HEADER 1.10.135.10 1qh4A01 ATOM 33 N SER A 6 7.485 -2.072 25.211 1.00 17.58 N ANISOU 33 N SER A 6 2304 2764 1614 -98 -457 410 N ATOM 34 CA SER A 6 8.141 -0.898 24.739 1.00 14.92 C ANISOU 34 CA SER A 6 1718 2467 1485 230 255 -61 C ATOM 35 C SER A 6 9.068 -0.306 25.810 1.00 15.71 C ANISOU 35 C SER A 6 1680 2598 1693 273 45 38 C ATOM 36 O SER A 6 10.105 0.260 25.455 1.00 15.24 O ANISOU 36 O SER A 6 2186 2073 1531 16 237 -74 O ATOM 37 CB SER A 6 7.160 0.195 24.221 1.00 19.33 C ANISOU 37 CB SER A 6 2396 2422 2524 136 -765 68 C ATOM 38 OG SER A 6 6.369 -0.377 23.194 1.00 25.89 O ANISOU 38 OG SER A 6 3939 3067 2830 1010 -1522 -699 O ATOM 39 N HIS A 7 8.702 -0.402 27.076 1.00 13.33 N ANISOU 39 N HIS A 7 1644 1749 1671 159 146 -201 N ATOM 40 CA HIS A 7 9.569 0.259 28.061 1.00 13.61 C ANISOU 40 CA HIS A 7 1479 1727 1966 85 219 -418 C ATOM 41 C HIS A 7 10.865 -0.528 28.180 1.00 12.97 C ANISOU 41 C HIS A 7 1469 1673 1788 -5 317 115 C ATOM 42 O HIS A 7 11.873 0.104 28.412 1.00 12.60 O ANISOU 42 O HIS A 7 1449 1521 1817 197 267 -215 O ATOM 43 CB HIS A 7 8.878 0.449 29.413 1.00 15.50 C ANISOU 43 CB HIS A 7 1779 2418 1692 608 -25 -330 C ATOM 44 CG HIS A 7 9.596 1.474 30.268 1.00 15.37 C ANISOU 44 CG HIS A 7 1522 2613 1707 436 155 -379 C ATOM 45 ND1 HIS A 7 10.206 1.208 31.462 1.00 19.24 N ANISOU 45 ND1 HIS A 7 2178 3002 2131 -328 -461 24 N ATOM 46 CD2 HIS A 7 9.804 2.805 30.093 1.00 22.58 C ANISOU 46 CD2 HIS A 7 3402 2248 2930 979 -1247 -615 C ATOM 47 CE1 HIS A 7 10.748 2.279 31.988 1.00 21.43 C ANISOU 47 CE1 HIS A 7 2943 2591 2607 476 -887 -445 C ATOM 48 NE2 HIS A 7 10.538 3.291 31.169 1.00 19.51 N ANISOU 48 NE2 HIS A 7 2250 2625 2539 396 -457 -386 N ATOM 49 N ASN A 8 10.878 -1.850 28.020 1.00 13.01 N ANISOU 49 N ASN A 8 1198 1686 2059 -50 186 1 N ATOM 50 CA ASN A 8 12.134 -2.554 28.109 1.00 11.84 C ANISOU 50 CA ASN A 8 1178 1618 1702 -113 91 -284 C ATOM 51 C ASN A 8 13.001 -2.156 26.918 1.00 12.06 C ANISOU 51 C ASN A 8 1233 1633 1718 17 74 -283 C ATOM 52 O ASN A 8 14.221 -2.089 27.110 1.00 13.17 O ANISOU 52 O ASN A 8 1185 1988 1832 -120 157 -156 O ATOM 53 CB ASN A 8 11.997 -4.074 28.258 1.00 10.96 C ANISOU 53 CB ASN A 8 875 1620 1669 -152 46 -433 C ATOM 54 CG ASN A 8 13.272 -4.642 28.906 1.00 10.78 C ANISOU 54 CG ASN A 8 699 1725 1672 -28 356 -307 C ATOM 55 OD1 ASN A 8 13.676 -4.172 29.952 1.00 14.07 O ANISOU 55 OD1 ASN A 8 1688 1951 1708 562 -286 -219 O ATOM 56 ND2 ASN A 8 13.891 -5.630 28.306 1.00 15.44 N ANISOU 56 ND2 ASN A 8 1822 1680 2363 470 241 -383 N ATOM 57 N LEU A 9 12.422 -1.875 25.749 1.00 11.93 N ANISOU 57 N LEU A 9 1425 1404 1706 89 56 -191 N ATOM 58 CA LEU A 9 13.247 -1.440 24.649 1.00 12.57 C ANISOU 58 CA LEU A 9 1423 1638 1715 -13 169 -447 C ATOM 59 C LEU A 9 13.850 -0.068 24.915 1.00 12.69 C ANISOU 59 C LEU A 9 1672 1602 1549 -87 235 -299 C ATOM 60 O LEU A 9 14.960 0.205 24.493 1.00 13.65 O ANISOU 60 O LEU A 9 1765 1917 1506 -323 265 -176 O ATOM 61 CB LEU A 9 12.494 -1.474 23.335 1.00 15.99 C ANISOU 61 CB LEU A 9 2222 2236 1618 -514 5 -306 C ATOM 62 CG LEU A 9 12.049 -2.929 22.977 1.00 17.73 C ANISOU 62 CG LEU A 9 2391 2373 1972 -722 -130 -410 C ATOM 63 CD1 LEU A 9 11.430 -2.837 21.606 1.00 21.99 C ANISOU 63 CD1 LEU A 9 2694 3417 2245 -840 -600 -549 C ATOM 64 CD2 LEU A 9 13.097 -4.004 23.069 1.00 26.45 C ANISOU 64 CD2 LEU A 9 4011 2536 3502 131 -1202 -969 C ATOM 65 N LEU A 10 13.127 0.814 25.576 1.00 12.84 N ANISOU 65 N LEU A 10 1936 1454 1487 87 95 -234 N ATOM 66 CA LEU A 10 13.661 2.096 26.006 1.00 12.20 C ANISOU 66 CA LEU A 10 1762 1241 1633 142 -64 127 C ATOM 67 C LEU A 10 14.872 1.848 26.899 1.00 11.18 C ANISOU 67 C LEU A 10 1542 1346 1360 187 210 -181 C ATOM 68 O LEU A 10 15.927 2.466 26.730 1.00 13.84 O ANISOU 68 O LEU A 10 1712 1878 1671 -212 230 -157 O ATOM 69 CB LEU A 10 12.555 2.880 26.710 1.00 14.61 C ANISOU 69 CB LEU A 10 2047 1522 1982 601 -391 -347 C ATOM 70 CG LEU A 10 12.905 4.247 27.284 1.00 14.91 C ANISOU 70 CG LEU A 10 2142 1374 2148 91 47 -175 C ATOM 71 CD1 LEU A 10 11.625 5.107 27.476 1.00 20.10 C ANISOU 71 CD1 LEU A 10 2708 1921 3007 570 577 -768 C ATOM 72 CD2 LEU A 10 13.582 4.265 28.657 1.00 21.41 C ANISOU 72 CD2 LEU A 10 2846 2962 2328 -697 -277 -558 C ATOM 73 N LYS A 11 14.770 0.965 27.867 1.00 11.03 N ANISOU 73 N LYS A 11 1293 1636 1263 -66 -142 -108 N ATOM 74 CA LYS A 11 15.886 0.654 28.743 1.00 10.62 C ANISOU 74 CA LYS A 11 1151 1767 1119 -91 -63 -378 C ATOM 75 C LYS A 11 17.055 0.076 28.000 1.00 10.82 C ANISOU 75 C LYS A 11 1348 1488 1273 68 -40 -278 C ATOM 76 O LYS A 11 18.199 0.313 28.383 1.00 11.47 O ANISOU 76 O LYS A 11 1215 1758 1385 -67 66 -332 O ATOM 77 CB LYS A 11 15.427 -0.276 29.875 1.00 11.44 C ANISOU 77 CB LYS A 11 1368 1689 1287 259 -37 -86 C ATOM 78 CG LYS A 11 14.488 0.492 30.835 1.00 11.70 C ANISOU 78 CG LYS A 11 1529 1749 1169 142 47 -195 C ATOM 79 CD LYS A 11 14.105 -0.259 32.072 1.00 12.79 C ANISOU 79 CD LYS A 11 1455 1974 1430 -120 -17 17 C ATOM 80 CE LYS A 11 13.066 -1.317 31.875 1.00 11.85 C ANISOU 80 CE LYS A 11 1393 1771 1338 103 -368 56 C ATOM 81 NZ LYS A 11 12.686 -1.949 33.173 1.00 11.41 N ANISOU 81 NZ LYS A 11 1233 1689 1413 -9 -311 117 N ATOM 82 N MET A 12 16.810 -0.688 26.945 1.00 10.29 N ANISOU 82 N MET A 12 1244 1488 1179 -72 141 -221 N ATOM 83 CA MET A 12 17.931 -1.266 26.192 1.00 12.23 C ANISOU 83 CA MET A 12 1373 1820 1454 -71 333 -385 C ATOM 84 C MET A 12 18.686 -0.210 25.395 1.00 13.12 C ANISOU 84 C MET A 12 1507 2009 1470 -22 504 -353 C ATOM 85 O MET A 12 19.798 -0.483 24.964 1.00 15.47 O ANISOU 85 O MET A 12 1244 2249 2386 -67 457 -181 O ATOM 86 CB MET A 12 17.435 -2.331 25.224 1.00 12.73 C ANISOU 86 CB MET A 12 1327 2002 1509 111 174 -488 C ATOM 87 CG MET A 12 16.849 -3.564 25.843 1.00 13.47 C ANISOU 87 CG MET A 12 1378 1832 1907 -111 -61 -659 C ATOM 88 SD MET A 12 17.935 -4.325 27.024 1.00 16.09 S ANISOU 88 SD MET A 12 2048 2055 2013 266 55 -269 S ATOM 89 CE MET A 12 17.219 -3.704 28.562 1.00 19.47 C ANISOU 89 CE MET A 12 1969 3568 1859 318 458 91 C ATOM 90 N LYS A 13 18.081 0.964 25.216 1.00 13.02 N ANISOU 90 N LYS A 13 1136 1830 1980 -301 22 -322 N ATOM 91 CA LYS A 13 18.758 2.074 24.566 1.00 13.56 C ANISOU 91 CA LYS A 13 1241 2427 1485 -415 -55 99 C ATOM 92 C LYS A 13 19.666 2.825 25.548 1.00 14.17 C ANISOU 92 C LYS A 13 1759 1815 1810 -593 -374 312 C ATOM 93 O LYS A 13 20.540 3.572 25.134 1.00 21.47 O ANISOU 93 O LYS A 13 1869 3705 2584 -1422 -267 532 O ATOM 94 CB LYS A 13 17.785 3.066 23.960 1.00 16.84 C ANISOU 94 CB LYS A 13 1765 2513 2122 -325 -463 241 C ATOM 95 CG LYS A 13 17.029 2.570 22.744 1.00 23.31 C ANISOU 95 CG LYS A 13 3195 2714 2949 -786 -1648 533 C ATOM 96 CD LYS A 13 16.214 3.699 22.180 1.00 32.77 C ANISOU 96 CD LYS A 13 3194 5327 3928 1237 -1552 652 C ATOM 97 CE LYS A 13 14.760 3.744 22.540 1.00 40.48 C ANISOU 97 CE LYS A 13 2960 6674 5747 -34 -1702 314 C ATOM 98 NZ LYS A 13 13.901 2.756 21.841 1.00 52.24 N ANISOU 98 NZ LYS A 13 4254 9730 5867 -227 -2727 -1547 N ATOM 99 N TYR A 14 19.463 2.659 26.861 1.00 12.94 N ANISOU 99 N TYR A 14 1166 1984 1767 -134 -302 -31 N ATOM 100 CA TYR A 14 20.395 3.083 27.874 1.00 11.98 C ANISOU 100 CA TYR A 14 1139 1719 1695 -210 -195 145 C ATOM 101 C TYR A 14 21.461 2.020 27.983 1.00 11.58 C ANISOU 101 C TYR A 14 1165 1768 1467 -178 -97 190 C ATOM 102 O TYR A 14 21.272 0.844 27.617 1.00 13.51 O ANISOU 102 O TYR A 14 1194 1768 2170 -53 -27 -29 O ATOM 103 CB TYR A 14 19.607 3.302 29.202 1.00 12.94 C ANISOU 103 CB TYR A 14 1297 1938 1682 -129 -110 -5 C ATOM 104 CG TYR A 14 18.940 4.646 29.191 1.00 13.23 C ANISOU 104 CG TYR A 14 1627 1745 1655 -175 -118 84 C ATOM 105 CD1 TYR A 14 17.658 4.820 28.663 1.00 13.50 C ANISOU 105 CD1 TYR A 14 1374 1715 2042 41 100 -533 C ATOM 106 CD2 TYR A 14 19.536 5.802 29.692 1.00 13.41 C ANISOU 106 CD2 TYR A 14 1518 1957 1620 -141 3 -221 C ATOM 107 CE1 TYR A 14 17.017 6.044 28.640 1.00 13.46 C ANISOU 107 CE1 TYR A 14 1686 1795 1632 173 -21 -585 C ATOM 108 CE2 TYR A 14 18.888 7.016 29.645 1.00 13.74 C ANISOU 108 CE2 TYR A 14 1508 1735 1977 -341 317 -99 C ATOM 109 CZ TYR A 14 17.633 7.171 29.125 1.00 13.12 C ANISOU 109 CZ TYR A 14 1612 1645 1729 12 385 -405 C ATOM 110 OH TYR A 14 17.010 8.406 29.086 1.00 15.81 O ANISOU 110 OH TYR A 14 2428 1604 1973 183 219 -148 O ATOM 111 N SER A 15 22.619 2.372 28.503 1.00 13.35 N ANISOU 111 N SER A 15 1102 2146 1824 18 -97 -151 N ATOM 112 CA SER A 15 23.660 1.376 28.677 1.00 12.81 C ANISOU 112 CA SER A 15 1101 2212 1556 69 -124 -257 C ATOM 113 C SER A 15 23.376 0.464 29.852 1.00 14.00 C ANISOU 113 C SER A 15 763 2541 2015 128 -45 124 C ATOM 114 O SER A 15 22.539 0.745 30.738 1.00 12.76 O ANISOU 114 O SER A 15 945 1914 1988 -98 11 -15 O ATOM 115 CB SER A 15 24.988 2.118 28.880 1.00 12.20 C ANISOU 115 CB SER A 15 1073 2038 1525 131 44 -215 C ATOM 116 OG SER A 15 24.989 2.719 30.168 1.00 13.05 O ANISOU 116 OG SER A 15 1280 2064 1614 -4 -29 -327 O ATOM 117 N VAL A 16 24.133 -0.646 29.896 1.00 12.54 N ANISOU 117 N VAL A 16 879 2498 1386 107 126 -1 N ATOM 118 CA VAL A 16 24.011 -1.578 31.022 1.00 12.67 C ANISOU 118 CA VAL A 16 1167 2203 1443 107 515 -118 C ATOM 119 C VAL A 16 24.253 -0.868 32.341 1.00 10.95 C ANISOU 119 C VAL A 16 1111 1627 1420 280 287 70 C ATOM 120 O VAL A 16 23.492 -1.036 33.285 1.00 12.43 O ANISOU 120 O VAL A 16 1253 2008 1463 -93 395 -348 O ATOM 121 CB VAL A 16 24.993 -2.767 30.855 1.00 15.37 C ANISOU 121 CB VAL A 16 2137 1804 1900 263 320 -424 C ATOM 122 CG1 VAL A 16 24.883 -3.683 32.053 1.00 19.48 C ANISOU 122 CG1 VAL A 16 2672 2287 2444 650 801 112 C ATOM 123 CG2 VAL A 16 24.683 -3.491 29.578 1.00 17.89 C ANISOU 123 CG2 VAL A 16 1774 2638 2384 -45 -4 -888 C ATOM 124 N ASP A 17 25.331 -0.083 32.419 1.00 12.88 N ANISOU 124 N ASP A 17 1037 2091 1765 142 449 -130 N ATOM 125 CA ASP A 17 25.629 0.621 33.661 1.00 12.04 C ANISOU 125 CA ASP A 17 871 2069 1633 136 207 112 C ATOM 126 C ASP A 17 24.691 1.802 33.934 1.00 11.57 C ANISOU 126 C ASP A 17 682 2077 1636 20 -193 -308 C ATOM 127 O ASP A 17 24.588 2.205 35.101 1.00 13.54 O ANISOU 127 O ASP A 17 1219 2298 1627 52 -135 -350 O ATOM 128 CB ASP A 17 27.105 0.971 33.715 1.00 14.50 C ANISOU 128 CB ASP A 17 798 2835 1875 268 178 -19 C ATOM 129 CG ASP A 17 27.825 1.484 32.510 1.00 12.72 C ANISOU 129 CG ASP A 17 686 2178 1971 109 63 67 C ATOM 130 OD1 ASP A 17 27.316 1.413 31.364 1.00 15.17 O ANISOU 130 OD1 ASP A 17 1480 2397 1887 -221 -74 -34 O ATOM 131 OD2 ASP A 17 28.967 1.956 32.693 1.00 14.88 O ANISOU 131 OD2 ASP A 17 964 2159 2529 -80 -184 64 O ATOM 132 N ASP A 18 24.038 2.326 32.930 1.00 12.17 N ANISOU 132 N ASP A 18 843 2133 1647 133 -9 -25 N ATOM 133 CA ASP A 18 23.020 3.363 33.154 1.00 11.76 C ANISOU 133 CA ASP A 18 990 1735 1744 -11 45 -34 C ATOM 134 C ASP A 18 21.853 2.783 33.962 1.00 10.41 C ANISOU 134 C ASP A 18 841 1552 1564 111 -69 -210 C ATOM 135 O ASP A 18 21.273 3.451 34.795 1.00 11.03 O ANISOU 135 O ASP A 18 1155 1654 1381 41 -34 -303 O ATOM 136 CB ASP A 18 22.471 3.874 31.842 1.00 12.40 C ANISOU 136 CB ASP A 18 952 1901 1860 67 33 96 C ATOM 137 CG ASP A 18 23.332 4.826 31.045 1.00 13.74 C ANISOU 137 CG ASP A 18 1339 2045 1835 -223 68 65 C ATOM 138 OD1 ASP A 18 24.194 5.499 31.612 1.00 14.43 O ANISOU 138 OD1 ASP A 18 1588 1939 1955 -234 168 -390 O ATOM 139 OD2 ASP A 18 23.038 4.940 29.815 1.00 14.55 O ANISOU 139 OD2 ASP A 18 1563 2063 1903 -173 -155 173 O ATOM 140 N GLU A 19 21.483 1.522 33.666 1.00 10.12 N ANISOU 140 N GLU A 19 933 1491 1422 113 281 -215 N ATOM 141 CA GLU A 19 20.325 0.915 34.291 1.00 10.41 C ANISOU 141 CA GLU A 19 645 1799 1510 31 28 -101 C ATOM 142 C GLU A 19 20.671 -0.014 35.462 1.00 10.50 C ANISOU 142 C GLU A 19 393 1949 1645 -121 -42 81 C ATOM 143 O GLU A 19 19.773 -0.354 36.242 1.00 11.26 O ANISOU 143 O GLU A 19 765 1910 1605 41 224 -52 O ATOM 144 CB GLU A 19 19.564 0.091 33.237 1.00 10.40 C ANISOU 144 CB GLU A 19 1017 1542 1392 79 30 -86 C ATOM 145 CG GLU A 19 18.933 0.901 32.147 1.00 11.71 C ANISOU 145 CG GLU A 19 1244 1748 1458 364 -29 -156 C ATOM 146 CD GLU A 19 17.804 1.810 32.579 1.00 9.79 C ANISOU 146 CD GLU A 19 953 1400 1365 53 -11 -263 C ATOM 147 OE1 GLU A 19 17.303 1.658 33.730 1.00 10.64 O ANISOU 147 OE1 GLU A 19 1169 1398 1476 124 32 -195 O ATOM 148 OE2 GLU A 19 17.411 2.704 31.808 1.00 11.38 O ANISOU 148 OE2 GLU A 19 1049 1744 1530 163 -42 -46 O ATOM 149 N TYR A 20 21.920 -0.427 35.598 1.00 10.99 N ANISOU 149 N TYR A 20 560 2143 1474 -31 -198 -100 N ATOM 150 CA TYR A 20 22.282 -1.393 36.641 1.00 10.20 C ANISOU 150 CA TYR A 20 673 1776 1425 27 -86 -178 C ATOM 151 C TYR A 20 21.914 -0.861 38.020 1.00 9.99 C ANISOU 151 C TYR A 20 613 1659 1524 -69 100 -181 C ATOM 152 O TYR A 20 22.342 0.256 38.360 1.00 10.86 O ANISOU 152 O TYR A 20 1089 1641 1398 -143 -11 -75 O ATOM 153 CB TYR A 20 23.785 -1.674 36.552 1.00 10.88 C ANISOU 153 CB TYR A 20 758 1937 1438 208 -5 -205 C ATOM 154 CG TYR A 20 24.293 -2.757 37.452 1.00 10.71 C ANISOU 154 CG TYR A 20 753 1933 1384 148 33 -163 C ATOM 155 CD1 TYR A 20 23.899 -4.071 37.320 1.00 11.52 C ANISOU 155 CD1 TYR A 20 1086 1939 1352 171 104 -134 C ATOM 156 CD2 TYR A 20 25.203 -2.463 38.456 1.00 13.65 C ANISOU 156 CD2 TYR A 20 1470 2183 1534 68 -307 -119 C ATOM 157 CE1 TYR A 20 24.353 -5.081 38.138 1.00 13.21 C ANISOU 157 CE1 TYR A 20 1245 2027 1747 175 -40 10 C ATOM 158 CE2 TYR A 20 25.683 -3.450 39.281 1.00 14.39 C ANISOU 158 CE2 TYR A 20 2021 2309 1137 533 -391 -471 C ATOM 159 CZ TYR A 20 25.272 -4.751 39.125 1.00 13.68 C ANISOU 159 CZ TYR A 20 1660 2166 1370 628 -125 -208 C ATOM 160 OH TYR A 20 25.735 -5.726 39.952 1.00 17.26 O ANISOU 160 OH TYR A 20 2128 2695 1736 1100 77 241 O ATOM 161 N PRO A 21 21.211 -1.604 38.863 1.00 10.47 N ANISOU 161 N PRO A 21 816 1736 1425 -92 -46 -94 N ATOM 162 CA PRO A 21 20.838 -1.054 40.197 1.00 10.43 C ANISOU 162 CA PRO A 21 894 1757 1314 248 -115 2 C ATOM 163 C PRO A 21 22.057 -0.859 41.092 1.00 10.89 C ANISOU 163 C PRO A 21 941 1868 1329 251 -78 -217 C ATOM 164 O PRO A 21 23.054 -1.537 40.969 1.00 12.30 O ANISOU 164 O PRO A 21 831 2121 1723 239 -47 -133 O ATOM 165 CB PRO A 21 19.916 -2.121 40.734 1.00 12.30 C ANISOU 165 CB PRO A 21 1207 2114 1354 -42 -12 -63 C ATOM 166 CG PRO A 21 20.391 -3.392 40.092 1.00 12.79 C ANISOU 166 CG PRO A 21 1557 1831 1469 -103 6 64 C ATOM 167 CD PRO A 21 20.722 -2.997 38.681 1.00 11.02 C ANISOU 167 CD PRO A 21 946 1699 1543 -100 151 -12 C ATOM 168 N ASP A 22 21.901 0.095 41.999 1.00 12.76 N ANISOU 168 N ASP A 22 1227 2322 1299 188 93 -412 N ATOM 169 CA ASP A 22 22.902 0.418 43.005 1.00 12.26 C ANISOU 169 CA ASP A 22 1258 2096 1303 -55 222 -421 C ATOM 170 C ASP A 22 22.576 -0.432 44.231 1.00 13.26 C ANISOU 170 C ASP A 22 1280 2295 1464 169 88 -170 C ATOM 171 O ASP A 22 21.692 -0.119 45.029 1.00 14.76 O ANISOU 171 O ASP A 22 1515 2794 1301 389 260 103 O ATOM 172 CB ASP A 22 22.864 1.893 43.327 1.00 14.91 C ANISOU 172 CB ASP A 22 1539 2063 2061 -177 164 -438 C ATOM 173 CG ASP A 22 23.794 2.345 44.433 1.00 19.44 C ANISOU 173 CG ASP A 22 1739 2502 3147 -260 -379 -933 C ATOM 174 OD1 ASP A 22 24.510 1.453 44.916 1.00 18.35 O ANISOU 174 OD1 ASP A 22 1776 2902 2295 -167 -127 -646 O ATOM 175 OD2 ASP A 22 23.754 3.553 44.766 1.00 23.72 O ANISOU 175 OD2 ASP A 22 3110 2597 3305 -249 -579 -1063 O ATOM 176 N LEU A 23 23.303 -1.544 44.362 1.00 13.91 N ANISOU 176 N LEU A 23 988 2246 2050 87 -68 -140 N ATOM 177 CA LEU A 23 23.077 -2.483 45.467 1.00 14.96 C ANISOU 177 CA LEU A 23 1544 2242 1899 23 -319 -163 C ATOM 178 C LEU A 23 24.195 -2.459 46.513 1.00 17.18 C ANISOU 178 C LEU A 23 1985 2521 2022 165 -553 -391 C ATOM 179 O LEU A 23 24.389 -3.445 47.226 1.00 19.47 O ANISOU 179 O LEU A 23 2165 2890 2343 541 -730 -114 O ATOM 180 CB LEU A 23 22.884 -3.898 44.911 1.00 16.38 C ANISOU 180 CB LEU A 23 2137 2172 1914 231 -709 -74 C ATOM 181 CG LEU A 23 21.815 -3.987 43.814 1.00 16.14 C ANISOU 181 CG LEU A 23 2104 2171 1860 321 -639 -316 C ATOM 182 CD1 LEU A 23 21.757 -5.412 43.278 1.00 19.98 C ANISOU 182 CD1 LEU A 23 3143 1949 2501 -289 -591 -237 C ATOM 183 CD2 LEU A 23 20.420 -3.601 44.305 1.00 17.74 C ANISOU 183 CD2 LEU A 23 1761 2436 2545 -403 -247 22 C ATOM 184 N SER A 24 24.924 -1.349 46.610 1.00 19.71 N ANISOU 184 N SER A 24 1690 2669 3127 167 -748 -751 N ATOM 185 CA SER A 24 26.049 -1.199 47.509 1.00 24.14 C ANISOU 185 CA SER A 24 1360 4123 3690 -174 -675 -621 C ATOM 186 C SER A 24 25.680 -1.235 48.971 1.00 29.09 C ANISOU 186 C SER A 24 2547 5184 3322 -285 -1212 -531 C ATOM 187 O SER A 24 26.584 -1.408 49.791 1.00 44.95 O ANISOU 187 O SER A 24 3898 8671 4509 -347 -2424 129 O ATOM 188 CB SER A 24 26.840 0.081 47.186 1.00 34.36 C ANISOU 188 CB SER A 24 2840 5250 4964 -1598 -1444 0 C ATOM 189 OG SER A 24 26.023 1.235 47.159 1.00 34.57 O ANISOU 189 OG SER A 24 4327 4398 4411 -1691 -891 480 O ATOM 190 N VAL A 25 24.408 -1.109 49.349 1.00 26.08 N ANISOU 190 N VAL A 25 3002 3901 3006 -972 -349 -565 N ATOM 191 CA VAL A 25 24.185 -1.238 50.791 1.00 27.86 C ANISOU 191 CA VAL A 25 3442 4312 2831 -653 -1104 -251 C ATOM 192 C VAL A 25 23.268 -2.412 51.055 1.00 23.64 C ANISOU 192 C VAL A 25 2805 4375 1802 -447 -1247 -106 C ATOM 193 O VAL A 25 22.733 -2.486 52.155 1.00 28.99 O ANISOU 193 O VAL A 25 4247 4576 2192 -509 -430 -612 O ATOM 194 CB VAL A 25 23.637 0.041 51.447 1.00 31.32 C ANISOU 194 CB VAL A 25 4474 4742 2686 -902 -886 -976 C ATOM 195 CG1 VAL A 25 24.664 1.158 51.302 1.00 36.61 C ANISOU 195 CG1 VAL A 25 6753 4404 2753 -1667 -1390 260 C ATOM 196 CG2 VAL A 25 22.299 0.478 50.872 1.00 31.66 C ANISOU 196 CG2 VAL A 25 5192 4866 1974 487 -387 -419 C ATOM 197 N HIS A 26 23.092 -3.300 50.095 1.00 20.89 N ANISOU 197 N HIS A 26 2007 4059 1871 -129 -734 -110 N ATOM 198 CA HIS A 26 22.066 -4.337 50.185 1.00 20.90 C ANISOU 198 CA HIS A 26 2273 3251 2418 185 -992 97 C ATOM 199 C HIS A 26 22.503 -5.680 50.761 1.00 26.10 C ANISOU 199 C HIS A 26 3709 3581 2626 758 -1181 227 C ATOM 200 O HIS A 26 23.610 -6.143 50.461 1.00 35.45 O ANISOU 200 O HIS A 26 4191 3949 5329 1443 -721 585 O ATOM 201 CB HIS A 26 21.476 -4.528 48.768 1.00 17.19 C ANISOU 201 CB HIS A 26 2132 2288 2109 79 -576 -7 C ATOM 202 CG HIS A 26 20.670 -3.356 48.293 1.00 16.86 C ANISOU 202 CG HIS A 26 2204 2304 1896 108 -560 -1 C ATOM 203 ND1 HIS A 26 21.174 -2.081 48.213 1.00 17.15 N ANISOU 203 ND1 HIS A 26 2092 2387 2037 212 -80 247 N ATOM 204 CD2 HIS A 26 19.385 -3.296 47.841 1.00 16.68 C ANISOU 204 CD2 HIS A 26 2341 2652 1344 156 -619 27 C ATOM 205 CE1 HIS A 26 20.216 -1.277 47.740 1.00 17.31 C ANISOU 205 CE1 HIS A 26 2592 2310 1676 477 -456 -213 C ATOM 206 NE2 HIS A 26 19.120 -1.979 47.513 1.00 18.11 N ANISOU 206 NE2 HIS A 26 2558 2729 1593 405 -624 -20 N ATOM 207 N ASN A 27 21.620 -6.258 51.565 1.00 26.76 N ANISOU 207 N ASN A 27 4070 2924 3173 -194 -1551 197 N ATOM 208 CA ASN A 27 21.739 -7.516 52.253 1.00 27.53 C ANISOU 208 CA ASN A 27 3939 3246 3275 -111 -2465 399 C ATOM 209 C ASN A 27 20.606 -8.475 51.880 1.00 26.56 C ANISOU 209 C ASN A 27 4202 3533 2357 -806 -1009 108 C ATOM 210 O ASN A 27 19.775 -8.874 52.707 1.00 27.87 O ANISOU 210 O ASN A 27 4222 4121 2245 -29 -431 -239 O ATOM 211 CB ASN A 27 21.702 -7.433 53.782 1.00 31.83 C ANISOU 211 CB ASN A 27 5615 3240 3239 -384 -2477 304 C ATOM 212 CG ASN A 27 22.194 -8.697 54.460 1.00 31.06 C ANISOU 212 CG ASN A 27 4793 3966 3042 348 -736 946 C ATOM 213 OD1 ASN A 27 23.266 -9.211 54.112 1.00 41.63 O ANISOU 213 OD1 ASN A 27 5023 6448 4348 1311 -372 1571 O ATOM 214 ND2 ASN A 27 21.471 -9.237 55.451 1.00 42.06 N ANISOU 214 ND2 ASN A 27 6257 7081 2641 1167 -194 2025 N ATOM 215 N ASN A 28 20.607 -8.826 50.605 1.00 17.44 N ANISOU 215 N ASN A 28 2108 2212 2308 218 -738 284 N ATOM 216 CA ASN A 28 19.610 -9.810 50.219 1.00 15.79 C ANISOU 216 CA ASN A 28 1818 2317 1864 132 -285 325 C ATOM 217 C ASN A 28 20.230 -10.749 49.194 1.00 14.79 C ANISOU 217 C ASN A 28 1621 2401 1597 -30 -335 371 C ATOM 218 O ASN A 28 21.293 -10.459 48.687 1.00 15.59 O ANISOU 218 O ASN A 28 1539 2240 2145 53 -282 302 O ATOM 219 CB ASN A 28 18.335 -9.122 49.764 1.00 14.98 C ANISOU 219 CB ASN A 28 2059 2214 1420 141 -481 146 C ATOM 220 CG ASN A 28 18.446 -8.278 48.516 1.00 13.95 C ANISOU 220 CG ASN A 28 1677 2110 1513 -39 -367 134 C ATOM 221 OD1 ASN A 28 18.907 -8.717 47.474 1.00 16.12 O ANISOU 221 OD1 ASN A 28 2033 2398 1694 440 63 459 O ATOM 222 ND2 ASN A 28 18.020 -7.033 48.605 1.00 16.80 N ANISOU 222 ND2 ASN A 28 2477 1951 1955 -130 -119 114 N ATOM 223 N HIS A 29 19.588 -11.889 48.995 1.00 15.35 N ANISOU 223 N HIS A 29 1532 2335 1965 39 -289 236 N ATOM 224 CA HIS A 29 20.200 -12.930 48.188 1.00 15.59 C ANISOU 224 CA HIS A 29 1672 1975 2274 452 -236 649 C ATOM 225 C HIS A 29 20.420 -12.466 46.738 1.00 14.92 C ANISOU 225 C HIS A 29 1815 1643 2212 530 -3 468 C ATOM 226 O HIS A 29 21.436 -12.779 46.143 1.00 16.36 O ANISOU 226 O HIS A 29 1522 2219 2476 532 -108 373 O ATOM 227 CB HIS A 29 19.364 -14.203 48.210 1.00 16.24 C ANISOU 227 CB HIS A 29 1886 2011 2274 392 366 478 C ATOM 228 CG HIS A 29 19.433 -14.981 49.498 1.00 16.55 C ANISOU 228 CG HIS A 29 1644 2138 2507 155 -111 693 C ATOM 229 ND1 HIS A 29 20.547 -15.670 49.830 1.00 19.07 N ANISOU 229 ND1 HIS A 29 1932 2474 2838 462 -218 511 N ATOM 230 CD2 HIS A 29 18.569 -15.195 50.493 1.00 15.80 C ANISOU 230 CD2 HIS A 29 1888 2071 2045 243 -234 561 C ATOM 231 CE1 HIS A 29 20.358 -16.281 50.981 1.00 19.62 C ANISOU 231 CE1 HIS A 29 2230 2725 2501 654 -604 444 C ATOM 232 NE2 HIS A 29 19.156 -16.008 51.420 1.00 18.48 N ANISOU 232 NE2 HIS A 29 2413 2059 2550 531 -213 779 N ATOM 233 N MET A 30 19.432 -11.747 46.212 1.00 13.03 N ANISOU 233 N MET A 30 1333 1797 1821 234 -252 261 N ATOM 234 CA MET A 30 19.546 -11.230 44.853 1.00 12.51 C ANISOU 234 CA MET A 30 1199 1862 1694 87 -270 25 C ATOM 235 C MET A 30 20.818 -10.397 44.712 1.00 13.23 C ANISOU 235 C MET A 30 1203 1933 1889 -4 -317 155 C ATOM 236 O MET A 30 21.603 -10.534 43.770 1.00 13.67 O ANISOU 236 O MET A 30 1583 1882 1729 157 -184 503 O ATOM 237 CB MET A 30 18.292 -10.441 44.519 1.00 12.13 C ANISOU 237 CB MET A 30 1151 2124 1333 129 -202 145 C ATOM 238 CG MET A 30 18.249 -9.807 43.142 1.00 12.43 C ANISOU 238 CG MET A 30 1487 1841 1397 160 -35 126 C ATOM 239 SD MET A 30 19.199 -8.276 42.965 1.00 13.12 S ANISOU 239 SD MET A 30 1521 1821 1641 148 -154 73 S ATOM 240 CE MET A 30 18.213 -7.143 43.986 1.00 14.52 C ANISOU 240 CE MET A 30 1587 2048 1881 19 -127 -333 C ATOM 241 N ALA A 31 21.034 -9.495 45.648 1.00 13.34 N ANISOU 241 N ALA A 31 1499 1824 1745 -128 -227 283 N ATOM 242 CA ALA A 31 22.149 -8.563 45.569 1.00 14.07 C ANISOU 242 CA ALA A 31 1616 2011 1721 -241 -26 5 C ATOM 243 C ALA A 31 23.487 -9.275 45.677 1.00 15.85 C ANISOU 243 C ALA A 31 1510 2864 1649 -152 -634 70 C ATOM 244 O ALA A 31 24.459 -8.809 45.088 1.00 19.02 O ANISOU 244 O ALA A 31 1565 2770 2891 -45 -153 44 O ATOM 245 CB ALA A 31 22.067 -7.459 46.617 1.00 19.60 C ANISOU 245 CB ALA A 31 2154 3104 2190 -430 -414 -897 C ATOM 246 N LYS A 32 23.512 -10.415 46.386 1.00 17.24 N ANISOU 246 N LYS A 32 1585 2933 2032 154 -450 159 N ATOM 247 CA LYS A 32 24.751 -11.168 46.486 1.00 17.95 C ANISOU 247 CA LYS A 32 1436 3445 1939 174 -387 429 C ATOM 248 C LYS A 32 25.121 -11.848 45.159 1.00 17.12 C ANISOU 248 C LYS A 32 1206 3342 1956 267 -331 500 C ATOM 249 O LYS A 32 26.278 -12.200 44.934 1.00 23.90 O ANISOU 249 O LYS A 32 1196 5073 2811 500 -396 -233 O ATOM 250 CB LYS A 32 24.613 -12.242 47.550 1.00 21.92 C ANISOU 250 CB LYS A 32 1946 4218 2166 725 -82 968 C ATOM 251 CG LYS A 32 24.623 -11.647 48.953 1.00 28.73 C ANISOU 251 CG LYS A 32 2993 5818 2107 853 927 687 C ATOM 252 CD LYS A 32 24.677 -12.703 50.001 1.00 34.50 C ANISOU 252 CD LYS A 32 3838 7096 2176 816 317 1346 C ATOM 253 CE LYS A 32 25.938 -13.533 50.060 1.00 39.50 C ANISOU 253 CE LYS A 32 4876 7097 3037 1608 690 1745 C ATOM 254 NZ LYS A 32 25.632 -14.747 50.881 1.00 38.12 N ANISOU 254 NZ LYS A 32 3727 7134 3621 954 721 1689 N ATOM 255 N VAL A 33 24.126 -12.066 44.293 1.00 16.09 N ANISOU 255 N VAL A 33 1386 2440 2287 276 -561 251 N ATOM 256 CA VAL A 33 24.341 -12.756 43.029 1.00 15.97 C ANISOU 256 CA VAL A 33 1140 2522 2408 498 -463 202 C ATOM 257 C VAL A 33 24.460 -11.827 41.832 1.00 15.38 C ANISOU 257 C VAL A 33 1379 2177 2287 478 -291 -49 C ATOM 258 O VAL A 33 25.235 -12.087 40.900 1.00 17.70 O ANISOU 258 O VAL A 33 1688 2474 2561 773 -8 67 O ATOM 259 CB VAL A 33 23.148 -13.713 42.762 1.00 17.58 C ANISOU 259 CB VAL A 33 1742 2443 2496 180 -531 89 C ATOM 260 CG1 VAL A 33 23.222 -14.372 41.394 1.00 18.27 C ANISOU 260 CG1 VAL A 33 2051 2397 2494 361 -411 120 C ATOM 261 CG2 VAL A 33 23.116 -14.756 43.868 1.00 17.10 C ANISOU 261 CG2 VAL A 33 1448 2563 2485 483 8 82 C ATOM 262 N LEU A 34 23.690 -10.751 41.784 1.00 15.25 N ANISOU 262 N LEU A 34 1548 2131 2116 442 188 145 N ATOM 263 CA LEU A 34 23.710 -9.884 40.607 1.00 15.13 C ANISOU 263 CA LEU A 34 1235 2326 2187 489 275 239 C ATOM 264 C LEU A 34 25.097 -9.258 40.441 1.00 15.80 C ANISOU 264 C LEU A 34 1366 2826 1811 159 260 -89 C ATOM 265 O LEU A 34 25.790 -8.833 41.393 1.00 17.42 O ANISOU 265 O LEU A 34 1749 2944 1925 327 -60 -55 O ATOM 266 CB LEU A 34 22.590 -8.830 40.747 1.00 16.66 C ANISOU 266 CB LEU A 34 1486 2613 2229 755 -68 226 C ATOM 267 CG LEU A 34 22.205 -8.188 39.419 1.00 14.52 C ANISOU 267 CG LEU A 34 1230 2355 1930 485 247 152 C ATOM 268 CD1 LEU A 34 21.381 -9.149 38.584 1.00 21.29 C ANISOU 268 CD1 LEU A 34 2698 2309 3080 570 -1071 105 C ATOM 269 CD2 LEU A 34 21.482 -6.886 39.646 1.00 14.71 C ANISOU 269 CD2 LEU A 34 1270 2341 1978 526 160 228 C ATOM 270 N THR A 35 25.524 -9.251 39.180 1.00 14.73 N ANISOU 270 N THR A 35 1114 2659 1823 398 243 -127 N ATOM 271 CA THR A 35 26.749 -8.644 38.724 1.00 13.63 C ANISOU 271 CA THR A 35 1022 2368 1790 439 96 -110 C ATOM 272 C THR A 35 26.449 -7.843 37.464 1.00 13.22 C ANISOU 272 C THR A 35 675 2464 1885 250 -176 -72 C ATOM 273 O THR A 35 25.419 -8.096 36.852 1.00 12.55 O ANISOU 273 O THR A 35 752 2200 1818 165 -56 -382 O ATOM 274 CB THR A 35 27.881 -9.626 38.420 1.00 14.62 C ANISOU 274 CB THR A 35 950 3240 1363 864 -220 -60 C ATOM 275 OG1 THR A 35 27.427 -10.396 37.293 1.00 16.92 O ANISOU 275 OG1 THR A 35 1877 2772 1778 1018 -270 -303 O ATOM 276 CG2 THR A 35 28.158 -10.547 39.601 1.00 18.01 C ANISOU 276 CG2 THR A 35 2125 2932 1785 1017 -190 77 C ATOM 277 N LEU A 36 27.314 -6.899 37.113 1.00 13.74 N ANISOU 277 N LEU A 36 675 2711 1833 84 -215 7 N ATOM 278 CA LEU A 36 27.112 -6.114 35.894 1.00 14.25 C ANISOU 278 CA LEU A 36 851 2539 2026 132 -375 77 C ATOM 279 C LEU A 36 27.020 -7.057 34.697 1.00 15.86 C ANISOU 279 C LEU A 36 1476 2704 1848 243 -357 128 C ATOM 280 O LEU A 36 26.223 -6.886 33.779 1.00 15.43 O ANISOU 280 O LEU A 36 1338 2871 1653 276 -157 -18 O ATOM 281 CB LEU A 36 28.239 -5.092 35.751 1.00 16.69 C ANISOU 281 CB LEU A 36 914 2896 2531 -37 -307 346 C ATOM 282 CG LEU A 36 28.080 -3.985 34.725 1.00 16.85 C ANISOU 282 CG LEU A 36 1140 2363 2899 294 177 165 C ATOM 283 CD1 LEU A 36 26.907 -3.106 35.104 1.00 18.77 C ANISOU 283 CD1 LEU A 36 1103 2674 3355 355 210 -167 C ATOM 284 CD2 LEU A 36 29.331 -3.134 34.687 1.00 19.79 C ANISOU 284 CD2 LEU A 36 1277 2782 3462 28 824 -21 C ATOM 285 N ASP A 37 27.863 -8.094 34.687 1.00 15.52 N ANISOU 285 N ASP A 37 1396 2867 1632 263 -294 3 N ATOM 286 CA ASP A 37 27.903 -9.007 33.555 1.00 16.96 C ANISOU 286 CA ASP A 37 1542 3187 1715 459 -360 -160 C ATOM 287 C ASP A 37 26.627 -9.811 33.423 1.00 15.17 C ANISOU 287 C ASP A 37 1371 2687 1705 694 -170 -354 C ATOM 288 O ASP A 37 26.071 -10.024 32.325 1.00 15.71 O ANISOU 288 O ASP A 37 1636 2597 1736 567 -283 -295 O ATOM 289 CB ASP A 37 29.112 -9.962 33.617 1.00 22.57 C ANISOU 289 CB ASP A 37 1423 3908 3246 730 -280 -738 C ATOM 290 CG ASP A 37 29.549 -10.326 32.209 1.00 29.44 C ANISOU 290 CG ASP A 37 1760 5840 3584 1186 417 -752 C ATOM 291 OD1 ASP A 37 29.158 -9.683 31.212 1.00 31.86 O ANISOU 291 OD1 ASP A 37 3068 5797 3241 856 252 -878 O ATOM 292 OD2 ASP A 37 30.337 -11.265 32.104 1.00 37.43 O ANISOU 292 OD2 ASP A 37 4221 5450 4549 1852 1241 -783 O ATOM 293 N LEU A 38 26.112 -10.299 34.559 1.00 14.81 N ANISOU 293 N LEU A 38 1576 2188 1862 623 -588 34 N ATOM 294 CA LEU A 38 24.867 -11.047 34.539 1.00 14.78 C ANISOU 294 CA LEU A 38 1661 1763 2193 648 -245 -129 C ATOM 295 C LEU A 38 23.712 -10.173 34.079 1.00 12.58 C ANISOU 295 C LEU A 38 1282 1457 2040 245 -115 -29 C ATOM 296 O LEU A 38 22.837 -10.572 33.306 1.00 13.74 O ANISOU 296 O LEU A 38 1336 1916 1970 352 -94 -442 O ATOM 297 CB LEU A 38 24.597 -11.523 35.965 1.00 16.42 C ANISOU 297 CB LEU A 38 1946 2049 2242 545 -418 73 C ATOM 298 CG LEU A 38 23.456 -12.507 36.130 1.00 20.12 C ANISOU 298 CG LEU A 38 2651 2742 2250 -165 -205 52 C ATOM 299 CD1 LEU A 38 23.522 -13.630 35.126 1.00 28.27 C ANISOU 299 CD1 LEU A 38 3592 2996 4153 -17 -1028 -982 C ATOM 300 CD2 LEU A 38 23.481 -13.096 37.563 1.00 31.35 C ANISOU 300 CD2 LEU A 38 4348 4514 3051 -953 -563 1321 C ATOM 301 N TYR A 39 23.715 -8.930 34.566 1.00 12.15 N ANISOU 301 N TYR A 39 1081 1643 1892 323 -104 -187 N ATOM 302 CA TYR A 39 22.670 -7.978 34.201 1.00 11.96 C ANISOU 302 CA TYR A 39 1035 1833 1676 490 12 -417 C ATOM 303 C TYR A 39 22.760 -7.763 32.699 1.00 12.05 C ANISOU 303 C TYR A 39 911 2033 1636 525 -64 -355 C ATOM 304 O TYR A 39 21.747 -7.738 31.996 1.00 12.62 O ANISOU 304 O TYR A 39 993 1917 1884 240 -167 -119 O ATOM 305 CB TYR A 39 22.833 -6.684 35.003 1.00 11.80 C ANISOU 305 CB TYR A 39 1128 1737 1617 421 -56 -271 C ATOM 306 CG TYR A 39 21.681 -5.735 34.854 1.00 10.76 C ANISOU 306 CG TYR A 39 942 1587 1559 297 3 -178 C ATOM 307 CD1 TYR A 39 20.463 -6.027 35.494 1.00 11.57 C ANISOU 307 CD1 TYR A 39 946 1935 1516 230 -84 62 C ATOM 308 CD2 TYR A 39 21.780 -4.572 34.132 1.00 10.36 C ANISOU 308 CD2 TYR A 39 896 1900 1141 266 -17 -68 C ATOM 309 CE1 TYR A 39 19.400 -5.149 35.364 1.00 10.65 C ANISOU 309 CE1 TYR A 39 709 1767 1571 55 79 92 C ATOM 310 CE2 TYR A 39 20.702 -3.707 34.011 1.00 10.35 C ANISOU 310 CE2 TYR A 39 987 1774 1171 300 300 75 C ATOM 311 CZ TYR A 39 19.516 -4.000 34.620 1.00 9.68 C ANISOU 311 CZ TYR A 39 929 1705 1044 253 199 -137 C ATOM 312 OH TYR A 39 18.430 -3.130 34.502 1.00 11.11 O ANISOU 312 OH TYR A 39 852 1688 1683 223 4 -84 O ATOM 313 N LYS A 40 23.965 -7.602 32.159 1.00 11.15 N ANISOU 313 N LYS A 40 866 1778 1595 445 -179 -246 N ATOM 314 CA LYS A 40 24.140 -7.417 30.710 1.00 11.49 C ANISOU 314 CA LYS A 40 733 1975 1657 187 -290 -10 C ATOM 315 C LYS A 40 23.563 -8.552 29.883 1.00 12.52 C ANISOU 315 C LYS A 40 1112 1987 1656 182 -265 -166 C ATOM 316 O LYS A 40 22.945 -8.369 28.822 1.00 12.47 O ANISOU 316 O LYS A 40 985 2155 1599 346 -184 -318 O ATOM 317 CB LYS A 40 25.627 -7.238 30.377 1.00 13.08 C ANISOU 317 CB LYS A 40 810 2391 1771 186 -189 -81 C ATOM 318 CG LYS A 40 25.937 -7.033 28.910 1.00 15.46 C ANISOU 318 CG LYS A 40 936 2983 1953 356 -8 294 C ATOM 319 CD LYS A 40 27.394 -6.690 28.650 1.00 20.57 C ANISOU 319 CD LYS A 40 1015 3951 2849 344 518 67 C ATOM 320 CE LYS A 40 27.780 -6.698 27.167 1.00 28.25 C ANISOU 320 CE LYS A 40 2145 5509 3079 840 1120 841 C ATOM 321 NZ LYS A 40 29.175 -6.191 27.000 1.00 41.43 N ANISOU 321 NZ LYS A 40 2240 8837 4664 448 1705 1833 N ATOM 322 N LYS A 41 23.841 -9.787 30.355 1.00 12.90 N ANISOU 322 N LYS A 41 1217 1959 1726 382 -275 -266 N ATOM 323 CA LYS A 41 23.430 -10.980 29.594 1.00 12.83 C ANISOU 323 CA LYS A 41 1028 2008 1840 134 169 -244 C ATOM 324 C LYS A 41 21.932 -11.151 29.587 1.00 12.50 C ANISOU 324 C LYS A 41 967 2220 1562 266 107 -337 C ATOM 325 O LYS A 41 21.372 -11.573 28.590 1.00 12.44 O ANISOU 325 O LYS A 41 1231 1895 1601 65 42 -176 O ATOM 326 CB LYS A 41 24.132 -12.187 30.246 1.00 14.63 C ANISOU 326 CB LYS A 41 1327 1934 2299 378 -329 -583 C ATOM 327 CG LYS A 41 25.629 -12.169 29.910 1.00 22.53 C ANISOU 327 CG LYS A 41 1371 2681 4507 593 -16 -610 C ATOM 328 CD LYS A 41 26.282 -13.397 30.474 1.00 32.28 C ANISOU 328 CD LYS A 41 2296 3433 6535 1655 -112 -332 C ATOM 329 CE LYS A 41 27.768 -13.497 30.228 1.00 33.88 C ANISOU 329 CE LYS A 41 2188 3615 7069 1423 -191 172 C ATOM 330 NZ LYS A 41 28.365 -14.461 31.215 1.00 51.98 N ANISOU 330 NZ LYS A 41 4111 6611 9029 2544 -2131 1120 N ATOM 331 N LEU A 42 21.283 -10.848 30.695 1.00 11.51 N ANISOU 331 N LEU A 42 1077 1658 1640 335 224 -108 N ATOM 332 CA LEU A 42 19.889 -11.171 30.945 1.00 11.68 C ANISOU 332 CA LEU A 42 1021 1856 1560 415 167 -146 C ATOM 333 C LEU A 42 18.873 -10.051 30.773 1.00 9.50 C ANISOU 333 C LEU A 42 829 1559 1221 100 123 -319 C ATOM 334 O LEU A 42 17.668 -10.339 30.628 1.00 10.44 O ANISOU 334 O LEU A 42 861 1490 1617 89 -88 -122 O ATOM 335 CB LEU A 42 19.740 -11.694 32.393 1.00 12.08 C ANISOU 335 CB LEU A 42 1226 1607 1758 -41 116 105 C ATOM 336 CG LEU A 42 19.994 -13.166 32.648 1.00 14.28 C ANISOU 336 CG LEU A 42 1903 1700 1824 407 -435 -184 C ATOM 337 CD1 LEU A 42 21.375 -13.582 32.175 1.00 19.66 C ANISOU 337 CD1 LEU A 42 2660 1986 2824 652 706 -244 C ATOM 338 CD2 LEU A 42 19.810 -13.481 34.121 1.00 18.66 C ANISOU 338 CD2 LEU A 42 2376 2361 2353 1027 373 775 C ATOM 339 N ARG A 43 19.341 -8.803 30.810 1.00 10.37 N ANISOU 339 N ARG A 43 783 1640 1518 43 -152 -207 N ATOM 340 CA ARG A 43 18.397 -7.687 30.825 1.00 10.12 C ANISOU 340 CA ARG A 43 988 1626 1232 213 -202 -258 C ATOM 341 C ARG A 43 17.586 -7.513 29.528 1.00 9.72 C ANISOU 341 C ARG A 43 995 1643 1055 110 -73 -237 C ATOM 342 O ARG A 43 16.597 -6.789 29.508 1.00 10.45 O ANISOU 342 O ARG A 43 1130 1574 1265 182 -248 -74 O ATOM 343 CB ARG A 43 19.073 -6.369 31.159 1.00 10.19 C ANISOU 343 CB ARG A 43 878 1712 1283 134 -97 -284 C ATOM 344 CG ARG A 43 19.907 -5.789 30.025 1.00 12.23 C ANISOU 344 CG ARG A 43 1261 1862 1523 40 281 -432 C ATOM 345 CD ARG A 43 20.577 -4.506 30.451 1.00 15.38 C ANISOU 345 CD ARG A 43 1939 2058 1847 -452 -295 36 C ATOM 346 NE ARG A 43 21.088 -3.749 29.312 1.00 14.34 N ANISOU 346 NE ARG A 43 1846 1826 1778 -6 131 -184 N ATOM 347 CZ ARG A 43 20.858 -2.503 28.985 1.00 12.97 C ANISOU 347 CZ ARG A 43 1412 1949 1568 74 -372 -95 C ATOM 348 NH1 ARG A 43 20.052 -1.694 29.658 1.00 13.65 N ANISOU 348 NH1 ARG A 43 1603 1797 1788 88 82 195 N ATOM 349 NH2 ARG A 43 21.406 -1.973 27.889 1.00 14.74 N ANISOU 349 NH2 ARG A 43 1786 1731 2082 275 144 2 N ATOM 350 N ASP A 44 17.976 -8.166 28.458 1.00 10.32 N ANISOU 350 N ASP A 44 1086 1664 1170 -73 8 -304 N ATOM 351 CA ASP A 44 17.301 -8.128 27.155 1.00 9.56 C ANISOU 351 CA ASP A 44 1345 1209 1076 5 34 -419 C ATOM 352 C ASP A 44 16.273 -9.241 26.962 1.00 10.06 C ANISOU 352 C ASP A 44 1258 1323 1243 -7 -84 -304 C ATOM 353 O ASP A 44 15.648 -9.287 25.912 1.00 12.52 O ANISOU 353 O ASP A 44 1366 2009 1383 -2 -243 -444 O ATOM 354 CB ASP A 44 18.341 -8.211 26.042 1.00 10.62 C ANISOU 354 CB ASP A 44 1326 1515 1194 -10 116 -339 C ATOM 355 CG ASP A 44 19.277 -9.408 26.023 1.00 10.62 C ANISOU 355 CG ASP A 44 1280 1589 1166 27 129 -253 C ATOM 356 OD1 ASP A 44 19.314 -10.168 27.042 1.00 11.97 O ANISOU 356 OD1 ASP A 44 1313 1988 1248 13 22 -26 O ATOM 357 OD2 ASP A 44 20.003 -9.597 24.990 1.00 11.54 O ANISOU 357 OD2 ASP A 44 1152 1912 1319 132 190 -207 O ATOM 358 N ARG A 45 16.106 -10.060 27.980 1.00 10.38 N ANISOU 358 N ARG A 45 961 1520 1464 18 29 -185 N ATOM 359 CA ARG A 45 15.177 -11.167 27.899 1.00 9.64 C ANISOU 359 CA ARG A 45 1151 1482 1031 -62 -5 -293 C ATOM 360 C ARG A 45 13.807 -10.762 28.433 1.00 9.63 C ANISOU 360 C ARG A 45 1068 1576 1017 19 -34 -110 C ATOM 361 O ARG A 45 13.662 -9.868 29.266 1.00 11.64 O ANISOU 361 O ARG A 45 1205 1743 1473 -143 211 -441 O ATOM 362 CB ARG A 45 15.660 -12.335 28.767 1.00 9.66 C ANISOU 362 CB ARG A 45 921 1626 1123 -61 -63 -196 C ATOM 363 CG ARG A 45 16.992 -12.943 28.340 1.00 11.28 C ANISOU 363 CG ARG A 45 1350 1777 1157 230 202 -222 C ATOM 364 CD ARG A 45 17.338 -14.136 29.246 1.00 11.77 C ANISOU 364 CD ARG A 45 1359 2039 1075 353 -16 -189 C ATOM 365 NE ARG A 45 18.684 -14.592 28.930 1.00 12.72 N ANISOU 365 NE ARG A 45 1534 2019 1279 466 92 -422 N ATOM 366 CZ ARG A 45 19.300 -15.553 29.600 1.00 16.84 C ANISOU 366 CZ ARG A 45 1620 2607 2169 879 571 236 C ATOM 367 NH1 ARG A 45 18.669 -16.126 30.614 1.00 19.47 N ANISOU 367 NH1 ARG A 45 2027 3251 2118 1237 717 577 N ATOM 368 NH2 ARG A 45 20.521 -15.916 29.247 1.00 22.28 N ANISOU 368 NH2 ARG A 45 1687 2959 3818 1006 1007 950 N ATOM 369 N GLN A 46 12.777 -11.476 27.982 1.00 10.05 N ANISOU 369 N GLN A 46 1124 1461 1233 111 -14 -196 N ATOM 370 CA GLN A 46 11.463 -11.369 28.605 1.00 10.31 C ANISOU 370 CA GLN A 46 1043 1508 1365 108 74 -296 C ATOM 371 C GLN A 46 10.799 -12.732 28.476 1.00 9.30 C ANISOU 371 C GLN A 46 1040 1550 943 171 -110 -327 C ATOM 372 O GLN A 46 10.995 -13.397 27.483 1.00 11.75 O ANISOU 372 O GLN A 46 1462 1730 1271 175 216 -561 O ATOM 373 CB GLN A 46 10.585 -10.271 28.029 1.00 11.36 C ANISOU 373 CB GLN A 46 934 1507 1876 0 58 -133 C ATOM 374 CG GLN A 46 10.065 -10.521 26.616 1.00 15.87 C ANISOU 374 CG GLN A 46 1622 2053 2355 -138 -774 -165 C ATOM 375 CD GLN A 46 9.437 -9.287 25.979 1.00 20.19 C ANISOU 375 CD GLN A 46 3725 2146 1802 671 -651 -458 C ATOM 376 OE1 GLN A 46 8.795 -8.512 26.695 1.00 22.83 O ANISOU 376 OE1 GLN A 46 3846 2808 2021 1156 -659 -621 O ATOM 377 NE2 GLN A 46 9.598 -9.084 24.668 1.00 26.01 N ANISOU 377 NE2 GLN A 46 4905 3110 1869 1713 -526 -320 N ATOM 378 N THR A 47 10.024 -13.053 29.509 1.00 9.82 N ANISOU 378 N THR A 47 1160 1646 927 -33 -94 -350 N ATOM 379 CA THR A 47 9.187 -14.252 29.397 1.00 10.24 C ANISOU 379 CA THR A 47 1195 1252 1443 162 -43 -418 C ATOM 380 C THR A 47 8.039 -14.057 28.389 1.00 11.00 C ANISOU 380 C THR A 47 1150 1385 1645 220 -182 -588 C ATOM 381 O THR A 47 7.811 -12.957 27.903 1.00 10.71 O ANISOU 381 O THR A 47 1062 1531 1475 209 -45 -384 O ATOM 382 CB THR A 47 8.594 -14.705 30.744 1.00 10.57 C ANISOU 382 CB THR A 47 959 1449 1607 26 56 -379 C ATOM 383 OG1 THR A 47 7.568 -13.740 31.042 1.00 10.91 O ANISOU 383 OG1 THR A 47 1168 1382 1595 75 87 -269 O ATOM 384 CG2 THR A 47 9.620 -14.777 31.847 1.00 11.17 C ANISOU 384 CG2 THR A 47 1332 1385 1526 84 -80 -244 C ATOM 385 N SER A 48 7.294 -15.134 28.137 1.00 11.85 N ANISOU 385 N SER A 48 1391 1522 1591 42 -135 -566 N ATOM 386 CA SER A 48 6.133 -15.084 27.230 1.00 12.41 C ANISOU 386 CA SER A 48 1203 1663 1849 -15 -125 -504 C ATOM 387 C SER A 48 4.998 -14.227 27.751 1.00 12.78 C ANISOU 387 C SER A 48 1317 1528 2012 28 -441 -896 C ATOM 388 O SER A 48 4.045 -13.958 27.009 1.00 16.35 O ANISOU 388 O SER A 48 1403 2804 2007 478 -432 -982 O ATOM 389 CB SER A 48 5.667 -16.515 26.943 1.00 19.27 C ANISOU 389 CB SER A 48 1660 1581 4082 546 -1193 -1321 C ATOM 390 OG SER A 48 6.712 -17.196 26.218 1.00 30.89 O ANISOU 390 OG SER A 48 2535 3468 5734 954 -921 -2981 O ATOM 391 N SER A 49 5.044 -13.738 28.992 1.00 11.20 N ANISOU 391 N SER A 49 1153 1373 1729 84 -224 -402 N ATOM 392 CA SER A 49 4.088 -12.790 29.533 1.00 10.47 C ANISOU 392 CA SER A 49 1096 1477 1407 44 -142 -291 C ATOM 393 C SER A 49 4.730 -11.402 29.656 1.00 9.43 C ANISOU 393 C SER A 49 1000 1499 1085 24 -194 -330 C ATOM 394 O SER A 49 4.108 -10.484 30.191 1.00 10.68 O ANISOU 394 O SER A 49 1142 1513 1405 -132 155 -345 O ATOM 395 CB SER A 49 3.540 -13.164 30.908 1.00 11.40 C ANISOU 395 CB SER A 49 1218 1626 1489 117 -188 19 C ATOM 396 OG SER A 49 4.527 -13.017 31.900 1.00 10.22 O ANISOU 396 OG SER A 49 1084 1389 1409 -23 -65 -136 O ATOM 397 N GLY A 50 5.969 -11.200 29.203 1.00 10.77 N ANISOU 397 N GLY A 50 1005 1623 1465 -18 -85 -297 N ATOM 398 CA GLY A 50 6.618 -9.899 29.304 1.00 9.46 C ANISOU 398 CA GLY A 50 962 1592 1039 13 12 -139 C ATOM 399 C GLY A 50 7.468 -9.706 30.522 1.00 8.99 C ANISOU 399 C GLY A 50 873 1405 1136 -55 10 -17 C ATOM 400 O GLY A 50 8.023 -8.598 30.680 1.00 10.69 O ANISOU 400 O GLY A 50 1287 1248 1526 -143 -64 -2 O ATOM 401 N PHE A 51 7.565 -10.674 31.410 1.00 9.36 N ANISOU 401 N PHE A 51 1173 1277 1106 -45 -23 -83 N ATOM 402 CA PHE A 51 8.294 -10.451 32.697 1.00 8.89 C ANISOU 402 CA PHE A 51 843 1453 1081 74 58 -25 C ATOM 403 C PHE A 51 9.792 -10.375 32.433 1.00 8.85 C ANISOU 403 C PHE A 51 889 1216 1259 148 51 -22 C ATOM 404 O PHE A 51 10.352 -11.213 31.724 1.00 10.25 O ANISOU 404 O PHE A 51 860 1529 1506 12 132 -239 O ATOM 405 CB PHE A 51 7.916 -11.558 33.676 1.00 9.44 C ANISOU 405 CB PHE A 51 911 1422 1253 37 -77 79 C ATOM 406 CG PHE A 51 8.066 -11.187 35.139 1.00 9.66 C ANISOU 406 CG PHE A 51 1099 1394 1180 191 26 211 C ATOM 407 CD1 PHE A 51 7.120 -10.345 35.719 1.00 10.40 C ANISOU 407 CD1 PHE A 51 1262 1473 1215 215 127 171 C ATOM 408 CD2 PHE A 51 9.107 -11.658 35.911 1.00 9.81 C ANISOU 408 CD2 PHE A 51 1168 1390 1168 85 -43 145 C ATOM 409 CE1 PHE A 51 7.217 -10.018 37.066 1.00 9.76 C ANISOU 409 CE1 PHE A 51 1322 1069 1318 123 30 142 C ATOM 410 CE2 PHE A 51 9.193 -11.335 37.252 1.00 9.77 C ANISOU 410 CE2 PHE A 51 1135 1378 1201 115 -119 56 C ATOM 411 CZ PHE A 51 8.233 -10.523 37.827 1.00 10.85 C ANISOU 411 CZ PHE A 51 1273 1503 1348 163 -59 -19 C ATOM 412 N THR A 52 10.484 -9.396 32.984 1.00 9.66 N ANISOU 412 N THR A 52 928 1388 1355 29 -8 -86 N ATOM 413 CA THR A 52 11.889 -9.134 32.778 1.00 9.36 C ANISOU 413 CA THR A 52 892 1402 1263 169 57 -9 C ATOM 414 C THR A 52 12.714 -9.301 34.043 1.00 9.16 C ANISOU 414 C THR A 52 899 1353 1227 102 54 -204 C ATOM 415 O THR A 52 12.204 -9.419 35.162 1.00 9.97 O ANISOU 415 O THR A 52 1109 1449 1231 -50 174 -135 O ATOM 416 CB THR A 52 12.094 -7.696 32.254 1.00 9.90 C ANISOU 416 CB THR A 52 1197 1459 1105 -61 50 -119 C ATOM 417 OG1 THR A 52 11.766 -6.821 33.320 1.00 11.65 O ANISOU 417 OG1 THR A 52 1051 1691 1684 24 -36 -534 O ATOM 418 CG2 THR A 52 11.199 -7.390 31.080 1.00 11.15 C ANISOU 418 CG2 THR A 52 1354 1713 1171 354 157 189 C ATOM 419 N LEU A 53 14.035 -9.256 33.840 1.00 8.86 N ANISOU 419 N LEU A 53 906 1330 1130 246 39 -263 N ATOM 420 CA LEU A 53 14.946 -9.315 34.993 1.00 9.02 C ANISOU 420 CA LEU A 53 893 1300 1234 273 -17 -248 C ATOM 421 C LEU A 53 14.696 -8.115 35.919 1.00 8.17 C ANISOU 421 C LEU A 53 767 1225 1112 73 -170 -181 C ATOM 422 O LEU A 53 14.699 -8.280 37.132 1.00 9.58 O ANISOU 422 O LEU A 53 1034 1561 1043 264 -165 -136 O ATOM 423 CB LEU A 53 16.396 -9.337 34.564 1.00 10.47 C ANISOU 423 CB LEU A 53 907 1579 1492 201 38 -163 C ATOM 424 CG LEU A 53 17.449 -9.417 35.675 1.00 11.59 C ANISOU 424 CG LEU A 53 785 1877 1740 229 -74 -258 C ATOM 425 CD1 LEU A 53 17.286 -10.701 36.481 1.00 12.94 C ANISOU 425 CD1 LEU A 53 1227 2055 1636 461 -120 -95 C ATOM 426 CD2 LEU A 53 18.832 -9.260 35.096 1.00 14.49 C ANISOU 426 CD2 LEU A 53 931 2919 1656 -92 3 -589 C ATOM 427 N ASP A 54 14.475 -6.922 35.387 1.00 9.84 N ANISOU 427 N ASP A 54 1199 1290 1250 236 -15 -119 N ATOM 428 CA ASP A 54 14.181 -5.771 36.252 1.00 9.54 C ANISOU 428 CA ASP A 54 787 1268 1571 154 76 -152 C ATOM 429 C ASP A 54 12.948 -6.089 37.078 1.00 8.28 C ANISOU 429 C ASP A 54 701 1235 1211 205 -193 -120 C ATOM 430 O ASP A 54 12.890 -5.742 38.254 1.00 9.55 O ANISOU 430 O ASP A 54 1019 1357 1254 -5 -58 -223 O ATOM 431 CB ASP A 54 13.985 -4.518 35.412 1.00 10.59 C ANISOU 431 CB ASP A 54 887 1338 1800 226 44 19 C ATOM 432 CG ASP A 54 15.247 -3.794 34.997 1.00 10.20 C ANISOU 432 CG ASP A 54 905 1228 1744 368 336 -62 C ATOM 433 OD1 ASP A 54 16.321 -4.114 35.550 1.00 9.96 O ANISOU 433 OD1 ASP A 54 1047 1411 1326 139 100 -84 O ATOM 434 OD2 ASP A 54 15.123 -2.913 34.107 1.00 10.59 O ANISOU 434 OD2 ASP A 54 967 1365 1693 190 -2 -4 O ATOM 435 N ASP A 55 11.973 -6.749 36.515 1.00 8.86 N ANISOU 435 N ASP A 55 869 1326 1172 64 -54 -165 N ATOM 436 CA ASP A 55 10.737 -7.141 37.201 1.00 9.77 C ANISOU 436 CA ASP A 55 781 1435 1495 141 -88 -15 C ATOM 437 C ASP A 55 11.043 -8.142 38.319 1.00 8.43 C ANISOU 437 C ASP A 55 551 1394 1260 116 2 -156 C ATOM 438 O ASP A 55 10.502 -8.027 39.399 1.00 10.11 O ANISOU 438 O ASP A 55 1097 1416 1329 153 307 -86 O ATOM 439 CB ASP A 55 9.723 -7.707 36.234 1.00 9.16 C ANISOU 439 CB ASP A 55 732 1355 1393 125 -83 45 C ATOM 440 CG ASP A 55 9.203 -6.736 35.188 1.00 9.35 C ANISOU 440 CG ASP A 55 968 1351 1233 -50 -21 51 C ATOM 441 OD1 ASP A 55 9.126 -5.518 35.458 1.00 13.27 O ANISOU 441 OD1 ASP A 55 1340 1176 2525 -85 -726 61 O ATOM 442 OD2 ASP A 55 8.813 -7.263 34.117 1.00 12.35 O ANISOU 442 OD2 ASP A 55 1530 1903 1261 324 -155 -241 O ATOM 443 N VAL A 56 11.882 -9.106 38.025 1.00 9.01 N ANISOU 443 N VAL A 56 783 1429 1211 246 51 -81 N ATOM 444 CA VAL A 56 12.297 -10.092 39.011 1.00 9.74 C ANISOU 444 CA VAL A 56 902 1407 1392 245 -163 -92 C ATOM 445 C VAL A 56 12.939 -9.418 40.236 1.00 10.28 C ANISOU 445 C VAL A 56 966 1632 1310 -15 -128 -18 C ATOM 446 O VAL A 56 12.644 -9.782 41.401 1.00 10.71 O ANISOU 446 O VAL A 56 1199 1506 1364 -32 -29 -48 O ATOM 447 CB VAL A 56 13.310 -11.082 38.390 1.00 9.33 C ANISOU 447 CB VAL A 56 669 1345 1533 112 23 76 C ATOM 448 CG1 VAL A 56 13.989 -11.925 39.469 1.00 11.83 C ANISOU 448 CG1 VAL A 56 1019 1776 1699 533 400 479 C ATOM 449 CG2 VAL A 56 12.668 -11.992 37.363 1.00 11.91 C ANISOU 449 CG2 VAL A 56 1081 1641 1804 -129 358 -408 C ATOM 450 N ILE A 57 13.826 -8.471 40.008 1.00 9.54 N ANISOU 450 N ILE A 57 942 1339 1345 192 -109 -36 N ATOM 451 CA ILE A 57 14.700 -7.958 41.086 1.00 9.21 C ANISOU 451 CA ILE A 57 883 1354 1264 98 -9 -2 C ATOM 452 C ILE A 57 14.157 -6.715 41.775 1.00 10.07 C ANISOU 452 C ILE A 57 950 1421 1454 108 149 -113 C ATOM 453 O ILE A 57 14.759 -6.302 42.772 1.00 10.25 O ANISOU 453 O ILE A 57 984 1414 1495 68 124 -161 O ATOM 454 CB ILE A 57 16.134 -7.675 40.581 1.00 9.66 C ANISOU 454 CB ILE A 57 851 1130 1687 181 35 -36 C ATOM 455 CG1 ILE A 57 16.154 -6.459 39.673 1.00 10.15 C ANISOU 455 CG1 ILE A 57 1115 1064 1675 59 205 -119 C ATOM 456 CG2 ILE A 57 16.759 -8.916 39.917 1.00 10.94 C ANISOU 456 CG2 ILE A 57 1097 1170 1889 281 225 51 C ATOM 457 CD1 ILE A 57 17.556 -6.080 39.203 1.00 12.12 C ANISOU 457 CD1 ILE A 57 953 1808 1843 -146 -95 228 C ATOM 458 N GLN A 58 13.099 -6.091 41.273 1.00 10.11 N ANISOU 458 N GLN A 58 1317 1216 1308 136 -34 -156 N ATOM 459 CA GLN A 58 12.705 -4.799 41.799 1.00 9.55 C ANISOU 459 CA GLN A 58 1232 1213 1184 199 -56 -27 C ATOM 460 C GLN A 58 12.530 -4.773 43.308 1.00 9.55 C ANISOU 460 C GLN A 58 1229 1181 1217 188 -74 -63 C ATOM 461 O GLN A 58 12.968 -3.830 43.962 1.00 10.72 O ANISOU 461 O GLN A 58 1165 1514 1395 -91 -122 -185 O ATOM 462 CB GLN A 58 11.381 -4.314 41.202 1.00 10.56 C ANISOU 462 CB GLN A 58 1184 1425 1401 168 -149 -78 C ATOM 463 CG GLN A 58 11.069 -2.860 41.523 1.00 10.13 C ANISOU 463 CG GLN A 58 868 1447 1534 161 -175 -150 C ATOM 464 CD GLN A 58 12.073 -1.920 40.914 1.00 10.04 C ANISOU 464 CD GLN A 58 939 1490 1384 120 -127 -146 C ATOM 465 OE1 GLN A 58 12.196 -1.825 39.681 1.00 12.55 O ANISOU 465 OE1 GLN A 58 1962 1502 1305 -71 -256 -81 O ATOM 466 NE2 GLN A 58 12.794 -1.186 41.718 1.00 10.00 N ANISOU 466 NE2 GLN A 58 1320 1327 1150 13 32 -138 N ATOM 467 N THR A 59 11.910 -5.785 43.896 1.00 10.48 N ANISOU 467 N THR A 59 1348 1384 1250 16 119 -101 N ATOM 468 CA THR A 59 11.706 -5.766 45.357 1.00 11.01 C ANISOU 468 CA THR A 59 1134 1735 1314 -56 362 -370 C ATOM 469 C THR A 59 13.042 -5.790 46.103 1.00 12.11 C ANISOU 469 C THR A 59 1452 1839 1312 78 24 -209 C ATOM 470 O THR A 59 13.167 -5.155 47.173 1.00 12.59 O ANISOU 470 O THR A 59 1739 1719 1326 -118 157 -194 O ATOM 471 CB THR A 59 10.800 -6.916 45.810 1.00 12.51 C ANISOU 471 CB THR A 59 1809 1739 1205 -269 145 -83 C ATOM 472 OG1 THR A 59 10.574 -6.695 47.236 1.00 14.39 O ANISOU 472 OG1 THR A 59 2363 1901 1203 -358 224 -61 O ATOM 473 CG2 THR A 59 11.309 -8.312 45.575 1.00 12.88 C ANISOU 473 CG2 THR A 59 1666 1802 1427 -412 167 -181 C ATOM 474 N GLY A 60 14.032 -6.488 45.569 1.00 11.23 N ANISOU 474 N GLY A 60 1413 1528 1327 135 -140 -74 N ATOM 475 CA GLY A 60 15.357 -6.537 46.163 1.00 10.43 C ANISOU 475 CA GLY A 60 1450 1564 949 35 -92 -34 C ATOM 476 C GLY A 60 16.156 -5.275 45.963 1.00 12.67 C ANISOU 476 C GLY A 60 1683 1689 1441 -163 -406 115 C ATOM 477 O GLY A 60 17.084 -5.019 46.734 1.00 17.60 O ANISOU 477 O GLY A 60 2539 1983 2165 -616 -1164 447 O ATOM 478 N VAL A 61 15.864 -4.449 44.967 1.00 11.02 N ANISOU 478 N VAL A 61 1249 1424 1512 80 -149 -9 N ATOM 479 CA VAL A 61 16.485 -3.123 44.810 1.00 11.12 C ANISOU 479 CA VAL A 61 1324 1529 1373 54 -98 -25 C ATOM 480 C VAL A 61 15.857 -2.192 45.849 1.00 11.21 C ANISOU 480 C VAL A 61 1439 1471 1349 26 -224 -57 C ATOM 481 O VAL A 61 16.550 -1.430 46.540 1.00 13.12 O ANISOU 481 O VAL A 61 1860 1756 1368 -208 -293 -142 O ATOM 482 CB VAL A 61 16.311 -2.593 43.388 1.00 10.85 C ANISOU 482 CB VAL A 61 1095 1597 1432 133 44 55 C ATOM 483 CG1 VAL A 61 16.947 -1.191 43.266 1.00 11.14 C ANISOU 483 CG1 VAL A 61 1360 1660 1213 -64 -45 1 C ATOM 484 CG2 VAL A 61 16.872 -3.573 42.355 1.00 12.21 C ANISOU 484 CG2 VAL A 61 1406 1872 1359 -231 -112 -323 C ATOM 485 N ASP A 62 14.518 -2.261 45.989 1.00 11.39 N ANISOU 485 N ASP A 62 1535 1369 1425 34 69 -170 N ATOM 486 CA ASP A 62 13.849 -1.372 46.903 1.00 12.21 C ANISOU 486 CA ASP A 62 1730 1531 1380 167 -10 -156 C ATOM 487 C ASP A 62 14.091 -1.699 48.367 1.00 13.25 C ANISOU 487 C ASP A 62 1756 1912 1367 391 131 -81 C ATOM 488 O ASP A 62 13.959 -0.782 49.179 1.00 15.75 O ANISOU 488 O ASP A 62 2509 2033 1443 506 -577 -261 O ATOM 489 CB ASP A 62 12.350 -1.430 46.633 1.00 12.10 C ANISOU 489 CB ASP A 62 1609 1780 1208 69 259 -47 C ATOM 490 CG ASP A 62 11.916 -0.838 45.315 1.00 10.64 C ANISOU 490 CG ASP A 62 1382 1442 1220 257 254 -208 C ATOM 491 OD1 ASP A 62 12.776 -0.507 44.449 1.00 11.72 O ANISOU 491 OD1 ASP A 62 1407 1831 1217 116 178 -59 O ATOM 492 OD2 ASP A 62 10.669 -0.697 45.106 1.00 13.73 O ANISOU 492 OD2 ASP A 62 1347 2093 1778 -14 127 138 O ATOM 493 N ASN A 63 14.374 -2.940 48.703 1.00 13.04 N ANISOU 493 N ASN A 63 1948 1869 1139 182 -121 -196 N ATOM 494 CA ASN A 63 14.495 -3.390 50.095 1.00 12.88 C ANISOU 494 CA ASN A 63 1822 1832 1240 123 -86 -123 C ATOM 495 C ASN A 63 15.870 -3.952 50.360 1.00 14.24 C ANISOU 495 C ASN A 63 1803 1834 1773 -50 -347 67 C ATOM 496 O ASN A 63 16.095 -5.124 50.125 1.00 17.19 O ANISOU 496 O ASN A 63 2028 1894 2609 254 -348 18 O ATOM 497 CB ASN A 63 13.403 -4.435 50.334 1.00 13.34 C ANISOU 497 CB ASN A 63 1794 1833 1442 94 -313 -29 C ATOM 498 CG ASN A 63 12.014 -3.861 50.164 1.00 14.82 C ANISOU 498 CG ASN A 63 1816 1830 1987 163 -216 -40 C ATOM 499 OD1 ASN A 63 11.563 -3.078 50.991 1.00 16.42 O ANISOU 499 OD1 ASN A 63 2061 1826 2354 244 -197 -219 O ATOM 500 ND2 ASN A 63 11.287 -4.181 49.110 1.00 13.29 N ANISOU 500 ND2 ASN A 63 1350 1956 1744 331 -1 162 N ATOM 501 N PRO A 64 16.802 -3.105 50.770 1.00 16.79 N ANISOU 501 N PRO A 64 2168 2418 1791 -435 -578 83 N ATOM 502 CA PRO A 64 18.174 -3.557 50.960 1.00 18.73 C ANISOU 502 CA PRO A 64 1990 2675 2453 -698 -534 442 C ATOM 503 C PRO A 64 18.326 -4.639 52.044 1.00 27.62 C ANISOU 503 C PRO A 64 2522 4639 3332 -1109 -1892 1770 C ATOM 504 O PRO A 64 19.332 -5.339 51.964 1.00 39.21 O ANISOU 504 O PRO A 64 3140 5816 5943 -118 -2178 2885 O ATOM 505 CB PRO A 64 18.952 -2.277 51.333 1.00 23.05 C ANISOU 505 CB PRO A 64 2254 3151 3354 -769 -250 -800 C ATOM 506 CG PRO A 64 17.975 -1.154 51.335 1.00 23.90 C ANISOU 506 CG PRO A 64 2659 2952 3468 -739 -914 -534 C ATOM 507 CD PRO A 64 16.612 -1.674 51.008 1.00 21.51 C ANISOU 507 CD PRO A 64 2635 2500 3037 -562 -1013 -612 C ATOM 508 N GLY A 65 17.355 -4.761 52.932 1.00 38.56 N ANISOU 508 N GLY A 65 4646 6811 3193 -728 -867 2898 N ATOM 509 CA GLY A 65 17.282 -5.713 54.023 1.00 47.98 C ANISOU 509 CA GLY A 65 6241 8435 3555 -504 -1372 3827 C ATOM 510 C GLY A 65 18.071 -5.271 55.240 1.00 53.55 C ANISOU 510 C GLY A 65 7307 9734 3305 -99 -1331 2990 C ATOM 511 O GLY A 65 18.681 -4.198 55.333 1.00 59.86 O ANISOU 511 O GLY A 65 9184 10171 3390 -891 -1934 2368 O ATOM 512 N HIS A 66 18.083 -6.134 56.252 1.00 56.53 N ANISOU 512 N HIS A 66 7850 10241 3389 649 -1636 3236 N ATOM 513 CA HIS A 66 18.870 -5.797 57.440 1.00 57.75 C ANISOU 513 CA HIS A 66 7727 10921 3295 527 -1378 2737 C ATOM 514 C HIS A 66 20.123 -6.662 57.430 1.00 58.57 C ANISOU 514 C HIS A 66 7206 10613 4437 44 -2083 1671 C ATOM 515 O HIS A 66 20.065 -7.785 56.920 1.00 57.05 O ANISOU 515 O HIS A 66 6642 8455 6580 -1287 -1206 3678 O ATOM 516 CB HIS A 66 18.074 -5.983 58.729 1.00 65.30 C ANISOU 516 CB HIS A 66 8911 12251 3649 -661 -581 1359 C ATOM 517 CG HIS A 66 18.229 -4.802 59.642 1.00 71.23 C ANISOU 517 CG HIS A 66 9430 12806 4828 -288 -907 514 C ATOM 518 ND1 HIS A 66 17.664 -3.578 59.352 1.00 72.39 N ANISOU 518 ND1 HIS A 66 9249 13033 5223 169 -754 137 N ATOM 519 CD2 HIS A 66 18.887 -4.648 60.811 1.00 72.41 C ANISOU 519 CD2 HIS A 66 9803 12910 4801 -168 -925 169 C ATOM 520 CE1 HIS A 66 17.961 -2.723 60.314 1.00 74.22 C ANISOU 520 CE1 HIS A 66 9793 13034 5372 -16 -978 159 C ATOM 521 NE2 HIS A 66 18.706 -3.347 61.213 1.00 74.65 N ANISOU 521 NE2 HIS A 66 10082 12881 5399 -44 -1108 141 N ATOM 522 N PRO A 67 21.241 -6.194 57.970 1.00 68.86 N ANISOU 522 N PRO A 67 8038 11460 6665 -24 -3262 894 N ATOM 523 CA PRO A 67 22.507 -6.925 57.931 1.00 70.69 C ANISOU 523 CA PRO A 67 7852 11447 7561 -132 -4137 588 C ATOM 524 C PRO A 67 22.475 -8.264 58.661 1.00 68.88 C ANISOU 524 C PRO A 67 7582 11120 7470 -288 -4055 255 C ATOM 525 O PRO A 67 23.439 -9.022 58.538 1.00 63.52 O ANISOU 525 O PRO A 67 7545 9497 7093 -1158 -4111 -1399 O ATOM 526 CB PRO A 67 23.477 -6.001 58.686 1.00 72.32 C ANISOU 526 CB PRO A 67 8305 11028 8144 -342 -3788 219 C ATOM 527 CG PRO A 67 22.571 -5.213 59.584 1.00 73.28 C ANISOU 527 CG PRO A 67 8294 11476 8072 -118 -3750 311 C ATOM 528 CD PRO A 67 21.391 -4.911 58.686 1.00 72.44 C ANISOU 528 CD PRO A 67 8448 11731 7346 -23 -3514 491 C ATOM 529 N PHE A 68 21.407 -8.506 59.396 1.00 67.40 N ANISOU 529 N PHE A 68 7495 11277 6837 -197 -4276 104 N ATOM 530 CA PHE A 68 21.138 -9.720 60.133 1.00 68.18 C ANISOU 530 CA PHE A 68 7813 11335 6756 321 -3496 152 C ATOM 531 C PHE A 68 20.347 -10.732 59.321 1.00 69.13 C ANISOU 531 C PHE A 68 8375 11397 6494 -606 -3113 608 C ATOM 532 O PHE A 68 20.927 -11.653 58.735 1.00 71.94 O ANISOU 532 O PHE A 68 7434 11926 7973 -476 -4190 -515 O ATOM 533 CB PHE A 68 20.400 -9.358 61.434 1.00 71.03 C ANISOU 533 CB PHE A 68 8148 11401 7439 531 -2978 -146 C ATOM 534 CG PHE A 68 21.377 -8.878 62.501 1.00 67.46 C ANISOU 534 CG PHE A 68 7442 10939 7249 1163 -2478 -794 C ATOM 535 CD1 PHE A 68 22.614 -8.369 62.142 1.00 67.30 C ANISOU 535 CD1 PHE A 68 7656 10799 7117 1019 -2449 -615 C ATOM 536 CD2 PHE A 68 21.061 -8.937 63.844 1.00 66.96 C ANISOU 536 CD2 PHE A 68 7146 10961 7334 1348 -2342 -887 C ATOM 537 CE1 PHE A 68 23.515 -7.937 63.094 1.00 67.30 C ANISOU 537 CE1 PHE A 68 7509 10773 7289 1101 -2503 -640 C ATOM 538 CE2 PHE A 68 21.951 -8.510 64.815 1.00 67.88 C ANISOU 538 CE2 PHE A 68 7376 11204 7212 1288 -2569 -514 C ATOM 539 CZ PHE A 68 23.181 -8.008 64.437 1.00 68.06 C ANISOU 539 CZ PHE A 68 7443 11214 7203 1090 -2781 -363 C ATOM 540 N ILE A 69 19.020 -10.590 59.263 1.00 60.55 N ANISOU 540 N ILE A 69 8255 10922 3832 -931 -2328 675 N ATOM 541 CA ILE A 69 18.226 -11.603 58.590 1.00 58.68 C ANISOU 541 CA ILE A 69 8323 10443 3530 -1267 -1599 906 C ATOM 542 C ILE A 69 18.249 -11.416 57.079 1.00 51.69 C ANISOU 542 C ILE A 69 7203 8981 3456 -185 -1489 617 C ATOM 543 O ILE A 69 18.005 -10.314 56.593 1.00 51.41 O ANISOU 543 O ILE A 69 8624 8554 2354 1553 -1026 -845 O ATOM 544 CB ILE A 69 16.763 -11.604 59.070 1.00 59.66 C ANISOU 544 CB ILE A 69 8926 9551 4190 -1802 -574 1265 C ATOM 545 CG1 ILE A 69 16.027 -12.908 58.756 1.00 62.61 C ANISOU 545 CG1 ILE A 69 9738 8813 5238 -1745 -96 1692 C ATOM 546 CG2 ILE A 69 15.981 -10.420 58.518 1.00 57.02 C ANISOU 546 CG2 ILE A 69 7531 8932 5201 -2265 1899 2463 C ATOM 547 CD1 ILE A 69 16.863 -14.164 58.878 1.00 75.54 C ANISOU 547 CD1 ILE A 69 11757 9769 7175 -268 -1194 398 C ATOM 548 N MET A 70 18.545 -12.472 56.335 1.00 42.64 N ANISOU 548 N MET A 70 5694 7175 3332 -152 -2192 1820 N ATOM 549 CA MET A 70 18.563 -12.376 54.876 1.00 38.73 C ANISOU 549 CA MET A 70 4416 7039 3259 392 -2146 1200 C ATOM 550 C MET A 70 17.182 -12.464 54.252 1.00 32.86 C ANISOU 550 C MET A 70 3813 5408 3265 156 -1511 1710 C ATOM 551 O MET A 70 16.364 -13.316 54.590 1.00 44.34 O ANISOU 551 O MET A 70 4796 6796 5256 -465 -1767 3869 O ATOM 552 CB MET A 70 19.472 -13.481 54.312 1.00 44.76 C ANISOU 552 CB MET A 70 4123 8235 4647 1073 -3721 -302 C ATOM 553 CG MET A 70 20.959 -13.084 54.183 1.00 45.65 C ANISOU 553 CG MET A 70 3979 9544 3822 1196 -3724 -451 C ATOM 554 SD MET A 70 21.122 -12.208 52.612 1.00 60.13 S ANISOU 554 SD MET A 70 7716 7087 8043 -1620 -4826 2601 S ATOM 555 CE MET A 70 21.865 -13.416 51.552 1.00107.14 C ANISOU 555 CE MET A 70 14546 15711 10452 -9682 8647 -2220 C ATOM 556 N THR A 71 16.868 -11.587 53.306 1.00 21.68 N ANISOU 556 N THR A 71 2395 4011 1833 125 -497 509 N ATOM 557 CA THR A 71 15.660 -11.651 52.489 1.00 19.79 C ANISOU 557 CA THR A 71 2107 3589 1825 519 -314 511 C ATOM 558 C THR A 71 16.097 -12.146 51.101 1.00 16.17 C ANISOU 558 C THR A 71 1629 2659 1857 284 -389 611 C ATOM 559 O THR A 71 17.264 -12.055 50.747 1.00 16.53 O ANISOU 559 O THR A 71 1738 2552 1992 134 -389 278 O ATOM 560 CB THR A 71 14.913 -10.313 52.406 1.00 19.49 C ANISOU 560 CB THR A 71 2582 3390 1433 512 371 661 C ATOM 561 OG1 THR A 71 15.799 -9.291 51.921 1.00 23.00 O ANISOU 561 OG1 THR A 71 2464 3812 2463 5 -118 905 O ATOM 562 CG2 THR A 71 14.424 -9.836 53.786 1.00 29.82 C ANISOU 562 CG2 THR A 71 3720 5595 2013 1350 878 127 C ATOM 563 N VAL A 72 15.180 -12.683 50.285 1.00 16.62 N ANISOU 563 N VAL A 72 1668 2741 1905 189 -461 748 N ATOM 564 CA VAL A 72 15.506 -13.219 48.983 1.00 16.23 C ANISOU 564 CA VAL A 72 2086 1904 2178 -102 -351 598 C ATOM 565 C VAL A 72 15.733 -12.111 47.970 1.00 12.36 C ANISOU 565 C VAL A 72 1333 1599 1765 57 -320 237 C ATOM 566 O VAL A 72 16.711 -12.192 47.197 1.00 15.16 O ANISOU 566 O VAL A 72 1429 2115 2218 356 -75 381 O ATOM 567 CB VAL A 72 14.446 -14.259 48.531 1.00 20.79 C ANISOU 567 CB VAL A 72 3289 1736 2873 -640 -620 851 C ATOM 568 CG1 VAL A 72 14.599 -14.576 47.081 1.00 24.42 C ANISOU 568 CG1 VAL A 72 3768 2528 2983 -846 -844 308 C ATOM 569 CG2 VAL A 72 14.589 -15.508 49.396 1.00 25.80 C ANISOU 569 CG2 VAL A 72 4162 1902 3737 -456 -1278 1163 C ATOM 570 N GLY A 73 14.923 -11.072 47.964 1.00 13.01 N ANISOU 570 N GLY A 73 1542 1921 1482 317 -6 353 N ATOM 571 CA GLY A 73 15.119 -9.934 47.084 1.00 12.43 C ANISOU 571 CA GLY A 73 1766 1508 1449 199 -257 47 C ATOM 572 C GLY A 73 14.772 -10.107 45.642 1.00 11.30 C ANISOU 572 C GLY A 73 971 1909 1414 3 -247 215 C ATOM 573 O GLY A 73 15.209 -9.324 44.818 1.00 12.70 O ANISOU 573 O GLY A 73 1581 1685 1558 -7 98 42 O ATOM 574 N CYS A 74 13.960 -11.119 45.316 1.00 11.43 N ANISOU 574 N CYS A 74 1089 1741 1513 75 -257 189 N ATOM 575 CA CYS A 74 13.509 -11.340 43.960 1.00 11.35 C ANISOU 575 CA CYS A 74 1371 1430 1511 87 -238 114 C ATOM 576 C CYS A 74 12.226 -12.166 43.992 1.00 13.06 C ANISOU 576 C CYS A 74 1374 2252 1336 -279 -112 50 C ATOM 577 O CYS A 74 11.944 -12.845 44.973 1.00 12.31 O ANISOU 577 O CYS A 74 1457 1734 1488 -26 -170 39 O ATOM 578 CB CYS A 74 14.571 -12.006 43.095 1.00 12.23 C ANISOU 578 CB CYS A 74 1333 1578 1735 33 -90 83 C ATOM 579 SG CYS A 74 15.306 -13.483 43.745 1.00 14.30 S ANISOU 579 SG CYS A 74 1675 1707 2050 319 -254 -51 S ATOM 580 N VAL A 75 11.476 -12.095 42.907 1.00 11.27 N ANISOU 580 N VAL A 75 1457 1365 1459 7 -136 -123 N ATOM 581 CA VAL A 75 10.259 -12.846 42.727 1.00 11.86 C ANISOU 581 CA VAL A 75 1373 1766 1368 19 -293 -40 C ATOM 582 C VAL A 75 10.164 -13.345 41.282 1.00 11.21 C ANISOU 582 C VAL A 75 1349 1500 1409 -86 -135 -12 C ATOM 583 O VAL A 75 10.709 -12.771 40.347 1.00 10.67 O ANISOU 583 O VAL A 75 1312 1239 1502 47 52 -55 O ATOM 584 CB VAL A 75 9.004 -12.031 43.008 1.00 11.98 C ANISOU 584 CB VAL A 75 1446 1597 1510 -58 -56 -14 C ATOM 585 CG1 VAL A 75 8.902 -11.622 44.479 1.00 15.48 C ANISOU 585 CG1 VAL A 75 1556 2619 1706 12 41 -418 C ATOM 586 CG2 VAL A 75 8.899 -10.777 42.151 1.00 13.81 C ANISOU 586 CG2 VAL A 75 1480 1553 2213 -16 61 164 C ATOM 587 N ALA A 76 9.385 -14.415 41.154 1.00 10.59 N ANISOU 587 N ALA A 76 1138 1343 1542 49 -47 -21 N ATOM 588 CA ALA A 76 8.936 -14.885 39.860 1.00 10.40 C ANISOU 588 CA ALA A 76 1295 1204 1453 49 -276 186 C ATOM 589 C ALA A 76 7.583 -14.232 39.514 1.00 11.67 C ANISOU 589 C ALA A 76 1544 1406 1485 402 -79 87 C ATOM 590 O ALA A 76 6.746 -14.001 40.378 1.00 12.42 O ANISOU 590 O ALA A 76 1448 1783 1490 194 -44 -37 O ATOM 591 CB ALA A 76 8.818 -16.364 39.827 1.00 12.17 C ANISOU 591 CB ALA A 76 1281 1173 2169 134 -261 -91 C ATOM 592 N GLY A 77 7.399 -13.943 38.225 1.00 10.15 N ANISOU 592 N GLY A 77 1161 1248 1447 188 -127 119 N ATOM 593 CA GLY A 77 6.167 -13.408 37.751 1.00 10.45 C ANISOU 593 CA GLY A 77 835 1354 1782 -37 -43 167 C ATOM 594 C GLY A 77 5.259 -14.326 36.975 1.00 10.62 C ANISOU 594 C GLY A 77 1119 1215 1701 -62 -32 85 C ATOM 595 O GLY A 77 4.091 -14.051 36.682 1.00 10.34 O ANISOU 595 O GLY A 77 1051 1394 1483 -73 64 -164 O ATOM 596 N ASP A 78 5.805 -15.497 36.644 1.00 12.14 N ANISOU 596 N ASP A 78 1136 1382 2094 2 -217 -62 N ATOM 597 CA ASP A 78 5.142 -16.554 35.909 1.00 11.54 C ANISOU 597 CA ASP A 78 1384 1147 1854 -61 -4 56 C ATOM 598 C ASP A 78 5.993 -17.820 36.066 1.00 11.30 C ANISOU 598 C ASP A 78 1274 1303 1716 30 74 -59 C ATOM 599 O ASP A 78 7.102 -17.782 36.632 1.00 11.92 O ANISOU 599 O ASP A 78 1397 1378 1756 57 -61 -67 O ATOM 600 CB ASP A 78 4.871 -16.182 34.467 1.00 11.75 C ANISOU 600 CB ASP A 78 1327 1257 1880 -1 -8 -30 C ATOM 601 CG ASP A 78 6.095 -15.784 33.671 1.00 11.47 C ANISOU 601 CG ASP A 78 1324 1333 1702 261 93 -80 C ATOM 602 OD1 ASP A 78 7.248 -16.069 34.107 1.00 12.34 O ANISOU 602 OD1 ASP A 78 1340 1515 1833 255 82 94 O ATOM 603 OD2 ASP A 78 5.904 -15.197 32.584 1.00 12.27 O ANISOU 603 OD2 ASP A 78 1339 1638 1684 24 -64 -28 O ATOM 604 N GLU A 79 5.499 -18.931 35.530 1.00 13.23 N ANISOU 604 N GLU A 79 1531 1192 2302 7 -341 -30 N ATOM 605 CA GLU A 79 6.253 -20.175 35.686 1.00 13.10 C ANISOU 605 CA GLU A 79 1590 1146 2242 -104 -101 162 C ATOM 606 C GLU A 79 7.605 -20.117 35.004 1.00 13.43 C ANISOU 606 C GLU A 79 1694 1180 2230 35 -11 30 C ATOM 607 O GLU A 79 8.593 -20.585 35.546 1.00 14.83 O ANISOU 607 O GLU A 79 1795 1532 2308 276 -13 -52 O ATOM 608 CB GLU A 79 5.430 -21.361 35.153 1.00 13.55 C ANISOU 608 CB GLU A 79 1636 1230 2283 49 102 -360 C ATOM 609 CG GLU A 79 6.046 -22.698 35.447 1.00 13.99 C ANISOU 609 CG GLU A 79 1924 1245 2147 30 116 -208 C ATOM 610 CD GLU A 79 5.137 -23.865 35.190 1.00 15.77 C ANISOU 610 CD GLU A 79 2061 1290 2641 -61 -277 130 C ATOM 611 OE1 GLU A 79 3.974 -23.715 34.751 1.00 17.26 O ANISOU 611 OE1 GLU A 79 2047 1461 3052 72 -346 -372 O ATOM 612 OE2 GLU A 79 5.588 -25.006 35.412 1.00 22.34 O ANISOU 612 OE2 GLU A 79 2594 1271 4624 -97 -1360 116 O ATOM 613 N GLU A 80 7.619 -19.527 33.794 1.00 14.10 N ANISOU 613 N GLU A 80 1527 1699 2132 74 35 48 N ATOM 614 CA GLU A 80 8.803 -19.411 32.969 1.00 15.49 C ANISOU 614 CA GLU A 80 1694 1889 2304 123 266 -171 C ATOM 615 C GLU A 80 9.935 -18.634 33.605 1.00 13.53 C ANISOU 615 C GLU A 80 1568 1711 1864 146 363 182 C ATOM 616 O GLU A 80 11.094 -18.766 33.260 1.00 14.01 O ANISOU 616 O GLU A 80 1547 1813 1963 251 226 63 O ATOM 617 CB GLU A 80 8.422 -18.655 31.660 1.00 16.48 C ANISOU 617 CB GLU A 80 1699 2637 1926 185 346 -206 C ATOM 618 CG GLU A 80 7.996 -19.571 30.557 1.00 19.32 C ANISOU 618 CG GLU A 80 2479 2484 2378 234 269 -457 C ATOM 619 CD GLU A 80 7.914 -18.856 29.217 1.00 22.74 C ANISOU 619 CD GLU A 80 4042 2196 2401 47 -832 -539 C ATOM 620 OE1 GLU A 80 8.210 -17.658 29.080 1.00 25.21 O ANISOU 620 OE1 GLU A 80 5689 2006 1886 123 -778 -798 O ATOM 621 OE2 GLU A 80 7.523 -19.475 28.222 1.00 31.85 O ANISOU 621 OE2 GLU A 80 6888 2409 2804 -643 -1054 -806 O ATOM 622 N SER A 81 9.566 -17.773 34.564 1.00 12.37 N ANISOU 622 N SER A 81 1230 1740 1731 287 16 176 N ATOM 623 CA SER A 81 10.574 -16.899 35.154 1.00 12.32 C ANISOU 623 CA SER A 81 1096 1363 2221 310 215 218 C ATOM 624 C SER A 81 11.757 -17.662 35.734 1.00 12.49 C ANISOU 624 C SER A 81 1216 1477 2053 449 25 105 C ATOM 625 O SER A 81 12.898 -17.205 35.610 1.00 12.32 O ANISOU 625 O SER A 81 1299 1567 1813 374 -22 -188 O ATOM 626 CB SER A 81 9.959 -16.061 36.272 1.00 11.98 C ANISOU 626 CB SER A 81 745 1414 2391 198 4 -12 C ATOM 627 OG SER A 81 9.096 -15.045 35.839 1.00 11.75 O ANISOU 627 OG SER A 81 1096 1386 1984 316 43 -167 O ATOM 628 N TYR A 82 11.502 -18.811 36.336 1.00 12.83 N ANISOU 628 N TYR A 82 1436 1256 2182 480 56 -65 N ATOM 629 CA TYR A 82 12.584 -19.562 36.973 1.00 13.08 C ANISOU 629 CA TYR A 82 1654 1478 1837 657 151 57 C ATOM 630 C TYR A 82 13.553 -20.141 35.956 1.00 12.78 C ANISOU 630 C TYR A 82 1309 1470 2078 376 43 -254 C ATOM 631 O TYR A 82 14.677 -20.379 36.311 1.00 17.44 O ANISOU 631 O TYR A 82 1492 2949 2185 864 31 -303 O ATOM 632 CB TYR A 82 12.022 -20.687 37.858 1.00 12.82 C ANISOU 632 CB TYR A 82 1741 1260 1869 418 -26 -114 C ATOM 633 CG TYR A 82 11.449 -20.161 39.160 1.00 12.06 C ANISOU 633 CG TYR A 82 1579 1237 1766 387 -8 9 C ATOM 634 CD1 TYR A 82 12.347 -19.740 40.128 1.00 13.27 C ANISOU 634 CD1 TYR A 82 1564 1654 1824 493 -58 -111 C ATOM 635 CD2 TYR A 82 10.080 -20.044 39.436 1.00 12.27 C ANISOU 635 CD2 TYR A 82 1548 1329 1785 108 73 230 C ATOM 636 CE1 TYR A 82 11.877 -19.244 41.325 1.00 12.70 C ANISOU 636 CE1 TYR A 82 1361 1664 1801 -61 42 -146 C ATOM 637 CE2 TYR A 82 9.610 -19.537 40.660 1.00 12.57 C ANISOU 637 CE2 TYR A 82 1322 1798 1657 369 -57 279 C ATOM 638 CZ TYR A 82 10.535 -19.132 41.599 1.00 11.88 C ANISOU 638 CZ TYR A 82 1392 1572 1549 254 36 402 C ATOM 639 OH TYR A 82 10.150 -18.627 42.839 1.00 13.81 O ANISOU 639 OH TYR A 82 1511 2038 1697 297 30 112 O ATOM 640 N GLU A 83 13.130 -20.353 34.717 1.00 13.92 N ANISOU 640 N GLU A 83 1757 1681 1851 574 117 26 N ATOM 641 CA GLU A 83 14.010 -20.848 33.669 1.00 14.36 C ANISOU 641 CA GLU A 83 1824 1645 1985 611 141 -26 C ATOM 642 C GLU A 83 14.637 -19.722 32.875 1.00 12.68 C ANISOU 642 C GLU A 83 1611 1586 1622 600 65 -256 C ATOM 643 O GLU A 83 15.829 -19.703 32.623 1.00 15.93 O ANISOU 643 O GLU A 83 1523 1630 2899 481 4 -207 O ATOM 644 CB GLU A 83 13.154 -21.726 32.722 1.00 17.14 C ANISOU 644 CB GLU A 83 2178 1631 2703 416 329 -561 C ATOM 645 CG GLU A 83 13.924 -22.279 31.557 1.00 16.96 C ANISOU 645 CG GLU A 83 2557 1785 2101 189 453 -118 C ATOM 646 CD GLU A 83 13.287 -23.368 30.763 1.00 21.51 C ANISOU 646 CD GLU A 83 2699 2859 2614 -211 658 -936 C ATOM 647 OE1 GLU A 83 12.195 -23.874 31.095 1.00 31.70 O ANISOU 647 OE1 GLU A 83 2514 4592 4938 -882 573 -1214 O ATOM 648 OE2 GLU A 83 13.941 -23.746 29.779 1.00 27.23 O ANISOU 648 OE2 GLU A 83 4626 3509 2213 -111 1008 -870 O ATOM 649 N VAL A 84 13.812 -18.746 32.473 1.00 12.23 N ANISOU 649 N VAL A 84 1457 1696 1493 463 202 -69 N ATOM 650 CA VAL A 84 14.286 -17.614 31.692 1.00 12.55 C ANISOU 650 CA VAL A 84 1752 1664 1353 278 160 -151 C ATOM 651 C VAL A 84 15.345 -16.811 32.478 1.00 13.57 C ANISOU 651 C VAL A 84 1490 2098 1567 126 244 -119 C ATOM 652 O VAL A 84 16.282 -16.296 31.863 1.00 16.02 O ANISOU 652 O VAL A 84 1860 2247 1979 -84 550 -209 O ATOM 653 CB VAL A 84 13.154 -16.662 31.282 1.00 12.61 C ANISOU 653 CB VAL A 84 1823 1407 1562 191 -22 -190 C ATOM 654 CG1 VAL A 84 13.697 -15.433 30.584 1.00 13.33 C ANISOU 654 CG1 VAL A 84 1911 1458 1697 164 103 -203 C ATOM 655 CG2 VAL A 84 12.169 -17.422 30.424 1.00 13.50 C ANISOU 655 CG2 VAL A 84 1788 2056 1288 -128 139 -163 C ATOM 656 N PHE A 85 15.229 -16.745 33.806 1.00 12.15 N ANISOU 656 N PHE A 85 1240 1783 1593 122 185 -283 N ATOM 657 CA PHE A 85 16.231 -16.083 34.633 1.00 12.33 C ANISOU 657 CA PHE A 85 1375 1371 1937 337 -90 -181 C ATOM 658 C PHE A 85 16.976 -17.024 35.554 1.00 13.83 C ANISOU 658 C PHE A 85 1312 1643 2298 556 -147 -79 C ATOM 659 O PHE A 85 17.348 -16.652 36.674 1.00 14.49 O ANISOU 659 O PHE A 85 1308 1966 2231 494 -155 -101 O ATOM 660 CB PHE A 85 15.553 -14.932 35.403 1.00 11.41 C ANISOU 660 CB PHE A 85 1472 1387 1476 386 -63 -13 C ATOM 661 CG PHE A 85 14.851 -14.013 34.421 1.00 8.93 C ANISOU 661 CG PHE A 85 1168 991 1234 61 -156 -192 C ATOM 662 CD1 PHE A 85 15.638 -13.237 33.599 1.00 11.47 C ANISOU 662 CD1 PHE A 85 1627 1179 1552 -172 -49 -66 C ATOM 663 CD2 PHE A 85 13.486 -13.936 34.281 1.00 11.42 C ANISOU 663 CD2 PHE A 85 1221 1447 1671 318 72 -129 C ATOM 664 CE1 PHE A 85 15.096 -12.406 32.633 1.00 13.30 C ANISOU 664 CE1 PHE A 85 2065 1494 1495 -256 -157 88 C ATOM 665 CE2 PHE A 85 12.885 -13.083 33.336 1.00 11.52 C ANISOU 665 CE2 PHE A 85 1327 1322 1728 483 -254 -423 C ATOM 666 CZ PHE A 85 13.730 -12.319 32.545 1.00 12.78 C ANISOU 666 CZ PHE A 85 2172 1275 1407 246 -324 -332 C ATOM 667 N LYS A 86 17.196 -18.255 35.108 1.00 15.97 N ANISOU 667 N LYS A 86 1371 1778 2921 672 -393 -323 N ATOM 668 CA LYS A 86 17.835 -19.237 35.966 1.00 16.92 C ANISOU 668 CA LYS A 86 1338 1705 3385 752 -270 -143 C ATOM 669 C LYS A 86 19.234 -18.796 36.444 1.00 15.57 C ANISOU 669 C LYS A 86 1223 1598 3093 895 -178 35 C ATOM 670 O LYS A 86 19.646 -19.185 37.554 1.00 17.90 O ANISOU 670 O LYS A 86 1902 1697 3202 871 -461 99 O ATOM 671 CB LYS A 86 17.885 -20.603 35.292 1.00 18.40 C ANISOU 671 CB LYS A 86 1723 1900 3367 947 -337 -386 C ATOM 672 CG LYS A 86 18.679 -20.790 34.046 1.00 22.71 C ANISOU 672 CG LYS A 86 2349 2579 3702 513 126 -645 C ATOM 673 CD LYS A 86 18.824 -22.205 33.503 1.00 29.62 C ANISOU 673 CD LYS A 86 4623 3177 3455 -581 777 -1613 C ATOM 674 CE LYS A 86 17.532 -22.739 32.928 1.00 37.19 C ANISOU 674 CE LYS A 86 4912 3982 5235 -814 291 -1854 C ATOM 675 NZ LYS A 86 17.646 -24.166 32.504 1.00 51.74 N ANISOU 675 NZ LYS A 86 7126 3886 8648 -2283 1142 -2631 N ATOM 676 N GLU A 87 19.941 -18.015 35.668 1.00 15.99 N ANISOU 676 N GLU A 87 1450 2097 2528 553 -23 -384 N ATOM 677 CA GLU A 87 21.291 -17.577 36.041 1.00 16.56 C ANISOU 677 CA GLU A 87 1397 1986 2909 593 68 -347 C ATOM 678 C GLU A 87 21.238 -16.691 37.292 1.00 14.59 C ANISOU 678 C GLU A 87 1432 1612 2500 368 -108 86 C ATOM 679 O GLU A 87 22.240 -16.606 37.994 1.00 16.76 O ANISOU 679 O GLU A 87 1697 1918 2753 506 -356 189 O ATOM 680 CB GLU A 87 22.013 -16.860 34.909 1.00 17.89 C ANISOU 680 CB GLU A 87 1476 2529 2795 502 172 -336 C ATOM 681 CG GLU A 87 22.326 -17.702 33.683 1.00 20.21 C ANISOU 681 CG GLU A 87 2047 2727 2904 694 155 -415 C ATOM 682 CD GLU A 87 21.266 -17.649 32.619 1.00 23.64 C ANISOU 682 CD GLU A 87 2578 3704 2701 1003 -20 -532 C ATOM 683 OE1 GLU A 87 20.062 -17.363 32.870 1.00 19.40 O ANISOU 683 OE1 GLU A 87 2330 2988 2053 516 -43 367 O ATOM 684 OE2 GLU A 87 21.632 -17.902 31.447 1.00 26.29 O ANISOU 684 OE2 GLU A 87 3251 4074 2664 1546 234 -118 O ATOM 685 N LEU A 88 20.108 -16.068 37.577 1.00 15.42 N ANISOU 685 N LEU A 88 1678 2078 2105 676 -95 -142 N ATOM 686 CA LEU A 88 19.878 -15.321 38.813 1.00 15.02 C ANISOU 686 CA LEU A 88 1769 1855 2082 329 -306 -128 C ATOM 687 C LEU A 88 19.261 -16.242 39.861 1.00 15.10 C ANISOU 687 C LEU A 88 1477 2151 2110 371 -106 -177 C ATOM 688 O LEU A 88 19.755 -16.347 40.990 1.00 16.07 O ANISOU 688 O LEU A 88 1577 2251 2276 443 -312 93 O ATOM 689 CB LEU A 88 18.981 -14.110 38.550 1.00 15.89 C ANISOU 689 CB LEU A 88 1595 1609 2834 284 -358 -462 C ATOM 690 CG LEU A 88 18.715 -13.079 39.666 1.00 18.47 C ANISOU 690 CG LEU A 88 2110 2024 2886 -79 -290 -871 C ATOM 691 CD1 LEU A 88 17.653 -13.491 40.661 1.00 30.66 C ANISOU 691 CD1 LEU A 88 1764 7216 2669 -221 -191 -972 C ATOM 692 CD2 LEU A 88 19.994 -12.673 40.367 1.00 20.97 C ANISOU 692 CD2 LEU A 88 2455 1939 3574 -483 -675 -552 C ATOM 693 N PHE A 89 18.154 -16.905 39.539 1.00 14.80 N ANISOU 693 N PHE A 89 1725 1717 2179 427 -431 136 N ATOM 694 CA PHE A 89 17.460 -17.689 40.558 1.00 14.20 C ANISOU 694 CA PHE A 89 1367 1754 2275 530 -275 3 C ATOM 695 C PHE A 89 18.240 -18.901 41.055 1.00 14.10 C ANISOU 695 C PHE A 89 1644 1591 2122 467 -345 36 C ATOM 696 O PHE A 89 18.107 -19.172 42.252 1.00 15.17 O ANISOU 696 O PHE A 89 1650 2015 2099 181 -376 33 O ATOM 697 CB PHE A 89 16.101 -18.160 40.049 1.00 13.97 C ANISOU 697 CB PHE A 89 1514 1772 2022 557 -292 -222 C ATOM 698 CG PHE A 89 15.008 -17.126 39.894 1.00 12.28 C ANISOU 698 CG PHE A 89 1225 1545 1897 294 -15 101 C ATOM 699 CD1 PHE A 89 14.509 -16.532 41.041 1.00 13.92 C ANISOU 699 CD1 PHE A 89 1938 1397 1954 553 113 198 C ATOM 700 CD2 PHE A 89 14.468 -16.762 38.677 1.00 14.22 C ANISOU 700 CD2 PHE A 89 1663 1710 2030 460 -366 -99 C ATOM 701 CE1 PHE A 89 13.495 -15.601 41.008 1.00 12.37 C ANISOU 701 CE1 PHE A 89 1534 1242 1923 229 156 98 C ATOM 702 CE2 PHE A 89 13.438 -15.826 38.629 1.00 12.56 C ANISOU 702 CE2 PHE A 89 1261 1586 1923 194 -164 16 C ATOM 703 CZ PHE A 89 12.952 -15.245 39.782 1.00 12.45 C ANISOU 703 CZ PHE A 89 1297 1404 2028 142 -24 95 C ATOM 704 N ASP A 90 19.026 -19.597 40.214 1.00 15.37 N ANISOU 704 N ASP A 90 1457 1994 2387 693 -260 82 N ATOM 705 CA ASP A 90 19.700 -20.798 40.706 1.00 18.33 C ANISOU 705 CA ASP A 90 2026 1815 3123 799 -492 0 C ATOM 706 C ASP A 90 20.645 -20.468 41.850 1.00 19.10 C ANISOU 706 C ASP A 90 1902 2220 3136 721 -610 382 C ATOM 707 O ASP A 90 20.582 -21.128 42.910 1.00 18.79 O ANISOU 707 O ASP A 90 1852 2145 3143 652 -444 313 O ATOM 708 CB ASP A 90 20.338 -21.531 39.521 1.00 19.81 C ANISOU 708 CB ASP A 90 1705 2366 3456 1102 -458 -115 C ATOM 709 CG ASP A 90 19.317 -22.284 38.679 1.00 21.80 C ANISOU 709 CG ASP A 90 2934 1960 3389 652 -658 -159 C ATOM 710 OD1 ASP A 90 18.125 -22.342 39.057 1.00 23.58 O ANISOU 710 OD1 ASP A 90 2519 2152 4288 424 -1192 -88 O ATOM 711 OD2 ASP A 90 19.691 -22.825 37.621 1.00 28.29 O ANISOU 711 OD2 ASP A 90 4665 2099 3986 1499 -692 -669 O ATOM 712 N PRO A 91 21.554 -19.509 41.720 1.00 18.32 N ANISOU 712 N PRO A 91 1804 2376 2781 673 -530 385 N ATOM 713 CA PRO A 91 22.433 -19.205 42.851 1.00 18.19 C ANISOU 713 CA PRO A 91 1732 2254 2927 850 -572 279 C ATOM 714 C PRO A 91 21.621 -18.681 44.025 1.00 18.59 C ANISOU 714 C PRO A 91 1823 2339 2903 809 -522 221 C ATOM 715 O PRO A 91 21.987 -18.981 45.162 1.00 18.53 O ANISOU 715 O PRO A 91 1752 2315 2973 568 -651 231 O ATOM 716 CB PRO A 91 23.381 -18.140 42.323 1.00 20.12 C ANISOU 716 CB PRO A 91 1921 2715 3010 528 -553 405 C ATOM 717 CG PRO A 91 23.243 -18.145 40.850 1.00 22.31 C ANISOU 717 CG PRO A 91 1824 3608 3047 160 -537 448 C ATOM 718 CD PRO A 91 21.922 -18.739 40.511 1.00 19.98 C ANISOU 718 CD PRO A 91 1304 3099 3189 781 -708 941 C ATOM 719 N VAL A 92 20.518 -17.949 43.831 1.00 17.31 N ANISOU 719 N VAL A 92 1733 2190 2656 651 -479 92 N ATOM 720 CA VAL A 92 19.718 -17.469 44.979 1.00 15.95 C ANISOU 720 CA VAL A 92 1623 1994 2442 535 -443 449 C ATOM 721 C VAL A 92 19.148 -18.654 45.715 1.00 16.51 C ANISOU 721 C VAL A 92 1985 1841 2447 578 -799 561 C ATOM 722 O VAL A 92 19.159 -18.773 46.935 1.00 18.21 O ANISOU 722 O VAL A 92 1944 2543 2432 19 -503 555 O ATOM 723 CB VAL A 92 18.616 -16.509 44.475 1.00 13.71 C ANISOU 723 CB VAL A 92 1506 1542 2161 299 -588 308 C ATOM 724 CG1 VAL A 92 17.508 -16.299 45.511 1.00 16.31 C ANISOU 724 CG1 VAL A 92 1479 2088 2630 331 -340 266 C ATOM 725 CG2 VAL A 92 19.192 -15.171 44.087 1.00 15.27 C ANISOU 725 CG2 VAL A 92 1644 1629 2529 123 -548 239 C ATOM 726 N ILE A 93 18.613 -19.590 44.937 1.00 17.08 N ANISOU 726 N ILE A 93 2204 1803 2483 601 -689 448 N ATOM 727 CA ILE A 93 17.996 -20.780 45.531 1.00 16.26 C ANISOU 727 CA ILE A 93 2339 1516 2323 777 -311 166 C ATOM 728 C ILE A 93 19.013 -21.618 46.290 1.00 17.83 C ANISOU 728 C ILE A 93 2418 1844 2514 735 -268 461 C ATOM 729 O ILE A 93 18.764 -22.121 47.379 1.00 19.40 O ANISOU 729 O ILE A 93 2746 2011 2613 283 -660 638 O ATOM 730 CB ILE A 93 17.274 -21.609 44.463 1.00 15.78 C ANISOU 730 CB ILE A 93 2584 1360 2052 835 -105 91 C ATOM 731 CG1 ILE A 93 15.999 -20.920 43.963 1.00 14.53 C ANISOU 731 CG1 ILE A 93 1997 1253 2270 358 -21 39 C ATOM 732 CG2 ILE A 93 16.973 -23.008 44.985 1.00 17.28 C ANISOU 732 CG2 ILE A 93 2290 1625 2650 539 -244 317 C ATOM 733 CD1 ILE A 93 15.477 -21.360 42.630 1.00 17.36 C ANISOU 733 CD1 ILE A 93 2488 1540 2568 333 -423 -74 C ATOM 734 N GLU A 94 20.204 -21.764 45.706 1.00 18.51 N ANISOU 734 N GLU A 94 2230 1808 2994 818 -361 -242 N ATOM 735 CA GLU A 94 21.251 -22.533 46.334 1.00 21.21 C ANISOU 735 CA GLU A 94 2139 2372 3550 410 -558 662 C ATOM 736 C GLU A 94 21.622 -21.934 47.685 1.00 23.84 C ANISOU 736 C GLU A 94 3074 2308 3677 738 -1048 715 C ATOM 737 O GLU A 94 21.778 -22.667 48.665 1.00 24.85 O ANISOU 737 O GLU A 94 3649 1987 3806 618 -1321 673 O ATOM 738 CB GLU A 94 22.443 -22.615 45.370 1.00 21.42 C ANISOU 738 CB GLU A 94 1470 2689 3979 355 -760 823 C ATOM 739 CG GLU A 94 23.574 -23.472 45.872 1.00 25.58 C ANISOU 739 CG GLU A 94 2152 3271 4295 981 -1388 298 C ATOM 740 CD GLU A 94 24.590 -23.953 44.862 1.00 32.08 C ANISOU 740 CD GLU A 94 2926 3927 5337 1792 -670 473 C ATOM 741 OE1 GLU A 94 24.339 -23.961 43.640 1.00 30.02 O ANISOU 741 OE1 GLU A 94 2557 3676 5172 690 -213 -52 O ATOM 742 OE2 GLU A 94 25.702 -24.362 45.308 1.00 39.54 O ANISOU 742 OE2 GLU A 94 2663 5984 6378 1949 -320 1475 O ATOM 743 N ASP A 95 21.743 -20.622 47.783 1.00 17.93 N ANISOU 743 N ASP A 95 1584 2385 2845 331 -472 919 N ATOM 744 CA ASP A 95 22.159 -19.957 49.014 1.00 22.61 C ANISOU 744 CA ASP A 95 1754 3260 3578 538 -841 131 C ATOM 745 C ASP A 95 21.037 -19.986 50.041 1.00 20.90 C ANISOU 745 C ASP A 95 1811 3201 2928 222 -1110 -117 C ATOM 746 O ASP A 95 21.277 -20.259 51.224 1.00 26.62 O ANISOU 746 O ASP A 95 2283 4905 2928 1150 -1324 -198 O ATOM 747 CB ASP A 95 22.576 -18.537 48.645 1.00 24.55 C ANISOU 747 CB ASP A 95 1604 3230 4493 194 -90 -520 C ATOM 748 CG ASP A 95 23.443 -17.869 49.685 1.00 33.57 C ANISOU 748 CG ASP A 95 2412 4237 6106 3 -1450 -682 C ATOM 749 OD1 ASP A 95 24.339 -18.536 50.238 1.00 44.12 O ANISOU 749 OD1 ASP A 95 3246 6714 6802 1231 -1991 -774 O ATOM 750 OD2 ASP A 95 23.210 -16.663 49.898 1.00 40.02 O ANISOU 750 OD2 ASP A 95 3046 5193 6967 608 -1326 -2746 O ATOM 751 N ARG A 96 19.806 -19.749 49.563 1.00 18.60 N ANISOU 751 N ARG A 96 1816 2872 2380 332 -799 264 N ATOM 752 CA ARG A 96 18.654 -19.695 50.460 1.00 18.93 C ANISOU 752 CA ARG A 96 2007 2142 3042 425 -491 422 C ATOM 753 C ARG A 96 18.299 -21.060 51.006 1.00 18.08 C ANISOU 753 C ARG A 96 2262 2169 2438 449 -895 512 C ATOM 754 O ARG A 96 17.792 -21.176 52.132 1.00 21.47 O ANISOU 754 O ARG A 96 3114 2424 2620 133 -487 294 O ATOM 755 CB ARG A 96 17.433 -19.114 49.711 1.00 16.37 C ANISOU 755 CB ARG A 96 2025 1419 2775 334 -455 341 C ATOM 756 CG ARG A 96 16.136 -19.127 50.498 1.00 17.54 C ANISOU 756 CG ARG A 96 2106 1400 3160 453 -315 30 C ATOM 757 CD ARG A 96 16.215 -18.345 51.794 1.00 18.71 C ANISOU 757 CD ARG A 96 2654 1710 2744 16 -101 294 C ATOM 758 NE ARG A 96 14.975 -18.411 52.542 1.00 20.76 N ANISOU 758 NE ARG A 96 2831 2283 2773 -110 -12 310 N ATOM 759 CZ ARG A 96 14.541 -19.444 53.244 1.00 20.31 C ANISOU 759 CZ ARG A 96 1913 2603 3201 -36 -435 784 C ATOM 760 NH1 ARG A 96 15.288 -20.532 53.247 1.00 25.71 N ANISOU 760 NH1 ARG A 96 2978 3068 3723 636 20 1364 N ATOM 761 NH2 ARG A 96 13.377 -19.374 53.901 1.00 23.33 N ANISOU 761 NH2 ARG A 96 2187 3552 3124 -84 -188 677 N ATOM 762 N HIS A 97 18.548 -22.096 50.216 1.00 17.94 N ANISOU 762 N HIS A 97 2369 2055 2391 479 -716 670 N ATOM 763 CA HIS A 97 18.079 -23.432 50.605 1.00 19.78 C ANISOU 763 CA HIS A 97 2429 1998 3089 599 -809 930 C ATOM 764 C HIS A 97 19.194 -24.416 50.906 1.00 20.72 C ANISOU 764 C HIS A 97 2240 2192 3439 682 -809 791 C ATOM 765 O HIS A 97 19.173 -25.593 50.558 1.00 23.73 O ANISOU 765 O HIS A 97 2595 2124 4298 692 -555 814 O ATOM 766 CB HIS A 97 17.169 -23.982 49.509 1.00 19.65 C ANISOU 766 CB HIS A 97 1910 2115 3442 365 -645 838 C ATOM 767 CG HIS A 97 15.846 -23.262 49.470 1.00 16.66 C ANISOU 767 CG HIS A 97 2215 1773 2343 571 -449 246 C ATOM 768 ND1 HIS A 97 14.837 -23.377 50.435 1.00 19.19 N ANISOU 768 ND1 HIS A 97 2558 2029 2706 692 -148 597 N ATOM 769 CD2 HIS A 97 15.352 -22.356 48.565 1.00 16.00 C ANISOU 769 CD2 HIS A 97 1793 1931 2357 347 -553 306 C ATOM 770 CE1 HIS A 97 13.829 -22.593 50.084 1.00 17.07 C ANISOU 770 CE1 HIS A 97 1579 2417 2491 15 -659 588 C ATOM 771 NE2 HIS A 97 14.115 -21.969 48.956 1.00 15.38 N ANISOU 771 NE2 HIS A 97 1777 1869 2196 291 -475 200 N ATOM 772 N GLY A 98 20.220 -23.961 51.603 1.00 24.81 N ANISOU 772 N GLY A 98 2726 2910 3791 626 -1371 929 N ATOM 773 CA GLY A 98 21.290 -24.791 52.071 1.00 28.35 C ANISOU 773 CA GLY A 98 3079 3816 3875 1097 -1597 965 C ATOM 774 C GLY A 98 22.112 -25.577 51.094 1.00 28.20 C ANISOU 774 C GLY A 98 3241 3170 4304 1077 -1482 939 C ATOM 775 O GLY A 98 22.562 -26.708 51.357 1.00 31.41 O ANISOU 775 O GLY A 98 4335 2500 5100 550 -1620 863 O ATOM 776 N GLY A 99 22.412 -25.023 49.913 1.00 26.75 N ANISOU 776 N GLY A 99 3623 2652 3889 868 -1572 403 N ATOM 777 CA GLY A 99 23.270 -25.724 48.984 1.00 28.49 C ANISOU 777 CA GLY A 99 2790 3808 4227 1204 -1750 279 C ATOM 778 C GLY A 99 22.482 -26.476 47.923 1.00 27.41 C ANISOU 778 C GLY A 99 2617 3746 4052 1663 -1510 -88 C ATOM 779 O GLY A 99 23.095 -27.265 47.195 1.00 35.00 O ANISOU 779 O GLY A 99 3609 4005 5685 2233 -1379 -794 O ATOM 780 N TYR A 100 21.180 -26.221 47.855 1.00 24.99 N ANISOU 780 N TYR A 100 2333 3147 4014 940 -1087 363 N ATOM 781 CA TYR A 100 20.352 -26.916 46.868 1.00 22.49 C ANISOU 781 CA TYR A 100 2332 2212 4000 848 -942 650 C ATOM 782 C TYR A 100 20.824 -26.530 45.468 1.00 23.52 C ANISOU 782 C TYR A 100 2567 2461 3910 850 -760 477 C ATOM 783 O TYR A 100 20.801 -25.355 45.083 1.00 24.62 O ANISOU 783 O TYR A 100 2651 2512 4194 844 -517 689 O ATOM 784 CB TYR A 100 18.885 -26.587 47.075 1.00 22.03 C ANISOU 784 CB TYR A 100 2205 2052 4115 592 -876 1029 C ATOM 785 CG TYR A 100 17.950 -27.503 46.311 1.00 20.33 C ANISOU 785 CG TYR A 100 2073 2185 3467 733 -110 350 C ATOM 786 CD1 TYR A 100 17.666 -28.781 46.787 1.00 23.45 C ANISOU 786 CD1 TYR A 100 3024 1959 3927 614 -1041 279 C ATOM 787 CD2 TYR A 100 17.366 -27.097 45.119 1.00 20.98 C ANISOU 787 CD2 TYR A 100 2086 2510 3373 465 -109 450 C ATOM 788 CE1 TYR A 100 16.814 -29.619 46.089 1.00 22.67 C ANISOU 788 CE1 TYR A 100 2670 1932 4014 921 -1195 232 C ATOM 789 CE2 TYR A 100 16.527 -27.945 44.438 1.00 23.38 C ANISOU 789 CE2 TYR A 100 2648 2353 3883 525 -641 546 C ATOM 790 CZ TYR A 100 16.250 -29.203 44.905 1.00 22.92 C ANISOU 790 CZ TYR A 100 2947 2037 3723 744 -959 354 C ATOM 791 OH TYR A 100 15.384 -30.042 44.210 1.00 21.94 O ANISOU 791 OH TYR A 100 2883 2162 3290 759 -723 161 O ATOM 792 N LYS A 101 21.300 -27.497 44.722 1.00 24.83 N ANISOU 792 N LYS A 101 2307 2655 4472 837 -639 227 N ATOM 793 CA LYS A 101 21.966 -27.320 43.448 1.00 24.29 C ANISOU 793 CA LYS A 101 1983 2557 4690 886 -442 188 C ATOM 794 C LYS A 101 21.040 -27.342 42.249 1.00 22.81 C ANISOU 794 C LYS A 101 2118 2114 4434 951 -294 288 C ATOM 795 O LYS A 101 19.927 -27.894 42.337 1.00 21.81 O ANISOU 795 O LYS A 101 2208 2464 3616 761 -292 235 O ATOM 796 CB LYS A 101 23.028 -28.432 43.282 1.00 25.43 C ANISOU 796 CB LYS A 101 2085 2574 5002 961 -682 139 C ATOM 797 CG LYS A 101 23.904 -28.545 44.517 1.00 31.08 C ANISOU 797 CG LYS A 101 2613 3067 6127 756 -1682 168 C ATOM 798 CD LYS A 101 24.928 -27.434 44.617 1.00 34.59 C ANISOU 798 CD LYS A 101 3047 3341 6756 412 -1642 47 C ATOM 799 CE LYS A 101 26.080 -27.877 45.513 1.00 35.73 C ANISOU 799 CE LYS A 101 2124 4621 6829 264 -1203 199 C ATOM 800 NZ LYS A 101 27.001 -26.738 45.789 1.00 40.78 N ANISOU 800 NZ LYS A 101 3014 4975 7505 98 -1437 -1001 N ATOM 801 N PRO A 102 21.453 -26.737 41.141 1.00 22.60 N ANISOU 801 N PRO A 102 2306 1984 4297 567 -24 -156 N ATOM 802 CA PRO A 102 20.583 -26.712 39.960 1.00 25.85 C ANISOU 802 CA PRO A 102 2464 3211 4145 292 -39 130 C ATOM 803 C PRO A 102 20.187 -28.088 39.446 1.00 24.36 C ANISOU 803 C PRO A 102 1613 3454 4189 98 -176 66 C ATOM 804 O PRO A 102 19.203 -28.270 38.736 1.00 30.84 O ANISOU 804 O PRO A 102 2045 5742 3931 -298 -310 -273 O ATOM 805 CB PRO A 102 21.451 -25.959 38.939 1.00 26.30 C ANISOU 805 CB PRO A 102 2723 2739 4530 566 164 313 C ATOM 806 CG PRO A 102 22.313 -25.061 39.772 1.00 26.94 C ANISOU 806 CG PRO A 102 3093 2548 4595 349 590 -11 C ATOM 807 CD PRO A 102 22.690 -25.966 40.909 1.00 24.93 C ANISOU 807 CD PRO A 102 2455 2185 4833 350 -1 -308 C TER END