REMARK 4 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 888 REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC) TITLE LUF7357 MODEL 1 ATOM 1 N PRO A 1 7.723 11.755 142.399 1.00138.31 N1+ ANISOU 1 N PRO A 1 18527 21599 12425 -919 -209 -127 ATOM 2 CA PRO A 1 6.346 11.363 142.726 1.00138.99 C ANISOU 2 CA PRO A 1 18827 21554 12427 -1124 -74 77 ATOM 3 C PRO A 1 5.357 11.730 141.611 1.00144.31 C ANISOU 3 C PRO A 1 19555 22419 12856 -1355 136 86 ATOM 4 O PRO A 1 5.776 11.979 140.473 1.00144.78 O ANISOU 4 O PRO A 1 19560 22704 12744 -1319 143 -29 ATOM 5 CB PRO A 1 6.067 12.127 144.025 1.00138.04 C ANISOU 5 CB PRO A 1 18501 21303 12647 -1184 -9 23 ATOM 6 CG PRO A 1 7.418 12.297 144.664 1.00140.40 C ANISOU 6 CG PRO A 1 18613 21557 13175 -951 -184 -107 ATOM 7 CD PRO A 1 8.480 12.147 143.603 1.00137.06 C ANISOU 7 CD PRO A 1 18161 21313 12604 -798 -300 -221 ATOM 8 N CYS A 2 4.042 11.729 141.933 1.00140.99 N ANISOU 8 N CYS A 2 19241 21920 12410 -1599 310 213 ATOM 9 CA CYS A 2 2.969 12.053 140.988 1.00142.63 C ANISOU 9 CA CYS A 2 19492 22313 12389 -1860 539 225 ATOM 10 C CYS A 2 2.853 13.569 140.803 1.00147.05 C ANISOU 10 C CYS A 2 19664 23094 13114 -1932 690 -34 ATOM 11 O CYS A 2 3.273 14.329 141.686 1.00144.04 O ANISOU 11 O CYS A 2 19031 22647 13050 -1838 645 -164 ATOM 12 CB CYS A 2 1.642 11.450 141.445 1.00143.49 C ANISOU 12 CB CYS A 2 19847 22252 12419 -2110 669 441 ATOM 13 SG CYS A 2 0.290 11.657 140.251 1.00150.18 S ANISOU 13 SG CYS A 2 20788 23335 12939 -2469 965 478 ATOM 14 N GLN A 3 2.264 13.999 139.655 1.00146.77 N ANISOU 14 N GLN A 3 19593 23319 12854 -2094 868 -108 ATOM 15 CA GLN A 3 2.023 15.404 139.299 1.00146.30 C ANISOU 15 CA GLN A 3 19184 23497 12905 -2163 1024 -364 ATOM 16 C GLN A 3 1.103 16.051 140.358 1.00149.19 C ANISOU 16 C GLN A 3 19385 23784 13515 -2317 1148 -385 ATOM 17 O GLN A 3 -0.131 15.982 140.257 1.00150.65 O ANISOU 17 O GLN A 3 19636 24027 13579 -2582 1338 -311 ATOM 18 CB GLN A 3 1.432 15.512 137.881 1.00 0.00 C ATOM 19 CG GLN A 3 2.031 14.618 136.782 1.00 0.00 C ATOM 20 CD GLN A 3 1.395 14.781 135.409 1.00 0.00 C ATOM 21 OE1 GLN A 3 1.824 15.600 134.604 1.00 0.00 O ATOM 22 NE2 GLN A 3 0.354 14.004 135.128 1.00 0.00 N ATOM 23 N LYS A 4 1.733 16.627 141.410 1.00142.32 N ANISOU 23 N LYS A 4 18316 22777 12982 -2153 1033 -479 ATOM 24 CA LYS A 4 1.076 17.264 142.553 1.00140.31 C ANISOU 24 CA LYS A 4 17895 22431 12987 -2238 1099 -511 ATOM 25 C LYS A 4 0.327 18.549 142.152 1.00143.66 C ANISOU 25 C LYS A 4 18023 23112 13448 -2364 1293 -727 ATOM 26 O LYS A 4 0.590 19.124 141.089 1.00144.28 O ANISOU 26 O LYS A 4 17982 23425 13415 -2328 1348 -892 ATOM 27 CB LYS A 4 2.109 17.576 143.653 1.00139.73 C ANISOU 27 CB LYS A 4 17696 22167 13228 -2004 916 -564 ATOM 28 CG LYS A 4 2.841 16.317 144.151 1.00 0.00 C ATOM 29 CD LYS A 4 3.285 16.385 145.623 1.00 0.00 C ATOM 30 CE LYS A 4 3.928 15.072 146.097 1.00 0.00 C ATOM 31 NZ LYS A 4 2.944 13.979 146.131 1.00 0.00 N1+ ATOM 32 N VAL A 5 -0.613 18.987 143.010 1.00138.34 N ANISOU 32 N VAL A 5 17227 22406 12928 -2503 1389 -740 ATOM 33 CA VAL A 5 -1.401 20.200 142.786 1.00137.97 C ANISOU 33 CA VAL A 5 16878 22606 12940 -2609 1559 -956 ATOM 34 C VAL A 5 -0.612 21.435 143.235 1.00136.47 C ANISOU 34 C VAL A 5 16398 22419 13036 -2364 1458 -1172 ATOM 35 O VAL A 5 0.199 21.346 144.165 1.00133.02 O ANISOU 35 O VAL A 5 15986 21751 12804 -2192 1290 -1119 ATOM 36 CB VAL A 5 -2.754 20.106 143.515 1.00 0.00 C ATOM 37 CG1 VAL A 5 -3.667 21.314 143.195 1.00 0.00 C ATOM 38 CG2 VAL A 5 -3.661 18.866 143.388 1.00 0.00 C ATOM 39 N ASN A 6 -0.849 22.587 142.566 1.00131.93 N ANISOU 39 N ASN A 6 15558 22105 12464 -2347 1562 -1419 ATOM 40 CA ASN A 6 -0.186 23.851 142.897 1.00128.75 C ANISOU 40 CA ASN A 6 14897 21706 12317 -2116 1477 -1636 ATOM 41 C ASN A 6 -0.991 24.580 143.982 1.00128.21 C ANISOU 41 C ASN A 6 14632 21622 12459 -2154 1514 -1698 ATOM 42 O ASN A 6 -2.024 25.206 143.699 1.00129.48 O ANISOU 42 O ASN A 6 14600 22019 12576 -2285 1672 -1839 ATOM 43 CB ASN A 6 0.033 24.721 141.645 1.00 0.00 C ATOM 44 CG ASN A 6 -1.222 25.234 140.939 1.00 0.00 C ATOM 45 OD1 ASN A 6 -2.345 24.998 141.368 1.00 0.00 O ATOM 46 ND2 ASN A 6 -1.039 25.989 139.859 1.00 0.00 N ATOM 47 N GLU A 7 -0.522 24.441 145.235 1.00118.85 N ANISOU 47 N GLU A 7 13498 20172 11489 -2044 1369 -1594 ATOM 48 CA GLU A 7 -1.101 25.064 146.426 1.00115.99 C ANISOU 48 CA GLU A 7 12979 19754 11338 -2041 1361 -1634 ATOM 49 C GLU A 7 -0.266 26.297 146.801 1.00114.98 C ANISOU 49 C GLU A 7 12663 19581 11443 -1770 1244 -1808 ATOM 50 O GLU A 7 -0.579 26.971 147.782 1.00114.24 O ANISOU 50 O GLU A 7 12434 19440 11533 -1711 1208 -1859 ATOM 51 CB GLU A 7 -1.264 24.092 147.609 1.00 0.00 C ATOM 52 CG GLU A 7 -1.265 24.710 149.016 1.00 0.00 C ATOM 53 CD GLU A 7 -1.426 23.737 150.181 1.00 0.00 C ATOM 54 OE1 GLU A 7 -0.389 23.247 150.680 1.00 0.00 O ATOM 55 OE2 GLU A 7 -2.594 23.504 150.556 1.00 0.00 O1- ATOM 56 N ARG A 8 0.783 26.591 146.004 1.00108.20 N ANISOU 56 N ARG A 8 11810 18734 10567 -1610 1184 -1901 ATOM 57 CA ARG A 8 1.702 27.716 146.197 1.00105.30 C ANISOU 57 CA ARG A 8 11313 18295 10400 -1361 1075 -2062 ATOM 58 C ARG A 8 0.990 29.085 146.228 1.00106.76 C ANISOU 58 C ARG A 8 11225 18683 10656 -1303 1150 -2304 ATOM 59 O ARG A 8 1.270 29.883 147.122 1.00105.75 O ANISOU 59 O ARG A 8 10992 18453 10735 -1124 1058 -2389 ATOM 60 CB ARG A 8 2.891 27.616 145.223 1.00 0.00 C ATOM 61 CG ARG A 8 3.923 26.478 145.393 1.00 0.00 C ATOM 62 CD ARG A 8 5.084 26.378 144.404 1.00 0.00 C ATOM 63 NE ARG A 8 5.959 25.236 144.686 1.00 0.00 N ATOM 64 CZ ARG A 8 7.009 24.870 143.928 1.00 0.00 C ATOM 65 NH1 ARG A 8 7.325 25.570 142.817 1.00 0.00 N ATOM 66 NH2 ARG A 8 7.724 23.790 144.301 1.00 0.00 N1+ ATOM 67 N ALA A 9 0.026 29.352 145.337 1.00 31.02 N ATOM 68 CA ALA A 9 -0.692 30.631 145.321 1.00 32.28 C ATOM 69 C ALA A 9 -1.710 30.740 146.478 1.00 31.44 C ATOM 70 O ALA A 9 -1.989 31.833 146.958 1.00 32.07 O ATOM 71 CB ALA A 9 -1.493 30.778 144.014 1.00 0.00 C ATOM 72 N PHE A 10 -2.282 29.617 146.930 1.00 31.02 N ATOM 73 CA PHE A 10 -3.275 29.581 148.021 1.00 30.54 C ATOM 74 C PHE A 10 -2.561 29.583 149.398 1.00 30.29 C ATOM 75 O PHE A 10 -3.202 29.798 150.424 1.00 30.82 O ATOM 76 CB PHE A 10 -4.225 28.374 147.904 1.00 0.00 C ATOM 77 CG PHE A 10 -5.589 28.673 147.323 1.00 0.00 C ATOM 78 CD1 PHE A 10 -5.794 28.583 145.935 1.00 0.00 C ATOM 79 CD2 PHE A 10 -6.651 29.039 148.167 1.00 0.00 C ATOM 80 CE1 PHE A 10 -7.062 28.853 145.392 1.00 0.00 C ATOM 81 CE2 PHE A 10 -7.920 29.311 147.624 1.00 0.00 C ATOM 82 CZ PHE A 10 -8.125 29.218 146.236 1.00 0.00 C ATOM 83 N GLY A 11 -1.230 29.415 149.439 1.00 27.98 N ATOM 84 CA GLY A 11 -0.428 29.545 150.655 1.00 27.56 C ATOM 85 C GLY A 11 -0.188 31.002 151.070 1.00 27.51 C ATOM 86 O GLY A 11 0.161 31.270 152.215 1.00 28.08 O ATOM 87 N ALA A 12 -0.391 31.942 150.144 1.00 52.35 N ANISOU 87 N ALA A 12 7676 8284 3929 646 -691 1620 ATOM 88 CA ALA A 12 -0.032 33.356 150.218 1.00 51.97 C ANISOU 88 CA ALA A 12 7681 8142 3922 752 -626 1748 ATOM 89 C ALA A 12 -1.060 34.227 150.929 1.00 52.78 C ANISOU 89 C ALA A 12 7681 8260 4112 912 -634 1856 ATOM 90 O ALA A 12 -0.760 35.350 151.331 1.00 52.58 O ANISOU 90 O ALA A 12 7701 8114 4161 1014 -552 1937 ATOM 91 CB ALA A 12 0.083 33.765 148.759 1.00 53.00 C ANISOU 91 CB ALA A 12 7889 8306 3944 742 -662 1825 ATOM 92 N GLN A 13 -2.273 33.709 151.081 1.00 53.86 N ANISOU 92 N GLN A 13 7681 8543 4242 937 -727 1857 ATOM 93 CA GLN A 13 -3.346 34.482 151.692 1.00 55.34 C ANISOU 93 CA GLN A 13 7751 8768 4506 1098 -735 1964 ATOM 94 C GLN A 13 -3.472 34.198 153.182 1.00 52.43 C ANISOU 94 C GLN A 13 7317 8365 4240 1124 -681 1900 ATOM 95 O GLN A 13 -3.973 35.026 153.941 1.00 52.50 O ANISOU 95 O GLN A 13 7278 8335 4334 1272 -635 1979 ATOM 96 CB GLN A 13 -4.677 34.192 150.997 1.00 59.86 C ANISOU 96 CB GLN A 13 8188 9540 5016 1122 -867 2022 ATOM 97 CG GLN A 13 -4.577 34.044 149.491 1.00 64.12 C ANISOU 97 CG GLN A 13 8792 10146 5424 1052 -943 2044 ATOM 98 CD GLN A 13 -5.847 33.480 148.886 1.00 67.45 C ANISOU 98 CD GLN A 13 9074 10779 5775 1037 -1082 2067 ATOM 99 OE1 GLN A 13 -6.791 33.148 149.603 1.00 67.84 O ANISOU 99 OE1 GLN A 13 8967 10932 5877 1067 -1120 2063 ATOM 100 NE2 GLN A 13 -5.877 33.370 147.563 1.00 69.12 N ANISOU 100 NE2 GLN A 13 9339 11061 5862 986 -1157 2091 ATOM 101 N LEU A 14 -3.004 33.026 153.596 1.00 49.46 N ANISOU 101 N LEU A 14 6948 7995 3849 984 -682 1758 ATOM 102 CA LEU A 14 -3.189 32.566 154.967 1.00 46.36 C ANISOU 102 CA LEU A 14 6485 7595 3535 988 -645 1689 ATOM 103 C LEU A 14 -1.934 32.699 155.830 1.00 43.46 C ANISOU 103 C LEU A 14 6236 7051 3227 960 -527 1616 ATOM 104 O LEU A 14 -2.002 33.172 156.962 1.00 42.60 O ANISOU 104 O LEU A 14 6113 6871 3202 1050 -458 1629 ATOM 105 CB LEU A 14 -3.657 31.110 154.966 1.00 45.48 C ANISOU 105 CB LEU A 14 6288 7618 3375 851 -730 1580 ATOM 106 CG LEU A 14 -3.678 30.405 156.321 1.00 43.85 C ANISOU 106 CG LEU A 14 6027 7401 3232 816 -693 1488 ATOM 107 CD1 LEU A 14 -4.732 31.019 157.231 1.00 44.40 C ANISOU 107 CD1 LEU A 14 5965 7529 3377 964 -682 1576 ATOM 108 CD2 LEU A 14 -3.910 28.913 156.142 1.00 43.48 C ANISOU 108 CD2 LEU A 14 5937 7455 3131 653 -767 1370 ATOM 109 N LEU A 15 -0.792 32.277 155.297 1.00 41.89 N ANISOU 109 N LEU A 15 6149 6784 2982 838 -501 1540 ATOM 110 CA LEU A 15 0.445 32.234 156.077 1.00 39.94 C ANISOU 110 CA LEU A 15 5995 6392 2787 788 -398 1460 ATOM 111 C LEU A 15 0.968 33.604 156.540 1.00 40.85 C ANISOU 111 C LEU A 15 6193 6353 2976 897 -296 1539 ATOM 112 O LEU A 15 1.415 33.724 157.681 1.00 40.47 O ANISOU 112 O LEU A 15 6173 6207 2998 912 -220 1492 ATOM 113 CB LEU A 15 1.541 31.505 155.290 1.00 38.04 C ANISOU 113 CB LEU A 15 5846 6127 2481 641 -390 1373 ATOM 114 CG LEU A 15 1.727 30.013 155.580 1.00 36.65 C ANISOU 114 CG LEU A 15 5650 5993 2284 513 -416 1230 ATOM 115 CD1 LEU A 15 0.404 29.273 155.513 1.00 37.39 C ANISOU 115 CD1 LEU A 15 5629 6234 2344 506 -521 1220 ATOM 116 CD2 LEU A 15 2.734 29.397 154.620 1.00 36.15 C ANISOU 116 CD2 LEU A 15 5684 5903 2147 396 -402 1162 ATOM 117 N PRO A 16 0.936 34.636 155.669 1.00 42.89 N ANISOU 117 N PRO A 16 6502 6580 3216 967 -291 1655 ATOM 118 CA PRO A 16 1.438 35.919 156.185 1.00 43.02 C ANISOU 118 CA PRO A 16 6612 6425 3309 1063 -185 1721 ATOM 119 C PRO A 16 0.646 36.500 157.375 1.00 43.82 C ANISOU 119 C PRO A 16 6671 6481 3497 1210 -147 1760 ATOM 120 O PRO A 16 1.289 36.939 158.329 1.00 43.34 O ANISOU 120 O PRO A 16 6693 6271 3503 1227 -50 1727 ATOM 121 CB PRO A 16 1.354 36.843 154.963 1.00 44.40 C ANISOU 121 CB PRO A 16 6837 6590 3442 1115 -199 1847 ATOM 122 CG PRO A 16 1.465 35.928 153.801 1.00 44.63 C ANISOU 122 CG PRO A 16 6848 6747 3361 991 -283 1808 ATOM 123 CD PRO A 16 0.735 34.681 154.208 1.00 43.88 C ANISOU 123 CD PRO A 16 6638 6788 3248 941 -362 1716 ATOM 124 N PRO A 17 -0.702 36.504 157.339 1.00 45.18 N ANISOU 124 N PRO A 17 6719 6779 3669 1314 -216 1827 ATOM 125 CA PRO A 17 -1.344 37.034 158.549 1.00 45.44 C ANISOU 125 CA PRO A 17 6718 6759 3787 1457 -159 1856 ATOM 126 C PRO A 17 -1.274 36.082 159.744 1.00 44.58 C ANISOU 126 C PRO A 17 6563 6675 3699 1394 -145 1736 ATOM 127 O PRO A 17 -1.215 36.544 160.884 1.00 43.74 O ANISOU 127 O PRO A 17 6501 6458 3659 1473 -60 1726 ATOM 128 CB PRO A 17 -2.796 37.244 158.112 1.00 47.05 C ANISOU 128 CB PRO A 17 6778 7114 3983 1581 -238 1965 ATOM 129 CG PRO A 17 -2.998 36.275 157.009 1.00 47.28 C ANISOU 129 CG PRO A 17 6736 7316 3914 1452 -359 1937 ATOM 130 CD PRO A 17 -1.690 36.222 156.280 1.00 46.39 C ANISOU 130 CD PRO A 17 6766 7109 3752 1325 -332 1891 ATOM 131 N LEU A 18 -1.280 34.777 159.488 1.00 44.37 N ANISOU 131 N LEU A 18 6462 6783 3613 1253 -224 1645 ATOM 132 CA LEU A 18 -1.244 33.793 160.566 1.00 35.27 C ANISOU 132 CA LEU A 18 5262 5663 2476 1184 -217 1532 ATOM 133 C LEU A 18 0.067 33.854 161.338 1.00 42.94 C ANISOU 133 C LEU A 18 6367 6465 3483 1120 -119 1443 ATOM 134 O LEU A 18 0.071 33.963 162.564 1.00 42.12 O ANISOU 134 O LEU A 18 6257 6271 3473 1134 -56 1375 ATOM 135 CB LEU A 18 -1.453 32.383 160.017 1.00 34.88 C ANISOU 135 CB LEU A 18 5128 5768 2358 1032 -318 1450 ATOM 136 CG LEU A 18 -1.382 31.261 161.052 1.00 33.48 C ANISOU 136 CG LEU A 18 4906 5621 2193 942 -313 1330 ATOM 137 CD1 LEU A 18 -2.480 31.428 162.086 1.00 33.84 C ANISOU 137 CD1 LEU A 18 4835 5718 2307 1041 -303 1357 ATOM 138 CD2 LEU A 18 -1.472 29.901 160.381 1.00 33.27 C ANISOU 138 CD2 LEU A 18 4831 5709 2101 783 -403 1245 ATOM 139 N TYR A 19 1.179 33.782 160.613 1.00 41.60 N ANISOU 139 N TYR A 19 6291 6233 3283 1016 -105 1408 ATOM 140 CA TYR A 19 2.498 33.794 161.235 1.00 38.08 C ANISOU 140 CA TYR A 19 5956 5644 2869 940 -19 1325 ATOM 141 C TYR A 19 2.777 35.127 161.918 1.00 39.00 C ANISOU 141 C TYR A 19 6167 5578 3075 1028 80 1365 ATOM 142 O TYR A 19 3.472 35.179 162.931 1.00 38.73 O ANISOU 142 O TYR A 19 6179 5425 3113 974 146 1272 ATOM 143 CB TYR A 19 3.585 33.496 160.201 1.00 35.68 C ANISOU 143 CB TYR A 19 5710 5326 2520 815 -23 1292 ATOM 144 CG TYR A 19 3.559 32.079 159.675 1.00 34.26 C ANISOU 144 CG TYR A 19 5462 5275 2280 692 -99 1206 ATOM 145 CD1 TYR A 19 2.850 31.083 160.336 1.00 30.84 C ANISOU 145 CD1 TYR A 19 4937 4933 1849 668 -147 1140 ATOM 146 CD2 TYR A 19 4.247 31.735 158.520 1.00 33.90 C ANISOU 146 CD2 TYR A 19 5455 5251 2175 598 -116 1190 ATOM 147 CE1 TYR A 19 2.825 29.786 159.857 1.00 34.32 C ANISOU 147 CE1 TYR A 19 5337 5465 2237 550 -210 1058 ATOM 148 CE2 TYR A 19 4.228 30.440 158.035 1.00 33.34 C ANISOU 148 CE2 TYR A 19 5348 5272 2046 489 -175 1106 ATOM 149 CZ TYR A 19 3.516 29.471 158.706 1.00 30.74 C ANISOU 149 CZ TYR A 19 4941 5015 1725 464 -222 1038 ATOM 150 OH TYR A 19 3.495 28.184 158.225 1.00 30.56 O ANISOU 150 OH TYR A 19 4906 5058 1646 355 -275 951 ATOM 151 N SER A 20 2.231 36.203 161.361 1.00 40.59 N ANISOU 151 N SER A 20 6400 5752 3272 1160 88 1500 ATOM 152 CA SER A 20 2.386 37.524 161.959 1.00 42.61 C ANISOU 152 CA SER A 20 6757 5816 3616 1251 186 1540 ATOM 153 C SER A 20 1.684 37.589 163.310 1.00 44.05 C ANISOU 153 C SER A 20 6882 5963 3891 1316 221 1480 ATOM 154 O SER A 20 2.227 38.123 164.275 1.00 43.76 O ANISOU 154 O SER A 20 6932 5764 3931 1301 307 1414 ATOM 155 CB SER A 20 1.837 38.606 161.030 1.00 44.20 C ANISOU 155 CB SER A 20 6999 6000 3795 1392 186 1707 ATOM 156 OG SER A 20 2.501 38.583 159.779 1.00 44.74 O ANISOU 156 OG SER A 20 7098 6092 3811 1297 155 1729 ATOM 157 N LEU A 21 0.477 37.034 163.371 1.00 46.29 N ANISOU 157 N LEU A 21 7019 6408 4162 1381 153 1502 ATOM 158 CA LEU A 21 -0.306 37.027 164.600 1.00 47.23 C ANISOU 158 CA LEU A 21 7066 6521 4360 1449 187 1455 ATOM 159 C LEU A 21 0.353 36.146 165.657 1.00 44.37 C ANISOU 159 C LEU A 21 6702 6132 4026 1307 207 1295 ATOM 160 O LEU A 21 0.374 36.487 166.840 1.00 44.29 O ANISOU 160 O LEU A 21 6723 6016 4088 1331 281 1230 ATOM 161 CB LEU A 21 -1.732 36.548 164.324 1.00 50.51 C ANISOU 161 CB LEU A 21 7303 7140 4746 1533 104 1523 ATOM 162 CG LEU A 21 -2.788 36.962 165.349 1.00 55.18 C ANISOU 162 CG LEU A 21 7817 7729 5420 1673 155 1536 ATOM 163 CD1 LEU A 21 -2.878 38.477 165.437 1.00 60.41 C ANISOU 163 CD1 LEU A 21 8592 8220 6142 1843 250 1627 ATOM 164 CD2 LEU A 21 -4.140 36.365 164.994 1.00 57.05 C ANISOU 164 CD2 LEU A 21 7854 8198 5623 1730 62 1606 ATOM 165 N VAL A 22 0.890 35.013 165.217 1.00 42.26 N ANISOU 165 N VAL A 22 6402 5959 3695 1165 144 1233 ATOM 166 CA VAL A 22 1.634 34.121 166.098 1.00 39.91 C ANISOU 166 CA VAL A 22 6110 5637 3418 1030 158 1093 ATOM 167 C VAL A 22 2.888 34.814 166.622 1.00 38.78 C ANISOU 167 C VAL A 22 6108 5308 3320 981 244 1041 ATOM 168 O VAL A 22 3.231 34.696 167.798 1.00 38.66 O ANISOU 168 O VAL A 22 6111 5223 3355 938 288 946 ATOM 169 CB VAL A 22 2.027 32.817 165.374 1.00 38.81 C ANISOU 169 CB VAL A 22 5927 5621 3199 900 81 1048 ATOM 170 CG1 VAL A 22 3.007 32.010 166.206 1.00 28.17 C ANISOU 170 CG1 VAL A 22 4607 4223 1873 773 107 918 ATOM 171 CG2 VAL A 22 0.787 31.997 165.056 1.00 30.06 C ANISOU 171 CG2 VAL A 22 4676 4698 2047 915 -7 1074 ATOM 172 N PHE A 23 3.558 35.550 165.742 1.00 38.97 N ANISOU 172 N PHE A 23 6229 5257 3321 981 264 1106 ATOM 173 CA PHE A 23 4.785 36.251 166.100 1.00 36.84 C ANISOU 173 CA PHE A 23 6090 4817 3089 916 342 1067 ATOM 174 C PHE A 23 4.548 37.300 167.177 1.00 37.77 C ANISOU 174 C PHE A 23 6278 4783 3289 993 423 1052 ATOM 175 O PHE A 23 5.326 37.410 168.122 1.00 37.67 O ANISOU 175 O PHE A 23 6327 4669 3318 913 472 957 ATOM 176 CB PHE A 23 5.406 36.914 164.870 1.00 36.52 C ANISOU 176 CB PHE A 23 6138 4732 3006 910 354 1160 ATOM 177 CG PHE A 23 6.635 37.721 165.175 1.00 36.21 C ANISOU 177 CG PHE A 23 6229 4520 3009 835 435 1131 ATOM 178 CD1 PHE A 23 7.861 37.102 165.338 1.00 35.09 C ANISOU 178 CD1 PHE A 23 6094 4379 2859 686 441 1043 ATOM 179 CD2 PHE A 23 6.565 39.099 165.298 1.00 37.33 C ANISOU 179 CD2 PHE A 23 6485 4497 3200 911 508 1194 ATOM 180 CE1 PHE A 23 8.995 37.840 165.619 1.00 34.64 C ANISOU 180 CE1 PHE A 23 6142 4180 2840 602 510 1019 ATOM 181 CE2 PHE A 23 7.696 39.842 165.579 1.00 37.02 C ANISOU 181 CE2 PHE A 23 6570 4297 3200 820 581 1164 ATOM 182 CZ PHE A 23 8.912 39.210 165.740 1.00 35.36 C ANISOU 182 CZ PHE A 23 6350 4108 2979 660 578 1076 ATOM 183 N VAL A 24 3.476 38.071 167.027 1.00 39.94 N ANISOU 183 N VAL A 24 6547 5045 3585 1151 439 1146 ATOM 184 CA VAL A 24 3.171 39.147 167.962 1.00 42.41 C ANISOU 184 CA VAL A 24 6943 5200 3972 1246 529 1139 ATOM 185 C VAL A 24 2.865 38.603 169.355 1.00 43.22 C ANISOU 185 C VAL A 24 6990 5321 4110 1227 547 1022 ATOM 186 O VAL A 24 3.435 39.060 170.346 1.00 42.68 O ANISOU 186 O VAL A 24 7018 5115 4083 1183 615 937 ATOM 187 CB VAL A 24 1.983 39.998 167.476 1.00 0.00 C ATOM 188 CG1 VAL A 24 2.174 40.322 165.993 1.00 0.00 C ATOM 189 CG2 VAL A 24 0.640 39.278 167.658 1.00 0.00 C ATOM 190 N ILE A 25 1.971 37.622 169.424 1.00 44.68 N ANISOU 190 N ILE A 25 7022 5682 4273 1250 484 1019 ATOM 191 CA ILE A 25 1.586 37.035 170.703 1.00 46.65 C ANISOU 191 CA ILE A 25 7209 5966 4548 1234 501 921 ATOM 192 C ILE A 25 2.754 36.296 171.350 1.00 42.89 C ANISOU 192 C ILE A 25 6768 5467 4063 1061 494 797 ATOM 193 O ILE A 25 2.976 36.402 172.556 1.00 42.20 O ANISOU 193 O ILE A 25 6724 5306 4005 1034 546 707 ATOM 194 CB ILE A 25 0.395 36.074 170.530 1.00 0.00 C ATOM 195 CG1 ILE A 25 0.864 34.682 170.056 1.00 0.00 C ATOM 196 CG2 ILE A 25 -0.659 36.665 169.577 1.00 0.00 C ATOM 197 CD1 ILE A 25 -0.200 33.595 169.835 1.00 0.00 C ATOM 198 N GLY A 26 3.498 35.549 170.542 1.00 41.20 N ANISOU 198 N GLY A 26 6533 5319 3801 951 431 793 ATOM 199 CA GLY A 26 4.591 34.739 171.046 1.00 39.98 C ANISOU 199 CA GLY A 26 6391 5164 3635 801 418 690 ATOM 200 C GLY A 26 5.781 35.544 171.523 1.00 39.42 C ANISOU 200 C GLY A 26 6451 4934 3593 732 479 641 ATOM 201 O GLY A 26 6.421 35.193 172.516 1.00 27.08 O ANISOU 201 O GLY A 26 4904 3345 2041 644 491 545 ATOM 202 N LEU A 27 6.083 36.624 170.813 1.00 39.23 N ANISOU 202 N LEU A 27 6523 4806 3579 765 515 710 ATOM 203 CA LEU A 27 7.225 37.450 171.165 1.00 39.56 C ANISOU 203 CA LEU A 27 6692 4691 3646 682 573 670 ATOM 204 C LEU A 27 6.994 38.137 172.504 1.00 40.97 C ANISOU 204 C LEU A 27 6945 4752 3870 712 639 600 ATOM 205 O LEU A 27 7.802 37.999 173.417 1.00 43.84 O ANISOU 205 O LEU A 27 7343 5074 4239 603 651 502 ATOM 206 CB LEU A 27 7.508 38.495 170.070 1.00 0.00 C ATOM 207 CG LEU A 27 8.689 39.490 170.184 1.00 0.00 C ATOM 208 CD1 LEU A 27 10.042 38.783 170.201 1.00 0.00 C ATOM 209 CD2 LEU A 27 8.639 40.521 169.056 1.00 0.00 C ATOM 210 N VAL A 28 5.885 38.860 172.625 1.00 37.80 N ANISOU 210 N VAL A 28 6565 4303 3496 864 683 651 ATOM 211 CA VAL A 28 5.580 39.561 173.868 1.00 37.82 C ANISOU 211 CA VAL A 28 6650 4186 3535 910 760 583 ATOM 212 C VAL A 28 5.314 38.575 175.005 1.00 37.89 C ANISOU 212 C VAL A 28 6570 4296 3529 873 739 486 ATOM 213 O VAL A 28 5.516 38.896 176.174 1.00 37.92 O ANISOU 213 O VAL A 28 6649 4216 3542 843 789 395 ATOM 214 CB VAL A 28 4.365 40.509 173.712 1.00 37.47 C ANISOU 214 CB VAL A 28 6637 4077 3525 1108 821 669 ATOM 215 CG1 VAL A 28 4.597 41.481 172.566 1.00 38.76 C ANISOU 215 CG1 VAL A 28 6893 4136 3698 1153 842 780 ATOM 216 CG2 VAL A 28 3.081 39.723 173.493 1.00 37.11 C ANISOU 216 CG2 VAL A 28 6420 4214 3466 1221 773 725 ATOM 217 N GLY A 29 4.874 37.370 174.654 1.00 37.39 N ANISOU 217 N GLY A 29 6359 4411 3437 868 664 506 ATOM 218 CA GLY A 29 4.588 36.347 175.642 1.00 35.45 C ANISOU 218 CA GLY A 29 6026 4267 3175 831 643 430 ATOM 219 C GLY A 29 5.851 35.820 176.290 1.00 36.27 C ANISOU 219 C GLY A 29 6163 4357 3259 670 621 333 ATOM 220 O GLY A 29 6.015 35.904 177.508 1.00 37.33 O ANISOU 220 O GLY A 29 6343 4448 3392 637 656 248 ATOM 221 N ASN A 30 6.748 35.277 175.473 1.00 37.19 N ANISOU 221 N ASN A 30 6255 4520 3356 575 566 348 ATOM 222 CA ASN A 30 8.005 34.730 175.971 1.00 36.85 C ANISOU 222 CA ASN A 30 6223 4481 3296 430 540 272 ATOM 223 C ASN A 30 8.953 35.809 176.479 1.00 36.66 C ANISOU 223 C ASN A 30 6330 4310 3290 360 589 224 ATOM 224 O ASN A 30 9.818 35.539 177.309 1.00 36.99 O ANISOU 224 O ASN A 30 6386 4349 3318 252 577 146 ATOM 225 CB ASN A 30 8.698 33.907 174.886 1.00 37.79 C ANISOU 225 CB ASN A 30 6280 4687 3391 362 481 307 ATOM 226 CG ASN A 30 8.035 32.566 174.666 1.00 40.44 C ANISOU 226 CG ASN A 30 6495 5170 3700 380 424 316 ATOM 227 OD1 ASN A 30 8.285 31.609 175.401 1.00 40.38 O ANISOU 227 OD1 ASN A 30 6443 5221 3680 322 399 257 ATOM 228 ND2 ASN A 30 7.188 32.484 173.646 1.00 40.87 N ANISOU 228 ND2 ASN A 30 6501 5285 3743 455 401 392 ATOM 229 N ILE A 31 8.796 37.029 175.976 1.00 36.51 N ANISOU 229 N ILE A 31 6407 4167 3298 417 642 274 ATOM 230 CA ILE A 31 9.606 38.138 176.456 1.00 37.80 C ANISOU 230 CA ILE A 31 6712 4171 3480 344 696 227 ATOM 231 C ILE A 31 9.185 38.496 177.875 1.00 38.85 C ANISOU 231 C ILE A 31 6909 4239 3612 366 743 137 ATOM 232 O ILE A 31 10.025 38.799 178.722 1.00 38.59 O ANISOU 232 O ILE A 31 6953 4141 3569 252 754 51 ATOM 233 CB ILE A 31 9.475 39.362 175.531 1.00 0.00 C ATOM 234 CG1 ILE A 31 8.030 39.902 175.519 1.00 0.00 C ATOM 235 CG2 ILE A 31 9.964 39.036 174.109 1.00 0.00 C ATOM 236 CD1 ILE A 31 7.721 41.129 174.646 1.00 0.00 C ATOM 237 N LEU A 32 7.880 38.453 178.128 1.00 39.95 N ANISOU 237 N LEU A 32 7014 4407 3758 511 772 159 ATOM 238 CA LEU A 32 7.351 38.727 179.459 1.00 40.31 C ANISOU 238 CA LEU A 32 7114 4406 3796 551 828 78 ATOM 239 C LEU A 32 7.799 37.657 180.440 1.00 44.49 C ANISOU 239 C LEU A 32 7578 5045 4282 445 778 -7 ATOM 240 O LEU A 32 8.102 37.951 181.595 1.00 46.72 O ANISOU 240 O LEU A 32 7943 5271 4539 390 808 -101 ATOM 241 CB LEU A 32 5.825 38.812 179.433 1.00 37.51 C ANISOU 241 CB LEU A 32 6707 4086 3461 737 871 133 ATOM 242 CG LEU A 32 5.239 40.213 179.621 1.00 38.56 C ANISOU 242 CG LEU A 32 6977 4046 3628 863 977 144 ATOM 243 CD1 LEU A 32 5.743 41.169 178.546 1.00 40.33 C ANISOU 243 CD1 LEU A 32 7299 4141 3885 862 992 217 ATOM 244 CD2 LEU A 32 3.722 40.157 179.629 1.00 39.18 C ANISOU 244 CD2 LEU A 32 6968 4193 3725 1054 1016 206 ATOM 245 N VAL A 33 7.811 36.393 179.992 1.00 43.47 N ANISOU 245 N VAL A 33 7309 5070 4137 419 702 28 ATOM 246 CA VAL A 33 8.323 35.259 180.763 1.00 42.51 C ANISOU 246 CA VAL A 33 7123 5054 3976 322 650 -34 ATOM 247 C VAL A 33 9.784 35.489 181.189 1.00 43.02 C ANISOU 247 C VAL A 33 7257 5067 4023 171 629 -100 ATOM 248 O VAL A 33 10.115 35.321 182.363 1.00 44.39 O ANISOU 248 O VAL A 33 7458 5250 4160 105 625 -180 ATOM 249 CB VAL A 33 8.175 33.933 179.962 1.00 25.50 C ANISOU 249 CB VAL A 33 4826 3049 1815 316 577 21 ATOM 250 CG1 VAL A 33 8.984 32.722 180.469 1.00 24.60 C ANISOU 250 CG1 VAL A 33 4663 3020 1665 207 523 -33 ATOM 251 CG2 VAL A 33 6.689 33.560 179.862 1.00 25.54 C ANISOU 251 CG2 VAL A 33 4744 3133 1826 439 586 70 ATOM 252 N VAL A 34 10.607 35.977 180.254 1.00 42.20 N ANISOU 252 N VAL A 34 7177 4916 3942 113 616 -61 ATOM 253 CA VAL A 34 12.014 36.251 180.527 1.00 40.99 C ANISOU 253 CA VAL A 34 7071 4726 3778 -41 594 -111 ATOM 254 C VAL A 34 12.187 37.429 181.484 1.00 42.28 C ANISOU 254 C VAL A 34 7385 4745 3934 -85 650 -191 ATOM 255 O VAL A 34 12.969 37.355 182.434 1.00 44.36 O ANISOU 255 O VAL A 34 7674 5021 4161 -202 625 -271 ATOM 256 CB VAL A 34 12.790 36.535 179.225 1.00 41.61 C ANISOU 256 CB VAL A 34 7143 4783 3884 -88 583 -43 ATOM 257 CG1 VAL A 34 14.184 37.059 179.533 1.00 42.25 C ANISOU 257 CG1 VAL A 34 7280 4812 3962 -250 575 -91 ATOM 258 CG2 VAL A 34 12.864 35.280 178.371 1.00 40.56 C ANISOU 258 CG2 VAL A 34 6873 4796 3743 -73 525 15 ATOM 259 N LEU A 35 11.454 38.509 181.232 1.00 42.16 N ANISOU 259 N LEU A 35 7475 4595 3950 10 726 -169 ATOM 260 CA LEU A 35 11.514 39.693 182.085 1.00 43.80 C ANISOU 260 CA LEU A 35 7851 4640 4152 -19 795 -249 ATOM 261 C LEU A 35 11.176 39.345 183.530 1.00 41.63 C ANISOU 261 C LEU A 35 7590 4405 3822 -22 801 -346 ATOM 262 O LEU A 35 11.818 39.827 184.461 1.00 42.62 O ANISOU 262 O LEU A 35 7818 4466 3909 -135 809 -443 ATOM 263 CB LEU A 35 10.564 40.779 181.570 1.00 46.64 C ANISOU 263 CB LEU A 35 8312 4852 4556 127 885 -197 ATOM 264 CG LEU A 35 10.944 41.454 180.250 1.00 47.85 C ANISOU 264 CG LEU A 35 8504 4921 4757 123 898 -105 ATOM 265 CD1 LEU A 35 9.852 42.415 179.799 1.00 48.66 C ANISOU 265 CD1 LEU A 35 8694 4893 4901 299 984 -38 ATOM 266 CD2 LEU A 35 12.280 42.173 180.375 1.00 48.77 C ANISOU 266 CD2 LEU A 35 8728 4928 4872 -63 899 -157 ATOM 267 N VAL A 36 10.131 38.514 183.727 1.00 38.27 N ANISOU 267 N VAL A 36 7062 4093 3387 94 797 -319 ATOM 268 CA VAL A 36 9.700 37.975 185.026 1.00 35.66 C ANISOU 268 CA VAL A 36 6731 3818 2999 100 808 -397 ATOM 269 C VAL A 36 10.802 37.122 185.681 1.00 37.32 C ANISOU 269 C VAL A 36 6891 4134 3154 -55 722 -450 ATOM 270 O VAL A 36 11.160 37.351 186.839 1.00 39.27 O ANISOU 270 O VAL A 36 7221 4358 3343 -134 728 -544 ATOM 271 CB VAL A 36 8.390 37.124 184.904 1.00 0.00 C ATOM 272 CG1 VAL A 36 8.101 36.120 186.046 1.00 0.00 C ATOM 273 CG2 VAL A 36 7.165 38.030 184.721 1.00 0.00 C ATOM 274 N LEU A 37 11.364 36.177 184.920 1.00 36.86 N ANISOU 274 N LEU A 37 6701 4192 3110 -96 644 -388 ATOM 275 CA LEU A 37 12.438 35.307 185.391 1.00 36.11 C ANISOU 275 CA LEU A 37 6539 4212 2971 -220 561 -418 ATOM 276 C LEU A 37 13.681 36.076 185.864 1.00 38.90 C ANISOU 276 C LEU A 37 6975 4502 3301 -379 539 -483 ATOM 277 O LEU A 37 14.335 35.610 186.798 1.00 39.06 O ANISOU 277 O LEU A 37 6972 4602 3266 -481 481 -532 ATOM 278 CB LEU A 37 12.790 34.264 184.316 1.00 31.63 C ANISOU 278 CB LEU A 37 5825 3761 2432 -217 497 -336 ATOM 279 CG LEU A 37 11.736 33.147 184.183 1.00 29.48 C ANISOU 279 CG LEU A 37 5451 3585 2164 -104 494 -284 ATOM 280 CD1 LEU A 37 11.959 32.338 182.900 1.00 29.66 C ANISOU 280 CD1 LEU A 37 5361 3696 2214 -110 438 -212 ATOM 281 CD2 LEU A 37 11.660 32.234 185.426 1.00 25.25 C ANISOU 281 CD2 LEU A 37 4894 3129 1569 -111 480 -330 ATOM 282 N VAL A 38 13.937 37.258 185.282 1.00 41.10 N ANISOU 282 N VAL A 38 7352 4642 3622 -403 583 -479 ATOM 283 CA VAL A 38 15.143 38.030 185.557 1.00 42.83 C ANISOU 283 CA VAL A 38 7652 4794 3826 -571 565 -537 ATOM 284 C VAL A 38 14.905 39.130 186.595 1.00 47.74 C ANISOU 284 C VAL A 38 8455 5275 4409 -604 627 -643 ATOM 285 O VAL A 38 15.757 39.382 187.447 1.00 49.39 O ANISOU 285 O VAL A 38 8719 5486 4563 -754 591 -727 ATOM 286 CB VAL A 38 15.704 38.660 184.269 1.00 0.00 C ATOM 287 CG1 VAL A 38 15.716 37.604 183.162 1.00 0.00 C ATOM 288 CG2 VAL A 38 14.872 39.861 183.799 1.00 0.00 C ATOM 289 N GLN A 39 13.741 39.770 186.537 1.00 51.30 N ANISOU 289 N GLN A 39 9000 5609 4884 -461 721 -641 ATOM 290 CA GLN A 39 13.474 40.927 187.387 1.00 55.60 C ANISOU 290 CA GLN A 39 9740 5987 5397 -474 802 -741 ATOM 291 C GLN A 39 12.534 40.649 188.560 1.00 54.96 C ANISOU 291 C GLN A 39 9690 5939 5252 -382 844 -806 ATOM 292 O GLN A 39 12.263 41.540 189.366 1.00 57.31 O ANISOU 292 O GLN A 39 10156 6106 5511 -384 919 -900 ATOM 293 CB GLN A 39 12.908 42.080 186.538 1.00 0.00 C ATOM 294 CG GLN A 39 13.164 42.050 185.022 1.00 0.00 C ATOM 295 CD GLN A 39 12.574 43.222 184.251 1.00 0.00 C ATOM 296 OE1 GLN A 39 13.216 44.251 184.069 1.00 0.00 O ATOM 297 NE2 GLN A 39 11.334 43.083 183.793 1.00 0.00 N ATOM 298 N TYR A 40 12.039 39.421 188.660 1.00 52.14 N ANISOU 298 N TYR A 40 9179 5752 4880 -306 803 -758 ATOM 299 CA TYR A 40 11.200 39.039 189.792 1.00 52.40 C ANISOU 299 CA TYR A 40 9225 5839 4846 -233 841 -811 ATOM 300 C TYR A 40 11.762 37.809 190.499 1.00 51.18 C ANISOU 300 C TYR A 40 8958 5867 4620 -322 743 -823 ATOM 301 O TYR A 40 11.970 37.824 191.711 1.00 51.94 O ANISOU 301 O TYR A 40 9113 5987 4634 -390 735 -908 ATOM 302 CB TYR A 40 9.752 38.779 189.337 1.00 0.00 C ATOM 303 CG TYR A 40 8.966 40.009 188.959 1.00 0.00 C ATOM 304 CD1 TYR A 40 9.429 41.306 189.302 1.00 0.00 C ATOM 305 CD2 TYR A 40 7.869 39.898 188.123 1.00 0.00 C ATOM 306 CE1 TYR A 40 9.178 42.373 188.426 1.00 0.00 C ATOM 307 CE2 TYR A 40 7.434 41.035 187.431 1.00 0.00 C ATOM 308 CZ TYR A 40 8.138 42.259 187.530 1.00 0.00 C ATOM 309 OH TYR A 40 7.844 43.412 186.897 1.00 0.00 O ATOM 310 N LYS A 41 12.008 36.748 189.738 1.00 50.51 N ANISOU 310 N LYS A 41 8708 5911 4574 -317 668 -731 ATOM 311 CA LYS A 41 12.586 35.527 190.290 1.00 50.53 C ANISOU 311 CA LYS A 41 8599 6078 4520 -388 577 -725 ATOM 312 C LYS A 41 14.100 35.663 190.425 1.00 53.05 C ANISOU 312 C LYS A 41 8924 6422 4813 -567 491 -758 ATOM 313 O LYS A 41 14.714 35.006 191.268 1.00 55.67 O ANISOU 313 O LYS A 41 9206 6866 5079 -646 419 -781 ATOM 314 CB LYS A 41 12.239 34.321 189.414 1.00 48.82 C ANISOU 314 CB LYS A 41 8216 5977 4356 -309 538 -617 ATOM 315 CG LYS A 41 11.158 33.405 189.986 1.00 48.28 C ANISOU 315 CG LYS A 41 8087 6001 4258 -209 562 -597 ATOM 316 CD LYS A 41 11.732 32.468 191.040 1.00 48.97 C ANISOU 316 CD LYS A 41 8103 6211 4294 -283 487 -612 ATOM 317 CE LYS A 41 10.738 31.380 191.434 1.00 48.55 C ANISOU 317 CE LYS A 41 7944 6257 4245 -193 497 -564 ATOM 318 NZ LYS A 41 11.336 30.387 192.376 1.00 47.44 N1+ ANISOU 318 NZ LYS A 41 7720 6233 4073 -252 419 -557 ATOM 319 N ARG A 42 14.687 36.512 189.580 1.00 53.75 N ANISOU 319 N ARG A 42 9054 6409 4960 -624 498 -749 ATOM 320 CA ARG A 42 16.120 36.835 189.604 1.00 54.74 C ANISOU 320 CA ARG A 42 9183 6544 5071 -804 429 -778 ATOM 321 C ARG A 42 16.983 35.592 189.314 1.00 51.81 C ANISOU 321 C ARG A 42 8633 6351 4702 -849 327 -709 ATOM 322 O ARG A 42 18.181 35.570 189.582 1.00 50.83 O ANISOU 322 O ARG A 42 8473 6290 4549 -993 253 -729 ATOM 323 CB ARG A 42 16.485 37.494 190.947 1.00 0.00 C ATOM 324 CG ARG A 42 17.016 38.945 190.966 1.00 0.00 C ATOM 325 CD ARG A 42 17.374 39.585 192.308 1.00 0.00 C ATOM 326 NE ARG A 42 17.861 40.960 192.156 1.00 0.00 N ATOM 327 CZ ARG A 42 19.146 41.298 191.947 1.00 0.00 C ATOM 328 NH1 ARG A 42 20.106 40.348 191.922 1.00 0.00 N ATOM 329 NH2 ARG A 42 19.447 42.601 191.776 1.00 0.00 N1+ ATOM 330 N LEU A 43 16.360 34.572 188.730 1.00 49.23 N ANISOU 330 N LEU A 43 8192 6101 4412 -724 326 -627 ATOM 331 CA LEU A 43 17.053 33.340 188.339 1.00 45.94 C ANISOU 331 CA LEU A 43 7617 5832 4007 -737 247 -556 ATOM 332 C LEU A 43 17.793 32.685 189.503 1.00 47.86 C ANISOU 332 C LEU A 43 7819 6199 4166 -822 168 -589 ATOM 333 O LEU A 43 18.992 32.419 189.418 1.00 48.28 O ANISOU 333 O LEU A 43 7792 6335 4216 -920 96 -570 ATOM 334 CB LEU A 43 18.040 33.618 187.200 1.00 41.68 C ANISOU 334 CB LEU A 43 7024 5282 3531 -806 226 -508 ATOM 335 CG LEU A 43 17.465 34.178 185.897 1.00 38.37 C ANISOU 335 CG LEU A 43 6631 4757 3189 -726 293 -455 ATOM 336 CD1 LEU A 43 18.571 34.393 184.873 1.00 37.91 C ANISOU 336 CD1 LEU A 43 6518 4707 3179 -810 272 -408 ATOM 337 CD2 LEU A 43 16.396 33.255 185.342 1.00 35.54 C ANISOU 337 CD2 LEU A 43 6202 4446 2856 -574 311 -391 ATOM 338 N LYS A 44 17.078 32.441 190.593 1.00 50.57 N ANISOU 338 N LYS A 44 8213 6563 4438 -782 183 -632 ATOM 339 CA LYS A 44 17.696 31.918 191.802 1.00 52.15 C ANISOU 339 CA LYS A 44 8355 6872 4588 -841 107 -649 ATOM 340 C LYS A 44 17.496 30.412 191.933 1.00 47.95 C ANISOU 340 C LYS A 44 7686 6465 4070 -750 69 -569 ATOM 341 O LYS A 44 18.298 29.725 192.567 1.00 47.45 O ANISOU 341 O LYS A 44 7544 6511 3974 -792 -9 -548 ATOM 342 CB LYS A 44 17.138 32.631 193.030 1.00 0.00 C ATOM 343 CG LYS A 44 16.834 34.112 192.786 1.00 0.00 C ATOM 344 CD LYS A 44 16.320 34.868 194.018 1.00 0.00 C ATOM 345 CE LYS A 44 16.010 36.353 193.792 1.00 0.00 C ATOM 346 NZ LYS A 44 15.520 37.031 195.006 1.00 0.00 N1+ ATOM 347 N ASN A 45 16.428 29.903 191.327 1.00 44.71 N ANISOU 347 N ASN A 45 7249 6032 3706 -626 123 -522 ATOM 348 CA ASN A 45 16.111 28.481 191.402 1.00 40.67 C ANISOU 348 CA ASN A 45 6624 5615 3214 -544 98 -450 ATOM 349 C ASN A 45 16.528 27.744 190.131 1.00 36.40 C ANISOU 349 C ASN A 45 6000 5108 2722 -523 76 -376 ATOM 350 O ASN A 45 16.626 28.340 189.058 1.00 35.88 O ANISOU 350 O ASN A 45 5967 4982 2682 -537 103 -373 ATOM 351 CB ASN A 45 14.606 28.281 191.659 1.00 0.00 C ATOM 352 CG ASN A 45 14.204 27.029 192.438 1.00 0.00 C ATOM 353 OD1 ASN A 45 14.943 26.526 193.276 1.00 0.00 O ATOM 354 ND2 ASN A 45 12.993 26.532 192.197 1.00 0.00 N ATOM 355 N MET A 46 16.777 26.445 190.266 1.00 33.96 N ANISOU 355 N MET A 46 5594 4890 2420 -486 33 -317 ATOM 356 CA MET A 46 17.120 25.594 189.130 1.00 32.12 C ANISOU 356 CA MET A 46 5285 4689 2231 -453 19 -248 ATOM 357 C MET A 46 16.032 25.627 188.067 1.00 32.57 C ANISOU 357 C MET A 46 5354 4679 2341 -377 81 -229 ATOM 358 O MET A 46 16.315 25.673 186.869 1.00 33.00 O ANISOU 358 O MET A 46 5395 4717 2425 -377 88 -201 ATOM 359 CB MET A 46 17.345 24.143 189.594 1.00 0.00 C ATOM 360 CG MET A 46 17.763 23.103 188.540 1.00 0.00 C ATOM 361 SD MET A 46 18.058 21.399 189.078 1.00 0.00 S ATOM 362 CE MET A 46 16.347 20.902 189.400 1.00 0.00 C ATOM 363 N THR A 47 14.772 25.523 188.507 1.00 33.35 N ANISOU 363 N THR A 47 5474 4752 2444 -315 125 -241 ATOM 364 CA THR A 47 13.629 25.530 187.608 1.00 33.25 C ANISOU 364 CA THR A 47 5461 4700 2475 -243 176 -217 ATOM 365 C THR A 47 13.511 26.865 186.839 1.00 35.38 C ANISOU 365 C THR A 47 5814 4881 2748 -251 220 -243 ATOM 366 O THR A 47 12.978 26.872 185.729 1.00 36.47 O ANISOU 366 O THR A 47 5939 4990 2927 -197 247 -208 ATOM 367 CB THR A 47 12.315 25.276 188.389 1.00 34.86 C ANISOU 367 CB THR A 47 5659 4915 2671 -184 216 -220 ATOM 368 OG1 THR A 47 12.527 24.296 189.401 1.00 37.26 O ANISOU 368 OG1 THR A 47 5916 5228 3014 -126 236 -173 ATOM 369 CG2 THR A 47 11.149 24.797 187.514 1.00 36.41 C ANISOU 369 CG2 THR A 47 5949 5048 2838 -174 275 -278 ATOM 370 N SER A 48 14.082 27.952 187.407 1.00 36.25 N ANISOU 370 N SER A 48 6006 4945 2823 -319 223 -300 ATOM 371 CA SER A 48 14.057 29.250 186.741 1.00 36.84 C ANISOU 371 CA SER A 48 6145 4916 2938 -324 264 -319 ATOM 372 C SER A 48 14.983 29.240 185.530 1.00 34.68 C ANISOU 372 C SER A 48 5817 4644 2715 -360 235 -274 ATOM 373 O SER A 48 14.730 29.916 184.534 1.00 34.39 O ANISOU 373 O SER A 48 5804 4538 2726 -331 270 -250 ATOM 374 CB SER A 48 14.465 30.373 187.713 1.00 0.00 C ATOM 375 OG SER A 48 14.894 31.524 186.975 1.00 0.00 O ATOM 376 N ILE A 49 16.055 28.462 185.626 1.00 32.94 N ANISOU 376 N ILE A 49 5524 4509 2482 -416 175 -255 ATOM 377 CA ILE A 49 17.017 28.345 184.540 1.00 33.12 C ANISOU 377 CA ILE A 49 5484 4551 2548 -447 154 -211 ATOM 378 C ILE A 49 16.401 27.645 183.334 1.00 32.03 C ANISOU 378 C ILE A 49 5298 4422 2452 -360 173 -152 ATOM 379 O ILE A 49 16.534 28.110 182.201 1.00 32.35 O ANISOU 379 O ILE A 49 5338 4422 2530 -354 195 -122 ATOM 380 CB ILE A 49 18.274 27.577 184.987 1.00 34.64 C ANISOU 380 CB ILE A 49 5597 4849 2718 -509 89 -199 ATOM 381 CG1 ILE A 49 18.927 28.279 186.180 1.00 36.53 C ANISOU 381 CG1 ILE A 49 5879 5097 2904 -613 55 -259 ATOM 382 CG2 ILE A 49 19.260 27.446 183.838 1.00 34.27 C ANISOU 382 CG2 ILE A 49 5476 4829 2717 -531 81 -150 ATOM 383 CD1 ILE A 49 19.336 29.711 185.895 1.00 37.34 C ANISOU 383 CD1 ILE A 49 6052 5110 3025 -700 79 -297 ATOM 384 N TYR A 50 15.721 26.531 183.586 1.00 30.84 N ANISOU 384 N TYR A 50 5110 4322 2287 -299 165 -134 ATOM 385 CA TYR A 50 15.109 25.752 182.515 1.00 20.82 C ANISOU 385 CA TYR A 50 3798 3066 1045 -231 175 -87 ATOM 386 C TYR A 50 13.999 26.529 181.808 1.00 25.97 C ANISOU 386 C TYR A 50 4491 3655 1722 -176 219 -78 ATOM 387 O TYR A 50 13.912 26.519 180.581 1.00 26.59 O ANISOU 387 O TYR A 50 4550 3725 1826 -150 227 -39 ATOM 388 CB TYR A 50 14.553 24.439 183.060 1.00 20.39 C ANISOU 388 CB TYR A 50 3709 3068 968 -193 160 -75 ATOM 389 CG TYR A 50 15.598 23.455 183.540 1.00 20.85 C ANISOU 389 CG TYR A 50 3721 3192 1009 -221 117 -61 ATOM 390 CD1 TYR A 50 16.932 23.581 183.172 1.00 20.77 C ANISOU 390 CD1 TYR A 50 3673 3206 1011 -263 94 -49 ATOM 391 CD2 TYR A 50 15.242 22.392 184.360 1.00 20.53 C ANISOU 391 CD2 TYR A 50 3647 3190 964 -191 101 -50 ATOM 392 CE1 TYR A 50 17.883 22.674 183.614 1.00 20.72 C ANISOU 392 CE1 TYR A 50 3612 3270 991 -272 56 -26 ATOM 393 CE2 TYR A 50 16.182 21.483 184.804 1.00 20.39 C ANISOU 393 CE2 TYR A 50 3592 3228 927 -201 64 -26 ATOM 394 CZ TYR A 50 17.498 21.626 184.430 1.00 20.60 C ANISOU 394 CZ TYR A 50 3594 3287 946 -239 40 -13 ATOM 395 OH TYR A 50 18.424 20.712 184.880 1.00 20.86 O ANISOU 395 OH TYR A 50 3575 3385 965 -232 3 21 ATOM 396 N LEU A 51 13.131 27.181 182.606 1.00 21.26 N ANISOU 396 N LEU A 51 3948 3017 1112 -151 251 -109 ATOM 397 CA LEU A 51 12.050 28.048 182.116 1.00 23.22 C ANISOU 397 CA LEU A 51 4231 3207 1386 -83 296 -94 ATOM 398 C LEU A 51 12.596 29.167 181.219 1.00 23.85 C ANISOU 398 C LEU A 51 4357 3210 1494 -104 315 -81 ATOM 399 O LEU A 51 11.978 29.510 180.213 1.00 22.59 O ANISOU 399 O LEU A 51 4201 3023 1361 -47 336 -37 ATOM 400 CB LEU A 51 11.286 28.672 183.308 1.00 22.07 C ANISOU 400 CB LEU A 51 4140 3027 1219 -47 339 -135 ATOM 401 CG LEU A 51 10.195 27.777 183.932 1.00 21.80 C ANISOU 401 CG LEU A 51 4063 3064 1157 -14 340 -137 ATOM 402 CD1 LEU A 51 9.764 28.308 185.316 1.00 24.79 C ANISOU 402 CD1 LEU A 51 4508 3408 1505 10 391 -188 ATOM 403 CD2 LEU A 51 8.994 27.585 182.976 1.00 21.44 C ANISOU 403 CD2 LEU A 51 3948 3060 1137 55 343 -82 ATOM 404 N LEU A 52 13.778 29.677 181.587 1.00 25.42 N ANISOU 404 N LEU A 52 4592 3380 1686 -192 305 -116 ATOM 405 CA LEU A 52 14.455 30.727 180.837 1.00 25.44 C ANISOU 405 CA LEU A 52 4641 3308 1716 -236 324 -102 ATOM 406 C LEU A 52 14.921 30.202 179.487 1.00 27.69 C ANISOU 406 C LEU A 52 4862 3639 2022 -232 308 -40 ATOM 407 O LEU A 52 14.718 30.842 178.456 1.00 31.33 O ANISOU 407 O LEU A 52 5350 4049 2505 -204 336 2 ATOM 408 CB LEU A 52 15.642 31.278 181.628 1.00 25.98 C ANISOU 408 CB LEU A 52 4745 3356 1768 -354 308 -155 ATOM 409 CG LEU A 52 16.530 32.302 180.915 1.00 26.20 C ANISOU 409 CG LEU A 52 4816 3314 1825 -431 326 -141 ATOM 410 CD1 LEU A 52 15.749 33.567 180.589 1.00 26.96 C ANISOU 410 CD1 LEU A 52 5024 3274 1946 -383 390 -138 ATOM 411 CD2 LEU A 52 17.758 32.630 181.750 1.00 26.34 C ANISOU 411 CD2 LEU A 52 4841 3344 1821 -568 293 -194 ATOM 412 N ASN A 53 15.544 29.028 179.499 1.00 25.44 N ANISOU 412 N ASN A 53 4496 3448 1724 -254 267 -34 ATOM 413 CA ASN A 53 16.021 28.408 178.270 1.00 26.59 C ANISOU 413 CA ASN A 53 4584 3640 1880 -246 260 16 ATOM 414 C ASN A 53 14.878 27.943 177.370 1.00 27.05 C ANISOU 414 C ASN A 53 4630 3711 1937 -159 267 54 ATOM 415 O ASN A 53 15.009 27.932 176.145 1.00 21.06 O ANISOU 415 O ASN A 53 3862 2958 1181 -145 276 97 ATOM 416 CB ASN A 53 16.943 27.237 178.600 1.00 25.52 C ANISOU 416 CB ASN A 53 4372 3594 1733 -277 222 12 ATOM 417 CG ASN A 53 18.320 27.689 179.050 1.00 24.85 C ANISOU 417 CG ASN A 53 4269 3523 1651 -372 208 -4 ATOM 418 OD1 ASN A 53 18.911 28.597 178.463 1.00 23.83 O ANISOU 418 OD1 ASN A 53 4160 3354 1540 -424 231 9 ATOM 419 ND2 ASN A 53 18.831 27.069 180.107 1.00 24.21 N ANISOU 419 ND2 ASN A 53 4148 3504 1549 -400 168 -27 ATOM 420 N LEU A 54 13.766 27.505 177.974 1.00 27.24 N ANISOU 420 N LEU A 54 4651 3747 1950 -107 263 40 ATOM 421 CA LEU A 54 12.542 27.128 177.267 1.00 20.61 C ANISOU 421 CA LEU A 54 3792 2932 1109 -35 263 75 ATOM 422 C LEU A 54 11.950 28.338 176.523 1.00 38.61 C ANISOU 422 C LEU A 54 6117 5149 3403 10 294 111 ATOM 423 O LEU A 54 11.538 28.208 175.374 1.00 40.67 O ANISOU 423 O LEU A 54 6362 5433 3658 48 288 160 ATOM 424 CB LEU A 54 11.556 26.480 178.271 1.00 20.41 C ANISOU 424 CB LEU A 54 3744 2940 1072 0 257 55 ATOM 425 CG LEU A 54 10.157 26.107 177.729 1.00 20.36 C ANISOU 425 CG LEU A 54 3699 2974 1062 62 251 90 ATOM 426 CD1 LEU A 54 10.213 25.243 176.458 1.00 20.00 C ANISOU 426 CD1 LEU A 54 3619 2979 1002 48 221 114 ATOM 427 CD2 LEU A 54 9.314 25.435 178.829 1.00 20.27 C ANISOU 427 CD2 LEU A 54 3659 3002 1042 80 252 70 ATOM 428 N ALA A 55 12.007 29.516 177.157 1.00 36.61 N ANISOU 428 N ALA A 55 5931 4815 3166 7 327 89 ATOM 429 CA ALA A 55 11.531 30.759 176.562 1.00 34.59 C ANISOU 429 CA ALA A 55 5737 4477 2930 57 366 128 ATOM 430 C ALA A 55 12.429 31.174 175.410 1.00 37.18 C ANISOU 430 C ALA A 55 6085 4781 3263 17 371 171 ATOM 431 O ALA A 55 11.953 31.645 174.377 1.00 37.71 O ANISOU 431 O ALA A 55 6169 4829 3331 72 384 233 ATOM 432 CB ALA A 55 11.467 31.860 177.602 1.00 31.57 C ANISOU 432 CB ALA A 55 5440 3994 2560 53 410 82 ATOM 433 N ILE A 56 13.732 30.994 175.597 1.00 36.55 N ANISOU 433 N ILE A 56 5996 4710 3181 -78 362 144 ATOM 434 CA ILE A 56 14.709 31.326 174.569 1.00 22.91 C ANISOU 434 CA ILE A 56 4275 2971 1457 -128 374 184 ATOM 435 C ILE A 56 14.515 30.442 173.341 1.00 34.08 C ANISOU 435 C ILE A 56 5635 4468 2846 -88 356 232 ATOM 436 O ILE A 56 14.629 30.905 172.206 1.00 33.51 O ANISOU 436 O ILE A 56 5588 4380 2766 -78 376 289 ATOM 437 CB ILE A 56 16.149 31.184 175.101 1.00 25.35 C ANISOU 437 CB ILE A 56 4560 3301 1772 -239 364 146 ATOM 438 CG1 ILE A 56 16.439 32.281 176.126 1.00 23.71 C ANISOU 438 CG1 ILE A 56 4427 3001 1580 -302 383 98 ATOM 439 CG2 ILE A 56 17.159 31.257 173.969 1.00 25.56 C ANISOU 439 CG2 ILE A 56 4565 3348 1799 -286 381 193 ATOM 440 CD1 ILE A 56 17.867 32.294 176.621 1.00 24.02 C ANISOU 440 CD1 ILE A 56 4436 3070 1622 -426 366 66 ATOM 441 N SER A 57 14.199 29.173 173.576 1.00 21.74 N ANISOU 441 N SER A 57 4007 2987 1264 -68 320 209 ATOM 442 CA SER A 57 13.951 28.235 172.490 1.00 27.72 C ANISOU 442 CA SER A 57 4725 3818 1989 -37 301 239 ATOM 443 C SER A 57 12.821 28.723 171.592 1.00 29.69 C ANISOU 443 C SER A 57 4997 4061 2222 34 301 294 ATOM 444 O SER A 57 12.948 28.725 170.369 1.00 30.25 O ANISOU 444 O SER A 57 5076 4156 2263 41 303 340 ATOM 445 CB SER A 57 13.620 26.849 173.043 1.00 27.28 C ANISOU 445 CB SER A 57 4615 3830 1921 -29 266 201 ATOM 446 OG SER A 57 14.734 26.291 173.716 1.00 27.87 O ANISOU 446 OG SER A 57 4661 3923 2004 -82 263 165 ATOM 447 N ASP A 58 11.722 29.148 172.207 1.00 31.86 N ANISOU 447 N ASP A 58 5281 4311 2513 89 300 293 ATOM 448 CA ASP A 58 10.570 29.630 171.457 1.00 34.49 C ANISOU 448 CA ASP A 58 5619 4651 2834 170 295 355 ATOM 449 C ASP A 58 10.904 30.896 170.683 1.00 32.67 C ANISOU 449 C ASP A 58 5460 4344 2610 185 332 415 ATOM 450 O ASP A 58 10.480 31.062 169.540 1.00 33.49 O ANISOU 450 O ASP A 58 5567 4476 2682 228 321 483 ATOM 451 CB ASP A 58 9.388 29.880 172.391 1.00 39.79 C ANISOU 451 CB ASP A 58 6277 5312 3529 235 299 343 ATOM 452 CG ASP A 58 8.813 28.596 172.952 1.00 46.41 C ANISOU 452 CG ASP A 58 7042 6238 4355 227 263 304 ATOM 453 OD1 ASP A 58 9.557 27.595 173.024 1.00 48.65 O ANISOU 453 OD1 ASP A 58 7303 6557 4623 162 243 266 ATOM 454 OD2 ASP A 58 7.617 28.587 173.319 1.00 50.76 O1- ANISOU 454 OD2 ASP A 58 7554 6820 4912 286 259 315 ATOM 455 N LEU A 59 11.668 31.785 171.309 1.00 30.33 N ANISOU 455 N LEU A 59 5226 3949 2350 141 373 393 ATOM 456 CA LEU A 59 12.082 33.024 170.661 1.00 29.74 C ANISOU 456 CA LEU A 59 5232 3781 2286 137 417 449 ATOM 457 C LEU A 59 12.966 32.738 169.454 1.00 30.43 C ANISOU 457 C LEU A 59 5310 3913 2338 87 417 489 ATOM 458 O LEU A 59 12.748 33.286 168.374 1.00 31.93 O ANISOU 458 O LEU A 59 5538 4090 2505 125 430 568 ATOM 459 CB LEU A 59 12.817 33.929 171.648 1.00 24.93 C ANISOU 459 CB LEU A 59 4694 3058 1720 71 459 401 ATOM 460 CG LEU A 59 11.964 34.486 172.785 1.00 26.56 C ANISOU 460 CG LEU A 59 4942 3194 1955 128 480 363 ATOM 461 CD1 LEU A 59 12.827 35.259 173.764 1.00 27.39 C ANISOU 461 CD1 LEU A 59 5125 3195 2088 37 515 299 ATOM 462 CD2 LEU A 59 10.859 35.369 172.227 1.00 27.77 C ANISOU 462 CD2 LEU A 59 5144 3289 2118 250 509 439 ATOM 463 N LEU A 60 13.955 31.869 169.642 1.00 29.33 N ANISOU 463 N LEU A 60 5122 3831 2192 9 406 440 ATOM 464 CA LEU A 60 14.842 31.463 168.556 1.00 29.52 C ANISOU 464 CA LEU A 60 5127 3908 2180 -33 416 470 ATOM 465 C LEU A 60 14.047 30.906 167.385 1.00 31.90 C ANISOU 465 C LEU A 60 5414 4287 2421 32 389 517 ATOM 466 O LEU A 60 14.478 30.980 166.236 1.00 35.21 O ANISOU 466 O LEU A 60 5851 4730 2796 21 408 567 ATOM 467 CB LEU A 60 15.849 30.420 169.041 1.00 27.94 C ANISOU 467 CB LEU A 60 4861 3772 1984 -99 406 408 ATOM 468 CG LEU A 60 16.956 30.895 169.982 1.00 26.97 C ANISOU 468 CG LEU A 60 4737 3604 1905 -187 427 370 ATOM 469 CD1 LEU A 60 17.785 29.713 170.453 1.00 25.60 C ANISOU 469 CD1 LEU A 60 4481 3514 1731 -224 406 322 ATOM 470 CD2 LEU A 60 17.831 31.927 169.292 1.00 27.32 C ANISOU 470 CD2 LEU A 60 4826 3595 1958 -249 478 420 ATOM 471 N PHE A 61 12.880 30.353 167.688 1.00 30.60 N ANISOU 471 N PHE A 61 5214 4166 2247 92 343 501 ATOM 472 CA PHE A 61 12.017 29.774 166.671 1.00 31.40 C ANISOU 472 CA PHE A 61 5292 4352 2285 141 303 538 ATOM 473 C PHE A 61 11.186 30.843 165.972 1.00 33.21 C ANISOU 473 C PHE A 61 5564 4555 2500 215 304 629 ATOM 474 O PHE A 61 11.157 30.911 164.744 1.00 33.41 O ANISOU 474 O PHE A 61 5609 4622 2463 229 297 690 ATOM 475 CB PHE A 61 11.101 28.720 167.297 1.00 32.34 C ANISOU 475 CB PHE A 61 5348 4538 2403 160 252 488 ATOM 476 CG PHE A 61 10.295 27.939 166.297 1.00 33.46 C ANISOU 476 CG PHE A 61 5460 4779 2475 181 202 509 ATOM 477 CD1 PHE A 61 9.050 28.385 165.887 1.00 34.44 C ANISOU 477 CD1 PHE A 61 5568 4939 2579 250 167 570 ATOM 478 CD2 PHE A 61 10.779 26.748 165.777 1.00 33.91 C ANISOU 478 CD2 PHE A 61 5472 4895 2519 124 183 460 ATOM 479 CE1 PHE A 61 8.306 27.665 164.969 1.00 35.01 C ANISOU 479 CE1 PHE A 61 5597 5113 2590 249 107 584 ATOM 480 CE2 PHE A 61 10.038 26.022 164.861 1.00 33.71 C ANISOU 480 CE2 PHE A 61 5407 4954 2446 119 132 464 ATOM 481 CZ PHE A 61 8.799 26.482 164.457 1.00 34.06 C ANISOU 481 CZ PHE A 61 5446 5042 2454 171 89 524 ATOM 482 N LEU A 62 10.517 31.685 166.753 1.00 34.42 N ANISOU 482 N LEU A 62 5735 4637 2705 270 317 640 ATOM 483 CA LEU A 62 9.519 32.587 166.190 1.00 37.65 C ANISOU 483 CA LEU A 62 6171 5030 3105 368 313 732 ATOM 484 C LEU A 62 10.117 33.822 165.512 1.00 38.10 C ANISOU 484 C LEU A 62 6323 4988 3164 371 367 809 ATOM 485 O LEU A 62 9.426 34.502 164.755 1.00 39.29 O ANISOU 485 O LEU A 62 6502 5135 3291 454 363 904 ATOM 486 CB LEU A 62 8.517 33.006 167.273 1.00 41.29 C ANISOU 486 CB LEU A 62 6615 5451 3622 443 318 718 ATOM 487 CG LEU A 62 8.992 33.734 168.531 1.00 44.66 C ANISOU 487 CG LEU A 62 7101 5750 4119 420 376 662 ATOM 488 CD1 LEU A 62 8.960 35.243 168.337 1.00 47.82 C ANISOU 488 CD1 LEU A 62 7605 6015 4550 476 435 730 ATOM 489 CD2 LEU A 62 8.149 33.325 169.730 1.00 43.44 C ANISOU 489 CD2 LEU A 62 6892 5620 3995 458 366 603 ATOM 490 N PHE A 63 11.393 34.111 165.755 1.00 36.87 N ANISOU 490 N PHE A 63 6214 4760 3036 279 416 775 ATOM 491 CA PHE A 63 12.042 35.213 165.045 1.00 36.97 C ANISOU 491 CA PHE A 63 6318 4682 3047 260 472 851 ATOM 492 C PHE A 63 12.276 34.843 163.584 1.00 37.37 C ANISOU 492 C PHE A 63 6363 4822 3012 254 459 917 ATOM 493 O PHE A 63 12.593 35.699 162.757 1.00 39.20 O ANISOU 493 O PHE A 63 6670 5002 3224 256 499 1003 ATOM 494 CB PHE A 63 13.388 35.613 165.677 1.00 0.00 C ATOM 495 CG PHE A 63 14.300 36.441 164.799 1.00 0.00 C ATOM 496 CD1 PHE A 63 14.215 37.844 164.826 1.00 0.00 C ATOM 497 CD2 PHE A 63 15.231 35.810 163.956 1.00 0.00 C ATOM 498 CE1 PHE A 63 15.065 38.616 164.016 1.00 0.00 C ATOM 499 CE2 PHE A 63 16.082 36.582 163.144 1.00 0.00 C ATOM 500 CZ PHE A 63 15.998 37.986 163.175 1.00 0.00 C ATOM 501 N THR A 64 12.121 33.561 163.272 1.00 36.26 N ANISOU 501 N THR A 64 6147 4813 2818 243 407 874 ATOM 502 CA THR A 64 12.295 33.076 161.911 1.00 34.69 C ANISOU 502 CA THR A 64 5928 4710 2542 229 388 911 ATOM 503 C THR A 64 10.989 33.182 161.122 1.00 33.98 C ANISOU 503 C THR A 64 5812 4688 2410 316 325 981 ATOM 504 O THR A 64 10.998 33.179 159.891 1.00 34.95 O ANISOU 504 O THR A 64 5926 4872 2482 309 306 1030 ATOM 505 CB THR A 64 12.787 31.614 161.891 1.00 33.42 C ANISOU 505 CB THR A 64 5680 4649 2369 163 360 814 ATOM 506 OG1 THR A 64 11.742 30.745 162.344 1.00 31.94 O ANISOU 506 OG1 THR A 64 5429 4528 2179 197 293 766 ATOM 507 CG2 THR A 64 14.005 31.447 162.789 1.00 32.52 C ANISOU 507 CG2 THR A 64 5574 4484 2297 89 412 750 ATOM 508 N LEU A 65 9.873 33.283 161.841 1.00 32.48 N ANISOU 508 N LEU A 65 5607 4497 2237 397 293 987 ATOM 509 CA LEU A 65 8.546 33.376 161.227 1.00 33.93 C ANISOU 509 CA LEU A 65 5747 4760 2384 487 227 1059 ATOM 510 C LEU A 65 8.380 34.483 160.170 1.00 36.60 C ANISOU 510 C LEU A 65 6139 5066 2700 543 238 1182 ATOM 511 O LEU A 65 7.784 34.229 159.122 1.00 36.03 O ANISOU 511 O LEU A 65 6020 5099 2569 557 173 1227 ATOM 512 CB LEU A 65 7.475 33.557 162.310 1.00 28.94 C ANISOU 512 CB LEU A 65 5086 4114 1795 578 214 1057 ATOM 513 CG LEU A 65 7.171 32.364 163.219 1.00 27.82 C ANISOU 513 CG LEU A 65 4854 4039 1676 534 176 947 ATOM 514 CD1 LEU A 65 6.058 32.712 164.193 1.00 28.01 C ANISOU 514 CD1 LEU A 65 4828 4048 1765 621 171 951 ATOM 515 CD2 LEU A 65 6.803 31.136 162.402 1.00 27.67 C ANISOU 515 CD2 LEU A 65 4764 4168 1579 487 99 923 ATOM 516 N PRO A 66 8.885 35.712 160.432 1.00 39.14 N ANISOU 516 N PRO A 66 6565 5239 3065 569 318 1239 ATOM 517 CA PRO A 66 8.707 36.745 159.402 1.00 32.51 C ANISOU 517 CA PRO A 66 5779 4365 2209 623 329 1362 ATOM 518 C PRO A 66 9.329 36.377 158.057 1.00 41.28 C ANISOU 518 C PRO A 66 6873 5560 3253 542 310 1376 ATOM 519 O PRO A 66 8.842 36.816 157.015 1.00 43.59 O ANISOU 519 O PRO A 66 7169 5892 3500 587 278 1470 ATOM 520 CB PRO A 66 9.415 37.962 160.002 1.00 32.96 C ANISOU 520 CB PRO A 66 5965 4228 2330 622 430 1392 ATOM 521 CG PRO A 66 9.354 37.749 161.459 1.00 31.99 C ANISOU 521 CG PRO A 66 5840 4048 2268 619 451 1300 ATOM 522 CD PRO A 66 9.502 36.273 161.649 1.00 38.83 C ANISOU 522 CD PRO A 66 6601 5054 3101 546 394 1193 ATOM 523 N PHE A 67 10.387 35.575 158.083 1.00 38.77 N ANISOU 523 N PHE A 67 6534 5271 2925 429 332 1286 ATOM 524 CA PHE A 67 11.046 35.156 156.854 1.00 37.35 C ANISOU 524 CA PHE A 67 6340 5173 2680 355 328 1291 ATOM 525 C PHE A 67 10.242 34.085 156.126 1.00 38.15 C ANISOU 525 C PHE A 67 6361 5430 2704 351 233 1262 ATOM 526 O PHE A 67 10.137 34.112 154.901 1.00 39.92 O ANISOU 526 O PHE A 67 6591 5722 2854 338 205 1315 ATOM 527 CB PHE A 67 12.469 34.644 157.146 1.00 0.00 C ATOM 528 CG PHE A 67 13.449 35.687 157.634 1.00 0.00 C ATOM 529 CD1 PHE A 67 13.706 35.817 159.011 1.00 0.00 C ATOM 530 CD2 PHE A 67 14.104 36.526 156.716 1.00 0.00 C ATOM 531 CE1 PHE A 67 14.621 36.782 159.468 1.00 0.00 C ATOM 532 CE2 PHE A 67 15.019 37.491 157.173 1.00 0.00 C ATOM 533 CZ PHE A 67 15.277 37.619 158.549 1.00 0.00 C ATOM 534 N TRP A 68 9.674 33.145 156.875 1.00 37.59 N ANISOU 534 N TRP A 68 6224 5411 2648 350 184 1178 ATOM 535 CA TRP A 68 8.883 32.084 156.261 1.00 38.13 C ANISOU 535 CA TRP A 68 6228 5614 2647 327 94 1142 ATOM 536 C TRP A 68 7.860 32.492 155.217 1.00 40.70 C ANISOU 536 C TRP A 68 6542 5988 2932 412 23 1243 ATOM 537 O TRP A 68 7.674 31.649 154.398 1.00 42.23 O ANISOU 537 O TRP A 68 6722 6282 3042 385 -45 1257 ATOM 538 CB TRP A 68 8.565 30.972 157.267 1.00 35.25 C ANISOU 538 CB TRP A 68 5799 5282 2313 301 64 1034 ATOM 539 CG TRP A 68 9.759 30.452 158.024 1.00 32.95 C ANISOU 539 CG TRP A 68 5509 4938 2074 238 130 941 ATOM 540 CD1 TRP A 68 9.882 30.343 159.379 1.00 32.26 C ANISOU 540 CD1 TRP A 68 5411 4788 2057 247 155 885 ATOM 541 CD2 TRP A 68 10.995 29.975 157.470 1.00 31.02 C ANISOU 541 CD2 TRP A 68 5272 4704 1809 163 180 897 ATOM 542 NE1 TRP A 68 11.112 29.825 159.703 1.00 30.74 N ANISOU 542 NE1 TRP A 68 5218 4569 1893 180 209 813 ATOM 543 CE2 TRP A 68 11.815 29.593 158.550 1.00 30.05 C ANISOU 543 CE2 TRP A 68 5137 4527 1755 135 228 821 ATOM 544 CE3 TRP A 68 11.486 29.832 156.168 1.00 29.64 C ANISOU 544 CE3 TRP A 68 5112 4587 1563 124 190 918 ATOM 545 CZ2 TRP A 68 13.097 29.081 158.368 1.00 29.66 C ANISOU 545 CZ2 TRP A 68 5082 4480 1709 79 285 771 ATOM 546 CZ3 TRP A 68 12.758 29.324 155.991 1.00 31.17 C ANISOU 546 CZ3 TRP A 68 5302 4783 1759 72 256 864 ATOM 547 CH2 TRP A 68 13.550 28.954 157.085 1.00 30.42 C ANISOU 547 CH2 TRP A 68 5187 4634 1739 54 302 794 ATOM 548 N ILE A 69 7.248 33.685 155.083 1.00 74.05 N ATOM 549 CA ILE A 69 5.756 33.732 154.911 1.00 62.87 C ATOM 550 C ILE A 69 4.923 34.942 154.458 1.00 59.18 C ATOM 551 O ILE A 69 4.849 35.236 153.277 1.00 59.42 O ATOM 552 CB ILE A 69 5.158 33.170 156.182 1.00 0.00 C ATOM 553 CG1 ILE A 69 3.534 33.153 156.669 1.00 0.00 C ATOM 554 CG2 ILE A 69 5.970 34.077 157.298 1.00 0.00 C ATOM 555 CD1 ILE A 69 2.211 31.704 157.572 1.00 0.00 C ATOM 556 N ASP A 70 4.549 35.746 155.478 1.00 61.02 N ATOM 557 CA ASP A 70 4.855 37.150 155.806 1.00 50.85 C ATOM 558 C ASP A 70 6.245 37.562 155.374 1.00 46.91 C ATOM 559 O ASP A 70 6.475 38.757 155.167 1.00 43.18 O ATOM 560 CB ASP A 70 4.562 37.560 157.272 1.00 0.00 C ATOM 561 CG ASP A 70 4.410 39.080 157.424 1.00 0.00 C ATOM 562 OD1 ASP A 70 3.512 39.624 156.734 1.00 0.00 O ATOM 563 OD2 ASP A 70 5.163 39.663 158.232 1.00 0.00 O1- ATOM 564 N TYR A 71 6.999 36.529 154.859 1.00 43.19 N ANISOU 564 N TYR A 71 6993 6155 3264 603 78 1542 ATOM 565 CA TYR A 71 7.520 36.566 153.479 1.00 44.58 C ANISOU 565 CA TYR A 71 7236 6309 3394 605 99 1646 ATOM 566 C TYR A 71 7.759 35.709 152.241 1.00 43.58 C ANISOU 566 C TYR A 71 7094 6310 3155 509 49 1616 ATOM 567 O TYR A 71 7.436 36.114 151.126 1.00 45.06 O ANISOU 567 O TYR A 71 7308 6543 3269 527 13 1705 ATOM 568 CB TYR A 71 8.763 37.424 153.779 1.00 0.00 C ATOM 569 CG TYR A 71 9.434 38.109 152.604 1.00 0.00 C ATOM 570 CD1 TYR A 71 10.471 37.460 151.910 1.00 0.00 C ATOM 571 CD2 TYR A 71 9.038 39.402 152.217 1.00 0.00 C ATOM 572 CE1 TYR A 71 11.098 38.093 150.823 1.00 0.00 C ATOM 573 CE2 TYR A 71 9.663 40.035 151.129 1.00 0.00 C ATOM 574 CZ TYR A 71 10.692 39.379 150.429 1.00 0.00 C ATOM 575 OH TYR A 71 11.299 39.990 149.371 1.00 0.00 O ATOM 576 N LYS A 72 8.326 34.524 152.445 1.00 36.19 N ANISOU 576 N LYS A 72 6123 5425 2204 410 52 1491 ATOM 577 CA LYS A 72 8.610 33.610 151.345 1.00 41.14 C ANISOU 577 CA LYS A 72 6747 6158 2724 315 18 1444 ATOM 578 C LYS A 72 7.330 33.029 150.763 1.00 43.04 C ANISOU 578 C LYS A 72 6956 6513 2885 329 -102 1447 ATOM 579 O LYS A 72 7.246 32.764 149.564 1.00 45.45 O ANISOU 579 O LYS A 72 7297 6890 3081 284 -143 1463 ATOM 580 CB LYS A 72 9.535 32.471 151.813 1.00 0.00 C ATOM 581 CG LYS A 72 9.992 31.554 150.674 1.00 0.00 C ATOM 582 CD LYS A 72 11.027 30.499 151.084 1.00 0.00 C ATOM 583 CE LYS A 72 10.481 29.340 151.929 1.00 0.00 C ATOM 584 NZ LYS A 72 9.621 28.422 151.161 1.00 0.00 N1+ ATOM 585 N LEU A 73 6.335 32.827 151.619 1.00 41.58 N ANISOU 585 N LEU A 73 6706 6343 2749 389 -156 1430 ATOM 586 CA LEU A 73 5.052 32.299 151.179 1.00 41.71 C ANISOU 586 CA LEU A 73 6676 6473 2701 409 -272 1434 ATOM 587 C LEU A 73 4.318 33.324 150.320 1.00 44.13 C ANISOU 587 C LEU A 73 6993 6810 2963 501 -319 1579 ATOM 588 O LEU A 73 3.590 32.966 149.394 1.00 44.55 O ANISOU 588 O LEU A 73 7039 6968 2920 492 -410 1597 ATOM 589 CB LEU A 73 4.194 31.893 152.391 1.00 0.00 C ATOM 590 CG LEU A 73 4.686 30.409 152.489 1.00 0.00 C ATOM 591 CD1 LEU A 73 4.294 29.264 151.518 1.00 0.00 C ATOM 592 CD2 LEU A 73 5.795 29.993 153.485 1.00 0.00 C ATOM 593 N LYS A 74 4.517 34.601 150.633 1.00 45.02 N ANISOU 593 N LYS A 74 7134 6825 3146 592 -254 1681 ATOM 594 CA LYS A 74 3.900 35.682 149.874 1.00 47.86 C ANISOU 594 CA LYS A 74 7514 7193 3478 693 -284 1830 ATOM 595 C LYS A 74 4.649 35.929 148.568 1.00 49.81 C ANISOU 595 C LYS A 74 7854 7443 3629 626 -265 1874 ATOM 596 O LYS A 74 4.045 36.246 147.543 1.00 51.63 O ANISOU 596 O LYS A 74 8098 7742 3775 661 -332 1962 ATOM 597 CB LYS A 74 3.852 36.969 150.718 1.00 0.00 C ATOM 598 CG LYS A 74 3.905 38.248 149.877 1.00 0.00 C ATOM 599 CD LYS A 74 3.910 39.546 150.694 1.00 0.00 C ATOM 600 CE LYS A 74 3.962 40.839 149.869 1.00 0.00 C ATOM 601 NZ LYS A 74 3.966 42.055 150.701 1.00 0.00 N1+ ATOM 602 N ASP A 75 5.969 35.780 148.614 1.00 50.25 N ANISOU 602 N ASP A 75 7966 7432 3695 531 -173 1815 ATOM 603 CA ASP A 75 6.809 35.995 147.442 1.00 52.44 C ANISOU 603 CA ASP A 75 8324 7716 3885 461 -136 1852 ATOM 604 C ASP A 75 7.668 34.772 147.138 1.00 52.58 C ANISOU 604 C ASP A 75 8349 7789 3842 323 -114 1721 ATOM 605 O ASP A 75 7.162 33.733 146.709 1.00 52.52 O ANISOU 605 O ASP A 75 8329 7875 3750 273 -192 1646 ATOM 606 CB ASP A 75 7.706 37.230 147.648 1.00 0.00 C ATOM 607 CG ASP A 75 8.239 37.895 146.377 1.00 0.00 C ATOM 608 OD1 ASP A 75 7.539 38.801 145.869 1.00 0.00 O ATOM 609 OD2 ASP A 75 9.313 37.456 145.916 1.00 0.00 O1- ATOM 610 N ASP A 76 8.972 34.910 147.360 1.00 52.45 N ANISOU 610 N ASP A 76 8353 7708 3868 268 -3 1693 ATOM 611 CA ASP A 76 9.919 33.812 147.205 1.00 52.53 C ANISOU 611 CA ASP A 76 8350 7768 3842 157 40 1573 ATOM 612 C ASP A 76 11.160 34.109 148.035 1.00 50.03 C ANISOU 612 C ASP A 76 8021 7358 3631 143 159 1545 ATOM 613 O ASP A 76 11.360 35.243 148.469 1.00 50.01 O ANISOU 613 O ASP A 76 8051 7247 3704 197 210 1627 ATOM 614 CB ASP A 76 10.296 33.604 145.727 1.00 0.00 C ATOM 615 CG ASP A 76 10.888 34.818 145.005 1.00 0.00 C ATOM 616 OD1 ASP A 76 11.882 35.368 145.533 1.00 0.00 O ATOM 617 OD2 ASP A 76 10.310 35.195 143.965 1.00 0.00 O1- ATOM 618 N TRP A 77 11.993 33.097 148.256 1.00 47.54 N ANISOU 618 N TRP A 77 7665 7078 3319 74 204 1430 ATOM 619 CA TRP A 77 13.188 33.277 149.074 1.00 44.24 C ANISOU 619 CA TRP A 77 7233 6577 2998 61 309 1396 ATOM 620 C TRP A 77 14.216 34.153 148.366 1.00 44.27 C ANISOU 620 C TRP A 77 7290 6545 2983 38 401 1480 ATOM 621 O TRP A 77 14.677 33.827 147.274 1.00 45.34 O ANISOU 621 O TRP A 77 7438 6766 3024 -8 422 1484 ATOM 622 CB TRP A 77 13.811 31.930 149.437 1.00 41.34 C ANISOU 622 CB TRP A 77 6805 6264 2639 11 333 1257 ATOM 623 CG TRP A 77 14.912 32.069 150.435 1.00 38.01 C ANISOU 623 CG TRP A 77 6367 5754 2321 3 424 1219 ATOM 624 CD1 TRP A 77 16.250 32.116 150.179 1.00 36.42 C ANISOU 624 CD1 TRP A 77 6170 5544 2123 -38 523 1214 ATOM 625 CD2 TRP A 77 14.769 32.206 151.854 1.00 36.05 C ANISOU 625 CD2 TRP A 77 6101 5416 2181 29 423 1184 ATOM 626 NE1 TRP A 77 16.951 32.263 151.351 1.00 36.16 N ANISOU 626 NE1 TRP A 77 6122 5425 2195 -46 577 1179 ATOM 627 CE2 TRP A 77 16.065 32.321 152.394 1.00 35.60 C ANISOU 627 CE2 TRP A 77 6041 5300 2186 -7 517 1157 ATOM 628 CE3 TRP A 77 13.672 32.237 152.719 1.00 34.95 C ANISOU 628 CE3 TRP A 77 5947 5247 2087 78 353 1173 ATOM 629 CZ2 TRP A 77 16.293 32.465 153.762 1.00 33.82 C ANISOU 629 CZ2 TRP A 77 5806 4984 2058 -5 538 1118 ATOM 630 CZ3 TRP A 77 13.900 32.380 154.077 1.00 33.92 C ANISOU 630 CZ3 TRP A 77 5807 5025 2056 90 381 1133 ATOM 631 CH2 TRP A 77 15.201 32.491 154.584 1.00 31.74 C ANISOU 631 CH2 TRP A 77 5538 4690 1833 44 470 1104 ATOM 632 N VAL A 78 14.577 35.264 149.002 1.00 43.92 N ANISOU 632 N VAL A 78 7284 6374 3029 63 460 1546 ATOM 633 CA VAL A 78 15.455 36.251 148.383 1.00 45.17 C ANISOU 633 CA VAL A 78 7503 6481 3180 35 547 1643 ATOM 634 C VAL A 78 16.645 36.608 149.269 1.00 44.16 C ANISOU 634 C VAL A 78 7376 6250 3152 -8 651 1619 ATOM 635 O VAL A 78 17.415 37.515 148.952 1.00 44.64 O ANISOU 635 O VAL A 78 7488 6247 3227 -43 731 1699 ATOM 636 CB VAL A 78 14.685 37.545 148.053 1.00 46.06 C ANISOU 636 CB VAL A 78 7689 6518 3292 100 521 1783 ATOM 637 CG1 VAL A 78 13.604 37.275 147.017 1.00 46.68 C ANISOU 637 CG1 VAL A 78 7772 6709 3257 133 419 1824 ATOM 638 CG2 VAL A 78 14.080 38.136 149.319 1.00 44.77 C ANISOU 638 CG2 VAL A 78 7538 6230 3243 170 509 1788 ATOM 639 N PHE A 79 16.799 35.888 150.374 1.00 42.93 N ANISOU 639 N PHE A 79 7167 6081 3064 -15 648 1510 ATOM 640 CA PHE A 79 17.786 36.251 151.384 1.00 43.72 C ANISOU 640 CA PHE A 79 7272 6078 3260 -60 730 1485 ATOM 641 C PHE A 79 19.134 35.559 151.180 1.00 43.68 C ANISOU 641 C PHE A 79 7216 6138 3243 -134 807 1428 ATOM 642 O PHE A 79 20.106 35.868 151.867 1.00 43.01 O ANISOU 642 O PHE A 79 7128 5987 3228 -190 882 1417 ATOM 643 CB PHE A 79 17.236 35.940 152.775 1.00 42.71 C ANISOU 643 CB PHE A 79 7121 5895 3211 -28 688 1408 ATOM 644 CG PHE A 79 15.912 36.590 153.053 1.00 44.20 C ANISOU 644 CG PHE A 79 7352 6025 3418 58 621 1463 ATOM 645 CD1 PHE A 79 15.850 37.884 153.544 1.00 45.19 C ANISOU 645 CD1 PHE A 79 7561 6000 3610 79 663 1539 ATOM 646 CD2 PHE A 79 14.727 35.914 152.808 1.00 44.41 C ANISOU 646 CD2 PHE A 79 7336 6144 3394 116 522 1441 ATOM 647 CE1 PHE A 79 14.632 38.489 153.793 1.00 45.81 C ANISOU 647 CE1 PHE A 79 7676 6023 3707 179 612 1594 ATOM 648 CE2 PHE A 79 13.506 36.513 153.056 1.00 44.97 C ANISOU 648 CE2 PHE A 79 7431 6173 3481 205 464 1500 ATOM 649 CZ PHE A 79 13.458 37.802 153.549 1.00 45.73 C ANISOU 649 CZ PHE A 79 7608 6121 3647 248 512 1579 ATOM 650 N GLY A 80 19.191 34.631 150.232 1.00 43.94 N ANISOU 650 N GLY A 80 7210 6301 3185 -135 792 1392 ATOM 651 CA GLY A 80 20.438 33.966 149.906 1.00 43.49 C ANISOU 651 CA GLY A 80 7107 6312 3107 -186 872 1345 ATOM 652 C GLY A 80 20.559 32.581 150.506 1.00 42.25 C ANISOU 652 C GLY A 80 6878 6210 2964 -176 851 1213 ATOM 653 O GLY A 80 19.703 32.150 151.278 1.00 40.84 O ANISOU 653 O GLY A 80 6684 6013 2821 -140 775 1156 ATOM 654 N ASP A 81 21.632 31.884 150.148 1.00 43.10 N ANISOU 654 N ASP A 81 6944 6385 3046 -204 924 1169 ATOM 655 CA ASP A 81 21.864 30.526 150.625 1.00 41.19 C ANISOU 655 CA ASP A 81 6643 6192 2817 -189 917 1049 ATOM 656 C ASP A 81 22.359 30.502 152.068 1.00 40.64 C ANISOU 656 C ASP A 81 6534 6053 2854 -204 938 1009 ATOM 657 O ASP A 81 21.927 29.671 152.868 1.00 38.67 O ANISOU 657 O ASP A 81 6255 5798 2639 -177 884 925 ATOM 658 CB ASP A 81 22.871 29.808 149.708 1.00 0.00 C ATOM 659 CG ASP A 81 22.292 29.167 148.444 1.00 0.00 C ATOM 660 OD1 ASP A 81 22.243 29.877 147.413 1.00 0.00 O ATOM 661 OD2 ASP A 81 21.872 27.995 148.545 1.00 0.00 O1- ATOM 662 N ALA A 82 23.264 31.418 152.396 1.00 42.13 N ANISOU 662 N ALA A 82 6725 6189 3093 -257 1015 1072 ATOM 663 CA ALA A 82 23.810 31.496 153.745 1.00 33.40 C ANISOU 663 CA ALA A 82 5587 5023 2081 -292 1038 1041 ATOM 664 C ALA A 82 22.711 31.821 154.745 1.00 38.64 C ANISOU 664 C ALA A 82 6288 5598 2797 -267 951 1023 ATOM 665 O ALA A 82 22.656 31.252 155.833 1.00 39.65 O ANISOU 665 O ALA A 82 6384 5710 2974 -262 922 951 ATOM 666 CB ALA A 82 24.918 32.533 153.812 1.00 35.38 C ANISOU 666 CB ALA A 82 5839 5232 2370 -377 1136 1119 ATOM 667 N MET A 83 21.830 32.737 154.362 1.00 38.90 N ANISOU 667 N MET A 83 6389 5576 2815 -246 912 1094 ATOM 668 CA MET A 83 20.710 33.125 155.208 1.00 38.33 C ANISOU 668 CA MET A 83 6356 5422 2785 -209 837 1088 ATOM 669 C MET A 83 19.719 31.973 155.356 1.00 36.14 C ANISOU 669 C MET A 83 6038 5210 2484 -146 746 1006 ATOM 670 O MET A 83 19.063 31.834 156.389 1.00 35.36 O ANISOU 670 O MET A 83 5935 5068 2432 -123 694 963 ATOM 671 CB MET A 83 20.013 34.357 154.631 1.00 39.01 C ANISOU 671 CB MET A 83 6525 5443 2856 -186 825 1195 ATOM 672 CG MET A 83 19.434 35.294 155.673 1.00 39.56 C ANISOU 672 CG MET A 83 6658 5376 2996 -173 808 1219 ATOM 673 SD MET A 83 20.706 35.980 156.746 1.00 55.02 S ANISOU 673 SD MET A 83 8641 7225 5039 -287 899 1210 ATOM 674 CE MET A 83 19.758 37.209 157.641 1.00 52.79 C ANISOU 674 CE MET A 83 8471 6770 4816 -255 878 1249 ATOM 675 N CYS A 84 19.620 31.148 154.319 1.00 34.97 N ANISOU 675 N CYS A 84 5863 5165 2260 -129 730 983 ATOM 676 CA CYS A 84 18.739 29.986 154.340 1.00 35.22 C ANISOU 676 CA CYS A 84 5859 5259 2264 -91 650 903 ATOM 677 C CYS A 84 19.208 28.944 155.349 1.00 34.97 C ANISOU 677 C CYS A 84 5773 5229 2286 -96 657 802 ATOM 678 O CYS A 84 18.407 28.408 156.115 1.00 34.13 O ANISOU 678 O CYS A 84 5647 5112 2208 -72 591 746 ATOM 679 CB CYS A 84 18.646 29.357 152.950 1.00 36.91 C ANISOU 679 CB CYS A 84 6073 5576 2377 -88 643 897 ATOM 680 SG CYS A 84 17.811 27.755 152.916 1.00 40.09 S ANISOU 680 SG CYS A 84 6437 6054 2742 -67 565 782 ATOM 681 N LYS A 85 20.507 28.660 155.344 1.00 35.21 N ANISOU 681 N LYS A 85 5776 5277 2325 -127 740 785 ATOM 682 CA LYS A 85 21.077 27.680 156.260 1.00 33.75 C ANISOU 682 CA LYS A 85 5540 5099 2185 -128 755 702 ATOM 683 C LYS A 85 21.097 28.223 157.686 1.00 33.14 C ANISOU 683 C LYS A 85 5462 4941 2189 -148 744 701 ATOM 684 O LYS A 85 21.074 27.458 158.649 1.00 34.50 O ANISOU 684 O LYS A 85 5600 5110 2400 -138 718 633 ATOM 685 CB LYS A 85 22.489 27.285 155.818 1.00 29.75 C ANISOU 685 CB LYS A 85 4999 4644 1659 -149 855 697 ATOM 686 CG LYS A 85 22.553 26.732 154.398 1.00 35.17 C ANISOU 686 CG LYS A 85 5698 5408 2258 -133 877 690 ATOM 687 CD LYS A 85 23.975 26.378 153.984 1.00 31.42 C ANISOU 687 CD LYS A 85 5187 4987 1765 -149 988 688 ATOM 688 CE LYS A 85 24.256 24.894 154.159 1.00 35.04 C ANISOU 688 CE LYS A 85 5618 5478 2219 -111 1001 588 ATOM 689 NZ LYS A 85 23.406 24.055 153.270 1.00 34.97 N1+ ANISOU 689 NZ LYS A 85 5652 5497 2138 -81 950 532 ATOM 690 N ILE A 86 21.128 29.545 157.815 1.00 33.58 N ANISOU 690 N ILE A 86 5565 4929 2266 -180 765 776 ATOM 691 CA ILE A 86 21.147 30.183 159.128 1.00 33.95 C ANISOU 691 CA ILE A 86 5631 4888 2380 -215 760 774 ATOM 692 C ILE A 86 19.804 30.059 159.845 1.00 34.36 C ANISOU 692 C ILE A 86 5699 4903 2452 -164 671 740 ATOM 693 O ILE A 86 19.741 29.621 160.994 1.00 30.95 O ANISOU 693 O ILE A 86 5244 4454 2060 -168 645 680 ATOM 694 CB ILE A 86 21.535 31.668 158.999 1.00 0.00 C ATOM 695 CG1 ILE A 86 22.270 32.165 160.261 1.00 0.00 C ATOM 696 CG2 ILE A 86 20.304 32.537 158.688 1.00 0.00 C ATOM 697 CD1 ILE A 86 22.731 33.631 160.302 1.00 0.00 C ATOM 698 N LEU A 87 18.731 30.448 159.164 1.00 35.76 N ANISOU 698 N LEU A 87 5911 5079 2597 -116 625 784 ATOM 699 CA LEU A 87 17.407 30.431 159.773 1.00 36.48 C ANISOU 699 CA LEU A 87 6011 5146 2705 -64 548 767 ATOM 700 C LEU A 87 16.846 29.019 159.883 1.00 37.06 C ANISOU 700 C LEU A 87 6019 5297 2765 -38 486 684 ATOM 701 O LEU A 87 15.945 28.766 160.681 1.00 37.58 O ANISOU 701 O LEU A 87 6072 5350 2857 -11 431 651 ATOM 702 CB LEU A 87 16.444 31.339 158.985 1.00 0.00 C ATOM 703 CG LEU A 87 16.715 32.853 158.812 1.00 0.00 C ATOM 704 CD1 LEU A 87 16.146 33.397 157.504 1.00 0.00 C ATOM 705 CD2 LEU A 87 16.166 33.641 160.002 1.00 0.00 C ATOM 706 N SER A 88 17.380 28.099 159.089 1.00 36.90 N ANISOU 706 N SER A 88 5964 5351 2705 -49 503 650 ATOM 707 CA SER A 88 17.050 26.691 159.255 1.00 36.27 C ANISOU 707 CA SER A 88 5836 5324 2620 -37 462 565 ATOM 708 C SER A 88 17.646 26.208 160.573 1.00 35.86 C ANISOU 708 C SER A 88 5755 5239 2633 -50 478 507 ATOM 709 O SER A 88 17.033 25.422 161.297 1.00 36.64 O ANISOU 709 O SER A 88 5827 5339 2756 -36 429 450 ATOM 710 CB SER A 88 17.570 25.838 158.083 1.00 0.00 C ATOM 711 OG SER A 88 16.598 24.843 157.736 1.00 0.00 O ATOM 712 N GLY A 89 18.839 26.706 160.885 1.00 34.74 N ANISOU 712 N GLY A 89 5618 5070 2514 -84 547 528 ATOM 713 CA GLY A 89 19.501 26.394 162.138 1.00 33.09 C ANISOU 713 CA GLY A 89 5381 4838 2353 -106 562 487 ATOM 714 C GLY A 89 18.712 26.862 163.346 1.00 33.41 C ANISOU 714 C GLY A 89 5439 4817 2436 -106 513 476 ATOM 715 O GLY A 89 18.500 26.099 164.285 1.00 33.02 O ANISOU 715 O GLY A 89 5360 4771 2415 -96 479 419 ATOM 716 N PHE A 90 18.274 28.118 163.322 1.00 34.54 N ANISOU 716 N PHE A 90 5641 4901 2582 -112 514 533 ATOM 717 CA PHE A 90 17.465 28.663 164.407 1.00 24.17 C ANISOU 717 CA PHE A 90 4360 3522 1300 -100 479 525 ATOM 718 C PHE A 90 16.148 27.905 164.532 1.00 24.75 C ANISOU 718 C PHE A 90 4400 3632 1372 -42 407 491 ATOM 719 O PHE A 90 15.665 27.656 165.637 1.00 23.07 O ANISOU 719 O PHE A 90 4175 3401 1189 -33 377 450 ATOM 720 CB PHE A 90 17.188 30.161 164.181 1.00 0.00 C ATOM 721 CG PHE A 90 18.392 31.070 164.290 1.00 0.00 C ATOM 722 CD1 PHE A 90 19.577 30.595 164.881 1.00 0.00 C ATOM 723 CD2 PHE A 90 18.329 32.387 163.803 1.00 0.00 C ATOM 724 CE1 PHE A 90 20.700 31.435 164.978 1.00 0.00 C ATOM 725 CE2 PHE A 90 19.452 33.227 163.901 1.00 0.00 C ATOM 726 CZ PHE A 90 20.638 32.751 164.489 1.00 0.00 C ATOM 727 N TYR A 91 15.580 27.540 163.387 1.00 23.99 N ANISOU 727 N TYR A 91 4288 3593 1234 -13 380 510 ATOM 728 CA TYR A 91 14.323 26.800 163.329 1.00 32.87 C ANISOU 728 CA TYR A 91 5378 4766 2344 20 312 484 ATOM 729 C TYR A 91 14.427 25.458 164.048 1.00 30.42 C ANISOU 729 C TYR A 91 5016 4482 2061 5 293 401 ATOM 730 O TYR A 91 13.569 25.108 164.860 1.00 28.60 O ANISOU 730 O TYR A 91 4766 4251 1851 18 251 373 ATOM 731 CB TYR A 91 13.915 26.589 161.870 1.00 35.43 C ANISOU 731 CB TYR A 91 5700 5159 2604 28 290 514 ATOM 732 CG TYR A 91 12.571 25.931 161.653 1.00 24.45 C ANISOU 732 CG TYR A 91 4279 3831 1181 44 216 499 ATOM 733 CD1 TYR A 91 11.409 26.686 161.598 1.00 24.87 C ANISOU 733 CD1 TYR A 91 4345 3888 1216 85 173 559 ATOM 734 CD2 TYR A 91 12.468 24.558 161.466 1.00 28.54 C ANISOU 734 CD2 TYR A 91 4759 4403 1681 20 192 429 ATOM 735 CE1 TYR A 91 10.179 26.091 161.380 1.00 25.05 C ANISOU 735 CE1 TYR A 91 4334 3984 1202 89 102 552 ATOM 736 CE2 TYR A 91 11.242 23.954 161.249 1.00 27.32 C ANISOU 736 CE2 TYR A 91 4580 4311 1489 19 125 415 ATOM 737 CZ TYR A 91 10.101 24.726 161.207 1.00 24.82 C ANISOU 737 CZ TYR A 91 4267 4013 1150 44 76 478 ATOM 738 OH TYR A 91 8.878 24.132 160.992 1.00 25.65 O ANISOU 738 OH TYR A 91 4343 4194 1209 30 4 472 ATOM 739 N TYR A 92 15.484 24.712 163.748 1.00 29.68 N ANISOU 739 N TYR A 92 4905 4410 1963 -16 329 368 ATOM 740 CA TYR A 92 15.671 23.392 164.335 1.00 28.62 C ANISOU 740 CA TYR A 92 4734 4289 1849 -20 319 299 ATOM 741 C TYR A 92 16.159 23.470 165.783 1.00 28.31 C ANISOU 741 C TYR A 92 4684 4209 1862 -30 329 279 ATOM 742 O TYR A 92 15.646 22.763 166.649 1.00 29.60 O ANISOU 742 O TYR A 92 4826 4369 2052 -25 296 239 ATOM 743 CB TYR A 92 16.652 22.564 163.485 1.00 0.00 C ATOM 744 CG TYR A 92 16.268 22.300 162.041 1.00 0.00 C ATOM 745 CD1 TYR A 92 17.269 22.145 161.065 1.00 0.00 C ATOM 746 CD2 TYR A 92 14.914 22.230 161.670 1.00 0.00 C ATOM 747 CE1 TYR A 92 16.917 21.904 159.725 1.00 0.00 C ATOM 748 CE2 TYR A 92 14.561 21.987 160.331 1.00 0.00 C ATOM 749 CZ TYR A 92 15.563 21.821 159.358 1.00 0.00 C ATOM 750 OH TYR A 92 15.224 21.583 158.058 1.00 0.00 O ATOM 751 N THR A 93 17.144 24.325 166.042 1.00 27.85 N ANISOU 751 N THR A 93 4645 4125 1813 -55 375 307 ATOM 752 CA THR A 93 17.695 24.469 167.388 1.00 26.71 C ANISOU 752 CA THR A 93 4495 3952 1701 -81 382 288 ATOM 753 C THR A 93 16.620 24.943 168.359 1.00 26.28 C ANISOU 753 C THR A 93 4457 3858 1670 -72 339 279 ATOM 754 O THR A 93 16.488 24.408 169.460 1.00 26.84 O ANISOU 754 O THR A 93 4506 3927 1765 -73 315 240 ATOM 755 CB THR A 93 18.885 25.446 167.416 1.00 0.00 C ATOM 756 OG1 THR A 93 19.915 24.952 166.553 1.00 0.00 O ATOM 757 CG2 THR A 93 19.472 25.651 168.818 1.00 0.00 C ATOM 758 N GLY A 94 15.845 25.936 167.939 1.00 26.38 N ANISOU 758 N GLY A 94 4513 3840 1671 -54 334 321 ATOM 759 CA GLY A 94 14.740 26.431 168.739 1.00 26.21 C ANISOU 759 CA GLY A 94 4504 3784 1673 -27 304 318 ATOM 760 C GLY A 94 13.715 25.351 169.035 1.00 26.36 C ANISOU 760 C GLY A 94 4480 3847 1687 1 256 283 ATOM 761 O GLY A 94 13.151 25.303 170.127 1.00 26.56 O ANISOU 761 O GLY A 94 4501 3858 1732 9 240 259 ATOM 762 N LEU A 95 13.481 24.476 168.062 1.00 27.06 N ANISOU 762 N LEU A 95 4535 3990 1755 6 236 279 ATOM 763 CA LEU A 95 12.511 23.400 168.220 1.00 28.08 C ANISOU 763 CA LEU A 95 4625 4161 1883 11 192 246 ATOM 764 C LEU A 95 12.983 22.337 169.205 1.00 30.12 C ANISOU 764 C LEU A 95 4856 4415 2175 -7 193 192 ATOM 765 O LEU A 95 12.323 22.077 170.210 1.00 31.55 O ANISOU 765 O LEU A 95 5022 4591 2374 -5 173 173 ATOM 766 CB LEU A 95 12.204 22.743 166.862 1.00 0.00 C ATOM 767 CG LEU A 95 12.927 21.453 166.402 1.00 0.00 C ATOM 768 CD1 LEU A 95 12.772 20.314 167.407 1.00 0.00 C ATOM 769 CD2 LEU A 95 12.434 21.019 165.022 1.00 0.00 C ATOM 770 N TYR A 96 14.120 21.715 168.903 1.00 30.71 N ANISOU 770 N TYR A 96 4926 4492 2251 -19 221 175 ATOM 771 CA TYR A 96 14.651 20.645 169.740 1.00 30.21 C ANISOU 771 CA TYR A 96 4845 4423 2210 -24 225 136 ATOM 772 C TYR A 96 14.970 21.141 171.144 1.00 29.59 C ANISOU 772 C TYR A 96 4763 4320 2159 -33 226 134 ATOM 773 O TYR A 96 14.748 20.432 172.122 1.00 29.34 O ANISOU 773 O TYR A 96 4716 4287 2146 -33 209 110 ATOM 774 CB TYR A 96 15.907 20.027 169.098 1.00 0.00 C ATOM 775 CG TYR A 96 15.722 19.279 167.792 1.00 0.00 C ATOM 776 CD1 TYR A 96 15.994 19.922 166.570 1.00 0.00 C ATOM 777 CD2 TYR A 96 15.261 17.951 167.794 1.00 0.00 C ATOM 778 CE1 TYR A 96 15.821 19.234 165.356 1.00 0.00 C ATOM 779 CE2 TYR A 96 15.089 17.261 166.581 1.00 0.00 C ATOM 780 CZ TYR A 96 15.372 17.902 165.361 1.00 0.00 C ATOM 781 OH TYR A 96 15.208 17.235 164.182 1.00 0.00 O ATOM 782 N SER A 97 15.484 22.363 171.236 1.00 29.53 N ANISOU 782 N SER A 97 4780 4293 2149 -47 247 159 ATOM 783 CA SER A 97 15.736 22.983 172.523 1.00 29.67 C ANISOU 783 CA SER A 97 4809 4285 2180 -70 245 149 ATOM 784 C SER A 97 14.451 23.114 173.316 1.00 30.37 C ANISOU 784 C SER A 97 4900 4359 2280 -52 218 136 ATOM 785 O SER A 97 14.434 22.911 174.530 1.00 29.54 O ANISOU 785 O SER A 97 4787 4250 2186 -61 207 112 ATOM 786 CB SER A 97 16.351 24.379 172.308 1.00 0.00 C ATOM 787 OG SER A 97 15.402 25.235 171.660 1.00 0.00 O ATOM 788 N GLU A 98 13.369 23.445 172.619 1.00 31.02 N ANISOU 788 N GLU A 98 4992 4443 2351 -23 209 158 ATOM 789 CA GLU A 98 12.064 23.568 173.239 1.00 31.02 C ANISOU 789 CA GLU A 98 4991 4444 2351 2 192 155 ATOM 790 C GLU A 98 11.628 22.295 173.935 1.00 31.28 C ANISOU 790 C GLU A 98 4980 4508 2398 -7 169 124 ATOM 791 O GLU A 98 11.370 22.298 175.134 1.00 32.39 O ANISOU 791 O GLU A 98 5119 4640 2547 -8 170 106 ATOM 792 CB GLU A 98 11.023 23.949 172.170 1.00 0.00 C ATOM 793 CG GLU A 98 9.573 24.124 172.648 1.00 0.00 C ATOM 794 CD GLU A 98 8.551 24.501 171.580 1.00 0.00 C ATOM 795 OE1 GLU A 98 8.755 24.105 170.411 1.00 0.00 O ATOM 796 OE2 GLU A 98 7.574 25.181 171.958 1.00 0.00 O1- ATOM 797 N ILE A 99 11.559 21.200 173.185 1.00 31.63 N ANISOU 797 N ILE A 99 4999 4583 2436 -15 154 117 ATOM 798 CA ILE A 99 11.089 19.931 173.732 1.00 31.69 C ANISOU 798 CA ILE A 99 4985 4607 2450 -29 137 93 ATOM 799 C ILE A 99 12.068 19.372 174.770 1.00 30.68 C ANISOU 799 C ILE A 99 4854 4459 2345 -37 148 74 ATOM 800 O ILE A 99 11.651 18.770 175.761 1.00 31.50 O ANISOU 800 O ILE A 99 4949 4564 2455 -44 141 64 ATOM 801 CB ILE A 99 10.842 18.886 172.603 1.00 20.75 C ANISOU 801 CB ILE A 99 3598 3242 1042 -41 123 84 ATOM 802 CG1 ILE A 99 10.423 17.532 173.186 1.00 20.87 C ANISOU 802 CG1 ILE A 99 3615 3254 1060 -64 114 58 ATOM 803 CG2 ILE A 99 12.066 18.732 171.716 1.00 19.47 C ANISOU 803 CG2 ILE A 99 3451 3069 877 -37 146 80 ATOM 804 CD1 ILE A 99 9.196 17.592 174.076 1.00 20.13 C ANISOU 804 CD1 ILE A 99 3505 3182 961 -75 99 65 ATOM 805 N PHE A 100 13.363 19.593 174.565 1.00 29.20 N ANISOU 805 N PHE A 100 4674 4262 2160 -37 166 77 ATOM 806 CA PHE A 100 14.364 19.098 175.504 1.00 28.77 C ANISOU 806 CA PHE A 100 4615 4204 2110 -41 171 71 ATOM 807 C PHE A 100 14.200 19.723 176.888 1.00 31.01 C ANISOU 807 C PHE A 100 4899 4485 2399 -53 161 64 ATOM 808 O PHE A 100 14.231 19.020 177.899 1.00 34.94 O ANISOU 808 O PHE A 100 5388 4990 2898 -54 150 58 ATOM 809 CB PHE A 100 15.779 19.357 174.983 1.00 26.65 C ANISOU 809 CB PHE A 100 4353 3944 1828 -43 195 83 ATOM 810 CG PHE A 100 16.195 18.442 173.866 1.00 25.88 C ANISOU 810 CG PHE A 100 4262 3852 1718 -22 217 83 ATOM 811 CD1 PHE A 100 15.416 17.351 173.516 1.00 24.62 C ANISOU 811 CD1 PHE A 100 4114 3681 1559 -15 209 65 ATOM 812 CD2 PHE A 100 17.371 18.672 173.166 1.00 25.10 C ANISOU 812 CD2 PHE A 100 4169 3770 1600 -17 254 98 ATOM 813 CE1 PHE A 100 15.798 16.510 172.487 1.00 24.26 C ANISOU 813 CE1 PHE A 100 4093 3630 1494 1 235 54 ATOM 814 CE2 PHE A 100 17.760 17.834 172.135 1.00 23.42 C ANISOU 814 CE2 PHE A 100 3969 3560 1369 10 286 93 ATOM 815 CZ PHE A 100 16.972 16.752 171.796 1.00 23.63 C ANISOU 815 CZ PHE A 100 4018 3566 1397 19 276 67 ATOM 816 N PHE A 101 14.017 21.039 176.936 1.00 26.21 N ANISOU 816 N PHE A 101 4311 3860 1787 -61 168 65 ATOM 817 CA PHE A 101 13.885 21.721 178.219 1.00 23.87 C ANISOU 817 CA PHE A 101 4031 3552 1485 -76 166 48 ATOM 818 C PHE A 101 12.523 21.481 178.859 1.00 22.71 C ANISOU 818 C PHE A 101 3878 3410 1342 -56 164 40 ATOM 819 O PHE A 101 12.360 21.679 180.062 1.00 23.03 O ANISOU 819 O PHE A 101 3926 3449 1373 -63 165 23 ATOM 820 CB PHE A 101 14.147 23.219 178.062 1.00 23.97 C ANISOU 820 CB PHE A 101 4085 3527 1495 -93 184 47 ATOM 821 CG PHE A 101 15.606 23.565 177.987 1.00 25.12 C ANISOU 821 CG PHE A 101 4218 3676 1650 -137 184 48 ATOM 822 CD1 PHE A 101 16.402 23.499 179.119 1.00 24.80 C ANISOU 822 CD1 PHE A 101 4161 3658 1604 -175 164 29 ATOM 823 CD2 PHE A 101 16.186 23.938 176.788 1.00 24.92 C ANISOU 823 CD2 PHE A 101 4189 3644 1634 -144 203 73 ATOM 824 CE1 PHE A 101 17.747 23.804 179.056 1.00 24.22 C ANISOU 824 CE1 PHE A 101 4057 3605 1539 -223 158 35 ATOM 825 CE2 PHE A 101 17.529 24.246 176.718 1.00 20.12 C ANISOU 825 CE2 PHE A 101 3555 3052 1037 -191 207 80 ATOM 826 CZ PHE A 101 18.311 24.178 177.853 1.00 24.66 C ANISOU 826 CZ PHE A 101 4103 3655 1613 -232 183 61 ATOM 827 N ILE A 102 11.549 21.049 178.064 1.00 21.41 N ANISOU 827 N ILE A 102 3698 3258 1178 -37 161 54 ATOM 828 CA ILE A 102 10.264 20.632 178.617 1.00 20.19 C ANISOU 828 CA ILE A 102 3530 3126 1016 -29 162 54 ATOM 829 C ILE A 102 10.436 19.300 179.347 1.00 21.85 C ANISOU 829 C ILE A 102 3721 3349 1233 -47 151 48 ATOM 830 O ILE A 102 9.868 19.087 180.419 1.00 23.02 O ANISOU 830 O ILE A 102 3865 3508 1371 -51 159 44 ATOM 831 CB ILE A 102 9.180 20.495 177.528 1.00 19.30 C ANISOU 831 CB ILE A 102 3407 3039 886 -17 154 74 ATOM 832 CG1 ILE A 102 8.870 21.854 176.905 1.00 20.22 C ANISOU 832 CG1 ILE A 102 3547 3142 994 20 166 95 ATOM 833 CG2 ILE A 102 7.904 19.919 178.112 1.00 20.36 C ANISOU 833 CG2 ILE A 102 3525 3211 1001 -21 155 78 ATOM 834 CD1 ILE A 102 7.812 21.797 175.821 1.00 21.28 C ANISOU 834 CD1 ILE A 102 3651 3320 1116 39 147 126 ATOM 835 N ILE A 103 11.237 18.415 178.761 1.00 22.07 N ANISOU 835 N ILE A 103 3746 3370 1269 -54 142 51 ATOM 836 CA ILE A 103 11.541 17.122 179.365 1.00 21.34 C ANISOU 836 CA ILE A 103 3657 3274 1175 -62 138 53 ATOM 837 C ILE A 103 12.310 17.293 180.676 1.00 22.36 C ANISOU 837 C ILE A 103 3786 3411 1299 -61 134 55 ATOM 838 O ILE A 103 12.028 16.613 181.662 1.00 22.98 O ANISOU 838 O ILE A 103 3869 3495 1367 -65 133 62 ATOM 839 CB ILE A 103 12.353 16.233 178.399 1.00 21.85 C ANISOU 839 CB ILE A 103 3738 3322 1240 -56 140 56 ATOM 840 CG1 ILE A 103 11.519 15.897 177.161 1.00 21.56 C ANISOU 840 CG1 ILE A 103 3711 3285 1197 -68 138 48 ATOM 841 CG2 ILE A 103 12.811 14.956 179.088 1.00 21.61 C ANISOU 841 CG2 ILE A 103 3735 3276 1202 -51 144 66 ATOM 842 CD1 ILE A 103 12.240 15.029 176.152 1.00 21.92 C ANISOU 842 CD1 ILE A 103 3788 3307 1234 -62 150 39 ATOM 843 N LEU A 104 13.275 18.209 180.682 1.00 22.81 N ANISOU 843 N LEU A 104 3844 3471 1353 -62 131 49 ATOM 844 CA LEU A 104 14.066 18.492 181.878 1.00 23.11 C ANISOU 844 CA LEU A 104 3885 3527 1371 -74 117 47 ATOM 845 C LEU A 104 13.181 18.962 183.026 1.00 23.38 C ANISOU 845 C LEU A 104 3925 3565 1394 -81 122 30 ATOM 846 O LEU A 104 13.319 18.499 184.157 1.00 25.44 O ANISOU 846 O LEU A 104 4185 3846 1633 -85 111 35 ATOM 847 CB LEU A 104 15.138 19.543 181.578 1.00 23.15 C ANISOU 847 CB LEU A 104 3897 3534 1364 -96 113 39 ATOM 848 CG LEU A 104 16.372 19.061 180.814 1.00 19.28 C ANISOU 848 CG LEU A 104 3399 3062 863 -93 112 61 ATOM 849 CD1 LEU A 104 17.255 20.230 180.419 1.00 19.53 C ANISOU 849 CD1 LEU A 104 3413 3098 908 -127 114 56 ATOM 850 CD2 LEU A 104 17.151 18.063 181.650 1.00 20.48 C ANISOU 850 CD2 LEU A 104 3528 3251 1003 -78 91 85 ATOM 851 N LEU A 105 12.260 19.892 182.730 1.00 23.12 N ANISOU 851 N LEU A 105 3904 3514 1367 -76 143 14 ATOM 852 CA LEU A 105 11.271 20.400 183.684 1.00 21.66 C ANISOU 852 CA LEU A 105 3734 3333 1165 -72 164 -4 ATOM 853 C LEU A 105 10.306 19.298 184.159 1.00 22.98 C ANISOU 853 C LEU A 105 3880 3524 1327 -66 172 15 ATOM 854 O LEU A 105 9.973 19.260 185.346 1.00 24.78 O ANISOU 854 O LEU A 105 4114 3769 1531 -68 186 9 ATOM 855 CB LEU A 105 10.504 21.576 183.042 1.00 19.85 C ANISOU 855 CB LEU A 105 3532 3076 933 -52 193 -15 ATOM 856 CG LEU A 105 11.303 22.890 182.995 1.00 20.25 C ANISOU 856 CG LEU A 105 3633 3084 975 -66 200 -39 ATOM 857 CD1 LEU A 105 10.770 23.864 181.922 1.00 21.46 C ANISOU 857 CD1 LEU A 105 3820 3203 1132 -34 227 -26 ATOM 858 CD2 LEU A 105 11.358 23.555 184.382 1.00 20.39 C ANISOU 858 CD2 LEU A 105 3695 3090 961 -79 217 -79 ATOM 859 N THR A 106 9.901 18.410 183.237 1.00 22.56 N ANISOU 859 N THR A 106 3812 3471 1290 -66 167 35 ATOM 860 CA THR A 106 9.046 17.257 183.518 1.00 24.01 C ANISOU 860 CA THR A 106 3989 3670 1464 -78 176 54 ATOM 861 C THR A 106 9.711 16.287 184.512 1.00 24.24 C ANISOU 861 C THR A 106 4029 3699 1481 -86 168 70 ATOM 862 O THR A 106 9.050 15.867 185.465 1.00 24.66 O ANISOU 862 O THR A 106 4087 3770 1512 -95 185 81 ATOM 863 CB THR A 106 8.644 16.481 182.232 1.00 25.57 C ANISOU 863 CB THR A 106 4186 3858 1672 -92 167 65 ATOM 864 OG1 THR A 106 8.013 17.360 181.322 1.00 28.75 O ANISOU 864 OG1 THR A 106 4577 4276 2071 -83 170 61 ATOM 865 CG2 THR A 106 7.664 15.314 182.442 1.00 23.41 C ANISOU 865 CG2 THR A 106 3923 3589 1382 -126 177 82 ATOM 866 N ILE A 107 11.016 16.011 184.332 1.00 23.96 N ANISOU 866 N ILE A 107 4000 3651 1452 -80 144 78 ATOM 867 CA ILE A 107 11.751 15.155 185.254 1.00 19.65 C ANISOU 867 CA ILE A 107 3469 3112 884 -76 132 105 ATOM 868 C ILE A 107 11.925 15.833 186.604 1.00 28.49 C ANISOU 868 C ILE A 107 4584 4267 1974 -79 125 96 ATOM 869 O ILE A 107 11.715 15.219 187.651 1.00 29.64 O ANISOU 869 O ILE A 107 4742 4430 2090 -81 129 119 ATOM 870 CB ILE A 107 13.140 14.785 184.696 1.00 23.83 C ANISOU 870 CB ILE A 107 4005 3634 1414 -58 112 120 ATOM 871 CG1 ILE A 107 12.998 13.985 183.402 1.00 23.12 C ANISOU 871 CG1 ILE A 107 3937 3504 1345 -52 126 123 ATOM 872 CG2 ILE A 107 13.948 14.007 185.723 1.00 20.09 C ANISOU 872 CG2 ILE A 107 3548 3180 904 -44 95 160 ATOM 873 CD1 ILE A 107 14.318 13.553 182.811 1.00 22.56 C ANISOU 873 CD1 ILE A 107 3882 3423 1266 -20 123 140 ATOM 874 N ASP A 108 12.300 17.108 186.567 1.00 28.51 N ANISOU 874 N ASP A 108 4581 4276 1976 -83 118 62 ATOM 875 CA ASP A 108 12.598 17.866 187.775 1.00 30.09 C ANISOU 875 CA ASP A 108 4792 4503 2139 -94 108 40 ATOM 876 C ASP A 108 11.411 17.933 188.724 1.00 27.39 C ANISOU 876 C ASP A 108 4460 4172 1774 -93 143 31 ATOM 877 O ASP A 108 11.550 17.694 189.921 1.00 26.39 O ANISOU 877 O ASP A 108 4345 4076 1606 -96 136 38 ATOM 878 CB ASP A 108 13.047 19.282 187.417 1.00 34.74 C ANISOU 878 CB ASP A 108 5395 5075 2731 -112 105 -3 ATOM 879 CG ASP A 108 13.323 20.130 188.640 1.00 39.94 C ANISOU 879 CG ASP A 108 6082 5750 3343 -137 96 -39 ATOM 880 OD1 ASP A 108 13.886 19.593 189.619 1.00 44.06 O ANISOU 880 OD1 ASP A 108 6601 6314 3825 -144 66 -23 ATOM 881 OD2 ASP A 108 12.974 21.329 188.625 1.00 38.69 O1- ANISOU 881 OD2 ASP A 108 5960 5560 3182 -149 121 -83 ATOM 882 N ARG A 109 10.251 18.302 188.170 1.00 28.61 N ANISOU 882 N ARG A 109 4612 4310 1947 -85 181 20 ATOM 883 CA ARG A 109 9.014 18.433 188.929 1.00 29.86 C ANISOU 883 CA ARG A 109 4778 4490 2078 -79 226 14 ATOM 884 C ARG A 109 8.465 17.071 189.364 1.00 27.87 C ANISOU 884 C ARG A 109 4518 4257 1816 -88 237 60 ATOM 885 O ARG A 109 7.816 16.998 190.408 1.00 29.50 O ANISOU 885 O ARG A 109 4731 4492 1986 -90 272 66 ATOM 886 CB ARG A 109 8.013 19.281 188.122 1.00 32.82 C ANISOU 886 CB ARG A 109 5153 4853 2464 -61 266 -5 ATOM 887 CG ARG A 109 8.495 20.744 188.044 1.00 36.87 C ANISOU 887 CG ARG A 109 5707 5344 2960 -49 288 -54 ATOM 888 CD ARG A 109 8.212 21.493 189.359 1.00 42.76 C ANISOU 888 CD ARG A 109 6477 6113 3656 -56 305 -77 ATOM 889 NE ARG A 109 9.154 22.591 189.621 1.00 47.84 N ANISOU 889 NE ARG A 109 7176 6724 4277 -64 307 -134 ATOM 890 CZ ARG A 109 8.908 23.651 190.408 1.00 52.25 C ANISOU 890 CZ ARG A 109 7750 7285 4819 -101 255 -150 ATOM 891 NH1 ARG A 109 7.697 23.849 190.939 1.00 50.49 N ANISOU 891 NH1 ARG A 109 7488 7097 4599 -115 203 -109 ATOM 892 NH2 ARG A 109 9.883 24.523 190.675 1.00 57.01 N1+ ANISOU 892 NH2 ARG A 109 8414 7854 5394 -124 259 -207 ATOM 893 N TYR A 110 8.799 16.015 188.611 1.00 26.37 N ANISOU 893 N TYR A 110 4323 4045 1653 -97 215 91 ATOM 894 CA TYR A 110 8.445 14.652 188.981 1.00 25.25 C ANISOU 894 CA TYR A 110 4196 3901 1497 -115 226 136 ATOM 895 C TYR A 110 9.242 14.223 190.204 1.00 23.57 C ANISOU 895 C TYR A 110 4002 3707 1247 -109 208 162 ATOM 896 O TYR A 110 8.670 13.789 191.203 1.00 21.98 O ANISOU 896 O TYR A 110 3814 3528 1009 -118 234 187 ATOM 897 CB TYR A 110 8.691 13.683 187.825 1.00 28.18 C ANISOU 897 CB TYR A 110 4579 4229 1898 -128 210 156 ATOM 898 CG TYR A 110 8.940 12.258 188.270 1.00 30.21 C ANISOU 898 CG TYR A 110 4880 4462 2138 -142 212 205 ATOM 899 CD1 TYR A 110 7.924 11.495 188.831 1.00 31.81 C ANISOU 899 CD1 TYR A 110 5104 4664 2317 -179 248 235 ATOM 900 CD2 TYR A 110 10.191 11.674 188.121 1.00 31.00 C ANISOU 900 CD2 TYR A 110 5004 4535 2238 -117 183 228 ATOM 901 CE1 TYR A 110 8.149 10.194 189.238 1.00 33.02 C ANISOU 901 CE1 TYR A 110 5314 4780 2452 -194 256 287 ATOM 902 CE2 TYR A 110 10.425 10.374 188.521 1.00 32.28 C ANISOU 902 CE2 TYR A 110 5223 4663 2379 -117 191 282 ATOM 903 CZ TYR A 110 9.402 9.638 189.080 1.00 34.73 C ANISOU 903 CZ TYR A 110 5566 4961 2670 -157 227 311 ATOM 904 OH TYR A 110 9.635 8.341 189.480 1.00 38.70 O ANISOU 904 OH TYR A 110 6140 5412 3151 -159 239 372 ATOM 905 N LEU A 111 10.563 14.359 190.122 1.00 21.28 N ANISOU 905 N LEU A 111 3710 3418 957 -94 163 161 ATOM 906 CA LEU A 111 11.447 13.975 191.217 1.00 21.80 C ANISOU 906 CA LEU A 111 3790 3519 976 -85 134 193 ATOM 907 C LEU A 111 11.135 14.740 192.498 1.00 33.10 C ANISOU 907 C LEU A 111 5225 4994 2358 -89 144 168 ATOM 908 O LEU A 111 11.333 14.227 193.598 1.00 22.93 O ANISOU 908 O LEU A 111 3955 3741 1018 -85 136 203 ATOM 909 CB LEU A 111 12.908 14.196 190.824 1.00 21.72 C ANISOU 909 CB LEU A 111 3768 3519 964 -72 84 195 ATOM 910 CG LEU A 111 13.444 13.275 189.728 1.00 25.71 C ANISOU 910 CG LEU A 111 4283 3985 1500 -56 78 228 ATOM 911 CD1 LEU A 111 14.899 13.589 189.416 1.00 25.02 C ANISOU 911 CD1 LEU A 111 4180 3927 1401 -39 34 234 ATOM 912 CD2 LEU A 111 13.286 11.823 190.136 1.00 26.53 C ANISOU 912 CD2 LEU A 111 4430 4063 1585 -45 91 293 ATOM 913 N ALA A 112 10.631 15.961 192.342 1.00 31.01 N ANISOU 913 N ALA A 112 4954 4726 2104 -93 165 110 ATOM 914 CA ALA A 112 10.345 16.840 193.473 1.00 29.08 C ANISOU 914 CA ALA A 112 4729 4512 1809 -96 183 71 ATOM 915 C ALA A 112 9.123 16.397 194.280 1.00 28.82 C ANISOU 915 C ALA A 112 4705 4501 1744 -94 240 91 ATOM 916 O ALA A 112 9.108 16.525 195.503 1.00 30.26 O ANISOU 916 O ALA A 112 4910 4722 1865 -94 248 88 ATOM 917 CB ALA A 112 10.160 18.265 192.987 1.00 22.57 C ANISOU 917 CB ALA A 112 3911 3662 1003 -99 199 5 ATOM 918 N ILE A 113 8.100 15.883 193.601 1.00 27.58 N ANISOU 918 N ILE A 113 4532 4326 1620 -98 280 114 ATOM 919 CA ILE A 113 6.883 15.449 194.285 1.00 28.57 C ANISOU 919 CA ILE A 113 4662 4478 1714 -104 342 139 ATOM 920 C ILE A 113 7.058 14.056 194.896 1.00 29.96 C ANISOU 920 C ILE A 113 4859 4660 1866 -120 335 209 ATOM 921 O ILE A 113 6.270 13.634 195.742 1.00 31.43 O ANISOU 921 O ILE A 113 5056 4874 2011 -131 383 238 ATOM 922 CB ILE A 113 5.661 15.448 193.333 1.00 27.58 C ANISOU 922 CB ILE A 113 4512 4345 1623 -112 389 140 ATOM 923 CG1 ILE A 113 4.354 15.484 194.133 1.00 27.51 C ANISOU 923 CG1 ILE A 113 4498 4383 1570 -114 468 151 ATOM 924 CG2 ILE A 113 5.708 14.255 192.388 1.00 27.77 C ANISOU 924 CG2 ILE A 113 4533 4331 1686 -142 367 184 ATOM 925 CD1 ILE A 113 3.103 15.430 193.280 1.00 23.96 C ANISOU 925 CD1 ILE A 113 4015 3948 1141 -130 519 163 ATOM 926 N VAL A 114 8.098 13.348 194.468 1.00 30.26 N ANISOU 926 N VAL A 114 4904 4669 1923 -120 281 239 ATOM 927 CA VAL A 114 8.434 12.055 195.053 1.00 29.60 C ANISOU 927 CA VAL A 114 4852 4582 1811 -127 273 312 ATOM 928 C VAL A 114 9.534 12.261 196.095 1.00 29.75 C ANISOU 928 C VAL A 114 4880 4650 1773 -103 226 322 ATOM 929 O VAL A 114 9.927 11.334 196.804 1.00 30.71 O ANISOU 929 O VAL A 114 5029 4787 1854 -97 213 389 ATOM 930 CB VAL A 114 8.885 11.042 193.977 1.00 30.86 C ANISOU 930 CB VAL A 114 5028 4679 2016 -134 251 348 ATOM 931 CG1 VAL A 114 8.912 9.628 194.537 1.00 34.07 C ANISOU 931 CG1 VAL A 114 5487 5062 2395 -144 264 431 ATOM 932 CG2 VAL A 114 7.952 11.098 192.787 1.00 30.36 C ANISOU 932 CG2 VAL A 114 4952 4579 2004 -161 282 320 ATOM 933 N HIS A 115 10.010 13.501 196.183 1.00 29.15 N ANISOU 933 N HIS A 115 4789 4599 1689 -92 200 257 ATOM 934 CA HIS A 115 11.045 13.896 197.137 1.00 29.41 C ANISOU 934 CA HIS A 115 4833 4683 1658 -79 150 251 ATOM 935 C HIS A 115 12.311 13.054 196.999 1.00 29.70 C ANISOU 935 C HIS A 115 4868 4731 1686 -60 88 314 ATOM 936 O HIS A 115 12.847 12.558 197.989 1.00 30.67 O ANISOU 936 O HIS A 115 5009 4900 1742 -43 60 365 ATOM 937 CB HIS A 115 10.512 13.819 198.572 1.00 29.30 C ANISOU 937 CB HIS A 115 4850 4718 1566 -78 180 265 ATOM 938 CG HIS A 115 9.372 14.751 198.840 1.00 30.76 C ANISOU 938 CG HIS A 115 5038 4906 1743 -87 244 203 ATOM 939 ND1 HIS A 115 9.554 16.083 199.145 1.00 31.95 N ANISOU 939 ND1 HIS A 115 5202 5067 1868 -89 239 123 ATOM 940 CD2 HIS A 115 8.033 14.545 198.846 1.00 26.21 C ANISOU 940 CD2 HIS A 115 4458 4325 1176 -94 320 213 ATOM 941 CE1 HIS A 115 8.379 16.657 199.326 1.00 32.05 C ANISOU 941 CE1 HIS A 115 5220 5082 1875 -88 312 86 ATOM 942 NE2 HIS A 115 7.439 15.745 199.150 1.00 26.46 N ANISOU 942 NE2 HIS A 115 4495 4372 1187 -88 361 142 ATOM 943 N ALA A 116 12.780 12.899 195.764 1.00 24.49 N ANISOU 943 N ALA A 116 4187 4031 1087 -58 70 315 ATOM 944 CA ALA A 116 14.040 12.217 195.493 1.00 30.68 C ANISOU 944 CA ALA A 116 4965 4829 1862 -34 17 372 ATOM 945 C ALA A 116 15.198 12.979 196.121 1.00 32.98 C ANISOU 945 C ALA A 116 5253 5181 2098 -18 -49 353 ATOM 946 O ALA A 116 15.446 14.133 195.775 1.00 33.16 O ANISOU 946 O ALA A 116 5265 5197 2138 -42 -63 280 ATOM 947 CB ALA A 116 14.253 12.068 193.997 1.00 31.28 C ANISOU 947 CB ALA A 116 5028 4847 2009 -34 20 363 ATOM 948 N VAL A 117 15.901 12.322 197.038 1.00 36.67 N ANISOU 948 N VAL A 117 5742 5693 2498 15 -90 420 ATOM 949 CA VAL A 117 16.965 12.955 197.815 1.00 38.83 C ANISOU 949 CA VAL A 117 6042 6005 2707 8 -166 403 ATOM 950 C VAL A 117 18.076 13.527 196.939 1.00 41.86 C ANISOU 950 C VAL A 117 6385 6396 3123 -18 -221 379 ATOM 951 O VAL A 117 18.496 14.669 197.125 1.00 42.25 O ANISOU 951 O VAL A 117 6412 6483 3159 -72 -256 312 ATOM 952 CB VAL A 117 17.588 11.963 198.816 1.00 37.84 C ANISOU 952 CB VAL A 117 5965 5900 2512 37 -214 495 ATOM 953 CG1 VAL A 117 18.630 12.662 199.673 1.00 38.01 C ANISOU 953 CG1 VAL A 117 5972 6005 2465 -2 -303 477 ATOM 954 CG2 VAL A 117 16.508 11.341 199.687 1.00 37.64 C ANISOU 954 CG2 VAL A 117 5961 5877 2462 58 -151 528 ATOM 955 N PHE A 118 18.546 12.732 195.983 1.00 44.23 N ANISOU 955 N PHE A 118 6674 6669 3463 9 -225 437 ATOM 956 CA PHE A 118 19.628 13.162 195.107 1.00 48.12 C ANISOU 956 CA PHE A 118 7094 7203 3985 -9 -268 432 ATOM 957 C PHE A 118 19.204 14.328 194.220 1.00 46.03 C ANISOU 957 C PHE A 118 6813 6903 3772 -51 -233 337 ATOM 958 O PHE A 118 20.018 15.185 193.880 1.00 47.65 O ANISOU 958 O PHE A 118 6967 7155 3982 -96 -271 304 ATOM 959 CB PHE A 118 20.121 11.995 194.246 1.00 54.83 C ANISOU 959 CB PHE A 118 7914 8047 4870 52 -260 519 ATOM 960 CG PHE A 118 19.050 11.361 193.399 1.00 59.17 C ANISOU 960 CG PHE A 118 8514 8498 5471 64 -180 516 ATOM 961 CD1 PHE A 118 18.257 10.343 193.908 1.00 62.08 C ANISOU 961 CD1 PHE A 118 8929 8825 5833 74 -143 566 ATOM 962 CD2 PHE A 118 18.848 11.769 192.090 1.00 60.06 C ANISOU 962 CD2 PHE A 118 8609 8572 5641 63 -142 465 ATOM 963 CE1 PHE A 118 17.275 9.753 193.132 1.00 61.87 C ANISOU 963 CE1 PHE A 118 8937 8707 5865 87 -72 555 ATOM 964 CE2 PHE A 118 17.868 11.183 191.309 1.00 60.66 C ANISOU 964 CE2 PHE A 118 8725 8553 5772 76 -75 453 ATOM 965 CZ PHE A 118 17.081 10.173 191.831 1.00 60.95 C ANISOU 965 CZ PHE A 118 8811 8541 5807 84 -42 495 ATOM 966 N ALA A 119 17.928 14.361 193.851 1.00 43.30 N ANISOU 966 N ALA A 119 6496 6490 3467 -40 -160 300 ATOM 967 CA ALA A 119 17.405 15.437 193.015 1.00 40.53 C ANISOU 967 CA ALA A 119 6130 6099 3170 -77 -124 221 ATOM 968 C ALA A 119 17.400 16.759 193.774 1.00 39.22 C ANISOU 968 C ALA A 119 5976 5953 2974 -131 -141 148 ATOM 969 O ALA A 119 17.682 17.813 193.204 1.00 38.39 O ANISOU 969 O ALA A 119 5861 5835 2892 -176 -145 93 ATOM 970 CB ALA A 119 16.006 15.100 192.528 1.00 39.53 C ANISOU 970 CB ALA A 119 6012 5913 3094 -65 -53 210 ATOM 971 N LEU A 120 17.076 16.693 195.063 1.00 38.80 N ANISOU 971 N LEU A 120 5951 5927 2863 -130 -145 147 ATOM 972 CA LEU A 120 17.063 17.872 195.922 1.00 37.91 C ANISOU 972 CA LEU A 120 5864 5833 2705 -182 -158 76 ATOM 973 C LEU A 120 18.477 18.400 196.131 1.00 37.81 C ANISOU 973 C LEU A 120 5829 5882 2654 -240 -241 66 ATOM 974 O LEU A 120 18.701 19.610 196.185 1.00 38.43 O ANISOU 974 O LEU A 120 5921 5957 2722 -308 -252 -7 ATOM 975 CB LEU A 120 16.405 17.546 197.267 1.00 38.21 C ANISOU 975 CB LEU A 120 5942 5897 2679 -163 -140 85 ATOM 976 CG LEU A 120 16.496 18.583 198.389 1.00 38.80 C ANISOU 976 CG LEU A 120 6057 6002 2682 -213 -158 16 ATOM 977 CD1 LEU A 120 15.125 18.839 198.989 1.00 38.81 C ANISOU 977 CD1 LEU A 120 6097 5981 2667 -195 -79 -19 ATOM 978 CD2 LEU A 120 17.468 18.121 199.467 1.00 39.58 C ANISOU 978 CD2 LEU A 120 6160 6181 2696 -222 -236 58 ATOM 979 N ARG A 121 19.431 17.482 196.241 1.00 38.06 N ANISOU 979 N ARG A 121 5823 5976 2663 -219 -300 144 ATOM 980 CA ARG A 121 20.834 17.849 196.388 1.00 39.18 C ANISOU 980 CA ARG A 121 5907 6207 2771 -276 -387 153 ATOM 981 C ARG A 121 21.401 18.336 195.058 1.00 41.16 C ANISOU 981 C ARG A 121 6105 6455 3080 -310 -386 140 ATOM 982 O ARG A 121 22.455 18.969 195.016 1.00 44.51 O ANISOU 982 O ARG A 121 6473 6954 3485 -383 -446 127 ATOM 983 CB ARG A 121 21.655 16.657 196.915 1.00 0.00 C ATOM 984 CG ARG A 121 23.156 16.844 197.228 1.00 0.00 C ATOM 985 CD ARG A 121 23.957 15.651 197.751 1.00 0.00 C ATOM 986 NE ARG A 121 25.362 15.989 197.999 1.00 0.00 N ATOM 987 CZ ARG A 121 26.342 15.912 197.080 1.00 0.00 C ATOM 988 NH1 ARG A 121 26.079 15.444 195.841 1.00 0.00 N ATOM 989 NH2 ARG A 121 27.583 16.303 197.432 1.00 0.00 N1+ ATOM 990 N ALA A 122 20.690 18.038 193.974 1.00 38.70 N ANISOU 990 N ALA A 122 5807 6063 2835 -263 -318 144 ATOM 991 CA ALA A 122 21.112 18.442 192.639 1.00 38.77 C ANISOU 991 CA ALA A 122 5775 6062 2894 -286 -304 134 ATOM 992 C ALA A 122 20.403 19.716 192.185 1.00 37.49 C ANISOU 992 C ALA A 122 5663 5818 2764 -336 -255 45 ATOM 993 O ALA A 122 20.783 20.322 191.187 1.00 38.74 O ANISOU 993 O ALA A 122 5803 5965 2953 -375 -246 28 ATOM 994 CB ALA A 122 20.860 17.317 191.644 1.00 24.41 C ANISOU 994 CB ALA A 122 3944 4209 1121 -204 -262 195 ATOM 995 N ARG A 123 19.373 20.118 192.921 1.00 35.57 N ANISOU 995 N ARG A 123 5483 5523 2509 -330 -219 -3 ATOM 996 CA ARG A 123 18.571 21.281 192.552 1.00 36.11 C ANISOU 996 CA ARG A 123 5603 5510 2606 -358 -165 -78 ATOM 997 C ARG A 123 19.336 22.584 192.793 1.00 38.82 C ANISOU 997 C ARG A 123 5969 5866 2916 -463 -199 -141 ATOM 998 O ARG A 123 19.012 23.351 193.699 1.00 39.14 O ANISOU 998 O ARG A 123 6068 5887 2916 -500 -192 -202 ATOM 999 CB ARG A 123 17.253 21.281 193.330 1.00 37.17 C ANISOU 999 CB ARG A 123 5785 5606 2731 -316 -112 -103 ATOM 1000 CG ARG A 123 16.187 22.208 192.766 1.00 38.36 C ANISOU 1000 CG ARG A 123 5979 5674 2923 -310 -41 -156 ATOM 1001 CD ARG A 123 14.874 21.472 192.543 1.00 38.87 C ANISOU 1001 CD ARG A 123 6030 5713 3023 -237 17 -126 ATOM 1002 NE ARG A 123 14.457 20.721 193.724 1.00 40.49 N ANISOU 1002 NE ARG A 123 6238 5963 3184 -212 19 -102 ATOM 1003 CZ ARG A 123 14.112 19.436 193.711 1.00 41.29 C ANISOU 1003 CZ ARG A 123 6308 6084 3296 -168 25 -38 ATOM 1004 NH1 ARG A 123 14.128 18.751 192.573 1.00 39.93 N ANISOU 1004 NH1 ARG A 123 6102 5889 3180 -146 29 2 ATOM 1005 NH2 ARG A 123 13.748 18.836 194.836 1.00 42.86 N1+ ANISOU 1005 NH2 ARG A 123 6519 6320 3445 -153 32 -15 ATOM 1006 N THR A 124 20.351 22.822 191.967 1.00 40.57 N ANISOU 1006 N THR A 124 6146 6120 3150 -517 -231 -127 ATOM 1007 CA THR A 124 21.220 23.988 192.101 1.00 43.99 C ANISOU 1007 CA THR A 124 6590 6574 3549 -640 -269 -180 ATOM 1008 C THR A 124 21.361 24.699 190.760 1.00 48.56 C ANISOU 1008 C THR A 124 7180 7099 4171 -679 -232 -194 ATOM 1009 O THR A 124 21.276 24.062 189.710 1.00 51.48 O ANISOU 1009 O THR A 124 7505 7460 4594 -613 -204 -141 ATOM 1010 CB THR A 124 22.621 23.587 192.610 1.00 44.66 C ANISOU 1010 CB THR A 124 6585 6800 3585 -697 -365 -138 ATOM 1011 OG1 THR A 124 22.496 22.607 193.648 1.00 45.28 O ANISOU 1011 OG1 THR A 124 6647 6930 3628 -630 -396 -95 ATOM 1012 CG2 THR A 124 23.380 24.798 193.141 1.00 46.24 C ANISOU 1012 CG2 THR A 124 6806 7028 3737 -842 -415 -206 ATOM 1013 N VAL A 125 21.582 26.011 190.790 1.00 48.63 N ANISOU 1013 N VAL A 125 7254 7062 4161 -784 -228 -264 ATOM 1014 CA VAL A 125 21.803 26.768 189.560 1.00 50.05 C ANISOU 1014 CA VAL A 125 7431 7169 4416 -812 -188 -267 ATOM 1015 C VAL A 125 23.081 26.323 188.845 1.00 50.15 C ANISOU 1015 C VAL A 125 7309 7271 4476 -832 -229 -202 ATOM 1016 O VAL A 125 23.204 26.479 187.632 1.00 50.87 O ANISOU 1016 O VAL A 125 7369 7318 4641 -811 -187 -174 ATOM 1017 CB VAL A 125 21.877 28.283 189.829 1.00 52.39 C ANISOU 1017 CB VAL A 125 7830 7383 4692 -927 -173 -354 ATOM 1018 CG1 VAL A 125 20.543 28.795 190.352 1.00 52.78 C ANISOU 1018 CG1 VAL A 125 8017 7328 4708 -882 -109 -416 ATOM 1019 CG2 VAL A 125 23.001 28.600 190.807 1.00 53.47 C ANISOU 1019 CG2 VAL A 125 7943 7616 4757 -1064 -259 -387 ATOM 1020 N THR A 126 24.026 25.771 189.600 1.00 50.06 N ANISOU 1020 N THR A 126 7213 7391 4418 -868 -309 -173 ATOM 1021 CA THR A 126 25.241 25.212 189.020 1.00 49.42 C ANISOU 1021 CA THR A 126 6985 7413 4380 -866 -344 -100 ATOM 1022 C THR A 126 24.895 23.997 188.167 1.00 45.92 C ANISOU 1022 C THR A 126 6494 6960 3993 -719 -300 -28 ATOM 1023 O THR A 126 25.337 23.878 187.024 1.00 45.70 O ANISOU 1023 O THR A 126 6403 6928 4033 -691 -266 10 ATOM 1024 CB THR A 126 26.258 24.806 190.105 1.00 54.18 C ANISOU 1024 CB THR A 126 7499 8173 4913 -918 -445 -73 ATOM 1025 OG1 THR A 126 26.642 25.962 190.860 1.00 59.28 O ANISOU 1025 OG1 THR A 126 8193 8833 5499 -1076 -492 -148 ATOM 1026 CG2 THR A 126 27.497 24.183 189.474 1.00 53.58 C ANISOU 1026 CG2 THR A 126 7256 8212 4890 -894 -473 13 ATOM 1027 N PHE A 127 24.093 23.100 188.732 1.00 43.39 N ANISOU 1027 N PHE A 127 6214 6634 3640 -631 -297 -13 ATOM 1028 CA PHE A 127 23.617 21.925 188.014 1.00 40.64 C ANISOU 1028 CA PHE A 127 5847 6258 3338 -504 -253 43 ATOM 1029 C PHE A 127 22.769 22.344 186.817 1.00 38.31 C ANISOU 1029 C PHE A 127 5608 5846 3101 -476 -175 19 ATOM 1030 O PHE A 127 22.746 21.668 185.789 1.00 36.57 O ANISOU 1030 O PHE A 127 5356 5607 2933 -403 -137 59 ATOM 1031 CB PHE A 127 22.817 21.018 188.951 1.00 38.83 C ANISOU 1031 CB PHE A 127 5668 6032 3056 -440 -261 58 ATOM 1032 CG PHE A 127 22.340 19.741 188.313 1.00 37.49 C ANISOU 1032 CG PHE A 127 5489 5827 2927 -324 -219 113 ATOM 1033 CD1 PHE A 127 21.109 19.682 187.676 1.00 36.61 C ANISOU 1033 CD1 PHE A 127 5448 5615 2846 -285 -154 90 ATOM 1034 CD2 PHE A 127 23.116 18.595 188.364 1.00 37.02 C ANISOU 1034 CD2 PHE A 127 5354 5836 2876 -256 -244 189 ATOM 1035 CE1 PHE A 127 20.666 18.507 187.091 1.00 34.37 C ANISOU 1035 CE1 PHE A 127 5165 5298 2596 -198 -119 132 ATOM 1036 CE2 PHE A 127 22.678 17.416 187.783 1.00 35.42 C ANISOU 1036 CE2 PHE A 127 5164 5583 2710 -156 -199 232 ATOM 1037 CZ PHE A 127 21.452 17.373 187.146 1.00 33.59 C ANISOU 1037 CZ PHE A 127 5010 5250 2505 -137 -139 198 ATOM 1038 N GLY A 128 22.075 23.468 186.961 1.00 37.28 N ANISOU 1038 N GLY A 128 5569 5638 2959 -531 -150 -47 ATOM 1039 CA GLY A 128 21.246 23.996 185.895 1.00 35.14 C ANISOU 1039 CA GLY A 128 5352 5262 2737 -503 -83 -64 ATOM 1040 C GLY A 128 22.059 24.471 184.710 1.00 36.15 C ANISOU 1040 C GLY A 128 5430 5385 2920 -534 -64 -43 ATOM 1041 O GLY A 128 21.811 24.059 183.580 1.00 38.87 O ANISOU 1041 O GLY A 128 5760 5701 3308 -470 -23 -11 ATOM 1042 N VAL A 129 23.032 25.338 184.975 1.00 35.59 N ANISOU 1042 N VAL A 129 5336 5344 2842 -641 -94 -62 ATOM 1043 CA VAL A 129 23.879 25.899 183.929 1.00 34.33 C ANISOU 1043 CA VAL A 129 5127 5186 2732 -690 -72 -40 ATOM 1044 C VAL A 129 24.594 24.807 183.139 1.00 34.28 C ANISOU 1044 C VAL A 129 5007 5257 2760 -619 -66 30 ATOM 1045 O VAL A 129 24.634 24.850 181.910 1.00 33.61 O ANISOU 1045 O VAL A 129 4911 5140 2718 -589 -14 56 ATOM 1046 CB VAL A 129 24.924 26.869 184.519 1.00 35.26 C ANISOU 1046 CB VAL A 129 5221 5345 2831 -836 -117 -69 ATOM 1047 CG1 VAL A 129 25.940 27.277 183.460 1.00 35.45 C ANISOU 1047 CG1 VAL A 129 5168 5395 2908 -891 -93 -31 ATOM 1048 CG2 VAL A 129 24.238 28.090 185.106 1.00 35.13 C ANISOU 1048 CG2 VAL A 129 5341 5222 2785 -909 -104 -147 ATOM 1049 N ILE A 130 25.139 23.824 183.847 1.00 35.15 N ANISOU 1049 N ILE A 130 5041 5467 2847 -584 -115 63 ATOM 1050 CA ILE A 130 25.878 22.743 183.205 1.00 24.58 C ANISOU 1050 CA ILE A 130 3599 4200 1541 -503 -103 131 ATOM 1051 C ILE A 130 24.985 21.914 182.285 1.00 28.29 C ANISOU 1051 C ILE A 130 4118 4596 2035 -389 -43 144 ATOM 1052 O ILE A 130 25.289 21.751 181.104 1.00 29.53 O ANISOU 1052 O ILE A 130 4246 4746 2229 -354 7 170 ATOM 1053 CB ILE A 130 26.532 21.813 184.243 1.00 0.00 C ATOM 1054 CG1 ILE A 130 25.518 21.375 185.320 1.00 0.00 C ATOM 1055 CG2 ILE A 130 27.771 22.473 184.874 1.00 0.00 C ATOM 1056 CD1 ILE A 130 26.005 20.438 186.437 1.00 0.00 C ATOM 1057 N THR A 131 23.880 21.404 182.821 1.00 26.95 N ANISOU 1057 N THR A 131 4025 4377 1839 -339 -46 126 ATOM 1058 CA THR A 131 22.987 20.549 182.044 1.00 26.03 C ANISOU 1058 CA THR A 131 3953 4197 1738 -248 1 135 ATOM 1059 C THR A 131 22.251 21.335 180.963 1.00 24.42 C ANISOU 1059 C THR A 131 3812 3912 1556 -261 50 109 ATOM 1060 O THR A 131 21.738 20.752 180.009 1.00 24.43 O ANISOU 1060 O THR A 131 3836 3876 1570 -201 89 119 ATOM 1061 CB THR A 131 21.954 19.836 182.939 1.00 28.42 C ANISOU 1061 CB THR A 131 4317 4474 2008 -207 -14 126 ATOM 1062 OG1 THR A 131 21.158 20.807 183.627 1.00 31.53 O ANISOU 1062 OG1 THR A 131 4778 4828 2372 -265 -24 76 ATOM 1063 CG2 THR A 131 22.653 18.947 183.956 1.00 28.87 C ANISOU 1063 CG2 THR A 131 4321 4609 2039 -180 -61 167 ATOM 1064 N SER A 132 22.200 22.656 181.110 1.00 23.69 N ANISOU 1064 N SER A 132 3751 3789 1460 -341 48 76 ATOM 1065 CA SER A 132 21.612 23.507 180.080 1.00 24.82 C ANISOU 1065 CA SER A 132 3951 3856 1624 -350 94 65 ATOM 1066 C SER A 132 22.557 23.657 178.895 1.00 25.19 C ANISOU 1066 C SER A 132 3944 3927 1700 -361 127 100 ATOM 1067 O SER A 132 22.119 23.688 177.746 1.00 21.63 O ANISOU 1067 O SER A 132 3524 3436 1259 -325 170 113 ATOM 1068 CB SER A 132 21.259 24.884 180.641 1.00 26.14 C ANISOU 1068 CB SER A 132 4187 3965 1782 -424 90 22 ATOM 1069 OG SER A 132 20.231 24.789 181.610 1.00 26.95 O ANISOU 1069 OG SER A 132 4347 4039 1854 -401 77 -12 ATOM 1070 N ILE A 133 23.853 23.755 179.185 1.00 25.74 N ANISOU 1070 N ILE A 133 3930 4073 1778 -414 107 118 ATOM 1071 CA ILE A 133 24.876 23.849 178.148 1.00 23.19 C ANISOU 1071 CA ILE A 133 3537 3793 1483 -426 145 157 ATOM 1072 C ILE A 133 24.908 22.566 177.322 1.00 23.32 C ANISOU 1072 C ILE A 133 3524 3832 1504 -317 181 189 ATOM 1073 O ILE A 133 24.983 22.607 176.091 1.00 22.86 O ANISOU 1073 O ILE A 133 3473 3758 1454 -295 237 207 ATOM 1074 CB ILE A 133 26.267 24.118 178.751 1.00 0.00 C ATOM 1075 CG1 ILE A 133 26.168 24.988 180.021 1.00 0.00 C ATOM 1076 CG2 ILE A 133 27.208 24.750 177.710 1.00 0.00 C ATOM 1077 CD1 ILE A 133 27.468 25.352 180.755 1.00 0.00 C ATOM 1078 N ILE A 134 24.834 21.428 178.007 1.00 23.84 N ANISOU 1078 N ILE A 134 3570 3929 1559 -250 154 195 ATOM 1079 CA ILE A 134 24.801 20.131 177.340 1.00 26.64 C ANISOU 1079 CA ILE A 134 3920 4286 1918 -145 191 217 ATOM 1080 C ILE A 134 23.527 19.986 176.512 1.00 27.56 C ANISOU 1080 C ILE A 134 4138 4315 2020 -112 223 191 ATOM 1081 O ILE A 134 23.549 19.432 175.412 1.00 28.67 O ANISOU 1081 O ILE A 134 4292 4444 2158 -60 272 200 ATOM 1082 CB ILE A 134 24.894 18.969 178.353 1.00 26.62 C ANISOU 1082 CB ILE A 134 3893 4316 1907 -83 154 234 ATOM 1083 CG1 ILE A 134 26.102 19.160 179.272 1.00 30.27 C ANISOU 1083 CG1 ILE A 134 4245 4882 2373 -119 106 265 ATOM 1084 CG2 ILE A 134 24.975 17.630 177.635 1.00 22.59 C ANISOU 1084 CG2 ILE A 134 3389 3792 1404 25 203 256 ATOM 1085 CD1 ILE A 134 27.418 19.307 178.532 1.00 30.64 C ANISOU 1085 CD1 ILE A 134 4183 5009 2451 -121 141 306 ATOM 1086 N ILE A 135 22.420 20.499 177.042 1.00 25.96 N ANISOU 1086 N ILE A 135 4004 4057 1802 -142 194 159 ATOM 1087 CA ILE A 135 21.135 20.438 176.354 1.00 23.92 C ANISOU 1087 CA ILE A 135 3826 3733 1529 -117 213 140 ATOM 1088 C ILE A 135 21.155 21.244 175.056 1.00 22.32 C ANISOU 1088 C ILE A 135 3644 3510 1327 -135 253 149 ATOM 1089 O ILE A 135 20.603 20.816 174.043 1.00 21.94 O ANISOU 1089 O ILE A 135 3636 3442 1261 -97 279 150 ATOM 1090 CB ILE A 135 19.993 20.954 177.249 1.00 0.00 C ATOM 1091 CG1 ILE A 135 19.887 20.132 178.550 1.00 0.00 C ATOM 1092 CG2 ILE A 135 18.657 20.973 176.486 1.00 0.00 C ATOM 1093 CD1 ILE A 135 19.588 18.629 178.436 1.00 0.00 C ATOM 1094 N TRP A 136 21.792 22.412 175.085 1.00 22.50 N ANISOU 1094 N TRP A 136 3646 3538 1364 -201 257 158 ATOM 1095 CA TRP A 136 21.901 23.231 173.883 1.00 21.43 C ANISOU 1095 CA TRP A 136 3534 3381 1228 -222 301 179 ATOM 1096 C TRP A 136 22.814 22.563 172.856 1.00 26.79 C ANISOU 1096 C TRP A 136 4166 4111 1903 -189 349 207 ATOM 1097 O TRP A 136 22.603 22.702 171.652 1.00 26.97 O ANISOU 1097 O TRP A 136 4225 4119 1903 -173 390 222 ATOM 1098 CB TRP A 136 22.404 24.639 174.221 1.00 21.97 C ANISOU 1098 CB TRP A 136 3602 3430 1317 -313 299 182 ATOM 1099 CG TRP A 136 21.345 25.522 174.828 1.00 25.26 C ANISOU 1099 CG TRP A 136 4096 3769 1731 -333 277 154 ATOM 1100 CD1 TRP A 136 21.333 26.040 176.092 1.00 27.00 C ANISOU 1100 CD1 TRP A 136 4329 3973 1956 -383 243 121 ATOM 1101 CD2 TRP A 136 20.140 25.978 174.199 1.00 21.48 C ANISOU 1101 CD2 TRP A 136 3695 3225 1240 -295 292 160 ATOM 1102 NE1 TRP A 136 20.199 26.792 176.286 1.00 26.43 N ANISOU 1102 NE1 TRP A 136 4342 3821 1880 -372 246 101 ATOM 1103 CE2 TRP A 136 19.449 26.770 175.138 1.00 24.94 C ANISOU 1103 CE2 TRP A 136 4187 3605 1686 -313 274 130 ATOM 1104 CE3 TRP A 136 19.577 25.795 172.932 1.00 25.47 C ANISOU 1104 CE3 TRP A 136 4229 3723 1725 -244 318 188 ATOM 1105 CZ2 TRP A 136 18.228 27.376 174.852 1.00 25.22 C ANISOU 1105 CZ2 TRP A 136 4291 3575 1716 -271 286 135 ATOM 1106 CZ3 TRP A 136 18.364 26.398 172.649 1.00 25.70 C ANISOU 1106 CZ3 TRP A 136 4323 3697 1744 -212 317 196 ATOM 1107 CH2 TRP A 136 17.704 27.178 173.604 1.00 26.00 C ANISOU 1107 CH2 TRP A 136 4402 3679 1799 -220 303 173 ATOM 1108 N ALA A 137 23.816 21.829 173.333 1.00 26.06 N ANISOU 1108 N ALA A 137 3992 4083 1827 -171 347 217 ATOM 1109 CA ALA A 137 24.705 21.084 172.445 1.00 24.94 C ANISOU 1109 CA ALA A 137 3800 3992 1683 -119 404 243 ATOM 1110 C ALA A 137 23.946 20.015 171.668 1.00 25.47 C ANISOU 1110 C ALA A 137 3938 4023 1717 -39 430 225 ATOM 1111 O ALA A 137 23.997 19.976 170.438 1.00 27.19 O ANISOU 1111 O ALA A 137 4185 4240 1907 -20 484 231 ATOM 1112 CB ALA A 137 25.853 20.430 173.236 1.00 0.00 C ATOM 1113 N LEU A 138 23.245 19.149 172.395 1.00 21.82 N ANISOU 1113 N LEU A 138 3507 3533 1251 -1 393 200 ATOM 1114 CA LEU A 138 22.462 18.081 171.785 1.00 21.58 C ANISOU 1114 CA LEU A 138 3549 3460 1189 56 410 175 ATOM 1115 C LEU A 138 21.424 18.644 170.817 1.00 22.05 C ANISOU 1115 C LEU A 138 3684 3483 1209 30 412 161 ATOM 1116 O LEU A 138 21.132 18.041 169.784 1.00 21.46 O ANISOU 1116 O LEU A 138 3662 3396 1094 60 444 146 ATOM 1117 CB LEU A 138 21.752 17.228 172.853 1.00 0.00 C ATOM 1118 CG LEU A 138 22.548 16.371 173.868 1.00 0.00 C ATOM 1119 CD1 LEU A 138 21.641 15.710 174.903 1.00 0.00 C ATOM 1120 CD2 LEU A 138 23.390 15.319 173.146 1.00 0.00 C ATOM 1121 N ALA A 139 20.877 19.807 171.153 1.00 22.26 N ANISOU 1121 N ALA A 139 3721 3494 1245 -23 378 166 ATOM 1122 CA ALA A 139 19.926 20.482 170.281 1.00 20.88 C ANISOU 1122 CA ALA A 139 3606 3291 1037 -38 377 168 ATOM 1123 C ALA A 139 20.599 20.906 168.982 1.00 21.46 C ANISOU 1123 C ALA A 139 3684 3387 1084 -42 433 196 ATOM 1124 O ALA A 139 19.997 20.838 167.911 1.00 22.32 O ANISOU 1124 O ALA A 139 3848 3490 1141 -29 444 197 ATOM 1125 CB ALA A 139 19.317 21.684 170.983 1.00 20.64 C ANISOU 1125 CB ALA A 139 3585 3230 1029 -80 341 174 ATOM 1126 N ILE A 140 21.852 21.340 169.083 1.00 27.36 N ANISOU 1126 N ILE A 140 4369 4168 1861 -66 466 222 ATOM 1127 CA ILE A 140 22.615 21.755 167.911 1.00 28.89 C ANISOU 1127 CA ILE A 140 4557 4391 2031 -75 531 255 ATOM 1128 C ILE A 140 22.981 20.556 167.034 1.00 30.27 C ANISOU 1128 C ILE A 140 4741 4594 2165 -10 585 241 ATOM 1129 O ILE A 140 22.804 20.597 165.816 1.00 23.35 O ANISOU 1129 O ILE A 140 3918 3722 1230 0 625 248 ATOM 1130 CB ILE A 140 23.894 22.513 168.314 1.00 0.00 C ATOM 1131 CG1 ILE A 140 23.580 23.650 169.308 1.00 0.00 C ATOM 1132 CG2 ILE A 140 24.638 23.041 167.074 1.00 0.00 C ATOM 1133 CD1 ILE A 140 24.747 24.510 169.819 1.00 0.00 C ATOM 1134 N LEU A 141 23.476 19.488 167.656 1.00 30.64 N ANISOU 1134 N LEU A 141 4747 4658 2238 37 589 223 ATOM 1135 CA LEU A 141 23.868 18.285 166.922 1.00 31.17 C ANISOU 1135 CA LEU A 141 4835 4736 2272 110 650 204 ATOM 1136 C LEU A 141 22.681 17.618 166.231 1.00 35.58 C ANISOU 1136 C LEU A 141 5506 5246 2767 127 637 159 ATOM 1137 O LEU A 141 22.847 16.954 165.208 1.00 42.32 O ANISOU 1137 O LEU A 141 6403 6102 3576 163 690 138 ATOM 1138 CB LEU A 141 24.559 17.277 167.859 1.00 0.00 C ATOM 1139 CG LEU A 141 25.916 17.594 168.533 1.00 0.00 C ATOM 1140 CD1 LEU A 141 26.346 16.502 169.510 1.00 0.00 C ATOM 1141 CD2 LEU A 141 27.001 17.827 167.482 1.00 0.00 C ATOM 1142 N ALA A 142 21.487 17.796 166.789 1.00 33.93 N ANISOU 1142 N ALA A 142 5330 4999 2563 94 561 142 ATOM 1143 CA ALA A 142 20.270 17.262 166.183 1.00 32.63 C ANISOU 1143 CA ALA A 142 5204 4802 2392 81 514 101 ATOM 1144 C ALA A 142 19.762 18.184 165.080 1.00 33.08 C ANISOU 1144 C ALA A 142 5267 4878 2423 47 501 120 ATOM 1145 O ALA A 142 18.817 17.851 164.363 1.00 34.13 O ANISOU 1145 O ALA A 142 5426 5007 2533 37 466 95 ATOM 1146 CB ALA A 142 19.192 17.056 167.238 1.00 30.65 C ANISOU 1146 CB ALA A 142 4952 4519 2177 62 441 83 ATOM 1147 N SER A 143 20.391 19.346 164.949 1.00 31.67 N ANISOU 1147 N SER A 143 5068 4722 2241 28 530 169 ATOM 1148 CA SER A 143 19.995 20.315 163.937 1.00 32.12 C ANISOU 1148 CA SER A 143 5140 4792 2272 4 525 203 ATOM 1149 C SER A 143 20.945 20.285 162.750 1.00 32.16 C ANISOU 1149 C SER A 143 5152 4836 2231 13 602 220 ATOM 1150 O SER A 143 20.596 20.725 161.656 1.00 33.26 O ANISOU 1150 O SER A 143 5312 4993 2330 1 601 239 ATOM 1151 CB SER A 143 19.945 21.722 164.532 1.00 34.88 C ANISOU 1151 CB SER A 143 5485 5124 2646 -30 511 253 ATOM 1152 OG SER A 143 19.000 21.794 165.585 1.00 37.91 O ANISOU 1152 OG SER A 143 5865 5473 3066 -33 445 235 ATOM 1153 N MET A 144 22.145 19.761 162.978 1.00 30.91 N ANISOU 1153 N MET A 144 4972 4698 2075 39 674 216 ATOM 1154 CA MET A 144 23.181 19.703 161.948 1.00 30.81 C ANISOU 1154 CA MET A 144 4954 4729 2023 54 766 234 ATOM 1155 C MET A 144 22.729 19.031 160.641 1.00 32.72 C ANISOU 1155 C MET A 144 5243 4976 2212 69 770 194 ATOM 1156 O MET A 144 22.966 19.585 159.568 1.00 34.72 O ANISOU 1156 O MET A 144 5507 5265 2421 52 806 224 ATOM 1157 CB MET A 144 24.442 18.994 162.477 1.00 0.00 C ATOM 1158 CG MET A 144 25.812 19.501 161.997 1.00 0.00 C ATOM 1159 SD MET A 144 27.303 18.676 162.611 1.00 0.00 S ATOM 1160 CE MET A 144 28.551 19.660 161.743 1.00 0.00 C ATOM 1161 N PRO A 145 22.074 17.852 160.713 1.00 25.67 N ANISOU 1161 N PRO A 145 4387 4050 1316 93 735 129 ATOM 1162 CA PRO A 145 21.631 17.271 159.439 1.00 26.38 C ANISOU 1162 CA PRO A 145 4532 4150 1343 94 738 88 ATOM 1163 C PRO A 145 20.675 18.186 158.674 1.00 34.50 C ANISOU 1163 C PRO A 145 5569 5206 2334 50 676 120 ATOM 1164 O PRO A 145 20.800 18.328 157.458 1.00 35.76 O ANISOU 1164 O PRO A 145 5755 5405 2428 45 705 127 ATOM 1165 CB PRO A 145 20.919 15.983 159.867 1.00 27.45 C ANISOU 1165 CB PRO A 145 4709 4232 1488 109 698 18 ATOM 1166 CG PRO A 145 21.507 15.648 161.188 1.00 26.61 C ANISOU 1166 CG PRO A 145 4572 4095 1442 144 718 24 ATOM 1167 CD PRO A 145 21.750 16.966 161.848 1.00 26.47 C ANISOU 1167 CD PRO A 145 4492 4105 1460 116 700 90 ATOM 1168 N GLY A 146 19.742 18.807 159.389 1.00 33.30 N ANISOU 1168 N GLY A 146 5397 5037 2218 26 596 143 ATOM 1169 CA GLY A 146 18.802 19.729 158.782 1.00 32.28 C ANISOU 1169 CA GLY A 146 5274 4933 2058 2 539 186 ATOM 1170 C GLY A 146 19.490 20.912 158.129 1.00 31.31 C ANISOU 1170 C GLY A 146 5147 4837 1912 -9 589 259 ATOM 1171 O GLY A 146 19.089 21.351 157.055 1.00 31.80 O ANISOU 1171 O GLY A 146 5234 4937 1913 -18 577 290 ATOM 1172 N LEU A 147 20.531 21.425 158.778 1.00 30.62 N ANISOU 1172 N LEU A 147 5032 4735 1867 -13 645 291 ATOM 1173 CA LEU A 147 21.276 22.568 158.259 1.00 31.28 C ANISOU 1173 CA LEU A 147 5113 4836 1934 -35 703 366 ATOM 1174 C LEU A 147 22.071 22.208 157.006 1.00 32.95 C ANISOU 1174 C LEU A 147 5337 5102 2081 -28 781 364 ATOM 1175 O LEU A 147 22.035 22.930 156.008 1.00 34.27 O ANISOU 1175 O LEU A 147 5527 5298 2197 -45 796 416 ATOM 1176 CB LEU A 147 22.247 23.134 159.312 1.00 0.00 C ATOM 1177 CG LEU A 147 22.897 24.530 159.150 1.00 0.00 C ATOM 1178 CD1 LEU A 147 23.642 24.970 160.409 1.00 0.00 C ATOM 1179 CD2 LEU A 147 23.830 24.555 157.940 1.00 0.00 C ATOM 1180 N TYR A 148 22.781 21.085 157.067 1.00 32.47 N ANISOU 1180 N TYR A 148 5266 5051 2019 2 835 307 ATOM 1181 CA TYR A 148 23.667 20.666 155.986 1.00 29.19 C ANISOU 1181 CA TYR A 148 4862 4683 1546 17 927 298 ATOM 1182 C TYR A 148 22.940 20.500 154.653 1.00 37.17 C ANISOU 1182 C TYR A 148 5929 5724 2470 12 899 282 ATOM 1183 O TYR A 148 23.362 21.051 153.635 1.00 38.98 O ANISOU 1183 O TYR A 148 6170 6000 2642 -3 949 326 ATOM 1184 CB TYR A 148 24.373 19.341 156.329 1.00 0.00 C ATOM 1185 CG TYR A 148 25.856 19.406 156.643 1.00 0.00 C ATOM 1186 CD1 TYR A 148 26.800 19.248 155.612 1.00 0.00 C ATOM 1187 CD2 TYR A 148 26.293 19.604 157.964 1.00 0.00 C ATOM 1188 CE1 TYR A 148 28.175 19.304 155.899 1.00 0.00 C ATOM 1189 CE2 TYR A 148 27.667 19.662 158.253 1.00 0.00 C ATOM 1190 CZ TYR A 148 28.610 19.514 157.219 1.00 0.00 C ATOM 1191 OH TYR A 148 29.945 19.572 157.494 1.00 0.00 O ATOM 1192 N PHE A 149 21.842 19.750 154.664 1.00 35.97 N ANISOU 1192 N PHE A 149 5810 5552 2302 19 820 223 ATOM 1193 CA PHE A 149 21.150 19.407 153.425 1.00 35.84 C ANISOU 1193 CA PHE A 149 5848 5576 2193 14 791 197 ATOM 1194 C PHE A 149 20.027 20.380 153.072 1.00 36.51 C ANISOU 1194 C PHE A 149 5937 5688 2248 -14 704 257 ATOM 1195 O PHE A 149 19.193 20.081 152.220 1.00 37.78 O ANISOU 1195 O PHE A 149 6134 5891 2332 -19 655 237 ATOM 1196 CB PHE A 149 20.596 17.981 153.509 1.00 33.38 C ANISOU 1196 CB PHE A 149 5577 5236 1868 31 761 99 ATOM 1197 CG PHE A 149 21.656 16.932 153.698 1.00 30.75 C ANISOU 1197 CG PHE A 149 5259 4870 1553 73 855 41 ATOM 1198 CD1 PHE A 149 22.470 16.553 152.643 1.00 35.47 C ANISOU 1198 CD1 PHE A 149 5893 5501 2084 95 948 19 ATOM 1199 CD2 PHE A 149 21.842 16.328 154.931 1.00 37.44 C ANISOU 1199 CD2 PHE A 149 6088 5657 2481 99 856 13 ATOM 1200 CE1 PHE A 149 23.450 15.592 152.813 1.00 37.50 C ANISOU 1200 CE1 PHE A 149 6163 5725 2358 151 1045 -29 ATOM 1201 CE2 PHE A 149 22.819 15.366 155.109 1.00 37.88 C ANISOU 1201 CE2 PHE A 149 6158 5683 2552 155 948 -30 ATOM 1202 CZ PHE A 149 23.624 14.998 154.047 1.00 38.73 C ANISOU 1202 CZ PHE A 149 6298 5819 2598 186 1045 -51 ATOM 1203 N SER A 150 20.007 21.543 153.717 1.00 36.30 N ANISOU 1203 N SER A 150 5877 5638 2278 -27 688 332 ATOM 1204 CA SER A 150 19.047 22.584 153.354 1.00 38.42 C ANISOU 1204 CA SER A 150 6155 5924 2519 -41 621 404 ATOM 1205 C SER A 150 19.748 23.693 152.579 1.00 41.63 C ANISOU 1205 C SER A 150 6574 6353 2890 -57 683 492 ATOM 1206 O SER A 150 20.758 24.234 153.029 1.00 41.08 O ANISOU 1206 O SER A 150 6483 6254 2870 -68 752 528 ATOM 1207 CB SER A 150 18.346 23.186 154.586 1.00 0.00 C ATOM 1208 OG SER A 150 18.179 24.598 154.411 1.00 0.00 O ATOM 1209 N LYS A 151 19.207 24.023 151.409 1.00 46.09 N ANISOU 1209 N LYS A 151 7174 6975 3364 -63 657 532 ATOM 1210 CA LYS A 151 19.838 24.980 150.506 1.00 48.85 C ANISOU 1210 CA LYS A 151 7545 7351 3663 -81 718 618 ATOM 1211 C LYS A 151 18.761 25.926 149.942 1.00 49.50 C ANISOU 1211 C LYS A 151 7659 7458 3692 -86 651 705 ATOM 1212 O LYS A 151 17.593 25.542 149.850 1.00 48.39 O ANISOU 1212 O LYS A 151 7516 7336 3533 -75 556 691 ATOM 1213 CB LYS A 151 20.603 24.240 149.403 1.00 52.34 C ANISOU 1213 CB LYS A 151 8009 7859 4019 -82 792 578 ATOM 1214 CG LYS A 151 21.758 23.388 149.904 1.00 56.08 C ANISOU 1214 CG LYS A 151 8456 8314 4540 -70 879 509 ATOM 1215 CD LYS A 151 22.053 22.235 148.957 1.00 60.55 C ANISOU 1215 CD LYS A 151 9056 8931 5019 -53 923 430 ATOM 1216 CE LYS A 151 22.950 21.200 149.621 1.00 63.23 C ANISOU 1216 CE LYS A 151 9373 9237 5415 -25 994 351 ATOM 1217 NZ LYS A 151 22.572 19.806 149.255 1.00 62.79 N1+ ANISOU 1217 NZ LYS A 151 9365 9182 5309 2 981 244 ATOM 1218 N THR A 152 19.150 27.130 149.492 1.00 27.91 N ATOM 1219 CA THR A 152 18.356 27.878 148.512 1.00 28.04 C ATOM 1220 C THR A 152 18.630 27.234 147.138 1.00 26.58 C ATOM 1221 O THR A 152 19.782 26.951 146.811 1.00 27.10 O ATOM 1222 CB THR A 152 18.736 29.370 148.560 1.00 0.00 C ATOM 1223 OG1 THR A 152 17.639 30.114 149.099 1.00 0.00 O ATOM 1224 CG2 THR A 152 19.099 29.950 147.187 1.00 0.00 C ATOM 1225 N GLN A 153 17.586 27.021 146.334 1.00 59.11 N ANISOU 1225 N GLN A 153 8983 8883 4592 -114 588 874 ATOM 1226 CA GLN A 153 17.667 26.526 144.966 1.00 63.79 C ANISOU 1226 CA GLN A 153 9609 9574 5055 -119 600 860 ATOM 1227 C GLN A 153 16.478 27.016 144.153 1.00 67.38 C ANISOU 1227 C GLN A 153 10087 10086 5428 -123 502 928 ATOM 1228 O GLN A 153 15.374 27.162 144.675 1.00 67.78 O ANISOU 1228 O GLN A 153 10117 10120 5515 -117 405 940 ATOM 1229 CB GLN A 153 17.733 24.998 144.917 1.00 65.14 C ANISOU 1229 CB GLN A 153 9772 9783 5197 -99 606 722 ATOM 1230 CG GLN A 153 19.118 24.450 144.613 1.00 67.22 C ANISOU 1230 CG GLN A 153 10047 10052 5441 -103 730 672 ATOM 1231 CD GLN A 153 19.111 22.954 144.382 1.00 68.48 C ANISOU 1231 CD GLN A 153 10227 10239 5555 -81 737 539 ATOM 1232 OE1 GLN A 153 19.779 22.201 145.091 1.00 67.96 O ANISOU 1232 OE1 GLN A 153 10145 10113 5563 -70 789 461 ATOM 1233 NE2 GLN A 153 18.350 22.513 143.387 1.00 70.11 N ANISOU 1233 NE2 GLN A 153 10473 10528 5637 -72 683 514 ATOM 1234 N TRP A 154 16.714 27.270 142.870 1.00 71.24 N ANISOU 1234 N TRP A 154 10618 10646 5803 -139 529 977 ATOM 1235 CA TRP A 154 15.650 27.678 141.964 1.00 73.84 C ANISOU 1235 CA TRP A 154 10974 11046 6037 -151 436 1044 ATOM 1236 C TRP A 154 14.891 26.457 141.457 1.00 75.19 C ANISOU 1236 C TRP A 154 11121 11324 6125 -114 373 946 ATOM 1237 O TRP A 154 15.425 25.661 140.687 1.00 76.78 O ANISOU 1237 O TRP A 154 11349 11588 6238 -91 429 878 ATOM 1238 CB TRP A 154 16.219 28.484 140.782 1.00 0.00 C ATOM 1239 CG TRP A 154 16.311 27.788 139.459 1.00 0.00 C ATOM 1240 CD1 TRP A 154 15.341 27.772 138.516 1.00 0.00 C ATOM 1241 CD2 TRP A 154 17.419 27.007 138.919 1.00 0.00 C ATOM 1242 NE1 TRP A 154 15.773 27.029 137.434 1.00 0.00 N ATOM 1243 CE2 TRP A 154 17.045 26.533 137.629 1.00 0.00 C ATOM 1244 CE3 TRP A 154 18.702 26.654 139.382 1.00 0.00 C ATOM 1245 CZ2 TRP A 154 17.896 25.741 136.844 1.00 0.00 C ATOM 1246 CZ3 TRP A 154 19.566 25.859 138.606 1.00 0.00 C ATOM 1247 CH2 TRP A 154 19.166 25.401 137.339 1.00 0.00 C ATOM 1248 N GLU A 155 13.648 26.308 141.906 1.00 75.53 N ANISOU 1248 N GLU A 155 11122 11382 6194 -94 263 939 ATOM 1249 CA GLU A 155 12.793 25.214 141.455 1.00 78.00 C ANISOU 1249 CA GLU A 155 11430 11780 6425 12 204 851 ATOM 1250 C GLU A 155 11.600 25.743 140.663 1.00 78.60 C ANISOU 1250 C GLU A 155 11520 11933 6412 110 114 934 ATOM 1251 O GLU A 155 10.809 26.533 141.182 1.00 77.18 O ANISOU 1251 O GLU A 155 11261 11766 6296 19 29 1023 ATOM 1252 CB GLU A 155 12.305 24.382 142.643 1.00 79.09 C ANISOU 1252 CB GLU A 155 11547 11845 6657 57 167 751 ATOM 1253 CG GLU A 155 13.140 23.143 142.925 1.00 80.51 C ANISOU 1253 CG GLU A 155 11759 11983 6848 33 236 615 ATOM 1254 CD GLU A 155 12.307 21.990 143.458 1.00 81.45 C ANISOU 1254 CD GLU A 155 11904 12070 6976 62 167 501 ATOM 1255 OE1 GLU A 155 11.062 22.084 143.419 1.00 82.11 O ANISOU 1255 OE1 GLU A 155 12016 12152 7030 112 64 517 ATOM 1256 OE2 GLU A 155 12.897 20.989 143.917 1.00 81.28 O1- ANISOU 1256 OE2 GLU A 155 11893 12006 6984 28 216 396 ATOM 1257 N PHE A 156 11.481 25.295 139.414 1.00 80.31 N ANISOU 1257 N PHE A 156 11865 12176 6474 214 117 900 ATOM 1258 CA PHE A 156 10.423 25.737 138.505 1.00 82.75 C ANISOU 1258 CA PHE A 156 12449 12333 6658 353 38 935 ATOM 1259 C PHE A 156 10.408 27.259 138.377 1.00 83.56 C ANISOU 1259 C PHE A 156 12963 12010 6774 135 3 1023 ATOM 1260 O PHE A 156 9.347 27.886 138.418 1.00 83.55 O ANISOU 1260 O PHE A 156 12951 12043 6752 -7 -139 1110 ATOM 1261 CB PHE A 156 9.049 25.224 138.975 1.00 0.00 C ATOM 1262 CG PHE A 156 8.854 23.726 138.905 1.00 0.00 C ATOM 1263 CD1 PHE A 156 9.031 22.941 140.059 1.00 0.00 C ATOM 1264 CD2 PHE A 156 8.495 23.117 137.690 1.00 0.00 C ATOM 1265 CE1 PHE A 156 8.845 21.550 139.998 1.00 0.00 C ATOM 1266 CE2 PHE A 156 8.309 21.724 137.629 1.00 0.00 C ATOM 1267 CZ PHE A 156 8.484 20.941 138.784 1.00 0.00 C ATOM 1268 N THR A 157 11.602 27.831 138.231 1.00 84.55 N ANISOU 1268 N THR A 157 12479 12703 6943 -328 31 1180 ATOM 1269 CA THR A 157 11.805 29.275 138.102 1.00 86.16 C ANISOU 1269 CA THR A 157 12890 12696 7149 -348 44 1302 ATOM 1270 C THR A 157 11.346 30.050 139.339 1.00 85.92 C ANISOU 1270 C THR A 157 12868 12524 7252 -276 13 1357 ATOM 1271 O THR A 157 11.050 31.242 139.255 1.00 86.98 O ANISOU 1271 O THR A 157 13058 12605 7385 -218 -6 1490 ATOM 1272 CB THR A 157 11.089 29.813 136.849 1.00 0.00 C ATOM 1273 OG1 THR A 157 11.620 29.159 135.691 1.00 0.00 O ATOM 1274 CG2 THR A 157 11.233 31.329 136.669 1.00 0.00 C ATOM 1275 N HIS A 158 11.294 29.372 140.482 1.00 84.80 N ANISOU 1275 N HIS A 158 12628 12369 7224 -269 13 1265 ATOM 1276 CA HIS A 158 10.977 30.011 141.759 1.00 84.55 C ANISOU 1276 CA HIS A 158 12563 12239 7323 -201 0 1308 ATOM 1277 C HIS A 158 11.999 29.601 142.814 1.00 84.63 C ANISOU 1277 C HIS A 158 12440 12260 7455 -188 101 1241 ATOM 1278 O HIS A 158 12.303 28.418 142.958 1.00 89.44 O ANISOU 1278 O HIS A 158 12962 12950 8071 -194 127 1124 ATOM 1279 CB HIS A 158 9.567 29.646 142.258 1.00 0.00 C ATOM 1280 CG HIS A 158 8.413 30.024 141.358 1.00 0.00 C ATOM 1281 ND1 HIS A 158 7.568 29.121 140.854 1.00 0.00 N ATOM 1282 CD2 HIS A 158 7.994 31.245 140.887 1.00 0.00 C ATOM 1283 CE1 HIS A 158 6.657 29.754 140.097 1.00 0.00 C ATOM 1284 NE2 HIS A 158 6.876 31.068 140.081 1.00 0.00 N ATOM 1285 N HIS A 159 12.531 30.573 143.551 1.00 80.81 N ANISOU 1285 N HIS A 159 11950 11690 7062 -143 164 1315 ATOM 1286 CA HIS A 159 13.483 30.273 144.617 1.00 76.31 C ANISOU 1286 CA HIS A 159 11312 11079 6604 -126 253 1251 ATOM 1287 C HIS A 159 12.793 29.652 145.824 1.00 69.61 C ANISOU 1287 C HIS A 159 10408 10197 5843 -109 195 1171 ATOM 1288 O HIS A 159 11.735 30.111 146.252 1.00 69.22 O ANISOU 1288 O HIS A 159 10380 10103 5817 -84 112 1217 ATOM 1289 CB HIS A 159 14.240 31.539 145.059 1.00 0.00 C ATOM 1290 CG HIS A 159 14.763 32.432 143.958 1.00 0.00 C ATOM 1291 ND1 HIS A 159 15.980 32.282 143.428 1.00 0.00 N ATOM 1292 CD2 HIS A 159 14.188 33.495 143.304 1.00 0.00 C ATOM 1293 CE1 HIS A 159 16.158 33.217 142.480 1.00 0.00 C ATOM 1294 NE2 HIS A 159 15.083 33.994 142.365 1.00 0.00 N ATOM 1295 N THR A 160 13.399 28.605 146.371 1.00 63.37 N ANISOU 1295 N THR A 160 9554 9425 5099 -108 242 1055 ATOM 1296 CA THR A 160 12.891 27.988 147.587 1.00 56.74 C ANISOU 1296 CA THR A 160 8659 8551 4347 -92 201 978 ATOM 1297 C THR A 160 14.021 27.677 148.558 1.00 51.95 C ANISOU 1297 C THR A 160 8023 7885 3832 -77 294 917 ATOM 1298 O THR A 160 15.101 27.237 148.160 1.00 51.48 O ANISOU 1298 O THR A 160 7968 7845 3749 -84 377 877 ATOM 1299 CB THR A 160 12.110 26.694 147.292 1.00 0.00 C ATOM 1300 OG1 THR A 160 12.998 25.736 146.706 1.00 0.00 O ATOM 1301 CG2 THR A 160 10.918 26.903 146.351 1.00 0.00 C ATOM 1302 N CYS A 161 13.769 27.936 149.834 1.00 47.96 N ANISOU 1302 N CYS A 161 7497 7301 3426 -59 278 914 ATOM 1303 CA CYS A 161 14.651 27.477 150.893 1.00 42.81 C ANISOU 1303 CA CYS A 161 6812 6580 2872 -50 342 838 ATOM 1304 C CYS A 161 14.089 26.167 151.415 1.00 38.63 C ANISOU 1304 C CYS A 161 6237 6087 2353 -47 292 730 ATOM 1305 O CYS A 161 13.181 26.164 152.242 1.00 38.60 O ANISOU 1305 O CYS A 161 6209 6063 2396 -38 228 723 ATOM 1306 CB CYS A 161 14.760 28.515 152.010 1.00 41.86 C ANISOU 1306 CB CYS A 161 6699 6346 2859 -28 361 889 ATOM 1307 SG CYS A 161 15.854 28.049 153.369 1.00 46.02 S ANISOU 1307 SG CYS A 161 7190 6796 3498 -33 431 806 ATOM 1308 N SER A 162 14.611 25.055 150.910 1.00 37.27 N ANISOU 1308 N SER A 162 6062 5963 2135 -51 326 646 ATOM 1309 CA SER A 162 14.077 23.754 151.265 1.00 37.17 C ANISOU 1309 CA SER A 162 6026 5973 2124 -39 284 543 ATOM 1310 C SER A 162 15.137 22.706 151.530 1.00 36.47 C ANISOU 1310 C SER A 162 5945 5844 2068 -40 358 447 ATOM 1311 O SER A 162 16.316 22.925 151.250 1.00 36.53 O ANISOU 1311 O SER A 162 5968 5834 2079 -46 444 460 ATOM 1312 CB SER A 162 13.142 23.263 150.144 1.00 0.00 C ATOM 1313 OG SER A 162 13.905 22.962 148.969 1.00 0.00 O ATOM 1314 N LEU A 163 14.717 21.557 152.081 1.00 35.06 N ANISOU 1314 N LEU A 163 5759 5650 1913 -34 326 356 ATOM 1315 CA LEU A 163 15.593 20.419 152.375 1.00 36.04 C ANISOU 1315 CA LEU A 163 5899 5728 2067 -35 388 263 ATOM 1316 C LEU A 163 15.865 19.558 151.145 1.00 39.70 C ANISOU 1316 C LEU A 163 6419 6239 2427 -36 420 205 ATOM 1317 O LEU A 163 14.958 19.307 150.353 1.00 42.53 O ANISOU 1317 O LEU A 163 6805 6658 2696 -38 359 193 ATOM 1318 CB LEU A 163 14.791 19.630 153.427 1.00 0.00 C ATOM 1319 CG LEU A 163 13.817 20.335 154.402 1.00 0.00 C ATOM 1320 CD1 LEU A 163 12.758 21.154 153.669 1.00 0.00 C ATOM 1321 CD2 LEU A 163 13.156 19.320 155.335 1.00 0.00 C ATOM 1322 N HIS A 164 17.107 19.111 150.995 1.00 41.24 N ANISOU 1322 N HIS A 164 6634 6407 2628 -31 517 170 ATOM 1323 CA HIS A 164 17.487 18.267 149.870 1.00 43.03 C ANISOU 1323 CA HIS A 164 6924 6667 2758 -28 565 108 ATOM 1324 C HIS A 164 18.329 17.079 150.321 1.00 42.87 C ANISOU 1324 C HIS A 164 6930 6579 2779 -12 639 19 ATOM 1325 O HIS A 164 19.448 16.883 149.847 1.00 43.27 O ANISOU 1325 O HIS A 164 7001 6633 2808 7 740 7 ATOM 1326 CB HIS A 164 18.253 19.087 148.815 1.00 0.00 C ATOM 1327 CG HIS A 164 18.343 18.489 147.430 1.00 0.00 C ATOM 1328 ND1 HIS A 164 19.341 17.683 147.058 1.00 0.00 N ATOM 1329 CD2 HIS A 164 17.520 18.610 146.336 1.00 0.00 C ATOM 1330 CE1 HIS A 164 19.149 17.317 145.781 1.00 0.00 C ATOM 1331 NE2 HIS A 164 18.040 17.864 145.286 1.00 0.00 N ATOM 1332 N PHE A 165 17.782 16.291 151.240 1.00 42.66 N ANISOU 1332 N PHE A 165 6905 6491 2812 -15 593 -39 ATOM 1333 CA PHE A 165 18.444 15.080 151.711 1.00 43.12 C ANISOU 1333 CA PHE A 165 7001 6474 2909 7 657 -120 ATOM 1334 C PHE A 165 18.903 14.038 150.551 1.00 44.86 C ANISOU 1334 C PHE A 165 7316 6698 3031 8 696 -204 ATOM 1335 O PHE A 165 18.994 12.845 150.862 1.00 45.67 O ANISOU 1335 O PHE A 165 7459 6849 3045 -24 632 -225 ATOM 1336 CB PHE A 165 17.700 14.483 152.909 1.00 43.80 C ANISOU 1336 CB PHE A 165 7077 6492 3071 -5 593 -155 ATOM 1337 CG PHE A 165 17.614 15.395 154.097 1.00 44.67 C ANISOU 1337 CG PHE A 165 7105 6590 3278 -4 559 -86 ATOM 1338 CD1 PHE A 165 16.570 16.296 154.222 1.00 45.01 C ANISOU 1338 CD1 PHE A 165 7105 6673 3322 -27 470 -30 ATOM 1339 CD2 PHE A 165 18.567 15.337 155.100 1.00 45.06 C ANISOU 1339 CD2 PHE A 165 7121 6587 3411 27 618 -77 ATOM 1340 CE1 PHE A 165 16.486 17.131 155.320 1.00 44.45 C ANISOU 1340 CE1 PHE A 165 6970 6582 3337 -24 445 28 ATOM 1341 CE2 PHE A 165 18.490 16.170 156.199 1.00 43.90 C ANISOU 1341 CE2 PHE A 165 6908 6429 3345 23 586 -20 ATOM 1342 CZ PHE A 165 17.448 17.068 156.309 1.00 43.69 C ANISOU 1342 CZ PHE A 165 6848 6431 3320 -4 501 29 ATOM 1343 N PRO A 166 19.340 14.337 149.269 1.00 45.49 N ATOM 1344 CA PRO A 166 20.667 13.884 148.817 1.00 46.48 C ATOM 1345 C PRO A 166 21.775 14.969 148.850 1.00 46.57 C ATOM 1346 O PRO A 166 21.715 15.895 149.629 1.00 47.48 O ATOM 1347 CD PRO A 166 18.590 14.667 148.011 1.00 0.00 C ATOM 1348 CB PRO A 166 20.364 13.437 147.392 1.00 0.00 C ATOM 1349 CG PRO A 166 19.572 14.525 146.806 1.00 0.00 C ATOM 1350 N HIS A 167 22.780 14.815 147.975 1.00 46.56 N ATOM 1351 CA HIS A 167 23.910 15.660 147.528 1.00 46.60 C ATOM 1352 C HIS A 167 25.145 14.783 147.647 1.00 45.94 C ATOM 1353 O HIS A 167 25.749 14.449 146.640 1.00 45.45 O ATOM 1354 CB HIS A 167 24.113 17.024 148.235 1.00 0.00 C ATOM 1355 CG HIS A 167 24.574 18.122 147.318 1.00 0.00 C ATOM 1356 ND1 HIS A 167 25.782 18.796 147.468 1.00 0.00 N ATOM 1357 CD2 HIS A 167 23.839 18.769 146.343 1.00 0.00 C ATOM 1358 CE1 HIS A 167 25.785 19.746 146.543 1.00 0.00 C ATOM 1359 NE2 HIS A 167 24.633 19.803 145.870 1.00 0.00 N ATOM 1360 N GLU A 168 25.379 14.307 148.868 1.00 45.12 N ATOM 1361 CA GLU A 168 26.131 13.116 149.218 1.00 45.15 C ATOM 1362 C GLU A 168 24.990 12.154 149.596 1.00 44.68 C ATOM 1363 O GLU A 168 24.130 12.522 150.399 1.00 44.85 O ATOM 1364 CB GLU A 168 27.027 13.451 150.436 1.00 0.00 C ATOM 1365 CG GLU A 168 27.927 14.689 150.201 1.00 0.00 C ATOM 1366 CD GLU A 168 28.575 15.207 151.473 1.00 0.00 C ATOM 1367 OE1 GLU A 168 29.669 14.706 151.800 1.00 0.00 O ATOM 1368 OE2 GLU A 168 27.952 16.102 152.084 1.00 0.00 O1- ATOM 1369 N SER A 169 24.890 10.979 148.958 1.00 43.43 N ATOM 1370 CA SER A 169 24.033 9.865 149.393 1.00 42.93 C ATOM 1371 C SER A 169 22.502 10.109 149.297 1.00 42.14 C ATOM 1372 O SER A 169 21.793 10.281 150.279 1.00 42.83 O ATOM 1373 CB SER A 169 24.513 9.375 150.778 1.00 0.00 C ATOM 1374 OG SER A 169 25.248 8.177 150.653 1.00 0.00 O ATOM 1375 N LEU A 170 21.913 10.135 148.095 1.00 42.35 N ATOM 1376 CA LEU A 170 20.471 10.368 147.905 1.00 41.75 C ATOM 1377 C LEU A 170 19.593 9.336 148.550 1.00 41.87 C ATOM 1378 O LEU A 170 19.835 8.238 148.052 1.00 42.26 O ATOM 1379 CB LEU A 170 20.190 10.366 146.345 1.00 0.00 C ATOM 1380 CG LEU A 170 18.727 10.316 145.736 1.00 0.00 C ATOM 1381 CD1 LEU A 170 17.706 11.353 146.251 1.00 0.00 C ATOM 1382 CD2 LEU A 170 18.774 10.534 144.210 1.00 0.00 C ATOM 1383 N ARG A 171 18.567 9.710 149.435 1.00 55.65 N ANISOU 1383 N ARG A 171 8998 7877 4269 -2 780 -519 ATOM 1384 CA ARG A 171 17.267 9.013 149.926 1.00 55.65 C ANISOU 1384 CA ARG A 171 9063 7810 4271 -59 706 -589 ATOM 1385 C ARG A 171 17.444 8.456 151.336 1.00 55.78 C ANISOU 1385 C ARG A 171 9069 7720 4406 -37 722 -596 ATOM 1386 O ARG A 171 16.505 8.457 152.134 1.00 56.28 O ANISOU 1386 O ARG A 171 9103 7766 4515 -85 633 -586 ATOM 1387 CB ARG A 171 17.216 7.869 148.917 1.00 0.00 C ATOM 1388 CG ARG A 171 17.994 6.565 149.202 1.00 0.00 C ATOM 1389 CD ARG A 171 17.933 5.429 148.181 1.00 0.00 C ATOM 1390 NE ARG A 171 18.722 4.264 148.597 1.00 0.00 N ATOM 1391 CZ ARG A 171 20.028 4.088 148.326 1.00 0.00 C ATOM 1392 NH1 ARG A 171 20.696 4.990 147.575 1.00 0.00 N ATOM 1393 NH2 ARG A 171 20.642 2.991 148.814 1.00 0.00 N1+ ATOM 1394 N GLU A 172 18.653 7.994 151.639 1.00 54.90 N ANISOU 1394 N GLU A 172 8979 7542 4338 41 838 -607 ATOM 1395 CA GLU A 172 18.940 7.407 152.935 1.00 53.47 C ANISOU 1395 CA GLU A 172 8799 7260 4259 79 865 -609 ATOM 1396 C GLU A 172 18.918 8.412 154.071 1.00 50.64 C ANISOU 1396 C GLU A 172 8311 6940 3991 86 817 -518 ATOM 1397 O GLU A 172 18.503 8.093 155.185 1.00 48.80 O ANISOU 1397 O GLU A 172 8069 6648 3826 75 778 -515 ATOM 1398 CB GLU A 172 20.316 6.716 152.890 1.00 0.00 C ATOM 1399 CG GLU A 172 21.158 6.936 151.623 1.00 0.00 C ATOM 1400 CD GLU A 172 22.519 6.247 151.590 1.00 0.00 C ATOM 1401 OE1 GLU A 172 22.577 5.091 151.113 1.00 0.00 O ATOM 1402 OE2 GLU A 172 23.486 6.897 152.041 1.00 0.00 O1- ATOM 1403 N TRP A 173 19.361 9.632 153.787 1.00 48.41 N ANISOU 1403 N TRP A 173 7936 6753 3705 100 822 -444 ATOM 1404 CA TRP A 173 19.466 10.664 154.812 1.00 45.28 C ANISOU 1404 CA TRP A 173 7426 6388 3391 106 788 -358 ATOM 1405 C TRP A 173 18.112 11.234 155.215 1.00 42.94 C ANISOU 1405 C TRP A 173 7085 6124 3108 37 661 -331 ATOM 1406 O TRP A 173 17.938 11.687 156.346 1.00 42.87 O ANISOU 1406 O TRP A 173 7009 6103 3176 36 623 -287 ATOM 1407 CB TRP A 173 20.383 11.787 154.334 1.00 45.87 C ANISOU 1407 CB TRP A 173 7430 6543 3455 131 841 -288 ATOM 1408 CG TRP A 173 21.821 11.408 154.382 1.00 47.22 C ANISOU 1408 CG TRP A 173 7603 6692 3648 211 970 -290 ATOM 1409 CD1 TRP A 173 22.584 10.945 153.352 1.00 49.23 C ANISOU 1409 CD1 TRP A 173 7910 6954 3839 252 1068 -325 ATOM 1410 CD2 TRP A 173 22.673 11.444 155.531 1.00 46.08 C ANISOU 1410 CD2 TRP A 173 7398 6520 3591 269 1018 -251 ATOM 1411 NE1 TRP A 173 23.863 10.696 153.787 1.00 48.84 N ANISOU 1411 NE1 TRP A 173 7829 6886 3840 339 1179 -307 ATOM 1412 CE2 TRP A 173 23.943 10.995 155.120 1.00 47.38 C ANISOU 1412 CE2 TRP A 173 7573 6683 3745 351 1148 -260 ATOM 1413 CE3 TRP A 173 22.485 11.816 156.865 1.00 45.43 C ANISOU 1413 CE3 TRP A 173 7252 6421 3590 263 965 -208 ATOM 1414 CZ2 TRP A 173 25.020 10.909 155.998 1.00 48.63 C ANISOU 1414 CZ2 TRP A 173 7669 6835 3975 432 1223 -220 ATOM 1415 CZ3 TRP A 173 23.555 11.729 157.734 1.00 46.66 C ANISOU 1415 CZ3 TRP A 173 7357 6567 3806 336 1035 -174 ATOM 1416 CH2 TRP A 173 24.807 11.279 157.297 1.00 49.82 C ANISOU 1416 CH2 TRP A 173 7757 6975 4196 422 1162 -177 ATOM 1417 N LYS A 174 17.156 11.216 154.294 1.00 42.31 N ANISOU 1417 N LYS A 174 7040 6088 2947 -16 597 -356 ATOM 1418 CA LYS A 174 15.811 11.676 154.608 1.00 41.56 C ANISOU 1418 CA LYS A 174 6903 6031 2858 -71 481 -330 ATOM 1419 C LYS A 174 15.099 10.676 155.509 1.00 41.47 C ANISOU 1419 C LYS A 174 6929 5939 2889 -107 441 -382 ATOM 1420 O LYS A 174 14.309 11.056 156.374 1.00 39.77 O ANISOU 1420 O LYS A 174 6654 5733 2725 -132 371 -348 ATOM 1421 CB LYS A 174 14.994 11.912 153.324 1.00 0.00 C ATOM 1422 CG LYS A 174 15.510 11.114 152.122 1.00 0.00 C ATOM 1423 CD LYS A 174 14.747 11.368 150.816 1.00 0.00 C ATOM 1424 CE LYS A 174 15.249 10.577 149.600 1.00 0.00 C ATOM 1425 NZ LYS A 174 14.483 10.858 148.374 1.00 0.00 N1+ ATOM 1426 N LEU A 175 15.386 9.395 155.297 1.00 42.32 N ANISOU 1426 N LEU A 175 7141 5964 2973 -109 494 -464 ATOM 1427 CA LEU A 175 14.840 8.340 156.138 1.00 39.68 C ANISOU 1427 CA LEU A 175 6864 5536 2678 -147 474 -514 ATOM 1428 C LEU A 175 15.397 8.434 157.546 1.00 37.37 C ANISOU 1428 C LEU A 175 6520 5192 2486 -96 504 -471 ATOM 1429 O LEU A 175 14.657 8.340 158.525 1.00 36.49 O ANISOU 1429 O LEU A 175 6384 5058 2423 -133 447 -460 ATOM 1430 CB LEU A 175 15.146 6.952 155.545 1.00 0.00 C ATOM 1431 CG LEU A 175 14.551 6.499 154.190 1.00 0.00 C ATOM 1432 CD1 LEU A 175 15.089 5.140 153.747 1.00 0.00 C ATOM 1433 CD2 LEU A 175 13.024 6.476 154.250 1.00 0.00 C ATOM 1434 N PHE A 176 16.709 8.622 157.639 1.00 36.01 N ANISOU 1434 N PHE A 176 6331 5009 2341 -12 594 -446 ATOM 1435 CA PHE A 176 17.365 8.741 158.931 1.00 33.83 C ANISOU 1435 CA PHE A 176 6005 4698 2152 44 626 -402 ATOM 1436 C PHE A 176 16.856 9.954 159.693 1.00 31.89 C ANISOU 1436 C PHE A 176 5643 4519 1955 18 548 -328 ATOM 1437 O PHE A 176 16.590 9.877 160.891 1.00 31.96 O ANISOU 1437 O PHE A 176 5625 4495 2022 15 520 -309 ATOM 1438 CB PHE A 176 18.881 8.834 158.772 1.00 33.34 C ANISOU 1438 CB PHE A 176 5931 4637 2100 138 736 -380 ATOM 1439 CG PHE A 176 19.581 9.307 160.011 1.00 31.45 C ANISOU 1439 CG PHE A 176 5611 4400 1938 192 755 -316 ATOM 1440 CD1 PHE A 176 19.743 8.458 161.094 1.00 31.00 C ANISOU 1440 CD1 PHE A 176 5590 4262 1927 234 776 -324 ATOM 1441 CD2 PHE A 176 20.062 10.603 160.102 1.00 29.85 C ANISOU 1441 CD2 PHE A 176 5305 4282 1757 197 751 -245 ATOM 1442 CE1 PHE A 176 20.377 8.890 162.243 1.00 30.08 C ANISOU 1442 CE1 PHE A 176 5397 4161 1869 284 787 -262 ATOM 1443 CE2 PHE A 176 20.698 11.041 161.247 1.00 30.19 C ANISOU 1443 CE2 PHE A 176 5276 4332 1861 236 763 -190 ATOM 1444 CZ PHE A 176 20.856 10.183 162.320 1.00 30.02 C ANISOU 1444 CZ PHE A 176 5283 4244 1880 282 779 -198 ATOM 1445 N GLN A 177 16.728 11.076 158.994 1.00 27.56 N ANISOU 1445 N GLN A 177 5034 4060 1378 3 519 -286 ATOM 1446 CA GLN A 177 16.278 12.311 159.621 1.00 35.08 C ANISOU 1446 CA GLN A 177 5888 5066 2373 -12 457 -215 ATOM 1447 C GLN A 177 14.860 12.169 160.160 1.00 31.47 C ANISOU 1447 C GLN A 177 5421 4608 1928 -67 364 -223 ATOM 1448 O GLN A 177 14.533 12.704 161.218 1.00 28.97 O ANISOU 1448 O GLN A 177 5044 4294 1671 -69 328 -183 ATOM 1449 CB GLN A 177 16.351 13.482 158.624 1.00 0.00 C ATOM 1450 CG GLN A 177 15.912 14.873 159.114 1.00 0.00 C ATOM 1451 CD GLN A 177 16.708 15.416 160.291 1.00 0.00 C ATOM 1452 OE1 GLN A 177 17.885 15.112 160.457 1.00 0.00 O ATOM 1453 NE2 GLN A 177 16.071 16.224 161.132 1.00 0.00 N ATOM 1454 N ALA A 178 14.027 11.435 159.431 1.00 31.78 N ANISOU 1454 N ALA A 178 5523 4646 1907 -116 329 -277 ATOM 1455 CA ALA A 178 12.640 11.237 159.826 1.00 30.51 C ANISOU 1455 CA ALA A 178 5353 4494 1745 -180 243 -287 ATOM 1456 C ALA A 178 12.535 10.446 161.127 1.00 30.46 C ANISOU 1456 C ALA A 178 5366 4407 1801 -192 249 -305 ATOM 1457 O ALA A 178 11.846 10.864 162.056 1.00 30.43 O ANISOU 1457 O ALA A 178 5302 4420 1840 -209 200 -270 ATOM 1458 CB ALA A 178 11.838 10.517 158.726 1.00 0.00 C ATOM 1459 N LEU A 179 13.224 9.310 161.200 1.00 31.55 N ANISOU 1459 N LEU A 179 5594 4455 1938 -177 316 -358 ATOM 1460 CA LEU A 179 13.152 8.466 162.389 1.00 30.87 C ANISOU 1460 CA LEU A 179 5547 4283 1900 -185 328 -372 ATOM 1461 C LEU A 179 13.867 9.112 163.572 1.00 30.72 C ANISOU 1461 C LEU A 179 5452 4266 1953 -120 350 -309 ATOM 1462 O LEU A 179 13.493 8.889 164.720 1.00 31.39 O ANISOU 1462 O LEU A 179 5527 4321 2079 -133 329 -294 ATOM 1463 CB LEU A 179 13.741 7.066 162.137 1.00 0.00 C ATOM 1464 CG LEU A 179 13.758 5.981 163.242 1.00 0.00 C ATOM 1465 CD1 LEU A 179 12.351 5.579 163.678 1.00 0.00 C ATOM 1466 CD2 LEU A 179 14.547 4.755 162.786 1.00 0.00 C ATOM 1467 N LYS A 180 14.884 9.922 163.294 1.00 30.34 N ANISOU 1467 N LYS A 180 5352 4259 1914 -57 391 -272 ATOM 1468 CA LYS A 180 15.605 10.614 164.355 1.00 29.70 C ANISOU 1468 CA LYS A 180 5199 4190 1894 -7 407 -214 ATOM 1469 C LYS A 180 14.719 11.677 164.985 1.00 30.77 C ANISOU 1469 C LYS A 180 5247 4382 2063 -42 332 -169 ATOM 1470 O LYS A 180 14.675 11.821 166.204 1.00 31.86 O ANISOU 1470 O LYS A 180 5350 4507 2248 -35 318 -142 ATOM 1471 CB LYS A 180 16.897 11.260 163.820 1.00 0.00 C ATOM 1472 CG LYS A 180 17.906 10.242 163.282 1.00 0.00 C ATOM 1473 CD LYS A 180 18.511 9.322 164.349 1.00 0.00 C ATOM 1474 CE LYS A 180 19.495 9.997 165.314 1.00 0.00 C ATOM 1475 NZ LYS A 180 20.046 9.069 166.318 1.00 0.00 N1+ ATOM 1476 N LEU A 181 14.018 12.424 164.140 1.00 32.43 N ANISOU 1476 N LEU A 181 5426 4656 2241 -73 287 -157 ATOM 1477 CA LEU A 181 13.105 13.459 164.604 1.00 35.54 C ANISOU 1477 CA LEU A 181 5747 5100 2657 -92 224 -112 ATOM 1478 C LEU A 181 11.978 12.851 165.435 1.00 37.65 C ANISOU 1478 C LEU A 181 6020 5349 2938 -137 177 -129 ATOM 1479 O LEU A 181 11.584 13.402 166.464 1.00 37.47 O ANISOU 1479 O LEU A 181 5943 5335 2957 -134 152 -96 ATOM 1480 CB LEU A 181 12.533 14.245 163.409 1.00 0.00 C ATOM 1481 CG LEU A 181 11.550 15.424 163.610 1.00 0.00 C ATOM 1482 CD1 LEU A 181 12.182 16.580 164.381 1.00 0.00 C ATOM 1483 CD2 LEU A 181 11.008 15.911 162.266 1.00 0.00 C ATOM 1484 N ASN A 182 11.474 11.704 164.990 1.00 40.09 N ANISOU 1484 N ASN A 182 6399 5626 3207 -185 168 -183 ATOM 1485 CA ASN A 182 10.404 11.011 165.698 1.00 42.60 C ANISOU 1485 CA ASN A 182 6733 5924 3528 -248 128 -201 ATOM 1486 C ASN A 182 10.834 10.486 167.060 1.00 40.31 C ANISOU 1486 C ASN A 182 6458 5568 3290 -230 161 -195 ATOM 1487 O ASN A 182 10.038 10.444 167.994 1.00 40.61 O ANISOU 1487 O ASN A 182 6471 5612 3349 -266 130 -180 ATOM 1488 CB ASN A 182 9.871 9.856 164.855 1.00 48.20 C ANISOU 1488 CB ASN A 182 7532 6605 4177 -321 117 -267 ATOM 1489 CG ASN A 182 8.972 10.325 163.739 1.00 53.83 C ANISOU 1489 CG ASN A 182 8220 7404 4830 -362 55 -268 ATOM 1490 OD1 ASN A 182 7.813 10.667 163.969 1.00 53.14 O ANISOU 1490 OD1 ASN A 182 8079 7378 4734 -410 -10 -245 ATOM 1491 ND2 ASN A 182 9.498 10.348 162.520 1.00 58.31 N ANISOU 1491 ND2 ASN A 182 8823 7984 5348 -342 76 -289 ATOM 1492 N LEU A 183 12.091 10.076 167.170 1.00 37.60 N ANISOU 1492 N LEU A 183 6157 5168 2961 -173 226 -202 ATOM 1493 CA LEU A 183 12.611 9.598 168.444 1.00 34.58 C ANISOU 1493 CA LEU A 183 5792 4729 2617 -141 257 -186 ATOM 1494 C LEU A 183 12.756 10.748 169.434 1.00 34.38 C ANISOU 1494 C LEU A 183 5667 4755 2641 -110 236 -129 ATOM 1495 O LEU A 183 12.224 10.692 170.540 1.00 38.74 O ANISOU 1495 O LEU A 183 6201 5303 3217 -129 214 -111 ATOM 1496 CB LEU A 183 13.972 8.897 168.276 1.00 0.00 C ATOM 1497 CG LEU A 183 14.722 8.281 169.482 1.00 0.00 C ATOM 1498 CD1 LEU A 183 13.938 7.140 170.128 1.00 0.00 C ATOM 1499 CD2 LEU A 183 16.114 7.805 169.069 1.00 0.00 C ATOM 1500 N PHE A 184 13.464 11.795 169.022 1.00 30.47 N ANISOU 1500 N PHE A 184 5116 4306 2155 -70 247 -103 ATOM 1501 CA PHE A 184 13.767 12.911 169.910 1.00 28.20 C ANISOU 1501 CA PHE A 184 4753 4054 1909 -47 235 -57 ATOM 1502 C PHE A 184 12.538 13.760 170.229 1.00 27.51 C ANISOU 1502 C PHE A 184 4611 4009 1832 -80 181 -38 ATOM 1503 O PHE A 184 12.463 14.377 171.293 1.00 27.10 O ANISOU 1503 O PHE A 184 4518 3966 1812 -72 170 -13 ATOM 1504 CB PHE A 184 14.864 13.798 169.292 1.00 0.00 C ATOM 1505 CG PHE A 184 16.236 13.167 169.197 1.00 0.00 C ATOM 1506 CD1 PHE A 184 16.522 12.000 169.928 1.00 0.00 C ATOM 1507 CD2 PHE A 184 17.223 13.744 168.381 1.00 0.00 C ATOM 1508 CE1 PHE A 184 17.793 11.408 169.838 1.00 0.00 C ATOM 1509 CE2 PHE A 184 18.496 13.152 168.291 1.00 0.00 C ATOM 1510 CZ PHE A 184 18.780 11.983 169.020 1.00 0.00 C ATOM 1511 N GLY A 185 11.576 13.790 169.312 1.00 26.75 N ANISOU 1511 N GLY A 185 4520 3943 1701 -113 150 -50 ATOM 1512 CA GLY A 185 10.423 14.660 169.458 1.00 26.21 C ANISOU 1512 CA GLY A 185 4402 3927 1630 -129 104 -24 ATOM 1513 C GLY A 185 9.121 13.968 169.817 1.00 26.24 C ANISOU 1513 C GLY A 185 4412 3942 1615 -184 68 -38 ATOM 1514 O GLY A 185 8.085 14.621 169.954 1.00 25.35 O ANISOU 1514 O GLY A 185 4257 3883 1491 -195 32 -12 ATOM 1515 N LEU A 186 9.164 12.649 169.975 1.00 26.13 N ANISOU 1515 N LEU A 186 4459 3878 1593 -223 81 -75 ATOM 1516 CA LEU A 186 7.954 11.890 170.264 1.00 26.69 C ANISOU 1516 CA LEU A 186 4545 3957 1640 -301 50 -91 ATOM 1517 C LEU A 186 8.230 10.676 171.145 1.00 28.54 C ANISOU 1517 C LEU A 186 4845 4112 1885 -328 82 -110 ATOM 1518 O LEU A 186 7.711 10.585 172.254 1.00 30.65 O ANISOU 1518 O LEU A 186 5094 4384 2168 -350 79 -89 ATOM 1519 CB LEU A 186 7.280 11.453 168.963 1.00 26.65 C ANISOU 1519 CB LEU A 186 4570 3981 1575 -364 14 -124 ATOM 1520 CG LEU A 186 6.049 10.553 169.074 1.00 23.33 C ANISOU 1520 CG LEU A 186 4170 3575 1118 -476 -24 -148 ATOM 1521 CD1 LEU A 186 4.985 11.184 169.960 1.00 23.40 C ANISOU 1521 CD1 LEU A 186 4093 3661 1137 -497 -55 -102 ATOM 1522 CD2 LEU A 186 5.490 10.261 167.691 1.00 24.29 C ANISOU 1522 CD2 LEU A 186 4314 3737 1176 -539 -68 -183 ATOM 1523 N VAL A 187 9.046 9.748 170.655 1.00 29.89 N ANISOU 1523 N VAL A 187 5104 4211 2043 -320 119 -146 ATOM 1524 CA VAL A 187 9.337 8.522 171.396 1.00 30.25 C ANISOU 1524 CA VAL A 187 5239 4166 2088 -336 157 -160 ATOM 1525 C VAL A 187 10.027 8.809 172.728 1.00 31.65 C ANISOU 1525 C VAL A 187 5384 4331 2309 -270 181 -114 ATOM 1526 O VAL A 187 9.657 8.244 173.758 1.00 32.57 O ANISOU 1526 O VAL A 187 5529 4419 2428 -299 187 -98 ATOM 1527 CB VAL A 187 10.210 7.559 170.568 1.00 31.02 C ANISOU 1527 CB VAL A 187 5448 4180 2158 -315 207 -206 ATOM 1528 CG1 VAL A 187 10.751 6.437 171.445 1.00 30.80 C ANISOU 1528 CG1 VAL A 187 5522 4048 2132 -293 260 -204 ATOM 1529 CG2 VAL A 187 9.413 6.995 169.400 1.00 31.33 C ANISOU 1529 CG2 VAL A 187 5543 4216 2143 -404 181 -264 ATOM 1530 N LEU A 188 11.019 9.694 172.712 1.00 31.84 N ANISOU 1530 N LEU A 188 5353 4384 2362 -191 193 -91 ATOM 1531 CA LEU A 188 11.730 10.056 173.937 1.00 20.87 C ANISOU 1531 CA LEU A 188 3927 2996 1006 -137 206 -49 ATOM 1532 C LEU A 188 10.836 10.787 174.951 1.00 20.43 C ANISOU 1532 C LEU A 188 3801 2992 971 -163 172 -22 ATOM 1533 O LEU A 188 10.792 10.385 176.111 1.00 20.41 O ANISOU 1533 O LEU A 188 3810 2971 974 -164 180 0 ATOM 1534 CB LEU A 188 12.973 10.898 173.618 1.00 24.60 C ANISOU 1534 CB LEU A 188 4355 3496 1494 -70 223 -34 ATOM 1535 CG LEU A 188 13.722 11.482 174.821 1.00 25.00 C ANISOU 1535 CG LEU A 188 4358 3570 1571 -28 223 5 ATOM 1536 CD1 LEU A 188 14.239 10.373 175.723 1.00 24.78 C ANISOU 1536 CD1 LEU A 188 4391 3492 1532 4 248 25 ATOM 1537 CD2 LEU A 188 14.863 12.384 174.371 1.00 23.99 C ANISOU 1537 CD2 LEU A 188 4188 3477 1448 13 238 18 ATOM 1538 N PRO A 189 10.119 11.854 174.532 1.00 28.63 N ANISOU 1538 N PRO A 189 4772 4094 2013 -176 142 -20 ATOM 1539 CA PRO A 189 9.259 12.511 175.526 1.00 28.19 C ANISOU 1539 CA PRO A 189 4662 4081 1969 -189 125 4 ATOM 1540 C PRO A 189 8.146 11.611 176.053 1.00 28.83 C ANISOU 1540 C PRO A 189 4770 4158 2028 -258 120 3 ATOM 1541 O PRO A 189 7.815 11.678 177.237 1.00 20.26 O ANISOU 1541 O PRO A 189 3665 3083 949 -261 129 25 ATOM 1542 CB PRO A 189 8.659 13.691 174.753 1.00 19.88 C ANISOU 1542 CB PRO A 189 3557 3087 910 -182 100 10 ATOM 1543 CG PRO A 189 9.586 13.926 173.631 1.00 19.88 C ANISOU 1543 CG PRO A 189 3569 3076 908 -152 108 0 ATOM 1544 CD PRO A 189 10.094 12.576 173.247 1.00 28.55 C ANISOU 1544 CD PRO A 189 4737 4119 1991 -169 128 -29 ATOM 1545 N LEU A 190 7.577 10.788 175.177 1.00 29.47 N ANISOU 1545 N LEU A 190 4896 4226 2073 -323 109 -24 ATOM 1546 CA LEU A 190 6.480 9.904 175.553 1.00 30.00 C ANISOU 1546 CA LEU A 190 4989 4296 2115 -416 103 -27 ATOM 1547 C LEU A 190 6.927 8.913 176.612 1.00 31.88 C ANISOU 1547 C LEU A 190 5283 4456 2374 -413 140 -13 ATOM 1548 O LEU A 190 6.219 8.667 177.586 1.00 36.33 O ANISOU 1548 O LEU A 190 5822 5032 2950 -450 146 12 ATOM 1549 CB LEU A 190 5.943 9.157 174.332 1.00 31.50 C ANISOU 1549 CB LEU A 190 5225 4478 2264 -497 80 -69 ATOM 1550 CG LEU A 190 4.618 8.415 174.507 1.00 33.16 C ANISOU 1550 CG LEU A 190 5420 4710 2468 -612 60 -73 ATOM 1551 CD1 LEU A 190 3.485 9.405 174.713 1.00 33.56 C ANISOU 1551 CD1 LEU A 190 5344 4883 2525 -623 25 -38 ATOM 1552 CD2 LEU A 190 4.336 7.514 173.313 1.00 34.04 C ANISOU 1552 CD2 LEU A 190 5608 4794 2533 -703 38 -128 ATOM 1553 N LEU A 191 8.112 8.348 176.417 1.00 30.46 N ANISOU 1553 N LEU A 191 5176 4200 2197 -362 168 -23 ATOM 1554 CA LEU A 191 8.658 7.383 177.359 1.00 30.04 C ANISOU 1554 CA LEU A 191 5182 4069 2163 -340 203 1 ATOM 1555 C LEU A 191 8.973 8.047 178.697 1.00 29.03 C ANISOU 1555 C LEU A 191 4996 3982 2053 -288 204 49 ATOM 1556 O LEU A 191 8.638 7.514 179.756 1.00 29.16 O ANISOU 1556 O LEU A 191 5025 3981 2075 -308 217 81 ATOM 1557 CB LEU A 191 9.908 6.723 176.777 1.00 30.05 C ANISOU 1557 CB LEU A 191 5263 3990 2166 -276 236 -14 ATOM 1558 CG LEU A 191 10.701 5.822 177.720 1.00 30.75 C ANISOU 1558 CG LEU A 191 5405 4001 2276 -219 273 26 ATOM 1559 CD1 LEU A 191 9.910 4.565 178.027 1.00 31.34 C ANISOU 1559 CD1 LEU A 191 5564 3993 2351 -296 292 26 ATOM 1560 CD2 LEU A 191 12.048 5.476 177.115 1.00 31.59 C ANISOU 1560 CD2 LEU A 191 5558 4057 2390 -125 309 19 ATOM 1561 N VAL A 192 9.612 9.213 178.640 1.00 28.20 N ANISOU 1561 N VAL A 192 4834 3929 1951 -228 191 52 ATOM 1562 CA VAL A 192 9.923 9.992 179.837 1.00 27.69 C ANISOU 1562 CA VAL A 192 4712 3908 1902 -187 186 83 ATOM 1563 C VAL A 192 8.670 10.258 180.665 1.00 28.18 C ANISOU 1563 C VAL A 192 4735 4014 1956 -236 183 96 ATOM 1564 O VAL A 192 8.677 10.112 181.886 1.00 29.61 O ANISOU 1564 O VAL A 192 4917 4200 2132 -229 194 126 ATOM 1565 CB VAL A 192 10.578 11.340 179.484 1.00 0.00 C ATOM 1566 CG1 VAL A 192 10.212 12.369 180.556 1.00 0.00 C ATOM 1567 CG2 VAL A 192 12.107 11.238 179.395 1.00 0.00 C ATOM 1568 N MET A 193 7.589 10.631 179.990 1.00 28.83 N ANISOU 1568 N MET A 193 4785 4138 2030 -283 170 78 ATOM 1569 CA MET A 193 6.350 10.974 180.673 1.00 30.47 C ANISOU 1569 CA MET A 193 4938 4404 2234 -321 174 93 ATOM 1570 C MET A 193 5.698 9.753 181.315 1.00 34.86 C ANISOU 1570 C MET A 193 5525 4932 2787 -388 195 112 ATOM 1571 O MET A 193 5.097 9.852 182.385 1.00 39.96 O ANISOU 1571 O MET A 193 6142 5613 3428 -401 216 139 ATOM 1572 CB MET A 193 5.375 11.637 179.703 1.00 31.19 C ANISOU 1572 CB MET A 193 4968 4557 2324 -345 150 78 ATOM 1573 CG MET A 193 4.597 12.788 180.312 1.00 32.00 C ANISOU 1573 CG MET A 193 4994 4734 2433 -317 159 95 ATOM 1574 SD MET A 193 3.334 13.427 179.200 1.00111.59 S ANISOU 1574 SD MET A 193 14989 14898 12512 -336 128 97 ATOM 1575 CE MET A 193 2.392 11.939 178.870 1.00 57.76 C ANISOU 1575 CE MET A 193 8172 8089 5685 -457 113 94 ATOM 1576 N ILE A 194 5.816 8.604 180.659 1.00 33.51 N ANISOU 1576 N ILE A 194 5423 4694 2617 -433 195 99 ATOM 1577 CA ILE A 194 5.265 7.364 181.197 1.00 32.33 C ANISOU 1577 CA ILE A 194 5322 4494 2467 -507 219 118 ATOM 1578 C ILE A 194 5.997 6.958 182.474 1.00 32.47 C ANISOU 1578 C ILE A 194 5385 4468 2482 -458 248 163 ATOM 1579 O ILE A 194 5.369 6.568 183.462 1.00 31.70 O ANISOU 1579 O ILE A 194 5287 4380 2378 -499 273 200 ATOM 1580 CB ILE A 194 5.339 6.224 180.165 1.00 0.00 C ATOM 1581 CG1 ILE A 194 4.029 6.114 179.358 1.00 0.00 C ATOM 1582 CG2 ILE A 194 5.695 4.888 180.841 1.00 0.00 C ATOM 1583 CD1 ILE A 194 3.931 5.025 178.277 1.00 0.00 C ATOM 1584 N ILE A 195 7.323 7.059 182.447 1.00 33.37 N ANISOU 1584 N ILE A 195 5533 4547 2600 -371 245 166 ATOM 1585 CA ILE A 195 8.142 6.792 183.625 1.00 34.02 C ANISOU 1585 CA ILE A 195 5645 4608 2672 -312 259 215 ATOM 1586 C ILE A 195 7.689 7.660 184.791 1.00 32.26 C ANISOU 1586 C ILE A 195 5361 4471 2427 -310 260 237 ATOM 1587 O ILE A 195 7.477 7.170 185.901 1.00 34.78 O ANISOU 1587 O ILE A 195 5704 4786 2724 -323 282 282 ATOM 1588 CB ILE A 195 9.636 7.056 183.351 1.00 21.90 C ANISOU 1588 CB ILE A 195 4117 3059 1144 -216 246 215 ATOM 1589 CG1 ILE A 195 10.142 6.155 182.226 1.00 22.25 C ANISOU 1589 CG1 ILE A 195 4232 3016 1208 -204 261 192 ATOM 1590 CG2 ILE A 195 10.457 6.843 184.608 1.00 22.12 C ANISOU 1590 CG2 ILE A 195 4159 3090 1156 -157 248 273 ATOM 1591 CD1 ILE A 195 11.571 6.436 181.820 1.00 22.03 C ANISOU 1591 CD1 ILE A 195 4195 2987 1189 -108 258 192 ATOM 1592 N CYS A 196 7.527 8.951 184.520 1.00 28.15 N ANISOU 1592 N CYS A 196 4770 4021 1906 -292 241 205 ATOM 1593 CA CYS A 196 7.129 9.911 185.541 1.00 27.32 C ANISOU 1593 CA CYS A 196 4601 3987 1794 -274 247 211 ATOM 1594 C CYS A 196 5.727 9.631 186.073 1.00 30.35 C ANISOU 1594 C CYS A 196 4975 4407 2152 -345 282 230 ATOM 1595 O CYS A 196 5.509 9.658 187.282 1.00 33.21 O ANISOU 1595 O CYS A 196 5329 4796 2494 -339 306 258 ATOM 1596 CB CYS A 196 7.212 11.333 184.989 1.00 20.76 C ANISOU 1596 CB CYS A 196 3702 3201 985 -234 226 171 ATOM 1597 SG CYS A 196 8.895 11.854 184.586 1.00 39.33 S ANISOU 1597 SG CYS A 196 6048 5532 3362 -165 193 156 ATOM 1598 N TYR A 197 4.782 9.362 185.177 1.00 31.78 N ANISOU 1598 N TYR A 197 5126 4593 2355 -406 280 214 ATOM 1599 CA TYR A 197 3.417 9.053 185.593 1.00 35.45 C ANISOU 1599 CA TYR A 197 5548 5104 2817 -479 311 235 ATOM 1600 C TYR A 197 3.368 7.797 186.454 1.00 34.28 C ANISOU 1600 C TYR A 197 5467 4903 2654 -529 344 281 ATOM 1601 O TYR A 197 2.631 7.740 187.439 1.00 34.52 O ANISOU 1601 O TYR A 197 5474 4979 2664 -559 384 315 ATOM 1602 CB TYR A 197 2.500 8.887 184.381 1.00 40.32 C ANISOU 1602 CB TYR A 197 6117 5745 3459 -548 289 211 ATOM 1603 CG TYR A 197 1.794 10.159 183.975 1.00 43.15 C ANISOU 1603 CG TYR A 197 6372 6197 3824 -516 278 196 ATOM 1604 CD1 TYR A 197 0.831 10.732 184.796 1.00 44.78 C ANISOU 1604 CD1 TYR A 197 6502 6486 4025 -511 316 218 ATOM 1605 CD2 TYR A 197 2.083 10.782 182.768 1.00 44.19 C ANISOU 1605 CD2 TYR A 197 6488 6335 3968 -484 236 164 ATOM 1606 CE1 TYR A 197 0.181 11.896 184.429 1.00 46.94 C ANISOU 1606 CE1 TYR A 197 6685 6840 4311 -464 313 211 ATOM 1607 CE2 TYR A 197 1.437 11.946 182.391 1.00 45.65 C ANISOU 1607 CE2 TYR A 197 6584 6599 4160 -444 227 161 ATOM 1608 CZ TYR A 197 0.488 12.499 183.225 1.00 48.32 C ANISOU 1608 CZ TYR A 197 6849 7013 4500 -430 266 185 ATOM 1609 OH TYR A 197 -0.155 13.657 182.851 1.00 50.82 O ANISOU 1609 OH TYR A 197 7080 7400 4827 -373 264 189 ATOM 1610 N THR A 198 4.156 6.794 186.078 1.00 33.50 N ANISOU 1610 N THR A 198 5457 4705 2565 -532 334 286 ATOM 1611 CA THR A 198 4.226 5.555 186.842 1.00 33.45 C ANISOU 1611 CA THR A 198 5534 4627 2547 -567 367 339 ATOM 1612 C THR A 198 4.794 5.815 188.233 1.00 34.13 C ANISOU 1612 C THR A 198 5636 4740 2592 -502 383 386 ATOM 1613 O THR A 198 4.188 5.438 189.236 1.00 35.47 O ANISOU 1613 O THR A 198 5815 4927 2733 -542 422 433 ATOM 1614 CB THR A 198 5.078 4.505 186.104 1.00 0.00 C ATOM 1615 OG1 THR A 198 6.396 5.028 185.909 1.00 0.00 O ATOM 1616 CG2 THR A 198 4.501 4.100 184.742 1.00 0.00 C ATOM 1617 N GLY A 199 5.950 6.472 188.282 1.00 32.30 N ANISOU 1617 N GLY A 199 5405 4518 2351 -409 351 374 ATOM 1618 CA GLY A 199 6.617 6.782 189.536 1.00 23.74 C ANISOU 1618 CA GLY A 199 4315 3468 1235 -344 346 408 ATOM 1619 C GLY A 199 5.656 7.813 190.367 1.00 34.84 C ANISOU 1619 C GLY A 199 5650 4965 2622 -351 368 403 ATOM 1620 O GLY A 199 5.637 7.758 191.603 1.00 34.43 O ANISOU 1620 O GLY A 199 5604 4938 2537 -329 380 441 ATOM 1621 N ILE A 200 4.857 8.726 189.723 1.00 31.02 N ATOM 1622 CA ILE A 200 3.928 9.796 190.234 1.00 32.28 C ATOM 1623 C ILE A 200 2.651 9.326 190.800 1.00 31.44 C ATOM 1624 O ILE A 200 2.179 9.891 191.784 1.00 32.07 O ATOM 1625 CB ILE A 200 3.479 10.795 189.106 1.00 0.00 C ATOM 1626 CG1 ILE A 200 4.389 11.982 189.273 1.00 0.00 C ATOM 1627 CG2 ILE A 200 2.011 11.312 188.864 1.00 0.00 C ATOM 1628 CD1 ILE A 200 4.543 12.874 188.042 1.00 0.00 C ATOM 1629 N ILE A 201 2.095 8.322 190.119 1.00 31.02 N ATOM 1630 CA ILE A 201 0.894 7.630 190.467 1.00 30.54 C ATOM 1631 C ILE A 201 1.045 7.326 191.935 1.00 30.29 C ATOM 1632 O ILE A 201 0.451 7.999 192.752 1.00 30.82 O ATOM 1633 CB ILE A 201 0.746 6.387 189.570 1.00 0.00 C ATOM 1634 CG1 ILE A 201 -0.037 6.716 188.282 1.00 0.00 C ATOM 1635 CG2 ILE A 201 0.095 5.224 190.340 1.00 0.00 C ATOM 1636 CD1 ILE A 201 -0.277 5.585 187.270 1.00 0.00 C ATOM 1637 N LYS A 202 2.110 6.617 192.314 1.00 27.98 N ATOM 1638 CA LYS A 202 2.256 6.218 193.684 1.00 27.56 C ATOM 1639 C LYS A 202 2.959 7.216 194.650 1.00 27.51 C ATOM 1640 O LYS A 202 2.698 7.037 195.843 1.00 28.08 O ATOM 1641 CB LYS A 202 2.859 4.804 193.646 1.00 0.00 C ATOM 1642 CG LYS A 202 4.336 4.680 193.996 1.00 0.00 C ATOM 1643 CD LYS A 202 4.761 3.218 193.903 1.00 0.00 C ATOM 1644 CE LYS A 202 6.180 3.033 194.424 1.00 0.00 C ATOM 1645 NZ LYS A 202 6.590 1.620 194.370 1.00 0.00 N1+ ATOM 1646 N ILE A 203 3.811 8.221 194.270 1.00 60.51 N ANISOU 1646 N ILE A 203 7810 9147 6034 667 -1092 -2145 ATOM 1647 CA ILE A 203 4.333 9.179 195.300 1.00 59.44 C ANISOU 1647 CA ILE A 203 7541 9261 5781 690 -1039 -2225 ATOM 1648 C ILE A 203 3.172 10.074 195.749 1.00 63.86 C ANISOU 1648 C ILE A 203 8110 9844 6311 529 -1056 -2234 ATOM 1649 O ILE A 203 2.834 10.079 196.933 1.00 66.91 O ANISOU 1649 O ILE A 203 8501 10298 6626 559 -1084 -2387 ATOM 1650 CB ILE A 203 5.619 9.981 195.026 1.00 0.00 C ATOM 1651 CG1 ILE A 203 6.376 10.288 196.334 1.00 0.00 C ATOM 1652 CG2 ILE A 203 5.311 11.268 194.240 1.00 0.00 C ATOM 1653 CD1 ILE A 203 6.856 9.105 197.190 1.00 0.00 C ATOM 1654 N LEU A 204 2.566 10.817 194.813 1.00 57.81 N ANISOU 1654 N LEU A 204 7335 9039 5591 366 -1044 -2090 ATOM 1655 CA LEU A 204 1.448 11.711 195.079 1.00 58.28 C ANISOU 1655 CA LEU A 204 7374 9140 5629 211 -1065 -2102 ATOM 1656 C LEU A 204 0.297 10.949 195.756 1.00 64.66 C ANISOU 1656 C LEU A 204 8310 9789 6470 165 -1149 -2276 ATOM 1657 O LEU A 204 -0.251 11.424 196.761 1.00 65.25 O ANISOU 1657 O LEU A 204 8344 9975 6472 132 -1178 -2394 ATOM 1658 CB LEU A 204 0.989 12.367 193.764 1.00 57.34 C ANISOU 1658 CB LEU A 204 7233 8974 5580 57 -1041 -1938 ATOM 1659 CG LEU A 204 1.356 13.851 193.513 1.00 61.33 C ANISOU 1659 CG LEU A 204 7589 9690 6024 21 -985 -1816 ATOM 1660 CD1 LEU A 204 2.800 14.137 193.781 1.00 60.53 C ANISOU 1660 CD1 LEU A 204 7413 9734 5852 150 -918 -1755 ATOM 1661 CD2 LEU A 204 1.076 14.246 192.062 1.00 63.51 C ANISOU 1661 CD2 LEU A 204 7850 9899 6383 -103 -960 -1673 ATOM 1662 N LEU A 205 0.004 9.731 195.266 1.00 61.98 N ANISOU 1662 N LEU A 205 8135 9187 6229 177 -1193 -2301 ATOM 1663 CA LEU A 205 -1.073 8.910 195.810 1.00 63.81 C ANISOU 1663 CA LEU A 205 8526 9213 6505 123 -1271 -2460 ATOM 1664 C LEU A 205 -1.000 8.600 197.384 1.00 70.25 C ANISOU 1664 C LEU A 205 9363 10070 7257 297 -1313 -2665 ATOM 1665 O LEU A 205 -1.892 7.931 197.898 1.00 72.21 O ANISOU 1665 O LEU A 205 9660 10287 7491 233 -1365 -2827 ATOM 1666 CB LEU A 205 -1.494 7.804 194.829 1.00 64.29 C ANISOU 1666 CB LEU A 205 8797 8949 6680 80 -1306 -2403 ATOM 1667 CG LEU A 205 -2.286 8.265 193.593 1.00 67.42 C ANISOU 1667 CG LEU A 205 9216 9263 7139 -152 -1270 -2247 ATOM 1668 CD1 LEU A 205 -2.417 7.149 192.586 1.00 67.32 C ANISOU 1668 CD1 LEU A 205 9423 8952 7205 -158 -1294 -2158 ATOM 1669 CD2 LEU A 205 -3.666 8.788 193.976 1.00 71.43 C ANISOU 1669 CD2 LEU A 205 9712 9773 7655 -382 -1282 -2339 ATOM 1670 N ARG A 206 -0.098 9.211 198.205 1.00 39.20 N ATOM 1671 CA ARG A 206 -0.401 9.771 199.550 1.00 38.03 C ATOM 1672 C ARG A 206 -0.277 11.314 199.406 1.00 38.61 C ATOM 1673 O ARG A 206 0.843 11.819 199.504 1.00 38.19 O ATOM 1674 CB ARG A 206 0.588 9.211 200.664 1.00 0.00 C ATOM 1675 CG ARG A 206 1.933 9.956 200.992 1.00 0.00 C ATOM 1676 CD ARG A 206 2.899 9.427 202.059 1.00 0.00 C ATOM 1677 NE ARG A 206 4.033 10.384 202.220 1.00 0.00 N ATOM 1678 CZ ARG A 206 5.151 10.409 201.474 1.00 0.00 C ATOM 1679 NH1 ARG A 206 5.309 9.566 200.455 1.00 0.00 N ATOM 1680 NH2 ARG A 206 6.116 11.293 201.747 1.00 0.00 N1+ ATOM 1681 N ARG A 207 -1.307 12.104 198.989 1.00 39.83 N ATOM 1682 CA ARG A 207 -0.972 13.497 198.550 1.00 39.77 C ATOM 1683 C ARG A 207 -0.496 14.248 199.779 1.00 40.23 C ATOM 1684 O ARG A 207 0.461 15.013 199.738 1.00 39.92 O ATOM 1685 CB ARG A 207 -2.132 14.259 197.882 1.00 0.00 C ATOM 1686 CG ARG A 207 -2.086 14.540 196.364 1.00 0.00 C ATOM 1687 CD ARG A 207 -3.245 15.298 195.716 1.00 0.00 C ATOM 1688 NE ARG A 207 -3.052 15.484 194.274 1.00 0.00 N ATOM 1689 CZ ARG A 207 -2.404 16.523 193.717 1.00 0.00 C ATOM 1690 NH1 ARG A 207 -1.926 17.523 194.490 1.00 0.00 N ATOM 1691 NH2 ARG A 207 -2.256 16.543 192.377 1.00 0.00 N1+ ATOM 1692 N PRO A 208 -1.170 13.862 200.869 1.00 40.52 N ATOM 1693 CA PRO A 208 -1.300 14.510 202.117 1.00 40.12 C ATOM 1694 C PRO A 208 -1.949 15.875 201.740 1.00 40.07 C ATOM 1695 O PRO A 208 -2.803 16.000 200.870 1.00 39.51 O ATOM 1696 CD PRO A 208 -0.106 13.036 201.644 1.00 0.00 C ATOM 1697 CB PRO A 208 0.087 14.645 202.772 1.00 0.00 C ATOM 1698 CG PRO A 208 1.073 13.806 202.248 1.00 0.00 C ATOM 1699 N ASN A 209 -1.225 16.812 202.262 1.00 39.24 N ATOM 1700 CA ASN A 209 -0.628 18.006 201.869 1.00 39.28 C ATOM 1701 C ASN A 209 -0.450 18.526 200.339 1.00 39.02 C ATOM 1702 O ASN A 209 0.374 17.941 199.675 1.00 37.21 O ATOM 1703 CB ASN A 209 0.579 17.919 203.000 1.00 0.00 C ATOM 1704 CG ASN A 209 1.683 18.832 203.704 1.00 0.00 C ATOM 1705 OD1 ASN A 209 2.829 18.901 203.282 1.00 0.00 O ATOM 1706 ND2 ASN A 209 1.551 19.134 204.996 1.00 0.00 N ATOM 1707 N GLU A 210 -0.986 19.778 199.918 1.00 55.49 N ANISOU 1707 N GLU A 210 7667 8793 4623 -485 -522 -1212 ATOM 1708 CA GLU A 210 -0.698 21.275 200.328 1.00 56.55 C ANISOU 1708 CA GLU A 210 7751 9109 4626 -579 -516 -1172 ATOM 1709 C GLU A 210 0.733 21.614 199.902 1.00 63.49 C ANISOU 1709 C GLU A 210 8505 10146 5473 -571 -437 -1087 ATOM 1710 O GLU A 210 1.087 22.802 199.905 1.00 64.33 O ANISOU 1710 O GLU A 210 8584 10322 5537 -685 -465 -972 ATOM 1711 CB GLU A 210 -0.705 20.932 201.828 1.00 59.85 C ANISOU 1711 CB GLU A 210 8249 9617 4875 -563 -496 -1322 ATOM 1712 CG GLU A 210 -2.082 20.722 202.438 1.00 70.96 C ANISOU 1712 CG GLU A 210 9802 10881 6277 -611 -582 -1416 ATOM 1713 CD GLU A 210 -2.111 20.273 203.890 1.00 98.94 C ANISOU 1713 CD GLU A 210 13442 14500 9651 -581 -562 -1590 ATOM 1714 OE1 GLU A 210 -1.025 20.100 204.491 1.00104.64 O ANISOU 1714 OE1 GLU A 210 14100 15415 10243 -513 -471 -1648 ATOM 1715 OE2 GLU A 210 -3.227 20.112 204.435 1.00 94.50 O1- ANISOU 1715 OE2 GLU A 210 13015 13821 9071 -642 -636 -1675 ATOM 1716 N LYS A 211 1.543 20.632 199.494 1.00 60.39 N ANISOU 1716 N LYS A 211 8047 9814 5086 -440 -347 -1147 ATOM 1717 CA LYS A 211 2.896 20.800 198.979 1.00 59.02 C ANISOU 1717 CA LYS A 211 7740 9825 4859 -450 -262 -1092 ATOM 1718 C LYS A 211 2.908 21.459 197.585 1.00 63.76 C ANISOU 1718 C LYS A 211 8289 10346 5590 -515 -291 -934 ATOM 1719 O LYS A 211 1.867 21.713 196.977 1.00 64.52 O ANISOU 1719 O LYS A 211 8388 10294 5834 -445 -318 -915 ATOM 1720 CB LYS A 211 3.555 19.398 198.913 1.00 61.09 C ANISOU 1720 CB LYS A 211 7928 10192 5093 -267 -175 -1220 ATOM 1721 CG LYS A 211 3.731 18.732 200.286 1.00 73.84 C ANISOU 1721 CG LYS A 211 9551 11977 6527 -201 -120 -1388 ATOM 1722 CD LYS A 211 4.405 17.351 200.231 1.00 83.25 C ANISOU 1722 CD LYS A 211 10657 13291 7682 30 -46 -1539 ATOM 1723 CE LYS A 211 3.486 16.241 199.699 1.00 95.31 C ANISOU 1723 CE LYS A 211 12194 15001 9021 108 5 -1728 ATOM 1724 NZ LYS A 211 4.163 14.934 199.699 1.00 0.00 N1+ ATOM 1725 N LYS A 212 4.115 21.554 197.020 1.00 31.02 N ATOM 1726 CA LYS A 212 4.402 21.746 195.595 1.00 32.28 C ATOM 1727 C LYS A 212 3.839 20.638 194.663 1.00 31.44 C ATOM 1728 O LYS A 212 4.171 20.626 193.480 1.00 32.07 O ATOM 1729 CB LYS A 212 5.931 21.923 195.438 1.00 0.00 C ATOM 1730 CG LYS A 212 6.776 20.734 195.949 1.00 0.00 C ATOM 1731 CD LYS A 212 8.289 20.981 195.840 1.00 0.00 C ATOM 1732 CE LYS A 212 9.105 19.878 196.529 1.00 0.00 C ATOM 1733 NZ LYS A 212 10.552 20.082 196.355 1.00 0.00 N1+ ATOM 1734 N SER A 213 2.970 19.751 195.171 1.00 31.02 N ATOM 1735 CA SER A 213 2.267 18.716 194.418 1.00 30.54 C ATOM 1736 C SER A 213 1.276 19.330 193.410 1.00 30.29 C ATOM 1737 O SER A 213 0.944 18.717 192.398 1.00 30.82 O ATOM 1738 CB SER A 213 1.534 17.805 195.438 1.00 0.00 C ATOM 1739 OG SER A 213 0.651 18.545 196.278 1.00 0.00 O ATOM 1740 N LYS A 214 0.872 20.587 193.638 1.00 27.98 N ATOM 1741 CA LYS A 214 0.131 21.412 192.686 1.00 27.56 C ATOM 1742 C LYS A 214 0.938 21.804 191.424 1.00 27.51 C ATOM 1743 O LYS A 214 0.325 22.185 190.429 1.00 28.08 O ATOM 1744 CB LYS A 214 -0.421 22.644 193.432 1.00 0.00 C ATOM 1745 CG LYS A 214 0.642 23.597 194.015 1.00 0.00 C ATOM 1746 CD LYS A 214 0.002 24.760 194.784 1.00 0.00 C ATOM 1747 CE LYS A 214 1.029 25.782 195.291 1.00 0.00 C ATOM 1748 NZ LYS A 214 0.362 26.957 195.872 1.00 0.00 N1+ ATOM 1749 N ALA A 215 2.280 21.718 191.468 1.00 31.02 N ATOM 1750 CA ALA A 215 3.144 22.035 190.326 1.00 30.54 C ATOM 1751 C ALA A 215 3.184 20.904 189.285 1.00 30.29 C ATOM 1752 O ALA A 215 3.428 21.173 188.105 1.00 30.82 O ATOM 1753 CB ALA A 215 4.564 22.350 190.814 1.00 0.00 C ATOM 1754 N VAL A 216 2.917 19.665 189.723 1.00 27.98 N ATOM 1755 CA VAL A 216 2.778 18.480 188.877 1.00 27.56 C ATOM 1756 C VAL A 216 1.385 18.525 188.217 1.00 27.51 C ATOM 1757 O VAL A 216 0.435 17.866 188.632 1.00 28.08 O ATOM 1758 CB VAL A 216 3.030 17.183 189.696 1.00 0.00 C ATOM 1759 CG1 VAL A 216 2.765 15.856 188.955 1.00 0.00 C ATOM 1760 CG2 VAL A 216 4.483 17.184 190.206 1.00 0.00 C ATOM 1761 N ARG A 217 1.298 19.441 187.254 1.00 28.55 N ANISOU 1761 N ARG A 217 4664 4203 1980 223 129 -165 ATOM 1762 CA ARG A 217 0.090 19.898 186.595 1.00 30.69 C ANISOU 1762 CA ARG A 217 4876 4542 2243 195 168 -181 ATOM 1763 C ARG A 217 0.554 20.687 185.370 1.00 31.35 C ANISOU 1763 C ARG A 217 4933 4618 2359 193 138 -199 ATOM 1764 O ARG A 217 0.264 20.287 184.246 1.00 35.17 O ANISOU 1764 O ARG A 217 5357 5155 2851 144 156 -218 ATOM 1765 CB ARG A 217 -0.756 20.753 187.575 1.00 33.69 C ANISOU 1765 CB ARG A 217 5285 4945 2571 235 202 -169 ATOM 1766 CG ARG A 217 -2.091 21.288 187.017 1.00 36.10 C ANISOU 1766 CG ARG A 217 5565 5326 2824 184 265 -162 ATOM 1767 CD ARG A 217 -2.837 22.189 188.019 1.00 39.71 C ANISOU 1767 CD ARG A 217 6044 5824 3220 223 306 -155 ATOM 1768 NE ARG A 217 -2.238 23.530 188.125 1.00 43.43 N ANISOU 1768 NE ARG A 217 6510 6366 3624 167 368 -139 ATOM 1769 CZ ARG A 217 -2.128 24.292 189.227 1.00 45.03 C ANISOU 1769 CZ ARG A 217 6776 6554 3780 205 379 -111 ATOM 1770 NH1 ARG A 217 -2.515 23.872 190.434 1.00 45.05 N ANISOU 1770 NH1 ARG A 217 6855 6466 3796 295 328 -104 ATOM 1771 NH2 ARG A 217 -1.618 25.520 189.131 1.00 47.29 N1+ ANISOU 1771 NH2 ARG A 217 7052 6921 3993 142 442 -89 ATOM 1772 N LEU A 218 1.309 21.769 185.624 1.00 28.74 N ANISOU 1772 N LEU A 218 4657 4227 2037 236 93 -192 ATOM 1773 CA LEU A 218 1.763 22.727 184.620 1.00 26.75 C ANISOU 1773 CA LEU A 218 4395 3968 1801 230 66 -201 ATOM 1774 C LEU A 218 2.610 22.083 183.528 1.00 27.44 C ANISOU 1774 C LEU A 218 4418 4091 1918 163 56 -219 ATOM 1775 O LEU A 218 2.200 22.106 182.374 1.00 27.94 O ANISOU 1775 O LEU A 218 4431 4198 1985 126 67 -232 ATOM 1776 CB LEU A 218 2.552 23.885 185.261 1.00 0.00 C ATOM 1777 CG LEU A 218 1.687 24.856 186.078 1.00 0.00 C ATOM 1778 CD1 LEU A 218 1.414 24.346 187.510 1.00 0.00 C ATOM 1779 CD2 LEU A 218 2.316 26.252 186.067 1.00 0.00 C ATOM 1780 N ILE A 219 3.765 21.520 183.903 1.00 28.14 N ANISOU 1780 N ILE A 219 4510 4164 2017 151 36 -222 ATOM 1781 CA ILE A 219 4.708 20.993 182.918 1.00 29.12 C ANISOU 1781 CA ILE A 219 4578 4327 2158 102 25 -246 ATOM 1782 C ILE A 219 4.178 19.761 182.163 1.00 30.41 C ANISOU 1782 C ILE A 219 4684 4538 2333 63 67 -272 ATOM 1783 O ILE A 219 4.463 19.600 180.978 1.00 30.65 O ANISOU 1783 O ILE A 219 4662 4613 2370 15 73 -302 ATOM 1784 CB ILE A 219 6.110 20.738 183.518 1.00 18.98 C ANISOU 1784 CB ILE A 219 3318 3024 867 110 -13 -245 ATOM 1785 CG1 ILE A 219 7.166 20.532 182.412 1.00 27.44 C ANISOU 1785 CG1 ILE A 219 4329 4156 1941 58 -24 -276 ATOM 1786 CG2 ILE A 219 6.145 19.592 184.548 1.00 19.12 C ANISOU 1786 CG2 ILE A 219 3372 3012 881 143 1 -233 ATOM 1787 CD1 ILE A 219 7.387 21.762 181.517 1.00 18.81 C ANISOU 1787 CD1 ILE A 219 3200 3110 837 18 -32 -285 ATOM 1788 N PHE A 220 3.315 18.990 182.830 1.00 32.01 N ANISOU 1788 N PHE A 220 4898 4738 2526 74 99 -266 ATOM 1789 CA PHE A 220 2.556 17.929 182.190 1.00 33.76 C ANISOU 1789 CA PHE A 220 5068 5013 2745 29 139 -299 ATOM 1790 C PHE A 220 1.587 18.498 181.139 1.00 32.10 C ANISOU 1790 C PHE A 220 4809 4841 2547 -16 158 -309 ATOM 1791 O PHE A 220 1.639 18.035 180.006 1.00 35.17 O ANISOU 1791 O PHE A 220 5147 5252 2965 -65 173 -340 ATOM 1792 CB PHE A 220 1.910 17.006 183.240 1.00 39.81 C ANISOU 1792 CB PHE A 220 5860 5779 3486 43 170 -286 ATOM 1793 CG PHE A 220 2.935 16.157 183.982 1.00 46.67 C ANISOU 1793 CG PHE A 220 6787 6587 4357 76 158 -279 ATOM 1794 CD1 PHE A 220 3.630 16.677 185.096 1.00 50.17 C ANISOU 1794 CD1 PHE A 220 7232 7007 4822 85 128 -300 ATOM 1795 CD2 PHE A 220 3.355 14.924 183.435 1.00 51.63 C ANISOU 1795 CD2 PHE A 220 7476 7188 4954 95 181 -248 ATOM 1796 CE1 PHE A 220 4.677 15.960 185.661 1.00 50.88 C ANISOU 1796 CE1 PHE A 220 7386 7042 4903 123 114 -294 ATOM 1797 CE2 PHE A 220 4.388 14.210 184.030 1.00 51.19 C ANISOU 1797 CE2 PHE A 220 7499 7061 4890 128 167 -233 ATOM 1798 CZ PHE A 220 5.048 14.729 185.136 1.00 50.30 C ANISOU 1798 CZ PHE A 220 7389 6922 4800 149 131 -257 ATOM 1799 N VAL A 221 0.828 19.565 181.455 1.00 29.00 N ANISOU 1799 N VAL A 221 4449 4446 2125 4 157 -284 ATOM 1800 CA VAL A 221 -0.036 20.231 180.488 1.00 28.21 C ANISOU 1800 CA VAL A 221 4343 4356 2020 -23 169 -285 ATOM 1801 C VAL A 221 0.791 20.809 179.344 1.00 27.78 C ANISOU 1801 C VAL A 221 4275 4294 1987 -44 143 -290 ATOM 1802 O VAL A 221 0.427 20.672 178.176 1.00 27.13 O ANISOU 1802 O VAL A 221 4203 4193 1913 -92 158 -300 ATOM 1803 CB VAL A 221 -0.861 21.352 181.146 1.00 0.00 C ATOM 1804 CG1 VAL A 221 -0.932 22.546 180.191 1.00 0.00 C ATOM 1805 CG2 VAL A 221 -2.289 20.901 181.483 1.00 0.00 C ATOM 1806 N ILE A 222 1.947 21.423 179.659 1.00 27.36 N ANISOU 1806 N ILE A 222 4230 4233 1931 -13 107 -282 ATOM 1807 CA ILE A 222 2.838 22.028 178.666 1.00 25.34 C ANISOU 1807 CA ILE A 222 3950 3989 1688 -44 86 -286 ATOM 1808 C ILE A 222 3.325 20.963 177.667 1.00 27.83 C ANISOU 1808 C ILE A 222 4228 4302 2043 -115 109 -317 ATOM 1809 O ILE A 222 3.374 21.223 176.464 1.00 28.55 O ANISOU 1809 O ILE A 222 4359 4354 2134 -169 119 -315 ATOM 1810 CB ILE A 222 4.046 22.768 179.331 1.00 22.04 C ANISOU 1810 CB ILE A 222 3552 3563 1258 -16 47 -278 ATOM 1811 CG1 ILE A 222 3.573 24.015 180.120 1.00 20.89 C ANISOU 1811 CG1 ILE A 222 3484 3369 1083 42 22 -248 ATOM 1812 CG2 ILE A 222 5.189 23.163 178.369 1.00 21.61 C ANISOU 1812 CG2 ILE A 222 3441 3551 1218 -58 34 -290 ATOM 1813 CD1 ILE A 222 4.536 24.526 181.207 1.00 19.30 C ANISOU 1813 CD1 ILE A 222 3300 3180 852 44 16 -233 ATOM 1814 N MET A 223 3.572 19.745 178.171 1.00 30.32 N ANISOU 1814 N MET A 223 4528 4615 2378 -111 122 -340 ATOM 1815 CA MET A 223 4.039 18.667 177.310 1.00 33.30 C ANISOU 1815 CA MET A 223 4922 4950 2779 -170 151 -376 ATOM 1816 C MET A 223 2.905 18.026 176.512 1.00 37.29 C ANISOU 1816 C MET A 223 5601 5286 3281 -158 191 -364 ATOM 1817 O MET A 223 3.080 17.689 175.341 1.00 39.59 O ANISOU 1817 O MET A 223 5972 5516 3555 20 176 -367 ATOM 1818 CB MET A 223 4.758 17.607 178.141 1.00 18.37 C ANISOU 1818 CB MET A 223 2994 3095 891 -121 146 -403 ATOM 1819 CG MET A 223 5.104 16.352 177.370 1.00 19.55 C ANISOU 1819 CG MET A 223 3154 3220 1054 -159 182 -456 ATOM 1820 SD MET A 223 6.500 15.467 178.073 1.00 69.78 S ANISOU 1820 SD MET A 223 9537 9576 7399 -99 168 -486 ATOM 1821 CE MET A 223 7.856 16.384 177.355 1.00 21.42 C ANISOU 1821 CE MET A 223 3495 3377 1266 -135 156 -466 ATOM 1822 N ILE A 224 1.747 17.858 177.142 1.00 38.87 N ANISOU 1822 N ILE A 224 5757 5541 3472 -182 207 -363 ATOM 1823 CA ILE A 224 0.592 17.289 176.454 1.00 19.02 C ANISOU 1823 CA ILE A 224 3381 2921 925 24 211 -344 ATOM 1824 C ILE A 224 0.175 18.180 175.290 1.00 21.38 C ANISOU 1824 C ILE A 224 3632 3301 1190 27 196 -349 ATOM 1825 O ILE A 224 -0.106 17.692 174.195 1.00 22.48 O ANISOU 1825 O ILE A 224 3727 3515 1300 51 198 -385 ATOM 1826 CB ILE A 224 -0.605 17.095 177.403 1.00 21.38 C ANISOU 1826 CB ILE A 224 3693 3226 1204 9 239 -328 ATOM 1827 CG1 ILE A 224 -0.307 15.995 178.419 1.00 21.52 C ANISOU 1827 CG1 ILE A 224 3510 3434 1232 316 184 -337 ATOM 1828 CG2 ILE A 224 -1.853 16.727 176.620 1.00 19.78 C ANISOU 1828 CG2 ILE A 224 3431 3139 947 77 249 -351 ATOM 1829 CD1 ILE A 224 -0.057 14.650 177.792 1.00 24.70 C ANISOU 1829 CD1 ILE A 224 3894 3869 1622 259 201 -400 ATOM 1830 N ILE A 225 0.150 19.487 175.526 1.00 21.50 N ANISOU 1830 N ILE A 225 3636 3334 1200 -39 183 -322 ATOM 1831 CA ILE A 225 -0.208 20.441 174.482 1.00 23.07 C ANISOU 1831 CA ILE A 225 3817 3591 1356 -21 164 -313 ATOM 1832 C ILE A 225 0.837 20.428 173.367 1.00 23.93 C ANISOU 1832 C ILE A 225 3931 3694 1467 4 149 -325 ATOM 1833 O ILE A 225 0.495 20.518 172.186 1.00 26.13 O ANISOU 1833 O ILE A 225 4181 4045 1701 19 145 -339 ATOM 1834 CB ILE A 225 -0.369 21.864 175.049 1.00 0.00 C ATOM 1835 CG1 ILE A 225 -1.798 22.095 175.582 1.00 0.00 C ATOM 1836 CG2 ILE A 225 0.018 22.924 174.002 1.00 0.00 C ATOM 1837 CD1 ILE A 225 -2.133 23.468 176.189 1.00 0.00 C ATOM 1838 N PHE A 226 2.107 20.298 173.743 1.00 21.70 N ANISOU 1838 N PHE A 226 3672 3352 1221 1 143 -324 ATOM 1839 CA PHE A 226 3.177 20.126 172.767 1.00 19.52 C ANISOU 1839 CA PHE A 226 3375 3109 934 36 136 -347 ATOM 1840 C PHE A 226 2.894 18.931 171.867 1.00 21.78 C ANISOU 1840 C PHE A 226 3611 3466 1199 40 160 -404 ATOM 1841 O PHE A 226 3.040 19.013 170.649 1.00 26.34 O ANISOU 1841 O PHE A 226 4153 4116 1740 24 163 -427 ATOM 1842 CB PHE A 226 4.538 19.939 173.463 1.00 0.00 C ATOM 1843 CG PHE A 226 5.722 19.751 172.539 1.00 0.00 C ATOM 1844 CD1 PHE A 226 6.094 18.458 172.132 1.00 0.00 C ATOM 1845 CD2 PHE A 226 6.450 20.866 172.089 1.00 0.00 C ATOM 1846 CE1 PHE A 226 7.189 18.280 171.269 1.00 0.00 C ATOM 1847 CE2 PHE A 226 7.546 20.688 171.227 1.00 0.00 C ATOM 1848 CZ PHE A 226 7.916 19.394 170.817 1.00 0.00 C ATOM 1849 N PHE A 227 2.510 17.816 172.484 1.00 21.16 N ANISOU 1849 N PHE A 227 3535 3362 1142 51 176 -427 ATOM 1850 CA PHE A 227 2.155 16.608 171.748 1.00 22.08 C ANISOU 1850 CA PHE A 227 3624 3532 1235 43 198 -491 ATOM 1851 C PHE A 227 1.047 16.899 170.746 1.00 24.08 C ANISOU 1851 C PHE A 227 3809 3877 1461 2 194 -499 ATOM 1852 O PHE A 227 1.139 16.522 169.583 1.00 23.23 O ANISOU 1852 O PHE A 227 3649 3835 1341 -33 199 -544 ATOM 1853 CB PHE A 227 1.716 15.495 172.705 1.00 22.03 C ANISOU 1853 CB PHE A 227 3640 3483 1249 68 211 -504 ATOM 1854 CG PHE A 227 2.856 14.725 173.312 1.00 21.84 C ANISOU 1854 CG PHE A 227 3649 3390 1260 111 212 -518 ATOM 1855 CD1 PHE A 227 4.003 14.462 172.582 1.00 22.04 C ANISOU 1855 CD1 PHE A 227 3676 3416 1282 102 221 -557 ATOM 1856 CD2 PHE A 227 2.778 14.264 174.615 1.00 19.58 C ANISOU 1856 CD2 PHE A 227 3380 3062 998 176 201 -494 ATOM 1857 CE1 PHE A 227 5.050 13.752 173.141 1.00 20.05 C ANISOU 1857 CE1 PHE A 227 3471 3094 1052 131 228 -571 ATOM 1858 CE2 PHE A 227 3.822 13.554 175.180 1.00 19.62 C ANISOU 1858 CE2 PHE A 227 3370 3058 1025 256 182 -514 ATOM 1859 CZ PHE A 227 4.959 13.298 174.443 1.00 19.86 C ANISOU 1859 CZ PHE A 227 3487 3005 1053 192 212 -540 ATOM 1860 N LEU A 228 0.006 17.584 171.206 1.00 24.75 N ANISOU 1860 N LEU A 228 3898 3975 1532 6 186 -459 ATOM 1861 CA LEU A 228 -1.122 17.935 170.353 1.00 25.13 C ANISOU 1861 CA LEU A 228 3876 4125 1545 -21 175 -463 ATOM 1862 C LEU A 228 -0.688 18.690 169.097 1.00 26.07 C ANISOU 1862 C LEU A 228 3972 4296 1637 -31 157 -458 ATOM 1863 O LEU A 228 -1.208 18.447 168.008 1.00 28.23 O ANISOU 1863 O LEU A 228 4178 4667 1880 -65 151 -490 ATOM 1864 CB LEU A 228 -2.134 18.768 171.142 1.00 20.91 C ANISOU 1864 CB LEU A 228 3356 3597 992 2 169 -416 ATOM 1865 CG LEU A 228 -3.266 19.433 170.358 1.00 21.62 C ANISOU 1865 CG LEU A 228 3374 3806 1034 1 148 -407 ATOM 1866 CD1 LEU A 228 -4.208 18.393 169.774 1.00 22.28 C ANISOU 1866 CD1 LEU A 228 3359 4006 1102 -47 155 -461 ATOM 1867 CD2 LEU A 228 -4.021 20.405 171.247 1.00 21.66 C ANISOU 1867 CD2 LEU A 228 3401 3811 1019 41 144 -360 ATOM 1868 N PHE A 229 0.278 19.591 169.247 1.00 25.05 N ANISOU 1868 N PHE A 229 3903 4107 1509 -9 148 -419 ATOM 1869 CA PHE A 229 0.674 20.474 168.154 1.00 24.82 C ANISOU 1869 CA PHE A 229 3874 4120 1438 -17 133 -401 ATOM 1870 C PHE A 229 1.701 19.866 167.201 1.00 27.54 C ANISOU 1870 C PHE A 229 4174 4506 1785 -47 150 -446 ATOM 1871 O PHE A 229 1.743 20.221 166.024 1.00 30.16 O ANISOU 1871 O PHE A 229 4480 4911 2070 -69 147 -449 ATOM 1872 CB PHE A 229 1.224 21.789 168.716 1.00 24.34 C ANISOU 1872 CB PHE A 229 3912 3977 1359 6 116 -341 ATOM 1873 CG PHE A 229 0.162 22.798 169.056 1.00 25.51 C ANISOU 1873 CG PHE A 229 4109 4116 1468 12 97 -297 ATOM 1874 CD1 PHE A 229 -0.748 22.553 170.070 1.00 25.66 C ANISOU 1874 CD1 PHE A 229 4110 4129 1508 16 103 -297 ATOM 1875 CD2 PHE A 229 0.081 23.998 168.368 1.00 27.16 C ANISOU 1875 CD2 PHE A 229 4373 4334 1614 6 74 -256 ATOM 1876 CE1 PHE A 229 -1.723 23.482 170.387 1.00 25.63 C ANISOU 1876 CE1 PHE A 229 4109 4161 1468 26 87 -264 ATOM 1877 CE2 PHE A 229 -0.892 24.931 168.681 1.00 26.86 C ANISOU 1877 CE2 PHE A 229 4354 4316 1536 -1 53 -219 ATOM 1878 CZ PHE A 229 -1.794 24.672 169.692 1.00 25.42 C ANISOU 1878 CZ PHE A 229 4120 4160 1379 23 60 -227 ATOM 1879 N TRP A 230 2.527 18.952 167.700 1.00 27.06 N ANISOU 1879 N TRP A 230 4111 4402 1767 -47 171 -482 ATOM 1880 CA TRP A 230 3.642 18.450 166.901 1.00 28.14 C ANISOU 1880 CA TRP A 230 4214 4578 1901 -71 194 -527 ATOM 1881 C TRP A 230 3.573 16.961 166.548 1.00 28.83 C ANISOU 1881 C TRP A 230 4272 4682 2000 -89 221 -608 ATOM 1882 O TRP A 230 4.365 16.483 165.734 1.00 29.36 O ANISOU 1882 O TRP A 230 4313 4790 2052 -106 246 -659 ATOM 1883 CB TRP A 230 4.963 18.731 167.619 1.00 21.28 C ANISOU 1883 CB TRP A 230 3376 3656 1053 -50 198 -510 ATOM 1884 CG TRP A 230 5.553 20.074 167.300 1.00 25.51 C ANISOU 1884 CG TRP A 230 3928 4212 1553 -59 184 -459 ATOM 1885 CD1 TRP A 230 5.814 21.088 168.177 1.00 24.72 C ANISOU 1885 CD1 TRP A 230 3892 4050 1450 -33 158 -403 ATOM 1886 CD2 TRP A 230 5.954 20.548 166.009 1.00 26.31 C ANISOU 1886 CD2 TRP A 230 3994 4400 1603 -99 196 -460 ATOM 1887 NE1 TRP A 230 6.358 22.161 167.512 1.00 24.45 N ANISOU 1887 NE1 TRP A 230 3869 4056 1366 -53 153 -370 ATOM 1888 CE2 TRP A 230 6.453 21.854 166.177 1.00 22.26 C ANISOU 1888 CE2 TRP A 230 3530 3870 1056 -98 178 -400 ATOM 1889 CE3 TRP A 230 5.942 19.993 164.724 1.00 23.00 C ANISOU 1889 CE3 TRP A 230 3516 4071 1151 -136 221 -508 ATOM 1890 CZ2 TRP A 230 6.934 22.613 165.115 1.00 23.07 C ANISOU 1890 CZ2 TRP A 230 3626 4044 1094 -139 188 -378 ATOM 1891 CZ3 TRP A 230 6.417 20.749 163.671 1.00 23.78 C ANISOU 1891 CZ3 TRP A 230 3603 4244 1186 -173 230 -489 ATOM 1892 CH2 TRP A 230 6.907 22.044 163.872 1.00 23.81 C ANISOU 1892 CH2 TRP A 230 3659 4229 1157 -177 216 -420 ATOM 1893 N THR A 231 2.643 16.227 167.148 1.00 27.42 N ANISOU 1893 N THR A 231 4106 4473 1838 -86 219 -625 ATOM 1894 CA THR A 231 2.525 14.800 166.851 1.00 25.98 C ANISOU 1894 CA THR A 231 3925 4291 1657 -106 243 -708 ATOM 1895 C THR A 231 1.929 14.509 165.467 1.00 28.78 C ANISOU 1895 C THR A 231 4224 4745 1967 -165 245 -762 ATOM 1896 O THR A 231 2.418 13.613 164.775 1.00 30.02 O ANISOU 1896 O THR A 231 4387 4911 2109 -180 270 -839 ATOM 1897 CB THR A 231 1.687 14.061 167.910 1.00 24.86 C ANISOU 1897 CB THR A 231 3821 4093 1533 -97 243 -712 ATOM 1898 OG1 THR A 231 2.176 14.386 169.217 1.00 23.63 O ANISOU 1898 OG1 THR A 231 3723 3851 1405 -38 238 -658 ATOM 1899 CG2 THR A 231 1.771 12.558 167.705 1.00 25.68 C ANISOU 1899 CG2 THR A 231 3958 4167 1631 -109 267 -803 ATOM 1900 N PRO A 232 0.872 15.244 165.053 1.00 30.36 N ANISOU 1900 N PRO A 232 4377 5022 2137 -192 218 -729 ATOM 1901 CA PRO A 232 0.375 14.954 163.702 1.00 31.89 C ANISOU 1901 CA PRO A 232 4519 5321 2276 -249 215 -784 ATOM 1902 C PRO A 232 1.430 15.165 162.617 1.00 33.31 C ANISOU 1902 C PRO A 232 4691 5542 2423 -252 232 -804 ATOM 1903 O PRO A 232 1.402 14.464 161.609 1.00 26.30 O ANISOU 1903 O PRO A 232 3785 4712 1494 -293 246 -880 ATOM 1904 CB PRO A 232 -0.793 15.940 163.531 1.00 31.03 C ANISOU 1904 CB PRO A 232 4367 5293 2132 -252 178 -727 ATOM 1905 CG PRO A 232 -0.609 16.962 164.596 1.00 32.09 C ANISOU 1905 CG PRO A 232 4543 5352 2297 -189 167 -641 ATOM 1906 CD PRO A 232 0.013 16.227 165.735 1.00 31.11 C ANISOU 1906 CD PRO A 232 4469 5118 2233 -168 191 -654 ATOM 1907 N TYR A 233 2.356 16.097 162.825 1.00 31.62 N ANISOU 1907 N TYR A 233 4493 5303 2218 -217 234 -744 ATOM 1908 CA TYR A 233 3.435 16.297 161.864 1.00 29.15 C ANISOU 1908 CA TYR A 233 4166 5042 1868 -228 259 -763 ATOM 1909 C TYR A 233 4.418 15.131 161.874 1.00 28.96 C ANISOU 1909 C TYR A 233 4156 4984 1863 -216 302 -844 ATOM 1910 O TYR A 233 4.801 14.628 160.822 1.00 30.11 O ANISOU 1910 O TYR A 233 4285 5192 1964 -237 331 -912 ATOM 1911 CB TYR A 233 4.187 17.599 162.140 1.00 27.23 C ANISOU 1911 CB TYR A 233 3941 4785 1622 -207 252 -681 ATOM 1912 CG TYR A 233 5.451 17.729 161.320 1.00 25.62 C ANISOU 1912 CG TYR A 233 3713 4639 1380 -227 288 -701 ATOM 1913 CD1 TYR A 233 5.400 18.102 159.984 1.00 26.69 C ANISOU 1913 CD1 TYR A 233 3826 4877 1436 -266 294 -707 ATOM 1914 CD2 TYR A 233 6.696 17.465 161.879 1.00 25.68 C ANISOU 1914 CD2 TYR A 233 3720 4615 1424 -208 317 -717 ATOM 1915 CE1 TYR A 233 6.553 18.215 159.229 1.00 27.47 C ANISOU 1915 CE1 TYR A 233 3900 5045 1491 -290 335 -726 ATOM 1916 CE2 TYR A 233 7.854 17.575 161.131 1.00 26.13 C ANISOU 1916 CE2 TYR A 233 3739 4749 1440 -230 356 -741 ATOM 1917 CZ TYR A 233 7.777 17.951 159.808 1.00 27.19 C ANISOU 1917 CZ TYR A 233 3851 4986 1496 -274 368 -745 ATOM 1918 OH TYR A 233 8.928 18.063 159.062 1.00 28.13 O ANISOU 1918 OH TYR A 233 3928 5195 1565 -301 416 -769 ATOM 1919 N ASN A 234 4.832 14.713 163.066 1.00 29.37 N ANISOU 1919 N ASN A 234 4249 4937 1972 -172 309 -839 ATOM 1920 CA ASN A 234 5.800 13.629 163.202 1.00 30.40 C ANISOU 1920 CA ASN A 234 4414 5022 2116 -136 349 -912 ATOM 1921 C ASN A 234 5.315 12.330 162.570 1.00 32.27 C ANISOU 1921 C ASN A 234 4680 5255 2327 -151 368 -1015 ATOM 1922 O ASN A 234 6.100 11.586 161.986 1.00 34.48 O ANISOU 1922 O ASN A 234 4980 5540 2582 -128 409 -1095 ATOM 1923 CB ASN A 234 6.128 13.393 164.677 1.00 30.27 C ANISOU 1923 CB ASN A 234 4454 4893 2152 -81 344 -883 ATOM 1924 CG ASN A 234 6.941 14.521 165.282 1.00 31.33 C ANISOU 1924 CG ASN A 234 4571 5030 2305 -67 331 -806 ATOM 1925 OD1 ASN A 234 7.792 15.116 164.619 1.00 31.73 O ANISOU 1925 OD1 ASN A 234 4571 5156 2329 -84 347 -801 ATOM 1926 ND2 ASN A 234 6.679 14.826 166.547 1.00 33.00 N ANISOU 1926 ND2 ASN A 234 4824 5162 2551 -40 304 -748 ATOM 1927 N LEU A 235 4.019 12.066 162.676 1.00 32.34 N ANISOU 1927 N LEU A 235 4693 5259 2335 -190 340 -1019 ATOM 1928 CA LEU A 235 3.460 10.827 162.155 1.00 33.63 C ANISOU 1928 CA LEU A 235 4893 5414 2472 -222 351 -1123 ATOM 1929 C LEU A 235 3.318 10.851 160.632 1.00 35.71 C ANISOU 1929 C LEU A 235 5111 5791 2665 -276 358 -1179 ATOM 1930 O LEU A 235 3.686 9.885 159.963 1.00 38.20 O ANISOU 1930 O LEU A 235 5471 6096 2946 -273 388 -1282 ATOM 1931 CB LEU A 235 2.096 10.518 162.800 1.00 0.00 C ATOM 1932 CG LEU A 235 0.880 11.459 162.616 1.00 0.00 C ATOM 1933 CD1 LEU A 235 0.548 11.694 161.144 1.00 0.00 C ATOM 1934 CD2 LEU A 235 -0.341 10.917 163.358 1.00 0.00 C ATOM 1935 N THR A 236 2.807 11.950 160.080 1.00 35.39 N ANISOU 1935 N THR A 236 4998 5854 2595 -316 329 -1115 ATOM 1936 CA THR A 236 2.571 12.014 158.637 1.00 35.85 C ANISOU 1936 CA THR A 236 5019 6030 2572 -366 330 -1161 ATOM 1937 C THR A 236 3.869 11.980 157.838 1.00 35.38 C ANISOU 1937 C THR A 236 4963 6005 2474 -339 376 -1201 ATOM 1938 O THR A 236 3.877 11.529 156.696 1.00 36.72 O ANISOU 1938 O THR A 236 5133 6246 2573 -369 394 -1280 ATOM 1939 CB THR A 236 1.776 13.266 158.222 1.00 0.00 C ATOM 1940 OG1 THR A 236 0.387 13.047 158.490 1.00 0.00 O ATOM 1941 CG2 THR A 236 1.941 13.630 156.741 1.00 0.00 C ATOM 1942 N ILE A 237 4.965 12.444 158.428 1.00 34.85 N ANISOU 1942 N ILE A 237 4897 5899 2447 -286 399 -1151 ATOM 1943 CA ILE A 237 6.246 12.378 157.735 1.00 37.47 C ANISOU 1943 CA ILE A 237 5216 6280 2739 -262 452 -1193 ATOM 1944 C ILE A 237 6.843 10.986 157.896 1.00 31.39 C ANISOU 1944 C ILE A 237 4515 5432 1982 -206 498 -1304 ATOM 1945 O ILE A 237 7.659 10.558 157.086 1.00 38.93 O ANISOU 1945 O ILE A 237 5472 6434 2886 -183 550 -1380 ATOM 1946 CB ILE A 237 7.246 13.441 158.241 1.00 29.85 C ANISOU 1946 CB ILE A 237 4214 5328 1801 -239 459 -1105 ATOM 1947 CG1 ILE A 237 7.720 13.120 159.659 1.00 31.92 C ANISOU 1947 CG1 ILE A 237 4512 5472 2145 -179 461 -1086 ATOM 1948 CG2 ILE A 237 6.628 14.827 158.170 1.00 29.39 C ANISOU 1948 CG2 ILE A 237 4126 5314 1727 -280 413 -996 ATOM 1949 CD1 ILE A 237 8.769 14.072 160.176 1.00 28.16 C ANISOU 1949 CD1 ILE A 237 3996 5014 1688 -165 467 -1015 ATOM 1950 N LEU A 238 6.424 10.279 158.940 1.00 33.94 N ANISOU 1950 N LEU A 238 4904 5630 2361 -176 482 -1314 ATOM 1951 CA LEU A 238 6.865 8.908 159.149 1.00 36.67 C ANISOU 1951 CA LEU A 238 5350 5872 2711 -111 520 -1419 ATOM 1952 C LEU A 238 6.168 7.995 158.147 1.00 40.45 C ANISOU 1952 C LEU A 238 5876 6366 3128 -153 522 -1533 ATOM 1953 O LEU A 238 6.764 7.052 157.628 1.00 41.71 O ANISOU 1953 O LEU A 238 6108 6491 3250 -102 569 -1644 ATOM 1954 CB LEU A 238 6.583 8.461 160.584 1.00 35.80 C ANISOU 1954 CB LEU A 238 5314 5621 2668 -68 498 -1390 ATOM 1955 CG LEU A 238 7.259 7.178 161.068 1.00 36.83 C ANISOU 1955 CG LEU A 238 5573 5616 2805 32 537 -1476 ATOM 1956 CD1 LEU A 238 8.770 7.259 160.893 1.00 36.92 C ANISOU 1956 CD1 LEU A 238 5566 5654 2809 106 604 -1496 ATOM 1957 CD2 LEU A 238 6.902 6.926 162.524 1.00 35.22 C ANISOU 1957 CD2 LEU A 238 5430 5297 2655 65 506 -1433 ATOM 1958 N ILE A 239 4.900 8.292 157.877 1.00 42.66 N ANISOU 1958 N ILE A 239 6115 6700 3393 -245 472 -1510 ATOM 1959 CA ILE A 239 4.143 7.593 156.845 1.00 45.49 C ANISOU 1959 CA ILE A 239 6498 7103 3684 -313 464 -1614 ATOM 1960 C ILE A 239 4.693 7.929 155.462 1.00 50.86 C ANISOU 1960 C ILE A 239 7137 7911 4278 -323 495 -1651 ATOM 1961 O ILE A 239 4.783 7.066 154.591 1.00 55.56 O ANISOU 1961 O ILE A 239 7791 8512 4806 -326 520 -1774 ATOM 1962 CB ILE A 239 2.650 7.961 156.921 1.00 0.00 C ATOM 1963 CG1 ILE A 239 1.759 6.702 156.864 1.00 0.00 C ATOM 1964 CG2 ILE A 239 2.271 8.967 155.820 1.00 0.00 C ATOM 1965 CD1 ILE A 239 0.235 6.888 156.931 1.00 0.00 C ATOM 1966 N SER A 240 5.066 9.191 155.275 1.00 52.48 N ANISOU 1966 N SER A 240 7250 8213 4476 -328 493 -1548 ATOM 1967 CA SER A 240 5.568 9.680 153.994 1.00 56.19 C ANISOU 1967 CA SER A 240 7674 8819 4855 -346 521 -1564 ATOM 1968 C SER A 240 6.995 9.210 153.717 1.00 58.08 C ANISOU 1968 C SER A 240 7940 9054 5076 -269 599 -1632 ATOM 1969 O SER A 240 7.527 9.408 152.625 1.00 58.75 O ANISOU 1969 O SER A 240 7996 9252 5075 -278 638 -1668 ATOM 1970 CB SER A 240 5.501 11.218 153.960 1.00 0.00 C ATOM 1971 OG SER A 240 5.758 11.688 152.631 1.00 0.00 O ATOM 1972 N VAL A 241 7.612 8.585 154.714 1.00 59.51 N ANISOU 1972 N VAL A 241 8176 9108 5327 -189 625 -1651 ATOM 1973 CA VAL A 241 8.989 8.128 154.586 1.00 62.84 C ANISOU 1973 CA VAL A 241 8615 9525 5736 -99 704 -1715 ATOM 1974 C VAL A 241 9.076 6.603 154.591 1.00 68.38 C ANISOU 1974 C VAL A 241 9456 10099 6427 -26 741 -1856 ATOM 1975 O VAL A 241 9.208 5.978 153.539 1.00 69.77 O ANISOU 1975 O VAL A 241 9677 10312 6520 -17 781 -1969 ATOM 1976 CB VAL A 241 9.873 8.694 155.713 1.00 0.00 C ATOM 1977 CG1 VAL A 241 9.893 10.220 155.612 1.00 0.00 C ATOM 1978 CG2 VAL A 241 9.366 8.295 157.105 1.00 0.00 C ATOM 1979 N PHE A 242 8.988 6.010 155.777 1.00 72.21 N ANISOU 1979 N PHE A 242 10024 10426 6986 30 727 -1850 ATOM 1980 CA PHE A 242 9.248 4.585 155.939 1.00 79.06 C ANISOU 1980 CA PHE A 242 11046 11147 7845 122 766 -1981 ATOM 1981 C PHE A 242 8.084 3.711 155.477 1.00 85.26 C ANISOU 1981 C PHE A 242 11930 11876 8589 64 719 -2081 ATOM 1982 O PHE A 242 8.269 2.782 154.689 1.00 86.97 O ANISOU 1982 O PHE A 242 12240 12066 8739 97 757 -2226 ATOM 1983 CB PHE A 242 9.577 4.277 157.397 1.00 0.00 C ATOM 1984 CG PHE A 242 10.511 3.108 157.621 1.00 0.00 C ATOM 1985 CD1 PHE A 242 11.807 3.132 157.074 1.00 0.00 C ATOM 1986 CD2 PHE A 242 10.088 2.000 158.375 1.00 0.00 C ATOM 1987 CE1 PHE A 242 12.679 2.051 157.286 1.00 0.00 C ATOM 1988 CE2 PHE A 242 10.961 0.918 158.586 1.00 0.00 C ATOM 1989 CZ PHE A 242 12.257 0.944 158.041 1.00 0.00 C ATOM 1990 N GLN A 243 6.887 4.015 155.967 1.00 89.80 N ANISOU 1990 N GLN A 243 12477 12441 9204 -29 638 -2012 ATOM 1991 CA GLN A 243 5.727 3.160 155.737 1.00 92.53 C ANISOU 1991 CA GLN A 243 12891 12740 9527 -112 590 -2112 ATOM 1992 C GLN A 243 5.075 3.377 154.374 1.00 92.37 C ANISOU 1992 C GLN A 243 12824 12854 9419 -214 572 -2152 ATOM 1993 O GLN A 243 4.083 2.722 154.047 1.00 95.39 O ANISOU 1993 O GLN A 243 13249 13223 9773 -308 532 -2241 ATOM 1994 CB GLN A 243 4.696 3.367 156.848 1.00 91.25 C ANISOU 1994 CB GLN A 243 12695 12536 9440 -186 528 -2032 ATOM 1995 CG GLN A 243 5.186 2.912 158.210 1.00 93.06 C ANISOU 1995 CG GLN A 243 12996 12623 9742 -95 538 -2024 ATOM 1996 CD GLN A 243 4.167 3.148 159.303 1.00 94.27 C ANISOU 1996 CD GLN A 243 13110 12750 9960 -176 487 -1945 ATOM 1997 OE1 GLN A 243 3.292 4.004 159.178 1.00 95.32 O ANISOU 1997 OE1 GLN A 243 13138 12985 10095 -274 450 -1852 ATOM 1998 NE2 GLN A 243 4.277 2.388 160.385 1.00 95.64 N ANISOU 1998 NE2 GLN A 243 13368 12787 10182 -132 488 -1987 ATOM 1999 N ASP A 244 5.626 4.292 153.582 1.00 88.13 N ANISOU 1999 N ASP A 244 12185 12467 8833 -218 605 -2104 ATOM 2000 CA ASP A 244 5.175 4.457 152.206 1.00 86.10 C ANISOU 2000 CA ASP A 244 11890 12353 8473 -303 597 -2159 ATOM 2001 C ASP A 244 5.822 3.368 151.359 1.00 87.73 C ANISOU 2001 C ASP A 244 12220 12516 8596 -236 655 -2325 ATOM 2002 O ASP A 244 5.397 3.093 150.237 1.00 89.57 O ANISOU 2002 O ASP A 244 12474 12828 8731 -298 647 -2418 ATOM 2003 CB ASP A 244 5.519 5.859 151.670 1.00 0.00 C ATOM 2004 CG ASP A 244 5.832 5.950 150.175 1.00 0.00 C ATOM 2005 OD1 ASP A 244 4.870 6.167 149.402 1.00 0.00 O ATOM 2006 OD2 ASP A 244 7.017 5.761 149.831 1.00 0.00 O1- ATOM 2007 N PHE A 245 6.859 2.750 151.915 1.00 87.94 N ANISOU 2007 N PHE A 245 12338 12417 8659 -100 714 -2366 ATOM 2008 CA PHE A 245 7.508 1.612 151.282 1.00 90.46 C ANISOU 2008 CA PHE A 245 12800 12664 8908 -8 777 -2534 ATOM 2009 C PHE A 245 6.788 0.328 151.675 1.00 93.10 C ANISOU 2009 C PHE A 245 13286 12830 9259 -21 732 -2669 ATOM 2010 O PHE A 245 6.714 -0.621 150.894 1.00 94.79 O ANISOU 2010 O PHE A 245 13621 12999 9394 -11 743 -2835 ATOM 2011 CB PHE A 245 8.981 1.541 151.674 1.00 0.00 C ATOM 2012 CG PHE A 245 9.951 2.129 150.673 1.00 0.00 C ATOM 2013 CD1 PHE A 245 10.307 3.487 150.758 1.00 0.00 C ATOM 2014 CD2 PHE A 245 10.497 1.322 149.661 1.00 0.00 C ATOM 2015 CE1 PHE A 245 11.212 4.036 149.833 1.00 0.00 C ATOM 2016 CE2 PHE A 245 11.402 1.871 148.735 1.00 0.00 C ATOM 2017 CZ PHE A 245 11.760 3.228 148.822 1.00 0.00 C ATOM 2018 N LEU A 246 6.259 0.310 152.896 1.00 93.53 N ANISOU 2018 N LEU A 246 13333 12790 9413 -48 680 -2603 ATOM 2019 CA LEU A 246 5.471 -0.818 153.379 1.00 97.39 C ANISOU 2019 CA LEU A 246 13941 13128 9935 -95 629 -2722 ATOM 2020 C LEU A 246 4.191 -0.959 152.561 1.00106.88 C ANISOU 2020 C LEU A 246 15121 14407 11082 -278 569 -2783 ATOM 2021 O LEU A 246 3.894 -2.029 152.027 1.00108.43 O ANISOU 2021 O LEU A 246 15442 14525 11231 -313 559 -2957 ATOM 2022 CB LEU A 246 5.130 -0.646 154.871 1.00 0.00 C ATOM 2023 CG LEU A 246 4.319 -1.713 155.646 1.00 0.00 C ATOM 2024 CD1 LEU A 246 5.045 -3.054 155.715 1.00 0.00 C ATOM 2025 CD2 LEU A 246 3.976 -1.217 157.051 1.00 0.00 C ATOM 2026 N PHE A 247 3.440 0.135 152.471 1.00115.11 N ANISOU 2026 N PHE A 247 16005 15602 12127 -392 530 -2644 ATOM 2027 CA PHE A 247 2.204 0.174 151.710 1.00117.18 C ANISOU 2027 CA PHE A 247 16220 15973 12332 -566 475 -2681 ATOM 2028 C PHE A 247 1.891 1.601 151.309 1.00116.71 C ANISOU 2028 C PHE A 247 15991 16106 12248 -606 453 -2520 ATOM 2029 O PHE A 247 2.807 2.384 151.059 1.00121.63 O ANISOU 2029 O PHE A 247 16560 16797 12858 -514 496 -2440 ATOM 2030 CB PHE A 247 1.054 -0.381 152.571 1.00 0.00 C ATOM 2031 CG PHE A 247 0.819 -1.871 152.462 1.00 0.00 C ATOM 2032 CD1 PHE A 247 0.494 -2.440 151.217 1.00 0.00 C ATOM 2033 CD2 PHE A 247 0.923 -2.688 153.601 1.00 0.00 C ATOM 2034 CE1 PHE A 247 0.281 -3.825 151.112 1.00 0.00 C ATOM 2035 CE2 PHE A 247 0.710 -4.073 153.496 1.00 0.00 C ATOM 2036 CZ PHE A 247 0.388 -4.642 152.250 1.00 0.00 C ATOM 2037 N THR A 248 0.604 1.935 151.238 1.00105.88 N ANISOU 2037 N THR A 248 14530 14830 10868 -756 392 -2483 ATOM 2038 CA THR A 248 0.164 3.306 150.965 1.00 95.02 C ANISOU 2038 CA THR A 248 12996 13633 9475 -793 364 -2336 ATOM 2039 C THR A 248 0.694 3.868 149.645 1.00 90.08 C ANISOU 2039 C THR A 248 12330 13157 8737 -771 389 -2347 ATOM 2040 O THR A 248 0.758 5.085 149.471 1.00 89.08 O ANISOU 2040 O THR A 248 12089 13158 8601 -763 384 -2221 ATOM 2041 CB THR A 248 0.590 4.240 152.113 1.00 0.00 C ATOM 2042 OG1 THR A 248 -0.007 3.785 153.331 1.00 0.00 O ATOM 2043 CG2 THR A 248 0.194 5.704 151.885 1.00 0.00 C ATOM 2044 N HIS A 249 1.067 2.990 148.720 1.00 87.42 N ANISOU 2044 N HIS A 249 12101 12803 8312 -759 415 -2501 ATOM 2045 CA HIS A 249 1.737 3.417 147.494 1.00 84.91 C ANISOU 2045 CA HIS A 249 11764 12619 7880 -725 455 -2524 ATOM 2046 C HIS A 249 0.768 3.858 146.397 1.00 84.71 C ANISOU 2046 C HIS A 249 11667 12781 7737 -843 399 -2532 ATOM 2047 O HIS A 249 -0.220 3.179 146.111 1.00 84.74 O ANISOU 2047 O HIS A 249 11706 12789 7701 -948 345 -2628 ATOM 2048 CB HIS A 249 2.640 2.288 146.962 1.00 0.00 C ATOM 2049 CG HIS A 249 2.859 2.247 145.468 1.00 0.00 C ATOM 2050 ND1 HIS A 249 2.064 1.559 144.643 1.00 0.00 N ATOM 2051 CD2 HIS A 249 3.816 2.834 144.676 1.00 0.00 C ATOM 2052 CE1 HIS A 249 2.509 1.710 143.385 1.00 0.00 C ATOM 2053 NE2 HIS A 249 3.591 2.487 143.349 1.00 0.00 N ATOM 2054 N GLU A 250 1.072 5.001 145.788 1.00 84.14 N ANISOU 2054 N GLU A 250 11499 12865 7607 -826 409 -2431 ATOM 2055 CA GLU A 250 0.306 5.534 144.664 1.00 85.84 C ANISOU 2055 CA GLU A 250 11652 13270 7691 -910 358 -2426 ATOM 2056 C GLU A 250 1.064 6.678 143.990 1.00 85.95 C ANISOU 2056 C GLU A 250 11604 13417 7636 -858 393 -2327 ATOM 2057 O GLU A 250 2.062 7.165 144.522 1.00 84.71 O ANISOU 2057 O GLU A 250 11427 13210 7548 -774 450 -2246 ATOM 2058 CB GLU A 250 -1.082 6.015 145.125 1.00 0.00 C ATOM 2059 CG GLU A 250 -1.722 7.155 144.316 1.00 0.00 C ATOM 2060 CD GLU A 250 -3.098 7.624 144.783 1.00 0.00 C ATOM 2061 OE1 GLU A 250 -3.145 8.546 145.627 1.00 0.00 O ATOM 2062 OE2 GLU A 250 -4.085 7.049 144.277 1.00 0.00 O1- ATOM 2063 N CYS A 251 0.594 7.098 142.819 1.00 87.66 N ANISOU 2063 N CYS A 251 11794 13806 7708 -913 359 -2334 ATOM 2064 CA CYS A 251 1.235 8.189 142.090 1.00 86.86 C ANISOU 2064 CA CYS A 251 11649 13836 7519 -876 388 -2239 ATOM 2065 C CYS A 251 0.877 9.538 142.701 1.00 85.10 C ANISOU 2065 C CYS A 251 11326 13647 7359 -867 343 -2047 ATOM 2066 O CYS A 251 1.722 10.427 142.809 1.00 84.60 O ANISOU 2066 O CYS A 251 11238 13595 7311 -813 384 -1941 ATOM 2067 CB CYS A 251 0.837 8.162 140.612 1.00 89.22 C ANISOU 2067 CB CYS A 251 11970 14305 7624 -933 362 -2313 ATOM 2068 SG CYS A 251 1.435 6.722 139.697 1.00 99.33 S ANISOU 2068 SG CYS A 251 13388 15558 8795 -926 427 -2546 ATOM 2069 N GLU A 252 -0.382 9.681 143.100 1.00 84.45 N ANISOU 2069 N GLU A 252 11195 13584 7309 -921 258 -2007 ATOM 2070 CA GLU A 252 -0.846 10.904 143.740 1.00 83.26 C ANISOU 2070 CA GLU A 252 10965 13454 7215 -899 211 -1836 ATOM 2071 C GLU A 252 -0.628 10.839 145.248 1.00 80.14 C ANISOU 2071 C GLU A 252 10556 12893 7001 -857 230 -1782 ATOM 2072 O GLU A 252 -0.994 11.760 145.976 1.00 78.48 O ANISOU 2072 O GLU A 252 10292 12670 6855 -831 196 -1650 ATOM 2073 CB GLU A 252 -2.320 11.145 143.427 1.00 0.00 C ATOM 2074 CG GLU A 252 -2.647 11.712 142.036 1.00 0.00 C ATOM 2075 CD GLU A 252 -4.124 11.949 141.734 1.00 0.00 C ATOM 2076 OE1 GLU A 252 -4.605 13.069 142.018 1.00 0.00 O ATOM 2077 OE2 GLU A 252 -4.748 11.000 141.217 1.00 0.00 O1- ATOM 2078 N GLN A 253 -0.026 9.745 145.707 1.00 79.93 N ANISOU 2078 N GLN A 253 10591 12735 7044 -843 284 -1886 ATOM 2079 CA GLN A 253 0.213 9.529 147.131 1.00 77.83 C ANISOU 2079 CA GLN A 253 10329 12306 6936 -802 302 -1848 ATOM 2080 C GLN A 253 1.229 10.513 147.700 1.00 76.48 C ANISOU 2080 C GLN A 253 10132 12096 6830 -722 341 -1722 ATOM 2081 O GLN A 253 0.940 11.231 148.659 1.00 74.96 O ANISOU 2081 O GLN A 253 9897 11858 6726 -702 312 -1607 ATOM 2082 CB GLN A 253 0.692 8.087 147.383 1.00 0.00 C ATOM 2083 CG GLN A 253 0.861 7.629 148.841 1.00 0.00 C ATOM 2084 CD GLN A 253 -0.413 7.664 149.673 1.00 0.00 C ATOM 2085 OE1 GLN A 253 -0.471 8.298 150.721 1.00 0.00 O ATOM 2086 NE2 GLN A 253 -1.453 6.973 149.217 1.00 0.00 N ATOM 2087 N SER A 254 2.419 10.536 147.105 1.00 77.63 N ANISOU 2087 N SER A 254 10305 12265 6926 -681 408 -1750 ATOM 2088 CA SER A 254 3.502 11.397 147.571 1.00 76.84 C ANISOU 2088 CA SER A 254 10178 12140 6877 -622 451 -1647 ATOM 2089 C SER A 254 3.091 12.868 147.548 1.00 76.66 C ANISOU 2089 C SER A 254 10105 12191 6833 -633 402 -1493 ATOM 2090 O SER A 254 3.429 13.630 148.454 1.00 78.04 O ANISOU 2090 O SER A 254 10259 12299 7093 -598 400 -1386 ATOM 2091 CB SER A 254 4.772 11.205 146.721 1.00 0.00 C ATOM 2092 OG SER A 254 4.413 10.818 145.389 1.00 0.00 O ATOM 2093 N ARG A 255 2.345 13.255 146.517 1.00 75.98 N ANISOU 2093 N ARG A 255 10011 12235 6623 -676 359 -1484 ATOM 2094 CA ARG A 255 1.886 14.633 146.376 1.00 74.55 C ANISOU 2094 CA ARG A 255 9809 12120 6397 -673 309 -1342 ATOM 2095 C ARG A 255 0.938 15.029 147.508 1.00 70.50 C ANISOU 2095 C ARG A 255 9266 11534 5987 -656 246 -1262 ATOM 2096 O ARG A 255 1.043 16.125 148.060 1.00 69.50 O ANISOU 2096 O ARG A 255 9141 11370 5895 -616 231 -1137 ATOM 2097 CB ARG A 255 1.195 14.832 145.014 1.00 0.00 C ATOM 2098 CG ARG A 255 -0.325 14.505 144.895 1.00 0.00 C ATOM 2099 CD ARG A 255 -1.068 14.406 143.527 1.00 0.00 C ATOM 2100 NE ARG A 255 -1.791 15.571 143.061 1.00 0.00 N ATOM 2101 CZ ARG A 255 -2.320 15.727 141.812 1.00 0.00 C ATOM 2102 NH1 ARG A 255 -2.535 14.710 140.980 1.00 0.00 N ATOM 2103 NH2 ARG A 255 -2.628 16.943 141.372 1.00 0.00 N1+ ATOM 2104 N HIS A 256 0.017 14.132 147.849 1.00 68.51 N ANISOU 2104 N HIS A 256 8994 11262 5775 -689 213 -1338 ATOM 2105 CA HIS A 256 -0.948 14.388 148.914 1.00 64.64 C ANISOU 2105 CA HIS A 256 8466 10722 5374 -678 161 -1275 ATOM 2106 C HIS A 256 -0.295 14.298 150.291 1.00 58.70 C ANISOU 2106 C HIS A 256 7726 9808 4768 -634 197 -1242 ATOM 2107 O HIS A 256 -0.657 15.036 151.209 1.00 55.85 O ANISOU 2107 O HIS A 256 7349 9398 4474 -597 169 -1144 ATOM 2108 CB HIS A 256 -2.129 13.404 148.824 1.00 0.00 C ATOM 2109 CG HIS A 256 -3.335 13.867 148.040 1.00 0.00 C ATOM 2110 ND1 HIS A 256 -4.349 14.528 148.604 1.00 0.00 N ATOM 2111 CD2 HIS A 256 -3.654 13.738 146.709 1.00 0.00 C ATOM 2112 CE1 HIS A 256 -5.267 14.801 147.662 1.00 0.00 C ATOM 2113 NE2 HIS A 256 -4.888 14.333 146.474 1.00 0.00 N ATOM 2114 N LEU A 257 0.665 13.389 150.429 1.00 55.33 N ANISOU 2114 N LEU A 257 7336 9304 4383 -628 259 -1327 ATOM 2115 CA LEU A 257 1.406 13.251 151.676 1.00 51.52 C ANISOU 2115 CA LEU A 257 6872 8677 4025 -578 293 -1300 ATOM 2116 C LEU A 257 2.252 14.493 151.933 1.00 50.75 C ANISOU 2116 C LEU A 257 6770 8571 3944 -532 307 -1182 ATOM 2117 O LEU A 257 2.504 14.856 153.082 1.00 49.58 O ANISOU 2117 O LEU A 257 6624 8324 3891 -493 306 -1116 ATOM 2118 CB LEU A 257 2.284 11.998 151.647 1.00 50.60 C ANISOU 2118 CB LEU A 257 6807 8491 3929 -565 354 -1422 ATOM 2119 CG LEU A 257 1.577 10.675 151.948 1.00 50.11 C ANISOU 2119 CG LEU A 257 6786 8360 3894 -600 344 -1532 ATOM 2120 CD1 LEU A 257 2.449 9.486 151.574 1.00 39.17 C ANISOU 2120 CD1 LEU A 257 5480 6915 2488 -573 404 -1666 ATOM 2121 CD2 LEU A 257 1.197 10.611 153.418 1.00 36.27 C ANISOU 2121 CD2 LEU A 257 5035 6488 2259 -581 325 -1477 ATOM 2122 N ASP A 258 2.683 15.144 150.857 1.00 52.09 N ANISOU 2122 N ASP A 258 6940 8843 4009 -543 320 -1158 ATOM 2123 CA ASP A 258 3.421 16.397 150.966 1.00 51.07 C ANISOU 2123 CA ASP A 258 6818 8713 3871 -518 332 -1045 ATOM 2124 C ASP A 258 2.509 17.512 151.449 1.00 48.55 C ANISOU 2124 C ASP A 258 6509 8377 3560 -498 267 -927 ATOM 2125 O ASP A 258 2.899 18.325 152.285 1.00 47.75 O ANISOU 2125 O ASP A 258 6430 8197 3517 -464 265 -840 ATOM 2126 CB ASP A 258 4.049 16.777 149.626 1.00 54.52 C ANISOU 2126 CB ASP A 258 7266 9273 4176 -545 367 -1050 ATOM 2127 CG ASP A 258 5.360 16.066 149.379 1.00 58.38 C ANISOU 2127 CG ASP A 258 7746 9769 4665 -542 449 -1135 ATOM 2128 OD1 ASP A 258 5.545 14.956 149.922 1.00 59.17 O ANISOU 2128 OD1 ASP A 258 7846 9795 4842 -520 472 -1226 ATOM 2129 OD2 ASP A 258 6.207 16.618 148.646 1.00 61.58 O1- ANISOU 2129 OD2 ASP A 258 8151 10258 4988 -558 494 -1109 ATOM 2130 N LEU A 259 1.294 17.545 150.913 1.00 47.57 N ANISOU 2130 N LEU A 259 6373 8332 3371 -513 212 -931 ATOM 2131 CA LEU A 259 0.304 18.527 151.329 1.00 45.33 C ANISOU 2131 CA LEU A 259 6098 8044 3081 -477 148 -830 ATOM 2132 C LEU A 259 0.014 18.389 152.821 1.00 42.23 C ANISOU 2132 C LEU A 259 5693 7530 2822 -444 138 -810 ATOM 2133 O LEU A 259 -0.016 19.381 153.548 1.00 41.23 O ANISOU 2133 O LEU A 259 5604 7336 2727 -394 119 -713 ATOM 2134 CB LEU A 259 -0.989 18.370 150.507 1.00 0.00 C ATOM 2135 CG LEU A 259 -1.018 18.633 148.982 1.00 0.00 C ATOM 2136 CD1 LEU A 259 -2.373 18.297 148.363 1.00 0.00 C ATOM 2137 CD2 LEU A 259 -0.635 20.081 148.675 1.00 0.00 C ATOM 2138 N ALA A 260 -0.180 17.153 153.273 1.00 40.33 N ANISOU 2138 N ALA A 260 5416 7256 2651 -472 153 -903 ATOM 2139 CA ALA A 260 -0.426 16.884 154.685 1.00 37.32 C ANISOU 2139 CA ALA A 260 5029 6762 2387 -448 151 -890 ATOM 2140 C ALA A 260 0.778 17.284 155.533 1.00 35.60 C ANISOU 2140 C ALA A 260 4853 6429 2246 -406 188 -840 ATOM 2141 O ALA A 260 0.622 17.757 156.658 1.00 34.62 O ANISOU 2141 O ALA A 260 4746 6219 2190 -366 173 -777 ATOM 2142 CB ALA A 260 -0.762 15.416 154.898 1.00 36.11 C ANISOU 2142 CB ALA A 260 4856 6589 2275 -496 166 -1003 ATOM 2143 N VAL A 261 1.975 17.093 154.988 1.00 35.67 N ANISOU 2143 N VAL A 261 4874 6446 2233 -417 236 -874 ATOM 2144 CA VAL A 261 3.202 17.484 155.674 1.00 34.74 C ANISOU 2144 CA VAL A 261 4778 6249 2171 -388 271 -833 ATOM 2145 C VAL A 261 3.254 18.998 155.868 1.00 36.80 C ANISOU 2145 C VAL A 261 5078 6496 2408 -364 246 -713 ATOM 2146 O VAL A 261 3.618 19.486 156.938 1.00 35.84 O ANISOU 2146 O VAL A 261 4984 6281 2353 -332 244 -659 ATOM 2147 CB VAL A 261 4.454 17.028 154.902 1.00 0.00 C ATOM 2148 CG1 VAL A 261 5.592 18.014 155.171 1.00 0.00 C ATOM 2149 CG2 VAL A 261 4.909 15.621 155.311 1.00 0.00 C ATOM 2150 N GLN A 262 2.877 19.735 154.829 1.00 40.45 N ANISOU 2150 N GLN A 262 5560 7046 2763 -377 226 -674 ATOM 2151 CA GLN A 262 2.878 21.191 154.885 1.00 43.69 C ANISOU 2151 CA GLN A 262 6043 7433 3125 -349 201 -560 ATOM 2152 C GLN A 262 1.888 21.713 155.919 1.00 43.99 C ANISOU 2152 C GLN A 262 6114 7389 3210 -293 150 -502 ATOM 2153 O GLN A 262 2.222 22.586 156.721 1.00 42.59 O ANISOU 2153 O GLN A 262 6004 7119 3061 -258 145 -432 ATOM 2154 CB GLN A 262 2.552 21.780 153.513 1.00 47.06 C ANISOU 2154 CB GLN A 262 6501 7969 3410 -366 185 -530 ATOM 2155 CG GLN A 262 3.563 21.444 152.437 1.00 49.56 C ANISOU 2155 CG GLN A 262 6797 8377 3658 -421 241 -577 ATOM 2156 CD GLN A 262 3.087 21.841 151.057 1.00 55.47 C ANISOU 2156 CD GLN A 262 7576 9245 4256 -438 222 -558 ATOM 2157 OE1 GLN A 262 2.450 21.052 150.357 1.00 59.98 O ANISOU 2157 OE1 GLN A 262 8102 9904 4784 -458 207 -633 ATOM 2158 NE2 GLN A 262 3.389 23.070 150.658 1.00 58.05 N ANISOU 2158 NE2 GLN A 262 7991 9574 4491 -432 219 -456 ATOM 2159 N VAL A 263 0.673 21.177 155.896 1.00 44.21 N ANISOU 2159 N VAL A 263 6095 7463 3240 -288 115 -537 ATOM 2160 CA VAL A 263 -0.380 21.631 156.797 1.00 30.16 C ANISOU 2160 CA VAL A 263 4331 5637 1492 -235 71 -489 ATOM 2161 C VAL A 263 -0.029 21.347 158.253 1.00 28.63 C ANISOU 2161 C VAL A 263 4141 5320 1417 -215 90 -492 ATOM 2162 O VAL A 263 -0.133 22.225 159.108 1.00 27.98 O ANISOU 2162 O VAL A 263 4126 5152 1354 -165 73 -423 ATOM 2163 CB VAL A 263 -1.735 20.968 156.467 1.00 31.69 C ANISOU 2163 CB VAL A 263 4442 5938 1661 -248 34 -539 ATOM 2164 CG1 VAL A 263 -2.781 21.350 157.502 1.00 30.19 C ANISOU 2164 CG1 VAL A 263 4245 5718 1508 -194 -1 -497 ATOM 2165 CG2 VAL A 263 -2.195 21.363 155.075 1.00 32.47 C ANISOU 2165 CG2 VAL A 263 4542 6168 1627 -258 2 -528 ATOM 2166 N THR A 264 0.396 20.118 158.526 1.00 33.22 N ANISOU 2166 N THR A 264 4668 5887 2068 -250 125 -572 ATOM 2167 CA THR A 264 0.711 19.704 159.887 1.00 26.93 C ANISOU 2167 CA THR A 264 3880 4979 1374 -230 141 -577 ATOM 2168 C THR A 264 1.898 20.467 160.459 1.00 40.39 C ANISOU 2168 C THR A 264 5645 6596 3104 -206 158 -523 ATOM 2169 O THR A 264 1.920 20.785 161.649 1.00 40.57 O ANISOU 2169 O THR A 264 5707 6524 3182 -169 150 -486 ATOM 2170 CB THR A 264 1.009 18.203 159.958 1.00 26.90 C ANISOU 2170 CB THR A 264 3833 4968 1419 -267 174 -674 ATOM 2171 OG1 THR A 264 1.946 17.859 158.932 1.00 27.72 O ANISOU 2171 OG1 THR A 264 3926 5124 1483 -300 208 -724 ATOM 2172 CG2 THR A 264 -0.264 17.400 159.765 1.00 27.42 C ANISOU 2172 CG2 THR A 264 3850 5097 1472 -301 155 -729 ATOM 2173 N GLU A 265 2.885 20.758 159.617 1.00 41.17 N ANISOU 2173 N GLU A 265 5750 6739 3156 -234 183 -523 ATOM 2174 CA GLU A 265 4.046 21.518 160.064 1.00 26.53 C ANISOU 2174 CA GLU A 265 3940 4829 1312 -228 200 -475 ATOM 2175 C GLU A 265 3.641 22.954 160.371 1.00 33.38 C ANISOU 2175 C GLU A 265 4905 5641 2136 -188 163 -380 ATOM 2176 O GLU A 265 4.160 23.570 161.299 1.00 25.84 O ANISOU 2176 O GLU A 265 4006 4600 1211 -164 160 -338 ATOM 2177 CB GLU A 265 5.162 21.488 159.020 1.00 27.48 C ANISOU 2177 CB GLU A 265 4030 5033 1378 -280 242 -498 ATOM 2178 CG GLU A 265 6.466 22.103 159.507 1.00 40.70 C ANISOU 2178 CG GLU A 265 5722 6677 3066 -294 266 -462 ATOM 2179 CD GLU A 265 7.661 21.702 158.664 1.00 41.20 C ANISOU 2179 CD GLU A 265 5722 6838 3093 -350 322 -510 ATOM 2180 OE1 GLU A 265 7.460 21.142 157.565 1.00 42.50 O ANISOU 2180 OE1 GLU A 265 5853 7091 3205 -372 342 -562 ATOM 2181 OE2 GLU A 265 8.804 21.946 159.105 1.00 40.56 O1- ANISOU 2181 OE2 GLU A 265 5624 6756 3030 -372 347 -501 ATOM 2182 N VAL A 266 2.705 23.480 159.589 1.00 35.46 N ANISOU 2182 N VAL A 266 5201 5954 2317 -175 133 -348 ATOM 2183 CA VAL A 266 2.142 24.799 159.848 1.00 35.82 C ANISOU 2183 CA VAL A 266 5369 5937 2306 -121 94 -262 ATOM 2184 C VAL A 266 1.485 24.821 161.224 1.00 38.58 C ANISOU 2184 C VAL A 266 5744 6189 2726 -74 72 -253 ATOM 2185 O VAL A 266 1.650 25.773 161.987 1.00 42.95 O ANISOU 2185 O VAL A 266 6411 6638 3271 -36 58 -197 ATOM 2186 CB VAL A 266 1.111 25.198 158.775 1.00 0.00 C ATOM 2187 CG1 VAL A 266 0.064 26.116 159.408 1.00 0.00 C ATOM 2188 CG2 VAL A 266 1.759 25.927 157.590 1.00 0.00 C ATOM 2189 N ILE A 267 0.752 23.756 161.535 1.00 35.36 N ANISOU 2189 N ILE A 267 5237 5820 2379 -82 73 -310 ATOM 2190 CA ILE A 267 0.115 23.610 162.839 1.00 34.61 C ANISOU 2190 CA ILE A 267 5146 5656 2350 -50 63 -308 ATOM 2191 C ILE A 267 1.143 23.639 163.962 1.00 33.41 C ANISOU 2191 C ILE A 267 5040 5390 2265 -42 83 -301 ATOM 2192 O ILE A 267 0.975 24.345 164.955 1.00 33.79 O ANISOU 2192 O ILE A 267 5174 5344 2320 -11 68 -260 ATOM 2193 CB ILE A 267 -0.691 22.299 162.901 1.00 0.00 C ATOM 2194 CG1 ILE A 267 -1.857 22.311 161.892 1.00 0.00 C ATOM 2195 CG2 ILE A 267 -1.190 22.024 164.331 1.00 0.00 C ATOM 2196 CD1 ILE A 267 -2.622 21.000 161.651 1.00 0.00 C ATOM 2197 N ALA A 268 2.211 22.866 163.794 1.00 33.41 N ANISOU 2197 N ALA A 268 4981 5408 2305 -75 115 -346 ATOM 2198 CA ALA A 268 3.273 22.802 164.777 1.00 31.83 C ANISOU 2198 CA ALA A 268 4802 5131 2162 -68 130 -346 ATOM 2199 C ALA A 268 4.006 24.119 164.948 1.00 34.26 C ANISOU 2199 C ALA A 268 5201 5389 2425 -48 117 -284 ATOM 2200 O ALA A 268 4.495 24.426 166.034 1.00 34.13 O ANISOU 2200 O ALA A 268 5229 5298 2442 -18 109 -267 ATOM 2201 CB ALA A 268 4.277 21.706 164.374 1.00 0.00 C ATOM 2202 N TYR A 269 4.086 24.902 163.878 1.00 34.32 N ANISOU 2202 N TYR A 269 5242 5447 2349 -59 114 -250 ATOM 2203 CA TYR A 269 4.797 26.174 163.927 1.00 33.12 C ANISOU 2203 CA TYR A 269 5175 5268 2140 -37 104 -189 ATOM 2204 C TYR A 269 4.052 27.211 164.762 1.00 32.61 C ANISOU 2204 C TYR A 269 5212 5099 2079 52 62 -133 ATOM 2205 O TYR A 269 4.639 28.203 165.196 1.00 33.68 O ANISOU 2205 O TYR A 269 5356 5236 2205 102 49 -90 ATOM 2206 CB TYR A 269 5.036 26.712 162.504 1.00 0.00 C ATOM 2207 CG TYR A 269 6.218 27.026 161.678 1.00 0.00 C ATOM 2208 CD1 TYR A 269 6.924 25.887 161.654 1.00 0.00 C ATOM 2209 CD2 TYR A 269 6.082 27.797 160.460 1.00 0.00 C ATOM 2210 CE1 TYR A 269 6.605 25.196 160.525 1.00 0.00 C ATOM 2211 CE2 TYR A 269 6.456 27.197 159.253 1.00 0.00 C ATOM 2212 CZ TYR A 269 6.776 25.829 159.301 1.00 0.00 C ATOM 2213 OH TYR A 269 7.474 25.229 158.304 1.00 0.00 O ATOM 2214 N THR A 270 2.764 26.980 164.994 1.00 31.53 N ANISOU 2214 N THR A 270 5106 4910 1963 47 45 -138 ATOM 2215 CA THR A 270 1.962 27.901 165.793 1.00 32.09 C ANISOU 2215 CA THR A 270 5286 4856 2052 26 14 -93 ATOM 2216 C THR A 270 2.025 27.554 167.277 1.00 34.07 C ANISOU 2216 C THR A 270 5518 5032 2396 -26 20 -113 ATOM 2217 O THR A 270 1.262 28.093 168.078 1.00 36.36 O ANISOU 2217 O THR A 270 5686 5445 2686 -208 7 -98 ATOM 2218 CB THR A 270 0.486 27.901 165.359 1.00 31.07 C ANISOU 2218 CB THR A 270 5119 4822 1863 -51 -6 -88 ATOM 2219 OG1 THR A 270 -0.107 26.635 165.674 1.00 30.38 O ANISOU 2219 OG1 THR A 270 4924 4806 1812 -14 12 -148 ATOM 2220 CG2 THR A 270 0.366 28.161 163.866 1.00 32.41 C ANISOU 2220 CG2 THR A 270 5320 5063 1931 -23 -18 -68 ATOM 2221 N HIS A 271 2.933 26.653 167.640 1.00 33.84 N ANISOU 2221 N HIS A 271 5405 5032 2418 69 39 -154 ATOM 2222 CA HIS A 271 3.058 26.216 169.026 1.00 32.95 C ANISOU 2222 CA HIS A 271 5288 4845 2387 56 42 -170 ATOM 2223 C HIS A 271 4.023 27.091 169.823 1.00 33.04 C ANISOU 2223 C HIS A 271 5124 5018 2412 277 9 -156 ATOM 2224 O HIS A 271 3.957 27.141 171.053 1.00 34.51 O ANISOU 2224 O HIS A 271 4974 5502 2637 65 11 -182 ATOM 2225 CB HIS A 271 3.510 24.755 169.090 1.00 31.72 C ANISOU 2225 CB HIS A 271 5023 4760 2269 53 69 -228 ATOM 2226 CG HIS A 271 3.803 24.279 170.478 1.00 30.62 C ANISOU 2226 CG HIS A 271 4884 4550 2202 59 69 -238 ATOM 2227 ND1 HIS A 271 5.085 24.153 170.967 1.00 30.28 N ANISOU 2227 ND1 HIS A 271 4803 4522 2179 100 62 -249 ATOM 2228 CD2 HIS A 271 2.977 23.922 171.491 1.00 29.28 C ANISOU 2228 CD2 HIS A 271 4724 4331 2072 -9 80 -240 ATOM 2229 CE1 HIS A 271 5.037 23.728 172.217 1.00 29.78 C ANISOU 2229 CE1 HIS A 271 4760 4386 2172 108 57 -252 ATOM 2230 NE2 HIS A 271 3.770 23.580 172.558 1.00 29.29 N ANISOU 2230 NE2 HIS A 271 4734 4273 2122 -8 78 -245 ATOM 2231 N CYS A 272 4.903 27.797 169.123 1.00 33.19 N ANISOU 2231 N CYS A 272 5109 5139 2362 214 11 -137 ATOM 2232 CA CYS A 272 5.925 28.611 169.777 1.00 36.18 C ANISOU 2232 CA CYS A 272 5458 5579 2708 123 -1 -122 ATOM 2233 C CYS A 272 5.352 29.822 170.517 1.00 38.66 C ANISOU 2233 C CYS A 272 5775 5935 2980 43 -25 -82 ATOM 2234 O CYS A 272 6.101 30.614 171.086 1.00 41.76 O ANISOU 2234 O CYS A 272 6277 6265 3327 -4 -43 -62 ATOM 2235 CB CYS A 272 6.957 29.085 168.751 1.00 38.27 C ANISOU 2235 CB CYS A 272 5818 5839 2885 48 14 -98 ATOM 2236 SG CYS A 272 6.285 30.155 167.458 1.00 51.97 S ANISOU 2236 SG CYS A 272 7593 7635 4517 54 12 -31 ATOM 2237 N CYS A 273 4.030 29.966 170.509 1.00 37.01 N ANISOU 2237 N CYS A 273 5534 5760 2766 5 -28 -68 ATOM 2238 CA CYS A 273 3.383 31.078 171.196 1.00 36.91 C ANISOU 2238 CA CYS A 273 5677 5659 2688 1 -55 -27 ATOM 2239 C CYS A 273 2.394 30.589 172.250 1.00 35.47 C ANISOU 2239 C CYS A 273 5503 5411 2564 24 -50 -55 ATOM 2240 O CYS A 273 1.621 31.374 172.799 1.00 35.84 O ANISOU 2240 O CYS A 273 5667 5350 2602 107 -67 -30 ATOM 2241 CB CYS A 273 2.659 31.976 170.193 1.00 38.57 C ANISOU 2241 CB CYS A 273 5962 5876 2817 14 -71 33 ATOM 2242 SG CYS A 273 1.111 31.290 169.572 1.00 48.10 S ANISOU 2242 SG CYS A 273 7118 7143 4016 -10 -66 21 ATOM 2243 N VAL A 274 2.426 29.292 172.537 1.00 33.59 N ANISOU 2243 N VAL A 274 5154 5212 2398 -22 -24 -105 ATOM 2244 CA VAL A 274 1.418 28.680 173.394 1.00 32.40 C ANISOU 2244 CA VAL A 274 5023 5012 2274 2 -10 -127 ATOM 2245 C VAL A 274 1.823 28.634 174.866 1.00 31.71 C ANISOU 2245 C VAL A 274 4965 4845 2239 53 -15 -140 ATOM 2246 O VAL A 274 0.998 28.897 175.745 1.00 32.27 O ANISOU 2246 O VAL A 274 5098 4843 2322 140 -16 -134 ATOM 2247 CB VAL A 274 1.093 27.253 172.916 1.00 0.00 C ATOM 2248 CG1 VAL A 274 0.109 26.611 173.897 1.00 0.00 C ATOM 2249 CG2 VAL A 274 0.475 27.236 171.511 1.00 0.00 C ATOM 2250 N ASN A 275 3.125 28.354 175.085 1.00 30.57 N ANISOU 2250 N ASN A 275 4776 4722 2117 12 -19 -159 ATOM 2251 CA ASN A 275 3.848 28.288 176.367 1.00 29.55 C ANISOU 2251 CA ASN A 275 4681 4517 2029 39 -29 -172 ATOM 2252 C ASN A 275 3.443 29.402 177.356 1.00 28.56 C ANISOU 2252 C ASN A 275 4705 4257 1891 114 -53 -148 ATOM 2253 O ASN A 275 2.875 29.059 178.394 1.00 27.19 O ANISOU 2253 O ASN A 275 4561 4029 1742 166 -48 -156 ATOM 2254 CB ASN A 275 5.384 28.268 176.100 1.00 29.83 C ANISOU 2254 CB ASN A 275 4667 4596 2070 4 -41 -191 ATOM 2255 CG ASN A 275 6.038 26.903 176.278 1.00 31.50 C ANISOU 2255 CG ASN A 275 4738 4887 2343 -18 -16 -225 ATOM 2256 OD1 ASN A 275 5.852 26.271 177.315 1.00 32.85 O ANISOU 2256 OD1 ASN A 275 4873 5053 2554 -51 12 -240 ATOM 2257 ND2 ASN A 275 6.860 26.469 175.329 1.00 31.52 N ANISOU 2257 ND2 ASN A 275 4701 4925 2350 27 -27 -238 ATOM 2258 N PRO A 276 3.627 30.703 177.017 1.00 28.28 N ANISOU 2258 N PRO A 276 4775 4162 1808 121 -79 -119 ATOM 2259 CA PRO A 276 3.179 31.801 177.897 1.00 28.49 C ANISOU 2259 CA PRO A 276 4966 4044 1814 197 -101 -106 ATOM 2260 C PRO A 276 1.677 31.789 178.231 1.00 28.67 C ANISOU 2260 C PRO A 276 5012 4049 1831 316 -84 -101 ATOM 2261 O PRO A 276 1.308 32.197 179.332 1.00 23.29 O ANISOU 2261 O PRO A 276 4427 3276 1146 401 -89 -108 ATOM 2262 CB PRO A 276 3.569 33.084 177.144 1.00 29.19 C ANISOU 2262 CB PRO A 276 5178 4067 1844 168 -129 -72 ATOM 2263 CG PRO A 276 4.642 32.648 176.162 1.00 28.31 C ANISOU 2263 CG PRO A 276 4961 4065 1731 63 -124 -73 ATOM 2264 CD PRO A 276 4.224 31.240 175.792 1.00 27.70 C ANISOU 2264 CD PRO A 276 4703 4133 1690 63 -89 -97 ATOM 2265 N VAL A 277 0.839 31.313 177.294 1.00 30.08 N ANISOU 2265 N VAL A 277 5104 4325 2000 325 -64 -93 ATOM 2266 CA VAL A 277 -0.608 31.330 177.483 1.00 31.39 C ANISOU 2266 CA VAL A 277 5270 4505 2152 442 -48 -91 ATOM 2267 C VAL A 277 -1.020 30.256 178.482 1.00 34.56 C ANISOU 2267 C VAL A 277 5594 4938 2598 451 -18 -121 ATOM 2268 O VAL A 277 -1.887 30.479 179.329 1.00 38.20 O ANISOU 2268 O VAL A 277 6092 5374 3047 562 -6 -124 ATOM 2269 CB VAL A 277 -1.362 31.118 176.157 1.00 0.00 C ATOM 2270 CG1 VAL A 277 -2.863 31.047 176.443 1.00 0.00 C ATOM 2271 CG2 VAL A 277 -1.100 32.249 175.153 1.00 0.00 C ATOM 2272 N ILE A 278 -0.276 29.138 178.524 1.00 31.74 N ANISOU 2272 N ILE A 278 5135 4639 2285 338 -4 -142 ATOM 2273 CA ILE A 278 -0.413 28.108 179.559 1.00 31.01 C ANISOU 2273 CA ILE A 278 4987 4566 2229 330 23 -163 ATOM 2274 C ILE A 278 -0.108 28.671 180.954 1.00 32.60 C ANISOU 2274 C ILE A 278 5274 4675 2436 384 11 -164 ATOM 2275 O ILE A 278 -0.864 28.426 181.897 1.00 32.57 O ANISOU 2275 O ILE A 278 5272 4672 2431 439 33 -170 ATOM 2276 CB ILE A 278 0.543 26.896 179.365 1.00 20.48 C ANISOU 2276 CB ILE A 278 3558 3290 934 208 36 -186 ATOM 2277 CG1 ILE A 278 0.546 26.353 177.927 1.00 25.05 C ANISOU 2277 CG1 ILE A 278 4076 3943 1497 144 51 -193 ATOM 2278 CG2 ILE A 278 0.229 25.763 180.357 1.00 20.16 C ANISOU 2278 CG2 ILE A 278 3485 3254 920 201 63 -202 ATOM 2279 CD1 ILE A 278 -0.837 26.289 177.273 1.00 24.62 C ANISOU 2279 CD1 ILE A 278 3959 3924 1471 31 72 -225 ATOM 2280 N TYR A 279 0.966 29.462 181.051 1.00 34.39 N ANISOU 2280 N TYR A 279 5579 4829 2658 360 -24 -160 ATOM 2281 CA TYR A 279 1.377 30.100 182.297 1.00 21.98 C ANISOU 2281 CA TYR A 279 4114 3158 1078 398 -45 -165 ATOM 2282 C TYR A 279 0.335 31.142 182.754 1.00 32.86 C ANISOU 2282 C TYR A 279 5593 4477 2416 532 -37 -161 ATOM 2283 O TYR A 279 0.200 31.372 183.950 1.00 23.09 O ANISOU 2283 O TYR A 279 4384 3217 1172 587 -25 -171 ATOM 2284 CB TYR A 279 2.783 30.725 182.174 1.00 24.43 C ANISOU 2284 CB TYR A 279 4508 3402 1373 336 -88 -162 ATOM 2285 CG TYR A 279 3.906 29.929 181.512 1.00 23.40 C ANISOU 2285 CG TYR A 279 4278 3345 1270 223 -97 -172 ATOM 2286 CD1 TYR A 279 3.842 28.537 181.268 1.00 22.38 C ANISOU 2286 CD1 TYR A 279 4030 3293 1179 195 -75 -187 ATOM 2287 CD2 TYR A 279 5.045 30.639 181.087 1.00 24.47 C ANISOU 2287 CD2 TYR A 279 4444 3472 1380 150 -128 -168 ATOM 2288 CE1 TYR A 279 4.848 27.909 180.507 1.00 23.80 C ANISOU 2288 CE1 TYR A 279 4123 3545 1374 119 -83 -201 ATOM 2289 CE2 TYR A 279 6.084 29.994 180.391 1.00 24.60 C ANISOU 2289 CE2 TYR A 279 4358 3580 1409 71 -133 -182 ATOM 2290 CZ TYR A 279 5.968 28.633 180.066 1.00 25.65 C ANISOU 2290 CZ TYR A 279 4371 3794 1582 66 -111 -201 ATOM 2291 OH TYR A 279 6.924 28.031 179.304 1.00 27.97 O ANISOU 2291 OH TYR A 279 4566 4183 1878 15 -118 -221 ATOM 2292 N ALA A 280 -0.436 31.709 181.818 1.00 35.05 N ANISOU 2292 N ALA A 280 5925 4737 2657 595 -43 -145 ATOM 2293 CA ALA A 280 -1.563 32.579 182.127 1.00 35.85 C ANISOU 2293 CA ALA A 280 6133 4780 2708 750 -39 -143 ATOM 2294 C ALA A 280 -2.814 31.825 182.625 1.00 36.51 C ANISOU 2294 C ALA A 280 6118 4968 2786 834 7 -149 ATOM 2295 O ALA A 280 -3.586 32.440 183.354 1.00 37.14 O ANISOU 2295 O ALA A 280 6264 5021 2825 962 21 -156 ATOM 2296 CB ALA A 280 -1.897 33.446 180.904 1.00 34.76 C ANISOU 2296 CB ALA A 280 6079 4603 2524 805 -59 -120 ATOM 2297 N PHE A 281 -3.029 30.556 182.229 1.00 37.90 N ANISOU 2297 N PHE A 281 6142 5267 2993 758 32 -149 ATOM 2298 CA PHE A 281 -4.288 29.863 182.487 1.00 40.85 C ANISOU 2298 CA PHE A 281 6418 5752 3351 810 77 -155 ATOM 2299 C PHE A 281 -4.173 28.796 183.571 1.00 40.80 C ANISOU 2299 C PHE A 281 6366 5768 3368 749 106 -168 ATOM 2300 O PHE A 281 -5.121 28.563 184.319 1.00 40.62 O ANISOU 2300 O PHE A 281 6319 5803 3313 813 145 -173 ATOM 2301 CB PHE A 281 -4.822 29.231 181.200 1.00 44.73 C ANISOU 2301 CB PHE A 281 6790 6359 3846 755 87 -151 ATOM 2302 CG PHE A 281 -5.686 30.151 180.386 1.00 51.09 C ANISOU 2302 CG PHE A 281 7611 7200 4599 878 75 -134 ATOM 2303 CD1 PHE A 281 -6.067 31.387 180.883 1.00 56.27 C ANISOU 2303 CD1 PHE A 281 8385 7788 5207 1043 63 -125 ATOM 2304 CD2 PHE A 281 -6.126 29.776 179.126 1.00 52.23 C ANISOU 2304 CD2 PHE A 281 7666 7444 4733 839 73 -128 ATOM 2305 CE1 PHE A 281 -6.864 32.236 180.137 1.00 57.84 C ANISOU 2305 CE1 PHE A 281 8608 8020 5348 1178 49 -107 ATOM 2306 CE2 PHE A 281 -6.923 30.619 178.376 1.00 53.95 C ANISOU 2306 CE2 PHE A 281 7896 7708 4894 966 55 -107 ATOM 2307 CZ PHE A 281 -7.293 31.850 178.882 1.00 55.95 C ANISOU 2307 CZ PHE A 281 8263 7894 5099 1141 43 -94 ATOM 2308 N VAL A 282 -2.975 28.204 183.688 1.00 40.92 N ANISOU 2308 N VAL A 282 6369 5748 3429 630 90 -173 ATOM 2309 CA VAL A 282 -2.634 27.157 184.650 1.00 22.48 C ANISOU 2309 CA VAL A 282 3998 3433 1111 572 114 -180 ATOM 2310 C VAL A 282 -1.549 27.649 185.644 1.00 34.37 C ANISOU 2310 C VAL A 282 5605 4842 2611 597 89 -181 ATOM 2311 O VAL A 282 -1.417 27.082 186.731 1.00 35.85 O ANISOU 2311 O VAL A 282 5808 5039 2775 621 113 -183 ATOM 2312 CB VAL A 282 -2.088 25.889 183.915 1.00 21.54 C ANISOU 2312 CB VAL A 282 3793 3353 1039 439 114 -186 ATOM 2313 CG1 VAL A 282 -2.045 24.632 184.808 1.00 25.65 C ANISOU 2313 CG1 VAL A 282 4290 3892 1564 392 140 -189 ATOM 2314 CG2 VAL A 282 -2.899 25.547 182.648 1.00 24.45 C ANISOU 2314 CG2 VAL A 282 4080 3805 1404 398 134 -192 ATOM 2315 N GLY A 283 -0.802 28.711 185.305 1.00 33.97 N ANISOU 2315 N GLY A 283 5630 4706 2572 580 41 -182 ATOM 2316 CA GLY A 283 0.311 29.208 186.113 1.00 34.13 C ANISOU 2316 CA GLY A 283 5746 4640 2582 575 8 -189 ATOM 2317 C GLY A 283 -0.185 30.195 187.166 1.00 35.46 C ANISOU 2317 C GLY A 283 6055 4723 2694 683 -1 -197 ATOM 2318 O GLY A 283 -0.257 31.402 186.937 1.00 34.66 O ANISOU 2318 O GLY A 283 6038 4562 2569 737 -19 -197 ATOM 2319 N GLU A 284 -0.510 29.675 188.354 1.00 38.44 N ANISOU 2319 N GLU A 284 6472 5092 3040 718 11 -204 ATOM 2320 CA GLU A 284 -0.887 30.458 189.530 1.00 41.29 C ANISOU 2320 CA GLU A 284 6972 5379 3336 827 7 -219 ATOM 2321 C GLU A 284 0.218 31.440 189.976 1.00 40.05 C ANISOU 2321 C GLU A 284 6958 5099 3160 791 -55 -235 ATOM 2322 O GLU A 284 -0.067 32.616 190.205 1.00 40.35 O ANISOU 2322 O GLU A 284 7142 5041 3147 869 -73 -249 ATOM 2323 CB GLU A 284 -1.340 29.503 190.656 1.00 45.08 C ANISOU 2323 CB GLU A 284 7440 5914 3774 870 50 -222 ATOM 2324 CG GLU A 284 -0.331 28.402 191.055 1.00 48.48 C ANISOU 2324 CG GLU A 284 7843 6356 4220 775 34 -217 ATOM 2325 CD GLU A 284 -0.898 27.500 192.144 1.00 54.47 C ANISOU 2325 CD GLU A 284 8615 7163 4920 816 76 -217 ATOM 2326 OE1 GLU A 284 -0.765 27.876 193.328 1.00 56.55 O ANISOU 2326 OE1 GLU A 284 8868 7481 5137 903 130 -220 ATOM 2327 OE2 GLU A 284 -1.464 26.447 191.777 1.00 59.09 O1- ANISOU 2327 OE2 GLU A 284 9218 7740 5494 764 56 -212 ATOM 2328 N ARG A 285 1.470 30.960 190.035 1.00 37.69 N ANISOU 2328 N ARG A 285 6622 4805 2893 674 -91 -234 ATOM 2329 CA ARG A 285 2.608 31.781 190.443 1.00 38.59 C ANISOU 2329 CA ARG A 285 6853 4829 2981 612 -155 -252 ATOM 2330 C ARG A 285 3.024 32.774 189.345 1.00 39.13 C ANISOU 2330 C ARG A 285 6984 4832 3053 580 -183 -250 ATOM 2331 O ARG A 285 3.431 33.882 189.683 1.00 39.55 O ANISOU 2331 O ARG A 285 7193 4775 3058 568 -227 -266 ATOM 2332 CB ARG A 285 3.773 30.903 190.949 1.00 0.00 C ATOM 2333 CG ARG A 285 4.871 31.700 191.682 1.00 0.00 C ATOM 2334 CD ARG A 285 5.991 30.830 192.276 1.00 0.00 C ATOM 2335 NE ARG A 285 6.822 30.203 191.238 1.00 0.00 N ATOM 2336 CZ ARG A 285 7.691 29.197 191.421 1.00 0.00 C ATOM 2337 NH1 ARG A 285 7.884 28.657 192.629 1.00 0.00 N ATOM 2338 NH2 ARG A 285 8.383 28.732 190.378 1.00 0.00 N1+ ATOM 2339 N PHE A 286 2.872 32.412 188.062 1.00 38.72 N ANISOU 2339 N PHE A 286 6819 4845 3047 559 -159 -229 ATOM 2340 CA PHE A 286 3.095 33.344 186.958 1.00 37.20 C ANISOU 2340 CA PHE A 286 6678 4605 2850 523 -180 -219 ATOM 2341 C PHE A 286 2.077 34.493 186.974 1.00 41.15 C ANISOU 2341 C PHE A 286 7334 5003 3298 648 -176 -219 ATOM 2342 O PHE A 286 2.496 35.643 186.935 1.00 42.69 O ANISOU 2342 O PHE A 286 7683 5083 3453 626 -215 -220 ATOM 2343 CB PHE A 286 3.164 32.625 185.604 1.00 33.46 C ANISOU 2343 CB PHE A 286 6043 4243 2427 479 -152 -199 ATOM 2344 CG PHE A 286 3.556 33.517 184.437 1.00 33.03 C ANISOU 2344 CG PHE A 286 6031 4159 2359 429 -172 -183 ATOM 2345 CD1 PHE A 286 4.856 34.057 184.376 1.00 32.46 C ANISOU 2345 CD1 PHE A 286 5978 4075 2281 301 -212 -185 ATOM 2346 CD2 PHE A 286 2.614 33.899 183.459 1.00 32.80 C ANISOU 2346 CD2 PHE A 286 6021 4128 2313 508 -152 -165 ATOM 2347 CE1 PHE A 286 5.217 34.894 183.331 1.00 32.26 C ANISOU 2347 CE1 PHE A 286 5999 4028 2232 244 -226 -165 ATOM 2348 CE2 PHE A 286 3.003 34.715 182.404 1.00 32.44 C ANISOU 2348 CE2 PHE A 286 6027 4054 2244 461 -171 -143 ATOM 2349 CZ PHE A 286 4.300 35.208 182.338 1.00 32.24 C ANISOU 2349 CZ PHE A 286 6029 4010 2212 323 -206 -142 ATOM 2350 N ARG A 287 0.783 34.192 187.164 1.00 41.18 N ANISOU 2350 N ARG A 287 7304 5052 3293 780 -130 -218 ATOM 2351 CA ARG A 287 -0.262 35.204 187.367 1.00 42.30 C ANISOU 2351 CA ARG A 287 7582 5115 3373 936 -123 -221 ATOM 2352 C ARG A 287 0.007 36.149 188.555 1.00 45.57 C ANISOU 2352 C ARG A 287 8198 5391 3724 975 -155 -248 ATOM 2353 O ARG A 287 -0.289 37.339 188.466 1.00 46.92 O ANISOU 2353 O ARG A 287 8552 5436 3837 1061 -176 -253 ATOM 2354 CB ARG A 287 -1.630 34.519 187.513 1.00 40.75 C ANISOU 2354 CB ARG A 287 7275 5036 3171 1066 -63 -216 ATOM 2355 CG ARG A 287 -2.228 34.072 186.169 1.00 38.70 C ANISOU 2355 CG ARG A 287 6859 4897 2949 1055 -38 -193 ATOM 2356 CD ARG A 287 -3.520 33.264 186.342 1.00 37.98 C ANISOU 2356 CD ARG A 287 6677 4923 2830 1189 15 -191 ATOM 2357 NE ARG A 287 -3.238 31.872 186.718 1.00 36.53 N ANISOU 2357 NE ARG A 287 6405 4820 2655 1162 53 -202 ATOM 2358 CZ ARG A 287 -4.119 30.861 186.668 1.00 34.43 C ANISOU 2358 CZ ARG A 287 5983 4661 2438 1047 77 -195 ATOM 2359 NH1 ARG A 287 -5.356 31.045 186.197 1.00 33.18 N ANISOU 2359 NH1 ARG A 287 5732 4548 2328 953 66 -182 ATOM 2360 NH2 ARG A 287 -3.756 29.646 187.083 1.00 33.91 N1+ ANISOU 2360 NH2 ARG A 287 5867 4653 2365 1024 111 -201 ATOM 2361 N LYS A 288 0.615 35.629 189.624 1.00 47.58 N ANISOU 2361 N LYS A 288 8428 5668 3981 913 -163 -267 ATOM 2362 CA LYS A 288 1.044 36.421 190.770 1.00 51.02 C ANISOU 2362 CA LYS A 288 9047 5987 4350 924 -201 -298 ATOM 2363 C LYS A 288 2.214 37.315 190.371 1.00 54.57 C ANISOU 2363 C LYS A 288 9636 6316 4784 800 -268 -304 ATOM 2364 O LYS A 288 2.289 38.474 190.778 1.00 56.16 O ANISOU 2364 O LYS A 288 10051 6371 4915 834 -303 -324 ATOM 2365 CB LYS A 288 1.437 35.511 191.949 1.00 0.00 C ATOM 2366 CG LYS A 288 2.078 36.272 193.114 1.00 0.00 C ATOM 2367 CD LYS A 288 2.527 35.384 194.282 1.00 0.00 C ATOM 2368 CE LYS A 288 3.172 36.128 195.459 1.00 0.00 C ATOM 2369 NZ LYS A 288 3.584 35.230 196.552 1.00 0.00 N1+ ATOM 2370 N TYR A 289 3.183 36.767 189.624 1.00 56.63 N ANISOU 2370 N TYR A 289 9776 6639 5100 652 -286 -286 ATOM 2371 CA TYR A 289 4.297 37.554 189.091 1.00 59.49 C ANISOU 2371 CA TYR A 289 10241 6918 5443 510 -344 -287 ATOM 2372 C TYR A 289 3.810 38.655 188.153 1.00 60.10 C ANISOU 2372 C TYR A 289 10471 6876 5488 562 -348 -268 ATOM 2373 O TYR A 289 4.412 39.724 188.146 1.00 61.61 O ANISOU 2373 O TYR A 289 10903 6894 5611 495 -404 -270 ATOM 2374 CB TYR A 289 5.369 36.672 188.415 1.00 61.55 C ANISOU 2374 CB TYR A 289 10313 7308 5765 361 -351 -272 ATOM 2375 CG TYR A 289 6.270 35.909 189.372 1.00 63.51 C ANISOU 2375 CG TYR A 289 10433 7664 6035 308 -361 -289 ATOM 2376 CD1 TYR A 289 6.833 36.560 190.493 1.00 65.32 C ANISOU 2376 CD1 TYR A 289 10753 7851 6214 334 -386 -319 ATOM 2377 CD2 TYR A 289 6.548 34.544 189.151 1.00 63.19 C ANISOU 2377 CD2 TYR A 289 10189 7766 6052 240 -346 -274 ATOM 2378 CE1 TYR A 289 7.565 35.830 191.443 1.00 65.86 C ANISOU 2378 CE1 TYR A 289 10712 8020 6290 293 -400 -330 ATOM 2379 CE2 TYR A 289 7.310 33.821 190.087 1.00 63.56 C ANISOU 2379 CE2 TYR A 289 10136 7905 6110 208 -359 -286 ATOM 2380 CZ TYR A 289 7.770 34.452 191.258 1.00 65.09 C ANISOU 2380 CZ TYR A 289 10421 8056 6252 234 -387 -311 ATOM 2381 OH TYR A 289 8.402 33.728 192.222 1.00 65.86 O ANISOU 2381 OH TYR A 289 10427 8247 6349 209 -405 -318 ATOM 2382 N LEU A 290 2.680 38.430 187.470 1.00 59.63 N ANISOU 2382 N LEU A 290 10337 6869 5450 690 -298 -246 ATOM 2383 CA LEU A 290 2.094 39.441 186.598 1.00 61.52 C ANISOU 2383 CA LEU A 290 10761 6978 5635 791 -304 -223 ATOM 2384 C LEU A 290 1.423 40.538 187.415 1.00 63.61 C ANISOU 2384 C LEU A 290 11314 7054 5802 970 -320 -241 ATOM 2385 O LEU A 290 1.393 41.700 187.011 1.00 65.12 O ANISOU 2385 O LEU A 290 11793 7039 5911 1028 -357 -229 ATOM 2386 CB LEU A 290 1.082 38.807 185.642 1.00 60.61 C ANISOU 2386 CB LEU A 290 10449 7013 5567 878 -249 -197 ATOM 2387 CG LEU A 290 1.643 37.871 184.571 1.00 59.35 C ANISOU 2387 CG LEU A 290 10067 7007 5478 729 -237 -173 ATOM 2388 CD1 LEU A 290 0.517 37.215 183.783 1.00 58.50 C ANISOU 2388 CD1 LEU A 290 9794 7035 5396 827 -189 -153 ATOM 2389 CD2 LEU A 290 2.582 38.628 183.644 1.00 59.71 C ANISOU 2389 CD2 LEU A 290 10236 6959 5491 604 -279 -150 ATOM 2390 N ARG A 291 0.883 40.157 188.568 1.00 64.25 N ANISOU 2390 N ARG A 291 11330 7200 5881 1061 -292 -269 ATOM 2391 CA ARG A 291 0.195 41.098 189.441 1.00 66.76 C ANISOU 2391 CA ARG A 291 11896 7372 6098 1250 -299 -290 ATOM 2392 C ARG A 291 1.169 42.096 190.050 1.00 70.00 C ANISOU 2392 C ARG A 291 12598 7570 6429 1159 -372 -312 ATOM 2393 O ARG A 291 0.832 43.261 190.249 1.00 72.08 O ANISOU 2393 O ARG A 291 13172 7627 6586 1289 -402 -314 ATOM 2394 CB ARG A 291 -0.555 40.350 190.559 1.00 0.00 C ATOM 2395 CG ARG A 291 -1.425 41.145 191.558 1.00 0.00 C ATOM 2396 CD ARG A 291 -2.163 40.388 192.662 1.00 0.00 C ATOM 2397 NE ARG A 291 -2.943 41.282 193.525 1.00 0.00 N ATOM 2398 CZ ARG A 291 -2.465 41.894 194.623 1.00 0.00 C ATOM 2399 NH1 ARG A 291 -1.201 41.662 195.039 1.00 0.00 N ATOM 2400 NH2 ARG A 291 -3.280 42.731 195.297 1.00 0.00 N1+ ATOM 2401 N GLN A 292 2.378 41.635 190.349 1.00 71.03 N ANISOU 2401 N GLN A 292 12634 7754 6601 937 -405 -327 ATOM 2402 CA GLN A 292 3.387 42.514 190.924 1.00 73.86 C ANISOU 2402 CA GLN A 292 13245 7937 6881 812 -481 -350 ATOM 2403 C GLN A 292 4.145 43.252 189.822 1.00 74.21 C ANISOU 2403 C GLN A 292 13469 7829 6897 671 -533 -316 ATOM 2404 O GLN A 292 4.857 44.219 190.089 1.00 76.56 O ANISOU 2404 O GLN A 292 14047 7934 7107 563 -601 -324 ATOM 2405 CB GLN A 292 4.379 41.741 191.813 1.00 0.00 C ATOM 2406 CG GLN A 292 5.765 42.362 192.053 1.00 0.00 C ATOM 2407 CD GLN A 292 6.688 41.540 192.941 1.00 0.00 C ATOM 2408 OE1 GLN A 292 7.443 40.699 192.466 1.00 0.00 O ATOM 2409 NE2 GLN A 292 6.633 41.770 194.249 1.00 0.00 N ATOM 2410 N LEU A 293 3.983 42.799 188.582 1.00 72.33 N ANISOU 2410 N LEU A 293 13078 7681 6725 656 -499 -277 ATOM 2411 CA LEU A 293 4.612 43.466 187.448 1.00 72.42 C ANISOU 2411 CA LEU A 293 13255 7560 6701 522 -538 -240 ATOM 2412 C LEU A 293 3.796 44.683 187.033 1.00 72.99 C ANISOU 2412 C LEU A 293 13677 7384 6673 695 -552 -215 ATOM 2413 O LEU A 293 4.332 45.651 186.494 1.00 74.46 O ANISOU 2413 O LEU A 293 14160 7353 6777 588 -606 -187 ATOM 2414 CB LEU A 293 4.765 42.496 186.261 1.00 0.00 C ATOM 2415 CG LEU A 293 5.758 42.592 185.005 1.00 0.00 C ATOM 2416 CD1 LEU A 293 5.715 41.360 184.104 1.00 0.00 C ATOM 2417 CD2 LEU A 293 5.436 43.751 184.136 1.00 0.00 C ATOM 2418 N PHE A 294 2.494 44.621 187.295 1.00 71.65 N ANISOU 2418 N PHE A 294 13479 7248 6498 966 -505 -222 ATOM 2419 CA PHE A 294 1.574 45.692 186.934 1.00 72.15 C ANISOU 2419 CA PHE A 294 13853 7102 6457 1198 -514 -200 ATOM 2420 C PHE A 294 0.818 46.203 188.157 1.00 72.82 C ANISOU 2420 C PHE A 294 14102 7108 6459 1420 -514 -225 ATOM 2421 O PHE A 294 1.183 47.218 188.749 1.00 74.79 O ANISOU 2421 O PHE A 294 14690 7132 6595 1404 -573 -228 ATOM 2422 CB PHE A 294 0.586 45.209 185.870 1.00 71.07 C ANISOU 2422 CB PHE A 294 13522 7112 6369 1358 -456 -178 ATOM 2423 CG PHE A 294 1.244 44.677 184.627 1.00 69.69 C ANISOU 2423 CG PHE A 294 13164 7051 6265 1152 -450 -151 ATOM 2424 CD1 PHE A 294 2.335 45.327 184.073 1.00 70.81 C ANISOU 2424 CD1 PHE A 294 13518 7025 6361 933 -506 -130 ATOM 2425 CD2 PHE A 294 0.773 43.526 184.014 1.00 67.54 C ANISOU 2425 CD2 PHE A 294 12511 7060 6092 1164 -391 -142 ATOM 2426 CE1 PHE A 294 2.943 44.841 182.931 1.00 69.65 C ANISOU 2426 CE1 PHE A 294 13190 7008 6265 746 -497 -99 ATOM 2427 CE2 PHE A 294 1.378 43.035 182.871 1.00 66.28 C ANISOU 2427 CE2 PHE A 294 12179 7020 5984 983 -386 -110 ATOM 2428 CZ PHE A 294 2.465 43.694 182.330 1.00 67.36 C ANISOU 2428 CZ PHE A 294 12513 7007 6074 783 -436 -88 TER 2429 PHE A 294 HETATM 2430 C1 UNK Z 999 3.755 26.022 191.124 1.00 0.00 C HETATM 2431 C2 UNK Z 999 4.965 26.574 190.379 1.00 0.00 C HETATM 2432 O1 UNK Z 999 6.087 26.263 190.782 1.00 0.00 O HETATM 2433 C3 UNK Z 999 4.758 27.454 189.221 1.00 0.00 C HETATM 2434 C4 UNK Z 999 3.666 28.147 188.849 1.00 0.00 C HETATM 2435 C5 UNK Z 999 3.949 29.022 187.722 1.00 0.00 C HETATM 2436 O2 UNK Z 999 3.194 29.816 187.155 1.00 0.00 O HETATM 2437 N1 UNK Z 999 5.271 28.856 187.468 1.00 0.00 N HETATM 2438 C6 UNK Z 999 5.817 27.686 188.167 1.00 0.00 C HETATM 2439 C7 UNK Z 999 6.084 26.409 187.276 1.00 0.00 C HETATM 2440 C8 UNK Z 999 6.214 26.642 185.744 1.00 0.00 C HETATM 2441 C9 UNK Z 999 6.469 25.347 184.945 1.00 0.00 C HETATM 2442 C10 UNK Z 999 7.690 24.580 185.478 1.00 0.00 C HETATM 2443 C11 UNK Z 999 7.546 24.300 186.982 1.00 0.00 C HETATM 2444 C12 UNK Z 999 7.306 25.595 187.782 1.00 0.00 C HETATM 2445 C13 UNK Z 999 6.001 29.760 186.669 1.00 0.00 C HETATM 2446 C14 UNK Z 999 5.774 29.848 185.288 1.00 0.00 C HETATM 2447 C15 UNK Z 999 6.451 30.795 184.521 1.00 0.00 C HETATM 2448 C16 UNK Z 999 7.329 31.684 185.134 1.00 0.00 C HETATM 2449 C17 UNK Z 999 7.553 31.615 186.506 1.00 0.00 C HETATM 2450 C18 UNK Z 999 6.889 30.662 187.274 1.00 0.00 C HETATM 2451 F1 UNK Z 999 7.086 30.658 188.611 1.00 0.00 F HETATM 2452 CL1 UNK Z 999 8.094 32.917 184.212 1.00 0.00 Cl HETATM 2453 O3 UNK Z 999 2.503 28.236 189.408 1.00 0.00 O1- CONECT 680 1307 CONECT 1307 680 CONECT 2430 2431 CONECT 2431 2430 2432 2433 CONECT 2431 2432 CONECT 2432 2431 CONECT 2432 2431 CONECT 2433 2431 2434 2438 CONECT 2433 2434 CONECT 2434 2433 2435 2453 CONECT 2434 2433 CONECT 2435 2434 2436 2437 CONECT 2435 2436 CONECT 2436 2435 CONECT 2436 2435 CONECT 2437 2435 2438 2445 CONECT 2438 2433 2437 2439 CONECT 2439 2438 2440 2444 CONECT 2440 2439 2441 CONECT 2441 2440 2442 CONECT 2442 2441 2443 CONECT 2443 2442 2444 CONECT 2444 2439 2443 CONECT 2445 2437 2446 2450 CONECT 2445 2446 CONECT 2446 2445 2447 CONECT 2446 2445 CONECT 2447 2446 2448 CONECT 2447 2448 CONECT 2448 2447 2449 2452 CONECT 2448 2447 CONECT 2449 2448 2450 CONECT 2449 2450 CONECT 2450 2445 2449 2451 CONECT 2450 2449 CONECT 2451 2450 CONECT 2452 2448 CONECT 2453 2434 ENDMDL END