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*** ***elNémo ID: 2404101821253350890Job options:ID = 2404101821253350890 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:CRYST1 54.300 145.800 105.300 90.00 90.00 90.00 C 2 2 21 8 ATOM 1 N MET A 1 16.807 19.807 45.664 1.00 78.68 A N ANISOU 1 N MET A 1 11789 6426 11679 -920 -3273 -53 A N ATOM 2 CA MET A 1 16.753 18.367 46.021 1.00 75.46 A C ANISOU 2 CA MET A 1 11096 6663 10914 -779 -2837 -203 A C ATOM 3 C MET A 1 16.076 17.580 44.913 1.00 73.85 A C ANISOU 3 C MET A 1 10797 6798 10464 -700 -2528 42 A C ATOM 4 O MET A 1 15.232 18.106 44.189 1.00 71.64 A O ANISOU 4 O MET A 1 10683 6301 10234 -568 -2664 160 A O ATOM 5 CB MET A 1 16.000 18.157 47.334 1.00 72.49 A C ANISOU 5 CB MET A 1 10737 6387 10418 -335 -2858 -755 A C ATOM 6 CG MET A 1 16.458 16.938 48.121 1.00 82.02 A C ANISOU 6 CG MET A 1 11702 8107 11358 -328 -2560 -901 A C ATOM 7 SD MET A 1 16.108 16.949 49.901 1.00 95.84 A S ANISOU 7 SD MET A 1 13515 9940 12961 38 -2666 -1496 A S ATOM 8 CE MET A 1 15.795 18.677 50.261 1.00 85.33 A C ANISOU 8 CE MET A 1 12535 7923 11962 198 -3198 -1795 A C ATOM 9 N LYS A 2 16.445 16.312 44.801 1.00 68.68 A N ANISOU 9 N LYS A 2 9887 6656 9553 -763 -2153 97 A N ATOM 10 CA LYS A 2 15.884 15.404 43.813 1.00 61.36 A C ANISOU 10 CA LYS A 2 8862 6079 8371 -692 -1867 269 A C ATOM 11 C LYS A 2 15.292 14.200 44.530 1.00 58.49 A C ANISOU 11 C LYS A 2 8330 6102 7793 -411 -1629 -37 A C ATOM 12 O LYS A 2 15.796 13.772 45.573 1.00 58.82 A O ANISOU 12 O LYS A 2 8266 6276 7809 -400 -1574 -241 A O ATOM 13 CB LYS A 2 16.966 14.972 42.821 1.00 69.53 A C ANISOU 13 CB LYS A 2 9756 7356 9308 -1061 -1643 658 A C ATOM 14 CG LYS A 2 16.472 14.197 41.622 1.00 70.47 A C ANISOU 14 CG LYS A 2 9837 7791 9148 -1010 -1405 843 A C ATOM 15 CD LYS A 2 17.630 13.891 40.681 1.00 73.65 A C ANISOU 15 CD LYS A 2 10098 8460 9426 -1353 -1171 1193 A C ATOM 16 CE LYS A 2 17.149 13.333 39.354 1.00 80.88 A C ANISOU 16 CE LYS A 2 11050 9654 10028 -1308 -990 1382 A C ATOM 17 NZ LYS A 2 18.219 13.355 38.321 1.00 69.03 A N ANISOU 17 NZ LYS A 2 9457 8396 8373 -1644 -782 1763 A N ATOM 18 N ARG A 3 14.206 13.658 43.982 1.00 57.21 A N ANISOU 18 N ARG A 3 8143 6111 7481 -200 -1516 -47 A N ATOM 19 CA ARG A 3 13.617 12.447 44.540 1.00 50.94 A C ANISOU 19 CA ARG A 3 7174 5679 6503 -0 -1287 -261 A C ATOM 20 C ARG A 3 13.247 11.494 43.412 1.00 55.44 A C ANISOU 20 C ARG A 3 7658 6511 6895 -24 -1097 -87 A C ATOM 21 O ARG A 3 12.552 11.874 42.464 1.00 56.61 A O ANISOU 21 O ARG A 3 7904 6568 7036 30 -1199 43 A O ATOM 22 CB ARG A 3 12.390 12.772 45.406 1.00 53.22 A C ANISOU 22 CB ARG A 3 7481 5916 6825 352 -1385 -583 A C ATOM 23 CG ARG A 3 11.741 11.548 46.049 1.00 53.93 A C ANISOU 23 CG ARG A 3 7369 6395 6728 506 -1138 -750 A C ATOM 24 CD ARG A 3 10.907 11.939 47.260 1.00 61.42 A C ANISOU 24 CD ARG A 3 8299 7368 7670 810 -1184 -1092 A C ATOM 25 NE ARG A 3 9.933 12.965 46.909 1.00 66.41 A N ANISOU 25 NE ARG A 3 9014 7760 8459 1056 -1394 -1189 A N ATOM 26 CZ ARG A 3 9.777 14.121 47.542 1.00 71.33 A C ANISOU 26 CZ ARG A 3 9783 8099 9221 1263 -1629 -1441 A C ATOM 27 NH1 ARG A 3 10.466 14.416 48.634 1.00 74.62 A N ANISOU 27 NH1 ARG A 3 10284 8464 9606 1256 -1683 -1654 A N ATOM 28 NH2 ARG A 3 8.900 15.002 47.070 1.00 71.03 A N ANISOU 28 NH2 ARG A 3 9819 7806 9362 1506 -1851 -1503 A N ATOM 29 N LEU A 4 13.723 10.255 43.535 1.00 52.11 A N ANISOU 29 N LEU A 4 7074 6393 6333 -89 -861 -100 A N ATOM 30 CA LEU A 4 13.534 9.200 42.553 1.00 52.98 A C ANISOU 30 CA LEU A 4 7110 6747 6272 -109 -692 1 A C ATOM 31 C LEU A 4 12.698 8.068 43.136 1.00 50.38 A C ANISOU 31 C LEU A 4 6650 6615 5878 57 -586 -188 A C ATOM 32 O LEU A 4 12.909 7.644 44.277 1.00 48.44 A O ANISOU 32 O LEU A 4 6320 6441 5643 90 -523 -322 A O ATOM 33 CB LEU A 4 14.881 8.631 42.102 1.00 51.89 A C ANISOU 33 CB LEU A 4 6885 6777 6056 -319 -520 141 A C ATOM 34 CG LEU A 4 15.322 8.900 40.667 1.00 69.77 A C ANISOU 34 CG LEU A 4 9213 9099 8197 -479 -471 406 A C ATOM 35 CD1 LEU A 4 15.349 10.384 40.370 1.00 78.19 A C ANISOU 35 CD1 LEU A 4 10453 9870 9385 -602 -678 610 A C ATOM 36 CD2 LEU A 4 16.691 8.266 40.444 1.00 70.16 A C ANISOU 36 CD2 LEU A 4 9092 9386 8178 -637 -253 477 A C ATOM 37 N THR A 5 11.765 7.565 42.337 1.00 46.49 A N ANISOU 37 N THR A 5 6141 6213 5311 134 -584 -172 A N ATOM 38 CA THR A 5 10.937 6.421 42.702 1.00 45.48 A C ANISOU 38 CA THR A 5 5870 6259 5151 225 -500 -296 A C ATOM 39 C THR A 5 11.048 5.397 41.584 1.00 48.66 A C ANISOU 39 C THR A 5 6270 6786 5432 155 -441 -232 A C ATOM 40 O THR A 5 10.759 5.718 40.427 1.00 48.05 A O ANISOU 40 O THR A 5 6291 6693 5272 154 -531 -143 A O ATOM 41 CB THR A 5 9.470 6.824 42.897 1.00 49.50 A C ANISOU 41 CB THR A 5 6315 6752 5738 410 -611 -396 A C ATOM 42 CG2 THR A 5 8.670 5.650 43.421 1.00 51.72 A C ANISOU 42 CG2 THR A 5 6401 7235 6015 437 -504 -482 A C ATOM 43 OG1 THR A 5 9.370 7.915 43.818 1.00 48.85 A O ANISOU 43 OG1 THR A 5 6268 6539 5755 533 -688 -507 A O ATOM 44 N TYR A 6 11.460 4.172 41.911 1.00 46.53 A N ANISOU 44 N TYR A 6 5915 6627 5139 113 -320 -287 A N ATOM 45 CA TYR A 6 11.542 3.131 40.895 1.00 44.48 A C ANISOU 45 CA TYR A 6 5671 6455 4776 90 -293 -300 A C ATOM 46 C TYR A 6 11.044 1.805 41.457 1.00 43.90 A C ANISOU 46 C TYR A 6 5492 6410 4778 98 -280 -394 A C ATOM 47 O TYR A 6 10.893 1.627 42.667 1.00 43.46 A O ANISOU 47 O TYR A 6 5348 6354 4811 94 -239 -403 A O ATOM 48 CB TYR A 6 12.978 2.986 40.339 1.00 46.98 A C ANISOU 48 CB TYR A 6 6022 6843 4985 21 -171 -250 A C ATOM 49 CG TYR A 6 13.946 2.287 41.268 1.00 42.38 A C ANISOU 49 CG TYR A 6 5334 6282 4486 6 -70 -300 A C ATOM 50 CD1 TYR A 6 14.028 0.902 41.302 1.00 42.66 A C ANISOU 50 CD1 TYR A 6 5327 6343 4541 57 -49 -405 A C ATOM 51 CD2 TYR A 6 14.767 3.013 42.127 1.00 49.05 A C ANISOU 51 CD2 TYR A 6 6135 7091 5410 -53 -47 -247 A C ATOM 52 CE1 TYR A 6 14.895 0.255 42.164 1.00 52.06 A C ANISOU 52 CE1 TYR A 6 6433 7525 5823 68 -5 -430 A C ATOM 53 CE2 TYR A 6 15.646 2.373 42.987 1.00 46.95 A C ANISOU 53 CE2 TYR A 6 5769 6853 5216 -53 -2 -286 A C ATOM 54 CZ TYR A 6 15.705 0.996 42.999 1.00 49.06 A C ANISOU 54 CZ TYR A 6 5996 7150 5496 17 21 -365 A C ATOM 55 OH TYR A 6 16.562 0.357 43.863 1.00 49.90 A O ANISOU 55 OH TYR A 6 6015 7258 5687 41 20 -382 A O ATOM 56 N ILE A 7 10.758 0.884 40.538 1.00 45.02 A N ANISOU 56 N ILE A 7 5664 6572 4868 100 -335 -456 A N ATOM 57 CA ILE A 7 10.435 -0.501 40.856 1.00 45.77 A C ANISOU 57 CA ILE A 7 5697 6627 5065 71 -368 -530 A C ATOM 58 C ILE A 7 11.364 -1.412 40.065 1.00 49.38 A C ANISOU 58 C ILE A 7 6244 7078 5441 108 -351 -634 A C ATOM 59 O ILE A 7 11.847 -1.057 38.985 1.00 46.31 A O ANISOU 59 O ILE A 7 5950 6781 4865 156 -321 -666 A O ATOM 60 CB ILE A 7 8.938 -0.812 40.573 1.00 46.92 A C ANISOU 60 CB ILE A 7 5769 6763 5297 43 -525 -558 A C ATOM 61 CG1 ILE A 7 8.664 -0.998 39.078 1.00 51.88 A C ANISOU 61 CG1 ILE A 7 6515 7401 5796 79 -676 -650 A C ATOM 62 CG2 ILE A 7 8.057 0.270 41.181 1.00 57.75 A C ANISOU 62 CG2 ILE A 7 7022 8192 6728 78 -526 -494 A C ATOM 63 CD1 ILE A 7 7.342 -1.707 38.799 1.00 60.84 A C ANISOU 63 CD1 ILE A 7 7556 8497 7065 19 -885 -712 A C ATOM 64 N SER A 8 11.632 -2.590 40.619 1.00 43.95 A N ANISOU 64 N SER A 8 5528 6290 4883 100 -368 -684 A N ATOM 65 CA SER A 8 12.480 -3.557 39.940 1.00 44.97 A C ANISOU 65 CA SER A 8 5731 6382 4975 196 -378 -842 A C ATOM 66 C SER A 8 12.052 -4.959 40.342 1.00 48.24 A C ANISOU 66 C SER A 8 6154 6576 5599 163 -538 -900 A C ATOM 67 O SER A 8 11.263 -5.147 41.268 1.00 46.99 A O ANISOU 67 O SER A 8 5919 6339 5596 28 -590 -759 A O ATOM 68 CB SER A 8 13.963 -3.334 40.263 1.00 47.36 A C ANISOU 68 CB SER A 8 5983 6769 5244 268 -214 -826 A C ATOM 69 OG SER A 8 14.220 -3.605 41.634 1.00 50.17 A O ANISOU 69 OG SER A 8 6262 7030 5768 226 -218 -722 A O ATOM 70 N LYS A 9 12.588 -5.946 39.628 1.00 50.26 A N ANISOU 70 N LYS A 9 6506 6736 5856 288 -618 -1108 A N ATOM 71 CA LYS A 9 12.295 -7.353 39.857 1.00 50.03 A C ANISOU 71 CA LYS A 9 6534 6413 6063 268 -831 -1187 A C ATOM 72 C LYS A 9 13.530 -8.056 40.407 1.00 53.85 A C ANISOU 72 C LYS A 9 7020 6781 6660 410 -808 -1227 A C ATOM 73 O LYS A 9 14.652 -7.789 39.961 1.00 54.01 A O ANISOU 73 O LYS A 9 7014 6965 6541 599 -661 -1354 A O ATOM 74 CB LYS A 9 11.850 -8.027 38.551 1.00 57.80 A C ANISOU 74 CB LYS A 9 7663 7307 6992 343 -1030 -1467 A C ATOM 75 CG LYS A 9 11.288 -9.428 38.734 1.00 69.92 A C ANISOU 75 CG LYS A 9 9275 8462 8830 262 -1331 -1542 A C ATOM 76 CD LYS A 9 11.084 -10.178 37.407 1.00 83.29 A C ANISOU 76 CD LYS A 9 11153 10032 10461 392 -1571 -1912 A C ATOM 77 CE LYS A 9 12.295 -11.011 36.987 1.00114.69 A C ANISOU 77 CE LYS A 9 15258 13898 14422 702 -1590 -2228 A C ATOM 78 NZ LYS A 9 12.007 -12.475 37.027 1.00109.77 A N ANISOU 78 NZ LYS A 9 14785 12785 14138 699 -1964 -2402 A N ATOM 79 N PHE A 10 13.325 -8.948 41.379 1.00 54.89 A N ANISOU 79 N PHE A 10 7161 6644 7049 314 -959 -1091 A N ATOM 80 CA PHE A 10 14.411 -9.810 41.838 1.00 51.78 A C ANISOU 80 CA PHE A 10 6798 6065 6811 479 -1032 -1138 A C ATOM 81 C PHE A 10 14.999 -10.574 40.650 1.00 58.21 A C ANISOU 81 C PHE A 10 7719 6779 7620 755 -1130 -1523 A C ATOM 82 O PHE A 10 14.269 -11.227 39.900 1.00 57.02 A O ANISOU 82 O PHE A 10 7703 6437 7524 739 -1334 -1706 A O ATOM 83 CB PHE A 10 13.911 -10.824 42.878 1.00 61.98 A C ANISOU 83 CB PHE A 10 8148 7015 8387 307 -1255 -911 A C ATOM 84 CG PHE A 10 13.580 -10.246 44.248 1.00 55.27 A C ANISOU 84 CG PHE A 10 7197 6304 7500 91 -1137 -539 A C ATOM 85 CD1 PHE A 10 13.358 -8.895 44.441 1.00 52.33 A C ANISOU 85 CD1 PHE A 10 6704 6281 6900 31 -898 -462 A C ATOM 86 CD2 PHE A 10 13.464 -11.098 45.342 1.00 63.26 A C ANISOU 86 CD2 PHE A 10 8260 7080 8696 -45 -1291 -269 A C ATOM 87 CE1 PHE A 10 13.040 -8.399 45.702 1.00 53.05 A C ANISOU 87 CE1 PHE A 10 6720 6511 6926 -121 -800 -188 A C ATOM 88 CE2 PHE A 10 13.148 -10.608 46.602 1.00 63.54 A C ANISOU 88 CE2 PHE A 10 8220 7298 8625 -228 -1169 58 A C ATOM 89 CZ PHE A 10 12.933 -9.261 46.781 1.00 61.18 A C ANISOU 89 CZ PHE A 10 7794 7374 8078 -248 -917 67 A C ATOM 90 N ASER A 11 16.321 -10.496 40.478 0.70 58.65 A N ANISOU 90 N ASER A 11 7694 6983 7607 1019 -994 -1671 A N ATOM 91 N BSER A 11 16.322 -10.492 40.484 0.30 58.72 A N ANISOU 91 N BSER A 11 7702 6992 7616 1018 -993 -1669 A N ATOM 92 CA ASER A 11 16.972 -11.324 39.470 0.70 61.15 A C ANISOU 92 CA ASER A 11 8086 7230 7918 1345 -1069 -2075 A C ATOM 93 CA BSER A 11 16.994 -11.318 39.488 0.30 61.20 A C ANISOU 93 CA BSER A 11 8089 7239 7926 1347 -1066 -2072 A C ATOM 94 C ASER A 11 17.003 -12.787 39.887 0.70 61.19 A C ANISOU 94 C ASER A 11 8233 6728 8290 1450 -1417 -2165 A C ATOM 95 C BSER A 11 17.038 -12.781 39.906 0.30 61.39 A C ANISOU 95 C BSER A 11 8253 6757 8316 1455 -1412 -2163 A C ATOM 96 O ASER A 11 17.113 -13.669 39.029 0.70 66.98 A O ANISOU 96 O ASER A 11 9106 7266 9076 1691 -1594 -2544 A O ATOM 97 O BSER A 11 17.173 -13.659 39.047 0.30 67.01 A O ANISOU 97 O BSER A 11 9103 7279 9080 1702 -1585 -2545 A O ATOM 98 CB ASER A 11 18.396 -10.833 39.216 0.70 62.14 A C ANISOU 98 CB ASER A 11 8012 7709 7890 1600 -797 -2193 A C ATOM 99 CB BSER A 11 18.418 -10.812 39.249 0.30 62.20 A C ANISOU 99 CB BSER A 11 8013 7721 7898 1597 -792 -2184 A C ATOM 100 OG ASER A 11 19.248 -11.193 40.291 0.70 67.01 A O ANISOU 100 OG ASER A 11 8510 8196 8754 1687 -859 -2067 A O ATOM 101 OG BSER A 11 18.425 -9.661 38.426 0.30 63.44 A O ANISOU 101 OG BSER A 11 8098 8308 7699 1538 -510 -2181 A O ATOM 102 N AARG A 12 16.899 -13.052 41.184 0.70 64.25 A N ANISOU 102 N AARG A 12 8608 6889 8916 1276 -1537 -1823 A N ATOM 103 N BARG A 12 16.925 -13.055 41.201 0.30 64.34 A N ANISOU 103 N BARG A 12 8617 6901 8930 1280 -1536 -1822 A N ATOM 104 CA AARG A 12 16.951 -14.400 41.728 0.70 71.50 A C ANISOU 104 CA AARG A 12 9678 7283 10206 1330 -1897 -1802 A C ATOM 105 CA BARG A 12 16.976 -14.409 41.732 0.30 71.46 A C ANISOU 105 CA BARG A 12 9671 7277 10204 1337 -1898 -1805 A C ATOM 106 C AARG A 12 16.277 -14.386 43.091 0.70 68.49 A C ANISOU 106 C AARG A 12 9302 6767 9953 962 -1972 -1298 A C ATOM 107 C BARG A 12 16.350 -14.396 43.118 0.30 68.58 A C ANISOU 107 C BARG A 12 9310 6778 9968 978 -1972 -1299 A C ATOM 108 O AARG A 12 16.056 -13.314 43.667 0.70 63.38 A O ANISOU 108 O AARG A 12 8515 6470 9095 768 -1720 -1041 A O ATOM 109 O BARG A 12 16.224 -13.330 43.733 0.30 64.00 A O ANISOU 109 O BARG A 12 8586 6550 9181 800 -1719 -1042 A O ATOM 110 CB AARG A 12 18.403 -14.895 41.848 0.70 72.89 A C ANISOU 110 CB AARG A 12 9781 7406 10509 1739 -1936 -1995 A C ATOM 111 CB BARG A 12 18.424 -14.930 41.785 0.30 72.90 A C ANISOU 111 CB BARG A 12 9787 7401 10511 1758 -1941 -2021 A C ATOM 112 CG AARG A 12 19.171 -14.305 43.030 0.70 77.27 A C ANISOU 112 CG AARG A 12 10147 8161 11051 1702 -1806 -1669 A C ATOM 113 CG BARG A 12 19.061 -14.954 43.172 0.30 79.52 A C ANISOU 113 CG BARG A 12 10535 8177 11502 1725 -1996 -1667 A C ATOM 114 CD AARG A 12 20.665 -14.618 42.940 0.70 85.31 A C ANISOU 114 CD AARG A 12 11002 9240 12170 2138 -1808 -1913 A C ATOM 115 CD BARG A 12 20.542 -15.331 43.091 0.30 82.81 A C ANISOU 115 CD BARG A 12 10808 8618 12038 2181 -2024 -1921 A C ATOM 116 NE AARG A 12 21.475 -13.707 43.742 0.70 88.12 A N ANISOU 116 NE AARG A 12 11107 9949 12426 2101 -1615 -1685 A N ATOM 117 NE BARG A 12 21.391 -14.482 43.921 0.30 87.89 A N ANISOU 117 NE BARG A 12 11200 9610 12584 2168 -1837 -1693 A N ATOM 118 CZ AARG A 12 21.528 -13.717 45.068 0.70 90.62 A C ANISOU 118 CZ AARG A 12 11440 10151 12843 1941 -1758 -1310 A C ATOM 119 CZ BARG A 12 21.884 -13.308 43.548 0.30 87.28 A C ANISOU 119 CZ BARG A 12 10874 10055 12234 2165 -1477 -1749 A C ATOM 120 NH1AARG A 12 20.826 -14.582 45.783 0.70 90.10 A N ANISOU 120 NH1AARG A 12 11616 9646 12970 1780 -2062 -1060 A N ATOM 121 NH1BARG A 12 21.625 -12.794 42.356 0.30 82.06 A N ANISOU 121 NH1BARG A 12 10187 9670 11324 2177 -1231 -1990 A N ATOM 122 NH2AARG A 12 22.306 -12.837 45.693 0.70 88.58 A N ANISOU 122 NH2AARG A 12 10952 10230 12475 1924 -1608 -1171 A N ATOM 123 NH2BARG A 12 22.660 -12.634 44.392 0.30 86.22 A N ANISOU 123 NH2BARG A 12 10525 10159 12075 2131 -1391 -1543 A N ATOM 124 N PRO A 13 15.920 -15.551 43.623 1.00 74.22 A N ANISOU 124 N PRO A 13 10199 6993 11010 856 -2318 -1144 A N ATOM 125 CA PRO A 13 15.408 -15.600 44.997 1.00 72.40 A C ANISOU 125 CA PRO A 13 9969 6686 10853 513 -2363 -618 A C ATOM 126 C PRO A 13 16.387 -14.965 45.974 1.00 77.10 A C ANISOU 126 C PRO A 13 10434 7561 11298 618 -2192 -425 A C ATOM 127 O PRO A 13 17.581 -15.278 45.981 1.00 79.87 A O ANISOU 127 O PRO A 13 10764 7840 11741 953 -2276 -587 A O ATOM 128 CB PRO A 13 15.236 -17.100 45.268 1.00 80.89 A C ANISOU 128 CB PRO A 13 11276 7115 12342 463 -2812 -518 A C ATOM 129 CG PRO A 13 15.481 -17.809 43.965 1.00 85.68 A C ANISOU 129 CG PRO A 13 12016 7430 13109 775 -3025 -1054 A C ATOM 130 CD PRO A 13 15.663 -16.799 42.885 1.00 86.50 A C ANISOU 130 CD PRO A 13 11974 8037 12855 962 -2690 -1429 A C ATOM 131 N LEU A 14 15.871 -14.060 46.799 1.00 74.15 A N ANISOU 131 N LEU A 14 9957 7520 10695 348 -1969 -106 A N ATOM 132 CA LEU A 14 16.630 -13.429 47.868 1.00 65.35 A C ANISOU 132 CA LEU A 14 8749 6664 9415 387 -1852 102 A C ATOM 133 C LEU A 14 15.977 -13.778 49.197 1.00 72.43 A C ANISOU 133 C LEU A 14 9736 7480 10303 76 -1945 590 A C ATOM 134 O LEU A 14 14.755 -13.660 49.341 1.00 69.66 A O ANISOU 134 O LEU A 14 9375 7200 9892 -239 -1855 780 A O ATOM 135 CB LEU A 14 16.683 -11.909 47.696 1.00 61.09 A C ANISOU 135 CB LEU A 14 8025 6629 8557 376 -1501 7 A C ATOM 136 CG LEU A 14 17.165 -11.361 46.355 1.00 59.93 A C ANISOU 136 CG LEU A 14 7777 6659 8335 597 -1342 -390 A C ATOM 137 CD1 LEU A 14 17.112 -9.841 46.366 1.00 63.03 A C ANISOU 137 CD1 LEU A 14 8025 7479 8447 512 -1046 -376 A C ATOM 138 CD2 LEU A 14 18.574 -11.841 46.051 1.00 74.85 A C ANISOU 138 CD2 LEU A 14 9608 8475 10356 952 -1430 -621 A C ATOM 139 N SER A 15 16.785 -14.203 50.162 1.00 66.14 A N ANISOU 139 N SER A 15 9010 6571 9550 165 -2121 803 A N ATOM 140 CA SER A 15 16.252 -14.499 51.481 1.00 73.53 A C ANISOU 140 CA SER A 15 10050 7495 10393 -128 -2191 1307 A C ATOM 141 C SER A 15 16.006 -13.204 52.247 1.00 67.72 A C ANISOU 141 C SER A 15 9184 7307 9240 -252 -1870 1423 A C ATOM 142 O SER A 15 16.483 -12.128 51.879 1.00 59.65 A O ANISOU 142 O SER A 15 8014 6593 8059 -89 -1667 1139 A O ATOM 143 CB SER A 15 17.206 -15.396 52.265 1.00 74.93 A C ANISOU 143 CB SER A 15 10380 7359 10729 24 -2538 1519 A C ATOM 144 OG SER A 15 18.550 -14.994 52.077 1.00 81.22 A O ANISOU 144 OG SER A 15 11055 8278 11527 406 -2553 1223 A O ATOM 145 N GLY A 16 15.247 -13.315 53.335 1.00 66.09 A N ANISOU 145 N GLY A 16 9038 7221 8851 -548 -1829 1847 A N ATOM 146 CA GLY A 16 15.019 -12.150 54.169 1.00 70.84 A C ANISOU 146 CA GLY A 16 9545 8340 9032 -621 -1549 1923 A C ATOM 147 C GLY A 16 16.315 -11.551 54.682 1.00 66.85 A C ANISOU 147 C GLY A 16 9034 7994 8371 -362 -1608 1804 A C ATOM 148 O GLY A 16 16.452 -10.329 54.775 1.00 60.85 A O ANISOU 148 O GLY A 16 8160 7593 7368 -296 -1399 1607 A O ATOM 149 N AASP A 17 17.294 -12.402 54.997 0.53 64.96 A N ANISOU 149 N AASP A 17 8913 7462 8308 -206 -1932 1908 A N ATOM 150 N BASP A 17 17.282 -12.404 55.025 0.47 64.99 A N ANISOU 150 N BASP A 17 8919 7469 8306 -212 -1932 1918 A N ATOM 151 CA AASP A 17 18.540 -11.891 55.558 0.53 67.95 A C ANISOU 151 CA AASP A 17 9251 8002 8566 24 -2038 1820 A C ATOM 152 CA BASP A 17 18.548 -11.900 55.545 0.47 67.96 A C ANISOU 152 CA BASP A 17 9252 7997 8572 26 -2041 1817 A C ATOM 153 C AASP A 17 19.352 -11.133 54.514 0.53 64.84 A C ANISOU 153 C AASP A 17 8639 7694 8302 273 -1931 1352 A C ATOM 154 C BASP A 17 19.277 -11.073 54.496 0.47 64.83 A C ANISOU 154 C BASP A 17 8635 7712 8287 259 -1909 1348 A C ATOM 155 O AASP A 17 20.053 -10.174 54.858 0.53 61.40 A O ANISOU 155 O AASP A 17 8090 7540 7700 362 -1880 1224 A O ATOM 156 O BASP A 17 19.841 -10.018 54.807 0.47 61.03 A O ANISOU 156 O BASP A 17 8039 7535 7613 323 -1819 1214 A O ATOM 157 CB AASP A 17 19.354 -13.035 56.176 0.53 69.49 A C ANISOU 157 CB AASP A 17 9607 7856 8942 147 -2453 2073 A C ATOM 158 CB BASP A 17 19.428 -13.059 56.014 0.47 69.55 A C ANISOU 158 CB BASP A 17 9597 7832 8997 179 -2458 2022 A C ATOM 159 CG AASP A 17 19.799 -14.073 55.159 0.53 73.91 A C ANISOU 159 CG AASP A 17 10174 7922 9985 364 -2685 1884 A C ATOM 160 CG BASP A 17 18.981 -13.632 57.343 0.47 75.18 A C ANISOU 160 CG BASP A 17 10545 8540 9482 -55 -2608 2564 A C ATOM 161 OD1AASP A 17 18.930 -14.735 54.555 0.53 75.99 A O ANISOU 161 OD1AASP A 17 10524 7907 10443 215 -2684 1917 A O ATOM 162 OD1BASP A 17 18.142 -12.998 58.019 0.47 79.60 A O ANISOU 162 OD1BASP A 17 11119 9485 9642 -299 -2350 2739 A O ATOM 163 OD2AASP A 17 21.026 -14.250 54.992 0.53 77.98 A O ANISOU 163 OD2AASP A 17 10600 8333 10696 696 -2890 1687 A O ATOM 164 OD2BASP A 17 19.477 -14.716 57.719 0.47 85.93 A O ANISOU 164 OD2BASP A 17 12077 9523 11050 20 -2987 2819 A O ATOM 165 N GLU A 18 19.253 -11.523 53.240 1.00 61.23 A N ANISOU 165 N GLU A 18 8124 7018 8122 368 -1899 1100 A N ATOM 166 CA GLU A 18 19.951 -10.792 52.187 1.00 66.45 A C ANISOU 166 CA GLU A 18 8573 7825 8848 571 -1745 698 A C ATOM 167 C GLU A 18 19.325 -9.423 51.973 1.00 57.32 A C ANISOU 167 C GLU A 18 7323 7023 7430 417 -1423 596 A C ATOM 168 O GLU A 18 20.033 -8.441 51.717 1.00 58.40 A O ANISOU 168 O GLU A 18 7300 7385 7505 504 -1312 402 A O ATOM 169 CB GLU A 18 19.939 -11.587 50.882 1.00 65.01 A C ANISOU 169 CB GLU A 18 8389 7358 8953 726 -1788 443 A C ATOM 170 CG GLU A 18 20.665 -12.922 50.956 1.00 73.89 A C ANISOU 170 CG GLU A 18 9601 8076 10399 963 -2141 454 A C ATOM 171 CD GLU A 18 20.602 -13.683 49.643 1.00 91.17 A C ANISOU 171 CD GLU A 18 11813 9983 12843 1150 -2193 125 A C ATOM 172 OE1 GLU A 18 21.493 -13.469 48.792 1.00 87.76 A O ANISOU 172 OE1 GLU A 18 11193 9684 12468 1445 -2100 -234 A O ATOM 173 OE2 GLU A 18 19.651 -14.477 49.455 1.00 77.11 A O ANISOU 173 OE2 GLU A 18 10231 7873 11194 992 -2323 219 A O ATOM 174 N ILE A 19 17.994 -9.339 52.063 1.00 57.00 A N ANISOU 174 N ILE A 19 7365 7026 7267 183 -1290 731 A N ATOM 175 CA ILE A 19 17.321 -8.052 51.915 1.00 56.99 A C ANISOU 175 CA ILE A 19 7281 7332 7042 77 -1021 630 A C ATOM 176 C ILE A 19 17.703 -7.125 53.060 1.00 54.44 A C ANISOU 176 C ILE A 19 6952 7283 6452 65 -996 694 A C ATOM 177 O ILE A 19 17.939 -5.927 52.856 1.00 52.28 A O ANISOU 177 O ILE A 19 6585 7199 6079 99 -873 504 A O ATOM 178 CB ILE A 19 15.796 -8.250 51.828 1.00 65.54 A C ANISOU 178 CB ILE A 19 8401 8420 8082 -145 -905 761 A C ATOM 179 CG1 ILE A 19 15.419 -8.888 50.485 1.00 63.02 A C ANISOU 179 CG1 ILE A 19 8077 7855 8012 -126 -944 597 A C ATOM 180 CG2 ILE A 19 15.060 -6.918 52.002 1.00 53.92 A C ANISOU 180 CG2 ILE A 19 6843 7282 6361 -216 -661 690 A C ATOM 181 CD1 ILE A 19 14.307 -9.919 50.591 1.00 71.68 A C ANISOU 181 CD1 ILE A 19 9249 8744 9242 -350 -1039 821 A C ATOM 182 N AGLU A 20 17.755 -7.659 54.284 0.65 56.94 A N ANISOU 182 N AGLU A 20 7390 7608 6636 8 -1140 969 A N ATOM 183 N BGLU A 20 17.787 -7.660 54.278 0.35 57.04 A N ANISOU 183 N BGLU A 20 7401 7618 6652 13 -1144 966 A N ATOM 184 CA AGLU A 20 18.193 -6.860 55.424 0.65 60.29 A C ANISOU 184 CA AGLU A 20 7844 8297 6768 23 -1170 1000 A C ATOM 185 CA BGLU A 20 18.174 -6.831 55.413 0.35 60.26 A C ANISOU 185 CA BGLU A 20 7838 8298 6760 21 -1163 995 A C ATOM 186 C AGLU A 20 19.605 -6.338 55.210 0.65 57.29 A C ANISOU 186 C AGLU A 20 7340 7918 6509 201 -1304 782 A C ATOM 187 C BGLU A 20 19.628 -6.380 55.307 0.35 57.30 A C ANISOU 187 C BGLU A 20 7352 7921 6499 200 -1321 801 A C ATOM 188 O AGLU A 20 19.909 -5.185 55.538 0.65 52.45 A O ANISOU 188 O AGLU A 20 6678 7510 5739 205 -1267 633 A O ATOM 189 O BGLU A 20 19.978 -5.304 55.807 0.35 53.32 A O ANISOU 189 O BGLU A 20 6817 7629 5815 207 -1313 680 A O ATOM 190 CB AGLU A 20 18.139 -7.688 56.711 0.65 58.83 A C ANISOU 190 CB AGLU A 20 7836 8117 6398 -54 -1345 1365 A C ATOM 191 CB BGLU A 20 17.947 -7.591 56.721 0.35 59.65 A C ANISOU 191 CB BGLU A 20 7940 8258 6468 -78 -1301 1365 A C ATOM 192 CG AGLU A 20 16.900 -7.457 57.565 0.65 66.38 A C ANISOU 192 CG AGLU A 20 8875 9361 6987 -251 -1141 1571 A C ATOM 193 CG BGLU A 20 16.479 -7.735 57.139 0.35 64.78 A C ANISOU 193 CG BGLU A 20 8645 9071 6899 -307 -1084 1593 A C ATOM 194 CD AGLU A 20 16.811 -6.041 58.106 0.65 76.12 A C ANISOU 194 CD AGLU A 20 10079 10963 7882 -200 -990 1347 A C ATOM 195 CD BGLU A 20 15.705 -6.427 57.100 0.35 69.28 A C ANISOU 195 CD BGLU A 20 9113 9973 7238 -322 -791 1366 A C ATOM 196 OE1AGLU A 20 17.713 -5.630 58.869 0.65 67.31 A O ANISOU 196 OE1AGLU A 20 9028 9952 6594 -97 -1169 1293 A O ATOM 197 OE1BGLU A 20 16.104 -5.474 57.801 0.35 71.88 A O ANISOU 197 OE1BGLU A 20 9470 10542 7299 -231 -791 1224 A O ATOM 198 OE2AGLU A 20 15.835 -5.337 57.765 0.65 71.85 A O ANISOU 198 OE2AGLU A 20 9449 10584 7265 -247 -728 1206 A O ATOM 199 OE2BGLU A 20 14.689 -6.355 56.374 0.35 70.46 A O ANISOU 199 OE2BGLU A 20 9158 10122 7492 -412 -598 1314 A O ATOM 200 N ALA A 21 20.487 -7.179 54.669 1.00 51.54 A N ANISOU 200 N ALA A 21 6543 6959 6082 352 -1475 749 A N ATOM 201 CA ALA A 21 21.876 -6.766 54.491 1.00 52.79 A C ANISOU 201 CA ALA A 21 6509 7165 6384 517 -1595 565 A C ATOM 202 C ALA A 21 21.980 -5.648 53.461 1.00 50.17 A C ANISOU 202 C ALA A 21 5996 6968 6099 496 -1359 298 A C ATOM 203 O ALA A 21 22.804 -4.738 53.607 1.00 52.06 A O ANISOU 203 O ALA A 21 6089 7355 6336 500 -1394 184 A O ATOM 204 CB ALA A 21 22.736 -7.960 54.083 1.00 63.28 A C ANISOU 204 CB ALA A 21 7764 8240 8038 734 -1807 558 A C ATOM 205 N ILE A 22 21.143 -5.693 52.420 1.00 51.99 A N ANISOU 205 N ILE A 22 6241 7138 6373 450 -1147 219 A N ATOM 206 CA ILE A 22 21.080 -4.587 51.468 1.00 51.34 A C ANISOU 206 CA ILE A 22 6041 7184 6282 401 -931 30 A C ATOM 207 C ILE A 22 20.673 -3.306 52.178 1.00 56.50 A C ANISOU 207 C ILE A 22 6752 8002 6714 269 -882 28 A C ATOM 208 O ILE A 22 21.249 -2.237 51.943 1.00 51.22 A O ANISOU 208 O ILE A 22 5972 7422 6067 234 -856 -90 A O ATOM 209 CB ILE A 22 20.118 -4.923 50.313 1.00 55.19 A C ANISOU 209 CB ILE A 22 6579 7581 6810 380 -764 -33 A C ATOM 210 CG1 ILE A 22 20.732 -5.994 49.405 1.00 56.52 A C ANISOU 210 CG1 ILE A 22 6677 7599 7199 562 -815 -145 A C ATOM 211 CG2 ILE A 22 19.767 -3.656 49.516 1.00 57.03 A C ANISOU 211 CG2 ILE A 22 6760 7951 6957 294 -565 -153 A C ATOM 212 CD1 ILE A 22 19.724 -6.688 48.515 1.00 59.43 A C ANISOU 212 CD1 ILE A 22 7161 7809 7609 548 -763 -198 A C ATOM 213 N GLY A 23 19.687 -3.396 53.073 1.00 51.25 A N ANISOU 213 N GLY A 23 6257 7381 5836 194 -875 155 A N ATOM 214 CA GLY A 23 19.261 -2.219 53.808 1.00 51.21 A C ANISOU 214 CA GLY A 23 6319 7544 5595 131 -834 93 A C ATOM 215 C GLY A 23 20.325 -1.695 54.753 1.00 49.00 A C ANISOU 215 C GLY A 23 6029 7344 5244 159 -1048 48 A C ATOM 216 O GLY A 23 20.469 -0.480 54.921 1.00 51.31 A O ANISOU 216 O GLY A 23 6319 7701 5476 126 -1065 -111 A O ATOM 217 N ARG A 24 21.064 -2.599 55.405 1.00 51.58 A N ANISOU 217 N ARG A 24 6366 7643 5591 222 -1258 186 A N ATOM 218 CA ARG A 24 22.138 -2.178 56.299 1.00 52.74 A C ANISOU 218 CA ARG A 24 6484 7870 5684 254 -1522 143 A C ATOM 219 C ARG A 24 23.205 -1.400 55.542 1.00 56.11 A C ANISOU 219 C ARG A 24 6664 8272 6384 242 -1560 -37 A C ATOM 220 O ARG A 24 23.612 -0.310 55.959 1.00 52.95 A O ANISOU 220 O ARG A 24 6246 7936 5938 174 -1676 -170 A O ATOM 221 CB ARG A 24 22.783 -3.387 56.984 1.00 67.42 A C ANISOU 221 CB ARG A 24 8376 9673 7567 351 -1779 348 A C ATOM 222 CG ARG A 24 22.052 -3.893 58.198 1.00 68.00 A C ANISOU 222 CG ARG A 24 8714 9845 7277 314 -1840 579 A C ATOM 223 CD ARG A 24 22.977 -4.607 59.177 1.00 63.12 A C ANISOU 223 CD ARG A 24 8157 9216 6610 404 -2209 761 A C ATOM 224 NE ARG A 24 23.745 -5.706 58.596 1.00 56.02 A N ANISOU 224 NE ARG A 24 7125 8066 6093 539 -2369 847 A N ATOM 225 CZ ARG A 24 23.217 -6.841 58.152 1.00 64.56 A C ANISOU 225 CZ ARG A 24 8282 8925 7322 551 -2315 1025 A C ATOM 226 NH1 ARG A 24 21.910 -7.039 58.149 1.00 54.89 A N ANISOU 226 NH1 ARG A 24 7222 7710 5923 394 -2085 1166 A N ATOM 227 NH2 ARG A 24 24.022 -7.801 57.707 1.00 62.92 A N ANISOU 227 NH2 ARG A 24 7967 8471 7469 733 -2517 1046 A N ATOM 228 N ILE A 25 23.710 -1.973 54.445 1.00 47.01 A N ANISOU 228 N ILE A 25 5310 7033 5517 304 -1476 -43 A N ATOM 229 CA ILE A 25 24.767 -1.295 53.702 1.00 53.93 A C ANISOU 229 CA ILE A 25 5901 7954 6637 268 -1467 -167 A C ATOM 230 C ILE A 25 24.231 0.000 53.114 1.00 49.20 A C ANISOU 230 C ILE A 25 5335 7365 5995 105 -1287 -263 A C ATOM 231 O ILE A 25 24.924 1.026 53.096 1.00 50.38 A O ANISOU 231 O ILE A 25 5352 7542 6247 -19 -1370 -334 A O ATOM 232 CB ILE A 25 25.336 -2.218 52.612 1.00 55.42 A C ANISOU 232 CB ILE A 25 5866 8112 7078 408 -1362 -180 A C ATOM 233 CG1 ILE A 25 26.221 -3.294 53.236 1.00 62.77 A C ANISOU 233 CG1 ILE A 25 6700 9005 8143 601 -1631 -118 A C ATOM 234 CG2 ILE A 25 26.129 -1.417 51.588 1.00 57.80 A C ANISOU 234 CG2 ILE A 25 5866 8535 7562 325 -1214 -279 A C ATOM 235 CD1 ILE A 25 26.350 -4.535 52.381 1.00 70.30 A C ANISOU 235 CD1 ILE A 25 7574 9846 9289 816 -1561 -148 A C ATOM 236 N SER A 26 22.992 -0.029 52.625 1.00 48.87 A N ANISOU 236 N SER A 26 5463 7276 5831 95 -1074 -252 A N ATOM 237 CA ASER A 26 22.375 1.172 52.067 0.82 52.73 A C ANISOU 237 CA ASER A 26 6011 7739 6286 -23 -941 -329 A C ATOM 238 CA BSER A 26 22.409 1.179 52.061 0.18 52.71 A C ANISOU 238 CA BSER A 26 6003 7737 6288 -24 -943 -329 A C ATOM 239 C SER A 26 22.278 2.273 53.114 1.00 52.06 A C ANISOU 239 C SER A 26 6059 7652 6071 -85 -1112 -426 A C ATOM 240 O SER A 26 22.539 3.446 52.826 1.00 50.88 A O ANISOU 240 O SER A 26 5881 7432 6020 -204 -1156 -505 A O ATOM 241 CB ASER A 26 20.979 0.854 51.525 0.82 49.32 A C ANISOU 241 CB ASER A 26 5727 7270 5740 9 -737 -304 A C ATOM 242 CB BSER A 26 21.052 0.869 51.442 0.18 49.58 A C ANISOU 242 CB BSER A 26 5745 7302 5790 6 -734 -306 A C ATOM 243 OG ASER A 26 21.021 -0.039 50.430 0.82 47.02 A O ANISOU 243 OG ASER A 26 5347 6954 5564 65 -606 -270 A O ATOM 244 OG BSER A 26 20.402 2.076 51.110 0.18 51.16 A O ANISOU 244 OG BSER A 26 6027 7462 5949 -70 -669 -378 A O ATOM 245 N SER A 27 21.879 1.908 54.336 1.00 52.61 A N ANISOU 245 N SER A 27 6294 7793 5902 -7 -1220 -420 A N ATOM 246 CA ASER A 27 21.798 2.883 55.418 0.56 58.27 A C ANISOU 246 CA ASER A 27 7164 8543 6432 -17 -1398 -571 A C ATOM 247 CA BSER A 27 21.797 2.885 55.415 0.44 58.26 A C ANISOU 247 CA BSER A 27 7163 8542 6431 -17 -1398 -571 A C ATOM 248 C SER A 27 23.153 3.529 55.673 1.00 57.19 A C ANISOU 248 C SER A 27 6892 8362 6477 -112 -1679 -651 A C ATOM 249 O SER A 27 23.257 4.753 55.812 1.00 60.07 A O ANISOU 249 O SER A 27 7312 8628 6884 -199 -1810 -813 A O ATOM 250 CB ASER A 27 21.286 2.208 56.691 0.56 60.82 A C ANISOU 250 CB ASER A 27 7671 9031 6408 85 -1452 -513 A C ATOM 251 CB BSER A 27 21.274 2.215 56.686 0.44 60.83 A C ANISOU 251 CB BSER A 27 7673 9032 6409 85 -1449 -514 A C ATOM 252 OG ASER A 27 21.077 3.160 57.716 0.56 72.20 A O ANISOU 252 OG ASER A 27 9287 10550 7594 120 -1593 -713 A O ATOM 253 OG BSER A 27 20.819 3.179 57.615 0.44 71.88 A O ANISOU 253 OG BSER A 27 9259 10512 7539 127 -1534 -715 A O ATOM 254 N GLN A 28 24.207 2.712 55.747 1.00 53.64 A N ANISOU 254 N GLN A 28 6251 7964 6168 -94 -1806 -544 A N ATOM 255 CA GLN A 28 25.528 3.229 56.072 1.00 53.39 A C ANISOU 255 CA GLN A 28 6026 7929 6330 -190 -2103 -607 A C ATOM 256 C GLN A 28 26.020 4.214 55.024 1.00 58.07 A C ANISOU 256 C GLN A 28 6412 8421 7233 -391 -2033 -635 A C ATOM 257 O GLN A 28 26.582 5.261 55.361 1.00 59.65 A O ANISOU 257 O GLN A 28 6579 8537 7549 -550 -2275 -742 A O ATOM 258 CB GLN A 28 26.517 2.072 56.206 1.00 54.06 A C ANISOU 258 CB GLN A 28 5888 8102 6552 -88 -2231 -479 A C ATOM 259 CG GLN A 28 26.278 1.206 57.432 1.00 61.92 A C ANISOU 259 CG GLN A 28 7102 9173 7250 66 -2416 -399 A C ATOM 260 CD GLN A 28 27.017 -0.120 57.367 1.00 67.68 A C ANISOU 260 CD GLN A 28 7653 9914 8147 217 -2517 -238 A C ATOM 261 NE2 GLN A 28 26.487 -1.127 58.055 1.00 65.12 A N ANISOU 261 NE2 GLN A 28 7561 9593 7589 340 -2568 -73 A N ATOM 262 OE1 GLN A 28 28.055 -0.234 56.713 1.00 64.22 A O ANISOU 262 OE1 GLN A 28 6864 9483 8052 228 -2552 -256 A O ATOM 263 N ALYS A 29 25.829 3.890 53.743 0.45 51.27 A N ANISOU 263 N ALYS A 29 5418 7562 6500 -402 -1723 -528 A N ATOM 264 N BLYS A 29 25.830 3.889 53.744 0.55 51.20 A N ANISOU 264 N BLYS A 29 5410 7554 6491 -402 -1724 -528 A N ATOM 265 CA ALYS A 29 26.327 4.758 52.681 0.45 57.81 A C ANISOU 265 CA ALYS A 29 6045 8342 7579 -616 -1625 -485 A C ATOM 266 CA BLYS A 29 26.326 4.759 52.682 0.55 57.81 A C ANISOU 266 CA BLYS A 29 6044 8342 7578 -616 -1626 -485 A C ATOM 267 C ALYS A 29 25.463 6.006 52.535 0.45 57.72 A C ANISOU 267 C ALYS A 29 6287 8132 7511 -731 -1621 -553 A C ATOM 268 C BLYS A 29 25.463 6.007 52.541 0.55 57.74 A C ANISOU 268 C BLYS A 29 6290 8134 7513 -731 -1623 -554 A C ATOM 269 O ALYS A 29 25.986 7.116 52.376 0.45 56.34 A O ANISOU 269 O ALYS A 29 6049 7824 7535 -959 -1767 -556 A O ATOM 270 O BLYS A 29 25.985 7.120 52.399 0.55 56.30 A O ANISOU 270 O BLYS A 29 6046 7817 7528 -958 -1773 -559 A O ATOM 271 CB ALYS A 29 26.385 3.977 51.367 0.45 59.49 A C ANISOU 271 CB ALYS A 29 6065 8671 7868 -559 -1296 -366 A C ATOM 272 CB BLYS A 29 26.383 3.978 51.368 0.55 59.49 A C ANISOU 272 CB BLYS A 29 6066 8670 7867 -559 -1296 -366 A C ATOM 273 CG ALYS A 29 27.409 2.842 51.389 0.45 60.61 A C ANISOU 273 CG ALYS A 29 5903 8983 8144 -415 -1323 -338 A C ATOM 274 CG BLYS A 29 27.426 2.858 51.392 0.55 60.61 A C ANISOU 274 CG BLYS A 29 5898 8983 8146 -418 -1326 -337 A C ATOM 275 CD ALYS A 29 27.499 2.113 50.056 0.45 63.06 A C ANISOU 275 CD ALYS A 29 6032 9420 8508 -317 -999 -292 A C ATOM 276 CD BLYS A 29 27.403 2.005 50.130 0.55 63.00 A C ANISOU 276 CD BLYS A 29 6056 9401 8481 -291 -1006 -297 A C ATOM 277 CE ALYS A 29 28.373 2.864 49.066 0.45 66.17 A C ANISOU 277 CE ALYS A 29 6089 9965 9087 -531 -844 -215 A C ATOM 278 CE BLYS A 29 28.177 2.654 48.993 0.55 66.28 A C ANISOU 278 CE BLYS A 29 6151 9973 9060 -478 -809 -225 A C ATOM 279 NZ ALYS A 29 28.065 2.486 47.658 0.45 65.05 A N ANISOU 279 NZ ALYS A 29 5907 9950 8857 -466 -482 -183 A N ATOM 280 NZ BLYS A 29 29.598 2.927 49.352 0.55 69.04 A N ANISOU 280 NZ BLYS A 29 6090 10465 9676 -592 -980 -205 A N ATOM 281 N ASN A 30 24.142 5.848 52.607 1.00 54.11 A N ANISOU 281 N ASN A 30 6106 7637 6815 -578 -1482 -604 A N ATOM 282 CA ASN A 30 23.251 6.991 52.432 1.00 56.01 A C ANISOU 282 CA ASN A 30 6574 7685 7024 -620 -1487 -691 A C ATOM 283 C ASN A 30 23.469 8.036 53.520 1.00 56.19 A C ANISOU 283 C ASN A 30 6748 7557 7045 -665 -1830 -897 A C ATOM 284 O ASN A 30 23.466 9.242 53.245 1.00 57.46 A O ANISOU 284 O ASN A 30 6989 7471 7372 -807 -1964 -949 A O ATOM 285 CB ASN A 30 21.797 6.521 52.426 1.00 50.98 A C ANISOU 285 CB ASN A 30 6137 7094 6139 -416 -1285 -726 A C ATOM 286 CG ASN A 30 21.420 5.768 51.159 1.00 53.48 A C ANISOU 286 CG ASN A 30 6358 7477 6485 -398 -997 -565 A C ATOM 287 ND2 ASN A 30 20.164 5.343 51.086 1.00 50.07 A N ANISOU 287 ND2 ASN A 30 6056 7080 5886 -258 -848 -582 A N ATOM 288 OD1 ASN A 30 22.241 5.568 50.260 1.00 50.02 A O ANISOU 288 OD1 ASN A 30 5716 7084 6207 -506 -912 -441 A O ATOM 289 N GLN A 31 23.663 7.593 54.766 1.00 55.83 A N ANISOU 289 N GLN A 31 6769 7639 6806 -545 -2007 -1017 A N ATOM 290 CA GLN A 31 23.916 8.533 55.852 1.00 56.36 A C ANISOU 290 CA GLN A 31 7002 7589 6823 -563 -2369 -1265 A C ATOM 291 C GLN A 31 25.079 9.458 55.522 1.00 63.51 A C ANISOU 291 C GLN A 31 7731 8286 8112 -858 -2634 -1246 A C ATOM 292 O GLN A 31 25.017 10.666 55.779 1.00 67.39 A O ANISOU 292 O GLN A 31 8394 8505 8707 -947 -2891 -1430 A O ATOM 293 CB GLN A 31 24.201 7.764 57.143 1.00 63.07 A C ANISOU 293 CB GLN A 31 7908 8667 7388 -419 -2536 -1334 A C ATOM 294 CG GLN A 31 24.338 8.640 58.377 1.00 83.28 A C ANISOU 294 CG GLN A 31 10697 11164 9783 -381 -2918 -1645 A C ATOM 295 CD GLN A 31 23.767 7.981 59.616 1.00 98.37 A C ANISOU 295 CD GLN A 31 12832 13357 11188 -137 -2923 -1736 A C ATOM 296 NE2 GLN A 31 22.763 8.614 60.215 1.00113.30 A N ANISOU 296 NE2 GLN A 31 15007 15269 12774 41 -2898 -2005 A N ATOM 297 OE1 GLN A 31 24.212 6.906 60.022 1.00 93.25 A O ANISOU 297 OE1 GLN A 31 12097 12917 10417 -99 -2944 -1555 A O ATOM 298 N GLN A 32 26.156 8.906 54.959 1.00 61.37 A N ANISOU 298 N GLN A 32 7102 8139 8077 -1014 -2585 -1031 A N ATOM 299 CA GLN A 32 27.314 9.725 54.630 1.00 65.29 A C ANISOU 299 CA GLN A 32 7348 8498 8960 -1343 -2807 -962 A C ATOM 300 C GLN A 32 26.999 10.728 53.530 1.00 69.31 A C ANISOU 300 C GLN A 32 7899 8754 9680 -1560 -2691 -837 A C ATOM 301 O GLN A 32 27.581 11.822 53.507 1.00 70.48 A O ANISOU 301 O GLN A 32 8014 8646 10121 -1851 -2969 -835 A O ATOM 302 CB GLN A 32 28.481 8.841 54.193 1.00 75.69 A C ANISOU 302 CB GLN A 32 8206 10080 10471 -1421 -2712 -758 A C ATOM 303 CG GLN A 32 28.979 7.895 55.251 1.00 73.10 A C ANISOU 303 CG GLN A 32 7810 9957 10006 -1228 -2911 -838 A C ATOM 304 CD GLN A 32 30.173 7.100 54.776 1.00 61.84 A C ANISOU 304 CD GLN A 32 5891 8769 8837 -1266 -2849 -668 A C ATOM 305 NE2 GLN A 32 29.935 5.855 54.386 1.00 76.69 A N ANISOU 305 NE2 GLN A 32 7710 10829 10598 -1018 -2567 -575 A N ATOM 306 OE1 GLN A 32 31.291 7.609 54.727 1.00 70.58 A O ANISOU 306 OE1 GLN A 32 6655 9891 10270 -1514 -3055 -629 A O ATOM 307 N ALA A 33 26.101 10.371 52.612 1.00 67.61 A N ANISOU 307 N ALA A 33 7762 8590 9335 -1442 -2321 -712 A N ATOM 308 CA ALA A 33 25.768 11.200 51.464 1.00 67.89 A C ANISOU 308 CA ALA A 33 7848 8421 9525 -1627 -2198 -536 A C ATOM 309 C ALA A 33 24.571 12.105 51.718 1.00 72.57 A C ANISOU 309 C ALA A 33 8849 8695 10030 -1493 -2326 -724 A C ATOM 310 O ALA A 33 24.117 12.786 50.791 1.00 72.20 A O ANISOU 310 O ALA A 33 8902 8441 10089 -1594 -2258 -575 A O ATOM 311 CB ALA A 33 25.493 10.317 50.244 1.00 65.18 A C ANISOU 311 CB ALA A 33 7359 8328 9077 -1561 -1761 -308 A C ATOM 312 N AASN A 34 24.058 12.138 52.946 0.46 67.36 A N ANISOU 312 N AASN A 34 8420 8008 9164 -1248 -2515 -1047 A N ATOM 313 N BASN A 34 24.055 12.130 52.945 0.54 67.34 A N ANISOU 313 N BASN A 34 8418 8009 9161 -1247 -2513 -1047 A N ATOM 314 CA AASN A 34 22.869 12.924 53.268 0.46 66.95 A C ANISOU 314 CA AASN A 34 8721 7714 9002 -1035 -2610 -1293 A C ATOM 315 CA BASN A 34 22.869 12.918 53.270 0.54 66.93 A C ANISOU 315 CA BASN A 34 8718 7714 8999 -1034 -2609 -1293 A C ATOM 316 C AASN A 34 21.722 12.560 52.330 0.46 66.42 A C ANISOU 316 C AASN A 34 8704 7722 8811 -873 -2259 -1159 A C ATOM 317 C BASN A 34 21.724 12.560 52.330 0.54 66.41 A C ANISOU 317 C BASN A 34 8703 7721 8810 -874 -2259 -1159 A C ATOM 318 O AASN A 34 21.020 13.425 51.802 0.46 67.82 A O ANISOU 318 O AASN A 34 9058 7620 9092 -847 -2310 -1167 A O ATOM 319 O BASN A 34 21.029 13.428 51.796 0.54 67.84 A O ANISOU 319 O BASN A 34 9058 7620 9096 -850 -2311 -1165 A O ATOM 320 CB AASN A 34 23.165 14.424 53.213 0.46 70.34 A C ANISOU 320 CB AASN A 34 9306 7661 9760 -1247 -2991 -1367 A C ATOM 321 CB BASN A 34 23.174 14.415 53.224 0.54 70.34 A C ANISOU 321 CB BASN A 34 9303 7663 9758 -1247 -2992 -1368 A C ATOM 322 CG AASN A 34 24.074 14.882 54.339 0.46 73.75 A C ANISOU 322 CG AASN A 34 9758 7975 10288 -1357 -3424 -1609 A C ATOM 323 CG BASN A 34 22.184 15.237 54.031 0.54 74.53 A C ANISOU 323 CG BASN A 34 10205 7942 10172 -949 -3220 -1777 A C ATOM 324 ND2AASN A 34 24.956 15.827 54.039 0.46 77.59 A N ANISOU 324 ND2AASN A 34 10178 8119 11182 -1734 -3733 -1498 A N ATOM 325 ND2BASN A 34 21.993 16.491 53.635 0.54 75.61 A N ANISOU 325 ND2BASN A 34 10538 7591 10601 -1044 -3481 -1809 A N ATOM 326 OD1AASN A 34 23.980 14.396 55.466 0.46 76.11 A O ANISOU 326 OD1AASN A 34 10136 8493 10290 -1124 -3499 -1876 A O ATOM 327 OD1BASN A 34 21.602 14.751 55.000 0.54 76.65 A O ANISOU 327 OD1BASN A 34 10581 8456 10086 -628 -3164 -2056 A O ATOM 328 N VAL A 35 21.547 11.260 52.110 1.00 59.58 A N ANISOU 328 N VAL A 35 7683 7209 7745 -765 -1942 -1035 A N ATOM 329 CA VAL A 35 20.461 10.717 51.306 1.00 60.27 A C ANISOU 329 CA VAL A 35 7794 7408 7696 -611 -1633 -932 A C ATOM 330 C VAL A 35 19.506 9.999 52.248 1.00 54.33 A C ANISOU 330 C VAL A 35 7135 6877 6630 -315 -1530 -1124 A C ATOM 331 O VAL A 35 19.937 9.386 53.229 1.00 54.38 A O ANISOU 331 O VAL A 35 7109 7068 6485 -267 -1582 -1199 A O ATOM 332 CB VAL A 35 21.006 9.765 50.224 1.00 52.84 A C ANISOU 332 CB VAL A 35 6606 6677 6792 -739 -1368 -645 A C ATOM 333 CG1 VAL A 35 19.896 8.917 49.638 1.00 52.76 A C ANISOU 333 CG1 VAL A 35 6625 6825 6598 -552 -1094 -598 A C ATOM 334 CG2 VAL A 35 21.739 10.561 49.141 1.00 61.29 A C ANISOU 334 CG2 VAL A 35 7583 7591 8113 -1038 -1395 -410 A C ATOM 335 N THR A 36 18.209 10.098 51.972 1.00 52.87 A N ANISOU 335 N THR A 36 7052 6689 6345 -125 -1395 -1183 A N ATOM 336 CA THR A 36 17.203 9.411 52.767 1.00 48.23 A C ANISOU 336 CA THR A 36 6497 6361 5465 119 -1242 -1315 A C ATOM 337 C THR A 36 16.260 8.682 51.824 1.00 53.65 A C ANISOU 337 C THR A 36 7092 7165 6126 170 -975 -1150 A C ATOM 338 O THR A 36 16.219 8.959 50.622 1.00 53.38 A O ANISOU 338 O THR A 36 7036 6986 6261 78 -947 -1004 A O ATOM 339 CB THR A 36 16.404 10.372 53.655 1.00 55.17 A C ANISOU 339 CB THR A 36 7563 7170 6229 357 -1375 -1651 A C ATOM 340 CG2 THR A 36 17.279 10.958 54.733 1.00 60.67 A C ANISOU 340 CG2 THR A 36 8380 7782 6891 332 -1671 -1870 A C ATOM 341 OG1 THR A 36 15.856 11.431 52.857 1.00 57.02 A O ANISOU 341 OG1 THR A 36 7886 7096 6682 402 -1469 -1694 A O ATOM 342 N GLY A 37 15.492 7.748 52.368 1.00 49.64 A N ANISOU 342 N GLY A 37 6537 6927 5397 298 -796 -1158 A N ATOM 343 CA GLY A 37 14.556 7.027 51.532 1.00 53.89 A C ANISOU 343 CA GLY A 37 6976 7562 5937 324 -589 -1021 A C ATOM 344 C GLY A 37 14.021 5.781 52.211 1.00 53.93 A C ANISOU 344 C GLY A 37 6901 7852 5737 363 -417 -950 A C ATOM 345 O GLY A 37 14.241 5.541 53.400 1.00 50.73 A O ANISOU 345 O GLY A 37 6539 7606 5132 402 -437 -1004 A O ATOM 346 N VAL A 38 13.316 4.990 51.407 1.00 51.03 A N ANISOU 346 N VAL A 38 6431 7538 5420 333 -273 -809 A N ATOM 347 CA AVAL A 38 12.656 3.783 51.879 0.77 49.05 A C ANISOU 347 CA AVAL A 38 6093 7506 5039 318 -123 -689 A C ATOM 348 CA BVAL A 38 12.627 3.791 51.865 0.23 49.36 A C ANISOU 348 CA BVAL A 38 6131 7546 5079 319 -121 -690 A C ATOM 349 C VAL A 38 12.776 2.713 50.802 1.00 53.16 A C ANISOU 349 C VAL A 38 6545 7945 5708 196 -86 -511 A C ATOM 350 O VAL A 38 12.788 3.005 49.603 1.00 48.75 A O ANISOU 350 O VAL A 38 5982 7251 5291 178 -110 -513 A O ATOM 351 CB AVAL A 38 11.182 4.084 52.242 0.77 55.67 A C ANISOU 351 CB AVAL A 38 6845 8534 5774 453 5 -785 A C ATOM 352 CB BVAL A 38 11.135 4.063 52.151 0.23 55.79 A C ANISOU 352 CB BVAL A 38 6852 8542 5802 450 8 -779 A C ATOM 353 CG1AVAL A 38 10.370 4.354 50.988 0.77 53.89 A C ANISOU 353 CG1AVAL A 38 6538 8199 5741 481 8 -787 A C ATOM 354 CG1BVAL A 38 10.451 2.808 52.674 0.23 59.30 A C ANISOU 354 CG1BVAL A 38 7176 9230 6126 364 172 -596 A C ATOM 355 CG2AVAL A 38 10.590 2.955 53.057 0.77 59.00 A C ANISOU 355 CG2AVAL A 38 7169 9231 6017 391 166 -629 A C ATOM 356 CG2BVAL A 38 10.987 5.208 53.131 0.23 58.44 A C ANISOU 356 CG2BVAL A 38 7268 8952 5984 640 -35 -1036 A C ATOM 357 N LEU A 39 12.896 1.465 51.248 1.00 48.06 A N ANISOU 357 N LEU A 39 5873 7374 5014 119 -49 -359 A N ATOM 358 CA LEU A 39 13.030 0.308 50.371 1.00 44.52 A C ANISOU 358 CA LEU A 39 5387 6816 4712 33 -53 -233 A C ATOM 359 C LEU A 39 11.989 -0.715 50.793 1.00 49.73 A C ANISOU 359 C LEU A 39 5982 7575 5336 -46 21 -84 A C ATOM 360 O LEU A 39 11.999 -1.174 51.937 1.00 49.28 A O ANISOU 360 O LEU A 39 5947 7643 5134 -85 42 37 A O ATOM 361 CB LEU A 39 14.437 -0.286 50.453 1.00 45.46 A C ANISOU 361 CB LEU A 39 5541 6840 4890 14 -153 -181 A C ATOM 362 CG LEU A 39 14.700 -1.573 49.671 1.00 53.41 A C ANISOU 362 CG LEU A 39 6530 7714 6049 -14 -185 -105 A C ATOM 363 CD1 LEU A 39 14.432 -1.351 48.194 1.00 49.44 A C ANISOU 363 CD1 LEU A 39 6004 7143 5637 -1 -145 -200 A C ATOM 364 CD2 LEU A 39 16.130 -2.076 49.898 1.00 60.54 A C ANISOU 364 CD2 LEU A 39 7428 8551 7024 31 -293 -86 A C ATOM 365 N LEU A 40 11.083 -1.059 49.886 1.00 49.40 A N ANISOU 365 N LEU A 40 5860 7491 5419 -91 45 -73 A N ATOM 366 CA LEU A 40 10.057 -2.052 50.159 1.00 47.44 A C ANISOU 366 CA LEU A 40 5511 7311 5202 -224 92 92 A C ATOM 367 C LEU A 40 10.244 -3.230 49.222 1.00 50.67 A C ANISOU 367 C LEU A 40 5957 7476 5817 -316 -35 148 A C ATOM 368 O LEU A 40 10.702 -3.073 48.089 1.00 49.93 A O ANISOU 368 O LEU A 40 5917 7244 5808 -244 -105 8 A O ATOM 369 CB LEU A 40 8.656 -1.474 49.975 1.00 54.15 A C ANISOU 369 CB LEU A 40 6184 8333 6056 -204 188 33 A C ATOM 370 CG LEU A 40 8.335 -0.322 50.915 1.00 66.96 A C ANISOU 370 CG LEU A 40 7761 10202 7479 -55 310 -84 A C ATOM 371 CD1 LEU A 40 8.173 0.926 50.119 1.00 69.45 A C ANISOU 371 CD1 LEU A 40 8084 10439 7865 116 252 -301 A C ATOM 372 CD2 LEU A 40 7.060 -0.622 51.670 1.00 69.91 A C ANISOU 372 CD2 LEU A 40 7911 10886 7766 -118 485 23 A C ATOM 373 N CYS A 41 9.895 -4.417 49.693 1.00 47.90 A N ANISOU 373 N CYS A 41 5594 7073 5535 -477 -72 354 A N ATOM 374 CA CYS A 41 9.824 -5.554 48.796 1.00 51.88 A C ANISOU 374 CA CYS A 41 6137 7303 6271 -563 -234 370 A C ATOM 375 C CYS A 41 8.524 -6.307 49.029 1.00 52.46 A C ANISOU 375 C CYS A 41 6073 7400 6458 -801 -239 568 A C ATOM 376 O CYS A 41 7.967 -6.329 50.129 1.00 54.55 A O ANISOU 376 O CYS A 41 6237 7886 6606 -926 -107 784 A O ATOM 377 CB CYS A 41 11.026 -6.485 48.942 1.00 55.46 A C ANISOU 377 CB CYS A 41 6752 7513 6809 -522 -382 417 A C ATOM 378 SG CYS A 41 11.138 -7.352 50.481 1.00 61.43 A S ANISOU 378 SG CYS A 41 7567 8264 7511 -670 -420 769 A S ATOM 379 N LEU A 42 8.036 -6.897 47.950 1.00 51.08 A N ANISOU 379 N LEU A 42 5884 7025 6498 -871 -394 487 A N ATOM 380 CA LEU A 42 6.783 -7.638 47.991 1.00 54.40 A C ANISOU 380 CA LEU A 42 6140 7429 7099 -1139 -452 664 A C ATOM 381 C LEU A 42 6.823 -8.643 46.859 1.00 55.81 A C ANISOU 381 C LEU A 42 6438 7227 7540 -1190 -740 542 A C ATOM 382 O LEU A 42 6.890 -8.246 45.688 1.00 53.82 A O ANISOU 382 O LEU A 42 6232 6935 7282 -1034 -818 264 A O ATOM 383 CB LEU A 42 5.588 -6.695 47.850 1.00 53.44 A C ANISOU 383 CB LEU A 42 5748 7629 6927 -1139 -310 605 A C ATOM 384 CG LEU A 42 4.202 -7.337 47.942 1.00 61.06 A C ANISOU 384 CG LEU A 42 6438 8668 8093 -1436 -340 798 A C ATOM 385 CD1 LEU A 42 3.985 -8.028 49.284 1.00 68.57 A C ANISOU 385 CD1 LEU A 42 7311 9738 9005 -1693 -210 1181 A C ATOM 386 CD2 LEU A 42 3.141 -6.277 47.697 1.00 64.91 A C ANISOU 386 CD2 LEU A 42 6631 9488 8544 -1342 -219 673 A C ATOM 387 N ASP A 43 6.801 -9.924 47.199 1.00 59.33 A N ANISOU 387 N ASP A 43 6961 7385 8198 -1398 -916 746 A N ATOM 388 CA ASP A 43 6.683 -11.009 46.234 1.00 67.45 A C ANISOU 388 CA ASP A 43 8110 7997 9520 -1474 -1243 622 A C ATOM 389 C ASP A 43 7.581 -10.782 45.018 1.00 67.24 A C ANISOU 389 C ASP A 43 8273 7850 9424 -1146 -1335 211 A C ATOM 390 O ASP A 43 7.136 -10.755 43.873 1.00 63.38 A O ANISOU 390 O ASP A 43 7790 7310 8980 -1108 -1474 -34 A O ATOM 391 CB ASP A 43 5.233 -11.185 45.786 1.00 76.09 A C ANISOU 391 CB ASP A 43 8976 9129 10806 -1740 -1343 665 A C ATOM 392 CG ASP A 43 5.011 -12.492 45.054 1.00 86.87 A C ANISOU 392 CG ASP A 43 10477 10008 12523 -1904 -1741 595 A C ATOM 393 OD1 ASP A 43 5.620 -13.506 45.458 1.00 79.90 A O ANISOU 393 OD1 ASP A 43 9800 8755 11805 -1963 -1913 723 A O ATOM 394 OD2 ASP A 43 4.254 -12.505 44.060 1.00 78.51 A O ANISOU 394 OD2 ASP A 43 9338 8910 11581 -1955 -1923 392 A O ATOM 395 N GLY A 44 8.869 -10.605 45.297 1.00 58.21 A N ANISOU 395 N GLY A 44 7268 6702 8148 -911 -1253 150 A N ATOM 396 CA GLY A 44 9.863 -10.554 44.241 1.00 59.44 A C ANISOU 396 CA GLY A 44 7575 6770 8240 -610 -1308 -202 A C ATOM 397 C GLY A 44 9.984 -9.231 43.530 1.00 54.20 A C ANISOU 397 C GLY A 44 6849 6435 7308 -444 -1110 -389 A C ATOM 398 O GLY A 44 10.657 -9.166 42.491 1.00 52.83 A O ANISOU 398 O GLY A 44 6780 6252 7042 -230 -1133 -665 A O ATOM 399 N ILE A 45 9.335 -8.180 44.042 1.00 53.61 A N ANISOU 399 N ILE A 45 6613 6654 7104 -530 -922 -245 A N ATOM 400 CA ILE A 45 9.427 -6.829 43.508 1.00 49.56 A C ANISOU 400 CA ILE A 45 6059 6403 6369 -389 -766 -366 A C ATOM 401 C ILE A 45 10.049 -5.928 44.562 1.00 49.56 A C ANISOU 401 C ILE A 45 6013 6594 6226 -334 -559 -244 A C ATOM 402 O ILE A 45 9.688 -5.998 45.740 1.00 48.04 A O ANISOU 402 O ILE A 45 5739 6473 6043 -451 -492 -43 A O ATOM 403 CB ILE A 45 8.041 -6.273 43.093 1.00 50.58 A C ANISOU 403 CB ILE A 45 6042 6672 6505 -485 -793 -361 A C ATOM 404 CG1 ILE A 45 7.342 -7.235 42.137 1.00 54.02 A C ANISOU 404 CG1 ILE A 45 6513 6907 7106 -578 -1060 -481 A C ATOM 405 CG2 ILE A 45 8.188 -4.885 42.493 1.00 52.81 A C ANISOU 405 CG2 ILE A 45 6333 7155 6579 -323 -687 -462 A C ATOM 406 CD1 ILE A 45 8.071 -7.392 40.810 1.00 64.82 A C ANISOU 406 CD1 ILE A 45 8092 8187 8350 -382 -1167 -769 A C ATOM 407 N PHE A 46 10.992 -5.089 44.135 1.00 45.25 A N ANISOU 407 N PHE A 46 5520 6142 5532 -172 -465 -362 A N ATOM 408 CA PHE A 46 11.512 -3.998 44.947 1.00 45.48 A C ANISOU 408 CA PHE A 46 5510 6336 5435 -128 -317 -296 A C ATOM 409 C PHE A 46 10.802 -2.703 44.565 1.00 44.27 A C ANISOU 409 C PHE A 46 5306 6328 5185 -104 -258 -333 A C ATOM 410 O PHE A 46 10.549 -2.454 43.384 1.00 46.97 A O ANISOU 410 O PHE A 46 5688 6664 5495 -64 -311 -429 A O ATOM 411 CB PHE A 46 13.014 -3.792 44.727 1.00 43.76 A C ANISOU 411 CB PHE A 46 5344 6119 5166 -3 -275 -374 A C ATOM 412 CG PHE A 46 13.905 -4.781 45.432 1.00 49.28 A C ANISOU 412 CG PHE A 46 6063 6699 5962 31 -340 -326 A C ATOM 413 CD1 PHE A 46 13.917 -4.883 46.812 1.00 51.49 A C ANISOU 413 CD1 PHE A 46 6330 6999 6235 -36 -348 -153 A C ATOM 414 CD2 PHE A 46 14.776 -5.569 44.699 1.00 46.87 A C ANISOU 414 CD2 PHE A 46 5795 6282 5732 163 -402 -467 A C ATOM 415 CE1 PHE A 46 14.768 -5.774 47.446 1.00 50.51 A C ANISOU 415 CE1 PHE A 46 6244 6750 6199 9 -455 -80 A C ATOM 416 CE2 PHE A 46 15.631 -6.459 45.325 1.00 54.15 A C ANISOU 416 CE2 PHE A 46 6727 7068 6780 242 -502 -434 A C ATOM 417 CZ PHE A 46 15.625 -6.563 46.700 1.00 52.24 A C ANISOU 417 CZ PHE A 46 6486 6812 6550 156 -547 -221 A C ATOM 418 N PHE A 47 10.511 -1.871 45.562 1.00 44.20 A N ANISOU 418 N PHE A 47 5231 6447 5118 -103 -170 -270 A N ATOM 419 CA PHE A 47 10.096 -0.488 45.359 1.00 46.18 A C ANISOU 419 CA PHE A 47 5462 6782 5301 -23 -142 -329 A C ATOM 420 C PHE A 47 11.033 0.384 46.188 1.00 46.96 A C ANISOU 420 C PHE A 47 5613 6909 5321 29 -86 -338 A C ATOM 421 O PHE A 47 11.244 0.090 47.368 1.00 47.59 A O ANISOU 421 O PHE A 47 5674 7052 5357 8 -44 -288 A O ATOM 422 CB PHE A 47 8.652 -0.208 45.814 1.00 46.77 A C ANISOU 422 CB PHE A 47 5378 6987 5404 -23 -118 -315 A C ATOM 423 CG PHE A 47 7.639 -1.255 45.414 1.00 54.32 A C ANISOU 423 CG PHE A 47 6216 7938 6485 -142 -186 -265 A C ATOM 424 CD1 PHE A 47 7.637 -2.510 46.006 1.00 50.05 A C ANISOU 424 CD1 PHE A 47 5645 7357 6015 -296 -183 -138 A C ATOM 425 CD2 PHE A 47 6.636 -0.950 44.506 1.00 57.54 A C ANISOU 425 CD2 PHE A 47 6536 8366 6960 -114 -291 -326 A C ATOM 426 CE1 PHE A 47 6.703 -3.458 45.656 1.00 51.42 A C ANISOU 426 CE1 PHE A 47 5707 7481 6350 -452 -284 -77 A C ATOM 427 CE2 PHE A 47 5.691 -1.896 44.150 1.00 56.10 A C ANISOU 427 CE2 PHE A 47 6220 8171 6924 -252 -397 -290 A C ATOM 428 CZ PHE A 47 5.719 -3.151 44.729 1.00 50.71 A C ANISOU 428 CZ PHE A 47 5506 7424 6338 -438 -391 -166 A C ATOM 429 N GLN A 48 11.580 1.452 45.604 1.00 46.21 A N ANISOU 429 N GLN A 48 5592 6764 5203 76 -111 -384 A N ATOM 430 CA GLN A 48 12.456 2.327 46.374 1.00 47.15 A C ANISOU 430 CA GLN A 48 5755 6869 5291 92 -111 -405 A C ATOM 431 C GLN A 48 12.202 3.793 46.056 1.00 48.93 A C ANISOU 431 C GLN A 48 6044 7015 5533 147 -180 -453 A C ATOM 432 O GLN A 48 11.911 4.157 44.910 1.00 45.89 A O ANISOU 432 O GLN A 48 5701 6569 5165 148 -225 -418 A O ATOM 433 CB GLN A 48 13.931 2.007 46.121 1.00 50.55 A C ANISOU 433 CB GLN A 48 6201 7265 5741 35 -106 -370 A C ATOM 434 CG GLN A 48 14.888 2.818 46.999 1.00 48.80 A C ANISOU 434 CG GLN A 48 5992 7025 5524 15 -154 -389 A C ATOM 435 CD GLN A 48 16.301 2.264 46.977 1.00 46.97 A C ANISOU 435 CD GLN A 48 5691 6812 5342 -31 -153 -352 A C ATOM 436 NE2 GLN A 48 16.908 2.121 48.151 1.00 48.17 A N ANISOU 436 NE2 GLN A 48 5824 6991 5488 -28 -223 -360 A N ATOM 437 OE1 GLN A 48 16.845 1.986 45.909 1.00 49.69 A O ANISOU 437 OE1 GLN A 48 5990 7175 5715 -51 -94 -326 A O ATOM 438 N ILE A 49 12.299 4.623 47.094 1.00 48.98 A N ANISOU 438 N ILE A 49 6081 7005 5524 205 -217 -538 A N ATOM 439 CA ILE A 49 12.310 6.078 46.980 1.00 47.57 A C ANISOU 439 CA ILE A 49 6003 6664 5408 259 -342 -603 A C ATOM 440 C ILE A 49 13.626 6.575 47.562 1.00 49.41 A C ANISOU 440 C ILE A 49 6298 6808 5669 168 -416 -616 A C ATOM 441 O ILE A 49 13.992 6.194 48.680 1.00 48.22 A O ANISOU 441 O ILE A 49 6124 6757 5440 181 -402 -682 A O ATOM 442 CB ILE A 49 11.125 6.728 47.713 1.00 52.25 A C ANISOU 442 CB ILE A 49 6575 7291 5985 458 -370 -772 A C ATOM 443 CG1 ILE A 49 9.797 6.242 47.132 1.00 46.29 A C ANISOU 443 CG1 ILE A 49 5690 6651 5247 532 -316 -751 A C ATOM 444 CG2 ILE A 49 11.188 8.238 47.583 1.00 53.24 A C ANISOU 444 CG2 ILE A 49 6843 7162 6224 543 -561 -864 A C ATOM 445 CD1 ILE A 49 8.608 6.447 48.066 1.00 54.81 A C ANISOU 445 CD1 ILE A 49 6631 7910 6283 726 -251 -911 A C ATOM 446 N LEU A 50 14.326 7.427 46.810 1.00 45.59 A N ANISOU 446 N LEU A 50 5885 6145 5291 56 -512 -529 A N ATOM 447 CA LEU A 50 15.581 8.032 47.249 1.00 46.84 A C ANISOU 447 CA LEU A 50 6067 6193 5536 -81 -621 -521 A C ATOM 448 C LEU A 50 15.508 9.544 47.093 1.00 56.73 A C ANISOU 448 C LEU A 50 7472 7149 6935 -102 -831 -542 A C ATOM 449 O LEU A 50 15.031 10.039 46.067 1.00 52.01 A O ANISOU 449 O LEU A 50 6946 6429 6385 -112 -866 -420 A O ATOM 450 CB LEU A 50 16.765 7.518 46.434 1.00 52.91 A C ANISOU 450 CB LEU A 50 6722 7043 6338 -271 -527 -336 A C ATOM 451 CG LEU A 50 17.117 6.033 46.458 1.00 60.00 A C ANISOU 451 CG LEU A 50 7479 8164 7152 -244 -369 -321 A C ATOM 452 CD1 LEU A 50 17.906 5.691 45.198 1.00 61.05 A C ANISOU 452 CD1 LEU A 50 7514 8392 7291 -354 -244 -175 A C ATOM 453 CD2 LEU A 50 17.912 5.681 47.693 1.00 60.75 A C ANISOU 453 CD2 LEU A 50 7507 8315 7260 -245 -436 -393 A C ATOM 454 N GLU A 51 16.013 10.280 48.087 1.00 54.10 A N ANISOU 454 N GLU A 51 7208 6671 6676 -113 -1013 -691 A N ATOM 455 CA GLU A 51 15.949 11.737 48.044 1.00 52.19 A C ANISOU 455 CA GLU A 51 7144 6064 6620 -125 -1278 -746 A C ATOM 456 C GLU A 51 17.222 12.343 48.619 1.00 59.72 A C ANISOU 456 C GLU A 51 8117 6849 7726 -337 -1483 -765 A C ATOM 457 O GLU A 51 17.791 11.836 49.590 1.00 55.14 A O ANISOU 457 O GLU A 51 7460 6432 7059 -334 -1484 -893 A O ATOM 458 CB GLU A 51 14.707 12.268 48.789 1.00 65.22 A C ANISOU 458 CB GLU A 51 8913 7642 8227 205 -1373 -1050 A C ATOM 459 CG GLU A 51 14.654 11.922 50.261 1.00 61.17 A C ANISOU 459 CG GLU A 51 8383 7329 7531 368 -1350 -1336 A C ATOM 460 CD GLU A 51 13.288 12.155 50.894 1.00 68.58 A C ANISOU 460 CD GLU A 51 9349 8363 8344 726 -1315 -1622 A C ATOM 461 OE1 GLU A 51 12.390 12.729 50.235 1.00 65.22 A O ANISOU 461 OE1 GLU A 51 8957 7784 8039 876 -1370 -1637 A O ATOM 462 OE2 GLU A 51 13.117 11.759 52.065 1.00 61.49 A O ANISOU 462 OE2 GLU A 51 8425 7726 7214 866 -1232 -1826 A O ATOM 463 N GLY A 52 17.670 13.416 47.982 1.00 60.07 A N ANISOU 463 N GLY A 52 8258 6560 8006 -545 -1681 -606 A N ATOM 464 CA GLY A 52 18.866 14.120 48.392 1.00 63.23 A C ANISOU 464 CA GLY A 52 8657 6745 8623 -813 -1923 -586 A C ATOM 465 C GLY A 52 19.310 15.041 47.272 1.00 65.76 A C ANISOU 465 C GLY A 52 9031 6769 9185 -1127 -2039 -244 A C ATOM 466 O GLY A 52 18.587 15.257 46.301 1.00 62.48 A O ANISOU 466 O GLY A 52 8718 6277 8743 -1080 -1982 -66 A O ATOM 467 N AGLU A 53 20.522 15.569 47.433 0.44 68.04 A N ANISOU 467 N AGLU A 53 9240 6907 9706 -1468 -2219 -128 A N ATOM 468 N BGLU A 53 20.512 15.587 47.433 0.56 68.01 A N ANISOU 468 N BGLU A 53 9240 6896 9705 -1467 -2224 -129 A N ATOM 469 CA AGLU A 53 21.112 16.414 46.404 0.44 70.70 A C ANISOU 469 CA AGLU A 53 9586 6998 10279 -1858 -2312 275 A C ATOM 470 CA BGLU A 53 21.051 16.458 46.397 0.56 70.67 A C ANISOU 470 CA BGLU A 53 9600 6973 10277 -1847 -2322 271 A C ATOM 471 C AGLU A 53 21.196 15.656 45.084 0.44 73.08 A C ANISOU 471 C AGLU A 53 9712 7678 10378 -1961 -1917 638 A C ATOM 472 C BGLU A 53 21.200 15.682 45.093 0.56 73.07 A C ANISOU 472 C BGLU A 53 9715 7666 10383 -1964 -1925 638 A C ATOM 473 O AGLU A 53 21.594 14.488 45.045 0.44 69.73 A O ANISOU 473 O AGLU A 53 9029 7703 9762 -1912 -1611 622 A O ATOM 474 O BGLU A 53 21.644 14.530 45.078 0.56 69.70 A O ANISOU 474 O BGLU A 53 9022 7686 9773 -1926 -1625 622 A O ATOM 475 CB AGLU A 53 22.503 16.880 46.843 0.44 75.62 A C ANISOU 475 CB AGLU A 53 10044 7503 11185 -2250 -2521 355 A C ATOM 476 CB BGLU A 53 22.392 17.052 46.824 0.56 75.63 A C ANISOU 476 CB BGLU A 53 10097 7429 11211 -2244 -2566 352 A C ATOM 477 CG AGLU A 53 22.576 17.359 48.294 0.44 77.45 A C ANISOU 477 CG AGLU A 53 10416 7469 11542 -2122 -2906 -84 A C ATOM 478 CG BGLU A 53 22.271 18.256 47.761 0.56 70.98 A C ANISOU 478 CG BGLU A 53 9794 6276 10901 -2224 -3079 63 A C ATOM 479 CD AGLU A 53 22.987 16.258 49.261 0.44 75.90 A C ANISOU 479 CD AGLU A 53 10007 7700 11133 -1959 -2773 -336 A C ATOM 480 CD BGLU A 53 21.486 19.410 47.159 0.56 73.94 A C ANISOU 480 CD BGLU A 53 10513 6117 11463 -2208 -3335 178 A C ATOM 481 OE1AGLU A 53 22.184 15.317 49.469 0.44 64.68 A O ANISOU 481 OE1AGLU A 53 8597 6590 9389 -1605 -2513 -495 A O ATOM 482 OE1BGLU A 53 20.238 19.361 47.187 0.56 83.62 A O ANISOU 482 OE1BGLU A 53 11939 7308 12525 -1785 -3303 -38 A O ATOM 483 OE2AGLU A 53 24.105 16.340 49.814 0.44 77.98 A O ANISOU 483 OE2AGLU A 53 10088 7973 11568 -2200 -2958 -356 A O ATOM 484 OE2BGLU A 53 22.114 20.369 46.663 0.56 83.84 A O ANISOU 484 OE2BGLU A 53 11825 6980 13051 -2625 -3587 501 A O ATOM 485 N ALA A 54 20.810 16.328 43.992 1.00 77.04 A N ANISOU 485 N ALA A 54 10379 7982 10910 -2084 -1951 956 A N ATOM 486 CA ALA A 54 20.761 15.660 42.694 1.00 81.27 A C ANISOU 486 CA ALA A 54 10808 8892 11178 -2141 -1597 1267 A C ATOM 487 C ALA A 54 22.077 14.975 42.347 1.00 79.82 A C ANISOU 487 C ALA A 54 10249 9142 10938 -2417 -1297 1463 A C ATOM 488 O ALA A 54 22.083 13.854 41.827 1.00 71.82 A O ANISOU 488 O ALA A 54 9065 8579 9643 -2282 -951 1454 A O ATOM 489 CB ALA A 54 20.393 16.674 41.607 1.00 87.24 A C ANISOU 489 CB ALA A 54 11812 9346 11988 -2320 -1743 1656 A C ATOM 490 N GLU A 55 23.202 15.639 42.619 1.00 86.87 A N ANISOU 490 N GLU A 55 10990 9900 12118 -2796 -1443 1622 A N ATOM 491 CA GLU A 55 24.503 15.047 42.321 1.00 91.82 A C ANISOU 491 CA GLU A 55 11185 10969 12733 -3053 -1162 1801 A C ATOM 492 C GLU A 55 24.676 13.707 43.025 1.00 81.37 A C ANISOU 492 C GLU A 55 9632 10022 11264 -2737 -976 1445 A C ATOM 493 O GLU A 55 25.175 12.744 42.431 1.00 79.27 A O ANISOU 493 O GLU A 55 9083 10226 10809 -2700 -621 1510 A O ATOM 494 CB GLU A 55 25.621 16.007 42.735 1.00104.25 A C ANISOU 494 CB GLU A 55 12603 12296 14712 -3510 -1428 1976 A C ATOM 495 CG GLU A 55 25.764 17.241 41.853 1.00133.22 A C ANISOU 495 CG GLU A 55 16416 15647 18553 -3950 -1565 2470 A C ATOM 496 CD GLU A 55 24.643 18.248 42.051 1.00147.86 A C ANISOU 496 CD GLU A 55 18783 16859 20537 -3812 -1977 2390 A C ATOM 497 OE1 GLU A 55 24.025 18.252 43.138 1.00105.88 A O ANISOU 497 OE1 GLU A 55 13654 11289 15287 -3466 -2229 1918 A O ATOM 498 OE2 GLU A 55 24.383 19.037 41.118 1.00165.70 A O ANISOU 498 OE2 GLU A 55 21257 18883 22821 -4035 -2051 2803 A O ATOM 499 N LYS A 56 24.268 13.629 44.294 1.00 77.78 A N ANISOU 499 N LYS A 56 9308 9365 10879 -2493 -1221 1065 A N ATOM 500 CA ALYS A 56 24.438 12.396 45.054 0.66 77.45 A C ANISOU 500 CA ALYS A 56 9085 9634 10708 -2220 -1097 777 A C ATOM 501 CA BLYS A 56 24.441 12.394 45.050 0.34 77.46 A C ANISOU 501 CA BLYS A 56 9086 9637 10709 -2221 -1096 778 A C ATOM 502 C LYS A 56 23.461 11.321 44.589 1.00 75.06 A C ANISOU 502 C LYS A 56 8873 9567 10081 -1874 -824 678 A C ATOM 503 O LYS A 56 23.830 10.149 44.469 1.00 64.98 A O ANISOU 503 O LYS A 56 7375 8642 8674 -1743 -589 622 A O ATOM 504 CB ALYS A 56 24.259 12.677 46.547 0.66 75.91 A C ANISOU 504 CB ALYS A 56 9037 9185 10618 -2081 -1441 435 A C ATOM 505 CB BLYS A 56 24.273 12.671 46.544 0.34 75.97 A C ANISOU 505 CB BLYS A 56 9041 9197 10627 -2083 -1440 436 A C ATOM 506 CG ALYS A 56 25.165 13.778 47.105 0.66 78.44 A C ANISOU 506 CG ALYS A 56 9313 9206 11286 -2416 -1805 465 A C ATOM 507 CG BLYS A 56 25.575 12.964 47.284 0.34 80.00 A C ANISOU 507 CG BLYS A 56 9303 9688 11404 -2339 -1667 418 A C ATOM 508 CD ALYS A 56 26.625 13.339 47.164 0.66 82.02 A C ANISOU 508 CD ALYS A 56 9310 9961 11894 -2660 -1742 587 A C ATOM 509 CD BLYS A 56 26.391 14.051 46.593 0.34 81.90 A C ANISOU 509 CD BLYS A 56 9423 9747 11949 -2818 -1772 761 A C ATOM 510 CE ALYS A 56 27.419 14.134 48.202 0.66 86.99 A C ANISOU 510 CE ALYS A 56 9894 10320 12840 -2889 -2189 460 A C ATOM 511 CE BLYS A 56 27.545 14.542 47.464 0.34 86.81 A C ANISOU 511 CE BLYS A 56 9832 10250 12902 -3098 -2112 702 A C ATOM 512 NZ ALYS A 56 28.461 13.306 48.879 0.66 81.06 A N ANISOU 512 NZ ALYS A 56 8764 9900 12134 -2870 -2206 355 A N ATOM 513 NZ BLYS A 56 27.119 14.920 48.843 0.34 83.72 A N ANISOU 513 NZ BLYS A 56 9737 9539 12534 -2895 -2525 288 A N ATOM 514 N ILE A 57 22.210 11.705 44.321 1.00 69.37 A N ANISOU 514 N ILE A 57 8465 8635 9258 -1718 -886 645 A N ATOM 515 CA ILE A 57 21.198 10.740 43.892 1.00 70.53 A C ANISOU 515 CA ILE A 57 8690 8975 9135 -1420 -680 548 A C ATOM 516 C ILE A 57 21.600 10.094 42.571 1.00 64.80 A C ANISOU 516 C ILE A 57 7806 8587 8227 -1494 -368 763 A C ATOM 517 O ILE A 57 21.500 8.873 42.399 1.00 62.29 A O ANISOU 517 O ILE A 57 7386 8545 7738 -1296 -166 639 A O ATOM 518 CB ILE A 57 19.822 11.425 43.781 1.00 67.88 A C ANISOU 518 CB ILE A 57 8668 8352 8769 -1261 -840 494 A C ATOM 519 CG1 ILE A 57 19.394 11.998 45.135 1.00 67.46 A C ANISOU 519 CG1 ILE A 57 8759 8026 8849 -1115 -1114 205 A C ATOM 520 CG2 ILE A 57 18.767 10.461 43.256 1.00 70.83 A C ANISOU 520 CG2 ILE A 57 9083 8929 8898 -1002 -657 419 A C ATOM 521 CD1 ILE A 57 19.278 10.955 46.236 1.00 66.73 A C ANISOU 521 CD1 ILE A 57 8570 8155 8631 -895 -1038 -68 A C ATOM 522 N ASP A 58 22.039 10.906 41.610 1.00 67.26 A N ANISOU 522 N ASP A 58 8116 8880 8559 -1778 -334 1090 A N ATOM 523 CA ASP A 58 22.398 10.362 40.304 1.00 77.50 A C ANISOU 523 CA ASP A 58 9282 10559 9605 -1836 -12 1290 A C ATOM 524 C ASP A 58 23.486 9.299 40.434 1.00 75.93 A C ANISOU 524 C ASP A 58 8707 10754 9389 -1793 230 1182 A C ATOM 525 O ASP A 58 23.392 8.231 39.815 1.00 70.47 A O ANISOU 525 O ASP A 58 7947 10372 8457 -1585 470 1076 A O ATOM 526 CB ASP A 58 22.827 11.499 39.374 1.00 79.22 A C ANISOU 526 CB ASP A 58 9541 10718 9843 -2208 -14 1721 A C ATOM 527 CG ASP A 58 21.640 12.288 38.822 1.00 72.70 A C ANISOU 527 CG ASP A 58 9107 9577 8938 -2170 -210 1861 A C ATOM 528 OD1 ASP A 58 20.516 12.141 39.350 1.00 73.15 A O ANISOU 528 OD1 ASP A 58 9368 9421 9005 -1869 -382 1591 A O ATOM 529 OD2 ASP A 58 21.834 13.069 37.871 1.00 79.85 A O ANISOU 529 OD2 ASP A 58 10102 10460 9777 -2444 -200 2260 A O ATOM 530 N AARG A 59 24.522 9.562 41.235 0.57 73.16 A N ANISOU 530 N AARG A 59 8110 10379 9308 -1965 135 1180 A N ATOM 531 N BARG A 59 24.507 9.562 41.256 0.43 73.16 A N ANISOU 531 N BARG A 59 8114 10374 9310 -1962 130 1175 A N ATOM 532 CA AARG A 59 25.589 8.578 41.401 0.57 70.74 A C ANISOU 532 CA AARG A 59 7410 10439 9030 -1892 324 1071 A C ATOM 533 CA BARG A 59 25.600 8.609 41.428 0.43 70.79 A C ANISOU 533 CA BARG A 59 7417 10436 9046 -1899 315 1073 A C ATOM 534 C AARG A 59 25.058 7.304 42.046 0.57 70.08 A C ANISOU 534 C AARG A 59 7385 10382 8859 -1495 312 728 A C ATOM 535 C BARG A 59 25.111 7.319 42.081 0.43 70.09 A C ANISOU 535 C BARG A 59 7374 10384 8873 -1503 307 730 A C ATOM 536 O AARG A 59 25.307 6.198 41.557 0.57 71.06 A O ANISOU 536 O AARG A 59 7354 10804 8841 -1290 537 620 A O ATOM 537 O BARG A 59 25.473 6.218 41.651 0.43 70.77 A O ANISOU 537 O BARG A 59 7273 10778 8840 -1308 529 623 A O ATOM 538 CB AARG A 59 26.736 9.161 42.229 0.57 78.40 A C ANISOU 538 CB AARG A 59 8099 11346 10342 -2156 145 1129 A C ATOM 539 CB BARG A 59 26.717 9.229 42.270 0.43 78.38 A C ANISOU 539 CB BARG A 59 8111 11318 10352 -2168 125 1131 A C ATOM 540 CG AARG A 59 27.842 8.158 42.621 0.57 83.15 A C ANISOU 540 CG AARG A 59 8265 12289 11039 -2034 255 981 A C ATOM 541 CG BARG A 59 27.404 10.457 41.676 0.43 78.14 A C ANISOU 541 CG BARG A 59 7961 11248 10480 -2640 116 1518 A C ATOM 542 CD AARG A 59 28.123 7.100 41.547 0.57 85.21 A C ANISOU 542 CD AARG A 59 8311 13010 11054 -1832 657 957 A C ATOM 543 CD BARG A 59 28.106 10.195 40.346 0.43 81.01 A C ANISOU 543 CD BARG A 59 8020 12110 10651 -2780 539 1787 A C ATOM 544 NE AARG A 59 29.405 6.428 41.744 0.57 97.54 A N ANISOU 544 NE AARG A 59 9369 14917 12773 -1771 768 878 A N ATOM 545 NE BARG A 59 27.818 11.253 39.382 0.43 83.92 A N ANISOU 545 NE BARG A 59 8589 12369 10926 -3105 570 2191 A N ATOM 546 CZ AARG A 59 29.978 5.634 40.848 0.57101.17 A C ANISOU 546 CZ AARG A 59 9528 15832 13080 -1610 1121 840 A C ATOM 547 CZ BARG A 59 26.720 11.321 38.640 0.43 74.15 A C ANISOU 547 CZ BARG A 59 7740 11043 9393 -2968 607 2249 A C ATOM 548 NH1AARG A 59 29.402 5.374 39.685 0.57 93.27 A N ANISOU 548 NH1AARG A 59 8704 15010 11724 -1504 1397 866 A N ATOM 549 NH1BARG A 59 25.829 10.344 38.628 0.43 77.60 A N ANISOU 549 NH1BARG A 59 8363 11535 9587 -2538 666 1931 A N ATOM 550 NH2AARG A 59 31.155 5.082 41.129 0.57107.05 A N ANISOU 550 NH2AARG A 59 9778 16872 14024 -1525 1181 746 A N ATOM 551 NH2BARG A 59 26.516 12.395 37.882 0.43 77.47 A N ANISOU 551 NH2BARG A 59 8362 11298 9775 -3289 553 2658 A N ATOM 552 N ILE A 60 24.317 7.438 43.148 1.00 67.45 A N ANISOU 552 N ILE A 60 7283 9740 8604 -1380 47 555 A N ATOM 553 CA ILE A 60 23.808 6.248 43.829 1.00 67.11 A C ANISOU 553 CA ILE A 60 7298 9719 8481 -1061 30 300 A C ATOM 554 C ILE A 60 22.916 5.440 42.893 1.00 61.59 A C ANISOU 554 C ILE A 60 6738 9126 7539 -862 215 251 A C ATOM 555 O ILE A 60 23.006 4.209 42.835 1.00 61.14 A O ANISOU 555 O ILE A 60 6595 9216 7419 -648 315 107 A O ATOM 556 CB ILE A 60 23.074 6.640 45.125 1.00 64.48 A C ANISOU 556 CB ILE A 60 7195 9097 8205 -993 -246 154 A C ATOM 557 CG1 ILE A 60 24.084 7.025 46.215 1.00 69.61 A C ANISOU 557 CG1 ILE A 60 7690 9695 9064 -1115 -466 111 A C ATOM 558 CG2 ILE A 60 22.207 5.499 45.639 1.00 60.89 A C ANISOU 558 CG2 ILE A 60 6860 8664 7611 -710 -228 -24 A C ATOM 559 CD1 ILE A 60 23.719 8.271 46.984 1.00 69.28 A C ANISOU 559 CD1 ILE A 60 7868 9335 9121 -1226 -753 57 A C ATOM 560 N TYR A 61 22.043 6.115 42.143 1.00 66.87 A N ANISOU 560 N TYR A 61 7633 9690 8085 -922 220 363 A N ATOM 561 CA TYR A 61 21.161 5.399 41.225 1.00 59.77 A C ANISOU 561 CA TYR A 61 6871 8886 6951 -747 343 306 A C ATOM 562 C TYR A 61 21.964 4.599 40.203 1.00 63.12 A C ANISOU 562 C TYR A 61 7099 9662 7222 -695 607 303 A C ATOM 563 O TYR A 61 21.649 3.434 39.935 1.00 56.11 A O ANISOU 563 O TYR A 61 6230 8865 6223 -463 673 110 A O ATOM 564 CB TYR A 61 20.219 6.389 40.535 1.00 66.27 A C ANISOU 564 CB TYR A 61 7947 9554 7678 -833 264 462 A C ATOM 565 CG TYR A 61 19.123 5.751 39.709 1.00 67.58 A C ANISOU 565 CG TYR A 61 8279 9779 7620 -654 302 384 A C ATOM 566 CD1 TYR A 61 18.168 4.938 40.299 1.00 59.34 A C ANISOU 566 CD1 TYR A 61 7303 8644 6599 -452 216 170 A C ATOM 567 CD2 TYR A 61 19.031 5.982 38.345 1.00 63.90 A C ANISOU 567 CD2 TYR A 61 7901 9469 6911 -712 404 544 A C ATOM 568 CE1 TYR A 61 17.153 4.357 39.552 1.00 62.49 A C ANISOU 568 CE1 TYR A 61 7827 9078 6837 -321 205 95 A C ATOM 569 CE2 TYR A 61 18.017 5.406 37.584 1.00 71.54 A C ANISOU 569 CE2 TYR A 61 9029 10486 7669 -548 382 448 A C ATOM 570 CZ TYR A 61 17.083 4.594 38.198 1.00 71.13 A C ANISOU 570 CZ TYR A 61 9017 10312 7699 -359 268 213 A C ATOM 571 OH TYR A 61 16.072 4.014 37.461 1.00 68.94 A O ANISOU 571 OH TYR A 61 8869 10067 7258 -229 204 113 A O ATOM 572 N GLU A 62 23.022 5.192 39.644 1.00 64.99 A N ANISOU 572 N GLU A 62 7130 10103 7458 -907 756 503 A N ATOM 573 CA GLU A 62 23.826 4.476 38.656 1.00 63.21 A C ANISOU 573 CA GLU A 62 6677 10292 7048 -827 1055 476 A C ATOM 574 C GLU A 62 24.423 3.206 39.252 1.00 64.71 A C ANISOU 574 C GLU A 62 6644 10580 7362 -563 1079 196 A C ATOM 575 O GLU A 62 24.474 2.164 38.588 1.00 64.72 A O ANISOU 575 O GLU A 62 6608 10786 7198 -312 1231 -0 A O ATOM 576 CB GLU A 62 24.928 5.386 38.109 1.00 72.79 A C ANISOU 576 CB GLU A 62 7635 11750 8270 -1145 1232 780 A C ATOM 577 N AARG A 63 24.859 3.269 40.510 0.50 65.40 A N ANISOU 577 N AARG A 63 6609 10501 7739 -595 891 161 A N ATOM 578 N BARG A 63 24.896 3.280 40.502 0.50 65.42 A N ANISOU 578 N BARG A 63 6602 10512 7744 -599 896 165 A N ATOM 579 CA AARG A 63 25.415 2.090 41.168 0.50 66.90 A C ANISOU 579 CA AARG A 63 6613 10735 8069 -338 848 -64 A C ATOM 580 CA BARG A 63 25.411 2.090 41.174 0.50 66.89 A C ANISOU 580 CA BARG A 63 6614 10733 8070 -338 847 -65 A C ATOM 581 C AARG A 63 24.337 1.044 41.425 0.50 62.20 A C ANISOU 581 C AARG A 63 6297 9927 7408 -79 728 -266 A C ATOM 582 C BARG A 63 24.312 1.047 41.342 0.50 62.20 A C ANISOU 582 C BARG A 63 6304 9937 7394 -79 740 -265 A C ATOM 583 O AARG A 63 24.589 -0.161 41.300 0.50 60.03 A O ANISOU 583 O AARG A 63 5947 9715 7147 186 758 -465 A O ATOM 584 O BARG A 63 24.523 -0.145 41.093 0.50 60.08 A O ANISOU 584 O BARG A 63 5969 9746 7113 187 789 -467 A O ATOM 585 CB AARG A 63 26.096 2.517 42.470 0.50 68.25 A C ANISOU 585 CB AARG A 63 6623 10780 8528 -462 626 -19 A C ATOM 586 CB BARG A 63 25.992 2.448 42.547 0.50 68.23 A C ANISOU 586 CB BARG A 63 6651 10749 8523 -441 606 -35 A C ATOM 587 CG AARG A 63 26.333 1.413 43.487 0.50 68.89 A C ANISOU 587 CG AARG A 63 6645 10774 8755 -207 450 -207 A C ATOM 588 CG BARG A 63 27.098 3.502 42.576 0.50 74.23 A C ANISOU 588 CG BARG A 63 7107 11643 9453 -750 625 163 A C ATOM 589 CD AARG A 63 27.268 0.344 42.963 0.50 69.79 A C ANISOU 589 CD AARG A 63 6444 11159 8913 49 607 -357 A C ATOM 590 CD BARG A 63 28.077 3.220 43.729 0.50 78.07 A C ANISOU 590 CD BARG A 63 7314 12130 10219 -713 419 83 A C ATOM 591 NE AARG A 63 26.561 -0.917 42.774 0.50 70.69 A N ANISOU 591 NE AARG A 63 6773 11149 8936 358 585 -559 A N ATOM 592 NE BARG A 63 27.376 2.878 44.964 0.50 75.37 A N ANISOU 592 NE BARG A 63 7252 11485 9902 -575 127 -43 A N ATOM 593 CZ AARG A 63 26.980 -1.907 42.002 0.50 71.65 A C ANISOU 593 CZ AARG A 63 6757 11448 9021 641 732 -758 A C ATOM 594 CZ BARG A 63 26.702 3.740 45.716 0.50 67.53 A C ANISOU 594 CZ BARG A 63 6532 10219 8907 -723 -87 -6 A C ATOM 595 NH1AARG A 63 28.108 -1.819 41.315 0.50 78.94 A N ANISOU 595 NH1AARG A 63 7288 12754 9951 685 970 -789 A N ATOM 596 NH1BARG A 63 26.730 5.039 45.472 0.50 76.33 A N ANISOU 596 NH1BARG A 63 7683 11244 10076 -1020 -119 147 A N ATOM 597 NH2AARG A 63 26.252 -3.016 41.920 0.50 73.35 A N ANISOU 597 NH2AARG A 63 7218 11453 9197 888 635 -941 A N ATOM 598 NH2BARG A 63 25.984 3.285 46.738 0.50 70.22 A N ANISOU 598 NH2BARG A 63 7119 10374 9188 -564 -277 -123 A N ATOM 599 N ILE A 64 23.130 1.481 41.787 1.00 55.85 A N ANISOU 599 N ILE A 64 5800 8862 6559 -152 578 -218 A N ATOM 600 CA ILE A 64 22.030 0.544 41.986 1.00 53.28 A C ANISOU 600 CA ILE A 64 5702 8357 6185 30 476 -362 A C ATOM 601 C ILE A 64 21.664 -0.139 40.673 1.00 59.24 A C ANISOU 601 C ILE A 64 6536 9238 6736 172 613 -481 A C ATOM 602 O ILE A 64 21.274 -1.313 40.665 1.00 54.24 A O ANISOU 602 O ILE A 64 5983 8508 6119 369 544 -661 A O ATOM 603 CB ILE A 64 20.815 1.268 42.602 1.00 55.50 A C ANISOU 603 CB ILE A 64 6224 8406 6458 -79 323 -285 A C ATOM 604 CG1 ILE A 64 21.063 1.603 44.079 1.00 61.99 A C ANISOU 604 CG1 ILE A 64 7017 9102 7435 -134 153 -262 A C ATOM 605 CG2 ILE A 64 19.560 0.418 42.467 1.00 57.99 A C ANISOU 605 CG2 ILE A 64 6730 8603 6701 48 264 -387 A C ATOM 606 CD1 ILE A 64 20.166 2.733 44.615 1.00 57.21 A C ANISOU 606 CD1 ILE A 64 6594 8331 6813 -244 37 -206 A C ATOM 607 N LEU A 65 21.773 0.577 39.546 1.00 55.05 A N ANISOU 607 N LEU A 65 6007 8910 6000 66 782 -377 A N ATOM 608 CA LEU A 65 21.457 -0.028 38.254 1.00 59.41 A C ANISOU 608 CA LEU A 65 6658 9630 6286 214 903 -512 A C ATOM 609 C LEU A 65 22.401 -1.168 37.917 1.00 66.14 A C ANISOU 609 C LEU A 65 7310 10684 7134 473 1033 -757 A C ATOM 610 O LEU A 65 22.044 -2.055 37.134 1.00 62.83 A O ANISOU 610 O LEU A 65 7013 10307 6552 686 1046 -991 A O ATOM 611 CB LEU A 65 21.516 1.006 37.127 1.00 65.79 A C ANISOU 611 CB LEU A 65 7507 10670 6819 37 1069 -302 A C ATOM 612 CG LEU A 65 20.536 2.173 37.215 1.00 71.72 A C ANISOU 612 CG LEU A 65 8488 11202 7562 -172 911 -70 A C ATOM 613 CD1 LEU A 65 20.853 3.213 36.161 1.00 72.92 A C ANISOU 613 CD1 LEU A 65 8662 11570 7475 -377 1060 210 A C ATOM 614 CD2 LEU A 65 19.116 1.671 37.065 1.00 73.22 A C ANISOU 614 CD2 LEU A 65 8935 11199 7685 -42 727 -209 A C ATOM 615 N ALA A 66 23.612 -1.149 38.470 1.00 59.61 A N ANISOU 615 N ALA A 66 6170 9984 6496 478 1105 -734 A N ATOM 616 CA ALA A 66 24.599 -2.176 38.190 1.00 58.37 A C ANISOU 616 CA ALA A 66 5765 10035 6378 770 1223 -983 A C ATOM 617 C ALA A 66 24.488 -3.389 39.107 1.00 59.72 A C ANISOU 617 C ALA A 66 5985 9887 6817 1013 968 -1185 A C ATOM 618 O ALA A 66 25.191 -4.381 38.872 1.00 61.36 A O ANISOU 618 O ALA A 66 6035 10186 7094 1323 1002 -1440 A O ATOM 619 CB ALA A 66 26.008 -1.583 38.303 1.00 66.77 A C ANISOU 619 CB ALA A 66 6398 11424 7548 664 1413 -851 A C ATOM 620 N ASP A 67 23.627 -3.341 40.126 1.00 54.82 A N ANISOU 620 N ASP A 67 5581 8908 6342 891 715 -1072 A N ATOM 621 CA ASP A 67 23.517 -4.428 41.095 1.00 57.61 A C ANISOU 621 CA ASP A 67 5998 8955 6937 1057 462 -1168 A C ATOM 622 C ASP A 67 22.899 -5.651 40.432 1.00 61.72 A C ANISOU 622 C ASP A 67 6722 9308 7420 1291 378 -1425 A C ATOM 623 O ASP A 67 21.784 -5.587 39.910 1.00 57.96 A O ANISOU 623 O ASP A 67 6491 8740 6790 1201 348 -1431 A O ATOM 624 CB ASP A 67 22.680 -3.990 42.295 1.00 52.75 A C ANISOU 624 CB ASP A 67 5559 8078 6406 840 266 -956 A C ATOM 625 CG ASP A 67 22.927 -4.849 43.534 1.00 55.99 A C ANISOU 625 CG ASP A 67 5967 8259 7048 945 24 -941 A C ATOM 626 OD1 ASP A 67 22.707 -6.073 43.464 1.00 55.96 A O ANISOU 626 OD1 ASP A 67 6070 8049 7141 1138 -109 -1074 A O ATOM 627 OD2 ASP A 67 23.318 -4.299 44.587 1.00 56.19 A O ANISOU 627 OD2 ASP A 67 5911 8286 7152 828 -66 -789 A O ATOM 628 N AGLU A 68 23.618 -6.772 40.457 0.65 63.42 A N ANISOU 628 N AGLU A 68 6834 9458 7803 1602 298 -1652 A N ATOM 629 N BGLU A 68 23.622 -6.772 40.465 0.35 63.55 A N ANISOU 629 N BGLU A 68 6850 9475 7821 1602 297 -1651 A N ATOM 630 CA AGLU A 68 23.139 -7.968 39.778 0.65 68.54 A C ANISOU 630 CA AGLU A 68 7687 9904 8449 1850 175 -1949 A C ATOM 631 CA BGLU A 68 23.166 -7.992 39.813 0.35 68.59 A C ANISOU 631 CA BGLU A 68 7689 9905 8468 1856 169 -1950 A C ATOM 632 C AGLU A 68 21.933 -8.605 40.461 0.65 64.63 A C ANISOU 632 C AGLU A 68 7499 8945 8112 1730 -135 -1856 A C ATOM 633 C BGLU A 68 21.912 -8.579 40.446 0.35 64.72 A C ANISOU 633 C BGLU A 68 7512 8961 8117 1723 -131 -1853 A C ATOM 634 O AGLU A 68 21.355 -9.541 39.897 0.65 67.23 A O ANISOU 634 O AGLU A 68 8033 9044 8467 1862 -290 -2079 A O ATOM 635 O BGLU A 68 21.287 -9.454 39.836 0.35 66.99 A O ANISOU 635 O BGLU A 68 8009 9034 8410 1842 -274 -2071 A O ATOM 636 CB AGLU A 68 24.279 -8.989 39.667 0.65 73.66 A C ANISOU 636 CB AGLU A 68 8138 10566 9281 2261 138 -2244 A C ATOM 637 CB BGLU A 68 24.281 -9.043 39.838 0.35 73.97 A C ANISOU 637 CB BGLU A 68 8182 10561 9364 2256 102 -2222 A C ATOM 638 CG AGLU A 68 24.694 -9.617 40.993 0.65 80.72 A C ANISOU 638 CG AGLU A 68 8984 11142 10545 2336 -152 -2131 A C ATOM 639 CG BGLU A 68 24.723 -9.451 41.241 0.35 80.55 A C ANISOU 639 CG BGLU A 68 8941 11123 10541 2278 -160 -2055 A C ATOM 640 CD AGLU A 68 26.160 -10.018 41.029 0.65 88.16 A C ANISOU 640 CD AGLU A 68 9559 12270 11667 2686 -114 -2317 A C ATOM 641 CD BGLU A 68 24.412 -10.903 41.562 0.35 82.40 A C ANISOU 641 CD BGLU A 68 9404 10861 11045 2506 -518 -2201 A C ATOM 642 OE1AGLU A 68 26.954 -9.482 40.225 0.65 86.89 A O ANISOU 642 OE1AGLU A 68 9093 12585 11338 2771 213 -2438 A O ATOM 643 OE1BGLU A 68 23.326 -11.384 41.176 0.35 80.61 A O ANISOU 643 OE1BGLU A 68 9487 10363 10778 2436 -644 -2267 A O ATOM 644 OE2AGLU A 68 26.520 -10.870 41.869 0.65 96.07 A O ANISOU 644 OE2AGLU A 68 10563 12957 12984 2875 -416 -2321 A O ATOM 645 OE2BGLU A 68 25.256 -11.563 42.205 0.35 85.29 A O ANISOU 645 OE2BGLU A 68 9637 11083 11687 2747 -706 -2236 A O ATOM 646 N ARG A 69 21.515 -8.118 41.631 1.00 60.13 A N ANISOU 646 N ARG A 69 6961 8251 7635 1472 -229 -1541 A N ATOM 647 CA ARG A 69 20.421 -8.763 42.350 1.00 57.58 A C ANISOU 647 CA ARG A 69 6874 7550 7452 1338 -483 -1410 A C ATOM 648 C ARG A 69 19.038 -8.328 41.891 1.00 60.72 A C ANISOU 648 C ARG A 69 7443 7935 7692 1110 -460 -1349 A C ATOM 649 O ARG A 69 18.046 -8.889 42.367 1.00 55.62 A O ANISOU 649 O ARG A 69 6950 7016 7167 973 -649 -1241 A O ATOM 650 CB ARG A 69 20.555 -8.515 43.851 1.00 59.39 A C ANISOU 650 CB ARG A 69 7064 7706 7797 1189 -584 -1110 A C ATOM 651 CG ARG A 69 21.809 -9.163 44.421 1.00 73.09 A C ANISOU 651 CG ARG A 69 8654 9377 9741 1427 -715 -1152 A C ATOM 652 CD ARG A 69 22.063 -8.750 45.843 1.00 65.92 A C ANISOU 652 CD ARG A 69 7702 8475 8868 1285 -814 -867 A C ATOM 653 NE ARG A 69 22.716 -7.448 45.888 1.00 63.31 A N ANISOU 653 NE ARG A 69 7153 8490 8411 1190 -620 -830 A N ATOM 654 CZ ARG A 69 23.257 -6.916 46.972 1.00 63.96 A C ANISOU 654 CZ ARG A 69 7140 8650 8511 1106 -704 -666 A C ATOM 655 NH1 ARG A 69 23.324 -7.588 48.111 1.00 62.98 A N ANISOU 655 NH1 ARG A 69 7112 8333 8486 1138 -962 -513 A N ATOM 656 NH2 ARG A 69 23.751 -5.683 46.909 1.00 59.08 A N ANISOU 656 NH2 ARG A 69 6345 8299 7806 977 -554 -644 A N ATOM 657 N HIS A 70 18.928 -7.360 40.992 1.00 57.34 A N ANISOU 657 N HIS A 70 6980 7796 7012 1055 -252 -1387 A N ATOM 658 CA HIS A 70 17.618 -7.020 40.453 1.00 53.36 A C ANISOU 658 CA HIS A 70 6630 7269 6374 889 -281 -1356 A C ATOM 659 C HIS A 70 17.776 -6.636 38.992 1.00 57.63 A C ANISOU 659 C HIS A 70 7194 8073 6630 988 -130 -1542 A C ATOM 660 O HIS A 70 18.888 -6.471 38.481 1.00 52.30 A O ANISOU 660 O HIS A 70 6383 7650 5837 1142 59 -1649 A O ATOM 661 CB HIS A 70 16.915 -5.940 41.297 1.00 46.69 A C ANISOU 661 CB HIS A 70 5764 6470 5507 634 -242 -1069 A C ATOM 662 CG HIS A 70 17.594 -4.605 41.335 1.00 47.88 A C ANISOU 662 CG HIS A 70 5788 6880 5523 572 -46 -953 A C ATOM 663 CD2 HIS A 70 18.833 -4.205 40.959 1.00 50.31 A C ANISOU 663 CD2 HIS A 70 5943 7407 5765 651 116 -991 A C ATOM 664 ND1 HIS A 70 16.963 -3.482 41.834 1.00 47.19 A N ANISOU 664 ND1 HIS A 70 5711 6831 5388 392 -21 -770 A N ATOM 665 CE1 HIS A 70 17.783 -2.448 41.759 1.00 53.10 A C ANISOU 665 CE1 HIS A 70 6358 7751 6065 347 111 -696 A C ATOM 666 NE2 HIS A 70 18.922 -2.859 41.227 1.00 51.46 A N ANISOU 666 NE2 HIS A 70 6032 7676 5845 475 208 -804 A N ATOM 667 N THR A 71 16.641 -6.571 38.304 1.00 50.70 A N ANISOU 667 N THR A 71 6476 7156 5632 902 -223 -1581 A N ATOM 668 CA THR A 71 16.603 -6.366 36.865 1.00 52.07 A C ANISOU 668 CA THR A 71 6740 7561 5484 1000 -144 -1764 A C ATOM 669 C THR A 71 15.262 -5.730 36.524 1.00 50.94 A C ANISOU 669 C THR A 71 6717 7402 5236 810 -254 -1640 A C ATOM 670 O THR A 71 14.440 -5.466 37.406 1.00 49.85 A O ANISOU 670 O THR A 71 6550 7101 5289 630 -354 -1441 A O ATOM 671 CB THR A 71 16.831 -7.685 36.118 1.00 61.62 A C ANISOU 671 CB THR A 71 8061 8662 6688 1268 -271 -2154 A C ATOM 672 CG2 THR A 71 15.644 -8.623 36.283 1.00 59.06 A C ANISOU 672 CG2 THR A 71 7913 7938 6591 1189 -621 -2236 A C ATOM 673 OG1 THR A 71 17.040 -7.424 34.726 1.00 64.53 A O ANISOU 673 OG1 THR A 71 8504 9363 6651 1403 -134 -2351 A O ATOM 674 N ASP A 72 15.048 -5.472 35.236 1.00 54.37 A N ANISOU 674 N ASP A 72 7274 8039 5343 870 -235 -1759 A N ATOM 675 CA ASP A 72 13.847 -4.785 34.769 1.00 58.23 A C ANISOU 675 CA ASP A 72 7869 8547 5708 726 -368 -1641 A C ATOM 676 C ASP A 72 13.539 -3.566 35.639 1.00 53.85 A C ANISOU 676 C ASP A 72 7204 7988 5268 533 -298 -1300 A C ATOM 677 O ASP A 72 12.450 -3.423 36.197 1.00 49.82 A O ANISOU 677 O ASP A 72 6672 7318 4941 414 -456 -1199 A O ATOM 678 CB ASP A 72 12.648 -5.737 34.736 1.00 61.80 A C ANISOU 678 CB ASP A 72 8418 8716 6346 690 -699 -1795 A C ATOM 679 CG ASP A 72 12.868 -6.929 33.831 1.00 75.08 A C ANISOU 679 CG ASP A 72 10259 10339 7929 895 -841 -2187 A C ATOM 680 OD1 ASP A 72 13.823 -6.903 33.027 1.00 93.62 A O ANISOU 680 OD1 ASP A 72 12651 12954 9965 1095 -653 -2358 A O ATOM 681 OD2 ASP A 72 12.069 -7.886 33.908 1.00 86.93 A O ANISOU 681 OD2 ASP A 72 11834 11534 9661 852 -1145 -2333 A O ATOM 682 N AILE A 73 14.544 -2.699 35.775 0.43 52.74 A N ANISOU 682 N AILE A 73 6973 8031 5036 509 -62 -1142 A N ATOM 683 N BILE A 73 14.517 -2.671 35.744 0.57 52.73 A N ANISOU 683 N BILE A 73 6977 8034 5026 506 -64 -1139 A N ATOM 684 CA AILE A 73 14.378 -1.471 36.535 0.43 49.14 A C ANISOU 684 CA AILE A 73 6447 7545 4680 350 -23 -865 A C ATOM 685 CA BILE A 73 14.377 -1.486 36.591 0.57 49.06 A C ANISOU 685 CA BILE A 73 6432 7526 4683 348 -24 -865 A C ATOM 686 C AILE A 73 13.534 -0.500 35.728 0.43 51.59 A C ANISOU 686 C AILE A 73 6885 7916 4801 286 -114 -734 A C ATOM 687 C BILE A 73 13.650 -0.396 35.812 0.57 51.53 A C ANISOU 687 C BILE A 73 6863 7912 4801 276 -91 -711 A C ATOM 688 O AILE A 73 13.739 -0.326 34.519 0.43 50.56 A O ANISOU 688 O AILE A 73 6872 7985 4352 324 -72 -745 A O ATOM 689 O BILE A 73 14.064 -0.029 34.708 0.57 50.30 A O ANISOU 689 O BILE A 73 6800 7972 4339 291 -4 -673 A O ATOM 690 CB AILE A 73 15.750 -0.856 36.870 0.43 53.08 A C ANISOU 690 CB AILE A 73 6809 8187 5174 311 204 -740 A C ATOM 691 CB BILE A 73 15.756 -0.998 37.069 0.57 53.28 A C ANISOU 691 CB BILE A 73 6818 8179 5247 318 193 -756 A C ATOM 692 CG1AILE A 73 16.427 -1.645 37.991 0.43 52.61 A C ANISOU 692 CG1AILE A 73 6604 8015 5370 367 221 -819 A C ATOM 693 CG1BILE A 73 16.508 -2.129 37.780 0.57 53.27 A C ANISOU 693 CG1BILE A 73 6698 8104 5440 434 214 -913 A C ATOM 694 CG2AILE A 73 15.594 0.608 37.269 0.43 50.47 A C ANISOU 694 CG2AILE A 73 6475 7820 4881 145 205 -475 A C ATOM 695 CG2BILE A 73 15.602 0.206 37.988 0.57 51.28 A C ANISOU 695 CG2BILE A 73 6518 7828 5137 164 177 -526 A C ATOM 696 CD1AILE A 73 16.898 -3.018 37.568 0.43 55.22 A C ANISOU 696 CD1AILE A 73 6931 8353 5697 568 217 -1086 A C ATOM 697 CD1BILE A 73 17.986 -1.840 38.030 0.57 54.79 A C ANISOU 697 CD1BILE A 73 6694 8469 5654 445 411 -861 A C ATOM 698 N LEU A 74 12.569 0.136 36.387 1.00 52.40 A N ANISOU 698 N LEU A 74 6966 7865 5079 211 -247 -612 A N ATOM 699 CA LEU A 74 11.775 1.187 35.750 1.00 48.86 A C ANISOU 699 CA LEU A 74 6623 7430 4512 180 -375 -466 A C ATOM 700 C LEU A 74 11.604 2.350 36.715 1.00 47.13 A C ANISOU 700 C LEU A 74 6338 7078 4489 117 -383 -291 A C ATOM 701 O LEU A 74 11.037 2.190 37.799 1.00 45.41 A O ANISOU 701 O LEU A 74 6002 6744 4507 127 -425 -342 A O ATOM 702 CB LEU A 74 10.405 0.669 35.301 1.00 49.85 A C ANISOU 702 CB LEU A 74 6787 7497 4656 227 -630 -585 A C ATOM 703 CG LEU A 74 9.531 1.739 34.645 1.00 52.27 A C ANISOU 703 CG LEU A 74 7189 7808 4864 234 -819 -436 A C ATOM 704 CD1 LEU A 74 10.161 2.217 33.337 1.00 59.10 A C ANISOU 704 CD1 LEU A 74 8262 8862 5332 233 -774 -324 A C ATOM 705 CD2 LEU A 74 8.118 1.196 34.400 1.00 57.60 A C ANISOU 705 CD2 LEU A 74 7817 8427 5641 273 -1100 -564 A C ATOM 706 N CYS A 75 12.083 3.522 36.312 1.00 49.77 A N ANISOU 706 N CYS A 75 6761 7433 4718 49 -351 -86 A N ATOM 707 CA CYS A 75 11.890 4.734 37.097 1.00 48.80 A C ANISOU 707 CA CYS A 75 6629 7126 4788 12 -424 47 A C ATOM 708 C CYS A 75 10.474 5.250 36.859 1.00 49.18 A C ANISOU 708 C CYS A 75 6731 7064 4892 110 -672 57 A C ATOM 709 O CYS A 75 10.107 5.565 35.723 1.00 50.07 A O ANISOU 709 O CYS A 75 6989 7219 4814 123 -804 162 A O ATOM 710 CB CYS A 75 12.925 5.789 36.713 1.00 54.70 A C ANISOU 710 CB CYS A 75 7458 7875 5450 -134 -347 289 A C ATOM 711 SG CYS A 75 12.722 7.375 37.601 1.00 58.60 A S ANISOU 711 SG CYS A 75 8001 8046 6216 -174 -520 422 A S ATOM 712 N LEU A 76 9.676 5.330 37.929 1.00 50.87 A N ANISOU 712 N LEU A 76 6811 7170 5347 194 -738 -51 A N ATOM 713 CA LEU A 76 8.288 5.766 37.815 1.00 45.85 A C ANISOU 713 CA LEU A 76 6141 6468 4815 327 -962 -78 A C ATOM 714 C LEU A 76 8.130 7.268 37.982 1.00 52.31 A C ANISOU 714 C LEU A 76 7052 7079 5743 398 -1108 35 A C ATOM 715 O LEU A 76 7.176 7.848 37.448 1.00 53.91 A O ANISOU 715 O LEU A 76 7294 7207 5983 523 -1346 76 A O ATOM 716 CB LEU A 76 7.422 5.072 38.875 1.00 52.38 A C ANISOU 716 CB LEU A 76 6723 7342 5836 393 -930 -255 A C ATOM 717 CG LEU A 76 7.292 3.547 38.843 1.00 60.49 A C ANISOU 717 CG LEU A 76 7647 8488 6849 316 -864 -360 A C ATOM 718 CD1 LEU A 76 6.578 3.049 40.095 1.00 62.40 A C ANISOU 718 CD1 LEU A 76 7646 8777 7287 322 -794 -443 A C ATOM 719 CD2 LEU A 76 6.554 3.082 37.604 1.00 61.20 A C ANISOU 719 CD2 LEU A 76 7781 8629 6844 328 -1068 -391 A C ATOM 720 N LYS A 77 9.035 7.910 38.719 1.00 45.57 A N ANISOU 720 N LYS A 77 6240 6105 4970 331 -1015 76 A N ATOM 721 CA LYS A 77 8.878 9.326 39.021 1.00 46.56 A C ANISOU 721 CA LYS A 77 6472 5960 5260 408 -1199 136 A C ATOM 722 C LYS A 77 10.243 9.917 39.332 1.00 55.37 A C ANISOU 722 C LYS A 77 7690 6950 6397 218 -1118 259 A C ATOM 723 O LYS A 77 11.014 9.341 40.105 1.00 51.69 A O ANISOU 723 O LYS A 77 7114 6588 5936 134 -927 164 A O ATOM 724 CB LYS A 77 7.909 9.514 40.194 1.00 53.38 A C ANISOU 724 CB LYS A 77 7166 6785 6331 636 -1245 -111 A C ATOM 725 CG LYS A 77 7.091 10.794 40.142 1.00 64.30 A C ANISOU 725 CG LYS A 77 8628 7910 7893 856 -1531 -126 A C ATOM 726 CD LYS A 77 6.333 11.035 41.445 1.00 65.67 A C ANISOU 726 CD LYS A 77 8613 8098 8241 1111 -1514 -424 A C ATOM 727 CE LYS A 77 6.048 12.513 41.660 1.00106.07 A C ANISOU 727 CE LYS A 77 13875 12858 13568 1334 -1792 -490 A C ATOM 728 NZ LYS A 77 4.837 12.762 42.493 1.00107.57 A N ANISOU 728 NZ LYS A 77 13836 13129 13908 1699 -1828 -802 A N ATOM 729 N SER A 78 10.537 11.059 38.715 1.00 53.57 A N ANISOU 729 N SER A 78 7665 6489 6198 132 -1293 496 A N ATOM 730 CA SER A 78 11.778 11.789 38.947 1.00 64.01 A C ANISOU 730 CA SER A 78 9073 7647 7601 -98 -1272 658 A C ATOM 731 C SER A 78 11.398 13.226 39.272 1.00 66.80 A C ANISOU 731 C SER A 78 9601 7564 8215 -13 -1595 686 A C ATOM 732 O SER A 78 11.001 13.979 38.380 1.00 63.21 A O ANISOU 732 O SER A 78 9338 6915 7763 -11 -1822 920 A O ATOM 733 CB SER A 78 12.698 11.723 37.728 1.00 63.48 A C ANISOU 733 CB SER A 78 9086 7733 7299 -369 -1151 994 A C ATOM 734 OG SER A 78 13.926 12.389 37.973 1.00 77.83 A O ANISOU 734 OG SER A 78 10917 9427 9229 -638 -1116 1175 A O ATOM 735 N GLU A 79 11.505 13.601 40.541 1.00 53.51 A N ANISOU 735 N GLU A 79 7874 5715 6742 78 -1646 437 A N ATOM 736 CA GLU A 79 11.158 14.941 40.992 1.00 57.87 A C ANISOU 736 CA GLU A 79 8601 5815 7570 213 -1978 366 A C ATOM 737 C GLU A 79 12.425 15.759 41.184 1.00 65.17 A C ANISOU 737 C GLU A 79 9657 6455 8651 -97 -2079 539 A C ATOM 738 O GLU A 79 13.351 15.330 41.880 1.00 57.55 A O ANISOU 738 O GLU A 79 8561 5634 7671 -255 -1909 450 A O ATOM 739 CB GLU A 79 10.371 14.892 42.302 1.00 66.04 A C ANISOU 739 CB GLU A 79 9515 6868 8710 556 -1991 -80 A C ATOM 740 CG GLU A 79 9.206 13.926 42.282 1.00 58.87 A C ANISOU 740 CG GLU A 79 8386 6313 7668 797 -1836 -243 A C ATOM 741 CD GLU A 79 8.599 13.707 43.657 1.00 66.19 A C ANISOU 741 CD GLU A 79 9136 7387 8625 1069 -1741 -640 A C ATOM 742 OE1 GLU A 79 7.925 14.625 44.169 1.00 69.93 A O ANISOU 742 OE1 GLU A 79 9657 7642 9271 1365 -1946 -869 A O ATOM 743 OE2 GLU A 79 8.779 12.604 44.212 1.00 61.49 A O ANISOU 743 OE2 GLU A 79 8357 7136 7868 1000 -1463 -718 A O ATOM 744 N VAL A 80 12.461 16.932 40.569 1.00 65.15 A N ANISOU 744 N VAL A 80 9903 6032 8819 -199 -2386 806 A N ATOM 745 CA VAL A 80 13.555 17.874 40.741 1.00 69.96 A C ANISOU 745 CA VAL A 80 10648 6278 9654 -526 -2562 999 A C ATOM 746 C VAL A 80 12.969 19.145 41.339 1.00 77.22 A C ANISOU 746 C VAL A 80 11805 6607 10928 -292 -3010 799 A C ATOM 747 O VAL A 80 11.764 19.399 41.263 1.00 84.68 A O ANISOU 747 O VAL A 80 12822 7431 11923 91 -3185 634 A O ATOM 748 CB VAL A 80 14.292 18.147 39.415 1.00 79.82 A C ANISOU 748 CB VAL A 80 11996 7534 10798 -942 -2529 1576 A C ATOM 749 CG1 VAL A 80 14.620 16.828 38.718 1.00 72.21 A C ANISOU 749 CG1 VAL A 80 10809 7191 9435 -1041 -2090 1684 A C ATOM 750 CG2 VAL A 80 13.450 19.008 38.492 1.00 74.58 A C ANISOU 750 CG2 VAL A 80 11621 6528 10189 -847 -2860 1848 A C ATOM 751 N GLU A 81 13.832 19.938 41.963 1.00 84.94 A N ANISOU 751 N GLU A 81 12888 7212 12174 -505 -3221 779 A N ATOM 752 CA GLU A 81 13.382 21.140 42.658 1.00 90.58 A C ANISOU 752 CA GLU A 81 13849 7321 13247 -262 -3680 502 A C ATOM 753 C GLU A 81 12.507 20.775 43.858 1.00 93.60 A C ANISOU 753 C GLU A 81 14110 7882 13570 254 -3616 -126 A C ATOM 754 O GLU A 81 11.530 21.460 44.163 1.00 99.14 A O ANISOU 754 O GLU A 81 14946 8279 14446 673 -3894 -418 A O ATOM 755 CB GLU A 81 12.633 22.070 41.698 1.00102.34 A C ANISOU 755 CB GLU A 81 15619 8358 14907 -161 -4043 783 A C ATOM 756 CG GLU A 81 12.644 23.537 42.086 1.00112.11 A C ANISOU 756 CG GLU A 81 17192 8797 16608 -108 -4609 701 A C ATOM 757 CD GLU A 81 12.111 24.431 40.980 1.00132.15 A C ANISOU 757 CD GLU A 81 20034 10858 19320 -105 -4991 1126 A C ATOM 758 OE1 GLU A 81 10.994 24.166 40.485 1.00142.39 A O ANISOU 758 OE1 GLU A 81 21299 12322 20481 267 -4980 1087 A O ATOM 759 OE2 GLU A 81 12.807 25.402 40.611 1.00120.05 A O ANISOU 759 OE2 GLU A 81 18747 8809 18056 -489 -5311 1510 A O ATOM 760 N VAL A 82 12.848 19.678 44.536 1.00 76.63 A N ANISOU 760 N VAL A 82 11698 6253 11166 236 -3242 -323 A N ATOM 761 CA VAL A 82 12.158 19.295 45.764 1.00 87.78 A C ANISOU 761 CA VAL A 82 12988 7897 12467 654 -3140 -865 A C ATOM 762 C VAL A 82 12.695 20.146 46.907 1.00 93.89 A C ANISOU 762 C VAL A 82 13928 8304 13441 690 -3436 -1212 A C ATOM 763 O VAL A 82 13.903 20.400 46.999 1.00 89.34 A O ANISOU 763 O VAL A 82 13406 7553 12986 293 -3542 -1048 A O ATOM 764 CB VAL A 82 12.337 17.792 46.045 1.00 82.79 A C ANISOU 764 CB VAL A 82 12050 7918 11486 591 -2671 -886 A C ATOM 765 CG1 VAL A 82 11.750 17.422 47.402 1.00 84.85 A C ANISOU 765 CG1 VAL A 82 12198 8442 11599 953 -2555 -1382 A C ATOM 766 CG2 VAL A 82 11.690 16.961 44.946 1.00 76.55 A C ANISOU 766 CG2 VAL A 82 11121 7450 10514 599 -2435 -624 A C ATOM 767 N GLN A 83 11.796 20.588 47.789 1.00 94.46 A N ANISOU 767 N GLN A 83 14063 8280 13547 1177 -3579 -1718 A N ATOM 768 CA GLN A 83 12.143 21.530 48.847 1.00 99.20 A C ANISOU 768 CA GLN A 83 14883 8474 14335 1301 -3934 -2134 A C ATOM 769 C GLN A 83 11.884 20.978 50.243 1.00101.21 A C ANISOU 769 C GLN A 83 15005 9168 14280 1619 -3725 -2661 A C ATOM 770 O GLN A 83 12.021 21.719 51.226 1.00 99.34 A O ANISOU 770 O GLN A 83 14959 8663 14121 1817 -4012 -3111 A O ATOM 771 CB GLN A 83 11.372 22.847 48.656 1.00 98.64 A C ANISOU 771 CB GLN A 83 15092 7767 14619 1643 -4402 -2319 A C ATOM 772 CG GLN A 83 9.885 22.816 49.043 1.00120.04 A C ANISOU 772 CG GLN A 83 17691 10691 17227 2300 -4320 -2762 A C ATOM 773 CD GLN A 83 9.061 21.817 48.243 1.00127.84 A C ANISOU 773 CD GLN A 83 18375 12204 17992 2354 -3933 -2488 A C ATOM 774 NE2 GLN A 83 7.837 22.204 47.896 1.00130.80 A N ANISOU 774 NE2 GLN A 83 18715 12488 18493 2795 -4058 -2619 A N ATOM 775 OE1 GLN A 83 9.515 20.712 47.946 1.00107.85 A O ANISOU 775 OE1 GLN A 83 15639 10139 15200 2020 -3557 -2184 A O ATOM 776 N GLU A 84 11.525 19.702 50.365 1.00101.70 A N ANISOU 776 N GLU A 84 14770 9891 13980 1664 -3254 -2612 A N ATOM 777 CA GLU A 84 11.167 19.135 51.661 1.00 93.51 A C ANISOU 777 CA GLU A 84 13605 9323 12601 1958 -3025 -3042 A C ATOM 778 C GLU A 84 11.274 17.620 51.576 1.00 92.60 A C ANISOU 778 C GLU A 84 13194 9831 12160 1758 -2553 -2771 A C ATOM 779 O GLU A 84 10.704 17.006 50.669 1.00 86.66 A O ANISOU 779 O GLU A 84 12270 9269 11387 1722 -2340 -2486 A O ATOM 780 CB GLU A 84 9.751 19.581 52.058 1.00113.51 A C ANISOU 780 CB GLU A 84 16108 11914 15108 2548 -3035 -3475 A C ATOM 781 CG GLU A 84 9.165 18.925 53.303 1.00129.11 A C ANISOU 781 CG GLU A 84 17894 14499 16661 2872 -2706 -3870 A C ATOM 782 CD GLU A 84 7.643 18.978 53.328 1.00149.05 A C ANISOU 782 CD GLU A 84 20208 17283 19143 3378 -2547 -4121 A C ATOM 783 OE1 GLU A 84 7.060 18.771 54.413 1.00152.49 A O ANISOU 783 OE1 GLU A 84 20512 18166 19259 3721 -2326 -4521 A O ATOM 784 OE2 GLU A 84 7.030 19.233 52.268 1.00134.34 A O ANISOU 784 OE2 GLU A 84 18291 15205 17547 3434 -2644 -3912 A O ATOM 785 N ARG A 85 12.008 17.026 52.516 1.00 82.12 A N ANISOU 785 N ARG A 85 11827 8786 10591 1635 -2438 -2865 A N ATOM 786 CA ARG A 85 12.199 15.583 52.518 1.00 73.38 A C ANISOU 786 CA ARG A 85 10475 8199 9207 1448 -2049 -2609 A C ATOM 787 C ARG A 85 10.937 14.871 52.982 1.00 69.10 A C ANISOU 787 C ARG A 85 9730 8145 8381 1768 -1722 -2764 A C ATOM 788 O ARG A 85 10.226 15.345 53.872 1.00 71.49 A O ANISOU 788 O ARG A 85 10064 8549 8550 2140 -1740 -3173 A O ATOM 789 CB ARG A 85 13.360 15.190 53.432 1.00 72.38 A C ANISOU 789 CB ARG A 85 10374 8205 8919 1245 -2079 -2652 A C ATOM 790 CG ARG A 85 14.724 15.239 52.778 1.00 76.23 A C ANISOU 790 CG ARG A 85 10873 8446 9644 800 -2226 -2321 A C ATOM 791 CD ARG A 85 15.824 14.917 53.776 1.00 71.76 A C ANISOU 791 CD ARG A 85 10306 8013 8947 648 -2316 -2411 A C ATOM 792 NE ARG A 85 17.078 15.556 53.401 1.00 73.35 A N ANISOU 792 NE ARG A 85 10554 7846 9472 285 -2610 -2251 A N ATOM 793 CZ ARG A 85 18.007 14.997 52.638 1.00 70.75 A C ANISOU 793 CZ ARG A 85 10033 7591 9260 -68 -2499 -1860 A C ATOM 794 NH1 ARG A 85 17.871 13.767 52.169 1.00 65.80 A N ANISOU 794 NH1 ARG A 85 9196 7346 8458 -87 -2137 -1623 A N ATOM 795 NH2 ARG A 85 19.100 15.692 52.334 1.00 71.56 A N ANISOU 795 NH2 ARG A 85 10138 7376 9674 -411 -2765 -1715 A N ATOM 796 N AMET A 86 10.665 13.728 52.354 0.61 67.77 A N ANISOU 796 N AMET A 86 9339 8284 8125 1615 -1425 -2440 A N ATOM 797 N BMET A 86 10.663 13.712 52.384 0.39 67.78 A N ANISOU 797 N BMET A 86 9339 8296 8119 1617 -1420 -2444 A N ATOM 798 CA AMET A 86 9.551 12.877 52.745 0.61 66.87 A C ANISOU 798 CA AMET A 86 8982 8655 7769 1807 -1099 -2492 A C ATOM 799 CA BMET A 86 9.514 12.912 52.789 0.39 66.88 A C ANISOU 799 CA BMET A 86 8985 8660 7766 1825 -1101 -2512 A C ATOM 800 C AMET A 86 9.897 12.042 53.970 0.61 67.53 A C ANISOU 800 C AMET A 86 9018 9146 7493 1765 -903 -2551 A C ATOM 801 C BMET A 86 9.848 11.898 53.875 0.39 67.53 A C ANISOU 801 C BMET A 86 8991 9174 7494 1743 -871 -2506 A C ATOM 802 O AMET A 86 9.077 11.903 54.885 0.61 68.48 A O ANISOU 802 O AMET A 86 9036 9634 7348 2020 -720 -2776 A O ATOM 803 O BMET A 86 8.943 11.482 54.608 0.39 70.92 A O ANISOU 803 O BMET A 86 9261 10018 7668 1943 -631 -2636 A O ATOM 804 CB AMET A 86 9.185 11.961 51.579 0.61 65.95 A C ANISOU 804 CB AMET A 86 8678 8648 7731 1620 -925 -2123 A C ATOM 805 CB BMET A 86 8.924 12.178 51.578 0.39 65.70 A C ANISOU 805 CB BMET A 86 8643 8596 7723 1703 -948 -2184 A C ATOM 806 CG AMET A 86 7.722 11.884 51.247 0.61 70.37 A C ANISOU 806 CG AMET A 86 9021 9395 8322 1866 -807 -2181 A C ATOM 807 CG BMET A 86 8.052 13.057 50.693 0.39 67.98 A C ANISOU 807 CG BMET A 86 8940 8619 8269 1912 -1125 -2229 A C ATOM 808 SD AMET A 86 7.505 10.949 49.720 0.61 66.71 A S ANISOU 808 SD AMET A 86 8419 8945 7981 1605 -731 -1768 A S ATOM 809 SD BMET A 86 6.784 12.150 49.779 0.39 70.01 A S ANISOU 809 SD BMET A 86 8882 9174 8546 1938 -920 -2025 A S ATOM 810 CE AMET A 86 6.842 12.219 48.648 0.61 72.87 A C ANISOU 810 CE AMET A 86 9295 9332 9059 1815 -1041 -1803 A C ATOM 811 CE BMET A 86 5.893 11.354 51.112 0.39 74.12 A C ANISOU 811 CE BMET A 86 9102 10290 8771 2119 -566 -2227 A C ATOM 812 N PHE A 87 11.112 11.496 54.004 1.00 68.16 A N ANISOU 812 N PHE A 87 9162 9187 7550 1455 -943 -2339 A N ATOM 813 CA PHE A 87 11.543 10.552 55.036 1.00 68.60 A C ANISOU 813 CA PHE A 87 9183 9601 7281 1374 -796 -2298 A C ATOM 814 C PHE A 87 12.824 11.048 55.699 1.00 69.89 A C ANISOU 814 C PHE A 87 9548 9577 7429 1274 -1076 -2425 A C ATOM 815 O PHE A 87 13.874 10.403 55.624 1.00 59.72 A O ANISOU 815 O PHE A 87 8240 8286 6167 1013 -1113 -2194 A O ATOM 816 CB PHE A 87 11.748 9.167 54.424 1.00 69.16 A C ANISOU 816 CB PHE A 87 9088 9829 7360 1111 -594 -1897 A C ATOM 817 CG PHE A 87 10.623 8.724 53.523 1.00 63.12 A C ANISOU 817 CG PHE A 87 8133 9152 6697 1142 -407 -1753 A C ATOM 818 CD1 PHE A 87 9.405 8.335 54.055 1.00 69.96 A C ANISOU 818 CD1 PHE A 87 8825 10382 7375 1308 -175 -1818 A C ATOM 819 CD2 PHE A 87 10.789 8.699 52.148 1.00 61.91 A C ANISOU 819 CD2 PHE A 87 7961 8752 6810 994 -467 -1550 A C ATOM 820 CE1 PHE A 87 8.372 7.924 53.230 1.00 68.95 A C ANISOU 820 CE1 PHE A 87 8487 10334 7378 1312 -44 -1690 A C ATOM 821 CE2 PHE A 87 9.761 8.291 51.317 1.00 63.58 A C ANISOU 821 CE2 PHE A 87 8012 9042 7102 1022 -349 -1439 A C ATOM 822 CZ PHE A 87 8.550 7.906 51.861 1.00 65.10 A C ANISOU 822 CZ PHE A 87 8012 9563 7161 1177 -157 -1514 A C ATOM 823 N PRO A 88 12.769 12.198 56.374 1.00 65.42 A N ANISOU 823 N PRO A 88 9171 8848 6839 1496 -1307 -2819 A N ATOM 824 CA PRO A 88 14.007 12.794 56.905 1.00 73.49 A C ANISOU 824 CA PRO A 88 10389 9616 7918 1368 -1657 -2958 A C ATOM 825 C PRO A 88 14.729 11.951 57.948 1.00 75.71 A C ANISOU 825 C PRO A 88 10674 10231 7860 1274 -1632 -2917 A C ATOM 826 O PRO A 88 15.941 12.131 58.124 1.00 74.74 A O ANISOU 826 O PRO A 88 10623 9919 7854 1066 -1911 -2895 A O ATOM 827 CB PRO A 88 13.518 14.121 57.508 1.00 74.29 A C ANISOU 827 CB PRO A 88 10706 9503 8017 1703 -1902 -3463 A C ATOM 828 CG PRO A 88 12.083 13.874 57.824 1.00 79.56 A C ANISOU 828 CG PRO A 88 11247 10566 8417 2060 -1577 -3625 A C ATOM 829 CD PRO A 88 11.592 13.033 56.677 1.00 74.25 A C ANISOU 829 CD PRO A 88 10323 9984 7905 1892 -1297 -3192 A C ATOM 830 N ASP A 89 14.044 11.048 58.647 1.00 72.00 A N ANISOU 830 N ASP A 89 10119 10250 6987 1402 -1331 -2880 A N ATOM 831 CA ASP A 89 14.671 10.273 59.713 1.00 88.83 A C ANISOU 831 CA ASP A 89 12299 12700 8753 1334 -1342 -2817 A C ATOM 832 C ASP A 89 15.253 8.944 59.238 1.00 77.07 A C ANISOU 832 C ASP A 89 10643 11297 7343 1048 -1215 -2344 A C ATOM 833 O ASP A 89 15.769 8.183 60.062 1.00 72.13 A O ANISOU 833 O ASP A 89 10051 10912 6442 989 -1242 -2226 A O ATOM 834 CB ASP A 89 13.660 9.995 60.835 1.00 99.11 A C ANISOU 834 CB ASP A 89 13620 14520 9517 1608 -1087 -2992 A C ATOM 835 CG ASP A 89 13.199 11.256 61.542 1.00107.46 A C ANISOU 835 CG ASP A 89 14864 15557 10408 1964 -1232 -3552 A C ATOM 836 OD1 ASP A 89 14.000 12.208 61.658 1.00105.59 A O ANISOU 836 OD1 ASP A 89 14834 14935 10352 1961 -1639 -3824 A O ATOM 837 OD2 ASP A 89 12.033 11.289 61.992 1.00100.51 A O ANISOU 837 OD2 ASP A 89 13896 15026 9269 2227 -936 -3690 A O ATOM 838 N TRP A 90 15.186 8.645 57.943 1.00 62.32 A N ANISOU 838 N TRP A 90 8615 9233 5830 895 -1104 -2084 A N ATOM 839 CA TRP A 90 15.487 7.307 57.437 1.00 60.69 A C ANISOU 839 CA TRP A 90 8250 9125 5686 697 -945 -1691 A C ATOM 840 C TRP A 90 16.562 7.385 56.361 1.00 62.00 A C ANISOU 840 C TRP A 90 8335 8971 6249 477 -1088 -1532 A C ATOM 841 O TRP A 90 16.273 7.738 55.217 1.00 53.90 A O ANISOU 841 O TRP A 90 7248 7749 5482 431 -1027 -1472 A O ATOM 842 CB TRP A 90 14.234 6.645 56.862 1.00 61.75 A C ANISOU 842 CB TRP A 90 8236 9419 5807 737 -622 -1530 A C ATOM 843 CG TRP A 90 13.170 6.315 57.851 1.00 66.63 A C ANISOU 843 CG TRP A 90 8839 10442 6037 895 -402 -1587 A C ATOM 844 CD1 TRP A 90 13.276 6.301 59.203 1.00 71.71 A C ANISOU 844 CD1 TRP A 90 9607 11374 6267 995 -426 -1706 A C ATOM 845 CD2 TRP A 90 11.831 5.922 57.546 1.00 72.12 A C ANISOU 845 CD2 TRP A 90 9357 11345 6700 954 -112 -1504 A C ATOM 846 CE2 TRP A 90 11.174 5.693 58.767 1.00 82.33 A C ANISOU 846 CE2 TRP A 90 10645 13080 7556 1076 71 -1560 A C ATOM 847 CE3 TRP A 90 11.123 5.743 56.352 1.00 68.91 A C ANISOU 847 CE3 TRP A 90 8782 10817 6582 907 0 -1384 A C ATOM 848 NE1 TRP A 90 12.077 5.935 59.769 1.00 75.48 A N ANISOU 848 NE1 TRP A 90 9988 12262 6428 1110 -123 -1687 A N ATOM 849 CZ2 TRP A 90 9.839 5.298 58.832 1.00 85.41 A C ANISOU 849 CZ2 TRP A 90 10819 13806 7828 1131 386 -1483 A C ATOM 850 CZ3 TRP A 90 9.804 5.349 56.418 1.00 68.22 A C ANISOU 850 CZ3 TRP A 90 8497 11024 6399 970 260 -1331 A C ATOM 851 CH2 TRP A 90 9.174 5.132 57.650 1.00 80.88 A C ANISOU 851 CH2 TRP A 90 10050 13076 7602 1071 463 -1372 A C ATOM 852 N SER A 91 17.798 7.027 56.710 1.00 53.92 A N ANISOU 852 N SER A 91 7292 7936 5259 345 -1272 -1447 A N ATOM 853 CA ASER A 91 18.839 6.931 55.691 0.72 51.99 A C ANISOU 853 CA ASER A 91 6894 7490 5370 140 -1340 -1269 A C ATOM 854 CA BSER A 91 18.841 6.931 55.692 0.28 52.21 A C ANISOU 854 CA BSER A 91 6922 7518 5398 140 -1341 -1269 A C ATOM 855 C SER A 91 18.469 5.901 54.631 1.00 56.41 A C ANISOU 855 C SER A 91 7306 8100 6028 98 -1073 -1015 A C ATOM 856 O SER A 91 18.699 6.116 53.436 1.00 52.96 A O ANISOU 856 O SER A 91 6773 7511 5837 -7 -1019 -921 A O ATOM 857 CB ASER A 91 20.176 6.584 56.346 0.72 54.87 A C ANISOU 857 CB ASER A 91 7202 7897 5750 45 -1579 -1229 A C ATOM 858 CB BSER A 91 20.178 6.583 56.345 0.28 55.04 A C ANISOU 858 CB BSER A 91 7222 7918 5771 45 -1579 -1229 A C ATOM 859 OG ASER A 91 20.694 7.707 57.028 0.72 60.86 A O ANISOU 859 OG ASER A 91 8078 8524 6522 24 -1894 -1479 A O ATOM 860 OG BSER A 91 20.042 5.485 57.230 0.28 61.04 A O ANISOU 860 OG BSER A 91 8020 8936 6238 135 -1535 -1129 A O ATOM 861 N MET A 92 17.899 4.774 55.052 1.00 53.97 A N ANISOU 861 N MET A 92 6991 8000 5514 166 -920 -894 A N ATOM 862 CA MET A 92 17.277 3.801 54.161 1.00 55.60 A C ANISOU 862 CA MET A 92 7100 8230 5795 145 -699 -705 A C ATOM 863 C MET A 92 16.471 2.834 55.014 1.00 62.82 A C ANISOU 863 C MET A 92 8054 9370 6447 199 -581 -596 A C ATOM 864 O MET A 92 17.019 1.862 55.548 1.00 61.41 A O ANISOU 864 O MET A 92 7878 9251 6202 165 -648 -435 A O ATOM 865 CB MET A 92 18.284 3.022 53.320 1.00 48.56 A C ANISOU 865 CB MET A 92 6068 7251 5131 50 -714 -548 A C ATOM 866 CG MET A 92 17.655 2.232 52.153 1.00 53.98 A C ANISOU 866 CG MET A 92 6684 7904 5921 40 -526 -432 A C ATOM 867 SD MET A 92 16.174 2.928 51.397 1.00 52.97 A S ANISOU 867 SD MET A 92 6597 7750 5782 76 -378 -502 A S ATOM 868 CE MET A 92 16.852 4.489 50.832 1.00 51.38 A C ANISOU 868 CE MET A 92 6421 7369 5731 20 -498 -608 A C ATOM 869 N GLN A 93 15.183 3.100 55.165 1.00 51.80 A N ANISOU 869 N GLN A 93 6670 8103 4910 278 -416 -661 A N ATOM 870 CA GLN A 93 14.317 2.222 55.934 1.00 57.17 A C ANISOU 870 CA GLN A 93 7342 9042 5339 281 -258 -512 A C ATOM 871 C GLN A 93 13.881 1.071 55.040 1.00 59.71 A C ANISOU 871 C GLN A 93 7550 9285 5851 164 -147 -277 A C ATOM 872 O GLN A 93 13.435 1.286 53.910 1.00 57.33 A O ANISOU 872 O GLN A 93 7167 8854 5760 158 -89 -322 A O ATOM 873 CB GLN A 93 13.108 2.991 56.460 1.00 58.30 A C ANISOU 873 CB GLN A 93 7478 9412 5263 427 -104 -698 A C ATOM 874 CG GLN A 93 12.167 2.168 57.318 1.00 63.78 A C ANISOU 874 CG GLN A 93 8115 10460 5657 403 110 -520 A C ATOM 875 CD GLN A 93 12.612 2.102 58.763 1.00 70.32 A C ANISOU 875 CD GLN A 93 9098 11543 6076 445 51 -517 A C ATOM 876 NE2 GLN A 93 11.665 1.876 59.663 1.00 85.18 A N ANISOU 876 NE2 GLN A 93 10942 13832 7590 481 278 -454 A N ATOM 877 OE1 GLN A 93 13.797 2.256 59.067 1.00 82.16 A O ANISOU 877 OE1 GLN A 93 10736 12907 7575 442 -199 -566 A O ATOM 878 N THR A 94 14.015 -0.147 55.542 1.00 55.45 A N ANISOU 878 N THR A 94 7030 8799 5240 72 -157 -26 A N ATOM 879 CA THR A 94 13.721 -1.349 54.771 1.00 56.76 A C ANISOU 879 CA THR A 94 7127 8821 5620 -45 -124 183 A C ATOM 880 C THR A 94 12.461 -1.980 55.338 1.00 55.76 A C ANISOU 880 C THR A 94 6944 8905 5335 -149 46 384 A C ATOM 881 O THR A 94 12.382 -2.232 56.539 1.00 55.45 A O ANISOU 881 O THR A 94 6973 9093 5004 -179 76 531 A O ATOM 882 CB THR A 94 14.905 -2.310 54.814 1.00 61.30 A C ANISOU 882 CB THR A 94 7763 9212 6317 -72 -318 327 A C ATOM 883 CG2 THR A 94 14.601 -3.588 54.057 1.00 61.87 A C ANISOU 883 CG2 THR A 94 7802 9080 6624 -163 -330 498 A C ATOM 884 OG1 THR A 94 16.035 -1.668 54.210 1.00 59.77 A O ANISOU 884 OG1 THR A 94 7540 8882 6286 7 -432 141 A O ATOM 885 N ILE A 95 11.467 -2.196 54.482 1.00 53.48 A N ANISOU 885 N ILE A 95 6519 8578 5223 -215 154 400 A N ATOM 886 CA ILE A 95 10.187 -2.755 54.891 1.00 54.87 A C ANISOU 886 CA ILE A 95 6562 8972 5314 -355 327 600 A C ATOM 887 C ILE A 95 9.948 -3.988 54.032 1.00 55.33 A C ANISOU 887 C ILE A 95 6581 8759 5682 -538 236 791 A C ATOM 888 O ILE A 95 9.678 -3.871 52.830 1.00 55.99 A O ANISOU 888 O ILE A 95 6596 8673 6006 -517 196 645 A O ATOM 889 CB ILE A 95 9.041 -1.747 54.743 1.00 61.24 A C ANISOU 889 CB ILE A 95 7186 10019 6062 -249 514 400 A C ATOM 890 CG1 ILE A 95 9.243 -0.550 55.674 1.00 67.89 A C ANISOU 890 CG1 ILE A 95 8100 11100 6596 -35 573 163 A C ATOM 891 CG2 ILE A 95 7.717 -2.401 55.089 1.00 63.98 A C ANISOU 891 CG2 ILE A 95 7312 10631 6367 -421 709 628 A C ATOM 892 CD1 ILE A 95 8.581 0.726 55.182 1.00 68.89 A C ANISOU 892 CD1 ILE A 95 8122 11268 6786 174 629 -157 A C ATOM 893 N ASN A 96 10.052 -5.168 54.641 1.00 54.62 A N ANISOU 893 N ASN A 96 6562 8608 5582 -715 169 1114 A N ATOM 894 CA ASN A 96 9.751 -6.426 53.961 1.00 63.54 A C ANISOU 894 CA ASN A 96 7680 9434 7026 -908 37 1303 A C ATOM 895 C ASN A 96 8.268 -6.723 54.153 1.00 52.12 A C ANISOU 895 C ASN A 96 6014 8206 5583 -1142 209 1505 A C ATOM 896 O ASN A 96 7.841 -7.193 55.210 1.00 58.28 A O ANISOU 896 O ASN A 96 6765 9206 6172 -1328 316 1834 A O ATOM 897 CB ASN A 96 10.620 -7.557 54.495 1.00 67.72 A C ANISOU 897 CB ASN A 96 8410 9716 7605 -981 -178 1568 A C ATOM 898 CG ASN A 96 10.506 -8.815 53.660 1.00 75.89 A C ANISOU 898 CG ASN A 96 9486 10321 9027 -1119 -391 1672 A C ATOM 899 ND2 ASN A 96 11.601 -9.554 53.549 1.00 69.01 A N ANISOU 899 ND2 ASN A 96 8796 9108 8318 -1019 -647 1687 A N ATOM 900 OD1 ASN A 96 9.444 -9.114 53.110 1.00 70.14 A O ANISOU 900 OD1 ASN A 96 8619 9563 8468 -1296 -353 1711 A O ATOM 901 N LEU A 97 7.473 -6.455 53.123 1.00 58.68 A N ANISOU 901 N LEU A 97 6670 9003 6623 -1146 231 1330 A N ATOM 902 CA LEU A 97 6.037 -6.640 53.252 1.00 71.54 A C ANISOU 902 CA LEU A 97 8011 10878 8294 -1359 389 1493 A C ATOM 903 C LEU A 97 5.639 -8.109 53.210 1.00 65.40 A C ANISOU 903 C LEU A 97 7223 9852 7775 -1715 240 1853 A C ATOM 904 O LEU A 97 4.558 -8.456 53.698 1.00 65.36 A O ANISOU 904 O LEU A 97 6971 10096 7766 -1983 389 2128 A O ATOM 905 CB LEU A 97 5.315 -5.859 52.157 1.00 71.12 A C ANISOU 905 CB LEU A 97 7765 10858 8399 -1233 402 1190 A C ATOM 906 CG LEU A 97 4.837 -4.471 52.598 1.00 77.35 A C ANISOU 906 CG LEU A 97 8391 12059 8941 -998 640 976 A C ATOM 907 CD1 LEU A 97 4.758 -3.558 51.371 1.00 76.47 A C ANISOU 907 CD1 LEU A 97 8263 11809 8985 -776 533 636 A C ATOM 908 CD2 LEU A 97 3.526 -4.511 53.340 1.00 92.61 A C ANISOU 908 CD2 LEU A 97 9973 14439 10776 -1137 898 1151 A C ATOM 909 N ASP A 98 6.483 -8.982 52.648 1.00 62.29 A N ANISOU 909 N ASP A 98 7076 8970 7621 -1726 -58 1855 A N ATOM 910 CA ASP A 98 6.200 -10.413 52.723 1.00 69.23 A C ANISOU 910 CA ASP A 98 8007 9527 8771 -2059 -261 2206 A C ATOM 911 C ASP A 98 6.067 -10.871 54.168 1.00 69.41 A C ANISOU 911 C ASP A 98 8044 9771 8557 -2293 -135 2686 A C ATOM 912 O ASP A 98 5.254 -11.752 54.473 1.00 76.22 A O ANISOU 912 O ASP A 98 8795 10597 9567 -2677 -157 3080 A O ATOM 913 CB ASP A 98 7.297 -11.228 52.027 1.00 65.97 A C ANISOU 913 CB ASP A 98 7896 8551 8620 -1938 -613 2081 A C ATOM 914 CG ASP A 98 7.372 -10.969 50.527 1.00 69.47 A C ANISOU 914 CG ASP A 98 8340 8790 9266 -1747 -742 1641 A C ATOM 915 OD1 ASP A 98 6.310 -10.892 49.870 1.00 67.66 A O ANISOU 915 OD1 ASP A 98 7913 8616 9178 -1883 -739 1572 A O ATOM 916 OD2 ASP A 98 8.500 -10.875 50.000 1.00 76.46 A O ANISOU 916 OD2 ASP A 98 9413 9480 10159 -1465 -855 1377 A O ATOM 917 N GLU A 99 6.842 -10.272 55.071 1.00 80.23 A N ANISOU 917 N GLU A 99 9551 11386 9547 -2088 -15 2676 A N ATOM 918 CA GLU A 99 6.899 -10.690 56.465 1.00 89.99 A C ANISOU 918 CA GLU A 99 10874 12848 10471 -2265 72 3125 A C ATOM 919 C GLU A 99 5.906 -9.958 57.356 1.00 78.75 A C ANISOU 919 C GLU A 99 9179 12100 8641 -2341 487 3232 A C ATOM 920 O GLU A 99 5.762 -10.326 58.527 1.00 81.02 A O ANISOU 920 O GLU A 99 9506 12673 8605 -2531 615 3647 A O ATOM 921 CB GLU A 99 8.316 -10.470 57.005 1.00 94.25 A C ANISOU 921 CB GLU A 99 11716 13306 10790 -1988 -71 3040 A C ATOM 922 CG GLU A 99 9.358 -11.376 56.378 1.00 96.42 A C ANISOU 922 CG GLU A 99 12239 12960 11436 -1907 -473 3010 A C ATOM 923 CD GLU A 99 10.728 -11.207 57.002 1.00112.01 A C ANISOU 923 CD GLU A 99 14447 14897 13214 -1650 -628 2967 A C ATOM 924 OE1 GLU A 99 11.587 -12.093 56.799 1.00106.13 A O ANISOU 924 OE1 GLU A 99 13898 13692 12735 -1585 -964 3036 A O ATOM 925 OE2 GLU A 99 10.947 -10.185 57.686 1.00111.72 A O ANISOU 925 OE2 GLU A 99 14390 15281 12778 -1494 -443 2837 A O ATOM 926 N ASN A 100 5.219 -8.945 56.840 1.00 83.69 A N ANISOU 926 N ASN A 100 10915 14604 6278 1618 -1195 1798 A N ATOM 927 CA ASN A 100 4.296 -8.150 57.638 1.00 80.72 A C ANISOU 927 CA ASN A 100 10677 14374 5619 1494 -1015 1677 A C ATOM 928 C ASN A 100 2.925 -8.815 57.667 1.00 78.41 A C ANISOU 928 C ASN A 100 10571 13860 5360 1406 -631 1925 A C ATOM 929 O ASN A 100 2.429 -9.289 56.640 1.00 89.17 A O ANISOU 929 O ASN A 100 11851 14913 7115 1310 -464 1996 A O ATOM 930 CB ASN A 100 4.196 -6.735 57.062 1.00 81.46 A C ANISOU 930 CB ASN A 100 10565 14483 5903 1292 -1012 1252 A C ATOM 931 CG ASN A 100 3.258 -5.845 57.850 1.00 82.24 A C ANISOU 931 CG ASN A 100 10791 14720 5735 1191 -830 1081 A C ATOM 932 ND2 ASN A 100 3.825 -4.941 58.638 1.00 79.61 A N ANISOU 932 ND2 ASN A 100 10464 14683 5102 1206 -1026 824 A N ATOM 933 OD1 ASN A 100 2.037 -5.963 57.745 1.00 87.44 A O ANISOU 933 OD1 ASN A 100 11527 15232 6466 1099 -516 1155 A O ATOM 934 N THR A 101 2.316 -8.847 58.855 1.00 84.90 A N ANISOU 934 N THR A 101 11640 14858 5759 1426 -484 2040 A N ATOM 935 CA THR A 101 0.995 -9.437 59.049 1.00 89.62 A C ANISOU 935 CA THR A 101 12409 15297 6345 1313 -84 2259 A C ATOM 936 C THR A 101 0.099 -8.521 59.874 1.00 84.27 A C ANISOU 936 C THR A 101 11803 14841 5374 1206 129 2063 A C ATOM 937 O THR A 101 -0.757 -8.991 60.629 1.00 91.45 A O ANISOU 937 O THR A 101 12929 15784 6035 1167 423 2268 A O ATOM 938 CB THR A 101 1.092 -10.810 59.721 1.00 80.92 A C ANISOU 938 CB THR A 101 11616 14129 5003 1461 -34 2722 A C ATOM 939 CG2 THR A 101 1.392 -11.895 58.691 1.00 93.99 A C ANISOU 939 CG2 THR A 101 13214 15420 7075 1501 -61 2935 A C ATOM 940 OG1 THR A 101 2.122 -10.790 60.718 1.00 92.37 A O ANISOU 940 OG1 THR A 101 13193 15755 6148 1639 -348 2711 A O ATOM 941 N AASP A 102 0.275 -7.211 59.749 0.81 83.90 A N ANISOU 941 N AASP A 102 11587 14938 5352 1152 7 1661 A N ATOM 942 N BASP A 102 0.304 -7.213 59.759 0.19 83.96 A N ANISOU 942 N BASP A 102 11596 14949 5355 1155 -1 1662 A N ATOM 943 CA AASP A 102 -0.636 -6.286 60.410 0.81 86.93 A C ANISOU 943 CA AASP A 102 12018 15493 5517 1061 226 1429 A C ATOM 944 CA BASP A 102 -0.515 -6.241 60.469 0.19 86.52 A C ANISOU 944 CA BASP A 102 11971 15467 5436 1074 190 1417 A C ATOM 945 C AASP A 102 -1.983 -6.285 59.693 0.81 87.50 A C ANISOU 945 C AASP A 102 11968 15336 5943 895 585 1393 A C ATOM 946 C BASP A 102 -1.925 -6.233 59.889 0.19 87.31 A C ANISOU 946 C BASP A 102 11973 15361 5839 910 572 1388 A C ATOM 947 O AASP A 102 -2.050 -6.267 58.459 0.81 79.00 A O ANISOU 947 O AASP A 102 10682 14004 5329 824 558 1323 A O ATOM 948 O BASP A 102 -2.100 -6.254 58.670 0.19 80.54 A O ANISOU 948 O BASP A 102 10910 14241 5450 830 578 1330 A O ATOM 949 CB AASP A 102 -0.041 -4.881 60.438 0.81 84.95 A C ANISOU 949 CB AASP A 102 11643 15410 5225 1052 -13 995 A C ATOM 950 CB BASP A 102 0.100 -4.845 60.380 0.19 84.54 A C ANISOU 950 CB BASP A 102 11575 15358 5189 1057 -54 980 A C ATOM 951 CG AASP A 102 -0.966 -3.872 61.094 0.81 87.63 A C ANISOU 951 CG AASP A 102 12037 15902 5355 985 208 718 A C ATOM 952 CG BASP A 102 1.346 -4.698 61.231 0.19 80.85 A C ANISOU 952 CG BASP A 102 11188 15114 4417 1177 -407 922 A C ATOM 953 OD1AASP A 102 -1.866 -3.349 60.402 0.81 90.91 A O ANISOU 953 OD1AASP A 102 12309 16142 6091 878 413 544 A O ATOM 954 OD1BASP A 102 1.582 -5.558 62.104 0.19 80.78 A O ANISOU 954 OD1BASP A 102 11390 15135 4170 1282 -440 1191 A O ATOM 955 OD2AASP A 102 -0.798 -3.608 62.298 0.81 99.99 A O ANISOU 955 OD2AASP A 102 13785 17654 6553 1028 166 650 A O ATOM 956 OD2BASP A 102 2.091 -3.716 61.027 0.19 81.89 A O ANISOU 956 OD2BASP A 102 11173 15322 4620 1141 -649 587 A O ATOM 957 N APHE A 103 -3.064 -6.303 60.482 0.48 87.24 A N ANISOU 957 N APHE A 103 12054 15418 5674 835 923 1428 A N ATOM 958 N CPHE A 103 -2.887 -6.737 59.641 0.52 89.12 A N ANISOU 958 N CPHE A 103 12187 15444 6229 813 862 1513 A N ATOM 959 CA APHE A 103 -4.400 -6.479 59.919 0.48 89.99 A C ANISOU 959 CA APHE A 103 12265 15589 6338 681 1282 1421 A C ATOM 960 CA CPHE A 103 -4.311 -6.504 59.871 0.52 89.95 A C ANISOU 960 CA CPHE A 103 12258 15573 6345 687 1256 1428 A C ATOM 961 C APHE A 103 -4.726 -5.404 58.891 0.48 86.62 A C ANISOU 961 C APHE A 103 11560 15043 6307 630 1228 1048 A C ATOM 962 C CPHE A 103 -4.796 -5.389 58.944 0.52 86.62 A C ANISOU 962 C CPHE A 103 11564 15054 6293 627 1249 1044 A C ATOM 963 O APHE A 103 -5.384 -5.677 57.880 0.48 80.97 A O ANISOU 963 O APHE A 103 10661 14095 6008 538 1345 1052 A O ATOM 964 O CPHE A 103 -5.619 -5.629 58.059 0.52 80.93 A O ANISOU 964 O CPHE A 103 10664 14128 5959 528 1415 1039 A O ATOM 965 CB APHE A 103 -5.446 -6.464 61.036 0.48 96.16 A C ANISOU 965 CB APHE A 103 13187 16581 6767 626 1660 1445 A C ATOM 966 CB CPHE A 103 -4.559 -6.170 61.345 0.52 95.89 A C ANISOU 966 CB CPHE A 103 13237 16660 6535 733 1398 1402 A C ATOM 967 CG APHE A 103 -5.905 -5.080 61.420 0.48100.19 A C ANISOU 967 CG APHE A 103 13614 17298 7154 640 1717 1026 A C ATOM 968 CG CPHE A 103 -5.982 -5.787 61.663 0.52102.11 A C ANISOU 968 CG CPHE A 103 13958 17528 7310 619 1815 1251 A C ATOM 969 CD1APHE A 103 -5.183 -4.320 62.329 0.48101.95 A C ANISOU 969 CD1APHE A 103 13996 17785 6955 752 1515 850 A C ATOM 970 CD1CPHE A 103 -6.991 -6.738 61.674 0.52100.78 A C ANISOU 970 CD1CPHE A 103 13797 17258 7238 481 2197 1498 A C ATOM 971 CD2APHE A 103 -7.055 -4.537 60.866 0.48 97.16 A C ANISOU 971 CD2APHE A 103 12993 16836 7088 555 1957 786 A C ATOM 972 CD2CPHE A 103 -6.301 -4.478 61.991 0.52105.42 A C ANISOU 972 CD2CPHE A 103 14305 18129 7620 650 1834 847 A C ATOM 973 CE1APHE A 103 -5.605 -3.049 62.682 0.48100.53 A C ANISOU 973 CE1APHE A 103 13765 17726 6706 760 1568 441 A C ATOM 974 CE1CPHE A 103 -8.296 -6.385 61.978 0.52 93.21 A C ANISOU 974 CE1CPHE A 103 12725 16409 6280 373 2593 1333 A C ATOM 975 CE2APHE A 103 -7.478 -3.266 61.214 0.48 98.96 A C ANISOU 975 CE2APHE A 103 13160 17224 7216 603 2008 395 A C ATOM 976 CE2CPHE A 103 -7.604 -4.121 62.300 0.52102.09 A C ANISOU 976 CE2CPHE A 103 13795 17801 7193 579 2220 686 A C ATOM 977 CZ APHE A 103 -6.752 -2.521 62.123 0.48101.16 A C ANISOU 977 CZ APHE A 103 13625 17739 7073 704 1829 223 A C ATOM 978 CZ CPHE A 103 -8.601 -5.076 62.294 0.52 92.49 A C ANISOU 978 CZ CPHE A 103 12542 16518 6082 440 2601 925 A C ATOM 979 N LEU A 104 -4.275 -4.175 59.130 1.00 85.09 A N ANISOU 979 N LEU A 104 11351 14996 5982 689 1043 720 A N ATOM 980 CA LEU A 104 -4.597 -3.080 58.225 1.00 84.42 A C ANISOU 980 CA LEU A 104 11065 14775 6238 657 1000 377 A C ATOM 981 C LEU A 104 -3.669 -3.065 57.018 1.00 77.05 A C ANISOU 981 C LEU A 104 10011 13614 5650 649 710 368 A C ATOM 982 O LEU A 104 -4.076 -2.621 55.938 1.00 78.87 A O ANISOU 982 O LEU A 104 10081 13635 6250 606 717 221 A O ATOM 983 CB LEU A 104 -4.525 -1.739 58.959 1.00 91.59 A C ANISOU 983 CB LEU A 104 12038 15882 6881 708 947 16 A C ATOM 984 CG LEU A 104 -4.717 -0.492 58.092 1.00 87.52 A C ANISOU 984 CG LEU A 104 11379 15192 6682 701 870 -342 A C ATOM 985 CD1 LEU A 104 -5.473 0.576 58.871 1.00 96.34 A C ANISOU 985 CD1 LEU A 104 12546 16464 7593 751 1038 -665 A C ATOM 986 CD2 LEU A 104 -3.388 0.064 57.604 1.00100.23 A C ANISOU 986 CD2 LEU A 104 12989 16723 8373 689 515 -467 A C ATOM 987 N ILE A 105 -2.433 -3.545 57.179 1.00 79.58 A N ANISOU 987 N ILE A 105 10405 13987 5845 702 456 518 A N ATOM 988 CA ILE A 105 -1.524 -3.665 56.043 1.00 71.70 A C ANISOU 988 CA ILE A 105 9277 12793 5173 690 219 525 A C ATOM 989 C ILE A 105 -2.034 -4.704 55.053 1.00 62.39 A C ANISOU 989 C ILE A 105 8011 11349 4346 643 350 756 A C ATOM 990 O ILE A 105 -1.795 -4.589 53.851 1.00 60.18 A O ANISOU 990 O ILE A 105 7593 10859 4413 602 256 686 A O ATOM 991 CB ILE A 105 -0.105 -4.032 56.513 1.00 74.42 A C ANISOU 991 CB ILE A 105 9681 13293 5302 783 -76 627 A C ATOM 992 CG1 ILE A 105 0.542 -2.931 57.353 1.00 84.58 A C ANISOU 992 CG1 ILE A 105 11016 14842 6278 802 -262 337 A C ATOM 993 CG2 ILE A 105 0.820 -4.261 55.320 1.00 71.14 A C ANISOU 993 CG2 ILE A 105 9103 12688 5237 769 -278 638 A C ATOM 994 CD1 ILE A 105 0.288 -1.560 56.865 1.00 84.68 A C ANISOU 994 CD1 ILE A 105 10946 14764 6464 702 -253 -38 A C ATOM 995 N ARG A 106 -2.713 -5.742 55.536 1.00 63.11 A N ANISOU 995 N ARG A 106 8196 11438 4344 634 574 1029 A N ATOM 996 CA ARG A 106 -3.086 -6.867 54.675 1.00 65.08 A C ANISOU 996 CA ARG A 106 8386 11426 4915 574 684 1256 A C ATOM 997 C ARG A 106 -3.816 -6.430 53.412 1.00 59.66 A C ANISOU 997 C ARG A 106 7490 10536 4641 482 745 1061 A C ATOM 998 O ARG A 106 -3.364 -6.785 52.311 1.00 57.46 A O ANISOU 998 O ARG A 106 7125 10052 4657 470 617 1091 A O ATOM 999 CB ARG A 106 -3.900 -7.853 55.531 1.00 70.70 A C ANISOU 999 CB ARG A 106 9252 12173 5440 531 979 1534 A C ATOM 1000 CG ARG A 106 -5.013 -8.614 54.814 1.00 94.02 A C ANISOU 1000 CG ARG A 106 12097 14895 8731 382 1245 1629 A C ATOM 1001 CD ARG A 106 -4.475 -9.817 54.052 1.00 96.59 A C ANISOU 1001 CD ARG A 106 12452 14948 9301 382 1159 1876 A C ATOM 1002 NE ARG A 106 -4.294 -10.970 54.928 1.00103.01 A N ANISOU 1002 NE ARG A 106 13527 15740 9873 414 1265 2243 A N ATOM 1003 CZ ARG A 106 -5.286 -11.659 55.475 1.00 99.33 A C ANISOU 1003 CZ ARG A 106 13166 15237 9338 278 1608 2427 A C ATOM 1004 NH1 ARG A 106 -6.551 -11.343 55.254 1.00 96.56 A N ANISOU 1004 NH1 ARG A 106 12632 14899 9158 102 1877 2256 A N ATOM 1005 NH2 ARG A 106 -5.001 -12.688 56.269 1.00104.54 A N ANISOU 1005 NH2 ARG A 106 14123 15848 9751 323 1686 2791 A N ATOM 1006 N PRO A 107 -4.911 -5.668 53.475 1.00 59.19 A N ANISOU 1006 N PRO A 107 7343 10530 4616 436 921 851 A N ATOM 1007 CA PRO A 107 -5.587 -5.285 52.221 1.00 60.30 A C ANISOU 1007 CA PRO A 107 7289 10480 5141 389 934 676 A C ATOM 1008 C PRO A 107 -4.743 -4.389 51.328 1.00 58.57 A C ANISOU 1008 C PRO A 107 7032 10157 5065 430 665 484 A C ATOM 1009 O PRO A 107 -4.820 -4.501 50.095 1.00 54.64 A O ANISOU 1009 O PRO A 107 6432 9453 4877 401 602 458 A O ATOM 1010 CB PRO A 107 -6.861 -4.576 52.713 1.00 57.55 A C ANISOU 1010 CB PRO A 107 6861 10266 4739 384 1162 477 A C ATOM 1011 CG PRO A 107 -6.521 -4.109 54.104 1.00 67.24 A C ANISOU 1011 CG PRO A 107 8260 11753 5536 443 1187 443 A C ATOM 1012 CD PRO A 107 -5.628 -5.178 54.666 1.00 69.16 A C ANISOU 1012 CD PRO A 107 8676 12033 5568 446 1123 762 A C ATOM 1013 N ILE A 108 -3.924 -3.509 51.905 1.00 53.93 A N ANISOU 1013 N ILE A 108 6534 9705 4252 482 512 342 A N ATOM 1014 CA ILE A 108 -3.062 -2.676 51.072 1.00 54.23 A C ANISOU 1014 CA ILE A 108 6548 9629 4429 478 287 166 A C ATOM 1015 C ILE A 108 -2.039 -3.542 50.340 1.00 52.60 A C ANISOU 1015 C ILE A 108 6310 9307 4370 461 138 345 A C ATOM 1016 O ILE A 108 -1.753 -3.321 49.155 1.00 52.09 A O ANISOU 1016 O ILE A 108 6178 9057 4556 425 51 276 A O ATOM 1017 CB ILE A 108 -2.388 -1.585 51.927 1.00 63.48 A C ANISOU 1017 CB ILE A 108 7815 10974 5329 500 166 -46 A C ATOM 1018 CG1 ILE A 108 -3.435 -0.841 52.762 1.00 63.60 A C ANISOU 1018 CG1 ILE A 108 7877 11115 5174 540 342 -224 A C ATOM 1019 CG2 ILE A 108 -1.634 -0.596 51.027 1.00 61.28 A C ANISOU 1019 CG2 ILE A 108 7519 10542 5224 450 -14 -255 A C ATOM 1020 CD1 ILE A 108 -2.857 0.071 53.829 1.00 68.80 A C ANISOU 1020 CD1 ILE A 108 8659 11976 5505 561 250 -430 A C ATOM 1021 N LYS A 109 -1.489 -4.552 51.020 1.00 58.11 A N ANISOU 1021 N LYS A 109 7068 10107 4904 503 115 581 A N ATOM 1022 CA LYS A 109 -0.559 -5.475 50.374 1.00 54.73 A C ANISOU 1022 CA LYS A 109 6603 9567 4624 526 -13 752 A C ATOM 1023 C LYS A 109 -1.177 -6.125 49.148 1.00 53.08 A C ANISOU 1023 C LYS A 109 6314 9098 4758 470 85 822 A C ATOM 1024 O LYS A 109 -0.537 -6.235 48.097 1.00 52.04 A O ANISOU 1024 O LYS A 109 6114 8823 4837 458 -26 794 A O ATOM 1025 CB LYS A 109 -0.121 -6.565 51.348 1.00 58.99 A C ANISOU 1025 CB LYS A 109 7255 10225 4935 622 -27 1028 A C ATOM 1026 CG LYS A 109 1.346 -6.622 51.590 1.00 73.98 A C ANISOU 1026 CG LYS A 109 9139 12251 6717 719 -289 1039 A C ATOM 1027 CD LYS A 109 1.660 -7.487 52.811 1.00 72.23 A C ANISOU 1027 CD LYS A 109 9077 12196 6172 859 -323 1297 A C ATOM 1028 CE LYS A 109 1.587 -8.978 52.502 1.00 68.06 A C ANISOU 1028 CE LYS A 109 8618 11457 5785 924 -246 1623 A C ATOM 1029 NZ LYS A 109 1.983 -9.805 53.689 1.00 73.36 A N ANISOU 1029 NZ LYS A 109 9492 12264 6117 1092 -302 1904 A N ATOM 1030 N VAL A 110 -2.418 -6.599 49.279 1.00 55.25 A N ANISOU 1030 N VAL A 110 6588 9322 5083 426 302 902 A N ATOM 1031 CA VAL A 110 -3.075 -7.296 48.175 1.00 52.42 A C ANISOU 1031 CA VAL A 110 6141 8734 5041 358 389 951 A C ATOM 1032 C VAL A 110 -3.264 -6.370 46.986 1.00 48.50 A C ANISOU 1032 C VAL A 110 5545 8126 4755 334 305 713 A C ATOM 1033 O VAL A 110 -3.012 -6.752 45.834 1.00 52.23 A O ANISOU 1033 O VAL A 110 5971 8421 5452 311 238 718 A O ATOM 1034 CB VAL A 110 -4.417 -7.881 48.644 1.00 55.65 A C ANISOU 1034 CB VAL A 110 6535 9148 5461 282 651 1041 A C ATOM 1035 CG1 VAL A 110 -5.045 -8.709 47.536 1.00 58.43 A C ANISOU 1035 CG1 VAL A 110 6785 9271 6145 191 723 1076 A C ATOM 1036 CG2 VAL A 110 -4.211 -8.732 49.872 1.00 61.67 A C ANISOU 1036 CG2 VAL A 110 7459 10009 5966 303 753 1302 A C ATOM 1037 N ALEU A 111 -3.722 -5.143 47.242 0.73 54.00 A N ANISOU 1037 N ALEU A 111 6234 8915 5368 351 312 502 A N ATOM 1038 N BLEU A 111 -3.708 -5.140 47.228 0.27 53.90 A N ANISOU 1038 N BLEU A 111 6222 8901 5357 351 309 501 A N ATOM 1039 CA ALEU A 111 -3.926 -4.187 46.160 0.73 51.55 A C ANISOU 1039 CA ALEU A 111 5882 8477 5228 355 227 295 A C ATOM 1040 CA BLEU A 111 -3.918 -4.235 46.106 0.27 51.66 A C ANISOU 1040 CA BLEU A 111 5893 8481 5253 353 225 301 A C ATOM 1041 C ALEU A 111 -2.606 -3.853 45.481 0.73 52.39 A C ANISOU 1041 C ALEU A 111 6035 8503 5367 341 45 259 A C ATOM 1042 C BLEU A 111 -2.596 -3.838 45.464 0.27 52.33 A C ANISOU 1042 C BLEU A 111 6028 8493 5361 341 43 256 A C ATOM 1043 O ALEU A 111 -2.509 -3.857 44.250 0.73 50.53 A O ANISOU 1043 O ALEU A 111 5778 8097 5324 318 -12 226 A O ATOM 1044 O BLEU A 111 -2.493 -3.781 44.234 0.27 50.66 A O ANISOU 1044 O BLEU A 111 5798 8111 5338 319 -17 215 A O ATOM 1045 CB ALEU A 111 -4.579 -2.912 46.697 0.73 54.14 A C ANISOU 1045 CB ALEU A 111 6229 8898 5442 406 266 78 A C ATOM 1046 CB BLEU A 111 -4.677 -2.998 46.557 0.27 54.10 A C ANISOU 1046 CB BLEU A 111 6210 8872 5472 403 272 86 A C ATOM 1047 CG ALEU A 111 -6.097 -2.776 46.608 0.73 58.23 A C ANISOU 1047 CG ALEU A 111 6632 9423 6069 440 413 -15 A C ATOM 1048 CG BLEU A 111 -6.119 -3.253 46.972 0.27 56.32 A C ANISOU 1048 CG BLEU A 111 6384 9232 5784 415 472 70 A C ATOM 1049 CD1ALEU A 111 -6.607 -3.033 45.193 0.73 59.51 A C ANISOU 1049 CD1ALEU A 111 6696 9398 6517 435 359 -38 A C ATOM 1050 CD1BLEU A 111 -6.643 -1.957 47.489 0.27 60.71 A C ANISOU 1050 CD1BLEU A 111 6960 9878 6229 502 499 -165 A C ATOM 1051 CD2ALEU A 111 -6.778 -3.698 47.616 0.73 59.40 A C ANISOU 1051 CD2ALEU A 111 6726 9725 6120 395 630 127 A C ATOM 1052 CD2BLEU A 111 -6.984 -3.759 45.836 0.27 55.59 A C ANISOU 1052 CD2BLEU A 111 6148 8995 5980 391 496 66 A C ATOM 1053 N LEU A 112 -1.576 -3.552 46.276 1.00 49.85 A N ANISOU 1053 N LEU A 112 5769 8323 4849 348 -44 250 A N ATOM 1054 CA LEU A 112 -0.292 -3.167 45.704 1.00 49.76 A C ANISOU 1054 CA LEU A 112 5760 8271 4876 308 -197 182 A C ATOM 1055 C LEU A 112 0.266 -4.285 44.834 1.00 50.48 A C ANISOU 1055 C LEU A 112 5789 8249 5143 305 -225 334 A C ATOM 1056 O LEU A 112 0.796 -4.032 43.741 1.00 50.24 A O ANISOU 1056 O LEU A 112 5742 8091 5256 256 -280 262 A O ATOM 1057 CB LEU A 112 0.686 -2.788 46.812 1.00 47.50 A C ANISOU 1057 CB LEU A 112 5498 8201 4349 314 -300 132 A C ATOM 1058 CG LEU A 112 2.065 -2.316 46.357 1.00 55.55 A C ANISOU 1058 CG LEU A 112 6472 9225 5408 242 -448 21 A C ATOM 1059 CD1 LEU A 112 1.901 -1.063 45.537 1.00 59.32 A C ANISOU 1059 CD1 LEU A 112 7015 9532 5992 147 -437 -187 A C ATOM 1060 CD2 LEU A 112 2.947 -2.045 47.559 1.00 58.02 A C ANISOU 1060 CD2 LEU A 112 6774 9796 5475 253 -573 -44 A C ATOM 1061 N GLN A 113 0.130 -5.533 45.285 1.00 48.50 A N ANISOU 1061 N GLN A 113 5525 8023 4878 357 -170 545 A N ATOM 1062 CA GLN A 113 0.623 -6.650 44.490 1.00 48.97 A C ANISOU 1062 CA GLN A 113 5543 7946 5115 374 -189 678 A C ATOM 1063 C GLN A 113 -0.177 -6.800 43.204 1.00 51.99 A C ANISOU 1063 C GLN A 113 5903 8119 5734 319 -123 629 A C ATOM 1064 O GLN A 113 0.402 -7.036 42.137 1.00 52.12 A O ANISOU 1064 O GLN A 113 5893 8014 5895 304 -172 602 A O ATOM 1065 CB GLN A 113 0.569 -7.943 45.298 1.00 57.07 A C ANISOU 1065 CB GLN A 113 6612 8998 6075 448 -133 926 A C ATOM 1066 CG GLN A 113 0.799 -9.192 44.465 1.00 67.69 A C ANISOU 1066 CG GLN A 113 7941 10142 7635 472 -116 1058 A C ATOM 1067 CD GLN A 113 1.577 -10.251 45.210 1.00 86.32 A C ANISOU 1067 CD GLN A 113 10357 12536 9905 604 -165 1280 A C ATOM 1068 NE2 GLN A 113 1.174 -10.524 46.445 1.00 84.88 A N ANISOU 1068 NE2 GLN A 113 10283 12458 9507 642 -101 1437 A N ATOM 1069 OE1 GLN A 113 2.534 -10.816 44.684 1.00103.11 A O ANISOU 1069 OE1 GLN A 113 12439 14596 12141 687 -256 1311 A O ATOM 1070 N THR A 114 -1.505 -6.655 43.288 1.00 49.00 A N ANISOU 1070 N THR A 114 5519 7716 5384 293 -15 597 A N ATOM 1071 CA THR A 114 -2.356 -6.792 42.109 1.00 50.72 A C ANISOU 1071 CA THR A 114 5693 7768 5811 255 16 529 A C ATOM 1072 C THR A 114 -2.064 -5.692 41.093 1.00 48.57 A C ANISOU 1072 C THR A 114 5456 7423 5574 250 -87 353 A C ATOM 1073 O THR A 114 -1.955 -5.957 39.889 1.00 46.72 A O ANISOU 1073 O THR A 114 5226 7048 5479 230 -124 327 A O ATOM 1074 CB THR A 114 -3.829 -6.759 42.534 1.00 50.94 A C ANISOU 1074 CB THR A 114 5660 7837 5856 238 143 498 A C ATOM 1075 CG2 THR A 114 -4.762 -6.774 41.334 1.00 50.17 A C ANISOU 1075 CG2 THR A 114 5485 7612 5965 216 132 385 A C ATOM 1076 OG1 THR A 114 -4.128 -7.899 43.353 1.00 52.71 A O ANISOU 1076 OG1 THR A 114 5878 8089 6061 204 279 685 A O ATOM 1077 N ALEU A 115 -1.926 -4.450 41.562 0.60 47.80 A N ANISOU 1077 N ALEU A 115 5414 7406 5342 262 -125 231 A N ATOM 1078 N BLEU A 115 -1.924 -4.453 41.568 0.41 47.89 A N ANISOU 1078 N BLEU A 115 5425 7418 5352 262 -125 232 A N ATOM 1079 CA ALEU A 115 -1.626 -3.344 40.658 0.60 48.43 A C ANISOU 1079 CA ALEU A 115 5581 7380 5442 244 -202 85 A C ATOM 1080 CA BLEU A 115 -1.628 -3.333 40.680 0.41 48.45 A C ANISOU 1080 CA BLEU A 115 5583 7384 5440 245 -202 84 A C ATOM 1081 C ALEU A 115 -0.238 -3.482 40.045 0.60 49.08 A C ANISOU 1081 C ALEU A 115 5680 7421 5546 180 -258 102 A C ATOM 1082 C BLEU A 115 -0.242 -3.464 40.059 0.41 49.05 A C ANISOU 1082 C BLEU A 115 5678 7418 5540 180 -258 100 A C ATOM 1083 O ALEU A 115 -0.035 -3.159 38.867 0.60 45.45 A O ANISOU 1083 O ALEU A 115 5288 6823 5159 145 -282 45 A O ATOM 1084 O BLEU A 115 -0.048 -3.130 38.882 0.41 45.50 A O ANISOU 1084 O BLEU A 115 5295 6829 5163 145 -282 43 A O ATOM 1085 CB ALEU A 115 -1.735 -2.018 41.405 0.60 48.76 A C ANISOU 1085 CB ALEU A 115 5700 7486 5339 261 -216 -55 A C ATOM 1086 CB BLEU A 115 -1.739 -2.026 41.462 0.41 48.82 A C ANISOU 1086 CB BLEU A 115 5706 7502 5342 262 -214 -53 A C ATOM 1087 CG ALEU A 115 -3.100 -1.341 41.363 0.60 55.52 A C ANISOU 1087 CG ALEU A 115 6572 8302 6220 351 -186 -164 A C ATOM 1088 CG BLEU A 115 -2.002 -0.736 40.691 0.41 48.95 A C ANISOU 1088 CG BLEU A 115 5857 7362 5379 278 -261 -208 A C ATOM 1089 CD1ALEU A 115 -3.226 -0.321 42.477 0.60 58.56 A C ANISOU 1089 CD1ALEU A 115 7016 8789 6444 386 -165 -289 A C ATOM 1090 CD1BLEU A 115 -3.387 -0.732 40.075 0.41 54.41 A C ANISOU 1090 CD1BLEU A 115 6525 7972 6178 384 -255 -241 A C ATOM 1091 CD2ALEU A 115 -3.315 -0.681 40.012 0.60 54.44 A C ANISOU 1091 CD2ALEU A 115 6539 7964 6180 379 -260 -244 A C ATOM 1092 CD2BLEU A 115 -1.827 0.449 41.627 0.41 52.19 A C ANISOU 1092 CD2BLEU A 115 6359 7828 5642 277 -267 -348 A C ATOM 1093 N THR A 116 0.737 -3.931 40.835 1.00 45.11 A N ANISOU 1093 N THR A 116 5117 7054 4968 173 -279 172 A N ATOM 1094 CA THR A 116 2.095 -4.048 40.314 1.00 44.42 A C ANISOU 1094 CA THR A 116 4992 6968 4917 120 -326 157 A C ATOM 1095 C THR A 116 2.166 -5.120 39.234 1.00 44.87 A C ANISOU 1095 C THR A 116 5015 6896 5138 139 -296 237 A C ATOM 1096 O THR A 116 2.804 -4.921 38.190 1.00 45.87 A O ANISOU 1096 O THR A 116 5159 6942 5329 80 -293 170 A O ATOM 1097 CB THR A 116 3.071 -4.349 41.444 1.00 51.47 A C ANISOU 1097 CB THR A 116 5795 8066 5695 150 -389 203 A C ATOM 1098 CG2 THR A 116 4.500 -4.430 40.905 1.00 51.32 A C ANISOU 1098 CG2 THR A 116 5677 8085 5738 101 -439 151 A C ATOM 1099 OG1 THR A 116 3.018 -3.300 42.418 1.00 49.04 A O ANISOU 1099 OG1 THR A 116 5532 7884 5217 120 -424 91 A O ATOM 1100 N GLU A 117 1.523 -6.263 39.475 1.00 45.17 A N ANISOU 1100 N GLU A 117 5017 6905 5238 206 -256 370 A N ATOM 1101 CA GLU A 117 1.532 -7.338 38.488 1.00 50.79 A C ANISOU 1101 CA GLU A 117 5711 7473 6114 220 -225 423 A C ATOM 1102 C GLU A 117 0.944 -6.852 37.171 1.00 48.55 A C ANISOU 1102 C GLU A 117 5499 7048 5899 170 -221 307 A C ATOM 1103 O GLU A 117 1.493 -7.115 36.098 1.00 46.44 A O ANISOU 1103 O GLU A 117 5250 6693 5701 150 -217 267 A O ATOM 1104 CB GLU A 117 0.738 -8.541 38.999 1.00 53.68 A C ANISOU 1104 CB GLU A 117 6059 7791 6545 263 -162 571 A C ATOM 1105 CG GLU A 117 1.290 -9.172 40.273 1.00 89.20 A C ANISOU 1105 CG GLU A 117 10542 12403 10948 341 -168 731 A C ATOM 1106 CD GLU A 117 1.579 -10.656 40.122 1.00125.16 A C ANISOU 1106 CD GLU A 117 15101 16825 15629 410 -136 881 A C ATOM 1107 OE1 GLU A 117 0.906 -11.313 39.302 1.00130.15 A O ANISOU 1107 OE1 GLU A 117 15750 17274 16426 364 -71 871 A O ATOM 1108 OE2 GLU A 117 2.486 -11.164 40.819 1.00120.02 A O ANISOU 1108 OE2 GLU A 117 14440 16247 14913 521 -188 998 A O ATOM 1109 N SER A 118 -0.170 -6.128 37.246 1.00 41.89 A N ANISOU 1109 N SER A 118 4700 6193 5022 170 -227 246 A N ATOM 1110 CA SER A 118 -0.810 -5.605 36.043 1.00 41.87 A C ANISOU 1110 CA SER A 118 4783 6070 5057 165 -261 143 A C ATOM 1111 C SER A 118 0.072 -4.570 35.358 1.00 43.91 A C ANISOU 1111 C SER A 118 5166 6283 5234 114 -284 62 A C ATOM 1112 O SER A 118 0.277 -4.618 34.138 1.00 42.88 A O ANISOU 1112 O SER A 118 5119 6048 5127 91 -287 26 A O ATOM 1113 CB SER A 118 -2.162 -5.006 36.427 1.00 43.60 A C ANISOU 1113 CB SER A 118 4994 6314 5258 217 -276 87 A C ATOM 1114 OG SER A 118 -2.848 -4.528 35.284 1.00 45.79 A O ANISOU 1114 OG SER A 118 5349 6486 5561 255 -346 -9 A O ATOM 1115 N HIS A 119 0.619 -3.636 36.139 1.00 45.53 A N ANISOU 1115 N HIS A 119 5398 6565 5336 78 -287 27 A N ATOM 1116 CA HIS A 119 1.506 -2.615 35.596 1.00 42.09 A C ANISOU 1116 CA HIS A 119 5083 6073 4835 -19 -279 -54 A C ATOM 1117 C HIS A 119 2.662 -3.240 34.829 1.00 43.77 A C ANISOU 1117 C HIS A 119 5246 6284 5100 -89 -229 -42 A C ATOM 1118 O HIS A 119 3.002 -2.798 33.724 1.00 43.76 A O ANISOU 1118 O HIS A 119 5375 6174 5079 -159 -188 -89 A O ATOM 1119 CB HIS A 119 2.034 -1.739 36.735 1.00 43.23 A C ANISOU 1119 CB HIS A 119 5217 6324 4882 -74 -289 -113 A C ATOM 1120 CG HIS A 119 2.670 -0.461 36.277 1.00 42.08 A C ANISOU 1120 CG HIS A 119 5232 6078 4679 -202 -266 -220 A C ATOM 1121 CD2 HIS A 119 2.212 0.812 36.294 1.00 45.76 A C ANISOU 1121 CD2 HIS A 119 5893 6418 5078 -213 -276 -303 A C ATOM 1122 ND1 HIS A 119 3.937 -0.405 35.737 1.00 42.49 A N ANISOU 1122 ND1 HIS A 119 5260 6136 4747 -347 -207 -254 A N ATOM 1123 CE1 HIS A 119 4.233 0.849 35.445 1.00 47.27 A C ANISOU 1123 CE1 HIS A 119 6048 6617 5296 -476 -168 -346 A C ATOM 1124 NE2 HIS A 119 3.204 1.608 35.775 1.00 46.65 A N ANISOU 1124 NE2 HIS A 119 6123 6438 5165 -388 -217 -371 A N ATOM 1125 N ARG A 120 3.283 -4.275 35.401 1.00 40.75 A N ANISOU 1125 N ARG A 120 4688 6020 4776 -57 -223 23 A N ATOM 1126 CA ARG A 120 4.486 -4.838 34.797 1.00 43.59 A C ANISOU 1126 CA ARG A 120 4960 6405 5197 -96 -173 9 A C ATOM 1127 C ARG A 120 4.176 -5.554 33.488 1.00 43.53 A C ANISOU 1127 C ARG A 120 5018 6258 5263 -70 -129 11 A C ATOM 1128 O ARG A 120 5.045 -5.633 32.613 1.00 47.94 A O ANISOU 1128 O ARG A 120 5577 6801 5837 -128 -54 -46 A O ATOM 1129 CB ARG A 120 5.176 -5.781 35.787 1.00 45.69 A C ANISOU 1129 CB ARG A 120 5031 6824 5504 -11 -208 83 A C ATOM 1130 CG ARG A 120 5.587 -5.081 37.074 1.00 49.87 A C ANISOU 1130 CG ARG A 120 5495 7529 5925 -35 -274 58 A C ATOM 1131 CD ARG A 120 7.099 -5.030 37.267 1.00 48.75 A C ANISOU 1131 CD ARG A 120 5176 7554 5794 -81 -292 -19 A C ATOM 1132 NE ARG A 120 7.753 -4.011 36.450 1.00 48.31 A N ANISOU 1132 NE ARG A 120 5157 7463 5738 -270 -214 -168 A N ATOM 1133 CZ ARG A 120 9.063 -3.796 36.423 1.00 49.98 A C ANISOU 1133 CZ ARG A 120 5193 7818 5980 -368 -194 -281 A C ATOM 1134 NH1 ARG A 120 9.902 -4.479 37.199 1.00 49.95 A N ANISOU 1134 NH1 ARG A 120 4947 8027 6005 -262 -286 -275 A N ATOM 1135 NH2 ARG A 120 9.548 -2.861 35.610 1.00 51.89 A N ANISOU 1135 NH2 ARG A 120 5503 7992 6222 -578 -78 -405 A N ATOM 1136 N ILE A 121 2.950 -6.053 33.330 1.00 40.96 A N ANISOU 1136 N ILE A 121 4740 5845 4978 6 -167 53 A N ATOM 1137 CA ILE A 121 2.515 -6.625 32.059 1.00 41.62 A C ANISOU 1137 CA ILE A 121 4903 5801 5110 22 -153 19 A C ATOM 1138 C ILE A 121 2.270 -5.521 31.036 1.00 44.03 A C ANISOU 1138 C ILE A 121 5415 6019 5295 -30 -161 -55 A C ATOM 1139 O ILE A 121 2.728 -5.600 29.891 1.00 45.89 A O ANISOU 1139 O ILE A 121 5747 6195 5493 -70 -105 -104 A O ATOM 1140 CB ILE A 121 1.255 -7.482 32.263 1.00 45.09 A C ANISOU 1140 CB ILE A 121 5299 6188 5643 91 -200 60 A C ATOM 1141 CG1 ILE A 121 1.626 -8.806 32.934 1.00 44.69 A C ANISOU 1141 CG1 ILE A 121 5114 6151 5716 138 -162 154 A C ATOM 1142 CG2 ILE A 121 0.537 -7.732 30.934 1.00 46.28 A C ANISOU 1142 CG2 ILE A 121 5551 6223 5809 97 -234 -22 A C ATOM 1143 CD1 ILE A 121 0.446 -9.448 33.659 1.00 51.14 A C ANISOU 1143 CD1 ILE A 121 5879 6943 6610 161 -170 227 A C ATOM 1144 N LEU A 122 1.552 -4.470 31.438 1.00 40.12 A N ANISOU 1144 N LEU A 122 5011 5509 4722 -17 -222 -62 A N ATOM 1145 CA LEU A 122 1.255 -3.375 30.519 1.00 43.24 A C ANISOU 1145 CA LEU A 122 5649 5788 4993 -31 -246 -108 A C ATOM 1146 C LEU A 122 2.528 -2.696 30.016 1.00 42.21 A C ANISOU 1146 C LEU A 122 5634 5627 4776 -176 -129 -132 A C ATOM 1147 O LEU A 122 2.551 -2.185 28.891 1.00 43.06 A O ANISOU 1147 O LEU A 122 5970 5618 4771 -208 -100 -147 A O ATOM 1148 CB LEU A 122 0.342 -2.349 31.196 1.00 43.94 A C ANISOU 1148 CB LEU A 122 5807 5855 5034 38 -329 -119 A C ATOM 1149 CG LEU A 122 -1.084 -2.783 31.547 1.00 50.35 A C ANISOU 1149 CG LEU A 122 6510 6701 5920 174 -428 -125 A C ATOM 1150 CD1 LEU A 122 -1.801 -1.617 32.240 1.00 54.49 A C ANISOU 1150 CD1 LEU A 122 7100 7214 6390 253 -482 -162 A C ATOM 1151 CD2 LEU A 122 -1.836 -3.254 30.324 1.00 49.23 A C ANISOU 1151 CD2 LEU A 122 6428 6492 5786 244 -510 -161 A C ATOM 1152 N GLU A 123 3.594 -2.676 30.823 1.00 40.16 A N ANISOU 1152 N GLU A 123 5219 5481 4558 -270 -59 -141 A N ATOM 1153 CA GLU A 123 4.828 -2.051 30.360 1.00 42.05 A C ANISOU 1153 CA GLU A 123 5517 5715 4744 -445 74 -193 A C ATOM 1154 C GLU A 123 5.319 -2.676 29.063 1.00 41.87 A C ANISOU 1154 C GLU A 123 5540 5660 4707 -475 180 -211 A C ATOM 1155 O GLU A 123 5.920 -1.987 28.232 1.00 43.43 A O ANISOU 1155 O GLU A 123 5910 5788 4804 -616 308 -242 A O ATOM 1156 CB GLU A 123 5.930 -2.176 31.411 1.00 44.13 A C ANISOU 1156 CB GLU A 123 5526 6159 5081 -523 106 -230 A C ATOM 1157 CG GLU A 123 5.713 -1.399 32.691 1.00 45.02 A C ANISOU 1157 CG GLU A 123 5613 6326 5166 -535 25 -248 A C ATOM 1158 CD GLU A 123 6.611 -1.912 33.793 1.00 47.49 A C ANISOU 1158 CD GLU A 123 5640 6864 5541 -539 -5 -270 A C ATOM 1159 OE1 GLU A 123 7.759 -2.291 33.473 1.00 47.64 A O ANISOU 1159 OE1 GLU A 123 5501 6981 5618 -613 71 -319 A O ATOM 1160 OE2 GLU A 123 6.179 -1.955 34.971 1.00 43.36 A O ANISOU 1160 OE2 GLU A 123 5045 6433 4997 -454 -106 -243 A O ATOM 1161 N LYS A 124 5.110 -3.983 28.893 1.00 41.07 A N ANISOU 1161 N LYS A 124 5301 5601 4702 -358 149 -199 A N ATOM 1162 CA ALYS A 124 5.628 -4.672 27.719 0.60 47.44 A C ANISOU 1162 CA ALYS A 124 6136 6391 5500 -374 258 -247 A C ATOM 1163 CA BLYS A 124 5.624 -4.675 27.720 0.40 47.43 A C ANISOU 1163 CA BLYS A 124 6134 6389 5499 -373 258 -247 A C ATOM 1164 C LYS A 124 4.819 -4.355 26.466 1.00 40.80 A C ANISOU 1164 C LYS A 124 5592 5406 4503 -350 232 -252 A C ATOM 1165 O LYS A 124 5.302 -4.600 25.352 1.00 42.88 A O ANISOU 1165 O LYS A 124 5959 5648 4684 -396 349 -303 A O ATOM 1166 CB ALYS A 124 5.635 -6.186 27.950 0.60 49.12 A C ANISOU 1166 CB ALYS A 124 6134 6654 5874 -246 229 -247 A C ATOM 1167 CB BLYS A 124 5.618 -6.190 27.947 0.40 49.15 A C ANISOU 1167 CB BLYS A 124 6140 6656 5878 -244 227 -246 A C ATOM 1168 CG ALYS A 124 6.579 -6.677 29.042 0.60 54.33 A C ANISOU 1168 CG ALYS A 124 6514 7461 6668 -222 245 -233 A C ATOM 1169 CG BLYS A 124 6.405 -6.681 29.159 0.40 54.54 A C ANISOU 1169 CG BLYS A 124 6546 7482 6697 -209 222 -220 A C ATOM 1170 CD ALYS A 124 8.022 -6.327 28.740 0.60 58.69 A C ANISOU 1170 CD ALYS A 124 6964 8124 7213 -344 398 -322 A C ATOM 1171 CD BLYS A 124 7.793 -6.070 29.232 0.40 57.56 A C ANISOU 1171 CD BLYS A 124 6816 7990 7064 -343 343 -291 A C ATOM 1172 CE ALYS A 124 8.980 -7.224 29.509 0.60 71.57 A C ANISOU 1172 CE ALYS A 124 8285 9910 8998 -247 392 -335 A C ATOM 1173 CE BLYS A 124 8.717 -6.835 30.185 0.40 69.69 A C ANISOU 1173 CE BLYS A 124 8043 9695 8739 -256 318 -292 A C ATOM 1174 NZ ALYS A 124 10.314 -6.585 29.657 0.60 69.50 A N ANISOU 1174 NZ ALYS A 124 7847 9819 8742 -386 495 -436 A N ATOM 1175 NZ BLYS A 124 8.035 -7.908 30.966 0.40 65.71 A N ANISOU 1175 NZ BLYS A 124 7473 9163 8329 -67 190 -182 A N ATOM 1176 N TYR A 125 3.602 -3.835 26.623 1.00 40.69 A N ANISOU 1176 N TYR A 125 5710 5313 4437 -262 77 -211 A N ATOM 1177 CA TYR A 125 2.759 -3.465 25.495 1.00 42.99 A C ANISOU 1177 CA TYR A 125 6283 5487 4565 -197 -1 -215 A C ATOM 1178 C TYR A 125 2.769 -1.970 25.225 1.00 44.38 A C ANISOU 1178 C TYR A 125 6759 5540 4562 -255 19 -169 A C ATOM 1179 O TYR A 125 2.065 -1.518 24.317 1.00 47.43 A O ANISOU 1179 O TYR A 125 7423 5818 4781 -170 -69 -150 A O ATOM 1180 CB TYR A 125 1.317 -3.923 25.735 1.00 42.47 A C ANISOU 1180 CB TYR A 125 6147 5419 4570 -31 -206 -223 A C ATOM 1181 CG TYR A 125 1.148 -5.413 25.689 1.00 39.41 A C ANISOU 1181 CG TYR A 125 5553 5085 4337 11 -221 -273 A C ATOM 1182 CD1 TYR A 125 1.106 -6.091 24.487 1.00 38.62 A C ANISOU 1182 CD1 TYR A 125 5548 4952 4173 27 -219 -351 A C ATOM 1183 CD2 TYR A 125 1.079 -6.157 26.865 1.00 45.67 A C ANISOU 1183 CD2 TYR A 125 6082 5946 5327 27 -225 -241 A C ATOM 1184 CE1 TYR A 125 0.967 -7.452 24.443 1.00 39.88 A C ANISOU 1184 CE1 TYR A 125 5542 5122 4489 54 -223 -416 A C ATOM 1185 CE2 TYR A 125 0.938 -7.519 26.829 1.00 48.74 A C ANISOU 1185 CE2 TYR A 125 6324 6332 5864 57 -222 -273 A C ATOM 1186 CZ TYR A 125 0.882 -8.163 25.617 1.00 47.28 A C ANISOU 1186 CZ TYR A 125 6232 6090 5641 66 -221 -369 A C ATOM 1187 OH TYR A 125 0.741 -9.521 25.577 1.00 45.21 A O ANISOU 1187 OH TYR A 125 5845 5788 5543 86 -212 -420 A O ATOM 1188 N THR A 126 3.568 -1.208 25.962 1.00 44.55 A N ANISOU 1188 N THR A 126 6747 5568 4612 -395 125 -158 A N ATOM 1189 CA ATHR A 126 3.638 0.243 25.880 0.87 46.75 A C ANISOU 1189 CA ATHR A 126 7316 5689 4756 -479 165 -120 A C ATOM 1190 CA BTHR A 126 3.616 0.236 25.806 0.13 46.98 A C ANISOU 1190 CA BTHR A 126 7360 5714 4777 -476 164 -118 A C ATOM 1191 C THR A 126 5.007 0.677 25.371 1.00 49.36 A C ANISOU 1191 C THR A 126 7737 5999 5017 -733 416 -137 A C ATOM 1192 O THR A 126 6.020 0.075 25.730 1.00 51.11 A O ANISOU 1192 O THR A 126 7674 6382 5364 -848 538 -201 A O ATOM 1193 CB ATHR A 126 3.417 0.862 27.265 0.87 49.56 A C ANISOU 1193 CB ATHR A 126 7555 6061 5214 -471 92 -130 A C ATOM 1194 CB BTHR A 126 3.224 0.940 27.108 0.13 50.24 A C ANISOU 1194 CB BTHR A 126 7696 6118 5275 -444 72 -122 A C ATOM 1195 CG2ATHR A 126 3.319 2.369 27.161 0.87 52.24 A C ANISOU 1195 CG2ATHR A 126 8236 6185 5429 -528 114 -104 A C ATOM 1196 CG2BTHR A 126 1.737 0.750 27.381 0.13 52.22 A C ANISOU 1196 CG2BTHR A 126 7921 6364 5556 -196 -148 -110 A C ATOM 1197 OG1ATHR A 126 2.227 0.324 27.850 0.87 52.01 A O ANISOU 1197 OG1ATHR A 126 7714 6435 5612 -261 -95 -128 A O ATOM 1198 OG1BTHR A 126 3.979 0.390 28.193 0.13 51.20 A O ANISOU 1198 OG1BTHR A 126 7474 6423 5556 -528 123 -168 A O ATOM 1199 N GLN A 127 5.049 1.745 24.577 1.00 58.62 A N ANISOU 1199 N GLN A 127 9303 6974 5998 -818 500 -80 A N ATOM 1200 CA GLN A 127 6.343 2.257 24.133 1.00 59.10 A C ANISOU 1200 CA GLN A 127 9455 7003 5997 -1109 781 -99 A C ATOM 1201 C GLN A 127 7.088 2.903 25.300 1.00 59.18 A C ANISOU 1201 C GLN A 127 9279 7050 6155 -1303 852 -168 A C ATOM 1202 O GLN A 127 6.490 3.636 26.091 1.00 54.76 A O ANISOU 1202 O GLN A 127 8795 6388 5624 -1241 719 -156 A O ATOM 1203 CB GLN A 127 6.194 3.276 23.004 1.00 67.87 A C ANISOU 1203 CB GLN A 127 11090 7857 6842 -1171 876 5 A C ATOM 1204 CG GLN A 127 5.120 2.955 21.997 1.00 78.11 A C ANISOU 1204 CG GLN A 127 12645 9087 7947 -916 705 79 A C ATOM 1205 CD GLN A 127 4.324 4.161 21.599 1.00102.95 A C ANISOU 1205 CD GLN A 127 16273 11952 10891 -807 598 203 A C ATOM 1206 NE2 GLN A 127 3.166 3.914 21.003 1.00102.37 A N ANISOU 1206 NE2 GLN A 127 16353 11855 10689 -517 352 246 A N ATOM 1207 OE1 GLN A 127 4.743 5.304 21.786 1.00106.03 A O ANISOU 1207 OE1 GLN A 127 16906 12139 11241 -976 730 254 A O ATOM 1208 N PRO A 128 8.402 2.675 25.419 1.00 60.31 A N ANISOU 1208 N PRO A 128 9172 7350 6393 -1536 1058 -263 A N ATOM 1209 CA PRO A 128 9.134 3.230 26.569 1.00 63.92 A C ANISOU 1209 CA PRO A 128 9407 7886 6995 -1722 1092 -364 A C ATOM 1210 C PRO A 128 9.119 4.744 26.616 1.00 63.23 A C ANISOU 1210 C PRO A 128 9673 7530 6821 -1912 1168 -347 A C ATOM 1211 O PRO A 128 9.246 5.324 27.702 1.00 62.64 A O ANISOU 1211 O PRO A 128 9491 7464 6844 -1989 1105 -429 A O ATOM 1212 CB PRO A 128 10.562 2.692 26.370 1.00 77.22 A C ANISOU 1212 CB PRO A 128 10770 9794 8777 -1932 1314 -482 A C ATOM 1213 CG PRO A 128 10.422 1.571 25.391 1.00 62.78 A C ANISOU 1213 CG PRO A 128 8922 8036 6897 -1773 1345 -447 A C ATOM 1214 CD PRO A 128 9.314 1.983 24.491 1.00 73.92 A C ANISOU 1214 CD PRO A 128 10801 9196 8090 -1648 1278 -310 A C ATOM 1215 N SER A 129 8.979 5.402 25.462 1.00 49.00 A N ANISOU 1215 N SER A 129 5956 5976 6686 618 427 339 A N ATOM 1216 CA SER A 129 8.929 6.860 25.440 1.00 64.56 A C ANISOU 1216 CA SER A 129 7835 7955 8741 437 328 377 A C ATOM 1217 C SER A 129 7.768 7.400 26.267 1.00 60.01 A C ANISOU 1217 C SER A 129 7394 7330 8079 265 85 141 A C ATOM 1218 O SER A 129 7.854 8.506 26.816 1.00 56.43 A O ANISOU 1218 O SER A 129 6900 6854 7688 117 -109 154 A O ATOM 1219 CB SER A 129 8.825 7.345 23.994 1.00 66.51 A C ANISOU 1219 CB SER A 129 8188 8191 8892 586 526 423 A C ATOM 1220 OG SER A 129 7.563 7.026 23.448 1.00 63.54 A O ANISOU 1220 OG SER A 129 8143 7709 8290 648 498 151 A O ATOM 1221 N ILE A 130 6.667 6.654 26.355 1.00 53.90 A N ANISOU 1221 N ILE A 130 6795 6523 7162 313 69 -27 A N ATOM 1222 CA ILE A 130 5.562 7.076 27.208 1.00 55.51 A C ANISOU 1222 CA ILE A 130 7074 6738 7280 237 -89 -137 A C ATOM 1223 C ILE A 130 6.025 7.172 28.658 1.00 52.68 A C ANISOU 1223 C ILE A 130 6626 6431 6958 208 -238 -97 A C ATOM 1224 O ILE A 130 5.687 8.127 29.370 1.00 50.99 A O ANISOU 1224 O ILE A 130 6512 6212 6651 200 -397 -148 A O ATOM 1225 CB ILE A 130 4.372 6.111 27.063 1.00 55.37 A C ANISOU 1225 CB ILE A 130 7155 6683 7200 284 -96 -179 A C ATOM 1226 CG1 ILE A 130 3.762 6.152 25.658 1.00 66.12 A C ANISOU 1226 CG1 ILE A 130 8700 7924 8500 312 -62 -245 A C ATOM 1227 CG2 ILE A 130 3.275 6.447 28.069 1.00 58.58 A C ANISOU 1227 CG2 ILE A 130 7552 7169 7536 282 -187 -154 A C ATOM 1228 CD1 ILE A 130 3.441 7.538 25.140 1.00 67.44 A C ANISOU 1228 CD1 ILE A 130 8923 8102 8597 260 -41 -304 A C ATOM 1229 N PHE A 131 6.808 6.187 29.120 1.00 54.07 A N ANISOU 1229 N PHE A 131 6672 6637 7237 234 -211 -11 A N ATOM 1230 CA PHE A 131 7.207 6.163 30.526 1.00 55.37 A C ANISOU 1230 CA PHE A 131 6790 6832 7417 230 -377 19 A C ATOM 1231 C PHE A 131 8.102 7.342 30.877 1.00 56.07 A C ANISOU 1231 C PHE A 131 6867 6837 7600 122 -611 76 A C ATOM 1232 O PHE A 131 8.012 7.882 31.986 1.00 57.21 A O ANISOU 1232 O PHE A 131 7165 6928 7644 155 -867 20 A O ATOM 1233 CB PHE A 131 7.921 4.854 30.862 1.00 55.29 A C ANISOU 1233 CB PHE A 131 6627 6861 7518 267 -301 112 A C ATOM 1234 CG PHE A 131 7.030 3.661 30.830 1.00 51.78 A C ANISOU 1234 CG PHE A 131 6219 6438 7016 348 -211 84 A C ATOM 1235 CD1 PHE A 131 7.205 2.682 29.872 1.00 63.01 A C ANISOU 1235 CD1 PHE A 131 7663 7797 8479 405 -93 99 A C ATOM 1236 CD2 PHE A 131 6.025 3.510 31.770 1.00 66.86 A C ANISOU 1236 CD2 PHE A 131 8159 8413 8833 406 -274 93 A C ATOM 1237 CE1 PHE A 131 6.383 1.578 29.838 1.00 63.89 A C ANISOU 1237 CE1 PHE A 131 7841 7848 8587 441 -136 99 A C ATOM 1238 CE2 PHE A 131 5.206 2.407 31.745 1.00 68.46 A C ANISOU 1238 CE2 PHE A 131 8322 8616 9075 436 -249 173 A C ATOM 1239 CZ PHE A 131 5.387 1.439 30.778 1.00 69.24 A C ANISOU 1239 CZ PHE A 131 8456 8589 9264 415 -229 164 A C ATOM 1240 N LYS A 132 8.989 7.750 29.970 1.00 52.56 A N ANISOU 1240 N LYS A 132 6262 6359 7351 23 -566 231 A N ATOM 1241 CA LYS A 132 9.844 8.873 30.320 1.00 62.05 A C ANISOU 1241 CA LYS A 132 7407 7434 8737 -137 -890 372 A C ATOM 1242 C LYS A 132 9.021 10.141 30.483 1.00 61.57 A C ANISOU 1242 C LYS A 132 7639 7256 8499 -155 -1125 195 A C ATOM 1243 O LYS A 132 9.321 10.963 31.351 1.00 56.31 A O ANISOU 1243 O LYS A 132 7138 6415 7841 -212 -1545 186 A O ATOM 1244 CB LYS A 132 10.971 9.091 29.300 1.00 72.62 A C ANISOU 1244 CB LYS A 132 8420 8789 10383 -225 -774 712 A C ATOM 1245 CG LYS A 132 10.676 8.806 27.835 1.00 86.29 A C ANISOU 1245 CG LYS A 132 10121 10630 12034 -79 -362 737 A C ATOM 1246 CD LYS A 132 10.266 10.076 27.092 1.00 94.10 A C ANISOU 1246 CD LYS A 132 11188 11553 13013 -160 -422 722 A C ATOM 1247 CE LYS A 132 10.585 9.989 25.607 1.00 99.68 A C ANISOU 1247 CE LYS A 132 11764 12360 13750 -5 -50 930 A C ATOM 1248 NZ LYS A 132 10.026 11.128 24.826 1.00 99.87 A N ANISOU 1248 NZ LYS A 132 11890 12333 13724 -62 -71 879 A N ATOM 1249 N ILE A 133 7.957 10.302 29.693 1.00 50.50 A N ANISOU 1249 N ILE A 133 6356 5917 6914 -79 -903 50 A N ATOM 1250 CA ILE A 133 7.097 11.470 29.854 1.00 51.58 A C ANISOU 1250 CA ILE A 133 6785 5967 6848 -46 -1085 -110 A C ATOM 1251 C ILE A 133 6.417 11.431 31.219 1.00 50.02 A C ANISOU 1251 C ILE A 133 6872 5768 6365 161 -1240 -251 A C ATOM 1252 O ILE A 133 6.413 12.420 31.963 1.00 50.51 A O ANISOU 1252 O ILE A 133 7242 5668 6283 232 -1594 -327 A O ATOM 1253 CB ILE A 133 6.071 11.545 28.708 1.00 56.87 A C ANISOU 1253 CB ILE A 133 7490 6718 7398 -3 -799 -199 A C ATOM 1254 CG1 ILE A 133 6.788 11.697 27.363 1.00 54.46 A C ANISOU 1254 CG1 ILE A 133 6974 6410 7307 -114 -640 -43 A C ATOM 1255 CG2 ILE A 133 5.121 12.708 28.921 1.00 51.33 A C ANISOU 1255 CG2 ILE A 133 7085 5953 6465 69 -949 -345 A C ATOM 1256 CD1 ILE A 133 5.874 11.561 26.166 1.00 63.91 A C ANISOU 1256 CD1 ILE A 133 8248 7659 8374 -40 -373 -139 A C ATOM 1257 N ILE A 134 5.832 10.286 31.568 1.00 49.46 A N ANISOU 1257 N ILE A 134 6734 5862 6196 304 -997 -256 A N ATOM 1258 CA ILE A 134 5.159 10.162 32.859 1.00 53.37 A C ANISOU 1258 CA ILE A 134 7452 6414 6410 580 -1059 -298 A C ATOM 1259 C ILE A 134 6.131 10.467 33.990 1.00 54.35 A C ANISOU 1259 C ILE A 134 7749 6380 6522 614 -1439 -310 A C ATOM 1260 O ILE A 134 5.835 11.248 34.905 1.00 52.98 A O ANISOU 1260 O ILE A 134 7982 6098 6051 860 -1704 -404 A O ATOM 1261 CB ILE A 134 4.557 8.753 33.014 1.00 50.91 A C ANISOU 1261 CB ILE A 134 6934 6298 6113 672 -764 -197 A C ATOM 1262 CG1 ILE A 134 3.473 8.513 31.959 1.00 55.70 A C ANISOU 1262 CG1 ILE A 134 7437 6985 6741 635 -523 -161 A C ATOM 1263 CG2 ILE A 134 4.020 8.557 34.448 1.00 55.39 A C ANISOU 1263 CG2 ILE A 134 7670 6965 6411 1008 -789 -143 A C ATOM 1264 CD1 ILE A 134 2.999 7.073 31.898 1.00 51.20 A C ANISOU 1264 CD1 ILE A 134 6647 6512 6295 634 -356 -17 A C ATOM 1265 N SER A 135 7.314 9.860 33.937 1.00 51.70 A N ANISOU 1265 N SER A 135 7146 6004 6492 403 -1499 -198 A N ATOM 1266 CA SER A 135 8.256 9.981 35.043 1.00 58.04 A C ANISOU 1266 CA SER A 135 8078 6640 7336 404 -1899 -169 A C ATOM 1267 C SER A 135 8.685 11.423 35.275 1.00 58.18 A C ANISOU 1267 C SER A 135 8418 6339 7348 334 -2444 -210 A C ATOM 1268 O SER A 135 9.069 11.772 36.396 1.00 63.85 A O ANISOU 1268 O SER A 135 9479 6840 7940 452 -2902 -261 A O ATOM 1269 CB SER A 135 9.474 9.093 34.778 1.00 58.88 A C ANISOU 1269 CB SER A 135 7764 6777 7829 169 -1835 33 A C ATOM 1270 OG SER A 135 10.331 9.680 33.813 1.00 64.72 A O ANISOU 1270 OG SER A 135 8261 7420 8910 -104 -1922 219 A O ATOM 1271 N GLN A 136 8.603 12.270 34.250 1.00 58.97 A N ANISOU 1271 N GLN A 136 8462 6374 7569 161 -2452 -189 A N ATOM 1272 CA GLN A 136 8.990 13.671 34.357 1.00 65.88 A C ANISOU 1272 CA GLN A 136 9630 6908 8492 51 -3021 -195 A C ATOM 1273 C GLN A 136 7.876 14.549 34.907 1.00 68.07 A C ANISOU 1273 C GLN A 136 10514 7089 8260 409 -3177 -459 A C ATOM 1274 O GLN A 136 8.091 15.754 35.085 1.00 72.59 A O ANISOU 1274 O GLN A 136 11462 7322 8796 378 -3723 -513 A O ATOM 1275 CB GLN A 136 9.420 14.193 32.983 1.00 75.82 A C ANISOU 1275 CB GLN A 136 10525 8158 10124 -274 -2937 4 A C ATOM 1276 CG GLN A 136 10.759 13.652 32.508 1.00 82.20 A C ANISOU 1276 CG GLN A 136 10780 8999 11451 -567 -2900 381 A C ATOM 1277 CD GLN A 136 11.116 14.127 31.112 1.00103.39 A C ANISOU 1277 CD GLN A 136 13094 11736 14452 -774 -2712 647 A C ATOM 1278 NE2 GLN A 136 12.390 14.015 30.757 1.00133.09 A N ANISOU 1278 NE2 GLN A 136 16385 15482 18701 -999 -2783 1102 A N ATOM 1279 OE1 GLN A 136 10.254 14.581 30.357 1.00 93.15 A O ANISOU 1279 OE1 GLN A 136 11915 10511 12966 -703 -2485 491 A O ATOM 1280 N GLY A 137 6.699 13.984 35.165 1.00 66.85 A N ANISOU 1280 N GLY A 137 10458 7213 7730 763 -2729 -573 A N ATOM 1281 CA GLY A 137 5.594 14.721 35.739 1.00 63.49 A C ANISOU 1281 CA GLY A 137 10578 6766 6779 1215 -2775 -738 A C ATOM 1282 C GLY A 137 4.564 15.224 34.757 1.00 61.84 A C ANISOU 1282 C GLY A 137 10320 6699 6476 1237 -2450 -770 A C ATOM 1283 O GLY A 137 3.692 16.006 35.152 1.00 70.22 A O ANISOU 1283 O GLY A 137 11846 7728 7107 1625 -2505 -875 A O ATOM 1284 N THR A 138 4.631 14.804 33.496 1.00 56.64 A N ANISOU 1284 N THR A 138 9159 6191 6172 885 -2120 -676 A N ATOM 1285 CA THR A 138 3.692 15.222 32.467 1.00 61.90 A C ANISOU 1285 CA THR A 138 9759 6973 6786 868 -1833 -700 A C ATOM 1286 C THR A 138 2.754 14.065 32.162 1.00 57.42 A C ANISOU 1286 C THR A 138 8887 6727 6203 958 -1314 -600 A C ATOM 1287 O THR A 138 3.184 12.912 32.094 1.00 57.35 A O ANISOU 1287 O THR A 138 8556 6817 6416 823 -1154 -507 A O ATOM 1288 CB THR A 138 4.435 15.649 31.199 1.00 62.62 A C ANISOU 1288 CB THR A 138 9568 6957 7266 450 -1888 -641 A C ATOM 1289 CG2 THR A 138 3.466 15.910 30.056 1.00 62.63 A C ANISOU 1289 CG2 THR A 138 9484 7093 7220 432 -1557 -671 A C ATOM 1290 OG1 THR A 138 5.182 16.842 31.465 1.00 70.80 A O ANISOU 1290 OG1 THR A 138 10870 7659 8372 338 -2446 -659 A O ATOM 1291 N ASN A 139 1.468 14.360 32.005 1.00 54.72 A N ANISOU 1291 N ASN A 139 8648 6524 5618 1190 -1093 -581 A N ATOM 1292 CA ASN A 139 0.524 13.329 31.604 1.00 51.81 A C ANISOU 1292 CA ASN A 139 7954 6403 5328 1208 -701 -407 A C ATOM 1293 C ASN A 139 0.489 13.342 30.084 1.00 45.98 A C ANISOU 1293 C ASN A 139 6993 5628 4849 872 -593 -439 A C ATOM 1294 O ASN A 139 0.031 14.333 29.497 1.00 46.22 A O ANISOU 1294 O ASN A 139 7167 5607 4787 869 -614 -510 A O ATOM 1295 CB ASN A 139 -0.856 13.575 32.187 1.00 59.41 A C ANISOU 1295 CB ASN A 139 9061 7552 5958 1636 -512 -248 A C ATOM 1296 CG ASN A 139 -1.852 12.511 31.767 1.00 55.41 A C ANISOU 1296 CG ASN A 139 8152 7262 5639 1593 -199 39 A C ATOM 1297 ND2 ASN A 139 -3.005 12.486 32.422 1.00 70.82 A N ANISOU 1297 ND2 ASN A 139 10095 9433 7379 1988 7 336 A N ATOM 1298 OD1 ASN A 139 -1.579 11.709 30.872 1.00 55.42 A O ANISOU 1298 OD1 ASN A 139 7869 7214 5974 1238 -172 36 A O ATOM 1299 N PRO A 140 0.993 12.309 29.405 1.00 44.97 A N ANISOU 1299 N PRO A 140 6576 5505 5006 632 -490 -398 A N ATOM 1300 CA PRO A 140 1.062 12.371 27.935 1.00 42.88 A C ANISOU 1300 CA PRO A 140 6204 5175 4912 408 -404 -441 A C ATOM 1301 C PRO A 140 -0.297 12.518 27.283 1.00 45.44 A C ANISOU 1301 C PRO A 140 6544 5556 5165 451 -277 -394 A C ATOM 1302 O PRO A 140 -0.377 12.990 26.144 1.00 45.83 A O ANISOU 1302 O PRO A 140 6621 5530 5263 326 -250 -468 A O ATOM 1303 CB PRO A 140 1.736 11.046 27.547 1.00 48.76 A C ANISOU 1303 CB PRO A 140 6738 5916 5874 293 -316 -385 A C ATOM 1304 CG PRO A 140 1.612 10.163 28.747 1.00 51.81 A C ANISOU 1304 CG PRO A 140 7056 6397 6232 419 -320 -287 A C ATOM 1305 CD PRO A 140 1.558 11.058 29.945 1.00 48.56 A C ANISOU 1305 CD PRO A 140 6846 6008 5595 612 -456 -315 A C ATOM 1306 N LEU A 141 -1.373 12.159 27.982 1.00 47.66 A N ANISOU 1306 N LEU A 141 6786 5976 5346 642 -197 -219 A N ATOM 1307 CA LEU A 141 -2.702 12.303 27.404 1.00 51.36 A C ANISOU 1307 CA LEU A 141 7206 6501 5808 670 -104 -74 A C ATOM 1308 C LEU A 141 -3.087 13.759 27.191 1.00 51.18 A C ANISOU 1308 C LEU A 141 7409 6467 5569 769 -112 -181 A C ATOM 1309 O LEU A 141 -3.973 14.033 26.370 1.00 51.48 A O ANISOU 1309 O LEU A 141 7414 6508 5638 716 -54 -117 A O ATOM 1310 CB LEU A 141 -3.735 11.618 28.299 1.00 51.08 A C ANISOU 1310 CB LEU A 141 6992 6654 5763 886 1 279 A C ATOM 1311 CG LEU A 141 -3.545 10.105 28.431 1.00 52.94 A C ANISOU 1311 CG LEU A 141 6981 6874 6260 758 -34 435 A C ATOM 1312 CD1 LEU A 141 -4.385 9.560 29.574 1.00 61.58 A C ANISOU 1312 CD1 LEU A 141 7868 8189 7343 1019 79 850 A C ATOM 1313 CD2 LEU A 141 -3.901 9.403 27.139 1.00 54.21 A C ANISOU 1313 CD2 LEU A 141 7049 6857 6690 479 -149 463 A C ATOM 1314 N ASN A 142 -2.442 14.693 27.894 1.00 48.58 A N ANISOU 1314 N ASN A 142 7338 6086 5033 904 -239 -338 A N ATOM 1315 CA ASN A 142 -2.771 16.108 27.807 1.00 54.51 A C ANISOU 1315 CA ASN A 142 8381 6781 5551 1033 -317 -450 A C ATOM 1316 C ASN A 142 -1.866 16.886 26.859 1.00 50.78 A C ANISOU 1316 C ASN A 142 7971 6107 5218 741 -483 -657 A C ATOM 1317 O ASN A 142 -1.995 18.112 26.771 1.00 54.21 A O ANISOU 1317 O ASN A 142 8662 6444 5492 805 -617 -762 A O ATOM 1318 CB ASN A 142 -2.699 16.753 29.194 1.00 60.59 A C ANISOU 1318 CB ASN A 142 9514 7543 5963 1425 -457 -480 A C ATOM 1319 CG ASN A 142 -3.756 16.227 30.136 1.00 66.95 A C ANISOU 1319 CG ASN A 142 10282 8604 6553 1851 -217 -188 A C ATOM 1320 ND2 ASN A 142 -3.429 16.183 31.421 1.00 72.78 A N ANISOU 1320 ND2 ASN A 142 11268 9356 7029 2198 -303 -181 A N ATOM 1321 OD1 ASN A 142 -4.854 15.856 29.715 1.00 67.97 A O ANISOU 1321 OD1 ASN A 142 10148 8910 6765 1880 28 78 A O ATOM 1322 N ILE A 143 -0.935 16.218 26.183 1.00 48.31 A N ANISOU 1322 N ILE A 143 7436 5732 5189 468 -476 -674 A N ATOM 1323 CA ILE A 143 -0.079 16.893 25.212 1.00 44.63 A C ANISOU 1323 CA ILE A 143 6946 5126 4887 239 -563 -747 A C ATOM 1324 C ILE A 143 -0.919 17.269 24.001 1.00 48.65 A C ANISOU 1324 C ILE A 143 7457 5649 5377 188 -413 -773 A C ATOM 1325 O ILE A 143 -1.641 16.433 23.449 1.00 49.31 A O ANISOU 1325 O ILE A 143 7436 5801 5500 185 -247 -718 A O ATOM 1326 CB ILE A 143 1.104 15.992 24.827 1.00 47.91 A C ANISOU 1326 CB ILE A 143 7112 5523 5567 77 -513 -672 A C ATOM 1327 CG1 ILE A 143 2.061 15.805 26.016 1.00 50.34 A C ANISOU 1327 CG1 ILE A 143 7414 5785 5930 87 -722 -632 A C ATOM 1328 CG2 ILE A 143 1.870 16.555 23.631 1.00 52.14 A C ANISOU 1328 CG2 ILE A 143 7545 5982 6282 -85 -487 -624 A C ATOM 1329 CD1 ILE A 143 2.999 14.615 25.835 1.00 53.52 A C ANISOU 1329 CD1 ILE A 143 7548 6231 6555 5 -602 -517 A C ATOM 1330 N ARG A 144 -0.838 18.537 23.586 1.00 46.07 A N ANISOU 1330 N ARG A 144 7272 5224 5009 137 -528 -845 A N ATOM 1331 CA ARG A 144 -1.597 19.020 22.440 1.00 48.75 A C ANISOU 1331 CA ARG A 144 7635 5569 5320 93 -401 -879 A C ATOM 1332 C ARG A 144 -0.895 18.622 21.139 1.00 47.36 A C ANISOU 1332 C ARG A 144 7289 5359 5348 -62 -270 -842 A C ATOM 1333 O ARG A 144 0.338 18.569 21.084 1.00 46.43 A O ANISOU 1333 O ARG A 144 7037 5198 5405 -146 -313 -756 A O ATOM 1334 CB ARG A 144 -1.739 20.540 22.519 1.00 54.72 A C ANISOU 1334 CB ARG A 144 8629 6221 5942 120 -587 -962 A C ATOM 1335 CG ARG A 144 -2.339 21.028 23.851 1.00 71.56 A C ANISOU 1335 CG ARG A 144 11060 8361 7770 407 -731 -1002 A C ATOM 1336 CD ARG A 144 -3.740 21.649 23.812 1.00 96.85 A C ANISOU 1336 CD ARG A 144 14444 11657 10697 643 -608 -999 A C ATOM 1337 NE ARG A 144 -3.644 23.084 23.564 1.00115.75 A N ANISOU 1337 NE ARG A 144 17121 13877 12981 639 -829 -1125 A N ATOM 1338 CZ ARG A 144 -4.207 23.724 22.547 1.00132.51 A C ANISOU 1338 CZ ARG A 144 19236 16000 15111 553 -734 -1153 A C ATOM 1339 NH1 ARG A 144 -5.192 23.190 21.857 1.00125.08 A N ANISOU 1339 NH1 ARG A 144 18104 15225 14196 551 -442 -1060 A N ATOM 1340 NH2 ARG A 144 -3.799 24.954 22.249 1.00139.78 A N ANISOU 1340 NH2 ARG A 144 20362 16722 16028 465 -991 -1253 A N ATOM 1341 N PRO A 145 -1.647 18.318 20.077 1.00 44.35 A N ANISOU 1341 N PRO A 145 6924 4988 4940 -57 -118 -863 A N ATOM 1342 CA PRO A 145 -0.995 17.967 18.806 1.00 41.98 A C ANISOU 1342 CA PRO A 145 6572 4643 4735 -78 19 -831 A C ATOM 1343 C PRO A 145 -0.249 19.153 18.220 1.00 43.80 A C ANISOU 1343 C PRO A 145 6761 4839 5043 -147 15 -771 A C ATOM 1344 O PRO A 145 -0.611 20.312 18.427 1.00 48.44 A O ANISOU 1344 O PRO A 145 7435 5388 5581 -208 -118 -822 A O ATOM 1345 CB PRO A 145 -2.161 17.538 17.906 1.00 50.05 A C ANISOU 1345 CB PRO A 145 7730 5620 5665 -36 70 -892 A C ATOM 1346 CG PRO A 145 -3.340 18.201 18.482 1.00 49.78 A C ANISOU 1346 CG PRO A 145 7745 5633 5537 -48 -7 -907 A C ATOM 1347 CD PRO A 145 -3.118 18.227 19.965 1.00 47.18 A C ANISOU 1347 CD PRO A 145 7359 5386 5182 4 -84 -867 A C ATOM 1348 N LYS A 146 0.839 18.852 17.519 1.00 43.39 A N ANISOU 1348 N LYS A 146 5882 4156 6449 564 642 -488 A N ATOM 1349 CA ALYS A 146 1.684 19.877 16.929 0.40 47.92 A C ANISOU 1349 CA ALYS A 146 6532 4621 7054 495 569 -501 A C ATOM 1350 CA BLYS A 146 1.667 19.884 16.919 0.61 47.92 A C ANISOU 1350 CA BLYS A 146 6531 4620 7056 497 569 -500 A C ATOM 1351 C LYS A 146 2.152 19.408 15.561 1.00 44.90 A C ANISOU 1351 C LYS A 146 6071 4305 6686 414 455 -386 A C ATOM 1352 O LYS A 146 2.324 18.212 15.330 1.00 46.44 A O ANISOU 1352 O LYS A 146 6192 4640 6813 372 413 -348 A O ATOM 1353 CB ALYS A 146 2.936 20.192 17.771 0.40 49.67 A C ANISOU 1353 CB ALYS A 146 6886 4820 7165 404 543 -639 A C ATOM 1354 CB BLYS A 146 2.871 20.218 17.805 0.61 49.71 A C ANISOU 1354 CB BLYS A 146 6892 4821 7173 412 549 -640 A C ATOM 1355 CG ALYS A 146 2.770 20.095 19.273 0.40 51.07 A C ANISOU 1355 CG ALYS A 146 7156 5011 7239 461 630 -768 A C ATOM 1356 CG BLYS A 146 3.747 19.009 18.069 0.61 48.47 A C ANISOU 1356 CG BLYS A 146 6713 4827 6877 323 488 -658 A C ATOM 1357 CD ALYS A 146 2.314 21.404 19.889 0.40 53.83 A C ANISOU 1357 CD ALYS A 146 7619 5185 7647 543 715 -861 A C ATOM 1358 CD BLYS A 146 4.775 19.265 19.160 0.61 58.39 A C ANISOU 1358 CD BLYS A 146 8093 6075 8016 264 463 -808 A C ATOM 1359 CE ALYS A 146 1.803 21.170 21.303 0.40 51.09 A C ANISOU 1359 CE ALYS A 146 7353 4867 7192 640 834 -964 A C ATOM 1360 CE BLYS A 146 5.641 18.030 19.383 0.61 60.16 A C ANISOU 1360 CE BLYS A 146 8285 6466 8108 192 395 -809 A C ATOM 1361 NZ ALYS A 146 2.566 20.080 21.991 0.40 43.13 A N ANISOU 1361 NZ ALYS A 146 6369 4017 6002 577 789 -1009 A N ATOM 1362 NZ BLYS A 146 7.076 18.387 19.596 0.61 71.25 A N ANISOU 1362 NZ BLYS A 146 9748 7863 9461 73 292 -900 A N ATOM 1363 N ALA A 147 2.380 20.362 14.666 1.00 44.39 A N ANISOU 1363 N ALA A 147 6035 4131 6703 397 414 -332 A N ATOM 1364 CA ALA A 147 3.010 20.051 13.387 1.00 42.43 A C ANISOU 1364 CA ALA A 147 5746 3934 6442 317 318 -230 A C ATOM 1365 C ALA A 147 4.516 20.206 13.551 1.00 44.93 A C ANISOU 1365 C ALA A 147 6136 4246 6690 182 280 -296 A C ATOM 1366 O ALA A 147 4.983 21.205 14.106 1.00 47.80 A O ANISOU 1366 O ALA A 147 6595 4484 7085 152 305 -381 A O ATOM 1367 CB ALA A 147 2.491 20.966 12.279 1.00 48.50 A C ANISOU 1367 CB ALA A 147 6511 4591 7324 374 298 -116 A C ATOM 1368 N VAL A 148 5.273 19.219 13.080 1.00 40.47 A N ANISOU 1368 N VAL A 148 5522 3814 6042 100 218 -262 A N ATOM 1369 CA VAL A 148 6.717 19.215 13.277 1.00 43.01 A C ANISOU 1369 CA VAL A 148 5881 4156 6307 -25 181 -322 A C ATOM 1370 C VAL A 148 7.375 18.485 12.119 1.00 44.49 A C ANISOU 1370 C VAL A 148 6008 4442 6455 -89 124 -223 A C ATOM 1371 O VAL A 148 6.800 17.571 11.522 1.00 43.15 A O ANISOU 1371 O VAL A 148 5772 4370 6252 -45 104 -148 A O ATOM 1372 CB VAL A 148 7.081 18.561 14.634 1.00 49.20 A C ANISOU 1372 CB VAL A 148 6683 5023 6986 -40 186 -449 A C ATOM 1373 CG1 VAL A 148 6.419 17.200 14.764 1.00 48.96 A C ANISOU 1373 CG1 VAL A 148 6578 5137 6888 17 197 -412 A C ATOM 1374 CG2 VAL A 148 8.578 18.431 14.787 1.00 60.58 A C ANISOU 1374 CG2 VAL A 148 8134 6508 8375 -165 125 -504 A C ATOM 1375 N GLU A 149 8.608 18.880 11.811 1.00 44.11 A N ANISOU 1375 N GLU A 149 5982 4366 6413 -196 103 -227 A N ATOM 1376 CA GLU A 149 9.359 18.189 10.776 1.00 44.75 A C ANISOU 1376 CA GLU A 149 6012 4542 6448 -255 70 -140 A C ATOM 1377 C GLU A 149 10.029 16.948 11.358 1.00 42.15 A C ANISOU 1377 C GLU A 149 5633 4366 6017 -294 39 -200 A C ATOM 1378 O GLU A 149 10.694 17.021 12.396 1.00 43.31 A O ANISOU 1378 O GLU A 149 5794 4519 6141 -342 28 -308 A O ATOM 1379 CB GLU A 149 10.409 19.120 10.160 1.00 53.28 A C ANISOU 1379 CB GLU A 149 7123 5528 7595 -353 81 -103 A C ATOM 1380 CG GLU A 149 10.736 18.763 8.714 1.00 66.70 A C ANISOU 1380 CG GLU A 149 8797 7280 9266 -367 80 36 A C ATOM 1381 CD GLU A 149 10.760 19.964 7.784 1.00 84.48 A C ANISOU 1381 CD GLU A 149 11109 9385 11605 -375 119 140 A C ATOM 1382 OE1 GLU A 149 10.458 19.795 6.578 1.00 83.04 A O ANISOU 1382 OE1 GLU A 149 10937 9228 11385 -328 118 269 A O ATOM 1383 OE2 GLU A 149 11.084 21.072 8.262 1.00 82.41 A O ANISOU 1383 OE2 GLU A 149 10893 8975 11443 -426 148 92 A O ATOM 1384 N LYS A 150 9.864 15.815 10.676 1.00 41.68 A N ANISOU 1384 N LYS A 150 5520 4424 5891 -269 20 -131 A N ATOM 1385 CA LYS A 150 10.498 14.561 11.054 1.00 40.69 A C ANISOU 1385 CA LYS A 150 5349 4437 5675 -295 -4 -165 A C ATOM 1386 C LYS A 150 11.118 13.887 9.837 1.00 41.57 A C ANISOU 1386 C LYS A 150 5424 4625 5747 -326 -18 -78 A C ATOM 1387 O LYS A 150 10.709 14.120 8.695 1.00 42.08 A O ANISOU 1387 O LYS A 150 5502 4660 5826 -301 -16 15 A O ATOM 1388 CB LYS A 150 9.497 13.570 11.671 1.00 41.36 A C ANISOU 1388 CB LYS A 150 5411 4593 5712 -216 3 -187 A C ATOM 1389 CG LYS A 150 8.747 14.096 12.865 1.00 45.81 A C ANISOU 1389 CG LYS A 150 6014 5094 6298 -163 41 -265 A C ATOM 1390 CD LYS A 150 9.583 14.057 14.117 1.00 45.93 A C ANISOU 1390 CD LYS A 150 6065 5137 6251 -201 32 -375 A C ATOM 1391 CE LYS A 150 8.701 14.041 15.336 1.00 51.74 A C ANISOU 1391 CE LYS A 150 6843 5858 6957 -122 83 -444 A C ATOM 1392 NZ LYS A 150 9.405 14.593 16.503 1.00 53.04 A N ANISOU 1392 NZ LYS A 150 7082 5998 7074 -151 69 -566 A N ATOM 1393 N ILE A 151 12.088 13.016 10.108 1.00 38.45 A N ANISOU 1393 N ILE A 151 4989 4330 5291 -368 -33 -108 A N ATOM 1394 CA ILE A 151 12.534 12.002 9.160 1.00 39.21 A C ANISOU 1394 CA ILE A 151 5050 4520 5326 -370 -37 -44 A C ATOM 1395 C ILE A 151 11.751 10.730 9.451 1.00 37.92 A C ANISOU 1395 C ILE A 151 4871 4437 5101 -305 -53 -57 A C ATOM 1396 O ILE A 151 11.812 10.210 10.568 1.00 37.82 A O ANISOU 1396 O ILE A 151 4847 4465 5059 -294 -56 -124 A O ATOM 1397 CB ILE A 151 14.044 11.732 9.289 1.00 40.13 A C ANISOU 1397 CB ILE A 151 5121 4698 5430 -442 -36 -65 A C ATOM 1398 CG1 ILE A 151 14.865 13.014 9.180 1.00 52.15 A C ANISOU 1398 CG1 ILE A 151 6643 6131 7041 -526 -17 -65 A C ATOM 1399 CG2 ILE A 151 14.443 10.699 8.247 1.00 37.72 A C ANISOU 1399 CG2 ILE A 151 4792 4481 5060 -427 -21 2 A C ATOM 1400 CD1 ILE A 151 14.754 13.707 7.874 1.00 53.65 A C ANISOU 1400 CD1 ILE A 151 6867 6250 7266 -534 28 42 A C ATOM 1401 N VAL A 152 11.021 10.214 8.457 1.00 36.22 A N ANISOU 1401 N VAL A 152 4658 4240 4866 -262 -65 7 A N ATOM 1402 CA VAL A 152 10.235 8.994 8.618 1.00 35.97 A C ANISOU 1402 CA VAL A 152 4602 4266 4798 -214 -82 -3 A C ATOM 1403 C VAL A 152 11.016 7.823 8.034 1.00 38.25 A C ANISOU 1403 C VAL A 152 4879 4641 5013 -226 -87 13 A C ATOM 1404 O VAL A 152 11.569 7.922 6.933 1.00 38.78 A O ANISOU 1404 O VAL A 152 4964 4718 5050 -242 -85 63 A O ATOM 1405 CB VAL A 152 8.850 9.125 7.965 1.00 36.68 A C ANISOU 1405 CB VAL A 152 4690 4317 4928 -160 -110 41 A C ATOM 1406 CG1 VAL A 152 8.030 7.847 8.202 1.00 39.05 A C ANISOU 1406 CG1 VAL A 152 4951 4668 5220 -127 -125 24 A C ATOM 1407 CG2 VAL A 152 8.150 10.324 8.516 1.00 38.93 A C ANISOU 1407 CG2 VAL A 152 4985 4511 5294 -135 -92 31 A C ATOM 1408 N PHE A 153 11.094 6.737 8.807 1.00 35.29 A N ANISOU 1408 N PHE A 153 4481 4322 4604 -212 -82 -28 A N ATOM 1409 CA PHE A 153 11.814 5.505 8.499 1.00 36.18 A C ANISOU 1409 CA PHE A 153 4584 4508 4654 -210 -80 -24 A C ATOM 1410 C PHE A 153 10.791 4.385 8.326 1.00 36.04 A C ANISOU 1410 C PHE A 153 4565 4499 4631 -172 -95 -23 A C ATOM 1411 O PHE A 153 9.930 4.199 9.188 1.00 35.84 A O ANISOU 1411 O PHE A 153 4523 4453 4641 -151 -86 -44 A O ATOM 1412 CB PHE A 153 12.796 5.198 9.652 1.00 35.94 A C ANISOU 1412 CB PHE A 153 4531 4524 4601 -221 -66 -69 A C ATOM 1413 CG PHE A 153 13.461 3.837 9.598 1.00 37.57 A C ANISOU 1413 CG PHE A 153 4723 4801 4752 -199 -58 -67 A C ATOM 1414 CD1 PHE A 153 12.764 2.668 9.857 1.00 37.12 A C ANISOU 1414 CD1 PHE A 153 4675 4751 4677 -158 -53 -70 A C ATOM 1415 CD2 PHE A 153 14.829 3.748 9.364 1.00 40.56 A C ANISOU 1415 CD2 PHE A 153 5071 5230 5112 -219 -48 -60 A C ATOM 1416 CE1 PHE A 153 13.396 1.439 9.812 1.00 38.42 A C ANISOU 1416 CE1 PHE A 153 4836 4962 4799 -132 -40 -66 A C ATOM 1417 CE2 PHE A 153 15.466 2.528 9.339 1.00 37.54 A C ANISOU 1417 CE2 PHE A 153 4672 4904 4685 -185 -35 -55 A C ATOM 1418 CZ PHE A 153 14.754 1.372 9.567 1.00 40.94 A C ANISOU 1418 CZ PHE A 153 5129 5333 5091 -138 -32 -59 A C ATOM 1419 N PHE A 154 10.877 3.657 7.208 1.00 33.94 A N ANISOU 1419 N PHE A 154 4318 4256 4322 -165 -114 0 A N ATOM 1420 CA PHE A 154 10.089 2.451 6.965 1.00 34.55 A C ANISOU 1420 CA PHE A 154 4394 4336 4397 -144 -138 -11 A C ATOM 1421 C PHE A 154 11.035 1.316 6.595 1.00 41.62 A C ANISOU 1421 C PHE A 154 5312 5277 5225 -136 -119 -20 A C ATOM 1422 O PHE A 154 11.903 1.498 5.731 1.00 39.64 A O ANISOU 1422 O PHE A 154 5089 5052 4920 -139 -108 1 A O ATOM 1423 CB PHE A 154 9.120 2.602 5.802 1.00 37.13 A C ANISOU 1423 CB PHE A 154 4738 4636 4734 -135 -202 10 A C ATOM 1424 CG PHE A 154 7.718 2.889 6.205 1.00 38.75 A C ANISOU 1424 CG PHE A 154 4895 4797 5031 -124 -232 8 A C ATOM 1425 CD1 PHE A 154 7.401 4.094 6.790 1.00 44.78 A C ANISOU 1425 CD1 PHE A 154 5640 5524 5852 -117 -212 20 A C ATOM 1426 CD2 PHE A 154 6.723 1.957 6.002 1.00 47.16 A C ANISOU 1426 CD2 PHE A 154 5929 5849 6139 -121 -275 -9 A C ATOM 1427 CE1 PHE A 154 6.103 4.371 7.165 1.00 48.33 A C ANISOU 1427 CE1 PHE A 154 6035 5932 6395 -94 -224 22 A C ATOM 1428 CE2 PHE A 154 5.420 2.228 6.378 1.00 47.19 A C ANISOU 1428 CE2 PHE A 154 5865 5815 6251 -110 -294 -5 A C ATOM 1429 CZ PHE A 154 5.118 3.433 6.964 1.00 44.99 A C ANISOU 1429 CZ PHE A 154 5564 5508 6024 -91 -262 13 A C ATOM 1430 N SER A 155 10.853 0.146 7.199 1.00 35.08 A N ANISOU 1430 N SER A 155 4474 4450 4403 -120 -104 -43 A N ATOM 1431 CA ASER A 155 11.579 -1.055 6.791 0.70 34.92 A C ANISOU 1431 CA ASER A 155 4482 4455 4330 -100 -86 -53 A C ATOM 1432 CA BSER A 155 11.575 -1.052 6.786 0.30 35.16 A C ANISOU 1432 CA BSER A 155 4512 4485 4360 -100 -86 -53 A C ATOM 1433 C SER A 155 10.603 -2.221 6.768 1.00 41.88 A C ANISOU 1433 C SER A 155 5372 5292 5247 -95 -104 -75 A C ATOM 1434 O SER A 155 9.747 -2.335 7.647 1.00 41.33 A O ANISOU 1434 O SER A 155 5267 5191 5245 -101 -94 -76 A O ATOM 1435 CB ASER A 155 12.777 -1.358 7.715 0.70 35.92 A C ANISOU 1435 CB ASER A 155 4587 4626 4433 -80 -37 -52 A C ATOM 1436 CB BSER A 155 12.750 -1.361 7.716 0.30 35.88 A C ANISOU 1436 CB BSER A 155 4584 4622 4429 -81 -37 -52 A C ATOM 1437 OG ASER A 155 12.425 -1.678 9.053 0.70 36.57 A O ANISOU 1437 OG ASER A 155 4651 4700 4543 -67 -19 -58 A O ATOM 1438 OG BSER A 155 13.566 -2.384 7.169 0.30 40.40 A O ANISOU 1438 OG BSER A 155 5180 5216 4954 -49 -12 -54 A O ATOM 1439 N ASP A 156 10.740 -3.085 5.762 1.00 35.66 A N ANISOU 1439 N ASP A 156 4633 4497 4417 -85 -123 -96 A N ATOM 1440 CA ASP A 156 9.772 -4.152 5.523 1.00 35.85 A C ANISOU 1440 CA ASP A 156 4669 4464 4487 -96 -158 -129 A C ATOM 1441 C ASP A 156 10.504 -5.392 5.040 1.00 37.38 A C ANISOU 1441 C ASP A 156 4926 4649 4626 -68 -132 -158 A C ATOM 1442 O ASP A 156 11.379 -5.302 4.177 1.00 38.07 A O ANISOU 1442 O ASP A 156 5065 4774 4627 -42 -121 -161 A O ATOM 1443 CB ASP A 156 8.740 -3.630 4.501 1.00 37.50 A C ANISOU 1443 CB ASP A 156 4883 4655 4711 -120 -252 -142 A C ATOM 1444 CG ASP A 156 7.631 -4.607 4.174 1.00 39.25 A C ANISOU 1444 CG ASP A 156 5098 4816 5001 -147 -316 -187 A C ATOM 1445 OD1 ASP A 156 7.877 -5.764 3.805 1.00 38.09 A O ANISOU 1445 OD1 ASP A 156 5004 4639 4831 -145 -314 -229 A O ATOM 1446 OD2 ASP A 156 6.467 -4.154 4.215 1.00 43.09 A O ANISOU 1446 OD2 ASP A 156 5519 5278 5573 -173 -374 -183 A O ATOM 1447 N ILE A 157 10.156 -6.552 5.617 1.00 36.39 A N ANISOU 1447 N ILE A 157 4801 4467 4559 -67 -107 -174 A N ATOM 1448 CA ILE A 157 10.783 -7.814 5.233 1.00 37.45 A C ANISOU 1448 CA ILE A 157 5001 4571 4658 -33 -76 -204 A C ATOM 1449 C ILE A 157 10.433 -8.189 3.798 1.00 38.78 A C ANISOU 1449 C ILE A 157 5243 4709 4782 -46 -146 -267 A C ATOM 1450 O ILE A 157 9.273 -8.121 3.365 1.00 37.18 A O ANISOU 1450 O ILE A 157 5029 4467 4630 -94 -233 -299 A O ATOM 1451 CB ILE A 157 10.362 -8.941 6.204 1.00 34.92 A C ANISOU 1451 CB ILE A 157 4670 4175 4424 -34 -31 -198 A C ATOM 1452 CG1 ILE A 157 10.830 -8.594 7.622 1.00 38.29 A C ANISOU 1452 CG1 ILE A 157 5049 4643 4856 -4 37 -135 A C ATOM 1453 CG2 ILE A 157 10.882 -10.318 5.711 1.00 40.10 A C ANISOU 1453 CG2 ILE A 157 5407 4770 5058 2 -2 -237 A C ATOM 1454 CD1 ILE A 157 10.348 -9.550 8.670 1.00 38.32 A C ANISOU 1454 CD1 ILE A 157 5050 4577 4934 2 95 -107 A C ATOM 1455 N VAL A 158 11.451 -8.623 3.058 1.00 37.67 A N ANISOU 1455 N VAL A 158 5180 4588 4546 5 -111 -288 A N ATOM 1456 CA VAL A 158 11.281 -9.101 1.693 1.00 38.05 A C ANISOU 1456 CA VAL A 158 5329 4608 4519 11 -165 -358 A C ATOM 1457 C VAL A 158 10.674 -10.501 1.686 1.00 38.51 A C ANISOU 1457 C VAL A 158 5430 4557 4644 -8 -188 -428 A C ATOM 1458 O VAL A 158 11.196 -11.418 2.328 1.00 41.44 A O ANISOU 1458 O VAL A 158 5810 4883 5052 25 -108 -420 A O ATOM 1459 CB VAL A 158 12.633 -9.090 0.955 1.00 39.70 A C ANISOU 1459 CB VAL A 158 5608 4874 4601 83 -90 -353 A C ATOM 1460 CG1 VAL A 158 12.434 -9.579 -0.456 1.00 43.21 A C ANISOU 1460 CG1 VAL A 158 6183 5291 4943 99 -141 -432 A C ATOM 1461 CG2 VAL A 158 13.254 -7.692 1.018 1.00 41.69 A C ANISOU 1461 CG2 VAL A 158 5805 5221 4815 86 -58 -279 A C ATOM 1462 N SER A 159 9.548 -10.653 0.974 1.00 38.84 A N ANISOU 1462 N SER A 159 5496 4550 4713 -64 -305 -493 A N ATOM 1463 CA ASER A 159 8.931 -11.955 0.723 0.82 42.57 A C ANISOU 1463 CA ASER A 159 6018 4905 5251 -98 -348 -580 A C ATOM 1464 CA BSER A 159 8.920 -11.952 0.723 0.18 42.70 A C ANISOU 1464 CA BSER A 159 6034 4921 5268 -98 -349 -580 A C ATOM 1465 C SER A 159 8.595 -12.684 2.023 1.00 45.61 A C ANISOU 1465 C SER A 159 6329 5208 5792 -127 -279 -543 A C ATOM 1466 O SER A 159 8.742 -13.903 2.128 1.00 48.14 A O ANISOU 1466 O SER A 159 6707 5429 6156 -120 -236 -582 A O ATOM 1467 CB ASER A 159 9.833 -12.820 -0.170 0.82 45.92 A C ANISOU 1467 CB ASER A 159 6588 5302 5557 -32 -311 -649 A C ATOM 1468 CB BSER A 159 9.796 -12.821 -0.186 0.18 46.18 A C ANISOU 1468 CB BSER A 159 6621 5334 5591 -34 -315 -651 A C ATOM 1469 OG ASER A 159 9.060 -13.739 -0.920 0.82 60.64 A O ANISOU 1469 OG ASER A 159 8530 7064 7444 -77 -410 -765 A O ATOM 1470 OG BSER A 159 10.823 -13.457 0.551 0.18 52.50 A O ANISOU 1470 OG BSER A 159 7427 6117 6404 30 -178 -610 A O ATOM 1471 N PHE A 160 8.116 -11.937 3.017 1.00 42.77 A N ANISOU 1471 N PHE A 160 5852 4883 5515 -156 -259 -467 A N ATOM 1472 CA PHE A 160 7.694 -12.563 4.268 1.00 40.31 A C ANISOU 1472 CA PHE A 160 5477 4498 5340 -180 -184 -421 A C ATOM 1473 C PHE A 160 6.597 -13.599 4.057 1.00 46.75 A C ANISOU 1473 C PHE A 160 6288 5180 6295 -260 -236 -485 A C ATOM 1474 O PHE A 160 6.526 -14.586 4.799 1.00 47.65 A O ANISOU 1474 O PHE A 160 6405 5195 6505 -268 -153 -463 A O ATOM 1475 CB PHE A 160 7.190 -11.505 5.239 1.00 41.97 A C ANISOU 1475 CB PHE A 160 5574 4768 5606 -198 -162 -342 A C ATOM 1476 CG PHE A 160 6.721 -12.067 6.550 1.00 48.37 A C ANISOU 1476 CG PHE A 160 6329 5511 6538 -215 -69 -284 A C ATOM 1477 CD1 PHE A 160 7.632 -12.419 7.528 1.00 54.24 A C ANISOU 1477 CD1 PHE A 160 7103 6266 7240 -147 42 -220 A C ATOM 1478 CD2 PHE A 160 5.376 -12.252 6.795 1.00 54.98 A C ANISOU 1478 CD2 PHE A 160 7082 6276 7533 -293 -91 -287 A C ATOM 1479 CE1 PHE A 160 7.201 -12.937 8.739 1.00 52.60 A C ANISOU 1479 CE1 PHE A 160 6864 5998 7124 -151 136 -155 A C ATOM 1480 CE2 PHE A 160 4.945 -12.779 7.998 1.00 54.68 A C ANISOU 1480 CE2 PHE A 160 7000 6172 7604 -304 19 -221 A C ATOM 1481 CZ PHE A 160 5.866 -13.116 8.964 1.00 50.41 A C ANISOU 1481 CZ PHE A 160 6513 5644 6998 -230 135 -153 A C ATOM 1482 N SER A 161 5.722 -13.384 3.073 1.00 43.79 A N ANISOU 1482 N SER A 161 5902 4796 5940 -320 -375 -560 A N ATOM 1483 CA SER A 161 4.596 -14.293 2.870 1.00 51.09 A C ANISOU 1483 CA SER A 161 6796 5593 7023 -414 -446 -630 A C ATOM 1484 C SER A 161 5.081 -15.717 2.671 1.00 54.07 A C ANISOU 1484 C SER A 161 7290 5847 7408 -405 -401 -693 A C ATOM 1485 O SER A 161 4.365 -16.681 2.969 1.00 54.61 A O ANISOU 1485 O SER A 161 7330 5777 7640 -479 -394 -720 A O ATOM 1486 CB SER A 161 3.778 -13.842 1.663 1.00 59.84 A C ANISOU 1486 CB SER A 161 7894 6727 8114 -463 -633 -716 A C ATOM 1487 OG SER A 161 3.035 -12.675 1.965 1.00 64.55 A O ANISOU 1487 OG SER A 161 8358 7402 8766 -482 -675 -654 A O ATOM 1488 N THR A 162 6.302 -15.858 2.175 1.00 49.09 A N ANISOU 1488 N THR A 162 6786 5256 6612 -314 -359 -713 A N ATOM 1489 CA THR A 162 6.873 -17.174 1.941 1.00 57.85 A C ANISOU 1489 CA THR A 162 8017 6247 7715 -282 -305 -774 A C ATOM 1490 C THR A 162 7.161 -17.883 3.259 1.00 59.00 A C ANISOU 1490 C THR A 162 8135 6315 7965 -258 -153 -679 A C ATOM 1491 O THR A 162 6.863 -19.075 3.410 1.00 56.37 A O ANISOU 1491 O THR A 162 7844 5824 7749 -294 -122 -714 A O ATOM 1492 CB THR A 162 8.140 -17.010 1.105 1.00 64.99 A C ANISOU 1492 CB THR A 162 9048 7231 8414 -175 -280 -804 A C ATOM 1493 CG2 THR A 162 8.880 -18.334 0.971 1.00 79.30 A C ANISOU 1493 CG2 THR A 162 10988 8926 10218 -114 -196 -854 A C ATOM 1494 OG1 THR A 162 7.773 -16.543 -0.199 1.00 59.22 A O ANISOU 1494 OG1 THR A 162 8374 6547 7579 -197 -422 -898 A O ATOM 1495 N PHE A 163 7.766 -17.170 4.218 1.00 50.76 A N ANISOU 1495 N PHE A 163 7032 5378 6875 -194 -61 -560 A N ATOM 1496 CA PHE A 163 7.979 -17.734 5.547 1.00 48.96 A C ANISOU 1496 CA PHE A 163 6781 5095 6726 -162 73 -457 A C ATOM 1497 C PHE A 163 6.670 -18.290 6.092 1.00 46.05 A C ANISOU 1497 C PHE A 163 6342 4596 6557 -269 80 -446 A C ATOM 1498 O PHE A 163 6.600 -19.437 6.544 1.00 53.72 A O ANISOU 1498 O PHE A 163 7357 5424 7631 -275 161 -428 A O ATOM 1499 CB PHE A 163 8.502 -16.676 6.532 1.00 48.06 A C ANISOU 1499 CB PHE A 163 6594 5125 6542 -103 132 -344 A C ATOM 1500 CG PHE A 163 9.907 -16.195 6.271 1.00 48.78 A C ANISOU 1500 CG PHE A 163 6728 5337 6470 1 153 -330 A C ATOM 1501 CD1 PHE A 163 10.145 -15.146 5.399 1.00 62.02 A C ANISOU 1501 CD1 PHE A 163 8396 7128 8042 0 78 -368 A C ATOM 1502 CD2 PHE A 163 10.981 -16.755 6.943 1.00 49.90 A C ANISOU 1502 CD2 PHE A 163 6907 5480 6573 103 251 -267 A C ATOM 1503 CE1 PHE A 163 11.434 -14.687 5.181 1.00 56.40 A C ANISOU 1503 CE1 PHE A 163 7706 6522 7203 87 113 -346 A C ATOM 1504 CE2 PHE A 163 12.270 -16.308 6.724 1.00 51.70 A C ANISOU 1504 CE2 PHE A 163 7146 5821 6676 194 270 -252 A C ATOM 1505 CZ PHE A 163 12.496 -15.268 5.851 1.00 51.46 A C ANISOU 1505 CZ PHE A 163 7098 5898 6556 180 208 -291 A C ATOM 1506 N ALA A 164 5.621 -17.463 6.055 1.00 52.66 A N ANISOU 1506 N ALA A 164 7065 5479 7463 -352 4 -449 A N ATOM 1507 CA ALA A 164 4.337 -17.830 6.639 1.00 52.37 A C ANISOU 1507 CA ALA A 164 6926 5338 7634 -455 24 -424 A C ATOM 1508 C ALA A 164 3.752 -19.071 5.989 1.00 65.31 A C ANISOU 1508 C ALA A 164 8606 6799 9411 -543 -27 -524 A C ATOM 1509 O ALA A 164 3.001 -19.813 6.633 1.00 61.94 A O ANISOU 1509 O ALA A 164 8126 6237 9172 -616 44 -487 A O ATOM 1510 CB ALA A 164 3.363 -16.658 6.508 1.00 52.40 A C ANISOU 1510 CB ALA A 164 6793 5433 7682 -515 -66 -424 A C ATOM 1511 N GLU A 165 4.084 -19.318 4.723 1.00 62.39 A N ANISOU 1511 N GLU A 165 8337 6418 8949 -539 -143 -653 A N ATOM 1512 CA GLU A 165 3.492 -20.444 4.015 1.00 71.97 A C ANISOU 1512 CA GLU A 165 9599 7458 10287 -631 -218 -775 A C ATOM 1513 C GLU A 165 4.240 -21.744 4.273 1.00 68.75 A C ANISOU 1513 C GLU A 165 9326 6902 9894 -580 -98 -774 A C ATOM 1514 O GLU A 165 3.636 -22.820 4.208 1.00 68.36 A O ANISOU 1514 O GLU A 165 9295 6663 10015 -669 -100 -831 A O ATOM 1515 CB GLU A 165 3.454 -20.155 2.512 1.00 82.31 A C ANISOU 1515 CB GLU A 165 10978 8818 11476 -644 -406 -925 A C ATOM 1516 CG GLU A 165 2.056 -19.917 1.967 1.00105.64 A C ANISOU 1516 CG GLU A 165 13816 11752 14570 -778 -580 -1005 A C ATOM 1517 CD GLU A 165 1.173 -21.146 2.079 1.00142.94 A C ANISOU 1517 CD GLU A 165 18507 16265 19538 -907 -594 -1069 A C ATOM 1518 OE1 GLU A 165 0.168 -21.092 2.819 1.00143.73 A O ANISOU 1518 OE1 GLU A 165 18437 16321 19852 -1001 -563 -1002 A O ATOM 1519 OE2 GLU A 165 1.485 -22.167 1.430 1.00140.09 A O ANISOU 1519 OE2 GLU A 165 18291 15774 19163 -916 -625 -1187 A O ATOM 1520 N LYS A 166 5.533 -21.667 4.592 1.00 61.39 A N ANISOU 1520 N LYS A 166 8480 6043 8802 -439 6 -708 A N ATOM 1521 CA LYS A 166 6.399 -22.834 4.613 1.00 64.46 A C ANISOU 1521 CA LYS A 166 9012 6307 9175 -360 102 -719 A C ATOM 1522 C LYS A 166 6.824 -23.292 6.004 1.00 68.08 A C ANISOU 1522 C LYS A 166 9462 6718 9686 -291 279 -561 A C ATOM 1523 O LYS A 166 7.251 -24.442 6.147 1.00 66.90 A O ANISOU 1523 O LYS A 166 9418 6416 9586 -246 365 -558 A O ATOM 1524 CB LYS A 166 7.668 -22.550 3.794 1.00 72.34 A C ANISOU 1524 CB LYS A 166 10123 7415 9949 -232 88 -770 A C ATOM 1525 CG LYS A 166 7.406 -22.164 2.344 1.00 88.94 A C ANISOU 1525 CG LYS A 166 12276 9565 11954 -273 -74 -923 A C ATOM 1526 CD LYS A 166 6.795 -23.308 1.550 1.00107.43 A C ANISOU 1526 CD LYS A 166 14716 11710 14394 -356 -152 -1079 A C ATOM 1527 CE LYS A 166 6.362 -22.851 0.165 1.00112.18 A C ANISOU 1527 CE LYS A 166 15364 12371 14891 -404 -341 -1231 A C ATOM 1528 NZ LYS A 166 7.177 -23.474 -0.912 1.00118.85 A N ANISOU 1528 NZ LYS A 166 16410 13169 15581 -319 -348 -1361 A N ATOM 1529 N LEU A 167 6.726 -22.437 7.020 1.00 52.41 A N ANISOU 1529 N LEU A 167 7369 4856 7687 -272 335 -431 A N ATOM 1530 CA LEU A 167 7.249 -22.712 8.352 1.00 47.66 A C ANISOU 1530 CA LEU A 167 6776 4250 7083 -182 490 -275 A C ATOM 1531 C LEU A 167 6.121 -22.891 9.368 1.00 48.19 A C ANISOU 1531 C LEU A 167 6752 4230 7327 -272 570 -180 A C ATOM 1532 O LEU A 167 5.036 -22.329 9.196 1.00 50.46 A O ANISOU 1532 O LEU A 167 6925 4537 7711 -387 504 -213 A O ATOM 1533 CB LEU A 167 8.142 -21.564 8.838 1.00 50.47 A C ANISOU 1533 CB LEU A 167 7095 4823 7259 -74 500 -196 A C ATOM 1534 CG LEU A 167 9.398 -21.232 8.032 1.00 59.41 A C ANISOU 1534 CG LEU A 167 8291 6068 8214 28 454 -253 A C ATOM 1535 CD1 LEU A 167 10.101 -20.017 8.622 1.00 58.03 A C ANISOU 1535 CD1 LEU A 167 8049 6097 7904 101 459 -173 A C ATOM 1536 CD2 LEU A 167 10.315 -22.435 8.012 1.00 61.78 A C ANISOU 1536 CD2 LEU A 167 8712 6257 8505 133 536 -247 A C ATOM 1537 N PRO A 168 6.352 -23.648 10.445 1.00 48.55 A N ANISOU 1537 N PRO A 168 6845 4183 7420 -213 721 -53 A N ATOM 1538 CA PRO A 168 5.377 -23.678 11.542 1.00 52.17 A C ANISOU 1538 CA PRO A 168 7220 4585 8016 -276 830 65 A C ATOM 1539 C PRO A 168 5.212 -22.298 12.157 1.00 50.08 A C ANISOU 1539 C PRO A 168 6852 4521 7654 -256 822 127 A C ATOM 1540 O PRO A 168 6.118 -21.462 12.117 1.00 45.81 A O ANISOU 1540 O PRO A 168 6326 4153 6926 -161 773 125 A O ATOM 1541 CB PRO A 168 5.988 -24.671 12.541 1.00 53.38 A C ANISOU 1541 CB PRO A 168 7483 4632 8169 -171 993 202 A C ATOM 1542 CG PRO A 168 6.941 -25.483 11.731 1.00 59.86 A C ANISOU 1542 CG PRO A 168 8431 5374 8939 -99 957 120 A C ATOM 1543 CD PRO A 168 7.507 -24.515 10.739 1.00 52.42 A C ANISOU 1543 CD PRO A 168 7467 4613 7837 -74 809 1 A C ATOM 1544 N AVAL A 169 4.036 -22.072 12.743 0.65 48.08 A N ANISOU 1544 N AVAL A 169 6489 4235 7543 -348 881 182 A N ATOM 1545 N BVAL A 169 4.039 -22.079 12.757 0.35 48.11 A N ANISOU 1545 N BVAL A 169 6494 4239 7547 -347 883 184 A N ATOM 1546 CA AVAL A 169 3.673 -20.737 13.212 0.65 47.38 A C ANISOU 1546 CA AVAL A 169 6296 4317 7390 -344 869 219 A C ATOM 1547 CA BVAL A 169 3.669 -20.743 13.219 0.35 47.40 A C ANISOU 1547 CA BVAL A 169 6298 4318 7394 -344 870 220 A C ATOM 1548 C AVAL A 169 4.703 -20.198 14.202 0.65 45.58 A C ANISOU 1548 C AVAL A 169 6133 4230 6956 -194 936 322 A C ATOM 1549 C BVAL A 169 4.698 -20.198 14.203 0.35 45.62 A C ANISOU 1549 C BVAL A 169 6137 4235 6961 -194 937 322 A C ATOM 1550 O AVAL A 169 5.069 -19.018 14.154 0.65 44.25 A O ANISOU 1550 O AVAL A 169 5930 4233 6651 -153 864 298 A O ATOM 1551 O BVAL A 169 5.065 -19.019 14.148 0.35 44.45 A O ANISOU 1551 O BVAL A 169 5954 4257 6676 -154 863 297 A O ATOM 1552 CB AVAL A 169 2.260 -20.772 13.824 0.65 50.34 A C ANISOU 1552 CB AVAL A 169 6547 4610 7970 -450 963 282 A C ATOM 1553 CB BVAL A 169 2.257 -20.767 13.836 0.35 50.27 A C ANISOU 1553 CB BVAL A 169 6538 4602 7961 -449 964 283 A C ATOM 1554 CG1AVAL A 169 2.016 -19.564 14.688 0.65 45.16 A C ANISOU 1554 CG1AVAL A 169 5818 4108 7231 -404 1015 357 A C ATOM 1555 CG1BVAL A 169 1.271 -21.426 12.882 0.35 51.93 A C ANISOU 1555 CG1BVAL A 169 6673 4658 8399 -606 884 178 A C ATOM 1556 CG2AVAL A 169 1.217 -20.859 12.723 0.65 55.59 A C ANISOU 1556 CG2AVAL A 169 7099 5198 8822 -604 835 156 A C ATOM 1557 CG2BVAL A 169 2.263 -21.493 15.173 0.35 46.38 A C ANISOU 1557 CG2BVAL A 169 6105 4019 7497 -394 1173 446 A C ATOM 1558 N GLU A 170 5.173 -21.036 15.126 1.00 48.62 A N ANISOU 1558 N GLU A 170 6615 4543 7317 -109 1070 438 A N ATOM 1559 CA GLU A 170 6.121 -20.547 16.124 1.00 47.12 A C ANISOU 1559 CA GLU A 170 6484 4491 6927 36 1116 533 A C ATOM 1560 C GLU A 170 7.409 -20.046 15.490 1.00 48.69 A C ANISOU 1560 C GLU A 170 6718 4826 6954 120 990 460 A C ATOM 1561 O GLU A 170 8.016 -19.089 15.984 1.00 49.19 A O ANISOU 1561 O GLU A 170 6772 5054 6863 193 960 483 A O ATOM 1562 CB GLU A 170 6.438 -21.646 17.127 1.00 52.16 A C ANISOU 1562 CB GLU A 170 7234 5019 7565 124 1266 674 A C ATOM 1563 CG GLU A 170 5.261 -22.008 17.958 1.00 72.45 A C ANISOU 1563 CG GLU A 170 9772 7474 10280 59 1423 777 A C ATOM 1564 CD GLU A 170 5.639 -22.161 19.390 1.00 97.52 A C ANISOU 1564 CD GLU A 170 13043 10681 13329 190 1563 944 A C ATOM 1565 OE1 GLU A 170 6.430 -23.078 19.701 1.00121.28 A O ANISOU 1565 OE1 GLU A 170 16173 13621 16287 292 1610 1019 A O ATOM 1566 OE2 GLU A 170 5.134 -21.389 20.232 1.00 88.75 A O ANISOU 1566 OE2 GLU A 170 11896 9660 12165 200 1632 1004 A O ATOM 1567 N GLU A 171 7.845 -20.679 14.406 1.00 47.39 A N ANISOU 1567 N GLU A 171 6596 4593 6818 109 922 368 A N ATOM 1568 CA AGLU A 171 9.076 -20.241 13.763 0.44 45.43 A C ANISOU 1568 CA AGLU A 171 6373 4468 6418 191 826 305 A C ATOM 1569 CA BGLU A 171 9.072 -20.259 13.738 0.56 45.35 A C ANISOU 1569 CA BGLU A 171 6365 4457 6411 190 825 303 A C ATOM 1570 C GLU A 171 8.872 -18.955 12.978 1.00 50.08 A C ANISOU 1570 C GLU A 171 6876 5192 6961 126 704 208 A C ATOM 1571 O GLU A 171 9.776 -18.113 12.930 1.00 45.79 A O ANISOU 1571 O GLU A 171 6321 4800 6277 192 650 200 A O ATOM 1572 CB AGLU A 171 9.608 -21.346 12.854 0.44 55.27 A C ANISOU 1572 CB AGLU A 171 7706 5593 7702 215 813 239 A C ATOM 1573 CB BGLU A 171 9.542 -21.360 12.787 0.56 55.24 A C ANISOU 1573 CB BGLU A 171 7701 5582 7707 206 809 232 A C ATOM 1574 CG AGLU A 171 10.385 -22.418 13.596 0.44 63.93 A C ANISOU 1574 CG AGLU A 171 8903 6606 8781 341 917 344 A C ATOM 1575 CG BGLU A 171 10.962 -21.834 13.014 0.56 70.83 A C ANISOU 1575 CG BGLU A 171 9756 7589 9568 364 840 280 A C ATOM 1576 CD AGLU A 171 11.719 -22.718 12.942 0.44 76.14 A C ANISOU 1576 CD AGLU A 171 10508 8190 10231 456 880 299 A C ATOM 1577 CD BGLU A 171 11.166 -23.260 12.541 0.56 74.84 A C ANISOU 1577 CD BGLU A 171 10368 7904 10164 392 890 256 A C ATOM 1578 OE1AGLU A 171 12.681 -21.951 13.170 0.44 75.11 A O ANISOU 1578 OE1AGLU A 171 10344 8234 9960 546 839 322 A O ATOM 1579 OE1BGLU A 171 11.241 -23.469 11.311 0.56 67.00 A O ANISOU 1579 OE1BGLU A 171 9402 6866 9188 354 824 126 A O ATOM 1580 OE2AGLU A 171 11.804 -23.718 12.197 0.44 78.54 A O ANISOU 1580 OE2AGLU A 171 10889 8344 10608 456 894 235 A O ATOM 1581 OE2BGLU A 171 11.242 -24.169 13.397 0.56 74.13 A O ANISOU 1581 OE2BGLU A 171 10345 7701 10120 456 999 367 A O ATOM 1582 N VAL A 172 7.696 -18.775 12.376 1.00 42.78 A N ANISOU 1582 N VAL A 172 5885 4212 6160 -1 657 141 A N ATOM 1583 CA VAL A 172 7.387 -17.526 11.688 1.00 41.54 A C ANISOU 1583 CA VAL A 172 5646 4174 5963 -56 544 66 A C ATOM 1584 C VAL A 172 7.456 -16.355 12.660 1.00 40.90 A C ANISOU 1584 C VAL A 172 5511 4232 5797 -16 570 137 A C ATOM 1585 O VAL A 172 8.050 -15.313 12.364 1.00 40.12 A O ANISOU 1585 O VAL A 172 5392 4268 5583 13 498 105 A O ATOM 1586 CB VAL A 172 6.001 -17.609 11.022 1.00 43.19 A C ANISOU 1586 CB VAL A 172 5779 4292 6338 -193 486 -3 A C ATOM 1587 CG1 VAL A 172 5.662 -16.265 10.368 1.00 42.43 A C ANISOU 1587 CG1 VAL A 172 5603 4324 6197 -232 368 -63 A C ATOM 1588 CG2 VAL A 172 5.931 -18.756 10.018 1.00 48.07 A C ANISOU 1588 CG2 VAL A 172 6463 4765 7034 -240 440 -97 A C ATOM 1589 N VAL A 173 6.804 -16.493 13.819 1.00 39.18 A N ANISOU 1589 N VAL A 173 5274 3976 5638 -18 680 230 A N ATOM 1590 CA VAL A 173 6.809 -15.412 14.801 1.00 38.69 A C ANISOU 1590 CA VAL A 173 5179 4035 5486 25 713 287 A C ATOM 1591 C VAL A 173 8.227 -15.163 15.306 1.00 41.03 A C ANISOU 1591 C VAL A 173 5544 4445 5602 145 702 320 A C ATOM 1592 O VAL A 173 8.617 -14.017 15.557 1.00 40.62 A O ANISOU 1592 O VAL A 173 5465 4522 5445 172 654 307 A O ATOM 1593 CB VAL A 173 5.823 -15.738 15.945 1.00 43.28 A C ANISOU 1593 CB VAL A 173 5743 4542 6160 9 856 386 A C ATOM 1594 CG1 VAL A 173 5.912 -14.701 17.063 1.00 46.92 A C ANISOU 1594 CG1 VAL A 173 6203 5125 6500 75 904 442 A C ATOM 1595 CG2 VAL A 173 4.395 -15.799 15.405 1.00 44.14 A C ANISOU 1595 CG2 VAL A 173 5743 4558 6470 -120 853 347 A C ATOM 1596 N SER A 174 9.036 -16.216 15.422 1.00 43.64 A N ANISOU 1596 N SER A 174 5956 4723 5903 219 737 357 A N ATOM 1597 CA ASER A 174 10.409 -16.037 15.876 0.90 46.07 A C ANISOU 1597 CA ASER A 174 6309 5141 6055 338 713 390 A C ATOM 1598 CA BSER A 174 10.413 -16.041 15.874 0.10 46.15 A C ANISOU 1598 CA BSER A 174 6319 5150 6065 338 713 390 A C ATOM 1599 C SER A 174 11.216 -15.196 14.890 1.00 46.20 A C ANISOU 1599 C SER A 174 6283 5269 6002 333 595 299 A C ATOM 1600 O SER A 174 12.005 -14.336 15.298 1.00 42.93 A O ANISOU 1600 O SER A 174 5849 4987 5477 384 551 305 A O ATOM 1601 CB ASER A 174 11.060 -17.406 16.088 0.90 52.62 A C ANISOU 1601 CB ASER A 174 7227 5877 6889 425 774 451 A C ATOM 1602 CB BSER A 174 11.074 -17.405 16.076 0.10 52.52 A C ANISOU 1602 CB BSER A 174 7214 5865 6876 426 773 450 A C ATOM 1603 OG ASER A 174 12.385 -17.264 16.555 0.90 58.45 A O ANISOU 1603 OG ASER A 174 7991 6728 7490 549 742 488 A O ATOM 1604 OG BSER A 174 12.355 -17.270 16.665 0.10 57.94 A O ANISOU 1604 OG BSER A 174 7929 6662 7422 552 748 497 A O ATOM 1605 N VAL A 175 11.014 -15.414 13.587 1.00 40.99 A N ANISOU 1605 N VAL A 175 5613 4555 5407 270 545 213 A N ATOM 1606 CA VAL A 175 11.730 -14.641 12.571 1.00 41.31 A C ANISOU 1606 CA VAL A 175 5624 4692 5379 266 453 137 A C ATOM 1607 C VAL A 175 11.341 -13.169 12.638 1.00 42.56 A C ANISOU 1607 C VAL A 175 5710 4953 5508 213 399 116 A C ATOM 1608 O VAL A 175 12.200 -12.278 12.658 1.00 38.42 A O ANISOU 1608 O VAL A 175 5159 4544 4894 245 355 109 A O ATOM 1609 CB VAL A 175 11.466 -15.229 11.171 1.00 43.49 A C ANISOU 1609 CB VAL A 175 5929 4881 5713 215 414 49 A C ATOM 1610 CG1 VAL A 175 11.988 -14.284 10.080 1.00 46.53 A C ANISOU 1610 CG1 VAL A 175 6289 5368 6021 202 331 -21 A C ATOM 1611 CG2 VAL A 175 12.104 -16.610 11.067 1.00 47.66 A C ANISOU 1611 CG2 VAL A 175 6541 5312 6255 287 470 60 A C ATOM 1612 N VAL A 176 10.038 -12.879 12.664 1.00 38.23 A N ANISOU 1612 N VAL A 176 5122 4355 5049 130 402 105 A N ATOM 1613 CA VAL A 176 9.646 -11.474 12.628 1.00 34.88 A C ANISOU 1613 CA VAL A 176 4633 4015 4607 89 351 82 A C ATOM 1614 C VAL A 176 10.066 -10.773 13.915 1.00 36.17 A C ANISOU 1614 C VAL A 176 4795 4262 4685 145 386 136 A C ATOM 1615 O VAL A 176 10.513 -9.618 13.890 1.00 36.78 A O ANISOU 1615 O VAL A 176 4844 4434 4697 146 333 111 A O ATOM 1616 CB VAL A 176 8.136 -11.337 12.338 1.00 39.56 A C ANISOU 1616 CB VAL A 176 5167 4535 5327 -2 343 61 A C ATOM 1617 CG1 VAL A 176 7.300 -11.786 13.494 1.00 48.50 A C ANISOU 1617 CG1 VAL A 176 6288 5603 6536 -5 450 131 A C ATOM 1618 CG2 VAL A 176 7.801 -9.888 11.972 1.00 47.90 A C ANISOU 1618 CG2 VAL A 176 6162 5669 6367 -36 274 27 A C ATOM 1619 N ASN A 177 9.964 -11.457 15.053 1.00 37.32 A N ANISOU 1619 N ASN A 177 4982 4373 4824 195 473 208 A N ATOM 1620 CA ASN A 177 10.370 -10.836 16.308 1.00 38.65 A C ANISOU 1620 CA ASN A 177 5170 4626 4887 258 497 252 A C ATOM 1621 C ASN A 177 11.880 -10.606 16.345 1.00 39.96 A C ANISOU 1621 C ASN A 177 5350 4895 4938 327 430 243 A C ATOM 1622 O ASN A 177 12.339 -9.601 16.899 1.00 40.24 A O ANISOU 1622 O ASN A 177 5372 5026 4891 345 387 228 A O ATOM 1623 CB ASN A 177 9.910 -11.690 17.488 1.00 43.28 A C ANISOU 1623 CB ASN A 177 5816 5151 5478 307 613 343 A C ATOM 1624 CG ASN A 177 8.410 -11.565 17.754 1.00 40.49 A C ANISOU 1624 CG ASN A 177 5425 4724 5236 241 696 361 A C ATOM 1625 ND2 ASN A 177 7.920 -12.352 18.698 1.00 48.09 A N ANISOU 1625 ND2 ASN A 177 6436 5617 6220 274 821 451 A N ATOM 1626 OD1 ASN A 177 7.709 -10.777 17.118 1.00 42.62 A O ANISOU 1626 OD1 ASN A 177 5620 4998 5578 167 653 304 A O ATOM 1627 N SER A 178 12.665 -11.513 15.751 1.00 41.03 A N ANISOU 1627 N SER A 178 5505 5008 5077 365 419 245 A N ATOM 1628 CA SER A 178 14.110 -11.300 15.665 1.00 39.57 A C ANISOU 1628 CA SER A 178 5304 4922 4809 429 359 237 A C ATOM 1629 C SER A 178 14.431 -10.070 14.822 1.00 40.79 A C ANISOU 1629 C SER A 178 5392 5151 4956 368 282 166 A C ATOM 1630 O SER A 178 15.290 -9.262 15.182 1.00 40.13 A O ANISOU 1630 O SER A 178 5272 5168 4810 388 229 156 A O ATOM 1631 CB SER A 178 14.793 -12.528 15.060 1.00 43.41 A C ANISOU 1631 CB SER A 178 5821 5356 5318 486 380 250 A C ATOM 1632 OG SER A 178 14.696 -13.637 15.923 1.00 50.06 A O ANISOU 1632 OG SER A 178 6731 6129 6160 559 451 330 A O ATOM 1633 N TYR A 179 13.739 -9.918 13.695 1.00 37.71 A N ANISOU 1633 N TYR A 179 4986 4708 4632 291 272 117 A N ATOM 1634 CA TYR A 179 13.900 -8.736 12.851 1.00 36.06 A C ANISOU 1634 CA TYR A 179 4729 4556 4417 234 211 65 A C ATOM 1635 C TYR A 179 13.545 -7.457 13.601 1.00 39.10 A C ANISOU 1635 C TYR A 179 5083 4989 4782 203 188 59 A C ATOM 1636 O TYR A 179 14.290 -6.469 13.553 1.00 37.49 A O ANISOU 1636 O TYR A 179 4843 4861 4542 193 141 37 A O ATOM 1637 CB TYR A 179 13.032 -8.915 11.613 1.00 37.85 A C ANISOU 1637 CB TYR A 179 4964 4710 4708 170 199 22 A C ATOM 1638 CG TYR A 179 12.921 -7.711 10.734 1.00 37.84 A C ANISOU 1638 CG TYR A 179 4928 4750 4701 114 142 -17 A C ATOM 1639 CD1 TYR A 179 13.987 -7.292 9.952 1.00 37.74 A C ANISOU 1639 CD1 TYR A 179 4904 4798 4638 126 121 -31 A C ATOM 1640 CD2 TYR A 179 11.742 -6.990 10.679 1.00 40.02 A C ANISOU 1640 CD2 TYR A 179 5180 4997 5028 55 120 -29 A C ATOM 1641 CE1 TYR A 179 13.864 -6.196 9.135 1.00 38.98 A C ANISOU 1641 CE1 TYR A 179 5041 4980 4787 77 82 -52 A C ATOM 1642 CE2 TYR A 179 11.618 -5.907 9.872 1.00 40.06 A C ANISOU 1642 CE2 TYR A 179 5163 5030 5027 14 68 -53 A C ATOM 1643 CZ TYR A 179 12.679 -5.500 9.115 1.00 39.40 A C ANISOU 1643 CZ TYR A 179 5083 5001 4885 24 51 -62 A C ATOM 1644 OH TYR A 179 12.512 -4.404 8.298 1.00 43.38 A O ANISOU 1644 OH TYR A 179 5577 5523 5383 -14 11 -71 A O ATOM 1645 N PHE A 180 12.415 -7.453 14.313 1.00 37.43 A N ANISOU 1645 N PHE A 180 4888 4730 4605 187 230 77 A N ATOM 1646 CA PHE A 180 12.006 -6.252 15.028 1.00 36.14 A C ANISOU 1646 CA PHE A 180 4709 4601 4423 168 221 64 A C ATOM 1647 C PHE A 180 12.985 -5.906 16.145 1.00 37.54 A C ANISOU 1647 C PHE A 180 4905 4860 4497 227 201 73 A C ATOM 1648 O PHE A 180 13.209 -4.723 16.439 1.00 39.10 A O ANISOU 1648 O PHE A 180 5087 5106 4664 206 158 35 A O ATOM 1649 CB PHE A 180 10.595 -6.428 15.600 1.00 35.44 A C ANISOU 1649 CB PHE A 180 4629 4442 4395 153 293 89 A C ATOM 1650 CG PHE A 180 9.487 -6.382 14.572 1.00 34.85 A C ANISOU 1650 CG PHE A 180 4508 4300 4435 83 283 66 A C ATOM 1651 CD1 PHE A 180 9.632 -5.708 13.362 1.00 37.10 A C ANISOU 1651 CD1 PHE A 180 4760 4601 4734 39 205 21 A C ATOM 1652 CD2 PHE A 180 8.274 -6.991 14.842 1.00 41.76 A C ANISOU 1652 CD2 PHE A 180 5367 5093 5405 63 351 95 A C ATOM 1653 CE1 PHE A 180 8.596 -5.663 12.436 1.00 39.22 A C ANISOU 1653 CE1 PHE A 180 4992 4816 5095 -16 175 1 A C ATOM 1654 CE2 PHE A 180 7.236 -6.940 13.920 1.00 40.85 A C ANISOU 1654 CE2 PHE A 180 5193 4922 5405 -3 320 69 A C ATOM 1655 CZ PHE A 180 7.387 -6.273 12.732 1.00 39.07 A C ANISOU 1655 CZ PHE A 180 4944 4723 5179 -38 224 20 A C ATOM 1656 N ASER A 181 13.580 -6.920 16.776 0.64 37.66 A N ANISOU 1656 N ASER A 181 4959 4887 4461 301 224 119 A N ATOM 1657 N BSER A 181 13.553 -6.922 16.796 0.36 37.87 A N ANISOU 1657 N BSER A 181 4987 4913 4488 301 225 120 A N ATOM 1658 CA ASER A 181 14.542 -6.679 17.845 0.64 41.84 A C ANISOU 1658 CA ASER A 181 5508 5505 4886 366 182 128 A C ATOM 1659 CA BSER A 181 14.539 -6.676 17.841 0.36 41.90 A C ANISOU 1659 CA BSER A 181 5515 5512 4893 366 182 128 A C ATOM 1660 C ASER A 181 15.817 -6.038 17.315 0.64 39.21 A C ANISOU 1660 C ASER A 181 5105 5252 4540 352 91 85 A C ATOM 1661 C BSER A 181 15.771 -5.987 17.271 0.36 39.31 A C ANISOU 1661 C BSER A 181 5117 5263 4556 346 91 83 A C ATOM 1662 O ASER A 181 16.365 -5.121 17.938 0.64 41.45 A O ANISOU 1662 O ASER A 181 5373 5605 4770 348 25 50 A O ATOM 1663 O BSER A 181 16.234 -4.971 17.803 0.36 41.70 A O ANISOU 1663 O BSER A 181 5401 5629 4815 333 28 42 A O ATOM 1664 CB ASER A 181 14.864 -7.996 18.548 0.64 43.43 A C ANISOU 1664 CB ASER A 181 5767 5694 5039 462 224 203 A C ATOM 1665 CB BSER A 181 14.921 -7.997 18.510 0.36 43.42 A C ANISOU 1665 CB BSER A 181 5763 5696 5038 462 221 202 A C ATOM 1666 OG ASER A 181 13.758 -8.434 19.313 0.64 49.90 A O ANISOU 1666 OG ASER A 181 6655 6448 5858 478 320 252 A O ATOM 1667 OG BSER A 181 15.839 -7.781 19.566 0.36 46.59 A O ANISOU 1667 OG BSER A 181 6184 6191 5326 536 161 211 A O ATOM 1668 N VAL A 182 16.312 -6.532 16.180 1.00 38.10 A N ANISOU 1668 N VAL A 182 4925 5100 4451 343 90 87 A N ATOM 1669 CA VAL A 182 17.468 -5.928 15.515 1.00 39.48 A C ANISOU 1669 CA VAL A 182 5021 5343 4636 322 32 56 A C ATOM 1670 C VAL A 182 17.202 -4.466 15.167 1.00 42.36 A C ANISOU 1670 C VAL A 182 5351 5714 5028 231 -3 3 A C ATOM 1671 O VAL A 182 18.013 -3.584 15.471 1.00 40.83 A O ANISOU 1671 O VAL A 182 5107 5584 4822 210 -64 -27 A O ATOM 1672 CB VAL A 182 17.828 -6.733 14.253 1.00 42.84 A C ANISOU 1672 CB VAL A 182 5430 5739 5107 333 68 67 A C ATOM 1673 CG1 VAL A 182 18.816 -5.960 13.372 1.00 47.78 A C ANISOU 1673 CG1 VAL A 182 5975 6424 5758 295 38 40 A C ATOM 1674 CG2 VAL A 182 18.385 -8.082 14.655 1.00 47.42 A C ANISOU 1674 CG2 VAL A 182 6035 6315 5665 435 95 117 A C ATOM 1675 N CYS A 183 16.087 -4.190 14.485 1.00 37.86 A N ANISOU 1675 N CYS A 183 4805 5075 4507 176 30 -8 A N ATOM 1676 CA CYS A 183 15.838 -2.814 14.063 1.00 36.79 A C ANISOU 1676 CA CYS A 183 4642 4935 4403 101 2 -47 A C ATOM 1677 C CYS A 183 15.623 -1.891 15.252 1.00 38.55 A C ANISOU 1677 C CYS A 183 4881 5172 4592 95 -24 -77 A C ATOM 1678 O CYS A 183 16.122 -0.760 15.256 1.00 38.19 A O ANISOU 1678 O CYS A 183 4804 5150 4557 49 -71 -116 A O ATOM 1679 CB CYS A 183 14.626 -2.719 13.124 1.00 39.24 A C ANISOU 1679 CB CYS A 183 4971 5170 4770 58 29 -47 A C ATOM 1680 SG CYS A 183 14.711 -3.652 11.606 1.00 40.92 A S ANISOU 1680 SG CYS A 183 5190 5354 5003 59 47 -35 A S ATOM 1681 N THR A 184 14.851 -2.336 16.251 1.00 37.10 A N ANISOU 1681 N THR A 184 4757 4967 4372 138 14 -62 A N ATOM 1682 CA THR A 184 14.554 -1.480 17.391 1.00 39.17 A C ANISOU 1682 CA THR A 184 5059 5240 4586 144 3 -98 A C ATOM 1683 C THR A 184 15.824 -1.086 18.131 1.00 39.35 A C ANISOU 1683 C THR A 184 5068 5345 4538 161 -82 -134 A C ATOM 1684 O THR A 184 15.987 0.071 18.531 1.00 38.73 A O ANISOU 1684 O THR A 184 4992 5274 4449 124 -131 -196 A O ATOM 1685 CB THR A 184 13.597 -2.187 18.355 1.00 41.58 A C ANISOU 1685 CB THR A 184 5434 5513 4849 203 81 -61 A C ATOM 1686 CG2 THR A 184 13.481 -1.397 19.644 1.00 50.72 A C ANISOU 1686 CG2 THR A 184 6655 6696 5921 231 74 -101 A C ATOM 1687 OG1 THR A 184 12.303 -2.279 17.750 1.00 44.04 A O ANISOU 1687 OG1 THR A 184 5736 5745 5252 170 148 -43 A O ATOM 1688 N ALA A 185 16.730 -2.044 18.343 1.00 38.89 A N ANISOU 1688 N ALA A 185 4995 5344 4437 220 -107 -98 A N ATOM 1689 CA ALA A 185 17.935 -1.749 19.109 1.00 42.99 A C ANISOU 1689 CA ALA A 185 5488 5952 4894 244 -207 -130 A C ATOM 1690 C ALA A 185 18.768 -0.671 18.424 1.00 40.87 A C ANISOU 1690 C ALA A 185 5124 5705 4700 157 -274 -183 A C ATOM 1691 O ALA A 185 19.284 0.241 19.085 1.00 41.04 A O ANISOU 1691 O ALA A 185 5133 5761 4698 126 -358 -249 A O ATOM 1692 CB ALA A 185 18.744 -3.031 19.318 1.00 42.06 A C ANISOU 1692 CB ALA A 185 5357 5888 4737 334 -220 -68 A C ATOM 1693 N ILE A 186 18.888 -0.744 17.099 1.00 38.59 A N ANISOU 1693 N ILE A 186 4774 5388 4501 113 -234 -157 A N ATOM 1694 CA ILE A 186 19.751 0.185 16.378 1.00 37.60 A C ANISOU 1694 CA ILE A 186 4554 5279 4453 33 -273 -186 A C ATOM 1695 C ILE A 186 19.087 1.550 16.224 1.00 38.66 A C ANISOU 1695 C ILE A 186 4714 5345 4629 -50 -271 -235 A C ATOM 1696 O ILE A 186 19.732 2.588 16.404 1.00 38.03 A O ANISOU 1696 O ILE A 186 4589 5274 4588 -115 -332 -287 A O ATOM 1697 CB ILE A 186 20.132 -0.436 15.026 1.00 36.81 A C ANISOU 1697 CB ILE A 186 4400 5176 4411 33 -213 -134 A C ATOM 1698 CG1 ILE A 186 21.112 -1.597 15.284 1.00 44.41 A C ANISOU 1698 CG1 ILE A 186 5316 6210 5348 119 -228 -96 A C ATOM 1699 CG2 ILE A 186 20.755 0.621 14.121 1.00 43.62 A C ANISOU 1699 CG2 ILE A 186 5183 6032 5358 -56 -215 -147 A C ATOM 1700 CD1 ILE A 186 21.396 -2.466 14.090 1.00 45.73 A C ANISOU 1700 CD1 ILE A 186 5458 6366 5550 150 -153 -48 A C ATOM 1701 N ILE A 187 17.800 1.575 15.892 1.00 37.18 A N ANISOU 1701 N ILE A 187 4594 5085 4449 -51 -205 -219 A N ATOM 1702 CA ILE A 187 17.086 2.850 15.784 1.00 38.62 A C ANISOU 1702 CA ILE A 187 4805 5195 4675 -111 -199 -258 A C ATOM 1703 C ILE A 187 17.138 3.607 17.105 1.00 38.81 A C ANISOU 1703 C ILE A 187 4873 5225 4649 -111 -253 -333 A C ATOM 1704 O ILE A 187 17.394 4.818 17.144 1.00 40.22 A O ANISOU 1704 O ILE A 187 5041 5367 4872 -177 -291 -389 A O ATOM 1705 CB ILE A 187 15.636 2.616 15.325 1.00 36.74 A C ANISOU 1705 CB ILE A 187 4618 4887 4455 -93 -127 -224 A C ATOM 1706 CG1 ILE A 187 15.616 2.195 13.850 1.00 38.46 A C ANISOU 1706 CG1 ILE A 187 4802 5090 4721 -111 -97 -172 A C ATOM 1707 CG2 ILE A 187 14.792 3.884 15.562 1.00 39.94 A C ANISOU 1707 CG2 ILE A 187 5060 5219 4895 -124 -119 -265 A C ATOM 1708 CD1 ILE A 187 14.293 1.559 13.413 1.00 44.21 A C ANISOU 1708 CD1 ILE A 187 5566 5767 5465 -85 -49 -140 A C ATOM 1709 N THR A 188 16.894 2.902 18.215 1.00 39.19 A N ANISOU 1709 N THR A 188 4982 5309 4597 -34 -253 -335 A N ATOM 1710 CA THR A 188 16.899 3.552 19.520 1.00 40.59 A C ANISOU 1710 CA THR A 188 5230 5499 4696 -18 -303 -413 A C ATOM 1711 C THR A 188 18.292 4.071 19.872 1.00 42.21 A C ANISOU 1711 C THR A 188 5374 5764 4898 -61 -427 -476 A C ATOM 1712 O THR A 188 18.433 5.171 20.421 1.00 40.33 A O ANISOU 1712 O THR A 188 5166 5501 4658 -107 -486 -566 A O ATOM 1713 CB THR A 188 16.383 2.571 20.578 1.00 42.99 A C ANISOU 1713 CB THR A 188 5622 5836 4878 86 -264 -383 A C ATOM 1714 CG2 THR A 188 16.378 3.216 21.960 1.00 54.72 A C ANISOU 1714 CG2 THR A 188 7205 7339 6248 118 -312 -466 A C ATOM 1715 OG1 THR A 188 15.037 2.171 20.241 1.00 46.91 A O ANISOU 1715 OG1 THR A 188 6152 6263 5407 109 -145 -328 A O ATOM 1716 N ARG A 189 19.328 3.303 19.538 1.00 41.25 A N ANISOU 1716 N ARG A 189 5163 5719 4790 -48 -468 -433 A N ATOM 1717 CA ARG A 189 20.706 3.719 19.788 1.00 43.25 A C ANISOU 1717 CA ARG A 189 5323 6039 5071 -92 -590 -484 A C ATOM 1718 C ARG A 189 21.065 5.005 19.054 1.00 43.13 A C ANISOU 1718 C ARG A 189 5236 5962 5188 -217 -604 -529 A C ATOM 1719 O ARG A 189 21.880 5.794 19.550 1.00 47.59 A O ANISOU 1719 O ARG A 189 5756 6545 5783 -279 -711 -610 A O ATOM 1720 CB ARG A 189 21.636 2.582 19.369 1.00 47.62 A C ANISOU 1720 CB ARG A 189 5777 6675 5639 -43 -599 -410 A C ATOM 1721 CG ARG A 189 23.086 2.755 19.713 1.00 59.62 A C ANISOU 1721 CG ARG A 189 7177 8284 7191 -65 -729 -448 A C ATOM 1722 CD ARG A 189 23.814 1.455 19.384 1.00 58.83 A C ANISOU 1722 CD ARG A 189 6996 8261 7094 20 -716 -362 A C ATOM 1723 NE ARG A 189 23.316 0.359 20.209 1.00 48.16 A N ANISOU 1723 NE ARG A 189 5755 6939 5606 147 -704 -318 A N ATOM 1724 CZ ARG A 189 23.023 -0.858 19.771 1.00 51.10 A C ANISOU 1724 CZ ARG A 189 6152 7300 5964 228 -610 -228 A C ATOM 1725 NH1 ARG A 189 23.202 -1.203 18.508 1.00 50.44 A N ANISOU 1725 NH1 ARG A 189 5996 7189 5979 206 -527 -180 A N ATOM 1726 NH2 ARG A 189 22.548 -1.758 20.629 1.00 54.31 A N ANISOU 1726 NH2 ARG A 189 6667 7718 6251 335 -595 -187 A N ATOM 1727 N GLN A 190 20.472 5.236 17.882 1.00 41.40 A N ANISOU 1727 N GLN A 190 5010 5667 5051 -256 -503 -476 A N ATOM 1728 CA GLN A 190 20.711 6.439 17.102 1.00 41.96 A C ANISOU 1728 CA GLN A 190 5032 5665 5247 -365 -493 -495 A C ATOM 1729 C GLN A 190 19.708 7.551 17.392 1.00 43.38 A C ANISOU 1729 C GLN A 190 5312 5735 5434 -396 -473 -552 A C ATOM 1730 O GLN A 190 19.711 8.563 16.690 1.00 43.58 A O ANISOU 1730 O GLN A 190 5319 5676 5564 -477 -448 -553 A O ATOM 1731 CB GLN A 190 20.696 6.123 15.610 1.00 44.22 A C ANISOU 1731 CB GLN A 190 5266 5932 5605 -380 -398 -399 A C ATOM 1732 CG GLN A 190 21.836 5.251 15.145 1.00 45.12 A C ANISOU 1732 CG GLN A 190 5267 6136 5741 -362 -400 -347 A C ATOM 1733 CD GLN A 190 23.156 5.996 15.108 1.00 48.43 A C ANISOU 1733 CD GLN A 190 5555 6579 6266 -452 -460 -378 A C ATOM 1734 NE2 GLN A 190 24.244 5.270 15.272 1.00 49.95 A N ANISOU 1734 NE2 GLN A 190 5637 6872 6469 -420 -503 -363 A N ATOM 1735 OE1 GLN A 190 23.192 7.214 14.945 1.00 50.92 A O ANISOU 1735 OE1 GLN A 190 5863 6817 6667 -549 -466 -415 A O ATOM 1736 N GLY A 191 18.883 7.409 18.426 1.00 42.20 A N ANISOU 1736 N GLY A 191 5273 5582 5179 -327 -475 -594 A N ATOM 1737 CA GLY A 191 18.038 8.494 18.857 1.00 44.76 A C ANISOU 1737 CA GLY A 191 5692 5806 5509 -343 -456 -662 A C ATOM 1738 C GLY A 191 16.697 8.550 18.171 1.00 45.16 A C ANISOU 1738 C GLY A 191 5788 5776 5592 -312 -343 -600 A C ATOM 1739 O GLY A 191 15.972 9.540 18.343 1.00 45.26 A O ANISOU 1739 O GLY A 191 5866 5693 5638 -323 -315 -645 A O ATOM 1740 N GLY A 192 16.347 7.511 17.395 1.00 40.96 A N ANISOU 1740 N GLY A 192 5224 5280 5061 -271 -284 -503 A N ATOM 1741 CA GLY A 192 15.036 7.419 16.788 1.00 41.54 A C ANISOU 1741 CA GLY A 192 5329 5291 5164 -238 -198 -447 A C ATOM 1742 C GLY A 192 13.994 6.786 17.706 1.00 39.68 A C ANISOU 1742 C GLY A 192 5163 5063 4849 -150 -146 -448 A C ATOM 1743 O GLY A 192 14.298 6.214 18.744 1.00 40.37 A O ANISOU 1743 O GLY A 192 5288 5213 4837 -103 -167 -474 A O ATOM 1744 N GLU A 193 12.739 6.897 17.286 1.00 37.63 A N ANISOU 1744 N GLU A 193 4918 4739 4641 -125 -74 -411 A N ATOM 1745 CA GLU A 193 11.587 6.381 18.017 1.00 40.35 A C ANISOU 1745 CA GLU A 193 5310 5074 4946 -50 2 -399 A C ATOM 1746 C GLU A 193 10.885 5.362 17.134 1.00 40.26 A C ANISOU 1746 C GLU A 193 5246 5066 4984 -35 45 -312 A C ATOM 1747 O GLU A 193 10.451 5.692 16.029 1.00 40.36 A O ANISOU 1747 O GLU A 193 5217 5034 5083 -64 43 -278 A O ATOM 1748 CB GLU A 193 10.649 7.534 18.386 1.00 44.50 A C ANISOU 1748 CB GLU A 193 5883 5510 5514 -32 48 -443 A C ATOM 1749 CG GLU A 193 9.345 7.142 19.057 1.00 62.17 A C ANISOU 1749 CG GLU A 193 8154 7729 7740 47 152 -423 A C ATOM 1750 CD GLU A 193 9.510 6.794 20.527 1.00 67.22 A C ANISOU 1750 CD GLU A 193 8884 8416 8242 108 181 -467 A C ATOM 1751 OE1 GLU A 193 8.482 6.531 21.181 1.00 73.70 A O ANISOU 1751 OE1 GLU A 193 9738 9218 9045 177 288 -448 A O ATOM 1752 OE2 GLU A 193 10.652 6.810 21.030 1.00 60.40 A O ANISOU 1752 OE2 GLU A 193 8054 7608 7287 91 97 -519 A O ATOM 1753 N VAL A 194 10.774 4.127 17.606 1.00 36.56 A N ANISOU 1753 N VAL A 194 4787 4644 4460 11 79 -277 A N ATOM 1754 CA VAL A 194 9.973 3.141 16.890 1.00 35.68 A C ANISOU 1754 CA VAL A 194 4632 4517 4406 20 122 -209 A C ATOM 1755 C VAL A 194 8.528 3.369 17.312 1.00 38.93 A C ANISOU 1755 C VAL A 194 5049 4870 4873 56 206 -200 A C ATOM 1756 O VAL A 194 8.191 3.241 18.492 1.00 41.67 A O ANISOU 1756 O VAL A 194 5449 5222 5162 108 274 -210 A O ATOM 1757 CB VAL A 194 10.433 1.712 17.193 1.00 46.64 A C ANISOU 1757 CB VAL A 194 6029 5958 5734 52 134 -171 A C ATOM 1758 CG1 VAL A 194 9.537 0.714 16.501 1.00 47.87 A C ANISOU 1758 CG1 VAL A 194 6147 6078 5964 51 178 -114 A C ATOM 1759 CG2 VAL A 194 11.865 1.526 16.734 1.00 43.42 A C ANISOU 1759 CG2 VAL A 194 5599 5610 5289 27 57 -178 A C ATOM 1760 N THR A 195 7.680 3.745 16.368 1.00 36.39 A N ANISOU 1760 N THR A 195 4672 4496 4659 35 205 -177 A N ATOM 1761 CA THR A 195 6.323 4.126 16.742 1.00 37.02 A C ANISOU 1761 CA THR A 195 4732 4519 4813 72 283 -169 A C ATOM 1762 C THR A 195 5.272 3.069 16.426 1.00 41.03 A C ANISOU 1762 C THR A 195 5171 5011 5407 78 330 -111 A C ATOM 1763 O THR A 195 4.251 3.005 17.120 1.00 41.53 A O ANISOU 1763 O THR A 195 5216 5044 5520 119 427 -95 A O ATOM 1764 CB THR A 195 5.949 5.460 16.079 1.00 42.88 A C ANISOU 1764 CB THR A 195 5454 5203 5635 60 250 -186 A C ATOM 1765 CG2 THR A 195 5.758 5.335 14.572 1.00 40.29 A C ANISOU 1765 CG2 THR A 195 5061 4865 5382 21 177 -141 A C ATOM 1766 OG1 THR A 195 4.751 5.962 16.682 1.00 40.83 A O ANISOU 1766 OG1 THR A 195 5182 4890 5441 114 336 -188 A O ATOM 1767 N LYS A 196 5.484 2.222 15.430 1.00 35.82 A N ANISOU 1767 N LYS A 196 4472 4366 4772 38 271 -83 A N ATOM 1768 CA LYS A 196 4.472 1.228 15.114 1.00 36.82 A C ANISOU 1768 CA LYS A 196 4530 4464 4995 30 302 -41 A C ATOM 1769 C LYS A 196 5.080 0.062 14.349 1.00 37.82 A C ANISOU 1769 C LYS A 196 4660 4611 5098 -6 247 -28 A C ATOM 1770 O LYS A 196 5.975 0.249 13.524 1.00 37.59 A O ANISOU 1770 O LYS A 196 4654 4611 5018 -30 166 -44 A O ATOM 1771 CB LYS A 196 3.362 1.871 14.276 1.00 42.12 A C ANISOU 1771 CB LYS A 196 5116 5090 5796 20 267 -31 A C ATOM 1772 CG LYS A 196 2.070 1.113 14.243 1.00 51.63 A C ANISOU 1772 CG LYS A 196 6225 6258 7136 14 311 4 A C ATOM 1773 CD LYS A 196 0.998 1.883 13.462 1.00 53.83 A C ANISOU 1773 CD LYS A 196 6407 6502 7545 17 258 12 A C ATOM 1774 CE LYS A 196 0.757 3.309 13.950 1.00 63.12 A C ANISOU 1774 CE LYS A 196 7596 7656 8729 72 299 0 A C ATOM 1775 NZ LYS A 196 -0.260 3.335 15.027 1.00 44.84 A N ANISOU 1775 NZ LYS A 196 5231 5311 6497 122 439 17 A N ATOM 1776 N PHE A 197 4.560 -1.133 14.619 1.00 36.70 A N ANISOU 1776 N PHE A 197 4496 4444 5003 -9 303 4 A N ATOM 1777 CA PHE A 197 4.798 -2.311 13.793 1.00 35.16 A C ANISOU 1777 CA PHE A 197 4297 4240 4825 -44 256 10 A C ATOM 1778 C PHE A 197 3.558 -2.546 12.938 1.00 39.96 A C ANISOU 1778 C PHE A 197 4811 4794 5576 -86 218 13 A C ATOM 1779 O PHE A 197 2.428 -2.520 13.447 1.00 37.64 A O ANISOU 1779 O PHE A 197 4447 4461 5393 -84 285 36 A O ATOM 1780 CB PHE A 197 5.071 -3.549 14.639 1.00 38.64 A C ANISOU 1780 CB PHE A 197 4779 4669 5233 -22 339 44 A C ATOM 1781 CG PHE A 197 6.260 -3.413 15.538 1.00 38.84 A C ANISOU 1781 CG PHE A 197 4890 4755 5114 29 360 44 A C ATOM 1782 CD1 PHE A 197 7.508 -3.158 15.009 1.00 38.60 A C ANISOU 1782 CD1 PHE A 197 4890 4778 4997 27 278 15 A C ATOM 1783 CD2 PHE A 197 6.116 -3.515 16.906 1.00 47.34 A C ANISOU 1783 CD2 PHE A 197 6011 5836 6141 81 460 74 A C ATOM 1784 CE1 PHE A 197 8.612 -3.028 15.839 1.00 38.25 A C ANISOU 1784 CE1 PHE A 197 4903 4795 4836 71 278 11 A C ATOM 1785 CE2 PHE A 197 7.212 -3.379 17.744 1.00 43.43 A C ANISOU 1785 CE2 PHE A 197 5596 5404 5502 133 454 68 A C ATOM 1786 CZ PHE A 197 8.451 -3.137 17.213 1.00 40.95 A C ANISOU 1786 CZ PHE A 197 5294 5146 5121 124 354 34 A C ATOM 1787 N ILE A 198 3.759 -2.773 11.646 1.00 37.87 A N ANISOU 1787 N ILE A 198 4546 4531 5312 -122 110 -12 A N ATOM 1788 CA ILE A 198 2.656 -2.935 10.700 1.00 37.87 A C ANISOU 1788 CA ILE A 198 4464 4492 5434 -162 33 -23 A C ATOM 1789 C ILE A 198 2.914 -4.250 9.967 1.00 38.58 A C ANISOU 1789 C ILE A 198 4584 4555 5520 -201 -15 -48 A C ATOM 1790 O ILE A 198 3.553 -4.281 8.913 1.00 40.72 A O ANISOU 1790 O ILE A 198 4910 4850 5710 -207 -103 -80 A O ATOM 1791 CB ILE A 198 2.535 -1.754 9.733 1.00 39.80 A C ANISOU 1791 CB ILE A 198 4695 4761 5666 -156 -70 -35 A C ATOM 1792 CG1 ILE A 198 2.431 -0.439 10.512 1.00 41.16 A C ANISOU 1792 CG1 ILE A 198 4859 4945 5837 -113 -13 -17 A C ATOM 1793 CG2 ILE A 198 1.319 -1.916 8.843 1.00 41.41 A C ANISOU 1793 CG2 ILE A 198 4805 4932 5995 -188 -166 -44 A C ATOM 1794 CD1 ILE A 198 2.727 0.811 9.696 1.00 47.29 A C ANISOU 1794 CD1 ILE A 198 5660 5740 6567 -98 -93 -18 A C ATOM 1795 N GLY A 199 2.427 -5.354 10.529 1.00 39.97 A N ANISOU 1795 N GLY A 199 4732 4672 5783 -225 55 -33 A N ATOM 1796 CA GLY A 199 2.721 -6.650 9.947 1.00 40.03 A C ANISOU 1796 CA GLY A 199 4783 4633 5791 -258 24 -62 A C ATOM 1797 C GLY A 199 4.197 -6.976 10.068 1.00 38.93 A C ANISOU 1797 C GLY A 199 4759 4533 5498 -213 52 -62 A C ATOM 1798 O GLY A 199 4.697 -7.158 11.179 1.00 39.74 A O ANISOU 1798 O GLY A 199 4896 4648 5556 -171 153 -19 A O ATOM 1799 N ASP A 200 4.901 -7.048 8.935 1.00 34.07 A N ANISOU 1799 N ASP A 200 4203 3943 4798 -213 -36 -107 A N ATOM 1800 CA ASP A 200 6.338 -7.309 8.891 1.00 34.55 A C ANISOU 1800 CA ASP A 200 4354 4048 4727 -165 -12 -108 A C ATOM 1801 C ASP A 200 7.148 -6.034 8.694 1.00 38.49 A C ANISOU 1801 C ASP A 200 4867 4635 5122 -136 -37 -102 A C ATOM 1802 O ASP A 200 8.266 -6.080 8.168 1.00 37.86 A O ANISOU 1802 O ASP A 200 4843 4597 4945 -109 -48 -113 A O ATOM 1803 CB ASP A 200 6.647 -8.289 7.763 1.00 36.14 A C ANISOU 1803 CB ASP A 200 4617 4211 4902 -177 -67 -161 A C ATOM 1804 CG ASP A 200 6.437 -7.669 6.384 1.00 35.64 A C ANISOU 1804 CG ASP A 200 4566 4177 4799 -198 -184 -208 A C ATOM 1805 OD1 ASP A 200 5.642 -6.716 6.287 1.00 37.84 A O ANISOU 1805 OD1 ASP A 200 4780 4474 5123 -218 -234 -197 A O ATOM 1806 OD2 ASP A 200 7.022 -8.131 5.388 1.00 36.49 A O ANISOU 1806 OD2 ASP A 200 4752 4285 4826 -185 -224 -252 A O ATOM 1807 N CYS A 201 6.601 -4.895 9.100 1.00 37.24 A N ANISOU 1807 N CYS A 201 4657 4497 4996 -140 -39 -83 A N ATOM 1808 CA CYS A 201 7.163 -3.591 8.776 1.00 35.28 A C ANISOU 1808 CA CYS A 201 4418 4307 4678 -128 -72 -80 A C ATOM 1809 C CYS A 201 7.364 -2.779 10.045 1.00 41.29 A C ANISOU 1809 C CYS A 201 5165 5093 5429 -104 -8 -57 A C ATOM 1810 O CYS A 201 6.523 -2.804 10.948 1.00 36.32 A O ANISOU 1810 O CYS A 201 4499 4433 4866 -99 46 -42 A O ATOM 1811 CB CYS A 201 6.237 -2.848 7.802 1.00 41.19 A C ANISOU 1811 CB CYS A 201 5133 5042 5475 -151 -158 -89 A C ATOM 1812 SG CYS A 201 6.537 -1.098 7.677 1.00 44.87 A S ANISOU 1812 SG CYS A 201 5599 5545 5903 -136 -175 -66 A S ATOM 1813 N VAL A 202 8.498 -2.082 10.117 1.00 34.46 A N ANISOU 1813 N VAL A 202 4330 4281 4481 -89 -9 -58 A N ATOM 1814 CA AVAL A 202 8.841 -1.150 11.188 0.74 34.60 A C ANISOU 1814 CA AVAL A 202 4348 4325 4474 -73 25 -57 A C ATOM 1815 CA BVAL A 202 8.758 -1.157 11.209 0.26 34.82 A C ANISOU 1815 CA BVAL A 202 4373 4349 4506 -73 26 -56 A C ATOM 1816 C VAL A 202 8.616 0.271 10.691 1.00 35.78 A C ANISOU 1816 C VAL A 202 4484 4466 4645 -92 -14 -62 A C ATOM 1817 O VAL A 202 9.182 0.648 9.658 1.00 37.22 A O ANISOU 1817 O VAL A 202 4681 4665 4797 -109 -57 -58 A O ATOM 1818 CB AVAL A 202 10.318 -1.303 11.609 0.74 37.13 A C ANISOU 1818 CB AVAL A 202 4697 4705 4706 -53 33 -61 A C ATOM 1819 CB BVAL A 202 10.129 -1.406 11.862 0.26 38.27 A C ANISOU 1819 CB BVAL A 202 4841 4842 4857 -48 45 -59 A C ATOM 1820 CG1AVAL A 202 10.712 -0.160 12.531 0.74 35.09 A C ANISOU 1820 CG1AVAL A 202 4441 4470 4421 -50 37 -78 A C ATOM 1821 CG1BVAL A 202 11.243 -1.105 10.907 0.26 42.13 A C ANISOU 1821 CG1BVAL A 202 5334 5371 5302 -63 5 -64 A C ATOM 1822 CG2AVAL A 202 10.574 -2.631 12.256 0.74 39.57 A C ANISOU 1822 CG2AVAL A 202 5027 5017 4991 -17 76 -45 A C ATOM 1823 CG2BVAL A 202 10.266 -0.590 13.154 0.26 33.27 A C ANISOU 1823 CG2BVAL A 202 4217 4227 4195 -30 70 -71 A C ATOM 1824 N MET A 203 7.839 1.068 11.433 1.00 34.61 A N ANISOU 1824 N MET A 203 4317 4290 4545 -81 14 -64 A N ATOM 1825 CA AMET A 203 7.705 2.496 11.193 0.44 35.91 A C ANISOU 1825 CA AMET A 203 4478 4432 4732 -88 -9 -69 A C ATOM 1826 CA BMET A 203 7.694 2.498 11.197 0.56 35.87 A C ANISOU 1826 CA BMET A 203 4473 4426 4728 -88 -9 -69 A C ATOM 1827 C MET A 203 8.339 3.250 12.355 1.00 37.44 A C ANISOU 1827 C MET A 203 4704 4636 4885 -78 26 -99 A C ATOM 1828 O MET A 203 7.992 3.024 13.522 1.00 36.82 A O ANISOU 1828 O MET A 203 4637 4556 4796 -47 83 -113 A O ATOM 1829 CB AMET A 203 6.236 2.900 11.038 0.44 37.96 A C ANISOU 1829 CB AMET A 203 4690 4639 5095 -73 -10 -54 A C ATOM 1830 CB BMET A 203 6.218 2.874 11.059 0.56 37.96 A C ANISOU 1830 CB BMET A 203 4688 4638 5095 -73 -9 -54 A C ATOM 1831 CG AMET A 203 6.044 4.374 10.736 0.44 37.42 A C ANISOU 1831 CG AMET A 203 4626 4534 5059 -67 -32 -50 A C ATOM 1832 CG BMET A 203 5.933 4.363 11.090 0.56 38.40 A C ANISOU 1832 CG BMET A 203 4748 4655 5189 -60 -12 -56 A C ATOM 1833 SD AMET A 203 4.319 4.779 10.418 0.44 43.18 A S ANISOU 1833 SD AMET A 203 5277 5207 5921 -33 -47 -23 A S ATOM 1834 SD BMET A 203 4.160 4.665 11.144 0.56 39.16 A S ANISOU 1834 SD BMET A 203 4763 4695 5422 -21 3 -34 A S ATOM 1835 CE AMET A 203 4.377 6.542 10.687 0.44 40.20 A C ANISOU 1835 CE AMET A 203 4934 4774 5566 -7 -28 -27 A C ATOM 1836 CE BMET A 203 4.161 6.419 11.471 0.56 41.79 A C ANISOU 1836 CE BMET A 203 5130 4972 5777 8 24 -46 A C ATOM 1837 N ALA A 204 9.274 4.140 12.037 1.00 36.65 A N ANISOU 1837 N ALA A 204 4623 4544 4759 -106 -5 -112 A N ATOM 1838 CA ALA A 204 9.998 4.876 13.059 1.00 33.78 A C ANISOU 1838 CA ALA A 204 4288 4187 4359 -111 4 -157 A C ATOM 1839 C ALA A 204 10.196 6.305 12.587 1.00 33.98 A C ANISOU 1839 C ALA A 204 4323 4161 4428 -145 -19 -165 A C ATOM 1840 O ALA A 204 9.984 6.622 11.414 1.00 36.32 A O ANISOU 1840 O ALA A 204 4607 4430 4761 -160 -40 -122 A O ATOM 1841 CB ALA A 204 11.358 4.222 13.356 1.00 37.21 A C ANISOU 1841 CB ALA A 204 4724 4695 4719 -121 -16 -170 A C ATOM 1842 N TYR A 205 10.619 7.175 13.502 1.00 37.05 A N ANISOU 1842 N TYR A 205 4742 4529 4806 -156 -17 -221 A N ATOM 1843 CA TYR A 205 10.944 8.524 13.077 1.00 38.83 A C ANISOU 1843 CA TYR A 205 4981 4689 5086 -199 -34 -231 A C ATOM 1844 C TYR A 205 12.075 9.116 13.904 1.00 39.02 A C ANISOU 1844 C TYR A 205 5022 4719 5085 -243 -62 -302 A C ATOM 1845 O TYR A 205 12.366 8.686 15.027 1.00 39.69 A O ANISOU 1845 O TYR A 205 5127 4853 5101 -222 -71 -356 A O ATOM 1846 CB TYR A 205 9.709 9.448 13.106 1.00 39.39 A C ANISOU 1846 CB TYR A 205 5073 4666 5228 -163 -4 -229 A C ATOM 1847 CG TYR A 205 8.965 9.589 14.420 1.00 39.84 A C ANISOU 1847 CG TYR A 205 5164 4700 5275 -108 44 -286 A C ATOM 1848 CD1 TYR A 205 9.350 10.528 15.373 1.00 45.03 A C ANISOU 1848 CD1 TYR A 205 5881 5312 5916 -117 48 -368 A C ATOM 1849 CD2 TYR A 205 7.824 8.842 14.665 1.00 45.32 A C ANISOU 1849 CD2 TYR A 205 5833 5407 5981 -48 93 -258 A C ATOM 1850 CE1 TYR A 205 8.641 10.675 16.557 1.00 47.68 A C ANISOU 1850 CE1 TYR A 205 6267 5626 6223 -54 106 -423 A C ATOM 1851 CE2 TYR A 205 7.114 8.976 15.838 1.00 44.48 A C ANISOU 1851 CE2 TYR A 205 5759 5279 5864 10 163 -299 A C ATOM 1852 CZ TYR A 205 7.516 9.897 16.777 1.00 51.59 A C ANISOU 1852 CZ TYR A 205 6736 6142 6726 14 173 -381 A C ATOM 1853 OH TYR A 205 6.797 10.030 17.944 1.00 52.84 A O ANISOU 1853 OH TYR A 205 6944 6279 6853 83 255 -425 A O ATOM 1854 N PHE A 206 12.721 10.111 13.290 1.00 38.41 A N ANISOU 1854 N PHE A 206 4938 4590 5066 -307 -79 -297 A N ATOM 1855 CA PHE A 206 13.822 10.874 13.858 1.00 40.04 A C ANISOU 1855 CA PHE A 206 5144 4780 5288 -375 -117 -365 A C ATOM 1856 C PHE A 206 13.463 12.355 13.793 1.00 42.48 A C ANISOU 1856 C PHE A 206 5500 4957 5684 -403 -103 -389 A C ATOM 1857 O PHE A 206 12.620 12.768 12.992 1.00 42.63 A O ANISOU 1857 O PHE A 206 5534 4908 5754 -376 -67 -326 A O ATOM 1858 CB PHE A 206 15.135 10.644 13.080 1.00 39.19 A C ANISOU 1858 CB PHE A 206 4965 4725 5199 -441 -138 -326 A C ATOM 1859 CG PHE A 206 15.654 9.222 13.124 1.00 39.26 A C ANISOU 1859 CG PHE A 206 4927 4856 5132 -409 -150 -304 A C ATOM 1860 CD1 PHE A 206 15.041 8.215 12.389 1.00 39.25 A C ANISOU 1860 CD1 PHE A 206 4926 4890 5096 -355 -117 -236 A C ATOM 1861 CD2 PHE A 206 16.785 8.903 13.869 1.00 44.06 A C ANISOU 1861 CD2 PHE A 206 5491 5538 5712 -431 -203 -354 A C ATOM 1862 CE1 PHE A 206 15.523 6.908 12.422 1.00 40.55 A C ANISOU 1862 CE1 PHE A 206 5059 5148 5200 -321 -121 -219 A C ATOM 1863 CE2 PHE A 206 17.272 7.601 13.903 1.00 40.18 A C ANISOU 1863 CE2 PHE A 206 4958 5150 5159 -388 -210 -326 A C ATOM 1864 CZ PHE A 206 16.645 6.607 13.179 1.00 39.90 A C ANISOU 1864 CZ PHE A 206 4934 5135 5091 -333 -162 -258 A C ATOM 1865 N ASP A 207 14.127 13.161 14.623 1.00 43.41 A N ANISOU 1865 N ASP A 207 5641 5031 5820 -456 -139 -484 A N ATOM 1866 CA ASP A 207 14.005 14.608 14.499 1.00 44.66 A C ANISOU 1866 CA ASP A 207 5845 5044 6079 -500 -126 -511 A C ATOM 1867 C ASP A 207 14.392 15.049 13.092 1.00 42.09 A C ANISOU 1867 C ASP A 207 5481 4671 5842 -557 -99 -406 A C ATOM 1868 O ASP A 207 15.189 14.401 12.408 1.00 44.03 A O ANISOU 1868 O ASP A 207 5657 4998 6073 -592 -103 -347 A O ATOM 1869 CB ASP A 207 14.897 15.330 15.511 1.00 45.57 A C ANISOU 1869 CB ASP A 207 5983 5123 6208 -573 -188 -639 A C ATOM 1870 CG ASP A 207 14.359 15.272 16.920 1.00 63.13 A C ANISOU 1870 CG ASP A 207 8291 7356 8339 -506 -203 -751 A C ATOM 1871 OD1 ASP A 207 13.167 14.957 17.099 1.00 55.61 A O ANISOU 1871 OD1 ASP A 207 7382 6402 7345 -406 -140 -725 A O ATOM 1872 OD2 ASP A 207 15.138 15.561 17.853 1.00 58.89 A O ANISOU 1872 OD2 ASP A 207 7776 6828 7771 -553 -278 -866 A O ATOM 1873 N GLY A 208 13.839 16.189 12.671 1.00 44.53 A N ANISOU 1873 N GLY A 208 5842 4839 6238 -558 -62 -381 A N ATOM 1874 CA GLY A 208 14.006 16.640 11.301 1.00 42.61 A C ANISOU 1874 CA GLY A 208 5586 4541 6063 -589 -23 -261 A C ATOM 1875 C GLY A 208 15.426 17.005 10.932 1.00 47.11 A C ANISOU 1875 C GLY A 208 6102 5100 6698 -709 -24 -250 A C ATOM 1876 O GLY A 208 15.778 16.979 9.749 1.00 51.24 A O ANISOU 1876 O GLY A 208 6601 5628 7241 -730 21 -136 A O ATOM 1877 N ASP A 209 16.251 17.344 11.912 1.00 46.11 A N ANISOU 1877 N ASP A 209 5955 4960 6606 -787 -73 -365 A N ATOM 1878 CA ASP A 209 17.644 17.677 11.649 1.00 50.43 A C ANISOU 1878 CA ASP A 209 6420 5500 7241 -912 -81 -363 A C ATOM 1879 C ASP A 209 18.580 16.510 11.949 1.00 47.20 A C ANISOU 1879 C ASP A 209 5908 5261 6765 -926 -130 -386 A C ATOM 1880 O ASP A 209 19.789 16.714 12.101 1.00 48.69 A O ANISOU 1880 O ASP A 209 6007 5464 7031 -1028 -162 -420 A O ATOM 1881 CB ASP A 209 18.045 18.918 12.450 1.00 52.33 A C ANISOU 1881 CB ASP A 209 6690 5599 7592 -1007 -119 -479 A C ATOM 1882 CG ASP A 209 17.927 18.719 13.943 1.00 59.19 A C ANISOU 1882 CG ASP A 209 7596 6509 8383 -981 -210 -641 A C ATOM 1883 OD1 ASP A 209 17.354 17.697 14.370 1.00 61.84 A O ANISOU 1883 OD1 ASP A 209 7946 6966 8584 -879 -224 -648 A O ATOM 1884 OD2 ASP A 209 18.402 19.593 14.697 1.00 72.80 A O ANISOU 1884 OD2 ASP A 209 9343 8139 10180 -1064 -265 -763 A O ATOM 1885 N CYS A 210 18.053 15.289 12.010 1.00 41.65 A N ANISOU 1885 N CYS A 210 5207 4682 5934 -825 -136 -364 A N ATOM 1886 CA CYS A 210 18.848 14.101 12.317 1.00 45.08 A C ANISOU 1886 CA CYS A 210 5556 5272 6300 -815 -179 -378 A C ATOM 1887 C CYS A 210 18.937 13.142 11.128 1.00 44.56 A C ANISOU 1887 C CYS A 210 5450 5291 6191 -772 -116 -257 A C ATOM 1888 O CYS A 210 18.884 11.920 11.280 1.00 42.60 A O ANISOU 1888 O CYS A 210 5183 5155 5847 -703 -130 -251 A O ATOM 1889 CB CYS A 210 18.274 13.406 13.550 1.00 42.49 A C ANISOU 1889 CB CYS A 210 5276 5013 5856 -734 -238 -465 A C ATOM 1890 SG CYS A 210 18.564 14.400 15.030 1.00 50.27 A S ANISOU 1890 SG CYS A 210 6307 5930 6863 -789 -329 -631 A S ATOM 1891 N ALA A 211 19.124 13.686 9.926 1.00 44.52 A N ANISOU 1891 N ALA A 211 5441 5224 6250 -810 -41 -159 A N ATOM 1892 CA ALA A 211 19.257 12.828 8.754 1.00 40.79 A C ANISOU 1892 CA ALA A 211 4949 4829 5721 -766 22 -52 A C ATOM 1893 C ALA A 211 20.491 11.943 8.857 1.00 39.79 A C ANISOU 1893 C ALA A 211 4708 4824 5588 -785 16 -59 A C ATOM 1894 O ALA A 211 20.462 10.778 8.441 1.00 40.93 A O ANISOU 1894 O ALA A 211 4846 5063 5643 -712 36 -21 A O ATOM 1895 CB ALA A 211 19.331 13.672 7.482 1.00 47.14 A C ANISOU 1895 CB ALA A 211 5782 5543 6584 -802 112 60 A C ATOM 1896 N ASP A 212 21.598 12.488 9.373 1.00 44.32 A N ANISOU 1896 N ASP A 212 5185 5388 6265 -881 -13 -107 A N ATOM 1897 CA ASP A 212 22.816 11.691 9.484 1.00 43.14 A C ANISOU 1897 CA ASP A 212 4904 5358 6130 -893 -24 -110 A C ATOM 1898 C ASP A 212 22.576 10.457 10.344 1.00 47.31 A C ANISOU 1898 C ASP A 212 5438 5998 6539 -798 -99 -166 A C ATOM 1899 O ASP A 212 23.020 9.350 10.000 1.00 43.06 A O ANISOU 1899 O ASP A 212 4849 5561 5951 -739 -72 -124 A O ATOM 1900 CB ASP A 212 23.960 12.524 10.065 1.00 45.46 A C ANISOU 1900 CB ASP A 212 5080 5624 6571 -1018 -73 -171 A C ATOM 1901 CG ASP A 212 24.429 13.617 9.124 1.00 49.00 A C ANISOU 1901 CG ASP A 212 5496 5962 7161 -1121 26 -94 A C ATOM 1902 OD1 ASP A 212 24.705 13.316 7.951 1.00 47.19 A O ANISOU 1902 OD1 ASP A 212 5247 5757 6926 -1101 145 24 A O ATOM 1903 OD2 ASP A 212 24.536 14.781 9.561 1.00 55.89 A O ANISOU 1903 OD2 ASP A 212 6370 6717 8147 -1222 -8 -150 A O ATOM 1904 N GLN A 213 21.873 10.627 11.470 1.00 41.48 A N ANISOU 1904 N GLN A 213 4771 5237 5753 -776 -182 -257 A N ATOM 1905 CA GLN A 213 21.594 9.482 12.337 1.00 40.78 A C ANISOU 1905 CA GLN A 213 4703 5244 5546 -682 -240 -298 A C ATOM 1906 C GLN A 213 20.641 8.495 11.677 1.00 38.69 A C ANISOU 1906 C GLN A 213 4511 5002 5188 -585 -176 -229 A C ATOM 1907 O GLN A 213 20.785 7.280 11.848 1.00 40.06 A O ANISOU 1907 O GLN A 213 4668 5264 5289 -513 -183 -217 A O ATOM 1908 CB GLN A 213 21.036 9.943 13.688 1.00 41.17 A C ANISOU 1908 CB GLN A 213 4828 5261 5554 -675 -324 -407 A C ATOM 1909 CG GLN A 213 21.955 10.790 14.593 1.00 46.98 A C ANISOU 1909 CG GLN A 213 5509 5983 6359 -765 -425 -510 A C ATOM 1910 CD GLN A 213 22.377 12.148 14.036 1.00 62.58 A C ANISOU 1910 CD GLN A 213 7448 7841 8489 -891 -400 -512 A C ATOM 1911 NE2 GLN A 213 23.510 12.645 14.518 1.00 95.57 A N ANISOU 1911 NE2 GLN A 213 11523 12027 12762 -988 -483 -581 A N ATOM 1912 OE1 GLN A 213 21.688 12.756 13.224 1.00 53.88 A O ANISOU 1912 OE1 GLN A 213 6410 6637 7426 -901 -314 -453 A O ATOM 1913 N ALA A 214 19.648 8.988 10.932 1.00 40.17 A N ANISOU 1913 N ALA A 214 4778 5105 5378 -579 -122 -185 A N ATOM 1914 CA ALA A 214 18.737 8.089 10.229 1.00 41.04 A C ANISOU 1914 CA ALA A 214 4948 5234 5412 -498 -80 -128 A C ATOM 1915 C ALA A 214 19.475 7.268 9.175 1.00 38.29 A C ANISOU 1915 C ALA A 214 4554 4952 5045 -480 -24 -59 A C ATOM 1916 O ALA A 214 19.208 6.068 9.003 1.00 37.18 A O ANISOU 1916 O ALA A 214 4432 4866 4830 -408 -15 -44 A O ATOM 1917 CB ALA A 214 17.611 8.896 9.580 1.00 38.92 A C ANISOU 1917 CB ALA A 214 4760 4866 5163 -496 -50 -92 A C ATOM 1918 N ILE A 215 20.382 7.904 8.441 1.00 36.28 A N ANISOU 1918 N ILE A 215 4242 4682 4859 -543 25 -14 A N ATOM 1919 CA ILE A 215 21.171 7.187 7.441 1.00 34.14 A C ANISOU 1919 CA ILE A 215 3929 4475 4570 -519 100 52 A C ATOM 1920 C ILE A 215 22.053 6.151 8.120 1.00 38.24 A C ANISOU 1920 C ILE A 215 4357 5095 5076 -483 70 19 A C ATOM 1921 O ILE A 215 22.143 4.998 7.678 1.00 37.22 A O ANISOU 1921 O ILE A 215 4237 5023 4882 -408 106 45 A O ATOM 1922 CB ILE A 215 21.984 8.178 6.592 1.00 37.30 A C ANISOU 1922 CB ILE A 215 4280 4832 5060 -598 179 116 A C ATOM 1923 CG1 ILE A 215 21.049 9.012 5.698 1.00 40.23 A C ANISOU 1923 CG1 ILE A 215 4764 5106 5415 -603 220 176 A C ATOM 1924 CG2 ILE A 215 23.021 7.451 5.718 1.00 41.16 A C ANISOU 1924 CG2 ILE A 215 4702 5398 5540 -572 273 179 A C ATOM 1925 CD1 ILE A 215 21.732 10.173 4.973 1.00 42.07 A C ANISOU 1925 CD1 ILE A 215 4971 5269 5746 -687 305 248 A C ATOM 1926 N GLN A 216 22.714 6.546 9.212 1.00 40.06 A N ANISOU 1926 N GLN A 216 4506 5346 5370 -531 -4 -43 A N ATOM 1927 CA GLN A 216 23.624 5.634 9.899 1.00 38.27 A C ANISOU 1927 CA GLN A 216 4183 5221 5136 -489 -49 -68 A C ATOM 1928 C GLN A 216 22.875 4.436 10.468 1.00 40.07 A C ANISOU 1928 C GLN A 216 4489 5485 5249 -385 -83 -87 A C ATOM 1929 O GLN A 216 23.347 3.298 10.373 1.00 39.56 A O ANISOU 1929 O GLN A 216 4392 5490 5151 -311 -63 -62 A O ATOM 1930 CB GLN A 216 24.369 6.371 11.011 1.00 39.39 A C ANISOU 1930 CB GLN A 216 4234 5376 5356 -562 -151 -142 A C ATOM 1931 CG GLN A 216 25.449 5.531 11.688 1.00 44.86 A C ANISOU 1931 CG GLN A 216 4807 6183 6055 -518 -215 -161 A C ATOM 1932 CD GLN A 216 26.586 5.207 10.754 1.00 45.02 A C ANISOU 1932 CD GLN A 216 4692 6255 6157 -522 -128 -90 A C ATOM 1933 NE2 GLN A 216 26.707 3.937 10.392 1.00 49.07 A N ANISOU 1933 NE2 GLN A 216 5209 6831 6604 -413 -77 -45 A N ATOM 1934 OE1 GLN A 216 27.343 6.089 10.349 1.00 48.30 A O ANISOU 1934 OE1 GLN A 216 5004 6647 6701 -620 -97 -75 A O ATOM 1935 N ALA A 217 21.720 4.677 11.091 1.00 38.41 A N ANISOU 1935 N ALA A 217 4381 5224 4990 -376 -123 -127 A N ATOM 1936 CA ALA A 217 20.901 3.576 11.580 1.00 37.00 A C ANISOU 1936 CA ALA A 217 4278 5063 4717 -286 -133 -132 A C ATOM 1937 C ALA A 217 20.560 2.605 10.461 1.00 36.94 A C ANISOU 1937 C ALA A 217 4310 5055 4672 -231 -58 -74 A C ATOM 1938 O ALA A 217 20.594 1.380 10.652 1.00 37.65 A O ANISOU 1938 O ALA A 217 4411 5183 4712 -156 -51 -64 A O ATOM 1939 CB ALA A 217 19.614 4.119 12.205 1.00 38.87 A C ANISOU 1939 CB ALA A 217 4611 5231 4927 -290 -156 -170 A C ATOM 1940 N SER A 218 20.170 3.134 9.305 1.00 36.49 A N ANISOU 1940 N SER A 218 4288 4946 4631 -264 -5 -37 A N ATOM 1941 CA SER A 218 19.801 2.277 8.185 1.00 37.31 A C ANISOU 1941 CA SER A 218 4446 5045 4682 -214 53 4 A C ATOM 1942 C SER A 218 20.976 1.422 7.744 1.00 38.79 A C ANISOU 1942 C SER A 218 4573 5300 4865 -171 104 30 A C ATOM 1943 O SER A 218 20.824 0.221 7.485 1.00 36.90 A O ANISOU 1943 O SER A 218 4375 5075 4572 -99 127 34 A O ATOM 1944 CB SER A 218 19.307 3.130 7.014 1.00 39.62 A C ANISOU 1944 CB SER A 218 4793 5281 4981 -252 90 43 A C ATOM 1945 OG SER A 218 18.212 3.929 7.406 1.00 38.61 A O ANISOU 1945 OG SER A 218 4712 5087 4870 -278 45 23 A O ATOM 1946 N LEU A 219 22.152 2.033 7.631 1.00 36.26 A N ANISOU 1946 N LEU A 219 4151 5014 4611 -215 128 48 A N ATOM 1947 CA LEU A 219 23.335 1.300 7.203 1.00 37.95 A C ANISOU 1947 CA LEU A 219 4285 5296 4840 -169 191 78 A C ATOM 1948 C LEU A 219 23.696 0.226 8.220 1.00 40.23 A C ANISOU 1948 C LEU A 219 4533 5642 5112 -95 138 52 A C ATOM 1949 O LEU A 219 24.066 -0.896 7.852 1.00 39.22 A O ANISOU 1949 O LEU A 219 4406 5543 4953 -11 189 72 A O ATOM 1950 CB LEU A 219 24.488 2.284 7.020 1.00 38.58 A C ANISOU 1950 CB LEU A 219 4237 5397 5026 -245 224 104 A C ATOM 1951 CG LEU A 219 24.426 3.113 5.734 1.00 39.59 A C ANISOU 1951 CG LEU A 219 4404 5475 5165 -295 322 163 A C ATOM 1952 CD1 LEU A 219 25.567 4.134 5.732 1.00 42.47 A C ANISOU 1952 CD1 LEU A 219 4626 5845 5663 -387 357 189 A C ATOM 1953 CD2 LEU A 219 24.409 2.287 4.434 1.00 49.25 A C ANISOU 1953 CD2 LEU A 219 5703 6710 6299 -217 432 211 A C ATOM 1954 N ASP A 220 23.561 0.544 9.510 1.00 38.07 A N ANISOU 1954 N ASP A 220 4238 5378 4849 -115 39 8 A N ATOM 1955 CA ASP A 220 23.936 -0.403 10.555 1.00 36.46 A C ANISOU 1955 CA ASP A 220 4004 5232 4617 -37 -18 -6 A C ATOM 1956 C ASP A 220 22.951 -1.563 10.628 1.00 39.76 A C ANISOU 1956 C ASP A 220 4542 5613 4951 43 1 -0 A C ATOM 1957 O ASP A 220 23.351 -2.689 10.956 1.00 38.55 A O ANISOU 1957 O ASP A 220 4380 5494 4774 133 5 17 A O ATOM 1958 CB ASP A 220 24.047 0.311 11.913 1.00 40.11 A C ANISOU 1958 CB ASP A 220 4433 5718 5091 -78 -134 -59 A C ATOM 1959 CG ASP A 220 25.284 1.217 12.019 1.00 44.01 A C ANISOU 1959 CG ASP A 220 4775 6257 5688 -152 -175 -75 A C ATOM 1960 OD1 ASP A 220 26.266 1.001 11.290 1.00 44.59 A O ANISOU 1960 OD1 ASP A 220 4741 6372 5828 -145 -115 -32 A O ATOM 1961 OD2 ASP A 220 25.293 2.138 12.856 1.00 48.59 A O ANISOU 1961 OD2 ASP A 220 5341 6830 6290 -219 -266 -133 A O ATOM 1962 N ILE A 221 21.673 -1.315 10.327 1.00 36.17 A N ANISOU 1962 N ILE A 221 4194 5085 4466 12 12 -11 A N ATOM 1963 CA ILE A 221 20.694 -2.400 10.256 1.00 35.05 A C ANISOU 1963 CA ILE A 221 4152 4896 4271 70 36 -6 A C ATOM 1964 C ILE A 221 21.052 -3.351 9.119 1.00 37.05 A C ANISOU 1964 C ILE A 221 4424 5145 4510 123 110 18 A C ATOM 1965 O ILE A 221 21.060 -4.578 9.286 1.00 36.28 A O ANISOU 1965 O ILE A 221 4360 5038 4388 200 130 26 A O ATOM 1966 CB ILE A 221 19.270 -1.829 10.090 1.00 36.29 A C ANISOU 1966 CB ILE A 221 4390 4979 4421 19 26 -24 A C ATOM 1967 CG1 ILE A 221 18.724 -1.282 11.411 1.00 37.66 A C ANISOU 1967 CG1 ILE A 221 4575 5145 4590 2 -28 -52 A C ATOM 1968 CG2 ILE A 221 18.341 -2.887 9.493 1.00 40.37 A C ANISOU 1968 CG2 ILE A 221 4990 5439 4910 56 59 -18 A C ATOM 1969 CD1 ILE A 221 17.457 -0.401 11.204 1.00 38.98 A C ANISOU 1969 CD1 ILE A 221 4793 5242 4775 -51 -31 -67 A C ATOM 1970 N LEU A 222 21.367 -2.801 7.942 1.00 36.56 A N ANISOU 1970 N LEU A 222 4351 5082 4458 88 161 32 A N ATOM 1971 CA LEU A 222 21.733 -3.650 6.818 1.00 38.06 A C ANISOU 1971 CA LEU A 222 4575 5269 4616 146 241 47 A C ATOM 1972 C LEU A 222 22.970 -4.490 7.131 1.00 41.10 A C ANISOU 1972 C LEU A 222 4878 5713 5024 228 275 66 A C ATOM 1973 O LEU A 222 23.042 -5.658 6.735 1.00 39.73 A O ANISOU 1973 O LEU A 222 4758 5519 4820 309 325 66 A O ATOM 1974 CB LEU A 222 21.954 -2.812 5.555 1.00 39.82 A C ANISOU 1974 CB LEU A 222 4806 5492 4832 102 301 70 A C ATOM 1975 CG LEU A 222 20.737 -2.076 4.979 1.00 42.16 A C ANISOU 1975 CG LEU A 222 5196 5728 5096 43 271 63 A C ATOM 1976 CD1 LEU A 222 21.129 -1.196 3.791 1.00 49.32 A C ANISOU 1976 CD1 LEU A 222 6112 6639 5988 10 338 105 A C ATOM 1977 CD2 LEU A 222 19.665 -3.071 4.578 1.00 40.97 A C ANISOU 1977 CD2 LEU A 222 5161 5523 4885 82 251 31 A C ATOM 1978 N AMET A 223 23.966 -3.906 7.814 0.44 39.91 A N ANISOU 1978 N AMET A 223 4595 5632 4935 210 245 79 A N ATOM 1979 N BMET A 223 23.949 -3.918 7.843 0.56 39.87 A N ANISOU 1979 N BMET A 223 4591 5627 4929 211 243 79 A N ATOM 1980 CA AMET A 223 25.146 -4.672 8.212 0.44 40.56 A C ANISOU 1980 CA AMET A 223 4578 5781 5053 296 258 102 A C ATOM 1981 CA BMET A 223 25.150 -4.674 8.194 0.56 40.51 A C ANISOU 1981 CA BMET A 223 4571 5773 5046 296 260 102 A C ATOM 1982 C AMET A 223 24.768 -5.782 9.178 0.44 40.22 A C ANISOU 1982 C AMET A 223 4590 5720 4970 379 211 98 A C ATOM 1983 C BMET A 223 24.843 -5.751 9.226 0.56 40.17 A C ANISOU 1983 C BMET A 223 4575 5721 4969 380 207 99 A C ATOM 1984 O AMET A 223 25.190 -6.934 9.026 0.44 41.64 A O ANISOU 1984 O AMET A 223 4781 5898 5143 483 260 118 A O ATOM 1985 O BMET A 223 25.376 -6.866 9.147 0.56 41.25 A O ANISOU 1985 O BMET A 223 4706 5864 5103 485 252 121 A O ATOM 1986 CB AMET A 223 26.182 -3.766 8.884 0.44 43.92 A C ANISOU 1986 CB AMET A 223 4840 6285 5563 247 201 107 A C ATOM 1987 CB BMET A 223 26.229 -3.720 8.719 0.56 43.80 A C ANISOU 1987 CB BMET A 223 4822 6269 5551 244 214 110 A C ATOM 1988 CG AMET A 223 27.361 -3.352 8.030 0.44 54.87 A C ANISOU 1988 CG AMET A 223 6098 7720 7030 231 287 142 A C ATOM 1989 CG BMET A 223 27.443 -4.390 9.348 0.56 44.30 A C ANISOU 1989 CG BMET A 223 4752 6415 5664 331 191 132 A C ATOM 1990 SD AMET A 223 28.709 -4.538 7.746 0.44 61.51 A S ANISOU 1990 SD AMET A 223 6824 8630 7917 369 371 185 A S ATOM 1991 SD BMET A 223 28.670 -3.172 9.886 0.56 62.22 A S ANISOU 1991 SD BMET A 223 6808 8773 8061 244 117 128 A S ATOM 1992 CE AMET A 223 27.970 -6.170 7.693 0.44 40.35 A C ANISOU 1992 CE AMET A 223 4312 5886 5133 501 401 178 A C ATOM 1993 CE BMET A 223 27.857 -2.444 11.309 0.56 55.26 A C ANISOU 1993 CE BMET A 223 5987 7877 7131 175 -47 66 A C ATOM 1994 N GLU A 224 23.994 -5.435 10.209 1.00 37.43 A N ANISOU 1994 N GLU A 224 4277 5351 4592 342 125 77 A N ATOM 1995 CA GLU A 224 23.631 -6.418 11.218 1.00 39.14 A C ANISOU 1995 CA GLU A 224 4553 5551 4768 420 91 88 A C ATOM 1996 C GLU A 224 22.879 -7.593 10.597 1.00 39.87 A C ANISOU 1996 C GLU A 224 4765 5553 4831 470 163 93 A C ATOM 1997 O GLU A 224 23.106 -8.752 10.981 1.00 40.41 A O ANISOU 1997 O GLU A 224 4860 5604 4890 569 183 121 A O ATOM 1998 CB GLU A 224 22.808 -5.746 12.317 1.00 40.46 A C ANISOU 1998 CB GLU A 224 4761 5709 4903 367 12 65 A C ATOM 1999 CG GLU A 224 22.762 -6.534 13.602 1.00 41.78 A C ANISOU 1999 CG GLU A 224 4965 5891 5020 452 -30 89 A C ATOM 2000 CD GLU A 224 24.109 -6.596 14.323 1.00 47.72 A C ANISOU 2000 CD GLU A 224 5604 6746 5780 516 -101 108 A C ATOM 2001 OE1 GLU A 224 24.988 -5.726 14.110 1.00 49.22 A O ANISOU 2001 OE1 GLU A 224 5672 7003 6026 464 -141 86 A O ATOM 2002 OE2 GLU A 224 24.289 -7.551 15.094 1.00 55.03 A O ANISOU 2002 OE2 GLU A 224 6561 7685 6664 621 -118 149 A O ATOM 2003 N LEU A 225 22.004 -7.326 9.621 1.00 38.15 A N ANISOU 2003 N LEU A 225 4622 5271 4603 407 198 65 A N ATOM 2004 CA LEU A 225 21.281 -8.419 8.970 1.00 37.02 A C ANISOU 2004 CA LEU A 225 4590 5037 4439 441 249 52 A C ATOM 2005 C LEU A 225 22.223 -9.298 8.149 1.00 40.12 A C ANISOU 2005 C LEU A 225 4979 5432 4832 530 327 60 A C ATOM 2006 O LEU A 225 22.024 -10.516 8.061 1.00 40.98 A O ANISOU 2006 O LEU A 225 5165 5471 4935 599 365 57 A O ATOM 2007 CB LEU A 225 20.154 -7.859 8.097 1.00 35.91 A C ANISOU 2007 CB LEU A 225 4521 4840 4285 354 242 16 A C ATOM 2008 CG LEU A 225 19.034 -7.174 8.886 1.00 41.56 A C ANISOU 2008 CG LEU A 225 5249 5531 5011 284 181 8 A C ATOM 2009 CD1 LEU A 225 18.040 -6.568 7.902 1.00 47.02 A C ANISOU 2009 CD1 LEU A 225 5991 6177 5698 210 168 -22 A C ATOM 2010 CD2 LEU A 225 18.337 -8.134 9.829 1.00 46.29 A C ANISOU 2010 CD2 LEU A 225 5899 6071 5617 319 180 19 A C ATOM 2011 N GLU A 226 23.247 -8.715 7.524 1.00 38.86 A N ANISOU 2011 N GLU A 226 4733 5344 4687 531 365 71 A N ATOM 2012 CA AGLU A 226 24.202 -9.546 6.792 0.56 42.65 A C ANISOU 2012 CA AGLU A 226 5202 5833 5171 630 459 82 A C ATOM 2013 CA BGLU A 226 24.205 -9.541 6.795 0.44 42.68 A C ANISOU 2013 CA BGLU A 226 5205 5837 5175 630 458 82 A C ATOM 2014 C GLU A 226 24.957 -10.464 7.746 1.00 40.02 A C ANISOU 2014 C GLU A 226 4810 5523 4872 742 451 120 A C ATOM 2015 O GLU A 226 25.170 -11.643 7.443 1.00 43.46 A O ANISOU 2015 O GLU A 226 5304 5905 5304 844 516 122 A O ATOM 2016 CB AGLU A 226 25.180 -8.683 5.988 0.56 44.01 A C ANISOU 2016 CB AGLU A 226 5274 6082 5365 608 520 100 A C ATOM 2017 CB BGLU A 226 25.190 -8.672 6.012 0.44 44.03 A C ANISOU 2017 CB BGLU A 226 5274 6086 5369 608 518 101 A C ATOM 2018 CG AGLU A 226 26.378 -9.455 5.421 0.56 49.16 A C ANISOU 2018 CG AGLU A 226 5875 6764 6039 725 630 123 A C ATOM 2019 CG BGLU A 226 26.135 -9.493 5.149 0.44 48.63 A C ANISOU 2019 CG BGLU A 226 5850 6677 5952 717 641 112 A C ATOM 2020 CD AGLU A 226 26.116 -10.067 4.054 0.56 55.04 A C ANISOU 2020 CD AGLU A 226 6758 7443 6711 768 736 88 A C ATOM 2021 CD BGLU A 226 27.208 -8.665 4.472 0.44 54.88 A C ANISOU 2021 CD BGLU A 226 6519 7550 6784 701 723 147 A C ATOM 2022 OE1AGLU A 226 24.940 -10.103 3.630 0.56 48.52 A O ANISOU 2022 OE1AGLU A 226 6075 6541 5818 714 701 41 A O ATOM 2023 OE1BGLU A 226 27.235 -7.435 4.675 0.44 60.68 A O ANISOU 2023 OE1BGLU A 226 7174 8327 7554 596 677 161 A O ATOM 2024 OE2AGLU A 226 27.086 -10.542 3.419 0.56 63.25 A O ANISOU 2024 OE2AGLU A 226 7765 8507 7760 862 851 104 A O ATOM 2025 OE2BGLU A 226 28.030 -9.250 3.737 0.44 66.11 A O ANISOU 2025 OE2BGLU A 226 7925 8986 8210 796 844 161 A O ATOM 2026 N ILE A 227 25.384 -9.935 8.901 1.00 41.17 A N ANISOU 2026 N ILE A 227 4849 5745 5048 732 367 149 A N ATOM 2027 CA ILE A 227 26.059 -10.767 9.894 1.00 42.32 A C ANISOU 2027 CA ILE A 227 4945 5921 5212 847 338 194 A C ATOM 2028 C ILE A 227 25.132 -11.872 10.380 1.00 43.41 A C ANISOU 2028 C ILE A 227 5228 5954 5313 897 341 201 A C ATOM 2029 O ILE A 227 25.551 -13.022 10.561 1.00 44.20 A O ANISOU 2029 O ILE A 227 5351 6020 5424 1019 381 236 A O ATOM 2030 CB ILE A 227 26.563 -9.898 11.065 1.00 46.59 A C ANISOU 2030 CB ILE A 227 5364 6567 5771 815 221 210 A C ATOM 2031 CG1 ILE A 227 27.695 -8.985 10.576 1.00 51.51 A C ANISOU 2031 CG1 ILE A 227 5819 7286 6468 775 228 210 A C ATOM 2032 CG2 ILE A 227 27.032 -10.780 12.218 1.00 53.03 A C ANISOU 2032 CG2 ILE A 227 6162 7410 6577 940 166 260 A C ATOM 2033 CD1 ILE A 227 28.055 -7.864 11.540 1.00 54.73 A C ANISOU 2033 CD1 ILE A 227 6112 7779 6903 699 101 198 A C ATOM 2034 N LEU A 228 23.859 -11.541 10.598 1.00 38.75 A N ANISOU 2034 N LEU A 228 4730 5302 4689 804 309 174 A N ATOM 2035 CA LEU A 228 22.896 -12.516 11.102 1.00 39.06 A C ANISOU 2035 CA LEU A 228 4894 5235 4714 832 321 187 A C ATOM 2036 C LEU A 228 22.698 -13.650 10.107 1.00 43.29 A C ANISOU 2036 C LEU A 228 5526 5658 5264 879 410 163 A C ATOM 2037 O LEU A 228 22.680 -14.829 10.485 1.00 42.53 A O ANISOU 2037 O LEU A 228 5495 5483 5181 968 446 195 A O ATOM 2038 CB LEU A 228 21.568 -11.813 11.376 1.00 40.40 A C ANISOU 2038 CB LEU A 228 5118 5367 4866 714 281 159 A C ATOM 2039 CG LEU A 228 20.474 -12.605 12.077 1.00 50.03 A C ANISOU 2039 CG LEU A 228 6442 6484 6085 719 297 181 A C ATOM 2040 CD1 LEU A 228 20.868 -12.876 13.514 1.00 60.62 A C ANISOU 2040 CD1 LEU A 228 7771 7868 7392 802 266 250 A C ATOM 2041 CD2 LEU A 228 19.169 -11.810 12.023 1.00 49.77 A C ANISOU 2041 CD2 LEU A 228 6438 6416 6057 597 273 144 A C ATOM 2042 N ARG A 229 22.535 -13.298 8.826 1.00 39.54 A N ANISOU 2042 N ARG A 229 5075 5168 4780 822 444 105 A N ATOM 2043 CA ARG A 229 22.360 -14.288 7.769 1.00 40.71 A C ANISOU 2043 CA ARG A 229 5330 5213 4925 863 519 61 A C ATOM 2044 C ARG A 229 23.566 -15.218 7.661 1.00 42.20 A C ANISOU 2044 C ARG A 229 5495 5406 5134 1011 595 90 A C ATOM 2045 O ARG A 229 23.412 -16.435 7.513 1.00 43.33 A O ANISOU 2045 O ARG A 229 5737 5434 5292 1084 648 80 A O ATOM 2046 CB ARG A 229 22.146 -13.578 6.433 1.00 43.26 A C ANISOU 2046 CB ARG A 229 5680 5551 5207 790 535 -0 A C ATOM 2047 CG ARG A 229 20.772 -12.950 6.258 1.00 38.55 A C ANISOU 2047 CG ARG A 229 5138 4913 4595 662 467 -41 A C ATOM 2048 CD ARG A 229 20.543 -12.579 4.808 1.00 40.93 A C ANISOU 2048 CD ARG A 229 5505 5208 4841 621 484 -100 A C ATOM 2049 NE ARG A 229 21.482 -11.576 4.311 1.00 40.66 A N ANISOU 2049 NE ARG A 229 5387 5283 4779 620 518 -74 A N ATOM 2050 CZ ARG A 229 21.262 -10.266 4.344 1.00 41.80 A C ANISOU 2050 CZ ARG A 229 5473 5489 4920 531 471 -57 A C ATOM 2051 NH1 ARG A 229 20.147 -9.761 4.858 1.00 38.25 A N ANISOU 2051 NH1 ARG A 229 5035 5011 4487 446 387 -66 A N ATOM 2052 NH2 ARG A 229 22.161 -9.445 3.806 1.00 41.44 A N ANISOU 2052 NH2 ARG A 229 5358 5525 4862 529 520 -29 A N ATOM 2053 N ASN A 230 24.773 -14.656 7.729 1.00 41.33 A N ANISOU 2053 N ASN A 230 5245 5420 5037 1056 603 128 A N ATOM 2054 CA ASN A 230 25.980 -15.455 7.547 1.00 43.18 A C ANISOU 2054 CA ASN A 230 5430 5672 5306 1205 681 159 A C ATOM 2055 C ASN A 230 26.264 -16.353 8.746 1.00 47.52 A C ANISOU 2055 C ASN A 230 5970 6199 5888 1317 654 228 A C ATOM 2056 O ASN A 230 26.788 -17.460 8.576 1.00 45.06 A O ANISOU 2056 O ASN A 230 5693 5824 5603 1452 728 246 A O ATOM 2057 CB ASN A 230 27.180 -14.533 7.287 1.00 44.18 A C ANISOU 2057 CB ASN A 230 5382 5943 5462 1210 697 185 A C ATOM 2058 CG ASN A 230 27.098 -13.815 5.942 1.00 51.48 A C ANISOU 2058 CG ASN A 230 6331 6880 6350 1134 764 135 A C ATOM 2059 ND2 ASN A 230 27.986 -12.860 5.733 1.00 57.01 A N ANISOU 2059 ND2 ASN A 230 6881 7695 7086 1107 782 163 A N ATOM 2060 OD1 ASN A 230 26.232 -14.106 5.114 1.00 57.20 A O ANISOU 2060 OD1 ASN A 230 7209 7511 7014 1098 794 74 A O ATOM 2061 N ASER A 231 25.926 -15.915 9.957 0.53 46.13 A N ANISOU 2061 N ASER A 231 5760 6067 5701 1276 553 270 A N ATOM 2062 N BSER A 231 25.930 -15.899 9.954 0.47 46.14 A N ANISOU 2062 N BSER A 231 5760 6070 5703 1275 552 269 A N ATOM 2063 CA ASER A 231 26.288 -16.645 11.164 0.53 46.16 A C ANISOU 2063 CA ASER A 231 5752 6072 5714 1392 517 350 A C ATOM 2064 CA BSER A 231 26.279 -16.619 11.169 0.47 46.16 A C ANISOU 2064 CA BSER A 231 5752 6074 5714 1390 515 350 A C ATOM 2065 C ASER A 231 25.169 -17.530 11.701 0.53 46.47 A C ANISOU 2065 C ASER A 231 5952 5966 5738 1392 531 368 A C ATOM 2066 C BSER A 231 25.248 -17.665 11.572 0.47 46.54 A C ANISOU 2066 C BSER A 231 5966 5965 5753 1407 545 366 A C ATOM 2067 O ASER A 231 25.341 -18.153 12.753 0.53 48.77 A O ANISOU 2067 O ASER A 231 6261 6245 6023 1490 509 448 A O ATOM 2068 O BSER A 231 25.566 -18.541 12.384 0.47 48.01 A O ANISOU 2068 O BSER A 231 6176 6117 5947 1530 549 443 A O ATOM 2069 CB ASER A 231 26.720 -15.662 12.256 0.53 48.25 A C ANISOU 2069 CB ASER A 231 5889 6483 5960 1366 395 388 A C ATOM 2070 CB BSER A 231 26.464 -15.627 12.327 0.47 48.10 A C ANISOU 2070 CB BSER A 231 5894 6449 5932 1346 390 384 A C ATOM 2071 OG ASER A 231 25.592 -14.988 12.777 0.53 45.85 A O ANISOU 2071 OG ASER A 231 5651 6163 5608 1241 336 365 A O ATOM 2072 OG BSER A 231 27.464 -14.670 12.031 0.47 50.80 A O ANISOU 2072 OG BSER A 231 6068 6928 6307 1321 357 370 A O ATOM 2073 N ALA A 232 24.043 -17.609 11.012 1.00 44.26 A N ANISOU 2073 N ALA A 232 5786 5576 5456 1288 566 302 A N ATOM 2074 CA ALA A 232 22.950 -18.445 11.490 1.00 45.29 A C ANISOU 2074 CA ALA A 232 6050 5558 5600 1272 588 320 A C ATOM 2075 C ALA A 232 23.266 -19.932 11.317 1.00 46.92 A C ANISOU 2075 C ALA A 232 6347 5629 5852 1403 676 346 A C ATOM 2076 O ALA A 232 24.064 -20.321 10.458 1.00 50.23 A O ANISOU 2076 O ALA A 232 6755 6042 6289 1484 734 314 A O ATOM 2077 CB ALA A 232 21.659 -18.103 10.745 1.00 50.35 A C ANISOU 2077 CB ALA A 232 6764 6120 6246 1118 587 235 A C ATOM 2078 N PRO A 233 22.656 -20.789 12.133 1.00 52.53 A N ANISOU 2078 N PRO A 233 7154 6220 6586 1433 700 408 A N ATOM 2079 CA PRO A 233 22.913 -22.226 12.011 1.00 56.46 A C ANISOU 2079 CA PRO A 233 7750 6562 7139 1558 788 437 A C ATOM 2080 C PRO A 233 22.432 -22.778 10.678 1.00 52.47 A C ANISOU 2080 C PRO A 233 7346 5912 6677 1505 852 322 A C ATOM 2081 O PRO A 233 21.543 -22.223 10.023 1.00 49.16 A O ANISOU 2081 O PRO A 233 6948 5480 6250 1355 822 232 A O ATOM 2082 CB PRO A 233 22.116 -22.842 13.171 1.00 53.89 A C ANISOU 2082 CB PRO A 233 7514 6131 6830 1561 803 531 A C ATOM 2083 CG PRO A 233 21.453 -21.723 13.883 1.00 57.35 A C ANISOU 2083 CG PRO A 233 7900 6679 7213 1445 728 543 A C ATOM 2084 CD PRO A 233 22.025 -20.436 13.416 1.00 54.55 A C ANISOU 2084 CD PRO A 233 7413 6505 6808 1394 651 481 A C ATOM 2085 N GLU A 234 23.004 -23.917 10.297 1.00 50.74 A N ANISOU 2085 N GLU A 234 7199 5579 6502 1635 937 322 A N ATOM 2086 CA GLU A 234 22.560 -24.599 9.090 1.00 48.02 A C ANISOU 2086 CA GLU A 234 6979 5073 6192 1599 997 203 A C ATOM 2087 C GLU A 234 21.058 -24.822 9.144 1.00 52.27 A C ANISOU 2087 C GLU A 234 7615 5466 6779 1441 976 160 A C ATOM 2088 O GLU A 234 20.523 -25.272 10.160 1.00 53.79 A O ANISOU 2088 O GLU A 234 7840 5577 7020 1436 988 249 A O ATOM 2089 CB GLU A 234 23.263 -25.949 8.928 1.00 57.63 A C ANISOU 2089 CB GLU A 234 8284 6147 7465 1772 1100 222 A C ATOM 2090 CG GLU A 234 24.709 -25.974 9.335 1.00 73.28 A C ANISOU 2090 CG GLU A 234 10154 8253 9435 1961 1123 316 A C ATOM 2091 CD GLU A 234 25.454 -27.120 8.685 1.00 94.27 A C ANISOU 2091 CD GLU A 234 12894 10784 12143 2127 1238 290 A C ATOM 2092 OE1 GLU A 234 24.784 -28.040 8.161 1.00 71.63 A O ANISOU 2092 OE1 GLU A 234 10194 7702 9322 2101 1297 214 A O ATOM 2093 OE2 GLU A 234 26.702 -27.104 8.704 1.00118.11 A O ANISOU 2093 OE2 GLU A 234 15805 13910 15161 2285 1269 342 A O ATOM 2094 N GLY A 235 20.383 -24.517 8.042 1.00 50.76 A N ANISOU 2094 N GLY A 235 7467 5243 6575 1317 948 28 A N ATOM 2095 CA GLY A 235 18.960 -24.731 7.939 1.00 56.79 A C ANISOU 2095 CA GLY A 235 8303 5870 7403 1162 916 -30 A C ATOM 2096 C GLY A 235 18.101 -23.668 8.583 1.00 49.84 A C ANISOU 2096 C GLY A 235 7332 5092 6514 1028 838 8 A C ATOM 2097 O GLY A 235 16.871 -23.763 8.501 1.00 52.25 A O ANISOU 2097 O GLY A 235 7670 5296 6887 893 810 -36 A O ATOM 2098 N SER A 236 18.699 -22.656 9.207 1.00 45.66 A N ANISOU 2098 N SER A 236 6683 4754 5910 1060 802 82 A N ATOM 2099 CA SER A 236 17.913 -21.627 9.876 1.00 45.27 A C ANISOU 2099 CA SER A 236 6557 4796 5848 946 737 115 A C ATOM 2100 C SER A 236 17.217 -20.715 8.867 1.00 46.76 A C ANISOU 2100 C SER A 236 6721 5031 6014 809 665 5 A C ATOM 2101 O SER A 236 17.815 -20.299 7.868 1.00 41.91 A O ANISOU 2101 O SER A 236 6098 4491 5337 826 649 -62 A O ATOM 2102 CB SER A 236 18.802 -20.779 10.793 1.00 45.87 A C ANISOU 2102 CB SER A 236 6522 5058 5847 1018 706 206 A C ATOM 2103 OG SER A 236 18.090 -19.624 11.233 1.00 47.01 A O ANISOU 2103 OG SER A 236 6600 5297 5966 906 642 210 A O ATOM 2104 N PRO A 237 15.960 -20.343 9.118 1.00 44.64 A N ANISOU 2104 N PRO A 237 6438 4729 5794 679 624 -5 A N ATOM 2105 CA PRO A 237 15.299 -19.385 8.225 1.00 43.24 A C ANISOU 2105 CA PRO A 237 6227 4609 5593 561 542 -95 A C ATOM 2106 C PRO A 237 15.897 -17.987 8.281 1.00 44.18 A C ANISOU 2106 C PRO A 237 6247 4922 5619 565 497 -73 A C ATOM 2107 O PRO A 237 15.687 -17.208 7.341 1.00 44.05 A O ANISOU 2107 O PRO A 237 6216 4961 5560 502 441 -142 A O ATOM 2108 CB PRO A 237 13.839 -19.405 8.713 1.00 48.30 A C ANISOU 2108 CB PRO A 237 6854 5164 6334 439 523 -87 A C ATOM 2109 CG PRO A 237 13.923 -19.857 10.113 1.00 54.92 A C ANISOU 2109 CG PRO A 237 7689 5973 7206 498 597 35 A C ATOM 2110 CD PRO A 237 15.039 -20.849 10.153 1.00 51.22 A C ANISOU 2110 CD PRO A 237 7288 5456 6717 637 662 67 A C ATOM 2111 N LEU A 238 16.656 -17.653 9.331 1.00 42.84 A N ANISOU 2111 N LEU A 238 6014 4850 5415 639 514 20 A N ATOM 2112 CA LEU A 238 17.302 -16.348 9.399 1.00 39.26 A C ANISOU 2112 CA LEU A 238 5463 4566 4889 637 468 33 A C ATOM 2113 C LEU A 238 18.314 -16.148 8.275 1.00 39.66 A C ANISOU 2113 C LEU A 238 5502 4679 4886 683 479 -14 A C ATOM 2114 O LEU A 238 18.674 -15.003 7.965 1.00 39.61 A O ANISOU 2114 O LEU A 238 5424 4792 4836 649 444 -23 A O ATOM 2115 CB LEU A 238 17.989 -16.189 10.750 1.00 43.84 A C ANISOU 2115 CB LEU A 238 5985 5228 5442 715 472 129 A C ATOM 2116 CG LEU A 238 17.065 -16.215 11.974 1.00 47.13 A C ANISOU 2116 CG LEU A 238 6417 5607 5882 681 476 190 A C ATOM 2117 CD1 LEU A 238 17.887 -16.061 13.239 1.00 53.63 A C ANISOU 2117 CD1 LEU A 238 7204 6528 6646 777 466 277 A C ATOM 2118 CD2 LEU A 238 16.000 -15.144 11.876 1.00 49.94 A C ANISOU 2118 CD2 LEU A 238 6738 5990 6249 554 429 150 A C ATOM 2119 N ARG A 239 18.764 -17.232 7.646 1.00 39.81 A N ANISOU 2119 N ARG A 239 5597 4614 4914 761 539 -44 A N ATOM 2120 CA ARG A 239 19.691 -17.111 6.520 1.00 40.95 A C ANISOU 2120 CA ARG A 239 5745 4812 5005 815 574 -90 A C ATOM 2121 C ARG A 239 19.087 -16.333 5.352 1.00 42.35 A C ANISOU 2121 C ARG A 239 5952 5010 5131 716 530 -171 A C ATOM 2122 O ARG A 239 19.834 -15.753 4.550 1.00 37.59 A O ANISOU 2122 O ARG A 239 5325 4493 4465 741 556 -186 A O ATOM 2123 CB ARG A 239 20.129 -18.510 6.067 1.00 42.29 A C ANISOU 2123 CB ARG A 239 6014 4861 5194 922 656 -119 A C ATOM 2124 CG ARG A 239 21.043 -18.525 4.842 1.00 41.93 A C ANISOU 2124 CG ARG A 239 5992 4853 5085 993 719 -172 A C ATOM 2125 CD ARG A 239 22.006 -19.720 4.860 1.00 45.43 A C ANISOU 2125 CD ARG A 239 6473 5230 5557 1154 819 -154 A C ATOM 2126 NE ARG A 239 23.089 -19.464 5.799 1.00 42.41 A N ANISOU 2126 NE ARG A 239 5949 4965 5199 1247 833 -46 A N ATOM 2127 CZ ARG A 239 23.151 -19.926 7.043 1.00 43.54 A C ANISOU 2127 CZ ARG A 239 6062 5087 5393 1299 816 40 A C ATOM 2128 NH1 ARG A 239 22.395 -20.930 7.453 1.00 46.48 A N ANISOU 2128 NH1 ARG A 239 6545 5301 5815 1300 827 44 A N ATOM 2129 NH2 ARG A 239 23.968 -19.337 7.909 1.00 46.34 A N ANISOU 2129 NH2 ARG A 239 6275 5583 5750 1346 782 126 A N ATOM 2130 N VAL A 240 17.759 -16.287 5.228 1.00 40.48 A N ANISOU 2130 N VAL A 240 5762 4696 4921 608 466 -217 A N ATOM 2131 CA VAL A 240 17.171 -15.604 4.079 1.00 40.21 A C ANISOU 2131 CA VAL A 240 5765 4682 4832 528 409 -291 A C ATOM 2132 C VAL A 240 16.272 -14.460 4.544 1.00 42.04 A C ANISOU 2132 C VAL A 240 5919 4968 5086 421 328 -265 A C ATOM 2133 O VAL A 240 15.287 -14.130 3.887 1.00 43.47 A O ANISOU 2133 O VAL A 240 6132 5122 5263 339 256 -320 A O ATOM 2134 CB VAL A 240 16.401 -16.582 3.166 1.00 42.31 A C ANISOU 2134 CB VAL A 240 6165 4807 5105 502 387 -395 A C ATOM 2135 CG1 VAL A 240 17.380 -17.509 2.447 1.00 47.86 A C ANISOU 2135 CG1 VAL A 240 6961 5466 5757 617 475 -438 A C ATOM 2136 CG2 VAL A 240 15.354 -17.393 3.944 1.00 45.70 A C ANISOU 2136 CG2 VAL A 240 6607 5101 5655 444 364 -394 A C ATOM 2137 N LEU A 241 16.657 -13.811 5.635 1.00 38.76 A N ANISOU 2137 N LEU A 241 5403 4636 4688 430 334 -185 A N ATOM 2138 CA LEU A 241 15.990 -12.606 6.128 1.00 40.54 A C ANISOU 2138 CA LEU A 241 5555 4921 4927 347 273 -159 A C ATOM 2139 C LEU A 241 16.630 -11.380 5.477 1.00 39.15 A C ANISOU 2139 C LEU A 241 5335 4856 4684 335 261 -156 A C ATOM 2140 O LEU A 241 17.778 -11.030 5.781 1.00 40.17 A O ANISOU 2140 O LEU A 241 5399 5069 4794 386 299 -113 A O ATOM 2141 CB LEU A 241 16.096 -12.536 7.648 1.00 38.47 A C ANISOU 2141 CB LEU A 241 5229 4684 4702 367 287 -86 A C ATOM 2142 CG LEU A 241 15.562 -11.290 8.364 1.00 39.37 A C ANISOU 2142 CG LEU A 241 5273 4862 4824 301 240 -59 A C ATOM 2143 CD1 LEU A 241 14.117 -11.110 8.012 1.00 41.19 A C ANISOU 2143 CD1 LEU A 241 5522 5025 5104 212 196 -96 A C ATOM 2144 CD2 LEU A 241 15.729 -11.403 9.870 1.00 45.26 A C ANISOU 2144 CD2 LEU A 241 5987 5628 5580 340 260 6 A C ATOM 2145 N TYR A 242 15.876 -10.723 4.602 1.00 37.73 A N ANISOU 2145 N TYR A 242 5184 4674 4479 268 206 -195 A N ATOM 2146 CA TYR A 242 16.273 -9.502 3.921 1.00 37.92 A C ANISOU 2146 CA TYR A 242 5182 4783 4444 247 197 -182 A C ATOM 2147 C TYR A 242 15.219 -8.422 4.160 1.00 40.46 A C ANISOU 2147 C TYR A 242 5465 5112 4798 163 121 -173 A C ATOM 2148 O TYR A 242 14.041 -8.716 4.395 1.00 37.93 A O ANISOU 2148 O TYR A 242 5156 4725 4532 119 69 -196 A O ATOM 2149 CB TYR A 242 16.427 -9.731 2.425 1.00 38.68 A C ANISOU 2149 CB TYR A 242 5377 4869 4452 271 210 -231 A C ATOM 2150 CG TYR A 242 17.564 -10.651 2.039 1.00 40.06 A C ANISOU 2150 CG TYR A 242 5591 5043 4586 367 306 -242 A C ATOM 2151 CD1 TYR A 242 17.374 -12.023 1.934 1.00 42.84 A C ANISOU 2151 CD1 TYR A 242 6028 5298 4952 410 322 -295 A C ATOM 2152 CD2 TYR A 242 18.819 -10.139 1.754 1.00 43.16 A C ANISOU 2152 CD2 TYR A 242 5935 5524 4942 415 387 -197 A C ATOM 2153 CE1 TYR A 242 18.409 -12.867 1.573 1.00 46.41 A C ANISOU 2153 CE1 TYR A 242 6521 5740 5372 512 418 -306 A C ATOM 2154 CE2 TYR A 242 19.851 -10.970 1.388 1.00 40.79 A C ANISOU 2154 CE2 TYR A 242 5658 5224 4615 514 486 -203 A C ATOM 2155 CZ TYR A 242 19.648 -12.335 1.305 1.00 47.03 A C ANISOU 2155 CZ TYR A 242 6540 5917 5411 569 502 -258 A C ATOM 2156 OH TYR A 242 20.691 -13.180 0.944 1.00 51.61 A O ANISOU 2156 OH TYR A 242 7149 6490 5971 683 610 -265 A O ATOM 2157 N SER A 243 15.653 -7.167 4.079 1.00 39.16 A N ANISOU 2157 N SER A 243 5249 5020 4611 142 121 -136 A N ATOM 2158 CA SER A 243 14.786 -6.021 4.308 1.00 37.82 A C ANISOU 2158 CA SER A 243 5043 4854 4474 76 60 -122 A C ATOM 2159 C SER A 243 15.066 -4.945 3.274 1.00 46.17 A C ANISOU 2159 C SER A 243 6118 5952 5471 61 58 -103 A C ATOM 2160 O SER A 243 16.163 -4.861 2.725 1.00 41.41 A O ANISOU 2160 O SER A 243 5521 5395 4818 94 123 -84 A O ATOM 2161 CB SER A 243 15.008 -5.432 5.704 1.00 41.48 A C ANISOU 2161 CB SER A 243 5421 5349 4991 64 68 -86 A C ATOM 2162 OG SER A 243 14.112 -4.370 5.988 1.00 41.46 A O ANISOU 2162 OG SER A 243 5391 5337 5026 10 20 -79 A O ATOM 2163 N GLY A 244 14.051 -4.121 3.020 1.00 37.46 A N ANISOU 2163 N GLY A 244 5020 4829 4383 15 -10 -100 A N ATOM 2164 CA GLY A 244 14.235 -2.831 2.392 1.00 37.96 A C ANISOU 2164 CA GLY A 244 5087 4924 4414 -5 -12 -59 A C ATOM 2165 C GLY A 244 14.102 -1.730 3.432 1.00 38.98 A C ANISOU 2165 C GLY A 244 5133 5056 4621 -46 -20 -29 A C ATOM 2166 O GLY A 244 13.584 -1.947 4.525 1.00 40.48 A O ANISOU 2166 O GLY A 244 5280 5226 4876 -56 -38 -45 A O ATOM 2167 N ILE A 245 14.594 -0.539 3.086 1.00 33.61 A N ANISOU 2167 N ILE A 245 4442 4396 3933 -67 2 15 A N ATOM 2168 CA ILE A 245 14.491 0.628 3.955 1.00 33.00 A C ANISOU 2168 CA ILE A 245 4303 4307 3927 -108 -7 34 A C ATOM 2169 C ILE A 245 14.237 1.846 3.088 1.00 34.72 A C ANISOU 2169 C ILE A 245 4556 4503 4134 -128 -17 81 A C ATOM 2170 O ILE A 245 14.919 2.046 2.076 1.00 36.24 A O ANISOU 2170 O ILE A 245 4789 4715 4264 -119 30 120 A O ATOM 2171 CB ILE A 245 15.758 0.863 4.804 1.00 33.83 A C ANISOU 2171 CB ILE A 245 4334 4454 4066 -122 43 39 A C ATOM 2172 CG1 ILE A 245 16.080 -0.350 5.671 1.00 37.73 A C ANISOU 2172 CG1 ILE A 245 4801 4973 4561 -85 50 7 A C ATOM 2173 CG2 ILE A 245 15.563 2.094 5.680 1.00 38.85 A C ANISOU 2173 CG2 ILE A 245 4926 5064 4770 -169 20 39 A C ATOM 2174 CD1 ILE A 245 17.412 -0.231 6.407 1.00 43.59 A C ANISOU 2174 CD1 ILE A 245 5463 5772 5328 -86 81 13 A C ATOM 2175 N GLY A 246 13.257 2.647 3.481 1.00 33.41 A N ANISOU 2175 N GLY A 246 4378 4291 4025 -147 -67 84 A N ATOM 2176 CA GLY A 246 12.992 3.916 2.821 1.00 34.43 A C ANISOU 2176 CA GLY A 246 4538 4385 4159 -159 -77 138 A C ATOM 2177 C GLY A 246 12.936 5.020 3.854 1.00 38.22 A C ANISOU 2177 C GLY A 246 4967 4823 4733 -195 -70 136 A C ATOM 2178 O GLY A 246 12.421 4.828 4.952 1.00 37.55 A O ANISOU 2178 O GLY A 246 4841 4727 4700 -196 -90 90 A O ATOM 2179 N LEU A 247 13.500 6.187 3.494 1.00 35.48 A N ANISOU 2179 N LEU A 247 4629 4445 4406 -225 -32 186 A N ATOM 2180 CA LEU A 247 13.482 7.361 4.362 1.00 34.88 A C ANISOU 2180 CA LEU A 247 4522 4310 4422 -265 -26 178 A C ATOM 2181 C LEU A 247 12.927 8.560 3.609 1.00 39.46 A C ANISOU 2181 C LEU A 247 5153 4814 5024 -259 -32 245 A C ATOM 2182 O LEU A 247 13.260 8.766 2.439 1.00 37.93 A O ANISOU 2182 O LEU A 247 5014 4624 4775 -251 -3 316 A O ATOM 2183 CB LEU A 247 14.875 7.747 4.871 1.00 36.15 A C ANISOU 2183 CB LEU A 247 4629 4484 4622 -324 28 167 A C ATOM 2184 CG LEU A 247 15.815 6.676 5.421 1.00 39.99 A C ANISOU 2184 CG LEU A 247 5057 5054 5084 -324 42 124 A C ATOM 2185 CD1 LEU A 247 17.196 7.280 5.613 1.00 41.47 A C ANISOU 2185 CD1 LEU A 247 5178 5251 5329 -388 87 132 A C ATOM 2186 CD2 LEU A 247 15.292 6.137 6.721 1.00 40.12 A C ANISOU 2186 CD2 LEU A 247 5050 5083 5111 -305 -4 54 A C ATOM 2187 N ALA A 248 12.112 9.370 4.292 1.00 36.69 A N ANISOU 2187 N ALA A 248 4795 4393 4752 -256 -59 227 A N ATOM 2188 CA ALA A 248 11.589 10.611 3.732 1.00 37.35 A C ANISOU 2188 CA ALA A 248 4926 4388 4877 -242 -61 293 A C ATOM 2189 C ALA A 248 11.530 11.658 4.835 1.00 41.53 A C ANISOU 2189 C ALA A 248 5435 4831 5513 -273 -44 250 A C ATOM 2190 O ALA A 248 11.576 11.338 6.022 1.00 43.93 A O ANISOU 2190 O ALA A 248 5696 5154 5841 -287 -48 166 A O ATOM 2191 CB ALA A 248 10.200 10.398 3.100 1.00 41.91 A C ANISOU 2191 CB ALA A 248 5531 4962 5432 -168 -137 323 A C ATOM 2192 N LYS A 249 11.423 12.922 4.437 1.00 39.87 A N ANISOU 2192 N LYS A 249 5268 4520 5359 -278 -23 309 A N ATOM 2193 CA ALYS A 249 11.384 14.035 5.374 0.46 40.65 A C ANISOU 2193 CA ALYS A 249 5367 4513 5563 -307 -2 265 A C ATOM 2194 CA BLYS A 249 11.378 14.030 5.378 0.54 40.62 A C ANISOU 2194 CA BLYS A 249 5364 4511 5560 -306 -3 264 A C ATOM 2195 C LYS A 249 10.189 14.926 5.075 1.00 44.69 A C ANISOU 2195 C LYS A 249 5924 4927 6131 -237 -21 315 A C ATOM 2196 O LYS A 249 9.883 15.200 3.913 1.00 44.77 A O ANISOU 2196 O LYS A 249 5981 4918 6112 -196 -32 418 A O ATOM 2197 CB ALYS A 249 12.676 14.851 5.298 0.46 43.25 A C ANISOU 2197 CB ALYS A 249 5701 4786 5945 -399 57 281 A C ATOM 2198 CB BLYS A 249 12.666 14.855 5.330 0.54 43.23 A C ANISOU 2198 CB BLYS A 249 5698 4784 5944 -399 57 279 A C ATOM 2199 CG ALYS A 249 12.706 16.044 6.221 0.46 44.94 A C ANISOU 2199 CG ALYS A 249 5928 4875 6273 -441 71 222 A C ATOM 2200 CG BLYS A 249 12.685 15.991 6.325 0.54 44.94 A C ANISOU 2200 CG BLYS A 249 5924 4879 6271 -440 68 212 A C ATOM 2201 CD ALYS A 249 14.081 16.679 6.225 0.46 49.27 A C ANISOU 2201 CD ALYS A 249 6455 5376 6889 -554 119 222 A C ATOM 2202 CD BLYS A 249 13.921 16.840 6.167 0.54 49.78 A C ANISOU 2202 CD BLYS A 249 6533 5421 6962 -545 121 230 A C ATOM 2203 CE ALYS A 249 14.171 17.786 7.257 0.46 50.18 A C ANISOU 2203 CE ALYS A 249 6587 5363 7117 -607 117 132 A C ATOM 2204 CE BLYS A 249 13.853 18.047 7.082 0.54 49.31 A C ANISOU 2204 CE BLYS A 249 6501 5215 7018 -587 123 155 A C ATOM 2205 NZ ALYS A 249 13.757 19.091 6.680 0.46 51.87 A N ANISOU 2205 NZ ALYS A 249 6878 5411 7421 -599 161 210 A N ATOM 2206 NZ BLYS A 249 15.140 18.782 7.115 0.54 52.44 A N ANISOU 2206 NZ BLYS A 249 6871 5542 7512 -713 162 147 A N ATOM 2207 N GLY A 250 9.523 15.387 6.123 1.00 41.84 A N ANISOU 2207 N GLY A 250 5552 4503 5844 -213 -23 246 A N ATOM 2208 CA GLY A 250 8.450 16.338 5.903 1.00 45.10 A C ANISOU 2208 CA GLY A 250 5998 4809 6329 -139 -30 294 A C ATOM 2209 C GLY A 250 7.762 16.718 7.192 1.00 44.97 A C ANISOU 2209 C GLY A 250 5968 4733 6387 -106 -12 201 A C ATOM 2210 O GLY A 250 8.091 16.231 8.277 1.00 44.42 A O ANISOU 2210 O GLY A 250 5872 4709 6296 -139 1 100 A O ATOM 2211 N LYS A 251 6.790 17.614 7.047 1.00 45.41 A N ANISOU 2211 N LYS A 251 5921 4359 6975 45 107 660 A N ATOM 2212 CA LYS A 251 6.026 18.110 8.184 1.00 45.87 A C ANISOU 2212 CA LYS A 251 5974 4333 7122 82 141 535 A C ATOM 2213 C LYS A 251 4.912 17.121 8.490 1.00 46.56 A C ANISOU 2213 C LYS A 251 6007 4647 7036 141 12 522 A C ATOM 2214 O LYS A 251 4.099 16.814 7.611 1.00 50.46 A O ANISOU 2214 O LYS A 251 6466 5283 7424 246 -31 686 A O ATOM 2215 CB LYS A 251 5.459 19.494 7.876 1.00 49.70 A C ANISOU 2215 CB LYS A 251 6494 4590 7800 217 307 670 A C ATOM 2216 CG LYS A 251 4.501 20.042 8.927 1.00 60.76 A C ANISOU 2216 CG LYS A 251 7886 5906 9295 289 358 557 A C ATOM 2217 CD LYS A 251 3.497 21.026 8.325 1.00107.14 A C ANISOU 2217 CD LYS A 251 13771 11656 15282 513 486 786 A C ATOM 2218 CE LYS A 251 2.214 20.332 7.869 1.00125.19 A C ANISOU 2218 CE LYS A 251 15973 14235 17360 670 357 938 A C ATOM 2219 NZ LYS A 251 0.988 21.067 8.301 1.00107.81 A N ANISOU 2219 NZ LYS A 251 13744 11972 15246 856 439 982 A N ATOM 2220 N VAL A 252 4.854 16.638 9.730 1.00 41.81 A N ANISOU 2220 N VAL A 252 5385 4104 6397 71 -41 327 A N ATOM 2221 CA VAL A 252 3.838 15.679 10.141 1.00 40.13 A C ANISOU 2221 CA VAL A 252 5126 4086 6038 105 -140 303 A C ATOM 2222 C VAL A 252 3.156 16.197 11.403 1.00 45.07 A C ANISOU 2222 C VAL A 252 5730 4667 6729 136 -105 165 A C ATOM 2223 O VAL A 252 3.646 17.105 12.076 1.00 44.64 A O ANISOU 2223 O VAL A 252 5693 4452 6814 97 -18 39 A O ATOM 2224 CB VAL A 252 4.417 14.268 10.377 1.00 41.30 A C ANISOU 2224 CB VAL A 252 5265 4389 6038 0 -232 233 A C ATOM 2225 CG1 VAL A 252 5.050 13.715 9.088 1.00 46.21 A C ANISOU 2225 CG1 VAL A 252 5903 5061 6593 -29 -256 349 A C ATOM 2226 CG2 VAL A 252 5.432 14.259 11.528 1.00 42.36 A C ANISOU 2226 CG2 VAL A 252 5399 4500 6197 -95 -224 61 A C ATOM 2227 N ILE A 253 1.987 15.630 11.700 1.00 39.16 A N ANISOU 2227 N ILE A 253 4932 4069 5878 195 -163 172 A N ATOM 2228 CA ILE A 253 1.288 15.924 12.948 1.00 38.64 A C ANISOU 2228 CA ILE A 253 4833 4010 5838 220 -144 35 A C ATOM 2229 C ILE A 253 1.708 14.875 13.968 1.00 41.03 A C ANISOU 2229 C ILE A 253 5116 4454 6019 112 -212 -101 A C ATOM 2230 O ILE A 253 1.672 13.675 13.684 1.00 43.57 A O ANISOU 2230 O ILE A 253 5431 4911 6211 76 -279 -45 A O ATOM 2231 CB ILE A 253 -0.237 15.933 12.748 1.00 40.81 A C ANISOU 2231 CB ILE A 253 5048 4392 6064 351 -157 124 A C ATOM 2232 CG1 ILE A 253 -0.616 17.067 11.806 1.00 46.95 A C ANISOU 2232 CG1 ILE A 253 5833 5046 6960 503 -70 292 A C ATOM 2233 CG2 ILE A 253 -0.934 16.152 14.071 1.00 45.20 A C ANISOU 2233 CG2 ILE A 253 5564 4975 6634 371 -137 -27 A C ATOM 2234 CD1 ILE A 253 -2.040 16.999 11.283 1.00 55.04 A C ANISOU 2234 CD1 ILE A 253 6767 6251 7893 654 -96 430 A C ATOM 2235 N GLU A 254 2.136 15.323 15.144 1.00 39.49 A N ANISOU 2235 N GLU A 254 4904 4233 5866 65 -176 -278 A N ATOM 2236 CA GLU A 254 2.537 14.438 16.228 1.00 40.79 A C ANISOU 2236 CA GLU A 254 5030 4572 5898 -4 -228 -385 A C ATOM 2237 C GLU A 254 1.573 14.648 17.385 1.00 45.69 A C ANISOU 2237 C GLU A 254 5593 5277 6492 38 -213 -498 A C ATOM 2238 O GLU A 254 1.384 15.779 17.838 1.00 46.16 A O ANISOU 2238 O GLU A 254 5638 5232 6669 56 -138 -623 A O ATOM 2239 CB GLU A 254 3.973 14.722 16.668 1.00 44.34 A C ANISOU 2239 CB GLU A 254 5467 5016 6364 -103 -209 -514 A C ATOM 2240 CG GLU A 254 4.479 13.785 17.747 1.00 44.49 A C ANISOU 2240 CG GLU A 254 5423 5267 6215 -139 -260 -584 A C ATOM 2241 CD GLU A 254 5.949 13.994 18.045 1.00 59.95 A C ANISOU 2241 CD GLU A 254 7337 7286 8156 -229 -253 -697 A C ATOM 2242 OE1 GLU A 254 6.453 15.103 17.798 1.00 55.45 A O ANISOU 2242 OE1 GLU A 254 6773 6567 7728 -294 -186 -806 A O ATOM 2243 OE2 GLU A 254 6.612 13.025 18.460 1.00 59.80 A O ANISOU 2243 OE2 GLU A 254 7276 7460 7987 -229 -300 -664 A O ATOM 2244 N GLY A 255 0.948 13.578 17.858 1.00 39.51 A N ANISOU 2244 N GLY A 255 4778 4667 5568 49 -263 -459 A N ATOM 2245 CA GLY A 255 0.045 13.734 18.983 1.00 42.54 A C ANISOU 2245 CA GLY A 255 5098 5157 5909 87 -246 -561 A C ATOM 2246 C GLY A 255 -0.685 12.443 19.284 1.00 39.65 A C ANISOU 2246 C GLY A 255 4707 4960 5399 91 -283 -475 A C ATOM 2247 O GLY A 255 -0.351 11.383 18.757 1.00 37.87 A O ANISOU 2247 O GLY A 255 4518 4759 5112 53 -307 -362 A O ATOM 2248 N ASN A 256 -1.680 12.557 20.159 1.00 39.37 A N ANISOU 2248 N ASN A 256 4609 5028 5322 131 -265 -541 A N ATOM 2249 CA ASN A 256 -2.495 11.420 20.566 1.00 40.64 A C ANISOU 2249 CA ASN A 256 4739 5343 5360 125 -270 -472 A C ATOM 2250 C ASN A 256 -3.618 11.223 19.564 1.00 39.84 A C ANISOU 2250 C ASN A 256 4632 5221 5285 145 -277 -377 A C ATOM 2251 O ASN A 256 -4.478 12.098 19.399 1.00 41.48 A O ANISOU 2251 O ASN A 256 4797 5409 5554 221 -266 -405 A O ATOM 2252 CB ASN A 256 -3.075 11.624 21.961 1.00 40.04 A C ANISOU 2252 CB ASN A 256 4581 5423 5210 155 -244 -585 A C ATOM 2253 CG ASN A 256 -2.020 11.536 23.044 1.00 43.05 A C ANISOU 2253 CG ASN A 256 4928 5932 5495 130 -242 -671 A C ATOM 2254 ND2 ASN A 256 -1.834 12.627 23.760 1.00 47.29 A N ANISOU 2254 ND2 ASN A 256 5410 6494 6062 136 -221 -865 A N ATOM 2255 OD1 ASN A 256 -1.355 10.509 23.211 1.00 42.78 A O ANISOU 2255 OD1 ASN A 256 4908 5984 5361 109 -249 -569 A O ATOM 2256 N AILE A 257 -3.645 10.048 18.936 0.58 38.10 A N ANISOU 2256 N AILE A 257 4439 5025 5011 79 -282 -276 A N ATOM 2257 N BILE A 257 -3.608 10.078 18.902 0.42 38.28 A N ANISOU 2257 N BILE A 257 4464 5042 5037 80 -283 -275 A N ATOM 2258 CA AILE A 257 -4.558 9.740 17.841 0.58 41.75 A C ANISOU 2258 CA AILE A 257 4875 5516 5472 64 -290 -212 A C ATOM 2259 CA BILE A 257 -4.582 9.742 17.879 0.42 41.76 A C ANISOU 2259 CA BILE A 257 4875 5520 5472 65 -290 -214 A C ATOM 2260 C AILE A 257 -5.199 8.387 18.121 0.58 41.44 A C ANISOU 2260 C AILE A 257 4814 5584 5348 -26 -246 -193 A C ATOM 2261 C BILE A 257 -5.220 8.423 18.279 0.42 41.48 A C ANISOU 2261 C BILE A 257 4816 5596 5350 -21 -244 -199 A C ATOM 2262 O AILE A 257 -4.487 7.387 18.278 0.58 43.51 A O ANISOU 2262 O AILE A 257 5139 5807 5587 -93 -206 -151 A O ATOM 2263 O BILE A 257 -4.524 7.493 18.701 0.42 43.47 A O ANISOU 2263 O BILE A 257 5123 5822 5570 -75 -202 -163 A O ATOM 2264 CB AILE A 257 -3.818 9.719 16.489 0.58 43.57 A C ANISOU 2264 CB AILE A 257 5163 5649 5744 40 -318 -140 A C ATOM 2265 CB BILE A 257 -3.936 9.641 16.482 0.42 43.49 A C ANISOU 2265 CB BILE A 257 5146 5652 5726 36 -316 -140 A C ATOM 2266 CG1AILE A 257 -3.345 11.135 16.121 0.58 41.83 A C ANISOU 2266 CG1AILE A 257 4961 5303 5629 131 -331 -139 A C ATOM 2267 CG1BILE A 257 -2.929 10.780 16.254 0.42 41.38 A C ANISOU 2267 CG1BILE A 257 4928 5237 5557 94 -331 -143 A C ATOM 2268 CG2AILE A 257 -4.696 9.094 15.417 0.58 42.90 A C ANISOU 2268 CG2AILE A 257 5026 5667 5607 -8 -323 -98 A C ATOM 2269 CG2BILE A 257 -5.013 9.641 15.415 0.42 44.80 A C ANISOU 2269 CG2BILE A 257 5237 5920 5863 46 -333 -99 A C ATOM 2270 CD1AILE A 257 -2.054 11.172 15.328 0.58 49.29 A C ANISOU 2270 CD1AILE A 257 5982 6126 6618 95 -343 -91 A C ATOM 2271 CD1BILE A 257 -3.545 12.089 15.820 0.42 45.51 A C ANISOU 2271 CD1BILE A 257 5415 5713 6164 210 -324 -127 A C ATOM 2272 N GLY A 258 -6.528 8.350 18.173 1.00 40.90 A N ANISOU 2272 N GLY A 258 4653 5644 5242 -26 -233 -218 A N ATOM 2273 CA GLY A 258 -7.235 7.105 18.431 1.00 43.60 A C ANISOU 2273 CA GLY A 258 4966 6079 5522 -138 -163 -218 A C ATOM 2274 C GLY A 258 -8.637 7.346 18.959 1.00 42.87 A C ANISOU 2274 C GLY A 258 4753 6155 5383 -116 -149 -271 A C ATOM 2275 O GLY A 258 -9.244 8.391 18.725 1.00 48.61 A O ANISOU 2275 O GLY A 258 5404 6944 6121 -10 -199 -296 A O ATOM 2276 N SER A 259 -9.152 6.330 19.646 1.00 45.69 A N ANISOU 2276 N SER A 259 5090 6580 5691 -210 -61 -275 A N ATOM 2277 CA SER A 259 -10.501 6.333 20.192 1.00 49.61 A C ANISOU 2277 CA SER A 259 5464 7256 6132 -220 -28 -327 A C ATOM 2278 C SER A 259 -10.464 6.599 21.692 1.00 51.63 A C ANISOU 2278 C SER A 259 5715 7554 6348 -144 -1 -334 A C ATOM 2279 O SER A 259 -9.404 6.637 22.315 1.00 49.97 A O ANISOU 2279 O SER A 259 5586 7263 6138 -100 -1 -300 A O ATOM 2280 CB SER A 259 -11.186 4.987 19.926 1.00 51.45 A C ANISOU 2280 CB SER A 259 5664 7544 6339 -406 81 -341 A C ATOM 2281 OG SER A 259 -10.541 3.967 20.689 1.00 51.19 A O ANISOU 2281 OG SER A 259 5737 7393 6321 -468 195 -268 A O ATOM 2282 N GLU A 260 -11.649 6.752 22.288 1.00 55.38 A N ANISOU 2282 N GLU A 260 6074 8200 6770 -132 27 -386 A N ATOM 2283 CA GLU A 260 -11.700 6.812 23.746 1.00 57.46 A C ANISOU 2283 CA GLU A 260 6317 8547 6969 -81 71 -395 A C ATOM 2284 C GLU A 260 -11.178 5.521 24.365 1.00 51.51 A C ANISOU 2284 C GLU A 260 5639 7756 6177 -169 181 -289 A C ATOM 2285 O GLU A 260 -10.692 5.523 25.501 1.00 65.86 A O ANISOU 2285 O GLU A 260 7467 9631 7924 -103 207 -255 A O ATOM 2286 CB GLU A 260 -13.128 7.072 24.243 1.00 61.76 A C ANISOU 2286 CB GLU A 260 6715 9295 7457 -65 97 -465 A C ATOM 2287 CG GLU A 260 -13.869 8.183 23.538 1.00 79.30 A C ANISOU 2287 CG GLU A 260 8840 11578 9713 40 20 -534 A C ATOM 2288 CD GLU A 260 -14.734 7.669 22.408 1.00 88.74 A C ANISOU 2288 CD GLU A 260 9947 12874 10895 -58 21 -530 A C ATOM 2289 OE1 GLU A 260 -14.276 6.761 21.679 1.00 70.72 A O ANISOU 2289 OE1 GLU A 260 7733 10506 8632 -196 46 -492 A O ATOM 2290 OE2 GLU A 260 -15.877 8.157 22.263 1.00 94.36 A O ANISOU 2290 OE2 GLU A 260 10508 13776 11568 3 6 -578 A O ATOM 2291 N LEU A 261 -11.271 4.414 23.630 1.00 55.45 A N ANISOU 2291 N LEU A 261 6181 8169 6718 -311 262 -237 A N ATOM 2292 CA LEU A 261 -10.897 3.107 24.150 1.00 59.01 A C ANISOU 2292 CA LEU A 261 6712 8544 7166 -388 415 -114 A C ATOM 2293 C LEU A 261 -9.384 2.920 24.135 1.00 61.97 A C ANISOU 2293 C LEU A 261 7212 8771 7561 -318 402 -12 A C ATOM 2294 O LEU A 261 -8.807 2.354 25.072 1.00 55.37 A O ANISOU 2294 O LEU A 261 6419 7946 6672 -262 488 118 A O ATOM 2295 CB LEU A 261 -11.570 2.026 23.306 1.00 65.31 A C ANISOU 2295 CB LEU A 261 7509 9275 8030 -585 536 -135 A C ATOM 2296 CG LEU A 261 -12.903 1.401 23.736 1.00 79.56 A C ANISOU 2296 CG LEU A 261 9213 11205 9810 -716 670 -172 A C ATOM 2297 CD1 LEU A 261 -13.009 -0.007 23.131 1.00 75.12 A C ANISOU 2297 CD1 LEU A 261 8714 10483 9346 -930 863 -164 A C ATOM 2298 CD2 LEU A 261 -13.098 1.355 25.250 1.00 73.28 A C ANISOU 2298 CD2 LEU A 261 8392 10522 8927 -630 741 -79 A C ATOM 2299 N LYS A 262 -8.724 3.402 23.087 1.00 47.79 A N ANISOU 2299 N LYS A 262 5464 6865 5829 -308 298 -55 A N ATOM 2300 CA LYS A 262 -7.306 3.157 22.913 1.00 42.84 A C ANISOU 2300 CA LYS A 262 4945 6103 5227 -260 291 33 A C ATOM 2301 C LYS A 262 -6.731 4.242 22.020 1.00 46.98 A C ANISOU 2301 C LYS A 262 5479 6573 5797 -212 141 -48 A C ATOM 2302 O LYS A 262 -7.282 4.519 20.952 1.00 44.36 A O ANISOU 2302 O LYS A 262 5120 6222 5514 -268 96 -116 A O ATOM 2303 CB LYS A 262 -7.061 1.782 22.298 1.00 48.35 A C ANISOU 2303 CB LYS A 262 5738 6632 6002 -374 437 118 A C ATOM 2304 CG LYS A 262 -5.604 1.367 22.318 1.00 55.68 A C ANISOU 2304 CG LYS A 262 6772 7441 6945 -296 461 241 A C ATOM 2305 CD LYS A 262 -5.022 1.405 20.925 1.00 56.28 A C ANISOU 2305 CD LYS A 262 6907 7371 7106 -353 407 188 A C ATOM 2306 CE LYS A 262 -3.674 0.705 20.851 1.00 62.30 A C ANISOU 2306 CE LYS A 262 7775 7999 7899 -295 475 318 A C ATOM 2307 NZ LYS A 262 -2.562 1.626 21.169 1.00 61.82 A N ANISOU 2307 NZ LYS A 262 7699 8014 7774 -158 336 331 A N ATOM 2308 N ARG A 263 -5.643 4.860 22.454 1.00 44.41 A N ANISOU 2308 N ARG A 263 5178 6246 5448 -112 75 -40 A N ATOM 2309 CA AARG A 263 -4.936 5.886 21.701 0.50 43.41 A C ANISOU 2309 CA AARG A 263 5073 6041 5380 -72 -37 -104 A C ATOM 2310 CA BARG A 263 -4.964 5.802 21.582 0.50 43.55 A C ANISOU 2310 CA BARG A 263 5095 6047 5404 -82 -33 -99 A C ATOM 2311 C ARG A 263 -3.483 5.481 21.488 1.00 44.43 A C ANISOU 2311 C ARG A 263 5285 6079 5518 -58 -34 -28 A C ATOM 2312 O ARG A 263 -2.938 4.654 22.223 1.00 41.79 A O ANISOU 2312 O ARG A 263 4973 5784 5121 -29 39 74 A O ATOM 2313 CB AARG A 263 -4.994 7.239 22.427 0.50 49.19 A C ANISOU 2313 CB AARG A 263 5736 6859 6094 17 -106 -221 A C ATOM 2314 CB BARG A 263 -5.178 7.251 22.028 0.50 50.40 A C ANISOU 2314 CB BARG A 263 5894 6981 6273 2 -113 -220 A C ATOM 2315 CG AARG A 263 -6.213 8.083 22.066 0.50 50.56 A C ANISOU 2315 CG AARG A 263 5839 7058 6312 38 -137 -305 A C ATOM 2316 CG BARG A 263 -4.504 7.643 23.309 0.50 50.60 A C ANISOU 2316 CG BARG A 263 5888 7118 6221 68 -117 -266 A C ATOM 2317 CD AARG A 263 -6.677 8.948 23.223 0.50 56.80 A C ANISOU 2317 CD AARG A 263 6548 7971 7062 115 -138 -416 A C ATOM 2318 CD BARG A 263 -5.256 8.802 23.959 0.50 53.85 A C ANISOU 2318 CD BARG A 263 6211 7619 6630 124 -140 -413 A C ATOM 2319 NE AARG A 263 -8.103 9.237 23.120 0.50 61.50 A N ANISOU 2319 NE AARG A 263 7058 8645 7663 136 -128 -454 A N ATOM 2320 NE BARG A 263 -6.595 8.434 24.404 0.50 60.19 A N ANISOU 2320 NE BARG A 263 6946 8541 7383 118 -93 -406 A N ATOM 2321 CZ AARG A 263 -8.656 9.932 22.134 0.50 60.53 A C ANISOU 2321 CZ AARG A 263 6911 8468 7619 180 -163 -463 A C ATOM 2322 CZ BARG A 263 -7.438 9.262 25.010 0.50 58.51 A C ANISOU 2322 CZ BARG A 263 6646 8426 7158 173 -94 -523 A C ATOM 2323 NH1AARG A 263 -7.921 10.492 21.187 0.50 60.91 A N ANISOU 2323 NH1AARG A 263 7023 8362 7757 205 -204 -438 A N ATOM 2324 NH1BARG A 263 -7.101 10.512 25.287 0.50 62.00 A N ANISOU 2324 NH1BARG A 263 7067 8841 7651 235 -123 -668 A N ATOM 2325 NH2AARG A 263 -9.978 10.067 22.095 0.50 60.70 A N ANISOU 2325 NH2AARG A 263 6831 8616 7618 209 -150 -483 A N ATOM 2326 NH2BARG A 263 -8.648 8.826 25.347 0.50 64.29 A N ANISOU 2326 NH2BARG A 263 7309 9281 7837 157 -48 -506 A N ATOM 2327 N AASP A 264 -2.859 6.125 20.503 0.28 38.03 A N ANISOU 2327 N AASP A 264 4509 5163 4779 -60 -109 -63 A N ATOM 2328 N BASP A 264 -2.870 6.072 20.467 0.72 37.59 A N ANISOU 2328 N BASP A 264 4455 5103 4723 -64 -106 -60 A N ATOM 2329 CA AASP A 264 -1.447 5.968 20.190 0.28 41.21 A C ANISOU 2329 CA AASP A 264 4973 5492 5194 -45 -123 -15 A C ATOM 2330 CA BASP A 264 -1.447 5.996 20.209 0.72 41.16 A C ANISOU 2330 CA BASP A 264 4965 5488 5187 -43 -125 -17 A C ATOM 2331 C AASP A 264 -0.820 7.350 20.090 0.28 40.18 A C ANISOU 2331 C AASP A 264 4821 5344 5102 -7 -211 -115 A C ATOM 2332 C BASP A 264 -0.896 7.410 20.266 0.72 39.94 A C ANISOU 2332 C BASP A 264 4779 5333 5062 -0 -211 -125 A C ATOM 2333 O AASP A 264 -1.380 8.235 19.433 0.28 41.52 A O ANISOU 2333 O AASP A 264 4977 5451 5345 -7 -251 -174 A O ATOM 2334 O BASP A 264 -1.586 8.367 19.891 0.72 41.93 A O ANISOU 2334 O BASP A 264 5005 5549 5378 8 -247 -200 A O ATOM 2335 CB AASP A 264 -1.243 5.227 18.865 0.28 45.86 A C ANISOU 2335 CB AASP A 264 5635 5942 5847 -118 -95 41 A C ATOM 2336 CB BASP A 264 -1.106 5.424 18.817 0.72 46.76 A C ANISOU 2336 CB BASP A 264 5748 6053 5966 -110 -112 32 A C ATOM 2337 CG AASP A 264 -1.518 3.750 18.973 0.28 43.91 A C ANISOU 2337 CG AASP A 264 5432 5659 5594 -172 37 128 A C ATOM 2338 CG BASP A 264 -1.716 4.070 18.557 0.72 42.35 A C ANISOU 2338 CG BASP A 264 5223 5452 5415 -191 2 90 A C ATOM 2339 OD1AASP A 264 -0.832 3.072 19.765 0.28 43.59 A O ANISOU 2339 OD1AASP A 264 5418 5632 5511 -112 109 232 A O ATOM 2340 OD1BASP A 264 -1.802 3.248 19.496 0.72 44.53 A O ANISOU 2340 OD1BASP A 264 5508 5762 5651 -173 101 166 A O ATOM 2341 OD2AASP A 264 -2.420 3.267 18.258 0.28 45.16 A O ANISOU 2341 OD2AASP A 264 5587 5781 5789 -274 83 94 A O ATOM 2342 OD2BASP A 264 -2.065 3.816 17.382 0.72 39.10 A O ANISOU 2342 OD2BASP A 264 4827 4979 5051 -277 7 58 A O ATOM 2343 N TYR A 265 0.327 7.535 20.728 1.00 39.67 A N ANISOU 2343 N TYR A 265 4742 5344 4989 28 -226 -133 A N ATOM 2344 CA TYR A 265 1.095 8.768 20.595 1.00 37.50 A C ANISOU 2344 CA TYR A 265 4448 5032 4769 28 -280 -250 A C ATOM 2345 C TYR A 265 1.982 8.544 19.376 1.00 38.33 A C ANISOU 2345 C TYR A 265 4625 5000 4939 -6 -294 -179 A C ATOM 2346 O TYR A 265 2.903 7.724 19.428 1.00 41.33 A O ANISOU 2346 O TYR A 265 5024 5418 5263 4 -276 -99 A O ATOM 2347 CB TYR A 265 1.903 9.077 21.842 1.00 42.37 A C ANISOU 2347 CB TYR A 265 4982 5836 5282 54 -286 -341 A C ATOM 2348 CG TYR A 265 2.532 10.441 21.754 1.00 42.33 A C ANISOU 2348 CG TYR A 265 4947 5777 5359 16 -311 -516 A C ATOM 2349 CD1 TYR A 265 1.833 11.575 22.119 1.00 49.23 A C ANISOU 2349 CD1 TYR A 265 5784 6616 6305 12 -296 -676 A C ATOM 2350 CD2 TYR A 265 3.812 10.595 21.244 1.00 43.69 A C ANISOU 2350 CD2 TYR A 265 5133 5910 5558 -22 -328 -524 A C ATOM 2351 CE1 TYR A 265 2.408 12.834 22.011 1.00 54.21 A C ANISOU 2351 CE1 TYR A 265 6402 7145 7050 -37 -277 -845 A C ATOM 2352 CE2 TYR A 265 4.399 11.846 21.138 1.00 51.10 A C ANISOU 2352 CE2 TYR A 265 6047 6774 6595 -84 -322 -695 A C ATOM 2353 CZ TYR A 265 3.690 12.959 21.518 1.00 52.84 A C ANISOU 2353 CZ TYR A 265 6242 6929 6905 -95 -286 -856 A C ATOM 2354 OH TYR A 265 4.265 14.206 21.405 1.00 57.61 A O ANISOU 2354 OH TYR A 265 6835 7412 7643 -169 -239 -1035 A O ATOM 2355 N THR A 266 1.674 9.208 18.263 1.00 37.68 A N ANISOU 2355 N THR A 266 4578 4775 4964 -28 -316 -188 A N ATOM 2356 CA THR A 266 2.310 8.837 16.995 1.00 39.13 A C ANISOU 2356 CA THR A 266 4825 4854 5190 -62 -323 -105 A C ATOM 2357 C THR A 266 2.241 10.009 16.017 1.00 43.75 A C ANISOU 2357 C THR A 266 5423 5317 5883 -60 -345 -123 A C ATOM 2358 O THR A 266 1.920 11.139 16.399 1.00 40.49 A O ANISOU 2358 O THR A 266 4981 4868 5535 -29 -338 -205 A O ATOM 2359 CB THR A 266 1.655 7.557 16.450 1.00 39.30 A C ANISOU 2359 CB THR A 266 4880 4873 5178 -94 -286 -16 A C ATOM 2360 CG2 THR A 266 0.258 7.812 15.937 1.00 42.40 A C ANISOU 2360 CG2 THR A 266 5242 5278 5591 -105 -294 -30 A C ATOM 2361 OG1 THR A 266 2.460 7.006 15.396 1.00 41.11 A O ANISOU 2361 OG1 THR A 266 5165 5027 5427 -131 -277 44 A O ATOM 2362 N ILE A 267 2.582 9.753 14.748 1.00 37.10 A N ANISOU 2362 N ILE A 267 4624 4407 5064 -86 -352 -42 A N ATOM 2363 CA ILE A 267 2.624 10.806 13.741 1.00 36.77 A C ANISOU 2363 CA ILE A 267 4595 4263 5114 -65 -357 -12 A C ATOM 2364 C ILE A 267 1.675 10.476 12.598 1.00 41.29 A C ANISOU 2364 C ILE A 267 5155 4878 5654 -52 -369 76 A C ATOM 2365 O ILE A 267 1.330 9.321 12.344 1.00 42.86 A O ANISOU 2365 O ILE A 267 5351 5158 5776 -103 -368 90 A O ATOM 2366 CB ILE A 267 4.049 11.068 13.183 1.00 35.67 A C ANISOU 2366 CB ILE A 267 4493 4044 5017 -104 -352 3 A C ATOM 2367 CG1 ILE A 267 4.638 9.784 12.586 1.00 40.46 A C ANISOU 2367 CG1 ILE A 267 5130 4695 5548 -146 -360 66 A C ATOM 2368 CG2 ILE A 267 4.959 11.657 14.245 1.00 40.65 A C ANISOU 2368 CG2 ILE A 267 5100 4671 5677 -129 -337 -118 A C ATOM 2369 CD1 ILE A 267 5.898 10.036 11.775 1.00 44.93 A C ANISOU 2369 CD1 ILE A 267 5722 5200 6148 -178 -357 98 A C ATOM 2370 N LEU A 268 1.281 11.538 11.891 1.00 39.90 A N ANISOU 2370 N LEU A 268 4964 4656 5542 17 -363 134 A N ATOM 2371 CA ALEU A 268 0.359 11.489 10.765 0.59 40.99 A C ANISOU 2371 CA ALEU A 268 5052 4897 5626 60 -379 229 A C ATOM 2372 CA BLEU A 268 0.373 11.475 10.756 0.41 41.00 A C ANISOU 2372 CA BLEU A 268 5054 4898 5626 59 -380 229 A C ATOM 2373 C LEU A 268 0.838 12.478 9.710 1.00 41.37 A C ANISOU 2373 C LEU A 268 5117 4861 5740 126 -357 347 A C ATOM 2374 O LEU A 268 1.109 13.633 10.042 1.00 46.62 A O ANISOU 2374 O LEU A 268 5810 5369 6533 187 -305 354 A O ATOM 2375 CB ALEU A 268 -1.059 11.883 11.207 0.59 46.22 A C ANISOU 2375 CB ALEU A 268 5639 5648 6276 144 -378 219 A C ATOM 2376 CB BLEU A 268 -1.056 11.800 11.209 0.41 46.19 A C ANISOU 2376 CB BLEU A 268 5634 5649 6265 137 -379 216 A C ATOM 2377 CG ALEU A 268 -2.123 10.862 11.565 0.59 47.84 A C ANISOU 2377 CG ALEU A 268 5778 6027 6373 91 -395 161 A C ATOM 2378 CG BLEU A 268 -2.243 11.365 10.367 0.41 49.34 A C ANISOU 2378 CG BLEU A 268 5935 6264 6550 155 -406 267 A C ATOM 2379 CD1ALEU A 268 -3.346 11.613 12.099 0.59 45.21 A C ANISOU 2379 CD1ALEU A 268 5366 5758 6053 201 -386 154 A C ATOM 2380 CD1BLEU A 268 -2.394 9.873 10.451 0.41 54.14 A C ANISOU 2380 CD1BLEU A 268 6533 6978 7061 10 -413 180 A C ATOM 2381 CD2ALEU A 268 -2.492 10.053 10.346 0.59 54.80 A C ANISOU 2381 CD2ALEU A 268 6605 7072 7145 31 -416 195 A C ATOM 2382 CD2BLEU A 268 -3.494 12.048 10.878 0.41 47.54 A C ANISOU 2382 CD2BLEU A 268 5623 6109 6329 271 -397 270 A C ATOM 2383 N GLY A 269 0.919 12.063 8.448 1.00 43.66 A N ANISOU 2383 N GLY A 269 5386 5256 5947 113 -379 434 A N ATOM 2384 CA GLY A 269 1.232 13.025 7.401 1.00 43.45 A C ANISOU 2384 CA GLY A 269 5362 5184 5965 200 -346 586 A C ATOM 2385 C GLY A 269 1.782 12.393 6.140 1.00 42.09 A C ANISOU 2385 C GLY A 269 5178 5126 5687 145 -370 647 A C ATOM 2386 O GLY A 269 2.137 11.217 6.104 1.00 39.07 A O ANISOU 2386 O GLY A 269 4807 4809 5230 25 -399 550 A O ATOM 2387 N ASP A 270 1.907 13.240 5.102 1.00 43.62 A N ANISOU 2387 N ASP A 270 5354 5331 5890 244 -337 819 A N ATOM 2388 CA AASP A 270 2.259 12.748 3.772 0.35 46.82 A C ANISOU 2388 CA AASP A 270 5718 5908 6162 214 -359 892 A C ATOM 2389 CA BASP A 270 2.258 12.750 3.771 0.65 46.83 A C ANISOU 2389 CA BASP A 270 5720 5909 6164 214 -359 893 A C ATOM 2390 C ASP A 270 3.641 12.110 3.738 1.00 43.30 A C ANISOU 2390 C ASP A 270 5353 5358 5741 78 -357 808 A C ATOM 2391 O ASP A 270 3.875 11.184 2.954 1.00 44.12 A O ANISOU 2391 O ASP A 270 5427 5615 5721 -0 -383 771 A O ATOM 2392 CB AASP A 270 2.192 13.884 2.745 0.35 48.76 A C ANISOU 2392 CB AASP A 270 5929 6183 6413 372 -306 1132 A C ATOM 2393 CB BASP A 270 2.188 13.898 2.752 0.65 48.74 A C ANISOU 2393 CB BASP A 270 5928 6179 6413 374 -305 1133 A C ATOM 2394 CG AASP A 270 2.429 13.401 1.323 0.35 51.43 A C ANISOU 2394 CG AASP A 270 6196 6773 6573 356 -333 1214 A C ATOM 2395 CG BASP A 270 0.773 14.404 2.526 0.65 53.20 A C ANISOU 2395 CG BASP A 270 6377 6932 6903 546 -308 1255 A C ATOM 2396 OD1AASP A 270 1.677 12.517 0.861 0.35 50.40 A O ANISOU 2396 OD1AASP A 270 5954 6939 6255 313 -397 1138 A O ATOM 2397 OD1BASP A 270 -0.184 13.634 2.719 0.65 55.36 A O ANISOU 2397 OD1BASP A 270 6559 7425 7050 508 -375 1145 A O ATOM 2398 OD2AASP A 270 3.373 13.898 0.671 0.35 48.76 A O ANISOU 2398 OD2AASP A 270 5902 6347 6277 372 -281 1336 A O ATOM 2399 OD2BASP A 270 0.615 15.582 2.149 0.65 58.96 A O ANISOU 2399 OD2BASP A 270 7103 7592 7708 726 -226 1471 A O ATOM 2400 N ALA A 271 4.575 12.591 4.563 1.00 40.82 A N ANISOU 2400 N ALA A 271 5126 4807 5578 46 -318 763 A N ATOM 2401 CA ALA A 271 5.917 12.007 4.565 1.00 41.79 A C ANISOU 2401 CA ALA A 271 5302 4866 5710 -65 -317 692 A C ATOM 2402 C ALA A 271 5.879 10.521 4.878 1.00 41.41 A C ANISOU 2402 C ALA A 271 5253 4914 5568 -155 -357 559 A C ATOM 2403 O ALA A 271 6.782 9.775 4.486 1.00 39.86 A O ANISOU 2403 O ALA A 271 5079 4732 5335 -223 -351 525 A O ATOM 2404 CB ALA A 271 6.810 12.722 5.578 1.00 41.38 A C ANISOU 2404 CB ALA A 271 5308 4605 5811 -95 -273 625 A C ATOM 2405 N VAL A 272 4.857 10.068 5.604 1.00 42.60 A N ANISOU 2405 N VAL A 272 5378 5115 5691 -154 -377 485 A N ATOM 2406 CA VAL A 272 4.751 8.645 5.887 1.00 39.31 A C ANISOU 2406 CA VAL A 272 4969 4756 5210 -241 -375 375 A C ATOM 2407 C VAL A 272 4.492 7.864 4.603 1.00 41.26 A C ANISOU 2407 C VAL A 272 5168 5169 5339 -299 -372 361 A C ATOM 2408 O VAL A 272 5.127 6.829 4.362 1.00 39.01 A O ANISOU 2408 O VAL A 272 4918 4872 5034 -379 -335 291 A O ATOM 2409 CB VAL A 272 3.655 8.365 6.931 1.00 41.09 A C ANISOU 2409 CB VAL A 272 5173 5003 5435 -236 -379 307 A C ATOM 2410 CG1 VAL A 272 3.487 6.862 7.097 1.00 41.99 A C ANISOU 2410 CG1 VAL A 272 5301 5152 5501 -332 -338 211 A C ATOM 2411 CG2 VAL A 272 3.979 9.038 8.272 1.00 39.81 A C ANISOU 2411 CG2 VAL A 272 5046 4711 5368 -192 -377 286 A C ATOM 2412 N ASN A 273 3.528 8.320 3.777 1.00 41.05 A N ANISOU 2412 N ASN A 273 5049 5324 5225 -254 -399 419 A N ATOM 2413 CA AASN A 273 3.285 7.580 2.549 0.55 43.10 A C ANISOU 2413 CA AASN A 273 5231 5802 5341 -325 -397 373 A C ATOM 2414 CA BASN A 273 3.260 7.685 2.483 0.46 43.00 A C ANISOU 2414 CA BASN A 273 5214 5801 5325 -314 -400 387 A C ATOM 2415 C ASN A 273 4.513 7.628 1.640 1.00 41.07 A C ANISOU 2415 C ASN A 273 5006 5527 5070 -337 -381 426 A C ATOM 2416 O ASN A 273 4.768 6.654 0.924 1.00 41.11 A O ANISOU 2416 O ASN A 273 4993 5633 4995 -436 -353 324 A O ATOM 2417 CB AASN A 273 2.041 8.106 1.830 0.55 44.94 A C ANISOU 2417 CB AASN A 273 5323 6309 5445 -254 -436 438 A C ATOM 2418 CB BASN A 273 2.245 8.448 1.622 0.46 43.18 A C ANISOU 2418 CB BASN A 273 5102 6079 5226 -217 -440 496 A C ATOM 2419 CG AASN A 273 0.766 7.265 2.112 0.55 45.86 A C ANISOU 2419 CG AASN A 273 5349 6595 5481 -342 -436 283 A C ATOM 2420 CG BASN A 273 1.058 8.882 2.363 0.46 49.50 A C ANISOU 2420 CG BASN A 273 5851 6916 6041 -145 -461 508 A C ATOM 2421 ND2AASN A 273 -0.282 7.563 1.352 0.55 51.13 A N ANISOU 2421 ND2AASN A 273 5855 7580 5993 -294 -474 316 A N ATOM 2422 ND2BASN A 273 -0.121 8.546 1.853 0.46 43.60 A N ANISOU 2422 ND2BASN A 273 4956 6470 5139 -161 -485 458 A N ATOM 2423 OD1AASN A 273 0.723 6.367 2.983 0.55 48.19 A O ANISOU 2423 OD1AASN A 273 5707 6757 5846 -447 -393 146 A O ATOM 2424 OD1BASN A 273 1.181 9.568 3.363 0.46 52.74 A O ANISOU 2424 OD1BASN A 273 6336 7114 6590 -75 -452 552 A O ATOM 2425 N VAL A 274 5.265 8.731 1.649 1.00 40.21 A N ANISOU 2425 N VAL A 274 4942 5290 5044 -250 -382 569 A N ATOM 2426 CA VAL A 274 6.435 8.822 0.789 1.00 38.40 A C ANISOU 2426 CA VAL A 274 4736 5055 4801 -266 -360 628 A C ATOM 2427 C VAL A 274 7.489 7.814 1.227 1.00 40.28 A C ANISOU 2427 C VAL A 274 5050 5166 5089 -359 -328 503 A C ATOM 2428 O VAL A 274 8.078 7.118 0.389 1.00 39.95 A O ANISOU 2428 O VAL A 274 4999 5204 4977 -418 -302 457 A O ATOM 2429 CB VAL A 274 6.992 10.261 0.767 1.00 44.42 A C ANISOU 2429 CB VAL A 274 5530 5679 5668 -170 -337 802 A C ATOM 2430 CG1 VAL A 274 8.282 10.314 -0.055 1.00 43.38 A C ANISOU 2430 CG1 VAL A 274 5419 5535 5527 -205 -304 856 A C ATOM 2431 CG2 VAL A 274 5.968 11.225 0.170 1.00 48.98 A C ANISOU 2431 CG2 VAL A 274 6029 6387 6194 -37 -339 973 A C ATOM 2432 N ALA A 275 7.741 7.712 2.537 1.00 39.11 A N ANISOU 2432 N ALA A 275 4967 4843 5050 -359 -322 452 A N ATOM 2433 CA ALA A 275 8.717 6.743 3.032 1.00 38.95 A C ANISOU 2433 CA ALA A 275 5004 4730 5065 -407 -282 370 A C ATOM 2434 C ALA A 275 8.291 5.322 2.699 1.00 39.23 A C ANISOU 2434 C ALA A 275 5037 4828 5039 -482 -231 252 A C ATOM 2435 O ALA A 275 9.117 4.483 2.333 1.00 37.34 A O ANISOU 2435 O ALA A 275 4828 4564 4797 -518 -172 203 A O ATOM 2436 CB ALA A 275 8.906 6.897 4.540 1.00 37.42 A C ANISOU 2436 CB ALA A 275 4850 4406 4961 -374 -286 350 A C ATOM 2437 N ALA A 276 6.999 5.026 2.819 1.00 38.50 A N ANISOU 2437 N ALA A 276 4906 4814 4909 -514 -234 191 A N ATOM 2438 CA ALA A 276 6.530 3.680 2.520 1.00 39.06 A C ANISOU 2438 CA ALA A 276 4970 4928 4943 -621 -153 44 A C ATOM 2439 C ALA A 276 6.660 3.367 1.039 1.00 41.79 A C ANISOU 2439 C ALA A 276 5253 5448 5178 -691 -136 -20 A C ATOM 2440 O ALA A 276 6.999 2.235 0.669 1.00 41.81 A O ANISOU 2440 O ALA A 276 5281 5419 5185 -780 -36 -150 A O ATOM 2441 CB ALA A 276 5.084 3.520 2.996 1.00 39.94 A C ANISOU 2441 CB ALA A 276 5032 5109 5034 -659 -157 -21 A C ATOM 2442 N ARG A 277 6.404 4.355 0.170 1.00 40.03 A N ANISOU 2442 N ARG A 277 4943 5414 4852 -644 -214 75 A N ATOM 2443 CA ARG A 277 6.558 4.142 -1.264 1.00 41.98 A C ANISOU 2443 CA ARG A 277 5107 5886 4957 -696 -204 31 A C ATOM 2444 C ARG A 277 8.022 3.945 -1.637 1.00 41.30 A C ANISOU 2444 C ARG A 277 5087 5695 4910 -693 -163 53 A C ATOM 2445 O ARG A 277 8.346 3.131 -2.510 1.00 43.63 A O ANISOU 2445 O ARG A 277 5355 6088 5134 -778 -101 -73 A O ATOM 2446 CB ARG A 277 5.974 5.330 -2.024 1.00 49.41 A C ANISOU 2446 CB ARG A 277 5934 7066 5772 -602 -288 187 A C ATOM 2447 CG ARG A 277 6.378 5.407 -3.476 1.00 69.42 A C ANISOU 2447 CG ARG A 277 8379 9851 8146 -611 -288 214 A C ATOM 2448 CD ARG A 277 5.318 6.136 -4.263 1.00 97.31 A C ANISOU 2448 CD ARG A 277 11750 13728 11495 -534 -350 321 A C ATOM 2449 NE ARG A 277 5.637 7.557 -4.302 1.00 99.66 A N ANISOU 2449 NE ARG A 277 12071 13957 11840 -360 -379 607 A N ATOM 2450 CZ ARG A 277 4.964 8.498 -3.652 1.00 90.37 A C ANISOU 2450 CZ ARG A 277 10899 12702 10737 -234 -406 754 A C ATOM 2451 NH1 ARG A 277 3.908 8.209 -2.908 1.00 89.28 A N ANISOU 2451 NH1 ARG A 277 10733 12579 10613 -254 -429 653 A N ATOM 2452 NH2 ARG A 277 5.374 9.760 -3.733 1.00 79.81 A N ANISOU 2452 NH2 ARG A 277 9599 11248 9476 -89 -389 1001 A N ATOM 2453 N LEU A 278 8.917 4.693 -1.002 1.00 40.31 A N ANISOU 2453 N LEU A 278 5035 5389 4891 -603 -189 193 A N ATOM 2454 CA LEU A 278 10.331 4.528 -1.312 1.00 38.23 A C ANISOU 2454 CA LEU A 278 4815 5051 4658 -599 -151 213 A C ATOM 2455 C LEU A 278 10.837 3.159 -0.872 1.00 39.93 A C ANISOU 2455 C LEU A 278 5100 5131 4941 -646 -52 76 A C ATOM 2456 O LEU A 278 11.625 2.527 -1.592 1.00 41.02 A O ANISOU 2456 O LEU A 278 5240 5294 5052 -678 13 13 A O ATOM 2457 CB LEU A 278 11.151 5.643 -0.672 1.00 40.57 A C ANISOU 2457 CB LEU A 278 5153 5210 5054 -518 -189 363 A C ATOM 2458 CG LEU A 278 10.905 7.055 -1.225 1.00 44.87 A C ANISOU 2458 CG LEU A 278 5650 5829 5571 -459 -235 528 A C ATOM 2459 CD1 LEU A 278 11.653 8.123 -0.392 1.00 46.80 A C ANISOU 2459 CD1 LEU A 278 5943 5883 5956 -415 -238 622 A C ATOM 2460 CD2 LEU A 278 11.262 7.142 -2.696 1.00 58.29 A C ANISOU 2460 CD2 LEU A 278 7285 7723 7141 -469 -221 584 A C ATOM 2461 N GLU A 279 10.412 2.689 0.310 1.00 37.81 A N ANISOU 2461 N GLU A 279 4887 4715 4764 -636 -24 42 A N ATOM 2462 CA GLU A 279 10.822 1.360 0.763 1.00 40.11 A C ANISOU 2462 CA GLU A 279 5250 4856 5134 -652 104 -50 A C ATOM 2463 C GLU A 279 10.388 0.300 -0.242 1.00 39.05 A C ANISOU 2463 C GLU A 279 5093 4794 4952 -777 211 -235 A C ATOM 2464 O GLU A 279 11.150 -0.619 -0.574 1.00 41.55 A O ANISOU 2464 O GLU A 279 5451 5027 5308 -792 332 -311 A O ATOM 2465 CB GLU A 279 10.232 1.080 2.151 1.00 38.47 A C ANISOU 2465 CB GLU A 279 5093 4513 5013 -618 127 -32 A C ATOM 2466 CG GLU A 279 10.762 -0.176 2.849 1.00 35.81 A C ANISOU 2466 CG GLU A 279 4840 3992 4774 -581 277 -51 A C ATOM 2467 CD GLU A 279 10.231 -1.478 2.277 1.00 46.43 A C ANISOU 2467 CD GLU A 279 6213 5277 6153 -697 443 -220 A C ATOM 2468 OE1 GLU A 279 9.070 -1.521 1.810 1.00 40.47 A O ANISOU 2468 OE1 GLU A 279 5404 4625 5347 -824 437 -345 A O ATOM 2469 OE2 GLU A 279 10.977 -2.485 2.299 1.00 40.97 A O ANISOU 2469 OE2 GLU A 279 5588 4436 5543 -663 598 -239 A O ATOM 2470 N ALA A 280 9.171 0.433 -0.768 1.00 40.08 A N ANISOU 2470 N ALA A 280 5139 5101 4988 -869 176 -324 A N ATOM 2471 CA ALA A 280 8.667 -0.538 -1.729 1.00 43.10 A C ANISOU 2471 CA ALA A 280 5468 5603 5305 -1023 280 -550 A C ATOM 2472 C ALA A 280 9.472 -0.524 -3.023 1.00 42.13 A C ANISOU 2472 C ALA A 280 5292 5638 5077 -1044 286 -591 A C ATOM 2473 O ALA A 280 9.606 -1.564 -3.681 1.00 45.72 A O ANISOU 2473 O ALA A 280 5742 6103 5527 -1156 422 -797 A O ATOM 2474 CB ALA A 280 7.185 -0.258 -2.002 1.00 46.80 A C ANISOU 2474 CB ALA A 280 5816 6308 5657 -1109 218 -631 A C ATOM 2475 N LEU A 281 10.017 0.634 -3.399 1.00 42.81 A N ANISOU 2475 N LEU A 281 5340 5838 5087 -944 161 -406 A N ATOM 2476 CA LEU A 281 10.835 0.732 -4.599 1.00 45.21 A C ANISOU 2476 CA LEU A 281 5591 6305 5283 -953 166 -413 A C ATOM 2477 C LEU A 281 12.090 -0.136 -4.536 1.00 47.41 A C ANISOU 2477 C LEU A 281 5959 6389 5667 -940 289 -472 A C ATOM 2478 O LEU A 281 12.631 -0.502 -5.589 1.00 48.82 A O ANISOU 2478 O LEU A 281 6091 6697 5761 -988 345 -570 A O ATOM 2479 CB LEU A 281 11.249 2.185 -4.827 1.00 52.36 A C ANISOU 2479 CB LEU A 281 6461 7303 6131 -838 39 -165 A C ATOM 2480 CG LEU A 281 10.346 3.090 -5.657 1.00 71.31 A C ANISOU 2480 CG LEU A 281 8728 10013 8353 -821 -53 -77 A C ATOM 2481 CD1 LEU A 281 10.983 4.478 -5.690 1.00 66.58 A C ANISOU 2481 CD1 LEU A 281 8141 9383 7773 -693 -122 194 A C ATOM 2482 CD2 LEU A 281 10.139 2.545 -7.064 1.00 62.88 A C ANISOU 2482 CD2 LEU A 281 7530 9281 7080 -918 -18 -232 A C ATOM 2483 N THR A 282 12.566 -0.471 -3.332 1.00 42.34 A N ANISOU 2483 N THR A 282 5429 5468 5192 -861 337 -408 A N ATOM 2484 CA THR A 282 13.779 -1.266 -3.225 1.00 40.79 A C ANISOU 2484 CA THR A 282 5303 5107 5089 -807 459 -426 A C ATOM 2485 C THR A 282 13.614 -2.657 -3.811 1.00 43.75 A C ANISOU 2485 C THR A 282 5698 5429 5496 -916 651 -670 A C ATOM 2486 O THR A 282 14.619 -3.315 -4.088 1.00 52.67 A O ANISOU 2486 O THR A 282 6866 6469 6679 -874 769 -710 A O ATOM 2487 CB THR A 282 14.230 -1.417 -1.762 1.00 40.16 A C ANISOU 2487 CB THR A 282 5316 4789 5155 -679 482 -295 A C ATOM 2488 CG2 THR A 282 14.517 -0.064 -1.142 1.00 41.78 A C ANISOU 2488 CG2 THR A 282 5495 5040 5341 -594 317 -102 A C ATOM 2489 OG1 THR A 282 13.213 -2.073 -1.001 1.00 40.20 A O ANISOU 2489 OG1 THR A 282 5371 4661 5242 -719 557 -362 A O ATOM 2490 N ARG A 283 12.375 -3.147 -3.943 1.00 44.00 A N ANISOU 2490 N ARG A 283 5702 5502 5514 -1057 704 -848 A N ATOM 2491 CA ARG A 283 12.167 -4.448 -4.560 1.00 43.39 A C ANISOU 2491 CA ARG A 283 5634 5372 5479 -1201 913 -1130 A C ATOM 2492 C ARG A 283 12.542 -4.446 -6.039 1.00 58.42 A C ANISOU 2492 C ARG A 283 7431 7545 7219 -1286 916 -1279 A C ATOM 2493 O ARG A 283 12.804 -5.513 -6.602 1.00 57.89 A O ANISOU 2493 O ARG A 283 7381 7410 7204 -1379 1111 -1513 A O ATOM 2494 CB ARG A 283 10.717 -4.898 -4.417 1.00 48.46 A C ANISOU 2494 CB ARG A 283 6242 6044 6127 -1370 970 -1317 A C ATOM 2495 CG ARG A 283 10.184 -4.947 -2.985 1.00 51.74 A C ANISOU 2495 CG ARG A 283 6750 6223 6688 -1306 980 -1187 A C ATOM 2496 CD ARG A 283 10.980 -5.913 -2.141 1.00 50.38 A C ANISOU 2496 CD ARG A 283 6733 5677 6733 -1199 1179 -1124 A C ATOM 2497 NE ARG A 283 10.380 -6.119 -0.823 1.00 44.95 A N ANISOU 2497 NE ARG A 283 6123 4787 6169 -1152 1223 -1018 A N ATOM 2498 CZ ARG A 283 10.532 -5.308 0.215 1.00 40.92 A C ANISOU 2498 CZ ARG A 283 5631 4264 5653 -993 1072 -766 A C ATOM 2499 NH1 ARG A 283 11.262 -4.209 0.136 1.00 44.70 A N ANISOU 2499 NH1 ARG A 283 6064 4889 6030 -875 877 -601 A N ATOM 2500 NH2 ARG A 283 9.927 -5.603 1.359 1.00 40.34 A N ANISOU 2500 NH2 ARG A 283 5617 4031 5678 -964 1133 -693 A N ATOM 2501 N GLN A 284 12.566 -3.279 -6.679 1.00 52.04 A N ANISOU 2501 N GLN A 284 6512 7038 6221 -1252 724 -1148 A N ATOM 2502 CA GLN A 284 12.894 -3.195 -8.099 1.00 56.96 A C ANISOU 2502 CA GLN A 284 7015 7972 6654 -1318 717 -1258 A C ATOM 2503 C GLN A 284 14.309 -2.704 -8.364 1.00 59.99 A C ANISOU 2503 C GLN A 284 7421 8343 7029 -1184 679 -1078 A C ATOM 2504 O GLN A 284 14.722 -2.661 -9.525 1.00 57.23 A O ANISOU 2504 O GLN A 284 6978 8243 6525 -1225 687 -1153 A O ATOM 2505 CB GLN A 284 11.905 -2.280 -8.836 1.00 55.67 A C ANISOU 2505 CB GLN A 284 6684 8220 6249 -1367 557 -1228 A C ATOM 2506 CG GLN A 284 10.462 -2.334 -8.367 1.00 79.55 A C ANISOU 2506 CG GLN A 284 9663 11300 9263 -1453 529 -1310 A C ATOM 2507 CD GLN A 284 9.667 -1.126 -8.834 1.00111.46 A C ANISOU 2507 CD GLN A 284 13552 15714 13085 -1403 342 -1149 A C ATOM 2508 NE2 GLN A 284 8.526 -0.883 -8.199 1.00104.86 A N ANISOU 2508 NE2 GLN A 284 12687 14896 12258 -1415 284 -1129 A N ATOM 2509 OE1 GLN A 284 10.076 -0.421 -9.759 1.00109.84 A O ANISOU 2509 OE1 GLN A 284 13251 15779 12704 -1341 265 -1027 A O ATOM 2510 N LEU A 285 15.061 -2.350 -7.330 1.00 54.36 A N ANISOU 2510 N LEU A 285 6812 7380 6462 -1034 644 -858 A N ATOM 2511 CA LEU A 285 16.410 -1.820 -7.454 1.00 54.26 A C ANISOU 2511 CA LEU A 285 6805 7364 6447 -916 606 -688 A C ATOM 2512 C LEU A 285 17.401 -2.799 -6.843 1.00 60.22 A C ANISOU 2512 C LEU A 285 7662 7843 7374 -829 760 -716 A C ATOM 2513 O LEU A 285 17.033 -3.683 -6.070 1.00 59.29 A O ANISOU 2513 O LEU A 285 7634 7490 7404 -824 880 -789 A O ATOM 2514 CB LEU A 285 16.510 -0.465 -6.748 1.00 56.89 A C ANISOU 2514 CB LEU A 285 7142 7685 6790 -817 437 -414 A C ATOM 2515 CG LEU A 285 15.577 0.614 -7.298 1.00 60.33 A C ANISOU 2515 CG LEU A 285 7483 8366 7075 -853 303 -325 A C ATOM 2516 CD1 LEU A 285 15.622 1.855 -6.426 1.00 67.84 A C ANISOU 2516 CD1 LEU A 285 8465 9217 8096 -758 185 -84 A C ATOM 2517 CD2 LEU A 285 15.959 0.966 -8.727 1.00 67.17 A C ANISOU 2517 CD2 LEU A 285 8238 9533 7751 -882 291 -319 A C ATOM 2518 N SER A 286 18.677 -2.633 -7.184 1.00 59.37 A N ANISOU 2518 N SER A 286 7535 7774 7248 -747 768 -637 A N ATOM 2519 CA SER A 286 19.698 -3.405 -6.485 1.00 63.80 A C ANISOU 2519 CA SER A 286 8174 8107 7961 -613 896 -602 A C ATOM 2520 C SER A 286 19.905 -2.901 -5.060 1.00 63.74 A C ANISOU 2520 C SER A 286 8212 7959 8047 -482 811 -386 A C ATOM 2521 O SER A 286 20.333 -3.675 -4.196 1.00 59.74 A O ANISOU 2521 O SER A 286 7774 7255 7670 -360 925 -346 A O ATOM 2522 CB SER A 286 21.017 -3.370 -7.262 1.00 70.75 A C ANISOU 2522 CB SER A 286 8997 9108 8778 -559 929 -587 A C ATOM 2523 OG SER A 286 21.425 -2.040 -7.523 1.00 75.38 A O ANISOU 2523 OG SER A 286 9502 9890 9250 -556 757 -415 A O ATOM 2524 N GLN A 287 19.581 -1.637 -4.793 1.00 54.20 A N ANISOU 2524 N GLN A 287 6961 6856 6776 -501 629 -247 A N ATOM 2525 CA GLN A 287 19.832 -1.032 -3.495 1.00 46.35 A C ANISOU 2525 CA GLN A 287 5986 5775 5850 -400 543 -76 A C ATOM 2526 C GLN A 287 18.722 -1.368 -2.504 1.00 42.86 A C ANISOU 2526 C GLN A 287 5614 5182 5490 -402 553 -88 A C ATOM 2527 O GLN A 287 17.541 -1.358 -2.851 1.00 48.11 A O ANISOU 2527 O GLN A 287 6280 5876 6122 -513 535 -179 A O ATOM 2528 CB GLN A 287 19.947 0.486 -3.643 1.00 49.18 A C ANISOU 2528 CB GLN A 287 6277 6276 6134 -434 380 53 A C ATOM 2529 CG GLN A 287 21.236 0.927 -4.344 1.00 50.19 A C ANISOU 2529 CG GLN A 287 6333 6535 6203 -420 376 106 A C ATOM 2530 CD GLN A 287 21.124 0.941 -5.858 1.00 60.59 A C ANISOU 2530 CD GLN A 287 7600 8027 7395 -509 397 35 A C ATOM 2531 NE2 GLN A 287 22.240 1.215 -6.522 1.00 74.15 A N ANISOU 2531 NE2 GLN A 287 9255 9864 9056 -499 413 75 A N ATOM 2532 OE1 GLN A 287 20.061 0.707 -6.426 1.00 53.51 A O ANISOU 2532 OE1 GLN A 287 6703 7191 6436 -588 401 -61 A O ATOM 2533 N ALA A 288 19.116 -1.642 -1.261 1.00 41.50 A N ANISOU 2533 N ALA A 288 5479 4884 5405 -273 581 13 A N ATOM 2534 CA ALA A 288 18.177 -1.968 -0.194 1.00 42.85 A C ANISOU 2534 CA ALA A 288 5712 4917 5651 -254 602 31 A C ATOM 2535 C ALA A 288 17.760 -0.755 0.619 1.00 37.26 A C ANISOU 2535 C ALA A 288 4970 4273 4914 -257 432 134 A C ATOM 2536 O ALA A 288 16.888 -0.891 1.484 1.00 41.43 A O ANISOU 2536 O ALA A 288 5538 4718 5486 -251 431 147 A O ATOM 2537 CB ALA A 288 18.784 -3.001 0.756 1.00 46.17 A C ANISOU 2537 CB ALA A 288 6186 5186 6170 -86 750 108 A C ATOM 2538 N LEU A 289 18.402 0.398 0.391 1.00 38.42 A N ANISOU 2538 N LEU A 289 5045 4551 5000 -267 311 201 A N ATOM 2539 CA LEU A 289 18.123 1.662 1.070 1.00 37.15 A C ANISOU 2539 CA LEU A 289 4850 4432 4833 -283 176 276 A C ATOM 2540 C LEU A 289 17.919 2.745 0.022 1.00 43.98 A C ANISOU 2540 C LEU A 289 5674 5397 5641 -380 97 287 A C ATOM 2541 O LEU A 289 18.775 2.939 -0.846 1.00 40.45 A O ANISOU 2541 O LEU A 289 5185 5035 5149 -397 110 299 A O ATOM 2542 CB LEU A 289 19.289 2.043 2.001 1.00 38.82 A C ANISOU 2542 CB LEU A 289 5004 4696 5050 -193 146 353 A C ATOM 2543 CG LEU A 289 19.349 3.468 2.532 1.00 37.48 A C ANISOU 2543 CG LEU A 289 4778 4582 4881 -241 33 387 A C ATOM 2544 CD1 LEU A 289 18.185 3.686 3.526 1.00 41.15 A C ANISOU 2544 CD1 LEU A 289 5279 4978 5379 -239 -11 383 A C ATOM 2545 CD2 LEU A 289 20.693 3.695 3.216 1.00 44.66 A C ANISOU 2545 CD2 LEU A 289 5595 5606 5769 -181 24 412 A C ATOM 2546 N AVAL A 290 16.801 3.459 0.084 0.47 36.76 A N ANISOU 2546 N AVAL A 290 4764 4481 4723 -428 28 301 A N ATOM 2547 N BVAL A 290 16.785 3.438 0.111 0.53 36.71 A N ANISOU 2547 N BVAL A 290 4759 4471 4717 -427 29 300 A N ATOM 2548 CA AVAL A 290 16.601 4.604 -0.800 0.47 38.30 A C ANISOU 2548 CA AVAL A 290 4917 4765 4869 -479 -31 367 A C ATOM 2549 CA BVAL A 290 16.449 4.562 -0.754 0.53 38.26 A C ANISOU 2549 CA BVAL A 290 4915 4755 4865 -480 -32 361 A C ATOM 2550 C AVAL A 290 15.888 5.706 -0.036 0.47 39.95 A C ANISOU 2550 C AVAL A 290 5130 4916 5135 -472 -101 431 A C ATOM 2551 C BVAL A 290 16.003 5.717 0.129 0.53 39.83 A C ANISOU 2551 C BVAL A 290 5116 4888 5130 -467 -101 430 A C ATOM 2552 O AVAL A 290 15.002 5.442 0.784 0.47 40.35 A O ANISOU 2552 O AVAL A 290 5209 4907 5215 -456 -117 395 A O ATOM 2553 O BVAL A 290 15.426 5.510 1.202 0.53 38.66 A O ANISOU 2553 O BVAL A 290 4996 4666 5028 -440 -116 400 A O ATOM 2554 CB AVAL A 290 15.819 4.225 -2.074 0.47 41.93 A C ANISOU 2554 CB AVAL A 290 5354 5352 5225 -534 -13 315 A C ATOM 2555 CB BVAL A 290 15.342 4.177 -1.761 0.53 42.88 A C ANISOU 2555 CB BVAL A 290 5486 5446 5360 -534 -24 302 A C ATOM 2556 CG1AVAL A 290 16.616 3.224 -2.897 0.47 44.40 A C ANISOU 2556 CG1AVAL A 290 5658 5723 5490 -553 73 226 A C ATOM 2557 CG1BVAL A 290 14.763 5.408 -2.420 0.53 44.82 A C ANISOU 2557 CG1BVAL A 290 5682 5797 5549 -540 -88 416 A C ATOM 2558 CG2AVAL A 290 14.449 3.679 -1.716 0.47 38.22 A C ANISOU 2558 CG2AVAL A 290 4905 4864 4755 -560 -13 232 A C ATOM 2559 CG2BVAL A 290 15.883 3.205 -2.798 0.53 45.63 A C ANISOU 2559 CG2BVAL A 290 5818 5881 5639 -570 57 205 A C ATOM 2560 N PHE A 291 16.267 6.944 -0.315 1.00 37.80 A N ANISOU 2560 N PHE A 291 4829 4648 4885 -486 -122 524 A N ATOM 2561 CA PHE A 291 15.731 8.092 0.400 1.00 36.01 A C ANISOU 2561 CA PHE A 291 4610 4330 4741 -479 -156 575 A C ATOM 2562 C PHE A 291 15.587 9.278 -0.537 1.00 42.55 A C ANISOU 2562 C PHE A 291 5419 5173 5574 -485 -140 708 A C ATOM 2563 O PHE A 291 16.194 9.339 -1.610 1.00 41.08 A O ANISOU 2563 O PHE A 291 5205 5076 5328 -502 -108 770 A O ATOM 2564 CB PHE A 291 16.576 8.447 1.649 1.00 38.69 A C ANISOU 2564 CB PHE A 291 4939 4595 5168 -486 -157 526 A C ATOM 2565 CG PHE A 291 18.079 8.481 1.421 1.00 36.83 A C ANISOU 2565 CG PHE A 291 4656 4410 4928 -518 -124 518 A C ATOM 2566 CD1 PHE A 291 18.689 9.625 0.949 1.00 36.67 A C ANISOU 2566 CD1 PHE A 291 4607 4364 4961 -581 -88 575 A C ATOM 2567 CD2 PHE A 291 18.869 7.376 1.716 1.00 38.82 A C ANISOU 2567 CD2 PHE A 291 4887 4732 5130 -478 -109 463 A C ATOM 2568 CE1 PHE A 291 20.072 9.671 0.752 1.00 43.07 A C ANISOU 2568 CE1 PHE A 291 5357 5242 5764 -627 -52 555 A C ATOM 2569 CE2 PHE A 291 20.247 7.405 1.506 1.00 42.89 A C ANISOU 2569 CE2 PHE A 291 5338 5330 5629 -495 -80 457 A C ATOM 2570 CZ PHE A 291 20.843 8.557 1.041 1.00 42.58 A C ANISOU 2570 CZ PHE A 291 5258 5287 5632 -582 -59 491 A C ATOM 2571 N SER A 292 14.745 10.219 -0.116 1.00 41.70 A N ANISOU 2571 N SER A 292 5326 4979 5539 -455 -148 767 A N ATOM 2572 CA SER A 292 14.420 11.381 -0.919 1.00 41.46 A C ANISOU 2572 CA SER A 292 5286 4936 5530 -420 -106 934 A C ATOM 2573 C SER A 292 15.531 12.425 -0.869 1.00 45.06 A C ANISOU 2573 C SER A 292 5749 5258 6113 -472 -25 985 A C ATOM 2574 O SER A 292 16.384 12.425 0.019 1.00 42.03 A O ANISOU 2574 O SER A 292 5364 4798 5806 -542 -18 864 A O ATOM 2575 CB SER A 292 13.134 12.013 -0.418 1.00 47.00 A C ANISOU 2575 CB SER A 292 6003 5571 6286 -349 -119 981 A C ATOM 2576 OG SER A 292 13.359 12.516 0.884 1.00 46.75 A O ANISOU 2576 OG SER A 292 6003 5358 6401 -380 -105 889 A O ATOM 2577 N SER A 293 15.472 13.358 -1.815 1.00 44.66 A N ANISOU 2577 N SER A 293 5694 5194 6081 -438 49 1172 A N ATOM 2578 CA SER A 293 16.475 14.416 -1.868 1.00 43.46 A C ANISOU 2578 CA SER A 293 5553 4888 6072 -506 163 1230 A C ATOM 2579 C SER A 293 16.429 15.309 -0.634 1.00 47.82 A C ANISOU 2579 C SER A 293 6141 5204 6825 -552 218 1138 A C ATOM 2580 O SER A 293 17.450 15.898 -0.261 1.00 48.70 A O ANISOU 2580 O SER A 293 6244 5201 7060 -667 300 1061 A O ATOM 2581 CB SER A 293 16.271 15.251 -3.131 1.00 53.34 A C ANISOU 2581 CB SER A 293 6799 6158 7309 -432 259 1491 A C ATOM 2582 OG SER A 293 14.961 15.782 -3.149 1.00 58.12 A O ANISOU 2582 OG SER A 293 7421 6731 7930 -301 268 1624 A O ATOM 2583 N GLU A 294 15.258 15.447 -0.001 1.00 47.60 A N ANISOU 2583 N GLU A 294 6140 5117 6829 -474 183 1124 A N ATOM 2584 CA GLU A 294 15.192 16.251 1.218 1.00 49.17 A C ANISOU 2584 CA GLU A 294 6365 5107 7209 -524 239 1001 A C ATOM 2585 C GLU A 294 16.011 15.629 2.343 1.00 47.40 A C ANISOU 2585 C GLU A 294 6101 4940 6969 -635 174 755 A C ATOM 2586 O GLU A 294 16.605 16.351 3.150 1.00 47.40 A O ANISOU 2586 O GLU A 294 6085 4822 7103 -742 247 617 A O ATOM 2587 CB GLU A 294 13.741 16.447 1.657 1.00 53.27 A C ANISOU 2587 CB GLU A 294 6911 5583 7747 -404 211 1035 A C ATOM 2588 CG GLU A 294 12.932 17.349 0.713 1.00 62.81 A C ANISOU 2588 CG GLU A 294 8142 6724 8998 -265 307 1298 A C ATOM 2589 CD GLU A 294 12.478 16.658 -0.566 1.00 84.22 A C ANISOU 2589 CD GLU A 294 10807 9702 11492 -165 235 1469 A C ATOM 2590 OE1 GLU A 294 12.549 15.413 -0.648 1.00 64.78 A O ANISOU 2590 OE1 GLU A 294 8307 7446 8861 -206 110 1355 A O ATOM 2591 OE2 GLU A 294 12.056 17.373 -1.500 1.00105.48 A O ANISOU 2591 OE2 GLU A 294 13492 12404 14180 -42 319 1719 A O ATOM 2592 N VAL A 295 16.074 14.299 2.398 1.00 43.91 A N ANISOU 2592 N VAL A 295 5632 4690 6362 -611 57 697 A N ATOM 2593 CA VAL A 295 16.947 13.637 3.365 1.00 40.38 A C ANISOU 2593 CA VAL A 295 5132 4336 5873 -676 7 517 A C ATOM 2594 C VAL A 295 18.408 13.856 2.995 1.00 44.55 A C ANISOU 2594 C VAL A 295 5605 4905 6417 -778 64 489 A C ATOM 2595 O VAL A 295 19.241 14.192 3.847 1.00 45.27 A O ANISOU 2595 O VAL A 295 5630 5013 6557 -876 88 336 A O ATOM 2596 CB VAL A 295 16.604 12.140 3.446 1.00 41.18 A C ANISOU 2596 CB VAL A 295 5234 4593 5820 -600 -92 499 A C ATOM 2597 CG1 VAL A 295 17.596 11.407 4.317 1.00 40.77 A C ANISOU 2597 CG1 VAL A 295 5120 4659 5711 -622 -123 374 A C ATOM 2598 CG2 VAL A 295 15.169 11.950 3.965 1.00 43.47 A C ANISOU 2598 CG2 VAL A 295 5563 4853 6102 -525 -139 499 A C ATOM 2599 N LYS A 296 18.741 13.669 1.719 1.00 42.60 A N ANISOU 2599 N LYS A 296 5365 4709 6112 -764 88 624 A N ATOM 2600 CA LYS A 296 20.111 13.892 1.265 1.00 42.32 A C ANISOU 2600 CA LYS A 296 5271 4721 6087 -862 151 611 A C ATOM 2601 C LYS A 296 20.568 15.313 1.570 1.00 47.21 A C ANISOU 2601 C LYS A 296 5880 5164 6893 -991 282 568 A C ATOM 2602 O LYS A 296 21.703 15.533 2.021 1.00 47.89 A O ANISOU 2602 O LYS A 296 5881 5302 7011 -1119 321 426 A O ATOM 2603 CB LYS A 296 20.196 13.590 -0.234 1.00 48.69 A C ANISOU 2603 CB LYS A 296 6092 5608 6800 -817 169 781 A C ATOM 2604 CG LYS A 296 21.600 13.679 -0.834 1.00 48.78 A C ANISOU 2604 CG LYS A 296 6038 5699 6797 -908 232 782 A C ATOM 2605 CD LYS A 296 21.709 14.810 -1.821 1.00 51.10 A C ANISOU 2605 CD LYS A 296 6354 5881 7179 -948 363 957 A C ATOM 2606 CE LYS A 296 23.095 14.873 -2.446 1.00 57.19 A C ANISOU 2606 CE LYS A 296 7054 6746 7930 -1049 433 958 A C ATOM 2607 NZ LYS A 296 23.570 16.281 -2.518 1.00 66.58 A N ANISOU 2607 NZ LYS A 296 8247 7740 9312 -1177 605 1005 A N ATOM 2608 N ASN A 297 19.703 16.296 1.343 1.00 49.32 A N ANISOU 2608 N ASN A 297 6222 5224 7292 -961 368 681 A N ATOM 2609 CA ASN A 297 20.124 17.681 1.488 1.00 50.33 A C ANISOU 2609 CA ASN A 297 6359 5126 7637 -1087 544 654 A C ATOM 2610 C ASN A 297 20.214 18.116 2.942 1.00 51.80 A C ANISOU 2610 C ASN A 297 6506 5245 7931 -1196 562 392 A C ATOM 2611 O ASN A 297 20.902 19.099 3.234 1.00 51.86 A O ANISOU 2611 O ASN A 297 6484 5112 8107 -1362 712 269 A O ATOM 2612 CB ASN A 297 19.171 18.595 0.715 1.00 54.96 A C ANISOU 2612 CB ASN A 297 7042 5501 8341 -983 663 899 A C ATOM 2613 CG ASN A 297 19.361 18.477 -0.783 1.00 58.45 A C ANISOU 2613 CG ASN A 297 7491 6030 8688 -914 695 1156 A C ATOM 2614 ND2 ASN A 297 18.291 18.693 -1.539 1.00 64.86 A N ANISOU 2614 ND2 ASN A 297 8352 6825 9465 -745 711 1399 A N ATOM 2615 OD1 ASN A 297 20.469 18.216 -1.256 1.00 65.84 A O ANISOU 2615 OD1 ASN A 297 8372 7076 9568 -1007 710 1135 A O ATOM 2616 N SER A 298 19.564 17.394 3.852 1.00 50.75 A N ANISOU 2616 N SER A 298 6362 5223 7698 -1118 424 290 A N ATOM 2617 CA SER A 298 19.615 17.686 5.278 1.00 54.86 A C ANISOU 2617 CA SER A 298 6823 5751 8270 -1207 422 34 A C ATOM 2618 C SER A 298 20.773 17.002 6.000 1.00 52.72 A C ANISOU 2618 C SER A 298 6410 5761 7861 -1293 342 -162 A C ATOM 2619 O SER A 298 21.030 17.324 7.164 1.00 57.25 A O ANISOU 2619 O SER A 298 6893 6404 8453 -1393 351 -397 A O ATOM 2620 CB SER A 298 18.298 17.266 5.945 1.00 58.37 A C ANISOU 2620 CB SER A 298 7315 6199 8663 -1068 322 39 A C ATOM 2621 OG SER A 298 17.195 17.939 5.367 1.00 64.03 A O ANISOU 2621 OG SER A 298 8139 6695 9496 -970 396 214 A O ATOM 2622 N ALA A 299 21.464 16.064 5.359 1.00 48.74 A N ANISOU 2622 N ALA A 299 5868 5445 7208 -1247 270 -73 A N ATOM 2623 CA ALA A 299 22.623 15.441 5.987 1.00 53.26 A C ANISOU 2623 CA ALA A 299 6289 6304 7645 -1298 210 -226 A C ATOM 2624 C ALA A 299 23.796 16.415 6.029 1.00 52.14 A C ANISOU 2624 C ALA A 299 6039 6168 7604 -1517 335 -387 A C ATOM 2625 O ALA A 299 23.936 17.291 5.170 1.00 55.31 A O ANISOU 2625 O ALA A 299 6500 6352 8162 -1610 474 -309 A O ATOM 2626 CB ALA A 299 23.020 14.173 5.232 1.00 51.74 A C ANISOU 2626 CB ALA A 299 6093 6281 7286 -1172 126 -81 A C ATOM 2627 N THR A 300 24.656 16.261 7.044 1.00 52.60 A N ANISOU 2627 N THR A 300 5920 6499 7565 -1602 299 -612 A N ATOM 2628 CA THR A 300 25.819 17.126 7.176 1.00 56.36 A C ANISOU 2628 CA THR A 300 6256 7041 8117 -1841 419 -817 A C ATOM 2629 C THR A 300 27.145 16.424 6.904 1.00 59.99 A C ANISOU 2629 C THR A 300 6558 7830 8408 -1849 370 -827 A C ATOM 2630 O THR A 300 28.144 17.105 6.657 1.00 63.53 A O ANISOU 2630 O THR A 300 6899 8315 8923 -2051 482 -950 A O ATOM 2631 CB THR A 300 25.879 17.759 8.579 1.00 63.20 A C ANISOU 2631 CB THR A 300 6993 8014 9007 -1990 446 -1138 A C ATOM 2632 CG2 THR A 300 24.558 18.418 8.925 1.00 63.67 A C ANISOU 2632 CG2 THR A 300 7201 7758 9231 -1965 499 -1142 A C ATOM 2633 OG1 THR A 300 26.150 16.760 9.564 1.00 60.37 A O ANISOU 2633 OG1 THR A 300 6483 8061 8396 -1876 288 -1215 A O ATOM 2634 N LYS A 301 27.183 15.094 6.937 1.00 52.79 A N ANISOU 2634 N LYS A 301 5625 7143 7291 -1635 227 -701 A N ATOM 2635 CA LYS A 301 28.403 14.347 6.665 1.00 56.77 A C ANISOU 2635 CA LYS A 301 5981 7957 7633 -1597 189 -685 A C ATOM 2636 C LYS A 301 28.530 14.052 5.176 1.00 53.34 A C ANISOU 2636 C LYS A 301 5660 7378 7228 -1543 225 -463 A C ATOM 2637 O LYS A 301 27.549 14.064 4.435 1.00 51.81 A O ANISOU 2637 O LYS A 301 5655 6915 7117 -1468 236 -290 A O ATOM 2638 CB LYS A 301 28.431 13.042 7.467 1.00 55.75 A C ANISOU 2638 CB LYS A 301 5771 8129 7280 -1372 53 -645 A C ATOM 2639 CG LYS A 301 28.324 13.254 8.971 1.00 65.13 A C ANISOU 2639 CG LYS A 301 6821 9536 8390 -1401 8 -848 A C ATOM 2640 CD LYS A 301 27.659 12.091 9.689 1.00 82.53 A C ANISOU 2640 CD LYS A 301 9056 11858 10443 -1143 -101 -723 A C ATOM 2641 CE LYS A 301 28.667 11.308 10.526 1.00 90.20 A C ANISOU 2641 CE LYS A 301 9788 13314 11170 -1020 -162 -758 A C ATOM 2642 NZ LYS A 301 28.017 10.266 11.376 1.00 96.16 A N ANISOU 2642 NZ LYS A 301 10566 14183 11788 -769 -237 -627 A N ATOM 2643 N SER A 302 29.767 13.798 4.742 1.00 50.14 A N ANISOU 2643 N SER A 302 5118 7195 6737 -1581 245 -479 A N ATOM 2644 CA SER A 302 30.058 13.553 3.324 1.00 52.55 A C ANISOU 2644 CA SER A 302 5498 7417 7052 -1549 291 -296 A C ATOM 2645 C SER A 302 29.848 12.074 2.992 1.00 52.07 A C ANISOU 2645 C SER A 302 5490 7456 6837 -1291 192 -138 A C ATOM 2646 O SER A 302 30.777 11.315 2.701 1.00 53.50 A O ANISOU 2646 O SER A 302 5568 7866 6894 -1212 179 -113 A O ATOM 2647 CB SER A 302 31.475 14.000 2.982 1.00 64.91 A C ANISOU 2647 CB SER A 302 6888 9169 8607 -1721 376 -395 A C ATOM 2648 OG SER A 302 31.682 15.353 3.336 1.00 87.29 A O ANISOU 2648 OG SER A 302 9670 11888 11607 -1987 500 -574 A O ATOM 2649 N TRP A 303 28.581 11.684 3.023 1.00 45.48 A N ANISOU 2649 N TRP A 303 4821 6435 6026 -1166 141 -38 A N ATOM 2650 CA TRP A 303 28.187 10.337 2.657 1.00 43.57 A C ANISOU 2650 CA TRP A 303 4659 6216 5680 -953 83 93 A C ATOM 2651 C TRP A 303 28.496 10.053 1.193 1.00 43.75 A C ANISOU 2651 C TRP A 303 4730 6207 5686 -940 133 212 A C ATOM 2652 O TRP A 303 28.568 10.959 0.354 1.00 42.52 A O ANISOU 2652 O TRP A 303 4603 5940 5612 -1071 204 256 A O ATOM 2653 CB TRP A 303 26.690 10.141 2.874 1.00 43.81 A C ANISOU 2653 CB TRP A 303 4851 6038 5757 -871 39 155 A C ATOM 2654 CG TRP A 303 26.252 10.315 4.289 1.00 47.49 A C ANISOU 2654 CG TRP A 303 5281 6538 6226 -862 -10 49 A C ATOM 2655 CD1 TRP A 303 25.643 11.406 4.839 1.00 48.15 A C ANISOU 2655 CD1 TRP A 303 5389 6482 6424 -981 6 -37 A C ATOM 2656 CD2 TRP A 303 26.382 9.353 5.336 1.00 42.46 A C ANISOU 2656 CD2 TRP A 303 4571 6096 5467 -713 -69 28 A C ATOM 2657 CE2 TRP A 303 25.825 9.924 6.504 1.00 43.54 A C ANISOU 2657 CE2 TRP A 303 4682 6234 5628 -759 -101 -80 A C ATOM 2658 CE3 TRP A 303 26.913 8.064 5.402 1.00 42.06 A C ANISOU 2658 CE3 TRP A 303 4475 6214 5292 -530 -78 103 A C ATOM 2659 NE1 TRP A 303 25.381 11.178 6.176 1.00 45.95 A N ANISOU 2659 NE1 TRP A 303 5049 6322 6086 -929 -52 -134 A N ATOM 2660 CZ2 TRP A 303 25.793 9.247 7.721 1.00 45.61 A C ANISOU 2660 CZ2 TRP A 303 4863 6696 5770 -629 -154 -104 A C ATOM 2661 CZ3 TRP A 303 26.883 7.396 6.617 1.00 47.92 A C ANISOU 2661 CZ3 TRP A 303 5147 7126 5934 -386 -116 102 A C ATOM 2662 CH2 TRP A 303 26.332 7.990 7.758 1.00 50.74 A C ANISOU 2662 CH2 TRP A 303 5468 7516 6294 -437 -160 4 A C ATOM 2663 N ASN A 304 28.622 8.764 0.875 1.00 42.81 A N ANISOU 2663 N ASN A 304 4626 6177 5463 -772 112 272 A N ATOM 2664 CA ASN A 304 28.896 8.336 -0.500 1.00 42.89 A C ANISOU 2664 CA ASN A 304 4673 6191 5433 -748 161 357 A C ATOM 2665 C ASN A 304 27.572 8.189 -1.255 1.00 40.75 A C ANISOU 2665 C ASN A 304 4566 5727 5188 -719 154 444 A C ATOM 2666 O ASN A 304 27.125 7.096 -1.602 1.00 42.98 A O ANISOU 2666 O ASN A 304 4916 6000 5416 -602 150 463 A O ATOM 2667 CB ASN A 304 29.689 7.035 -0.510 1.00 46.43 A C ANISOU 2667 CB ASN A 304 5053 6817 5772 -585 172 356 A C ATOM 2668 CG ASN A 304 31.109 7.197 0.025 1.00 50.45 A C ANISOU 2668 CG ASN A 304 5359 7589 6219 -604 182 286 A C ATOM 2669 ND2 ASN A 304 31.607 6.152 0.662 1.00 51.25 A N ANISOU 2669 ND2 ASN A 304 5383 7858 6230 -416 175 292 A N ATOM 2670 OD1 ASN A 304 31.748 8.246 -0.132 1.00 51.16 A O ANISOU 2670 OD1 ASN A 304 5356 7740 6343 -782 210 232 A O ATOM 2671 N PHE A 305 26.948 9.340 -1.518 1.00 41.05 A N ANISOU 2671 N PHE A 305 4661 5622 5316 -831 169 490 A N ATOM 2672 CA PHE A 305 25.643 9.355 -2.160 1.00 41.50 A C ANISOU 2672 CA PHE A 305 4841 5546 5380 -798 155 581 A C ATOM 2673 C PHE A 305 25.739 8.886 -3.604 1.00 43.47 A C ANISOU 2673 C PHE A 305 5102 5882 5531 -773 192 656 A C ATOM 2674 O PHE A 305 26.702 9.208 -4.314 1.00 39.69 A O ANISOU 2674 O PHE A 305 4556 5498 5028 -833 251 690 A O ATOM 2675 CB PHE A 305 25.046 10.765 -2.176 1.00 44.91 A C ANISOU 2675 CB PHE A 305 5318 5815 5932 -893 189 649 A C ATOM 2676 CG PHE A 305 24.744 11.342 -0.821 1.00 45.76 A C ANISOU 2676 CG PHE A 305 5424 5819 6145 -932 166 553 A C ATOM 2677 CD1 PHE A 305 23.757 10.797 -0.011 1.00 45.19 A C ANISOU 2677 CD1 PHE A 305 5407 5702 6061 -843 90 514 A C ATOM 2678 CD2 PHE A 305 25.428 12.463 -0.379 1.00 49.10 A C ANISOU 2678 CD2 PHE A 305 5782 6194 6680 -1076 236 487 A C ATOM 2679 CE1 PHE A 305 23.478 11.359 1.233 1.00 44.95 A C ANISOU 2679 CE1 PHE A 305 5364 5603 6113 -881 73 416 A C ATOM 2680 CE2 PHE A 305 25.151 13.015 0.861 1.00 49.62 A C ANISOU 2680 CE2 PHE A 305 5833 6186 6835 -1129 225 362 A C ATOM 2681 CZ PHE A 305 24.180 12.471 1.654 1.00 45.27 A C ANISOU 2681 CZ PHE A 305 5334 5612 6255 -1024 138 332 A C ATOM 2682 N ILE A 306 24.704 8.185 -4.053 1.00 39.69 A N ANISOU 2682 N ILE A 306 4698 5389 4993 -701 164 671 A N ATOM 2683 CA ILE A 306 24.500 7.884 -5.465 1.00 39.05 A C ANISOU 2683 CA ILE A 306 4621 5417 4801 -694 196 726 A C ATOM 2684 C ILE A 306 23.087 8.312 -5.848 1.00 41.33 A C ANISOU 2684 C ILE A 306 4969 5663 5073 -685 166 809 A C ATOM 2685 O ILE A 306 22.121 8.014 -5.131 1.00 42.42 A O ANISOU 2685 O ILE A 306 5161 5712 5244 -647 115 759 A O ATOM 2686 CB ILE A 306 24.740 6.390 -5.767 1.00 39.26 A C ANISOU 2686 CB ILE A 306 4643 5534 4739 -623 215 612 A C ATOM 2687 CG1 ILE A 306 24.501 6.105 -7.248 1.00 40.94 A C ANISOU 2687 CG1 ILE A 306 4839 5898 4818 -638 251 628 A C ATOM 2688 CG2 ILE A 306 23.881 5.490 -4.860 1.00 43.13 A C ANISOU 2688 CG2 ILE A 306 5204 5915 5268 -554 184 522 A C ATOM 2689 CD1 ILE A 306 25.039 4.787 -7.701 1.00 48.43 A C ANISOU 2689 CD1 ILE A 306 5769 6936 5698 -593 311 496 A C ATOM 2690 N TRP A 307 22.982 9.059 -6.944 1.00 42.50 A N ANISOU 2690 N TRP A 307 5093 5891 5164 -707 205 952 A N ATOM 2691 CA TRP A 307 21.708 9.503 -7.509 1.00 44.08 A C ANISOU 2691 CA TRP A 307 5315 6125 5307 -668 186 1070 A C ATOM 2692 C TRP A 307 21.130 8.392 -8.378 1.00 49.95 A C ANISOU 2692 C TRP A 307 6030 7079 5870 -639 163 983 A C ATOM 2693 O TRP A 307 21.792 7.933 -9.311 1.00 49.79 A O ANISOU 2693 O TRP A 307 5953 7230 5733 -656 203 955 A O ATOM 2694 CB TRP A 307 21.955 10.770 -8.330 1.00 49.79 A C ANISOU 2694 CB TRP A 307 6012 6869 6037 -682 264 1294 A C ATOM 2695 CG TRP A 307 20.735 11.482 -8.827 1.00 57.07 A C ANISOU 2695 CG TRP A 307 6943 7823 6915 -605 266 1478 A C ATOM 2696 CD1 TRP A 307 19.437 11.117 -8.646 1.00 63.64 A C ANISOU 2696 CD1 TRP A 307 7789 8702 7689 -540 191 1444 A C ATOM 2697 CD2 TRP A 307 20.711 12.688 -9.603 1.00 72.27 A C ANISOU 2697 CD2 TRP A 307 8854 9756 8848 -570 363 1747 A C ATOM 2698 CE2 TRP A 307 19.360 12.997 -9.852 1.00 77.93 A C ANISOU 2698 CE2 TRP A 307 9569 10543 9499 -456 334 1879 A C ATOM 2699 CE3 TRP A 307 21.703 13.538 -10.107 1.00 78.34 A C ANISOU 2699 CE3 TRP A 307 9606 10480 9679 -619 487 1899 A C ATOM 2700 NE1 TRP A 307 18.600 12.024 -9.259 1.00 69.03 A N ANISOU 2700 NE1 TRP A 307 8452 9449 8326 -452 221 1675 A N ATOM 2701 CZ2 TRP A 307 18.973 14.122 -10.584 1.00 82.10 A C ANISOU 2701 CZ2 TRP A 307 10082 11097 10016 -359 429 2186 A C ATOM 2702 CZ3 TRP A 307 21.317 14.653 -10.834 1.00 79.90 A C ANISOU 2702 CZ3 TRP A 307 9803 10672 9884 -542 595 2199 A C ATOM 2703 CH2 TRP A 307 19.964 14.933 -11.066 1.00 80.08 A C ANISOU 2703 CH2 TRP A 307 9827 10765 9836 -398 567 2353 A C ATOM 2704 N LEU A 308 19.893 7.967 -8.094 1.00 48.77 A N ANISOU 2704 N LEU A 308 5908 6929 5694 -609 108 919 A N ATOM 2705 CA LEU A 308 19.260 6.863 -8.814 1.00 56.70 A C ANISOU 2705 CA LEU A 308 6874 8127 6540 -617 101 778 A C ATOM 2706 C LEU A 308 18.258 7.375 -9.846 1.00 68.13 A C ANISOU 2706 C LEU A 308 8247 9821 7819 -588 80 899 A C ATOM 2707 O LEU A 308 17.413 8.222 -9.538 1.00 65.02 A O ANISOU 2707 O LEU A 308 7863 9377 7462 -534 46 1041 A O ATOM 2708 CB LEU A 308 18.551 5.912 -7.843 1.00 49.43 A C ANISOU 2708 CB LEU A 308 6014 7075 5691 -621 74 601 A C ATOM 2709 CG LEU A 308 19.403 5.262 -6.754 1.00 50.09 A C ANISOU 2709 CG LEU A 308 6160 6955 5916 -611 101 501 A C ATOM 2710 CD1 LEU A 308 18.515 4.506 -5.786 1.00 62.06 A C ANISOU 2710 CD1 LEU A 308 7738 8339 7502 -600 88 386 A C ATOM 2711 CD2 LEU A 308 20.435 4.340 -7.357 1.00 56.13 A C ANISOU 2711 CD2 LEU A 308 6899 7798 6632 -620 178 395 A C ATOM 2712 N THR A 309 18.333 6.830 -11.059 1.00 86.05 A N ANISOU 2712 N THR A 309 10425 12378 9890 -613 106 837 A N ATOM 2713 CA THR A 309 17.466 7.237 -12.169 1.00101.59 A C ANISOU 2713 CA THR A 309 12279 14682 11638 -574 88 952 A C ATOM 2714 C THR A 309 16.215 6.367 -12.269 1.00101.67 A C ANISOU 2714 C THR A 309 12233 14871 11526 -612 46 748 A C ATOM 2715 O THR A 309 15.875 5.858 -13.339 1.00103.00 A O ANISOU 2715 O THR A 309 12276 15395 11465 -651 54 642 A O ATOM 2716 CB THR A 309 18.252 7.198 -13.475 1.00 78.16 A C ANISOU 2716 CB THR A 309 9215 11995 8488 -587 143 994 A C ATOM 2717 N ASP A 310 15.506 6.201 -11.152 0.00 82.60 A N ANISOU 2717 N ASP A 310 9895 12233 9256 -615 7 677 A N ATOM 2718 CA ASP A 310 14.318 5.355 -11.095 0.00 77.16 A C ANISOU 2718 CA ASP A 310 9158 11673 8486 -675 -18 464 A C ATOM 2719 C ASP A 310 13.200 6.052 -10.331 0.00 70.53 A C ANISOU 2719 C ASP A 310 8334 10754 7709 -605 -86 586 A C ATOM 2720 O ASP A 310 12.525 5.448 -9.491 0.00 67.66 A O ANISOU 2720 O ASP A 310 8016 10257 7434 -653 -98 428 A O ATOM 2721 CB ASP A 310 14.636 4.002 -10.457 0.00 76.68 A C ANISOU 2721 CB ASP A 310 9184 11397 8553 -775 45 177 A C ATOM 2722 N SER A 311 12.985 7.337 -10.618 0.00 68.62 A N ANISOU 2722 N SER A 311 8054 10587 7430 -483 -112 879 A N ATOM 2723 CA SER A 311 11.941 8.118 -9.954 0.00 63.72 A C ANISOU 2723 CA SER A 311 7443 9893 6874 -388 -159 1019 A C ATOM 2724 C SER A 311 10.640 7.962 -10.738 0.00 60.61 A C ANISOU 2724 C SER A 311 6876 9927 6225 -360 -205 999 A C ATOM 2725 O SER A 311 10.256 8.803 -11.554 0.00 59.05 A O ANISOU 2725 O SER A 311 6566 10004 5867 -231 -212 1242 A O ATOM 2726 CB SER A 311 12.357 9.579 -9.835 0.00 64.14 A C ANISOU 2726 CB SER A 311 7549 9773 7047 -261 -126 1342 A C ATOM 2727 N GLU A 312 9.953 6.853 -10.478 0.00 60.26 A N ANISOU 2727 N GLU A 312 6800 9955 6141 -483 -223 705 A N ATOM 2728 CA GLU A 312 8.660 6.547 -11.077 0.00 59.01 A C ANISOU 2728 CA GLU A 312 6457 10221 5744 -501 -266 607 A C ATOM 2729 C GLU A 312 7.586 6.443 -10.000 0.00 59.24 A C ANISOU 2729 C GLU A 312 6516 10108 5883 -509 -304 532 A C ATOM 2730 O GLU A 312 6.756 5.531 -10.005 0.00 59.06 A O ANISOU 2730 O GLU A 312 6408 10259 5773 -638 -306 267 A O ATOM 2731 CB GLU A 312 8.730 5.258 -11.893 0.00 57.48 A C ANISOU 2731 CB GLU A 312 6161 10299 5378 -683 -225 271 A C ATOM 2732 N LEU A 313 7.595 7.388 -9.064 0.00 60.68 A N ANISOU 2732 N LEU A 313 6814 9976 6263 -383 -321 748 A N ATOM 2733 CA LEU A 313 6.688 7.344 -7.931 0.00 65.73 A C ANISOU 2733 CA LEU A 313 7499 10448 7029 -383 -351 685 A C ATOM 2734 C LEU A 313 5.241 7.538 -8.384 0.00 65.81 A C ANISOU 2734 C LEU A 313 7313 10868 6823 -323 -406 710 A C ATOM 2735 O LEU A 313 4.958 7.964 -9.508 0.00 62.24 A O ANISOU 2735 O LEU A 313 6694 10822 6132 -232 -425 848 A O ATOM 2736 CB LEU A 313 7.067 8.415 -6.909 0.00 69.36 A C ANISOU 2736 CB LEU A 313 8108 10515 7732 -260 -346 901 A C ATOM 2737 N LYS A 314 4.318 7.214 -7.480 0.00 68.61 A N ANISOU 2737 N LYS A 314 7674 11143 7251 -366 -428 581 A N ATOM 2738 CA LYS A 314 2.892 7.380 -7.716 0.00 67.25 A C ANISOU 2738 CA LYS A 314 7310 11349 6894 -313 -481 586 A C ATOM 2739 C LYS A 314 2.244 7.917 -6.449 0.00 68.95 A C ANISOU 2739 C LYS A 314 7608 11295 7295 -223 -501 669 A C ATOM 2740 O LYS A 314 2.668 7.601 -5.334 0.00 71.98 A O ANISOU 2740 O LYS A 314 8168 11268 7912 -297 -473 573 A O ATOM 2741 CB LYS A 314 2.228 6.060 -8.129 0.00 64.18 A C ANISOU 2741 CB LYS A 314 6778 11273 6336 -537 -470 221 A C ATOM 2742 N GLY A 315 1.209 8.736 -6.631 0.00 65.17 A N ANISOU 2742 N GLY A 315 6987 11077 6697 -49 -543 854 A N ATOM 2743 CA GLY A 315 0.523 9.360 -5.522 0.00 64.29 A C ANISOU 2743 CA GLY A 315 6933 10750 6744 62 -555 946 A C ATOM 2744 C GLY A 315 1.173 10.616 -4.990 0.00 63.83 A C ANISOU 2744 C GLY A 315 7038 10302 6912 243 -513 1227 A C ATOM 2745 O GLY A 315 0.573 11.294 -4.145 0.00 61.89 A O ANISOU 2745 O GLY A 315 6826 9895 6793 361 -508 1320 A O ATOM 2746 N LYS A 316 2.373 10.954 -5.450 0.00 64.77 A N ANISOU 2746 N LYS A 316 7252 10265 7092 256 -468 1346 A N ATOM 2747 CA LYS A 316 3.062 12.150 -4.989 0.00 62.50 A C ANISOU 2747 CA LYS A 316 7115 9599 7035 390 -399 1580 A C ATOM 2748 C LYS A 316 2.413 13.385 -5.613 0.00 57.95 A C ANISOU 2748 C LYS A 316 6436 9198 6384 657 -360 1926 A C ATOM 2749 O LYS A 316 1.376 13.313 -6.280 0.00 57.17 A O ANISOU 2749 O LYS A 316 6140 9540 6043 756 -405 1987 A O ATOM 2750 CB LYS A 316 4.548 12.067 -5.327 0.00 65.20 A C ANISOU 2750 CB LYS A 316 7569 9751 7454 300 -352 1583 A C ATOM 2751 N SER A 317 3.033 14.544 -5.397 0.00 56.71 A N ANISOU 2751 N SER A 317 6406 8702 6439 782 -256 2159 A N ATOM 2752 CA SER A 317 2.575 15.803 -5.969 0.00 55.26 A C ANISOU 2752 CA SER A 317 6162 8595 6241 1061 -166 2535 A C ATOM 2753 C SER A 317 3.416 16.251 -7.156 0.00 55.48 A C ANISOU 2753 C SER A 317 6174 8719 6189 1132 -89 2783 A C ATOM 2754 O SER A 317 2.867 16.752 -8.142 0.00 55.89 A O ANISOU 2754 O SER A 317 6075 9119 6043 1348 -59 3072 A O ATOM 2755 CB SER A 317 2.583 16.901 -4.901 0.00 53.63 A C ANISOU 2755 CB SER A 317 6111 7907 6360 1163 -54 2635 A C ATOM 2756 N GLU A 318 4.732 16.080 -7.088 0.00 57.01 A N ANISOU 2756 N GLU A 318 6505 8642 6516 964 -51 2689 A N ATOM 2757 CA GLU A 318 5.617 16.486 -8.173 0.00 58.60 A C ANISOU 2757 CA GLU A 318 6698 8915 6654 1009 33 2912 A C ATOM 2758 C GLU A 318 6.835 15.564 -8.216 0.00 61.33 A C ANISOU 2758 C GLU A 318 7113 9185 7006 754 -8 2653 A C ATOM 2759 O GLU A 318 7.980 16.010 -8.306 0.00 62.41 A O ANISOU 2759 O GLU A 318 7355 9067 7291 705 87 2730 A O ATOM 2760 CB GLU A 318 6.030 17.949 -8.016 0.00 57.89 A C ANISOU 2760 CB GLU A 318 6732 8431 6831 1166 225 3226 A C ATOM 2761 N SER A 319 6.595 14.254 -8.153 0.00 62.69 A N ANISOU 2761 N SER A 319 7221 9575 7025 590 -134 2340 A N ATOM 2762 CA SER A 319 7.669 13.272 -8.243 0.00 65.65 A C ANISOU 2762 CA SER A 319 7648 9904 7392 375 -161 2096 A C ATOM 2763 C SER A 319 8.665 13.442 -7.101 0.00 68.65 A C ANISOU 2763 C SER A 319 8217 9791 8076 267 -117 1990 A C ATOM 2764 O SER A 319 8.332 14.027 -6.065 0.00 67.26 A O ANISOU 2764 O SER A 319 8124 9334 8098 308 -94 2001 A O ATOM 2765 CB SER A 319 8.380 13.389 -9.593 1.00 76.01 A C ANISOU 2765 CB SER A 319 8884 11467 8530 403 -116 2255 A C ATOM 2766 N ILE A 320 9.886 12.934 -7.277 1.00 82.83 A N ANISOU 2766 N ILE A 320 10066 11511 9896 130 -101 1876 A N ATOM 2767 CA ILE A 320 10.904 13.006 -6.234 1.00 73.37 A C ANISOU 2767 CA ILE A 320 9009 9927 8942 21 -68 1757 A C ATOM 2768 C ILE A 320 12.231 12.461 -6.747 1.00 67.23 A C ANISOU 2768 C ILE A 320 8243 9171 8130 -95 -46 1677 A C ATOM 2769 O ILE A 320 12.282 11.377 -7.340 1.00 66.45 A O ANISOU 2769 O ILE A 320 8081 9310 7858 -163 -94 1530 A O ATOM 2770 CB ILE A 320 10.454 12.236 -4.976 1.00 64.03 A C ANISOU 2770 CB ILE A 320 7875 8614 7838 -58 -141 1505 A C ATOM 2771 N ASP A 321 13.314 13.213 -6.535 1.00 64.58 A N ANISOU 2771 N ASP A 321 7980 8593 7963 -126 41 1758 A N ATOM 2772 CA ASP A 321 14.649 12.683 -6.780 1.00 56.26 A C ANISOU 2772 CA ASP A 321 6938 7536 6905 -242 59 1655 A C ATOM 2773 C ASP A 321 15.005 11.666 -5.703 1.00 53.62 A C ANISOU 2773 C ASP A 321 6652 7085 6638 -345 -3 1380 A C ATOM 2774 O ASP A 321 14.783 11.906 -4.510 1.00 56.02 A O ANISOU 2774 O ASP A 321 7015 7179 7092 -353 -17 1309 A O ATOM 2775 CB ASP A 321 15.692 13.799 -6.802 1.00 64.95 A C ANISOU 2775 CB ASP A 321 8083 8423 8170 -266 181 1802 A C ATOM 2776 CG ASP A 321 15.630 14.625 -8.062 1.00 77.95 A C ANISOU 2776 CG ASP A 321 9680 10207 9731 -165 274 2101 A C ATOM 2777 OD1 ASP A 321 15.837 14.051 -9.150 1.00 80.36 A O ANISOU 2777 OD1 ASP A 321 9903 10811 9822 -162 252 2126 A O ATOM 2778 OD2 ASP A 321 15.387 15.846 -7.962 1.00 88.37 A O ANISOU 2778 OD2 ASP A 321 11042 11336 11199 -83 386 2314 A O ATOM 2779 N ILE A 322 15.561 10.534 -6.125 1.00 52.36 A N ANISOU 2779 N ILE A 322 6463 7065 6365 -410 -25 1234 A N ATOM 2780 CA ILE A 322 15.819 9.391 -5.256 1.00 47.05 A C ANISOU 2780 CA ILE A 322 5829 6315 5733 -472 -61 1005 A C ATOM 2781 C ILE A 322 17.326 9.187 -5.123 1.00 42.51 A C ANISOU 2781 C ILE A 322 5266 5671 5215 -528 -20 952 A C ATOM 2782 O ILE A 322 18.055 9.260 -6.116 1.00 44.54 A O ANISOU 2782 O ILE A 322 5479 6050 5394 -545 23 1013 A O ATOM 2783 CB ILE A 322 15.161 8.122 -5.828 1.00 53.23 A C ANISOU 2783 CB ILE A 322 6568 7301 6355 -495 -88 857 A C ATOM 2784 CG1 ILE A 322 13.627 8.212 -5.834 1.00 65.42 A C ANISOU 2784 CG1 ILE A 322 8074 8954 7829 -455 -137 870 A C ATOM 2785 CG2 ILE A 322 15.616 6.928 -5.041 1.00 56.27 A C ANISOU 2785 CG2 ILE A 322 7005 7570 6804 -543 -77 659 A C ATOM 2786 CD1 ILE A 322 13.032 9.085 -4.774 1.00 65.61 A C ANISOU 2786 CD1 ILE A 322 8149 8783 7997 -396 -160 953 A C ATOM 2787 N TYR A 323 17.784 8.898 -3.905 1.00 39.44 A N ANISOU 2787 N TYR A 323 4918 5125 4942 -548 -32 841 A N ATOM 2788 CA TYR A 323 19.202 8.678 -3.632 1.00 37.68 A C ANISOU 2788 CA TYR A 323 4680 4877 4760 -585 2 785 A C ATOM 2789 C TYR A 323 19.410 7.407 -2.820 1.00 40.98 A C ANISOU 2789 C TYR A 323 5117 5274 5181 -561 -12 634 A C ATOM 2790 O TYR A 323 18.498 6.920 -2.150 1.00 41.32 A O ANISOU 2790 O TYR A 323 5200 5260 5240 -532 -42 576 A O ATOM 2791 CB TYR A 323 19.813 9.846 -2.851 1.00 41.62 A C ANISOU 2791 CB TYR A 323 5178 5235 5403 -627 25 824 A C ATOM 2792 CG TYR A 323 19.978 11.087 -3.674 1.00 41.01 A C ANISOU 2792 CG TYR A 323 5088 5133 5361 -656 94 988 A C ATOM 2793 CD1 TYR A 323 18.934 11.977 -3.843 1.00 45.19 A C ANISOU 2793 CD1 TYR A 323 5650 5587 5934 -610 110 1122 A C ATOM 2794 CD2 TYR A 323 21.191 11.377 -4.277 1.00 46.09 A C ANISOU 2794 CD2 TYR A 323 5684 5827 6001 -718 162 1026 A C ATOM 2795 CE1 TYR A 323 19.088 13.120 -4.606 1.00 51.75 A C ANISOU 2795 CE1 TYR A 323 6477 6374 6813 -610 207 1314 A C ATOM 2796 CE2 TYR A 323 21.361 12.516 -5.022 1.00 46.77 A C ANISOU 2796 CE2 TYR A 323 5766 5871 6135 -744 254 1199 A C ATOM 2797 CZ TYR A 323 20.307 13.386 -5.185 1.00 55.43 A C ANISOU 2797 CZ TYR A 323 6906 6871 7284 -683 285 1354 A C ATOM 2798 OH TYR A 323 20.481 14.520 -5.946 1.00 57.52 A O ANISOU 2798 OH TYR A 323 7172 7072 7609 -684 410 1566 A O ATOM 2799 N SER A 324 20.634 6.886 -2.856 1.00 40.12 A N ANISOU 2799 N SER A 324 4974 5212 5058 -560 25 588 A N ATOM 2800 CA SER A 324 21.042 5.833 -1.936 1.00 37.64 A C ANISOU 2800 CA SER A 324 4669 4868 4766 -501 36 493 A C ATOM 2801 C SER A 324 22.490 6.105 -1.522 1.00 39.36 A C ANISOU 2801 C SER A 324 4813 5139 5004 -500 53 494 A C ATOM 2802 O SER A 324 23.030 7.193 -1.754 1.00 38.92 A O ANISOU 2802 O SER A 324 4710 5103 4976 -576 56 543 A O ATOM 2803 CB SER A 324 20.858 4.442 -2.560 1.00 38.76 A C ANISOU 2803 CB SER A 324 4838 5045 4844 -466 95 411 A C ATOM 2804 OG SER A 324 21.159 3.409 -1.635 1.00 40.32 A O ANISOU 2804 OG SER A 324 5060 5175 5085 -380 138 359 A O ATOM 2805 N ILE A 325 23.088 5.128 -0.843 1.00 38.79 A N ANISOU 2805 N ILE A 325 4722 5095 4924 -412 79 445 A N ATOM 2806 CA ILE A 325 24.503 5.130 -0.487 1.00 40.09 A C ANISOU 2806 CA ILE A 325 4784 5378 5070 -383 98 438 A C ATOM 2807 C ILE A 325 25.174 4.018 -1.283 1.00 47.07 A C ANISOU 2807 C ILE A 325 5658 6330 5897 -307 178 423 A C ATOM 2808 O ILE A 325 24.684 2.883 -1.299 1.00 45.05 A O ANISOU 2808 O ILE A 325 5473 6000 5645 -224 233 393 A O ATOM 2809 CB ILE A 325 24.703 4.902 1.023 1.00 42.52 A C ANISOU 2809 CB ILE A 325 5049 5717 5390 -298 71 419 A C ATOM 2810 CG1 ILE A 325 24.090 6.027 1.855 1.00 49.98 A C ANISOU 2810 CG1 ILE A 325 5992 6605 6391 -384 4 398 A C ATOM 2811 CG2 ILE A 325 26.188 4.749 1.360 1.00 46.14 A C ANISOU 2811 CG2 ILE A 325 5368 6371 5793 -243 93 411 A C ATOM 2812 CD1 ILE A 325 24.602 7.406 1.530 1.00 50.88 A C ANISOU 2812 CD1 ILE A 325 6046 6737 6549 -533 2 384 A C ATOM 2813 N ASP A 326 26.310 4.318 -1.901 1.00 44.71 A N ANISOU 2813 N ASP A 326 5269 6162 5557 -339 205 432 A N ATOM 2814 CA AASP A 326 27.057 3.334 -2.683 0.68 49.88 A C ANISOU 2814 CA AASP A 326 5900 6895 6156 -264 291 408 A C ATOM 2815 CA BASP A 326 27.054 3.333 -2.681 0.32 50.06 A C ANISOU 2815 CA BASP A 326 5924 6918 6180 -263 291 408 A C ATOM 2816 C ASP A 326 28.191 2.802 -1.814 1.00 57.49 A C ANISOU 2816 C ASP A 326 6766 7974 7104 -129 320 416 A C ATOM 2817 O ASP A 326 29.241 3.436 -1.695 1.00 61.88 A O ANISOU 2817 O ASP A 326 7192 8693 7626 -167 301 422 A O ATOM 2818 CB AASP A 326 27.584 3.950 -3.975 0.68 46.95 A C ANISOU 2818 CB AASP A 326 5479 6630 5730 -369 310 425 A C ATOM 2819 CB BASP A 326 27.574 3.942 -3.978 0.32 47.11 A C ANISOU 2819 CB BASP A 326 5500 6649 5750 -369 310 425 A C ATOM 2820 CG AASP A 326 28.319 2.947 -4.843 0.68 52.89 A C ANISOU 2820 CG AASP A 326 6203 7476 6419 -297 405 379 A C ATOM 2821 CG BASP A 326 28.246 2.918 -4.872 0.32 52.99 A C ANISOU 2821 CG BASP A 326 6222 7481 6431 -298 405 377 A C ATOM 2822 OD1AASP A 326 28.274 1.741 -4.531 0.68 52.35 A O ANISOU 2822 OD1AASP A 326 6176 7344 6371 -167 473 331 A O ATOM 2823 OD1BASP A 326 27.606 1.892 -5.188 0.32 55.81 A O ANISOU 2823 OD1BASP A 326 6661 7754 6790 -244 465 310 A O ATOM 2824 OD2AASP A 326 28.937 3.365 -5.842 0.68 46.96 A O ANISOU 2824 OD2AASP A 326 5388 6849 5604 -367 429 395 A O ATOM 2825 OD2BASP A 326 29.412 3.141 -5.257 0.32 50.59 A O ANISOU 2825 OD2BASP A 326 5813 7328 6082 -306 435 390 A O ATOM 2826 N ASN A 327 27.969 1.639 -1.205 1.00 72.17 A N ANISOU 2826 N ASN A 327 8675 9760 8986 32 379 422 A N ATOM 2827 CA AASN A 327 28.970 0.937 -0.414 0.55 82.33 A C ANISOU 2827 CA AASN A 327 9869 11171 10243 221 430 470 A C ATOM 2828 CA BASN A 327 29.009 0.948 -0.451 0.45 82.29 A C ANISOU 2828 CA BASN A 327 9860 11171 10236 219 431 469 A C ATOM 2829 C ASN A 327 28.914 -0.540 -0.794 1.00 95.85 A C ANISOU 2829 C ASN A 327 11667 12756 11994 380 584 470 A C ATOM 2830 O ASN A 327 28.190 -0.939 -1.712 1.00100.16 A O ANISOU 2830 O ASN A 327 12325 13152 12579 305 642 394 A O ATOM 2831 CB AASN A 327 28.745 1.160 1.091 0.55 79.08 A C ANISOU 2831 CB AASN A 327 9417 10802 9829 287 364 517 A C ATOM 2832 CB BASN A 327 28.883 1.227 1.057 0.45 79.14 A C ANISOU 2832 CB BASN A 327 9408 10834 9828 282 361 515 A C ATOM 2833 CG AASN A 327 27.529 0.412 1.633 0.55 72.67 A C ANISOU 2833 CG AASN A 327 8751 9774 9086 360 402 544 A C ATOM 2834 CG BASN A 327 29.458 2.590 1.461 0.45 67.04 A C ANISOU 2834 CG BASN A 327 7732 9490 8252 138 254 476 A C ATOM 2835 ND2AASN A 327 27.227 0.637 2.906 0.55 69.03 A N ANISOU 2835 ND2AASN A 327 8259 9359 8611 410 343 586 A N ATOM 2836 ND2BASN A 327 29.055 3.081 2.634 0.45 52.31 A N ANISOU 2836 ND2BASN A 327 5835 7657 6383 123 180 466 A N ATOM 2837 OD1AASN A 327 26.877 -0.356 0.927 0.55 79.18 A O ANISOU 2837 OD1AASN A 327 9703 10411 9971 360 491 511 A O ATOM 2838 OD1BASN A 327 30.266 3.178 0.740 0.45 58.92 A O ANISOU 2838 OD1BASN A 327 6617 8576 7195 34 254 442 A O ATOM 2839 N GLU A 328 29.659 -1.369 -0.060 1.00101.99 A N ANISOU 2839 N GLU A 328 12386 13604 12762 606 667 553 A N ATOM 2840 CA GLU A 328 29.696 -2.795 -0.372 1.00112.82 A C ANISOU 2840 CA GLU A 328 13845 14817 14204 779 858 564 A C ATOM 2841 C GLU A 328 28.320 -3.446 -0.258 1.00124.95 A C ANISOU 2841 C GLU A 328 15564 16059 15854 749 932 526 A C ATOM 2842 O GLU A 328 28.031 -4.412 -0.973 1.00125.92 A O ANISOU 2842 O GLU A 328 15791 15995 16058 764 1095 445 A O ATOM 2843 CB GLU A 328 30.694 -3.502 0.548 1.00112.67 A C ANISOU 2843 CB GLU A 328 13722 14932 14154 1068 943 712 A C ATOM 2844 CG GLU A 328 30.325 -3.467 2.028 1.00124.33 A C ANISOU 2844 CG GLU A 328 15177 16449 15614 1183 894 836 A C ATOM 2845 CD GLU A 328 30.990 -2.327 2.776 1.00122.30 A C ANISOU 2845 CD GLU A 328 14720 16532 15216 1132 717 852 A C ATOM 2846 OE1 GLU A 328 31.533 -1.415 2.117 1.00121.33 A O ANISOU 2846 OE1 GLU A 328 14505 16553 15041 955 627 755 A O ATOM 2847 OE2 GLU A 328 30.962 -2.340 4.025 1.00109.03 A O ANISOU 2847 OE2 GLU A 328 12967 14983 13477 1259 681 952 A O ATOM 2848 N MET A 329 27.462 -2.937 0.626 1.00121.91 A N ANISOU 2848 N MET A 329 17299 15451 13568 -1288 5199 1036 A N ATOM 2849 CA MET A 329 26.167 -3.557 0.873 1.00118.45 A C ANISOU 2849 CA MET A 329 16760 14815 13429 -722 4830 1050 A C ATOM 2850 C MET A 329 25.191 -3.322 -0.272 1.00133.91 A C ANISOU 2850 C MET A 329 18991 16797 15094 -481 4636 1466 A C ATOM 2851 O MET A 329 24.816 -4.264 -0.979 1.00139.19 A O ANISOU 2851 O MET A 329 19409 17875 15601 -229 4397 1322 A O ATOM 2852 CB MET A 329 25.570 -3.025 2.177 1.00107.28 A C ANISOU 2852 CB MET A 329 15524 12702 12534 -558 4805 1169 A C ATOM 2853 CG MET A 329 24.710 -4.035 2.908 1.00106.12 A C ANISOU 2853 CG MET A 329 15046 12447 12827 -51 4483 914 A C ATOM 2854 SD MET A 329 25.640 -5.159 3.964 1.00108.85 A S ANISOU 2854 SD MET A 329 14812 13067 13480 -125 4524 233 A S ATOM 2855 CE MET A 329 26.612 -4.015 4.929 1.00 92.06 A C ANISOU 2855 CE MET A 329 12950 10544 11486 -637 4904 295 A C ATOM 2856 N THR A 330 24.775 -2.070 -0.464 1.00128.32 A N ANISOU 2856 N THR A 330 18800 15649 14306 -560 4737 1988 A N ATOM 2857 CA THR A 330 23.788 -1.756 -1.486 1.00120.86 A C ANISOU 2857 CA THR A 330 18139 14675 13109 -318 4548 2432 A C ATOM 2858 C THR A 330 24.259 -2.110 -2.888 1.00125.76 A C ANISOU 2858 C THR A 330 18693 15930 13159 -492 4563 2402 A C ATOM 2859 O THR A 330 23.452 -2.070 -3.823 1.00121.60 A O ANISOU 2859 O THR A 330 18330 15482 12391 -274 4361 2710 A O ATOM 2860 CB THR A 330 23.437 -0.267 -1.429 1.00118.32 A C ANISOU 2860 CB THR A 330 18402 13776 12780 -433 4719 2996 A C ATOM 2861 CG2 THR A 330 22.634 0.045 -0.173 1.00113.53 A C ANISOU 2861 CG2 THR A 330 17905 12500 12733 -142 4639 3104 A C ATOM 2862 OG1 THR A 330 24.643 0.510 -1.436 1.00119.79 A O ANISOU 2862 OG1 THR A 330 18774 13994 12747 -987 5111 2998 A O ATOM 2863 N ARG A 331 25.533 -2.456 -3.058 1.00134.75 A N ANISOU 2863 N ARG A 331 19598 17522 14079 -874 4797 2048 A N ATOM 2864 CA ARG A 331 26.086 -2.736 -4.378 1.00141.34 A C ANISOU 2864 CA ARG A 331 20394 18951 14357 -1077 4861 2016 A C ATOM 2865 C ARG A 331 25.953 -4.215 -4.736 1.00145.25 A C ANISOU 2865 C ARG A 331 20417 19970 14803 -807 4608 1598 A C ATOM 2866 O ARG A 331 25.349 -4.562 -5.757 1.00145.09 A O ANISOU 2866 O ARG A 331 20441 20204 14482 -613 4396 1734 A O ATOM 2867 CB ARG A 331 27.553 -2.288 -4.429 1.00126.99 A C ANISOU 2867 CB ARG A 331 18587 17353 12310 -1645 5273 1883 A C ATOM 2868 CG ARG A 331 28.199 -2.478 -5.786 1.00129.89 A C ANISOU 2868 CG ARG A 331 18948 18312 12093 -1889 5389 1871 A C ATOM 2869 CD ARG A 331 29.608 -1.886 -5.887 1.00132.00 A C ANISOU 2869 CD ARG A 331 19274 18760 12120 -2466 5812 1813 A C ATOM 2870 NE ARG A 331 29.791 -0.618 -5.187 1.00132.24 A N ANISOU 2870 NE ARG A 331 19673 18248 12323 -2730 6041 2101 A N ATOM 2871 CZ ARG A 331 30.476 -0.461 -4.060 1.00130.01 A C ANISOU 2871 CZ ARG A 331 19259 17774 12364 -2953 6222 1880 A C ATOM 2872 NH1 ARG A 331 31.024 -1.489 -3.432 1.00126.20 A N ANISOU 2872 NH1 ARG A 331 18267 17579 12106 -2924 6195 1372 A N ATOM 2873 NH2 ARG A 331 30.626 0.761 -3.559 1.00131.78 A N ANISOU 2873 NH2 ARG A 331 19882 17508 12681 -3221 6440 2181 A N ATOM 2874 N LYS A 332 26.500 -5.098 -3.897 0.81147.57 A N ANISOU 2874 N LYS A 332 20265 20419 15385 -791 4625 1092 A N ATOM 2875 CA LYS A 332 26.558 -6.529 -4.199 0.81140.00 A C ANISOU 2875 CA LYS A 332 18843 19982 14367 -584 4441 646 A C ATOM 2876 C LYS A 332 25.277 -7.201 -3.712 0.81138.49 A C ANISOU 2876 C LYS A 332 18509 19557 14553 -41 4045 607 A C ATOM 2877 O LYS A 332 25.212 -7.798 -2.635 0.81134.42 A O ANISOU 2877 O LYS A 332 17692 18899 14483 142 3965 286 A O ATOM 2878 CB LYS A 332 27.796 -7.157 -3.569 0.81126.57 A C ANISOU 2878 CB LYS A 332 16728 18583 12781 -829 4665 132 A C ATOM 2879 N SER A 333 24.239 -7.102 -4.539 0.93142.33 A N ANISOU 2879 N SER A 333 19215 20014 14850 216 3790 949 A N ATOM 2880 CA SER A 333 22.976 -7.779 -4.290 0.93144.35 A C ANISOU 2880 CA SER A 333 19335 20119 15394 728 3390 945 A C ATOM 2881 C SER A 333 22.487 -8.402 -5.590 0.93146.42 A C ANISOU 2881 C SER A 333 19578 20825 15230 879 3152 999 A C ATOM 2882 O SER A 333 22.854 -7.971 -6.686 0.93155.00 A O ANISOU 2882 O SER A 333 20898 22177 15819 625 3277 1210 A O ATOM 2883 CB SER A 333 21.916 -6.817 -3.733 0.93134.12 A C ANISOU 2883 CB SER A 333 18387 18150 14423 952 3279 1419 A C ATOM 2884 N SER A 334 21.656 -9.434 -5.457 0.79141.89 A N ANISOU 2884 N SER A 334 18729 20332 14850 1288 2806 802 A N ATOM 2885 CA SER A 334 20.955 -10.004 -6.600 0.79143.59 A C ANISOU 2885 CA SER A 334 18955 20889 14715 1485 2516 899 A C ATOM 2886 C SER A 334 19.750 -9.171 -7.014 0.79164.18 A C ANISOU 2886 C SER A 334 21948 23138 17293 1693 2296 1500 A C ATOM 2887 O SER A 334 18.971 -9.611 -7.866 0.79163.46 A O ANISOU 2887 O SER A 334 21873 23265 16969 1904 1998 1629 A O ATOM 2888 CB SER A 334 20.504 -11.434 -6.290 0.79128.55 A C ANISOU 2888 CB SER A 334 16612 19201 13030 1837 2224 461 A C ATOM 2889 OG SER A 334 21.606 -12.319 -6.228 0.79109.60 A O ANISOU 2889 OG SER A 334 13861 17248 10532 1651 2412 -79 A O ATOM 2890 N GLY A 335 19.586 -7.985 -6.436 0.93154.58 A N ANISOU 2890 N GLY A 335 21046 21384 16302 1634 2439 1874 A N ATOM 2891 CA GLY A 335 18.409 -7.180 -6.686 0.93141.15 A C ANISOU 2891 CA GLY A 335 19697 19289 14643 1868 2243 2454 A C ATOM 2892 C GLY A 335 17.176 -7.820 -6.075 0.93146.93 A C ANISOU 2892 C GLY A 335 20223 19787 15816 2374 1861 2435 A C ATOM 2893 O GLY A 335 17.229 -8.852 -5.408 0.93149.35 A O ANISOU 2893 O GLY A 335 20132 20204 16412 2541 1755 1971 A O ATOM 2894 N GLY A 336 16.040 -7.173 -6.307 0.62138.51 A N ANISOU 2894 N GLY A 336 19438 18385 14806 2625 1657 2965 A N ATOM 2895 CA GLY A 336 14.769 -7.739 -5.914 0.62135.65 A C ANISOU 2895 CA GLY A 336 18903 17831 14807 3112 1268 3021 A C ATOM 2896 C GLY A 336 14.211 -8.659 -6.982 0.62145.33 A C ANISOU 2896 C GLY A 336 19971 19549 15698 3278 919 2973 A C ATOM 2897 O GLY A 336 14.716 -8.724 -8.101 0.62148.15 A O ANISOU 2897 O GLY A 336 20420 20355 15517 3027 976 2975 A O ATOM 2898 N LEU A 337 13.154 -9.383 -6.613 1.00146.03 A N ANISOU 2898 N LEU A 337 19826 19545 16113 3702 555 2926 A N ATOM 2899 CA LEU A 337 12.568 -10.392 -7.490 1.00142.33 A C ANISOU 2899 CA LEU A 337 19166 19530 15383 3882 192 2826 A C ATOM 2900 C LEU A 337 13.475 -11.616 -7.557 1.00135.47 A C ANISOU 2900 C LEU A 337 17928 19180 14366 3735 256 2165 A C ATOM 2901 O LEU A 337 13.012 -12.748 -7.384 1.00127.22 A O ANISOU 2901 O LEU A 337 16550 18313 13476 3995 -17 1846 A O ATOM 2902 CB LEU A 337 12.323 -9.825 -8.890 1.00137.00 A C ANISOU 2902 CB LEU A 337 18827 19082 14145 3751 117 3283 A C ATOM 2903 N GLU A 338 14.767 -11.403 -7.820 0.78139.20 A N ANISOU 2903 N GLU A 338 18456 19899 14537 3321 621 1962 A N ATOM 2904 CA GLU A 338 15.726 -12.497 -7.716 0.78138.36 A C ANISOU 2904 CA GLU A 338 17987 20232 14352 3181 741 1329 A C ATOM 2905 C GLU A 338 15.846 -12.977 -6.275 0.78132.98 A C ANISOU 2905 C GLU A 338 16984 19279 14264 3347 783 946 A C ATOM 2906 O GLU A 338 15.983 -14.179 -6.022 0.78123.45 A O ANISOU 2906 O GLU A 338 15398 18347 13160 3472 679 455 A O ATOM 2907 CB GLU A 338 17.088 -12.057 -8.251 0.78139.15 A C ANISOU 2907 CB GLU A 338 18223 20617 14032 2699 1147 1241 A C ATOM 2908 N ILE A 339 15.791 -12.051 -5.315 1.00134.79 A N ANISOU 2908 N ILE A 339 17371 18960 14882 3351 939 1163 A N ATOM 2909 CA ILE A 339 15.848 -12.444 -3.911 1.00128.12 A C ANISOU 2909 CA ILE A 339 16251 17818 14612 3515 971 830 A C ATOM 2910 C ILE A 339 14.601 -13.238 -3.536 1.00108.88 A C ANISOU 2910 C ILE A 339 13592 15251 12526 4000 563 790 A C ATOM 2911 O ILE A 339 14.683 -14.252 -2.834 1.00101.62 A O ANISOU 2911 O ILE A 339 12299 14415 11899 4162 487 321 A O ATOM 2912 CB ILE A 339 16.036 -11.202 -3.018 1.00125.98 A C ANISOU 2912 CB ILE A 339 16253 16966 14646 3394 1234 1109 A C ATOM 2913 CG1 ILE A 339 17.513 -10.791 -2.979 1.00131.16 A C ANISOU 2913 CG1 ILE A 339 16956 17787 15092 2908 1663 912 A C ATOM 2914 CG2 ILE A 339 15.557 -11.470 -1.600 1.00102.38 A C ANISOU 2914 CG2 ILE A 339 13067 13530 12302 3695 1150 940 A C ATOM 2915 CD1 ILE A 339 17.768 -9.407 -2.398 1.00126.63 A C ANISOU 2915 CD1 ILE A 339 16748 16693 14672 2699 1947 1260 A C ATOM 2916 N ALA A 340 13.431 -12.809 -4.020 0.79110.11 A N ANISOU 2916 N ALA A 340 16369 15999 9467 4027 -849 -2318 A N ATOM 2917 CA ALA A 340 12.189 -13.495 -3.673 0.79 92.61 A C ANISOU 2917 CA ALA A 340 13682 13929 7576 4062 -788 -2954 A C ATOM 2918 C ALA A 340 12.195 -14.941 -4.159 0.79101.08 A C ANISOU 2918 C ALA A 340 14433 15161 8813 3946 -789 -3157 A C ATOM 2919 O ALA A 340 11.666 -15.832 -3.484 0.79 80.56 A O ANISOU 2919 O ALA A 340 11501 12547 6560 3610 -560 -3438 A O ATOM 2920 CB ALA A 340 10.991 -12.743 -4.255 0.79 91.32 A C ANISOU 2920 CB ALA A 340 13315 13840 7541 4586 -1146 -3405 A C ATOM 2921 N ARG A 341 12.773 -15.194 -5.336 0.91 99.52 A N ANISOU 2921 N ARG A 341 14293 15060 8462 4129 -1033 -2964 A N ATOM 2922 CA ARG A 341 12.892 -16.570 -5.808 0.91 96.10 A C ANISOU 2922 CA ARG A 341 13565 14761 8189 4043 -1075 -3165 A C ATOM 2923 C ARG A 341 13.832 -17.370 -4.913 0.91 97.43 A C ANISOU 2923 C ARG A 341 13863 14786 8371 3565 -810 -2957 A C ATOM 2924 O ARG A 341 13.564 -18.538 -4.605 0.91 89.09 A O ANISOU 2924 O ARG A 341 12533 13692 7624 3318 -766 -3203 A O ATOM 2925 CB ARG A 341 13.381 -16.594 -7.258 0.91 88.30 A C ANISOU 2925 CB ARG A 341 12630 13913 7007 4332 -1351 -3011 A C ATOM 2926 N ASN A 342 14.933 -16.754 -4.477 0.89 98.28 A N ANISOU 2926 N ASN A 342 14360 14715 8265 3365 -674 -2451 A N ATOM 2927 CA ASN A 342 15.889 -17.462 -3.633 0.89 95.78 A C ANISOU 2927 CA ASN A 342 14209 14200 7983 2958 -530 -2260 A C ATOM 2928 C ASN A 342 15.247 -17.896 -2.321 0.89100.11 A C ANISOU 2928 C ASN A 342 14715 14512 8811 2536 -309 -2359 A C ATOM 2929 O ASN A 342 15.504 -19.003 -1.832 0.89 91.18 A O ANISOU 2929 O ASN A 342 13565 13200 7878 2188 -303 -2381 A O ATOM 2930 CB ASN A 342 17.105 -16.575 -3.366 0.89 95.24 A C ANISOU 2930 CB ASN A 342 14505 13950 7731 2825 -443 -1750 A C ATOM 2931 N ILE A 343 14.402 -17.041 -1.741 0.82 87.03 A N ANISOU 2931 N ILE A 343 13067 12843 7157 2546 -136 -2442 A N ATOM 2932 CA ILE A 343 13.810 -17.347 -0.442 0.82 86.83 A C ANISOU 2932 CA ILE A 343 13045 12638 7310 2081 176 -2544 A C ATOM 2933 C ILE A 343 12.893 -18.562 -0.539 0.82 83.52 A C ANISOU 2933 C ILE A 343 12203 12290 7239 1889 216 -2973 A C ATOM 2934 O ILE A 343 12.912 -19.438 0.334 0.82 79.80 A O ANISOU 2934 O ILE A 343 11845 11593 6881 1362 392 -2932 A O ATOM 2935 CB ILE A 343 13.068 -16.111 0.099 0.82 73.64 A C ANISOU 2935 CB ILE A 343 11391 11003 5585 2188 357 -2655 A C ATOM 2936 CG1 ILE A 343 14.078 -15.079 0.614 0.82 82.12 A C ANISOU 2936 CG1 ILE A 343 12972 11873 6357 2181 368 -2172 A C ATOM 2937 CG2 ILE A 343 12.116 -16.493 1.225 0.82 78.82 A C ANISOU 2937 CG2 ILE A 343 11892 11617 6441 1729 751 -2960 A C ATOM 2938 CD1 ILE A 343 13.836 -13.664 0.141 0.82 86.84 A C ANISOU 2938 CD1 ILE A 343 13625 12552 6816 2645 207 -2170 A C ATOM 2939 N GLY A 344 12.088 -18.644 -1.600 0.84 81.69 A N ANISOU 2939 N GLY A 344 11524 12336 7179 2298 16 -3388 A N ATOM 2940 CA GLY A 344 11.158 -19.754 -1.727 0.84 82.53 A C ANISOU 2940 CA GLY A 344 11167 12505 7684 2128 38 -3851 A C ATOM 2941 C GLY A 344 11.847 -21.093 -1.927 0.84 81.18 A C ANISOU 2941 C GLY A 344 11046 12182 7617 1901 -140 -3740 A C ATOM 2942 O GLY A 344 11.406 -22.112 -1.388 0.84 88.60 A O ANISOU 2942 O GLY A 344 11865 12960 8838 1441 -14 -3900 A O ATOM 2943 N HIS A 345 12.929 -21.115 -2.705 1.00 80.41 A N ANISOU 2943 N HIS A 345 11122 12125 7305 2199 -438 -3497 A N ATOM 2944 CA HIS A 345 13.638 -22.372 -2.933 1.00 86.91 A C ANISOU 2944 CA HIS A 345 11947 12804 8272 2052 -676 -3476 A C ATOM 2945 C HIS A 345 14.315 -22.861 -1.658 1.00 86.61 A C ANISOU 2945 C HIS A 345 12339 12328 8242 1471 -561 -3135 A C ATOM 2946 O HIS A 345 14.312 -24.062 -1.365 1.00 84.72 A O ANISOU 2946 O HIS A 345 12096 11832 8261 1134 -691 -3217 A O ATOM 2947 CB HIS A 345 14.666 -22.198 -4.051 1.00 85.30 A C ANISOU 2947 CB HIS A 345 11788 12801 7822 2496 -961 -3373 A C ATOM 2948 N TYR A 346 14.895 -21.941 -0.887 1.00 76.28 A N ANISOU 2948 N TYR A 346 11449 10883 6649 1355 -374 -2753 A N ATOM 2949 CA TYR A 346 15.553 -22.316 0.360 1.00 80.21 A C ANISOU 2949 CA TYR A 346 12444 10931 7102 839 -325 -2426 A C ATOM 2950 C TYR A 346 14.549 -22.871 1.361 1.00 87.82 A C ANISOU 2950 C TYR A 346 13473 11702 8194 272 -31 -2539 A C ATOM 2951 O TYR A 346 14.785 -23.913 1.984 1.00 85.38 A O ANISOU 2951 O TYR A 346 13451 11004 7988 -186 -149 -2439 A O ATOM 2952 CB TYR A 346 16.277 -21.095 0.934 1.00 84.31 A C ANISOU 2952 CB TYR A 346 13362 11374 7299 883 -191 -2050 A C ATOM 2953 CG TYR A 346 16.928 -21.302 2.281 1.00 80.17 A C ANISOU 2953 CG TYR A 346 13416 10371 6674 401 -173 -1720 A C ATOM 2954 CD1 TYR A 346 16.210 -21.162 3.465 1.00 78.77 A C ANISOU 2954 CD1 TYR A 346 13516 10033 6381 -56 181 -1672 A C ATOM 2955 CD2 TYR A 346 18.275 -21.628 2.365 1.00 68.15 A C ANISOU 2955 CD2 TYR A 346 12170 8560 5164 409 -525 -1502 A C ATOM 2956 CE1 TYR A 346 16.827 -21.346 4.697 1.00 81.23 A C ANISOU 2956 CE1 TYR A 346 14465 9880 6517 -494 153 -1352 A C ATOM 2957 CE2 TYR A 346 18.892 -21.816 3.563 1.00 65.65 A C ANISOU 2957 CE2 TYR A 346 12426 7757 4761 25 -620 -1227 A C ATOM 2958 CZ TYR A 346 18.172 -21.674 4.739 1.00 71.36 A C ANISOU 2958 CZ TYR A 346 13524 8297 5294 -429 -294 -1118 A C ATOM 2959 OH TYR A 346 18.813 -21.867 5.939 1.00 68.66 A O ANISOU 2959 OH TYR A 346 13859 7439 4790 -810 -436 -827 A O ATOM 2960 N LEU A 347 13.414 -22.190 1.524 1.00 90.53 A N ANISOU 2960 N LEU A 347 13562 12298 8537 272 345 -2777 A N ATOM 2961 CA LEU A 347 12.441 -22.595 2.531 1.00 96.98 A C ANISOU 2961 CA LEU A 347 14412 12995 9440 -338 757 -2931 A C ATOM 2962 C LEU A 347 11.663 -23.836 2.109 1.00 97.13 A C ANISOU 2962 C LEU A 347 14026 13017 9862 -546 694 -3303 A C ATOM 2963 O LEU A 347 11.197 -24.592 2.968 1.00 95.53 A O ANISOU 2963 O LEU A 347 14006 12563 9728 -1218 950 -3315 A O ATOM 2964 CB LEU A 347 11.485 -21.438 2.820 1.00100.55 A C ANISOU 2964 CB LEU A 347 14622 13754 9830 -238 1178 -3188 A C ATOM 2965 CG LEU A 347 12.119 -20.251 3.555 1.00 94.65 A C ANISOU 2965 CG LEU A 347 14343 12923 8697 -185 1304 -2830 A C ATOM 2966 CD1 LEU A 347 11.090 -19.141 3.759 1.00 85.19 A C ANISOU 2966 CD1 LEU A 347 12826 12029 7513 -22 1648 -3196 A C ATOM 2967 CD2 LEU A 347 12.743 -20.684 4.886 1.00 78.00 A C ANISOU 2967 CD2 LEU A 347 12936 10375 6325 -823 1443 -2429 A C ATOM 2968 N GLU A 348 11.512 -24.064 0.804 0.93 98.43 A N ANISOU 2968 N GLU A 348 13683 13444 10273 -11 355 -3606 A N ATOM 2969 CA GLU A 348 10.891 -25.302 0.344 0.93107.60 A C ANISOU 2969 CA GLU A 348 14460 14565 11858 -166 200 -3966 A C ATOM 2970 C GLU A 348 11.671 -26.525 0.810 0.93109.45 A C ANISOU 2970 C GLU A 348 15146 14299 12141 -618 -75 -3675 A C ATOM 2971 O GLU A 348 11.083 -27.597 1.000 0.93112.87 A O ANISOU 2971 O GLU A 348 15481 14521 12884 -1068 -72 -3860 A O ATOM 2972 CB GLU A 348 10.784 -25.291 -1.184 0.93101.42 A C ANISOU 2972 CB GLU A 348 13147 14135 11252 566 -207 -4314 A C ATOM 2973 CG GLU A 348 10.192 -26.554 -1.832 0.93119.41 A C ANISOU 2973 CG GLU A 348 14973 16390 14007 530 -470 -4742 A C ATOM 2974 CD GLU A 348 8.780 -26.897 -1.375 0.93122.30 A C ANISOU 2974 CD GLU A 348 14931 16775 14760 77 -91 -5175 A C ATOM 2975 OE1 GLU A 348 8.024 -27.464 -2.193 0.93120.18 A O ANISOU 2975 OE1 GLU A 348 14086 16656 14919 288 -299 -5685 A O ATOM 2976 OE2 GLU A 348 8.420 -26.619 -0.213 0.93132.76 A O ANISOU 2976 OE2 GLU A 348 16490 17980 15974 -503 424 -5050 A O ATOM 2977 N ARG A 349 12.982 -26.387 1.014 0.88108.64 A N ANISOU 2977 N ARG A 349 15541 13964 11774 -516 -349 -3251 A N ATOM 2978 CA ARG A 349 13.860 -27.525 1.249 0.88108.30 A C ANISOU 2978 CA ARG A 349 15881 13429 11839 -762 -806 -3057 A C ATOM 2979 C ARG A 349 14.255 -27.712 2.710 0.88116.35 A C ANISOU 2979 C ARG A 349 17691 13905 12611 -1428 -703 -2622 A C ATOM 2980 O ARG A 349 14.939 -28.691 3.025 0.88126.21 A O ANISOU 2980 O ARG A 349 19355 14641 13958 -1673 -1159 -2459 A O ATOM 2981 CB ARG A 349 15.126 -27.389 0.392 0.88101.91 A C ANISOU 2981 CB ARG A 349 15024 12709 10988 -165 -1278 -3000 A C ATOM 2982 N VAL A 350 13.856 -26.809 3.605 1.00109.68 A N ANISOU 2982 N VAL A 350 17101 13134 11441 -1706 -173 -2457 A N ATOM 2983 CA VAL A 350 14.089 -27.011 5.035 1.00109.18 A C ANISOU 2983 CA VAL A 350 17849 12566 11067 -2394 -33 -2070 A C ATOM 2984 C VAL A 350 12.793 -27.473 5.697 1.00114.98 A C ANISOU 2984 C VAL A 350 18581 13277 11827 -3119 511 -2237 A C ATOM 2985 O VAL A 350 12.519 -28.670 5.782 1.00116.83 A O ANISOU 2985 O VAL A 350 18935 13172 12282 -3574 347 -2276 A O ATOM 2986 CB VAL A 350 14.626 -25.740 5.732 1.00106.14 A C ANISOU 2986 CB VAL A 350 17851 12230 10248 -2286 190 -1770 A C ATOM 2987 CG1 VAL A 350 15.706 -25.071 4.890 1.00102.03 A C ANISOU 2987 CG1 VAL A 350 17131 11885 9751 -1552 -194 -1705 A C ATOM 2988 CG2 VAL A 350 13.490 -24.768 6.037 1.00103.89 A C ANISOU 2988 CG2 VAL A 350 17267 12386 9822 -2378 891 -1991 A C TER HETATM 2989 P FMN A 401 29.908 -1.125 48.728 1.00 80.16 B P HETATM 2990 O1P FMN A 401 30.328 -0.295 49.919 1.00 66.02 B O HETATM 2991 O2P FMN A 401 30.159 -2.587 48.992 1.00 77.71 B O HETATM 2992 O3P FMN A 401 30.634 -0.685 47.479 1.00 66.14 B O HETATM 2993 C5' FMN A 401 27.812 -1.182 47.198 1.00 62.58 B C HETATM 2994 O5' FMN A 401 28.304 -0.895 48.468 1.00 79.20 B O HETATM 2995 C4' FMN A 401 26.315 -0.898 47.238 1.00 55.44 B C HETATM 2996 O4' FMN A 401 26.105 0.484 47.216 1.00 56.43 B O HETATM 2997 C3' FMN A 401 25.665 -1.580 46.036 1.00 52.72 B C HETATM 2998 O3' FMN A 401 25.606 -2.940 46.371 1.00 47.86 B O HETATM 2999 C2' FMN A 401 24.265 -1.031 45.756 1.00 51.18 B C HETATM 3000 O2' FMN A 401 23.718 -1.606 44.600 1.00 50.49 B O HETATM 3001 C1' FMN A 401 23.375 -1.465 46.892 1.00 48.63 B C HETATM 3002 N1 FMN A 401 23.391 1.112 48.009 1.00 51.27 B N HETATM 3003 C2 FMN A 401 23.458 2.445 48.616 1.00 56.74 B C HETATM 3004 O2 FMN A 401 24.507 2.896 48.926 1.00 59.82 B O HETATM 3005 N3 FMN A 401 22.211 3.215 48.829 1.00 50.59 B N HETATM 3006 C4 FMN A 401 20.926 2.654 48.445 1.00 48.53 B C HETATM 3007 C4A FMN A 401 20.884 1.282 47.815 1.00 47.46 B C HETATM 3008 O4 FMN A 401 19.937 3.283 48.640 1.00 49.76 B O HETATM 3009 C5A FMN A 401 19.624 -0.661 46.796 1.00 49.02 B C HETATM 3010 N5 FMN A 401 19.638 0.686 47.414 1.00 46.03 B N HETATM 3011 C6 FMN A 401 18.393 -1.204 46.413 1.00 44.22 B C HETATM 3012 C7 FMN A 401 18.373 -2.470 45.841 1.00 47.67 B C HETATM 3013 C7M FMN A 401 16.909 -2.766 45.545 1.00 46.58 B C HETATM 3014 C8 FMN A 401 19.558 -3.185 45.646 1.00 47.22 B C HETATM 3015 C8M FMN A 401 19.412 -4.555 45.004 1.00 44.84 B C HETATM 3016 C9 FMN A 401 20.779 -2.644 46.030 1.00 47.73 B C HETATM 3017 C9A FMN A 401 20.814 -1.375 46.604 1.00 46.46 B C HETATM 3018 C10 FMN A 401 22.112 0.546 47.613 1.00 46.06 B C HETATM 3019 N10 FMN A 401 22.107 -0.760 47.022 1.00 44.08 B N HETATM 3020 PA AATP A 402 3.895 -7.915 2.546 0.58 39.31 C P HETATM 3021 PA BATP A 402 3.798 -7.650 2.584 0.42 39.37 C P HETATM 3022 PB AATP A 402 5.886 -9.876 1.598 0.58 39.28 C P HETATM 3023 PB BATP A 402 5.640 -9.691 1.531 0.42 39.25 C P HETATM 3024 PG AATP A 402 7.385 -7.849 0.094 0.58 37.87 C P HETATM 3025 PG BATP A 402 7.142 -7.762 -0.148 0.42 39.30 C P HETATM 3026 C5'AATP A 402 3.474 -9.154 4.837 0.58 41.05 C C HETATM 3027 C5'BATP A 402 3.779 -9.393 4.565 0.42 41.35 C C HETATM 3028 O5'AATP A 402 2.945 -8.582 3.620 0.58 41.65 C O HETATM 3029 O5'BATP A 402 3.159 -8.281 3.884 0.42 42.78 C O HETATM 3030 C4'AATP A 402 2.539 -8.949 6.011 0.58 39.22 C C HETATM 3031 C4'BATP A 402 2.745 -9.988 5.489 0.42 41.52 C C HETATM 3032 O4'AATP A 402 2.355 -7.533 6.171 0.58 37.58 C O HETATM 3033 O4'BATP A 402 2.329 -8.936 6.385 0.42 38.46 C O HETATM 3034 C3'AATP A 402 1.137 -9.432 5.688 0.58 39.51 C C HETATM 3035 C3'BATP A 402 1.504 -10.339 4.666 0.42 40.08 C C HETATM 3036 O3'AATP A 402 1.070 -10.753 6.216 0.58 41.54 C O HETATM 3037 O3'BATP A 402 0.874 -11.446 5.300 0.42 40.98 C O HETATM 3038 C2'AATP A 402 0.281 -8.579 6.616 0.58 38.98 C C HETATM 3039 C2'BATP A 402 0.585 -9.154 4.930 0.42 40.35 C C HETATM 3040 O2'AATP A 402 0.467 -9.042 7.952 0.58 37.38 C O HETATM 3041 O2'BATP A 402 -0.749 -9.654 4.980 0.42 41.34 C O HETATM 3042 C1'AATP A 402 1.037 -7.249 6.607 0.58 40.09 C C HETATM 3043 C1'BATP A 402 0.925 -8.895 6.382 0.42 39.37 C C HETATM 3044 N1 AATP A 402 -1.632 -2.918 5.858 0.58 36.62 C N HETATM 3045 N1 BATP A 402 -1.110 -6.072 10.120 0.42 37.86 C N HETATM 3046 O1AAATP A 402 3.156 -7.025 1.627 0.58 39.45 C O HETATM 3047 O1ABATP A 402 2.809 -6.892 1.791 0.42 42.40 C O HETATM 3048 O1BAATP A 402 6.711 -9.622 2.800 0.58 39.42 C O HETATM 3049 O1BBATP A 402 6.563 -9.493 2.669 0.42 39.01 C O HETATM 3050 O1GAATP A 402 8.769 -8.263 -0.300 0.58 36.44 C O HETATM 3051 O1GBATP A 402 8.421 -8.286 -0.724 0.42 39.27 C O HETATM 3052 C2 AATP A 402 -1.265 -3.557 6.969 0.58 41.75 C C HETATM 3053 C2 BATP A 402 -0.783 -7.364 10.042 0.42 27.87 C C HETATM 3054 O2AAATP A 402 5.075 -7.253 3.279 0.58 35.90 C O HETATM 3055 O2ABATP A 402 5.052 -6.873 2.998 0.42 35.52 C O HETATM 3056 O2BAATP A 402 5.650 -11.327 1.211 0.58 41.87 C O HETATM 3057 O2BBATP A 402 5.304 -11.133 1.174 0.42 41.14 C O HETATM 3058 O2GAATP A 402 7.314 -7.049 1.393 0.58 38.50 C O HETATM 3059 O2GBATP A 402 7.328 -6.993 1.151 0.42 38.00 C O HETATM 3060 N3 AATP A 402 -0.570 -4.690 7.089 0.58 39.36 C N HETATM 3061 N3 BATP A 402 -0.256 -8.035 9.022 0.42 38.52 C N HETATM 3062 O3AAATP A 402 4.481 -9.147 1.730 0.58 42.33 C O HETATM 3063 O3ABATP A 402 4.274 -8.919 1.771 0.42 41.48 C O HETATM 3064 O3BAATP A 402 6.513 -9.140 0.382 0.58 40.56 C O HETATM 3065 O3BBATP A 402 6.181 -8.971 0.244 0.42 38.75 C O HETATM 3066 O3GAATP A 402 6.620 -7.108 -1.004 0.58 38.25 C O HETATM 3067 O3GBATP A 402 6.329 -6.921 -1.129 0.42 38.58 C O HETATM 3068 C4 AATP A 402 -0.248 -5.187 5.891 0.58 40.40 C C HETATM 3069 C4 BATP A 402 -0.048 -7.228 7.982 0.42 41.04 C C HETATM 3070 C5 AATP A 402 -0.563 -4.648 4.655 0.58 46.36 C C HETATM 3071 C5 BATP A 402 -0.327 -5.874 7.909 0.42 39.12 C C HETATM 3072 C6 AATP A 402 -1.309 -3.453 4.659 0.58 48.47 C C HETATM 3073 C6 BATP A 402 -0.892 -5.282 9.053 0.42 37.75 C C HETATM 3074 N6 AATP A 402 -1.688 -2.806 3.552 0.58 50.77 C N HETATM 3075 N6 BATP A 402 -1.219 -3.991 9.145 0.42 43.00 C N HETATM 3076 N7 AATP A 402 -0.080 -5.452 3.630 0.58 44.58 C N HETATM 3077 N7 BATP A 402 0.021 -5.369 6.665 0.42 43.16 C N HETATM 3078 C8 AATP A 402 0.538 -6.419 4.262 0.58 41.49 C C HETATM 3079 C8 BATP A 402 0.498 -6.412 6.031 0.42 40.44 C C HETATM 3080 N9 AATP A 402 0.465 -6.330 5.628 0.58 40.01 C N HETATM 3081 N9 BATP A 402 0.504 -7.563 6.776 0.42 37.32 C N HETATM 3082 MG MG A 403 7.209 -7.599 3.370 1.00 35.90 D MG ATOM 3083 N MET B 1 -16.805 -19.958 45.596 1.00 78.68 D000 N ANISOU 3083 N MET B 1 11789 6426 11679 -920 -3273 -53 D000 N ATOM 3084 CA MET B 1 -16.751 -18.519 45.959 1.00 75.46 D000 C ANISOU 3084 CA MET B 1 11096 6663 10914 -779 -2837 -203 D000 C ATOM 3085 C MET B 1 -16.075 -17.728 44.854 1.00 73.85 D000 C ANISOU 3085 C MET B 1 10797 6798 10464 -700 -2528 42 D000 C ATOM 3086 O MET B 1 -15.232 -18.251 44.127 1.00 71.64 D000 O ANISOU 3086 O MET B 1 10683 6301 10234 -568 -2664 160 D000 O ATOM 3087 CB MET B 1 -15.998 -18.314 47.273 1.00 72.49 D000 C ANISOU 3087 CB MET B 1 10737 6387 10418 -335 -2858 -755 D000 C ATOM 3088 CG MET B 1 -16.455 -17.099 48.065 1.00 82.02 D000 C ANISOU 3088 CG MET B 1 11702 8107 11358 -328 -2560 -901 D000 C ATOM 3089 SD MET B 1 -16.103 -17.117 49.845 1.00 95.84 D000 S ANISOU 3089 SD MET B 1 13515 9940 12961 38 -2666 -1496 D000 S ATOM 3090 CE MET B 1 -15.790 -18.846 50.197 1.00 85.33 D000 C ANISOU 3090 CE MET B 1 12535 7923 11962 198 -3198 -1795 D000 C ATOM 3091 N LYS B 2 -16.444 -16.459 44.748 1.00 68.68 D000 N ANISOU 3091 N LYS B 2 9887 6656 9553 -763 -2153 97 D000 N ATOM 3092 CA LYS B 2 -15.884 -15.547 43.762 1.00 61.36 D000 C ANISOU 3092 CA LYS B 2 8862 6079 8371 -692 -1867 269 D000 C ATOM 3093 C LYS B 2 -15.291 -14.346 44.484 1.00 58.49 D000 C ANISOU 3093 C LYS B 2 8330 6102 7793 -411 -1629 -37 D000 C ATOM 3094 O LYS B 2 -15.794 -13.923 45.529 1.00 58.82 D000 O ANISOU 3094 O LYS B 2 8266 6276 7809 -400 -1574 -241 D000 O ATOM 3095 CB LYS B 2 -16.967 -15.112 42.773 1.00 69.53 D000 C ANISOU 3095 CB LYS B 2 9756 7356 9308 -1061 -1643 658 D000 C ATOM 3096 CG LYS B 2 -16.474 -14.332 41.577 1.00 70.47 D000 C ANISOU 3096 CG LYS B 2 9837 7791 9148 -1010 -1405 843 D000 C ATOM 3097 CD LYS B 2 -17.632 -14.022 40.639 1.00 73.65 D000 C ANISOU 3097 CD LYS B 2 10098 8460 9426 -1353 -1171 1193 D000 C ATOM 3098 CE LYS B 2 -17.152 -13.459 39.313 1.00 80.88 D000 C ANISOU 3098 CE LYS B 2 11050 9654 10028 -1308 -990 1382 D000 C ATOM 3099 NZ LYS B 2 -18.223 -13.476 38.281 1.00 69.03 D000 N ANISOU 3099 NZ LYS B 2 9457 8396 8373 -1644 -782 1763 D000 N ATOM 3100 N ARG B 3 -14.206 -13.802 43.938 1.00 57.21 D000 N ANISOU 3100 N ARG B 3 8143 6111 7481 -200 -1516 -47 D000 N ATOM 3101 CA ARG B 3 -13.616 -12.594 44.500 1.00 50.94 D000 C ANISOU 3101 CA ARG B 3 7174 5679 6503 -0 -1287 -261 D000 C ATOM 3102 C ARG B 3 -13.247 -11.636 43.376 1.00 55.44 D000 C ANISOU 3102 C ARG B 3 7658 6511 6895 -24 -1097 -87 D000 C ATOM 3103 O ARG B 3 -12.552 -12.012 42.425 1.00 56.61 D000 O ANISOU 3103 O ARG B 3 7904 6568 7036 30 -1199 43 D000 O ATOM 3104 CB ARG B 3 -12.389 -12.922 45.363 1.00 53.22 D000 C ANISOU 3104 CB ARG B 3 7481 5916 6825 352 -1385 -583 D000 C ATOM 3105 CG ARG B 3 -11.739 -11.700 46.011 1.00 53.93 D000 C ANISOU 3105 CG ARG B 3 7369 6395 6728 506 -1138 -750 D000 C ATOM 3106 CD ARG B 3 -10.905 -12.097 47.220 1.00 61.42 D000 C ANISOU 3106 CD ARG B 3 8299 7368 7670 810 -1184 -1092 D000 C ATOM 3107 NE ARG B 3 -9.931 -13.121 46.864 1.00 66.41 D000 N ANISOU 3107 NE ARG B 3 9014 7760 8459 1056 -1394 -1189 D000 N ATOM 3108 CZ ARG B 3 -9.774 -14.279 47.493 1.00 71.33 D000 C ANISOU 3108 CZ ARG B 3 9783 8099 9221 1263 -1629 -1441 D000 C ATOM 3109 NH1 ARG B 3 -10.462 -14.579 48.583 1.00 74.62 D000 N ANISOU 3109 NH1 ARG B 3 10284 8464 9606 1256 -1683 -1654 D000 N ATOM 3110 NH2 ARG B 3 -8.898 -15.158 47.016 1.00 71.03 D000 N ANISOU 3110 NH2 ARG B 3 9819 7806 9362 1506 -1851 -1503 D000 N ATOM 3111 N LEU B 4 -13.723 -10.397 43.504 1.00 52.11 D000 N ANISOU 3111 N LEU B 4 7074 6393 6333 -89 -861 -100 D000 N ATOM 3112 CA LEU B 4 -13.534 -9.338 42.526 1.00 52.98 D000 C ANISOU 3112 CA LEU B 4 7110 6747 6272 -109 -692 1 D000 C ATOM 3113 C LEU B 4 -12.698 -8.209 43.113 1.00 50.38 D000 C ANISOU 3113 C LEU B 4 6650 6615 5878 57 -586 -188 D000 C ATOM 3114 O LEU B 4 -12.908 -7.790 44.256 1.00 48.44 D000 O ANISOU 3114 O LEU B 4 6320 6441 5643 90 -523 -322 D000 O ATOM 3115 CB LEU B 4 -14.882 -8.768 42.078 1.00 51.89 D000 C ANISOU 3115 CB LEU B 4 6885 6777 6056 -319 -520 141 D000 C ATOM 3116 CG LEU B 4 -15.324 -9.031 40.643 1.00 69.77 D000 C ANISOU 3116 CG LEU B 4 9213 9099 8197 -479 -471 406 D000 C ATOM 3117 CD1 LEU B 4 -15.351 -10.514 40.340 1.00 78.19 D000 C ANISOU 3117 CD1 LEU B 4 10453 9870 9385 -602 -678 610 D000 C ATOM 3118 CD2 LEU B 4 -16.693 -8.396 40.423 1.00 70.16 D000 C ANISOU 3118 CD2 LEU B 4 9092 9386 8178 -637 -253 477 D000 C ATOM 3119 N THR B 5 -11.766 -7.703 42.315 1.00 46.49 D000 N ANISOU 3119 N THR B 5 6141 6213 5311 134 -584 -172 D000 N ATOM 3120 CA THR B 5 -10.938 -6.560 42.684 1.00 45.48 D000 C ANISOU 3120 CA THR B 5 5870 6259 5151 225 -500 -296 D000 C ATOM 3121 C THR B 5 -11.049 -5.531 41.570 1.00 48.66 D000 C ANISOU 3121 C THR B 5 6270 6786 5432 155 -441 -232 D000 C ATOM 3122 O THR B 5 -10.761 -5.848 40.411 1.00 48.05 D000 O ANISOU 3122 O THR B 5 6291 6693 5272 154 -531 -143 D000 O ATOM 3123 CB THR B 5 -9.471 -6.963 42.877 1.00 49.50 D000 C ANISOU 3123 CB THR B 5 6315 6752 5738 410 -611 -396 D000 C ATOM 3124 CG2 THR B 5 -8.670 -5.792 43.404 1.00 51.72 D000 C ANISOU 3124 CG2 THR B 5 6401 7235 6015 437 -504 -482 D000 C ATOM 3125 OG1 THR B 5 -9.370 -8.059 43.793 1.00 48.85 D000 O ANISOU 3125 OG1 THR B 5 6268 6539 5755 533 -688 -507 D000 O ATOM 3126 N TYR B 6 -11.461 -4.308 41.903 1.00 46.53 D000 N ANISOU 3126 N TYR B 6 5915 6627 5139 113 -320 -287 D000 N ATOM 3127 CA TYR B 6 -11.544 -3.263 40.891 1.00 44.48 D000 C ANISOU 3127 CA TYR B 6 5671 6455 4776 90 -293 -300 D000 C ATOM 3128 C TYR B 6 -11.045 -1.939 41.458 1.00 43.90 D000 C ANISOU 3128 C TYR B 6 5492 6410 4778 98 -280 -394 D000 C ATOM 3129 O TYR B 6 -10.894 -1.766 42.668 1.00 43.46 D000 O ANISOU 3129 O TYR B 6 5348 6354 4811 94 -239 -403 D000 O ATOM 3130 CB TYR B 6 -12.980 -3.116 40.337 1.00 46.98 D000 C ANISOU 3130 CB TYR B 6 6022 6843 4985 21 -171 -250 D000 C ATOM 3131 CG TYR B 6 -13.947 -2.420 41.269 1.00 42.38 D000 C ANISOU 3131 CG TYR B 6 5334 6282 4486 6 -70 -300 D000 C ATOM 3132 CD1 TYR B 6 -14.029 -1.036 41.308 1.00 42.66 D000 C ANISOU 3132 CD1 TYR B 6 5327 6343 4541 57 -49 -405 D000 C ATOM 3133 CD2 TYR B 6 -14.768 -3.150 42.126 1.00 49.05 D000 C ANISOU 3133 CD2 TYR B 6 6135 7091 5410 -53 -47 -247 D000 C ATOM 3134 CE1 TYR B 6 -14.896 -0.392 42.174 1.00 52.06 D000 C ANISOU 3134 CE1 TYR B 6 6433 7525 5823 68 -5 -430 D000 C ATOM 3135 CE2 TYR B 6 -15.647 -2.514 42.989 1.00 46.95 D000 C ANISOU 3135 CE2 TYR B 6 5769 6853 5216 -53 -2 -286 D000 C ATOM 3136 CZ TYR B 6 -15.705 -1.136 43.007 1.00 49.06 D000 C ANISOU 3136 CZ TYR B 6 5996 7150 5496 17 21 -365 D000 C ATOM 3137 OH TYR B 6 -16.562 -0.501 43.874 1.00 49.90 D000 O ANISOU 3137 OH TYR B 6 6015 7258 5687 41 20 -382 D000 O ATOM 3138 N ILE B 7 -10.761 -1.014 40.543 1.00 45.02 D000 N ANISOU 3138 N ILE B 7 5664 6572 4868 100 -335 -456 D000 N ATOM 3139 CA ILE B 7 -10.437 0.370 40.866 1.00 45.77 D000 C ANISOU 3139 CA ILE B 7 5697 6627 5065 71 -368 -530 D000 C ATOM 3140 C ILE B 7 -11.366 1.283 40.079 1.00 49.38 D000 C ANISOU 3140 C ILE B 7 6244 7078 5441 108 -351 -634 D000 C ATOM 3141 O ILE B 7 -11.850 0.933 38.998 1.00 46.31 D000 O ANISOU 3141 O ILE B 7 5950 6781 4865 156 -321 -666 D000 O ATOM 3142 CB ILE B 7 -8.940 0.682 40.582 1.00 46.92 D000 C ANISOU 3142 CB ILE B 7 5769 6763 5297 43 -525 -558 D000 C ATOM 3143 CG1 ILE B 7 -8.667 0.873 39.089 1.00 51.88 D000 C ANISOU 3143 CG1 ILE B 7 6515 7401 5796 79 -676 -650 D000 C ATOM 3144 CG2 ILE B 7 -8.058 -0.403 41.185 1.00 57.75 D000 C ANISOU 3144 CG2 ILE B 7 7022 8192 6728 78 -526 -494 D000 C ATOM 3145 CD1 ILE B 7 -7.345 1.584 38.812 1.00 60.84 D000 C ANISOU 3145 CD1 ILE B 7 7556 8497 7065 19 -885 -712 D000 C ATOM 3146 N SER B 8 -11.634 2.459 40.638 1.00 43.95 D000 N ANISOU 3146 N SER B 8 5528 6290 4883 100 -368 -684 D000 N ATOM 3147 CA SER B 8 -12.483 3.429 39.963 1.00 44.97 D000 C ANISOU 3147 CA SER B 8 5731 6382 4975 196 -378 -842 D000 C ATOM 3148 C SER B 8 -12.055 4.829 40.371 1.00 48.24 D000 C ANISOU 3148 C SER B 8 6154 6576 5599 163 -538 -900 D000 C ATOM 3149 O SER B 8 -11.265 5.014 41.297 1.00 46.99 D000 O ANISOU 3149 O SER B 8 5919 6339 5596 28 -590 -759 D000 O ATOM 3150 CB SER B 8 -13.966 3.204 40.287 1.00 47.36 D000 C ANISOU 3150 CB SER B 8 5983 6769 5244 268 -214 -826 D000 C ATOM 3151 OG SER B 8 -14.222 3.470 41.659 1.00 50.17 D000 O ANISOU 3151 OG SER B 8 6262 7030 5768 226 -218 -722 D000 O ATOM 3152 N LYS B 9 -12.591 5.819 39.662 1.00 50.26 D000 N ANISOU 3152 N LYS B 9 6506 6736 5856 288 -618 -1108 D000 N ATOM 3153 CA LYS B 9 -12.298 7.225 39.896 1.00 50.03 D000 C ANISOU 3153 CA LYS B 9 6534 6413 6063 268 -831 -1187 D000 C ATOM 3154 C LYS B 9 -13.532 7.926 40.449 1.00 53.85 D000 C ANISOU 3154 C LYS B 9 7020 6781 6660 410 -808 -1227 D000 C ATOM 3155 O LYS B 9 -14.654 7.661 40.003 1.00 54.01 D000 O ANISOU 3155 O LYS B 9 7014 6965 6541 599 -661 -1354 D000 O ATOM 3156 CB LYS B 9 -11.854 7.904 38.592 1.00 57.80 D000 C ANISOU 3156 CB LYS B 9 7663 7307 6992 343 -1030 -1467 D000 C ATOM 3157 CG LYS B 9 -11.291 9.305 38.780 1.00 69.92 D000 C ANISOU 3157 CG LYS B 9 9275 8462 8830 262 -1331 -1542 D000 C ATOM 3158 CD LYS B 9 -11.089 10.060 37.456 1.00 83.29 D000 C ANISOU 3158 CD LYS B 9 11153 10032 10461 392 -1571 -1912 D000 C ATOM 3159 CE LYS B 9 -12.300 10.895 37.040 1.00114.69 D000 C ANISOU 3159 CE LYS B 9 15258 13898 14422 702 -1590 -2228 D000 C ATOM 3160 NZ LYS B 9 -12.011 12.359 37.086 1.00109.77 D000 N ANISOU 3160 NZ LYS B 9 14785 12785 14138 699 -1964 -2402 D000 N ATOM 3161 N PHE B 10 -13.327 8.815 41.425 1.00 54.89 D000 N ANISOU 3161 N PHE B 10 7161 6644 7049 314 -959 -1091 D000 N ATOM 3162 CA PHE B 10 -14.413 9.675 41.888 1.00 51.78 D000 C ANISOU 3162 CA PHE B 10 6798 6065 6811 479 -1032 -1138 D000 C ATOM 3163 C PHE B 10 -15.001 10.443 40.704 1.00 58.21 D000 C ANISOU 3163 C PHE B 10 7719 6779 7620 755 -1130 -1523 D000 C ATOM 3164 O PHE B 10 -14.272 11.099 39.956 1.00 57.02 D000 O ANISOU 3164 O PHE B 10 7703 6437 7524 739 -1334 -1706 D000 O ATOM 3165 CB PHE B 10 -13.911 10.684 42.932 1.00 61.98 D000 C ANISOU 3165 CB PHE B 10 8148 7015 8387 307 -1255 -911 D000 C ATOM 3166 CG PHE B 10 -13.580 10.101 44.299 1.00 55.27 D000 C ANISOU 3166 CG PHE B 10 7197 6304 7500 91 -1137 -539 D000 C ATOM 3167 CD1 PHE B 10 -13.357 8.748 44.487 1.00 52.33 D000 C ANISOU 3167 CD1 PHE B 10 6704 6281 6900 31 -898 -462 D000 C ATOM 3168 CD2 PHE B 10 -13.463 10.948 45.397 1.00 63.26 D000 C ANISOU 3168 CD2 PHE B 10 8260 7080 8696 -45 -1291 -269 D000 C ATOM 3169 CE1 PHE B 10 -13.038 8.247 45.746 1.00 53.05 D000 C ANISOU 3169 CE1 PHE B 10 6720 6511 6926 -121 -800 -188 D000 C ATOM 3170 CE2 PHE B 10 -13.146 10.453 46.654 1.00 63.54 D000 C ANISOU 3170 CE2 PHE B 10 8220 7298 8625 -228 -1169 58 D000 C ATOM 3171 CZ PHE B 10 -12.931 9.105 46.828 1.00 61.18 D000 C ANISOU 3171 CZ PHE B 10 7794 7374 8078 -248 -917 67 D000 C ATOM 3172 N ASER B 11 -16.324 10.365 40.533 0.70 58.65 D000 N ANISOU 3172 N ASER B 11 7694 6983 7607 1019 -994 -1671 D000 N ATOM 3173 N BSER B 11 -16.325 10.362 40.539 0.30 58.72 D000 N ANISOU 3173 N BSER B 11 7702 6992 7616 1018 -993 -1669 D000 N ATOM 3174 CA ASER B 11 -16.975 11.198 39.528 0.70 61.15 D000 C ANISOU 3174 CA ASER B 11 8086 7230 7918 1345 -1069 -2075 D000 C ATOM 3175 CA BSER B 11 -16.997 11.192 39.546 0.30 61.20 D000 C ANISOU 3175 CA BSER B 11 8089 7239 7926 1347 -1066 -2072 D000 C ATOM 3176 C ASER B 11 -17.005 12.659 39.951 0.70 61.19 D000 C ANISOU 3176 C ASER B 11 8233 6728 8290 1450 -1417 -2165 D000 C ATOM 3177 C BSER B 11 -17.041 12.653 39.970 0.30 61.39 D000 C ANISOU 3177 C BSER B 11 8253 6757 8316 1455 -1412 -2163 D000 C ATOM 3178 O ASER B 11 -17.116 13.545 39.097 0.70 66.98 D000 O ANISOU 3178 O ASER B 11 9106 7266 9076 1691 -1594 -2544 D000 O ATOM 3179 O BSER B 11 -17.176 13.535 39.114 0.30 67.01 D000 O ANISOU 3179 O BSER B 11 9103 7279 9080 1702 -1585 -2545 D000 O ATOM 3180 CB ASER B 11 -18.400 10.708 39.274 0.70 62.14 D000 C ANISOU 3180 CB ASER B 11 8012 7709 7890 1600 -797 -2193 D000 C ATOM 3181 CB BSER B 11 -18.421 10.687 39.306 0.30 62.20 D000 C ANISOU 3181 CB BSER B 11 8013 7721 7898 1597 -792 -2184 D000 C ATOM 3182 OG ASER B 11 -19.251 11.063 40.351 0.70 67.01 D000 O ANISOU 3182 OG ASER B 11 8510 8196 8754 1687 -859 -2067 D000 O ATOM 3183 OG BSER B 11 -18.429 9.539 38.479 0.30 63.44 D000 O ANISOU 3183 OG BSER B 11 8098 8308 7699 1538 -510 -2181 D000 O ATOM 3184 N AARG B 12 -16.901 12.919 41.249 0.70 64.25 D000 N ANISOU 3184 N AARG B 12 8608 6889 8916 1276 -1537 -1823 D000 N ATOM 3185 N BARG B 12 -16.927 12.922 41.266 0.30 64.34 D000 N ANISOU 3185 N BARG B 12 8617 6901 8930 1280 -1536 -1822 D000 N ATOM 3186 CA AARG B 12 -16.953 14.264 41.799 0.70 71.50 D000 C ANISOU 3186 CA AARG B 12 9678 7283 10206 1330 -1897 -1802 D000 C ATOM 3187 CA BARG B 12 -16.978 14.274 41.802 0.30 71.46 D000 C ANISOU 3187 CA BARG B 12 9671 7277 10204 1337 -1898 -1805 D000 C ATOM 3188 C AARG B 12 -16.277 14.245 43.161 0.70 68.49 D000 C ANISOU 3188 C AARG B 12 9302 6767 9953 962 -1972 -1298 D000 C ATOM 3189 C BARG B 12 -16.350 14.255 43.188 0.30 68.58 D000 C ANISOU 3189 C BARG B 12 9310 6778 9968 978 -1972 -1299 D000 C ATOM 3190 O AARG B 12 -16.056 13.171 43.732 0.70 63.38 D000 O ANISOU 3190 O AARG B 12 8515 6470 9095 768 -1720 -1041 D000 O ATOM 3191 O BARG B 12 -16.223 13.187 43.799 0.30 64.00 D000 O ANISOU 3191 O BARG B 12 8586 6550 9181 800 -1719 -1042 D000 O ATOM 3192 CB AARG B 12 -18.404 14.759 41.922 0.70 72.89 D000 C ANISOU 3192 CB AARG B 12 9781 7406 10509 1739 -1936 -1995 D000 C ATOM 3193 CB BARG B 12 -18.425 14.795 41.859 0.30 72.90 D000 C ANISOU 3193 CB BARG B 12 9787 7401 10511 1758 -1941 -2021 D000 C ATOM 3194 CG AARG B 12 -19.172 14.165 43.102 0.70 77.27 D000 C ANISOU 3194 CG AARG B 12 10147 8161 11051 1702 -1806 -1669 D000 C ATOM 3195 CG BARG B 12 -19.062 14.813 43.246 0.30 79.52 D000 C ANISOU 3195 CG BARG B 12 10535 8177 11502 1725 -1996 -1667 D000 C ATOM 3196 CD AARG B 12 -20.665 14.478 43.014 0.70 85.31 D000 C ANISOU 3196 CD AARG B 12 11002 9240 12170 2138 -1808 -1913 D000 C ATOM 3197 CD BARG B 12 -20.542 15.191 43.168 0.30 82.81 D000 C ANISOU 3197 CD BARG B 12 10808 8618 12038 2181 -2024 -1921 D000 C ATOM 3198 NE AARG B 12 -21.475 13.564 43.813 0.70 88.12 D000 N ANISOU 3198 NE AARG B 12 11107 9949 12426 2101 -1615 -1685 D000 N ATOM 3199 NE BARG B 12 -21.391 14.338 43.995 0.30 87.89 D000 N ANISOU 3199 NE BARG B 12 11200 9610 12584 2168 -1837 -1693 D000 N ATOM 3200 CZ AARG B 12 -21.527 13.568 45.139 0.70 90.62 D000 C ANISOU 3200 CZ AARG B 12 11440 10151 12843 1941 -1758 -1310 D000 C ATOM 3201 CZ BARG B 12 -21.884 13.165 43.618 0.30 87.28 D000 C ANISOU 3201 CZ BARG B 12 10874 10055 12234 2165 -1477 -1749 D000 C ATOM 3202 NH1AARG B 12 -20.824 14.430 45.857 0.70 90.10 D000 N ANISOU 3202 NH1AARG B 12 11616 9646 12970 1780 -2062 -1060 D000 N ATOM 3203 NH1BARG B 12 -21.626 12.656 42.424 0.30 82.06 D000 N ANISOU 3203 NH1BARG B 12 10187 9670 11324 2177 -1231 -1990 D000 N ATOM 3204 NH2AARG B 12 -22.305 12.686 45.761 0.70 88.58 D000 N ANISOU 3204 NH2AARG B 12 10952 10230 12475 1924 -1608 -1171 D000 N ATOM 3205 NH2BARG B 12 -22.660 12.487 44.460 0.30 86.22 D000 N ANISOU 3205 NH2BARG B 12 10525 10159 12075 2131 -1391 -1543 D000 N ATOM 3206 N PRO B 13 -15.920 15.408 43.697 1.00 74.22 D000 N ANISOU 3206 N PRO B 13 10199 6993 11010 856 -2318 -1144 D000 N ATOM 3207 CA PRO B 13 -15.407 15.452 45.071 1.00 72.40 D000 C ANISOU 3207 CA PRO B 13 9969 6686 10853 513 -2363 -618 D000 C ATOM 3208 C PRO B 13 -16.385 14.813 46.047 1.00 77.10 D000 C ANISOU 3208 C PRO B 13 10434 7561 11298 618 -2192 -425 D000 C ATOM 3209 O PRO B 13 -17.579 15.126 46.056 1.00 79.87 D000 O ANISOU 3209 O PRO B 13 10764 7840 11741 953 -2276 -587 D000 O ATOM 3210 CB PRO B 13 -15.235 16.951 45.348 1.00 80.89 D000 C ANISOU 3210 CB PRO B 13 11276 7115 12342 463 -2812 -518 D000 C ATOM 3211 CG PRO B 13 -15.480 17.665 44.048 1.00 85.68 D000 C ANISOU 3211 CG PRO B 13 12016 7430 13109 775 -3025 -1054 D000 C ATOM 3212 CD PRO B 13 -15.663 16.659 42.964 1.00 86.50 D000 C ANISOU 3212 CD PRO B 13 11974 8037 12855 962 -2690 -1429 D000 C ATOM 3213 N LEU B 14 -15.868 13.904 46.867 1.00 74.15 D000 N ANISOU 3213 N LEU B 14 9957 7520 10695 348 -1969 -106 D000 N ATOM 3214 CA LEU B 14 -16.627 13.269 47.935 1.00 65.35 D000 C ANISOU 3214 CA LEU B 14 8749 6664 9415 387 -1852 102 D000 C ATOM 3215 C LEU B 14 -15.973 13.613 49.264 1.00 72.43 D000 C ANISOU 3215 C LEU B 14 9736 7480 10303 76 -1945 590 D000 C ATOM 3216 O LEU B 14 -14.750 13.494 49.407 1.00 69.66 D000 O ANISOU 3216 O LEU B 14 9375 7200 9892 -239 -1855 780 D000 O ATOM 3217 CB LEU B 14 -16.680 11.750 47.756 1.00 61.09 D000 C ANISOU 3217 CB LEU B 14 8025 6629 8557 376 -1501 7 D000 C ATOM 3218 CG LEU B 14 -17.162 11.207 46.414 1.00 59.93 D000 C ANISOU 3218 CG LEU B 14 7777 6659 8335 597 -1342 -390 D000 C ATOM 3219 CD1 LEU B 14 -17.110 9.687 46.418 1.00 63.03 D000 C ANISOU 3219 CD1 LEU B 14 8025 7479 8447 512 -1046 -376 D000 C ATOM 3220 CD2 LEU B 14 -18.572 11.688 46.113 1.00 74.85 D000 C ANISOU 3220 CD2 LEU B 14 9608 8475 10356 952 -1430 -621 D000 C ATOM 3221 N SER B 15 -16.780 14.033 50.232 1.00 66.14 D000 N ANISOU 3221 N SER B 15 9010 6571 9550 165 -2121 803 D000 N ATOM 3222 CA SER B 15 -16.246 14.325 51.551 1.00 73.53 D000 C ANISOU 3222 CA SER B 15 10050 7495 10393 -128 -2191 1307 D000 C ATOM 3223 C SER B 15 -15.999 13.026 52.312 1.00 67.72 D000 C ANISOU 3223 C SER B 15 9184 7307 9240 -252 -1870 1423 D000 C ATOM 3224 O SER B 15 -16.476 11.952 51.940 1.00 59.65 D000 O ANISOU 3224 O SER B 15 8014 6593 8059 -89 -1667 1139 D000 O ATOM 3225 CB SER B 15 -17.199 15.218 52.340 1.00 74.93 D000 C ANISOU 3225 CB SER B 15 10380 7359 10729 24 -2538 1519 D000 C ATOM 3226 OG SER B 15 -18.543 14.817 52.151 1.00 81.22 D000 O ANISOU 3226 OG SER B 15 11055 8278 11527 406 -2553 1223 D000 O ATOM 3227 N GLY B 16 -15.239 13.133 53.399 1.00 66.09 D000 N ANISOU 3227 N GLY B 16 9038 7221 8851 -548 -1829 1847 D000 N ATOM 3228 CA GLY B 16 -15.011 11.965 54.229 1.00 70.84 D000 C ANISOU 3228 CA GLY B 16 9545 8340 9032 -621 -1549 1923 D000 C ATOM 3229 C GLY B 16 -16.306 11.364 54.740 1.00 66.85 D000 C ANISOU 3229 C GLY B 16 9034 7994 8371 -362 -1608 1804 D000 C ATOM 3230 O GLY B 16 -16.444 10.141 54.829 1.00 60.85 D000 O ANISOU 3230 O GLY B 16 8160 7593 7368 -296 -1399 1607 D000 O ATOM 3231 N AASP B 17 -17.285 12.213 55.059 0.53 64.96 D000 N ANISOU 3231 N AASP B 17 8913 7462 8308 -206 -1932 1908 D000 N ATOM 3232 N BASP B 17 -17.273 12.216 55.088 0.47 64.99 D000 N ANISOU 3232 N BASP B 17 8919 7469 8306 -212 -1932 1918 D000 N ATOM 3233 CA AASP B 17 -18.531 11.700 55.620 0.53 67.95 D000 C ANISOU 3233 CA AASP B 17 9251 8002 8566 24 -2038 1820 D000 C ATOM 3234 CA BASP B 17 -18.539 11.710 55.607 0.47 67.96 D000 C ANISOU 3234 CA BASP B 17 9252 7997 8572 26 -2041 1817 D000 C ATOM 3235 C AASP B 17 -19.344 10.946 54.574 0.53 64.84 D000 C ANISOU 3235 C AASP B 17 8639 7694 8302 273 -1931 1352 D000 C ATOM 3236 C BASP B 17 -19.269 10.887 54.555 0.47 64.83 D000 C ANISOU 3236 C BASP B 17 8635 7712 8287 259 -1909 1348 D000 C ATOM 3237 O AASP B 17 -20.044 9.986 54.914 0.53 61.40 D000 O ANISOU 3237 O AASP B 17 8090 7540 7700 362 -1880 1224 D000 O ATOM 3238 O BASP B 17 -19.833 9.830 54.862 0.47 61.03 D000 O ANISOU 3238 O BASP B 17 8039 7535 7613 323 -1819 1214 D000 O ATOM 3239 CB AASP B 17 -19.345 12.842 56.243 0.53 69.49 D000 C ANISOU 3239 CB AASP B 17 9607 7856 8942 147 -2453 2073 D000 C ATOM 3240 CB BASP B 17 -19.419 12.866 56.081 0.47 69.55 D000 C ANISOU 3240 CB BASP B 17 9597 7832 8997 179 -2458 2022 D000 C ATOM 3241 CG AASP B 17 -19.790 13.884 55.231 0.53 73.91 D000 C ANISOU 3241 CG AASP B 17 10174 7922 9985 364 -2685 1884 D000 C ATOM 3242 CG BASP B 17 -18.970 13.434 57.412 0.47 75.18 D000 C ANISOU 3242 CG BASP B 17 10545 8540 9482 -55 -2608 2564 D000 C ATOM 3243 OD1AASP B 17 -18.921 14.548 54.628 0.53 75.99 D000 O ANISOU 3243 OD1AASP B 17 10524 7907 10443 215 -2684 1917 D000 O ATOM 3244 OD1BASP B 17 -18.131 12.797 58.085 0.47 79.60 D000 O ANISOU 3244 OD1BASP B 17 11119 9485 9642 -299 -2350 2739 D000 O ATOM 3245 OD2AASP B 17 -21.018 14.061 55.065 0.53 77.98 D000 O ANISOU 3245 OD2AASP B 17 10600 8333 10696 696 -2890 1687 D000 O ATOM 3246 OD2BASP B 17 -19.466 14.517 57.793 0.47 85.93 D000 O ANISOU 3246 OD2BASP B 17 12077 9523 11050 20 -2987 2819 D000 O ATOM 3247 N GLU B 18 -19.246 11.341 53.300 1.00 61.23 D000 N ANISOU 3247 N GLU B 18 8124 7018 8122 368 -1899 1100 D000 N ATOM 3248 CA GLU B 18 -19.945 10.615 52.245 1.00 66.45 D000 C ANISOU 3248 CA GLU B 18 8573 7825 8848 571 -1745 698 D000 C ATOM 3249 C GLU B 18 -19.318 9.246 52.025 1.00 57.32 D000 C ANISOU 3249 C GLU B 18 7323 7023 7430 417 -1423 596 D000 C ATOM 3250 O GLU B 18 -20.026 8.266 51.766 1.00 58.40 D000 O ANISOU 3250 O GLU B 18 7300 7385 7505 504 -1312 402 D000 O ATOM 3251 CB GLU B 18 -19.933 11.414 50.943 1.00 65.01 D000 C ANISOU 3251 CB GLU B 18 8389 7358 8953 726 -1788 443 D000 C ATOM 3252 CG GLU B 18 -20.659 12.750 51.023 1.00 73.89 D000 C ANISOU 3252 CG GLU B 18 9601 8076 10399 963 -2141 454 D000 C ATOM 3253 CD GLU B 18 -20.597 13.516 49.713 1.00 91.17 D000 C ANISOU 3253 CD GLU B 18 11813 9983 12843 1150 -2193 125 D000 C ATOM 3254 OE1 GLU B 18 -21.489 13.305 48.862 1.00 87.76 D000 O ANISOU 3254 OE1 GLU B 18 11193 9684 12468 1445 -2100 -234 D000 O ATOM 3255 OE2 GLU B 18 -19.647 14.311 49.527 1.00 77.11 D000 O ANISOU 3255 OE2 GLU B 18 10231 7873 11194 992 -2323 219 D000 O ATOM 3256 N ILE B 19 -17.987 9.162 52.114 1.00 57.00 D000 N ANISOU 3256 N ILE B 19 7365 7026 7267 183 -1290 731 D000 N ATOM 3257 CA ILE B 19 -17.315 7.876 51.960 1.00 56.99 D000 C ANISOU 3257 CA ILE B 19 7281 7332 7042 77 -1021 630 D000 C ATOM 3258 C ILE B 19 -17.696 6.944 53.102 1.00 54.44 D000 C ANISOU 3258 C ILE B 19 6952 7283 6452 65 -996 694 D000 C ATOM 3259 O ILE B 19 -17.932 5.747 52.893 1.00 52.28 D000 O ANISOU 3259 O ILE B 19 6585 7199 6079 99 -873 504 D000 O ATOM 3260 CB ILE B 19 -15.790 8.075 51.872 1.00 65.54 D000 C ANISOU 3260 CB ILE B 19 8401 8420 8082 -145 -905 761 D000 C ATOM 3261 CG1 ILE B 19 -15.414 8.718 50.532 1.00 63.02 D000 C ANISOU 3261 CG1 ILE B 19 8077 7855 8012 -126 -944 597 D000 C ATOM 3262 CG2 ILE B 19 -15.054 6.742 52.041 1.00 53.92 D000 C ANISOU 3262 CG2 ILE B 19 6843 7282 6361 -216 -661 690 D000 C ATOM 3263 CD1 ILE B 19 -14.301 9.748 50.642 1.00 71.68 D000 C ANISOU 3263 CD1 ILE B 19 9249 8744 9242 -350 -1039 821 D000 C ATOM 3264 N AGLU B 20 -17.747 7.473 54.328 0.65 56.94 D000 N ANISOU 3264 N AGLU B 20 7390 7608 6636 8 -1140 969 D000 N ATOM 3265 N BGLU B 20 -17.779 7.474 54.322 0.35 57.04 D000 N ANISOU 3265 N BGLU B 20 7401 7618 6652 13 -1144 966 D000 N ATOM 3266 CA AGLU B 20 -18.184 6.670 55.465 0.65 60.29 D000 C ANISOU 3266 CA AGLU B 20 7844 8297 6768 23 -1170 1000 D000 C ATOM 3267 CA BGLU B 20 -18.165 6.641 55.454 0.35 60.26 D000 C ANISOU 3267 CA BGLU B 20 7838 8298 6760 21 -1163 995 D000 C ATOM 3268 C AGLU B 20 -19.596 6.149 55.250 0.65 57.29 D000 C ANISOU 3268 C AGLU B 20 7340 7918 6509 201 -1304 782 D000 C ATOM 3269 C BGLU B 20 -19.619 6.190 55.348 0.35 57.30 D000 C ANISOU 3269 C BGLU B 20 7352 7921 6499 200 -1321 801 D000 C ATOM 3270 O AGLU B 20 -19.900 4.994 55.574 0.65 52.45 D000 O ANISOU 3270 O AGLU B 20 6678 7510 5739 205 -1267 633 D000 O ATOM 3271 O BGLU B 20 -19.968 5.113 55.843 0.35 53.32 D000 O ANISOU 3271 O BGLU B 20 6817 7629 5815 207 -1313 680 D000 O ATOM 3272 CB AGLU B 20 -18.129 7.493 56.755 0.65 58.83 D000 C ANISOU 3272 CB AGLU B 20 7836 8117 6398 -54 -1345 1365 D000 C ATOM 3273 CB BGLU B 20 -17.937 7.395 56.765 0.35 59.65 D000 C ANISOU 3273 CB BGLU B 20 7940 8258 6468 -78 -1301 1365 D000 C ATOM 3274 CG AGLU B 20 -16.889 7.258 57.607 0.65 66.38 D000 C ANISOU 3274 CG AGLU B 20 8875 9361 6987 -251 -1141 1571 D000 C ATOM 3275 CG BGLU B 20 -16.468 7.538 57.182 0.35 64.78 D000 C ANISOU 3275 CG BGLU B 20 8645 9071 6899 -307 -1084 1593 D000 C ATOM 3276 CD AGLU B 20 -16.800 5.840 58.142 0.65 76.12 D000 C ANISOU 3276 CD AGLU B 20 10079 10963 7882 -200 -990 1347 D000 C ATOM 3277 CD BGLU B 20 -15.694 6.230 57.137 0.35 69.28 D000 C ANISOU 3277 CD BGLU B 20 9113 9973 7238 -322 -791 1366 D000 C ATOM 3278 OE1AGLU B 20 -17.701 5.425 58.904 0.65 67.31 D000 O ANISOU 3278 OE1AGLU B 20 9028 9952 6594 -97 -1169 1293 D000 O ATOM 3279 OE1BGLU B 20 -16.093 5.274 57.835 0.35 71.88 D000 O ANISOU 3279 OE1BGLU B 20 9470 10542 7299 -231 -791 1224 D000 O ATOM 3280 OE2AGLU B 20 -15.824 5.137 57.798 0.65 71.85 D000 O ANISOU 3280 OE2AGLU B 20 9449 10584 7265 -247 -728 1206 D000 O ATOM 3281 OE2BGLU B 20 -14.679 6.161 56.411 0.35 70.46 D000 O ANISOU 3281 OE2BGLU B 20 9158 10122 7492 -412 -598 1314 D000 O ATOM 3282 N ALA B 21 -20.478 6.992 54.713 1.00 51.54 D000 N ANISOU 3282 N ALA B 21 6543 6959 6082 352 -1475 749 D000 N ATOM 3283 CA ALA B 21 -21.867 6.579 54.534 1.00 52.79 D000 C ANISOU 3283 CA ALA B 21 6509 7165 6384 517 -1595 565 D000 C ATOM 3284 C ALA B 21 -21.972 5.466 53.500 1.00 50.17 D000 C ANISOU 3284 C ALA B 21 5996 6968 6099 496 -1359 298 D000 C ATOM 3285 O ALA B 21 -22.796 4.555 53.643 1.00 52.06 D000 O ANISOU 3285 O ALA B 21 6089 7355 6336 500 -1394 184 D000 O ATOM 3286 CB ALA B 21 -22.728 7.775 54.132 1.00 63.28 D000 C ANISOU 3286 CB ALA B 21 7764 8240 8038 734 -1807 558 D000 C ATOM 3287 N ILE B 22 -21.136 5.515 52.459 1.00 51.99 D000 N ANISOU 3287 N ILE B 22 6241 7138 6373 450 -1147 219 D000 N ATOM 3288 CA ILE B 22 -21.074 4.413 51.502 1.00 51.34 D000 C ANISOU 3288 CA ILE B 22 6041 7184 6282 401 -931 30 D000 C ATOM 3289 C ILE B 22 -20.666 3.129 52.207 1.00 56.50 D000 C ANISOU 3289 C ILE B 22 6752 8002 6714 269 -882 28 D000 C ATOM 3290 O ILE B 22 -21.242 2.060 51.967 1.00 51.22 D000 O ANISOU 3290 O ILE B 22 5972 7422 6067 234 -856 -90 D000 O ATOM 3291 CB ILE B 22 -20.113 4.753 50.348 1.00 55.19 D000 C ANISOU 3291 CB ILE B 22 6579 7581 6810 380 -764 -33 D000 C ATOM 3292 CG1 ILE B 22 -20.727 5.828 49.445 1.00 56.52 D000 C ANISOU 3292 CG1 ILE B 22 6677 7599 7199 562 -815 -145 D000 C ATOM 3293 CG2 ILE B 22 -19.763 3.490 49.545 1.00 57.03 D000 C ANISOU 3293 CG2 ILE B 22 6760 7951 6957 294 -565 -153 D000 C ATOM 3294 CD1 ILE B 22 -19.721 6.525 48.556 1.00 59.43 D000 C ANISOU 3294 CD1 ILE B 22 7161 7809 7609 548 -763 -198 D000 C ATOM 3295 N GLY B 23 -19.680 3.215 53.101 1.00 51.25 D000 N ANISOU 3295 N GLY B 23 6257 7381 5836 194 -875 155 D000 N ATOM 3296 CA GLY B 23 -19.253 2.035 53.831 1.00 51.21 D000 C ANISOU 3296 CA GLY B 23 6319 7544 5595 131 -834 93 D000 C ATOM 3297 C GLY B 23 -20.316 1.507 54.775 1.00 49.00 D000 C ANISOU 3297 C GLY B 23 6029 7344 5244 159 -1048 48 D000 C ATOM 3298 O GLY B 23 -20.461 0.292 54.938 1.00 51.31 D000 O ANISOU 3298 O GLY B 23 6319 7701 5476 126 -1065 -111 D000 O ATOM 3299 N ARG B 24 -21.055 2.409 55.431 1.00 51.58 D000 N ANISOU 3299 N ARG B 24 6366 7643 5591 222 -1258 186 D000 N ATOM 3300 CA ARG B 24 -22.128 1.984 56.324 1.00 52.74 D000 C ANISOU 3300 CA ARG B 24 6484 7870 5684 254 -1522 143 D000 C ATOM 3301 C ARG B 24 -23.196 1.210 55.565 1.00 56.11 D000 C ANISOU 3301 C ARG B 24 6664 8272 6384 242 -1560 -37 D000 C ATOM 3302 O ARG B 24 -23.603 0.118 55.978 1.00 52.95 D000 O ANISOU 3302 O ARG B 24 6246 7936 5938 174 -1676 -170 D000 O ATOM 3303 CB ARG B 24 -22.773 3.190 57.014 1.00 67.42 D000 C ANISOU 3303 CB ARG B 24 8376 9673 7567 351 -1779 348 D000 C ATOM 3304 CG ARG B 24 -22.040 3.691 58.230 1.00 68.00 D000 C ANISOU 3304 CG ARG B 24 8714 9845 7277 314 -1840 579 D000 C ATOM 3305 CD ARG B 24 -22.965 4.401 59.213 1.00 63.12 D000 C ANISOU 3305 CD ARG B 24 8157 9216 6610 404 -2209 761 D000 C ATOM 3306 NE ARG B 24 -23.734 5.503 58.636 1.00 56.02 D000 N ANISOU 3306 NE ARG B 24 7125 8066 6093 539 -2369 847 D000 N ATOM 3307 CZ ARG B 24 -23.206 6.639 58.197 1.00 64.56 D000 C ANISOU 3307 CZ ARG B 24 8282 8925 7322 551 -2315 1025 D000 C ATOM 3308 NH1 ARG B 24 -21.899 6.837 58.193 1.00 54.89 D000 N ANISOU 3308 NH1 ARG B 24 7222 7710 5923 394 -2085 1166 D000 N ATOM 3309 NH2 ARG B 24 -24.012 7.601 57.756 1.00 62.92 D000 N ANISOU 3309 NH2 ARG B 24 7967 8471 7469 733 -2517 1046 D000 N ATOM 3310 N ILE B 25 -23.701 1.786 54.471 1.00 47.01 D000 N ANISOU 3310 N ILE B 25 5310 7033 5517 304 -1476 -43 D000 N ATOM 3311 CA ILE B 25 -24.759 1.112 53.726 1.00 53.93 D000 C ANISOU 3311 CA ILE B 25 5901 7954 6637 268 -1467 -167 D000 C ATOM 3312 C ILE B 25 -24.223 -0.181 53.132 1.00 49.20 D000 C ANISOU 3312 C ILE B 25 5335 7365 5995 105 -1287 -263 D000 C ATOM 3313 O ILE B 25 -24.916 -1.207 53.111 1.00 50.38 D000 O ANISOU 3313 O ILE B 25 5352 7542 6247 -19 -1370 -334 D000 O ATOM 3314 CB ILE B 25 -25.329 2.039 52.640 1.00 55.42 D000 C ANISOU 3314 CB ILE B 25 5866 8112 7078 408 -1362 -180 D000 C ATOM 3315 CG1 ILE B 25 -26.214 3.113 53.269 1.00 62.77 D000 C ANISOU 3315 CG1 ILE B 25 6700 9005 8143 601 -1631 -118 D000 C ATOM 3316 CG2 ILE B 25 -26.123 1.242 51.613 1.00 57.80 D000 C ANISOU 3316 CG2 ILE B 25 5866 8535 7562 325 -1214 -279 D000 C ATOM 3317 CD1 ILE B 25 -26.343 4.357 52.419 1.00 70.30 D000 C ANISOU 3317 CD1 ILE B 25 7574 9846 9289 816 -1561 -148 D000 C ATOM 3318 N SER B 26 -22.985 -0.150 52.642 1.00 48.87 D000 N ANISOU 3318 N SER B 26 5463 7276 5831 95 -1074 -252 D000 N ATOM 3319 CA ASER B 26 -22.369 -1.349 52.079 0.82 52.73 D000 C ANISOU 3319 CA ASER B 26 6011 7739 6286 -23 -941 -329 D000 C ATOM 3320 CA BSER B 26 -22.403 -1.356 52.073 0.18 52.71 D000 C ANISOU 3320 CA BSER B 26 6003 7737 6288 -24 -943 -329 D000 C ATOM 3321 C SER B 26 -22.271 -2.454 53.121 1.00 52.06 D000 C ANISOU 3321 C SER B 26 6059 7652 6071 -85 -1112 -426 D000 C ATOM 3322 O SER B 26 -22.532 -3.626 52.829 1.00 50.88 D000 O ANISOU 3322 O SER B 26 5881 7432 6020 -204 -1156 -505 D000 O ATOM 3323 CB ASER B 26 -20.973 -1.029 51.537 0.82 49.32 D000 C ANISOU 3323 CB ASER B 26 5727 7270 5740 9 -737 -304 D000 C ATOM 3324 CB BSER B 26 -21.046 -1.043 51.454 0.18 49.58 D000 C ANISOU 3324 CB BSER B 26 5745 7302 5790 6 -734 -306 D000 C ATOM 3325 OG ASER B 26 -21.015 -0.132 50.446 0.82 47.02 D000 O ANISOU 3325 OG ASER B 26 5347 6954 5564 65 -606 -270 D000 O ATOM 3326 OG BSER B 26 -20.396 -2.248 51.117 0.18 51.16 D000 O ANISOU 3326 OG BSER B 26 6027 7462 5949 -70 -669 -378 D000 O ATOM 3327 N SER B 27 -21.871 -2.094 54.345 1.00 52.61 D000 N ANISOU 3327 N SER B 27 6294 7793 5902 -7 -1220 -420 D000 N ATOM 3328 CA ASER B 27 -21.789 -3.073 55.422 0.56 58.27 D000 C ANISOU 3328 CA ASER B 27 7164 8543 6432 -17 -1398 -571 D000 C ATOM 3329 CA BSER B 27 -21.788 -3.076 55.419 0.44 58.26 D000 C ANISOU 3329 CA BSER B 27 7163 8542 6431 -17 -1398 -571 D000 C ATOM 3330 C SER B 27 -23.144 -3.720 55.676 1.00 57.19 D000 C ANISOU 3330 C SER B 27 6892 8362 6477 -112 -1679 -651 D000 C ATOM 3331 O SER B 27 -23.248 -4.945 55.810 1.00 60.07 D000 O ANISOU 3331 O SER B 27 7312 8628 6884 -199 -1810 -813 D000 O ATOM 3332 CB ASER B 27 -21.276 -2.403 56.698 0.56 60.82 D000 C ANISOU 3332 CB ASER B 27 7671 9031 6408 85 -1452 -513 D000 C ATOM 3333 CB BSER B 27 -21.264 -2.410 56.692 0.44 60.83 D000 C ANISOU 3333 CB BSER B 27 7673 9032 6409 85 -1449 -514 D000 C ATOM 3334 OG ASER B 27 -21.067 -3.360 57.718 0.56 72.20 D000 O ANISOU 3334 OG ASER B 27 9287 10550 7594 120 -1593 -713 D000 O ATOM 3335 OG BSER B 27 -20.808 -3.378 57.618 0.44 71.88 D000 O ANISOU 3335 OG BSER B 27 9259 10512 7539 127 -1534 -715 D000 O ATOM 3336 N GLN B 28 -24.198 -2.904 55.754 1.00 53.64 D000 N ANISOU 3336 N GLN B 28 6251 7964 6168 -94 -1806 -544 D000 N ATOM 3337 CA GLN B 28 -25.519 -3.422 56.078 1.00 53.39 D000 C ANISOU 3337 CA GLN B 28 6026 7929 6330 -190 -2103 -607 D000 C ATOM 3338 C GLN B 28 -26.011 -4.402 55.026 1.00 58.07 D000 C ANISOU 3338 C GLN B 28 6412 8421 7233 -391 -2033 -635 D000 C ATOM 3339 O GLN B 28 -26.573 -5.451 55.359 1.00 59.65 D000 O ANISOU 3339 O GLN B 28 6579 8537 7549 -550 -2275 -742 D000 O ATOM 3340 CB GLN B 28 -26.507 -2.265 56.217 1.00 54.06 D000 C ANISOU 3340 CB GLN B 28 5888 8102 6552 -88 -2231 -479 D000 C ATOM 3341 CG GLN B 28 -26.268 -1.404 57.446 1.00 61.92 D000 C ANISOU 3341 CG GLN B 28 7102 9173 7250 66 -2416 -399 D000 C ATOM 3342 CD GLN B 28 -27.007 -0.078 57.387 1.00 67.68 D000 C ANISOU 3342 CD GLN B 28 7653 9914 8147 217 -2517 -238 D000 C ATOM 3343 NE2 GLN B 28 -26.476 0.926 58.079 1.00 65.12 D000 N ANISOU 3343 NE2 GLN B 28 7561 9593 7589 340 -2568 -73 D000 N ATOM 3344 OE1 GLN B 28 -28.045 0.039 56.735 1.00 64.22 D000 O ANISOU 3344 OE1 GLN B 28 6864 9483 8052 228 -2552 -256 D000 O ATOM 3345 N ALYS B 29 -25.821 -4.074 53.747 0.45 51.27 D000 N ANISOU 3345 N ALYS B 29 5418 7562 6500 -402 -1723 -528 D000 N ATOM 3346 N BLYS B 29 -25.822 -4.073 53.748 0.55 51.20 D000 N ANISOU 3346 N BLYS B 29 5410 7554 6491 -402 -1724 -528 D000 N ATOM 3347 CA ALYS B 29 -26.320 -4.937 52.681 0.45 57.81 D000 C ANISOU 3347 CA ALYS B 29 6045 8342 7579 -616 -1625 -485 D000 C ATOM 3348 CA BLYS B 29 -26.319 -4.938 52.682 0.55 57.81 D000 C ANISOU 3348 CA BLYS B 29 6044 8342 7578 -616 -1626 -485 D000 C ATOM 3349 C ALYS B 29 -25.456 -6.184 52.530 0.45 57.72 D000 C ANISOU 3349 C ALYS B 29 6287 8132 7511 -731 -1621 -553 D000 C ATOM 3350 C BLYS B 29 -25.456 -6.186 52.536 0.55 57.74 D000 C ANISOU 3350 C BLYS B 29 6290 8134 7513 -731 -1623 -554 D000 C ATOM 3351 O ALYS B 29 -25.979 -7.294 52.367 0.45 56.34 D000 O ANISOU 3351 O ALYS B 29 6049 7824 7535 -959 -1767 -556 D000 O ATOM 3352 O BLYS B 29 -25.978 -7.298 52.390 0.55 56.30 D000 O ANISOU 3352 O BLYS B 29 6046 7817 7528 -958 -1773 -559 D000 O ATOM 3353 CB ALYS B 29 -26.379 -4.151 51.370 0.45 59.49 D000 C ANISOU 3353 CB ALYS B 29 6065 8671 7868 -559 -1296 -366 D000 C ATOM 3354 CB BLYS B 29 -26.377 -4.152 51.372 0.55 59.49 D000 C ANISOU 3354 CB BLYS B 29 6066 8670 7867 -559 -1296 -366 D000 C ATOM 3355 CG ALYS B 29 -27.403 -3.016 51.398 0.45 60.61 D000 C ANISOU 3355 CG ALYS B 29 5903 8983 8144 -415 -1323 -338 D000 C ATOM 3356 CG BLYS B 29 -27.420 -3.032 51.401 0.55 60.61 D000 C ANISOU 3356 CG BLYS B 29 5898 8983 8146 -418 -1326 -337 D000 C ATOM 3357 CD ALYS B 29 -27.494 -2.282 50.068 0.45 63.06 D000 C ANISOU 3357 CD ALYS B 29 6032 9420 8508 -317 -999 -292 D000 C ATOM 3358 CD BLYS B 29 -27.398 -2.174 50.142 0.55 63.00 D000 C ANISOU 3358 CD BLYS B 29 6056 9401 8481 -291 -1006 -297 D000 C ATOM 3359 CE ALYS B 29 -28.369 -3.028 49.076 0.45 66.17 D000 C ANISOU 3359 CE ALYS B 29 6089 9965 9087 -531 -844 -215 D000 C ATOM 3360 CE BLYS B 29 -28.173 -2.818 49.004 0.55 66.28 D000 C ANISOU 3360 CE BLYS B 29 6151 9973 9060 -478 -809 -225 D000 C ATOM 3361 NZ ALYS B 29 -28.061 -2.645 47.669 0.45 65.05 D000 N ANISOU 3361 NZ ALYS B 29 5907 9950 8857 -466 -482 -183 D000 N ATOM 3362 NZ BLYS B 29 -29.593 -3.093 49.362 0.55 69.04 D000 N ANISOU 3362 NZ BLYS B 29 6090 10465 9676 -592 -980 -205 D000 N ATOM 3363 N ASN B 30 -24.135 -6.027 52.602 1.00 54.11 D000 N ANISOU 3363 N ASN B 30 6106 7637 6815 -578 -1482 -604 D000 N ATOM 3364 CA ASN B 30 -23.244 -7.169 52.421 1.00 56.01 D000 C ANISOU 3364 CA ASN B 30 6574 7685 7024 -620 -1487 -691 D000 C ATOM 3365 C ASN B 30 -23.461 -8.219 53.505 1.00 56.19 D000 C ANISOU 3365 C ASN B 30 6748 7557 7045 -665 -1830 -897 D000 C ATOM 3366 O ASN B 30 -23.459 -9.423 53.225 1.00 57.46 D000 O ANISOU 3366 O ASN B 30 6989 7471 7372 -807 -1964 -949 D000 O ATOM 3367 CB ASN B 30 -21.790 -6.700 52.416 1.00 50.98 D000 C ANISOU 3367 CB ASN B 30 6137 7094 6139 -416 -1285 -726 D000 C ATOM 3368 CG ASN B 30 -21.414 -5.942 51.152 1.00 53.48 D000 C ANISOU 3368 CG ASN B 30 6358 7477 6485 -398 -997 -565 D000 C ATOM 3369 ND2 ASN B 30 -20.158 -5.516 51.080 1.00 50.07 D000 N ANISOU 3369 ND2 ASN B 30 6056 7080 5886 -258 -848 -582 D000 N ATOM 3370 OD1 ASN B 30 -22.236 -5.738 50.255 1.00 50.02 D000 O ANISOU 3370 OD1 ASN B 30 5716 7084 6207 -506 -912 -441 D000 O ATOM 3371 N GLN B 31 -23.654 -7.781 54.753 1.00 55.83 D000 N ANISOU 3371 N GLN B 31 6769 7639 6806 -545 -2007 -1017 D000 N ATOM 3372 CA GLN B 31 -23.906 -8.725 55.836 1.00 56.36 D000 C ANISOU 3372 CA GLN B 31 7002 7589 6823 -563 -2369 -1265 D000 C ATOM 3373 C GLN B 31 -25.069 -9.649 55.503 1.00 63.51 D000 C ANISOU 3373 C GLN B 31 7731 8286 8112 -858 -2634 -1246 D000 C ATOM 3374 O GLN B 31 -25.008 -10.858 55.755 1.00 67.39 D000 O ANISOU 3374 O GLN B 31 8394 8505 8707 -947 -2891 -1430 D000 O ATOM 3375 CB GLN B 31 -24.190 -7.961 57.130 1.00 63.07 D000 C ANISOU 3375 CB GLN B 31 7908 8667 7388 -419 -2536 -1334 D000 C ATOM 3376 CG GLN B 31 -24.326 -8.842 58.360 1.00 83.28 D000 C ANISOU 3376 CG GLN B 31 10697 11164 9783 -381 -2918 -1645 D000 C ATOM 3377 CD GLN B 31 -23.754 -8.188 59.602 1.00 98.37 D000 C ANISOU 3377 CD GLN B 31 12832 13357 11188 -137 -2923 -1736 D000 C ATOM 3378 NE2 GLN B 31 -22.750 -8.823 60.197 1.00113.30 D000 N ANISOU 3378 NE2 GLN B 31 15007 15269 12774 41 -2898 -2005 D000 N ATOM 3379 OE1 GLN B 31 -24.200 -7.114 60.012 1.00 93.25 D000 O ANISOU 3379 OE1 GLN B 31 12097 12917 10417 -99 -2944 -1555 D000 O ATOM 3380 N GLN B 32 -26.147 -9.094 54.943 1.00 61.37 D000 N ANISOU 3380 N GLN B 32 7102 8139 8077 -1014 -2585 -1031 D000 N ATOM 3381 CA GLN B 32 -27.306 -9.912 54.611 1.00 65.29 D000 C ANISOU 3381 CA GLN B 32 7348 8498 8960 -1343 -2807 -962 D000 C ATOM 3382 C GLN B 32 -26.991 -10.911 53.507 1.00 69.31 D000 C ANISOU 3382 C GLN B 32 7899 8754 9680 -1560 -2691 -837 D000 C ATOM 3383 O GLN B 32 -27.573 -12.004 53.480 1.00 70.48 D000 O ANISOU 3383 O GLN B 32 8014 8646 10121 -1851 -2969 -835 D000 O ATOM 3384 CB GLN B 32 -28.473 -9.027 54.179 1.00 75.69 D000 C ANISOU 3384 CB GLN B 32 8206 10080 10471 -1421 -2712 -758 D000 C ATOM 3385 CG GLN B 32 -28.970 -8.084 55.241 1.00 73.10 D000 C ANISOU 3385 CG GLN B 32 7810 9957 10006 -1228 -2911 -838 D000 C ATOM 3386 CD GLN B 32 -30.165 -7.287 54.770 1.00 61.84 D000 C ANISOU 3386 CD GLN B 32 5891 8769 8837 -1266 -2849 -668 D000 C ATOM 3387 NE2 GLN B 32 -29.927 -6.041 54.385 1.00 76.69 D000 N ANISOU 3387 NE2 GLN B 32 7710 10829 10598 -1018 -2567 -575 D000 N ATOM 3388 OE1 GLN B 32 -31.282 -7.796 54.720 1.00 70.58 D000 O ANISOU 3388 OE1 GLN B 32 6655 9891 10270 -1514 -3055 -629 D000 O ATOM 3389 N ALA B 33 -26.094 -10.549 52.590 1.00 67.61 D000 N ANISOU 3389 N ALA B 33 7762 8590 9335 -1442 -2321 -712 D000 N ATOM 3390 CA ALA B 33 -25.762 -11.374 51.439 1.00 67.89 D000 C ANISOU 3390 CA ALA B 33 7848 8421 9525 -1627 -2198 -536 D000 C ATOM 3391 C ALA B 33 -24.565 -12.280 51.687 1.00 72.57 D000 C ANISOU 3391 C ALA B 33 8849 8695 10030 -1493 -2326 -724 D000 C ATOM 3392 O ALA B 33 -24.112 -12.958 50.757 1.00 72.20 D000 O ANISOU 3392 O ALA B 33 8902 8441 10089 -1594 -2258 -575 D000 O ATOM 3393 CB ALA B 33 -25.488 -10.487 50.222 1.00 65.18 D000 C ANISOU 3393 CB ALA B 33 7359 8328 9077 -1561 -1761 -308 D000 C ATOM 3394 N AASN B 34 -24.051 -12.319 52.915 0.46 67.36 D000 N ANISOU 3394 N AASN B 34 8420 8008 9164 -1248 -2515 -1047 D000 N ATOM 3395 N BASN B 34 -24.047 -12.311 52.914 0.54 67.34 D000 N ANISOU 3395 N BASN B 34 8418 8009 9161 -1247 -2513 -1047 D000 N ATOM 3396 CA AASN B 34 -22.861 -13.106 53.233 0.46 66.95 D000 C ANISOU 3396 CA AASN B 34 8721 7714 9002 -1035 -2610 -1293 D000 C ATOM 3397 CA BASN B 34 -22.862 -13.100 53.235 0.54 66.93 D000 C ANISOU 3397 CA BASN B 34 8718 7714 8999 -1034 -2609 -1293 D000 C ATOM 3398 C AASN B 34 -21.715 -12.738 52.296 0.46 66.42 D000 C ANISOU 3398 C AASN B 34 8704 7722 8811 -873 -2259 -1159 D000 C ATOM 3399 C BASN B 34 -21.717 -12.738 52.295 0.54 66.41 D000 C ANISOU 3399 C BASN B 34 8703 7721 8810 -874 -2259 -1159 D000 C ATOM 3400 O AASN B 34 -21.014 -13.601 51.763 0.46 67.82 D000 O ANISOU 3400 O AASN B 34 9058 7620 9092 -847 -2310 -1167 D000 O ATOM 3401 O BASN B 34 -21.023 -13.604 51.758 0.54 67.84 D000 O ANISOU 3401 O BASN B 34 9058 7620 9096 -850 -2311 -1165 D000 O ATOM 3402 CB AASN B 34 -23.158 -14.605 53.172 0.46 70.34 D000 C ANISOU 3402 CB AASN B 34 9306 7661 9760 -1247 -2991 -1367 D000 C ATOM 3403 CB BASN B 34 -23.167 -14.597 53.184 0.54 70.34 D000 C ANISOU 3403 CB BASN B 34 9303 7663 9758 -1247 -2992 -1368 D000 C ATOM 3404 CG AASN B 34 -24.066 -15.067 54.297 0.46 73.75 D000 C ANISOU 3404 CG AASN B 34 9758 7975 10288 -1357 -3424 -1609 D000 C ATOM 3405 CG BASN B 34 -22.176 -15.421 53.986 0.54 74.53 D000 C ANISOU 3405 CG BASN B 34 10205 7942 10172 -949 -3220 -1777 D000 C ATOM 3406 ND2AASN B 34 -24.948 -16.012 53.994 0.46 77.59 D000 N ANISOU 3406 ND2AASN B 34 10178 8119 11182 -1734 -3733 -1498 D000 N ATOM 3407 ND2BASN B 34 -21.985 -16.674 53.585 0.54 75.61 D000 N ANISOU 3407 ND2BASN B 34 10538 7591 10601 -1044 -3481 -1809 D000 N ATOM 3408 OD1AASN B 34 -23.971 -14.586 55.426 0.46 76.11 D000 O ANISOU 3408 OD1AASN B 34 10136 8493 10290 -1124 -3499 -1876 D000 O ATOM 3409 OD1BASN B 34 -21.593 -14.940 54.957 0.54 76.65 D000 O ANISOU 3409 OD1BASN B 34 10581 8456 10086 -628 -3164 -2056 D000 O ATOM 3410 N VAL B 35 -21.540 -11.437 52.081 1.00 59.58 D000 N ANISOU 3410 N VAL B 35 7683 7209 7745 -765 -1942 -1035 D000 N ATOM 3411 CA VAL B 35 -20.455 -10.891 51.278 1.00 60.27 D000 C ANISOU 3411 CA VAL B 35 7794 7408 7696 -611 -1633 -932 D000 C ATOM 3412 C VAL B 35 -19.500 -10.176 52.222 1.00 54.33 D000 C ANISOU 3412 C VAL B 35 7135 6877 6630 -315 -1530 -1124 D000 C ATOM 3413 O VAL B 35 -19.929 -9.568 53.206 1.00 54.38 D000 O ANISOU 3413 O VAL B 35 7109 7068 6485 -267 -1582 -1199 D000 O ATOM 3414 CB VAL B 35 -21.001 -9.934 50.200 1.00 52.84 D000 C ANISOU 3414 CB VAL B 35 6606 6677 6792 -739 -1368 -645 D000 C ATOM 3415 CG1 VAL B 35 -19.892 -9.084 49.616 1.00 52.76 D000 C ANISOU 3415 CG1 VAL B 35 6625 6825 6598 -552 -1094 -598 D000 C ATOM 3416 CG2 VAL B 35 -21.735 -10.726 49.115 1.00 61.29 D000 C ANISOU 3416 CG2 VAL B 35 7583 7591 8113 -1038 -1395 -410 D000 C ATOM 3417 N THR B 36 -18.203 -10.275 51.945 1.00 52.87 D000 N ANISOU 3417 N THR B 36 7052 6689 6345 -125 -1395 -1183 D000 N ATOM 3418 CA THR B 36 -17.196 -9.590 52.742 1.00 48.23 D000 C ANISOU 3418 CA THR B 36 6497 6361 5465 119 -1242 -1315 D000 C ATOM 3419 C THR B 36 -16.253 -8.858 51.801 1.00 53.65 D000 C ANISOU 3419 C THR B 36 7092 7165 6126 170 -975 -1150 D000 C ATOM 3420 O THR B 36 -16.213 -9.130 50.598 1.00 53.38 D000 O ANISOU 3420 O THR B 36 7036 6986 6261 78 -947 -1004 D000 O ATOM 3421 CB THR B 36 -16.397 -10.555 53.625 1.00 55.17 D000 C ANISOU 3421 CB THR B 36 7563 7170 6229 357 -1375 -1651 D000 C ATOM 3422 CG2 THR B 36 -17.271 -11.145 54.702 1.00 60.67 D000 C ANISOU 3422 CG2 THR B 36 8380 7782 6891 332 -1671 -1870 D000 C ATOM 3423 OG1 THR B 36 -15.848 -11.611 52.823 1.00 57.02 D000 O ANISOU 3423 OG1 THR B 36 7886 7096 6682 402 -1469 -1694 D000 O ATOM 3424 N GLY B 37 -15.485 -7.926 52.348 1.00 49.64 D000 N ANISOU 3424 N GLY B 37 6537 6927 5397 298 -796 -1158 D000 N ATOM 3425 CA GLY B 37 -14.549 -7.201 51.515 1.00 53.89 D000 C ANISOU 3425 CA GLY B 37 6976 7562 5937 324 -589 -1021 D000 C ATOM 3426 C GLY B 37 -14.015 -5.959 52.198 1.00 53.93 D000 C ANISOU 3426 C GLY B 37 6901 7852 5737 363 -417 -950 D000 C ATOM 3427 O GLY B 37 -14.233 -5.723 53.388 1.00 50.73 D000 O ANISOU 3427 O GLY B 37 6539 7606 5132 402 -437 -1004 D000 O ATOM 3428 N VAL B 38 -13.310 -5.164 51.396 1.00 51.03 D000 N ANISOU 3428 N VAL B 38 6431 7538 5420 333 -273 -809 D000 N ATOM 3429 CA AVAL B 38 -12.649 -3.959 51.873 0.77 49.05 D000 C ANISOU 3429 CA AVAL B 38 6093 7506 5039 318 -123 -689 D000 C ATOM 3430 CA BVAL B 38 -12.620 -3.967 51.859 0.23 49.36 D000 C ANISOU 3430 CA BVAL B 38 6131 7546 5079 319 -121 -690 D000 C ATOM 3431 C VAL B 38 -12.771 -2.885 50.801 1.00 53.16 D000 C ANISOU 3431 C VAL B 38 6545 7945 5708 196 -86 -511 D000 C ATOM 3432 O VAL B 38 -12.784 -3.172 49.600 1.00 48.75 D000 O ANISOU 3432 O VAL B 38 5982 7251 5291 178 -110 -513 D000 O ATOM 3433 CB AVAL B 38 -11.175 -4.261 52.234 0.77 55.67 D000 C ANISOU 3433 CB AVAL B 38 6845 8534 5774 453 5 -785 D000 C ATOM 3434 CB BVAL B 38 -11.128 -4.240 52.143 0.23 55.79 D000 C ANISOU 3434 CB BVAL B 38 6852 8542 5802 450 8 -779 D000 C ATOM 3435 CG1AVAL B 38 -10.365 -4.526 50.978 0.77 53.89 D000 C ANISOU 3435 CG1AVAL B 38 6538 8199 5741 481 8 -787 D000 C ATOM 3436 CG1BVAL B 38 -10.444 -2.987 52.670 0.23 59.30 D000 C ANISOU 3436 CG1BVAL B 38 7176 9230 6126 364 172 -596 D000 C ATOM 3437 CG2AVAL B 38 -10.583 -3.136 53.053 0.77 59.00 D000 C ANISOU 3437 CG2AVAL B 38 7169 9231 6017 391 166 -629 D000 C ATOM 3438 CG2BVAL B 38 -10.980 -5.389 53.118 0.23 58.44 D000 C ANISOU 3438 CG2BVAL B 38 7268 8952 5984 640 -35 -1036 D000 C ATOM 3439 N LEU B 39 -12.890 -1.638 51.251 1.00 48.06 D000 N ANISOU 3439 N LEU B 39 5873 7374 5014 119 -49 -359 D000 N ATOM 3440 CA LEU B 39 -13.024 -0.478 50.380 1.00 44.52 D000 C ANISOU 3440 CA LEU B 39 5387 6816 4712 33 -53 -233 D000 C ATOM 3441 C LEU B 39 -11.983 0.543 50.805 1.00 49.73 D000 C ANISOU 3441 C LEU B 39 5982 7575 5336 -46 21 -84 D000 C ATOM 3442 O LEU B 39 -11.993 0.998 51.951 1.00 49.28 D000 O ANISOU 3442 O LEU B 39 5947 7643 5134 -85 42 37 D000 O ATOM 3443 CB LEU B 39 -14.432 0.115 50.465 1.00 45.46 D000 C ANISOU 3443 CB LEU B 39 5541 6840 4890 14 -153 -181 D000 C ATOM 3444 CG LEU B 39 -14.695 1.406 49.688 1.00 53.41 D000 C ANISOU 3444 CG LEU B 39 6530 7714 6049 -14 -185 -105 D000 C ATOM 3445 CD1 LEU B 39 -14.428 1.189 48.210 1.00 49.44 D000 C ANISOU 3445 CD1 LEU B 39 6004 7143 5637 -1 -145 -200 D000 C ATOM 3446 CD2 LEU B 39 -16.125 1.907 49.919 1.00 60.54 D000 C ANISOU 3446 CD2 LEU B 39 7428 8551 7024 31 -293 -86 D000 C ATOM 3447 N LEU B 40 -11.079 0.891 49.898 1.00 49.40 D000 N ANISOU 3447 N LEU B 40 5860 7491 5419 -91 45 -73 D000 N ATOM 3448 CA LEU B 40 -10.052 1.883 50.175 1.00 47.44 D000 C ANISOU 3448 CA LEU B 40 5511 7311 5202 -224 92 92 D000 C ATOM 3449 C LEU B 40 -10.240 3.065 49.242 1.00 50.67 D000 C ANISOU 3449 C LEU B 40 5957 7476 5817 -316 -35 148 D000 C ATOM 3450 O LEU B 40 -10.698 2.912 48.109 1.00 49.93 D000 O ANISOU 3450 O LEU B 40 5917 7244 5808 -244 -105 8 D000 O ATOM 3451 CB LEU B 40 -8.651 1.306 49.988 1.00 54.15 D000 C ANISOU 3451 CB LEU B 40 6184 8333 6056 -204 188 33 D000 C ATOM 3452 CG LEU B 40 -8.329 0.149 50.923 1.00 66.96 D000 C ANISOU 3452 CG LEU B 40 7761 10202 7479 -55 310 -84 D000 C ATOM 3453 CD1 LEU B 40 -8.168 -1.095 50.121 1.00 69.45 D000 C ANISOU 3453 CD1 LEU B 40 8084 10439 7865 116 252 -301 D000 C ATOM 3454 CD2 LEU B 40 -7.054 0.447 51.678 1.00 69.91 D000 C ANISOU 3454 CD2 LEU B 40 7911 10886 7766 -118 485 23 D000 C ATOM 3455 N CYS B 41 -9.890 4.249 49.718 1.00 47.90 D000 N ANISOU 3455 N CYS B 41 5594 7073 5535 -477 -72 354 D000 N ATOM 3456 CA CYS B 41 -9.820 5.390 48.825 1.00 51.88 D000 C ANISOU 3456 CA CYS B 41 6137 7303 6271 -563 -234 370 D000 C ATOM 3457 C CYS B 41 -8.520 6.142 49.060 1.00 52.46 D000 C ANISOU 3457 C CYS B 41 6073 7400 6458 -801 -239 568 D000 C ATOM 3458 O CYS B 41 -7.962 6.160 50.161 1.00 54.55 D000 O ANISOU 3458 O CYS B 41 6237 7886 6606 -926 -107 784 D000 O ATOM 3459 CB CYS B 41 -11.022 6.320 48.976 1.00 55.46 D000 C ANISOU 3459 CB CYS B 41 6752 7513 6809 -522 -382 417 D000 C ATOM 3460 SG CYS B 41 -11.133 7.181 50.519 1.00 61.43 D000 S ANISOU 3460 SG CYS B 41 7567 8264 7511 -670 -420 769 D000 S ATOM 3461 N LEU B 42 -8.033 6.737 47.984 1.00 51.08 D000 N ANISOU 3461 N LEU B 42 5884 7025 6498 -871 -394 487 D000 N ATOM 3462 CA LEU B 42 -6.780 7.478 48.027 1.00 54.40 D000 C ANISOU 3462 CA LEU B 42 6140 7429 7099 -1139 -452 664 D000 C ATOM 3463 C LEU B 42 -6.821 8.487 46.898 1.00 55.81 D000 C ANISOU 3463 C LEU B 42 6438 7227 7540 -1190 -740 542 D000 C ATOM 3464 O LEU B 42 -6.889 8.095 45.726 1.00 53.82 D000 O ANISOU 3464 O LEU B 42 6232 6935 7282 -1034 -818 264 D000 O ATOM 3465 CB LEU B 42 -5.585 6.535 47.881 1.00 53.44 D000 C ANISOU 3465 CB LEU B 42 5748 7629 6927 -1139 -310 605 D000 C ATOM 3466 CG LEU B 42 -4.199 7.177 47.974 1.00 61.06 D000 C ANISOU 3466 CG LEU B 42 6438 8668 8093 -1436 -340 798 D000 C ATOM 3467 CD1 LEU B 42 -3.981 7.862 49.319 1.00 68.57 D000 C ANISOU 3467 CD1 LEU B 42 7311 9738 9005 -1693 -210 1181 D000 C ATOM 3468 CD2 LEU B 42 -3.138 6.118 47.724 1.00 64.91 D000 C ANISOU 3468 CD2 LEU B 42 6631 9488 8544 -1342 -219 673 D000 C ATOM 3469 N ASP B 43 -6.798 9.767 47.244 1.00 59.33 D000 N ANISOU 3469 N ASP B 43 6961 7385 8198 -1398 -916 746 D000 N ATOM 3470 CA ASP B 43 -6.681 10.855 46.283 1.00 67.45 D000 C ANISOU 3470 CA ASP B 43 8110 7997 9520 -1474 -1243 622 D000 C ATOM 3471 C ASP B 43 -7.580 10.633 45.067 1.00 67.24 D000 C ANISOU 3471 C ASP B 43 8273 7850 9424 -1146 -1335 211 D000 C ATOM 3472 O ASP B 43 -7.136 10.611 43.921 1.00 63.38 D000 O ANISOU 3472 O ASP B 43 7790 7310 8980 -1108 -1474 -34 D000 O ATOM 3473 CB ASP B 43 -5.231 11.033 45.834 1.00 76.09 D000 C ANISOU 3473 CB ASP B 43 8976 9129 10806 -1740 -1343 665 D000 C ATOM 3474 CG ASP B 43 -5.010 12.344 45.107 1.00 86.87 D000 C ANISOU 3474 CG ASP B 43 10477 10008 12523 -1904 -1741 595 D000 C ATOM 3475 OD1 ASP B 43 -5.618 13.356 45.517 1.00 79.90 D000 O ANISOU 3475 OD1 ASP B 43 9800 8755 11805 -1963 -1913 723 D000 O ATOM 3476 OD2 ASP B 43 -4.253 12.360 44.113 1.00 78.51 D000 O ANISOU 3476 OD2 ASP B 43 9338 8910 11581 -1955 -1923 392 D000 O ATOM 3477 N GLY B 44 -8.868 10.455 45.346 1.00 58.21 D000 N ANISOU 3477 N GLY B 44 7268 6702 8148 -911 -1253 150 D000 N ATOM 3478 CA GLY B 44 -9.863 10.408 44.291 1.00 59.44 D000 C ANISOU 3478 CA GLY B 44 7575 6770 8240 -610 -1308 -202 D000 C ATOM 3479 C GLY B 44 -9.983 9.088 43.574 1.00 54.20 D000 C ANISOU 3479 C GLY B 44 6849 6435 7308 -444 -1110 -389 D000 C ATOM 3480 O GLY B 44 -10.658 9.027 42.536 1.00 52.83 D000 O ANISOU 3480 O GLY B 44 6780 6252 7042 -230 -1133 -665 D000 O ATOM 3481 N ILE B 45 -9.335 8.036 44.081 1.00 53.61 D000 N ANISOU 3481 N ILE B 45 6613 6654 7104 -530 -922 -245 D000 N ATOM 3482 CA ILE B 45 -9.427 6.686 43.542 1.00 49.56 D000 C ANISOU 3482 CA ILE B 45 6059 6403 6369 -389 -766 -366 D000 C ATOM 3483 C ILE B 45 -10.048 5.781 44.593 1.00 49.56 D000 C ANISOU 3483 C ILE B 45 6013 6594 6226 -334 -559 -244 D000 C ATOM 3484 O ILE B 45 -9.686 5.846 45.771 1.00 48.04 D000 O ANISOU 3484 O ILE B 45 5739 6473 6043 -451 -492 -43 D000 O ATOM 3485 CB ILE B 45 -8.041 6.133 43.124 1.00 50.58 D000 C ANISOU 3485 CB ILE B 45 6042 6672 6505 -485 -793 -361 D000 C ATOM 3486 CG1 ILE B 45 -7.343 7.098 42.171 1.00 54.02 D000 C ANISOU 3486 CG1 ILE B 45 6513 6907 7106 -578 -1060 -481 D000 C ATOM 3487 CG2 ILE B 45 -8.189 4.747 42.519 1.00 52.81 D000 C ANISOU 3487 CG2 ILE B 45 6333 7155 6579 -323 -687 -462 D000 C ATOM 3488 CD1 ILE B 45 -8.073 7.261 40.846 1.00 64.82 D000 C ANISOU 3488 CD1 ILE B 45 8092 8187 8350 -382 -1167 -769 D000 C ATOM 3489 N PHE B 46 -10.991 4.944 44.164 1.00 45.25 D000 N ANISOU 3489 N PHE B 46 5520 6142 5532 -172 -465 -362 D000 N ATOM 3490 CA PHE B 46 -11.511 3.850 44.971 1.00 45.48 D000 C ANISOU 3490 CA PHE B 46 5510 6336 5435 -128 -317 -296 D000 C ATOM 3491 C PHE B 46 -10.801 2.556 44.583 1.00 44.27 D000 C ANISOU 3491 C PHE B 46 5306 6328 5185 -104 -258 -333 D000 C ATOM 3492 O PHE B 46 -10.549 2.312 43.401 1.00 46.97 D000 O ANISOU 3492 O PHE B 46 5688 6664 5495 -64 -311 -429 D000 O ATOM 3493 CB PHE B 46 -13.013 3.645 44.752 1.00 43.76 D000 C ANISOU 3493 CB PHE B 46 5344 6119 5166 -3 -275 -374 D000 C ATOM 3494 CG PHE B 46 -13.903 4.631 45.462 1.00 49.28 D000 C ANISOU 3494 CG PHE B 46 6063 6699 5962 31 -340 -326 D000 C ATOM 3495 CD1 PHE B 46 -13.914 4.727 46.842 1.00 51.49 D000 C ANISOU 3495 CD1 PHE B 46 6330 6999 6235 -36 -348 -153 D000 C ATOM 3496 CD2 PHE B 46 -14.775 5.422 44.733 1.00 46.87 D000 C ANISOU 3496 CD2 PHE B 46 5795 6282 5732 163 -402 -467 D000 C ATOM 3497 CE1 PHE B 46 -14.765 5.616 47.480 1.00 50.51 D000 C ANISOU 3497 CE1 PHE B 46 6244 6750 6199 9 -455 -80 D000 C ATOM 3498 CE2 PHE B 46 -15.630 6.310 45.362 1.00 54.15 D000 C ANISOU 3498 CE2 PHE B 46 6727 7068 6780 242 -502 -434 D000 C ATOM 3499 CZ PHE B 46 -15.623 6.407 46.738 1.00 52.24 D000 C ANISOU 3499 CZ PHE B 46 6486 6812 6550 156 -547 -221 D000 C ATOM 3500 N PHE B 47 -10.510 1.720 45.577 1.00 44.20 D000 N ANISOU 3500 N PHE B 47 5231 6447 5118 -103 -170 -270 D000 N ATOM 3501 CA PHE B 47 -10.095 0.338 45.368 1.00 46.18 D000 C ANISOU 3501 CA PHE B 47 5462 6782 5301 -23 -142 -329 D000 C ATOM 3502 C PHE B 47 -11.030 -0.537 46.195 1.00 46.96 D000 C ANISOU 3502 C PHE B 47 5613 6909 5321 29 -86 -338 D000 C ATOM 3503 O PHE B 47 -11.241 -0.248 47.376 1.00 47.59 D000 O ANISOU 3503 O PHE B 47 5674 7052 5357 8 -44 -288 D000 O ATOM 3504 CB PHE B 47 -8.650 0.056 45.821 1.00 46.77 D000 C ANISOU 3504 CB PHE B 47 5378 6987 5404 -23 -118 -315 D000 C ATOM 3505 CG PHE B 47 -7.638 1.105 45.424 1.00 54.32 D000 C ANISOU 3505 CG PHE B 47 6216 7938 6485 -142 -186 -265 D000 C ATOM 3506 CD1 PHE B 47 -7.635 2.357 46.021 1.00 50.05 D000 C ANISOU 3506 CD1 PHE B 47 5645 7357 6015 -296 -183 -138 D000 C ATOM 3507 CD2 PHE B 47 -6.636 0.804 44.514 1.00 57.54 D000 C ANISOU 3507 CD2 PHE B 47 6536 8366 6960 -114 -291 -326 D000 C ATOM 3508 CE1 PHE B 47 -6.701 3.307 45.675 1.00 51.42 D000 C ANISOU 3508 CE1 PHE B 47 5707 7481 6350 -452 -284 -77 D000 C ATOM 3509 CE2 PHE B 47 -5.690 1.751 44.162 1.00 56.10 D000 C ANISOU 3509 CE2 PHE B 47 6220 8171 6924 -252 -397 -290 D000 C ATOM 3510 CZ PHE B 47 -5.718 3.003 44.746 1.00 50.71 D000 C ANISOU 3510 CZ PHE B 47 5506 7424 6338 -438 -391 -166 D000 C ATOM 3511 N GLN B 48 -11.578 -1.602 45.607 1.00 46.21 D000 N ANISOU 3511 N GLN B 48 5592 6764 5203 76 -111 -384 D000 N ATOM 3512 CA GLN B 48 -12.453 -2.481 46.373 1.00 47.15 D000 C ANISOU 3512 CA GLN B 48 5755 6869 5291 92 -111 -405 D000 C ATOM 3513 C GLN B 48 -12.200 -3.946 46.049 1.00 48.93 D000 C ANISOU 3513 C GLN B 48 6044 7015 5533 147 -180 -453 D000 C ATOM 3514 O GLN B 48 -11.910 -4.305 44.902 1.00 45.89 D000 O ANISOU 3514 O GLN B 48 5701 6569 5165 148 -225 -418 D000 O ATOM 3515 CB GLN B 48 -13.929 -2.160 46.123 1.00 50.55 D000 C ANISOU 3515 CB GLN B 48 6201 7265 5741 35 -106 -370 D000 C ATOM 3516 CG GLN B 48 -14.886 -2.974 46.999 1.00 48.80 D000 C ANISOU 3516 CG GLN B 48 5992 7025 5524 15 -154 -389 D000 C ATOM 3517 CD GLN B 48 -16.299 -2.420 46.980 1.00 46.97 D000 C ANISOU 3517 CD GLN B 48 5691 6812 5342 -31 -153 -352 D000 C ATOM 3518 NE2 GLN B 48 -16.904 -2.282 48.155 1.00 48.17 D000 N ANISOU 3518 NE2 GLN B 48 5824 6991 5488 -28 -223 -360 D000 N ATOM 3519 OE1 GLN B 48 -16.843 -2.138 45.914 1.00 49.69 D000 O ANISOU 3519 OE1 GLN B 48 5990 7175 5715 -51 -94 -326 D000 O ATOM 3520 N ILE B 49 -12.297 -4.780 47.084 1.00 48.98 D000 N ANISOU 3520 N ILE B 49 6081 7005 5524 205 -217 -538 D000 N ATOM 3521 CA ILE B 49 -12.307 -6.235 46.965 1.00 47.57 D000 C ANISOU 3521 CA ILE B 49 6003 6664 5408 259 -342 -603 D000 C ATOM 3522 C ILE B 49 -13.623 -6.734 47.545 1.00 49.41 D000 C ANISOU 3522 C ILE B 49 6298 6808 5669 168 -416 -616 D000 C ATOM 3523 O ILE B 49 -13.988 -6.357 48.666 1.00 48.22 D000 O ANISOU 3523 O ILE B 49 6124 6757 5440 181 -402 -682 D000 O ATOM 3524 CB ILE B 49 -11.121 -6.887 47.694 1.00 52.25 D000 C ANISOU 3524 CB ILE B 49 6575 7291 5985 458 -370 -772 D000 C ATOM 3525 CG1 ILE B 49 -9.794 -6.399 47.114 1.00 46.29 D000 C ANISOU 3525 CG1 ILE B 49 5690 6651 5247 532 -316 -751 D000 C ATOM 3526 CG2 ILE B 49 -11.185 -8.397 47.558 1.00 53.24 D000 C ANISOU 3526 CG2 ILE B 49 6843 7162 6224 543 -561 -864 D000 C ATOM 3527 CD1 ILE B 49 -8.605 -6.608 48.047 1.00 54.81 D000 C ANISOU 3527 CD1 ILE B 49 6631 7910 6283 726 -251 -911 D000 C ATOM 3528 N LEU B 50 -14.323 -7.582 46.791 1.00 45.59 D000 N ANISOU 3528 N LEU B 50 5885 6145 5291 56 -512 -529 D000 N ATOM 3529 CA LEU B 50 -15.578 -8.189 47.229 1.00 46.84 D000 C ANISOU 3529 CA LEU B 50 6067 6193 5536 -81 -621 -521 D000 C ATOM 3530 C LEU B 50 -15.505 -9.701 47.066 1.00 56.73 D000 C ANISOU 3530 C LEU B 50 7472 7149 6935 -102 -831 -542 D000 C ATOM 3531 O LEU B 50 -15.029 -10.192 46.038 1.00 52.01 D000 O ANISOU 3531 O LEU B 50 6946 6429 6385 -112 -866 -420 D000 O ATOM 3532 CB LEU B 50 -16.763 -7.672 46.416 1.00 52.91 D000 C ANISOU 3532 CB LEU B 50 6722 7043 6338 -271 -527 -336 D000 C ATOM 3533 CG LEU B 50 -17.114 -6.187 46.447 1.00 60.00 D000 C ANISOU 3533 CG LEU B 50 7479 8164 7152 -244 -369 -321 D000 C ATOM 3534 CD1 LEU B 50 -17.905 -5.840 45.189 1.00 61.05 D000 C ANISOU 3534 CD1 LEU B 50 7514 8392 7291 -354 -244 -175 D000 C ATOM 3535 CD2 LEU B 50 -17.909 -5.840 47.684 1.00 60.75 D000 C ANISOU 3535 CD2 LEU B 50 7507 8315 7260 -245 -436 -393 D000 C ATOM 3536 N GLU B 51 -16.009 -10.440 48.057 1.00 54.10 D000 N ANISOU 3536 N GLU B 51 7208 6671 6676 -113 -1013 -691 D000 N ATOM 3537 CA GLU B 51 -15.945 -11.897 48.009 1.00 52.19 D000 C ANISOU 3537 CA GLU B 51 7144 6064 6620 -125 -1278 -746 D000 C ATOM 3538 C GLU B 51 -17.218 -12.506 48.582 1.00 59.72 D000 C ANISOU 3538 C GLU B 51 8117 6849 7726 -337 -1483 -765 D000 C ATOM 3539 O GLU B 51 -17.786 -12.002 49.556 1.00 55.14 D000 O ANISOU 3539 O GLU B 51 7460 6432 7059 -334 -1484 -893 D000 O ATOM 3540 CB GLU B 51 -14.703 -12.432 48.751 1.00 65.22 D000 C ANISOU 3540 CB GLU B 51 8913 7642 8227 205 -1373 -1050 D000 C ATOM 3541 CG GLU B 51 -14.649 -12.092 50.224 1.00 61.17 D000 C ANISOU 3541 CG GLU B 51 8383 7329 7531 368 -1350 -1336 D000 C ATOM 3542 CD GLU B 51 -13.283 -12.327 50.855 1.00 68.58 D000 C ANISOU 3542 CD GLU B 51 9349 8363 8344 726 -1315 -1622 D000 C ATOM 3543 OE1 GLU B 51 -12.385 -12.898 50.193 1.00 65.22 D000 O ANISOU 3543 OE1 GLU B 51 8957 7784 8039 876 -1370 -1637 D000 O ATOM 3544 OE2 GLU B 51 -13.110 -11.935 52.028 1.00 61.49 D000 O ANISOU 3544 OE2 GLU B 51 8425 7726 7214 866 -1232 -1826 D000 O ATOM 3545 N GLY B 52 -17.666 -13.576 47.941 1.00 60.07 D000 N ANISOU 3545 N GLY B 52 8258 6560 8006 -545 -1681 -606 D000 N ATOM 3546 CA GLY B 52 -18.863 -14.282 48.349 1.00 63.23 D000 C ANISOU 3546 CA GLY B 52 8657 6745 8623 -813 -1923 -586 D000 C ATOM 3547 C GLY B 52 -19.307 -15.198 47.226 1.00 65.76 D000 C ANISOU 3547 C GLY B 52 9031 6769 9185 -1127 -2039 -244 D000 C ATOM 3548 O GLY B 52 -18.585 -15.411 46.253 1.00 62.48 D000 O ANISOU 3548 O GLY B 52 8718 6277 8743 -1080 -1982 -66 D000 O ATOM 3549 N AGLU B 53 -20.519 -15.727 47.385 0.44 68.04 D000 N ANISOU 3549 N AGLU B 53 9240 6907 9706 -1468 -2219 -128 D000 N ATOM 3550 N BGLU B 53 -20.509 -15.745 47.385 0.56 68.01 D000 N ANISOU 3550 N BGLU B 53 9240 6896 9705 -1467 -2224 -129 D000 N ATOM 3551 CA AGLU B 53 -21.110 -16.568 46.354 0.44 70.70 D000 C ANISOU 3551 CA AGLU B 53 9586 6998 10279 -1858 -2312 275 D000 C ATOM 3552 CA BGLU B 53 -21.049 -16.612 46.346 0.56 70.67 D000 C ANISOU 3552 CA BGLU B 53 9600 6973 10277 -1847 -2322 271 D000 C ATOM 3553 C AGLU B 53 -21.195 -15.805 45.036 0.44 73.08 D000 C ANISOU 3553 C AGLU B 53 9712 7678 10378 -1961 -1917 638 D000 C ATOM 3554 C BGLU B 53 -21.199 -15.830 45.045 0.56 73.07 D000 C ANISOU 3554 C BGLU B 53 9715 7666 10383 -1964 -1925 638 D000 C ATOM 3555 O AGLU B 53 -21.592 -14.637 45.002 0.44 69.73 D000 O ANISOU 3555 O AGLU B 53 9029 7703 9762 -1912 -1611 622 D000 O ATOM 3556 O BGLU B 53 -21.642 -14.678 45.036 0.56 69.70 D000 O ANISOU 3556 O BGLU B 53 9022 7686 9773 -1926 -1625 622 D000 O ATOM 3557 CB AGLU B 53 -22.500 -17.036 46.791 0.44 75.62 D000 C ANISOU 3557 CB AGLU B 53 10044 7503 11185 -2250 -2521 355 D000 C ATOM 3558 CB BGLU B 53 -22.390 -17.208 46.772 0.56 75.63 D000 C ANISOU 3558 CB BGLU B 53 10097 7429 11211 -2244 -2566 352 D000 C ATOM 3559 CG AGLU B 53 -22.572 -17.521 48.241 0.44 77.45 D000 C ANISOU 3559 CG AGLU B 53 10416 7469 11542 -2122 -2906 -84 D000 C ATOM 3560 CG BGLU B 53 -22.267 -18.415 47.705 0.56 70.98 D000 C ANISOU 3560 CG BGLU B 53 9794 6276 10901 -2224 -3079 63 D000 C ATOM 3561 CD AGLU B 53 -22.983 -16.423 49.212 0.44 75.90 D000 C ANISOU 3561 CD AGLU B 53 10007 7700 11133 -1959 -2773 -336 D000 C ATOM 3562 CD BGLU B 53 -21.483 -19.567 47.097 0.56 73.94 D000 C ANISOU 3562 CD BGLU B 53 10513 6117 11463 -2208 -3335 178 D000 C ATOM 3563 OE1AGLU B 53 -22.180 -15.483 49.424 0.44 64.68 D000 O ANISOU 3563 OE1AGLU B 53 8597 6590 9389 -1605 -2513 -495 D000 O ATOM 3564 OE1BGLU B 53 -20.235 -19.518 47.124 0.56 83.62 D000 O ANISOU 3564 OE1BGLU B 53 11939 7308 12525 -1785 -3303 -38 D000 O ATOM 3565 OE2AGLU B 53 -24.100 -16.508 49.766 0.44 77.98 D000 O ANISOU 3565 OE2AGLU B 53 10088 7973 11568 -2200 -2958 -356 D000 O ATOM 3566 OE2BGLU B 53 -22.112 -20.524 46.597 0.56 83.84 D000 O ANISOU 3566 OE2BGLU B 53 11825 6980 13051 -2625 -3587 501 D000 O ATOM 3567 N ALA B 54 -20.810 -16.472 43.942 1.00 77.04 D000 N ANISOU 3567 N ALA B 54 10379 7982 10910 -2084 -1951 956 D000 N ATOM 3568 CA ALA B 54 -20.761 -15.799 42.646 1.00 81.27 D000 C ANISOU 3568 CA ALA B 54 10808 8892 11178 -2141 -1597 1267 D000 C ATOM 3569 C ALA B 54 -22.077 -15.113 42.303 1.00 79.82 D000 C ANISOU 3569 C ALA B 54 10249 9142 10938 -2417 -1297 1463 D000 C ATOM 3570 O ALA B 54 -22.084 -13.989 41.788 1.00 71.82 D000 O ANISOU 3570 O ALA B 54 9065 8579 9643 -2282 -951 1454 D000 O ATOM 3571 CB ALA B 54 -20.394 -16.808 41.555 1.00 87.24 D000 C ANISOU 3571 CB ALA B 54 11812 9346 11988 -2320 -1743 1656 D000 C ATOM 3572 N GLU B 55 -23.203 -15.777 42.574 1.00 86.87 D000 N ANISOU 3572 N GLU B 55 10990 9900 12118 -2796 -1443 1622 D000 N ATOM 3573 CA GLU B 55 -24.504 -15.185 42.279 1.00 91.82 D000 C ANISOU 3573 CA GLU B 55 11185 10969 12733 -3053 -1162 1801 D000 C ATOM 3574 C GLU B 55 -24.677 -13.848 42.988 1.00 81.37 D000 C ANISOU 3574 C GLU B 55 9632 10022 11264 -2737 -976 1445 D000 C ATOM 3575 O GLU B 55 -25.176 -12.882 42.399 1.00 79.27 D000 O ANISOU 3575 O GLU B 55 9083 10226 10809 -2700 -621 1510 D000 O ATOM 3576 CB GLU B 55 -25.622 -16.146 42.690 1.00104.25 D000 C ANISOU 3576 CB GLU B 55 12603 12296 14712 -3510 -1428 1976 D000 C ATOM 3577 CG GLU B 55 -25.765 -17.377 41.803 1.00133.22 D000 C ANISOU 3577 CG GLU B 55 16416 15647 18553 -3950 -1565 2470 D000 C ATOM 3578 CD GLU B 55 -24.644 -18.384 41.996 1.00147.86 D000 C ANISOU 3578 CD GLU B 55 18783 16859 20537 -3812 -1977 2390 D000 C ATOM 3579 OE1 GLU B 55 -24.025 -18.393 43.083 1.00105.88 D000 O ANISOU 3579 OE1 GLU B 55 13654 11289 15287 -3466 -2229 1918 D000 O ATOM 3580 OE2 GLU B 55 -24.385 -19.169 41.059 1.00165.70 D000 O ANISOU 3580 OE2 GLU B 55 21257 18883 22821 -4035 -2051 2803 D000 O ATOM 3581 N LYS B 56 -24.268 -13.775 44.257 1.00 77.78 D000 N ANISOU 3581 N LYS B 56 9308 9365 10879 -2493 -1221 1065 D000 N ATOM 3582 CA ALYS B 56 -24.437 -12.544 45.022 0.66 77.45 D000 C ANISOU 3582 CA ALYS B 56 9085 9634 10708 -2220 -1097 777 D000 C ATOM 3583 CA BLYS B 56 -24.440 -12.542 45.018 0.34 77.46 D000 C ANISOU 3583 CA BLYS B 56 9086 9637 10709 -2221 -1096 778 D000 C ATOM 3584 C LYS B 56 -23.460 -11.468 44.561 1.00 75.06 D000 C ANISOU 3584 C LYS B 56 8873 9567 10081 -1874 -824 678 D000 C ATOM 3585 O LYS B 56 -23.829 -10.295 44.446 1.00 64.98 D000 O ANISOU 3585 O LYS B 56 7375 8642 8674 -1743 -589 622 D000 O ATOM 3586 CB ALYS B 56 -24.257 -12.831 46.514 0.66 75.91 D000 C ANISOU 3586 CB ALYS B 56 9037 9185 10618 -2081 -1441 435 D000 C ATOM 3587 CB BLYS B 56 -24.270 -12.826 46.511 0.34 75.97 D000 C ANISOU 3587 CB BLYS B 56 9041 9197 10627 -2083 -1440 436 D000 C ATOM 3588 CG ALYS B 56 -25.162 -13.935 47.068 0.66 78.44 D000 C ANISOU 3588 CG ALYS B 56 9313 9206 11286 -2416 -1805 465 D000 C ATOM 3589 CG BLYS B 56 -25.572 -13.122 47.251 0.34 80.00 D000 C ANISOU 3589 CG BLYS B 56 9303 9688 11404 -2339 -1667 418 D000 C ATOM 3590 CD ALYS B 56 -26.622 -13.496 47.131 0.66 82.02 D000 C ANISOU 3590 CD ALYS B 56 9310 9961 11894 -2660 -1742 587 D000 C ATOM 3591 CD BLYS B 56 -26.389 -14.205 46.556 0.34 81.90 D000 C ANISOU 3591 CD BLYS B 56 9423 9747 11949 -2818 -1772 761 D000 C ATOM 3592 CE ALYS B 56 -27.415 -14.295 48.165 0.66 86.99 D000 C ANISOU 3592 CE ALYS B 56 9894 10320 12840 -2889 -2189 460 D000 C ATOM 3593 CE BLYS B 56 -27.542 -14.700 47.426 0.34 86.81 D000 C ANISOU 3593 CE BLYS B 56 9832 10250 12902 -3098 -2112 702 D000 C ATOM 3594 NZ ALYS B 56 -28.457 -13.470 48.847 0.66 81.06 D000 N ANISOU 3594 NZ ALYS B 56 8764 9900 12134 -2870 -2206 355 D000 N ATOM 3595 NZ BLYS B 56 -27.115 -15.084 48.803 0.34 83.72 D000 N ANISOU 3595 NZ BLYS B 56 9737 9539 12534 -2895 -2525 288 D000 N ATOM 3596 N ILE B 57 -22.210 -11.851 44.290 1.00 69.37 D000 N ANISOU 3596 N ILE B 57 8465 8635 9258 -1718 -886 645 D000 N ATOM 3597 CA ILE B 57 -21.198 -10.884 43.864 1.00 70.53 D000 C ANISOU 3597 CA ILE B 57 8690 8975 9135 -1420 -680 548 D000 C ATOM 3598 C ILE B 57 -21.601 -10.232 42.546 1.00 64.80 D000 C ANISOU 3598 C ILE B 57 7806 8587 8227 -1494 -368 763 D000 C ATOM 3599 O ILE B 57 -21.501 -9.011 42.379 1.00 62.29 D000 O ANISOU 3599 O ILE B 57 7386 8545 7738 -1296 -166 639 D000 O ATOM 3600 CB ILE B 57 -19.821 -11.569 43.750 1.00 67.88 D000 C ANISOU 3600 CB ILE B 57 8668 8352 8769 -1261 -840 494 D000 C ATOM 3601 CG1 ILE B 57 -19.393 -12.147 45.101 1.00 67.46 D000 C ANISOU 3601 CG1 ILE B 57 8759 8026 8849 -1115 -1114 205 D000 C ATOM 3602 CG2 ILE B 57 -18.767 -10.602 43.228 1.00 70.83 D000 C ANISOU 3602 CG2 ILE B 57 9083 8929 8898 -1002 -657 419 D000 C ATOM 3603 CD1 ILE B 57 -19.276 -11.109 46.206 1.00 66.73 D000 C ANISOU 3603 CD1 ILE B 57 8570 8155 8631 -895 -1038 -68 D000 C ATOM 3604 N ASP B 58 -22.040 -11.041 41.582 1.00 67.26 D000 N ANISOU 3604 N ASP B 58 8116 8880 8559 -1778 -334 1090 D000 N ATOM 3605 CA ASP B 58 -22.400 -10.492 40.279 1.00 77.50 D000 C ANISOU 3605 CA ASP B 58 9282 10559 9605 -1836 -12 1290 D000 C ATOM 3606 C ASP B 58 -23.488 -9.429 40.414 1.00 75.93 D000 C ANISOU 3606 C ASP B 58 8707 10754 9389 -1793 230 1182 D000 C ATOM 3607 O ASP B 58 -23.394 -8.359 39.799 1.00 70.47 D000 O ANISOU 3607 O ASP B 58 7947 10372 8457 -1585 470 1076 D000 O ATOM 3608 CB ASP B 58 -22.831 -11.625 39.345 1.00 79.22 D000 C ANISOU 3608 CB ASP B 58 9541 10718 9843 -2208 -14 1721 D000 C ATOM 3609 CG ASP B 58 -21.644 -12.411 38.789 1.00 72.70 D000 C ANISOU 3609 CG ASP B 58 9107 9577 8938 -2170 -210 1861 D000 C ATOM 3610 OD1 ASP B 58 -20.519 -12.266 39.317 1.00 73.15 D000 O ANISOU 3610 OD1 ASP B 58 9368 9421 9005 -1869 -382 1591 D000 O ATOM 3611 OD2 ASP B 58 -21.839 -13.189 37.834 1.00 79.85 D000 O ANISOU 3611 OD2 ASP B 58 10102 10460 9777 -2444 -200 2260 D000 O ATOM 3612 N AARG B 59 -24.523 -9.695 41.215 0.57 73.16 D000 N ANISOU 3612 N AARG B 59 8110 10379 9308 -1965 135 1180 D000 N ATOM 3613 N BARG B 59 -24.509 -9.695 41.236 0.43 73.16 D000 N ANISOU 3613 N BARG B 59 8114 10374 9310 -1962 130 1175 D000 N ATOM 3614 CA AARG B 59 -25.591 -8.711 41.385 0.57 70.74 D000 C ANISOU 3614 CA AARG B 59 7410 10439 9030 -1892 324 1071 D000 C ATOM 3615 CA BARG B 59 -25.601 -8.742 41.412 0.43 70.79 D000 C ANISOU 3615 CA BARG B 59 7417 10436 9046 -1899 315 1073 D000 C ATOM 3616 C AARG B 59 -25.059 -7.441 42.035 0.57 70.08 D000 C ANISOU 3616 C AARG B 59 7385 10382 8859 -1495 312 728 D000 C ATOM 3617 C BARG B 59 -25.112 -7.456 42.071 0.43 70.09 D000 C ANISOU 3617 C BARG B 59 7374 10384 8873 -1503 307 730 D000 C ATOM 3618 O AARG B 59 -25.309 -6.332 41.551 0.57 71.06 D000 O ANISOU 3618 O AARG B 59 7354 10804 8841 -1290 537 620 D000 O ATOM 3619 O BARG B 59 -25.475 -6.353 41.645 0.43 70.77 D000 O ANISOU 3619 O BARG B 59 7273 10778 8840 -1308 529 623 D000 O ATOM 3620 CB AARG B 59 -26.737 -9.299 42.212 0.57 78.40 D000 C ANISOU 3620 CB AARG B 59 8099 11346 10342 -2156 145 1129 D000 C ATOM 3621 CB BARG B 59 -26.718 -9.366 42.253 0.43 78.38 D000 C ANISOU 3621 CB BARG B 59 8111 11318 10352 -2168 125 1131 D000 C ATOM 3622 CG AARG B 59 -27.842 -8.297 42.609 0.57 83.15 D000 C ANISOU 3622 CG AARG B 59 8265 12289 11039 -2034 255 981 D000 C ATOM 3623 CG BARG B 59 -27.405 -10.592 41.654 0.43 78.14 D000 C ANISOU 3623 CG BARG B 59 7961 11248 10480 -2640 116 1518 D000 C ATOM 3624 CD AARG B 59 -28.124 -7.235 41.540 0.57 85.21 D000 C ANISOU 3624 CD AARG B 59 8311 13010 11054 -1832 657 957 D000 C ATOM 3625 CD BARG B 59 -28.109 -10.324 40.326 0.43 81.01 D000 C ANISOU 3625 CD BARG B 59 8020 12110 10651 -2780 539 1787 D000 C ATOM 3626 NE AARG B 59 -29.406 -6.563 41.740 0.57 97.54 D000 N ANISOU 3626 NE AARG B 59 9369 14917 12773 -1771 768 878 D000 N ATOM 3627 NE BARG B 59 -27.821 -11.378 39.358 0.43 83.92 D000 N ANISOU 3627 NE BARG B 59 8589 12369 10926 -3105 570 2191 D000 N ATOM 3628 CZ AARG B 59 -29.980 -5.766 40.848 0.57101.17 D000 C ANISOU 3628 CZ AARG B 59 9528 15832 13080 -1610 1121 840 D000 C ATOM 3629 CZ BARG B 59 -26.723 -11.444 38.614 0.43 74.15 D000 C ANISOU 3629 CZ BARG B 59 7740 11043 9393 -2968 607 2249 D000 C ATOM 3630 NH1AARG B 59 -29.405 -5.501 39.686 0.57 93.27 D000 N ANISOU 3630 NH1AARG B 59 8704 15010 11724 -1504 1397 866 D000 N ATOM 3631 NH1BARG B 59 -25.832 -10.467 38.606 0.43 77.60 D000 N ANISOU 3631 NH1BARG B 59 8363 11535 9587 -2538 666 1931 D000 N ATOM 3632 NH2AARG B 59 -31.157 -5.215 41.132 0.57107.05 D000 N ANISOU 3632 NH2AARG B 59 9778 16872 14024 -1525 1181 746 D000 N ATOM 3633 NH2BARG B 59 -26.520 -12.515 37.852 0.43 77.47 D000 N ANISOU 3633 NH2BARG B 59 8362 11298 9775 -3289 553 2658 D000 N ATOM 3634 N ILE B 60 -24.317 -7.579 43.136 1.00 67.45 D000 N ANISOU 3634 N ILE B 60 7283 9740 8604 -1380 47 555 D000 N ATOM 3635 CA ILE B 60 -23.808 -6.391 43.821 1.00 67.11 D000 C ANISOU 3635 CA ILE B 60 7298 9719 8481 -1061 30 300 D000 C ATOM 3636 C ILE B 60 -22.916 -5.580 42.888 1.00 61.59 D000 C ANISOU 3636 C ILE B 60 6738 9126 7539 -862 215 251 D000 C ATOM 3637 O ILE B 60 -23.007 -4.348 42.835 1.00 61.14 D000 O ANISOU 3637 O ILE B 60 6595 9216 7419 -648 315 107 D000 O ATOM 3638 CB ILE B 60 -23.072 -6.789 45.116 1.00 64.48 D000 C ANISOU 3638 CB ILE B 60 7195 9097 8205 -993 -246 154 D000 C ATOM 3639 CG1 ILE B 60 -24.082 -7.178 46.205 1.00 69.61 D000 C ANISOU 3639 CG1 ILE B 60 7690 9695 9064 -1115 -466 111 D000 C ATOM 3640 CG2 ILE B 60 -22.206 -5.650 45.634 1.00 60.89 D000 C ANISOU 3640 CG2 ILE B 60 6860 8664 7611 -710 -228 -24 D000 C ATOM 3641 CD1 ILE B 60 -23.716 -8.428 46.968 1.00 69.28 D000 C ANISOU 3641 CD1 ILE B 60 7868 9335 9121 -1226 -753 57 D000 C ATOM 3642 N TYR B 61 -22.044 -6.252 42.135 1.00 66.87 D000 N ANISOU 3642 N TYR B 61 7633 9690 8085 -922 220 363 D000 N ATOM 3643 CA TYR B 61 -21.162 -5.532 41.219 1.00 59.77 D000 C ANISOU 3643 CA TYR B 61 6871 8886 6951 -747 343 306 D000 C ATOM 3644 C TYR B 61 -21.966 -4.728 40.201 1.00 63.12 D000 C ANISOU 3644 C TYR B 61 7099 9662 7222 -695 607 303 D000 C ATOM 3645 O TYR B 61 -21.652 -3.562 39.937 1.00 56.11 D000 O ANISOU 3645 O TYR B 61 6230 8865 6223 -463 673 110 D000 O ATOM 3646 CB TYR B 61 -20.222 -6.520 40.525 1.00 66.27 D000 C ANISOU 3646 CB TYR B 61 7947 9554 7678 -833 264 462 D000 C ATOM 3647 CG TYR B 61 -19.126 -5.878 39.700 1.00 67.58 D000 C ANISOU 3647 CG TYR B 61 8279 9779 7620 -654 302 384 D000 C ATOM 3648 CD1 TYR B 61 -18.171 -5.067 40.293 1.00 59.34 D000 C ANISOU 3648 CD1 TYR B 61 7303 8644 6599 -452 216 170 D000 C ATOM 3649 CD2 TYR B 61 -19.035 -6.104 38.335 1.00 63.90 D000 C ANISOU 3649 CD2 TYR B 61 7901 9469 6911 -712 404 544 D000 C ATOM 3650 CE1 TYR B 61 -17.156 -4.484 39.547 1.00 62.49 D000 C ANISOU 3650 CE1 TYR B 61 7827 9078 6837 -321 205 95 D000 C ATOM 3651 CE2 TYR B 61 -18.022 -5.525 37.576 1.00 71.54 D000 C ANISOU 3651 CE2 TYR B 61 9029 10486 7669 -548 382 448 D000 C ATOM 3652 CZ TYR B 61 -17.087 -4.715 38.192 1.00 71.13 D000 C ANISOU 3652 CZ TYR B 61 9017 10312 7699 -359 268 213 D000 C ATOM 3653 OH TYR B 61 -16.077 -4.132 37.456 1.00 68.94 D000 O ANISOU 3653 OH TYR B 61 8869 10067 7258 -229 204 113 D000 O ATOM 3654 N GLU B 62 -23.025 -5.319 39.641 1.00 64.99 D000 N ANISOU 3654 N GLU B 62 7130 10103 7458 -907 756 503 D000 N ATOM 3655 CA GLU B 62 -23.830 -4.599 38.655 1.00 63.21 D000 C ANISOU 3655 CA GLU B 62 6677 10292 7048 -827 1055 476 D000 C ATOM 3656 C GLU B 62 -24.426 -3.332 39.258 1.00 64.71 D000 C ANISOU 3656 C GLU B 62 6644 10580 7362 -563 1079 196 D000 C ATOM 3657 O GLU B 62 -24.477 -2.287 38.598 1.00 64.72 D000 O ANISOU 3657 O GLU B 62 6608 10786 7198 -312 1231 -0 D000 O ATOM 3658 CB GLU B 62 -24.932 -5.506 38.106 1.00 72.79 D000 C ANISOU 3658 CB GLU B 62 7635 11750 8270 -1145 1232 780 D000 C ATOM 3659 N AARG B 63 -24.861 -3.400 40.515 0.50 65.40 D000 N ANISOU 3659 N AARG B 63 6609 10501 7739 -595 891 161 D000 N ATOM 3660 N BARG B 63 -24.899 -3.410 40.507 0.50 65.42 D000 N ANISOU 3660 N BARG B 63 6602 10512 7744 -599 896 165 D000 N ATOM 3661 CA AARG B 63 -25.417 -2.223 41.178 0.50 66.90 D000 C ANISOU 3661 CA AARG B 63 6613 10735 8069 -338 848 -64 D000 C ATOM 3662 CA BARG B 63 -25.413 -2.223 41.184 0.50 66.89 D000 C ANISOU 3662 CA BARG B 63 6614 10733 8070 -338 847 -65 D000 C ATOM 3663 C AARG B 63 -24.338 -1.178 41.439 0.50 62.20 D000 C ANISOU 3663 C AARG B 63 6297 9927 7408 -79 728 -266 D000 C ATOM 3664 C BARG B 63 -24.314 -1.181 41.356 0.50 62.20 D000 C ANISOU 3664 C BARG B 63 6304 9937 7394 -79 740 -265 D000 C ATOM 3665 O AARG B 63 -24.591 0.027 41.319 0.50 60.03 D000 O ANISOU 3665 O AARG B 63 5947 9715 7147 186 758 -465 D000 O ATOM 3666 O BARG B 63 -24.525 0.012 41.112 0.50 60.08 D000 O ANISOU 3666 O BARG B 63 5969 9746 7113 187 789 -467 D000 O ATOM 3667 CB AARG B 63 -26.097 -2.655 42.480 0.50 68.25 D000 C ANISOU 3667 CB AARG B 63 6623 10780 8528 -462 626 -19 D000 C ATOM 3668 CB BARG B 63 -25.993 -2.587 42.556 0.50 68.23 D000 C ANISOU 3668 CB BARG B 63 6651 10749 8523 -441 606 -35 D000 C ATOM 3669 CG AARG B 63 -26.333 -1.556 43.501 0.50 68.89 D000 C ANISOU 3669 CG AARG B 63 6645 10774 8755 -207 450 -207 D000 C ATOM 3670 CG BARG B 63 -27.098 -3.641 42.583 0.50 74.23 D000 C ANISOU 3670 CG BARG B 63 7107 11643 9453 -750 625 163 D000 C ATOM 3671 CD AARG B 63 -27.269 -0.484 42.982 0.50 69.79 D000 C ANISOU 3671 CD AARG B 63 6444 11159 8913 49 607 -357 D000 C ATOM 3672 CD BARG B 63 -28.076 -3.364 43.737 0.50 78.07 D000 C ANISOU 3672 CD BARG B 63 7314 12130 10219 -713 419 83 D000 C ATOM 3673 NE AARG B 63 -26.561 0.777 42.798 0.50 70.69 D000 N ANISOU 3673 NE AARG B 63 6773 11149 8936 358 585 -559 D000 N ATOM 3674 NE BARG B 63 -27.375 -3.026 44.973 0.50 75.37 D000 N ANISOU 3674 NE BARG B 63 7252 11485 9902 -575 127 -43 D000 N ATOM 3675 CZ AARG B 63 -26.981 1.771 42.030 0.50 71.65 D000 C ANISOU 3675 CZ AARG B 63 6757 11448 9021 641 732 -758 D000 C ATOM 3676 CZ BARG B 63 -26.701 -3.891 45.721 0.50 67.53 D000 C ANISOU 3676 CZ BARG B 63 6532 10219 8907 -723 -87 -6 D000 C ATOM 3677 NH1AARG B 63 -28.110 1.685 41.343 0.50 78.94 D000 N ANISOU 3677 NH1AARG B 63 7288 12754 9951 685 970 -789 D000 N ATOM 3678 NH1BARG B 63 -26.728 -5.190 45.472 0.50 76.33 D000 N ANISOU 3678 NH1BARG B 63 7683 11244 10076 -1020 -119 147 D000 N ATOM 3679 NH2AARG B 63 -26.253 2.880 41.952 0.50 73.35 D000 N ANISOU 3679 NH2AARG B 63 7218 11453 9197 888 635 -941 D000 N ATOM 3680 NH2BARG B 63 -25.982 -3.441 46.744 0.50 70.22 D000 N ANISOU 3680 NH2BARG B 63 7119 10374 9188 -564 -277 -123 D000 N ATOM 3681 N ILE B 64 -23.131 -1.617 41.799 1.00 55.85 D000 N ANISOU 3681 N ILE B 64 5800 8862 6559 -152 578 -218 D000 N ATOM 3682 CA ILE B 64 -22.031 -0.680 42.001 1.00 53.28 D000 C ANISOU 3682 CA ILE B 64 5702 8357 6185 30 476 -362 D000 C ATOM 3683 C ILE B 64 -21.666 0.008 40.690 1.00 59.24 D000 C ANISOU 3683 C ILE B 64 6536 9238 6736 172 613 -481 D000 C ATOM 3684 O ILE B 64 -21.276 1.183 40.686 1.00 54.24 D000 O ANISOU 3684 O ILE B 64 5983 8508 6119 369 544 -661 D000 O ATOM 3685 CB ILE B 64 -20.816 -1.406 42.613 1.00 55.50 D000 C ANISOU 3685 CB ILE B 64 6224 8406 6458 -79 323 -285 D000 C ATOM 3686 CG1 ILE B 64 -21.063 -1.748 44.088 1.00 61.99 D000 C ANISOU 3686 CG1 ILE B 64 7017 9102 7435 -134 153 -262 D000 C ATOM 3687 CG2 ILE B 64 -19.561 -0.556 42.480 1.00 57.99 D000 C ANISOU 3687 CG2 ILE B 64 6730 8603 6701 48 264 -387 D000 C ATOM 3688 CD1 ILE B 64 -20.165 -2.880 44.619 1.00 57.21 D000 C ANISOU 3688 CD1 ILE B 64 6594 8331 6813 -244 37 -206 D000 C ATOM 3689 N LEU B 65 -21.776 -0.704 39.560 1.00 55.05 D000 N ANISOU 3689 N LEU B 65 6007 8910 6000 66 782 -377 D000 N ATOM 3690 CA LEU B 65 -21.461 -0.093 38.270 1.00 59.41 D000 C ANISOU 3690 CA LEU B 65 6658 9630 6286 214 903 -512 D000 C ATOM 3691 C LEU B 65 -22.405 1.049 37.939 1.00 66.14 D000 C ANISOU 3691 C LEU B 65 7310 10684 7134 473 1033 -757 D000 C ATOM 3692 O LEU B 65 -22.049 1.938 37.159 1.00 62.83 D000 O ANISOU 3692 O LEU B 65 7013 10307 6552 686 1046 -991 D000 O ATOM 3693 CB LEU B 65 -21.520 -1.123 37.139 1.00 65.79 D000 C ANISOU 3693 CB LEU B 65 7507 10670 6819 37 1069 -302 D000 C ATOM 3694 CG LEU B 65 -20.540 -2.290 37.222 1.00 71.72 D000 C ANISOU 3694 CG LEU B 65 8488 11202 7562 -172 911 -70 D000 C ATOM 3695 CD1 LEU B 65 -20.859 -3.326 36.163 1.00 72.92 D000 C ANISOU 3695 CD1 LEU B 65 8662 11570 7475 -377 1060 210 D000 C ATOM 3696 CD2 LEU B 65 -19.121 -1.787 37.073 1.00 73.22 D000 C ANISOU 3696 CD2 LEU B 65 8935 11199 7685 -42 727 -209 D000 C ATOM 3697 N ALA B 66 -23.615 1.027 38.492 1.00 59.61 D000 N ANISOU 3697 N ALA B 66 6170 9984 6496 478 1105 -734 D000 N ATOM 3698 CA ALA B 66 -24.603 2.055 38.217 1.00 58.37 D000 C ANISOU 3698 CA ALA B 66 5765 10035 6378 770 1223 -983 D000 C ATOM 3699 C ALA B 66 -24.492 3.265 39.139 1.00 59.72 D000 C ANISOU 3699 C ALA B 66 5985 9887 6817 1013 968 -1185 D000 C ATOM 3700 O ALA B 66 -25.195 4.257 38.908 1.00 61.36 D000 O ANISOU 3700 O ALA B 66 6035 10186 7094 1323 1002 -1440 D000 O ATOM 3701 CB ALA B 66 -26.012 1.461 38.329 1.00 66.77 D000 C ANISOU 3701 CB ALA B 66 6398 11424 7548 664 1413 -851 D000 C ATOM 3702 N ASP B 67 -23.629 3.212 40.157 1.00 54.82 D000 N ANISOU 3702 N ASP B 67 5581 8908 6342 891 715 -1072 D000 N ATOM 3703 CA ASP B 67 -23.518 4.295 41.130 1.00 57.61 D000 C ANISOU 3703 CA ASP B 67 5998 8955 6937 1057 462 -1168 D000 C ATOM 3704 C ASP B 67 -22.901 5.521 40.472 1.00 61.72 D000 C ANISOU 3704 C ASP B 67 6722 9308 7420 1291 378 -1425 D000 C ATOM 3705 O ASP B 67 -21.786 5.459 39.949 1.00 57.96 D000 O ANISOU 3705 O ASP B 67 6491 8740 6790 1201 348 -1431 D000 O ATOM 3706 CB ASP B 67 -22.681 3.853 42.328 1.00 52.75 D000 C ANISOU 3706 CB ASP B 67 5559 8078 6406 840 266 -956 D000 C ATOM 3707 CG ASP B 67 -22.927 4.706 43.571 1.00 55.99 D000 C ANISOU 3707 CG ASP B 67 5967 8259 7048 945 24 -941 D000 C ATOM 3708 OD1 ASP B 67 -22.707 5.931 43.505 1.00 55.96 D000 O ANISOU 3708 OD1 ASP B 67 6070 8049 7141 1138 -109 -1074 D000 O ATOM 3709 OD2 ASP B 67 -23.317 4.152 44.622 1.00 56.19 D000 O ANISOU 3709 OD2 ASP B 67 5911 8286 7152 828 -66 -789 D000 O ATOM 3710 N AGLU B 68 -23.620 6.642 40.502 0.65 63.42 D000 N ANISOU 3710 N AGLU B 68 6834 9458 7803 1602 298 -1652 D000 N ATOM 3711 N BGLU B 68 -23.625 6.642 40.510 0.35 63.55 D000 N ANISOU 3711 N BGLU B 68 6850 9475 7821 1602 297 -1651 D000 N ATOM 3712 CA AGLU B 68 -23.142 7.841 39.828 0.65 68.54 D000 C ANISOU 3712 CA AGLU B 68 7687 9904 8449 1850 175 -1949 D000 C ATOM 3713 CA BGLU B 68 -23.169 7.865 39.863 0.35 68.59 D000 C ANISOU 3713 CA BGLU B 68 7689 9905 8468 1856 169 -1950 D000 C ATOM 3714 C AGLU B 68 -21.935 8.475 40.512 0.65 64.63 D000 C ANISOU 3714 C AGLU B 68 7499 8945 8112 1730 -135 -1856 D000 C ATOM 3715 C BGLU B 68 -21.914 8.449 40.497 0.35 64.72 D000 C ANISOU 3715 C BGLU B 68 7512 8961 8117 1723 -131 -1853 D000 C ATOM 3716 O AGLU B 68 -21.358 9.413 39.951 0.65 67.23 D000 O ANISOU 3716 O AGLU B 68 8033 9044 8467 1862 -290 -2079 D000 O ATOM 3717 O BGLU B 68 -21.290 9.327 39.890 0.35 66.99 D000 O ANISOU 3717 O BGLU B 68 8009 9034 8410 1842 -274 -2071 D000 O ATOM 3718 CB AGLU B 68 -24.282 8.862 39.721 0.65 73.66 D000 C ANISOU 3718 CB AGLU B 68 8138 10566 9281 2261 138 -2244 D000 C ATOM 3719 CB BGLU B 68 -24.284 8.916 39.892 0.35 73.97 D000 C ANISOU 3719 CB BGLU B 68 8182 10561 9364 2256 102 -2222 D000 C ATOM 3720 CG AGLU B 68 -24.695 9.485 41.050 0.65 80.72 D000 C ANISOU 3720 CG AGLU B 68 8984 11142 10545 2336 -152 -2131 D000 C ATOM 3721 CG BGLU B 68 -24.725 9.318 41.298 0.35 80.55 D000 C ANISOU 3721 CG BGLU B 68 8941 11123 10541 2278 -160 -2055 D000 C ATOM 3722 CD AGLU B 68 -26.162 9.886 41.089 0.65 88.16 D000 C ANISOU 3722 CD AGLU B 68 9559 12270 11667 2686 -114 -2317 D000 C ATOM 3723 CD BGLU B 68 -24.414 10.769 41.625 0.35 82.40 D000 C ANISOU 3723 CD BGLU B 68 9404 10861 11045 2506 -518 -2201 D000 C ATOM 3724 OE1AGLU B 68 -26.956 9.353 40.284 0.65 86.89 D000 O ANISOU 3724 OE1AGLU B 68 9093 12585 11338 2771 213 -2438 D000 O ATOM 3725 OE1BGLU B 68 -23.327 11.251 41.239 0.35 80.61 D000 O ANISOU 3725 OE1BGLU B 68 9487 10363 10778 2436 -644 -2267 D000 O ATOM 3726 OE2AGLU B 68 -26.521 10.734 41.933 0.65 96.07 D000 O ANISOU 3726 OE2AGLU B 68 10563 12957 12984 2875 -416 -2321 D000 O ATOM 3727 OE2BGLU B 68 -25.257 11.426 42.270 0.35 85.29 D000 O ANISOU 3727 OE2BGLU B 68 9637 11083 11687 2747 -706 -2236 D000 O ATOM 3728 N ARG B 69 -21.516 7.983 41.680 1.00 60.13 D000 N ANISOU 3728 N ARG B 69 6961 8251 7635 1472 -229 -1541 D000 N ATOM 3729 CA ARG B 69 -20.422 8.625 42.401 1.00 57.58 D000 C ANISOU 3729 CA ARG B 69 6874 7550 7452 1338 -483 -1410 D000 C ATOM 3730 C ARG B 69 -19.039 8.192 41.938 1.00 60.72 D000 C ANISOU 3730 C ARG B 69 7443 7935 7692 1110 -460 -1349 D000 C ATOM 3731 O ARG B 69 -18.047 8.751 42.416 1.00 55.62 D000 O ANISOU 3731 O ARG B 69 6950 7016 7167 973 -649 -1241 D000 O ATOM 3732 CB ARG B 69 -20.555 8.371 43.901 1.00 59.39 D000 C ANISOU 3732 CB ARG B 69 7064 7706 7797 1189 -584 -1110 D000 C ATOM 3733 CG ARG B 69 -21.808 9.017 44.474 1.00 73.09 D000 C ANISOU 3733 CG ARG B 69 8654 9377 9741 1427 -715 -1152 D000 C ATOM 3734 CD ARG B 69 -22.061 8.598 45.895 1.00 65.92 D000 C ANISOU 3734 CD ARG B 69 7702 8475 8868 1285 -814 -867 D000 C ATOM 3735 NE ARG B 69 -22.714 7.296 45.935 1.00 63.31 D000 N ANISOU 3735 NE ARG B 69 7153 8490 8411 1190 -620 -830 D000 N ATOM 3736 CZ ARG B 69 -23.254 6.760 47.018 1.00 63.96 D000 C ANISOU 3736 CZ ARG B 69 7140 8650 8511 1106 -704 -666 D000 C ATOM 3737 NH1 ARG B 69 -23.321 7.427 48.159 1.00 62.98 D000 N ANISOU 3737 NH1 ARG B 69 7112 8333 8486 1138 -962 -513 D000 N ATOM 3738 NH2 ARG B 69 -23.749 5.527 46.950 1.00 59.08 D000 N ANISOU 3738 NH2 ARG B 69 6345 8299 7806 977 -554 -644 D000 N ATOM 3739 N HIS B 70 -18.929 7.228 41.036 1.00 57.34 D000 N ANISOU 3739 N HIS B 70 6980 7796 7012 1055 -252 -1387 D000 N ATOM 3740 CA HIS B 70 -17.621 6.890 40.494 1.00 53.36 D000 C ANISOU 3740 CA HIS B 70 6630 7269 6374 889 -281 -1356 D000 C ATOM 3741 C HIS B 70 -17.780 6.512 39.032 1.00 57.63 D000 C ANISOU 3741 C HIS B 70 7194 8073 6630 988 -130 -1542 D000 C ATOM 3742 O HIS B 70 -18.892 6.348 38.521 1.00 52.30 D000 O ANISOU 3742 O HIS B 70 6383 7650 5837 1142 59 -1649 D000 O ATOM 3743 CB HIS B 70 -16.917 5.807 41.333 1.00 46.69 D000 C ANISOU 3743 CB HIS B 70 5764 6470 5507 634 -242 -1069 D000 C ATOM 3744 CG HIS B 70 -17.595 4.471 41.366 1.00 47.88 D000 C ANISOU 3744 CG HIS B 70 5788 6880 5523 572 -46 -953 D000 C ATOM 3745 CD2 HIS B 70 -18.835 4.073 40.990 1.00 50.31 D000 C ANISOU 3745 CD2 HIS B 70 5943 7407 5765 651 116 -991 D000 C ATOM 3746 ND1 HIS B 70 -16.964 3.346 41.860 1.00 47.19 D000 N ANISOU 3746 ND1 HIS B 70 5711 6831 5388 392 -21 -770 D000 N ATOM 3747 CE1 HIS B 70 -17.785 2.313 41.782 1.00 53.10 D000 C ANISOU 3747 CE1 HIS B 70 6358 7751 6065 347 111 -696 D000 C ATOM 3748 NE2 HIS B 70 -18.924 2.726 41.253 1.00 51.46 D000 N ANISOU 3748 NE2 HIS B 70 6032 7676 5845 475 208 -804 D000 N ATOM 3749 N THR B 71 -16.645 6.450 38.343 1.00 50.70 D000 N ANISOU 3749 N THR B 71 6476 7156 5632 902 -223 -1581 D000 N ATOM 3750 CA THR B 71 -16.608 6.250 36.903 1.00 52.07 D000 C ANISOU 3750 CA THR B 71 6740 7561 5484 1000 -144 -1764 D000 C ATOM 3751 C THR B 71 -15.268 5.615 36.558 1.00 50.94 D000 C ANISOU 3751 C THR B 71 6717 7402 5236 810 -254 -1640 D000 C ATOM 3752 O THR B 71 -14.444 5.348 37.439 1.00 49.85 D000 O ANISOU 3752 O THR B 71 6550 7101 5289 630 -354 -1441 D000 O ATOM 3753 CB THR B 71 -16.837 7.573 36.162 1.00 61.62 D000 C ANISOU 3753 CB THR B 71 8061 8662 6688 1268 -271 -2154 D000 C ATOM 3754 CG2 THR B 71 -15.649 8.510 36.329 1.00 59.06 D000 C ANISOU 3754 CG2 THR B 71 7913 7938 6591 1189 -621 -2236 D000 C ATOM 3755 OG1 THR B 71 -17.046 7.317 34.768 1.00 64.53 D000 O ANISOU 3755 OG1 THR B 71 8504 9363 6651 1403 -134 -2351 D000 O ATOM 3756 N ASP B 72 -15.055 5.362 35.270 1.00 54.37 D000 N ANISOU 3756 N ASP B 72 7274 8039 5343 870 -235 -1759 D000 N ATOM 3757 CA ASP B 72 -13.854 4.678 34.798 1.00 58.23 D000 C ANISOU 3757 CA ASP B 72 7869 8547 5708 726 -368 -1641 D000 C ATOM 3758 C ASP B 72 -13.545 3.455 35.664 1.00 53.85 D000 C ANISOU 3758 C ASP B 72 7204 7988 5268 533 -298 -1300 D000 C ATOM 3759 O ASP B 72 -12.455 3.310 36.220 1.00 49.82 D000 O ANISOU 3759 O ASP B 72 6672 7318 4941 414 -456 -1199 D000 O ATOM 3760 CB ASP B 72 -12.654 5.630 34.769 1.00 61.80 D000 C ANISOU 3760 CB ASP B 72 8418 8716 6346 690 -699 -1795 D000 C ATOM 3761 CG ASP B 72 -12.876 6.826 33.869 1.00 75.08 D000 C ANISOU 3761 CG ASP B 72 10259 10339 7929 895 -841 -2187 D000 C ATOM 3762 OD1 ASP B 72 -13.831 6.803 33.065 1.00 93.62 D000 O ANISOU 3762 OD1 ASP B 72 12651 12954 9965 1095 -653 -2358 D000 O ATOM 3763 OD2 ASP B 72 -12.076 7.782 33.949 1.00 86.93 D000 O ANISOU 3763 OD2 ASP B 72 11834 11534 9661 852 -1145 -2333 D000 O ATOM 3764 N AILE B 73 -14.550 2.588 35.797 0.43 52.74 D000 N ANISOU 3764 N AILE B 73 6973 8031 5036 509 -62 -1142 D000 N ATOM 3765 N BILE B 73 -14.523 2.560 35.766 0.57 52.73 D000 N ANISOU 3765 N BILE B 73 6977 8034 5026 506 -64 -1139 D000 N ATOM 3766 CA AILE B 73 -14.383 1.357 36.551 0.43 49.14 D000 C ANISOU 3766 CA AILE B 73 6447 7545 4680 350 -23 -865 D000 C ATOM 3767 CA BILE B 73 -14.382 1.372 36.607 0.57 49.06 D000 C ANISOU 3767 CA BILE B 73 6432 7526 4683 348 -24 -865 D000 C ATOM 3768 C AILE B 73 -13.540 0.389 35.740 0.43 51.59 D000 C ANISOU 3768 C AILE B 73 6885 7916 4801 286 -114 -734 D000 C ATOM 3769 C BILE B 73 -13.656 0.284 35.824 0.57 51.53 D000 C ANISOU 3769 C BILE B 73 6863 7912 4801 276 -91 -711 D000 C ATOM 3770 O AILE B 73 -13.745 0.220 34.530 0.43 50.56 D000 O ANISOU 3770 O AILE B 73 6872 7985 4352 324 -72 -745 D000 O ATOM 3771 O BILE B 73 -14.070 -0.078 34.718 0.57 50.30 D000 O ANISOU 3771 O BILE B 73 6800 7972 4339 291 -4 -673 D000 O ATOM 3772 CB AILE B 73 -15.755 0.740 36.886 0.43 53.08 D000 C ANISOU 3772 CB AILE B 73 6809 8187 5174 311 204 -740 D000 C ATOM 3773 CB BILE B 73 -15.761 0.882 37.084 0.57 53.28 D000 C ANISOU 3773 CB BILE B 73 6818 8179 5247 318 193 -756 D000 C ATOM 3774 CG1AILE B 73 -16.431 1.525 38.009 0.43 52.61 D000 C ANISOU 3774 CG1AILE B 73 6604 8015 5370 367 221 -819 D000 C ATOM 3775 CG1BILE B 73 -16.512 2.010 37.801 0.57 53.27 D000 C ANISOU 3775 CG1BILE B 73 6698 8104 5440 434 214 -913 D000 C ATOM 3776 CG2AILE B 73 -15.599 -0.725 37.278 0.43 50.47 D000 C ANISOU 3776 CG2AILE B 73 6475 7820 4881 145 205 -475 D000 C ATOM 3777 CG2BILE B 73 -15.606 -0.326 37.999 0.57 51.28 D000 C ANISOU 3777 CG2BILE B 73 6518 7828 5137 164 177 -526 D000 C ATOM 3778 CD1AILE B 73 -16.902 2.899 37.593 0.43 55.22 D000 C ANISOU 3778 CD1AILE B 73 6931 8353 5697 568 217 -1086 D000 C ATOM 3779 CD1BILE B 73 -17.990 1.720 38.051 0.57 54.79 D000 C ANISOU 3779 CD1BILE B 73 6694 8469 5654 445 411 -861 D000 C ATOM 3780 N LEU B 74 -12.574 -0.250 36.396 1.00 52.40 D000 N ANISOU 3780 N LEU B 74 6966 7865 5079 211 -247 -612 D000 N ATOM 3781 CA LEU B 74 -11.781 -1.298 35.754 1.00 48.86 D000 C ANISOU 3781 CA LEU B 74 6623 7430 4512 180 -375 -466 D000 C ATOM 3782 C LEU B 74 -11.609 -2.465 36.714 1.00 47.13 D000 C ANISOU 3782 C LEU B 74 6338 7078 4489 117 -383 -291 D000 C ATOM 3783 O LEU B 74 -11.041 -2.309 37.798 1.00 45.41 D000 O ANISOU 3783 O LEU B 74 6002 6744 4507 127 -425 -342 D000 O ATOM 3784 CB LEU B 74 -10.411 -0.779 35.306 1.00 49.85 D000 C ANISOU 3784 CB LEU B 74 6787 7497 4656 227 -630 -585 D000 C ATOM 3785 CG LEU B 74 -9.538 -1.846 34.645 1.00 52.27 D000 C ANISOU 3785 CG LEU B 74 7189 7808 4864 234 -819 -436 D000 C ATOM 3786 CD1 LEU B 74 -10.169 -2.318 33.336 1.00 59.10 D000 C ANISOU 3786 CD1 LEU B 74 8262 8862 5332 233 -774 -324 D000 C ATOM 3787 CD2 LEU B 74 -8.125 -1.302 34.401 1.00 57.60 D000 C ANISOU 3787 CD2 LEU B 74 7817 8427 5641 273 -1100 -564 D000 C ATOM 3788 N CYS B 75 -12.088 -3.636 36.307 1.00 49.77 D000 N ANISOU 3788 N CYS B 75 6761 7433 4718 49 -351 -86 D000 N ATOM 3789 CA CYS B 75 -11.895 -4.851 37.086 1.00 48.80 D000 C ANISOU 3789 CA CYS B 75 6629 7126 4788 12 -424 47 D000 C ATOM 3790 C CYS B 75 -10.479 -5.366 36.846 1.00 49.18 D000 C ANISOU 3790 C CYS B 75 6731 7064 4892 110 -672 57 D000 C ATOM 3791 O CYS B 75 -10.113 -5.676 35.708 1.00 50.07 D000 O ANISOU 3791 O CYS B 75 6989 7219 4814 123 -804 162 D000 O ATOM 3792 CB CYS B 75 -12.930 -5.904 36.700 1.00 54.70 D000 C ANISOU 3792 CB CYS B 75 7458 7875 5450 -134 -347 289 D000 C ATOM 3793 SG CYS B 75 -12.727 -7.494 37.580 1.00 58.60 D000 S ANISOU 3793 SG CYS B 75 8001 8046 6216 -174 -520 422 D000 S ATOM 3794 N LEU B 76 -9.681 -5.450 37.915 1.00 50.87 D000 N ANISOU 3794 N LEU B 76 6811 7170 5347 194 -738 -51 D000 N ATOM 3795 CA LEU B 76 -8.292 -5.885 37.798 1.00 45.85 D000 C ANISOU 3795 CA LEU B 76 6141 6468 4815 327 -962 -78 D000 C ATOM 3796 C LEU B 76 -8.134 -7.388 37.959 1.00 52.31 D000 C ANISOU 3796 C LEU B 76 7052 7079 5743 398 -1108 35 D000 C ATOM 3797 O LEU B 76 -7.181 -7.966 37.422 1.00 53.91 D000 O ANISOU 3797 O LEU B 76 7294 7207 5983 523 -1346 76 D000 O ATOM 3798 CB LEU B 76 -7.426 -5.196 38.860 1.00 52.38 D000 C ANISOU 3798 CB LEU B 76 6723 7342 5836 393 -930 -255 D000 C ATOM 3799 CG LEU B 76 -7.296 -3.671 38.834 1.00 60.49 D000 C ANISOU 3799 CG LEU B 76 7647 8488 6849 316 -864 -360 D000 C ATOM 3800 CD1 LEU B 76 -6.580 -3.178 40.088 1.00 62.40 D000 C ANISOU 3800 CD1 LEU B 76 7646 8777 7287 322 -794 -443 D000 C ATOM 3801 CD2 LEU B 76 -6.558 -3.200 37.596 1.00 61.20 D000 C ANISOU 3801 CD2 LEU B 76 7781 8629 6844 328 -1068 -391 D000 C ATOM 3802 N LYS B 77 -9.039 -8.033 38.694 1.00 45.57 D000 N ANISOU 3802 N LYS B 77 6240 6105 4970 331 -1015 76 D000 N ATOM 3803 CA LYS B 77 -8.882 -9.450 38.990 1.00 46.56 D000 C ANISOU 3803 CA LYS B 77 6472 5960 5260 408 -1199 136 D000 C ATOM 3804 C LYS B 77 -10.246 -10.043 39.300 1.00 55.37 D000 C ANISOU 3804 C LYS B 77 7690 6950 6397 218 -1118 259 D000 C ATOM 3805 O LYS B 77 -11.016 -9.469 40.075 1.00 51.69 D000 O ANISOU 3805 O LYS B 77 7114 6588 5936 134 -927 164 D000 O ATOM 3806 CB LYS B 77 -7.912 -9.643 40.162 1.00 53.38 D000 C ANISOU 3806 CB LYS B 77 7166 6785 6331 636 -1245 -111 D000 C ATOM 3807 CG LYS B 77 -7.093 -10.923 40.103 1.00 64.30 D000 C ANISOU 3807 CG LYS B 77 8628 7910 7893 856 -1531 -126 D000 C ATOM 3808 CD LYS B 77 -6.334 -11.169 41.406 1.00 65.67 D000 C ANISOU 3808 CD LYS B 77 8613 8098 8241 1111 -1514 -424 D000 C ATOM 3809 CE LYS B 77 -6.049 -12.648 41.614 1.00106.07 D000 C ANISOU 3809 CE LYS B 77 13875 12858 13568 1334 -1792 -490 D000 C ATOM 3810 NZ LYS B 77 -4.838 -12.900 42.445 1.00107.57 D000 N ANISOU 3810 NZ LYS B 77 13836 13129 13908 1699 -1828 -802 D000 N ATOM 3811 N SER B 78 -10.541 -11.182 38.678 1.00 53.57 D000 N ANISOU 3811 N SER B 78 7665 6489 6198 132 -1293 496 D000 N ATOM 3812 CA SER B 78 -11.781 -11.913 38.908 1.00 64.01 D000 C ANISOU 3812 CA SER B 78 9073 7647 7601 -98 -1272 658 D000 C ATOM 3813 C SER B 78 -11.401 -13.351 39.227 1.00 66.80 D000 C ANISOU 3813 C SER B 78 9601 7564 8215 -13 -1595 686 D000 C ATOM 3814 O SER B 78 -11.005 -14.101 38.332 1.00 63.21 D000 O ANISOU 3814 O SER B 78 9338 6915 7763 -11 -1822 920 D000 O ATOM 3815 CB SER B 78 -12.702 -11.842 37.690 1.00 63.48 D000 C ANISOU 3815 CB SER B 78 9086 7733 7299 -369 -1151 994 D000 C ATOM 3816 OG SER B 78 -13.930 -12.509 37.933 1.00 77.83 D000 O ANISOU 3816 OG SER B 78 10917 9427 9229 -638 -1116 1175 D000 O ATOM 3817 N GLU B 79 -11.508 -13.732 40.495 1.00 53.51 D000 N ANISOU 3817 N GLU B 79 7874 5715 6742 78 -1646 437 D000 N ATOM 3818 CA GLU B 79 -11.159 -15.073 40.940 1.00 57.87 D000 C ANISOU 3818 CA GLU B 79 8601 5815 7570 213 -1978 366 D000 C ATOM 3819 C GLU B 79 -12.427 -15.892 41.130 1.00 65.17 D000 C ANISOU 3819 C GLU B 79 9657 6455 8651 -97 -2079 539 D000 C ATOM 3820 O GLU B 79 -13.352 -15.465 41.828 1.00 57.55 D000 O ANISOU 3820 O GLU B 79 8561 5634 7671 -255 -1909 450 D000 O ATOM 3821 CB GLU B 79 -10.371 -15.030 42.250 1.00 66.04 D000 C ANISOU 3821 CB GLU B 79 9515 6868 8710 556 -1991 -80 D000 C ATOM 3822 CG GLU B 79 -9.207 -14.063 42.233 1.00 58.87 D000 C ANISOU 3822 CG GLU B 79 8386 6313 7668 797 -1836 -243 D000 C ATOM 3823 CD GLU B 79 -8.599 -13.849 43.608 1.00 66.19 D000 C ANISOU 3823 CD GLU B 79 9136 7387 8625 1069 -1741 -640 D000 C ATOM 3824 OE1 GLU B 79 -7.925 -14.770 44.115 1.00 69.93 D000 O ANISOU 3824 OE1 GLU B 79 9657 7642 9271 1365 -1946 -869 D000 O ATOM 3825 OE2 GLU B 79 -8.779 -12.749 44.168 1.00 61.49 D000 O ANISOU 3825 OE2 GLU B 79 8357 7136 7868 1000 -1463 -718 D000 O ATOM 3826 N VAL B 80 -12.463 -17.062 40.510 1.00 65.15 D000 N ANISOU 3826 N VAL B 80 9903 6032 8819 -199 -2386 806 D000 N ATOM 3827 CA VAL B 80 -13.557 -18.005 40.679 1.00 69.96 D000 C ANISOU 3827 CA VAL B 80 10648 6278 9654 -526 -2562 999 D000 C ATOM 3828 C VAL B 80 -12.971 -19.278 41.271 1.00 77.22 D000 C ANISOU 3828 C VAL B 80 11805 6607 10928 -292 -3010 799 D000 C ATOM 3829 O VAL B 80 -11.766 -19.532 41.194 1.00 84.68 D000 O ANISOU 3829 O VAL B 80 12822 7431 11923 91 -3185 634 D000 O ATOM 3830 CB VAL B 80 -14.295 -18.272 39.353 1.00 79.82 D000 C ANISOU 3830 CB VAL B 80 11996 7534 10798 -942 -2529 1576 D000 C ATOM 3831 CG1 VAL B 80 -14.624 -16.951 38.661 1.00 72.21 D000 C ANISOU 3831 CG1 VAL B 80 10809 7191 9435 -1041 -2090 1684 D000 C ATOM 3832 CG2 VAL B 80 -13.454 -19.130 38.425 1.00 74.58 D000 C ANISOU 3832 CG2 VAL B 80 11621 6528 10189 -847 -2860 1848 D000 C ATOM 3833 N GLU B 81 -13.834 -20.074 41.893 1.00 84.94 D000 N ANISOU 3833 N GLU B 81 12888 7212 12174 -505 -3221 779 D000 N ATOM 3834 CA GLU B 81 -13.383 -21.279 42.583 1.00 90.58 D000 C ANISOU 3834 CA GLU B 81 13849 7321 13247 -262 -3680 502 D000 C ATOM 3835 C GLU B 81 -12.507 -20.919 43.784 1.00 93.60 D000 C ANISOU 3835 C GLU B 81 14110 7882 13570 254 -3616 -126 D000 C ATOM 3836 O GLU B 81 -11.530 -21.604 44.085 1.00 99.14 D000 O ANISOU 3836 O GLU B 81 14946 8279 14446 673 -3894 -418 D000 O ATOM 3837 CB GLU B 81 -12.635 -22.205 41.618 1.00102.34 D000 C ANISOU 3837 CB GLU B 81 15619 8358 14907 -161 -4043 783 D000 C ATOM 3838 CG GLU B 81 -12.645 -23.673 42.001 1.00112.11 D000 C ANISOU 3838 CG GLU B 81 17192 8797 16608 -108 -4609 701 D000 C ATOM 3839 CD GLU B 81 -12.113 -24.563 40.891 1.00132.15 D000 C ANISOU 3839 CD GLU B 81 20034 10858 19320 -105 -4991 1126 D000 C ATOM 3840 OE1 GLU B 81 -10.996 -24.296 40.396 1.00142.39 D000 O ANISOU 3840 OE1 GLU B 81 21299 12322 20481 267 -4980 1087 D000 O ATOM 3841 OE2 GLU B 81 -12.809 -25.532 40.519 1.00120.05 D000 O ANISOU 3841 OE2 GLU B 81 18747 8809 18056 -489 -5311 1510 D000 O ATOM 3842 N VAL B 82 -12.848 -19.824 44.467 1.00 76.63 D000 N ANISOU 3842 N VAL B 82 11698 6253 11166 236 -3242 -323 D000 N ATOM 3843 CA VAL B 82 -12.156 -19.446 45.695 1.00 87.78 D000 C ANISOU 3843 CA VAL B 82 12988 7897 12467 654 -3140 -865 D000 C ATOM 3844 C VAL B 82 -12.693 -20.302 46.836 1.00 93.89 D000 C ANISOU 3844 C VAL B 82 13928 8304 13441 690 -3436 -1212 D000 C ATOM 3845 O VAL B 82 -13.901 -20.557 46.927 1.00 89.34 D000 O ANISOU 3845 O VAL B 82 13406 7553 12986 293 -3542 -1048 D000 O ATOM 3846 CB VAL B 82 -12.335 -17.945 45.982 1.00 82.79 D000 C ANISOU 3846 CB VAL B 82 12050 7918 11486 591 -2671 -886 D000 C ATOM 3847 CG1 VAL B 82 -11.747 -17.580 47.341 1.00 84.85 D000 C ANISOU 3847 CG1 VAL B 82 12198 8442 11599 953 -2555 -1382 D000 C ATOM 3848 CG2 VAL B 82 -11.689 -17.109 44.886 1.00 76.55 D000 C ANISOU 3848 CG2 VAL B 82 11121 7450 10514 599 -2435 -624 D000 C ATOM 3849 N GLN B 83 -11.793 -20.747 47.715 1.00 94.46 D000 N ANISOU 3849 N GLN B 83 14063 8280 13547 1177 -3579 -1718 D000 N ATOM 3850 CA GLN B 83 -12.139 -21.694 48.769 1.00 99.20 D000 C ANISOU 3850 CA GLN B 83 14883 8474 14335 1301 -3934 -2134 D000 C ATOM 3851 C GLN B 83 -11.879 -21.148 50.168 1.00101.21 D000 C ANISOU 3851 C GLN B 83 15005 9168 14280 1619 -3725 -2661 D000 C ATOM 3852 O GLN B 83 -12.015 -21.892 51.147 1.00 99.34 D000 O ANISOU 3852 O GLN B 83 14959 8663 14121 1817 -4012 -3111 D000 O ATOM 3853 CB GLN B 83 -11.368 -23.010 48.572 1.00 98.64 D000 C ANISOU 3853 CB GLN B 83 15092 7767 14619 1643 -4402 -2319 D000 C ATOM 3854 CG GLN B 83 -9.880 -22.981 48.959 1.00120.04 D000 C ANISOU 3854 CG GLN B 83 17691 10691 17227 2300 -4320 -2762 D000 C ATOM 3855 CD GLN B 83 -9.057 -21.978 48.162 1.00127.84 D000 C ANISOU 3855 CD GLN B 83 18375 12204 17992 2354 -3933 -2488 D000 C ATOM 3856 NE2 GLN B 83 -7.834 -22.364 47.812 1.00130.80 D000 N ANISOU 3856 NE2 GLN B 83 18715 12488 18493 2795 -4058 -2619 D000 N ATOM 3857 OE1 GLN B 83 -9.512 -20.872 47.870 1.00107.85 D000 O ANISOU 3857 OE1 GLN B 83 15639 10139 15200 2020 -3557 -2184 D000 O ATOM 3858 N GLU B 84 -11.520 -19.872 50.294 1.00101.70 D000 N ANISOU 3858 N GLU B 84 14770 9891 13980 1664 -3254 -2612 D000 N ATOM 3859 CA GLU B 84 -11.161 -19.310 51.592 1.00 93.51 D000 C ANISOU 3859 CA GLU B 84 13605 9323 12601 1958 -3025 -3042 D000 C ATOM 3860 C GLU B 84 -11.268 -17.795 51.514 1.00 92.60 D000 C ANISOU 3860 C GLU B 84 13194 9831 12160 1758 -2553 -2771 D000 C ATOM 3861 O GLU B 84 -10.698 -17.177 50.609 1.00 86.66 D000 O ANISOU 3861 O GLU B 84 12270 9269 11387 1722 -2340 -2486 D000 O ATOM 3862 CB GLU B 84 -9.744 -19.758 51.987 1.00113.51 D000 C ANISOU 3862 CB GLU B 84 16108 11914 15108 2548 -3035 -3475 D000 C ATOM 3863 CG GLU B 84 -9.158 -19.107 53.234 1.00129.11 D000 C ANISOU 3863 CG GLU B 84 17894 14499 16661 2872 -2706 -3870 D000 C ATOM 3864 CD GLU B 84 -7.636 -19.160 53.257 1.00149.05 D000 C ANISOU 3864 CD GLU B 84 20208 17283 19143 3378 -2547 -4121 D000 C ATOM 3865 OE1 GLU B 84 -7.051 -18.957 54.342 1.00152.49 D000 O ANISOU 3865 OE1 GLU B 84 20512 18166 19259 3721 -2326 -4521 D000 O ATOM 3866 OE2 GLU B 84 -7.023 -19.410 52.195 1.00134.34 D000 O ANISOU 3866 OE2 GLU B 84 18291 15205 17547 3434 -2644 -3912 D000 O ATOM 3867 N ARG B 85 -12.001 -17.205 52.456 1.00 82.12 D000 N ANISOU 3867 N ARG B 85 11827 8786 10591 1635 -2438 -2865 D000 N ATOM 3868 CA ARG B 85 -12.192 -15.761 52.464 1.00 73.38 D000 C ANISOU 3868 CA ARG B 85 10475 8199 9207 1448 -2049 -2609 D000 C ATOM 3869 C ARG B 85 -10.930 -15.052 52.930 1.00 69.10 D000 C ANISOU 3869 C ARG B 85 9730 8145 8381 1768 -1722 -2764 D000 C ATOM 3870 O ARG B 85 -10.218 -15.529 53.818 1.00 71.49 D000 O ANISOU 3870 O ARG B 85 10064 8549 8550 2140 -1740 -3173 D000 O ATOM 3871 CB ARG B 85 -13.352 -15.372 53.381 1.00 72.38 D000 C ANISOU 3871 CB ARG B 85 10374 8205 8919 1245 -2079 -2652 D000 C ATOM 3872 CG ARG B 85 -14.717 -15.419 52.728 1.00 76.23 D000 C ANISOU 3872 CG ARG B 85 10873 8446 9644 800 -2226 -2321 D000 C ATOM 3873 CD ARG B 85 -15.817 -15.101 53.728 1.00 71.76 D000 C ANISOU 3873 CD ARG B 85 10306 8013 8947 648 -2316 -2411 D000 C ATOM 3874 NE ARG B 85 -17.071 -15.738 53.351 1.00 73.35 D000 N ANISOU 3874 NE ARG B 85 10554 7846 9472 285 -2610 -2251 D000 N ATOM 3875 CZ ARG B 85 -18.001 -15.176 52.591 1.00 70.75 D000 C ANISOU 3875 CZ ARG B 85 10033 7591 9260 -68 -2499 -1860 D000 C ATOM 3876 NH1 ARG B 85 -17.864 -13.945 52.127 1.00 65.80 D000 N ANISOU 3876 NH1 ARG B 85 9196 7346 8458 -87 -2137 -1623 D000 N ATOM 3877 NH2 ARG B 85 -19.093 -15.870 52.285 1.00 71.56 D000 N ANISOU 3877 NH2 ARG B 85 10138 7376 9674 -411 -2765 -1715 D000 N ATOM 3878 N AMET B 86 -10.658 -13.906 52.306 0.61 67.77 D000 N ANISOU 3878 N AMET B 86 9339 8284 8125 1615 -1425 -2440 D000 N ATOM 3879 N BMET B 86 -10.656 -13.890 52.336 0.39 67.78 D000 N ANISOU 3879 N BMET B 86 9339 8296 8119 1617 -1420 -2444 D000 N ATOM 3880 CA AMET B 86 -9.544 -13.056 52.700 0.61 66.87 D000 C ANISOU 3880 CA AMET B 86 8982 8655 7769 1807 -1099 -2492 D000 C ATOM 3881 CA BMET B 86 -9.507 -13.092 52.744 0.39 66.88 D000 C ANISOU 3881 CA BMET B 86 8985 8660 7766 1825 -1101 -2512 D000 C ATOM 3882 C AMET B 86 -9.889 -12.227 53.929 0.61 67.53 D000 C ANISOU 3882 C AMET B 86 9018 9146 7493 1765 -903 -2551 D000 C ATOM 3883 C BMET B 86 -9.840 -12.082 53.834 0.39 67.53 D000 C ANISOU 3883 C BMET B 86 8991 9174 7494 1743 -871 -2506 D000 C ATOM 3884 O AMET B 86 -9.069 -12.091 54.844 0.61 68.48 D000 O ANISOU 3884 O AMET B 86 9036 9634 7348 2020 -720 -2776 D000 O ATOM 3885 O BMET B 86 -8.935 -11.669 54.568 0.39 70.92 D000 O ANISOU 3885 O BMET B 86 9261 10018 7668 1943 -631 -2636 D000 O ATOM 3886 CB AMET B 86 -9.179 -12.136 51.537 0.61 65.95 D000 C ANISOU 3886 CB AMET B 86 8678 8648 7731 1620 -925 -2123 D000 C ATOM 3887 CB BMET B 86 -8.918 -12.353 51.536 0.39 65.70 D000 C ANISOU 3887 CB BMET B 86 8643 8596 7723 1703 -948 -2184 D000 C ATOM 3888 CG AMET B 86 -7.716 -12.057 51.205 0.61 70.37 D000 C ANISOU 3888 CG AMET B 86 9021 9395 8322 1866 -807 -2181 D000 C ATOM 3889 CG BMET B 86 -8.047 -13.228 50.646 0.39 67.98 D000 C ANISOU 3889 CG BMET B 86 8940 8619 8269 1912 -1125 -2229 D000 C ATOM 3890 SD AMET B 86 -7.500 -11.116 49.681 0.61 66.71 D000 S ANISOU 3890 SD AMET B 86 8419 8945 7981 1605 -731 -1768 D000 S ATOM 3891 SD BMET B 86 -6.780 -12.318 49.735 0.39 70.01 D000 S ANISOU 3891 SD BMET B 86 8882 9174 8546 1938 -920 -2025 D000 S ATOM 3892 CE AMET B 86 -6.838 -12.382 48.604 0.61 72.87 D000 C ANISOU 3892 CE AMET B 86 9295 9332 9059 1815 -1041 -1803 D000 C ATOM 3893 CE BMET B 86 -5.887 -11.527 51.070 0.39 74.12 D000 C ANISOU 3893 CE BMET B 86 9102 10290 8771 2119 -566 -2227 D000 C ATOM 3894 N PHE B 87 -11.104 -11.681 53.966 1.00 68.16 D000 N ANISOU 3894 N PHE B 87 9162 9187 7550 1455 -943 -2339 D000 N ATOM 3895 CA PHE B 87 -11.534 -10.740 55.002 1.00 68.60 D000 C ANISOU 3895 CA PHE B 87 9183 9601 7281 1374 -796 -2298 D000 C ATOM 3896 C PHE B 87 -12.815 -11.240 55.664 1.00 69.89 D000 C ANISOU 3896 C PHE B 87 9548 9577 7429 1274 -1076 -2425 D000 C ATOM 3897 O PHE B 87 -13.864 -10.594 55.592 1.00 59.72 D000 O ANISOU 3897 O PHE B 87 8240 8286 6167 1013 -1113 -2194 D000 O ATOM 3898 CB PHE B 87 -11.740 -9.353 54.396 1.00 69.16 D000 C ANISOU 3898 CB PHE B 87 9088 9829 7360 1111 -594 -1897 D000 C ATOM 3899 CG PHE B 87 -10.616 -8.907 53.496 1.00 63.12 D000 C ANISOU 3899 CG PHE B 87 8133 9152 6697 1142 -407 -1753 D000 C ATOM 3900 CD1 PHE B 87 -9.397 -8.520 54.029 1.00 69.96 D000 C ANISOU 3900 CD1 PHE B 87 8825 10382 7375 1308 -175 -1818 D000 C ATOM 3901 CD2 PHE B 87 -10.783 -8.876 52.121 1.00 61.91 D000 C ANISOU 3901 CD2 PHE B 87 7961 8752 6810 994 -467 -1550 D000 C ATOM 3902 CE1 PHE B 87 -8.365 -8.105 53.204 1.00 68.95 D000 C ANISOU 3902 CE1 PHE B 87 8487 10334 7378 1312 -44 -1690 D000 C ATOM 3903 CE2 PHE B 87 -9.755 -8.464 51.290 1.00 63.58 D000 C ANISOU 3903 CE2 PHE B 87 8012 9042 7102 1022 -349 -1439 D000 C ATOM 3904 CZ PHE B 87 -8.543 -8.082 51.835 1.00 65.10 D000 C ANISOU 3904 CZ PHE B 87 8012 9563 7161 1177 -157 -1514 D000 C ATOM 3905 N PRO B 88 -12.759 -12.392 56.334 1.00 65.42 D000 N ANISOU 3905 N PRO B 88 9171 8848 6839 1496 -1307 -2819 D000 N ATOM 3906 CA PRO B 88 -13.996 -12.990 56.864 1.00 73.49 D000 C ANISOU 3906 CA PRO B 88 10389 9616 7918 1368 -1657 -2958 D000 C ATOM 3907 C PRO B 88 -14.718 -12.152 57.911 1.00 75.71 D000 C ANISOU 3907 C PRO B 88 10674 10231 7860 1274 -1632 -2917 D000 C ATOM 3908 O PRO B 88 -15.930 -12.332 58.087 1.00 74.74 D000 O ANISOU 3908 O PRO B 88 10623 9919 7854 1066 -1911 -2895 D000 O ATOM 3909 CB PRO B 88 -13.507 -14.320 57.461 1.00 74.29 D000 C ANISOU 3909 CB PRO B 88 10706 9503 8017 1703 -1902 -3463 D000 C ATOM 3910 CG PRO B 88 -12.072 -14.074 57.777 1.00 79.56 D000 C ANISOU 3910 CG PRO B 88 11247 10566 8417 2060 -1577 -3625 D000 C ATOM 3911 CD PRO B 88 -11.582 -13.228 56.633 1.00 74.25 D000 C ANISOU 3911 CD PRO B 88 10323 9984 7905 1892 -1297 -3192 D000 C ATOM 3912 N ASP B 89 -14.032 -11.251 58.613 1.00 72.00 D000 N ANISOU 3912 N ASP B 89 10119 10250 6987 1402 -1331 -2880 D000 N ATOM 3913 CA ASP B 89 -14.659 -10.481 59.682 1.00 88.83 D000 C ANISOU 3913 CA ASP B 89 12299 12700 8753 1334 -1342 -2817 D000 C ATOM 3914 C ASP B 89 -15.241 -9.150 59.213 1.00 77.07 D000 C ANISOU 3914 C ASP B 89 10643 11297 7343 1048 -1215 -2344 D000 C ATOM 3915 O ASP B 89 -15.757 -8.392 60.040 1.00 72.13 D000 O ANISOU 3915 O ASP B 89 10051 10912 6442 989 -1242 -2226 D000 O ATOM 3916 CB ASP B 89 -13.647 -10.207 60.805 1.00 99.11 D000 C ANISOU 3916 CB ASP B 89 13620 14520 9517 1608 -1087 -2992 D000 C ATOM 3917 CG ASP B 89 -13.185 -11.471 61.506 1.00107.46 D000 C ANISOU 3917 CG ASP B 89 14864 15557 10408 1964 -1232 -3552 D000 C ATOM 3918 OD1 ASP B 89 -13.986 -12.424 61.620 1.00105.59 D000 O ANISOU 3918 OD1 ASP B 89 14834 14935 10352 1961 -1639 -3824 D000 O ATOM 3919 OD2 ASP B 89 -12.019 -11.506 61.956 1.00100.51 D000 O ANISOU 3919 OD2 ASP B 89 13896 15026 9269 2227 -936 -3690 D000 O ATOM 3920 N TRP B 90 -15.175 -8.845 57.920 1.00 62.32 D000 N ANISOU 3920 N TRP B 90 8615 9233 5830 895 -1104 -2084 D000 N ATOM 3921 CA TRP B 90 -15.476 -7.505 57.419 1.00 60.69 D000 C ANISOU 3921 CA TRP B 90 8250 9125 5686 697 -945 -1691 D000 C ATOM 3922 C TRP B 90 -16.552 -7.579 56.343 1.00 62.00 D000 C ANISOU 3922 C TRP B 90 8335 8971 6249 477 -1088 -1532 D000 C ATOM 3923 O TRP B 90 -16.264 -7.927 55.198 1.00 53.90 D000 O ANISOU 3923 O TRP B 90 7248 7749 5482 431 -1027 -1472 D000 O ATOM 3924 CB TRP B 90 -14.224 -6.841 56.846 1.00 61.75 D000 C ANISOU 3924 CB TRP B 90 8236 9419 5807 737 -622 -1530 D000 C ATOM 3925 CG TRP B 90 -13.159 -6.515 57.835 1.00 66.63 D000 C ANISOU 3925 CG TRP B 90 8839 10442 6037 895 -402 -1587 D000 C ATOM 3926 CD1 TRP B 90 -13.264 -6.506 59.188 1.00 71.71 D000 C ANISOU 3926 CD1 TRP B 90 9607 11374 6267 995 -426 -1706 D000 C ATOM 3927 CD2 TRP B 90 -11.820 -6.121 57.531 1.00 72.12 D000 C ANISOU 3927 CD2 TRP B 90 9357 11345 6700 954 -112 -1504 D000 C ATOM 3928 CE2 TRP B 90 -11.162 -5.897 58.752 1.00 82.33 D000 C ANISOU 3928 CE2 TRP B 90 10645 13080 7556 1076 71 -1560 D000 C ATOM 3929 CE3 TRP B 90 -11.113 -5.937 56.337 1.00 68.91 D000 C ANISOU 3929 CE3 TRP B 90 8782 10817 6582 907 0 -1384 D000 C ATOM 3930 NE1 TRP B 90 -12.065 -6.142 59.753 1.00 75.48 D000 N ANISOU 3930 NE1 TRP B 90 9988 12262 6428 1110 -123 -1687 D000 N ATOM 3931 CZ2 TRP B 90 -9.827 -5.502 58.818 1.00 85.41 D000 C ANISOU 3931 CZ2 TRP B 90 10819 13806 7828 1131 386 -1483 D000 C ATOM 3932 CZ3 TRP B 90 -9.795 -5.544 56.404 1.00 68.22 D000 C ANISOU 3932 CZ3 TRP B 90 8497 11024 6399 970 260 -1331 D000 C ATOM 3933 CH2 TRP B 90 -9.163 -5.332 57.636 1.00 80.88 D000 C ANISOU 3933 CH2 TRP B 90 10050 13076 7602 1071 463 -1372 D000 C ATOM 3934 N SER B 91 -17.788 -7.222 56.695 1.00 53.92 D000 N ANISOU 3934 N SER B 91 7292 7936 5259 345 -1272 -1447 D000 N ATOM 3935 CA ASER B 91 -18.830 -7.122 55.677 0.72 51.99 D000 C ANISOU 3935 CA ASER B 91 6894 7490 5370 140 -1340 -1269 D000 C ATOM 3936 CA BSER B 91 -18.831 -7.122 55.678 0.28 52.21 D000 C ANISOU 3936 CA BSER B 91 6922 7518 5398 140 -1341 -1269 D000 C ATOM 3937 C SER B 91 -18.460 -6.088 54.621 1.00 56.41 D000 C ANISOU 3937 C SER B 91 7306 8100 6028 98 -1073 -1015 D000 C ATOM 3938 O SER B 91 -18.692 -6.298 53.425 1.00 52.96 D000 O ANISOU 3938 O SER B 91 6773 7511 5837 -7 -1019 -921 D000 O ATOM 3939 CB ASER B 91 -20.167 -6.778 56.334 0.72 54.87 D000 C ANISOU 3939 CB ASER B 91 7202 7897 5750 45 -1579 -1229 D000 C ATOM 3940 CB BSER B 91 -20.168 -6.777 56.334 0.28 55.04 D000 C ANISOU 3940 CB BSER B 91 7222 7918 5771 45 -1579 -1229 D000 C ATOM 3941 OG ASER B 91 -20.683 -7.904 57.013 0.72 60.86 D000 O ANISOU 3941 OG ASER B 91 8078 8524 6522 24 -1894 -1479 D000 O ATOM 3942 OG BSER B 91 -20.031 -5.683 57.222 0.28 61.04 D000 O ANISOU 3942 OG BSER B 91 8020 8936 6238 135 -1535 -1129 D000 O ATOM 3943 N MET B 92 -17.890 -4.963 55.046 1.00 53.97 D000 N ANISOU 3943 N MET B 92 6991 8000 5514 166 -920 -894 D000 N ATOM 3944 CA MET B 92 -17.269 -3.986 54.158 1.00 55.60 D000 C ANISOU 3944 CA MET B 92 7100 8230 5795 145 -699 -705 D000 C ATOM 3945 C MET B 92 -16.462 -3.023 55.015 1.00 62.82 D000 C ANISOU 3945 C MET B 92 8054 9370 6447 199 -581 -596 D000 C ATOM 3946 O MET B 92 -17.010 -2.053 55.553 1.00 61.41 D000 O ANISOU 3946 O MET B 92 7878 9251 6202 165 -648 -435 D000 O ATOM 3947 CB MET B 92 -18.276 -3.204 53.321 1.00 48.56 D000 C ANISOU 3947 CB MET B 92 6068 7251 5131 50 -714 -548 D000 C ATOM 3948 CG MET B 92 -17.649 -2.409 52.157 1.00 53.98 D000 C ANISOU 3948 CG MET B 92 6684 7904 5921 40 -526 -432 D000 C ATOM 3949 SD MET B 92 -16.168 -3.102 51.397 1.00 52.97 D000 S ANISOU 3949 SD MET B 92 6597 7750 5782 76 -378 -502 D000 S ATOM 3950 CE MET B 92 -16.846 -4.661 50.826 1.00 51.38 D000 C ANISOU 3950 CE MET B 92 6421 7369 5731 20 -498 -608 D000 C ATOM 3951 N GLN B 93 -15.174 -3.290 55.163 1.00 51.80 D000 N ANISOU 3951 N GLN B 93 6670 8103 4910 278 -416 -661 D000 N ATOM 3952 CA GLN B 93 -14.307 -2.415 55.936 1.00 57.17 D000 C ANISOU 3952 CA GLN B 93 7342 9042 5339 281 -258 -512 D000 C ATOM 3953 C GLN B 93 -13.872 -1.260 55.046 1.00 59.71 D000 C ANISOU 3953 C GLN B 93 7550 9285 5851 164 -147 -277 D000 C ATOM 3954 O GLN B 93 -13.427 -1.470 53.915 1.00 57.33 D000 O ANISOU 3954 O GLN B 93 7167 8854 5760 158 -89 -322 D000 O ATOM 3955 CB GLN B 93 -13.098 -3.186 56.457 1.00 58.30 D000 C ANISOU 3955 CB GLN B 93 7478 9412 5263 427 -104 -698 D000 C ATOM 3956 CG GLN B 93 -12.156 -2.366 57.318 1.00 63.78 D000 C ANISOU 3956 CG GLN B 93 8115 10460 5657 403 110 -520 D000 C ATOM 3957 CD GLN B 93 -12.600 -2.306 58.764 1.00 70.32 D000 C ANISOU 3957 CD GLN B 93 9098 11543 6076 445 51 -517 D000 C ATOM 3958 NE2 GLN B 93 -11.652 -2.084 59.664 1.00 85.18 D000 N ANISOU 3958 NE2 GLN B 93 10942 13832 7590 481 278 -454 D000 N ATOM 3959 OE1 GLN B 93 -13.785 -2.461 59.068 1.00 82.16 D000 O ANISOU 3959 OE1 GLN B 93 10736 12907 7575 442 -199 -566 D000 O ATOM 3960 N THR B 94 -14.006 -0.043 55.553 1.00 55.45 D000 N ANISOU 3960 N THR B 94 7030 8799 5240 72 -157 -26 D000 N ATOM 3961 CA THR B 94 -13.713 1.161 54.786 1.00 56.76 D000 C ANISOU 3961 CA THR B 94 7127 8821 5620 -45 -124 183 D000 C ATOM 3962 C THR B 94 -12.452 1.790 55.355 1.00 55.76 D000 C ANISOU 3962 C THR B 94 6944 8905 5335 -149 46 384 D000 C ATOM 3963 O THR B 94 -12.372 2.037 56.557 1.00 55.45 D000 O ANISOU 3963 O THR B 94 6973 9093 5004 -179 76 531 D000 O ATOM 3964 CB THR B 94 -14.897 2.122 54.835 1.00 61.30 D000 C ANISOU 3964 CB THR B 94 7763 9212 6317 -72 -318 327 D000 C ATOM 3965 CG2 THR B 94 -14.593 3.403 54.082 1.00 61.87 D000 C ANISOU 3965 CG2 THR B 94 7802 9080 6624 -163 -330 498 D000 C ATOM 3966 OG1 THR B 94 -16.026 1.483 54.228 1.00 59.77 D000 O ANISOU 3966 OG1 THR B 94 7540 8882 6286 7 -432 141 D000 O ATOM 3967 N ILE B 95 -11.458 2.009 54.500 1.00 53.48 D000 N ANISOU 3967 N ILE B 95 6519 8578 5223 -215 154 400 D000 N ATOM 3968 CA ILE B 95 -10.178 2.567 54.909 1.00 54.87 D000 C ANISOU 3968 CA ILE B 95 6562 8972 5314 -355 327 600 D000 C ATOM 3969 C ILE B 95 -9.940 3.803 54.055 1.00 55.33 D000 C ANISOU 3969 C ILE B 95 6581 8759 5682 -538 236 791 D000 C ATOM 3970 O ILE B 95 -9.671 3.691 52.853 1.00 55.99 D000 O ANISOU 3970 O ILE B 95 6596 8673 6006 -517 196 645 D000 O ATOM 3971 CB ILE B 95 -9.032 1.560 54.757 1.00 61.24 D000 C ANISOU 3971 CB ILE B 95 7186 10019 6062 -249 514 400 D000 C ATOM 3972 CG1 ILE B 95 -9.234 0.359 55.683 1.00 67.89 D000 C ANISOU 3972 CG1 ILE B 95 8100 11100 6596 -35 573 163 D000 C ATOM 3973 CG2 ILE B 95 -7.708 2.212 55.104 1.00 63.98 D000 C ANISOU 3973 CG2 ILE B 95 7312 10631 6367 -421 709 628 D000 C ATOM 3974 CD1 ILE B 95 -8.572 -0.916 55.185 1.00 68.89 D000 C ANISOU 3974 CD1 ILE B 95 8122 11268 6786 174 629 -157 D000 C ATOM 3975 N ASN B 96 -10.044 4.981 54.669 1.00 54.62 D000 N ANISOU 3975 N ASN B 96 6562 8608 5582 -715 169 1114 D000 N ATOM 3976 CA ASN B 96 -9.743 6.241 53.994 1.00 63.54 D000 C ANISOU 3976 CA ASN B 96 7680 9434 7026 -908 37 1303 D000 C ATOM 3977 C ASN B 96 -8.260 6.538 54.186 1.00 52.12 D000 C ANISOU 3977 C ASN B 96 6014 8206 5583 -1142 209 1505 D000 C ATOM 3978 O ASN B 96 -7.832 7.004 55.245 1.00 58.28 D000 O ANISOU 3978 O ASN B 96 6765 9206 6172 -1328 316 1834 D000 O ATOM 3979 CB ASN B 96 -10.612 7.371 54.534 1.00 67.72 D000 C ANISOU 3979 CB ASN B 96 8410 9716 7605 -981 -178 1568 D000 C ATOM 3980 CG ASN B 96 -10.498 8.632 53.703 1.00 75.89 D000 C ANISOU 3980 CG ASN B 96 9486 10321 9027 -1119 -391 1672 D000 C ATOM 3981 ND2 ASN B 96 -11.593 9.372 53.596 1.00 69.01 D000 N ANISOU 3981 ND2 ASN B 96 8796 9108 8318 -1019 -647 1687 D000 N ATOM 3982 OD1 ASN B 96 -9.437 8.932 53.153 1.00 70.14 D000 O ANISOU 3982 OD1 ASN B 96 8619 9563 8468 -1296 -353 1711 D000 O ATOM 3983 N LEU B 97 -7.465 6.274 53.154 1.00 58.68 D000 N ANISOU 3983 N LEU B 97 6670 9003 6623 -1146 231 1330 D000 N ATOM 3984 CA LEU B 97 -6.029 6.458 53.283 1.00 71.54 D000 C ANISOU 3984 CA LEU B 97 8011 10878 8294 -1359 389 1493 D000 C ATOM 3985 C LEU B 97 -5.631 7.927 53.247 1.00 65.40 D000 C ANISOU 3985 C LEU B 97 7223 9852 7775 -1715 240 1853 D000 C ATOM 3986 O LEU B 97 -4.550 8.273 53.735 1.00 65.36 D000 O ANISOU 3986 O LEU B 97 6971 10096 7766 -1983 389 2128 D000 O ATOM 3987 CB LEU B 97 -5.308 5.682 52.184 1.00 71.12 D000 C ANISOU 3987 CB LEU B 97 7765 10858 8399 -1233 402 1190 D000 C ATOM 3988 CG LEU B 97 -4.830 4.292 52.619 1.00 77.35 D000 C ANISOU 3988 CG LEU B 97 8391 12059 8941 -998 640 976 D000 C ATOM 3989 CD1 LEU B 97 -4.752 3.384 51.388 1.00 76.47 D000 C ANISOU 3989 CD1 LEU B 97 8263 11809 8985 -776 533 636 D000 C ATOM 3990 CD2 LEU B 97 -3.519 4.329 53.361 1.00 92.61 D000 C ANISOU 3990 CD2 LEU B 97 9973 14439 10776 -1137 898 1151 D000 C ATOM 3991 N ASP B 98 -6.476 8.803 52.689 1.00 62.29 D000 N ANISOU 3991 N ASP B 98 7076 8970 7621 -1726 -58 1855 D000 N ATOM 3992 CA ASP B 98 -6.193 10.234 52.769 1.00 69.23 D000 C ANISOU 3992 CA ASP B 98 8007 9527 8771 -2059 -261 2206 D000 C ATOM 3993 C ASP B 98 -6.058 10.685 54.216 1.00 69.41 D000 C ANISOU 3993 C ASP B 98 8044 9771 8557 -2293 -135 2686 D000 C ATOM 3994 O ASP B 98 -5.246 11.565 54.523 1.00 76.22 D000 O ANISOU 3994 O ASP B 98 8795 10597 9567 -2677 -157 3080 D000 O ATOM 3995 CB ASP B 98 -7.290 11.051 52.077 1.00 65.97 D000 C ANISOU 3995 CB ASP B 98 7896 8551 8620 -1938 -613 2081 D000 C ATOM 3996 CG ASP B 98 -7.366 10.798 50.576 1.00 69.47 D000 C ANISOU 3996 CG ASP B 98 8340 8790 9266 -1747 -742 1641 D000 C ATOM 3997 OD1 ASP B 98 -6.305 10.724 49.918 1.00 67.66 D000 O ANISOU 3997 OD1 ASP B 98 7913 8616 9178 -1883 -739 1572 D000 O ATOM 3998 OD2 ASP B 98 -8.495 10.707 50.050 1.00 76.46 D000 O ANISOU 3998 OD2 ASP B 98 9413 9480 10159 -1465 -855 1377 D000 O ATOM 3999 N GLU B 99 -6.833 10.083 55.117 1.00 80.23 D000 N ANISOU 3999 N GLU B 99 9551 11386 9547 -2088 -15 2676 D000 N ATOM 4000 CA GLU B 99 -6.890 10.496 56.513 1.00 89.99 D000 C ANISOU 4000 CA GLU B 99 10874 12848 10471 -2265 72 3125 D000 C ATOM 4001 C GLU B 99 -5.895 9.760 57.400 1.00 78.75 D000 C ANISOU 4001 C GLU B 99 9179 12100 8641 -2341 487 3232 D000 C ATOM 4002 O GLU B 99 -5.751 10.123 58.573 1.00 81.02 D000 O ANISOU 4002 O GLU B 99 9506 12673 8605 -2531 615 3647 D000 O ATOM 4003 CB GLU B 99 -8.305 10.273 57.053 1.00 94.25 D000 C ANISOU 4003 CB GLU B 99 11716 13306 10790 -1988 -71 3040 D000 C ATOM 4004 CG GLU B 99 -9.348 11.182 56.430 1.00 96.42 D000 C ANISOU 4004 CG GLU B 99 12239 12960 11436 -1907 -473 3010 D000 C ATOM 4005 CD GLU B 99 -10.718 11.010 57.054 1.00112.01 D000 C ANISOU 4005 CD GLU B 99 14447 14897 13214 -1650 -628 2967 D000 C ATOM 4006 OE1 GLU B 99 -11.576 11.897 56.856 1.00106.13 D000 O ANISOU 4006 OE1 GLU B 99 13898 13692 12735 -1585 -964 3036 D000 O ATOM 4007 OE2 GLU B 99 -10.937 9.985 57.735 1.00111.72 D000 O ANISOU 4007 OE2 GLU B 99 14390 15281 12778 -1494 -443 2837 D000 O ATOM 4008 N ASN B 100 -5.208 8.749 56.879 1.00 83.69 D000 N ANISOU 4008 N ASN B 100 10915 14604 6278 1618 -1195 1798 D000 N ATOM 4009 CA ASN B 100 -4.285 7.951 57.674 1.00 80.72 D000 C ANISOU 4009 CA ASN B 100 10677 14374 5619 1494 -1015 1677 D000 C ATOM 4010 C ASN B 100 -2.914 8.616 57.704 1.00 78.41 D000 C ANISOU 4010 C ASN B 100 10571 13860 5360 1406 -631 1925 D000 C ATOM 4011 O ASN B 100 -2.419 9.094 56.679 1.00 89.17 D000 O ANISOU 4011 O ASN B 100 11851 14913 7115 1310 -464 1996 D000 O ATOM 4012 CB ASN B 100 -4.185 6.538 57.092 1.00 81.46 D000 C ANISOU 4012 CB ASN B 100 10565 14483 5903 1292 -1012 1252 D000 C ATOM 4013 CG ASN B 100 -3.247 5.645 57.875 1.00 82.24 D000 C ANISOU 4013 CG ASN B 100 10791 14720 5735 1191 -830 1081 D000 C ATOM 4014 ND2 ASN B 100 -3.814 4.737 58.660 1.00 79.61 D000 N ANISOU 4014 ND2 ASN B 100 10464 14683 5102 1206 -1026 824 D000 N ATOM 4015 OD1 ASN B 100 -2.026 5.763 57.770 1.00 87.44 D000 O ANISOU 4015 OD1 ASN B 100 11527 15232 6466 1099 -516 1155 D000 O ATOM 4016 N THR B 101 -2.304 8.643 58.892 1.00 84.90 D000 N ANISOU 4016 N THR B 101 11640 14858 5759 1426 -484 2040 D000 N ATOM 4017 CA THR B 101 -0.983 9.232 59.087 1.00 89.62 D000 C ANISOU 4017 CA THR B 101 12409 15297 6345 1313 -84 2259 D000 C ATOM 4018 C THR B 101 -0.086 8.312 59.908 1.00 84.27 D000 C ANISOU 4018 C THR B 101 11803 14841 5374 1206 129 2063 D000 C ATOM 4019 O THR B 101 0.770 8.780 60.664 1.00 91.45 D000 O ANISOU 4019 O THR B 101 12929 15784 6035 1167 423 2268 D000 O ATOM 4020 CB THR B 101 -1.080 10.602 59.765 1.00 80.92 D000 C ANISOU 4020 CB THR B 101 11616 14129 5003 1461 -34 2722 D000 C ATOM 4021 CG2 THR B 101 -1.381 11.692 58.740 1.00 93.99 D000 C ANISOU 4021 CG2 THR B 101 13214 15420 7075 1501 -61 2935 D000 C ATOM 4022 OG1 THR B 101 -2.109 10.578 60.763 1.00 92.37 D000 O ANISOU 4022 OG1 THR B 101 13193 15755 6148 1639 -348 2711 D000 O ATOM 4023 N AASP B 102 -0.262 7.003 59.778 0.81 83.90 D000 N ANISOU 4023 N AASP B 102 11587 14938 5352 1152 7 1661 D000 N ATOM 4024 N BASP B 102 -0.291 7.005 59.788 0.19 83.96 D000 N ANISOU 4024 N BASP B 102 11596 14949 5355 1155 -1 1662 D000 N ATOM 4025 CA AASP B 102 0.649 6.076 60.434 0.81 86.93 D000 C ANISOU 4025 CA AASP B 102 12018 15493 5517 1061 226 1429 D000 C ATOM 4026 CA BASP B 102 0.528 6.031 60.494 0.19 86.52 D000 C ANISOU 4026 CA BASP B 102 11971 15467 5436 1074 190 1417 D000 C ATOM 4027 C AASP B 102 1.996 6.077 59.716 0.81 87.50 D000 C ANISOU 4027 C AASP B 102 11968 15336 5943 895 585 1393 D000 C ATOM 4028 C BASP B 102 1.937 6.025 59.912 0.19 87.31 D000 C ANISOU 4028 C BASP B 102 11973 15361 5839 910 572 1388 D000 C ATOM 4029 O AASP B 102 2.062 6.065 58.482 0.81 79.00 D000 O ANISOU 4029 O AASP B 102 10682 14004 5329 824 558 1323 D000 O ATOM 4030 O BASP B 102 2.111 6.051 58.693 0.19 80.54 D000 O ANISOU 4030 O BASP B 102 10910 14241 5450 830 578 1330 D000 O ATOM 4031 CB AASP B 102 0.054 4.670 60.457 0.81 84.95 D000 C ANISOU 4031 CB AASP B 102 11643 15410 5225 1052 -13 995 D000 C ATOM 4032 CB BASP B 102 -0.087 4.634 60.399 0.19 84.54 D000 C ANISOU 4032 CB BASP B 102 11575 15358 5189 1057 -54 980 D000 C ATOM 4033 CG AASP B 102 0.979 3.659 61.108 0.81 87.63 D000 C ANISOU 4033 CG AASP B 102 12037 15902 5355 985 208 718 D000 C ATOM 4034 CG BASP B 102 -1.333 4.484 61.251 0.19 80.85 D000 C ANISOU 4034 CG BASP B 102 11188 15114 4417 1177 -407 922 D000 C ATOM 4035 OD1AASP B 102 1.879 3.139 60.413 0.81 90.91 D000 O ANISOU 4035 OD1AASP B 102 12309 16142 6091 878 413 544 D000 O ATOM 4036 OD1BASP B 102 -1.568 5.341 62.127 0.19 80.78 D000 O ANISOU 4036 OD1BASP B 102 11390 15135 4170 1282 -440 1191 D000 O ATOM 4037 OD2AASP B 102 0.812 3.390 62.312 0.81 99.99 D000 O ANISOU 4037 OD2AASP B 102 13785 17654 6553 1028 166 650 D000 O ATOM 4038 OD2BASP B 102 -2.078 3.504 61.043 0.19 81.89 D000 O ANISOU 4038 OD2BASP B 102 11173 15322 4620 1141 -649 587 D000 O ATOM 4039 N APHE B 103 3.076 6.092 60.505 0.48 87.24 D000 N ANISOU 4039 N APHE B 103 12054 15418 5674 835 923 1428 D000 N ATOM 4040 N CPHE B 103 2.900 6.529 59.665 0.52 89.12 D000 N ANISOU 4040 N CPHE B 103 12187 15444 6229 813 862 1513 D000 N ATOM 4041 CA APHE B 103 4.413 6.270 59.942 0.48 89.99 D000 C ANISOU 4041 CA APHE B 103 12265 15589 6338 681 1282 1421 D000 C ATOM 4042 CA CPHE B 103 4.323 6.296 59.893 0.52 89.95 D000 C ANISOU 4042 CA CPHE B 103 12258 15573 6345 687 1256 1428 D000 C ATOM 4043 C APHE B 103 4.737 5.199 58.909 0.48 86.62 D000 C ANISOU 4043 C APHE B 103 11560 15043 6307 630 1228 1048 D000 C ATOM 4044 C CPHE B 103 4.808 5.185 58.961 0.52 86.62 D000 C ANISOU 4044 C CPHE B 103 11564 15054 6293 627 1249 1044 D000 C ATOM 4045 O APHE B 103 5.395 5.477 57.899 0.48 80.97 D000 O ANISOU 4045 O APHE B 103 10661 14095 6008 538 1345 1052 D000 O ATOM 4046 O CPHE B 103 5.630 5.428 58.077 0.52 80.93 D000 O ANISOU 4046 O CPHE B 103 10664 14128 5959 528 1415 1039 D000 O ATOM 4047 CB APHE B 103 5.459 6.251 61.057 0.48 96.16 D000 C ANISOU 4047 CB APHE B 103 13187 16581 6767 626 1660 1445 D000 C ATOM 4048 CB CPHE B 103 4.573 5.956 61.366 0.52 95.89 D000 C ANISOU 4048 CB CPHE B 103 13237 16660 6535 733 1398 1402 D000 C ATOM 4049 CG APHE B 103 5.919 4.866 61.436 0.48100.19 D000 C ANISOU 4049 CG APHE B 103 13614 17298 7154 640 1717 1026 D000 C ATOM 4050 CG CPHE B 103 5.996 5.571 61.682 0.52102.11 D000 C ANISOU 4050 CG CPHE B 103 13958 17528 7310 619 1815 1251 D000 C ATOM 4051 CD1APHE B 103 5.198 4.102 62.342 0.48101.95 D000 C ANISOU 4051 CD1APHE B 103 13996 17785 6955 752 1515 850 D000 C ATOM 4052 CD1CPHE B 103 7.005 6.523 61.696 0.52100.78 D000 C ANISOU 4052 CD1CPHE B 103 13797 17258 7238 481 2197 1498 D000 C ATOM 4053 CD2APHE B 103 7.068 4.325 60.879 0.48 97.16 D000 C ANISOU 4053 CD2APHE B 103 12993 16836 7088 555 1957 786 D000 C ATOM 4054 CD2CPHE B 103 6.315 4.261 62.004 0.52105.42 D000 C ANISOU 4054 CD2CPHE B 103 14305 18129 7620 650 1834 847 D000 C ATOM 4055 CE1APHE B 103 5.619 2.829 62.690 0.48100.53 D000 C ANISOU 4055 CE1APHE B 103 13765 17726 6706 760 1568 441 D000 C ATOM 4056 CE1CPHE B 103 8.310 6.168 61.997 0.52 93.21 D000 C ANISOU 4056 CE1CPHE B 103 12725 16409 6280 373 2593 1333 D000 C ATOM 4057 CE2APHE B 103 7.492 3.052 61.221 0.48 98.96 D000 C ANISOU 4057 CE2APHE B 103 13160 17224 7216 603 2008 395 D000 C ATOM 4058 CE2CPHE B 103 7.618 3.903 62.310 0.52102.09 D000 C ANISOU 4058 CE2CPHE B 103 13795 17801 7193 579 2220 686 D000 C ATOM 4059 CZ APHE B 103 6.767 2.304 62.127 0.48101.16 D000 C ANISOU 4059 CZ APHE B 103 13625 17739 7073 704 1829 223 D000 C ATOM 4060 CZ CPHE B 103 8.615 4.858 62.308 0.52 92.49 D000 C ANISOU 4060 CZ CPHE B 103 12542 16518 6082 440 2601 925 D000 C ATOM 4061 N LEU B 104 4.287 3.970 59.143 1.00 85.09 D000 N ANISOU 4061 N LEU B 104 11351 14996 5982 689 1043 720 D000 N ATOM 4062 CA LEU B 104 4.608 2.878 58.233 1.00 84.42 D000 C ANISOU 4062 CA LEU B 104 11065 14775 6238 657 1000 377 D000 C ATOM 4063 C LEU B 104 3.680 2.869 57.027 1.00 77.05 D000 C ANISOU 4063 C LEU B 104 10011 13614 5650 649 710 368 D000 C ATOM 4064 O LEU B 104 4.085 2.429 55.945 1.00 78.87 D000 O ANISOU 4064 O LEU B 104 10081 13635 6250 606 717 221 D000 O ATOM 4065 CB LEU B 104 4.537 1.535 58.962 1.00 91.59 D000 C ANISOU 4065 CB LEU B 104 12038 15882 6881 708 947 16 D000 C ATOM 4066 CG LEU B 104 4.728 0.291 58.090 1.00 87.52 D000 C ANISOU 4066 CG LEU B 104 11379 15192 6682 701 870 -342 D000 C ATOM 4067 CD1 LEU B 104 5.485 -0.780 58.864 1.00 96.34 D000 C ANISOU 4067 CD1 LEU B 104 12546 16464 7593 751 1038 -665 D000 C ATOM 4068 CD2 LEU B 104 3.399 -0.263 57.601 1.00100.23 D000 C ANISOU 4068 CD2 LEU B 104 12989 16723 8373 689 515 -467 D000 C ATOM 4069 N ILE B 105 2.443 3.347 57.191 1.00 79.58 D000 N ANISOU 4069 N ILE B 105 10405 13987 5845 702 456 518 D000 N ATOM 4070 CA ILE B 105 1.534 3.472 56.056 1.00 71.70 D000 C ANISOU 4070 CA ILE B 105 9277 12793 5173 690 219 525 D000 C ATOM 4071 C ILE B 105 2.043 4.515 55.070 1.00 62.39 D000 C ANISOU 4071 C ILE B 105 8011 11349 4346 643 350 756 D000 C ATOM 4072 O ILE B 105 1.803 4.405 53.867 1.00 60.18 D000 O ANISOU 4072 O ILE B 105 7593 10859 4413 602 256 686 D000 O ATOM 4073 CB ILE B 105 0.115 3.838 56.529 1.00 74.42 D000 C ANISOU 4073 CB ILE B 105 9681 13293 5302 783 -76 627 D000 C ATOM 4074 CG1 ILE B 105 -0.532 2.733 57.365 1.00 84.58 D000 C ANISOU 4074 CG1 ILE B 105 11016 14842 6278 802 -262 337 D000 C ATOM 4075 CG2 ILE B 105 -0.811 4.072 55.337 1.00 71.14 D000 C ANISOU 4075 CG2 ILE B 105 9103 12688 5237 769 -278 638 D000 C ATOM 4076 CD1 ILE B 105 -0.278 1.364 56.871 1.00 84.68 D000 C ANISOU 4076 CD1 ILE B 105 10946 14764 6464 702 -253 -38 D000 C ATOM 4077 N ARG B 106 2.722 5.552 55.556 1.00 63.11 D000 N ANISOU 4077 N ARG B 106 8196 11438 4344 634 574 1029 D000 N ATOM 4078 CA ARG B 106 3.095 6.680 54.700 1.00 65.08 D000 C ANISOU 4078 CA ARG B 106 8386 11426 4915 574 684 1256 D000 C ATOM 4079 C ARG B 106 3.824 6.248 53.434 1.00 59.66 D000 C ANISOU 4079 C ARG B 106 7490 10536 4641 482 745 1061 D000 C ATOM 4080 O ARG B 106 3.371 6.607 52.336 1.00 57.46 D000 O ANISOU 4080 O ARG B 106 7125 10052 4657 470 617 1091 D000 O ATOM 4081 CB ARG B 106 3.909 7.663 55.560 1.00 70.70 D000 C ANISOU 4081 CB ARG B 106 9252 12173 5440 531 979 1534 D000 C ATOM 4082 CG ARG B 106 5.022 8.426 54.844 1.00 94.02 D000 C ANISOU 4082 CG ARG B 106 12097 14895 8731 382 1245 1629 D000 C ATOM 4083 CD ARG B 106 4.483 9.633 54.088 1.00 96.59 D000 C ANISOU 4083 CD ARG B 106 12452 14948 9301 382 1159 1876 D000 C ATOM 4084 NE ARG B 106 4.303 10.781 54.968 1.00103.01 D000 N ANISOU 4084 NE ARG B 106 13527 15740 9873 414 1265 2243 D000 N ATOM 4085 CZ ARG B 106 5.295 11.468 55.517 1.00 99.33 D000 C ANISOU 4085 CZ ARG B 106 13166 15237 9338 278 1608 2427 D000 C ATOM 4086 NH1 ARG B 106 6.560 11.154 55.294 1.00 96.56 D000 N ANISOU 4086 NH1 ARG B 106 12632 14899 9158 102 1877 2256 D000 N ATOM 4087 NH2 ARG B 106 5.011 12.494 56.315 1.00104.54 D000 N ANISOU 4087 NH2 ARG B 106 14123 15848 9751 323 1686 2791 D000 N ATOM 4088 N PRO B 107 4.919 5.485 53.493 1.00 59.19 D000 N ANISOU 4088 N PRO B 107 7343 10530 4616 436 921 851 D000 N ATOM 4089 CA PRO B 107 5.594 5.108 52.238 1.00 60.30 D000 C ANISOU 4089 CA PRO B 107 7289 10480 5141 389 934 676 D000 C ATOM 4090 C PRO B 107 4.749 4.215 51.342 1.00 58.57 D000 C ANISOU 4090 C PRO B 107 7032 10157 5065 430 665 484 D000 C ATOM 4091 O PRO B 107 4.825 4.332 50.109 1.00 54.64 D000 O ANISOU 4091 O PRO B 107 6432 9453 4877 401 602 458 D000 O ATOM 4092 CB PRO B 107 6.869 4.397 52.726 1.00 57.55 D000 C ANISOU 4092 CB PRO B 107 6861 10266 4739 384 1162 477 D000 C ATOM 4093 CG PRO B 107 6.529 3.924 54.115 1.00 67.24 D000 C ANISOU 4093 CG PRO B 107 8260 11753 5536 443 1187 443 D000 C ATOM 4094 CD PRO B 107 5.636 4.991 54.682 1.00 69.16 D000 C ANISOU 4094 CD PRO B 107 8676 12033 5568 446 1123 762 D000 C ATOM 4095 N ILE B 108 3.930 3.333 51.916 1.00 53.93 D000 N ANISOU 4095 N ILE B 108 6534 9705 4252 482 512 342 D000 N ATOM 4096 CA ILE B 108 3.068 2.503 51.080 1.00 54.23 D000 C ANISOU 4096 CA ILE B 108 6548 9629 4429 478 287 166 D000 C ATOM 4097 C ILE B 108 2.044 3.372 50.352 1.00 52.60 D000 C ANISOU 4097 C ILE B 108 6310 9307 4370 461 138 345 D000 C ATOM 4098 O ILE B 108 1.757 3.156 49.166 1.00 52.09 D000 O ANISOU 4098 O ILE B 108 6178 9057 4556 425 51 276 D000 O ATOM 4099 CB ILE B 108 2.394 1.409 51.931 1.00 63.48 D000 C ANISOU 4099 CB ILE B 108 7815 10974 5329 500 166 -46 D000 C ATOM 4100 CG1 ILE B 108 3.442 0.661 52.762 1.00 63.60 D000 C ANISOU 4100 CG1 ILE B 108 7877 11115 5174 540 342 -224 D000 C ATOM 4101 CG2 ILE B 108 1.640 0.424 51.028 1.00 61.28 D000 C ANISOU 4101 CG2 ILE B 108 7519 10542 5224 450 -14 -255 D000 C ATOM 4102 CD1 ILE B 108 2.865 -0.255 53.826 1.00 68.80 D000 C ANISOU 4102 CD1 ILE B 108 8659 11976 5505 561 250 -430 D000 C ATOM 4103 N LYS B 109 1.495 4.379 51.037 1.00 58.11 D000 N ANISOU 4103 N LYS B 109 7068 10107 4904 503 115 581 D000 N ATOM 4104 CA LYS B 109 0.564 5.305 50.395 1.00 54.73 D000 C ANISOU 4104 CA LYS B 109 6603 9567 4624 526 -13 752 D000 C ATOM 4105 C LYS B 109 1.182 5.960 49.171 1.00 53.08 D000 C ANISOU 4105 C LYS B 109 6314 9098 4758 470 85 822 D000 C ATOM 4106 O LYS B 109 0.541 6.074 48.122 1.00 52.04 D000 O ANISOU 4106 O LYS B 109 6114 8823 4837 458 -26 794 D000 O ATOM 4107 CB LYS B 109 0.127 6.391 51.374 1.00 58.99 D000 C ANISOU 4107 CB LYS B 109 7255 10225 4935 622 -27 1028 D000 C ATOM 4108 CG LYS B 109 -1.340 6.447 51.617 1.00 73.98 D000 C ANISOU 4108 CG LYS B 109 9139 12251 6717 719 -289 1039 D000 C ATOM 4109 CD LYS B 109 -1.653 7.307 52.842 1.00 72.23 D000 C ANISOU 4109 CD LYS B 109 9077 12196 6172 859 -323 1297 D000 C ATOM 4110 CE LYS B 109 -1.580 8.799 52.539 1.00 68.06 D000 C ANISOU 4110 CE LYS B 109 8618 11457 5785 924 -246 1623 D000 C ATOM 4111 NZ LYS B 109 -1.975 9.622 53.730 1.00 73.36 D000 N ANISOU 4111 NZ LYS B 109 9492 12264 6117 1092 -302 1904 D000 N ATOM 4112 N VAL B 110 2.422 6.433 49.303 1.00 55.25 D000 N ANISOU 4112 N VAL B 110 6588 9322 5083 426 302 902 D000 N ATOM 4113 CA VAL B 110 3.078 7.135 48.202 1.00 52.42 D000 C ANISOU 4113 CA VAL B 110 6141 8734 5041 358 389 951 D000 C ATOM 4114 C VAL B 110 3.267 6.214 47.009 1.00 48.50 D000 C ANISOU 4114 C VAL B 110 5545 8126 4755 334 305 713 D000 C ATOM 4115 O VAL B 110 3.014 6.600 45.859 1.00 52.23 D000 O ANISOU 4115 O VAL B 110 5971 8421 5452 311 238 718 D000 O ATOM 4116 CB VAL B 110 4.421 7.718 48.672 1.00 55.65 D000 C ANISOU 4116 CB VAL B 110 6535 9148 5461 282 651 1041 D000 C ATOM 4117 CG1 VAL B 110 5.048 8.550 47.567 1.00 58.43 D000 C ANISOU 4117 CG1 VAL B 110 6785 9271 6145 191 723 1076 D000 C ATOM 4118 CG2 VAL B 110 4.216 8.564 49.904 1.00 61.67 D000 C ANISOU 4118 CG2 VAL B 110 7459 10009 5966 303 753 1302 D000 C ATOM 4119 N ALEU B 111 3.725 4.986 47.259 0.73 54.00 D000 N ANISOU 4119 N ALEU B 111 6234 8915 5368 351 312 502 D000 N ATOM 4120 N BLEU B 111 3.710 4.983 47.246 0.27 53.90 D000 N ANISOU 4120 N BLEU B 111 6222 8901 5357 351 309 501 D000 N ATOM 4121 CA ALEU B 111 3.928 4.034 46.174 0.73 51.55 D000 C ANISOU 4121 CA ALEU B 111 5882 8477 5228 355 227 295 D000 C ATOM 4122 CA BLEU B 111 3.920 4.082 46.119 0.27 51.66 D000 C ANISOU 4122 CA BLEU B 111 5893 8481 5253 353 225 301 D000 C ATOM 4123 C ALEU B 111 2.607 3.703 45.494 0.73 52.39 D000 C ANISOU 4123 C ALEU B 111 6035 8503 5367 341 45 259 D000 C ATOM 4124 C BLEU B 111 2.598 3.688 45.477 0.27 52.33 D000 C ANISOU 4124 C BLEU B 111 6028 8493 5361 341 43 256 D000 C ATOM 4125 O ALEU B 111 2.509 3.711 44.263 0.73 50.53 D000 O ANISOU 4125 O ALEU B 111 5778 8097 5324 318 -12 226 D000 O ATOM 4126 O BLEU B 111 2.493 3.636 44.247 0.27 50.66 D000 O ANISOU 4126 O BLEU B 111 5798 8111 5338 319 -17 215 D000 O ATOM 4127 CB ALEU B 111 4.581 2.757 46.705 0.73 54.14 D000 C ANISOU 4127 CB ALEU B 111 6229 8898 5442 406 266 78 D000 C ATOM 4128 CB BLEU B 111 4.679 2.843 46.565 0.27 54.10 D000 C ANISOU 4128 CB BLEU B 111 6210 8872 5472 403 272 86 D000 C ATOM 4129 CG ALEU B 111 6.099 2.622 46.615 0.73 58.23 D000 C ANISOU 4129 CG ALEU B 111 6632 9423 6069 440 413 -15 D000 C ATOM 4130 CG BLEU B 111 6.121 3.097 46.980 0.27 56.32 D000 C ANISOU 4130 CG BLEU B 111 6384 9232 5784 415 472 70 D000 C ATOM 4131 CD1ALEU B 111 6.609 2.884 45.199 0.73 59.51 D000 C ANISOU 4131 CD1ALEU B 111 6696 9398 6517 435 359 -38 D000 C ATOM 4132 CD1BLEU B 111 6.646 1.799 47.492 0.27 60.71 D000 C ANISOU 4132 CD1BLEU B 111 6960 9878 6229 502 499 -165 D000 C ATOM 4133 CD2ALEU B 111 6.781 3.540 47.625 0.73 59.40 D000 C ANISOU 4133 CD2ALEU B 111 6726 9725 6120 395 630 127 D000 C ATOM 4134 CD2BLEU B 111 6.986 3.607 45.846 0.27 55.59 D000 C ANISOU 4134 CD2BLEU B 111 6148 8995 5980 391 496 66 D000 C ATOM 4135 N LEU B 112 1.578 3.399 46.288 1.00 49.85 D000 N ANISOU 4135 N LEU B 112 5769 8323 4849 348 -44 250 D000 N ATOM 4136 CA LEU B 112 0.293 3.016 45.716 1.00 49.76 D000 C ANISOU 4136 CA LEU B 112 5760 8271 4876 308 -197 182 D000 C ATOM 4137 C LEU B 112 -0.265 4.137 44.852 1.00 50.48 D000 C ANISOU 4137 C LEU B 112 5789 8249 5143 305 -225 334 D000 C ATOM 4138 O LEU B 112 -0.796 3.889 43.758 1.00 50.24 D000 O ANISOU 4138 O LEU B 112 5742 8091 5256 256 -280 262 D000 O ATOM 4139 CB LEU B 112 -0.683 2.633 46.823 1.00 47.50 D000 C ANISOU 4139 CB LEU B 112 5498 8201 4349 314 -300 132 D000 C ATOM 4140 CG LEU B 112 -2.063 2.162 46.368 1.00 55.55 D000 C ANISOU 4140 CG LEU B 112 6472 9225 5408 242 -448 21 D000 C ATOM 4141 CD1 LEU B 112 -1.899 0.912 45.542 1.00 59.32 D000 C ANISOU 4141 CD1 LEU B 112 7015 9532 5992 147 -437 -187 D000 C ATOM 4142 CD2 LEU B 112 -2.944 1.887 47.569 1.00 58.02 D000 C ANISOU 4142 CD2 LEU B 112 6774 9796 5475 253 -573 -44 D000 C ATOM 4143 N GLN B 113 -0.129 5.384 45.307 1.00 48.50 D000 N ANISOU 4143 N GLN B 113 5525 8023 4878 357 -170 545 D000 N ATOM 4144 CA GLN B 113 -0.623 6.504 44.517 1.00 48.97 D000 C ANISOU 4144 CA GLN B 113 5543 7946 5115 374 -189 678 D000 C ATOM 4145 C GLN B 113 0.176 6.659 43.231 1.00 51.99 D000 C ANISOU 4145 C GLN B 113 5903 8119 5734 319 -123 629 D000 C ATOM 4146 O GLN B 113 -0.403 6.899 42.165 1.00 52.12 D000 O ANISOU 4146 O GLN B 113 5893 8014 5895 304 -172 602 D000 O ATOM 4147 CB GLN B 113 -0.568 7.794 45.330 1.00 57.07 D000 C ANISOU 4147 CB GLN B 113 6612 8998 6075 448 -133 926 D000 C ATOM 4148 CG GLN B 113 -0.799 9.046 44.502 1.00 67.69 D000 C ANISOU 4148 CG GLN B 113 7941 10142 7635 472 -116 1058 D000 C ATOM 4149 CD GLN B 113 -1.576 10.102 45.252 1.00 86.32 D000 C ANISOU 4149 CD GLN B 113 10357 12536 9905 604 -165 1280 D000 C ATOM 4150 NE2 GLN B 113 -1.172 10.370 46.488 1.00 84.88 D000 N ANISOU 4150 NE2 GLN B 113 10283 12458 9507 642 -101 1437 D000 N ATOM 4151 OE1 GLN B 113 -2.533 10.669 44.730 1.00103.11 D000 O ANISOU 4151 OE1 GLN B 113 12439 14596 12141 687 -256 1311 D000 O ATOM 4152 N THR B 114 1.505 6.513 43.314 1.00 49.00 D000 N ANISOU 4152 N THR B 114 5519 7716 5384 293 -15 597 D000 N ATOM 4153 CA THR B 114 2.355 6.655 42.134 1.00 50.72 D000 C ANISOU 4153 CA THR B 114 5693 7768 5811 255 16 529 D000 C ATOM 4154 C THR B 114 2.062 5.560 41.114 1.00 48.57 D000 C ANISOU 4154 C THR B 114 5456 7423 5574 250 -87 353 D000 C ATOM 4155 O THR B 114 1.953 5.829 39.911 1.00 46.72 D000 O ANISOU 4155 O THR B 114 5226 7048 5479 230 -124 327 D000 O ATOM 4156 CB THR B 114 3.828 6.621 42.558 1.00 50.94 D000 C ANISOU 4156 CB THR B 114 5660 7837 5856 238 143 498 D000 C ATOM 4157 CG2 THR B 114 4.760 6.640 41.357 1.00 50.17 D000 C ANISOU 4157 CG2 THR B 114 5485 7612 5965 216 132 385 D000 C ATOM 4158 OG1 THR B 114 4.128 7.757 43.382 1.00 52.71 D000 O ANISOU 4158 OG1 THR B 114 5878 8089 6061 204 279 685 D000 O ATOM 4159 N ALEU B 115 1.924 4.315 41.578 0.60 47.80 D000 N ANISOU 4159 N ALEU B 115 5414 7406 5342 262 -125 231 D000 N ATOM 4160 N BLEU B 115 1.922 4.318 41.584 0.41 47.89 D000 N ANISOU 4160 N BLEU B 115 5425 7418 5352 262 -125 232 D000 N ATOM 4161 CA ALEU B 115 1.624 3.213 40.670 0.60 48.43 D000 C ANISOU 4161 CA ALEU B 115 5581 7380 5442 244 -202 85 D000 C ATOM 4162 CA BLEU B 115 1.625 3.202 40.692 0.41 48.45 D000 C ANISOU 4162 CA BLEU B 115 5583 7384 5440 245 -202 84 D000 C ATOM 4163 C ALEU B 115 0.236 3.354 40.059 0.60 49.08 D000 C ANISOU 4163 C ALEU B 115 5680 7421 5546 180 -258 102 D000 C ATOM 4164 C BLEU B 115 0.240 3.335 40.072 0.41 49.05 D000 C ANISOU 4164 C BLEU B 115 5678 7418 5540 180 -258 100 D000 C ATOM 4165 O ALEU B 115 0.032 3.035 38.879 0.60 45.45 D000 O ANISOU 4165 O ALEU B 115 5288 6823 5159 145 -282 45 D000 O ATOM 4166 O BLEU B 115 0.044 3.007 38.895 0.41 45.50 D000 O ANISOU 4166 O BLEU B 115 5295 6829 5163 145 -282 43 D000 O ATOM 4167 CB ALEU B 115 1.733 1.884 41.412 0.60 48.76 D000 C ANISOU 4167 CB ALEU B 115 5700 7486 5339 261 -216 -55 D000 C ATOM 4168 CB BLEU B 115 1.737 1.892 41.469 0.41 48.82 D000 C ANISOU 4168 CB BLEU B 115 5706 7502 5342 262 -214 -53 D000 C ATOM 4169 CG ALEU B 115 3.099 1.207 41.366 0.60 55.52 D000 C ANISOU 4169 CG ALEU B 115 6572 8302 6220 351 -186 -164 D000 C ATOM 4170 CG BLEU B 115 1.999 0.605 40.693 0.41 48.95 D000 C ANISOU 4170 CG BLEU B 115 5857 7362 5379 278 -261 -208 D000 C ATOM 4171 CD1ALEU B 115 3.225 0.183 42.476 0.60 58.56 D000 C ANISOU 4171 CD1ALEU B 115 7016 8789 6444 386 -165 -289 D000 C ATOM 4172 CD1BLEU B 115 3.384 0.603 40.076 0.41 54.41 D000 C ANISOU 4172 CD1BLEU B 115 6525 7972 6178 384 -255 -241 D000 C ATOM 4173 CD2ALEU B 115 3.312 0.552 40.012 0.60 54.44 D000 C ANISOU 4173 CD2ALEU B 115 6539 7964 6180 379 -260 -244 D000 C ATOM 4174 CD2BLEU B 115 1.826 -0.584 41.623 0.41 52.19 D000 C ANISOU 4174 CD2BLEU B 115 6359 7828 5642 277 -267 -348 D000 C ATOM 4175 N THR B 116 -0.739 3.799 40.851 1.00 45.11 D000 N ANISOU 4175 N THR B 116 5117 7054 4968 173 -279 172 D000 N ATOM 4176 CA THR B 116 -2.097 3.919 40.331 1.00 44.42 D000 C ANISOU 4176 CA THR B 116 4992 6968 4917 120 -326 157 D000 C ATOM 4177 C THR B 116 -2.169 4.995 39.256 1.00 44.87 D000 C ANISOU 4177 C THR B 116 5015 6896 5138 139 -296 237 D000 C ATOM 4178 O THR B 116 -2.808 4.800 38.211 1.00 45.87 D000 O ANISOU 4178 O THR B 116 5159 6942 5329 80 -293 170 D000 O ATOM 4179 CB THR B 116 -3.072 4.215 41.463 1.00 51.47 D000 C ANISOU 4179 CB THR B 116 5795 8066 5695 150 -389 203 D000 C ATOM 4180 CG2 THR B 116 -4.502 4.298 40.926 1.00 51.32 D000 C ANISOU 4180 CG2 THR B 116 5677 8085 5738 101 -439 151 D000 C ATOM 4181 OG1 THR B 116 -3.019 3.162 42.434 1.00 49.04 D000 O ANISOU 4181 OG1 THR B 116 5532 7884 5217 120 -424 91 D000 O ATOM 4182 N GLU B 117 -1.526 6.137 39.501 1.00 45.17 D000 N ANISOU 4182 N GLU B 117 5017 6905 5238 206 -256 370 D000 N ATOM 4183 CA GLU B 117 -1.536 7.216 38.519 1.00 50.79 D000 C ANISOU 4183 CA GLU B 117 5711 7473 6114 220 -225 423 D000 C ATOM 4184 C GLU B 117 -0.949 6.735 37.199 1.00 48.55 D000 C ANISOU 4184 C GLU B 117 5499 7048 5899 170 -221 307 D000 C ATOM 4185 O GLU B 117 -1.499 7.002 36.128 1.00 46.44 D000 O ANISOU 4185 O GLU B 117 5250 6693 5701 150 -217 267 D000 O ATOM 4186 CB GLU B 117 -0.741 8.417 39.034 1.00 53.68 D000 C ANISOU 4186 CB GLU B 117 6059 7791 6545 263 -162 571 D000 C ATOM 4187 CG GLU B 117 -1.292 9.043 40.311 1.00 89.20 D000 C ANISOU 4187 CG GLU B 117 10542 12403 10948 341 -168 731 D000 C ATOM 4188 CD GLU B 117 -1.582 10.527 40.166 1.00125.16 D000 C ANISOU 4188 CD GLU B 117 15101 16825 15629 410 -136 881 D000 C ATOM 4189 OE1 GLU B 117 -0.909 11.188 39.348 1.00130.15 D000 O ANISOU 4189 OE1 GLU B 117 15750 17274 16426 364 -71 871 D000 O ATOM 4190 OE2 GLU B 117 -2.488 11.032 40.865 1.00120.02 D000 O ANISOU 4190 OE2 GLU B 117 14440 16247 14913 521 -188 998 D000 O ATOM 4191 N SER B 118 0.166 6.011 37.270 1.00 41.89 D000 N ANISOU 4191 N SER B 118 4700 6193 5022 170 -227 246 D000 N ATOM 4192 CA SER B 118 0.804 5.492 36.065 1.00 41.87 D000 C ANISOU 4192 CA SER B 118 4783 6070 5057 165 -261 143 D000 C ATOM 4193 C SER B 118 -0.078 4.461 35.376 1.00 43.91 D000 C ANISOU 4193 C SER B 118 5166 6283 5234 114 -284 62 D000 C ATOM 4194 O SER B 118 -0.284 4.513 34.156 1.00 42.88 D000 O ANISOU 4194 O SER B 118 5119 6048 5127 91 -287 26 D000 O ATOM 4195 CB SER B 118 2.156 4.893 36.445 1.00 43.60 D000 C ANISOU 4195 CB SER B 118 4994 6314 5258 217 -276 87 D000 C ATOM 4196 OG SER B 118 2.841 4.418 35.300 1.00 45.79 D000 O ANISOU 4196 OG SER B 118 5349 6486 5561 255 -346 -9 D000 O ATOM 4197 N HIS B 119 -0.625 3.523 36.154 1.00 45.53 D000 N ANISOU 4197 N HIS B 119 5398 6565 5336 78 -287 27 D000 N ATOM 4198 CA HIS B 119 -1.512 2.504 35.608 1.00 42.09 D000 C ANISOU 4198 CA HIS B 119 5083 6073 4835 -19 -279 -54 D000 C ATOM 4199 C HIS B 119 -2.669 3.132 34.844 1.00 43.77 D000 C ANISOU 4199 C HIS B 119 5246 6284 5100 -89 -229 -42 D000 C ATOM 4200 O HIS B 119 -3.009 2.695 33.737 1.00 43.76 D000 O ANISOU 4200 O HIS B 119 5375 6174 5079 -159 -188 -89 D000 O ATOM 4201 CB HIS B 119 -2.039 1.624 36.743 1.00 43.23 D000 C ANISOU 4201 CB HIS B 119 5217 6324 4882 -74 -289 -113 D000 C ATOM 4202 CG HIS B 119 -2.676 0.348 36.281 1.00 42.08 D000 C ANISOU 4202 CG HIS B 119 5232 6078 4679 -202 -266 -220 D000 C ATOM 4203 CD2 HIS B 119 -2.218 -0.925 36.292 1.00 45.76 D000 C ANISOU 4203 CD2 HIS B 119 5893 6418 5078 -213 -276 -303 D000 C ATOM 4204 ND1 HIS B 119 -3.943 0.294 35.741 1.00 42.49 D000 N ANISOU 4204 ND1 HIS B 119 5260 6136 4747 -347 -207 -254 D000 N ATOM 4205 CE1 HIS B 119 -4.239 -0.959 35.444 1.00 47.27 D000 C ANISOU 4205 CE1 HIS B 119 6048 6617 5296 -476 -168 -346 D000 C ATOM 4206 NE2 HIS B 119 -3.210 -1.719 35.771 1.00 46.65 D000 N ANISOU 4206 NE2 HIS B 119 6123 6438 5165 -388 -217 -371 D000 N ATOM 4207 N ARG B 120 -3.289 4.166 35.420 1.00 40.75 D000 N ANISOU 4207 N ARG B 120 4688 6020 4776 -57 -223 23 D000 N ATOM 4208 CA ARG B 120 -4.493 4.731 34.820 1.00 43.59 D000 C ANISOU 4208 CA ARG B 120 4960 6405 5197 -96 -173 9 D000 C ATOM 4209 C ARG B 120 -4.184 5.452 33.513 1.00 43.53 D000 C ANISOU 4209 C ARG B 120 5018 6258 5263 -70 -129 11 D000 C ATOM 4210 O ARG B 120 -5.054 5.534 32.639 1.00 47.94 D000 O ANISOU 4210 O ARG B 120 5577 6801 5837 -128 -54 -46 D000 O ATOM 4211 CB ARG B 120 -5.182 5.670 35.814 1.00 45.69 D000 C ANISOU 4211 CB ARG B 120 5031 6824 5504 -11 -208 83 D000 C ATOM 4212 CG ARG B 120 -5.592 4.965 37.099 1.00 49.87 D000 C ANISOU 4212 CG ARG B 120 5495 7529 5925 -35 -274 58 D000 C ATOM 4213 CD ARG B 120 -7.103 4.913 37.292 1.00 48.75 D000 C ANISOU 4213 CD ARG B 120 5176 7554 5794 -81 -292 -19 D000 C ATOM 4214 NE ARG B 120 -7.759 3.897 36.472 1.00 48.31 D000 N ANISOU 4214 NE ARG B 120 5157 7463 5738 -270 -214 -168 D000 N ATOM 4215 CZ ARG B 120 -9.068 3.682 36.445 1.00 49.98 D000 C ANISOU 4215 CZ ARG B 120 5193 7818 5980 -368 -194 -281 D000 C ATOM 4216 NH1 ARG B 120 -9.906 4.362 37.225 1.00 49.95 D000 N ANISOU 4216 NH1 ARG B 120 4947 8027 6005 -262 -286 -275 D000 N ATOM 4217 NH2 ARG B 120 -9.554 2.751 35.628 1.00 51.89 D000 N ANISOU 4217 NH2 ARG B 120 5503 7992 6222 -578 -78 -405 D000 N ATOM 4218 N ILE B 121 -2.958 5.952 33.356 1.00 40.96 D000 N ANISOU 4218 N ILE B 121 4740 5845 4978 6 -167 53 D000 N ATOM 4219 CA ILE B 121 -2.524 6.528 32.087 1.00 41.62 D000 C ANISOU 4219 CA ILE B 121 4903 5801 5110 22 -153 19 D000 C ATOM 4220 C ILE B 121 -2.279 5.428 31.060 1.00 44.03 D000 C ANISOU 4220 C ILE B 121 5415 6019 5295 -30 -161 -55 D000 C ATOM 4221 O ILE B 121 -2.739 5.513 29.915 1.00 45.89 D000 O ANISOU 4221 O ILE B 121 5747 6195 5493 -70 -105 -104 D000 O ATOM 4222 CB ILE B 121 -1.263 7.384 32.294 1.00 45.09 D000 C ANISOU 4222 CB ILE B 121 5299 6188 5643 91 -200 60 D000 C ATOM 4223 CG1 ILE B 121 -1.634 8.706 32.970 1.00 44.69 D000 C ANISOU 4223 CG1 ILE B 121 5114 6151 5716 138 -162 154 D000 C ATOM 4224 CG2 ILE B 121 -0.547 7.640 30.965 1.00 46.28 D000 C ANISOU 4224 CG2 ILE B 121 5551 6223 5809 97 -234 -22 D000 C ATOM 4225 CD1 ILE B 121 -0.454 9.345 33.697 1.00 51.14 D000 C ANISOU 4225 CD1 ILE B 121 5879 6943 6610 161 -170 227 D000 C ATOM 4226 N LEU B 122 -1.561 4.376 31.457 1.00 40.12 D000 N ANISOU 4226 N LEU B 122 5011 5509 4722 -17 -222 -62 D000 N ATOM 4227 CA LEU B 122 -1.265 3.284 30.534 1.00 43.24 D000 C ANISOU 4227 CA LEU B 122 5649 5788 4993 -31 -246 -108 D000 C ATOM 4228 C LEU B 122 -2.538 2.608 30.028 1.00 42.21 D000 C ANISOU 4228 C LEU B 122 5634 5627 4776 -176 -129 -132 D000 C ATOM 4229 O LEU B 122 -2.562 2.102 28.902 1.00 43.06 D000 O ANISOU 4229 O LEU B 122 5970 5618 4771 -208 -100 -147 D000 O ATOM 4230 CB LEU B 122 -0.351 2.257 31.205 1.00 43.94 D000 C ANISOU 4230 CB LEU B 122 5807 5855 5034 38 -329 -119 D000 C ATOM 4231 CG LEU B 122 1.075 2.689 31.558 1.00 50.35 D000 C ANISOU 4231 CG LEU B 122 6510 6701 5920 174 -428 -125 D000 C ATOM 4232 CD1 LEU B 122 1.792 1.520 32.245 1.00 54.49 D000 C ANISOU 4232 CD1 LEU B 122 7100 7214 6390 253 -482 -162 D000 C ATOM 4233 CD2 LEU B 122 1.826 3.164 30.335 1.00 49.23 D000 C ANISOU 4233 CD2 LEU B 122 6428 6492 5786 244 -510 -161 D000 C ATOM 4234 N GLU B 123 -3.604 2.585 30.836 1.00 40.16 D000 N ANISOU 4234 N GLU B 123 5219 5481 4558 -270 -59 -141 D000 N ATOM 4235 CA GLU B 123 -4.838 1.961 30.372 1.00 42.05 D000 C ANISOU 4235 CA GLU B 123 5517 5715 4744 -445 74 -193 D000 C ATOM 4236 C GLU B 123 -5.329 2.592 29.078 1.00 41.87 D000 C ANISOU 4236 C GLU B 123 5540 5660 4707 -475 180 -211 D000 C ATOM 4237 O GLU B 123 -5.931 1.906 28.244 1.00 43.43 D000 O ANISOU 4237 O GLU B 123 5910 5788 4804 -616 308 -242 D000 O ATOM 4238 CB GLU B 123 -5.939 2.083 31.424 1.00 44.13 D000 C ANISOU 4238 CB GLU B 123 5526 6159 5081 -523 106 -230 D000 C ATOM 4239 CG GLU B 123 -5.721 1.300 32.701 1.00 45.02 D000 C ANISOU 4239 CG GLU B 123 5613 6326 5166 -535 25 -248 D000 C ATOM 4240 CD GLU B 123 -6.619 1.809 33.806 1.00 47.49 D000 C ANISOU 4240 CD GLU B 123 5640 6864 5541 -539 -5 -270 D000 C ATOM 4241 OE1 GLU B 123 -7.767 2.189 33.487 1.00 47.64 D000 O ANISOU 4241 OE1 GLU B 123 5501 6981 5618 -613 71 -319 D000 O ATOM 4242 OE2 GLU B 123 -6.185 1.847 34.984 1.00 43.36 D000 O ANISOU 4242 OE2 GLU B 123 5045 6433 4997 -454 -106 -243 D000 O ATOM 4243 N LYS B 124 -5.121 3.899 28.913 1.00 41.07 D000 N ANISOU 4243 N LYS B 124 5301 5601 4702 -358 149 -199 D000 N ATOM 4244 CA ALYS B 124 -5.640 4.593 27.742 0.60 47.44 D000 C ANISOU 4244 CA ALYS B 124 6136 6391 5500 -374 258 -247 D000 C ATOM 4245 CA BLYS B 124 -5.636 4.596 27.742 0.40 47.43 D000 C ANISOU 4245 CA BLYS B 124 6134 6389 5499 -373 258 -247 D000 C ATOM 4246 C LYS B 124 -4.832 4.281 26.487 1.00 40.80 D000 C ANISOU 4246 C LYS B 124 5592 5406 4503 -350 232 -252 D000 C ATOM 4247 O LYS B 124 -5.316 4.531 25.374 1.00 42.88 D000 O ANISOU 4247 O LYS B 124 5959 5648 4684 -396 349 -303 D000 O ATOM 4248 CB ALYS B 124 -5.647 6.106 27.979 0.60 49.12 D000 C ANISOU 4248 CB ALYS B 124 6134 6654 5874 -246 229 -247 D000 C ATOM 4249 CB BLYS B 124 -5.630 6.110 27.976 0.40 49.15 D000 C ANISOU 4249 CB BLYS B 124 6140 6656 5878 -244 227 -246 D000 C ATOM 4250 CG ALYS B 124 -6.590 6.593 29.073 0.60 54.33 D000 C ANISOU 4250 CG ALYS B 124 6514 7461 6668 -222 245 -233 D000 C ATOM 4251 CG BLYS B 124 -6.415 6.596 29.191 0.40 54.54 D000 C ANISOU 4251 CG BLYS B 124 6546 7482 6697 -209 222 -220 D000 C ATOM 4252 CD ALYS B 124 -8.033 6.244 28.772 0.60 58.69 D000 C ANISOU 4252 CD ALYS B 124 6964 8124 7213 -344 398 -322 D000 C ATOM 4253 CD BLYS B 124 -7.803 5.985 29.263 0.40 57.56 D000 C ANISOU 4253 CD BLYS B 124 6816 7990 7064 -343 343 -291 D000 C ATOM 4254 CE ALYS B 124 -8.990 7.138 29.545 0.60 71.57 D000 C ANISOU 4254 CE ALYS B 124 8285 9910 8998 -247 392 -335 D000 C ATOM 4255 CE BLYS B 124 -8.728 6.746 30.219 0.40 69.69 D000 C ANISOU 4255 CE BLYS B 124 8043 9695 8739 -256 318 -292 D000 C ATOM 4256 NZ ALYS B 124 -10.325 6.499 29.691 0.60 69.50 D000 N ANISOU 4256 NZ ALYS B 124 7847 9819 8742 -386 495 -436 D000 N ATOM 4257 NZ BLYS B 124 -8.045 7.816 31.004 0.40 65.71 D000 N ANISOU 4257 NZ BLYS B 124 7473 9163 8329 -67 190 -182 D000 N ATOM 4258 N TYR B 125 -3.615 3.761 26.641 1.00 40.69 D000 N ANISOU 4258 N TYR B 125 5710 5313 4437 -262 77 -211 D000 N ATOM 4259 CA TYR B 125 -2.773 3.395 25.511 1.00 42.99 D000 C ANISOU 4259 CA TYR B 125 6283 5487 4565 -197 -1 -215 D000 C ATOM 4260 C TYR B 125 -2.783 1.902 25.235 1.00 44.38 D000 C ANISOU 4260 C TYR B 125 6759 5540 4562 -255 19 -169 D000 C ATOM 4261 O TYR B 125 -2.079 1.453 24.325 1.00 47.43 D000 O ANISOU 4261 O TYR B 125 7423 5818 4781 -170 -69 -150 D000 O ATOM 4262 CB TYR B 125 -1.330 3.852 25.752 1.00 42.47 D000 C ANISOU 4262 CB TYR B 125 6147 5419 4570 -31 -206 -223 D000 C ATOM 4263 CG TYR B 125 -1.162 5.342 25.712 1.00 39.41 D000 C ANISOU 4263 CG TYR B 125 5553 5085 4337 11 -221 -273 D000 C ATOM 4264 CD1 TYR B 125 -1.121 6.025 24.512 1.00 38.62 D000 C ANISOU 4264 CD1 TYR B 125 5548 4952 4173 27 -219 -351 D000 C ATOM 4265 CD2 TYR B 125 -1.092 6.082 26.890 1.00 45.67 D000 C ANISOU 4265 CD2 TYR B 125 6082 5946 5327 27 -225 -241 D000 C ATOM 4266 CE1 TYR B 125 -0.981 7.387 24.473 1.00 39.88 D000 C ANISOU 4266 CE1 TYR B 125 5542 5122 4489 54 -223 -416 D000 C ATOM 4267 CE2 TYR B 125 -0.951 7.443 26.859 1.00 48.74 D000 C ANISOU 4267 CE2 TYR B 125 6324 6332 5864 57 -222 -273 D000 C ATOM 4268 CZ TYR B 125 -0.895 8.092 25.650 1.00 47.28 D000 C ANISOU 4268 CZ TYR B 125 6232 6090 5641 66 -221 -369 D000 C ATOM 4269 OH TYR B 125 -0.754 9.451 25.616 1.00 45.21 D000 O ANISOU 4269 OH TYR B 125 5845 5788 5543 86 -212 -420 D000 O ATOM 4270 N THR B 126 -3.582 1.136 25.970 1.00 44.55 D000 N ANISOU 4270 N THR B 126 6747 5568 4612 -395 125 -158 D000 N ATOM 4271 CA ATHR B 126 -3.652 -0.315 25.882 0.87 46.75 D000 C ANISOU 4271 CA ATHR B 126 7316 5689 4756 -479 165 -120 D000 C ATOM 4272 CA BTHR B 126 -3.630 -0.308 25.807 0.13 46.98 D000 C ANISOU 4272 CA BTHR B 126 7360 5714 4777 -476 164 -118 D000 C ATOM 4273 C THR B 126 -5.021 -0.747 25.371 1.00 49.36 D000 C ANISOU 4273 C THR B 126 7737 5999 5017 -733 416 -137 D000 C ATOM 4274 O THR B 126 -6.034 -0.146 25.734 1.00 51.11 D000 O ANISOU 4274 O THR B 126 7674 6382 5364 -848 538 -201 D000 O ATOM 4275 CB ATHR B 126 -3.429 -0.939 27.264 0.87 49.56 D000 C ANISOU 4275 CB ATHR B 126 7555 6061 5214 -471 92 -130 D000 C ATOM 4276 CB BTHR B 126 -3.236 -1.016 27.107 0.13 50.24 D000 C ANISOU 4276 CB BTHR B 126 7696 6118 5275 -444 72 -122 D000 C ATOM 4277 CG2ATHR B 126 -3.331 -2.446 27.154 0.87 52.24 D000 C ANISOU 4277 CG2ATHR B 126 8236 6185 5429 -528 114 -104 D000 C ATOM 4278 CG2BTHR B 126 -1.749 -0.828 27.379 0.13 52.22 D000 C ANISOU 4278 CG2BTHR B 126 7921 6364 5556 -196 -148 -110 D000 C ATOM 4279 OG1ATHR B 126 -2.239 -0.403 27.850 0.87 52.01 D000 O ANISOU 4279 OG1ATHR B 126 7714 6435 5612 -261 -95 -128 D000 O ATOM 4280 OG1BTHR B 126 -3.990 -0.471 28.195 0.13 51.20 D000 O ANISOU 4280 OG1BTHR B 126 7474 6423 5556 -528 123 -168 D000 O ATOM 4281 N GLN B 127 -5.064 -1.811 24.574 1.00 58.62 D000 N ANISOU 4281 N GLN B 127 9303 6974 5998 -818 500 -80 D000 N ATOM 4282 CA GLN B 127 -6.357 -2.322 24.129 1.00 59.10 D000 C ANISOU 4282 CA GLN B 127 9455 7003 5997 -1109 781 -99 D000 C ATOM 4283 C GLN B 127 -7.102 -2.972 25.294 1.00 59.18 D000 C ANISOU 4283 C GLN B 127 9279 7050 6155 -1303 852 -168 D000 C ATOM 4284 O GLN B 127 -6.503 -3.708 26.081 1.00 54.76 D000 O ANISOU 4284 O GLN B 127 8795 6388 5624 -1241 719 -156 D000 O ATOM 4285 CB GLN B 127 -6.209 -3.336 22.995 1.00 67.87 D000 C ANISOU 4285 CB GLN B 127 11090 7857 6842 -1171 876 5 D000 C ATOM 4286 CG GLN B 127 -5.137 -3.011 21.989 1.00 78.11 D000 C ANISOU 4286 CG GLN B 127 12645 9087 7947 -916 705 79 D000 C ATOM 4287 CD GLN B 127 -4.340 -4.215 21.585 1.00102.95 D000 C ANISOU 4287 CD GLN B 127 16273 11952 10891 -807 598 203 D000 C ATOM 4288 NE2 GLN B 127 -3.183 -3.966 20.990 1.00102.37 D000 N ANISOU 4288 NE2 GLN B 127 16353 11855 10689 -517 352 246 D000 N ATOM 4289 OE1 GLN B 127 -4.760 -5.359 21.768 1.00106.03 D000 O ANISOU 4289 OE1 GLN B 127 16906 12139 11241 -976 730 254 D000 O ATOM 4290 N PRO B 128 -8.416 -2.744 25.414 1.00 60.31 D000 N ANISOU 4290 N PRO B 128 9172 7350 6393 -1536 1058 -263 D000 N ATOM 4291 CA PRO B 128 -9.147 -3.304 26.563 1.00 63.92 D000 C ANISOU 4291 CA PRO B 128 9407 7886 6995 -1722 1092 -364 D000 C ATOM 4292 C PRO B 128 -9.132 -4.818 26.604 1.00 63.23 D000 C ANISOU 4292 C PRO B 128 9673 7530 6821 -1912 1168 -347 D000 C ATOM 4293 O PRO B 128 -9.258 -5.403 27.688 1.00 62.64 D000 O ANISOU 4293 O PRO B 128 9491 7464 6844 -1989 1105 -429 D000 O ATOM 4294 CB PRO B 128 -10.575 -2.766 26.367 1.00 77.22 D000 C ANISOU 4294 CB PRO B 128 10770 9794 8777 -1932 1314 -482 D000 C ATOM 4295 CG PRO B 128 -10.435 -1.641 25.393 1.00 62.78 D000 C ANISOU 4295 CG PRO B 128 8922 8036 6897 -1773 1345 -447 D000 C ATOM 4296 CD PRO B 128 -9.328 -2.049 24.490 1.00 73.92 D000 C ANISOU 4296 CD PRO B 128 10801 9196 8090 -1648 1278 -310 D000 C ATOM 4297 N SER B 129 -8.992 -5.472 25.447 1.00 49.00 D000 N ANISOU 4297 N SER B 129 5956 5976 6686 618 427 339 D000 N ATOM 4298 CA SER B 129 -8.943 -6.929 25.419 1.00 64.56 D000 C ANISOU 4298 CA SER B 129 7835 7955 8741 437 328 377 D000 C ATOM 4299 C SER B 129 -7.781 -7.473 26.243 1.00 60.01 D000 C ANISOU 4299 C SER B 129 7394 7330 8079 265 85 141 D000 C ATOM 4300 O SER B 129 -7.866 -8.581 26.787 1.00 56.43 D000 O ANISOU 4300 O SER B 129 6900 6854 7688 117 -109 154 D000 O ATOM 4301 CB SER B 129 -8.840 -7.409 23.971 1.00 66.51 D000 C ANISOU 4301 CB SER B 129 8188 8191 8892 586 526 423 D000 C ATOM 4302 OG SER B 129 -7.578 -7.088 23.426 1.00 63.54 D000 O ANISOU 4302 OG SER B 129 8143 7709 8290 648 498 151 D000 O ATOM 4303 N ILE B 130 -6.680 -6.727 26.333 1.00 53.90 D000 N ANISOU 4303 N ILE B 130 6795 6523 7162 313 69 -27 D000 N ATOM 4304 CA ILE B 130 -5.574 -7.153 27.184 1.00 55.51 D000 C ANISOU 4304 CA ILE B 130 7074 6738 7280 237 -89 -137 D000 C ATOM 4305 C ILE B 130 -6.037 -7.255 28.634 1.00 52.68 D000 C ANISOU 4305 C ILE B 130 6626 6431 6958 208 -238 -97 D000 C ATOM 4306 O ILE B 130 -5.698 -8.212 29.342 1.00 50.99 D000 O ANISOU 4306 O ILE B 130 6512 6212 6651 200 -397 -148 D000 O ATOM 4307 CB ILE B 130 -4.384 -6.187 27.042 1.00 55.37 D000 C ANISOU 4307 CB ILE B 130 7155 6683 7200 284 -96 -179 D000 C ATOM 4308 CG1 ILE B 130 -3.775 -6.223 25.636 1.00 66.12 D000 C ANISOU 4308 CG1 ILE B 130 8700 7924 8500 312 -62 -245 D000 C ATOM 4309 CG2 ILE B 130 -3.287 -6.527 28.046 1.00 58.58 D000 C ANISOU 4309 CG2 ILE B 130 7552 7169 7536 282 -187 -154 D000 C ATOM 4310 CD1 ILE B 130 -3.455 -7.606 25.112 1.00 67.44 D000 C ANISOU 4310 CD1 ILE B 130 8923 8102 8597 260 -41 -304 D000 C ATOM 4311 N PHE B 131 -6.819 -6.271 29.100 1.00 54.07 D000 N ANISOU 4311 N PHE B 131 6672 6637 7237 234 -211 -11 D000 N ATOM 4312 CA PHE B 131 -7.216 -6.253 30.507 1.00 55.37 D000 C ANISOU 4312 CA PHE B 131 6790 6832 7417 230 -377 19 D000 C ATOM 4313 C PHE B 131 -8.111 -7.434 30.854 1.00 56.07 D000 C ANISOU 4313 C PHE B 131 6867 6837 7600 122 -611 76 D000 C ATOM 4314 O PHE B 131 -8.021 -7.978 31.960 1.00 57.21 D000 O ANISOU 4314 O PHE B 131 7165 6928 7644 155 -867 20 D000 O ATOM 4315 CB PHE B 131 -7.930 -4.945 30.849 1.00 55.29 D000 C ANISOU 4315 CB PHE B 131 6627 6861 7518 267 -301 112 D000 C ATOM 4316 CG PHE B 131 -7.040 -3.753 30.821 1.00 51.78 D000 C ANISOU 4316 CG PHE B 131 6219 6438 7016 348 -211 84 D000 C ATOM 4317 CD1 PHE B 131 -7.216 -2.769 29.867 1.00 63.01 D000 C ANISOU 4317 CD1 PHE B 131 7663 7797 8479 405 -93 99 D000 C ATOM 4318 CD2 PHE B 131 -6.034 -3.606 31.760 1.00 66.86 D000 C ANISOU 4318 CD2 PHE B 131 8159 8413 8833 406 -274 93 D000 C ATOM 4319 CE1 PHE B 131 -6.394 -1.665 29.836 1.00 63.89 D000 C ANISOU 4319 CE1 PHE B 131 7841 7848 8587 441 -136 99 D000 C ATOM 4320 CE2 PHE B 131 -5.215 -2.502 31.739 1.00 68.46 D000 C ANISOU 4320 CE2 PHE B 131 8322 8616 9075 436 -249 173 D000 C ATOM 4321 CZ PHE B 131 -5.396 -1.530 30.776 1.00 69.24 D000 C ANISOU 4321 CZ PHE B 131 8456 8589 9264 415 -229 164 D000 C ATOM 4322 N LYS B 132 -8.999 -7.838 29.946 1.00 52.56 D000 N ANISOU 4322 N LYS B 132 6262 6359 7351 23 -566 231 D000 N ATOM 4323 CA LYS B 132 -9.854 -8.962 30.292 1.00 62.05 D000 C ANISOU 4323 CA LYS B 132 7407 7434 8737 -137 -890 372 D000 C ATOM 4324 C LYS B 132 -9.031 -10.231 30.449 1.00 61.57 D000 C ANISOU 4324 C LYS B 132 7639 7256 8499 -155 -1125 195 D000 C ATOM 4325 O LYS B 132 -9.330 -11.057 31.314 1.00 56.31 D000 O ANISOU 4325 O LYS B 132 7138 6415 7841 -212 -1545 186 D000 O ATOM 4326 CB LYS B 132 -10.982 -9.176 29.272 1.00 72.62 D000 C ANISOU 4326 CB LYS B 132 8420 8789 10383 -225 -774 712 D000 C ATOM 4327 CG LYS B 132 -10.688 -8.885 27.808 1.00 86.29 D000 C ANISOU 4327 CG LYS B 132 10121 10630 12034 -79 -362 737 D000 C ATOM 4328 CD LYS B 132 -10.279 -10.152 27.059 1.00 94.10 D000 C ANISOU 4328 CD LYS B 132 11188 11553 13013 -160 -422 722 D000 C ATOM 4329 CE LYS B 132 -10.598 -10.059 25.575 1.00 99.68 D000 C ANISOU 4329 CE LYS B 132 11764 12360 13750 -5 -50 930 D000 C ATOM 4330 NZ LYS B 132 -10.040 -11.195 24.789 1.00 99.87 D000 N ANISOU 4330 NZ LYS B 132 11890 12333 13724 -62 -71 879 D000 N ATOM 4331 N ILE B 133 -7.967 -10.389 29.657 1.00 50.50 D000 N ANISOU 4331 N ILE B 133 6356 5917 6914 -79 -903 50 D000 N ATOM 4332 CA ILE B 133 -7.108 -11.558 29.814 1.00 51.58 D000 C ANISOU 4332 CA ILE B 133 6785 5967 6848 -46 -1085 -110 D000 C ATOM 4333 C ILE B 133 -6.427 -11.524 31.178 1.00 50.02 D000 C ANISOU 4333 C ILE B 133 6872 5768 6365 161 -1240 -251 D000 C ATOM 4334 O ILE B 133 -6.422 -12.516 31.918 1.00 50.51 D000 O ANISOU 4334 O ILE B 133 7242 5668 6283 232 -1594 -327 D000 O ATOM 4335 CB ILE B 133 -6.082 -11.628 28.666 1.00 56.87 D000 C ANISOU 4335 CB ILE B 133 7490 6718 7398 -3 -799 -199 D000 C ATOM 4336 CG1 ILE B 133 -6.800 -11.774 27.321 1.00 54.46 D000 C ANISOU 4336 CG1 ILE B 133 6974 6410 7307 -114 -640 -43 D000 C ATOM 4337 CG2 ILE B 133 -5.132 -12.792 28.874 1.00 51.33 D000 C ANISOU 4337 CG2 ILE B 133 7085 5953 6465 69 -949 -345 D000 C ATOM 4338 CD1 ILE B 133 -5.887 -11.634 26.123 1.00 63.91 D000 C ANISOU 4338 CD1 ILE B 133 8248 7659 8374 -40 -373 -139 D000 C ATOM 4339 N ILE B 134 -5.841 -10.380 31.531 1.00 49.46 D000 N ANISOU 4339 N ILE B 134 6734 5862 6196 304 -997 -256 D000 N ATOM 4340 CA ILE B 134 -5.167 -10.261 32.822 1.00 53.37 D000 C ANISOU 4340 CA ILE B 134 7452 6414 6410 580 -1059 -298 D000 C ATOM 4341 C ILE B 134 -6.138 -10.571 33.953 1.00 54.35 D000 C ANISOU 4341 C ILE B 134 7749 6380 6522 614 -1439 -310 D000 C ATOM 4342 O ILE B 134 -5.842 -11.356 34.864 1.00 52.98 D000 O ANISOU 4342 O ILE B 134 7982 6098 6051 860 -1704 -404 D000 O ATOM 4343 CB ILE B 134 -4.565 -8.853 32.982 1.00 50.91 D000 C ANISOU 4343 CB ILE B 134 6934 6298 6113 672 -764 -197 D000 C ATOM 4344 CG1 ILE B 134 -3.481 -8.609 31.927 1.00 55.70 D000 C ANISOU 4344 CG1 ILE B 134 7437 6985 6741 635 -523 -161 D000 C ATOM 4345 CG2 ILE B 134 -4.027 -8.663 34.416 1.00 55.39 D000 C ANISOU 4345 CG2 ILE B 134 7670 6965 6411 1008 -789 -143 D000 C ATOM 4346 CD1 ILE B 134 -3.008 -7.168 31.872 1.00 51.20 D000 C ANISOU 4346 CD1 ILE B 134 6647 6512 6295 634 -356 -17 D000 C ATOM 4347 N SER B 135 -7.321 -9.964 33.903 1.00 51.70 D000 N ANISOU 4347 N SER B 135 7146 6004 6492 403 -1499 -198 D000 N ATOM 4348 CA SER B 135 -8.263 -10.089 35.009 1.00 58.04 D000 C ANISOU 4348 CA SER B 135 8078 6640 7336 404 -1899 -169 D000 C ATOM 4349 C SER B 135 -8.691 -11.532 35.235 1.00 58.18 D000 C ANISOU 4349 C SER B 135 8418 6339 7348 334 -2444 -210 D000 C ATOM 4350 O SER B 135 -9.075 -11.886 36.356 1.00 63.85 D000 O ANISOU 4350 O SER B 135 9479 6840 7940 452 -2902 -261 D000 O ATOM 4351 CB SER B 135 -9.481 -9.201 34.748 1.00 58.88 D000 C ANISOU 4351 CB SER B 135 7764 6777 7829 169 -1835 33 D000 C ATOM 4352 OG SER B 135 -10.339 -9.783 33.781 1.00 64.72 D000 O ANISOU 4352 OG SER B 135 8261 7420 8910 -104 -1922 219 D000 O ATOM 4353 N GLN B 136 -8.610 -12.375 34.206 1.00 58.97 D000 N ANISOU 4353 N GLN B 136 8462 6374 7569 161 -2452 -189 D000 N ATOM 4354 CA GLN B 136 -8.997 -13.776 34.308 1.00 65.88 D000 C ANISOU 4354 CA GLN B 136 9630 6908 8492 51 -3021 -195 D000 C ATOM 4355 C GLN B 136 -7.882 -14.656 34.854 1.00 68.07 D000 C ANISOU 4355 C GLN B 136 10514 7089 8260 409 -3177 -459 D000 C ATOM 4356 O GLN B 136 -8.097 -15.862 35.027 1.00 72.59 D000 O ANISOU 4356 O GLN B 136 11462 7322 8796 378 -3723 -513 D000 O ATOM 4357 CB GLN B 136 -9.428 -14.293 32.933 1.00 75.82 D000 C ANISOU 4357 CB GLN B 136 10525 8158 10124 -274 -2937 4 D000 C ATOM 4358 CG GLN B 136 -10.768 -13.750 32.461 1.00 82.20 D000 C ANISOU 4358 CG GLN B 136 10780 8999 11451 -567 -2900 381 D000 C ATOM 4359 CD GLN B 136 -11.126 -14.220 31.063 1.00103.39 D000 C ANISOU 4359 CD GLN B 136 13094 11736 14452 -774 -2712 647 D000 C ATOM 4360 NE2 GLN B 136 -12.400 -14.106 30.710 1.00133.09 D000 N ANISOU 4360 NE2 GLN B 136 16385 15482 18701 -999 -2783 1102 D000 N ATOM 4361 OE1 GLN B 136 -10.264 -14.670 30.306 1.00 93.15 D000 O ANISOU 4361 OE1 GLN B 136 11915 10511 12966 -703 -2485 491 D000 O ATOM 4362 N GLY B 137 -6.705 -14.092 35.113 1.00 66.85 D000 N ANISOU 4362 N GLY B 137 10458 7213 7730 763 -2729 -573 D000 N ATOM 4363 CA GLY B 137 -5.600 -14.832 35.684 1.00 63.49 D000 C ANISOU 4363 CA GLY B 137 10578 6766 6779 1215 -2775 -738 D000 C ATOM 4364 C GLY B 137 -4.570 -15.331 34.699 1.00 61.84 D000 C ANISOU 4364 C GLY B 137 10320 6699 6476 1237 -2450 -770 D000 C ATOM 4365 O GLY B 137 -3.698 -16.115 35.091 1.00 70.22 D000 O ANISOU 4365 O GLY B 137 11846 7728 7107 1625 -2505 -875 D000 O ATOM 4366 N THR B 138 -4.638 -14.906 33.440 1.00 56.64 D000 N ANISOU 4366 N THR B 138 9159 6191 6172 885 -2120 -676 D000 N ATOM 4367 CA THR B 138 -3.701 -15.319 32.409 1.00 61.90 D000 C ANISOU 4367 CA THR B 138 9759 6973 6786 868 -1833 -700 D000 C ATOM 4368 C THR B 138 -2.763 -14.161 32.108 1.00 57.42 D000 C ANISOU 4368 C THR B 138 8887 6727 6203 958 -1314 -600 D000 C ATOM 4369 O THR B 138 -3.192 -13.008 32.044 1.00 57.35 D000 O ANISOU 4369 O THR B 138 8556 6817 6416 823 -1154 -507 D000 O ATOM 4370 CB THR B 138 -4.444 -15.742 31.139 1.00 62.62 D000 C ANISOU 4370 CB THR B 138 9568 6957 7266 450 -1888 -641 D000 C ATOM 4371 CG2 THR B 138 -3.476 -15.998 29.994 1.00 62.63 D000 C ANISOU 4371 CG2 THR B 138 9484 7093 7220 432 -1557 -671 D000 C ATOM 4372 OG1 THR B 138 -5.191 -16.936 31.401 1.00 70.80 D000 O ANISOU 4372 OG1 THR B 138 10870 7659 8372 338 -2446 -659 D000 O ATOM 4373 N ASN B 139 -1.477 -14.456 31.948 1.00 54.72 D000 N ANISOU 4373 N ASN B 139 8648 6524 5618 1190 -1093 -581 D000 N ATOM 4374 CA ASN B 139 -0.533 -13.423 31.551 1.00 51.81 D000 C ANISOU 4374 CA ASN B 139 7954 6403 5328 1208 -701 -407 D000 C ATOM 4375 C ASN B 139 -0.499 -13.430 30.031 1.00 45.98 D000 C ANISOU 4375 C ASN B 139 6993 5628 4849 872 -593 -439 D000 C ATOM 4376 O ASN B 139 -0.041 -14.419 29.439 1.00 46.22 D000 O ANISOU 4376 O ASN B 139 7167 5607 4787 869 -614 -510 D000 O ATOM 4377 CB ASN B 139 0.847 -13.672 32.132 1.00 59.41 D000 C ANISOU 4377 CB ASN B 139 9061 7552 5958 1636 -512 -248 D000 C ATOM 4378 CG ASN B 139 1.843 -12.606 31.715 1.00 55.41 D000 C ANISOU 4378 CG ASN B 139 8152 7262 5639 1593 -199 39 D000 C ATOM 4379 ND2 ASN B 139 2.997 -12.584 32.369 1.00 70.82 D000 N ANISOU 4379 ND2 ASN B 139 10095 9433 7379 1988 7 336 D000 N ATOM 4380 OD1 ASN B 139 1.570 -11.800 30.824 1.00 55.42 D000 O ANISOU 4380 OD1 ASN B 139 7869 7214 5974 1238 -172 36 D000 O ATOM 4381 N PRO B 140 -1.004 -12.394 29.356 1.00 44.97 D000 N ANISOU 4381 N PRO B 140 6576 5505 5006 632 -490 -398 D000 N ATOM 4382 CA PRO B 140 -1.074 -12.450 27.886 1.00 42.88 D000 C ANISOU 4382 CA PRO B 140 6204 5175 4912 408 -404 -441 D000 C ATOM 4383 C PRO B 140 0.285 -12.595 27.232 1.00 45.44 D000 C ANISOU 4383 C PRO B 140 6544 5556 5165 451 -277 -394 D000 C ATOM 4384 O PRO B 140 0.364 -13.062 26.091 1.00 45.83 D000 O ANISOU 4384 O PRO B 140 6621 5530 5263 326 -250 -468 D000 O ATOM 4385 CB PRO B 140 -1.748 -11.124 27.504 1.00 48.76 D000 C ANISOU 4385 CB PRO B 140 6738 5916 5874 293 -316 -385 D000 C ATOM 4386 CG PRO B 140 -1.623 -10.246 28.708 1.00 51.81 D000 C ANISOU 4386 CG PRO B 140 7056 6397 6232 419 -320 -287 D000 C ATOM 4387 CD PRO B 140 -1.569 -11.146 29.902 1.00 48.56 D000 C ANISOU 4387 CD PRO B 140 6846 6008 5595 612 -456 -315 D000 C ATOM 4388 N LEU B 141 1.361 -12.239 27.932 1.00 47.66 D000 N ANISOU 4388 N LEU B 141 6786 5976 5346 642 -197 -219 D000 N ATOM 4389 CA LEU B 141 2.690 -12.380 27.352 1.00 51.36 D000 C ANISOU 4389 CA LEU B 141 7206 6501 5808 670 -104 -74 D000 C ATOM 4390 C LEU B 141 3.075 -13.835 27.133 1.00 51.18 D000 C ANISOU 4390 C LEU B 141 7409 6467 5569 769 -112 -181 D000 C ATOM 4391 O LEU B 141 3.960 -14.107 26.311 1.00 51.48 D000 O ANISOU 4391 O LEU B 141 7414 6508 5638 716 -54 -117 D000 O ATOM 4392 CB LEU B 141 3.723 -11.699 28.249 1.00 51.08 D000 C ANISOU 4392 CB LEU B 141 6992 6654 5763 886 1 279 D000 C ATOM 4393 CG LEU B 141 3.534 -10.187 28.387 1.00 52.94 D000 C ANISOU 4393 CG LEU B 141 6981 6874 6260 758 -34 435 D000 C ATOM 4394 CD1 LEU B 141 4.374 -9.646 29.532 1.00 61.58 D000 C ANISOU 4394 CD1 LEU B 141 7868 8189 7343 1019 79 850 D000 C ATOM 4395 CD2 LEU B 141 3.889 -9.479 27.099 1.00 54.21 D000 C ANISOU 4395 CD2 LEU B 141 7049 6857 6690 479 -149 463 D000 C ATOM 4396 N ASN B 142 2.430 -14.772 27.833 1.00 48.58 D000 N ANISOU 4396 N ASN B 142 7338 6086 5033 904 -239 -338 D000 N ATOM 4397 CA ASN B 142 2.759 -16.187 27.740 1.00 54.51 D000 C ANISOU 4397 CA ASN B 142 8381 6781 5551 1033 -317 -450 D000 C ATOM 4398 C ASN B 142 1.854 -16.961 26.789 1.00 50.78 D000 C ANISOU 4398 C ASN B 142 7971 6107 5218 741 -483 -657 D000 C ATOM 4399 O ASN B 142 1.982 -18.187 26.696 1.00 54.21 D000 O ANISOU 4399 O ASN B 142 8662 6444 5492 805 -617 -762 D000 O ATOM 4400 CB ASN B 142 2.688 -16.838 29.124 1.00 60.59 D000 C ANISOU 4400 CB ASN B 142 9514 7543 5963 1425 -457 -480 D000 C ATOM 4401 CG ASN B 142 3.746 -16.315 30.068 1.00 66.95 D000 C ANISOU 4401 CG ASN B 142 10282 8604 6553 1851 -217 -188 D000 C ATOM 4402 ND2 ASN B 142 3.420 -16.276 31.353 1.00 72.78 D000 N ANISOU 4402 ND2 ASN B 142 11268 9356 7029 2198 -303 -181 D000 N ATOM 4403 OD1 ASN B 142 4.844 -15.943 29.647 1.00 67.97 D000 O ANISOU 4403 OD1 ASN B 142 10148 8910 6765 1880 28 78 D000 O ATOM 4404 N ILE B 143 0.922 -16.291 26.117 1.00 48.31 D000 N ANISOU 4404 N ILE B 143 7436 5732 5189 468 -476 -674 D000 N ATOM 4405 CA ILE B 143 0.066 -16.962 25.144 1.00 44.63 D000 C ANISOU 4405 CA ILE B 143 6946 5126 4887 239 -563 -747 D000 C ATOM 4406 C ILE B 143 0.904 -17.333 23.930 1.00 48.65 D000 C ANISOU 4406 C ILE B 143 7457 5649 5377 188 -413 -773 D000 C ATOM 4407 O ILE B 143 1.626 -16.494 23.382 1.00 49.31 D000 O ANISOU 4407 O ILE B 143 7436 5801 5500 185 -247 -718 D000 O ATOM 4408 CB ILE B 143 -1.118 -16.059 24.763 1.00 47.91 D000 C ANISOU 4408 CB ILE B 143 7112 5523 5567 77 -513 -672 D000 C ATOM 4409 CG1 ILE B 143 -2.074 -15.877 25.954 1.00 50.34 D000 C ANISOU 4409 CG1 ILE B 143 7414 5785 5930 87 -722 -632 D000 C ATOM 4410 CG2 ILE B 143 -1.885 -16.617 23.565 1.00 52.14 D000 C ANISOU 4410 CG2 ILE B 143 7545 5982 6282 -85 -487 -624 D000 C ATOM 4411 CD1 ILE B 143 -3.013 -14.686 25.778 1.00 53.52 D000 C ANISOU 4411 CD1 ILE B 143 7548 6231 6555 5 -602 -517 D000 C ATOM 4412 N ARG B 144 0.823 -18.599 23.511 1.00 46.07 D000 N ANISOU 4412 N ARG B 144 7272 5224 5009 137 -528 -845 D000 N ATOM 4413 CA ARG B 144 1.581 -19.078 22.362 1.00 48.75 D000 C ANISOU 4413 CA ARG B 144 7635 5569 5320 93 -401 -879 D000 C ATOM 4414 C ARG B 144 0.878 -18.674 21.063 1.00 47.36 D000 C ANISOU 4414 C ARG B 144 7289 5359 5348 -62 -270 -842 D000 C ATOM 4415 O ARG B 144 -0.355 -18.621 21.010 1.00 46.43 D000 O ANISOU 4415 O ARG B 144 7037 5198 5405 -146 -313 -756 D000 O ATOM 4416 CB ARG B 144 1.723 -20.598 22.435 1.00 54.72 D000 C ANISOU 4416 CB ARG B 144 8629 6221 5942 120 -587 -962 D000 C ATOM 4417 CG ARG B 144 2.324 -21.091 23.764 1.00 71.56 D000 C ANISOU 4417 CG ARG B 144 11060 8361 7770 407 -731 -1002 D000 C ATOM 4418 CD ARG B 144 3.725 -21.712 23.722 1.00 96.85 D000 C ANISOU 4418 CD ARG B 144 14444 11657 10697 643 -608 -999 D000 C ATOM 4419 NE ARG B 144 3.629 -23.146 23.469 1.00115.75 D000 N ANISOU 4419 NE ARG B 144 17121 13877 12981 639 -829 -1125 D000 N ATOM 4420 CZ ARG B 144 4.191 -23.782 22.449 1.00132.51 D000 C ANISOU 4420 CZ ARG B 144 19236 16000 15111 553 -734 -1153 D000 C ATOM 4421 NH1 ARG B 144 5.176 -23.245 21.760 1.00125.08 D000 N ANISOU 4421 NH1 ARG B 144 18104 15225 14196 551 -442 -1060 D000 N ATOM 4422 NH2 ARG B 144 3.782 -25.011 22.146 1.00139.78 D000 N ANISOU 4422 NH2 ARG B 144 20362 16722 16028 465 -991 -1253 D000 N ATOM 4423 N PRO B 145 1.629 -18.366 20.002 1.00 44.35 D000 N ANISOU 4423 N PRO B 145 6924 4988 4940 -57 -118 -863 D000 N ATOM 4424 CA PRO B 145 0.976 -18.010 18.733 1.00 41.98 D000 C ANISOU 4424 CA PRO B 145 6572 4643 4735 -78 19 -831 D000 C ATOM 4425 C PRO B 145 0.230 -19.194 18.143 1.00 43.80 D000 C ANISOU 4425 C PRO B 145 6761 4839 5043 -147 15 -771 D000 C ATOM 4426 O PRO B 145 0.592 -20.353 18.345 1.00 48.44 D000 O ANISOU 4426 O PRO B 145 7435 5388 5581 -208 -118 -822 D000 O ATOM 4427 CB PRO B 145 2.142 -17.577 17.834 1.00 50.05 D000 C ANISOU 4427 CB PRO B 145 7730 5620 5665 -36 70 -892 D000 C ATOM 4428 CG PRO B 145 3.321 -18.242 18.406 1.00 49.78 D000 C ANISOU 4428 CG PRO B 145 7745 5633 5537 -48 -7 -907 D000 C ATOM 4429 CD PRO B 145 3.100 -18.274 19.889 1.00 47.18 D000 C ANISOU 4429 CD PRO B 145 7359 5386 5182 4 -84 -867 D000 C ATOM 4430 N LYS B 146 -0.858 -18.889 17.444 1.00 43.39 D000 N ANISOU 4430 N LYS B 146 5882 4156 6449 564 642 -488 D000 N ATOM 4431 CA ALYS B 146 -1.705 -19.912 16.851 0.40 47.92 D000 C ANISOU 4431 CA ALYS B 146 6532 4621 7054 495 569 -501 D000 C ATOM 4432 CA BLYS B 146 -1.687 -19.919 16.840 0.61 47.92 D000 C ANISOU 4432 CA BLYS B 146 6531 4620 7056 497 569 -500 D000 C ATOM 4433 C LYS B 146 -2.174 -19.438 15.484 1.00 44.90 D000 C ANISOU 4433 C LYS B 146 6071 4305 6686 414 455 -386 D000 C ATOM 4434 O LYS B 146 -2.346 -18.241 15.258 1.00 46.44 D000 O ANISOU 4434 O LYS B 146 6192 4640 6813 372 413 -348 D000 O ATOM 4435 CB ALYS B 146 -2.955 -20.231 17.691 0.40 49.67 D000 C ANISOU 4435 CB ALYS B 146 6886 4820 7165 404 543 -639 D000 C ATOM 4436 CB BLYS B 146 -2.890 -20.257 17.726 0.61 49.71 D000 C ANISOU 4436 CB BLYS B 146 6892 4821 7173 412 549 -640 D000 C ATOM 4437 CG ALYS B 146 -2.789 -20.140 19.194 0.40 51.07 D000 C ANISOU 4437 CG ALYS B 146 7156 5011 7239 461 630 -768 D000 C ATOM 4438 CG BLYS B 146 -3.766 -19.049 17.996 0.61 48.47 D000 C ANISOU 4438 CG BLYS B 146 6713 4827 6877 323 488 -658 D000 C ATOM 4439 CD ALYS B 146 -2.332 -21.451 19.805 0.40 53.83 D000 C ANISOU 4439 CD ALYS B 146 7619 5185 7647 543 715 -861 D000 C ATOM 4440 CD BLYS B 146 -4.793 -19.309 19.086 0.61 58.39 D000 C ANISOU 4440 CD BLYS B 146 8093 6075 8016 264 463 -808 D000 C ATOM 4441 CE ALYS B 146 -1.820 -21.223 21.219 0.40 51.09 D000 C ANISOU 4441 CE ALYS B 146 7353 4867 7192 640 834 -964 D000 C ATOM 4442 CE BLYS B 146 -5.659 -18.075 19.315 0.61 60.16 D000 C ANISOU 4442 CE BLYS B 146 8285 6466 8108 192 395 -809 D000 C ATOM 4443 NZ ALYS B 146 -2.582 -20.136 21.912 0.40 43.13 D000 N ANISOU 4443 NZ ALYS B 146 6369 4017 6002 577 789 -1009 D000 N ATOM 4444 NZ BLYS B 146 -7.094 -18.433 19.527 0.61 71.25 D000 N ANISOU 4444 NZ BLYS B 146 9748 7863 9461 73 292 -900 D000 N ATOM 4445 N ALA B 147 -2.402 -20.388 14.585 1.00 44.39 D000 N ANISOU 4445 N ALA B 147 6035 4131 6703 397 414 -332 D000 N ATOM 4446 CA ALA B 147 -3.033 -20.072 13.308 1.00 42.43 D000 C ANISOU 4446 CA ALA B 147 5746 3934 6442 317 318 -230 D000 C ATOM 4447 C ALA B 147 -4.538 -20.228 13.473 1.00 44.93 D000 C ANISOU 4447 C ALA B 147 6136 4246 6690 182 280 -296 D000 C ATOM 4448 O ALA B 147 -5.005 -21.229 14.024 1.00 47.80 D000 O ANISOU 4448 O ALA B 147 6595 4484 7085 152 305 -381 D000 O ATOM 4449 CB ALA B 147 -2.515 -20.982 12.196 1.00 48.50 D000 C ANISOU 4449 CB ALA B 147 6511 4591 7324 374 298 -116 D000 C ATOM 4450 N VAL B 148 -5.296 -19.239 13.007 1.00 40.47 D000 N ANISOU 4450 N VAL B 148 5522 3814 6042 100 218 -262 D000 N ATOM 4451 CA VAL B 148 -6.739 -19.235 13.205 1.00 43.01 D000 C ANISOU 4451 CA VAL B 148 5881 4156 6307 -25 181 -322 D000 C ATOM 4452 C VAL B 148 -7.399 -18.501 12.051 1.00 44.49 D000 C ANISOU 4452 C VAL B 148 6008 4442 6455 -89 124 -223 D000 C ATOM 4453 O VAL B 148 -6.824 -17.584 11.457 1.00 43.15 D000 O ANISOU 4453 O VAL B 148 5772 4370 6252 -45 104 -148 D000 O ATOM 4454 CB VAL B 148 -7.103 -18.587 14.564 1.00 49.20 D000 C ANISOU 4454 CB VAL B 148 6683 5023 6986 -40 186 -449 D000 C ATOM 4455 CG1 VAL B 148 -6.440 -17.226 14.700 1.00 48.96 D000 C ANISOU 4455 CG1 VAL B 148 6578 5137 6888 17 197 -412 D000 C ATOM 4456 CG2 VAL B 148 -8.600 -18.458 14.719 1.00 60.58 D000 C ANISOU 4456 CG2 VAL B 148 8134 6508 8375 -165 125 -504 D000 C ATOM 4457 N GLU B 149 -8.632 -18.894 11.741 1.00 44.11 D000 N ANISOU 4457 N GLU B 149 5982 4366 6413 -196 103 -227 D000 N ATOM 4458 CA GLU B 149 -9.384 -18.200 10.710 1.00 44.75 D000 C ANISOU 4458 CA GLU B 149 6012 4542 6448 -255 70 -140 D000 C ATOM 4459 C GLU B 149 -10.053 -16.961 11.298 1.00 42.15 D000 C ANISOU 4459 C GLU B 149 5633 4366 6017 -294 39 -200 D000 C ATOM 4460 O GLU B 149 -10.718 -17.038 12.336 1.00 43.31 D000 O ANISOU 4460 O GLU B 149 5794 4519 6141 -342 28 -308 D000 O ATOM 4461 CB GLU B 149 -10.434 -19.128 10.091 1.00 53.28 D000 C ANISOU 4461 CB GLU B 149 7123 5528 7595 -353 81 -103 D000 C ATOM 4462 CG GLU B 149 -10.763 -18.766 8.647 1.00 66.70 D000 C ANISOU 4462 CG GLU B 149 8797 7280 9266 -367 80 36 D000 C ATOM 4463 CD GLU B 149 -10.787 -19.962 7.712 1.00 84.48 D000 C ANISOU 4463 CD GLU B 149 11109 9385 11605 -375 119 140 D000 C ATOM 4464 OE1 GLU B 149 -10.486 -19.789 6.506 1.00 83.04 D000 O ANISOU 4464 OE1 GLU B 149 10937 9228 11385 -328 118 269 D000 O ATOM 4465 OE2 GLU B 149 -11.111 -21.072 8.186 1.00 82.41 D000 O ANISOU 4465 OE2 GLU B 149 10893 8975 11443 -426 148 92 D000 O ATOM 4466 N LYS B 150 -9.889 -15.826 10.619 1.00 41.68 D000 N ANISOU 4466 N LYS B 150 5520 4424 5891 -269 20 -131 D000 N ATOM 4467 CA LYS B 150 -10.523 -14.572 11.003 1.00 40.69 D000 C ANISOU 4467 CA LYS B 150 5349 4437 5675 -295 -4 -165 D000 C ATOM 4468 C LYS B 150 -11.144 -13.893 9.789 1.00 41.57 D000 C ANISOU 4468 C LYS B 150 5424 4625 5747 -326 -18 -78 D000 C ATOM 4469 O LYS B 150 -10.736 -14.122 8.646 1.00 42.08 D000 O ANISOU 4469 O LYS B 150 5502 4660 5826 -301 -16 15 D000 O ATOM 4470 CB LYS B 150 -9.522 -13.584 11.623 1.00 41.36 D000 C ANISOU 4470 CB LYS B 150 5411 4593 5712 -216 3 -187 D000 C ATOM 4471 CG LYS B 150 -8.770 -14.115 12.815 1.00 45.81 D000 C ANISOU 4471 CG LYS B 150 6014 5094 6298 -163 41 -265 D000 C ATOM 4472 CD LYS B 150 -9.605 -14.081 14.068 1.00 45.93 D000 C ANISOU 4472 CD LYS B 150 6065 5137 6251 -201 32 -375 D000 C ATOM 4473 CE LYS B 150 -8.723 -14.070 15.286 1.00 51.74 D000 C ANISOU 4473 CE LYS B 150 6843 5858 6957 -122 83 -444 D000 C ATOM 4474 NZ LYS B 150 -9.425 -14.626 16.451 1.00 53.04 D000 N ANISOU 4474 NZ LYS B 150 7082 5998 7074 -151 69 -566 D000 N ATOM 4475 N ILE B 151 -12.113 -13.024 10.065 1.00 38.45 D000 N ANISOU 4475 N ILE B 151 4989 4330 5291 -368 -33 -108 D000 N ATOM 4476 CA ILE B 151 -12.560 -12.006 9.121 1.00 39.21 D000 C ANISOU 4476 CA ILE B 151 5050 4520 5326 -370 -37 -44 D000 C ATOM 4477 C ILE B 151 -11.776 -10.735 9.416 1.00 37.92 D000 C ANISOU 4477 C ILE B 151 4871 4437 5101 -305 -53 -57 D000 C ATOM 4478 O ILE B 151 -11.837 -10.220 10.535 1.00 37.82 D000 O ANISOU 4478 O ILE B 151 4847 4465 5059 -294 -56 -124 D000 O ATOM 4479 CB ILE B 151 -14.070 -11.737 9.252 1.00 40.13 D000 C ANISOU 4479 CB ILE B 151 5121 4698 5430 -442 -36 -65 D000 C ATOM 4480 CG1 ILE B 151 -14.891 -13.018 9.139 1.00 52.15 D000 C ANISOU 4480 CG1 ILE B 151 6643 6131 7041 -526 -17 -65 D000 C ATOM 4481 CG2 ILE B 151 -14.470 -10.700 8.215 1.00 37.72 D000 C ANISOU 4481 CG2 ILE B 151 4792 4481 5060 -427 -21 2 D000 C ATOM 4482 CD1 ILE B 151 -14.781 -13.706 7.830 1.00 53.65 D000 C ANISOU 4482 CD1 ILE B 151 6867 6250 7266 -534 28 42 D000 C ATOM 4483 N VAL B 152 -11.048 -10.215 8.425 1.00 36.22 D000 N ANISOU 4483 N VAL B 152 4658 4240 4866 -262 -65 7 D000 N ATOM 4484 CA VAL B 152 -10.261 -8.996 8.590 1.00 35.97 D000 C ANISOU 4484 CA VAL B 152 4602 4266 4798 -214 -82 -3 D000 C ATOM 4485 C VAL B 152 -11.043 -7.822 8.011 1.00 38.25 D000 C ANISOU 4485 C VAL B 152 4879 4641 5013 -226 -87 13 D000 C ATOM 4486 O VAL B 152 -11.596 -7.917 6.910 1.00 38.78 D000 O ANISOU 4486 O VAL B 152 4964 4718 5050 -242 -85 63 D000 O ATOM 4487 CB VAL B 152 -8.877 -9.124 7.935 1.00 36.68 D000 C ANISOU 4487 CB VAL B 152 4690 4317 4928 -160 -110 41 D000 C ATOM 4488 CG1 VAL B 152 -8.057 -7.847 8.176 1.00 39.05 D000 C ANISOU 4488 CG1 VAL B 152 4951 4668 5220 -127 -125 24 D000 C ATOM 4489 CG2 VAL B 152 -8.177 -10.325 8.480 1.00 38.93 D000 C ANISOU 4489 CG2 VAL B 152 4985 4511 5294 -135 -92 31 D000 C ATOM 4490 N PHE B 153 -11.120 -6.740 8.789 1.00 35.29 D000 N ANISOU 4490 N PHE B 153 4481 4322 4604 -212 -82 -28 D000 N ATOM 4491 CA PHE B 153 -11.841 -5.507 8.486 1.00 36.18 D000 C ANISOU 4491 CA PHE B 153 4584 4508 4654 -210 -80 -24 D000 C ATOM 4492 C PHE B 153 -10.818 -4.386 8.317 1.00 36.04 D000 C ANISOU 4492 C PHE B 153 4565 4499 4631 -172 -95 -23 D000 C ATOM 4493 O PHE B 153 -9.956 -4.203 9.179 1.00 35.84 D000 O ANISOU 4493 O PHE B 153 4523 4453 4641 -151 -86 -44 D000 O ATOM 4494 CB PHE B 153 -12.822 -5.204 9.640 1.00 35.94 D000 C ANISOU 4494 CB PHE B 153 4531 4524 4601 -221 -66 -69 D000 C ATOM 4495 CG PHE B 153 -13.487 -3.843 9.593 1.00 37.57 D000 C ANISOU 4495 CG PHE B 153 4723 4801 4752 -199 -58 -67 D000 C ATOM 4496 CD1 PHE B 153 -12.789 -2.675 9.856 1.00 37.12 D000 C ANISOU 4496 CD1 PHE B 153 4675 4751 4677 -158 -53 -70 D000 C ATOM 4497 CD2 PHE B 153 -14.855 -3.753 9.361 1.00 40.56 D000 C ANISOU 4497 CD2 PHE B 153 5071 5230 5112 -219 -48 -60 D000 C ATOM 4498 CE1 PHE B 153 -13.421 -1.446 9.816 1.00 38.42 D000 C ANISOU 4498 CE1 PHE B 153 4836 4962 4799 -132 -40 -66 D000 C ATOM 4499 CE2 PHE B 153 -15.491 -2.533 9.340 1.00 37.54 D000 C ANISOU 4499 CE2 PHE B 153 4672 4904 4685 -185 -35 -55 D000 C ATOM 4500 CZ PHE B 153 -14.780 -1.378 9.573 1.00 40.94 D000 C ANISOU 4500 CZ PHE B 153 5129 5333 5091 -138 -32 -59 D000 C ATOM 4501 N PHE B 154 -10.904 -3.653 7.202 1.00 33.94 D000 N ANISOU 4501 N PHE B 154 4318 4256 4322 -165 -114 0 D000 N ATOM 4502 CA PHE B 154 -10.117 -2.446 6.963 1.00 34.55 D000 C ANISOU 4502 CA PHE B 154 4394 4336 4397 -144 -138 -11 D000 C ATOM 4503 C PHE B 154 -11.063 -1.310 6.598 1.00 41.62 D000 C ANISOU 4503 C PHE B 154 5312 5277 5225 -136 -119 -20 D000 C ATOM 4504 O PHE B 154 -11.931 -1.488 5.734 1.00 39.64 D000 O ANISOU 4504 O PHE B 154 5089 5052 4920 -139 -108 1 D000 O ATOM 4505 CB PHE B 154 -9.149 -2.592 5.798 1.00 37.13 D000 C ANISOU 4505 CB PHE B 154 4738 4636 4734 -135 -202 10 D000 C ATOM 4506 CG PHE B 154 -7.746 -2.882 6.199 1.00 38.75 D000 C ANISOU 4506 CG PHE B 154 4895 4797 5031 -124 -232 8 D000 C ATOM 4507 CD1 PHE B 154 -7.429 -4.088 6.779 1.00 44.78 D000 C ANISOU 4507 CD1 PHE B 154 5640 5524 5852 -117 -212 20 D000 C ATOM 4508 CD2 PHE B 154 -6.752 -1.948 5.999 1.00 47.16 D000 C ANISOU 4508 CD2 PHE B 154 5929 5849 6139 -121 -275 -9 D000 C ATOM 4509 CE1 PHE B 154 -6.131 -4.367 7.152 1.00 48.33 D000 C ANISOU 4509 CE1 PHE B 154 6035 5932 6395 -94 -224 22 D000 C ATOM 4510 CE2 PHE B 154 -5.448 -2.221 6.373 1.00 47.19 D000 C ANISOU 4510 CE2 PHE B 154 5865 5815 6251 -110 -294 -5 D000 C ATOM 4511 CZ PHE B 154 -5.146 -3.428 6.954 1.00 44.99 D000 C ANISOU 4511 CZ PHE B 154 5564 5508 6024 -91 -262 13 D000 C ATOM 4512 N SER B 155 -10.881 -0.142 7.206 1.00 35.08 D000 N ANISOU 4512 N SER B 155 4474 4450 4403 -120 -104 -43 D000 N ATOM 4513 CA ASER B 155 -11.607 1.060 6.804 0.70 34.92 D000 C ANISOU 4513 CA ASER B 155 4482 4455 4330 -100 -86 -53 D000 C ATOM 4514 CA BSER B 155 -11.602 1.057 6.799 0.30 35.16 D000 C ANISOU 4514 CA BSER B 155 4512 4485 4360 -100 -86 -53 D000 C ATOM 4515 C SER B 155 -10.630 2.226 6.785 1.00 41.88 D000 C ANISOU 4515 C SER B 155 5372 5292 5247 -95 -104 -75 D000 C ATOM 4516 O SER B 155 -9.774 2.337 7.664 1.00 41.33 D000 O ANISOU 4516 O SER B 155 5267 5191 5245 -101 -94 -76 D000 O ATOM 4517 CB ASER B 155 -12.804 1.360 7.730 0.70 35.92 D000 C ANISOU 4517 CB ASER B 155 4587 4626 4433 -80 -37 -52 D000 C ATOM 4518 CB BSER B 155 -12.777 1.362 7.731 0.30 35.88 D000 C ANISOU 4518 CB BSER B 155 4584 4622 4429 -81 -37 -52 D000 C ATOM 4519 OG ASER B 155 -12.451 1.674 9.070 0.70 36.57 D000 O ANISOU 4519 OG ASER B 155 4651 4700 4543 -67 -19 -58 D000 O ATOM 4520 OG BSER B 155 -13.594 2.388 7.189 0.30 40.40 D000 O ANISOU 4520 OG BSER B 155 5180 5216 4954 -49 -12 -54 D000 O ATOM 4521 N ASP B 156 -10.768 3.094 5.783 1.00 35.66 D000 N ANISOU 4521 N ASP B 156 4633 4497 4417 -85 -123 -96 D000 N ATOM 4522 CA ASP B 156 -9.801 4.163 5.547 1.00 35.85 D000 C ANISOU 4522 CA ASP B 156 4669 4464 4487 -96 -158 -129 D000 C ATOM 4523 C ASP B 156 -10.533 5.405 5.069 1.00 37.38 D000 C ANISOU 4523 C ASP B 156 4926 4649 4626 -68 -132 -158 D000 C ATOM 4524 O ASP B 156 -11.409 5.317 4.207 1.00 38.07 D000 O ANISOU 4524 O ASP B 156 5065 4774 4627 -42 -121 -161 D000 O ATOM 4525 CB ASP B 156 -8.770 3.644 4.523 1.00 37.50 D000 C ANISOU 4525 CB ASP B 156 4883 4655 4711 -120 -252 -142 D000 C ATOM 4526 CG ASP B 156 -7.660 4.622 4.199 1.00 39.25 D000 C ANISOU 4526 CG ASP B 156 5098 4816 5001 -147 -316 -187 D000 C ATOM 4527 OD1 ASP B 156 -7.907 5.782 3.834 1.00 38.09 D000 O ANISOU 4527 OD1 ASP B 156 5004 4639 4831 -145 -314 -229 D000 O ATOM 4528 OD2 ASP B 156 -6.497 4.169 4.237 1.00 43.09 D000 O ANISOU 4528 OD2 ASP B 156 5519 5278 5573 -173 -374 -183 D000 O ATOM 4529 N ILE B 157 -10.185 6.562 5.651 1.00 36.39 D000 N ANISOU 4529 N ILE B 157 4801 4467 4559 -67 -107 -174 D000 N ATOM 4530 CA ILE B 157 -10.812 7.826 5.273 1.00 37.45 D000 C ANISOU 4530 CA ILE B 157 5001 4571 4658 -33 -76 -204 D000 C ATOM 4531 C ILE B 157 -10.464 8.207 3.839 1.00 38.78 D000 C ANISOU 4531 C ILE B 157 5243 4709 4782 -46 -146 -267 D000 C ATOM 4532 O ILE B 157 -9.304 8.140 3.404 1.00 37.18 D000 O ANISOU 4532 O ILE B 157 5029 4467 4630 -94 -233 -299 D000 O ATOM 4533 CB ILE B 157 -10.391 8.949 6.248 1.00 34.92 D000 C ANISOU 4533 CB ILE B 157 4670 4175 4424 -34 -31 -198 D000 C ATOM 4534 CG1 ILE B 157 -10.857 8.596 7.665 1.00 38.29 D000 C ANISOU 4534 CG1 ILE B 157 5049 4643 4856 -4 37 -135 D000 C ATOM 4535 CG2 ILE B 157 -10.911 10.327 5.761 1.00 40.10 D000 C ANISOU 4535 CG2 ILE B 157 5407 4770 5058 2 -2 -237 D000 C ATOM 4536 CD1 ILE B 157 -10.375 9.548 8.716 1.00 38.32 D000 C ANISOU 4536 CD1 ILE B 157 5050 4577 4934 2 95 -107 D000 C ATOM 4537 N VAL B 158 -11.482 8.643 3.102 1.00 37.67 D000 N ANISOU 4537 N VAL B 158 5180 4588 4546 5 -111 -288 D000 N ATOM 4538 CA VAL B 158 -11.313 9.127 1.739 1.00 38.05 D000 C ANISOU 4538 CA VAL B 158 5329 4608 4519 11 -165 -358 D000 C ATOM 4539 C VAL B 158 -10.706 10.527 1.737 1.00 38.51 D000 C ANISOU 4539 C VAL B 158 5430 4557 4644 -8 -188 -428 D000 C ATOM 4540 O VAL B 158 -11.228 11.442 2.383 1.00 41.44 D000 O ANISOU 4540 O VAL B 158 5810 4883 5052 25 -108 -420 D000 O ATOM 4541 CB VAL B 158 -12.665 9.119 1.001 1.00 39.70 D000 C ANISOU 4541 CB VAL B 158 5608 4874 4601 83 -90 -353 D000 C ATOM 4542 CG1 VAL B 158 -12.467 9.613 -0.408 1.00 43.21 D000 C ANISOU 4542 CG1 VAL B 158 6183 5291 4943 99 -141 -432 D000 C ATOM 4543 CG2 VAL B 158 -13.286 7.721 1.059 1.00 41.69 D000 C ANISOU 4543 CG2 VAL B 158 5805 5221 4815 86 -58 -279 D000 C ATOM 4544 N SER B 159 -9.580 10.682 1.024 1.00 38.84 D000 N ANISOU 4544 N SER B 159 5496 4550 4713 -64 -305 -493 D000 N ATOM 4545 CA ASER B 159 -8.964 11.984 0.778 0.82 42.57 D000 C ANISOU 4545 CA ASER B 159 6018 4905 5251 -98 -348 -580 D000 C ATOM 4546 CA BSER B 159 -8.952 11.982 0.778 0.18 42.70 D000 C ANISOU 4546 CA BSER B 159 6034 4921 5268 -98 -349 -580 D000 C ATOM 4547 C SER B 159 -8.626 12.709 2.080 1.00 45.61 D000 C ANISOU 4547 C SER B 159 6329 5208 5792 -127 -279 -543 D000 C ATOM 4548 O SER B 159 -8.774 13.927 2.191 1.00 48.14 D000 O ANISOU 4548 O SER B 159 6707 5429 6156 -120 -236 -582 D000 O ATOM 4549 CB ASER B 159 -9.866 12.854 -0.111 0.82 45.92 D000 C ANISOU 4549 CB ASER B 159 6588 5302 5557 -32 -311 -649 D000 C ATOM 4550 CB BSER B 159 -9.830 12.854 -0.127 0.18 46.18 D000 C ANISOU 4550 CB BSER B 159 6621 5334 5591 -34 -315 -651 D000 C ATOM 4551 OG ASER B 159 -9.093 13.775 -0.858 0.82 60.64 D000 O ANISOU 4551 OG ASER B 159 8530 7064 7444 -77 -410 -765 D000 O ATOM 4552 OG BSER B 159 -10.856 13.488 0.613 0.18 52.50 D000 O ANISOU 4552 OG BSER B 159 7427 6117 6404 30 -178 -610 D000 O ATOM 4553 N PHE B 160 -8.147 11.958 3.072 1.00 42.77 D000 N ANISOU 4553 N PHE B 160 5852 4883 5515 -156 -259 -467 D000 N ATOM 4554 CA PHE B 160 -7.723 12.579 4.325 1.00 40.31 D000 C ANISOU 4554 CA PHE B 160 5477 4498 5340 -180 -184 -421 D000 C ATOM 4555 C PHE B 160 -6.627 13.616 4.117 1.00 46.75 D000 C ANISOU 4555 C PHE B 160 6288 5180 6295 -260 -236 -485 D000 C ATOM 4556 O PHE B 160 -6.556 14.599 4.863 1.00 47.65 D000 O ANISOU 4556 O PHE B 160 6405 5195 6505 -268 -153 -463 D000 O ATOM 4557 CB PHE B 160 -7.219 11.516 5.291 1.00 41.97 D000 C ANISOU 4557 CB PHE B 160 5574 4768 5606 -198 -162 -342 D000 C ATOM 4558 CG PHE B 160 -6.749 12.074 6.603 1.00 48.37 D000 C ANISOU 4558 CG PHE B 160 6329 5511 6538 -215 -69 -284 D000 C ATOM 4559 CD1 PHE B 160 -7.660 12.421 7.583 1.00 54.24 D000 C ANISOU 4559 CD1 PHE B 160 7103 6266 7240 -147 42 -220 D000 C ATOM 4560 CD2 PHE B 160 -5.404 12.257 6.848 1.00 54.98 D000 C ANISOU 4560 CD2 PHE B 160 7082 6276 7533 -293 -91 -287 D000 C ATOM 4561 CE1 PHE B 160 -7.227 12.935 8.797 1.00 52.60 D000 C ANISOU 4561 CE1 PHE B 160 6864 5998 7124 -151 136 -155 D000 C ATOM 4562 CE2 PHE B 160 -4.972 12.780 8.053 1.00 54.68 D000 C ANISOU 4562 CE2 PHE B 160 7000 6172 7604 -304 19 -221 D000 C ATOM 4563 CZ PHE B 160 -5.892 13.113 9.021 1.00 50.41 D000 C ANISOU 4563 CZ PHE B 160 6513 5644 6998 -230 135 -153 D000 C ATOM 4564 N SER B 161 -5.752 13.404 3.131 1.00 43.79 D000 N ANISOU 4564 N SER B 161 5902 4796 5940 -320 -375 -560 D000 N ATOM 4565 CA SER B 161 -4.627 14.314 2.931 1.00 51.09 D000 C ANISOU 4565 CA SER B 161 6796 5593 7023 -414 -446 -630 D000 C ATOM 4566 C SER B 161 -5.112 15.738 2.738 1.00 54.07 D000 C ANISOU 4566 C SER B 161 7290 5847 7408 -405 -401 -693 D000 C ATOM 4567 O SER B 161 -4.396 16.702 3.039 1.00 54.61 D000 O ANISOU 4567 O SER B 161 7330 5777 7640 -479 -394 -720 D000 O ATOM 4568 CB SER B 161 -3.810 13.868 1.721 1.00 59.84 D000 C ANISOU 4568 CB SER B 161 7894 6727 8114 -463 -633 -716 D000 C ATOM 4569 OG SER B 161 -3.066 12.700 2.018 1.00 64.55 D000 O ANISOU 4569 OG SER B 161 8358 7402 8766 -482 -675 -654 D000 O ATOM 4570 N THR B 162 -6.333 15.882 2.243 1.00 49.09 D000 N ANISOU 4570 N THR B 162 6786 5256 6612 -314 -359 -713 D000 N ATOM 4571 CA THR B 162 -6.905 17.199 2.016 1.00 57.85 D000 C ANISOU 4571 CA THR B 162 8017 6247 7715 -282 -305 -774 D000 C ATOM 4572 C THR B 162 -7.192 17.902 3.337 1.00 59.00 D000 C ANISOU 4572 C THR B 162 8135 6315 7965 -258 -153 -679 D000 C ATOM 4573 O THR B 162 -6.893 19.094 3.492 1.00 56.37 D000 O ANISOU 4573 O THR B 162 7844 5824 7749 -294 -122 -714 D000 O ATOM 4574 CB THR B 162 -8.172 17.038 1.180 1.00 64.99 D000 C ANISOU 4574 CB THR B 162 9048 7231 8414 -175 -280 -804 D000 C ATOM 4575 CG2 THR B 162 -8.912 18.363 1.052 1.00 79.30 D000 C ANISOU 4575 CG2 THR B 162 10988 8926 10218 -114 -196 -854 D000 C ATOM 4576 OG1 THR B 162 -7.806 16.576 -0.127 1.00 59.22 D000 O ANISOU 4576 OG1 THR B 162 8374 6547 7579 -197 -422 -898 D000 O ATOM 4577 N PHE B 163 -7.796 17.185 4.293 1.00 50.76 D000 N ANISOU 4577 N PHE B 163 7032 5378 6875 -194 -61 -560 D000 N ATOM 4578 CA PHE B 163 -8.008 17.744 5.625 1.00 48.96 D000 C ANISOU 4578 CA PHE B 163 6781 5095 6726 -162 73 -457 D000 C ATOM 4579 C PHE B 163 -6.698 18.298 6.171 1.00 46.05 D000 C ANISOU 4579 C PHE B 163 6342 4596 6557 -269 80 -446 D000 C ATOM 4580 O PHE B 163 -6.628 19.443 6.628 1.00 53.72 D000 O ANISOU 4580 O PHE B 163 7357 5424 7631 -275 161 -428 D000 O ATOM 4581 CB PHE B 163 -8.530 16.683 6.605 1.00 48.06 D000 C ANISOU 4581 CB PHE B 163 6594 5125 6542 -103 132 -344 D000 C ATOM 4582 CG PHE B 163 -9.935 16.203 6.344 1.00 48.78 D000 C ANISOU 4582 CG PHE B 163 6728 5337 6470 1 153 -330 D000 C ATOM 4583 CD1 PHE B 163 -10.174 15.157 5.468 1.00 62.02 D000 C ANISOU 4583 CD1 PHE B 163 8396 7128 8042 0 78 -368 D000 C ATOM 4584 CD2 PHE B 163 -11.009 16.759 7.019 1.00 49.90 D000 C ANISOU 4584 CD2 PHE B 163 6907 5480 6573 103 251 -267 D000 C ATOM 4585 CE1 PHE B 163 -11.463 14.699 5.248 1.00 56.40 D000 C ANISOU 4585 CE1 PHE B 163 7706 6522 7203 87 113 -346 D000 C ATOM 4586 CE2 PHE B 163 -12.298 16.313 6.799 1.00 51.70 D000 C ANISOU 4586 CE2 PHE B 163 7146 5821 6676 194 270 -252 D000 C ATOM 4587 CZ PHE B 163 -12.525 15.277 5.922 1.00 51.46 D000 C ANISOU 4587 CZ PHE B 163 7098 5898 6556 180 208 -291 D000 C ATOM 4588 N ALA B 164 -5.649 17.472 6.129 1.00 52.66 D000 N ANISOU 4588 N ALA B 164 7065 5479 7463 -352 4 -449 D000 N ATOM 4589 CA ALA B 164 -4.365 17.836 6.714 1.00 52.37 D000 C ANISOU 4589 CA ALA B 164 6926 5338 7634 -455 24 -424 D000 C ATOM 4590 C ALA B 164 -3.781 19.080 6.069 1.00 65.31 D000 C ANISOU 4590 C ALA B 164 8606 6799 9411 -543 -27 -524 D000 C ATOM 4591 O ALA B 164 -3.029 19.819 6.715 1.00 61.94 D000 O ANISOU 4591 O ALA B 164 8126 6237 9172 -616 44 -487 D000 O ATOM 4592 CB ALA B 164 -3.391 16.664 6.577 1.00 52.40 D000 C ANISOU 4592 CB ALA B 164 6793 5433 7682 -515 -66 -424 D000 C ATOM 4593 N GLU B 165 -4.114 19.332 4.804 1.00 62.39 D000 N ANISOU 4593 N GLU B 165 8337 6418 8949 -539 -143 -653 D000 N ATOM 4594 CA GLU B 165 -3.522 20.461 4.100 1.00 71.97 D000 C ANISOU 4594 CA GLU B 165 9599 7458 10287 -631 -218 -775 D000 C ATOM 4595 C GLU B 165 -4.270 21.760 4.364 1.00 68.75 D000 C ANISOU 4595 C GLU B 165 9326 6902 9894 -580 -98 -774 D000 C ATOM 4596 O GLU B 165 -3.666 22.836 4.302 1.00 68.36 D000 O ANISOU 4596 O GLU B 165 9295 6663 10015 -669 -100 -831 D000 O ATOM 4597 CB GLU B 165 -3.485 20.177 2.596 1.00 82.31 D000 C ANISOU 4597 CB GLU B 165 10978 8818 11476 -644 -406 -925 D000 C ATOM 4598 CG GLU B 165 -2.087 19.942 2.049 1.00105.64 D000 C ANISOU 4598 CG GLU B 165 13816 11752 14570 -778 -580 -1005 D000 C ATOM 4599 CD GLU B 165 -1.204 21.170 2.165 1.00142.94 D000 C ANISOU 4599 CD GLU B 165 18507 16265 19538 -907 -594 -1069 D000 C ATOM 4600 OE1 GLU B 165 -0.199 21.113 2.904 1.00143.73 D000 O ANISOU 4600 OE1 GLU B 165 18437 16321 19852 -1001 -563 -1002 D000 O ATOM 4601 OE2 GLU B 165 -1.517 22.194 1.520 1.00140.09 D000 O ANISOU 4601 OE2 GLU B 165 18291 15774 19163 -916 -625 -1187 D000 O ATOM 4602 N LYS B 166 -5.563 21.681 4.683 1.00 61.39 D000 N ANISOU 4602 N LYS B 166 8480 6043 8802 -439 6 -708 D000 N ATOM 4603 CA LYS B 166 -6.428 22.848 4.710 1.00 64.46 D000 C ANISOU 4603 CA LYS B 166 9012 6307 9175 -360 102 -719 D000 C ATOM 4604 C LYS B 166 -6.852 23.301 6.102 1.00 68.08 D000 C ANISOU 4604 C LYS B 166 9462 6718 9686 -291 279 -561 D000 C ATOM 4605 O LYS B 166 -7.279 24.449 6.251 1.00 66.90 D000 O ANISOU 4605 O LYS B 166 9418 6416 9586 -246 365 -558 D000 O ATOM 4606 CB LYS B 166 -7.698 22.567 3.891 1.00 72.34 D000 C ANISOU 4606 CB LYS B 166 10123 7415 9949 -232 88 -770 D000 C ATOM 4607 CG LYS B 166 -7.437 22.187 2.439 1.00 88.94 D000 C ANISOU 4607 CG LYS B 166 12276 9565 11954 -273 -74 -923 D000 C ATOM 4608 CD LYS B 166 -6.826 23.334 1.649 1.00107.43 D000 C ANISOU 4608 CD LYS B 166 14716 11710 14394 -356 -152 -1079 D000 C ATOM 4609 CE LYS B 166 -6.394 22.883 0.262 1.00112.18 D000 C ANISOU 4609 CE LYS B 166 15364 12371 14891 -404 -341 -1231 D000 C ATOM 4610 NZ LYS B 166 -7.211 23.510 -0.812 1.00118.85 D000 N ANISOU 4610 NZ LYS B 166 16410 13169 15581 -319 -348 -1361 D000 N ATOM 4611 N LEU B 167 -6.754 22.441 7.115 1.00 52.41 D000 N ANISOU 4611 N LEU B 167 7369 4856 7687 -272 335 -431 D000 N ATOM 4612 CA LEU B 167 -7.276 22.711 8.449 1.00 47.66 D000 C ANISOU 4612 CA LEU B 167 6776 4250 7083 -182 490 -275 D000 C ATOM 4613 C LEU B 167 -6.147 22.885 9.464 1.00 48.19 D000 C ANISOU 4613 C LEU B 167 6752 4230 7327 -272 570 -180 D000 C ATOM 4614 O LEU B 167 -5.062 22.324 9.290 1.00 50.46 D000 O ANISOU 4614 O LEU B 167 6925 4537 7711 -387 504 -213 D000 O ATOM 4615 CB LEU B 167 -8.169 21.561 8.931 1.00 50.47 D000 C ANISOU 4615 CB LEU B 167 7095 4823 7259 -74 500 -196 D000 C ATOM 4616 CG LEU B 167 -9.424 21.232 8.124 1.00 59.41 D000 C ANISOU 4616 CG LEU B 167 8291 6068 8214 28 454 -253 D000 C ATOM 4617 CD1 LEU B 167 -10.128 20.015 8.710 1.00 58.03 D000 C ANISOU 4617 CD1 LEU B 167 8049 6097 7904 101 459 -173 D000 C ATOM 4618 CD2 LEU B 167 -10.342 22.436 8.110 1.00 61.78 D000 C ANISOU 4618 CD2 LEU B 167 8712 6257 8505 133 536 -247 D000 C ATOM 4619 N PRO B 168 -6.378 23.639 10.545 1.00 48.55 D000 N ANISOU 4619 N PRO B 168 6845 4183 7420 -213 721 -53 D000 N ATOM 4620 CA PRO B 168 -5.401 23.664 11.641 1.00 52.17 D000 C ANISOU 4620 CA PRO B 168 7220 4585 8016 -276 830 65 D000 C ATOM 4621 C PRO B 168 -5.236 22.281 12.250 1.00 50.08 D000 C ANISOU 4621 C PRO B 168 6852 4521 7654 -256 822 127 D000 C ATOM 4622 O PRO B 168 -6.142 21.445 12.208 1.00 45.81 D000 O ANISOU 4622 O PRO B 168 6326 4153 6926 -161 773 125 D000 O ATOM 4623 CB PRO B 168 -6.011 24.653 12.644 1.00 53.38 D000 C ANISOU 4623 CB PRO B 168 7483 4632 8169 -171 993 202 D000 C ATOM 4624 CG PRO B 168 -6.965 25.468 11.839 1.00 59.86 D000 C ANISOU 4624 CG PRO B 168 8431 5374 8939 -99 957 120 D000 C ATOM 4625 CD PRO B 168 -7.532 24.504 10.843 1.00 52.42 D000 C ANISOU 4625 CD PRO B 168 7467 4613 7837 -74 809 1 D000 C ATOM 4626 N AVAL B 169 -4.059 22.053 12.834 0.65 48.08 D000 N ANISOU 4626 N AVAL B 169 6489 4235 7543 -348 881 182 D000 N ATOM 4627 N BVAL B 169 -4.062 22.060 12.849 0.35 48.11 D000 N ANISOU 4627 N BVAL B 169 6494 4239 7547 -347 883 184 D000 N ATOM 4628 CA AVAL B 169 -3.696 20.717 13.298 0.65 47.38 D000 C ANISOU 4628 CA AVAL B 169 6296 4317 7390 -344 869 219 D000 C ATOM 4629 CA BVAL B 169 -3.692 20.723 13.305 0.35 47.40 D000 C ANISOU 4629 CA BVAL B 169 6298 4318 7394 -344 870 220 D000 C ATOM 4630 C AVAL B 169 -4.725 20.173 14.287 0.65 45.58 D000 C ANISOU 4630 C AVAL B 169 6133 4230 6956 -194 936 322 D000 C ATOM 4631 C BVAL B 169 -4.720 20.173 14.288 0.35 45.62 D000 C ANISOU 4631 C BVAL B 169 6137 4235 6961 -194 937 322 D000 C ATOM 4632 O AVAL B 169 -5.091 18.994 14.234 0.65 44.25 D000 O ANISOU 4632 O AVAL B 169 5930 4233 6651 -153 864 298 D000 O ATOM 4633 O BVAL B 169 -5.087 18.994 14.228 0.35 44.45 D000 O ANISOU 4633 O BVAL B 169 5954 4257 6676 -154 863 297 D000 O ATOM 4634 CB AVAL B 169 -2.282 20.749 13.910 0.65 50.34 D000 C ANISOU 4634 CB AVAL B 169 6547 4610 7970 -450 963 282 D000 C ATOM 4635 CB BVAL B 169 -2.279 20.744 13.921 0.35 50.27 D000 C ANISOU 4635 CB BVAL B 169 6538 4602 7961 -449 964 283 D000 C ATOM 4636 CG1AVAL B 169 -2.038 19.537 14.768 0.65 45.16 D000 C ANISOU 4636 CG1AVAL B 169 5818 4108 7231 -404 1015 357 D000 C ATOM 4637 CG1BVAL B 169 -1.294 21.407 12.969 0.35 51.93 D000 C ANISOU 4637 CG1BVAL B 169 6673 4658 8399 -606 884 178 D000 C ATOM 4638 CG2AVAL B 169 -1.240 20.840 12.808 0.65 55.59 D000 C ANISOU 4638 CG2AVAL B 169 7099 5198 8822 -604 835 156 D000 C ATOM 4639 CG2BVAL B 169 -2.285 21.464 15.261 0.35 46.38 D000 C ANISOU 4639 CG2BVAL B 169 6105 4019 7497 -394 1173 446 D000 C ATOM 4640 N GLU B 170 -5.194 21.008 15.215 1.00 48.62 D000 N ANISOU 4640 N GLU B 170 6615 4543 7317 -109 1070 438 D000 N ATOM 4641 CA GLU B 170 -6.141 20.515 16.212 1.00 47.12 D000 C ANISOU 4641 CA GLU B 170 6484 4491 6927 36 1116 533 D000 C ATOM 4642 C GLU B 170 -7.430 20.016 15.576 1.00 48.69 D000 C ANISOU 4642 C GLU B 170 6718 4826 6954 120 990 460 D000 C ATOM 4643 O GLU B 170 -8.036 19.057 16.066 1.00 49.19 D000 O ANISOU 4643 O GLU B 170 6772 5054 6863 193 960 483 D000 O ATOM 4644 CB GLU B 170 -6.458 21.609 17.218 1.00 52.16 D000 C ANISOU 4644 CB GLU B 170 7234 5019 7565 124 1266 674 D000 C ATOM 4645 CG GLU B 170 -5.281 21.969 18.050 1.00 72.45 D000 C ANISOU 4645 CG GLU B 170 9772 7474 10280 59 1423 777 D000 C ATOM 4646 CD GLU B 170 -5.657 22.116 19.483 1.00 97.52 D000 C ANISOU 4646 CD GLU B 170 13043 10681 13329 190 1563 944 D000 C ATOM 4647 OE1 GLU B 170 -6.448 23.031 19.799 1.00121.28 D000 O ANISOU 4647 OE1 GLU B 170 16173 13621 16287 292 1610 1019 D000 O ATOM 4648 OE2 GLU B 170 -5.152 21.340 20.322 1.00 88.75 D000 O ANISOU 4648 OE2 GLU B 170 11896 9660 12165 200 1632 1004 D000 O ATOM 4649 N GLU B 171 -7.867 20.654 14.495 1.00 47.39 D000 N ANISOU 4649 N GLU B 171 6596 4593 6818 109 922 368 D000 N ATOM 4650 CA AGLU B 171 -9.099 20.219 13.851 0.44 45.43 D000 C ANISOU 4650 CA AGLU B 171 6373 4468 6418 191 826 305 D000 C ATOM 4651 CA BGLU B 171 -9.095 20.237 13.826 0.56 45.35 D000 C ANISOU 4651 CA BGLU B 171 6365 4457 6411 190 825 303 D000 C ATOM 4652 C GLU B 171 -8.895 18.935 13.061 1.00 50.08 D000 C ANISOU 4652 C GLU B 171 6876 5192 6961 126 704 208 D000 C ATOM 4653 O GLU B 171 -9.799 18.094 13.010 1.00 45.79 D000 O ANISOU 4653 O GLU B 171 6321 4800 6277 192 650 200 D000 O ATOM 4654 CB AGLU B 171 -9.632 21.327 12.947 0.44 55.27 D000 C ANISOU 4654 CB AGLU B 171 7706 5593 7702 215 813 239 D000 C ATOM 4655 CB BGLU B 171 -9.565 21.341 12.880 0.56 55.24 D000 C ANISOU 4655 CB BGLU B 171 7701 5582 7707 206 809 232 D000 C ATOM 4656 CG AGLU B 171 -10.408 22.396 13.694 0.44 63.93 D000 C ANISOU 4656 CG AGLU B 171 8903 6606 8781 341 917 344 D000 C ATOM 4657 CG BGLU B 171 -10.985 21.814 13.110 0.56 70.83 D000 C ANISOU 4657 CG BGLU B 171 9756 7589 9568 364 840 280 D000 C ATOM 4658 CD AGLU B 171 -11.742 22.698 13.042 0.44 76.14 D000 C ANISOU 4658 CD AGLU B 171 10508 8190 10231 456 880 299 D000 C ATOM 4659 CD BGLU B 171 -11.189 23.242 12.643 0.56 74.84 D000 C ANISOU 4659 CD BGLU B 171 10368 7904 10164 392 890 256 D000 C ATOM 4660 OE1AGLU B 171 -12.704 21.930 13.268 0.44 75.11 D000 O ANISOU 4660 OE1AGLU B 171 10344 8234 9960 546 839 322 D000 O ATOM 4661 OE1BGLU B 171 -11.265 23.456 11.414 0.56 67.00 D000 O ANISOU 4661 OE1BGLU B 171 9402 6866 9188 354 824 126 D000 O ATOM 4662 OE2AGLU B 171 -11.827 23.701 12.302 0.44 78.54 D000 O ANISOU 4662 OE2AGLU B 171 10889 8344 10608 456 894 235 D000 O ATOM 4663 OE2BGLU B 171 -11.265 24.147 13.503 0.56 74.13 D000 O ANISOU 4663 OE2BGLU B 171 10345 7701 10120 456 999 367 D000 O ATOM 4664 N VAL B 172 -7.719 18.758 12.457 1.00 42.78 D000 N ANISOU 4664 N VAL B 172 5885 4212 6160 -1 657 141 D000 N ATOM 4665 CA VAL B 172 -7.411 17.512 11.765 1.00 41.54 D000 C ANISOU 4665 CA VAL B 172 5646 4174 5963 -56 544 66 D000 C ATOM 4666 C VAL B 172 -7.479 16.337 12.731 1.00 40.90 D000 C ANISOU 4666 C VAL B 172 5511 4232 5797 -16 570 137 D000 C ATOM 4667 O VAL B 172 -8.074 15.296 12.431 1.00 40.12 D000 O ANISOU 4667 O VAL B 172 5392 4268 5583 13 498 105 D000 O ATOM 4668 CB VAL B 172 -6.025 17.597 11.097 1.00 43.19 D000 C ANISOU 4668 CB VAL B 172 5779 4292 6338 -193 486 -3 D000 C ATOM 4669 CG1 VAL B 172 -5.687 16.256 10.438 1.00 42.43 D000 C ANISOU 4669 CG1 VAL B 172 5603 4324 6197 -232 368 -63 D000 C ATOM 4670 CG2 VAL B 172 -5.956 18.749 10.098 1.00 48.07 D000 C ANISOU 4670 CG2 VAL B 172 6463 4765 7034 -240 440 -97 D000 C ATOM 4671 N VAL B 173 -6.827 16.470 13.890 1.00 39.18 D000 N ANISOU 4671 N VAL B 173 5274 3976 5638 -18 680 230 D000 N ATOM 4672 CA VAL B 173 -6.831 15.385 14.868 1.00 38.69 D000 C ANISOU 4672 CA VAL B 173 5179 4035 5486 25 713 287 D000 C ATOM 4673 C VAL B 173 -8.248 15.134 15.373 1.00 41.03 D000 C ANISOU 4673 C VAL B 173 5544 4445 5602 145 702 320 D000 C ATOM 4674 O VAL B 173 -8.639 13.987 15.620 1.00 40.62 D000 O ANISOU 4674 O VAL B 173 5465 4522 5445 172 654 307 D000 O ATOM 4675 CB VAL B 173 -5.844 15.706 16.013 1.00 43.28 D000 C ANISOU 4675 CB VAL B 173 5743 4542 6160 9 856 386 D000 C ATOM 4676 CG1 VAL B 173 -5.932 14.665 17.126 1.00 46.92 D000 C ANISOU 4676 CG1 VAL B 173 6203 5125 6500 75 904 442 D000 C ATOM 4677 CG2 VAL B 173 -4.416 15.770 15.472 1.00 44.14 D000 C ANISOU 4677 CG2 VAL B 173 5743 4558 6470 -120 853 347 D000 C ATOM 4678 N SER B 174 -9.057 16.186 15.494 1.00 43.64 D000 N ANISOU 4678 N SER B 174 5956 4723 5903 219 737 357 D000 N ATOM 4679 CA ASER B 174 -10.430 16.006 15.949 0.90 46.07 D000 C ANISOU 4679 CA ASER B 174 6309 5141 6055 338 713 390 D000 C ATOM 4680 CA BSER B 174 -10.434 16.010 15.946 0.10 46.15 D000 C ANISOU 4680 CA BSER B 174 6319 5150 6065 338 713 390 D000 C ATOM 4681 C SER B 174 -11.238 15.169 14.960 1.00 46.20 D000 C ANISOU 4681 C SER B 174 6283 5269 6002 333 595 299 D000 C ATOM 4682 O SER B 174 -12.027 14.307 15.364 1.00 42.93 D000 O ANISOU 4682 O SER B 174 5849 4987 5477 384 551 305 D000 O ATOM 4683 CB ASER B 174 -11.081 17.374 16.166 0.90 52.62 D000 C ANISOU 4683 CB ASER B 174 7227 5877 6889 425 774 451 D000 C ATOM 4684 CB BSER B 174 -11.094 17.373 16.154 0.10 52.52 D000 C ANISOU 4684 CB BSER B 174 7214 5865 6876 426 773 450 D000 C ATOM 4685 OG ASER B 174 -12.406 17.230 16.634 0.90 58.45 D000 O ANISOU 4685 OG ASER B 174 7991 6728 7490 549 742 488 D000 O ATOM 4686 OG BSER B 174 -12.375 17.235 16.743 0.10 57.94 D000 O ANISOU 4686 OG BSER B 174 7929 6662 7422 552 748 497 D000 O ATOM 4687 N VAL B 175 -11.037 15.392 13.657 1.00 40.99 D000 N ANISOU 4687 N VAL B 175 5613 4555 5407 270 545 213 D000 N ATOM 4688 CA VAL B 175 -11.753 14.623 12.639 1.00 41.31 D000 C ANISOU 4688 CA VAL B 175 5624 4692 5379 266 453 137 D000 C ATOM 4689 C VAL B 175 -11.364 13.150 12.699 1.00 42.56 D000 C ANISOU 4689 C VAL B 175 5710 4953 5508 213 399 116 D000 C ATOM 4690 O VAL B 175 -12.223 12.259 12.716 1.00 38.42 D000 O ANISOU 4690 O VAL B 175 5159 4544 4894 245 355 109 D000 O ATOM 4691 CB VAL B 175 -11.491 15.216 11.241 1.00 43.49 D000 C ANISOU 4691 CB VAL B 175 5929 4881 5713 215 414 49 D000 C ATOM 4692 CG1 VAL B 175 -12.014 14.276 10.146 1.00 46.53 D000 C ANISOU 4692 CG1 VAL B 175 6289 5368 6021 202 331 -21 D000 C ATOM 4693 CG2 VAL B 175 -12.128 16.598 11.143 1.00 47.66 D000 C ANISOU 4693 CG2 VAL B 175 6541 5312 6255 287 470 60 D000 C ATOM 4694 N VAL B 176 -10.062 12.861 12.723 1.00 38.23 D000 N ANISOU 4694 N VAL B 176 5122 4355 5049 130 402 105 D000 N ATOM 4695 CA VAL B 176 -9.669 11.456 12.681 1.00 34.88 D000 C ANISOU 4695 CA VAL B 176 4633 4015 4607 89 351 82 D000 C ATOM 4696 C VAL B 176 -10.088 10.749 13.966 1.00 36.17 D000 C ANISOU 4696 C VAL B 176 4795 4262 4685 145 386 136 D000 C ATOM 4697 O VAL B 176 -10.535 9.595 13.937 1.00 36.78 D000 O ANISOU 4697 O VAL B 176 4844 4434 4697 146 333 111 D000 O ATOM 4698 CB VAL B 176 -8.159 11.320 12.389 1.00 39.56 D000 C ANISOU 4698 CB VAL B 176 5167 4535 5327 -2 343 61 D000 C ATOM 4699 CG1 VAL B 176 -7.323 11.764 13.547 1.00 48.50 D000 C ANISOU 4699 CG1 VAL B 176 6288 5603 6536 -5 450 131 D000 C ATOM 4700 CG2 VAL B 176 -7.825 9.873 12.017 1.00 47.90 D000 C ANISOU 4700 CG2 VAL B 176 6162 5669 6367 -36 274 27 D000 C ATOM 4701 N ASN B 177 -9.985 11.429 15.107 1.00 37.32 D000 N ANISOU 4701 N ASN B 177 4982 4373 4824 195 473 208 D000 N ATOM 4702 CA ASN B 177 -10.391 10.803 16.360 1.00 38.65 D000 C ANISOU 4702 CA ASN B 177 5170 4626 4887 258 497 252 D000 C ATOM 4703 C ASN B 177 -11.901 10.573 16.396 1.00 39.96 D000 C ANISOU 4703 C ASN B 177 5350 4895 4938 327 430 243 D000 C ATOM 4704 O ASN B 177 -12.359 9.565 16.947 1.00 40.24 D000 O ANISOU 4704 O ASN B 177 5372 5026 4891 345 387 228 D000 O ATOM 4705 CB ASN B 177 -9.930 11.652 17.542 1.00 43.28 D000 C ANISOU 4705 CB ASN B 177 5816 5151 5478 307 613 343 D000 C ATOM 4706 CG ASN B 177 -8.430 11.526 17.807 1.00 40.49 D000 C ANISOU 4706 CG ASN B 177 5425 4724 5236 241 696 361 D000 C ATOM 4707 ND2 ASN B 177 -7.939 12.309 18.753 1.00 48.09 D000 N ANISOU 4707 ND2 ASN B 177 6436 5617 6220 274 821 451 D000 N ATOM 4708 OD1 ASN B 177 -7.729 10.741 17.167 1.00 42.62 D000 O ANISOU 4708 OD1 ASN B 177 5620 4998 5578 167 653 304 D000 O ATOM 4709 N SER B 178 -12.686 11.482 15.807 1.00 41.03 D000 N ANISOU 4709 N SER B 178 5505 5008 5077 365 419 245 D000 N ATOM 4710 CA SER B 178 -14.131 11.270 15.721 1.00 39.57 D000 C ANISOU 4710 CA SER B 178 5304 4922 4809 429 359 237 D000 C ATOM 4711 C SER B 178 -14.452 10.043 14.873 1.00 40.79 D000 C ANISOU 4711 C SER B 178 5392 5151 4956 368 282 166 D000 C ATOM 4712 O SER B 178 -15.312 9.234 15.231 1.00 40.13 D000 O ANISOU 4712 O SER B 178 5272 5168 4810 388 229 156 D000 O ATOM 4713 CB SER B 178 -14.815 12.500 15.122 1.00 43.41 D000 C ANISOU 4713 CB SER B 178 5821 5356 5318 486 380 250 D000 C ATOM 4714 OG SER B 178 -14.716 13.606 15.989 1.00 50.06 D000 O ANISOU 4714 OG SER B 178 6731 6129 6160 559 451 330 D000 O ATOM 4715 N TYR B 179 -13.762 9.895 13.745 1.00 37.71 D000 N ANISOU 4715 N TYR B 179 4986 4708 4632 291 272 117 D000 N ATOM 4716 CA TYR B 179 -13.923 8.717 12.897 1.00 36.06 D000 C ANISOU 4716 CA TYR B 179 4729 4556 4417 234 211 65 D000 C ATOM 4717 C TYR B 179 -13.568 7.435 13.641 1.00 39.10 D000 C ANISOU 4717 C TYR B 179 5083 4989 4782 203 188 59 D000 C ATOM 4718 O TYR B 179 -14.312 6.447 13.590 1.00 37.49 D000 O ANISOU 4718 O TYR B 179 4843 4861 4542 193 141 37 D000 O ATOM 4719 CB TYR B 179 -13.056 8.901 11.658 1.00 37.85 D000 C ANISOU 4719 CB TYR B 179 4964 4710 4708 170 199 22 D000 C ATOM 4720 CG TYR B 179 -12.946 7.700 10.775 1.00 37.84 D000 C ANISOU 4720 CG TYR B 179 4928 4750 4701 114 142 -17 D000 C ATOM 4721 CD1 TYR B 179 -14.013 7.285 9.992 1.00 37.74 D000 C ANISOU 4721 CD1 TYR B 179 4904 4798 4638 126 121 -31 D000 C ATOM 4722 CD2 TYR B 179 -11.767 6.979 10.716 1.00 40.02 D000 C ANISOU 4722 CD2 TYR B 179 5180 4997 5028 55 120 -29 D000 C ATOM 4723 CE1 TYR B 179 -13.890 6.192 9.170 1.00 38.98 D000 C ANISOU 4723 CE1 TYR B 179 5041 4980 4787 77 82 -52 D000 C ATOM 4724 CE2 TYR B 179 -11.644 5.900 9.905 1.00 40.06 D000 C ANISOU 4724 CE2 TYR B 179 5163 5030 5027 14 68 -53 D000 C ATOM 4725 CZ TYR B 179 -12.705 5.496 9.147 1.00 39.40 D000 C ANISOU 4725 CZ TYR B 179 5083 5001 4885 24 51 -62 D000 C ATOM 4726 OH TYR B 179 -12.538 4.403 8.325 1.00 43.38 D000 O ANISOU 4726 OH TYR B 179 5577 5523 5383 -14 11 -71 D000 O ATOM 4727 N PHE B 180 -12.437 7.428 14.352 1.00 37.43 D000 N ANISOU 4727 N PHE B 180 4888 4730 4605 187 230 77 D000 N ATOM 4728 CA PHE B 180 -12.027 6.224 15.062 1.00 36.14 D000 C ANISOU 4728 CA PHE B 180 4709 4601 4423 168 221 64 D000 C ATOM 4729 C PHE B 180 -13.006 5.874 16.179 1.00 37.54 D000 C ANISOU 4729 C PHE B 180 4905 4860 4497 227 201 73 D000 C ATOM 4730 O PHE B 180 -13.229 4.690 16.468 1.00 39.10 D000 O ANISOU 4730 O PHE B 180 5087 5106 4664 206 158 35 D000 O ATOM 4731 CB PHE B 180 -10.616 6.398 15.633 1.00 35.44 D000 C ANISOU 4731 CB PHE B 180 4629 4442 4395 153 293 89 D000 C ATOM 4732 CG PHE B 180 -9.509 6.356 14.605 1.00 34.85 D000 C ANISOU 4732 CG PHE B 180 4508 4300 4435 83 283 66 D000 C ATOM 4733 CD1 PHE B 180 -9.655 5.687 13.392 1.00 37.10 D000 C ANISOU 4733 CD1 PHE B 180 4760 4601 4734 39 205 21 D000 C ATOM 4734 CD2 PHE B 180 -8.296 6.964 14.877 1.00 41.76 D000 C ANISOU 4734 CD2 PHE B 180 5367 5093 5405 63 351 95 D000 C ATOM 4735 CE1 PHE B 180 -8.620 5.646 12.466 1.00 39.22 D000 C ANISOU 4735 CE1 PHE B 180 4992 4816 5095 -16 175 1 D000 C ATOM 4736 CE2 PHE B 180 -7.258 6.917 13.954 1.00 40.85 D000 C ANISOU 4736 CE2 PHE B 180 5193 4922 5405 -3 320 69 D000 C ATOM 4737 CZ PHE B 180 -7.410 6.255 12.763 1.00 39.07 D000 C ANISOU 4737 CZ PHE B 180 4944 4723 5179 -38 224 20 D000 C ATOM 4738 N ASER B 181 -13.600 6.885 16.814 0.64 37.66 D000 N ANISOU 4738 N ASER B 181 4959 4887 4461 301 224 119 D000 N ATOM 4739 N BSER B 181 -13.573 6.887 16.834 0.36 37.87 D000 N ANISOU 4739 N BSER B 181 4987 4913 4488 301 225 120 D000 N ATOM 4740 CA ASER B 181 -14.562 6.640 17.883 0.64 41.84 D000 C ANISOU 4740 CA ASER B 181 5508 5505 4886 366 182 128 D000 C ATOM 4741 CA BSER B 181 -14.559 6.637 17.879 0.36 41.90 D000 C ANISOU 4741 CA BSER B 181 5515 5512 4893 366 182 128 D000 C ATOM 4742 C ASER B 181 -15.837 6.001 17.351 0.64 39.21 D000 C ANISOU 4742 C ASER B 181 5105 5252 4540 352 91 85 D000 C ATOM 4743 C BSER B 181 -15.791 5.950 17.307 0.36 39.31 D000 C ANISOU 4743 C BSER B 181 5117 5263 4556 346 91 83 D000 C ATOM 4744 O ASER B 181 -16.384 5.082 17.971 0.64 41.45 D000 O ANISOU 4744 O ASER B 181 5373 5605 4770 348 25 50 D000 O ATOM 4745 O BSER B 181 -16.254 4.932 17.835 0.36 41.70 D000 O ANISOU 4745 O BSER B 181 5401 5629 4815 333 28 42 D000 O ATOM 4746 CB ASER B 181 -14.883 7.954 18.591 0.64 43.43 D000 C ANISOU 4746 CB ASER B 181 5767 5694 5039 462 224 203 D000 C ATOM 4747 CB BSER B 181 -14.940 7.955 18.554 0.36 43.42 D000 C ANISOU 4747 CB BSER B 181 5763 5696 5038 462 221 202 D000 C ATOM 4748 OG ASER B 181 -13.777 8.389 19.357 0.64 49.90 D000 O ANISOU 4748 OG ASER B 181 6655 6448 5858 478 320 252 D000 O ATOM 4749 OG BSER B 181 -15.857 7.735 19.609 0.36 46.59 D000 O ANISOU 4749 OG BSER B 181 6184 6191 5326 536 161 211 D000 O ATOM 4750 N VAL B 182 -16.333 6.500 16.218 1.00 38.10 D000 N ANISOU 4750 N VAL B 182 4925 5100 4451 343 90 87 D000 N ATOM 4751 CA VAL B 182 -17.489 5.898 15.552 1.00 39.48 D000 C ANISOU 4751 CA VAL B 182 5021 5343 4636 322 32 56 D000 C ATOM 4752 C VAL B 182 -17.223 4.438 15.198 1.00 42.36 D000 C ANISOU 4752 C VAL B 182 5351 5714 5028 231 -3 3 D000 C ATOM 4753 O VAL B 182 -18.034 3.554 15.499 1.00 40.83 D000 O ANISOU 4753 O VAL B 182 5107 5584 4822 210 -64 -27 D000 O ATOM 4754 CB VAL B 182 -17.850 6.709 14.294 1.00 42.84 D000 C ANISOU 4754 CB VAL B 182 5430 5739 5107 333 68 67 D000 C ATOM 4755 CG1 VAL B 182 -18.839 5.939 13.410 1.00 47.78 D000 C ANISOU 4755 CG1 VAL B 182 5975 6424 5758 295 38 40 D000 C ATOM 4756 CG2 VAL B 182 -18.407 8.055 14.702 1.00 47.42 D000 C ANISOU 4756 CG2 VAL B 182 6035 6315 5665 435 95 117 D000 C ATOM 4757 N CYS B 183 -16.109 4.164 14.514 1.00 37.86 D000 N ANISOU 4757 N CYS B 183 4805 5075 4507 176 30 -8 D000 N ATOM 4758 CA CYS B 183 -15.860 2.790 14.086 1.00 36.79 D000 C ANISOU 4758 CA CYS B 183 4642 4935 4403 101 2 -47 D000 C ATOM 4759 C CYS B 183 -15.645 1.862 15.272 1.00 38.55 D000 C ANISOU 4759 C CYS B 183 4881 5172 4592 95 -24 -77 D000 C ATOM 4760 O CYS B 183 -16.144 0.731 15.271 1.00 38.19 D000 O ANISOU 4760 O CYS B 183 4804 5150 4557 49 -71 -116 D000 O ATOM 4761 CB CYS B 183 -14.649 2.699 13.146 1.00 39.24 D000 C ANISOU 4761 CB CYS B 183 4971 5170 4770 58 29 -47 D000 C ATOM 4762 SG CYS B 183 -14.735 3.638 11.632 1.00 40.92 D000 S ANISOU 4762 SG CYS B 183 5190 5354 5003 59 47 -35 D000 S ATOM 4763 N THR B 184 -14.871 2.303 16.271 1.00 37.10 D000 N ANISOU 4763 N THR B 184 4757 4967 4372 138 14 -62 D000 N ATOM 4764 CA THR B 184 -14.574 1.443 17.408 1.00 39.17 D000 C ANISOU 4764 CA THR B 184 5059 5240 4586 144 3 -98 D000 C ATOM 4765 C THR B 184 -15.843 1.046 18.147 1.00 39.35 D000 C ANISOU 4765 C THR B 184 5068 5345 4538 161 -82 -134 D000 C ATOM 4766 O THR B 184 -16.006 -0.112 18.542 1.00 38.73 D000 O ANISOU 4766 O THR B 184 4992 5274 4449 124 -131 -196 D000 O ATOM 4767 CB THR B 184 -13.616 2.146 18.374 1.00 41.58 D000 C ANISOU 4767 CB THR B 184 5434 5513 4849 203 81 -61 D000 C ATOM 4768 CG2 THR B 184 -13.499 1.351 19.660 1.00 50.72 D000 C ANISOU 4768 CG2 THR B 184 6655 6696 5921 231 74 -101 D000 C ATOM 4769 OG1 THR B 184 -12.323 2.241 17.768 1.00 44.04 D000 O ANISOU 4769 OG1 THR B 184 5736 5745 5252 170 148 -43 D000 O ATOM 4770 N ALA B 185 -16.749 2.003 18.364 1.00 38.89 D000 N ANISOU 4770 N ALA B 185 4995 5344 4437 220 -107 -98 D000 N ATOM 4771 CA ALA B 185 -17.953 1.704 19.129 1.00 42.99 D000 C ANISOU 4771 CA ALA B 185 5488 5952 4894 244 -207 -130 D000 C ATOM 4772 C ALA B 185 -18.787 0.630 18.441 1.00 40.87 D000 C ANISOU 4772 C ALA B 185 5124 5705 4700 157 -274 -183 D000 C ATOM 4773 O ALA B 185 -19.302 -0.286 19.099 1.00 41.04 D000 O ANISOU 4773 O ALA B 185 5133 5761 4698 126 -358 -249 D000 O ATOM 4774 CB ALA B 185 -18.763 2.986 19.344 1.00 42.06 D000 C ANISOU 4774 CB ALA B 185 5357 5888 4737 334 -220 -68 D000 C ATOM 4775 N ILE B 186 -18.909 0.708 17.116 1.00 38.59 D000 N ANISOU 4775 N ILE B 186 4774 5388 4501 113 -234 -157 D000 N ATOM 4776 CA ILE B 186 -19.771 -0.218 16.393 1.00 37.60 D000 C ANISOU 4776 CA ILE B 186 4554 5279 4453 33 -273 -186 D000 C ATOM 4777 C ILE B 186 -19.108 -1.582 16.232 1.00 38.66 D000 C ANISOU 4777 C ILE B 186 4714 5345 4629 -50 -271 -235 D000 C ATOM 4778 O ILE B 186 -19.752 -2.622 16.409 1.00 38.03 D000 O ANISOU 4778 O ILE B 186 4589 5274 4588 -115 -332 -287 D000 O ATOM 4779 CB ILE B 186 -20.154 0.408 15.043 1.00 36.81 D000 C ANISOU 4779 CB ILE B 186 4400 5176 4411 33 -213 -134 D000 C ATOM 4780 CG1 ILE B 186 -21.133 1.568 15.306 1.00 44.41 D000 C ANISOU 4780 CG1 ILE B 186 5316 6210 5348 119 -228 -96 D000 C ATOM 4781 CG2 ILE B 186 -20.778 -0.645 14.134 1.00 43.62 D000 C ANISOU 4781 CG2 ILE B 186 5183 6032 5358 -56 -215 -147 D000 C ATOM 4782 CD1 ILE B 186 -21.418 2.442 14.116 1.00 45.73 D000 C ANISOU 4782 CD1 ILE B 186 5458 6366 5550 150 -153 -48 D000 C ATOM 4783 N ILE B 187 -17.821 -1.606 15.899 1.00 37.18 D000 N ANISOU 4783 N ILE B 187 4594 5085 4449 -51 -205 -219 D000 N ATOM 4784 CA ILE B 187 -17.107 -2.881 15.786 1.00 38.62 D000 C ANISOU 4784 CA ILE B 187 4805 5195 4675 -111 -199 -258 D000 C ATOM 4785 C ILE B 187 -17.158 -3.643 17.104 1.00 38.81 D000 C ANISOU 4785 C ILE B 187 4873 5225 4649 -111 -253 -333 D000 C ATOM 4786 O ILE B 187 -17.414 -4.854 17.137 1.00 40.22 D000 O ANISOU 4786 O ILE B 187 5041 5367 4872 -177 -291 -389 D000 O ATOM 4787 CB ILE B 187 -15.657 -2.645 15.326 1.00 36.74 D000 C ANISOU 4787 CB ILE B 187 4618 4887 4455 -93 -127 -224 D000 C ATOM 4788 CG1 ILE B 187 -15.638 -2.218 13.853 1.00 38.46 D000 C ANISOU 4788 CG1 ILE B 187 4802 5090 4721 -111 -97 -172 D000 C ATOM 4789 CG2 ILE B 187 -14.814 -3.914 15.558 1.00 39.94 D000 C ANISOU 4789 CG2 ILE B 187 5060 5219 4895 -124 -119 -265 D000 C ATOM 4790 CD1 ILE B 187 -14.316 -1.581 13.418 1.00 44.21 D000 C ANISOU 4790 CD1 ILE B 187 5566 5767 5465 -85 -49 -140 D000 C ATOM 4791 N THR B 188 -16.913 -2.943 18.216 1.00 39.19 D000 N ANISOU 4791 N THR B 188 4982 5309 4597 -34 -253 -335 D000 N ATOM 4792 CA THR B 188 -16.918 -3.598 19.519 1.00 40.59 D000 C ANISOU 4792 CA THR B 188 5230 5499 4696 -18 -303 -413 D000 C ATOM 4793 C THR B 188 -18.310 -4.118 19.869 1.00 42.21 D000 C ANISOU 4793 C THR B 188 5374 5764 4898 -61 -427 -476 D000 C ATOM 4794 O THR B 188 -18.450 -5.221 20.414 1.00 40.33 D000 O ANISOU 4794 O THR B 188 5166 5501 4658 -107 -486 -566 D000 O ATOM 4795 CB THR B 188 -16.400 -2.621 20.580 1.00 42.99 D000 C ANISOU 4795 CB THR B 188 5622 5836 4878 86 -264 -383 D000 C ATOM 4796 CG2 THR B 188 -16.394 -3.272 21.960 1.00 54.72 D000 C ANISOU 4796 CG2 THR B 188 7205 7339 6248 118 -312 -466 D000 C ATOM 4797 OG1 THR B 188 -15.055 -2.220 20.244 1.00 46.91 D000 O ANISOU 4797 OG1 THR B 188 6152 6263 5407 109 -145 -328 D000 O ATOM 4798 N ARG B 189 -19.346 -3.349 19.540 1.00 41.25 D000 N ANISOU 4798 N ARG B 189 5163 5719 4790 -48 -468 -433 D000 N ATOM 4799 CA ARG B 189 -20.724 -3.766 19.788 1.00 43.25 D000 C ANISOU 4799 CA ARG B 189 5323 6039 5071 -92 -590 -484 D000 C ATOM 4800 C ARG B 189 -21.084 -5.049 19.049 1.00 43.13 D000 C ANISOU 4800 C ARG B 189 5236 5962 5188 -217 -604 -529 D000 C ATOM 4801 O ARG B 189 -21.898 -5.840 19.543 1.00 47.59 D000 O ANISOU 4801 O ARG B 189 5756 6545 5783 -279 -711 -610 D000 O ATOM 4802 CB ARG B 189 -21.654 -2.627 19.375 1.00 47.62 D000 C ANISOU 4802 CB ARG B 189 5777 6675 5639 -43 -599 -410 D000 C ATOM 4803 CG ARG B 189 -23.104 -2.802 19.719 1.00 59.62 D000 C ANISOU 4803 CG ARG B 189 7177 8284 7191 -65 -729 -448 D000 C ATOM 4804 CD ARG B 189 -23.832 -1.500 19.396 1.00 58.83 D000 C ANISOU 4804 CD ARG B 189 6996 8261 7094 20 -716 -362 D000 C ATOM 4805 NE ARG B 189 -23.334 -0.407 20.225 1.00 48.16 D000 N ANISOU 4805 NE ARG B 189 5755 6939 5606 147 -704 -318 D000 N ATOM 4806 CZ ARG B 189 -23.041 0.811 19.792 1.00 51.10 D000 C ANISOU 4806 CZ ARG B 189 6152 7300 5964 228 -610 -228 D000 C ATOM 4807 NH1 ARG B 189 -23.221 1.161 18.530 1.00 50.44 D000 N ANISOU 4807 NH1 ARG B 189 5996 7189 5979 206 -527 -180 D000 N ATOM 4808 NH2 ARG B 189 -22.565 1.708 20.653 1.00 54.31 D000 N ANISOU 4808 NH2 ARG B 189 6667 7718 6251 335 -595 -187 D000 N ATOM 4809 N GLN B 190 -20.491 -5.276 17.877 1.00 41.40 D000 N ANISOU 4809 N GLN B 190 5010 5667 5051 -256 -503 -476 D000 N ATOM 4810 CA GLN B 190 -20.731 -6.475 17.092 1.00 41.96 D000 C ANISOU 4810 CA GLN B 190 5032 5665 5247 -365 -493 -495 D000 C ATOM 4811 C GLN B 190 -19.728 -7.589 17.377 1.00 43.38 D000 C ANISOU 4811 C GLN B 190 5312 5735 5434 -396 -473 -552 D000 C ATOM 4812 O GLN B 190 -19.731 -8.597 16.671 1.00 43.58 D000 O ANISOU 4812 O GLN B 190 5319 5676 5564 -477 -448 -553 D000 O ATOM 4813 CB GLN B 190 -20.717 -6.153 15.601 1.00 44.22 D000 C ANISOU 4813 CB GLN B 190 5266 5932 5605 -380 -398 -399 D000 C ATOM 4814 CG GLN B 190 -21.858 -5.280 15.140 1.00 45.12 D000 C ANISOU 4814 CG GLN B 190 5267 6136 5741 -362 -400 -347 D000 C ATOM 4815 CD GLN B 190 -23.177 -6.024 15.101 1.00 48.43 D000 C ANISOU 4815 CD GLN B 190 5555 6579 6266 -452 -460 -378 D000 C ATOM 4816 NE2 GLN B 190 -24.266 -5.299 15.270 1.00 49.95 D000 N ANISOU 4816 NE2 GLN B 190 5637 6872 6469 -420 -503 -363 D000 N ATOM 4817 OE1 GLN B 190 -23.214 -7.241 14.933 1.00 50.92 D000 O ANISOU 4817 OE1 GLN B 190 5863 6817 6667 -549 -466 -415 D000 O ATOM 4818 N GLY B 191 -18.902 -7.450 18.410 1.00 42.20 D000 N ANISOU 4818 N GLY B 191 5273 5582 5179 -327 -475 -594 D000 N ATOM 4819 CA GLY B 191 -18.056 -8.537 18.837 1.00 44.76 D000 C ANISOU 4819 CA GLY B 191 5692 5806 5509 -343 -456 -662 D000 C ATOM 4820 C GLY B 191 -16.717 -8.590 18.149 1.00 45.16 D000 C ANISOU 4820 C GLY B 191 5788 5776 5592 -312 -343 -600 D000 C ATOM 4821 O GLY B 191 -15.991 -9.581 18.316 1.00 45.26 D000 O ANISOU 4821 O GLY B 191 5866 5693 5638 -323 -315 -645 D000 O ATOM 4822 N GLY B 192 -16.366 -7.549 17.377 1.00 40.96 D000 N ANISOU 4822 N GLY B 192 5224 5280 5061 -271 -284 -503 D000 N ATOM 4823 CA GLY B 192 -15.057 -7.454 16.769 1.00 41.54 D000 C ANISOU 4823 CA GLY B 192 5329 5291 5164 -238 -198 -447 D000 C ATOM 4824 C GLY B 192 -14.014 -6.825 17.690 1.00 39.68 D000 C ANISOU 4824 C GLY B 192 5163 5063 4849 -150 -146 -448 D000 C ATOM 4825 O GLY B 192 -14.317 -6.257 18.730 1.00 40.37 D000 O ANISOU 4825 O GLY B 192 5288 5213 4837 -103 -167 -474 D000 O ATOM 4826 N GLU B 193 -12.759 -6.933 17.268 1.00 37.63 D000 N ANISOU 4826 N GLU B 193 4918 4739 4641 -125 -74 -411 D000 N ATOM 4827 CA GLU B 193 -11.606 -6.421 18.000 1.00 40.35 D000 C ANISOU 4827 CA GLU B 193 5310 5074 4946 -50 2 -399 D000 C ATOM 4828 C GLU B 193 -10.905 -5.398 17.121 1.00 40.26 D000 C ANISOU 4828 C GLU B 193 5246 5066 4984 -35 45 -312 D000 C ATOM 4829 O GLU B 193 -10.472 -5.724 16.014 1.00 40.36 D000 O ANISOU 4829 O GLU B 193 5217 5034 5083 -64 43 -278 D000 O ATOM 4830 CB GLU B 193 -10.668 -7.576 18.363 1.00 44.50 D000 C ANISOU 4830 CB GLU B 193 5883 5510 5514 -32 48 -443 D000 C ATOM 4831 CG GLU B 193 -9.364 -7.186 19.035 1.00 62.17 D000 C ANISOU 4831 CG GLU B 193 8154 7729 7740 47 152 -423 D000 C ATOM 4832 CD GLU B 193 -9.527 -6.844 20.506 1.00 67.22 D000 C ANISOU 4832 CD GLU B 193 8884 8416 8242 108 181 -467 D000 C ATOM 4833 OE1 GLU B 193 -8.499 -6.583 21.161 1.00 73.70 D000 O ANISOU 4833 OE1 GLU B 193 9738 9218 9045 177 288 -448 D000 O ATOM 4834 OE2 GLU B 193 -10.669 -6.862 21.010 1.00 60.40 D000 O ANISOU 4834 OE2 GLU B 193 8054 7608 7287 91 97 -519 D000 O ATOM 4835 N VAL B 194 -10.794 -4.166 17.597 1.00 36.56 D000 N ANISOU 4835 N VAL B 194 4787 4644 4460 11 79 -277 D000 N ATOM 4836 CA VAL B 194 -9.993 -3.177 16.884 1.00 35.68 D000 C ANISOU 4836 CA VAL B 194 4632 4517 4406 20 122 -209 D000 C ATOM 4837 C VAL B 194 -8.548 -3.406 17.305 1.00 38.93 D000 C ANISOU 4837 C VAL B 194 5049 4870 4873 56 206 -200 D000 C ATOM 4838 O VAL B 194 -8.210 -3.283 18.485 1.00 41.67 D000 O ANISOU 4838 O VAL B 194 5449 5222 5162 108 274 -210 D000 O ATOM 4839 CB VAL B 194 -10.453 -1.748 17.194 1.00 46.64 D000 C ANISOU 4839 CB VAL B 194 6029 5958 5734 52 134 -171 D000 C ATOM 4840 CG1 VAL B 194 -9.557 -0.747 16.505 1.00 47.87 D000 C ANISOU 4840 CG1 VAL B 194 6147 6078 5964 51 178 -114 D000 C ATOM 4841 CG2 VAL B 194 -11.885 -1.560 16.736 1.00 43.42 D000 C ANISOU 4841 CG2 VAL B 194 5599 5610 5289 27 57 -178 D000 C ATOM 4842 N THR B 195 -7.701 -3.778 16.358 1.00 36.39 D000 N ANISOU 4842 N THR B 195 4672 4496 4659 35 205 -177 D000 N ATOM 4843 CA THR B 195 -6.343 -4.161 16.730 1.00 37.02 D000 C ANISOU 4843 CA THR B 195 4732 4519 4813 72 283 -169 D000 C ATOM 4844 C THR B 195 -5.293 -3.102 16.418 1.00 41.03 D000 C ANISOU 4844 C THR B 195 5171 5011 5407 78 330 -111 D000 C ATOM 4845 O THR B 195 -4.271 -3.042 17.111 1.00 41.53 D000 O ANISOU 4845 O THR B 195 5216 5044 5520 119 427 -95 D000 O ATOM 4846 CB THR B 195 -5.970 -5.492 16.062 1.00 42.88 D000 C ANISOU 4846 CB THR B 195 5454 5203 5635 60 250 -186 D000 C ATOM 4847 CG2 THR B 195 -5.780 -5.361 14.555 1.00 40.29 D000 C ANISOU 4847 CG2 THR B 195 5061 4865 5382 21 177 -141 D000 C ATOM 4848 OG1 THR B 195 -4.771 -5.996 16.661 1.00 40.83 D000 O ANISOU 4848 OG1 THR B 195 5182 4890 5441 114 336 -188 D000 O ATOM 4849 N LYS B 196 -5.505 -2.251 15.425 1.00 35.82 D000 N ANISOU 4849 N LYS B 196 4472 4366 4772 38 271 -83 D000 N ATOM 4850 CA LYS B 196 -4.493 -1.256 15.112 1.00 36.82 D000 C ANISOU 4850 CA LYS B 196 4530 4464 4995 30 302 -41 D000 C ATOM 4851 C LYS B 196 -5.102 -0.087 14.353 1.00 37.82 D000 C ANISOU 4851 C LYS B 196 4660 4611 5098 -6 247 -28 D000 C ATOM 4852 O LYS B 196 -5.997 -0.270 13.527 1.00 37.59 D000 O ANISOU 4852 O LYS B 196 4654 4611 5018 -30 166 -44 D000 O ATOM 4853 CB LYS B 196 -3.384 -1.896 14.271 1.00 42.12 D000 C ANISOU 4853 CB LYS B 196 5116 5090 5796 20 267 -31 D000 C ATOM 4854 CG LYS B 196 -2.093 -1.138 14.240 1.00 51.63 D000 C ANISOU 4854 CG LYS B 196 6225 6258 7136 14 311 4 D000 C ATOM 4855 CD LYS B 196 -1.021 -1.905 13.456 1.00 53.83 D000 C ANISOU 4855 CD LYS B 196 6407 6502 7545 17 258 12 D000 C ATOM 4856 CE LYS B 196 -0.779 -3.332 13.937 1.00 63.12 D000 C ANISOU 4856 CE LYS B 196 7596 7656 8729 72 299 0 D000 C ATOM 4857 NZ LYS B 196 0.238 -3.363 15.013 1.00 44.84 D000 N ANISOU 4857 NZ LYS B 196 5231 5311 6497 122 439 17 D000 N ATOM 4858 N PHE B 197 -4.582 1.107 14.627 1.00 36.70 D000 N ANISOU 4858 N PHE B 197 4496 4444 5003 -9 303 4 D000 N ATOM 4859 CA PHE B 197 -4.820 2.288 13.806 1.00 35.16 D000 C ANISOU 4859 CA PHE B 197 4297 4240 4825 -44 256 10 D000 C ATOM 4860 C PHE B 197 -3.581 2.527 12.951 1.00 39.96 D000 C ANISOU 4860 C PHE B 197 4811 4794 5576 -86 218 13 D000 C ATOM 4861 O PHE B 197 -2.451 2.499 13.459 1.00 37.64 D000 O ANISOU 4861 O PHE B 197 4447 4461 5393 -84 285 36 D000 O ATOM 4862 CB PHE B 197 -5.093 3.523 14.657 1.00 38.64 D000 C ANISOU 4862 CB PHE B 197 4779 4669 5233 -22 339 44 D000 C ATOM 4863 CG PHE B 197 -6.281 3.383 15.556 1.00 38.84 D000 C ANISOU 4863 CG PHE B 197 4890 4755 5114 29 360 44 D000 C ATOM 4864 CD1 PHE B 197 -7.530 3.130 15.028 1.00 38.60 D000 C ANISOU 4864 CD1 PHE B 197 4890 4778 4997 27 278 15 D000 C ATOM 4865 CD2 PHE B 197 -6.136 3.480 16.925 1.00 47.34 D000 C ANISOU 4865 CD2 PHE B 197 6011 5836 6141 81 460 74 D000 C ATOM 4866 CE1 PHE B 197 -8.633 2.997 15.858 1.00 38.25 D000 C ANISOU 4866 CE1 PHE B 197 4903 4795 4836 71 278 11 D000 C ATOM 4867 CE2 PHE B 197 -7.231 3.340 17.763 1.00 43.43 D000 C ANISOU 4867 CE2 PHE B 197 5596 5404 5502 133 454 68 D000 C ATOM 4868 CZ PHE B 197 -8.471 3.100 17.232 1.00 40.95 D000 C ANISOU 4868 CZ PHE B 197 5294 5146 5121 124 354 34 D000 C ATOM 4869 N ILE B 198 -3.783 2.759 11.660 1.00 37.87 D000 N ANISOU 4869 N ILE B 198 4546 4531 5312 -122 110 -12 D000 N ATOM 4870 CA ILE B 198 -2.681 2.925 10.714 1.00 37.87 D000 C ANISOU 4870 CA ILE B 198 4464 4492 5434 -162 33 -23 D000 C ATOM 4871 C ILE B 198 -2.939 4.243 9.987 1.00 38.58 D000 C ANISOU 4871 C ILE B 198 4584 4555 5520 -201 -15 -48 D000 C ATOM 4872 O ILE B 198 -3.579 4.278 8.933 1.00 40.72 D000 O ANISOU 4872 O ILE B 198 4910 4850 5710 -207 -103 -80 D000 O ATOM 4873 CB ILE B 198 -2.560 1.747 9.742 1.00 39.80 D000 C ANISOU 4873 CB ILE B 198 4695 4761 5666 -156 -70 -35 D000 C ATOM 4874 CG1 ILE B 198 -2.456 0.429 10.516 1.00 41.16 D000 C ANISOU 4874 CG1 ILE B 198 4859 4945 5837 -113 -13 -17 D000 C ATOM 4875 CG2 ILE B 198 -1.345 1.913 8.851 1.00 41.41 D000 C ANISOU 4875 CG2 ILE B 198 4805 4932 5995 -188 -166 -44 D000 C ATOM 4876 CD1 ILE B 198 -2.752 -0.817 9.694 1.00 47.29 D000 C ANISOU 4876 CD1 ILE B 198 5660 5740 6567 -98 -93 -18 D000 C ATOM 4877 N GLY B 199 -2.452 5.344 10.553 1.00 39.97 D000 N ANISOU 4877 N GLY B 199 4732 4672 5783 -225 55 -33 D000 N ATOM 4878 CA GLY B 199 -2.746 6.642 9.976 1.00 40.03 D000 C ANISOU 4878 CA GLY B 199 4783 4633 5791 -258 24 -62 D000 C ATOM 4879 C GLY B 199 -4.222 6.968 10.099 1.00 38.93 D000 C ANISOU 4879 C GLY B 199 4759 4533 5498 -213 52 -62 D000 C ATOM 4880 O GLY B 199 -4.722 7.146 11.211 1.00 39.74 D000 O ANISOU 4880 O GLY B 199 4896 4648 5556 -171 153 -19 D000 O ATOM 4881 N ASP B 200 -4.927 7.045 8.967 1.00 34.07 D000 N ANISOU 4881 N ASP B 200 4203 3943 4798 -213 -36 -107 D000 N ATOM 4882 CA ASP B 200 -6.364 7.306 8.926 1.00 34.55 D000 C ANISOU 4882 CA ASP B 200 4354 4048 4727 -165 -12 -108 D000 C ATOM 4883 C ASP B 200 -7.175 6.032 8.724 1.00 38.49 D000 C ANISOU 4883 C ASP B 200 4867 4635 5122 -136 -37 -102 D000 C ATOM 4884 O ASP B 200 -8.293 6.080 8.198 1.00 37.86 D000 O ANISOU 4884 O ASP B 200 4843 4597 4945 -109 -48 -113 D000 O ATOM 4885 CB ASP B 200 -6.675 8.290 7.802 1.00 36.14 D000 C ANISOU 4885 CB ASP B 200 4617 4211 4902 -177 -67 -161 D000 C ATOM 4886 CG ASP B 200 -6.465 7.676 6.419 1.00 35.64 D000 C ANISOU 4886 CG ASP B 200 4566 4177 4799 -198 -184 -208 D000 C ATOM 4887 OD1 ASP B 200 -5.670 6.723 6.318 1.00 37.84 D000 O ANISOU 4887 OD1 ASP B 200 4780 4474 5123 -218 -234 -197 D000 O ATOM 4888 OD2 ASP B 200 -7.051 8.142 5.426 1.00 36.49 D000 O ANISOU 4888 OD2 ASP B 200 4752 4285 4826 -185 -224 -252 D000 O ATOM 4889 N CYS B 201 -6.627 4.891 9.125 1.00 37.24 D000 N ANISOU 4889 N CYS B 201 4657 4497 4996 -140 -39 -83 D000 N ATOM 4890 CA CYS B 201 -7.189 3.588 8.796 1.00 35.28 D000 C ANISOU 4890 CA CYS B 201 4418 4307 4678 -128 -72 -80 D000 C ATOM 4891 C CYS B 201 -7.389 2.771 10.062 1.00 41.29 D000 C ANISOU 4891 C CYS B 201 5165 5093 5429 -104 -8 -57 D000 C ATOM 4892 O CYS B 201 -6.548 2.792 10.964 1.00 36.32 D000 O ANISOU 4892 O CYS B 201 4499 4433 4866 -99 46 -42 D000 O ATOM 4893 CB CYS B 201 -6.264 2.849 7.818 1.00 41.19 D000 C ANISOU 4893 CB CYS B 201 5133 5042 5475 -151 -158 -89 D000 C ATOM 4894 SG CYS B 201 -6.564 1.100 7.686 1.00 44.87 D000 S ANISOU 4894 SG CYS B 201 5599 5545 5903 -136 -175 -66 D000 S ATOM 4895 N VAL B 202 -8.523 2.074 10.131 1.00 34.46 D000 N ANISOU 4895 N VAL B 202 4330 4281 4481 -89 -9 -58 D000 N ATOM 4896 CA AVAL B 202 -8.866 1.138 11.200 0.74 34.60 D000 C ANISOU 4896 CA AVAL B 202 4348 4325 4474 -73 25 -57 D000 C ATOM 4897 CA BVAL B 202 -8.782 1.145 11.220 0.26 34.82 D000 C ANISOU 4897 CA BVAL B 202 4373 4349 4506 -73 26 -56 D000 C ATOM 4898 C VAL B 202 -8.641 -0.281 10.697 1.00 35.78 D000 C ANISOU 4898 C VAL B 202 4484 4466 4645 -92 -14 -62 D000 C ATOM 4899 O VAL B 202 -9.208 -0.654 9.662 1.00 37.22 D000 O ANISOU 4899 O VAL B 202 4681 4665 4797 -109 -57 -58 D000 O ATOM 4900 CB AVAL B 202 -10.342 1.289 11.622 0.74 37.13 D000 C ANISOU 4900 CB AVAL B 202 4697 4705 4706 -53 33 -61 D000 C ATOM 4901 CB BVAL B 202 -10.153 1.391 11.876 0.26 38.27 D000 C ANISOU 4901 CB BVAL B 202 4841 4842 4857 -48 45 -59 D000 C ATOM 4902 CG1AVAL B 202 -10.735 0.142 12.540 0.74 35.09 D000 C ANISOU 4902 CG1AVAL B 202 4441 4470 4421 -50 37 -78 D000 C ATOM 4903 CG1BVAL B 202 -11.267 1.094 10.920 0.26 42.13 D000 C ANISOU 4903 CG1BVAL B 202 5334 5371 5302 -63 5 -64 D000 C ATOM 4904 CG2AVAL B 202 -10.598 2.614 12.275 0.74 39.57 D000 C ANISOU 4904 CG2AVAL B 202 5027 5017 4991 -17 76 -45 D000 C ATOM 4905 CG2BVAL B 202 -10.289 0.570 13.164 0.26 33.27 D000 C ANISOU 4905 CG2BVAL B 202 4217 4227 4195 -30 70 -71 D000 C ATOM 4906 N MET B 203 -7.863 -1.082 11.434 1.00 34.61 D000 N ANISOU 4906 N MET B 203 4317 4290 4545 -81 14 -64 D000 N ATOM 4907 CA AMET B 203 -7.730 -2.508 11.189 0.44 35.91 D000 C ANISOU 4907 CA AMET B 203 4478 4432 4732 -88 -9 -69 D000 C ATOM 4908 CA BMET B 203 -7.719 -2.511 11.192 0.56 35.87 D000 C ANISOU 4908 CA BMET B 203 4473 4426 4728 -88 -9 -69 D000 C ATOM 4909 C MET B 203 -8.363 -3.267 12.348 1.00 37.44 D000 C ANISOU 4909 C MET B 203 4704 4636 4885 -78 26 -99 D000 C ATOM 4910 O MET B 203 -8.015 -3.045 13.516 1.00 36.82 D000 O ANISOU 4910 O MET B 203 4637 4556 4796 -47 83 -113 D000 O ATOM 4911 CB AMET B 203 -6.261 -2.912 11.031 0.44 37.96 D000 C ANISOU 4911 CB AMET B 203 4690 4639 5095 -73 -10 -54 D000 C ATOM 4912 CB BMET B 203 -6.243 -2.886 11.052 0.56 37.96 D000 C ANISOU 4912 CB BMET B 203 4688 4638 5095 -73 -9 -54 D000 C ATOM 4913 CG AMET B 203 -6.069 -4.385 10.723 0.44 37.42 D000 C ANISOU 4913 CG AMET B 203 4626 4534 5059 -67 -32 -50 D000 C ATOM 4914 CG BMET B 203 -5.957 -4.375 11.077 0.56 38.40 D000 C ANISOU 4914 CG BMET B 203 4748 4655 5189 -60 -12 -56 D000 C ATOM 4915 SD AMET B 203 -4.344 -4.789 10.402 0.44 43.18 D000 S ANISOU 4915 SD AMET B 203 5277 5207 5921 -33 -47 -23 D000 S ATOM 4916 SD BMET B 203 -4.184 -4.677 11.129 0.56 39.16 D000 S ANISOU 4916 SD BMET B 203 4763 4695 5422 -21 3 -34 D000 S ATOM 4917 CE AMET B 203 -4.402 -6.552 10.664 0.44 40.20 D000 C ANISOU 4917 CE AMET B 203 4934 4774 5566 -7 -28 -27 D000 C ATOM 4918 CE BMET B 203 -4.186 -6.433 11.448 0.56 41.79 D000 C ANISOU 4918 CE BMET B 203 5130 4972 5777 8 24 -46 D000 C ATOM 4919 N ALA B 204 -9.298 -4.156 12.028 1.00 36.65 D000 N ANISOU 4919 N ALA B 204 4623 4544 4759 -106 -5 -112 D000 N ATOM 4920 CA ALA B 204 -10.021 -4.896 13.047 1.00 33.78 D000 C ANISOU 4920 CA ALA B 204 4288 4187 4359 -111 4 -157 D000 C ATOM 4921 C ALA B 204 -10.219 -6.322 12.569 1.00 33.98 D000 C ANISOU 4921 C ALA B 204 4323 4161 4428 -145 -19 -165 D000 C ATOM 4922 O ALA B 204 -10.008 -6.635 11.395 1.00 36.32 D000 O ANISOU 4922 O ALA B 204 4607 4430 4761 -160 -40 -122 D000 O ATOM 4923 CB ALA B 204 -11.381 -4.243 13.347 1.00 37.21 D000 C ANISOU 4923 CB ALA B 204 4724 4695 4719 -121 -16 -170 D000 C ATOM 4924 N TYR B 205 -10.641 -7.196 13.481 1.00 37.05 D000 N ANISOU 4924 N TYR B 205 4742 4529 4806 -156 -17 -221 D000 N ATOM 4925 CA TYR B 205 -10.967 -8.544 13.051 1.00 38.83 D000 C ANISOU 4925 CA TYR B 205 4981 4689 5086 -199 -34 -231 D000 C ATOM 4926 C TYR B 205 -12.097 -9.139 13.876 1.00 39.02 D000 C ANISOU 4926 C TYR B 205 5022 4719 5085 -243 -62 -302 D000 C ATOM 4927 O TYR B 205 -12.387 -8.714 15.002 1.00 39.69 D000 O ANISOU 4927 O TYR B 205 5127 4853 5101 -222 -71 -356 D000 O ATOM 4928 CB TYR B 205 -9.732 -9.468 13.075 1.00 39.39 D000 C ANISOU 4928 CB TYR B 205 5073 4666 5228 -163 -4 -229 D000 C ATOM 4929 CG TYR B 205 -8.987 -9.614 14.388 1.00 39.84 D000 C ANISOU 4929 CG TYR B 205 5164 4700 5275 -108 44 -286 D000 C ATOM 4930 CD1 TYR B 205 -9.371 -10.557 15.337 1.00 45.03 D000 C ANISOU 4930 CD1 TYR B 205 5881 5312 5916 -117 48 -368 D000 C ATOM 4931 CD2 TYR B 205 -7.846 -8.868 14.635 1.00 45.32 D000 C ANISOU 4931 CD2 TYR B 205 5833 5407 5981 -48 93 -258 D000 C ATOM 4932 CE1 TYR B 205 -8.661 -10.708 16.520 1.00 47.68 D000 C ANISOU 4932 CE1 TYR B 205 6267 5626 6223 -54 106 -423 D000 C ATOM 4933 CE2 TYR B 205 -7.135 -9.007 15.808 1.00 44.48 D000 C ANISOU 4933 CE2 TYR B 205 5759 5279 5864 10 163 -299 D000 C ATOM 4934 CZ TYR B 205 -7.537 -9.932 16.743 1.00 51.59 D000 C ANISOU 4934 CZ TYR B 205 6736 6142 6726 14 173 -381 D000 C ATOM 4935 OH TYR B 205 -6.816 -10.069 17.908 1.00 52.84 D000 O ANISOU 4935 OH TYR B 205 6944 6279 6853 83 255 -425 D000 O ATOM 4936 N PHE B 206 -12.743 -10.132 13.259 1.00 38.41 D000 N ANISOU 4936 N PHE B 206 4938 4590 5066 -307 -79 -297 D000 N ATOM 4937 CA PHE B 206 -13.845 -10.897 13.825 1.00 40.04 D000 C ANISOU 4937 CA PHE B 206 5144 4780 5288 -375 -117 -365 D000 C ATOM 4938 C PHE B 206 -13.486 -12.378 13.753 1.00 42.48 D000 C ANISOU 4938 C PHE B 206 5500 4957 5684 -403 -103 -389 D000 C ATOM 4939 O PHE B 206 -12.643 -12.787 12.950 1.00 42.63 D000 O ANISOU 4939 O PHE B 206 5534 4908 5754 -376 -67 -326 D000 O ATOM 4940 CB PHE B 206 -15.158 -10.664 13.049 1.00 39.19 D000 C ANISOU 4940 CB PHE B 206 4965 4725 5199 -441 -138 -326 D000 C ATOM 4941 CG PHE B 206 -15.677 -9.242 13.099 1.00 39.26 D000 C ANISOU 4941 CG PHE B 206 4927 4856 5132 -409 -150 -304 D000 C ATOM 4942 CD1 PHE B 206 -15.064 -8.232 12.368 1.00 39.25 D000 C ANISOU 4942 CD1 PHE B 206 4926 4890 5096 -355 -117 -236 D000 C ATOM 4943 CD2 PHE B 206 -16.807 -8.926 13.846 1.00 44.06 D000 C ANISOU 4943 CD2 PHE B 206 5491 5538 5712 -431 -203 -354 D000 C ATOM 4944 CE1 PHE B 206 -15.546 -6.925 12.406 1.00 40.55 D000 C ANISOU 4944 CE1 PHE B 206 5059 5148 5200 -321 -121 -219 D000 C ATOM 4945 CE2 PHE B 206 -17.294 -7.624 13.886 1.00 40.18 D000 C ANISOU 4945 CE2 PHE B 206 4958 5150 5159 -388 -210 -326 D000 C ATOM 4946 CZ PHE B 206 -16.668 -6.627 13.165 1.00 39.90 D000 C ANISOU 4946 CZ PHE B 206 4934 5135 5091 -333 -162 -258 D000 C ATOM 4947 N ASP B 207 -14.149 -13.187 14.581 1.00 43.41 D000 N ANISOU 4947 N ASP B 207 5641 5031 5820 -456 -139 -484 D000 N ATOM 4948 CA ASP B 207 -14.027 -14.633 14.451 1.00 44.66 D000 C ANISOU 4948 CA ASP B 207 5845 5044 6079 -500 -126 -511 D000 C ATOM 4949 C ASP B 207 -14.415 -15.069 13.042 1.00 42.09 D000 C ANISOU 4949 C ASP B 207 5481 4671 5842 -557 -99 -406 D000 C ATOM 4950 O ASP B 207 -15.212 -14.418 12.362 1.00 44.03 D000 O ANISOU 4950 O ASP B 207 5657 4998 6073 -592 -103 -347 D000 O ATOM 4951 CB ASP B 207 -14.918 -15.359 15.461 1.00 45.57 D000 C ANISOU 4951 CB ASP B 207 5983 5123 6208 -573 -188 -639 D000 C ATOM 4952 CG ASP B 207 -14.380 -15.307 16.870 1.00 63.13 D000 C ANISOU 4952 CG ASP B 207 8291 7356 8339 -506 -203 -751 D000 C ATOM 4953 OD1 ASP B 207 -13.187 -14.993 17.049 1.00 55.61 D000 O ANISOU 4953 OD1 ASP B 207 7382 6402 7345 -406 -140 -725 D000 O ATOM 4954 OD2 ASP B 207 -15.158 -15.600 17.802 1.00 58.89 D000 O ANISOU 4954 OD2 ASP B 207 7776 6828 7771 -553 -278 -866 D000 O ATOM 4955 N GLY B 208 -13.862 -16.207 12.617 1.00 44.53 D000 N ANISOU 4955 N GLY B 208 5842 4839 6238 -558 -62 -381 D000 N ATOM 4956 CA GLY B 208 -14.030 -16.653 11.245 1.00 42.61 D000 C ANISOU 4956 CA GLY B 208 5586 4541 6063 -589 -23 -261 D000 C ATOM 4957 C GLY B 208 -15.451 -17.016 10.876 1.00 47.11 D000 C ANISOU 4957 C GLY B 208 6102 5100 6698 -709 -24 -250 D000 C ATOM 4958 O GLY B 208 -15.804 -16.986 9.692 1.00 51.24 D000 O ANISOU 4958 O GLY B 208 6601 5628 7241 -730 21 -136 D000 O ATOM 4959 N ASP B 209 -16.275 -17.359 11.854 1.00 46.11 D000 N ANISOU 4959 N ASP B 209 5955 4960 6606 -787 -73 -365 D000 N ATOM 4960 CA ASP B 209 -17.668 -17.691 11.592 1.00 50.43 D000 C ANISOU 4960 CA ASP B 209 6420 5500 7241 -912 -81 -363 D000 C ATOM 4961 C ASP B 209 -18.604 -16.525 11.897 1.00 47.20 D000 C ANISOU 4961 C ASP B 209 5908 5261 6765 -926 -130 -386 D000 C ATOM 4962 O ASP B 209 -19.812 -16.730 12.049 1.00 48.69 D000 O ANISOU 4962 O ASP B 209 6007 5464 7031 -1028 -162 -420 D000 O ATOM 4963 CB ASP B 209 -18.068 -18.936 12.388 1.00 52.33 D000 C ANISOU 4963 CB ASP B 209 6690 5599 7592 -1007 -119 -479 D000 C ATOM 4964 CG ASP B 209 -17.950 -18.743 13.882 1.00 59.19 D000 C ANISOU 4964 CG ASP B 209 7596 6509 8383 -981 -210 -641 D000 C ATOM 4965 OD1 ASP B 209 -17.376 -17.722 14.312 1.00 61.84 D000 O ANISOU 4965 OD1 ASP B 209 7946 6966 8584 -879 -224 -648 D000 O ATOM 4966 OD2 ASP B 209 -18.424 -19.620 14.632 1.00 72.80 D000 O ANISOU 4966 OD2 ASP B 209 9343 8139 10180 -1064 -265 -763 D000 O ATOM 4967 N CYS B 210 -18.077 -15.304 11.962 1.00 41.65 D000 N ANISOU 4967 N CYS B 210 5207 4682 5934 -825 -136 -364 D000 N ATOM 4968 CA CYS B 210 -18.872 -14.117 12.275 1.00 45.08 D000 C ANISOU 4968 CA CYS B 210 5556 5272 6300 -815 -179 -378 D000 C ATOM 4969 C CYS B 210 -18.962 -13.154 11.089 1.00 44.56 D000 C ANISOU 4969 C CYS B 210 5450 5291 6191 -772 -116 -257 D000 C ATOM 4970 O CYS B 210 -18.908 -11.932 11.246 1.00 42.60 D000 O ANISOU 4970 O CYS B 210 5183 5155 5847 -703 -130 -251 D000 O ATOM 4971 CB CYS B 210 -18.297 -13.428 13.510 1.00 42.49 D000 C ANISOU 4971 CB CYS B 210 5276 5013 5856 -734 -238 -465 D000 C ATOM 4972 SG CYS B 210 -18.585 -14.428 14.986 1.00 50.27 D000 S ANISOU 4972 SG CYS B 210 6307 5930 6863 -789 -329 -631 D000 S ATOM 4973 N ALA B 211 -19.149 -13.693 9.886 1.00 44.52 D000 N ANISOU 4973 N ALA B 211 5441 5224 6250 -810 -41 -159 D000 N ATOM 4974 CA ALA B 211 -19.283 -12.831 8.718 1.00 40.79 D000 C ANISOU 4974 CA ALA B 211 4949 4829 5721 -766 22 -52 D000 C ATOM 4975 C ALA B 211 -20.518 -11.946 8.824 1.00 39.79 D000 C ANISOU 4975 C ALA B 211 4708 4824 5588 -785 16 -59 D000 C ATOM 4976 O ALA B 211 -20.489 -10.780 8.413 1.00 40.93 D000 O ANISOU 4976 O ALA B 211 4846 5063 5643 -712 36 -21 D000 O ATOM 4977 CB ALA B 211 -19.359 -13.669 7.441 1.00 47.14 D000 C ANISOU 4977 CB ALA B 211 5782 5543 6584 -802 112 60 D000 C ATOM 4978 N ASP B 212 -21.624 -12.493 9.339 1.00 44.32 D000 N ANISOU 4978 N ASP B 212 5185 5388 6265 -881 -13 -107 D000 N ATOM 4979 CA ASP B 212 -22.841 -11.696 9.454 1.00 43.14 D000 C ANISOU 4979 CA ASP B 212 4904 5358 6130 -893 -24 -110 D000 C ATOM 4980 C ASP B 212 -22.601 -10.466 10.319 1.00 47.31 D000 C ANISOU 4980 C ASP B 212 5438 5998 6539 -798 -99 -166 D000 C ATOM 4981 O ASP B 212 -23.045 -9.358 9.980 1.00 43.06 D000 O ANISOU 4981 O ASP B 212 4849 5561 5951 -739 -72 -124 D000 O ATOM 4982 CB ASP B 212 -23.986 -12.532 10.033 1.00 45.46 D000 C ANISOU 4982 CB ASP B 212 5080 5624 6571 -1018 -73 -171 D000 C ATOM 4983 CG ASP B 212 -24.455 -13.621 9.088 1.00 49.00 D000 C ANISOU 4983 CG ASP B 212 5496 5962 7161 -1121 26 -94 D000 C ATOM 4984 OD1 ASP B 212 -24.732 -13.315 7.916 1.00 47.19 D000 O ANISOU 4984 OD1 ASP B 212 5247 5757 6926 -1101 145 24 D000 O ATOM 4985 OD2 ASP B 212 -24.562 -14.787 9.520 1.00 55.89 D000 O ANISOU 4985 OD2 ASP B 212 6370 6717 8147 -1222 -8 -150 D000 O ATOM 4986 N GLN B 213 -21.898 -10.640 11.443 1.00 41.48 D000 N ANISOU 4986 N GLN B 213 4771 5237 5753 -776 -182 -257 D000 N ATOM 4987 CA GLN B 213 -21.618 -9.499 12.316 1.00 40.78 D000 C ANISOU 4987 CA GLN B 213 4703 5244 5546 -682 -240 -298 D000 C ATOM 4988 C GLN B 213 -20.665 -8.509 11.659 1.00 38.69 D000 C ANISOU 4988 C GLN B 213 4511 5002 5188 -585 -176 -229 D000 C ATOM 4989 O GLN B 213 -20.809 -7.295 11.834 1.00 40.06 D000 O ANISOU 4989 O GLN B 213 4668 5264 5289 -513 -183 -217 D000 O ATOM 4990 CB GLN B 213 -21.059 -9.965 13.664 1.00 41.17 D000 C ANISOU 4990 CB GLN B 213 4828 5261 5554 -675 -324 -407 D000 C ATOM 4991 CG GLN B 213 -21.977 -10.816 14.566 1.00 46.98 D000 C ANISOU 4991 CG GLN B 213 5509 5983 6359 -765 -425 -510 D000 C ATOM 4992 CD GLN B 213 -22.400 -12.172 14.004 1.00 62.58 D000 C ANISOU 4992 CD GLN B 213 7448 7841 8489 -891 -400 -512 D000 C ATOM 4993 NE2 GLN B 213 -23.532 -12.671 14.485 1.00 95.57 D000 N ANISOU 4993 NE2 GLN B 213 11523 12027 12762 -988 -483 -581 D000 N ATOM 4994 OE1 GLN B 213 -21.711 -12.776 13.189 1.00 53.88 D000 O ANISOU 4994 OE1 GLN B 213 6410 6637 7426 -901 -314 -453 D000 O ATOM 4995 N ALA B 214 -19.673 -8.999 10.911 1.00 40.17 D000 N ANISOU 4995 N ALA B 214 4778 5105 5378 -579 -122 -185 D000 N ATOM 4996 CA ALA B 214 -18.762 -8.098 10.210 1.00 41.04 D000 C ANISOU 4996 CA ALA B 214 4948 5234 5412 -498 -80 -128 D000 C ATOM 4997 C ALA B 214 -19.501 -7.272 9.160 1.00 38.29 D000 C ANISOU 4997 C ALA B 214 4554 4952 5045 -480 -24 -59 D000 C ATOM 4998 O ALA B 214 -19.235 -6.071 8.993 1.00 37.18 D000 O ANISOU 4998 O ALA B 214 4432 4866 4830 -408 -15 -44 D000 O ATOM 4999 CB ALA B 214 -17.637 -8.902 9.557 1.00 38.92 D000 C ANISOU 4999 CB ALA B 214 4760 4866 5163 -496 -50 -92 D000 C ATOM 5000 N ILE B 215 -20.409 -7.906 8.425 1.00 36.28 D000 N ANISOU 5000 N ILE B 215 4242 4682 4859 -543 25 -14 D000 N ATOM 5001 CA ILE B 215 -21.198 -7.184 7.428 1.00 34.14 D000 C ANISOU 5001 CA ILE B 215 3929 4475 4570 -519 100 52 D000 C ATOM 5002 C ILE B 215 -22.080 -6.151 8.112 1.00 38.24 D000 C ANISOU 5002 C ILE B 215 4357 5095 5076 -483 70 19 D000 C ATOM 5003 O ILE B 215 -22.170 -4.996 7.675 1.00 37.22 D000 O ANISOU 5003 O ILE B 215 4237 5023 4882 -408 106 45 D000 O ATOM 5004 CB ILE B 215 -22.012 -8.172 6.576 1.00 37.30 D000 C ANISOU 5004 CB ILE B 215 4280 4832 5060 -598 179 116 D000 C ATOM 5005 CG1 ILE B 215 -21.078 -9.002 5.677 1.00 40.23 D000 C ANISOU 5005 CG1 ILE B 215 4764 5106 5415 -603 220 176 D000 C ATOM 5006 CG2 ILE B 215 -23.050 -7.441 5.706 1.00 41.16 D000 C ANISOU 5006 CG2 ILE B 215 4702 5398 5540 -572 273 179 D000 C ATOM 5007 CD1 ILE B 215 -21.761 -10.160 4.949 1.00 42.07 D000 C ANISOU 5007 CD1 ILE B 215 4971 5269 5746 -687 305 248 D000 C ATOM 5008 N GLN B 216 -22.740 -6.550 9.203 1.00 40.06 D000 N ANISOU 5008 N GLN B 216 4506 5346 5370 -531 -4 -43 D000 N ATOM 5009 CA GLN B 216 -23.650 -5.641 9.894 1.00 38.27 D000 C ANISOU 5009 CA GLN B 216 4183 5221 5136 -489 -49 -68 D000 C ATOM 5010 C GLN B 216 -22.900 -4.445 10.468 1.00 40.07 D000 C ANISOU 5010 C GLN B 216 4489 5485 5249 -385 -83 -87 D000 C ATOM 5011 O GLN B 216 -23.372 -3.307 10.377 1.00 39.56 D000 O ANISOU 5011 O GLN B 216 4392 5490 5151 -311 -63 -62 D000 O ATOM 5012 CB GLN B 216 -24.394 -6.383 11.004 1.00 39.39 D000 C ANISOU 5012 CB GLN B 216 4234 5376 5356 -562 -151 -142 D000 C ATOM 5013 CG GLN B 216 -25.473 -5.545 11.685 1.00 44.86 D000 C ANISOU 5013 CG GLN B 216 4807 6183 6055 -518 -215 -161 D000 C ATOM 5014 CD GLN B 216 -26.611 -5.218 10.753 1.00 45.02 D000 C ANISOU 5014 CD GLN B 216 4692 6255 6157 -522 -128 -90 D000 C ATOM 5015 NE2 GLN B 216 -26.732 -3.946 10.397 1.00 49.07 D000 N ANISOU 5015 NE2 GLN B 216 5209 6831 6604 -413 -77 -45 D000 N ATOM 5016 OE1 GLN B 216 -27.368 -6.097 10.345 1.00 48.30 D000 O ANISOU 5016 OE1 GLN B 216 5004 6647 6701 -620 -97 -75 D000 O ATOM 5017 N ALA B 217 -21.745 -4.689 11.089 1.00 38.41 D000 N ANISOU 5017 N ALA B 217 4381 5224 4990 -376 -123 -127 D000 N ATOM 5018 CA ALA B 217 -20.925 -3.590 11.582 1.00 37.00 D000 C ANISOU 5018 CA ALA B 217 4278 5063 4717 -286 -133 -132 D000 C ATOM 5019 C ALA B 217 -20.585 -2.615 10.466 1.00 36.94 D000 C ANISOU 5019 C ALA B 217 4310 5055 4672 -231 -58 -74 D000 C ATOM 5020 O ALA B 217 -20.619 -1.391 10.662 1.00 37.65 D000 O ANISOU 5020 O ALA B 217 4411 5183 4712 -156 -51 -64 D000 O ATOM 5021 CB ALA B 217 -19.638 -4.135 12.204 1.00 38.87 D000 C ANISOU 5021 CB ALA B 217 4611 5231 4927 -290 -156 -170 D000 C ATOM 5022 N SER B 218 -20.196 -3.138 9.307 1.00 36.49 D000 N ANISOU 5022 N SER B 218 4288 4946 4631 -264 -5 -37 D000 N ATOM 5023 CA SER B 218 -19.827 -2.277 8.191 1.00 37.31 D000 C ANISOU 5023 CA SER B 218 4446 5045 4682 -214 53 4 D000 C ATOM 5024 C SER B 218 -21.003 -1.421 7.754 1.00 38.79 D000 C ANISOU 5024 C SER B 218 4573 5300 4865 -171 104 30 D000 C ATOM 5025 O SER B 218 -20.851 -0.219 7.500 1.00 36.90 D000 O ANISOU 5025 O SER B 218 4375 5075 4572 -99 127 34 D000 O ATOM 5026 CB SER B 218 -19.334 -3.126 7.016 1.00 39.62 D000 C ANISOU 5026 CB SER B 218 4793 5281 4981 -252 90 43 D000 C ATOM 5027 OG SER B 218 -18.240 -3.926 7.404 1.00 38.61 D000 O ANISOU 5027 OG SER B 218 4712 5087 4870 -278 45 23 D000 O ATOM 5028 N LEU B 219 -22.179 -2.031 7.640 1.00 36.26 D000 N ANISOU 5028 N LEU B 219 4151 5014 4611 -215 128 48 D000 N ATOM 5029 CA LEU B 219 -23.363 -1.297 7.215 1.00 37.95 D000 C ANISOU 5029 CA LEU B 219 4285 5296 4840 -169 191 78 D000 C ATOM 5030 C LEU B 219 -23.723 -0.226 8.237 1.00 40.23 D000 C ANISOU 5030 C LEU B 219 4533 5642 5112 -95 138 52 D000 C ATOM 5031 O LEU B 219 -24.093 0.897 7.874 1.00 39.22 D000 O ANISOU 5031 O LEU B 219 4406 5543 4953 -11 189 72 D000 O ATOM 5032 CB LEU B 219 -24.515 -2.279 7.030 1.00 38.58 D000 C ANISOU 5032 CB LEU B 219 4237 5397 5026 -245 224 104 D000 C ATOM 5033 CG LEU B 219 -24.455 -3.103 5.740 1.00 39.59 D000 C ANISOU 5033 CG LEU B 219 4404 5475 5165 -295 322 163 D000 C ATOM 5034 CD1 LEU B 219 -25.596 -4.124 5.735 1.00 42.47 D000 C ANISOU 5034 CD1 LEU B 219 4626 5845 5663 -387 357 189 D000 C ATOM 5035 CD2 LEU B 219 -24.439 -2.272 4.444 1.00 49.25 D000 C ANISOU 5035 CD2 LEU B 219 5703 6710 6299 -217 432 211 D000 C ATOM 5036 N ASP B 220 -23.586 -0.550 9.525 1.00 38.07 D000 N ANISOU 5036 N ASP B 220 4238 5378 4849 -115 39 8 D000 N ATOM 5037 CA ASP B 220 -23.961 0.393 10.575 1.00 36.46 D000 C ANISOU 5037 CA ASP B 220 4004 5232 4617 -37 -18 -6 D000 C ATOM 5038 C ASP B 220 -22.976 1.553 10.652 1.00 39.76 D000 C ANISOU 5038 C ASP B 220 4542 5613 4951 43 1 -0 D000 C ATOM 5039 O ASP B 220 -23.376 2.677 10.985 1.00 38.55 D000 O ANISOU 5039 O ASP B 220 4380 5494 4774 133 5 17 D000 O ATOM 5040 CB ASP B 220 -24.071 -0.326 11.930 1.00 40.11 D000 C ANISOU 5040 CB ASP B 220 4433 5718 5091 -78 -134 -59 D000 C ATOM 5041 CG ASP B 220 -25.307 -1.233 12.033 1.00 44.01 D000 C ANISOU 5041 CG ASP B 220 4775 6257 5688 -152 -175 -75 D000 C ATOM 5042 OD1 ASP B 220 -26.290 -1.014 11.305 1.00 44.59 D000 O ANISOU 5042 OD1 ASP B 220 4741 6372 5828 -145 -115 -32 D000 O ATOM 5043 OD2 ASP B 220 -25.316 -2.157 12.867 1.00 48.59 D000 O ANISOU 5043 OD2 ASP B 220 5341 6830 6290 -219 -266 -133 D000 O ATOM 5044 N ILE B 221 -21.698 1.306 10.349 1.00 36.17 D000 N ANISOU 5044 N ILE B 221 4194 5085 4466 12 12 -11 D000 N ATOM 5045 CA ILE B 221 -20.719 2.391 10.282 1.00 35.05 D000 C ANISOU 5045 CA ILE B 221 4152 4896 4271 70 36 -6 D000 C ATOM 5046 C ILE B 221 -21.078 3.347 9.149 1.00 37.05 D000 C ANISOU 5046 C ILE B 221 4424 5145 4510 123 110 18 D000 C ATOM 5047 O ILE B 221 -21.086 4.574 9.320 1.00 36.28 D000 O ANISOU 5047 O ILE B 221 4360 5038 4388 200 130 26 D000 O ATOM 5048 CB ILE B 221 -19.295 1.821 10.112 1.00 36.29 D000 C ANISOU 5048 CB ILE B 221 4390 4979 4421 19 26 -24 D000 C ATOM 5049 CG1 ILE B 221 -18.749 1.268 11.430 1.00 37.66 D000 C ANISOU 5049 CG1 ILE B 221 4575 5145 4590 2 -28 -52 D000 C ATOM 5050 CG2 ILE B 221 -18.367 2.882 9.518 1.00 40.37 D000 C ANISOU 5050 CG2 ILE B 221 4990 5439 4910 56 59 -18 D000 C ATOM 5051 CD1 ILE B 221 -17.481 0.389 11.219 1.00 38.98 D000 C ANISOU 5051 CD1 ILE B 221 4793 5242 4775 -51 -31 -67 D000 C ATOM 5052 N LEU B 222 -21.394 2.802 7.970 1.00 36.56 D000 N ANISOU 5052 N LEU B 222 4351 5082 4458 88 161 32 D000 N ATOM 5053 CA LEU B 222 -21.760 3.655 6.849 1.00 38.06 D000 C ANISOU 5053 CA LEU B 222 4575 5269 4616 146 241 47 D000 C ATOM 5054 C LEU B 222 -22.998 4.494 7.166 1.00 41.10 D000 C ANISOU 5054 C LEU B 222 4878 5713 5024 228 275 66 D000 C ATOM 5055 O LEU B 222 -23.070 5.664 6.776 1.00 39.73 D000 O ANISOU 5055 O LEU B 222 4758 5519 4820 309 325 66 D000 O ATOM 5056 CB LEU B 222 -21.983 2.822 5.583 1.00 39.82 D000 C ANISOU 5056 CB LEU B 222 4806 5492 4832 102 301 70 D000 C ATOM 5057 CG LEU B 222 -20.767 2.089 5.003 1.00 42.16 D000 C ANISOU 5057 CG LEU B 222 5196 5728 5096 43 271 63 D000 C ATOM 5058 CD1 LEU B 222 -21.159 1.214 3.811 1.00 49.32 D000 C ANISOU 5058 CD1 LEU B 222 6112 6639 5988 10 338 105 D000 C ATOM 5059 CD2 LEU B 222 -19.694 3.086 4.605 1.00 40.97 D000 C ANISOU 5059 CD2 LEU B 222 5161 5523 4885 82 251 31 D000 C ATOM 5060 N AMET B 223 -23.993 3.907 7.848 0.44 39.91 D000 N ANISOU 5060 N AMET B 223 4595 5632 4935 210 245 79 D000 N ATOM 5061 N BMET B 223 -23.976 3.919 7.877 0.56 39.87 D000 N ANISOU 5061 N BMET B 223 4591 5627 4929 211 243 79 D000 N ATOM 5062 CA AMET B 223 -25.173 4.671 8.250 0.44 40.56 D000 C ANISOU 5062 CA AMET B 223 4578 5781 5053 296 258 102 D000 C ATOM 5063 CA BMET B 223 -25.177 4.673 8.232 0.56 40.51 D000 C ANISOU 5063 CA BMET B 223 4571 5773 5046 296 260 102 D000 C ATOM 5064 C AMET B 223 -24.794 5.777 9.220 0.44 40.22 D000 C ANISOU 5064 C AMET B 223 4590 5720 4970 379 211 98 D000 C ATOM 5065 C BMET B 223 -24.869 5.747 9.268 0.56 40.17 D000 C ANISOU 5065 C BMET B 223 4575 5721 4969 380 207 99 D000 C ATOM 5066 O AMET B 223 -25.216 6.931 9.073 0.44 41.64 D000 O ANISOU 5066 O AMET B 223 4781 5898 5143 483 260 118 D000 O ATOM 5067 O BMET B 223 -25.402 6.862 9.194 0.56 41.25 D000 O ANISOU 5067 O BMET B 223 4706 5864 5103 485 252 121 D000 O ATOM 5068 CB AMET B 223 -26.208 3.763 8.919 0.44 43.92 D000 C ANISOU 5068 CB AMET B 223 4840 6285 5563 247 201 107 D000 C ATOM 5069 CB BMET B 223 -26.255 3.717 8.754 0.56 43.80 D000 C ANISOU 5069 CB BMET B 223 4822 6269 5551 244 214 110 D000 C ATOM 5070 CG AMET B 223 -27.388 3.353 8.065 0.44 54.87 D000 C ANISOU 5070 CG AMET B 223 6098 7720 7030 231 287 142 D000 C ATOM 5071 CG BMET B 223 -27.469 4.385 9.387 0.56 44.30 D000 C ANISOU 5071 CG BMET B 223 4752 6415 5664 331 191 132 D000 C ATOM 5072 SD AMET B 223 -28.736 4.540 7.786 0.44 61.51 D000 S ANISOU 5072 SD AMET B 223 6824 8630 7917 369 371 185 D000 S ATOM 5073 SD BMET B 223 -28.695 3.165 9.920 0.56 62.22 D000 S ANISOU 5073 SD BMET B 223 6808 8773 8061 244 117 128 D000 S ATOM 5074 CE AMET B 223 -27.997 6.171 7.739 0.44 40.35 D000 C ANISOU 5074 CE AMET B 223 4312 5886 5133 501 401 178 D000 C ATOM 5075 CE BMET B 223 -27.881 2.431 11.340 0.56 55.26 D000 C ANISOU 5075 CE BMET B 223 5987 7877 7131 175 -47 66 D000 C ATOM 5076 N GLU B 224 -24.019 5.426 10.249 1.00 37.43 D000 N ANISOU 5076 N GLU B 224 4277 5351 4592 342 125 77 D000 N ATOM 5077 CA GLU B 224 -23.655 6.406 11.261 1.00 39.14 D000 C ANISOU 5077 CA GLU B 224 4553 5551 4768 420 91 88 D000 C ATOM 5078 C GLU B 224 -22.904 7.583 10.645 1.00 39.87 D000 C ANISOU 5078 C GLU B 224 4765 5553 4831 470 163 93 D000 C ATOM 5079 O GLU B 224 -23.130 8.740 11.034 1.00 40.41 D000 O ANISOU 5079 O GLU B 224 4860 5604 4890 569 183 121 D000 O ATOM 5080 CB GLU B 224 -22.831 5.729 12.357 1.00 40.46 D000 C ANISOU 5080 CB GLU B 224 4761 5709 4903 367 12 65 D000 C ATOM 5081 CG GLU B 224 -22.784 6.512 13.645 1.00 41.78 D000 C ANISOU 5081 CG GLU B 224 4965 5891 5020 452 -30 89 D000 C ATOM 5082 CD GLU B 224 -24.131 6.571 14.368 1.00 47.72 D000 C ANISOU 5082 CD GLU B 224 5604 6746 5780 516 -101 108 D000 C ATOM 5083 OE1 GLU B 224 -25.010 5.702 14.152 1.00 49.22 D000 O ANISOU 5083 OE1 GLU B 224 5672 7003 6026 464 -141 86 D000 O ATOM 5084 OE2 GLU B 224 -24.311 7.523 15.143 1.00 55.03 D000 O ANISOU 5084 OE2 GLU B 224 6561 7685 6664 621 -118 149 D000 O ATOM 5085 N LEU B 225 -22.030 7.320 9.667 1.00 38.15 D000 N ANISOU 5085 N LEU B 225 4622 5271 4603 407 198 65 D000 N ATOM 5086 CA LEU B 225 -21.308 8.416 9.020 1.00 37.02 D000 C ANISOU 5086 CA LEU B 225 4590 5037 4439 441 249 52 D000 C ATOM 5087 C LEU B 225 -22.250 9.298 8.203 1.00 40.12 D000 C ANISOU 5087 C LEU B 225 4979 5432 4832 530 327 60 D000 C ATOM 5088 O LEU B 225 -22.051 10.516 8.120 1.00 40.98 D000 O ANISOU 5088 O LEU B 225 5165 5471 4935 599 365 57 D000 O ATOM 5089 CB LEU B 225 -20.180 7.859 8.144 1.00 35.91 D000 C ANISOU 5089 CB LEU B 225 4521 4840 4285 354 242 16 D000 C ATOM 5090 CG LEU B 225 -19.060 7.171 8.929 1.00 41.56 D000 C ANISOU 5090 CG LEU B 225 5249 5531 5011 284 181 8 D000 C ATOM 5091 CD1 LEU B 225 -18.067 6.569 7.942 1.00 47.02 D000 C ANISOU 5091 CD1 LEU B 225 5991 6177 5698 210 168 -22 D000 C ATOM 5092 CD2 LEU B 225 -18.363 8.128 9.876 1.00 46.29 D000 C ANISOU 5092 CD2 LEU B 225 5899 6071 5617 319 180 19 D000 C ATOM 5093 N GLU B 226 -23.275 8.718 7.577 1.00 38.86 D000 N ANISOU 5093 N GLU B 226 4733 5344 4687 531 365 71 D000 N ATOM 5094 CA AGLU B 226 -24.229 9.551 6.849 0.56 42.65 D000 C ANISOU 5094 CA AGLU B 226 5202 5833 5171 630 459 82 D000 C ATOM 5095 CA BGLU B 226 -24.233 9.547 6.852 0.44 42.68 D000 C ANISOU 5095 CA BGLU B 226 5205 5837 5175 630 458 82 D000 C ATOM 5096 C GLU B 226 -24.984 10.465 7.807 1.00 40.02 D000 C ANISOU 5096 C GLU B 226 4810 5523 4872 742 451 120 D000 C ATOM 5097 O GLU B 226 -25.197 11.646 7.509 1.00 43.46 D000 O ANISOU 5097 O GLU B 226 5304 5905 5304 844 516 122 D000 O ATOM 5098 CB AGLU B 226 -25.208 8.691 6.042 0.56 44.01 D000 C ANISOU 5098 CB AGLU B 226 5274 6082 5365 608 520 100 D000 C ATOM 5099 CB BGLU B 226 -25.219 8.680 6.066 0.44 44.03 D000 C ANISOU 5099 CB BGLU B 226 5274 6086 5369 608 518 101 D000 C ATOM 5100 CG AGLU B 226 -26.406 9.466 5.479 0.56 49.16 D000 C ANISOU 5100 CG AGLU B 226 5875 6764 6039 725 630 123 D000 C ATOM 5101 CG BGLU B 226 -26.164 9.505 5.207 0.44 48.63 D000 C ANISOU 5101 CG BGLU B 226 5850 6677 5952 717 641 112 D000 C ATOM 5102 CD AGLU B 226 -26.145 10.083 4.115 0.56 55.04 D000 C ANISOU 5102 CD AGLU B 226 6758 7443 6711 768 736 88 D000 C ATOM 5103 CD BGLU B 226 -27.237 8.679 4.527 0.44 54.88 D000 C ANISOU 5103 CD BGLU B 226 6519 7550 6784 701 723 147 D000 C ATOM 5104 OE1AGLU B 226 -24.971 10.121 3.689 0.56 48.52 D000 O ANISOU 5104 OE1AGLU B 226 6075 6541 5818 714 701 41 D000 O ATOM 5105 OE1BGLU B 226 -27.265 7.449 4.726 0.44 60.68 D000 O ANISOU 5105 OE1BGLU B 226 7174 8327 7554 596 677 161 D000 O ATOM 5106 OE2AGLU B 226 -27.117 10.560 3.482 0.56 63.25 D000 O ANISOU 5106 OE2AGLU B 226 7765 8507 7760 862 851 104 D000 O ATOM 5107 OE2BGLU B 226 -28.060 9.268 3.796 0.44 66.11 D000 O ANISOU 5107 OE2BGLU B 226 7925 8986 8210 796 844 161 D000 O ATOM 5108 N ILE B 227 -25.410 9.932 8.960 1.00 41.17 D000 N ANISOU 5108 N ILE B 227 4849 5745 5048 732 367 149 D000 N ATOM 5109 CA ILE B 227 -26.085 10.760 9.957 1.00 42.32 D000 C ANISOU 5109 CA ILE B 227 4945 5921 5212 847 338 194 D000 C ATOM 5110 C ILE B 227 -25.157 11.863 10.447 1.00 43.41 D000 C ANISOU 5110 C ILE B 227 5228 5954 5313 897 341 201 D000 C ATOM 5111 O ILE B 227 -25.576 13.012 10.633 1.00 44.20 D000 O ANISOU 5111 O ILE B 227 5351 6020 5424 1019 381 236 D000 O ATOM 5112 CB ILE B 227 -26.588 9.886 11.125 1.00 46.59 D000 C ANISOU 5112 CB ILE B 227 5364 6567 5771 815 221 210 D000 C ATOM 5113 CG1 ILE B 227 -27.720 8.975 10.633 1.00 51.51 D000 C ANISOU 5113 CG1 ILE B 227 5819 7286 6468 775 228 210 D000 C ATOM 5114 CG2 ILE B 227 -27.056 10.764 12.282 1.00 53.03 D000 C ANISOU 5114 CG2 ILE B 227 6162 7410 6577 940 166 260 D000 C ATOM 5115 CD1 ILE B 227 -28.079 7.850 11.592 1.00 54.73 D000 C ANISOU 5115 CD1 ILE B 227 6112 7779 6903 699 101 198 D000 C ATOM 5116 N LEU B 228 -23.884 11.531 10.663 1.00 38.75 D000 N ANISOU 5116 N LEU B 228 4730 5302 4689 804 309 174 D000 N ATOM 5117 CA LEU B 228 -22.920 12.504 11.169 1.00 39.06 D000 C ANISOU 5117 CA LEU B 228 4894 5235 4714 832 321 187 D000 C ATOM 5118 C LEU B 228 -22.723 13.642 10.179 1.00 43.29 D000 C ANISOU 5118 C LEU B 228 5526 5658 5264 879 410 163 D000 C ATOM 5119 O LEU B 228 -22.705 14.819 10.561 1.00 42.53 D000 O ANISOU 5119 O LEU B 228 5495 5483 5181 968 446 195 D000 O ATOM 5120 CB LEU B 228 -21.592 11.799 11.440 1.00 40.40 D000 C ANISOU 5120 CB LEU B 228 5118 5367 4866 714 281 159 D000 C ATOM 5121 CG LEU B 228 -20.498 12.589 12.143 1.00 50.03 D000 C ANISOU 5121 CG LEU B 228 6442 6484 6085 719 297 181 D000 C ATOM 5122 CD1 LEU B 228 -20.890 12.855 13.581 1.00 60.62 D000 C ANISOU 5122 CD1 LEU B 228 7771 7868 7392 802 266 250 D000 C ATOM 5123 CD2 LEU B 228 -19.193 11.795 12.085 1.00 49.77 D000 C ANISOU 5123 CD2 LEU B 228 6438 6416 6057 597 273 144 D000 C ATOM 5124 N ARG B 229 -22.562 13.295 8.897 1.00 39.54 D000 N ANISOU 5124 N ARG B 229 5075 5168 4780 822 444 105 D000 N ATOM 5125 CA ARG B 229 -22.387 14.290 7.843 1.00 40.71 D000 C ANISOU 5125 CA ARG B 229 5330 5213 4925 863 519 61 D000 C ATOM 5126 C ARG B 229 -23.594 15.220 7.740 1.00 42.20 D000 C ANISOU 5126 C ARG B 229 5495 5406 5134 1011 595 90 D000 C ATOM 5127 O ARG B 229 -23.439 16.438 7.596 1.00 43.33 D000 O ANISOU 5127 O ARG B 229 5737 5434 5292 1084 648 80 D000 O ATOM 5128 CB ARG B 229 -22.174 13.585 6.504 1.00 43.26 D000 C ANISOU 5128 CB ARG B 229 5680 5551 5207 790 535 -0 D000 C ATOM 5129 CG ARG B 229 -20.800 12.957 6.326 1.00 38.55 D000 C ANISOU 5129 CG ARG B 229 5138 4913 4595 662 467 -41 D000 C ATOM 5130 CD ARG B 229 -20.572 12.592 4.874 1.00 40.93 D000 C ANISOU 5130 CD ARG B 229 5505 5208 4841 621 484 -100 D000 C ATOM 5131 NE ARG B 229 -21.512 11.591 4.373 1.00 40.66 D000 N ANISOU 5131 NE ARG B 229 5387 5283 4779 620 518 -74 D000 N ATOM 5132 CZ ARG B 229 -21.292 10.282 4.402 1.00 41.80 D000 C ANISOU 5132 CZ ARG B 229 5473 5489 4920 531 471 -57 D000 C ATOM 5133 NH1 ARG B 229 -20.176 9.774 4.913 1.00 38.25 D000 N ANISOU 5133 NH1 ARG B 229 5035 5011 4487 446 387 -66 D000 N ATOM 5134 NH2 ARG B 229 -22.191 9.463 3.861 1.00 41.44 D000 N ANISOU 5134 NH2 ARG B 229 5358 5525 4862 529 520 -29 D000 N ATOM 5135 N ASN B 230 -24.800 14.657 7.807 1.00 41.33 D000 N ANISOU 5135 N ASN B 230 5245 5420 5037 1056 603 128 D000 N ATOM 5136 CA ASN B 230 -26.007 15.457 7.629 1.00 43.18 D000 C ANISOU 5136 CA ASN B 230 5430 5672 5306 1205 681 159 D000 C ATOM 5137 C ASN B 230 -26.291 16.350 8.832 1.00 47.52 D000 C ANISOU 5137 C ASN B 230 5970 6199 5888 1317 654 228 D000 C ATOM 5138 O ASN B 230 -26.814 17.458 8.667 1.00 45.06 D000 O ANISOU 5138 O ASN B 230 5693 5824 5603 1452 728 246 D000 O ATOM 5139 CB ASN B 230 -27.207 14.536 7.366 1.00 44.18 D000 C ANISOU 5139 CB ASN B 230 5382 5943 5462 1210 697 185 D000 C ATOM 5140 CG ASN B 230 -27.127 13.824 6.018 1.00 51.48 D000 C ANISOU 5140 CG ASN B 230 6331 6880 6350 1134 764 135 D000 C ATOM 5141 ND2 ASN B 230 -28.015 12.870 5.806 1.00 57.01 D000 N ANISOU 5141 ND2 ASN B 230 6881 7695 7086 1107 782 163 D000 N ATOM 5142 OD1 ASN B 230 -26.261 14.118 5.191 1.00 57.20 D000 O ANISOU 5142 OD1 ASN B 230 7209 7511 7014 1098 794 74 D000 O ATOM 5143 N ASER B 231 -25.951 15.908 10.040 0.53 46.13 D000 N ANISOU 5143 N ASER B 231 5760 6067 5701 1276 553 270 D000 N ATOM 5144 N BSER B 231 -25.955 15.891 10.038 0.47 46.14 D000 N ANISOU 5144 N BSER B 231 5760 6070 5703 1275 552 269 D000 N ATOM 5145 CA ASER B 231 -26.313 16.633 11.251 0.53 46.16 D000 C ANISOU 5145 CA ASER B 231 5752 6072 5714 1392 517 350 D000 C ATOM 5146 CA BSER B 231 -26.304 16.606 11.256 0.47 46.16 D000 C ANISOU 5146 CA BSER B 231 5752 6074 5714 1390 515 350 D000 C ATOM 5147 C ASER B 231 -25.193 17.515 11.790 0.53 46.47 D000 C ANISOU 5147 C ASER B 231 5952 5966 5738 1392 531 368 D000 C ATOM 5148 C BSER B 231 -25.272 17.651 11.663 0.47 46.54 D000 C ANISOU 5148 C BSER B 231 5966 5965 5753 1407 545 366 D000 C ATOM 5149 O ASER B 231 -25.364 18.134 12.845 0.53 48.77 D000 O ANISOU 5149 O ASER B 231 6261 6245 6023 1490 509 448 D000 O ATOM 5150 O BSER B 231 -25.589 18.524 12.478 0.47 48.01 D000 O ANISOU 5150 O BSER B 231 6176 6117 5947 1530 549 443 D000 O ATOM 5151 CB ASER B 231 -26.743 15.645 12.339 0.53 48.25 D000 C ANISOU 5151 CB ASER B 231 5889 6483 5960 1366 395 388 D000 C ATOM 5152 CB BSER B 231 -26.487 15.610 12.410 0.47 48.10 D000 C ANISOU 5152 CB BSER B 231 5894 6449 5932 1346 390 384 D000 C ATOM 5153 OG ASER B 231 -25.615 14.969 12.857 0.53 45.85 D000 O ANISOU 5153 OG ASER B 231 5651 6163 5608 1241 336 365 D000 O ATOM 5154 OG BSER B 231 -27.488 14.655 12.111 0.47 50.80 D000 O ANISOU 5154 OG BSER B 231 6068 6928 6307 1321 357 370 D000 O ATOM 5155 N ALA B 232 -24.067 17.597 11.101 1.00 44.26 D000 N ANISOU 5155 N ALA B 232 5786 5576 5456 1288 566 302 D000 N ATOM 5156 CA ALA B 232 -22.975 18.432 11.582 1.00 45.29 D000 C ANISOU 5156 CA ALA B 232 6050 5558 5600 1272 588 320 D000 C ATOM 5157 C ALA B 232 -23.291 19.919 11.415 1.00 46.92 D000 C ANISOU 5157 C ALA B 232 6347 5629 5852 1403 676 346 D000 C ATOM 5158 O ALA B 232 -24.089 20.312 10.558 1.00 50.23 D000 O ANISOU 5158 O ALA B 232 6755 6042 6289 1484 734 314 D000 O ATOM 5159 CB ALA B 232 -21.684 18.092 10.835 1.00 50.35 D000 C ANISOU 5159 CB ALA B 232 6764 6120 6246 1118 587 235 D000 C ATOM 5160 N PRO B 233 -22.680 20.773 12.234 1.00 52.53 D000 N ANISOU 5160 N PRO B 233 7154 6220 6586 1433 700 408 D000 N ATOM 5161 CA PRO B 233 -22.937 22.211 12.118 1.00 56.46 D000 C ANISOU 5161 CA PRO B 233 7750 6562 7139 1558 788 437 D000 C ATOM 5162 C PRO B 233 -22.457 22.767 10.786 1.00 52.47 D000 C ANISOU 5162 C PRO B 233 7346 5912 6677 1505 852 322 D000 C ATOM 5163 O PRO B 233 -21.569 22.215 10.129 1.00 49.16 D000 O ANISOU 5163 O PRO B 233 6948 5480 6250 1355 822 232 D000 O ATOM 5164 CB PRO B 233 -22.139 22.821 13.280 1.00 53.89 D000 C ANISOU 5164 CB PRO B 233 7514 6131 6830 1561 803 531 D000 C ATOM 5165 CG PRO B 233 -21.476 21.700 13.987 1.00 57.35 D000 C ANISOU 5165 CG PRO B 233 7900 6679 7213 1445 728 543 D000 C ATOM 5166 CD PRO B 233 -22.048 20.414 13.515 1.00 54.55 D000 C ANISOU 5166 CD PRO B 233 7413 6505 6808 1394 651 481 D000 C ATOM 5167 N GLU B 234 -23.029 23.908 10.410 1.00 50.74 D000 N ANISOU 5167 N GLU B 234 7199 5579 6502 1635 937 322 D000 N ATOM 5168 CA GLU B 234 -22.586 24.595 9.206 1.00 48.02 D000 C ANISOU 5168 CA GLU B 234 6979 5073 6192 1599 997 203 D000 C ATOM 5169 C GLU B 234 -21.084 24.817 9.260 1.00 52.27 D000 C ANISOU 5169 C GLU B 234 7615 5466 6779 1441 976 160 D000 C ATOM 5170 O GLU B 234 -20.548 25.263 10.277 1.00 53.79 D000 O ANISOU 5170 O GLU B 234 7840 5577 7020 1436 988 249 D000 O ATOM 5171 CB GLU B 234 -23.289 25.945 9.050 1.00 57.63 D000 C ANISOU 5171 CB GLU B 234 8284 6147 7465 1772 1100 222 D000 C ATOM 5172 CG GLU B 234 -24.735 25.969 9.458 1.00 73.28 D000 C ANISOU 5172 CG GLU B 234 10154 8253 9435 1961 1123 316 D000 C ATOM 5173 CD GLU B 234 -25.480 27.118 8.813 1.00 94.27 D000 C ANISOU 5173 CD GLU B 234 12894 10784 12143 2127 1238 290 D000 C ATOM 5174 OE1 GLU B 234 -24.811 28.040 8.293 1.00 71.63 D000 O ANISOU 5174 OE1 GLU B 234 10194 7702 9322 2101 1297 214 D000 O ATOM 5175 OE2 GLU B 234 -26.729 27.102 8.833 1.00118.11 D000 O ANISOU 5175 OE2 GLU B 234 15805 13910 15161 2285 1269 342 D000 O ATOM 5176 N GLY B 235 -20.410 24.517 8.156 1.00 50.76 D000 N ANISOU 5176 N GLY B 235 7467 5243 6575 1317 948 28 D000 N ATOM 5177 CA GLY B 235 -18.986 24.732 8.053 1.00 56.79 D000 C ANISOU 5177 CA GLY B 235 8303 5870 7403 1162 916 -30 D000 C ATOM 5178 C GLY B 235 -18.128 23.666 8.691 1.00 49.84 D000 C ANISOU 5178 C GLY B 235 7332 5092 6514 1028 838 8 D000 C ATOM 5179 O GLY B 235 -16.898 23.761 8.610 1.00 52.25 D000 O ANISOU 5179 O GLY B 235 7670 5296 6887 893 810 -36 D000 O ATOM 5180 N SER B 236 -18.725 22.651 9.313 1.00 45.66 D000 N ANISOU 5180 N SER B 236 6683 4754 5910 1060 802 82 D000 N ATOM 5181 CA SER B 236 -17.938 21.620 9.976 1.00 45.27 D000 C ANISOU 5181 CA SER B 236 6557 4796 5848 946 737 115 D000 C ATOM 5182 C SER B 236 -17.243 20.712 8.963 1.00 46.76 D000 C ANISOU 5182 C SER B 236 6721 5031 6014 809 665 5 D000 C ATOM 5183 O SER B 236 -17.841 20.300 7.963 1.00 41.91 D000 O ANISOU 5183 O SER B 236 6098 4491 5337 826 649 -62 D000 O ATOM 5184 CB SER B 236 -18.826 20.768 10.890 1.00 45.87 D000 C ANISOU 5184 CB SER B 236 6522 5058 5847 1018 706 206 D000 C ATOM 5185 OG SER B 236 -18.115 19.611 11.326 1.00 47.01 D000 O ANISOU 5185 OG SER B 236 6600 5297 5966 906 642 210 D000 O ATOM 5186 N PRO B 237 -15.986 20.338 9.212 1.00 44.64 D000 N ANISOU 5186 N PRO B 237 6438 4729 5794 679 624 -5 D000 N ATOM 5187 CA PRO B 237 -15.325 19.385 8.315 1.00 43.24 D000 C ANISOU 5187 CA PRO B 237 6227 4609 5593 561 542 -95 D000 C ATOM 5188 C PRO B 237 -15.924 17.986 8.365 1.00 44.18 D000 C ANISOU 5188 C PRO B 237 6247 4922 5619 565 497 -73 D000 C ATOM 5189 O PRO B 237 -15.715 17.211 7.422 1.00 44.05 D000 O ANISOU 5189 O PRO B 237 6216 4961 5560 502 441 -142 D000 O ATOM 5190 CB PRO B 237 -13.866 19.403 8.802 1.00 48.30 D000 C ANISOU 5190 CB PRO B 237 6854 5164 6334 439 523 -87 D000 C ATOM 5191 CG PRO B 237 -13.949 19.849 10.204 1.00 54.92 D000 C ANISOU 5191 CG PRO B 237 7689 5973 7206 498 597 35 D000 C ATOM 5192 CD PRO B 237 -15.064 20.841 10.249 1.00 51.22 D000 C ANISOU 5192 CD PRO B 237 7288 5456 6717 637 662 67 D000 C ATOM 5193 N LEU B 238 -16.682 17.648 9.415 1.00 42.84 D000 N ANISOU 5193 N LEU B 238 6014 4850 5415 639 514 20 D000 N ATOM 5194 CA LEU B 238 -17.328 16.343 9.478 1.00 39.26 D000 C ANISOU 5194 CA LEU B 238 5463 4566 4889 637 468 33 D000 C ATOM 5195 C LEU B 238 -18.340 16.147 8.354 1.00 39.66 D000 C ANISOU 5195 C LEU B 238 5502 4679 4886 683 479 -14 D000 C ATOM 5196 O LEU B 238 -18.701 15.004 8.040 1.00 39.61 D000 O ANISOU 5196 O LEU B 238 5424 4792 4836 649 444 -23 D000 O ATOM 5197 CB LEU B 238 -18.014 16.178 10.828 1.00 43.84 D000 C ANISOU 5197 CB LEU B 238 5985 5228 5442 715 472 129 D000 C ATOM 5198 CG LEU B 238 -17.089 16.199 12.052 1.00 47.13 D000 C ANISOU 5198 CG LEU B 238 6417 5607 5882 681 476 190 D000 C ATOM 5199 CD1 LEU B 238 -17.910 16.041 13.317 1.00 53.63 D000 C ANISOU 5199 CD1 LEU B 238 7204 6528 6646 777 466 277 D000 C ATOM 5200 CD2 LEU B 238 -16.024 15.129 11.949 1.00 49.94 D000 C ANISOU 5200 CD2 LEU B 238 6738 5990 6249 554 429 150 D000 C ATOM 5201 N ARG B 239 -18.791 17.234 7.730 1.00 39.81 D000 N ANISOU 5201 N ARG B 239 5597 4614 4914 761 539 -44 D000 N ATOM 5202 CA ARG B 239 -19.719 17.118 6.604 1.00 40.95 D000 C ANISOU 5202 CA ARG B 239 5745 4812 5005 815 574 -90 D000 C ATOM 5203 C ARG B 239 -19.116 16.344 5.432 1.00 42.35 D000 C ANISOU 5203 C ARG B 239 5952 5010 5131 716 530 -171 D000 C ATOM 5204 O ARG B 239 -19.864 15.768 4.629 1.00 37.59 D000 O ANISOU 5204 O ARG B 239 5325 4493 4465 741 556 -186 D000 O ATOM 5205 CB ARG B 239 -20.158 18.518 6.157 1.00 42.29 D000 C ANISOU 5205 CB ARG B 239 6014 4861 5194 922 656 -119 D000 C ATOM 5206 CG ARG B 239 -21.072 18.538 4.933 1.00 41.93 D000 C ANISOU 5206 CG ARG B 239 5992 4853 5085 993 719 -172 D000 C ATOM 5207 CD ARG B 239 -22.036 19.733 4.956 1.00 45.43 D000 C ANISOU 5207 CD ARG B 239 6473 5230 5557 1154 819 -154 D000 C ATOM 5208 NE ARG B 239 -23.118 19.473 5.895 1.00 42.41 D000 N ANISOU 5208 NE ARG B 239 5949 4965 5199 1247 833 -46 D000 N ATOM 5209 CZ ARG B 239 -23.179 19.930 7.141 1.00 43.54 D000 C ANISOU 5209 CZ ARG B 239 6062 5087 5393 1299 816 40 D000 C ATOM 5210 NH1 ARG B 239 -22.422 20.932 7.554 1.00 46.48 D000 N ANISOU 5210 NH1 ARG B 239 6545 5301 5815 1300 827 44 D000 N ATOM 5211 NH2 ARG B 239 -23.995 19.338 8.005 1.00 46.34 D000 N ANISOU 5211 NH2 ARG B 239 6275 5583 5750 1346 782 126 D000 N ATOM 5212 N VAL B 240 -17.788 16.299 5.307 1.00 40.48 D000 N ANISOU 5212 N VAL B 240 5762 4696 4921 608 466 -217 D000 N ATOM 5213 CA VAL B 240 -17.201 15.620 4.155 1.00 40.21 D000 C ANISOU 5213 CA VAL B 240 5765 4682 4832 528 409 -291 D000 C ATOM 5214 C VAL B 240 -16.302 14.474 4.615 1.00 42.04 D000 C ANISOU 5214 C VAL B 240 5919 4968 5086 421 328 -265 D000 C ATOM 5215 O VAL B 240 -15.317 14.146 3.956 1.00 43.47 D000 O ANISOU 5215 O VAL B 240 6132 5122 5263 339 256 -320 D000 O ATOM 5216 CB VAL B 240 -16.431 16.602 3.245 1.00 42.31 D000 C ANISOU 5216 CB VAL B 240 6165 4807 5105 502 387 -395 D000 C ATOM 5217 CG1 VAL B 240 -17.411 17.532 2.530 1.00 47.86 D000 C ANISOU 5217 CG1 VAL B 240 6961 5466 5757 617 475 -438 D000 C ATOM 5218 CG2 VAL B 240 -15.384 17.410 4.026 1.00 45.70 D000 C ANISOU 5218 CG2 VAL B 240 6607 5101 5655 444 364 -394 D000 C ATOM 5219 N LEU B 241 -16.686 13.821 5.703 1.00 38.76 D000 N ANISOU 5219 N LEU B 241 5403 4636 4688 430 334 -185 D000 N ATOM 5220 CA LEU B 241 -16.018 12.614 6.191 1.00 40.54 D000 C ANISOU 5220 CA LEU B 241 5555 4921 4927 347 273 -159 D000 C ATOM 5221 C LEU B 241 -16.659 11.390 5.536 1.00 39.15 D000 C ANISOU 5221 C LEU B 241 5335 4856 4684 335 261 -156 D000 C ATOM 5222 O LEU B 241 -17.807 11.040 5.839 1.00 40.17 D000 O ANISOU 5222 O LEU B 241 5399 5069 4794 386 299 -113 D000 O ATOM 5223 CB LEU B 241 -16.123 12.538 7.710 1.00 38.47 D000 C ANISOU 5223 CB LEU B 241 5229 4684 4702 367 287 -86 D000 C ATOM 5224 CG LEU B 241 -15.588 11.289 8.421 1.00 39.37 D000 C ANISOU 5224 CG LEU B 241 5273 4862 4824 301 240 -59 D000 C ATOM 5225 CD1 LEU B 241 -14.144 11.110 8.067 1.00 41.19 D000 C ANISOU 5225 CD1 LEU B 241 5522 5025 5104 212 196 -96 D000 C ATOM 5226 CD2 LEU B 241 -15.755 11.395 9.928 1.00 45.26 D000 C ANISOU 5226 CD2 LEU B 241 5987 5628 5580 340 260 6 D000 C ATOM 5227 N TYR B 242 -15.905 10.737 4.657 1.00 37.73 D000 N ANISOU 5227 N TYR B 242 5184 4674 4479 268 206 -195 D000 N ATOM 5228 CA TYR B 242 -16.303 9.519 3.971 1.00 37.92 D000 C ANISOU 5228 CA TYR B 242 5182 4783 4444 247 197 -182 D000 C ATOM 5229 C TYR B 242 -15.249 8.438 4.205 1.00 40.46 D000 C ANISOU 5229 C TYR B 242 5465 5112 4798 163 121 -173 D000 C ATOM 5230 O TYR B 242 -14.071 8.731 4.440 1.00 37.93 D000 O ANISOU 5230 O TYR B 242 5156 4725 4532 119 69 -196 D000 O ATOM 5231 CB TYR B 242 -16.459 9.754 2.476 1.00 38.68 D000 C ANISOU 5231 CB TYR B 242 5377 4869 4452 271 210 -231 D000 C ATOM 5232 CG TYR B 242 -17.596 10.676 2.095 1.00 40.06 D000 C ANISOU 5232 CG TYR B 242 5591 5043 4586 367 306 -242 D000 C ATOM 5233 CD1 TYR B 242 -17.405 12.048 1.995 1.00 42.84 D000 C ANISOU 5233 CD1 TYR B 242 6028 5298 4952 410 322 -295 D000 C ATOM 5234 CD2 TYR B 242 -18.850 10.164 1.809 1.00 43.16 D000 C ANISOU 5234 CD2 TYR B 242 5935 5524 4942 415 387 -197 D000 C ATOM 5235 CE1 TYR B 242 -18.440 12.893 1.639 1.00 46.41 D000 C ANISOU 5235 CE1 TYR B 242 6521 5740 5372 512 418 -306 D000 C ATOM 5236 CE2 TYR B 242 -19.883 10.997 1.447 1.00 40.79 D000 C ANISOU 5236 CE2 TYR B 242 5658 5224 4615 514 486 -203 D000 C ATOM 5237 CZ TYR B 242 -19.680 12.362 1.370 1.00 47.03 D000 C ANISOU 5237 CZ TYR B 242 6540 5917 5411 569 502 -258 D000 C ATOM 5238 OH TYR B 242 -20.724 13.209 1.013 1.00 51.61 D000 O ANISOU 5238 OH TYR B 242 7149 6490 5971 683 610 -265 D000 O ATOM 5239 N SER B 243 -15.683 7.183 4.120 1.00 39.16 D000 N ANISOU 5239 N SER B 243 5249 5020 4611 142 121 -136 D000 N ATOM 5240 CA SER B 243 -14.816 6.036 4.344 1.00 37.82 D000 C ANISOU 5240 CA SER B 243 5043 4854 4474 76 60 -122 D000 C ATOM 5241 C SER B 243 -15.096 4.965 3.305 1.00 46.17 D000 C ANISOU 5241 C SER B 243 6118 5952 5471 61 58 -103 D000 C ATOM 5242 O SER B 243 -16.194 4.883 2.757 1.00 41.41 D000 O ANISOU 5242 O SER B 243 5521 5395 4818 94 123 -84 D000 O ATOM 5243 CB SER B 243 -15.037 5.442 5.737 1.00 41.48 D000 C ANISOU 5243 CB SER B 243 5421 5349 4991 64 68 -86 D000 C ATOM 5244 OG SER B 243 -14.140 4.379 6.017 1.00 41.46 D000 O ANISOU 5244 OG SER B 243 5391 5337 5026 10 20 -79 D000 O ATOM 5245 N GLY B 244 -14.082 4.142 3.047 1.00 37.46 D000 N ANISOU 5245 N GLY B 244 5020 4829 4383 15 -10 -100 D000 N ATOM 5246 CA GLY B 244 -14.267 2.855 2.414 1.00 37.96 D000 C ANISOU 5246 CA GLY B 244 5087 4924 4414 -5 -12 -59 D000 C ATOM 5247 C GLY B 244 -14.132 1.749 3.449 1.00 38.98 D000 C ANISOU 5247 C GLY B 244 5133 5056 4621 -46 -20 -29 D000 C ATOM 5248 O GLY B 244 -13.614 1.962 4.543 1.00 40.48 D000 O ANISOU 5248 O GLY B 244 5280 5226 4876 -56 -38 -45 D000 O ATOM 5249 N ILE B 245 -14.625 0.560 3.100 1.00 33.61 D000 N ANISOU 5249 N ILE B 245 4442 4396 3933 -67 2 15 D000 N ATOM 5250 CA ILE B 245 -14.521 -0.611 3.964 1.00 33.00 D000 C ANISOU 5250 CA ILE B 245 4303 4307 3927 -108 -7 34 D000 C ATOM 5251 C ILE B 245 -14.268 -1.826 3.091 1.00 34.72 D000 C ANISOU 5251 C ILE B 245 4556 4503 4134 -128 -17 81 D000 C ATOM 5252 O ILE B 245 -14.951 -2.022 2.079 1.00 36.24 D000 O ANISOU 5252 O ILE B 245 4789 4715 4264 -119 30 120 D000 O ATOM 5253 CB ILE B 245 -15.787 -0.849 4.813 1.00 33.83 D000 C ANISOU 5253 CB ILE B 245 4334 4454 4066 -122 43 39 D000 C ATOM 5254 CG1 ILE B 245 -16.109 0.360 5.684 1.00 37.73 D000 C ANISOU 5254 CG1 ILE B 245 4801 4973 4561 -85 50 7 D000 C ATOM 5255 CG2 ILE B 245 -15.592 -2.084 5.684 1.00 38.85 D000 C ANISOU 5255 CG2 ILE B 245 4926 5064 4770 -169 20 39 D000 C ATOM 5256 CD1 ILE B 245 -17.440 0.238 6.421 1.00 43.59 D000 C ANISOU 5256 CD1 ILE B 245 5463 5772 5328 -86 81 13 D000 C ATOM 5257 N GLY B 246 -13.288 -2.628 3.480 1.00 33.41 D000 N ANISOU 5257 N GLY B 246 4378 4291 4025 -147 -67 84 D000 N ATOM 5258 CA GLY B 246 -13.023 -3.895 2.816 1.00 34.43 D000 C ANISOU 5258 CA GLY B 246 4538 4385 4159 -159 -77 138 D000 C ATOM 5259 C GLY B 246 -12.966 -5.003 3.844 1.00 38.22 D000 C ANISOU 5259 C GLY B 246 4967 4823 4733 -195 -70 136 D000 C ATOM 5260 O GLY B 246 -12.450 -4.815 4.942 1.00 37.55 D000 O ANISOU 5260 O GLY B 246 4841 4727 4700 -196 -90 90 D000 O ATOM 5261 N LEU B 247 -13.530 -6.168 3.480 1.00 35.48 D000 N ANISOU 5261 N LEU B 247 4629 4445 4406 -225 -32 186 D000 N ATOM 5262 CA LEU B 247 -13.512 -7.345 4.343 1.00 34.88 D000 C ANISOU 5262 CA LEU B 247 4522 4310 4422 -265 -26 178 D000 C ATOM 5263 C LEU B 247 -12.958 -8.542 3.584 1.00 39.46 D000 C ANISOU 5263 C LEU B 247 5153 4814 5024 -259 -32 245 D000 C ATOM 5264 O LEU B 247 -13.292 -8.743 2.414 1.00 37.93 D000 O ANISOU 5264 O LEU B 247 5014 4624 4775 -251 -3 316 D000 O ATOM 5265 CB LEU B 247 -14.904 -7.733 4.851 1.00 36.15 D000 C ANISOU 5265 CB LEU B 247 4629 4484 4622 -324 28 167 D000 C ATOM 5266 CG LEU B 247 -15.844 -6.665 5.406 1.00 39.99 D000 C ANISOU 5266 CG LEU B 247 5057 5054 5084 -324 42 124 D000 C ATOM 5267 CD1 LEU B 247 -17.224 -7.270 5.597 1.00 41.47 D000 C ANISOU 5267 CD1 LEU B 247 5178 5251 5329 -388 87 132 D000 C ATOM 5268 CD2 LEU B 247 -15.320 -6.131 6.708 1.00 40.12 D000 C ANISOU 5268 CD2 LEU B 247 5050 5083 5111 -305 -4 54 D000 C ATOM 5269 N ALA B 248 -12.142 -9.354 4.264 1.00 36.69 D000 N ANISOU 5269 N ALA B 248 4795 4393 4752 -256 -59 227 D000 N ATOM 5270 CA ALA B 248 -11.619 -10.593 3.698 1.00 37.35 D000 C ANISOU 5270 CA ALA B 248 4926 4388 4877 -242 -61 293 D000 C ATOM 5271 C ALA B 248 -11.559 -11.645 4.797 1.00 41.53 D000 C ANISOU 5271 C ALA B 248 5435 4831 5513 -273 -44 250 D000 C ATOM 5272 O ALA B 248 -11.604 -11.330 5.986 1.00 43.93 D000 O ANISOU 5272 O ALA B 248 5696 5154 5841 -287 -48 166 D000 O ATOM 5273 CB ALA B 248 -10.231 -10.378 3.066 1.00 41.91 D000 C ANISOU 5273 CB ALA B 248 5531 4962 5432 -168 -137 323 D000 C ATOM 5274 N LYS B 249 -11.453 -12.908 4.393 1.00 39.87 D000 N ANISOU 5274 N LYS B 249 5268 4520 5359 -278 -23 309 D000 N ATOM 5275 CA ALYS B 249 -11.413 -14.024 5.326 0.46 40.65 D000 C ANISOU 5275 CA ALYS B 249 5367 4513 5563 -307 -2 265 D000 C ATOM 5276 CA BLYS B 249 -11.407 -14.018 5.331 0.54 40.62 D000 C ANISOU 5276 CA BLYS B 249 5364 4511 5560 -306 -3 264 D000 C ATOM 5277 C LYS B 249 -10.219 -14.914 5.022 1.00 44.69 D000 C ANISOU 5277 C LYS B 249 5924 4927 6131 -237 -21 315 D000 C ATOM 5278 O LYS B 249 -9.913 -15.183 3.859 1.00 44.77 D000 O ANISOU 5278 O LYS B 249 5981 4918 6112 -196 -32 418 D000 O ATOM 5279 CB ALYS B 249 -12.705 -14.840 5.248 0.46 43.25 D000 C ANISOU 5279 CB ALYS B 249 5701 4786 5945 -399 57 281 D000 C ATOM 5280 CB BLYS B 249 -12.695 -14.844 5.280 0.54 43.23 D000 C ANISOU 5280 CB BLYS B 249 5698 4784 5944 -399 57 279 D000 C ATOM 5281 CG ALYS B 249 -12.735 -16.036 6.167 0.46 44.94 D000 C ANISOU 5281 CG ALYS B 249 5928 4875 6273 -441 71 222 D000 C ATOM 5282 CG BLYS B 249 -12.713 -15.983 6.271 0.54 44.94 D000 C ANISOU 5282 CG BLYS B 249 5924 4879 6271 -440 68 212 D000 C ATOM 5283 CD ALYS B 249 -14.110 -16.671 6.168 0.46 49.27 D000 C ANISOU 5283 CD ALYS B 249 6455 5376 6889 -554 119 222 D000 C ATOM 5284 CD BLYS B 249 -13.950 -16.832 6.110 0.54 49.78 D000 C ANISOU 5284 CD BLYS B 249 6533 5421 6962 -545 121 230 D000 C ATOM 5285 CE ALYS B 249 -14.198 -17.782 7.196 0.46 50.18 D000 C ANISOU 5285 CE ALYS B 249 6587 5363 7117 -607 117 132 D000 C ATOM 5286 CE BLYS B 249 -13.881 -18.043 7.020 0.54 49.31 D000 C ANISOU 5286 CE BLYS B 249 6501 5215 7018 -587 123 155 D000 C ATOM 5287 NZ ALYS B 249 -13.785 -19.085 6.613 0.46 51.87 D000 N ANISOU 5287 NZ ALYS B 249 6878 5411 7421 -599 161 210 D000 N ATOM 5288 NZ BLYS B 249 -15.168 -18.778 7.051 0.54 52.44 D000 N ANISOU 5288 NZ BLYS B 249 6871 5542 7512 -713 162 147 D000 N ATOM 5289 N GLY B 250 -9.551 -15.379 6.068 1.00 41.84 D000 N ANISOU 5289 N GLY B 250 5552 4503 5844 -213 -23 246 D000 N ATOM 5290 CA GLY B 250 -8.479 -16.328 5.844 1.00 45.10 D000 C ANISOU 5290 CA GLY B 250 5998 4809 6329 -139 -30 294 D000 C ATOM 5291 C GLY B 250 -7.789 -16.714 7.131 1.00 44.97 D000 C ANISOU 5291 C GLY B 250 5968 4733 6387 -106 -12 201 D000 C ATOM 5292 O GLY B 250 -8.117 -16.231 8.218 1.00 44.42 D000 O ANISOU 5292 O GLY B 250 5872 4709 6296 -139 1 100 D000 O ATOM 5293 N LYS B 251 -6.818 -17.609 6.981 1.00 45.41 D000 N ANISOU 5293 N LYS B 251 5921 4359 6975 45 107 660 D000 N ATOM 5294 CA LYS B 251 -6.052 -18.110 8.116 1.00 45.87 D000 C ANISOU 5294 CA LYS B 251 5974 4333 7122 82 141 535 D000 C ATOM 5295 C LYS B 251 -4.938 -17.123 8.424 1.00 46.56 D000 C ANISOU 5295 C LYS B 251 6007 4647 7036 141 12 522 D000 C ATOM 5296 O LYS B 251 -4.126 -16.812 7.547 1.00 50.46 D000 O ANISOU 5296 O LYS B 251 6466 5283 7424 246 -31 686 D000 O ATOM 5297 CB LYS B 251 -5.486 -19.493 7.801 1.00 49.70 D000 C ANISOU 5297 CB LYS B 251 6494 4590 7800 217 307 670 D000 C ATOM 5298 CG LYS B 251 -4.528 -20.045 8.850 1.00 60.76 D000 C ANISOU 5298 CG LYS B 251 7886 5906 9295 289 358 557 D000 C ATOM 5299 CD LYS B 251 -3.524 -21.027 8.243 1.00107.14 D000 C ANISOU 5299 CD LYS B 251 13771 11656 15282 513 486 786 D000 C ATOM 5300 CE LYS B 251 -2.241 -20.331 7.789 1.00125.19 D000 C ANISOU 5300 CE LYS B 251 15973 14235 17360 670 357 938 D000 C ATOM 5301 NZ LYS B 251 -1.014 -21.067 8.217 1.00107.81 D000 N ANISOU 5301 NZ LYS B 251 13744 11972 15246 856 439 982 D000 N ATOM 5302 N VAL B 252 -4.879 -16.644 9.666 1.00 41.81 D000 N ANISOU 5302 N VAL B 252 5385 4104 6397 71 -41 327 D000 N ATOM 5303 CA VAL B 252 -3.863 -15.687 10.081 1.00 40.13 D000 C ANISOU 5303 CA VAL B 252 5126 4086 6038 105 -140 303 D000 C ATOM 5304 C VAL B 252 -3.181 -16.210 11.340 1.00 45.07 D000 C ANISOU 5304 C VAL B 252 5730 4667 6729 136 -105 165 D000 C ATOM 5305 O VAL B 252 -3.670 -17.121 12.010 1.00 44.64 D000 O ANISOU 5305 O VAL B 252 5693 4452 6814 97 -18 39 D000 O ATOM 5306 CB VAL B 252 -4.443 -14.276 10.323 1.00 41.30 D000 C ANISOU 5306 CB VAL B 252 5265 4389 6038 0 -232 233 D000 C ATOM 5307 CG1 VAL B 252 -5.077 -13.719 9.037 1.00 46.21 D000 C ANISOU 5307 CG1 VAL B 252 5903 5061 6593 -29 -256 349 D000 C ATOM 5308 CG2 VAL B 252 -5.457 -14.273 11.475 1.00 42.36 D000 C ANISOU 5308 CG2 VAL B 252 5399 4500 6197 -95 -224 61 D000 C ATOM 5309 N ILE B 253 -2.011 -15.645 11.639 1.00 39.16 D000 N ANISOU 5309 N ILE B 253 4932 4069 5878 195 -163 172 D000 N ATOM 5310 CA ILE B 253 -1.311 -15.943 12.885 1.00 38.64 D000 C ANISOU 5310 CA ILE B 253 4833 4010 5838 220 -144 35 D000 C ATOM 5311 C ILE B 253 -1.730 -14.898 13.910 1.00 41.03 D000 C ANISOU 5311 C ILE B 253 5116 4454 6019 112 -212 -101 D000 C ATOM 5312 O ILE B 253 -1.694 -13.697 13.630 1.00 43.57 D000 O ANISOU 5312 O ILE B 253 5431 4911 6211 76 -279 -45 D000 O ATOM 5313 CB ILE B 253 0.214 -15.952 12.684 1.00 40.81 D000 C ANISOU 5313 CB ILE B 253 5048 4392 6064 351 -157 124 D000 C ATOM 5314 CG1 ILE B 253 0.592 -17.081 11.737 1.00 46.95 D000 C ANISOU 5314 CG1 ILE B 253 5833 5046 6960 503 -70 292 D000 C ATOM 5315 CG2 ILE B 253 0.912 -16.176 14.005 1.00 45.20 D000 C ANISOU 5315 CG2 ILE B 253 5564 4975 6634 371 -137 -27 D000 C ATOM 5316 CD1 ILE B 253 2.015 -17.011 11.213 1.00 55.04 D000 C ANISOU 5316 CD1 ILE B 253 6767 6251 7893 654 -96 430 D000 C ATOM 5317 N GLU B 254 -2.157 -15.352 15.084 1.00 39.49 D000 N ANISOU 5317 N GLU B 254 4904 4233 5866 65 -176 -278 D000 N ATOM 5318 CA GLU B 254 -2.558 -14.470 16.172 1.00 40.79 D000 C ANISOU 5318 CA GLU B 254 5030 4572 5898 -4 -228 -385 D000 C ATOM 5319 C GLU B 254 -1.593 -14.685 17.327 1.00 45.69 D000 C ANISOU 5319 C GLU B 254 5593 5277 6492 38 -213 -498 D000 C ATOM 5320 O GLU B 254 -1.404 -15.818 17.776 1.00 46.16 D000 O ANISOU 5320 O GLU B 254 5638 5232 6669 56 -138 -623 D000 O ATOM 5321 CB GLU B 254 -3.994 -14.756 16.612 1.00 44.34 D000 C ANISOU 5321 CB GLU B 254 5467 5016 6364 -103 -209 -514 D000 C ATOM 5322 CG GLU B 254 -4.498 -13.824 17.695 1.00 44.49 D000 C ANISOU 5322 CG GLU B 254 5423 5267 6215 -139 -260 -584 D000 C ATOM 5323 CD GLU B 254 -5.968 -14.033 17.994 1.00 59.95 D000 C ANISOU 5323 CD GLU B 254 7337 7286 8156 -229 -253 -697 D000 C ATOM 5324 OE1 GLU B 254 -6.473 -15.142 17.742 1.00 55.45 D000 O ANISOU 5324 OE1 GLU B 254 6773 6567 7728 -294 -186 -806 D000 O ATOM 5325 OE2 GLU B 254 -6.631 -13.067 18.413 1.00 59.80 D000 O ANISOU 5325 OE2 GLU B 254 7276 7460 7987 -229 -300 -664 D000 O ATOM 5326 N GLY B 255 -0.967 -13.617 17.804 1.00 39.51 D000 N ANISOU 5326 N GLY B 255 4778 4667 5568 49 -263 -459 D000 N ATOM 5327 CA GLY B 255 -0.064 -13.777 18.927 1.00 42.54 D000 C ANISOU 5327 CA GLY B 255 5098 5157 5909 87 -246 -561 D000 C ATOM 5328 C GLY B 255 0.667 -12.488 19.233 1.00 39.65 D000 C ANISOU 5328 C GLY B 255 4707 4960 5399 91 -283 -475 D000 C ATOM 5329 O GLY B 255 0.333 -11.426 18.711 1.00 37.87 D000 O ANISOU 5329 O GLY B 255 4518 4759 5112 53 -307 -362 D000 O ATOM 5330 N ASN B 256 1.662 -12.605 20.108 1.00 39.37 D000 N ANISOU 5330 N ASN B 256 4609 5028 5322 131 -265 -541 D000 N ATOM 5331 CA ASN B 256 2.478 -11.470 20.518 1.00 40.64 D000 C ANISOU 5331 CA ASN B 256 4739 5343 5360 125 -270 -472 D000 C ATOM 5332 C ASN B 256 3.600 -11.268 19.516 1.00 39.84 D000 C ANISOU 5332 C ASN B 256 4632 5221 5285 145 -277 -377 D000 C ATOM 5333 O ASN B 256 4.459 -12.144 19.347 1.00 41.48 D000 O ANISOU 5333 O ASN B 256 4797 5409 5554 221 -266 -405 D000 O ATOM 5334 CB ASN B 256 3.059 -11.680 21.912 1.00 40.04 D000 C ANISOU 5334 CB ASN B 256 4581 5423 5210 155 -244 -585 D000 C ATOM 5335 CG ASN B 256 2.005 -11.596 22.996 1.00 43.05 D000 C ANISOU 5335 CG ASN B 256 4928 5932 5495 130 -242 -671 D000 C ATOM 5336 ND2 ASN B 256 1.819 -12.690 23.707 1.00 47.29 D000 N ANISOU 5336 ND2 ASN B 256 5410 6494 6062 136 -221 -865 D000 N ATOM 5337 OD1 ASN B 256 1.340 -10.570 23.167 1.00 42.78 D000 O ANISOU 5337 OD1 ASN B 256 4908 5984 5361 109 -249 -569 D000 O ATOM 5338 N AILE B 257 3.626 -10.092 18.893 0.58 38.10 D000 N ANISOU 5338 N AILE B 257 4439 5025 5011 79 -282 -276 D000 N ATOM 5339 N BILE B 257 3.589 -10.121 18.859 0.42 38.28 D000 N ANISOU 5339 N BILE B 257 4464 5042 5037 80 -283 -275 D000 N ATOM 5340 CA AILE B 257 4.538 -9.778 17.798 0.58 41.75 D000 C ANISOU 5340 CA AILE B 257 4875 5516 5472 64 -290 -212 D000 C ATOM 5341 CA BILE B 257 4.563 -9.781 17.837 0.42 41.76 D000 C ANISOU 5341 CA BILE B 257 4875 5520 5472 65 -290 -214 D000 C ATOM 5342 C AILE B 257 5.180 -8.427 18.084 0.58 41.44 D000 C ANISOU 5342 C AILE B 257 4814 5584 5348 -26 -246 -193 D000 C ATOM 5343 C BILE B 257 5.201 -8.463 18.241 0.42 41.48 D000 C ANISOU 5343 C BILE B 257 4816 5596 5350 -21 -244 -199 D000 C ATOM 5344 O AILE B 257 4.467 -7.427 18.245 0.58 43.51 D000 O ANISOU 5344 O AILE B 257 5139 5807 5587 -93 -206 -151 D000 O ATOM 5345 O BILE B 257 4.505 -7.535 18.668 0.42 43.47 D000 O ANISOU 5345 O BILE B 257 5123 5822 5570 -75 -202 -163 D000 O ATOM 5346 CB AILE B 257 3.797 -9.752 16.446 0.58 43.57 D000 C ANISOU 5346 CB AILE B 257 5163 5649 5744 40 -318 -140 D000 C ATOM 5347 CB BILE B 257 3.915 -9.675 16.440 0.42 43.49 D000 C ANISOU 5347 CB BILE B 257 5146 5652 5726 36 -316 -140 D000 C ATOM 5348 CG1AILE B 257 3.324 -11.168 16.074 0.58 41.83 D000 C ANISOU 5348 CG1AILE B 257 4961 5303 5629 131 -331 -139 D000 C ATOM 5349 CG1BILE B 257 2.908 -10.813 16.208 0.42 41.38 D000 C ANISOU 5349 CG1BILE B 257 4928 5237 5557 94 -331 -143 D000 C ATOM 5350 CG2AILE B 257 4.675 -9.123 15.377 0.58 42.90 D000 C ANISOU 5350 CG2AILE B 257 5026 5667 5607 -8 -323 -98 D000 C ATOM 5351 CG2BILE B 257 4.991 -9.670 15.373 0.42 44.80 D000 C ANISOU 5351 CG2BILE B 257 5237 5920 5863 46 -333 -99 D000 C ATOM 5352 CD1AILE B 257 2.032 -11.201 15.282 0.58 49.29 D000 C ANISOU 5352 CD1AILE B 257 5982 6126 6618 95 -343 -91 D000 C ATOM 5353 CD1BILE B 257 3.524 -12.120 15.769 0.42 45.51 D000 C ANISOU 5353 CD1BILE B 257 5415 5713 6164 210 -324 -127 D000 C ATOM 5354 N GLY B 258 6.509 -8.391 18.135 1.00 40.90 D000 N ANISOU 5354 N GLY B 258 4653 5644 5242 -26 -233 -218 D000 N ATOM 5355 CA GLY B 258 7.216 -7.147 18.397 1.00 43.60 D000 C ANISOU 5355 CA GLY B 258 4966 6079 5522 -138 -163 -218 D000 C ATOM 5356 C GLY B 258 8.619 -7.390 18.923 1.00 42.87 D000 C ANISOU 5356 C GLY B 258 4753 6155 5383 -116 -149 -271 D000 C ATOM 5357 O GLY B 258 9.226 -8.434 18.685 1.00 48.61 D000 O ANISOU 5357 O GLY B 258 5404 6944 6121 -10 -199 -296 D000 O ATOM 5358 N SER B 259 9.134 -6.376 19.614 1.00 45.69 D000 N ANISOU 5358 N SER B 259 5090 6580 5691 -210 -61 -275 D000 N ATOM 5359 CA SER B 259 10.483 -6.381 20.159 1.00 49.61 D000 C ANISOU 5359 CA SER B 259 5464 7256 6132 -220 -28 -327 D000 C ATOM 5360 C SER B 259 10.447 -6.653 21.658 1.00 51.63 D000 C ANISOU 5360 C SER B 259 5715 7554 6348 -144 -1 -334 D000 C ATOM 5361 O SER B 259 9.388 -6.694 22.281 1.00 49.97 D000 O ANISOU 5361 O SER B 259 5586 7263 6138 -100 -1 -300 D000 O ATOM 5362 CB SER B 259 11.168 -5.034 19.898 1.00 51.45 D000 C ANISOU 5362 CB SER B 259 5664 7544 6339 -406 81 -341 D000 C ATOM 5363 OG SER B 259 10.524 -4.017 20.664 1.00 51.19 D000 O ANISOU 5363 OG SER B 259 5737 7393 6321 -468 195 -268 D000 O ATOM 5364 N GLU B 260 11.633 -6.809 22.252 1.00 55.38 D000 N ANISOU 5364 N GLU B 260 6074 8200 6770 -132 27 -386 D000 N ATOM 5365 CA GLU B 260 11.685 -6.874 23.709 1.00 57.46 D000 C ANISOU 5365 CA GLU B 260 6317 8547 6969 -81 71 -395 D000 C ATOM 5366 C GLU B 260 11.163 -5.586 24.334 1.00 51.51 D000 C ANISOU 5366 C GLU B 260 5639 7756 6177 -169 181 -289 D000 C ATOM 5367 O GLU B 260 10.679 -5.592 25.470 1.00 65.86 D000 O ANISOU 5367 O GLU B 260 7467 9631 7924 -103 207 -255 D000 O ATOM 5368 CB GLU B 260 13.113 -7.136 24.205 1.00 61.76 D000 C ANISOU 5368 CB GLU B 260 6715 9295 7457 -65 97 -465 D000 C ATOM 5369 CG GLU B 260 13.854 -8.245 23.494 1.00 79.30 D000 C ANISOU 5369 CG GLU B 260 8840 11578 9713 40 20 -534 D000 C ATOM 5370 CD GLU B 260 14.718 -7.726 22.366 1.00 88.74 D000 C ANISOU 5370 CD GLU B 260 9947 12874 10895 -58 21 -530 D000 C ATOM 5371 OE1 GLU B 260 14.260 -6.816 21.641 1.00 70.72 D000 O ANISOU 5371 OE1 GLU B 260 7733 10506 8632 -196 46 -492 D000 O ATOM 5372 OE2 GLU B 260 15.860 -8.213 22.218 1.00 94.36 D000 O ANISOU 5372 OE2 GLU B 260 10508 13776 11568 3 6 -578 D000 O ATOM 5373 N LEU B 261 11.256 -4.476 23.604 1.00 55.45 D000 N ANISOU 5373 N LEU B 261 6181 8169 6718 -311 262 -237 D000 N ATOM 5374 CA LEU B 261 10.882 -3.171 24.129 1.00 59.01 D000 C ANISOU 5374 CA LEU B 261 6712 8544 7166 -388 415 -114 D000 C ATOM 5375 C LEU B 261 9.370 -2.985 24.116 1.00 61.97 D000 C ANISOU 5375 C LEU B 261 7212 8771 7561 -318 402 -12 D000 C ATOM 5376 O LEU B 261 8.793 -2.422 25.056 1.00 55.37 D000 O ANISOU 5376 O LEU B 261 6419 7946 6672 -262 488 118 D000 O ATOM 5377 CB LEU B 261 11.555 -2.087 23.289 1.00 65.31 D000 C ANISOU 5377 CB LEU B 261 7509 9275 8030 -585 536 -135 D000 C ATOM 5378 CG LEU B 261 12.888 -1.463 23.720 1.00 79.56 D000 C ANISOU 5378 CG LEU B 261 9213 11205 9810 -716 670 -172 D000 C ATOM 5379 CD1 LEU B 261 12.994 -0.053 23.121 1.00 75.12 D000 C ANISOU 5379 CD1 LEU B 261 8714 10483 9346 -930 863 -164 D000 C ATOM 5380 CD2 LEU B 261 13.084 -1.424 25.234 1.00 73.28 D000 C ANISOU 5380 CD2 LEU B 261 8392 10522 8927 -630 741 -79 D000 C ATOM 5381 N LYS B 262 8.709 -3.462 23.067 1.00 47.79 D000 N ANISOU 5381 N LYS B 262 5464 6865 5829 -308 298 -55 D000 N ATOM 5382 CA LYS B 262 7.290 -3.217 22.895 1.00 42.84 D000 C ANISOU 5382 CA LYS B 262 4945 6103 5227 -260 291 33 D000 C ATOM 5383 C LYS B 262 6.715 -4.298 21.998 1.00 46.98 D000 C ANISOU 5383 C LYS B 262 5479 6573 5797 -212 141 -48 D000 C ATOM 5384 O LYS B 262 7.265 -4.570 20.929 1.00 44.36 D000 O ANISOU 5384 O LYS B 262 5120 6222 5514 -268 96 -116 D000 O ATOM 5385 CB LYS B 262 7.045 -1.839 22.285 1.00 48.35 D000 C ANISOU 5385 CB LYS B 262 5738 6632 6002 -374 437 118 D000 C ATOM 5386 CG LYS B 262 5.588 -1.424 22.308 1.00 55.68 D000 C ANISOU 5386 CG LYS B 262 6772 7441 6945 -296 461 241 D000 C ATOM 5387 CD LYS B 262 5.005 -1.456 20.915 1.00 56.28 D000 C ANISOU 5387 CD LYS B 262 6907 7371 7106 -353 407 188 D000 C ATOM 5388 CE LYS B 262 3.657 -0.756 20.845 1.00 62.30 D000 C ANISOU 5388 CE LYS B 262 7775 7999 7899 -295 475 318 D000 C ATOM 5389 NZ LYS B 262 2.545 -1.678 21.160 1.00 61.82 D000 N ANISOU 5389 NZ LYS B 262 7699 8014 7774 -158 336 331 D000 N ATOM 5390 N ARG B 263 5.627 -4.918 22.430 1.00 44.41 D000 N ANISOU 5390 N ARG B 263 5178 6246 5448 -112 75 -40 D000 N ATOM 5391 CA AARG B 263 4.920 -5.941 21.674 0.50 43.41 D000 C ANISOU 5391 CA AARG B 263 5073 6041 5380 -72 -37 -104 D000 C ATOM 5392 CA BARG B 263 4.947 -5.856 21.555 0.50 43.55 D000 C ANISOU 5392 CA BARG B 263 5095 6047 5404 -82 -33 -99 D000 C ATOM 5393 C ARG B 263 3.466 -5.534 21.463 1.00 44.43 D000 C ANISOU 5393 C ARG B 263 5285 6079 5518 -58 -34 -28 D000 C ATOM 5394 O ARG B 263 2.922 -4.711 22.202 1.00 41.79 D000 O ANISOU 5394 O ARG B 263 4973 5784 5121 -29 39 74 D000 O ATOM 5395 CB AARG B 263 4.978 -7.296 22.394 0.50 49.19 D000 C ANISOU 5395 CB AARG B 263 5736 6859 6094 17 -106 -221 D000 C ATOM 5396 CB BARG B 263 5.161 -7.306 21.995 0.50 50.40 D000 C ANISOU 5396 CB BARG B 263 5894 6981 6273 2 -113 -220 D000 C ATOM 5397 CG AARG B 263 6.197 -8.139 22.029 0.50 50.56 D000 C ANISOU 5397 CG AARG B 263 5839 7058 6312 38 -137 -305 D000 C ATOM 5398 CG BARG B 263 4.489 -7.704 23.274 0.50 50.60 D000 C ANISOU 5398 CG BARG B 263 5888 7118 6221 68 -117 -266 D000 C ATOM 5399 CD AARG B 263 6.662 -9.009 23.182 0.50 56.80 D000 C ANISOU 5399 CD AARG B 263 6548 7971 7062 115 -138 -416 D000 C ATOM 5400 CD BARG B 263 5.241 -8.865 23.919 0.50 53.85 D000 C ANISOU 5400 CD BARG B 263 6211 7619 6630 124 -140 -413 D000 C ATOM 5401 NE AARG B 263 8.088 -9.298 23.077 0.50 61.50 D000 N ANISOU 5401 NE AARG B 263 7058 8645 7663 136 -128 -454 D000 N ATOM 5402 NE BARG B 263 6.581 -8.499 24.365 0.50 60.19 D000 N ANISOU 5402 NE BARG B 263 6946 8541 7383 118 -93 -406 D000 N ATOM 5403 CZ AARG B 263 8.639 -9.988 22.087 0.50 60.53 D000 C ANISOU 5403 CZ AARG B 263 6911 8468 7619 180 -163 -463 D000 C ATOM 5404 CZ BARG B 263 7.424 -9.330 24.967 0.50 58.51 D000 C ANISOU 5404 CZ BARG B 263 6646 8426 7158 173 -94 -523 D000 C ATOM 5405 NH1AARG B 263 7.904 -10.544 21.139 0.50 60.91 D000 N ANISOU 5405 NH1AARG B 263 7023 8362 7757 205 -204 -438 D000 N ATOM 5406 NH1BARG B 263 7.087 -10.581 25.239 0.50 62.00 D000 N ANISOU 5406 NH1BARG B 263 7067 8841 7651 235 -123 -668 D000 N ATOM 5407 NH2AARG B 263 9.962 -10.123 22.047 0.50 60.70 D000 N ANISOU 5407 NH2AARG B 263 6831 8616 7618 209 -150 -483 D000 N ATOM 5408 NH2BARG B 263 8.634 -8.895 25.305 0.50 64.29 D000 N ANISOU 5408 NH2BARG B 263 7309 9281 7837 157 -48 -506 D000 N ATOM 5409 N AASP B 264 2.841 -6.175 20.476 0.28 38.03 D000 N ANISOU 5409 N AASP B 264 4509 5163 4779 -60 -109 -63 D000 N ATOM 5410 N BASP B 264 2.852 -6.121 20.441 0.72 37.59 D000 N ANISOU 5410 N BASP B 264 4455 5103 4723 -64 -106 -60 D000 N ATOM 5411 CA AASP B 264 1.429 -6.016 20.165 0.28 41.21 D000 C ANISOU 5411 CA AASP B 264 4973 5492 5194 -45 -123 -15 D000 C ATOM 5412 CA BASP B 264 1.429 -6.044 20.183 0.72 41.16 D000 C ANISOU 5412 CA BASP B 264 4965 5488 5187 -43 -125 -17 D000 C ATOM 5413 C AASP B 264 0.803 -7.398 20.059 0.28 40.18 D000 C ANISOU 5413 C AASP B 264 4821 5344 5102 -7 -211 -115 D000 C ATOM 5414 C BASP B 264 0.879 -7.459 20.235 0.72 39.94 D000 C ANISOU 5414 C BASP B 264 4779 5333 5062 -0 -211 -125 D000 C ATOM 5415 O AASP B 264 1.362 -8.281 19.399 0.28 41.52 D000 O ANISOU 5415 O AASP B 264 4977 5451 5345 -7 -251 -174 D000 O ATOM 5416 O BASP B 264 1.568 -8.415 19.856 0.72 41.93 D000 O ANISOU 5416 O BASP B 264 5005 5549 5378 8 -247 -200 D000 O ATOM 5417 CB AASP B 264 1.225 -5.270 18.843 0.28 45.86 D000 C ANISOU 5417 CB AASP B 264 5635 5942 5847 -118 -95 41 D000 C ATOM 5418 CB BASP B 264 1.087 -5.467 18.794 0.72 46.76 D000 C ANISOU 5418 CB BASP B 264 5748 6053 5966 -110 -112 32 D000 C ATOM 5419 CG AASP B 264 1.500 -3.793 18.957 0.28 43.91 D000 C ANISOU 5419 CG AASP B 264 5432 5659 5594 -172 37 128 D000 C ATOM 5420 CG BASP B 264 1.697 -4.112 18.539 0.72 42.35 D000 C ANISOU 5420 CG BASP B 264 5223 5452 5415 -191 2 90 D000 C ATOM 5421 OD1AASP B 264 0.814 -3.118 19.752 0.28 43.59 D000 O ANISOU 5421 OD1AASP B 264 5418 5632 5511 -112 109 232 D000 O ATOM 5422 OD1BASP B 264 1.784 -3.294 19.482 0.72 44.53 D000 O ANISOU 5422 OD1BASP B 264 5508 5762 5651 -173 101 166 D000 O ATOM 5423 OD2AASP B 264 2.401 -3.307 18.243 0.28 45.16 D000 O ANISOU 5423 OD2AASP B 264 5587 5781 5789 -274 83 94 D000 O ATOM 5424 OD2BASP B 264 2.045 -3.853 17.365 0.72 39.10 D000 O ANISOU 5424 OD2BASP B 264 4827 4979 5051 -277 7 58 D000 O ATOM 5425 N TYR B 265 -0.345 -7.586 20.698 1.00 39.67 D000 N ANISOU 5425 N TYR B 265 4742 5344 4989 28 -226 -133 D000 N ATOM 5426 CA TYR B 265 -1.112 -8.818 20.560 1.00 37.50 D000 C ANISOU 5426 CA TYR B 265 4448 5032 4769 28 -280 -250 D000 C ATOM 5427 C TYR B 265 -2.001 -8.589 19.343 1.00 38.33 D000 C ANISOU 5427 C TYR B 265 4625 5000 4939 -6 -294 -179 D000 C ATOM 5428 O TYR B 265 -2.921 -7.769 19.399 1.00 41.33 D000 O ANISOU 5428 O TYR B 265 5024 5418 5263 4 -276 -99 D000 O ATOM 5429 CB TYR B 265 -1.920 -9.132 21.807 1.00 42.37 D000 C ANISOU 5429 CB TYR B 265 4982 5836 5282 54 -286 -341 D000 C ATOM 5430 CG TYR B 265 -2.549 -10.496 21.713 1.00 42.33 D000 C ANISOU 5430 CG TYR B 265 4947 5777 5359 16 -311 -516 D000 C ATOM 5431 CD1 TYR B 265 -1.850 -11.632 22.074 1.00 49.23 D000 C ANISOU 5431 CD1 TYR B 265 5784 6616 6305 12 -296 -676 D000 C ATOM 5432 CD2 TYR B 265 -3.829 -10.647 21.204 1.00 43.69 D000 C ANISOU 5432 CD2 TYR B 265 5133 5910 5558 -22 -328 -524 D000 C ATOM 5433 CE1 TYR B 265 -2.425 -12.889 21.961 1.00 54.21 D000 C ANISOU 5433 CE1 TYR B 265 6402 7145 7050 -37 -277 -845 D000 C ATOM 5434 CE2 TYR B 265 -4.416 -11.898 21.093 1.00 51.10 D000 C ANISOU 5434 CE2 TYR B 265 6047 6774 6595 -84 -322 -695 D000 C ATOM 5435 CZ TYR B 265 -3.707 -13.013 21.469 1.00 52.84 D000 C ANISOU 5435 CZ TYR B 265 6242 6929 6905 -95 -286 -856 D000 C ATOM 5436 OH TYR B 265 -4.282 -14.259 21.351 1.00 57.61 D000 O ANISOU 5436 OH TYR B 265 6835 7412 7643 -169 -239 -1035 D000 O ATOM 5437 N THR B 266 -1.693 -9.249 18.227 1.00 37.68 D000 N ANISOU 5437 N THR B 266 4578 4775 4964 -28 -316 -188 D000 N ATOM 5438 CA THR B 266 -2.330 -8.872 16.961 1.00 39.13 D000 C ANISOU 5438 CA THR B 266 4825 4854 5190 -62 -323 -105 D000 C ATOM 5439 C THR B 266 -2.262 -10.041 15.978 1.00 43.75 D000 C ANISOU 5439 C THR B 266 5423 5317 5883 -60 -345 -123 D000 C ATOM 5440 O THR B 266 -1.941 -11.172 16.355 1.00 40.49 D000 O ANISOU 5440 O THR B 266 4981 4868 5535 -29 -338 -205 D000 O ATOM 5441 CB THR B 266 -1.675 -7.590 16.421 1.00 39.30 D000 C ANISOU 5441 CB THR B 266 4880 4873 5178 -94 -286 -16 D000 C ATOM 5442 CG2 THR B 266 -0.279 -7.844 15.906 1.00 42.40 D000 C ANISOU 5442 CG2 THR B 266 5242 5278 5591 -105 -294 -30 D000 C ATOM 5443 OG1 THR B 266 -2.481 -7.035 15.369 1.00 41.11 D000 O ANISOU 5443 OG1 THR B 266 5165 5027 5427 -131 -277 44 D000 O ATOM 5444 N ILE B 267 -2.604 -9.780 14.711 1.00 37.10 D000 N ANISOU 5444 N ILE B 267 4624 4407 5064 -86 -352 -42 D000 N ATOM 5445 CA ILE B 267 -2.646 -10.829 13.700 1.00 36.77 D000 C ANISOU 5445 CA ILE B 267 4595 4263 5114 -65 -357 -12 D000 C ATOM 5446 C ILE B 267 -1.699 -10.494 12.557 1.00 41.29 D000 C ANISOU 5446 C ILE B 267 5155 4878 5654 -52 -369 76 D000 C ATOM 5447 O ILE B 267 -1.354 -9.338 12.308 1.00 42.86 D000 O ANISOU 5447 O ILE B 267 5351 5158 5776 -103 -368 90 D000 O ATOM 5448 CB ILE B 267 -4.072 -11.088 13.141 1.00 35.67 D000 C ANISOU 5448 CB ILE B 267 4493 4044 5017 -104 -352 3 D000 C ATOM 5449 CG1 ILE B 267 -4.662 -9.802 12.550 1.00 40.46 D000 C ANISOU 5449 CG1 ILE B 267 5130 4695 5548 -146 -360 66 D000 C ATOM 5450 CG2 ILE B 267 -4.981 -11.682 14.202 1.00 40.65 D000 C ANISOU 5450 CG2 ILE B 267 5100 4671 5677 -129 -337 -118 D000 C ATOM 5451 CD1 ILE B 267 -5.922 -10.050 11.739 1.00 44.93 D000 C ANISOU 5451 CD1 ILE B 267 5722 5200 6148 -178 -357 98 D000 C ATOM 5452 N LEU B 268 -1.305 -11.553 11.846 1.00 39.90 D000 N ANISOU 5452 N LEU B 268 4964 4656 5542 17 -363 134 D000 N ATOM 5453 CA ALEU B 268 -0.384 -11.499 10.719 0.59 40.99 D000 C ANISOU 5453 CA ALEU B 268 5052 4897 5626 60 -379 229 D000 C ATOM 5454 CA BLEU B 268 -0.398 -11.485 10.710 0.41 41.00 D000 C ANISOU 5454 CA BLEU B 268 5054 4898 5626 59 -380 229 D000 C ATOM 5455 C LEU B 268 -0.864 -12.485 9.660 1.00 41.37 D000 C ANISOU 5455 C LEU B 268 5117 4861 5740 126 -357 347 D000 C ATOM 5456 O LEU B 268 -1.134 -13.641 9.988 1.00 46.62 D000 O ANISOU 5456 O LEU B 268 5810 5369 6533 187 -305 354 D000 O ATOM 5457 CB ALEU B 268 1.034 -11.895 11.159 0.59 46.22 D000 C ANISOU 5457 CB ALEU B 268 5639 5648 6276 144 -378 219 D000 C ATOM 5458 CB BLEU B 268 1.032 -11.813 11.161 0.41 46.19 D000 C ANISOU 5458 CB BLEU B 268 5634 5649 6265 137 -379 216 D000 C ATOM 5459 CG ALEU B 268 2.098 -10.876 11.519 0.59 47.84 D000 C ANISOU 5459 CG ALEU B 268 5778 6027 6373 91 -395 161 D000 C ATOM 5460 CG BLEU B 268 2.218 -11.374 10.320 0.41 49.34 D000 C ANISOU 5460 CG BLEU B 268 5935 6264 6550 155 -406 267 D000 C ATOM 5461 CD1ALEU B 268 3.322 -11.628 12.050 0.59 45.21 D000 C ANISOU 5461 CD1ALEU B 268 5366 5758 6053 201 -386 154 D000 C ATOM 5462 CD1BLEU B 268 2.369 -9.883 10.409 0.41 54.14 D000 C ANISOU 5462 CD1BLEU B 268 6533 6978 7061 10 -413 180 D000 C ATOM 5463 CD2ALEU B 268 2.466 -10.062 10.304 0.59 54.80 D000 C ANISOU 5463 CD2ALEU B 268 6605 7072 7145 31 -416 195 D000 C ATOM 5464 CD2BLEU B 268 3.469 -12.059 10.827 0.41 47.54 D000 C ANISOU 5464 CD2BLEU B 268 5623 6109 6329 271 -397 270 D000 C ATOM 5465 N GLY B 269 -0.946 -12.064 8.400 1.00 43.66 D000 N ANISOU 5465 N GLY B 269 5386 5256 5947 113 -379 434 D000 N ATOM 5466 CA GLY B 269 -1.259 -13.022 7.349 1.00 43.45 D000 C ANISOU 5466 CA GLY B 269 5362 5184 5965 200 -346 586 D000 C ATOM 5467 C GLY B 269 -1.810 -12.385 6.092 1.00 42.09 D000 C ANISOU 5467 C GLY B 269 5178 5126 5687 145 -370 647 D000 C ATOM 5468 O GLY B 269 -2.165 -11.209 6.061 1.00 39.07 D000 O ANISOU 5468 O GLY B 269 4807 4809 5230 25 -399 550 D000 O ATOM 5469 N ASP B 270 -1.936 -13.228 5.050 1.00 43.62 D000 N ANISOU 5469 N ASP B 270 5354 5331 5890 244 -337 819 D000 N ATOM 5470 CA AASP B 270 -2.289 -12.730 3.722 0.35 46.82 D000 C ANISOU 5470 CA AASP B 270 5718 5908 6162 214 -359 892 D000 C ATOM 5471 CA BASP B 270 -2.288 -12.733 3.721 0.65 46.83 D000 C ANISOU 5471 CA BASP B 270 5720 5909 6164 214 -359 893 D000 C ATOM 5472 C ASP B 270 -3.671 -12.092 3.692 1.00 43.30 D000 C ANISOU 5472 C ASP B 270 5353 5358 5741 78 -357 808 D000 C ATOM 5473 O ASP B 270 -3.906 -11.163 2.912 1.00 44.12 D000 O ANISOU 5473 O ASP B 270 5427 5615 5721 -0 -383 771 D000 O ATOM 5474 CB AASP B 270 -2.223 -13.863 2.691 0.35 48.76 D000 C ANISOU 5474 CB AASP B 270 5929 6183 6413 372 -306 1132 D000 C ATOM 5475 CB BASP B 270 -2.219 -13.876 2.698 0.65 48.74 D000 C ANISOU 5475 CB BASP B 270 5928 6179 6413 374 -305 1133 D000 C ATOM 5476 CG AASP B 270 -2.461 -13.374 1.271 0.35 51.43 D000 C ANISOU 5476 CG AASP B 270 6196 6773 6573 356 -333 1214 D000 C ATOM 5477 CG BASP B 270 -0.804 -14.381 2.469 0.65 53.20 D000 C ANISOU 5477 CG BASP B 270 6377 6932 6903 546 -308 1255 D000 C ATOM 5478 OD1AASP B 270 -1.709 -12.488 0.812 0.35 50.40 D000 O ANISOU 5478 OD1AASP B 270 5954 6939 6255 313 -397 1138 D000 O ATOM 5479 OD1BASP B 270 0.153 -13.612 2.664 0.65 55.36 D000 O ANISOU 5479 OD1BASP B 270 6559 7425 7050 508 -375 1145 D000 O ATOM 5480 OD2AASP B 270 -3.405 -13.867 0.618 0.35 48.76 D000 O ANISOU 5480 OD2AASP B 270 5902 6347 6277 372 -281 1336 D000 O ATOM 5481 OD2BASP B 270 -0.646 -15.557 2.087 0.65 58.96 D000 O ANISOU 5481 OD2BASP B 270 7103 7592 7708 726 -226 1471 D000 O ATOM 5482 N ALA B 271 -4.605 -12.577 4.516 1.00 40.82 D000 N ANISOU 5482 N ALA B 271 5126 4807 5578 46 -318 763 D000 N ATOM 5483 CA ALA B 271 -5.947 -11.993 4.521 1.00 41.79 D000 C ANISOU 5483 CA ALA B 271 5302 4866 5710 -65 -317 692 D000 C ATOM 5484 C ALA B 271 -5.908 -10.508 4.841 1.00 41.41 D000 C ANISOU 5484 C ALA B 271 5253 4914 5568 -155 -357 559 D000 C ATOM 5485 O ALA B 271 -6.812 -9.760 4.451 1.00 39.86 D000 O ANISOU 5485 O ALA B 271 5079 4732 5335 -223 -351 525 D000 O ATOM 5486 CB ALA B 271 -6.839 -12.712 5.532 1.00 41.38 D000 C ANISOU 5486 CB ALA B 271 5308 4605 5811 -95 -273 625 D000 C ATOM 5487 N VAL B 272 -4.885 -10.058 5.568 1.00 42.60 D000 N ANISOU 5487 N VAL B 272 5378 5115 5691 -154 -377 485 D000 N ATOM 5488 CA VAL B 272 -4.779 -8.636 5.856 1.00 39.31 D000 C ANISOU 5488 CA VAL B 272 4969 4756 5210 -241 -375 375 D000 C ATOM 5489 C VAL B 272 -4.522 -7.850 4.575 1.00 41.26 D000 C ANISOU 5489 C VAL B 272 5168 5169 5339 -299 -372 361 D000 C ATOM 5490 O VAL B 272 -5.157 -6.813 4.339 1.00 39.01 D000 O ANISOU 5490 O VAL B 272 4918 4872 5034 -379 -335 291 D000 O ATOM 5491 CB VAL B 272 -3.682 -8.360 6.900 1.00 41.09 D000 C ANISOU 5491 CB VAL B 272 5173 5003 5435 -236 -379 307 D000 C ATOM 5492 CG1 VAL B 272 -3.515 -6.858 7.072 1.00 41.99 D000 C ANISOU 5492 CG1 VAL B 272 5301 5152 5501 -332 -338 211 D000 C ATOM 5493 CG2 VAL B 272 -4.006 -9.039 8.239 1.00 39.81 D000 C ANISOU 5493 CG2 VAL B 272 5046 4711 5368 -192 -377 286 D000 C ATOM 5494 N ASN B 273 -3.558 -8.302 3.747 1.00 41.05 D000 N ANISOU 5494 N ASN B 273 5049 5324 5225 -254 -399 419 D000 N ATOM 5495 CA AASN B 273 -3.317 -7.558 2.521 0.55 43.10 D000 C ANISOU 5495 CA AASN B 273 5231 5802 5341 -325 -397 373 D000 C ATOM 5496 CA BASN B 273 -3.291 -7.662 2.455 0.46 43.00 D000 C ANISOU 5496 CA BASN B 273 5214 5801 5325 -314 -400 387 D000 C ATOM 5497 C ASN B 273 -4.545 -7.601 1.613 1.00 41.07 D000 C ANISOU 5497 C ASN B 273 5006 5527 5070 -337 -381 426 D000 C ATOM 5498 O ASN B 273 -4.800 -6.625 0.901 1.00 41.11 D000 O ANISOU 5498 O ASN B 273 4993 5633 4995 -436 -353 324 D000 O ATOM 5499 CB AASN B 273 -2.073 -8.081 1.799 0.55 44.94 D000 C ANISOU 5499 CB AASN B 273 5323 6309 5445 -254 -436 438 D000 C ATOM 5500 CB BASN B 273 -2.277 -8.422 1.590 0.46 43.18 D000 C ANISOU 5500 CB BASN B 273 5102 6079 5226 -217 -440 496 D000 C ATOM 5501 CG AASN B 273 -0.797 -7.241 2.083 0.55 45.86 D000 C ANISOU 5501 CG AASN B 273 5349 6595 5481 -342 -436 283 D000 C ATOM 5502 CG BASN B 273 -1.089 -8.859 2.329 0.46 49.50 D000 C ANISOU 5502 CG BASN B 273 5851 6916 6041 -145 -461 508 D000 C ATOM 5503 ND2AASN B 273 0.250 -7.535 1.322 0.55 51.13 D000 N ANISOU 5503 ND2AASN B 273 5855 7580 5993 -294 -474 316 D000 N ATOM 5504 ND2BASN B 273 0.090 -8.521 1.818 0.46 43.60 D000 N ANISOU 5504 ND2BASN B 273 4956 6470 5139 -161 -485 458 D000 N ATOM 5505 OD1AASN B 273 -0.754 -6.347 2.958 0.55 48.19 D000 O ANISOU 5505 OD1AASN B 273 5707 6757 5846 -447 -393 146 D000 O ATOM 5506 OD1BASN B 273 -1.211 -9.548 3.325 0.46 52.74 D000 O ANISOU 5506 OD1BASN B 273 6336 7114 6590 -75 -452 552 D000 O ATOM 5507 N VAL B 274 -5.297 -8.705 1.618 1.00 40.21 D000 N ANISOU 5507 N VAL B 274 4942 5290 5044 -250 -382 569 D000 N ATOM 5508 CA VAL B 274 -6.467 -8.793 0.759 1.00 38.40 D000 C ANISOU 5508 CA VAL B 274 4736 5055 4801 -266 -360 628 D000 C ATOM 5509 C VAL B 274 -7.521 -7.786 1.202 1.00 40.28 D000 C ANISOU 5509 C VAL B 274 5050 5166 5089 -359 -328 503 D000 C ATOM 5510 O VAL B 274 -8.111 -7.086 0.367 1.00 39.95 D000 O ANISOU 5510 O VAL B 274 4999 5204 4977 -418 -302 457 D000 O ATOM 5511 CB VAL B 274 -7.025 -10.231 0.731 1.00 44.42 D000 C ANISOU 5511 CB VAL B 274 5530 5679 5668 -170 -337 802 D000 C ATOM 5512 CG1 VAL B 274 -8.315 -10.281 -0.091 1.00 43.38 D000 C ANISOU 5512 CG1 VAL B 274 5419 5535 5527 -205 -304 856 D000 C ATOM 5513 CG2 VAL B 274 -6.001 -11.193 0.129 1.00 48.98 D000 C ANISOU 5513 CG2 VAL B 274 6029 6387 6194 -37 -339 973 D000 C ATOM 5514 N ALA B 275 -7.772 -7.690 2.512 1.00 39.11 D000 N ANISOU 5514 N ALA B 275 4967 4843 5050 -359 -322 452 D000 N ATOM 5515 CA ALA B 275 -8.748 -6.722 3.011 1.00 38.95 D000 C ANISOU 5515 CA ALA B 275 5004 4730 5065 -407 -282 370 D000 C ATOM 5516 C ALA B 275 -8.322 -5.300 2.684 1.00 39.23 D000 C ANISOU 5516 C ALA B 275 5037 4828 5039 -482 -231 252 D000 C ATOM 5517 O ALA B 275 -9.148 -4.460 2.322 1.00 37.34 D000 O ANISOU 5517 O ALA B 275 4828 4564 4797 -518 -172 203 D000 O ATOM 5518 CB ALA B 275 -8.935 -6.883 4.519 1.00 37.42 D000 C ANISOU 5518 CB ALA B 275 4850 4406 4961 -374 -286 350 D000 C ATOM 5519 N ALA B 276 -7.030 -5.005 2.804 1.00 38.50 D000 N ANISOU 5519 N ALA B 276 4906 4814 4909 -514 -234 191 D000 N ATOM 5520 CA ALA B 276 -6.562 -3.658 2.510 1.00 39.06 D000 C ANISOU 5520 CA ALA B 276 4970 4928 4943 -621 -153 44 D000 C ATOM 5521 C ALA B 276 -6.692 -3.338 1.031 1.00 41.79 D000 C ANISOU 5521 C ALA B 276 5253 5448 5178 -691 -136 -20 D000 C ATOM 5522 O ALA B 276 -7.032 -2.205 0.666 1.00 41.81 D000 O ANISOU 5522 O ALA B 276 5281 5419 5185 -780 -36 -150 D000 O ATOM 5523 CB ALA B 276 -5.115 -3.499 2.986 1.00 39.94 D000 C ANISOU 5523 CB ALA B 276 5032 5109 5034 -659 -157 -21 D000 C ATOM 5524 N ARG B 277 -6.437 -4.323 0.157 1.00 40.03 D000 N ANISOU 5524 N ARG B 277 4943 5414 4852 -644 -214 75 D000 N ATOM 5525 CA ARG B 277 -6.592 -4.104 -1.275 1.00 41.98 D000 C ANISOU 5525 CA ARG B 277 5107 5886 4957 -696 -204 31 D000 C ATOM 5526 C ARG B 277 -8.056 -3.906 -1.646 1.00 41.30 D000 C ANISOU 5526 C ARG B 277 5087 5695 4910 -693 -163 53 D000 C ATOM 5527 O ARG B 277 -8.381 -3.088 -2.516 1.00 43.63 D000 O ANISOU 5527 O ARG B 277 5355 6088 5134 -778 -101 -73 D000 O ATOM 5528 CB ARG B 277 -6.008 -5.289 -2.041 1.00 49.41 D000 C ANISOU 5528 CB ARG B 277 5934 7066 5772 -602 -288 187 D000 C ATOM 5529 CG ARG B 277 -6.414 -5.361 -3.493 1.00 69.42 D000 C ANISOU 5529 CG ARG B 277 8379 9851 8146 -611 -288 214 D000 C ATOM 5530 CD ARG B 277 -5.355 -6.086 -4.283 1.00 97.31 D000 C ANISOU 5530 CD ARG B 277 11750 13728 11495 -534 -350 321 D000 C ATOM 5531 NE ARG B 277 -5.673 -7.507 -4.328 1.00 99.66 D000 N ANISOU 5531 NE ARG B 277 12071 13957 11840 -360 -379 607 D000 N ATOM 5532 CZ ARG B 277 -5.000 -8.451 -3.682 1.00 90.37 D000 C ANISOU 5532 CZ ARG B 277 10899 12702 10737 -234 -406 754 D000 C ATOM 5533 NH1 ARG B 277 -3.943 -8.164 -2.938 1.00 89.28 D000 N ANISOU 5533 NH1 ARG B 277 10733 12579 10613 -254 -429 653 D000 N ATOM 5534 NH2 ARG B 277 -5.410 -9.712 -3.768 1.00 79.81 D000 N ANISOU 5534 NH2 ARG B 277 9599 11248 9476 -89 -389 1001 D000 N ATOM 5535 N LEU B 278 -8.951 -4.656 -1.014 1.00 40.31 D000 N ANISOU 5535 N LEU B 278 5035 5389 4891 -603 -189 193 D000 N ATOM 5536 CA LEU B 278 -10.365 -4.490 -1.322 1.00 38.23 D000 C ANISOU 5536 CA LEU B 278 4815 5051 4658 -599 -151 213 D000 C ATOM 5537 C LEU B 278 -10.871 -3.122 -0.877 1.00 39.93 D000 C ANISOU 5537 C LEU B 278 5100 5131 4941 -646 -52 76 D000 C ATOM 5538 O LEU B 278 -11.659 -2.488 -1.593 1.00 41.02 D000 O ANISOU 5538 O LEU B 278 5240 5294 5052 -678 13 13 D000 O ATOM 5539 CB LEU B 278 -11.185 -5.608 -0.686 1.00 40.57 D000 C ANISOU 5539 CB LEU B 278 5153 5210 5054 -518 -189 363 D000 C ATOM 5540 CG LEU B 278 -10.939 -7.017 -1.245 1.00 44.87 D000 C ANISOU 5540 CG LEU B 278 5650 5829 5571 -459 -235 528 D000 C ATOM 5541 CD1 LEU B 278 -11.686 -8.089 -0.416 1.00 46.80 D000 C ANISOU 5541 CD1 LEU B 278 5943 5883 5956 -415 -238 622 D000 C ATOM 5542 CD2 LEU B 278 -11.297 -7.098 -2.716 1.00 58.29 D000 C ANISOU 5542 CD2 LEU B 278 7285 7723 7141 -469 -221 584 D000 C ATOM 5543 N GLU B 279 -10.445 -2.658 0.307 1.00 37.81 D000 N ANISOU 5543 N GLU B 279 4887 4715 4764 -636 -24 42 D000 N ATOM 5544 CA GLU B 279 -10.854 -1.331 0.766 1.00 40.11 D000 C ANISOU 5544 CA GLU B 279 5250 4856 5134 -652 104 -50 D000 C ATOM 5545 C GLU B 279 -10.421 -0.266 -0.235 1.00 39.05 D000 C ANISOU 5545 C GLU B 279 5093 4794 4952 -777 211 -235 D000 C ATOM 5546 O GLU B 279 -11.183 0.654 -0.563 1.00 41.55 D000 O ANISOU 5546 O GLU B 279 5451 5027 5308 -792 332 -311 D000 O ATOM 5547 CB GLU B 279 -10.264 -1.056 2.154 1.00 38.47 D000 C ANISOU 5547 CB GLU B 279 5093 4513 5013 -618 127 -32 D000 C ATOM 5548 CG GLU B 279 -10.793 0.198 2.858 1.00 35.81 D000 C ANISOU 5548 CG GLU B 279 4840 3992 4774 -581 277 -51 D000 C ATOM 5549 CD GLU B 279 -10.262 1.502 2.291 1.00 46.43 D000 C ANISOU 5549 CD GLU B 279 6213 5277 6153 -697 443 -220 D000 C ATOM 5550 OE1 GLU B 279 -9.101 1.546 1.823 1.00 40.47 D000 O ANISOU 5550 OE1 GLU B 279 5404 4625 5347 -824 437 -345 D000 O ATOM 5551 OE2 GLU B 279 -11.008 2.508 2.317 1.00 40.97 D000 O ANISOU 5551 OE2 GLU B 279 5588 4436 5543 -663 598 -239 D000 O ATOM 5552 N ALA B 280 -9.204 -0.397 -0.762 1.00 40.08 D000 N ANISOU 5552 N ALA B 280 5139 5101 4988 -869 176 -324 D000 N ATOM 5553 CA ALA B 280 -8.701 0.578 -1.720 1.00 43.10 D000 C ANISOU 5553 CA ALA B 280 5468 5603 5305 -1023 280 -550 D000 C ATOM 5554 C ALA B 280 -9.507 0.568 -3.013 1.00 42.13 D000 C ANISOU 5554 C ALA B 280 5292 5638 5077 -1044 286 -591 D000 C ATOM 5555 O ALA B 280 -9.641 1.611 -3.668 1.00 45.72 D000 O ANISOU 5555 O ALA B 280 5742 6103 5527 -1156 422 -797 D000 O ATOM 5556 CB ALA B 280 -7.220 0.299 -1.995 1.00 46.80 D000 C ANISOU 5556 CB ALA B 280 5816 6308 5657 -1109 218 -631 D000 C ATOM 5557 N LEU B 281 -10.052 -0.587 -3.394 1.00 42.81 D000 N ANISOU 5557 N LEU B 281 5340 5838 5087 -944 161 -406 D000 N ATOM 5558 CA LEU B 281 -10.871 -0.681 -4.594 1.00 45.21 D000 C ANISOU 5558 CA LEU B 281 5591 6305 5283 -953 166 -413 D000 C ATOM 5559 C LEU B 281 -12.126 0.187 -4.526 1.00 47.41 D000 C ANISOU 5559 C LEU B 281 5959 6389 5667 -940 289 -472 D000 C ATOM 5560 O LEU B 281 -12.669 0.557 -5.578 1.00 48.82 D000 O ANISOU 5560 O LEU B 281 6091 6697 5761 -988 345 -570 D000 O ATOM 5561 CB LEU B 281 -11.286 -2.132 -4.827 1.00 52.36 D000 C ANISOU 5561 CB LEU B 281 6461 7303 6131 -838 39 -165 D000 C ATOM 5562 CG LEU B 281 -10.383 -3.035 -5.662 1.00 71.31 D000 C ANISOU 5562 CG LEU B 281 8728 10013 8353 -821 -53 -77 D000 C ATOM 5563 CD1 LEU B 281 -11.020 -4.422 -5.699 1.00 66.58 D000 C ANISOU 5563 CD1 LEU B 281 8141 9383 7773 -693 -122 194 D000 C ATOM 5564 CD2 LEU B 281 -10.178 -2.484 -7.067 1.00 62.88 D000 C ANISOU 5564 CD2 LEU B 281 7530 9281 7080 -918 -18 -232 D000 C ATOM 5565 N THR B 282 -12.601 0.517 -3.321 1.00 42.34 D000 N ANISOU 5565 N THR B 282 5429 5468 5192 -861 337 -408 D000 N ATOM 5566 CA THR B 282 -13.815 1.311 -3.210 1.00 40.79 D000 C ANISOU 5566 CA THR B 282 5303 5107 5089 -807 459 -426 D000 C ATOM 5567 C THR B 282 -13.650 2.705 -3.790 1.00 43.75 D000 C ANISOU 5567 C THR B 282 5698 5429 5496 -916 651 -670 D000 C ATOM 5568 O THR B 282 -14.655 3.364 -4.063 1.00 52.67 D000 O ANISOU 5568 O THR B 282 6866 6469 6679 -874 769 -710 D000 O ATOM 5569 CB THR B 282 -14.264 1.457 -1.745 1.00 40.16 D000 C ANISOU 5569 CB THR B 282 5316 4789 5155 -679 482 -295 D000 C ATOM 5570 CG2 THR B 282 -14.551 0.101 -1.131 1.00 41.78 D000 C ANISOU 5570 CG2 THR B 282 5495 5040 5341 -594 317 -102 D000 C ATOM 5571 OG1 THR B 282 -13.247 2.110 -0.983 1.00 40.20 D000 O ANISOU 5571 OG1 THR B 282 5371 4661 5242 -719 557 -362 D000 O ATOM 5572 N ARG B 283 -12.411 3.195 -3.921 1.00 44.00 D000 N ANISOU 5572 N ARG B 283 5702 5502 5514 -1057 704 -848 D000 N ATOM 5573 CA ARG B 283 -12.204 4.499 -4.532 1.00 43.39 D000 C ANISOU 5573 CA ARG B 283 5634 5372 5479 -1201 913 -1130 D000 C ATOM 5574 C ARG B 283 -12.580 4.503 -6.012 1.00 58.42 D000 C ANISOU 5574 C ARG B 283 7431 7545 7219 -1286 916 -1279 D000 C ATOM 5575 O ARG B 283 -12.842 5.573 -6.570 1.00 57.89 D000 O ANISOU 5575 O ARG B 283 7381 7410 7204 -1379 1111 -1513 D000 O ATOM 5576 CB ARG B 283 -10.754 4.948 -4.390 1.00 48.46 D000 C ANISOU 5576 CB ARG B 283 6242 6044 6127 -1370 970 -1317 D000 C ATOM 5577 CG ARG B 283 -10.219 4.992 -2.957 1.00 51.74 D000 C ANISOU 5577 CG ARG B 283 6750 6223 6688 -1306 980 -1187 D000 C ATOM 5578 CD ARG B 283 -11.015 5.955 -2.108 1.00 50.38 D000 C ANISOU 5578 CD ARG B 283 6733 5677 6733 -1199 1179 -1124 D000 C ATOM 5579 NE ARG B 283 -10.414 6.155 -0.791 1.00 44.95 D000 N ANISOU 5579 NE ARG B 283 6123 4787 6169 -1152 1223 -1018 D000 N ATOM 5580 CZ ARG B 283 -10.564 5.340 0.244 1.00 40.92 D000 C ANISOU 5580 CZ ARG B 283 5631 4264 5653 -993 1072 -766 D000 C ATOM 5581 NH1 ARG B 283 -11.295 4.241 0.162 1.00 44.70 D000 N ANISOU 5581 NH1 ARG B 283 6064 4889 6030 -875 877 -601 D000 N ATOM 5582 NH2 ARG B 283 -9.959 5.630 1.389 1.00 40.34 D000 N ANISOU 5582 NH2 ARG B 283 5617 4031 5678 -964 1133 -693 D000 N ATOM 5583 N GLN B 284 -12.604 3.338 -6.656 1.00 52.04 D000 N ANISOU 5583 N GLN B 284 6512 7038 6221 -1252 724 -1148 D000 N ATOM 5584 CA GLN B 284 -12.933 3.260 -8.076 1.00 56.96 D000 C ANISOU 5584 CA GLN B 284 7015 7972 6654 -1318 717 -1258 D000 C ATOM 5585 C GLN B 284 -14.348 2.770 -8.342 1.00 59.99 D000 C ANISOU 5585 C GLN B 284 7421 8343 7029 -1184 679 -1078 D000 C ATOM 5586 O GLN B 284 -14.762 2.732 -9.503 1.00 57.23 D000 O ANISOU 5586 O GLN B 284 6978 8243 6525 -1225 687 -1153 D000 O ATOM 5587 CB GLN B 284 -11.945 2.349 -8.818 1.00 55.67 D000 C ANISOU 5587 CB GLN B 284 6684 8220 6249 -1367 557 -1228 D000 C ATOM 5588 CG GLN B 284 -10.501 2.400 -8.350 1.00 79.55 D000 C ANISOU 5588 CG GLN B 284 9663 11300 9263 -1453 529 -1310 D000 C ATOM 5589 CD GLN B 284 -9.707 1.194 -8.822 1.00111.46 D000 C ANISOU 5589 CD GLN B 284 13552 15714 13085 -1403 342 -1149 D000 C ATOM 5590 NE2 GLN B 284 -8.565 0.949 -8.188 1.00104.86 D000 N ANISOU 5590 NE2 GLN B 284 12687 14896 12258 -1415 284 -1129 D000 N ATOM 5591 OE1 GLN B 284 -10.116 0.493 -9.750 1.00109.84 D000 O ANISOU 5591 OE1 GLN B 284 13251 15779 12704 -1341 265 -1027 D000 O ATOM 5592 N LEU B 285 -15.099 2.413 -7.309 1.00 54.36 D000 N ANISOU 5592 N LEU B 285 6812 7380 6462 -1034 644 -858 D000 N ATOM 5593 CA LEU B 285 -16.448 1.883 -7.435 1.00 54.26 D000 C ANISOU 5593 CA LEU B 285 6805 7364 6447 -916 606 -688 D000 C ATOM 5594 C LEU B 285 -17.440 2.859 -6.819 1.00 60.22 D000 C ANISOU 5594 C LEU B 285 7662 7843 7374 -829 760 -716 D000 C ATOM 5595 O LEU B 285 -17.071 3.740 -6.042 1.00 59.29 D000 O ANISOU 5595 O LEU B 285 7634 7490 7404 -824 880 -789 D000 O ATOM 5596 CB LEU B 285 -16.548 0.525 -6.733 1.00 56.89 D000 C ANISOU 5596 CB LEU B 285 7142 7685 6790 -817 437 -414 D000 C ATOM 5597 CG LEU B 285 -15.616 -0.552 -7.288 1.00 60.33 D000 C ANISOU 5597 CG LEU B 285 7483 8366 7075 -853 303 -325 D000 C ATOM 5598 CD1 LEU B 285 -15.660 -1.796 -6.422 1.00 67.84 D000 C ANISOU 5598 CD1 LEU B 285 8465 9217 8096 -758 185 -84 D000 C ATOM 5599 CD2 LEU B 285 -15.999 -0.898 -8.719 1.00 67.17 D000 C ANISOU 5599 CD2 LEU B 285 8238 9533 7751 -882 291 -319 D000 C ATOM 5600 N SER B 286 -18.716 2.695 -7.159 1.00 59.37 D000 N ANISOU 5600 N SER B 286 7535 7774 7248 -747 768 -637 D000 N ATOM 5601 CA SER B 286 -19.736 3.464 -6.456 1.00 63.80 D000 C ANISOU 5601 CA SER B 286 8174 8107 7961 -613 896 -602 D000 C ATOM 5602 C SER B 286 -19.942 2.954 -5.033 1.00 63.74 D000 C ANISOU 5602 C SER B 286 8212 7959 8047 -482 811 -386 D000 C ATOM 5603 O SER B 286 -20.369 3.725 -4.165 1.00 59.74 D000 O ANISOU 5603 O SER B 286 7774 7255 7670 -360 925 -346 D000 O ATOM 5604 CB SER B 286 -21.055 3.432 -7.233 1.00 70.75 D000 C ANISOU 5604 CB SER B 286 8997 9108 8778 -559 929 -587 D000 C ATOM 5605 OG SER B 286 -21.463 2.103 -7.499 1.00 75.38 D000 O ANISOU 5605 OG SER B 286 9502 9890 9250 -556 757 -415 D000 O ATOM 5606 N GLN B 287 -19.618 1.689 -4.772 1.00 54.20 D000 N ANISOU 5606 N GLN B 287 6961 6856 6776 -501 629 -247 D000 N ATOM 5607 CA GLN B 287 -19.868 1.079 -3.476 1.00 46.35 D000 C ANISOU 5607 CA GLN B 287 5986 5775 5850 -400 543 -76 D000 C ATOM 5608 C GLN B 287 -18.757 1.411 -2.484 1.00 42.86 D000 C ANISOU 5608 C GLN B 287 5614 5182 5490 -402 553 -88 D000 C ATOM 5609 O GLN B 287 -17.576 1.403 -2.832 1.00 48.11 D000 O ANISOU 5609 O GLN B 287 6280 5876 6122 -513 535 -179 D000 O ATOM 5610 CB GLN B 287 -19.983 -0.438 -3.630 1.00 49.18 D000 C ANISOU 5610 CB GLN B 287 6277 6276 6134 -434 380 53 D000 C ATOM 5611 CG GLN B 287 -21.272 -0.877 -4.331 1.00 50.19 D000 C ANISOU 5611 CG GLN B 287 6333 6535 6203 -420 376 106 D000 C ATOM 5612 CD GLN B 287 -21.162 -0.885 -5.846 1.00 60.59 D000 C ANISOU 5612 CD GLN B 287 7600 8027 7395 -509 397 35 D000 C ATOM 5613 NE2 GLN B 287 -22.278 -1.156 -6.510 1.00 74.15 D000 N ANISOU 5613 NE2 GLN B 287 9255 9864 9056 -499 413 75 D000 N ATOM 5614 OE1 GLN B 287 -20.098 -0.648 -6.414 1.00 53.51 D000 O ANISOU 5614 OE1 GLN B 287 6703 7191 6436 -588 401 -61 D000 O ATOM 5615 N ALA B 288 -19.150 1.680 -1.239 1.00 41.50 D000 N ANISOU 5615 N ALA B 288 5479 4884 5405 -273 581 13 D000 N ATOM 5616 CA ALA B 288 -18.211 2.001 -0.172 1.00 42.85 D000 C ANISOU 5616 CA ALA B 288 5712 4917 5651 -254 602 31 D000 C ATOM 5617 C ALA B 288 -17.793 0.785 0.636 1.00 37.26 D000 C ANISOU 5617 C ALA B 288 4970 4273 4914 -257 432 134 D000 C ATOM 5618 O ALA B 288 -16.920 0.917 1.501 1.00 41.43 D000 O ANISOU 5618 O ALA B 288 5538 4718 5486 -251 431 147 D000 O ATOM 5619 CB ALA B 288 -18.817 3.031 0.783 1.00 46.17 D000 C ANISOU 5619 CB ALA B 288 6186 5186 6170 -86 750 108 D000 C ATOM 5620 N LEU B 289 -18.434 -0.366 0.403 1.00 38.42 D000 N ANISOU 5620 N LEU B 289 5045 4551 5000 -267 311 201 D000 N ATOM 5621 CA LEU B 289 -18.155 -1.634 1.078 1.00 37.15 D000 C ANISOU 5621 CA LEU B 289 4850 4432 4833 -283 176 276 D000 C ATOM 5622 C LEU B 289 -17.952 -2.713 0.024 1.00 43.98 D000 C ANISOU 5622 C LEU B 289 5674 5397 5641 -380 97 287 D000 C ATOM 5623 O LEU B 289 -18.809 -2.902 -0.843 1.00 40.45 D000 O ANISOU 5623 O LEU B 289 5185 5035 5149 -397 110 299 D000 O ATOM 5624 CB LEU B 289 -19.320 -2.019 2.007 1.00 38.82 D000 C ANISOU 5624 CB LEU B 289 5004 4696 5050 -193 146 353 D000 C ATOM 5625 CG LEU B 289 -19.380 -3.446 2.533 1.00 37.48 D000 C ANISOU 5625 CG LEU B 289 4778 4582 4881 -241 33 387 D000 C ATOM 5626 CD1 LEU B 289 -18.215 -3.667 3.525 1.00 41.15 D000 C ANISOU 5626 CD1 LEU B 289 5279 4978 5379 -239 -11 383 D000 C ATOM 5627 CD2 LEU B 289 -20.724 -3.675 3.217 1.00 44.66 D000 C ANISOU 5627 CD2 LEU B 289 5595 5606 5769 -181 24 412 D000 C ATOM 5628 N AVAL B 290 -16.834 -3.426 0.083 0.47 36.76 D000 N ANISOU 5628 N AVAL B 290 4764 4481 4723 -428 28 301 D000 N ATOM 5629 N BVAL B 290 -16.818 -3.406 0.110 0.53 36.71 D000 N ANISOU 5629 N BVAL B 290 4759 4471 4717 -427 29 300 D000 N ATOM 5630 CA AVAL B 290 -16.634 -4.568 -0.805 0.47 38.30 D000 C ANISOU 5630 CA AVAL B 290 4917 4765 4869 -479 -31 367 D000 C ATOM 5631 CA BVAL B 290 -16.482 -4.526 -0.760 0.53 38.26 D000 C ANISOU 5631 CA BVAL B 290 4915 4755 4865 -480 -32 361 D000 C ATOM 5632 C AVAL B 290 -15.921 -5.673 -0.047 0.47 39.95 D000 C ANISOU 5632 C AVAL B 290 5130 4916 5135 -472 -101 431 D000 C ATOM 5633 C BVAL B 290 -16.036 -5.685 0.118 0.53 39.83 D000 C ANISOU 5633 C BVAL B 290 5116 4888 5130 -467 -101 430 D000 C ATOM 5634 O AVAL B 290 -15.034 -5.413 0.774 0.47 40.35 D000 O ANISOU 5634 O AVAL B 290 5209 4907 5215 -456 -117 395 D000 O ATOM 5635 O BVAL B 290 -15.459 -5.482 1.191 0.53 38.66 D000 O ANISOU 5635 O BVAL B 290 4996 4666 5028 -440 -116 400 D000 O ATOM 5636 CB AVAL B 290 -15.854 -4.184 -2.079 0.47 41.93 D000 C ANISOU 5636 CB AVAL B 290 5354 5352 5225 -534 -13 315 D000 C ATOM 5637 CB BVAL B 290 -15.376 -4.137 -1.766 0.53 42.88 D000 C ANISOU 5637 CB BVAL B 290 5486 5446 5360 -534 -24 302 D000 C ATOM 5638 CG1AVAL B 290 -16.651 -3.180 -2.897 0.47 44.40 D000 C ANISOU 5638 CG1AVAL B 290 5658 5723 5490 -553 73 226 D000 C ATOM 5639 CG1BVAL B 290 -14.798 -5.366 -2.430 0.53 44.82 D000 C ANISOU 5639 CG1BVAL B 290 5682 5797 5549 -540 -88 416 D000 C ATOM 5640 CG2AVAL B 290 -14.484 -3.640 -1.720 0.47 38.22 D000 C ANISOU 5640 CG2AVAL B 290 4905 4864 4755 -560 -13 232 D000 C ATOM 5641 CG2BVAL B 290 -15.918 -3.161 -2.799 0.53 45.63 D000 C ANISOU 5641 CG2BVAL B 290 5818 5881 5639 -570 57 205 D000 C ATOM 5642 N PHE B 291 -16.300 -6.910 -0.331 1.00 37.80 D000 N ANISOU 5642 N PHE B 291 4829 4648 4885 -486 -122 524 D000 N ATOM 5643 CA PHE B 291 -15.764 -8.061 0.380 1.00 36.01 D000 C ANISOU 5643 CA PHE B 291 4610 4330 4741 -479 -156 575 D000 C ATOM 5644 C PHE B 291 -15.621 -9.243 -0.563 1.00 42.55 D000 C ANISOU 5644 C PHE B 291 5419 5173 5574 -485 -140 708 D000 C ATOM 5645 O PHE B 291 -16.229 -9.300 -1.635 1.00 41.08 D000 O ANISOU 5645 O PHE B 291 5205 5076 5328 -502 -108 770 D000 O ATOM 5646 CB PHE B 291 -16.608 -8.421 1.628 1.00 38.69 D000 C ANISOU 5646 CB PHE B 291 4939 4595 5168 -486 -157 526 D000 C ATOM 5647 CG PHE B 291 -18.111 -8.454 1.401 1.00 36.83 D000 C ANISOU 5647 CG PHE B 291 4656 4410 4928 -518 -124 518 D000 C ATOM 5648 CD1 PHE B 291 -18.721 -9.597 0.925 1.00 36.67 D000 C ANISOU 5648 CD1 PHE B 291 4607 4364 4961 -581 -88 575 D000 C ATOM 5649 CD2 PHE B 291 -18.901 -7.351 1.701 1.00 38.82 D000 C ANISOU 5649 CD2 PHE B 291 4887 4732 5130 -478 -109 463 D000 C ATOM 5650 CE1 PHE B 291 -20.105 -9.641 0.728 1.00 43.07 D000 C ANISOU 5650 CE1 PHE B 291 5357 5242 5764 -627 -52 555 D000 C ATOM 5651 CE2 PHE B 291 -20.279 -7.378 1.492 1.00 42.89 D000 C ANISOU 5651 CE2 PHE B 291 5338 5330 5629 -495 -80 457 D000 C ATOM 5652 CZ PHE B 291 -20.875 -8.528 1.022 1.00 42.58 D000 C ANISOU 5652 CZ PHE B 291 5258 5287 5632 -582 -59 491 D000 C ATOM 5653 N SER B 292 -14.778 -10.186 -0.145 1.00 41.70 D000 N ANISOU 5653 N SER B 292 5326 4979 5539 -455 -148 767 D000 N ATOM 5654 CA SER B 292 -14.453 -11.344 -0.954 1.00 41.46 D000 C ANISOU 5654 CA SER B 292 5286 4936 5530 -420 -106 934 D000 C ATOM 5655 C SER B 292 -15.565 -12.388 -0.907 1.00 45.06 D000 C ANISOU 5655 C SER B 292 5749 5258 6113 -472 -25 985 D000 C ATOM 5656 O SER B 292 -16.417 -12.392 -0.019 1.00 42.03 D000 O ANISOU 5656 O SER B 292 5364 4798 5806 -542 -18 864 D000 O ATOM 5657 CB SER B 292 -13.168 -11.979 -0.456 1.00 47.00 D000 C ANISOU 5657 CB SER B 292 6003 5571 6286 -349 -119 981 D000 C ATOM 5658 OG SER B 292 -13.392 -12.486 0.843 1.00 46.75 D000 O ANISOU 5658 OG SER B 292 6003 5358 6401 -380 -105 889 D000 O ATOM 5659 N SER B 293 -15.506 -13.318 -1.857 1.00 44.66 D000 N ANISOU 5659 N SER B 293 5694 5194 6081 -438 49 1172 D000 N ATOM 5660 CA SER B 293 -16.510 -14.376 -1.914 1.00 43.46 D000 C ANISOU 5660 CA SER B 293 5553 4888 6072 -506 163 1230 D000 C ATOM 5661 C SER B 293 -16.462 -15.274 -0.683 1.00 47.82 D000 C ANISOU 5661 C SER B 293 6141 5204 6825 -552 218 1138 D000 C ATOM 5662 O SER B 293 -17.483 -15.864 -0.312 1.00 48.70 D000 O ANISOU 5662 O SER B 293 6244 5201 7060 -667 300 1061 D000 O ATOM 5663 CB SER B 293 -16.306 -15.206 -3.180 1.00 53.34 D000 C ANISOU 5663 CB SER B 293 6799 6158 7309 -432 259 1491 D000 C ATOM 5664 OG SER B 293 -14.996 -15.737 -3.201 1.00 58.12 D000 O ANISOU 5664 OG SER B 293 7421 6731 7930 -301 268 1624 D000 O ATOM 5665 N GLU B 294 -15.291 -15.414 -0.052 1.00 47.60 D000 N ANISOU 5665 N GLU B 294 6140 5117 6829 -474 183 1124 D000 N ATOM 5666 CA GLU B 294 -15.224 -16.223 1.164 1.00 49.17 D000 C ANISOU 5666 CA GLU B 294 6365 5107 7209 -524 239 1001 D000 C ATOM 5667 C GLU B 294 -16.042 -15.605 2.292 1.00 47.40 D000 C ANISOU 5667 C GLU B 294 6101 4940 6969 -635 174 755 D000 C ATOM 5668 O GLU B 294 -16.635 -16.331 3.097 1.00 47.40 D000 O ANISOU 5668 O GLU B 294 6085 4822 7103 -742 247 617 D000 O ATOM 5669 CB GLU B 294 -13.772 -16.421 1.601 1.00 53.27 D000 C ANISOU 5669 CB GLU B 294 6911 5583 7747 -404 211 1035 D000 C ATOM 5670 CG GLU B 294 -12.964 -17.319 0.653 1.00 62.81 D000 C ANISOU 5670 CG GLU B 294 8142 6724 8998 -265 307 1298 D000 C ATOM 5671 CD GLU B 294 -12.511 -16.623 -0.623 1.00 84.22 D000 C ANISOU 5671 CD GLU B 294 10807 9702 11492 -165 235 1469 D000 C ATOM 5672 OE1 GLU B 294 -12.583 -15.378 -0.700 1.00 64.78 D000 O ANISOU 5672 OE1 GLU B 294 8307 7446 8861 -206 110 1355 D000 O ATOM 5673 OE2 GLU B 294 -12.090 -17.334 -1.561 1.00105.48 D000 O ANISOU 5673 OE2 GLU B 294 13492 12404 14180 -42 319 1719 D000 O ATOM 5674 N VAL B 295 -16.105 -14.276 2.353 1.00 43.91 D000 N ANISOU 5674 N VAL B 295 5632 4690 6362 -611 57 697 D000 N ATOM 5675 CA VAL B 295 -16.978 -13.618 3.323 1.00 40.38 D000 C ANISOU 5675 CA VAL B 295 5132 4336 5873 -676 7 517 D000 C ATOM 5676 C VAL B 295 -18.439 -13.835 2.954 1.00 44.55 D000 C ANISOU 5676 C VAL B 295 5605 4905 6417 -778 64 489 D000 C ATOM 5677 O VAL B 295 -19.271 -14.175 3.805 1.00 45.27 D000 O ANISOU 5677 O VAL B 295 5630 5013 6557 -876 88 336 D000 O ATOM 5678 CB VAL B 295 -16.635 -12.121 3.410 1.00 41.18 D000 C ANISOU 5678 CB VAL B 295 5234 4593 5820 -600 -92 499 D000 C ATOM 5679 CG1 VAL B 295 -17.626 -11.392 4.285 1.00 40.77 D000 C ANISOU 5679 CG1 VAL B 295 5120 4659 5711 -622 -123 374 D000 C ATOM 5680 CG2 VAL B 295 -15.199 -11.933 3.929 1.00 43.47 D000 C ANISOU 5680 CG2 VAL B 295 5563 4853 6102 -525 -139 499 D000 C ATOM 5681 N LYS B 296 -18.773 -13.644 1.678 1.00 42.60 D000 N ANISOU 5681 N LYS B 296 5365 4709 6112 -764 88 624 D000 N ATOM 5682 CA LYS B 296 -20.143 -13.864 1.225 1.00 42.32 D000 C ANISOU 5682 CA LYS B 296 5271 4721 6087 -862 151 611 D000 C ATOM 5683 C LYS B 296 -20.600 -15.287 1.524 1.00 47.21 D000 C ANISOU 5683 C LYS B 296 5880 5164 6893 -991 282 568 D000 C ATOM 5684 O LYS B 296 -21.735 -15.508 1.975 1.00 47.89 D000 O ANISOU 5684 O LYS B 296 5881 5302 7011 -1119 321 426 D000 O ATOM 5685 CB LYS B 296 -20.229 -13.556 -0.273 1.00 48.69 D000 C ANISOU 5685 CB LYS B 296 6092 5608 6800 -817 169 781 D000 C ATOM 5686 CG LYS B 296 -21.634 -13.643 -0.872 1.00 48.78 D000 C ANISOU 5686 CG LYS B 296 6038 5699 6797 -908 232 782 D000 C ATOM 5687 CD LYS B 296 -21.743 -14.770 -1.864 1.00 51.10 D000 C ANISOU 5687 CD LYS B 296 6354 5881 7179 -948 363 957 D000 C ATOM 5688 CE LYS B 296 -23.130 -14.831 -2.488 1.00 57.19 D000 C ANISOU 5688 CE LYS B 296 7054 6746 7930 -1049 433 958 D000 C ATOM 5689 NZ LYS B 296 -23.605 -16.238 -2.565 1.00 66.58 D000 N ANISOU 5689 NZ LYS B 296 8247 7740 9312 -1177 605 1005 D000 N ATOM 5690 N ASN B 297 -19.735 -16.269 1.292 1.00 49.32 D000 N ANISOU 5690 N ASN B 297 6222 5224 7292 -961 368 681 D000 N ATOM 5691 CA ASN B 297 -20.155 -17.654 1.432 1.00 50.33 D000 C ANISOU 5691 CA ASN B 297 6359 5126 7637 -1087 544 654 D000 C ATOM 5692 C ASN B 297 -20.245 -18.095 2.884 1.00 51.80 D000 C ANISOU 5692 C ASN B 297 6506 5245 7931 -1196 562 392 D000 C ATOM 5693 O ASN B 297 -20.933 -19.079 3.173 1.00 51.86 D000 O ANISOU 5693 O ASN B 297 6484 5112 8107 -1362 712 269 D000 O ATOM 5694 CB ASN B 297 -19.204 -18.565 0.655 1.00 54.96 D000 C ANISOU 5694 CB ASN B 297 7042 5501 8341 -983 663 899 D000 C ATOM 5695 CG ASN B 297 -19.394 -18.441 -0.843 1.00 58.45 D000 C ANISOU 5695 CG ASN B 297 7491 6030 8688 -914 695 1156 D000 C ATOM 5696 ND2 ASN B 297 -18.325 -18.654 -1.600 1.00 64.86 D000 N ANISOU 5696 ND2 ASN B 297 8352 6825 9465 -745 711 1399 D000 N ATOM 5697 OD1 ASN B 297 -20.503 -18.178 -1.314 1.00 65.84 D000 O ANISOU 5697 OD1 ASN B 297 8372 7076 9568 -1007 710 1135 D000 O ATOM 5698 N SER B 298 -19.594 -17.377 3.797 1.00 50.75 D000 N ANISOU 5698 N SER B 298 6362 5223 7698 -1118 424 290 D000 N ATOM 5699 CA SER B 298 -19.644 -17.675 5.221 1.00 54.86 D000 C ANISOU 5699 CA SER B 298 6823 5751 8270 -1207 422 34 D000 C ATOM 5700 C SER B 298 -20.802 -16.993 5.947 1.00 52.72 D000 C ANISOU 5700 C SER B 298 6410 5761 7861 -1293 342 -162 D000 C ATOM 5701 O SER B 298 -21.058 -17.320 7.110 1.00 57.25 D000 O ANISOU 5701 O SER B 298 6893 6404 8453 -1393 351 -397 D000 O ATOM 5702 CB SER B 298 -18.326 -17.257 5.889 1.00 58.37 D000 C ANISOU 5702 CB SER B 298 7315 6199 8663 -1068 322 39 D000 C ATOM 5703 OG SER B 298 -17.224 -17.928 5.308 1.00 64.03 D000 O ANISOU 5703 OG SER B 298 8139 6695 9496 -970 396 214 D000 O ATOM 5704 N ALA B 299 -21.493 -16.053 5.310 1.00 48.74 D000 N ANISOU 5704 N ALA B 299 5868 5445 7208 -1247 270 -73 D000 N ATOM 5705 CA ALA B 299 -22.652 -15.432 5.942 1.00 53.26 D000 C ANISOU 5705 CA ALA B 299 6289 6304 7645 -1298 210 -226 D000 C ATOM 5706 C ALA B 299 -23.824 -16.406 5.981 1.00 52.14 D000 C ANISOU 5706 C ALA B 299 6039 6168 7604 -1517 335 -387 D000 C ATOM 5707 O ALA B 299 -23.965 -17.279 5.119 1.00 55.31 D000 O ANISOU 5707 O ALA B 299 6500 6352 8162 -1610 474 -309 D000 O ATOM 5708 CB ALA B 299 -23.049 -14.161 5.192 1.00 51.74 D000 C ANISOU 5708 CB ALA B 299 6093 6281 7286 -1172 126 -81 D000 C ATOM 5709 N THR B 300 -24.684 -16.257 6.998 1.00 52.60 D000 N ANISOU 5709 N THR B 300 5920 6499 7565 -1602 299 -612 D000 N ATOM 5710 CA THR B 300 -25.846 -17.122 7.127 1.00 56.36 D000 C ANISOU 5710 CA THR B 300 6256 7041 8117 -1841 419 -817 D000 C ATOM 5711 C THR B 300 -27.173 -16.419 6.859 1.00 59.99 D000 C ANISOU 5711 C THR B 300 6558 7830 8408 -1849 370 -827 D000 C ATOM 5712 O THR B 300 -28.172 -17.099 6.610 1.00 63.53 D000 O ANISOU 5712 O THR B 300 6899 8315 8923 -2051 482 -950 D000 O ATOM 5713 CB THR B 300 -25.905 -17.761 8.527 1.00 63.20 D000 C ANISOU 5713 CB THR B 300 6993 8014 9007 -1990 446 -1138 D000 C ATOM 5714 CG2 THR B 300 -24.584 -18.421 8.870 1.00 63.67 D000 C ANISOU 5714 CG2 THR B 300 7201 7758 9231 -1965 499 -1142 D000 C ATOM 5715 OG1 THR B 300 -26.176 -16.766 9.516 1.00 60.37 D000 O ANISOU 5715 OG1 THR B 300 6483 8061 8396 -1876 288 -1215 D000 O ATOM 5716 N LYS B 301 -27.210 -15.089 6.897 1.00 52.79 D000 N ANISOU 5716 N LYS B 301 5625 7143 7291 -1635 227 -701 D000 N ATOM 5717 CA LYS B 301 -28.431 -14.341 6.629 1.00 56.77 D000 C ANISOU 5717 CA LYS B 301 5981 7957 7633 -1597 189 -685 D000 C ATOM 5718 C LYS B 301 -28.559 -14.040 5.141 1.00 53.34 D000 C ANISOU 5718 C LYS B 301 5660 7378 7228 -1543 225 -463 D000 C ATOM 5719 O LYS B 301 -27.578 -14.049 4.399 1.00 51.81 D000 O ANISOU 5719 O LYS B 301 5655 6915 7117 -1468 236 -290 D000 O ATOM 5720 CB LYS B 301 -28.458 -13.040 7.436 1.00 55.75 D000 C ANISOU 5720 CB LYS B 301 5771 8129 7280 -1372 53 -645 D000 C ATOM 5721 CG LYS B 301 -28.350 -13.257 8.939 1.00 65.13 D000 C ANISOU 5721 CG LYS B 301 6821 9536 8390 -1401 8 -848 D000 C ATOM 5722 CD LYS B 301 -27.684 -12.097 9.662 1.00 82.53 D000 C ANISOU 5722 CD LYS B 301 9056 11858 10443 -1143 -101 -723 D000 C ATOM 5723 CE LYS B 301 -28.692 -11.317 10.503 1.00 90.20 D000 C ANISOU 5723 CE LYS B 301 9788 13314 11170 -1020 -162 -758 D000 C ATOM 5724 NZ LYS B 301 -28.042 -10.279 11.356 1.00 96.16 D000 N ANISOU 5724 NZ LYS B 301 10566 14183 11788 -769 -237 -627 D000 N ATOM 5725 N SER B 302 -29.797 -13.784 4.709 1.00 50.14 D000 N ANISOU 5725 N SER B 302 5118 7195 6737 -1581 245 -479 D000 N ATOM 5726 CA SER B 302 -30.088 -13.534 3.292 1.00 52.55 D000 C ANISOU 5726 CA SER B 302 5498 7417 7052 -1549 291 -296 D000 C ATOM 5727 C SER B 302 -29.878 -12.054 2.966 1.00 52.07 D000 C ANISOU 5727 C SER B 302 5490 7456 6837 -1291 192 -138 D000 C ATOM 5728 O SER B 302 -30.808 -11.293 2.679 1.00 53.50 D000 O ANISOU 5728 O SER B 302 5568 7866 6894 -1212 179 -113 D000 O ATOM 5729 CB SER B 302 -31.506 -13.979 2.950 1.00 64.91 D000 C ANISOU 5729 CB SER B 302 6888 9169 8607 -1721 376 -395 D000 C ATOM 5730 OG SER B 302 -31.712 -15.334 3.299 1.00 87.29 D000 O ANISOU 5730 OG SER B 302 9670 11888 11607 -1987 500 -574 D000 O ATOM 5731 N TRP B 303 -28.612 -11.664 2.997 1.00 45.48 D000 N ANISOU 5731 N TRP B 303 4821 6435 6026 -1166 141 -38 D000 N ATOM 5732 CA TRP B 303 -28.218 -10.315 2.637 1.00 43.57 D000 C ANISOU 5732 CA TRP B 303 4659 6216 5680 -953 83 93 D000 C ATOM 5733 C TRP B 303 -28.528 -10.025 1.174 1.00 43.75 D000 C ANISOU 5733 C TRP B 303 4730 6207 5686 -940 133 212 D000 C ATOM 5734 O TRP B 303 -28.600 -10.928 0.332 1.00 42.52 D000 O ANISOU 5734 O TRP B 303 4603 5940 5612 -1071 204 256 D000 O ATOM 5735 CB TRP B 303 -26.721 -10.120 2.853 1.00 43.81 D000 C ANISOU 5735 CB TRP B 303 4851 6038 5757 -871 39 155 D000 C ATOM 5736 CG TRP B 303 -26.282 -10.300 4.268 1.00 47.49 D000 C ANISOU 5736 CG TRP B 303 5281 6538 6226 -862 -10 49 D000 C ATOM 5737 CD1 TRP B 303 -25.672 -11.393 4.812 1.00 48.15 D000 C ANISOU 5737 CD1 TRP B 303 5389 6482 6424 -981 6 -37 D000 C ATOM 5738 CD2 TRP B 303 -26.411 -9.341 5.319 1.00 42.46 D000 C ANISOU 5738 CD2 TRP B 303 4571 6096 5467 -713 -69 28 D000 C ATOM 5739 CE2 TRP B 303 -25.853 -9.917 6.484 1.00 43.54 D000 C ANISOU 5739 CE2 TRP B 303 4682 6234 5628 -759 -101 -80 D000 C ATOM 5740 CE3 TRP B 303 -26.942 -8.053 5.390 1.00 42.06 D000 C ANISOU 5740 CE3 TRP B 303 4475 6214 5292 -530 -78 103 D000 C ATOM 5741 NE1 TRP B 303 -25.409 -11.170 6.150 1.00 45.95 D000 N ANISOU 5741 NE1 TRP B 303 5049 6322 6086 -929 -52 -134 D000 N ATOM 5742 CZ2 TRP B 303 -25.820 -9.246 7.704 1.00 45.61 D000 C ANISOU 5742 CZ2 TRP B 303 4863 6696 5770 -629 -154 -104 D000 C ATOM 5743 CZ3 TRP B 303 -26.911 -7.390 6.608 1.00 47.92 D000 C ANISOU 5743 CZ3 TRP B 303 5147 7126 5934 -386 -116 102 D000 C ATOM 5744 CH2 TRP B 303 -26.359 -7.988 7.746 1.00 50.74 D000 C ANISOU 5744 CH2 TRP B 303 5468 7516 6294 -437 -160 4 D000 C ATOM 5745 N ASN B 304 -28.655 -8.735 0.861 1.00 42.81 D000 N ANISOU 5745 N ASN B 304 4626 6177 5463 -772 112 272 D000 N ATOM 5746 CA ASN B 304 -28.930 -8.301 -0.512 1.00 42.89 D000 C ANISOU 5746 CA ASN B 304 4673 6191 5433 -748 161 357 D000 C ATOM 5747 C ASN B 304 -27.606 -8.152 -1.267 1.00 40.75 D000 C ANISOU 5747 C ASN B 304 4566 5727 5188 -719 154 444 D000 C ATOM 5748 O ASN B 304 -27.159 -7.057 -1.610 1.00 42.98 D000 O ANISOU 5748 O ASN B 304 4916 6000 5416 -602 150 463 D000 O ATOM 5749 CB ASN B 304 -29.722 -7.000 -0.515 1.00 46.43 D000 C ANISOU 5749 CB ASN B 304 5053 6817 5772 -585 172 356 D000 C ATOM 5750 CG ASN B 304 -31.142 -7.165 0.020 1.00 50.45 D000 C ANISOU 5750 CG ASN B 304 5359 7589 6219 -604 182 286 D000 C ATOM 5751 ND2 ASN B 304 -31.639 -6.122 0.662 1.00 51.25 D000 N ANISOU 5751 ND2 ASN B 304 5383 7858 6230 -416 175 292 D000 N ATOM 5752 OD1 ASN B 304 -31.781 -8.213 -0.141 1.00 51.16 D000 O ANISOU 5752 OD1 ASN B 304 5356 7740 6343 -782 210 232 D000 O ATOM 5753 N PHE B 305 -26.982 -9.301 -1.535 1.00 41.05 D000 N ANISOU 5753 N PHE B 305 4661 5622 5316 -831 169 490 D000 N ATOM 5754 CA PHE B 305 -25.678 -9.313 -2.178 1.00 41.50 D000 C ANISOU 5754 CA PHE B 305 4841 5546 5380 -798 155 581 D000 C ATOM 5755 C PHE B 305 -25.775 -8.839 -3.620 1.00 43.47 D000 C ANISOU 5755 C PHE B 305 5102 5882 5531 -773 192 656 D000 C ATOM 5756 O PHE B 305 -26.739 -9.158 -4.331 1.00 39.69 D000 O ANISOU 5756 O PHE B 305 4556 5498 5028 -833 251 690 D000 O ATOM 5757 CB PHE B 305 -25.081 -10.723 -2.201 1.00 44.91 D000 C ANISOU 5757 CB PHE B 305 5318 5815 5932 -893 189 649 D000 C ATOM 5758 CG PHE B 305 -24.777 -11.306 -0.848 1.00 45.76 D000 C ANISOU 5758 CG PHE B 305 5424 5819 6145 -932 166 553 D000 C ATOM 5759 CD1 PHE B 305 -23.790 -10.764 -0.036 1.00 45.19 D000 C ANISOU 5759 CD1 PHE B 305 5407 5702 6061 -843 90 514 D000 C ATOM 5760 CD2 PHE B 305 -25.462 -12.429 -0.410 1.00 49.10 D000 C ANISOU 5760 CD2 PHE B 305 5782 6194 6680 -1076 236 487 D000 C ATOM 5761 CE1 PHE B 305 -23.510 -11.332 1.205 1.00 44.95 D000 C ANISOU 5761 CE1 PHE B 305 5364 5603 6113 -881 73 416 D000 C ATOM 5762 CE2 PHE B 305 -25.184 -12.985 0.828 1.00 49.62 D000 C ANISOU 5762 CE2 PHE B 305 5833 6186 6835 -1129 225 362 D000 C ATOM 5763 CZ PHE B 305 -24.211 -12.445 1.622 1.00 45.27 D000 C ANISOU 5763 CZ PHE B 305 5334 5612 6255 -1024 138 332 D000 C ATOM 5764 N ILE B 306 -24.740 -8.136 -4.068 1.00 39.69 D000 N ANISOU 5764 N ILE B 306 4698 5389 4993 -701 164 671 D000 N ATOM 5765 CA ILE B 306 -24.538 -7.829 -5.478 1.00 39.05 D000 C ANISOU 5765 CA ILE B 306 4621 5417 4801 -694 196 726 D000 C ATOM 5766 C ILE B 306 -23.124 -8.256 -5.864 1.00 41.33 D000 C ANISOU 5766 C ILE B 306 4969 5663 5073 -685 166 809 D000 C ATOM 5767 O ILE B 306 -22.158 -7.961 -5.146 1.00 42.42 D000 O ANISOU 5767 O ILE B 306 5161 5712 5244 -647 115 759 D000 O ATOM 5768 CB ILE B 306 -24.778 -6.334 -5.774 1.00 39.26 D000 C ANISOU 5768 CB ILE B 306 4643 5534 4739 -623 215 612 D000 C ATOM 5769 CG1 ILE B 306 -24.540 -6.043 -7.254 1.00 40.94 D000 C ANISOU 5769 CG1 ILE B 306 4839 5898 4818 -638 251 628 D000 C ATOM 5770 CG2 ILE B 306 -23.918 -5.438 -4.864 1.00 43.13 D000 C ANISOU 5770 CG2 ILE B 306 5204 5915 5268 -554 184 522 D000 C ATOM 5771 CD1 ILE B 306 -25.078 -4.723 -7.701 1.00 48.43 D000 C ANISOU 5771 CD1 ILE B 306 5769 6936 5698 -593 311 496 D000 C ATOM 5772 N TRP B 307 -23.021 -8.998 -6.963 1.00 42.50 D000 N ANISOU 5772 N TRP B 307 5093 5891 5164 -707 205 952 D000 N ATOM 5773 CA TRP B 307 -21.747 -9.440 -7.531 1.00 44.08 D000 C ANISOU 5773 CA TRP B 307 5315 6125 5307 -668 186 1070 D000 C ATOM 5774 C TRP B 307 -21.169 -8.325 -8.396 1.00 49.95 D000 C ANISOU 5774 C TRP B 307 6030 7079 5870 -639 163 983 D000 C ATOM 5775 O TRP B 307 -21.833 -7.862 -9.326 1.00 49.79 D000 O ANISOU 5775 O TRP B 307 5953 7230 5733 -656 203 955 D000 O ATOM 5776 CB TRP B 307 -21.994 -10.704 -8.357 1.00 49.79 D000 C ANISOU 5776 CB TRP B 307 6012 6869 6037 -682 264 1294 D000 C ATOM 5777 CG TRP B 307 -20.775 -11.414 -8.857 1.00 57.07 D000 C ANISOU 5777 CG TRP B 307 6943 7823 6915 -605 266 1478 D000 C ATOM 5778 CD1 TRP B 307 -19.477 -11.050 -8.676 1.00 63.64 D000 C ANISOU 5778 CD1 TRP B 307 7789 8702 7689 -540 191 1444 D000 C ATOM 5779 CD2 TRP B 307 -20.751 -12.617 -9.638 1.00 72.27 D000 C ANISOU 5779 CD2 TRP B 307 8854 9756 8848 -570 363 1747 D000 C ATOM 5780 CE2 TRP B 307 -19.400 -12.925 -9.890 1.00 77.93 D000 C ANISOU 5780 CE2 TRP B 307 9569 10543 9499 -456 334 1879 D000 C ATOM 5781 CE3 TRP B 307 -21.743 -13.465 -10.145 1.00 78.34 D000 C ANISOU 5781 CE3 TRP B 307 9606 10480 9679 -619 487 1899 D000 C ATOM 5782 NE1 TRP B 307 -18.640 -11.954 -9.293 1.00 69.03 D000 N ANISOU 5782 NE1 TRP B 307 8452 9449 8326 -452 221 1675 D000 N ATOM 5783 CZ2 TRP B 307 -19.014 -14.046 -10.626 1.00 82.10 D000 C ANISOU 5783 CZ2 TRP B 307 10082 11097 10016 -359 429 2186 D000 C ATOM 5784 CZ3 TRP B 307 -21.358 -14.576 -10.877 1.00 79.90 D000 C ANISOU 5784 CZ3 TRP B 307 9803 10672 9884 -542 595 2199 D000 C ATOM 5785 CH2 TRP B 307 -20.006 -14.856 -11.110 1.00 80.08 D000 C ANISOU 5785 CH2 TRP B 307 9827 10765 9836 -398 567 2353 D000 C ATOM 5786 N LEU B 308 -19.932 -7.901 -8.111 1.00 48.77 D000 N ANISOU 5786 N LEU B 308 5908 6929 5694 -609 108 919 D000 N ATOM 5787 CA LEU B 308 -19.299 -6.795 -8.827 1.00 56.70 D000 C ANISOU 5787 CA LEU B 308 6874 8127 6540 -617 101 778 D000 C ATOM 5788 C LEU B 308 -18.298 -7.303 -9.862 1.00 68.13 D000 C ANISOU 5788 C LEU B 308 8247 9821 7819 -588 80 899 D000 C ATOM 5789 O LEU B 308 -17.453 -8.151 -9.557 1.00 65.02 D000 O ANISOU 5789 O LEU B 308 7863 9377 7462 -534 46 1041 D000 O ATOM 5790 CB LEU B 308 -18.590 -5.848 -7.853 1.00 49.43 D000 C ANISOU 5790 CB LEU B 308 6014 7075 5691 -621 74 601 D000 C ATOM 5791 CG LEU B 308 -19.442 -5.203 -6.760 1.00 50.09 D000 C ANISOU 5791 CG LEU B 308 6160 6955 5916 -611 101 501 D000 C ATOM 5792 CD1 LEU B 308 -18.552 -4.450 -5.790 1.00 62.06 D000 C ANISOU 5792 CD1 LEU B 308 7738 8339 7502 -600 88 386 D000 C ATOM 5793 CD2 LEU B 308 -20.474 -4.277 -7.359 1.00 56.13 D000 C ANISOU 5793 CD2 LEU B 308 6899 7798 6632 -620 178 395 D000 C ATOM 5794 N THR B 309 -18.375 -6.753 -11.072 1.00 86.05 D000 N ANISOU 5794 N THR B 309 10425 12378 9890 -613 106 837 D000 N ATOM 5795 CA THR B 309 -17.509 -7.156 -12.184 1.00101.59 D000 C ANISOU 5795 CA THR B 309 12279 14682 11638 -574 88 952 D000 C ATOM 5796 C THR B 309 -16.257 -6.284 -12.282 1.00101.67 D000 C ANISOU 5796 C THR B 309 12233 14871 11526 -612 46 748 D000 C ATOM 5797 O THR B 309 -15.918 -5.771 -13.350 1.00103.00 D000 O ANISOU 5797 O THR B 309 12276 15395 11465 -651 54 642 D000 O ATOM 5798 CB THR B 309 -18.296 -7.111 -13.490 1.00 78.16 D000 C ANISOU 5798 CB THR B 309 9215 11995 8488 -587 143 994 D000 C ATOM 5799 N ASP B 310 -15.548 -6.124 -11.165 0.00 82.60 D000 N ANISOU 5799 N ASP B 310 9895 12233 9256 -615 7 677 D000 N ATOM 5800 CA ASP B 310 -14.359 -5.278 -11.106 0.00 77.16 D000 C ANISOU 5800 CA ASP B 310 9158 11673 8486 -675 -18 464 D000 C ATOM 5801 C ASP B 310 -13.241 -5.978 -10.346 0.00 70.53 D000 C ANISOU 5801 C ASP B 310 8334 10754 7709 -605 -86 586 D000 C ATOM 5802 O ASP B 310 -12.565 -5.377 -9.504 0.00 67.66 D000 O ANISOU 5802 O ASP B 310 8016 10257 7434 -653 -98 428 D000 O ATOM 5803 CB ASP B 310 -14.677 -3.928 -10.462 0.00 76.68 D000 C ANISOU 5803 CB ASP B 310 9184 11397 8553 -775 45 177 D000 C ATOM 5804 N SER B 311 -13.026 -7.262 -10.638 0.00 68.62 D000 N ANISOU 5804 N SER B 311 8054 10587 7430 -483 -112 879 D000 N ATOM 5805 CA SER B 311 -11.981 -8.045 -9.978 0.00 63.72 D000 C ANISOU 5805 CA SER B 311 7443 9893 6874 -388 -159 1019 D000 C ATOM 5806 C SER B 311 -10.681 -7.886 -10.762 0.00 60.61 D000 C ANISOU 5806 C SER B 311 6876 9927 6225 -360 -205 999 D000 C ATOM 5807 O SER B 311 -10.298 -8.724 -11.581 0.00 59.05 D000 O ANISOU 5807 O SER B 311 6566 10004 5867 -231 -212 1242 D000 O ATOM 5808 CB SER B 311 -12.398 -9.506 -9.864 0.00 64.14 D000 C ANISOU 5808 CB SER B 311 7549 9773 7047 -261 -126 1342 D000 C ATOM 5809 N GLU B 312 -9.994 -6.778 -10.498 0.00 60.26 D000 N ANISOU 5809 N GLU B 312 6800 9955 6141 -483 -223 705 D000 N ATOM 5810 CA GLU B 312 -8.701 -6.469 -11.097 0.00 59.01 D000 C ANISOU 5810 CA GLU B 312 6457 10221 5744 -501 -266 607 D000 C ATOM 5811 C GLU B 312 -7.627 -6.370 -10.020 0.00 59.24 D000 C ANISOU 5811 C GLU B 312 6516 10108 5883 -509 -304 532 D000 C ATOM 5812 O GLU B 312 -6.796 -5.458 -10.022 0.00 59.06 D000 O ANISOU 5812 O GLU B 312 6408 10259 5773 -638 -306 267 D000 O ATOM 5813 CB GLU B 312 -8.772 -5.178 -11.908 0.00 57.48 D000 C ANISOU 5813 CB GLU B 312 6161 10299 5378 -683 -225 271 D000 C ATOM 5814 N LEU B 313 -7.635 -7.318 -9.088 0.00 60.68 D000 N ANISOU 5814 N LEU B 313 6814 9976 6263 -383 -321 748 D000 N ATOM 5815 CA LEU B 313 -6.727 -7.279 -7.955 0.00 65.73 D000 C ANISOU 5815 CA LEU B 313 7499 10448 7029 -383 -351 685 D000 C ATOM 5816 C LEU B 313 -5.281 -7.471 -8.410 0.00 65.81 D000 C ANISOU 5816 C LEU B 313 7313 10868 6823 -323 -406 710 D000 C ATOM 5817 O LEU B 313 -4.998 -7.893 -9.536 0.00 62.24 D000 O ANISOU 5817 O LEU B 313 6694 10822 6132 -232 -425 848 D000 O ATOM 5818 CB LEU B 313 -7.106 -8.354 -6.938 0.00 69.36 D000 C ANISOU 5818 CB LEU B 313 8108 10515 7732 -260 -346 901 D000 C ATOM 5819 N LYS B 314 -4.357 -7.151 -7.506 0.00 68.61 D000 N ANISOU 5819 N LYS B 314 7674 11143 7251 -366 -428 581 D000 N ATOM 5820 CA LYS B 314 -2.931 -7.316 -7.743 0.00 67.25 D000 C ANISOU 5820 CA LYS B 314 7310 11349 6894 -313 -481 586 D000 C ATOM 5821 C LYS B 314 -2.282 -7.858 -6.479 0.00 68.95 D000 C ANISOU 5821 C LYS B 314 7608 11295 7295 -223 -501 669 D000 C ATOM 5822 O LYS B 314 -2.705 -7.546 -5.362 0.00 71.98 D000 O ANISOU 5822 O LYS B 314 8168 11268 7912 -297 -473 573 D000 O ATOM 5823 CB LYS B 314 -2.268 -5.994 -8.151 0.00 64.18 D000 C ANISOU 5823 CB LYS B 314 6778 11273 6336 -537 -470 221 D000 C ATOM 5824 N GLY B 315 -1.247 -8.676 -6.665 0.00 65.17 D000 N ANISOU 5824 N GLY B 315 6987 11077 6697 -49 -543 854 D000 N ATOM 5825 CA GLY B 315 -0.560 -9.305 -5.559 0.00 64.29 D000 C ANISOU 5825 CA GLY B 315 6933 10750 6744 62 -555 946 D000 C ATOM 5826 C GLY B 315 -1.210 -10.564 -5.032 0.00 63.83 D000 C ANISOU 5826 C GLY B 315 7038 10302 6912 243 -513 1227 D000 C ATOM 5827 O GLY B 315 -0.609 -11.245 -4.190 0.00 61.89 D000 O ANISOU 5827 O GLY B 315 6826 9895 6793 361 -508 1320 D000 O ATOM 5828 N LYS B 316 -2.410 -10.899 -5.492 0.00 64.77 D000 N ANISOU 5828 N LYS B 316 7252 10265 7092 256 -468 1346 D000 N ATOM 5829 CA LYS B 316 -3.099 -12.097 -5.035 0.00 62.50 D000 C ANISOU 5829 CA LYS B 316 7115 9599 7035 390 -399 1580 D000 C ATOM 5830 C LYS B 316 -2.450 -13.329 -5.665 0.00 57.95 D000 C ANISOU 5830 C LYS B 316 6436 9198 6384 657 -360 1926 D000 C ATOM 5831 O LYS B 316 -1.414 -13.254 -6.332 0.00 57.17 D000 O ANISOU 5831 O LYS B 316 6140 9540 6043 756 -405 1987 D000 O ATOM 5832 CB LYS B 316 -4.585 -12.013 -5.372 0.00 65.20 D000 C ANISOU 5832 CB LYS B 316 7569 9751 7454 300 -352 1583 D000 C ATOM 5833 N SER B 317 -3.070 -14.489 -5.454 0.00 56.71 D000 N ANISOU 5833 N SER B 317 6406 8702 6439 782 -256 2159 D000 N ATOM 5834 CA SER B 317 -2.612 -15.746 -6.031 0.00 55.26 D000 C ANISOU 5834 CA SER B 317 6162 8595 6241 1061 -166 2535 D000 C ATOM 5835 C SER B 317 -3.454 -16.189 -7.219 0.00 55.48 D000 C ANISOU 5835 C SER B 317 6174 8719 6189 1132 -89 2783 D000 C ATOM 5836 O SER B 317 -2.906 -16.686 -8.208 0.00 55.89 D000 O ANISOU 5836 O SER B 317 6075 9119 6043 1348 -59 3072 D000 O ATOM 5837 CB SER B 317 -2.620 -16.848 -4.967 0.00 53.63 D000 C ANISOU 5837 CB SER B 317 6111 7907 6360 1163 -54 2635 D000 C ATOM 5838 N GLU B 318 -4.771 -16.018 -7.149 0.00 57.01 D000 N ANISOU 5838 N GLU B 318 6505 8642 6516 964 -51 2689 D000 N ATOM 5839 CA GLU B 318 -5.656 -16.420 -8.235 0.00 58.60 D000 C ANISOU 5839 CA GLU B 318 6698 8915 6654 1009 33 2912 D000 C ATOM 5840 C GLU B 318 -6.875 -15.498 -8.274 0.00 61.33 D000 C ANISOU 5840 C GLU B 318 7113 9185 7006 754 -8 2653 D000 C ATOM 5841 O GLU B 318 -8.020 -15.944 -8.364 0.00 62.41 D000 O ANISOU 5841 O GLU B 318 7355 9067 7291 705 87 2730 D000 O ATOM 5842 CB GLU B 318 -6.069 -17.884 -8.083 0.00 57.89 D000 C ANISOU 5842 CB GLU B 318 6732 8431 6831 1166 225 3226 D000 C ATOM 5843 N SER B 319 -6.634 -14.189 -8.205 0.00 62.69 D000 N ANISOU 5843 N SER B 319 7221 9575 7025 590 -134 2340 D000 N ATOM 5844 CA SER B 319 -7.709 -13.206 -8.291 0.00 65.65 D000 C ANISOU 5844 CA SER B 319 7648 9904 7392 375 -161 2096 D000 C ATOM 5845 C SER B 319 -8.703 -13.381 -7.149 0.00 68.65 D000 C ANISOU 5845 C SER B 319 8217 9791 8076 267 -117 1990 D000 C ATOM 5846 O SER B 319 -8.369 -13.969 -6.115 0.00 67.26 D000 O ANISOU 5846 O SER B 319 8124 9334 8098 308 -94 2001 D000 O ATOM 5847 CB SER B 319 -8.421 -13.318 -9.640 1.00 76.01 D000 C ANISOU 5847 CB SER B 319 8884 11467 8530 403 -116 2255 D000 C ATOM 5848 N ILE B 320 -9.924 -12.872 -7.322 1.00 82.83 D000 N ANISOU 5848 N ILE B 320 10066 11511 9896 130 -101 1876 D000 N ATOM 5849 CA ILE B 320 -10.942 -12.948 -6.278 1.00 73.37 D000 C ANISOU 5849 CA ILE B 320 9009 9927 8942 21 -68 1757 D000 C ATOM 5850 C ILE B 320 -12.270 -12.401 -6.788 1.00 67.23 D000 C ANISOU 5850 C ILE B 320 8243 9171 8130 -95 -46 1677 D000 C ATOM 5851 O ILE B 320 -12.320 -11.315 -7.376 1.00 66.45 D000 O ANISOU 5851 O ILE B 320 8081 9310 7858 -163 -94 1530 D000 O ATOM 5852 CB ILE B 320 -10.490 -12.184 -5.017 1.00 64.03 D000 C ANISOU 5852 CB ILE B 320 7875 8614 7838 -58 -141 1505 D000 C ATOM 5853 N ASP B 321 -13.352 -13.154 -6.578 1.00 64.58 D000 N ANISOU 5853 N ASP B 321 7980 8593 7963 -126 41 1758 D000 N ATOM 5854 CA ASP B 321 -14.687 -12.623 -6.819 1.00 56.26 D000 C ANISOU 5854 CA ASP B 321 6938 7536 6905 -242 59 1655 D000 C ATOM 5855 C ASP B 321 -15.042 -11.610 -5.738 1.00 53.62 D000 C ANISOU 5855 C ASP B 321 6652 7085 6638 -345 -3 1380 D000 C ATOM 5856 O ASP B 321 -14.820 -11.856 -4.546 1.00 56.02 D000 O ANISOU 5856 O ASP B 321 7015 7179 7092 -353 -17 1309 D000 O ATOM 5857 CB ASP B 321 -15.731 -13.739 -6.845 1.00 64.95 D000 C ANISOU 5857 CB ASP B 321 8083 8423 8170 -266 181 1802 D000 C ATOM 5858 CG ASP B 321 -15.669 -14.560 -8.108 1.00 77.95 D000 C ANISOU 5858 CG ASP B 321 9680 10207 9731 -165 274 2101 D000 C ATOM 5859 OD1 ASP B 321 -15.877 -13.981 -9.195 1.00 80.36 D000 O ANISOU 5859 OD1 ASP B 321 9903 10811 9822 -162 252 2126 D000 O ATOM 5860 OD2 ASP B 321 -15.427 -15.781 -8.014 1.00 88.37 D000 O ANISOU 5860 OD2 ASP B 321 11042 11336 11199 -83 386 2314 D000 O ATOM 5861 N ILE B 322 -15.599 -10.477 -6.155 1.00 52.36 D000 N ANISOU 5861 N ILE B 322 6463 7065 6365 -410 -25 1234 D000 N ATOM 5862 CA ILE B 322 -15.856 -9.338 -5.282 1.00 47.05 D000 C ANISOU 5862 CA ILE B 322 5829 6315 5733 -472 -61 1005 D000 C ATOM 5863 C ILE B 322 -17.363 -9.134 -5.147 1.00 42.51 D000 C ANISOU 5863 C ILE B 322 5266 5671 5215 -528 -20 952 D000 C ATOM 5864 O ILE B 322 -18.092 -9.203 -6.140 1.00 44.54 D000 O ANISOU 5864 O ILE B 322 5479 6050 5394 -545 23 1013 D000 O ATOM 5865 CB ILE B 322 -15.198 -8.066 -5.849 1.00 53.23 D000 C ANISOU 5865 CB ILE B 322 6568 7301 6355 -495 -88 857 D000 C ATOM 5866 CG1 ILE B 322 -13.664 -8.156 -5.857 1.00 65.42 D000 C ANISOU 5866 CG1 ILE B 322 8074 8954 7829 -455 -137 870 D000 C ATOM 5867 CG2 ILE B 322 -15.653 -6.875 -5.057 1.00 56.27 D000 C ANISOU 5867 CG2 ILE B 322 7005 7570 6804 -543 -77 659 D000 C ATOM 5868 CD1 ILE B 322 -13.068 -9.033 -4.800 1.00 65.61 D000 C ANISOU 5868 CD1 ILE B 322 8149 8783 7997 -396 -160 953 D000 C ATOM 5869 N TYR B 323 -17.820 -8.849 -3.927 1.00 39.44 D000 N ANISOU 5869 N TYR B 323 4918 5125 4942 -548 -32 841 D000 N ATOM 5870 CA TYR B 323 -19.238 -8.631 -3.652 1.00 37.68 D000 C ANISOU 5870 CA TYR B 323 4680 4877 4760 -585 2 785 D000 C ATOM 5871 C TYR B 323 -19.445 -7.363 -2.835 1.00 40.98 D000 C ANISOU 5871 C TYR B 323 5117 5274 5181 -561 -12 634 D000 C ATOM 5872 O TYR B 323 -18.533 -6.878 -2.163 1.00 41.32 D000 O ANISOU 5872 O TYR B 323 5200 5260 5240 -532 -42 576 D000 O ATOM 5873 CB TYR B 323 -19.848 -9.801 -2.876 1.00 41.62 D000 C ANISOU 5873 CB TYR B 323 5178 5235 5403 -627 25 824 D000 C ATOM 5874 CG TYR B 323 -20.014 -11.040 -3.703 1.00 41.01 D000 C ANISOU 5874 CG TYR B 323 5088 5133 5361 -656 94 988 D000 C ATOM 5875 CD1 TYR B 323 -18.970 -11.928 -3.876 1.00 45.19 D000 C ANISOU 5875 CD1 TYR B 323 5650 5587 5934 -610 110 1122 D000 C ATOM 5876 CD2 TYR B 323 -21.227 -11.327 -4.307 1.00 46.09 D000 C ANISOU 5876 CD2 TYR B 323 5684 5827 6001 -718 162 1026 D000 C ATOM 5877 CE1 TYR B 323 -19.125 -13.068 -4.644 1.00 51.75 D000 C ANISOU 5877 CE1 TYR B 323 6477 6374 6813 -610 207 1314 D000 C ATOM 5878 CE2 TYR B 323 -21.397 -12.463 -5.056 1.00 46.77 D000 C ANISOU 5878 CE2 TYR B 323 5766 5871 6135 -744 254 1199 D000 C ATOM 5879 CZ TYR B 323 -20.344 -13.332 -5.223 1.00 55.43 D000 C ANISOU 5879 CZ TYR B 323 6906 6871 7284 -683 285 1354 D000 C ATOM 5880 OH TYR B 323 -20.518 -14.463 -5.989 1.00 57.52 D000 O ANISOU 5880 OH TYR B 323 7172 7072 7609 -684 410 1566 D000 O ATOM 5881 N SER B 324 -20.670 -6.842 -2.868 1.00 40.12 D000 N ANISOU 5881 N SER B 324 4974 5212 5058 -560 25 588 D000 N ATOM 5882 CA SER B 324 -21.077 -5.792 -1.943 1.00 37.64 D000 C ANISOU 5882 CA SER B 324 4669 4868 4766 -501 36 493 D000 C ATOM 5883 C SER B 324 -22.524 -6.066 -1.529 1.00 39.36 D000 C ANISOU 5883 C SER B 324 4813 5139 5004 -500 53 494 D000 C ATOM 5884 O SER B 324 -23.065 -7.153 -1.766 1.00 38.92 D000 O ANISOU 5884 O SER B 324 4710 5103 4976 -576 56 543 D000 O ATOM 5885 CB SER B 324 -20.893 -4.399 -2.562 1.00 38.76 D000 C ANISOU 5885 CB SER B 324 4838 5045 4844 -466 95 411 D000 C ATOM 5886 OG SER B 324 -21.193 -3.370 -1.632 1.00 40.32 D000 O ANISOU 5886 OG SER B 324 5060 5175 5085 -380 138 359 D000 O ATOM 5887 N ILE B 325 -23.122 -5.092 -0.846 1.00 38.79 D000 N ANISOU 5887 N ILE B 325 4722 5095 4924 -412 79 445 D000 N ATOM 5888 CA ILE B 325 -24.536 -5.095 -0.489 1.00 40.09 D000 C ANISOU 5888 CA ILE B 325 4784 5378 5070 -383 98 438 D000 C ATOM 5889 C ILE B 325 -25.208 -3.980 -1.280 1.00 47.07 D000 C ANISOU 5889 C ILE B 325 5658 6330 5897 -307 178 423 D000 C ATOM 5890 O ILE B 325 -24.718 -2.845 -1.291 1.00 45.05 D000 O ANISOU 5890 O ILE B 325 5473 6000 5645 -224 233 393 D000 O ATOM 5891 CB ILE B 325 -24.736 -4.873 1.022 1.00 42.52 D000 C ANISOU 5891 CB ILE B 325 5049 5717 5390 -298 71 419 D000 C ATOM 5892 CG1 ILE B 325 -24.121 -6.001 1.849 1.00 49.98 D000 C ANISOU 5892 CG1 ILE B 325 5992 6605 6391 -384 4 398 D000 C ATOM 5893 CG2 ILE B 325 -26.220 -4.722 1.361 1.00 46.14 D000 C ANISOU 5893 CG2 ILE B 325 5368 6371 5793 -243 93 411 D000 C ATOM 5894 CD1 ILE B 325 -24.634 -7.379 1.519 1.00 50.88 D000 C ANISOU 5894 CD1 ILE B 325 6046 6737 6549 -533 2 384 D000 C ATOM 5895 N ASP B 326 -26.344 -4.278 -1.899 1.00 44.71 D000 N ANISOU 5895 N ASP B 326 5269 6162 5557 -339 205 432 D000 N ATOM 5896 CA AASP B 326 -27.092 -3.291 -2.676 0.68 49.88 D000 C ANISOU 5896 CA AASP B 326 5900 6895 6156 -264 291 408 D000 C ATOM 5897 CA BASP B 326 -27.089 -3.289 -2.673 0.32 50.06 D000 C ANISOU 5897 CA BASP B 326 5924 6918 6180 -263 291 408 D000 C ATOM 5898 C ASP B 326 -28.225 -2.762 -1.804 1.00 57.49 D000 C ANISOU 5898 C ASP B 326 6766 7974 7104 -129 320 416 D000 C ATOM 5899 O ASP B 326 -29.275 -3.396 -1.687 1.00 61.88 D000 O ANISOU 5899 O ASP B 326 7192 8693 7626 -167 301 422 D000 O ATOM 5900 CB AASP B 326 -27.620 -3.902 -3.970 0.68 46.95 D000 C ANISOU 5900 CB AASP B 326 5479 6630 5730 -369 310 425 D000 C ATOM 5901 CB BASP B 326 -27.610 -3.893 -3.973 0.32 47.11 D000 C ANISOU 5901 CB BASP B 326 5500 6649 5750 -369 310 425 D000 C ATOM 5902 CG AASP B 326 -28.356 -2.895 -4.833 0.68 52.89 D000 C ANISOU 5902 CG AASP B 326 6203 7476 6419 -297 405 379 D000 C ATOM 5903 CG BASP B 326 -28.282 -2.866 -4.862 0.32 52.99 D000 C ANISOU 5903 CG BASP B 326 6222 7481 6431 -298 405 377 D000 C ATOM 5904 OD1AASP B 326 -28.311 -1.690 -4.517 0.68 52.35 D000 O ANISOU 5904 OD1AASP B 326 6176 7344 6371 -167 473 331 D000 O ATOM 5905 OD1BASP B 326 -27.643 -1.838 -5.175 0.32 55.81 D000 O ANISOU 5905 OD1BASP B 326 6661 7754 6790 -244 465 310 D000 O ATOM 5906 OD2AASP B 326 -28.975 -3.309 -5.834 0.68 46.96 D000 O ANISOU 5906 OD2AASP B 326 5388 6849 5604 -367 429 395 D000 O ATOM 5907 OD2BASP B 326 -29.449 -3.087 -5.248 0.32 50.59 D000 O ANISOU 5907 OD2BASP B 326 5813 7328 6082 -306 435 390 D000 O ATOM 5908 N ASN B 327 -28.003 -1.602 -1.190 1.00 72.17 D000 N ANISOU 5908 N ASN B 327 8675 9760 8986 32 379 422 D000 N ATOM 5909 CA AASN B 327 -29.004 -0.903 -0.395 0.55 82.33 D000 C ANISOU 5909 CA AASN B 327 9869 11171 10243 221 430 470 D000 C ATOM 5910 CA BASN B 327 -29.043 -0.913 -0.432 0.45 82.29 D000 C ANISOU 5910 CA BASN B 327 9860 11171 10236 219 431 469 D000 C ATOM 5911 C ASN B 327 -28.948 0.576 -0.770 1.00 95.85 D000 C ANISOU 5911 C ASN B 327 11667 12756 11994 380 584 470 D000 C ATOM 5912 O ASN B 327 -28.224 0.979 -1.687 1.00100.16 D000 O ANISOU 5912 O ASN B 327 12325 13152 12579 305 642 394 D000 O ATOM 5913 CB AASN B 327 -28.777 -1.131 1.108 0.55 79.08 D000 C ANISOU 5913 CB AASN B 327 9417 10802 9829 287 364 517 D000 C ATOM 5914 CB BASN B 327 -28.915 -1.198 1.074 0.45 79.14 D000 C ANISOU 5914 CB BASN B 327 9408 10834 9828 282 361 515 D000 C ATOM 5915 CG AASN B 327 -27.561 -0.386 1.653 0.55 72.67 D000 C ANISOU 5915 CG AASN B 327 8751 9774 9086 360 402 544 D000 C ATOM 5916 CG BASN B 327 -29.490 -2.563 1.473 0.45 67.04 D000 C ANISOU 5916 CG BASN B 327 7732 9490 8252 138 254 476 D000 C ATOM 5917 ND2AASN B 327 -27.257 -0.616 2.924 0.55 69.03 D000 N ANISOU 5917 ND2AASN B 327 8259 9359 8611 410 343 586 D000 N ATOM 5918 ND2BASN B 327 -29.086 -3.059 2.644 0.45 52.31 D000 N ANISOU 5918 ND2BASN B 327 5835 7657 6383 123 180 466 D000 N ATOM 5919 OD1AASN B 327 -26.909 0.385 0.949 0.55 79.18 D000 O ANISOU 5919 OD1AASN B 327 9703 10411 9971 360 491 511 D000 O ATOM 5920 OD1BASN B 327 -30.299 -3.148 0.751 0.45 58.92 D000 O ANISOU 5920 OD1BASN B 327 6617 8576 7195 34 254 442 D000 O ATOM 5921 N GLU B 328 -29.692 1.402 -0.032 1.00101.99 D000 N ANISOU 5921 N GLU B 328 12386 13604 12762 606 667 553 D000 N ATOM 5922 CA GLU B 328 -29.729 2.829 -0.338 1.00112.82 D000 C ANISOU 5922 CA GLU B 328 13845 14817 14204 779 858 564 D000 C ATOM 5923 C GLU B 328 -28.353 3.479 -0.222 1.00124.95 D000 C ANISOU 5923 C GLU B 328 15564 16059 15854 749 932 526 D000 C ATOM 5924 O GLU B 328 -28.065 4.449 -0.934 1.00125.92 D000 O ANISOU 5924 O GLU B 328 15791 15995 16058 764 1095 445 D000 O ATOM 5925 CB GLU B 328 -30.727 3.532 0.586 1.00112.67 D000 C ANISOU 5925 CB GLU B 328 13722 14932 14154 1068 943 712 D000 C ATOM 5926 CG GLU B 328 -30.357 3.492 2.065 1.00124.33 D000 C ANISOU 5926 CG GLU B 328 15177 16449 15614 1183 894 836 D000 C ATOM 5927 CD GLU B 328 -31.021 2.348 2.809 1.00122.30 D000 C ANISOU 5927 CD GLU B 328 14720 16532 15216 1132 717 852 D000 C ATOM 5928 OE1 GLU B 328 -31.564 1.439 2.146 1.00121.33 D000 O ANISOU 5928 OE1 GLU B 328 14505 16553 15041 955 627 755 D000 O ATOM 5929 OE2 GLU B 328 -30.992 2.356 4.058 1.00109.03 D000 O ANISOU 5929 OE2 GLU B 328 12967 14983 13477 1259 681 952 D000 O ATOM 5930 N MET B 329 -27.494 2.967 0.659 1.00121.91 D000 N ANISOU 5930 N MET B 329 17299 15451 13568 -1288 5199 1036 D000 N ATOM 5931 CA MET B 329 -26.199 3.586 0.907 1.00118.45 D000 C ANISOU 5931 CA MET B 329 16760 14815 13429 -722 4830 1050 D000 C ATOM 5932 C MET B 329 -25.224 3.356 -0.240 1.00133.91 D000 C ANISOU 5932 C MET B 329 18991 16797 15094 -481 4636 1466 D000 C ATOM 5933 O MET B 329 -24.850 4.300 -0.943 1.00139.19 D000 O ANISOU 5933 O MET B 329 19409 17875 15601 -229 4397 1322 D000 O ATOM 5934 CB MET B 329 -25.602 3.049 2.209 1.00107.28 D000 C ANISOU 5934 CB MET B 329 15524 12702 12534 -558 4805 1169 D000 C ATOM 5935 CG MET B 329 -24.741 4.056 2.943 1.00106.12 D000 C ANISOU 5935 CG MET B 329 15046 12447 12827 -51 4483 914 D000 C ATOM 5936 SD MET B 329 -25.670 5.176 4.004 1.00108.85 D000 S ANISOU 5936 SD MET B 329 14812 13067 13480 -125 4524 233 D000 S ATOM 5937 CE MET B 329 -26.641 4.028 4.965 1.00 92.06 D000 C ANISOU 5937 CE MET B 329 12950 10544 11486 -637 4904 295 D000 C ATOM 5938 N THR B 330 -24.808 2.104 -0.437 1.00128.32 D000 N ANISOU 5938 N THR B 330 18800 15649 14306 -560 4737 1988 D000 N ATOM 5939 CA THR B 330 -23.822 1.794 -1.461 1.00120.86 D000 C ANISOU 5939 CA THR B 330 18139 14675 13109 -318 4548 2432 D000 C ATOM 5940 C THR B 330 -24.294 2.154 -2.861 1.00125.76 D000 C ANISOU 5940 C THR B 330 18693 15930 13159 -492 4563 2402 D000 C ATOM 5941 O THR B 330 -23.488 2.118 -3.797 1.00121.60 D000 O ANISOU 5941 O THR B 330 18330 15482 12391 -274 4361 2710 D000 O ATOM 5942 CB THR B 330 -23.471 0.306 -1.410 1.00118.32 D000 C ANISOU 5942 CB THR B 330 18402 13776 12780 -433 4719 2996 D000 C ATOM 5943 CG2 THR B 330 -22.667 -0.012 -0.156 1.00113.53 D000 C ANISOU 5943 CG2 THR B 330 17905 12500 12733 -142 4639 3104 D000 C ATOM 5944 OG1 THR B 330 -24.677 -0.472 -1.419 1.00119.79 D000 O ANISOU 5944 OG1 THR B 330 18774 13994 12747 -987 5111 2998 D000 O ATOM 5945 N ARG B 331 -25.569 2.501 -3.028 1.00134.75 D000 N ANISOU 5945 N ARG B 331 19598 17522 14079 -874 4797 2048 D000 N ATOM 5946 CA ARG B 331 -26.122 2.786 -4.347 1.00141.34 D000 C ANISOU 5946 CA ARG B 331 20394 18951 14357 -1077 4861 2016 D000 C ATOM 5947 C ARG B 331 -25.990 4.267 -4.699 1.00145.25 D000 C ANISOU 5947 C ARG B 331 20417 19970 14803 -807 4608 1598 D000 C ATOM 5948 O ARG B 331 -25.387 4.617 -5.719 1.00145.09 D000 O ANISOU 5948 O ARG B 331 20441 20204 14482 -613 4396 1734 D000 O ATOM 5949 CB ARG B 331 -27.589 2.338 -4.398 1.00126.99 D000 C ANISOU 5949 CB ARG B 331 18587 17353 12310 -1645 5273 1883 D000 C ATOM 5950 CG ARG B 331 -28.236 2.534 -5.755 1.00129.89 D000 C ANISOU 5950 CG ARG B 331 18948 18312 12093 -1889 5389 1871 D000 C ATOM 5951 CD ARG B 331 -29.645 1.942 -5.857 1.00132.00 D000 C ANISOU 5951 CD ARG B 331 19274 18760 12120 -2466 5812 1813 D000 C ATOM 5952 NE ARG B 331 -29.827 0.671 -5.162 1.00132.24 D000 N ANISOU 5952 NE ARG B 331 19673 18248 12323 -2730 6041 2101 D000 N ATOM 5953 CZ ARG B 331 -30.512 0.510 -4.035 1.00130.01 D000 C ANISOU 5953 CZ ARG B 331 19259 17774 12364 -2953 6222 1880 D000 C ATOM 5954 NH1 ARG B 331 -31.060 1.535 -3.402 1.00126.20 D000 N ANISOU 5954 NH1 ARG B 331 18267 17579 12106 -2924 6195 1372 D000 N ATOM 5955 NH2 ARG B 331 -30.662 -0.714 -3.539 1.00131.78 D000 N ANISOU 5955 NH2 ARG B 331 19882 17508 12681 -3221 6440 2181 D000 N ATOM 5956 N LYS B 332 -26.536 5.146 -3.856 0.81147.57 D000 N ANISOU 5956 N LYS B 332 20265 20419 15385 -791 4625 1092 D000 N ATOM 5957 CA LYS B 332 -26.594 6.578 -4.153 0.81140.00 D000 C ANISOU 5957 CA LYS B 332 18843 19982 14367 -584 4441 646 D000 C ATOM 5958 C LYS B 332 -25.313 7.248 -3.663 0.81138.49 D000 C ANISOU 5958 C LYS B 332 18509 19557 14553 -41 4045 607 D000 C ATOM 5959 O LYS B 332 -25.247 7.841 -2.584 0.81134.42 D000 O ANISOU 5959 O LYS B 332 17692 18899 14483 142 3965 286 D000 O ATOM 5960 CB LYS B 332 -27.831 7.204 -3.519 0.81126.57 D000 C ANISOU 5960 CB LYS B 332 16728 18583 12781 -829 4665 132 D000 C ATOM 5961 N SER B 333 -24.275 7.153 -4.492 0.93142.33 D000 N ANISOU 5961 N SER B 333 19215 20014 14850 216 3790 949 D000 N ATOM 5962 CA SER B 333 -23.012 7.829 -4.241 0.93144.35 D000 C ANISOU 5962 CA SER B 333 19335 20119 15394 728 3390 945 D000 C ATOM 5963 C SER B 333 -22.524 8.457 -5.539 0.93146.42 D000 C ANISOU 5963 C SER B 333 19578 20825 15230 879 3152 999 D000 C ATOM 5964 O SER B 333 -22.892 8.030 -6.636 0.93155.00 D000 O ANISOU 5964 O SER B 333 20898 22177 15819 625 3277 1210 D000 O ATOM 5965 CB SER B 333 -21.952 6.864 -3.689 0.93134.12 D000 C ANISOU 5965 CB SER B 333 18387 18150 14423 952 3279 1419 D000 C ATOM 5966 N SER B 334 -21.693 9.488 -5.402 0.79141.89 D000 N ANISOU 5966 N SER B 334 18729 20332 14850 1288 2806 802 D000 N ATOM 5967 CA SER B 334 -20.993 10.063 -6.543 0.79143.59 D000 C ANISOU 5967 CA SER B 334 18955 20889 14715 1485 2516 899 D000 C ATOM 5968 C SER B 334 -19.789 9.232 -6.962 0.79164.18 D000 C ANISOU 5968 C SER B 334 21948 23138 17293 1693 2296 1500 D000 C ATOM 5969 O SER B 334 -19.010 9.676 -7.813 0.79163.46 D000 O ANISOU 5969 O SER B 334 21873 23265 16969 1904 1998 1629 D000 O ATOM 5970 CB SER B 334 -20.541 11.492 -6.228 0.79128.55 D000 C ANISOU 5970 CB SER B 334 16612 19201 13030 1837 2224 461 D000 C ATOM 5971 OG SER B 334 -21.644 12.376 -6.162 0.79109.60 D000 O ANISOU 5971 OG SER B 334 13861 17248 10532 1651 2412 -79 D000 O ATOM 5972 N GLY B 335 -19.624 8.044 -6.389 0.93154.58 D000 N ANISOU 5972 N GLY B 335 21046 21384 16302 1634 2439 1874 D000 N ATOM 5973 CA GLY B 335 -18.447 7.240 -6.643 0.93141.15 D000 C ANISOU 5973 CA GLY B 335 19697 19289 14643 1868 2243 2454 D000 C ATOM 5974 C GLY B 335 -17.214 7.877 -6.030 0.93146.93 D000 C ANISOU 5974 C GLY B 335 20223 19787 15816 2374 1861 2435 D000 C ATOM 5975 O GLY B 335 -17.266 8.907 -5.359 0.93149.35 D000 O ANISOU 5975 O GLY B 335 20132 20204 16412 2541 1755 1971 D000 O ATOM 5976 N GLY B 336 -16.077 7.231 -6.266 0.62138.51 D000 N ANISOU 5976 N GLY B 336 19438 18385 14806 2625 1657 2965 D000 N ATOM 5977 CA GLY B 336 -14.806 7.795 -5.872 0.62135.65 D000 C ANISOU 5977 CA GLY B 336 18903 17831 14807 3112 1268 3021 D000 C ATOM 5978 C GLY B 336 -14.249 8.719 -6.936 0.62145.33 D000 C ANISOU 5978 C GLY B 336 19971 19549 15698 3278 919 2973 D000 C ATOM 5979 O GLY B 336 -14.755 8.789 -8.055 0.62148.15 D000 O ANISOU 5979 O GLY B 336 20420 20355 15517 3027 976 2975 D000 O ATOM 5980 N LEU B 337 -13.192 9.442 -6.565 1.00146.03 D000 N ANISOU 5980 N LEU B 337 19826 19545 16113 3702 555 2926 D000 N ATOM 5981 CA LEU B 337 -12.607 10.455 -7.438 1.00142.33 D000 C ANISOU 5981 CA LEU B 337 19166 19530 15383 3882 192 2826 D000 C ATOM 5982 C LEU B 337 -13.514 11.679 -7.500 1.00135.47 D000 C ANISOU 5982 C LEU B 337 17928 19180 14366 3735 256 2165 D000 C ATOM 5983 O LEU B 337 -13.051 12.810 -7.323 1.00127.22 D000 O ANISOU 5983 O LEU B 337 16550 18313 13476 3995 -17 1846 D000 O ATOM 5984 CB LEU B 337 -12.363 9.894 -8.841 1.00137.00 D000 C ANISOU 5984 CB LEU B 337 18827 19082 14145 3751 117 3283 D000 C ATOM 5985 N GLU B 338 -14.806 11.467 -7.763 0.78139.20 D000 N ANISOU 5985 N GLU B 338 18456 19899 14537 3321 621 1962 D000 N ATOM 5986 CA GLU B 338 -15.765 12.561 -7.654 0.78138.36 D000 C ANISOU 5986 CA GLU B 338 17987 20232 14352 3181 741 1329 D000 C ATOM 5987 C GLU B 338 -15.884 13.034 -6.210 0.78132.98 D000 C ANISOU 5987 C GLU B 338 16984 19279 14264 3347 783 946 D000 C ATOM 5988 O GLU B 338 -16.021 14.236 -5.953 0.78123.45 D000 O ANISOU 5988 O GLU B 338 15398 18347 13160 3472 679 455 D000 O ATOM 5989 CB GLU B 338 -17.127 12.123 -8.189 0.78139.15 D000 C ANISOU 5989 CB GLU B 338 18223 20617 14032 2699 1147 1241 D000 C ATOM 5990 N ILE B 339 -15.828 12.105 -5.254 1.00134.79 D000 N ANISOU 5990 N ILE B 339 17371 18960 14882 3351 939 1163 D000 N ATOM 5991 CA ILE B 339 -15.884 12.492 -3.849 1.00128.12 D000 C ANISOU 5991 CA ILE B 339 16251 17818 14612 3515 971 830 D000 C ATOM 5992 C ILE B 339 -14.637 13.285 -3.471 1.00108.88 D000 C ANISOU 5992 C ILE B 339 13592 15251 12526 4000 563 790 D000 C ATOM 5993 O ILE B 339 -14.719 14.296 -2.765 1.00101.62 D000 O ANISOU 5993 O ILE B 339 12299 14415 11899 4162 487 321 D000 O ATOM 5994 CB ILE B 339 -16.071 11.247 -2.961 1.00125.98 D000 C ANISOU 5994 CB ILE B 339 16253 16966 14646 3394 1234 1109 D000 C ATOM 5995 CG1 ILE B 339 -17.548 10.836 -2.923 1.00131.16 D000 C ANISOU 5995 CG1 ILE B 339 16956 17787 15092 2908 1663 912 D000 C ATOM 5996 CG2 ILE B 339 -15.592 11.509 -1.542 1.00102.38 D000 C ANISOU 5996 CG2 ILE B 339 13067 13530 12302 3695 1150 940 D000 C ATOM 5997 CD1 ILE B 339 -17.803 9.450 -2.346 1.00126.63 D000 C ANISOU 5997 CD1 ILE B 339 16748 16693 14672 2699 1947 1260 D000 C ATOM 5998 N ALA B 340 -13.467 12.858 -3.958 0.79110.11 D000 N ANISOU 5998 N ALA B 340 16369 15999 9467 4027 -849 -2318 D000 N ATOM 5999 CA ALA B 340 -12.224 13.542 -3.610 0.79 92.61 D000 C ANISOU 5999 CA ALA B 340 13682 13929 7576 4062 -788 -2954 D000 C ATOM 6000 C ALA B 340 -12.231 14.990 -4.090 0.79101.08 D000 C ANISOU 6000 C ALA B 340 14433 15161 8813 3946 -789 -3157 D000 C ATOM 6001 O ALA B 340 -11.701 15.878 -3.411 0.79 80.56 D000 O ANISOU 6001 O ALA B 340 11501 12547 6560 3610 -560 -3438 D000 O ATOM 6002 CB ALA B 340 -11.027 12.793 -4.196 0.79 91.32 D000 C ANISOU 6002 CB ALA B 340 13315 13840 7541 4586 -1146 -3405 D000 C ATOM 6003 N ARG B 341 -12.810 15.248 -5.265 0.91 99.52 D000 N ANISOU 6003 N ARG B 341 14293 15060 8462 4129 -1033 -2964 D000 N ATOM 6004 CA ARG B 341 -12.929 16.626 -5.731 0.91 96.10 D000 C ANISOU 6004 CA ARG B 341 13565 14761 8189 4043 -1075 -3165 D000 C ATOM 6005 C ARG B 341 -13.869 17.423 -4.833 0.91 97.43 D000 C ANISOU 6005 C ARG B 341 13863 14786 8371 3565 -810 -2957 D000 C ATOM 6006 O ARG B 341 -13.600 18.589 -4.520 0.91 89.09 D000 O ANISOU 6006 O ARG B 341 12533 13692 7624 3318 -766 -3203 D000 O ATOM 6007 CB ARG B 341 -13.419 16.656 -7.180 0.91 88.30 D000 C ANISOU 6007 CB ARG B 341 12630 13913 7007 4332 -1351 -3011 D000 C ATOM 6008 N ASN B 342 -14.970 16.805 -4.399 0.89 98.28 D000 N ANISOU 6008 N ASN B 342 14360 14715 8265 3365 -674 -2451 D000 N ATOM 6009 CA ASN B 342 -15.924 17.509 -3.550 0.89 95.78 D000 C ANISOU 6009 CA ASN B 342 14209 14200 7983 2958 -530 -2260 D000 C ATOM 6010 C ASN B 342 -15.282 17.938 -2.237 0.89100.11 D000 C ANISOU 6010 C ASN B 342 14715 14512 8811 2536 -309 -2359 D000 C ATOM 6011 O ASN B 342 -15.538 19.043 -1.744 0.89 91.18 D000 O ANISOU 6011 O ASN B 342 13565 13200 7878 2188 -303 -2381 D000 O ATOM 6012 CB ASN B 342 -17.140 16.621 -3.286 0.89 95.24 D000 C ANISOU 6012 CB ASN B 342 14505 13950 7731 2825 -443 -1750 D000 C ATOM 6013 N ILE B 343 -14.437 17.081 -1.661 0.82 87.03 D000 N ANISOU 6013 N ILE B 343 13067 12843 7157 2546 -136 -2442 D000 N ATOM 6014 CA ILE B 343 -13.843 17.382 -0.362 0.82 86.83 D000 C ANISOU 6014 CA ILE B 343 13045 12638 7310 2081 176 -2544 D000 C ATOM 6015 C ILE B 343 -12.926 18.597 -0.454 0.82 83.52 D000 C ANISOU 6015 C ILE B 343 12203 12290 7239 1889 216 -2973 D000 C ATOM 6016 O ILE B 343 -12.944 19.470 0.422 0.82 79.80 D000 O ANISOU 6016 O ILE B 343 11845 11593 6881 1362 392 -2932 D000 O ATOM 6017 CB ILE B 343 -13.101 16.143 0.174 0.82 73.64 D000 C ANISOU 6017 CB ILE B 343 11391 11003 5585 2188 357 -2655 D000 C ATOM 6018 CG1 ILE B 343 -14.110 15.109 0.686 0.82 82.12 D000 C ANISOU 6018 CG1 ILE B 343 12972 11873 6357 2181 368 -2172 D000 C ATOM 6019 CG2 ILE B 343 -12.149 16.521 1.301 0.82 78.82 D000 C ANISOU 6019 CG2 ILE B 343 11892 11617 6441 1729 751 -2960 D000 C ATOM 6020 CD1 ILE B 343 -13.869 13.696 0.206 0.82 86.84 D000 C ANISOU 6020 CD1 ILE B 343 13625 12552 6816 2645 207 -2170 D000 C ATOM 6021 N GLY B 344 -12.122 18.683 -1.515 0.84 81.69 D000 N ANISOU 6021 N GLY B 344 11524 12336 7179 2298 16 -3388 D000 N ATOM 6022 CA GLY B 344 -11.193 19.793 -1.639 0.84 82.53 D000 C ANISOU 6022 CA GLY B 344 11167 12505 7684 2128 38 -3851 D000 C ATOM 6023 C GLY B 344 -11.881 21.133 -1.833 0.84 81.18 D000 C ANISOU 6023 C GLY B 344 11046 12182 7617 1901 -140 -3740 D000 C ATOM 6024 O GLY B 344 -11.440 22.150 -1.290 0.84 88.60 D000 O ANISOU 6024 O GLY B 344 11865 12960 8838 1441 -14 -3900 D000 O ATOM 6025 N HIS B 345 -12.964 21.158 -2.610 1.00 80.41 D000 N ANISOU 6025 N HIS B 345 11122 12125 7305 2199 -438 -3497 D000 N ATOM 6026 CA HIS B 345 -13.673 22.416 -2.833 1.00 86.91 D000 C ANISOU 6026 CA HIS B 345 11947 12804 8272 2052 -676 -3476 D000 C ATOM 6027 C HIS B 345 -14.349 22.900 -1.555 1.00 86.61 D000 C ANISOU 6027 C HIS B 345 12339 12328 8242 1471 -561 -3135 D000 C ATOM 6028 O HIS B 345 -14.346 24.100 -1.257 1.00 84.72 D000 O ANISOU 6028 O HIS B 345 12096 11832 8261 1134 -691 -3217 D000 O ATOM 6029 CB HIS B 345 -14.702 22.247 -3.950 1.00 85.30 D000 C ANISOU 6029 CB HIS B 345 11788 12801 7822 2496 -961 -3373 D000 C ATOM 6030 N TYR B 346 -14.929 21.977 -0.787 1.00 76.28 D000 N ANISOU 6030 N TYR B 346 11449 10883 6649 1355 -374 -2753 D000 N ATOM 6031 CA TYR B 346 -15.586 22.347 0.462 1.00 80.21 D000 C ANISOU 6031 CA TYR B 346 12444 10931 7102 839 -325 -2426 D000 C ATOM 6032 C TYR B 346 -14.581 22.898 1.464 1.00 87.82 D000 C ANISOU 6032 C TYR B 346 13473 11702 8194 272 -31 -2539 D000 C ATOM 6033 O TYR B 346 -14.817 23.938 2.092 1.00 85.38 D000 O ANISOU 6033 O TYR B 346 13451 11004 7988 -186 -149 -2439 D000 O ATOM 6034 CB TYR B 346 -16.309 21.124 1.031 1.00 84.31 D000 C ANISOU 6034 CB TYR B 346 13362 11374 7299 883 -191 -2050 D000 C ATOM 6035 CG TYR B 346 -16.960 21.325 2.380 1.00 80.17 D000 C ANISOU 6035 CG TYR B 346 13416 10371 6674 401 -173 -1720 D000 C ATOM 6036 CD1 TYR B 346 -16.240 21.180 3.562 1.00 78.77 D000 C ANISOU 6036 CD1 TYR B 346 13516 10033 6381 -56 181 -1672 D000 C ATOM 6037 CD2 TYR B 346 -18.306 21.651 2.466 1.00 68.15 D000 C ANISOU 6037 CD2 TYR B 346 12170 8560 5164 409 -525 -1502 D000 C ATOM 6038 CE1 TYR B 346 -16.857 21.360 4.796 1.00 81.23 D000 C ANISOU 6038 CE1 TYR B 346 14465 9880 6517 -494 153 -1352 D000 C ATOM 6039 CE2 TYR B 346 -18.922 21.835 3.665 1.00 65.65 D000 C ANISOU 6039 CE2 TYR B 346 12426 7757 4761 25 -620 -1227 D000 C ATOM 6040 CZ TYR B 346 -18.202 21.687 4.840 1.00 71.36 D000 C ANISOU 6040 CZ TYR B 346 13524 8297 5294 -429 -294 -1118 D000 C ATOM 6041 OH TYR B 346 -18.842 21.876 6.041 1.00 68.66 D000 O ANISOU 6041 OH TYR B 346 13859 7439 4790 -810 -436 -827 D000 O ATOM 6042 N LEU B 347 -13.446 22.216 1.624 1.00 90.53 D000 N ANISOU 6042 N LEU B 347 13562 12298 8537 272 345 -2777 D000 N ATOM 6043 CA LEU B 347 -12.472 22.618 2.631 1.00 96.98 D000 C ANISOU 6043 CA LEU B 347 14412 12995 9440 -338 757 -2931 D000 C ATOM 6044 C LEU B 347 -11.694 23.860 2.214 1.00 97.13 D000 C ANISOU 6044 C LEU B 347 14026 13017 9862 -546 694 -3303 D000 C ATOM 6045 O LEU B 347 -11.228 24.613 3.075 1.00 95.53 D000 O ANISOU 6045 O LEU B 347 14006 12563 9728 -1218 950 -3315 D000 O ATOM 6046 CB LEU B 347 -11.516 21.459 2.915 1.00100.55 D000 C ANISOU 6046 CB LEU B 347 14622 13754 9830 -238 1178 -3188 D000 C ATOM 6047 CG LEU B 347 -12.149 20.269 3.646 1.00 94.65 D000 C ANISOU 6047 CG LEU B 347 14343 12923 8697 -185 1304 -2830 D000 C ATOM 6048 CD1 LEU B 347 -11.120 19.158 3.844 1.00 85.19 D000 C ANISOU 6048 CD1 LEU B 347 12826 12029 7513 -22 1648 -3196 D000 C ATOM 6049 CD2 LEU B 347 -12.773 20.697 4.979 1.00 78.00 D000 C ANISOU 6049 CD2 LEU B 347 12936 10375 6325 -823 1443 -2429 D000 C ATOM 6050 N GLU B 348 -11.545 24.093 0.910 0.93 98.43 D000 N ANISOU 6050 N GLU B 348 13683 13444 10273 -11 355 -3606 D000 N ATOM 6051 CA GLU B 348 -10.924 25.333 0.454 0.93107.60 D000 C ANISOU 6051 CA GLU B 348 14460 14565 11858 -166 200 -3966 D000 C ATOM 6052 C GLU B 348 -11.703 26.555 0.926 0.93109.45 D000 C ANISOU 6052 C GLU B 348 15146 14299 12141 -618 -75 -3675 D000 C ATOM 6053 O GLU B 348 -11.116 27.626 1.120 0.93112.87 D000 O ANISOU 6053 O GLU B 348 15481 14521 12884 -1068 -72 -3860 D000 O ATOM 6054 CB GLU B 348 -10.817 25.329 -1.074 0.93101.42 D000 C ANISOU 6054 CB GLU B 348 13147 14135 11252 566 -207 -4314 D000 C ATOM 6055 CG GLU B 348 -10.227 26.593 -1.717 0.93119.41 D000 C ANISOU 6055 CG GLU B 348 14973 16390 14007 530 -470 -4742 D000 C ATOM 6056 CD GLU B 348 -8.814 26.935 -1.260 0.93122.30 D000 C ANISOU 6056 CD GLU B 348 14931 16775 14760 77 -91 -5175 D000 C ATOM 6057 OE1 GLU B 348 -8.059 27.505 -2.076 0.93120.18 D000 O ANISOU 6057 OE1 GLU B 348 14086 16656 14919 288 -299 -5685 D000 O ATOM 6058 OE2 GLU B 348 -8.453 26.652 -0.100 0.93132.76 D000 O ANISOU 6058 OE2 GLU B 348 16490 17980 15974 -503 424 -5050 D000 O ATOM 6059 N ARG B 349 -13.014 26.415 1.131 0.88108.64 D000 N ANISOU 6059 N ARG B 349 15541 13964 11774 -516 -349 -3251 D000 N ATOM 6060 CA ARG B 349 -13.892 27.553 1.370 0.88108.30 D000 C ANISOU 6060 CA ARG B 349 15881 13429 11839 -762 -806 -3057 D000 C ATOM 6061 C ARG B 349 -14.285 27.733 2.833 0.88116.35 D000 C ANISOU 6061 C ARG B 349 17691 13905 12611 -1428 -703 -2622 D000 C ATOM 6062 O ARG B 349 -14.970 28.711 3.152 0.88126.21 D000 O ANISOU 6062 O ARG B 349 19355 14641 13958 -1673 -1159 -2459 D000 O ATOM 6063 CB ARG B 349 -15.159 27.420 0.514 0.88101.91 D000 C ANISOU 6063 CB ARG B 349 15024 12709 10988 -165 -1278 -3000 D000 C ATOM 6064 N VAL B 350 -13.887 26.827 3.724 1.00109.68 D000 N ANISOU 6064 N VAL B 350 17101 13134 11441 -1706 -173 -2457 D000 N ATOM 6065 CA VAL B 350 -14.118 27.024 5.155 1.00109.18 D000 C ANISOU 6065 CA VAL B 350 17849 12566 11067 -2394 -33 -2070 D000 C ATOM 6066 C VAL B 350 -12.822 27.483 5.817 1.00114.98 D000 C ANISOU 6066 C VAL B 350 18581 13277 11827 -3119 511 -2237 D000 C ATOM 6067 O VAL B 350 -12.547 28.679 5.907 1.00116.83 D000 O ANISOU 6067 O VAL B 350 18935 13172 12282 -3574 347 -2276 D000 O ATOM 6068 CB VAL B 350 -14.655 25.749 5.846 1.00106.14 D000 C ANISOU 6068 CB VAL B 350 17851 12230 10248 -2286 190 -1770 D000 C ATOM 6069 CG1 VAL B 350 -15.735 25.084 5.003 1.00102.03 D000 C ANISOU 6069 CG1 VAL B 350 17131 11885 9751 -1552 -194 -1705 D000 C ATOM 6070 CG2 VAL B 350 -13.518 24.777 6.147 1.00103.89 D000 C ANISOU 6070 CG2 VAL B 350 17267 12386 9822 -2378 891 -1991 D000 C TER HETATM 6071 P FMN B 401 -29.904 0.961 48.754 1.00 80.16 D000 P HETATM 6072 O1P FMN B 401 -30.323 0.127 49.943 1.00 66.02 D000 O HETATM 6073 O2P FMN B 401 -30.155 2.423 49.025 1.00 77.71 D000 O HETATM 6074 O3P FMN B 401 -30.631 0.526 47.505 1.00 66.14 D000 O HETATM 6075 C5' FMN B 401 -27.809 1.025 47.224 1.00 62.58 D000 C HETATM 6076 O5' FMN B 401 -28.300 0.732 48.493 1.00 79.20 D000 O HETATM 6077 C4' FMN B 401 -26.313 0.741 47.261 1.00 55.44 D000 C HETATM 6078 O4' FMN B 401 -26.102 -0.641 47.233 1.00 56.43 D000 O HETATM 6079 C3' FMN B 401 -25.663 1.427 46.061 1.00 52.72 D000 C HETATM 6080 O3' FMN B 401 -25.604 2.786 46.402 1.00 47.86 D000 O HETATM 6081 C2' FMN B 401 -24.264 0.879 45.778 1.00 51.18 D000 C HETATM 6082 O2' FMN B 401 -23.717 1.459 44.624 1.00 50.49 D000 O HETATM 6083 C1' FMN B 401 -23.372 1.309 46.916 1.00 48.63 D000 C HETATM 6084 N1 FMN B 401 -23.388 -1.272 48.022 1.00 51.27 D000 N HETATM 6085 C2 FMN B 401 -23.454 -2.608 48.624 1.00 56.74 D000 C HETATM 6086 O2 FMN B 401 -24.503 -3.060 48.933 1.00 59.82 D000 O HETATM 6087 N3 FMN B 401 -22.206 -3.378 48.833 1.00 50.59 D000 N HETATM 6088 C4 FMN B 401 -20.922 -2.816 48.450 1.00 48.53 D000 C HETATM 6089 C4A FMN B 401 -20.880 -1.442 47.825 1.00 47.46 D000 C HETATM 6090 O4 FMN B 401 -19.933 -3.446 48.642 1.00 49.76 D000 O HETATM 6091 C5A FMN B 401 -19.622 0.505 46.813 1.00 49.02 D000 C HETATM 6092 N5 FMN B 401 -19.635 -0.844 47.426 1.00 46.03 D000 N HETATM 6093 C6 FMN B 401 -18.391 1.050 46.431 1.00 44.22 D000 C HETATM 6094 C7 FMN B 401 -18.372 2.318 45.865 1.00 47.67 D000 C HETATM 6095 C7M FMN B 401 -16.908 2.616 45.568 1.00 46.58 D000 C HETATM 6096 C8 FMN B 401 -19.557 3.034 45.673 1.00 47.22 D000 C HETATM 6097 C8M FMN B 401 -19.411 4.407 45.037 1.00 44.84 D000 C HETATM 6098 C9 FMN B 401 -20.777 2.492 46.056 1.00 47.73 D000 C HETATM 6099 C9A FMN B 401 -20.811 1.221 46.625 1.00 46.46 D000 C HETATM 6100 C10 FMN B 401 -22.109 -0.705 47.627 1.00 46.06 D000 C HETATM 6101 N10 FMN B 401 -22.104 0.604 47.041 1.00 44.08 D000 N HETATM 6102 PA AATP B 402 -3.926 7.937 2.580 0.58 39.31 D000 P HETATM 6103 PA BATP B 402 -3.829 7.672 2.618 0.42 39.37 D000 P HETATM 6104 PB AATP B 402 -5.918 9.903 1.642 0.58 39.28 D000 P HETATM 6105 PB BATP B 402 -5.672 9.718 1.574 0.42 39.25 D000 P HETATM 6106 PG AATP B 402 -7.418 7.881 0.131 0.58 37.87 D000 P HETATM 6107 PG BATP B 402 -7.175 7.796 -0.111 0.42 39.30 D000 P HETATM 6108 C5'AATP B 402 -3.503 9.167 4.877 0.58 41.05 D000 C HETATM 6109 C5'BATP B 402 -3.808 9.407 4.606 0.42 41.35 D000 C HETATM 6110 O5'AATP B 402 -2.975 8.600 3.656 0.58 41.65 D000 O HETATM 6111 O5'BATP B 402 -3.189 8.298 3.919 0.42 42.78 D000 O HETATM 6112 C4'AATP B 402 -2.567 8.958 6.049 0.58 39.22 D000 C HETATM 6113 C4'BATP B 402 -2.773 9.998 5.531 0.42 41.52 D000 C HETATM 6114 O4'AATP B 402 -2.384 7.540 6.203 0.58 37.58 D000 O HETATM 6115 O4'BATP B 402 -2.357 8.942 6.423 0.42 38.46 D000 O HETATM 6116 C3'AATP B 402 -1.165 9.441 5.727 0.58 39.51 D000 C HETATM 6117 C3'BATP B 402 -1.533 10.353 4.709 0.42 40.08 D000 C HETATM 6118 O3'AATP B 402 -1.098 10.761 6.260 0.58 41.54 D000 O HETATM 6119 O3'BATP B 402 -0.903 11.457 5.347 0.42 40.98 D000 O HETATM 6120 C2'AATP B 402 -0.309 8.585 6.651 0.58 38.98 D000 C HETATM 6121 C2'BATP B 402 -0.614 9.167 4.968 0.42 40.35 D000 C HETATM 6122 O2'AATP B 402 -0.494 9.043 7.989 0.58 37.38 D000 O HETATM 6123 O2'BATP B 402 0.719 9.667 5.018 0.42 41.34 D000 O HETATM 6124 C1'AATP B 402 -1.065 7.255 6.637 0.58 40.09 D000 C HETATM 6125 C1'BATP B 402 -0.953 8.902 6.418 0.42 39.37 D000 C HETATM 6126 N1 AATP B 402 1.604 2.928 5.869 0.58 36.62 D000 N HETATM 6127 N1 BATP B 402 1.085 6.064 10.144 0.42 37.86 D000 N HETATM 6128 O1AAATP B 402 -3.188 7.051 1.658 0.58 39.45 D000 O HETATM 6129 O1ABATP B 402 -2.840 6.917 1.821 0.42 42.40 D000 O HETATM 6130 O1BAATP B 402 -6.742 9.643 2.844 0.58 39.42 D000 O HETATM 6131 O1BBATP B 402 -6.594 9.515 2.712 0.42 39.01 D000 O HETATM 6132 O1GAATP B 402 -8.802 8.297 -0.260 0.58 36.44 D000 O HETATM 6133 O1GBATP B 402 -8.454 8.321 -0.684 0.42 39.27 D000 O HETATM 6134 C2 AATP B 402 1.237 3.561 6.983 0.58 41.75 D000 C HETATM 6135 C2 BATP B 402 0.758 7.356 10.071 0.42 27.87 D000 C HETATM 6136 O2AAATP B 402 -5.105 7.272 3.312 0.58 35.90 D000 O HETATM 6137 O2ABATP B 402 -5.082 6.893 3.029 0.42 35.52 D000 O HETATM 6138 O2BAATP B 402 -5.683 11.355 1.260 0.58 41.87 D000 O HETATM 6139 O2BBATP B 402 -5.336 11.161 1.222 0.42 41.14 D000 O HETATM 6140 O2GAATP B 402 -7.346 7.076 1.427 0.58 38.50 D000 O HETATM 6141 O2GBATP B 402 -7.361 7.021 1.184 0.42 38.00 D000 O HETATM 6142 N3 AATP B 402 0.542 4.694 7.108 0.58 39.36 D000 N HETATM 6143 N3 BATP B 402 0.230 8.031 9.054 0.42 38.52 D000 N HETATM 6144 O3AAATP B 402 -4.513 9.173 1.770 0.58 42.33 D000 O HETATM 6145 O3ABATP B 402 -4.305 8.944 1.810 0.42 41.48 D000 O HETATM 6146 O3BAATP B 402 -6.546 9.171 0.424 0.58 40.56 D000 O HETATM 6147 O3BBATP B 402 -6.214 9.002 0.285 0.42 38.75 D000 O HETATM 6148 O3GAATP B 402 -6.654 7.145 -0.970 0.58 38.25 D000 O HETATM 6149 O3GBATP B 402 -6.363 6.958 -1.096 0.42 38.58 D000 O HETATM 6150 C4 AATP B 402 0.219 5.196 5.911 0.58 40.40 D000 C HETATM 6151 C4 BATP B 402 0.021 7.228 8.011 0.42 41.04 D000 C HETATM 6152 C5 AATP B 402 0.534 4.662 4.673 0.58 46.36 D000 C HETATM 6153 C5 BATP B 402 0.300 5.874 7.932 0.42 39.12 D000 C HETATM 6154 C6 AATP B 402 1.279 3.467 4.672 0.58 48.47 D000 C HETATM 6155 C6 BATP B 402 0.866 5.278 9.073 0.42 37.75 D000 C HETATM 6156 N6 AATP B 402 1.658 2.825 3.562 0.58 50.77 D000 N HETATM 6157 N6 BATP B 402 1.193 3.986 9.160 0.42 43.00 D000 N HETATM 6158 N7 AATP B 402 0.050 5.470 3.652 0.58 44.58 D000 N HETATM 6159 N7 BATP B 402 -0.049 5.375 6.687 0.42 43.16 D000 N HETATM 6160 C8 AATP B 402 -0.568 6.434 4.289 0.58 41.49 D000 C HETATM 6161 C8 BATP B 402 -0.526 6.421 6.057 0.42 40.44 D000 C HETATM 6162 N9 AATP B 402 -0.494 6.340 5.654 0.58 40.01 D000 N HETATM 6163 N9 BATP B 402 -0.531 7.568 6.806 0.42 37.32 D000 N HETATM 6164 MG MG B 403 -7.239 7.618 3.406 1.00 35.90 D000MG HETATM 6165 MG MG B 404 -4.616 5.431 4.804 1.00 40.01 D000MG HETATM 6166 O HOH B 501 -16.582 4.184 -3.405 1.00 54.93 D000 O HETATM 6167 O HOH B 502 -7.765 1.305 27.123 1.00 51.97 D000 O HETATM 6168 O HOH B 503 -15.702 -9.630 -9.305 1.00 64.93 D000 O HETATM 6169 O HOH B 504 -5.899 5.020 1.874 1.00 38.16 D000 O HETATM 6170 O HOH B 505 2.708 -1.241 17.015 1.00 38.93 D000 O HETATM 6171 O HOH B 506 0.505 -2.838 22.140 1.00 58.25 D000 O HETATM 6172 O HOH B 507 -18.074 3.624 57.316 1.00 68.84 D000 O HETATM 6173 O HOH B 508 1.253 -16.637 3.285 1.00 71.58 D000 O HETATM 6174 O HOH B 509 -4.480 5.601 0.085 1.00 55.23 D000 O HETATM 6175 O HOH B 510 15.376 -4.763 20.703 1.00 64.22 D000 O HETATM 6176 O HOH B 511 -20.024 5.652 59.886 1.00 59.34 D000 O HETATM 6177 O HOH B 512 -22.700 11.075 48.700 1.00 70.50 D000 O HETATM 6178 O HOH B 513 -23.701 9.673 13.901 1.00 53.32 D000 O HETATM 6179 O HOH B 514 -20.503 -10.177 55.806 1.00 61.82 D000 O HETATM 6180 O HOH B 515 -8.921 9.937 -2.644 1.00 56.46 D000 O HETATM 6181 O HOH B 516 -23.858 -2.542 14.965 1.00 52.83 D000 O HETATM 6182 O HOH B 517 -17.163 19.978 13.706 1.00 61.97 D000 O HETATM 6183 O HOH B 518 -9.542 1.433 31.746 1.00 57.81 D000 O HETATM 6184 O HOH B 519 10.300 -1.610 19.700 1.00 58.64 D000 O HETATM 6185 O HOH B 520 -6.825 0.194 1.978 1.00 46.34 D000 O HETATM 6186 O HOH B 521 -25.449 3.400 12.894 1.00 53.21 D000 O HETATM 6187 O HOH B 522 -18.841 -11.083 16.301 1.00 54.48 D000 O HETATM 6188 O HOH B 523 -11.409 -12.915 16.985 1.00 54.36 D000 O HETATM 6189 O HOH B 524 -21.124 15.691 2.267 1.00 47.01 D000 O HETATM 6190 O HOH B 525 -11.969 -17.853 14.562 1.00 61.83 D000 O HETATM 6191 O HOH B 526 -9.966 -10.531 42.943 1.00 53.49 D000 O HETATM 6192 O HOH B 527 -23.982 -17.017 1.746 1.00 61.56 D000 O HETATM 6193 O HOH B 528 -7.368 3.408 0.844 1.00 46.75 D000 O HETATM 6194 O HOH B 529 -27.155 -6.125 57.949 1.00 51.32 D000 O HETATM 6195 O HOH B 530 3.105 -6.032 16.077 1.00 45.18 D000 O HETATM 6196 O HOH B 531 5.121 -14.496 20.626 1.00 53.47 D000 O HETATM 6197 O HOH B 532 -26.617 -16.144 2.877 1.00 62.66 D000 O HETATM 6198 O HOH B 533 -29.470 -13.525 -0.032 1.00 57.31 D000 O HETATM 6199 O HOH B 534 -21.504 6.566 4.667 1.00 44.51 D000 O HETATM 6200 O HOH B 535 -24.031 12.690 3.186 1.00 53.34 D000 O HETATM 6201 O HOH B 536 -21.539 9.482 57.409 1.00 57.95 D000 O HETATM 6202 O HOH B 537 -27.619 -3.551 13.575 1.00 60.15 D000 O HETATM 6203 O HOH B 538 -4.754 -15.337 5.266 1.00 50.95 D000 O HETATM 6204 O HOH B 539 -3.421 9.025 36.110 1.00 56.08 D000 O HETATM 6205 O HOH B 540 7.877 -6.144 25.130 1.00 56.48 D000 O HETATM 6206 O HOH B 541 -11.032 -13.833 1.514 1.00 50.08 D000 O HETATM 6207 O HOH B 542 -3.134 4.111 6.167 1.00 43.32 D000 O HETATM 6208 O HOH B 543 -23.530 -5.729 21.825 1.00 59.87 D000 O HETATM 6209 O HOH B 544 2.525 -15.149 21.082 1.00 50.13 D000 O HETATM 6210 O HOH B 545 -13.477 12.004 3.977 1.00 43.31 D000 O HETATM 6211 O HOH B 546 -8.036 4.956 32.976 1.00 58.34 D000 O HETATM 6212 O HOH B 547 -5.675 -7.213 19.050 1.00 49.47 D000 O HETATM 6213 O HOH B 548 -2.429 -16.712 20.262 1.00 52.31 D000 O HETATM 6214 O HOH B 549 -27.537 -0.271 8.871 1.00 58.69 D000 O HETATM 6215 O HOH B 550 -7.757 18.049 18.719 1.00 65.71 D000 O HETATM 6216 O HOH B 551 -28.652 -11.086 -3.449 1.00 48.48 D000 O HETATM 6217 O HOH B 552 -19.405 -0.251 21.961 1.00 53.07 D000 O HETATM 6218 O HOH B 553 -15.754 -11.852 16.585 1.00 48.13 D000 O HETATM 6219 O HOH B 554 -6.831 4.253 -1.930 1.00 55.52 D000 O HETATM 6220 O HOH B 555 -2.642 20.764 9.408 1.00 62.02 D000 O HETATM 6221 O HOH B 556 -27.211 20.625 11.330 1.00 60.81 D000 O HETATM 6222 O HOH B 557 -0.003 7.508 56.500 1.00 69.20 D000 O HETATM 6223 O HOH B 558 -15.171 -7.073 21.380 1.00 72.16 D000 O HETATM 6224 O HOH B 559 -5.294 1.552 3.869 1.00 49.36 D000 O HETATM 6225 O HOH B 560 -1.752 -23.126 15.318 1.00 58.44 D000 O HETATM 6226 O HOH B 561 -13.604 -4.019 33.852 1.00 52.95 D000 O HETATM 6227 O HOH B 562 -6.725 -2.247 -4.794 1.00 62.56 D000 O HETATM 6228 O HOH B 563 -2.843 6.657 13.428 1.00 47.84 D000 O HETATM 6229 O HOH B 564 2.814 8.269 38.466 1.00 56.28 D000 O HETATM 6230 O HOH B 565 -22.771 4.070 18.067 1.00 59.23 D000 O HETATM 6231 O HOH B 566 -3.617 4.232 2.864 1.00 48.44 D000 O HETATM 6232 O HOH B 567 -6.317 -18.653 4.224 1.00 58.19 D000 O HETATM 6233 O HOH B 568 -29.085 -6.566 2.896 1.00 47.10 D000 O HETATM 6234 O HOH B 569 -24.773 -1.142 -4.556 1.00 65.11 D000 O HETATM 6235 O HOH B 570 -0.493 -15.866 5.483 1.00 61.95 D000 O HETATM 6236 O HOH B 571 -0.418 -17.275 32.385 1.00 73.54 D000 O HETATM 6237 O HOH B 572 -12.721 14.213 18.353 1.00 58.13 D000 O HETATM 6238 O HOH B 573 -20.563 4.891 16.672 1.00 53.19 D000 O HETATM 6239 O HOH B 574 -11.545 -6.010 32.985 1.00 65.22 D000 O HETATM 6240 O HOH B 575 -10.011 -21.356 13.058 1.00 66.19 D000 O HETATM 6241 O HOH B 576 -18.793 6.944 3.965 1.00 50.34 D000 O HETATM 6242 O HOH B 577 -15.197 -18.807 -2.052 1.00 74.49 D000 O HETATM 6243 O HOH B 578 -9.918 14.655 20.074 1.00 68.74 D000 O HETATM 6244 O HOH B 579 -18.011 -19.943 8.744 1.00 73.76 D000 O HETATM 6245 O HOH B 580 -0.010 -0.018 17.249 0.50 54.26 D000 O HETATM 6246 O HOH B 581 -20.178 -12.440 18.511 1.00 75.26 D000 O HETATM 6247 MG MG A 404 4.587 -5.418 4.778 1.00 40.01 E MG HETATM 6248 O HOH A 501 16.547 -4.138 -3.435 1.00 54.93 F O HETATM 6249 O HOH A 502 7.752 -1.381 27.111 1.00 51.97 F O HETATM 6250 O HOH A 503 15.662 9.700 -9.278 1.00 64.93 F O HETATM 6251 O HOH A 504 5.868 -4.995 1.849 1.00 38.16 F O HETATM 6252 O HOH A 505 -2.728 1.205 17.022 1.00 38.93 F O HETATM 6253 O HOH A 506 -0.521 2.782 22.151 1.00 58.25 F O HETATM 6254 O HOH A 507 18.084 -3.822 57.288 1.00 68.84 F O HETATM 6255 O HOH A 508 -1.283 16.657 3.353 1.00 71.58 F O HETATM 6256 O HOH A 509 4.447 -5.569 0.059 1.00 55.23 F O HETATM 6257 O HOH A 510 -15.393 4.712 20.734 1.00 64.22 F O HETATM 6258 O HOH A 511 20.036 -5.860 59.848 1.00 59.34 F O HETATM 6259 O HOH A 512 22.704 -11.238 48.638 1.00 70.50 F O HETATM 6260 O HOH A 513 23.678 -9.696 13.844 1.00 53.32 F O HETATM 6261 O HOH A 514 20.513 9.986 55.831 1.00 61.82 F O HETATM 6262 O HOH A 515 8.885 -9.894 -2.690 1.00 56.46 F O HETATM 6263 O HOH A 516 23.836 2.515 14.957 1.00 52.83 F O HETATM 6264 O HOH A 517 17.140 -20.000 13.612 1.00 61.97 F O HETATM 6265 O HOH A 518 9.533 -1.528 31.733 1.00 57.81 F O HETATM 6266 O HOH A 519 -10.318 1.563 19.714 1.00 58.64 F O HETATM 6267 O HOH A 520 6.794 -0.169 1.972 1.00 46.34 F O HETATM 6268 O HOH A 521 25.426 -3.419 12.861 1.00 53.21 F O HETATM 6269 O HOH A 522 18.821 11.050 16.331 1.00 54.48 F O HETATM 6270 O HOH A 523 11.389 12.879 17.028 1.00 54.36 F O HETATM 6271 O HOH A 524 21.092 -15.667 2.188 1.00 47.01 F O HETATM 6272 O HOH A 525 11.947 17.827 14.625 1.00 61.83 F O HETATM 6273 O HOH A 526 9.966 10.391 42.978 1.00 53.49 F O HETATM 6274 O HOH A 527 23.951 17.043 1.797 1.00 61.56 F O HETATM 6275 O HOH A 528 7.335 -3.379 0.824 1.00 46.75 F O HETATM 6276 O HOH A 529 27.166 5.924 57.953 1.00 51.32 F O HETATM 6277 O HOH A 530 -3.126 6.000 16.103 1.00 45.18 F O HETATM 6278 O HOH A 531 -5.138 14.445 20.688 1.00 53.47 F O HETATM 6279 O HOH A 532 26.586 16.165 2.922 1.00 62.66 F O HETATM 6280 O HOH A 533 29.437 13.558 0.000 1.00 57.31 F O HETATM 6281 O HOH A 534 21.475 -6.552 4.625 1.00 44.51 F O HETATM 6282 O HOH A 535 24.000 -12.670 3.117 1.00 53.34 F O HETATM 6283 O HOH A 536 21.549 -9.680 57.354 1.00 57.95 F O HETATM 6284 O HOH A 537 27.596 3.529 13.568 1.00 60.15 F O HETATM 6285 O HOH A 538 4.725 15.349 5.324 1.00 50.95 F O HETATM 6286 O HOH A 539 3.415 -9.137 36.071 1.00 56.08 F O HETATM 6287 O HOH A 540 -7.891 6.075 25.161 1.00 56.48 F O HETATM 6288 O HOH A 541 11.000 13.860 1.562 1.00 50.08 F O HETATM 6289 O HOH A 542 3.105 -4.103 6.148 1.00 43.32 F O HETATM 6290 O HOH A 543 23.513 5.674 21.830 1.00 59.87 F O HETATM 6291 O HOH A 544 -2.542 15.097 21.145 1.00 50.13 F O HETATM 6292 O HOH A 545 13.447 -11.988 3.918 1.00 43.31 F O HETATM 6293 O HOH A 546 8.028 -5.056 32.949 1.00 58.34 F O HETATM 6294 O HOH A 547 5.657 7.169 19.074 1.00 49.47 F O HETATM 6295 O HOH A 548 2.411 16.663 20.327 1.00 52.31 F O HETATM 6296 O HOH A 549 27.511 0.268 8.851 1.00 58.69 F O HETATM 6297 O HOH A 550 7.739 -18.092 18.641 1.00 65.71 F O HETATM 6298 O HOH A 551 28.616 11.132 -3.426 1.00 48.48 F O HETATM 6299 O HOH A 552 19.389 0.196 21.947 1.00 53.07 F O HETATM 6300 O HOH A 553 15.733 11.818 16.621 1.00 48.13 F O HETATM 6301 O HOH A 554 6.796 -4.213 -1.952 1.00 55.52 F O HETATM 6302 O HOH A 555 2.616 -20.769 9.322 1.00 62.02 F O HETATM 6303 O HOH A 556 27.187 -20.638 11.227 1.00 60.81 F O HETATM 6304 O HOH A 557 0.013 -7.702 56.469 1.00 69.20 F O HETATM 6305 O HOH A 558 15.155 7.019 21.397 1.00 72.16 F O HETATM 6306 O HOH A 559 5.264 -1.535 3.858 1.00 49.36 F O HETATM 6307 O HOH A 560 1.730 23.097 15.410 1.00 58.44 F O HETATM 6308 O HOH A 561 13.597 3.915 33.857 1.00 52.95 F O HETATM 6309 O HOH A 562 6.688 2.299 -4.790 1.00 62.56 F O HETATM 6310 O HOH A 563 2.820 -6.678 13.399 1.00 47.84 F O HETATM 6311 O HOH A 564 -2.817 -8.391 38.435 1.00 56.28 F O HETATM 6312 O HOH A 565 22.752 -4.110 18.034 1.00 59.23 F O HETATM 6313 O HOH A 566 3.586 -4.211 2.844 1.00 48.44 F O HETATM 6314 O HOH A 567 6.287 18.669 4.294 1.00 58.19 F O HETATM 6315 O HOH A 568 29.054 6.588 2.900 1.00 47.10 F O HETATM 6316 O HOH A 569 24.737 1.193 -4.571 1.00 65.11 F O HETATM 6317 O HOH A 570 0.464 15.877 5.547 1.00 61.95 F O HETATM 6318 O HOH A 571 0.409 17.177 32.454 1.00 73.54 F O HETATM 6319 O HOH A 572 12.702 -14.254 18.286 1.00 58.13 F O HETATM 6320 O HOH A 573 20.542 -4.925 16.636 1.00 53.19 F O HETATM 6321 O HOH A 574 11.537 5.910 33.001 1.00 65.22 F O HETATM 6322 O HOH A 575 9.988 21.336 13.136 1.00 66.19 F O HETATM 6323 O HOH A 576 18.763 -6.928 3.923 1.00 50.34 F O HETATM 6324 O HOH A 577 15.162 18.848 -1.988 1.00 74.49 F O HETATM 6325 O HOH A 578 9.900 -14.703 20.008 1.00 68.74 F O HETATM 6326 O HOH A 579 17.984 19.940 8.810 1.00 73.76 F O HETATM 6327 O HOH A 580 -0.010 -0.018 17.249 0.50 54.26 F O HETATM 6328 O HOH A 581 20.159 12.398 18.545 1.00 75.26 F O CONECT 2989 2990 2991 2992 2994 CONECT 2990 2989 CONECT 2991 2989 CONECT 2992 2989 CONECT 2993 2994 2995 CONECT 2994 2989 2993 CONECT 2995 2993 2996 2997 CONECT 2996 2995 CONECT 2997 2995 2998 2999 CONECT 2998 2997 CONECT 2999 2997 3000 3001 CONECT 3000 2999 CONECT 3001 2999 3019 CONECT 3002 3003 3018 CONECT 3003 3002 3004 3005 CONECT 3004 3003 CONECT 3005 3003 3006 CONECT 3006 3005 3007 3008 CONECT 3007 3006 3010 3018 CONECT 3008 3006 CONECT 3009 3010 3011 3017 CONECT 3010 3007 3009 CONECT 3011 3009 3012 CONECT 3012 3011 3013 3014 CONECT 3013 3012 CONECT 3014 3012 3015 3016 CONECT 3015 3014 CONECT 3016 3014 3017 CONECT 3017 3009 3016 3019 CONECT 3018 3002 3007 3019 CONECT 3019 3001 3017 3018 CONECT 3020 3028 3046 3054 3062 CONECT 3021 3029 3047 3055 3063 CONECT 3022 3048 3056 3062 3064 CONECT 3023 3049 3057 3063 3065 CONECT 3024 3050 3058 3064 3066 CONECT 3025 3051 3059 3065 3067 CONECT 3026 3028 3030 CONECT 3027 3029 3031 CONECT 3028 3020 3026 CONECT 3029 3021 3027 CONECT 3030 3026 3032 3034 CONECT 3031 3027 3033 3035 CONECT 3032 3030 3042 CONECT 3033 3031 3043 CONECT 3034 3030 3036 3038 CONECT 3035 3031 3037 3039 CONECT 3036 3034 CONECT 3037 3035 CONECT 3038 3034 3040 3042 CONECT 3039 3035 3041 3043 CONECT 3040 3038 CONECT 3041 3039 CONECT 3042 3032 3038 3080 CONECT 3043 3033 3039 3081 CONECT 3044 3052 3072 CONECT 3045 3053 3073 CONECT 3046 3020 CONECT 3047 3021 CONECT 3048 3022 CONECT 3049 3023 CONECT 3050 3024 CONECT 3051 3025 CONECT 3052 3044 3060 CONECT 3053 3045 3061 CONECT 3054 3020 CONECT 3055 3021 CONECT 3056 3022 CONECT 3057 3023 CONECT 3058 3024 CONECT 3059 3025 CONECT 3060 3052 3068 CONECT 3061 3053 3069 CONECT 3062 3020 3022 CONECT 3063 3021 3023 CONECT 3064 3022 3024 CONECT 3065 3023 3025 CONECT 3066 3024 CONECT 3067 3025 CONECT 3068 3060 3070 3080 CONECT 3069 3061 3071 3081 CONECT 3070 3068 3072 3076 CONECT 3071 3069 3073 3077 CONECT 3072 3044 3070 3074 CONECT 3073 3045 3071 3075 CONECT 3074 3072 CONECT 3075 3073 CONECT 3076 3070 3078 CONECT 3077 3071 3079 CONECT 3078 3076 3080 CONECT 3079 3077 3081 CONECT 3080 3042 3068 3078 CONECT 3081 3043 3069 3079 CONECT 6071 6072 6073 6074 6076 CONECT 6072 6071 CONECT 6073 6071 CONECT 6074 6071 CONECT 6075 6076 6077 CONECT 6076 6071 6075 CONECT 6077 6075 6078 6079 CONECT 6078 6077 CONECT 6079 6077 6080 6081 CONECT 6080 6079 CONECT 6081 6079 6082 6083 CONECT 6082 6081 CONECT 6083 6081 6101 CONECT 6084 6085 6100 CONECT 6085 6084 6086 6087 CONECT 6086 6085 CONECT 6087 6085 6088 CONECT 6088 6087 6089 6090 CONECT 6089 6088 6092 6100 CONECT 6090 6088 CONECT 6091 6092 6093 6099 CONECT 6092 6089 6091 CONECT 6093 6091 6094 CONECT 6094 6093 6095 6096 CONECT 6095 6094 CONECT 6096 6094 6097 6098 CONECT 6097 6096 CONECT 6098 6096 6099 CONECT 6099 6091 6098 6101 CONECT 6100 6084 6089 6101 CONECT 6101 6083 6099 6100 CONECT 6102 6110 6128 6136 6144 CONECT 6103 6111 6129 6137 6145 CONECT 6104 6130 6138 6144 6146 CONECT 6105 6131 6139 6145 6147 CONECT 6106 6132 6140 6146 6148 CONECT 6107 6133 6141 6147 6149 CONECT 6108 6110 6112 CONECT 6109 6111 6113 CONECT 6110 6102 6108 CONECT 6111 6103 6109 CONECT 6112 6108 6114 6116 CONECT 6113 6109 6115 6117 CONECT 6114 6112 6124 CONECT 6115 6113 6125 CONECT 6116 6112 6118 6120 CONECT 6117 6113 6119 6121 CONECT 6118 6116 CONECT 6119 6117 CONECT 6120 6116 6122 6124 CONECT 6121 6117 6123 6125 CONECT 6122 6120 CONECT 6123 6121 CONECT 6124 6114 6120 6162 CONECT 6125 6115 6121 6163 CONECT 6126 6134 6154 CONECT 6127 6135 6155 CONECT 6128 6102 CONECT 6129 6103 CONECT 6130 6104 CONECT 6131 6105 CONECT 6132 6106 CONECT 6133 6107 CONECT 6134 6126 6142 CONECT 6135 6127 6143 CONECT 6136 6102 CONECT 6137 6103 CONECT 6138 6104 CONECT 6139 6105 CONECT 6140 6106 CONECT 6141 6107 CONECT 6142 6134 6150 CONECT 6143 6135 6151 CONECT 6144 6102 6104 CONECT 6145 6103 6105 CONECT 6146 6104 6106 CONECT 6147 6105 6107 CONECT 6148 6106 CONECT 6149 6107 CONECT 6150 6142 6152 6162 CONECT 6151 6143 6153 6163 CONECT 6152 6150 6154 6158 CONECT 6153 6151 6155 6159 CONECT 6154 6126 6152 6156 CONECT 6155 6127 6153 6157 CONECT 6156 6154 CONECT 6157 6155 CONECT 6158 6152 6160 CONECT 6159 6153 6161 CONECT 6160 6158 6162 CONECT 6161 6159 6163 CONECT 6162 6124 6150 6160 CONECT 6163 6125 6151 6161 END If you find results from this site helpful for your research, please cite one of our papers:
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