ATOM 1337 N SER B 2 17.612 49.836 12.432 1.00 50.14 ATOM 1338 CA SER B 2 17.606 48.656 11.533 1.00 44.95 ATOM 1339 C SER B 2 17.172 49.143 10.161 1.00 41.68 ATOM 1340 O SER B 2 16.727 50.285 10.015 1.00 48.19 ATOM 1341 CB SER B 2 16.633 47.621 12.086 1.00 43.78 ATOM 1342 OG SER B 2 16.836 47.480 13.491 1.00 43.93 ATOM 1343 N HIS B 3 17.310 48.291 9.162 1.00 33.10 ATOM 1344 CA HIS B 3 16.942 48.640 7.792 1.00 32.61 ATOM 1345 C HIS B 3 15.491 49.124 7.669 1.00 29.73 ATOM 1346 O HIS B 3 14.586 48.540 8.253 1.00 36.46 ATOM 1347 CB HIS B 3 17.144 47.406 6.904 1.00 35.10 ATOM 1348 CG HIS B 3 17.025 47.671 5.437 1.00 29.98 ATOM 1349 ND1 HIS B 3 16.015 48.427 4.892 1.00 32.91 ATOM 1350 CD2 HIS B 3 17.794 47.269 4.400 1.00 30.60 ATOM 1351 CE1 HIS B 3 16.164 48.487 3.581 1.00 26.85 ATOM 1352 NE2 HIS B 3 17.239 47.795 3.259 1.00 30.12 ATOM 1353 N PRO B 4 15.249 50.198 6.899 1.00 25.20 ATOM 1354 CA PRO B 4 13.873 50.696 6.738 1.00 25.25 ATOM 1355 C PRO B 4 12.802 49.668 6.304 1.00 20.03 ATOM 1356 O PRO B 4 11.650 49.753 6.713 1.00 26.98 ATOM 1357 CB PRO B 4 14.028 51.853 5.727 1.00 19.37 ATOM 1358 CG PRO B 4 15.451 51.731 5.210 1.00 18.41 ATOM 1359 CD PRO B 4 16.209 51.181 6.375 1.00 20.91 ATOM 1360 N ASP B 5 13.160 48.695 5.492 1.00 16.32 ATOM 1361 CA ASP B 5 12.162 47.746 5.093 1.00 21.67 ATOM 1362 C ASP B 5 11.633 46.966 6.272 1.00 27.58 ATOM 1363 O ASP B 5 10.546 46.412 6.184 1.00 35.35 ATOM 1364 CB ASP B 5 12.668 46.817 3.995 1.00 21.84 ATOM 1365 CG ASP B 5 12.542 47.436 2.602 1.00 27.79 ATOM 1366 OD1 ASP B 5 11.954 48.542 2.492 1.00 28.90 ATOM 1367 OD2 ASP B 5 13.031 46.825 1.614 1.00 26.03 ATOM 1368 N LEU B 6 12.336 46.977 7.402 1.00 26.60 ATOM 1369 CA LEU B 6 11.850 46.232 8.574 1.00 25.74 ATOM 1370 C LEU B 6 10.418 46.626 8.913 1.00 22.97 ATOM 1371 O LEU B 6 9.588 45.772 9.204 1.00 24.88 ATOM 1372 CB LEU B 6 12.742 46.458 9.804 1.00 30.28 ATOM 1373 CG LEU B 6 12.227 45.967 11.169 1.00 27.26 ATOM 1374 CD1 LEU B 6 12.283 44.443 11.265 1.00 28.66 ATOM 1375 CD2 LEU B 6 13.050 46.597 12.276 1.00 23.99 ATOM 1376 N ASN B 7 10.115 47.913 8.825 1.00 23.12 ATOM 1377 CA ASN B 7 8.782 48.377 9.137 1.00 26.49 ATOM 1378 C ASN B 7 7.761 47.654 8.292 1.00 30.16 ATOM 1379 O ASN B 7 6.721 47.227 8.804 1.00 35.68 ATOM 1380 CB ASN B 7 8.677 49.888 8.971 1.00 31.40 ATOM 1381 CG ASN B 7 9.431 50.629 10.056 1.00 37.49 ATOM 1382 OD1 ASN B 7 9.202 50.399 11.245 1.00 38.54 ATOM 1383 ND2 ASN B 7 10.365 51.489 9.658 1.00 34.77 ATOM 1384 HD21 ASN B 7 10.857 51.969 10.356 1.00 0.00 ATOM 1385 HD22 ASN B 7 10.520 51.603 8.698 1.00 0.00 ATOM 1386 N LYS B 8 8.070 47.453 7.014 1.00 28.69 ATOM 1387 CA LYS B 8 7.138 46.743 6.149 1.00 25.10 ATOM 1388 C LYS B 8 6.979 45.336 6.729 1.00 23.05 ATOM 1389 O LYS B 8 5.867 44.811 6.804 1.00 24.54 ATOM 1390 CB LYS B 8 7.646 46.701 4.696 1.00 29.30 ATOM 1391 CG LYS B 8 7.888 48.090 4.073 1.00 40.61 ATOM 1392 CD LYS B 8 8.571 48.057 2.678 1.00 43.23 ATOM 1393 CE LYS B 8 8.806 49.493 2.127 1.00 51.13 ATOM 1394 NZ LYS B 8 9.626 49.613 0.855 1.00 44.07 ATOM 1395 N LEU B 9 8.072 44.770 7.248 1.00 22.53 ATOM 1396 CA LEU B 9 8.029 43.420 7.819 1.00 20.99 ATOM 1397 C LEU B 9 7.203 43.374 9.089 1.00 26.37 ATOM 1398 O LEU B 9 6.702 42.308 9.459 1.00 26.98 ATOM 1399 CB LEU B 9 9.431 42.859 8.080 1.00 13.75 ATOM 1400 CG LEU B 9 9.528 41.382 8.492 1.00 14.30 ATOM 1401 CD1 LEU B 9 10.754 40.793 7.931 1.00 14.53 ATOM 1402 CD2 LEU B 9 9.531 41.169 9.978 1.00 11.77 ATOM 1403 N LEU B 10 7.046 44.517 9.756 1.00 29.66 ATOM 1404 CA LEU B 10 6.253 44.541 10.983 1.00 31.74 ATOM 1405 C LEU B 10 4.750 44.545 10.692 1.00 30.89 ATOM 1406 O LEU B 10 3.958 44.127 11.542 1.00 30.58 ATOM 1407 CB LEU B 10 6.666 45.690 11.932 1.00 27.76 ATOM 1408 CG LEU B 10 8.112 45.730 12.475 1.00 24.77 ATOM 1409 CD1 LEU B 10 8.159 46.543 13.743 1.00 27.46 ATOM 1410 CD2 LEU B 10 8.659 44.358 12.770 1.00 27.70 ATOM 1411 N GLU B 11 4.370 44.962 9.481 1.00 31.31 ATOM 1412 CA GLU B 11 2.957 44.985 9.075 1.00 34.98 ATOM 1413 C GLU B 11 2.476 43.593 8.658 1.00 31.35 ATOM 1414 O GLU B 11 1.347 43.210 8.929 1.00 35.43 ATOM 1415 CB GLU B 11 2.717 45.943 7.895 1.00 40.60 ATOM 1416 CG GLU B 11 2.769 47.444 8.198 1.00 50.04 ATOM 1417 CD GLU B 11 2.584 48.315 6.937 1.00 56.51 ATOM 1418 OE1 GLU B 11 2.449 47.770 5.813 1.00 54.08 ATOM 1419 OE2 GLU B 11 2.579 49.559 7.072 1.00 61.51 ATOM 1420 N LEU B 12 3.329 42.832 7.993 1.00 26.68 ATOM 1421 CA LEU B 12 2.921 41.515 7.545 1.00 27.27 ATOM 1422 C LEU B 12 2.993 40.438 8.612 1.00 30.37 ATOM 1423 O LEU B 12 2.292 39.418 8.525 1.00 32.89 ATOM 1424 CB LEU B 12 3.761 41.068 6.342 1.00 26.73 ATOM 1425 CG LEU B 12 3.958 41.984 5.129 1.00 27.25 ATOM 1426 CD1 LEU B 12 4.731 41.242 4.071 1.00 30.24 ATOM 1427 CD2 LEU B 12 2.637 42.435 4.558 1.00 32.31 ATOM 1428 N TRP B 13 3.784 40.676 9.648 1.00 31.07 ATOM 1429 CA TRP B 13 3.971 39.660 10.681 1.00 31.47 ATOM 1430 C TRP B 13 2.766 38.924 11.238 1.00 29.59 ATOM 1431 O TRP B 13 2.730 37.696 11.141 1.00 33.64 ATOM 1432 CB TRP B 13 4.882 40.138 11.819 1.00 35.83 ATOM 1433 CG TRP B 13 5.635 38.987 12.454 1.00 36.05 ATOM 1434 CD1 TRP B 13 5.593 38.592 13.759 1.00 38.72 ATOM 1435 CD2 TRP B 13 6.504 38.062 11.787 1.00 38.71 ATOM 1436 NE1 TRP B 13 6.374 37.480 13.945 1.00 40.53 ATOM 1437 CE2 TRP B 13 6.946 37.135 12.751 1.00 38.40 ATOM 1438 CE3 TRP B 13 6.945 37.921 10.464 1.00 38.95 ATOM 1439 CZ2 TRP B 13 7.807 36.088 12.436 1.00 40.36 ATOM 1440 CZ3 TRP B 13 7.798 36.877 10.152 1.00 34.41 ATOM 1441 CH2 TRP B 13 8.221 35.976 11.131 1.00 38.19 ATOM 1442 N PRO B 14 1.770 39.635 11.827 1.00 27.77 ATOM 1443 CA PRO B 14 0.616 38.892 12.360 1.00 22.69 ATOM 1444 C PRO B 14 0.077 37.888 11.367 1.00 19.02 ATOM 1445 O PRO B 14 -0.078 36.716 11.677 1.00 21.89 ATOM 1446 CB PRO B 14 -0.403 39.992 12.690 1.00 16.94 ATOM 1447 CG PRO B 14 0.120 41.231 11.992 1.00 22.09 ATOM 1448 CD PRO B 14 1.604 41.080 12.071 1.00 24.81 ATOM 1449 N HIS B 15 -0.028 38.298 10.121 1.00 16.46 ATOM 1450 CA HIS B 15 -0.553 37.385 9.143 1.00 19.96 ATOM 1451 C HIS B 15 0.331 36.164 9.030 1.00 21.12 ATOM 1452 O HIS B 15 -0.159 35.061 8.820 1.00 26.65 ATOM 1453 CB HIS B 15 -0.813 38.110 7.820 1.00 20.65 ATOM 1454 CG HIS B 15 -1.738 39.282 7.978 1.00 30.93 ATOM 1455 ND1 HIS B 15 -1.287 40.579 8.117 1.00 40.04 ATOM 1456 CD2 HIS B 15 -3.082 39.339 8.145 1.00 34.83 ATOM 1457 CE1 HIS B 15 -2.306 41.384 8.369 1.00 37.91 ATOM 1458 NE2 HIS B 15 -3.406 40.654 8.390 1.00 41.87 ATOM 1459 N ILE B 16 1.608 36.322 9.341 1.00 22.59 ATOM 1460 CA ILE B 16 2.529 35.199 9.247 1.00 22.57 ATOM 1461 C ILE B 16 2.361 34.246 10.412 1.00 23.90 ATOM 1462 O ILE B 16 2.327 33.025 10.228 1.00 28.67 ATOM 1463 CB ILE B 16 3.992 35.674 9.142 1.00 22.23 ATOM 1464 CG1 ILE B 16 4.093 36.772 8.089 1.00 11.42 ATOM 1465 CG2 ILE B 16 4.892 34.520 8.710 1.00 20.98 ATOM 1466 CD1 ILE B 16 3.662 36.311 6.726 1.00 2.00 ATOM 1467 N GLN B 17 2.213 34.794 11.609 1.00 22.20 ATOM 1468 CA GLN B 17 2.038 33.956 12.794 1.00 21.72 ATOM 1469 C GLN B 17 0.815 33.057 12.609 1.00 23.09 ATOM 1470 O GLN B 17 0.855 31.889 12.991 1.00 31.49 ATOM 1471 CB GLN B 17 1.902 34.806 14.069 1.00 18.20 ATOM 1472 CG GLN B 17 1.902 34.018 15.385 1.00 31.91 ATOM 1473 CD GLN B 17 3.272 33.464 15.785 1.00 38.77 ATOM 1474 OE1 GLN B 17 4.265 34.193 15.807 1.00 39.60 ATOM 1475 NE2 GLN B 17 3.319 32.177 16.142 1.00 40.05 ATOM 1476 HE21 GLN B 17 4.192 31.829 16.420 1.00 0.00 ATOM 1477 HE22 GLN B 17 2.496 31.655 16.114 1.00 0.00 ATOM 1478 N GLU B 18 -0.247 33.573 11.989 1.00 17.38 ATOM 1479 CA GLU B 18 -1.456 32.777 11.758 1.00 16.84 ATOM 1480 C GLU B 18 -1.148 31.518 10.918 1.00 15.53 ATOM 1481 O GLU B 18 -1.612 30.422 11.222 1.00 15.58 ATOM 1482 CB GLU B 18 -2.537 33.616 11.060 1.00 22.68 ATOM 1483 CG GLU B 18 -2.929 34.921 11.761 1.00 30.42 ATOM 1484 CD GLU B 18 -4.265 35.504 11.261 1.00 39.64 ATOM 1485 OE1 GLU B 18 -5.289 34.785 11.353 1.00 45.57 ATOM 1486 OE2 GLU B 18 -4.304 36.681 10.805 1.00 38.85 ATOM 1487 N TYR B 19 -0.345 31.678 9.875 1.00 11.94 ATOM 1488 CA TYR B 19 0.020 30.562 9.032 1.00 10.06 ATOM 1489 C TYR B 19 0.741 29.562 9.918 1.00 15.84 ATOM 1490 O TYR B 19 0.466 28.371 9.878 1.00 25.29 ATOM 1491 CB TYR B 19 0.938 31.033 7.897 1.00 5.57 ATOM 1492 CG TYR B 19 1.126 30.028 6.763 1.00 17.65 ATOM 1493 CD1 TYR B 19 0.198 29.924 5.723 1.00 22.70 ATOM 1494 CD2 TYR B 19 2.218 29.181 6.730 1.00 22.16 ATOM 1495 CE1 TYR B 19 0.359 29.005 4.694 1.00 20.66 ATOM 1496 CE2 TYR B 19 2.380 28.257 5.705 1.00 27.84 ATOM 1497 CZ TYR B 19 1.450 28.175 4.692 1.00 25.36 ATOM 1498 OH TYR B 19 1.614 27.248 3.687 1.00 29.04 ATOM 1499 N GLN B 20 1.630 30.052 10.769 1.00 17.41 ATOM 1500 CA GLN B 20 2.384 29.172 11.651 1.00 15.21 ATOM 1501 C GLN B 20 1.439 28.488 12.624 1.00 15.57 ATOM 1502 O GLN B 20 1.507 27.284 12.789 1.00 19.25 ATOM 1503 CB GLN B 20 3.478 29.971 12.361 1.00 14.47 ATOM 1504 CG GLN B 20 4.485 29.182 13.195 1.00 17.18 ATOM 1505 CD GLN B 20 5.155 28.011 12.479 1.00 17.50 ATOM 1506 OE1 GLN B 20 5.576 28.101 11.318 1.00 23.36 ATOM 1507 NE2 GLN B 20 5.290 26.911 13.195 1.00 17.08 ATOM 1508 HE21 GLN B 20 5.702 26.129 12.793 1.00 0.00 ATOM 1509 HE22 GLN B 20 4.963 26.911 14.118 1.00 0.00 ATOM 1510 N ASP B 21 0.495 29.230 13.194 1.00 19.85 ATOM 1511 CA ASP B 21 -0.472 28.646 14.126 1.00 22.70 ATOM 1512 C ASP B 21 -1.268 27.597 13.358 1.00 23.07 ATOM 1513 O ASP B 21 -1.587 26.528 13.877 1.00 26.07 ATOM 1514 CB ASP B 21 -1.434 29.714 14.683 1.00 26.10 ATOM 1515 CG ASP B 21 -0.789 30.615 15.748 1.00 30.30 ATOM 1516 OD1 ASP B 21 0.331 30.290 16.228 1.00 28.09 ATOM 1517 OD2 ASP B 21 -1.420 31.654 16.100 1.00 26.45 ATOM 1518 N LEU B 22 -1.532 27.889 12.093 1.00 23.73 ATOM 1519 CA LEU B 22 -2.271 26.976 11.237 1.00 24.15 ATOM 1520 C LEU B 22 -1.456 25.718 10.870 1.00 25.98 ATOM 1521 O LEU B 22 -1.997 24.618 10.792 1.00 25.56 ATOM 1522 CB LEU B 22 -2.730 27.718 9.986 1.00 17.87 ATOM 1523 CG LEU B 22 -3.526 26.956 8.924 1.00 16.42 ATOM 1524 CD1 LEU B 22 -4.513 26.014 9.557 1.00 13.93 ATOM 1525 CD2 LEU B 22 -4.225 27.946 8.013 1.00 10.18 ATOM 1526 N ALA B 23 -0.158 25.875 10.661 1.00 26.53 ATOM 1527 CA ALA B 23 0.688 24.747 10.327 1.00 27.33 ATOM 1528 C ALA B 23 0.829 23.828 11.548 1.00 31.12 ATOM 1529 O ALA B 23 0.773 22.605 11.425 1.00 32.75 ATOM 1530 CB ALA B 23 2.056 25.246 9.867 1.00 25.41 ATOM 1531 N LEU B 24 0.945 24.431 12.729 1.00 35.01 ATOM 1532 CA LEU B 24 1.105 23.719 14.004 1.00 34.35 ATOM 1533 C LEU B 24 -0.108 22.857 14.366 1.00 35.38 ATOM 1534 O LEU B 24 -0.028 21.953 15.196 1.00 37.77 ATOM 1535 CB LEU B 24 1.371 24.745 15.105 1.00 38.20 ATOM 1536 CG LEU B 24 2.329 24.449 16.258 1.00 37.62 ATOM 1537 CD1 LEU B 24 3.646 23.935 15.718 1.00 37.56 ATOM 1538 CD2 LEU B 24 2.545 25.721 17.067 1.00 34.79 ATOM 1539 N LYS B 25 -1.243 23.168 13.756 1.00 40.53 ATOM 1540 CA LYS B 25 -2.491 22.424 13.954 1.00 37.85 ATOM 1541 C LYS B 25 -2.510 21.217 13.012 1.00 34.17 ATOM 1542 O LYS B 25 -3.421 20.406 13.043 1.00 37.54 ATOM 1543 CB LYS B 25 -3.680 23.335 13.622 1.00 39.08 ATOM 1544 CG LYS B 25 -5.045 22.729 13.859 1.00 48.51 ATOM 1545 CD LYS B 25 -6.153 23.694 13.452 1.00 55.16 ATOM 1546 CE LYS B 25 -7.534 23.089 13.672 1.00 57.06 ATOM 1547 NZ LYS B 25 -8.632 24.058 13.369 1.00 60.62 ATOM 1548 N HIS B 26 -1.503 21.111 12.154 1.00 32.76 ATOM 1549 CA HIS B 26 -1.440 20.023 11.202 1.00 24.87 ATOM 1550 C HIS B 26 -0.160 19.237 11.266 1.00 23.00 ATOM 1551 O HIS B 26 0.176 18.528 10.325 1.00 30.02 ATOM 1552 CB HIS B 26 -1.668 20.557 9.787 1.00 25.78 ATOM 1553 CG HIS B 26 -3.087 20.955 9.524 1.00 27.44 ATOM 1554 ND1 HIS B 26 -3.596 22.183 9.889 1.00 33.16 ATOM 1555 CD2 HIS B 26 -4.125 20.262 8.998 1.00 24.55 ATOM 1556 CE1 HIS B 26 -4.885 22.227 9.606 1.00 27.72 ATOM 1557 NE2 HIS B 26 -5.230 21.074 9.065 1.00 22.16 ATOM 1558 N GLY B 27 0.544 19.343 12.384 1.00 22.93 ATOM 1559 CA GLY B 27 1.794 18.616 12.550 1.00 24.13 ATOM 1560 C GLY B 27 3.053 19.259 11.973 1.00 23.05 ATOM 1561 O GLY B 27 4.062 18.575 11.820 1.00 27.22 ATOM 1562 N ILE B 28 3.016 20.565 11.706 1.00 18.32 ATOM 1563 CA ILE B 28 4.150 21.276 11.143 1.00 17.04 ATOM 1564 C ILE B 28 4.688 22.177 12.240 1.00 23.80 ATOM 1565 O ILE B 28 4.018 23.136 12.624 1.00 28.35 ATOM 1566 CB ILE B 28 3.738 22.213 9.940 1.00 14.57 ATOM 1567 CG1 ILE B 28 3.024 21.455 8.808 1.00 13.71 ATOM 1568 CG2 ILE B 28 4.933 22.903 9.385 1.00 9.27 ATOM 1569 CD1 ILE B 28 3.757 20.255 8.311 1.00 6.48 ATOM 1570 N ASN B 29 5.897 21.888 12.722 1.00 25.51 ATOM 1571 CA ASN B 29 6.545 22.687 13.765 1.00 24.98 ATOM 1572 C ASN B 29 7.243 23.987 13.289 1.00 27.81 ATOM 1573 O ASN B 29 7.529 24.883 14.101 1.00 26.15 ATOM 1574 CB ASN B 29 7.552 21.826 14.527 1.00 30.17 ATOM 1575 CG ASN B 29 6.892 20.872 15.515 1.00 40.70 ATOM 1576 OD1 ASN B 29 5.812 21.146 16.035 1.00 49.61 ATOM 1577 ND2 ASN B 29 7.556 19.752 15.795 1.00 46.67 ATOM 1578 HD21 ASN B 29 7.146 19.126 16.422 1.00 0.00 ATOM 1579 HD22 ASN B 29 8.427 19.607 15.356 1.00 0.00 ATOM 1580 N ASP B 30 7.507 24.104 11.984 1.00 28.63 ATOM 1581 CA ASP B 30 8.191 25.280 11.425 1.00 24.61 ATOM 1582 C ASP B 30 7.865 25.462 9.947 1.00 18.78 ATOM 1583 O ASP B 30 8.224 24.613 9.148 1.00 18.55 ATOM 1584 CB ASP B 30 9.705 25.101 11.568 1.00 23.49 ATOM 1585 CG ASP B 30 10.451 26.411 11.514 1.00 28.12 ATOM 1586 OD1 ASP B 30 9.978 27.355 10.839 1.00 25.04 ATOM 1587 OD2 ASP B 30 11.510 26.495 12.169 1.00 30.05 ATOM 1588 N ILE B 31 7.225 26.570 9.574 1.00 14.50 ATOM 1589 CA ILE B 31 6.885 26.790 8.162 1.00 15.65 ATOM 1590 C ILE B 31 8.031 27.244 7.238 1.00 16.77 ATOM 1591 O ILE B 31 7.851 27.289 6.023 1.00 18.12 ATOM 1592 CB ILE B 31 5.689 27.765 7.991 1.00 9.01 ATOM 1593 CG1 ILE B 31 6.011 29.114 8.634 1.00 10.41 ATOM 1594 CG2 ILE B 31 4.467 27.168 8.592 1.00 4.94 ATOM 1595 CD1 ILE B 31 5.034 30.197 8.319 1.00 2.00 ATOM 1596 N PHE B 32 9.186 27.580 7.818 1.00 18.17 ATOM 1597 CA PHE B 32 10.356 28.047 7.069 1.00 13.65 ATOM 1598 C PHE B 32 11.503 27.024 6.985 1.00 15.54 ATOM 1599 O PHE B 32 12.683 27.390 6.916 1.00 12.59 ATOM 1600 CB PHE B 32 10.910 29.314 7.705 1.00 9.20 ATOM 1601 CG PHE B 32 9.957 30.450 7.749 1.00 9.66 ATOM 1602 CD1 PHE B 32 9.126 30.727 6.677 1.00 15.82 ATOM 1603 CD2 PHE B 32 9.901 31.263 8.865 1.00 6.88 ATOM 1604 CE1 PHE B 32 8.250 31.811 6.724 1.00 16.66 ATOM 1605 CE2 PHE B 32 9.029 32.348 8.922 1.00 3.45 ATOM 1606 CZ PHE B 32 8.203 32.622 7.852 1.00 5.14 ATOM 1607 N GLN B 33 11.161 25.745 6.934 1.00 17.40 ATOM 1608 CA GLN B 33 12.166 24.703 6.870 1.00 15.15 ATOM 1609 C GLN B 33 11.574 23.443 6.296 1.00 17.24 ATOM 1610 O GLN B 33 10.409 23.150 6.540 1.00 20.88 ATOM 1611 CB GLN B 33 12.696 24.398 8.266 1.00 12.66 ATOM 1612 CG GLN B 33 14.150 24.766 8.455 1.00 23.92 ATOM 1613 CD GLN B 33 14.670 24.348 9.786 1.00 16.54 ATOM 1614 OE1 GLN B 33 14.680 25.143 10.709 1.00 11.82 ATOM 1615 NE2 GLN B 33 15.062 23.085 9.915 1.00 18.90 ATOM 1616 HE21 GLN B 33 15.387 22.911 10.830 1.00 0.00 ATOM 1617 HE22 GLN B 33 15.031 22.413 9.204 1.00 0.00 ATOM 1618 N ASP B 34 12.392 22.682 5.568 1.00 16.73 ATOM 1619 CA ASP B 34 11.973 21.413 4.955 1.00 16.03 ATOM 1620 C ASP B 34 10.677 21.544 4.160 1.00 15.14 ATOM 1621 O ASP B 34 9.929 20.571 4.015 1.00 14.04 ATOM 1622 CB ASP B 34 11.788 20.331 6.030 1.00 22.75 ATOM 1623 CG ASP B 34 13.044 20.056 6.824 1.00 20.22 ATOM 1624 OD1 ASP B 34 14.011 20.837 6.708 1.00 28.79 ATOM 1625 OD2 ASP B 34 13.059 19.054 7.571 1.00 21.28 ATOM 1626 N ASN B 35 10.410 22.754 3.675 1.00 12.02 ATOM 1627 CA ASN B 35 9.207 23.055 2.900 1.00 15.61 ATOM 1628 C ASN B 35 7.881 23.101 3.678 1.00 11.94 ATOM 1629 O ASN B 35 6.823 22.920 3.102 1.00 14.36 ATOM 1630 CB ASN B 35 9.093 22.136 1.681 1.00 12.40 ATOM 1631 CG ASN B 35 10.028 22.538 0.571 1.00 9.74 ATOM 1632 OD1 ASN B 35 10.295 23.726 0.351 1.00 6.74 ATOM 1633 ND2 ASN B 35 10.545 21.552 -0.129 1.00 5.60 ATOM 1634 HD21 ASN B 35 11.136 21.790 -0.877 1.00 0.00 ATOM 1635 HD22 ASN B 35 10.345 20.621 0.099 1.00 0.00 ATOM 1636 N GLY B 36 7.952 23.460 4.956 1.00 14.17 ATOM 1637 CA GLY B 36 6.777 23.561 5.806 1.00 8.04 ATOM 1638 C GLY B 36 5.632 24.231 5.112 1.00 10.18 ATOM 1639 O GLY B 36 4.628 23.585 4.804 1.00 15.23 ATOM 1640 N GLY B 37 5.805 25.509 4.804 1.00 12.40 ATOM 1641 CA GLY B 37 4.768 26.245 4.104 1.00 15.31 ATOM 1642 C GLY B 37 4.229 25.496 2.897 1.00 15.13 ATOM 1643 O GLY B 37 3.042 25.217 2.846 1.00 20.67 ATOM 1644 N LYS B 38 5.103 25.117 1.966 1.00 13.16 ATOM 1645 CA LYS B 38 4.714 24.381 0.768 1.00 12.07 ATOM 1646 C LYS B 38 4.017 23.070 1.120 1.00 14.18 ATOM 1647 O LYS B 38 3.048 22.678 0.471 1.00 15.98 ATOM 1648 CB LYS B 38 5.939 24.056 -0.075 1.00 14.23 ATOM 1649 CG LYS B 38 6.590 25.237 -0.753 1.00 15.06 ATOM 1650 CD LYS B 38 7.948 24.782 -1.223 1.00 26.90 ATOM 1651 CE LYS B 38 8.764 25.888 -1.875 1.00 35.02 ATOM 1652 NZ LYS B 38 8.252 26.290 -3.225 1.00 40.85 ATOM 1653 N LEU B 39 4.464 22.430 2.191 1.00 12.95 ATOM 1654 CA LEU B 39 3.877 21.171 2.596 1.00 11.20 ATOM 1655 C LEU B 39 2.522 21.357 3.232 1.00 12.27 ATOM 1656 O LEU B 39 1.701 20.444 3.196 1.00 16.63 ATOM 1657 CB LEU B 39 4.771 20.375 3.547 1.00 7.98 ATOM 1658 CG LEU B 39 4.109 19.023 3.910 1.00 5.38 ATOM 1659 CD1 LEU B 39 4.176 18.048 2.765 1.00 2.00 ATOM 1660 CD2 LEU B 39 4.726 18.399 5.133 1.00 6.85 ATOM 1661 N LEU B 40 2.267 22.504 3.844 1.00 13.19 ATOM 1662 CA LEU B 40 0.941 22.705 4.431 1.00 17.26 ATOM 1663 C LEU B 40 -0.044 22.582 3.277 1.00 21.40 ATOM 1664 O LEU B 40 -0.919 21.717 3.290 1.00 27.30 ATOM 1665 CB LEU B 40 0.831 24.091 5.040 1.00 20.80 ATOM 1666 CG LEU B 40 -0.306 24.347 6.025 1.00 22.83 ATOM 1667 CD1 LEU B 40 -0.205 23.453 7.259 1.00 18.22 ATOM 1668 CD2 LEU B 40 -0.221 25.808 6.428 1.00 24.59 ATOM 1669 N GLN B 41 0.183 23.376 2.232 1.00 21.02 ATOM 1670 CA GLN B 41 -0.650 23.378 1.034 1.00 21.75 ATOM 1671 C GLN B 41 -1.068 22.003 0.518 1.00 19.24 ATOM 1672 O GLN B 41 -2.254 21.731 0.318 1.00 20.20 ATOM 1673 CB GLN B 41 0.088 24.077 -0.091 1.00 28.51 ATOM 1674 CG GLN B 41 -0.242 25.537 -0.246 1.00 37.01 ATOM 1675 CD GLN B 41 0.515 26.175 -1.406 1.00 42.49 ATOM 1676 OE1 GLN B 41 1.671 25.830 -1.677 1.00 49.50 ATOM 1677 NE2 GLN B 41 -0.133 27.103 -2.100 1.00 43.44 ATOM 1678 HE21 GLN B 41 0.366 27.544 -2.815 1.00 0.00 ATOM 1679 HE22 GLN B 41 -1.056 27.333 -1.873 1.00 0.00 ATOM 1680 N VAL B 42 -0.091 21.151 0.251 1.00 16.29 ATOM 1681 CA VAL B 42 -0.381 19.825 -0.284 1.00 11.76 ATOM 1682 C VAL B 42 -1.256 19.056 0.620 1.00 9.56 ATOM 1683 O VAL B 42 -2.075 18.288 0.164 1.00 10.59 ATOM 1684 CB VAL B 42 0.863 18.995 -0.473 1.00 13.09 ATOM 1685 CG1 VAL B 42 0.493 17.554 -0.816 1.00 6.75 ATOM 1686 CG2 VAL B 42 1.721 19.613 -1.551 1.00 17.86 ATOM 1687 N LEU B 43 -1.033 19.214 1.911 1.00 12.32 ATOM 1688 CA LEU B 43 -1.838 18.510 2.889 1.00 19.10 ATOM 1689 C LEU B 43 -3.301 18.939 2.841 1.00 18.44 ATOM 1690 O LEU B 43 -4.161 18.108 2.570 1.00 21.37 ATOM 1691 CB LEU B 43 -1.272 18.654 4.321 1.00 17.00 ATOM 1692 CG LEU B 43 -0.072 17.757 4.655 1.00 12.09 ATOM 1693 CD1 LEU B 43 0.310 17.881 6.119 1.00 2.72 ATOM 1694 CD2 LEU B 43 -0.392 16.304 4.302 1.00 2.44 ATOM 1695 N LEU B 44 -3.600 20.218 3.065 1.00 13.80 ATOM 1696 CA LEU B 44 -5.005 20.629 3.039 1.00 15.87 ATOM 1697 C LEU B 44 -5.708 20.268 1.730 1.00 19.55 ATOM 1698 O LEU B 44 -6.907 19.987 1.731 1.00 27.41 ATOM 1699 CB LEU B 44 -5.159 22.111 3.326 1.00 7.24 ATOM 1700 CG LEU B 44 -4.508 22.549 4.619 1.00 4.55 ATOM 1701 CD1 LEU B 44 -4.666 24.029 4.769 1.00 2.00 ATOM 1702 CD2 LEU B 44 -5.122 21.792 5.793 1.00 4.05 ATOM 1703 N ILE B 45 -4.974 20.269 0.620 1.00 19.60 ATOM 1704 CA ILE B 45 -5.565 19.909 -0.656 1.00 21.13 ATOM 1705 C ILE B 45 -5.864 18.408 -0.697 1.00 24.21 ATOM 1706 O ILE B 45 -7.015 18.010 -0.684 1.00 26.42 ATOM 1707 CB ILE B 45 -4.642 20.241 -1.799 1.00 17.71 ATOM 1708 CG1 ILE B 45 -4.414 21.740 -1.861 1.00 19.83 ATOM 1709 CG2 ILE B 45 -5.233 19.759 -3.091 1.00 15.77 ATOM 1710 CD1 ILE B 45 -3.662 22.179 -3.111 1.00 16.28 ATOM 1711 N THR B 46 -4.818 17.586 -0.692 1.00 25.70 ATOM 1712 CA THR B 46 -4.947 16.135 -0.739 1.00 24.92 ATOM 1713 C THR B 46 -5.559 15.532 0.518 1.00 28.12 ATOM 1714 O THR B 46 -5.882 14.346 0.554 1.00 35.80 ATOM 1715 CB THR B 46 -3.577 15.452 -0.961 1.00 25.42 ATOM 1716 OG1 THR B 46 -2.700 15.779 0.120 1.00 26.43 ATOM 1717 CG2 THR B 46 -2.940 15.913 -2.259 1.00 23.97 ATOM 1718 N GLY B 47 -5.715 16.330 1.558 1.00 26.87 ATOM 1719 CA GLY B 47 -6.278 15.793 2.778 1.00 24.72 ATOM 1720 C GLY B 47 -5.442 14.670 3.354 1.00 24.73 ATOM 1721 O GLY B 47 -5.975 13.650 3.784 1.00 31.61 ATOM 1722 N LEU B 48 -4.127 14.814 3.301 1.00 22.20 ATOM 1723 CA LEU B 48 -3.260 13.796 3.862 1.00 23.87 ATOM 1724 C LEU B 48 -2.926 14.223 5.283 1.00 25.86 ATOM 1725 O LEU B 48 -3.152 15.380 5.637 1.00 30.66 ATOM 1726 CB LEU B 48 -1.996 13.620 3.023 1.00 27.84 ATOM 1727 CG LEU B 48 -2.124 12.711 1.790 1.00 37.23 ATOM 1728 CD1 LEU B 48 -0.793 12.652 1.043 1.00 37.01 ATOM 1729 CD2 LEU B 48 -2.565 11.293 2.188 1.00 38.26 ATOM 1730 N THR B 49 -2.359 13.318 6.079 1.00 25.09 ATOM 1731 CA THR B 49 -2.033 13.620 7.470 1.00 31.67 ATOM 1732 C THR B 49 -0.611 13.180 7.833 1.00 31.71 ATOM 1733 O THR B 49 -0.226 12.074 7.475 1.00 36.31 ATOM 1734 CB THR B 49 -3.027 12.873 8.406 1.00 37.59 ATOM 1735 OG1 THR B 49 -4.308 12.771 7.768 1.00 37.97 ATOM 1736 CG2 THR B 49 -3.211 13.634 9.724 1.00 45.10 ATOM 1737 N VAL B 50 0.158 14.026 8.533 1.00 32.41 ATOM 1738 CA VAL B 50 1.539 13.693 8.958 1.00 36.23 ATOM 1739 C VAL B 50 1.543 13.112 10.375 1.00 42.45 ATOM 1740 O VAL B 50 1.028 13.742 11.292 1.00 46.18 ATOM 1741 CB VAL B 50 2.496 14.941 8.964 1.00 32.48 ATOM 1742 CG1 VAL B 50 2.548 15.576 7.601 1.00 33.85 ATOM 1743 CG2 VAL B 50 2.086 15.966 10.006 1.00 22.15 ATOM 1744 N LEU B 51 2.116 11.931 10.586 1.00 50.29 ATOM 1745 CA LEU B 51 2.095 11.384 11.945 1.00 58.79 ATOM 1746 C LEU B 51 3.357 11.606 12.754 1.00 64.22 ATOM 1747 O LEU B 51 4.437 11.242 12.316 1.00 64.22 ATOM 1748 CB LEU B 51 1.735 9.897 11.961 1.00 58.60 ATOM 1749 CG LEU B 51 0.261 9.503 12.142 1.00 58.89 ATOM 1750 CD1 LEU B 51 0.211 8.016 12.464 1.00 61.63 ATOM 1751 CD2 LEU B 51 -0.423 10.296 13.264 1.00 54.26 ATOM 1752 N PRO B 52 3.220 12.155 13.977 1.00 71.43 ATOM 1753 CA PRO B 52 4.330 12.437 14.897 1.00 75.71 ATOM 1754 C PRO B 52 5.336 11.291 14.993 1.00 76.08 ATOM 1755 O PRO B 52 4.982 10.111 14.851 1.00 76.25 ATOM 1756 CB PRO B 52 3.621 12.701 16.239 1.00 80.46 ATOM 1757 CG PRO B 52 2.264 12.046 16.077 1.00 79.36 ATOM 1758 CD PRO B 52 1.935 12.410 14.647 1.00 77.32 ATOM 1759 N GLY B 53 6.582 11.652 15.287 1.00 75.83 ATOM 1760 CA GLY B 53 7.634 10.660 15.332 1.00 73.11 ATOM 1761 C GLY B 53 7.767 10.240 13.883 1.00 71.52 ATOM 1762 O GLY B 53 8.088 9.092 13.577 1.00 69.44 ATOM 1763 N ARG B 54 7.425 11.176 12.993 1.00 71.44 ATOM 1764 CA ARG B 54 7.486 10.945 11.563 1.00 67.79 ATOM 1765 C ARG B 54 8.905 11.034 11.109 1.00 68.54 ATOM 1766 O ARG B 54 9.737 11.769 11.671 1.00 63.95 ATOM 1767 CB ARG B 54 6.609 11.911 10.740 1.00 66.07 ATOM 1768 CG ARG B 54 6.923 13.402 10.839 1.00 58.48 ATOM 1769 CD ARG B 54 6.068 14.186 9.844 1.00 56.31 ATOM 1770 NE ARG B 54 6.018 15.617 10.147 1.00 60.06 ATOM 1771 CZ ARG B 54 6.660 16.567 9.466 1.00 62.60 ATOM 1772 NH1 ARG B 54 7.413 16.258 8.423 1.00 63.76 ATOM 1773 NH2 ARG B 54 6.558 17.840 9.833 1.00 64.64 ATOM 1774 HH11 ARG B 54 7.504 15.308 8.127 1.00 0.00 ATOM 1775 HH12 ARG B 54 7.897 16.981 7.927 1.00 0.00 ATOM 1776 HH21 ARG B 54 6.000 18.103 10.617 1.00 0.00 ATOM 1777 HH22 ARG B 54 7.051 18.545 9.319 1.00 0.00 ATOM 1778 N GLU B 55 9.138 10.314 10.030 1.00 70.94 ATOM 1779 CA GLU B 55 10.439 10.202 9.420 1.00 73.47 ATOM 1780 C GLU B 55 10.566 11.144 8.213 1.00 65.28 ATOM 1781 O GLU B 55 10.331 10.756 7.070 1.00 66.79 ATOM 1782 CB GLU B 55 10.650 8.712 9.085 1.00 82.95 ATOM 1783 CG GLU B 55 10.289 7.810 10.319 1.00 94.76 ATOM 1784 CD GLU B 55 10.319 6.290 10.081 1.00101.42 ATOM 1785 OE1 GLU B 55 9.255 5.724 9.715 1.00103.95 ATOM 1786 OE2 GLU B 55 11.385 5.660 10.324 1.00102.54 ATOM 1787 N GLY B 56 10.845 12.412 8.500 1.00 55.38 ATOM 1788 CA GLY B 56 11.007 13.390 7.443 1.00 46.54 ATOM 1789 C GLY B 56 9.765 14.166 7.073 1.00 40.69 ATOM 1790 O GLY B 56 9.277 14.954 7.876 1.00 38.00 ATOM 1791 N ASN B 57 9.308 13.982 5.835 1.00 35.28 ATOM 1792 CA ASN B 57 8.118 14.642 5.290 1.00 30.35 ATOM 1793 C ASN B 57 7.222 13.533 4.698 1.00 32.36 ATOM 1794 O ASN B 57 7.068 13.415 3.484 1.00 30.87 ATOM 1795 CB ASN B 57 8.505 15.635 4.171 1.00 22.47 ATOM 1796 CG ASN B 57 8.958 17.018 4.688 1.00 25.36 ATOM 1797 OD1 ASN B 57 9.083 17.269 5.895 1.00 23.14 ATOM 1798 ND2 ASN B 57 9.203 17.923 3.753 1.00 19.81 ATOM 1799 HD21 ASN B 57 9.469 18.807 4.066 1.00 0.00 ATOM 1800 HD22 ASN B 57 9.140 17.665 2.813 1.00 0.00 ATOM 1801 N ASP B 58 6.672 12.684 5.557 1.00 33.28 ATOM 1802 CA ASP B 58 5.811 11.594 5.108 1.00 30.56 ATOM 1803 C ASP B 58 4.452 11.518 5.812 1.00 32.82 ATOM 1804 O ASP B 58 4.329 11.511 7.058 1.00 31.90 ATOM 1805 CB ASP B 58 6.545 10.248 5.101 1.00 30.72 ATOM 1806 CG ASP B 58 7.380 10.011 6.338 1.00 37.65 ATOM 1807 OD1 ASP B 58 7.729 10.971 7.053 1.00 43.52 ATOM 1808 OD2 ASP B 58 7.719 8.838 6.586 1.00 42.81 ATOM 1809 N ALA B 59 3.434 11.496 4.961 1.00 29.01 ATOM 1810 CA ALA B 59 2.052 11.488 5.360 1.00 24.35 ATOM 1811 C ALA B 59 1.359 10.165 5.101 1.00 25.67 ATOM 1812 O ALA B 59 1.889 9.321 4.382 1.00 26.05 ATOM 1813 CB ALA B 59 1.362 12.555 4.600 1.00 18.29 ATOM 1814 N VAL B 60 0.169 10.004 5.689 1.00 29.41 ATOM 1815 CA VAL B 60 -0.683 8.813 5.516 1.00 32.40 ATOM 1816 C VAL B 60 -2.087 9.274 5.175 1.00 35.54 ATOM 1817 O VAL B 60 -2.445 10.425 5.468 1.00 31.06 ATOM 1818 CB VAL B 60 -0.844 7.957 6.793 1.00 20.39 ATOM 1819 CG1 VAL B 60 0.480 7.427 7.241 1.00 25.93 ATOM 1820 CG2 VAL B 60 -1.515 8.753 7.886 1.00 21.44 ATOM 1821 N ASP B 61 -2.865 8.383 4.552 1.00 42.51 ATOM 1822 CA ASP B 61 -4.260 8.677 4.210 1.00 46.40 ATOM 1823 C ASP B 61 -5.172 8.035 5.247 1.00 49.79 ATOM 1824 O ASP B 61 -4.708 7.255 6.092 1.00 50.99 ATOM 1825 CB ASP B 61 -4.632 8.204 2.791 1.00 42.06 ATOM 1826 CG ASP B 61 -4.651 6.677 2.630 1.00 44.82 ATOM 1827 OD1 ASP B 61 -4.344 5.932 3.594 1.00 41.07 ATOM 1828 OD2 ASP B 61 -4.974 6.221 1.503 1.00 39.74 ATOM 1829 N ASN B 62 -6.473 8.266 5.106 1.00 54.70 ATOM 1830 CA ASN B 62 -7.469 7.732 6.038 1.00 58.33 ATOM 1831 C ASN B 62 -7.455 6.204 6.143 1.00 57.13 ATOM 1832 O ASN B 62 -8.293 5.632 6.822 1.00 55.05 ATOM 1833 CB ASN B 62 -8.892 8.224 5.666 1.00 66.15 ATOM 1834 CG ASN B 62 -9.118 9.742 5.933 1.00 72.63 ATOM 1835 OD1 ASN B 62 -8.170 10.518 6.104 1.00 75.90 ATOM 1836 ND2 ASN B 62 -10.391 10.160 5.934 1.00 75.15 ATOM 1837 HD21 ASN B 62 -10.522 11.117 6.099 1.00 0.00 ATOM 1838 HD22 ASN B 62 -11.110 9.518 5.771 1.00 0.00 ATOM 1839 N ALA B 63 -6.483 5.552 5.507 1.00 60.89 ATOM 1840 CA ALA B 63 -6.378 4.096 5.523 1.00 63.94 ATOM 1841 C ALA B 63 -5.003 3.552 5.913 1.00 68.19 ATOM 1842 O ALA B 63 -4.717 2.373 5.680 1.00 73.38 ATOM 1843 CB ALA B 63 -6.771 3.540 4.166 1.00 60.87 ATOM 1844 N GLY B 64 -4.129 4.405 6.439 1.00 67.62 ATOM 1845 CA GLY B 64 -2.816 3.927 6.838 1.00 64.81 ATOM 1846 C GLY B 64 -1.800 3.745 5.725 1.00 65.57 ATOM 1847 O GLY B 64 -0.683 3.293 5.986 1.00 69.46 ATOM 1848 N GLN B 65 -2.184 4.037 4.485 1.00 64.56 ATOM 1849 CA GLN B 65 -1.255 3.935 3.360 1.00 61.61 ATOM 1850 C GLN B 65 -0.227 5.039 3.576 1.00 56.33 ATOM 1851 O GLN B 65 -0.578 6.231 3.562 1.00 48.31 ATOM 1852 CB GLN B 65 -1.951 4.192 2.013 1.00 70.72 ATOM 1853 CG GLN B 65 -2.777 3.034 1.441 1.00 86.00 ATOM 1854 CD GLN B 65 -3.413 3.352 0.071 1.00 93.01 ATOM 1855 OE1 GLN B 65 -2.765 3.906 -0.822 1.00 97.81 ATOM 1856 NE2 GLN B 65 -4.686 2.991 -0.092 1.00 95.61 ATOM 1857 HE21 GLN B 65 -5.098 3.193 -0.958 1.00 0.00 ATOM 1858 HE22 GLN B 65 -5.139 2.545 0.649 1.00 0.00 ATOM 1859 N GLU B 66 1.015 4.640 3.838 1.00 52.00 ATOM 1860 CA GLU B 66 2.106 5.590 4.047 1.00 46.72 ATOM 1861 C GLU B 66 2.631 6.124 2.697 1.00 41.89 ATOM 1862 O GLU B 66 2.837 5.358 1.743 1.00 36.69 ATOM 1863 CB GLU B 66 3.228 4.938 4.866 1.00 48.09 ATOM 1864 CG GLU B 66 4.437 5.837 5.073 1.00 51.18 ATOM 1865 CD GLU B 66 5.215 5.510 6.326 1.00 52.64 ATOM 1866 OE1 GLU B 66 5.236 4.326 6.743 1.00 56.69 ATOM 1867 OE2 GLU B 66 5.801 6.452 6.897 1.00 52.26 ATOM 1868 N TYR B 67 2.851 7.431 2.627 1.00 34.46 ATOM 1869 CA TYR B 67 3.311 8.059 1.406 1.00 36.68 ATOM 1870 C TYR B 67 4.570 8.878 1.615 1.00 36.33 ATOM 1871 O TYR B 67 4.927 9.180 2.747 1.00 39.40 ATOM 1872 CB TYR B 67 2.229 8.986 0.858 1.00 37.35 ATOM 1873 CG TYR B 67 1.016 8.297 0.278 1.00 42.43 ATOM 1874 CD1 TYR B 67 1.027 7.828 -1.032 1.00 43.31 ATOM 1875 CD2 TYR B 67 -0.183 8.208 0.999 1.00 43.34 ATOM 1876 CE1 TYR B 67 -0.124 7.299 -1.626 1.00 46.09 ATOM 1877 CE2 TYR B 67 -1.344 7.677 0.412 1.00 46.81 ATOM 1878 CZ TYR B 67 -1.305 7.231 -0.906 1.00 49.35 ATOM 1879 OH TYR B 67 -2.447 6.775 -1.537 1.00 56.97 ATOM 1880 N GLU B 68 5.197 9.269 0.501 1.00 32.03 ATOM 1881 CA GLU B 68 6.411 10.090 0.469 1.00 26.21 ATOM 1882 C GLU B 68 6.084 11.341 -0.391 1.00 23.34 ATOM 1883 O GLU B 68 5.617 11.222 -1.514 1.00 27.23 ATOM 1884 CB GLU B 68 7.559 9.282 -0.147 1.00 26.93 ATOM 1885 CG GLU B 68 8.919 9.974 -0.157 1.00 34.47 ATOM 1886 CD GLU B 68 9.667 9.885 1.170 1.00 39.50 ATOM 1887 OE1 GLU B 68 10.128 8.768 1.499 1.00 41.68 ATOM 1888 OE2 GLU B 68 9.807 10.924 1.866 1.00 40.28 ATOM 1889 N LEU B 69 6.330 12.531 0.135 1.00 19.02 ATOM 1890 CA LEU B 69 6.007 13.769 -0.557 1.00 17.61 ATOM 1891 C LEU B 69 7.233 14.626 -0.916 1.00 22.51 ATOM 1892 O LEU B 69 8.033 14.978 -0.036 1.00 27.81 ATOM 1893 CB LEU B 69 5.027 14.591 0.309 1.00 9.13 ATOM 1894 CG LEU B 69 3.591 14.088 0.570 1.00 17.39 ATOM 1895 CD1 LEU B 69 3.572 12.703 1.203 1.00 13.52 ATOM 1896 CD2 LEU B 69 2.813 15.072 1.450 1.00 10.09 ATOM 1897 N LYS B 70 7.357 14.978 -2.201 1.00 22.04 ATOM 1898 CA LYS B 70 8.455 15.814 -2.725 1.00 20.54 ATOM 1899 C LYS B 70 7.908 17.150 -3.233 1.00 22.68 ATOM 1900 O LYS B 70 6.763 17.224 -3.699 1.00 23.14 ATOM 1901 CB LYS B 70 9.193 15.091 -3.863 1.00 12.78 ATOM 1902 CG LYS B 70 9.797 13.773 -3.425 1.00 14.50 ATOM 1903 CD LYS B 70 10.729 14.027 -2.217 1.00 24.78 ATOM 1904 CE LYS B 70 11.111 12.760 -1.458 1.00 21.06 ATOM 1905 NZ LYS B 70 12.262 13.004 -0.550 1.00 21.26 ATOM 1906 N SER B 71 8.732 18.191 -3.191 1.00 22.92 ATOM 1907 CA SER B 71 8.309 19.519 -3.632 1.00 24.22 ATOM 1908 C SER B 71 9.360 20.113 -4.578 1.00 21.75 ATOM 1909 O SER B 71 10.520 19.737 -4.496 1.00 21.95 ATOM 1910 CB SER B 71 8.119 20.402 -2.407 1.00 30.66 ATOM 1911 OG SER B 71 7.022 21.284 -2.587 1.00 50.85 ATOM 1912 N ILE B 72 8.972 21.009 -5.485 1.00 17.29 ATOM 1913 CA ILE B 72 9.946 21.567 -6.421 1.00 15.26 ATOM 1914 C ILE B 72 9.559 22.890 -7.038 1.00 17.15 ATOM 1915 O ILE B 72 8.392 23.129 -7.321 1.00 23.61 ATOM 1916 CB ILE B 72 10.259 20.587 -7.553 1.00 12.79 ATOM 1917 CG1 ILE B 72 11.359 21.144 -8.449 1.00 15.94 ATOM 1918 CG2 ILE B 72 9.032 20.324 -8.382 1.00 16.30 ATOM 1919 CD1 ILE B 72 11.956 20.101 -9.398 1.00 12.98 ATOM 1920 N ASN B 73 10.545 23.751 -7.243 1.00 16.61 ATOM 1921 CA ASN B 73 10.292 25.042 -7.830 1.00 20.94 ATOM 1922 C ASN B 73 10.646 24.997 -9.304 1.00 27.77 ATOM 1923 O ASN B 73 11.742 25.346 -9.693 1.00 33.75 ATOM 1924 CB ASN B 73 11.107 26.117 -7.136 1.00 20.51 ATOM 1925 CG ASN B 73 10.898 27.485 -7.752 1.00 30.86 ATOM 1926 OD1 ASN B 73 10.180 27.634 -8.749 1.00 34.21 ATOM 1927 ND2 ASN B 73 11.509 28.501 -7.153 1.00 33.18 ATOM 1928 HD21 ASN B 73 11.420 29.387 -7.551 1.00 0.00 ATOM 1929 HD22 ASN B 73 12.032 28.358 -6.332 1.00 0.00 ATOM 1930 N ILE B 74 9.687 24.603 -10.123 1.00 35.31 ATOM 1931 CA ILE B 74 9.852 24.497 -11.563 1.00 36.92 ATOM 1932 C ILE B 74 10.487 25.723 -12.195 1.00 37.46 ATOM 1933 O ILE B 74 10.957 25.675 -13.326 1.00 36.84 ATOM 1934 CB ILE B 74 8.471 24.176 -12.221 1.00 39.98 ATOM 1935 CG1 ILE B 74 8.432 22.702 -12.615 1.00 45.22 ATOM 1936 CG2 ILE B 74 8.128 25.124 -13.377 1.00 42.66 ATOM 1937 CD1 ILE B 74 9.735 22.195 -13.243 1.00 43.88 ATOM 1938 N ASP B 75 10.515 26.821 -11.462 1.00 41.65 ATOM 1939 CA ASP B 75 11.096 28.033 -12.001 1.00 48.59 ATOM 1940 C ASP B 75 12.609 28.172 -11.831 1.00 46.06 ATOM 1941 O ASP B 75 13.163 29.200 -12.192 1.00 46.96 ATOM 1942 CB ASP B 75 10.363 29.274 -11.459 1.00 56.35 ATOM 1943 CG ASP B 75 9.848 30.184 -12.580 1.00 62.53 ATOM 1944 OD1 ASP B 75 9.352 29.657 -13.610 1.00 62.54 ATOM 1945 OD2 ASP B 75 9.955 31.423 -12.435 1.00 65.75 ATOM 1946 N LEU B 76 13.286 27.160 -11.292 1.00 44.70 ATOM 1947 CA LEU B 76 14.739 27.256 -11.135 1.00 41.73 ATOM 1948 C LEU B 76 15.585 25.985 -11.132 1.00 42.88 ATOM 1949 O LEU B 76 16.812 26.069 -11.151 1.00 50.46 ATOM 1950 CB LEU B 76 15.109 28.163 -9.965 1.00 35.85 ATOM 1951 CG LEU B 76 14.621 27.927 -8.551 1.00 32.55 ATOM 1952 CD1 LEU B 76 15.301 26.719 -7.945 1.00 40.18 ATOM 1953 CD2 LEU B 76 14.992 29.147 -7.755 1.00 29.66 ATOM 1954 N THR B 77 14.934 24.824 -11.104 1.00 42.62 ATOM 1955 CA THR B 77 15.587 23.505 -11.149 1.00 42.24 ATOM 1956 C THR B 77 14.606 22.563 -11.863 1.00 41.32 ATOM 1957 O THR B 77 13.396 22.685 -11.665 1.00 40.76 ATOM 1958 CB THR B 77 15.904 22.942 -9.739 1.00 41.68 ATOM 1959 OG1 THR B 77 15.009 23.508 -8.773 1.00 46.70 ATOM 1960 CG2 THR B 77 17.350 23.226 -9.355 1.00 43.13 ATOM 1961 N LYS B 78 15.097 21.633 -12.684 1.00 40.13 ATOM 1962 CA LYS B 78 14.184 20.739 -13.401 1.00 38.04 ATOM 1963 C LYS B 78 14.192 19.243 -13.055 1.00 35.43 ATOM 1964 O LYS B 78 13.917 18.391 -13.921 1.00 32.76 ATOM 1965 CB LYS B 78 14.309 20.955 -14.912 1.00 46.54 ATOM 1966 CG LYS B 78 13.744 22.286 -15.371 1.00 56.27 ATOM 1967 CD LYS B 78 13.615 22.358 -16.876 1.00 68.74 ATOM 1968 CE LYS B 78 12.688 23.500 -17.282 1.00 76.22 ATOM 1969 NZ LYS B 78 12.734 23.747 -18.757 1.00 81.61 ATOM 1970 N GLY B 79 14.405 18.938 -11.770 1.00 34.86 ATOM 1971 CA GLY B 79 14.432 17.555 -11.289 1.00 28.34 ATOM 1972 C GLY B 79 14.337 17.434 -9.774 1.00 18.45 ATOM 1973 O GLY B 79 14.983 18.166 -9.065 1.00 18.93 ATOM 1974 N PHE B 80 13.546 16.494 -9.282 1.00 17.97 ATOM 1975 CA PHE B 80 13.361 16.303 -7.844 1.00 18.01 ATOM 1976 C PHE B 80 14.585 15.715 -7.122 1.00 23.12 ATOM 1977 O PHE B 80 15.349 14.941 -7.708 1.00 27.56 ATOM 1978 CB PHE B 80 12.146 15.398 -7.584 1.00 12.26 ATOM 1979 CG PHE B 80 10.831 15.997 -7.992 1.00 12.12 ATOM 1980 CD1 PHE B 80 10.100 16.768 -7.103 1.00 14.70 ATOM 1981 CD2 PHE B 80 10.308 15.763 -9.249 1.00 12.05 ATOM 1982 CE1 PHE B 80 8.887 17.285 -7.454 1.00 9.56 ATOM 1983 CE2 PHE B 80 9.085 16.281 -9.609 1.00 15.84 ATOM 1984 CZ PHE B 80 8.375 17.041 -8.712 1.00 15.41 ATOM 1985 N SER B 81 14.754 16.086 -5.846 1.00 24.52 ATOM 1986 CA SER B 81 15.850 15.599 -5.014 1.00 18.32 ATOM 1987 C SER B 81 15.411 14.334 -4.299 1.00 17.44 ATOM 1988 O SER B 81 14.234 14.111 -4.086 1.00 18.18 ATOM 1989 CB SER B 81 16.283 16.653 -3.977 1.00 19.17 ATOM 1990 OG SER B 81 17.048 17.711 -4.543 1.00 26.86 ATOM 1991 N THR B 82 16.371 13.536 -3.872 1.00 18.98 ATOM 1992 CA THR B 82 16.057 12.308 -3.194 1.00 21.84 ATOM 1993 C THR B 82 16.714 12.236 -1.830 1.00 26.47 ATOM 1994 O THR B 82 16.069 12.475 -0.811 1.00 29.25 ATOM 1995 CB THR B 82 16.517 11.138 -4.032 1.00 21.84 ATOM 1996 OG1 THR B 82 17.865 11.367 -4.456 1.00 19.69 ATOM 1997 CG2 THR B 82 15.649 11.002 -5.250 1.00 23.29 ATOM 1998 N HIS B 83 18.017 11.952 -1.828 1.00 32.05 ATOM 1999 CA HIS B 83 18.807 11.808 -0.603 1.00 31.42 ATOM 2000 C HIS B 83 20.269 12.140 -0.888 1.00 31.07 ATOM 2001 O HIS B 83 20.823 11.756 -1.922 1.00 31.42 ATOM 2002 CB HIS B 83 18.701 10.365 -0.094 1.00 32.93 ATOM 2003 CG HIS B 83 19.002 10.190 1.366 1.00 36.55 ATOM 2004 ND1 HIS B 83 20.189 9.659 1.827 1.00 37.87 ATOM 2005 CD2 HIS B 83 18.231 10.384 2.460 1.00 35.81 ATOM 2006 CE1 HIS B 83 20.133 9.527 3.138 1.00 37.45 ATOM 2007 NE2 HIS B 83 18.955 9.958 3.546 1.00 34.77 ATOM 2008 N HIS B 84 20.884 12.825 0.068 1.00 30.68 ATOM 2009 CA HIS B 84 22.273 13.246 -0.006 1.00 25.05 ATOM 2010 C HIS B 84 23.234 12.050 -0.040 1.00 23.34 ATOM 2011 O HIS B 84 24.374 12.155 -0.518 1.00 24.65 ATOM 2012 CB HIS B 84 22.559 14.117 1.215 1.00 26.54 ATOM 2013 CG HIS B 84 23.606 15.159 0.992 1.00 29.82 ATOM 2014 ND1 HIS B 84 23.499 16.446 1.475 1.00 35.66 ATOM 2015 CD2 HIS B 84 24.775 15.107 0.312 1.00 26.98 ATOM 2016 CE1 HIS B 84 24.556 17.143 1.099 1.00 38.43 ATOM 2017 NE2 HIS B 84 25.347 16.353 0.393 1.00 36.46 ATOM 2018 N HIS B 85 22.781 10.930 0.518 1.00 23.15 ATOM 2019 CA HIS B 85 23.568 9.693 0.586 1.00 22.49 ATOM 2020 C HIS B 85 22.712 8.514 0.179 1.00 19.47 ATOM 2021 O HIS B 85 22.261 7.763 1.039 1.00 20.25 ATOM 2022 CB HIS B 85 24.066 9.447 2.014 1.00 27.21 ATOM 2023 CG HIS B 85 25.182 10.350 2.431 1.00 32.04 ATOM 2024 ND1 HIS B 85 26.487 9.916 2.534 1.00 35.88 ATOM 2025 CD2 HIS B 85 25.194 11.667 2.752 1.00 31.46 ATOM 2026 CE1 HIS B 85 27.256 10.928 2.894 1.00 40.26 ATOM 2027 NE2 HIS B 85 26.496 12.003 3.032 1.00 36.58 ATOM 2028 N MET B 86 22.419 8.421 -1.112 1.00 15.95 ATOM 2029 CA MET B 86 21.609 7.359 -1.679 1.00 12.10 ATOM 2030 C MET B 86 22.328 6.049 -1.478 1.00 17.07 ATOM 2031 O MET B 86 23.544 6.022 -1.643 1.00 17.95 ATOM 2032 CB MET B 86 21.506 7.598 -3.173 1.00 17.45 ATOM 2033 CG MET B 86 20.577 6.665 -3.876 1.00 28.01 ATOM 2034 SD MET B 86 18.918 7.013 -3.328 1.00 37.24 ATOM 2035 CE MET B 86 18.719 5.759 -2.205 1.00 44.57 ATOM 2036 N ASN B 87 21.595 4.974 -1.163 1.00 19.83 ATOM 2037 CA ASN B 87 22.174 3.620 -0.969 1.00 24.41 ATOM 2038 C ASN B 87 21.101 2.510 -0.836 1.00 26.36 ATOM 2039 O ASN B 87 19.911 2.800 -0.805 1.00 25.99 ATOM 2040 CB ASN B 87 23.184 3.581 0.202 1.00 23.34 ATOM 2041 CG ASN B 87 22.528 3.572 1.568 1.00 26.57 ATOM 2042 OD1 ASN B 87 21.678 2.739 1.853 1.00 27.72 ATOM 2043 ND2 ASN B 87 22.953 4.475 2.433 1.00 27.86 ATOM 2044 HD21 ASN B 87 22.562 4.483 3.327 1.00 0.00 ATOM 2045 HD22 ASN B 87 23.647 5.100 2.138 1.00 0.00 ATOM 2046 N PRO B 88 21.507 1.230 -0.765 1.00 28.11 ATOM 2047 CA PRO B 88 20.535 0.136 -0.649 1.00 28.79 ATOM 2048 C PRO B 88 19.642 0.131 0.584 1.00 31.42 ATOM 2049 O PRO B 88 18.541 -0.414 0.551 1.00 36.79 ATOM 2050 CB PRO B 88 21.421 -1.107 -0.669 1.00 30.27 ATOM 2051 CG PRO B 88 22.562 -0.680 -1.509 1.00 31.72 ATOM 2052 CD PRO B 88 22.861 0.680 -0.941 1.00 31.33 ATOM 2053 N VAL B 89 20.140 0.666 1.690 1.00 32.90 ATOM 2054 CA VAL B 89 19.376 0.706 2.932 1.00 33.91 ATOM 2055 C VAL B 89 18.186 1.628 2.718 1.00 34.59 ATOM 2056 O VAL B 89 17.049 1.296 3.085 1.00 35.73 ATOM 2057 CB VAL B 89 20.230 1.249 4.103 1.00 39.77 ATOM 2058 CG1 VAL B 89 19.392 1.326 5.383 1.00 43.55 ATOM 2059 CG2 VAL B 89 21.476 0.382 4.308 1.00 39.67 ATOM 2060 N ILE B 90 18.471 2.786 2.122 1.00 28.76 ATOM 2061 CA ILE B 90 17.457 3.783 1.824 1.00 22.75 ATOM 2062 C ILE B 90 16.471 3.198 0.826 1.00 24.38 ATOM 2063 O ILE B 90 15.299 3.050 1.120 1.00 31.16 ATOM 2064 CB ILE B 90 18.031 5.026 1.132 1.00 14.08 ATOM 2065 CG1 ILE B 90 19.120 5.696 1.948 1.00 12.61 ATOM 2066 CG2 ILE B 90 16.944 5.999 0.918 1.00 16.61 ATOM 2067 CD1 ILE B 90 18.609 6.519 3.087 1.00 12.16 ATOM 2068 N ILE B 91 16.956 2.890 -0.368 1.00 25.11 ATOM 2069 CA ILE B 91 16.123 2.348 -1.429 1.00 27.60 ATOM 2070 C ILE B 91 15.124 1.327 -0.920 1.00 31.15 ATOM 2071 O ILE B 91 13.964 1.375 -1.299 1.00 35.26 ATOM 2072 CB ILE B 91 16.984 1.698 -2.526 1.00 26.48 ATOM 2073 CG1 ILE B 91 17.804 2.767 -3.249 1.00 23.67 ATOM 2074 CG2 ILE B 91 16.119 0.927 -3.499 1.00 28.73 ATOM 2075 CD1 ILE B 91 18.948 2.224 -4.054 1.00 16.67 ATOM 2076 N ALA B 92 15.552 0.455 -0.010 1.00 35.90 ATOM 2077 CA ALA B 92 14.686 -0.598 0.533 1.00 40.94 ATOM 2078 C ALA B 92 13.605 -0.110 1.511 1.00 44.39 ATOM 2079 O ALA B 92 12.950 -0.914 2.195 1.00 49.68 ATOM 2080 CB ALA B 92 15.538 -1.706 1.161 1.00 44.35 ATOM 2081 N LYS B 93 13.450 1.210 1.586 1.00 43.73 ATOM 2082 CA LYS B 93 12.448 1.875 2.415 1.00 40.84 ATOM 2083 C LYS B 93 11.645 2.788 1.497 1.00 37.31 ATOM 2084 O LYS B 93 10.750 3.476 1.928 1.00 41.15 ATOM 2085 CB LYS B 93 13.105 2.718 3.502 1.00 39.38 ATOM 2086 CG LYS B 93 13.286 2.007 4.818 1.00 43.47 ATOM 2087 CD LYS B 93 14.292 2.740 5.698 1.00 45.20 ATOM 2088 CE LYS B 93 14.087 4.251 5.657 1.00 42.10 ATOM 2089 NZ LYS B 93 15.048 4.915 6.564 1.00 39.32 ATOM 2090 N TYR B 94 12.005 2.821 0.227 1.00 37.48 ATOM 2091 CA TYR B 94 11.304 3.650 -0.723 1.00 37.96 ATOM 2092 C TYR B 94 10.430 2.747 -1.586 1.00 37.54 ATOM 2093 O TYR B 94 9.225 2.844 -1.509 1.00 45.30 ATOM 2094 CB TYR B 94 12.289 4.491 -1.576 1.00 37.98 ATOM 2095 N ARG B 95 11.002 1.770 -2.278 1.00 38.49 ATOM 2096 CA ARG B 95 10.192 0.897 -3.142 1.00 45.05 ATOM 2097 C ARG B 95 8.918 0.325 -2.519 1.00 49.91 ATOM 2098 O ARG B 95 8.086 -0.241 -3.238 1.00 53.69 ATOM 2099 CB ARG B 95 11.018 -0.252 -3.757 1.00 40.83 ATOM 2100 CG ARG B 95 11.735 -1.126 -2.766 1.00 35.93 ATOM 2101 CD ARG B 95 12.390 -2.309 -3.431 1.00 40.72 ATOM 2102 NE ARG B 95 13.189 -1.947 -4.596 1.00 44.75 ATOM 2103 CZ ARG B 95 14.375 -2.479 -4.899 1.00 47.84 ATOM 2104 NH1 ARG B 95 14.922 -3.410 -4.112 1.00 47.09 ATOM 2105 NH2 ARG B 95 14.992 -2.110 -6.022 1.00 40.30 ATOM 2106 HH11 ARG B 95 14.465 -3.716 -3.278 1.00 0.00 ATOM 2107 HH12 ARG B 95 15.823 -3.783 -4.350 1.00 0.00 ATOM 2108 HH21 ARG B 95 14.559 -1.446 -6.632 1.00 0.00 ATOM 2109 HH22 ARG B 95 15.881 -2.494 -6.270 1.00 0.00 ATOM 2110 N GLN B 96 8.765 0.463 -1.202 1.00 49.18 ATOM 2111 CA GLN B 96 7.587 -0.052 -0.523 1.00 50.01 ATOM 2112 C GLN B 96 6.412 0.926 -0.539 1.00 49.20 ATOM 2113 O GLN B 96 5.260 0.511 -0.376 1.00 54.43 ATOM 2114 CB GLN B 96 7.926 -0.463 0.924 1.00 57.07 ATOM 2115 CG GLN B 96 8.688 0.594 1.756 1.00 67.06 ATOM 2116 CD GLN B 96 8.654 0.337 3.277 1.00 71.95 ATOM 2117 OE1 GLN B 96 8.118 1.151 4.045 1.00 73.45 ATOM 2118 NE2 GLN B 96 9.237 -0.783 3.712 1.00 69.98 ATOM 2119 HE21 GLN B 96 9.219 -0.928 4.677 1.00 0.00 ATOM 2120 HE22 GLN B 96 9.657 -1.396 3.075 1.00 0.00 ATOM 2121 N VAL B 97 6.686 2.211 -0.756 1.00 42.33 ATOM 2122 CA VAL B 97 5.627 3.214 -0.744 1.00 41.97 ATOM 2123 C VAL B 97 5.616 4.208 -1.908 1.00 39.44 ATOM 2124 O VAL B 97 6.645 4.457 -2.546 1.00 40.02 ATOM 2125 CB VAL B 97 5.601 4.019 0.598 1.00 44.82 ATOM 2126 CG1 VAL B 97 5.638 3.078 1.804 1.00 45.88 ATOM 2127 CG2 VAL B 97 6.733 5.033 0.649 1.00 47.57 ATOM 2128 N PRO B 98 4.427 4.756 -2.218 1.00 33.27 ATOM 2129 CA PRO B 98 4.087 5.722 -3.262 1.00 29.38 ATOM 2130 C PRO B 98 4.519 7.152 -2.971 1.00 28.27 ATOM 2131 O PRO B 98 4.442 7.614 -1.820 1.00 24.31 ATOM 2132 CB PRO B 98 2.575 5.619 -3.325 1.00 32.61 ATOM 2133 CG PRO B 98 2.311 4.227 -2.900 1.00 32.39 ATOM 2134 CD PRO B 98 3.193 4.135 -1.715 1.00 34.48 ATOM 2135 N TRP B 99 4.873 7.872 -4.042 1.00 23.89 ATOM 2136 CA TRP B 99 5.347 9.258 -3.945 1.00 23.27 ATOM 2137 C TRP B 99 4.440 10.308 -4.565 1.00 21.66 ATOM 2138 O TRP B 99 4.008 10.187 -5.709 1.00 25.81 ATOM 2139 CB TRP B 99 6.728 9.401 -4.600 1.00 27.51 ATOM 2140 CG TRP B 99 7.861 8.667 -3.913 1.00 35.88 ATOM 2141 CD1 TRP B 99 7.779 7.552 -3.112 1.00 39.54 ATOM 2142 CD2 TRP B 99 9.244 8.994 -3.988 1.00 32.42 ATOM 2143 NE1 TRP B 99 9.024 7.173 -2.693 1.00 32.61 ATOM 2144 CE2 TRP B 99 9.944 8.039 -3.218 1.00 32.93 ATOM 2145 CE3 TRP B 99 9.964 9.998 -4.638 1.00 35.60 ATOM 2146 CZ2 TRP B 99 11.328 8.064 -3.085 1.00 40.97 ATOM 2147 CZ3 TRP B 99 11.342 10.022 -4.506 1.00 39.41 ATOM 2148 CH2 TRP B 99 12.011 9.060 -3.737 1.00 44.12 ATOM 2149 N ILE B 100 4.161 11.358 -3.816 1.00 15.44 ATOM 2150 CA ILE B 100 3.353 12.423 -4.346 1.00 15.07 ATOM 2151 C ILE B 100 4.377 13.471 -4.702 1.00 17.76 ATOM 2152 O ILE B 100 5.375 13.598 -3.994 1.00 12.93 ATOM 2153 CB ILE B 100 2.390 12.981 -3.297 1.00 17.70 ATOM 2154 CG1 ILE B 100 1.238 12.001 -3.081 1.00 24.26 ATOM 2155 CG2 ILE B 100 1.808 14.309 -3.750 1.00 12.63 ATOM 2156 CD1 ILE B 100 1.640 10.706 -2.438 1.00 29.90 ATOM 2157 N PHE B 101 4.153 14.189 -5.805 1.00 20.38 ATOM 2158 CA PHE B 101 5.051 15.248 -6.246 1.00 15.20 ATOM 2159 C PHE B 101 4.302 16.549 -6.462 1.00 15.34 ATOM 2160 O PHE B 101 3.430 16.632 -7.318 1.00 17.94 ATOM 2161 CB PHE B 101 5.698 14.878 -7.563 1.00 16.57 ATOM 2162 CG PHE B 101 6.661 13.758 -7.466 1.00 21.18 ATOM 2163 CD1 PHE B 101 6.215 12.446 -7.337 1.00 24.51 ATOM 2164 CD2 PHE B 101 8.012 13.995 -7.564 1.00 18.83 ATOM 2165 CE1 PHE B 101 7.116 11.385 -7.315 1.00 19.56 ATOM 2166 CE2 PHE B 101 8.921 12.936 -7.547 1.00 28.14 ATOM 2167 CZ PHE B 101 8.469 11.629 -7.423 1.00 17.82 ATOM 2168 N ALA B 102 4.689 17.584 -5.739 1.00 14.25 ATOM 2169 CA ALA B 102 4.053 18.874 -5.897 1.00 16.96 ATOM 2170 C ALA B 102 4.936 19.738 -6.771 1.00 22.02 ATOM 2171 O ALA B 102 6.157 19.688 -6.658 1.00 27.08 ATOM 2172 CB ALA B 102 3.884 19.520 -4.569 1.00 11.88 ATOM 2173 N ILE B 103 4.333 20.561 -7.614 1.00 23.00 ATOM 2174 CA ILE B 103 5.110 21.430 -8.478 1.00 22.06 ATOM 2175 C ILE B 103 4.706 22.834 -8.184 1.00 22.68 ATOM 2176 O ILE B 103 3.525 23.081 -8.001 1.00 19.87 ATOM 2177 CB ILE B 103 4.832 21.129 -9.943 1.00 28.35 ATOM 2178 CG1 ILE B 103 5.675 19.923 -10.354 1.00 28.13 ATOM 2179 CG2 ILE B 103 5.068 22.370 -10.831 1.00 24.51 ATOM 2180 CD1 ILE B 103 5.546 19.556 -11.789 1.00 29.27 ATOM 2181 N TYR B 104 5.684 23.739 -8.124 1.00 24.43 ATOM 2182 CA TYR B 104 5.445 25.156 -7.842 1.00 23.87 ATOM 2183 C TYR B 104 6.208 26.060 -8.790 1.00 25.49 ATOM 2184 O TYR B 104 7.195 25.672 -9.392 1.00 28.70 ATOM 2185 CB TYR B 104 5.896 25.534 -6.427 1.00 23.46 ATOM 2186 CG TYR B 104 5.190 24.838 -5.288 1.00 22.92 ATOM 2187 CD1 TYR B 104 5.455 23.503 -4.990 1.00 19.88 ATOM 2188 CD2 TYR B 104 4.295 25.527 -4.471 1.00 25.94 ATOM 2189 CE1 TYR B 104 4.852 22.867 -3.909 1.00 16.15 ATOM 2190 CE2 TYR B 104 3.682 24.893 -3.380 1.00 23.82 ATOM 2191 CZ TYR B 104 3.975 23.562 -3.113 1.00 21.65 ATOM 2192 OH TYR B 104 3.407 22.923 -2.042 1.00 28.78 ATOM 2193 N ARG B 105 5.731 27.280 -8.921 1.00 28.49 ATOM 2194 CA ARG B 105 6.387 28.268 -9.744 1.00 33.12 ATOM 2195 C ARG B 105 6.680 29.306 -8.670 1.00 36.93 ATOM 2196 O ARG B 105 5.909 30.244 -8.443 1.00 42.94 ATOM 2197 CB ARG B 105 5.432 28.770 -10.838 1.00 36.27 ATOM 2198 CG ARG B 105 4.937 27.616 -11.745 1.00 43.56 ATOM 2199 CD ARG B 105 4.594 28.016 -13.183 1.00 47.96 ATOM 2200 NE ARG B 105 5.730 28.588 -13.906 1.00 51.35 ATOM 2201 CZ ARG B 105 5.690 29.742 -14.573 1.00 56.90 ATOM 2202 NH1 ARG B 105 4.576 30.464 -14.626 1.00 56.48 ATOM 2203 NH2 ARG B 105 6.777 30.201 -15.173 1.00 64.82 ATOM 2204 HH11 ARG B 105 3.736 30.152 -14.185 1.00 0.00 ATOM 2205 HH12 ARG B 105 4.574 31.319 -15.140 1.00 0.00 ATOM 2206 HH21 ARG B 105 7.654 29.720 -15.125 1.00 0.00 ATOM 2207 HH22 ARG B 105 6.721 31.075 -15.658 1.00 0.00 ATOM 2208 N GLY B 106 7.767 29.062 -7.943 1.00 36.39 ATOM 2209 CA GLY B 106 8.138 29.922 -6.835 1.00 34.20 ATOM 2210 C GLY B 106 7.390 29.268 -5.693 1.00 34.54 ATOM 2211 O GLY B 106 7.650 28.101 -5.369 1.00 31.96 ATOM 2212 N ILE B 107 6.489 30.009 -5.057 1.00 37.87 ATOM 2213 CA ILE B 107 5.659 29.421 -4.002 1.00 38.71 ATOM 2214 C ILE B 107 4.215 29.524 -4.511 1.00 42.14 ATOM 2215 O ILE B 107 3.428 30.325 -4.023 1.00 45.12 ATOM 2216 CB ILE B 107 5.824 30.087 -2.596 1.00 31.40 ATOM 2217 CG1 ILE B 107 5.509 31.582 -2.622 1.00 24.19 ATOM 2218 CG2 ILE B 107 7.225 29.828 -2.033 1.00 29.51 ATOM 2219 CD1 ILE B 107 5.433 32.148 -1.197 1.00 16.43 ATOM 2220 N ALA B 108 3.913 28.751 -5.555 1.00 40.37 ATOM 2221 CA ALA B 108 2.598 28.734 -6.185 1.00 37.96 ATOM 2222 C ALA B 108 2.420 27.395 -6.914 1.00 41.27 ATOM 2223 O ALA B 108 2.816 27.250 -8.084 1.00 43.11 ATOM 2224 CB ALA B 108 2.483 29.895 -7.169 1.00 34.89 ATOM 2225 N ILE B 109 1.828 26.423 -6.213 1.00 38.28 ATOM 2226 CA ILE B 109 1.610 25.073 -6.740 1.00 31.38 ATOM 2227 C ILE B 109 0.790 25.010 -8.017 1.00 31.68 ATOM 2228 O ILE B 109 -0.312 25.510 -8.074 1.00 34.89 ATOM 2229 CB ILE B 109 0.999 24.152 -5.673 1.00 21.64 ATOM 2230 CG1 ILE B 109 0.963 22.710 -6.145 1.00 20.42 ATOM 2231 CG2 ILE B 109 -0.376 24.555 -5.354 1.00 11.57 ATOM 2232 CD1 ILE B 109 0.846 21.760 -4.980 1.00 5.41 ATOM 2233 N GLU B 110 1.371 24.412 -9.045 1.00 35.61 ATOM 2234 CA GLU B 110 0.733 24.278 -10.339 1.00 34.24 ATOM 2235 C GLU B 110 0.183 22.882 -10.532 1.00 31.86 ATOM 2236 O GLU B 110 -0.687 22.693 -11.361 1.00 32.67 ATOM 2237 CB GLU B 110 1.736 24.607 -11.464 1.00 41.53 ATOM 2238 CG GLU B 110 1.253 24.343 -12.901 1.00 45.62 ATOM 2239 CD GLU B 110 2.031 25.144 -13.931 1.00 50.91 ATOM 2240 OE1 GLU B 110 1.778 26.372 -14.018 1.00 48.78 ATOM 2241 OE2 GLU B 110 2.882 24.548 -14.642 1.00 52.99 ATOM 2242 N ALA B 111 0.685 21.898 -9.794 1.00 27.95 ATOM 2243 CA ALA B 111 0.184 20.540 -9.981 1.00 24.78 ATOM 2244 C ALA B 111 0.713 19.554 -8.975 1.00 23.88 ATOM 2245 O ALA B 111 1.669 19.837 -8.251 1.00 28.21 ATOM 2246 CB ALA B 111 0.503 20.049 -11.366 1.00 19.89 ATOM 2247 N ILE B 112 0.109 18.376 -8.975 1.00 17.26 ATOM 2248 CA ILE B 112 0.490 17.322 -8.064 1.00 19.26 ATOM 2249 C ILE B 112 0.309 15.985 -8.751 1.00 17.36 ATOM 2250 O ILE B 112 -0.812 15.540 -8.984 1.00 19.48 ATOM 2251 CB ILE B 112 -0.400 17.303 -6.796 1.00 18.41 ATOM 2252 CG1 ILE B 112 -0.395 18.661 -6.098 1.00 14.49 ATOM 2253 CG2 ILE B 112 0.078 16.221 -5.837 1.00 16.41 ATOM 2254 CD1 ILE B 112 -1.268 18.708 -4.871 1.00 2.00 ATOM 2255 N TYR B 113 1.414 15.353 -9.098 1.00 15.87 ATOM 2256 CA TYR B 113 1.345 14.058 -9.739 1.00 15.60 ATOM 2257 C TYR B 113 1.610 13.005 -8.676 1.00 16.25 ATOM 2258 O TYR B 113 2.063 13.322 -7.575 1.00 21.42 ATOM 2259 CB TYR B 113 2.342 13.992 -10.901 1.00 12.00 ATOM 2260 CG TYR B 113 1.909 14.812 -12.124 1.00 17.23 ATOM 2261 CD1 TYR B 113 2.247 16.170 -12.247 1.00 17.21 ATOM 2262 CD2 TYR B 113 1.148 14.230 -13.156 1.00 8.45 ATOM 2263 CE1 TYR B 113 1.840 16.930 -13.373 1.00 12.13 ATOM 2264 CE2 TYR B 113 0.740 14.975 -14.270 1.00 9.40 ATOM 2265 CZ TYR B 113 1.090 16.324 -14.377 1.00 15.25 ATOM 2266 OH TYR B 113 0.699 17.063 -15.489 1.00 23.24 ATOM 2267 N ARG B 114 1.301 11.759 -8.990 1.00 18.17 ATOM 2268 CA ARG B 114 1.479 10.649 -8.057 1.00 23.08 ATOM 2269 C ARG B 114 2.171 9.487 -8.765 1.00 23.23 ATOM 2270 O ARG B 114 1.877 9.219 -9.923 1.00 24.57 ATOM 2271 CB ARG B 114 0.096 10.215 -7.558 1.00 30.23 ATOM 2272 CG ARG B 114 -0.009 8.832 -6.933 1.00 33.57 ATOM 2273 CD ARG B 114 -1.450 8.538 -6.565 1.00 39.80 ATOM 2274 NE ARG B 114 -1.622 7.211 -5.994 1.00 42.91 ATOM 2275 CZ ARG B 114 -2.201 6.210 -6.636 1.00 47.78 ATOM 2276 NH1 ARG B 114 -2.648 6.391 -7.872 1.00 57.13 ATOM 2277 NH2 ARG B 114 -2.390 5.048 -6.024 1.00 57.42 ATOM 2278 HH11 ARG B 114 -2.548 7.265 -8.345 1.00 0.00 ATOM 2279 HH12 ARG B 114 -3.073 5.624 -8.353 1.00 0.00 ATOM 2280 HH21 ARG B 114 -2.103 4.932 -5.074 1.00 0.00 ATOM 2281 HH22 ARG B 114 -2.822 4.283 -6.502 1.00 0.00 ATOM 2282 N LEU B 115 3.101 8.817 -8.086 1.00 26.15 ATOM 2283 CA LEU B 115 3.818 7.684 -8.670 1.00 26.76 ATOM 2284 C LEU B 115 3.815 6.441 -7.786 1.00 33.44 ATOM 2285 O LEU B 115 3.922 6.521 -6.547 1.00 30.82 ATOM 2286 CB LEU B 115 5.247 8.070 -9.079 1.00 27.77 ATOM 2287 CG LEU B 115 5.336 8.869 -10.391 1.00 30.19 ATOM 2288 CD1 LEU B 115 6.758 9.277 -10.701 1.00 28.59 ATOM 2289 CD2 LEU B 115 4.776 8.037 -11.538 1.00 32.16 ATOM 2290 N GLU B 116 3.600 5.303 -8.445 1.00 40.09 ATOM 2291 CA GLU B 116 3.540 3.982 -7.814 1.00 46.03 ATOM 2292 C GLU B 116 4.934 3.357 -7.881 1.00 47.24 ATOM 2293 O GLU B 116 5.658 3.573 -8.858 1.00 49.49 ATOM 2294 CB GLU B 116 2.543 3.094 -8.581 1.00 48.63 ATOM 2295 CG GLU B 116 1.072 3.490 -8.464 1.00 46.39 ATOM 2296 CD GLU B 116 0.450 2.973 -7.189 1.00 50.45 ATOM 2297 OE1 GLU B 116 0.375 1.729 -7.034 1.00 53.97 ATOM 2298 OE2 GLU B 116 0.053 3.802 -6.342 1.00 44.96 ATOM 2299 N PRO B 117 5.285 2.488 -6.911 1.00 46.28 ATOM 2300 CA PRO B 117 6.609 1.848 -6.904 1.00 43.42 ATOM 2301 C PRO B 117 6.945 1.140 -8.222 1.00 42.45 ATOM 2302 O PRO B 117 8.112 0.967 -8.574 1.00 39.94 ATOM 2303 CB PRO B 117 6.507 0.878 -5.728 1.00 44.47 ATOM 2304 CG PRO B 117 5.516 1.557 -4.804 1.00 44.48 ATOM 2305 CD PRO B 117 4.464 1.992 -5.791 1.00 45.10 ATOM 2306 N LYS B 118 5.907 0.748 -8.950 1.00 45.38 ATOM 2307 CA LYS B 118 6.067 0.095 -10.242 1.00 45.88 ATOM 2308 C LYS B 118 6.740 1.094 -11.199 1.00 43.01 ATOM 2309 O LYS B 118 7.733 0.776 -11.865 1.00 40.00 ATOM 2310 CB LYS B 118 4.680 -0.343 -10.761 1.00 51.84 ATOM 2311 CG LYS B 118 4.666 -0.910 -12.178 1.00 62.20 ATOM 2312 CD LYS B 118 3.765 -2.138 -12.314 1.00 70.17 ATOM 2313 CE LYS B 118 4.009 -2.840 -13.668 1.00 76.50 ATOM 2314 NZ LYS B 118 3.421 -4.220 -13.796 1.00 77.34 ATOM 2315 N ASP B 119 6.250 2.333 -11.167 1.00 42.59 ATOM 2316 CA ASP B 119 6.743 3.404 -12.026 1.00 41.08 ATOM 2317 C ASP B 119 8.175 3.801 -11.742 1.00 41.17 ATOM 2318 O ASP B 119 8.930 4.085 -12.667 1.00 44.25 ATOM 2319 CB ASP B 119 5.868 4.656 -11.895 1.00 43.96 ATOM 2320 CG ASP B 119 4.399 4.384 -12.150 1.00 48.17 ATOM 2321 OD1 ASP B 119 3.982 4.320 -13.335 1.00 51.27 ATOM 2322 OD2 ASP B 119 3.660 4.252 -11.152 1.00 43.26 ATOM 2323 N LEU B 120 8.539 3.856 -10.463 1.00 39.25 ATOM 2324 CA LEU B 120 9.885 4.253 -10.048 1.00 35.37 ATOM 2325 C LEU B 120 10.990 3.184 -10.189 1.00 37.43 ATOM 2326 O LEU B 120 12.173 3.523 -10.220 1.00 32.26 ATOM 2327 CB LEU B 120 9.838 4.783 -8.618 1.00 31.72 ATOM 2328 CG LEU B 120 8.874 5.948 -8.339 1.00 32.03 ATOM 2329 CD1 LEU B 120 8.419 5.923 -6.880 1.00 25.72 ATOM 2330 CD2 LEU B 120 9.508 7.278 -8.696 1.00 17.71 ATOM 2331 N GLU B 121 10.611 1.913 -10.312 1.00 40.08 ATOM 2332 CA GLU B 121 11.577 0.819 -10.453 1.00 42.07 ATOM 2333 C GLU B 121 12.734 1.163 -11.370 1.00 37.56 ATOM 2334 O GLU B 121 13.897 0.865 -11.082 1.00 37.35 ATOM 2335 CB GLU B 121 10.901 -0.458 -10.973 1.00 46.33 ATOM 2336 CG GLU B 121 10.146 -1.241 -9.905 1.00 56.10 ATOM 2337 CD GLU B 121 10.979 -1.502 -8.651 1.00 64.17 ATOM 2338 OE1 GLU B 121 12.092 -2.081 -8.766 1.00 64.91 ATOM 2339 OE2 GLU B 121 10.509 -1.124 -7.549 1.00 64.41 ATOM 2340 N PHE B 122 12.409 1.807 -12.474 1.00 35.70 ATOM 2341 CA PHE B 122 13.416 2.189 -13.443 1.00 36.09 ATOM 2342 C PHE B 122 14.611 2.893 -12.805 1.00 35.94 ATOM 2343 O PHE B 122 15.733 2.770 -13.274 1.00 38.73 ATOM 2344 CB PHE B 122 12.795 3.097 -14.497 1.00 36.36 ATOM 2345 CG PHE B 122 13.787 3.677 -15.431 1.00 38.15 ATOM 2346 CD1 PHE B 122 14.401 2.879 -16.385 1.00 43.53 ATOM 2347 CD2 PHE B 122 14.138 5.013 -15.340 1.00 40.24 ATOM 2348 CE1 PHE B 122 15.360 3.404 -17.244 1.00 46.36 ATOM 2349 CE2 PHE B 122 15.092 5.551 -16.191 1.00 48.03 ATOM 2350 CZ PHE B 122 15.708 4.744 -17.147 1.00 48.31 ATOM 2351 N TYR B 123 14.362 3.642 -11.741 1.00 33.75 ATOM 2352 CA TYR B 123 15.420 4.362 -11.077 1.00 24.45 ATOM 2353 C TYR B 123 16.174 3.562 -10.030 1.00 21.99 ATOM 2354 O TYR B 123 17.402 3.602 -9.986 1.00 25.27 ATOM 2355 CB TYR B 123 14.887 5.684 -10.521 1.00 20.62 ATOM 2356 CG TYR B 123 14.913 6.787 -11.551 1.00 19.66 ATOM 2357 CD1 TYR B 123 16.121 7.278 -12.027 1.00 21.55 ATOM 2358 CD2 TYR B 123 13.745 7.312 -12.077 1.00 17.52 ATOM 2359 CE1 TYR B 123 16.173 8.254 -13.002 1.00 22.40 ATOM 2360 CE2 TYR B 123 13.783 8.297 -13.057 1.00 21.71 ATOM 2361 CZ TYR B 123 15.004 8.759 -13.519 1.00 25.53 ATOM 2362 OH TYR B 123 15.081 9.692 -14.535 1.00 31.68 ATOM 2363 N TYR B 124 15.466 2.804 -9.212 1.00 18.20 ATOM 2364 CA TYR B 124 16.141 2.015 -8.185 1.00 25.21 ATOM 2365 C TYR B 124 17.037 0.927 -8.794 1.00 26.67 ATOM 2366 O TYR B 124 18.042 0.522 -8.196 1.00 23.37 ATOM 2367 CB TYR B 124 15.132 1.351 -7.257 1.00 28.83 ATOM 2368 CG TYR B 124 14.044 2.256 -6.749 1.00 34.65 ATOM 2369 CD1 TYR B 124 14.340 3.442 -6.084 1.00 35.75 ATOM 2370 CD2 TYR B 124 12.706 1.902 -6.909 1.00 40.92 ATOM 2371 CE1 TYR B 124 13.326 4.255 -5.587 1.00 37.05 ATOM 2372 CE2 TYR B 124 11.686 2.700 -6.417 1.00 41.44 ATOM 2373 CZ TYR B 124 12.001 3.872 -5.758 1.00 41.88 ATOM 2374 OH TYR B 124 10.976 4.632 -5.255 1.00 47.34 ATOM 2375 N ASP B 125 16.648 0.433 -9.965 1.00 28.36 ATOM 2376 CA ASP B 125 17.419 -0.597 -10.639 1.00 33.94 ATOM 2377 C ASP B 125 18.772 -0.020 -11.026 1.00 34.82 ATOM 2378 O ASP B 125 19.795 -0.675 -10.883 1.00 39.16 ATOM 2379 CB ASP B 125 16.678 -1.097 -11.886 1.00 41.76 ATOM 2380 CG ASP B 125 16.204 -2.547 -11.755 1.00 44.03 ATOM 2381 OD1 ASP B 125 17.066 -3.462 -11.766 1.00 48.84 ATOM 2382 OD2 ASP B 125 14.971 -2.766 -11.667 1.00 43.76 ATOM 2383 N LYS B 126 18.773 1.224 -11.489 1.00 36.26 ATOM 2384 CA LYS B 126 19.995 1.914 -11.889 1.00 36.67 ATOM 2385 C LYS B 126 20.913 2.302 -10.724 1.00 36.90 ATOM 2386 O LYS B 126 22.135 2.338 -10.888 1.00 37.78 ATOM 2387 CB LYS B 126 19.643 3.183 -12.667 1.00 38.04 ATOM 2388 CG LYS B 126 19.217 2.957 -14.115 1.00 49.88 ATOM 2389 CD LYS B 126 18.877 4.275 -14.834 1.00 57.65 ATOM 2390 CE LYS B 126 20.010 5.303 -14.709 1.00 64.53 ATOM 2391 NZ LYS B 126 19.777 6.553 -15.488 1.00 63.31 ATOM 2392 N TRP B 127 20.321 2.611 -9.566 1.00 35.53 ATOM 2393 CA TRP B 127 21.067 3.038 -8.376 1.00 33.31 ATOM 2394 C TRP B 127 21.731 1.926 -7.573 1.00 35.64 ATOM 2395 O TRP B 127 22.818 2.115 -7.015 1.00 36.71 ATOM 2396 CB TRP B 127 20.186 3.900 -7.473 1.00 30.06 ATOM 2397 CG TRP B 127 19.685 5.162 -8.157 1.00 31.50 ATOM 2398 CD1 TRP B 127 20.225 5.784 -9.256 1.00 31.03 ATOM 2399 CD2 TRP B 127 18.555 5.946 -7.776 1.00 27.35 ATOM 2400 NE1 TRP B 127 19.499 6.907 -9.573 1.00 24.43 ATOM 2401 CE2 TRP B 127 18.469 7.028 -8.680 1.00 28.69 ATOM 2402 CE3 TRP B 127 17.597 5.836 -6.763 1.00 27.42 ATOM 2403 CZ2 TRP B 127 17.459 7.996 -8.594 1.00 31.08 ATOM 2404 CZ3 TRP B 127 16.587 6.800 -6.682 1.00 21.11 ATOM 2405 CH2 TRP B 127 16.529 7.863 -7.591 1.00 17.89 ATOM 2406 N GLU B 128 21.066 0.786 -7.451 1.00 35.55 ATOM 2407 CA GLU B 128 21.682 -0.321 -6.743 1.00 35.76 ATOM 2408 C GLU B 128 22.816 -0.777 -7.651 1.00 37.16 ATOM 2409 O GLU B 128 23.952 -0.969 -7.205 1.00 34.57 ATOM 2410 CB GLU B 128 20.686 -1.454 -6.520 1.00 37.17 ATOM 2411 CG GLU B 128 20.090 -1.470 -5.123 1.00 45.45 ATOM 2412 CD GLU B 128 19.299 -2.735 -4.819 1.00 47.60 ATOM 2413 OE1 GLU B 128 19.755 -3.848 -5.181 1.00 47.95 ATOM 2414 OE2 GLU B 128 18.219 -2.609 -4.205 1.00 51.45 ATOM 2415 N ARG B 129 22.499 -0.839 -8.944 1.00 39.83 ATOM 2416 CA ARG B 129 23.431 -1.249 -9.986 1.00 45.88 ATOM 2417 C ARG B 129 24.736 -0.531 -9.736 1.00 46.08 ATOM 2418 O ARG B 129 25.757 -1.162 -9.436 1.00 51.05 ATOM 2419 CB ARG B 129 22.900 -0.852 -11.368 1.00 53.39 ATOM 2420 CG ARG B 129 23.280 -1.803 -12.506 1.00 70.73 ATOM 2421 CD ARG B 129 22.052 -2.595 -13.020 1.00 86.75 ATOM 2422 NE ARG B 129 22.387 -3.603 -14.034 1.00 99.48 ATOM 2423 CZ ARG B 129 22.594 -3.347 -15.329 1.00107.46 ATOM 2424 NH1 ARG B 129 22.500 -2.107 -15.802 1.00109.94 ATOM 2425 NH2 ARG B 129 22.928 -4.335 -16.159 1.00110.91 ATOM 2426 HH11 ARG B 129 22.267 -1.336 -15.207 1.00 0.00 ATOM 2427 HH12 ARG B 129 22.656 -1.943 -16.777 1.00 0.00 ATOM 2428 HH21 ARG B 129 23.030 -5.270 -15.823 1.00 0.00 ATOM 2429 HH22 ARG B 129 23.084 -4.141 -17.128 1.00 0.00 ATOM 2430 N LYS B 130 24.664 0.798 -9.736 1.00 44.04 ATOM 2431 CA LYS B 130 25.847 1.621 -9.530 1.00 38.95 ATOM 2432 C LYS B 130 26.519 1.445 -8.193 1.00 40.37 ATOM 2433 O LYS B 130 27.699 1.128 -8.143 1.00 45.32 ATOM 2434 CB LYS B 130 25.554 3.096 -9.754 1.00 28.17 ATOM 2435 CG LYS B 130 26.804 3.934 -9.814 1.00 21.10 ATOM 2436 CD LYS B 130 26.427 5.315 -10.192 1.00 29.32 ATOM 2437 CE LYS B 130 27.615 6.219 -10.308 1.00 38.32 ATOM 2438 NZ LYS B 130 27.072 7.609 -10.367 1.00 41.71 ATOM 2439 N TRP B 131 25.782 1.618 -7.108 1.00 40.44 ATOM 2440 CA TRP B 131 26.391 1.488 -5.805 1.00 43.40 ATOM 2441 C TRP B 131 27.182 0.195 -5.655 1.00 48.35 ATOM 2442 O TRP B 131 28.278 0.210 -5.094 1.00 50.77 ATOM 2443 CB TRP B 131 25.336 1.573 -4.719 1.00 43.34 ATOM 2444 CG TRP B 131 25.907 1.685 -3.349 1.00 41.68 ATOM 2445 CD1 TRP B 131 26.365 2.819 -2.745 1.00 40.25 ATOM 2446 CD2 TRP B 131 25.984 0.649 -2.370 1.00 38.83 ATOM 2447 NE1 TRP B 131 26.699 2.559 -1.445 1.00 38.29 ATOM 2448 CE2 TRP B 131 26.472 1.234 -1.185 1.00 37.47 ATOM 2449 CE3 TRP B 131 25.678 -0.715 -2.376 1.00 38.88 ATOM 2450 CZ2 TRP B 131 26.654 0.502 -0.010 1.00 35.57 ATOM 2451 CZ3 TRP B 131 25.857 -1.445 -1.201 1.00 37.65 ATOM 2452 CH2 TRP B 131 26.339 -0.834 -0.038 1.00 33.59 ATOM 2453 N TYR B 132 26.669 -0.903 -6.209 1.00 53.43 ATOM 2454 CA TYR B 132 27.342 -2.203 -6.101 1.00 57.16 ATOM 2455 C TYR B 132 28.659 -2.373 -6.850 1.00 57.14 ATOM 2456 O TYR B 132 29.460 -3.234 -6.492 1.00 55.93 ATOM 2457 CB TYR B 132 26.383 -3.354 -6.427 1.00 61.95 ATOM 2458 CG TYR B 132 25.544 -3.802 -5.243 1.00 68.71 ATOM 2459 CD1 TYR B 132 26.082 -4.636 -4.257 1.00 74.20 ATOM 2460 CD2 TYR B 132 24.223 -3.367 -5.082 1.00 71.88 ATOM 2461 CE1 TYR B 132 25.318 -5.030 -3.127 1.00 75.95 ATOM 2462 CE2 TYR B 132 23.453 -3.756 -3.959 1.00 74.88 ATOM 2463 CZ TYR B 132 24.010 -4.583 -2.984 1.00 74.25 ATOM 2464 OH TYR B 132 23.279 -4.947 -1.867 1.00 68.85 ATOM 2465 N SER B 133 28.895 -1.541 -7.861 1.00 59.31 ATOM 2466 CA SER B 133 30.138 -1.591 -8.635 1.00 63.69 ATOM 2467 C SER B 133 30.928 -0.268 -8.553 1.00 64.16 ATOM 2468 O SER B 133 32.084 -0.186 -8.971 1.00 67.51 ATOM 2469 CB SER B 133 29.827 -1.951 -10.085 1.00 66.24 ATOM 2470 OG SER B 133 28.668 -1.269 -10.526 1.00 63.10 ATOM 2471 N ASP B 134 30.280 0.744 -7.980 1.00 63.09 ATOM 2472 CA ASP B 134 30.816 2.092 -7.762 1.00 60.82 ATOM 2473 C ASP B 134 31.904 1.952 -6.695 1.00 61.78 ATOM 2474 O ASP B 134 32.830 2.766 -6.588 1.00 61.90 ATOM 2475 CB ASP B 134 29.680 2.957 -7.176 1.00 57.26 ATOM 2476 CG ASP B 134 29.794 4.431 -7.515 1.00 56.94 ATOM 2477 OD1 ASP B 134 30.391 4.768 -8.563 1.00 60.61 ATOM 2478 OD2 ASP B 134 29.235 5.252 -6.744 1.00 43.17 ATOM 2479 N GLY B 135 31.752 0.897 -5.902 1.00 63.37 ATOM 2480 CA GLY B 135 32.641 0.622 -4.791 1.00 63.56 ATOM 2481 C GLY B 135 31.860 0.905 -3.507 1.00 61.84 ATOM 2482 O GLY B 135 32.422 1.354 -2.505 1.00 62.67 ATOM 2483 N HIS B 136 30.549 0.659 -3.551 1.00 56.91 ATOM 2484 CA HIS B 136 29.667 0.881 -2.410 1.00 50.87 ATOM 2485 C HIS B 136 29.783 2.336 -1.993 1.00 42.95 ATOM 2486 O HIS B 136 29.713 2.687 -0.823 1.00 45.20 ATOM 2487 CB HIS B 136 30.030 -0.077 -1.269 1.00 59.42 ATOM 2488 CG HIS B 136 29.940 -1.532 -1.647 1.00 68.04 ATOM 2489 ND1 HIS B 136 31.029 -2.264 -2.073 1.00 73.29 ATOM 2490 CD2 HIS B 136 28.888 -2.387 -1.671 1.00 68.46 ATOM 2491 CE1 HIS B 136 30.654 -3.502 -2.344 1.00 72.53 ATOM 2492 NE2 HIS B 136 29.359 -3.602 -2.109 1.00 68.73 ATOM 2493 N LYS B 137 29.938 3.180 -2.996 1.00 37.81 ATOM 2494 CA LYS B 137 30.088 4.601 -2.808 1.00 37.28 ATOM 2495 C LYS B 137 28.694 5.192 -2.905 1.00 36.31 ATOM 2496 O LYS B 137 27.999 4.954 -3.888 1.00 38.68 ATOM 2497 CB LYS B 137 31.018 5.121 -3.900 1.00 41.69 ATOM 2498 CG LYS B 137 31.252 6.601 -3.921 1.00 55.40 ATOM 2499 CD LYS B 137 30.249 7.296 -4.829 1.00 65.23 ATOM 2500 CE LYS B 137 30.535 8.784 -4.936 1.00 72.56 ATOM 2501 NZ LYS B 137 31.842 9.078 -5.603 1.00 79.75 ATOM 2502 N ASP B 138 28.268 5.879 -1.843 1.00 35.24 ATOM 2503 CA ASP B 138 26.948 6.513 -1.750 1.00 32.82 ATOM 2504 C ASP B 138 26.714 7.520 -2.850 1.00 34.91 ATOM 2505 O ASP B 138 27.642 8.237 -3.232 1.00 37.97 ATOM 2506 CB ASP B 138 26.793 7.244 -0.416 1.00 33.95 ATOM 2507 CG ASP B 138 26.430 6.319 0.727 1.00 42.98 ATOM 2508 OD1 ASP B 138 26.443 5.087 0.524 1.00 44.80 ATOM 2509 OD2 ASP B 138 26.130 6.824 1.836 1.00 46.34 ATOM 2510 N ILE B 139 25.469 7.628 -3.310 1.00 32.98 ATOM 2511 CA ILE B 139 25.147 8.574 -4.374 1.00 30.29 ATOM 2512 C ILE B 139 24.486 9.813 -3.802 1.00 31.54 ATOM 2513 O ILE B 139 23.375 9.765 -3.272 1.00 36.69 ATOM 2514 CB ILE B 139 24.252 7.973 -5.482 1.00 25.39 ATOM 2515 CG1 ILE B 139 24.744 6.584 -5.868 1.00 23.38 ATOM 2516 CG2 ILE B 139 24.373 8.806 -6.744 1.00 18.56 ATOM 2517 CD1 ILE B 139 23.732 5.807 -6.657 1.00 22.33 ATOM 2518 N ASN B 140 25.171 10.932 -3.986 1.00 26.82 ATOM 2519 CA ASN B 140 24.749 12.230 -3.496 1.00 23.25 ATOM 2520 C ASN B 140 23.677 12.995 -4.281 1.00 25.37 ATOM 2521 O ASN B 140 23.979 13.750 -5.211 1.00 24.88 ATOM 2522 CB ASN B 140 25.993 13.086 -3.337 1.00 19.92 ATOM 2523 CG ASN B 140 25.687 14.505 -2.983 1.00 26.77 ATOM 2524 OD1 ASN B 140 24.571 14.844 -2.591 1.00 25.96 ATOM 2525 ND2 ASN B 140 26.698 15.361 -3.097 1.00 30.14 ATOM 2526 HD21 ASN B 140 26.511 16.301 -2.913 1.00 0.00 ATOM 2527 HD22 ASN B 140 27.569 15.016 -3.380 1.00 0.00 ATOM 2528 N ASN B 141 22.425 12.808 -3.887 1.00 26.95 ATOM 2529 CA ASN B 141 21.311 13.521 -4.487 1.00 21.96 ATOM 2530 C ASN B 141 21.107 13.302 -5.982 1.00 19.42 ATOM 2531 O ASN B 141 21.180 14.231 -6.785 1.00 17.04 ATOM 2532 CB ASN B 141 21.444 15.013 -4.180 1.00 25.40 ATOM 2533 CG ASN B 141 20.108 15.694 -4.056 1.00 32.65 ATOM 2534 OD1 ASN B 141 19.141 15.077 -3.628 1.00 40.69 ATOM 2535 ND2 ASN B 141 20.043 16.971 -4.403 1.00 32.96 ATOM 2536 HD21 ASN B 141 19.173 17.428 -4.368 1.00 0.00 ATOM 2537 HD22 ASN B 141 20.872 17.400 -4.707 1.00 0.00 ATOM 2538 N PRO B 142 20.873 12.052 -6.379 1.00 17.86 ATOM 2539 CA PRO B 142 20.651 11.752 -7.790 1.00 16.20 ATOM 2540 C PRO B 142 19.248 12.299 -8.009 1.00 20.94 ATOM 2541 O PRO B 142 18.369 11.930 -7.249 1.00 21.62 ATOM 2542 CB PRO B 142 20.577 10.233 -7.801 1.00 13.94 ATOM 2543 CG PRO B 142 21.108 9.793 -6.468 1.00 14.97 ATOM 2544 CD PRO B 142 20.699 10.852 -5.547 1.00 17.31 ATOM 2545 N LYS B 143 19.034 13.174 -8.998 1.00 24.18 ATOM 2546 CA LYS B 143 17.697 13.753 -9.274 1.00 22.91 ATOM 2547 C LYS B 143 16.779 12.910 -10.202 1.00 24.08 ATOM 2548 O LYS B 143 17.257 12.093 -11.015 1.00 25.25 ATOM 2549 CB LYS B 143 17.811 15.162 -9.902 1.00 21.08 ATOM 2550 CG LYS B 143 18.855 16.099 -9.326 1.00 19.73 ATOM 2551 CD LYS B 143 18.826 16.107 -7.802 1.00 29.31 ATOM 2552 CE LYS B 143 19.938 16.956 -7.197 1.00 20.49 ATOM 2553 NZ LYS B 143 19.780 18.369 -7.567 1.00 27.57 ATOM 2554 N ILE B 144 15.470 13.155 -10.096 1.00 20.20 ATOM 2555 CA ILE B 144 14.435 12.497 -10.913 1.00 19.68 ATOM 2556 C ILE B 144 13.797 13.597 -11.753 1.00 20.14 ATOM 2557 O ILE B 144 13.199 14.525 -11.219 1.00 15.73 ATOM 2558 CB ILE B 144 13.362 11.873 -10.029 1.00 21.20 ATOM 2559 CG1 ILE B 144 14.014 10.792 -9.172 1.00 16.26 ATOM 2560 CG2 ILE B 144 12.163 11.389 -10.873 1.00 11.47 ATOM 2561 CD1 ILE B 144 13.093 10.124 -8.232 1.00 11.58 ATOM 2562 N PRO B 145 13.917 13.513 -13.080 1.00 22.10 ATOM 2563 CA PRO B 145 13.352 14.540 -13.972 1.00 26.17 ATOM 2564 C PRO B 145 11.847 14.741 -13.927 1.00 23.40 ATOM 2565 O PRO B 145 11.101 13.759 -14.010 1.00 25.91 ATOM 2566 CB PRO B 145 13.827 14.090 -15.354 1.00 26.90 ATOM 2567 CG PRO B 145 13.919 12.597 -15.210 1.00 31.20 ATOM 2568 CD PRO B 145 14.546 12.427 -13.842 1.00 20.50 ATOM 2569 N VAL B 146 11.404 16.007 -13.863 1.00 20.92 ATOM 2570 CA VAL B 146 9.963 16.305 -13.821 1.00 19.94 ATOM 2571 C VAL B 146 9.293 15.723 -15.032 1.00 21.83 ATOM 2572 O VAL B 146 8.271 15.079 -14.887 1.00 27.34 ATOM 2573 CB VAL B 146 9.580 17.818 -13.766 1.00 16.81 ATOM 2574 CG1 VAL B 146 10.262 18.503 -12.630 1.00 17.77 ATOM 2575 CG2 VAL B 146 9.869 18.520 -15.080 1.00 23.86 ATOM 2576 N LYS B 147 9.881 15.918 -16.217 1.00 26.54 ATOM 2577 CA LYS B 147 9.320 15.378 -17.462 1.00 28.36 ATOM 2578 C LYS B 147 8.944 13.909 -17.260 1.00 25.05 ATOM 2579 O LYS B 147 7.835 13.499 -17.602 1.00 25.95 ATOM 2580 CB LYS B 147 10.319 15.519 -18.620 1.00 36.57 ATOM 2581 CG LYS B 147 10.104 14.522 -19.771 1.00 48.58 ATOM 2582 CD LYS B 147 11.232 14.602 -20.818 1.00 56.04 ATOM 2583 CE LYS B 147 11.297 13.355 -21.740 1.00 56.62 ATOM 2584 NZ LYS B 147 10.136 13.141 -22.666 1.00 56.13 ATOM 2585 N TYR B 148 9.829 13.157 -16.614 1.00 17.43 ATOM 2586 CA TYR B 148 9.581 11.762 -16.353 1.00 11.31 ATOM 2587 C TYR B 148 8.350 11.638 -15.515 1.00 17.31 ATOM 2588 O TYR B 148 7.541 10.742 -15.747 1.00 22.08 ATOM 2589 CB TYR B 148 10.729 11.138 -15.593 1.00 12.52 ATOM 2590 CG TYR B 148 10.522 9.665 -15.306 1.00 11.20 ATOM 2591 CD1 TYR B 148 9.871 9.239 -14.153 1.00 15.45 ATOM 2592 CD2 TYR B 148 11.009 8.703 -16.164 1.00 13.34 ATOM 2593 CE1 TYR B 148 9.716 7.885 -13.859 1.00 12.02 ATOM 2594 CE2 TYR B 148 10.860 7.353 -15.892 1.00 15.38 ATOM 2595 CZ TYR B 148 10.215 6.947 -14.741 1.00 21.53 ATOM 2596 OH TYR B 148 10.049 5.598 -14.503 1.00 24.95 ATOM 2597 N VAL B 149 8.237 12.496 -14.500 1.00 22.24 ATOM 2598 CA VAL B 149 7.080 12.487 -13.585 1.00 26.67 ATOM 2599 C VAL B 149 5.758 12.879 -14.282 1.00 26.46 ATOM 2600 O VAL B 149 4.748 12.185 -14.153 1.00 27.47 ATOM 2601 CB VAL B 149 7.322 13.388 -12.300 1.00 28.82 ATOM 2602 CG1 VAL B 149 6.054 13.453 -11.435 1.00 27.08 ATOM 2603 CG2 VAL B 149 8.481 12.834 -11.435 1.00 18.16 ATOM 2604 N MET B 150 5.764 13.953 -15.053 1.00 24.99 ATOM 2605 CA MET B 150 4.549 14.351 -15.732 1.00 34.44 ATOM 2606 C MET B 150 4.102 13.281 -16.717 1.00 39.72 ATOM 2607 O MET B 150 2.913 13.134 -16.995 1.00 44.12 ATOM 2608 CB MET B 150 4.751 15.653 -16.497 1.00 34.56 ATOM 2609 CG MET B 150 4.978 16.860 -15.641 1.00 35.32 ATOM 2610 SD MET B 150 5.023 18.299 -16.701 1.00 50.28 ATOM 2611 CE MET B 150 3.862 19.362 -15.859 1.00 49.85 ATOM 2612 N GLU B 151 5.048 12.497 -17.211 1.00 43.29 ATOM 2613 CA GLU B 151 4.713 11.495 -18.205 1.00 48.87 ATOM 2614 C GLU B 151 4.528 10.061 -17.743 1.00 49.46 ATOM 2615 O GLU B 151 4.297 9.182 -18.572 1.00 54.68 ATOM 2616 CB GLU B 151 5.719 11.566 -19.364 1.00 55.90 ATOM 2617 CG GLU B 151 5.808 12.970 -20.006 1.00 61.40 ATOM 2618 CD GLU B 151 6.749 13.043 -21.198 1.00 63.77 ATOM 2619 OE1 GLU B 151 7.691 12.209 -21.266 1.00 64.58 ATOM 2620 OE2 GLU B 151 6.535 13.942 -22.057 1.00 58.60 ATOM 2621 N HIS B 152 4.607 9.803 -16.444 1.00 46.78 ATOM 2622 CA HIS B 152 4.434 8.432 -15.964 1.00 45.51 ATOM 2623 C HIS B 152 3.489 8.290 -14.796 1.00 47.19 ATOM 2624 O HIS B 152 3.342 7.189 -14.259 1.00 48.54 ATOM 2625 CB HIS B 152 5.774 7.806 -15.562 1.00 45.77 ATOM 2626 CG HIS B 152 6.646 7.438 -16.722 1.00 45.71 ATOM 2627 ND1 HIS B 152 6.492 6.263 -17.426 1.00 36.95 ATOM 2628 CD2 HIS B 152 7.663 8.105 -17.319 1.00 43.03 ATOM 2629 CE1 HIS B 152 7.371 6.226 -18.410 1.00 39.02 ATOM 2630 NE2 HIS B 152 8.094 7.331 -18.366 1.00 41.85 ATOM 2631 N GLY B 153 2.834 9.380 -14.408 1.00 48.01 ATOM 2632 CA GLY B 153 1.941 9.304 -13.265 1.00 47.40 ATOM 2633 C GLY B 153 0.539 9.851 -13.412 1.00 46.91 ATOM 2634 O GLY B 153 0.165 10.411 -14.453 1.00 53.89 ATOM 2635 N THR B 154 -0.248 9.683 -12.356 1.00 40.02 ATOM 2636 CA THR B 154 -1.613 10.157 -12.361 1.00 38.61 ATOM 2637 C THR B 154 -1.678 11.564 -11.770 1.00 33.13 ATOM 2638 O THR B 154 -1.019 11.866 -10.775 1.00 32.32 ATOM 2639 CB THR B 154 -2.517 9.186 -11.600 1.00 42.15 ATOM 2640 OG1 THR B 154 -2.103 9.118 -10.233 1.00 52.38 ATOM 2641 CG2 THR B 154 -2.404 7.783 -12.206 1.00 43.76 ATOM 2642 N LYS B 155 -2.396 12.449 -12.445 1.00 28.93 ATOM 2643 CA LYS B 155 -2.542 13.817 -11.982 1.00 20.97 ATOM 2644 C LYS B 155 -3.557 13.775 -10.862 1.00 21.90 ATOM 2645 O LYS B 155 -4.634 13.176 -10.983 1.00 28.38 ATOM 2646 CB LYS B 155 -3.044 14.691 -13.114 1.00 17.49 ATOM 2647 CG LYS B 155 -2.702 16.147 -12.988 1.00 19.35 ATOM 2648 CD LYS B 155 -2.846 16.859 -14.324 1.00 16.42 ATOM 2649 CE LYS B 155 -2.389 18.287 -14.233 1.00 25.96 ATOM 2650 NZ LYS B 155 -3.178 19.029 -13.191 1.00 26.85 ATOM 2651 N ILE B 156 -3.192 14.377 -9.753 1.00 15.98 ATOM 2652 CA ILE B 156 -4.043 14.384 -8.592 1.00 14.38 ATOM 2653 C ILE B 156 -4.612 15.766 -8.393 1.00 11.50 ATOM 2654 O ILE B 156 -5.633 15.957 -7.718 1.00 14.26 ATOM 2655 CB ILE B 156 -3.220 13.925 -7.369 1.00 17.64 ATOM 2656 CG1 ILE B 156 -3.247 12.412 -7.292 1.00 25.31 ATOM 2657 CG2 ILE B 156 -3.717 14.517 -6.071 1.00 20.96 ATOM 2658 CD1 ILE B 156 -2.848 11.927 -5.925 1.00 37.47 ATOM 2659 N TYR B 157 -3.953 16.737 -8.997 1.00 10.64 ATOM 2660 CA TYR B 157 -4.377 18.116 -8.858 1.00 14.76 ATOM 2661 C TYR B 157 -3.746 18.930 -9.950 1.00 17.35 ATOM 2662 O TYR B 157 -4.440 19.822 -10.478 1.00 21.12 ATOM 2663 CB TYR B 157 -3.933 18.689 -7.518 1.00 6.95 ATOM 2664 CG TYR B 157 -4.112 20.168 -7.468 1.00 5.68 ATOM 2665 CD1 TYR B 157 -3.136 21.013 -7.960 1.00 7.65 ATOM 2666 CD2 TYR B 157 -5.298 20.720 -7.029 1.00 10.09 ATOM 2667 CE1 TYR B 157 -3.334 22.367 -8.034 1.00 17.35 ATOM 2668 CE2 TYR B 157 -5.520 22.088 -7.093 1.00 17.12 ATOM 2669 CZ TYR B 157 -4.530 22.914 -7.603 1.00 23.23 ATOM 2670 OH TYR B 157 -4.734 24.282 -7.695 1.00 26.34 ATOM 2671 OXT TYR B 157 -2.549 18.684 -10.211 1.00 25.28 TER