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CCR5.pdb
executable file
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CCR5.pdb
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TITLE CCR5 with ligand maraviroc _4MBS Processed 2013-09-11 10:26
ATOM 1 N PRO A 19 -7.860 -1.819 69.502 1.00138.31 N
ANISOU 1 N PRO A 19 18527 21599 12425 -919 -209 -127 N
ATOM 2 CA PRO A 19 -9.053 -1.020 69.190 1.00138.99 C
ANISOU 2 CA PRO A 19 18827 21554 12427 -1124 -74 77 C
ATOM 3 C PRO A 19 -10.206 -1.294 70.163 1.00144.31 C
ANISOU 3 C PRO A 19 19555 22419 12856 -1355 136 86 C
ATOM 4 O PRO A 19 -9.977 -1.840 71.251 1.00144.78 O
ANISOU 4 O PRO A 19 19560 22704 12744 -1319 143 -29 O
ATOM 5 CB PRO A 19 -9.391 -1.444 67.758 1.00138.04 C
ANISOU 5 CB PRO A 19 18501 21303 12647 -1184 -9 23 C
ATOM 6 CG PRO A 19 -8.072 -1.859 67.165 1.00140.40 C
ANISOU 6 CG PRO A 19 18613 21557 13175 -951 -184 -107 C
ATOM 7 CD PRO A 19 -7.114 -2.186 68.285 1.00137.06 C
ANISOU 7 CD PRO A 19 18161 21313 12604 -798 -300 -221 C
ATOM 8 N CYS A 20 -11.441 -0.883 69.784 1.00140.99 N
ANISOU 8 N CYS A 20 19241 21920 12410 -1599 310 213 N
ATOM 9 CA CYS A 20 -12.648 -1.064 70.596 1.00142.63 C
ANISOU 9 CA CYS A 20 19492 22313 12389 -1860 539 225 C
ATOM 10 C CYS A 20 -13.165 -2.502 70.481 1.00147.05 C
ANISOU 10 C CYS A 20 19664 23094 13114 -1932 690 -34 C
ATOM 11 O CYS A 20 -12.869 -3.182 69.490 1.00144.04 O
ANISOU 11 O CYS A 20 19031 22647 13050 -1838 645 -164 O
ATOM 12 CB CYS A 20 -13.726 -0.057 70.199 1.00143.49 C
ANISOU 12 CB CYS A 20 19847 22252 12419 -2110 669 441 C
ATOM 13 SG CYS A 20 -15.196 -0.096 71.262 1.00150.18 S
ANISOU 13 SG CYS A 20 20788 23335 12939 -2469 965 478 S
ATOM 14 N GLN A 21 -13.953 -2.949 71.495 1.00146.77 N
ANISOU 14 N GLN A 21 19593 23319 12854 -2094 868 -108 N
ATOM 15 CA GLN A 21 -14.579 -4.277 71.563 1.00146.30 C
ANISOU 15 CA GLN A 21 19184 23497 12905 -2163 1024 -364 C
ATOM 16 C GLN A 21 -15.527 -4.459 70.356 1.00149.19 C
ANISOU 16 C GLN A 21 19385 23784 13515 -2317 1148 -385 C
ATOM 17 O GLN A 21 -16.706 -4.079 70.408 1.00150.65 O
ANISOU 17 O GLN A 21 19636 24027 13579 -2582 1338 -311 O
ATOM 18 CB GLN A 21 -15.314 -4.465 72.905 1.00150.59 C
ANISOU 18 CB GLN A 21 19767 24337 13114 -2326 1202 -413 C
ATOM 19 N LYS A 22 -14.966 -4.993 69.246 1.00142.32 N
ANISOU 19 N LYS A 22 18316 22777 12982 -2153 1033 -479 N
ATOM 20 CA LYS A 22 -15.650 -5.222 67.971 1.00140.31 C
ANISOU 20 CA LYS A 22 17895 22431 12987 -2238 1099 -511 C
ATOM 21 C LYS A 22 -16.738 -6.308 68.082 1.00143.66 C
ANISOU 21 C LYS A 22 18023 23112 13448 -2364 1293 -727 C
ATOM 22 O LYS A 22 -16.736 -7.106 69.026 1.00144.28 O
ANISOU 22 O LYS A 22 17982 23425 13415 -2328 1348 -892 O
ATOM 23 CB LYS A 22 -14.629 -5.605 66.884 1.00139.73 C
ANISOU 23 CB LYS A 22 17696 22167 13228 -2004 916 -564 C
ATOM 24 N ILE A 23 -17.672 -6.321 67.111 1.00138.34 N
ANISOU 24 N ILE A 23 17227 22406 12928 -2503 1389 -740 N
ATOM 25 CA ILE A 23 -18.761 -7.296 67.060 1.00137.97 C
ANISOU 25 CA ILE A 23 16878 22606 12940 -2609 1559 -956 C
ATOM 26 C ILE A 23 -18.275 -8.602 66.422 1.00136.47 C
ANISOU 26 C ILE A 23 16398 22419 13036 -2364 1458 -1172 C
ATOM 27 O ILE A 23 -17.382 -8.575 65.567 1.00133.02 O
ANISOU 27 O ILE A 23 15986 21751 12804 -2192 1290 -1119 O
ATOM 28 CB ILE A 23 -19.972 -6.716 66.296 1.00142.03 C
ANISOU 28 CB ILE A 23 17381 23098 13484 -2868 1698 -888 C
ATOM 29 N ASN A 24 -18.862 -9.745 66.845 1.00131.93 N
ANISOU 29 N ASN A 24 15558 22105 12464 -2347 1562 -1419 N
ATOM 30 CA ASN A 24 -18.515 -11.063 66.311 1.00128.75 C
ANISOU 30 CA ASN A 24 14897 21706 12317 -2116 1477 -1636 C
ATOM 31 C ASN A 24 -19.371 -11.350 65.069 1.00128.21 C
ANISOU 31 C ASN A 24 14632 21622 12459 -2154 1514 -1698 C
ATOM 32 O ASN A 24 -20.553 -11.714 65.175 1.00129.48 O
ANISOU 32 O ASN A 24 14600 22019 12576 -2285 1672 -1839 O
ATOM 33 CB ASN A 24 -18.649 -12.165 67.383 1.00130.82 C
ANISOU 33 CB ASN A 24 14986 22235 12486 -2040 1545 -1885 C
ATOM 34 CG ASN A 24 -18.408 -13.572 66.877 1.00149.40 C
ANISOU 34 CG ASN A 24 17085 24586 15093 -1808 1470 -2122 C
ATOM 35 ND2 ASN A 24 -17.150 -13.950 66.688 1.00135.38 N
ANISOU 35 ND2 ASN A 24 15363 22616 13461 -1596 1297 -2127 N
ATOM 36 OD1 ASN A 24 -19.344 -14.343 66.661 1.00147.57 O
ANISOU 36 OD1 ASN A 24 16612 24529 14928 -1815 1565 -2309 O
ATOM 37 N VAL A 25 -18.763 -11.129 63.890 1.00118.85 N
ANISOU 37 N VAL A 25 13498 20172 11489 -2044 1369 -1594 N
ATOM 38 CA VAL A 25 -19.364 -11.357 62.576 1.00115.99 C
ANISOU 38 CA VAL A 25 12979 19754 11338 -2041 1361 -1634 C
ATOM 39 C VAL A 25 -18.840 -12.685 62.014 1.00114.98 C
ANISOU 39 C VAL A 25 12663 19581 11443 -1770 1244 -1808 C
ATOM 40 O VAL A 25 -19.218 -13.070 60.908 1.00114.24 O
ANISOU 40 O VAL A 25 12434 19440 11533 -1711 1208 -1859 O
ATOM 41 CB VAL A 25 -19.154 -10.171 61.581 1.00118.27 C
ANISOU 41 CB VAL A 25 13462 19784 11690 -2118 1290 -1402 C
ATOM 42 CG1 VAL A 25 -20.005 -8.965 61.966 1.00120.09 C
ANISOU 42 CG1 VAL A 25 13853 20060 11715 -2416 1431 -1258 C
ATOM 43 CG2 VAL A 25 -17.681 -9.784 61.442 1.00115.89 C
ANISOU 43 CG2 VAL A 25 13363 19229 11441 -1950 1113 -1259 C
ATOM 44 N LYS A 26 -17.982 -13.384 62.790 1.00108.20 N
ANISOU 44 N LYS A 26 11810 18734 10567 -1610 1184 -1901 N
ATOM 45 CA LYS A 26 -17.367 -14.664 62.430 1.00105.30 C
ANISOU 45 CA LYS A 26 11313 18295 10400 -1361 1075 -2062 C
ATOM 46 C LYS A 26 -18.420 -15.771 62.305 1.00106.76 C
ANISOU 46 C LYS A 26 11225 18683 10656 -1303 1150 -2304 C
ATOM 47 O LYS A 26 -18.301 -16.620 61.420 1.00105.75 O
ANISOU 47 O LYS A 26 10992 18453 10735 -1124 1058 -2389 O
ATOM 48 CB LYS A 26 -16.295 -15.056 63.458 1.00107.77 C
ANISOU 48 CB LYS A 26 11706 18597 10646 -1250 1014 -2120 C
ATOM 49 N GLN A 27 -19.463 -15.740 63.162 1.00102.15 N
ANISOU 49 N GLN A 27 10529 18391 9892 -1452 1314 -2414 N
ATOM 50 CA GLN A 27 -20.561 -16.715 63.136 1.00101.89 C
ANISOU 50 CA GLN A 27 10208 18605 9902 -1404 1398 -2670 C
ATOM 51 C GLN A 27 -21.408 -16.539 61.874 1.00 99.67 C
ANISOU 51 C GLN A 27 9804 18312 9754 -1450 1399 -2652 C
ATOM 52 O GLN A 27 -21.883 -17.525 61.313 1.00 99.62 O
ANISOU 52 O GLN A 27 9583 18374 9893 -1285 1360 -2839 O
ATOM 53 CB GLN A 27 -21.437 -16.588 64.393 1.00106.33 C
ANISOU 53 CB GLN A 27 10683 19505 10212 -1587 1594 -2785 C
ATOM 54 CG GLN A 27 -21.750 -17.920 65.073 1.00128.02 C
ANISOU 54 CG GLN A 27 13201 22480 12961 -1419 1630 -3099 C
ATOM 55 CD GLN A 27 -22.866 -18.693 64.403 1.00150.42 C
ANISOU 55 CD GLN A 27 15734 25497 15923 -1344 1666 -3318 C
ATOM 56 NE2 GLN A 27 -24.060 -18.646 64.984 1.00143.28 N
ANISOU 56 NE2 GLN A 27 14633 24946 14860 -1513 1855 -3471 N
ATOM 57 OE1 GLN A 27 -22.666 -19.375 63.391 1.00145.12 O
ANISOU 57 OE1 GLN A 27 14994 24665 15481 -1127 1525 -3366 O
ATOM 58 N ILE A 28 -21.567 -15.286 61.418 1.00 91.31 N
ANISOU 58 N ILE A 28 8892 17156 8643 -1662 1429 -2432 N
ATOM 59 CA ILE A 28 -22.289 -14.926 60.198 1.00 88.66 C
ANISOU 59 CA ILE A 28 8476 16787 8422 -1737 1423 -2391 C
ATOM 60 C ILE A 28 -21.441 -15.325 58.981 1.00 86.05 C
ANISOU 60 C ILE A 28 8194 16175 8326 -1502 1228 -2330 C
ATOM 61 O ILE A 28 -21.949 -16.008 58.096 1.00 86.19 O
ANISOU 61 O ILE A 28 8029 16229 8489 -1380 1178 -2453 O
ATOM 62 CB ILE A 28 -22.629 -13.407 60.212 1.00 91.85 C
ANISOU 62 CB ILE A 28 9071 17144 8684 -2045 1516 -2170 C
ATOM 63 CG1 ILE A 28 -23.811 -13.125 61.141 1.00 94.80 C
ANISOU 63 CG1 ILE A 28 9344 17832 8843 -2314 1737 -2258 C
ATOM 64 CG2 ILE A 28 -22.890 -12.843 58.809 1.00 91.51 C
ANISOU 64 CG2 ILE A 28 9043 16942 8786 -2091 1452 -2066 C
ATOM 65 CD1 ILE A 28 -23.547 -12.099 62.176 1.00101.19 C
ANISOU 65 CD1 ILE A 28 10403 18635 9410 -2488 1822 -2100 C
ATOM 66 N ALA A 29 -20.147 -14.926 58.972 1.00 77.09 N
ANISOU 66 N ALA A 29 7299 14778 7213 -1435 1119 -2152 N
ATOM 67 CA ALA A 29 -19.172 -15.151 57.902 1.00 73.03 C
ANISOU 67 CA ALA A 29 6872 13986 6891 -1251 951 -2063 C
ATOM 68 C ALA A 29 -18.964 -16.630 57.594 1.00 73.77 C
ANISOU 68 C ALA A 29 6823 14064 7143 -986 864 -2246 C
ATOM 69 O ALA A 29 -18.773 -16.977 56.424 1.00 72.91 O
ANISOU 69 O ALA A 29 6701 13805 7196 -855 758 -2222 O
ATOM 70 CB ALA A 29 -17.843 -14.505 58.258 1.00 72.18 C
ANISOU 70 CB ALA A 29 7014 13670 6742 -1244 878 -1884 C
ATOM 71 N ALA A 30 -19.040 -17.497 58.627 1.00 69.04 N
ANISOU 71 N ALA A 30 6126 13619 6487 -906 908 -2432 N
ATOM 72 CA ALA A 30 -18.915 -18.956 58.523 1.00 68.68 C
ANISOU 72 CA ALA A 30 5957 13564 6574 -649 833 -2633 C
ATOM 73 C ALA A 30 -20.075 -19.579 57.712 1.00 73.11 C
ANISOU 73 C ALA A 30 6287 14264 7226 -561 831 -2784 C
ATOM 74 O ALA A 30 -19.905 -20.642 57.115 1.00 72.58 O
ANISOU 74 O ALA A 30 6170 14098 7311 -320 720 -2883 O
ATOM 75 CB ALA A 30 -18.871 -19.574 59.911 1.00 70.72 C
ANISOU 75 CB ALA A 30 6160 13989 6721 -615 900 -2811 C
ATOM 76 N ARG A 31 -21.244 -18.917 57.697 1.00 70.26 N
ANISOU 76 N ARG A 31 5794 14132 6769 -758 951 -2805 N
ATOM 77 CA ARG A 31 -22.423 -19.372 56.956 1.00 71.59 C
ANISOU 77 CA ARG A 31 5715 14480 7007 -704 955 -2964 C
ATOM 78 C ARG A 31 -22.531 -18.700 55.582 1.00 73.63 C
ANISOU 78 C ARG A 31 6024 14596 7355 -759 885 -2805 C
ATOM 79 O ARG A 31 -22.972 -19.340 54.630 1.00 73.73 O
ANISOU 79 O ARG A 31 5899 14626 7488 -596 796 -2902 O
ATOM 80 CB ARG A 31 -23.718 -19.097 57.755 1.00 74.98 C
ANISOU 80 CB ARG A 31 5930 15285 7275 -911 1144 -3120 C
ATOM 81 CG ARG A 31 -23.786 -19.768 59.128 1.00 88.01 C
ANISOU 81 CG ARG A 31 7494 17134 8812 -865 1233 -3311 C
ATOM 82 CD ARG A 31 -24.687 -20.989 59.133 1.00106.27 C
ANISOU 82 CD ARG A 31 9495 19702 11181 -667 1234 -3632 C
ATOM 83 NE ARG A 31 -24.619 -21.712 60.407 1.00126.41 N
ANISOU 83 NE ARG A 31 11978 22415 13636 -585 1301 -3827 N
ATOM 84 CZ ARG A 31 -25.582 -22.501 60.892 1.00146.55 C
ANISOU 84 CZ ARG A 31 14240 25294 16148 -502 1378 -4131 C
ATOM 85 NH1 ARG A 31 -26.716 -22.668 60.221 1.00138.84 N1+
ANISOU 85 NH1 ARG A 31 12995 24537 15218 -493 1398 -4281 N1+
ATOM 86 NH2 ARG A 31 -25.421 -23.115 62.056 1.00133.12 N
ANISOU 86 NH2 ARG A 31 12503 23721 14356 -426 1435 -4303 N
ATOM 87 N LEU A 32 -22.164 -17.412 55.491 1.00 69.04 N
ANISOU 87 N LEU A 32 5641 13885 6708 -978 919 -2573 N
ATOM 88 CA LEU A 32 -22.320 -16.617 54.280 1.00 68.67 C
ANISOU 88 CA LEU A 32 5649 13718 6723 -1066 872 -2430 C
ATOM 89 C LEU A 32 -21.147 -16.714 53.289 1.00 71.00 C
ANISOU 89 C LEU A 32 6128 13690 7158 -893 706 -2274 C
ATOM 90 O LEU A 32 -21.415 -16.801 52.090 1.00 70.70 O
ANISOU 90 O LEU A 32 6042 13601 7221 -824 625 -2265 O
ATOM 91 CB LEU A 32 -22.566 -15.140 54.644 1.00 69.19 C
ANISOU 91 CB LEU A 32 5849 13796 6645 -1388 993 -2267 C
ATOM 92 CG LEU A 32 -23.102 -14.249 53.516 1.00 74.25 C
ANISOU 92 CG LEU A 32 6507 14379 7327 -1537 983 -2168 C
ATOM 93 CD1 LEU A 32 -24.574 -13.923 53.726 1.00 77.19 C
ANISOU 93 CD1 LEU A 32 6658 15050 7619 -1760 1131 -2314 C
ATOM 94 CD2 LEU A 32 -22.289 -12.978 53.398 1.00 75.97 C
ANISOU 94 CD2 LEU A 32 7019 14358 7486 -1689 978 -1911 C
ATOM 95 N LEU A 33 -19.879 -16.657 53.749 1.00 65.50 N
ANISOU 95 N LEU A 33 5634 12794 6460 -838 660 -2157 N
ATOM 96 CA LEU A 33 -18.754 -16.645 52.808 1.00 63.07 C
ANISOU 96 CA LEU A 33 5495 12198 6272 -714 525 -2009 C
ATOM 97 C LEU A 33 -18.520 -17.987 52.062 1.00 65.48 C
ANISOU 97 C LEU A 33 5737 12415 6726 -441 405 -2108 C
ATOM 98 O LEU A 33 -18.285 -17.919 50.856 1.00 62.88 O
ANISOU 98 O LEU A 33 5464 11941 6487 -375 315 -2018 O
ATOM 99 CB LEU A 33 -17.440 -16.174 53.461 1.00 62.25 C
ANISOU 99 CB LEU A 33 5605 11921 6125 -741 508 -1870 C
ATOM 100 CG LEU A 33 -17.434 -14.770 54.103 1.00 67.51 C
ANISOU 100 CG LEU A 33 6402 12607 6640 -972 589 -1728 C
ATOM 101 CD1 LEU A 33 -16.138 -14.514 54.810 1.00 66.38 C
ANISOU 101 CD1 LEU A 33 6435 12329 6457 -945 549 -1637 C
ATOM 102 CD2 LEU A 33 -17.683 -13.654 53.072 1.00 69.80 C
ANISOU 102 CD2 LEU A 33 6772 12802 6946 -1095 575 -1577 C
ATOM 103 N PRO A 34 -18.562 -19.196 52.689 1.00 63.71 N
ANISOU 103 N PRO A 34 5421 12258 6529 -272 394 -2287 N
ATOM 104 CA PRO A 34 -18.304 -20.422 51.906 1.00 63.50 C
ANISOU 104 CA PRO A 34 5386 12100 6641 -6 266 -2356 C
ATOM 105 C PRO A 34 -19.162 -20.576 50.635 1.00 67.58 C
ANISOU 105 C PRO A 34 5786 12672 7220 77 199 -2386 C
ATOM 106 O PRO A 34 -18.527 -20.794 49.601 1.00 66.21 O
ANISOU 106 O PRO A 34 5739 12284 7135 190 90 -2276 O
ATOM 107 CB PRO A 34 -18.567 -21.553 52.905 1.00 66.64 C
ANISOU 107 CB PRO A 34 5669 12620 7033 137 286 -2581 C
ATOM 108 CG PRO A 34 -18.284 -20.933 54.223 1.00 70.60 C
ANISOU 108 CG PRO A 34 6213 13207 7405 -43 400 -2567 C
ATOM 109 CD PRO A 34 -18.780 -19.524 54.118 1.00 65.95 C
ANISOU 109 CD PRO A 34 5629 12716 6712 -303 489 -2432 C
ATOM 110 N PRO A 35 -20.528 -20.429 50.612 1.00 64.61 N
ANISOU 110 N PRO A 35 5179 12575 6796 13 258 -2525 N
ATOM 111 CA PRO A 35 -21.250 -20.592 49.332 1.00 64.68 C
ANISOU 111 CA PRO A 35 5077 12632 6866 108 171 -2560 C
ATOM 112 C PRO A 35 -20.878 -19.533 48.291 1.00 67.33 C
ANISOU 112 C PRO A 35 5559 12808 7214 -21 138 -2345 C
ATOM 113 O PRO A 35 -20.725 -19.863 47.107 1.00 65.75 O
ANISOU 113 O PRO A 35 5404 12489 7089 131 15 -2298 O
ATOM 114 CB PRO A 35 -22.725 -20.475 49.734 1.00 68.35 C
ANISOU 114 CB PRO A 35 5254 13456 7259 1 272 -2761 C
ATOM 115 CG PRO A 35 -22.749 -20.734 51.189 1.00 73.69 C
ANISOU 115 CG PRO A 35 5879 14263 7857 -46 385 -2874 C
ATOM 116 CD PRO A 35 -21.478 -20.157 51.710 1.00 67.10 C
ANISOU 116 CD PRO A 35 5314 13189 6993 -147 407 -2670 C
ATOM 117 N LEU A 36 -20.704 -18.275 48.744 1.00 64.57 N
ANISOU 117 N LEU A 36 5301 12450 6783 -287 242 -2214 N
ATOM 118 CA LEU A 36 -20.328 -17.153 47.882 1.00 63.60 C
ANISOU 118 CA LEU A 36 5328 12174 6664 -420 220 -2020 C
ATOM 119 C LEU A 36 -18.993 -17.439 47.177 1.00 64.08 C
ANISOU 119 C LEU A 36 5596 11945 6806 -268 107 -1873 C
ATOM 120 O LEU A 36 -18.938 -17.377 45.950 1.00 63.17 O
ANISOU 120 O LEU A 36 5518 11741 6743 -202 20 -1810 O
ATOM 121 CB LEU A 36 -20.261 -15.831 48.688 1.00 63.64 C
ANISOU 121 CB LEU A 36 5432 12189 6559 -701 344 -1908 C
ATOM 122 CG LEU A 36 -19.789 -14.571 47.926 1.00 67.19 C
ANISOU 122 CG LEU A 36 6063 12459 7008 -831 320 -1709 C
ATOM 123 CD1 LEU A 36 -20.840 -14.086 46.923 1.00 68.25 C
ANISOU 123 CD1 LEU A 36 6086 12690 7156 -923 314 -1748 C
ATOM 124 CD2 LEU A 36 -19.440 -13.462 48.889 1.00 68.99 C
ANISOU 124 CD2 LEU A 36 6443 12645 7127 -1038 414 -1589 C
ATOM 125 N TYR A 37 -17.959 -17.812 47.953 1.00 58.90 N
ANISOU 125 N TYR A 37 5062 11161 6155 -215 111 -1838 N
ATOM 126 CA TYR A 37 -16.602 -18.102 47.484 1.00 57.35 C
ANISOU 126 CA TYR A 37 5059 10702 6030 -107 30 -1713 C
ATOM 127 C TYR A 37 -16.590 -19.306 46.540 1.00 62.87 C
ANISOU 127 C TYR A 37 5750 11318 6821 134 -84 -1763 C
ATOM 128 O TYR A 37 -15.869 -19.281 45.542 1.00 63.46 O
ANISOU 128 O TYR A 37 5960 11210 6941 188 -155 -1638 O
ATOM 129 CB TYR A 37 -15.643 -18.321 48.667 1.00 57.72 C
ANISOU 129 CB TYR A 37 5199 10675 6057 -119 67 -1710 C
ATOM 130 CG TYR A 37 -15.272 -17.082 49.459 1.00 58.76 C
ANISOU 130 CG TYR A 37 5413 10821 6092 -324 145 -1609 C
ATOM 131 CD1 TYR A 37 -16.051 -15.925 49.396 1.00 60.70 C
ANISOU 131 CD1 TYR A 37 5628 11175 6258 -505 207 -1557 C
ATOM 132 CD2 TYR A 37 -14.181 -17.088 50.329 1.00 59.34 C
ANISOU 132 CD2 TYR A 37 5596 10805 6145 -335 154 -1578 C
ATOM 133 CE1 TYR A 37 -15.739 -14.798 50.152 1.00 61.04 C
ANISOU 133 CE1 TYR A 37 5778 11215 6200 -676 269 -1457 C
ATOM 134 CE2 TYR A 37 -13.871 -15.973 51.110 1.00 59.73 C
ANISOU 134 CE2 TYR A 37 5725 10880 6089 -495 209 -1492 C
ATOM 135 CZ TYR A 37 -14.649 -14.825 51.008 1.00 66.52 C
ANISOU 135 CZ TYR A 37 6581 11827 6866 -657 263 -1423 C
ATOM 136 OH TYR A 37 -14.366 -13.698 51.740 1.00 65.35 O
ANISOU 136 OH TYR A 37 6546 11681 6604 -801 306 -1323 O
ATOM 137 N SER A 38 -17.419 -20.323 46.820 1.00 60.63 N
ANISOU 137 N SER A 38 5309 11174 6552 282 -104 -1948 N
ATOM 138 CA SER A 38 -17.557 -21.517 45.979 1.00 61.74 C
ANISOU 138 CA SER A 38 5445 11246 6767 543 -227 -2012 C
ATOM 139 C SER A 38 -18.098 -21.139 44.608 1.00 64.39 C
ANISOU 139 C SER A 38 5748 11613 7107 564 -299 -1959 C
ATOM 140 O SER A 38 -17.601 -21.641 43.609 1.00 63.93 O
ANISOU 140 O SER A 38 5815 11383 7091 716 -403 -1879 O
ATOM 141 CB SER A 38 -18.468 -22.551 46.637 1.00 68.48 C
ANISOU 141 CB SER A 38 6109 12285 7626 703 -234 -2248 C
ATOM 142 OG SER A 38 -17.887 -23.093 47.812 1.00 78.45 O
ANISOU 142 OG SER A 38 7421 13492 8893 727 -189 -2312 O
ATOM 143 N LEU A 39 -19.085 -20.223 44.567 1.00 61.57 N
ANISOU 143 N LEU A 39 5232 11467 6693 395 -238 -1999 N
ATOM 144 CA LEU A 39 -19.714 -19.728 43.337 1.00 62.32 C
ANISOU 144 CA LEU A 39 5270 11626 6784 380 -296 -1976 C
ATOM 145 C LEU A 39 -18.696 -18.962 42.487 1.00 64.40 C
ANISOU 145 C LEU A 39 5753 11662 7053 306 -323 -1758 C
ATOM 146 O LEU A 39 -18.495 -19.326 41.325 1.00 63.28 O
ANISOU 146 O LEU A 39 5682 11424 6936 450 -430 -1705 O
ATOM 147 CB LEU A 39 -20.930 -18.836 43.667 1.00 63.78 C
ANISOU 147 CB LEU A 39 5250 12077 6908 161 -197 -2076 C
ATOM 148 CG LEU A 39 -22.334 -19.358 43.236 1.00 71.54 C
ANISOU 148 CG LEU A 39 5958 13332 7891 261 -247 -2292 C
ATOM 149 CD1 LEU A 39 -23.259 -19.565 44.429 1.00 72.68 C
ANISOU 149 CD1 LEU A 39 5873 13749 7994 185 -134 -2493 C
ATOM 150 CD2 LEU A 39 -22.976 -18.442 42.218 1.00 75.31 C
ANISOU 150 CD2 LEU A 39 6373 13892 8350 125 -264 -2272 C
ATOM 151 N VAL A 40 -18.018 -17.944 43.089 1.00 59.88 N
ANISOU 151 N VAL A 40 5292 11008 6451 100 -229 -1639 N
ATOM 152 CA VAL A 40 -16.967 -17.112 42.476 1.00 58.31 C
ANISOU 152 CA VAL A 40 5290 10612 6254 20 -239 -1450 C
ATOM 153 C VAL A 40 -15.856 -18.024 41.895 1.00 61.65 C
ANISOU 153 C VAL A 40 5873 10820 6731 201 -321 -1370 C
ATOM 154 O VAL A 40 -15.424 -17.813 40.763 1.00 61.05 O
ANISOU 154 O VAL A 40 5899 10637 6661 233 -377 -1267 O
ATOM 155 CB VAL A 40 -16.383 -16.061 43.488 1.00 61.62 C
ANISOU 155 CB VAL A 40 5794 10991 6628 -183 -137 -1367 C
ATOM 156 CG1 VAL A 40 -15.097 -15.395 42.961 1.00 60.15 C
ANISOU 156 CG1 VAL A 40 5803 10597 6453 -217 -158 -1196 C
ATOM 157 CG2 VAL A 40 -17.415 -14.999 43.849 1.00 61.75 C
ANISOU 157 CG2 VAL A 40 5712 11173 6577 -391 -54 -1403 C
ATOM 158 N PHE A 41 -15.412 -19.035 42.667 1.00 58.49 N
ANISOU 158 N PHE A 41 5502 10357 6364 308 -320 -1424 N
ATOM 159 CA PHE A 41 -14.376 -19.966 42.226 1.00 58.12 C
ANISOU 159 CA PHE A 41 5624 10090 6368 454 -383 -1355 C
ATOM 160 C PHE A 41 -14.791 -20.755 40.981 1.00 62.64 C
ANISOU 160 C PHE A 41 6213 10633 6954 654 -499 -1361 C
ATOM 161 O PHE A 41 -13.975 -20.853 40.074 1.00 61.73 O
ANISOU 161 O PHE A 41 6264 10345 6844 690 -540 -1231 O
ATOM 162 CB PHE A 41 -13.970 -20.943 43.343 1.00 60.31 C
ANISOU 162 CB PHE A 41 5923 10310 6683 528 -362 -1442 C
ATOM 163 CG PHE A 41 -12.956 -21.973 42.896 1.00 61.44 C
ANISOU 163 CG PHE A 41 6256 10205 6882 664 -422 -1380 C
ATOM 164 CD1 PHE A 41 -11.620 -21.625 42.710 1.00 62.55 C
ANISOU 164 CD1 PHE A 41 6566 10165 7036 559 -390 -1240 C
ATOM 165 CD2 PHE A 41 -13.345 -23.282 42.619 1.00 64.39 C
ANISOU 165 CD2 PHE A 41 6646 10527 7292 895 -511 -1463 C
ATOM 166 CE1 PHE A 41 -10.690 -22.574 42.281 1.00 63.78 C
ANISOU 166 CE1 PHE A 41 6906 10090 7238 649 -428 -1181 C
ATOM 167 CE2 PHE A 41 -12.413 -24.232 42.191 1.00 67.48 C
ANISOU 167 CE2 PHE A 41 7251 10661 7729 1005 -561 -1391 C
ATOM 168 CZ PHE A 41 -11.093 -23.875 42.037 1.00 64.62 C
ANISOU 168 CZ PHE A 41 7057 10119 7377 864 -510 -1249 C
ATOM 169 N ILE A 42 -16.019 -21.336 40.950 1.00 60.80 N
ANISOU 169 N ILE A 42 5807 10575 6717 788 -553 -1516 N
ATOM 170 CA ILE A 42 -16.518 -22.152 39.834 1.00 61.98 C
ANISOU 170 CA ILE A 42 5958 10725 6868 1016 -686 -1545 C
ATOM 171 C ILE A 42 -16.648 -21.285 38.573 1.00 67.39 C
ANISOU 171 C ILE A 42 6664 11435 7508 947 -721 -1445 C
ATOM 172 O ILE A 42 -16.039 -21.609 37.556 1.00 67.84 O
ANISOU 172 O ILE A 42 6890 11334 7551 1046 -794 -1328 O
ATOM 173 CB ILE A 42 -17.839 -22.886 40.212 1.00 66.87 C
ANISOU 173 CB ILE A 42 6346 11570 7491 1177 -736 -1768 C
ATOM 174 CG1 ILE A 42 -17.547 -23.981 41.274 1.00 67.93 C
ANISOU 174 CG1 ILE A 42 6509 11627 7673 1307 -728 -1865 C
ATOM 175 CG2 ILE A 42 -18.519 -23.508 38.970 1.00 68.40 C
ANISOU 175 CG2 ILE A 42 6508 11815 7667 1413 -892 -1810 C
ATOM 176 CD1 ILE A 42 -18.724 -24.532 42.036 1.00 73.13 C
ANISOU 176 CD1 ILE A 42 6917 12536 8334 1414 -730 -2109 C
ATOM 177 N PHE A 43 -17.390 -20.171 38.658 1.00 64.64 N
ANISOU 177 N PHE A 43 6161 11272 7129 763 -661 -1488 N
ATOM 178 CA PHE A 43 -17.607 -19.227 37.560 1.00 64.30 C
ANISOU 178 CA PHE A 43 6119 11266 7044 673 -686 -1423 C
ATOM 179 C PHE A 43 -16.266 -18.623 37.029 1.00 66.22 C
ANISOU 179 C PHE A 43 6592 11287 7279 588 -661 -1224 C
ATOM 180 O PHE A 43 -16.083 -18.509 35.814 1.00 66.28 O
ANISOU 180 O PHE A 43 6685 11245 7255 646 -729 -1149 O
ATOM 181 CB PHE A 43 -18.576 -18.122 38.023 1.00 66.46 C
ANISOU 181 CB PHE A 43 6210 11746 7296 451 -601 -1510 C
ATOM 182 CG PHE A 43 -19.090 -17.222 36.927 1.00 68.64 C
ANISOU 182 CG PHE A 43 6447 12095 7536 366 -636 -1498 C
ATOM 183 CD1 PHE A 43 -19.856 -17.733 35.882 1.00 73.33 C
ANISOU 183 CD1 PHE A 43 6943 12808 8111 527 -759 -1587 C
ATOM 184 CD2 PHE A 43 -18.828 -15.856 36.948 1.00 70.06 C
ANISOU 184 CD2 PHE A 43 6694 12227 7699 134 -557 -1410 C
ATOM 185 CE1 PHE A 43 -20.315 -16.898 34.856 1.00 74.65 C
ANISOU 185 CE1 PHE A 43 7074 13047 8241 445 -796 -1590 C
ATOM 186 CE2 PHE A 43 -19.284 -15.023 35.922 1.00 72.99 C
ANISOU 186 CE2 PHE A 43 7043 12650 8042 57 -592 -1411 C
ATOM 187 CZ PHE A 43 -20.027 -15.549 34.883 1.00 72.43 C
ANISOU 187 CZ PHE A 43 6866 12703 7952 203 -708 -1505 C
ATOM 188 N GLY A 44 -15.346 -18.293 37.933 1.00 60.45 N
ANISOU 188 N GLY A 44 5950 10446 6571 464 -567 -1155 N
ATOM 189 CA GLY A 44 -14.038 -17.742 37.594 1.00 58.78 C
ANISOU 189 CA GLY A 44 5922 10055 6357 381 -533 -998 C
ATOM 190 C GLY A 44 -13.068 -18.720 36.958 1.00 63.90 C
ANISOU 190 C GLY A 44 6749 10514 7016 521 -583 -907 C
ATOM 191 O GLY A 44 -12.334 -18.348 36.028 1.00 61.69 O
ANISOU 191 O GLY A 44 6594 10139 6707 493 -589 -791 O
ATOM 192 N PHE A 45 -13.011 -19.967 37.502 1.00 62.50 N
ANISOU 192 N PHE A 45 6599 10271 6877 659 -609 -961 N
ATOM 193 CA PHE A 45 -12.123 -21.021 37.009 1.00 62.97 C
ANISOU 193 CA PHE A 45 6857 10120 6948 784 -650 -876 C
ATOM 194 C PHE A 45 -12.538 -21.430 35.599 1.00 67.14 C
ANISOU 194 C PHE A 45 7447 10645 7419 943 -761 -834 C
ATOM 195 O PHE A 45 -11.674 -21.589 34.736 1.00 67.31 O
ANISOU 195 O PHE A 45 7655 10512 7406 952 -769 -700 O
ATOM 196 CB PHE A 45 -12.104 -22.245 37.942 1.00 65.95 C
ANISOU 196 CB PHE A 45 7255 10421 7383 904 -662 -964 C
ATOM 197 CG PHE A 45 -11.138 -23.315 37.493 1.00 68.79 C
ANISOU 197 CG PHE A 45 7854 10526 7757 1004 -694 -870 C
ATOM 198 CD1 PHE A 45 -9.800 -23.271 37.873 1.00 70.72 C
ANISOU 198 CD1 PHE A 45 8238 10600 8032 863 -608 -788 C
ATOM 199 CD2 PHE A 45 -11.555 -24.349 36.653 1.00 72.84 C
ANISOU 199 CD2 PHE A 45 8462 10968 8245 1235 -813 -863 C
ATOM 200 CE1 PHE A 45 -8.896 -24.240 37.427 1.00 72.60 C
ANISOU 200 CE1 PHE A 45 8711 10593 8281 919 -621 -698 C
ATOM 201 CE2 PHE A 45 -10.647 -25.310 36.197 1.00 76.59 C
ANISOU 201 CE2 PHE A 45 9200 11179 8721 1310 -837 -755 C
ATOM 202 CZ PHE A 45 -9.323 -25.249 36.586 1.00 73.68 C
ANISOU 202 CZ PHE A 45 8972 10636 8388 1136 -731 -672 C
ATOM 203 N VAL A 46 -13.854 -21.607 35.380 1.00 62.32 N
ANISOU 203 N VAL A 46 6671 10217 6790 1065 -844 -956 N
ATOM 204 CA VAL A 46 -14.430 -21.961 34.082 1.00 62.42 C
ANISOU 204 CA VAL A 46 6707 10273 6736 1237 -971 -945 C
ATOM 205 C VAL A 46 -14.111 -20.817 33.095 1.00 65.06 C
ANISOU 205 C VAL A 46 7080 10630 7009 1095 -946 -843 C
ATOM 206 O VAL A 46 -13.557 -21.069 32.027 1.00 65.72 O
ANISOU 206 O VAL A 46 7336 10607 7029 1166 -993 -726 O
ATOM 207 CB VAL A 46 -15.967 -22.267 34.183 1.00 66.68 C
ANISOU 207 CB VAL A 46 7007 11054 7274 1380 -1061 -1138 C
ATOM 208 CG1 VAL A 46 -16.633 -22.300 32.804 1.00 67.73 C
ANISOU 208 CG1 VAL A 46 7120 11289 7325 1519 -1194 -1144 C
ATOM 209 CG2 VAL A 46 -16.231 -23.570 34.936 1.00 67.37 C
ANISOU 209 CG2 VAL A 46 7085 11102 7411 1585 -1114 -1242 C
ATOM 210 N GLY A 47 -14.425 -19.586 33.501 1.00 59.89 N
ANISOU 210 N GLY A 47 6284 10104 6369 898 -869 -886 N
ATOM 211 CA GLY A 47 -14.235 -18.367 32.723 1.00 58.72 C
ANISOU 211 CA GLY A 47 6150 9987 6175 757 -842 -822 C
ATOM 212 C GLY A 47 -12.822 -18.132 32.236 1.00 62.98 C
ANISOU 212 C GLY A 47 6896 10345 6691 692 -790 -662 C
ATOM 213 O GLY A 47 -12.614 -17.931 31.039 1.00 62.23 O
ANISOU 213 O GLY A 47 6885 10237 6521 723 -831 -594 O
ATOM 214 N ASN A 48 -11.837 -18.169 33.162 1.00 60.47 N
ANISOU 214 N ASN A 48 6647 9902 6426 599 -697 -614 N
ATOM 215 CA ASN A 48 -10.420 -17.932 32.863 1.00 59.27 C
ANISOU 215 CA ASN A 48 6659 9600 6262 511 -628 -487 C
ATOM 216 C ASN A 48 -9.774 -19.108 32.120 1.00 65.19 C
ANISOU 216 C ASN A 48 7603 10193 6972 634 -663 -391 C
ATOM 217 O ASN A 48 -8.886 -18.864 31.303 1.00 64.26 O
ANISOU 217 O ASN A 48 7612 10004 6800 581 -628 -287 O
ATOM 218 CB ASN A 48 -9.646 -17.566 34.121 1.00 56.81 C
ANISOU 218 CB ASN A 48 6332 9236 6017 373 -528 -492 C
ATOM 219 CG ASN A 48 -9.924 -16.143 34.547 1.00 70.93 C
ANISOU 219 CG ASN A 48 8007 11133 7810 227 -484 -529 C
ATOM 220 ND2 ASN A 48 -10.865 -15.959 35.464 1.00 56.71 N
ANISOU 220 ND2 ASN A 48 6071 9441 6037 199 -479 -625 N
ATOM 221 OD1 ASN A 48 -9.353 -15.188 34.013 1.00 71.21 O
ANISOU 221 OD1 ASN A 48 8080 11159 7816 144 -457 -475 O
ATOM 222 N MET A 49 -10.241 -20.354 32.340 1.00 65.84 N
ANISOU 222 N MET A 49 7718 10225 7073 802 -734 -428 N
ATOM 223 CA MET A 49 -9.724 -21.513 31.596 1.00 68.71 C
ANISOU 223 CA MET A 49 8305 10415 7389 936 -782 -328 C
ATOM 224 C MET A 49 -10.148 -21.420 30.136 1.00 71.57 C
ANISOU 224 C MET A 49 8720 10841 7633 1038 -871 -274 C
ATOM 225 O MET A 49 -9.331 -21.704 29.261 1.00 72.65 O
ANISOU 225 O MET A 49 9060 10853 7691 1038 -857 -141 O
ATOM 226 CB MET A 49 -10.154 -22.867 32.196 1.00 73.59 C
ANISOU 226 CB MET A 49 8958 10948 8054 1121 -855 -391 C
ATOM 227 CG MET A 49 -9.238 -23.380 33.319 1.00 78.66 C
ANISOU 227 CG MET A 49 9679 11422 8786 1037 -767 -392 C
ATOM 228 SD MET A 49 -7.437 -23.444 33.010 1.00 84.64 S
ANISOU 228 SD MET A 49 10680 11948 9530 856 -646 -228 S
ATOM 229 CE MET A 49 -7.366 -24.585 31.567 1.00 83.69 C
ANISOU 229 CE MET A 49 10847 11655 9295 1042 -742 -86 C
ATOM 230 N LEU A 50 -11.396 -20.975 29.873 1.00 66.10 N
ANISOU 230 N LEU A 50 7841 10354 6920 1105 -955 -383 N
ATOM 231 CA LEU A 50 -11.899 -20.780 28.515 1.00 66.33 C
ANISOU 231 CA LEU A 50 7885 10483 6835 1198 -1050 -364 C
ATOM 232 C LEU A 50 -11.075 -19.721 27.777 1.00 67.64 C
ANISOU 232 C LEU A 50 8113 10645 6940 1029 -968 -273 C
ATOM 233 O LEU A 50 -10.655 -19.975 26.653 1.00 68.48 O
ANISOU 233 O LEU A 50 8380 10706 6932 1089 -1000 -172 O
ATOM 234 CB LEU A 50 -13.381 -20.377 28.508 1.00 66.84 C
ANISOU 234 CB LEU A 50 7700 10788 6907 1258 -1139 -530 C
ATOM 235 CG LEU A 50 -14.417 -21.471 28.732 1.00 73.39 C
ANISOU 235 CG LEU A 50 8450 11685 7749 1494 -1267 -642 C
ATOM 236 CD1 LEU A 50 -15.781 -20.857 29.034 1.00 73.71 C
ANISOU 236 CD1 LEU A 50 8193 11990 7825 1467 -1301 -835 C
ATOM 237 CD2 LEU A 50 -14.539 -22.369 27.519 1.00 76.85 C
ANISOU 237 CD2 LEU A 50 9049 12085 8067 1734 -1414 -578 C
ATOM 238 N VAL A 51 -10.800 -18.566 28.428 1.00 61.13 N
ANISOU 238 N VAL A 51 7177 9866 6185 829 -862 -308 N
ATOM 239 CA VAL A 51 -10.012 -17.464 27.858 1.00 59.28 C
ANISOU 239 CA VAL A 51 6980 9636 5907 680 -784 -250 C
ATOM 240 C VAL A 51 -8.645 -17.995 27.422 1.00 62.89 C
ANISOU 240 C VAL A 51 7654 9930 6313 653 -715 -107 C
ATOM 241 O VAL A 51 -8.273 -17.801 26.269 1.00 62.05 O
ANISOU 241 O VAL A 51 7647 9835 6094 659 -718 -38 O
ATOM 242 CB VAL A 51 -9.881 -16.246 28.826 1.00 60.93 C
ANISOU 242 CB VAL A 51 7055 9889 6205 497 -694 -310 C
ATOM 243 CG1 VAL A 51 -8.867 -15.220 28.317 1.00 59.57 C
ANISOU 243 CG1 VAL A 51 6938 9698 5996 372 -616 -254 C
ATOM 244 CG2 VAL A 51 -11.234 -15.581 29.073 1.00 60.34 C
ANISOU 244 CG2 VAL A 51 6790 9976 6160 483 -745 -440 C
ATOM 245 N ILE A 52 -7.947 -18.716 28.319 1.00 60.45 N
ANISOU 245 N ILE A 52 7418 9476 6076 622 -654 -72 N
ATOM 246 CA ILE A 52 -6.616 -19.293 28.097 1.00 61.23 C
ANISOU 246 CA ILE A 52 7716 9405 6144 557 -568 49 C
ATOM 247 C ILE A 52 -6.610 -20.264 26.895 1.00 67.24 C
ANISOU 247 C ILE A 52 8692 10084 6774 696 -634 161 C
ATOM 248 O ILE A 52 -5.741 -20.125 26.029 1.00 67.63 O
ANISOU 248 O ILE A 52 8874 10097 6724 618 -567 261 O
ATOM 249 CB ILE A 52 -6.099 -19.963 29.403 1.00 64.38 C
ANISOU 249 CB ILE A 52 8133 9669 6659 509 -511 29 C
ATOM 250 CG1 ILE A 52 -5.564 -18.908 30.378 1.00 62.44 C
ANISOU 250 CG1 ILE A 52 7740 9483 6500 332 -414 -35 C
ATOM 251 CG2 ILE A 52 -5.031 -21.029 29.131 1.00 67.71 C
ANISOU 251 CG2 ILE A 52 8799 9879 7050 488 -456 148 C
ATOM 252 CD1 ILE A 52 -5.608 -19.318 31.787 1.00 70.82 C
ANISOU 252 CD1 ILE A 52 8735 10501 7674 318 -398 -111 C
ATOM 253 N LEU A 53 -7.567 -21.216 26.822 1.00 64.78 N
ANISOU 253 N LEU A 53 8414 9753 6449 905 -766 139 N
ATOM 254 CA LEU A 53 -7.593 -22.168 25.706 1.00 66.45 C
ANISOU 254 CA LEU A 53 8854 9874 6520 1065 -850 253 C
ATOM 255 C LEU A 53 -7.958 -21.487 24.389 1.00 69.92 C
ANISOU 255 C LEU A 53 9278 10473 6815 1101 -904 270 C
ATOM 256 O LEU A 53 -7.478 -21.930 23.351 1.00 71.91 O
ANISOU 256 O LEU A 53 9750 10653 6921 1142 -911 399 O
ATOM 257 CB LEU A 53 -8.531 -23.361 25.955 1.00 68.29 C
ANISOU 257 CB LEU A 53 9124 10053 6771 1317 -999 211 C
ATOM 258 CG LEU A 53 -8.308 -24.207 27.224 1.00 73.72 C
ANISOU 258 CG LEU A 53 9837 10578 7595 1328 -972 172 C
ATOM 259 CD1 LEU A 53 -9.307 -25.347 27.287 1.00 75.84 C
ANISOU 259 CD1 LEU A 53 10143 10811 7860 1618 -1139 117 C
ATOM 260 CD2 LEU A 53 -6.867 -24.734 27.337 1.00 76.62 C
ANISOU 260 CD2 LEU A 53 10448 10695 7968 1176 -840 307 C
ATOM 261 N ILE A 54 -8.771 -20.407 24.422 1.00 63.93 N
ANISOU 261 N ILE A 54 8278 9923 6089 1071 -936 140 N
ATOM 262 CA ILE A 54 -9.179 -19.655 23.226 1.00 63.26 C
ANISOU 262 CA ILE A 54 8155 10001 5879 1094 -990 123 C
ATOM 263 C ILE A 54 -7.980 -18.826 22.710 1.00 67.18 C
ANISOU 263 C ILE A 54 8725 10482 6317 904 -848 200 C
ATOM 264 O ILE A 54 -7.781 -18.751 21.501 1.00 68.32 O
ANISOU 264 O ILE A 54 8988 10666 6304 936 -864 267 O
ATOM 265 CB ILE A 54 -10.456 -18.812 23.496 1.00 64.76 C
ANISOU 265 CB ILE A 54 8071 10399 6134 1106 -1066 -54 C
ATOM 266 CG1 ILE A 54 -11.688 -19.726 23.514 1.00 66.06 C
ANISOU 266 CG1 ILE A 54 8174 10633 6294 1336 -1231 -135 C
ATOM 267 CG2 ILE A 54 -10.654 -17.685 22.477 1.00 65.04 C
ANISOU 267 CG2 ILE A 54 8044 10588 6079 1048 -1078 -95 C
ATOM 268 CD1 ILE A 54 -12.862 -19.222 24.317 1.00 71.44 C
ANISOU 268 CD1 ILE A 54 8573 11484 7087 1318 -1271 -321 C
ATOM 269 N LEU A 55 -7.163 -18.264 23.612 1.00 62.77 N
ANISOU 269 N LEU A 55 8101 9876 5875 721 -713 185 N
ATOM 270 CA LEU A 55 -5.969 -17.496 23.249 1.00 62.08 C
ANISOU 270 CA LEU A 55 8054 9788 5747 549 -576 232 C
ATOM 271 C LEU A 55 -4.835 -18.393 22.753 1.00 68.46 C
ANISOU 271 C LEU A 55 9107 10447 6459 507 -491 385 C
ATOM 272 O LEU A 55 -4.166 -18.025 21.793 1.00 69.49 O
ANISOU 272 O LEU A 55 9319 10623 6462 441 -424 441 O
ATOM 273 CB LEU A 55 -5.452 -16.667 24.438 1.00 60.21 C
ANISOU 273 CB LEU A 55 7667 9549 5661 388 -475 159 C
ATOM 274 CG LEU A 55 -6.273 -15.473 24.906 1.00 63.11 C
ANISOU 274 CG LEU A 55 7821 10049 6109 363 -514 25 C
ATOM 275 CD1 LEU A 55 -5.774 -14.998 26.255 1.00 61.42 C
ANISOU 275 CD1 LEU A 55 7508 9795 6034 241 -434 -21 C
ATOM 276 CD2 LEU A 55 -6.233 -14.327 23.896 1.00 65.12 C
ANISOU 276 CD2 LEU A 55 8040 10424 6278 328 -510 -12 C
ATOM 277 N ILE A 56 -4.590 -19.538 23.408 1.00 66.85 N
ANISOU 277 N ILE A 56 9023 10065 6312 532 -482 445 N
ATOM 278 CA ILE A 56 -3.496 -20.439 23.030 1.00 69.69 C
ANISOU 278 CA ILE A 56 9640 10250 6591 462 -389 594 C
ATOM 279 C ILE A 56 -3.846 -21.284 21.779 1.00 78.89 C
ANISOU 279 C ILE A 56 11042 11368 7563 626 -484 718 C
ATOM 280 O ILE A 56 -2.956 -21.501 20.956 1.00 80.31 O
ANISOU 280 O ILE A 56 11416 11494 7602 535 -390 842 O
ATOM 281 CB ILE A 56 -3.050 -21.326 24.238 1.00 73.06 C
ANISOU 281 CB ILE A 56 10125 10478 7156 412 -342 603 C
ATOM 282 CG1 ILE A 56 -2.476 -20.440 25.368 1.00 71.35 C
ANISOU 282 CG1 ILE A 56 9697 10321 7093 231 -234 494 C
ATOM 283 CG2 ILE A 56 -2.018 -22.409 23.829 1.00 75.88 C
ANISOU 283 CG2 ILE A 56 10787 10615 7428 336 -252 763 C
ATOM 284 CD1 ILE A 56 -2.371 -21.103 26.731 1.00 80.50 C
ANISOU 284 CD1 ILE A 56 10837 11343 8405 208 -221 447 C
ATOM 285 N ASN A 57 -5.117 -21.722 21.609 1.00 78.38 N
ANISOU 285 N ASN A 57 10956 11345 7479 864 -667 679 N
ATOM 286 CA ASN A 57 -5.495 -22.580 20.477 1.00 81.48 C
ANISOU 286 CA ASN A 57 11582 11696 7682 1056 -784 792 C
ATOM 287 C ASN A 57 -6.232 -21.858 19.317 1.00 88.37 C
ANISOU 287 C ASN A 57 12372 12799 8406 1155 -884 746 C
ATOM 288 O ASN A 57 -5.903 -22.155 18.173 1.00 90.22 O
ANISOU 288 O ASN A 57 12820 13021 8437 1192 -889 870 O
ATOM 289 CB ASN A 57 -6.289 -23.801 20.955 1.00 81.95 C
ANISOU 289 CB ASN A 57 11724 11623 7788 1291 -937 791 C
ATOM 290 CG ASN A 57 -5.496 -24.679 21.914 1.00104.30 C
ANISOU 290 CG ASN A 57 14703 14192 10734 1207 -845 852 C
ATOM 291 ND2 ASN A 57 -5.985 -24.843 23.133 1.00 95.51 N
ANISOU 291 ND2 ASN A 57 13426 13062 9802 1255 -884 727 N
ATOM 292 OD1 ASN A 57 -4.424 -25.203 21.589 1.00 99.32 O
ANISOU 292 OD1 ASN A 57 14329 13377 10029 1082 -731 1003 O
ATOM 293 N TYR A 58 -7.194 -20.948 19.564 1.00 85.99 N
ANISOU 293 N TYR A 58 11784 12698 8189 1186 -958 574 N
ATOM 294 CA TYR A 58 -7.864 -20.260 18.446 1.00 87.84 C
ANISOU 294 CA TYR A 58 11946 13145 8285 1262 -1050 514 C
ATOM 295 C TYR A 58 -7.055 -19.014 18.023 1.00 88.97 C
ANISOU 295 C TYR A 58 12026 13385 8394 1050 -903 496 C
ATOM 296 O TYR A 58 -6.712 -18.917 16.843 1.00 89.92 O
ANISOU 296 O TYR A 58 12279 13566 8322 1057 -892 565 O
ATOM 297 CB TYR A 58 -9.351 -19.931 18.747 1.00 91.28 C
ANISOU 297 CB TYR A 58 12124 13754 8805 1397 -1210 330 C
ATOM 298 CG TYR A 58 -9.864 -18.602 18.212 1.00 96.71 C
ANISOU 298 CG TYR A 58 12612 14663 9472 1328 -1226 194 C
ATOM 299 CD1 TYR A 58 -10.040 -18.394 16.845 1.00101.08 C
ANISOU 299 CD1 TYR A 58 13240 15340 9826 1401 -1295 207 C
ATOM 300 CD2 TYR A 58 -10.202 -17.564 19.077 1.00 96.95 C
ANISOU 300 CD2 TYR A 58 12395 14768 9674 1193 -1178 49 C
ATOM 301 CE1 TYR A 58 -10.505 -17.172 16.352 1.00103.11 C
ANISOU 301 CE1 TYR A 58 13323 15786 10069 1334 -1310 67 C
ATOM 302 CE2 TYR A 58 -10.676 -16.341 18.595 1.00 97.94 C
ANISOU 302 CE2 TYR A 58 12365 15062 9786 1123 -1194 -76 C
ATOM 303 CZ TYR A 58 -10.829 -16.150 17.233 1.00109.80 C
ANISOU 303 CZ TYR A 58 13937 16681 11103 1194 -1261 -75 C
ATOM 304 OH TYR A 58 -11.290 -14.944 16.761 1.00113.66 O
ANISOU 304 OH TYR A 58 14280 17323 11584 1122 -1278 -214 O
ATOM 305 N LYS A 59 -6.749 -18.073 18.964 1.00 82.03 N
ANISOU 305 N LYS A 59 10953 12527 7689 878 -797 400 N
ATOM 306 CA LYS A 59 -5.969 -16.856 18.684 1.00 80.04 C
ANISOU 306 CA LYS A 59 10626 12361 7423 702 -668 361 C
ATOM 307 C LYS A 59 -4.475 -17.172 18.452 1.00 85.52 C
ANISOU 307 C LYS A 59 11499 12950 8044 555 -496 494 C
ATOM 308 O LYS A 59 -3.789 -16.401 17.782 1.00 85.86 O
ANISOU 308 O LYS A 59 11533 13089 8002 450 -400 482 O
ATOM 309 CB LYS A 59 -6.134 -15.822 19.794 1.00 79.05 C
ANISOU 309 CB LYS A 59 10262 12277 7495 595 -631 223 C
ATOM 310 CG LYS A 59 -7.247 -14.829 19.511 1.00 84.84 C
ANISOU 310 CG LYS A 59 10816 13174 8245 646 -740 73 C
ATOM 311 N ARG A 60 -3.984 -18.302 19.012 1.00 82.23 N
ANISOU 311 N ARG A 60 11240 12341 7664 542 -455 606 N
ATOM 312 CA ARG A 60 -2.632 -18.870 18.868 1.00 82.61 C
ANISOU 312 CA ARG A 60 11488 12255 7645 390 -293 743 C
ATOM 313 C ARG A 60 -1.480 -17.946 19.350 1.00 83.61 C
ANISOU 313 C ARG A 60 11480 12431 7860 158 -112 680 C
ATOM 314 O ARG A 60 -0.319 -18.267 19.083 1.00 85.24 O
ANISOU 314 O ARG A 60 11820 12575 7992 4 39 769 O
ATOM 315 CB ARG A 60 -2.376 -19.309 17.403 1.00 85.18 C
ANISOU 315 CB ARG A 60 12054 12599 7709 431 -288 877 C
ATOM 316 CG ARG A 60 -3.244 -20.467 16.927 1.00 97.23 C
ANISOU 316 CG ARG A 60 13784 14035 9125 666 -459 976 C
ATOM 317 CD ARG A 60 -2.647 -21.824 17.260 1.00111.13 C
ANISOU 317 CD ARG A 60 15823 15526 10878 647 -412 1138 C
ATOM 318 NE ARG A 60 -3.521 -22.925 16.840 1.00125.01 N
ANISOU 318 NE ARG A 60 17780 17185 12534 911 -600 1223 N
ATOM 319 CZ ARG A 60 -3.496 -23.494 15.639 1.00145.99 C
ANISOU 319 CZ ARG A 60 20709 19818 14942 1011 -649 1371 C
ATOM 320 NH1 ARG A 60 -2.638 -23.076 14.714 1.00138.79 N1+
ANISOU 320 NH1 ARG A 60 19902 18981 13851 850 -507 1450 N1+
ATOM 321 NH2 ARG A 60 -4.330 -24.485 15.351 1.00133.59 N
ANISOU 321 NH2 ARG A 60 19309 18159 13290 1283 -843 1434 N
ATOM 322 N LEU A 61 -1.783 -16.855 20.098 1.00 75.67 N
ANISOU 322 N LEU A 61 10218 11527 7007 131 -127 527 N
ATOM 323 CA LEU A 61 -0.813 -15.879 20.639 1.00 73.28 C
ANISOU 323 CA LEU A 61 9760 11286 6795 -43 7 441 C
ATOM 324 C LEU A 61 0.100 -15.297 19.536 1.00 78.00 C
ANISOU 324 C LEU A 61 10391 12007 7237 -142 126 451 C
ATOM 325 O LEU A 61 1.326 -15.419 19.596 1.00 78.70 O
ANISOU 325 O LEU A 61 10517 12076 7309 -308 284 482 O
ATOM 326 CB LEU A 61 0.042 -16.473 21.774 1.00 72.70 C
ANISOU 326 CB LEU A 61 9703 11070 6852 -172 107 466 C
ATOM 327 CG LEU A 61 -0.658 -17.226 22.899 1.00 76.52 C
ANISOU 327 CG LEU A 61 10178 11418 7478 -89 16 460 C
ATOM 328 CD1 LEU A 61 0.365 -17.913 23.784 1.00 76.62 C
ANISOU 328 CD1 LEU A 61 10250 11282 7579 -234 130 492 C
ATOM 329 CD2 LEU A 61 -1.555 -16.303 23.728 1.00 76.54 C
ANISOU 329 CD2 LEU A 61 9950 11516 7615 -28 -74 321 C
ATOM 330 N LYS A 62 -0.512 -14.672 18.525 1.00 74.34 N
ANISOU 330 N LYS A 62 9907 11685 6656 -46 52 408 N
ATOM 331 CA LYS A 62 0.199 -14.073 17.385 1.00 74.68 C
ANISOU 331 CA LYS A 62 9972 11872 6530 -112 149 396 C
ATOM 332 C LYS A 62 0.523 -12.580 17.625 1.00 75.20 C
ANISOU 332 C LYS A 62 9809 12080 6684 -163 189 223 C
ATOM 333 O LYS A 62 1.288 -11.985 16.862 1.00 76.14 O
ANISOU 333 O LYS A 62 9907 12330 6692 -230 291 179 O
ATOM 334 CB LYS A 62 -0.614 -14.251 16.072 1.00 78.08 C
ANISOU 334 CB LYS A 62 10523 12384 6761 33 40 437 C
ATOM 335 CG LYS A 62 -1.995 -13.595 16.073 1.00 90.56 C
ANISOU 335 CG LYS A 62 11965 14045 8401 187 -140 316 C
ATOM 336 CD LYS A 62 -2.832 -14.027 14.880 1.00102.59 C
ANISOU 336 CD LYS A 62 13615 15636 9727 342 -267 361 C
ATOM 337 CE LYS A 62 -4.258 -13.511 14.965 1.00118.76 C
ANISOU 337 CE LYS A 62 15513 17762 11847 477 -448 228 C
ATOM 338 NZ LYS A 62 -5.104 -14.291 15.914 1.00129.24 N1+
ANISOU 338 NZ LYS A 62 16811 18977 13317 564 -555 244 N1+
ATOM 339 N SER A 63 -0.043 -11.998 18.682 1.00 67.98 N
ANISOU 339 N SER A 63 8735 11136 5957 -126 110 125 N
ATOM 340 CA SER A 63 0.117 -10.588 19.005 1.00 66.19 C
ANISOU 340 CA SER A 63 8321 11007 5822 -143 116 -31 C
ATOM 341 C SER A 63 0.661 -10.366 20.421 1.00 68.93 C
ANISOU 341 C SER A 63 8551 11286 6353 -221 162 -75 C
ATOM 342 O SER A 63 0.528 -11.243 21.283 1.00 67.74 O
ANISOU 342 O SER A 63 8440 11008 6288 -239 152 -5 O
ATOM 343 CB SER A 63 -1.232 -9.891 18.862 1.00 68.13 C
ANISOU 343 CB SER A 63 8500 11289 6099 -19 -40 -117 C
ATOM 344 OG SER A 63 -1.255 -8.622 19.493 1.00 75.86 O
ANISOU 344 OG SER A 63 9325 12295 7201 -29 -57 -252 O
ATOM 345 N MET A 64 1.243 -9.163 20.654 1.00 65.52 N
ANISOU 345 N MET A 64 7976 10944 5977 -249 199 -203 N
ATOM 346 CA MET A 64 1.751 -8.691 21.953 1.00 64.28 C
ANISOU 346 CA MET A 64 7690 10755 5980 -295 220 -272 C
ATOM 347 C MET A 64 0.558 -8.605 22.926 1.00 63.49 C
ANISOU 347 C MET A 64 7560 10556 6006 -223 90 -277 C
ATOM 348 O MET A 64 0.652 -9.082 24.048 1.00 61.60 O
ANISOU 348 O MET A 64 7300 10232 5874 -261 95 -252 O
ATOM 349 CB MET A 64 2.478 -7.336 21.786 1.00 67.09 C
ANISOU 349 CB MET A 64 7913 11240 6339 -290 257 -418 C
ATOM 350 CG MET A 64 2.791 -6.622 23.076 1.00 70.77 C
ANISOU 350 CG MET A 64 8250 11683 6955 -289 233 -503 C
ATOM 351 SD MET A 64 4.207 -5.513 22.885 1.00 77.48 S
ANISOU 351 SD MET A 64 8948 12702 7788 -304 323 -662 S
ATOM 352 CE MET A 64 3.569 -4.017 23.669 1.00 73.51 C
ANISOU 352 CE MET A 64 8368 12158 7402 -164 175 -779 C
ATOM 353 N THR A 65 -0.579 -8.074 22.447 1.00 59.22 N
ANISOU 353 N THR A 65 7023 10036 5444 -132 -19 -314 N
ATOM 354 CA THR A 65 -1.847 -7.957 23.175 1.00 58.33 C
ANISOU 354 CA THR A 65 6879 9856 5427 -81 -134 -330 C
ATOM 355 C THR A 65 -2.288 -9.323 23.734 1.00 62.54 C
ANISOU 355 C THR A 65 7473 10298 5993 -78 -153 -230 C
ATOM 356 O THR A 65 -2.702 -9.395 24.892 1.00 61.34 O
ANISOU 356 O THR A 65 7267 10083 5955 -86 -185 -242 O
ATOM 357 CB THR A 65 -2.913 -7.381 22.239 1.00 65.03 C
ANISOU 357 CB THR A 65 7736 10762 6209 -8 -230 -386 C
ATOM 358 CG2 THR A 65 -4.212 -7.015 22.963 1.00 58.60 C
ANISOU 358 CG2 THR A 65 6867 9902 5495 13 -333 -432 C
ATOM 359 OG1 THR A 65 -2.362 -6.243 21.572 1.00 69.49 O
ANISOU 359 OG1 THR A 65 8269 11407 6727 -2 -203 -480 O
ATOM 360 N ASP A 66 -2.155 -10.398 22.916 1.00 60.26 N
ANISOU 360 N ASP A 66 7305 9998 5595 -60 -131 -134 N
ATOM 361 CA ASP A 66 -2.518 -11.776 23.256 1.00 60.00 C
ANISOU 361 CA ASP A 66 7363 9863 5572 -29 -157 -38 C
ATOM 362 C ASP A 66 -1.631 -12.327 24.374 1.00 61.34 C
ANISOU 362 C ASP A 66 7533 9935 5840 -121 -70 -6 C
ATOM 363 O ASP A 66 -2.128 -13.087 25.209 1.00 61.23 O
ANISOU 363 O ASP A 66 7532 9830 5903 -91 -112 18 O
ATOM 364 CB ASP A 66 -2.471 -12.679 22.016 1.00 63.85 C
ANISOU 364 CB ASP A 66 8015 10351 5895 22 -159 64 C
ATOM 365 CG ASP A 66 -3.459 -12.292 20.923 1.00 78.02 C
ANISOU 365 CG ASP A 66 9808 12252 7583 130 -267 24 C
ATOM 366 OD1 ASP A 66 -4.492 -11.641 21.248 1.00 76.91 O
ANISOU 366 OD1 ASP A 66 9549 12154 7519 176 -361 -74 O
ATOM 367 OD2 ASP A 66 -3.218 -12.661 19.741 1.00 86.91 O1-
ANISOU 367 OD2 ASP A 66 11059 13422 8541 161 -255 87 O1-
ATOM 368 N ILE A 67 -0.350 -11.909 24.428 1.00 55.45 N
ANISOU 368 N ILE A 67 6754 9220 5094 -231 47 -28 N
ATOM 369 CA ILE A 67 0.563 -12.314 25.499 1.00 54.47 C
ANISOU 369 CA ILE A 67 6605 9027 5064 -335 129 -27 C
ATOM 370 C ILE A 67 0.088 -11.700 26.830 1.00 55.70 C
ANISOU 370 C ILE A 67 6628 9174 5361 -313 66 -109 C
ATOM 371 O ILE A 67 0.031 -12.418 27.835 1.00 54.19 O
ANISOU 371 O ILE A 67 6443 8894 5254 -332 63 -94 O
ATOM 372 CB ILE A 67 2.056 -11.971 25.209 1.00 57.84 C
ANISOU 372 CB ILE A 67 6997 9528 5452 -464 269 -57 C
ATOM 373 CG1 ILE A 67 2.554 -12.568 23.869 1.00 59.87 C
ANISOU 373 CG1 ILE A 67 7400 9803 5545 -511 353 32 C
ATOM 374 CG2 ILE A 67 2.981 -12.353 26.384 1.00 57.74 C
ANISOU 374 CG2 ILE A 67 6931 9461 5546 -580 345 -84 C
ATOM 375 CD1 ILE A 67 2.485 -14.124 23.711 1.00 68.13 C
ANISOU 375 CD1 ILE A 67 8656 10689 6542 -529 370 180 C
ATOM 376 N TYR A 68 -0.288 -10.399 26.827 1.00 50.59 N
ANISOU 376 N TYR A 68 5881 8610 4730 -273 15 -195 N
ATOM 377 CA TYR A 68 -0.718 -9.708 28.046 1.00 48.68 C
ANISOU 377 CA TYR A 68 5541 8357 4596 -260 -40 -261 C
ATOM 378 C TYR A 68 -2.084 -10.190 28.519 1.00 53.81 C
ANISOU 378 C TYR A 68 6202 8955 5287 -203 -128 -240 C
ATOM 379 O TYR A 68 -2.286 -10.326 29.732 1.00 54.31 O
ANISOU 379 O TYR A 68 6222 8979 5435 -220 -139 -258 O
ATOM 380 CB TYR A 68 -0.703 -8.193 27.876 1.00 47.76 C
ANISOU 380 CB TYR A 68 5352 8316 4478 -233 -70 -349 C
ATOM 381 CG TYR A 68 0.656 -7.607 27.577 1.00 48.24 C
ANISOU 381 CG TYR A 68 5362 8455 4513 -271 9 -404 C
ATOM 382 CD1 TYR A 68 1.811 -8.170 28.103 1.00 50.37 C
ANISOU 382 CD1 TYR A 68 5600 8728 4811 -355 98 -403 C
ATOM 383 CD2 TYR A 68 0.785 -6.445 26.826 1.00 49.42 C
ANISOU 383 CD2 TYR A 68 5479 8684 4615 -223 -7 -481 C
ATOM 384 CE1 TYR A 68 3.067 -7.628 27.833 1.00 51.31 C
ANISOU 384 CE1 TYR A 68 5639 8951 4905 -397 175 -479 C
ATOM 385 CE2 TYR A 68 2.034 -5.882 26.569 1.00 50.96 C
ANISOU 385 CE2 TYR A 68 5601 8976 4785 -242 65 -557 C
ATOM 386 CZ TYR A 68 3.172 -6.481 27.068 1.00 57.07 C
ANISOU 386 CZ TYR A 68 6326 9776 5583 -332 158 -558 C
ATOM 387 OH TYR A 68 4.394 -5.911 26.825 1.00 59.24 O
ANISOU 387 OH TYR A 68 6498 10176 5834 -355 230 -657 O
ATOM 388 N LEU A 69 -2.990 -10.493 27.571 1.00 49.83 N
ANISOU 388 N LEU A 69 5750 8469 4716 -134 -187 -214 N
ATOM 389 CA LEU A 69 -4.315 -11.026 27.861 1.00 49.48 C
ANISOU 389 CA LEU A 69 5695 8409 4698 -70 -272 -215 C
ATOM 390 C LEU A 69 -4.216 -12.420 28.524 1.00 55.21 C
ANISOU 390 C LEU A 69 6471 9044 5462 -55 -258 -161 C
ATOM 391 O LEU A 69 -4.997 -12.724 29.426 1.00 55.50 O
ANISOU 391 O LEU A 69 6454 9068 5567 -30 -300 -193 O
ATOM 392 CB LEU A 69 -5.158 -11.102 26.577 1.00 50.10 C
ANISOU 392 CB LEU A 69 5810 8546 4679 11 -344 -211 C
ATOM 393 CG LEU A 69 -5.737 -9.783 26.058 1.00 54.08 C
ANISOU 393 CG LEU A 69 6254 9131 5161 9 -389 -293 C
ATOM 394 CD1 LEU A 69 -6.438 -9.989 24.716 1.00 54.35 C
ANISOU 394 CD1 LEU A 69 6331 9236 5084 88 -458 -294 C
ATOM 395 CD2 LEU A 69 -6.667 -9.088 27.096 1.00 53.54 C
ANISOU 395 CD2 LEU A 69 6091 9064 5189 -27 -431 -365 C
ATOM 396 N LEU A 70 -3.248 -13.251 28.084 1.00 52.61 N
ANISOU 396 N LEU A 70 6252 8651 5087 -79 -193 -86 N
ATOM 397 CA LEU A 70 -2.995 -14.585 28.626 1.00 52.80 C
ANISOU 397 CA LEU A 70 6362 8555 5145 -74 -172 -32 C
ATOM 398 C LEU A 70 -2.461 -14.480 30.057 1.00 53.81 C
ANISOU 398 C LEU A 70 6412 8649 5386 -156 -124 -85 C
ATOM 399 O LEU A 70 -2.942 -15.208 30.932 1.00 53.07 O
ANISOU 399 O LEU A 70 6312 8496 5356 -119 -156 -101 O
ATOM 400 CB LEU A 70 -2.004 -15.372 27.719 1.00 54.22 C
ANISOU 400 CB LEU A 70 6705 8662 5234 -114 -98 68 C
ATOM 401 CG LEU A 70 -1.385 -16.657 28.309 1.00 59.43 C
ANISOU 401 CG LEU A 70 7484 9160 5936 -153 -49 124 C
ATOM 402 CD1 LEU A 70 -2.429 -17.767 28.430 1.00 61.05 C
ANISOU 402 CD1 LEU A 70 7766 9279 6152 0 -155 149 C
ATOM 403 CD2 LEU A 70 -0.206 -17.118 27.503 1.00 59.68 C
ANISOU 403 CD2 LEU A 70 7670 9129 5877 -253 58 216 C
ATOM 404 N ASN A 71 -1.487 -13.570 30.288 1.00 48.59 N
ANISOU 404 N ASN A 71 5683 8039 4740 -254 -56 -124 N
ATOM 405 CA ASN A 71 -0.881 -13.339 31.600 1.00 47.99 C
ANISOU 405 CA ASN A 71 5523 7956 4753 -326 -20 -184 C
ATOM 406 C ASN A 71 -1.881 -12.732 32.582 1.00 51.63 C
ANISOU 406 C ASN A 71 5889 8459 5270 -283 -91 -244 C
ATOM 407 O ASN A 71 -1.823 -13.048 33.777 1.00 52.16 O
ANISOU 407 O ASN A 71 5919 8498 5402 -306 -87 -280 O
ATOM 408 CB ASN A 71 0.351 -12.475 31.485 1.00 46.27 C
ANISOU 408 CB ASN A 71 5247 7808 4526 -413 53 -224 C
ATOM 409 CG ASN A 71 1.557 -13.263 31.047 1.00 60.62 C
ANISOU 409 CG ASN A 71 7137 9579 6315 -514 158 -186 C
ATOM 410 ND2 ASN A 71 1.852 -13.259 29.759 1.00 53.04 N
ANISOU 410 ND2 ASN A 71 6245 8650 5257 -527 202 -136 N
ATOM 411 OD1 ASN A 71 2.211 -13.928 31.841 1.00 54.73 O
ANISOU 411 OD1 ASN A 71 6400 8768 5628 -590 206 -200 O
ATOM 412 N LEU A 72 -2.818 -11.903 32.081 1.00 46.52 N
ANISOU 412 N LEU A 72 5209 7876 4589 -231 -153 -258 N
ATOM 413 CA LEU A 72 -3.882 -11.337 32.905 1.00 45.55 C
ANISOU 413 CA LEU A 72 5013 7790 4504 -215 -208 -307 C
ATOM 414 C LEU A 72 -4.808 -12.462 33.393 1.00 50.97 C
ANISOU 414 C LEU A 72 5700 8449 5220 -164 -242 -309 C
ATOM 415 O LEU A 72 -5.205 -12.452 34.566 1.00 51.48 O
ANISOU 415 O LEU A 72 5705 8524 5330 -182 -246 -353 O
ATOM 416 CB LEU A 72 -4.673 -10.254 32.141 1.00 44.84 C
ANISOU 416 CB LEU A 72 4904 7762 4373 -194 -259 -329 C
ATOM 417 CG LEU A 72 -5.789 -9.524 32.913 1.00 46.52 C
ANISOU 417 CG LEU A 72 5055 8005 4614 -214 -302 -376 C
ATOM 418 CD1 LEU A 72 -5.286 -8.959 34.207 1.00 45.43 C
ANISOU 418 CD1 LEU A 72 4893 7853 4516 -265 -277 -395 C
ATOM 419 CD2 LEU A 72 -6.399 -8.424 32.068 1.00 45.64 C
ANISOU 419 CD2 LEU A 72 4945 7930 4465 -215 -343 -403 C
ATOM 420 N ALA A 73 -5.117 -13.443 32.509 1.00 48.19 N
ANISOU 420 N ALA A 73 5417 8064 4830 -89 -268 -267 N
ATOM 421 CA ALA A 73 -5.959 -14.603 32.844 1.00 48.88 C
ANISOU 421 CA ALA A 73 5510 8124 4940 -2 -315 -280 C
ATOM 422 C ALA A 73 -5.257 -15.486 33.873 1.00 54.03 C
ANISOU 422 C ALA A 73 6195 8681 5654 -28 -269 -284 C
ATOM 423 O ALA A 73 -5.907 -15.945 34.808 1.00 54.45 O
ANISOU 423 O ALA A 73 6191 8744 5754 7 -291 -343 O
ATOM 424 CB ALA A 73 -6.307 -15.404 31.595 1.00 50.35 C
ANISOU 424 CB ALA A 73 5788 8287 5056 106 -369 -227 C
ATOM 425 N ILE A 74 -3.925 -15.681 33.730 1.00 51.51 N
ANISOU 425 N ILE A 74 5955 8281 5334 -101 -198 -238 N
ATOM 426 CA ILE A 74 -3.119 -16.492 34.653 1.00 51.53 C
ANISOU 426 CA ILE A 74 5994 8185 5398 -151 -147 -254 C
ATOM 427 C ILE A 74 -3.131 -15.855 36.067 1.00 56.79 C
ANISOU 427 C ILE A 74 6537 8919 6121 -206 -137 -340 C
ATOM 428 O ILE A 74 -3.379 -16.586 37.020 1.00 56.66 O
ANISOU 428 O ILE A 74 6509 8866 6153 -183 -145 -389 O
ATOM 429 CB ILE A 74 -1.685 -16.751 34.122 1.00 54.21 C
ANISOU 429 CB ILE A 74 6433 8446 5721 -252 -61 -199 C
ATOM 430 CG1 ILE A 74 -1.729 -17.664 32.885 1.00 55.66 C
ANISOU 430 CG1 ILE A 74 6783 8532 5834 -193 -70 -99 C
ATOM 431 CG2 ILE A 74 -0.786 -17.367 35.205 1.00 54.45 C
ANISOU 431 CG2 ILE A 74 6470 8393 5825 -341 -3 -245 C
ATOM 432 CD1 ILE A 74 -0.484 -17.590 31.979 1.00 62.72 C
ANISOU 432 CD1 ILE A 74 7769 9397 6667 -309 27 -31 C
ATOM 433 N SER A 75 -2.930 -14.511 36.211 1.00 54.45 N
ANISOU 433 N SER A 75 6161 8719 5810 -262 -129 -360 N
ATOM 434 CA SER A 75 -2.961 -13.858 37.538 1.00 54.22 C
ANISOU 434 CA SER A 75 6042 8750 5809 -302 -130 -426 C
ATOM 435 C SER A 75 -4.356 -13.910 38.168 1.00 60.33 C
ANISOU 435 C SER A 75 6761 9576 6586 -253 -174 -464 C
ATOM 436 O SER A 75 -4.474 -13.853 39.389 1.00 61.33 O
ANISOU 436 O SER A 75 6839 9734 6731 -277 -167 -518 O
ATOM 437 CB SER A 75 -2.460 -12.420 37.485 1.00 56.56 C
ANISOU 437 CB SER A 75 6294 9118 6079 -346 -127 -432 C
ATOM 438 OG SER A 75 -3.065 -11.665 36.455 1.00 66.69 O
ANISOU 438 OG SER A 75 7588 10436 7318 -314 -158 -400 O
ATOM 439 N ASP A 76 -5.403 -14.056 37.358 1.00 58.04 N
ANISOU 439 N ASP A 76 6472 9312 6271 -188 -217 -448 N
ATOM 440 CA ASP A 76 -6.752 -14.209 37.886 1.00 58.53 C
ANISOU 440 CA ASP A 76 6457 9446 6334 -150 -250 -504 C
ATOM 441 C ASP A 76 -6.913 -15.624 38.439 1.00 62.47 C
ANISOU 441 C ASP A 76 6966 9897 6874 -77 -256 -547 C
ATOM 442 O ASP A 76 -7.516 -15.805 39.491 1.00 61.92 O
ANISOU 442 O ASP A 76 6822 9886 6819 -77 -250 -621 O
ATOM 443 CB ASP A 76 -7.799 -13.902 36.805 1.00 61.58 C
ANISOU 443 CB ASP A 76 6820 9896 6683 -106 -301 -498 C
ATOM 444 CG ASP A 76 -8.215 -12.436 36.741 1.00 81.62 C
ANISOU 444 CG ASP A 76 9319 12503 9192 -187 -302 -501 C
ATOM 445 OD1 ASP A 76 -8.230 -11.772 37.813 1.00 83.97 O
ANISOU 445 OD1 ASP A 76 9588 12825 9492 -262 -273 -522 O
ATOM 446 OD2 ASP A 76 -8.591 -11.967 35.630 1.00 87.79 O1-
ANISOU 446 OD2 ASP A 76 10109 13308 9939 -173 -336 -486 O1-
ATOM 447 N LEU A 77 -6.309 -16.614 37.760 1.00 59.85 N
ANISOU 447 N LEU A 77 6739 9448 6553 -20 -261 -502 N
ATOM 448 CA LEU A 77 -6.316 -18.026 38.136 1.00 61.08 C
ANISOU 448 CA LEU A 77 6949 9508 6750 64 -274 -534 C
ATOM 449 C LEU A 77 -5.539 -18.246 39.445 1.00 67.51 C
ANISOU 449 C LEU A 77 7754 10283 7614 -10 -222 -591 C
ATOM 450 O LEU A 77 -6.005 -19.002 40.302 1.00 68.90 O
ANISOU 450 O LEU A 77 7899 10458 7823 47 -234 -674 O
ATOM 451 CB LEU A 77 -5.714 -18.852 36.991 1.00 62.10 C
ANISOU 451 CB LEU A 77 7239 9495 6863 117 -285 -445 C
ATOM 452 CG LEU A 77 -6.380 -20.178 36.629 1.00 68.96 C
ANISOU 452 CG LEU A 77 8184 10285 7734 287 -358 -453 C
ATOM 453 CD1 LEU A 77 -7.877 -20.019 36.333 1.00 69.05 C
ANISOU 453 CD1 LEU A 77 8074 10446 7714 406 -441 -511 C
ATOM 454 CD2 LEU A 77 -5.717 -20.784 35.409 1.00 73.97 C
ANISOU 454 CD2 LEU A 77 9012 10772 8323 319 -363 -334 C
ATOM 455 N PHE A 78 -4.379 -17.552 39.614 1.00 62.71 N
ANISOU 455 N PHE A 78 7158 9662 7007 -131 -168 -563 N
ATOM 456 CA PHE A 78 -3.546 -17.582 40.826 1.00 62.34 C
ANISOU 456 CA PHE A 78 7085 9606 6995 -213 -126 -627 C
ATOM 457 C PHE A 78 -4.344 -17.108 42.012 1.00 63.36 C
ANISOU 457 C PHE A 78 7103 9861 7109 -211 -138 -705 C
ATOM 458 O PHE A 78 -4.350 -17.760 43.048 1.00 63.81 O
ANISOU 458 O PHE A 78 7141 9911 7193 -201 -130 -789 O
ATOM 459 CB PHE A 78 -2.303 -16.687 40.660 1.00 64.47 C
ANISOU 459 CB PHE A 78 7351 9893 7254 -325 -83 -598 C
ATOM 460 CG PHE A 78 -1.091 -17.291 39.990 1.00 67.50 C
ANISOU 460 CG PHE A 78 7830 10158 7658 -388 -32 -559 C
ATOM 461 CD1 PHE A 78 -1.213 -18.385 39.136 1.00 71.93 C
ANISOU 461 CD1 PHE A 78 8521 10584 8224 -337 -34 -500 C
ATOM 462 CD2 PHE A 78 0.169 -16.746 40.184 1.00 71.14 C
ANISOU 462 CD2 PHE A 78 8255 10651 8125 -501 18 -582 C
ATOM 463 CE1 PHE A 78 -0.092 -18.937 38.514 1.00 74.52 C
ANISOU 463 CE1 PHE A 78 8961 10794 8557 -424 29 -451 C
ATOM 464 CE2 PHE A 78 1.291 -17.295 39.558 1.00 75.59 C
ANISOU 464 CE2 PHE A 78 8896 11122 8703 -592 84 -555 C
ATOM 465 CZ PHE A 78 1.153 -18.387 38.724 1.00 74.72 C
ANISOU 465 CZ PHE A 78 8936 10863 8592 -565 98 -482 C
ATOM 466 N PHE A 79 -5.046 -15.981 41.842 1.00 57.55 N
ANISOU 466 N PHE A 79 6306 9237 6323 -226 -153 -680 N
ATOM 467 CA PHE A 79 -5.935 -15.377 42.831 1.00 56.88 C
ANISOU 467 CA PHE A 79 6134 9277 6200 -248 -153 -733 C
ATOM 468 C PHE A 79 -7.073 -16.340 43.177 1.00 58.71 C
ANISOU 468 C PHE A 79 6311 9550 6444 -167 -166 -810 C
ATOM 469 O PHE A 79 -7.388 -16.506 44.352 1.00 57.03 O
ANISOU 469 O PHE A 79 6041 9408 6218 -181 -145 -891 O
ATOM 470 CB PHE A 79 -6.505 -14.073 42.256 1.00 58.58 C
ANISOU 470 CB PHE A 79 6331 9563 6365 -287 -167 -677 C
ATOM 471 CG PHE A 79 -6.931 -13.045 43.266 1.00 61.10 C
ANISOU 471 CG PHE A 79 6611 9976 6627 -359 -153 -693 C
ATOM 472 CD1 PHE A 79 -8.221 -13.032 43.758 1.00 66.40 C
ANISOU 472 CD1 PHE A 79 7218 10747 7266 -376 -140 -739 C
ATOM 473 CD2 PHE A 79 -6.063 -12.031 43.657 1.00 64.21 C
ANISOU 473 CD2 PHE A 79 7042 10365 6991 -410 -154 -661 C
ATOM 474 CE1 PHE A 79 -8.627 -12.050 44.665 1.00 68.13 C
ANISOU 474 CE1 PHE A 79 7431 11042 7413 -464 -116 -736 C
ATOM 475 CE2 PHE A 79 -6.468 -11.048 44.561 1.00 67.31 C
ANISOU 475 CE2 PHE A 79 7437 10825 7313 -467 -150 -657 C
ATOM 476 CZ PHE A 79 -7.754 -11.050 45.041 1.00 66.05 C
ANISOU 476 CZ PHE A 79 7236 10746 7112 -504 -126 -684 C
ATOM 477 N LEU A 80 -7.653 -17.003 42.141 1.00 55.46 N
ANISOU 477 N LEU A 80 5918 9104 6051 -70 -206 -794 N
ATOM 478 CA LEU A 80 -8.766 -17.952 42.246 1.00 55.98 C
ANISOU 478 CA LEU A 80 5921 9218 6129 45 -239 -879 C
ATOM 479 C LEU A 80 -8.412 -19.201 43.069 1.00 60.01 C
ANISOU 479 C LEU A 80 6462 9650 6690 114 -235 -962 C
ATOM 480 O LEU A 80 -9.232 -19.613 43.888 1.00 59.00 O
ANISOU 480 O LEU A 80 6238 9620 6559 163 -234 -1075 O
ATOM 481 CB LEU A 80 -9.258 -18.386 40.844 1.00 56.23 C
ANISOU 481 CB LEU A 80 5988 9218 6160 156 -303 -837 C
ATOM 482 CG LEU A 80 -10.319 -17.512 40.184 1.00 59.41 C
ANISOU 482 CG LEU A 80 6297 9758 6515 135 -326 -834 C
ATOM 483 CD1 LEU A 80 -10.219 -17.567 38.675 1.00 58.43 C
ANISOU 483 CD1 LEU A 80 6252 9577 6373 200 -382 -752 C
ATOM 484 CD2 LEU A 80 -11.690 -17.906 40.618 1.00 63.80 C
ANISOU 484 CD2 LEU A 80 6707 10468 7067 197 -346 -958 C
ATOM 485 N LEU A 81 -7.213 -19.802 42.848 1.00 58.05 N
ANISOU 485 N LEU A 81 6346 9226 6486 111 -229 -918 N
ATOM 486 CA LEU A 81 -6.743 -21.018 43.552 1.00 59.72 C
ANISOU 486 CA LEU A 81 6619 9318 6754 164 -227 -997 C
ATOM 487 C LEU A 81 -6.805 -20.883 45.094 1.00 63.16 C
ANISOU 487 C LEU A 81 6958 9859 7182 110 -188 -1116 C
ATOM 488 O LEU A 81 -6.994 -21.895 45.767 1.00 64.21 O
ANISOU 488 O LEU A 81 7091 9955 7351 193 -199 -1227 O
ATOM 489 CB LEU A 81 -5.298 -21.408 43.134 1.00 60.34 C
ANISOU 489 CB LEU A 81 6853 9200 6873 97 -200 -925 C
ATOM 490 CG LEU A 81 -5.070 -21.826 41.664 1.00 66.25 C
ANISOU 490 CG LEU A 81 7743 9811 7618 149 -228 -805 C
ATOM 491 CD1 LEU A 81 -3.656 -21.490 41.200 1.00 66.43 C
ANISOU 491 CD1 LEU A 81 7859 9739 7643 1 -166 -718 C
ATOM 492 CD2 LEU A 81 -5.397 -23.297 41.424 1.00 69.91 C
ANISOU 492 CD2 LEU A 81 8329 10116 8119 310 -283 -830 C
ATOM 493 N THR A 82 -6.672 -19.635 45.634 1.00 57.21 N
ANISOU 493 N THR A 82 6133 9234 6372 -15 -150 -1095 N
ATOM 494 CA THR A 82 -6.685 -19.311 47.063 1.00 55.96 C
ANISOU 494 CA THR A 82 5899 9190 6173 -77 -115 -1186 C
ATOM 495 C THR A 82 -8.096 -19.281 47.645 1.00 59.81 C
ANISOU 495 C THR A 82 6264 9852 6608 -38 -105 -1271 C
ATOM 496 O THR A 82 -8.269 -19.635 48.810 1.00 61.18 O
ANISOU 496 O THR A 82 6384 10102 6758 -36 -79 -1386 O
ATOM 497 CB THR A 82 -5.995 -17.960 47.344 1.00 57.10 C
ANISOU 497 CB THR A 82 6042 9394 6261 -206 -94 -1117 C
ATOM 498 CG2 THR A 82 -4.613 -17.833 46.685 1.00 55.25 C
ANISOU 498 CG2 THR A 82 5893 9031 6070 -257 -95 -1046 C
ATOM 499 OG1 THR A 82 -6.854 -16.870 46.988 1.00 47.59 O
ANISOU 499 OG1 THR A 82 4792 8298 4992 -240 -93 -1051 O
ATOM 500 N VAL A 83 -9.086 -18.833 46.853 1.00 55.09 N