ATOM 1 N ASN A 4 -10.562 2.879 -2.093 1.00 21.23 N ANISOU 1 N ASN A 4 2685 2760 2618 29 -43 203 N ATOM 2 CA ASN A 4 -9.148 2.626 -2.488 1.00 20.91 C ANISOU 2 CA ASN A 4 2696 2653 2596 25 -8 93 C ATOM 3 C ASN A 4 -8.222 2.549 -1.280 1.00 18.34 C ANISOU 3 C ASN A 4 2339 2342 2287 -3 -45 105 C ATOM 4 O ASN A 4 -7.159 3.192 -1.227 1.00 19.67 O ANISOU 4 O ASN A 4 2649 2501 2321 0 -31 210 O ATOM 5 CB ASN A 4 -8.652 3.691 -3.468 1.00 22.24 C ANISOU 5 CB ASN A 4 2847 2759 2842 0 0 54 C ATOM 6 CG ASN A 4 -7.526 3.179 -4.356 1.00 25.73 C ANISOU 6 CG ASN A 4 3242 3149 3384 -46 53 -98 C ATOM 7 OD1 ASN A 4 -7.599 2.060 -4.883 1.00 32.09 O ANISOU 7 OD1 ASN A 4 4149 3568 4475 -83 62 -135 O ATOM 8 ND2 ASN A 4 -6.480 3.993 -4.535 1.00 30.78 N ANISOU 8 ND2 ASN A 4 3884 3778 4030 -200 111 -52 N ATOM 9 N PHE A 5 -8.623 1.731 -0.317 1.00 14.19 N ANISOU 9 N PHE A 5 1817 1761 1811 22 -84 110 N ATOM 10 CA PHE A 5 -7.852 1.588 0.907 1.00 11.40 C ANISOU 10 CA PHE A 5 1398 1459 1472 27 -49 74 C ATOM 11 C PHE A 5 -7.729 0.122 1.289 1.00 9.91 C ANISOU 11 C PHE A 5 1176 1255 1332 87 -29 110 C ATOM 12 O PHE A 5 -6.625 -0.339 1.495 1.00 10.00 O ANISOU 12 O PHE A 5 977 1230 1592 89 161 51 O ATOM 13 CB PHE A 5 -8.500 2.419 2.014 1.00 11.18 C ANISOU 13 CB PHE A 5 1351 1408 1487 -9 -52 141 C ATOM 14 CG PHE A 5 -7.723 2.458 3.297 1.00 9.95 C ANISOU 14 CG PHE A 5 1143 1295 1340 9 -27 -1 C ATOM 15 CD1 PHE A 5 -6.719 3.392 3.488 1.00 13.05 C ANISOU 15 CD1 PHE A 5 1571 1769 1616 -86 -93 154 C ATOM 16 CD2 PHE A 5 -8.023 1.587 4.322 1.00 11.09 C ANISOU 16 CD2 PHE A 5 1399 1332 1480 -74 -164 0 C ATOM 17 CE1 PHE A 5 -6.043 3.433 4.682 1.00 13.57 C ANISOU 17 CE1 PHE A 5 1450 1844 1859 -454 -126 -18 C ATOM 18 CE2 PHE A 5 -7.323 1.622 5.517 1.00 11.00 C ANISOU 18 CE2 PHE A 5 1204 1495 1480 -7 -290 136 C ATOM 19 CZ PHE A 5 -6.346 2.540 5.699 1.00 12.63 C ANISOU 19 CZ PHE A 5 1502 1627 1668 50 -171 -11 C ATOM 20 N PHE A 6 -8.847 -0.592 1.373 1.00 8.29 N ANISOU 20 N PHE A 6 1017 1153 977 104 2 16 N ATOM 21 CA PHE A 6 -8.857 -1.981 1.831 1.00 8.05 C ANISOU 21 CA PHE A 6 976 1128 952 63 -56 27 C ATOM 22 C PHE A 6 -8.695 -2.994 0.702 1.00 7.91 C ANISOU 22 C PHE A 6 963 1094 948 81 -39 20 C ATOM 23 O PHE A 6 -9.135 -2.760 -0.421 1.00 9.35 O ANISOU 23 O PHE A 6 1202 1418 930 230 -177 35 O ATOM 24 CB PHE A 6 -10.159 -2.268 2.587 1.00 8.32 C ANISOU 24 CB PHE A 6 1038 1088 1035 75 52 64 C ATOM 25 CG PHE A 6 -10.358 -1.395 3.791 1.00 7.88 C ANISOU 25 CG PHE A 6 1030 1101 863 71 199 137 C ATOM 26 CD1 PHE A 6 -11.200 -0.301 3.766 1.00 8.45 C ANISOU 26 CD1 PHE A 6 1071 1357 780 105 10 17 C ATOM 27 CD2 PHE A 6 -9.661 -1.673 4.964 1.00 7.79 C ANISOU 27 CD2 PHE A 6 1116 1074 770 266 -8 -44 C ATOM 28 CE1 PHE A 6 -11.349 0.507 4.902 1.00 8.99 C ANISOU 28 CE1 PHE A 6 1224 1318 873 270 133 -36 C ATOM 29 CE2 PHE A 6 -9.789 -0.875 6.083 1.00 9.80 C ANISOU 29 CE2 PHE A 6 1453 1505 763 200 106 87 C ATOM 30 CZ PHE A 6 -10.635 0.216 6.058 1.00 9.94 C ANISOU 30 CZ PHE A 6 1501 1359 916 146 213 -19 C ATOM 31 N GLY A 7 -8.063 -4.123 0.992 1.00 7.42 N ANISOU 31 N GLY A 7 932 1059 829 7 -103 3 N ATOM 32 CA GLY A 7 -8.089 -5.261 0.103 1.00 7.71 C ANISOU 32 CA GLY A 7 959 1060 909 -88 -8 -12 C ATOM 33 C GLY A 7 -7.172 -5.213 -1.098 1.00 8.30 C ANISOU 33 C GLY A 7 1004 1213 937 -101 15 5 C ATOM 34 O GLY A 7 -7.349 -5.998 -2.014 1.00 9.67 O ANISOU 34 O GLY A 7 1190 1312 1171 -264 6 -145 O ATOM 35 N LYS A 8 -6.219 -4.286 -1.134 1.00 7.76 N ANISOU 35 N LYS A 8 1001 1095 853 -102 42 -75 N ATOM 36 CA LYS A 8 -5.291 -4.215 -2.279 1.00 8.59 C ANISOU 36 CA LYS A 8 1038 1241 982 -56 36 -51 C ATOM 37 C LYS A 8 -4.405 -5.456 -2.346 1.00 8.75 C ANISOU 37 C LYS A 8 1021 1250 1054 -136 50 -10 C ATOM 38 O LYS A 8 -4.125 -6.110 -1.346 1.00 9.74 O ANISOU 38 O LYS A 8 1226 1427 1045 46 -28 -164 O ATOM 39 CB LYS A 8 -4.411 -2.968 -2.210 1.00 8.97 C ANISOU 39 CB LYS A 8 1107 1289 1011 -59 126 -70 C ATOM 40 CG LYS A 8 -5.144 -1.648 -2.211 1.00 11.04 C ANISOU 40 CG LYS A 8 1399 1421 1374 -176 96 179 C ATOM 41 CD LYS A 8 -4.227 -0.426 -2.006 1.00 12.04 C ANISOU 41 CD LYS A 8 1414 1465 1693 -64 224 45 C ATOM 42 CE LYS A 8 -5.038 0.846 -1.972 1.00 13.26 C ANISOU 42 CE LYS A 8 1810 1753 1475 -98 99 107 C ATOM 43 NZ LYS A 8 -4.240 2.056 -1.775 1.00 15.66 N ANISOU 43 NZ LYS A 8 2457 1699 1792 -267 245 10 N ATOM 44 N THR A 9 -3.979 -5.779 -3.557 1.00 9.17 N ANISOU 44 N THR A 9 1037 1262 1183 -123 8 -183 N ATOM 45 CA THR A 9 -2.950 -6.781 -3.780 1.00 9.69 C ANISOU 45 CA THR A 9 1091 1309 1283 -77 25 -121 C ATOM 46 C THR A 9 -1.600 -6.139 -3.498 1.00 8.55 C ANISOU 46 C THR A 9 956 1180 1109 -77 22 -141 C ATOM 47 O THR A 9 -1.327 -5.005 -3.910 1.00 9.67 O ANISOU 47 O THR A 9 1028 1378 1267 -120 -82 113 O ATOM 48 CB THR A 9 -3.006 -7.275 -5.224 1.00 11.19 C ANISOU 48 CB THR A 9 1160 1535 1556 32 -59 -268 C ATOM 49 OG1 THR A 9 -4.285 -7.878 -5.454 1.00 13.59 O ANISOU 49 OG1 THR A 9 1270 1856 2035 -66 -144 -671 O ATOM 50 CG2 THR A 9 -1.967 -8.372 -5.492 1.00 13.35 C ANISOU 50 CG2 THR A 9 1560 1847 1662 73 -120 -291 C ATOM 51 N LEU A 10 -0.756 -6.860 -2.787 1.00 7.98 N ANISOU 51 N LEU A 10 911 1095 1025 -104 109 28 N ATOM 52 CA LEU A 10 0.609 -6.426 -2.554 1.00 7.45 C ANISOU 52 CA LEU A 10 938 997 893 -105 89 -121 C ATOM 53 C LEU A 10 1.337 -6.260 -3.898 1.00 7.55 C ANISOU 53 C LEU A 10 1006 959 901 -153 48 -94 C ATOM 54 O LEU A 10 1.376 -7.185 -4.698 1.00 9.05 O ANISOU 54 O LEU A 10 1160 1158 1120 -283 128 -84 O ATOM 55 CB LEU A 10 1.335 -7.445 -1.673 1.00 7.72 C ANISOU 55 CB LEU A 10 968 990 975 -109 34 -90 C ATOM 56 CG LEU A 10 2.806 -7.118 -1.392 1.00 8.39 C ANISOU 56 CG LEU A 10 1007 1113 1065 92 200 -26 C ATOM 57 CD1 LEU A 10 2.932 -5.895 -0.492 1.00 9.27 C ANISOU 57 CD1 LEU A 10 783 1321 1418 -53 -45 -56 C ATOM 58 CD2 LEU A 10 3.533 -8.317 -0.765 1.00 10.14 C ANISOU 58 CD2 LEU A 10 1382 1154 1313 87 43 12 C ATOM 59 N ALA A 11 1.879 -5.065 -4.122 1.00 7.84 N ANISOU 59 N ALA A 11 1051 1089 838 -130 93 -52 N ATOM 60 CA ALA A 11 2.469 -4.725 -5.417 1.00 8.28 C ANISOU 60 CA ALA A 11 1074 1061 1011 -108 135 -76 C ATOM 61 C ALA A 11 3.438 -3.572 -5.242 1.00 8.51 C ANISOU 61 C ALA A 11 986 1128 1119 -179 139 3 C ATOM 62 O ALA A 11 3.318 -2.818 -4.301 1.00 9.00 O ANISOU 62 O ALA A 11 1155 1104 1160 -181 335 -185 O ATOM 63 CB ALA A 11 1.380 -4.332 -6.386 1.00 9.48 C ANISOU 63 CB ALA A 11 1199 1285 1116 -149 156 8 C ATOM 64 N ALA A 12 4.352 -3.422 -6.198 1.00 8.20 N ANISOU 64 N ALA A 12 1082 1068 965 -192 222 -198 N ATOM 65 CA ALA A 12 5.306 -2.332 -6.213 1.00 8.81 C ANISOU 65 CA ALA A 12 1119 1112 1115 -131 130 12 C ATOM 66 C ALA A 12 5.339 -1.681 -7.570 1.00 9.25 C ANISOU 66 C ALA A 12 1245 1186 1083 -216 201 -39 C ATOM 67 O ALA A 12 5.260 -2.357 -8.590 1.00 10.96 O ANISOU 67 O ALA A 12 1660 1304 1197 -363 312 -197 O ATOM 68 CB ALA A 12 6.671 -2.815 -5.875 1.00 10.31 C ANISOU 68 CB ALA A 12 1255 1234 1428 -200 75 50 C ATOM 69 N ARG A 13 5.485 -0.364 -7.592 1.00 8.97 N ANISOU 69 N ARG A 13 1273 1201 933 -237 172 2 N ATOM 70 CA ARG A 13 5.676 0.418 -8.813 1.00 9.11 C ANISOU 70 CA ARG A 13 1262 1226 972 -211 150 58 C ATOM 71 C ARG A 13 6.892 1.317 -8.615 1.00 9.52 C ANISOU 71 C ARG A 13 1390 1135 1090 -284 70 -37 C ATOM 72 O ARG A 13 6.989 2.045 -7.643 1.00 9.85 O ANISOU 72 O ARG A 13 1414 1369 957 -532 25 -113 O ATOM 73 CB ARG A 13 4.457 1.290 -9.060 1.00 10.48 C ANISOU 73 CB ARG A 13 1384 1429 1168 -270 67 220 C ATOM 74 CG ARG A 13 3.238 0.508 -9.508 1.00 12.18 C ANISOU 74 CG ARG A 13 1531 1638 1458 -204 16 168 C ATOM 75 CD ARG A 13 2.015 1.353 -9.643 1.00 14.73 C ANISOU 75 CD ARG A 13 1791 1875 1929 -121 -78 308 C ATOM 76 NE ARG A 13 1.634 2.008 -8.402 1.00 16.01 N ANISOU 76 NE ARG A 13 1839 1973 2268 -220 -120 321 N ATOM 77 CZ ARG A 13 0.960 1.437 -7.410 1.00 14.89 C ANISOU 77 CZ ARG A 13 1873 1897 1886 -130 -126 388 C ATOM 78 NH1 ARG A 13 0.557 0.185 -7.522 1.00 14.28 N ANISOU 78 NH1 ARG A 13 1802 1823 1801 -289 -229 382 N ATOM 79 NH2 ARG A 13 0.651 2.127 -6.317 1.00 14.70 N ANISOU 79 NH2 ARG A 13 1714 1615 2253 -326 -200 419 N ATOM 80 N PRO A 14 7.828 1.297 -9.541 1.00 9.59 N ANISOU 80 N PRO A 14 1330 1217 1096 -191 50 -93 N ATOM 81 CA PRO A 14 8.881 2.305 -9.530 1.00 9.94 C ANISOU 81 CA PRO A 14 1348 1231 1195 -132 -6 -31 C ATOM 82 C PRO A 14 8.327 3.694 -9.769 1.00 10.01 C ANISOU 82 C PRO A 14 1294 1273 1235 -108 3 -12 C ATOM 83 O PRO A 14 7.314 3.897 -10.422 1.00 11.97 O ANISOU 83 O PRO A 14 1559 1341 1647 -261 -249 111 O ATOM 84 CB PRO A 14 9.795 1.876 -10.680 1.00 10.74 C ANISOU 84 CB PRO A 14 1316 1337 1426 -135 17 -53 C ATOM 85 CG PRO A 14 9.412 0.505 -11.011 1.00 13.80 C ANISOU 85 CG PRO A 14 1657 1774 1811 -59 85 -188 C ATOM 86 CD PRO A 14 8.001 0.334 -10.633 1.00 11.62 C ANISOU 86 CD PRO A 14 1504 1472 1439 -218 189 -150 C ATOM 87 N VAL A 15 9.024 4.678 -9.231 1.00 10.07 N ANISOU 87 N VAL A 15 1277 1204 1343 -138 -81 -42 N ATOM 88 CA VAL A 15 8.722 6.076 -9.472 1.00 10.27 C ANISOU 88 CA VAL A 15 1267 1269 1364 -24 -30 9 C ATOM 89 C VAL A 15 9.729 6.495 -10.533 1.00 10.19 C ANISOU 89 C VAL A 15 1367 1164 1340 -68 -23 -74 C ATOM 90 O VAL A 15 10.921 6.620 -10.254 1.00 10.06 O ANISOU 90 O VAL A 15 1230 1063 1530 -43 143 -75 O ATOM 91 CB VAL A 15 8.868 6.881 -8.194 1.00 10.73 C ANISOU 91 CB VAL A 15 1297 1326 1453 -9 -67 29 C ATOM 92 CG1 VAL A 15 8.689 8.364 -8.461 1.00 11.38 C ANISOU 92 CG1 VAL A 15 1450 1369 1502 106 -50 -134 C ATOM 93 CG2 VAL A 15 7.863 6.394 -7.180 1.00 12.77 C ANISOU 93 CG2 VAL A 15 1665 1587 1600 116 2 -94 C ATOM 94 N AGLU A 16 9.261 6.690 -11.756 0.70 11.47 N ANISOU 94 N AGLU A 16 1498 1366 1492 -100 -16 -95 N ATOM 95 CA AGLU A 16 10.176 6.898 -12.869 0.70 12.62 C ANISOU 95 CA AGLU A 16 1680 1542 1572 -94 -17 -65 C ATOM 96 C AGLU A 16 11.047 8.161 -12.755 0.70 11.82 C ANISOU 96 C AGLU A 16 1559 1481 1449 -101 8 -46 C ATOM 97 O AGLU A 16 12.170 8.176 -13.240 0.70 12.34 O ANISOU 97 O AGLU A 16 1657 1527 1502 -90 140 -157 O ATOM 98 CB AGLU A 16 9.409 6.864 -14.198 0.70 13.47 C ANISOU 98 CB AGLU A 16 1810 1657 1648 -105 -32 -111 C ATOM 99 CG AGLU A 16 8.725 5.519 -14.456 0.70 17.31 C ANISOU 99 CG AGLU A 16 2154 2106 2316 -83 -88 -22 C ATOM 100 CD AGLU A 16 7.582 5.584 -15.462 0.70 22.44 C ANISOU 100 CD AGLU A 16 2736 2756 3035 71 -80 -116 C ATOM 101 OE1AGLU A 16 7.554 4.717 -16.361 0.70 24.93 O ANISOU 101 OE1AGLU A 16 2992 3109 3368 -67 -71 -197 O ATOM 102 OE2AGLU A 16 6.705 6.482 -15.347 0.70 26.19 O ANISOU 102 OE2AGLU A 16 3061 3280 3610 233 -105 -101 O ATOM 103 N ALA A 17 10.543 9.199 -12.094 1.00 10.68 N ANISOU 103 N ALA A 17 1445 1294 1318 -69 -45 -1 N ATOM 104 CA ALA A 17 11.290 10.449 -11.953 1.00 10.21 C ANISOU 104 CA ALA A 17 1325 1278 1273 -63 -22 11 C ATOM 105 C ALA A 17 12.441 10.354 -10.942 1.00 9.14 C ANISOU 105 C ALA A 17 1273 1101 1097 -44 -48 51 C ATOM 106 O ALA A 17 13.372 11.172 -10.986 1.00 8.56 O ANISOU 106 O ALA A 17 1282 976 993 -133 -43 171 O ATOM 107 CB ALA A 17 10.345 11.589 -11.588 1.00 11.79 C ANISOU 107 CB ALA A 17 1407 1397 1676 2 -181 43 C ATOM 108 N ILE A 18 12.391 9.362 -10.048 1.00 8.20 N ANISOU 108 N ILE A 18 1175 955 984 -101 10 76 N ATOM 109 CA ILE A 18 13.370 9.235 -8.967 1.00 7.94 C ANISOU 109 CA ILE A 18 1054 977 985 -35 76 45 C ATOM 110 C ILE A 18 13.889 7.798 -8.919 1.00 7.82 C ANISOU 110 C ILE A 18 1027 938 1005 -57 143 97 C ATOM 111 O ILE A 18 13.306 6.937 -8.255 1.00 7.68 O ANISOU 111 O ILE A 18 1137 905 874 -101 210 60 O ATOM 112 CB ILE A 18 12.783 9.671 -7.630 1.00 8.47 C ANISOU 112 CB ILE A 18 1086 1037 1093 47 20 71 C ATOM 113 CG1 ILE A 18 12.213 11.098 -7.726 1.00 8.96 C ANISOU 113 CG1 ILE A 18 1056 1182 1165 69 149 23 C ATOM 114 CG2 ILE A 18 13.864 9.591 -6.566 1.00 8.01 C ANISOU 114 CG2 ILE A 18 1067 1052 922 27 114 -64 C ATOM 115 CD1 ILE A 18 11.639 11.639 -6.427 1.00 10.03 C ANISOU 115 CD1 ILE A 18 1260 1117 1432 203 85 -45 C ATOM 116 N PRO A 19 14.978 7.528 -9.634 1.00 7.87 N ANISOU 116 N PRO A 19 1113 898 976 -61 196 84 N ATOM 117 CA PRO A 19 15.533 6.177 -9.698 1.00 8.65 C ANISOU 117 CA PRO A 19 1174 1053 1058 1 155 57 C ATOM 118 C PRO A 19 15.723 5.568 -8.322 1.00 8.15 C ANISOU 118 C PRO A 19 1139 944 1010 -11 110 27 C ATOM 119 O PRO A 19 16.201 6.215 -7.404 1.00 8.28 O ANISOU 119 O PRO A 19 1175 976 996 -129 271 51 O ATOM 120 CB PRO A 19 16.870 6.389 -10.395 1.00 9.70 C ANISOU 120 CB PRO A 19 1241 1252 1192 42 153 63 C ATOM 121 CG PRO A 19 16.606 7.531 -11.305 1.00 9.92 C ANISOU 121 CG PRO A 19 1254 1197 1316 13 163 30 C ATOM 122 CD PRO A 19 15.698 8.463 -10.522 1.00 7.92 C ANISOU 122 CD PRO A 19 1196 947 864 -26 172 66 C ATOM 123 N GLY A 20 15.306 4.309 -8.179 1.00 7.13 N ANISOU 123 N GLY A 20 1037 781 889 -30 100 7 N ATOM 124 CA GLY A 20 15.428 3.591 -6.926 1.00 7.37 C ANISOU 124 CA GLY A 20 990 857 953 50 87 78 C ATOM 125 C GLY A 20 14.229 3.674 -6.008 1.00 7.04 C ANISOU 125 C GLY A 20 967 792 914 35 142 52 C ATOM 126 O GLY A 20 14.056 2.851 -5.110 1.00 8.42 O ANISOU 126 O GLY A 20 1144 1012 1042 132 299 374 O ATOM 127 N BMET A 21 13.410 4.704 -6.158 0.60 6.49 N ANISOU 127 N BMET A 21 835 826 803 -23 64 148 N ATOM 128 CA BMET A 21 12.214 4.778 -5.341 0.60 6.26 C ANISOU 128 CA BMET A 21 847 828 702 6 43 31 C ATOM 129 C BMET A 21 11.180 3.772 -5.786 0.60 6.12 C ANISOU 129 C BMET A 21 799 763 762 -35 -13 49 C ATOM 130 O BMET A 21 11.044 3.469 -6.976 0.60 7.31 O ANISOU 130 O BMET A 21 945 1052 780 -15 83 -244 O ATOM 131 CB BMET A 21 11.607 6.167 -5.400 0.60 5.92 C ANISOU 131 CB BMET A 21 929 763 557 50 11 -89 C ATOM 132 CG BMET A 21 10.311 6.342 -4.680 0.60 8.15 C ANISOU 132 CG BMET A 21 944 915 1237 -72 -135 218 C ATOM 133 SD BMET A 21 9.829 8.097 -4.707 0.60 10.11 S ANISOU 133 SD BMET A 21 1012 1189 1639 -38 83 -155 S ATOM 134 CE BMET A 21 11.246 8.867 -4.171 0.60 4.87 C ANISOU 134 CE BMET A 21 618 301 931 68 -116 -172 C ATOM 135 N LEU A 22 10.465 3.233 -4.827 1.00 6.33 N ANISOU 135 N LEU A 22 830 783 791 -22 -24 -14 N ATOM 136 CA LEU A 22 9.368 2.301 -5.071 1.00 6.92 C ANISOU 136 CA LEU A 22 865 860 902 -38 -32 -26 C ATOM 137 C LEU A 22 8.169 2.664 -4.247 1.00 6.94 C ANISOU 137 C LEU A 22 849 1013 773 -38 -17 16 C ATOM 138 O LEU A 22 8.302 2.990 -3.071 1.00 8.95 O ANISOU 138 O LEU A 22 893 1638 869 -72 -99 -70 O ATOM 139 CB LEU A 22 9.766 0.862 -4.686 1.00 7.93 C ANISOU 139 CB LEU A 22 947 978 1088 -56 -20 3 C ATOM 140 CG LEU A 22 10.982 0.302 -5.401 1.00 10.32 C ANISOU 140 CG LEU A 22 1297 1086 1535 59 53 92 C ATOM 141 CD1 LEU A 22 11.563 -0.871 -4.624 1.00 12.68 C ANISOU 141 CD1 LEU A 22 1507 1565 1744 188 134 217 C ATOM 142 CD2 LEU A 22 10.591 -0.112 -6.797 1.00 13.51 C ANISOU 142 CD2 LEU A 22 1771 1582 1779 137 254 20 C ATOM 143 N GLU A 23 6.996 2.606 -4.854 1.00 6.42 N ANISOU 143 N GLU A 23 775 941 723 -100 63 -12 N ATOM 144 CA GLU A 23 5.743 2.752 -4.133 1.00 7.19 C ANISOU 144 CA GLU A 23 912 914 902 -69 63 -16 C ATOM 145 C GLU A 23 5.063 1.397 -4.027 1.00 6.88 C ANISOU 145 C GLU A 23 944 865 804 -144 45 -26 C ATOM 146 O GLU A 23 4.948 0.706 -5.019 1.00 8.42 O ANISOU 146 O GLU A 23 1277 1102 818 -321 216 -116 O ATOM 147 CB GLU A 23 4.843 3.750 -4.878 1.00 8.51 C ANISOU 147 CB GLU A 23 920 1142 1171 -20 26 43 C ATOM 148 CG GLU A 23 3.471 3.981 -4.275 1.00 10.50 C ANISOU 148 CG GLU A 23 1268 1238 1482 11 3 143 C ATOM 149 CD GLU A 23 2.725 5.073 -4.996 1.00 12.91 C ANISOU 149 CD GLU A 23 1605 1532 1765 -42 -235 165 C ATOM 150 OE1 GLU A 23 3.100 6.214 -4.837 1.00 14.30 O ANISOU 150 OE1 GLU A 23 1880 1256 2296 -134 -201 350 O ATOM 151 OE2 GLU A 23 1.758 4.785 -5.709 1.00 15.49 O ANISOU 151 OE2 GLU A 23 1884 1389 2613 -211 -550 467 O ATOM 152 N PHE A 24 4.660 1.021 -2.823 1.00 6.87 N ANISOU 152 N PHE A 24 971 812 827 -118 73 -56 N ATOM 153 CA PHE A 24 3.989 -0.236 -2.575 1.00 6.74 C ANISOU 153 CA PHE A 24 853 829 876 -101 72 -58 C ATOM 154 C PHE A 24 2.535 -0.053 -2.210 1.00 6.51 C ANISOU 154 C PHE A 24 837 792 842 -68 132 -66 C ATOM 155 O PHE A 24 2.182 0.778 -1.380 1.00 8.09 O ANISOU 155 O PHE A 24 1017 1049 1007 -199 242 -223 O ATOM 156 CB PHE A 24 4.636 -1.020 -1.441 1.00 7.49 C ANISOU 156 CB PHE A 24 961 860 1023 -45 128 -15 C ATOM 157 CG PHE A 24 6.046 -1.439 -1.703 1.00 8.61 C ANISOU 157 CG PHE A 24 1111 1118 1040 -81 78 133 C ATOM 158 CD1 PHE A 24 7.085 -0.568 -1.493 1.00 9.30 C ANISOU 158 CD1 PHE A 24 1170 1338 1023 -145 62 332 C ATOM 159 CD2 PHE A 24 6.326 -2.695 -2.213 1.00 11.18 C ANISOU 159 CD2 PHE A 24 976 1701 1569 -1 13 -247 C ATOM 160 CE1 PHE A 24 8.377 -0.937 -1.729 1.00 10.68 C ANISOU 160 CE1 PHE A 24 1170 1630 1255 -231 -161 343 C ATOM 161 CE2 PHE A 24 7.671 -3.057 -2.464 1.00 13.01 C ANISOU 161 CE2 PHE A 24 1527 1760 1655 197 -47 -207 C ATOM 162 CZ PHE A 24 8.667 -2.153 -2.229 1.00 11.58 C ANISOU 162 CZ PHE A 24 1067 2145 1185 94 68 143 C ATOM 163 N ASP A 25 1.688 -0.874 -2.801 1.00 6.73 N ANISOU 163 N ASP A 25 839 905 811 -164 128 -22 N ATOM 164 CA ASP A 25 0.347 -1.119 -2.279 1.00 6.41 C ANISOU 164 CA ASP A 25 752 870 811 -40 55 19 C ATOM 165 C ASP A 25 0.417 -2.215 -1.225 1.00 5.72 C ANISOU 165 C ASP A 25 684 709 780 17 81 5 C ATOM 166 O ASP A 25 1.004 -3.287 -1.477 1.00 7.15 O ANISOU 166 O ASP A 25 879 933 903 105 125 -66 O ATOM 167 CB ASP A 25 -0.578 -1.595 -3.381 1.00 7.01 C ANISOU 167 CB ASP A 25 936 921 804 -130 33 63 C ATOM 168 CG ASP A 25 -0.852 -0.572 -4.429 1.00 9.34 C ANISOU 168 CG ASP A 25 1261 1159 1128 -215 -222 -26 C ATOM 169 OD1 ASP A 25 -0.728 0.646 -4.194 1.00 12.28 O ANISOU 169 OD1 ASP A 25 2053 1295 1317 -186 -435 239 O ATOM 170 OD2 ASP A 25 -1.207 -0.942 -5.563 1.00 11.89 O ANISOU 170 OD2 ASP A 25 1913 1302 1302 -401 -398 122 O ATOM 171 N ILE A 26 -0.160 -1.943 -0.062 1.00 5.55 N ANISOU 171 N ILE A 26 693 665 751 44 54 51 N ATOM 172 CA ILE A 26 -0.155 -2.843 1.071 1.00 5.04 C ANISOU 172 CA ILE A 26 649 605 661 65 27 44 C ATOM 173 C ILE A 26 -1.567 -3.338 1.317 1.00 5.12 C ANISOU 173 C ILE A 26 606 632 705 50 92 59 C ATOM 174 O ILE A 26 -2.490 -2.516 1.452 1.00 5.90 O ANISOU 174 O ILE A 26 719 714 808 70 123 127 O ATOM 175 CB ILE A 26 0.367 -2.124 2.326 1.00 5.57 C ANISOU 175 CB ILE A 26 741 612 761 27 41 12 C ATOM 176 CG1 ILE A 26 1.759 -1.534 2.118 1.00 7.09 C ANISOU 176 CG1 ILE A 26 1025 949 716 -68 78 -174 C ATOM 177 CG2 ILE A 26 0.305 -3.012 3.541 1.00 6.75 C ANISOU 177 CG2 ILE A 26 907 884 770 140 89 -15 C ATOM 178 CD1 ILE A 26 2.856 -2.567 1.826 1.00 8.89 C ANISOU 178 CD1 ILE A 26 952 1157 1266 -106 106 -59 C ATOM 179 N PRO A 27 -1.755 -4.647 1.406 1.00 5.51 N ANISOU 179 N PRO A 27 674 647 771 43 89 15 N ATOM 180 CA PRO A 27 -3.079 -5.172 1.759 1.00 5.27 C ANISOU 180 CA PRO A 27 607 668 726 62 62 10 C ATOM 181 C PRO A 27 -3.476 -4.808 3.183 1.00 4.78 C ANISOU 181 C PRO A 27 608 635 572 118 32 104 C ATOM 182 O PRO A 27 -2.747 -5.101 4.121 1.00 6.02 O ANISOU 182 O PRO A 27 735 909 644 231 -90 4 O ATOM 183 CB PRO A 27 -2.928 -6.697 1.578 1.00 5.38 C ANISOU 183 CB PRO A 27 634 680 730 4 -7 38 C ATOM 184 CG PRO A 27 -1.734 -6.859 0.704 1.00 6.69 C ANISOU 184 CG PRO A 27 825 785 932 34 22 -32 C ATOM 185 CD PRO A 27 -0.809 -5.738 1.092 1.00 6.88 C ANISOU 185 CD PRO A 27 840 750 1021 0 177 -12 C ATOM 186 N VAL A 28 -4.618 -4.144 3.310 1.00 4.98 N ANISOU 186 N VAL A 28 624 648 618 68 -39 83 N ATOM 187 CA VAL A 28 -5.202 -3.801 4.608 1.00 5.22 C ANISOU 187 CA VAL A 28 625 744 613 75 -36 54 C ATOM 188 C VAL A 28 -6.585 -4.427 4.671 1.00 5.54 C ANISOU 188 C VAL A 28 706 785 612 109 -38 -2 C ATOM 189 O VAL A 28 -7.405 -4.241 3.769 1.00 6.60 O ANISOU 189 O VAL A 28 730 990 787 97 -170 44 O ATOM 190 CB VAL A 28 -5.312 -2.278 4.779 1.00 5.41 C ANISOU 190 CB VAL A 28 668 772 615 -2 -41 -10 C ATOM 191 CG1 VAL A 28 -5.908 -1.931 6.130 1.00 6.71 C ANISOU 191 CG1 VAL A 28 861 926 763 -6 47 -111 C ATOM 192 CG2 VAL A 28 -3.959 -1.591 4.579 1.00 6.00 C ANISOU 192 CG2 VAL A 28 777 715 785 81 97 -38 C ATOM 193 N HIS A 29 -6.817 -5.209 5.707 1.00 5.31 N ANISOU 193 N HIS A 29 608 740 670 -93 21 -34 N ATOM 194 CA HIS A 29 -8.027 -6.005 5.829 1.00 5.58 C ANISOU 194 CA HIS A 29 719 759 643 -88 -53 -84 C ATOM 195 C HIS A 29 -8.863 -5.560 6.986 1.00 5.51 C ANISOU 195 C HIS A 29 655 765 671 -38 -70 -56 C ATOM 196 O HIS A 29 -8.384 -5.576 8.105 1.00 5.45 O ANISOU 196 O HIS A 29 833 798 436 -57 -63 -123 O ATOM 197 CB HIS A 29 -7.639 -7.461 6.002 1.00 6.89 C ANISOU 197 CB HIS A 29 844 855 918 -2 156 -122 C ATOM 198 CG HIS A 29 -6.823 -8.007 4.878 1.00 9.27 C ANISOU 198 CG HIS A 29 1494 924 1103 -80 176 -40 C ATOM 199 ND1 HIS A 29 -7.301 -8.063 3.594 1.00 11.67 N ANISOU 199 ND1 HIS A 29 2238 967 1226 -8 487 -203 N ATOM 200 CD2 HIS A 29 -5.560 -8.476 4.834 1.00 11.81 C ANISOU 200 CD2 HIS A 29 1843 1285 1357 22 387 -177 C ATOM 201 CE1 HIS A 29 -6.369 -8.560 2.803 1.00 10.50 C ANISOU 201 CE1 HIS A 29 1883 1071 1036 329 721 -395 C ATOM 202 NE2 HIS A 29 -5.295 -8.805 3.527 1.00 11.78 N ANISOU 202 NE2 HIS A 29 1914 1158 1401 11 691 -295 N ATOM 203 N GLY A 30 -10.114 -5.201 6.719 1.00 6.56 N ANISOU 203 N GLY A 30 896 1005 589 65 -36 -164 N ATOM 204 CA GLY A 30 -11.060 -4.741 7.718 1.00 6.66 C ANISOU 204 CA GLY A 30 847 995 687 -29 -42 -98 C ATOM 205 C GLY A 30 -11.916 -3.621 7.182 1.00 7.30 C ANISOU 205 C GLY A 30 977 1070 727 -11 -56 -145 C ATOM 206 O GLY A 30 -12.303 -3.623 6.013 1.00 8.83 O ANISOU 206 O GLY A 30 1217 1430 708 153 -238 -122 O ATOM 207 N ASP A 31 -12.235 -2.667 8.046 1.00 8.00 N ANISOU 207 N ASP A 31 1065 1144 830 0 -102 -93 N ATOM 208 CA ASP A 31 -13.041 -1.520 7.693 1.00 8.59 C ANISOU 208 CA ASP A 31 1221 1136 904 -39 -50 -33 C ATOM 209 C ASP A 31 -12.746 -0.385 8.652 1.00 8.34 C ANISOU 209 C ASP A 31 1201 1175 791 -27 -44 -47 C ATOM 210 O ASP A 31 -11.754 -0.456 9.370 1.00 9.26 O ANISOU 210 O ASP A 31 1242 1356 918 -273 10 -45 O ATOM 211 CB ASP A 31 -14.535 -1.873 7.590 1.00 8.72 C ANISOU 211 CB ASP A 31 1218 1139 954 17 -20 -81 C ATOM 212 CG ASP A 31 -15.149 -2.426 8.862 1.00 10.28 C ANISOU 212 CG ASP A 31 1382 1305 1216 -275 -211 -70 C ATOM 213 OD1 ASP A 31 -14.882 -1.963 9.983 1.00 9.62 O ANISOU 213 OD1 ASP A 31 1522 1248 886 -301 -169 35 O ATOM 214 OD2 ASP A 31 -16.026 -3.318 8.803 1.00 14.79 O ANISOU 214 OD2 ASP A 31 2162 1889 1567 -544 246 -405 O ATOM 215 N ASN A 32 -13.592 0.643 8.674 1.00 8.92 N ANISOU 215 N ASN A 32 1401 1136 851 -88 -51 19 N ATOM 216 CA ASN A 32 -13.396 1.809 9.541 1.00 10.07 C ANISOU 216 CA ASN A 32 1510 1202 1113 -23 -64 2 C ATOM 217 C ASN A 32 -13.260 1.463 11.025 1.00 9.12 C ANISOU 217 C ASN A 32 1405 1139 921 -57 -11 23 C ATOM 218 O ASN A 32 -12.657 2.215 11.798 1.00 10.53 O ANISOU 218 O ASN A 32 1682 1264 1055 -180 -81 84 O ATOM 219 CB ASN A 32 -14.557 2.800 9.385 1.00 10.55 C ANISOU 219 CB ASN A 32 1579 1223 1205 44 -70 -1 C ATOM 220 CG ASN A 32 -15.837 2.274 10.010 1.00 12.72 C ANISOU 220 CG ASN A 32 1816 1443 1573 143 -131 -25 C ATOM 221 OD1 ASN A 32 -16.459 1.327 9.493 1.00 13.18 O ANISOU 221 OD1 ASN A 32 1554 1439 2012 97 -548 73 O ATOM 222 ND2 ASN A 32 -16.233 2.863 11.138 1.00 12.93 N ANISOU 222 ND2 ASN A 32 1968 1120 1825 662 -106 -38 N ATOM 223 N ARG A 33 -13.845 0.346 11.437 1.00 7.59 N ANISOU 223 N ARG A 33 1137 930 815 23 -105 44 N ATOM 224 CA ARG A 33 -13.831 -0.064 12.846 1.00 6.98 C ANISOU 224 CA ARG A 33 1016 888 749 42 -77 21 C ATOM 225 C ARG A 33 -12.522 -0.692 13.295 1.00 7.00 C ANISOU 225 C ARG A 33 923 989 747 134 -10 -99 C ATOM 226 O ARG A 33 -12.253 -0.793 14.499 1.00 7.42 O ANISOU 226 O ARG A 33 1027 1058 734 141 -58 -198 O ATOM 227 CB ARG A 33 -14.957 -1.055 13.103 1.00 5.77 C ANISOU 227 CB ARG A 33 808 722 660 101 -148 21 C ATOM 228 CG ARG A 33 -16.320 -0.457 12.893 1.00 7.17 C ANISOU 228 CG ARG A 33 971 825 926 100 -93 109 C ATOM 229 CD ARG A 33 -17.408 -1.484 12.932 1.00 7.56 C ANISOU 229 CD ARG A 33 821 908 1143 135 -235 43 C ATOM 230 NE ARG A 33 -17.386 -2.320 11.753 1.00 8.38 N ANISOU 230 NE ARG A 33 891 909 1381 266 -214 66 N ATOM 231 CZ ARG A 33 -18.286 -3.252 11.480 1.00 10.15 C ANISOU 231 CZ ARG A 33 1116 1308 1430 122 -203 73 C ATOM 232 NH1 ARG A 33 -19.287 -3.486 12.313 1.00 12.02 N ANISOU 232 NH1 ARG A 33 1509 1307 1751 288 -161 73 N ATOM 233 NH2 ARG A 33 -18.174 -3.953 10.371 1.00 11.53 N ANISOU 233 NH2 ARG A 33 1320 1321 1740 -174 -192 -93 N ATOM 234 N GLY A 34 -11.709 -1.141 12.349 1.00 6.78 N ANISOU 234 N GLY A 34 754 1121 699 83 -137 -181 N ATOM 235 CA GLY A 34 -10.478 -1.814 12.695 1.00 7.42 C ANISOU 235 CA GLY A 34 818 1197 802 135 -121 -180 C ATOM 236 C GLY A 34 -9.965 -2.643 11.538 1.00 6.79 C ANISOU 236 C GLY A 34 791 1073 714 71 -155 -240 C ATOM 237 O GLY A 34 -10.731 -3.122 10.696 1.00 8.25 O ANISOU 237 O GLY A 34 794 1631 708 2 -280 -287 O ATOM 238 N TRP A 35 -8.657 -2.827 11.499 1.00 5.32 N ANISOU 238 N TRP A 35 581 819 621 -2 -110 -173 N ATOM 239 CA TRP A 35 -8.028 -3.558 10.407 1.00 4.57 C ANISOU 239 CA TRP A 35 575 626 533 11 -64 -111 C ATOM 240 C TRP A 35 -6.669 -4.088 10.781 1.00 4.51 C ANISOU 240 C TRP A 35 552 667 492 0 -23 -114 C ATOM 241 O TRP A 35 -6.147 -3.813 11.860 1.00 5.48 O ANISOU 241 O TRP A 35 709 817 554 -43 -158 -148 O ATOM 242 CB TRP A 35 -7.968 -2.668 9.147 1.00 4.58 C ANISOU 242 CB TRP A 35 534 651 555 34 -75 -156 C ATOM 243 CG TRP A 35 -7.477 -1.251 9.359 1.00 4.95 C ANISOU 243 CG TRP A 35 609 584 687 -36 -82 -73 C ATOM 244 CD1 TRP A 35 -8.258 -0.112 9.371 1.00 6.84 C ANISOU 244 CD1 TRP A 35 974 757 865 -140 -92 -110 C ATOM 245 CD2 TRP A 35 -6.131 -0.809 9.551 1.00 5.84 C ANISOU 245 CD2 TRP A 35 1036 707 475 -99 81 -218 C ATOM 246 NE1 TRP A 35 -7.474 0.996 9.572 1.00 7.36 N ANISOU 246 NE1 TRP A 35 1208 643 945 43 -139 -74 N ATOM 247 CE2 TRP A 35 -6.167 0.597 9.682 1.00 6.54 C ANISOU 247 CE2 TRP A 35 875 621 987 -182 -154 -126 C ATOM 248 CE3 TRP A 35 -4.896 -1.446 9.675 1.00 6.48 C ANISOU 248 CE3 TRP A 35 780 785 894 -110 -18 -203 C ATOM 249 CZ2 TRP A 35 -5.011 1.356 9.914 1.00 7.47 C ANISOU 249 CZ2 TRP A 35 1061 884 893 -243 -4 -25 C ATOM 250 CZ3 TRP A 35 -3.762 -0.679 9.886 1.00 7.38 C ANISOU 250 CZ3 TRP A 35 961 1013 828 -66 37 -167 C ATOM 251 CH2 TRP A 35 -3.836 0.697 10.011 1.00 7.54 C ANISOU 251 CH2 TRP A 35 974 1148 741 -384 94 -72 C ATOM 252 N BPHE A 36 -6.076 -4.843 9.879 0.70 4.69 N ANISOU 252 N BPHE A 36 560 700 519 51 -34 -148 N ATOM 253 CA BPHE A 36 -4.725 -5.344 10.081 0.70 5.55 C ANISOU 253 CA BPHE A 36 612 777 719 29 -24 31 C ATOM 254 C BPHE A 36 -4.018 -5.411 8.742 0.70 5.63 C ANISOU 254 C BPHE A 36 703 766 668 47 -51 -34 C ATOM 255 O BPHE A 36 -4.641 -5.563 7.687 0.70 5.40 O ANISOU 255 O BPHE A 36 700 819 531 69 -53 -62 O ATOM 256 CB BPHE A 36 -4.697 -6.705 10.775 0.70 7.54 C ANISOU 256 CB BPHE A 36 877 985 1002 118 -24 -50 C ATOM 257 CG BPHE A 36 -5.466 -7.766 10.076 0.70 9.71 C ANISOU 257 CG BPHE A 36 1237 1259 1193 128 -7 -1 C ATOM 258 CD1BPHE A 36 -4.870 -8.551 9.087 0.70 13.11 C ANISOU 258 CD1BPHE A 36 1841 1560 1581 4 48 -1 C ATOM 259 CD2BPHE A 36 -6.787 -8.015 10.419 0.70 10.06 C ANISOU 259 CD2BPHE A 36 1267 1142 1412 -180 -166 -35 C ATOM 260 CE1BPHE A 36 -5.592 -9.568 8.457 0.70 13.33 C ANISOU 260 CE1BPHE A 36 2068 1556 1441 -76 52 33 C ATOM 261 CE2BPHE A 36 -7.511 -9.018 9.776 0.70 10.70 C ANISOU 261 CE2BPHE A 36 1478 1232 1352 -282 16 -63 C ATOM 262 CZ BPHE A 36 -6.903 -9.792 8.795 0.70 11.90 C ANISOU 262 CZ BPHE A 36 1757 1347 1415 -52 -55 -137 C ATOM 263 N LYS A 37 -2.696 -5.299 8.810 1.00 5.11 N ANISOU 263 N LYS A 37 583 745 611 87 -97 -67 N ATOM 264 CA LYS A 37 -1.836 -5.386 7.639 1.00 4.72 C ANISOU 264 CA LYS A 37 510 634 649 17 -22 -3 C ATOM 265 C LYS A 37 -0.497 -5.994 7.987 1.00 5.64 C ANISOU 265 C LYS A 37 682 717 740 104 -85 42 C ATOM 266 O LYS A 37 -0.013 -5.875 9.107 1.00 5.97 O ANISOU 266 O LYS A 37 682 828 756 131 -30 -45 O ATOM 267 CB LYS A 37 -1.610 -4.005 7.018 1.00 5.39 C ANISOU 267 CB LYS A 37 605 668 772 75 -7 144 C ATOM 268 CG LYS A 37 -0.938 -2.969 7.910 1.00 5.68 C ANISOU 268 CG LYS A 37 692 765 701 84 17 40 C ATOM 269 CD LYS A 37 -0.443 -1.798 7.126 1.00 6.19 C ANISOU 269 CD LYS A 37 853 703 795 141 -35 7 C ATOM 270 CE LYS A 37 0.077 -0.621 7.915 1.00 6.00 C ANISOU 270 CE LYS A 37 735 709 836 192 150 20 C ATOM 271 NZ LYS A 37 0.716 0.382 7.023 1.00 6.57 N ANISOU 271 NZ LYS A 37 844 765 884 -19 45 200 N ATOM 272 N GLU A 38 0.106 -6.597 6.984 1.00 6.16 N ANISOU 272 N GLU A 38 677 787 873 122 -126 -77 N ATOM 273 CA GLU A 38 1.531 -6.891 6.987 1.00 6.60 C ANISOU 273 CA GLU A 38 730 927 851 159 -23 -100 C ATOM 274 C GLU A 38 2.213 -5.700 6.325 1.00 7.43 C ANISOU 274 C GLU A 38 808 1060 954 159 -8 -25 C ATOM 275 O GLU A 38 2.244 -5.572 5.102 1.00 9.68 O ANISOU 275 O GLU A 38 1256 1509 911 132 -117 119 O ATOM 276 CB GLU A 38 1.829 -8.190 6.250 1.00 8.30 C ANISOU 276 CB GLU A 38 984 1166 1000 226 -100 -112 C ATOM 277 CG GLU A 38 1.035 -9.367 6.726 1.00 9.48 C ANISOU 277 CG GLU A 38 1118 1250 1234 291 -98 -373 C ATOM 278 CD GLU A 38 1.458 -10.679 6.100 1.00 11.61 C ANISOU 278 CD GLU A 38 1599 1394 1418 188 -107 -324 C ATOM 279 OE1 GLU A 38 2.142 -10.666 5.047 1.00 15.00 O ANISOU 279 OE1 GLU A 38 2041 1426 2230 271 -30 -925 O ATOM 280 OE2 GLU A 38 1.056 -11.700 6.693 1.00 15.34 O ANISOU 280 OE2 GLU A 38 2287 1255 2286 262 -359 -321 O ATOM 281 N ASN A 39 2.671 -4.764 7.137 1.00 7.31 N ANISOU 281 N ASN A 39 770 1084 922 6 2 92 N ATOM 282 CA ASN A 39 3.290 -3.548 6.651 1.00 8.04 C ANISOU 282 CA ASN A 39 789 1128 1137 60 -83 107 C ATOM 283 C ASN A 39 4.614 -3.758 5.920 1.00 8.14 C ANISOU 283 C ASN A 39 919 1124 1050 153 -6 106 C ATOM 284 O ASN A 39 4.943 -3.005 5.010 1.00 9.69 O ANISOU 284 O ASN A 39 1077 1351 1251 18 28 238 O ATOM 285 CB ASN A 39 3.521 -2.602 7.825 1.00 7.89 C ANISOU 285 CB ASN A 39 737 1155 1103 149 -19 74 C ATOM 286 CG ASN A 39 3.984 -1.263 7.386 1.00 8.73 C ANISOU 286 CG ASN A 39 896 1071 1348 140 -145 40 C ATOM 287 OD1 ASN A 39 3.309 -0.583 6.593 1.00 10.25 O ANISOU 287 OD1 ASN A 39 983 1095 1815 190 -34 266 O ATOM 288 ND2 ASN A 39 5.129 -0.842 7.914 1.00 10.22 N ANISOU 288 ND2 ASN A 39 1138 1204 1540 46 -68 -4 N ATOM 289 N PHE A 40 5.391 -4.731 6.353 1.00 8.36 N ANISOU 289 N PHE A 40 813 1279 1084 179 80 104 N ATOM 290 CA PHE A 40 6.643 -5.104 5.723 1.00 8.56 C ANISOU 290 CA PHE A 40 897 1295 1061 132 15 77 C ATOM 291 C PHE A 40 6.795 -6.600 5.841 1.00 8.02 C ANISOU 291 C PHE A 40 786 1281 979 44 -49 14 C ATOM 292 O PHE A 40 6.588 -7.172 6.900 1.00 8.24 O ANISOU 292 O PHE A 40 867 1298 965 133 -71 117 O ATOM 293 CB PHE A 40 7.828 -4.379 6.375 1.00 8.98 C ANISOU 293 CB PHE A 40 924 1242 1246 109 90 47 C ATOM 294 CG PHE A 40 9.111 -4.693 5.704 1.00 9.19 C ANISOU 294 CG PHE A 40 849 1246 1395 5 -12 -8 C ATOM 295 CD1 PHE A 40 9.405 -4.112 4.489 1.00 10.98 C ANISOU 295 CD1 PHE A 40 889 1516 1763 -130 251 108 C ATOM 296 CD2 PHE A 40 9.962 -5.656 6.206 1.00 11.51 C ANISOU 296 CD2 PHE A 40 875 1590 1908 -98 126 24 C ATOM 297 CE1 PHE A 40 10.569 -4.439 3.808 1.00 14.18 C ANISOU 297 CE1 PHE A 40 1421 2078 1887 -242 217 57 C ATOM 298 CE2 PHE A 40 11.142 -5.969 5.525 1.00 13.12 C ANISOU 298 CE2 PHE A 40 1192 1594 2196 -102 -13 -165 C ATOM 299 CZ PHE A 40 11.415 -5.356 4.332 1.00 14.27 C ANISOU 299 CZ PHE A 40 1437 1938 2047 -69 171 -274 C ATOM 300 N GLN A 41 7.172 -7.246 4.751 1.00 8.19 N ANISOU 300 N GLN A 41 769 1297 1044 37 -50 67 N ATOM 301 CA GLN A 41 7.393 -8.681 4.749 1.00 8.30 C ANISOU 301 CA GLN A 41 904 1227 1021 -59 -58 -45 C ATOM 302 C GLN A 41 8.566 -8.956 3.809 1.00 7.75 C ANISOU 302 C GLN A 41 982 1005 956 -22 -30 -55 C ATOM 303 O GLN A 41 8.459 -8.800 2.606 1.00 8.36 O ANISOU 303 O GLN A 41 987 1250 938 -22 -68 -88 O ATOM 304 CB GLN A 41 6.088 -9.408 4.361 1.00 8.68 C ANISOU 304 CB GLN A 41 963 1283 1052 -78 59 25 C ATOM 305 CG GLN A 41 5.913 -10.754 4.993 1.00 10.67 C ANISOU 305 CG GLN A 41 1272 1571 1211 -233 -55 62 C ATOM 306 CD GLN A 41 6.647 -11.859 4.274 1.00 9.95 C ANISOU 306 CD GLN A 41 1139 1447 1195 -396 -322 64 C ATOM 307 OE1 GLN A 41 7.688 -11.622 3.651 1.00 9.92 O ANISOU 307 OE1 GLN A 41 1166 1500 1103 -410 -156 35 O ATOM 308 NE2 GLN A 41 6.101 -13.072 4.327 1.00 12.18 N ANISOU 308 NE2 GLN A 41 1501 1540 1587 -442 -494 235 N ATOM 309 N LYS A 42 9.743 -9.208 4.376 1.00 8.53 N ANISOU 309 N LYS A 42 1055 1193 993 -57 -97 -57 N ATOM 310 CA LYS A 42 10.991 -9.193 3.606 1.00 8.58 C ANISOU 310 CA LYS A 42 1094 1134 1032 58 -46 -15 C ATOM 311 C LYS A 42 10.968 -10.217 2.463 1.00 9.08 C ANISOU 311 C LYS A 42 1043 1256 1148 32 -45 -48 C ATOM 312 O LYS A 42 11.373 -9.933 1.350 1.00 9.17 O ANISOU 312 O LYS A 42 942 1424 1119 58 83 -146 O ATOM 313 CB LYS A 42 12.178 -9.470 4.535 1.00 8.83 C ANISOU 313 CB LYS A 42 1037 1197 1121 -69 -38 -82 C ATOM 314 CG LYS A 42 13.541 -9.500 3.880 1.00 8.63 C ANISOU 314 CG LYS A 42 1114 1031 1132 -59 -21 -39 C ATOM 315 CD LYS A 42 14.602 -9.770 4.922 1.00 10.42 C ANISOU 315 CD LYS A 42 1135 1198 1625 -41 -49 181 C ATOM 316 CE LYS A 42 15.971 -9.903 4.335 1.00 11.81 C ANISOU 316 CE LYS A 42 1282 1480 1722 -29 -39 250 C ATOM 317 NZ LYS A 42 16.973 -10.021 5.457 1.00 13.09 N ANISOU 317 NZ LYS A 42 1311 1456 2204 -179 -299 439 N ATOM 318 N GLU A 43 10.491 -11.416 2.752 1.00 9.31 N ANISOU 318 N GLU A 43 1203 1171 1164 -12 -15 -24 N ATOM 319 CA GLU A 43 10.451 -12.499 1.761 1.00 10.83 C ANISOU 319 CA GLU A 43 1411 1356 1348 -4 -49 -51 C ATOM 320 C GLU A 43 9.556 -12.195 0.555 1.00 9.74 C ANISOU 320 C GLU A 43 1347 1165 1188 -46 -37 -76 C ATOM 321 O GLU A 43 9.893 -12.548 -0.576 1.00 11.68 O ANISOU 321 O GLU A 43 1558 1516 1363 93 63 -182 O ATOM 322 CB GLU A 43 10.023 -13.808 2.440 1.00 11.79 C ANISOU 322 CB GLU A 43 1572 1454 1451 -16 -127 -7 C ATOM 323 CG GLU A 43 10.189 -15.078 1.642 1.00 14.02 C ANISOU 323 CG GLU A 43 1953 1722 1650 -20 -155 108 C ATOM 324 CD GLU A 43 10.079 -16.336 2.511 1.00 14.00 C ANISOU 324 CD GLU A 43 2028 1604 1688 16 46 249 C ATOM 325 OE1 GLU A 43 8.946 -16.721 2.883 1.00 19.95 O ANISOU 325 OE1 GLU A 43 2969 2376 2233 -37 -79 28 O ATOM 326 OE2 GLU A 43 11.125 -16.925 2.837 1.00 18.50 O ANISOU 326 OE2 GLU A 43 2832 2119 2077 24 38 64 O ATOM 327 N ALYS A 44 8.450 -11.519 0.782 0.50 9.41 N ANISOU 327 N ALYS A 44 1177 1204 1191 -109 -58 -84 N ATOM 328 CA ALYS A 44 7.596 -11.131 -0.318 0.50 8.93 C ANISOU 328 CA ALYS A 44 1136 1150 1106 -100 -69 -23 C ATOM 329 C ALYS A 44 8.065 -9.854 -0.998 0.50 8.81 C ANISOU 329 C ALYS A 44 1049 1186 1110 -90 -39 22 C ATOM 330 O ALYS A 44 7.884 -9.712 -2.208 0.50 8.61 O ANISOU 330 O ALYS A 44 938 1289 1044 -258 -49 23 O ATOM 331 CB ALYS A 44 6.151 -11.026 0.153 0.50 8.96 C ANISOU 331 CB ALYS A 44 1120 1183 1100 -105 -110 -111 C ATOM 332 CG ALYS A 44 5.612 -12.370 0.636 0.50 9.79 C ANISOU 332 CG ALYS A 44 1171 1453 1096 -113 -168 -25 C ATOM 333 CD ALYS A 44 4.139 -12.325 0.994 0.50 8.95 C ANISOU 333 CD ALYS A 44 1105 1365 929 4 92 -54 C ATOM 334 CE ALYS A 44 3.578 -13.736 1.200 0.50 8.38 C ANISOU 334 CE ALYS A 44 955 1251 978 -47 1 3 C ATOM 335 NZ ALYS A 44 3.365 -14.455 -0.100 0.50 9.45 N ANISOU 335 NZ ALYS A 44 868 1535 1187 -168 -182 108 N ATOM 336 N AMET A 45 8.696 -8.934 -0.267 0.70 8.30 N ANISOU 336 N AMET A 45 1000 1062 1093 -34 3 -6 N ATOM 337 CA AMET A 45 8.992 -7.644 -0.886 0.70 8.68 C ANISOU 337 CA AMET A 45 1120 1040 1138 9 29 11 C ATOM 338 C AMET A 45 10.279 -7.656 -1.693 0.70 8.20 C ANISOU 338 C AMET A 45 1014 1008 1091 -8 25 -66 C ATOM 339 O AMET A 45 10.414 -6.878 -2.632 0.70 7.59 O ANISOU 339 O AMET A 45 796 1073 1014 35 -2 -117 O ATOM 340 CB AMET A 45 8.886 -6.523 0.136 0.70 8.90 C ANISOU 340 CB AMET A 45 1173 1031 1175 47 25 8 C ATOM 341 CG AMET A 45 7.435 -6.376 0.589 0.70 9.86 C ANISOU 341 CG AMET A 45 1377 1092 1276 -35 -24 13 C ATOM 342 SD AMET A 45 7.231 -5.210 1.893 0.70 11.72 S ANISOU 342 SD AMET A 45 1605 1551 1297 513 121 -127 S ATOM 343 CE AMET A 45 7.817 -3.719 1.120 0.70 12.30 C ANISOU 343 CE AMET A 45 1417 1503 1750 40 5 -103 C ATOM 344 N LEU A 46 11.203 -8.562 -1.387 1.00 8.57 N ANISOU 344 N LEU A 46 966 1126 1163 3 49 -34 N ATOM 345 CA LEU A 46 12.421 -8.666 -2.213 1.00 9.35 C ANISOU 345 CA LEU A 46 1076 1210 1263 30 36 -6 C ATOM 346 C LEU A 46 12.076 -8.945 -3.696 1.00 9.73 C ANISOU 346 C LEU A 46 1124 1324 1246 24 27 -24 C ATOM 347 O LEU A 46 12.565 -8.246 -4.602 1.00 10.81 O ANISOU 347 O LEU A 46 1160 1517 1431 23 -81 -53 O ATOM 348 CB LEU A 46 13.380 -9.713 -1.626 1.00 9.92 C ANISOU 348 CB LEU A 46 1145 1259 1362 50 55 0 C ATOM 349 CG LEU A 46 14.131 -9.312 -0.360 1.00 10.48 C ANISOU 349 CG LEU A 46 1144 1314 1523 121 58 42 C ATOM 350 CD1 LEU A 46 14.891 -10.481 0.264 1.00 12.83 C ANISOU 350 CD1 LEU A 46 1526 1546 1801 148 -177 153 C ATOM 351 CD2 LEU A 46 15.084 -8.197 -0.668 1.00 12.97 C ANISOU 351 CD2 LEU A 46 1699 1492 1735 -113 -195 101 C ATOM 352 N PRO A 47 11.245 -9.951 -3.993 1.00 10.75 N ANISOU 352 N PRO A 47 1324 1444 1317 -61 41 -77 N ATOM 353 CA PRO A 47 10.898 -10.185 -5.416 1.00 11.09 C ANISOU 353 CA PRO A 47 1381 1515 1317 -60 30 -138 C ATOM 354 C PRO A 47 10.130 -9.063 -6.115 1.00 11.40 C ANISOU 354 C PRO A 47 1354 1608 1369 -96 -18 -144 C ATOM 355 O PRO A 47 10.111 -9.003 -7.332 1.00 12.56 O ANISOU 355 O PRO A 47 1462 1889 1419 12 -43 -263 O ATOM 356 CB PRO A 47 10.059 -11.478 -5.398 1.00 12.14 C ANISOU 356 CB PRO A 47 1495 1579 1536 -14 -7 -64 C ATOM 357 CG PRO A 47 10.172 -12.032 -4.057 1.00 12.23 C ANISOU 357 CG PRO A 47 1535 1576 1533 -241 3 15 C ATOM 358 CD PRO A 47 10.677 -10.992 -3.126 1.00 11.02 C ANISOU 358 CD PRO A 47 1415 1447 1324 -87 6 -147 C ATOM 359 N LEU A 48 9.492 -8.179 -5.356 1.00 11.15 N ANISOU 359 N LEU A 48 1341 1570 1325 -54 27 -153 N ATOM 360 CA LEU A 48 8.826 -6.997 -5.921 1.00 11.60 C ANISOU 360 CA LEU A 48 1406 1610 1390 6 -6 -38 C ATOM 361 C LEU A 48 9.776 -5.838 -6.203 1.00 11.76 C ANISOU 361 C LEU A 48 1330 1578 1558 66 -14 86 C ATOM 362 O LEU A 48 9.365 -4.802 -6.719 1.00 14.37 O ANISOU 362 O LEU A 48 1401 2188 1869 138 -81 367 O ATOM 363 CB LEU A 48 7.732 -6.513 -4.976 1.00 12.05 C ANISOU 363 CB LEU A 48 1349 1692 1537 27 2 1 C ATOM 364 CG LEU A 48 6.618 -7.538 -4.785 1.00 13.95 C ANISOU 364 CG LEU A 48 1623 1945 1732 -38 47 32 C ATOM 365 CD1 LEU A 48 5.627 -7.041 -3.766 1.00 15.57 C ANISOU 365 CD1 LEU A 48 1693 2301 1921 155 88 36 C ATOM 366 CD2 LEU A 48 5.905 -7.875 -6.078 1.00 16.46 C ANISOU 366 CD2 LEU A 48 1834 2417 2000 -11 49 126 C ATOM 367 N GLY A 49 11.035 -5.992 -5.809 1.00 11.12 N ANISOU 367 N GLY A 49 1256 1508 1459 117 -76 52 N ATOM 368 CA GLY A 49 12.062 -5.020 -6.091 1.00 10.85 C ANISOU 368 CA GLY A 49 1342 1408 1370 67 -23 39 C ATOM 369 C GLY A 49 12.613 -4.302 -4.870 1.00 10.33 C ANISOU 369 C GLY A 49 1234 1344 1344 57 -88 52 C ATOM 370 O GLY A 49 13.498 -3.484 -5.017 1.00 10.38 O ANISOU 370 O GLY A 49 1199 1253 1493 -46 -238 92 O ATOM 371 N PHE A 50 12.115 -4.573 -3.671 1.00 9.74 N ANISOU 371 N PHE A 50 1150 1233 1316 -17 -104 26 N ATOM 372 CA PHE A 50 12.733 -3.992 -2.475 1.00 8.86 C ANISOU 372 CA PHE A 50 1066 1088 1211 55 -55 -58 C ATOM 373 C PHE A 50 14.215 -4.399 -2.475 1.00 8.87 C ANISOU 373 C PHE A 50 989 1104 1275 1 -100 -18 C ATOM 374 O PHE A 50 14.511 -5.603 -2.611 1.00 9.24 O ANISOU 374 O PHE A 50 1083 1032 1395 10 -183 -125 O ATOM 375 CB PHE A 50 12.024 -4.463 -1.198 1.00 8.94 C ANISOU 375 CB PHE A 50 1066 1168 1162 97 -54 -42 C ATOM 376 CG PHE A 50 12.408 -3.681 0.012 1.00 9.21 C ANISOU 376 CG PHE A 50 1078 1269 1151 120 8 -91 C ATOM 377 CD1 PHE A 50 11.606 -2.674 0.489 1.00 10.72 C ANISOU 377 CD1 PHE A 50 1048 1495 1529 256 -182 -190 C ATOM 378 CD2 PHE A 50 13.577 -3.954 0.684 1.00 9.91 C ANISOU 378 CD2 PHE A 50 1048 1307 1411 160 -71 3 C ATOM 379 CE1 PHE A 50 11.987 -1.946 1.606 1.00 11.56 C ANISOU 379 CE1 PHE A 50 1369 1361 1659 278 -150 -318 C ATOM 380 CE2 PHE A 50 13.940 -3.228 1.799 1.00 9.57 C ANISOU 380 CE2 PHE A 50 970 1250 1414 -56 -141 -29 C ATOM 381 CZ PHE A 50 13.149 -2.224 2.252 1.00 10.49 C ANISOU 381 CZ PHE A 50 1308 1347 1328 -141 -299 -188 C ATOM 382 N PRO A 51 15.157 -3.448 -2.404 1.00 8.54 N ANISOU 382 N PRO A 51 1068 964 1212 29 -151 -60 N ATOM 383 CA PRO A 51 16.560 -3.805 -2.674 1.00 8.86 C ANISOU 383 CA PRO A 51 1094 1091 1181 3 -75 -63 C ATOM 384 C PRO A 51 17.239 -4.631 -1.586 1.00 8.28 C ANISOU 384 C PRO A 51 1072 953 1119 -63 -25 -100 C ATOM 385 O PRO A 51 17.155 -4.282 -0.406 1.00 7.98 O ANISOU 385 O PRO A 51 923 1028 1078 -82 -67 -93 O ATOM 386 CB PRO A 51 17.244 -2.447 -2.854 1.00 9.42 C ANISOU 386 CB PRO A 51 1125 1149 1305 0 -51 27 C ATOM 387 CG PRO A 51 16.415 -1.520 -2.077 1.00 9.81 C ANISOU 387 CG PRO A 51 1354 1058 1315 -29 -143 10 C ATOM 388 CD PRO A 51 14.986 -2.000 -2.176 1.00 8.98 C ANISOU 388 CD PRO A 51 1010 1061 1339 18 -76 4 C ATOM 389 N GLU A 52 17.919 -5.701 -1.995 1.00 8.93 N ANISOU 389 N GLU A 52 1232 1066 1096 110 -120 -96 N ATOM 390 CA GLU A 52 18.738 -6.479 -1.057 1.00 9.70 C ANISOU 390 CA GLU A 52 1326 1099 1260 112 -94 -55 C ATOM 391 C GLU A 52 19.768 -5.606 -0.335 1.00 9.33 C ANISOU 391 C GLU A 52 1178 1151 1213 92 -75 -50 C ATOM 392 O GLU A 52 20.092 -5.860 0.820 1.00 10.07 O ANISOU 392 O GLU A 52 1285 1336 1203 189 -162 -111 O ATOM 393 CB GLU A 52 19.465 -7.651 -1.742 1.00 11.21 C ANISOU 393 CB GLU A 52 1498 1321 1437 134 -145 -66 C ATOM 394 CG GLU A 52 20.242 -8.563 -0.780 1.00 14.89 C ANISOU 394 CG GLU A 52 1963 1765 1928 46 -238 -29 C ATOM 395 CD GLU A 52 19.410 -9.138 0.367 1.00 18.58 C ANISOU 395 CD GLU A 52 2477 2307 2272 -186 -378 -11 C ATOM 396 OE1 GLU A 52 18.291 -9.639 0.113 1.00 21.39 O ANISOU 396 OE1 GLU A 52 2739 2680 2706 -223 -488 -4 O ATOM 397 OE2 GLU A 52 19.877 -9.089 1.546 1.00 20.59 O ANISOU 397 OE2 GLU A 52 2680 2556 2585 -78 -555 1 O ATOM 398 N SER A 53 20.247 -4.553 -0.982 1.00 9.08 N ANISOU 398 N SER A 53 1177 1194 1076 50 -46 -8 N ATOM 399 CA SER A 53 21.254 -3.683 -0.378 1.00 9.19 C ANISOU 399 CA SER A 53 1107 1280 1105 -31 6 -37 C ATOM 400 C SER A 53 20.757 -3.046 0.903 1.00 8.61 C ANISOU 400 C SER A 53 1047 1163 1059 -73 -45 -136 C ATOM 401 O SER A 53 21.556 -2.700 1.751 1.00 9.84 O ANISOU 401 O SER A 53 1167 1341 1228 -245 -62 -99 O ATOM 402 CB SER A 53 21.699 -2.608 -1.361 1.00 10.15 C ANISOU 402 CB SER A 53 1187 1421 1246 -72 34 -40 C ATOM 403 OG SER A 53 20.611 -1.815 -1.755 1.00 12.17 O ANISOU 403 OG SER A 53 1624 1552 1446 -206 78 179 O ATOM 404 N PHE A 54 19.447 -2.939 1.076 1.00 7.84 N ANISOU 404 N PHE A 54 991 987 1001 -65 -90 -231 N ATOM 405 CA PHE A 54 18.921 -2.404 2.336 1.00 7.75 C ANISOU 405 CA PHE A 54 1025 938 979 -7 -95 -168 C ATOM 406 C PHE A 54 19.436 -3.171 3.553 1.00 7.63 C ANISOU 406 C PHE A 54 1045 902 952 -89 -77 -190 C ATOM 407 O PHE A 54 19.697 -2.586 4.591 1.00 8.64 O ANISOU 407 O PHE A 54 1290 955 1037 58 -152 -243 O ATOM 408 CB PHE A 54 17.400 -2.412 2.337 1.00 7.49 C ANISOU 408 CB PHE A 54 974 849 1020 -64 -163 -79 C ATOM 409 CG PHE A 54 16.783 -1.706 3.516 1.00 7.15 C ANISOU 409 CG PHE A 54 930 871 915 -149 -167 82 C ATOM 410 CD1 PHE A 54 16.627 -0.339 3.507 1.00 6.89 C ANISOU 410 CD1 PHE A 54 1073 708 834 -41 -161 -76 C ATOM 411 CD2 PHE A 54 16.325 -2.414 4.603 1.00 7.43 C ANISOU 411 CD2 PHE A 54 864 889 1068 -182 -86 -47 C ATOM 412 CE1 PHE A 54 16.014 0.315 4.566 1.00 7.67 C ANISOU 412 CE1 PHE A 54 1070 755 1088 55 -80 -247 C ATOM 413 CE2 PHE A 54 15.752 -1.789 5.652 1.00 9.95 C ANISOU 413 CE2 PHE A 54 1261 1434 1085 -135 30 92 C ATOM 414 CZ PHE A 54 15.586 -0.426 5.651 1.00 7.92 C ANISOU 414 CZ PHE A 54 822 1108 1079 -26 45 -424 C ATOM 415 N PHE A 55 19.589 -4.486 3.376 1.00 7.79 N ANISOU 415 N PHE A 55 945 922 1093 -165 -110 -46 N ATOM 416 CA PHE A 55 19.952 -5.400 4.436 1.00 7.79 C ANISOU 416 CA PHE A 55 979 943 1036 -151 -126 -103 C ATOM 417 C PHE A 55 21.408 -5.746 4.544 1.00 7.24 C ANISOU 417 C PHE A 55 956 857 935 -58 -172 -160 C ATOM 418 O PHE A 55 21.783 -6.529 5.414 1.00 7.37 O ANISOU 418 O PHE A 55 1061 841 896 -148 -194 -171 O ATOM 419 CB PHE A 55 19.192 -6.700 4.203 1.00 7.56 C ANISOU 419 CB PHE A 55 871 919 1081 -185 -117 -101 C ATOM 420 CG PHE A 55 17.718 -6.496 4.117 1.00 9.44 C ANISOU 420 CG PHE A 55 1170 1096 1321 -189 -226 -55 C ATOM 421 CD1 PHE A 55 17.074 -6.455 2.885 1.00 10.62 C ANISOU 421 CD1 PHE A 55 1134 1254 1646 -252 -231 180 C ATOM 422 CD2 PHE A 55 16.991 -6.302 5.272 1.00 10.40 C ANISOU 422 CD2 PHE A 55 978 1177 1796 -143 22 125 C ATOM 423 CE1 PHE A 55 15.730 -6.232 2.830 1.00 14.62 C ANISOU 423 CE1 PHE A 55 1592 1698 2264 -315 -291 200 C ATOM 424 CE2 PHE A 55 15.638 -6.073 5.206 1.00 13.61 C ANISOU 424 CE2 PHE A 55 1423 1547 2200 -198 73 105 C ATOM 425 CZ PHE A 55 15.027 -6.038 3.992 1.00 12.61 C ANISOU 425 CZ PHE A 55 1193 1353 2243 -247 -88 230 C ATOM 426 N ALA A 56 22.231 -5.167 3.680 1.00 7.39 N ANISOU 426 N ALA A 56 927 944 937 -27 -119 -231 N ATOM 427 CA ALA A 56 23.608 -5.622 3.521 1.00 7.49 C ANISOU 427 CA ALA A 56 911 1016 918 66 -49 -173 C ATOM 428 C ALA A 56 24.483 -5.540 4.760 1.00 7.20 C ANISOU 428 C ALA A 56 873 1024 838 63 -107 -265 C ATOM 429 O ALA A 56 25.416 -6.323 4.895 1.00 7.95 O ANISOU 429 O ALA A 56 1139 1069 809 105 -309 -520 O ATOM 430 CB ALA A 56 24.287 -4.874 2.377 1.00 8.57 C ANISOU 430 CB ALA A 56 1034 1217 1005 72 -68 -101 C ATOM 431 N GLU A 57 24.223 -4.589 5.654 1.00 7.60 N ANISOU 431 N GLU A 57 856 1182 847 63 -32 -268 N ATOM 432 CA GLU A 57 25.060 -4.412 6.854 1.00 7.53 C ANISOU 432 CA GLU A 57 820 1093 948 11 -12 -216 C ATOM 433 C GLU A 57 24.382 -4.930 8.112 1.00 7.01 C ANISOU 433 C GLU A 57 890 955 817 56 4 -303 C ATOM 434 O GLU A 57 24.929 -4.831 9.200 1.00 8.28 O ANISOU 434 O GLU A 57 1006 1241 899 17 -82 -407 O ATOM 435 CB GLU A 57 25.472 -2.953 7.044 1.00 8.67 C ANISOU 435 CB GLU A 57 1005 1232 1054 -134 23 -198 C ATOM 436 CG GLU A 57 26.290 -2.391 5.909 1.00 9.96 C ANISOU 436 CG GLU A 57 1256 1378 1150 -221 0 -219 C ATOM 437 CD GLU A 57 26.817 -1.008 6.219 1.00 11.75 C ANISOU 437 CD GLU A 57 1338 1697 1430 -153 267 -261 C ATOM 438 OE1 GLU A 57 26.042 -0.167 6.735 1.00 13.10 O ANISOU 438 OE1 GLU A 57 1516 1918 1541 -180 270 -211 O ATOM 439 OE2 GLU A 57 28.007 -0.769 5.941 1.00 15.25 O ANISOU 439 OE2 GLU A 57 1644 2160 1988 -253 172 75 O ATOM 440 N GLY A 58 23.170 -5.447 7.993 1.00 7.39 N ANISOU 440 N GLY A 58 945 934 927 9 94 -287 N ATOM 441 CA GLY A 58 22.473 -5.964 9.158 1.00 7.93 C ANISOU 441 CA GLY A 58 1109 949 954 8 117 -171 C ATOM 442 C GLY A 58 22.072 -4.866 10.156 1.00 7.90 C ANISOU 442 C GLY A 58 1263 902 836 78 283 -123 C ATOM 443 O GLY A 58 21.963 -5.123 11.363 1.00 11.03 O ANISOU 443 O GLY A 58 2087 1146 956 -66 314 -11 O ATOM 444 N LYS A 59 21.834 -3.661 9.680 1.00 6.76 N ANISOU 444 N LYS A 59 901 951 716 106 205 -131 N ATOM 445 CA LYS A 59 21.442 -2.555 10.554 1.00 6.67 C ANISOU 445 CA LYS A 59 900 971 663 184 119 -163 C ATOM 446 C LYS A 59 19.960 -2.279 10.413 1.00 7.30 C ANISOU 446 C LYS A 59 911 1095 767 162 66 -176 C ATOM 447 O LYS A 59 19.424 -2.302 9.307 1.00 9.19 O ANISOU 447 O LYS A 59 1001 1684 804 272 -21 -266 O ATOM 448 CB LYS A 59 22.216 -1.295 10.180 1.00 6.55 C ANISOU 448 CB LYS A 59 953 891 642 241 221 -168 C ATOM 449 CG LYS A 59 23.714 -1.387 10.358 1.00 6.97 C ANISOU 449 CG LYS A 59 888 1031 728 154 107 -95 C ATOM 450 CD LYS A 59 24.379 -0.144 9.858 1.00 8.58 C ANISOU 450 CD LYS A 59 997 1244 1018 129 133 -103 C ATOM 451 CE LYS A 59 25.866 -0.156 10.005 1.00 8.51 C ANISOU 451 CE LYS A 59 1005 1014 1211 77 26 -138 C ATOM 452 NZ LYS A 59 26.499 0.958 9.259 1.00 8.80 N ANISOU 452 NZ LYS A 59 1008 1130 1202 -44 14 -150 N ATOM 453 N LEU A 60 19.296 -1.993 11.528 1.00 6.01 N ANISOU 453 N LEU A 60 643 977 661 99 44 -165 N ATOM 454 CA LEU A 60 17.862 -1.796 11.528 1.00 6.04 C ANISOU 454 CA LEU A 60 700 889 706 38 8 -81 C ATOM 455 C LEU A 60 17.446 -0.852 12.635 1.00 4.94 C ANISOU 455 C LEU A 60 502 771 603 -15 30 -50 C ATOM 456 O LEU A 60 17.792 -1.038 13.804 1.00 5.04 O ANISOU 456 O LEU A 60 512 806 594 62 149 10 O ATOM 457 CB LEU A 60 17.158 -3.126 11.721 1.00 6.91 C ANISOU 457 CB LEU A 60 821 967 836 19 74 -133 C ATOM 458 CG LEU A 60 15.647 -3.069 11.624 1.00 10.04 C ANISOU 458 CG LEU A 60 1183 1158 1473 2 -14 -51 C ATOM 459 CD1 LEU A 60 15.198 -2.733 10.223 1.00 11.76 C ANISOU 459 CD1 LEU A 60 1251 1424 1790 -188 -171 -66 C ATOM 460 CD2 LEU A 60 15.072 -4.399 12.088 1.00 11.87 C ANISOU 460 CD2 LEU A 60 1312 1445 1750 -207 38 -67 C ATOM 461 N GLN A 61 16.638 0.113 12.261 1.00 5.27 N ANISOU 461 N GLN A 61 666 787 547 52 71 -85 N ATOM 462 CA GLN A 61 16.008 1.034 13.203 1.00 4.96 C ANISOU 462 CA GLN A 61 584 782 516 92 103 21 C ATOM 463 C GLN A 61 14.620 1.383 12.690 1.00 5.35 C ANISOU 463 C GLN A 61 667 832 531 82 94 -3 C ATOM 464 O GLN A 61 14.420 1.591 11.508 1.00 7.10 O ANISOU 464 O GLN A 61 829 1257 611 138 96 6 O ATOM 465 CB GLN A 61 16.884 2.279 13.348 1.00 5.70 C ANISOU 465 CB GLN A 61 764 774 627 42 113 58 C ATOM 466 CG GLN A 61 16.305 3.387 14.202 1.00 5.98 C ANISOU 466 CG GLN A 61 814 736 720 117 162 69 C ATOM 467 CD GLN A 61 17.254 4.543 14.443 1.00 6.30 C ANISOU 467 CD GLN A 61 701 823 866 84 302 -167 C ATOM 468 OE1 GLN A 61 18.464 4.370 14.214 1.00 7.72 O ANISOU 468 OE1 GLN A 61 987 989 955 62 445 28 O ATOM 469 NE2 GLN A 61 16.770 5.620 14.947 1.00 9.61 N ANISOU 469 NE2 GLN A 61 1198 1050 1403 62 208 -139 N ATOM 470 N ASN A 62 13.670 1.424 13.623 1.00 5.09 N ANISOU 470 N ASN A 62 569 874 489 26 114 24 N ATOM 471 CA ASN A 62 12.292 1.831 13.330 1.00 5.36 C ANISOU 471 CA ASN A 62 624 792 618 60 54 32 C ATOM 472 C ASN A 62 11.998 3.058 14.157 1.00 5.06 C ANISOU 472 C ASN A 62 640 682 597 1 76 32 C ATOM 473 O ASN A 62 12.035 2.984 15.389 1.00 5.75 O ANISOU 473 O ASN A 62 738 891 555 91 182 52 O ATOM 474 CB ASN A 62 11.349 0.690 13.732 1.00 6.49 C ANISOU 474 CB ASN A 62 772 788 904 41 92 13 C ATOM 475 CG ASN A 62 9.852 1.002 13.660 1.00 6.86 C ANISOU 475 CG ASN A 62 816 955 836 -59 37 153 C ATOM 476 OD1 ASN A 62 9.085 0.412 14.443 1.00 8.25 O ANISOU 476 OD1 ASN A 62 762 1325 1045 -144 126 122 O ATOM 477 ND2 ASN A 62 9.412 1.824 12.724 1.00 7.14 N ANISOU 477 ND2 ASN A 62 934 923 856 10 -63 72 N ATOM 478 N ASN A 63 11.713 4.172 13.492 1.00 5.54 N ANISOU 478 N ASN A 63 748 722 632 84 209 6 N ATOM 479 CA ASN A 63 11.307 5.398 14.144 1.00 5.42 C ANISOU 479 CA ASN A 63 667 749 642 78 93 14 C ATOM 480 C ASN A 63 9.818 5.607 13.930 1.00 5.63 C ANISOU 480 C ASN A 63 684 788 665 75 67 -5 C ATOM 481 O ASN A 63 9.270 5.226 12.903 1.00 6.65 O ANISOU 481 O ASN A 63 759 913 851 174 55 -33 O ATOM 482 CB ASN A 63 12.057 6.590 13.539 1.00 6.58 C ANISOU 482 CB ASN A 63 769 771 958 148 117 40 C ATOM 483 CG ASN A 63 13.553 6.596 13.854 1.00 7.37 C ANISOU 483 CG ASN A 63 812 967 1018 30 282 110 C ATOM 484 OD1 ASN A 63 14.340 7.250 13.146 1.00 14.75 O ANISOU 484 OD1 ASN A 63 1463 2172 1967 -171 327 716 O ATOM 485 ND2 ASN A 63 13.947 5.914 14.869 1.00 5.59 N ANISOU 485 ND2 ASN A 63 370 901 853 24 190 -162 N ATOM 486 N VAL A 64 9.190 6.261 14.900 1.00 5.47 N ANISOU 486 N VAL A 64 625 809 644 54 45 15 N ATOM 487 CA VAL A 64 7.789 6.622 14.800 1.00 5.57 C ANISOU 487 CA VAL A 64 722 711 684 46 0 36 C ATOM 488 C VAL A 64 7.611 8.062 15.228 1.00 5.78 C ANISOU 488 C VAL A 64 640 784 773 58 29 -111 C ATOM 489 O VAL A 64 8.106 8.469 16.267 1.00 6.33 O ANISOU 489 O VAL A 64 583 885 936 157 -68 -141 O ATOM 490 CB VAL A 64 6.909 5.729 15.684 1.00 6.03 C ANISOU 490 CB VAL A 64 682 877 732 3 87 33 C ATOM 491 CG1 VAL A 64 5.473 6.189 15.571 1.00 7.58 C ANISOU 491 CG1 VAL A 64 727 1100 1052 -68 191 -58 C ATOM 492 CG2 VAL A 64 7.026 4.296 15.273 1.00 7.32 C ANISOU 492 CG2 VAL A 64 1022 859 897 -50 -12 23 C ATOM 493 N ASER A 65 6.880 8.829 14.442 0.70 6.33 N ANISOU 493 N ASER A 65 729 774 902 121 -25 -143 N ATOM 494 CA ASER A 65 6.443 10.133 14.911 0.70 6.92 C ANISOU 494 CA ASER A 65 774 858 995 89 -27 -127 C ATOM 495 C ASER A 65 4.927 10.205 14.829 0.70 6.56 C ANISOU 495 C ASER A 65 684 757 1049 79 -111 -102 C ATOM 496 O ASER A 65 4.286 9.746 13.876 0.70 8.00 O ANISOU 496 O ASER A 65 850 1031 1156 88 -182 -120 O ATOM 497 CB ASER A 65 7.060 11.234 14.082 0.70 7.80 C ANISOU 497 CB ASER A 65 916 841 1204 96 -66 -184 C ATOM 498 OG ASER A 65 6.663 11.117 12.738 0.70 9.06 O ANISOU 498 OG ASER A 65 1175 1078 1187 33 50 315 O ATOM 499 N PHE A 66 4.386 10.866 15.828 1.00 5.74 N ANISOU 499 N PHE A 66 664 734 782 -50 -83 -41 N ATOM 500 CA PHE A 66 2.952 11.073 15.971 1.00 5.74 C ANISOU 500 CA PHE A 66 700 727 752 -11 -79 51 C ATOM 501 C PHE A 66 2.747 12.571 15.852 1.00 5.80 C ANISOU 501 C PHE A 66 678 751 775 -3 -82 -27 C ATOM 502 O PHE A 66 3.264 13.329 16.660 1.00 6.71 O ANISOU 502 O PHE A 66 813 781 956 142 -289 -178 O ATOM 503 CB PHE A 66 2.476 10.513 17.301 1.00 6.66 C ANISOU 503 CB PHE A 66 819 912 798 30 26 34 C ATOM 504 CG PHE A 66 0.991 10.511 17.434 1.00 7.41 C ANISOU 504 CG PHE A 66 967 1051 796 66 74 152 C ATOM 505 CD1 PHE A 66 0.219 9.718 16.617 1.00 8.25 C ANISOU 505 CD1 PHE A 66 806 1153 1173 -141 150 419 C ATOM 506 CD2 PHE A 66 0.364 11.361 18.325 1.00 11.41 C ANISOU 506 CD2 PHE A 66 1010 2047 1277 120 -4 -102 C ATOM 507 CE1 PHE A 66 -1.168 9.727 16.724 1.00 10.04 C ANISOU 507 CE1 PHE A 66 1149 1257 1407 -110 -24 247 C ATOM 508 CE2 PHE A 66 -1.009 11.371 18.430 1.00 12.64 C ANISOU 508 CE2 PHE A 66 1058 2129 1615 30 348 -82 C ATOM 509 CZ PHE A 66 -1.760 10.555 17.608 1.00 12.09 C ANISOU 509 CZ PHE A 66 938 1939 1714 -69 168 96 C ATOM 510 N SER A 67 1.991 12.993 14.834 1.00 5.92 N ANISOU 510 N SER A 67 735 698 816 -66 -131 63 N ATOM 511 CA SER A 67 1.914 14.396 14.457 1.00 6.14 C ANISOU 511 CA SER A 67 778 691 862 -52 -79 81 C ATOM 512 C SER A 67 0.503 14.803 14.138 1.00 5.48 C ANISOU 512 C SER A 67 747 650 682 -85 -36 110 C ATOM 513 O SER A 67 -0.283 13.991 13.682 1.00 6.64 O ANISOU 513 O SER A 67 813 787 924 -168 -151 155 O ATOM 514 CB SER A 67 2.788 14.649 13.217 1.00 7.31 C ANISOU 514 CB SER A 67 797 785 1194 -32 -54 200 C ATOM 515 OG SER A 67 4.150 14.329 13.456 1.00 9.45 O ANISOU 515 OG SER A 67 936 1105 1549 3 59 187 O ATOM 516 N ARG A 68 0.212 16.080 14.319 1.00 6.59 N ANISOU 516 N ARG A 68 810 859 833 -17 -54 108 N ATOM 517 CA ARG A 68 -1.112 16.625 14.091 1.00 7.25 C ANISOU 517 CA ARG A 68 832 932 987 17 -8 58 C ATOM 518 C ARG A 68 -1.281 17.302 12.744 1.00 6.19 C ANISOU 518 C ARG A 68 774 775 802 77 15 -89 C ATOM 519 O ARG A 68 -0.319 17.651 12.081 1.00 6.61 O ANISOU 519 O ARG A 68 854 834 824 -67 -53 -34 O ATOM 520 CB ARG A 68 -1.502 17.589 15.229 1.00 9.60 C ANISOU 520 CB ARG A 68 1195 1245 1207 33 -65 116 C ATOM 521 CG ARG A 68 -0.730 18.910 15.271 1.00 13.36 C ANISOU 521 CG ARG A 68 1679 1759 1635 67 80 -22 C ATOM 522 CD ARG A 68 -0.836 19.685 16.598 1.00 16.60 C ANISOU 522 CD ARG A 68 2122 2085 2099 -62 94 -149 C ATOM 523 NE ARG A 68 -0.449 21.084 16.405 1.00 17.55 N ANISOU 523 NE ARG A 68 2588 2073 2005 -153 271 -354 N ATOM 524 CZ ARG A 68 -0.607 22.057 17.304 1.00 22.89 C ANISOU 524 CZ ARG A 68 3058 2785 2853 -116 218 -114 C ATOM 525 NH1 ARG A 68 -1.121 21.819 18.508 1.00 25.50 N ANISOU 525 NH1 ARG A 68 3235 3163 3289 -291 62 111 N ATOM 526 NH2 ARG A 68 -0.224 23.291 16.999 1.00 25.33 N ANISOU 526 NH2 ARG A 68 3330 3060 3231 -172 201 99 N ATOM 527 N LYS A 69 -2.537 17.497 12.362 1.00 6.68 N ANISOU 527 N LYS A 69 804 800 931 -74 36 -89 N ATOM 528 CA LYS A 69 -2.897 18.139 11.112 1.00 5.94 C ANISOU 528 CA LYS A 69 788 679 790 -28 -29 -174 C ATOM 529 C LYS A 69 -2.082 19.393 10.857 1.00 6.05 C ANISOU 529 C LYS A 69 783 680 834 0 -27 10 C ATOM 530 O LYS A 69 -1.901 20.226 11.731 1.00 6.67 O ANISOU 530 O LYS A 69 862 680 991 -91 -88 -49 O ATOM 531 CB LYS A 69 -4.379 18.507 11.114 1.00 6.97 C ANISOU 531 CB LYS A 69 974 755 916 -87 12 -168 C ATOM 532 CG LYS A 69 -4.916 18.906 9.757 1.00 8.90 C ANISOU 532 CG LYS A 69 1084 1057 1238 -63 -111 8 C ATOM 533 CD LYS A 69 -6.405 19.298 9.808 1.00 10.56 C ANISOU 533 CD LYS A 69 1312 1467 1233 64 -107 274 C ATOM 534 CE LYS A 69 -7.010 19.434 8.419 1.00 13.24 C ANISOU 534 CE LYS A 69 1297 2065 1668 228 -202 181 C ATOM 535 NZ LYS A 69 -8.468 19.769 8.470 1.00 19.91 N ANISOU 535 NZ LYS A 69 2279 2935 2350 254 60 -17 N ATOM 536 N ASN A 70 -1.626 19.509 9.620 1.00 6.20 N ANISOU 536 N ASN A 70 851 699 805 -8 0 -96 N ATOM 537 CA ASN A 70 -0.875 20.658 9.082 1.00 6.77 C ANISOU 537 CA ASN A 70 917 729 925 0 85 14 C ATOM 538 C ASN A 70 0.589 20.719 9.439 1.00 5.91 C ANISOU 538 C ASN A 70 847 686 711 -3 90 -36 C ATOM 539 O ASN A 70 1.303 21.516 8.850 1.00 6.35 O ANISOU 539 O ASN A 70 851 658 903 -109 -2 79 O ATOM 540 CB ASN A 70 -1.528 22.010 9.353 1.00 7.83 C ANISOU 540 CB ASN A 70 1010 843 1121 -27 17 13 C ATOM 541 CG ASN A 70 -2.874 22.127 8.731 1.00 10.18 C ANISOU 541 CG ASN A 70 1282 1064 1518 -23 30 127 C ATOM 542 OD1 ASN A 70 -3.119 21.649 7.638 1.00 11.74 O ANISOU 542 OD1 ASN A 70 1387 1037 2035 117 -268 207 O ATOM 543 ND2 ASN A 70 -3.776 22.831 9.427 1.00 12.74 N ANISOU 543 ND2 ASN A 70 1131 1342 2367 460 224 64 N ATOM 544 N VAL A 71 1.061 19.859 10.334 1.00 6.41 N ANISOU 544 N VAL A 71 782 890 762 -23 84 13 N ATOM 545 CA VAL A 71 2.497 19.701 10.554 1.00 5.80 C ANISOU 545 CA VAL A 71 805 766 631 -63 82 28 C ATOM 546 C VAL A 71 3.132 19.355 9.219 1.00 5.83 C ANISOU 546 C VAL A 71 790 772 653 -36 30 -43 C ATOM 547 O VAL A 71 2.645 18.485 8.479 1.00 6.28 O ANISOU 547 O VAL A 71 934 632 819 -58 44 -23 O ATOM 548 CB VAL A 71 2.785 18.637 11.623 1.00 6.20 C ANISOU 548 CB VAL A 71 829 874 653 -35 96 9 C ATOM 549 CG1 VAL A 71 4.239 18.172 11.562 1.00 7.90 C ANISOU 549 CG1 VAL A 71 1065 1057 877 -25 -97 141 C ATOM 550 CG2 VAL A 71 2.466 19.196 12.981 1.00 7.23 C ANISOU 550 CG2 VAL A 71 1006 1061 681 -132 2 73 C ATOM 551 N LEU A 72 4.230 20.036 8.917 1.00 5.93 N ANISOU 551 N LEU A 72 826 815 611 -32 72 -58 N ATOM 552 CA LEU A 72 4.923 19.863 7.659 1.00 5.85 C ANISOU 552 CA LEU A 72 797 730 693 -43 136 -99 C ATOM 553 C LEU A 72 6.394 19.733 8.022 1.00 6.33 C ANISOU 553 C LEU A 72 817 789 799 1 83 -72 C ATOM 554 O LEU A 72 6.982 20.648 8.610 1.00 7.44 O ANISOU 554 O LEU A 72 823 1003 1002 -69 88 -88 O ATOM 555 CB LEU A 72 4.641 21.066 6.771 1.00 6.01 C ANISOU 555 CB LEU A 72 823 887 571 -94 70 -34 C ATOM 556 CG LEU A 72 5.083 20.991 5.311 1.00 7.40 C ANISOU 556 CG LEU A 72 1043 1108 660 -243 39 45 C ATOM 557 CD1 LEU A 72 4.444 22.120 4.534 1.00 8.44 C ANISOU 557 CD1 LEU A 72 1045 1442 717 -204 -51 51 C ATOM 558 CD2 LEU A 72 6.586 20.976 5.145 1.00 8.01 C ANISOU 558 CD2 LEU A 72 1204 1049 790 48 45 161 C ATOM 559 N AARG A 73 6.967 18.556 7.729 0.70 6.31 N ANISOU 559 N AARG A 73 877 717 801 -38 72 -135 N ATOM 560 CA AARG A 73 8.359 18.223 8.006 0.70 7.38 C ANISOU 560 CA AARG A 73 962 971 869 -55 54 -98 C ATOM 561 C AARG A 73 9.084 18.011 6.680 0.70 6.57 C ANISOU 561 C AARG A 73 785 928 783 -77 11 -126 C ATOM 562 O AARG A 73 8.539 17.404 5.748 0.70 7.66 O ANISOU 562 O AARG A 73 957 1011 940 -170 56 -99 O ATOM 563 CB AARG A 73 8.450 16.935 8.845 0.70 8.72 C ANISOU 563 CB AARG A 73 1061 1224 1026 -58 29 -19 C ATOM 564 CG AARG A 73 7.692 16.957 10.148 0.70 9.66 C ANISOU 564 CG AARG A 73 1107 1304 1256 49 -18 -15 C ATOM 565 CD AARG A 73 8.212 17.969 11.126 0.70 11.72 C ANISOU 565 CD AARG A 73 1607 1432 1414 -40 78 255 C ATOM 566 NE AARG A 73 7.513 17.922 12.413 0.70 12.79 N ANISOU 566 NE AARG A 73 1685 1872 1301 -61 127 183 N ATOM 567 CZ AARG A 73 7.242 18.995 13.159 0.70 13.80 C ANISOU 567 CZ AARG A 73 1942 1977 1325 -64 65 16 C ATOM 568 NH1AARG A 73 7.597 20.197 12.740 0.70 15.96 N ANISOU 568 NH1AARG A 73 2201 2251 1610 -388 58 -24 N ATOM 569 NH2AARG A 73 6.613 18.867 14.335 0.70 13.82 N ANISOU 569 NH2AARG A 73 1911 2150 1188 -137 137 -138 N ATOM 570 N GLY A 74 10.319 18.510 6.590 1.00 7.01 N ANISOU 570 N GLY A 74 895 936 831 -111 -27 -69 N ATOM 571 CA GLY A 74 11.159 18.228 5.451 1.00 7.45 C ANISOU 571 CA GLY A 74 924 990 916 -61 35 -35 C ATOM 572 C GLY A 74 11.835 19.477 4.926 1.00 6.70 C ANISOU 572 C GLY A 74 873 957 714 -28 -20 50 C ATOM 573 O GLY A 74 11.694 20.541 5.521 1.00 7.42 O ANISOU 573 O GLY A 74 1138 906 774 -107 -69 -36 O ATOM 574 N LEU A 75 12.568 19.396 3.827 1.00 6.32 N ANISOU 574 N LEU A 75 867 877 658 -76 38 -7 N ATOM 575 CA LEU A 75 12.808 18.183 3.049 1.00 6.41 C ANISOU 575 CA LEU A 75 812 828 794 -90 21 67 C ATOM 576 C LEU A 75 14.225 17.724 3.346 1.00 6.33 C ANISOU 576 C LEU A 75 822 807 773 -17 25 69 C ATOM 577 O LEU A 75 15.174 18.470 3.151 1.00 7.05 O ANISOU 577 O LEU A 75 723 989 965 -11 4 231 O ATOM 578 CB LEU A 75 12.618 18.500 1.563 1.00 6.12 C ANISOU 578 CB LEU A 75 767 725 831 -2 -1 78 C ATOM 579 CG LEU A 75 11.176 18.787 1.179 1.00 6.25 C ANISOU 579 CG LEU A 75 748 859 765 -98 -42 104 C ATOM 580 CD1 LEU A 75 11.059 19.626 -0.070 1.00 7.25 C ANISOU 580 CD1 LEU A 75 921 942 891 121 -44 120 C ATOM 581 CD2 LEU A 75 10.396 17.493 0.982 1.00 8.03 C ANISOU 581 CD2 LEU A 75 768 1129 1150 -6 -29 258 C ATOM 582 N HIS A 76 14.365 16.520 3.896 1.00 6.28 N ANISOU 582 N HIS A 76 786 724 875 39 -76 54 N ATOM 583 CA HIS A 76 15.629 16.025 4.417 1.00 6.87 C ANISOU 583 CA HIS A 76 885 939 784 49 -120 68 C ATOM 584 C HIS A 76 16.099 14.778 3.673 1.00 6.74 C ANISOU 584 C HIS A 76 801 872 885 29 -73 186 C ATOM 585 O HIS A 76 15.349 13.800 3.576 1.00 6.89 O ANISOU 585 O HIS A 76 806 856 954 -94 -58 184 O ATOM 586 CB HIS A 76 15.493 15.611 5.898 1.00 8.27 C ANISOU 586 CB HIS A 76 1200 1037 904 155 -68 87 C ATOM 587 CG HIS A 76 14.826 16.607 6.798 1.00 10.53 C ANISOU 587 CG HIS A 76 1646 1524 830 103 65 273 C ATOM 588 ND1 HIS A 76 14.341 16.253 8.036 1.00 15.41 N ANISOU 588 ND1 HIS A 76 2671 1714 1469 336 594 -89 N ATOM 589 CD2 HIS A 76 14.633 17.933 6.692 1.00 9.92 C ANISOU 589 CD2 HIS A 76 1552 1472 743 313 195 -92 C ATOM 590 CE1 HIS A 76 13.823 17.314 8.629 1.00 16.21 C ANISOU 590 CE1 HIS A 76 2493 1985 1678 319 612 -49 C ATOM 591 NE2 HIS A 76 13.961 18.342 7.819 1.00 11.98 N ANISOU 591 NE2 HIS A 76 1921 1504 1125 331 208 172 N ATOM 592 N ALA A 77 17.313 14.800 3.152 1.00 6.81 N ANISOU 592 N ALA A 77 851 687 1049 6 -48 93 N ATOM 593 CA ALA A 77 17.983 13.629 2.596 1.00 7.64 C ANISOU 593 CA ALA A 77 911 838 1153 1 -34 72 C ATOM 594 C ALA A 77 18.986 13.164 3.639 1.00 8.40 C ANISOU 594 C ALA A 77 1065 808 1317 -46 -86 206 C ATOM 595 O ALA A 77 20.106 13.630 3.687 1.00 9.73 O ANISOU 595 O ALA A 77 1179 1079 1436 -77 -332 325 O ATOM 596 CB ALA A 77 18.697 13.979 1.296 1.00 8.09 C ANISOU 596 CB ALA A 77 917 885 1271 -2 -30 98 C ATOM 597 N GLU A 78 18.557 12.247 4.508 1.00 9.85 N ANISOU 597 N GLU A 78 1130 1111 1499 -43 -149 350 N ATOM 598 CA GLU A 78 19.417 11.682 5.540 1.00 10.52 C ANISOU 598 CA GLU A 78 1297 1189 1507 -9 -74 185 C ATOM 599 C GLU A 78 20.286 10.597 4.901 1.00 10.16 C ANISOU 599 C GLU A 78 1278 1063 1518 -82 -166 241 C ATOM 600 O GLU A 78 19.923 10.012 3.885 1.00 10.83 O ANISOU 600 O GLU A 78 1663 908 1543 57 -321 319 O ATOM 601 CB GLU A 78 18.556 11.156 6.703 1.00 11.20 C ANISOU 601 CB GLU A 78 1416 1207 1630 48 -20 217 C ATOM 602 CG GLU A 78 17.726 12.238 7.392 1.00 13.82 C ANISOU 602 CG GLU A 78 1628 1669 1951 47 129 307 C ATOM 603 CD GLU A 78 17.074 11.757 8.673 1.00 15.20 C ANISOU 603 CD GLU A 78 1709 2056 2011 -75 -8 206 C ATOM 604 OE1 GLU A 78 16.437 10.676 8.643 1.00 17.14 O ANISOU 604 OE1 GLU A 78 1520 2374 2617 -188 -189 753 O ATOM 605 OE2 GLU A 78 17.182 12.454 9.700 1.00 19.41 O ANISOU 605 OE2 GLU A 78 2288 2494 2590 -19 449 215 O ATOM 606 N PRO A 79 21.439 10.309 5.485 1.00 10.00 N ANISOU 606 N PRO A 79 1207 990 1600 -91 -202 167 N ATOM 607 CA PRO A 79 22.401 9.415 4.835 1.00 10.80 C ANISOU 607 CA PRO A 79 1257 1139 1708 -164 -161 108 C ATOM 608 C PRO A 79 22.146 7.915 5.037 1.00 10.20 C ANISOU 608 C PRO A 79 1257 985 1632 -94 -226 181 C ATOM 609 O PRO A 79 23.028 7.183 5.442 1.00 12.05 O ANISOU 609 O PRO A 79 1447 1027 2104 -74 -450 228 O ATOM 610 CB PRO A 79 23.743 9.878 5.433 1.00 11.07 C ANISOU 610 CB PRO A 79 1357 1078 1771 -108 -259 113 C ATOM 611 CG PRO A 79 23.378 10.423 6.756 1.00 11.66 C ANISOU 611 CG PRO A 79 1286 1382 1762 -42 -283 156 C ATOM 612 CD PRO A 79 21.984 10.927 6.703 1.00 11.48 C ANISOU 612 CD PRO A 79 1296 1352 1714 -105 -147 119 C ATOM 613 N TRP A 80 20.920 7.487 4.764 1.00 9.16 N ANISOU 613 N TRP A 80 1073 906 1499 -60 -229 52 N ATOM 614 CA TRP A 80 20.487 6.093 4.852 1.00 8.71 C ANISOU 614 CA TRP A 80 1093 926 1289 -131 -121 61 C ATOM 615 C TRP A 80 19.258 5.926 4.003 1.00 7.63 C ANISOU 615 C TRP A 80 932 808 1159 -98 -85 85 C ATOM 616 O TRP A 80 18.611 6.903 3.637 1.00 8.61 O ANISOU 616 O TRP A 80 1027 793 1450 -119 -305 77 O ATOM 617 CB TRP A 80 20.220 5.677 6.320 1.00 8.76 C ANISOU 617 CB TRP A 80 1112 928 1285 -177 -242 75 C ATOM 618 CG TRP A 80 19.576 6.690 7.192 1.00 9.28 C ANISOU 618 CG TRP A 80 1287 933 1304 -163 -221 126 C ATOM 619 CD1 TRP A 80 18.275 7.073 7.197 1.00 9.13 C ANISOU 619 CD1 TRP A 80 1128 1053 1287 -544 -272 202 C ATOM 620 CD2 TRP A 80 20.219 7.462 8.227 1.00 8.38 C ANISOU 620 CD2 TRP A 80 1151 753 1278 -220 -227 18 C ATOM 621 NE1 TRP A 80 18.061 8.039 8.143 1.00 10.02 N ANISOU 621 NE1 TRP A 80 1101 1341 1365 -144 -71 309 N ATOM 622 CE2 TRP A 80 19.240 8.294 8.793 1.00 8.51 C ANISOU 622 CE2 TRP A 80 1010 1015 1206 -269 -68 262 C ATOM 623 CE3 TRP A 80 21.524 7.539 8.715 1.00 10.05 C ANISOU 623 CE3 TRP A 80 1384 965 1469 -117 -230 -56 C ATOM 624 CZ2 TRP A 80 19.516 9.178 9.829 1.00 9.31 C ANISOU 624 CZ2 TRP A 80 1232 1054 1250 -150 -2 209 C ATOM 625 CZ3 TRP A 80 21.797 8.407 9.762 1.00 9.24 C ANISOU 625 CZ3 TRP A 80 1416 816 1276 29 -310 -89 C ATOM 626 CH2 TRP A 80 20.791 9.209 10.309 1.00 9.79 C ANISOU 626 CH2 TRP A 80 1358 903 1458 -74 -133 -11 C ATOM 627 N ASP A 81 18.923 4.677 3.706 1.00 6.88 N ANISOU 627 N ASP A 81 861 827 924 -63 -19 -54 N ATOM 628 CA ASP A 81 17.703 4.339 3.003 1.00 6.41 C ANISOU 628 CA ASP A 81 841 813 781 -29 -9 16 C ATOM 629 C ASP A 81 16.538 4.324 3.999 1.00 6.45 C ANISOU 629 C ASP A 81 827 904 719 -135 -23 35 C ATOM 630 O ASP A 81 16.735 4.122 5.207 1.00 7.28 O ANISOU 630 O ASP A 81 853 1172 738 -207 -84 84 O ATOM 631 CB ASP A 81 17.830 2.955 2.348 1.00 6.11 C ANISOU 631 CB ASP A 81 868 683 767 -101 6 -6 C ATOM 632 CG ASP A 81 18.980 2.848 1.411 1.00 8.10 C ANISOU 632 CG ASP A 81 1349 866 860 192 141 145 C ATOM 633 OD1 ASP A 81 19.157 3.730 0.553 1.00 9.06 O ANISOU 633 OD1 ASP A 81 1504 921 1015 111 339 166 O ATOM 634 OD2 ASP A 81 19.758 1.878 1.525 1.00 12.30 O ANISOU 634 OD2 ASP A 81 2162 1485 1026 538 344 334 O ATOM 635 N LYS A 82 15.324 4.499 3.480 1.00 6.60 N ANISOU 635 N LYS A 82 819 1087 600 -123 86 102 N ATOM 636 CA LYS A 82 14.135 4.552 4.313 1.00 7.08 C ANISOU 636 CA LYS A 82 856 1027 805 -74 43 53 C ATOM 637 C LYS A 82 12.964 3.812 3.678 1.00 6.54 C ANISOU 637 C LYS A 82 796 997 692 -73 20 65 C ATOM 638 O LYS A 82 12.735 3.893 2.469 1.00 8.37 O ANISOU 638 O LYS A 82 928 1423 828 -304 30 139 O ATOM 639 CB LYS A 82 13.682 5.995 4.494 1.00 8.58 C ANISOU 639 CB LYS A 82 1074 1165 1021 -109 38 61 C ATOM 640 CG LYS A 82 14.573 6.893 5.237 1.00 10.61 C ANISOU 640 CG LYS A 82 1398 1339 1293 -25 31 47 C ATOM 641 CD LYS A 82 13.920 8.252 5.573 1.00 12.16 C ANISOU 641 CD LYS A 82 1753 1247 1618 -20 -68 -47 C ATOM 642 CE LYS A 82 14.756 8.917 6.593 1.00 13.83 C ANISOU 642 CE LYS A 82 1848 1866 1539 110 63 39 C ATOM 643 NZ LYS A 82 14.318 10.277 6.877 1.00 12.98 N ANISOU 643 NZ LYS A 82 1728 1499 1701 190 138 142 N ATOM 644 N TYR A 83 12.187 3.137 4.516 1.00 5.97 N ANISOU 644 N TYR A 83 735 940 590 -40 -16 77 N ATOM 645 CA TYR A 83 10.914 2.554 4.132 1.00 5.77 C ANISOU 645 CA TYR A 83 696 868 629 -28 6 -37 C ATOM 646 C TYR A 83 9.860 3.233 4.995 1.00 6.02 C ANISOU 646 C TYR A 83 725 886 676 48 -14 -72 C ATOM 647 O TYR A 83 9.865 3.093 6.221 1.00 7.41 O ANISOU 647 O TYR A 83 869 1317 628 117 10 -83 O ATOM 648 CB TYR A 83 10.905 1.047 4.358 1.00 6.45 C ANISOU 648 CB TYR A 83 782 946 722 -46 -70 17 C ATOM 649 CG TYR A 83 9.590 0.399 4.037 1.00 6.02 C ANISOU 649 CG TYR A 83 828 725 733 -63 -80 -7 C ATOM 650 CD1 TYR A 83 9.160 0.263 2.740 1.00 6.51 C ANISOU 650 CD1 TYR A 83 824 918 729 -58 31 -46 C ATOM 651 CD2 TYR A 83 8.774 -0.098 5.034 1.00 7.37 C ANISOU 651 CD2 TYR A 83 986 1060 754 -230 -163 101 C ATOM 652 CE1 TYR A 83 7.978 -0.360 2.452 1.00 7.56 C ANISOU 652 CE1 TYR A 83 1044 1018 811 -205 -99 98 C ATOM 653 CE2 TYR A 83 7.562 -0.713 4.748 1.00 8.52 C ANISOU 653 CE2 TYR A 83 1007 1203 1026 -333 -152 357 C ATOM 654 CZ TYR A 83 7.184 -0.845 3.448 1.00 7.50 C ANISOU 654 CZ TYR A 83 838 952 1060 -283 -279 256 C ATOM 655 OH TYR A 83 6.020 -1.473 3.099 1.00 9.67 O ANISOU 655 OH TYR A 83 1113 1193 1366 -488 -381 410 O ATOM 656 N ILE A 84 8.991 3.989 4.359 1.00 6.25 N ANISOU 656 N ILE A 84 819 951 601 4 77 -79 N ATOM 657 CA ILE A 84 8.043 4.871 5.026 1.00 6.69 C ANISOU 657 CA ILE A 84 811 940 791 16 44 -55 C ATOM 658 C ILE A 84 6.635 4.310 4.953 1.00 5.96 C ANISOU 658 C ILE A 84 760 820 682 76 84 -56 C ATOM 659 O ILE A 84 6.177 3.898 3.893 1.00 6.09 O ANISOU 659 O ILE A 84 818 754 740 51 53 27 O ATOM 660 CB ILE A 84 8.052 6.260 4.355 1.00 7.85 C ANISOU 660 CB ILE A 84 857 1021 1105 48 141 -132 C ATOM 661 CG1 ILE A 84 9.488 6.803 4.359 1.00 12.77 C ANISOU 661 CG1 ILE A 84 1253 1577 2019 -38 184 -114 C ATOM 662 CG2 ILE A 84 7.030 7.178 4.989 1.00 9.92 C ANISOU 662 CG2 ILE A 84 1217 1024 1529 42 121 -76 C ATOM 663 CD1 ILE A 84 9.895 7.591 5.448 1.00 17.81 C ANISOU 663 CD1 ILE A 84 1926 2448 2391 82 -101 42 C ATOM 664 N SER A 85 5.946 4.372 6.086 1.00 6.33 N ANISOU 664 N SER A 85 707 1029 668 0 65 -14 N ATOM 665 CA SER A 85 4.597 3.875 6.171 1.00 6.24 C ANISOU 665 CA SER A 85 760 888 723 -62 141 28 C ATOM 666 C SER A 85 3.789 4.669 7.187 1.00 6.10 C ANISOU 666 C SER A 85 785 848 683 -88 88 32 C ATOM 667 O SER A 85 4.335 5.456 7.956 1.00 6.86 O ANISOU 667 O SER A 85 807 887 912 -17 59 -22 O ATOM 668 CB SER A 85 4.623 2.421 6.554 1.00 7.73 C ANISOU 668 CB SER A 85 910 1064 961 -82 156 -66 C ATOM 669 OG SER A 85 5.067 2.178 7.877 1.00 9.22 O ANISOU 669 OG SER A 85 1406 1141 956 -118 151 60 O ATOM 670 N VAL A 86 2.485 4.407 7.207 1.00 5.85 N ANISOU 670 N VAL A 86 690 788 741 -53 29 -31 N ATOM 671 CA VAL A 86 1.573 4.933 8.197 1.00 5.49 C ANISOU 671 CA VAL A 86 665 741 679 -31 25 22 C ATOM 672 C VAL A 86 0.948 3.788 8.982 1.00 5.31 C ANISOU 672 C VAL A 86 616 730 669 -12 -26 20 C ATOM 673 O VAL A 86 0.468 2.818 8.397 1.00 6.41 O ANISOU 673 O VAL A 86 849 765 820 -13 -32 -83 O ATOM 674 CB VAL A 86 0.507 5.807 7.532 1.00 6.07 C ANISOU 674 CB VAL A 86 755 820 730 -45 24 20 C ATOM 675 CG1 VAL A 86 -0.652 6.103 8.454 1.00 6.75 C ANISOU 675 CG1 VAL A 86 734 963 867 0 25 34 C ATOM 676 CG2 VAL A 86 1.139 7.084 7.051 1.00 7.36 C ANISOU 676 CG2 VAL A 86 917 946 932 -20 30 157 C ATOM 677 N ALA A 87 0.993 3.894 10.309 1.00 5.61 N ANISOU 677 N ALA A 87 799 647 685 -18 -79 -60 N ATOM 678 CA ALA A 87 0.585 2.817 11.203 1.00 6.29 C ANISOU 678 CA ALA A 87 804 759 824 -42 -55 77 C ATOM 679 C ALA A 87 -0.820 2.940 11.757 1.00 6.26 C ANISOU 679 C ALA A 87 728 690 959 -20 -11 94 C ATOM 680 O ALA A 87 -1.320 1.996 12.323 1.00 7.40 O ANISOU 680 O ALA A 87 889 709 1212 -13 -62 226 O ATOM 681 CB ALA A 87 1.563 2.673 12.320 1.00 6.75 C ANISOU 681 CB ALA A 87 832 889 841 78 -51 176 C ATOM 682 N ASP A 88 -1.448 4.106 11.617 1.00 6.16 N ANISOU 682 N ASP A 88 645 754 941 -25 -40 129 N ATOM 683 CA ASP A 88 -2.790 4.305 12.093 1.00 6.65 C ANISOU 683 CA ASP A 88 870 792 862 -29 42 72 C ATOM 684 C ASP A 88 -3.718 4.647 10.946 1.00 5.18 C ANISOU 684 C ASP A 88 650 529 789 -52 40 92 C ATOM 685 O ASP A 88 -3.423 4.355 9.794 1.00 6.77 O ANISOU 685 O ASP A 88 963 812 796 -32 -46 122 O ATOM 686 CB ASP A 88 -2.844 5.296 13.257 1.00 6.08 C ANISOU 686 CB ASP A 88 806 719 783 -145 -48 132 C ATOM 687 CG ASP A 88 -2.566 6.718 12.865 1.00 6.12 C ANISOU 687 CG ASP A 88 858 769 695 -29 -73 43 C ATOM 688 OD1 ASP A 88 -2.178 6.965 11.706 1.00 6.66 O ANISOU 688 OD1 ASP A 88 960 756 812 -159 43 209 O ATOM 689 OD2 ASP A 88 -2.720 7.632 13.730 1.00 7.66 O ANISOU 689 OD2 ASP A 88 991 967 952 -144 2 16 O ATOM 690 N GLY A 89 -4.862 5.244 11.252 1.00 5.56 N ANISOU 690 N GLY A 89 726 628 758 -46 114 84 N ATOM 691 CA GLY A 89 -5.825 5.592 10.234 1.00 6.33 C ANISOU 691 CA GLY A 89 666 741 997 -29 48 144 C ATOM 692 C GLY A 89 -5.586 6.934 9.565 1.00 6.15 C ANISOU 692 C GLY A 89 715 721 899 -46 -2 111 C ATOM 693 O GLY A 89 -6.440 7.417 8.829 1.00 8.41 O ANISOU 693 O GLY A 89 937 951 1307 15 -110 196 O ATOM 694 N GLY A 90 -4.457 7.574 9.832 1.00 5.94 N ANISOU 694 N GLY A 90 829 630 798 -19 -23 39 N ATOM 695 CA GLY A 90 -4.182 8.894 9.291 1.00 6.00 C ANISOU 695 CA GLY A 90 854 668 755 60 -6 53 C ATOM 696 C GLY A 90 -3.625 8.891 7.897 1.00 5.54 C ANISOU 696 C GLY A 90 720 628 754 7 57 63 C ATOM 697 O GLY A 90 -3.499 7.855 7.241 1.00 5.98 O ANISOU 697 O GLY A 90 884 639 747 2 1 102 O ATOM 698 N LYS A 91 -3.249 10.073 7.434 1.00 6.09 N ANISOU 698 N LYS A 91 919 632 762 34 104 8 N ATOM 699 CA LYS A 91 -2.697 10.205 6.114 1.00 6.94 C ANISOU 699 CA LYS A 91 974 744 917 20 54 12 C ATOM 700 C LYS A 91 -1.849 11.441 6.012 1.00 5.80 C ANISOU 700 C LYS A 91 849 540 814 0 53 58 C ATOM 701 O LYS A 91 -2.102 12.444 6.671 1.00 6.26 O ANISOU 701 O LYS A 91 893 564 922 -48 145 -69 O ATOM 702 CB LYS A 91 -3.759 10.196 5.037 1.00 9.34 C ANISOU 702 CB LYS A 91 1217 1127 1202 -201 129 101 C ATOM 703 CG LYS A 91 -4.770 11.200 5.160 1.00 12.33 C ANISOU 703 CG LYS A 91 1622 1447 1613 -146 -40 -57 C ATOM 704 CD LYS A 91 -5.709 11.182 3.969 1.00 15.20 C ANISOU 704 CD LYS A 91 1841 1955 1979 0 -55 76 C ATOM 705 CE LYS A 91 -6.825 12.187 4.108 1.00 18.11 C ANISOU 705 CE LYS A 91 2223 2285 2372 0 -170 51 C ATOM 706 NZ LYS A 91 -7.784 12.096 2.946 1.00 19.53 N ANISOU 706 NZ LYS A 91 2250 2711 2459 -19 -316 239 N ATOM 707 N VAL A 92 -0.827 11.365 5.172 1.00 5.78 N ANISOU 707 N VAL A 92 862 534 800 0 84 16 N ATOM 708 CA VAL A 92 0.048 12.482 4.870 1.00 5.76 C ANISOU 708 CA VAL A 92 845 552 790 -23 69 -1 C ATOM 709 C VAL A 92 0.202 12.667 3.384 1.00 5.82 C ANISOU 709 C VAL A 92 841 575 794 -80 32 17 C ATOM 710 O VAL A 92 0.052 11.729 2.606 1.00 6.45 O ANISOU 710 O VAL A 92 1019 643 788 -71 99 -1 O ATOM 711 CB VAL A 92 1.455 12.323 5.527 1.00 5.96 C ANISOU 711 CB VAL A 92 875 629 759 -45 74 75 C ATOM 712 CG1 VAL A 92 1.352 12.075 7.018 1.00 6.29 C ANISOU 712 CG1 VAL A 92 875 675 838 -35 73 11 C ATOM 713 CG2 VAL A 92 2.257 11.244 4.869 1.00 6.66 C ANISOU 713 CG2 VAL A 92 871 791 869 -4 68 19 C ATOM 714 N LEU A 93 0.537 13.899 3.015 1.00 5.20 N ANISOU 714 N LEU A 93 829 545 601 -61 144 -38 N ATOM 715 CA LEU A 93 1.011 14.202 1.667 1.00 6.00 C ANISOU 715 CA LEU A 93 862 656 758 -3 25 16 C ATOM 716 C LEU A 93 2.519 13.995 1.658 1.00 5.86 C ANISOU 716 C LEU A 93 857 613 756 -46 -21 3 C ATOM 717 O LEU A 93 3.273 14.799 2.199 1.00 8.24 O ANISOU 717 O LEU A 93 967 743 1420 -32 -276 -158 O ATOM 718 CB LEU A 93 0.646 15.620 1.285 1.00 6.11 C ANISOU 718 CB LEU A 93 865 653 802 24 55 -49 C ATOM 719 CG LEU A 93 1.145 16.101 -0.065 1.00 7.92 C ANISOU 719 CG LEU A 93 1056 890 1062 135 1 165 C ATOM 720 CD1 LEU A 93 0.630 15.248 -1.215 1.00 9.72 C ANISOU 720 CD1 LEU A 93 1496 1210 986 241 66 261 C ATOM 721 CD2 LEU A 93 0.781 17.558 -0.250 1.00 8.96 C ANISOU 721 CD2 LEU A 93 1277 1010 1117 53 37 320 C ATOM 722 N GLY A 94 2.948 12.870 1.129 1.00 5.78 N ANISOU 722 N GLY A 94 775 616 802 -92 50 65 N ATOM 723 CA GLY A 94 4.357 12.559 1.033 1.00 6.08 C ANISOU 723 CA GLY A 94 783 779 745 -44 82 7 C ATOM 724 C GLY A 94 4.979 13.282 -0.136 1.00 5.91 C ANISOU 724 C GLY A 94 815 726 704 -1 65 43 C ATOM 725 O GLY A 94 4.365 13.413 -1.187 1.00 6.10 O ANISOU 725 O GLY A 94 775 879 661 -26 127 -30 O ATOM 726 N THR A 95 6.197 13.770 0.079 1.00 5.50 N ANISOU 726 N THR A 95 756 797 534 -17 71 70 N ATOM 727 CA THR A 95 6.873 14.634 -0.877 1.00 5.42 C ANISOU 727 CA THR A 95 738 705 614 35 71 43 C ATOM 728 C THR A 95 8.351 14.308 -0.926 1.00 4.91 C ANISOU 728 C THR A 95 679 676 509 -7 33 96 C ATOM 729 O THR A 95 8.991 14.209 0.116 1.00 6.03 O ANISOU 729 O THR A 95 808 900 582 39 13 23 O ATOM 730 CB THR A 95 6.687 16.089 -0.457 1.00 6.17 C ANISOU 730 CB THR A 95 839 737 765 56 -11 10 C ATOM 731 OG1 THR A 95 5.282 16.375 -0.431 1.00 6.85 O ANISOU 731 OG1 THR A 95 837 841 925 236 36 -43 O ATOM 732 CG2 THR A 95 7.351 17.072 -1.441 1.00 7.31 C ANISOU 732 CG2 THR A 95 1119 826 829 102 -122 -15 C ATOM 733 N TRP A 96 8.871 14.190 -2.152 1.00 5.51 N ANISOU 733 N TRP A 96 719 793 580 74 39 59 N ATOM 734 CA TRP A 96 10.265 13.816 -2.382 1.00 5.54 C ANISOU 734 CA TRP A 96 760 755 589 123 -2 -15 C ATOM 735 C TRP A 96 10.895 14.714 -3.427 1.00 6.32 C ANISOU 735 C TRP A 96 832 867 700 83 -31 -47 C ATOM 736 O TRP A 96 10.267 15.066 -4.425 1.00 6.37 O ANISOU 736 O TRP A 96 827 976 617 29 154 163 O ATOM 737 CB TRP A 96 10.379 12.328 -2.777 1.00 5.98 C ANISOU 737 CB TRP A 96 838 749 682 107 71 79 C ATOM 738 CG TRP A 96 9.851 11.489 -1.695 1.00 5.45 C ANISOU 738 CG TRP A 96 685 656 728 90 151 140 C ATOM 739 CD1 TRP A 96 10.511 11.094 -0.570 1.00 7.06 C ANISOU 739 CD1 TRP A 96 905 699 1076 5 -23 67 C ATOM 740 CD2 TRP A 96 8.497 11.033 -1.549 1.00 6.13 C ANISOU 740 CD2 TRP A 96 870 615 844 53 122 53 C ATOM 741 NE1 TRP A 96 9.656 10.403 0.249 1.00 6.68 N ANISOU 741 NE1 TRP A 96 955 730 854 78 -55 246 N ATOM 742 CE2 TRP A 96 8.408 10.375 -0.320 1.00 6.66 C ANISOU 742 CE2 TRP A 96 932 575 1023 164 -3 82 C ATOM 743 CE3 TRP A 96 7.350 11.137 -2.340 1.00 5.92 C ANISOU 743 CE3 TRP A 96 887 472 889 18 114 73 C ATOM 744 CZ2 TRP A 96 7.217 9.816 0.148 1.00 7.10 C ANISOU 744 CZ2 TRP A 96 1174 738 784 -6 134 124 C ATOM 745 CZ3 TRP A 96 6.180 10.572 -1.886 1.00 6.08 C ANISOU 745 CZ3 TRP A 96 815 589 906 12 -9 10 C ATOM 746 CH2 TRP A 96 6.124 9.910 -0.655 1.00 7.16 C ANISOU 746 CH2 TRP A 96 1000 570 1151 60 75 95 C ATOM 747 N VAL A 97 12.152 15.070 -3.181 1.00 5.28 N ANISOU 747 N VAL A 97 689 735 579 -56 38 14 N ATOM 748 CA VAL A 97 12.983 15.793 -4.140 1.00 5.63 C ANISOU 748 CA VAL A 97 706 722 711 -42 50 57 C ATOM 749 C VAL A 97 14.330 15.089 -4.212 1.00 5.66 C ANISOU 749 C VAL A 97 723 756 668 -33 57 4 C ATOM 750 O VAL A 97 15.013 14.939 -3.203 1.00 5.99 O ANISOU 750 O VAL A 97 761 785 729 -4 34 47 O ATOM 751 CB VAL A 97 13.197 17.262 -3.721 1.00 6.58 C ANISOU 751 CB VAL A 97 839 912 749 25 106 15 C ATOM 752 CG1 VAL A 97 14.032 17.995 -4.745 1.00 7.15 C ANISOU 752 CG1 VAL A 97 822 920 973 92 107 18 C ATOM 753 CG2 VAL A 97 11.861 17.962 -3.527 1.00 7.67 C ANISOU 753 CG2 VAL A 97 1090 913 909 1 52 126 C ATOM 754 N ASP A 98 14.731 14.674 -5.400 1.00 5.57 N ANISOU 754 N ASP A 98 739 683 693 54 13 2 N ATOM 755 CA ASP A 98 15.991 13.956 -5.568 1.00 5.63 C ANISOU 755 CA ASP A 98 712 683 742 -15 41 65 C ATOM 756 C ASP A 98 17.133 14.959 -5.422 1.00 5.78 C ANISOU 756 C ASP A 98 707 734 753 22 90 60 C ATOM 757 O ASP A 98 17.189 15.919 -6.174 1.00 6.36 O ANISOU 757 O ASP A 98 871 783 760 52 -8 -54 O ATOM 758 CB ASP A 98 15.988 13.311 -6.946 1.00 6.30 C ANISOU 758 CB ASP A 98 801 668 921 -41 -32 1 C ATOM 759 CG ASP A 98 17.038 12.266 -7.138 1.00 7.21 C ANISOU 759 CG ASP A 98 1037 919 780 108 -14 -16 C ATOM 760 OD1 ASP A 98 18.044 12.242 -6.397 1.00 6.99 O ANISOU 760 OD1 ASP A 98 848 706 1101 144 10 -125 O ATOM 761 OD2 ASP A 98 16.903 11.431 -8.068 1.00 6.89 O ANISOU 761 OD2 ASP A 98 983 700 934 -55 56 -140 O ATOM 762 N LEU A 99 18.018 14.736 -4.458 1.00 5.48 N ANISOU 762 N LEU A 99 668 694 719 -121 67 36 N ATOM 763 CA LEU A 99 19.193 15.612 -4.281 1.00 5.53 C ANISOU 763 CA LEU A 99 665 740 696 -36 -31 55 C ATOM 764 C LEU A 99 20.513 14.973 -4.720 1.00 5.24 C ANISOU 764 C LEU A 99 632 663 695 -90 23 107 C ATOM 765 O LEU A 99 21.586 15.499 -4.436 1.00 6.48 O ANISOU 765 O LEU A 99 644 802 1014 1 16 -69 O ATOM 766 CB LEU A 99 19.272 16.132 -2.839 1.00 5.79 C ANISOU 766 CB LEU A 99 680 733 785 -79 42 -3 C ATOM 767 CG LEU A 99 18.064 16.943 -2.386 1.00 5.87 C ANISOU 767 CG LEU A 99 799 664 766 -61 -60 -54 C ATOM 768 CD1 LEU A 99 18.272 17.453 -0.971 1.00 6.16 C ANISOU 768 CD1 LEU A 99 853 768 717 -3 96 31 C ATOM 769 CD2 LEU A 99 17.757 18.101 -3.357 1.00 6.46 C ANISOU 769 CD2 LEU A 99 878 783 791 -48 69 -70 C ATOM 770 N ARG A 100 20.445 13.893 -5.472 1.00 5.90 N ANISOU 770 N ARG A 100 606 817 816 -16 30 56 N ATOM 771 CA ARG A 100 21.621 13.233 -5.976 1.00 6.12 C ANISOU 771 CA ARG A 100 762 787 774 26 21 -44 C ATOM 772 C ARG A 100 22.113 13.908 -7.246 1.00 6.63 C ANISOU 772 C ARG A 100 812 795 912 26 -39 -69 C ATOM 773 O ARG A 100 21.357 14.228 -8.156 1.00 6.55 O ANISOU 773 O ARG A 100 760 826 901 46 -75 -147 O ATOM 774 CB ARG A 100 21.327 11.759 -6.298 1.00 6.66 C ANISOU 774 CB ARG A 100 849 823 855 60 31 -54 C ATOM 775 CG ARG A 100 20.961 10.945 -5.060 1.00 7.10 C ANISOU 775 CG ARG A 100 912 926 858 33 123 -1 C ATOM 776 CD ARG A 100 20.423 9.556 -5.352 1.00 6.88 C ANISOU 776 CD ARG A 100 968 686 959 152 53 14 C ATOM 777 NE ARG A 100 19.191 9.626 -6.122 1.00 7.00 N ANISOU 777 NE ARG A 100 818 627 1215 -13 86 -12 N ATOM 778 CZ ARG A 100 18.446 8.585 -6.479 1.00 6.92 C ANISOU 778 CZ ARG A 100 855 767 1007 14 151 -68 C ATOM 779 NH1 ARG A 100 18.822 7.355 -6.167 1.00 8.41 N ANISOU 779 NH1 ARG A 100 1134 779 1280 -3 -4 67 N ATOM 780 NH2 ARG A 100 17.330 8.763 -7.158 1.00 7.42 N ANISOU 780 NH2 ARG A 100 1064 734 1018 -82 77 -71 N ATOM 781 N GLU A 101 23.418 14.098 -7.306 1.00 7.28 N ANISOU 781 N GLU A 101 916 986 863 37 37 -53 N ATOM 782 CA GLU A 101 24.057 14.618 -8.504 1.00 8.20 C ANISOU 782 CA GLU A 101 1024 1089 1000 -19 4 -45 C ATOM 783 C GLU A 101 23.739 13.720 -9.700 1.00 7.99 C ANISOU 783 C GLU A 101 958 1099 978 60 28 -125 C ATOM 784 O GLU A 101 23.842 12.503 -9.613 1.00 8.56 O ANISOU 784 O GLU A 101 1084 1228 939 102 -12 -194 O ATOM 785 CB GLU A 101 25.564 14.657 -8.275 1.00 9.09 C ANISOU 785 CB GLU A 101 1048 1314 1091 -60 20 31 C ATOM 786 CG GLU A 101 26.349 15.257 -9.416 1.00 12.19 C ANISOU 786 CG GLU A 101 1453 1707 1471 -17 37 -18 C ATOM 787 CD GLU A 101 27.825 15.306 -9.109 1.00 16.42 C ANISOU 787 CD GLU A 101 1938 2128 2174 -100 -27 2 C ATOM 788 OE1 GLU A 101 28.415 14.216 -8.972 1.00 17.90 O ANISOU 788 OE1 GLU A 101 1735 2616 2449 146 181 -55 O ATOM 789 OE2 GLU A 101 28.367 16.428 -8.979 1.00 21.87 O ANISOU 789 OE2 GLU A 101 2588 2882 2839 -103 -171 88 O ATOM 790 N GLY A 102 23.404 14.359 -10.817 1.00 6.27 N ANISOU 790 N GLY A 102 748 948 683 47 12 -210 N ATOM 791 CA GLY A 102 23.073 13.670 -12.055 1.00 6.13 C ANISOU 791 CA GLY A 102 734 893 702 64 48 -181 C ATOM 792 C GLY A 102 21.820 14.230 -12.701 1.00 5.55 C ANISOU 792 C GLY A 102 606 920 582 106 105 -162 C ATOM 793 O GLY A 102 21.290 15.284 -12.317 1.00 6.16 O ANISOU 793 O GLY A 102 639 974 726 -42 73 -209 O ATOM 794 N GLU A 103 21.315 13.484 -13.672 1.00 5.84 N ANISOU 794 N GLU A 103 659 826 733 76 -30 -166 N ATOM 795 CA GLU A 103 20.242 13.957 -14.535 1.00 5.28 C ANISOU 795 CA GLU A 103 714 737 553 133 -62 -87 C ATOM 796 C GLU A 103 18.881 14.031 -13.845 1.00 5.79 C ANISOU 796 C GLU A 103 673 827 699 106 -12 40 C ATOM 797 O GLU A 103 17.942 14.602 -14.392 1.00 7.14 O ANISOU 797 O GLU A 103 862 1180 667 330 -18 251 O ATOM 798 CB GLU A 103 20.127 13.050 -15.756 1.00 5.20 C ANISOU 798 CB GLU A 103 737 659 580 154 -114 -85 C ATOM 799 CG GLU A 103 21.284 13.236 -16.725 1.00 5.09 C ANISOU 799 CG GLU A 103 646 724 563 85 -186 -211 C ATOM 800 CD GLU A 103 21.387 12.181 -17.803 1.00 5.10 C ANISOU 800 CD GLU A 103 751 414 770 123 -405 -92 C ATOM 801 OE1 GLU A 103 20.484 11.324 -17.938 1.00 5.78 O ANISOU 801 OE1 GLU A 103 693 610 890 263 -512 -238 O ATOM 802 OE2 GLU A 103 22.402 12.203 -18.511 1.00 5.20 O ANISOU 802 OE2 GLU A 103 690 717 569 271 -283 -373 O ATOM 803 N THR A 104 18.758 13.471 -12.644 1.00 4.70 N ANISOU 803 N THR A 104 608 640 538 66 43 -58 N ATOM 804 CA THR A 104 17.498 13.543 -11.895 1.00 5.22 C ANISOU 804 CA THR A 104 668 658 655 -10 77 -65 C ATOM 805 C THR A 104 17.552 14.519 -10.714 1.00 4.94 C ANISOU 805 C THR A 104 622 690 566 -20 173 -66 C ATOM 806 O THR A 104 16.588 14.597 -9.959 1.00 5.42 O ANISOU 806 O THR A 104 592 696 770 111 217 -95 O ATOM 807 CB THR A 104 17.037 12.156 -11.431 1.00 5.72 C ANISOU 807 CB THR A 104 636 822 716 -21 76 -82 C ATOM 808 OG1 THR A 104 17.977 11.637 -10.490 1.00 6.04 O ANISOU 808 OG1 THR A 104 739 590 965 20 -90 -7 O ATOM 809 CG2 THR A 104 16.949 11.176 -12.599 1.00 6.92 C ANISOU 809 CG2 THR A 104 842 963 822 32 122 -198 C ATOM 810 N PHE A 105 18.629 15.305 -10.590 1.00 5.06 N ANISOU 810 N PHE A 105 728 708 486 23 152 -152 N ATOM 811 CA PHE A 105 18.717 16.274 -9.516 1.00 5.30 C ANISOU 811 CA PHE A 105 763 707 542 -90 52 -2 C ATOM 812 C PHE A 105 17.535 17.241 -9.621 1.00 5.71 C ANISOU 812 C PHE A 105 792 715 661 -3 49 -73 C ATOM 813 O PHE A 105 17.278 17.841 -10.650 1.00 6.48 O ANISOU 813 O PHE A 105 964 782 713 77 108 165 O ATOM 814 CB PHE A 105 20.047 17.048 -9.562 1.00 5.25 C ANISOU 814 CB PHE A 105 632 673 690 -74 51 -90 C ATOM 815 CG PHE A 105 20.175 18.044 -8.443 1.00 6.31 C ANISOU 815 CG PHE A 105 963 749 683 -201 69 81 C ATOM 816 CD1 PHE A 105 20.513 17.632 -7.153 1.00 6.58 C ANISOU 816 CD1 PHE A 105 987 784 726 -131 44 -10 C ATOM 817 CD2 PHE A 105 19.885 19.390 -8.660 1.00 5.29 C ANISOU 817 CD2 PHE A 105 944 511 553 -21 17 6 C ATOM 818 CE1 PHE A 105 20.592 18.523 -6.111 1.00 6.86 C ANISOU 818 CE1 PHE A 105 1052 885 667 -117 -35 -93 C ATOM 819 CE2 PHE A 105 19.965 20.302 -7.591 1.00 7.45 C ANISOU 819 CE2 PHE A 105 1207 619 1003 119 -118 -85 C ATOM 820 CZ PHE A 105 20.326 19.868 -6.326 1.00 8.14 C ANISOU 820 CZ PHE A 105 1066 994 1030 -107 -1 -47 C ATOM 821 N GLY A 106 16.793 17.402 -8.530 1.00 6.02 N ANISOU 821 N GLY A 106 836 787 662 79 85 13 N ATOM 822 CA GLY A 106 15.634 18.270 -8.476 1.00 6.56 C ANISOU 822 CA GLY A 106 885 766 838 23 41 44 C ATOM 823 C GLY A 106 14.328 17.611 -8.868 1.00 6.26 C ANISOU 823 C GLY A 106 798 766 813 92 32 -44 C ATOM 824 O GLY A 106 13.278 18.211 -8.721 1.00 7.50 O ANISOU 824 O GLY A 106 824 925 1098 137 71 -153 O ATOM 825 N ASN A 107 14.363 16.383 -9.392 1.00 5.75 N ANISOU 825 N ASN A 107 787 759 638 58 24 -88 N ATOM 826 CA ASN A 107 13.131 15.713 -9.763 1.00 6.20 C ANISOU 826 CA ASN A 107 737 860 758 43 42 -33 C ATOM 827 C ASN A 107 12.290 15.445 -8.517 1.00 5.97 C ANISOU 827 C ASN A 107 693 832 744 47 74 89 C ATOM 828 O ASN A 107 12.821 15.260 -7.425 1.00 7.24 O ANISOU 828 O ASN A 107 767 1054 927 143 -48 4 O ATOM 829 CB ASN A 107 13.407 14.386 -10.457 1.00 6.16 C ANISOU 829 CB ASN A 107 827 784 727 -15 89 9 C ATOM 830 CG ASN A 107 13.857 14.537 -11.895 1.00 7.06 C ANISOU 830 CG ASN A 107 912 833 936 36 26 -60 C ATOM 831 OD1 ASN A 107 14.109 15.641 -12.382 1.00 8.68 O ANISOU 831 OD1 ASN A 107 1128 1049 1118 -38 39 -263 O ATOM 832 ND2 ASN A 107 13.953 13.404 -12.578 1.00 6.56 N ANISOU 832 ND2 ASN A 107 1125 794 574 210 78 -128 N ATOM 833 N THR A 108 10.983 15.411 -8.687 1.00 6.87 N ANISOU 833 N THR A 108 826 993 791 100 -10 0 N ATOM 834 CA THR A 108 10.087 15.290 -7.550 1.00 6.11 C ANISOU 834 CA THR A 108 781 843 694 61 102 53 C ATOM 835 C THR A 108 9.047 14.195 -7.740 1.00 6.58 C ANISOU 835 C THR A 108 838 891 769 92 -27 -32 C ATOM 836 O THR A 108 8.783 13.720 -8.845 1.00 6.93 O ANISOU 836 O THR A 108 935 1078 618 -4 62 1 O ATOM 837 CB THR A 108 9.322 16.600 -7.312 1.00 6.78 C ANISOU 837 CB THR A 108 839 884 850 90 28 28 C ATOM 838 OG1 THR A 108 8.395 16.801 -8.382 1.00 7.96 O ANISOU 838 OG1 THR A 108 987 998 1039 102 112 7 O ATOM 839 CG2 THR A 108 10.256 17.797 -7.263 1.00 7.38 C ANISOU 839 CG2 THR A 108 933 1017 851 130 162 87 C ATOM 840 N TYR A 109 8.437 13.836 -6.628 1.00 6.20 N ANISOU 840 N TYR A 109 820 844 690 28 54 33 N ATOM 841 CA TYR A 109 7.260 12.974 -6.598 1.00 6.33 C ANISOU 841 CA TYR A 109 812 798 793 57 33 -8 C ATOM 842 C TYR A 109 6.446 13.344 -5.367 1.00 5.62 C ANISOU 842 C TYR A 109 749 682 703 12 17 -24 C ATOM 843 O TYR A 109 7.004 13.728 -4.362 1.00 6.05 O ANISOU 843 O TYR A 109 814 806 676 94 -19 20 O ATOM 844 CB TYR A 109 7.666 11.485 -6.580 1.00 6.78 C ANISOU 844 CB TYR A 109 881 795 899 60 106 -51 C ATOM 845 CG TYR A 109 6.495 10.526 -6.607 1.00 7.06 C ANISOU 845 CG TYR A 109 969 856 854 105 43 -53 C ATOM 846 CD1 TYR A 109 5.634 10.498 -7.712 1.00 7.78 C ANISOU 846 CD1 TYR A 109 951 986 1019 -116 2 23 C ATOM 847 CD2 TYR A 109 6.245 9.655 -5.556 1.00 6.84 C ANISOU 847 CD2 TYR A 109 853 854 889 61 -46 -51 C ATOM 848 CE1 TYR A 109 4.555 9.603 -7.760 1.00 8.71 C ANISOU 848 CE1 TYR A 109 1222 1035 1050 -64 -97 -100 C ATOM 849 CE2 TYR A 109 5.176 8.765 -5.599 1.00 8.29 C ANISOU 849 CE2 TYR A 109 1077 968 1102 28 67 26 C ATOM 850 CZ TYR A 109 4.340 8.751 -6.695 1.00 8.52 C ANISOU 850 CZ TYR A 109 1061 962 1211 -65 -25 -126 C ATOM 851 OH TYR A 109 3.254 7.911 -6.797 1.00 10.40 O ANISOU 851 OH TYR A 109 1282 973 1696 -182 1 -223 O ATOM 852 N GLN A 110 5.131 13.214 -5.466 1.00 5.87 N ANISOU 852 N GLN A 110 780 730 719 38 14 -19 N ATOM 853 CA GLN A 110 4.230 13.372 -4.332 1.00 5.74 C ANISOU 853 CA GLN A 110 712 726 742 68 57 -35 C ATOM 854 C GLN A 110 3.142 12.332 -4.413 1.00 5.69 C ANISOU 854 C GLN A 110 739 734 689 44 100 -39 C ATOM 855 O GLN A 110 2.658 11.998 -5.500 1.00 6.58 O ANISOU 855 O GLN A 110 873 898 727 -85 86 -26 O ATOM 856 CB GLN A 110 3.595 14.753 -4.246 1.00 5.94 C ANISOU 856 CB GLN A 110 791 710 753 -23 -68 1 C ATOM 857 CG GLN A 110 4.612 15.892 -4.098 1.00 5.93 C ANISOU 857 CG GLN A 110 690 703 858 -3 7 100 C ATOM 858 CD GLN A 110 3.925 17.209 -3.899 1.00 6.72 C ANISOU 858 CD GLN A 110 826 706 1020 -31 125 147 C ATOM 859 OE1 GLN A 110 3.590 17.896 -4.868 1.00 6.62 O ANISOU 859 OE1 GLN A 110 951 713 852 17 102 119 O ATOM 860 NE2 GLN A 110 3.736 17.600 -2.653 1.00 7.60 N ANISOU 860 NE2 GLN A 110 1023 972 893 -16 -39 79 N ATOM 861 N THR A 111 2.708 11.851 -3.256 1.00 6.49 N ANISOU 861 N THR A 111 845 795 825 -56 7 7 N ATOM 862 CA THR A 111 1.580 10.926 -3.187 1.00 6.90 C ANISOU 862 CA THR A 111 894 840 885 -43 63 -35 C ATOM 863 C THR A 111 1.022 10.942 -1.789 1.00 6.66 C ANISOU 863 C THR A 111 937 782 810 -65 38 -18 C ATOM 864 O THR A 111 1.723 11.301 -0.843 1.00 7.21 O ANISOU 864 O THR A 111 924 949 864 -247 48 47 O ATOM 865 CB THR A 111 2.026 9.523 -3.617 1.00 8.62 C ANISOU 865 CB THR A 111 1148 1064 1063 -92 87 -72 C ATOM 866 OG1 THR A 111 0.874 8.751 -3.937 1.00 10.70 O ANISOU 866 OG1 THR A 111 1442 1287 1336 -417 137 -232 O ATOM 867 CG2 THR A 111 2.737 8.755 -2.525 1.00 9.03 C ANISOU 867 CG2 THR A 111 1163 854 1411 -150 222 -56 C ATOM 868 N VAL A 112 -0.240 10.565 -1.656 1.00 6.96 N ANISOU 868 N VAL A 112 993 956 696 -48 39 61 N ATOM 869 CA VAL A 112 -0.808 10.405 -0.318 1.00 7.71 C ANISOU 869 CA VAL A 112 1092 1002 833 -122 -12 -35 C ATOM 870 C VAL A 112 -0.366 9.073 0.285 1.00 7.30 C ANISOU 870 C VAL A 112 1105 833 833 -163 33 -41 C ATOM 871 O VAL A 112 -0.551 8.028 -0.318 1.00 9.96 O ANISOU 871 O VAL A 112 1858 984 939 -247 -102 -158 O ATOM 872 CB VAL A 112 -2.335 10.497 -0.348 1.00 9.14 C ANISOU 872 CB VAL A 112 1197 1255 1020 -46 67 9 C ATOM 873 CG1 VAL A 112 -2.932 10.131 1.017 1.00 11.28 C ANISOU 873 CG1 VAL A 112 1306 1626 1354 -145 140 20 C ATOM 874 CG2 VAL A 112 -2.772 11.888 -0.768 1.00 10.89 C ANISOU 874 CG2 VAL A 112 1259 1591 1285 47 -21 -54 C ATOM 875 N ILE A 113 0.241 9.131 1.463 1.00 6.86 N ANISOU 875 N ILE A 113 1099 655 850 -80 -20 -84 N ATOM 876 CA ILE A 113 0.619 7.940 2.211 1.00 7.09 C ANISOU 876 CA ILE A 113 1129 728 836 -74 137 0 C ATOM 877 C ILE A 113 -0.404 7.720 3.298 1.00 6.65 C ANISOU 877 C ILE A 113 1039 678 807 -123 126 -3 C ATOM 878 O ILE A 113 -0.645 8.596 4.124 1.00 7.06 O ANISOU 878 O ILE A 113 1133 568 980 -6 250 -68 O ATOM 879 CB ILE A 113 2.029 8.043 2.809 1.00 7.58 C ANISOU 879 CB ILE A 113 1183 796 901 -8 162 16 C ATOM 880 CG1 ILE A 113 3.088 8.454 1.806 1.00 9.65 C ANISOU 880 CG1 ILE A 113 1282 1082 1302 34 83 137 C ATOM 881 CG2 ILE A 113 2.416 6.713 3.509 1.00 8.46 C ANISOU 881 CG2 ILE A 113 1230 945 1037 108 88 92 C ATOM 882 CD1 ILE A 113 4.404 8.762 2.463 1.00 13.50 C ANISOU 882 CD1 ILE A 113 1750 1733 1645 20 98 165 C ATOM 883 N ASP A 114 -0.971 6.518 3.311 1.00 6.92 N ANISOU 883 N ASP A 114 1139 715 775 -133 218 -76 N ATOM 884 CA ASP A 114 -1.874 6.081 4.374 1.00 7.02 C ANISOU 884 CA ASP A 114 1048 802 816 -32 166 15 C ATOM 885 C ASP A 114 -1.473 4.643 4.695 1.00 6.04 C ANISOU 885 C ASP A 114 855 661 777 -68 63 -41 C ATOM 886 O ASP A 114 -0.485 4.151 4.165 1.00 6.65 O ANISOU 886 O ASP A 114 900 864 763 -119 119 -45 O ATOM 887 CB ASP A 114 -3.334 6.275 3.990 1.00 7.60 C ANISOU 887 CB ASP A 114 1355 651 880 -3 158 76 C ATOM 888 CG ASP A 114 -3.747 5.501 2.782 1.00 8.47 C ANISOU 888 CG ASP A 114 1395 697 1126 97 -79 232 C ATOM 889 OD1 ASP A 114 -3.173 4.444 2.485 1.00 7.34 O ANISOU 889 OD1 ASP A 114 1206 718 865 -30 -54 18 O ATOM 890 OD2 ASP A 114 -4.666 5.932 2.057 1.00 12.54 O ANISOU 890 OD2 ASP A 114 2192 971 1599 177 -576 93 O ATOM 891 N ALA A 115 -2.239 3.946 5.513 1.00 5.91 N ANISOU 891 N ALA A 115 831 715 697 10 32 -38 N ATOM 892 CA ALA A 115 -1.857 2.598 5.916 1.00 5.90 C ANISOU 892 CA ALA A 115 748 751 741 58 -2 46 C ATOM 893 C ALA A 115 -1.772 1.613 4.754 1.00 5.46 C ANISOU 893 C ALA A 115 750 686 637 31 -40 90 C ATOM 894 O ALA A 115 -1.121 0.574 4.888 1.00 6.24 O ANISOU 894 O ALA A 115 767 803 797 167 -73 55 O ATOM 895 CB ALA A 115 -2.814 2.074 6.970 1.00 7.03 C ANISOU 895 CB ALA A 115 1065 715 888 68 35 120 C ATOM 896 N SER A 116 -2.412 1.946 3.635 1.00 5.17 N ANISOU 896 N SER A 116 667 554 743 -14 -22 27 N ATOM 897 CA SER A 116 -2.422 1.067 2.468 1.00 5.22 C ANISOU 897 CA SER A 116 655 552 774 27 7 8 C ATOM 898 C SER A 116 -1.351 1.350 1.424 1.00 4.90 C ANISOU 898 C SER A 116 689 464 707 28 5 30 C ATOM 899 O SER A 116 -1.333 0.721 0.369 1.00 5.63 O ANISOU 899 O SER A 116 864 589 685 3 24 -46 O ATOM 900 CB SER A 116 -3.787 1.134 1.782 1.00 5.36 C ANISOU 900 CB SER A 116 739 499 798 -36 -3 -67 C ATOM 901 OG SER A 116 -3.954 2.286 0.986 1.00 7.05 O ANISOU 901 OG SER A 116 861 840 976 208 -105 73 O ATOM 902 N LYS A 117 -0.437 2.266 1.713 1.00 5.51 N ANISOU 902 N LYS A 117 706 698 688 -20 57 -63 N ATOM 903 CA LYS A 117 0.632 2.644 0.788 1.00 6.61 C ANISOU 903 CA LYS A 117 855 826 827 -50 76 -13 C ATOM 904 C LYS A 117 1.914 2.880 1.548 1.00 6.63 C ANISOU 904 C LYS A 117 799 889 827 -127 68 -50 C ATOM 905 O LYS A 117 1.924 3.568 2.542 1.00 9.21 O ANISOU 905 O LYS A 117 930 1487 1082 -136 192 -471 O ATOM 906 CB LYS A 117 0.287 3.891 -0.003 1.00 7.60 C ANISOU 906 CB LYS A 117 948 951 985 -76 161 29 C ATOM 907 CG LYS A 117 1.297 4.228 -1.106 1.00 11.57 C ANISOU 907 CG LYS A 117 1636 1309 1450 0 145 141 C ATOM 908 CD LYS A 117 0.903 5.504 -1.895 1.00 13.31 C ANISOU 908 CD LYS A 117 1935 1546 1576 -76 105 181 C ATOM 909 CE LYS A 117 -0.563 5.541 -2.379 1.00 14.23 C ANISOU 909 CE LYS A 117 2131 1675 1599 -50 -134 141 C ATOM 910 NZ LYS A 117 -1.150 6.928 -2.731 1.00 16.18 N ANISOU 910 NZ LYS A 117 2569 1721 1856 -292 -263 116 N ATOM 911 N BSER A 118 3.008 2.314 1.078 0.60 6.43 N ANISOU 911 N BSER A 118 823 851 770 -107 75 -77 N ATOM 912 CA BSER A 118 4.303 2.586 1.681 0.60 6.17 C ANISOU 912 CA BSER A 118 794 813 738 -65 28 -70 C ATOM 913 C BSER A 118 5.259 3.006 0.571 0.60 6.40 C ANISOU 913 C BSER A 118 795 847 787 -96 53 -23 C ATOM 914 O BSER A 118 4.940 2.897 -0.631 0.60 6.70 O ANISOU 914 O BSER A 118 827 871 846 -46 -14 -152 O ATOM 915 CB BSER A 118 4.854 1.355 2.368 0.60 6.54 C ANISOU 915 CB BSER A 118 762 863 860 -73 70 -111 C ATOM 916 OG BSER A 118 4.927 0.335 1.420 0.60 9.19 O ANISOU 916 OG BSER A 118 1198 1062 1231 -134 17 -73 O ATOM 917 N ILE A 119 6.418 3.522 0.956 1.00 6.34 N ANISOU 917 N ILE A 119 764 851 791 -133 23 10 N ATOM 918 CA ILE A 119 7.375 4.069 -0.008 1.00 6.50 C ANISOU 918 CA ILE A 119 756 873 839 -26 37 62 C ATOM 919 C ILE A 119 8.791 3.694 0.403 1.00 5.67 C ANISOU 919 C ILE A 119 751 705 698 -13 -71 61 C ATOM 920 O ILE A 119 9.184 3.911 1.546 1.00 6.75 O ANISOU 920 O ILE A 119 813 1027 724 103 -8 26 O ATOM 921 CB ILE A 119 7.282 5.625 -0.049 1.00 8.60 C ANISOU 921 CB ILE A 119 970 1077 1220 52 131 339 C ATOM 922 CG1 ILE A 119 5.859 6.139 -0.242 1.00 13.39 C ANISOU 922 CG1 ILE A 119 1521 1567 1999 34 19 70 C ATOM 923 CG2 ILE A 119 8.206 6.168 -1.103 1.00 9.86 C ANISOU 923 CG2 ILE A 119 1251 1079 1415 113 168 427 C ATOM 924 CD1 ILE A 119 5.294 5.953 -1.571 1.00 16.18 C ANISOU 924 CD1 ILE A 119 1960 1867 2320 198 -138 -55 C ATOM 925 N PHE A 120 9.562 3.174 -0.534 1.00 6.02 N ANISOU 925 N PHE A 120 698 883 704 -22 -61 69 N ATOM 926 CA PHE A 120 10.999 3.001 -0.374 1.00 5.81 C ANISOU 926 CA PHE A 120 758 829 621 59 -18 69 C ATOM 927 C PHE A 120 11.740 4.212 -0.964 1.00 5.99 C ANISOU 927 C PHE A 120 811 805 658 20 3 127 C ATOM 928 O PHE A 120 11.556 4.550 -2.142 1.00 6.77 O ANISOU 928 O PHE A 120 927 1021 622 71 46 66 O ATOM 929 CB PHE A 120 11.498 1.736 -1.026 1.00 6.22 C ANISOU 929 CB PHE A 120 855 782 727 -21 24 24 C ATOM 930 CG PHE A 120 12.965 1.586 -0.880 1.00 6.84 C ANISOU 930 CG PHE A 120 808 785 1007 -15 -64 -49 C ATOM 931 CD1 PHE A 120 13.503 1.158 0.317 1.00 9.18 C ANISOU 931 CD1 PHE A 120 896 1477 1112 104 86 0 C ATOM 932 CD2 PHE A 120 13.837 1.989 -1.873 1.00 8.17 C ANISOU 932 CD2 PHE A 120 823 1000 1278 75 -56 94 C ATOM 933 CE1 PHE A 120 14.886 1.084 0.495 1.00 11.17 C ANISOU 933 CE1 PHE A 120 1345 1675 1221 185 -281 -171 C ATOM 934 CE2 PHE A 120 15.217 1.923 -1.687 1.00 9.15 C ANISOU 934 CE2 PHE A 120 1088 1021 1366 -11 76 -70 C ATOM 935 CZ PHE A 120 15.723 1.470 -0.492 1.00 10.34 C ANISOU 935 CZ PHE A 120 973 1338 1616 120 -174 -325 C ATOM 936 N VAL A 121 12.551 4.873 -0.140 1.00 5.88 N ANISOU 936 N VAL A 121 789 801 645 -56 26 137 N ATOM 937 CA VAL A 121 13.259 6.092 -0.483 1.00 6.56 C ANISOU 937 CA VAL A 121 859 813 821 -51 69 173 C ATOM 938 C VAL A 121 14.761 5.825 -0.426 1.00 6.78 C ANISOU 938 C VAL A 121 858 819 899 -121 31 122 C ATOM 939 O VAL A 121 15.305 5.649 0.675 1.00 6.30 O ANISOU 939 O VAL A 121 697 940 757 -92 49 148 O ATOM 940 CB VAL A 121 12.909 7.242 0.500 1.00 7.31 C ANISOU 940 CB VAL A 121 914 783 1081 -27 46 142 C ATOM 941 CG1 VAL A 121 13.506 8.548 0.008 1.00 8.87 C ANISOU 941 CG1 VAL A 121 1071 981 1317 -54 135 201 C ATOM 942 CG2 VAL A 121 11.426 7.385 0.673 1.00 8.25 C ANISOU 942 CG2 VAL A 121 1120 881 1132 -40 265 257 C ATOM 943 N PRO A 122 15.459 5.818 -1.558 1.00 6.71 N ANISOU 943 N PRO A 122 857 803 888 -85 -3 90 N ATOM 944 CA PRO A 122 16.906 5.623 -1.521 1.00 7.48 C ANISOU 944 CA PRO A 122 907 977 958 -45 66 21 C ATOM 945 C PRO A 122 17.623 6.795 -0.841 1.00 7.15 C ANISOU 945 C PRO A 122 835 887 992 -68 78 106 C ATOM 946 O PRO A 122 17.199 7.948 -0.973 1.00 7.54 O ANISOU 946 O PRO A 122 769 858 1235 -43 50 140 O ATOM 947 CB PRO A 122 17.305 5.589 -2.999 1.00 8.98 C ANISOU 947 CB PRO A 122 1116 1214 1080 -108 104 -36 C ATOM 948 CG PRO A 122 16.095 5.589 -3.765 1.00 10.19 C ANISOU 948 CG PRO A 122 1264 1435 1170 94 58 8 C ATOM 949 CD PRO A 122 14.957 5.995 -2.930 1.00 7.39 C ANISOU 949 CD PRO A 122 883 988 934 -78 45 125 C ATOM 950 N ARG A 123 18.743 6.497 -0.213 1.00 7.13 N ANISOU 950 N ARG A 123 827 865 1017 -9 38 77 N ATOM 951 CA ARG A 123 19.630 7.518 0.311 1.00 7.38 C ANISOU 951 CA ARG A 123 877 927 1000 -12 18 111 C ATOM 952 C ARG A 123 19.946 8.522 -0.795 1.00 7.36 C ANISOU 952 C ARG A 123 867 927 1000 -32 52 88 C ATOM 953 O ARG A 123 20.281 8.149 -1.929 1.00 8.00 O ANISOU 953 O ARG A 123 1016 947 1075 -121 170 134 O ATOM 954 CB ARG A 123 20.906 6.853 0.789 1.00 8.61 C ANISOU 954 CB ARG A 123 1063 952 1254 -66 -5 141 C ATOM 955 CG ARG A 123 21.961 7.795 1.266 1.00 10.20 C ANISOU 955 CG ARG A 123 1229 1077 1569 14 -8 63 C ATOM 956 CD ARG A 123 23.107 7.057 1.917 1.00 12.67 C ANISOU 956 CD ARG A 123 1503 1343 1965 -63 -286 87 C ATOM 957 NE ARG A 123 24.212 7.962 2.194 1.00 14.83 N ANISOU 957 NE ARG A 123 1557 1703 2374 0 -347 157 N ATOM 958 CZ ARG A 123 25.332 7.637 2.825 1.00 15.43 C ANISOU 958 CZ ARG A 123 1742 1874 2246 6 -305 98 C ATOM 959 NH1 ARG A 123 25.497 6.424 3.315 1.00 17.26 N ANISOU 959 NH1 ARG A 123 1875 2098 2585 -4 -217 309 N ATOM 960 NH2 ARG A 123 26.287 8.540 2.972 1.00 15.57 N ANISOU 960 NH2 ARG A 123 1611 1961 2341 80 -153 138 N ATOM 961 N GLY A 124 19.849 9.801 -0.457 1.00 7.05 N ANISOU 961 N GLY A 124 844 858 976 -55 86 55 N ATOM 962 CA GLY A 124 20.079 10.881 -1.394 1.00 7.60 C ANISOU 962 CA GLY A 124 977 812 1097 -30 89 87 C ATOM 963 C GLY A 124 18.837 11.587 -1.875 1.00 7.26 C ANISOU 963 C GLY A 124 877 813 1065 -84 99 43 C ATOM 964 O GLY A 124 18.913 12.620 -2.497 1.00 7.71 O ANISOU 964 O GLY A 124 1045 786 1096 21 148 128 O ATOM 965 N VAL A 125 17.684 10.972 -1.642 1.00 6.69 N ANISOU 965 N VAL A 125 813 744 981 -65 86 142 N ATOM 966 CA VAL A 125 16.415 11.575 -2.005 1.00 6.29 C ANISOU 966 CA VAL A 125 840 746 801 24 131 112 C ATOM 967 C VAL A 125 15.803 12.212 -0.769 1.00 5.93 C ANISOU 967 C VAL A 125 823 679 750 8 184 67 C ATOM 968 O VAL A 125 15.592 11.558 0.238 1.00 7.78 O ANISOU 968 O VAL A 125 1319 840 796 99 357 179 O ATOM 969 CB VAL A 125 15.479 10.519 -2.592 1.00 6.34 C ANISOU 969 CB VAL A 125 901 676 829 69 119 59 C ATOM 970 CG1 VAL A 125 14.114 11.113 -2.885 1.00 7.21 C ANISOU 970 CG1 VAL A 125 1006 931 801 86 64 33 C ATOM 971 CG2 VAL A 125 16.093 9.893 -3.835 1.00 6.89 C ANISOU 971 CG2 VAL A 125 1006 681 931 46 114 -110 C ATOM 972 N ALA A 126 15.538 13.508 -0.837 1.00 5.58 N ANISOU 972 N ALA A 126 872 705 542 48 100 61 N ATOM 973 CA ALA A 126 14.972 14.219 0.297 1.00 5.58 C ANISOU 973 CA ALA A 126 723 739 656 37 51 3 C ATOM 974 C ALA A 126 13.521 13.838 0.499 1.00 5.60 C ANISOU 974 C ALA A 126 719 763 642 35 49 40 C ATOM 975 O ALA A 126 12.762 13.698 -0.446 1.00 6.93 O ANISOU 975 O ALA A 126 836 1079 717 -10 6 120 O ATOM 976 CB ALA A 126 15.084 15.717 0.081 1.00 6.23 C ANISOU 976 CB ALA A 126 847 760 758 25 58 9 C ATOM 977 N ASN A 127 13.159 13.680 1.761 1.00 5.78 N ANISOU 977 N ASN A 127 711 829 655 -86 44 52 N ATOM 978 CA ASN A 127 11.862 13.206 2.212 1.00 6.04 C ANISOU 978 CA ASN A 127 758 822 714 -54 99 103 C ATOM 979 C ASN A 127 11.166 14.257 3.054 1.00 5.63 C ANISOU 979 C ASN A 127 720 714 706 -20 77 115 C ATOM 980 O ASN A 127 11.795 14.964 3.863 1.00 6.61 O ANISOU 980 O ASN A 127 790 956 763 -6 119 -7 O ATOM 981 CB ASN A 127 12.090 11.953 3.081 1.00 6.94 C ANISOU 981 CB ASN A 127 815 839 980 26 13 145 C ATOM 982 CG ASN A 127 10.830 11.395 3.692 1.00 7.15 C ANISOU 982 CG ASN A 127 999 835 880 20 8 195 C ATOM 983 OD1 ASN A 127 10.010 10.845 2.991 1.00 8.25 O ANISOU 983 OD1 ASN A 127 942 1302 889 13 34 173 O ATOM 984 ND2 ASN A 127 10.712 11.482 5.003 1.00 9.44 N ANISOU 984 ND2 ASN A 127 1210 1267 1108 108 133 157 N ATOM 985 N GLY A 128 9.855 14.343 2.916 1.00 5.51 N ANISOU 985 N GLY A 128 716 751 626 11 71 -5 N ATOM 986 CA GLY A 128 9.037 15.210 3.737 1.00 6.30 C ANISOU 986 CA GLY A 128 833 794 766 -32 69 -14 C ATOM 987 C GLY A 128 7.583 14.808 3.679 1.00 5.67 C ANISOU 987 C GLY A 128 779 692 681 20 68 60 C ATOM 988 O GLY A 128 7.188 13.923 2.918 1.00 5.52 O ANISOU 988 O GLY A 128 689 650 757 49 88 41 O ATOM 989 N PHE A 129 6.768 15.467 4.489 1.00 5.92 N ANISOU 989 N PHE A 129 771 743 735 -18 120 -19 N ATOM 990 CA PHE A 129 5.346 15.215 4.516 1.00 6.49 C ANISOU 990 CA PHE A 129 798 788 879 13 87 -67 C ATOM 991 C PHE A 129 4.610 16.366 5.156 1.00 5.85 C ANISOU 991 C PHE A 129 789 700 733 -23 -22 -97 C ATOM 992 O PHE A 129 5.158 17.127 5.954 1.00 6.32 O ANISOU 992 O PHE A 129 793 715 891 -2 -85 -218 O ATOM 993 CB PHE A 129 5.023 13.926 5.264 1.00 6.93 C ANISOU 993 CB PHE A 129 775 806 1050 5 155 -111 C ATOM 994 CG PHE A 129 5.375 13.926 6.716 1.00 7.38 C ANISOU 994 CG PHE A 129 848 815 1141 -15 177 128 C ATOM 995 CD1 PHE A 129 4.450 14.320 7.671 1.00 8.22 C ANISOU 995 CD1 PHE A 129 910 1050 1162 52 129 183 C ATOM 996 CD2 PHE A 129 6.608 13.449 7.163 1.00 8.55 C ANISOU 996 CD2 PHE A 129 959 856 1434 176 227 205 C ATOM 997 CE1 PHE A 129 4.752 14.272 9.034 1.00 9.00 C ANISOU 997 CE1 PHE A 129 1034 1223 1163 289 174 152 C ATOM 998 CE2 PHE A 129 6.912 13.415 8.515 1.00 9.79 C ANISOU 998 CE2 PHE A 129 1046 1097 1573 215 173 314 C ATOM 999 CZ PHE A 129 5.992 13.827 9.441 1.00 9.80 C ANISOU 999 CZ PHE A 129 1216 1279 1226 180 75 423 C ATOM 1000 N GLN A 130 3.343 16.497 4.778 1.00 5.88 N ANISOU 1000 N GLN A 130 689 737 808 2 -25 -112 N ATOM 1001 CA GLN A 130 2.402 17.336 5.506 1.00 5.69 C ANISOU 1001 CA GLN A 130 757 672 730 66 16 -43 C ATOM 1002 C GLN A 130 1.234 16.478 5.974 1.00 5.46 C ANISOU 1002 C GLN A 130 785 580 707 22 6 -90 C ATOM 1003 O GLN A 130 0.667 15.716 5.201 1.00 5.73 O ANISOU 1003 O GLN A 130 838 626 710 -77 44 -161 O ATOM 1004 CB GLN A 130 1.910 18.522 4.670 1.00 5.95 C ANISOU 1004 CB GLN A 130 833 751 673 -20 13 -77 C ATOM 1005 CG GLN A 130 1.029 19.446 5.495 1.00 6.20 C ANISOU 1005 CG GLN A 130 697 765 892 -10 25 210 C ATOM 1006 CD GLN A 130 0.737 20.783 4.875 1.00 7.24 C ANISOU 1006 CD GLN A 130 795 993 961 -71 219 34 C ATOM 1007 OE1 GLN A 130 0.502 20.893 3.682 1.00 7.89 O ANISOU 1007 OE1 GLN A 130 905 1309 784 -54 142 430 O ATOM 1008 NE2 GLN A 130 0.677 21.810 5.726 1.00 8.79 N ANISOU 1008 NE2 GLN A 130 953 1016 1371 -32 173 -107 N ATOM 1009 N VAL A 131 0.861 16.613 7.241 1.00 4.76 N ANISOU 1009 N VAL A 131 694 523 588 -110 28 -57 N ATOM 1010 CA VAL A 131 -0.197 15.782 7.821 1.00 5.27 C ANISOU 1010 CA VAL A 131 768 559 676 -28 -11 57 C ATOM 1011 C VAL A 131 -1.545 16.271 7.336 1.00 5.51 C ANISOU 1011 C VAL A 131 775 651 667 27 -50 -40 C ATOM 1012 O VAL A 131 -1.864 17.452 7.481 1.00 5.74 O ANISOU 1012 O VAL A 131 813 556 811 110 -65 -7 O ATOM 1013 CB VAL A 131 -0.148 15.806 9.341 1.00 5.24 C ANISOU 1013 CB VAL A 131 704 581 704 21 -79 -24 C ATOM 1014 CG1 VAL A 131 -1.201 14.881 9.934 1.00 6.24 C ANISOU 1014 CG1 VAL A 131 833 654 883 -103 -17 0 C ATOM 1015 CG2 VAL A 131 1.229 15.415 9.820 1.00 6.19 C ANISOU 1015 CG2 VAL A 131 925 716 711 -10 -116 8 C ATOM 1016 N LEU A 132 -2.340 15.388 6.724 1.00 6.23 N ANISOU 1016 N LEU A 132 772 655 938 31 -28 14 N ATOM 1017 CA LEU A 132 -3.650 15.725 6.185 1.00 7.28 C ANISOU 1017 CA LEU A 132 929 826 1012 43 -38 9 C ATOM 1018 C LEU A 132 -4.814 15.396 7.117 1.00 7.37 C ANISOU 1018 C LEU A 132 863 825 1110 72 -19 -119 C ATOM 1019 O LEU A 132 -5.818 16.091 7.135 1.00 8.58 O ANISOU 1019 O LEU A 132 812 969 1479 159 -95 -200 O ATOM 1020 CB LEU A 132 -3.851 14.989 4.864 1.00 7.95 C ANISOU 1020 CB LEU A 132 977 914 1128 28 -30 51 C ATOM 1021 CG LEU A 132 -2.808 15.231 3.774 1.00 8.14 C ANISOU 1021 CG LEU A 132 1005 1008 1078 156 -53 19 C ATOM 1022 CD1 LEU A 132 -3.045 14.241 2.623 1.00 9.76 C ANISOU 1022 CD1 LEU A 132 1443 1149 1114 31 -167 -40 C ATOM 1023 CD2 LEU A 132 -2.830 16.662 3.296 1.00 11.32 C ANISOU 1023 CD2 LEU A 132 1445 1347 1507 138 148 -63 C ATOM 1024 N SER A 133 -4.686 14.315 7.857 1.00 7.59 N ANISOU 1024 N SER A 133 844 910 1126 39 0 -130 N ATOM 1025 CA SER A 133 -5.665 13.881 8.822 1.00 7.67 C ANISOU 1025 CA SER A 133 879 871 1161 28 41 -111 C ATOM 1026 C SER A 133 -5.480 14.638 10.144 1.00 7.87 C ANISOU 1026 C SER A 133 871 914 1202 -35 62 -142 C ATOM 1027 O SER A 133 -4.546 15.412 10.302 1.00 8.82 O ANISOU 1027 O SER A 133 943 910 1495 -36 124 -397 O ATOM 1028 CB SER A 133 -5.487 12.378 9.044 1.00 7.42 C ANISOU 1028 CB SER A 133 918 889 1012 -39 49 -149 C ATOM 1029 OG SER A 133 -4.146 12.064 9.365 1.00 7.14 O ANISOU 1029 OG SER A 133 939 656 1116 102 135 -172 O ATOM 1030 N ASP A 134 -6.386 14.443 11.092 1.00 8.22 N ANISOU 1030 N ASP A 134 908 997 1215 60 63 -236 N ATOM 1031 CA ASP A 134 -6.281 15.129 12.374 1.00 8.17 C ANISOU 1031 CA ASP A 134 1009 970 1124 -15 74 -169 C ATOM 1032 C ASP A 134 -4.981 14.792 13.095 1.00 7.47 C ANISOU 1032 C ASP A 134 922 840 1074 -92 96 -160 C ATOM 1033 O ASP A 134 -4.355 15.673 13.697 1.00 7.64 O ANISOU 1033 O ASP A 134 964 803 1133 -226 0 -165 O ATOM 1034 CB ASP A 134 -7.500 14.820 13.255 1.00 8.79 C ANISOU 1034 CB ASP A 134 1033 1029 1275 -28 59 -119 C ATOM 1035 CG ASP A 134 -8.820 15.398 12.702 1.00 10.36 C ANISOU 1035 CG ASP A 134 1019 1297 1619 68 422 -271 C ATOM 1036 OD1 ASP A 134 -8.807 16.226 11.783 1.00 14.31 O ANISOU 1036 OD1 ASP A 134 1050 1881 2506 420 175 -443 O ATOM 1037 OD2 ASP A 134 -9.914 15.052 13.181 1.00 16.80 O ANISOU 1037 OD2 ASP A 134 1656 1860 2866 -381 298 76 O ATOM 1038 N PHE A 135 -4.572 13.530 13.008 1.00 6.58 N ANISOU 1038 N PHE A 135 773 766 959 -184 145 -126 N ATOM 1039 CA PHE A 135 -3.291 13.059 13.504 1.00 7.14 C ANISOU 1039 CA PHE A 135 983 836 894 -41 64 -116 C ATOM 1040 C PHE A 135 -2.831 11.909 12.621 1.00 6.23 C ANISOU 1040 C PHE A 135 884 672 809 -78 34 -105 C ATOM 1041 O PHE A 135 -3.620 11.309 11.877 1.00 6.80 O ANISOU 1041 O PHE A 135 805 862 915 -44 34 -75 O ATOM 1042 CB PHE A 135 -3.383 12.528 14.923 1.00 9.08 C ANISOU 1042 CB PHE A 135 1214 1030 1203 -82 124 -134 C ATOM 1043 CG PHE A 135 -3.710 13.550 15.952 1.00 14.77 C ANISOU 1043 CG PHE A 135 1902 1803 1905 -138 153 34 C ATOM 1044 CD1 PHE A 135 -5.027 13.815 16.283 1.00 16.85 C ANISOU 1044 CD1 PHE A 135 2115 2109 2176 124 417 -155 C ATOM 1045 CD2 PHE A 135 -2.702 14.207 16.624 1.00 16.26 C ANISOU 1045 CD2 PHE A 135 2308 2125 1743 -228 170 -332 C ATOM 1046 CE1 PHE A 135 -5.341 14.767 17.262 1.00 19.25 C ANISOU 1046 CE1 PHE A 135 2461 2469 2384 -4 330 -146 C ATOM 1047 CE2 PHE A 135 -2.995 15.151 17.617 1.00 18.25 C ANISOU 1047 CE2 PHE A 135 2612 2302 2018 -264 311 -172 C ATOM 1048 CZ PHE A 135 -4.313 15.421 17.937 1.00 18.24 C ANISOU 1048 CZ PHE A 135 2353 2316 2261 -105 278 -391 C ATOM 1049 N VAL A 136 -1.554 11.563 12.736 1.00 5.81 N ANISOU 1049 N VAL A 136 809 648 748 -48 -57 -22 N ATOM 1050 CA VAL A 136 -1.006 10.426 12.013 1.00 5.90 C ANISOU 1050 CA VAL A 136 846 622 772 -48 -58 28 C ATOM 1051 C VAL A 136 0.154 9.804 12.774 1.00 5.32 C ANISOU 1051 C VAL A 136 692 634 693 -69 -90 10 C ATOM 1052 O VAL A 136 0.933 10.515 13.408 1.00 6.17 O ANISOU 1052 O VAL A 136 868 662 812 -101 -160 0 O ATOM 1053 CB VAL A 136 -0.576 10.814 10.578 1.00 6.44 C ANISOU 1053 CB VAL A 136 908 784 753 -42 -69 46 C ATOM 1054 CG1 VAL A 136 0.622 11.726 10.602 1.00 6.32 C ANISOU 1054 CG1 VAL A 136 971 716 713 -81 41 95 C ATOM 1055 CG2 VAL A 136 -0.310 9.584 9.682 1.00 6.52 C ANISOU 1055 CG2 VAL A 136 922 806 747 5 -23 116 C ATOM 1056 N ALA A 137 0.244 8.481 12.678 1.00 5.18 N ANISOU 1056 N ALA A 137 669 589 710 -88 -119 26 N ATOM 1057 CA ALA A 137 1.361 7.708 13.187 1.00 5.11 C ANISOU 1057 CA ALA A 137 697 592 652 -73 -59 80 C ATOM 1058 C ALA A 137 2.218 7.324 11.992 1.00 5.27 C ANISOU 1058 C ALA A 137 776 555 669 -114 -70 43 C ATOM 1059 O ALA A 137 1.827 6.500 11.161 1.00 7.35 O ANISOU 1059 O ALA A 137 991 907 891 -335 52 -76 O ATOM 1060 CB ALA A 137 0.885 6.478 13.929 1.00 6.01 C ANISOU 1060 CB ALA A 137 763 720 797 -165 23 106 C ATOM 1061 N TYR A 138 3.373 7.968 11.885 1.00 5.66 N ANISOU 1061 N TYR A 138 745 739 663 -30 4 -27 N ATOM 1062 CA TYR A 138 4.274 7.854 10.728 1.00 5.37 C ANISOU 1062 CA TYR A 138 668 720 651 -31 17 0 C ATOM 1063 C TYR A 138 5.423 6.956 11.185 1.00 5.90 C ANISOU 1063 C TYR A 138 714 799 726 -32 -9 -59 C ATOM 1064 O TYR A 138 6.163 7.333 12.076 1.00 7.25 O ANISOU 1064 O TYR A 138 847 979 927 86 -167 -118 O ATOM 1065 CB TYR A 138 4.732 9.258 10.376 1.00 6.48 C ANISOU 1065 CB TYR A 138 766 880 815 17 35 -9 C ATOM 1066 CG TYR A 138 5.616 9.473 9.175 1.00 6.53 C ANISOU 1066 CG TYR A 138 771 823 886 34 159 93 C ATOM 1067 CD1 TYR A 138 5.082 9.702 7.922 1.00 7.19 C ANISOU 1067 CD1 TYR A 138 763 1052 916 102 17 58 C ATOM 1068 CD2 TYR A 138 6.993 9.549 9.307 1.00 7.27 C ANISOU 1068 CD2 TYR A 138 791 1101 871 -30 42 314 C ATOM 1069 CE1 TYR A 138 5.890 9.987 6.851 1.00 7.11 C ANISOU 1069 CE1 TYR A 138 721 1005 974 13 122 237 C ATOM 1070 CE2 TYR A 138 7.806 9.831 8.231 1.00 6.79 C ANISOU 1070 CE2 TYR A 138 738 976 866 0 123 181 C ATOM 1071 CZ TYR A 138 7.266 10.061 7.004 1.00 6.67 C ANISOU 1071 CZ TYR A 138 781 867 884 38 203 257 C ATOM 1072 OH TYR A 138 8.084 10.403 5.959 1.00 8.35 O ANISOU 1072 OH TYR A 138 965 1139 1069 -12 299 355 O ATOM 1073 N SER A 139 5.525 5.767 10.603 1.00 6.41 N ANISOU 1073 N SER A 139 777 852 804 30 -66 -135 N ATOM 1074 CA SER A 139 6.415 4.715 11.054 1.00 6.72 C ANISOU 1074 CA SER A 139 817 906 829 49 -32 -96 C ATOM 1075 C SER A 139 7.347 4.326 9.941 1.00 7.28 C ANISOU 1075 C SER A 139 844 1032 889 100 -30 -33 C ATOM 1076 O SER A 139 6.883 3.926 8.858 1.00 7.79 O ANISOU 1076 O SER A 139 920 1152 888 52 -70 -120 O ATOM 1077 CB SER A 139 5.626 3.481 11.493 1.00 6.98 C ANISOU 1077 CB SER A 139 805 877 970 87 -68 -32 C ATOM 1078 OG SER A 139 6.489 2.428 11.919 1.00 7.96 O ANISOU 1078 OG SER A 139 907 935 1183 62 -101 86 O ATOM 1079 N TYR A 140 8.662 4.446 10.155 1.00 6.74 N ANISOU 1079 N TYR A 140 723 1055 781 164 40 -93 N ATOM 1080 CA TYR A 140 9.609 4.156 9.093 1.00 6.94 C ANISOU 1080 CA TYR A 140 883 1003 750 58 68 27 C ATOM 1081 C TYR A 140 10.763 3.308 9.568 1.00 6.05 C ANISOU 1081 C TYR A 140 757 878 662 36 2 -15 C ATOM 1082 O TYR A 140 11.095 3.286 10.755 1.00 6.70 O ANISOU 1082 O TYR A 140 805 1026 713 84 89 20 O ATOM 1083 CB TYR A 140 10.016 5.436 8.376 1.00 7.39 C ANISOU 1083 CB TYR A 140 879 1075 852 108 63 59 C ATOM 1084 CG TYR A 140 10.764 6.460 9.183 1.00 7.77 C ANISOU 1084 CG TYR A 140 977 968 1005 128 120 100 C ATOM 1085 CD1 TYR A 140 12.127 6.522 9.129 1.00 10.17 C ANISOU 1085 CD1 TYR A 140 1223 1338 1302 -42 -26 0 C ATOM 1086 CD2 TYR A 140 10.094 7.424 9.946 1.00 8.20 C ANISOU 1086 CD2 TYR A 140 996 1073 1044 103 -164 138 C ATOM 1087 CE1 TYR A 140 12.827 7.449 9.834 1.00 10.81 C ANISOU 1087 CE1 TYR A 140 1369 1439 1297 -246 65 10 C ATOM 1088 CE2 TYR A 140 10.786 8.400 10.656 1.00 10.01 C ANISOU 1088 CE2 TYR A 140 1468 1124 1209 141 -44 5 C ATOM 1089 CZ TYR A 140 12.169 8.413 10.572 1.00 9.60 C ANISOU 1089 CZ TYR A 140 1434 1046 1166 -268 -12 120 C ATOM 1090 OH TYR A 140 12.905 9.323 11.293 1.00 12.95 O ANISOU 1090 OH TYR A 140 1859 1520 1539 -502 -74 -36 O ATOM 1091 N LEU A 141 11.349 2.586 8.623 1.00 5.68 N ANISOU 1091 N LEU A 141 645 924 586 91 43 30 N ATOM 1092 CA LEU A 141 12.504 1.756 8.865 1.00 6.00 C ANISOU 1092 CA LEU A 141 743 939 596 82 55 -40 C ATOM 1093 C LEU A 141 13.696 2.415 8.166 1.00 5.90 C ANISOU 1093 C LEU A 141 710 979 550 25 56 42 C ATOM 1094 O LEU A 141 13.585 2.851 7.021 1.00 7.80 O ANISOU 1094 O LEU A 141 744 1556 663 70 38 291 O ATOM 1095 CB LEU A 141 12.326 0.342 8.262 1.00 6.92 C ANISOU 1095 CB LEU A 141 898 1043 686 19 27 -74 C ATOM 1096 CG LEU A 141 11.135 -0.458 8.746 1.00 8.70 C ANISOU 1096 CG LEU A 141 1121 1070 1111 -6 -56 -164 C ATOM 1097 CD1 LEU A 141 11.081 -1.830 8.077 1.00 10.22 C ANISOU 1097 CD1 LEU A 141 1652 1147 1080 -197 -157 -69 C ATOM 1098 CD2 LEU A 141 11.104 -0.608 10.247 1.00 9.24 C ANISOU 1098 CD2 LEU A 141 1178 1131 1201 -141 115 -46 C ATOM 1099 N VAL A 142 14.861 2.387 8.802 1.00 5.94 N ANISOU 1099 N VAL A 142 670 983 603 4 50 89 N ATOM 1100 CA VAL A 142 16.097 2.834 8.213 1.00 5.62 C ANISOU 1100 CA VAL A 142 686 804 645 -8 44 28 C ATOM 1101 C VAL A 142 17.172 1.789 8.432 1.00 5.07 C ANISOU 1101 C VAL A 142 633 787 505 -36 29 -12 C ATOM 1102 O VAL A 142 17.068 0.937 9.325 1.00 5.52 O ANISOU 1102 O VAL A 142 686 853 559 17 76 14 O ATOM 1103 CB VAL A 142 16.564 4.218 8.743 1.00 6.62 C ANISOU 1103 CB VAL A 142 758 889 869 14 165 39 C ATOM 1104 CG1 VAL A 142 15.454 5.246 8.528 1.00 9.06 C ANISOU 1104 CG1 VAL A 142 1040 1064 1336 62 13 -58 C ATOM 1105 CG2 VAL A 142 16.949 4.160 10.215 1.00 7.37 C ANISOU 1105 CG2 VAL A 142 818 893 1088 -90 138 -81 C ATOM 1106 N ASN A 143 18.223 1.895 7.621 1.00 5.24 N ANISOU 1106 N ASN A 143 571 730 687 -21 117 12 N ATOM 1107 CA ASN A 143 19.294 0.912 7.637 1.00 5.19 C ANISOU 1107 CA ASN A 143 649 647 675 -28 81 -60 C ATOM 1108 C ASN A 143 20.653 1.476 7.999 1.00 4.79 C ANISOU 1108 C ASN A 143 611 623 583 -7 90 -114 C ATOM 1109 O ASN A 143 21.679 0.925 7.608 1.00 5.56 O ANISOU 1109 O ASN A 143 588 902 623 -1 111 -259 O ATOM 1110 CB ASN A 143 19.376 0.153 6.310 1.00 5.63 C ANISOU 1110 CB ASN A 143 674 673 792 -16 -5 -109 C ATOM 1111 CG ASN A 143 19.784 1.040 5.152 1.00 5.81 C ANISOU 1111 CG ASN A 143 592 734 880 -24 60 -120 C ATOM 1112 OD1 ASN A 143 19.722 2.267 5.238 1.00 6.43 O ANISOU 1112 OD1 ASN A 143 1053 700 689 27 102 -54 O ATOM 1113 ND2 ASN A 143 20.198 0.422 4.041 1.00 7.75 N ANISOU 1113 ND2 ASN A 143 1002 1127 815 -126 188 -311 N ATOM 1114 N ASP A 144 20.679 2.535 8.793 1.00 5.46 N ANISOU 1114 N ASP A 144 695 775 602 -19 99 -135 N ATOM 1115 CA ASP A 144 21.929 2.985 9.383 1.00 5.00 C ANISOU 1115 CA ASP A 144 665 674 557 8 121 -147 C ATOM 1116 C ASP A 144 21.565 3.827 10.595 1.00 5.29 C ANISOU 1116 C ASP A 144 617 791 600 2 184 -157 C ATOM 1117 O ASP A 144 20.401 4.177 10.792 1.00 6.91 O ANISOU 1117 O ASP A 144 773 1120 730 95 90 -350 O ATOM 1118 CB ASP A 144 22.804 3.781 8.380 1.00 5.66 C ANISOU 1118 CB ASP A 144 683 782 685 28 144 -121 C ATOM 1119 CG ASP A 144 24.280 3.613 8.601 1.00 7.57 C ANISOU 1119 CG ASP A 144 1060 920 896 -64 207 -120 C ATOM 1120 OD1 ASP A 144 24.710 3.176 9.702 1.00 6.46 O ANISOU 1120 OD1 ASP A 144 720 738 996 -25 32 -264 O ATOM 1121 OD2 ASP A 144 25.084 3.907 7.693 1.00 9.73 O ANISOU 1121 OD2 ASP A 144 973 1417 1306 78 350 175 O ATOM 1122 N TYR A 145 22.577 4.100 11.394 1.00 6.19 N ANISOU 1122 N TYR A 145 824 944 581 37 140 -241 N ATOM 1123 CA TYR A 145 22.429 4.796 12.667 1.00 6.44 C ANISOU 1123 CA TYR A 145 937 883 627 19 120 -214 C ATOM 1124 C TYR A 145 23.176 6.116 12.596 1.00 7.91 C ANISOU 1124 C TYR A 145 1249 959 797 48 136 -183 C ATOM 1125 O TYR A 145 24.155 6.286 11.883 1.00 7.18 O ANISOU 1125 O TYR A 145 1306 663 757 -55 108 -291 O ATOM 1126 CB TYR A 145 23.005 3.954 13.823 1.00 6.69 C ANISOU 1126 CB TYR A 145 935 1004 601 -56 161 -174 C ATOM 1127 CG TYR A 145 22.566 2.518 13.803 1.00 5.05 C ANISOU 1127 CG TYR A 145 687 777 454 -212 115 -144 C ATOM 1128 CD1 TYR A 145 23.491 1.507 13.660 1.00 5.76 C ANISOU 1128 CD1 TYR A 145 512 1156 521 -101 208 -20 C ATOM 1129 CD2 TYR A 145 21.237 2.162 13.911 1.00 6.13 C ANISOU 1129 CD2 TYR A 145 568 974 787 -73 208 -92 C ATOM 1130 CE1 TYR A 145 23.117 0.180 13.615 1.00 7.46 C ANISOU 1130 CE1 TYR A 145 857 1187 790 -3 40 -215 C ATOM 1131 CE2 TYR A 145 20.849 0.836 13.875 1.00 6.00 C ANISOU 1131 CE2 TYR A 145 512 1097 670 -70 247 -204 C ATOM 1132 CZ TYR A 145 21.782 -0.149 13.735 1.00 5.83 C ANISOU 1132 CZ TYR A 145 696 1066 452 -177 182 -142 C ATOM 1133 OH TYR A 145 21.345 -1.469 13.693 1.00 6.80 O ANISOU 1133 OH TYR A 145 838 1060 684 -269 200 -144 O ATOM 1134 N ATRP A 146 22.700 7.081 13.356 0.70 9.80 N ANISOU 1134 N ATRP A 146 1536 1164 1023 55 128 -240 N ATOM 1135 CA ATRP A 146 23.354 8.372 13.420 0.70 11.33 C ANISOU 1135 CA ATRP A 146 1810 1269 1225 0 89 -156 C ATOM 1136 C ATRP A 146 24.839 8.226 13.845 0.70 10.87 C ANISOU 1136 C ATRP A 146 1828 1137 1164 -119 21 -239 C ATOM 1137 O ATRP A 146 25.134 7.462 14.763 0.70 12.12 O ANISOU 1137 O ATRP A 146 2267 1119 1218 -316 -54 -189 O ATOM 1138 CB ATRP A 146 22.567 9.230 14.418 0.70 12.53 C ANISOU 1138 CB ATRP A 146 1969 1427 1365 70 131 -243 C ATOM 1139 CG ATRP A 146 22.775 10.651 14.248 0.70 16.44 C ANISOU 1139 CG ATRP A 146 2366 2020 1860 -55 29 -58 C ATOM 1140 CD1ATRP A 146 22.044 11.501 13.489 0.70 19.00 C ANISOU 1140 CD1ATRP A 146 2722 2125 2369 -44 65 -239 C ATOM 1141 CD2ATRP A 146 23.822 11.414 14.826 0.70 18.98 C ANISOU 1141 CD2ATRP A 146 2810 2207 2192 -85 0 -213 C ATOM 1142 NE1ATRP A 146 22.570 12.768 13.562 0.70 20.70 N ANISOU 1142 NE1ATRP A 146 3092 2273 2499 -99 92 -278 N ATOM 1143 CE2ATRP A 146 23.676 12.735 14.371 0.70 20.72 C ANISOU 1143 CE2ATRP A 146 2848 2487 2535 -49 -17 -146 C ATOM 1144 CE3ATRP A 146 24.892 11.109 15.674 0.70 20.54 C ANISOU 1144 CE3ATRP A 146 2883 2523 2396 -84 -36 -156 C ATOM 1145 CZ2ATRP A 146 24.528 13.759 14.768 0.70 19.58 C ANISOU 1145 CZ2ATRP A 146 2804 2256 2379 -148 -46 -195 C ATOM 1146 CZ3ATRP A 146 25.750 12.123 16.056 0.70 20.72 C ANISOU 1146 CZ3ATRP A 146 2817 2482 2572 -37 -62 -113 C ATOM 1147 CH2ATRP A 146 25.571 13.428 15.594 0.70 21.16 C ANISOU 1147 CH2ATRP A 146 2807 2574 2656 -8 -39 -61 C ATOM 1148 N ALA A 147 25.767 8.919 13.164 1.00 10.48 N ANISOU 1148 N ALA A 147 1759 1123 1100 -118 46 -178 N ATOM 1149 CA ALA A 147 27.189 8.942 13.488 1.00 11.25 C ANISOU 1149 CA ALA A 147 1753 1281 1239 -133 32 -79 C ATOM 1150 C ALA A 147 27.736 10.319 13.105 1.00 11.42 C ANISOU 1150 C ALA A 147 1789 1272 1277 -224 -30 -104 C ATOM 1151 O ALA A 147 27.278 10.938 12.147 1.00 10.89 O ANISOU 1151 O ALA A 147 2002 1169 964 -381 -32 -215 O ATOM 1152 CB ALA A 147 27.940 7.862 12.771 1.00 11.98 C ANISOU 1152 CB ALA A 147 1820 1377 1353 -76 -71 -77 C ATOM 1153 N LEU A 148 28.710 10.806 13.864 1.00 11.69 N ANISOU 1153 N LEU A 148 1940 1231 1269 -203 -109 -88 N ATOM 1154 CA LEU A 148 29.275 12.115 13.584 1.00 11.50 C ANISOU 1154 CA LEU A 148 1748 1264 1358 -145 -54 -94 C ATOM 1155 C LEU A 148 29.826 12.173 12.167 1.00 11.19 C ANISOU 1155 C LEU A 148 1666 1269 1313 -87 -117 -131 C ATOM 1156 O LEU A 148 29.660 13.172 11.489 1.00 11.00 O ANISOU 1156 O LEU A 148 1963 1112 1103 -136 -162 -218 O ATOM 1157 CB LEU A 148 30.374 12.436 14.597 1.00 11.73 C ANISOU 1157 CB LEU A 148 1780 1272 1405 -119 -48 -96 C ATOM 1158 CG LEU A 148 31.088 13.781 14.456 1.00 13.11 C ANISOU 1158 CG LEU A 148 1814 1554 1610 -147 -110 -83 C ATOM 1159 CD1 LEU A 148 30.105 14.918 14.554 1.00 14.75 C ANISOU 1159 CD1 LEU A 148 2057 1697 1850 -74 -133 -92 C ATOM 1160 CD2 LEU A 148 32.159 13.928 15.510 1.00 14.53 C ANISOU 1160 CD2 LEU A 148 2114 1754 1650 11 -162 -133 C ATOM 1161 N GLU A 149 30.436 11.072 11.717 1.00 12.05 N ANISOU 1161 N GLU A 149 1691 1433 1452 -12 -81 -118 N ATOM 1162 CA GLU A 149 31.073 11.011 10.405 1.00 12.79 C ANISOU 1162 CA GLU A 149 1679 1602 1575 59 -31 -99 C ATOM 1163 C GLU A 149 30.059 11.124 9.266 1.00 11.63 C ANISOU 1163 C GLU A 149 1567 1495 1357 38 -18 -93 C ATOM 1164 O GLU A 149 30.431 11.458 8.150 1.00 12.20 O ANISOU 1164 O GLU A 149 1561 1576 1498 70 109 -160 O ATOM 1165 CB GLU A 149 31.923 9.719 10.265 1.00 14.28 C ANISOU 1165 CB GLU A 149 1828 1847 1749 87 -56 -67 C ATOM 1166 CG GLU A 149 31.116 8.434 10.127 1.00 18.50 C ANISOU 1166 CG GLU A 149 2366 2319 2344 165 22 -18 C ATOM 1167 CD GLU A 149 31.778 7.193 10.722 1.00 22.89 C ANISOU 1167 CD GLU A 149 2734 2936 3025 104 134 61 C ATOM 1168 OE1 GLU A 149 33.024 7.064 10.676 1.00 26.16 O ANISOU 1168 OE1 GLU A 149 2951 3631 3355 297 85 60 O ATOM 1169 OE2 GLU A 149 31.035 6.317 11.220 1.00 27.01 O ANISOU 1169 OE2 GLU A 149 3186 3510 3567 73 444 137 O ATOM 1170 N LEU A 150 28.786 10.853 9.555 1.00 10.31 N ANISOU 1170 N LEU A 150 1417 1340 1157 85 3 -129 N ATOM 1171 CA LEU A 150 27.717 10.977 8.546 1.00 9.38 C ANISOU 1171 CA LEU A 150 1283 1198 1080 108 20 -79 C ATOM 1172 C LEU A 150 27.134 12.367 8.419 1.00 10.30 C ANISOU 1172 C LEU A 150 1399 1236 1277 92 -28 -95 C ATOM 1173 O LEU A 150 26.431 12.647 7.473 1.00 10.00 O ANISOU 1173 O LEU A 150 1357 1228 1214 128 5 -144 O ATOM 1174 CB LEU A 150 26.583 10.004 8.842 1.00 9.02 C ANISOU 1174 CB LEU A 150 1328 1092 1007 115 55 -70 C ATOM 1175 CG LEU A 150 26.967 8.537 8.644 1.00 8.99 C ANISOU 1175 CG LEU A 150 1229 1087 1098 154 10 -127 C ATOM 1176 CD1 LEU A 150 25.792 7.668 9.041 1.00 10.00 C ANISOU 1176 CD1 LEU A 150 1449 1220 1130 13 100 -269 C ATOM 1177 CD2 LEU A 150 27.420 8.252 7.187 1.00 10.74 C ANISOU 1177 CD2 LEU A 150 1605 1222 1253 -128 152 -98 C ATOM 1178 N LYS A 151 27.465 13.249 9.355 1.00 12.00 N ANISOU 1178 N LYS A 151 1598 1485 1476 110 -132 -63 N ATOM 1179 CA LYS A 151 26.872 14.573 9.383 1.00 13.43 C ANISOU 1179 CA LYS A 151 1759 1577 1764 31 8 -67 C ATOM 1180 C LYS A 151 27.068 15.329 8.062 1.00 13.00 C ANISOU 1180 C LYS A 151 1722 1485 1731 20 -46 -64 C ATOM 1181 O LYS A 151 26.110 15.897 7.540 1.00 12.48 O ANISOU 1181 O LYS A 151 1547 1355 1839 100 -34 -18 O ATOM 1182 CB LYS A 151 27.435 15.370 10.560 1.00 14.73 C ANISOU 1182 CB LYS A 151 2027 1692 1875 84 15 -62 C ATOM 1183 CG LYS A 151 26.947 16.784 10.626 1.00 18.49 C ANISOU 1183 CG LYS A 151 2373 2289 2363 175 67 9 C ATOM 1184 CD LYS A 151 27.681 17.596 11.665 1.00 22.01 C ANISOU 1184 CD LYS A 151 2859 2661 2841 99 60 -52 C ATOM 1185 CE LYS A 151 26.836 18.807 12.060 1.00 23.87 C ANISOU 1185 CE LYS A 151 3058 2977 3033 144 13 10 C ATOM 1186 NZ LYS A 151 27.599 19.768 12.867 1.00 25.63 N ANISOU 1186 NZ LYS A 151 3388 3381 2967 -31 -99 -7 N ATOM 1187 N PRO A 152 28.273 15.334 7.499 1.00 13.06 N ANISOU 1187 N PRO A 152 1709 1490 1760 35 -39 -65 N ATOM 1188 CA PRO A 152 28.481 16.018 6.220 1.00 13.27 C ANISOU 1188 CA PRO A 152 1664 1645 1731 2 -13 -7 C ATOM 1189 C PRO A 152 27.750 15.419 5.027 1.00 12.81 C ANISOU 1189 C PRO A 152 1665 1588 1612 -6 -8 12 C ATOM 1190 O PRO A 152 27.764 16.034 3.967 1.00 14.33 O ANISOU 1190 O PRO A 152 1891 1836 1718 -126 -40 109 O ATOM 1191 CB PRO A 152 30.002 15.908 5.985 1.00 14.00 C ANISOU 1191 CB PRO A 152 1663 1823 1833 -53 -24 -23 C ATOM 1192 CG PRO A 152 30.578 15.395 7.202 1.00 14.66 C ANISOU 1192 CG PRO A 152 1890 1753 1926 74 -33 36 C ATOM 1193 CD PRO A 152 29.527 14.770 8.023 1.00 13.48 C ANISOU 1193 CD PRO A 152 1732 1602 1788 19 -44 -107 C ATOM 1194 N LYS A 153 27.110 14.269 5.199 1.00 11.74 N ANISOU 1194 N LYS A 153 1385 1529 1547 18 -35 46 N ATOM 1195 CA LYS A 153 26.481 13.542 4.099 1.00 12.45 C ANISOU 1195 CA LYS A 153 1574 1564 1592 8 9 41 C ATOM 1196 C LYS A 153 24.975 13.767 4.019 1.00 12.08 C ANISOU 1196 C LYS A 153 1519 1531 1539 50 -64 63 C ATOM 1197 O LYS A 153 24.305 13.227 3.142 1.00 14.66 O ANISOU 1197 O LYS A 153 1931 1860 1778 312 -252 112 O ATOM 1198 CB LYS A 153 26.782 12.055 4.206 1.00 12.77 C ANISOU 1198 CB LYS A 153 1539 1625 1686 86 -80 11 C ATOM 1199 CG LYS A 153 28.265 11.702 4.239 1.00 14.49 C ANISOU 1199 CG LYS A 153 1883 1696 1925 -20 -17 -22 C ATOM 1200 CD LYS A 153 29.028 12.277 3.075 1.00 16.67 C ANISOU 1200 CD LYS A 153 2108 2197 2029 49 -48 -149 C ATOM 1201 CE LYS A 153 30.364 11.567 2.889 1.00 18.65 C ANISOU 1201 CE LYS A 153 2338 2497 2248 -17 28 -28 C ATOM 1202 NZ LYS A 153 31.408 12.505 2.395 1.00 21.29 N ANISOU 1202 NZ LYS A 153 2748 2897 2443 -98 51 -197 N ATOM 1203 N TYR A 154 24.434 14.515 4.972 1.00 10.81 N ANISOU 1203 N TYR A 154 1381 1157 1567 110 -103 75 N ATOM 1204 CA TYR A 154 23.046 14.959 4.858 1.00 10.73 C ANISOU 1204 CA TYR A 154 1263 1189 1625 32 -48 205 C ATOM 1205 C TYR A 154 22.927 16.059 3.782 1.00 10.77 C ANISOU 1205 C TYR A 154 1272 1106 1712 7 -38 262 C ATOM 1206 O TYR A 154 23.862 16.831 3.548 1.00 12.03 O ANISOU 1206 O TYR A 154 1322 1188 2060 -66 -148 420 O ATOM 1207 CB TYR A 154 22.559 15.577 6.158 1.00 10.40 C ANISOU 1207 CB TYR A 154 1200 1048 1702 50 -40 227 C ATOM 1208 CG TYR A 154 22.322 14.671 7.353 1.00 10.87 C ANISOU 1208 CG TYR A 154 1218 1270 1640 95 184 197 C ATOM 1209 CD1 TYR A 154 23.377 14.018 7.970 1.00 11.84 C ANISOU 1209 CD1 TYR A 154 1533 1351 1612 126 37 211 C ATOM 1210 CD2 TYR A 154 21.058 14.552 7.936 1.00 12.33 C ANISOU 1210 CD2 TYR A 154 1601 1213 1868 88 183 230 C ATOM 1211 CE1 TYR A 154 23.175 13.245 9.108 1.00 13.66 C ANISOU 1211 CE1 TYR A 154 1904 1421 1863 72 95 153 C ATOM 1212 CE2 TYR A 154 20.842 13.763 9.060 1.00 12.39 C ANISOU 1212 CE2 TYR A 154 1657 1287 1762 -118 235 24 C ATOM 1213 CZ TYR A 154 21.914 13.120 9.641 1.00 13.53 C ANISOU 1213 CZ TYR A 154 2095 1177 1868 -38 158 169 C ATOM 1214 OH TYR A 154 21.739 12.365 10.769 1.00 16.38 O ANISOU 1214 OH TYR A 154 2596 1420 2208 -165 219 122 O ATOM 1215 N ALA A 155 21.766 16.162 3.175 1.00 9.67 N ANISOU 1215 N ALA A 155 1149 900 1624 -104 -22 251 N ATOM 1216 CA ALA A 155 21.419 17.350 2.399 1.00 9.32 C ANISOU 1216 CA ALA A 155 1012 1027 1501 -65 22 193 C ATOM 1217 C ALA A 155 19.980 17.692 2.730 1.00 8.22 C ANISOU 1217 C ALA A 155 896 807 1420 -43 43 154 C ATOM 1218 O ALA A 155 19.195 16.834 3.087 1.00 9.78 O ANISOU 1218 O ALA A 155 1010 949 1757 -134 149 183 O ATOM 1219 CB ALA A 155 21.602 17.112 0.930 1.00 9.60 C ANISOU 1219 CB ALA A 155 1003 1017 1627 42 84 139 C ATOM 1220 N PHE A 156 19.662 18.973 2.615 1.00 7.53 N ANISOU 1220 N PHE A 156 859 755 1245 18 46 241 N ATOM 1221 CA PHE A 156 18.367 19.546 2.949 1.00 7.90 C ANISOU 1221 CA PHE A 156 945 883 1171 57 -30 190 C ATOM 1222 C PHE A 156 17.937 20.507 1.870 1.00 7.08 C ANISOU 1222 C PHE A 156 877 741 1068 -80 -53 163 C ATOM 1223 O PHE A 156 18.770 21.217 1.306 1.00 8.30 O ANISOU 1223 O PHE A 156 925 1021 1206 -50 -121 392 O ATOM 1224 CB PHE A 156 18.416 20.323 4.269 1.00 8.77 C ANISOU 1224 CB PHE A 156 1027 992 1313 86 -5 183 C ATOM 1225 CG PHE A 156 18.956 19.539 5.418 1.00 9.37 C ANISOU 1225 CG PHE A 156 1158 1102 1296 16 -39 100 C ATOM 1226 CD1 PHE A 156 20.299 19.616 5.771 1.00 11.67 C ANISOU 1226 CD1 PHE A 156 1335 1476 1621 56 -183 149 C ATOM 1227 CD2 PHE A 156 18.141 18.685 6.122 1.00 11.47 C ANISOU 1227 CD2 PHE A 156 1502 1534 1321 107 -96 172 C ATOM 1228 CE1 PHE A 156 20.792 18.873 6.841 1.00 13.54 C ANISOU 1228 CE1 PHE A 156 1741 1644 1757 122 -158 74 C ATOM 1229 CE2 PHE A 156 18.649 17.937 7.178 1.00 12.96 C ANISOU 1229 CE2 PHE A 156 1838 1576 1509 168 7 321 C ATOM 1230 CZ PHE A 156 19.966 18.061 7.540 1.00 12.69 C ANISOU 1230 CZ PHE A 156 1753 1491 1577 239 -81 81 C ATOM 1231 N VAL A 157 16.642 20.569 1.613 1.00 6.64 N ANISOU 1231 N VAL A 157 908 707 907 45 41 213 N ATOM 1232 CA VAL A 157 16.130 21.629 0.752 1.00 6.03 C ANISOU 1232 CA VAL A 157 767 714 809 12 -18 118 C ATOM 1233 C VAL A 157 14.844 22.194 1.319 1.00 6.14 C ANISOU 1233 C VAL A 157 783 783 764 44 49 113 C ATOM 1234 O VAL A 157 14.047 21.491 1.932 1.00 6.31 O ANISOU 1234 O VAL A 157 798 799 798 4 16 21 O ATOM 1235 CB VAL A 157 15.964 21.121 -0.705 1.00 6.06 C ANISOU 1235 CB VAL A 157 795 731 775 50 101 15 C ATOM 1236 CG1 VAL A 157 14.940 20.016 -0.823 1.00 6.91 C ANISOU 1236 CG1 VAL A 157 817 796 1010 9 164 -15 C ATOM 1237 CG2 VAL A 157 15.650 22.284 -1.661 1.00 6.28 C ANISOU 1237 CG2 VAL A 157 812 780 791 59 34 -69 C ATOM 1238 N ASN A 158 14.666 23.489 1.119 1.00 5.59 N ANISOU 1238 N ASN A 158 682 677 763 -34 4 110 N ATOM 1239 CA ASN A 158 13.564 24.216 1.732 1.00 5.80 C ANISOU 1239 CA ASN A 158 801 722 677 3 34 128 C ATOM 1240 C ASN A 158 12.213 23.817 1.167 1.00 5.97 C ANISOU 1240 C ASN A 158 774 724 767 89 48 83 C ATOM 1241 O ASN A 158 11.984 23.931 -0.027 1.00 6.82 O ANISOU 1241 O ASN A 158 835 982 774 53 -11 123 O ATOM 1242 CB ASN A 158 13.765 25.727 1.562 1.00 6.11 C ANISOU 1242 CB ASN A 158 740 769 812 -46 -7 16 C ATOM 1243 CG ASN A 158 12.975 26.531 2.559 1.00 6.88 C ANISOU 1243 CG ASN A 158 839 808 964 88 -166 -12 C ATOM 1244 OD1 ASN A 158 11.754 26.653 2.432 1.00 8.46 O ANISOU 1244 OD1 ASN A 158 1098 1074 1042 187 -27 -288 O ATOM 1245 ND2 ASN A 158 13.659 27.090 3.560 1.00 8.27 N ANISOU 1245 ND2 ASN A 158 1233 931 977 -20 -206 -63 N ATOM 1246 N TYR A 159 11.294 23.447 2.060 1.00 5.98 N ANISOU 1246 N TYR A 159 853 771 647 41 46 47 N ATOM 1247 CA TYR A 159 9.945 23.037 1.680 1.00 6.05 C ANISOU 1247 CA TYR A 159 790 814 693 45 12 103 C ATOM 1248 C TYR A 159 9.207 24.100 0.862 1.00 6.95 C ANISOU 1248 C TYR A 159 855 939 847 -41 -26 142 C ATOM 1249 O TYR A 159 8.337 23.761 0.056 1.00 7.04 O ANISOU 1249 O TYR A 159 764 1097 812 -20 -42 172 O ATOM 1250 CB TYR A 159 9.104 22.664 2.924 1.00 7.35 C ANISOU 1250 CB TYR A 159 1007 951 832 -35 -13 197 C ATOM 1251 CG TYR A 159 8.613 23.856 3.693 1.00 7.51 C ANISOU 1251 CG TYR A 159 1070 1022 761 38 106 156 C ATOM 1252 CD1 TYR A 159 7.302 24.286 3.561 1.00 8.49 C ANISOU 1252 CD1 TYR A 159 1028 1085 1110 66 -36 15 C ATOM 1253 CD2 TYR A 159 9.455 24.596 4.507 1.00 7.81 C ANISOU 1253 CD2 TYR A 159 1030 1229 706 220 17 143 C ATOM 1254 CE1 TYR A 159 6.855 25.402 4.228 1.00 8.35 C ANISOU 1254 CE1 TYR A 159 990 1274 907 205 87 -72 C ATOM 1255 CE2 TYR A 159 9.003 25.717 5.177 1.00 9.12 C ANISOU 1255 CE2 TYR A 159 1253 1237 972 7 37 -16 C ATOM 1256 CZ TYR A 159 7.702 26.119 5.038 1.00 9.12 C ANISOU 1256 CZ TYR A 159 1380 1163 921 156 -40 95 C ATOM 1257 OH TYR A 159 7.258 27.232 5.719 1.00 12.00 O ANISOU 1257 OH TYR A 159 1709 1427 1422 391 -2 -116 O ATOM 1258 N ALA A 160 9.570 25.359 1.096 1.00 6.61 N ANISOU 1258 N ALA A 160 853 855 802 69 46 156 N ATOM 1259 CA ALA A 160 8.838 26.499 0.533 1.00 6.90 C ANISOU 1259 CA ALA A 160 900 847 875 159 69 105 C ATOM 1260 C ALA A 160 9.542 27.137 -0.675 1.00 7.25 C ANISOU 1260 C ALA A 160 921 850 980 168 186 133 C ATOM 1261 O ALA A 160 9.117 28.212 -1.130 1.00 8.66 O ANISOU 1261 O ALA A 160 1176 1011 1102 323 285 119 O ATOM 1262 CB ALA A 160 8.557 27.563 1.601 1.00 7.77 C ANISOU 1262 CB ALA A 160 1002 994 954 164 72 -16 C ATOM 1263 N ASP A 161 10.590 26.493 -1.211 1.00 6.69 N ANISOU 1263 N ASP A 161 891 763 886 204 73 123 N ATOM 1264 CA ASP A 161 11.218 27.010 -2.432 1.00 6.33 C ANISOU 1264 CA ASP A 161 807 723 873 118 93 35 C ATOM 1265 C ASP A 161 10.216 26.876 -3.559 1.00 6.61 C ANISOU 1265 C ASP A 161 833 776 902 95 156 99 C ATOM 1266 O ASP A 161 9.864 25.738 -3.932 1.00 6.35 O ANISOU 1266 O ASP A 161 647 843 922 122 88 188 O ATOM 1267 CB ASP A 161 12.465 26.190 -2.735 1.00 6.21 C ANISOU 1267 CB ASP A 161 667 810 880 172 63 49 C ATOM 1268 CG ASP A 161 13.153 26.597 -3.991 1.00 6.06 C ANISOU 1268 CG ASP A 161 751 618 933 124 -117 26 C ATOM 1269 OD1 ASP A 161 12.586 27.376 -4.797 1.00 6.71 O ANISOU 1269 OD1 ASP A 161 715 831 1002 80 167 433 O ATOM 1270 OD2 ASP A 161 14.276 26.164 -4.244 1.00 6.65 O ANISOU 1270 OD2 ASP A 161 707 893 924 88 166 46 O ATOM 1271 N PRO A 162 9.724 28.003 -4.104 1.00 7.10 N ANISOU 1271 N PRO A 162 892 882 921 103 98 67 N ATOM 1272 CA PRO A 162 8.618 27.922 -5.060 1.00 8.10 C ANISOU 1272 CA PRO A 162 987 1037 1054 111 27 24 C ATOM 1273 C PRO A 162 9.023 27.344 -6.417 1.00 8.37 C ANISOU 1273 C PRO A 162 1071 1099 1010 109 -49 49 C ATOM 1274 O PRO A 162 8.147 27.056 -7.238 1.00 10.64 O ANISOU 1274 O PRO A 162 1083 1601 1356 92 -101 24 O ATOM 1275 CB PRO A 162 8.179 29.394 -5.207 1.00 8.60 C ANISOU 1275 CB PRO A 162 1087 1056 1123 234 16 88 C ATOM 1276 CG PRO A 162 9.361 30.160 -4.929 1.00 8.48 C ANISOU 1276 CG PRO A 162 1147 970 1105 210 8 95 C ATOM 1277 CD PRO A 162 10.129 29.417 -3.880 1.00 6.75 C ANISOU 1277 CD PRO A 162 922 821 819 70 122 78 C ATOM 1278 N SER A 163 10.319 27.211 -6.674 1.00 7.76 N ANISOU 1278 N SER A 163 1053 926 970 -5 52 170 N ATOM 1279 CA SER A 163 10.790 26.592 -7.902 1.00 8.77 C ANISOU 1279 CA SER A 163 1215 1050 1065 3 27 51 C ATOM 1280 C SER A 163 10.751 25.068 -7.911 1.00 8.19 C ANISOU 1280 C SER A 163 1144 972 994 -2 130 45 C ATOM 1281 O SER A 163 10.912 24.442 -8.960 1.00 9.30 O ANISOU 1281 O SER A 163 1406 1157 970 -117 156 64 O ATOM 1282 CB SER A 163 12.209 27.029 -8.214 1.00 9.85 C ANISOU 1282 CB SER A 163 1290 1250 1203 -36 43 -18 C ATOM 1283 OG SER A 163 13.152 26.520 -7.323 1.00 13.74 O ANISOU 1283 OG SER A 163 1689 1791 1737 -218 186 51 O ATOM 1284 N LEU A 164 10.554 24.451 -6.747 1.00 6.67 N ANISOU 1284 N LEU A 164 883 838 812 29 38 115 N ATOM 1285 CA LEU A 164 10.406 23.000 -6.666 1.00 7.21 C ANISOU 1285 CA LEU A 164 892 911 934 37 80 57 C ATOM 1286 C LEU A 164 9.099 22.604 -7.314 1.00 6.80 C ANISOU 1286 C LEU A 164 946 826 810 24 50 98 C ATOM 1287 O LEU A 164 8.076 23.279 -7.134 1.00 6.64 O ANISOU 1287 O LEU A 164 757 876 888 132 -57 -24 O ATOM 1288 CB LEU A 164 10.394 22.535 -5.204 1.00 6.77 C ANISOU 1288 CB LEU A 164 881 844 846 25 -62 77 C ATOM 1289 CG LEU A 164 11.728 22.699 -4.455 1.00 7.88 C ANISOU 1289 CG LEU A 164 952 907 1135 -121 54 13 C ATOM 1290 CD1 LEU A 164 11.526 22.328 -2.981 1.00 8.14 C ANISOU 1290 CD1 LEU A 164 1060 877 1156 -40 29 323 C ATOM 1291 CD2 LEU A 164 12.836 21.844 -5.071 1.00 9.76 C ANISOU 1291 CD2 LEU A 164 1007 1256 1445 -112 64 15 C ATOM 1292 N ASP A 165 9.111 21.490 -8.031 1.00 6.82 N ANISOU 1292 N ASP A 165 986 798 806 93 67 77 N ATOM 1293 CA ASP A 165 7.936 20.974 -8.690 1.00 7.87 C ANISOU 1293 CA ASP A 165 1117 963 910 53 38 11 C ATOM 1294 C ASP A 165 7.078 20.170 -7.712 1.00 7.27 C ANISOU 1294 C ASP A 165 999 875 889 -6 21 -48 C ATOM 1295 O ASP A 165 6.840 18.963 -7.883 1.00 7.68 O ANISOU 1295 O ASP A 165 1026 932 958 -30 -20 27 O ATOM 1296 CB ASP A 165 8.359 20.152 -9.908 1.00 8.43 C ANISOU 1296 CB ASP A 165 1117 1139 946 8 89 -95 C ATOM 1297 CG ASP A 165 7.193 19.685 -10.734 1.00 11.36 C ANISOU 1297 CG ASP A 165 1523 1658 1135 -8 178 -270 C ATOM 1298 OD1 ASP A 165 6.108 20.315 -10.691 1.00 13.51 O ANISOU 1298 OD1 ASP A 165 1645 2094 1393 -87 -276 -255 O ATOM 1299 OD2 ASP A 165 7.292 18.683 -11.468 1.00 15.66 O ANISOU 1299 OD2 ASP A 165 2274 1915 1758 -177 348 -791 O ATOM 1300 N ILE A 166 6.608 20.860 -6.666 1.00 7.30 N ANISOU 1300 N ILE A 166 1039 847 888 -35 43 -40 N ATOM 1301 CA ILE A 166 5.745 20.311 -5.613 1.00 6.89 C ANISOU 1301 CA ILE A 166 850 867 898 -39 26 -23 C ATOM 1302 C ILE A 166 4.735 21.352 -5.203 1.00 6.85 C ANISOU 1302 C ILE A 166 856 858 886 -22 31 29 C ATOM 1303 O ILE A 166 4.938 22.536 -5.434 1.00 7.56 O ANISOU 1303 O ILE A 166 918 1014 941 -50 48 143 O ATOM 1304 CB ILE A 166 6.572 19.871 -4.381 1.00 7.33 C ANISOU 1304 CB ILE A 166 896 918 970 -41 21 65 C ATOM 1305 CG1 ILE A 166 7.189 21.085 -3.650 1.00 6.93 C ANISOU 1305 CG1 ILE A 166 717 1066 849 -52 -34 -4 C ATOM 1306 CG2 ILE A 166 7.617 18.840 -4.780 1.00 7.74 C ANISOU 1306 CG2 ILE A 166 921 1057 962 2 20 -1 C ATOM 1307 CD1 ILE A 166 7.945 20.742 -2.400 1.00 7.59 C ANISOU 1307 CD1 ILE A 166 1084 926 871 -79 66 -2 C ATOM 1308 N LYS A 167 3.660 20.914 -4.584 1.00 6.52 N ANISOU 1308 N LYS A 167 772 797 908 79 17 -44 N ATOM 1309 CA LYS A 167 2.743 21.815 -3.902 1.00 6.84 C ANISOU 1309 CA LYS A 167 814 843 942 80 14 -5 C ATOM 1310 C LYS A 167 2.345 21.161 -2.603 1.00 6.48 C ANISOU 1310 C LYS A 167 843 768 849 66 9 3 C ATOM 1311 O LYS A 167 2.167 19.944 -2.533 1.00 7.88 O ANISOU 1311 O LYS A 167 1205 770 1016 32 173 -30 O ATOM 1312 CB LYS A 167 1.484 22.047 -4.746 1.00 8.78 C ANISOU 1312 CB LYS A 167 984 1264 1087 122 33 112 C ATOM 1313 CG LYS A 167 1.715 22.663 -6.091 1.00 12.88 C ANISOU 1313 CG LYS A 167 1390 1891 1611 88 -21 34 C ATOM 1314 CD LYS A 167 2.071 24.109 -5.977 1.00 16.46 C ANISOU 1314 CD LYS A 167 2018 2181 2053 149 32 114 C ATOM 1315 CE LYS A 167 1.939 24.788 -7.325 1.00 19.73 C ANISOU 1315 CE LYS A 167 2466 2609 2421 -45 58 -10 C ATOM 1316 NZ LYS A 167 2.732 26.028 -7.410 1.00 22.01 N ANISOU 1316 NZ LYS A 167 2739 2805 2818 -36 -3 -96 N ATOM 1317 N TRP A 168 2.145 21.979 -1.575 1.00 6.54 N ANISOU 1317 N TRP A 168 1075 554 852 -10 94 -26 N ATOM 1318 CA TRP A 168 1.668 21.493 -0.296 1.00 7.22 C ANISOU 1318 CA TRP A 168 980 885 877 10 6 -34 C ATOM 1319 C TRP A 168 0.163 21.691 -0.158 1.00 8.42 C ANISOU 1319 C TRP A 168 1112 1052 1031 71 10 -33 C ATOM 1320 O TRP A 168 -0.439 22.528 -0.854 1.00 9.26 O ANISOU 1320 O TRP A 168 1085 1332 1099 216 -4 4 O ATOM 1321 CB TRP A 168 2.426 22.186 0.828 1.00 7.32 C ANISOU 1321 CB TRP A 168 987 897 895 5 46 -105 C ATOM 1322 CG TRP A 168 3.884 21.889 0.825 1.00 7.81 C ANISOU 1322 CG TRP A 168 1117 1043 807 -90 167 -77 C ATOM 1323 CD1 TRP A 168 4.885 22.698 0.369 1.00 7.99 C ANISOU 1323 CD1 TRP A 168 1167 1011 856 -71 46 25 C ATOM 1324 CD2 TRP A 168 4.508 20.659 1.220 1.00 6.97 C ANISOU 1324 CD2 TRP A 168 901 935 811 -9 306 -78 C ATOM 1325 NE1 TRP A 168 6.095 22.064 0.502 1.00 8.66 N ANISOU 1325 NE1 TRP A 168 1016 1181 1091 -132 195 -17 N ATOM 1326 CE2 TRP A 168 5.896 20.813 1.027 1.00 7.58 C ANISOU 1326 CE2 TRP A 168 1087 1025 767 52 230 -60 C ATOM 1327 CE3 TRP A 168 4.040 19.461 1.779 1.00 7.76 C ANISOU 1327 CE3 TRP A 168 1063 1085 801 12 225 -50 C ATOM 1328 CZ2 TRP A 168 6.814 19.828 1.364 1.00 7.42 C ANISOU 1328 CZ2 TRP A 168 901 1038 881 -77 172 -258 C ATOM 1329 CZ3 TRP A 168 4.959 18.492 2.132 1.00 8.50 C ANISOU 1329 CZ3 TRP A 168 1314 959 956 38 166 -168 C ATOM 1330 CH2 TRP A 168 6.326 18.673 1.903 1.00 7.55 C ANISOU 1330 CH2 TRP A 168 1116 838 916 67 73 -99 C ATOM 1331 N GLU A 169 -0.440 20.920 0.739 1.00 8.78 N ANISOU 1331 N GLU A 169 1020 1077 1237 -21 -45 -59 N ATOM 1332 CA GLU A 169 -1.879 20.998 0.989 1.00 9.87 C ANISOU 1332 CA GLU A 169 1239 1202 1308 -8 7 -83 C ATOM 1333 C GLU A 169 -2.263 22.351 1.552 1.00 9.30 C ANISOU 1333 C GLU A 169 1152 1113 1265 72 38 -35 C ATOM 1334 O GLU A 169 -3.227 22.962 1.118 1.00 9.95 O ANISOU 1334 O GLU A 169 1201 1245 1334 113 -29 -121 O ATOM 1335 CB GLU A 169 -2.279 19.875 1.961 1.00 10.80 C ANISOU 1335 CB GLU A 169 1276 1347 1480 -1 19 -47 C ATOM 1336 CG GLU A 169 -3.710 19.893 2.449 1.00 14.11 C ANISOU 1336 CG GLU A 169 1634 1771 1955 -27 24 -52 C ATOM 1337 CD GLU A 169 -4.717 19.588 1.377 1.00 18.67 C ANISOU 1337 CD GLU A 169 1945 2734 2412 6 -17 -232 C ATOM 1338 OE1 GLU A 169 -4.378 18.902 0.383 1.00 21.15 O ANISOU 1338 OE1 GLU A 169 2246 3140 2649 -77 -95 -391 O ATOM 1339 OE2 GLU A 169 -5.873 20.046 1.545 1.00 23.36 O ANISOU 1339 OE2 GLU A 169 2227 3689 2959 -165 -68 -271 O ATOM 1340 N ASN A 170 -1.516 22.801 2.538 1.00 8.00 N ANISOU 1340 N ASN A 170 1023 877 1138 79 90 29 N ATOM 1341 CA ASN A 170 -1.862 24.027 3.230 1.00 8.44 C ANISOU 1341 CA ASN A 170 1104 994 1105 23 27 46 C ATOM 1342 C ASN A 170 -0.591 24.714 3.682 1.00 9.11 C ANISOU 1342 C ASN A 170 1241 1007 1212 -29 9 59 C ATOM 1343 O ASN A 170 -0.086 24.524 4.779 1.00 8.13 O ANISOU 1343 O ASN A 170 1323 788 979 -54 13 -4 O ATOM 1344 CB ASN A 170 -2.804 23.741 4.402 1.00 9.44 C ANISOU 1344 CB ASN A 170 1246 1086 1254 -41 92 5 C ATOM 1345 CG ASN A 170 -3.430 24.994 4.951 1.00 11.42 C ANISOU 1345 CG ASN A 170 1403 1286 1646 -123 193 -59 C ATOM 1346 OD1 ASN A 170 -2.870 26.097 4.835 1.00 10.15 O ANISOU 1346 OD1 ASN A 170 1300 947 1608 -184 363 -57 O ATOM 1347 ND2 ASN A 170 -4.613 24.847 5.527 1.00 14.94 N ANISOU 1347 ND2 ASN A 170 1520 1945 2209 -52 434 -221 N ATOM 1348 N LEU A 171 -0.016 25.466 2.773 1.00 10.30 N ANISOU 1348 N LEU A 171 1444 1173 1294 -67 -111 215 N ATOM 1349 CA LEU A 171 1.214 26.147 3.032 1.00 11.44 C ANISOU 1349 CA LEU A 171 1495 1439 1413 -62 -101 254 C ATOM 1350 C LEU A 171 0.955 27.240 4.083 1.00 11.70 C ANISOU 1350 C LEU A 171 1545 1422 1477 -118 -148 212 C ATOM 1351 O LEU A 171 1.772 27.407 5.000 1.00 13.08 O ANISOU 1351 O LEU A 171 1830 1566 1571 -104 -353 293 O ATOM 1352 CB LEU A 171 1.789 26.673 1.705 1.00 11.92 C ANISOU 1352 CB LEU A 171 1607 1460 1461 -102 -98 323 C ATOM 1353 CG LEU A 171 3.105 27.400 1.755 1.00 13.56 C ANISOU 1353 CG LEU A 171 1701 1705 1745 87 -92 127 C ATOM 1354 CD1 LEU A 171 4.185 26.475 2.199 1.00 14.52 C ANISOU 1354 CD1 LEU A 171 1694 1970 1850 120 -5 125 C ATOM 1355 CD2 LEU A 171 3.384 27.961 0.382 1.00 14.80 C ANISOU 1355 CD2 LEU A 171 1928 1969 1725 45 -16 85 C ATOM 1356 N GLU A 172 -0.192 27.940 3.998 1.00 11.68 N ANISOU 1356 N GLU A 172 1614 1317 1506 -32 -163 125 N ATOM 1357 CA GLU A 172 -0.535 29.058 4.913 1.00 12.95 C ANISOU 1357 CA GLU A 172 1768 1479 1671 54 -128 16 C ATOM 1358 C GLU A 172 -0.605 28.699 6.371 1.00 13.08 C ANISOU 1358 C GLU A 172 1757 1517 1694 11 -142 -95 C ATOM 1359 O GLU A 172 -0.310 29.541 7.232 1.00 15.42 O ANISOU 1359 O GLU A 172 2059 1806 1993 -17 -176 -277 O ATOM 1360 CB GLU A 172 -1.932 29.733 4.666 1.00 14.42 C ANISOU 1360 CB GLU A 172 1965 1610 1900 76 -77 -39 C ATOM 1361 CG GLU A 172 -2.444 29.963 3.284 1.00 17.09 C ANISOU 1361 CG GLU A 172 2237 2129 2127 3 -64 -105 C ATOM 1362 CD GLU A 172 -2.930 28.715 2.576 1.00 14.60 C ANISOU 1362 CD GLU A 172 2014 1687 1844 -53 -41 5 C ATOM 1363 OE1 GLU A 172 -2.091 28.167 1.887 1.00 13.24 O ANISOU 1363 OE1 GLU A 172 1620 2222 1187 7 -41 482 O ATOM 1364 OE2 GLU A 172 -4.130 28.311 2.637 1.00 15.00 O ANISOU 1364 OE2 GLU A 172 1798 2349 1551 63 48 -219 O ATOM 1365 N GLU A 173 -1.088 27.492 6.651 1.00 11.93 N ANISOU 1365 N GLU A 173 1538 1360 1633 71 -132 7 N ATOM 1366 CA GLU A 173 -1.280 27.036 8.032 1.00 11.81 C ANISOU 1366 CA GLU A 173 1537 1433 1514 52 -77 0 C ATOM 1367 C GLU A 173 -0.276 25.956 8.437 1.00 10.51 C ANISOU 1367 C GLU A 173 1387 1265 1341 77 -144 80 C ATOM 1368 O GLU A 173 -0.451 25.276 9.456 1.00 11.95 O ANISOU 1368 O GLU A 173 1614 1427 1498 140 -177 -78 O ATOM 1369 CB GLU A 173 -2.684 26.468 8.216 1.00 13.03 C ANISOU 1369 CB GLU A 173 1609 1720 1621 68 -59 56 C ATOM 1370 CG GLU A 173 -3.802 27.483 8.001 1.00 15.26 C ANISOU 1370 CG GLU A 173 1908 2034 1855 105 -91 172 C ATOM 1371 CD GLU A 173 -5.177 26.842 8.100 1.00 18.49 C ANISOU 1371 CD GLU A 173 2288 2599 2137 117 104 314 C ATOM 1372 OE1 GLU A 173 -6.026 27.063 7.211 1.00 22.96 O ANISOU 1372 OE1 GLU A 173 2804 3120 2797 163 182 250 O ATOM 1373 OE2 GLU A 173 -5.413 26.093 9.074 1.00 23.56 O ANISOU 1373 OE2 GLU A 173 3048 3207 2696 -4 36 647 O ATOM 1374 N ALA A 174 0.758 25.781 7.635 1.00 9.18 N ANISOU 1374 N ALA A 174 1252 1099 1137 160 -241 71 N ATOM 1375 CA ALA A 174 1.762 24.760 7.911 1.00 8.60 C ANISOU 1375 CA ALA A 174 1155 943 1170 102 -158 -2 C ATOM 1376 C ALA A 174 2.415 25.038 9.267 1.00 8.72 C ANISOU 1376 C ALA A 174 1188 988 1136 27 -204 -34 C ATOM 1377 O ALA A 174 2.701 26.175 9.637 1.00 10.60 O ANISOU 1377 O ALA A 174 1451 1108 1466 -106 -397 -20 O ATOM 1378 CB ALA A 174 2.802 24.697 6.821 1.00 9.08 C ANISOU 1378 CB ALA A 174 1269 1028 1152 85 -221 12 C ATOM 1379 N GLU A 175 2.663 23.972 10.001 1.00 7.75 N ANISOU 1379 N GLU A 175 1053 919 972 57 -250 -4 N ATOM 1380 CA GLU A 175 3.374 24.037 11.265 1.00 7.41 C ANISOU 1380 CA GLU A 175 993 956 865 42 -123 -94 C ATOM 1381 C GLU A 175 4.752 23.425 11.054 1.00 7.63 C ANISOU 1381 C GLU A 175 933 1066 901 1 -51 -63 C ATOM 1382 O GLU A 175 4.881 22.238 10.840 1.00 7.43 O ANISOU 1382 O GLU A 175 832 1059 932 61 -112 -101 O ATOM 1383 CB GLU A 175 2.615 23.294 12.347 1.00 8.82 C ANISOU 1383 CB GLU A 175 1032 1249 1068 65 -61 -48 C ATOM 1384 CG GLU A 175 3.307 23.390 13.692 1.00 11.88 C ANISOU 1384 CG GLU A 175 1486 1704 1321 -102 -94 55 C ATOM 1385 CD GLU A 175 2.580 22.686 14.804 1.00 16.19 C ANISOU 1385 CD GLU A 175 1915 2452 1784 -260 -113 31 C ATOM 1386 OE1 GLU A 175 1.442 22.235 14.585 1.00 18.78 O ANISOU 1386 OE1 GLU A 175 2176 2894 2063 -370 224 9 O ATOM 1387 OE2 GLU A 175 3.161 22.603 15.893 1.00 20.13 O ANISOU 1387 OE2 GLU A 175 2597 3281 1771 -309 -250 442 O ATOM 1388 N VAL A 176 5.758 24.289 11.057 1.00 7.48 N ANISOU 1388 N VAL A 176 986 965 890 -31 -120 -112 N ATOM 1389 CA VAL A 176 7.077 23.963 10.582 1.00 8.06 C ANISOU 1389 CA VAL A 176 1027 1024 1009 -77 -73 -40 C ATOM 1390 C VAL A 176 8.127 24.311 11.618 1.00 8.51 C ANISOU 1390 C VAL A 176 1039 1138 1055 -34 -72 -118 C ATOM 1391 O VAL A 176 8.043 25.358 12.263 1.00 9.69 O ANISOU 1391 O VAL A 176 1088 1347 1246 -55 -80 -271 O ATOM 1392 CB VAL A 176 7.353 24.801 9.306 1.00 9.32 C ANISOU 1392 CB VAL A 176 1148 1313 1078 -220 -110 31 C ATOM 1393 CG1 VAL A 176 8.662 24.490 8.705 1.00 9.56 C ANISOU 1393 CG1 VAL A 176 1192 1179 1261 -245 -91 2 C ATOM 1394 CG2 VAL A 176 6.223 24.628 8.278 1.00 10.09 C ANISOU 1394 CG2 VAL A 176 1302 1435 1096 -247 -87 152 C ATOM 1395 N SER A 177 9.137 23.466 11.773 1.00 8.13 N ANISOU 1395 N SER A 177 1090 1073 924 -57 -38 -126 N ATOM 1396 CA SER A 177 10.234 23.749 12.712 1.00 8.45 C ANISOU 1396 CA SER A 177 1098 1173 940 -42 -23 -114 C ATOM 1397 C SER A 177 11.077 24.932 12.237 1.00 8.48 C ANISOU 1397 C SER A 177 1077 1202 941 -79 -87 -104 C ATOM 1398 O SER A 177 11.117 25.265 11.054 1.00 8.60 O ANISOU 1398 O SER A 177 980 1280 1005 -113 -170 -137 O ATOM 1399 CB SER A 177 11.117 22.527 12.863 1.00 9.54 C ANISOU 1399 CB SER A 177 1178 1364 1082 -118 -39 -45 C ATOM 1400 OG SER A 177 11.868 22.341 11.687 1.00 9.13 O ANISOU 1400 OG SER A 177 1076 1497 895 -74 -46 -84 O ATOM 1401 N GLU A 178 11.787 25.576 13.170 1.00 9.16 N ANISOU 1401 N GLU A 178 1205 1281 992 -83 -77 -175 N ATOM 1402 CA GLU A 178 12.705 26.642 12.789 1.00 9.72 C ANISOU 1402 CA GLU A 178 1276 1296 1121 -68 -87 -163 C ATOM 1403 C GLU A 178 13.784 26.157 11.818 1.00 9.00 C ANISOU 1403 C GLU A 178 1151 1280 986 -146 -155 -136 C ATOM 1404 O GLU A 178 14.150 26.854 10.874 1.00 9.78 O ANISOU 1404 O GLU A 178 1228 1394 1093 -137 -149 -114 O ATOM 1405 CB GLU A 178 13.362 27.254 14.044 1.00 10.05 C ANISOU 1405 CB GLU A 178 1338 1427 1051 -126 -37 -171 C ATOM 1406 CG GLU A 178 12.380 27.828 15.048 1.00 13.51 C ANISOU 1406 CG GLU A 178 1635 1905 1593 -198 112 -273 C ATOM 1407 CD GLU A 178 11.583 29.001 14.523 1.00 17.59 C ANISOU 1407 CD GLU A 178 2076 2570 2036 11 300 -232 C ATOM 1408 OE1 GLU A 178 11.994 29.654 13.539 1.00 19.79 O ANISOU 1408 OE1 GLU A 178 2498 2545 2476 -50 246 -329 O ATOM 1409 OE2 GLU A 178 10.528 29.297 15.128 1.00 24.42 O ANISOU 1409 OE2 GLU A 178 2763 3476 3037 192 399 -112 O ATOM 1410 N ALA A 179 14.288 24.960 12.039 1.00 9.16 N ANISOU 1410 N ALA A 179 1041 1437 1001 -22 -138 -72 N ATOM 1411 CA ALA A 179 15.295 24.414 11.133 1.00 8.93 C ANISOU 1411 CA ALA A 179 1100 1243 1049 27 -67 -56 C ATOM 1412 C ALA A 179 14.717 24.275 9.719 1.00 9.18 C ANISOU 1412 C ALA A 179 1115 1341 1032 -19 -80 -7 C ATOM 1413 O ALA A 179 15.371 24.639 8.733 1.00 9.37 O ANISOU 1413 O ALA A 179 1141 1285 1133 -74 66 40 O ATOM 1414 CB ALA A 179 15.790 23.088 11.635 1.00 10.11 C ANISOU 1414 CB ALA A 179 1219 1412 1209 50 -89 80 C ATOM 1415 N ASP A 180 13.503 23.746 9.599 1.00 8.07 N ANISOU 1415 N ASP A 180 1044 1182 839 -40 -29 -4 N ATOM 1416 CA ASP A 180 12.924 23.531 8.273 1.00 7.49 C ANISOU 1416 CA ASP A 180 1063 1004 778 -37 18 -132 C ATOM 1417 C ASP A 180 12.592 24.853 7.583 1.00 8.17 C ANISOU 1417 C ASP A 180 1156 1157 789 -119 1 -78 C ATOM 1418 O ASP A 180 12.608 24.937 6.366 1.00 8.86 O ANISOU 1418 O ASP A 180 1411 1074 880 -140 -55 -131 O ATOM 1419 CB ASP A 180 11.708 22.608 8.360 1.00 7.29 C ANISOU 1419 CB ASP A 180 980 1028 761 -36 -64 11 C ATOM 1420 CG ASP A 180 12.085 21.161 8.547 1.00 7.76 C ANISOU 1420 CG ASP A 180 950 1155 843 87 -20 -24 C ATOM 1421 OD1 ASP A 180 13.279 20.829 8.446 1.00 10.06 O ANISOU 1421 OD1 ASP A 180 1226 1285 1310 114 83 -119 O ATOM 1422 OD2 ASP A 180 11.207 20.311 8.824 1.00 8.15 O ANISOU 1422 OD2 ASP A 180 916 1180 999 -2 20 -80 O ATOM 1423 N GLU A 181 12.311 25.899 8.346 1.00 8.41 N ANISOU 1423 N GLU A 181 1188 1101 903 11 -14 -57 N ATOM 1424 CA GLU A 181 12.080 27.198 7.718 1.00 9.28 C ANISOU 1424 CA GLU A 181 1300 1177 1049 21 -49 -44 C ATOM 1425 C GLU A 181 13.320 27.727 7.017 1.00 9.02 C ANISOU 1425 C GLU A 181 1351 1098 977 25 -45 -103 C ATOM 1426 O GLU A 181 13.214 28.561 6.120 1.00 9.94 O ANISOU 1426 O GLU A 181 1649 1208 918 96 -11 -142 O ATOM 1427 CB GLU A 181 11.641 28.230 8.754 1.00 10.24 C ANISOU 1427 CB GLU A 181 1420 1272 1199 69 -28 -104 C ATOM 1428 CG GLU A 181 10.282 27.976 9.366 1.00 13.61 C ANISOU 1428 CG GLU A 181 1757 1789 1625 55 -79 2 C ATOM 1429 CD GLU A 181 9.095 28.285 8.461 1.00 15.98 C ANISOU 1429 CD GLU A 181 1855 2132 2081 298 -24 -10 C ATOM 1430 OE1 GLU A 181 9.266 28.387 7.229 1.00 15.57 O ANISOU 1430 OE1 GLU A 181 1795 2173 1945 610 -42 -113 O ATOM 1431 OE2 GLU A 181 7.969 28.409 9.005 1.00 19.77 O ANISOU 1431 OE2 GLU A 181 2193 2582 2736 121 80 146 O ATOM 1432 N ASN A 182 14.496 27.272 7.452 1.00 9.25 N ANISOU 1432 N ASN A 182 1346 1186 981 -41 -57 -98 N ATOM 1433 CA ASN A 182 15.760 27.872 7.059 1.00 9.35 C ANISOU 1433 CA ASN A 182 1325 1190 1036 -117 -39 -66 C ATOM 1434 C ASN A 182 16.699 27.015 6.205 1.00 9.09 C ANISOU 1434 C ASN A 182 1249 1257 945 -112 -105 -48 C ATOM 1435 O ASN A 182 17.799 27.435 5.889 1.00 11.01 O ANISOU 1435 O ASN A 182 1494 1553 1137 -357 -29 -112 O ATOM 1436 CB ASN A 182 16.469 28.390 8.301 1.00 11.12 C ANISOU 1436 CB ASN A 182 1427 1524 1273 -151 -44 -9 C ATOM 1437 CG ASN A 182 15.763 29.577 8.890 1.00 13.18 C ANISOU 1437 CG ASN A 182 1880 1564 1563 -303 -9 -47 C ATOM 1438 OD1 ASN A 182 15.825 30.685 8.336 1.00 17.15 O ANISOU 1438 OD1 ASN A 182 2595 1793 2126 -90 -82 -219 O ATOM 1439 ND2 ASN A 182 15.070 29.362 10.006 1.00 16.10 N ANISOU 1439 ND2 ASN A 182 2238 2012 1864 -369 -3 -205 N ATOM 1440 N HIS A 183 16.243 25.858 5.741 1.00 8.51 N ANISOU 1440 N HIS A 183 1253 1100 878 -136 -146 42 N ATOM 1441 CA HIS A 183 17.050 25.073 4.827 1.00 8.05 C ANISOU 1441 CA HIS A 183 1120 1056 883 -8 -92 84 C ATOM 1442 C HIS A 183 17.253 25.837 3.525 1.00 7.87 C ANISOU 1442 C HIS A 183 1101 1065 824 -17 -166 -10 C ATOM 1443 O HIS A 183 16.435 26.682 3.166 1.00 7.47 O ANISOU 1443 O HIS A 183 1079 983 775 60 -157 -88 O ATOM 1444 CB HIS A 183 16.417 23.704 4.579 1.00 7.42 C ANISOU 1444 CB HIS A 183 1040 1003 776 -17 -63 128 C ATOM 1445 CG HIS A 183 16.472 22.799 5.768 1.00 7.99 C ANISOU 1445 CG HIS A 183 1131 1125 777 112 -11 23 C ATOM 1446 ND1 HIS A 183 17.597 22.677 6.552 1.00 8.03 N ANISOU 1446 ND1 HIS A 183 1058 1301 691 162 97 187 N ATOM 1447 CD2 HIS A 183 15.528 22.016 6.342 1.00 9.78 C ANISOU 1447 CD2 HIS A 183 1298 1275 1141 272 0 57 C ATOM 1448 CE1 HIS A 183 17.351 21.828 7.539 1.00 9.63 C ANISOU 1448 CE1 HIS A 183 1335 1194 1130 100 0 270 C ATOM 1449 NE2 HIS A 183 16.106 21.403 7.423 1.00 10.09 N ANISOU 1449 NE2 HIS A 183 1448 1223 1162 289 -19 196 N ATOM 1450 N PRO A 184 18.335 25.554 2.815 1.00 7.39 N ANISOU 1450 N PRO A 184 1021 995 791 -39 -102 97 N ATOM 1451 CA PRO A 184 18.621 26.279 1.571 1.00 7.49 C ANISOU 1451 CA PRO A 184 1035 998 811 -35 -80 83 C ATOM 1452 C PRO A 184 17.598 25.963 0.482 1.00 6.80 C ANISOU 1452 C PRO A 184 855 839 890 -91 -111 -18 C ATOM 1453 O PRO A 184 17.049 24.879 0.418 1.00 6.58 O ANISOU 1453 O PRO A 184 873 866 761 -110 -70 101 O ATOM 1454 CB PRO A 184 20.000 25.769 1.171 1.00 8.13 C ANISOU 1454 CB PRO A 184 1051 1138 897 -74 -56 25 C ATOM 1455 CG PRO A 184 20.129 24.434 1.865 1.00 9.77 C ANISOU 1455 CG PRO A 184 1215 1329 1167 69 -53 148 C ATOM 1456 CD PRO A 184 19.387 24.581 3.146 1.00 8.55 C ANISOU 1456 CD PRO A 184 1049 1147 1050 24 -76 57 C ATOM 1457 N PHE A 185 17.395 26.926 -0.406 1.00 6.77 N ANISOU 1457 N PHE A 185 847 851 871 -17 -112 -30 N ATOM 1458 CA PHE A 185 16.666 26.681 -1.631 1.00 6.33 C ANISOU 1458 CA PHE A 185 805 832 765 -56 -54 -32 C ATOM 1459 C PHE A 185 17.477 25.757 -2.522 1.00 5.97 C ANISOU 1459 C PHE A 185 765 659 842 -16 -74 71 C ATOM 1460 O PHE A 185 18.674 25.624 -2.335 1.00 6.36 O ANISOU 1460 O PHE A 185 700 982 734 22 -44 12 O ATOM 1461 CB PHE A 185 16.407 28.020 -2.335 1.00 7.05 C ANISOU 1461 CB PHE A 185 907 882 887 13 -133 -46 C ATOM 1462 CG PHE A 185 15.191 28.777 -1.841 1.00 8.13 C ANISOU 1462 CG PHE A 185 1165 1031 893 -77 -137 -44 C ATOM 1463 CD1 PHE A 185 14.704 28.626 -0.547 1.00 8.23 C ANISOU 1463 CD1 PHE A 185 1088 962 1077 216 57 -14 C ATOM 1464 CD2 PHE A 185 14.533 29.637 -2.696 1.00 9.49 C ANISOU 1464 CD2 PHE A 185 1297 1175 1133 252 -127 -105 C ATOM 1465 CE1 PHE A 185 13.598 29.337 -0.116 1.00 9.94 C ANISOU 1465 CE1 PHE A 185 1470 1298 1009 102 155 -194 C ATOM 1466 CE2 PHE A 185 13.436 30.365 -2.260 1.00 10.79 C ANISOU 1466 CE2 PHE A 185 1459 1301 1336 104 -79 -73 C ATOM 1467 CZ PHE A 185 12.966 30.177 -0.977 1.00 9.75 C ANISOU 1467 CZ PHE A 185 1296 1064 1344 221 150 -166 C ATOM 1468 N LEU A 186 16.834 25.146 -3.516 1.00 5.89 N ANISOU 1468 N LEU A 186 704 710 823 -2 -16 11 N ATOM 1469 CA LEU A 186 17.494 24.146 -4.355 1.00 6.28 C ANISOU 1469 CA LEU A 186 834 723 829 19 -9 52 C ATOM 1470 C LEU A 186 18.764 24.687 -5.003 1.00 6.43 C ANISOU 1470 C LEU A 186 846 750 846 2 -7 -85 C ATOM 1471 O LEU A 186 19.770 23.966 -5.106 1.00 7.24 O ANISOU 1471 O LEU A 186 815 878 1055 20 51 -44 O ATOM 1472 CB LEU A 186 16.532 23.597 -5.407 1.00 6.53 C ANISOU 1472 CB LEU A 186 899 779 802 -106 80 58 C ATOM 1473 CG LEU A 186 17.048 22.388 -6.200 1.00 7.75 C ANISOU 1473 CG LEU A 186 1080 958 905 -58 68 -33 C ATOM 1474 CD1 LEU A 186 17.107 21.139 -5.351 1.00 8.64 C ANISOU 1474 CD1 LEU A 186 1116 882 1284 -128 133 -27 C ATOM 1475 CD2 LEU A 186 16.192 22.168 -7.437 1.00 8.88 C ANISOU 1475 CD2 LEU A 186 1301 1119 951 -118 -122 -114 C ATOM 1476 N LYS A 187 18.739 25.950 -5.421 1.00 6.42 N ANISOU 1476 N LYS A 187 740 738 960 -56 86 -20 N ATOM 1477 CA LYS A 187 19.891 26.567 -6.099 1.00 7.42 C ANISOU 1477 CA LYS A 187 880 951 985 -88 80 50 C ATOM 1478 C LYS A 187 21.143 26.582 -5.243 1.00 7.78 C ANISOU 1478 C LYS A 187 883 969 1101 -5 29 -14 C ATOM 1479 O LYS A 187 22.250 26.753 -5.760 1.00 9.27 O ANISOU 1479 O LYS A 187 841 1309 1369 -163 178 -82 O ATOM 1480 CB LYS A 187 19.568 28.002 -6.534 1.00 7.94 C ANISOU 1480 CB LYS A 187 991 1062 963 -13 71 42 C ATOM 1481 CG LYS A 187 19.361 28.977 -5.392 1.00 8.98 C ANISOU 1481 CG LYS A 187 1294 938 1177 -117 45 78 C ATOM 1482 CD LYS A 187 19.123 30.406 -5.879 1.00 10.46 C ANISOU 1482 CD LYS A 187 1319 1281 1373 -186 18 101 C ATOM 1483 CE LYS A 187 18.806 31.367 -4.723 1.00 11.07 C ANISOU 1483 CE LYS A 187 1355 1268 1582 -132 53 138 C ATOM 1484 NZ LYS A 187 20.012 31.698 -3.896 1.00 11.76 N ANISOU 1484 NZ LYS A 187 1341 1517 1607 -217 -99 -23 N ATOM 1485 N ASP A 188 20.967 26.475 -3.934 1.00 7.43 N ANISOU 1485 N ASP A 188 736 951 1135 -65 30 17 N ATOM 1486 CA ASP A 188 22.075 26.493 -2.959 1.00 9.11 C ANISOU 1486 CA ASP A 188 1081 1156 1221 -11 -82 -65 C ATOM 1487 C ASP A 188 22.383 25.135 -2.336 1.00 9.36 C ANISOU 1487 C ASP A 188 1136 1114 1304 46 -177 -88 C ATOM 1488 O ASP A 188 23.186 25.053 -1.408 1.00 11.23 O ANISOU 1488 O ASP A 188 1494 1192 1579 -49 -462 -73 O ATOM 1489 CB ASP A 188 21.758 27.510 -1.865 1.00 9.40 C ANISOU 1489 CB ASP A 188 1125 1169 1277 -40 -47 -52 C ATOM 1490 CG ASP A 188 21.653 28.900 -2.409 1.00 10.27 C ANISOU 1490 CG ASP A 188 1270 1273 1358 -37 168 -73 C ATOM 1491 OD1 ASP A 188 22.617 29.306 -3.095 1.00 12.19 O ANISOU 1491 OD1 ASP A 188 1606 1212 1812 -170 497 -81 O ATOM 1492 OD2 ASP A 188 20.666 29.641 -2.215 1.00 10.54 O ANISOU 1492 OD2 ASP A 188 1497 1036 1471 -141 108 28 O ATOM 1493 N VAL A 189 21.755 24.082 -2.833 1.00 8.22 N ANISOU 1493 N VAL A 189 1008 1024 1089 32 -105 -18 N ATOM 1494 CA VAL A 189 22.062 22.729 -2.422 1.00 8.49 C ANISOU 1494 CA VAL A 189 1044 1019 1163 84 -60 -46 C ATOM 1495 C VAL A 189 23.241 22.215 -3.227 1.00 9.09 C ANISOU 1495 C VAL A 189 1207 1048 1196 47 -33 -104 C ATOM 1496 O VAL A 189 23.291 22.366 -4.425 1.00 9.99 O ANISOU 1496 O VAL A 189 1306 1249 1240 382 20 -1 O ATOM 1497 CB VAL A 189 20.847 21.795 -2.654 1.00 7.95 C ANISOU 1497 CB VAL A 189 913 927 1181 32 -29 -106 C ATOM 1498 CG1 VAL A 189 21.219 20.327 -2.367 1.00 9.80 C ANISOU 1498 CG1 VAL A 189 1120 1169 1433 -44 2 -113 C ATOM 1499 CG2 VAL A 189 19.675 22.234 -1.780 1.00 10.12 C ANISOU 1499 CG2 VAL A 189 1209 1280 1355 144 33 -6 C ATOM 1500 N LYS A 190 24.207 21.623 -2.555 1.00 9.49 N ANISOU 1500 N LYS A 190 1148 1070 1385 13 -20 -60 N ATOM 1501 CA LYS A 190 25.302 20.939 -3.231 1.00 10.56 C ANISOU 1501 CA LYS A 190 1318 1196 1496 -24 -12 -39 C ATOM 1502 C LYS A 190 24.818 19.505 -3.551 1.00 8.56 C ANISOU 1502 C LYS A 190 963 906 1384 -26 63 4 C ATOM 1503 O LYS A 190 24.505 18.754 -2.623 1.00 9.14 O ANISOU 1503 O LYS A 190 1206 946 1319 89 96 -15 O ATOM 1504 CB LYS A 190 26.505 20.873 -2.298 1.00 12.47 C ANISOU 1504 CB LYS A 190 1594 1385 1758 5 -78 -15 C ATOM 1505 CG LYS A 190 27.712 20.196 -2.899 1.00 17.56 C ANISOU 1505 CG LYS A 190 2295 2184 2192 14 -43 -75 C ATOM 1506 CD LYS A 190 28.628 21.166 -3.600 1.00 22.00 C ANISOU 1506 CD LYS A 190 2790 2857 2709 57 4 -40 C ATOM 1507 CE LYS A 190 29.540 20.478 -4.633 1.00 24.23 C ANISOU 1507 CE LYS A 190 3095 3162 2947 52 7 0 C ATOM 1508 NZ LYS A 190 29.225 20.902 -6.049 1.00 25.76 N ANISOU 1508 NZ LYS A 190 3331 3400 3055 100 -100 93 N ATOM 1509 N PRO A 191 24.681 19.137 -4.821 1.00 8.07 N ANISOU 1509 N PRO A 191 962 863 1237 -27 117 103 N ATOM 1510 CA PRO A 191 24.192 17.791 -5.148 1.00 8.18 C ANISOU 1510 CA PRO A 191 932 968 1206 -4 23 41 C ATOM 1511 C PRO A 191 25.070 16.703 -4.534 1.00 8.26 C ANISOU 1511 C PRO A 191 934 956 1249 99 48 43 C ATOM 1512 O PRO A 191 26.289 16.832 -4.450 1.00 9.22 O ANISOU 1512 O PRO A 191 1010 1012 1480 48 -31 66 O ATOM 1513 CB PRO A 191 24.249 17.761 -6.682 1.00 9.04 C ANISOU 1513 CB PRO A 191 1025 1060 1347 23 48 -49 C ATOM 1514 CG PRO A 191 24.137 19.194 -7.093 1.00 9.76 C ANISOU 1514 CG PRO A 191 1239 1234 1235 56 72 161 C ATOM 1515 CD PRO A 191 24.875 19.957 -6.038 1.00 8.71 C ANISOU 1515 CD PRO A 191 1031 1027 1251 14 176 75 C ATOM 1516 N LEU A 192 24.430 15.641 -4.062 1.00 7.65 N ANISOU 1516 N LEU A 192 833 915 1158 108 -21 19 N ATOM 1517 CA LEU A 192 25.123 14.547 -3.388 1.00 8.02 C ANISOU 1517 CA LEU A 192 995 976 1075 99 -7 -47 C ATOM 1518 C LEU A 192 25.799 13.682 -4.430 1.00 8.58 C ANISOU 1518 C LEU A 192 1058 1104 1095 121 -38 -83 C ATOM 1519 O LEU A 192 25.162 13.127 -5.318 1.00 8.99 O ANISOU 1519 O LEU A 192 1114 1101 1199 303 -105 -93 O ATOM 1520 CB LEU A 192 24.141 13.733 -2.549 1.00 7.88 C ANISOU 1520 CB LEU A 192 940 872 1182 123 44 -75 C ATOM 1521 CG LEU A 192 23.599 14.472 -1.341 1.00 8.45 C ANISOU 1521 CG LEU A 192 1048 1018 1145 -35 131 -175 C ATOM 1522 CD1 LEU A 192 22.393 13.749 -0.811 1.00 9.97 C ANISOU 1522 CD1 LEU A 192 1120 1126 1539 -32 283 11 C ATOM 1523 CD2 LEU A 192 24.650 14.565 -0.266 1.00 11.22 C ANISOU 1523 CD2 LEU A 192 1376 1546 1339 -49 241 -63 C ATOM 1524 N ARG A 193 27.115 13.576 -4.305 1.00 10.47 N ANISOU 1524 N ARG A 193 1278 1452 1246 106 -36 -121 N ATOM 1525 CA ARG A 193 27.943 12.847 -5.253 1.00 12.53 C ANISOU 1525 CA ARG A 193 1545 1683 1530 56 49 -67 C ATOM 1526 C ARG A 193 27.979 11.391 -4.860 1.00 13.78 C ANISOU 1526 C ARG A 193 1716 1833 1686 131 90 -76 C ATOM 1527 O ARG A 193 27.572 11.021 -3.754 1.00 13.54 O ANISOU 1527 O ARG A 193 1764 1799 1581 165 209 -91 O ATOM 1528 CB ARG A 193 29.347 13.442 -5.258 1.00 13.16 C ANISOU 1528 CB ARG A 193 1629 1771 1599 117 55 -108 C ATOM 1529 CG ARG A 193 29.342 14.910 -5.608 1.00 16.61 C ANISOU 1529 CG ARG A 193 1958 2192 2158 -109 50 -32 C ATOM 1530 CD ARG A 193 30.459 15.325 -6.521 1.00 22.07 C ANISOU 1530 CD ARG A 193 2715 2827 2844 -1 -49 -35 C ATOM 1531 NE ARG A 193 31.688 15.588 -5.786 1.00 26.12 N ANISOU 1531 NE ARG A 193 3245 3416 3263 -1 -133 -54 N ATOM 1532 CZ ARG A 193 32.892 15.652 -6.344 1.00 28.11 C ANISOU 1532 CZ ARG A 193 3465 3706 3509 -19 -51 -53 C ATOM 1533 NH1 ARG A 193 33.049 15.461 -7.651 1.00 29.23 N ANISOU 1533 NH1 ARG A 193 3654 3830 3620 5 -15 9 N ATOM 1534 NH2 ARG A 193 33.954 15.908 -5.589 1.00 30.14 N ANISOU 1534 NH2 ARG A 193 3759 3961 3731 56 -118 -5 N ATOM 1535 N LYS A 194 28.469 10.545 -5.760 1.00 16.11 N ANISOU 1535 N LYS A 194 2110 2038 1973 104 83 -68 N ATOM 1536 CA LYS A 194 28.537 9.109 -5.485 1.00 18.43 C ANISOU 1536 CA LYS A 194 2393 2328 2278 67 57 -34 C ATOM 1537 C LYS A 194 29.327 8.853 -4.207 1.00 18.73 C ANISOU 1537 C LYS A 194 2375 2365 2375 91 41 -7 C ATOM 1538 O LYS A 194 28.948 7.994 -3.418 1.00 19.01 O ANISOU 1538 O LYS A 194 2467 2294 2459 247 158 -22 O ATOM 1539 CB LYS A 194 29.136 8.333 -6.665 1.00 19.14 C ANISOU 1539 CB LYS A 194 2485 2423 2362 86 21 -36 C ATOM 1540 CG LYS A 194 28.286 8.406 -7.934 1.00 22.10 C ANISOU 1540 CG LYS A 194 2858 2785 2754 39 -31 -23 C ATOM 1541 CD LYS A 194 27.060 7.510 -7.907 1.00 24.53 C ANISOU 1541 CD LYS A 194 3107 3148 3065 4 -45 -9 C ATOM 1542 CE LYS A 194 26.308 7.612 -9.244 1.00 25.76 C ANISOU 1542 CE LYS A 194 3290 3298 3198 -27 -68 -26 C ATOM 1543 NZ LYS A 194 25.195 6.635 -9.335 1.00 27.16 N ANISOU 1543 NZ LYS A 194 3430 3493 3396 0 -158 -44 N ATOM 1544 N GLU A 195 30.365 9.654 -3.967 1.00 19.76 N ANISOU 1544 N GLU A 195 2477 2540 2489 77 44 22 N ATOM 1545 CA GLU A 195 31.172 9.552 -2.743 1.00 20.62 C ANISOU 1545 CA GLU A 195 2573 2690 2571 59 3 27 C ATOM 1546 C GLU A 195 30.414 9.939 -1.463 1.00 20.96 C ANISOU 1546 C GLU A 195 2625 2742 2597 115 -8 28 C ATOM 1547 O GLU A 195 30.829 9.591 -0.360 1.00 21.05 O ANISOU 1547 O GLU A 195 2547 2929 2519 190 -38 87 O ATOM 1548 CB GLU A 195 32.457 10.391 -2.874 1.00 21.28 C ANISOU 1548 CB GLU A 195 2706 2730 2647 52 -31 41 C ATOM 1549 CG GLU A 195 32.237 11.900 -2.872 1.00 22.75 C ANISOU 1549 CG GLU A 195 2899 2955 2787 26 -16 -61 C ATOM 1550 CD GLU A 195 33.330 12.676 -3.581 1.00 25.41 C ANISOU 1550 CD GLU A 195 3370 3346 2938 10 -122 -128 C ATOM 1551 OE1 GLU A 195 33.257 12.840 -4.825 1.00 27.80 O ANISOU 1551 OE1 GLU A 195 3940 3614 3007 43 -205 -217 O ATOM 1552 OE2 GLU A 195 34.261 13.143 -2.891 1.00 27.09 O ANISOU 1552 OE2 GLU A 195 3582 3632 3078 -80 -185 -272 O ATOM 1553 N ASP A 196 29.314 10.674 -1.613 1.00 20.61 N ANISOU 1553 N ASP A 196 2495 2754 2581 55 -5 20 N ATOM 1554 CA ASP A 196 28.498 11.114 -0.482 1.00 20.85 C ANISOU 1554 CA ASP A 196 2607 2735 2577 10 -9 -24 C ATOM 1555 C ASP A 196 27.355 10.145 -0.143 1.00 20.48 C ANISOU 1555 C ASP A 196 2541 2704 2536 34 12 -11 C ATOM 1556 O ASP A 196 26.607 10.394 0.812 1.00 19.20 O ANISOU 1556 O ASP A 196 2316 2696 2281 43 55 -67 O ATOM 1557 CB ASP A 196 27.863 12.478 -0.782 1.00 21.14 C ANISOU 1557 CB ASP A 196 2661 2763 2607 7 -31 -17 C ATOM 1558 CG ASP A 196 28.876 13.575 -1.084 1.00 21.32 C ANISOU 1558 CG ASP A 196 2572 2917 2609 -19 -125 -127 C ATOM 1559 OD1 ASP A 196 29.957 13.616 -0.441 1.00 22.64 O ANISOU 1559 OD1 ASP A 196 2486 3297 2818 -132 -392 10 O ATOM 1560 OD2 ASP A 196 28.645 14.470 -1.937 1.00 18.76 O ANISOU 1560 OD2 ASP A 196 2276 2881 1970 -217 -322 -349 O ATOM 1561 N LEU A 197 27.199 9.077 -0.927 1.00 20.22 N ANISOU 1561 N LEU A 197 2495 2633 2553 20 30 2 N ATOM 1562 CA LEU A 197 26.064 8.157 -0.799 1.00 20.40 C ANISOU 1562 CA LEU A 197 2537 2635 2576 22 28 -11 C ATOM 1563 C LEU A 197 26.483 6.799 -0.244 1.00 20.85 C ANISOU 1563 C LEU A 197 2535 2761 2623 155 39 -3 C ATOM 1564 O LEU A 197 27.669 6.558 0.020 1.00 22.35 O ANISOU 1564 O LEU A 197 2692 3007 2791 44 37 59 O ATOM 1565 CB LEU A 197 25.387 7.971 -2.161 1.00 20.55 C ANISOU 1565 CB LEU A 197 2533 2656 2617 34 42 -17 C ATOM 1566 CG LEU A 197 24.838 9.241 -2.818 1.00 19.50 C ANISOU 1566 CG LEU A 197 2411 2583 2414 -7 29 -8 C ATOM 1567 CD1 LEU A 197 24.512 8.983 -4.298 1.00 21.28 C ANISOU 1567 CD1 LEU A 197 2590 2867 2626 -16 23 14 C ATOM 1568 CD2 LEU A 197 23.589 9.771 -2.073 1.00 16.01 C ANISOU 1568 CD2 LEU A 197 1976 1972 2136 0 15 -59 C TER 1569 LEU A 197 ATOM 1930 N ASN A 4 5.945 7.851 33.999 1.00 6.83 N ANISOU 1930 N ASN B 4 1335 588 670 581 -98 45 N ATOM 1931 CA ASN A 4 5.796 8.878 32.921 1.00 5.14 C ANISOU 1931 CA ASN B 4 823 498 630 257 45 104 C ATOM 1932 C ASN A 4 5.768 8.258 31.529 1.00 5.16 C ANISOU 1932 C ASN B 4 809 469 681 207 54 -5 C ATOM 1933 O ASN A 4 6.420 7.237 31.258 1.00 6.38 O ANISOU 1933 O ASN B 4 998 472 955 285 110 0 O ATOM 1934 CB ASN A 4 6.976 9.846 32.943 1.00 5.12 C ANISOU 1934 CB ASN B 4 755 483 707 258 21 79 C ATOM 1935 CG ASN A 4 6.946 10.827 34.095 1.00 5.59 C ANISOU 1935 CG ASN B 4 891 353 880 234 58 114 C ATOM 1936 OD1 ASN A 4 5.935 11.017 34.793 1.00 6.26 O ANISOU 1936 OD1 ASN B 4 929 556 893 332 138 360 O ATOM 1937 ND2 ASN A 4 8.080 11.487 34.285 1.00 7.64 N ANISOU 1937 ND2 ASN B 4 834 693 1374 268 -9 -200 N ATOM 1938 N PHE A 5 5.040 8.902 30.628 1.00 3.92 N ANISOU 1938 N PHE B 5 578 276 632 72 -44 -63 N ATOM 1939 CA PHE A 5 5.011 8.517 29.217 1.00 4.28 C ANISOU 1939 CA PHE B 5 518 479 628 29 101 -46 C ATOM 1940 C PHE A 5 6.208 9.098 28.473 1.00 3.72 C ANISOU 1940 C PHE B 5 479 428 505 -29 126 -15 C ATOM 1941 O PHE A 5 6.829 8.417 27.677 1.00 5.10 O ANISOU 1941 O PHE B 5 466 626 845 61 157 -278 O ATOM 1942 CB PHE A 5 3.720 9.045 28.593 1.00 4.87 C ANISOU 1942 CB PHE B 5 641 587 619 17 115 20 C ATOM 1943 CG PHE A 5 3.556 8.706 27.126 1.00 4.73 C ANISOU 1943 CG PHE B 5 575 621 600 39 -22 10 C ATOM 1944 CD1 PHE A 5 2.992 7.505 26.737 1.00 7.79 C ANISOU 1944 CD1 PHE B 5 1261 804 894 63 -20 -20 C ATOM 1945 CD2 PHE A 5 3.861 9.632 26.140 1.00 6.18 C ANISOU 1945 CD2 PHE B 5 859 807 679 -7 120 -4 C ATOM 1946 CE1 PHE A 5 2.787 7.214 25.385 1.00 9.32 C ANISOU 1946 CE1 PHE B 5 1329 915 1294 92 -222 -177 C ATOM 1947 CE2 PHE A 5 3.667 9.344 24.813 1.00 8.23 C ANISOU 1947 CE2 PHE B 5 1055 1240 830 228 149 -83 C ATOM 1948 CZ PHE A 5 3.135 8.133 24.443 1.00 7.81 C ANISOU 1948 CZ PHE B 5 897 1281 789 314 1 -69 C ATOM 1949 N PHE A 6 6.527 10.361 28.743 1.00 3.65 N ANISOU 1949 N PHE B 6 535 407 445 46 172 -74 N ATOM 1950 CA PHE A 6 7.601 11.062 28.036 1.00 3.37 C ANISOU 1950 CA PHE B 6 462 460 358 56 114 -58 C ATOM 1951 C PHE A 6 8.907 11.016 28.798 1.00 3.62 C ANISOU 1951 C PHE B 6 527 464 382 -9 145 -52 C ATOM 1952 O PHE A 6 8.907 11.014 30.037 1.00 5.11 O ANISOU 1952 O PHE B 6 821 820 299 221 88 35 O ATOM 1953 CB PHE A 6 7.223 12.535 27.799 1.00 3.78 C ANISOU 1953 CB PHE B 6 525 513 397 51 196 14 C ATOM 1954 CG PHE A 6 6.003 12.711 26.963 1.00 4.57 C ANISOU 1954 CG PHE B 6 718 647 372 87 235 40 C ATOM 1955 CD1 PHE A 6 4.789 13.017 27.538 1.00 5.74 C ANISOU 1955 CD1 PHE B 6 805 1080 294 337 131 160 C ATOM 1956 CD2 PHE A 6 6.057 12.539 25.587 1.00 6.07 C ANISOU 1956 CD2 PHE B 6 860 1076 368 98 159 268 C ATOM 1957 CE1 PHE A 6 3.650 13.160 26.755 1.00 6.50 C ANISOU 1957 CE1 PHE B 6 652 1276 540 282 81 170 C ATOM 1958 CE2 PHE A 6 4.929 12.678 24.806 1.00 7.47 C ANISOU 1958 CE2 PHE B 6 1010 1310 517 36 41 213 C ATOM 1959 CZ PHE A 6 3.727 12.992 25.380 1.00 7.99 C ANISOU 1959 CZ PHE B 6 970 1337 725 410 68 143 C ATOM 1960 N GLY A 7 10.009 11.006 28.061 1.00 3.67 N ANISOU 1960 N GLY B 7 515 446 434 91 80 31 N ATOM 1961 CA GLY A 7 11.303 11.273 28.628 1.00 5.11 C ANISOU 1961 CA GLY B 7 726 540 673 -13 -28 -2 C ATOM 1962 C GLY A 7 11.924 10.158 29.441 1.00 5.47 C ANISOU 1962 C GLY B 7 743 622 709 13 -67 24 C ATOM 1963 O GLY A 7 12.854 10.418 30.177 1.00 7.13 O ANISOU 1963 O GLY B 7 977 695 1036 33 -249 -52 O ATOM 1964 N LYS A 8 11.440 8.920 29.316 1.00 4.62 N ANISOU 1964 N LYS B 8 687 517 549 23 -25 17 N ATOM 1965 CA LYS A 8 12.052 7.814 30.052 1.00 5.81 C ANISOU 1965 CA LYS B 8 776 702 730 13 -86 37 C ATOM 1966 C LYS A 8 13.390 7.471 29.435 1.00 5.85 C ANISOU 1966 C LYS B 8 789 666 766 -19 -128 -35 C ATOM 1967 O LYS A 8 13.618 7.691 28.257 1.00 5.59 O ANISOU 1967 O LYS B 8 611 717 794 36 -89 -6 O ATOM 1968 CB LYS A 8 11.143 6.590 30.071 1.00 5.69 C ANISOU 1968 CB LYS B 8 731 730 698 89 -12 92 C ATOM 1969 CG LYS A 8 9.860 6.813 30.857 1.00 6.98 C ANISOU 1969 CG LYS B 8 899 759 994 32 144 53 C ATOM 1970 CD LYS A 8 9.086 5.520 31.009 1.00 7.91 C ANISOU 1970 CD LYS B 8 989 913 1101 16 61 88 C ATOM 1971 CE LYS A 8 8.434 5.152 29.708 1.00 6.16 C ANISOU 1971 CE LYS B 8 831 662 845 -183 -71 -62 C ATOM 1972 NZ LYS A 8 7.578 3.925 29.821 1.00 10.14 N ANISOU 1972 NZ LYS B 8 1272 1172 1406 -419 -46 101 N ATOM 1973 N THR A 9 14.266 6.906 30.255 1.00 6.43 N ANISOU 1973 N THR B 9 805 767 869 22 -109 1 N ATOM 1974 CA THR A 9 15.521 6.324 29.813 1.00 7.94 C ANISOU 1974 CA THR B 9 952 933 1131 12 -92 -97 C ATOM 1975 C THR A 9 15.257 4.958 29.168 1.00 6.29 C ANISOU 1975 C THR B 9 782 729 878 23 -108 -8 C ATOM 1976 O THR A 9 14.449 4.165 29.668 1.00 6.38 O ANISOU 1976 O THR B 9 947 562 913 -80 -51 -64 O ATOM 1977 CB THR A 9 16.457 6.165 31.039 1.00 9.04 C ANISOU 1977 CB THR B 9 1044 1043 1346 59 -154 -243 C ATOM 1978 OG1 THR A 9 16.756 7.454 31.603 1.00 12.19 O ANISOU 1978 OG1 THR B 9 1401 1275 1955 43 -379 -519 O ATOM 1979 CG2 THR A 9 17.833 5.592 30.648 1.00 11.63 C ANISOU 1979 CG2 THR B 9 1365 1457 1595 19 -93 -251 C ATOM 1980 N LEU A 10 15.953 4.666 28.087 1.00 5.68 N ANISOU 1980 N LEU B 10 660 628 870 80 -91 75 N ATOM 1981 CA LEU A 10 15.858 3.367 27.425 1.00 6.13 C ANISOU 1981 CA LEU B 10 730 744 852 13 -93 29 C ATOM 1982 C LEU A 10 16.370 2.311 28.387 1.00 5.81 C ANISOU 1982 C LEU B 10 689 663 854 41 -135 40 C ATOM 1983 O LEU A 10 17.511 2.392 28.850 1.00 7.38 O ANISOU 1983 O LEU B 10 734 920 1150 115 -372 99 O ATOM 1984 CB LEU A 10 16.695 3.334 26.154 1.00 6.55 C ANISOU 1984 CB LEU B 10 772 854 862 57 -67 -6 C ATOM 1985 CG LEU A 10 16.658 2.036 25.367 1.00 7.37 C ANISOU 1985 CG LEU B 10 921 1004 873 151 98 -10 C ATOM 1986 CD1 LEU A 10 15.293 1.712 24.839 1.00 7.55 C ANISOU 1986 CD1 LEU B 10 1169 737 960 60 149 -149 C ATOM 1987 CD2 LEU A 10 17.680 2.129 24.249 1.00 8.07 C ANISOU 1987 CD2 LEU B 10 915 1046 1105 86 214 -25 C ATOM 1988 N ALA A 11 15.533 1.338 28.702 1.00 5.38 N ANISOU 1988 N ALA B 11 684 563 796 146 -184 98 N ATOM 1989 CA ALA A 11 15.870 0.343 29.720 1.00 6.30 C ANISOU 1989 CA ALA B 11 808 721 864 92 -114 42 C ATOM 1990 C ALA A 11 15.110 -0.935 29.433 1.00 5.99 C ANISOU 1990 C ALA B 11 729 674 873 64 -116 95 C ATOM 1991 O ALA A 11 14.062 -0.908 28.792 1.00 7.23 O ANISOU 1991 O ALA B 11 766 762 1217 68 -118 76 O ATOM 1992 CB ALA A 11 15.494 0.862 31.087 1.00 7.09 C ANISOU 1992 CB ALA B 11 999 740 954 19 -89 50 C ATOM 1993 N ALA A 12 15.650 -2.047 29.938 1.00 6.04 N ANISOU 1993 N ALA B 12 721 697 876 25 -17 142 N ATOM 1994 CA ALA A 12 15.058 -3.370 29.787 1.00 6.38 C ANISOU 1994 CA ALA B 12 785 767 870 1 -18 27 C ATOM 1995 C ALA A 12 14.917 -3.983 31.166 1.00 6.33 C ANISOU 1995 C ALA B 12 768 732 903 -42 -90 66 C ATOM 1996 O ALA A 12 15.817 -3.870 31.999 1.00 7.40 O ANISOU 1996 O ALA B 12 857 968 984 9 -136 111 O ATOM 1997 CB ALA A 12 15.954 -4.265 28.927 1.00 7.81 C ANISOU 1997 CB ALA B 12 995 864 1107 -46 71 -38 C ATOM 1998 N ARG A 13 13.787 -4.636 31.390 1.00 5.81 N ANISOU 1998 N ARG B 13 708 685 813 -2 -101 147 N ATOM 1999 CA ARG A 13 13.582 -5.449 32.584 1.00 6.51 C ANISOU 1999 CA ARG B 13 908 722 843 -6 -127 93 C ATOM 2000 C ARG A 13 13.143 -6.855 32.171 1.00 6.43 C ANISOU 2000 C ARG B 13 876 757 810 -11 -203 88 C ATOM 2001 O ARG A 13 12.196 -7.017 31.409 1.00 7.27 O ANISOU 2001 O ARG B 13 942 732 1085 30 -161 -131 O ATOM 2002 CB ARG A 13 12.479 -4.856 33.453 1.00 7.83 C ANISOU 2002 CB ARG B 13 1206 784 984 -58 2 109 C ATOM 2003 CG ARG A 13 12.788 -3.477 34.049 1.00 9.60 C ANISOU 2003 CG ARG B 13 1409 1019 1217 -138 21 10 C ATOM 2004 CD ARG A 13 11.595 -2.895 34.803 1.00 11.64 C ANISOU 2004 CD ARG B 13 1834 1268 1317 -77 213 133 C ATOM 2005 NE ARG A 13 10.523 -2.470 33.910 1.00 12.80 N ANISOU 2005 NE ARG B 13 1850 1405 1606 -214 408 -43 N ATOM 2006 CZ ARG A 13 10.511 -1.334 33.226 1.00 13.08 C ANISOU 2006 CZ ARG B 13 1875 1459 1637 -80 201 17 C ATOM 2007 NH1 ARG A 13 11.513 -0.478 33.332 1.00 10.96 N ANISOU 2007 NH1 ARG B 13 1781 1189 1193 -236 74 6 N ATOM 2008 NH2 ARG A 13 9.497 -1.047 32.433 1.00 12.88 N ANISOU 2008 NH2 ARG B 13 1825 1196 1872 -373 341 -135 N ATOM 2009 N PRO A 14 13.795 -7.891 32.676 1.00 7.34 N ANISOU 2009 N PRO B 14 871 869 1047 -3 -228 11 N ATOM 2010 CA PRO A 14 13.254 -9.230 32.444 1.00 7.89 C ANISOU 2010 CA PRO B 14 1074 897 1027 35 -123 81 C ATOM 2011 C PRO A 14 11.913 -9.395 33.124 1.00 7.89 C ANISOU 2011 C PRO B 14 1073 938 984 17 -100 28 C ATOM 2012 O PRO A 14 11.661 -8.796 34.163 1.00 9.51 O ANISOU 2012 O PRO B 14 1266 1046 1301 -160 172 -169 O ATOM 2013 CB PRO A 14 14.301 -10.147 33.076 1.00 7.82 C ANISOU 2013 CB PRO B 14 957 921 1092 71 -191 66 C ATOM 2014 CG PRO A 14 15.069 -9.294 33.925 1.00 11.34 C ANISOU 2014 CG PRO B 14 1377 1355 1577 101 -115 -116 C ATOM 2015 CD PRO A 14 15.052 -7.919 33.447 1.00 9.21 C ANISOU 2015 CD PRO B 14 1068 1098 1332 3 -185 -29 C ATOM 2016 N VAL A 15 11.071 -10.229 32.547 1.00 7.39 N ANISOU 2016 N VAL B 15 1022 878 907 -2 -64 59 N ATOM 2017 CA VAL A 15 9.811 -10.641 33.152 1.00 7.18 C ANISOU 2017 CA VAL B 15 990 792 944 -39 -34 152 C ATOM 2018 C VAL A 15 10.074 -12.038 33.787 1.00 6.71 C ANISOU 2018 C VAL B 15 914 823 813 -42 -64 178 C ATOM 2019 O VAL A 15 10.160 -13.034 33.083 1.00 6.56 O ANISOU 2019 O VAL B 15 951 633 906 -185 -9 245 O ATOM 2020 CB VAL A 15 8.678 -10.650 32.099 1.00 8.22 C ANISOU 2020 CB VAL B 15 1030 1014 1077 -37 -30 -10 C ATOM 2021 CG1 VAL A 15 7.382 -11.192 32.669 1.00 7.94 C ANISOU 2021 CG1 VAL B 15 1120 925 970 55 -51 227 C ATOM 2022 CG2 VAL A 15 8.452 -9.240 31.547 1.00 9.50 C ANISOU 2022 CG2 VAL B 15 1147 1238 1225 -2 50 74 C ATOM 2023 N GLU A 16 10.285 -12.058 35.095 1.00 7.13 N ANISOU 2023 N GLU B 16 902 747 1060 -97 57 8 N ATOM 2024 CA GLU A 16 10.843 -13.251 35.746 1.00 7.56 C ANISOU 2024 CA GLU B 16 863 909 1098 -30 7 -25 C ATOM 2025 C GLU A 16 9.925 -14.472 35.633 1.00 7.13 C ANISOU 2025 C GLU B 16 807 877 1022 -20 -6 77 C ATOM 2026 O GLU A 16 10.418 -15.557 35.493 1.00 9.26 O ANISOU 2026 O GLU B 16 657 1283 1577 26 34 -325 O ATOM 2027 CB GLU A 16 11.215 -12.984 37.212 1.00 7.65 C ANISOU 2027 CB GLU B 16 913 895 1098 43 -21 41 C ATOM 2028 CG GLU A 16 10.058 -12.579 38.121 1.00 9.53 C ANISOU 2028 CG GLU B 16 1248 1093 1280 65 12 92 C ATOM 2029 CD GLU A 16 9.885 -11.073 38.256 1.00 14.20 C ANISOU 2029 CD GLU B 16 1778 1587 2029 242 256 -235 C ATOM 2030 OE1 GLU A 16 10.333 -10.314 37.356 1.00 11.74 O ANISOU 2030 OE1 GLU B 16 1401 1527 1532 248 167 190 O ATOM 2031 OE2 GLU A 16 9.287 -10.663 39.280 1.00 16.84 O ANISOU 2031 OE2 GLU B 16 2353 1679 2367 315 461 -53 O ATOM 2032 N ALA A 17 8.609 -14.268 35.577 1.00 7.55 N ANISOU 2032 N ALA B 17 835 911 1122 -70 19 33 N ATOM 2033 CA ALA A 17 7.661 -15.365 35.375 1.00 8.20 C ANISOU 2033 CA ALA B 17 893 1005 1215 -11 -7 -51 C ATOM 2034 C ALA A 17 7.747 -16.048 34.001 1.00 6.44 C ANISOU 2034 C ALA B 17 721 779 945 -13 -47 112 C ATOM 2035 O ALA A 17 7.301 -17.192 33.868 1.00 9.58 O ANISOU 2035 O ALA B 17 702 1334 1603 -105 46 -666 O ATOM 2036 CB ALA A 17 6.226 -14.878 35.642 1.00 8.83 C ANISOU 2036 CB ALA B 17 969 1077 1307 6 9 -66 C ATOM 2037 N ILE A 18 8.271 -15.350 32.979 1.00 6.78 N ANISOU 2037 N ILE B 18 669 838 1065 -75 0 -60 N ATOM 2038 CA ILE A 18 8.310 -15.925 31.651 1.00 6.13 C ANISOU 2038 CA ILE B 18 676 738 913 26 -65 144 C ATOM 2039 C ILE A 18 9.731 -15.802 31.109 1.00 6.50 C ANISOU 2039 C ILE B 18 666 784 1017 27 -95 19 C ATOM 2040 O ILE A 18 10.095 -14.749 30.613 1.00 8.04 O ANISOU 2040 O ILE B 18 584 1136 1334 -108 -25 -343 O ATOM 2041 CB ILE A 18 7.250 -15.232 30.722 1.00 6.37 C ANISOU 2041 CB ILE B 18 749 690 979 38 -71 147 C ATOM 2042 CG1 ILE A 18 5.843 -15.391 31.321 1.00 7.53 C ANISOU 2042 CG1 ILE B 18 784 1034 1042 142 -205 155 C ATOM 2043 CG2 ILE A 18 7.335 -15.843 29.360 1.00 7.24 C ANISOU 2043 CG2 ILE B 18 745 860 1145 103 -119 150 C ATOM 2044 CD1 ILE A 18 4.718 -14.669 30.594 1.00 8.91 C ANISOU 2044 CD1 ILE B 18 946 1200 1237 101 -104 37 C ATOM 2045 N PRO A 19 10.562 -16.870 31.288 1.00 6.05 N ANISOU 2045 N PRO B 19 679 630 987 -32 -47 124 N ATOM 2046 CA PRO A 19 11.965 -16.782 30.825 1.00 6.67 C ANISOU 2046 CA PRO B 19 721 809 1005 23 -49 38 C ATOM 2047 C PRO A 19 12.082 -16.301 29.368 1.00 6.62 C ANISOU 2047 C PRO B 19 768 755 992 89 -40 69 C ATOM 2048 O PRO A 19 11.378 -16.803 28.518 1.00 7.45 O ANISOU 2048 O PRO B 19 903 759 1167 -29 -24 -40 O ATOM 2049 CB PRO A 19 12.486 -18.217 31.000 1.00 7.94 C ANISOU 2049 CB PRO B 19 844 1021 1151 -25 29 -56 C ATOM 2050 CG PRO A 19 11.691 -18.708 32.111 1.00 7.76 C ANISOU 2050 CG PRO B 19 876 907 1164 42 -5 31 C ATOM 2051 CD PRO A 19 10.291 -18.175 31.959 1.00 6.42 C ANISOU 2051 CD PRO B 19 717 683 1040 33 -64 120 C ATOM 2052 N GLY A 20 12.953 -15.312 29.128 1.00 6.20 N ANISOU 2052 N GLY B 20 600 729 1026 13 -31 -24 N ATOM 2053 CA GLY A 20 13.245 -14.786 27.811 1.00 6.95 C ANISOU 2053 CA GLY B 20 741 905 992 60 61 -89 C ATOM 2054 C GLY A 20 12.439 -13.551 27.516 1.00 6.59 C ANISOU 2054 C GLY B 20 659 864 979 72 33 -54 C ATOM 2055 O GLY A 20 12.814 -12.759 26.630 1.00 6.23 O ANISOU 2055 O GLY B 20 853 548 964 145 187 250 O ATOM 2056 N MET A 21 11.324 -13.354 28.209 1.00 6.06 N ANISOU 2056 N MET B 21 741 665 894 -9 78 19 N ATOM 2057 CA MET A 21 10.572 -12.111 27.993 1.00 5.46 C ANISOU 2057 CA MET B 21 666 592 814 52 -19 71 C ATOM 2058 C MET A 21 11.255 -10.883 28.587 1.00 5.93 C ANISOU 2058 C MET B 21 631 780 840 -33 -63 -40 C ATOM 2059 O MET A 21 11.817 -10.935 29.669 1.00 5.13 O ANISOU 2059 O MET B 21 531 615 801 -46 0 101 O ATOM 2060 CB MET A 21 9.175 -12.237 28.572 1.00 6.04 C ANISOU 2060 CB MET B 21 653 670 969 6 -15 -16 C ATOM 2061 CG MET A 21 8.318 -10.998 28.510 1.00 8.01 C ANISOU 2061 CG MET B 21 1029 984 1029 73 42 -102 C ATOM 2062 SD MET A 21 6.612 -11.311 28.998 1.00 12.25 S ANISOU 2062 SD MET B 21 1115 2071 1468 309 166 77 S ATOM 2063 CE MET A 21 6.315 -12.670 28.256 1.00 5.16 C ANISOU 2063 CE MET B 21 274 879 808 -100 20 186 C ATOM 2064 N LEU A 22 11.187 -9.773 27.861 1.00 5.58 N ANISOU 2064 N LEU B 22 664 677 778 -24 -28 12 N ATOM 2065 CA LEU A 22 11.785 -8.492 28.267 1.00 6.32 C ANISOU 2065 CA LEU B 22 798 760 842 -40 -35 -33 C ATOM 2066 C LEU A 22 10.779 -7.363 28.065 1.00 5.98 C ANISOU 2066 C LEU B 22 858 719 695 32 -87 24 C ATOM 2067 O LEU A 22 10.097 -7.313 27.054 1.00 8.13 O ANISOU 2067 O LEU B 22 1347 870 871 198 -217 -128 O ATOM 2068 CB LEU A 22 13.006 -8.182 27.412 1.00 7.45 C ANISOU 2068 CB LEU B 22 966 868 995 -11 16 -31 C ATOM 2069 CG LEU A 22 14.163 -9.171 27.464 1.00 9.63 C ANISOU 2069 CG LEU B 22 1150 1141 1367 -52 161 88 C ATOM 2070 CD1 LEU A 22 15.084 -8.929 26.263 1.00 12.32 C ANISOU 2070 CD1 LEU B 22 1581 1472 1627 126 250 119 C ATOM 2071 CD2 LEU A 22 14.916 -9.002 28.746 1.00 13.09 C ANISOU 2071 CD2 LEU B 22 1413 1677 1882 125 72 172 C ATOM 2072 N GLU A 23 10.693 -6.477 29.039 1.00 5.72 N ANISOU 2072 N GLU B 23 789 638 744 40 -112 81 N ATOM 2073 CA GLU A 23 9.899 -5.266 28.927 1.00 6.56 C ANISOU 2073 CA GLU B 23 851 755 886 9 -43 55 C ATOM 2074 C GLU A 23 10.845 -4.098 28.807 1.00 5.96 C ANISOU 2074 C GLU B 23 798 655 812 -79 -133 78 C ATOM 2075 O GLU A 23 11.827 -4.001 29.540 1.00 7.26 O ANISOU 2075 O GLU B 23 993 753 1010 -164 -273 246 O ATOM 2076 CB GLU A 23 9.045 -5.105 30.183 1.00 7.79 C ANISOU 2076 CB GLU B 23 1038 835 1084 35 72 7 C ATOM 2077 CG GLU A 23 8.182 -3.851 30.224 1.00 10.12 C ANISOU 2077 CG GLU B 23 1289 1211 1344 -13 194 30 C ATOM 2078 CD GLU A 23 7.276 -3.833 31.435 1.00 12.71 C ANISOU 2078 CD GLU B 23 1732 1629 1468 -218 201 -77 C ATOM 2079 OE1 GLU A 23 6.478 -4.758 31.562 1.00 14.30 O ANISOU 2079 OE1 GLU B 23 1716 1767 1948 -527 472 -99 O ATOM 2080 OE2 GLU A 23 7.354 -2.908 32.250 1.00 15.02 O ANISOU 2080 OE2 GLU B 23 2045 1801 1859 -627 654 -249 O ATOM 2081 N PHE A 24 10.557 -3.198 27.875 1.00 5.81 N ANISOU 2081 N PHE B 24 748 689 771 -80 -70 58 N ATOM 2082 CA PHE A 24 11.397 -2.025 27.648 1.00 6.09 C ANISOU 2082 CA PHE B 24 718 707 889 -27 -67 24 C ATOM 2083 C PHE A 24 10.642 -0.739 27.922 1.00 5.45 C ANISOU 2083 C PHE B 24 656 619 795 -31 -69 116 C ATOM 2084 O PHE A 24 9.465 -0.597 27.557 1.00 6.51 O ANISOU 2084 O PHE B 24 764 568 1139 -12 -259 61 O ATOM 2085 CB PHE A 24 11.914 -1.966 26.203 1.00 6.32 C ANISOU 2085 CB PHE B 24 744 730 925 -32 -25 47 C ATOM 2086 CG PHE A 24 12.771 -3.138 25.805 1.00 7.85 C ANISOU 2086 CG PHE B 24 1133 851 997 -60 61 93 C ATOM 2087 CD1 PHE A 24 12.203 -4.301 25.332 1.00 8.53 C ANISOU 2087 CD1 PHE B 24 1417 922 901 -99 29 207 C ATOM 2088 CD2 PHE A 24 14.159 -3.054 25.854 1.00 11.07 C ANISOU 2088 CD2 PHE B 24 1426 1174 1604 288 -97 -312 C ATOM 2089 CE1 PHE A 24 13.012 -5.380 24.972 1.00 9.88 C ANISOU 2089 CE1 PHE B 24 1815 1001 937 -129 115 -7 C ATOM 2090 CE2 PHE A 24 14.959 -4.138 25.463 1.00 12.59 C ANISOU 2090 CE2 PHE B 24 1447 1698 1638 204 -62 -205 C ATOM 2091 CZ PHE A 24 14.370 -5.289 25.032 1.00 11.34 C ANISOU 2091 CZ PHE B 24 1866 1240 1200 475 -38 2 C ATOM 2092 N ASP A 25 11.348 0.207 28.528 1.00 5.36 N ANISOU 2092 N ASP B 25 759 542 733 15 -99 76 N ATOM 2093 CA ASP A 25 10.958 1.609 28.477 1.00 5.50 C ANISOU 2093 CA ASP B 25 747 626 713 5 21 50 C ATOM 2094 C ASP A 25 11.602 2.244 27.253 1.00 4.98 C ANISOU 2094 C ASP B 25 637 586 666 27 25 48 C ATOM 2095 O ASP A 25 12.801 2.136 27.059 1.00 5.62 O ANISOU 2095 O ASP B 25 604 776 754 170 -112 30 O ATOM 2096 CB ASP A 25 11.440 2.366 29.688 1.00 6.00 C ANISOU 2096 CB ASP B 25 895 664 721 -95 -32 130 C ATOM 2097 CG ASP A 25 10.753 1.970 30.947 1.00 8.75 C ANISOU 2097 CG ASP B 25 1219 1081 1024 -308 -65 -70 C ATOM 2098 OD1 ASP A 25 9.566 1.591 30.911 1.00 11.22 O ANISOU 2098 OD1 ASP B 25 1615 1767 881 -514 26 26 O ATOM 2099 OD2 ASP A 25 11.342 2.072 32.032 1.00 10.28 O ANISOU 2099 OD2 ASP B 25 1630 1454 821 -578 -126 101 O ATOM 2100 N ILE A 26 10.807 2.955 26.467 1.00 4.28 N ANISOU 2100 N ILE B 26 496 584 544 30 94 66 N ATOM 2101 CA ILE A 26 11.242 3.627 25.248 1.00 4.36 C ANISOU 2101 CA ILE B 26 518 597 541 22 74 40 C ATOM 2102 C ILE A 26 11.175 5.133 25.483 1.00 4.65 C ANISOU 2102 C ILE B 26 599 534 631 50 71 72 C ATOM 2103 O ILE A 26 10.134 5.647 25.894 1.00 4.53 O ANISOU 2103 O ILE B 26 525 524 672 43 133 66 O ATOM 2104 CB ILE A 26 10.317 3.258 24.084 1.00 4.94 C ANISOU 2104 CB ILE B 26 565 667 644 -16 108 80 C ATOM 2105 CG1 ILE A 26 10.328 1.746 23.861 1.00 6.71 C ANISOU 2105 CG1 ILE B 26 761 922 866 -7 -198 3 C ATOM 2106 CG2 ILE A 26 10.702 4.009 22.832 1.00 6.35 C ANISOU 2106 CG2 ILE B 26 702 883 824 150 80 66 C ATOM 2107 CD1 ILE A 26 11.650 1.121 23.554 1.00 9.78 C ANISOU 2107 CD1 ILE B 26 1239 1057 1419 18 -32 -60 C ATOM 2108 N PRO A 27 12.252 5.863 25.212 1.00 4.40 N ANISOU 2108 N PRO B 27 453 535 682 76 70 15 N ATOM 2109 CA PRO A 27 12.205 7.331 25.286 1.00 4.52 C ANISOU 2109 CA PRO B 27 516 582 618 6 82 31 C ATOM 2110 C PRO A 27 11.278 7.911 24.213 1.00 3.86 C ANISOU 2110 C PRO B 27 469 520 477 30 113 90 C ATOM 2111 O PRO A 27 11.451 7.632 23.030 1.00 4.51 O ANISOU 2111 O PRO B 27 566 732 413 197 125 -34 O ATOM 2112 CB PRO A 27 13.667 7.748 25.045 1.00 4.66 C ANISOU 2112 CB PRO B 27 589 526 654 19 56 -5 C ATOM 2113 CG PRO A 27 14.485 6.526 25.315 1.00 5.82 C ANISOU 2113 CG PRO B 27 632 722 855 21 86 6 C ATOM 2114 CD PRO A 27 13.612 5.384 24.874 1.00 5.50 C ANISOU 2114 CD PRO B 27 553 588 947 71 39 36 C ATOM 2115 N VAL A 28 10.283 8.671 24.643 1.00 3.15 N ANISOU 2115 N VAL B 28 390 416 389 35 113 98 N ATOM 2116 CA VAL A 28 9.356 9.360 23.762 1.00 3.11 C ANISOU 2116 CA VAL B 28 409 503 269 64 49 15 C ATOM 2117 C VAL A 28 9.510 10.836 24.050 1.00 3.44 C ANISOU 2117 C VAL B 28 412 495 400 100 8 -35 C ATOM 2118 O VAL A 28 9.425 11.255 25.203 1.00 3.97 O ANISOU 2118 O VAL B 28 694 485 327 0 148 -15 O ATOM 2119 CB VAL A 28 7.891 8.916 24.002 1.00 3.59 C ANISOU 2119 CB VAL B 28 507 547 309 46 21 -13 C ATOM 2120 CG1 VAL A 28 6.948 9.639 23.057 1.00 4.35 C ANISOU 2120 CG1 VAL B 28 479 831 343 -6 28 2 C ATOM 2121 CG2 VAL A 28 7.723 7.393 23.865 1.00 4.13 C ANISOU 2121 CG2 VAL B 28 404 672 493 74 27 71 C ATOM 2122 N HIS A 29 9.761 11.612 22.991 1.00 3.06 N ANISOU 2122 N HIS B 29 360 425 376 21 -107 -71 N ATOM 2123 CA HIS A 29 10.089 13.033 23.123 1.00 3.60 C ANISOU 2123 CA HIS B 29 421 409 537 0 -72 -54 C ATOM 2124 C HIS A 29 9.015 13.891 22.527 1.00 3.53 C ANISOU 2124 C HIS B 29 395 447 496 -19 -68 -30 C ATOM 2125 O HIS A 29 8.695 13.752 21.349 1.00 3.41 O ANISOU 2125 O HIS B 29 423 452 418 21 -162 -66 O ATOM 2126 CB HIS A 29 11.397 13.309 22.422 1.00 5.41 C ANISOU 2126 CB HIS B 29 562 644 849 20 -23 10 C ATOM 2127 CG HIS A 29 12.506 12.460 22.951 1.00 8.13 C ANISOU 2127 CG HIS B 29 841 895 1352 136 -17 -25 C ATOM 2128 ND1 HIS A 29 13.138 11.475 22.223 1.00 10.82 N ANISOU 2128 ND1 HIS B 29 950 1309 1852 -11 14 308 N ATOM 2129 CD2 HIS A 29 13.039 12.416 24.186 1.00 9.67 C ANISOU 2129 CD2 HIS B 29 1006 1192 1475 299 -284 79 C ATOM 2130 CE1 HIS A 29 14.047 10.891 22.988 1.00 8.62 C ANISOU 2130 CE1 HIS B 29 773 1020 1482 244 -203 241 C ATOM 2131 NE2 HIS A 29 13.991 11.429 24.189 1.00 12.74 N ANISOU 2131 NE2 HIS B 29 1062 1496 2282 424 -397 358 N ATOM 2132 N GLY A 30 8.442 14.770 23.335 1.00 4.07 N ANISOU 2132 N GLY B 30 504 532 509 50 -152 -58 N ATOM 2133 CA GLY A 30 7.412 15.668 22.874 1.00 4.26 C ANISOU 2133 CA GLY B 30 507 627 484 108 -189 -106 C ATOM 2134 C GLY A 30 6.367 15.842 23.946 1.00 5.60 C ANISOU 2134 C GLY B 30 676 864 585 184 -141 -84 C ATOM 2135 O GLY A 30 6.675 15.907 25.134 1.00 6.76 O ANISOU 2135 O GLY B 30 723 1188 656 305 -332 -149 O ATOM 2136 N ASP A 31 5.123 15.941 23.518 1.00 5.29 N ANISOU 2136 N ASP B 31 615 911 483 197 -33 -109 N ATOM 2137 CA ASP A 31 4.009 16.150 24.418 1.00 7.06 C ANISOU 2137 CA ASP B 31 882 1042 758 126 -23 16 C ATOM 2138 C ASP A 31 2.759 15.672 23.695 1.00 7.38 C ANISOU 2138 C ASP B 31 891 1212 699 124 -6 71 C ATOM 2139 O ASP A 31 2.833 14.992 22.650 1.00 6.10 O ANISOU 2139 O ASP B 31 698 1142 475 178 -144 220 O ATOM 2140 CB ASP A 31 3.932 17.623 24.855 1.00 8.25 C ANISOU 2140 CB ASP B 31 1083 1151 899 76 -72 1 C ATOM 2141 CG ASP A 31 3.827 18.582 23.684 1.00 9.86 C ANISOU 2141 CG ASP B 31 1504 1015 1226 46 -184 -88 C ATOM 2142 OD1 ASP A 31 4.380 19.696 23.772 1.00 13.92 O ANISOU 2142 OD1 ASP B 31 2176 1715 1397 -145 -242 176 O ATOM 2143 OD2 ASP A 31 3.200 18.314 22.647 1.00 11.72 O ANISOU 2143 OD2 ASP B 31 1525 1311 1616 637 -467 269 O ATOM 2144 N ASN A 32 1.619 16.037 24.273 1.00 9.27 N ANISOU 2144 N ASN B 32 1095 1550 878 89 31 164 N ATOM 2145 CA ASN A 32 0.308 15.720 23.763 1.00 10.94 C ANISOU 2145 CA ASN B 32 1323 1697 1136 -38 20 146 C ATOM 2146 C ASN A 32 0.086 16.083 22.305 1.00 8.75 C ANISOU 2146 C ASN B 32 1063 1434 826 95 48 110 C ATOM 2147 O ASN A 32 -0.625 15.370 21.604 1.00 10.54 O ANISOU 2147 O ASN B 32 1163 1892 950 100 179 284 O ATOM 2148 CB ASN A 32 -0.799 16.339 24.664 1.00 11.87 C ANISOU 2148 CB ASN B 32 1447 1766 1297 -62 1 155 C ATOM 2149 CG ASN A 32 -0.888 17.912 24.604 1.00 14.29 C ANISOU 2149 CG ASN B 32 1590 2213 1623 -105 63 64 C ATOM 2150 OD1 ASN A 32 0.119 18.629 24.688 1.00 18.28 O ANISOU 2150 OD1 ASN B 32 2214 2677 2054 -485 162 -137 O ATOM 2151 ND2 ASN A 32 -2.105 18.428 24.509 1.00 16.98 N ANISOU 2151 ND2 ASN B 32 1903 2566 1983 38 217 0 N ATOM 2152 N ARG A 33 0.698 17.184 21.892 1.00 7.53 N ANISOU 2152 N ARG B 33 853 1285 721 203 79 26 N ATOM 2153 CA ARG A 33 0.529 17.725 20.545 1.00 7.36 C ANISOU 2153 CA ARG B 33 958 1154 684 89 29 51 C ATOM 2154 C ARG A 33 1.254 16.900 19.491 1.00 5.63 C ANISOU 2154 C ARG B 33 632 998 509 188 41 48 C ATOM 2155 O ARG A 33 0.901 16.960 18.332 1.00 5.77 O ANISOU 2155 O ARG B 33 635 1238 318 265 -16 215 O ATOM 2156 CB ARG A 33 1.067 19.160 20.456 1.00 8.13 C ANISOU 2156 CB ARG B 33 1091 1196 800 110 0 0 C ATOM 2157 CG ARG A 33 0.292 20.208 21.229 1.00 11.02 C ANISOU 2157 CG ARG B 33 1479 1506 1202 -22 108 39 C ATOM 2158 CD ARG A 33 0.907 21.601 21.196 1.00 13.06 C ANISOU 2158 CD ARG B 33 1614 1867 1479 -13 53 -46 C ATOM 2159 NE ARG A 33 2.086 21.713 22.056 1.00 15.70 N ANISOU 2159 NE ARG B 33 1725 2407 1832 -117 115 -13 N ATOM 2160 CZ ARG A 33 3.342 21.921 21.647 1.00 16.55 C ANISOU 2160 CZ ARG B 33 1971 2468 1848 -98 71 -49 C ATOM 2161 NH1 ARG A 33 3.648 22.045 20.356 1.00 18.42 N ANISOU 2161 NH1 ARG B 33 2239 2676 2084 -57 179 -21 N ATOM 2162 NH2 ARG A 33 4.313 22.010 22.548 1.00 18.19 N ANISOU 2162 NH2 ARG B 33 2228 2556 2126 -133 -82 -17 N ATOM 2163 N GLY A 34 2.294 16.174 19.885 1.00 4.00 N ANISOU 2163 N GLY B 34 526 704 291 144 -40 -110 N ATOM 2164 CA GLY A 34 3.132 15.485 18.924 1.00 4.76 C ANISOU 2164 CA GLY B 34 535 783 489 122 -29 -83 C ATOM 2165 C GLY A 34 4.388 14.987 19.566 1.00 2.86 C ANISOU 2165 C GLY B 34 317 501 268 76 -25 -59 C ATOM 2166 O GLY A 34 4.926 15.624 20.465 1.00 3.15 O ANISOU 2166 O GLY B 34 423 466 306 102 -92 -32 O ATOM 2167 N TRP A 35 4.894 13.865 19.076 1.00 2.40 N ANISOU 2167 N TRP B 35 254 390 265 12 -3 -41 N ATOM 2168 CA TRP A 35 6.082 13.275 19.665 1.00 2.14 C ANISOU 2168 CA TRP B 35 265 288 260 -20 9 -15 C ATOM 2169 C TRP A 35 6.793 12.385 18.689 1.00 2.35 C ANISOU 2169 C TRP B 35 258 357 277 -18 10 -36 C ATOM 2170 O TRP A 35 6.277 12.093 17.601 1.00 2.91 O ANISOU 2170 O TRP B 35 255 444 407 -18 16 -171 O ATOM 2171 CB TRP A 35 5.746 12.522 20.971 1.00 2.51 C ANISOU 2171 CB TRP B 35 259 358 337 -8 19 14 C ATOM 2172 CG TRP A 35 4.579 11.585 20.908 1.00 2.73 C ANISOU 2172 CG TRP B 35 272 440 323 -2 -16 -100 C ATOM 2173 CD1 TRP A 35 3.340 11.806 21.456 1.00 3.61 C ANISOU 2173 CD1 TRP B 35 435 682 253 -200 3 -7 C ATOM 2174 CD2 TRP A 35 4.534 10.272 20.333 1.00 3.64 C ANISOU 2174 CD2 TRP B 35 524 552 305 -246 -72 115 C ATOM 2175 NE1 TRP A 35 2.532 10.718 21.240 1.00 5.52 N ANISOU 2175 NE1 TRP B 35 629 1029 437 -413 155 25 N ATOM 2176 CE2 TRP A 35 3.240 9.753 20.574 1.00 3.92 C ANISOU 2176 CE2 TRP B 35 679 512 296 -329 -99 86 C ATOM 2177 CE3 TRP A 35 5.453 9.466 19.659 1.00 4.32 C ANISOU 2177 CE3 TRP B 35 679 532 430 -212 -133 3 C ATOM 2178 CZ2 TRP A 35 2.843 8.482 20.148 1.00 5.32 C ANISOU 2178 CZ2 TRP B 35 601 837 581 -371 -215 203 C ATOM 2179 CZ3 TRP A 35 5.036 8.232 19.196 1.00 5.06 C ANISOU 2179 CZ3 TRP B 35 668 612 639 -152 -273 -56 C ATOM 2180 CH2 TRP A 35 3.742 7.749 19.453 1.00 5.54 C ANISOU 2180 CH2 TRP B 35 1037 440 625 -177 -254 145 C ATOM 2181 N PHE A 36 7.981 11.950 19.083 1.00 2.46 N ANISOU 2181 N PHE B 36 260 381 292 30 -16 -70 N ATOM 2182 CA PHE A 36 8.844 11.093 18.290 1.00 3.18 C ANISOU 2182 CA PHE B 36 336 483 389 43 -7 -103 C ATOM 2183 C PHE A 36 9.502 10.074 19.190 1.00 2.87 C ANISOU 2183 C PHE B 36 259 447 381 2 20 -101 C ATOM 2184 O PHE A 36 9.815 10.368 20.330 1.00 3.41 O ANISOU 2184 O PHE B 36 283 624 388 55 -55 -194 O ATOM 2185 CB PHE A 36 9.932 11.955 17.609 1.00 5.94 C ANISOU 2185 CB PHE B 36 732 781 742 202 248 -1 C ATOM 2186 CG PHE A 36 11.009 11.168 16.933 1.00 11.29 C ANISOU 2186 CG PHE B 36 1392 1535 1360 -185 142 -21 C ATOM 2187 CD1 PHE A 36 10.894 10.788 15.604 1.00 13.75 C ANISOU 2187 CD1 PHE B 36 1620 1922 1680 35 398 -285 C ATOM 2188 CD2 PHE A 36 12.130 10.791 17.652 1.00 13.49 C ANISOU 2188 CD2 PHE B 36 1324 1983 1818 -92 397 145 C ATOM 2189 CE1 PHE A 36 11.901 10.020 15.001 1.00 17.03 C ANISOU 2189 CE1 PHE B 36 2165 2109 2196 186 271 -550 C ATOM 2190 CE2 PHE A 36 13.140 10.035 17.049 1.00 17.59 C ANISOU 2190 CE2 PHE B 36 2051 2213 2419 -56 176 -101 C ATOM 2191 CZ PHE A 36 13.016 9.656 15.735 1.00 17.65 C ANISOU 2191 CZ PHE B 36 2164 2307 2234 12 264 -228 C ATOM 2192 N LYS A 37 9.739 8.887 18.652 1.00 2.67 N ANISOU 2192 N LYS B 37 276 393 343 41 -36 -111 N ATOM 2193 CA LYS A 37 10.525 7.875 19.344 1.00 2.57 C ANISOU 2193 CA LYS B 37 329 352 293 10 7 -60 C ATOM 2194 C LYS A 37 11.332 7.053 18.340 1.00 3.12 C ANISOU 2194 C LYS B 37 356 479 350 0 52 -126 C ATOM 2195 O LYS A 37 10.941 6.853 17.186 1.00 3.45 O ANISOU 2195 O LYS B 37 467 467 375 62 -18 -81 O ATOM 2196 CB LYS A 37 9.638 6.928 20.162 1.00 2.92 C ANISOU 2196 CB LYS B 37 323 320 463 41 48 -58 C ATOM 2197 CG LYS A 37 8.604 6.137 19.382 1.00 3.38 C ANISOU 2197 CG LYS B 37 382 433 465 -10 42 -78 C ATOM 2198 CD LYS A 37 8.042 5.003 20.190 1.00 3.61 C ANISOU 2198 CD LYS B 37 407 605 357 -100 103 -167 C ATOM 2199 CE LYS A 37 6.872 4.319 19.526 1.00 3.88 C ANISOU 2199 CE LYS B 37 579 419 476 22 203 -54 C ATOM 2200 NZ LYS A 37 6.465 3.088 20.311 1.00 4.02 N ANISOU 2200 NZ LYS B 37 642 462 422 -188 20 10 N ATOM 2201 N GLU A 38 12.437 6.511 18.831 1.00 3.29 N ANISOU 2201 N GLU B 38 375 475 398 24 40 -160 N ATOM 2202 CA GLU A 38 13.092 5.372 18.210 1.00 3.14 C ANISOU 2202 CA GLU B 38 394 432 364 20 42 -125 C ATOM 2203 C GLU A 38 12.391 4.141 18.787 1.00 4.22 C ANISOU 2203 C GLU B 38 660 511 430 40 92 -49 C ATOM 2204 O GLU A 38 12.645 3.726 19.912 1.00 6.16 O ANISOU 2204 O GLU B 38 1042 815 482 -257 -137 59 O ATOM 2205 CB GLU A 38 14.581 5.323 18.545 1.00 4.67 C ANISOU 2205 CB GLU B 38 511 665 595 137 17 -156 C ATOM 2206 CG GLU A 38 15.318 6.570 18.142 1.00 5.49 C ANISOU 2206 CG GLU B 38 497 815 772 121 -56 -127 C ATOM 2207 CD GLU A 38 16.809 6.543 18.448 1.00 7.61 C ANISOU 2207 CD GLU B 38 757 1152 982 165 -65 -223 C ATOM 2208 OE1 GLU A 38 17.256 5.782 19.345 1.00 9.85 O ANISOU 2208 OE1 GLU B 38 632 1331 1777 -90 -378 -177 O ATOM 2209 OE2 GLU A 38 17.511 7.321 17.776 1.00 10.49 O ANISOU 2209 OE2 GLU B 38 954 1450 1578 -252 222 -98 O ATOM 2210 N ASN A 39 11.464 3.571 18.036 1.00 3.53 N ANISOU 2210 N ASN B 39 457 442 441 25 67 71 N ATOM 2211 CA ASN A 39 10.734 2.414 18.506 1.00 3.70 C ANISOU 2211 CA ASN B 39 493 458 453 10 154 -31 C ATOM 2212 C ASN A 39 11.610 1.181 18.678 1.00 3.78 C ANISOU 2212 C ASN B 39 525 500 408 10 14 -34 C ATOM 2213 O ASN A 39 11.402 0.381 19.564 1.00 4.64 O ANISOU 2213 O ASN B 39 740 387 634 51 147 40 O ATOM 2214 CB ASN A 39 9.573 2.097 17.552 1.00 4.99 C ANISOU 2214 CB ASN B 39 497 703 696 55 127 149 C ATOM 2215 CG ASN A 39 8.693 1.012 18.087 1.00 5.64 C ANISOU 2215 CG ASN B 39 612 723 805 -9 122 25 C ATOM 2216 OD1 ASN A 39 8.140 1.129 19.196 1.00 6.83 O ANISOU 2216 OD1 ASN B 39 746 839 1007 -126 390 -20 O ATOM 2217 ND2 ASN A 39 8.581 -0.083 17.336 1.00 5.84 N ANISOU 2217 ND2 ASN B 39 637 903 676 -162 -23 4 N ATOM 2218 N PHE A 40 12.578 1.016 17.792 1.00 3.84 N ANISOU 2218 N PHE B 40 603 348 506 59 122 84 N ATOM 2219 CA PHE A 40 13.523 -0.068 17.840 1.00 4.56 C ANISOU 2219 CA PHE B 40 622 534 575 27 39 52 C ATOM 2220 C PHE A 40 14.820 0.409 17.235 1.00 4.30 C ANISOU 2220 C PHE B 40 620 516 498 52 60 10 C ATOM 2221 O PHE A 40 14.861 0.895 16.111 1.00 5.06 O ANISOU 2221 O PHE B 40 686 824 413 62 -16 212 O ATOM 2222 CB PHE A 40 13.023 -1.297 17.064 1.00 5.39 C ANISOU 2222 CB PHE B 40 697 616 734 -1 145 53 C ATOM 2223 CG PHE A 40 13.945 -2.477 17.225 1.00 6.86 C ANISOU 2223 CG PHE B 40 971 690 943 -64 82 -133 C ATOM 2224 CD1 PHE A 40 13.932 -3.239 18.401 1.00 8.17 C ANISOU 2224 CD1 PHE B 40 1278 547 1279 195 89 -49 C ATOM 2225 CD2 PHE A 40 14.886 -2.768 16.260 1.00 9.23 C ANISOU 2225 CD2 PHE B 40 1366 672 1469 15 158 -209 C ATOM 2226 CE1 PHE A 40 14.796 -4.283 18.582 1.00 11.18 C ANISOU 2226 CE1 PHE B 40 1712 1081 1452 101 -57 78 C ATOM 2227 CE2 PHE A 40 15.771 -3.845 16.458 1.00 9.85 C ANISOU 2227 CE2 PHE B 40 1241 933 1567 128 225 -304 C ATOM 2228 CZ PHE A 40 15.706 -4.577 17.622 1.00 11.39 C ANISOU 2228 CZ PHE B 40 1488 1109 1731 309 -31 -201 C ATOM 2229 N GLN A 41 15.911 0.273 17.977 1.00 4.50 N ANISOU 2229 N GLN B 41 556 642 509 90 59 145 N ATOM 2230 CA GLN A 41 17.225 0.680 17.482 1.00 4.11 C ANISOU 2230 CA GLN B 41 541 557 463 13 12 113 C ATOM 2231 C GLN A 41 18.152 -0.485 17.830 1.00 3.94 C ANISOU 2231 C GLN B 41 507 514 473 55 6 50 C ATOM 2232 O GLN A 41 18.443 -0.714 19.008 1.00 4.03 O ANISOU 2232 O GLN B 41 476 708 347 14 91 166 O ATOM 2233 CB GLN A 41 17.617 2.000 18.163 1.00 5.34 C ANISOU 2233 CB GLN B 41 655 691 682 37 -43 75 C ATOM 2234 CG GLN A 41 18.546 2.877 17.351 1.00 6.71 C ANISOU 2234 CG GLN B 41 837 752 959 -45 -126 50 C ATOM 2235 CD GLN A 41 20.013 2.468 17.414 1.00 5.73 C ANISOU 2235 CD GLN B 41 644 656 877 -310 -30 -80 C ATOM 2236 OE1 GLN A 41 20.333 1.278 17.607 1.00 5.33 O ANISOU 2236 OE1 GLN B 41 865 717 439 -134 85 152 O ATOM 2237 NE2 GLN A 41 20.913 3.437 17.243 1.00 7.73 N ANISOU 2237 NE2 GLN B 41 1179 981 775 -451 -48 -48 N ATOM 2238 N LYS A 42 18.518 -1.274 16.828 1.00 4.59 N ANISOU 2238 N LYS B 42 683 662 399 81 32 140 N ATOM 2239 CA LYS A 42 19.145 -2.572 17.068 1.00 5.15 C ANISOU 2239 CA LYS B 42 725 747 483 13 63 85 C ATOM 2240 C LYS A 42 20.440 -2.458 17.858 1.00 5.43 C ANISOU 2240 C LYS B 42 755 780 526 51 88 74 C ATOM 2241 O LYS A 42 20.687 -3.231 18.777 1.00 5.29 O ANISOU 2241 O LYS B 42 787 894 328 208 120 58 O ATOM 2242 CB LYS A 42 19.381 -3.254 15.715 1.00 5.31 C ANISOU 2242 CB LYS B 42 869 683 463 8 85 129 C ATOM 2243 CG LYS A 42 20.056 -4.601 15.805 1.00 6.07 C ANISOU 2243 CG LYS B 42 869 821 616 40 86 52 C ATOM 2244 CD LYS A 42 20.160 -5.188 14.398 1.00 6.84 C ANISOU 2244 CD LYS B 42 1133 655 809 26 261 -109 C ATOM 2245 CE LYS A 42 20.877 -6.528 14.368 1.00 8.95 C ANISOU 2245 CE LYS B 42 1466 839 1095 53 179 35 C ATOM 2246 NZ LYS A 42 20.923 -7.131 12.997 1.00 10.80 N ANISOU 2246 NZ LYS B 42 2029 888 1185 -127 639 -104 N ATOM 2247 N GLU A 43 21.264 -1.482 17.506 1.00 6.01 N ANISOU 2247 N GLU B 43 785 923 573 40 50 106 N ATOM 2248 CA GLU A 43 22.553 -1.302 18.168 1.00 7.16 C ANISOU 2248 CA GLU B 43 844 1050 823 14 56 81 C ATOM 2249 C GLU A 43 22.434 -0.923 19.644 1.00 6.28 C ANISOU 2249 C GLU B 43 731 1006 648 60 -34 140 C ATOM 2250 O GLU A 43 23.307 -1.294 20.466 1.00 7.14 O ANISOU 2250 O GLU B 43 831 1260 620 283 -108 248 O ATOM 2251 CB GLU A 43 23.335 -0.207 17.428 1.00 8.95 C ANISOU 2251 CB GLU B 43 1143 1251 1005 4 52 83 C ATOM 2252 CG GLU A 43 24.790 -0.150 17.692 1.00 12.15 C ANISOU 2252 CG GLU B 43 1605 1730 1280 -12 22 156 C ATOM 2253 CD GLU A 43 25.478 0.516 16.532 1.00 10.55 C ANISOU 2253 CD GLU B 43 1024 1858 1124 -140 184 386 C ATOM 2254 OE1 GLU A 43 25.571 1.742 16.602 1.00 15.45 O ANISOU 2254 OE1 GLU B 43 1719 2580 1571 9 73 344 O ATOM 2255 OE2 GLU A 43 25.932 -0.204 15.581 1.00 11.95 O ANISOU 2255 OE2 GLU B 43 931 2455 1152 -188 -236 779 O ATOM 2256 N LYS A 44 21.365 -0.200 19.993 1.00 5.06 N ANISOU 2256 N LYS B 44 563 820 537 34 -86 79 N ATOM 2257 CA LYS A 44 21.111 0.176 21.379 1.00 5.70 C ANISOU 2257 CA LYS B 44 706 876 581 5 -75 2 C ATOM 2258 C LYS A 44 20.425 -0.948 22.160 1.00 5.61 C ANISOU 2258 C LYS B 44 754 846 531 11 -33 18 C ATOM 2259 O LYS A 44 20.566 -1.056 23.367 1.00 7.31 O ANISOU 2259 O LYS B 44 1078 1194 505 -133 -70 -21 O ATOM 2260 CB LYS A 44 20.240 1.425 21.460 1.00 6.46 C ANISOU 2260 CB LYS B 44 924 962 568 58 -30 -49 C ATOM 2261 CG LYS A 44 20.907 2.671 20.959 1.00 7.52 C ANISOU 2261 CG LYS B 44 981 1076 799 55 -74 -48 C ATOM 2262 CD LYS A 44 19.947 3.878 21.033 1.00 9.00 C ANISOU 2262 CD LYS B 44 1143 1079 1197 -71 -215 -200 C ATOM 2263 CE LYS A 44 20.577 5.171 20.539 1.00 11.69 C ANISOU 2263 CE LYS B 44 1180 1512 1749 49 -242 -155 C ATOM 2264 NZ LYS A 44 19.662 6.344 20.697 1.00 13.97 N ANISOU 2264 NZ LYS B 44 1321 1512 2473 -19 -659 -281 N ATOM 2265 N MET A 45 19.689 -1.805 21.469 1.00 4.91 N ANISOU 2265 N MET B 45 587 867 409 19 -39 -8 N ATOM 2266 CA MET A 45 18.890 -2.842 22.127 1.00 5.80 C ANISOU 2266 CA MET B 45 657 963 583 10 62 41 C ATOM 2267 C MET A 45 19.677 -4.095 22.457 1.00 5.36 C ANISOU 2267 C MET B 45 662 862 511 61 44 14 C ATOM 2268 O MET A 45 19.442 -4.713 23.485 1.00 5.40 O ANISOU 2268 O MET B 45 799 926 325 -25 150 -92 O ATOM 2269 CB MET A 45 17.666 -3.199 21.288 1.00 6.50 C ANISOU 2269 CB MET B 45 746 1026 695 -35 43 177 C ATOM 2270 CG MET A 45 16.700 -2.104 21.187 1.00 7.32 C ANISOU 2270 CG MET B 45 722 1411 645 11 91 195 C ATOM 2271 SD MET A 45 15.739 -1.914 22.653 1.00 8.63 S ANISOU 2271 SD MET B 45 1052 1526 699 -4 180 -16 S ATOM 2272 CE MET A 45 14.394 -2.906 22.293 1.00 9.71 C ANISOU 2272 CE MET B 45 871 1645 1172 -124 231 -89 C ATOM 2273 N LEU A 46 20.605 -4.494 21.592 1.00 5.77 N ANISOU 2273 N LEU B 46 737 873 579 69 57 -43 N ATOM 2274 CA LEU A 46 21.405 -5.682 21.861 1.00 6.55 C ANISOU 2274 CA LEU B 46 878 864 744 44 52 -19 C ATOM 2275 C LEU A 46 22.138 -5.621 23.215 1.00 6.77 C ANISOU 2275 C LEU B 46 841 918 813 176 39 -37 C ATOM 2276 O LEU A 46 22.018 -6.552 24.005 1.00 6.94 O ANISOU 2276 O LEU B 46 1206 772 656 316 178 11 O ATOM 2277 CB LEU A 46 22.385 -5.928 20.718 1.00 7.28 C ANISOU 2277 CB LEU B 46 876 999 890 156 85 -14 C ATOM 2278 CG LEU A 46 21.765 -6.441 19.413 1.00 8.28 C ANISOU 2278 CG LEU B 46 958 1101 1085 105 167 -69 C ATOM 2279 CD1 LEU A 46 22.775 -6.476 18.284 1.00 11.18 C ANISOU 2279 CD1 LEU B 46 1420 1635 1193 42 204 -26 C ATOM 2280 CD2 LEU A 46 21.129 -7.805 19.566 1.00 11.73 C ANISOU 2280 CD2 LEU B 46 1495 1650 1312 -210 149 -38 C ATOM 2281 N PRO A 47 22.871 -4.556 23.533 1.00 7.47 N ANISOU 2281 N PRO B 47 938 997 902 95 -50 84 N ATOM 2282 CA PRO A 47 23.537 -4.510 24.848 1.00 8.66 C ANISOU 2282 CA PRO B 47 1140 1148 1001 81 -80 15 C ATOM 2283 C PRO A 47 22.588 -4.439 26.047 1.00 8.21 C ANISOU 2283 C PRO B 47 1020 1101 996 120 -98 10 C ATOM 2284 O PRO A 47 23.066 -4.722 27.145 1.00 8.74 O ANISOU 2284 O PRO B 47 1110 1279 932 220 -166 -87 O ATOM 2285 CB PRO A 47 24.423 -3.264 24.761 1.00 9.07 C ANISOU 2285 CB PRO B 47 1183 1212 1049 51 -41 0 C ATOM 2286 CG PRO A 47 23.899 -2.496 23.646 1.00 9.13 C ANISOU 2286 CG PRO B 47 1189 1118 1161 -8 -145 58 C ATOM 2287 CD PRO A 47 23.261 -3.415 22.692 1.00 8.31 C ANISOU 2287 CD PRO B 47 1068 1036 1054 59 35 -28 C ATOM 2288 N LEU A 48 21.303 -4.111 25.854 1.00 8.15 N ANISOU 2288 N LEU B 48 965 1138 991 114 -90 -3 N ATOM 2289 CA LEU A 48 20.305 -4.206 26.926 1.00 9.49 C ANISOU 2289 CA LEU B 48 1191 1295 1117 119 -25 -25 C ATOM 2290 C LEU A 48 19.703 -5.574 27.107 1.00 10.08 C ANISOU 2290 C LEU B 48 1283 1340 1204 128 79 -22 C ATOM 2291 O LEU A 48 18.904 -5.777 28.018 1.00 11.64 O ANISOU 2291 O LEU B 48 1570 1423 1427 135 329 -63 O ATOM 2292 CB LEU A 48 19.163 -3.227 26.687 1.00 10.08 C ANISOU 2292 CB LEU B 48 1272 1346 1209 124 -2 -62 C ATOM 2293 CG LEU A 48 19.601 -1.777 26.653 1.00 12.25 C ANISOU 2293 CG LEU B 48 1663 1507 1483 175 15 54 C ATOM 2294 CD1 LEU A 48 18.425 -0.933 26.277 1.00 14.42 C ANISOU 2294 CD1 LEU B 48 1939 1780 1760 291 -14 -32 C ATOM 2295 CD2 LEU A 48 20.201 -1.328 27.981 1.00 14.39 C ANISOU 2295 CD2 LEU B 48 1977 1621 1870 149 -24 -89 C ATOM 2296 N GLY A 49 20.059 -6.529 26.254 1.00 9.04 N ANISOU 2296 N GLY B 49 1186 1234 1012 54 82 -63 N ATOM 2297 CA GLY A 49 19.585 -7.893 26.399 1.00 9.67 C ANISOU 2297 CA GLY B 49 1311 1262 1098 32 114 -57 C ATOM 2298 C GLY A 49 18.634 -8.357 25.320 1.00 9.10 C ANISOU 2298 C GLY B 49 1164 1223 1070 -18 143 -50 C ATOM 2299 O GLY A 49 18.203 -9.508 25.352 1.00 9.79 O ANISOU 2299 O GLY B 49 1330 1361 1028 -125 297 -76 O ATOM 2300 N PHE A 50 18.253 -7.483 24.391 1.00 7.62 N ANISOU 2300 N PHE B 50 972 1003 919 -59 108 -80 N ATOM 2301 CA PHE A 50 17.459 -7.952 23.260 1.00 7.90 C ANISOU 2301 CA PHE B 50 1026 1081 892 -72 37 -37 C ATOM 2302 C PHE A 50 18.251 -9.057 22.558 1.00 6.98 C ANISOU 2302 C PHE B 50 925 943 782 -68 34 -19 C ATOM 2303 O PHE A 50 19.421 -8.853 22.249 1.00 7.41 O ANISOU 2303 O PHE B 50 942 1173 700 -8 194 -172 O ATOM 2304 CB PHE A 50 17.152 -6.813 22.288 1.00 7.72 C ANISOU 2304 CB PHE B 50 1033 1071 827 -36 34 3 C ATOM 2305 CG PHE A 50 16.147 -7.188 21.246 1.00 7.04 C ANISOU 2305 CG PHE B 50 909 962 801 -6 -11 -76 C ATOM 2306 CD1 PHE A 50 14.798 -6.939 21.437 1.00 8.43 C ANISOU 2306 CD1 PHE B 50 1045 1195 962 176 -59 -239 C ATOM 2307 CD2 PHE A 50 16.543 -7.839 20.097 1.00 7.88 C ANISOU 2307 CD2 PHE B 50 958 1136 897 51 138 -95 C ATOM 2308 CE1 PHE A 50 13.877 -7.313 20.488 1.00 10.11 C ANISOU 2308 CE1 PHE B 50 1149 1400 1292 133 8 -265 C ATOM 2309 CE2 PHE A 50 15.612 -8.201 19.145 1.00 7.80 C ANISOU 2309 CE2 PHE B 50 1013 961 989 47 85 -10 C ATOM 2310 CZ PHE A 50 14.285 -7.945 19.341 1.00 8.31 C ANISOU 2310 CZ PHE B 50 1055 1109 993 -57 -34 -232 C ATOM 2311 N PRO A 51 17.676 -10.244 22.352 1.00 7.19 N ANISOU 2311 N PRO B 51 884 979 868 -9 78 -41 N ATOM 2312 CA PRO A 51 18.516 -11.386 21.954 1.00 7.04 C ANISOU 2312 CA PRO B 51 820 958 895 -22 12 -35 C ATOM 2313 C PRO A 51 18.982 -11.340 20.508 1.00 7.88 C ANISOU 2313 C PRO B 51 827 1128 1036 -32 24 -100 C ATOM 2314 O PRO A 51 18.193 -11.128 19.592 1.00 7.42 O ANISOU 2314 O PRO B 51 933 1031 852 -43 103 -33 O ATOM 2315 CB PRO A 51 17.605 -12.583 22.213 1.00 7.18 C ANISOU 2315 CB PRO B 51 927 903 897 -65 63 -6 C ATOM 2316 CG PRO A 51 16.240 -12.044 22.039 1.00 8.60 C ANISOU 2316 CG PRO B 51 1029 1234 1002 -131 141 -69 C ATOM 2317 CD PRO A 51 16.278 -10.655 22.554 1.00 7.92 C ANISOU 2317 CD PRO B 51 976 1099 932 -23 148 -75 C ATOM 2318 N GLU A 52 20.284 -11.555 20.319 1.00 9.73 N ANISOU 2318 N GLU B 52 1049 1462 1183 -28 17 -76 N ATOM 2319 CA GLU A 52 20.867 -11.584 18.980 1.00 10.50 C ANISOU 2319 CA GLU B 52 1162 1548 1279 -60 22 -90 C ATOM 2320 C GLU A 52 20.261 -12.712 18.148 1.00 9.77 C ANISOU 2320 C GLU B 52 1095 1389 1226 31 -9 -64 C ATOM 2321 O GLU A 52 20.180 -12.599 16.928 1.00 10.45 O ANISOU 2321 O GLU B 52 1074 1712 1184 44 34 -146 O ATOM 2322 CB GLU A 52 22.387 -11.745 19.080 1.00 12.13 C ANISOU 2322 CB GLU B 52 1361 1809 1438 -85 8 -89 C ATOM 2323 CG GLU A 52 23.133 -11.817 17.750 1.00 15.44 C ANISOU 2323 CG GLU B 52 1827 2200 1838 -112 33 -130 C ATOM 2324 CD GLU A 52 23.078 -10.537 16.930 1.00 18.16 C ANISOU 2324 CD GLU B 52 2178 2553 2166 -296 -150 -92 C ATOM 2325 OE1 GLU A 52 22.250 -10.455 15.996 1.00 22.67 O ANISOU 2325 OE1 GLU B 52 2957 3141 2512 -383 -64 -131 O ATOM 2326 OE2 GLU A 52 23.892 -9.621 17.176 1.00 22.01 O ANISOU 2326 OE2 GLU B 52 3068 2795 2500 -391 -94 -313 O ATOM 2327 N SER A 53 19.800 -13.772 18.810 1.00 9.52 N ANISOU 2327 N SER B 53 1128 1343 1146 41 -71 -62 N ATOM 2328 CA SER A 53 19.122 -14.869 18.138 1.00 9.33 C ANISOU 2328 CA SER B 53 1266 1161 1115 33 -33 -28 C ATOM 2329 C SER A 53 17.903 -14.419 17.334 1.00 8.22 C ANISOU 2329 C SER B 53 1147 1005 970 14 -81 -35 C ATOM 2330 O SER A 53 17.519 -15.087 16.378 1.00 8.42 O ANISOU 2330 O SER B 53 1468 941 789 -22 -132 -95 O ATOM 2331 CB SER A 53 18.713 -15.945 19.160 1.00 9.92 C ANISOU 2331 CB SER B 53 1334 1231 1203 0 -13 -45 C ATOM 2332 OG SER A 53 17.709 -15.478 20.040 1.00 11.80 O ANISOU 2332 OG SER B 53 1821 1515 1147 -17 52 174 O ATOM 2333 N PHE A 54 17.291 -13.291 17.699 1.00 6.68 N ANISOU 2333 N PHE B 54 924 850 765 8 -97 -39 N ATOM 2334 CA PHE A 54 16.139 -12.797 16.948 1.00 6.07 C ANISOU 2334 CA PHE B 54 736 824 743 -44 -55 -53 C ATOM 2335 C PHE A 54 16.508 -12.622 15.476 1.00 5.92 C ANISOU 2335 C PHE B 54 678 811 758 -13 -88 -78 C ATOM 2336 O PHE A 54 15.683 -12.866 14.581 1.00 6.51 O ANISOU 2336 O PHE B 54 731 1027 712 -119 -123 -237 O ATOM 2337 CB PHE A 54 15.690 -11.461 17.531 1.00 5.47 C ANISOU 2337 CB PHE B 54 717 773 586 -74 -44 -17 C ATOM 2338 CG PHE A 54 14.471 -10.873 16.860 1.00 5.32 C ANISOU 2338 CG PHE B 54 772 747 501 -71 34 -111 C ATOM 2339 CD1 PHE A 54 13.208 -11.283 17.226 1.00 5.65 C ANISOU 2339 CD1 PHE B 54 691 793 661 -44 -30 -26 C ATOM 2340 CD2 PHE A 54 14.588 -9.932 15.851 1.00 6.85 C ANISOU 2340 CD2 PHE B 54 795 905 900 -98 -103 -102 C ATOM 2341 CE1 PHE A 54 12.084 -10.737 16.626 1.00 6.24 C ANISOU 2341 CE1 PHE B 54 601 901 866 25 75 -75 C ATOM 2342 CE2 PHE A 54 13.452 -9.385 15.245 1.00 8.04 C ANISOU 2342 CE2 PHE B 54 1067 954 1034 22 -55 157 C ATOM 2343 CZ PHE A 54 12.210 -9.798 15.641 1.00 6.63 C ANISOU 2343 CZ PHE B 54 706 782 1028 192 -271 61 C ATOM 2344 N PHE A 55 17.757 -12.227 15.233 1.00 6.22 N ANISOU 2344 N PHE B 55 832 734 796 -54 -9 -153 N ATOM 2345 CA PHE A 55 18.233 -11.899 13.897 1.00 6.92 C ANISOU 2345 CA PHE B 55 909 837 883 -128 8 -115 C ATOM 2346 C PHE A 55 18.932 -13.041 13.176 1.00 7.04 C ANISOU 2346 C PHE B 55 923 876 875 -53 16 -125 C ATOM 2347 O PHE A 55 19.373 -12.871 12.041 1.00 7.73 O ANISOU 2347 O PHE B 55 1261 914 761 -223 2 -183 O ATOM 2348 CB PHE A 55 19.206 -10.738 14.011 1.00 7.36 C ANISOU 2348 CB PHE B 55 1060 756 979 -158 0 -153 C ATOM 2349 CG PHE A 55 18.586 -9.539 14.632 1.00 7.97 C ANISOU 2349 CG PHE B 55 1168 847 1012 -265 133 -189 C ATOM 2350 CD1 PHE A 55 18.783 -9.256 15.972 1.00 10.25 C ANISOU 2350 CD1 PHE B 55 1515 1039 1338 -354 246 -162 C ATOM 2351 CD2 PHE A 55 17.749 -8.746 13.891 1.00 9.60 C ANISOU 2351 CD2 PHE B 55 1261 961 1424 -111 245 -158 C ATOM 2352 CE1 PHE A 55 18.170 -8.150 16.547 1.00 12.00 C ANISOU 2352 CE1 PHE B 55 1667 1267 1623 -324 333 -294 C ATOM 2353 CE2 PHE A 55 17.128 -7.645 14.460 1.00 11.12 C ANISOU 2353 CE2 PHE B 55 1477 1008 1739 -191 303 -74 C ATOM 2354 CZ PHE A 55 17.350 -7.352 15.788 1.00 11.46 C ANISOU 2354 CZ PHE B 55 1616 1066 1669 -270 361 -114 C ATOM 2355 N ALA A 56 19.046 -14.197 13.819 1.00 6.74 N ANISOU 2355 N ALA B 56 915 858 789 49 63 -153 N ATOM 2356 CA ALA A 56 19.909 -15.272 13.323 1.00 7.11 C ANISOU 2356 CA ALA B 56 964 887 850 96 8 -98 C ATOM 2357 C ALA A 56 19.589 -15.688 11.883 1.00 7.00 C ANISOU 2357 C ALA B 56 900 919 841 131 -57 -100 C ATOM 2358 O ALA A 56 20.498 -15.932 11.087 1.00 8.89 O ANISOU 2358 O ALA B 56 1088 1473 814 -33 -12 -158 O ATOM 2359 CB ALA A 56 19.810 -16.470 14.252 1.00 8.11 C ANISOU 2359 CB ALA B 56 1183 1059 840 96 -1 -90 C ATOM 2360 N GLU A 57 18.312 -15.800 11.547 1.00 6.31 N ANISOU 2360 N GLU B 57 761 824 813 144 -47 -80 N ATOM 2361 CA GLU A 57 17.917 -16.321 10.227 1.00 6.49 C ANISOU 2361 CA GLU B 57 817 785 864 139 -44 -44 C ATOM 2362 C GLU A 57 17.716 -15.225 9.173 1.00 7.08 C ANISOU 2362 C GLU B 57 803 979 907 95 -68 34 C ATOM 2363 O GLU A 57 17.390 -15.537 8.033 1.00 7.45 O ANISOU 2363 O GLU B 57 901 1001 926 83 -75 31 O ATOM 2364 CB GLU A 57 16.647 -17.156 10.341 1.00 7.06 C ANISOU 2364 CB GLU B 57 934 858 888 111 -114 -13 C ATOM 2365 CG GLU A 57 16.804 -18.389 11.207 1.00 7.80 C ANISOU 2365 CG GLU B 57 1055 843 1064 133 -49 -69 C ATOM 2366 CD GLU A 57 15.602 -19.307 11.134 1.00 11.39 C ANISOU 2366 CD GLU B 57 1590 1143 1594 245 -90 -18 C ATOM 2367 OE1 GLU A 57 14.469 -18.804 11.186 1.00 12.58 O ANISOU 2367 OE1 GLU B 57 1543 1483 1752 257 -21 122 O ATOM 2368 OE2 GLU A 57 15.793 -20.534 11.024 1.00 14.33 O ANISOU 2368 OE2 GLU B 57 2112 1230 2103 191 16 -47 O ATOM 2369 N GLY A 58 17.876 -13.964 9.564 1.00 7.43 N ANISOU 2369 N GLY B 58 901 977 943 56 -23 62 N ATOM 2370 CA GLY A 58 17.754 -12.825 8.651 1.00 7.60 C ANISOU 2370 CA GLY B 58 920 987 978 59 -33 123 C ATOM 2371 C GLY A 58 16.344 -12.548 8.159 1.00 7.88 C ANISOU 2371 C GLY B 58 936 1058 999 104 -23 204 C ATOM 2372 O GLY A 58 16.145 -11.997 7.078 1.00 9.76 O ANISOU 2372 O GLY B 58 1134 1409 1162 60 -95 552 O ATOM 2373 N LYS A 59 15.351 -12.950 8.939 1.00 6.28 N ANISOU 2373 N LYS B 59 718 825 842 174 -23 174 N ATOM 2374 CA LYS A 59 13.958 -12.794 8.542 1.00 6.21 C ANISOU 2374 CA LYS B 59 722 830 806 207 -25 68 C ATOM 2375 C LYS A 59 13.343 -11.612 9.265 1.00 6.16 C ANISOU 2375 C LYS B 59 793 800 744 211 -77 -8 C ATOM 2376 O LYS A 59 13.636 -11.367 10.440 1.00 6.83 O ANISOU 2376 O LYS B 59 945 952 697 460 -137 -47 O ATOM 2377 CB LYS A 59 13.190 -14.053 8.889 1.00 6.41 C ANISOU 2377 CB LYS B 59 750 819 865 254 26 64 C ATOM 2378 CG LYS A 59 13.661 -15.278 8.113 1.00 6.14 C ANISOU 2378 CG LYS B 59 763 698 872 131 39 -12 C ATOM 2379 CD LYS A 59 12.927 -16.508 8.590 1.00 7.62 C ANISOU 2379 CD LYS B 59 1038 821 1035 75 137 49 C ATOM 2380 CE LYS A 59 13.418 -17.769 7.924 1.00 7.39 C ANISOU 2380 CE LYS B 59 1084 671 1050 133 188 -183 C ATOM 2381 NZ LYS A 59 12.876 -18.984 8.616 1.00 8.92 N ANISOU 2381 NZ LYS B 59 1134 1167 1089 -138 372 104 N ATOM 2382 N LEU A 60 12.463 -10.881 8.580 1.00 5.54 N ANISOU 2382 N LEU B 60 672 737 693 170 -128 -44 N ATOM 2383 CA LEU A 60 11.846 -9.714 9.171 1.00 5.66 C ANISOU 2383 CA LEU B 60 693 725 731 72 -70 -35 C ATOM 2384 C LEU A 60 10.475 -9.454 8.575 1.00 4.66 C ANISOU 2384 C LEU B 60 606 532 632 63 -75 -37 C ATOM 2385 O LEU A 60 10.303 -9.425 7.368 1.00 3.68 O ANISOU 2385 O LEU B 60 520 350 528 124 2 44 O ATOM 2386 CB LEU A 60 12.747 -8.480 8.964 1.00 6.58 C ANISOU 2386 CB LEU B 60 776 803 921 64 -76 7 C ATOM 2387 CG LEU A 60 12.286 -7.182 9.634 1.00 9.58 C ANISOU 2387 CG LEU B 60 1139 1129 1372 -74 35 -99 C ATOM 2388 CD1 LEU A 60 12.347 -7.297 11.131 1.00 11.46 C ANISOU 2388 CD1 LEU B 60 1525 1275 1552 -180 20 -270 C ATOM 2389 CD2 LEU A 60 13.119 -6.010 9.155 1.00 11.85 C ANISOU 2389 CD2 LEU B 60 1505 1249 1748 -149 -25 -92 C ATOM 2390 N GLN A 61 9.527 -9.197 9.457 1.00 4.74 N ANISOU 2390 N GLN B 61 579 632 589 117 -114 53 N ATOM 2391 CA GLN A 61 8.172 -8.806 9.088 1.00 4.70 C ANISOU 2391 CA GLN B 61 614 597 575 113 -65 87 C ATOM 2392 C GLN A 61 7.635 -7.858 10.146 1.00 4.68 C ANISOU 2392 C GLN B 61 608 654 516 140 -62 105 C ATOM 2393 O GLN A 61 7.894 -8.040 11.320 1.00 5.91 O ANISOU 2393 O GLN B 61 864 808 570 271 -161 100 O ATOM 2394 CB GLN A 61 7.290 -10.061 8.934 1.00 5.07 C ANISOU 2394 CB GLN B 61 662 665 599 90 -3 99 C ATOM 2395 CG GLN A 61 5.812 -9.790 8.664 1.00 5.63 C ANISOU 2395 CG GLN B 61 621 778 739 95 64 182 C ATOM 2396 CD GLN A 61 5.002 -11.054 8.465 1.00 5.93 C ANISOU 2396 CD GLN B 61 568 673 1009 218 -91 84 C ATOM 2397 OE1 GLN A 61 5.606 -12.091 8.125 1.00 6.59 O ANISOU 2397 OE1 GLN B 61 812 646 1044 184 30 413 O ATOM 2398 NE2 GLN A 61 3.748 -11.015 8.624 1.00 9.33 N ANISOU 2398 NE2 GLN B 61 949 1108 1485 -1 -14 3 N ATOM 2399 N ASN A 62 6.922 -6.825 9.696 1.00 4.41 N ANISOU 2399 N ASN B 62 663 477 533 171 -43 65 N ATOM 2400 CA ASN A 62 6.255 -5.869 10.577 1.00 4.64 C ANISOU 2400 CA ASN B 62 610 587 563 109 30 64 C ATOM 2401 C ASN A 62 4.761 -5.937 10.303 1.00 4.79 C ANISOU 2401 C ASN B 62 597 612 609 31 0 81 C ATOM 2402 O ASN A 62 4.329 -5.680 9.185 1.00 4.92 O ANISOU 2402 O ASN B 62 542 686 639 171 -26 183 O ATOM 2403 CB ASN A 62 6.804 -4.445 10.303 1.00 5.83 C ANISOU 2403 CB ASN B 62 753 681 779 53 72 61 C ATOM 2404 CG ASN A 62 6.045 -3.314 10.998 1.00 6.27 C ANISOU 2404 CG ASN B 62 907 684 790 0 43 81 C ATOM 2405 OD1 ASN A 62 5.957 -2.220 10.427 1.00 7.27 O ANISOU 2405 OD1 ASN B 62 1185 631 944 147 37 64 O ATOM 2406 ND2 ASN A 62 5.561 -3.533 12.218 1.00 6.55 N ANISOU 2406 ND2 ASN B 62 903 806 780 -62 -14 14 N ATOM 2407 N ASN A 63 3.993 -6.308 11.319 1.00 4.74 N ANISOU 2407 N ASN B 63 521 663 616 147 -4 128 N ATOM 2408 CA ASN A 63 2.537 -6.306 11.255 1.00 4.67 C ANISOU 2408 CA ASN B 63 561 604 608 84 -7 67 C ATOM 2409 C ASN A 63 1.989 -5.147 12.076 1.00 4.75 C ANISOU 2409 C ASN B 63 592 633 578 69 39 27 C ATOM 2410 O ASN A 63 2.567 -4.745 13.093 1.00 5.00 O ANISOU 2410 O ASN B 63 546 755 597 106 39 -3 O ATOM 2411 CB ASN A 63 1.958 -7.594 11.828 1.00 5.72 C ANISOU 2411 CB ASN B 63 613 700 860 147 116 45 C ATOM 2412 CG ASN A 63 2.270 -8.843 11.004 1.00 7.40 C ANISOU 2412 CG ASN B 63 1005 669 1137 155 139 133 C ATOM 2413 OD1 ASN A 63 2.081 -9.970 11.495 1.00 13.96 O ANISOU 2413 OD1 ASN B 63 2448 1108 1745 153 403 342 O ATOM 2414 ND2 ASN A 63 2.673 -8.679 9.808 1.00 4.76 N ANISOU 2414 ND2 ASN B 63 616 368 823 156 -84 -134 N ATOM 2415 N VAL A 64 0.855 -4.613 11.641 1.00 4.28 N ANISOU 2415 N VAL B 64 583 532 510 95 20 -17 N ATOM 2416 CA VAL A 64 0.133 -3.584 12.375 1.00 4.68 C ANISOU 2416 CA VAL B 64 625 632 520 17 34 0 C ATOM 2417 C VAL A 64 -1.327 -3.971 12.425 1.00 4.94 C ANISOU 2417 C VAL B 64 590 663 623 77 -47 -50 C ATOM 2418 O VAL A 64 -1.942 -4.318 11.419 1.00 5.06 O ANISOU 2418 O VAL B 64 527 729 666 8 26 -250 O ATOM 2419 CB VAL A 64 0.280 -2.201 11.691 1.00 5.32 C ANISOU 2419 CB VAL B 64 766 526 728 43 18 81 C ATOM 2420 CG1 VAL A 64 -0.493 -1.132 12.421 1.00 7.31 C ANISOU 2420 CG1 VAL B 64 954 720 1100 100 -25 -63 C ATOM 2421 CG2 VAL A 64 1.765 -1.780 11.589 1.00 6.61 C ANISOU 2421 CG2 VAL B 64 775 855 881 -112 14 35 C ATOM 2422 N SER A 65 -1.899 -3.880 13.618 1.00 4.37 N ANISOU 2422 N SER B 65 376 668 615 28 48 -120 N ATOM 2423 CA SER A 65 -3.341 -3.926 13.757 1.00 5.54 C ANISOU 2423 CA SER B 65 592 730 782 -48 27 -159 C ATOM 2424 C SER A 65 -3.840 -2.624 14.356 1.00 4.87 C ANISOU 2424 C SER B 65 596 699 552 -40 89 -232 C ATOM 2425 O SER A 65 -3.225 -2.092 15.282 1.00 7.22 O ANISOU 2425 O SER B 65 740 1174 828 86 -87 -419 O ATOM 2426 CB SER A 65 -3.772 -5.106 14.561 1.00 7.57 C ANISOU 2426 CB SER B 65 692 1121 1060 -134 177 -100 C ATOM 2427 OG SER A 65 -3.301 -4.999 15.838 1.00 9.76 O ANISOU 2427 OG SER B 65 1121 1243 1344 -209 275 105 O ATOM 2428 N PHE A 66 -4.911 -2.099 13.796 1.00 4.79 N ANISOU 2428 N PHE B 66 605 654 558 -83 60 -57 N ATOM 2429 CA PHE A 66 -5.548 -0.868 14.249 1.00 4.89 C ANISOU 2429 CA PHE B 66 651 690 515 -43 56 -69 C ATOM 2430 C PHE A 66 -6.895 -1.293 14.782 1.00 5.39 C ANISOU 2430 C PHE B 66 658 729 659 -62 2 -108 C ATOM 2431 O PHE A 66 -7.722 -1.807 14.053 1.00 5.94 O ANISOU 2431 O PHE B 66 507 1105 644 -97 31 -341 O ATOM 2432 CB PHE A 66 -5.670 0.131 13.073 1.00 5.91 C ANISOU 2432 CB PHE B 66 779 765 702 37 38 4 C ATOM 2433 CG PHE A 66 -6.163 1.485 13.502 1.00 7.18 C ANISOU 2433 CG PHE B 66 1030 893 803 98 65 84 C ATOM 2434 CD1 PHE A 66 -5.407 2.276 14.354 1.00 7.87 C ANISOU 2434 CD1 PHE B 66 1336 671 981 -5 302 148 C ATOM 2435 CD2 PHE A 66 -7.402 1.953 13.085 1.00 10.88 C ANISOU 2435 CD2 PHE B 66 1682 1272 1177 416 -132 -206 C ATOM 2436 CE1 PHE A 66 -5.858 3.513 14.762 1.00 9.52 C ANISOU 2436 CE1 PHE B 66 1428 987 1199 -50 194 75 C ATOM 2437 CE2 PHE A 66 -7.866 3.205 13.508 1.00 12.07 C ANISOU 2437 CE2 PHE B 66 1739 1089 1755 550 -111 -53 C ATOM 2438 CZ PHE A 66 -7.086 3.972 14.337 1.00 11.65 C ANISOU 2438 CZ PHE B 66 1728 1024 1671 355 74 -125 C ATOM 2439 N SER A 67 -7.086 -1.117 16.079 1.00 4.36 N ANISOU 2439 N SER B 67 559 579 518 -171 68 -58 N ATOM 2440 CA SER A 67 -8.211 -1.742 16.786 1.00 5.09 C ANISOU 2440 CA SER B 67 641 648 643 -151 89 -41 C ATOM 2441 C SER A 67 -8.880 -0.747 17.729 1.00 4.37 C ANISOU 2441 C SER B 67 610 538 510 -102 64 22 C ATOM 2442 O SER A 67 -8.241 0.168 18.245 1.00 5.05 O ANISOU 2442 O SER B 67 698 563 655 -169 157 -18 O ATOM 2443 CB SER A 67 -7.740 -2.946 17.619 1.00 6.24 C ANISOU 2443 CB SER B 67 826 711 834 -198 296 -48 C ATOM 2444 OG SER A 67 -7.146 -3.945 16.803 1.00 8.05 O ANISOU 2444 OG SER B 67 1089 735 1233 -72 304 -71 O ATOM 2445 N ARG A 68 -10.159 -0.965 18.007 1.00 3.23 N ANISOU 2445 N ARG B 68 430 429 368 -85 142 -84 N ATOM 2446 CA ARG A 68 -10.945 -0.049 18.817 1.00 3.66 C ANISOU 2446 CA ARG B 68 479 362 548 -35 94 -32 C ATOM 2447 C ARG A 68 -11.117 -0.527 20.247 1.00 3.80 C ANISOU 2447 C ARG B 68 483 441 520 -22 43 -65 C ATOM 2448 O ARG A 68 -10.913 -1.703 20.559 1.00 3.55 O ANISOU 2448 O ARG B 68 399 570 379 85 56 -133 O ATOM 2449 CB ARG A 68 -12.283 0.197 18.161 1.00 3.99 C ANISOU 2449 CB ARG B 68 583 411 519 -33 87 -13 C ATOM 2450 CG ARG A 68 -13.269 -0.943 18.212 1.00 4.11 C ANISOU 2450 CG ARG B 68 626 281 655 63 4 -82 C ATOM 2451 CD ARG A 68 -14.492 -0.590 17.456 1.00 4.49 C ANISOU 2451 CD ARG B 68 680 334 690 -87 161 68 C ATOM 2452 NE ARG A 68 -15.444 -1.679 17.411 1.00 5.40 N ANISOU 2452 NE ARG B 68 568 527 954 -60 -81 2 N ATOM 2453 CZ ARG A 68 -16.622 -1.578 16.850 1.00 5.27 C ANISOU 2453 CZ ARG B 68 493 721 787 28 20 202 C ATOM 2454 NH1 ARG A 68 -16.976 -0.437 16.276 1.00 5.62 N ANISOU 2454 NH1 ARG B 68 785 605 744 -71 -97 190 N ATOM 2455 NH2 ARG A 68 -17.446 -2.616 16.840 1.00 7.82 N ANISOU 2455 NH2 ARG B 68 994 863 1113 -34 -185 356 N ATOM 2456 N LYS A 69 -11.529 0.412 21.107 1.00 3.48 N ANISOU 2456 N LYS B 69 460 413 447 -43 77 -11 N ATOM 2457 CA LYS A 69 -11.726 0.165 22.525 1.00 3.44 C ANISOU 2457 CA LYS B 69 467 394 446 -41 73 -51 C ATOM 2458 C LYS A 69 -12.537 -1.089 22.734 1.00 3.58 C ANISOU 2458 C LYS B 69 507 402 448 -71 93 -136 C ATOM 2459 O LYS A 69 -13.548 -1.300 22.069 1.00 3.08 O ANISOU 2459 O LYS B 69 441 345 382 -82 46 -101 O ATOM 2460 CB LYS A 69 -12.478 1.329 23.192 1.00 3.75 C ANISOU 2460 CB LYS B 69 450 497 475 -16 160 -123 C ATOM 2461 CG LYS A 69 -12.390 1.295 24.712 1.00 5.74 C ANISOU 2461 CG LYS B 69 856 632 691 57 183 -122 C ATOM 2462 CD LYS A 69 -13.039 2.525 25.344 1.00 7.56 C ANISOU 2462 CD LYS B 69 1072 1144 655 135 298 -213 C ATOM 2463 CE LYS A 69 -12.928 2.538 26.854 1.00 12.53 C ANISOU 2463 CE LYS B 69 1765 1563 1434 125 106 -122 C ATOM 2464 NZ LYS A 69 -13.320 3.862 27.391 1.00 16.96 N ANISOU 2464 NZ LYS B 69 2390 1679 2374 215 8 24 N ATOM 2465 N ASN A 70 -12.067 -1.902 23.677 1.00 2.98 N ANISOU 2465 N ASN B 70 325 377 427 -49 -50 -77 N ATOM 2466 CA ASN A 70 -12.737 -3.111 24.161 1.00 3.16 C ANISOU 2466 CA ASN B 70 391 385 421 -80 51 -36 C ATOM 2467 C ASN A 70 -12.539 -4.332 23.296 1.00 3.40 C ANISOU 2467 C ASN B 70 416 385 490 -31 44 -17 C ATOM 2468 O ASN A 70 -12.916 -5.407 23.691 1.00 4.74 O ANISOU 2468 O ASN B 70 736 326 736 -126 230 -183 O ATOM 2469 CB ASN A 70 -14.231 -2.891 24.473 1.00 4.13 C ANISOU 2469 CB ASN B 70 495 492 581 -61 29 -63 C ATOM 2470 CG ASN A 70 -14.437 -1.991 25.654 1.00 6.19 C ANISOU 2470 CG ASN B 70 561 773 1016 35 -2 -143 C ATOM 2471 OD1 ASN A 70 -13.777 -2.154 26.672 1.00 8.42 O ANISOU 2471 OD1 ASN B 70 1245 910 1043 -6 41 -190 O ATOM 2472 ND2 ASN A 70 -15.340 -1.026 25.528 1.00 10.93 N ANISOU 2472 ND2 ASN B 70 1209 1017 1924 308 -98 -282 N ATOM 2473 N VAL A 71 -11.912 -4.171 22.144 1.00 3.76 N ANISOU 2473 N VAL B 71 520 413 494 33 -3 -35 N ATOM 2474 CA VAL A 71 -11.421 -5.327 21.414 1.00 3.56 C ANISOU 2474 CA VAL B 71 450 449 453 -21 14 10 C ATOM 2475 C VAL A 71 -10.458 -6.100 22.297 1.00 3.63 C ANISOU 2475 C VAL B 71 415 504 460 -103 -26 -1 C ATOM 2476 O VAL A 71 -9.583 -5.509 22.937 1.00 3.47 O ANISOU 2476 O VAL B 71 333 486 499 -124 4 -105 O ATOM 2477 CB VAL A 71 -10.745 -4.913 20.101 1.00 3.98 C ANISOU 2477 CB VAL B 71 534 520 458 32 36 76 C ATOM 2478 CG1 VAL A 71 -9.883 -6.038 19.525 1.00 5.24 C ANISOU 2478 CG1 VAL B 71 728 781 479 -9 216 95 C ATOM 2479 CG2 VAL A 71 -11.808 -4.461 19.085 1.00 4.68 C ANISOU 2479 CG2 VAL B 71 683 464 628 -72 -83 -7 C ATOM 2480 N LEU A 72 -10.609 -7.416 22.293 1.00 3.50 N ANISOU 2480 N LEU B 72 467 526 335 37 -97 -49 N ATOM 2481 CA LEU A 72 -9.793 -8.293 23.111 1.00 3.41 C ANISOU 2481 CA LEU B 72 446 431 416 -23 1 -39 C ATOM 2482 C LEU A 72 -9.422 -9.453 22.216 1.00 4.02 C ANISOU 2482 C LEU B 72 499 542 485 55 8 -64 C ATOM 2483 O LEU A 72 -10.297 -10.181 21.744 1.00 3.71 O ANISOU 2483 O LEU B 72 435 571 401 112 -24 -205 O ATOM 2484 CB LEU A 72 -10.600 -8.764 24.327 1.00 3.28 C ANISOU 2484 CB LEU B 72 537 431 276 2 4 -54 C ATOM 2485 CG LEU A 72 -9.805 -9.492 25.417 1.00 5.23 C ANISOU 2485 CG LEU B 72 717 640 628 40 -11 -3 C ATOM 2486 CD1 LEU A 72 -10.648 -9.589 26.670 1.00 6.90 C ANISOU 2486 CD1 LEU B 72 1162 811 645 122 -45 -172 C ATOM 2487 CD2 LEU A 72 -9.369 -10.885 24.989 1.00 5.29 C ANISOU 2487 CD2 LEU B 72 767 855 386 154 -1 72 C ATOM 2488 N ARG A 73 -8.125 -9.586 21.978 1.00 3.81 N ANISOU 2488 N ARG B 73 509 579 359 52 -22 -174 N ATOM 2489 CA ARG A 73 -7.558 -10.589 21.084 1.00 4.38 C ANISOU 2489 CA ARG B 73 544 580 540 103 -34 -102 C ATOM 2490 C ARG A 73 -6.578 -11.466 21.831 1.00 4.27 C ANISOU 2490 C ARG B 73 436 672 513 62 14 -62 C ATOM 2491 O ARG A 73 -5.784 -10.962 22.609 1.00 4.94 O ANISOU 2491 O ARG B 73 568 653 657 102 -159 -229 O ATOM 2492 CB ARG A 73 -6.776 -9.902 19.958 1.00 5.85 C ANISOU 2492 CB ARG B 73 805 727 689 180 20 -46 C ATOM 2493 CG ARG A 73 -7.496 -8.877 19.113 1.00 10.47 C ANISOU 2493 CG ARG B 73 1400 1436 1141 167 83 -85 C ATOM 2494 CD ARG A 73 -8.230 -9.492 17.973 1.00 14.73 C ANISOU 2494 CD ARG B 73 2015 1649 1932 165 -305 -52 C ATOM 2495 NE ARG A 73 -8.973 -8.490 17.192 1.00 12.56 N ANISOU 2495 NE ARG B 73 1748 1450 1573 268 -334 210 N ATOM 2496 CZ ARG A 73 -10.287 -8.504 17.005 1.00 14.69 C ANISOU 2496 CZ ARG B 73 2041 1717 1824 45 -207 61 C ATOM 2497 NH1 ARG A 73 -11.048 -9.472 17.528 1.00 15.78 N ANISOU 2497 NH1 ARG B 73 2187 2142 1665 -111 -238 258 N ATOM 2498 NH2 ARG A 73 -10.845 -7.537 16.265 1.00 14.14 N ANISOU 2498 NH2 ARG B 73 1884 1833 1654 243 -429 199 N ATOM 2499 N GLY A 74 -6.597 -12.753 21.544 1.00 3.41 N ANISOU 2499 N GLY B 74 365 634 294 25 2 -74 N ATOM 2500 CA GLY A 74 -5.657 -13.689 22.125 1.00 3.81 C ANISOU 2500 CA GLY B 74 421 606 420 10 -25 -45 C ATOM 2501 C GLY A 74 -6.326 -14.968 22.565 1.00 4.27 C ANISOU 2501 C GLY B 74 527 686 408 -14 47 3 C ATOM 2502 O GLY A 74 -7.527 -15.158 22.321 1.00 4.84 O ANISOU 2502 O GLY B 74 664 914 260 -18 9 -51 O ATOM 2503 N LEU A 75 -5.591 -15.872 23.218 1.00 4.07 N ANISOU 2503 N LEU B 75 498 673 374 -14 -42 19 N ATOM 2504 CA LEU A 75 -4.166 -15.738 23.528 1.00 4.23 C ANISOU 2504 CA LEU B 75 543 631 433 -28 25 139 C ATOM 2505 C LEU A 75 -3.457 -16.685 22.570 1.00 3.92 C ANISOU 2505 C LEU B 75 500 520 467 -6 39 97 C ATOM 2506 O LEU A 75 -3.754 -17.875 22.534 1.00 4.70 O ANISOU 2506 O LEU B 75 601 704 479 50 87 55 O ATOM 2507 CB LEU A 75 -3.901 -16.120 24.997 1.00 4.43 C ANISOU 2507 CB LEU B 75 578 708 397 -29 -22 92 C ATOM 2508 CG LEU A 75 -4.512 -15.101 25.962 1.00 5.36 C ANISOU 2508 CG LEU B 75 804 809 422 61 -10 78 C ATOM 2509 CD1 LEU A 75 -4.749 -15.727 27.316 1.00 5.59 C ANISOU 2509 CD1 LEU B 75 720 1017 387 -32 171 31 C ATOM 2510 CD2 LEU A 75 -3.597 -13.931 26.123 1.00 5.75 C ANISOU 2510 CD2 LEU B 75 990 881 313 151 76 -104 C ATOM 2511 N HIS A 76 -2.531 -16.145 21.765 1.00 4.30 N ANISOU 2511 N HIS B 76 543 578 510 -17 -8 130 N ATOM 2512 CA HIS A 76 -1.933 -16.903 20.672 1.00 4.69 C ANISOU 2512 CA HIS B 76 582 620 580 -18 67 130 C ATOM 2513 C HIS A 76 -0.429 -17.012 20.819 1.00 5.10 C ANISOU 2513 C HIS B 76 585 696 656 66 69 127 C ATOM 2514 O HIS A 76 0.239 -15.997 20.931 1.00 4.91 O ANISOU 2514 O HIS B 76 597 459 807 62 146 88 O ATOM 2515 CB HIS A 76 -2.204 -16.216 19.320 1.00 5.85 C ANISOU 2515 CB HIS B 76 730 861 632 48 33 173 C ATOM 2516 CG HIS A 76 -3.620 -15.759 19.130 1.00 7.76 C ANISOU 2516 CG HIS B 76 1072 1180 695 115 -7 360 C ATOM 2517 ND1 HIS A 76 -3.920 -14.614 18.435 1.00 14.55 N ANISOU 2517 ND1 HIS B 76 1675 1927 1925 145 -31 610 N ATOM 2518 CD2 HIS A 76 -4.805 -16.256 19.554 1.00 9.73 C ANISOU 2518 CD2 HIS B 76 1114 1516 1064 423 -177 315 C ATOM 2519 CE1 HIS A 76 -5.228 -14.435 18.419 1.00 13.81 C ANISOU 2519 CE1 HIS B 76 1477 1928 1839 390 -77 468 C ATOM 2520 NE2 HIS A 76 -5.791 -15.425 19.082 1.00 11.41 N ANISOU 2520 NE2 HIS B 76 1307 1829 1196 318 35 395 N ATOM 2521 N ALA A 77 0.103 -18.226 20.810 1.00 4.45 N ANISOU 2521 N ALA B 77 489 551 650 -87 125 72 N ATOM 2522 CA ALA A 77 1.537 -18.489 20.733 1.00 5.49 C ANISOU 2522 CA ALA B 77 658 695 732 -49 45 39 C ATOM 2523 C ALA A 77 1.845 -18.898 19.296 1.00 6.26 C ANISOU 2523 C ALA B 77 794 758 828 -163 91 -20 C ATOM 2524 O ALA A 77 1.240 -19.809 18.736 1.00 8.46 O ANISOU 2524 O ALA B 77 1239 984 990 -123 221 -178 O ATOM 2525 CB ALA A 77 1.929 -19.594 21.700 1.00 5.50 C ANISOU 2525 CB ALA B 77 663 678 745 -16 91 38 C ATOM 2526 N GLU A 78 2.776 -18.199 18.672 1.00 8.18 N ANISOU 2526 N GLU B 78 1121 1052 935 -186 96 -34 N ATOM 2527 CA GLU A 78 3.021 -18.379 17.244 1.00 8.13 C ANISOU 2527 CA GLU B 78 1201 983 902 -173 59 -19 C ATOM 2528 C GLU A 78 4.452 -18.849 17.016 1.00 8.40 C ANISOU 2528 C GLU B 78 1179 1044 967 -230 27 -10 C ATOM 2529 O GLU A 78 5.262 -18.848 17.961 1.00 9.45 O ANISOU 2529 O GLU B 78 1304 1399 884 -445 0 87 O ATOM 2530 CB GLU A 78 2.702 -17.070 16.506 1.00 8.64 C ANISOU 2530 CB GLU B 78 1301 1049 931 -118 122 0 C ATOM 2531 CG GLU A 78 1.222 -16.744 16.543 1.00 9.12 C ANISOU 2531 CG GLU B 78 1462 1085 917 -110 56 -6 C ATOM 2532 CD GLU A 78 0.833 -15.583 15.665 1.00 11.67 C ANISOU 2532 CD GLU B 78 1871 1331 1232 66 103 -183 C ATOM 2533 OE1 GLU A 78 1.548 -14.572 15.631 1.00 11.37 O ANISOU 2533 OE1 GLU B 78 2030 1479 810 17 219 -445 O ATOM 2534 OE2 GLU A 78 -0.201 -15.687 14.988 1.00 13.83 O ANISOU 2534 OE2 GLU B 78 1516 1615 2121 -203 21 -13 O ATOM 2535 N PRO A 79 4.786 -19.286 15.801 1.00 8.30 N ANISOU 2535 N PRO B 79 1182 912 1059 -245 -26 -92 N ATOM 2536 CA PRO A 79 6.115 -19.873 15.547 1.00 8.74 C ANISOU 2536 CA PRO B 79 1149 1034 1135 -173 26 -114 C ATOM 2537 C PRO A 79 7.331 -18.978 15.592 1.00 9.01 C ANISOU 2537 C PRO B 79 1159 1001 1260 -138 68 -120 C ATOM 2538 O PRO A 79 8.465 -19.445 15.367 1.00 10.32 O ANISOU 2538 O PRO B 79 1327 1268 1325 -248 329 -226 O ATOM 2539 CB PRO A 79 5.989 -20.455 14.124 1.00 9.19 C ANISOU 2539 CB PRO B 79 1234 1137 1118 -118 19 -161 C ATOM 2540 CG PRO A 79 4.540 -20.553 13.888 1.00 8.69 C ANISOU 2540 CG PRO B 79 1109 1050 1141 -182 3 -183 C ATOM 2541 CD PRO A 79 3.901 -19.411 14.624 1.00 8.68 C ANISOU 2541 CD PRO B 79 1246 981 1069 -59 -17 -143 C ATOM 2542 N TRP A 80 7.130 -17.727 15.976 1.00 8.72 N ANISOU 2542 N TRP B 80 1052 1033 1224 -159 158 -177 N ATOM 2543 CA TRP A 80 8.149 -16.722 15.814 1.00 8.34 C ANISOU 2543 CA TRP B 80 1036 1014 1119 -143 86 -85 C ATOM 2544 C TRP A 80 8.190 -15.869 17.045 1.00 7.09 C ANISOU 2544 C TRP B 80 909 782 1000 -171 105 -72 C ATOM 2545 O TRP A 80 7.219 -15.787 17.793 1.00 7.90 O ANISOU 2545 O TRP B 80 1004 866 1131 -314 185 -235 O ATOM 2546 CB TRP A 80 7.886 -15.891 14.574 1.00 8.33 C ANISOU 2546 CB TRP B 80 1070 997 1097 -281 86 -207 C ATOM 2547 CG TRP A 80 6.442 -15.573 14.317 1.00 8.79 C ANISOU 2547 CG TRP B 80 1174 1080 1084 -344 121 -106 C ATOM 2548 CD1 TRP A 80 5.673 -14.681 14.980 1.00 8.72 C ANISOU 2548 CD1 TRP B 80 1449 802 1062 -467 18 -40 C ATOM 2549 CD2 TRP A 80 5.592 -16.209 13.354 1.00 8.44 C ANISOU 2549 CD2 TRP B 80 1050 1015 1141 -376 61 -120 C ATOM 2550 NE1 TRP A 80 4.392 -14.700 14.482 1.00 8.94 N ANISOU 2550 NE1 TRP B 80 1444 886 1067 -144 241 -33 N ATOM 2551 CE2 TRP A 80 4.323 -15.629 13.472 1.00 8.04 C ANISOU 2551 CE2 TRP B 80 1253 790 1010 -271 146 -11 C ATOM 2552 CE3 TRP A 80 5.796 -17.193 12.374 1.00 9.84 C ANISOU 2552 CE3 TRP B 80 1117 1324 1296 -301 16 -201 C ATOM 2553 CZ2 TRP A 80 3.251 -16.002 12.661 1.00 8.72 C ANISOU 2553 CZ2 TRP B 80 1225 982 1105 -170 108 73 C ATOM 2554 CZ3 TRP A 80 4.720 -17.587 11.578 1.00 9.33 C ANISOU 2554 CZ3 TRP B 80 964 1462 1117 -294 38 -157 C ATOM 2555 CH2 TRP A 80 3.476 -16.976 11.716 1.00 9.50 C ANISOU 2555 CH2 TRP B 80 1067 1244 1298 -284 91 -31 C ATOM 2556 N ASP A 81 9.345 -15.240 17.251 1.00 6.22 N ANISOU 2556 N ASP B 81 781 698 883 -68 -51 -35 N ATOM 2557 CA ASP A 81 9.522 -14.254 18.307 1.00 6.05 C ANISOU 2557 CA ASP B 81 803 742 754 -2 -41 27 C ATOM 2558 C ASP A 81 8.857 -12.945 17.875 1.00 5.90 C ANISOU 2558 C ASP B 81 893 646 701 -51 -74 35 C ATOM 2559 O ASP A 81 8.727 -12.678 16.694 1.00 6.19 O ANISOU 2559 O ASP B 81 1111 573 665 -53 -136 -75 O ATOM 2560 CB ASP A 81 11.016 -14.020 18.539 1.00 5.94 C ANISOU 2560 CB ASP B 81 760 735 762 -131 -45 26 C ATOM 2561 CG ASP A 81 11.757 -15.288 18.818 1.00 8.13 C ANISOU 2561 CG ASP B 81 857 1299 931 6 101 306 C ATOM 2562 OD1 ASP A 81 11.375 -15.997 19.768 1.00 8.73 O ANISOU 2562 OD1 ASP B 81 823 1269 1225 90 51 481 O ATOM 2563 OD2 ASP A 81 12.721 -15.671 18.130 1.00 12.20 O ANISOU 2563 OD2 ASP B 81 1328 2090 1216 390 175 684 O ATOM 2564 N LYS A 82 8.499 -12.110 18.851 1.00 5.86 N ANISOU 2564 N LYS B 82 954 585 687 16 -111 85 N ATOM 2565 CA LYS A 82 7.782 -10.865 18.584 1.00 6.39 C ANISOU 2565 CA LYS B 82 957 726 743 26 -54 74 C ATOM 2566 C LYS A 82 8.333 -9.718 19.409 1.00 5.99 C ANISOU 2566 C LYS B 82 951 659 665 67 -75 61 C ATOM 2567 O LYS A 82 8.600 -9.867 20.589 1.00 6.95 O ANISOU 2567 O LYS B 82 1374 512 751 -2 -141 46 O ATOM 2568 CB LYS A 82 6.296 -11.009 18.948 1.00 7.62 C ANISOU 2568 CB LYS B 82 1057 879 958 -70 -112 34 C ATOM 2569 CG LYS A 82 5.504 -11.972 18.113 1.00 9.72 C ANISOU 2569 CG LYS B 82 1286 1166 1238 -23 -61 31 C ATOM 2570 CD LYS A 82 4.020 -11.926 18.436 1.00 11.91 C ANISOU 2570 CD LYS B 82 1423 1547 1552 -158 40 11 C ATOM 2571 CE LYS A 82 3.278 -12.666 17.370 1.00 13.50 C ANISOU 2571 CE LYS B 82 1743 1799 1587 140 -68 101 C ATOM 2572 NZ LYS A 82 1.871 -12.745 17.688 1.00 12.47 N ANISOU 2572 NZ LYS B 82 1487 1625 1625 109 152 167 N ATOM 2573 N TYR A 83 8.440 -8.553 18.776 1.00 4.78 N ANISOU 2573 N TYR B 83 810 510 493 52 -121 -27 N ATOM 2574 CA TYR A 83 8.742 -7.306 19.486 1.00 4.51 C ANISOU 2574 CA TYR B 83 654 521 537 51 -137 4 C ATOM 2575 C TYR A 83 7.539 -6.411 19.288 1.00 5.50 C ANISOU 2575 C TYR B 83 726 691 672 96 -136 -40 C ATOM 2576 O TYR A 83 7.285 -5.964 18.179 1.00 6.57 O ANISOU 2576 O TYR B 83 1019 875 601 236 -173 -78 O ATOM 2577 CB TYR A 83 9.987 -6.649 18.929 1.00 5.37 C ANISOU 2577 CB TYR B 83 833 635 570 32 -63 -61 C ATOM 2578 CG TYR A 83 10.284 -5.308 19.560 1.00 4.83 C ANISOU 2578 CG TYR B 83 659 652 523 -56 -63 14 C ATOM 2579 CD1 TYR A 83 10.750 -5.227 20.868 1.00 5.35 C ANISOU 2579 CD1 TYR B 83 728 647 656 -36 -93 -1 C ATOM 2580 CD2 TYR A 83 10.081 -4.135 18.862 1.00 6.05 C ANISOU 2580 CD2 TYR B 83 1046 664 588 -182 -73 -15 C ATOM 2581 CE1 TYR A 83 11.041 -4.019 21.451 1.00 6.59 C ANISOU 2581 CE1 TYR B 83 1138 776 588 -179 -39 56 C ATOM 2582 CE2 TYR A 83 10.375 -2.910 19.438 1.00 7.33 C ANISOU 2582 CE2 TYR B 83 1398 698 687 -276 100 8 C ATOM 2583 CZ TYR A 83 10.832 -2.850 20.730 1.00 6.52 C ANISOU 2583 CZ TYR B 83 1279 619 576 -275 122 -129 C ATOM 2584 OH TYR A 83 11.165 -1.647 21.324 1.00 7.88 O ANISOU 2584 OH TYR B 83 1679 611 701 -490 209 -41 O ATOM 2585 N ILE A 84 6.824 -6.166 20.374 1.00 5.23 N ANISOU 2585 N ILE B 84 694 608 684 122 -182 19 N ATOM 2586 CA ILE A 84 5.508 -5.515 20.335 1.00 5.83 C ANISOU 2586 CA ILE B 84 728 684 801 115 -95 -43 C ATOM 2587 C ILE A 84 5.573 -4.102 20.897 1.00 4.95 C ANISOU 2587 C ILE B 84 651 598 631 85 -80 17 C ATOM 2588 O ILE A 84 6.152 -3.870 21.959 1.00 4.39 O ANISOU 2588 O ILE B 84 540 544 582 21 9 -22 O ATOM 2589 CB ILE A 84 4.508 -6.311 21.186 1.00 6.95 C ANISOU 2589 CB ILE B 84 727 786 1126 135 -63 -58 C ATOM 2590 CG1 ILE A 84 4.469 -7.787 20.741 1.00 12.48 C ANISOU 2590 CG1 ILE B 84 1457 1294 1987 80 29 -161 C ATOM 2591 CG2 ILE A 84 3.142 -5.605 21.249 1.00 8.97 C ANISOU 2591 CG2 ILE B 84 837 1078 1492 2 117 9 C ATOM 2592 CD1 ILE A 84 3.399 -8.223 19.901 1.00 17.94 C ANISOU 2592 CD1 ILE B 84 2402 2150 2265 141 116 -173 C ATOM 2593 N BSER A 85 5.038 -3.111 20.177 0.60 4.47 N ANISOU 2593 N BSER B 85 545 575 579 31 -104 41 N ATOM 2594 CA BSER A 85 4.784 -1.787 20.794 0.60 4.36 C ANISOU 2594 CA BSER B 85 553 487 616 -115 -82 125 C ATOM 2595 C BSER A 85 3.573 -1.159 20.145 0.60 4.06 C ANISOU 2595 C BSER B 85 505 487 550 -70 -97 8 C ATOM 2596 O BSER A 85 2.845 -1.782 19.369 0.60 4.54 O ANISOU 2596 O BSER B 85 583 451 692 -61 -205 -118 O ATOM 2597 CB BSER A 85 6.003 -0.800 20.764 0.60 5.08 C ANISOU 2597 CB BSER B 85 675 558 695 -199 -109 146 C ATOM 2598 OG BSER A 85 5.861 0.419 21.625 0.60 7.25 O ANISOU 2598 OG BSER B 85 569 893 1290 -438 -447 732 O ATOM 2599 N VAL A 86 3.363 0.088 20.512 1.00 4.60 N ANISOU 2599 N VAL B 86 618 498 631 6 -48 -69 N ATOM 2600 CA VAL A 86 2.243 0.887 20.059 1.00 4.39 C ANISOU 2600 CA VAL B 86 614 519 533 -18 -19 -9 C ATOM 2601 C VAL A 86 2.805 2.074 19.287 1.00 4.25 C ANISOU 2601 C VAL B 86 581 539 493 -9 29 -23 C ATOM 2602 O VAL A 86 3.754 2.713 19.738 1.00 4.58 O ANISOU 2602 O VAL B 86 513 576 649 -37 -48 -33 O ATOM 2603 CB VAL A 86 1.389 1.314 21.253 1.00 4.93 C ANISOU 2603 CB VAL B 86 704 537 629 -13 7 24 C ATOM 2604 CG1 VAL A 86 0.436 2.435 20.928 1.00 6.17 C ANISOU 2604 CG1 VAL B 86 875 684 784 77 42 39 C ATOM 2605 CG2 VAL A 86 0.621 0.099 21.784 1.00 6.20 C ANISOU 2605 CG2 VAL B 86 845 746 764 -48 126 59 C ATOM 2606 N ALA A 87 2.198 2.397 18.146 1.00 3.49 N ANISOU 2606 N ALA B 87 434 440 449 -92 18 -24 N ATOM 2607 CA ALA A 87 2.703 3.420 17.238 1.00 3.85 C ANISOU 2607 CA ALA B 87 528 504 428 -107 76 -47 C ATOM 2608 C ALA A 87 1.950 4.712 17.306 1.00 4.16 C ANISOU 2608 C ALA B 87 550 524 505 -96 54 -3 C ATOM 2609 O ALA A 87 2.414 5.672 16.749 1.00 5.15 O ANISOU 2609 O ALA B 87 652 557 746 -29 183 4 O ATOM 2610 CB ALA A 87 2.714 2.919 15.800 1.00 4.67 C ANISOU 2610 CB ALA B 87 651 421 701 27 89 -51 C ATOM 2611 N ASP A 88 0.797 4.755 17.965 1.00 3.92 N ANISOU 2611 N ASP B 88 515 358 615 -136 101 53 N ATOM 2612 CA ASP A 88 0.025 5.978 18.096 1.00 3.89 C ANISOU 2612 CA ASP B 88 437 447 592 -119 51 -9 C ATOM 2613 C ASP A 88 -0.138 6.347 19.554 1.00 3.89 C ANISOU 2613 C ASP B 88 510 383 585 -169 54 -21 C ATOM 2614 O ASP A 88 0.655 5.913 20.389 1.00 4.20 O ANISOU 2614 O ASP B 88 505 344 745 -152 43 -27 O ATOM 2615 CB ASP A 88 -1.300 5.915 17.316 1.00 4.05 C ANISOU 2615 CB ASP B 88 577 374 587 -68 100 111 C ATOM 2616 CG ASP A 88 -2.313 4.968 17.912 1.00 4.37 C ANISOU 2616 CG ASP B 88 699 507 452 -168 123 -26 C ATOM 2617 OD1 ASP A 88 -1.986 4.217 18.877 1.00 4.25 O ANISOU 2617 OD1 ASP B 88 576 567 469 -181 118 16 O ATOM 2618 OD2 ASP A 88 -3.465 4.937 17.422 1.00 5.18 O ANISOU 2618 OD2 ASP B 88 670 470 824 -236 -79 153 O ATOM 2619 N GLY A 89 -1.132 7.174 19.860 1.00 3.90 N ANISOU 2619 N GLY B 89 500 471 510 -150 62 22 N ATOM 2620 CA GLY A 89 -1.406 7.588 21.227 1.00 4.24 C ANISOU 2620 CA GLY B 89 540 524 544 -62 89 3 C ATOM 2621 C GLY A 89 -2.223 6.628 22.067 1.00 4.82 C ANISOU 2621 C GLY B 89 647 631 553 -31 133 -15 C ATOM 2622 O GLY A 89 -2.585 6.975 23.178 1.00 5.28 O ANISOU 2622 O GLY B 89 848 689 466 99 225 -5 O ATOM 2623 N GLY A 90 -2.522 5.429 21.551 1.00 4.95 N ANISOU 2623 N GLY B 90 583 682 613 -68 82 53 N ATOM 2624 CA GLY A 90 -3.403 4.502 22.270 1.00 5.38 C ANISOU 2624 CA GLY B 90 653 761 631 -53 78 79 C ATOM 2625 C GLY A 90 -2.693 3.637 23.278 1.00 5.17 C ANISOU 2625 C GLY B 90 627 675 660 -1 75 57 C ATOM 2626 O GLY A 90 -1.501 3.780 23.555 1.00 4.89 O ANISOU 2626 O GLY B 90 579 712 565 -62 107 73 O ATOM 2627 N LYS A 91 -3.451 2.718 23.845 1.00 5.42 N ANISOU 2627 N LYS B 91 575 755 728 -52 7 129 N ATOM 2628 CA LYS A 91 -2.915 1.828 24.845 1.00 6.41 C ANISOU 2628 CA LYS B 91 732 832 869 -34 -3 68 C ATOM 2629 C LYS A 91 -3.723 0.568 24.938 1.00 5.08 C ANISOU 2629 C LYS B 91 526 695 708 -109 91 79 C ATOM 2630 O LYS A 91 -4.938 0.557 24.676 1.00 5.35 O ANISOU 2630 O LYS B 91 543 708 781 -99 -12 74 O ATOM 2631 CB LYS A 91 -2.824 2.480 26.219 1.00 8.74 C ANISOU 2631 CB LYS B 91 1193 924 1202 -131 -27 138 C ATOM 2632 CG LYS A 91 -4.063 2.984 26.773 1.00 12.27 C ANISOU 2632 CG LYS B 91 1548 1505 1608 -162 -88 -28 C ATOM 2633 CD LYS A 91 -3.860 3.429 28.234 1.00 15.05 C ANISOU 2633 CD LYS B 91 2004 1873 1841 9 82 -54 C ATOM 2634 CE LYS A 91 -5.115 4.040 28.784 1.00 18.10 C ANISOU 2634 CE LYS B 91 2352 2303 2221 -69 76 -132 C ATOM 2635 NZ LYS A 91 -4.859 4.643 30.110 1.00 19.46 N ANISOU 2635 NZ LYS B 91 2869 2447 2076 -8 141 -194 N ATOM 2636 N VAL A 92 -3.022 -0.501 25.306 1.00 4.73 N ANISOU 2636 N VAL B 92 440 688 669 -95 56 71 N ATOM 2637 CA VAL A 92 -3.619 -1.805 25.511 1.00 5.07 C ANISOU 2637 CA VAL B 92 575 648 700 -87 41 98 C ATOM 2638 C VAL A 92 -3.180 -2.389 26.845 1.00 5.25 C ANISOU 2638 C VAL B 92 603 694 695 -101 10 57 C ATOM 2639 O VAL A 92 -2.127 -2.025 27.388 1.00 5.48 O ANISOU 2639 O VAL B 92 561 747 771 -176 -7 121 O ATOM 2640 CB VAL A 92 -3.290 -2.827 24.369 1.00 4.59 C ANISOU 2640 CB VAL B 92 500 609 633 -105 13 100 C ATOM 2641 CG1 VAL A 92 -3.695 -2.281 23.029 1.00 5.68 C ANISOU 2641 CG1 VAL B 92 653 764 738 -97 23 76 C ATOM 2642 CG2 VAL A 92 -1.839 -3.267 24.345 1.00 6.08 C ANISOU 2642 CG2 VAL B 92 767 696 845 32 9 68 C ATOM 2643 N LEU A 93 -3.993 -3.297 27.361 1.00 4.99 N ANISOU 2643 N LEU B 93 544 672 680 -61 -76 94 N ATOM 2644 CA LEU A 93 -3.582 -4.178 28.412 1.00 5.76 C ANISOU 2644 CA LEU B 93 687 763 738 -53 19 59 C ATOM 2645 C LEU A 93 -3.006 -5.407 27.729 1.00 5.36 C ANISOU 2645 C LEU B 93 658 738 640 -108 52 62 C ATOM 2646 O LEU A 93 -3.729 -6.202 27.131 1.00 7.11 O ANISOU 2646 O LEU B 93 733 982 986 -232 69 -265 O ATOM 2647 CB LEU A 93 -4.785 -4.553 29.275 1.00 5.95 C ANISOU 2647 CB LEU B 93 669 787 804 -47 35 104 C ATOM 2648 CG LEU A 93 -4.550 -5.598 30.368 1.00 7.54 C ANISOU 2648 CG LEU B 93 979 1034 852 12 181 83 C ATOM 2649 CD1 LEU A 93 -3.497 -5.110 31.332 1.00 9.51 C ANISOU 2649 CD1 LEU B 93 1252 1451 907 83 190 310 C ATOM 2650 CD2 LEU A 93 -5.874 -5.936 31.084 1.00 8.95 C ANISOU 2650 CD2 LEU B 93 1200 1171 1029 -9 219 188 C ATOM 2651 N GLY A 94 -1.697 -5.539 27.789 1.00 5.34 N ANISOU 2651 N GLY B 94 739 635 652 -58 7 159 N ATOM 2652 CA GLY A 94 -1.029 -6.696 27.240 1.00 5.34 C ANISOU 2652 CA GLY B 94 698 669 660 -23 -7 76 C ATOM 2653 C GLY A 94 -1.070 -7.860 28.232 1.00 5.45 C ANISOU 2653 C GLY B 94 651 751 666 10 -23 92 C ATOM 2654 O GLY A 94 -0.967 -7.671 29.434 1.00 4.97 O ANISOU 2654 O GLY B 94 697 593 596 38 -158 172 O ATOM 2655 N THR A 95 -1.208 -9.062 27.705 1.00 4.49 N ANISOU 2655 N THR B 95 630 637 439 66 -61 215 N ATOM 2656 CA THR A 95 -1.367 -10.263 28.522 1.00 5.21 C ANISOU 2656 CA THR B 95 647 706 625 -2 -12 82 C ATOM 2657 C THR A 95 -0.619 -11.403 27.887 1.00 4.56 C ANISOU 2657 C THR B 95 618 601 513 34 -47 129 C ATOM 2658 O THR A 95 -0.727 -11.626 26.663 1.00 4.81 O ANISOU 2658 O THR B 95 666 719 442 37 -57 61 O ATOM 2659 CB THR A 95 -2.870 -10.629 28.581 1.00 5.77 C ANISOU 2659 CB THR B 95 674 798 719 -1 8 61 C ATOM 2660 OG1 THR A 95 -3.598 -9.584 29.236 1.00 7.26 O ANISOU 2660 OG1 THR B 95 736 1103 918 128 52 -61 O ATOM 2661 CG2 THR A 95 -3.131 -11.872 29.401 1.00 7.43 C ANISOU 2661 CG2 THR B 95 850 1183 786 -10 10 -17 C ATOM 2662 N TRP A 96 0.108 -12.149 28.706 1.00 5.14 N ANISOU 2662 N TRP B 96 691 716 546 -2 12 139 N ATOM 2663 CA TRP A 96 0.936 -13.215 28.208 1.00 5.03 C ANISOU 2663 CA TRP B 96 656 683 570 24 17 146 C ATOM 2664 C TRP A 96 0.754 -14.423 29.109 1.00 5.28 C ANISOU 2664 C TRP B 96 695 706 602 9 0 179 C ATOM 2665 O TRP A 96 0.606 -14.345 30.373 1.00 6.88 O ANISOU 2665 O TRP B 96 866 1005 740 169 -86 -51 O ATOM 2666 CB TRP A 96 2.428 -12.821 28.192 1.00 6.10 C ANISOU 2666 CB TRP B 96 683 912 722 127 -34 25 C ATOM 2667 CG TRP A 96 2.588 -11.712 27.261 1.00 5.66 C ANISOU 2667 CG TRP B 96 513 817 820 164 23 -32 C ATOM 2668 CD1 TRP A 96 2.709 -11.792 25.921 1.00 6.20 C ANISOU 2668 CD1 TRP B 96 659 789 906 -157 214 151 C ATOM 2669 CD2 TRP A 96 2.516 -10.334 27.582 1.00 5.51 C ANISOU 2669 CD2 TRP B 96 544 747 800 -102 145 245 C ATOM 2670 NE1 TRP A 96 2.737 -10.530 25.368 1.00 5.96 N ANISOU 2670 NE1 TRP B 96 793 827 643 -19 271 239 N ATOM 2671 CE2 TRP A 96 2.622 -9.614 26.371 1.00 6.00 C ANISOU 2671 CE2 TRP B 96 608 848 823 -90 156 171 C ATOM 2672 CE3 TRP A 96 2.390 -9.619 28.771 1.00 5.77 C ANISOU 2672 CE3 TRP B 96 495 764 931 -119 83 125 C ATOM 2673 CZ2 TRP A 96 2.571 -8.241 26.324 1.00 6.70 C ANISOU 2673 CZ2 TRP B 96 752 901 893 -95 52 219 C ATOM 2674 CZ3 TRP A 96 2.367 -8.255 28.728 1.00 5.71 C ANISOU 2674 CZ3 TRP B 96 634 727 807 -109 98 66 C ATOM 2675 CH2 TRP A 96 2.463 -7.571 27.510 1.00 6.34 C ANISOU 2675 CH2 TRP B 96 623 842 942 -116 240 207 C ATOM 2676 N VAL A 97 0.753 -15.555 28.440 1.00 6.85 N ANISOU 2676 N VAL B 97 827 970 803 162 -98 -147 N ATOM 2677 CA VAL A 97 0.754 -16.814 29.125 1.00 5.86 C ANISOU 2677 CA VAL B 97 798 710 717 69 -47 42 C ATOM 2678 C VAL A 97 1.846 -17.677 28.510 1.00 6.86 C ANISOU 2678 C VAL B 97 787 947 870 8 -7 -172 C ATOM 2679 O VAL A 97 1.849 -17.931 27.316 1.00 5.87 O ANISOU 2679 O VAL B 97 834 664 729 82 -6 253 O ATOM 2680 CB VAL A 97 -0.632 -17.519 29.007 1.00 6.48 C ANISOU 2680 CB VAL B 97 817 790 852 23 -17 40 C ATOM 2681 CG1 VAL A 97 -0.660 -18.850 29.818 1.00 6.71 C ANISOU 2681 CG1 VAL B 97 884 779 883 37 99 107 C ATOM 2682 CG2 VAL A 97 -1.751 -16.602 29.491 1.00 7.38 C ANISOU 2682 CG2 VAL B 97 1009 908 887 -23 16 167 C ATOM 2683 N ASP A 98 2.751 -18.180 29.328 1.00 5.81 N ANISOU 2683 N ASP B 98 714 759 731 75 -26 42 N ATOM 2684 CA ASP A 98 3.805 -19.039 28.837 1.00 6.49 C ANISOU 2684 CA ASP B 98 755 903 805 43 27 -38 C ATOM 2685 C ASP A 98 3.215 -20.410 28.508 1.00 6.32 C ANISOU 2685 C ASP B 98 714 832 855 84 -29 -46 C ATOM 2686 O ASP A 98 2.673 -21.117 29.406 1.00 5.30 O ANISOU 2686 O ASP B 98 694 553 766 -84 -35 175 O ATOM 2687 CB ASP A 98 4.865 -19.153 29.908 1.00 6.69 C ANISOU 2687 CB ASP B 98 809 815 915 21 -29 -47 C ATOM 2688 CG ASP A 98 6.165 -19.650 29.386 1.00 7.39 C ANISOU 2688 CG ASP B 98 770 1033 1003 -79 37 -92 C ATOM 2689 OD1 ASP A 98 6.225 -20.179 28.259 1.00 7.44 O ANISOU 2689 OD1 ASP B 98 575 1155 1095 99 13 -92 O ATOM 2690 OD2 ASP A 98 7.208 -19.637 30.144 1.00 7.72 O ANISOU 2690 OD2 ASP B 98 715 1016 1201 -116 -92 -83 O ATOM 2691 N LEU A 99 3.300 -20.799 27.229 1.00 5.99 N ANISOU 2691 N LEU B 99 768 734 772 53 -29 31 N ATOM 2692 CA LEU A 99 2.789 -22.141 26.824 1.00 5.38 C ANISOU 2692 CA LEU B 99 743 542 758 -59 20 18 C ATOM 2693 C LEU A 99 3.883 -23.167 26.516 1.00 6.01 C ANISOU 2693 C LEU B 99 709 760 815 15 28 -52 C ATOM 2694 O LEU A 99 3.600 -24.276 25.979 1.00 5.82 O ANISOU 2694 O LEU B 99 669 478 1064 -7 12 -87 O ATOM 2695 CB LEU A 99 1.804 -22.069 25.645 1.00 5.97 C ANISOU 2695 CB LEU B 99 787 648 830 -19 48 0 C ATOM 2696 CG LEU A 99 0.518 -21.299 25.937 1.00 5.29 C ANISOU 2696 CG LEU B 99 665 617 729 -113 -15 82 C ATOM 2697 CD1 LEU A 99 -0.367 -21.333 24.723 1.00 6.04 C ANISOU 2697 CD1 LEU B 99 730 749 814 -26 26 100 C ATOM 2698 CD2 LEU A 99 -0.224 -21.834 27.202 1.00 6.45 C ANISOU 2698 CD2 LEU B 99 757 818 873 -48 -57 72 C ATOM 2699 N ARG A 100 5.103 -22.855 26.930 1.00 6.13 N ANISOU 2699 N ARG B 100 811 630 887 5 44 -64 N ATOM 2700 CA ARG A 100 6.246 -23.748 26.733 1.00 6.35 C ANISOU 2700 CA ARG B 100 747 817 849 40 -26 -12 C ATOM 2701 C ARG A 100 6.375 -24.765 27.844 1.00 6.21 C ANISOU 2701 C ARG B 100 773 707 878 5 1 40 C ATOM 2702 O ARG A 100 6.232 -24.383 29.022 1.00 6.89 O ANISOU 2702 O ARG B 100 752 904 959 37 -85 -162 O ATOM 2703 CB ARG A 100 7.535 -22.963 26.737 1.00 6.30 C ANISOU 2703 CB ARG B 100 738 751 906 68 -42 4 C ATOM 2704 CG ARG A 100 7.616 -21.980 25.610 1.00 7.19 C ANISOU 2704 CG ARG B 100 818 917 996 92 -27 10 C ATOM 2705 CD ARG A 100 8.765 -21.026 25.747 1.00 7.02 C ANISOU 2705 CD ARG B 100 694 1012 960 57 71 56 C ATOM 2706 NE ARG A 100 8.645 -20.245 26.962 1.00 6.91 N ANISOU 2706 NE ARG B 100 634 778 1210 -56 61 -65 N ATOM 2707 CZ ARG A 100 9.516 -19.332 27.359 1.00 6.63 C ANISOU 2707 CZ ARG B 100 665 722 1132 30 -14 25 C ATOM 2708 NH1 ARG A 100 10.546 -19.025 26.592 1.00 8.16 N ANISOU 2708 NH1 ARG B 100 817 1003 1279 -98 99 28 N ATOM 2709 NH2 ARG A 100 9.313 -18.711 28.511 1.00 7.58 N ANISOU 2709 NH2 ARG B 100 725 1022 1132 -67 -90 45 N ATOM 2710 N GLU A 101 6.603 -26.051 27.456 1.00 7.95 N ANISOU 2710 N GLU B 101 981 1025 1014 62 -29 -55 N ATOM 2711 CA GLU A 101 6.813 -27.161 28.374 1.00 8.80 C ANISOU 2711 CA GLU B 101 1086 1136 1120 20 -38 -35 C ATOM 2712 C GLU A 101 8.005 -26.991 29.332 1.00 8.97 C ANISOU 2712 C GLU B 101 1111 1148 1149 86 -64 -30 C ATOM 2713 O GLU A 101 9.133 -26.589 28.928 1.00 9.48 O ANISOU 2713 O GLU B 101 1028 1387 1187 90 -116 -137 O ATOM 2714 CB GLU A 101 7.049 -28.445 27.596 1.00 9.39 C ANISOU 2714 CB GLU B 101 1256 1142 1169 47 -33 -39 C ATOM 2715 CG GLU A 101 7.194 -29.695 28.454 1.00 12.18 C ANISOU 2715 CG GLU B 101 1604 1490 1531 81 -61 -41 C ATOM 2716 CD GLU A 101 7.475 -30.904 27.595 1.00 16.43 C ANISOU 2716 CD GLU B 101 2196 1939 2108 -17 16 -83 C ATOM 2717 OE1 GLU A 101 8.559 -30.934 26.977 1.00 17.92 O ANISOU 2717 OE1 GLU B 101 2315 2020 2473 371 50 -200 O ATOM 2718 OE2 GLU A 101 6.606 -31.799 27.519 1.00 21.47 O ANISOU 2718 OE2 GLU B 101 2899 2620 2636 -86 47 -186 O ATOM 2719 N GLY A 102 7.815 -27.400 30.608 1.00 12.08 N ANISOU 2719 N GLY B 102 1365 1612 1613 54 -31 -182 N ATOM 2720 CA GLY A 102 8.771 -27.119 31.711 1.00 14.08 C ANISOU 2720 CA GLY B 102 1609 1990 1749 85 -32 -250 C ATOM 2721 C GLY A 102 8.028 -26.415 32.835 1.00 15.10 C ANISOU 2721 C GLY B 102 1706 2200 1831 112 -49 -275 C ATOM 2722 O GLY A 102 6.815 -26.134 32.765 1.00 17.84 O ANISOU 2722 O GLY B 102 1704 2921 2154 98 -75 -741 O ATOM 2723 N GLU A 103 8.819 -26.026 33.890 1.00 14.15 N ANISOU 2723 N GLU B 103 1667 1906 1800 56 -71 -163 N ATOM 2724 CA GLU A 103 8.350 -25.258 35.123 1.00 14.11 C ANISOU 2724 CA GLU B 103 1729 1825 1806 34 -39 -97 C ATOM 2725 C GLU A 103 7.471 -23.950 34.874 1.00 13.23 C ANISOU 2725 C GLU B 103 1651 1692 1684 -6 -54 -70 C ATOM 2726 O GLU A 103 6.533 -23.655 35.649 1.00 15.70 O ANISOU 2726 O GLU B 103 1894 2046 2022 -27 2 -417 O ATOM 2727 CB GLU A 103 9.582 -24.905 35.990 1.00 14.16 C ANISOU 2727 CB GLU B 103 1731 1850 1798 51 -64 -62 C ATOM 2728 CG GLU A 103 10.776 -24.282 35.246 1.00 15.47 C ANISOU 2728 CG GLU B 103 1876 2061 1937 60 -39 -107 C ATOM 2729 CD GLU A 103 12.152 -24.619 35.829 1.00 17.48 C ANISOU 2729 CD GLU B 103 2025 2330 2283 48 125 -268 C ATOM 2730 OE1 GLU A 103 12.243 -25.361 36.823 1.00 19.16 O ANISOU 2730 OE1 GLU B 103 2137 2831 2311 124 117 -424 O ATOM 2731 OE2 GLU A 103 13.158 -24.115 35.275 1.00 18.89 O ANISOU 2731 OE2 GLU B 103 2058 2463 2657 -11 190 -526 O ATOM 2732 N THR A 104 7.718 -23.181 33.815 1.00 13.68 N ANISOU 2732 N THR B 104 1562 1832 1804 11 -62 -192 N ATOM 2733 CA THR A 104 7.007 -21.895 33.719 1.00 11.99 C ANISOU 2733 CA THR B 104 1347 1542 1666 -52 -87 -96 C ATOM 2734 C THR A 104 5.748 -21.934 32.840 1.00 11.36 C ANISOU 2734 C THR B 104 1252 1530 1532 129 -161 -11 C ATOM 2735 O THR A 104 5.162 -20.879 32.542 1.00 11.91 O ANISOU 2735 O THR B 104 1156 1501 1867 -83 -118 -162 O ATOM 2736 CB THR A 104 7.947 -20.731 33.265 1.00 11.96 C ANISOU 2736 CB THR B 104 1319 1586 1638 10 -133 -119 C ATOM 2737 OG1 THR A 104 8.394 -20.940 31.901 1.00 11.94 O ANISOU 2737 OG1 THR B 104 1103 1592 1840 -45 -140 -123 O ATOM 2738 CG2 THR A 104 9.207 -20.690 34.124 1.00 10.94 C ANISOU 2738 CG2 THR B 104 1236 1318 1600 -27 -107 32 C ATOM 2739 N PHE A 105 5.347 -23.114 32.392 1.00 11.27 N ANISOU 2739 N PHE B 105 1140 1581 1560 -51 -104 -193 N ATOM 2740 CA PHE A 105 4.074 -23.281 31.700 1.00 10.74 C ANISOU 2740 CA PHE B 105 1193 1529 1357 114 -97 -93 C ATOM 2741 C PHE A 105 2.909 -22.786 32.553 1.00 9.90 C ANISOU 2741 C PHE B 105 1037 1419 1303 87 -95 -149 C ATOM 2742 O PHE A 105 2.783 -23.138 33.735 1.00 10.14 O ANISOU 2742 O PHE B 105 1104 1373 1374 99 -10 41 O ATOM 2743 CB PHE A 105 3.820 -24.742 31.394 1.00 10.32 C ANISOU 2743 CB PHE B 105 1159 1351 1409 10 -60 -26 C ATOM 2744 CG PHE A 105 2.597 -24.955 30.575 1.00 9.93 C ANISOU 2744 CG PHE B 105 1175 1379 1217 154 -193 65 C ATOM 2745 CD1 PHE A 105 2.636 -24.745 29.204 1.00 10.63 C ANISOU 2745 CD1 PHE B 105 1116 1526 1398 -122 -51 -138 C ATOM 2746 CD2 PHE A 105 1.386 -25.308 31.176 1.00 9.89 C ANISOU 2746 CD2 PHE B 105 1076 1408 1270 -35 -49 54 C ATOM 2747 CE1 PHE A 105 1.478 -24.924 28.434 1.00 11.07 C ANISOU 2747 CE1 PHE B 105 1203 1745 1258 251 -249 -83 C ATOM 2748 CE2 PHE A 105 0.240 -25.500 30.435 1.00 9.59 C ANISOU 2748 CE2 PHE B 105 1175 1399 1069 61 -170 84 C ATOM 2749 CZ PHE A 105 0.275 -25.313 29.057 1.00 10.24 C ANISOU 2749 CZ PHE B 105 1220 1423 1245 -62 -29 56 C ATOM 2750 N GLY A 106 2.074 -21.966 31.898 1.00 7.76 N ANISOU 2750 N GLY B 106 825 1108 1015 21 31 -83 N ATOM 2751 CA GLY A 106 0.915 -21.328 32.503 1.00 7.91 C ANISOU 2751 CA GLY B 106 899 1072 1033 96 -52 -129 C ATOM 2752 C GLY A 106 1.218 -19.942 33.136 1.00 6.84 C ANISOU 2752 C GLY B 106 730 909 959 -22 69 -10 C ATOM 2753 O GLY A 106 0.313 -19.225 33.588 1.00 8.39 O ANISOU 2753 O GLY B 106 858 1037 1290 229 -90 -125 O ATOM 2754 N ASN A 107 2.511 -19.655 33.341 1.00 6.86 N ANISOU 2754 N ASN B 107 807 906 891 93 -87 -63 N ATOM 2755 CA ASN A 107 2.871 -18.404 33.992 1.00 6.43 C ANISOU 2755 CA ASN B 107 792 856 795 48 -9 27 C ATOM 2756 C ASN A 107 2.410 -17.245 33.144 1.00 7.66 C ANISOU 2756 C ASN B 107 874 1104 930 152 -34 -234 C ATOM 2757 O ASN A 107 2.332 -17.401 31.977 1.00 6.80 O ANISOU 2757 O ASN B 107 925 743 914 95 135 101 O ATOM 2758 CB ASN A 107 4.377 -18.293 34.170 1.00 7.04 C ANISOU 2758 CB ASN B 107 714 965 995 31 -77 -114 C ATOM 2759 CG ASN A 107 4.917 -19.104 35.320 1.00 7.53 C ANISOU 2759 CG ASN B 107 710 1183 965 252 -257 -94 C ATOM 2760 OD1 ASN A 107 4.219 -19.912 35.965 1.00 7.86 O ANISOU 2760 OD1 ASN B 107 956 871 1158 -64 -168 202 O ATOM 2761 ND2 ASN A 107 6.205 -18.891 35.588 1.00 8.44 N ANISOU 2761 ND2 ASN B 107 654 1361 1189 -122 127 -195 N ATOM 2762 N THR A 108 2.070 -16.152 33.798 1.00 6.34 N ANISOU 2762 N THR B 108 849 789 770 92 -26 117 N ATOM 2763 CA THR A 108 1.402 -15.063 33.171 1.00 7.26 C ANISOU 2763 CA THR B 108 823 941 991 120 -15 -66 C ATOM 2764 C THR A 108 2.115 -13.832 33.575 1.00 6.17 C ANISOU 2764 C THR B 108 856 798 690 81 -6 156 C ATOM 2765 O THR A 108 2.839 -13.760 34.594 1.00 7.30 O ANISOU 2765 O THR B 108 915 971 888 97 -169 -7 O ATOM 2766 CB THR A 108 -0.063 -14.930 33.635 1.00 6.79 C ANISOU 2766 CB THR B 108 840 890 850 84 29 47 C ATOM 2767 OG1 THR A 108 -0.125 -14.595 35.036 1.00 8.69 O ANISOU 2767 OG1 THR B 108 1014 1145 1142 174 30 -16 O ATOM 2768 CG2 THR A 108 -0.808 -16.236 33.507 1.00 7.30 C ANISOU 2768 CG2 THR B 108 944 907 919 155 70 166 C ATOM 2769 N TYR A 109 1.893 -12.840 32.727 1.00 5.77 N ANISOU 2769 N TYR B 109 761 763 667 44 -32 153 N ATOM 2770 CA TYR A 109 2.271 -11.504 33.040 1.00 6.20 C ANISOU 2770 CA TYR B 109 768 851 733 74 -26 66 C ATOM 2771 C TYR A 109 1.246 -10.637 32.324 1.00 5.10 C ANISOU 2771 C TYR B 109 653 726 559 4 -10 115 C ATOM 2772 O TYR A 109 0.680 -11.047 31.309 1.00 5.86 O ANISOU 2772 O TYR B 109 689 884 651 -29 11 25 O ATOM 2773 CB TYR A 109 3.683 -11.231 32.508 1.00 6.15 C ANISOU 2773 CB TYR B 109 681 847 808 22 -37 97 C ATOM 2774 CG TYR A 109 4.192 -9.830 32.786 1.00 7.03 C ANISOU 2774 CG TYR B 109 768 992 908 66 -68 38 C ATOM 2775 CD1 TYR A 109 4.354 -9.374 34.092 1.00 7.78 C ANISOU 2775 CD1 TYR B 109 1039 911 1004 -35 -17 10 C ATOM 2776 CD2 TYR A 109 4.524 -8.958 31.745 1.00 7.11 C ANISOU 2776 CD2 TYR B 109 819 996 885 64 -1 -32 C ATOM 2777 CE1 TYR A 109 4.829 -8.097 34.346 1.00 8.62 C ANISOU 2777 CE1 TYR B 109 1002 1201 1071 -116 -101 -61 C ATOM 2778 CE2 TYR A 109 4.997 -7.680 32.000 1.00 8.36 C ANISOU 2778 CE2 TYR B 109 963 1085 1128 -9 17 32 C ATOM 2779 CZ TYR A 109 5.138 -7.258 33.306 1.00 8.56 C ANISOU 2779 CZ TYR B 109 979 1043 1227 -92 -14 -53 C ATOM 2780 OH TYR A 109 5.589 -6.009 33.617 1.00 10.34 O ANISOU 2780 OH TYR B 109 1013 1252 1664 -295 -86 -207 O ATOM 2781 N GLN A 110 0.985 -9.467 32.888 1.00 5.42 N ANISOU 2781 N GLN B 110 704 730 624 0 -26 92 N ATOM 2782 CA GLN A 110 0.195 -8.429 32.237 1.00 5.61 C ANISOU 2782 CA GLN B 110 665 749 717 28 -40 30 C ATOM 2783 C GLN A 110 0.808 -7.086 32.511 1.00 5.51 C ANISOU 2783 C GLN B 110 671 721 700 12 -50 104 C ATOM 2784 O GLN A 110 1.349 -6.870 33.593 1.00 6.63 O ANISOU 2784 O GLN B 110 921 803 793 -42 -172 38 O ATOM 2785 CB GLN A 110 -1.241 -8.398 32.747 1.00 5.83 C ANISOU 2785 CB GLN B 110 745 763 707 -32 -4 12 C ATOM 2786 CG GLN A 110 -2.013 -9.643 32.469 1.00 6.01 C ANISOU 2786 CG GLN B 110 747 709 827 -17 89 -50 C ATOM 2787 CD GLN A 110 -3.460 -9.529 32.939 1.00 6.45 C ANISOU 2787 CD GLN B 110 787 705 955 -85 205 133 C ATOM 2788 OE1 GLN A 110 -3.751 -9.693 34.111 1.00 7.00 O ANISOU 2788 OE1 GLN B 110 843 828 985 -27 -5 6 O ATOM 2789 NE2 GLN A 110 -4.364 -9.235 32.010 1.00 7.17 N ANISOU 2789 NE2 GLN B 110 951 942 827 -107 -10 -3 N ATOM 2790 N THR A 111 0.737 -6.193 31.529 1.00 6.29 N ANISOU 2790 N THR B 111 822 784 785 -61 -58 83 N ATOM 2791 CA THR A 111 1.158 -4.822 31.732 1.00 7.02 C ANISOU 2791 CA THR B 111 865 861 942 -31 -59 76 C ATOM 2792 C THR A 111 0.484 -3.966 30.668 1.00 6.60 C ANISOU 2792 C THR B 111 882 824 799 -58 -93 103 C ATOM 2793 O THR A 111 0.105 -4.476 29.599 1.00 7.05 O ANISOU 2793 O THR B 111 1080 692 904 -213 -171 51 O ATOM 2794 CB THR A 111 2.706 -4.719 31.667 1.00 8.50 C ANISOU 2794 CB THR B 111 1046 993 1188 -41 -114 66 C ATOM 2795 OG1 THR A 111 3.132 -3.483 32.250 1.00 10.74 O ANISOU 2795 OG1 THR B 111 1306 1133 1642 -237 -421 -1 O ATOM 2796 CG2 THR A 111 3.218 -4.704 30.227 1.00 8.92 C ANISOU 2796 CG2 THR B 111 984 941 1463 -117 21 106 C ATOM 2797 N VAL A 112 0.347 -2.678 30.949 1.00 7.13 N ANISOU 2797 N VAL B 112 1000 910 798 -45 -132 69 N ATOM 2798 CA VAL A 112 -0.165 -1.727 29.967 1.00 7.86 C ANISOU 2798 CA VAL B 112 1023 1005 957 -80 -127 83 C ATOM 2799 C VAL A 112 0.939 -1.392 28.974 1.00 7.36 C ANISOU 2799 C VAL B 112 887 985 921 -186 -126 94 C ATOM 2800 O VAL A 112 2.035 -1.020 29.371 1.00 9.63 O ANISOU 2800 O VAL B 112 1024 1488 1146 -407 -340 199 O ATOM 2801 CB VAL A 112 -0.708 -0.436 30.630 1.00 8.86 C ANISOU 2801 CB VAL B 112 1188 1118 1061 -10 -100 60 C ATOM 2802 CG1 VAL A 112 -1.069 0.616 29.584 1.00 11.14 C ANISOU 2802 CG1 VAL B 112 1578 1213 1439 81 -102 55 C ATOM 2803 CG2 VAL A 112 -1.905 -0.740 31.507 1.00 10.89 C ANISOU 2803 CG2 VAL B 112 1448 1353 1336 133 -97 -44 C ATOM 2804 N ILE A 113 0.651 -1.556 27.686 1.00 6.59 N ANISOU 2804 N ILE B 113 709 932 860 -195 -96 133 N ATOM 2805 CA ILE A 113 1.549 -1.155 26.620 1.00 6.70 C ANISOU 2805 CA ILE B 113 711 918 914 -94 -53 165 C ATOM 2806 C ILE A 113 0.984 0.110 25.974 1.00 6.10 C ANISOU 2806 C ILE B 113 650 749 918 -138 -73 155 C ATOM 2807 O ILE A 113 -0.165 0.156 25.548 1.00 6.21 O ANISOU 2807 O ILE B 113 542 809 1009 -157 -1 232 O ATOM 2808 CB ILE A 113 1.689 -2.251 25.537 1.00 7.21 C ANISOU 2808 CB ILE B 113 784 952 1003 -71 -27 189 C ATOM 2809 CG1 ILE A 113 2.052 -3.622 26.120 1.00 9.39 C ANISOU 2809 CG1 ILE B 113 1089 1194 1284 -42 116 130 C ATOM 2810 CG2 ILE A 113 2.714 -1.840 24.486 1.00 8.45 C ANISOU 2810 CG2 ILE B 113 1033 1140 1035 -10 70 191 C ATOM 2811 CD1 ILE A 113 1.900 -4.718 25.055 1.00 13.31 C ANISOU 2811 CD1 ILE B 113 1731 1634 1690 42 61 152 C ATOM 2812 N ASP A 114 1.820 1.143 25.903 1.00 5.73 N ANISOU 2812 N ASP B 114 671 603 902 -143 -128 187 N ATOM 2813 CA ASP A 114 1.558 2.333 25.105 1.00 4.78 C ANISOU 2813 CA ASP B 114 528 591 696 -98 -109 109 C ATOM 2814 C ASP A 114 2.837 2.641 24.324 1.00 4.20 C ANISOU 2814 C ASP B 114 408 463 722 -34 -25 42 C ATOM 2815 O ASP A 114 3.753 1.830 24.289 1.00 4.31 O ANISOU 2815 O ASP B 114 417 416 803 -152 -113 3 O ATOM 2816 CB ASP A 114 1.091 3.500 25.975 1.00 4.24 C ANISOU 2816 CB ASP B 114 385 650 573 -58 -2 174 C ATOM 2817 CG ASP A 114 2.081 3.922 27.035 1.00 5.72 C ANISOU 2817 CG ASP B 114 561 943 669 -178 199 58 C ATOM 2818 OD1 ASP A 114 3.322 3.732 26.865 1.00 5.23 O ANISOU 2818 OD1 ASP B 114 467 778 741 -192 86 135 O ATOM 2819 OD2 ASP A 114 1.672 4.469 28.090 1.00 9.40 O ANISOU 2819 OD2 ASP B 114 964 1601 1006 -95 198 -89 O ATOM 2820 N ALA A 115 2.904 3.783 23.639 1.00 3.39 N ANISOU 2820 N ALA B 115 393 477 417 16 -40 92 N ATOM 2821 CA ALA A 115 4.061 4.048 22.785 1.00 3.40 C ANISOU 2821 CA ALA B 115 518 361 411 -39 49 65 C ATOM 2822 C ALA A 115 5.370 4.106 23.552 1.00 3.15 C ANISOU 2822 C ALA B 115 387 315 491 -45 84 -48 C ATOM 2823 O ALA A 115 6.436 4.015 22.938 1.00 3.44 O ANISOU 2823 O ALA B 115 361 498 447 -40 80 -96 O ATOM 2824 CB ALA A 115 3.855 5.320 21.968 1.00 4.28 C ANISOU 2824 CB ALA B 115 671 434 519 -17 -89 30 C ATOM 2825 N SER A 116 5.315 4.312 24.876 1.00 3.92 N ANISOU 2825 N SER B 116 423 506 561 -94 92 -28 N ATOM 2826 CA SER A 116 6.520 4.398 25.708 1.00 4.07 C ANISOU 2826 CA SER B 116 463 522 561 -38 64 6 C ATOM 2827 C SER A 116 6.985 3.070 26.297 1.00 3.93 C ANISOU 2827 C SER B 116 413 503 575 -74 82 26 C ATOM 2828 O SER A 116 7.936 3.049 27.060 1.00 4.17 O ANISOU 2828 O SER B 116 396 616 570 -35 8 -1 O ATOM 2829 CB SER A 116 6.309 5.386 26.857 1.00 4.58 C ANISOU 2829 CB SER B 116 473 590 677 -89 0 -46 C ATOM 2830 OG SER A 116 5.565 4.809 27.902 1.00 5.13 O ANISOU 2830 OG SER B 116 596 728 623 14 164 -73 O ATOM 2831 N LYS A 117 6.334 1.972 25.911 1.00 4.42 N ANISOU 2831 N LYS B 117 488 523 667 25 -36 -6 N ATOM 2832 CA LYS A 117 6.715 0.652 26.420 1.00 5.93 C ANISOU 2832 CA LYS B 117 729 690 832 12 -98 53 C ATOM 2833 C LYS A 117 6.701 -0.334 25.250 1.00 6.28 C ANISOU 2833 C LYS B 117 826 673 887 -16 -185 -2 C ATOM 2834 O LYS A 117 5.905 -0.224 24.312 1.00 8.64 O ANISOU 2834 O LYS B 117 1070 869 1340 227 -485 -201 O ATOM 2835 CB LYS A 117 5.769 0.179 27.541 1.00 6.95 C ANISOU 2835 CB LYS B 117 880 732 1029 -9 -49 129 C ATOM 2836 CG LYS A 117 6.211 -1.088 28.303 1.00 11.82 C ANISOU 2836 CG LYS B 117 1450 1474 1568 -38 70 180 C ATOM 2837 CD LYS A 117 5.273 -1.520 29.440 1.00 13.65 C ANISOU 2837 CD LYS B 117 1744 1705 1737 -102 24 266 C ATOM 2838 CE LYS A 117 5.048 -0.457 30.497 1.00 13.94 C ANISOU 2838 CE LYS B 117 1817 1974 1502 -199 0 137 C ATOM 2839 NZ LYS A 117 3.886 -0.834 31.384 1.00 15.69 N ANISOU 2839 NZ LYS B 117 2039 2202 1719 -495 -101 128 N ATOM 2840 N BSER A 118 7.611 -1.291 25.283 0.70 5.44 N ANISOU 2840 N BSER B 118 683 596 785 -38 -162 -78 N ATOM 2841 CA BSER A 118 7.577 -2.395 24.334 0.70 5.48 C ANISOU 2841 CA BSER B 118 722 633 725 -32 -96 1 C ATOM 2842 C BSER A 118 7.879 -3.691 25.051 0.70 5.76 C ANISOU 2842 C BSER B 118 726 663 798 -33 -62 9 C ATOM 2843 O BSER A 118 8.293 -3.713 26.220 0.70 5.06 O ANISOU 2843 O BSER B 118 613 532 776 -85 -101 3 O ATOM 2844 CB BSER A 118 8.579 -2.163 23.216 0.70 5.80 C ANISOU 2844 CB BSER B 118 709 623 869 -12 -98 -63 C ATOM 2845 OG BSER A 118 9.883 -2.038 23.760 0.70 6.54 O ANISOU 2845 OG BSER B 118 838 742 901 -143 -145 55 O ATOM 2846 N ILE A 119 7.626 -4.784 24.346 1.00 5.25 N ANISOU 2846 N ILE B 119 725 534 736 20 -77 36 N ATOM 2847 CA ILE A 119 7.782 -6.116 24.946 1.00 6.10 C ANISOU 2847 CA ILE B 119 835 705 778 2 59 81 C ATOM 2848 C ILE A 119 8.371 -7.062 23.944 1.00 5.01 C ANISOU 2848 C ILE B 119 682 600 621 -55 4 61 C ATOM 2849 O ILE A 119 7.903 -7.144 22.816 1.00 4.74 O ANISOU 2849 O ILE B 119 787 614 398 93 41 24 O ATOM 2850 CB ILE A 119 6.399 -6.687 25.390 1.00 8.35 C ANISOU 2850 CB ILE B 119 1187 877 1107 16 299 98 C ATOM 2851 CG1 ILE A 119 5.592 -5.692 26.241 1.00 13.21 C ANISOU 2851 CG1 ILE B 119 1627 1570 1822 3 161 -114 C ATOM 2852 CG2 ILE A 119 6.565 -8.026 26.099 1.00 9.59 C ANISOU 2852 CG2 ILE B 119 1286 1118 1239 48 380 222 C ATOM 2853 CD1 ILE A 119 6.072 -5.510 27.629 1.00 16.06 C ANISOU 2853 CD1 ILE B 119 1843 2154 2102 -16 159 -178 C ATOM 2854 N PHE A 120 9.366 -7.833 24.378 1.00 4.90 N ANISOU 2854 N PHE B 120 718 567 574 3 37 -9 N ATOM 2855 CA PHE A 120 9.873 -8.936 23.604 1.00 5.14 C ANISOU 2855 CA PHE B 120 686 685 581 18 22 71 C ATOM 2856 C PHE A 120 9.225 -10.214 24.126 1.00 4.95 C ANISOU 2856 C PHE B 120 687 604 590 36 28 136 C ATOM 2857 O PHE A 120 9.332 -10.564 25.312 1.00 5.67 O ANISOU 2857 O PHE B 120 707 765 680 104 -31 43 O ATOM 2858 CB PHE A 120 11.395 -9.052 23.701 1.00 5.80 C ANISOU 2858 CB PHE B 120 732 735 734 -28 3 58 C ATOM 2859 CG PHE A 120 11.920 -10.219 22.938 1.00 6.38 C ANISOU 2859 CG PHE B 120 718 805 899 -51 55 -47 C ATOM 2860 CD1 PHE A 120 12.014 -10.171 21.564 1.00 9.04 C ANISOU 2860 CD1 PHE B 120 1339 947 1145 263 -33 -111 C ATOM 2861 CD2 PHE A 120 12.238 -11.395 23.589 1.00 7.55 C ANISOU 2861 CD2 PHE B 120 956 853 1058 36 196 -80 C ATOM 2862 CE1 PHE A 120 12.454 -11.273 20.848 1.00 10.70 C ANISOU 2862 CE1 PHE B 120 1318 1633 1111 169 -92 -292 C ATOM 2863 CE2 PHE A 120 12.677 -12.500 22.874 1.00 8.82 C ANISOU 2863 CE2 PHE B 120 951 1046 1352 -39 64 -37 C ATOM 2864 CZ PHE A 120 12.776 -12.428 21.500 1.00 10.09 C ANISOU 2864 CZ PHE B 120 1036 1345 1451 36 -47 -430 C ATOM 2865 N VAL A 121 8.577 -10.911 23.207 1.00 5.38 N ANISOU 2865 N VAL B 121 792 596 656 24 55 127 N ATOM 2866 CA VAL A 121 7.831 -12.125 23.498 1.00 6.19 C ANISOU 2866 CA VAL B 121 873 694 783 -41 105 147 C ATOM 2867 C VAL A 121 8.483 -13.319 22.785 1.00 5.82 C ANISOU 2867 C VAL B 121 790 579 842 -86 42 110 C ATOM 2868 O VAL A 121 8.393 -13.433 21.569 1.00 5.25 O ANISOU 2868 O VAL B 121 851 362 778 -15 97 95 O ATOM 2869 CB VAL A 121 6.370 -12.023 23.040 1.00 6.53 C ANISOU 2869 CB VAL B 121 893 639 946 -121 155 97 C ATOM 2870 CG1 VAL A 121 5.587 -13.243 23.541 1.00 8.00 C ANISOU 2870 CG1 VAL B 121 1005 774 1259 -129 197 172 C ATOM 2871 CG2 VAL A 121 5.718 -10.741 23.528 1.00 7.79 C ANISOU 2871 CG2 VAL B 121 965 853 1139 18 142 259 C ATOM 2872 N PRO A 122 9.141 -14.218 23.516 1.00 6.49 N ANISOU 2872 N PRO B 122 907 705 852 -93 45 88 N ATOM 2873 CA PRO A 122 9.733 -15.385 22.856 1.00 7.29 C ANISOU 2873 CA PRO B 122 952 827 989 10 2 46 C ATOM 2874 C PRO A 122 8.670 -16.282 22.234 1.00 6.91 C ANISOU 2874 C PRO B 122 942 696 988 4 71 47 C ATOM 2875 O PRO A 122 7.541 -16.398 22.729 1.00 6.88 O ANISOU 2875 O PRO B 122 902 546 1165 11 181 -76 O ATOM 2876 CB PRO A 122 10.454 -16.130 23.988 1.00 8.44 C ANISOU 2876 CB PRO B 122 1120 970 1117 35 -100 93 C ATOM 2877 CG PRO A 122 10.435 -15.240 25.165 1.00 9.24 C ANISOU 2877 CG PRO B 122 1188 1138 1182 140 -43 46 C ATOM 2878 CD PRO A 122 9.402 -14.194 24.965 1.00 6.98 C ANISOU 2878 CD PRO B 122 989 772 892 -11 31 86 C ATOM 2879 N ARG A 123 9.026 -16.899 21.123 1.00 6.72 N ANISOU 2879 N ARG B 123 800 701 1052 19 42 -64 N ATOM 2880 CA ARG A 123 8.183 -17.923 20.522 1.00 7.25 C ANISOU 2880 CA ARG B 123 884 784 1087 2 61 -79 C ATOM 2881 C ARG A 123 7.766 -18.950 21.584 1.00 7.27 C ANISOU 2881 C ARG B 123 800 792 1170 14 96 -91 C ATOM 2882 O ARG A 123 8.566 -19.340 22.444 1.00 6.43 O ANISOU 2882 O ARG B 123 637 549 1256 31 240 -93 O ATOM 2883 CB ARG A 123 8.911 -18.575 19.329 1.00 7.76 C ANISOU 2883 CB ARG B 123 970 809 1169 -12 99 -60 C ATOM 2884 CG ARG A 123 10.157 -19.390 19.634 1.00 10.11 C ANISOU 2884 CG ARG B 123 1264 1293 1283 -8 99 -56 C ATOM 2885 CD ARG A 123 10.898 -19.884 18.387 1.00 10.49 C ANISOU 2885 CD ARG B 123 1320 1359 1304 -35 84 -24 C ATOM 2886 NE ARG A 123 11.332 -18.776 17.541 1.00 10.46 N ANISOU 2886 NE ARG B 123 1427 1167 1377 133 154 82 N ATOM 2887 CZ ARG A 123 11.753 -18.876 16.278 1.00 12.05 C ANISOU 2887 CZ ARG B 123 1656 1336 1584 14 31 38 C ATOM 2888 NH1 ARG A 123 12.096 -17.770 15.613 1.00 13.39 N ANISOU 2888 NH1 ARG B 123 2014 1394 1679 -36 153 194 N ATOM 2889 NH2 ARG A 123 11.845 -20.052 15.679 1.00 13.01 N ANISOU 2889 NH2 ARG B 123 1770 1606 1567 -48 -15 74 N ATOM 2890 N GLY A 124 6.504 -19.375 21.521 1.00 7.63 N ANISOU 2890 N GLY B 124 848 842 1206 8 90 -120 N ATOM 2891 CA GLY A 124 5.922 -20.275 22.497 1.00 7.25 C ANISOU 2891 CA GLY B 124 844 785 1124 58 60 10 C ATOM 2892 C GLY A 124 5.228 -19.638 23.685 1.00 7.47 C ANISOU 2892 C GLY B 124 860 893 1083 43 46 32 C ATOM 2893 O GLY A 124 4.585 -20.341 24.455 1.00 6.54 O ANISOU 2893 O GLY B 124 616 471 1396 69 144 97 O ATOM 2894 N VAL A 125 5.342 -18.319 23.847 1.00 6.49 N ANISOU 2894 N VAL B 125 772 742 952 19 57 11 N ATOM 2895 CA VAL A 125 4.603 -17.582 24.860 1.00 6.19 C ANISOU 2895 CA VAL B 125 704 799 845 16 19 109 C ATOM 2896 C VAL A 125 3.384 -16.997 24.179 1.00 5.82 C ANISOU 2896 C VAL B 125 655 728 829 33 51 204 C ATOM 2897 O VAL A 125 3.487 -16.331 23.138 1.00 6.80 O ANISOU 2897 O VAL B 125 717 888 978 88 30 501 O ATOM 2898 CB VAL A 125 5.484 -16.484 25.511 1.00 5.72 C ANISOU 2898 CB VAL B 125 604 735 833 -10 66 151 C ATOM 2899 CG1 VAL A 125 4.673 -15.609 26.479 1.00 7.19 C ANISOU 2899 CG1 VAL B 125 885 991 856 100 -23 89 C ATOM 2900 CG2 VAL A 125 6.665 -17.132 26.242 1.00 6.83 C ANISOU 2900 CG2 VAL B 125 585 946 1063 -3 -37 37 C ATOM 2901 N ALA A 126 2.216 -17.290 24.730 1.00 4.90 N ANISOU 2901 N ALA B 126 608 593 659 34 -44 232 N ATOM 2902 CA ALA A 126 0.977 -16.786 24.153 1.00 5.18 C ANISOU 2902 CA ALA B 126 620 685 661 42 -18 86 C ATOM 2903 C ALA A 126 0.812 -15.300 24.434 1.00 5.73 C ANISOU 2903 C ALA B 126 706 764 707 28 -15 17 C ATOM 2904 O ALA A 126 1.081 -14.826 25.520 1.00 6.37 O ANISOU 2904 O ALA B 126 934 848 637 71 38 67 O ATOM 2905 CB ALA A 126 -0.233 -17.578 24.682 1.00 5.68 C ANISOU 2905 CB ALA B 126 669 735 753 52 -35 89 C ATOM 2906 N ASN A 127 0.346 -14.593 23.412 1.00 5.49 N ANISOU 2906 N ASN B 127 703 667 713 4 -4 68 N ATOM 2907 CA ASN A 127 0.201 -13.150 23.405 1.00 5.19 C ANISOU 2907 CA ASN B 127 699 613 661 19 16 132 C ATOM 2908 C ASN A 127 -1.240 -12.719 23.168 1.00 5.16 C ANISOU 2908 C ASN B 127 681 609 669 0 72 132 C ATOM 2909 O ASN A 127 -1.967 -13.314 22.376 1.00 5.08 O ANISOU 2909 O ASN B 127 680 560 690 112 4 119 O ATOM 2910 CB ASN A 127 1.059 -12.606 22.242 1.00 6.15 C ANISOU 2910 CB ASN B 127 821 698 817 0 189 100 C ATOM 2911 CG ASN A 127 0.959 -11.089 22.056 1.00 5.99 C ANISOU 2911 CG ASN B 127 816 767 692 7 162 192 C ATOM 2912 OD1 ASN A 127 1.466 -10.329 22.855 1.00 6.67 O ANISOU 2912 OD1 ASN B 127 1054 764 715 130 71 186 O ATOM 2913 ND2 ASN A 127 0.326 -10.667 20.975 1.00 8.65 N ANISOU 2913 ND2 ASN B 127 1093 1116 1074 122 82 166 N ATOM 2914 N GLY A 128 -1.635 -11.665 23.849 1.00 4.94 N ANISOU 2914 N GLY B 128 581 640 654 -8 -6 83 N ATOM 2915 CA GLY A 128 -2.939 -11.082 23.649 1.00 5.63 C ANISOU 2915 CA GLY B 128 698 728 712 5 -32 72 C ATOM 2916 C GLY A 128 -2.993 -9.670 24.161 1.00 5.08 C ANISOU 2916 C GLY B 128 672 640 618 -33 88 149 C ATOM 2917 O GLY A 128 -2.071 -9.182 24.786 1.00 4.36 O ANISOU 2917 O GLY B 128 500 631 525 57 96 175 O ATOM 2918 N PHE A 129 -4.108 -9.007 23.902 1.00 4.92 N ANISOU 2918 N PHE B 129 614 575 679 9 -7 83 N ATOM 2919 CA PHE A 129 -4.294 -7.630 24.365 1.00 5.87 C ANISOU 2919 CA PHE B 129 661 733 835 25 -35 -9 C ATOM 2920 C PHE A 129 -5.750 -7.259 24.397 1.00 5.22 C ANISOU 2920 C PHE B 129 548 730 703 -22 -37 1 C ATOM 2921 O PHE A 129 -6.559 -7.833 23.685 1.00 4.81 O ANISOU 2921 O PHE B 129 569 638 619 -63 -90 -216 O ATOM 2922 CB PHE A 129 -3.520 -6.632 23.498 1.00 6.37 C ANISOU 2922 CB PHE B 129 658 709 1053 68 -18 -49 C ATOM 2923 CG PHE A 129 -3.992 -6.548 22.049 1.00 6.87 C ANISOU 2923 CG PHE B 129 807 723 1079 24 193 111 C ATOM 2924 CD1 PHE A 129 -4.997 -5.653 21.670 1.00 7.57 C ANISOU 2924 CD1 PHE B 129 1012 830 1030 70 179 111 C ATOM 2925 CD2 PHE A 129 -3.413 -7.340 21.066 1.00 8.16 C ANISOU 2925 CD2 PHE B 129 839 935 1324 116 335 133 C ATOM 2926 CE1 PHE A 129 -5.401 -5.542 20.341 1.00 8.52 C ANISOU 2926 CE1 PHE B 129 1047 1095 1095 299 224 95 C ATOM 2927 CE2 PHE A 129 -3.815 -7.236 19.731 1.00 9.28 C ANISOU 2927 CE2 PHE B 129 1127 1057 1341 132 468 147 C ATOM 2928 CZ PHE A 129 -4.811 -6.344 19.372 1.00 9.62 C ANISOU 2928 CZ PHE B 129 1380 1214 1059 139 364 180 C ATOM 2929 N GLN A 130 -6.077 -6.289 25.238 1.00 5.17 N ANISOU 2929 N GLN B 130 519 686 759 5 -76 -59 N ATOM 2930 CA GLN A 130 -7.386 -5.654 25.213 1.00 5.25 C ANISOU 2930 CA GLN B 130 534 759 701 21 -17 -7 C ATOM 2931 C GLN A 130 -7.182 -4.165 25.058 1.00 4.65 C ANISOU 2931 C GLN B 130 468 685 612 -87 -46 20 C ATOM 2932 O GLN A 130 -6.337 -3.552 25.739 1.00 4.87 O ANISOU 2932 O GLN B 130 467 705 675 -92 -177 -6 O ATOM 2933 CB GLN A 130 -8.189 -5.937 26.495 1.00 5.75 C ANISOU 2933 CB GLN B 130 700 760 724 2 -79 -2 C ATOM 2934 CG GLN A 130 -9.588 -5.343 26.394 1.00 6.49 C ANISOU 2934 CG GLN B 130 902 705 858 -17 171 30 C ATOM 2935 CD GLN A 130 -10.546 -5.793 27.417 1.00 8.55 C ANISOU 2935 CD GLN B 130 1244 787 1216 163 -109 84 C ATOM 2936 OE1 GLN A 130 -10.174 -5.978 28.552 1.00 9.65 O ANISOU 2936 OE1 GLN B 130 1920 895 849 220 204 192 O ATOM 2937 NE2 GLN A 130 -11.799 -5.931 27.024 1.00 9.95 N ANISOU 2937 NE2 GLN B 130 1115 977 1686 73 101 -61 N ATOM 2938 N VAL A 131 -7.904 -3.560 24.131 1.00 3.95 N ANISOU 2938 N VAL B 131 428 538 531 -81 -39 -5 N ATOM 2939 CA VAL A 131 -7.714 -2.155 23.832 1.00 4.40 C ANISOU 2939 CA VAL B 131 511 655 504 -56 60 11 C ATOM 2940 C VAL A 131 -8.400 -1.283 24.897 1.00 4.42 C ANISOU 2940 C VAL B 131 512 692 473 -32 37 -40 C ATOM 2941 O VAL A 131 -9.604 -1.423 25.139 1.00 4.53 O ANISOU 2941 O VAL B 131 518 706 495 -27 60 -44 O ATOM 2942 CB VAL A 131 -8.266 -1.814 22.436 1.00 4.46 C ANISOU 2942 CB VAL B 131 518 680 495 -8 8 -62 C ATOM 2943 CG1 VAL A 131 -7.981 -0.375 22.093 1.00 5.51 C ANISOU 2943 CG1 VAL B 131 682 722 688 -142 36 -11 C ATOM 2944 CG2 VAL A 131 -7.661 -2.752 21.361 1.00 5.02 C ANISOU 2944 CG2 VAL B 131 614 784 507 -111 27 -6 C ATOM 2945 N LEU A 132 -7.631 -0.367 25.489 1.00 3.67 N ANISOU 2945 N LEU B 132 398 539 457 -8 154 -113 N ATOM 2946 CA LEU A 132 -8.106 0.507 26.576 1.00 3.99 C ANISOU 2946 CA LEU B 132 470 600 445 0 170 -86 C ATOM 2947 C LEU A 132 -8.487 1.900 26.109 1.00 4.19 C ANISOU 2947 C LEU B 132 519 502 570 -79 116 -117 C ATOM 2948 O LEU A 132 -9.341 2.539 26.679 1.00 5.97 O ANISOU 2948 O LEU B 132 1009 503 754 30 222 -160 O ATOM 2949 CB LEU A 132 -7.050 0.625 27.656 1.00 5.23 C ANISOU 2949 CB LEU B 132 764 724 499 -17 109 -81 C ATOM 2950 CG LEU A 132 -6.554 -0.694 28.241 1.00 5.32 C ANISOU 2950 CG LEU B 132 661 713 647 12 -101 -250 C ATOM 2951 CD1 LEU A 132 -5.413 -0.405 29.192 1.00 6.76 C ANISOU 2951 CD1 LEU B 132 887 877 802 63 -141 -104 C ATOM 2952 CD2 LEU A 132 -7.672 -1.426 28.933 1.00 7.88 C ANISOU 2952 CD2 LEU B 132 937 972 1085 17 67 52 C ATOM 2953 N SER A 133 -7.817 2.379 25.068 1.00 4.51 N ANISOU 2953 N SER B 133 581 533 599 -63 131 -77 N ATOM 2954 CA SER A 133 -8.077 3.687 24.471 1.00 4.74 C ANISOU 2954 CA SER B 133 605 621 572 -88 32 -102 C ATOM 2955 C SER A 133 -9.132 3.555 23.388 1.00 4.82 C ANISOU 2955 C SER B 133 502 571 758 -54 40 -115 C ATOM 2956 O SER A 133 -9.555 2.460 23.045 1.00 5.50 O ANISOU 2956 O SER B 133 613 504 973 -151 76 -201 O ATOM 2957 CB SER A 133 -6.780 4.226 23.878 1.00 4.28 C ANISOU 2957 CB SER B 133 578 574 474 -167 -94 -144 C ATOM 2958 OG SER A 133 -6.201 3.245 23.019 1.00 4.93 O ANISOU 2958 OG SER B 133 508 657 706 -238 219 -49 O ATOM 2959 N ASP A 134 -9.582 4.673 22.839 1.00 5.09 N ANISOU 2959 N ASP B 134 673 589 669 -33 31 -132 N ATOM 2960 CA ASP A 134 -10.599 4.613 21.817 1.00 5.52 C ANISOU 2960 CA ASP B 134 701 647 748 -28 59 -65 C ATOM 2961 C ASP A 134 -10.151 3.816 20.601 1.00 4.50 C ANISOU 2961 C ASP B 134 570 523 614 -3 102 -49 C ATOM 2962 O ASP A 134 -10.943 3.072 20.042 1.00 4.68 O ANISOU 2962 O ASP B 134 563 491 723 -177 122 -118 O ATOM 2963 CB ASP A 134 -11.041 6.008 21.432 1.00 6.95 C ANISOU 2963 CB ASP B 134 1018 744 875 -32 0 -6 C ATOM 2964 CG ASP A 134 -11.846 6.671 22.525 1.00 9.71 C ANISOU 2964 CG ASP B 134 1498 824 1365 -20 224 111 C ATOM 2965 OD1 ASP A 134 -12.460 5.971 23.382 1.00 11.68 O ANISOU 2965 OD1 ASP B 134 1642 736 2060 32 353 263 O ATOM 2966 OD2 ASP A 134 -11.929 7.902 22.613 1.00 17.31 O ANISOU 2966 OD2 ASP B 134 2759 1078 2737 -193 215 127 O ATOM 2967 N PHE A 135 -8.900 4.006 20.175 1.00 5.02 N ANISOU 2967 N PHE B 135 593 608 706 -105 106 -138 N ATOM 2968 CA PHE A 135 -8.246 3.184 19.153 1.00 4.68 C ANISOU 2968 CA PHE B 135 683 495 601 -107 50 -36 C ATOM 2969 C PHE A 135 -6.804 3.003 19.542 1.00 3.96 C ANISOU 2969 C PHE B 135 601 422 479 -155 113 -85 C ATOM 2970 O PHE A 135 -6.265 3.730 20.378 1.00 4.52 O ANISOU 2970 O PHE B 135 628 611 477 -236 147 -219 O ATOM 2971 CB PHE A 135 -8.323 3.805 17.758 1.00 5.50 C ANISOU 2971 CB PHE B 135 687 612 789 -81 60 29 C ATOM 2972 CG PHE A 135 -9.710 3.886 17.212 1.00 8.93 C ANISOU 2972 CG PHE B 135 1439 772 1181 -327 -62 332 C ATOM 2973 CD1 PHE A 135 -10.506 4.971 17.501 1.00 10.45 C ANISOU 2973 CD1 PHE B 135 1120 1324 1524 -56 -43 423 C ATOM 2974 CD2 PHE A 135 -10.232 2.874 16.424 1.00 13.52 C ANISOU 2974 CD2 PHE B 135 1901 1608 1627 -224 -253 278 C ATOM 2975 CE1 PHE A 135 -11.810 5.064 17.021 1.00 13.32 C ANISOU 2975 CE1 PHE B 135 1636 1517 1904 -16 -210 340 C ATOM 2976 CE2 PHE A 135 -11.541 2.967 15.911 1.00 12.04 C ANISOU 2976 CE2 PHE B 135 1568 1354 1650 -320 -167 413 C ATOM 2977 CZ PHE A 135 -12.317 4.057 16.225 1.00 14.11 C ANISOU 2977 CZ PHE B 135 1597 1822 1940 -183 -325 222 C ATOM 2978 N VAL A 136 -6.161 2.043 18.900 1.00 4.48 N ANISOU 2978 N VAL B 136 565 589 548 -133 50 -31 N ATOM 2979 CA VAL A 136 -4.731 1.848 19.079 1.00 4.88 C ANISOU 2979 CA VAL B 136 587 692 572 -100 39 10 C ATOM 2980 C VAL A 136 -4.134 1.270 17.807 1.00 4.40 C ANISOU 2980 C VAL B 136 600 587 484 -97 10 -36 C ATOM 2981 O VAL A 136 -4.747 0.442 17.128 1.00 4.53 O ANISOU 2981 O VAL B 136 588 720 410 -292 77 -18 O ATOM 2982 CB VAL A 136 -4.419 0.921 20.291 1.00 5.30 C ANISOU 2982 CB VAL B 136 662 800 549 -140 57 26 C ATOM 2983 CG1 VAL A 136 -4.895 -0.496 20.025 1.00 5.46 C ANISOU 2983 CG1 VAL B 136 679 734 658 -105 22 156 C ATOM 2984 CG2 VAL A 136 -2.936 0.952 20.646 1.00 5.57 C ANISOU 2984 CG2 VAL B 136 749 790 575 -61 74 56 C ATOM 2985 N ALA A 137 -2.913 1.702 17.527 1.00 4.13 N ANISOU 2985 N ALA B 137 554 563 453 -204 63 -63 N ATOM 2986 CA ALA A 137 -2.082 1.174 16.445 1.00 4.17 C ANISOU 2986 CA ALA B 137 591 516 477 -134 69 7 C ATOM 2987 C ALA A 137 -1.015 0.286 17.082 1.00 4.32 C ANISOU 2987 C ALA B 137 599 574 469 -214 18 35 C ATOM 2988 O ALA A 137 -0.065 0.758 17.710 1.00 5.78 O ANISOU 2988 O ALA B 137 817 554 825 -250 -199 24 O ATOM 2989 CB ALA A 137 -1.461 2.319 15.643 1.00 5.20 C ANISOU 2989 CB ALA B 137 764 532 680 -145 63 71 C ATOM 2990 N TYR A 138 -1.219 -1.006 16.950 1.00 4.53 N ANISOU 2990 N TYR B 138 548 619 552 -15 -32 21 N ATOM 2991 CA TYR A 138 -0.410 -2.038 17.595 1.00 4.57 C ANISOU 2991 CA TYR B 138 594 559 582 -70 -18 39 C ATOM 2992 C TYR A 138 0.545 -2.585 16.543 1.00 5.02 C ANISOU 2992 C TYR B 138 674 604 628 16 -70 -37 C ATOM 2993 O TYR A 138 0.121 -3.187 15.567 1.00 5.95 O ANISOU 2993 O TYR B 138 725 854 678 9 -53 -222 O ATOM 2994 CB TYR A 138 -1.390 -3.074 18.091 1.00 5.65 C ANISOU 2994 CB TYR B 138 749 658 740 -9 -30 4 C ATOM 2995 CG TYR A 138 -0.883 -4.258 18.852 1.00 6.08 C ANISOU 2995 CG TYR B 138 778 691 840 48 96 125 C ATOM 2996 CD1 TYR A 138 -0.784 -4.228 20.246 1.00 6.82 C ANISOU 2996 CD1 TYR B 138 905 849 837 160 72 -6 C ATOM 2997 CD2 TYR A 138 -0.587 -5.440 18.197 1.00 6.71 C ANISOU 2997 CD2 TYR B 138 1111 680 755 44 110 76 C ATOM 2998 CE1 TYR A 138 -0.413 -5.385 20.973 1.00 6.33 C ANISOU 2998 CE1 TYR B 138 953 640 810 110 168 93 C ATOM 2999 CE2 TYR A 138 -0.208 -6.578 18.893 1.00 6.20 C ANISOU 2999 CE2 TYR B 138 978 614 763 8 121 115 C ATOM 3000 CZ TYR A 138 -0.135 -6.545 20.279 1.00 6.20 C ANISOU 3000 CZ TYR B 138 892 631 833 131 132 255 C ATOM 3001 OH TYR A 138 0.227 -7.678 20.975 1.00 7.20 O ANISOU 3001 OH TYR B 138 1130 636 970 216 221 349 O ATOM 3002 N SER A 139 1.834 -2.294 16.693 1.00 5.28 N ANISOU 3002 N SER B 139 655 748 602 45 -88 -171 N ATOM 3003 CA SER A 139 2.835 -2.540 15.658 1.00 5.93 C ANISOU 3003 CA SER B 139 711 807 734 91 -42 -60 C ATOM 3004 C SER A 139 3.891 -3.474 16.187 1.00 6.50 C ANISOU 3004 C SER B 139 814 857 797 109 -25 -18 C ATOM 3005 O SER A 139 4.514 -3.169 17.204 1.00 6.46 O ANISOU 3005 O SER B 139 785 885 784 20 -58 -67 O ATOM 3006 CB SER A 139 3.482 -1.217 15.224 1.00 6.28 C ANISOU 3006 CB SER B 139 741 845 801 17 41 -129 C ATOM 3007 OG SER A 139 4.432 -1.405 14.174 1.00 7.27 O ANISOU 3007 OG SER B 139 970 834 956 -119 118 -111 O ATOM 3008 N TYR A 140 4.124 -4.579 15.500 1.00 6.17 N ANISOU 3008 N TYR B 140 727 894 722 217 -48 -7 N ATOM 3009 CA TYR A 140 5.082 -5.550 16.012 1.00 6.22 C ANISOU 3009 CA TYR B 140 822 812 729 142 -57 80 C ATOM 3010 C TYR A 140 5.975 -6.103 14.927 1.00 5.68 C ANISOU 3010 C TYR B 140 757 751 650 77 -49 36 C ATOM 3011 O TYR A 140 5.640 -6.082 13.739 1.00 5.59 O ANISOU 3011 O TYR B 140 743 760 619 114 -48 101 O ATOM 3012 CB TYR A 140 4.384 -6.637 16.827 1.00 6.59 C ANISOU 3012 CB TYR B 140 867 824 812 171 39 35 C ATOM 3013 CG TYR A 140 3.377 -7.509 16.105 1.00 7.79 C ANISOU 3013 CG TYR B 140 949 978 1030 125 80 97 C ATOM 3014 CD1 TYR A 140 3.758 -8.737 15.595 1.00 9.48 C ANISOU 3014 CD1 TYR B 140 1284 1117 1200 -2 -47 -15 C ATOM 3015 CD2 TYR A 140 2.031 -7.125 15.966 1.00 7.55 C ANISOU 3015 CD2 TYR B 140 1055 1091 720 25 147 -8 C ATOM 3016 CE1 TYR A 140 2.862 -9.563 14.958 1.00 10.52 C ANISOU 3016 CE1 TYR B 140 1526 1118 1351 -125 -120 81 C ATOM 3017 CE2 TYR A 140 1.117 -7.955 15.330 1.00 9.85 C ANISOU 3017 CE2 TYR B 140 1084 1483 1174 -26 63 63 C ATOM 3018 CZ TYR A 140 1.557 -9.180 14.844 1.00 9.26 C ANISOU 3018 CZ TYR B 140 1277 1093 1147 -303 -38 164 C ATOM 3019 OH TYR A 140 0.709 -10.027 14.192 1.00 12.38 O ANISOU 3019 OH TYR B 140 1739 1392 1570 -448 -254 25 O ATOM 3020 N LEU A 141 7.166 -6.514 15.340 1.00 5.10 N ANISOU 3020 N LEU B 141 725 627 586 117 10 18 N ATOM 3021 CA LEU A 141 8.159 -7.107 14.458 1.00 5.44 C ANISOU 3021 CA LEU B 141 759 671 636 148 -91 35 C ATOM 3022 C LEU A 141 8.258 -8.579 14.787 1.00 5.13 C ANISOU 3022 C LEU B 141 825 557 565 137 -91 103 C ATOM 3023 O LEU A 141 8.281 -8.954 15.953 1.00 6.61 O ANISOU 3023 O LEU B 141 1358 652 499 273 -13 -5 O ATOM 3024 CB LEU A 141 9.532 -6.462 14.700 1.00 6.12 C ANISOU 3024 CB LEU B 141 870 758 695 63 -151 44 C ATOM 3025 CG LEU A 141 9.664 -4.944 14.543 1.00 8.06 C ANISOU 3025 CG LEU B 141 899 1088 1075 -15 -95 -94 C ATOM 3026 CD1 LEU A 141 11.102 -4.524 14.818 1.00 9.94 C ANISOU 3026 CD1 LEU B 141 1226 1418 1133 -306 -133 52 C ATOM 3027 CD2 LEU A 141 9.197 -4.509 13.182 1.00 8.93 C ANISOU 3027 CD2 LEU B 141 1141 985 1264 -79 -49 35 C ATOM 3028 N VAL A 142 8.333 -9.411 13.753 1.00 4.92 N ANISOU 3028 N VAL B 142 821 524 523 96 -62 74 N ATOM 3029 CA VAL A 142 8.526 -10.847 13.936 1.00 5.00 C ANISOU 3029 CA VAL B 142 683 549 667 55 -46 21 C ATOM 3030 C VAL A 142 9.669 -11.325 13.049 1.00 4.35 C ANISOU 3030 C VAL B 142 644 491 517 29 -85 35 C ATOM 3031 O VAL A 142 10.097 -10.635 12.109 1.00 4.06 O ANISOU 3031 O VAL B 142 609 483 449 66 -58 58 O ATOM 3032 CB VAL A 142 7.245 -11.660 13.643 1.00 5.98 C ANISOU 3032 CB VAL B 142 737 656 878 48 -4 31 C ATOM 3033 CG1 VAL A 142 6.083 -11.137 14.471 1.00 8.27 C ANISOU 3033 CG1 VAL B 142 955 987 1200 -13 43 -112 C ATOM 3034 CG2 VAL A 142 6.864 -11.643 12.158 1.00 6.86 C ANISOU 3034 CG2 VAL B 142 821 709 1075 46 -36 -37 C ATOM 3035 N ASN A 143 10.169 -12.508 13.367 1.00 3.93 N ANISOU 3035 N ASN B 143 550 364 577 -13 -25 60 N ATOM 3036 CA ASN A 143 11.368 -13.061 12.736 1.00 3.54 C ANISOU 3036 CA ASN B 143 503 376 463 21 -38 -17 C ATOM 3037 C ASN A 143 11.167 -14.409 12.045 1.00 3.31 C ANISOU 3037 C ASN B 143 473 360 423 -67 -58 33 C ATOM 3038 O ASN A 143 12.105 -15.152 11.874 1.00 3.84 O ANISOU 3038 O ASN B 143 556 503 400 43 -100 100 O ATOM 3039 CB ASN A 143 12.535 -13.159 13.736 1.00 3.85 C ANISOU 3039 CB ASN B 143 494 487 479 -8 -32 -26 C ATOM 3040 CG ASN A 143 12.274 -14.127 14.847 1.00 3.61 C ANISOU 3040 CG ASN B 143 482 278 611 50 -11 -19 C ATOM 3041 OD1 ASN A 143 11.146 -14.595 15.041 1.00 4.20 O ANISOU 3041 OD1 ASN B 143 575 535 485 -29 -39 9 O ATOM 3042 ND2 ASN A 143 13.335 -14.461 15.595 1.00 4.37 N ANISOU 3042 ND2 ASN B 143 400 662 596 2 -128 62 N ATOM 3043 N ASP A 144 9.955 -14.676 11.602 1.00 3.99 N ANISOU 3043 N ASP B 144 476 555 485 59 -94 1 N ATOM 3044 CA ASP A 144 9.698 -15.789 10.698 1.00 3.64 C ANISOU 3044 CA ASP B 144 509 461 412 22 -86 67 C ATOM 3045 C ASP A 144 8.387 -15.519 9.969 1.00 3.14 C ANISOU 3045 C ASP B 144 456 362 375 -8 -44 112 C ATOM 3046 O ASP A 144 7.660 -14.620 10.343 1.00 3.47 O ANISOU 3046 O ASP B 144 483 483 351 16 -82 36 O ATOM 3047 CB ASP A 144 9.671 -17.116 11.471 1.00 3.73 C ANISOU 3047 CB ASP B 144 563 311 541 95 -27 -50 C ATOM 3048 CG ASP A 144 10.178 -18.306 10.658 1.00 3.81 C ANISOU 3048 CG ASP B 144 484 373 588 93 -187 24 C ATOM 3049 OD1 ASP A 144 10.274 -18.231 9.411 1.00 4.45 O ANISOU 3049 OD1 ASP B 144 536 295 859 75 -14 -118 O ATOM 3050 OD2 ASP A 144 10.484 -19.374 11.232 1.00 7.80 O ANISOU 3050 OD2 ASP B 144 1174 1036 751 -129 161 318 O ATOM 3051 N TYR A 145 8.119 -16.308 8.936 1.00 2.96 N ANISOU 3051 N TYR B 145 394 354 374 -11 0 31 N ATOM 3052 CA TYR A 145 6.968 -16.154 8.066 1.00 3.74 C ANISOU 3052 CA TYR B 145 481 465 472 15 -46 132 C ATOM 3053 C TYR A 145 6.118 -17.397 8.123 1.00 4.54 C ANISOU 3053 C TYR B 145 501 617 605 -16 -74 122 C ATOM 3054 O TYR A 145 6.609 -18.501 8.376 1.00 4.51 O ANISOU 3054 O TYR B 145 434 553 725 -89 -249 305 O ATOM 3055 CB TYR A 145 7.429 -15.967 6.613 1.00 3.98 C ANISOU 3055 CB TYR B 145 505 534 473 -6 -21 117 C ATOM 3056 CG TYR A 145 8.618 -15.029 6.462 1.00 3.51 C ANISOU 3056 CG TYR B 145 648 285 400 -113 -240 68 C ATOM 3057 CD1 TYR A 145 9.828 -15.490 5.961 1.00 4.08 C ANISOU 3057 CD1 TYR B 145 782 355 413 -226 -211 69 C ATOM 3058 CD2 TYR A 145 8.536 -13.678 6.825 1.00 4.02 C ANISOU 3058 CD2 TYR B 145 880 347 299 131 -92 13 C ATOM 3059 CE1 TYR A 145 10.914 -14.650 5.820 1.00 4.49 C ANISOU 3059 CE1 TYR B 145 620 440 645 -6 -54 191 C ATOM 3060 CE2 TYR A 145 9.618 -12.854 6.674 1.00 4.91 C ANISOU 3060 CE2 TYR B 145 1066 453 345 220 -132 26 C ATOM 3061 CZ TYR A 145 10.799 -13.323 6.180 1.00 4.21 C ANISOU 3061 CZ TYR B 145 748 407 442 -144 -208 167 C ATOM 3062 OH TYR A 145 11.873 -12.465 6.039 1.00 4.64 O ANISOU 3062 OH TYR B 145 892 355 514 -89 -72 161 O ATOM 3063 N TRP A 146 4.843 -17.248 7.826 1.00 5.17 N ANISOU 3063 N TRP B 146 595 723 645 -38 -100 222 N ATOM 3064 CA TRP A 146 3.976 -18.403 7.735 1.00 5.84 C ANISOU 3064 CA TRP B 146 639 820 757 -79 -68 158 C ATOM 3065 C TRP A 146 4.518 -19.453 6.779 1.00 5.91 C ANISOU 3065 C TRP B 146 580 810 853 -103 -144 122 C ATOM 3066 O TRP A 146 4.964 -19.153 5.679 1.00 5.42 O ANISOU 3066 O TRP B 146 640 686 732 -40 -136 104 O ATOM 3067 CB TRP A 146 2.566 -18.009 7.262 1.00 6.91 C ANISOU 3067 CB TRP B 146 712 1065 845 -111 -111 139 C ATOM 3068 CG TRP A 146 1.626 -19.211 7.185 1.00 10.13 C ANISOU 3068 CG TRP B 146 1072 1677 1099 -201 -43 329 C ATOM 3069 CD1 TRP A 146 0.825 -19.674 8.182 1.00 14.86 C ANISOU 3069 CD1 TRP B 146 1743 2264 1640 -112 62 362 C ATOM 3070 CD2 TRP A 146 1.440 -20.117 6.075 1.00 8.68 C ANISOU 3070 CD2 TRP B 146 767 1327 1202 -381 -227 394 C ATOM 3071 NE1 TRP A 146 0.136 -20.783 7.762 1.00 14.58 N ANISOU 3071 NE1 TRP B 146 1762 2382 1395 -218 -33 238 N ATOM 3072 CE2 TRP A 146 0.509 -21.093 6.480 1.00 12.79 C ANISOU 3072 CE2 TRP B 146 1453 1940 1464 -150 -136 293 C ATOM 3073 CE3 TRP A 146 1.973 -20.203 4.781 1.00 9.22 C ANISOU 3073 CE3 TRP B 146 942 1208 1352 -102 -246 142 C ATOM 3074 CZ2 TRP A 146 0.073 -22.113 5.636 1.00 12.33 C ANISOU 3074 CZ2 TRP B 146 1433 1864 1387 -81 -215 316 C ATOM 3075 CZ3 TRP A 146 1.551 -21.226 3.944 1.00 10.59 C ANISOU 3075 CZ3 TRP B 146 1284 1395 1344 -36 -101 209 C ATOM 3076 CH2 TRP A 146 0.619 -22.177 4.380 1.00 10.89 C ANISOU 3076 CH2 TRP B 146 1219 1470 1446 -35 -64 160 C ATOM 3077 N ALA A 147 4.450 -20.702 7.211 1.00 6.78 N ANISOU 3077 N ALA B 147 731 926 917 -73 -172 165 N ATOM 3078 CA ALA A 147 4.719 -21.828 6.354 1.00 7.75 C ANISOU 3078 CA ALA B 147 861 1057 1026 -34 -89 118 C ATOM 3079 C ALA A 147 3.925 -22.960 6.924 1.00 8.47 C ANISOU 3079 C ALA B 147 1008 1138 1073 -12 -77 158 C ATOM 3080 O ALA A 147 3.743 -23.058 8.144 1.00 7.69 O ANISOU 3080 O ALA B 147 906 1090 925 -97 -221 187 O ATOM 3081 CB ALA A 147 6.188 -22.168 6.347 1.00 8.34 C ANISOU 3081 CB ALA B 147 840 1195 1134 -55 -102 151 C ATOM 3082 N LEU A 148 3.425 -23.787 6.033 1.00 8.85 N ANISOU 3082 N LEU B 148 1043 1227 1092 -117 -103 86 N ATOM 3083 CA LEU A 148 2.612 -24.908 6.439 1.00 9.80 C ANISOU 3083 CA LEU B 148 1228 1260 1233 -112 -4 17 C ATOM 3084 C LEU A 148 3.337 -25.663 7.577 1.00 9.50 C ANISOU 3084 C LEU B 148 1178 1199 1231 -114 -44 -18 C ATOM 3085 O LEU A 148 2.738 -26.054 8.566 1.00 11.92 O ANISOU 3085 O LEU B 148 1410 1924 1195 139 145 137 O ATOM 3086 CB LEU A 148 2.320 -25.827 5.230 1.00 10.62 C ANISOU 3086 CB LEU B 148 1349 1413 1273 -127 -22 18 C ATOM 3087 CG LEU A 148 0.879 -26.108 4.812 1.00 13.16 C ANISOU 3087 CG LEU B 148 1685 1753 1561 -72 -6 20 C ATOM 3088 CD1 LEU A 148 0.878 -27.281 3.868 1.00 14.36 C ANISOU 3088 CD1 LEU B 148 1879 1925 1652 -101 -66 -12 C ATOM 3089 CD2 LEU A 148 -0.042 -26.365 5.981 1.00 13.16 C ANISOU 3089 CD2 LEU B 148 1560 1817 1623 -174 -86 27 C ATOM 3090 N GLU A 149 4.637 -25.885 7.396 1.00 9.89 N ANISOU 3090 N GLU B 149 1312 1195 1248 -71 -21 -28 N ATOM 3091 CA GLU A 149 5.383 -26.811 8.257 1.00 11.05 C ANISOU 3091 CA GLU B 149 1347 1443 1405 -10 -19 12 C ATOM 3092 C GLU A 149 5.495 -26.288 9.676 1.00 9.76 C ANISOU 3092 C GLU B 149 1258 1134 1314 -27 -39 16 C ATOM 3093 O GLU A 149 5.858 -27.011 10.585 1.00 10.02 O ANISOU 3093 O GLU B 149 1242 1219 1345 -66 -33 112 O ATOM 3094 CB GLU A 149 6.780 -27.083 7.688 1.00 11.78 C ANISOU 3094 CB GLU B 149 1463 1510 1502 32 -1 -4 C ATOM 3095 CG GLU A 149 7.670 -25.856 7.676 1.00 16.33 C ANISOU 3095 CG GLU B 149 2004 2122 2079 63 67 68 C ATOM 3096 CD GLU A 149 8.590 -25.805 6.472 1.00 21.52 C ANISOU 3096 CD GLU B 149 2720 2665 2790 165 133 80 C ATOM 3097 OE1 GLU A 149 9.182 -26.851 6.134 1.00 24.35 O ANISOU 3097 OE1 GLU B 149 3108 3043 3099 310 185 6 O ATOM 3098 OE2 GLU A 149 8.727 -24.709 5.874 1.00 25.08 O ANISOU 3098 OE2 GLU B 149 3127 3003 3396 293 246 383 O ATOM 3099 N LEU A 150 5.202 -25.007 9.862 1.00 8.98 N ANISOU 3099 N LEU B 150 1136 1057 1218 -19 -33 41 N ATOM 3100 CA LEU A 150 5.211 -24.437 11.194 1.00 9.29 C ANISOU 3100 CA LEU B 150 1195 1091 1241 -7 -26 50 C ATOM 3101 C LEU A 150 3.897 -24.649 11.960 1.00 9.63 C ANISOU 3101 C LEU B 150 1251 1125 1283 -58 -32 -18 C ATOM 3102 O LEU A 150 3.822 -24.314 13.123 1.00 9.55 O ANISOU 3102 O LEU B 150 1227 1177 1224 -27 -35 78 O ATOM 3103 CB LEU A 150 5.524 -22.940 11.103 1.00 9.16 C ANISOU 3103 CB LEU B 150 1242 1019 1218 -16 -41 52 C ATOM 3104 CG LEU A 150 6.955 -22.439 11.270 1.00 10.72 C ANISOU 3104 CG LEU B 150 1351 1333 1387 25 53 118 C ATOM 3105 CD1 LEU A 150 8.088 -23.339 10.858 1.00 9.79 C ANISOU 3105 CD1 LEU B 150 1274 1168 1278 -30 -67 0 C ATOM 3106 CD2 LEU A 150 7.076 -21.100 10.555 1.00 7.64 C ANISOU 3106 CD2 LEU B 150 1172 401 1329 -249 16 -7 C ATOM 3107 N LYS A 151 2.881 -25.246 11.333 1.00 11.11 N ANISOU 3107 N LYS B 151 1394 1406 1419 -87 -28 -35 N ATOM 3108 CA LYS A 151 1.586 -25.449 11.988 1.00 12.77 C ANISOU 3108 CA LYS B 151 1607 1641 1604 -42 8 -34 C ATOM 3109 C LYS A 151 1.679 -26.038 13.413 1.00 12.90 C ANISOU 3109 C LYS B 151 1633 1638 1630 -50 45 -37 C ATOM 3110 O LYS A 151 0.952 -25.586 14.290 1.00 13.19 O ANISOU 3110 O LYS B 151 1695 1694 1621 -133 119 -81 O ATOM 3111 CB LYS A 151 0.667 -26.324 11.113 1.00 13.64 C ANISOU 3111 CB LYS B 151 1655 1801 1727 -54 30 19 C ATOM 3112 CG LYS A 151 -0.788 -26.406 11.601 1.00 16.92 C ANISOU 3112 CG LYS B 151 2070 2231 2126 -30 19 -10 C ATOM 3113 CD LYS A 151 -1.677 -27.200 10.639 1.00 20.88 C ANISOU 3113 CD LYS B 151 2520 2765 2647 3 11 0 C ATOM 3114 CE LYS A 151 -3.110 -27.333 11.170 1.00 22.94 C ANISOU 3114 CE LYS B 151 2809 3005 2901 9 30 49 C ATOM 3115 NZ LYS A 151 -3.816 -28.544 10.629 1.00 24.33 N ANISOU 3115 NZ LYS B 151 3212 3188 2843 9 -62 53 N ATOM 3116 N PRO A 152 2.537 -27.037 13.651 1.00 13.28 N ANISOU 3116 N PRO B 152 1736 1653 1656 -35 53 -25 N ATOM 3117 CA PRO A 152 2.718 -27.594 15.007 1.00 13.20 C ANISOU 3117 CA PRO B 152 1736 1617 1660 -17 13 -33 C ATOM 3118 C PRO A 152 3.352 -26.648 16.051 1.00 13.23 C ANISOU 3118 C PRO B 152 1726 1675 1625 -21 21 -25 C ATOM 3119 O PRO A 152 3.289 -26.938 17.246 1.00 13.98 O ANISOU 3119 O PRO B 152 1924 1759 1626 54 -10 -37 O ATOM 3120 CB PRO A 152 3.637 -28.806 14.764 1.00 13.55 C ANISOU 3120 CB PRO B 152 1785 1672 1690 -17 33 -7 C ATOM 3121 CG PRO A 152 3.496 -29.091 13.317 1.00 13.98 C ANISOU 3121 CG PRO B 152 1858 1731 1722 -8 61 -32 C ATOM 3122 CD PRO A 152 3.367 -27.760 12.668 1.00 13.47 C ANISOU 3122 CD PRO B 152 1775 1653 1689 -22 70 -13 C ATOM 3123 N LYS A 153 3.979 -25.568 15.608 1.00 12.52 N ANISOU 3123 N LYS B 153 1638 1536 1582 31 2 -29 N ATOM 3124 CA LYS A 153 4.545 -24.577 16.519 1.00 12.66 C ANISOU 3124 CA LYS B 153 1567 1661 1580 -6 -4 -42 C ATOM 3125 C LYS A 153 3.486 -23.620 17.105 1.00 11.86 C ANISOU 3125 C LYS B 153 1475 1521 1509 9 7 -87 C ATOM 3126 O LYS A 153 3.791 -22.872 18.024 1.00 12.51 O ANISOU 3126 O LYS B 153 1464 1815 1473 80 -1 -224 O ATOM 3127 CB LYS A 153 5.660 -23.778 15.822 1.00 13.35 C ANISOU 3127 CB LYS B 153 1668 1759 1645 2 2 -60 C ATOM 3128 CG LYS A 153 6.822 -24.626 15.290 1.00 14.12 C ANISOU 3128 CG LYS B 153 1727 1843 1795 -52 -30 -40 C ATOM 3129 CD LYS A 153 8.091 -23.785 15.167 1.00 16.43 C ANISOU 3129 CD LYS B 153 2040 2141 2060 23 -55 0 C ATOM 3130 CE LYS A 153 9.186 -24.450 14.325 1.00 16.98 C ANISOU 3130 CE LYS B 153 2132 2174 2146 -9 -55 -49 C ATOM 3131 NZ LYS A 153 10.317 -23.479 14.048 1.00 17.29 N ANISOU 3131 NZ LYS B 153 2192 2145 2231 83 -208 -25 N ATOM 3132 N TYR A 154 2.252 -23.633 16.594 1.00 10.55 N ANISOU 3132 N TYR B 154 1287 1364 1354 -38 26 -93 N ATOM 3133 CA TYR A 154 1.205 -22.786 17.170 1.00 9.56 C ANISOU 3133 CA TYR B 154 1187 1135 1308 -58 42 -44 C ATOM 3134 C TYR A 154 0.557 -23.452 18.370 1.00 9.16 C ANISOU 3134 C TYR B 154 1095 1102 1284 -106 83 -71 C ATOM 3135 O TYR A 154 0.275 -24.654 18.341 1.00 10.46 O ANISOU 3135 O TYR B 154 1389 1149 1435 -167 176 -160 O ATOM 3136 CB TYR A 154 0.078 -22.519 16.183 1.00 9.40 C ANISOU 3136 CB TYR B 154 1142 1154 1272 -110 68 -35 C ATOM 3137 CG TYR A 154 0.383 -21.629 15.013 1.00 9.55 C ANISOU 3137 CG TYR B 154 1069 1143 1416 -108 -26 42 C ATOM 3138 CD1 TYR A 154 1.076 -22.120 13.923 1.00 9.42 C ANISOU 3138 CD1 TYR B 154 1232 1020 1327 -142 72 -49 C ATOM 3139 CD2 TYR A 154 -0.079 -20.310 14.966 1.00 11.00 C ANISOU 3139 CD2 TYR B 154 1234 1401 1544 -67 95 50 C ATOM 3140 CE1 TYR A 154 1.320 -21.333 12.815 1.00 11.20 C ANISOU 3140 CE1 TYR B 154 1288 1440 1528 -237 35 -29 C ATOM 3141 CE2 TYR A 154 0.162 -19.511 13.872 1.00 11.48 C ANISOU 3141 CE2 TYR B 154 1282 1380 1698 -237 -28 64 C ATOM 3142 CZ TYR A 154 0.858 -20.031 12.790 1.00 11.07 C ANISOU 3142 CZ TYR B 154 1184 1399 1620 -299 39 75 C ATOM 3143 OH TYR A 154 1.089 -19.255 11.679 1.00 13.75 O ANISOU 3143 OH TYR B 154 1689 1702 1831 -551 -216 171 O ATOM 3144 N ALA A 155 0.285 -22.662 19.401 1.00 8.70 N ANISOU 3144 N ALA B 155 1017 1077 1210 -113 107 -19 N ATOM 3145 CA ALA A 155 -0.642 -23.052 20.453 1.00 8.28 C ANISOU 3145 CA ALA B 155 1052 973 1121 -38 74 -4 C ATOM 3146 C ALA A 155 -1.557 -21.875 20.801 1.00 7.76 C ANISOU 3146 C ALA B 155 912 968 1066 -18 41 -1 C ATOM 3147 O ALA A 155 -1.213 -20.730 20.582 1.00 8.05 O ANISOU 3147 O ALA B 155 1118 823 1118 8 212 2 O ATOM 3148 CB ALA A 155 0.123 -23.533 21.674 1.00 8.88 C ANISOU 3148 CB ALA B 155 1119 1067 1185 2 82 -26 C ATOM 3149 N PHE A 156 -2.723 -22.181 21.348 1.00 7.18 N ANISOU 3149 N PHE B 156 917 765 1047 -57 100 64 N ATOM 3150 CA PHE A 156 -3.728 -21.179 21.698 1.00 7.62 C ANISOU 3150 CA PHE B 156 944 903 1048 1 73 49 C ATOM 3151 C PHE A 156 -4.301 -21.479 23.058 1.00 7.09 C ANISOU 3151 C PHE B 156 858 890 942 34 98 49 C ATOM 3152 O PHE A 156 -4.492 -22.641 23.392 1.00 6.98 O ANISOU 3152 O PHE B 156 1023 539 1088 -2 153 261 O ATOM 3153 CB PHE A 156 -4.889 -21.209 20.709 1.00 8.65 C ANISOU 3153 CB PHE B 156 1056 1082 1148 29 96 37 C ATOM 3154 CG PHE A 156 -4.486 -21.041 19.290 1.00 10.59 C ANISOU 3154 CG PHE B 156 1392 1358 1271 96 133 57 C ATOM 3155 CD1 PHE A 156 -4.138 -22.131 18.515 1.00 11.29 C ANISOU 3155 CD1 PHE B 156 1478 1422 1387 -56 82 79 C ATOM 3156 CD2 PHE A 156 -4.473 -19.778 18.712 1.00 13.24 C ANISOU 3156 CD2 PHE B 156 1956 1664 1408 135 244 43 C ATOM 3157 CE1 PHE A 156 -3.765 -21.969 17.189 1.00 13.72 C ANISOU 3157 CE1 PHE B 156 1656 1895 1661 68 35 -52 C ATOM 3158 CE2 PHE A 156 -4.109 -19.610 17.386 1.00 14.63 C ANISOU 3158 CE2 PHE B 156 2130 1847 1580 124 154 211 C ATOM 3159 CZ PHE A 156 -3.751 -20.709 16.624 1.00 13.90 C ANISOU 3159 CZ PHE B 156 1884 1861 1536 122 137 41 C ATOM 3160 N VAL A 157 -4.629 -20.462 23.829 1.00 5.95 N ANISOU 3160 N VAL B 157 758 737 764 -16 59 153 N ATOM 3161 CA VAL A 157 -5.352 -20.670 25.076 1.00 5.53 C ANISOU 3161 CA VAL B 157 651 778 673 -2 55 53 C ATOM 3162 C VAL A 157 -6.429 -19.612 25.220 1.00 5.51 C ANISOU 3162 C VAL B 157 599 863 632 53 -8 77 C ATOM 3163 O VAL A 157 -6.310 -18.501 24.852 1.00 5.42 O ANISOU 3163 O VAL B 157 579 963 515 250 -39 -11 O ATOM 3164 CB VAL A 157 -4.414 -20.742 26.321 1.00 5.99 C ANISOU 3164 CB VAL B 157 645 854 775 1 -44 22 C ATOM 3165 CG1 VAL A 157 -3.712 -19.437 26.569 1.00 6.23 C ANISOU 3165 CG1 VAL B 157 703 861 801 -27 -43 50 C ATOM 3166 CG2 VAL A 157 -5.181 -21.183 27.582 1.00 6.78 C ANISOU 3166 CG2 VAL B 157 768 1033 774 102 -54 -141 C ATOM 3167 N ASN A 158 -7.553 -20.016 25.758 1.00 4.40 N ANISOU 3167 N ASN B 158 484 701 484 -174 124 134 N ATOM 3168 CA ASN A 158 -8.667 -19.123 25.856 1.00 6.03 C ANISOU 3168 CA ASN B 158 835 852 603 22 -45 17 C ATOM 3169 C ASN A 158 -8.470 -17.983 26.834 1.00 5.24 C ANISOU 3169 C ASN B 158 701 727 562 17 27 87 C ATOM 3170 O ASN A 158 -8.054 -18.156 27.987 1.00 6.83 O ANISOU 3170 O ASN B 158 854 1097 644 146 -245 -287 O ATOM 3171 CB ASN A 158 -9.848 -19.931 26.322 1.00 5.66 C ANISOU 3171 CB ASN B 158 730 815 604 -94 43 30 C ATOM 3172 CG ASN A 158 -11.112 -19.249 26.067 1.00 8.81 C ANISOU 3172 CG ASN B 158 1132 1419 796 347 9 -146 C ATOM 3173 OD1 ASN A 158 -11.480 -18.300 26.754 1.00 9.14 O ANISOU 3173 OD1 ASN B 158 1213 1642 616 280 -273 -409 O ATOM 3174 ND2 ASN A 158 -11.889 -19.806 25.092 1.00 7.78 N ANISOU 3174 ND2 ASN B 158 930 1590 436 98 -351 -78 N ATOM 3175 N TYR A 159 -8.801 -16.798 26.355 1.00 5.05 N ANISOU 3175 N TYR B 159 627 825 465 -59 40 10 N ATOM 3176 CA TYR A 159 -8.654 -15.580 27.116 1.00 5.93 C ANISOU 3176 CA TYR B 159 752 868 630 -33 100 30 C ATOM 3177 C TYR A 159 -9.413 -15.537 28.437 1.00 6.25 C ANISOU 3177 C TYR B 159 886 919 566 -78 144 82 C ATOM 3178 O TYR A 159 -8.948 -14.915 29.374 1.00 6.68 O ANISOU 3178 O TYR B 159 895 981 659 -274 223 -9 O ATOM 3179 CB TYR A 159 -9.116 -14.392 26.287 1.00 6.16 C ANISOU 3179 CB TYR B 159 726 944 669 -33 137 -19 C ATOM 3180 CG TYR A 159 -10.623 -14.271 26.203 1.00 5.75 C ANISOU 3180 CG TYR B 159 676 793 714 -81 188 67 C ATOM 3181 CD1 TYR A 159 -11.317 -13.342 26.985 1.00 7.98 C ANISOU 3181 CD1 TYR B 159 1007 1097 928 -34 109 -189 C ATOM 3182 CD2 TYR A 159 -11.356 -15.102 25.373 1.00 6.83 C ANISOU 3182 CD2 TYR B 159 964 1162 468 94 93 -133 C ATOM 3183 CE1 TYR A 159 -12.690 -13.230 26.918 1.00 8.36 C ANISOU 3183 CE1 TYR B 159 1024 1088 1062 63 71 -209 C ATOM 3184 CE2 TYR A 159 -12.733 -15.017 25.322 1.00 7.76 C ANISOU 3184 CE2 TYR B 159 818 1162 968 55 -2 -128 C ATOM 3185 CZ TYR A 159 -13.399 -14.075 26.090 1.00 8.14 C ANISOU 3185 CZ TYR B 159 943 1239 911 68 34 -149 C ATOM 3186 OH TYR A 159 -14.769 -13.966 26.034 1.00 10.60 O ANISOU 3186 OH TYR B 159 1027 1389 1611 183 207 -238 O ATOM 3187 N ALA A 160 -10.599 -16.167 28.478 1.00 6.88 N ANISOU 3187 N ALA B 160 877 915 821 -122 158 70 N ATOM 3188 CA ALA A 160 -11.515 -16.111 29.628 1.00 8.19 C ANISOU 3188 CA ALA B 160 1043 1062 1004 45 101 -32 C ATOM 3189 C ALA A 160 -11.374 -17.301 30.513 1.00 9.32 C ANISOU 3189 C ALA B 160 1266 1106 1166 235 -9 -62 C ATOM 3190 O ALA A 160 -12.218 -17.492 31.387 1.00 7.83 O ANISOU 3190 O ALA B 160 943 1023 1008 58 387 158 O ATOM 3191 CB ALA A 160 -12.952 -15.986 29.165 1.00 8.66 C ANISOU 3191 CB ALA B 160 1141 1073 1074 128 66 -20 C ATOM 3192 N ASP A 161 -10.323 -18.111 30.347 1.00 8.30 N ANISOU 3192 N ASP B 161 1050 1126 976 156 67 -28 N ATOM 3193 CA ASP A 161 -10.257 -19.296 31.227 1.00 7.93 C ANISOU 3193 CA ASP B 161 1090 948 973 62 89 46 C ATOM 3194 C ASP A 161 -10.093 -18.730 32.630 1.00 8.87 C ANISOU 3194 C ASP B 161 1102 1130 1136 151 -26 -129 C ATOM 3195 O ASP A 161 -9.102 -18.025 32.862 1.00 7.30 O ANISOU 3195 O ASP B 161 897 1049 828 24 246 -30 O ATOM 3196 CB ASP A 161 -9.029 -20.180 30.876 1.00 7.30 C ANISOU 3196 CB ASP B 161 982 862 927 121 53 27 C ATOM 3197 CG ASP A 161 -8.817 -21.373 31.853 1.00 8.04 C ANISOU 3197 CG ASP B 161 1011 1057 986 167 184 70 C ATOM 3198 OD1 ASP A 161 -9.471 -21.395 32.931 1.00 8.10 O ANISOU 3198 OD1 ASP B 161 1071 1120 886 794 -139 -377 O ATOM 3199 OD2 ASP A 161 -7.997 -22.315 31.599 1.00 9.79 O ANISOU 3199 OD2 ASP B 161 1402 995 1322 640 91 145 O ATOM 3200 N PRO A 162 -11.029 -19.001 33.552 1.00 9.26 N ANISOU 3200 N PRO B 162 1229 1152 1135 92 41 4 N ATOM 3201 CA PRO A 162 -10.962 -18.422 34.899 1.00 10.35 C ANISOU 3201 CA PRO B 162 1337 1305 1288 124 -41 -80 C ATOM 3202 C PRO A 162 -9.753 -18.874 35.736 1.00 11.06 C ANISOU 3202 C PRO B 162 1451 1367 1382 170 -101 -105 C ATOM 3203 O PRO A 162 -9.558 -18.313 36.834 1.00 12.92 O ANISOU 3203 O PRO B 162 1651 1567 1690 344 -218 -352 O ATOM 3204 CB PRO A 162 -12.305 -18.855 35.552 1.00 10.03 C ANISOU 3204 CB PRO B 162 1284 1274 1252 99 6 -51 C ATOM 3205 CG PRO A 162 -12.809 -20.024 34.763 1.00 10.09 C ANISOU 3205 CG PRO B 162 1317 1268 1248 88 39 -1 C ATOM 3206 CD PRO A 162 -12.223 -19.867 33.391 1.00 9.14 C ANISOU 3206 CD PRO B 162 1180 1135 1156 63 14 -4 C ATOM 3207 N SER A 163 -9.012 -19.896 35.287 1.00 11.64 N ANISOU 3207 N SER B 163 1521 1423 1477 126 -50 -120 N ATOM 3208 CA SER A 163 -7.893 -20.408 36.080 1.00 11.07 C ANISOU 3208 CA SER B 163 1425 1356 1425 44 -26 -28 C ATOM 3209 C SER A 163 -6.619 -19.624 35.774 1.00 11.20 C ANISOU 3209 C SER B 163 1483 1394 1376 96 -51 -25 C ATOM 3210 O SER A 163 -5.662 -19.670 36.526 1.00 12.45 O ANISOU 3210 O SER B 163 1568 1512 1650 171 -184 -174 O ATOM 3211 CB SER A 163 -7.668 -21.902 35.804 1.00 12.14 C ANISOU 3211 CB SER B 163 1564 1559 1487 147 -68 -111 C ATOM 3212 OG SER A 163 -7.103 -22.010 34.509 1.00 12.61 O ANISOU 3212 OG SER B 163 1813 1478 1497 117 96 97 O ATOM 3213 N LEU A 164 -6.599 -18.905 34.656 1.00 11.29 N ANISOU 3213 N LEU B 164 1448 1438 1404 107 -59 -126 N ATOM 3214 CA LEU A 164 -5.416 -18.102 34.300 1.00 11.33 C ANISOU 3214 CA LEU B 164 1444 1478 1382 151 -90 -186 C ATOM 3215 C LEU A 164 -5.262 -16.876 35.193 1.00 11.20 C ANISOU 3215 C LEU B 164 1276 1430 1549 56 -72 -274 C ATOM 3216 O LEU A 164 -6.255 -16.228 35.554 1.00 13.41 O ANISOU 3216 O LEU B 164 1566 1592 1934 402 -337 -662 O ATOM 3217 CB LEU A 164 -5.500 -17.585 32.882 1.00 10.96 C ANISOU 3217 CB LEU B 164 1332 1372 1458 38 -76 -215 C ATOM 3218 CG LEU A 164 -5.288 -18.558 31.732 1.00 10.66 C ANISOU 3218 CG LEU B 164 1498 1287 1264 105 -52 -64 C ATOM 3219 CD1 LEU A 164 -5.541 -17.805 30.463 1.00 10.06 C ANISOU 3219 CD1 LEU B 164 1304 1200 1318 -83 108 -57 C ATOM 3220 CD2 LEU A 164 -3.896 -19.191 31.729 1.00 10.67 C ANISOU 3220 CD2 LEU B 164 1408 1186 1458 -102 84 -67 C ATOM 3221 N ASP A 165 -4.026 -16.620 35.602 1.00 11.16 N ANISOU 3221 N ASP B 165 1371 1395 1472 114 -52 -171 N ATOM 3222 CA ASP A 165 -3.744 -15.637 36.652 1.00 10.26 C ANISOU 3222 CA ASP B 165 1266 1250 1380 -3 -1 -45 C ATOM 3223 C ASP A 165 -3.627 -14.305 35.965 1.00 9.60 C ANISOU 3223 C ASP B 165 1127 1133 1387 -45 12 -127 C ATOM 3224 O ASP A 165 -2.581 -13.673 35.974 1.00 10.33 O ANISOU 3224 O ASP B 165 1338 1185 1402 64 42 -108 O ATOM 3225 CB ASP A 165 -2.468 -16.016 37.441 1.00 10.99 C ANISOU 3225 CB ASP B 165 1356 1377 1442 54 -87 -116 C ATOM 3226 CG ASP A 165 -2.159 -15.061 38.598 1.00 13.55 C ANISOU 3226 CG ASP B 165 1579 1620 1946 138 -241 -214 C ATOM 3227 OD1 ASP A 165 -3.071 -14.313 39.022 1.00 16.20 O ANISOU 3227 OD1 ASP B 165 2100 1856 2198 230 -218 -373 O ATOM 3228 OD2 ASP A 165 -1.037 -15.019 39.169 1.00 17.65 O ANISOU 3228 OD2 ASP B 165 1826 2076 2803 171 -555 -363 O ATOM 3229 N ILE A 166 -4.744 -13.933 35.359 1.00 7.79 N ANISOU 3229 N ILE B 166 1109 954 896 0 26 42 N ATOM 3230 CA ILE A 166 -4.911 -12.701 34.631 1.00 7.66 C ANISOU 3230 CA ILE B 166 981 930 996 10 -7 -78 C ATOM 3231 C ILE A 166 -6.283 -12.125 34.947 1.00 7.91 C ANISOU 3231 C ILE B 166 1065 965 975 62 -33 -136 C ATOM 3232 O ILE A 166 -7.185 -12.800 35.425 1.00 7.09 O ANISOU 3232 O ILE B 166 1120 806 768 42 155 1 O ATOM 3233 CB ILE A 166 -4.779 -12.961 33.124 1.00 7.85 C ANISOU 3233 CB ILE B 166 995 904 1084 -11 -6 -62 C ATOM 3234 CG1 ILE A 166 -5.916 -13.853 32.596 1.00 7.65 C ANISOU 3234 CG1 ILE B 166 992 941 973 3 -30 -75 C ATOM 3235 CG2 ILE A 166 -3.409 -13.570 32.818 1.00 7.95 C ANISOU 3235 CG2 ILE B 166 1092 889 1038 9 43 0 C ATOM 3236 CD1 ILE A 166 -5.793 -14.164 31.080 1.00 7.54 C ANISOU 3236 CD1 ILE B 166 999 910 953 -123 41 -69 C ATOM 3237 N LYS A 167 -6.393 -10.839 34.695 1.00 5.92 N ANISOU 3237 N LYS B 167 891 791 564 -15 34 73 N ATOM 3238 CA LYS A 167 -7.617 -10.080 34.832 1.00 7.33 C ANISOU 3238 CA LYS B 167 1042 962 777 -9 25 12 C ATOM 3239 C LYS A 167 -7.730 -9.148 33.635 1.00 6.63 C ANISOU 3239 C LYS B 167 912 870 736 -21 63 42 C ATOM 3240 O LYS A 167 -6.824 -8.369 33.356 1.00 7.05 O ANISOU 3240 O LYS B 167 988 810 879 18 31 -60 O ATOM 3241 CB LYS A 167 -7.548 -9.223 36.089 1.00 8.31 C ANISOU 3241 CB LYS B 167 1214 1061 880 59 44 20 C ATOM 3242 CG LYS A 167 -8.878 -8.697 36.530 1.00 12.86 C ANISOU 3242 CG LYS B 167 1680 1605 1602 86 -78 -84 C ATOM 3243 CD LYS A 167 -9.398 -9.443 37.749 1.00 17.04 C ANISOU 3243 CD LYS B 167 2221 2153 2098 131 24 -58 C ATOM 3244 CE LYS A 167 -9.887 -8.515 38.870 1.00 19.48 C ANISOU 3244 CE LYS B 167 2528 2410 2463 106 -86 -87 C ATOM 3245 NZ LYS A 167 -8.867 -8.287 39.940 1.00 21.00 N ANISOU 3245 NZ LYS B 167 2701 2628 2649 146 -159 -181 N ATOM 3246 N TRP A 168 -8.856 -9.220 32.951 1.00 8.16 N ANISOU 3246 N TRP B 168 1085 1041 973 6 -39 -11 N ATOM 3247 CA TRP A 168 -9.180 -8.309 31.869 1.00 8.44 C ANISOU 3247 CA TRP B 168 1125 1093 987 23 -47 11 C ATOM 3248 C TRP A 168 -10.085 -7.173 32.368 1.00 10.32 C ANISOU 3248 C TRP B 168 1388 1302 1231 51 -15 -15 C ATOM 3249 O TRP A 168 -10.740 -7.299 33.398 1.00 11.23 O ANISOU 3249 O TRP B 168 1678 1385 1203 209 -8 -105 O ATOM 3250 CB TRP A 168 -9.912 -9.063 30.767 1.00 8.48 C ANISOU 3250 CB TRP B 168 1070 1049 1101 -58 -60 -4 C ATOM 3251 CG TRP A 168 -9.149 -10.169 30.135 1.00 7.50 C ANISOU 3251 CG TRP B 168 853 1103 890 -10 -95 51 C ATOM 3252 CD1 TRP A 168 -9.347 -11.494 30.312 1.00 8.00 C ANISOU 3252 CD1 TRP B 168 981 1089 967 96 -94 -27 C ATOM 3253 CD2 TRP A 168 -8.095 -10.049 29.167 1.00 6.86 C ANISOU 3253 CD2 TRP B 168 710 956 940 -39 -66 79 C ATOM 3254 NE1 TRP A 168 -8.477 -12.222 29.538 1.00 7.47 N ANISOU 3254 NE1 TRP B 168 863 955 1020 -20 84 82 N ATOM 3255 CE2 TRP A 168 -7.691 -11.354 28.827 1.00 7.27 C ANISOU 3255 CE2 TRP B 168 800 946 1016 -61 -92 108 C ATOM 3256 CE3 TRP A 168 -7.437 -8.965 28.562 1.00 6.63 C ANISOU 3256 CE3 TRP B 168 860 911 745 101 -55 154 C ATOM 3257 CZ2 TRP A 168 -6.694 -11.617 27.903 1.00 8.17 C ANISOU 3257 CZ2 TRP B 168 828 1076 1200 75 -293 -130 C ATOM 3258 CZ3 TRP A 168 -6.427 -9.228 27.640 1.00 8.65 C ANISOU 3258 CZ3 TRP B 168 941 1182 1163 139 -171 138 C ATOM 3259 CH2 TRP A 168 -6.075 -10.550 27.320 1.00 8.12 C ANISOU 3259 CH2 TRP B 168 923 1161 997 43 -31 -44 C ATOM 3260 N GLU A 169 -10.138 -6.066 31.625 1.00 11.62 N ANISOU 3260 N GLU B 169 1612 1433 1368 103 -42 -42 N ATOM 3261 CA GLU A 169 -11.116 -5.006 31.938 1.00 12.68 C ANISOU 3261 CA GLU B 169 1685 1576 1554 58 -25 -21 C ATOM 3262 C GLU A 169 -12.483 -5.351 31.416 1.00 12.83 C ANISOU 3262 C GLU B 169 1698 1602 1572 115 -27 -30 C ATOM 3263 O GLU A 169 -12.595 -5.933 30.360 1.00 13.51 O ANISOU 3263 O GLU B 169 1861 1725 1546 173 -131 36 O ATOM 3264 CB GLU A 169 -10.741 -3.677 31.297 1.00 13.66 C ANISOU 3264 CB GLU B 169 1822 1656 1712 61 -55 -66 C ATOM 3265 CG GLU A 169 -9.295 -3.279 31.396 1.00 15.96 C ANISOU 3265 CG GLU B 169 2085 1893 2083 55 2 -103 C ATOM 3266 CD GLU A 169 -9.063 -2.079 32.298 1.00 18.89 C ANISOU 3266 CD GLU B 169 2529 2227 2421 230 -110 -327 C ATOM 3267 OE1 GLU A 169 -9.928 -1.178 32.362 1.00 22.07 O ANISOU 3267 OE1 GLU B 169 2999 2438 2946 292 -176 -285 O ATOM 3268 OE2 GLU A 169 -7.994 -2.038 32.929 1.00 22.54 O ANISOU 3268 OE2 GLU B 169 3169 2597 2799 226 -366 -446 O ATOM 3269 N ASN A 170 -13.522 -5.007 32.185 1.00 12.44 N ANISOU 3269 N ASN B 170 1621 1574 1529 52 8 18 N ATOM 3270 CA ASN A 170 -14.881 -4.889 31.666 1.00 12.80 C ANISOU 3270 CA ASN B 170 1691 1568 1603 49 -32 12 C ATOM 3271 C ASN A 170 -15.276 -5.972 30.669 1.00 12.49 C ANISOU 3271 C ASN B 170 1681 1556 1507 49 -31 8 C ATOM 3272 O ASN A 170 -15.713 -5.653 29.568 1.00 12.25 O ANISOU 3272 O ASN B 170 1727 1538 1388 126 -146 114 O ATOM 3273 CB ASN A 170 -15.040 -3.509 31.008 1.00 13.08 C ANISOU 3273 CB ASN B 170 1715 1540 1714 33 -51 -16 C ATOM 3274 CG ASN A 170 -14.679 -2.370 31.945 1.00 14.78 C ANISOU 3274 CG ASN B 170 1907 1639 2070 18 -56 104 C ATOM 3275 OD1 ASN A 170 -13.826 -1.537 31.626 1.00 16.74 O ANISOU 3275 OD1 ASN B 170 2146 1573 2640 -2 -139 238 O ATOM 3276 ND2 ASN A 170 -15.313 -2.335 33.108 1.00 16.84 N ANISOU 3276 ND2 ASN B 170 2114 1723 2561 250 18 49 N ATOM 3277 N LEU A 171 -15.118 -7.240 31.057 1.00 12.15 N ANISOU 3277 N LEU B 171 1674 1520 1421 7 23 73 N ATOM 3278 CA LEU A 171 -15.304 -8.394 30.155 1.00 12.39 C ANISOU 3278 CA LEU B 171 1683 1565 1459 -3 67 50 C ATOM 3279 C LEU A 171 -16.671 -8.411 29.501 1.00 12.35 C ANISOU 3279 C LEU B 171 1661 1562 1467 -24 111 47 C ATOM 3280 O LEU A 171 -16.848 -8.904 28.380 1.00 12.08 O ANISOU 3280 O LEU B 171 1724 1583 1279 -37 219 29 O ATOM 3281 CB LEU A 171 -15.097 -9.724 30.903 1.00 12.69 C ANISOU 3281 CB LEU B 171 1726 1597 1498 14 75 60 C ATOM 3282 CG LEU A 171 -13.776 -10.472 30.699 1.00 14.19 C ANISOU 3282 CG LEU B 171 1777 1856 1757 7 89 23 C ATOM 3283 CD1 LEU A 171 -13.922 -11.918 31.105 1.00 15.88 C ANISOU 3283 CD1 LEU B 171 2126 1965 1941 158 57 -56 C ATOM 3284 CD2 LEU A 171 -13.285 -10.408 29.263 1.00 14.86 C ANISOU 3284 CD2 LEU B 171 1937 1925 1781 108 5 4 C ATOM 3285 N GLU A 172 -17.644 -7.880 30.224 1.00 12.45 N ANISOU 3285 N GLU B 172 1694 1599 1436 13 118 43 N ATOM 3286 CA GLU A 172 -18.996 -7.733 29.733 1.00 12.78 C ANISOU 3286 CA GLU B 172 1630 1644 1580 -21 57 0 C ATOM 3287 C GLU A 172 -19.069 -7.022 28.387 1.00 11.60 C ANISOU 3287 C GLU B 172 1434 1552 1419 -18 72 -23 C ATOM 3288 O GLU A 172 -19.924 -7.322 27.561 1.00 12.51 O ANISOU 3288 O GLU B 172 1498 1582 1670 -78 140 -91 O ATOM 3289 CB GLU A 172 -19.884 -6.984 30.762 1.00 13.47 C ANISOU 3289 CB GLU B 172 1781 1755 1580 26 70 12 C ATOM 3290 CG GLU A 172 -19.498 -7.129 32.246 1.00 16.30 C ANISOU 3290 CG GLU B 172 2097 2052 2044 45 -92 -10 C ATOM 3291 CD GLU A 172 -18.325 -6.239 32.673 1.00 16.92 C ANISOU 3291 CD GLU B 172 2230 2087 2111 32 -154 59 C ATOM 3292 OE1 GLU A 172 -18.286 -5.043 32.296 1.00 18.12 O ANISOU 3292 OE1 GLU B 172 2655 2094 2135 160 -157 124 O ATOM 3293 OE2 GLU A 172 -17.424 -6.741 33.381 1.00 18.74 O ANISOU 3293 OE2 GLU B 172 2508 2321 2290 262 -381 -7 O ATOM 3294 N GLU A 173 -18.162 -6.076 28.164 1.00 10.02 N ANISOU 3294 N GLU B 173 1239 1352 1213 -44 94 -26 N ATOM 3295 CA GLU A 173 -18.183 -5.252 26.954 1.00 9.74 C ANISOU 3295 CA GLU B 173 1217 1330 1153 11 32 -2 C ATOM 3296 C GLU A 173 -17.088 -5.620 25.955 1.00 8.13 C ANISOU 3296 C GLU B 173 1060 1128 901 -28 77 -8 C ATOM 3297 O GLU A 173 -16.887 -4.926 24.962 1.00 7.38 O ANISOU 3297 O GLU B 173 1031 1153 620 84 135 82 O ATOM 3298 CB GLU A 173 -18.056 -3.782 27.335 1.00 10.35 C ANISOU 3298 CB GLU B 173 1275 1396 1261 -14 22 0 C ATOM 3299 CG GLU A 173 -19.223 -3.272 28.164 1.00 13.65 C ANISOU 3299 CG GLU B 173 1802 1771 1611 114 26 -38 C ATOM 3300 CD GLU A 173 -18.934 -1.957 28.858 1.00 17.91 C ANISOU 3300 CD GLU B 173 2499 2223 2080 156 174 99 C ATOM 3301 OE1 GLU A 173 -18.113 -1.161 28.348 1.00 21.17 O ANISOU 3301 OE1 GLU B 173 2820 2635 2587 330 155 -16 O ATOM 3302 OE2 GLU A 173 -19.553 -1.724 29.924 1.00 22.94 O ANISOU 3302 OE2 GLU B 173 3451 2717 2544 131 200 213 O ATOM 3303 N ALA A 174 -16.371 -6.702 26.215 1.00 6.37 N ANISOU 3303 N ALA B 174 809 962 649 -40 99 18 N ATOM 3304 CA ALA A 174 -15.289 -7.123 25.339 1.00 6.06 C ANISOU 3304 CA ALA B 174 793 833 675 -55 50 -48 C ATOM 3305 C ALA A 174 -15.827 -7.562 23.985 1.00 5.56 C ANISOU 3305 C ALA B 174 703 768 640 -135 39 -50 C ATOM 3306 O ALA A 174 -16.891 -8.201 23.888 1.00 6.08 O ANISOU 3306 O ALA B 174 806 796 708 -314 69 -139 O ATOM 3307 CB ALA A 174 -14.500 -8.256 25.977 1.00 6.05 C ANISOU 3307 CB ALA B 174 776 919 603 3 32 -41 C ATOM 3308 N GLU A 175 -15.088 -7.190 22.949 1.00 4.66 N ANISOU 3308 N GLU B 175 639 681 449 -58 84 -70 N ATOM 3309 CA GLU A 175 -15.377 -7.545 21.569 1.00 5.34 C ANISOU 3309 CA GLU B 175 723 663 641 -21 -24 -81 C ATOM 3310 C GLU A 175 -14.356 -8.604 21.156 1.00 5.10 C ANISOU 3310 C GLU B 175 635 693 607 -15 -74 -132 C ATOM 3311 O GLU A 175 -13.166 -8.313 20.930 1.00 4.36 O ANISOU 3311 O GLU B 175 518 677 459 38 4 -292 O ATOM 3312 CB GLU A 175 -15.279 -6.305 20.684 1.00 5.94 C ANISOU 3312 CB GLU B 175 809 707 740 -48 57 -37 C ATOM 3313 CG GLU A 175 -15.667 -6.538 19.236 1.00 8.65 C ANISOU 3313 CG GLU B 175 1330 1021 935 -89 41 47 C ATOM 3314 CD GLU A 175 -15.531 -5.285 18.371 1.00 12.16 C ANISOU 3314 CD GLU B 175 1985 1513 1122 -181 -45 115 C ATOM 3315 OE1 GLU A 175 -15.268 -4.182 18.895 1.00 11.66 O ANISOU 3315 OE1 GLU B 175 1621 1556 1251 -47 -56 398 O ATOM 3316 OE2 GLU A 175 -15.698 -5.404 17.145 1.00 19.10 O ANISOU 3316 OE2 GLU B 175 3265 2210 1780 -194 -186 122 O ATOM 3317 N VAL A 176 -14.822 -9.844 21.133 1.00 6.03 N ANISOU 3317 N VAL B 176 736 758 796 -3 -71 -107 N ATOM 3318 CA VAL A 176 -13.972 -11.022 20.965 1.00 6.24 C ANISOU 3318 CA VAL B 176 745 846 778 29 -76 -122 C ATOM 3319 C VAL A 176 -14.425 -11.788 19.724 1.00 7.05 C ANISOU 3319 C VAL B 176 873 949 854 26 -105 -135 C ATOM 3320 O VAL A 176 -15.623 -11.944 19.498 1.00 7.80 O ANISOU 3320 O VAL B 176 860 1096 1007 205 -132 -250 O ATOM 3321 CB VAL A 176 -14.094 -11.951 22.198 1.00 6.80 C ANISOU 3321 CB VAL B 176 871 896 817 19 -37 -136 C ATOM 3322 CG1 VAL A 176 -13.166 -13.185 22.080 1.00 6.94 C ANISOU 3322 CG1 VAL B 176 1055 821 761 133 -1 -26 C ATOM 3323 CG2 VAL A 176 -13.762 -11.196 23.478 1.00 6.77 C ANISOU 3323 CG2 VAL B 176 942 931 697 14 -56 -123 C ATOM 3324 N SER A 177 -13.475 -12.268 18.928 1.00 6.57 N ANISOU 3324 N SER B 177 839 924 732 86 -158 -137 N ATOM 3325 CA SER A 177 -13.815 -13.064 17.748 1.00 7.12 C ANISOU 3325 CA SER B 177 946 995 763 51 -112 -106 C ATOM 3326 C SER A 177 -14.362 -14.428 18.133 1.00 7.09 C ANISOU 3326 C SER B 177 981 917 796 44 -88 -185 C ATOM 3327 O SER A 177 -14.062 -14.948 19.197 1.00 5.91 O ANISOU 3327 O SER B 177 838 698 710 168 -29 -390 O ATOM 3328 CB SER A 177 -12.600 -13.251 16.867 1.00 7.92 C ANISOU 3328 CB SER B 177 1172 1087 749 75 -78 -133 C ATOM 3329 OG SER A 177 -11.675 -14.122 17.463 1.00 7.18 O ANISOU 3329 OG SER B 177 1212 1142 373 136 -74 -179 O ATOM 3330 N GLU A 178 -15.152 -15.023 17.241 1.00 8.58 N ANISOU 3330 N GLU B 178 1116 1181 962 78 -82 -135 N ATOM 3331 CA GLU A 178 -15.640 -16.380 17.455 1.00 9.27 C ANISOU 3331 CA GLU B 178 1196 1228 1097 21 -112 -119 C ATOM 3332 C GLU A 178 -14.485 -17.364 17.677 1.00 8.33 C ANISOU 3332 C GLU B 178 1070 1124 967 -4 -129 -181 C ATOM 3333 O GLU A 178 -14.540 -18.215 18.565 1.00 7.86 O ANISOU 3333 O GLU B 178 936 1087 962 -48 -166 -320 O ATOM 3334 CB GLU A 178 -16.500 -16.844 16.268 1.00 10.20 C ANISOU 3334 CB GLU B 178 1288 1352 1234 44 -132 -107 C ATOM 3335 CG GLU A 178 -17.166 -18.187 16.472 1.00 14.06 C ANISOU 3335 CG GLU B 178 1803 1772 1766 92 -203 -99 C ATOM 3336 CD GLU A 178 -18.501 -18.323 15.740 1.00 18.23 C ANISOU 3336 CD GLU B 178 2282 2223 2419 114 -212 15 C ATOM 3337 OE1 GLU A 178 -18.804 -17.497 14.838 1.00 20.88 O ANISOU 3337 OE1 GLU B 178 2653 2512 2766 95 -339 43 O ATOM 3338 OE2 GLU A 178 -19.255 -19.267 16.063 1.00 22.91 O ANISOU 3338 OE2 GLU B 178 3027 2736 2941 227 -127 18 O ATOM 3339 N ALA A 179 -13.431 -17.232 16.881 1.00 8.22 N ANISOU 3339 N ALA B 179 1111 1089 924 20 -120 -185 N ATOM 3340 CA ALA A 179 -12.273 -18.108 17.015 1.00 8.67 C ANISOU 3340 CA ALA B 179 1105 1169 1018 52 -37 -97 C ATOM 3341 C ALA A 179 -11.673 -17.976 18.403 1.00 7.31 C ANISOU 3341 C ALA B 179 929 970 879 37 -48 -60 C ATOM 3342 O ALA A 179 -11.357 -18.969 19.040 1.00 8.23 O ANISOU 3342 O ALA B 179 1088 1074 962 148 -24 -126 O ATOM 3343 CB ALA A 179 -11.240 -17.774 15.972 1.00 9.12 C ANISOU 3343 CB ALA B 179 1254 1226 982 71 -20 -77 C ATOM 3344 N ASP A 180 -11.496 -16.746 18.882 1.00 7.25 N ANISOU 3344 N ASP B 180 905 995 855 109 -74 -113 N ATOM 3345 CA ASP A 180 -10.905 -16.547 20.210 1.00 6.31 C ANISOU 3345 CA ASP B 180 777 856 765 57 -118 -59 C ATOM 3346 C ASP A 180 -11.821 -17.051 21.317 1.00 6.68 C ANISOU 3346 C ASP B 180 827 905 804 26 -97 -68 C ATOM 3347 O ASP A 180 -11.355 -17.559 22.326 1.00 7.04 O ANISOU 3347 O ASP B 180 695 1096 882 -31 -208 -59 O ATOM 3348 CB ASP A 180 -10.494 -15.090 20.432 1.00 5.92 C ANISOU 3348 CB ASP B 180 710 839 697 51 -74 -78 C ATOM 3349 CG ASP A 180 -9.217 -14.731 19.715 1.00 6.73 C ANISOU 3349 CG ASP B 180 874 972 710 224 -61 -161 C ATOM 3350 OD1 ASP A 180 -8.532 -15.648 19.183 1.00 6.41 O ANISOU 3350 OD1 ASP B 180 658 925 851 263 42 -217 O ATOM 3351 OD2 ASP A 180 -8.817 -13.550 19.638 1.00 5.55 O ANISOU 3351 OD2 ASP B 180 590 902 614 326 -1 -265 O ATOM 3352 N GLU A 181 -13.131 -16.980 21.118 1.00 6.98 N ANISOU 3352 N GLU B 181 853 995 803 -5 -132 -104 N ATOM 3353 CA GLU A 181 -14.061 -17.480 22.135 1.00 7.95 C ANISOU 3353 CA GLU B 181 987 1077 955 -32 -52 -35 C ATOM 3354 C GLU A 181 -13.918 -18.988 22.328 1.00 7.40 C ANISOU 3354 C GLU B 181 834 1058 917 -84 -86 -6 C ATOM 3355 O GLU A 181 -14.179 -19.508 23.412 1.00 7.02 O ANISOU 3355 O GLU B 181 817 1002 845 -155 -157 38 O ATOM 3356 CB GLU A 181 -15.510 -17.167 21.768 1.00 8.62 C ANISOU 3356 CB GLU B 181 1086 1145 1041 18 -37 -18 C ATOM 3357 CG GLU A 181 -15.873 -15.700 21.756 1.00 11.85 C ANISOU 3357 CG GLU B 181 1553 1572 1375 96 42 -39 C ATOM 3358 CD GLU A 181 -16.259 -15.119 23.108 1.00 14.01 C ANISOU 3358 CD GLU B 181 1710 1949 1663 294 319 -18 C ATOM 3359 OE1 GLU A 181 -15.838 -15.641 24.169 1.00 14.09 O ANISOU 3359 OE1 GLU B 181 1450 2336 1564 678 342 -231 O ATOM 3360 OE2 GLU A 181 -16.994 -14.104 23.092 1.00 17.92 O ANISOU 3360 OE2 GLU B 181 2367 2234 2207 311 325 52 O ATOM 3361 N ASN A 182 -13.452 -19.674 21.289 1.00 8.05 N ANISOU 3361 N ASN B 182 929 1103 1025 -77 -95 -7 N ATOM 3362 CA ASN A 182 -13.398 -21.132 21.274 1.00 8.50 C ANISOU 3362 CA ASN B 182 1027 1129 1071 -61 -41 -9 C ATOM 3363 C ASN A 182 -12.014 -21.784 21.391 1.00 8.16 C ANISOU 3363 C ASN B 182 998 1088 1012 -36 -114 -30 C ATOM 3364 O ASN A 182 -11.887 -22.997 21.258 1.00 8.04 O ANISOU 3364 O ASN B 182 982 1049 1023 -75 -160 -2 O ATOM 3365 CB ASN A 182 -14.134 -21.624 20.029 1.00 9.07 C ANISOU 3365 CB ASN B 182 1111 1147 1188 -104 -105 -63 C ATOM 3366 CG ASN A 182 -15.631 -21.448 20.159 1.00 11.85 C ANISOU 3366 CG ASN B 182 1496 1502 1502 -132 -84 -58 C ATOM 3367 OD1 ASN A 182 -16.269 -22.153 20.931 1.00 15.90 O ANISOU 3367 OD1 ASN B 182 1699 2220 2119 -219 -127 -212 O ATOM 3368 ND2 ASN A 182 -16.183 -20.466 19.453 1.00 14.62 N ANISOU 3368 ND2 ASN B 182 1753 1850 1952 -260 -251 -105 N ATOM 3369 N HIS A 183 -10.981 -21.015 21.691 1.00 7.51 N ANISOU 3369 N HIS B 183 985 967 900 -61 -61 -3 N ATOM 3370 CA HIS A 183 -9.688 -21.645 21.918 1.00 7.23 C ANISOU 3370 CA HIS B 183 904 940 900 -33 -14 29 C ATOM 3371 C HIS A 183 -9.779 -22.581 23.135 1.00 8.14 C ANISOU 3371 C HIS B 183 1031 1095 965 23 -47 -36 C ATOM 3372 O HIS A 183 -10.610 -22.373 24.028 1.00 6.37 O ANISOU 3372 O HIS B 183 766 895 757 -164 46 204 O ATOM 3373 CB HIS A 183 -8.590 -20.589 22.083 1.00 7.10 C ANISOU 3373 CB HIS B 183 935 868 894 -68 -40 31 C ATOM 3374 CG HIS A 183 -8.224 -19.918 20.794 1.00 5.99 C ANISOU 3374 CG HIS B 183 667 926 681 98 -72 116 C ATOM 3375 ND1 HIS A 183 -8.131 -20.618 19.612 1.00 6.26 N ANISOU 3375 ND1 HIS B 183 796 950 631 306 71 328 N ATOM 3376 CD2 HIS A 183 -7.990 -18.621 20.484 1.00 8.33 C ANISOU 3376 CD2 HIS B 183 997 1244 922 181 65 81 C ATOM 3377 CE1 HIS A 183 -7.812 -19.791 18.638 1.00 7.13 C ANISOU 3377 CE1 HIS B 183 1157 989 559 105 172 465 C ATOM 3378 NE2 HIS A 183 -7.724 -18.572 19.137 1.00 7.66 N ANISOU 3378 NE2 HIS B 183 943 1237 729 91 -40 71 N ATOM 3379 N PRO A 184 -8.941 -23.613 23.172 1.00 7.97 N ANISOU 3379 N PRO B 184 1081 991 956 -43 0 105 N ATOM 3380 CA PRO A 184 -9.014 -24.608 24.246 1.00 8.48 C ANISOU 3380 CA PRO B 184 1065 1114 1040 -34 -24 43 C ATOM 3381 C PRO A 184 -8.582 -24.031 25.594 1.00 8.85 C ANISOU 3381 C PRO B 184 1163 1199 999 20 -17 70 C ATOM 3382 O PRO A 184 -7.843 -23.040 25.649 1.00 8.42 O ANISOU 3382 O PRO B 184 886 1324 988 -140 -104 -9 O ATOM 3383 CB PRO A 184 -8.044 -25.682 23.770 1.00 8.59 C ANISOU 3383 CB PRO B 184 1154 1071 1037 0 -14 76 C ATOM 3384 CG PRO A 184 -7.100 -25.000 22.868 1.00 9.56 C ANISOU 3384 CG PRO B 184 1214 1231 1187 34 0 7 C ATOM 3385 CD PRO A 184 -7.872 -23.926 22.203 1.00 8.88 C ANISOU 3385 CD PRO B 184 1156 1137 1078 78 -59 3 C ATOM 3386 N PHE A 185 -9.091 -24.661 26.665 1.00 8.63 N ANISOU 3386 N PHE B 185 1032 1147 1098 -138 -23 16 N ATOM 3387 CA PHE A 185 -8.678 -24.394 28.065 1.00 9.23 C ANISOU 3387 CA PHE B 185 1181 1225 1101 -27 -7 13 C ATOM 3388 C PHE A 185 -7.341 -25.034 28.420 1.00 10.43 C ANISOU 3388 C PHE B 185 1268 1462 1231 107 -46 -97 C ATOM 3389 O PHE A 185 -6.923 -26.011 27.787 1.00 10.34 O ANISOU 3389 O PHE B 185 1344 1356 1226 196 -206 -91 O ATOM 3390 CB PHE A 185 -9.764 -24.869 29.019 1.00 10.39 C ANISOU 3390 CB PHE B 185 1307 1461 1179 116 -18 -58 C ATOM 3391 CG PHE A 185 -11.022 -24.136 28.815 1.00 9.34 C ANISOU 3391 CG PHE B 185 1127 1404 1016 -113 46 18 C ATOM 3392 CD1 PHE A 185 -12.093 -24.731 28.177 1.00 11.27 C ANISOU 3392 CD1 PHE B 185 1386 1701 1193 186 -47 -128 C ATOM 3393 CD2 PHE A 185 -11.113 -22.810 29.189 1.00 11.38 C ANISOU 3393 CD2 PHE B 185 1464 1626 1234 136 6 -134 C ATOM 3394 CE1 PHE A 185 -13.252 -24.023 27.969 1.00 11.13 C ANISOU 3394 CE1 PHE B 185 1343 1700 1186 237 -8 15 C ATOM 3395 CE2 PHE A 185 -12.234 -22.095 28.979 1.00 10.26 C ANISOU 3395 CE2 PHE B 185 1263 1540 1095 -27 50 0 C ATOM 3396 CZ PHE A 185 -13.312 -22.674 28.358 1.00 10.12 C ANISOU 3396 CZ PHE B 185 1163 1460 1222 -48 92 32 C ATOM 3397 N LEU A 186 -6.634 -24.363 29.353 1.00 10.27 N ANISOU 3397 N LEU B 186 1276 1382 1242 80 -111 -91 N ATOM 3398 CA LEU A 186 -5.217 -24.619 29.632 1.00 9.99 C ANISOU 3398 CA LEU B 186 1258 1303 1232 76 -45 -3 C ATOM 3399 C LEU A 186 -4.975 -26.116 29.809 1.00 9.93 C ANISOU 3399 C LEU B 186 1163 1361 1247 -13 -38 -47 C ATOM 3400 O LEU A 186 -4.040 -26.695 29.273 1.00 11.23 O ANISOU 3400 O LEU B 186 1294 1695 1275 245 -118 -116 O ATOM 3401 CB LEU A 186 -4.778 -23.846 30.882 1.00 9.74 C ANISOU 3401 CB LEU B 186 1197 1262 1240 33 -37 4 C ATOM 3402 CG LEU A 186 -3.290 -23.877 31.230 1.00 11.26 C ANISOU 3402 CG LEU B 186 1313 1485 1477 142 -129 -200 C ATOM 3403 CD1 LEU A 186 -2.492 -23.180 30.150 1.00 9.85 C ANISOU 3403 CD1 LEU B 186 1192 1218 1330 22 -38 13 C ATOM 3404 CD2 LEU A 186 -3.053 -23.203 32.572 1.00 10.83 C ANISOU 3404 CD2 LEU B 186 1380 1452 1282 89 -94 -54 C ATOM 3405 N LYS A 187 -5.859 -26.768 30.533 1.00 10.58 N ANISOU 3405 N LYS B 187 1344 1393 1284 121 -75 -15 N ATOM 3406 CA LYS A 187 -5.679 -28.202 30.733 1.00 10.68 C ANISOU 3406 CA LYS B 187 1329 1395 1331 65 -27 -19 C ATOM 3407 C LYS A 187 -5.768 -29.080 29.457 1.00 11.02 C ANISOU 3407 C LYS B 187 1381 1446 1361 102 -11 -13 C ATOM 3408 O LYS A 187 -5.300 -30.225 29.449 1.00 11.03 O ANISOU 3408 O LYS B 187 1378 1430 1382 107 -48 30 O ATOM 3409 CB LYS A 187 -6.691 -28.715 31.744 1.00 10.59 C ANISOU 3409 CB LYS B 187 1309 1412 1300 66 -63 8 C ATOM 3410 CG LYS A 187 -8.136 -28.431 31.365 1.00 11.33 C ANISOU 3410 CG LYS B 187 1392 1497 1413 41 9 28 C ATOM 3411 CD LYS A 187 -8.924 -29.679 31.212 1.00 12.15 C ANISOU 3411 CD LYS B 187 1568 1571 1477 110 -20 -50 C ATOM 3412 CE LYS A 187 -10.310 -29.403 30.671 1.00 12.05 C ANISOU 3412 CE LYS B 187 1562 1440 1575 -24 27 -9 C ATOM 3413 NZ LYS A 187 -10.860 -30.652 30.076 1.00 13.66 N ANISOU 3413 NZ LYS B 187 2001 1574 1613 133 -118 -271 N ATOM 3414 N ASP A 188 -6.379 -28.551 28.402 1.00 11.14 N ANISOU 3414 N ASP B 188 1382 1460 1390 106 -40 -23 N ATOM 3415 CA ASP A 188 -6.375 -29.185 27.085 1.00 11.14 C ANISOU 3415 CA ASP B 188 1357 1448 1428 11 -32 -58 C ATOM 3416 C ASP A 188 -5.280 -28.755 26.095 1.00 11.70 C ANISOU 3416 C ASP B 188 1483 1549 1411 79 12 -61 C ATOM 3417 O ASP A 188 -5.173 -29.351 25.010 1.00 12.23 O ANISOU 3417 O ASP B 188 1486 1689 1471 -41 11 -210 O ATOM 3418 CB ASP A 188 -7.769 -29.003 26.453 1.00 11.45 C ANISOU 3418 CB ASP B 188 1402 1496 1451 50 -19 -28 C ATOM 3419 CG ASP A 188 -8.842 -29.797 27.187 1.00 12.48 C ANISOU 3419 CG ASP B 188 1570 1655 1515 313 -131 0 C ATOM 3420 OD1 ASP A 188 -9.925 -29.248 27.499 1.00 15.09 O ANISOU 3420 OD1 ASP B 188 1715 1964 2051 83 -13 0 O ATOM 3421 OD2 ASP A 188 -8.663 -30.977 27.509 1.00 13.49 O ANISOU 3421 OD2 ASP B 188 1377 1929 1818 -154 0 -80 O ATOM 3422 N VAL A 189 -4.499 -27.729 26.455 1.00 10.90 N ANISOU 3422 N VAL B 189 1351 1415 1374 13 -32 -53 N ATOM 3423 CA VAL A 189 -3.366 -27.270 25.649 1.00 11.10 C ANISOU 3423 CA VAL B 189 1345 1463 1409 51 -1 -20 C ATOM 3424 C VAL A 189 -2.264 -28.323 25.775 1.00 11.69 C ANISOU 3424 C VAL B 189 1380 1592 1467 73 20 9 C ATOM 3425 O VAL A 189 -1.860 -28.653 26.901 1.00 12.43 O ANISOU 3425 O VAL B 189 1421 1737 1563 232 45 35 O ATOM 3426 CB VAL A 189 -2.853 -25.883 26.137 1.00 10.63 C ANISOU 3426 CB VAL B 189 1328 1343 1366 40 -15 -3 C ATOM 3427 CG1 VAL A 189 -1.549 -25.477 25.431 1.00 10.66 C ANISOU 3427 CG1 VAL B 189 1263 1338 1446 -99 47 -45 C ATOM 3428 CG2 VAL A 189 -3.925 -24.802 25.921 1.00 10.56 C ANISOU 3428 CG2 VAL B 189 1279 1386 1346 51 1 30 C ATOM 3429 N LYS A 190 -1.795 -28.858 24.641 1.00 12.11 N ANISOU 3429 N LYS B 190 1428 1641 1533 49 -13 -45 N ATOM 3430 CA LYS A 190 -0.507 -29.569 24.635 1.00 12.72 C ANISOU 3430 CA LYS B 190 1587 1593 1651 22 21 -34 C ATOM 3431 C LYS A 190 0.699 -28.606 24.789 1.00 11.39 C ANISOU 3431 C LYS B 190 1342 1434 1551 -23 50 -38 C ATOM 3432 O LYS A 190 0.994 -27.826 23.867 1.00 11.56 O ANISOU 3432 O LYS B 190 1384 1379 1629 86 64 25 O ATOM 3433 CB LYS A 190 -0.333 -30.350 23.329 1.00 13.38 C ANISOU 3433 CB LYS B 190 1621 1751 1709 -32 18 -61 C ATOM 3434 CG LYS A 190 0.994 -31.105 23.254 1.00 17.01 C ANISOU 3434 CG LYS B 190 2132 2177 2153 -15 9 -44 C ATOM 3435 CD LYS A 190 0.887 -32.432 22.524 1.00 21.07 C ANISOU 3435 CD LYS B 190 2662 2717 2624 49 -17 -25 C ATOM 3436 CE LYS A 190 2.147 -33.277 22.714 1.00 23.16 C ANISOU 3436 CE LYS B 190 2946 2985 2868 69 2 -23 C ATOM 3437 NZ LYS A 190 1.939 -34.406 23.667 1.00 24.68 N ANISOU 3437 NZ LYS B 190 3154 3266 2957 34 52 4 N ATOM 3438 N PRO A 191 1.437 -28.673 25.906 1.00 10.85 N ANISOU 3438 N PRO B 191 1310 1365 1445 18 57 -9 N ATOM 3439 CA PRO A 191 2.608 -27.795 26.042 1.00 10.18 C ANISOU 3439 CA PRO B 191 1224 1242 1400 -59 69 -31 C ATOM 3440 C PRO A 191 3.580 -27.970 24.885 1.00 10.95 C ANISOU 3440 C PRO B 191 1272 1464 1423 102 56 -94 C ATOM 3441 O PRO A 191 3.783 -29.084 24.423 1.00 9.91 O ANISOU 3441 O PRO B 191 1165 1093 1506 -112 110 -126 O ATOM 3442 CB PRO A 191 3.239 -28.230 27.366 1.00 10.17 C ANISOU 3442 CB PRO B 191 1222 1233 1409 -80 79 -39 C ATOM 3443 CG PRO A 191 2.109 -28.808 28.132 1.00 10.83 C ANISOU 3443 CG PRO B 191 1397 1332 1385 24 83 23 C ATOM 3444 CD PRO A 191 1.271 -29.512 27.102 1.00 10.68 C ANISOU 3444 CD PRO B 191 1242 1355 1459 -14 47 -44 C ATOM 3445 N LEU A 192 4.167 -26.863 24.434 1.00 9.86 N ANISOU 3445 N LEU B 192 1205 1152 1388 -12 35 -50 N ATOM 3446 CA LEU A 192 5.085 -26.848 23.301 1.00 10.76 C ANISOU 3446 CA LEU B 192 1245 1452 1389 61 13 -96 C ATOM 3447 C LEU A 192 6.482 -27.245 23.739 1.00 11.17 C ANISOU 3447 C LEU B 192 1366 1376 1501 57 34 -82 C ATOM 3448 O LEU A 192 7.065 -26.676 24.655 1.00 11.81 O ANISOU 3448 O LEU B 192 1237 1683 1567 204 54 -274 O ATOM 3449 CB LEU A 192 5.150 -25.448 22.684 1.00 10.18 C ANISOU 3449 CB LEU B 192 1230 1248 1390 30 50 -65 C ATOM 3450 CG LEU A 192 3.872 -25.008 21.979 1.00 10.40 C ANISOU 3450 CG LEU B 192 1136 1447 1365 116 -49 -58 C ATOM 3451 CD1 LEU A 192 3.860 -23.490 21.766 1.00 10.22 C ANISOU 3451 CD1 LEU B 192 1226 1139 1517 168 0 26 C ATOM 3452 CD2 LEU A 192 3.744 -25.712 20.641 1.00 10.70 C ANISOU 3452 CD2 LEU B 192 1302 1261 1501 197 -38 67 C ATOM 3453 N ARG A 193 7.043 -28.231 23.052 1.00 12.12 N ANISOU 3453 N ARG B 193 1453 1557 1596 90 -23 -77 N ATOM 3454 CA ARG A 193 8.385 -28.657 23.407 1.00 13.32 C ANISOU 3454 CA ARG B 193 1661 1629 1768 66 -11 -28 C ATOM 3455 C ARG A 193 9.386 -27.671 22.831 1.00 14.36 C ANISOU 3455 C ARG B 193 1801 1764 1891 96 1 -22 C ATOM 3456 O ARG A 193 9.218 -27.187 21.714 1.00 14.19 O ANISOU 3456 O ARG B 193 1752 1699 1938 172 -15 -60 O ATOM 3457 CB ARG A 193 8.645 -30.063 22.893 1.00 13.42 C ANISOU 3457 CB ARG B 193 1698 1595 1805 73 -5 -20 C ATOM 3458 CG ARG A 193 7.613 -31.073 23.385 1.00 15.96 C ANISOU 3458 CG ARG B 193 2067 1891 2106 2 0 -4 C ATOM 3459 CD ARG A 193 8.005 -32.510 23.160 1.00 20.64 C ANISOU 3459 CD ARG B 193 2621 2576 2645 17 9 -57 C ATOM 3460 NE ARG A 193 7.076 -33.189 22.259 1.00 24.74 N ANISOU 3460 NE ARG B 193 3152 3181 3066 57 -38 -62 N ATOM 3461 CZ ARG A 193 6.397 -34.304 22.540 1.00 27.50 C ANISOU 3461 CZ ARG B 193 3527 3495 3426 40 -44 -25 C ATOM 3462 NH1 ARG A 193 6.506 -34.918 23.721 1.00 29.47 N ANISOU 3462 NH1 ARG B 193 3745 3825 3627 60 -9 -59 N ATOM 3463 NH2 ARG A 193 5.587 -34.817 21.623 1.00 29.24 N ANISOU 3463 NH2 ARG B 193 3760 3770 3578 62 -25 -59 N ATOM 3464 N LYS A 194 10.427 -27.382 23.602 1.00 16.28 N ANISOU 3464 N LYS B 194 2033 2046 2107 21 3 -37 N ATOM 3465 CA LYS A 194 11.439 -26.386 23.228 1.00 17.82 C ANISOU 3465 CA LYS B 194 2241 2244 2284 23 0 1 C ATOM 3466 C LYS A 194 12.182 -26.763 21.958 1.00 18.38 C ANISOU 3466 C LYS B 194 2282 2347 2354 37 1 12 C ATOM 3467 O LYS A 194 12.571 -25.909 21.169 1.00 18.18 O ANISOU 3467 O LYS B 194 2182 2349 2377 92 11 32 O ATOM 3468 CB LYS A 194 12.457 -26.242 24.356 1.00 18.71 C ANISOU 3468 CB LYS B 194 2341 2390 2375 -4 28 -32 C ATOM 3469 CG LYS A 194 11.903 -25.594 25.613 1.00 21.18 C ANISOU 3469 CG LYS B 194 2686 2703 2655 -45 24 -36 C ATOM 3470 CD LYS A 194 13.015 -25.333 26.635 1.00 23.25 C ANISOU 3470 CD LYS B 194 2929 2984 2920 4 -26 -6 C ATOM 3471 CE LYS A 194 13.170 -26.438 27.691 1.00 24.08 C ANISOU 3471 CE LYS B 194 3055 3030 3063 17 -26 -1 C ATOM 3472 NZ LYS A 194 12.292 -27.635 27.513 1.00 25.23 N ANISOU 3472 NZ LYS B 194 3200 3221 3163 12 -38 -55 N ATOM 3473 N GLU A 195 12.390 -28.064 21.799 1.00 19.15 N ANISOU 3473 N GLU B 195 2411 2410 2454 16 -5 -1 N ATOM 3474 CA GLU A 195 13.070 -28.643 20.645 1.00 20.21 C ANISOU 3474 CA GLU B 195 2547 2582 2546 23 -3 -3 C ATOM 3475 C GLU A 195 12.195 -28.617 19.393 1.00 20.59 C ANISOU 3475 C GLU B 195 2591 2663 2566 54 -1 5 C ATOM 3476 O GLU A 195 12.689 -28.798 18.282 1.00 21.04 O ANISOU 3476 O GLU B 195 2642 2762 2590 131 26 11 O ATOM 3477 CB GLU A 195 13.475 -30.096 20.941 1.00 20.36 C ANISOU 3477 CB GLU B 195 2580 2592 2561 19 -1 2 C ATOM 3478 CG GLU A 195 12.308 -31.053 21.225 1.00 21.15 C ANISOU 3478 CG GLU B 195 2645 2696 2694 19 -64 -21 C ATOM 3479 CD GLU A 195 11.940 -31.149 22.710 1.00 22.24 C ANISOU 3479 CD GLU B 195 2711 2995 2743 92 -255 30 C ATOM 3480 OE1 GLU A 195 12.194 -30.194 23.477 1.00 23.92 O ANISOU 3480 OE1 GLU B 195 2969 3329 2789 -35 -306 146 O ATOM 3481 OE2 GLU A 195 11.377 -32.172 23.119 1.00 23.66 O ANISOU 3481 OE2 GLU B 195 2864 3276 2847 106 -368 -76 O ATOM 3482 N ASP A 196 10.891 -28.436 19.586 1.00 20.85 N ANISOU 3482 N ASP B 196 2650 2666 2607 23 2 -14 N ATOM 3483 CA ASP A 196 9.947 -28.335 18.482 1.00 20.98 C ANISOU 3483 CA ASP B 196 2680 2649 2641 26 -22 -10 C ATOM 3484 C ASP A 196 9.814 -26.892 17.985 1.00 21.08 C ANISOU 3484 C ASP B 196 2713 2640 2654 27 -27 -18 C ATOM 3485 O ASP A 196 9.352 -26.676 16.859 1.00 21.09 O ANISOU 3485 O ASP B 196 2787 2596 2628 30 -61 -44 O ATOM 3486 CB ASP A 196 8.579 -28.896 18.904 1.00 21.04 C ANISOU 3486 CB ASP B 196 2709 2643 2641 7 -20 -29 C ATOM 3487 CG ASP A 196 8.571 -30.422 19.011 1.00 21.79 C ANISOU 3487 CG ASP B 196 2837 2788 2653 11 -69 -142 C ATOM 3488 OD1 ASP A 196 9.648 -31.055 18.905 1.00 22.52 O ANISOU 3488 OD1 ASP B 196 3167 2743 2647 34 -32 -406 O ATOM 3489 OD2 ASP A 196 7.526 -31.080 19.210 1.00 22.32 O ANISOU 3489 OD2 ASP B 196 2907 3109 2464 5 -171 -238 O ATOM 3490 N LEU A 197 10.227 -25.920 18.810 1.00 21.00 N ANISOU 3490 N LEU B 197 2714 2625 2640 6 -26 -4 N ATOM 3491 CA LEU A 197 10.137 -24.494 18.477 1.00 21.12 C ANISOU 3491 CA LEU B 197 2711 2653 2658 27 -8 6 C ATOM 3492 C LEU A 197 11.254 -24.073 17.514 1.00 21.28 C ANISOU 3492 C LEU B 197 2785 2639 2661 25 6 6 C ATOM 3493 O LEU A 197 11.206 -22.985 16.918 1.00 21.24 O ANISOU 3493 O LEU B 197 2797 2647 2625 49 -23 -21 O ATOM 3494 CB LEU A 197 10.219 -23.640 19.753 1.00 21.24 C ANISOU 3494 CB LEU B 197 2738 2652 2680 22 33 18 C ATOM 3495 CG LEU A 197 9.082 -23.769 20.777 1.00 21.08 C ANISOU 3495 CG LEU B 197 2683 2661 2664 -1 -2 18 C ATOM 3496 CD1 LEU A 197 9.501 -23.237 22.151 1.00 22.14 C ANISOU 3496 CD1 LEU B 197 2924 2740 2747 -52 56 -57 C ATOM 3497 CD2 LEU A 197 7.872 -23.051 20.295 1.00 20.44 C ANISOU 3497 CD2 LEU B 197 2574 2571 2620 -46 106 -55 C TER 3498 LEU B 197 END