM 511 C SER A 77 7.988 -14.660 22.290 1.00 17.34 C ANISOU 511 C SER C 77 2186 2448 1953 -422 -290 173 C ATOM 512 O SER A 77 6.825 -14.566 22.681 1.00 17.72 O ANISOU 512 O SER C 77 2148 2643 1940 -486 -65 281 O ATOM 513 CB SER A 77 9.094 -16.927 22.550 1.00 18.43 C ANISOU 513 CB SER C 77 2529 2465 2008 -172 -429 229 C ATOM 514 OG SER A 77 9.208 -18.237 21.962 1.00 20.68 O ANISOU 514 OG SER C 77 2851 2565 2442 -454 -335 252 O ATOM 515 N TYR A 78 8.903 -13.671 22.463 1.00 15.84 N ANISOU 515 N TYR C 78 1947 2422 1649 -504 -203 375 N ATOM 516 CA TYR A 78 8.540 -12.396 23.104 1.00 15.93 C ANISOU 516 CA TYR C 78 1858 2369 1825 -296 -181 178 C ATOM 517 C TYR A 78 7.490 -11.648 22.304 1.00 14.89 C ANISOU 517 C TYR C 78 1813 2303 1540 -331 -145 212 C ATOM 518 O TYR A 78 6.419 -11.301 22.843 1.00 17.10 O ANISOU 518 O TYR C 78 1881 2623 1993 -391 -168 388 O ATOM 519 CB TYR A 78 9.770 -11.481 23.214 1.00 14.67 C ANISOU 519 CB TYR C 78 1745 2324 1501 -409 -102 183 C ATOM 520 CG TYR A 78 9.480 -10.026 23.629 1.00 14.31 C ANISOU 520 CG TYR C 78 1589 2364 1481 -365 -85 66 C ATOM 521 CD1 TYR A 78 9.229 -9.725 24.931 1.00 14.15 C ANISOU 521 CD1 TYR C 78 1934 2054 1387 -247 -203 142 C ATOM 522 CD2 TYR A 78 9.495 -8.978 22.742 1.00 12.84 C ANISOU 522 CD2 TYR C 78 1433 2086 1359 -312 196 194 C ATOM 523 CE1 TYR A 78 8.990 -8.435 25.344 1.00 14.24 C ANISOU 523 CE1 TYR C 78 1737 2124 1548 -149 -106 58 C ATOM 524 CE2 TYR A 78 9.251 -7.697 23.107 1.00 11.88 C ANISOU 524 CE2 TYR C 78 995 2270 1248 -92 0 -46 C ATOM 525 CZ TYR A 78 8.985 -7.411 24.445 1.00 13.54 C ANISOU 525 CZ TYR C 78 1673 2181 1288 14 -154 -46 C ATOM 526 OH TYR A 78 8.773 -6.119 24.876 1.00 13.56 O ANISOU 526 OH TYR C 78 1574 2201 1377 -245 -4 -51 O ATOM 527 N TRP A 79 7.740 -11.435 20.991 1.00 15.71 N ANISOU 527 N TRP C 79 1665 2721 1581 -380 -150 305 N ATOM 528 CA TRP A 79 6.837 -10.680 20.138 1.00 15.28 C ANISOU 528 CA TRP C 79 1733 2404 1667 -92 -172 417 C ATOM 529 C TRP A 79 5.495 -11.473 19.956 1.00 17.05 C ANISOU 529 C TRP C 79 1685 2521 2269 -197 -93 210 C ATOM 530 O TRP A 79 4.435 -10.891 20.075 1.00 17.33 O ANISOU 530 O TRP C 79 1729 2923 1933 -303 -204 338 O ATOM 531 CB TRP A 79 7.427 -10.377 18.742 1.00 15.01 C ANISOU 531 CB TRP C 79 1559 2542 1599 -22 39 410 C ATOM 532 CG TRP A 79 8.588 -9.395 18.760 1.00 13.80 C ANISOU 532 CG TRP C 79 1610 2283 1349 -48 -305 361 C ATOM 533 CD1 TRP A 79 9.890 -9.627 18.421 1.00 13.67 C ANISOU 533 CD1 TRP C 79 1555 2289 1350 242 163 193 C ATOM 534 CD2 TRP A 79 8.512 -8.009 19.078 1.00 13.11 C ANISOU 534 CD2 TRP C 79 1444 2166 1369 292 311 499 C ATOM 535 NE1 TRP A 79 10.651 -8.474 18.591 1.00 12.06 N ANISOU 535 NE1 TRP C 79 1299 2112 1171 382 169 431 N ATOM 536 CE2 TRP A 79 9.817 -7.463 18.978 1.00 13.57 C ANISOU 536 CE2 TRP C 79 1609 2176 1370 75 285 422 C ATOM 537 CE3 TRP A 79 7.478 -7.173 19.499 1.00 15.54 C ANISOU 537 CE3 TRP C 79 1604 2504 1793 437 89 378 C ATOM 538 CZ2 TRP A 79 10.121 -6.159 19.323 1.00 13.09 C ANISOU 538 CZ2 TRP C 79 1453 2064 1454 551 344 180 C ATOM 539 CZ3 TRP A 79 7.769 -5.834 19.763 1.00 16.20 C ANISOU 539 CZ3 TRP C 79 1830 2397 1926 485 53 72 C ATOM 540 CH2 TRP A 79 9.062 -5.331 19.693 1.00 14.59 C ANISOU 540 CH2 TRP C 79 1933 2007 1601 223 -62 306 C ATOM 541 N LYS A 80 5.569 -12.803 19.831 1.00 17.20 N ANISOU 541 N LYS C 80 1663 2745 2126 -305 109 453 N ATOM 542 CA LYS A 80 4.321 -13.632 19.667 1.00 18.80 C ANISOU 542 CA LYS C 80 1894 2755 2493 -246 -79 146 C ATOM 543 C LYS A 80 3.469 -13.615 20.950 1.00 19.60 C ANISOU 543 C LYS C 80 2017 2946 2484 -236 -103 156 C ATOM 544 O LYS A 80 2.248 -13.577 20.861 1.00 20.41 O ANISOU 544 O LYS C 80 2087 2889 2778 -572 11 37 O ATOM 545 CB LYS A 80 4.682 -15.034 19.252 1.00 19.01 C ANISOU 545 CB LYS C 80 1902 2794 2527 -488 -27 209 C ATOM 546 CG LYS A 80 5.071 -15.097 17.780 1.00 22.30 C ANISOU 546 CG LYS C 80 2347 3319 2805 -156 -71 322 C ATOM 547 CD LYS A 80 5.398 -16.501 17.381 1.00 24.60 C ANISOU 547 CD LYS C 80 2802 3318 3224 -216 -113 198 C ATOM 548 CE LYS A 80 4.119 -17.380 17.326 1.00 28.51 C ANISOU 548 CE LYS C 80 3358 3606 3865 -356 -9 230 C ATOM 549 NZ LYS A 80 4.441 -18.702 16.693 1.00 30.99 N ANISOU 549 NZ LYS C 80 4042 3647 4086 -212 -128 206 N ATOM 550 N ALA A 81 4.097 -13.557 22.135 1.00 17.53 N ANISOU 550 N ALA C 81 1765 2637 2256 -188 -249 -51 N ATOM 551 CA ALA A 81 3.369 -13.426 23.402 1.00 18.99 C ANISOU 551 CA ALA C 81 1937 2889 2388 -229 -264 -46 C ATOM 552 C ALA A 81 2.668 -12.084 23.466 1.00 18.99 C ANISOU 552 C ALA C 81 1958 2844 2411 -150 -369 39 C ATOM 553 O ALA A 81 1.656 -11.938 24.196 1.00 23.42 O ANISOU 553 O ALA C 81 2539 3465 2893 -31 -762 67 O ATOM 554 CB ALA A 81 4.322 -13.621 24.599 1.00 17.46 C ANISOU 554 CB ALA C 81 1986 2731 1914 -82 -275 3 C ATOM 555 N LEU A 82 3.134 -11.093 22.729 1.00 18.93 N ANISOU 555 N LEU C 82 2176 2871 2142 -95 -298 -40 N ATOM 556 CA LEU A 82 2.502 -9.799 22.600 1.00 18.75 C ANISOU 556 CA LEU C 82 2047 2850 2224 -66 -109 37 C ATOM 557 C LEU A 82 1.547 -9.720 21.430 1.00 20.46 C ANISOU 557 C LEU C 82 2439 2950 2384 -34 -108 -93 C ATOM 558 O LEU A 82 0.991 -8.666 21.154 1.00 22.28 O ANISOU 558 O LEU C 82 2304 3246 2913 358 204 199 O ATOM 559 CB LEU A 82 3.561 -8.670 22.501 1.00 19.09 C ANISOU 559 CB LEU C 82 2331 2754 2166 -88 25 -210 C ATOM 560 CG LEU A 82 4.437 -8.464 23.769 1.00 19.37 C ANISOU 560 CG LEU C 82 1992 2996 2372 53 -77 205 C ATOM 561 CD1 LEU A 82 5.565 -7.469 23.511 1.00 21.38 C ANISOU 561 CD1 LEU C 82 2064 3303 2754 -23 -37 384 C ATOM 562 CD2 LEU A 82 3.552 -7.998 24.968 1.00 21.38 C ANISOU 562 CD2 LEU C 82 2421 3372 2330 -307 -154 269 C ATOM 563 N GLY A 83 1.374 -10.841 20.728 1.00 19.63 N ANISOU 563 N GLY C 83 2110 2981 2366 -152 -251 -55 N ATOM 564 CA GLY A 83 0.436 -10.933 19.590 1.00 19.90 C ANISOU 564 CA GLY C 83 2193 3054 2313 -81 -142 -106 C ATOM 565 C GLY A 83 0.905 -10.305 18.296 1.00 19.90 C ANISOU 565 C GLY C 83 2181 3158 2221 -78 -142 -119 C ATOM 566 O GLY A 83 0.087 -10.040 17.428 1.00 23.56 O ANISOU 566 O GLY C 83 2621 3728 2601 -29 -23 -179 O ATOM 567 N ILE A 84 2.234 -10.132 18.161 1.00 19.72 N ANISOU 567 N ILE C 84 2247 3078 2167 36 -71 3 N ATOM 568 CA ILE A 84 2.941 -9.523 16.998 1.00 20.70 C ANISOU 568 CA ILE C 84 2501 3118 2244 61 -116 48 C ATOM 569 C ILE A 84 3.713 -10.624 16.245 1.00 20.66 C ANISOU 569 C ILE C 84 2674 2954 2219 351 -18 -21 C ATOM 570 O ILE A 84 4.268 -11.517 16.928 1.00 22.67 O ANISOU 570 O ILE C 84 2762 3469 2381 584 -329 77 O ATOM 571 CB ILE A 84 4.003 -8.476 17.550 1.00 19.75 C ANISOU 571 CB ILE C 84 2281 2968 2253 101 -172 -7 C ATOM 572 CG1 ILE A 84 3.254 -7.480 18.466 1.00 24.17 C ANISOU 572 CG1 ILE C 84 3062 3170 2951 -10 -41 292 C ATOM 573 CG2 ILE A 84 4.732 -7.793 16.454 1.00 20.10 C ANISOU 573 CG2 ILE C 84 2414 3115 2106 -60 -225 -95 C ATOM 574 CD1 ILE A 84 3.965 -6.253 18.936 1.00 25.58 C ANISOU 574 CD1 ILE C 84 3278 3277 3163 -110 -79 113 C ATOM 575 N SER A 85 3.653 -10.596 14.907 1.00 19.70 N ANISOU 575 N SER C 85 2308 2943 2230 169 238 283 N ATOM 576 CA SER A 85 4.393 -11.515 14.004 1.00 18.92 C ANISOU 576 CA SER C 85 2225 2811 2150 165 189 253 C ATOM 577 C SER A 85 5.763 -10.952 13.619 1.00 18.47 C ANISOU 577 C SER C 85 2265 2567 2184 256 280 436 C ATOM 578 O SER A 85 5.866 -10.117 12.739 1.00 19.09 O ANISOU 578 O SER C 85 2203 2753 2294 255 496 156 O ATOM 579 CB ASER A 85 3.579 -11.742 12.689 0.65 19.53 C ANISOU 579 CB ASER C 85 2276 2900 2244 10 183 272 C ATOM 580 OG ASER A 85 2.265 -12.231 12.963 0.65 21.16 O ANISOU 580 OG ASER C 85 2392 3094 2554 -46 26 105 O ATOM 581 N PRO A 86 6.854 -11.376 14.307 1.00 16.48 N ANISOU 581 N PRO C 86 1940 2423 1899 319 311 442 N ATOM 582 CA PRO A 86 8.109 -10.710 13.971 1.00 16.29 C ANISOU 582 CA PRO C 86 2039 2400 1746 305 325 364 C ATOM 583 C PRO A 86 8.946 -11.431 12.895 1.00 15.22 C ANISOU 583 C PRO C 86 1791 2226 1764 389 343 233 C ATOM 584 O PRO A 86 8.588 -12.541 12.472 1.00 15.51 O ANISOU 584 O PRO C 86 2101 2368 1421 271 538 620 O ATOM 585 CB PRO A 86 8.866 -10.841 15.285 1.00 15.62 C ANISOU 585 CB PRO C 86 1687 2638 1606 291 362 440 C ATOM 586 CG PRO A 86 8.471 -12.202 15.754 1.00 16.81 C ANISOU 586 CG PRO C 86 1861 2587 1936 539 243 274 C ATOM 587 CD PRO A 86 7.002 -12.366 15.351 1.00 18.54 C ANISOU 587 CD PRO C 86 2278 2615 2151 256 287 444 C ATOM 588 N PHE A 87 10.091 -10.866 12.508 1.00 12.85 N ANISOU 588 N PHE C 87 1740 1750 1392 378 242 375 N ATOM 589 CA PHE A 87 10.916 -11.525 11.454 1.00 13.61 C ANISOU 589 CA PHE C 87 1938 1926 1306 346 318 330 C ATOM 590 C PHE A 87 11.833 -12.639 11.939 1.00 12.52 C ANISOU 590 C PHE C 87 1933 1608 1215 354 309 307 C ATOM 591 O PHE A 87 11.924 -13.698 11.315 1.00 13.64 O ANISOU 591 O PHE C 87 2168 1441 1573 344 270 255 O ATOM 592 CB PHE A 87 11.736 -10.490 10.755 1.00 13.19 C ANISOU 592 CB PHE C 87 2073 1723 1213 365 390 327 C ATOM 593 CG PHE A 87 12.502 -11.014 9.579 1.00 14.56 C ANISOU 593 CG PHE C 87 2286 1631 1614 263 206 179 C ATOM 594 CD1 PHE A 87 11.860 -11.309 8.390 1.00 17.38 C ANISOU 594 CD1 PHE C 87 2550 2058 1994 297 182 133 C ATOM 595 CD2 PHE A 87 13.871 -11.199 9.665 1.00 14.60 C ANISOU 595 CD2 PHE C 87 2598 1642 1307 302 -34 198 C ATOM 596 CE1 PHE A 87 12.560 -11.819 7.318 1.00 16.73 C ANISOU 596 CE1 PHE C 87 2671 2174 1509 127 120 1 C ATOM 597 CE2 PHE A 87 14.576 -11.735 8.575 1.00 16.89 C ANISOU 597 CE2 PHE C 87 2602 1991 1822 149 -213 -148 C ATOM 598 CZ PHE A 87 13.916 -11.983 7.414 1.00 16.90 C ANISOU 598 CZ PHE C 87 2577 2106 1736 270 -289 305 C ATOM 599 N HIS A 88 12.605 -12.364 12.982 1.00 10.73 N ANISOU 599 N HIS C 88 1573 1436 1064 238 75 221 N ATOM 600 CA HIS A 88 13.658 -13.299 13.395 1.00 10.51 C ANISOU 600 CA HIS C 88 1511 1420 1059 233 18 158 C ATOM 601 C HIS A 88 13.097 -14.360 14.310 1.00 10.87 C ANISOU 601 C HIS C 88 1494 1642 994 91 -25 71 C ATOM 602 O HIS A 88 12.140 -14.164 15.047 1.00 11.43 O ANISOU 602 O HIS C 88 1296 1769 1277 174 -231 15 O ATOM 603 CB HIS A 88 14.794 -12.552 14.140 1.00 10.81 C ANISOU 603 CB HIS C 88 1364 1417 1325 298 -79 -15 C ATOM 604 CG HIS A 88 15.393 -11.472 13.287 1.00 9.70 C ANISOU 604 CG HIS C 88 1302 1069 1311 170 -285 53 C ATOM 605 ND1 HIS A 88 14.968 -10.151 13.350 1.00 11.72 N ANISOU 605 ND1 HIS C 88 1585 1325 1544 221 -10 231 N ATOM 606 CD2 HIS A 88 16.359 -11.535 12.340 1.00 12.52 C ANISOU 606 CD2 HIS C 88 1880 1375 1502 195 -219 -46 C ATOM 607 CE1 HIS A 88 15.661 -9.455 12.469 1.00 12.24 C ANISOU 607 CE1 HIS C 88 1746 1046 1857 -19 -292 282 C ATOM 608 NE2 HIS A 88 16.512 -10.263 11.847 1.00 11.61 N ANISOU 608 NE2 HIS C 88 1899 1177 1334 55 44 86 N ATOM 609 N GLU A 89 13.760 -15.494 14.316 1.00 10.15 N ANISOU 609 N GLU C 89 1459 1557 840 109 -17 111 N ATOM 610 CA GLU A 89 13.439 -16.548 15.253 1.00 10.61 C ANISOU 610 CA GLU C 89 1258 1609 1161 -86 73 -16 C ATOM 611 C GLU A 89 13.922 -16.212 16.659 1.00 11.59 C ANISOU 611 C GLU C 89 1445 1831 1125 -29 -18 -101 C ATOM 612 O GLU A 89 13.226 -16.419 17.637 1.00 13.34 O ANISOU 612 O GLU C 89 1544 2353 1171 -106 -169 -199 O ATOM 613 CB GLU A 89 14.070 -17.859 14.806 1.00 12.12 C ANISOU 613 CB GLU C 89 1648 1679 1275 -45 -20 -95 C ATOM 614 CG GLU A 89 13.455 -18.458 13.560 1.00 14.41 C ANISOU 614 CG GLU C 89 2116 1861 1498 -67 -124 26 C ATOM 615 CD GLU A 89 11.997 -18.787 13.763 1.00 18.58 C ANISOU 615 CD GLU C 89 2717 2171 2169 -44 123 433 C ATOM 616 OE1 GLU A 89 11.695 -19.525 14.704 1.00 21.95 O ANISOU 616 OE1 GLU C 89 2557 3052 2729 -696 -24 363 O ATOM 617 OE2 GLU A 89 11.186 -18.274 13.033 1.00 20.36 O ANISOU 617 OE2 GLU C 89 2505 2938 2292 183 148 1242 O ATOM 618 N HIS A 90 15.127 -15.715 16.765 1.00 11.09 N ANISOU 618 N HIS C 90 1398 1854 960 -44 -18 -78 N ATOM 619 CA HIS A 90 15.797 -15.371 18.028 1.00 11.81 C ANISOU 619 CA HIS C 90 1670 1837 979 77 254 -175 C ATOM 620 C HIS A 90 16.917 -14.543 17.746 1.00 16.80 C ANISOU 620 C HIS C 90 2165 2336 1882 -161 25 -52 C ATOM 621 O HIS A 90 17.233 -14.404 16.612 1.00 13.68 O ANISOU 621 O HIS C 90 1796 3002 399 -790 37 -93 O ATOM 622 CB HIS A 90 16.106 -16.629 18.851 1.00 15.90 C ANISOU 622 CB HIS C 90 2304 2249 1487 69 343 -388 C ATOM 623 CG HIS A 90 16.820 -17.676 18.124 1.00 19.52 C ANISOU 623 CG HIS C 90 2479 2771 2167 363 530 -364 C ATOM 624 ND1 HIS A 90 16.303 -18.935 17.892 1.00 23.41 N ANISOU 624 ND1 HIS C 90 3217 2997 2679 74 -93 -202 N ATOM 625 CD2 HIS A 90 18.038 -17.648 17.536 1.00 26.46 C ANISOU 625 CD2 HIS C 90 3406 3325 3320 24 -175 -86 C ATOM 626 CE1 HIS A 90 17.198 -19.648 17.227 1.00 25.53 C ANISOU 626 CE1 HIS C 90 3550 2917 3231 213 -75 -107 C ATOM 627 NE2 HIS A 90 18.261 -18.892 17.001 1.00 29.40 N ANISOU 627 NE2 HIS C 90 3996 3339 3834 296 -198 76 N ATOM 628 N ALA A 91 17.567 -13.910 18.632 1.00 11.80 N ANISOU 628 N ALA C 91 1549 2221 713 -289 92 -249 N ATOM 629 CA ALA A 91 18.839 -13.264 18.467 1.00 15.51 C ANISOU 629 CA ALA C 91 1923 2645 1324 -262 36 -226 C ATOM 630 C ALA A 91 19.841 -14.200 19.277 1.00 12.95 C ANISOU 630 C ALA C 91 1608 2617 692 -418 -196 -719 C ATOM 631 O ALA A 91 19.600 -14.645 20.402 1.00 26.97 O ANISOU 631 O ALA C 91 2459 4358 3428 -80 171 -40 O ATOM 632 CB ALA A 91 18.788 -11.864 19.122 1.00 16.34 C ANISOU 632 CB ALA C 91 2462 2408 1337 -403 -58 -330 C ATOM 633 N GLU A 92 21.003 -14.437 18.542 1.00 18.54 N ANISOU 633 N GLU C 92 2069 3153 1820 -45 132 -181 N ATOM 634 CA GLU A 92 22.048 -15.292 19.049 1.00 18.47 C ANISOU 634 CA GLU C 92 2114 2962 1942 -112 31 -161 C ATOM 635 C GLU A 92 23.245 -14.397 19.229 1.00 17.49 C ANISOU 635 C GLU C 92 1960 2954 1729 -193 -39 -304 C ATOM 636 O GLU A 92 23.623 -13.645 18.298 1.00 21.99 O ANISOU 636 O GLU C 92 2401 3998 1954 -322 281 -697 O ATOM 637 CB GLU A 92 22.399 -16.406 18.029 1.00 20.74 C ANISOU 637 CB GLU C 92 2348 3222 2309 -36 82 -67 C ATOM 638 CG GLU A 92 21.328 -17.500 17.900 1.00 25.75 C ANISOU 638 CG GLU C 92 3190 3527 3064 -29 0 51 C ATOM 639 CD GLU A 92 21.733 -18.668 16.978 1.00 26.42 C ANISOU 639 CD GLU C 92 3176 3594 3268 -58 -11 123 C ATOM 640 OE1 GLU A 92 22.943 -18.776 16.618 1.00 35.62 O ANISOU 640 OE1 GLU C 92 4037 4829 4668 179 -173 -84 O ATOM 641 OE2 GLU A 92 20.874 -19.534 16.692 1.00 35.10 O ANISOU 641 OE2 GLU C 92 3954 4556 4825 -165 105 133 O ATOM 642 N VAL A 93 23.892 -14.451 20.367 1.00 13.48 N ANISOU 642 N VAL C 93 1652 2053 1415 120 57 -364 N ATOM 643 CA VAL A 93 25.105 -13.673 20.637 1.00 12.39 C ANISOU 643 CA VAL C 93 1751 1623 1333 74 -118 -275 C ATOM 644 C VAL A 93 26.185 -14.694 21.011 1.00 10.68 C ANISOU 644 C VAL C 93 1425 1404 1226 -31 -48 -342 C ATOM 645 O VAL A 93 26.045 -15.346 22.046 1.00 11.58 O ANISOU 645 O VAL C 93 1594 1532 1274 22 -148 -478 O ATOM 646 CB VAL A 93 24.818 -12.652 21.756 1.00 13.50 C ANISOU 646 CB VAL C 93 2018 1672 1438 230 -67 -249 C ATOM 647 CG1 VAL A 93 26.053 -11.856 22.002 1.00 17.08 C ANISOU 647 CG1 VAL C 93 2008 2249 2230 -278 -284 20 C ATOM 648 CG2 VAL A 93 23.580 -11.779 21.410 1.00 15.03 C ANISOU 648 CG2 VAL C 93 2034 1943 1732 247 -145 -341 C ATOM 649 N VAL A 94 27.229 -14.825 20.213 1.00 10.11 N ANISOU 649 N VAL C 94 1488 1303 1047 53 -17 -189 N ATOM 650 CA VAL A 94 28.235 -15.886 20.388 1.00 10.25 C ANISOU 650 CA VAL C 94 1406 1331 1157 -86 -110 -256 C ATOM 651 C VAL A 94 29.600 -15.209 20.583 1.00 9.74 C ANISOU 651 C VAL C 94 1331 1189 1181 -25 -23 -247 C ATOM 652 O VAL A 94 30.029 -14.367 19.800 1.00 10.34 O ANISOU 652 O VAL C 94 1479 1394 1056 -233 -25 -392 O ATOM 653 CB VAL A 94 28.266 -16.866 19.188 1.00 11.51 C ANISOU 653 CB VAL C 94 1519 1413 1438 -240 -30 -35 C ATOM 654 CG1 VAL A 94 29.227 -17.989 19.393 1.00 12.87 C ANISOU 654 CG1 VAL C 94 1684 1510 1696 238 -163 21 C ATOM 655 CG2 VAL A 94 26.843 -17.364 18.894 1.00 13.71 C ANISOU 655 CG2 VAL C 94 1612 1976 1619 -344 73 167 C ATOM 656 N PHE A 95 30.278 -15.620 21.665 1.00 9.84 N ANISOU 656 N PHE C 95 1404 1176 1158 60 32 -348 N ATOM 657 CA PHE A 95 31.519 -14.982 22.057 1.00 9.79 C ANISOU 657 CA PHE C 95 1425 1316 978 11 28 -254 C ATOM 658 C PHE A 95 32.364 -15.906 22.928 1.00 9.27 C ANISOU 658 C PHE C 95 1334 1154 1034 -5 71 -385 C ATOM 659 O PHE A 95 31.844 -16.755 23.638 1.00 11.59 O ANISOU 659 O PHE C 95 1493 1409 1499 12 -73 -498 O ATOM 660 CB PHE A 95 31.230 -13.698 22.830 1.00 11.07 C ANISOU 660 CB PHE C 95 1541 1373 1289 59 75 -177 C ATOM 661 CG PHE A 95 30.406 -13.885 24.053 1.00 11.89 C ANISOU 661 CG PHE C 95 1759 1288 1472 46 141 108 C ATOM 662 CD1 PHE A 95 29.030 -14.018 23.957 1.00 13.09 C ANISOU 662 CD1 PHE C 95 1883 1795 1294 92 -135 0 C ATOM 663 CD2 PHE A 95 31.007 -13.910 25.310 1.00 12.99 C ANISOU 663 CD2 PHE C 95 1971 1533 1429 94 -45 -187 C ATOM 664 CE1 PHE A 95 28.221 -14.133 25.045 1.00 13.64 C ANISOU 664 CE1 PHE C 95 1918 1757 1508 -82 -175 101 C ATOM 665 CE2 PHE A 95 30.180 -14.053 26.470 1.00 13.82 C ANISOU 665 CE2 PHE C 95 2529 1391 1330 307 101 66 C ATOM 666 CZ PHE A 95 28.804 -14.213 26.281 1.00 14.03 C ANISOU 666 CZ PHE C 95 2405 1752 1171 23 -429 -475 C ATOM 667 N THR A 96 33.662 -15.698 22.845 1.00 11.38 N ANISOU 667 N THR C 96 1532 1396 1393 -1 -17 -553 N ATOM 668 CA THR A 96 34.602 -16.308 23.764 1.00 11.70 C ANISOU 668 CA THR C 96 1395 1436 1612 -37 -6 -480 C ATOM 669 C THR A 96 34.619 -15.504 25.057 1.00 11.95 C ANISOU 669 C THR C 96 1520 1441 1576 -132 130 -467 C ATOM 670 O THR A 96 34.635 -14.288 25.016 1.00 14.73 O ANISOU 670 O THR C 96 2207 1617 1772 -140 305 -347 O ATOM 671 CB THR A 96 36.004 -16.350 23.161 1.00 12.82 C ANISOU 671 CB THR C 96 1355 1677 1838 56 -114 -484 C ATOM 672 OG1 THR A 96 35.982 -17.148 21.978 1.00 16.25 O ANISOU 672 OG1 THR C 96 1900 2155 2118 319 -169 -366 O ATOM 673 CG2 THR A 96 36.979 -16.945 24.136 1.00 15.54 C ANISOU 673 CG2 THR C 96 1729 2292 1883 222 39 -664 C ATOM 674 N ALA A 97 34.541 -16.185 26.194 1.00 12.13 N ANISOU 674 N ALA C 97 1603 1345 1660 -44 110 -441 N ATOM 675 CA ALA A 97 34.543 -15.513 27.474 1.00 12.15 C ANISOU 675 CA ALA C 97 1464 1545 1606 -4 143 -440 C ATOM 676 C ALA A 97 35.676 -16.036 28.343 1.00 11.52 C ANISOU 676 C ALA C 97 1516 1288 1572 -66 195 -582 C ATOM 677 O ALA A 97 36.032 -17.197 28.263 1.00 14.96 O ANISOU 677 O ALA C 97 1933 1686 2064 -35 240 -342 O ATOM 678 CB ALA A 97 33.188 -15.707 28.232 1.00 13.66 C ANISOU 678 CB ALA C 97 1410 2091 1690 -233 204 -495 C ATOM 679 N ASN A 98 36.199 -15.134 29.186 1.00 12.58 N ANISOU 679 N ASN C 98 1671 1449 1659 182 230 -413 N ATOM 680 CA ASN A 98 37.106 -15.450 30.268 1.00 14.13 C ANISOU 680 CA ASN C 98 1746 1775 1846 92 173 -298 C ATOM 681 C ASN A 98 38.428 -16.013 29.853 1.00 16.98 C ANISOU 681 C ASN C 98 1926 2242 2282 211 242 -150 C ATOM 682 O ASN A 98 39.117 -16.683 30.639 1.00 18.22 O ANISOU 682 O ASN C 98 1845 2659 2417 545 336 -241 O ATOM 683 CB ASN A 98 36.443 -16.371 31.308 1.00 14.84 C ANISOU 683 CB ASN C 98 2061 1777 1800 142 249 -331 C ATOM 684 CG ASN A 98 35.162 -15.831 31.814 1.00 13.93 C ANISOU 684 CG ASN C 98 1904 1854 1532 121 350 -580 C ATOM 685 OD1 ASN A 98 35.105 -14.680 32.303 1.00 15.14 O ANISOU 685 OD1 ASN C 98 2021 1893 1835 178 409 -229 O ATOM 686 ND2 ASN A 98 34.086 -16.601 31.624 1.00 15.44 N ANISOU 686 ND2 ASN C 98 1934 2096 1833 -229 134 -433 N ATOM 687 N ASP A 99 38.813 -15.742 28.626 1.00 17.34 N ANISOU 687 N ASP C 99 1801 2371 2413 292 190 -194 N ATOM 688 CA ASP A 99 40.043 -16.349 28.128 1.00 20.22 C ANISOU 688 CA ASP C 99 2220 2753 2708 94 21 -66 C ATOM 689 C ASP A 99 41.317 -15.621 28.576 1.00 20.44 C ANISOU 689 C ASP C 99 2039 2894 2831 178 56 -40 C ATOM 690 O ASP A 99 42.425 -16.103 28.338 1.00 21.77 O ANISOU 690 O ASP C 99 1801 3294 3176 248 -185 145 O ATOM 691 CB ASP A 99 39.931 -16.578 26.628 1.00 21.94 C ANISOU 691 CB ASP C 99 2458 2995 2882 246 -48 -136 C ATOM 692 CG ASP A 99 39.766 -15.342 25.900 1.00 24.82 C ANISOU 692 CG ASP C 99 3259 3237 2934 62 -173 -403 C ATOM 693 OD1 ASP A 99 39.063 -14.432 26.430 1.00 28.75 O ANISOU 693 OD1 ASP C 99 4225 3959 2736 -92 -439 -351 O ATOM 694 OD2 ASP A 99 40.310 -15.285 24.771 1.00 33.98 O ANISOU 694 OD2 ASP C 99 4006 4849 4053 278 -336 -135 O ATOM 695 N SER A 100 41.162 -14.464 29.223 1.00 20.87 N ANISOU 695 N SER C 100 1989 2998 2941 -18 155 47 N ATOM 696 CA SER A 100 42.277 -13.738 29.869 1.00 22.21 C ANISOU 696 CA SER C 100 2317 2988 3132 -26 205 -27 C ATOM 697 C SER A 100 41.947 -13.569 31.323 1.00 21.41 C ANISOU 697 C SER C 100 2241 2801 3091 -142 222 -109 C ATOM 698 O SER A 100 42.327 -12.576 31.953 1.00 26.51 O ANISOU 698 O SER C 100 3158 3282 3630 -309 152 -7 O ATOM 699 CB SER A 100 42.439 -12.366 29.227 1.00 23.54 C ANISOU 699 CB SER C 100 2430 3209 3303 -47 154 -14 C ATOM 700 OG SER A 100 42.771 -12.519 27.858 1.00 30.71 O ANISOU 700 OG SER C 100 3640 4268 3761 -152 -83 123 O ATOM 701 N GLY A 101 41.224 -14.525 31.890 1.00 19.67 N ANISOU 701 N GLY C 101 2101 2489 2881 47 348 -246 N ATOM 702 CA GLY A 101 40.843 -14.450 33.241 1.00 18.64 C ANISOU 702 CA GLY C 101 2032 2447 2599 78 337 -265 C ATOM 703 C GLY A 101 39.426 -13.946 33.371 1.00 17.71 C ANISOU 703 C GLY C 101 1975 2264 2489 102 391 -342 C ATOM 704 O GLY A 101 38.778 -13.499 32.360 1.00 17.08 O ANISOU 704 O GLY C 101 1792 2404 2292 139 742 -543 O ATOM 705 N PRO A 102 38.865 -13.995 34.579 1.00 17.46 N ANISOU 705 N PRO C 102 2029 2371 2232 164 635 -501 N ATOM 706 CA PRO A 102 37.453 -13.685 34.731 1.00 17.53 C ANISOU 706 CA PRO C 102 2075 2244 2341 -15 341 -416 C ATOM 707 C PRO A 102 37.151 -12.248 34.316 1.00 17.10 C ANISOU 707 C PRO C 102 1945 2192 2359 1 459 -427 C ATOM 708 O PRO A 102 37.848 -11.305 34.680 1.00 17.47 O ANISOU 708 O PRO C 102 2170 2218 2250 53 752 -549 O ATOM 709 CB PRO A 102 37.189 -13.896 36.232 1.00 17.91 C ANISOU 709 CB PRO C 102 2109 2436 2258 -165 470 -281 C ATOM 710 CG PRO A 102 38.521 -14.171 36.860 1.00 20.03 C ANISOU 710 CG PRO C 102 2403 2852 2355 182 570 -408 C ATOM 711 CD PRO A 102 39.544 -14.376 35.842 1.00 18.24 C ANISOU 711 CD PRO C 102 2050 2574 2302 153 656 -578 C ATOM 712 N ARG A 103 36.036 -12.079 33.601 1.00 15.99 N ANISOU 712 N ARG C 103 1878 2103 2094 -47 584 -451 N ATOM 713 CA ARG A 103 35.475 -10.745 33.317 1.00 15.78 C ANISOU 713 CA ARG C 103 1868 2082 2044 -36 404 -349 C ATOM 714 C ARG A 103 33.990 -10.768 33.622 1.00 15.32 C ANISOU 714 C ARG C 103 1793 2057 1969 -150 402 -413 C ATOM 715 O ARG A 103 33.393 -11.843 33.783 1.00 15.76 O ANISOU 715 O ARG C 103 1700 2159 2128 -220 439 -498 O ATOM 716 CB ARG A 103 35.700 -10.343 31.895 1.00 15.53 C ANISOU 716 CB ARG C 103 1839 1958 2102 -3 270 -256 C ATOM 717 CG ARG A 103 37.126 -10.229 31.465 1.00 17.14 C ANISOU 717 CG ARG C 103 1996 2232 2283 -80 330 -324 C ATOM 718 CD ARG A 103 37.840 -9.073 32.102 1.00 18.79 C ANISOU 718 CD ARG C 103 2190 2253 2694 -207 8 -109 C ATOM 719 NE ARG A 103 39.202 -8.950 31.571 1.00 21.35 N ANISOU 719 NE ARG C 103 2102 2694 3316 -275 212 -199 N ATOM 720 CZ ARG A 103 40.252 -9.620 32.034 1.00 22.26 C ANISOU 720 CZ ARG C 103 2204 3031 3223 -237 -97 -105 C ATOM 721 NH1 ARG A 103 40.169 -10.407 33.108 1.00 22.93 N ANISOU 721 NH1 ARG C 103 2148 2890 3670 -129 221 -100 N ATOM 722 NH2 ARG A 103 41.432 -9.424 31.424 1.00 23.62 N ANISOU 722 NH2 ARG C 103 1834 3295 3842 -433 -377 -243 N ATOM 723 N ARG A 104 33.411 -9.579 33.737 1.00 13.88 N ANISOU 723 N ARG C 104 1504 2111 1657 -143 325 -367 N ATOM 724 CA ARG A 104 31.975 -9.431 33.839 1.00 15.51 C ANISOU 724 CA ARG C 104 1884 2139 1869 -36 305 -411 C ATOM 725 C ARG A 104 31.398 -8.945 32.496 1.00 13.04 C ANISOU 725 C ARG C 104 1778 1677 1497 -61 313 -415 C ATOM 726 O ARG A 104 31.900 -7.996 31.928 1.00 14.43 O ANISOU 726 O ARG C 104 1898 1761 1822 -235 494 -520 O ATOM 727 CB ARG A 104 31.591 -8.426 34.910 1.00 17.07 C ANISOU 727 CB ARG C 104 1996 2449 2041 -60 222 -320 C ATOM 728 CG ARG A 104 32.168 -8.838 36.296 1.00 22.81 C ANISOU 728 CG ARG C 104 3028 3190 2446 164 300 -300 C ATOM 729 CD ARG A 104 31.535 -8.114 37.430 1.00 28.42 C ANISOU 729 CD ARG C 104 3633 3820 3343 -23 58 48 C ATOM 730 NE ARG A 104 32.297 -8.277 38.670 1.00 32.92 N ANISOU 730 NE ARG C 104 4281 4616 3611 43 257 -110 N ATOM 731 CZ ARG A 104 32.464 -9.426 39.333 1.00 37.24 C ANISOU 731 CZ ARG C 104 4829 4764 4554 -42 198 -164 C ATOM 732 NH1 ARG A 104 31.945 -10.593 38.891 1.00 39.33 N ANISOU 732 NH1 ARG C 104 5057 5088 4797 -71 133 29 N ATOM 733 NH2 ARG A 104 33.179 -9.418 40.462 1.00 39.15 N ANISOU 733 NH2 ARG C 104 5037 5232 4605 -126 239 -78 N ATOM 734 N TYR A 105 30.382 -9.673 32.065 1.00 11.48 N ANISOU 734 N TYR C 105 1377 1601 1383 -52 289 -445 N ATOM 735 CA TYR A 105 29.777 -9.455 30.772 1.00 11.42 C ANISOU 735 CA TYR C 105 1419 1542 1377 5 165 -303 C ATOM 736 C TYR A 105 28.339 -9.019 30.914 1.00 11.08 C ANISOU 736 C TYR C 105 1396 1468 1346 -37 121 -307 C ATOM 737 O TYR A 105 27.570 -9.722 31.519 1.00 13.05 O ANISOU 737 O TYR C 105 1476 1722 1758 -1 143 -677 O ATOM 738 CB TYR A 105 29.814 -10.739 29.920 1.00 11.46 C ANISOU 738 CB TYR C 105 1521 1445 1386 -23 136 -194 C ATOM 739 CG TYR A 105 31.206 -11.236 29.634 1.00 10.72 C ANISOU 739 CG TYR C 105 1466 1222 1384 76 64 -108 C ATOM 740 CD1 TYR A 105 31.897 -12.027 30.573 1.00 12.16 C ANISOU 740 CD1 TYR C 105 1762 1327 1529 -50 56 -327 C ATOM 741 CD2 TYR A 105 31.855 -10.894 28.476 1.00 12.50 C ANISOU 741 CD2 TYR C 105 1360 1743 1644 -186 225 -39 C ATOM 742 CE1 TYR A 105 33.171 -12.477 30.330 1.00 12.57 C ANISOU 742 CE1 TYR C 105 1686 1250 1840 -115 46 -458 C ATOM 743 CE2 TYR A 105 33.176 -11.328 28.277 1.00 12.80 C ANISOU 743 CE2 TYR C 105 1692 1595 1577 -152 182 -269 C ATOM 744 CZ TYR A 105 33.822 -12.114 29.213 1.00 11.42 C ANISOU 744 CZ TYR C 105 1208 1356 1775 30 113 -256 C ATOM 745 OH TYR A 105 35.125 -12.484 29.035 1.00 12.43 O ANISOU 745 OH TYR C 105 1532 1230 1961 138 118 -231 O ATOM 746 N THR A 106 27.977 -7.902 30.261 1.00 11.14 N ANISOU 746 N THR C 106 1255 1514 1462 52 272 -363 N ATOM 747 CA THR A 106 26.591 -7.524 30.056 1.00 10.97 C ANISOU 747 CA THR C 106 1293 1595 1277 91 69 -257 C ATOM 748 C THR A 106 26.326 -7.629 28.569 1.00 10.95 C ANISOU 748 C THR C 106 1260 1562 1336 163 85 -305 C ATOM 749 O THR A 106 26.975 -6.981 27.775 1.00 12.00 O ANISOU 749 O THR C 106 1515 1779 1263 -151 291 -455 O ATOM 750 CB THR A 106 26.314 -6.115 30.566 1.00 12.71 C ANISOU 750 CB THR C 106 1640 1715 1474 143 113 -242 C ATOM 751 OG1 THR A 106 26.560 -6.103 31.965 1.00 16.91 O ANISOU 751 OG1 THR C 106 2664 2359 1401 -220 58 22 O ATOM 752 CG2 THR A 106 24.866 -5.723 30.278 1.00 14.77 C ANISOU 752 CG2 THR C 106 1693 1919 1998 315 195 -124 C ATOM 753 N ILE A 107 25.325 -8.445 28.237 1.00 10.65 N ANISOU 753 N ILE C 107 1304 1711 1030 -19 177 -437 N ATOM 754 CA ILE A 107 24.831 -8.564 26.874 1.00 11.01 C ANISOU 754 CA ILE C 107 1289 1834 1060 57 -32 -285 C ATOM 755 C ILE A 107 23.534 -7.788 26.807 1.00 11.47 C ANISOU 755 C ILE C 107 1440 1845 1073 68 34 -164 C ATOM 756 O ILE A 107 22.577 -8.142 27.459 1.00 12.40 O ANISOU 756 O ILE C 107 1395 1960 1354 172 -97 -330 O ATOM 757 CB ILE A 107 24.626 -10.049 26.455 1.00 12.65 C ANISOU 757 CB ILE C 107 1601 1832 1370 19 -104 -304 C ATOM 758 CG1 ILE A 107 25.912 -10.873 26.677 1.00 15.22 C ANISOU 758 CG1 ILE C 107 2006 1908 1869 70 30 -381 C ATOM 759 CG2 ILE A 107 24.054 -10.142 25.024 1.00 15.10 C ANISOU 759 CG2 ILE C 107 1842 2575 1318 -209 14 -185 C ATOM 760 CD1 ILE A 107 27.146 -10.381 25.906 1.00 16.74 C ANISOU 760 CD1 ILE C 107 2003 2121 2235 51 -389 -15 C ATOM 761 N ALA A 108 23.553 -6.676 26.087 1.00 11.31 N ANISOU 761 N ALA C 108 1286 1911 1098 138 4 -173 N ATOM 762 CA ALA A 108 22.407 -5.827 25.911 1.00 12.44 C ANISOU 762 CA ALA C 108 1513 2057 1154 290 85 -224 C ATOM 763 C ALA A 108 21.822 -6.058 24.503 1.00 13.00 C ANISOU 763 C ALA C 108 1657 2040 1240 270 -34 -148 C ATOM 764 O ALA A 108 22.556 -6.318 23.536 1.00 14.07 O ANISOU 764 O ALA C 108 1626 2526 1192 339 -157 -17 O ATOM 765 CB ALA A 108 22.830 -4.356 26.071 1.00 15.05 C ANISOU 765 CB ALA C 108 1999 2107 1609 398 132 -347 C ATOM 766 N ALA A 109 20.510 -5.945 24.416 1.00 11.32 N ANISOU 766 N ALA C 109 1443 1756 1100 463 -38 -196 N ATOM 767 CA ALA A 109 19.825 -6.100 23.115 1.00 10.11 C ANISOU 767 CA ALA C 109 1295 1533 1011 440 53 -214 C ATOM 768 C ALA A 109 18.687 -5.111 23.086 1.00 10.13 C ANISOU 768 C ALA C 109 1236 1603 1008 349 -36 -59 C ATOM 769 O ALA A 109 18.008 -4.853 24.092 1.00 11.94 O ANISOU 769 O ALA C 109 1445 2057 1034 708 -116 -134 O ATOM 770 CB ALA A 109 19.333 -7.469 22.949 1.00 12.28 C ANISOU 770 CB ALA C 109 1312 1802 1551 207 -18 -39 C ATOM 771 N LEU A 110 18.483 -4.556 21.906 1.00 9.96 N ANISOU 771 N LEU C 110 1508 1420 855 399 43 43 N ATOM 772 CA LEU A 110 17.397 -3.626 21.598 1.00 10.00 C ANISOU 772 CA LEU C 110 1476 1444 879 352 173 20 C ATOM 773 C LEU A 110 16.546 -4.197 20.507 1.00 9.66 C ANISOU 773 C LEU C 110 1381 1374 914 291 226 98 C ATOM 774 O LEU A 110 17.075 -4.491 19.463 1.00 10.67 O ANISOU 774 O LEU C 110 1406 1863 784 379 -41 260 O ATOM 775 CB LEU A 110 18.017 -2.314 21.159 1.00 11.62 C ANISOU 775 CB LEU C 110 1592 1658 1162 271 107 0 C ATOM 776 CG LEU A 110 17.056 -1.262 20.706 1.00 12.13 C ANISOU 776 CG LEU C 110 1758 1450 1400 303 346 -109 C ATOM 777 CD1 LEU A 110 16.209 -0.747 21.849 1.00 12.73 C ANISOU 777 CD1 LEU C 110 1678 1380 1780 297 142 10 C ATOM 778 CD2 LEU A 110 17.822 -0.062 20.087 1.00 15.95 C ANISOU 778 CD2 LEU C 110 2247 2096 1715 145 24 -325 C ATOM 779 N LEU A 111 15.284 -4.414 20.758 1.00 9.45 N ANISOU 779 N LEU C 111 1332 1334 922 512 46 324 N ATOM 780 CA LEU A 111 14.409 -5.176 19.842 1.00 9.76 C ANISOU 780 CA LEU C 111 1365 1445 896 483 172 188 C ATOM 781 C LEU A 111 13.358 -4.348 19.099 1.00 10.72 C ANISOU 781 C LEU C 111 1579 1604 887 469 216 113 C ATOM 782 O LEU A 111 12.649 -3.562 19.763 1.00 10.78 O ANISOU 782 O LEU C 111 1529 1637 929 611 170 252 O ATOM 783 CB LEU A 111 13.651 -6.226 20.638 1.00 10.35 C ANISOU 783 CB LEU C 111 1525 1410 995 325 81 367 C ATOM 784 CG LEU A 111 14.478 -7.211 21.479 1.00 10.84 C ANISOU 784 CG LEU C 111 1526 1558 1034 245 213 183 C ATOM 785 CD1 LEU A 111 13.520 -8.265 22.097 1.00 12.77 C ANISOU 785 CD1 LEU C 111 1493 1779 1581 216 -154 -161 C ATOM 786 CD2 LEU A 111 15.639 -7.805 20.747 1.00 11.59 C ANISOU 786 CD2 LEU C 111 1376 1616 1411 456 32 36 C ATOM 787 N SER A 112 13.217 -4.621 17.833 1.00 11.88 N ANISOU 787 N SER C 112 1602 1731 1180 604 274 276 N ATOM 788 CA SER A 112 12.121 -4.209 17.020 1.00 11.24 C ANISOU 788 CA SER C 112 1772 1492 1004 483 291 201 C ATOM 789 C SER A 112 11.636 -5.424 16.222 1.00 11.28 C ANISOU 789 C SER C 112 1720 1527 1035 511 486 248 C ATOM 790 O SER A 112 12.371 -6.386 16.101 1.00 11.11 O ANISOU 790 O SER C 112 1822 1280 1118 547 444 133 O ATOM 791 CB SER A 112 12.558 -3.140 16.032 1.00 11.43 C ANISOU 791 CB SER C 112 1889 1359 1093 444 302 167 C ATOM 792 OG SER A 112 13.025 -1.977 16.720 1.00 13.64 O ANISOU 792 OG SER C 112 2339 1480 1363 431 472 140 O ATOM 793 N PRO A 113 10.406 -5.384 15.706 1.00 13.01 N ANISOU 793 N PRO C 113 1927 1679 1337 626 408 235 N ATOM 794 CA PRO A 113 9.931 -6.599 15.050 1.00 12.32 C ANISOU 794 CA PRO C 113 1767 1764 1149 439 259 421 C ATOM 795 C PRO A 113 10.790 -7.113 13.871 1.00 12.23 C ANISOU 795 C PRO C 113 1755 1668 1223 517 416 365 C ATOM 796 O PRO A 113 10.865 -8.337 13.717 1.00 14.18 O ANISOU 796 O PRO C 113 2207 1644 1535 540 412 176 O ATOM 797 CB PRO A 113 8.515 -6.218 14.574 1.00 13.87 C ANISOU 797 CB PRO C 113 1855 2010 1405 416 389 583 C ATOM 798 CG PRO A 113 8.076 -5.252 15.707 1.00 15.35 C ANISOU 798 CG PRO C 113 1864 2401 1566 667 268 585 C ATOM 799 CD PRO A 113 9.314 -4.434 15.968 1.00 13.27 C ANISOU 799 CD PRO C 113 1835 1821 1383 719 284 301 C ATOM 800 N TYR A 114 11.416 -6.209 13.116 1.00 10.81 N ANISOU 800 N TYR C 114 1517 1519 1071 488 329 319 N ATOM 801 CA TYR A 114 12.250 -6.622 11.949 1.00 11.85 C ANISOU 801 CA TYR C 114 1836 1515 1150 520 232 120 C ATOM 802 C TYR A 114 13.721 -6.250 12.096 1.00 12.47 C ANISOU 802 C TYR C 114 1867 1552 1319 483 132 240 C ATOM 803 O TYR A 114 14.491 -6.298 11.136 1.00 12.17 O ANISOU 803 O TYR C 114 1817 1755 1050 594 272 216 O ATOM 804 CB TYR A 114 11.700 -6.057 10.629 1.00 13.03 C ANISOU 804 CB TYR C 114 1887 1726 1337 418 316 176 C ATOM 805 CG TYR A 114 10.517 -6.859 10.097 1.00 11.91 C ANISOU 805 CG TYR C 114 1853 1655 1015 388 287 190 C ATOM 806 CD1 TYR A 114 9.294 -6.791 10.702 1.00 16.76 C ANISOU 806 CD1 TYR C 114 2177 2769 1422 -3 161 199 C ATOM 807 CD2 TYR A 114 10.619 -7.648 8.947 1.00 13.48 C ANISOU 807 CD2 TYR C 114 2348 1372 1400 330 377 194 C ATOM 808 CE1 TYR A 114 8.197 -7.513 10.196 1.00 18.81 C ANISOU 808 CE1 TYR C 114 2263 3255 1629 -97 92 435 C ATOM 809 CE2 TYR A 114 9.516 -8.322 8.452 1.00 15.31 C ANISOU 809 CE2 TYR C 114 2221 2125 1470 159 567 130 C ATOM 810 CZ TYR A 114 8.325 -8.263 9.067 1.00 18.00 C ANISOU 810 CZ TYR C 114 2482 2384 1972 -271 282 93 C ATOM 811 OH TYR A 114 7.201 -8.917 8.613 1.00 23.67 O ANISOU 811 OH TYR C 114 2924 3814 2253 -214 297 130 O ATOM 812 N SER A 115 14.151 -5.976 13.329 1.00 12.04 N ANISOU 812 N SER C 115 1786 1577 1208 416 213 260 N ATOM 813 CA SER A 115 15.531 -5.512 13.527 1.00 11.67 C ANISOU 813 CA SER C 115 1835 1531 1066 312 124 359 C ATOM 814 C SER A 115 15.914 -5.672 15.007 1.00 11.29 C ANISOU 814 C SER C 115 1613 1645 1033 434 104 306 C ATOM 815 O SER A 115 15.074 -5.479 15.889 1.00 13.30 O ANISOU 815 O SER C 115 1756 2220 1076 605 261 506 O ATOM 816 CB SER A 115 15.652 -4.064 13.111 1.00 13.44 C ANISOU 816 CB SER C 115 2250 1567 1288 316 58 504 C ATOM 817 OG SER A 115 16.966 -3.558 13.265 1.00 15.57 O ANISOU 817 OG SER C 115 2724 1596 1594 310 160 462 O ATOM 818 N TYR A 116 17.187 -5.966 15.258 1.00 10.14 N ANISOU 818 N TYR C 116 1358 1602 889 203 203 349 N ATOM 819 CA TYR A 116 17.701 -5.876 16.631 1.00 10.33 C ANISOU 819 CA TYR C 116 1565 1419 941 67 53 208 C ATOM 820 C TYR A 116 19.153 -5.460 16.608 1.00 10.66 C ANISOU 820 C TYR C 116 1543 1493 1011 150 184 124 C ATOM 821 O TYR A 116 19.843 -5.670 15.611 1.00 10.54 O ANISOU 821 O TYR C 116 1529 1638 836 130 73 71 O ATOM 822 CB TYR A 116 17.457 -7.157 17.398 1.00 11.89 C ANISOU 822 CB TYR C 116 1812 1708 995 27 -59 126 C ATOM 823 CG TYR A 116 18.195 -8.344 16.895 1.00 11.49 C ANISOU 823 CG TYR C 116 1914 1305 1146 -53 12 -7 C ATOM 824 CD1 TYR A 116 19.518 -8.596 17.252 1.00 11.33 C ANISOU 824 CD1 TYR C 116 1813 1322 1168 115 -141 193 C ATOM 825 CD2 TYR A 116 17.592 -9.191 15.994 1.00 12.03 C ANISOU 825 CD2 TYR C 116 1818 1474 1278 -172 9 65 C ATOM 826 CE1 TYR A 116 20.218 -9.690 16.704 1.00 12.56 C ANISOU 826 CE1 TYR C 116 1892 1628 1249 -65 -16 8 C ATOM 827 CE2 TYR A 116 18.241 -10.280 15.504 1.00 13.43 C ANISOU 827 CE2 TYR C 116 2019 1583 1499 -160 -34 128 C ATOM 828 CZ TYR A 116 19.542 -10.530 15.822 1.00 11.16 C ANISOU 828 CZ TYR C 116 1814 1192 1233 88 -114 51 C ATOM 829 OH TYR A 116 20.202 -11.608 15.296 1.00 14.80 O ANISOU 829 OH TYR C 116 2280 1535 1808 -180 -140 600 O ATOM 830 N SER A 117 19.585 -4.933 17.733 1.00 10.01 N ANISOU 830 N SER C 117 1501 1534 766 222 -18 65 N ATOM 831 CA ASER A 117 20.934 -4.557 17.999 0.50 10.74 C ANISOU 831 CA ASER C 117 1521 1598 959 66 -22 107 C ATOM 832 C SER A 117 21.386 -5.315 19.240 1.00 10.79 C ANISOU 832 C SER C 117 1404 1653 1039 63 -42 166 C ATOM 833 O SER A 117 20.583 -5.473 20.156 1.00 12.50 O ANISOU 833 O SER C 117 1587 2110 1050 262 -20 -251 O ATOM 834 CB ASER A 117 20.924 -3.051 18.285 0.50 11.32 C ANISOU 834 CB ASER C 117 1630 1606 1062 40 42 -25 C ATOM 835 OG ASER A 117 22.210 -2.552 18.520 0.50 14.67 O ANISOU 835 OG ASER C 117 2038 2179 1354 -249 198 -23 O ATOM 836 N THR A 118 22.653 -5.648 19.324 1.00 10.14 N ANISOU 836 N THR C 118 1134 1628 1089 30 10 -106 N ATOM 837 CA THR A 118 23.209 -6.153 20.545 1.00 11.24 C ANISOU 837 CA THR C 118 1348 1773 1148 122 -30 -81 C ATOM 838 C THR A 118 24.575 -5.557 20.759 1.00 11.37 C ANISOU 838 C THR C 118 1322 1898 1099 136 -24 -150 C ATOM 839 O THR A 118 25.359 -5.385 19.812 1.00 13.40 O ANISOU 839 O THR C 118 1500 2459 1132 -87 24 -117 O ATOM 840 CB THR A 118 23.223 -7.687 20.523 1.00 13.16 C ANISOU 840 CB THR C 118 1673 1934 1393 135 -33 -111 C ATOM 841 OG1 THR A 118 23.669 -8.204 21.752 1.00 14.00 O ANISOU 841 OG1 THR C 118 1775 2089 1455 283 -42 -301 O ATOM 842 CG2 THR A 118 24.156 -8.270 19.452 1.00 13.49 C ANISOU 842 CG2 THR C 118 1644 1760 1718 271 -353 12 C ATOM 843 N THR A 119 24.888 -5.287 22.027 1.00 11.14 N ANISOU 843 N THR C 119 1350 1804 1076 99 108 -315 N ATOM 844 CA THR A 119 26.186 -4.769 22.405 1.00 11.47 C ANISOU 844 CA THR C 119 1485 1663 1209 91 281 -223 C ATOM 845 C THR A 119 26.658 -5.486 23.633 1.00 11.57 C ANISOU 845 C THR C 119 1533 1527 1336 32 125 -128 C ATOM 846 O THR A 119 25.858 -5.930 24.450 1.00 13.19 O ANISOU 846 O THR C 119 1414 2110 1486 -71 26 -599 O ATOM 847 CB THR A 119 26.129 -3.281 22.712 1.00 14.40 C ANISOU 847 CB THR C 119 2010 1775 1685 204 446 -492 C ATOM 848 OG1 THR A 119 25.410 -2.640 21.677 1.00 18.62 O ANISOU 848 OG1 THR C 119 2983 2304 1788 279 267 -359 O ATOM 849 CG2 THR A 119 27.560 -2.704 22.747 1.00 15.13 C ANISOU 849 CG2 THR C 119 2233 1335 2181 -8 525 -414 C ATOM 850 N ALA A 120 27.953 -5.645 23.746 1.00 10.42 N ANISOU 850 N ALA C 120 1260 1645 1053 7 191 -337 N ATOM 851 CA ALA A 120 28.581 -6.231 24.959 1.00 10.91 C ANISOU 851 CA ALA C 120 1395 1444 1307 -24 348 -365 C ATOM 852 C ALA A 120 29.308 -5.145 25.720 1.00 10.14 C ANISOU 852 C ALA C 120 1115 1592 1142 -74 333 -372 C ATOM 853 O ALA A 120 30.008 -4.322 25.131 1.00 12.91 O ANISOU 853 O ALA C 120 1427 1970 1507 -312 249 -486 O ATOM 854 CB ALA A 120 29.518 -7.336 24.589 1.00 13.34 C ANISOU 854 CB ALA C 120 1616 1595 1857 -45 157 -200 C ATOM 855 N VAL A 121 29.127 -5.156 27.027 1.00 10.75 N ANISOU 855 N VAL C 121 1478 1392 1212 -60 162 -200 N ATOM 856 CA VAL A 121 29.932 -4.341 27.912 1.00 11.98 C ANISOU 856 CA VAL C 121 1631 1542 1379 -87 276 -300 C ATOM 857 C VAL A 121 30.706 -5.336 28.769 1.00 11.57 C ANISOU 857 C VAL C 121 1610 1549 1236 -164 306 -253 C ATOM 858 O VAL A 121 30.100 -6.132 29.505 1.00 13.13 O ANISOU 858 O VAL C 121 1711 1775 1502 -270 192 -508 O ATOM 859 CB VAL A 121 29.076 -3.387 28.801 1.00 13.84 C ANISOU 859 CB VAL C 121 1822 1829 1607 -103 211 -243 C ATOM 860 CG1 VAL A 121 29.986 -2.612 29.784 1.00 18.27 C ANISOU 860 CG1 VAL C 121 2525 2410 2006 -451 -123 118 C ATOM 861 CG2 VAL A 121 28.256 -2.448 27.925 1.00 18.15 C ANISOU 861 CG2 VAL C 121 2476 2136 2282 510 202 -350 C ATOM 862 N VAL A 122 32.029 -5.251 28.686 1.00 11.82 N ANISOU 862 N VAL C 122 1657 1502 1333 -132 201 -391 N ATOM 863 CA VAL A 122 32.914 -6.184 29.354 1.00 12.39 C ANISOU 863 CA VAL C 122 1624 1577 1504 -112 329 -336 C ATOM 864 C VAL A 122 33.771 -5.378 30.325 1.00 13.37 C ANISOU 864 C VAL C 122 1741 1652 1687 -196 347 -366 C ATOM 865 O VAL A 122 34.433 -4.426 29.936 1.00 14.25 O ANISOU 865 O VAL C 122 1756 1744 1912 -170 475 -312 O ATOM 866 CB VAL A 122 33.816 -6.908 28.338 1.00 12.48 C ANISOU 866 CB VAL C 122 1741 1446 1554 -77 355 -430 C ATOM 867 CG1 VAL A 122 34.700 -7.953 29.041 1.00 14.99 C ANISOU 867 CG1 VAL C 122 2198 1520 1978 331 389 -274 C ATOM 868 CG2 VAL A 122 32.984 -7.526 27.281 1.00 15.17 C ANISOU 868 CG2 VAL C 122 2602 1532 1630 -127 326 -21 C ATOM 869 N THR A 123 33.735 -5.786 31.592 1.00 14.44 N ANISOU 869 N THR C 123 1785 1934 1768 -307 471 -133 N ATOM 870 CA THR A 123 34.490 -5.078 32.645 1.00 16.61 C ANISOU 870 CA THR C 123 2073 2205 2031 -161 418 -59 C ATOM 871 C THR A 123 35.370 -6.055 33.396 1.00 16.78 C ANISOU 871 C THR C 123 2142 2058 2174 -153 489 -143 C ATOM 872 O THR A 123 35.084 -7.239 33.502 1.00 16.26 O ANISOU 872 O THR C 123 1822 2308 2047 -393 673 -338 O ATOM 873 CB THR A 123 33.583 -4.325 33.603 1.00 20.05 C ANISOU 873 CB THR C 123 2470 2670 2475 -31 354 53 C ATOM 874 OG1 THR A 123 32.892 -5.223 34.418 1.00 25.64 O ANISOU 874 OG1 THR C 123 3356 3545 2838 -11 -117 93 O ATOM 875 CG2 THR A 123 32.546 -3.545 32.864 1.00 21.04 C ANISOU 875 CG2 THR C 123 2489 2935 2567 400 198 215 C ATOM 876 N ASN A 124 36.478 -5.530 33.904 1.00 21.09 N ANISOU 876 N ASN C 124 2566 2551 2895 -105 554 -98 N ATOM 877 CA ASN A 124 37.412 -6.362 34.667 1.00 23.15 C ANISOU 877 CA ASN C 124 2945 2832 3016 -44 444 -134 C ATOM 878 C ASN A 124 37.220 -6.034 36.104 1.00 26.48 C ANISOU 878 C ASN C 124 3380 3247 3434 23 344 -86 C ATOM 879 O ASN A 124 37.542 -4.929 36.512 1.00 27.38 O ANISOU 879 O ASN C 124 3520 3367 3515 -60 514 -3 O ATOM 880 CB ASN A 124 38.863 -6.069 34.251 1.00 23.55 C ANISOU 880 CB ASN C 124 2938 2874 3136 -8 423 -154 C ATOM 881 CG ASN A 124 39.841 -7.042 34.849 1.00 24.52 C ANISOU 881 CG ASN C 124 2891 3114 3310 -130 540 -42 C ATOM 882 OD1 ASN A 124 39.527 -7.701 35.830 1.00 25.79 O ANISOU 882 OD1 ASN C 124 2941 3614 3245 -172 1181 -65 O ATOM 883 ND2 ASN A 124 41.000 -7.175 34.240 1.00 27.99 N ANISOU 883 ND2 ASN C 124 3441 3601 3590 -11 290 -4 N ATOM 884 N PRO A 125 36.793 -7.023 36.897 1.00 29.88 N ANISOU 884 N PRO C 125 3913 3795 3644 -88 156 -53 N ATOM 885 CA PRO A 125 36.492 -6.771 38.314 1.00 31.09 C ANISOU 885 CA PRO C 125 4011 3994 3808 0 146 15 C ATOM 886 C PRO A 125 37.744 -6.477 39.109 1.00 33.90 C ANISOU 886 C PRO C 125 4316 4418 4143 62 160 74 C ATOM 887 O PRO A 125 37.640 -5.843 40.152 1.00 35.88 O ANISOU 887 O PRO C 125 4561 4737 4335 133 128 254 O ATOM 888 CB PRO A 125 35.849 -8.079 38.784 1.00 31.73 C ANISOU 888 CB PRO C 125 4165 4031 3857 -4 52 -41 C ATOM 889 CG PRO A 125 36.220 -9.128 37.783 1.00 31.68 C ANISOU 889 CG PRO C 125 4142 4084 3809 -59 104 -23 C ATOM 890 CD PRO A 125 36.623 -8.443 36.514 1.00 30.35 C ANISOU 890 CD PRO C 125 3989 3843 3700 -86 192 -9 C TER 891 PRO C 125 ATOM 983 N PRO A 11 16.204 -13.585 -4.627 1.00 19.51 N ANISOU 983 N PRO D 11 2223 2738 2450 124 488 420 N ATOM 984 CA PRO A 11 15.270 -13.413 -3.523 1.00 19.02 C ANISOU 984 CA PRO D 11 2359 2607 2258 2 249 323 C ATOM 985 C PRO A 11 15.969 -13.082 -2.178 1.00 17.91 C ANISOU 985 C PRO D 11 2290 2504 2008 20 153 619 C ATOM 986 O PRO A 11 15.281 -12.755 -1.228 1.00 18.25 O ANISOU 986 O PRO D 11 2145 2629 2157 49 15 722 O ATOM 987 CB PRO A 11 14.616 -14.801 -3.375 1.00 21.03 C ANISOU 987 CB PRO D 11 2514 2965 2511 -54 251 334 C ATOM 988 CG PRO A 11 15.551 -15.704 -3.915 1.00 22.16 C ANISOU 988 CG PRO D 11 2701 2795 2924 -29 226 371 C ATOM 989 CD PRO A 11 16.287 -14.996 -5.018 1.00 21.32 C ANISOU 989 CD PRO D 11 2770 2752 2575 74 231 442 C ATOM 990 N LEU A 12 17.287 -13.254 -2.095 1.00 16.39 N ANISOU 990 N LEU D 12 2258 2285 1683 12 162 627 N ATOM 991 CA LEU A 12 18.059 -13.072 -0.844 1.00 16.62 C ANISOU 991 CA LEU D 12 2257 2229 1827 -26 171 394 C ATOM 992 C LEU A 12 19.338 -12.333 -1.130 1.00 17.31 C ANISOU 992 C LEU D 12 2352 2410 1814 -71 46 426 C ATOM 993 O LEU A 12 20.123 -12.770 -1.975 1.00 19.30 O ANISOU 993 O LEU D 12 2572 2773 1987 -4 -154 813 O ATOM 994 CB LEU A 12 18.398 -14.419 -0.217 1.00 17.00 C ANISOU 994 CB LEU D 12 2209 2345 1902 -6 215 404 C ATOM 995 CG LEU A 12 19.182 -14.392 1.095 1.00 16.94 C ANISOU 995 CG LEU D 12 2302 2243 1890 53 179 382 C ATOM 996 CD1 LEU A 12 18.353 -13.710 2.176 1.00 16.97 C ANISOU 996 CD1 LEU D 12 2516 2340 1592 287 -37 213 C ATOM 997 CD2 LEU A 12 19.584 -15.846 1.508 1.00 18.31 C ANISOU 997 CD2 LEU D 12 2497 2073 2385 121 213 238 C ATOM 998 N MET A 13 19.538 -11.202 -0.436 1.00 15.76 N ANISOU 998 N MET D 13 2309 2269 1408 0 174 366 N ATOM 999 CA AMET A 13 20.715 -10.366 -0.550 0.50 15.40 C ANISOU 999 CA AMET D 13 2199 2189 1460 -14 85 267 C ATOM 1000 C MET A 13 21.227 -10.120 0.874 1.00 13.93 C ANISOU 1000 C MET D 13 1944 2042 1303 13 119 237 C ATOM 1001 O MET A 13 20.411 -9.946 1.776 1.00 14.76 O ANISOU 1001 O MET D 13 2032 2299 1274 156 139 382 O ATOM 1002 CB AMET A 13 20.342 -9.010 -1.183 0.50 15.29 C ANISOU 1002 CB AMET D 13 2199 2270 1339 -60 162 191 C ATOM 1003 CG AMET A 13 21.568 -8.206 -1.675 0.50 17.29 C ANISOU 1003 CG AMET D 13 2453 2223 1894 3 176 133 C ATOM 1004 SD AMET A 13 22.318 -7.067 -0.492 0.50 17.20 S ANISOU 1004 SD AMET D 13 2337 2381 1814 -188 154 134 S ATOM 1005 CE AMET A 13 21.603 -5.525 -1.022 0.50 19.02 C ANISOU 1005 CE AMET D 13 2388 2435 2400 0 -4 -121 C ATOM 1006 N VAL A 14 22.528 -10.087 1.056 1.00 12.52 N ANISOU 1006 N VAL D 14 1851 1955 948 -31 55 127 N ATOM 1007 CA VAL A 14 23.113 -9.751 2.359 1.00 12.71 C ANISOU 1007 CA VAL D 14 1829 1945 1055 15 4 259 C ATOM 1008 C VAL A 14 24.012 -8.543 2.159 1.00 14.65 C ANISOU 1008 C VAL D 14 2097 2169 1300 -118 -163 111 C ATOM 1009 O VAL A 14 24.797 -8.480 1.212 1.00 15.89 O ANISOU 1009 O VAL D 14 2229 2481 1326 -324 -293 434 O ATOM 1010 CB VAL A 14 23.941 -10.944 2.950 1.00 12.99 C ANISOU 1010 CB VAL D 14 1804 1935 1195 232 -39 159 C ATOM 1011 CG1 VAL A 14 24.640 -10.567 4.256 1.00 14.46 C ANISOU 1011 CG1 VAL D 14 2103 2106 1285 215 169 101 C ATOM 1012 CG2 VAL A 14 23.046 -12.150 3.092 1.00 14.01 C ANISOU 1012 CG2 VAL D 14 2128 1749 1445 130 -50 166 C ATOM 1013 N LYS A 15 23.895 -7.574 3.046 1.00 13.18 N ANISOU 1013 N LYS D 15 1927 2038 1041 -25 -180 238 N ATOM 1014 CA LYS A 15 24.615 -6.325 2.980 1.00 14.34 C ANISOU 1014 CA LYS D 15 2026 2127 1294 -60 -49 114 C ATOM 1015 C LYS A 15 25.275 -6.071 4.302 1.00 12.53 C ANISOU 1015 C LYS D 15 1774 1829 1157 -254 5 144 C ATOM 1016 O LYS A 15 24.595 -6.176 5.337 1.00 13.15 O ANISOU 1016 O LYS D 15 1730 2318 948 -212 -147 119 O ATOM 1017 CB LYS A 15 23.701 -5.124 2.641 1.00 16.26 C ANISOU 1017 CB LYS D 15 2420 2258 1498 -95 126 131 C ATOM 1018 CG LYS A 15 24.506 -3.810 2.528 1.00 19.48 C ANISOU 1018 CG LYS D 15 2702 2499 2199 -66 27 -3 C ATOM 1019 CD LYS A 15 23.852 -2.690 1.682 1.00 23.37 C ANISOU 1019 CD LYS D 15 3137 2900 2840 -41 178 -50 C ATOM 1020 CE LYS A 15 24.850 -1.548 1.329 1.00 24.60 C ANISOU 1020 CE LYS D 15 3221 3089 3037 13 -25 -171 C ATOM 1021 NZ LYS A 15 25.840 -1.701 0.158 1.00 29.61 N ANISOU 1021 NZ LYS D 15 3671 3848 3730 95 -259 123 N ATOM 1022 N VAL A 16 26.554 -5.741 4.314 1.00 11.86 N ANISOU 1022 N VAL D 16 1807 1755 943 -194 -82 56 N ATOM 1023 CA VAL A 16 27.322 -5.566 5.564 1.00 12.09 C ANISOU 1023 CA VAL D 16 1824 1715 1051 -128 -34 -10 C ATOM 1024 C VAL A 16 28.060 -4.245 5.555 1.00 11.85 C ANISOU 1024 C VAL D 16 1911 1485 1103 -85 -127 -28 C ATOM 1025 O VAL A 16 28.795 -3.916 4.579 1.00 12.80 O ANISOU 1025 O VAL D 16 2031 1852 980 -189 -236 -64 O ATOM 1026 CB VAL A 16 28.320 -6.740 5.829 1.00 13.25 C ANISOU 1026 CB VAL D 16 1959 1840 1233 -101 -1 9 C ATOM 1027 CG1 VAL A 16 28.910 -6.693 7.248 1.00 12.98 C ANISOU 1027 CG1 VAL D 16 1846 2103 981 -12 237 -58 C ATOM 1028 CG2 VAL A 16 27.641 -8.115 5.597 1.00 13.50 C ANISOU 1028 CG2 VAL D 16 1849 1834 1443 -256 92 63 C ATOM 1029 N LEU A 17 27.909 -3.474 6.630 1.00 11.22 N ANISOU 1029 N LEU D 17 1536 1638 1085 -34 -100 16 N ATOM 1030 CA LEU A 17 28.526 -2.192 6.767 1.00 10.78 C ANISOU 1030 CA LEU D 17 1524 1475 1095 31 0 -182 C ATOM 1031 C LEU A 17 29.423 -2.136 8.001 1.00 10.50 C ANISOU 1031 C LEU D 17 1377 1485 1125 95 -143 3 C ATOM 1032 O LEU A 17 29.172 -2.858 8.974 1.00 11.50 O ANISOU 1032 O LEU D 17 1626 1596 1145 -151 -129 -125 O ATOM 1033 CB LEU A 17 27.471 -1.108 6.884 1.00 12.45 C ANISOU 1033 CB LEU D 17 1725 1577 1427 -61 165 -45 C ATOM 1034 CG LEU A 17 26.540 -0.871 5.677 1.00 13.61 C ANISOU 1034 CG LEU D 17 1767 1870 1531 -29 339 -261 C ATOM 1035 CD1 LEU A 17 25.549 0.223 5.997 1.00 17.10 C ANISOU 1035 CD1 LEU D 17 2164 2355 1977 322 301 -396 C ATOM 1036 CD2 LEU A 17 27.302 -0.531 4.392 1.00 17.18 C ANISOU 1036 CD2 LEU D 17 2193 2711 1620 185 247 -703 C ATOM 1037 N ASP A 18 30.420 -1.256 7.951 1.00 10.55 N ANISOU 1037 N ASP D 18 1470 1445 1091 -1 -80 -101 N ATOM 1038 CA ASP A 18 31.419 -1.085 9.009 1.00 10.40 C ANISOU 1038 CA ASP D 18 1417 1307 1225 9 -58 -220 C ATOM 1039 C ASP A 18 31.200 0.287 9.644 1.00 9.63 C ANISOU 1039 C ASP D 18 1310 1296 1052 -12 -95 -94 C ATOM 1040 O ASP A 18 31.334 1.333 9.001 1.00 10.39 O ANISOU 1040 O ASP D 18 1554 1301 1093 -58 -210 -178 O ATOM 1041 CB ASP A 18 32.793 -1.224 8.383 1.00 10.57 C ANISOU 1041 CB ASP D 18 1468 1264 1282 23 -154 -195 C ATOM 1042 CG ASP A 18 33.959 -0.918 9.302 1.00 12.24 C ANISOU 1042 CG ASP D 18 1645 1474 1531 61 -102 -209 C ATOM 1043 OD1 ASP A 18 33.813 -0.168 10.281 1.00 11.90 O ANISOU 1043 OD1 ASP D 18 1498 1591 1432 -19 159 -126 O ATOM 1044 OD2 ASP A 18 35.053 -1.455 8.972 1.00 15.26 O ANISOU 1044 OD2 ASP D 18 1551 2153 2093 197 -164 173 O ATOM 1045 N ALA A 19 30.751 0.260 10.904 1.00 10.01 N ANISOU 1045 N ALA D 19 1631 1226 945 71 -67 -223 N ATOM 1046 CA ALA A 19 30.405 1.441 11.676 1.00 10.10 C ANISOU 1046 CA ALA D 19 1520 1236 1079 157 -64 -287 C ATOM 1047 C ALA A 19 31.595 2.217 12.219 1.00 11.36 C ANISOU 1047 C ALA D 19 1825 1322 1168 -39 -219 -220 C ATOM 1048 O ALA A 19 31.425 3.343 12.689 1.00 12.16 O ANISOU 1048 O ALA D 19 1942 1410 1268 -77 -342 -161 O ATOM 1049 CB ALA A 19 29.526 1.030 12.818 1.00 11.00 C ANISOU 1049 CB ALA D 19 1599 1598 981 37 -207 -221 C ATOM 1050 N VAL A 20 32.790 1.619 12.178 1.00 11.61 N ANISOU 1050 N VAL D 20 1703 1380 1327 -122 37 -149 N ATOM 1051 CA VAL A 20 34.027 2.221 12.641 1.00 12.77 C ANISOU 1051 CA VAL D 20 1717 1580 1552 -216 -4 -279 C ATOM 1052 C VAL A 20 34.623 3.112 11.565 1.00 13.33 C ANISOU 1052 C VAL D 20 1734 1507 1823 -239 -84 -178 C ATOM 1053 O VAL A 20 35.076 4.208 11.839 1.00 16.45 O ANISOU 1053 O VAL D 20 2522 1717 2008 -383 -171 -280 O ATOM 1054 CB VAL A 20 35.038 1.154 13.113 1.00 13.48 C ANISOU 1054 CB VAL D 20 1685 1552 1882 -225 -1 -214 C ATOM 1055 CG1 VAL A 20 36.390 1.751 13.445 1.00 16.64 C ANISOU 1055 CG1 VAL D 20 1676 2281 2363 -364 293 -602 C ATOM 1056 CG2 VAL A 20 34.519 0.432 14.328 1.00 14.78 C ANISOU 1056 CG2 VAL D 20 2105 1836 1674 -318 140 -371 C ATOM 1057 N ARG A 21 34.645 2.590 10.361 1.00 13.74 N ANISOU 1057 N ARG D 21 1855 1779 1586 -234 -172 -420 N ATOM 1058 CA ARG A 21 35.234 3.317 9.226 1.00 15.17 C ANISOU 1058 CA ARG D 21 2041 1919 1804 -161 -247 -308 C ATOM 1059 C ARG A 21 34.230 3.989 8.337 1.00 14.59 C ANISOU 1059 C ARG D 21 2128 1816 1596 -89 -312 -212 C ATOM 1060 O ARG A 21 34.603 4.801 7.470 1.00 16.23 O ANISOU 1060 O ARG D 21 2482 1988 1694 -161 -371 -426 O ATOM 1061 CB ARG A 21 36.056 2.349 8.410 1.00 16.06 C ANISOU 1061 CB ARG D 21 2076 1982 2042 -64 -218 -455 C ATOM 1062 CG ARG A 21 37.146 1.705 9.344 1.00 21.23 C ANISOU 1062 CG ARG D 21 2445 2804 2816 95 45 -144 C ATOM 1063 CD ARG A 21 38.207 1.055 8.612 1.00 23.72 C ANISOU 1063 CD ARG D 21 2913 3038 3059 -2 -91 -88 C ATOM 1064 NE ARG A 21 37.674 -0.094 7.922 1.00 26.42 N ANISOU 1064 NE ARG D 21 3317 3093 3626 127 -129 201 N ATOM 1065 CZ ARG A 21 38.294 -0.694 6.922 1.00 29.11 C ANISOU 1065 CZ ARG D 21 3543 3808 3709 -43 -225 95 C ATOM 1066 NH1 ARG A 21 39.477 -0.244 6.479 1.00 28.24 N ANISOU 1066 NH1 ARG D 21 3246 3617 3865 -189 -147 -178 N ATOM 1067 NH2 ARG A 21 37.710 -1.733 6.360 1.00 29.43 N ANISOU 1067 NH2 ARG D 21 3748 3715 3719 17 -186 145 N ATOM 1068 N GLY A 22 32.951 3.679 8.522 1.00 13.01 N ANISOU 1068 N GLY D 22 1998 1431 1513 160 -383 -115 N ATOM 1069 CA GLY A 22 31.949 4.336 7.689 1.00 13.08 C ANISOU 1069 CA GLY D 22 1959 1547 1465 106 -210 -107 C ATOM 1070 C GLY A 22 32.045 3.869 6.236 1.00 12.56 C ANISOU 1070 C GLY D 22 2040 1418 1312 122 -289 -249 C ATOM 1071 O GLY A 22 32.081 4.650 5.272 1.00 13.91 O ANISOU 1071 O GLY D 22 2330 1584 1371 373 -379 -259 O ATOM 1072 N SER A 23 32.079 2.543 6.079 1.00 12.95 N ANISOU 1072 N SER D 23 2241 1392 1287 82 -249 -133 N ATOM 1073 CA SER A 23 32.339 1.954 4.770 1.00 13.79 C ANISOU 1073 CA SER D 23 2151 1716 1370 89 -249 -74 C ATOM 1074 C SER A 23 31.574 0.670 4.628 1.00 13.24 C ANISOU 1074 C SER D 23 2141 1623 1265 61 -288 67 C ATOM 1075 O SER A 23 31.180 0.060 5.617 1.00 14.41 O ANISOU 1075 O SER D 23 2310 1840 1323 -109 -438 -160 O ATOM 1076 CB SER A 23 33.824 1.662 4.639 1.00 16.12 C ANISOU 1076 CB SER D 23 2447 2012 1666 178 -384 -78 C ATOM 1077 OG SER A 23 34.166 0.562 5.468 1.00 19.24 O ANISOU 1077 OG SER D 23 2674 2414 2221 305 -370 -88 O ATOM 1078 N PRO A 24 31.426 0.185 3.410 1.00 12.93 N ANISOU 1078 N PRO D 24 2107 1606 1197 156 -245 -226 N ATOM 1079 CA PRO A 24 31.026 -1.208 3.262 1.00 14.23 C ANISOU 1079 CA PRO D 24 2114 1865 1425 -49 -70 -66 C ATOM 1080 C PRO A 24 32.041 -2.100 3.957 1.00 13.45 C ANISOU 1080 C PRO D 24 2033 1593 1483 1 -92 -18 C ATOM 1081 O PRO A 24 33.204 -1.744 4.042 1.00 14.35 O ANISOU 1081 O PRO D 24 2103 1693 1656 -60 -143 -259 O ATOM 1082 CB PRO A 24 31.092 -1.429 1.744 1.00 14.74 C ANISOU 1082 CB PRO D 24 2202 1902 1494 22 -12 88 C ATOM 1083 CG PRO A 24 31.007 -0.017 1.181 1.00 18.97 C ANISOU 1083 CG PRO D 24 2923 2489 1793 -156 71 -160 C ATOM 1084 CD PRO A 24 31.664 0.869 2.129 1.00 13.25 C ANISOU 1084 CD PRO D 24 2456 1557 1021 278 -326 -28 C ATOM 1085 N ALA A 25 31.601 -3.259 4.425 1.00 12.65 N ANISOU 1085 N ALA D 25 1879 1492 1432 -119 -87 -14 N ATOM 1086 CA ALA A 25 32.502 -4.279 4.950 1.00 13.20 C ANISOU 1086 CA ALA D 25 2018 1536 1459 -28 -105 0 C ATOM 1087 C ALA A 25 32.771 -5.263 3.818 1.00 12.86 C ANISOU 1087 C ALA D 25 1887 1524 1475 -67 -153 -1 C ATOM 1088 O ALA A 25 31.892 -6.018 3.437 1.00 12.97 O ANISOU 1088 O ALA D 25 1933 1495 1500 -55 -286 109 O ATOM 1089 CB ALA A 25 31.879 -4.999 6.160 1.00 13.12 C ANISOU 1089 CB ALA D 25 1999 1679 1304 -134 -67 -32 C ATOM 1090 N ILE A 26 33.986 -5.183 3.280 1.00 13.40 N ANISOU 1090 N ILE D 26 1968 1656 1468 -88 -149 127 N ATOM 1091 CA ILE A 26 34.379 -5.887 2.070 1.00 14.82 C ANISOU 1091 CA ILE D 26 2042 1906 1683 -88 -285 23 C ATOM 1092 C ILE A 26 35.055 -7.196 2.415 1.00 14.99 C ANISOU 1092 C ILE D 26 1993 1965 1737 -45 -336 90 C ATOM 1093 O ILE A 26 35.787 -7.307 3.382 1.00 14.77 O ANISOU 1093 O ILE D 26 1901 1943 1768 12 -363 144 O ATOM 1094 CB ILE A 26 35.333 -4.977 1.199 1.00 16.60 C ANISOU 1094 CB ILE D 26 2494 1987 1822 -222 -358 -132 C ATOM 1095 CG1 ILE A 26 34.649 -3.642 0.930 1.00 17.05 C ANISOU 1095 CG1 ILE D 26 2385 2273 1817 -218 -319 -300 C ATOM 1096 CG2 ILE A 26 35.727 -5.639 -0.087 1.00 18.69 C ANISOU 1096 CG2 ILE D 26 2582 2417 2103 71 -300 -44 C ATOM 1097 CD1 ILE A 26 35.566 -2.547 0.348 1.00 20.34 C ANISOU 1097 CD1 ILE D 26 2938 2529 2259 -347 -279 -253 C ATOM 1098 N ASN A 27 34.817 -8.199 1.558 1.00 14.15 N ANISOU 1098 N ASN D 27 1727 1874 1772 -163 -209 147 N ATOM 1099 CA AASN A 27 35.450 -9.493 1.678 0.50 14.98 C ANISOU 1099 CA AASN D 27 1835 1905 1948 -97 -165 83 C ATOM 1100 C ASN A 27 35.137 -10.205 2.996 1.00 15.09 C ANISOU 1100 C ASN D 27 1842 1872 2018 -106 56 38 C ATOM 1101 O ASN A 27 35.969 -10.937 3.535 1.00 17.98 O ANISOU 1101 O ASN D 27 1984 2229 2615 29 -43 -182 O ATOM 1102 CB AASN A 27 36.966 -9.352 1.455 0.50 15.62 C ANISOU 1102 CB AASN D 27 1873 1960 2099 -48 -245 212 C ATOM 1103 CG AASN A 27 37.623 -10.661 1.095 0.50 16.54 C ANISOU 1103 CG AASN D 27 2028 1968 2285 0 -187 289 C ATOM 1104 OD1AASN A 27 37.040 -11.498 0.401 0.50 21.71 O ANISOU 1104 OD1AASN D 27 2377 2628 3242 73 -91 339 O ATOM 1105 ND2AASN A 27 38.825 -10.861 1.630 0.50 20.31 N ANISOU 1105 ND2AASN D 27 2183 2394 3138 -90 -126 283 N ATOM 1106 N VAL A 28 33.908 -10.011 3.471 1.00 13.40 N ANISOU 1106 N VAL D 28 1632 1692 1765 -114 -31 1 N ATOM 1107 CA VAL A 28 33.388 -10.698 4.639 1.00 13.83 C ANISOU 1107 CA VAL D 28 1746 1728 1779 -142 -11 55 C ATOM 1108 C VAL A 28 32.773 -12.026 4.182 1.00 13.34 C ANISOU 1108 C VAL D 28 1651 1691 1726 -72 -89 125 C ATOM 1109 O VAL A 28 31.901 -12.041 3.319 1.00 12.86 O ANISOU 1109 O VAL D 28 1838 1484 1564 -34 -42 122 O ATOM 1110 CB VAL A 28 32.327 -9.849 5.398 1.00 14.30 C ANISOU 1110 CB VAL D 28 2112 1600 1720 -126 -16 47 C ATOM 1111 CG1 VAL A 28 31.789 -10.620 6.612 1.00 16.49 C ANISOU 1111 CG1 VAL D 28 2611 1777 1877 -143 -313 -227 C ATOM 1112 CG2 VAL A 28 32.952 -8.564 5.877 1.00 15.50 C ANISOU 1112 CG2 VAL D 28 2495 1578 1814 -346 155 173 C ATOM 1113 N ALA A 29 33.166 -13.115 4.808 1.00 12.96 N ANISOU 1113 N ALA D 29 1620 1640 1662 -26 184 245 N ATOM 1114 CA ALA A 29 32.560 -14.432 4.490 1.00 12.64 C ANISOU 1114 CA ALA D 29 1606 1553 1642 -18 25 177 C ATOM 1115 C ALA A 29 31.187 -14.540 5.121 1.00 11.77 C ANISOU 1115 C ALA D 29 1523 1529 1419 -22 56 172 C ATOM 1116 O ALA A 29 30.962 -14.113 6.253 1.00 11.68 O ANISOU 1116 O ALA D 29 1549 1660 1228 -119 39 266 O ATOM 1117 CB ALA A 29 33.416 -15.608 4.957 1.00 13.60 C ANISOU 1117 CB ALA D 29 1796 1486 1885 163 166 142 C ATOM 1118 N VAL A 30 30.254 -15.040 4.327 1.00 11.38 N ANISOU 1118 N VAL D 30 1485 1514 1322 -78 9 361 N ATOM 1119 CA VAL A 30 28.884 -15.199 4.697 1.00 11.50 C ANISOU 1119 CA VAL D 30 1438 1596 1333 -77 24 257 C ATOM 1120 C VAL A 30 28.460 -16.620 4.278 1.00 10.56 C ANISOU 1120 C VAL D 30 1338 1590 1084 -26 -76 350 C ATOM 1121 O VAL A 30 28.643 -17.043 3.127 1.00 12.98 O ANISOU 1121 O VAL D 30 1574 1955 1404 -151 -156 445 O ATOM 1122 CB VAL A 30 27.986 -14.165 3.995 1.00 11.82 C ANISOU 1122 CB VAL D 30 1439 1826 1225 109 -126 316 C ATOM 1123 CG1 VAL A 30 26.497 -14.454 4.340 1.00 14.11 C ANISOU 1123 CG1 VAL D 30 1236 2032 2092 71 72 162 C ATOM 1124 CG2 VAL A 30 28.384 -12.745 4.336 1.00 13.12 C ANISOU 1124 CG2 VAL D 30 1738 1415 1829 -130 -70 -89 C ATOM 1125 N HIS A 31 27.871 -17.325 5.276 1.00 11.71 N ANISOU 1125 N HIS D 31 1434 1652 1361 -125 57 275 N ATOM 1126 CA HIS A 31 27.317 -18.656 5.037 1.00 12.00 C ANISOU 1126 CA HIS D 31 1459 1656 1443 -68 -184 398 C ATOM 1127 C HIS A 31 25.851 -18.693 5.410 1.00 10.53 C ANISOU 1127 C HIS D 31 1296 1455 1247 -99 -242 667 C ATOM 1128 O HIS A 31 25.458 -18.210 6.478 1.00 14.81 O ANISOU 1128 O HIS D 31 1631 2243 1752 -299 -198 675 O ATOM 1129 CB HIS A 31 28.040 -19.722 5.854 1.00 14.46 C ANISOU 1129 CB HIS D 31 1730 1904 1859 -2 -201 303 C ATOM 1130 CG HIS A 31 29.490 -19.883 5.501 1.00 16.79 C ANISOU 1130 CG HIS D 31 2039 1933 2406 189 -173 -45 C ATOM 1131 ND1 HIS A 31 29.974 -21.000 4.847 1.00 20.86 N ANISOU 1131 ND1 HIS D 31 2316 2367 3243 422 -633 100 N ATOM 1132 CD2 HIS A 31 30.555 -19.067 5.698 1.00 18.91 C ANISOU 1132 CD2 HIS D 31 2220 2065 2899 74 -248 -136 C ATOM 1133 CE1 HIS A 31 31.280 -20.846 4.632 1.00 20.61 C ANISOU 1133 CE1 HIS D 31 2232 2460 3137 456 -402 64 C ATOM 1134 NE2 HIS A 31 31.668 -19.706 5.176 1.00 20.79 N ANISOU 1134 NE2 HIS D 31 2471 2418 3009 362 -268 -94 N ATOM 1135 N VAL A 32 25.092 -19.281 4.478 1.00 11.80 N ANISOU 1135 N VAL D 32 1413 1585 1485 -108 -92 546 N ATOM 1136 CA VAL A 32 23.674 -19.451 4.658 1.00 12.17 C ANISOU 1136 CA VAL D 32 1508 1478 1636 36 -93 503 C ATOM 1137 C VAL A 32 23.402 -20.928 4.833 1.00 11.86 C ANISOU 1137 C VAL D 32 1600 1409 1494 178 -122 341 C ATOM 1138 O VAL A 32 24.018 -21.763 4.126 1.00 13.14 O ANISOU 1138 O VAL D 32 1718 1538 1737 81 -231 669 O ATOM 1139 CB VAL A 32 22.829 -18.892 3.492 1.00 11.60 C ANISOU 1139 CB VAL D 32 1446 1500 1458 51 -72 470 C ATOM 1140 CG1 VAL A 32 21.341 -18.982 3.799 1.00 13.65 C ANISOU 1140 CG1 VAL D 32 1251 1921 2014 125 -157 295 C ATOM 1141 CG2 VAL A 32 23.235 -17.459 3.173 1.00 13.93 C ANISOU 1141 CG2 VAL D 32 1787 1691 1815 -23 -60 250 C ATOM 1142 N PHE A 33 22.566 -21.258 5.787 1.00 12.27 N ANISOU 1142 N PHE D 33 1549 1411 1700 34 -240 439 N ATOM 1143 CA PHE A 33 22.146 -22.610 6.108 1.00 13.45 C ANISOU 1143 CA PHE D 33 1767 1559 1785 114 -213 357 C ATOM 1144 C PHE A 33 20.611 -22.670 6.079 1.00 13.62 C ANISOU 1144 C PHE D 33 1752 1588 1832 -75 -142 329 C ATOM 1145 O PHE A 33 19.930 -21.674 6.381 1.00 12.66 O ANISOU 1145 O PHE D 33 1505 1681 1622 121 -139 525 O ATOM 1146 CB PHE A 33 22.636 -23.023 7.491 1.00 14.20 C ANISOU 1146 CB PHE D 33 1856 1493 2044 -21 -172 247 C ATOM 1147 CG PHE A 33 24.120 -22.903 7.680 1.00 14.80 C ANISOU 1147 CG PHE D 33 1838 1646 2139 50 -156 -42 C ATOM 1148 CD1 PHE A 33 24.696 -21.706 8.090 1.00 14.56 C ANISOU 1148 CD1 PHE D 33 1636 1714 2182 31 140 -168 C ATOM 1149 CD2 PHE A 33 24.943 -23.980 7.444 1.00 17.00 C ANISOU 1149 CD2 PHE D 33 2014 1853 2592 -68 -226 13 C ATOM 1150 CE1 PHE A 33 26.071 -21.549 8.232 1.00 15.29 C ANISOU 1150 CE1 PHE D 33 1782 1944 2084 0 142 -110 C ATOM 1151 CE2 PHE A 33 26.307 -23.842 7.579 1.00 17.87 C ANISOU 1151 CE2 PHE D 33 2004 2085 2699 247 -261 236 C ATOM 1152 CZ PHE A 33 26.877 -22.655 7.974 1.00 16.56 C ANISOU 1152 CZ PHE D 33 1813 2089 2387 56 -97 52 C ATOM 1153 N ARG A 34 20.077 -23.856 5.781 1.00 15.40 N ANISOU 1153 N ARG D 34 2006 1661 2182 -12 -190 414 N ATOM 1154 CA AARG A 34 18.656 -24.141 5.863 0.50 16.23 C ANISOU 1154 CA AARG D 34 2097 1891 2176 -23 -72 266 C ATOM 1155 C ARG A 34 18.459 -25.189 6.949 1.00 16.09 C ANISOU 1155 C ARG D 34 2111 1728 2274 -75 -17 307 C ATOM 1156 O ARG A 34 19.209 -26.171 7.004 1.00 17.50 O ANISOU 1156 O ARG D 34 2191 1788 2670 89 -309 24 O ATOM 1157 CB AARG A 34 18.135 -24.654 4.498 0.50 17.23 C ANISOU 1157 CB AARG D 34 2345 2032 2166 -69 -72 306 C ATOM 1158 CG AARG A 34 16.632 -24.870 4.445 0.50 17.97 C ANISOU 1158 CG AARG D 34 2286 2229 2311 -55 -29 197 C ATOM 1159 CD AARG A 34 15.942 -25.007 3.048 0.50 20.25 C ANISOU 1159 CD AARG D 34 2654 2510 2528 -29 -21 241 C ATOM 1160 NE AARG A 34 14.477 -25.002 3.246 0.50 22.63 N ANISOU 1160 NE AARG D 34 2831 2898 2869 -176 254 229 N ATOM 1161 CZ AARG A 34 13.745 -26.080 3.537 0.50 24.15 C ANISOU 1161 CZ AARG D 34 3009 3003 3163 -83 87 -18 C ATOM 1162 NH1AARG A 34 14.275 -27.298 3.556 0.50 24.09 N ANISOU 1162 NH1AARG D 34 2921 3000 3230 80 175 -34 N ATOM 1163 NH2AARG A 34 12.442 -25.963 3.724 0.50 23.40 N ANISOU 1163 NH2AARG D 34 2832 2759 3300 120 -9 55 N ATOM 1164 N LYS A 35 17.434 -25.031 7.778 1.00 17.04 N ANISOU 1164 N LYS D 35 2200 1951 2321 -1 -120 193 N ATOM 1165 CA LYS A 35 17.176 -26.003 8.831 1.00 19.32 C ANISOU 1165 CA LYS D 35 2507 2287 2546 -89 -47 148 C ATOM 1166 C LYS A 35 16.540 -27.256 8.230 1.00 19.54 C ANISOU 1166 C LYS D 35 2546 2205 2671 -145 49 147 C ATOM 1167 O LYS A 35 15.527 -27.160 7.525 1.00 19.33 O ANISOU 1167 O LYS D 35 2590 1932 2820 -219 189 165 O ATOM 1168 CB LYS A 35 16.272 -25.399 9.912 1.00 19.68 C ANISOU 1168 CB LYS D 35 2393 2495 2588 3 -183 124 C ATOM 1169 CG LYS A 35 16.380 -26.136 11.239 1.00 23.47 C ANISOU 1169 CG LYS D 35 3081 2860 2977 -4 -139 -6 C ATOM 1170 CD LYS A 35 15.407 -25.608 12.260 1.00 25.13 C ANISOU 1170 CD LYS D 35 3111 3224 3213 -49 -174 -38 C ATOM 1171 CE LYS A 35 16.016 -25.436 13.620 1.00 30.54 C ANISOU 1171 CE LYS D 35 3923 3921 3760 100 -97 -31 C ATOM 1172 NZ LYS A 35 14.986 -24.877 14.537 1.00 30.60 N ANISOU 1172 NZ LYS D 35 4220 3921 3483 178 -189 140 N ATOM 1173 N ALA A 36 17.169 -28.402 8.469 1.00 20.46 N ANISOU 1173 N ALA D 36 2687 2321 2762 -260 279 208 N ATOM 1174 CA ALA A 36 16.705 -29.694 7.962 1.00 23.21 C ANISOU 1174 CA ALA D 36 3088 2654 3078 -191 132 79 C ATOM 1175 C ALA A 36 15.650 -30.251 8.887 1.00 24.41 C ANISOU 1175 C ALA D 36 3245 2859 3170 -184 96 28 C ATOM 1176 O ALA A 36 15.483 -29.780 10.026 1.00 24.53 O ANISOU 1176 O ALA D 36 3244 2996 3078 -495 76 -227 O ATOM 1177 CB ALA A 36 17.888 -30.644 7.899 1.00 24.48 C ANISOU 1177 CB ALA D 36 3250 2717 3332 -101 118 -23 C ATOM 1178 N ALA A 37 14.972 -31.300 8.404 1.00 26.62 N ANISOU 1178 N ALA D 37 3501 3163 3450 -267 151 2 N ATOM 1179 CA ALA A 37 13.901 -31.924 9.194 1.00 28.10 C ANISOU 1179 CA ALA D 37 3744 3376 3554 -229 98 -30 C ATOM 1180 C ALA A 37 14.347 -32.454 10.553 1.00 29.91 C ANISOU 1180 C ALA D 37 4000 3634 3730 -184 69 -80 C ATOM 1181 O ALA A 37 13.557 -32.407 11.486 1.00 31.79 O ANISOU 1181 O ALA D 37 4251 3784 4043 -292 0 -161 O ATOM 1182 CB ALA A 37 13.259 -33.061 8.432 1.00 29.49 C ANISOU 1182 CB ALA D 37 3975 3408 3821 -300 119 25 C ATOM 1183 N ASP A 38 15.590 -32.940 10.627 1.00 30.39 N ANISOU 1183 N ASP D 38 4082 3682 3782 -158 113 -130 N ATOM 1184 CA ASP A 38 16.223 -33.370 11.889 1.00 30.89 C ANISOU 1184 CA ASP D 38 4097 3779 3859 -134 138 -86 C ATOM 1185 C ASP A 38 16.772 -32.231 12.746 1.00 31.45 C ANISOU 1185 C ASP D 38 4180 3819 3950 -110 186 -71 C ATOM 1186 O ASP A 38 17.432 -32.492 13.752 1.00 31.84 O ANISOU 1186 O ASP D 38 4320 3881 3897 -159 288 -241 O ATOM 1187 CB ASP A 38 17.341 -34.383 11.632 1.00 31.77 C ANISOU 1187 CB ASP D 38 4239 3838 3993 -119 79 -84 C ATOM 1188 CG ASP A 38 18.528 -33.818 10.856 1.00 34.29 C ANISOU 1188 CG ASP D 38 4379 4067 4580 -66 71 -72 C ATOM 1189 OD1 ASP A 38 18.598 -32.597 10.560 1.00 33.27 O ANISOU 1189 OD1 ASP D 38 4440 3691 4510 99 407 -44 O ATOM 1190 OD2 ASP A 38 19.422 -34.639 10.532 1.00 37.17 O ANISOU 1190 OD2 ASP D 38 4960 4015 5147 147 35 112 O ATOM 1191 N ASP A 39 16.490 -30.985 12.369 1.00 30.32 N ANISOU 1191 N ASP D 39 4017 3745 3756 -125 172 -126 N ATOM 1192 CA ASP A 39 16.883 -29.800 13.159 1.00 30.50 C ANISOU 1192 CA ASP D 39 4021 3817 3749 -36 94 -75 C ATOM 1193 C ASP A 39 18.358 -29.424 13.067 1.00 29.57 C ANISOU 1193 C ASP D 39 3901 3721 3611 23 127 -53 C ATOM 1194 O ASP A 39 18.796 -28.500 13.758 1.00 32.30 O ANISOU 1194 O ASP D 39 4125 4122 4024 -63 160 59 O ATOM 1195 CB ASP A 39 16.474 -29.915 14.647 1.00 32.06 C ANISOU 1195 CB ASP D 39 4185 4119 3877 -63 -39 -89 C ATOM 1196 CG ASP A 39 15.005 -29.603 14.884 1.00 35.52 C ANISOU 1196 CG ASP D 39 4501 4692 4301 64 -48 -88 C ATOM 1197 OD1 ASP A 39 14.281 -29.183 13.943 1.00 39.34 O ANISOU 1197 OD1 ASP D 39 5020 5148 4779 10 -4 -287 O ATOM 1198 OD2 ASP A 39 14.573 -29.792 16.050 1.00 41.39 O ANISOU 1198 OD2 ASP D 39 5404 5529 4792 35 -189 -217 O ATOM 1199 N THR A 40 19.112 -30.060 12.189 1.00 27.24 N ANISOU 1199 N THR D 40 3618 3295 3436 164 242 -234 N ATOM 1200 CA THR A 40 20.458 -29.612 11.931 1.00 26.69 C ANISOU 1200 CA THR D 40 3570 3168 3402 138 152 -106 C ATOM 1201 C THR A 40 20.462 -28.529 10.844 1.00 24.62 C ANISOU 1201 C THR D 40 3176 2927 3251 181 205 -116 C ATOM 1202 O THR A 40 19.485 -28.358 10.090 1.00 22.72 O ANISOU 1202 O THR D 40 2882 2601 3150 -48 483 -106 O ATOM 1203 CB THR A 40 21.340 -30.778 11.486 1.00 27.40 C ANISOU 1203 CB THR D 40 3626 3245 3538 188 163 -101 C ATOM 1204 OG1 THR A 40 20.870 -31.288 10.231 1.00 27.86 O ANISOU 1204 OG1 THR D 40 4025 2893 3666 460 241 170 O ATOM 1205 CG2 THR A 40 21.312 -31.920 12.543 1.00 28.55 C ANISOU 1205 CG2 THR D 40 3800 3248 3797 229 270 -215 C ATOM 1206 N TRP A 41 21.559 -27.803 10.778 1.00 23.53 N ANISOU 1206 N TRP D 41 3067 2802 3069 242 122 19 N ATOM 1207 CA TRP A 41 21.730 -26.736 9.826 1.00 22.73 C ANISOU 1207 CA TRP D 41 2902 2763 2971 223 30 29 C ATOM 1208 C TRP A 41 22.477 -27.259 8.619 1.00 23.56 C ANISOU 1208 C TRP D 41 2962 2776 3214 263 -43 49 C ATOM 1209 O TRP A 41 23.659 -27.647 8.732 1.00 26.91 O ANISOU 1209 O TRP D 41 3077 3425 3722 358 33 187 O ATOM 1210 CB TRP A 41 22.542 -25.606 10.446 1.00 22.01 C ANISOU 1210 CB TRP D 41 2867 2645 2848 216 16 42 C ATOM 1211 CG TRP A 41 21.789 -24.870 11.477 1.00 20.46 C ANISOU 1211 CG TRP D 41 2710 2694 2368 192 23 9 C ATOM 1212 CD1 TRP A 41 22.044 -24.849 12.805 1.00 22.34 C ANISOU 1212 CD1 TRP D 41 2796 2924 2766 232 192 9 C ATOM 1213 CD2 TRP A 41 20.625 -24.043 11.279 1.00 18.98 C ANISOU 1213 CD2 TRP D 41 2450 2381 2379 78 -53 236 C ATOM 1214 NE1 TRP A 41 21.141 -24.061 13.444 1.00 23.10 N ANISOU 1214 NE1 TRP D 41 2851 3357 2566 256 175 118 N ATOM 1215 CE2 TRP A 41 20.261 -23.539 12.526 1.00 21.14 C ANISOU 1215 CE2 TRP D 41 2661 3025 2345 253 138 82 C ATOM 1216 CE3 TRP A 41 19.890 -23.655 10.162 1.00 17.92 C ANISOU 1216 CE3 TRP D 41 2292 2043 2474 -204 95 182 C ATOM 1217 CZ2 TRP A 41 19.168 -22.675 12.699 1.00 22.54 C ANISOU 1217 CZ2 TRP D 41 2934 2903 2729 251 99 209 C ATOM 1218 CZ3 TRP A 41 18.808 -22.791 10.339 1.00 19.04 C ANISOU 1218 CZ3 TRP D 41 2440 2331 2461 -137 140 254 C ATOM 1219 CH2 TRP A 41 18.450 -22.341 11.594 1.00 20.04 C ANISOU 1219 CH2 TRP D 41 2558 2459 2596 134 38 199 C ATOM 1220 N GLU A 42 21.845 -27.256 7.461 1.00 22.04 N ANISOU 1220 N GLU D 42 2800 2614 2960 291 -227 61 N ATOM 1221 CA GLU A 42 22.565 -27.736 6.288 1.00 23.23 C ANISOU 1221 CA GLU D 42 3043 2680 3101 223 -187 108 C ATOM 1222 C GLU A 42 23.033 -26.599 5.396 1.00 20.80 C ANISOU 1222 C GLU D 42 2597 2294 3012 243 -235 153 C ATOM 1223 O GLU A 42 22.277 -25.632 5.171 1.00 18.68 O ANISOU 1223 O GLU D 42 2464 1796 2836 403 -330 423 O ATOM 1224 CB GLU A 42 21.772 -28.760 5.536 1.00 26.00 C ANISOU 1224 CB GLU D 42 3380 3110 3386 51 -114 143 C ATOM 1225 CG GLU A 42 20.482 -28.313 4.977 1.00 28.55 C ANISOU 1225 CG GLU D 42 3723 3420 3704 38 -7 150 C ATOM 1226 CD GLU A 42 19.896 -29.334 3.989 1.00 30.29 C ANISOU 1226 CD GLU D 42 4095 3589 3823 -24 -1 191 C ATOM 1227 OE1 GLU A 42 19.750 -30.498 4.421 1.00 36.03 O ANISOU 1227 OE1 GLU D 42 4909 3867 4910 -123 -146 66 O ATOM 1228 OE2 GLU A 42 19.574 -28.953 2.824 1.00 34.93 O ANISOU 1228 OE2 GLU D 42 4629 4476 4165 -247 400 178 O ATOM 1229 N PRO A 43 24.288 -26.682 4.922 1.00 20.31 N ANISOU 1229 N PRO D 43 2645 2114 2955 450 -273 247 N ATOM 1230 CA PRO A 43 24.761 -25.655 4.036 1.00 19.02 C ANISOU 1230 CA PRO D 43 2434 2090 2701 351 -233 355 C ATOM 1231 C PRO A 43 23.799 -25.429 2.913 1.00 17.10 C ANISOU 1231 C PRO D 43 2229 1850 2418 284 -266 479 C ATOM 1232 O PRO A 43 23.290 -26.382 2.303 1.00 18.95 O ANISOU 1232 O PRO D 43 2591 1934 2675 168 -95 524 O ATOM 1233 CB PRO A 43 26.075 -26.237 3.539 1.00 19.96 C ANISOU 1233 CB PRO D 43 2523 2233 2825 388 -336 244 C ATOM 1234 CG PRO A 43 26.528 -27.053 4.729 1.00 21.19 C ANISOU 1234 CG PRO D 43 2699 2438 2910 345 -45 211 C ATOM 1235 CD PRO A 43 25.347 -27.685 5.217 1.00 21.98 C ANISOU 1235 CD PRO D 43 2875 2436 3040 446 -201 153 C ATOM 1236 N PHE A 44 23.607 -24.171 2.583 1.00 15.13 N ANISOU 1236 N PHE D 44 1859 1752 2137 96 -243 401 N ATOM 1237 CA PHE A 44 22.686 -23.746 1.562 1.00 13.91 C ANISOU 1237 CA PHE D 44 1763 1752 1767 -35 -156 465 C ATOM 1238 C PHE A 44 23.313 -22.852 0.495 1.00 13.46 C ANISOU 1238 C PHE D 44 1692 1725 1695 -33 -151 543 C ATOM 1239 O PHE A 44 23.124 -23.072 -0.667 1.00 16.17 O ANISOU 1239 O PHE D 44 1986 2209 1949 -173 -62 555 O ATOM 1240 CB PHE A 44 21.464 -23.042 2.249 1.00 13.34 C ANISOU 1240 CB PHE D 44 1505 1820 1742 7 -182 375 C ATOM 1241 CG PHE A 44 20.427 -22.573 1.292 1.00 14.51 C ANISOU 1241 CG PHE D 44 1561 1916 2034 -39 -117 467 C ATOM 1242 CD1 PHE A 44 19.541 -23.476 0.719 1.00 15.13 C ANISOU 1242 CD1 PHE D 44 1888 1968 1890 -17 113 448 C ATOM 1243 CD2 PHE A 44 20.354 -21.247 0.910 1.00 15.28 C ANISOU 1243 CD2 PHE D 44 1717 2204 1882 69 -138 150 C ATOM 1244 CE1 PHE A 44 18.582 -23.025 -0.189 1.00 16.24 C ANISOU 1244 CE1 PHE D 44 1869 2541 1758 -17 25 427 C ATOM 1245 CE2 PHE A 44 19.426 -20.815 0.010 1.00 16.52 C ANISOU 1245 CE2 PHE D 44 1855 2352 2067 10 -281 171 C ATOM 1246 CZ PHE A 44 18.535 -21.704 -0.533 1.00 16.72 C ANISOU 1246 CZ PHE D 44 1933 2761 1657 89 98 182 C ATOM 1247 N ALA A 45 24.105 -21.865 0.909 1.00 13.69 N ANISOU 1247 N ALA D 45 1598 1748 1854 -123 -157 457 N ATOM 1248 CA ALA A 45 24.786 -20.978 -0.017 1.00 13.28 C ANISOU 1248 CA ALA D 45 1607 1834 1603 -57 -125 437 C ATOM 1249 C ALA A 45 25.826 -20.185 0.769 1.00 12.63 C ANISOU 1249 C ALA D 45 1608 1732 1456 -73 -138 477 C ATOM 1250 O ALA A 45 25.727 -20.067 1.985 1.00 14.17 O ANISOU 1250 O ALA D 45 1753 1959 1670 -187 -168 527 O ATOM 1251 CB ALA A 45 23.811 -20.022 -0.701 1.00 14.54 C ANISOU 1251 CB ALA D 45 1631 2059 1833 -53 -105 246 C ATOM 1252 N SER A 46 26.863 -19.688 0.063 1.00 12.12 N ANISOU 1252 N SER D 46 1487 1698 1420 -21 -190 435 N ATOM 1253 CA SER A 46 27.865 -18.865 0.707 1.00 12.01 C ANISOU 1253 CA SER D 46 1491 1586 1486 131 -195 464 C ATOM 1254 C SER A 46 28.589 -17.984 -0.278 1.00 11.89 C ANISOU 1254 C SER D 46 1566 1415 1535 117 -60 464 C ATOM 1255 O SER A 46 28.512 -18.179 -1.471 1.00 14.37 O ANISOU 1255 O SER D 46 1931 1849 1678 20 -95 632 O ATOM 1256 CB SER A 46 28.848 -19.730 1.533 1.00 13.34 C ANISOU 1256 CB SER D 46 1672 1782 1612 -32 9 232 C ATOM 1257 OG SER A 46 29.537 -20.645 0.702 1.00 13.27 O ANISOU 1257 OG SER D 46 1543 1879 1619 129 -381 469 O ATOM 1258 N GLY A 47 29.330 -17.027 0.259 1.00 11.99 N ANISOU 1258 N GLY D 47 1441 1539 1575 -78 -33 376 N ATOM 1259 CA GLY A 47 30.136 -16.145 -0.583 1.00 12.61 C ANISOU 1259 CA GLY D 47 1524 1576 1689 -6 -100 345 C ATOM 1260 C GLY A 47 30.881 -15.142 0.274 1.00 12.87 C ANISOU 1260 C GLY D 47 1612 1632 1646 -26 -203 372 C ATOM 1261 O GLY A 47 30.855 -15.256 1.508 1.00 13.51 O ANISOU 1261 O GLY D 47 1787 1674 1671 -54 -170 351 O ATOM 1262 N LYS A 48 31.493 -14.170 -0.398 1.00 13.90 N ANISOU 1262 N LYS D 48 2008 1699 1572 -149 -95 346 N ATOM 1263 CA LYS A 48 32.178 -13.082 0.297 1.00 14.68 C ANISOU 1263 CA LYS D 48 2089 1768 1719 -156 -30 246 C ATOM 1264 C LYS A 48 31.572 -11.777 -0.184 1.00 14.12 C ANISOU 1264 C LYS D 48 2222 1656 1485 -196 -111 168 C ATOM 1265 O LYS A 48 31.283 -11.600 -1.371 1.00 14.26 O ANISOU 1265 O LYS D 48 2104 1871 1443 -206 -59 286 O ATOM 1266 CB LYS A 48 33.663 -13.064 -0.052 1.00 17.86 C ANISOU 1266 CB LYS D 48 2340 2174 2269 -148 10 207 C ATOM 1267 CG LYS A 48 34.417 -14.305 0.363 1.00 24.01 C ANISOU 1267 CG LYS D 48 3121 2691 3309 -50 112 73 C ATOM 1268 CD LYS A 48 34.795 -14.337 1.836 1.00 30.07 C ANISOU 1268 CD LYS D 48 3942 3751 3731 -24 -85 6 C ATOM 1269 CE LYS A 48 36.283 -14.006 2.127 1.00 31.24 C ANISOU 1269 CE LYS D 48 4106 3801 3962 -73 21 96 C ATOM 1270 NZ LYS A 48 36.615 -13.734 3.601 1.00 31.98 N ANISOU 1270 NZ LYS D 48 4168 4048 3934 159 296 -122 N ATOM 1271 N THR A 49 31.380 -10.828 0.726 1.00 12.95 N ANISOU 1271 N THR D 49 2060 1587 1272 -175 -213 131 N ATOM 1272 CA THR A 49 30.827 -9.555 0.295 1.00 13.08 C ANISOU 1272 CA THR D 49 1929 1663 1375 -129 -167 127 C ATOM 1273 C THR A 49 31.780 -8.869 -0.711 1.00 13.76 C ANISOU 1273 C THR D 49 1983 1893 1351 -150 -190 314 C ATOM 1274 O THR A 49 32.987 -8.985 -0.612 1.00 14.66 O ANISOU 1274 O THR D 49 1990 2031 1548 -125 -213 181 O ATOM 1275 CB THR A 49 30.561 -8.627 1.489 1.00 12.95 C ANISOU 1275 CB THR D 49 1873 1708 1339 21 -250 190 C ATOM 1276 OG1 THR A 49 31.816 -8.407 2.172 1.00 12.70 O ANISOU 1276 OG1 THR D 49 1810 1605 1410 -17 -16 49 O ATOM 1277 CG2 THR A 49 29.481 -9.195 2.436 1.00 12.59 C ANISOU 1277 CG2 THR D 49 1581 1908 1295 -73 -330 138 C ATOM 1278 N SER A 50 31.183 -8.084 -1.592 1.00 14.16 N ANISOU 1278 N SER D 50 2013 1914 1450 -194 -254 110 N ATOM 1279 CA SER A 50 31.866 -7.381 -2.662 1.00 16.00 C ANISOU 1279 CA SER D 50 2348 2188 1539 -149 -245 32 C ATOM 1280 C SER A 50 32.418 -6.071 -2.145 1.00 17.58 C ANISOU 1280 C SER D 50 2458 2293 1926 -195 -316 -9 C ATOM 1281 O SER A 50 32.275 -5.710 -0.964 1.00 16.55 O ANISOU 1281 O SER D 50 2697 2081 1508 -371 -290 79 O ATOM 1282 CB SER A 50 30.871 -7.062 -3.780 1.00 16.75 C ANISOU 1282 CB SER D 50 2541 2335 1487 -181 -245 38 C ATOM 1283 OG SER A 50 29.961 -6.051 -3.307 1.00 19.50 O ANISOU 1283 OG SER D 50 2968 2467 1971 -93 -250 -283 O ATOM 1284 N GLU A 51 33.005 -5.310 -3.032 1.00 18.29 N ANISOU 1284 N GLU D 51 2861 2366 1722 -283 -351 -148 N ATOM 1285 CA GLU A 51 33.438 -3.961 -2.728 1.00 18.81 C ANISOU 1285 CA GLU D 51 2792 2415 1940 -221 -276 -93 C ATOM 1286 C GLU A 51 32.340 -3.034 -2.226 1.00 17.73 C ANISOU 1286 C GLU D 51 2661 2340 1732 -222 -148 -244 C ATOM 1287 O GLU A 51 32.675 -2.035 -1.568 1.00 20.11 O ANISOU 1287 O GLU D 51 3031 2433 2176 -136 -193 -50 O ATOM 1288 CB GLU A 51 34.139 -3.320 -3.976 1.00 22.34 C ANISOU 1288 CB GLU D 51 3293 2819 2376 -235 -323 -78 C ATOM 1289 CG GLU A 51 35.507 -3.879 -4.179 1.00 28.10 C ANISOU 1289 CG GLU D 51 3682 3557 3436 -53 -174 -82 C ATOM 1290 CD GLU A 51 36.554 -3.348 -3.179 1.00 34.43 C ANISOU 1290 CD GLU D 51 4330 4437 4312 -124 -16 7 C ATOM 1291 OE1 GLU A 51 36.418 -2.191 -2.719 1.00 42.21 O ANISOU 1291 OE1 GLU D 51 5416 5238 5381 157 -141 123 O ATOM 1292 OE2 GLU A 51 37.527 -4.090 -2.868 1.00 41.27 O ANISOU 1292 OE2 GLU D 51 5292 5261 5125 78 45 -147 O ATOM 1293 N SER A 52 31.076 -3.317 -2.517 1.00 17.58 N ANISOU 1293 N SER D 52 2829 2244 1606 -178 -260 -219 N ATOM 1294 CA SER A 52 29.993 -2.507 -2.018 1.00 18.83 C ANISOU 1294 CA SER D 52 2876 2392 1884 -43 -144 -164 C ATOM 1295 C SER A 52 29.408 -3.102 -0.738 1.00 17.30 C ANISOU 1295 C SER D 52 2655 2170 1747 109 -118 -190 C ATOM 1296 O SER A 52 28.407 -2.591 -0.216 1.00 19.81 O ANISOU 1296 O SER D 52 3031 2558 1936 356 38 -180 O ATOM 1297 CB SER A 52 28.914 -2.427 -3.057 1.00 21.03 C ANISOU 1297 CB SER D 52 3054 2731 2204 58 -143 -260 C ATOM 1298 OG SER A 52 28.355 -3.691 -3.262 1.00 25.20 O ANISOU 1298 OG SER D 52 3560 3387 2624 -69 229 -1 O ATOM 1299 N GLY A 53 30.035 -4.161 -0.197 1.00 16.04 N ANISOU 1299 N GLY D 53 2616 1963 1513 71 -123 -165 N ATOM 1300 CA GLY A 53 29.561 -4.776 1.031 1.00 15.76 C ANISOU 1300 CA GLY D 53 2476 2191 1322 -4 -199 21 C ATOM 1301 C GLY A 53 28.388 -5.690 0.843 1.00 15.19 C ANISOU 1301 C GLY D 53 2339 2117 1313 42 -101 -55 C ATOM 1302 O GLY A 53 27.777 -6.127 1.778 1.00 14.61 O ANISOU 1302 O GLY D 53 2203 2161 1185 13 -372 -54 O ATOM 1303 N GLU A 54 28.075 -6.035 -0.400 1.00 14.87 N ANISOU 1303 N GLU D 54 2212 2282 1154 -73 -122 -12 N ATOM 1304 CA GLU A 54 26.907 -6.812 -0.738 1.00 15.74 C ANISOU 1304 CA GLU D 54 2337 2191 1451 -81 -128 16 C ATOM 1305 C GLU A 54 27.315 -8.169 -1.256 1.00 15.01 C ANISOU 1305 C GLU D 54 1977 2334 1389 17 -110 11 C ATOM 1306 O GLU A 54 28.416 -8.385 -1.826 1.00 15.94 O ANISOU 1306 O GLU D 54 1975 2534 1548 -34 -443 354 O ATOM 1307 CB GLU A 54 26.079 -6.062 -1.807 1.00 16.70 C ANISOU 1307 CB GLU D 54 2324 2250 1770 56 -2 59 C ATOM 1308 CG GLU A 54 25.587 -4.688 -1.296 1.00 19.62 C ANISOU 1308 CG GLU D 54 2819 2397 2237 55 -108 65 C ATOM 1309 CD GLU A 54 24.696 -3.905 -2.249 1.00 22.25 C ANISOU 1309 CD GLU D 54 3049 2648 2756 213 122 113 C ATOM 1310 OE1 GLU A 54 24.435 -4.397 -3.354 1.00 27.72 O ANISOU 1310 OE1 GLU D 54 4232 3073 3228 343 693 16 O ATOM 1311 OE2 GLU A 54 24.282 -2.778 -1.906 1.00 32.72 O ANISOU 1311 OE2 GLU D 54 4533 3435 4462 257 18 201 O ATOM 1312 N LEU A 55 26.386 -9.088 -1.074 1.00 13.87 N ANISOU 1312 N LEU D 55 1971 2005 1291 -41 -275 112 N ATOM 1313 CA LEU A 55 26.526 -10.434 -1.561 1.00 14.49 C ANISOU 1313 CA LEU D 55 1960 2101 1444 -28 -178 38 C ATOM 1314 C LEU A 55 25.242 -10.791 -2.233 1.00 15.29 C ANISOU 1314 C LEU D 55 2161 2246 1401 21 -94 139 C ATOM 1315 O LEU A 55 24.208 -10.931 -1.578 1.00 15.59 O ANISOU 1315 O LEU D 55 2073 2222 1627 -51 -111 8 O ATOM 1316 CB LEU A 55 26.845 -11.383 -0.429 1.00 14.65 C ANISOU 1316 CB LEU D 55 1904 2143 1518 28 -217 -105 C ATOM 1317 CG LEU A 55 27.045 -12.835 -0.746 1.00 15.34 C ANISOU 1317 CG LEU D 55 1940 2331 1556 49 -98 3 C ATOM 1318 CD1 LEU A 55 27.984 -13.056 -1.918 1.00 16.56 C ANISOU 1318 CD1 LEU D 55 2363 2498 1430 90 -305 396 C ATOM 1319 CD2 LEU A 55 27.509 -13.581 0.507 1.00 16.52 C ANISOU 1319 CD2 LEU D 55 2415 2477 1384 -2 -25 -4 C ATOM 1320 N HIS A 56 25.339 -10.883 -3.560 1.00 16.88 N ANISOU 1320 N HIS D 56 2448 2443 1521 -20 20 271 N ATOM 1321 CA HIS A 56 24.226 -11.136 -4.461 1.00 18.95 C ANISOU 1321 CA HIS D 56 2588 2611 2001 -17 82 136 C ATOM 1322 C HIS A 56 24.407 -12.563 -4.964 1.00 19.15 C ANISOU 1322 C HIS D 56 2700 2692 1881 -4 226 157 C ATOM 1323 O HIS A 56 25.450 -13.177 -4.775 1.00 19.98 O ANISOU 1323 O HIS D 56 2726 2762 2104 18 -202 326 O ATOM 1324 CB HIS A 56 24.247 -10.159 -5.661 1.00 21.26 C ANISOU 1324 CB HIS D 56 2961 2972 2145 22 143 150 C ATOM 1325 CG HIS A 56 23.986 -8.746 -5.267 1.00 24.28 C ANISOU 1325 CG HIS D 56 3446 3019 2759 124 122 -227 C ATOM 1326 ND1 HIS A 56 22.730 -8.170 -5.325 1.00 29.42 N ANISOU 1326 ND1 HIS D 56 3839 3651 3689 238 294 156 N ATOM 1327 CD2 HIS A 56 24.806 -7.811 -4.737 1.00 28.56 C ANISOU 1327 CD2 HIS D 56 3818 3499 3531 104 311 66 C ATOM 1328 CE1 HIS A 56 22.804 -6.923 -4.886 1.00 28.26 C ANISOU 1328 CE1 HIS D 56 3845 3535 3354 159 99 132 C ATOM 1329 NE2 HIS A 56 24.053 -6.679 -4.531 1.00 27.62 N ANISOU 1329 NE2 HIS D 56 3866 3419 3209 287 186 70 N ATOM 1330 N GLY A 57 23.363 -13.087 -5.562 1.00 19.40 N ANISOU 1330 N GLY D 57 2520 2608 2243 -218 62 206 N ATOM 1331 CA GLY A 57 23.459 -14.364 -6.267 1.00 19.25 C ANISOU 1331 CA GLY D 57 2592 2586 2134 -64 31 253 C ATOM 1332 C GLY A 57 23.503 -15.590 -5.398 1.00 19.53 C ANISOU 1332 C GLY D 57 2538 2610 2270 -91 29 301 C ATOM 1333 O GLY A 57 23.892 -16.656 -5.834 1.00 20.78 O ANISOU 1333 O GLY D 57 2847 2699 2350 141 -258 515 O ATOM 1334 N LEU A 58 23.104 -15.461 -4.144 1.00 18.51 N ANISOU 1334 N LEU D 58 2324 2598 2109 -85 -127 318 N ATOM 1335 CA LEU A 58 23.145 -16.604 -3.241 1.00 17.62 C ANISOU 1335 CA LEU D 58 2190 2408 2095 86 -8 329 C ATOM 1336 C LEU A 58 22.238 -17.747 -3.637 1.00 17.26 C ANISOU 1336 C LEU D 58 2155 2446 1954 131 -79 355 C ATOM 1337 O LEU A 58 22.626 -18.919 -3.529 1.00 18.75 O ANISOU 1337 O LEU D 58 2526 2512 2086 -7 207 438 O ATOM 1338 CB LEU A 58 22.850 -16.194 -1.791 1.00 18.15 C ANISOU 1338 CB LEU D 58 2196 2577 2121 11 -112 293 C ATOM 1339 CG LEU A 58 24.014 -15.455 -1.130 1.00 16.34 C ANISOU 1339 CG LEU D 58 2135 2261 1810 -78 -100 215 C ATOM 1340 CD1 LEU A 58 23.504 -14.681 0.081 1.00 18.71 C ANISOU 1340 CD1 LEU D 58 2472 2791 1844 -233 -184 502 C ATOM 1341 CD2 LEU A 58 25.163 -16.382 -0.826 1.00 19.43 C ANISOU 1341 CD2 LEU D 58 2579 2215 2588 -136 340 183 C ATOM 1342 N THR A 59 21.052 -17.413 -4.136 1.00 17.26 N ANISOU 1342 N THR D 59 1970 2435 2153 149 -121 486 N ATOM 1343 CA THR A 59 20.058 -18.430 -4.422 1.00 18.03 C ANISOU 1343 CA THR D 59 2279 2443 2126 23 -11 351 C ATOM 1344 C THR A 59 19.109 -17.959 -5.494 1.00 18.78 C ANISOU 1344 C THR D 59 2303 2579 2254 -97 33 323 C ATOM 1345 O THR A 59 19.257 -16.892 -6.057 1.00 18.89 O ANISOU 1345 O THR D 59 2425 2704 2045 -44 257 354 O ATOM 1346 CB THR A 59 19.303 -18.829 -3.121 1.00 17.38 C ANISOU 1346 CB THR D 59 2120 2394 2089 -75 83 298 C ATOM 1347 OG1 THR A 59 18.518 -20.033 -3.326 1.00 19.05 O ANISOU 1347 OG1 THR D 59 2517 2664 2055 -189 -124 241 O ATOM 1348 CG2 THR A 59 18.444 -17.673 -2.581 1.00 18.52 C ANISOU 1348 CG2 THR D 59 2229 2709 2096 105 -97 342 C ATOM 1349 N THR A 60 18.135 -18.803 -5.802 1.00 19.28 N ANISOU 1349 N THR D 60 2363 2646 2316 -201 159 266 N ATOM 1350 CA THR A 60 17.140 -18.496 -6.824 1.00 20.10 C ANISOU 1350 CA THR D 60 2524 2730 2383 -154 134 303 C ATOM 1351 C THR A 60 15.789 -18.636 -6.186 1.00 19.55 C ANISOU 1351 C THR D 60 2513 2596 2316 -159 161 332 C ATOM 1352 O THR A 60 15.649 -19.277 -5.133 1.00 18.24 O ANISOU 1352 O THR D 60 2447 2359 2124 -246 135 637 O ATOM 1353 CB THR A 60 17.221 -19.444 -7.981 1.00 20.64 C ANISOU 1353 CB THR D 60 2407 2962 2471 -91 -36 300 C ATOM 1354 OG1 THR A 60 16.967 -20.786 -7.519 1.00 23.39 O ANISOU 1354 OG1 THR D 60 2856 3094 2937 -140 -25 869 O ATOM 1355 CG2 THR A 60 18.602 -19.304 -8.716 1.00 22.58 C ANISOU 1355 CG2 THR D 60 2751 3271 2555 -184 -265 433 C ATOM 1356 N GLU A 61 14.772 -18.074 -6.820 1.00 21.22 N ANISOU 1356 N GLU D 61 2629 2824 2609 -100 168 246 N ATOM 1357 CA GLU A 61 13.408 -18.236 -6.322 1.00 23.21 C ANISOU 1357 CA GLU D 61 2811 3070 2938 -110 147 173 C ATOM 1358 C GLU A 61 13.016 -19.718 -6.215 1.00 21.77 C ANISOU 1358 C GLU D 61 2555 2924 2791 -102 190 160 C ATOM 1359 O GLU A 61 12.393 -20.113 -5.259 1.00 20.91 O ANISOU 1359 O GLU D 61 2331 2954 2660 -289 218 268 O ATOM 1360 CB GLU A 61 12.416 -17.494 -7.196 1.00 25.25 C ANISOU 1360 CB GLU D 61 3107 3202 3283 -49 209 109 C ATOM 1361 CG GLU A 61 12.523 -15.991 -7.059 1.00 28.60 C ANISOU 1361 CG GLU D 61 3549 3606 3710 -51 274 17 C ATOM 1362 CD GLU A 61 11.300 -15.271 -7.572 1.00 31.59 C ANISOU 1362 CD GLU D 61 3917 4019 4065 152 187 77 C ATOM 1363 OE1 GLU A 61 10.779 -15.702 -8.638 1.00 37.91 O ANISOU 1363 OE1 GLU D 61 4868 5072 4463 -19 281 94 O ATOM 1364 OE2 GLU A 61 10.877 -14.291 -6.885 1.00 40.79 O ANISOU 1364 OE2 GLU D 61 5280 5074 5142 289 -13 320 O ATOM 1365 N GLU A 62 13.407 -20.540 -7.173 1.00 20.85 N ANISOU 1365 N GLU D 62 2380 2878 2664 -115 163 167 N ATOM 1366 CA GLU A 62 13.023 -21.938 -7.139 1.00 23.01 C ANISOU 1366 CA GLU D 62 2732 3039 2970 -101 96 127 C ATOM 1367 C GLU A 62 13.594 -22.641 -5.904 1.00 20.81 C ANISOU 1367 C GLU D 62 2334 2854 2716 -116 188 227 C ATOM 1368 O GLU A 62 12.926 -23.444 -5.262 1.00 22.10 O ANISOU 1368 O GLU D 62 2305 3112 2979 -287 265 217 O ATOM 1369 CB GLU A 62 13.484 -22.626 -8.432 1.00 24.99 C ANISOU 1369 CB GLU D 62 3087 3166 3242 -40 54 157 C ATOM 1370 CG GLU A 62 12.534 -22.418 -9.669 1.00 30.56 C ANISOU 1370 CG GLU D 62 3829 3938 3842 -29 168 108 C ATOM 1371 CD GLU A 62 12.497 -23.622 -10.631 1.00 31.58 C ANISOU 1371 CD GLU D 62 3982 4120 3898 -82 217 200 C ATOM 1372 OE1 GLU A 62 13.371 -24.536 -10.518 1.00 41.25 O ANISOU 1372 OE1 GLU D 62 5224 5064 5385 245 191 140 O ATOM 1373 OE2 GLU A 62 11.608 -23.629 -11.534 1.00 36.71 O ANISOU 1373 OE2 GLU D 62 4367 5362 4218 -111 612 180 O ATOM 1374 N GLU A 63 14.848 -22.356 -5.566 1.00 20.05 N ANISOU 1374 N GLU D 63 2298 2503 2815 -110 6 429 N ATOM 1375 CA GLU A 63 15.519 -23.045 -4.474 1.00 20.16 C ANISOU 1375 CA GLU D 63 2346 2585 2728 -62 32 360 C ATOM 1376 C GLU A 63 15.151 -22.516 -3.073 1.00 17.41 C ANISOU 1376 C GLU D 63 1876 2284 2453 -143 88 333 C ATOM 1377 O GLU A 63 15.174 -23.237 -2.089 1.00 18.86 O ANISOU 1377 O GLU D 63 2055 2271 2838 -90 416 514 O ATOM 1378 CB GLU A 63 17.046 -22.914 -4.671 1.00 20.76 C ANISOU 1378 CB GLU D 63 2329 2794 2765 -1 -26 377 C ATOM 1379 CG GLU A 63 17.624 -23.497 -6.008 1.00 23.84 C ANISOU 1379 CG GLU D 63 2803 3196 3058 73 68 384 C ATOM 1380 CD GLU A 63 19.057 -23.008 -6.377 1.00 26.41 C ANISOU 1380 CD GLU D 63 3110 3326 3596 -3 -111 289 C ATOM 1381 OE1 GLU A 63 19.338 -21.795 -6.613 1.00 32.52 O ANISOU 1381 OE1 GLU D 63 3759 4015 4582 -126 -291 -59 O ATOM 1382 OE2 GLU A 63 19.933 -23.892 -6.463 1.00 35.54 O ANISOU 1382 OE2 GLU D 63 4045 4481 4974 372 26 227 O ATOM 1383 N PHE A 64 14.746 -21.252 -3.006 1.00 16.31 N ANISOU 1383 N PHE D 64 1772 2173 2252 -133 191 306 N ATOM 1384 CA PHE A 64 14.528 -20.563 -1.718 1.00 16.65 C ANISOU 1384 CA PHE D 64 1870 2353 2100 -34 -1 248 C ATOM 1385 C PHE A 64 13.103 -20.741 -1.222 1.00 15.17 C ANISOU 1385 C PHE D 64 1807 2130 1825 20 -93 173 C ATOM 1386 O PHE A 64 12.309 -19.787 -1.139 1.00 16.79 O ANISOU 1386 O PHE D 64 1989 2236 2151 25 46 405 O ATOM 1387 CB PHE A 64 14.893 -19.085 -1.839 1.00 15.97 C ANISOU 1387 CB PHE D 64 1877 2355 1835 -81 48 184 C ATOM 1388 CG PHE A 64 15.025 -18.349 -0.520 1.00 15.22 C ANISOU 1388 CG PHE D 64 1875 2025 1881 -42 -174 112 C ATOM 1389 CD1 PHE A 64 15.880 -18.790 0.441 1.00 16.93 C ANISOU 1389 CD1 PHE D 64 2184 2068 2180 2 -12 293 C ATOM 1390 CD2 PHE A 64 14.310 -17.183 -0.278 1.00 19.21 C ANISOU 1390 CD2 PHE D 64 2590 2333 2374 -67 425 451 C ATOM 1391 CE1 PHE A 64 16.021 -18.037 1.620 1.00 16.60 C ANISOU 1391 CE1 PHE D 64 2168 2251 1886 -165 96 124 C ATOM 1392 CE2 PHE A 64 14.454 -16.489 0.895 1.00 17.94 C ANISOU 1392 CE2 PHE D 64 2456 2354 2007 348 24 420 C ATOM 1393 CZ PHE A 64 15.322 -16.928 1.813 1.00 18.15 C ANISOU 1393 CZ PHE D 64 2391 2438 2067 -159 149 314 C ATOM 1394 N VAL A 65 12.813 -21.972 -0.852 1.00 13.34 N ANISOU 1394 N VAL D 65 1418 1731 1919 -74 20 506 N ATOM 1395 CA VAL A 65 11.500 -22.353 -0.396 1.00 14.30 C ANISOU 1395 CA VAL D 65 1711 1807 1914 -91 -90 324 C ATOM 1396 C VAL A 65 11.278 -21.945 1.043 1.00 13.91 C ANISOU 1396 C VAL D 65 1624 1959 1700 -66 32 342 C ATOM 1397 O VAL A 65 12.210 -21.598 1.738 1.00 13.32 O ANISOU 1397 O VAL D 65 1526 2025 1507 -248 277 661 O ATOM 1398 CB VAL A 65 11.267 -23.853 -0.542 1.00 13.78 C ANISOU 1398 CB VAL D 65 1538 1736 1961 -278 93 583 C ATOM 1399 CG1 VAL A 65 11.276 -24.281 -2.063 1.00 16.79 C ANISOU 1399 CG1 VAL D 65 2308 1821 2250 -341 14 892 C ATOM 1400 CG2 VAL A 65 12.225 -24.704 0.312 1.00 17.51 C ANISOU 1400 CG2 VAL D 65 2439 1680 2531 20 106 429 C ATOM 1401 N GLU A 66 10.053 -21.949 1.500 1.00 12.41 N ANISOU 1401 N GLU D 66 1478 1740 1496 -51 254 477 N ATOM 1402 CA GLU A 66 9.753 -21.622 2.869 1.00 13.05 C ANISOU 1402 CA GLU D 66 1612 1762 1582 -66 86 488 C ATOM 1403 C GLU A 66 10.538 -22.518 3.796 1.00 14.13 C ANISOU 1403 C GLU D 66 1762 1863 1741 -150 112 370 C ATOM 1404 O GLU A 66 10.751 -23.702 3.568 1.00 15.79 O ANISOU 1404 O GLU D 66 2080 2062 1856 -239 262 580 O ATOM 1405 CB GLU A 66 8.234 -21.796 3.175 1.00 13.84 C ANISOU 1405 CB GLU D 66 1803 1845 1609 -19 22 651 C ATOM 1406 CG GLU A 66 7.372 -20.799 2.493 1.00 14.45 C ANISOU 1406 CG GLU D 66 1793 2122 1574 24 90 460 C ATOM 1407 CD GLU A 66 5.911 -20.869 2.857 1.00 15.27 C ANISOU 1407 CD GLU D 66 1788 2098 1913 88 -12 477 C ATOM 1408 OE1 GLU A 66 5.290 -21.968 2.678 1.00 16.05 O ANISOU 1408 OE1 GLU D 66 1946 2280 1870 103 -63 630 O ATOM 1409 OE2 GLU A 66 5.355 -19.785 3.209 1.00 20.24 O ANISOU 1409 OE2 GLU D 66 2707 2243 2741 -9 120 489 O ATOM 1410 N GLY A 67 10.878 -21.947 4.926 1.00 14.23 N ANISOU 1410 N GLY D 67 1858 1802 1746 -240 323 342 N ATOM 1411 CA GLY A 67 11.624 -22.671 5.961 1.00 14.64 C ANISOU 1411 CA GLY D 67 1863 1898 1800 -314 188 176 C ATOM 1412 C GLY A 67 12.431 -21.722 6.812 1.00 13.74 C ANISOU 1412 C GLY D 67 1717 1855 1649 -293 201 159 C ATOM 1413 O GLY A 67 12.338 -20.550 6.635 1.00 14.28 O ANISOU 1413 O GLY D 67 1902 1901 1622 -47 333 461 O ATOM 1414 N ILE A 68 13.204 -22.282 7.716 1.00 14.35 N ANISOU 1414 N ILE D 68 1752 1934 1764 -387 233 98 N ATOM 1415 CA ILE A 68 14.048 -21.493 8.613 1.00 13.09 C ANISOU 1415 CA ILE D 68 1687 1655 1631 -187 79 283 C ATOM 1416 C ILE A 68 15.468 -21.501 8.047 1.00 12.65 C ANISOU 1416 C ILE D 68 1749 1533 1522 -152 95 287 C ATOM 1417 O ILE A 68 16.020 -22.559 7.719 1.00 13.36 O ANISOU 1417 O ILE D 68 1865 1437 1773 -25 -156 273 O ATOM 1418 CB ILE A 68 14.012 -22.087 10.028 1.00 14.18 C ANISOU 1418 CB ILE D 68 1739 1932 1717 -190 -108 238 C ATOM 1419 CG1 ILE A 68 12.583 -22.037 10.592 1.00 17.27 C ANISOU 1419 CG1 ILE D 68 1842 2694 2023 23 -19 84 C ATOM 1420 CG2 ILE A 68 14.948 -21.315 10.959 1.00 14.95 C ANISOU 1420 CG2 ILE D 68 1790 2143 1744 -357 109 316 C ATOM 1421 CD1 ILE A 68 12.409 -22.599 12.008 1.00 19.44 C ANISOU 1421 CD1 ILE D 68 2295 2781 2310 -75 -160 -203 C ATOM 1422 N TYR A 69 16.036 -20.294 7.926 1.00 11.34 N ANISOU 1422 N TYR D 69 1287 1435 1586 -162 0 542 N ATOM 1423 CA TYR A 69 17.363 -20.102 7.406 1.00 11.09 C ANISOU 1423 CA TYR D 69 1330 1425 1455 -163 112 399 C ATOM 1424 C TYR A 69 18.198 -19.368 8.480 1.00 10.15 C ANISOU 1424 C TYR D 69 1297 1466 1090 -131 36 518 C ATOM 1425 O TYR A 69 17.701 -18.617 9.308 1.00 12.24 O ANISOU 1425 O TYR D 69 1307 1813 1531 88 -8 468 O ATOM 1426 CB TYR A 69 17.324 -19.245 6.143 1.00 12.00 C ANISOU 1426 CB TYR D 69 1295 1595 1668 -92 -42 368 C ATOM 1427 CG TYR A 69 16.660 -19.963 4.995 1.00 13.22 C ANISOU 1427 CG TYR D 69 1506 1773 1744 -40 -41 351 C ATOM 1428 CD1 TYR A 69 15.285 -19.987 4.856 1.00 11.16 C ANISOU 1428 CD1 TYR D 69 1266 1764 1208 -68 341 455 C ATOM 1429 CD2 TYR A 69 17.399 -20.656 4.042 1.00 12.72 C ANISOU 1429 CD2 TYR D 69 1400 2195 1237 -149 -42 419 C ATOM 1430 CE1 TYR A 69 14.650 -20.677 3.762 1.00 12.30 C ANISOU 1430 CE1 TYR D 69 1059 2038 1575 -83 325 573 C ATOM 1431 CE2 TYR A 69 16.804 -21.318 2.975 1.00 13.26 C ANISOU 1431 CE2 TYR D 69 1362 2074 1598 8 195 412 C ATOM 1432 CZ TYR A 69 15.465 -21.301 2.861 1.00 12.93 C ANISOU 1432 CZ TYR D 69 1352 1882 1676 -90 155 506 C ATOM 1433 OH TYR A 69 14.858 -21.964 1.792 1.00 13.09 O ANISOU 1433 OH TYR D 69 1589 1957 1425 -10 321 755 O ATOM 1434 N LYS A 70 19.502 -19.616 8.377 1.00 10.84 N ANISOU 1434 N LYS D 70 1298 1396 1425 27 -56 406 N ATOM 1435 CA ALYS A 70 20.469 -18.912 9.189 0.50 11.48 C ANISOU 1435 CA ALYS D 70 1413 1528 1420 -43 -57 269 C ATOM 1436 C LYS A 70 21.558 -18.349 8.264 1.00 10.23 C ANISOU 1436 C LYS D 70 1262 1330 1292 45 -85 433 C ATOM 1437 O LYS A 70 22.104 -19.050 7.418 1.00 12.29 O ANISOU 1437 O LYS D 70 1535 1570 1565 -52 -215 593 O ATOM 1438 CB ALYS A 70 21.043 -19.816 10.296 0.50 12.17 C ANISOU 1438 CB ALYS D 70 1637 1588 1397 -76 180 307 C ATOM 1439 CG ALYS A 70 22.230 -19.206 11.102 0.50 12.65 C ANISOU 1439 CG ALYS D 70 1557 1872 1377 48 108 328 C ATOM 1440 CD ALYS A 70 22.785 -20.168 12.158 0.50 12.87 C ANISOU 1440 CD ALYS D 70 1630 1791 1466 105 -224 134 C ATOM 1441 CE ALYS A 70 23.242 -21.504 11.648 0.50 15.69 C ANISOU 1441 CE ALYS D 70 2100 1897 1964 56 -33 -39 C ATOM 1442 NZ ALYS A 70 24.134 -22.173 12.659 0.50 18.95 N ANISOU 1442 NZ ALYS D 70 2504 2330 2363 176 215 47 N ATOM 1443 N VAL A 71 21.811 -17.049 8.480 1.00 11.17 N ANISOU 1443 N VAL D 71 1388 1421 1435 -133 -92 343 N ATOM 1444 CA VAL A 71 22.866 -16.321 7.828 1.00 11.39 C ANISOU 1444 CA VAL D 71 1462 1679 1183 -114 -195 354 C ATOM 1445 C VAL A 71 23.950 -16.080 8.866 1.00 11.23 C ANISOU 1445 C VAL D 71 1297 1644 1324 -45 -248 411 C ATOM 1446 O VAL A 71 23.690 -15.402 9.835 1.00 12.53 O ANISOU 1446 O VAL D 71 1322 2007 1431 -154 -156 634 O ATOM 1447 CB VAL A 71 22.370 -15.022 7.227 1.00 12.35 C ANISOU 1447 CB VAL D 71 1860 1733 1099 -87 -198 450 C ATOM 1448 CG1 VAL A 71 23.532 -14.215 6.575 1.00 15.40 C ANISOU 1448 CG1 VAL D 71 2045 2342 1464 -223 -253 93 C ATOM 1449 CG2 VAL A 71 21.243 -15.235 6.181 1.00 14.70 C ANISOU 1449 CG2 VAL D 71 1669 2131 1783 -24 -5 267 C ATOM 1450 N GLU A 72 25.137 -16.670 8.654 1.00 11.73 N ANISOU 1450 N GLU D 72 1336 1682 1439 -101 -6 334 N ATOM 1451 CA GLU A 72 26.281 -16.470 9.547 1.00 12.33 C ANISOU 1451 CA GLU D 72 1548 1701 1433 -126 -66 231 C ATOM 1452 C GLU A 72 27.305 -15.592 8.819 1.00 10.97 C ANISOU 1452 C GLU D 72 1460 1574 1131 -203 -107 290 C ATOM 1453 O GLU A 72 27.729 -15.867 7.704 1.00 14.58 O ANISOU 1453 O GLU D 72 1869 1898 1772 -350 -161 478 O ATOM 1454 CB GLU A 72 26.876 -17.809 9.851 1.00 15.12 C ANISOU 1454 CB GLU D 72 1938 1935 1871 -132 -39 108 C ATOM 1455 CG GLU A 72 28.002 -17.829 10.816 1.00 17.10 C ANISOU 1455 CG GLU D 72 2223 2126 2145 84 44 156 C ATOM 1456 CD GLU A 72 28.125 -19.223 11.452 1.00 21.67 C ANISOU 1456 CD GLU D 72 2991 2702 2538 293 -60 0 C ATOM 1457 OE1 GLU A 72 28.537 -20.118 10.732 1.00 29.69 O ANISOU 1457 OE1 GLU D 72 3855 3893 3529 452 -15 313 O ATOM 1458 OE2 GLU A 72 27.713 -19.406 12.617 1.00 33.75 O ANISOU 1458 OE2 GLU D 72 4889 4407 3526 -82 -282 -176 O ATOM 1459 N ILE A 73 27.649 -14.510 9.540 1.00 10.97 N ANISOU 1459 N ILE D 73 1607 1544 1015 -319 47 174 N ATOM 1460 CA ILE A 73 28.541 -13.491 8.982 1.00 11.91 C ANISOU 1460 CA ILE D 73 1689 1559 1275 -153 122 142 C ATOM 1461 C ILE A 73 29.832 -13.584 9.794 1.00 11.22 C ANISOU 1461 C ILE D 73 1534 1447 1282 -172 143 27 C ATOM 1462 O ILE A 73 29.827 -13.444 11.034 1.00 11.93 O ANISOU 1462 O ILE D 73 1737 1692 1103 -257 204 -25 O ATOM 1463 CB ILE A 73 27.933 -12.080 9.059 1.00 11.44 C ANISOU 1463 CB ILE D 73 1721 1603 1022 -17 254 163 C ATOM 1464 CG1 ILE A 73 26.594 -12.063 8.346 1.00 11.86 C ANISOU 1464 CG1 ILE D 73 1909 1507 1089 -22 199 254 C ATOM 1465 CG2 ILE A 73 28.878 -11.039 8.507 1.00 12.99 C ANISOU 1465 CG2 ILE D 73 2107 1682 1145 -114 280 -75 C ATOM 1466 CD1 ILE A 73 25.765 -10.796 8.494 1.00 15.00 C ANISOU 1466 CD1 ILE D 73 2177 1902 1618 55 247 214 C ATOM 1467 N ASP A 74 30.948 -13.782 9.112 1.00 12.14 N ANISOU 1467 N ASP D 74 1533 1665 1415 -48 166 176 N ATOM 1468 CA AASP A 74 32.250 -13.998 9.792 0.50 12.82 C ANISOU 1468 CA AASP D 74 1625 1638 1606 -50 202 128 C ATOM 1469 C ASP A 74 32.878 -12.681 10.194 1.00 12.80 C ANISOU 1469 C ASP D 74 1466 1721 1676 -74 214 77 C ATOM 1470 O ASP A 74 33.852 -12.248 9.625 1.00 13.71 O ANISOU 1470 O ASP D 74 1705 1911 1590 -67 204 305 O ATOM 1471 CB AASP A 74 33.250 -14.778 8.916 0.50 13.85 C ANISOU 1471 CB AASP D 74 1740 1643 1876 1 158 184 C ATOM 1472 CG AASP A 74 34.560 -15.094 9.655 0.50 14.20 C ANISOU 1472 CG AASP D 74 1598 1719 2079 -87 29 259 C ATOM 1473 OD1AASP A 74 34.685 -14.725 10.841 0.50 14.21 O ANISOU 1473 OD1AASP D 74 1481 1370 2547 -2 499 62 O ATOM 1474 OD2AASP A 74 35.470 -15.647 9.001 0.50 18.69 O ANISOU 1474 OD2AASP D 74 1587 2480 3032 122 465 756 O ATOM 1475 N THR A 75 32.279 -12.053 11.201 1.00 11.60 N ANISOU 1475 N THR D 75 1529 1505 1372 -144 213 176 N ATOM 1476 CA THR A 75 32.705 -10.772 11.689 1.00 11.89 C ANISOU 1476 CA THR D 75 1491 1522 1503 -54 282 19 C ATOM 1477 C THR A 75 34.101 -10.809 12.352 1.00 10.81 C ANISOU 1477 C THR D 75 1295 1426 1387 -54 251 -10 C ATOM 1478 O THR A 75 34.848 -9.856 12.251 1.00 11.66 O ANISOU 1478 O THR D 75 1637 1621 1172 -80 0 -78 O ATOM 1479 CB THR A 75 31.645 -10.229 12.665 1.00 11.34 C ANISOU 1479 CB THR D 75 1548 1215 1546 -178 348 13 C ATOM 1480 OG1 THR A 75 31.508 -11.103 13.762 1.00 11.52 O ANISOU 1480 OG1 THR D 75 1559 1387 1430 -91 6 -89 O ATOM 1481 CG2 THR A 75 30.296 -10.016 11.985 1.00 13.35 C ANISOU 1481 CG2 THR D 75 1446 1775 1848 210 418 27 C ATOM 1482 N LYS A 76 34.407 -11.910 13.010 1.00 12.68 N ANISOU 1482 N LYS D 76 1475 1586 1757 -155 335 -107 N ATOM 1483 CA LYS A 76 35.659 -12.010 13.749 1.00 13.52 C ANISOU 1483 CA LYS D 76 1593 1680 1861 -60 307 -89 C ATOM 1484 C LYS A 76 36.852 -11.885 12.773 1.00 13.51 C ANISOU 1484 C LYS D 76 1625 1716 1792 -12 320 -44 C ATOM 1485 O LYS A 76 37.811 -11.131 13.030 1.00 13.72 O ANISOU 1485 O LYS D 76 1515 1699 1996 -34 253 -82 O ATOM 1486 CB LYS A 76 35.720 -13.285 14.560 1.00 13.66 C ANISOU 1486 CB LYS D 76 1600 1683 1906 -260 342 -61 C ATOM 1487 CG LYS A 76 36.946 -13.360 15.474 1.00 16.48 C ANISOU 1487 CG LYS D 76 1849 2137 2276 -49 505 -202 C ATOM 1488 CD LYS A 76 36.881 -14.628 16.317 1.00 17.88 C ANISOU 1488 CD LYS D 76 2022 2419 2352 138 335 -376 C ATOM 1489 CE LYS A 76 37.965 -14.693 17.372 1.00 23.14 C ANISOU 1489 CE LYS D 76 2655 3167 2969 80 356 -268 C ATOM 1490 NZ LYS A 76 37.829 -15.885 18.266 1.00 26.36 N ANISOU 1490 NZ LYS D 76 3034 3308 3671 176 254 -647 N ATOM 1491 N SER A 77 36.789 -12.591 11.627 1.00 14.65 N ANISOU 1491 N SER D 77 1715 1811 2037 50 212 44 N ATOM 1492 CA SER A 77 37.889 -12.509 10.642 1.00 14.70 C ANISOU 1492 CA SER D 77 1665 2058 1860 109 222 140 C ATOM 1493 C SER A 77 37.996 -11.138 10.070 1.00 14.81 C ANISOU 1493 C SER D 77 1558 2257 1811 106 167 163 C ATOM 1494 O SER A 77 39.099 -10.668 9.765 1.00 15.97 O ANISOU 1494 O SER D 77 1355 2614 2096 96 20 -151 O ATOM 1495 CB SER A 77 37.725 -13.514 9.539 1.00 17.97 C ANISOU 1495 CB SER D 77 2063 2495 2267 37 236 168 C ATOM 1496 OG SER A 77 37.760 -14.791 10.083 1.00 21.73 O ANISOU 1496 OG SER D 77 2556 2353 3346 380 281 575 O ATOM 1497 N TYR A 78 36.849 -10.510 9.833 1.00 14.32 N ANISOU 1497 N TYR D 78 1456 2237 1745 165 255 37 N ATOM 1498 CA TYR A 78 36.838 -9.144 9.321 1.00 14.19 C ANISOU 1498 CA TYR D 78 1499 2220 1670 85 95 -129 C ATOM 1499 C TYR A 78 37.644 -8.183 10.210 1.00 13.73 C ANISOU 1499 C TYR D 78 1334 2117 1765 35 139 -238 C ATOM 1500 O TYR A 78 38.518 -7.440 9.768 1.00 15.65 O ANISOU 1500 O TYR D 78 1583 2424 1936 -77 -3 -320 O ATOM 1501 CB TYR A 78 35.398 -8.650 9.159 1.00 13.85 C ANISOU 1501 CB TYR D 78 1368 2198 1693 201 -16 -121 C ATOM 1502 CG TYR A 78 35.318 -7.228 8.658 1.00 13.32 C ANISOU 1502 CG TYR D 78 1285 2177 1599 136 -23 -18 C ATOM 1503 CD1 TYR A 78 35.597 -6.936 7.356 1.00 13.50 C ANISOU 1503 CD1 TYR D 78 1644 2110 1373 431 -157 99 C ATOM 1504 CD2 TYR A 78 34.998 -6.174 9.523 1.00 12.30 C ANISOU 1504 CD2 TYR D 78 1303 2052 1319 -10 -31 94 C ATOM 1505 CE1 TYR A 78 35.546 -5.654 6.900 1.00 14.11 C ANISOU 1505 CE1 TYR D 78 1803 2209 1347 441 -19 -53 C ATOM 1506 CE2 TYR A 78 34.947 -4.906 9.084 1.00 13.46 C ANISOU 1506 CE2 TYR D 78 1784 1957 1370 389 -102 196 C ATOM 1507 CZ TYR A 78 35.234 -4.613 7.753 1.00 13.50 C ANISOU 1507 CZ TYR D 78 1568 1999 1561 233 -48 -7 C ATOM 1508 OH TYR A 78 35.203 -3.311 7.251 1.00 15.21 O ANISOU 1508 OH TYR D 78 1638 2457 1680 264 -77 -6 O ATOM 1509 N TRP A 79 37.325 -8.175 11.508 1.00 12.41 N ANISOU 1509 N TRP D 79 1367 1825 1522 25 133 -170 N ATOM 1510 CA TRP A 79 37.987 -7.263 12.410 1.00 12.62 C ANISOU 1510 CA TRP D 79 1208 1828 1758 18 132 -113 C ATOM 1511 C TRP A 79 39.470 -7.619 12.606 1.00 13.90 C ANISOU 1511 C TRP D 79 1259 1918 2101 -74 211 -179 C ATOM 1512 O TRP A 79 40.349 -6.755 12.628 1.00 15.24 O ANISOU 1512 O TRP D 79 1332 2162 2294 -126 353 -184 O ATOM 1513 CB TRP A 79 37.273 -7.221 13.767 1.00 11.80 C ANISOU 1513 CB TRP D 79 1395 1571 1515 -5 133 -140 C ATOM 1514 CG TRP A 79 35.940 -6.611 13.704 1.00 10.84 C ANISOU 1514 CG TRP D 79 1407 1492 1220 -49 122 -139 C ATOM 1515 CD1 TRP A 79 34.744 -7.220 13.955 1.00 11.71 C ANISOU 1515 CD1 TRP D 79 1493 1376 1578 0 -82 -117 C ATOM 1516 CD2 TRP A 79 35.635 -5.262 13.366 1.00 10.77 C ANISOU 1516 CD2 TRP D 79 1282 1606 1204 -97 -50 -54 C ATOM 1517 NE1 TRP A 79 33.704 -6.339 13.776 1.00 11.62 N ANISOU 1517 NE1 TRP D 79 1388 1569 1455 -196 67 188 N ATOM 1518 CE2 TRP A 79 34.226 -5.121 13.413 1.00 10.61 C ANISOU 1518 CE2 TRP D 79 1181 1485 1364 -120 -55 26 C ATOM 1519 CE3 TRP A 79 36.408 -4.152 13.019 1.00 12.90 C ANISOU 1519 CE3 TRP D 79 1483 1721 1696 -109 -181 -128 C ATOM 1520 CZ2 TRP A 79 33.591 -3.929 13.102 1.00 12.51 C ANISOU 1520 CZ2 TRP D 79 1426 1792 1535 49 -185 -192 C ATOM 1521 CZ3 TRP A 79 35.745 -2.978 12.686 1.00 13.58 C ANISOU 1521 CZ3 TRP D 79 1775 1599 1787 -204 -187 -233 C ATOM 1522 CH2 TRP A 79 34.365 -2.872 12.767 1.00 12.55 C ANISOU 1522 CH2 TRP D 79 1696 1458 1612 280 31 -297 C ATOM 1523 N LYS A 80 39.759 -8.899 12.665 1.00 13.44 N ANISOU 1523 N LYS D 80 1138 1954 2011 37 387 -81 N ATOM 1524 CA LYS A 80 41.153 -9.305 12.839 1.00 15.87 C ANISOU 1524 CA LYS D 80 1489 2236 2304 85 245 -35 C ATOM 1525 C LYS A 80 41.995 -8.880 11.659 1.00 16.27 C ANISOU 1525 C LYS D 80 1275 2403 2504 117 159 -91 C ATOM 1526 O LYS A 80 43.166 -8.502 11.816 1.00 18.71 O ANISOU 1526 O LYS D 80 1482 2469 3157 37 281 -177 O ATOM 1527 CB LYS A 80 41.229 -10.793 13.098 1.00 16.36 C ANISOU 1527 CB LYS D 80 1484 2382 2347 130 260 31 C ATOM 1528 CG LYS A 80 40.756 -11.130 14.513 1.00 20.34 C ANISOU 1528 CG LYS D 80 2169 2728 2832 -21 4 -127 C ATOM 1529 CD LYS A 80 40.892 -12.566 14.859 1.00 23.15 C ANISOU 1529 CD LYS D 80 2601 3044 3148 64 93 -191 C ATOM 1530 CE LYS A 80 40.344 -12.826 16.260 1.00 27.28 C ANISOU 1530 CE LYS D 80 3274 3656 3433 14 -48 -194 C ATOM 1531 NZ LYS A 80 40.656 -11.893 17.470 1.00 31.61 N ANISOU 1531 NZ LYS D 80 3584 4049 4377 -124 227 65 N ATOM 1532 N ALA A 81 41.426 -8.875 10.465 1.00 16.95 N ANISOU 1532 N ALA D 81 1331 2691 2417 25 -134 -241 N ATOM 1533 CA ALA A 81 42.205 -8.444 9.291 1.00 19.00 C ANISOU 1533 CA ALA D 81 1810 2782 2628 -28 -153 -224 C ATOM 1534 C ALA A 81 42.507 -6.927 9.310 1.00 21.35 C ANISOU 1534 C ALA D 81 2151 3015 2945 -68 -209 -279 C ATOM 1535 O ALA A 81 43.461 -6.444 8.617 1.00 23.28 O ANISOU 1535 O ALA D 81 2249 3333 3262 -137 -566 -469 O ATOM 1536 CB ALA A 81 41.525 -8.887 7.997 1.00 20.73 C ANISOU 1536 CB ALA D 81 2159 2977 2741 -126 -123 -199 C ATOM 1537 N LEU A 82 41.740 -6.179 10.074 1.00 20.87 N ANISOU 1537 N LEU D 82 2107 2884 2937 -108 -217 -255 N ATOM 1538 CA LEU A 82 41.925 -4.780 10.285 1.00 21.41 C ANISOU 1538 CA LEU D 82 2278 2808 3049 -59 -116 -265 C ATOM 1539 C LEU A 82 42.768 -4.509 11.519 1.00 21.03 C ANISOU 1539 C LEU D 82 2212 2711 3065 -110 -36 -195 C ATOM 1540 O LEU A 82 42.977 -3.359 11.949 1.00 22.33 O ANISOU 1540 O LEU D 82 2279 2609 3596 -100 130 -394 O ATOM 1541 CB LEU A 82 40.569 -4.119 10.422 1.00 22.70 C ANISOU 1541 CB LEU D 82 2375 2920 3329 -147 -236 -263 C ATOM 1542 CG LEU A 82 39.823 -4.002 9.124 1.00 24.24 C ANISOU 1542 CG LEU D 82 2673 3226 3310 -59 -312 -251 C ATOM 1543 CD1 LEU A 82 38.384 -3.485 9.346 1.00 24.29 C ANISOU 1543 CD1 LEU D 82 2427 3355 3446 166 -203 -363 C ATOM 1544 CD2 LEU A 82 40.605 -2.990 8.250 1.00 25.31 C ANISOU 1544 CD2 LEU D 82 2964 3611 3040 9 -309 -559 C ATOM 1545 N GLY A 83 43.306 -5.576 12.088 1.00 19.31 N ANISOU 1545 N GLY D 83 2013 2437 2885 -119 -126 -184 N ATOM 1546 CA GLY A 83 44.125 -5.465 13.295 1.00 19.96 C ANISOU 1546 CA GLY D 83 2213 2459 2911 -257 37 -67 C ATOM 1547 C GLY A 83 43.368 -5.076 14.542 1.00 18.65 C ANISOU 1547 C GLY D 83 2017 2304 2761 -231 96 -15 C ATOM 1548 O GLY A 83 43.932 -4.492 15.464 1.00 22.00 O ANISOU 1548 O GLY D 83 2250 2666 3442 -334 256 53 O ATOM 1549 N ILE A 84 42.057 -5.374 14.589 1.00 19.51 N ANISOU 1549 N ILE D 84 2076 2489 2846 -285 59 6 N ATOM 1550 CA ILE A 84 41.204 -5.050 15.714 1.00 18.92 C ANISOU 1550 CA ILE D 84 2111 2452 2623 -285 144 17 C ATOM 1551 C ILE A 84 40.718 -6.367 16.349 1.00 19.15 C ANISOU 1551 C ILE D 84 2241 2561 2471 -229 208 58 C ATOM 1552 O ILE A 84 40.312 -7.263 15.595 1.00 18.83 O ANISOU 1552 O ILE D 84 1996 2679 2479 -322 256 113 O ATOM 1553 CB ILE A 84 40.012 -4.173 15.231 1.00 19.55 C ANISOU 1553 CB ILE D 84 2206 2491 2729 -300 -33 19 C ATOM 1554 CG1 ILE A 84 40.516 -2.794 14.753 1.00 21.26 C ANISOU 1554 CG1 ILE D 84 2425 2582 3071 -243 -72 49 C ATOM 1555 CG2 ILE A 84 38.975 -4.023 16.324 1.00 20.71 C ANISOU 1555 CG2 ILE D 84 2053 2773 3041 -168 -170 175 C ATOM 1556 CD1 ILE A 84 39.537 -2.013 13.869 1.00 21.10 C ANISOU 1556 CD1 ILE D 84 2605 2202 3208 -360 50 -24 C ATOM 1557 N SER A 85 40.758 -6.494 17.697 1.00 18.16 N ANISOU 1557 N SER D 85 1853 2762 2285 -266 299 32 N ATOM 1558 CA ASER A 85 40.200 -7.629 18.414 0.70 18.16 C ANISOU 1558 CA ASER D 85 2013 2674 2213 -96 251 -21 C ATOM 1559 C SER A 85 38.720 -7.400 18.676 1.00 18.29 C ANISOU 1559 C SER D 85 2076 2577 2296 -71 178 -6 C ATOM 1560 O SER A 85 38.342 -6.528 19.411 1.00 20.88 O ANISOU 1560 O SER D 85 2211 3023 2699 -407 4 384 O ATOM 1561 CB ASER A 85 40.874 -7.828 19.808 0.70 18.12 C ANISOU 1561 CB ASER D 85 1825 2852 2204 -62 320 -68 C ATOM 1562 OG ASER A 85 40.532 -9.103 20.394 0.70 18.26 O ANISOU 1562 OG ASER D 85 1771 2925 2241 279 113 -306 O ATOM 1563 N PRO A 86 37.876 -8.235 18.140 1.00 15.04 N ANISOU 1563 N PRO D 86 1935 2081 1695 -160 168 -163 N ATOM 1564 CA PRO A 86 36.432 -8.004 18.362 1.00 14.81 C ANISOU 1564 CA PRO D 86 1872 1961 1790 -199 138 -156 C ATOM 1565 C PRO A 86 35.849 -8.947 19.405 1.00 13.92 C ANISOU 1565 C PRO D 86 1845 1698 1745 -248 224 -249 C ATOM 1566 O PRO A 86 36.521 -9.892 19.867 1.00 16.09 O ANISOU 1566 O PRO D 86 2002 2085 2023 27 252 -428 O ATOM 1567 CB PRO A 86 35.835 -8.435 17.058 1.00 17.40 C ANISOU 1567 CB PRO D 86 2167 2385 2057 -261 156 -139 C ATOM 1568 CG PRO A 86 36.665 -9.546 16.653 1.00 16.51 C ANISOU 1568 CG PRO D 86 2365 2066 1841 -249 173 168 C ATOM 1569 CD PRO A 86 38.106 -9.314 17.160 1.00 16.83 C ANISOU 1569 CD PRO D 86 2303 2189 1901 199 204 -182 C ATOM 1570 N PHE A 87 34.603 -8.688 19.773 1.00 11.96 N ANISOU 1570 N PHE D 87 1755 1382 1408 -218 334 -111 N ATOM 1571 CA PHE A 87 33.951 -9.454 20.815 1.00 11.79 C ANISOU 1571 CA PHE D 87 1739 1461 1280 -202 287 -111 C ATOM 1572 C PHE A 87 33.344 -10.754 20.323 1.00 11.72 C ANISOU 1572 C PHE D 87 1826 1272 1353 -110 227 -101 C ATOM 1573 O PHE A 87 33.456 -11.797 20.946 1.00 11.39 O ANISOU 1573 O PHE D 87 1844 1181 1300 -59 327 -254 O ATOM 1574 CB PHE A 87 32.819 -8.613 21.414 1.00 12.34 C ANISOU 1574 CB PHE D 87 1950 1384 1353 -138 340 -71 C ATOM 1575 CG PHE A 87 32.082 -9.301 22.490 1.00 12.82 C ANISOU 1575 CG PHE D 87 2181 1086 1604 -4 166 137 C ATOM 1576 CD1 PHE A 87 32.693 -9.497 23.699 1.00 14.52 C ANISOU 1576 CD1 PHE D 87 2444 1457 1617 -4 183 -5 C ATOM 1577 CD2 PHE A 87 30.799 -9.761 22.313 1.00 13.87 C ANISOU 1577 CD2 PHE D 87 2374 1268 1625 85 29 -171 C ATOM 1578 CE1 PHE A 87 32.006 -10.148 24.720 1.00 14.38 C ANISOU 1578 CE1 PHE D 87 2592 1427 1443 119 182 -85 C ATOM 1579 CE2 PHE A 87 30.132 -10.424 23.332 1.00 14.92 C ANISOU 1579 CE2 PHE D 87 2258 1364 2046 -92 -88 12 C ATOM 1580 CZ PHE A 87 30.762 -10.590 24.544 1.00 14.24 C ANISOU 1580 CZ PHE D 87 2285 1441 1685 222 -241 -271 C ATOM 1581 N HIS A 88 32.614 -10.682 19.212 1.00 10.71 N ANISOU 1581 N HIS D 88 1742 1138 1186 -281 192 -184 N ATOM 1582 CA HIS A 88 31.774 -11.808 18.793 1.00 10.85 C ANISOU 1582 CA HIS D 88 1617 1356 1148 -193 163 -132 C ATOM 1583 C HIS A 88 32.577 -12.778 17.943 1.00 10.53 C ANISOU 1583 C HIS D 88 1589 1423 989 -141 82 -200 C ATOM 1584 O HIS A 88 33.489 -12.425 17.225 1.00 12.05 O ANISOU 1584 O HIS D 88 1839 1373 1365 -222 -10 -121 O ATOM 1585 CB HIS A 88 30.531 -11.324 18.018 1.00 11.62 C ANISOU 1585 CB HIS D 88 1594 1435 1382 -229 173 -163 C ATOM 1586 CG HIS A 88 29.659 -10.372 18.753 1.00 11.53 C ANISOU 1586 CG HIS D 88 1636 1244 1499 -10 361 -134 C ATOM 1587 ND1 HIS A 88 29.770 -8.992 18.647 1.00 12.65 N ANISOU 1587 ND1 HIS D 88 1836 1215 1753 55 366 -284 N ATOM 1588 CD2 HIS A 88 28.661 -10.611 19.646 1.00 13.56 C ANISOU 1588 CD2 HIS D 88 1854 1284 2012 -25 162 -39 C ATOM 1589 CE1 HIS A 88 28.881 -8.439 19.458 1.00 14.00 C ANISOU 1589 CE1 HIS D 88 1784 1241 2291 -119 110 -496 C ATOM 1590 NE2 HIS A 88 28.191 -9.393 20.068 1.00 13.84 N ANISOU 1590 NE2 HIS D 88 1715 1164 2379 66 73 -230 N ATOM 1591 N GLU A 89 32.176 -14.049 18.010 1.00 10.73 N ANISOU 1591 N GLU D 89 1578 1364 1135 -92 33 -78 N ATOM 1592 CA GLU A 89 32.753 -15.046 17.100 1.00 11.80 C ANISOU 1592 CA GLU D 89 1554 1591 1337 -177 2 14 C ATOM 1593 C GLU A 89 32.225 -14.874 15.691 1.00 12.69 C ANISOU 1593 C GLU D 89 1727 1767 1327 -192 -135 120 C ATOM 1594 O GLU A 89 32.923 -15.136 14.711 1.00 15.90 O ANISOU 1594 O GLU D 89 1542 2685 1812 -272 -230 401 O ATOM 1595 CB GLU A 89 32.358 -16.461 17.563 1.00 13.31 C ANISOU 1595 CB GLU D 89 1852 1580 1622 -67 -95 163 C ATOM 1596 CG GLU A 89 33.065 -16.912 18.765 1.00 13.90 C ANISOU 1596 CG GLU D 89 1913 1598 1769 -2 -225 -23 C ATOM 1597 CD GLU A 89 34.550 -17.059 18.552 1.00 17.24 C ANISOU 1597 CD GLU D 89 2237 2255 2057 287 43 -275 C ATOM 1598 OE1 GLU A 89 34.972 -17.900 17.748 1.00 21.84 O ANISOU 1598 OE1 GLU D 89 2629 3021 2645 108 -73 374 O ATOM 1599 OE2 GLU A 89 35.282 -16.288 19.177 1.00 19.92 O ANISOU 1599 OE2 GLU D 89 2337 2472 2759 181 149 -450 O ATOM 1600 N HIS A 90 30.978 -14.475 15.565 1.00 11.89 N ANISOU 1600 N HIS D 90 1735 1616 1164 -62 93 116 N ATOM 1601 CA HIS A 90 30.309 -14.247 14.264 1.00 12.13 C ANISOU 1601 CA HIS D 90 1677 1699 1230 -266 160 222 C ATOM 1602 C HIS A 90 29.016 -13.546 14.596 1.00 12.39 C ANISOU 1602 C HIS D 90 1873 1645 1186 -121 39 143 C ATOM 1603 O HIS A 90 28.675 -13.424 15.754 1.00 15.01 O ANISOU 1603 O HIS D 90 2023 2486 1194 112 52 84 O ATOM 1604 CB HIS A 90 30.078 -15.539 13.460 1.00 15.76 C ANISOU 1604 CB HIS D 90 2275 2192 1521 -118 195 305 C ATOM 1605 CG HIS A 90 29.513 -16.660 14.219 1.00 19.89 C ANISOU 1605 CG HIS D 90 2762 2381 2413 -203 378 336 C ATOM 1606 ND1 HIS A 90 30.238 -17.795 14.502 1.00 25.87 N ANISOU 1606 ND1 HIS D 90 3958 2697 3174 -151 211 -23 N ATOM 1607 CD2 HIS A 90 28.283 -16.848 14.729 1.00 26.97 C ANISOU 1607 CD2 HIS D 90 3663 3153 3429 -88 -192 -22 C ATOM 1608 CE1 HIS A 90 29.469 -18.627 15.188 1.00 25.50 C ANISOU 1608 CE1 HIS D 90 3708 2359 3620 -286 -39 72 C ATOM 1609 NE2 HIS A 90 28.269 -18.091 15.305 1.00 27.78 N ANISOU 1609 NE2 HIS D 90 4214 3059 3280 -90 -502 76 N ATOM 1610 N ALA A 91 28.319 -13.052 13.584 1.00 12.56 N ANISOU 1610 N ALA D 91 1771 2020 980 -96 172 157 N ATOM 1611 CA ALA A 91 26.979 -12.583 13.732 1.00 13.20 C ANISOU 1611 CA ALA D 91 1857 2137 1021 -216 207 438 C ATOM 1612 C ALA A 91 26.091 -13.615 12.974 1.00 12.61 C ANISOU 1612 C ALA D 91 1823 2188 779 -226 298 372 C ATOM 1613 O ALA A 91 26.377 -14.029 11.906 1.00 20.28 O ANISOU 1613 O ALA D 91 2386 3035 2282 -434 -235 236 O ATOM 1614 CB ALA A 91 26.814 -11.218 13.087 1.00 15.24 C ANISOU 1614 CB ALA D 91 2084 2217 1487 56 297 289 C ATOM 1615 N GLU A 92 25.005 -13.945 13.638 1.00 16.31 N ANISOU 1615 N GLU D 92 1852 2740 1604 -230 163 392 N ATOM 1616 CA GLU A 92 24.040 -14.935 13.138 1.00 16.37 C ANISOU 1616 CA GLU D 92 1895 2600 1725 -84 116 231 C ATOM 1617 C GLU A 92 22.672 -14.295 13.023 1.00 15.43 C ANISOU 1617 C GLU D 92 1577 2459 1826 -12 43 475 C ATOM 1618 O GLU A 92 22.257 -13.531 13.912 1.00 17.99 O ANISOU 1618 O GLU D 92 1847 3533 1454 124 229 828 O ATOM 1619 CB GLU A 92 23.866 -16.034 14.211 1.00 19.89 C ANISOU 1619 CB GLU D 92 2223 2827 2505 -9 9 -8 C ATOM 1620 CG GLU A 92 25.065 -16.817 14.574 1.00 25.38 C ANISOU 1620 CG GLU D 92 3278 3255 3109 44 30 -372 C ATOM 1621 CD GLU A 92 24.673 -18.222 15.058 1.00 25.61 C ANISOU 1621 CD GLU D 92 3217 3275 3238 -270 111 -39 C ATOM 1622 OE1 GLU A 92 23.481 -18.608 14.873 1.00 39.14 O ANISOU 1622 OE1 GLU D 92 4200 5319 5351 -194 107 -60 O ATOM 1623 OE2 GLU A 92 25.536 -18.932 15.604 1.00 36.86 O ANISOU 1623 OE2 GLU D 92 4403 4580 5020 145 46 -363 O ATOM 1624 N VAL A 93 21.998 -14.520 11.908 1.00 11.63 N ANISOU 1624 N VAL D 93 1401 1682 1334 -2 63 433 N ATOM 1625 CA VAL A 93 20.662 -14.011 11.670 1.00 11.09 C ANISOU 1625 CA VAL D 93 1322 1576 1315 -45 -83 299 C ATOM 1626 C VAL A 93 19.789 -15.200 11.285 1.00 9.59 C ANISOU 1626 C VAL D 93 1249 1342 1053 -39 -85 321 C ATOM 1627 O VAL A 93 20.066 -15.857 10.279 1.00 12.43 O ANISOU 1627 O VAL D 93 1549 1875 1296 -126 -155 658 O ATOM 1628 CB VAL A 93 20.662 -12.926 10.550 1.00 11.97 C ANISOU 1628 CB VAL D 93 1503 1616 1428 24 -129 282 C ATOM 1629 CG1 VAL A 93 19.287 -12.384 10.379 1.00 15.08 C ANISOU 1629 CG1 VAL D 93 1651 1968 2111 202 -185 79 C ATOM 1630 CG2 VAL A 93 21.724 -11.852 10.835 1.00 14.55 C ANISOU 1630 CG2 VAL D 93 1787 1771 1969 -291 -100 274 C ATOM 1631 N VAL A 94 18.774 -15.479 12.094 1.00 9.72 N ANISOU 1631 N VAL D 94 1283 1288 1121 21 -31 313 N ATOM 1632 CA VAL A 94 17.939 -16.675 11.945 1.00 10.46 C ANISOU 1632 CA VAL D 94 1354 1447 1172 22 156 136 C ATOM 1633 C VAL A 94 16.508 -16.220 11.738 1.00 10.40 C ANISOU 1633 C VAL D 94 1262 1433 1257 -65 48 211 C ATOM 1634 O VAL A 94 15.984 -15.456 12.538 1.00 10.61 O ANISOU 1634 O VAL D 94 1321 1517 1191 36 -78 377 O ATOM 1635 CB VAL A 94 18.044 -17.627 13.152 1.00 11.40 C ANISOU 1635 CB VAL D 94 1356 1657 1317 -34 147 -71 C ATOM 1636 CG1 VAL A 94 17.235 -18.870 12.887 1.00 13.52 C ANISOU 1636 CG1 VAL D 94 1761 1661 1713 -189 -93 24 C ATOM 1637 CG2 VAL A 94 19.518 -17.938 13.469 1.00 15.04 C ANISOU 1637 CG2 VAL D 94 1574 1890 2250 177 94 -143 C ATOM 1638 N PHE A 95 15.875 -16.719 10.687 1.00 10.81 N ANISOU 1638 N PHE D 95 1369 1506 1232 -99 -36 218 N ATOM 1639 CA PHE A 95 14.538 -16.219 10.288 1.00 11.08 C ANISOU 1639 CA PHE D 95 1317 1581 1311 20 50 271 C ATOM 1640 C PHE A 95 13.799 -17.260 9.485 1.00 11.93 C ANISOU 1640 C PHE D 95 1335 1741 1454 -65 69 222 C ATOM 1641 O PHE A 95 14.398 -18.183 8.938 1.00 12.29 O ANISOU 1641 O PHE D 95 1428 1643 1599 -73 220 388 O ATOM 1642 CB PHE A 95 14.656 -14.941 9.475 1.00 12.75 C ANISOU 1642 CB PHE D 95 1575 1737 1531 115 80 277 C ATOM 1643 CG PHE A 95 15.344 -15.108 8.163 1.00 12.04 C ANISOU 1643 CG PHE D 95 1612 1636 1328 53 138 72 C ATOM 1644 CD1 PHE A 95 16.699 -15.086 8.040 1.00 12.92 C ANISOU 1644 CD1 PHE D 95 1794 1711 1403 149 -25 201 C ATOM 1645 CD2 PHE A 95 14.596 -15.267 7.005 1.00 14.71 C ANISOU 1645 CD2 PHE D 95 2097 2020 1471 221 -43 219 C ATOM 1646 CE1 PHE A 95 17.299 -15.247 6.776 1.00 14.96 C ANISOU 1646 CE1 PHE D 95 1668 1915 2098 150 -150 -87 C ATOM 1647 CE2 PHE A 95 15.185 -15.460 5.772 1.00 15.82 C ANISOU 1647 CE2 PHE D 95 2463 2004 1542 -108 12 210 C ATOM 1648 CZ PHE A 95 16.539 -15.420 5.686 1.00 16.03 C ANISOU 1648 CZ PHE D 95 2460 2129 1503 -52 -455 -87 C ATOM 1649 N THR A 96 12.487 -17.092 9.416 1.00 14.15 N ANISOU 1649 N THR D 96 1389 2212 1772 28 77 542 N ATOM 1650 CA THR A 96 11.652 -17.908 8.541 1.00 14.29 C ANISOU 1650 CA THR D 96 1555 2127 1744 -2 135 300 C ATOM 1651 C THR A 96 11.314 -17.192 7.247 1.00 14.72 C ANISOU 1651 C THR D 96 1649 2107 1834 81 164 310 C ATOM 1652 O THR A 96 10.886 -16.050 7.275 1.00 17.41 O ANISOU 1652 O THR D 96 2303 2352 1957 327 384 510 O ATOM 1653 CB THR A 96 10.354 -18.340 9.276 1.00 14.51 C ANISOU 1653 CB THR D 96 1345 2235 1933 -104 327 356 C ATOM 1654 OG1 THR A 96 10.661 -19.095 10.426 1.00 16.73 O ANISOU 1654 OG1 THR D 96 1712 2997 1645 -237 19 269 O ATOM 1655 CG2 THR A 96 9.470 -19.211 8.359 1.00 16.36 C ANISOU 1655 CG2 THR D 96 1482 2866 1867 -491 427 539 C ATOM 1656 N ALA A 97 11.579 -17.851 6.126 1.00 14.16 N ANISOU 1656 N ALA D 97 1680 1924 1777 93 254 360 N ATOM 1657 CA ALA A 97 11.096 -17.376 4.831 1.00 15.72 C ANISOU 1657 CA ALA D 97 1874 2107 1992 -52 256 312 C ATOM 1658 C ALA A 97 9.628 -17.786 4.709 1.00 16.21 C ANISOU 1658 C ALA D 97 1976 2111 2070 -85 371 460 C ATOM 1659 O ALA A 97 9.285 -18.944 4.963 1.00 15.12 O ANISOU 1659 O ALA D 97 2022 2038 1685 85 520 400 O ATOM 1660 CB ALA A 97 11.881 -17.963 3.661 1.00 16.49 C ANISOU 1660 CB ALA D 97 2109 2128 2026 -136 73 265 C ATOM 1661 N ASN A 98 8.793 -16.819 4.333 1.00 18.10 N ANISOU 1661 N ASN D 98 2291 2226 2356 -25 336 446 N ATOM 1662 CA AASN A 98 7.350 -16.944 4.315 0.50 19.72 C ANISOU 1662 CA AASN D 98 2383 2523 2586 28 229 306 C ATOM 1663 C ASN A 98 6.837 -16.499 2.959 1.00 20.08 C ANISOU 1663 C ASN D 98 2384 2612 2633 5 330 263 C ATOM 1664 O ASN A 98 7.064 -15.387 2.579 1.00 21.10 O ANISOU 1664 O ASN D 98 2373 2784 2859 -268 848 389 O ATOM 1665 CB AASN A 98 6.785 -16.010 5.391 0.50 21.36 C ANISOU 1665 CB AASN D 98 2594 2734 2785 135 186 315 C ATOM 1666 CG AASN A 98 5.278 -16.037 5.468 0.50 21.76 C ANISOU 1666 CG AASN D 98 2544 2811 2913 43 89 360 C ATOM 1667 OD1AASN A 98 4.604 -16.990 5.049 0.50 22.58 O ANISOU 1667 OD1AASN D 98 2136 3433 3008 74 67 411 O ATOM 1668 ND2AASN A 98 4.730 -14.976 6.048 0.50 25.56 N ANISOU 1668 ND2AASN D 98 3351 2999 3359 318 -143 459 N ATOM 1669 N ASP A 99 6.148 -17.364 2.212 1.00 19.75 N ANISOU 1669 N ASP D 99 2412 2451 2641 51 367 329 N ATOM 1670 CA ASP A 99 5.617 -16.983 0.881 1.00 21.52 C ANISOU 1670 CA ASP D 99 2712 2675 2789 -43 295 261 C ATOM 1671 C ASP A 99 4.517 -15.923 0.892 1.00 24.27 C ANISOU 1671 C ASP D 99 2977 3073 3171 -73 367 206 C ATOM 1672 O ASP A 99 4.368 -15.197 -0.073 1.00 27.45 O ANISOU 1672 O ASP D 99 3557 3184 3686 -1 492 315 O ATOM 1673 CB ASP A 99 5.214 -18.256 0.098 1.00 18.69 C ANISOU 1673 CB ASP D 99 2112 2414 2575 -70 426 346 C ATOM 1674 CG ASP A 99 6.400 -18.998 -0.449 1.00 19.51 C ANISOU 1674 CG ASP D 99 2471 2416 2526 -172 419 525 C ATOM 1675 OD1 ASP A 99 7.562 -18.520 -0.338 1.00 23.39 O ANISOU 1675 OD1 ASP D 99 2608 2716 3562 18 78 269 O ATOM 1676 OD2 ASP A 99 6.187 -20.123 -0.933 1.00 18.61 O ANISOU 1676 OD2 ASP D 99 2341 2216 2512 -325 188 505 O ATOM 1677 N SER A 100 3.797 -15.810 1.985 1.00 27.53 N ANISOU 1677 N SER D 100 3223 3558 3677 156 332 186 N ATOM 1678 CA SER A 100 2.728 -14.805 2.101 1.00 29.50 C ANISOU 1678 CA SER D 100 3594 3648 3965 114 154 137 C ATOM 1679 C SER A 100 3.324 -13.404 1.950 1.00 31.98 C ANISOU 1679 C SER D 100 3948 3885 4317 65 215 54 C ATOM 1680 O SER A 100 2.836 -12.556 1.158 1.00 35.43 O ANISOU 1680 O SER D 100 4355 4200 4906 21 231 -88 O ATOM 1681 CB SER A 100 2.039 -14.951 3.460 1.00 31.09 C ANISOU 1681 CB SER D 100 3840 3899 4072 130 106 129 C ATOM 1682 OG SER A 100 1.710 -16.308 3.763 1.00 34.51 O ANISOU 1682 OG SER D 100 4134 4365 4612 -51 92 107 O ATOM 1683 N GLY A 101 4.417 -13.176 2.664 1.00 31.80 N ANISOU 1683 N GLY D 101 3992 3823 4267 6 145 133 N ATOM 1684 CA GLY A 101 5.063 -11.842 2.683 1.00 31.12 C ANISOU 1684 CA GLY D 101 3990 3793 4041 -11 87 197 C ATOM 1685 C GLY A 101 5.732 -11.494 1.363 1.00 31.55 C ANISOU 1685 C GLY D 101 4081 3871 4035 -6 9 274 C ATOM 1686 O GLY A 101 5.681 -12.284 0.395 1.00 32.22 O ANISOU 1686 O GLY D 101 4201 4074 3965 25 46 467 O ATOM 1687 N PRO A 102 6.315 -10.291 1.268 1.00 29.74 N ANISOU 1687 N PRO D 102 3911 3714 3674 0 76 377 N ATOM 1688 CA PRO A 102 7.009 -9.863 0.075 1.00 29.12 C ANISOU 1688 CA PRO D 102 3703 3662 3700 29 106 260 C ATOM 1689 C PRO A 102 8.166 -10.827 -0.273 1.00 28.30 C ANISOU 1689 C PRO D 102 3646 3613 3493 34 104 214 C ATOM 1690 O PRO A 102 8.632 -11.617 0.588 1.00 29.46 O ANISOU 1690 O PRO D 102 3810 3588 3793 106 176 279 O ATOM 1691 CB PRO A 102 7.458 -8.427 0.395 1.00 29.46 C ANISOU 1691 CB PRO D 102 3810 3739 3644 28 82 259 C ATOM 1692 CG PRO A 102 6.579 -7.973 1.509 1.00 29.98 C ANISOU 1692 CG PRO D 102 3927 3791 3673 71 34 264 C ATOM 1693 CD PRO A 102 6.269 -9.222 2.299 1.00 29.84 C ANISOU 1693 CD PRO D 102 4018 3653 3666 24 -30 417 C ATOM 1694 N ARG A 103 8.610 -10.742 -1.522 1.00 27.20 N ANISOU 1694 N ARG D 103 3416 3597 3322 -14 225 250 N ATOM 1695 CA AARG A 103 9.405 -11.747 -2.229 0.50 26.71 C ANISOU 1695 CA AARG D 103 3481 3457 3209 -8 152 198 C ATOM 1696 C ARG A 103 10.902 -11.580 -2.114 1.00 26.10 C ANISOU 1696 C ARG D 103 3429 3364 3124 20 161 222 C ATOM 1697 O ARG A 103 11.650 -12.505 -2.432 1.00 28.08 O ANISOU 1697 O ARG D 103 3852 3411 3405 53 17 303 O ATOM 1698 CB AARG A 103 9.133 -11.713 -3.760 0.50 26.49 C ANISOU 1698 CB AARG D 103 3465 3403 3196 -76 168 180 C ATOM 1699 CG AARG A 103 7.728 -11.406 -4.246 0.50 28.31 C ANISOU 1699 CG AARG D 103 3622 3574 3559 10 42 9 C ATOM 1700 CD AARG A 103 6.656 -12.409 -3.844 0.50 28.09 C ANISOU 1700 CD AARG D 103 3619 3593 3460 17 12 41 C ATOM 1701 NE AARG A 103 5.326 -11.802 -3.916 0.50 27.87 N ANISOU 1701 NE AARG D 103 3588 3530 3471 25 257 91 N ATOM 1702 CZ AARG A 103 4.690 -11.510 -5.051 0.50 28.42 C ANISOU 1702 CZ AARG D 103 3605 3624 3568 14 55 17 C ATOM 1703 NH1AARG A 103 5.222 -11.781 -6.233 0.50 29.03 N ANISOU 1703 NH1AARG D 103 3711 3811 3505 8 49 -150 N ATOM 1704 NH2AARG A 103 3.505 -10.947 -5.006 0.50 27.70 N ANISOU 1704 NH2AARG D 103 3528 3392 3604 -11 42 13 N ATOM 1705 N ARG A 104 11.370 -10.367 -1.788 1.00 22.83 N ANISOU 1705 N ARG D 104 3109 3037 2526 148 298 385 N ATOM 1706 CA ARG A 104 12.796 -10.159 -1.754 1.00 22.22 C ANISOU 1706 CA ARG D 104 3079 3049 2315 59 277 436 C ATOM 1707 C ARG A 104 13.225 -9.799 -0.330 1.00 19.15 C ANISOU 1707 C ARG D 104 2788 2740 1748 313 344 464 C ATOM 1708 O ARG A 104 12.653 -8.919 0.290 1.00 19.01 O ANISOU 1708 O ARG D 104 2667 2845 1709 582 483 430 O ATOM 1709 CB ARG A 104 13.212 -9.062 -2.712 1.00 23.11 C ANISOU 1709 CB ARG D 104 3175 3280 2323 32 228 380 C ATOM 1710 CG ARG A 104 12.712 -9.154 -4.151 1.00 28.95 C ANISOU 1710 CG ARG D 104 3804 3933 3259 -3 226 239 C ATOM 1711 CD ARG A 104 13.202 -7.876 -4.799 1.00 31.65 C ANISOU 1711 CD ARG D 104 4209 4123 3691 -85 59 98 C ATOM 1712 NE ARG A 104 12.425 -7.377 -5.930 1.00 38.62 N ANISOU 1712 NE ARG D 104 5113 4833 4727 -37 250 -256 N ATOM 1713 CZ ARG A 104 12.693 -6.224 -6.555 1.00 38.73 C ANISOU 1713 CZ ARG D 104 5158 4779 4777 -58 127 -177 C ATOM 1714 NH1 ARG A 104 13.711 -5.456 -6.145 1.00 41.59 N ANISOU 1714 NH1 ARG D 104 5257 5298 5245 -167 192 -44 N ATOM 1715 NH2 ARG A 104 11.953 -5.834 -7.598 1.00 40.67 N ANISOU 1715 NH2 ARG D 104 5259 5124 5070 -61 237 -119 N ATOM 1716 N TYR A 105 14.252 -10.485 0.118 1.00 16.68 N ANISOU 1716 N TYR D 105 2517 2396 1424 238 434 583 N ATOM 1717 CA TYR A 105 14.755 -10.314 1.482 1.00 16.44 C ANISOU 1717 CA TYR D 105 2256 2335 1653 182 191 375 C ATOM 1718 C TYR A 105 16.158 -9.747 1.392 1.00 14.72 C ANISOU 1718 C TYR D 105 2093 2076 1423 220 108 422 C ATOM 1719 O TYR A 105 17.016 -10.333 0.773 1.00 17.68 O ANISOU 1719 O TYR D 105 2077 2636 2003 284 -111 556 O ATOM 1720 CB TYR A 105 14.836 -11.665 2.192 1.00 17.20 C ANISOU 1720 CB TYR D 105 2155 2464 1916 205 90 211 C ATOM 1721 CG TYR A 105 13.554 -12.407 2.370 1.00 17.35 C ANISOU 1721 CG TYR D 105 2125 2319 2148 135 216 221 C ATOM 1722 CD1 TYR A 105 12.960 -13.045 1.280 1.00 20.88 C ANISOU 1722 CD1 TYR D 105 2667 2985 2278 47 214 405 C ATOM 1723 CD2 TYR A 105 12.923 -12.503 3.590 1.00 20.63 C ANISOU 1723 CD2 TYR D 105 2479 3165 2193 -146 367 4 C ATOM 1724 CE1 TYR A 105 11.791 -13.761 1.432 1.00 22.79 C ANISOU 1724 CE1 TYR D 105 2879 3066 2711 -155 21 65 C ATOM 1725 CE2 TYR A 105 11.713 -13.269 3.743 1.00 19.26 C ANISOU 1725 CE2 TYR D 105 2619 2632 2065 -14 -252 225 C ATOM 1726 CZ TYR A 105 11.166 -13.859 2.670 1.00 21.42 C ANISOU 1726 CZ TYR D 105 2308 3015 2815 69 180 -125 C ATOM 1727 OH TYR A 105 10.023 -14.616 2.820 1.00 22.65 O ANISOU 1727 OH TYR D 105 2385 2874 3346 64 138 -214 O ATOM 1728 N THR A 106 16.383 -8.606 2.043 1.00 14.18 N ANISOU 1728 N THR D 106 2126 2105 1156 254 199 323 N ATOM 1729 CA THR A 106 17.691 -8.102 2.249 1.00 13.99 C ANISOU 1729 CA THR D 106 2143 2016 1155 155 114 245 C ATOM 1730 C THR A 106 17.941 -8.239 3.745 1.00 12.93 C ANISOU 1730 C THR D 106 1957 1913 1040 182 145 265 C ATOM 1731 O THR A 106 17.224 -7.699 4.582 1.00 15.05 O ANISOU 1731 O THR D 106 2135 2247 1335 500 227 280 O ATOM 1732 CB THR A 106 17.818 -6.638 1.833 1.00 15.53 C ANISOU 1732 CB THR D 106 2296 2232 1372 281 185 144 C ATOM 1733 OG1 THR A 106 17.631 -6.559 0.427 1.00 19.16 O ANISOU 1733 OG1 THR D 106 3068 2645 1564 371 291 10 O ATOM 1734 CG2 THR A 106 19.169 -6.069 2.225 1.00 17.10 C ANISOU 1734 CG2 THR D 106 2453 2218 1823 61 30 196 C ATOM 1735 N ILE A 107 19.011 -8.921 4.071 1.00 13.03 N ANISOU 1735 N ILE D 107 1945 1970 1032 228 228 314 N ATOM 1736 CA ILE A 107 19.528 -9.036 5.453 1.00 12.59 C ANISOU 1736 CA ILE D 107 1774 1907 1100 39 70 243 C ATOM 1737 C ILE A 107 20.702 -8.071 5.528 1.00 13.04 C ANISOU 1737 C ILE D 107 1866 1921 1166 50 42 157 C ATOM 1738 O ILE A 107 21.726 -8.278 4.896 1.00 14.26 O ANISOU 1738 O ILE D 107 1881 2303 1235 -65 -23 324 O ATOM 1739 CB ILE A 107 19.940 -10.484 5.772 1.00 12.76 C ANISOU 1739 CB ILE D 107 1731 2037 1081 157 1 214 C ATOM 1740 CG1 ILE A 107 18.758 -11.461 5.523 1.00 14.84 C ANISOU 1740 CG1 ILE D 107 2270 1899 1467 31 -67 6 C ATOM 1741 CG2 ILE A 107 20.577 -10.566 7.144 1.00 14.44 C ANISOU 1741 CG2 ILE D 107 1978 2187 1322 123 92 69 C ATOM 1742 CD1 ILE A 107 17.535 -11.255 6.394 1.00 17.48 C ANISOU 1742 CD1 ILE D 107 2412 2410 1818 59 -252 27 C ATOM 1743 N ALA A 108 20.529 -7.005 6.280 1.00 12.66 N ANISOU 1743 N ALA D 108 1953 1906 950 3 108 213 N ATOM 1744 CA ALA A 108 21.555 -6.012 6.474 1.00 13.07 C ANISOU 1744 CA ALA D 108 2013 1883 1067 -12 -50 138 C ATOM 1745 C ALA A 108 22.183 -6.151 7.857 1.00 12.97 C ANISOU 1745 C ALA D 108 1940 1869 1116 -7 -25 151 C ATOM 1746 O ALA A 108 21.468 -6.428 8.795 1.00 12.96 O ANISOU 1746 O ALA D 108 1756 2074 1092 -179 -108 132 O ATOM 1747 CB ALA A 108 20.967 -4.623 6.313 1.00 14.94 C ANISOU 1747 CB ALA D 108 2367 1966 1343 140 -100 75 C ATOM 1748 N ALA A 109 23.475 -5.947 7.972 1.00 12.56 N ANISOU 1748 N ALA D 109 1963 1839 968 -211 -151 116 N ATOM 1749 CA ALA A 109 24.195 -5.944 9.251 1.00 11.72 C ANISOU 1749 CA ALA D 109 1725 1657 1070 -150 -80 -8 C ATOM 1750 C ALA A 109 25.124 -4.751 9.346 1.00 11.48 C ANISOU 1750 C ALA D 109 1743 1633 987 -240 -20 -77 C ATOM 1751 O ALA A 109 25.800 -4.426 8.351 1.00 13.13 O ANISOU 1751 O ALA D 109 2064 2009 916 -418 -456 5 O ATOM 1752 CB ALA A 109 24.985 -7.201 9.447 1.00 13.81 C ANISOU 1752 CB ALA D 109 2098 1734 1414 -81 -133 -73 C ATOM 1753 N LEU A 110 25.180 -4.126 10.505 1.00 10.63 N ANISOU 1753 N LEU D 110 1573 1442 1024 29 97 -136 N ATOM 1754 CA LEU A 110 26.040 -2.991 10.770 1.00 10.74 C ANISOU 1754 CA LEU D 110 1621 1385 1074 157 62 -107 C ATOM 1755 C LEU A 110 26.979 -3.382 11.895 1.00 10.81 C ANISOU 1755 C LEU D 110 1458 1595 1054 93 35 -103 C ATOM 1756 O LEU A 110 26.502 -3.717 12.980 1.00 11.28 O ANISOU 1756 O LEU D 110 1513 1790 981 118 -36 -181 O ATOM 1757 CB LEU A 110 25.162 -1.804 11.181 1.00 10.58 C ANISOU 1757 CB LEU D 110 1575 1465 978 157 32 -8 C ATOM 1758 CG LEU A 110 25.932 -0.526 11.612 1.00 11.97 C ANISOU 1758 CG LEU D 110 1779 1285 1483 199 199 -60 C ATOM 1759 CD1 LEU A 110 26.748 0.034 10.432 1.00 13.32 C ANISOU 1759 CD1 LEU D 110 1860 1454 1746 -191 277 -301 C ATOM 1760 CD2 LEU A 110 24.936 0.513 12.184 1.00 15.36 C ANISOU 1760 CD2 LEU D 110 2048 1860 1927 479 38 348 C ATOM 1761 N LEU A 111 28.296 -3.399 11.620 1.00 9.93 N ANISOU 1761 N LEU D 111 1398 1480 892 117 43 -228 N ATOM 1762 CA LEU A 111 29.277 -3.987 12.486 1.00 10.25 C ANISOU 1762 CA LEU D 111 1440 1380 1073 51 15 -300 C ATOM 1763 C LEU A 111 30.126 -2.947 13.232 1.00 10.10 C ANISOU 1763 C LEU D 111 1418 1292 1128 210 90 -239 C ATOM 1764 O LEU A 111 30.675 -2.022 12.642 1.00 9.86 O ANISOU 1764 O LEU D 111 1385 1314 1045 200 -165 -300 O ATOM 1765 CB LEU A 111 30.212 -4.864 11.696 1.00 9.54 C ANISOU 1765 CB LEU D 111 1369 1243 1010 93 41 -388 C ATOM 1766 CG LEU A 111 29.613 -5.909 10.817 1.00 11.02 C ANISOU 1766 CG LEU D 111 1495 1445 1246 197 -13 -232 C ATOM 1767 CD1 LEU A 111 30.759 -6.745 10.177 1.00 13.01 C ANISOU 1767 CD1 LEU D 111 1630 1749 1565 125 -474 68 C ATOM 1768 CD2 LEU A 111 28.597 -6.780 11.545 1.00 10.58 C ANISOU 1768 CD2 LEU D 111 1247 1470 1301 25 -111 -179 C ATOM 1769 N SER A 112 30.279 -3.179 14.535 1.00 11.12 N ANISOU 1769 N SER D 112 1696 1500 1028 -59 -16 -154 N ATOM 1770 CA SER A 112 31.300 -2.562 15.370 1.00 9.95 C ANISOU 1770 CA SER D 112 1412 1328 1040 192 18 -218 C ATOM 1771 C SER A 112 32.027 -3.659 16.146 1.00 9.47 C ANISOU 1771 C SER D 112 1311 1306 980 95 67 -123 C ATOM 1772 O SER A 112 31.513 -4.758 16.271 1.00 10.24 O ANISOU 1772 O SER D 112 1379 1356 1153 -55 130 -129 O ATOM 1773 CB SER A 112 30.682 -1.557 16.352 1.00 11.83 C ANISOU 1773 CB SER D 112 1729 1647 1116 263 55 -265 C ATOM 1774 OG SER A 112 29.958 -0.518 15.687 1.00 12.59 O ANISOU 1774 OG SER D 112 1988 1510 1284 583 -6 -189 O ATOM 1775 N PRO A 113 33.200 -3.347 16.742 1.00 9.91 N ANISOU 1775 N PRO D 113 1477 1102 1185 55 56 -78 N ATOM 1776 CA PRO A 113 33.915 -4.434 17.413 1.00 10.28 C ANISOU 1776 CA PRO D 113 1472 1214 1221 148 43 -115 C ATOM 1777 C PRO A 113 33.149 -5.165 18.516 1.00 11.06 C ANISOU 1777 C PRO D 113 1624 1262 1316 86 202 -98 C ATOM 1778 O PRO A 113 33.303 -6.385 18.654 1.00 10.96 O ANISOU 1778 O PRO D 113 1824 1058 1281 215 184 -79 O ATOM 1779 CB PRO A 113 35.217 -3.776 17.865 1.00 11.28 C ANISOU 1779 CB PRO D 113 1401 1396 1489 326 16 -209 C ATOM 1780 CG PRO A 113 35.436 -2.723 16.797 1.00 11.47 C ANISOU 1780 CG PRO D 113 1476 1392 1488 -213 24 -174 C ATOM 1781 CD PRO A 113 34.064 -2.200 16.485 1.00 11.46 C ANISOU 1781 CD PRO D 113 1814 1363 1176 -44 30 -196 C ATOM 1782 N TYR A 114 32.368 -4.425 19.312 1.00 9.63 N ANISOU 1782 N TYR D 114 1417 1161 1080 89 75 -245 N ATOM 1783 CA TYR A 114 31.608 -4.983 20.451 1.00 10.26 C ANISOU 1783 CA TYR D 114 1458 1181 1256 -32 7 -178 C ATOM 1784 C TYR A 114 30.118 -4.914 20.255 1.00 10.35 C ANISOU 1784 C TYR D 114 1437 1352 1141 -76 104 -167 C ATOM 1785 O TYR A 114 29.364 -5.110 21.189 1.00 11.86 O ANISOU 1785 O TYR D 114 1402 1947 1155 -78 70 -577 O ATOM 1786 CB TYR A 114 32.032 -4.332 21.773 1.00 10.71 C ANISOU 1786 CB TYR D 114 1488 1276 1304 125 196 -161 C ATOM 1787 CG TYR A 114 33.345 -4.844 22.312 1.00 10.23 C ANISOU 1787 CG TYR D 114 1500 1240 1145 33 388 -197 C ATOM 1788 CD1 TYR A 114 34.525 -4.452 21.733 1.00 15.39 C ANISOU 1788 CD1 TYR D 114 1551 2611 1683 229 283 -388 C ATOM 1789 CD2 TYR A 114 33.425 -5.689 23.391 1.00 9.91 C ANISOU 1789 CD2 TYR D 114 1455 986 1325 268 93 69 C ATOM 1790 CE1 TYR A 114 35.739 -4.866 22.235 1.00 18.90 C ANISOU 1790 CE1 TYR D 114 1843 3170 2167 46 141 -278 C ATOM 1791 CE2 TYR A 114 34.627 -6.189 23.860 1.00 13.28 C ANISOU 1791 CE2 TYR D 114 1753 1782 1508 290 393 100 C ATOM 1792 CZ TYR A 114 35.786 -5.721 23.274 1.00 17.40 C ANISOU 1792 CZ TYR D 114 1844 2483 2282 211 165 -190 C ATOM 1793 OH TYR A 114 37.014 -6.116 23.714 1.00 20.67 O ANISOU 1793 OH TYR D 114 1877 3526 2450 318 411 -321 O ATOM 1794 N SER A 115 29.644 -4.661 19.051 1.00 11.24 N ANISOU 1794 N SER D 115 1441 1627 1200 -63 37 -350 N ATOM 1795 CA SER A 115 28.222 -4.536 18.821 1.00 10.76 C ANISOU 1795 CA SER D 115 1332 1594 1163 -27 72 -216 C ATOM 1796 C SER A 115 27.881 -4.779 17.370 1.00 10.74 C ANISOU 1796 C SER D 115 1256 1595 1229 -12 94 -392 C ATOM 1797 O SER A 115 28.676 -4.445 16.496 1.00 12.46 O ANISOU 1797 O SER D 115 1214 2238 1282 -42 -11 -583 O ATOM 1798 CB SER A 115 27.799 -3.102 19.158 1.00 12.09 C ANISOU 1798 CB SER D 115 1667 1692 1233 -130 161 -242 C ATOM 1799 OG SER A 115 26.460 -2.838 19.046 1.00 15.48 O ANISOU 1799 OG SER D 115 2144 1743 1995 203 49 -423 O ATOM 1800 N TYR A 116 26.676 -5.270 17.106 1.00 10.23 N ANISOU 1800 N TYR D 116 1167 1701 1018 66 193 -366 N ATOM 1801 CA TYR A 116 26.141 -5.272 15.761 1.00 10.54 C ANISOU 1801 CA TYR D 116 1304 1667 1033 84 146 -115 C ATOM 1802 C TYR A 116 24.639 -5.152 15.793 1.00 9.98 C ANISOU 1802 C TYR D 116 1262 1597 932 56 73 -113 C ATOM 1803 O TYR A 116 23.990 -5.502 16.756 1.00 11.13 O ANISOU 1803 O TYR D 116 1329 1920 978 64 -3 -119 O ATOM 1804 CB TYR A 116 26.611 -6.463 14.950 1.00 12.27 C ANISOU 1804 CB TYR D 116 1564 1972 1125 110 68 -124 C ATOM 1805 CG TYR A 116 26.066 -7.788 15.413 1.00 12.30 C ANISOU 1805 CG TYR D 116 1819 1670 1184 245 84 -8 C ATOM 1806 CD1 TYR A 116 24.837 -8.269 15.022 1.00 12.50 C ANISOU 1806 CD1 TYR D 116 1931 1572 1246 228 -189 139 C ATOM 1807 CD2 TYR A 116 26.844 -8.578 16.251 1.00 13.51 C ANISOU 1807 CD2 TYR D 116 1753 2072 1306 511 2 -55 C ATOM 1808 CE1 TYR A 116 24.389 -9.506 15.484 1.00 15.44 C ANISOU 1808 CE1 TYR D 116 2026 1825 2015 179 -33 49 C ATOM 1809 CE2 TYR A 116 26.430 -9.787 16.636 1.00 16.23 C ANISOU 1809 CE2 TYR D 116 1976 2216 1973 449 -49 -372 C ATOM 1810 CZ TYR A 116 25.203 -10.253 16.322 1.00 15.06 C ANISOU 1810 CZ TYR D 116 2145 1790 1787 9 -158 -285 C ATOM 1811 OH TYR A 116 24.821 -11.519 16.791 1.00 19.46 O ANISOU 1811 OH TYR D 116 2542 2068 2780 62 -55 -555 O ATOM 1812 N SER A 117 24.144 -4.600 14.692 1.00 10.25 N ANISOU 1812 N SER D 117 1336 1659 899 -48 2 -106 N ATOM 1813 CA BSER A 117 22.749 -4.407 14.387 0.50 11.52 C ANISOU 1813 CA BSER D 117 1458 1719 1201 11 56 -45 C ATOM 1814 C SER A 117 22.416 -5.231 13.148 1.00 10.82 C ANISOU 1814 C SER D 117 1417 1761 931 66 82 -100 C ATOM 1815 O SER A 117 23.250 -5.306 12.228 1.00 12.07 O ANISOU 1815 O SER D 117 1620 2066 897 -54 50 -32 O ATOM 1816 CB BSER A 117 22.507 -2.933 14.029 0.50 12.28 C ANISOU 1816 CB BSER D 117 1500 1636 1527 172 74 206 C ATOM 1817 OG BSER A 117 21.122 -2.708 13.859 0.50 16.88 O ANISOU 1817 OG BSER D 117 1959 2614 1838 102 350 173 O ATOM 1818 N THR A 118 21.231 -5.777 13.096 1.00 10.16 N ANISOU 1818 N THR D 118 1368 1673 816 -65 77 13 N ATOM 1819 CA THR A 118 20.769 -6.401 11.856 1.00 10.89 C ANISOU 1819 CA THR D 118 1506 1680 952 -55 44 10 C ATOM 1820 C THR A 118 19.305 -6.037 11.637 1.00 12.41 C ANISOU 1820 C THR D 118 1625 1824 1267 -96 92 21 C ATOM 1821 O THR A 118 18.506 -5.972 12.548 1.00 13.64 O ANISOU 1821 O THR D 118 1569 2483 1128 -66 238 -76 O ATOM 1822 CB THR A 118 21.000 -7.904 11.858 1.00 12.68 C ANISOU 1822 CB THR D 118 1844 1808 1165 14 5 -97 C ATOM 1823 OG1 THR A 118 20.687 -8.445 10.583 1.00 12.66 O ANISOU 1823 OG1 THR D 118 1799 1852 1156 -167 -263 68 O ATOM 1824 CG2 THR A 118 20.163 -8.606 12.939 1.00 13.57 C ANISOU 1824 CG2 THR D 118 2160 1730 1267 -76 -339 -152 C ATOM 1825 N THR A 119 18.979 -5.818 10.372 1.00 11.66 N ANISOU 1825 N THR D 119 1680 1777 970 -84 90 51 N ATOM 1826 CA ATHR A 119 17.558 -5.552 9.992 0.50 12.69 C ANISOU 1826 CA ATHR D 119 1805 1665 1349 66 152 -71 C ATOM 1827 C THR A 119 17.280 -6.317 8.741 1.00 12.71 C ANISOU 1827 C THR D 119 1840 1657 1332 153 87 74 C ATOM 1828 O THR A 119 18.149 -6.692 7.973 1.00 13.22 O ANISOU 1828 O THR D 119 1857 2104 1059 164 -80 398 O ATOM 1829 CB ATHR A 119 17.114 -3.983 9.900 0.50 10.65 C ANISOU 1829 CB ATHR D 119 1504 1500 1041 129 107 219 C ATOM 1830 OG1ATHR A 119 15.679 -3.823 9.942 0.50 12.08 O ANISOU 1830 OG1ATHR D 119 1519 1656 1414 119 143 4 O ATOM 1831 CG2ATHR A 119 17.626 -3.326 8.675 0.50 12.55 C ANISOU 1831 CG2ATHR D 119 1855 1562 1349 59 -231 162 C ATOM 1832 N ALA A 120 16.014 -6.610 8.590 1.00 12.41 N ANISOU 1832 N ALA D 120 1849 1849 1016 112 96 292 N ATOM 1833 CA ALA A 120 15.461 -7.274 7.416 1.00 12.62 C ANISOU 1833 CA ALA D 120 1863 1759 1171 121 239 238 C ATOM 1834 C ALA A 120 14.614 -6.271 6.662 1.00 12.99 C ANISOU 1834 C ALA D 120 1921 1801 1214 246 164 408 C ATOM 1835 O ALA A 120 13.749 -5.617 7.245 1.00 15.48 O ANISOU 1835 O ALA D 120 2197 2368 1315 594 210 227 O ATOM 1836 CB ALA A 120 14.631 -8.463 7.892 1.00 15.51 C ANISOU 1836 CB ALA D 120 2338 1898 1656 -32 201 194 C ATOM 1837 N VAL A 121 14.885 -6.147 5.379 1.00 12.85 N ANISOU 1837 N VAL D 121 1687 1816 1379 338 208 166 N ATOM 1838 CA VAL A 121 14.098 -5.299 4.498 1.00 14.02 C ANISOU 1838 CA VAL D 121 2053 1887 1385 281 243 230 C ATOM 1839 C VAL A 121 13.461 -6.292 3.539 1.00 13.96 C ANISOU 1839 C VAL D 121 1931 1907 1465 378 396 263 C ATOM 1840 O VAL A 121 14.170 -6.936 2.736 1.00 16.47 O ANISOU 1840 O VAL D 121 2314 2232 1712 558 312 247 O ATOM 1841 CB VAL A 121 14.938 -4.249 3.788 1.00 14.62 C ANISOU 1841 CB VAL D 121 2348 1761 1443 293 291 168 C ATOM 1842 CG1 VAL A 121 14.014 -3.312 3.004 1.00 17.89 C ANISOU 1842 CG1 VAL D 121 2734 2198 1865 448 352 -19 C ATOM 1843 CG2 VAL A 121 15.849 -3.477 4.790 1.00 17.54 C ANISOU 1843 CG2 VAL D 121 2881 1911 1872 20 333 258 C ATOM 1844 N VAL A 122 12.151 -6.442 3.635 1.00 15.16 N ANISOU 1844 N VAL D 122 2246 1950 1563 198 353 344 N ATOM 1845 CA VAL A 122 11.406 -7.435 2.834 1.00 17.36 C ANISOU 1845 CA VAL D 122 2467 2345 1783 123 454 288 C ATOM 1846 C VAL A 122 10.442 -6.696 1.957 1.00 18.98 C ANISOU 1846 C VAL D 122 2534 2489 2188 266 404 281 C ATOM 1847 O VAL A 122 9.540 -6.045 2.458 1.00 18.06 O ANISOU 1847 O VAL D 122 2347 2616 1899 151 543 503 O ATOM 1848 CB VAL A 122 10.670 -8.439 3.765 1.00 17.87 C ANISOU 1848 CB VAL D 122 2532 2408 1848 95 342 308 C ATOM 1849 CG1 VAL A 122 10.070 -9.590 2.987 1.00 21.53 C ANISOU 1849 CG1 VAL D 122 3272 2434 2474 -447 376 505 C ATOM 1850 CG2 VAL A 122 11.679 -9.012 4.807 1.00 19.86 C ANISOU 1850 CG2 VAL D 122 2703 2758 2084 158 618 85 C ATOM 1851 N THR A 123 10.665 -6.803 0.642 1.00 19.13 N ANISOU 1851 N THR D 123 2648 2463 2156 205 526 188 N ATOM 1852 CA THR A 123 9.903 -6.019 -0.347 1.00 22.13 C ANISOU 1852 CA THR D 123 3152 2749 2507 248 464 116 C ATOM 1853 C THR A 123 9.394 -6.876 -1.492 1.00 24.25 C ANISOU 1853 C THR D 123 3554 2934 2725 287 607 179 C ATOM 1854 O THR A 123 9.776 -8.028 -1.658 1.00 23.69 O ANISOU 1854 O THR D 123 3625 2855 2520 381 1051 214 O ATOM 1855 CB THR A 123 10.771 -4.925 -0.979 1.00 22.76 C ANISOU 1855 CB THR D 123 3134 2740 2771 222 423 178 C ATOM 1856 OG1 THR A 123 11.930 -5.497 -1.601 1.00 27.46 O ANISOU 1856 OG1 THR D 123 3907 3577 2947 107 158 105 O ATOM 1857 CG2 THR A 123 11.190 -3.903 0.079 1.00 22.15 C ANISOU 1857 CG2 THR D 123 3270 2810 2336 -84 514 182 C ATOM 1858 N ASN A 124 8.495 -6.306 -2.285 1.00 26.41 N ANISOU 1858 N ASN D 124 3772 3319 2943 237 684 129 N ATOM 1859 CA ASN A 124 7.996 -6.966 -3.513 1.00 29.12 C ANISOU 1859 CA ASN D 124 4096 3602 3365 110 350 234 C ATOM 1860 C ASN A 124 8.500 -6.283 -4.757 1.00 32.11 C ANISOU 1860 C ASN D 124 4541 3906 3753 61 269 196 C ATOM 1861 O ASN A 124 8.451 -5.059 -4.775 1.00 33.62 O ANISOU 1861 O ASN D 124 4956 3895 3924 120 152 175 O ATOM 1862 CB ASN A 124 6.474 -6.961 -3.500 1.00 30.05 C ANISOU 1862 CB ASN D 124 4080 3820 3515 74 481 156 C ATOM 1863 CG ASN A 124 5.895 -8.213 -2.877 1.00 33.82 C ANISOU 1863 CG ASN D 124 4470 4419 3960 -23 261 147 C ATOM 1864 OD1 ASN A 124 6.494 -9.306 -2.943 1.00 36.43 O ANISOU 1864 OD1 ASN D 124 4575 4935 4329 133 367 348 O ATOM 1865 ND2 ASN A 124 4.734 -8.066 -2.237 1.00 37.51 N ANISOU 1865 ND2 ASN D 124 4367 4973 4910 192 59 179 N TER 1866 ASN D 124 END