HEADER 2.10.22.10 1bx7000 ATOM 1 N GLY A 3 46.621 -12.040 -25.886 1.00 68.79 N ANISOU 1 N GLY A 3 16910 6583 2643 -68 2189 1445 N ATOM 2 CA GLY A 3 47.272 -12.399 -24.624 1.00 59.21 C ANISOU 2 CA GLY A 3 10012 10370 2116 -1128 2766 -598 C ATOM 3 C GLY A 3 46.781 -11.500 -23.505 1.00 58.49 C ANISOU 3 C GLY A 3 7351 10516 4356 -1729 1740 -2584 C ATOM 4 O GLY A 3 45.844 -10.744 -23.812 1.00 48.85 O ANISOU 4 O GLY A 3 8848 6253 3462 -3265 1895 -332 O ATOM 5 N ASN A 4 47.353 -11.502 -22.297 1.00 41.83 N ANISOU 5 N ASN A 4 5736 6123 4036 -2993 2426 -2107 N ATOM 6 CA ASN A 4 46.779 -10.619 -21.269 1.00 29.17 C ANISOU 6 CA ASN A 4 2424 4821 3838 -1464 903 -891 C ATOM 7 C ASN A 4 47.188 -9.169 -21.422 1.00 31.83 C ANISOU 7 C ASN A 4 2596 5074 4424 -1962 143 -774 C ATOM 8 O ASN A 4 48.227 -8.670 -21.831 1.00 35.08 O ANISOU 8 O ASN A 4 3702 5723 3906 -2110 982 194 O ATOM 9 CB ASN A 4 47.121 -11.139 -19.895 1.00 29.96 C ANISOU 9 CB ASN A 4 2877 4945 3562 -1760 769 -1186 C ATOM 10 CG ASN A 4 46.263 -10.575 -18.779 1.00 36.68 C ANISOU 10 CG ASN A 4 2791 7782 3364 209 -144 -1424 C ATOM 11 OD1 ASN A 4 45.187 -10.010 -19.022 1.00 28.20 O ANISOU 11 OD1 ASN A 4 2543 4651 3521 -1064 522 728 O ATOM 12 ND2 ASN A 4 46.624 -10.764 -17.512 1.00 28.85 N ANISOU 12 ND2 ASN A 4 1973 5663 3325 -951 -124 -1187 N ATOM 13 N THR A 5 46.246 -8.318 -20.976 1.00 28.89 N ANISOU 13 N THR A 5 2345 4504 4127 -1388 -928 102 N ATOM 14 CA THR A 5 46.743 -6.947 -20.855 1.00 28.78 C ANISOU 14 CA THR A 5 3528 4633 2772 -1880 -123 254 C ATOM 15 C THR A 5 47.479 -6.868 -19.516 1.00 33.41 C ANISOU 15 C THR A 5 4073 4111 4511 -3335 -2002 2097 C ATOM 16 O THR A 5 47.545 -7.797 -18.721 1.00 33.04 O ANISOU 16 O THR A 5 5161 3338 4057 -2803 -880 1511 O ATOM 17 CB THR A 5 45.543 -5.997 -20.827 1.00 25.73 C ANISOU 17 CB THR A 5 3990 3958 1828 -1837 -407 1281 C ATOM 18 OG1 THR A 5 44.510 -6.568 -20.056 1.00 26.27 O ANISOU 18 OG1 THR A 5 3366 3748 2869 -1568 -284 1316 O ATOM 19 CG2 THR A 5 44.927 -5.831 -22.210 1.00 33.89 C ANISOU 19 CG2 THR A 5 5622 5064 2189 -2599 -1407 1156 C ATOM 20 N CYS A 6 47.916 -5.673 -19.214 1.00 28.40 N ANISOU 20 N CYS A 6 3614 3537 3641 -2435 -1885 2165 N ATOM 21 CA CYS A 6 48.600 -5.375 -17.996 1.00 23.73 C ANISOU 21 CA CYS A 6 2795 3157 3066 -1794 -933 1676 C ATOM 22 C CYS A 6 47.639 -4.552 -17.138 1.00 26.05 C ANISOU 22 C CYS A 6 2129 4561 3207 -905 -448 2916 C ATOM 23 O CYS A 6 47.467 -3.385 -17.467 1.00 25.10 O ANISOU 23 O CYS A 6 2303 4133 3099 -962 -233 2191 O ATOM 24 CB CYS A 6 49.887 -4.558 -18.295 1.00 22.27 C ANISOU 24 CB CYS A 6 1850 3593 3020 -1270 -809 1237 C ATOM 25 SG CYS A 6 50.771 -4.292 -16.720 1.00 18.96 S ANISOU 25 SG CYS A 6 2156 2532 2517 -874 -445 918 S ATOM 26 N GLY A 7 47.015 -5.188 -16.155 1.00 32.44 N ANISOU 26 N GLY A 7 2503 6327 3494 -1400 -594 3729 N ATOM 27 CA GLY A 7 45.985 -4.499 -15.408 1.00 38.45 C ANISOU 27 CA GLY A 7 2125 8955 3529 -1076 -250 3835 C ATOM 28 C GLY A 7 44.913 -3.969 -16.337 1.00 41.87 C ANISOU 28 C GLY A 7 2182 10821 2904 -270 597 4651 C ATOM 29 O GLY A 7 44.371 -2.905 -16.021 1.00 49.45 O ANISOU 29 O GLY A 7 3071 10370 5349 -91 -462 4407 O ATOM 30 N GLY A 8 44.619 -4.591 -17.477 1.00 40.24 N ANISOU 30 N GLY A 8 2152 8758 4380 -2652 -951 5242 N ATOM 31 CA GLY A 8 43.588 -4.090 -18.370 1.00 34.40 C ANISOU 31 CA GLY A 8 1927 6507 4638 -1601 -560 4198 C ATOM 32 C GLY A 8 44.021 -3.078 -19.414 1.00 26.75 C ANISOU 32 C GLY A 8 2110 4310 3743 -921 -218 2798 C ATOM 33 O GLY A 8 43.210 -2.604 -20.211 1.00 31.75 O ANISOU 33 O GLY A 8 2701 5153 4209 -473 -375 3285 O ATOM 34 N GLU A 9 45.315 -2.751 -19.448 1.00 27.27 N ANISOU 34 N GLU A 9 2099 4461 3802 -901 423 2598 N ATOM 35 CA GLU A 9 45.884 -1.747 -20.317 1.00 21.75 C ANISOU 35 CA GLU A 9 2300 3992 1973 -919 147 1736 C ATOM 36 C GLU A 9 47.001 -2.387 -21.145 1.00 18.29 C ANISOU 36 C GLU A 9 1871 2899 2178 -1050 -331 1431 C ATOM 37 O GLU A 9 47.590 -3.408 -20.757 1.00 22.65 O ANISOU 37 O GLU A 9 2615 3039 2952 -1006 -316 2054 O ATOM 38 CB GLU A 9 46.474 -0.557 -19.528 1.00 22.10 C ANISOU 38 CB GLU A 9 2340 3664 2395 -270 250 1284 C ATOM 39 CG AGLU A 9 45.376 0.219 -18.807 0.52 26.43 C ANISOU 39 CG AGLU A 9 2903 4874 2266 -559 1637 1543 C ATOM 40 CG BGLU A 9 46.823 -0.739 -18.090 0.48 39.16 C ANISOU 40 CG BGLU A 9 4044 7109 3725 -1015 -2795 1538 C ATOM 41 CD AGLU A 9 44.216 0.690 -19.643 0.52 27.43 C ANISOU 41 CD AGLU A 9 4187 4079 2155 1672 1887 961 C ATOM 42 CD BGLU A 9 47.848 -0.092 -17.217 0.48 38.75 C ANISOU 42 CD BGLU A 9 5111 3939 5672 -1919 -3490 2640 C ATOM 43 OE1AGLU A 9 44.319 1.021 -20.829 0.52 28.06 O ANISOU 43 OE1AGLU A 9 3502 4498 2661 986 1943 1780 O ATOM 44 OE1BGLU A 9 48.082 1.141 -17.376 0.48 30.43 O ANISOU 44 OE1BGLU A 9 4381 3276 3905 -100 2152 1413 O ATOM 45 OE2AGLU A 9 43.086 0.820 -19.124 0.52 35.07 O ANISOU 45 OE2AGLU A 9 3387 8186 1752 623 1259 1502 O ATOM 46 OE2BGLU A 9 48.379 -0.709 -16.253 0.48 14.52 O ANISOU 46 OE2BGLU A 9 821 2924 1770 -108 -330 51 O ATOM 47 N THR A 10 47.334 -1.778 -22.253 1.00 17.68 N ANISOU 47 N THR A 10 1532 2831 2355 -105 41 1595 N ATOM 48 CA THR A 10 48.488 -2.144 -23.049 1.00 14.00 C ANISOU 48 CA THR A 10 1186 1888 2246 -291 -402 1090 C ATOM 49 C THR A 10 49.643 -1.219 -22.673 1.00 13.44 C ANISOU 49 C THR A 10 1623 1834 1650 -500 -392 1001 C ATOM 50 O THR A 10 49.520 -0.007 -22.789 1.00 14.71 O ANISOU 50 O THR A 10 1942 1824 1823 -330 -249 678 O ATOM 51 CB THR A 10 48.174 -1.933 -24.559 1.00 14.37 C ANISOU 51 CB THR A 10 1998 1408 2054 -266 -514 485 C ATOM 52 OG1 THR A 10 47.188 -2.877 -24.939 1.00 23.51 O ANISOU 52 OG1 THR A 10 2244 3395 3293 -1067 -621 -235 O ATOM 53 CG2 THR A 10 49.424 -2.115 -25.388 1.00 17.33 C ANISOU 53 CG2 THR A 10 1796 2897 1893 -55 -684 1090 C ATOM 54 N CYS A 11 50.779 -1.749 -22.273 1.00 13.40 N ANISOU 54 N CYS A 11 1564 1833 1695 -606 -599 700 N ATOM 55 CA CYS A 11 51.946 -0.908 -21.952 1.00 11.17 C ANISOU 55 CA CYS A 11 1726 1486 1031 -529 -374 158 C ATOM 56 C CYS A 11 52.583 -0.486 -23.266 1.00 12.26 C ANISOU 56 C CYS A 11 1914 1595 1149 -574 -224 242 C ATOM 57 O CYS A 11 52.680 -1.248 -24.217 1.00 15.18 O ANISOU 57 O CYS A 11 2491 1955 1321 -990 101 -50 O ATOM 58 CB CYS A 11 52.902 -1.752 -21.125 1.00 12.66 C ANISOU 58 CB CYS A 11 1738 1876 1195 -597 -513 376 C ATOM 59 SG CYS A 11 52.265 -2.416 -19.580 1.00 13.61 S ANISOU 59 SG CYS A 11 2138 1615 1417 -550 -300 421 S ATOM 60 N SER A 12 53.058 0.752 -23.292 1.00 10.96 N ANISOU 60 N SER A 12 1598 1593 973 -439 -212 215 N ATOM 61 CA SER A 12 53.825 1.213 -24.450 1.00 8.88 C ANISOU 61 CA SER A 12 1327 1308 740 -282 -388 164 C ATOM 62 C SER A 12 55.216 0.639 -24.431 1.00 9.19 C ANISOU 62 C SER A 12 1263 1206 1025 -402 -436 312 C ATOM 63 O SER A 12 55.648 -0.055 -23.507 1.00 11.04 O ANISOU 63 O SER A 12 1570 1452 1172 -187 -531 434 O ATOM 64 CB SER A 12 53.840 2.750 -24.458 1.00 9.77 C ANISOU 64 CB SER A 12 1146 1302 1264 -348 -129 -56 C ATOM 65 OG SER A 12 54.954 3.211 -23.721 1.00 9.87 O ANISOU 65 OG SER A 12 1257 1251 1244 -320 -29 54 O ATOM 66 N ALA A 13 55.953 0.892 -25.518 1.00 8.65 N ANISOU 66 N ALA A 13 1420 860 1005 -135 -315 135 N ATOM 67 CA ALA A 13 57.320 0.352 -25.624 1.00 10.84 C ANISOU 67 CA ALA A 13 1445 1616 1060 -18 -313 -175 C ATOM 68 C ALA A 13 58.241 0.787 -24.516 1.00 10.00 C ANISOU 68 C ALA A 13 1547 1055 1197 -228 -464 109 C ATOM 69 O ALA A 13 59.270 0.174 -24.198 1.00 13.25 O ANISOU 69 O ALA A 13 1924 1952 1158 465 -532 53 O ATOM 70 CB ALA A 13 57.885 0.869 -26.949 1.00 13.29 C ANISOU 70 CB ALA A 13 1469 2446 1137 -225 -194 -145 C ATOM 71 N ALA A 14 58.079 1.962 -23.965 1.00 9.53 N ANISOU 71 N ALA A 14 1727 1073 822 -264 -320 347 N ATOM 72 CA ALA A 14 58.761 2.560 -22.851 1.00 9.63 C ANISOU 72 CA ALA A 14 1546 1363 750 -298 -150 66 C ATOM 73 C ALA A 14 58.399 1.973 -21.490 1.00 8.82 C ANISOU 73 C ALA A 14 1096 1428 826 72 -70 171 C ATOM 74 O ALA A 14 59.087 2.201 -20.493 1.00 10.45 O ANISOU 74 O ALA A 14 1383 1700 888 -128 -272 123 O ATOM 75 CB ALA A 14 58.450 4.057 -22.712 1.00 10.73 C ANISOU 75 CB ALA A 14 1495 1276 1305 -286 -640 176 C ATOM 76 N GLN A 15 57.292 1.272 -21.404 1.00 9.27 N ANISOU 76 N GLN A 15 1120 1619 784 -46 -26 129 N ATOM 77 CA GLN A 15 56.764 0.723 -20.140 1.00 10.11 C ANISOU 77 CA GLN A 15 1443 1505 893 -169 38 133 C ATOM 78 C GLN A 15 57.007 -0.767 -20.077 1.00 10.06 C ANISOU 78 C GLN A 15 1347 1505 970 -244 -187 161 C ATOM 79 O GLN A 15 57.277 -1.469 -21.074 1.00 12.87 O ANISOU 79 O GLN A 15 2362 1550 979 -399 -91 -27 O ATOM 80 CB GLN A 15 55.268 1.001 -20.055 1.00 9.74 C ANISOU 80 CB GLN A 15 1348 1150 1201 -438 170 257 C ATOM 81 CG GLN A 15 54.938 2.481 -19.899 1.00 9.47 C ANISOU 81 CG GLN A 15 1535 1237 828 -231 159 290 C ATOM 82 CD GLN A 15 53.424 2.674 -19.970 1.00 11.04 C ANISOU 82 CD GLN A 15 1553 1414 1229 -203 -94 117 C ATOM 83 OE1 GLN A 15 52.759 2.208 -20.897 1.00 12.31 O ANISOU 83 OE1 GLN A 15 1695 1824 1157 -338 -8 -17 O ATOM 84 NE2 GLN A 15 52.908 3.424 -18.993 1.00 11.21 N ANISOU 84 NE2 GLN A 15 1303 1556 1402 -117 -193 -48 N ATOM 85 N VAL A 16 56.912 -1.272 -18.858 1.00 11.55 N ANISOU 85 N VAL A 16 2040 1329 1020 -254 15 120 N ATOM 86 CA VAL A 16 56.982 -2.713 -18.522 1.00 11.27 C ANISOU 86 CA VAL A 16 1861 1306 1114 -103 -107 25 C ATOM 87 C VAL A 16 55.810 -2.987 -17.595 1.00 11.15 C ANISOU 87 C VAL A 16 2140 1254 843 -171 -221 313 C ATOM 88 O VAL A 16 55.419 -2.140 -16.790 1.00 11.50 O ANISOU 88 O VAL A 16 1575 1532 1263 -274 43 122 O ATOM 89 CB VAL A 16 58.365 -3.032 -17.940 1.00 14.19 C ANISOU 89 CB VAL A 16 2116 1766 1510 7 -493 35 C ATOM 90 CG1 VAL A 16 58.595 -2.206 -16.693 1.00 13.98 C ANISOU 90 CG1 VAL A 16 2210 1676 1426 139 -600 111 C ATOM 91 CG2 VAL A 16 58.495 -4.520 -17.657 1.00 20.92 C ANISOU 91 CG2 VAL A 16 3089 1701 3159 428 -1269 -223 C ATOM 92 N CYS A 17 55.295 -4.208 -17.625 1.00 13.85 N ANISOU 92 N CYS A 17 2425 1372 1464 -377 -164 311 N ATOM 93 CA CYS A 17 54.220 -4.587 -16.726 1.00 13.45 C ANISOU 93 CA CYS A 17 2294 1493 1322 -463 -196 186 C ATOM 94 C CYS A 17 54.797 -5.224 -15.463 1.00 13.99 C ANISOU 94 C CYS A 17 2417 1416 1484 -430 -243 337 C ATOM 95 O CYS A 17 55.423 -6.284 -15.585 1.00 15.97 O ANISOU 95 O CYS A 17 2660 1588 1821 -230 -315 203 O ATOM 96 CB CYS A 17 53.329 -5.644 -17.343 1.00 16.46 C ANISOU 96 CB CYS A 17 2666 1511 2076 -678 -667 472 C ATOM 97 SG CYS A 17 51.827 -6.012 -16.418 1.00 18.92 S ANISOU 97 SG CYS A 17 2730 2130 2327 -1036 -714 831 S ATOM 98 N LEU A 18 54.664 -4.517 -14.344 1.00 14.16 N ANISOU 98 N LEU A 18 2282 1762 1337 -110 -121 409 N ATOM 99 CA LEU A 18 55.178 -5.032 -13.071 1.00 15.24 C ANISOU 99 CA LEU A 18 2915 1478 1399 -696 -382 470 C ATOM 100 C LEU A 18 54.040 -5.038 -12.085 1.00 17.26 C ANISOU 100 C LEU A 18 2819 2211 1527 -678 -425 1107 C ATOM 101 O LEU A 18 53.395 -3.997 -11.889 1.00 18.81 O ANISOU 101 O LEU A 18 2272 2698 2176 -423 -155 1234 O ATOM 102 CB LEU A 18 56.388 -4.227 -12.648 1.00 15.28 C ANISOU 102 CB LEU A 18 2777 1897 1130 -636 -127 30 C ATOM 103 CG LEU A 18 57.611 -4.269 -13.540 1.00 17.18 C ANISOU 103 CG LEU A 18 3140 1958 1431 -816 274 -146 C ATOM 104 CD1 LEU A 18 58.642 -3.274 -13.021 1.00 15.31 C ANISOU 104 CD1 LEU A 18 2275 2083 1459 -158 -249 -102 C ATOM 105 CD2 LEU A 18 58.279 -5.635 -13.643 1.00 18.99 C ANISOU 105 CD2 LEU A 18 2725 2226 2264 -660 32 -390 C ATOM 106 N LYS A 19 53.835 -6.185 -11.447 1.00 21.22 N ANISOU 106 N LYS A 19 3271 2597 2196 -1128 -613 1573 N ATOM 107 CA LYS A 19 52.773 -6.351 -10.458 1.00 23.19 C ANISOU 107 CA LYS A 19 3082 3326 2401 -1048 -614 2022 C ATOM 108 C LYS A 19 51.464 -5.839 -11.015 1.00 24.54 C ANISOU 108 C LYS A 19 3413 3614 2297 -533 -482 2195 C ATOM 109 O LYS A 19 50.701 -5.243 -10.270 1.00 26.89 O ANISOU 109 O LYS A 19 2458 4403 3355 -1486 136 1603 O ATOM 110 CB LYS A 19 53.150 -5.608 -9.169 1.00 24.27 C ANISOU 110 CB LYS A 19 2282 4331 2610 -1187 10 1358 C ATOM 111 CG LYS A 19 54.503 -6.075 -8.633 1.00 27.55 C ANISOU 111 CG LYS A 19 2728 4221 3517 -1490 -867 1576 C ATOM 112 CD LYS A 19 54.806 -5.535 -7.250 1.00 31.77 C ANISOU 112 CD LYS A 19 3975 4803 3294 -1942 -1133 1911 C ATOM 113 CE LYS A 19 56.249 -5.866 -6.843 1.00 25.68 C ANISOU 113 CE LYS A 19 4585 3251 1922 -380 -960 431 C ATOM 114 NZ LYS A 19 56.547 -5.347 -5.479 1.00 32.42 N ANISOU 114 NZ LYS A 19 4404 4791 3122 -815 -1022 -1310 N ATOM 115 N GLY A 20 51.262 -6.151 -12.293 1.00 23.48 N ANISOU 115 N GLY A 20 3017 3140 2764 -1471 -913 1848 N ATOM 116 CA GLY A 20 49.970 -5.864 -12.914 1.00 25.70 C ANISOU 116 CA GLY A 20 3096 3237 3431 -1326 -1041 1977 C ATOM 117 C GLY A 20 49.664 -4.412 -13.193 1.00 25.60 C ANISOU 117 C GLY A 20 2186 3183 4359 -991 45 1677 C ATOM 118 O GLY A 20 48.511 -4.031 -13.459 1.00 27.31 O ANISOU 118 O GLY A 20 2077 3821 4478 -924 402 2191 O ATOM 119 N LYS A 21 50.711 -3.605 -13.266 1.00 19.58 N ANISOU 119 N LYS A 21 2291 2835 2313 -970 117 864 N ATOM 120 CA LYS A 21 50.547 -2.218 -13.736 1.00 17.84 C ANISOU 120 CA LYS A 21 1859 2922 1997 -870 175 914 C ATOM 121 C LYS A 21 51.622 -1.893 -14.764 1.00 16.82 C ANISOU 121 C LYS A 21 1641 3127 1623 -571 -5 968 C ATOM 122 O LYS A 21 52.780 -2.305 -14.618 1.00 15.77 O ANISOU 122 O LYS A 21 1829 2328 1833 -466 44 676 O ATOM 123 CB LYS A 21 50.716 -1.308 -12.506 0.52 13.99 C ANISOU 123 CB LYS A 21 1588 2510 1219 -667 -125 1559 C ATOM 124 CG ALYS A 21 50.293 0.137 -12.700 0.52 28.04 C ANISOU 124 CG ALYS A 21 4674 2807 3171 608 809 1184 C ATOM 125 CG BLYS A 21 49.655 -1.575 -11.441 0.48 25.45 C ANISOU 125 CG BLYS A 21 2969 3229 3472 -246 2036 771 C ATOM 126 N CYS A 22 51.261 -1.078 -15.750 1.00 14.23 N ANISOU 126 N CYS A 22 1710 2343 1355 -545 -27 454 N ATOM 127 CA CYS A 22 52.265 -0.512 -16.638 1.00 12.51 C ANISOU 127 CA CYS A 22 1808 1738 1206 -485 32 214 C ATOM 128 C CYS A 22 53.000 0.618 -15.941 1.00 12.26 C ANISOU 128 C CYS A 22 1688 1820 1151 -325 387 -142 C ATOM 129 O CYS A 22 52.409 1.562 -15.490 1.00 13.77 O ANISOU 129 O CYS A 22 1595 1810 1826 -222 393 -94 O ATOM 130 CB CYS A 22 51.617 0.045 -17.906 1.00 12.34 C ANISOU 130 CB CYS A 22 1375 1720 1594 -386 -7 474 C ATOM 131 SG CYS A 22 50.788 -1.169 -18.973 1.00 13.51 S ANISOU 131 SG CYS A 22 1699 1921 1512 -590 -250 608 S ATOM 132 N VAL A 23 54.329 0.484 -15.902 1.00 10.99 N ANISOU 132 N VAL A 23 1688 1081 1408 -221 123 109 N ATOM 133 CA VAL A 23 55.222 1.473 -15.319 1.00 10.32 C ANISOU 133 CA VAL A 23 1851 1061 1010 -206 144 48 C ATOM 134 C VAL A 23 56.354 1.742 -16.262 1.00 9.20 C ANISOU 134 C VAL A 23 1499 1155 842 -93 -70 186 C ATOM 135 O VAL A 23 56.683 0.922 -17.126 1.00 9.96 O ANISOU 135 O VAL A 23 1422 1261 1102 -292 -24 -5 O ATOM 136 CB VAL A 23 55.766 1.059 -13.954 1.00 11.52 C ANISOU 136 CB VAL A 23 1840 1528 1008 -152 286 278 C ATOM 137 CG1 VAL A 23 54.652 0.951 -12.930 1.00 14.55 C ANISOU 137 CG1 VAL A 23 2121 1974 1434 -59 631 611 C ATOM 138 CG2 VAL A 23 56.576 -0.218 -14.036 1.00 12.33 C ANISOU 138 CG2 VAL A 23 1796 1638 1251 -66 -35 226 C ATOM 139 N CYS A 24 56.955 2.911 -16.145 1.00 10.70 N ANISOU 139 N CYS A 24 1914 996 1156 -70 392 116 N ATOM 140 CA CYS A 24 58.128 3.183 -17.001 1.00 9.43 C ANISOU 140 CA CYS A 24 1358 1350 874 -197 -282 222 C ATOM 141 C CYS A 24 59.251 2.238 -16.622 1.00 9.67 C ANISOU 141 C CYS A 24 1411 1490 775 -155 -296 183 C ATOM 142 O CYS A 24 59.463 1.986 -15.465 1.00 10.20 O ANISOU 142 O CYS A 24 1578 1425 874 -99 -280 352 O ATOM 143 CB CYS A 24 58.602 4.627 -16.865 1.00 9.65 C ANISOU 143 CB CYS A 24 957 1470 1238 -224 -170 64 C ATOM 144 SG CYS A 24 57.353 5.887 -17.238 1.00 9.76 S ANISOU 144 SG CYS A 24 1342 1262 1105 -101 -46 191 S ATOM 145 N ASN A 25 59.924 1.696 -17.668 1.00 10.25 N ANISOU 145 N ASN A 25 1457 1588 851 -134 -155 253 N ATOM 146 CA ASN A 25 61.092 0.868 -17.364 1.00 10.07 C ANISOU 146 CA ASN A 25 1413 1268 1147 -252 -114 157 C ATOM 147 C ASN A 25 62.219 1.754 -16.807 1.00 10.28 C ANISOU 147 C ASN A 25 1251 1252 1402 -159 -32 181 C ATOM 148 O ASN A 25 62.164 2.981 -16.774 1.00 11.42 O ANISOU 148 O ASN A 25 1417 1163 1760 -254 -453 177 O ATOM 149 CB ASN A 25 61.545 0.092 -18.635 1.00 13.86 C ANISOU 149 CB ASN A 25 1628 2272 1368 86 -140 -282 C ATOM 150 CG ASN A 25 62.034 -1.289 -18.255 1.00 20.90 C ANISOU 150 CG ASN A 25 3031 2173 2736 710 -1172 -1088 C ATOM 151 OD1 ASN A 25 62.617 -1.502 -17.194 1.00 14.73 O ANISOU 151 OD1 ASN A 25 1536 1721 2339 -27 -136 -110 O ATOM 152 ND2 ASN A 25 61.625 -2.274 -19.040 1.00 26.49 N ANISOU 152 ND2 ASN A 25 3108 2649 4307 -3 -1404 -1539 N ATOM 153 N GLU A 26 63.266 1.104 -16.343 1.00 12.38 N ANISOU 153 N GLU A 26 1561 1326 1818 -195 -458 399 N ATOM 154 CA GLU A 26 64.406 1.837 -15.858 1.00 12.50 C ANISOU 154 CA GLU A 26 1442 1528 1779 -261 -357 363 C ATOM 155 C GLU A 26 64.966 2.705 -16.988 1.00 11.21 C ANISOU 155 C GLU A 26 949 1639 1670 -62 -148 41 C ATOM 156 O GLU A 26 64.768 2.414 -18.162 1.00 13.38 O ANISOU 156 O GLU A 26 1847 1583 1655 -367 -338 323 O ATOM 157 CB GLU A 26 65.464 0.954 -15.262 1.00 17.41 C ANISOU 157 CB GLU A 26 1459 1936 3221 -252 -662 727 C ATOM 158 CG AGLU A 26 65.448 -0.498 -15.200 0.55 19.38 C ANISOU 158 CG AGLU A 26 1590 1871 3903 657 450 313 C ATOM 159 CG BGLU A 26 66.139 -0.005 -16.192 0.45 16.72 C ANISOU 159 CG BGLU A 26 1451 1931 2972 4 694 1907 C ATOM 160 CD AGLU A 26 66.708 -1.123 -14.637 0.55 19.47 C ANISOU 160 CD AGLU A 26 2547 1807 3043 321 -1115 -311 C ATOM 161 CD BGLU A 26 67.022 -0.979 -15.421 0.45 17.27 C ANISOU 161 CD BGLU A 26 2726 916 2921 -338 -609 1165 C ATOM 162 OE1AGLU A 26 67.779 -0.514 -14.801 0.55 20.77 O ANISOU 162 OE1AGLU A 26 1752 4154 1987 817 296 103 O ATOM 163 OE1BGLU A 26 67.844 -0.603 -14.571 0.45 22.87 O ANISOU 163 OE1BGLU A 26 4536 953 3202 -357 -1466 797 O ATOM 164 OE2AGLU A 26 66.588 -2.188 -14.015 0.55 22.72 O ANISOU 164 OE2AGLU A 26 3524 2722 2388 1154 68 286 O ATOM 165 OE2BGLU A 26 66.874 -2.175 -15.692 0.45 21.00 O ANISOU 165 OE2BGLU A 26 2036 1341 4603 443 -934 -326 O ATOM 166 N VAL A 27 65.588 3.796 -16.582 1.00 12.90 N ANISOU 166 N VAL A 27 1923 1606 1373 -375 103 153 N ATOM 167 CA VAL A 27 66.095 4.799 -17.516 1.00 11.71 C ANISOU 167 CA VAL A 27 1867 1653 928 -166 -108 202 C ATOM 168 C VAL A 27 67.629 4.765 -17.573 1.00 12.40 C ANISOU 168 C VAL A 27 1863 1348 1499 -77 282 -3 C ATOM 169 O VAL A 27 68.286 4.829 -16.540 1.00 13.02 O ANISOU 169 O VAL A 27 1468 1924 1555 9 326 295 O ATOM 170 CB VAL A 27 65.657 6.226 -17.120 1.00 12.15 C ANISOU 170 CB VAL A 27 1375 1577 1663 -179 -269 198 C ATOM 171 CG1 VAL A 27 66.210 7.318 -18.047 1.00 12.99 C ANISOU 171 CG1 VAL A 27 1878 1680 1377 -349 -216 144 C ATOM 172 CG2 VAL A 27 64.129 6.314 -17.009 1.00 15.07 C ANISOU 172 CG2 VAL A 27 1438 1941 2347 -210 -209 270 C ATOM 173 N HIS A 28 68.101 4.611 -18.789 1.00 14.08 N ANISOU 173 N HIS A 28 2615 1152 1582 -67 639 123 N ATOM 174 CA HIS A 28 69.546 4.649 -19.038 1.00 16.18 C ANISOU 174 CA HIS A 28 2764 1128 2257 328 1216 361 C ATOM 175 C HIS A 28 69.749 5.432 -20.320 1.00 15.07 C ANISOU 175 C HIS A 28 2338 1497 1888 -364 499 110 C ATOM 176 O HIS A 28 69.394 4.906 -21.368 1.00 18.13 O ANISOU 176 O HIS A 28 2830 1853 2208 -457 378 -226 O ATOM 177 CB HIS A 28 70.133 3.241 -19.197 1.00 24.97 C ANISOU 177 CB HIS A 28 4392 1506 3589 970 2364 428 C ATOM 178 CG HIS A 28 70.011 2.466 -17.910 1.00 23.54 C ANISOU 178 CG HIS A 28 3020 1626 4297 1295 1814 1187 C ATOM 179 ND1 HIS A 28 70.896 2.629 -16.855 1.00 27.70 N ANISOU 179 ND1 HIS A 28 3310 2215 4999 367 1290 1784 N ATOM 180 CD2 HIS A 28 69.082 1.609 -17.416 1.00 29.09 C ANISOU 180 CD2 HIS A 28 2599 3562 4890 689 735 2587 C ATOM 181 CE1 HIS A 28 70.582 1.877 -15.819 1.00 26.36 C ANISOU 181 CE1 HIS A 28 3229 2723 4064 -521 1362 1073 C ATOM 182 NE2 HIS A 28 69.459 1.263 -16.112 1.00 26.86 N ANISOU 182 NE2 HIS A 28 2532 2610 5064 329 189 2491 N ATOM 183 N CYS A 29 70.118 6.686 -20.174 1.00 12.59 N ANISOU 183 N CYS A 29 1825 1450 1507 -300 563 248 N ATOM 184 CA CYS A 29 70.368 7.543 -21.322 1.00 11.10 C ANISOU 184 CA CYS A 29 1607 1562 1050 -255 453 30 C ATOM 185 C CYS A 29 71.755 8.151 -21.183 1.00 10.49 C ANISOU 185 C CYS A 29 1499 1025 1461 -32 348 174 C ATOM 186 O CYS A 29 72.056 8.817 -20.190 1.00 13.03 O ANISOU 186 O CYS A 29 1586 1811 1553 -146 103 59 O ATOM 187 CB CYS A 29 69.303 8.629 -21.383 1.00 12.22 C ANISOU 187 CB CYS A 29 1557 1731 1355 -184 158 141 C ATOM 188 SG CYS A 29 67.622 8.087 -21.758 1.00 12.53 S ANISOU 188 SG CYS A 29 1666 1583 1510 -262 305 -6 S ATOM 189 N ARG A 30 72.519 8.061 -22.254 1.00 10.89 N ANISOU 189 N ARG A 30 1288 1375 1476 -10 217 282 N ATOM 190 CA ARG A 30 73.863 8.607 -22.258 1.00 12.38 C ANISOU 190 CA ARG A 30 1347 1367 1991 59 358 403 C ATOM 191 C ARG A 30 73.885 10.107 -22.593 1.00 9.78 C ANISOU 191 C ARG A 30 1023 1333 1360 44 371 190 C ATOM 192 O ARG A 30 74.774 10.792 -22.131 1.00 12.00 O ANISOU 192 O ARG A 30 1394 1506 1659 -79 -103 256 O ATOM 193 CB AARG A 30 74.682 7.912 -23.365 0.55 13.35 C ANISOU 193 CB AARG A 30 1448 1341 2284 670 497 691 C ATOM 194 CB BARG A 30 74.732 7.862 -23.283 0.45 13.72 C ANISOU 194 CB BARG A 30 1110 1526 2577 387 180 62 C ATOM 195 CG AARG A 30 76.114 8.383 -23.478 0.55 14.63 C ANISOU 195 CG AARG A 30 1803 1867 1889 87 763 391 C ATOM 196 CG BARG A 30 74.874 6.380 -22.986 0.45 11.37 C ANISOU 196 CG BARG A 30 1344 1725 1251 368 371 429 C ATOM 197 CD AARG A 30 77.008 7.595 -24.382 0.55 22.06 C ANISOU 197 CD AARG A 30 1650 5035 1697 670 473 -587 C ATOM 198 CD BARG A 30 75.468 5.572 -24.127 0.45 10.59 C ANISOU 198 CD BARG A 30 1317 1249 1457 8 490 340 C ATOM 199 NE AARG A 30 78.397 7.975 -24.526 0.55 21.84 N ANISOU 199 NE AARG A 30 1753 4114 2430 595 525 -540 N ATOM 200 NE BARG A 30 75.791 4.213 -23.662 0.45 15.47 N ANISOU 200 NE BARG A 30 2637 1801 1439 893 -214 433 N ATOM 201 CZ AARG A 30 79.348 7.856 -23.631 0.55 15.95 C ANISOU 201 CZ AARG A 30 1836 1876 2350 -488 511 423 C ATOM 202 CZ BARG A 30 76.199 3.202 -24.404 0.45 15.14 C ANISOU 202 CZ BARG A 30 3941 632 1180 -391 -510 351 C ATOM 203 NH1AARG A 30 79.060 7.461 -22.408 0.55 35.17 N ANISOU 203 NH1AARG A 30 1838 9401 2125 -1086 1093 724 N ATOM 204 NH1BARG A 30 76.376 3.426 -25.702 0.45 11.06 N ANISOU 204 NH1BARG A 30 1646 1152 1403 384 -47 709 N ATOM 205 NH2AARG A 30 80.607 8.196 -23.936 0.55 18.14 N ANISOU 205 NH2AARG A 30 1818 3097 1979 -347 752 495 N ATOM 206 NH2BARG A 30 76.479 1.997 -23.895 0.45 18.48 N ANISOU 206 NH2BARG A 30 4390 720 1913 -518 -529 817 N ATOM 207 N ILE A 31 72.940 10.567 -23.389 1.00 9.82 N ANISOU 207 N ILE A 31 1222 1279 1229 -89 180 178 N ATOM 208 CA ILE A 31 72.961 11.993 -23.743 1.00 9.32 C ANISOU 208 CA ILE A 31 991 1219 1331 -32 380 99 C ATOM 209 C ILE A 31 72.878 12.888 -22.510 1.00 9.71 C ANISOU 209 C ILE A 31 1128 1417 1145 -9 221 85 C ATOM 210 O ILE A 31 72.153 12.609 -21.552 1.00 10.84 O ANISOU 210 O ILE A 31 1254 1609 1256 -228 264 96 O ATOM 211 CB ILE A 31 71.818 12.311 -24.725 1.00 9.19 C ANISOU 211 CB ILE A 31 1264 1013 1215 -181 216 51 C ATOM 212 CG1 ILE A 31 70.450 11.871 -24.226 1.00 9.53 C ANISOU 212 CG1 ILE A 31 1144 1486 990 -67 200 -78 C ATOM 213 CG2 ILE A 31 72.120 11.754 -26.111 1.00 11.07 C ANISOU 213 CG2 ILE A 31 995 1765 1445 -184 295 -394 C ATOM 214 CD1 ILE A 31 69.274 12.347 -25.046 1.00 11.20 C ANISOU 214 CD1 ILE A 31 1325 1772 1160 -193 -118 -305 C ATOM 215 N ARG A 32 73.627 14.006 -22.597 1.00 9.32 N ANISOU 215 N ARG A 32 1409 1287 846 38 414 102 N ATOM 216 CA ARG A 32 73.649 15.041 -21.573 1.00 9.22 C ANISOU 216 CA ARG A 32 1070 1212 1222 111 518 -18 C ATOM 217 C ARG A 32 72.925 16.266 -22.121 1.00 8.60 C ANISOU 217 C ARG A 32 1144 1143 980 -146 344 64 C ATOM 218 O ARG A 32 73.306 16.817 -23.133 1.00 10.67 O ANISOU 218 O ARG A 32 1283 1722 1050 -121 350 203 O ATOM 219 CB ARG A 32 75.084 15.398 -21.180 1.00 9.89 C ANISOU 219 CB ARG A 32 1200 1474 1084 47 352 0 C ATOM 220 CG ARG A 32 75.764 14.194 -20.487 1.00 13.14 C ANISOU 220 CG ARG A 32 1689 2094 1209 315 2 141 C ATOM 221 CD ARG A 32 76.537 13.401 -21.511 1.00 14.61 C ANISOU 221 CD ARG A 32 1710 1740 2100 435 -131 -233 C ATOM 222 NE ARG A 32 77.521 12.636 -20.750 1.00 19.70 N ANISOU 222 NE ARG A 32 1539 2277 3669 437 24 929 N ATOM 223 CZ ARG A 32 77.971 11.466 -20.787 1.00 17.59 C ANISOU 223 CZ ARG A 32 2425 2142 2116 378 -47 921 C ATOM 224 NH1 ARG A 32 77.405 10.628 -21.617 1.00 31.63 N ANISOU 224 NH1 ARG A 32 2873 3790 5353 -733 18 -987 N ATOM 225 NH2 ARG A 32 78.958 11.061 -19.985 1.00 25.07 N ANISOU 225 NH2 ARG A 32 2675 3266 3583 853 -228 2006 N ATOM 226 N CYS A 33 71.827 16.625 -21.483 1.00 9.28 N ANISOU 226 N CYS A 33 1149 1394 982 321 193 357 N ATOM 227 CA CYS A 33 70.879 17.592 -21.978 1.00 8.56 C ANISOU 227 CA CYS A 33 1309 1209 733 147 -139 278 C ATOM 228 C CYS A 33 70.682 18.755 -21.009 1.00 8.95 C ANISOU 228 C CYS A 33 1083 1228 1090 46 43 104 C ATOM 229 O CYS A 33 70.469 18.599 -19.816 1.00 10.16 O ANISOU 229 O CYS A 33 1386 1417 1055 26 255 27 O ATOM 230 CB CYS A 33 69.533 16.894 -22.164 1.00 11.63 C ANISOU 230 CB CYS A 33 1308 1486 1624 144 -275 -263 C ATOM 231 SG CYS A 33 69.528 15.531 -23.338 1.00 11.16 S ANISOU 231 SG CYS A 33 1466 1323 1452 176 -168 -47 S ATOM 232 N LYS A 34 70.628 19.973 -21.603 1.00 9.77 N ANISOU 232 N LYS A 34 1474 1196 1044 -4 -8 36 N ATOM 233 CA LYS A 34 70.502 21.199 -20.816 1.00 10.19 C ANISOU 233 CA LYS A 34 1237 1287 1349 42 164 -141 C ATOM 234 C LYS A 34 69.206 21.288 -20.030 1.00 10.39 C ANISOU 234 C LYS A 34 1279 1597 1072 35 45 -96 C ATOM 235 O LYS A 34 69.219 21.931 -18.954 1.00 11.47 O ANISOU 235 O LYS A 34 1611 1544 1201 62 115 -281 O ATOM 236 CB LYS A 34 70.674 22.433 -21.689 1.00 15.41 C ANISOU 236 CB LYS A 34 2491 1202 2163 -404 817 -108 C ATOM 237 CG LYS A 34 69.986 23.705 -21.356 1.00 34.61 C ANISOU 237 CG LYS A 34 6551 1218 5381 754 2109 533 C ATOM 238 CD LYS A 34 70.114 24.721 -22.498 1.00 39.29 C ANISOU 238 CD LYS A 34 8128 1584 5218 163 21 851 C ATOM 239 CE LYS A 34 69.901 24.077 -23.851 1.00 46.01 C ANISOU 239 CE LYS A 34 7939 4652 4888 -340 3501 -625 C ATOM 240 NZ LYS A 34 69.553 24.974 -24.974 1.00 64.91 N ANISOU 240 NZ LYS A 34 4393 14037 6234 672 -1788 1378 N ATOM 241 N TYR A 35 68.145 20.700 -20.500 1.00 9.14 N ANISOU 241 N TYR A 35 1311 1109 1053 5 138 24 N ATOM 242 CA TYR A 35 66.876 20.686 -19.789 1.00 10.43 C ANISOU 242 CA TYR A 35 1331 1654 980 27 217 201 C ATOM 243 C TYR A 35 66.463 19.256 -19.469 1.00 11.33 C ANISOU 243 C TYR A 35 1173 1635 1498 -83 248 103 C ATOM 244 O TYR A 35 65.277 18.985 -19.275 1.00 11.03 O ANISOU 244 O TYR A 35 1190 1678 1323 20 249 90 O ATOM 245 CB TYR A 35 65.746 21.399 -20.543 1.00 12.01 C ANISOU 245 CB TYR A 35 1629 1955 977 547 281 -42 C ATOM 246 CG TYR A 35 66.137 22.746 -21.037 1.00 15.23 C ANISOU 246 CG TYR A 35 2218 1685 1883 910 514 91 C ATOM 247 CD1 TYR A 35 66.454 23.757 -20.176 1.00 20.78 C ANISOU 247 CD1 TYR A 35 3892 1932 2071 32 418 148 C ATOM 248 CD2 TYR A 35 66.167 23.005 -22.406 1.00 17.63 C ANISOU 248 CD2 TYR A 35 3193 1544 1963 555 368 366 C ATOM 249 CE1 TYR A 35 66.807 25.027 -20.635 1.00 25.82 C ANISOU 249 CE1 TYR A 35 4813 1845 3155 55 -90 502 C ATOM 250 CE2 TYR A 35 66.536 24.245 -22.867 1.00 25.33 C ANISOU 250 CE2 TYR A 35 4769 2003 2852 -99 1062 506 C ATOM 251 CZ TYR A 35 66.882 25.236 -21.988 1.00 23.60 C ANISOU 251 CZ TYR A 35 3982 1652 3333 -131 132 877 C ATOM 252 OH TYR A 35 67.185 26.499 -22.454 1.00 31.12 O ANISOU 252 OH TYR A 35 4620 2362 4841 -1203 -312 1537 O ATOM 253 N GLY A 36 67.391 18.320 -19.414 1.00 10.34 N ANISOU 253 N GLY A 36 1143 1537 1249 -171 49 199 N ATOM 254 CA GLY A 36 67.035 16.951 -19.090 1.00 9.83 C ANISOU 254 CA GLY A 36 988 1609 1139 -242 -72 272 C ATOM 255 C GLY A 36 66.358 16.244 -20.245 1.00 10.22 C ANISOU 255 C GLY A 36 1214 1626 1044 -262 25 198 C ATOM 256 O GLY A 36 66.362 16.710 -21.397 1.00 9.73 O ANISOU 256 O GLY A 36 1335 1331 1032 0 102 140 O ATOM 257 N LEU A 37 65.798 15.078 -19.976 1.00 10.57 N ANISOU 257 N LEU A 37 1353 1654 1011 -360 91 211 N ATOM 258 CA LEU A 37 65.272 14.211 -21.003 1.00 10.28 C ANISOU 258 CA LEU A 37 1311 1450 1144 -135 -82 201 C ATOM 259 C LEU A 37 63.822 14.537 -21.321 1.00 10.55 C ANISOU 259 C LEU A 37 1320 1472 1218 -79 -15 389 C ATOM 260 O LEU A 37 63.063 14.967 -20.440 1.00 12.07 O ANISOU 260 O LEU A 37 1238 1754 1595 -220 56 180 O ATOM 261 CB LEU A 37 65.354 12.748 -20.543 1.00 10.88 C ANISOU 261 CB LEU A 37 1228 1504 1401 -60 -87 269 C ATOM 262 CG LEU A 37 66.793 12.268 -20.272 1.00 10.19 C ANISOU 262 CG LEU A 37 1068 1564 1241 -199 -116 216 C ATOM 263 CD1 LEU A 37 66.690 10.873 -19.630 1.00 10.36 C ANISOU 263 CD1 LEU A 37 1034 1704 1197 -115 -19 362 C ATOM 264 CD2 LEU A 37 67.580 12.226 -21.537 1.00 10.66 C ANISOU 264 CD2 LEU A 37 1247 1470 1332 -268 -9 364 C ATOM 265 N LYS A 38 63.403 14.235 -22.528 1.00 11.88 N ANISOU 265 N LYS A 38 1226 2049 1239 -168 -73 496 N ATOM 266 CA LYS A 38 62.014 14.377 -22.961 1.00 11.47 C ANISOU 266 CA LYS A 38 1373 1280 1707 60 -250 555 C ATOM 267 C LYS A 38 61.171 13.256 -22.374 1.00 11.39 C ANISOU 267 C LYS A 38 1224 1254 1850 -31 -377 370 C ATOM 268 O LYS A 38 61.546 12.097 -22.374 1.00 14.56 O ANISOU 268 O LYS A 38 1088 1305 3140 18 138 778 O ATOM 269 CB LYS A 38 62.057 14.315 -24.506 1.00 14.88 C ANISOU 269 CB LYS A 38 2066 1918 1671 -356 -647 490 C ATOM 270 CG LYS A 38 60.814 14.665 -25.230 1.00 19.01 C ANISOU 270 CG LYS A 38 2411 3020 1792 702 -578 262 C ATOM 271 CD LYS A 38 61.010 14.782 -26.705 1.00 19.51 C ANISOU 271 CD LYS A 38 2397 3163 1851 622 -626 764 C ATOM 272 CE LYS A 38 61.575 16.058 -27.289 1.00 28.93 C ANISOU 272 CE LYS A 38 4907 3245 2841 110 -549 1108 C ATOM 273 NZ LYS A 38 61.374 16.060 -28.774 1.00 57.21 N ANISOU 273 NZ LYS A 38 7517 10373 3847 -5936 -4407 4595 N ATOM 274 N LYS A 39 59.976 13.617 -21.900 1.00 11.36 N ANISOU 274 N LYS A 39 1185 1048 2083 -71 -357 421 N ATOM 275 CA LYS A 39 59.017 12.665 -21.369 1.00 11.14 C ANISOU 275 CA LYS A 39 1369 933 1932 -66 -198 275 C ATOM 276 C LYS A 39 57.889 12.412 -22.378 1.00 11.14 C ANISOU 276 C LYS A 39 1165 998 2070 54 -233 223 C ATOM 277 O LYS A 39 57.484 13.348 -23.030 1.00 13.06 O ANISOU 277 O LYS A 39 1132 1037 2792 47 -376 510 O ATOM 278 CB LYS A 39 58.382 13.182 -20.086 1.00 11.96 C ANISOU 278 CB LYS A 39 1339 1116 2089 31 -207 99 C ATOM 279 CG LYS A 39 59.336 13.119 -18.896 1.00 12.69 C ANISOU 279 CG LYS A 39 1492 1367 1963 114 -177 132 C ATOM 280 CD LYS A 39 58.705 13.776 -17.663 1.00 13.95 C ANISOU 280 CD LYS A 39 1735 1532 2032 6 62 37 C ATOM 281 CE LYS A 39 59.353 13.392 -16.365 1.00 18.35 C ANISOU 281 CE LYS A 39 3240 1708 2025 -304 -298 261 C ATOM 282 NZ LYS A 39 58.898 12.128 -15.757 1.00 17.81 N ANISOU 282 NZ LYS A 39 2597 1801 2367 -90 350 339 N ATOM 283 N ASP A 40 57.460 11.149 -22.458 1.00 9.14 N ANISOU 283 N ASP A 40 955 1007 1509 103 -46 294 N ATOM 284 CA ASP A 40 56.261 10.853 -23.220 1.00 9.57 C ANISOU 284 CA ASP A 40 1081 1114 1441 2 -114 292 C ATOM 285 C ASP A 40 55.037 11.145 -22.356 1.00 8.88 C ANISOU 285 C ASP A 40 980 946 1446 17 -185 113 C ATOM 286 O ASP A 40 55.152 11.684 -21.276 1.00 10.54 O ANISOU 286 O ASP A 40 1293 1345 1367 -48 -228 102 O ATOM 287 CB ASP A 40 56.306 9.428 -23.739 1.00 9.52 C ANISOU 287 CB ASP A 40 1346 1138 1134 120 47 296 C ATOM 288 CG ASP A 40 56.157 8.316 -22.711 1.00 8.27 C ANISOU 288 CG ASP A 40 998 1085 1060 -204 -140 214 C ATOM 289 OD1 ASP A 40 55.702 8.579 -21.592 1.00 9.56 O ANISOU 289 OD1 ASP A 40 1184 1455 993 -62 -33 309 O ATOM 290 OD2 ASP A 40 56.531 7.147 -23.037 1.00 9.99 O ANISOU 290 OD2 ASP A 40 1336 971 1488 -140 -142 194 O ATOM 291 N GLU A 41 53.872 10.821 -22.888 1.00 9.66 N ANISOU 291 N GLU A 41 1001 1312 1359 21 -142 132 N ATOM 292 CA GLU A 41 52.641 11.181 -22.198 1.00 10.09 C ANISOU 292 CA GLU A 41 990 1352 1491 12 -108 -5 C ATOM 293 C GLU A 41 52.379 10.398 -20.947 1.00 11.81 C ANISOU 293 C GLU A 41 1613 1488 1386 264 203 -63 C ATOM 294 O GLU A 41 51.479 10.797 -20.202 1.00 14.16 O ANISOU 294 O GLU A 41 1610 1910 1861 311 418 198 O ATOM 295 CB GLU A 41 51.462 11.047 -23.202 1.00 12.01 C ANISOU 295 CB GLU A 41 1110 1651 1801 268 -323 -160 C ATOM 296 CG GLU A 41 51.653 12.039 -24.341 1.00 12.63 C ANISOU 296 CG GLU A 41 1644 1394 1760 400 -513 -160 C ATOM 297 CD GLU A 41 52.447 11.551 -25.525 1.00 11.82 C ANISOU 297 CD GLU A 41 1703 1304 1483 311 -638 -91 C ATOM 298 OE1 GLU A 41 52.923 10.396 -25.499 1.00 11.62 O ANISOU 298 OE1 GLU A 41 1706 1228 1480 193 -344 -80 O ATOM 299 OE2 GLU A 41 52.694 12.348 -26.459 1.00 13.48 O ANISOU 299 OE2 GLU A 41 1952 1556 1612 571 -579 125 O ATOM 300 N ASN A 42 53.157 9.355 -20.685 1.00 11.36 N ANISOU 300 N ASN A 42 1535 1343 1440 97 34 -14 N ATOM 301 CA ASN A 42 53.066 8.668 -19.409 1.00 11.51 C ANISOU 301 CA ASN A 42 1156 1683 1535 159 441 117 C ATOM 302 C ASN A 42 54.180 9.099 -18.439 1.00 12.74 C ANISOU 302 C ASN A 42 1631 1686 1525 42 60 420 C ATOM 303 O ASN A 42 54.296 8.610 -17.316 1.00 17.17 O ANISOU 303 O ASN A 42 2747 2382 1394 -228 236 550 O ATOM 304 CB ASN A 42 53.194 7.147 -19.543 1.00 13.65 C ANISOU 304 CB ASN A 42 1696 1658 1834 123 -106 369 C ATOM 305 CG ASN A 42 51.986 6.652 -20.304 1.00 14.36 C ANISOU 305 CG ASN A 42 1258 1914 2286 -340 466 237 C ATOM 306 OD1 ASN A 42 50.861 6.831 -19.804 1.00 27.19 O ANISOU 306 OD1 ASN A 42 1518 4335 4478 -331 1145 -1308 O ATOM 307 ND2 ASN A 42 52.251 6.144 -21.437 1.00 11.63 N ANISOU 307 ND2 ASN A 42 807 1583 2028 -159 -40 460 N ATOM 308 N GLY A 43 55.058 10.011 -18.904 1.00 10.39 N ANISOU 308 N GLY A 43 1579 1094 1276 164 -42 159 N ATOM 309 CA GLY A 43 56.170 10.416 -18.092 1.00 10.63 C ANISOU 309 CA GLY A 43 1732 1273 1034 126 -41 95 C ATOM 310 C GLY A 43 57.447 9.668 -18.358 1.00 9.14 C ANISOU 310 C GLY A 43 1484 951 1037 -197 -42 234 C ATOM 311 O GLY A 43 58.498 9.996 -17.731 1.00 10.51 O ANISOU 311 O GLY A 43 1633 1290 1069 -145 -185 -51 O ATOM 312 N CYS A 44 57.458 8.693 -19.268 1.00 9.17 N ANISOU 312 N CYS A 44 1115 1114 1253 -126 -171 68 N ATOM 313 CA CYS A 44 58.642 7.896 -19.465 1.00 9.03 C ANISOU 313 CA CYS A 44 1080 1154 1197 -57 -193 258 C ATOM 314 C CYS A 44 59.640 8.587 -20.402 1.00 9.11 C ANISOU 314 C CYS A 44 1102 1041 1320 121 -129 365 C ATOM 315 O CYS A 44 59.260 9.312 -21.312 1.00 9.37 O ANISOU 315 O CYS A 44 1182 1270 1108 135 -84 354 O ATOM 316 CB CYS A 44 58.246 6.536 -20.093 1.00 8.94 C ANISOU 316 CB CYS A 44 1041 1300 1058 -93 21 64 C ATOM 317 SG CYS A 44 56.929 5.641 -19.226 1.00 9.57 S ANISOU 317 SG CYS A 44 1210 1311 1117 -169 -61 122 S ATOM 318 N GLU A 45 60.913 8.317 -20.151 1.00 13.13 N ANISOU 318 N GLU A 45 1078 1711 2200 -114 -171 1280 N ATOM 319 CA GLU A 45 62.028 8.901 -20.864 1.00 13.43 C ANISOU 319 CA GLU A 45 1155 1974 1976 -93 -25 1099 C ATOM 320 C GLU A 45 62.675 7.912 -21.813 1.00 13.37 C ANISOU 320 C GLU A 45 1428 2131 1521 -639 -296 666 C ATOM 321 O GLU A 45 63.788 7.460 -21.633 1.00 14.65 O ANISOU 321 O GLU A 45 1792 2490 1284 27 -195 175 O ATOM 322 CB AGLU A 45 62.958 9.431 -19.744 0.70 13.59 C ANISOU 322 CB AGLU A 45 1186 1793 2185 -261 444 194 C ATOM 323 CB BGLU A 45 63.016 9.651 -20.002 0.30 10.43 C ANISOU 323 CB BGLU A 45 777 1826 1361 18 873 523 C ATOM 324 CG AGLU A 45 62.486 10.491 -18.750 0.70 13.28 C ANISOU 324 CG AGLU A 45 1331 853 2862 -243 949 635 C ATOM 325 CG BGLU A 45 62.369 11.049 -19.852 0.30 14.41 C ANISOU 325 CG BGLU A 45 2141 2416 918 972 417 402 C ATOM 326 CD AGLU A 45 61.884 10.056 -17.418 0.70 13.38 C ANISOU 326 CD AGLU A 45 2021 1637 1426 -650 -171 152 C ATOM 327 CD BGLU A 45 62.800 11.552 -18.483 0.30 8.41 C ANISOU 327 CD BGLU A 45 413 1484 1300 -195 319 658 C ATOM 328 OE1AGLU A 45 61.574 8.909 -17.053 0.70 13.88 O ANISOU 328 OE1AGLU A 45 1546 2205 1524 -841 -937 1250 O ATOM 329 OE1BGLU A 45 63.331 10.666 -17.779 0.30 7.58 O ANISOU 329 OE1BGLU A 45 716 772 1394 -282 -24 106 O ATOM 330 OE2AGLU A 45 61.508 10.925 -16.586 0.70 20.68 O ANISOU 330 OE2AGLU A 45 2631 3207 2019 -171 -234 -775 O ATOM 331 OE2BGLU A 45 62.718 12.784 -18.292 0.30 12.39 O ANISOU 331 OE2BGLU A 45 1233 1308 2167 -174 -619 979 O ATOM 332 N TYR A 46 61.932 7.441 -22.806 1.00 21.70 N ANISOU 332 N TYR A 46 1738 4856 1650 -1671 -231 323 N ATOM 333 CA TYR A 46 62.313 6.419 -23.762 1.00 20.66 C ANISOU 333 CA TYR A 46 2520 4049 1280 -2101 -790 485 C ATOM 334 C TYR A 46 61.525 6.635 -25.055 1.00 28.86 C ANISOU 334 C TYR A 46 1833 7885 1246 -1435 -529 428 C ATOM 335 O TYR A 46 60.338 6.870 -25.045 1.00 54.94 O ANISOU 335 O TYR A 46 1126 17789 1959 -2290 -249 1796 O ATOM 336 CB TYR A 46 62.097 4.978 -23.274 1.00 31.45 C ANISOU 336 CB TYR A 46 5326 4511 2113 -3352 901 621 C ATOM 337 CG TYR A 46 62.491 3.955 -24.327 1.00 30.44 C ANISOU 337 CG TYR A 46 5946 3669 1951 -3113 380 958 C ATOM 338 CD1 TYR A 46 63.814 3.572 -24.504 1.00 29.23 C ANISOU 338 CD1 TYR A 46 6233 3193 1678 -2348 -575 331 C ATOM 339 CD2 TYR A 46 61.552 3.344 -25.152 1.00 32.28 C ANISOU 339 CD2 TYR A 46 5769 4038 2458 -3039 277 715 C ATOM 340 CE1 TYR A 46 64.165 2.639 -25.452 1.00 34.45 C ANISOU 340 CE1 TYR A 46 7005 3168 2915 -1197 -2081 -472 C ATOM 341 CE2 TYR A 46 61.914 2.444 -26.134 1.00 33.19 C ANISOU 341 CE2 TYR A 46 5921 4619 2070 -3485 406 592 C ATOM 342 CZ TYR A 46 63.235 2.080 -26.306 1.00 35.24 C ANISOU 342 CZ TYR A 46 6606 4422 2361 -1505 -1569 -563 C ATOM 343 OH TYR A 46 63.587 1.146 -27.279 1.00 36.52 O ANISOU 343 OH TYR A 46 7452 4023 2403 -2138 -1119 -591 O ATOM 344 N PRO A 47 62.142 6.681 -26.203 1.00 20.82 N ANISOU 344 N PRO A 47 1645 4971 1296 -1356 -517 486 N ATOM 345 CA PRO A 47 63.579 6.731 -26.430 1.00 16.07 C ANISOU 345 CA PRO A 47 1713 2722 1671 -874 -451 926 C ATOM 346 C PRO A 47 64.218 8.032 -25.859 1.00 15.28 C ANISOU 346 C PRO A 47 1527 2542 1738 -592 -7 507 C ATOM 347 O PRO A 47 63.503 8.954 -25.492 1.00 17.21 O ANISOU 347 O PRO A 47 1532 3054 1951 -146 22 568 O ATOM 348 CB PRO A 47 63.713 6.784 -27.955 1.00 20.55 C ANISOU 348 CB PRO A 47 2248 3954 1606 -1206 -92 344 C ATOM 349 CG PRO A 47 62.453 6.241 -28.473 1.00 24.27 C ANISOU 349 CG PRO A 47 2123 5808 1289 -1471 -157 814 C ATOM 350 CD PRO A 47 61.421 6.688 -27.489 1.00 21.34 C ANISOU 350 CD PRO A 47 2012 4810 1287 -944 -596 720 C ATOM 351 N CYS A 48 65.519 7.940 -25.637 1.00 13.36 N ANISOU 351 N CYS A 48 1558 1942 1577 -398 -53 135 N ATOM 352 CA CYS A 48 66.274 9.045 -25.042 1.00 11.98 C ANISOU 352 CA CYS A 48 1381 1651 1518 -205 252 23 C ATOM 353 C CYS A 48 66.323 10.216 -26.020 1.00 12.80 C ANISOU 353 C CYS A 48 1285 2010 1569 -353 199 309 C ATOM 354 O CYS A 48 66.869 10.084 -27.108 1.00 14.49 O ANISOU 354 O CYS A 48 2239 1851 1414 -442 191 67 O ATOM 355 CB CYS A 48 67.724 8.672 -24.747 1.00 12.43 C ANISOU 355 CB CYS A 48 1297 1761 1665 -302 241 211 C ATOM 356 SG CYS A 48 67.846 7.249 -23.590 1.00 12.11 S ANISOU 356 SG CYS A 48 1543 1651 1406 -190 218 37 S ATOM 357 N SER A 49 65.838 11.383 -25.598 1.00 12.57 N ANISOU 357 N SER A 49 1375 1969 1431 -214 339 590 N ATOM 358 CA SER A 49 65.906 12.627 -26.364 1.00 12.06 C ANISOU 358 CA SER A 49 1358 1939 1286 -630 131 448 C ATOM 359 C SER A 49 65.990 13.781 -25.377 1.00 11.80 C ANISOU 359 C SER A 49 987 2097 1399 -528 -36 279 C ATOM 360 O SER A 49 65.492 13.650 -24.250 1.00 12.93 O ANISOU 360 O SER A 49 1111 2444 1357 -484 0 342 O ATOM 361 CB SER A 49 64.646 12.763 -27.293 1.00 15.52 C ANISOU 361 CB SER A 49 2367 1863 1665 -283 -736 169 C ATOM 362 OG SER A 49 64.785 14.010 -27.919 1.00 59.55 O ANISOU 362 OG SER A 49 6935 5470 10220 -2534 -5089 5749 O ATOM 363 N CYS A 50 66.571 14.903 -25.738 1.00 12.65 N ANISOU 363 N CYS A 50 1693 1924 1189 -476 -14 277 N ATOM 364 CA CYS A 50 66.629 16.074 -24.854 1.00 11.19 C ANISOU 364 CA CYS A 50 1376 1665 1209 93 -6 448 C ATOM 365 C CYS A 50 65.280 16.776 -24.872 1.00 14.26 C ANISOU 365 C CYS A 50 1380 2836 1201 397 32 751 C ATOM 366 O CYS A 50 64.709 16.970 -25.982 1.00 16.38 O ANISOU 366 O CYS A 50 1670 3249 1305 531 -155 651 O ATOM 367 CB CYS A 50 67.716 17.045 -25.265 1.00 11.10 C ANISOU 367 CB CYS A 50 1438 1396 1384 51 -66 195 C ATOM 368 SG CYS A 50 69.413 16.445 -25.163 1.00 11.79 S ANISOU 368 SG CYS A 50 1396 1530 1553 63 228 101 S ATOM 369 N ALA A 51 64.823 17.177 -23.709 1.00 11.80 N ANISOU 369 N ALA A 51 1168 2011 1306 -11 -153 353 N ATOM 370 CA ALA A 51 63.614 17.963 -23.591 1.00 12.10 C ANISOU 370 CA ALA A 51 1282 1919 1397 19 -442 44 C ATOM 371 C ALA A 51 63.763 19.354 -24.186 1.00 15.70 C ANISOU 371 C ALA A 51 1594 2523 1848 367 -155 894 C ATOM 372 O ALA A 51 64.870 19.904 -24.161 1.00 14.99 O ANISOU 372 O ALA A 51 1723 1906 2066 329 -50 777 O ATOM 373 CB ALA A 51 63.178 18.102 -22.135 1.00 12.95 C ANISOU 373 CB ALA A 51 1333 1987 1601 -15 26 296 C ATOM 374 N LYS A 52 62.665 19.871 -24.761 1.00 22.62 N ANISOU 374 N LYS A 52 1857 3471 3266 692 -310 1588 N ATOM 375 CA LYS A 52 62.680 21.201 -25.328 1.00 28.85 C ANISOU 375 CA LYS A 52 2244 3924 4795 1048 -62 2565 C ATOM 376 C LYS A 52 62.816 22.273 -24.250 1.00 34.79 C ANISOU 376 C LYS A 52 3320 3212 6689 28 458 2008 C ATOM 377 O LYS A 52 63.406 23.299 -24.618 1.00 41.98 O ANISOU 377 O LYS A 52 4389 3798 7762 -408 -1059 3656 O ATOM 378 CB LYS A 52 61.409 21.414 -26.169 1.00 37.98 C ANISOU 378 CB LYS A 52 2732 4884 6816 1260 -968 3285 C ATOM 379 CG LYS A 52 61.164 20.317 -27.192 1.00 42.61 C ANISOU 379 CG LYS A 52 2108 5227 8856 -172 -2192 2777 C ATOM 380 CD LYS A 52 59.982 20.535 -28.130 1.00 44.71 C ANISOU 380 CD LYS A 52 1515 8251 7222 -342 -1020 4046 C ATOM 381 CE LYS A 52 59.401 19.180 -28.521 1.00 56.65 C ANISOU 381 CE LYS A 52 3658 9556 8312 985 -3418 11 C ATOM 382 NZ LYS A 52 58.664 19.221 -29.810 1.00 53.32 N ANISOU 382 NZ LYS A 52 7258 7680 5323 736 -1684 3057 N ATOM 383 N ALA A 53 62.352 22.102 -23.032 1.00 29.78 N ANISOU 383 N ALA A 53 2144 2714 6458 41 398 716 N ATOM 384 CA ALA A 53 62.313 23.010 -21.912 1.00 43.55 C ANISOU 384 CA ALA A 53 2081 6830 7637 1126 -2479 -1747 C ATOM 385 C ALA A 53 60.908 23.563 -21.561 1.00 65.86 C ANISOU 385 C ALA A 53 6844 6133 12047 5235 1796 428 C ATOM 386 O ALA A 53 60.814 24.560 -20.815 1.00 65.75 O ANISOU 386 O ALA A 53 2190 3250 19541 316 1131 -1095 O ATOM 387 CB ALA A 53 63.167 24.267 -22.010 1.00 64.60 C ANISOU 387 CB ALA A 53 6604 5644 12296 122 -6180 -1978 C TER 388 ALA A 53 END