MODEL 1 HETATM 1 N LIG 1 6.761 -43.477 9.846 1.00 0.00 N HETATM 2 C LIG 1 2.311 -46.534 9.818 1.00 0.00 C HETATM 3 C LIG 1 2.343 -45.333 9.102 1.00 0.00 C HETATM 4 C LIG 1 3.488 -44.529 9.128 1.00 0.00 C HETATM 5 C LIG 1 4.607 -44.923 9.871 1.00 0.00 C HETATM 6 C LIG 1 5.795 -44.119 9.863 1.00 0.00 C HETATM 7 C LIG 1 4.567 -46.113 10.604 1.00 0.00 C HETATM 8 C LIG 1 3.423 -46.916 10.577 1.00 0.00 C HETATM 9 C LIG 1 1.150 -47.416 9.711 1.00 0.00 C HETATM 10 C LIG 1 1.000 -48.425 10.580 1.00 0.00 C HETATM 11 C LIG 1 -0.171 -49.339 10.493 1.00 0.00 C HETATM 12 C LIG 1 -0.596 -50.006 11.752 1.00 0.00 C HETATM 13 C LIG 1 -1.652 -50.924 11.771 1.00 0.00 C HETATM 14 C LIG 1 -2.031 -51.507 12.974 1.00 0.00 C HETATM 15 C LIG 1 -1.368 -51.194 14.159 1.00 0.00 C HETATM 16 C LIG 1 -0.296 -50.306 14.147 1.00 0.00 C HETATM 17 C LIG 1 0.095 -49.717 12.938 1.00 0.00 C HETATM 18 O LIG 1 -0.745 -49.572 9.435 1.00 0.00 O HETATM 19 O LIG 1 -1.789 -51.771 15.322 1.00 0.00 O HETATM 20 F LIG 1 -3.052 -52.376 12.975 1.00 0.00 F HETATM 21 H LIG 1 -1.064 -51.766 15.968 1.00 0.00 H ATOM 22 N HIS A -14 21.795 -5.161 5.323 1.00 92.88 N ANISOU 22 N HIS A -14 9049 12300 13941 -2188 1087 -819 N ATOM 23 CA HIS A -14 21.981 -5.105 3.886 1.00 94.37 C ANISOU 23 CA HIS A -14 9241 12557 14060 -2257 1396 -645 C ATOM 24 C HIS A -14 20.904 -5.866 3.172 1.00 90.89 C ANISOU 24 C HIS A -14 9021 12149 13365 -2066 1478 -521 C ATOM 25 O HIS A -14 19.859 -5.293 2.803 1.00 89.40 O ANISOU 25 O HIS A -14 9124 11802 13043 -2102 1543 -342 O ATOM 26 CB HIS A -14 23.351 -5.647 3.502 1.00 93.30 C ANISOU 26 CB HIS A -14 8750 12648 14050 -2263 1488 -755 C ATOM 27 CG HIS A -14 24.039 -6.403 4.613 1.00 93.57 C ANISOU 27 CG HIS A -14 8535 12797 14221 -2121 1215 -998 C ATOM 28 CD2 HIS A -14 25.204 -6.124 5.323 1.00 97.13 C ANISOU 28 CD2 HIS A -14 8693 13307 14906 -2222 1086 -1167 C ATOM 29 ND1 HIS A -14 23.562 -7.559 5.104 1.00 90.50 N ANISOU 29 ND1 HIS A -14 8184 12473 13730 -1848 1029 -1075 N ATOM 30 CE1 HIS A -14 24.378 -8.001 6.079 1.00 92.06 C ANISOU 30 CE1 HIS A -14 8141 12763 14073 -1765 785 -1260 C ATOM 31 NE2 HIS A -14 25.382 -7.122 6.211 1.00 96.09 N ANISOU 31 NE2 HIS A -14 8444 13281 14786 -1991 816 -1326 N ATOM 32 N HIS A -13 21.130 -7.158 2.963 1.00138.04 N ANISOU 32 N HIS A -13 14861 18314 19274 -1855 1464 -618 N ATOM 33 CA HIS A -13 20.167 -7.993 2.271 1.00135.06 C ANISOU 33 CA HIS A -13 14671 17984 18663 -1667 1532 -536 C ATOM 34 C HIS A -13 19.159 -8.573 3.218 1.00131.08 C ANISOU 34 C HIS A -13 14309 17400 18096 -1491 1294 -597 C ATOM 35 O HIS A -13 17.936 -8.486 2.982 1.00128.45 O ANISOU 35 O HIS A -13 14242 16966 17597 -1448 1316 -474 O ATOM 36 CB HIS A -13 20.872 -9.108 1.507 1.00132.14 C ANISOU 36 CB HIS A -13 14108 17837 18262 -1522 1646 -624 C ATOM 37 CG HIS A -13 21.220 -8.746 0.083 1.00135.00 C ANISOU 37 CG HIS A -13 14475 18300 18518 -1639 1964 -486 C ATOM 38 CD2 HIS A -13 21.958 -9.428 -0.881 1.00137.57 C ANISOU 38 CD2 HIS A -13 14636 18832 18801 -1575 2157 -544 C ATOM 39 ND1 HIS A -13 20.818 -7.597 -0.489 1.00135.93 N ANISOU 39 ND1 HIS A -13 14786 18311 18551 -1834 2113 -262 N ATOM 40 CE1 HIS A -13 21.274 -7.544 -1.754 1.00138.99 C ANISOU 40 CE1 HIS A -13 15136 18847 18827 -1896 2388 -158 C ATOM 41 NE2 HIS A -13 21.971 -8.665 -1.993 1.00139.96 N ANISOU 41 NE2 HIS A -13 15038 19169 18973 -1740 2424 -346 N ATOM 42 N SER A -12 19.644 -9.171 4.300 1.00 74.21 N ANISOU 42 N SER A -12 6930 10246 11019 -1383 1057 -775 N ATOM 43 CA SER A -12 18.766 -9.753 5.306 1.00 70.85 C ANISOU 43 CA SER A -12 6623 9763 10535 -1218 816 -825 C ATOM 44 C SER A -12 17.707 -8.752 5.759 1.00 69.02 C ANISOU 44 C SER A -12 6647 9332 10247 -1335 782 -739 C ATOM 45 O SER A -12 16.783 -9.104 6.489 1.00 66.33 O ANISOU 45 O SER A -12 6439 8933 9829 -1224 626 -758 O ATOM 46 CB SER A -12 19.575 -10.239 6.510 1.00 20.36 C ATOM 47 OG SER A -12 20.214 -9.158 7.165 1.00 20.36 O ATOM 48 N SER A -11 17.847 -7.504 5.326 1.00 61.93 N ANISOU 48 N SER A -11 5818 8315 9397 -1555 931 -642 N ATOM 49 CA SER A -11 16.925 -6.452 5.737 1.00 60.85 C ANISOU 49 CA SER A -11 5929 7946 9244 -1660 899 -569 C ATOM 50 C SER A -11 16.783 -5.293 4.751 1.00 62.49 C ANISOU 50 C SER A -11 6290 8007 9445 -1841 1118 -366 C ATOM 51 O SER A -11 16.062 -4.337 5.027 1.00 62.35 O ANISOU 51 O SER A -11 6485 7761 9443 -1916 1091 -295 O ATOM 52 CB SER A -11 17.308 -5.920 7.122 1.00 58.33 C ANISOU 52 CB SER A -11 5540 7558 9065 -1729 666 -744 C ATOM 53 OG SER A -11 18.442 -5.074 7.053 1.00 62.06 O ANISOU 53 OG SER A -11 5848 8016 9716 -1930 716 -784 O ATOM 54 N GLY A -10 17.454 -5.363 3.607 1.00 63.93 N ANISOU 54 N GLY A -10 6375 8315 9600 -1900 1327 -266 N ATOM 55 CA GLY A -10 17.323 -4.293 2.646 1.00 66.06 C ANISOU 55 CA GLY A -10 6800 8462 9838 -2067 1520 -36 C ATOM 56 C GLY A -10 16.873 -4.794 1.303 1.00 65.60 C ANISOU 56 C GLY A -10 6857 8531 9537 -1976 1706 145 C ATOM 57 O GLY A -10 17.309 -5.829 0.845 1.00 65.47 O ANISOU 57 O GLY A -10 6689 8743 9444 -1861 1770 66 O ATOM 58 N LEU A -9 16.002 -4.046 0.659 1.00 51.93 N ANISOU 58 N LEU A -9 5399 6652 7682 -2015 1777 381 N ATOM 59 CA LEU A -9 15.632 -4.372 -0.694 1.00 52.52 C ANISOU 59 CA LEU A -9 5591 6866 7497 -1947 1944 571 C ATOM 60 C LEU A -9 16.362 -3.469 -1.659 1.00 57.19 C ANISOU 60 C LEU A -9 6162 7472 8095 -2155 2150 774 C ATOM 61 O LEU A -9 16.290 -2.262 -1.545 1.00 59.06 O ANISOU 61 O LEU A -9 6512 7481 8446 -2322 2142 917 O ATOM 62 CB LEU A -9 14.152 -4.193 -0.879 1.00 50.00 C ANISOU 62 CB LEU A -9 5588 6406 7004 -1831 1868 728 C ATOM 63 CG LEU A -9 13.559 -5.378 -1.578 1.00 48.09 C ANISOU 63 CG LEU A -9 5398 6376 6499 -1625 1896 718 C ATOM 64 CD1 LEU A -9 14.106 -6.599 -0.880 1.00 46.33 C ANISOU 64 CD1 LEU A -9 4932 6305 6366 -1513 1825 433 C ATOM 65 CD2 LEU A -9 12.051 -5.336 -1.512 1.00 45.45 C ANISOU 65 CD2 LEU A -9 5338 5904 6026 -1489 1771 819 C ATOM 66 N GLU A -8 17.068 -4.045 -2.618 1.00133.66 N ANISOU 66 N GLU A -8 15705 17417 17663 -2145 2341 788 N ATOM 67 CA GLU A -8 17.760 -3.218 -3.581 1.00138.58 C ANISOU 67 CA GLU A -8 16303 18079 18271 -2349 2566 1003 C ATOM 68 C GLU A -8 16.967 -3.111 -4.861 1.00139.49 C ANISOU 68 C GLU A -8 16673 18267 18060 -2287 2683 1285 C ATOM 69 O GLU A -8 15.861 -3.603 -4.942 1.00136.44 O ANISOU 69 O GLU A -8 16479 17878 17483 -2093 2568 1299 O ATOM 70 CB GLU A -8 19.214 -3.649 -3.821 1.00137.44 C ANISOU 70 CB GLU A -8 15816 18164 18241 -2428 2737 857 C ATOM 71 CG GLU A -8 20.211 -3.495 -2.682 1.00138.21 C ANISOU 71 CG GLU A -8 15631 18202 18679 -2542 2629 620 C ATOM 72 CD GLU A -8 21.588 -4.032 -3.052 1.00141.56 C ANISOU 72 CD GLU A -8 15708 18882 19198 -2583 2800 478 C ATOM 73 OE1 GLU A -8 21.730 -4.690 -4.105 1.00142.76 O ANISOU 73 OE1 GLU A -8 15837 19260 19147 -2488 2995 517 O ATOM 74 OE2 GLU A -8 22.549 -3.790 -2.295 1.00143.39 O1- ANISOU 74 OE2 GLU A -8 15679 19092 19709 -2706 2737 313 O1- ATOM 75 N VAL A -7 17.509 -2.432 -5.853 1.00 85.37 N ANISOU 75 N VAL A -7 9820 11479 11137 -2455 2903 1522 N ATOM 76 CA VAL A -7 16.681 -2.064 -6.998 1.00 86.97 C ANISOU 76 CA VAL A -7 10301 11712 11030 -2416 2974 1846 C ATOM 77 C VAL A -7 16.241 -3.236 -7.867 1.00 85.89 C ANISOU 77 C VAL A -7 10219 11862 10553 -2165 3042 1795 C ATOM 78 O VAL A -7 17.027 -3.786 -8.613 1.00 88.39 O ANISOU 78 O VAL A -7 10388 12434 10763 -2150 3265 1739 O ATOM 79 CB VAL A -7 17.326 -0.957 -7.857 1.00 88.31 C ANISOU 79 CB VAL A -7 10485 11871 11197 -2674 3193 2164 C ATOM 80 CG1 VAL A -7 17.232 -1.303 -9.320 1.00 91.12 C ANISOU 80 CG1 VAL A -7 10931 12512 11177 -2584 3412 2369 C ATOM 81 CG2 VAL A -7 16.638 0.367 -7.616 1.00 89.21 C ANISOU 81 CG2 VAL A -7 10850 11634 11410 -2815 3046 2420 C ATOM 82 N LEU A -6 14.964 -3.580 -7.753 1.00 85.27 N ANISOU 82 N LEU A -6 10359 11723 10316 -1970 2847 1800 N ATOM 83 CA LEU A -6 14.359 -4.633 -8.534 1.00 84.27 C ANISOU 83 CA LEU A -6 10328 11823 9866 -1726 2869 1742 C ATOM 84 C LEU A -6 12.884 -4.414 -8.845 1.00 83.02 C ANISOU 84 C LEU A -6 10476 11585 9482 -1590 2687 1925 C ATOM 85 O LEU A -6 12.129 -3.858 -8.070 1.00 80.83 O ANISOU 85 O LEU A -6 10314 11061 9338 -1617 2470 1974 O ATOM 86 CB LEU A -6 14.538 -5.959 -7.836 1.00 75.90 C ANISOU 86 CB LEU A -6 9091 10848 8900 -1567 2789 1360 C ATOM 87 CG LEU A -6 16.017 -6.281 -7.794 1.00 78.28 C ANISOU 87 CG LEU A -6 9079 11287 9376 -1665 2969 1182 C ATOM 88 CD1 LEU A -6 16.217 -7.538 -6.964 1.00 75.02 C ANISOU 88 CD1 LEU A -6 8477 10921 9105 -1509 2837 820 C ATOM 89 CD2 LEU A -6 16.572 -6.451 -9.198 1.00 82.69 C ANISOU 89 CD2 LEU A -6 9632 12103 9685 -1664 3258 1272 C ATOM 90 N PHE A -5 12.489 -4.881 -10.016 1.00 98.20 N ANISOU 90 N PHE A -5 12545 13704 11061 -1429 2765 1983 N ATOM 91 CA PHE A -5 11.106 -4.873 -10.429 1.00 97.40 C ANISOU 91 CA PHE A -5 12714 13571 10724 -1257 2565 2093 C ATOM 92 C PHE A -5 10.712 -6.289 -10.779 1.00 95.52 C ANISOU 92 C PHE A -5 12521 13496 10276 -1009 2567 1815 C ATOM 93 O PHE A -5 11.053 -6.821 -11.826 1.00 98.17 O ANISOU 93 O PHE A -5 12924 14020 10355 -940 2761 1755 O ATOM 94 CB PHE A -5 10.919 -3.874 -11.554 1.00 96.44 C ANISOU 94 CB PHE A -5 12785 13470 10388 -1313 2633 2461 C ATOM 95 CG PHE A -5 11.532 -2.547 -11.240 1.00 99.10 C ANISOU 95 CG PHE A -5 13076 13615 10964 -1610 2672 2698 C ATOM 96 CD1 PHE A -5 10.752 -1.455 -10.965 1.00 99.45 C ANISOU 96 CD1 PHE A -5 13311 13387 11088 -1719 2444 2917 C ATOM 97 CD2 PHE A -5 12.905 -2.421 -11.127 1.00101.31 C ANISOU 97 CD2 PHE A -5 13127 13941 11424 -1794 2924 2653 C ATOM 98 CE1 PHE A -5 11.328 -0.251 -10.635 1.00102.08 C ANISOU 98 CE1 PHE A -5 13644 13467 11676 -1980 2491 3094 C ATOM 99 CE2 PHE A -5 13.489 -1.220 -10.797 1.00103.94 C ANISOU 99 CE2 PHE A -5 13422 14064 12008 -2074 2963 2840 C ATOM 100 CZ PHE A -5 12.697 -0.135 -10.550 1.00104.32 C ANISOU 100 CZ PHE A -5 13692 13810 12134 -2162 2749 3058 C ATOM 101 N GLN A -4 10.033 -6.907 -9.830 1.00119.76 N ANISOU 101 N GLN A -4 15562 16475 13468 -912 2352 1617 N ATOM 102 CA GLN A -4 9.560 -8.262 -9.965 1.00117.56 C ANISOU 102 CA GLN A -4 15333 16290 13045 -721 2303 1325 C ATOM 103 C GLN A -4 8.055 -8.263 -9.788 1.00115.33 C ANISOU 103 C GLN A -4 15294 15856 12671 -594 2045 1349 C ATOM 104 O GLN A -4 7.547 -8.669 -8.756 1.00111.63 O ANISOU 104 O GLN A -4 14748 15294 12374 -551 1873 1216 O ATOM 105 CB GLN A -4 10.207 -9.176 -8.920 1.00112.92 C ANISOU 105 CB GLN A -4 14461 15724 12719 -726 2293 1027 C ATOM 106 CG GLN A -4 11.713 -9.007 -8.769 1.00115.03 C ANISOU 106 CG GLN A -4 14461 16058 13189 -879 2485 975 C ATOM 107 CD GLN A -4 12.345 -10.020 -7.821 1.00112.72 C ANISOU 107 CD GLN A -4 13902 15774 13153 -841 2422 645 C ATOM 108 NE2 GLN A -4 13.104 -10.961 -8.378 1.00114.43 N ANISOU 108 NE2 GLN A -4 13978 16174 13325 -775 2549 433 N ATOM 109 OE1 GLN A -4 12.161 -9.954 -6.609 1.00109.79 O ANISOU 109 OE1 GLN A -4 13457 15243 13016 -863 2258 583 O ATOM 110 N GLY A -3 7.337 -7.796 -10.800 1.00172.89 N ANISOU 110 N GLY A -3 22930 23088 19674 -579 2023 1488 N ATOM 111 CA GLY A -3 5.926 -8.021 -10.817 1.00171.21 C ANISOU 111 CA GLY A -3 22940 22831 19280 -605 1709 1418 C ATOM 112 C GLY A -3 5.208 -6.712 -10.848 1.00172.50 C ANISOU 112 C GLY A -3 23255 22865 19422 -755 1495 1723 C ATOM 113 O GLY A -3 5.797 -5.654 -11.076 1.00175.23 O ANISOU 113 O GLY A -3 23608 23173 19799 -965 1567 1942 O ATOM 114 N PRO A -2 3.910 -6.804 -10.608 1.00112.43 N ANISOU 114 N PRO A -2 15698 15221 11798 -587 1214 1777 N ATOM 115 CA PRO A -2 2.987 -5.728 -10.928 1.00114.44 C ANISOU 115 CA PRO A -2 16140 15329 12012 -552 1007 2082 C ATOM 116 C PRO A -2 3.495 -4.342 -10.558 1.00116.11 C ANISOU 116 C PRO A -2 16356 15303 12457 -718 1064 2338 C ATOM 117 O PRO A -2 4.340 -4.149 -9.687 1.00114.67 O ANISOU 117 O PRO A -2 15981 15037 12552 -831 1196 2285 O ATOM 118 CB PRO A -2 1.747 -6.098 -10.115 1.00104.86 C ANISOU 118 CB PRO A -2 14858 14024 10960 -323 746 2009 C ATOM 119 CG PRO A -2 2.257 -6.934 -8.980 1.00100.89 C ANISOU 119 CG PRO A -2 14117 13523 10694 -310 852 1746 C ATOM 120 CD PRO A -2 3.676 -7.335 -9.256 1.00101.79 C ANISOU 120 CD PRO A -2 14146 13790 10740 -495 1137 1617 C ATOM 121 N GLY A -1 2.966 -3.362 -11.261 1.00145.00 N ANISOU 121 N GLY A -1 20233 18851 16010 -720 945 2624 N ATOM 122 CA GLY A -1 3.005 -2.016 -10.779 1.00146.25 C ANISOU 122 CA GLY A -1 20430 18690 16450 -796 907 2866 C ATOM 123 C GLY A -1 1.673 -1.895 -10.083 1.00143.88 C ANISOU 123 C GLY A -1 20153 18176 16340 -553 632 2857 C ATOM 124 O GLY A -1 1.075 -2.883 -9.668 1.00140.58 O ANISOU 124 O GLY A -1 19634 17867 15912 -390 539 2645 O ATOM 125 N SER A 0 1.192 -0.662 -9.968 1.00190.03 N ANISOU 125 N SER A 0 26124 23708 22371 -528 499 3082 N ATOM 126 CA SER A 0 -0.112 -0.403 -9.371 1.00188.52 C ANISOU 126 CA SER A 0 25938 23300 22390 -285 233 3072 C ATOM 127 C SER A 0 -1.221 -0.663 -10.385 1.00190.38 C ANISOU 127 C SER A 0 26283 23701 22353 -102 -8 3170 C ATOM 128 O SER A 0 -0.954 -0.930 -11.556 1.00193.17 O ANISOU 128 O SER A 0 26757 24302 22338 -177 31 3260 O ATOM 129 CB SER A 0 -0.192 1.036 -8.859 1.00184.90 C ANISOU 129 CB SER A 0 25571 22421 22262 -313 180 3229 C ATOM 130 OG SER A 0 -0.601 1.921 -9.887 1.00189.86 O ANISOU 130 OG SER A 0 26425 22960 22755 -297 48 3527 O TER 131 SER A 0 ATOM 132 N ASP A 18 -2.466 -0.589 -9.929 1.00116.74 N ANISOU 132 N ASP A 18 17628 13802 12926 204 -60 3107 N ATOM 133 CA ASP A 18 -2.753 -0.298 -8.532 1.00113.21 C ANISOU 133 CA ASP A 18 17012 13097 12905 260 -98 2938 C ATOM 134 C ASP A 18 -3.005 -1.584 -7.756 1.00107.81 C ANISOU 134 C ASP A 18 16103 12597 12264 314 -136 2595 C ATOM 135 O ASP A 18 -3.769 -1.597 -6.791 1.00105.41 O ANISOU 135 O ASP A 18 15654 12168 12228 462 -274 2446 O ATOM 136 CB ASP A 18 -3.961 0.634 -8.417 1.00112.86 C ANISOU 136 CB ASP A 18 17009 12800 13071 511 -366 3079 C ATOM 137 CG ASP A 18 -3.655 2.044 -8.880 1.00118.00 C ANISOU 137 CG ASP A 18 17871 13166 13798 453 -311 3419 C ATOM 138 OD1 ASP A 18 -2.460 2.380 -9.020 1.00119.13 O ANISOU 138 OD1 ASP A 18 18094 13261 13908 187 -44 3508 O ATOM 139 OD2 ASP A 18 -4.611 2.816 -9.105 1.00121.28 O1- ANISOU 139 OD2 ASP A 18 18361 13398 14322 676 -532 3595 O1- ATOM 140 N ALA A 19 -2.360 -2.664 -8.184 1.00 66.81 N ANISOU 140 N ALA A 19 10874 7697 6812 197 -2 2470 N ATOM 141 CA ALA A 19 -2.494 -3.950 -7.511 1.00 62.10 C ANISOU 141 CA ALA A 19 10081 7267 6248 232 -18 2167 C ATOM 142 C ALA A 19 -2.256 -3.789 -6.016 1.00 58.49 C ANISOU 142 C ALA A 19 9464 6604 6154 191 66 2010 C ATOM 143 O ALA A 19 -1.123 -3.609 -5.574 1.00 57.77 O ANISOU 143 O ALA A 19 9329 6459 6160 -14 306 1969 O ATOM 144 CB ALA A 19 -1.525 -4.962 -8.101 1.00 59.36 C ANISOU 144 CB ALA A 19 9711 7210 5635 72 187 2055 C ATOM 145 N PRO A 20 -3.335 -3.849 -5.244 1.00 76.65 N ANISOU 145 N PRO A 20 11656 8809 8657 385 -135 1905 N ATOM 146 CA PRO A 20 -3.277 -3.635 -3.795 1.00 73.71 C ANISOU 146 CA PRO A 20 11140 8250 8617 372 -77 1751 C ATOM 147 C PRO A 20 -2.149 -4.401 -3.114 1.00 70.60 C ANISOU 147 C PRO A 20 10635 7953 8237 180 156 1578 C ATOM 148 O PRO A 20 -1.862 -5.541 -3.474 1.00 69.53 O ANISOU 148 O PRO A 20 10456 8057 7907 149 205 1487 O ATOM 149 CB PRO A 20 -4.625 -4.172 -3.321 1.00 72.23 C ANISOU 149 CB PRO A 20 10808 8102 8533 613 -311 1608 C ATOM 150 CG PRO A 20 -4.942 -5.258 -4.291 1.00 72.36 C ANISOU 150 CG PRO A 20 10836 8404 8254 669 -420 1580 C ATOM 151 CD PRO A 20 -4.366 -4.834 -5.616 1.00 75.88 C ANISOU 151 CD PRO A 20 11490 8921 8422 570 -361 1797 C ATOM 152 N GLU A 21 -1.523 -3.768 -2.128 1.00 55.16 N ANISOU 152 N GLU A 21 8619 5814 6525 59 287 1516 N ATOM 153 CA GLU A 21 -0.494 -4.403 -1.340 1.00 52.86 C ANISOU 153 CA GLU A 21 8182 5605 6296 -108 479 1338 C ATOM 154 C GLU A 21 -1.015 -4.742 0.039 1.00 50.94 C ANISOU 154 C GLU A 21 7794 5300 6261 -16 422 1150 C ATOM 155 O GLU A 21 -0.557 -5.680 0.657 1.00 49.67 O ANISOU 155 O GLU A 21 7470 5289 6115 -76 495 984 O ATOM 156 CB GLU A 21 0.728 -3.503 -1.214 1.00 54.32 C ANISOU 156 CB GLU A 21 8370 5672 6596 -338 667 1366 C ATOM 157 CG GLU A 21 1.409 -3.161 -2.518 1.00 57.43 C ANISOU 157 CG GLU A 21 8890 6135 6796 -464 781 1550 C ATOM 158 CD GLU A 21 2.237 -4.299 -3.074 1.00 56.78 C ANISOU 158 CD GLU A 21 8715 6347 6510 -561 932 1458 C ATOM 159 OE1 GLU A 21 2.876 -4.994 -2.286 1.00 54.77 O ANISOU 159 OE1 GLU A 21 8267 6180 6363 -633 1022 1252 O ATOM 160 OE2 GLU A 21 2.240 -4.502 -4.298 1.00 58.80 O1- ANISOU 160 OE2 GLU A 21 9085 6753 6503 -556 952 1580 O1- ATOM 161 N GLU A 22 -1.970 -3.968 0.530 1.00 62.85 N ANISOU 161 N GLU A 22 9313 6617 7948 132 283 1149 N ATOM 162 CA GLU A 22 -2.492 -4.204 1.886 1.00 61.43 C ANISOU 162 CA GLU A 22 8977 6397 7968 217 254 943 C ATOM 163 C GLU A 22 -4.013 -3.925 1.959 1.00 61.62 C ANISOU 163 C GLU A 22 8974 6342 8096 477 47 930 C ATOM 164 O GLU A 22 -4.486 -2.911 1.444 1.00 63.53 O ANISOU 164 O GLU A 22 9302 6429 8409 557 -59 1053 O ATOM 165 CB GLU A 22 -1.726 -3.307 2.868 1.00 61.50 C ANISOU 165 CB GLU A 22 8958 6225 8183 64 377 838 C ATOM 166 CG GLU A 22 -1.839 -3.620 4.347 1.00 60.45 C ANISOU 166 CG GLU A 22 8633 6147 8190 67 392 577 C ATOM 167 CD GLU A 22 -0.987 -2.655 5.187 1.00 61.10 C ANISOU 167 CD GLU A 22 8727 6039 8451 -97 503 465 C ATOM 168 OE1 GLU A 22 0.202 -2.455 4.855 1.00 61.81 O ANISOU 168 OE1 GLU A 22 8829 6143 8511 -300 607 508 O ATOM 169 OE2 GLU A 22 -1.500 -2.076 6.167 1.00 61.31 O1- ANISOU 169 OE2 GLU A 22 8705 5955 8636 -29 467 297 O1- ATOM 170 N GLU A 23 -4.783 -4.816 2.582 1.00 47.48 N ANISOU 170 N GLU A 23 6968 4726 6346 573 -21 747 N ATOM 171 CA GLU A 23 -6.210 -4.543 2.804 1.00 47.75 C ANISOU 171 CA GLU A 23 6909 4698 6535 806 -183 681 C ATOM 172 C GLU A 23 -6.514 -4.560 4.301 1.00 46.58 C ANISOU 172 C GLU A 23 6567 4554 6578 799 -96 432 C ATOM 173 O GLU A 23 -6.478 -5.628 4.914 1.00 45.22 O ANISOU 173 O GLU A 23 6232 4598 6352 724 -32 299 O ATOM 174 CB GLU A 23 -7.104 -5.572 2.086 1.00 47.83 C ANISOU 174 CB GLU A 23 6811 4932 6429 928 -347 671 C ATOM 175 CG GLU A 23 -6.822 -5.741 0.591 1.00 49.11 C ANISOU 175 CG GLU A 23 7168 5166 6327 932 -440 880 C ATOM 176 CD GLU A 23 -7.866 -6.618 -0.142 1.00 49.77 C ANISOU 176 CD GLU A 23 7139 5455 6316 1080 -656 829 C ATOM 177 OE1 GLU A 23 -8.573 -7.425 0.515 1.00 48.74 O ANISOU 177 OE1 GLU A 23 6749 5449 6319 1106 -676 621 O ATOM 178 OE2 GLU A 23 -7.978 -6.501 -1.387 1.00 51.28 O1- ANISOU 178 OE2 GLU A 23 7468 5712 6304 1120 -781 977 O1- ATOM 179 N ASP A 24 -6.826 -3.399 4.884 1.00 47.74 N ANISOU 179 N ASP A 24 6744 4457 6937 880 -88 368 N ATOM 180 CA ASP A 24 -7.140 -3.316 6.322 1.00 47.21 C ANISOU 180 CA ASP A 24 6512 4408 7018 876 14 103 C ATOM 181 C ASP A 24 -5.999 -3.825 7.217 1.00 45.54 C ANISOU 181 C ASP A 24 6273 4333 6695 642 175 1 C ATOM 182 O ASP A 24 -6.250 -4.490 8.208 1.00 44.56 O ANISOU 182 O ASP A 24 6001 4388 6543 613 242 -168 O ATOM 183 CB ASP A 24 -8.419 -4.110 6.662 1.00 47.01 C ANISOU 183 CB ASP A 24 6246 4576 7039 1010 -34 -41 C ATOM 184 CG ASP A 24 -9.710 -3.359 6.307 1.00 49.43 C ANISOU 184 CG ASP A 24 6500 4824 7456 1222 -148 -46 C ATOM 185 OD1 ASP A 24 -10.776 -4.015 6.205 1.00 49.69 O ANISOU 185 OD1 ASP A 24 6333 5031 7517 1311 -213 -116 O ATOM 186 OD2 ASP A 24 -9.673 -2.116 6.145 1.00 51.78 O1- ANISOU 186 OD2 ASP A 24 6940 4899 7834 1286 -163 13 O1- ATOM 187 N HIS A 25 -4.758 -3.517 6.856 1.00 37.00 N ANISOU 187 N HIS A 25 5333 3175 5550 476 232 109 N ATOM 188 CA HIS A 25 -3.572 -3.964 7.592 1.00 36.32 C ANISOU 188 CA HIS A 25 5201 3221 5377 269 342 14 C ATOM 189 C HIS A 25 -3.156 -5.400 7.289 1.00 35.18 C ANISOU 189 C HIS A 25 4974 3349 5042 204 342 68 C ATOM 190 O HIS A 25 -2.169 -5.906 7.823 1.00 34.88 O ANISOU 190 O HIS A 25 4883 3435 4936 65 399 4 O ATOM 191 CB HIS A 25 -3.722 -3.700 9.092 1.00 36.52 C ANISOU 191 CB HIS A 25 5136 3266 5476 254 400 -242 C ATOM 192 CG HIS A 25 -4.154 -2.301 9.392 1.00 38.30 C ANISOU 192 CG HIS A 25 5431 3201 5920 333 406 -344 C ATOM 193 CD2 HIS A 25 -3.651 -1.114 8.985 1.00 39.98 C ANISOU 193 CD2 HIS A 25 5783 3167 6240 277 389 -275 C ATOM 194 ND1 HIS A 25 -5.272 -2.018 10.138 1.00 39.19 N ANISOU 194 ND1 HIS A 25 5449 3326 6117 482 399 -522 N ATOM 195 CE1 HIS A 25 -5.428 -0.701 10.203 1.00 41.38 C ANISOU 195 CE1 HIS A 25 5810 3385 6526 529 362 -565 C ATOM 196 NE2 HIS A 25 -4.460 -0.134 9.512 1.00 42.09 N ANISOU 196 NE2 HIS A 25 6050 3302 6640 406 347 -413 N ATOM 197 N VAL A 26 -3.916 -6.052 6.425 1.00 22.83 N ANISOU 197 N VAL A 26 3394 1870 3411 317 258 168 N ATOM 198 CA VAL A 26 -3.604 -7.415 6.020 1.00 22.07 C ANISOU 198 CA VAL A 26 3229 1992 3165 269 252 201 C ATOM 199 C VAL A 26 -2.827 -7.417 4.717 1.00 22.82 C ANISOU 199 C VAL A 26 3445 2086 3139 206 262 359 C ATOM 200 O VAL A 26 -3.277 -6.879 3.722 1.00 23.90 O ANISOU 200 O VAL A 26 3708 2133 3242 288 194 495 O ATOM 201 CB VAL A 26 -4.881 -8.261 5.848 1.00 21.52 C ANISOU 201 CB VAL A 26 3045 2035 3095 400 161 170 C ATOM 202 CG1 VAL A 26 -4.515 -9.685 5.458 1.00 20.77 C ANISOU 202 CG1 VAL A 26 2889 2121 2880 339 159 179 C ATOM 203 CG2 VAL A 26 -5.695 -8.233 7.126 1.00 20.74 C ANISOU 203 CG2 VAL A 26 2821 1953 3106 442 202 12 C ATOM 204 N LEU A 27 -1.654 -8.022 4.723 1.00 25.78 N ANISOU 204 N LEU A 27 3781 2571 3442 67 348 339 N ATOM 205 CA LEU A 27 -0.847 -8.074 3.516 1.00 26.69 C ANISOU 205 CA LEU A 27 3989 2720 3432 -13 409 456 C ATOM 206 C LEU A 27 -1.452 -9.018 2.468 1.00 26.91 C ANISOU 206 C LEU A 27 4027 2891 3308 83 326 499 C ATOM 207 O LEU A 27 -1.826 -10.153 2.764 1.00 26.31 O ANISOU 207 O LEU A 27 3819 2943 3234 130 274 396 O ATOM 208 CB LEU A 27 0.603 -8.457 3.855 1.00 26.65 C ANISOU 208 CB LEU A 27 3887 2805 3436 -177 530 376 C ATOM 209 CG LEU A 27 1.353 -7.568 4.866 1.00 26.92 C ANISOU 209 CG LEU A 27 3886 2727 3616 -299 593 292 C ATOM 210 CD1 LEU A 27 2.828 -7.948 4.936 1.00 27.28 C ANISOU 210 CD1 LEU A 27 3804 2882 3677 -454 690 214 C ATOM 211 CD2 LEU A 27 1.214 -6.103 4.530 1.00 27.66 C ANISOU 211 CD2 LEU A 27 4149 2572 3788 -340 635 396 C ATOM 212 N VAL A 28 -1.571 -8.520 1.247 1.00 20.57 N ANISOU 212 N VAL A 28 3396 2053 2366 107 309 653 N ATOM 213 CA VAL A 28 -2.020 -9.320 0.123 1.00 21.37 C ANISOU 213 CA VAL A 28 3532 2311 2275 184 223 676 C ATOM 214 C VAL A 28 -0.821 -10.006 -0.517 1.00 21.77 C ANISOU 214 C VAL A 28 3577 2515 2180 51 376 642 C ATOM 215 O VAL A 28 0.126 -9.346 -0.954 1.00 22.37 O ANISOU 215 O VAL A 28 3761 2552 2186 -81 534 740 O ATOM 216 CB VAL A 28 -2.631 -8.442 -0.948 1.00 22.83 C ANISOU 216 CB VAL A 28 3939 2415 2320 278 119 873 C ATOM 217 CG1 VAL A 28 -3.089 -9.294 -2.127 1.00 23.82 C ANISOU 217 CG1 VAL A 28 4105 2743 2204 356 2 865 C ATOM 218 CG2 VAL A 28 -3.769 -7.613 -0.365 1.00 22.88 C ANISOU 218 CG2 VAL A 28 3939 2240 2516 436 -33 898 C ATOM 219 N LEU A 29 -0.852 -11.329 -0.568 1.00 30.86 N ANISOU 219 N LEU A 29 4592 3825 3310 78 346 491 N ATOM 220 CA LEU A 29 0.283 -12.072 -1.090 1.00 31.06 C ANISOU 220 CA LEU A 29 4569 3991 3243 -20 494 405 C ATOM 221 C LEU A 29 -0.136 -12.816 -2.328 1.00 32.29 C ANISOU 221 C LEU A 29 4791 4302 3176 45 432 361 C ATOM 222 O LEU A 29 -1.279 -13.300 -2.420 1.00 32.67 O ANISOU 222 O LEU A 29 4813 4372 3227 165 245 310 O ATOM 223 CB LEU A 29 0.834 -13.060 -0.055 1.00 29.61 C ANISOU 223 CB LEU A 29 4164 3835 3250 -39 519 237 C ATOM 224 CG LEU A 29 1.403 -12.453 1.236 1.00 28.68 C ANISOU 224 CG LEU A 29 3966 3612 3317 -109 563 239 C ATOM 225 CD1 LEU A 29 1.957 -13.574 2.130 1.00 27.35 C ANISOU 225 CD1 LEU A 29 3609 3499 3285 -99 547 98 C ATOM 226 CD2 LEU A 29 2.476 -11.396 0.901 1.00 29.24 C ANISOU 226 CD2 LEU A 29 4101 3642 3366 -259 733 312 C ATOM 227 N ARG A 30 0.794 -12.884 -3.275 1.00 45.31 N ANISOU 227 N ARG A 30 6512 6071 4631 -47 600 357 N ATOM 228 CA ARG A 30 0.592 -13.604 -4.512 1.00 46.54 C ANISOU 228 CA ARG A 30 6744 6412 4527 -5 575 274 C ATOM 229 C ARG A 30 1.827 -14.444 -4.729 1.00 46.36 C ANISOU 229 C ARG A 30 6589 6517 4510 -93 785 86 C ATOM 230 O ARG A 30 2.801 -14.315 -3.986 1.00 45.55 O ANISOU 230 O ARG A 30 6346 6357 4603 -181 927 58 O ATOM 231 CB ARG A 30 0.494 -12.626 -5.678 1.00 48.17 C ANISOU 231 CB ARG A 30 7239 6663 4402 -30 605 490 C ATOM 232 CG ARG A 30 -0.440 -11.491 -5.476 1.00 48.64 C ANISOU 232 CG ARG A 30 7447 6547 4488 54 433 720 C ATOM 233 CD ARG A 30 -0.168 -10.413 -6.507 1.00 50.39 C ANISOU 233 CD ARG A 30 7898 6764 4483 -16 498 961 C ATOM 234 NE ARG A 30 -1.020 -9.248 -6.280 1.00 50.98 N ANISOU 234 NE ARG A 30 8084 6624 4661 78 321 1172 N ATOM 235 CZ ARG A 30 -0.717 -8.248 -5.454 1.00 50.58 C ANISOU 235 CZ ARG A 30 8026 6336 4858 13 397 1275 C ATOM 236 NH1 ARG A 30 0.427 -8.258 -4.774 1.00 49.74 N1+ ANISOU 236 NH1 ARG A 30 7798 6191 4909 -157 631 1192 N1+ ATOM 237 NH2 ARG A 30 -1.560 -7.235 -5.308 1.00 51.34 N ANISOU 237 NH2 ARG A 30 8208 6233 5065 125 226 1430 N ATOM 238 N LYS A 31 1.792 -15.302 -5.743 1.00 71.21 N ANISOU 238 N LYS A 31 9763 9842 7454 -59 792 -72 N ATOM 239 CA LYS A 31 2.925 -16.166 -6.055 1.00 71.31 C ANISOU 239 CA LYS A 31 9633 9980 7481 -113 998 -299 C ATOM 240 C LYS A 31 4.102 -15.358 -6.592 1.00 72.48 C ANISOU 240 C LYS A 31 9818 10185 7534 -244 1250 -191 C ATOM 241 O LYS A 31 5.151 -15.913 -6.917 1.00 73.42 O ANISOU 241 O LYS A 31 9788 10382 7725 -265 1403 -349 O ATOM 242 CB LYS A 31 2.519 -17.239 -7.066 1.00 72.29 C ANISOU 242 CB LYS A 31 9785 10271 7412 -35 934 -527 C ATOM 243 CG LYS A 31 3.622 -18.231 -7.396 1.00 73.29 C ANISOU 243 CG LYS A 31 9742 10447 7657 -33 1096 -770 C ATOM 244 CD LYS A 31 3.151 -19.266 -8.404 1.00 74.93 C ANISOU 244 CD LYS A 31 9999 10748 7724 46 1004 -992 C ATOM 245 CE LYS A 31 2.904 -18.638 -9.766 1.00 77.86 C ANISOU 245 CE LYS A 31 10646 11265 7671 30 1027 -878 C ATOM 246 NZ LYS A 31 4.160 -18.117 -10.373 1.00 80.31 N1+ ANISOU 246 NZ LYS A 31 10977 11660 7877 -44 1305 -800 N1+ ATOM 247 N SER A 32 3.919 -14.044 -6.682 1.00 53.24 N ANISOU 247 N SER A 32 7553 7670 5007 -310 1253 85 N ATOM 248 CA SER A 32 4.965 -13.158 -7.179 1.00 55.26 C ANISOU 248 CA SER A 32 7822 7941 5233 -443 1457 215 C ATOM 249 C SER A 32 5.550 -12.310 -6.054 1.00 53.96 C ANISOU 249 C SER A 32 7551 7587 5365 -558 1515 301 C ATOM 250 O SER A 32 6.524 -11.585 -6.253 1.00 55.77 O ANISOU 250 O SER A 32 7745 7800 5645 -695 1685 370 O ATOM 251 CB SER A 32 4.419 -12.256 -8.288 1.00 57.98 C ANISOU 251 CB SER A 32 8439 8331 5258 -446 1418 464 C ATOM 252 OG SER A 32 4.186 -12.992 -9.476 1.00 60.33 O ANISOU 252 OG SER A 32 8817 8855 5252 -360 1405 358 O ATOM 253 N ASN A 33 4.949 -12.407 -4.873 1.00 45.06 N ANISOU 253 N ASN A 33 6373 6319 4428 -504 1375 282 N ATOM 254 CA ASN A 33 5.409 -11.652 -3.714 1.00 44.31 C ANISOU 254 CA ASN A 33 6176 6051 4608 -593 1398 327 C ATOM 255 C ASN A 33 5.316 -12.462 -2.425 1.00 42.60 C ANISOU 255 C ASN A 33 5762 5797 4625 -527 1311 160 C ATOM 256 O ASN A 33 5.226 -11.901 -1.333 1.00 41.87 O ANISOU 256 O ASN A 33 5621 5557 4730 -538 1227 201 O ATOM 257 CB ASN A 33 4.618 -10.350 -3.575 1.00 44.34 C ANISOU 257 CB ASN A 33 6401 5856 4590 -600 1304 574 C ATOM 258 CG ASN A 33 3.309 -10.539 -2.833 1.00 43.13 C ANISOU 258 CG ASN A 33 6310 5595 4485 -446 1090 595 C ATOM 259 ND2 ASN A 33 2.803 -9.464 -2.241 1.00 43.02 N ANISOU 259 ND2 ASN A 33 6391 5365 4589 -436 1009 737 N ATOM 260 OD1 ASN A 33 2.759 -11.640 -2.793 1.00 42.28 O ANISOU 260 OD1 ASN A 33 6105 5590 4371 -314 952 454 O ATOM 261 N PHE A 34 5.425 -13.770 -2.534 1.00 33.31 N ANISOU 261 N PHE A 34 4440 4744 3474 -429 1274 -37 N ATOM 262 CA PHE A 34 5.284 -14.638 -1.384 1.00 31.87 C ANISOU 262 CA PHE A 34 4070 4504 3536 -316 1105 -158 C ATOM 263 C PHE A 34 6.583 -14.871 -0.650 1.00 31.60 C ANISOU 263 C PHE A 34 3785 4491 3731 -369 1185 -292 C ATOM 264 O PHE A 34 6.637 -14.752 0.547 1.00 30.79 O ANISOU 264 O PHE A 34 3592 4299 3807 -350 1066 -283 O ATOM 265 CB PHE A 34 4.696 -15.985 -1.788 1.00 31.41 C ANISOU 265 CB PHE A 34 3984 4507 3442 -176 996 -300 C ATOM 266 CG PHE A 34 4.345 -16.869 -0.632 1.00 29.92 C ANISOU 266 CG PHE A 34 3665 4219 3486 -68 819 -363 C ATOM 267 CD1 PHE A 34 3.197 -16.663 0.071 1.00 29.23 C ANISOU 267 CD1 PHE A 34 3651 4022 3433 -19 656 -254 C ATOM 268 CD2 PHE A 34 5.171 -17.903 -0.256 1.00 29.22 C ANISOU 268 CD2 PHE A 34 3381 4140 3582 -14 825 -526 C ATOM 269 CE1 PHE A 34 2.869 -17.468 1.127 1.00 28.12 C ANISOU 269 CE1 PHE A 34 3417 3795 3471 53 530 -285 C ATOM 270 CE2 PHE A 34 4.857 -18.709 0.800 1.00 28.15 C ANISOU 270 CE2 PHE A 34 3170 3891 3635 81 663 -536 C ATOM 271 CZ PHE A 34 3.698 -18.497 1.491 1.00 27.56 C ANISOU 271 CZ PHE A 34 3195 3718 3556 99 529 -406 C ATOM 272 N ALA A 35 7.622 -15.228 -1.379 1.00 37.83 N ANISOU 272 N ALA A 35 4458 5402 4513 -411 1342 -418 N ATOM 273 CA ALA A 35 8.859 -15.640 -0.761 1.00 37.70 C ANISOU 273 CA ALA A 35 4177 5405 4743 -404 1338 -564 C ATOM 274 C ALA A 35 9.619 -14.446 -0.239 1.00 38.35 C ANISOU 274 C ALA A 35 4207 5439 4926 -559 1395 -497 C ATOM 275 O ALA A 35 10.368 -14.538 0.709 1.00 38.27 O ANISOU 275 O ALA A 35 3995 5416 5128 -554 1318 -591 O ATOM 276 CB ALA A 35 9.691 -16.413 -1.748 1.00 38.79 C ANISOU 276 CB ALA A 35 4217 5659 4860 -374 1444 -719 C ATOM 277 N GLU A 36 9.400 -13.323 -0.890 1.00 64.86 N ANISOU 277 N GLU A 36 7757 8759 8127 -689 1509 -334 N ATOM 278 CA GLU A 36 9.915 -12.048 -0.477 1.00 65.59 C ANISOU 278 CA GLU A 36 7853 8755 8313 -848 1561 -254 C ATOM 279 C GLU A 36 9.286 -11.631 0.833 1.00 64.64 C ANISOU 279 C GLU A 36 7749 8500 8313 -832 1405 -216 C ATOM 280 O GLU A 36 9.933 -11.063 1.672 1.00 65.01 O ANISOU 280 O GLU A 36 7673 8496 8532 -916 1377 -274 O ATOM 281 CB GLU A 36 9.587 -11.027 -1.553 1.00 65.80 C ANISOU 281 CB GLU A 36 8133 8736 8132 -953 1689 -51 C ATOM 282 CG GLU A 36 10.391 -9.757 -1.495 1.00 67.84 C ANISOU 282 CG GLU A 36 8384 8899 8492 -1142 1803 14 C ATOM 283 CD GLU A 36 9.531 -8.517 -1.341 1.00 67.74 C ANISOU 283 CD GLU A 36 8619 8679 8442 -1189 1752 229 C ATOM 284 OE1 GLU A 36 8.307 -8.649 -1.128 1.00 66.07 O ANISOU 284 OE1 GLU A 36 8561 8398 8144 -1064 1610 315 O ATOM 285 OE2 GLU A 36 10.091 -7.402 -1.422 1.00 69.91 O1- ANISOU 285 OE2 GLU A 36 8926 8843 8794 -1349 1851 304 O1- ATOM 286 N ALA A 37 8.007 -11.903 1.002 1.00 35.88 N ANISOU 286 N ALA A 37 4255 4806 4570 -727 1307 -133 N ATOM 287 CA ALA A 37 7.338 -11.577 2.237 1.00 35.27 C ANISOU 287 CA ALA A 37 4207 4605 4590 -676 1130 -101 C ATOM 288 C ALA A 37 7.859 -12.424 3.369 1.00 34.99 C ANISOU 288 C ALA A 37 3944 4633 4720 -591 983 -255 C ATOM 289 O ALA A 37 8.037 -11.951 4.470 1.00 35.13 O ANISOU 289 O ALA A 37 3904 4598 4844 -621 885 -290 O ATOM 290 CB ALA A 37 5.856 -11.766 2.094 1.00 34.50 C ANISOU 290 CB ALA A 37 4307 4445 4357 -529 991 16 C ATOM 291 N LEU A 38 8.099 -13.689 3.082 1.00 37.09 N ANISOU 291 N LEU A 38 4092 5003 4998 -475 957 -351 N ATOM 292 CA LEU A 38 8.588 -14.592 4.092 1.00 37.02 C ANISOU 292 CA LEU A 38 3892 5030 5143 -363 792 -462 C ATOM 293 C LEU A 38 10.026 -14.264 4.511 1.00 38.12 C ANISOU 293 C LEU A 38 3773 5246 5466 -458 829 -608 C ATOM 294 O LEU A 38 10.396 -14.433 5.643 1.00 38.48 O ANISOU 294 O LEU A 38 3698 5301 5620 -404 648 -664 O ATOM 295 CB LEU A 38 8.420 -16.041 3.646 1.00 36.21 C ANISOU 295 CB LEU A 38 3747 4965 5047 -201 746 -526 C ATOM 296 CG LEU A 38 7.451 -16.903 4.454 1.00 35.47 C ANISOU 296 CG LEU A 38 3741 4783 4955 -52 540 -456 C ATOM 297 CD1 LEU A 38 6.085 -16.263 4.605 1.00 34.90 C ANISOU 297 CD1 LEU A 38 3889 4628 4742 -78 508 -307 C ATOM 298 CD2 LEU A 38 7.303 -18.274 3.847 1.00 34.78 C ANISOU 298 CD2 LEU A 38 3621 4687 4906 77 521 -535 C ATOM 299 N ALA A 39 10.816 -13.758 3.592 1.00 37.58 N ANISOU 299 N ALA A 39 3672 5218 5390 -585 1017 -640 N ATOM 300 CA ALA A 39 12.155 -13.342 3.913 1.00 38.74 C ANISOU 300 CA ALA A 39 3621 5407 5692 -673 1024 -759 C ATOM 301 C ALA A 39 12.194 -12.027 4.681 1.00 39.42 C ANISOU 301 C ALA A 39 3743 5405 5830 -828 1001 -731 C ATOM 302 O ALA A 39 13.068 -11.809 5.480 1.00 40.23 O ANISOU 302 O ALA A 39 3666 5541 6080 -860 902 -856 O ATOM 303 CB ALA A 39 12.980 -13.248 2.655 1.00 39.57 C ANISOU 303 CB ALA A 39 3693 5576 5764 -759 1239 -798 C ATOM 304 N ALA A 40 11.235 -11.154 4.439 1.00 29.42 N ANISOU 304 N ALA A 40 2718 4013 4447 -912 1076 -578 N ATOM 305 CA ALA A 40 11.187 -9.864 5.139 1.00 29.91 C ANISOU 305 CA ALA A 40 2846 3944 4575 -1050 1055 -564 C ATOM 306 C ALA A 40 10.537 -9.894 6.530 1.00 29.68 C ANISOU 306 C ALA A 40 2811 3884 4583 -991 850 -613 C ATOM 307 O ALA A 40 10.809 -9.017 7.353 1.00 30.33 O ANISOU 307 O ALA A 40 2873 3901 4752 -1087 784 -694 O ATOM 308 CB ALA A 40 10.507 -8.824 4.272 1.00 29.77 C ANISOU 308 CB ALA A 40 3102 3767 4441 -1146 1204 -374 C ATOM 309 N HIS A 41 9.678 -10.886 6.787 1.00 36.75 N ANISOU 309 N HIS A 41 3788 4816 5361 -790 711 -547 N ATOM 310 CA HIS A 41 8.952 -10.964 8.067 1.00 36.90 C ANISOU 310 CA HIS A 41 3893 4809 5318 -681 498 -540 C ATOM 311 C HIS A 41 9.221 -12.258 8.804 1.00 37.00 C ANISOU 311 C HIS A 41 3783 4949 5328 -511 301 -586 C ATOM 312 O HIS A 41 8.730 -13.312 8.406 1.00 36.26 O ANISOU 312 O HIS A 41 3736 4865 5175 -374 284 -505 O ATOM 313 CB HIS A 41 7.429 -10.869 7.889 1.00 36.02 C ANISOU 313 CB HIS A 41 4040 4589 5057 -593 502 -382 C ATOM 314 CG HIS A 41 6.951 -9.632 7.178 1.00 35.76 C ANISOU 314 CG HIS A 41 4176 4395 5017 -702 649 -293 C ATOM 315 CD2 HIS A 41 6.408 -8.484 7.658 1.00 35.97 C ANISOU 315 CD2 HIS A 41 4331 4266 5072 -753 645 -288 C ATOM 316 ND1 HIS A 41 6.923 -9.531 5.812 1.00 35.41 N ANISOU 316 ND1 HIS A 41 4211 4323 4920 -745 807 -184 N ATOM 317 CE1 HIS A 41 6.414 -8.353 5.465 1.00 35.48 C ANISOU 317 CE1 HIS A 41 4402 4154 4925 -817 882 -79 C ATOM 318 NE2 HIS A 41 6.094 -7.708 6.565 1.00 35.69 N ANISOU 318 NE2 HIS A 41 4450 4083 5026 -817 787 -150 N ATOM 319 N LYS A 42 9.938 -12.180 9.912 1.00 28.67 N ANISOU 319 N LYS A 42 2590 3972 4330 -515 132 -709 N ATOM 320 CA LYS A 42 10.203 -13.366 10.703 1.00 28.98 C ANISOU 320 CA LYS A 42 2547 4112 4350 -336 -92 -713 C ATOM 321 C LYS A 42 8.968 -13.970 11.400 1.00 28.79 C ANISOU 321 C LYS A 42 2756 4048 4134 -205 -194 -556 C ATOM 322 O LYS A 42 9.022 -15.094 11.859 1.00 28.80 O ANISOU 322 O LYS A 42 2747 4085 4111 -54 -345 -495 O ATOM 323 CB LYS A 42 11.268 -13.067 11.736 1.00 30.17 C ANISOU 323 CB LYS A 42 2505 4380 4579 -366 -287 -882 C ATOM 324 CG LYS A 42 10.867 -11.977 12.680 1.00 31.05 C ANISOU 324 CG LYS A 42 2744 4469 4584 -471 -339 -938 C ATOM 325 CD LYS A 42 11.893 -11.843 13.798 1.00 32.60 C ANISOU 325 CD LYS A 42 2752 4817 4817 -477 -592 -1126 C ATOM 326 CE LYS A 42 11.978 -13.135 14.615 1.00 33.08 C ANISOU 326 CE LYS A 42 2820 4993 4754 -244 -864 -1036 C ATOM 327 NZ LYS A 42 12.603 -12.902 15.956 1.00 34.50 N1+ ANISOU 327 NZ LYS A 42 2929 5335 4844 -226 -1162 -1180 N1+ ATOM 328 N TYR A 43 7.891 -13.210 11.568 1.00 37.73 N ANISOU 328 N TYR A 43 4087 5099 5150 -264 -113 -497 N ATOM 329 CA TYR A 43 6.674 -13.807 12.104 1.00 37.80 C ANISOU 329 CA TYR A 43 4280 5080 5001 -163 -152 -362 C ATOM 330 C TYR A 43 5.502 -13.450 11.233 1.00 36.86 C ANISOU 330 C TYR A 43 4296 4847 4862 -186 16 -280 C ATOM 331 O TYR A 43 4.965 -12.351 11.373 1.00 36.38 O ANISOU 331 O TYR A 43 4323 4723 4777 -257 85 -310 O ATOM 332 CB TYR A 43 6.365 -13.232 13.485 1.00 38.79 C ANISOU 332 CB TYR A 43 4502 5258 4977 -187 -246 -409 C ATOM 333 CG TYR A 43 7.439 -13.437 14.523 1.00 40.03 C ANISOU 333 CG TYR A 43 4553 5557 5099 -160 -465 -502 C ATOM 334 CD1 TYR A 43 8.005 -14.687 14.735 1.00 40.39 C ANISOU 334 CD1 TYR A 43 4529 5664 5154 -21 -630 -424 C ATOM 335 CD2 TYR A 43 7.892 -12.371 15.290 1.00 40.89 C ANISOU 335 CD2 TYR A 43 4631 5729 5178 -262 -531 -680 C ATOM 336 CE1 TYR A 43 8.986 -14.869 15.691 1.00 41.58 C ANISOU 336 CE1 TYR A 43 4579 5953 5267 34 -879 -500 C ATOM 337 CE2 TYR A 43 8.877 -12.541 16.241 1.00 42.09 C ANISOU 337 CE2 TYR A 43 4673 6038 5283 -232 -773 -788 C ATOM 338 CZ TYR A 43 9.425 -13.793 16.445 1.00 42.42 C ANISOU 338 CZ TYR A 43 4644 6158 5316 -74 -960 -686 C ATOM 339 OH TYR A 43 10.413 -13.960 17.413 1.00 43.75 O ANISOU 339 OH TYR A 43 4700 6493 5430 -13 -1251 -786 O ATOM 340 N LEU A 44 5.013 -14.407 10.447 1.00 28.26 N ANISOU 340 N LEU A 44 3228 3725 3784 -108 54 -188 N ATOM 341 CA LEU A 44 3.964 -14.095 9.468 1.00 26.08 C ANISOU 341 CA LEU A 44 3053 3365 3490 -117 176 -127 C ATOM 342 C LEU A 44 2.852 -15.145 9.495 1.00 24.31 C ANISOU 342 C LEU A 44 2896 3115 3226 -28 153 -40 C ATOM 343 O LEU A 44 3.094 -16.311 9.211 1.00 23.76 O ANISOU 343 O LEU A 44 2778 3047 3202 35 113 -22 O ATOM 344 CB LEU A 44 4.558 -13.967 8.046 1.00 24.99 C ANISOU 344 CB LEU A 44 2862 3223 3411 -160 285 -147 C ATOM 345 CG LEU A 44 3.668 -13.325 6.962 1.00 23.73 C ANISOU 345 CG LEU A 44 2830 2990 3196 -180 385 -75 C ATOM 346 CD1 LEU A 44 3.434 -11.863 7.256 1.00 24.33 C ANISOU 346 CD1 LEU A 44 2992 2972 3280 -258 426 -65 C ATOM 347 CD2 LEU A 44 4.257 -13.465 5.575 1.00 23.34 C ANISOU 347 CD2 LEU A 44 2756 2979 3133 -215 495 -81 C ATOM 348 N LEU A 45 1.643 -14.733 9.864 1.00 19.39 N ANISOU 348 N LEU A 45 2365 2454 2547 -28 185 -6 N ATOM 349 CA LEU A 45 0.501 -15.636 9.764 1.00 17.68 C ANISOU 349 CA LEU A 45 2179 2208 2329 21 193 57 C ATOM 350 C LEU A 45 -0.142 -15.450 8.396 1.00 16.13 C ANISOU 350 C LEU A 45 1990 1971 2169 38 236 53 C ATOM 351 O LEU A 45 -0.418 -14.327 8.000 1.00 16.07 O ANISOU 351 O LEU A 45 2024 1933 2150 24 271 45 O ATOM 352 CB LEU A 45 -0.512 -15.346 10.865 1.00 17.98 C ANISOU 352 CB LEU A 45 2276 2256 2300 9 225 69 C ATOM 353 CG LEU A 45 -1.581 -16.413 11.139 1.00 17.85 C ANISOU 353 CG LEU A 45 2268 2220 2293 19 255 136 C ATOM 354 CD1 LEU A 45 -0.991 -17.727 11.587 1.00 18.18 C ANISOU 354 CD1 LEU A 45 2326 2249 2332 34 189 223 C ATOM 355 CD2 LEU A 45 -2.561 -15.927 12.171 1.00 17.83 C ANISOU 355 CD2 LEU A 45 2302 2255 2217 -12 340 118 C ATOM 356 N VAL A 46 -0.355 -16.540 7.663 1.00 29.22 N ANISOU 356 N VAL A 46 3618 3619 3867 74 218 55 N ATOM 357 CA VAL A 46 -0.965 -16.447 6.337 1.00 28.89 C ANISOU 357 CA VAL A 46 3588 3572 3815 98 225 34 C ATOM 358 C VAL A 46 -2.278 -17.227 6.262 1.00 28.72 C ANISOU 358 C VAL A 46 3540 3523 3848 123 194 22 C ATOM 359 O VAL A 46 -2.335 -18.426 6.580 1.00 29.00 O ANISOU 359 O VAL A 46 3540 3522 3956 117 179 18 O ATOM 360 CB VAL A 46 -0.023 -16.944 5.183 1.00 29.44 C ANISOU 360 CB VAL A 46 3634 3683 3870 104 241 -20 C ATOM 361 CG1 VAL A 46 -0.683 -16.705 3.832 1.00 30.22 C ANISOU 361 CG1 VAL A 46 3787 3811 3884 126 236 -36 C ATOM 362 CG2 VAL A 46 1.348 -16.264 5.232 1.00 30.02 C ANISOU 362 CG2 VAL A 46 3683 3794 3928 53 300 -31 C ATOM 363 N GLU A 47 -3.323 -16.529 5.833 1.00 28.71 N ANISOU 363 N GLU A 47 3547 3524 3838 150 176 15 N ATOM 364 CA GLU A 47 -4.612 -17.150 5.624 1.00 29.11 C ANISOU 364 CA GLU A 47 3525 3567 3968 166 137 -32 C ATOM 365 C GLU A 47 -4.884 -17.457 4.143 1.00 30.24 C ANISOU 365 C GLU A 47 3664 3750 4076 208 48 -98 C ATOM 366 O GLU A 47 -4.784 -16.572 3.284 1.00 30.93 O ANISOU 366 O GLU A 47 3826 3874 4051 255 9 -72 O ATOM 367 CB GLU A 47 -5.710 -16.257 6.145 1.00 29.09 C ANISOU 367 CB GLU A 47 3486 3560 4008 193 149 -35 C ATOM 368 CG GLU A 47 -7.066 -16.899 5.950 1.00 30.24 C ANISOU 368 CG GLU A 47 3501 3715 4274 196 113 -112 C ATOM 369 CD GLU A 47 -8.192 -15.886 5.764 1.00 30.84 C ANISOU 369 CD GLU A 47 3505 3806 4408 284 62 -157 C ATOM 370 OE1 GLU A 47 -9.369 -16.321 5.576 1.00 31.52 O ANISOU 370 OE1 GLU A 47 3434 3918 4624 293 19 -250 O ATOM 371 OE2 GLU A 47 -7.887 -14.664 5.780 1.00 30.64 O1- ANISOU 371 OE2 GLU A 47 3566 3750 4326 348 56 -109 O1- ATOM 372 N PHE A 48 -5.208 -18.718 3.863 1.00 24.84 N ANISOU 372 N PHE A 48 2912 3049 3477 185 17 -183 N ATOM 373 CA PHE A 48 -5.572 -19.149 2.526 1.00 26.30 C ANISOU 373 CA PHE A 48 3082 3289 3621 218 -82 -297 C ATOM 374 C PHE A 48 -7.076 -19.301 2.489 1.00 27.41 C ANISOU 374 C PHE A 48 3099 3435 3880 222 -167 -374 C ATOM 375 O PHE A 48 -7.660 -20.080 3.254 1.00 27.57 O ANISOU 375 O PHE A 48 3015 3383 4076 148 -118 -405 O ATOM 376 CB PHE A 48 -4.931 -20.493 2.187 1.00 26.52 C ANISOU 376 CB PHE A 48 3094 3276 3706 188 -69 -400 C ATOM 377 CG PHE A 48 -3.411 -20.488 2.221 1.00 25.57 C ANISOU 377 CG PHE A 48 3036 3160 3519 196 14 -366 C ATOM 378 CD1 PHE A 48 -2.729 -20.712 3.410 1.00 24.53 C ANISOU 378 CD1 PHE A 48 2895 2948 3476 176 74 -277 C ATOM 379 CD2 PHE A 48 -2.668 -20.293 1.060 1.00 26.56 C ANISOU 379 CD2 PHE A 48 3218 3387 3487 223 30 -433 C ATOM 380 CE1 PHE A 48 -1.327 -20.733 3.445 1.00 24.18 C ANISOU 380 CE1 PHE A 48 2858 2921 3409 196 122 -275 C ATOM 381 CE2 PHE A 48 -1.261 -20.308 1.093 1.00 26.06 C ANISOU 381 CE2 PHE A 48 3158 3341 3401 221 129 -434 C ATOM 382 CZ PHE A 48 -0.604 -20.529 2.285 1.00 24.72 C ANISOU 382 CZ PHE A 48 2940 3087 3366 214 161 -365 C ATOM 383 N TYR A 49 -7.716 -18.544 1.606 1.00 27.51 N ANISOU 383 N TYR A 49 3118 3531 3802 307 -295 -396 N ATOM 384 CA TYR A 49 -9.170 -18.512 1.608 1.00 28.09 C ANISOU 384 CA TYR A 49 3028 3629 4018 336 -399 -485 C ATOM 385 C TYR A 49 -9.740 -18.600 0.191 1.00 29.86 C ANISOU 385 C TYR A 49 3236 3965 4145 414 -615 -604 C ATOM 386 O TYR A 49 -8.992 -18.616 -0.784 1.00 30.84 O ANISOU 386 O TYR A 49 3511 4157 4051 442 -658 -601 O ATOM 387 CB TYR A 49 -9.635 -17.208 2.258 1.00 27.33 C ANISOU 387 CB TYR A 49 2920 3515 3950 410 -381 -389 C ATOM 388 CG TYR A 49 -9.322 -15.972 1.436 1.00 27.93 C ANISOU 388 CG TYR A 49 3156 3617 3840 535 -483 -282 C ATOM 389 CD1 TYR A 49 -10.297 -15.389 0.618 1.00 29.19 C ANISOU 389 CD1 TYR A 49 3275 3830 3985 675 -692 -308 C ATOM 390 CD2 TYR A 49 -8.050 -15.378 1.474 1.00 27.62 C ANISOU 390 CD2 TYR A 49 3307 3538 3648 510 -377 -147 C ATOM 391 CE1 TYR A 49 -10.010 -14.243 -0.145 1.00 30.05 C ANISOU 391 CE1 TYR A 49 3578 3929 3911 793 -790 -160 C ATOM 392 CE2 TYR A 49 -7.763 -14.245 0.733 1.00 28.52 C ANISOU 392 CE2 TYR A 49 3589 3643 3605 592 -439 -22 C ATOM 393 CZ TYR A 49 -8.738 -13.683 -0.076 1.00 29.82 C ANISOU 393 CZ TYR A 49 3759 3837 3736 735 -643 -8 C ATOM 394 OH TYR A 49 -8.447 -12.565 -0.819 1.00 30.74 O ANISOU 394 OH TYR A 49 4085 3913 3684 817 -709 162 O ATOM 395 N ALA A 50 -11.065 -18.642 0.088 1.00 28.30 N ANISOU 395 N ALA A 50 2847 3807 4099 448 -750 -722 N ATOM 396 CA ALA A 50 -11.737 -18.411 -1.189 1.00 29.71 C ANISOU 396 CA ALA A 50 3008 4119 4162 566 -1016 -817 C ATOM 397 C ALA A 50 -12.911 -17.470 -0.953 1.00 29.62 C ANISOU 397 C ALA A 50 2841 4126 4287 695 -1144 -809 C ATOM 398 O ALA A 50 -13.569 -17.535 0.081 1.00 28.95 O ANISOU 398 O ALA A 50 2556 3981 4461 642 -1030 -855 O ATOM 399 CB ALA A 50 -12.204 -19.723 -1.810 1.00 30.75 C ANISOU 399 CB ALA A 50 3002 4301 4379 484 -1122 -1067 C ATOM 400 N PRO A 51 -13.213 -16.635 -1.914 1.00 31.08 N ANISOU 400 N PRO A 51 3111 4395 4301 870 -1381 -758 N ATOM 401 CA PRO A 51 -14.294 -15.674 -1.753 1.00 31.51 C ANISOU 401 CA PRO A 51 3059 4425 4488 1002 -1478 -727 C ATOM 402 C PRO A 51 -15.693 -16.249 -1.536 1.00 32.99 C ANISOU 402 C PRO A 51 2954 4639 4942 945 -1501 -931 C ATOM 403 O PRO A 51 -16.458 -15.593 -0.901 1.00 33.87 O ANISOU 403 O PRO A 51 2941 4701 5227 997 -1456 -926 O ATOM 404 CB PRO A 51 -14.219 -14.874 -3.035 1.00 33.19 C ANISOU 404 CB PRO A 51 3500 4700 4411 1155 -1696 -593 C ATOM 405 CG PRO A 51 -12.811 -14.973 -3.419 1.00 32.83 C ANISOU 405 CG PRO A 51 3722 4678 4076 1118 -1633 -476 C ATOM 406 CD PRO A 51 -12.468 -16.382 -3.141 1.00 32.27 C ANISOU 406 CD PRO A 51 3538 4635 4089 933 -1495 -664 C ATOM 407 N TRP A 52 -15.993 -17.445 -2.014 1.00 29.51 N ANISOU 407 N TRP A 52 2411 4262 4538 833 -1550 -1118 N ATOM 408 CA TRP A 52 -17.307 -18.035 -1.847 1.00 31.86 C ANISOU 408 CA TRP A 52 2439 4572 5092 764 -1562 -1314 C ATOM 409 C TRP A 52 -17.475 -18.899 -0.643 1.00 30.75 C ANISOU 409 C TRP A 52 2134 4334 5214 559 -1292 -1391 C ATOM 410 O TRP A 52 -18.524 -19.469 -0.430 1.00 32.88 O ANISOU 410 O TRP A 52 2190 4601 5701 471 -1260 -1546 O ATOM 411 CB TRP A 52 -17.698 -18.840 -3.067 1.00 34.46 C ANISOU 411 CB TRP A 52 2744 5007 5342 754 -1767 -1488 C ATOM 412 CG TRP A 52 -16.547 -19.423 -3.830 1.00 33.36 C ANISOU 412 CG TRP A 52 2822 4911 4943 716 -1795 -1486 C ATOM 413 CD1 TRP A 52 -16.053 -19.003 -5.036 1.00 34.46 C ANISOU 413 CD1 TRP A 52 3190 5170 4732 836 -1979 -1415 C ATOM 414 CD2 TRP A 52 -15.714 -20.560 -3.466 1.00 31.43 C ANISOU 414 CD2 TRP A 52 2601 4587 4753 540 -1616 -1561 C ATOM 415 CE2 TRP A 52 -14.754 -20.713 -4.537 1.00 31.49 C ANISOU 415 CE2 TRP A 52 2842 4690 4433 582 -1709 -1562 C ATOM 416 CE3 TRP A 52 -15.666 -21.422 -2.403 1.00 30.11 C ANISOU 416 CE3 TRP A 52 2311 4274 4855 359 -1385 -1608 C ATOM 417 NE1 TRP A 52 -15.014 -19.769 -5.431 1.00 33.35 N ANISOU 417 NE1 TRP A 52 3197 5051 4422 748 -1911 -1466 N ATOM 418 CZ2 TRP A 52 -13.796 -21.694 -4.520 1.00 30.22 C ANISOU 418 CZ2 TRP A 52 2756 4472 4252 459 -1579 -1647 C ATOM 419 CZ3 TRP A 52 -14.699 -22.404 -2.404 1.00 28.88 C ANISOU 419 CZ3 TRP A 52 2249 4039 4683 240 -1278 -1656 C ATOM 420 CH2 TRP A 52 -13.794 -22.540 -3.442 1.00 28.92 C ANISOU 420 CH2 TRP A 52 2451 4132 4405 296 -1378 -1695 C ATOM 421 N CYS A 53 -16.442 -19.030 0.153 1.00 37.34 N ANISOU 421 N CYS A 53 3075 5086 6024 473 -1090 -1273 N ATOM 422 CA CYS A 53 -16.506 -19.796 1.370 1.00 36.57 C ANISOU 422 CA CYS A 53 2879 4886 6132 276 -814 -1285 C ATOM 423 C CYS A 53 -17.138 -18.969 2.458 1.00 36.80 C ANISOU 423 C CYS A 53 2811 4899 6272 297 -658 -1230 C ATOM 424 O CYS A 53 -16.767 -17.847 2.658 1.00 35.71 O ANISOU 424 O CYS A 53 2770 4765 6031 432 -667 -1110 O ATOM 425 CB CYS A 53 -15.096 -20.201 1.779 1.00 34.84 C ANISOU 425 CB CYS A 53 2824 4591 5825 195 -678 -1167 C ATOM 426 SG CYS A 53 -14.911 -20.876 3.420 1.00 34.58 S ANISOU 426 SG CYS A 53 2765 4419 5957 -19 -326 -1075 S ATOM 427 N GLY A 54 -18.103 -19.534 3.159 1.00 31.88 N ANISOU 427 N GLY A 54 2004 4252 5856 159 -504 -1328 N ATOM 428 CA GLY A 54 -18.811 -18.795 4.187 1.00 32.73 C ANISOU 428 CA GLY A 54 2005 4370 6060 172 -343 -1318 C ATOM 429 C GLY A 54 -17.957 -18.591 5.423 1.00 30.39 C ANISOU 429 C GLY A 54 1847 4018 5682 99 -82 -1160 C ATOM 430 O GLY A 54 -18.044 -17.558 6.087 1.00 30.32 O ANISOU 430 O GLY A 54 1850 4026 5643 186 0 -1119 O ATOM 431 N HIS A 55 -17.126 -19.581 5.731 1.00 40.83 N ANISOU 431 N HIS A 55 3280 5265 6968 -57 42 -1080 N ATOM 432 CA HIS A 55 -16.243 -19.506 6.878 1.00 39.12 C ANISOU 432 CA HIS A 55 3214 5001 6647 -132 272 -918 C ATOM 433 C HIS A 55 -15.300 -18.346 6.750 1.00 37.71 C ANISOU 433 C HIS A 55 3180 4843 6305 40 198 -824 C ATOM 434 O HIS A 55 -15.001 -17.651 7.745 1.00 37.16 O ANISOU 434 O HIS A 55 3186 4776 6156 52 358 -752 O ATOM 435 CB HIS A 55 -15.459 -20.803 7.036 1.00 38.94 C ANISOU 435 CB HIS A 55 3303 4869 6624 -301 362 -832 C ATOM 436 CG HIS A 55 -16.324 -22.005 7.332 1.00 40.96 C ANISOU 436 CG HIS A 55 3461 5058 7046 -489 476 -891 C ATOM 437 CD2 HIS A 55 -16.811 -23.010 6.499 1.00 42.70 C ANISOU 437 CD2 HIS A 55 3587 5221 7417 -559 366 -1023 C ATOM 438 ND1 HIS A 55 -16.778 -22.282 8.567 1.00 42.40 N ANISOU 438 ND1 HIS A 55 3643 5226 7243 -630 728 -816 N ATOM 439 CE1 HIS A 55 -17.518 -23.406 8.531 1.00 44.94 C ANISOU 439 CE1 HIS A 55 3870 5473 7733 -787 785 -878 C ATOM 440 NE2 HIS A 55 -17.538 -23.851 7.264 1.00 45.23 N ANISOU 440 NE2 HIS A 55 3844 5476 7867 -742 563 -1015 N ATOM 441 N CYS A 56 -14.819 -18.115 5.533 1.00 42.11 N ANISOU 441 N CYS A 56 3795 5414 6790 172 -43 -829 N ATOM 442 CA CYS A 56 -13.902 -17.012 5.269 1.00 41.25 C ANISOU 442 CA CYS A 56 3882 5296 6497 331 -123 -710 C ATOM 443 C CYS A 56 -14.614 -15.670 5.397 1.00 41.43 C ANISOU 443 C CYS A 56 3842 5333 6564 495 -173 -739 C ATOM 444 O CYS A 56 -14.156 -14.780 6.114 1.00 40.72 O ANISOU 444 O CYS A 56 3853 5198 6421 545 -64 -673 O ATOM 445 CB CYS A 56 -13.286 -17.150 3.875 1.00 41.59 C ANISOU 445 CB CYS A 56 4072 5355 6376 407 -347 -681 C ATOM 446 SG CYS A 56 -11.996 -18.411 3.751 1.00 41.83 S ANISOU 446 SG CYS A 56 4287 5327 6280 257 -267 -615 S ATOM 447 N LYS A 57 -15.736 -15.532 4.698 1.00 37.76 N ANISOU 447 N LYS A 57 3240 4917 6188 571 -342 -842 N ATOM 448 CA LYS A 57 -16.519 -14.303 4.743 1.00 39.40 C ANISOU 448 CA LYS A 57 3397 5117 6455 732 -409 -866 C ATOM 449 C LYS A 57 -16.778 -13.878 6.184 1.00 39.54 C ANISOU 449 C LYS A 57 3361 5115 6547 674 -147 -899 C ATOM 450 O LYS A 57 -16.746 -12.690 6.507 1.00 39.90 O ANISOU 450 O LYS A 57 3469 5107 6586 800 -138 -875 O ATOM 451 CB LYS A 57 -17.844 -14.484 4.001 1.00 42.39 C ANISOU 451 CB LYS A 57 3576 5565 6965 785 -590 -1007 C ATOM 452 CG LYS A 57 -17.712 -14.480 2.486 1.00 43.30 C ANISOU 452 CG LYS A 57 3781 5720 6953 907 -898 -976 C ATOM 453 CD LYS A 57 -19.022 -14.866 1.817 1.00 46.69 C ANISOU 453 CD LYS A 57 3994 6233 7514 932 -1071 -1148 C ATOM 454 CE LYS A 57 -18.898 -14.835 0.303 1.00 47.88 C ANISOU 454 CE LYS A 57 4261 6447 7483 1057 -1383 -1118 C ATOM 455 NZ LYS A 57 -18.667 -13.456 -0.208 1.00 48.65 N1+ ANISOU 455 NZ LYS A 57 4541 6499 7443 1276 -1540 -942 N1+ ATOM 456 N ALA A 58 -17.035 -14.856 7.046 1.00 37.12 N ANISOU 456 N ALA A 58 2961 4846 6299 475 68 -952 N ATOM 457 CA ALA A 58 -17.287 -14.589 8.453 1.00 37.73 C ANISOU 457 CA ALA A 58 3011 4938 6388 395 334 -982 C ATOM 458 C ALA A 58 -16.012 -14.173 9.186 1.00 35.48 C ANISOU 458 C ALA A 58 2948 4610 5923 381 462 -864 C ATOM 459 O ALA A 58 -16.051 -13.331 10.104 1.00 36.10 O ANISOU 459 O ALA A 58 3061 4689 5965 413 593 -899 O ATOM 460 CB ALA A 58 -17.908 -15.815 9.120 1.00 38.95 C ANISOU 460 CB ALA A 58 3044 5136 6620 173 530 -1032 C ATOM 461 N LEU A 59 -14.887 -14.780 8.792 1.00 36.75 N ANISOU 461 N LEU A 59 3250 4736 5978 331 424 -748 N ATOM 462 CA LEU A 59 -13.629 -14.654 9.538 1.00 35.43 C ANISOU 462 CA LEU A 59 3276 4538 5646 281 560 -643 C ATOM 463 C LEU A 59 -12.870 -13.369 9.222 1.00 34.72 C ANISOU 463 C LEU A 59 3349 4370 5471 438 450 -598 C ATOM 464 O LEU A 59 -12.148 -12.824 10.084 1.00 34.24 O ANISOU 464 O LEU A 59 3438 4289 5284 409 562 -568 O ATOM 465 CB LEU A 59 -12.735 -15.866 9.280 1.00 35.09 C ANISOU 465 CB LEU A 59 3365 4468 5498 150 545 -512 C ATOM 466 CG LEU A 59 -11.344 -15.815 9.903 1.00 34.52 C ANISOU 466 CG LEU A 59 3550 4366 5201 101 600 -368 C ATOM 467 CD1 LEU A 59 -11.422 -15.896 11.430 1.00 35.05 C ANISOU 467 CD1 LEU A 59 3647 4488 5183 -11 834 -359 C ATOM 468 CD2 LEU A 59 -10.441 -16.922 9.339 1.00 34.44 C ANISOU 468 CD2 LEU A 59 3653 4307 5125 34 517 -258 C ATOM 469 N ALA A 60 -13.054 -12.890 7.990 1.00 36.55 N ANISOU 469 N ALA A 60 3572 4556 5757 592 219 -587 N ATOM 470 CA ALA A 60 -12.319 -11.727 7.482 1.00 36.41 C ANISOU 470 CA ALA A 60 3754 4427 5651 717 101 -493 C ATOM 471 C ALA A 60 -12.248 -10.526 8.441 1.00 36.73 C ANISOU 471 C ALA A 60 3839 4386 5732 774 219 -556 C ATOM 472 O ALA A 60 -11.166 -10.026 8.730 1.00 36.11 O ANISOU 472 O ALA A 60 3961 4235 5525 726 261 -480 O ATOM 473 CB ALA A 60 -12.856 -11.308 6.116 1.00 37.27 C ANISOU 473 CB ALA A 60 3835 4506 5819 896 -161 -470 C ATOM 474 N PRO A 61 -13.398 -10.065 8.957 1.00 33.75 N ANISOU 474 N PRO A 61 3311 4039 5475 826 266 -684 N ATOM 475 CA PRO A 61 -13.339 -8.868 9.805 1.00 34.64 C ANISOU 475 CA PRO A 61 3490 4069 5601 877 359 -759 C ATOM 476 C PRO A 61 -12.605 -9.064 11.130 1.00 33.88 C ANISOU 476 C PRO A 61 3476 4031 5366 725 583 -810 C ATOM 477 O PRO A 61 -11.990 -8.120 11.629 1.00 34.07 O ANISOU 477 O PRO A 61 3632 3962 5351 744 620 -850 O ATOM 478 CB PRO A 61 -14.813 -8.546 10.053 1.00 37.38 C ANISOU 478 CB PRO A 61 3629 4467 6106 951 370 -898 C ATOM 479 CG PRO A 61 -15.530 -9.185 8.883 1.00 38.00 C ANISOU 479 CG PRO A 61 3577 4596 6266 1001 182 -858 C ATOM 480 CD PRO A 61 -14.786 -10.465 8.672 1.00 35.54 C ANISOU 480 CD PRO A 61 3311 4355 5837 849 211 -773 C ATOM 481 N GLU A 62 -12.668 -10.256 11.707 1.00 38.11 N ANISOU 481 N GLU A 62 3952 4711 5817 567 723 -804 N ATOM 482 CA GLU A 62 -11.886 -10.497 12.912 1.00 37.65 C ANISOU 482 CA GLU A 62 4017 4725 5563 427 904 -809 C ATOM 483 C GLU A 62 -10.402 -10.610 12.575 1.00 35.91 C ANISOU 483 C GLU A 62 4006 4445 5193 378 812 -663 C ATOM 484 O GLU A 62 -9.543 -10.199 13.356 1.00 35.92 O ANISOU 484 O GLU A 62 4149 4453 5047 320 860 -682 O ATOM 485 CB GLU A 62 -12.354 -11.750 13.636 1.00 38.28 C ANISOU 485 CB GLU A 62 4030 4955 5559 261 1065 -780 C ATOM 486 CG GLU A 62 -13.782 -11.675 14.175 1.00 40.82 C ANISOU 486 CG GLU A 62 4173 5354 5981 255 1170 -904 C ATOM 487 CD GLU A 62 -13.936 -10.711 15.356 1.00 43.08 C ANISOU 487 CD GLU A 62 4503 5684 6181 274 1302 -1043 C ATOM 488 OE1 GLU A 62 -15.081 -10.257 15.614 1.00 45.60 O ANISOU 488 OE1 GLU A 62 4662 6031 6633 329 1361 -1183 O ATOM 489 OE2 GLU A 62 -12.921 -10.412 16.034 1.00 42.56 O1- ANISOU 489 OE2 GLU A 62 4623 5631 5917 233 1342 -1032 O1- ATOM 490 N TYR A 63 -10.098 -11.171 11.412 1.00 26.18 N ANISOU 490 N TYR A 63 2796 3174 3979 388 655 -524 N ATOM 491 CA TYR A 63 -8.703 -11.308 11.013 1.00 25.48 C ANISOU 491 CA TYR A 63 2887 3046 3750 332 564 -385 C ATOM 492 C TYR A 63 -8.122 -9.882 10.872 1.00 25.70 C ANISOU 492 C TYR A 63 3027 2938 3801 400 515 -412 C ATOM 493 O TYR A 63 -6.997 -9.577 11.326 1.00 25.61 O ANISOU 493 O TYR A 63 3137 2911 3682 321 531 -399 O ATOM 494 CB TYR A 63 -8.619 -12.141 9.716 1.00 24.81 C ANISOU 494 CB TYR A 63 2788 2956 3682 342 430 -276 C ATOM 495 CG TYR A 63 -7.246 -12.692 9.352 1.00 24.00 C ANISOU 495 CG TYR A 63 2816 2855 3447 265 382 -158 C ATOM 496 CD1 TYR A 63 -6.706 -13.794 10.004 1.00 24.02 C ANISOU 496 CD1 TYR A 63 2839 2921 3366 162 436 -111 C ATOM 497 CD2 TYR A 63 -6.500 -12.125 8.316 1.00 23.88 C ANISOU 497 CD2 TYR A 63 2901 2773 3400 302 287 -90 C ATOM 498 CE1 TYR A 63 -5.447 -14.293 9.655 1.00 23.55 C ANISOU 498 CE1 TYR A 63 2861 2859 3229 124 379 -33 C ATOM 499 CE2 TYR A 63 -5.255 -12.620 7.966 1.00 23.50 C ANISOU 499 CE2 TYR A 63 2928 2744 3255 232 272 -20 C ATOM 500 CZ TYR A 63 -4.724 -13.698 8.646 1.00 23.11 C ANISOU 500 CZ TYR A 63 2861 2760 3158 156 310 -8 C ATOM 501 OH TYR A 63 -3.473 -14.179 8.269 1.00 23.02 O ANISOU 501 OH TYR A 63 2888 2765 3092 116 283 35 O ATOM 502 N ALA A 64 -8.934 -9.007 10.290 1.00 23.41 N ANISOU 502 N ALA A 64 2682 2536 3675 547 448 -459 N ATOM 503 CA ALA A 64 -8.568 -7.614 10.083 1.00 24.13 C ANISOU 503 CA ALA A 64 2889 2436 3844 623 401 -471 C ATOM 504 C ALA A 64 -8.371 -6.913 11.421 1.00 24.85 C ANISOU 504 C ALA A 64 3000 2510 3930 580 537 -649 C ATOM 505 O ALA A 64 -7.385 -6.186 11.623 1.00 24.95 O ANISOU 505 O ALA A 64 3149 2417 3914 517 537 -658 O ATOM 506 CB ALA A 64 -9.636 -6.894 9.253 1.00 25.13 C ANISOU 506 CB ALA A 64 2948 2433 4167 828 276 -476 C ATOM 507 N LYS A 65 -9.317 -7.142 12.329 1.00 38.61 N ANISOU 507 N LYS A 65 4601 4370 5701 600 666 -812 N ATOM 508 CA LYS A 65 -9.289 -6.525 13.646 1.00 39.83 C ANISOU 508 CA LYS A 65 4776 4561 5795 559 799 -1004 C ATOM 509 C LYS A 65 -7.995 -6.876 14.364 1.00 39.20 C ANISOU 509 C LYS A 65 4837 4571 5487 394 838 -988 C ATOM 510 O LYS A 65 -7.302 -5.993 14.887 1.00 40.18 O ANISOU 510 O LYS A 65 5059 4617 5591 359 842 -1108 O ATOM 511 CB LYS A 65 -10.498 -6.966 14.452 1.00 41.05 C ANISOU 511 CB LYS A 65 4775 4896 5925 551 925 -1101 C ATOM 512 CG LYS A 65 -10.579 -6.346 15.814 1.00 43.22 C ANISOU 512 CG LYS A 65 5083 5243 6096 509 1054 -1283 C ATOM 513 CD LYS A 65 -11.918 -6.617 16.501 1.00 45.47 C ANISOU 513 CD LYS A 65 5205 5675 6397 514 1194 -1381 C ATOM 514 CE LYS A 65 -11.807 -6.241 17.982 1.00 47.78 C ANISOU 514 CE LYS A 65 5567 6088 6498 441 1346 -1545 C ATOM 515 NZ LYS A 65 -12.895 -6.806 18.876 1.00 50.28 N1+ ANISOU 515 NZ LYS A 65 5767 6600 6740 382 1541 -1610 N1+ ATOM 516 N ALA A 66 -7.668 -8.164 14.388 1.00 24.06 N ANISOU 516 N ALA A 66 2925 2812 3404 292 835 -837 N ATOM 517 CA ALA A 66 -6.442 -8.630 15.024 1.00 24.14 C ANISOU 517 CA ALA A 66 3055 2926 3193 160 812 -783 C ATOM 518 C ALA A 66 -5.225 -7.942 14.417 1.00 24.06 C ANISOU 518 C ALA A 66 3135 2776 3230 135 686 -743 C ATOM 519 O ALA A 66 -4.288 -7.574 15.126 1.00 24.90 O ANISOU 519 O ALA A 66 3312 2913 3236 53 666 -829 O ATOM 520 CB ALA A 66 -6.319 -10.140 14.897 1.00 23.59 C ANISOU 520 CB ALA A 66 2975 2980 3008 93 797 -597 C ATOM 521 N ALA A 67 -5.248 -7.768 13.099 1.00 21.66 N ANISOU 521 N ALA A 67 2827 2332 3072 193 603 -619 N ATOM 522 CA ALA A 67 -4.158 -7.105 12.395 1.00 21.77 C ANISOU 522 CA ALA A 67 2927 2204 3139 146 528 -557 C ATOM 523 C ALA A 67 -4.067 -5.639 12.802 1.00 22.79 C ANISOU 523 C ALA A 67 3114 2149 3395 152 555 -719 C ATOM 524 O ALA A 67 -2.977 -5.115 13.035 1.00 23.39 O ANISOU 524 O ALA A 67 3248 2171 3470 39 540 -773 O ATOM 525 CB ALA A 67 -4.343 -7.230 10.891 1.00 21.04 C ANISOU 525 CB ALA A 67 2848 2020 3125 209 456 -378 C ATOM 526 N GLY A 68 -5.219 -4.983 12.888 1.00 25.33 N ANISOU 526 N GLY A 68 3400 2366 3859 287 592 -821 N ATOM 527 CA GLY A 68 -5.274 -3.589 13.286 1.00 27.05 C ANISOU 527 CA GLY A 68 3669 2366 4241 322 621 -1004 C ATOM 528 C GLY A 68 -4.745 -3.383 14.691 1.00 28.08 C ANISOU 528 C GLY A 68 3813 2611 4246 212 690 -1244 C ATOM 529 O GLY A 68 -3.980 -2.453 14.947 1.00 29.11 O ANISOU 529 O GLY A 68 4011 2617 4433 130 657 -1334 O ATOM 530 N LYS A 69 -5.154 -4.257 15.604 1.00 32.25 N ANISOU 530 N LYS A 69 4279 3405 4569 197 766 -1313 N ATOM 531 CA LYS A 69 -4.702 -4.187 16.988 1.00 33.56 C ANISOU 531 CA LYS A 69 4480 3748 4525 99 802 -1499 C ATOM 532 C LYS A 69 -3.204 -4.449 17.078 1.00 33.36 C ANISOU 532 C LYS A 69 4517 3779 4378 -51 698 -1466 C ATOM 533 O LYS A 69 -2.504 -3.841 17.889 1.00 34.92 O ANISOU 533 O LYS A 69 4755 4000 4514 -135 664 -1658 O ATOM 534 CB LYS A 69 -5.466 -5.191 17.854 1.00 33.77 C ANISOU 534 CB LYS A 69 4459 4051 4319 102 910 -1498 C ATOM 535 CG LYS A 69 -6.956 -4.909 17.964 1.00 34.79 C ANISOU 535 CG LYS A 69 4479 4171 4568 224 1008 -1548 C ATOM 536 CD LYS A 69 -7.712 -6.128 18.467 1.00 34.76 C ANISOU 536 CD LYS A 69 4412 4408 4388 192 1129 -1469 C ATOM 537 CE LYS A 69 -8.666 -5.760 19.592 1.00 37.42 C ANISOU 537 CE LYS A 69 4701 4859 4655 212 1268 -1632 C ATOM 538 NZ LYS A 69 -9.202 -6.966 20.281 1.00 38.27 N1+ ANISOU 538 NZ LYS A 69 4792 5203 4545 131 1405 -1535 N1+ ATOM 539 N LEU A 70 -2.717 -5.358 16.239 1.00 23.23 N ANISOU 539 N LEU A 70 3217 2539 3071 -77 621 -1208 N ATOM 540 CA LEU A 70 -1.298 -5.689 16.208 1.00 23.68 C ANISOU 540 CA LEU A 70 3281 2665 3052 -197 507 -1152 C ATOM 541 C LEU A 70 -0.475 -4.494 15.740 1.00 24.25 C ANISOU 541 C LEU A 70 3371 2507 3335 -282 476 -1237 C ATOM 542 O LEU A 70 0.612 -4.236 16.257 1.00 25.19 O ANISOU 542 O LEU A 70 3474 2676 3423 -404 405 -1366 O ATOM 543 CB LEU A 70 -1.048 -6.891 15.296 1.00 22.61 C ANISOU 543 CB LEU A 70 3106 2597 2890 -184 456 -887 C ATOM 544 CG LEU A 70 -1.275 -8.271 15.916 1.00 22.63 C ANISOU 544 CG LEU A 70 3100 2825 2673 -165 446 -788 C ATOM 545 CD1 LEU A 70 -0.929 -9.371 14.924 1.00 21.61 C ANISOU 545 CD1 LEU A 70 2928 2707 2576 -150 388 -568 C ATOM 546 CD2 LEU A 70 -0.466 -8.424 17.196 1.00 23.89 C ANISOU 546 CD2 LEU A 70 3297 3166 2613 -232 366 -897 C ATOM 547 N LYS A 71 -1.003 -3.768 14.760 1.00 36.07 N ANISOU 547 N LYS A 71 4902 3748 5053 -221 522 -1161 N ATOM 548 CA LYS A 71 -0.327 -2.587 14.234 1.00 36.93 C ANISOU 548 CA LYS A 71 5064 3583 5386 -314 524 -1197 C ATOM 549 C LYS A 71 -0.326 -1.452 15.252 1.00 38.94 C ANISOU 549 C LYS A 71 5339 3751 5705 -341 528 -1466 C ATOM 550 O LYS A 71 0.685 -0.774 15.438 1.00 40.22 O ANISOU 550 O LYS A 71 5494 3846 5940 -482 487 -1550 O ATOM 551 CB LYS A 71 -0.989 -2.127 12.934 1.00 36.60 C ANISOU 551 CB LYS A 71 5095 3288 5523 -213 549 -991 C ATOM 552 CG LYS A 71 -0.307 -0.937 12.278 1.00 38.24 C ANISOU 552 CG LYS A 71 5388 3218 5923 -315 553 -930 C ATOM 553 CD LYS A 71 -0.866 -0.677 10.889 1.00 38.62 C ANISOU 553 CD LYS A 71 5540 3081 6051 -212 542 -652 C ATOM 554 CE LYS A 71 -1.516 0.695 10.803 1.00 40.99 C ANISOU 554 CE LYS A 71 5937 3120 6519 -109 499 -661 C ATOM 555 NZ LYS A 71 -0.784 1.707 11.613 1.00 43.47 N1+ ANISOU 555 NZ LYS A 71 6257 3326 6933 -245 514 -860 N1+ ATOM 556 N ALA A 72 -1.464 -1.250 15.907 1.00 34.07 N ANISOU 556 N ALA A 72 4721 3175 5049 -200 568 -1574 N ATOM 557 CA ALA A 72 -1.597 -0.195 16.905 1.00 36.58 C ANISOU 557 CA ALA A 72 5054 3450 5395 -197 571 -1808 C ATOM 558 C ALA A 72 -0.617 -0.397 18.057 1.00 37.62 C ANISOU 558 C ALA A 72 5165 3805 5325 -336 514 -1998 C ATOM 559 O ALA A 72 -0.369 0.519 18.841 1.00 40.38 O ANISOU 559 O ALA A 72 5531 4111 5700 -378 493 -2205 O ATOM 560 CB ALA A 72 -3.025 -0.134 17.425 1.00 37.27 C ANISOU 560 CB ALA A 72 5115 3596 5449 -26 649 -1891 C ATOM 561 N GLU A 73 -0.064 -1.602 18.153 1.00 63.49 N ANISOU 561 N GLU A 73 8407 7320 8396 -396 468 -1926 N ATOM 562 CA GLU A 73 0.887 -1.926 19.209 1.00 64.50 C ANISOU 562 CA GLU A 73 8515 7694 8299 -499 359 -2068 C ATOM 563 C GLU A 73 2.317 -1.936 18.680 1.00 64.48 C ANISOU 563 C GLU A 73 8437 7654 8407 -650 250 -2031 C ATOM 564 O GLU A 73 3.258 -2.243 19.413 1.00 65.43 O ANISOU 564 O GLU A 73 8505 7978 8379 -727 115 -2130 O ATOM 565 CB GLU A 73 0.549 -3.280 19.837 1.00 63.95 C ANISOU 565 CB GLU A 73 8462 7944 7892 -449 353 -2003 C ATOM 566 CG GLU A 73 1.463 -3.676 20.986 1.00 65.84 C ANISOU 566 CG GLU A 73 8710 8456 7850 -517 199 -2104 C ATOM 567 CD GLU A 73 1.151 -5.057 21.528 1.00 65.78 C ANISOU 567 CD GLU A 73 8758 8740 7497 -464 185 -1960 C ATOM 568 OE1 GLU A 73 0.595 -5.882 20.773 1.00 63.91 O ANISOU 568 OE1 GLU A 73 8512 8490 7280 -414 267 -1758 O ATOM 569 OE2 GLU A 73 1.463 -5.318 22.709 1.00 67.60 O1- ANISOU 569 OE2 GLU A 73 9055 9195 7436 -470 87 -2018 O1- ATOM 570 N GLY A 74 2.474 -1.598 17.404 1.00 31.11 N ANISOU 570 N GLY A 74 4203 3180 4438 -686 307 -1873 N ATOM 571 CA GLY A 74 3.783 -1.568 16.779 1.00 31.03 C ANISOU 571 CA GLY A 74 4102 3130 4559 -842 256 -1815 C ATOM 572 C GLY A 74 4.488 -2.909 16.845 1.00 30.13 C ANISOU 572 C GLY A 74 3884 3291 4273 -871 155 -1765 C ATOM 573 O GLY A 74 5.715 -2.972 16.921 1.00 30.90 O ANISOU 573 O GLY A 74 3849 3478 4412 -983 56 -1815 O ATOM 574 N SER A 75 3.708 -3.984 16.817 1.00 25.70 N ANISOU 574 N SER A 75 3365 2880 3519 -727 165 -1595 N ATOM 575 CA SER A 75 4.260 -5.335 16.874 1.00 25.80 C ANISOU 575 CA SER A 75 3298 3143 3360 -687 52 -1445 C ATOM 576 C SER A 75 4.984 -5.749 15.576 1.00 25.43 C ANISOU 576 C SER A 75 3150 3035 3478 -729 77 -1256 C ATOM 577 O SER A 75 4.685 -5.241 14.499 1.00 24.61 O ANISOU 577 O SER A 75 3089 2720 3542 -751 208 -1145 O ATOM 578 CB SER A 75 3.141 -6.330 17.189 1.00 25.12 C ANISOU 578 CB SER A 75 3301 3192 3053 -534 85 -1292 C ATOM 579 OG SER A 75 3.617 -7.666 17.177 1.00 25.23 O ANISOU 579 OG SER A 75 3263 3385 2938 -484 -21 -1121 O ATOM 580 N GLU A 76 5.929 -6.682 15.699 1.00 44.51 N ANISOU 580 N GLU A 76 5436 5643 5831 -727 -52 -1223 N ATOM 581 CA GLU A 76 6.694 -7.182 14.560 1.00 44.35 C ANISOU 581 CA GLU A 76 5289 5610 5954 -758 -16 -1092 C ATOM 582 C GLU A 76 5.832 -8.118 13.768 1.00 43.22 C ANISOU 582 C GLU A 76 5225 5457 5741 -622 59 -850 C ATOM 583 O GLU A 76 6.073 -8.329 12.586 1.00 42.82 O ANISOU 583 O GLU A 76 5133 5345 5791 -640 151 -735 O ATOM 584 CB GLU A 76 7.921 -7.981 15.008 1.00 45.48 C ANISOU 584 CB GLU A 76 5240 5965 6077 -752 -199 -1159 C ATOM 585 CG GLU A 76 8.976 -7.170 15.701 1.00 47.05 C ANISOU 585 CG GLU A 76 5293 6211 6372 -899 -313 -1429 C ATOM 586 CD GLU A 76 10.114 -8.032 16.233 1.00 48.26 C ANISOU 586 CD GLU A 76 5237 6601 6499 -847 -551 -1500 C ATOM 587 OE1 GLU A 76 10.110 -8.373 17.447 1.00 49.01 O ANISOU 587 OE1 GLU A 76 5376 6874 6371 -760 -769 -1570 O ATOM 588 OE2 GLU A 76 11.016 -8.356 15.420 1.00 48.48 O1- ANISOU 588 OE2 GLU A 76 5054 6643 6724 -885 -518 -1488 O1- ATOM 589 N ILE A 77 4.853 -8.722 14.434 1.00 30.71 N ANISOU 589 N ILE A 77 3747 3948 3974 -500 24 -789 N ATOM 590 CA ILE A 77 4.054 -9.742 13.767 1.00 29.82 C ANISOU 590 CA ILE A 77 3680 3834 3815 -386 75 -587 C ATOM 591 C ILE A 77 3.120 -9.170 12.705 1.00 28.43 C ANISOU 591 C ILE A 77 3585 3483 3735 -372 217 -503 C ATOM 592 O ILE A 77 2.392 -8.208 12.967 1.00 28.01 O ANISOU 592 O ILE A 77 3614 3319 3711 -375 274 -573 O ATOM 593 CB ILE A 77 3.170 -10.507 14.732 1.00 29.67 C ANISOU 593 CB ILE A 77 3751 3922 3599 -293 38 -534 C ATOM 594 CG1 ILE A 77 3.994 -11.094 15.885 1.00 31.02 C ANISOU 594 CG1 ILE A 77 3896 4274 3615 -280 -137 -577 C ATOM 595 CG2 ILE A 77 2.450 -11.583 13.956 1.00 28.72 C ANISOU 595 CG2 ILE A 77 3648 3776 3490 -207 88 -350 C ATOM 596 CD1 ILE A 77 3.195 -11.303 17.205 1.00 31.02 C ANISOU 596 CD1 ILE A 77 4039 4393 3355 -246 -146 -581 C ATOM 597 N ARG A 78 3.116 -9.785 11.521 1.00 29.73 N ANISOU 597 N ARG A 78 3728 3625 3941 -339 259 -366 N ATOM 598 CA ARG A 78 2.155 -9.396 10.487 1.00 28.29 C ANISOU 598 CA ARG A 78 3635 3311 3802 -296 347 -265 C ATOM 599 C ARG A 78 1.270 -10.540 9.966 1.00 26.95 C ANISOU 599 C ARG A 78 3473 3195 3572 -185 335 -151 C ATOM 600 O ARG A 78 1.630 -11.733 10.017 1.00 27.14 O ANISOU 600 O ARG A 78 3433 3322 3556 -157 288 -120 O ATOM 601 CB ARG A 78 2.842 -8.644 9.349 1.00 28.54 C ANISOU 601 CB ARG A 78 3682 3231 3931 -392 430 -221 C ATOM 602 CG ARG A 78 3.567 -7.379 9.837 1.00 29.71 C ANISOU 602 CG ARG A 78 3827 3269 4193 -532 460 -345 C ATOM 603 CD ARG A 78 3.527 -6.251 8.799 1.00 29.60 C ANISOU 603 CD ARG A 78 3929 3033 4283 -607 573 -250 C ATOM 604 NE ARG A 78 2.157 -5.881 8.471 1.00 28.61 N ANISOU 604 NE ARG A 78 3946 2777 4146 -468 562 -153 N ATOM 605 CZ ARG A 78 1.809 -4.729 7.914 1.00 29.07 C ANISOU 605 CZ ARG A 78 4147 2592 4306 -478 610 -74 C ATOM 606 NH1 ARG A 78 2.750 -3.838 7.621 1.00 30.00 N1+ ANISOU 606 NH1 ARG A 78 4302 2556 4540 -657 704 -69 N1+ ATOM 607 NH2 ARG A 78 0.522 -4.471 7.654 1.00 28.52 N ANISOU 607 NH2 ARG A 78 4173 2420 4243 -310 559 0 N ATOM 608 N LEU A 79 0.085 -10.143 9.506 1.00 26.73 N ANISOU 608 N LEU A 79 3513 3079 3566 -116 364 -105 N ATOM 609 CA LEU A 79 -0.907 -11.058 8.950 1.00 25.32 C ANISOU 609 CA LEU A 79 3322 2937 3362 -25 345 -33 C ATOM 610 C LEU A 79 -1.044 -10.818 7.436 1.00 25.16 C ANISOU 610 C LEU A 79 3353 2856 3349 2 346 57 C ATOM 611 O LEU A 79 -1.037 -9.677 6.948 1.00 25.83 O ANISOU 611 O LEU A 79 3525 2819 3469 -8 369 95 O ATOM 612 CB LEU A 79 -2.266 -10.882 9.643 1.00 24.65 C ANISOU 612 CB LEU A 79 3233 2839 3296 44 358 -78 C ATOM 613 CG LEU A 79 -2.445 -11.491 11.048 1.00 25.24 C ANISOU 613 CG LEU A 79 3278 3019 3292 22 382 -133 C ATOM 614 CD1 LEU A 79 -1.485 -10.909 12.076 1.00 26.61 C ANISOU 614 CD1 LEU A 79 3482 3226 3403 -49 373 -223 C ATOM 615 CD2 LEU A 79 -3.887 -11.399 11.572 1.00 24.82 C ANISOU 615 CD2 LEU A 79 3191 2974 3266 75 449 -189 C ATOM 616 N ALA A 80 -1.176 -11.906 6.693 1.00 21.12 N ANISOU 616 N ALA A 80 2809 2423 2795 37 318 92 N ATOM 617 CA ALA A 80 -1.334 -11.816 5.259 1.00 21.77 C ANISOU 617 CA ALA A 80 2955 2497 2821 67 306 162 C ATOM 618 C ALA A 80 -2.423 -12.775 4.821 1.00 21.30 C ANISOU 618 C ALA A 80 2849 2493 2752 154 228 146 C ATOM 619 O ALA A 80 -2.944 -13.558 5.637 1.00 20.21 O ANISOU 619 O ALA A 80 2623 2383 2673 165 214 93 O ATOM 620 CB ALA A 80 -0.046 -12.167 4.581 1.00 22.84 C ANISOU 620 CB ALA A 80 3082 2696 2900 -12 373 164 C ATOM 621 N LYS A 81 -2.738 -12.726 3.528 1.00 24.97 N ANISOU 621 N LYS A 81 3379 2979 3131 200 178 190 N ATOM 622 CA LYS A 81 -3.728 -13.594 2.951 1.00 25.30 C ANISOU 622 CA LYS A 81 3365 3085 3165 273 77 140 C ATOM 623 C LYS A 81 -3.475 -13.864 1.466 1.00 27.73 C ANISOU 623 C LYS A 81 3756 3476 3305 287 41 153 C ATOM 624 O LYS A 81 -2.880 -13.055 0.745 1.00 28.85 O ANISOU 624 O LYS A 81 4037 3611 3315 263 86 252 O ATOM 625 CB LYS A 81 -5.138 -13.059 3.190 1.00 25.12 C ANISOU 625 CB LYS A 81 3298 3013 3232 372 -16 134 C ATOM 626 CG LYS A 81 -5.471 -11.689 2.571 1.00 26.38 C ANISOU 626 CG LYS A 81 3584 3085 3354 460 -85 239 C ATOM 627 CD LYS A 81 -6.831 -11.235 3.116 1.00 26.39 C ANISOU 627 CD LYS A 81 3476 3030 3519 578 -166 183 C ATOM 628 CE LYS A 81 -7.293 -9.862 2.643 1.00 27.56 C ANISOU 628 CE LYS A 81 3736 3042 3692 711 -265 283 C ATOM 629 NZ LYS A 81 -7.144 -9.721 1.184 1.00 29.43 N1+ ANISOU 629 NZ LYS A 81 4137 3311 3736 760 -385 418 N1+ ATOM 630 N VAL A 82 -3.958 -15.029 1.044 1.00 21.42 N ANISOU 630 N VAL A 82 2877 2754 2509 311 -30 44 N ATOM 631 CA VAL A 82 -3.807 -15.561 -0.282 1.00 23.86 C ANISOU 631 CA VAL A 82 3242 3174 2649 325 -72 -13 C ATOM 632 C VAL A 82 -5.171 -16.066 -0.696 1.00 24.22 C ANISOU 632 C VAL A 82 3212 3262 2729 403 -251 -107 C ATOM 633 O VAL A 82 -5.774 -16.952 -0.047 1.00 22.95 O ANISOU 633 O VAL A 82 2896 3067 2756 385 -274 -216 O ATOM 634 CB VAL A 82 -2.808 -16.735 -0.317 1.00 22.58 C ANISOU 634 CB VAL A 82 3016 3053 2510 262 28 -135 C ATOM 635 CG1 VAL A 82 -2.697 -17.293 -1.743 1.00 23.77 C ANISOU 635 CG1 VAL A 82 3227 3338 2467 279 0 -245 C ATOM 636 CG2 VAL A 82 -1.454 -16.268 0.136 1.00 21.41 C ANISOU 636 CG2 VAL A 82 2884 2883 2368 189 185 -73 C ATOM 637 N ASP A 83 -5.663 -15.494 -1.781 1.00 28.32 N ANISOU 637 N ASP A 83 3841 3854 3065 484 -383 -61 N ATOM 638 CA ASP A 83 -6.905 -15.959 -2.330 1.00 28.95 C ANISOU 638 CA ASP A 83 3831 4008 3162 565 -593 -180 C ATOM 639 C ASP A 83 -6.508 -17.154 -3.211 1.00 29.73 C ANISOU 639 C ASP A 83 3932 4227 3137 518 -597 -360 C ATOM 640 O ASP A 83 -5.853 -17.012 -4.267 1.00 30.33 O ANISOU 640 O ASP A 83 4175 4419 2930 518 -574 -341 O ATOM 641 CB ASP A 83 -7.545 -14.830 -3.135 1.00 29.84 C ANISOU 641 CB ASP A 83 4076 4152 3108 700 -775 -46 C ATOM 642 CG ASP A 83 -8.694 -15.300 -4.013 1.00 30.91 C ANISOU 642 CG ASP A 83 4134 4421 3189 800 -1045 -187 C ATOM 643 OD1 ASP A 83 -9.449 -14.427 -4.477 1.00 31.64 O ANISOU 643 OD1 ASP A 83 4284 4525 3213 948 -1249 -86 O ATOM 644 OD2 ASP A 83 -8.854 -16.518 -4.256 1.00 31.01 O1- ANISOU 644 OD2 ASP A 83 4025 4516 3241 741 -1074 -406 O1- ATOM 645 N ALA A 84 -6.953 -18.329 -2.786 1.00 34.79 N ANISOU 645 N ALA A 84 4391 4834 3995 471 -614 -543 N ATOM 646 CA ALA A 84 -6.506 -19.558 -3.402 1.00 35.17 C ANISOU 646 CA ALA A 84 4420 4933 4009 421 -592 -748 C ATOM 647 C ALA A 84 -7.060 -19.692 -4.794 1.00 36.30 C ANISOU 647 C ALA A 84 4623 5254 3916 482 -787 -886 C ATOM 648 O ALA A 84 -6.458 -20.372 -5.629 1.00 36.63 O ANISOU 648 O ALA A 84 4728 5391 3798 458 -750 -1046 O ATOM 649 CB ALA A 84 -6.907 -20.738 -2.568 1.00 34.57 C ANISOU 649 CB ALA A 84 4158 4723 4256 347 -567 -884 C ATOM 650 N THR A 85 -8.205 -19.065 -5.057 1.00 42.03 N ANISOU 650 N THR A 85 5320 6035 4614 573 -1005 -848 N ATOM 651 CA THR A 85 -8.839 -19.242 -6.368 1.00 43.33 C ANISOU 651 CA THR A 85 5530 6393 4541 647 -1253 -997 C ATOM 652 C THR A 85 -7.964 -18.577 -7.440 1.00 44.21 C ANISOU 652 C THR A 85 5938 6655 4205 683 -1210 -864 C ATOM 653 O THR A 85 -7.914 -19.031 -8.577 1.00 45.51 O ANISOU 653 O THR A 85 6191 6983 4118 680 -1279 -1004 O ATOM 654 CB THR A 85 -10.294 -18.706 -6.438 1.00 43.76 C ANISOU 654 CB THR A 85 5457 6487 4682 767 -1543 -995 C ATOM 655 CG2 THR A 85 -11.137 -19.285 -5.321 1.00 42.80 C ANISOU 655 CG2 THR A 85 5029 6225 5006 700 -1521 -1116 C ATOM 656 OG1 THR A 85 -10.286 -17.280 -6.341 1.00 44.05 O ANISOU 656 OG1 THR A 85 5642 6487 4607 881 -1569 -702 O ATOM 657 N GLU A 86 -7.318 -17.473 -7.097 1.00 46.16 N ANISOU 657 N GLU A 86 6336 6824 4378 688 -1063 -578 N ATOM 658 CA GLU A 86 -6.384 -16.893 -8.024 1.00 46.98 C ANISOU 658 CA GLU A 86 6716 7046 4088 672 -951 -437 C ATOM 659 C GLU A 86 -4.935 -17.257 -7.793 1.00 46.24 C ANISOU 659 C GLU A 86 6641 6929 4000 537 -621 -466 C ATOM 660 O GLU A 86 -4.102 -16.980 -8.637 1.00 46.70 O ANISOU 660 O GLU A 86 6893 7117 3735 492 -479 -410 O ATOM 661 CB GLU A 86 -6.530 -15.388 -8.014 1.00 47.53 C ANISOU 661 CB GLU A 86 6970 7038 4052 748 -998 -101 C ATOM 662 CG GLU A 86 -7.959 -14.952 -8.036 1.00 48.47 C ANISOU 662 CG GLU A 86 7002 7126 4287 897 -1310 -67 C ATOM 663 CD GLU A 86 -8.088 -13.447 -8.046 1.00 49.29 C ANISOU 663 CD GLU A 86 7270 7091 4366 966 -1335 261 C ATOM 664 OE1 GLU A 86 -7.672 -12.821 -9.054 1.00 51.60 O ANISOU 664 OE1 GLU A 86 7797 7440 4369 927 -1297 447 O ATOM 665 OE2 GLU A 86 -8.594 -12.888 -7.036 1.00 48.59 O1- ANISOU 665 OE2 GLU A 86 7066 6828 4570 1046 -1377 324 O1- ATOM 666 N GLU A 87 -4.588 -17.826 -6.640 1.00 47.01 N ANISOU 666 N GLU A 87 6540 6867 4455 473 -488 -540 N ATOM 667 CA GLU A 87 -3.291 -18.480 -6.591 1.00 46.24 C ANISOU 667 CA GLU A 87 6411 6779 4378 381 -239 -653 C ATOM 668 C GLU A 87 -3.425 -19.914 -6.147 1.00 45.46 C ANISOU 668 C GLU A 87 6107 6603 4564 368 -258 -918 C ATOM 669 O GLU A 87 -3.101 -20.231 -5.011 1.00 44.26 O ANISOU 669 O GLU A 87 5823 6283 4710 335 -172 -893 O ATOM 670 CB GLU A 87 -2.433 -17.733 -5.571 1.00 45.21 C ANISOU 670 CB GLU A 87 6264 6506 4406 318 -48 -454 C ATOM 671 CG GLU A 87 -2.522 -16.232 -5.631 1.00 45.72 C ANISOU 671 CG GLU A 87 6503 6536 4331 324 -49 -168 C ATOM 672 CD GLU A 87 -1.734 -15.658 -6.803 1.00 46.93 C ANISOU 672 CD GLU A 87 6884 6836 4113 266 94 -70 C ATOM 673 OE1 GLU A 87 -0.841 -16.379 -7.329 1.00 46.99 O ANISOU 673 OE1 GLU A 87 6866 6973 4016 200 268 -241 O ATOM 674 OE2 GLU A 87 -1.981 -14.477 -7.191 1.00 47.78 O1- ANISOU 674 OE2 GLU A 87 7200 6917 4038 285 52 183 O1- ATOM 675 N SER A 88 -3.672 -20.792 -7.113 1.00 35.31 N ANISOU 675 N SER A 88 4823 5442 3151 385 -342 -1178 N ATOM 676 CA SER A 88 -3.970 -22.184 -6.811 1.00 34.82 C ANISOU 676 CA SER A 88 4580 5268 3382 369 -390 -1448 C ATOM 677 C SER A 88 -2.716 -23.039 -6.690 1.00 34.23 C ANISOU 677 C SER A 88 4447 5130 3428 340 -177 -1603 C ATOM 678 O SER A 88 -2.634 -23.926 -5.851 1.00 33.02 O ANISOU 678 O SER A 88 4151 4771 3625 328 -156 -1677 O ATOM 679 CB SER A 88 -4.957 -22.770 -7.805 1.00 36.67 C ANISOU 679 CB SER A 88 4808 5626 3500 395 -613 -1694 C ATOM 680 OG SER A 88 -4.446 -22.526 -9.093 1.00 38.91 O ANISOU 680 OG SER A 88 5269 6099 3415 393 -552 -1691 O ATOM 681 N ASP A 89 -1.735 -22.764 -7.541 1.00 51.83 N ANISOU 681 N ASP A 89 6788 7529 5378 332 -13 -1633 N ATOM 682 CA ASP A 89 -0.417 -23.412 -7.443 1.00 51.75 C ANISOU 682 CA ASP A 89 6690 7451 5522 314 206 -1726 C ATOM 683 C ASP A 89 0.221 -23.127 -6.102 1.00 49.47 C ANISOU 683 C ASP A 89 6294 7015 5489 313 305 -1585 C ATOM 684 O ASP A 89 0.704 -24.024 -5.413 1.00 48.81 O ANISOU 684 O ASP A 89 6066 6753 5726 340 335 -1670 O ATOM 685 CB ASP A 89 0.511 -22.917 -8.556 1.00 53.78 C ANISOU 685 CB ASP A 89 7082 7898 5454 275 393 -1697 C ATOM 686 CG ASP A 89 0.050 -23.364 -9.932 1.00 57.22 C ANISOU 686 CG ASP A 89 7635 8471 5634 279 314 -1858 C ATOM 687 OD1 ASP A 89 -0.688 -24.374 -9.999 1.00 57.91 O ANISOU 687 OD1 ASP A 89 7633 8481 5890 306 152 -2058 O ATOM 688 OD2 ASP A 89 0.419 -22.714 -10.943 1.00 59.84 O1- ANISOU 688 OD2 ASP A 89 8157 8977 5604 245 417 -1780 O1- ATOM 689 N LEU A 90 0.209 -21.858 -5.735 1.00 35.54 N ANISOU 689 N LEU A 90 4614 5275 3614 276 327 -1294 N ATOM 690 CA LEU A 90 0.733 -21.438 -4.451 1.00 34.12 C ANISOU 690 CA LEU A 90 4349 4947 3669 255 388 -1105 C ATOM 691 C LEU A 90 0.101 -22.210 -3.311 1.00 33.01 C ANISOU 691 C LEU A 90 4091 4591 3859 286 256 -1102 C ATOM 692 O LEU A 90 0.803 -22.770 -2.475 1.00 31.82 O ANISOU 692 O LEU A 90 3830 4312 3948 305 303 -1114 O ATOM 693 CB LEU A 90 0.481 -19.949 -4.245 1.00 34.47 C ANISOU 693 CB LEU A 90 4517 5016 3562 212 386 -822 C ATOM 694 CG LEU A 90 1.047 -19.319 -2.983 1.00 33.20 C ANISOU 694 CG LEU A 90 4288 4732 3594 174 449 -649 C ATOM 695 CD1 LEU A 90 2.548 -19.657 -2.845 1.00 32.84 C ANISOU 695 CD1 LEU A 90 4115 4712 3650 146 630 -752 C ATOM 696 CD2 LEU A 90 0.815 -17.823 -3.022 1.00 33.86 C ANISOU 696 CD2 LEU A 90 4519 4827 3521 128 462 -413 C ATOM 697 N ALA A 91 -1.227 -22.233 -3.279 1.00 33.32 N ANISOU 697 N ALA A 91 4154 4596 3911 290 90 -1079 N ATOM 698 CA ALA A 91 -1.963 -22.934 -2.234 1.00 32.43 C ANISOU 698 CA ALA A 91 3940 4287 4095 282 0 -1063 C ATOM 699 C ALA A 91 -1.711 -24.436 -2.285 1.00 32.19 C ANISOU 699 C ALA A 91 3822 4121 4289 298 0 -1285 C ATOM 700 O ALA A 91 -1.540 -25.080 -1.254 1.00 31.26 O ANISOU 700 O ALA A 91 3639 3805 4432 298 9 -1225 O ATOM 701 CB ALA A 91 -3.449 -22.639 -2.348 1.00 33.33 C ANISOU 701 CB ALA A 91 4055 4422 4187 272 -158 -1040 C ATOM 702 N GLN A 92 -1.690 -24.986 -3.493 1.00 37.27 N ANISOU 702 N GLN A 92 4480 4862 4819 317 -15 -1541 N ATOM 703 CA GLN A 92 -1.411 -26.401 -3.690 1.00 38.45 C ANISOU 703 CA GLN A 92 4551 4865 5193 340 -11 -1790 C ATOM 704 C GLN A 92 -0.043 -26.740 -3.122 1.00 37.75 C ANISOU 704 C GLN A 92 4404 4680 5259 391 113 -1727 C ATOM 705 O GLN A 92 0.183 -27.839 -2.625 1.00 37.90 O ANISOU 705 O GLN A 92 4357 4487 5555 412 87 -1744 O ATOM 706 CB GLN A 92 -1.445 -26.738 -5.179 1.00 51.34 C ANISOU 706 CB GLN A 92 6227 6676 6605 339 -26 -1998 C ATOM 707 CG GLN A 92 -2.330 -27.919 -5.531 1.00 53.33 C ANISOU 707 CG GLN A 92 6415 6811 7035 305 -151 -2181 C ATOM 708 CD GLN A 92 -1.585 -28.996 -6.289 1.00 56.04 C ANISOU 708 CD GLN A 92 6728 7131 7434 334 -84 -2388 C ATOM 709 NE2 GLN A 92 -1.091 -28.653 -7.470 1.00 57.82 N ANISOU 709 NE2 GLN A 92 7033 7594 7341 353 -16 -2496 N ATOM 710 OE1 GLN A 92 -1.455 -30.123 -5.820 1.00 56.88 O ANISOU 710 OE1 GLN A 92 6752 7001 7861 338 -90 -2442 O ATOM 711 N GLN A 93 0.865 -25.776 -3.206 1.00 44.43 N ANISOU 711 N GLN A 93 5271 5688 5923 406 237 -1645 N ATOM 712 CA GLN A 93 2.225 -25.931 -2.717 1.00 44.20 C ANISOU 712 CA GLN A 93 5152 5614 6027 450 335 -1596 C ATOM 713 C GLN A 93 2.248 -26.324 -1.248 1.00 43.04 C ANISOU 713 C GLN A 93 4951 5233 6171 486 254 -1434 C ATOM 714 O GLN A 93 3.154 -27.022 -0.797 1.00 43.49 O ANISOU 714 O GLN A 93 4928 5180 6414 548 248 -1427 O ATOM 715 CB GLN A 93 2.995 -24.626 -2.910 1.00 44.04 C ANISOU 715 CB GLN A 93 5152 5802 5779 415 481 -1500 C ATOM 716 CG GLN A 93 4.492 -24.796 -3.089 1.00 45.14 C ANISOU 716 CG GLN A 93 5180 5992 5979 434 607 -1552 C ATOM 717 CD GLN A 93 5.070 -23.800 -4.070 1.00 46.10 C ANISOU 717 CD GLN A 93 5359 6353 5805 352 787 -1546 C ATOM 718 NE2 GLN A 93 6.264 -24.085 -4.565 1.00 47.95 N ANISOU 718 NE2 GLN A 93 5492 6654 6073 356 914 -1654 N ATOM 719 OE1 GLN A 93 4.448 -22.788 -4.382 1.00 45.81 O ANISOU 719 OE1 GLN A 93 5463 6431 5512 283 813 -1433 O ATOM 720 N TYR A 94 1.251 -25.868 -0.501 1.00 32.58 N ANISOU 720 N TYR A 94 3684 3845 4852 438 180 -1264 N ATOM 721 CA TYR A 94 1.193 -26.154 0.925 1.00 31.66 C ANISOU 721 CA TYR A 94 3557 3533 4938 447 115 -1060 C ATOM 722 C TYR A 94 0.059 -27.102 1.285 1.00 32.14 C ANISOU 722 C TYR A 94 3644 3380 5189 402 32 -1055 C ATOM 723 O TYR A 94 -0.273 -27.277 2.453 1.00 31.58 O ANISOU 723 O TYR A 94 3604 3162 5232 372 -2 -853 O ATOM 724 CB TYR A 94 1.143 -24.858 1.731 1.00 30.28 C ANISOU 724 CB TYR A 94 3427 3465 4612 393 128 -816 C ATOM 725 CG TYR A 94 2.418 -24.067 1.587 1.00 30.00 C ANISOU 725 CG TYR A 94 3341 3581 4478 416 216 -818 C ATOM 726 CD1 TYR A 94 3.491 -24.287 2.435 1.00 29.77 C ANISOU 726 CD1 TYR A 94 3222 3495 4593 484 196 -774 C ATOM 727 CD2 TYR A 94 2.564 -23.128 0.578 1.00 30.65 C ANISOU 727 CD2 TYR A 94 3460 3860 4327 364 315 -866 C ATOM 728 CE1 TYR A 94 4.665 -23.578 2.297 1.00 30.07 C ANISOU 728 CE1 TYR A 94 3167 3678 4582 484 280 -810 C ATOM 729 CE2 TYR A 94 3.735 -22.416 0.432 1.00 30.63 C ANISOU 729 CE2 TYR A 94 3397 3981 4258 346 432 -871 C ATOM 730 CZ TYR A 94 4.780 -22.646 1.294 1.00 30.36 C ANISOU 730 CZ TYR A 94 3232 3896 4407 398 418 -862 C ATOM 731 OH TYR A 94 5.946 -21.938 1.151 1.00 31.02 O ANISOU 731 OH TYR A 94 3211 4110 4465 360 538 -899 O ATOM 732 N GLY A 95 -0.514 -27.725 0.261 1.00 32.42 N ANISOU 732 N GLY A 95 3667 3408 5242 378 8 -1284 N ATOM 733 CA GLY A 95 -1.417 -28.862 0.440 1.00 33.49 C ANISOU 733 CA GLY A 95 3795 3336 5593 308 -57 -1312 C ATOM 734 C GLY A 95 -2.754 -28.416 0.998 1.00 33.04 C ANISOU 734 C GLY A 95 3749 3243 5561 198 -88 -1207 C ATOM 735 O GLY A 95 -3.446 -29.164 1.690 1.00 33.74 O ANISOU 735 O GLY A 95 3832 3134 5855 112 -97 -1120 O ATOM 736 N VAL A 96 -3.124 -27.187 0.642 1.00 25.79 N ANISOU 736 N VAL A 96 2845 2578 4378 183 -93 -1157 N ATOM 737 CA VAL A 96 -4.304 -26.564 1.178 1.00 26.14 C ANISOU 737 CA VAL A 96 2872 2663 4398 98 -117 -1021 C ATOM 738 C VAL A 96 -5.468 -27.188 0.462 1.00 27.61 C ANISOU 738 C VAL A 96 2976 2822 4694 24 -204 -1237 C ATOM 739 O VAL A 96 -5.641 -27.010 -0.747 1.00 28.28 O ANISOU 739 O VAL A 96 3053 3071 4622 58 -288 -1436 O ATOM 740 CB VAL A 96 -4.281 -25.062 0.850 1.00 25.75 C ANISOU 740 CB VAL A 96 2865 2861 4059 138 -120 -931 C ATOM 741 CG1 VAL A 96 -5.653 -24.455 1.001 1.00 26.48 C ANISOU 741 CG1 VAL A 96 2903 3015 4142 87 -180 -890 C ATOM 742 CG2 VAL A 96 -3.224 -24.330 1.703 1.00 24.17 C ANISOU 742 CG2 VAL A 96 2722 2681 3780 177 -34 -728 C ATOM 743 N ARG A 97 -6.271 -27.924 1.223 1.00 58.49 N ANISOU 743 N ARG A 97 6826 6531 8866 -90 -184 -1197 N ATOM 744 CA ARG A 97 -7.496 -28.482 0.693 1.00 60.02 C ANISOU 744 CA ARG A 97 6896 6693 9215 -196 -263 -1405 C ATOM 745 C ARG A 97 -8.615 -28.142 1.646 1.00 60.18 C ANISOU 745 C ARG A 97 6825 6694 9346 -316 -209 -1257 C ATOM 746 O ARG A 97 -8.793 -28.812 2.641 1.00 60.51 O ANISOU 746 O ARG A 97 6881 6549 9563 -411 -92 -1101 O ATOM 747 CB ARG A 97 -7.345 -30.005 0.618 1.00 61.60 C ANISOU 747 CB ARG A 97 7097 6688 9621 -229 -233 -1465 C ATOM 748 CG ARG A 97 -6.455 -30.556 -0.512 1.00 62.52 C ANISOU 748 CG ARG A 97 7250 6850 9656 -123 -278 -1673 C ATOM 749 CD ARG A 97 -6.887 -31.992 -0.810 1.00 65.57 C ANISOU 749 CD ARG A 97 7582 7057 10274 -191 -290 -1813 C ATOM 750 NE ARG A 97 -6.336 -32.539 -2.044 1.00 67.42 N ANISOU 750 NE ARG A 97 7820 7362 10436 -113 -339 -2071 N ATOM 751 CZ ARG A 97 -6.289 -31.887 -3.197 1.00 67.51 C ANISOU 751 CZ ARG A 97 7834 7646 10171 -52 -410 -2248 C ATOM 752 NH1 ARG A 97 -6.767 -30.651 -3.267 1.00 65.90 N1+ ANISOU 752 NH1 ARG A 97 7633 7652 9754 -46 -465 -2186 N1+ ATOM 753 NH2 ARG A 97 -5.762 -32.469 -4.272 1.00 69.70 N ANISOU 753 NH2 ARG A 97 8124 7986 10372 6 -425 -2477 N ATOM 754 N GLY A 98 -9.453 -27.189 1.277 1.00 42.54 N ANISOU 754 N GLY A 98 4496 4680 6986 -297 -289 -1298 N ATOM 755 CA GLY A 98 -10.444 -26.662 2.198 1.00 42.68 C ANISOU 755 CA GLY A 98 4404 4724 7087 -378 -213 -1172 C ATOM 756 C GLY A 98 -10.035 -25.338 2.831 1.00 42.01 C ANISOU 756 C GLY A 98 4411 4777 6774 -275 -152 -945 C ATOM 757 O GLY A 98 -8.843 -25.104 3.067 1.00 41.35 O ANISOU 757 O GLY A 98 4490 4683 6540 -198 -106 -809 O ATOM 758 N TYR A 99 -11.026 -24.485 3.109 1.00 38.72 N ANISOU 758 N TYR A 99 3868 4480 6363 -274 -155 -933 N ATOM 759 CA TYR A 99 -10.791 -23.119 3.571 1.00 37.77 C ANISOU 759 CA TYR A 99 3818 4481 6051 -167 -121 -773 C ATOM 760 C TYR A 99 -11.598 -22.773 4.789 1.00 37.39 C ANISOU 760 C TYR A 99 3666 4428 6113 -245 35 -693 C ATOM 761 O TYR A 99 -12.665 -23.351 5.005 1.00 37.99 O ANISOU 761 O TYR A 99 3552 4468 6414 -371 86 -795 O ATOM 762 CB TYR A 99 -11.136 -22.129 2.469 1.00 37.60 C ANISOU 762 CB TYR A 99 3769 4634 5883 -20 -313 -860 C ATOM 763 CG TYR A 99 -10.528 -22.547 1.179 1.00 38.44 C ANISOU 763 CG TYR A 99 3969 4785 5852 34 -452 -976 C ATOM 764 CD1 TYR A 99 -9.200 -22.258 0.892 1.00 38.26 C ANISOU 764 CD1 TYR A 99 4145 4780 5613 100 -414 -879 C ATOM 765 CD2 TYR A 99 -11.252 -23.290 0.274 1.00 39.30 C ANISOU 765 CD2 TYR A 99 3952 4926 6055 2 -603 -1213 C ATOM 766 CE1 TYR A 99 -8.626 -22.680 -0.285 1.00 39.05 C ANISOU 766 CE1 TYR A 99 4324 4942 5572 139 -497 -1010 C ATOM 767 CE2 TYR A 99 -10.698 -23.717 -0.902 1.00 40.05 C ANISOU 767 CE2 TYR A 99 4141 5081 5994 46 -716 -1356 C ATOM 768 CZ TYR A 99 -9.387 -23.414 -1.184 1.00 39.90 C ANISOU 768 CZ TYR A 99 4329 5092 5740 116 -648 -1252 C ATOM 769 OH TYR A 99 -8.831 -23.855 -2.364 1.00 40.49 O ANISOU 769 OH TYR A 99 4491 5250 5643 153 -721 -1421 O ATOM 770 N PRO A 100 -11.095 -21.807 5.586 1.00 29.96 N ANISOU 770 N PRO A 100 2836 3530 5016 -183 126 -533 N ATOM 771 CA PRO A 100 -9.771 -21.206 5.364 1.00 28.75 C ANISOU 771 CA PRO A 100 2884 3401 4639 -74 83 -427 C ATOM 772 C PRO A 100 -8.680 -22.121 5.918 1.00 29.30 C ANISOU 772 C PRO A 100 3088 3349 4695 -133 161 -319 C ATOM 773 O PRO A 100 -8.959 -22.928 6.800 1.00 30.07 O ANISOU 773 O PRO A 100 3176 3341 4910 -249 274 -255 O ATOM 774 CB PRO A 100 -9.848 -19.907 6.159 1.00 27.37 C ANISOU 774 CB PRO A 100 2736 3293 4371 -18 156 -340 C ATOM 775 CG PRO A 100 -10.746 -20.245 7.316 1.00 28.25 C ANISOU 775 CG PRO A 100 2735 3384 4616 -138 326 -335 C ATOM 776 CD PRO A 100 -11.804 -21.169 6.717 1.00 29.44 C ANISOU 776 CD PRO A 100 2689 3508 4989 -221 282 -485 C ATOM 777 N THR A 101 -7.469 -22.040 5.389 1.00 31.10 N ANISOU 777 N THR A 101 3435 3585 4796 -53 102 -298 N ATOM 778 CA THR A 101 -6.348 -22.741 6.010 1.00 30.50 C ANISOU 778 CA THR A 101 3464 3406 4720 -65 149 -194 C ATOM 779 C THR A 101 -5.238 -21.753 6.389 1.00 28.62 C ANISOU 779 C THR A 101 3323 3248 4303 6 160 -95 C ATOM 780 O THR A 101 -4.628 -21.121 5.519 1.00 27.59 O ANISOU 780 O THR A 101 3218 3200 4067 74 112 -145 O ATOM 781 CB THR A 101 -5.795 -23.858 5.119 1.00 30.49 C ANISOU 781 CB THR A 101 3465 3309 4810 -45 83 -309 C ATOM 782 CG2 THR A 101 -4.782 -24.683 5.893 1.00 29.90 C ANISOU 782 CG2 THR A 101 3475 3088 4799 -34 113 -195 C ATOM 783 OG1 THR A 101 -6.872 -24.705 4.678 1.00 32.14 O ANISOU 783 OG1 THR A 101 3570 3438 5203 -128 58 -445 O ATOM 784 N ILE A 102 -4.997 -21.634 7.698 1.00 20.03 N ANISOU 784 N ILE A 102 2295 2143 3174 -26 229 40 N ATOM 785 CA ILE A 102 -4.141 -20.587 8.256 1.00 18.84 C ANISOU 785 CA ILE A 102 2211 2077 2870 15 235 103 C ATOM 786 C ILE A 102 -2.871 -21.220 8.763 1.00 18.79 C ANISOU 786 C ILE A 102 2264 2023 2853 46 194 178 C ATOM 787 O ILE A 102 -2.916 -22.194 9.498 1.00 19.57 O ANISOU 787 O ILE A 102 2408 2022 3008 19 200 274 O ATOM 788 CB ILE A 102 -4.849 -19.804 9.398 1.00 19.68 C ANISOU 788 CB ILE A 102 2332 2240 2904 -30 325 153 C ATOM 789 CG1 ILE A 102 -6.142 -19.163 8.883 1.00 19.47 C ANISOU 789 CG1 ILE A 102 2205 2256 2939 -26 348 57 C ATOM 790 CG2 ILE A 102 -3.978 -18.709 9.944 1.00 18.99 C ANISOU 790 CG2 ILE A 102 2310 2228 2676 2 317 173 C ATOM 791 CD1 ILE A 102 -6.961 -18.504 9.952 1.00 19.86 C ANISOU 791 CD1 ILE A 102 2228 2357 2959 -63 465 56 C ATOM 792 N LYS A 103 -1.736 -20.647 8.369 1.00 26.80 N ANISOU 792 N LYS A 103 3275 3102 3807 102 151 139 N ATOM 793 CA LYS A 103 -0.447 -21.247 8.651 1.00 27.23 C ANISOU 793 CA LYS A 103 3326 3125 3893 160 85 164 C ATOM 794 C LYS A 103 0.557 -20.194 9.080 1.00 27.55 C ANISOU 794 C LYS A 103 3358 3276 3832 170 64 159 C ATOM 795 O LYS A 103 0.640 -19.106 8.511 1.00 26.96 O ANISOU 795 O LYS A 103 3267 3275 3702 142 110 96 O ATOM 796 CB LYS A 103 0.081 -21.992 7.409 1.00 26.74 C ANISOU 796 CB LYS A 103 3196 3018 3945 217 62 40 C ATOM 797 CG LYS A 103 -0.663 -23.278 7.083 1.00 27.21 C ANISOU 797 CG LYS A 103 3256 2927 4155 210 53 12 C ATOM 798 CD LYS A 103 -0.196 -23.858 5.736 1.00 27.28 C ANISOU 798 CD LYS A 103 3198 2921 4246 266 43 -174 C ATOM 799 CE LYS A 103 -0.881 -25.177 5.418 1.00 27.98 C ANISOU 799 CE LYS A 103 3281 2830 4521 251 22 -245 C ATOM 800 NZ LYS A 103 -0.898 -26.055 6.638 1.00 28.99 N1+ ANISOU 800 NZ LYS A 103 3473 2764 4780 247 -7 -72 N1+ ATOM 801 N PHE A 104 1.355 -20.542 10.073 1.00 21.67 N ANISOU 801 N PHE A 104 2628 2532 3072 208 -20 228 N ATOM 802 CA PHE A 104 2.245 -19.564 10.658 1.00 22.80 C ANISOU 802 CA PHE A 104 2747 2789 3127 199 -63 199 C ATOM 803 C PHE A 104 3.676 -19.874 10.277 1.00 23.11 C ANISOU 803 C PHE A 104 2656 2851 3273 271 -144 119 C ATOM 804 O PHE A 104 4.179 -20.988 10.462 1.00 23.33 O ANISOU 804 O PHE A 104 2655 2809 3402 370 -244 154 O ATOM 805 CB PHE A 104 2.076 -19.508 12.171 1.00 24.32 C ANISOU 805 CB PHE A 104 3042 3022 3175 186 -120 304 C ATOM 806 CG PHE A 104 3.044 -18.581 12.837 1.00 26.14 C ANISOU 806 CG PHE A 104 3237 3376 3319 176 -201 236 C ATOM 807 CD1 PHE A 104 2.907 -17.210 12.700 1.00 26.40 C ANISOU 807 CD1 PHE A 104 3257 3465 3309 94 -120 128 C ATOM 808 CD2 PHE A 104 4.107 -19.079 13.584 1.00 27.18 C ANISOU 808 CD2 PHE A 104 3340 3552 3435 255 -379 267 C ATOM 809 CE1 PHE A 104 3.798 -16.362 13.285 1.00 28.15 C ANISOU 809 CE1 PHE A 104 3432 3778 3484 61 -193 32 C ATOM 810 CE2 PHE A 104 5.003 -18.223 14.179 1.00 28.53 C ANISOU 810 CE2 PHE A 104 3447 3852 3541 235 -478 165 C ATOM 811 CZ PHE A 104 4.853 -16.864 14.029 1.00 28.89 C ANISOU 811 CZ PHE A 104 3474 3947 3556 123 -375 35 C ATOM 812 N PHE A 105 4.326 -18.872 9.720 1.00 22.45 N ANISOU 812 N PHE A 105 2486 2853 3191 219 -88 8 N ATOM 813 CA PHE A 105 5.688 -19.025 9.269 1.00 22.96 C ANISOU 813 CA PHE A 105 2380 2969 3376 260 -117 -106 C ATOM 814 C PHE A 105 6.649 -18.251 10.194 1.00 24.90 C ANISOU 814 C PHE A 105 2541 3318 3603 229 -213 -155 C ATOM 815 O PHE A 105 6.434 -17.046 10.514 1.00 25.70 O ANISOU 815 O PHE A 105 2693 3460 3612 116 -164 -175 O ATOM 816 CB PHE A 105 5.821 -18.543 7.833 1.00 21.88 C ANISOU 816 CB PHE A 105 2190 2862 3262 195 48 -207 C ATOM 817 CG PHE A 105 5.081 -19.380 6.825 1.00 20.55 C ANISOU 817 CG PHE A 105 2073 2627 3108 238 108 -216 C ATOM 818 CD1 PHE A 105 3.774 -19.086 6.470 1.00 19.49 C ANISOU 818 CD1 PHE A 105 2074 2456 2874 193 157 -154 C ATOM 819 CD2 PHE A 105 5.721 -20.441 6.167 1.00 20.50 C ANISOU 819 CD2 PHE A 105 1956 2599 3234 329 108 -327 C ATOM 820 CE1 PHE A 105 3.101 -19.863 5.486 1.00 18.67 C ANISOU 820 CE1 PHE A 105 1998 2310 2785 225 185 -202 C ATOM 821 CE2 PHE A 105 5.062 -21.203 5.185 1.00 19.52 C ANISOU 821 CE2 PHE A 105 1877 2418 3121 358 158 -386 C ATOM 822 CZ PHE A 105 3.757 -20.922 4.860 1.00 18.58 C ANISOU 822 CZ PHE A 105 1896 2278 2887 299 186 -323 C ATOM 823 N ARG A 106 7.692 -18.972 10.611 1.00 35.41 N ANISOU 823 N ARG A 106 3735 4677 5043 339 -368 -192 N ATOM 824 CA ARG A 106 8.750 -18.467 11.469 1.00 37.01 C ANISOU 824 CA ARG A 106 3807 4997 5259 338 -518 -272 C ATOM 825 C ARG A 106 10.084 -18.389 10.723 1.00 37.08 C ANISOU 825 C ARG A 106 3530 5080 5480 340 -485 -463 C ATOM 826 O ARG A 106 10.558 -19.390 10.175 1.00 36.55 O ANISOU 826 O ARG A 106 3339 4975 5573 469 -503 -509 O ATOM 827 CB ARG A 106 8.893 -19.394 12.668 1.00 38.00 C ANISOU 827 CB ARG A 106 3993 5112 5333 491 -770 -151 C ATOM 828 CG ARG A 106 9.709 -18.829 13.796 1.00 39.83 C ANISOU 828 CG ARG A 106 4151 5492 5491 493 -977 -214 C ATOM 829 CD ARG A 106 9.625 -19.704 15.040 1.00 41.09 C ANISOU 829 CD ARG A 106 4460 5648 5506 641 -1230 -32 C ATOM 830 NE ARG A 106 10.388 -19.082 16.121 1.00 43.01 N ANISOU 830 NE ARG A 106 4641 6071 5631 640 -1456 -119 N ATOM 831 CZ ARG A 106 9.917 -18.143 16.935 1.00 43.61 C ANISOU 831 CZ ARG A 106 4860 6251 5459 515 -1444 -143 C ATOM 832 NH1 ARG A 106 8.665 -17.719 16.810 1.00 42.97 N1+ ANISOU 832 NH1 ARG A 106 4978 6103 5243 395 -1209 -74 N1+ ATOM 833 NH2 ARG A 106 10.699 -17.630 17.879 1.00 44.98 N ANISOU 833 NH2 ARG A 106 4959 6601 5532 518 -1677 -264 N ATOM 834 N ASN A 107 10.670 -17.190 10.711 1.00 34.38 N ANISOU 834 N ASN A 107 3075 4831 5157 186 -420 -589 N ATOM 835 CA ASN A 107 11.935 -16.886 10.031 1.00 34.73 C ANISOU 835 CA ASN A 107 2823 4965 5407 124 -334 -788 C ATOM 836 C ASN A 107 11.984 -17.231 8.545 1.00 33.72 C ANISOU 836 C ASN A 107 2639 4812 5358 106 -86 -838 C ATOM 837 O ASN A 107 13.046 -17.538 7.984 1.00 34.04 O ANISOU 837 O ASN A 107 2532 4891 5512 121 -23 -949 O ATOM 838 CB ASN A 107 13.120 -17.468 10.786 1.00 35.90 C ANISOU 838 CB ASN A 107 2775 5189 5678 258 -573 -872 C ATOM 839 CG ASN A 107 13.409 -16.710 12.069 1.00 37.23 C ANISOU 839 CG ASN A 107 2934 5448 5765 204 -778 -909 C ATOM 840 ND2 ASN A 107 14.129 -15.586 11.946 1.00 37.96 N ANISOU 840 ND2 ASN A 107 2906 5594 5925 15 -672 -1058 N ATOM 841 OD1 ASN A 107 12.978 -17.112 13.150 1.00 37.69 O ANISOU 841 OD1 ASN A 107 3120 5521 5678 321 -1017 -800 O ATOM 842 N GLY A 108 10.816 -17.162 7.914 1.00 42.61 N ANISOU 842 N GLY A 108 4013 5849 6329 67 54 -710 N ATOM 843 CA GLY A 108 10.689 -17.384 6.489 1.00 41.67 C ANISOU 843 CA GLY A 108 3903 5727 6203 37 280 -749 C ATOM 844 C GLY A 108 10.894 -18.817 6.061 1.00 41.23 C ANISOU 844 C GLY A 108 3767 5643 6254 219 237 -816 C ATOM 845 O GLY A 108 10.938 -19.085 4.867 1.00 40.86 O ANISOU 845 O GLY A 108 3748 5609 6166 196 407 -876 O ATOM 846 N ASP A 109 11.007 -19.745 7.010 1.00 42.66 N ANISOU 846 N ASP A 109 3921 5761 6527 394 -3 -777 N ATOM 847 CA ASP A 109 11.206 -21.152 6.641 1.00 42.45 C ANISOU 847 CA ASP A 109 3891 5639 6600 557 -55 -810 C ATOM 848 C ASP A 109 9.888 -21.782 6.206 1.00 41.09 C ANISOU 848 C ASP A 109 3905 5339 6366 597 -18 -732 C ATOM 849 O ASP A 109 8.924 -21.858 6.968 1.00 40.82 O ANISOU 849 O ASP A 109 4042 5214 6252 609 -124 -563 O ATOM 850 CB ASP A 109 11.891 -21.969 7.760 1.00 44.01 C ANISOU 850 CB ASP A 109 4024 5783 6917 725 -320 -767 C ATOM 851 CG ASP A 109 12.149 -23.430 7.359 1.00 45.57 C ANISOU 851 CG ASP A 109 4219 5847 7250 884 -360 -807 C ATOM 852 OD1 ASP A 109 12.501 -23.705 6.186 1.00 46.63 O ANISOU 852 OD1 ASP A 109 4282 6003 7433 860 -188 -965 O ATOM 853 OD2 ASP A 109 11.990 -24.327 8.216 1.00 46.71 O1- ANISOU 853 OD2 ASP A 109 4448 5858 7442 1028 -562 -674 O1- ATOM 854 N THR A 110 9.872 -22.255 4.970 1.00 29.32 N ANISOU 854 N THR A 110 2428 3846 4867 587 134 -845 N ATOM 855 CA THR A 110 8.663 -22.739 4.333 1.00 28.25 C ANISOU 855 CA THR A 110 2453 3620 4660 592 187 -825 C ATOM 856 C THR A 110 8.475 -24.214 4.611 1.00 29.05 C ANISOU 856 C THR A 110 2600 3529 4906 734 45 -809 C ATOM 857 O THR A 110 7.464 -24.808 4.219 1.00 28.55 O ANISOU 857 O THR A 110 2663 3354 4830 735 56 -801 O ATOM 858 CB THR A 110 8.777 -22.583 2.822 1.00 28.76 C ANISOU 858 CB THR A 110 2523 3792 4612 510 397 -971 C ATOM 859 CG2 THR A 110 8.919 -21.092 2.427 1.00 28.24 C ANISOU 859 CG2 THR A 110 2466 3887 4377 338 569 -943 C ATOM 860 OG1 THR A 110 9.916 -23.339 2.366 1.00 30.58 O ANISOU 860 OG1 THR A 110 2614 4039 4967 575 415 -1126 O ATOM 861 N ALA A 111 9.464 -24.815 5.262 1.00 42.71 N ANISOU 861 N ALA A 111 4228 5216 6783 845 -89 -810 N ATOM 862 CA ALA A 111 9.452 -26.248 5.523 1.00 44.59 C ANISOU 862 CA ALA A 111 4513 5254 7176 980 -216 -785 C ATOM 863 C ALA A 111 8.783 -26.645 6.856 1.00 44.37 C ANISOU 863 C ALA A 111 4640 5063 7154 1038 -400 -535 C ATOM 864 O ALA A 111 8.532 -27.830 7.099 1.00 45.73 O ANISOU 864 O ALA A 111 4905 5034 7438 1119 -483 -467 O ATOM 865 CB ALA A 111 10.881 -26.788 5.467 1.00 47.58 C ANISOU 865 CB ALA A 111 4706 5655 7716 1091 -265 -916 C ATOM 866 N SER A 112 8.518 -25.671 7.725 1.00 32.83 N ANISOU 866 N SER A 112 3217 3687 5568 986 -456 -396 N ATOM 867 CA SER A 112 7.902 -25.975 9.023 1.00 33.20 C ANISOU 867 CA SER A 112 3438 3612 5564 1022 -617 -141 C ATOM 868 C SER A 112 6.784 -25.007 9.409 1.00 31.62 C ANISOU 868 C SER A 112 3376 3470 5170 879 -557 -14 C ATOM 869 O SER A 112 6.858 -24.357 10.447 1.00 32.34 O ANISOU 869 O SER A 112 3526 3661 5100 844 -643 107 O ATOM 870 CB SER A 112 8.965 -25.957 10.130 1.00 35.12 C ANISOU 870 CB SER A 112 3621 3924 5799 1127 -818 -64 C ATOM 871 OG SER A 112 9.431 -24.633 10.381 1.00 34.81 O ANISOU 871 OG SER A 112 3459 4105 5660 1054 -827 -131 O ATOM 872 N PRO A 113 5.749 -24.898 8.574 1.00 36.36 N ANISOU 872 N PRO A 113 4051 4046 5718 763 -391 -59 N ATOM 873 CA PRO A 113 4.626 -24.026 8.919 1.00 35.94 C ANISOU 873 CA PRO A 113 4140 4065 5451 606 -306 52 C ATOM 874 C PRO A 113 3.794 -24.662 10.031 1.00 36.67 C ANISOU 874 C PRO A 113 4410 4019 5503 591 -367 276 C ATOM 875 O PRO A 113 3.639 -25.880 10.039 1.00 37.03 O ANISOU 875 O PRO A 113 4502 3856 5710 655 -415 332 O ATOM 876 CB PRO A 113 3.826 -23.972 7.624 1.00 34.70 C ANISOU 876 CB PRO A 113 3984 3906 5295 530 -159 -74 C ATOM 877 CG PRO A 113 4.142 -25.255 6.953 1.00 34.95 C ANISOU 877 CG PRO A 113 3954 3784 5542 636 -184 -192 C ATOM 878 CD PRO A 113 5.568 -25.543 7.265 1.00 35.85 C ANISOU 878 CD PRO A 113 3930 3905 5787 781 -287 -241 C ATOM 879 N LYS A 114 3.293 -23.867 10.970 1.00 39.01 N ANISOU 879 N LYS A 114 4810 4419 5593 500 -351 396 N ATOM 880 CA LYS A 114 2.426 -24.425 11.982 1.00 39.83 C ANISOU 880 CA LYS A 114 5091 4421 5622 453 -350 607 C ATOM 881 C LYS A 114 0.985 -24.074 11.648 1.00 39.04 C ANISOU 881 C LYS A 114 5030 4327 5476 304 -172 587 C ATOM 882 O LYS A 114 0.677 -22.930 11.283 1.00 38.34 O ANISOU 882 O LYS A 114 4890 4386 5293 243 -92 481 O ATOM 883 CB LYS A 114 2.832 -23.977 13.387 1.00 41.41 C ANISOU 883 CB LYS A 114 5390 4740 5603 466 -456 747 C ATOM 884 CG LYS A 114 4.216 -24.486 13.817 1.00 42.63 C ANISOU 884 CG LYS A 114 5495 4881 5823 641 -691 781 C ATOM 885 CD LYS A 114 4.469 -25.961 13.409 1.00 42.97 C ANISOU 885 CD LYS A 114 5536 4660 6132 773 -771 838 C ATOM 886 CE LYS A 114 5.796 -26.534 13.999 1.00 44.81 C ANISOU 886 CE LYS A 114 5722 4878 6424 976 -1019 884 C ATOM 887 NZ LYS A 114 5.746 -26.801 15.489 1.00 46.86 N1+ ANISOU 887 NZ LYS A 114 6202 5166 6436 995 -1132 1144 N1+ ATOM 888 N GLU A 115 0.113 -25.071 11.747 1.00 39.93 N ANISOU 888 N GLU A 115 5220 4262 5689 250 -118 684 N ATOM 889 CA GLU A 115 -1.285 -24.910 11.393 1.00 39.41 C ANISOU 889 CA GLU A 115 5141 4193 5641 112 36 638 C ATOM 890 C GLU A 115 -1.970 -24.189 12.524 1.00 39.93 C ANISOU 890 C GLU A 115 5292 4384 5495 14 133 750 C ATOM 891 O GLU A 115 -1.728 -24.498 13.698 1.00 41.08 O ANISOU 891 O GLU A 115 5580 4519 5511 12 106 937 O ATOM 892 CB GLU A 115 -1.942 -26.275 11.154 1.00 40.06 C ANISOU 892 CB GLU A 115 5250 4026 5943 58 71 680 C ATOM 893 CG GLU A 115 -3.466 -26.217 11.003 1.00 40.52 C ANISOU 893 CG GLU A 115 5266 4083 6046 -108 226 638 C ATOM 894 CD GLU A 115 -3.960 -26.282 9.544 1.00 40.16 C ANISOU 894 CD GLU A 115 5069 4030 6158 -116 220 392 C ATOM 895 OE1 GLU A 115 -3.608 -27.248 8.834 1.00 40.46 O ANISOU 895 OE1 GLU A 115 5086 3901 6386 -71 155 302 O ATOM 896 OE2 GLU A 115 -4.725 -25.385 9.114 1.00 39.78 O1- ANISOU 896 OE2 GLU A 115 4928 4140 6044 -158 268 279 O1- ATOM 897 N TYR A 116 -2.806 -23.213 12.180 1.00 31.76 N ANISOU 897 N TYR A 116 4180 3475 4414 -52 238 629 N ATOM 898 CA TYR A 116 -3.574 -22.512 13.193 1.00 32.22 C ANISOU 898 CA TYR A 116 4290 3651 4301 -140 362 679 C ATOM 899 C TYR A 116 -4.955 -23.140 13.306 1.00 32.77 C ANISOU 899 C TYR A 116 4335 3640 4477 -275 523 711 C ATOM 900 O TYR A 116 -5.767 -22.995 12.399 1.00 32.42 O ANISOU 900 O TYR A 116 4147 3589 4583 -303 562 564 O ATOM 901 CB TYR A 116 -3.736 -21.058 12.782 1.00 31.46 C ANISOU 901 CB TYR A 116 4105 3705 4142 -117 384 516 C ATOM 902 CG TYR A 116 -4.615 -20.267 13.726 1.00 31.98 C ANISOU 902 CG TYR A 116 4192 3886 4072 -189 528 503 C ATOM 903 CD1 TYR A 116 -4.058 -19.572 14.792 1.00 32.53 C ANISOU 903 CD1 TYR A 116 4361 4078 3922 -180 518 523 C ATOM 904 CD2 TYR A 116 -5.998 -20.217 13.559 1.00 31.86 C ANISOU 904 CD2 TYR A 116 4075 3872 4158 -264 671 436 C ATOM 905 CE1 TYR A 116 -4.834 -18.867 15.660 1.00 32.89 C ANISOU 905 CE1 TYR A 116 4427 4236 3833 -241 666 472 C ATOM 906 CE2 TYR A 116 -6.792 -19.499 14.434 1.00 32.24 C ANISOU 906 CE2 TYR A 116 4115 4035 4101 -318 828 389 C ATOM 907 CZ TYR A 116 -6.191 -18.828 15.487 1.00 32.71 C ANISOU 907 CZ TYR A 116 4297 4210 3922 -305 835 405 C ATOM 908 OH TYR A 116 -6.931 -18.104 16.394 1.00 33.19 O ANISOU 908 OH TYR A 116 4357 4396 3857 -355 1006 321 O ATOM 909 N THR A 117 -5.194 -23.890 14.376 1.00 37.29 N ANISOU 909 N THR A 117 5045 4146 4977 -364 609 907 N ATOM 910 CA THR A 117 -6.523 -24.439 14.631 1.00 38.18 C ANISOU 910 CA THR A 117 5124 4191 5190 -538 813 944 C ATOM 911 C THR A 117 -7.333 -23.724 15.740 1.00 38.73 C ANISOU 911 C THR A 117 5222 4443 5050 -646 1026 965 C ATOM 912 O THR A 117 -8.451 -24.127 16.034 1.00 39.51 O ANISOU 912 O THR A 117 5250 4549 5211 -786 1167 946 O ATOM 913 CB THR A 117 -6.501 -25.968 14.870 1.00 39.45 C ANISOU 913 CB THR A 117 5404 4111 5473 -610 804 1124 C ATOM 914 CG2 THR A 117 -5.861 -26.710 13.658 1.00 38.89 C ANISOU 914 CG2 THR A 117 5271 3833 5673 -507 639 1044 C ATOM 915 OG1 THR A 117 -5.760 -26.259 16.059 1.00 40.68 O ANISOU 915 OG1 THR A 117 5792 4280 5384 -582 738 1351 O ATOM 916 N ALA A 118 -6.769 -22.685 16.365 1.00 34.45 N ANISOU 916 N ALA A 118 4749 4088 4252 -567 986 936 N ATOM 917 CA ALA A 118 -7.348 -22.061 17.572 1.00 35.19 C ANISOU 917 CA ALA A 118 4900 4373 4097 -649 1164 934 C ATOM 918 C ALA A 118 -8.612 -21.215 17.290 1.00 34.78 C ANISOU 918 C ALA A 118 4621 4429 4165 -688 1324 697 C ATOM 919 O ALA A 118 -9.238 -21.357 16.257 1.00 34.08 O ANISOU 919 O ALA A 118 4347 4254 4348 -693 1324 584 O ATOM 920 CB ALA A 118 -6.283 -21.231 18.313 1.00 35.33 C ANISOU 920 CB ALA A 118 5069 4543 3812 -551 1054 942 C ATOM 921 N GLY A 119 -9.033 -20.407 18.257 1.00 45.17 N ANISOU 921 N GLY A 119 5942 5933 5286 -702 1442 616 N ATOM 922 CA GLY A 119 -10.264 -19.634 18.143 1.00 45.49 C ANISOU 922 CA GLY A 119 5766 6064 5454 -707 1580 393 C ATOM 923 C GLY A 119 -10.357 -18.642 16.994 1.00 43.60 C ANISOU 923 C GLY A 119 5353 5796 5418 -584 1499 181 C ATOM 924 O GLY A 119 -9.360 -18.249 16.416 1.00 42.68 O ANISOU 924 O GLY A 119 5299 5631 5286 -489 1351 182 O ATOM 925 N ARG A 120 -11.582 -18.266 16.651 1.00 62.60 N ANISOU 925 N ARG A 120 7536 8228 8022 -574 1568 9 N ATOM 926 CA ARG A 120 -11.883 -17.419 15.502 1.00 61.43 C ANISOU 926 CA ARG A 120 7206 8041 8094 -440 1458 -171 C ATOM 927 C ARG A 120 -12.119 -15.923 15.815 1.00 61.45 C ANISOU 927 C ARG A 120 7162 8121 8067 -314 1473 -356 C ATOM 928 O ARG A 120 -12.520 -15.158 14.934 1.00 60.89 O ANISOU 928 O ARG A 120 6946 8002 8186 -183 1368 -489 O ATOM 929 CB ARG A 120 -13.038 -18.026 14.709 1.00 62.22 C ANISOU 929 CB ARG A 120 7083 8091 8467 -476 1444 -242 C ATOM 930 CG ARG A 120 -12.757 -19.508 14.362 1.00 62.82 C ANISOU 930 CG ARG A 120 7217 8046 8606 -601 1416 -85 C ATOM 931 CD ARG A 120 -13.833 -20.163 13.471 1.00 63.88 C ANISOU 931 CD ARG A 120 7129 8121 9020 -646 1370 -194 C ATOM 932 NE ARG A 120 -13.230 -20.804 12.294 1.00 63.45 N ANISOU 932 NE ARG A 120 7077 7939 9091 -623 1195 -172 N ATOM 933 CZ ARG A 120 -13.908 -21.388 11.307 1.00 63.92 C ANISOU 933 CZ ARG A 120 6970 7943 9374 -642 1090 -289 C ATOM 934 NH1 ARG A 120 -15.233 -21.430 11.343 1.00 65.32 N1+ ANISOU 934 NH1 ARG A 120 6955 8173 9691 -688 1143 -423 N1+ ATOM 935 NH2 ARG A 120 -13.254 -21.937 10.286 1.00 63.60 N ANISOU 935 NH2 ARG A 120 6952 7799 9413 -616 928 -290 N ATOM 936 N GLU A 121 -11.905 -15.506 17.055 1.00 49.18 N ANISOU 936 N GLU A 121 5735 6672 6279 -344 1583 -367 N ATOM 937 CA GLU A 121 -11.969 -14.079 17.416 1.00 49.63 C ANISOU 937 CA GLU A 121 5778 6769 6311 -228 1587 -559 C ATOM 938 C GLU A 121 -10.600 -13.383 17.375 1.00 48.15 C ANISOU 938 C GLU A 121 5761 6548 5986 -166 1470 -562 C ATOM 939 O GLU A 121 -9.568 -13.999 17.611 1.00 47.57 O ANISOU 939 O GLU A 121 5857 6493 5725 -234 1429 -414 O ATOM 940 CB GLU A 121 -12.611 -13.890 18.800 1.00 52.81 C ANISOU 940 CB GLU A 121 6199 7315 6552 -289 1779 -630 C ATOM 941 CG GLU A 121 -14.004 -14.507 18.954 1.00 55.74 C ANISOU 941 CG GLU A 121 6389 7730 7061 -370 1933 -651 C ATOM 942 CD GLU A 121 -14.084 -15.462 20.144 1.00 58.49 C ANISOU 942 CD GLU A 121 6865 8193 7166 -535 2115 -497 C ATOM 943 OE1 GLU A 121 -13.435 -16.542 20.096 1.00 57.83 O ANISOU 943 OE1 GLU A 121 6920 8065 6987 -628 2069 -268 O ATOM 944 OE2 GLU A 121 -14.795 -15.140 21.132 1.00 61.88 O1- ANISOU 944 OE2 GLU A 121 7263 8749 7501 -568 2303 -595 O1- ATOM 945 N ALA A 122 -10.594 -12.102 17.041 1.00 33.93 N ANISOU 945 N ALA A 122 3916 4678 4300 -37 1402 -729 N ATOM 946 CA ALA A 122 -9.349 -11.345 16.954 1.00 33.00 C ANISOU 946 CA ALA A 122 3941 4500 4098 5 1297 -764 C ATOM 947 C ALA A 122 -8.439 -11.558 18.156 1.00 33.83 C ANISOU 947 C ALA A 122 4239 4739 3875 -96 1325 -732 C ATOM 948 O ALA A 122 -7.233 -11.733 18.002 1.00 33.35 O ANISOU 948 O ALA A 122 4300 4654 3719 -113 1163 -626 O ATOM 949 CB ALA A 122 -9.634 -9.867 16.763 1.00 33.47 C ANISOU 949 CB ALA A 122 3949 4446 4323 139 1247 -954 C ATOM 950 N ASP A 123 -9.015 -11.578 19.354 1.00 51.87 N ANISOU 950 N ASP A 123 6547 7161 6000 -143 1453 -781 N ATOM 951 CA ASP A 123 -8.219 -11.786 20.562 1.00 53.32 C ANISOU 951 CA ASP A 123 6927 7494 5839 -217 1450 -740 C ATOM 952 C ASP A 123 -7.529 -13.150 20.671 1.00 53.05 C ANISOU 952 C ASP A 123 7028 7508 5619 -306 1393 -468 C ATOM 953 O ASP A 123 -6.435 -13.253 21.242 1.00 53.64 O ANISOU 953 O ASP A 123 7271 7662 5447 -327 1270 -414 O ATOM 954 CB ASP A 123 -9.066 -11.560 21.806 1.00 56.51 C ANISOU 954 CB ASP A 123 7335 8039 6097 -239 1621 -839 C ATOM 955 CG ASP A 123 -9.835 -10.277 21.740 1.00 57.91 C ANISOU 955 CG ASP A 123 7373 8150 6479 -141 1678 -1101 C ATOM 956 OD1 ASP A 123 -9.322 -9.281 22.311 1.00 59.10 O ANISOU 956 OD1 ASP A 123 7605 8311 6541 -106 1634 -1279 O ATOM 957 OD2 ASP A 123 -10.930 -10.270 21.098 1.00 58.09 O1- ANISOU 957 OD2 ASP A 123 7203 8101 6766 -96 1743 -1132 O1- ATOM 958 N ASP A 124 -8.152 -14.207 20.168 1.00 44.65 N ANISOU 958 N ASP A 124 5892 6388 4684 -353 1454 -301 N ATOM 959 CA ASP A 124 -7.494 -15.501 20.303 1.00 44.77 C ANISOU 959 CA ASP A 124 6053 6398 4559 -424 1385 -30 C ATOM 960 C ASP A 124 -6.418 -15.686 19.237 1.00 43.54 C ANISOU 960 C ASP A 124 5904 6106 4533 -361 1154 48 C ATOM 961 O ASP A 124 -5.430 -16.403 19.435 1.00 43.93 O ANISOU 961 O ASP A 124 6083 6147 4462 -356 996 221 O ATOM 962 CB ASP A 124 -8.495 -16.657 20.347 1.00 45.88 C ANISOU 962 CB ASP A 124 6131 6504 4797 -513 1518 128 C ATOM 963 CG ASP A 124 -9.608 -16.505 19.344 1.00 45.18 C ANISOU 963 CG ASP A 124 5794 6323 5048 -498 1589 2 C ATOM 964 OD1 ASP A 124 -10.793 -16.718 19.717 1.00 46.78 O ANISOU 964 OD1 ASP A 124 5881 6573 5320 -558 1749 -36 O ATOM 965 OD2 ASP A 124 -9.281 -16.194 18.180 1.00 43.59 O1- ANISOU 965 OD2 ASP A 124 5513 6010 5038 -424 1474 -55 O1- ATOM 966 N ILE A 125 -6.608 -15.004 18.114 1.00 28.72 N ANISOU 966 N ILE A 125 3870 4116 2926 -279 1095 -79 N ATOM 967 CA ILE A 125 -5.569 -14.897 17.111 1.00 27.76 C ANISOU 967 CA ILE A 125 3736 3883 2930 -204 874 -44 C ATOM 968 C ILE A 125 -4.357 -14.224 17.737 1.00 28.62 C ANISOU 968 C ILE A 125 3948 4061 2865 -189 747 -106 C ATOM 969 O ILE A 125 -3.238 -14.794 17.715 1.00 29.02 O ANISOU 969 O ILE A 125 4057 4111 2859 -178 581 7 O ATOM 970 CB ILE A 125 -6.049 -14.073 15.899 1.00 26.49 C ANISOU 970 CB ILE A 125 3430 3607 3027 -123 851 -164 C ATOM 971 CG1 ILE A 125 -6.944 -14.920 14.983 1.00 25.81 C ANISOU 971 CG1 ILE A 125 3223 3451 3133 -124 876 -98 C ATOM 972 CG2 ILE A 125 -4.879 -13.488 15.123 1.00 25.68 C ANISOU 972 CG2 ILE A 125 3350 3425 2982 -71 678 -172 C ATOM 973 CD1 ILE A 125 -7.871 -14.077 14.088 1.00 24.87 C ANISOU 973 CD1 ILE A 125 2954 3269 3227 -34 876 -232 C ATOM 974 N VAL A 126 -4.567 -13.038 18.327 1.00 29.22 N ANISOU 974 N VAL A 126 4030 4195 2877 -186 818 -312 N ATOM 975 CA VAL A 126 -3.404 -12.315 18.842 1.00 30.28 C ANISOU 975 CA VAL A 126 4236 4381 2887 -189 680 -419 C ATOM 976 C VAL A 126 -2.754 -13.134 19.932 1.00 31.72 C ANISOU 976 C VAL A 126 4562 4728 2763 -228 598 -301 C ATOM 977 O VAL A 126 -1.533 -13.261 19.992 1.00 32.51 O ANISOU 977 O VAL A 126 4686 4853 2814 -212 392 -269 O ATOM 978 CB VAL A 126 -3.637 -10.805 19.270 1.00 30.56 C ANISOU 978 CB VAL A 126 4260 4412 2939 -182 750 -706 C ATOM 979 CG1 VAL A 126 -4.588 -10.079 18.314 1.00 29.26 C ANISOU 979 CG1 VAL A 126 3972 4073 3071 -111 843 -789 C ATOM 980 CG2 VAL A 126 -4.123 -10.695 20.682 1.00 31.87 C ANISOU 980 CG2 VAL A 126 4521 4773 2814 -227 888 -830 C ATOM 981 N ASN A 127 -3.568 -13.738 20.775 1.00 38.86 N ANISOU 981 N ASN A 127 5558 5745 3463 -280 757 -221 N ATOM 982 CA ASN A 127 -3.001 -14.480 21.895 1.00 40.49 C ANISOU 982 CA ASN A 127 5952 6110 3323 -311 674 -73 C ATOM 983 C ASN A 127 -2.140 -15.672 21.467 1.00 40.50 C ANISOU 983 C ASN A 127 5983 6022 3383 -264 467 189 C ATOM 984 O ASN A 127 -0.987 -15.820 21.907 1.00 41.52 O ANISOU 984 O ASN A 127 6180 6225 3370 -217 230 228 O ATOM 985 CB ASN A 127 -4.094 -14.850 22.889 1.00 41.74 C ANISOU 985 CB ASN A 127 6198 6378 3283 -369 908 -16 C ATOM 986 CG ASN A 127 -4.423 -13.692 23.801 1.00 43.50 C ANISOU 986 CG ASN A 127 6424 6722 3381 -353 995 -282 C ATOM 987 ND2 ASN A 127 -5.683 -13.576 24.204 1.00 44.73 N ANISOU 987 ND2 ASN A 127 6520 6907 3569 -371 1238 -337 N ATOM 988 OD1 ASN A 127 -3.542 -12.888 24.119 1.00 44.14 O ANISOU 988 OD1 ASN A 127 6545 6862 3364 -327 835 -456 O ATOM 989 N TRP A 128 -2.689 -16.481 20.567 1.00 31.45 N ANISOU 989 N TRP A 128 4760 4712 2478 -265 540 332 N ATOM 990 CA TRP A 128 -1.958 -17.593 19.982 1.00 31.27 C ANISOU 990 CA TRP A 128 4736 4558 2587 -206 366 533 C ATOM 991 C TRP A 128 -0.593 -17.108 19.472 1.00 31.49 C ANISOU 991 C TRP A 128 4667 4577 2721 -118 125 426 C ATOM 992 O TRP A 128 0.484 -17.702 19.753 1.00 32.55 O ANISOU 992 O TRP A 128 4841 4731 2797 -46 -95 529 O ATOM 993 CB TRP A 128 -2.819 -18.162 18.862 1.00 29.77 C ANISOU 993 CB TRP A 128 4426 4192 2694 -226 490 578 C ATOM 994 CG TRP A 128 -2.402 -19.489 18.311 1.00 29.75 C ANISOU 994 CG TRP A 128 4434 4026 2842 -185 379 772 C ATOM 995 CD1 TRP A 128 -2.829 -20.736 18.724 1.00 30.35 C ANISOU 995 CD1 TRP A 128 4633 4009 2891 -239 440 1002 C ATOM 996 CD2 TRP A 128 -1.517 -19.720 17.202 1.00 29.04 C ANISOU 996 CD2 TRP A 128 4227 3823 2982 -89 213 736 C ATOM 997 CE2 TRP A 128 -1.448 -21.124 17.006 1.00 29.18 C ANISOU 997 CE2 TRP A 128 4294 3677 3114 -67 165 922 C ATOM 998 CE3 TRP A 128 -0.777 -18.881 16.361 1.00 28.48 C ANISOU 998 CE3 TRP A 128 4021 3767 3034 -32 122 565 C ATOM 999 NE1 TRP A 128 -2.258 -21.716 17.940 1.00 30.02 N ANISOU 999 NE1 TRP A 128 4555 3779 3073 -164 300 1094 N ATOM 1000 CZ2 TRP A 128 -0.660 -21.703 16.008 1.00 28.50 C ANISOU 1000 CZ2 TRP A 128 4109 3461 3257 31 27 901 C ATOM 1001 CZ3 TRP A 128 0.015 -19.468 15.366 1.00 28.18 C ANISOU 1001 CZ3 TRP A 128 3888 3623 3195 45 6 568 C ATOM 1002 CH2 TRP A 128 0.062 -20.866 15.205 1.00 28.02 C ANISOU 1002 CH2 TRP A 128 3904 3460 3282 86 -42 717 C ATOM 1003 N LEU A 129 -0.625 -16.000 18.746 1.00 21.55 N ANISOU 1003 N LEU A 129 3273 3286 1630 -123 168 219 N ATOM 1004 CA LEU A 129 0.617 -15.505 18.171 1.00 21.97 C ANISOU 1004 CA LEU A 129 3215 3317 1814 -81 -5 115 C ATOM 1005 C LEU A 129 1.623 -15.045 19.248 1.00 23.73 C ANISOU 1005 C LEU A 129 3485 3703 1827 -80 -181 19 C ATOM 1006 O LEU A 129 2.838 -15.263 19.120 1.00 24.29 O ANISOU 1006 O LEU A 129 3475 3795 1961 -29 -386 13 O ATOM 1007 CB LEU A 129 0.333 -14.374 17.190 1.00 20.70 C ANISOU 1007 CB LEU A 129 2941 3062 1861 -106 95 -50 C ATOM 1008 CG LEU A 129 -0.393 -14.676 15.864 1.00 18.96 C ANISOU 1008 CG LEU A 129 2644 2697 1863 -86 194 10 C ATOM 1009 CD1 LEU A 129 -1.068 -13.419 15.295 1.00 17.57 C ANISOU 1009 CD1 LEU A 129 2425 2448 1804 -97 303 -128 C ATOM 1010 CD2 LEU A 129 0.564 -15.277 14.833 1.00 19.01 C ANISOU 1010 CD2 LEU A 129 2563 2636 2024 -44 87 65 C ATOM 1011 N LYS A 130 1.110 -14.432 20.316 1.00 44.68 N ANISOU 1011 N LYS A 130 6254 6490 4234 -132 -106 -83 N ATOM 1012 CA LYS A 130 1.958 -13.951 21.413 1.00 46.44 C ANISOU 1012 CA LYS A 130 6536 6897 4211 -139 -284 -214 C ATOM 1013 C LYS A 130 2.630 -15.103 22.170 1.00 47.80 C ANISOU 1013 C LYS A 130 6824 7179 4157 -65 -505 2 C ATOM 1014 O LYS A 130 3.814 -15.013 22.507 1.00 48.89 O ANISOU 1014 O LYS A 130 6908 7416 4252 -16 -771 -69 O ATOM 1015 CB LYS A 130 1.165 -13.074 22.381 1.00 46.77 C ANISOU 1015 CB LYS A 130 6691 7069 4013 -209 -128 -399 C ATOM 1016 CG LYS A 130 0.552 -11.835 21.753 1.00 45.83 C ANISOU 1016 CG LYS A 130 6464 6817 4133 -251 53 -631 C ATOM 1017 CD LYS A 130 1.614 -10.783 21.459 1.00 46.16 C ANISOU 1017 CD LYS A 130 6388 6806 4345 -281 -93 -859 C ATOM 1018 CE LYS A 130 0.984 -9.398 21.281 1.00 45.50 C ANISOU 1018 CE LYS A 130 6271 6598 4417 -324 74 -1115 C ATOM 1019 NZ LYS A 130 1.943 -8.288 21.591 1.00 46.21 N1+ ANISOU 1019 NZ LYS A 130 6312 6684 4563 -395 -55 -1397 N1+ ATOM 1020 N LYS A 131 1.893 -16.184 22.430 1.00 53.10 N ANISOU 1020 N LYS A 131 7648 7821 4708 -54 -408 267 N ATOM 1021 CA LYS A 131 2.540 -17.363 23.000 1.00 54.34 C ANISOU 1021 CA LYS A 131 7933 8010 4704 39 -633 526 C ATOM 1022 C LYS A 131 3.626 -17.893 22.062 1.00 54.07 C ANISOU 1022 C LYS A 131 7709 7837 4998 157 -848 560 C ATOM 1023 O LYS A 131 4.696 -18.289 22.518 1.00 55.31 O ANISOU 1023 O LYS A 131 7863 8069 5084 268 -1145 611 O ATOM 1024 CB LYS A 131 1.549 -18.486 23.288 1.00 54.36 C ANISOU 1024 CB LYS A 131 8131 7931 4592 6 -461 831 C ATOM 1025 CG LYS A 131 0.275 -18.057 23.943 1.00 54.82 C ANISOU 1025 CG LYS A 131 8287 8081 4463 -108 -143 773 C ATOM 1026 CD LYS A 131 -0.666 -19.251 24.063 1.00 55.63 C ANISOU 1026 CD LYS A 131 8470 8058 4609 -138 57 1051 C ATOM 1027 CE LYS A 131 -0.164 -20.262 25.098 1.00 59.28 C ANISOU 1027 CE LYS A 131 9091 8574 4861 -43 -90 1320 C ATOM 1028 NZ LYS A 131 1.193 -20.805 24.809 1.00 59.36 N1+ ANISOU 1028 NZ LYS A 131 9062 8519 4973 105 -446 1416 N1+ ATOM 1029 N ARG A 132 3.365 -17.906 20.756 1.00 48.38 N ANISOU 1029 N ARG A 132 6823 6932 4629 143 -707 517 N ATOM 1030 CA ARG A 132 4.357 -18.505 19.865 1.00 48.27 C ANISOU 1030 CA ARG A 132 6633 6801 4906 253 -870 536 C ATOM 1031 C ARG A 132 5.549 -17.608 19.454 1.00 48.67 C ANISOU 1031 C ARG A 132 6449 6926 5118 260 -1006 282 C ATOM 1032 O ARG A 132 6.485 -18.066 18.794 1.00 48.58 O ANISOU 1032 O ARG A 132 6260 6856 5341 351 -1134 263 O ATOM 1033 CB ARG A 132 3.673 -19.175 18.666 1.00 46.78 C ANISOU 1033 CB ARG A 132 6391 6396 4988 248 -690 620 C ATOM 1034 CG ARG A 132 2.916 -20.429 19.099 1.00 46.96 C ANISOU 1034 CG ARG A 132 6608 6307 4927 260 -640 897 C ATOM 1035 CD ARG A 132 1.957 -21.001 18.050 1.00 45.57 C ANISOU 1035 CD ARG A 132 6390 5933 4992 211 -434 938 C ATOM 1036 NE ARG A 132 1.032 -21.925 18.712 1.00 46.13 N ANISOU 1036 NE ARG A 132 6661 5920 4946 151 -326 1178 N ATOM 1037 CZ ARG A 132 0.282 -21.587 19.768 1.00 46.98 C ANISOU 1037 CZ ARG A 132 6931 6160 4758 46 -192 1240 C ATOM 1038 NH1 ARG A 132 0.337 -20.349 20.253 1.00 47.20 N1+ ANISOU 1038 NH1 ARG A 132 6941 6398 4596 9 -170 1052 N1+ ATOM 1039 NH2 ARG A 132 -0.523 -22.477 20.348 1.00 47.61 N ANISOU 1039 NH2 ARG A 132 7193 6159 4736 -35 -60 1476 N ATOM 1040 N THR A 133 5.532 -16.351 19.886 1.00 60.75 N ANISOU 1040 N THR A 133 8456 7584 7043 1389 -1380 1916 N ATOM 1041 CA THR A 133 6.578 -15.394 19.533 1.00 61.09 C ANISOU 1041 CA THR A 133 8665 7367 7179 1125 -1430 2050 C ATOM 1042 C THR A 133 7.277 -14.867 20.781 1.00 58.92 C ANISOU 1042 C THR A 133 8357 6927 7104 1160 -1194 1988 C ATOM 1043 O THR A 133 6.783 -14.990 21.908 1.00 57.72 O ANISOU 1043 O THR A 133 8059 6731 7142 1263 -1146 1869 O ATOM 1044 CB THR A 133 6.016 -14.215 18.680 1.00 64.72 C ANISOU 1044 CB THR A 133 9319 7747 7526 1408 -1481 2155 C ATOM 1045 CG2 THR A 133 5.367 -14.763 17.413 1.00 67.31 C ANISOU 1045 CG2 THR A 133 9543 8467 7565 1543 -1510 2316 C ATOM 1046 OG1 THR A 133 5.034 -13.491 19.437 1.00 65.67 O ANISOU 1046 OG1 THR A 133 9234 7767 7950 1603 -1510 2188 O ATOM 1047 N GLY A 134 8.449 -14.291 20.590 1.00 84.43 N ANISOU 1047 N GLY A 134 11718 10078 10283 1072 -1037 2069 N ATOM 1048 CA GLY A 134 9.247 -13.950 21.745 1.00 82.46 C ANISOU 1048 CA GLY A 134 11442 9702 10185 1068 -796 1958 C ATOM 1049 C GLY A 134 10.094 -15.135 22.192 1.00 79.63 C ANISOU 1049 C GLY A 134 11074 9488 9693 964 -651 1805 C ATOM 1050 O GLY A 134 10.581 -15.914 21.367 1.00 79.60 O ANISOU 1050 O GLY A 134 11152 9644 9448 874 -656 1810 O ATOM 1051 N PRO A 135 10.281 -15.262 23.516 1.00 61.37 N ANISOU 1051 N PRO A 135 8675 7114 7531 987 -514 1660 N ATOM 1052 CA PRO A 135 11.192 -16.238 24.144 1.00 58.77 C ANISOU 1052 CA PRO A 135 8352 6868 7110 902 -375 1515 C ATOM 1053 C PRO A 135 10.626 -17.659 24.062 1.00 57.85 C ANISOU 1053 C PRO A 135 8182 6930 6870 893 -487 1429 C ATOM 1054 O PRO A 135 9.470 -17.878 24.438 1.00 58.47 O ANISOU 1054 O PRO A 135 8131 7032 7051 971 -604 1414 O ATOM 1055 CB PRO A 135 11.254 -15.767 25.598 1.00 58.05 C ANISOU 1055 CB PRO A 135 8184 6638 7233 945 -243 1422 C ATOM 1056 CG PRO A 135 9.858 -15.104 25.830 1.00 59.80 C ANISOU 1056 CG PRO A 135 8286 6778 7657 1093 -344 1461 C ATOM 1057 CD PRO A 135 9.380 -14.601 24.487 1.00 61.80 C ANISOU 1057 CD PRO A 135 8597 7032 7851 1120 -516 1624 C ATOM 1058 N ALA A 136 11.438 -18.620 23.631 1.00 40.35 N ANISOU 1058 N ALA A 136 6051 4824 4458 806 -442 1363 N ATOM 1059 CA ALA A 136 10.961 -19.989 23.443 1.00 40.08 C ANISOU 1059 CA ALA A 136 6001 4928 4301 786 -556 1270 C ATOM 1060 C ALA A 136 10.865 -20.745 24.781 1.00 38.64 C ANISOU 1060 C ALA A 136 5724 4734 4223 791 -514 1143 C ATOM 1061 O ALA A 136 10.118 -21.718 24.925 1.00 39.00 O ANISOU 1061 O ALA A 136 5688 4856 4272 760 -628 1061 O ATOM 1062 CB ALA A 136 11.850 -20.734 22.445 1.00 40.24 C ANISOU 1062 CB ALA A 136 6170 5044 4074 715 -510 1229 C ATOM 1063 N ALA A 137 11.618 -20.277 25.763 1.00 29.13 N ANISOU 1063 N ALA A 137 4488 3440 3140 765 -348 1099 N ATOM 1064 CA ALA A 137 11.521 -20.834 27.097 1.00 28.72 C ANISOU 1064 CA ALA A 137 4314 3392 3207 714 -297 966 C ATOM 1065 C ALA A 137 11.375 -19.713 28.091 1.00 29.25 C ANISOU 1065 C ALA A 137 4310 3352 3452 747 -202 959 C ATOM 1066 O ALA A 137 11.886 -18.610 27.901 1.00 29.18 O ANISOU 1066 O ALA A 137 4369 3231 3487 773 -130 1027 O ATOM 1067 CB ALA A 137 12.746 -21.693 27.428 1.00 27.29 C ANISOU 1067 CB ALA A 137 4177 3235 2956 627 -206 877 C ATOM 1068 N THR A 138 10.663 -20.019 29.158 1.00 38.45 N ANISOU 1068 N THR A 138 5347 4543 4717 735 -191 868 N ATOM 1069 CA THR A 138 10.429 -19.094 30.248 1.00 39.90 C ANISOU 1069 CA THR A 138 5468 4641 5050 763 -80 808 C ATOM 1070 C THR A 138 11.619 -19.057 31.203 1.00 39.24 C ANISOU 1070 C THR A 138 5442 4531 4938 660 39 713 C ATOM 1071 O THR A 138 12.126 -20.099 31.624 1.00 38.37 O ANISOU 1071 O THR A 138 5331 4510 4739 570 32 663 O ATOM 1072 CB THR A 138 9.193 -19.537 31.037 1.00 42.30 C ANISOU 1072 CB THR A 138 5610 5021 5443 778 -86 743 C ATOM 1073 CG2 THR A 138 8.737 -18.448 31.996 1.00 44.51 C ANISOU 1073 CG2 THR A 138 5824 5208 5880 845 47 669 C ATOM 1074 OG1 THR A 138 8.145 -19.867 30.110 1.00 43.24 O ANISOU 1074 OG1 THR A 138 5644 5202 5584 841 -240 829 O ATOM 1075 N THR A 139 12.057 -17.853 31.548 1.00 33.68 N ANISOU 1075 N THR A 139 4784 3692 4322 669 130 691 N ATOM 1076 CA THR A 139 13.171 -17.688 32.465 1.00 33.73 C ANISOU 1076 CA THR A 139 4833 3674 4309 555 212 593 C ATOM 1077 C THR A 139 12.781 -18.062 33.895 1.00 35.86 C ANISOU 1077 C THR A 139 5045 4018 4561 504 258 454 C ATOM 1078 O THR A 139 11.841 -17.509 34.440 1.00 38.41 O ANISOU 1078 O THR A 139 5321 4304 4970 568 320 386 O ATOM 1079 CB THR A 139 13.668 -16.246 32.388 1.00 34.29 C ANISOU 1079 CB THR A 139 4977 3555 4495 559 285 599 C ATOM 1080 CG2 THR A 139 14.586 -15.906 33.549 1.00 35.50 C ANISOU 1080 CG2 THR A 139 5157 3676 4655 430 352 457 C ATOM 1081 OG1 THR A 139 14.378 -16.089 31.151 1.00 32.72 O ANISOU 1081 OG1 THR A 139 4848 3321 4261 554 265 746 O ATOM 1082 N LEU A 140 13.497 -19.010 34.497 1.00 24.73 N ANISOU 1082 N LEU A 140 3639 2717 3039 396 234 419 N ATOM 1083 CA LEU A 140 13.244 -19.393 35.896 1.00 26.86 C ANISOU 1083 CA LEU A 140 3887 3076 3244 325 274 314 C ATOM 1084 C LEU A 140 14.294 -18.782 36.842 1.00 28.27 C ANISOU 1084 C LEU A 140 4134 3225 3384 218 306 210 C ATOM 1085 O LEU A 140 15.492 -19.068 36.736 1.00 26.51 O ANISOU 1085 O LEU A 140 3928 3019 3126 142 244 244 O ATOM 1086 CB LEU A 140 13.161 -20.917 36.073 1.00 24.86 C ANISOU 1086 CB LEU A 140 3596 2958 2890 273 202 367 C ATOM 1087 CG LEU A 140 12.291 -21.734 35.107 1.00 23.75 C ANISOU 1087 CG LEU A 140 3396 2850 2777 335 133 455 C ATOM 1088 CD1 LEU A 140 12.637 -23.222 35.221 1.00 21.77 C ANISOU 1088 CD1 LEU A 140 3149 2674 2450 263 56 500 C ATOM 1089 CD2 LEU A 140 10.785 -21.502 35.303 1.00 26.64 C ANISOU 1089 CD2 LEU A 140 3658 3240 3222 393 179 436 C ATOM 1090 N PRO A 141 13.843 -17.856 37.704 1.00 40.91 N ANISOU 1090 N PRO A 141 5765 4770 5009 217 405 71 N ATOM 1091 CA PRO A 141 14.661 -17.136 38.695 1.00 42.21 C ANISOU 1091 CA PRO A 141 6013 4897 5127 101 431 -74 C ATOM 1092 C PRO A 141 15.082 -17.965 39.921 1.00 41.89 C ANISOU 1092 C PRO A 141 5999 5035 4884 -31 381 -124 C ATOM 1093 O PRO A 141 16.093 -17.623 40.568 1.00 42.52 O ANISOU 1093 O PRO A 141 6137 5120 4900 -155 326 -204 O ATOM 1094 CB PRO A 141 13.779 -15.952 39.090 1.00 43.21 C ANISOU 1094 CB PRO A 141 6172 4891 5353 177 571 -221 C ATOM 1095 CG PRO A 141 12.386 -16.419 38.850 1.00 43.38 C ANISOU 1095 CG PRO A 141 6091 4978 5414 308 626 -167 C ATOM 1096 CD PRO A 141 12.447 -17.385 37.685 1.00 42.07 C ANISOU 1096 CD PRO A 141 5857 4874 5254 342 500 34 C ATOM 1097 N ASP A 142 14.355 -19.048 40.213 1.00 41.71 N ANISOU 1097 N ASP A 142 5930 5153 4764 -17 382 -59 N ATOM 1098 CA ASP A 142 14.643 -19.844 41.406 1.00 41.04 C ANISOU 1098 CA ASP A 142 5889 5234 4472 -139 338 -68 C ATOM 1099 C ASP A 142 13.877 -21.156 41.443 1.00 39.35 C ANISOU 1099 C ASP A 142 5616 5135 4199 -126 331 61 C ATOM 1100 O ASP A 142 13.075 -21.441 40.531 1.00 38.92 O ANISOU 1100 O ASP A 142 5477 5040 4272 -29 353 134 O ATOM 1101 CB ASP A 142 14.313 -19.036 42.662 1.00 43.18 C ANISOU 1101 CB ASP A 142 6255 5537 4615 -202 455 -267 C ATOM 1102 CG ASP A 142 12.849 -18.607 42.710 1.00 44.63 C ANISOU 1102 CG ASP A 142 6394 5694 4869 -91 651 -348 C ATOM 1103 OD1 ASP A 142 11.973 -19.342 42.162 1.00 44.00 O ANISOU 1103 OD1 ASP A 142 6202 5656 4861 -14 670 -222 O ATOM 1104 OD2 ASP A 142 12.583 -17.530 43.297 1.00 46.32 O1- ANISOU 1104 OD2 ASP A 142 6678 5839 5085 -81 783 -548 O1- ATOM 1105 N GLY A 143 14.101 -21.919 42.522 1.00 22.31 N ANISOU 1105 N GLY A 143 3513 3119 1847 -238 290 94 N ATOM 1106 CA GLY A 143 13.588 -23.274 42.651 1.00 21.85 C ANISOU 1106 CA GLY A 143 3419 3149 1735 -263 263 247 C ATOM 1107 C GLY A 143 12.079 -23.374 42.697 1.00 22.46 C ANISOU 1107 C GLY A 143 3423 3262 1847 -227 424 235 C ATOM 1108 O GLY A 143 11.475 -24.276 42.108 1.00 21.80 O ANISOU 1108 O GLY A 143 3255 3172 1854 -205 398 355 O ATOM 1109 N ALA A 144 11.463 -22.453 43.425 1.00 24.07 N ANISOU 1109 N ALA A 144 3651 3503 1991 -225 595 78 N ATOM 1110 CA ALA A 144 10.009 -22.375 43.446 1.00 25.62 C ANISOU 1110 CA ALA A 144 3732 3733 2268 -168 777 47 C ATOM 1111 C ALA A 144 9.443 -22.281 42.009 1.00 25.82 C ANISOU 1111 C ALA A 144 3611 3637 2562 -29 730 106 C ATOM 1112 O ALA A 144 8.438 -22.914 41.685 1.00 26.09 O ANISOU 1112 O ALA A 144 3511 3712 2690 -14 758 187 O ATOM 1113 CB ALA A 144 9.546 -21.184 44.311 1.00 27.74 C ANISOU 1113 CB ALA A 144 4046 4019 2474 -144 990 -175 C ATOM 1114 N ALA A 145 10.095 -21.498 41.152 1.00 36.10 N ANISOU 1114 N ALA A 145 4941 4797 3978 56 648 74 N ATOM 1115 CA ALA A 145 9.624 -21.330 39.770 1.00 36.24 C ANISOU 1115 CA ALA A 145 4854 4712 4202 185 585 142 C ATOM 1116 C ALA A 145 9.767 -22.625 38.999 1.00 34.15 C ANISOU 1116 C ALA A 145 4559 4474 3942 148 431 296 C ATOM 1117 O ALA A 145 8.834 -23.066 38.329 1.00 34.82 O ANISOU 1117 O ALA A 145 4527 4570 4134 189 401 359 O ATOM 1118 CB ALA A 145 10.369 -20.194 39.063 1.00 36.45 C ANISOU 1118 CB ALA A 145 4948 4580 4322 263 546 100 C ATOM 1119 N ALA A 146 10.940 -23.238 39.114 1.00 30.47 N ANISOU 1119 N ALA A 146 4192 4014 3372 71 328 346 N ATOM 1120 CA ALA A 146 11.193 -24.539 38.510 1.00 28.02 C ANISOU 1120 CA ALA A 146 3876 3704 3067 40 198 467 C ATOM 1121 C ALA A 146 10.111 -25.574 38.877 1.00 28.61 C ANISOU 1121 C ALA A 146 3873 3851 3144 -29 222 535 C ATOM 1122 O ALA A 146 9.505 -26.218 38.000 1.00 28.53 O ANISOU 1122 O ALA A 146 3792 3811 3236 -13 150 589 O ATOM 1123 CB ALA A 146 12.548 -25.018 38.922 1.00 25.84 C ANISOU 1123 CB ALA A 146 3692 3432 2695 -23 112 505 C ATOM 1124 N GLU A 147 9.876 -25.717 40.181 1.00 52.36 N ANISOU 1124 N GLU A 147 6903 6960 6030 -124 323 530 N ATOM 1125 CA GLU A 147 8.880 -26.651 40.701 1.00 53.03 C ANISOU 1125 CA GLU A 147 6917 7124 6107 -221 383 611 C ATOM 1126 C GLU A 147 7.489 -26.325 40.177 1.00 55.29 C ANISOU 1126 C GLU A 147 7021 7425 6561 -164 464 577 C ATOM 1127 O GLU A 147 6.779 -27.181 39.663 1.00 55.66 O ANISOU 1127 O GLU A 147 6966 7464 6717 -209 404 656 O ATOM 1128 CB GLU A 147 8.879 -26.624 42.235 1.00 53.68 C ANISOU 1128 CB GLU A 147 7075 7337 5985 -330 515 605 C ATOM 1129 CG GLU A 147 10.098 -27.272 42.848 1.00 52.29 C ANISOU 1129 CG GLU A 147 7052 7171 5643 -413 390 697 C ATOM 1130 CD GLU A 147 10.116 -27.220 44.381 1.00 53.48 C ANISOU 1130 CD GLU A 147 7310 7478 5533 -534 496 702 C ATOM 1131 OE1 GLU A 147 9.689 -26.195 44.974 1.00 55.30 O ANISOU 1131 OE1 GLU A 147 7547 7788 5676 -522 668 544 O ATOM 1132 OE2 GLU A 147 10.574 -28.213 44.999 1.00 52.76 O1- ANISOU 1132 OE2 GLU A 147 7309 7422 5314 -638 405 864 O1- ATOM 1133 N SER A 148 7.102 -25.071 40.317 1.00 38.60 N ANISOU 1133 N SER A 148 4856 5320 4488 -64 590 455 N ATOM 1134 CA SER A 148 5.824 -24.613 39.820 1.00 41.00 C ANISOU 1134 CA SER A 148 4960 5633 4986 27 657 427 C ATOM 1135 C SER A 148 5.654 -25.008 38.349 1.00 41.07 C ANISOU 1135 C SER A 148 4901 5564 5141 80 452 503 C ATOM 1136 O SER A 148 4.557 -25.356 37.913 1.00 42.67 O ANISOU 1136 O SER A 148 4921 5804 5489 77 425 544 O ATOM 1137 CB SER A 148 5.740 -23.098 39.992 1.00 42.71 C ANISOU 1137 CB SER A 148 5171 5802 5254 169 785 282 C ATOM 1138 OG SER A 148 4.490 -22.606 39.568 1.00 44.98 O ANISOU 1138 OG SER A 148 5240 6092 5759 286 849 265 O ATOM 1139 N LEU A 149 6.741 -24.966 37.584 1.00 34.85 N ANISOU 1139 N LEU A 149 4257 4680 4304 119 309 516 N ATOM 1140 CA LEU A 149 6.651 -25.290 36.164 1.00 34.83 C ANISOU 1140 CA LEU A 149 4233 4618 4384 168 128 569 C ATOM 1141 C LEU A 149 6.515 -26.793 35.906 1.00 33.77 C ANISOU 1141 C LEU A 149 4097 4490 4245 42 14 640 C ATOM 1142 O LEU A 149 5.611 -27.215 35.172 1.00 35.90 O ANISOU 1142 O LEU A 149 4248 4771 4623 27 -86 665 O ATOM 1143 CB LEU A 149 7.831 -24.715 35.368 1.00 32.27 C ANISOU 1143 CB LEU A 149 4059 4198 4003 249 52 558 C ATOM 1144 CG LEU A 149 7.901 -25.254 33.933 1.00 30.79 C ANISOU 1144 CG LEU A 149 3901 3970 3826 274 -123 607 C ATOM 1145 CD1 LEU A 149 6.754 -24.694 33.090 1.00 33.13 C ANISOU 1145 CD1 LEU A 149 4064 4282 4241 366 -196 632 C ATOM 1146 CD2 LEU A 149 9.240 -24.983 33.251 1.00 27.52 C ANISOU 1146 CD2 LEU A 149 3647 3484 3323 318 -159 607 C ATOM 1147 N VAL A 150 7.392 -27.610 36.498 1.00 29.75 N ANISOU 1147 N VAL A 150 3717 3960 3627 -51 11 673 N ATOM 1148 CA VAL A 150 7.293 -29.038 36.225 1.00 29.09 C ANISOU 1148 CA VAL A 150 3651 3831 3571 -160 -98 738 C ATOM 1149 C VAL A 150 5.945 -29.534 36.734 1.00 31.68 C ANISOU 1149 C VAL A 150 3810 4232 3994 -276 -38 783 C ATOM 1150 O VAL A 150 5.394 -30.500 36.231 1.00 32.49 O ANISOU 1150 O VAL A 150 3861 4293 4191 -368 -142 818 O ATOM 1151 CB VAL A 150 8.464 -29.905 36.816 1.00 26.20 C ANISOU 1151 CB VAL A 150 3441 3405 3107 -222 -123 795 C ATOM 1152 CG1 VAL A 150 9.671 -29.057 37.215 1.00 24.38 C ANISOU 1152 CG1 VAL A 150 3312 3185 2767 -146 -81 759 C ATOM 1153 CG2 VAL A 150 7.976 -30.792 37.964 1.00 26.34 C ANISOU 1153 CG2 VAL A 150 3440 3461 3108 -376 -58 896 C ATOM 1154 N GLU A 151 5.406 -28.836 37.724 1.00 74.99 N ANISOU 1154 N GLU A 151 9205 9825 9463 -277 144 768 N ATOM 1155 CA GLU A 151 4.174 -29.240 38.380 1.00 76.73 C ANISOU 1155 CA GLU A 151 9247 10142 9767 -393 263 815 C ATOM 1156 C GLU A 151 2.937 -28.963 37.535 1.00 79.39 C ANISOU 1156 C GLU A 151 9341 10512 10313 -349 209 791 C ATOM 1157 O GLU A 151 1.888 -29.568 37.748 1.00 80.39 O ANISOU 1157 O GLU A 151 9281 10700 10565 -472 247 844 O ATOM 1158 CB GLU A 151 4.047 -28.516 39.715 1.00 76.98 C ANISOU 1158 CB GLU A 151 9271 10292 9686 -394 508 780 C ATOM 1159 CG GLU A 151 2.925 -29.045 40.568 1.00 78.24 C ANISOU 1159 CG GLU A 151 9269 10571 9888 -540 683 846 C ATOM 1160 CD GLU A 151 2.963 -30.561 40.660 1.00 77.44 C ANISOU 1160 CD GLU A 151 9221 10415 9789 -736 590 998 C ATOM 1161 OE1 GLU A 151 4.030 -31.111 41.031 1.00 75.44 O ANISOU 1161 OE1 GLU A 151 9190 10094 9379 -781 521 1066 O ATOM 1162 OE2 GLU A 151 1.929 -31.203 40.346 1.00 78.81 O1- ANISOU 1162 OE2 GLU A 151 9203 10598 10143 -845 573 1055 O1- ATOM 1163 N SER A 152 3.072 -28.052 36.575 1.00 43.32 N ANISOU 1163 N SER A 152 4767 5904 5786 -181 110 729 N ATOM 1164 CA SER A 152 1.944 -27.548 35.804 1.00 45.48 C ANISOU 1164 CA SER A 152 4807 6221 6252 -98 39 720 C ATOM 1165 C SER A 152 1.588 -28.441 34.617 1.00 46.00 C ANISOU 1165 C SER A 152 4834 6251 6392 -175 -219 754 C ATOM 1166 O SER A 152 0.556 -28.258 33.967 1.00 47.09 O ANISOU 1166 O SER A 152 4755 6444 6694 -148 -330 765 O ATOM 1167 CB SER A 152 2.268 -26.136 35.290 1.00 46.01 C ANISOU 1167 CB SER A 152 4913 6245 6323 119 31 667 C ATOM 1168 OG SER A 152 3.293 -26.154 34.297 1.00 44.90 O ANISOU 1168 OG SER A 152 4985 6007 6067 165 -139 672 O ATOM 1169 N SER A 153 2.447 -29.394 34.298 1.00 56.08 N ANISOU 1169 N SER A 153 6322 7431 7554 -264 -329 759 N ATOM 1170 CA SER A 153 2.236 -30.150 33.073 1.00 56.44 C ANISOU 1170 CA SER A 153 6385 7425 7636 -323 -576 745 C ATOM 1171 C SER A 153 2.628 -31.597 33.265 1.00 55.40 C ANISOU 1171 C SER A 153 6383 7187 7479 -501 -619 759 C ATOM 1172 O SER A 153 3.461 -31.918 34.108 1.00 53.57 O ANISOU 1172 O SER A 153 6296 6902 7156 -528 -498 792 O ATOM 1173 CB SER A 153 3.019 -29.528 31.907 1.00 55.80 C ANISOU 1173 CB SER A 153 6475 7296 7430 -169 -708 700 C ATOM 1174 OG SER A 153 2.874 -30.282 30.702 1.00 55.90 O ANISOU 1174 OG SER A 153 6547 7270 7421 -231 -942 661 O ATOM 1175 N GLU A 154 2.015 -32.461 32.469 1.00 61.17 N ANISOU 1175 N GLU A 154 7063 7877 8301 -623 -810 735 N ATOM 1176 CA GLU A 154 2.285 -33.887 32.513 1.00 60.38 C ANISOU 1176 CA GLU A 154 7089 7629 8223 -796 -873 734 C ATOM 1177 C GLU A 154 3.753 -34.127 32.143 1.00 58.98 C ANISOU 1177 C GLU A 154 7210 7318 7882 -696 -893 679 C ATOM 1178 O GLU A 154 4.404 -35.036 32.672 1.00 57.23 O ANISOU 1178 O GLU A 154 7126 6962 7658 -766 -850 713 O ATOM 1179 CB GLU A 154 1.341 -34.609 31.536 1.00 61.77 C ANISOU 1179 CB GLU A 154 7164 7780 8526 -940 -1107 676 C ATOM 1180 CG GLU A 154 0.984 -36.042 31.915 1.00 61.69 C ANISOU 1180 CG GLU A 154 7152 7630 8656 -1191 -1135 706 C ATOM 1181 CD GLU A 154 0.086 -36.135 33.144 1.00 61.76 C ANISOU 1181 CD GLU A 154 6919 7729 8817 -1336 -952 845 C ATOM 1182 OE1 GLU A 154 -0.722 -35.205 33.391 1.00 62.48 O ANISOU 1182 OE1 GLU A 154 6754 8010 8975 -1275 -869 875 O ATOM 1183 OE2 GLU A 154 0.195 -37.157 33.861 1.00 60.95 O1- ANISOU 1183 OE2 GLU A 154 6887 7499 8773 -1507 -880 930 O1- ATOM 1184 N VAL A 155 4.259 -33.307 31.223 1.00 27.18 N ANISOU 1184 N VAL A 155 3268 3326 3734 -530 -955 608 N ATOM 1185 CA VAL A 155 5.668 -33.332 30.831 1.00 25.27 C ANISOU 1185 CA VAL A 155 3267 2992 3344 -415 -936 555 C ATOM 1186 C VAL A 155 6.192 -31.909 30.679 1.00 23.13 C ANISOU 1186 C VAL A 155 3010 2815 2963 -234 -856 564 C ATOM 1187 O VAL A 155 5.495 -31.049 30.140 1.00 23.86 O ANISOU 1187 O VAL A 155 2996 3005 3063 -172 -915 569 O ATOM 1188 CB VAL A 155 5.865 -34.046 29.489 1.00 26.32 C ANISOU 1188 CB VAL A 155 3549 3033 3419 -430 -1110 429 C ATOM 1189 CG1 VAL A 155 7.299 -33.919 29.028 1.00 24.32 C ANISOU 1189 CG1 VAL A 155 3507 2714 3017 -288 -1047 370 C ATOM 1190 CG2 VAL A 155 5.439 -35.514 29.598 1.00 27.43 C ANISOU 1190 CG2 VAL A 155 3708 3024 3691 -620 -1196 397 C ATOM 1191 N ALA A 156 7.413 -31.668 31.153 1.00 34.80 N ANISOU 1191 N ALA A 156 4609 4253 4360 -155 -735 577 N ATOM 1192 CA ALA A 156 8.049 -30.346 31.029 1.00 32.60 C ANISOU 1192 CA ALA A 156 4361 4033 3994 -9 -653 583 C ATOM 1193 C ALA A 156 9.557 -30.477 30.844 1.00 29.61 C ANISOU 1193 C ALA A 156 4148 3580 3522 59 -602 555 C ATOM 1194 O ALA A 156 10.143 -31.476 31.269 1.00 28.89 O ANISOU 1194 O ALA A 156 4119 3400 3456 12 -594 555 O ATOM 1195 CB ALA A 156 7.744 -29.461 32.264 1.00 32.61 C ANISOU 1195 CB ALA A 156 4243 4110 4038 3 -508 638 C ATOM 1196 N VAL A 157 10.173 -29.465 30.231 1.00 32.78 N ANISOU 1196 N VAL A 157 4604 4010 3840 169 -564 546 N ATOM 1197 CA VAL A 157 11.596 -29.499 29.904 1.00 30.88 C ANISOU 1197 CA VAL A 157 4485 3720 3529 235 -501 519 C ATOM 1198 C VAL A 157 12.326 -28.240 30.348 1.00 29.42 C ANISOU 1198 C VAL A 157 4283 3568 3326 296 -386 561 C ATOM 1199 O VAL A 157 11.884 -27.114 30.068 1.00 29.98 O ANISOU 1199 O VAL A 157 4325 3679 3388 342 -373 589 O ATOM 1200 CB VAL A 157 11.831 -29.678 28.380 1.00 31.67 C ANISOU 1200 CB VAL A 157 4707 3810 3515 284 -557 452 C ATOM 1201 CG1 VAL A 157 13.313 -29.527 28.051 1.00 30.35 C ANISOU 1201 CG1 VAL A 157 4628 3615 3288 361 -440 431 C ATOM 1202 CG2 VAL A 157 11.306 -31.037 27.904 1.00 33.83 C ANISOU 1202 CG2 VAL A 157 5033 4020 3802 210 -677 367 C ATOM 1203 N ILE A 158 13.452 -28.419 31.030 1.00 24.51 N ANISOU 1203 N ILE A 158 3678 2917 2719 295 -318 567 N ATOM 1204 CA ILE A 158 14.219 -27.269 31.517 1.00 23.64 C ANISOU 1204 CA ILE A 158 3548 2830 2605 321 -226 590 C ATOM 1205 C ILE A 158 15.669 -27.338 31.088 1.00 23.07 C ANISOU 1205 C ILE A 158 3514 2729 2521 364 -173 580 C ATOM 1206 O ILE A 158 16.290 -28.419 31.128 1.00 23.19 O ANISOU 1206 O ILE A 158 3542 2704 2567 372 -192 565 O ATOM 1207 CB ILE A 158 14.197 -27.175 33.039 1.00 23.86 C ANISOU 1207 CB ILE A 158 3518 2886 2661 255 -200 612 C ATOM 1208 CG1 ILE A 158 12.762 -26.991 33.545 1.00 25.23 C ANISOU 1208 CG1 ILE A 158 3626 3104 2855 216 -199 616 C ATOM 1209 CG2 ILE A 158 15.087 -26.035 33.515 1.00 23.65 C ANISOU 1209 CG2 ILE A 158 3487 2871 2629 259 -128 604 C ATOM 1210 CD1 ILE A 158 12.670 -27.004 35.067 1.00 25.65 C ANISOU 1210 CD1 ILE A 158 3649 3209 2889 137 -147 629 C ATOM 1211 N GLY A 159 16.169 -26.222 30.555 1.00 23.55 N ANISOU 1211 N GLY A 159 3591 2801 2558 397 -99 594 N ATOM 1212 CA GLY A 159 17.572 -26.100 30.266 1.00 23.83 C ANISOU 1212 CA GLY A 159 3620 2827 2607 419 -18 595 C ATOM 1213 C GLY A 159 18.305 -25.314 31.305 1.00 24.28 C ANISOU 1213 C GLY A 159 3602 2892 2731 366 16 614 C ATOM 1214 O GLY A 159 17.848 -24.248 31.722 1.00 24.43 O ANISOU 1214 O GLY A 159 3621 2905 2757 334 30 619 O ATOM 1215 N PHE A 160 19.542 -25.726 31.558 1.00 22.99 N ANISOU 1215 N PHE A 160 3373 2733 2629 365 34 616 N ATOM 1216 CA PHE A 160 20.359 -25.116 32.579 1.00 24.20 C ANISOU 1216 CA PHE A 160 3442 2908 2845 295 26 627 C ATOM 1217 C PHE A 160 21.582 -24.559 31.877 1.00 26.20 C ANISOU 1217 C PHE A 160 3632 3160 3162 299 129 641 C ATOM 1218 O PHE A 160 22.412 -25.303 31.393 1.00 27.60 O ANISOU 1218 O PHE A 160 3751 3347 3390 357 168 643 O ATOM 1219 CB PHE A 160 20.785 -26.184 33.596 1.00 24.66 C ANISOU 1219 CB PHE A 160 3440 2988 2942 284 -78 647 C ATOM 1220 CG PHE A 160 19.630 -26.806 34.363 1.00 23.21 C ANISOU 1220 CG PHE A 160 3315 2810 2694 254 -159 658 C ATOM 1221 CD1 PHE A 160 18.850 -27.811 33.788 1.00 22.19 C ANISOU 1221 CD1 PHE A 160 3243 2636 2554 300 -178 658 C ATOM 1222 CD2 PHE A 160 19.340 -26.389 35.667 1.00 23.40 C ANISOU 1222 CD2 PHE A 160 3341 2888 2661 164 -205 662 C ATOM 1223 CE1 PHE A 160 17.796 -28.381 34.485 1.00 21.59 C ANISOU 1223 CE1 PHE A 160 3198 2564 2442 248 -237 683 C ATOM 1224 CE2 PHE A 160 18.293 -26.953 36.378 1.00 22.69 C ANISOU 1224 CE2 PHE A 160 3296 2820 2503 124 -242 684 C ATOM 1225 CZ PHE A 160 17.512 -27.953 35.798 1.00 21.67 C ANISOU 1225 CZ PHE A 160 3197 2642 2393 162 -255 707 C ATOM 1226 N PHE A 161 21.690 -23.238 31.816 1.00 31.62 N ANISOU 1226 N PHE A 161 4327 3823 3864 236 188 651 N ATOM 1227 CA PHE A 161 22.791 -22.597 31.118 1.00 33.47 C ANISOU 1227 CA PHE A 161 4499 4051 4167 209 308 685 C ATOM 1228 C PHE A 161 23.267 -21.380 31.902 1.00 35.12 C ANISOU 1228 C PHE A 161 4655 4224 4465 79 299 677 C ATOM 1229 O PHE A 161 22.450 -20.544 32.317 1.00 34.29 O ANISOU 1229 O PHE A 161 4638 4056 4334 42 275 650 O ATOM 1230 CB PHE A 161 22.383 -22.233 29.674 1.00 32.38 C ANISOU 1230 CB PHE A 161 4477 3889 3937 264 424 732 C ATOM 1231 CG PHE A 161 22.063 -23.441 28.827 1.00 31.81 C ANISOU 1231 CG PHE A 161 4467 3855 3763 371 431 707 C ATOM 1232 CD1 PHE A 161 23.079 -24.146 28.194 1.00 33.97 C ANISOU 1232 CD1 PHE A 161 4680 4168 4060 422 539 688 C ATOM 1233 CD2 PHE A 161 20.759 -23.906 28.706 1.00 29.88 C ANISOU 1233 CD2 PHE A 161 4330 3603 3419 416 332 683 C ATOM 1234 CE1 PHE A 161 22.801 -25.286 27.446 1.00 34.14 C ANISOU 1234 CE1 PHE A 161 4782 4201 3991 520 550 625 C ATOM 1235 CE2 PHE A 161 20.469 -25.041 27.962 1.00 29.94 C ANISOU 1235 CE2 PHE A 161 4406 3628 3341 489 319 633 C ATOM 1236 CZ PHE A 161 21.499 -25.732 27.323 1.00 32.13 C ANISOU 1236 CZ PHE A 161 4656 3925 3626 543 430 594 C ATOM 1237 N LYS A 162 24.581 -21.285 32.110 1.00 47.62 N ANISOU 1237 N LYS A 162 6084 5841 6170 11 317 687 N ATOM 1238 CA LYS A 162 25.151 -20.131 32.809 1.00 49.24 C ANISOU 1238 CA LYS A 162 6231 6004 6474 -144 294 662 C ATOM 1239 C LYS A 162 24.964 -18.845 32.008 1.00 48.77 C ANISOU 1239 C LYS A 162 6263 5827 6440 -194 428 706 C ATOM 1240 O LYS A 162 24.391 -17.875 32.498 1.00 48.38 O ANISOU 1240 O LYS A 162 6308 5673 6400 -257 401 662 O ATOM 1241 CB LYS A 162 26.626 -20.352 33.113 1.00 51.81 C ANISOU 1241 CB LYS A 162 6333 6402 6949 -215 268 676 C ATOM 1242 CG LYS A 162 26.889 -21.627 33.886 1.00 53.19 C ANISOU 1242 CG LYS A 162 6412 6676 7122 -149 115 669 C ATOM 1243 CD LYS A 162 25.722 -21.966 34.837 1.00 51.80 C ANISOU 1243 CD LYS A 162 6391 6503 6790 -133 -20 624 C ATOM 1244 CE LYS A 162 25.849 -21.282 36.207 1.00 53.52 C ANISOU 1244 CE LYS A 162 6609 6745 6981 -288 -165 555 C ATOM 1245 NZ LYS A 162 24.591 -21.425 37.007 1.00 52.07 N1+ ANISOU 1245 NZ LYS A 162 6596 6565 6621 -278 -224 502 N1+ ATOM 1246 N ASP A 163 25.440 -18.843 30.772 1.00 56.83 N ANISOU 1246 N ASP A 163 7267 6856 7471 -162 583 797 N ATOM 1247 CA ASP A 163 25.166 -17.724 29.885 1.00 56.19 C ANISOU 1247 CA ASP A 163 7305 6661 7383 -195 709 886 C ATOM 1248 C ASP A 163 23.974 -18.076 29.028 1.00 54.11 C ANISOU 1248 C ASP A 163 7216 6400 6943 -49 718 930 C ATOM 1249 O ASP A 163 23.997 -19.065 28.311 1.00 53.89 O ANISOU 1249 O ASP A 163 7194 6471 6808 49 757 939 O ATOM 1250 CB ASP A 163 26.366 -17.421 29.003 1.00 57.95 C ANISOU 1250 CB ASP A 163 7423 6906 7689 -269 891 983 C ATOM 1251 CG ASP A 163 26.211 -16.124 28.225 1.00 57.77 C ANISOU 1251 CG ASP A 163 7527 6742 7682 -344 1016 1110 C ATOM 1252 OD1 ASP A 163 25.131 -15.866 27.631 1.00 56.14 O ANISOU 1252 OD1 ASP A 163 7516 6473 7343 -251 1010 1174 O ATOM 1253 OD2 ASP A 163 27.192 -15.349 28.209 1.00 59.46 O1- ANISOU 1253 OD2 ASP A 163 7634 6901 8057 -505 1110 1161 O1- ATOM 1254 N VAL A 164 22.931 -17.263 29.117 1.00 43.48 N ANISOU 1254 N VAL A 164 6002 4938 5580 -32 673 946 N ATOM 1255 CA VAL A 164 21.689 -17.524 28.403 1.00 41.79 C ANISOU 1255 CA VAL A 164 5927 4732 5221 101 634 993 C ATOM 1256 C VAL A 164 21.805 -17.259 26.887 1.00 42.05 C ANISOU 1256 C VAL A 164 6064 4771 5141 132 751 1146 C ATOM 1257 O VAL A 164 20.998 -17.750 26.094 1.00 41.20 O ANISOU 1257 O VAL A 164 6062 4724 4869 236 708 1183 O ATOM 1258 CB VAL A 164 20.525 -16.732 29.060 1.00 41.19 C ANISOU 1258 CB VAL A 164 5920 4532 5200 130 548 960 C ATOM 1259 CG1 VAL A 164 19.623 -16.067 28.033 1.00 40.80 C ANISOU 1259 CG1 VAL A 164 6003 4400 5100 219 553 1098 C ATOM 1260 CG2 VAL A 164 19.742 -17.640 29.965 1.00 40.51 C ANISOU 1260 CG2 VAL A 164 5795 4530 5069 185 431 840 C ATOM 1261 N GLU A 165 22.809 -16.478 26.497 1.00 49.40 N ANISOU 1261 N GLU A 165 6970 5649 6150 25 895 1239 N ATOM 1262 CA GLU A 165 23.036 -16.143 25.094 1.00 50.40 C ANISOU 1262 CA GLU A 165 7209 5793 6150 27 1038 1409 C ATOM 1263 C GLU A 165 24.096 -17.019 24.419 1.00 51.32 C ANISOU 1263 C GLU A 165 7246 6073 6180 21 1199 1395 C ATOM 1264 O GLU A 165 24.414 -16.806 23.246 1.00 52.90 O ANISOU 1264 O GLU A 165 7540 6320 6241 9 1359 1526 O ATOM 1265 CB GLU A 165 23.412 -14.661 24.955 1.00 52.17 C ANISOU 1265 CB GLU A 165 7473 5834 6514 -97 1131 1555 C ATOM 1266 CG GLU A 165 22.407 -13.723 25.612 1.00 51.92 C ANISOU 1266 CG GLU A 165 7521 5602 6604 -71 999 1550 C ATOM 1267 CD GLU A 165 21.004 -13.893 25.047 1.00 51.36 C ANISOU 1267 CD GLU A 165 7572 5563 6380 93 856 1585 C ATOM 1268 OE1 GLU A 165 20.859 -13.841 23.812 1.00 52.41 O ANISOU 1268 OE1 GLU A 165 7787 5778 6350 117 853 1692 O ATOM 1269 OE2 GLU A 165 20.046 -14.089 25.832 1.00 50.32 O1- ANISOU 1269 OE2 GLU A 165 7436 5392 6293 184 735 1495 O1- ATOM 1270 N SER A 166 24.640 -17.986 25.155 1.00 34.76 N ANISOU 1270 N SER A 166 4981 4061 4165 35 1165 1246 N ATOM 1271 CA SER A 166 25.656 -18.903 24.628 1.00 36.45 C ANISOU 1271 CA SER A 166 5085 4413 4350 63 1320 1205 C ATOM 1272 C SER A 166 25.095 -19.805 23.532 1.00 36.21 C ANISOU 1272 C SER A 166 5218 4483 4055 195 1354 1181 C ATOM 1273 O SER A 166 23.877 -19.946 23.382 1.00 34.55 O ANISOU 1273 O SER A 166 5169 4254 3705 265 1201 1175 O ATOM 1274 CB SER A 166 26.229 -19.785 25.739 1.00 37.12 C ANISOU 1274 CB SER A 166 4959 4543 4603 80 1226 1065 C ATOM 1275 OG SER A 166 25.292 -20.794 26.097 1.00 35.70 O ANISOU 1275 OG SER A 166 4852 4380 4331 197 1058 964 O ATOM 1276 N ASP A 167 26.007 -20.401 22.769 1.00 50.67 N ANISOU 1276 N ASP A 167 6998 6425 5829 223 1561 1156 N ATOM 1277 CA ASP A 167 25.691 -21.271 21.640 1.00 51.24 C ANISOU 1277 CA ASP A 167 7238 6601 5632 332 1637 1098 C ATOM 1278 C ASP A 167 24.691 -22.390 21.954 1.00 50.04 C ANISOU 1278 C ASP A 167 7163 6440 5409 445 1419 948 C ATOM 1279 O ASP A 167 23.653 -22.516 21.289 1.00 49.32 O ANISOU 1279 O ASP A 167 7280 6369 5090 485 1319 953 O ATOM 1280 CB ASP A 167 27.000 -21.872 21.128 1.00 54.03 C ANISOU 1280 CB ASP A 167 7452 7057 6018 360 1909 1034 C ATOM 1281 CG ASP A 167 26.846 -22.600 19.794 1.00 55.51 C ANISOU 1281 CG ASP A 167 7843 7359 5890 452 2059 962 C ATOM 1282 OD1 ASP A 167 25.961 -22.216 18.986 1.00 54.96 O ANISOU 1282 OD1 ASP A 167 8028 7311 5543 438 1995 1039 O ATOM 1283 OD2 ASP A 167 27.630 -23.549 19.541 1.00 57.63 O1- ANISOU 1283 OD2 ASP A 167 8011 7692 6193 541 2231 819 O1- ATOM 1284 N SER A 168 25.003 -23.205 22.959 1.00 34.43 N ANISOU 1284 N SER A 168 5015 4436 3632 485 1334 830 N ATOM 1285 CA SER A 168 24.166 -24.349 23.328 1.00 33.49 C ANISOU 1285 CA SER A 168 4952 4290 3484 572 1148 700 C ATOM 1286 C SER A 168 22.816 -23.928 23.871 1.00 30.53 C ANISOU 1286 C SER A 168 4666 3856 3079 540 917 743 C ATOM 1287 O SER A 168 21.814 -24.646 23.713 1.00 29.55 O ANISOU 1287 O SER A 168 4651 3727 2848 588 777 673 O ATOM 1288 CB SER A 168 24.868 -25.203 24.369 1.00 34.70 C ANISOU 1288 CB SER A 168 4898 4411 3876 612 1104 616 C ATOM 1289 OG SER A 168 26.010 -25.815 23.802 1.00 37.83 O ANISOU 1289 OG SER A 168 5196 4856 4324 685 1314 551 O ATOM 1290 N ALA A 169 22.804 -22.768 24.523 1.00 38.69 N ANISOU 1290 N ALA A 169 5638 4836 4227 456 886 845 N ATOM 1291 CA ALA A 169 21.580 -22.184 25.032 1.00 36.35 C ANISOU 1291 CA ALA A 169 5406 4476 3930 439 713 885 C ATOM 1292 C ALA A 169 20.706 -21.910 23.825 1.00 36.19 C ANISOU 1292 C ALA A 169 5578 4484 3689 478 690 958 C ATOM 1293 O ALA A 169 19.519 -22.226 23.809 1.00 35.21 O ANISOU 1293 O ALA A 169 5522 4362 3497 519 524 934 O ATOM 1294 CB ALA A 169 21.883 -20.897 25.773 1.00 36.01 C ANISOU 1294 CB ALA A 169 5288 4349 4046 346 729 962 C ATOM 1295 N LYS A 170 21.311 -21.342 22.794 1.00 39.45 N ANISOU 1295 N LYS A 170 6071 4932 3985 455 853 1059 N ATOM 1296 CA LYS A 170 20.593 -21.024 21.579 1.00 40.40 C ANISOU 1296 CA LYS A 170 6395 5099 3856 483 825 1161 C ATOM 1297 C LYS A 170 20.079 -22.255 20.836 1.00 41.02 C ANISOU 1297 C LYS A 170 6594 5279 3714 550 754 1033 C ATOM 1298 O LYS A 170 18.993 -22.222 20.241 1.00 41.33 O ANISOU 1298 O LYS A 170 6740 5350 3613 564 578 1055 O ATOM 1299 CB LYS A 170 21.467 -20.171 20.670 1.00 42.73 C ANISOU 1299 CB LYS A 170 6730 5420 4085 411 1020 1288 C ATOM 1300 CG LYS A 170 21.864 -18.839 21.311 1.00 42.99 C ANISOU 1300 CG LYS A 170 6667 5319 4346 319 1062 1413 C ATOM 1301 CD LYS A 170 20.661 -17.957 21.569 1.00 42.56 C ANISOU 1301 CD LYS A 170 6652 5154 4363 330 851 1482 C ATOM 1302 CE LYS A 170 21.086 -16.606 22.139 1.00 43.15 C ANISOU 1302 CE LYS A 170 6669 5064 4662 239 907 1584 C ATOM 1303 NZ LYS A 170 19.899 -15.729 22.423 1.00 42.97 N1+ ANISOU 1303 NZ LYS A 170 6682 4910 4735 279 725 1637 N1+ ATOM 1304 N GLN A 171 20.828 -23.345 20.850 1.00 37.62 N ANISOU 1304 N GLN A 171 6111 4888 3297 579 859 873 N ATOM 1305 CA GLN A 171 20.258 -24.545 20.244 1.00 38.75 C ANISOU 1305 CA GLN A 171 6380 5084 3259 633 771 718 C ATOM 1306 C GLN A 171 19.056 -25.049 21.049 1.00 37.02 C ANISOU 1306 C GLN A 171 6115 4802 3147 638 507 658 C ATOM 1307 O GLN A 171 18.021 -25.441 20.491 1.00 37.28 O ANISOU 1307 O GLN A 171 6270 4871 3022 643 338 619 O ATOM 1308 CB GLN A 171 21.330 -25.618 20.032 1.00 41.25 C ANISOU 1308 CB GLN A 171 6660 5423 3592 684 961 548 C ATOM 1309 CG GLN A 171 22.357 -25.164 18.999 1.00 43.50 C ANISOU 1309 CG GLN A 171 7009 5807 3714 677 1249 601 C ATOM 1310 CD GLN A 171 23.332 -26.241 18.587 1.00 46.36 C ANISOU 1310 CD GLN A 171 7346 6203 4065 755 1468 410 C ATOM 1311 NE2 GLN A 171 24.610 -26.016 18.872 1.00 47.37 N ANISOU 1311 NE2 GLN A 171 7273 6339 4387 759 1698 441 N ATOM 1312 OE1 GLN A 171 22.948 -27.259 17.994 1.00 47.98 O ANISOU 1312 OE1 GLN A 171 7706 6421 4103 812 1432 228 O ATOM 1313 N PHE A 172 19.200 -25.034 22.370 1.00 38.85 N ANISOU 1313 N PHE A 172 6166 4953 3642 623 471 653 N ATOM 1314 CA PHE A 172 18.123 -25.445 23.261 1.00 37.06 C ANISOU 1314 CA PHE A 172 5877 4675 3528 612 266 616 C ATOM 1315 C PHE A 172 16.865 -24.640 22.962 1.00 36.20 C ANISOU 1315 C PHE A 172 5825 4584 3345 606 112 722 C ATOM 1316 O PHE A 172 15.767 -25.191 22.880 1.00 36.27 O ANISOU 1316 O PHE A 172 5855 4609 3319 604 -64 676 O ATOM 1317 CB PHE A 172 18.534 -25.258 24.723 1.00 35.64 C ANISOU 1317 CB PHE A 172 5519 4430 3591 584 274 629 C ATOM 1318 CG PHE A 172 17.402 -25.423 25.696 1.00 33.91 C ANISOU 1318 CG PHE A 172 5238 4178 3469 559 106 621 C ATOM 1319 CD1 PHE A 172 16.883 -26.678 25.969 1.00 34.01 C ANISOU 1319 CD1 PHE A 172 5246 4171 3503 555 3 528 C ATOM 1320 CD2 PHE A 172 16.858 -24.324 26.338 1.00 32.71 C ANISOU 1320 CD2 PHE A 172 5031 4001 3397 536 72 703 C ATOM 1321 CE1 PHE A 172 15.841 -26.833 26.864 1.00 33.06 C ANISOU 1321 CE1 PHE A 172 5055 4034 3470 515 -121 536 C ATOM 1322 CE2 PHE A 172 15.816 -24.472 27.235 1.00 31.96 C ANISOU 1322 CE2 PHE A 172 4865 3893 3386 518 -41 686 C ATOM 1323 CZ PHE A 172 15.307 -25.728 27.498 1.00 32.20 C ANISOU 1323 CZ PHE A 172 4879 3931 3425 500 -132 612 C ATOM 1324 N LEU A 173 17.034 -23.332 22.797 1.00 27.79 N ANISOU 1324 N LEU A 173 4772 3504 2283 601 175 872 N ATOM 1325 CA LEU A 173 15.923 -22.455 22.455 1.00 28.22 C ANISOU 1325 CA LEU A 173 4867 3553 2302 620 35 999 C ATOM 1326 C LEU A 173 15.391 -22.806 21.072 1.00 30.29 C ANISOU 1326 C LEU A 173 5260 3921 2327 618 -66 994 C ATOM 1327 O LEU A 173 14.199 -22.664 20.798 1.00 30.92 O ANISOU 1327 O LEU A 173 5320 4030 2400 623 -262 1032 O ATOM 1328 CB LEU A 173 16.362 -20.990 22.496 1.00 28.42 C ANISOU 1328 CB LEU A 173 4859 3505 2436 591 133 1137 C ATOM 1329 CG LEU A 173 16.768 -20.442 23.866 1.00 27.04 C ANISOU 1329 CG LEU A 173 4567 3215 2490 575 206 1135 C ATOM 1330 CD1 LEU A 173 17.403 -19.067 23.727 1.00 27.70 C ANISOU 1330 CD1 LEU A 173 4659 3206 2660 526 321 1257 C ATOM 1331 CD2 LEU A 173 15.570 -20.392 24.802 1.00 25.91 C ANISOU 1331 CD2 LEU A 173 4333 3029 2484 611 61 1100 C ATOM 1332 N GLN A 174 16.285 -23.268 20.204 1.00 52.71 N ANISOU 1332 N GLN A 174 8228 6829 4971 611 75 944 N ATOM 1333 CA GLN A 174 15.906 -23.679 18.858 1.00 55.09 C ANISOU 1333 CA GLN A 174 8680 7246 5004 594 -2 907 C ATOM 1334 C GLN A 174 14.916 -24.835 18.921 1.00 55.26 C ANISOU 1334 C GLN A 174 8731 7289 4975 600 -213 761 C ATOM 1335 O GLN A 174 13.924 -24.858 18.192 1.00 56.64 O ANISOU 1335 O GLN A 174 8942 7541 5036 571 -411 777 O ATOM 1336 CB GLN A 174 17.141 -24.085 18.052 1.00 57.04 C ANISOU 1336 CB GLN A 174 9051 7560 5060 590 238 834 C ATOM 1337 CG GLN A 174 17.454 -23.158 16.889 1.00 59.52 C ANISOU 1337 CG GLN A 174 9446 7961 5208 537 320 977 C ATOM 1338 CD GLN A 174 17.720 -21.733 17.334 1.00 58.94 C ANISOU 1338 CD GLN A 174 9267 7800 5329 506 376 1183 C ATOM 1339 NE2 GLN A 174 18.956 -21.279 17.157 1.00 59.79 N ANISOU 1339 NE2 GLN A 174 9367 7907 5445 468 628 1238 N ATOM 1340 OE1 GLN A 174 16.826 -21.049 17.832 1.00 58.08 O ANISOU 1340 OE1 GLN A 174 9077 7615 5374 514 202 1283 O ATOM 1341 N ALA A 175 15.191 -25.794 19.800 1.00 46.43 N ANISOU 1341 N ALA A 175 7563 6099 3978 616 -181 620 N ATOM 1342 CA ALA A 175 14.299 -26.939 19.989 1.00 47.22 C ANISOU 1342 CA ALA A 175 7645 6182 4116 581 -373 469 C ATOM 1343 C ALA A 175 13.021 -26.515 20.709 1.00 46.09 C ANISOU 1343 C ALA A 175 7344 6021 4149 564 -579 564 C ATOM 1344 O ALA A 175 11.944 -27.026 20.426 1.00 47.47 O ANISOU 1344 O ALA A 175 7517 6232 4287 523 -796 516 O ATOM 1345 CB ALA A 175 14.998 -28.066 20.738 1.00 47.31 C ANISOU 1345 CB ALA A 175 7586 6093 4296 579 -267 305 C ATOM 1346 N ALA A 176 13.132 -25.571 21.636 1.00 41.41 N ANISOU 1346 N ALA A 176 6609 5371 3753 591 -505 687 N ATOM 1347 CA ALA A 176 11.936 -25.081 22.311 1.00 41.00 C ANISOU 1347 CA ALA A 176 6400 5304 3873 596 -655 766 C ATOM 1348 C ALA A 176 10.940 -24.519 21.304 1.00 42.69 C ANISOU 1348 C ALA A 176 6646 5602 3974 615 -842 873 C ATOM 1349 O ALA A 176 9.743 -24.714 21.457 1.00 43.74 O ANISOU 1349 O ALA A 176 6668 5764 4188 607 -1038 878 O ATOM 1350 CB ALA A 176 12.279 -24.046 23.396 1.00 39.12 C ANISOU 1350 CB ALA A 176 6038 4983 3842 627 -521 854 C ATOM 1351 N GLU A 177 11.432 -23.833 20.275 1.00 55.04 N ANISOU 1351 N GLU A 177 8313 7214 5384 617 -772 959 N ATOM 1352 CA GLU A 177 10.560 -23.318 19.202 1.00 57.29 C ANISOU 1352 CA GLU A 177 8609 7599 5559 615 -945 1074 C ATOM 1353 C GLU A 177 9.849 -24.404 18.382 1.00 59.18 C ANISOU 1353 C GLU A 177 8921 7956 5610 560 -1149 952 C ATOM 1354 O GLU A 177 8.752 -24.194 17.864 1.00 60.98 O ANISOU 1354 O GLU A 177 9077 8271 5820 561 -1363 1027 O ATOM 1355 CB GLU A 177 11.349 -22.445 18.222 1.00 58.73 C ANISOU 1355 CB GLU A 177 8918 7816 5582 607 -820 1202 C ATOM 1356 CG GLU A 177 11.626 -21.009 18.661 1.00 58.40 C ANISOU 1356 CG GLU A 177 8801 7657 5730 640 -718 1382 C ATOM 1357 CD GLU A 177 12.664 -20.323 17.763 1.00 60.12 C ANISOU 1357 CD GLU A 177 9162 7893 5789 599 -558 1490 C ATOM 1358 OE1 GLU A 177 12.656 -20.567 16.533 1.00 62.57 O ANISOU 1358 OE1 GLU A 177 9603 8343 5825 564 -604 1516 O ATOM 1359 OE2 GLU A 177 13.505 -19.559 18.291 1.00 59.32 O1- ANISOU 1359 OE2 GLU A 177 9040 7673 5825 591 -383 1543 O1- ATOM 1360 N ALA A 178 10.472 -25.560 18.239 1.00 41.24 N ANISOU 1360 N ALA A 178 6789 5678 3200 515 -1089 759 N ATOM 1361 CA ALA A 178 9.892 -26.576 17.373 1.00 43.53 C ANISOU 1361 CA ALA A 178 7182 6057 3298 442 -1275 610 C ATOM 1362 C ALA A 178 8.750 -27.387 18.023 1.00 43.96 C ANISOU 1362 C ALA A 178 7099 6080 3524 384 -1507 520 C ATOM 1363 O ALA A 178 8.000 -28.076 17.337 1.00 45.98 O ANISOU 1363 O ALA A 178 7386 6409 3674 301 -1714 418 O ATOM 1364 CB ALA A 178 10.986 -27.492 16.843 1.00 44.09 C ANISOU 1364 CB ALA A 178 7478 6119 3155 420 -1110 415 C ATOM 1365 N ILE A 179 8.640 -27.292 19.336 1.00 48.02 N ANISOU 1365 N ILE A 179 7454 6489 4302 413 -1468 557 N ATOM 1366 CA ILE A 179 7.662 -28.042 20.097 1.00 48.88 C ANISOU 1366 CA ILE A 179 7394 6560 4617 337 -1635 489 C ATOM 1367 C ILE A 179 6.647 -27.147 20.765 1.00 48.86 C ANISOU 1367 C ILE A 179 7133 6579 4854 387 -1721 655 C ATOM 1368 O ILE A 179 6.979 -26.139 21.357 1.00 47.29 O ANISOU 1368 O ILE A 179 6866 6335 4768 485 -1565 778 O ATOM 1369 CB ILE A 179 8.327 -28.867 21.186 1.00 47.76 C ANISOU 1369 CB ILE A 179 7201 6285 4660 297 -1438 371 C ATOM 1370 CG1 ILE A 179 9.522 -29.609 20.629 1.00 48.16 C ANISOU 1370 CG1 ILE A 179 7481 6287 4530 297 -1294 218 C ATOM 1371 CG2 ILE A 179 7.358 -29.866 21.743 1.00 49.30 C ANISOU 1371 CG2 ILE A 179 7247 6440 5044 171 -1582 285 C ATOM 1372 CD1 ILE A 179 9.698 -30.974 21.223 1.00 48.98 C ANISOU 1372 CD1 ILE A 179 7574 6257 4779 218 -1262 50 C ATOM 1373 N ASP A 180 5.397 -27.550 20.665 1.00 77.47 N ANISOU 1373 N ASP A 180 10602 10265 8569 314 -1968 641 N ATOM 1374 CA ASP A 180 4.280 -26.744 21.091 1.00 78.40 C ANISOU 1374 CA ASP A 180 10440 10426 8921 375 -2059 785 C ATOM 1375 C ASP A 180 3.593 -27.337 22.295 1.00 79.02 C ANISOU 1375 C ASP A 180 10265 10463 9297 291 -2035 732 C ATOM 1376 O ASP A 180 3.006 -26.626 23.078 1.00 79.32 O ANISOU 1376 O ASP A 180 10071 10500 9567 364 -1974 830 O ATOM 1377 CB ASP A 180 3.262 -26.654 19.965 1.00 80.83 C ANISOU 1377 CB ASP A 180 10687 10878 9147 357 -2295 815 C ATOM 1378 CG ASP A 180 3.661 -25.679 18.892 1.00 80.88 C ANISOU 1378 CG ASP A 180 10844 10955 8932 464 -2256 937 C ATOM 1379 OD1 ASP A 180 4.709 -25.865 18.258 1.00 80.38 O ANISOU 1379 OD1 ASP A 180 11035 10890 8615 441 -2139 883 O ATOM 1380 OD2 ASP A 180 2.915 -24.719 18.662 1.00 82.21 O1- ANISOU 1380 OD2 ASP A 180 10869 11179 9188 573 -2339 1095 O1- ATOM 1381 N ASP A 181 3.644 -28.648 22.434 1.00 61.30 N ANISOU 1381 N ASP A 181 8062 8177 7054 134 -2054 573 N ATOM 1382 CA ASP A 181 2.851 -29.305 23.447 1.00 62.26 C ANISOU 1382 CA ASP A 181 7938 8271 7446 18 -2042 542 C ATOM 1383 C ASP A 181 3.583 -29.494 24.745 1.00 60.76 C ANISOU 1383 C ASP A 181 7744 7971 7371 17 -1751 526 C ATOM 1384 O ASP A 181 3.045 -30.020 25.684 1.00 61.60 O ANISOU 1384 O ASP A 181 7677 8054 7673 -83 -1696 521 O ATOM 1385 CB ASP A 181 2.339 -30.649 22.946 1.00 64.07 C ANISOU 1385 CB ASP A 181 8195 8491 7659 -180 -2250 398 C ATOM 1386 CG ASP A 181 3.379 -31.415 22.188 1.00 63.94 C ANISOU 1386 CG ASP A 181 8514 8395 7388 -215 -2233 239 C ATOM 1387 OD1 ASP A 181 4.563 -31.171 22.419 1.00 62.28 O ANISOU 1387 OD1 ASP A 181 8463 8115 7087 -113 -2002 239 O ATOM 1388 OD2 ASP A 181 3.021 -32.261 21.358 1.00 65.59 O1- ANISOU 1388 OD2 ASP A 181 8819 8609 7493 -345 -2448 103 O1- ATOM 1389 N ILE A 182 4.824 -29.072 24.807 1.00 46.29 N ANISOU 1389 N ILE A 182 6100 6080 5409 116 -1568 529 N ATOM 1390 CA ILE A 182 5.523 -29.121 26.081 1.00 44.68 C ANISOU 1390 CA ILE A 182 5878 5794 5306 121 -1324 533 C ATOM 1391 C ILE A 182 5.984 -27.716 26.466 1.00 42.81 C ANISOU 1391 C ILE A 182 5625 5565 5074 270 -1169 630 C ATOM 1392 O ILE A 182 6.467 -26.950 25.623 1.00 41.86 O ANISOU 1392 O ILE A 182 5632 5459 4816 368 -1184 675 O ATOM 1393 CB ILE A 182 6.746 -30.045 26.004 1.00 43.49 C ANISOU 1393 CB ILE A 182 5942 5537 5043 86 -1235 430 C ATOM 1394 CG1 ILE A 182 6.319 -31.426 25.505 1.00 45.81 C ANISOU 1394 CG1 ILE A 182 6290 5779 5338 -58 -1394 309 C ATOM 1395 CG2 ILE A 182 7.428 -30.144 27.367 1.00 41.78 C ANISOU 1395 CG2 ILE A 182 5693 5251 4932 83 -1030 458 C ATOM 1396 CD1 ILE A 182 7.484 -32.294 25.038 1.00 45.53 C ANISOU 1396 CD1 ILE A 182 6495 5627 5177 -53 -1333 179 C ATOM 1397 N PRO A 183 5.817 -27.372 27.746 1.00 45.18 N ANISOU 1397 N PRO A 183 5783 5853 5530 275 -1014 660 N ATOM 1398 CA PRO A 183 6.370 -26.134 28.297 1.00 43.71 C ANISOU 1398 CA PRO A 183 5606 5639 5362 390 -846 710 C ATOM 1399 C PRO A 183 7.878 -26.244 28.503 1.00 40.84 C ANISOU 1399 C PRO A 183 5428 5207 4884 390 -712 674 C ATOM 1400 O PRO A 183 8.355 -27.273 28.981 1.00 39.97 O ANISOU 1400 O PRO A 183 5361 5064 4762 303 -677 620 O ATOM 1401 CB PRO A 183 5.645 -25.989 29.638 1.00 45.31 C ANISOU 1401 CB PRO A 183 5611 5865 5739 363 -725 711 C ATOM 1402 CG PRO A 183 5.129 -27.366 29.949 1.00 46.81 C ANISOU 1402 CG PRO A 183 5733 6076 5975 205 -781 676 C ATOM 1403 CD PRO A 183 4.849 -28.014 28.651 1.00 47.23 C ANISOU 1403 CD PRO A 183 5843 6139 5961 164 -1004 653 C ATOM 1404 N PHE A 184 8.593 -25.174 28.164 1.00 35.33 N ANISOU 1404 N PHE A 184 4818 4478 4127 485 -642 718 N ATOM 1405 CA PHE A 184 10.037 -25.122 28.318 1.00 32.64 C ANISOU 1405 CA PHE A 184 4608 4084 3707 484 -514 695 C ATOM 1406 C PHE A 184 10.415 -24.023 29.296 1.00 31.96 C ANISOU 1406 C PHE A 184 4482 3955 3707 517 -371 713 C ATOM 1407 O PHE A 184 9.762 -22.986 29.359 1.00 33.24 O ANISOU 1407 O PHE A 184 4578 4098 3953 588 -362 756 O ATOM 1408 CB PHE A 184 10.712 -24.874 26.968 1.00 31.64 C ANISOU 1408 CB PHE A 184 4640 3959 3423 532 -538 725 C ATOM 1409 CG PHE A 184 10.802 -26.093 26.125 1.00 32.21 C ANISOU 1409 CG PHE A 184 4811 4059 3370 486 -629 649 C ATOM 1410 CD1 PHE A 184 9.671 -26.620 25.530 1.00 34.51 C ANISOU 1410 CD1 PHE A 184 5074 4402 3638 451 -814 630 C ATOM 1411 CD2 PHE A 184 12.003 -26.727 25.935 1.00 31.17 C ANISOU 1411 CD2 PHE A 184 4788 3893 3162 476 -533 581 C ATOM 1412 CE1 PHE A 184 9.740 -27.767 24.752 1.00 35.62 C ANISOU 1412 CE1 PHE A 184 5329 4547 3660 393 -905 525 C ATOM 1413 CE2 PHE A 184 12.080 -27.868 25.169 1.00 32.63 C ANISOU 1413 CE2 PHE A 184 5078 4076 3244 445 -597 478 C ATOM 1414 CZ PHE A 184 10.942 -28.395 24.578 1.00 34.55 C ANISOU 1414 CZ PHE A 184 5326 4357 3445 396 -786 439 C ATOM 1415 N GLY A 185 11.508 -24.212 30.016 1.00 24.90 N ANISOU 1415 N GLY A 185 3630 3033 2797 472 -269 674 N ATOM 1416 CA GLY A 185 11.940 -23.183 30.925 1.00 24.72 C ANISOU 1416 CA GLY A 185 3590 2970 2834 477 -154 664 C ATOM 1417 C GLY A 185 13.436 -23.192 30.877 1.00 23.09 C ANISOU 1417 C GLY A 185 3462 2735 2577 448 -93 657 C ATOM 1418 O GLY A 185 14.030 -24.193 30.500 1.00 22.21 O ANISOU 1418 O GLY A 185 3387 2642 2408 428 -119 645 O ATOM 1419 N ILE A 186 14.045 -22.072 31.236 1.00 25.72 N ANISOU 1419 N ILE A 186 3809 3010 2953 446 -8 657 N ATOM 1420 CA ILE A 186 15.488 -21.964 31.213 1.00 25.12 C ANISOU 1420 CA ILE A 186 3766 2914 2863 403 50 656 C ATOM 1421 C ILE A 186 16.012 -21.203 32.436 1.00 26.34 C ANISOU 1421 C ILE A 186 3893 3035 3079 334 104 599 C ATOM 1422 O ILE A 186 15.384 -20.249 32.916 1.00 27.70 O ANISOU 1422 O ILE A 186 4066 3151 3309 346 140 564 O ATOM 1423 CB ILE A 186 15.962 -21.282 29.927 1.00 24.97 C ANISOU 1423 CB ILE A 186 3819 2851 2816 442 93 735 C ATOM 1424 CG1 ILE A 186 17.482 -21.191 29.914 1.00 25.22 C ANISOU 1424 CG1 ILE A 186 3844 2876 2863 384 178 737 C ATOM 1425 CG2 ILE A 186 15.359 -19.894 29.799 1.00 25.95 C ANISOU 1425 CG2 ILE A 186 3968 2880 3013 484 116 787 C ATOM 1426 CD1 ILE A 186 18.069 -21.028 28.543 1.00 25.64 C ANISOU 1426 CD1 ILE A 186 3966 2932 2843 410 249 815 C ATOM 1427 N THR A 187 17.171 -21.616 32.941 1.00 25.68 N ANISOU 1427 N THR A 187 3784 2984 2990 266 104 578 N ATOM 1428 CA THR A 187 17.727 -20.962 34.124 1.00 27.40 C ANISOU 1428 CA THR A 187 3982 3190 3238 175 118 511 C ATOM 1429 C THR A 187 19.239 -20.780 34.094 1.00 28.27 C ANISOU 1429 C THR A 187 4048 3296 3396 106 126 522 C ATOM 1430 O THR A 187 19.957 -21.639 33.585 1.00 27.71 O ANISOU 1430 O THR A 187 3930 3272 3326 129 112 570 O ATOM 1431 CB THR A 187 17.352 -21.741 35.422 1.00 27.79 C ANISOU 1431 CB THR A 187 4013 3329 3216 126 61 465 C ATOM 1432 CG2 THR A 187 18.242 -22.963 35.610 1.00 26.98 C ANISOU 1432 CG2 THR A 187 3868 3292 3090 102 -19 513 C ATOM 1433 OG1 THR A 187 17.502 -20.879 36.552 1.00 30.24 O ANISOU 1433 OG1 THR A 187 4344 3632 3512 43 82 370 O ATOM 1434 N SER A 188 19.700 -19.625 34.564 1.00 32.92 N ANISOU 1434 N SER A 188 4643 3817 4047 23 157 471 N ATOM 1435 CA SER A 188 21.116 -19.393 34.846 1.00 34.68 C ANISOU 1435 CA SER A 188 4788 4052 4338 -85 139 463 C ATOM 1436 C SER A 188 21.470 -19.415 36.350 1.00 36.86 C ANISOU 1436 C SER A 188 5041 4394 4571 -199 35 368 C ATOM 1437 O SER A 188 22.584 -19.067 36.750 1.00 38.86 O ANISOU 1437 O SER A 188 5218 4659 4887 -312 -15 343 O ATOM 1438 CB SER A 188 21.631 -18.127 34.154 1.00 35.40 C ANISOU 1438 CB SER A 188 4892 4014 4545 -137 235 489 C ATOM 1439 OG SER A 188 21.149 -16.963 34.811 1.00 36.69 O ANISOU 1439 OG SER A 188 5135 4057 4749 -193 250 394 O ATOM 1440 N ASN A 189 20.508 -19.764 37.194 1.00 36.11 N ANISOU 1440 N ASN A 189 5010 4350 4359 -182 3 314 N ATOM 1441 CA ASN A 189 20.716 -19.728 38.651 1.00 38.45 C ANISOU 1441 CA ASN A 189 5329 4728 4553 -297 -85 221 C ATOM 1442 C ASN A 189 21.355 -21.009 39.178 1.00 38.16 C ANISOU 1442 C ASN A 189 5221 4829 4449 -315 -225 306 C ATOM 1443 O ASN A 189 20.789 -22.085 39.038 1.00 35.86 O ANISOU 1443 O ASN A 189 4935 4580 4109 -233 -236 387 O ATOM 1444 CB ASN A 189 19.392 -19.453 39.362 1.00 39.10 C ANISOU 1444 CB ASN A 189 5517 4813 4526 -278 -18 124 C ATOM 1445 CG ASN A 189 19.553 -19.308 40.863 1.00 41.20 C ANISOU 1445 CG ASN A 189 5847 5175 4632 -407 -82 7 C ATOM 1446 ND2 ASN A 189 18.825 -18.363 41.446 1.00 42.58 N ANISOU 1446 ND2 ASN A 189 6122 5295 4762 -428 20 -155 N ATOM 1447 OD1 ASN A 189 20.306 -20.048 41.493 1.00 41.11 O ANISOU 1447 OD1 ASN A 189 5803 5288 4531 -480 -224 62 O ATOM 1448 N SER A 190 22.533 -20.891 39.783 1.00 42.90 N ANISOU 1448 N SER A 190 5749 5486 5065 -424 -347 295 N ATOM 1449 CA SER A 190 23.291 -22.063 40.227 1.00 42.99 C ANISOU 1449 CA SER A 190 5665 5613 5056 -421 -506 405 C ATOM 1450 C SER A 190 22.579 -22.862 41.346 1.00 41.55 C ANISOU 1450 C SER A 190 5585 5536 4667 -438 -588 436 C ATOM 1451 O SER A 190 22.751 -24.094 41.453 1.00 40.22 O ANISOU 1451 O SER A 190 5375 5414 4491 -379 -681 573 O ATOM 1452 CB SER A 190 24.697 -21.651 40.651 1.00 46.18 C ANISOU 1452 CB SER A 190 5938 6065 5541 -542 -643 391 C ATOM 1453 OG SER A 190 24.646 -20.660 41.673 1.00 47.52 O ANISOU 1453 OG SER A 190 6205 6258 5594 -702 -698 243 O ATOM 1454 N ASP A 191 21.791 -22.168 42.173 1.00 48.52 N ANISOU 1454 N ASP A 191 6604 6444 5386 -517 -537 311 N ATOM 1455 CA ASP A 191 20.889 -22.827 43.127 1.00 47.28 C ANISOU 1455 CA ASP A 191 6560 6391 5015 -536 -542 338 C ATOM 1456 C ASP A 191 19.946 -23.792 42.405 1.00 44.55 C ANISOU 1456 C ASP A 191 6204 5999 4722 -410 -452 450 C ATOM 1457 O ASP A 191 19.609 -24.867 42.923 1.00 43.51 O ANISOU 1457 O ASP A 191 6104 5935 4492 -414 -507 569 O ATOM 1458 CB ASP A 191 20.026 -21.813 43.892 1.00 48.62 C ANISOU 1458 CB ASP A 191 6868 6575 5029 -609 -420 151 C ATOM 1459 CG ASP A 191 20.840 -20.888 44.803 1.00 51.23 C ANISOU 1459 CG ASP A 191 7253 6953 5257 -768 -521 0 C ATOM 1460 OD1 ASP A 191 21.985 -21.235 45.190 1.00 51.89 O ANISOU 1460 OD1 ASP A 191 7271 7123 5323 -848 -731 72 O ATOM 1461 OD2 ASP A 191 20.314 -19.803 45.161 1.00 52.51 O1- ANISOU 1461 OD2 ASP A 191 7524 7062 5365 -813 -398 -202 O1- ATOM 1462 N VAL A 192 19.498 -23.406 41.215 1.00 30.38 N ANISOU 1462 N VAL A 192 4375 4086 3079 -313 -326 419 N ATOM 1463 CA VAL A 192 18.556 -24.249 40.495 1.00 27.92 C ANISOU 1463 CA VAL A 192 4058 3736 2814 -214 -263 498 C ATOM 1464 C VAL A 192 19.297 -25.422 39.854 1.00 26.40 C ANISOU 1464 C VAL A 192 3794 3514 2725 -147 -359 628 C ATOM 1465 O VAL A 192 18.742 -26.514 39.714 1.00 24.97 O ANISOU 1465 O VAL A 192 3626 3317 2546 -109 -373 714 O ATOM 1466 CB VAL A 192 17.703 -23.433 39.483 1.00 27.65 C ANISOU 1466 CB VAL A 192 4024 3604 2878 -133 -124 427 C ATOM 1467 CG1 VAL A 192 16.633 -24.302 38.871 1.00 25.79 C ANISOU 1467 CG1 VAL A 192 3776 3355 2670 -61 -92 495 C ATOM 1468 CG2 VAL A 192 17.049 -22.228 40.188 1.00 29.97 C ANISOU 1468 CG2 VAL A 192 4379 3896 3110 -176 -20 284 C ATOM 1469 N PHE A 193 20.559 -25.204 39.498 1.00 26.48 N ANISOU 1469 N PHE A 193 3719 3506 2837 -137 -415 635 N ATOM 1470 CA PHE A 193 21.434 -26.294 39.066 1.00 26.27 C ANISOU 1470 CA PHE A 193 3603 3456 2924 -61 -498 741 C ATOM 1471 C PHE A 193 21.519 -27.340 40.165 1.00 26.19 C ANISOU 1471 C PHE A 193 3614 3505 2831 -94 -645 859 C ATOM 1472 O PHE A 193 21.314 -28.524 39.910 1.00 24.98 O ANISOU 1472 O PHE A 193 3468 3290 2734 -22 -673 955 O ATOM 1473 CB PHE A 193 22.860 -25.796 38.738 1.00 28.61 C ANISOU 1473 CB PHE A 193 3763 3755 3353 -63 -528 731 C ATOM 1474 CG PHE A 193 23.008 -25.201 37.364 1.00 28.70 C ANISOU 1474 CG PHE A 193 3740 3689 3475 -2 -376 681 C ATOM 1475 CD1 PHE A 193 23.945 -25.709 36.477 1.00 29.60 C ANISOU 1475 CD1 PHE A 193 3736 3776 3736 88 -340 722 C ATOM 1476 CD2 PHE A 193 22.217 -24.129 36.957 1.00 28.09 C ANISOU 1476 CD2 PHE A 193 3751 3566 3355 -27 -259 603 C ATOM 1477 CE1 PHE A 193 24.096 -25.164 35.218 1.00 29.83 C ANISOU 1477 CE1 PHE A 193 3755 3755 3823 131 -182 690 C ATOM 1478 CE2 PHE A 193 22.353 -23.588 35.694 1.00 27.73 C ANISOU 1478 CE2 PHE A 193 3697 3455 3386 23 -131 596 C ATOM 1479 CZ PHE A 193 23.293 -24.105 34.822 1.00 28.75 C ANISOU 1479 CZ PHE A 193 3727 3578 3617 91 -88 641 C ATOM 1480 N SER A 194 21.840 -26.891 41.377 1.00 27.19 N ANISOU 1480 N SER A 194 3766 3743 2821 -211 -745 853 N ATOM 1481 CA SER A 194 21.970 -27.790 42.532 1.00 27.38 C ANISOU 1481 CA SER A 194 3833 3849 2720 -261 -907 994 C ATOM 1482 C SER A 194 20.689 -28.540 42.826 1.00 25.74 C ANISOU 1482 C SER A 194 3748 3630 2401 -273 -838 1062 C ATOM 1483 O SER A 194 20.708 -29.746 43.097 1.00 25.32 O ANISOU 1483 O SER A 194 3711 3544 2364 -247 -931 1230 O ATOM 1484 CB SER A 194 22.377 -27.021 43.786 1.00 29.33 C ANISOU 1484 CB SER A 194 4127 4245 2770 -410 -1019 944 C ATOM 1485 OG SER A 194 23.651 -26.419 43.615 1.00 31.40 O ANISOU 1485 OG SER A 194 4249 4523 3159 -429 -1120 900 O ATOM 1486 N LYS A 195 19.575 -27.817 42.772 1.00 29.36 N ANISOU 1486 N LYS A 195 4277 4104 2773 -312 -671 939 N ATOM 1487 CA LYS A 195 18.282 -28.416 43.053 1.00 28.53 C ANISOU 1487 CA LYS A 195 4251 4007 2583 -343 -580 992 C ATOM 1488 C LYS A 195 18.151 -29.714 42.251 1.00 27.30 C ANISOU 1488 C LYS A 195 4059 3715 2596 -257 -612 1116 C ATOM 1489 O LYS A 195 17.540 -30.686 42.724 1.00 27.70 O ANISOU 1489 O LYS A 195 4168 3756 2602 -305 -626 1247 O ATOM 1490 CB LYS A 195 17.177 -27.446 42.649 1.00 28.57 C ANISOU 1490 CB LYS A 195 4263 4006 2585 -337 -388 833 C ATOM 1491 CG LYS A 195 15.772 -27.869 42.996 1.00 28.58 C ANISOU 1491 CG LYS A 195 4301 4043 2515 -382 -267 864 C ATOM 1492 CD LYS A 195 14.807 -26.724 42.673 1.00 29.61 C ANISOU 1492 CD LYS A 195 4404 4175 2671 -352 -90 696 C ATOM 1493 CE LYS A 195 13.679 -26.589 43.705 1.00 31.05 C ANISOU 1493 CE LYS A 195 4628 4478 2692 -437 64 665 C ATOM 1494 NZ LYS A 195 12.926 -27.845 43.829 1.00 30.63 N1+ ANISOU 1494 NZ LYS A 195 4556 4436 2644 -489 75 826 N1+ ATOM 1495 N TYR A 196 18.726 -29.735 41.057 1.00 31.24 N ANISOU 1495 N TYR A 196 4478 4106 3286 -141 -613 1069 N ATOM 1496 CA TYR A 196 18.589 -30.864 40.151 1.00 30.47 C ANISOU 1496 CA TYR A 196 4367 3863 3348 -53 -623 1125 C ATOM 1497 C TYR A 196 19.873 -31.611 39.835 1.00 31.12 C ANISOU 1497 C TYR A 196 4380 3858 3587 52 -734 1198 C ATOM 1498 O TYR A 196 19.953 -32.319 38.872 1.00 30.73 O ANISOU 1498 O TYR A 196 4317 3675 3686 151 -712 1181 O ATOM 1499 CB TYR A 196 17.840 -30.457 38.892 1.00 29.16 C ANISOU 1499 CB TYR A 196 4191 3637 3251 0 -499 998 C ATOM 1500 CG TYR A 196 16.461 -29.983 39.197 1.00 29.20 C ANISOU 1500 CG TYR A 196 4228 3707 3160 -78 -403 955 C ATOM 1501 CD1 TYR A 196 15.473 -30.864 39.546 1.00 29.29 C ANISOU 1501 CD1 TYR A 196 4269 3700 3158 -147 -396 1035 C ATOM 1502 CD2 TYR A 196 16.154 -28.667 39.168 1.00 29.61 C ANISOU 1502 CD2 TYR A 196 4267 3825 3159 -84 -310 841 C ATOM 1503 CE1 TYR A 196 14.214 -30.437 39.846 1.00 29.53 C ANISOU 1503 CE1 TYR A 196 4288 3806 3127 -215 -289 998 C ATOM 1504 CE2 TYR A 196 14.898 -28.235 39.456 1.00 30.29 C ANISOU 1504 CE2 TYR A 196 4354 3963 3191 -129 -209 797 C ATOM 1505 CZ TYR A 196 13.929 -29.128 39.797 1.00 30.53 C ANISOU 1505 CZ TYR A 196 4386 4004 3211 -193 -193 874 C ATOM 1506 OH TYR A 196 12.678 -28.691 40.095 1.00 31.61 O ANISOU 1506 OH TYR A 196 4483 4208 3320 -233 -72 830 O ATOM 1507 N GLN A 197 20.863 -31.454 40.692 1.00 30.71 N ANISOU 1507 N GLN A 197 4281 3888 3499 30 -859 1272 N ATOM 1508 CA GLN A 197 22.061 -32.269 40.688 1.00 32.15 C ANISOU 1508 CA GLN A 197 4368 4003 3843 132 -996 1384 C ATOM 1509 C GLN A 197 22.920 -32.169 39.452 1.00 32.40 C ANISOU 1509 C GLN A 197 4271 3956 4085 272 -925 1287 C ATOM 1510 O GLN A 197 23.609 -33.089 39.130 1.00 33.45 O ANISOU 1510 O GLN A 197 4333 3977 4400 398 -976 1351 O ATOM 1511 CB GLN A 197 21.699 -33.724 40.928 1.00 32.56 C ANISOU 1511 CB GLN A 197 4483 3929 3961 168 -1010 1466 C ATOM 1512 CG GLN A 197 21.195 -34.026 42.319 1.00 33.61 C ANISOU 1512 CG GLN A 197 4707 4151 3912 46 -1053 1556 C ATOM 1513 CD GLN A 197 19.714 -33.819 42.461 1.00 32.74 C ANISOU 1513 CD GLN A 197 4704 4076 3661 -69 -923 1518 C ATOM 1514 NE2 GLN A 197 19.281 -33.482 43.645 1.00 33.62 N ANISOU 1514 NE2 GLN A 197 4884 4331 3560 -193 -917 1551 N ATOM 1515 OE1 GLN A 197 18.979 -33.970 41.523 1.00 31.46 O ANISOU 1515 OE1 GLN A 197 4557 3818 3580 -48 -834 1461 O ATOM 1516 N LEU A 198 22.884 -31.036 38.775 1.00 43.95 N ANISOU 1516 N LEU A 198 5707 5472 5522 252 -795 1138 N ATOM 1517 CA LEU A 198 23.647 -30.826 37.559 1.00 45.01 C ANISOU 1517 CA LEU A 198 5733 5555 5813 362 -687 1051 C ATOM 1518 C LEU A 198 25.123 -30.576 37.828 1.00 47.55 C ANISOU 1518 C LEU A 198 5860 5939 6267 390 -767 1091 C ATOM 1519 O LEU A 198 25.491 -29.856 38.732 1.00 48.61 O ANISOU 1519 O LEU A 198 5951 6192 6327 277 -872 1112 O ATOM 1520 CB LEU A 198 23.094 -29.635 36.792 1.00 44.38 C ANISOU 1520 CB LEU A 198 5702 5509 5650 315 -530 918 C ATOM 1521 CG LEU A 198 22.004 -29.725 35.733 1.00 42.84 C ANISOU 1521 CG LEU A 198 5623 5245 5410 349 -407 840 C ATOM 1522 CD1 LEU A 198 22.335 -30.713 34.641 1.00 43.36 C ANISOU 1522 CD1 LEU A 198 5684 5200 5592 483 -351 809 C ATOM 1523 CD2 LEU A 198 20.633 -29.964 36.318 1.00 40.85 C ANISOU 1523 CD2 LEU A 198 5488 4996 5039 272 -440 861 C ATOM 1524 N ASP A 199 25.971 -31.161 37.011 1.00 37.76 N ANISOU 1524 N ASP A 199 4494 4623 5231 537 -711 1086 N ATOM 1525 CA ASP A 199 27.383 -30.908 37.121 1.00 40.51 C ANISOU 1525 CA ASP A 199 4605 5035 5750 573 -761 1119 C ATOM 1526 C ASP A 199 27.825 -29.811 36.153 1.00 42.17 C ANISOU 1526 C ASP A 199 4730 5296 5998 545 -567 1001 C ATOM 1527 O ASP A 199 28.924 -29.321 36.240 1.00 44.59 O ANISOU 1527 O ASP A 199 4827 5678 6439 522 -585 1015 O ATOM 1528 CB ASP A 199 28.170 -32.199 36.902 1.00 41.52 C ANISOU 1528 CB ASP A 199 4603 5053 6121 768 -803 1195 C ATOM 1529 CG ASP A 199 29.545 -32.145 37.488 1.00 43.86 C ANISOU 1529 CG ASP A 199 4625 5434 6606 800 -952 1292 C ATOM 1530 OD1 ASP A 199 30.418 -32.887 37.038 1.00 45.40 O ANISOU 1530 OD1 ASP A 199 4638 5553 7059 982 -922 1318 O ATOM 1531 OD2 ASP A 199 29.755 -31.352 38.398 1.00 44.42 O1- ANISOU 1531 OD2 ASP A 199 4654 5648 6574 643 -1102 1332 O1- ATOM 1532 N LYS A 200 26.955 -29.399 35.247 1.00 42.59 N ANISOU 1532 N LYS A 200 4940 5309 5932 532 -393 902 N ATOM 1533 CA LYS A 200 27.342 -28.379 34.262 1.00 44.50 C ANISOU 1533 CA LYS A 200 5130 5585 6193 503 -200 826 C ATOM 1534 C LYS A 200 26.154 -28.039 33.384 1.00 42.27 C ANISOU 1534 C LYS A 200 5063 5258 5740 494 -66 752 C ATOM 1535 O LYS A 200 25.075 -28.562 33.603 1.00 39.45 O ANISOU 1535 O LYS A 200 4860 4855 5275 499 -130 749 O ATOM 1536 CB LYS A 200 28.512 -28.853 33.402 1.00 47.13 C ANISOU 1536 CB LYS A 200 5271 5907 6731 639 -66 815 C ATOM 1537 CG LYS A 200 28.188 -30.062 32.561 1.00 46.19 C ANISOU 1537 CG LYS A 200 5247 5674 6631 812 30 762 C ATOM 1538 CD LYS A 200 29.434 -30.916 32.399 1.00 48.47 C ANISOU 1538 CD LYS A 200 5303 5930 7182 978 64 779 C ATOM 1539 CE LYS A 200 29.101 -32.221 31.711 1.00 47.72 C ANISOU 1539 CE LYS A 200 5326 5681 7125 1155 139 703 C ATOM 1540 NZ LYS A 200 28.483 -31.913 30.409 1.00 47.89 N1+ ANISOU 1540 NZ LYS A 200 5534 5700 6962 1148 357 568 N1+ ATOM 1541 N ASP A 201 26.337 -27.148 32.414 1.00 43.65 N ANISOU 1541 N ASP A 201 5240 5450 5893 470 108 711 N ATOM 1542 CA ASP A 201 25.247 -26.813 31.507 1.00 41.16 C ANISOU 1542 CA ASP A 201 5123 5102 5414 473 207 666 C ATOM 1543 C ASP A 201 24.603 -28.097 30.971 1.00 39.62 C ANISOU 1543 C ASP A 201 5042 4839 5171 590 202 620 C ATOM 1544 O ASP A 201 25.298 -28.990 30.513 1.00 41.58 O ANISOU 1544 O ASP A 201 5226 5054 5520 704 263 590 O ATOM 1545 CB ASP A 201 25.774 -26.004 30.317 1.00 42.97 C ANISOU 1545 CB ASP A 201 5337 5355 5635 467 413 658 C ATOM 1546 CG ASP A 201 26.047 -24.533 30.653 1.00 43.00 C ANISOU 1546 CG ASP A 201 5296 5378 5665 320 431 699 C ATOM 1547 OD1 ASP A 201 26.107 -24.150 31.851 1.00 43.12 O ANISOU 1547 OD1 ASP A 201 5255 5402 5725 225 286 705 O ATOM 1548 OD2 ASP A 201 26.225 -23.761 29.680 1.00 43.17 O1- ANISOU 1548 OD2 ASP A 201 5351 5397 5652 294 596 723 O1- ATOM 1549 N GLY A 202 23.273 -28.193 31.026 1.00 34.99 N ANISOU 1549 N GLY A 202 4616 4224 4453 560 132 605 N ATOM 1550 CA GLY A 202 22.585 -29.378 30.549 1.00 33.81 C ANISOU 1550 CA GLY A 202 4578 3998 4269 632 104 553 C ATOM 1551 C GLY A 202 21.075 -29.245 30.524 1.00 31.34 C ANISOU 1551 C GLY A 202 4404 3679 3824 570 33 542 C ATOM 1552 O GLY A 202 20.533 -28.147 30.729 1.00 30.17 O ANISOU 1552 O GLY A 202 4272 3583 3607 499 32 570 O ATOM 1553 N VAL A 203 20.401 -30.376 30.285 1.00 22.45 N ANISOU 1553 N VAL A 203 3364 2475 2692 598 -28 498 N ATOM 1554 CA VAL A 203 18.964 -30.397 30.044 1.00 21.14 C ANISOU 1554 CA VAL A 203 3301 2307 2425 540 -97 477 C ATOM 1555 C VAL A 203 18.262 -31.542 30.737 1.00 20.80 C ANISOU 1555 C VAL A 203 3279 2180 2444 498 -213 494 C ATOM 1556 O VAL A 203 18.815 -32.638 30.868 1.00 21.80 O ANISOU 1556 O VAL A 203 3407 2200 2678 549 -235 486 O ATOM 1557 CB VAL A 203 18.656 -30.511 28.544 1.00 22.40 C ANISOU 1557 CB VAL A 203 3579 2463 2468 584 -47 381 C ATOM 1558 CG1 VAL A 203 17.140 -30.662 28.320 1.00 21.67 C ANISOU 1558 CG1 VAL A 203 3561 2373 2299 517 -165 363 C ATOM 1559 CG2 VAL A 203 19.252 -29.297 27.788 1.00 22.81 C ANISOU 1559 CG2 VAL A 203 3632 2603 2431 608 83 400 C ATOM 1560 N VAL A 204 17.033 -31.293 31.185 1.00 26.04 N ANISOU 1560 N VAL A 204 3951 2880 3061 407 -279 527 N ATOM 1561 CA VAL A 204 16.312 -32.331 31.898 1.00 26.06 C ANISOU 1561 CA VAL A 204 3965 2811 3126 335 -370 568 C ATOM 1562 C VAL A 204 14.839 -32.329 31.560 1.00 26.52 C ANISOU 1562 C VAL A 204 4042 2891 3143 254 -424 541 C ATOM 1563 O VAL A 204 14.218 -31.268 31.425 1.00 26.38 O ANISOU 1563 O VAL A 204 3987 2976 3059 242 -403 544 O ATOM 1564 CB VAL A 204 16.498 -32.204 33.444 1.00 25.39 C ANISOU 1564 CB VAL A 204 3814 2770 3062 273 -394 690 C ATOM 1565 CG1 VAL A 204 15.827 -33.355 34.164 1.00 25.71 C ANISOU 1565 CG1 VAL A 204 3880 2729 3159 188 -470 767 C ATOM 1566 CG2 VAL A 204 17.972 -32.154 33.810 1.00 25.61 C ANISOU 1566 CG2 VAL A 204 3789 2796 3143 344 -383 727 C ATOM 1567 N LEU A 205 14.284 -33.532 31.445 1.00 19.19 N ANISOU 1567 N LEU A 205 3159 1851 2282 199 -500 520 N ATOM 1568 CA LEU A 205 12.872 -33.710 31.148 1.00 19.73 C ANISOU 1568 CA LEU A 205 3214 1934 2348 98 -575 496 C ATOM 1569 C LEU A 205 12.186 -34.348 32.335 1.00 20.23 C ANISOU 1569 C LEU A 205 3221 1966 2501 -30 -603 605 C ATOM 1570 O LEU A 205 12.601 -35.411 32.824 1.00 21.09 O ANISOU 1570 O LEU A 205 3378 1938 2699 -55 -628 657 O ATOM 1571 CB LEU A 205 12.689 -34.600 29.903 1.00 22.00 C ANISOU 1571 CB LEU A 205 3611 2112 2635 98 -651 359 C ATOM 1572 CG LEU A 205 11.267 -35.085 29.573 1.00 24.59 C ANISOU 1572 CG LEU A 205 3918 2428 2997 -38 -776 323 C ATOM 1573 CD1 LEU A 205 11.098 -35.458 28.073 1.00 27.58 C ANISOU 1573 CD1 LEU A 205 4422 2769 3286 -28 -865 150 C ATOM 1574 CD2 LEU A 205 10.850 -36.225 30.472 1.00 24.69 C ANISOU 1574 CD2 LEU A 205 3910 2305 3168 -167 -816 394 C ATOM 1575 N PHE A 206 11.115 -33.700 32.774 1.00 29.05 N ANISOU 1575 N PHE A 206 4233 3205 3600 -105 -587 648 N ATOM 1576 CA PHE A 206 10.315 -34.139 33.906 1.00 29.76 C ANISOU 1576 CA PHE A 206 4250 3311 3749 -243 -570 757 C ATOM 1577 C PHE A 206 8.996 -34.645 33.393 1.00 32.56 C ANISOU 1577 C PHE A 206 4535 3648 4190 -360 -648 725 C ATOM 1578 O PHE A 206 8.477 -34.134 32.390 1.00 34.29 O ANISOU 1578 O PHE A 206 4716 3924 4387 -324 -709 635 O ATOM 1579 CB PHE A 206 10.046 -32.965 34.843 1.00 29.33 C ANISOU 1579 CB PHE A 206 4102 3423 3619 -239 -458 808 C ATOM 1580 CG PHE A 206 11.285 -32.294 35.324 1.00 27.42 C ANISOU 1580 CG PHE A 206 3913 3215 3288 -148 -403 819 C ATOM 1581 CD1 PHE A 206 11.811 -31.208 34.633 1.00 26.63 C ANISOU 1581 CD1 PHE A 206 3820 3158 3140 -32 -377 740 C ATOM 1582 CD2 PHE A 206 11.935 -32.754 36.469 1.00 26.56 C ANISOU 1582 CD2 PHE A 206 3847 3096 3147 -190 -392 923 C ATOM 1583 CE1 PHE A 206 12.961 -30.573 35.083 1.00 25.33 C ANISOU 1583 CE1 PHE A 206 3684 3021 2919 24 -333 747 C ATOM 1584 CE2 PHE A 206 13.087 -32.132 36.921 1.00 25.47 C ANISOU 1584 CE2 PHE A 206 3739 3004 2936 -123 -375 929 C ATOM 1585 CZ PHE A 206 13.606 -31.040 36.229 1.00 24.90 C ANISOU 1585 CZ PHE A 206 3653 2969 2840 -23 -342 832 C ATOM 1586 N LYS A 207 8.442 -35.634 34.082 1.00 36.49 N ANISOU 1586 N LYS A 207 5009 4069 4786 -512 -658 814 N ATOM 1587 CA LYS A 207 7.195 -36.212 33.646 1.00 39.17 C ANISOU 1587 CA LYS A 207 5259 4381 5242 -659 -742 787 C ATOM 1588 C LYS A 207 6.461 -36.836 34.803 1.00 39.49 C ANISOU 1588 C LYS A 207 5215 4416 5373 -843 -674 939 C ATOM 1589 O LYS A 207 7.078 -37.334 35.739 1.00 38.03 O ANISOU 1589 O LYS A 207 5119 4162 5169 -868 -616 1064 O ATOM 1590 CB LYS A 207 7.438 -37.255 32.561 1.00 40.10 C ANISOU 1590 CB LYS A 207 5512 4301 5424 -678 -886 668 C ATOM 1591 CG LYS A 207 8.332 -38.395 32.975 1.00 38.77 C ANISOU 1591 CG LYS A 207 5496 3908 5328 -683 -884 718 C ATOM 1592 CD LYS A 207 8.549 -39.324 31.797 1.00 40.07 C ANISOU 1592 CD LYS A 207 5803 3865 5555 -678 -1005 547 C ATOM 1593 CE LYS A 207 9.589 -40.372 32.092 1.00 39.09 C ANISOU 1593 CE LYS A 207 5831 3489 5531 -622 -994 578 C ATOM 1594 NZ LYS A 207 10.143 -40.938 30.833 1.00 40.25 N1+ ANISOU 1594 NZ LYS A 207 6137 3468 5689 -530 -1053 355 N1+ ATOM 1595 N LYS A 208 5.142 -36.892 34.665 1.00 48.13 N ANISOU 1595 N LYS A 208 6134 5578 6575 -980 -697 937 N ATOM 1596 CA LYS A 208 4.249 -37.261 35.739 1.00 48.65 C ANISOU 1596 CA LYS A 208 6065 5695 6724 -1166 -587 1084 C ATOM 1597 C LYS A 208 4.037 -38.771 35.868 1.00 48.87 C ANISOU 1597 C LYS A 208 6161 5501 6907 -1371 -658 1165 C ATOM 1598 O LYS A 208 3.096 -39.211 36.516 1.00 49.89 O ANISOU 1598 O LYS A 208 6155 5656 7145 -1572 -586 1284 O ATOM 1599 CB LYS A 208 2.936 -36.455 35.694 1.00 50.69 C ANISOU 1599 CB LYS A 208 6049 6159 7053 -1203 -533 1062 C ATOM 1600 CG LYS A 208 2.991 -35.235 36.627 1.00 50.43 C ANISOU 1600 CG LYS A 208 5944 6325 6892 -1090 -324 1097 C ATOM 1601 CD LYS A 208 1.858 -34.225 36.410 1.00 52.66 C ANISOU 1601 CD LYS A 208 5956 6791 7263 -1041 -271 1042 C ATOM 1602 CE LYS A 208 1.814 -33.216 37.571 1.00 52.57 C ANISOU 1602 CE LYS A 208 5884 6943 7146 -965 -15 1069 C ATOM 1603 NZ LYS A 208 3.163 -32.660 37.943 1.00 50.80 N1+ ANISOU 1603 NZ LYS A 208 5897 6695 6710 -825 26 1043 N1+ ATOM 1604 N PHE A 209 4.863 -39.551 35.178 1.00 56.05 N ANISOU 1604 N PHE A 209 7269 6183 7846 -1321 -790 1089 N ATOM 1605 CA PHE A 209 4.794 -41.008 35.250 1.00 57.27 C ANISOU 1605 CA PHE A 209 7526 6062 8173 -1493 -866 1150 C ATOM 1606 C PHE A 209 6.169 -41.664 35.142 1.00 56.71 C ANISOU 1606 C PHE A 209 7700 5754 8092 -1354 -912 1141 C ATOM 1607 O PHE A 209 7.138 -41.015 34.746 1.00 55.02 O ANISOU 1607 O PHE A 209 7560 5599 7746 -1133 -907 1046 O ATOM 1608 CB PHE A 209 3.894 -41.526 34.136 1.00 59.03 C ANISOU 1608 CB PHE A 209 7686 6195 8549 -1633 -1034 991 C ATOM 1609 CG PHE A 209 4.150 -40.857 32.812 1.00 59.09 C ANISOU 1609 CG PHE A 209 7730 6279 8444 -1464 -1153 760 C ATOM 1610 CD1 PHE A 209 5.197 -41.269 31.998 1.00 58.68 C ANISOU 1610 CD1 PHE A 209 7910 6047 8339 -1327 -1229 611 C ATOM 1611 CD2 PHE A 209 3.367 -39.789 32.403 1.00 60.27 C ANISOU 1611 CD2 PHE A 209 7682 6683 8536 -1431 -1174 708 C ATOM 1612 CE1 PHE A 209 5.447 -40.636 30.781 1.00 59.51 C ANISOU 1612 CE1 PHE A 209 8067 6243 8299 -1183 -1313 415 C ATOM 1613 CE2 PHE A 209 3.609 -39.149 31.199 1.00 61.17 C ANISOU 1613 CE2 PHE A 209 7849 6872 8520 -1280 -1290 536 C ATOM 1614 CZ PHE A 209 4.649 -39.574 30.381 1.00 60.82 C ANISOU 1614 CZ PHE A 209 8056 6666 8385 -1167 -1354 391 C ATOM 1615 N ASP A 210 6.226 -42.952 35.494 1.00 58.92 N ANISOU 1615 N ASP A 210 8089 5758 8539 -1485 -952 1251 N ATOM 1616 CA ASP A 210 7.431 -43.791 35.371 1.00 59.35 C ANISOU 1616 CA ASP A 210 8361 5527 8664 -1356 -1010 1249 C ATOM 1617 C ASP A 210 8.679 -43.254 36.108 1.00 57.50 C ANISOU 1617 C ASP A 210 8183 5385 8279 -1144 -936 1369 C ATOM 1618 O ASP A 210 8.585 -42.832 37.257 1.00 57.10 O ANISOU 1618 O ASP A 210 8074 5507 8114 -1192 -842 1572 O ATOM 1619 CB ASP A 210 7.735 -44.089 33.897 1.00 59.82 C ANISOU 1619 CB ASP A 210 8526 5428 8773 -1259 -1128 955 C ATOM 1620 CG ASP A 210 6.513 -44.632 33.135 1.00 62.31 C ANISOU 1620 CG ASP A 210 8793 5657 9224 -1489 -1246 816 C ATOM 1621 OD1 ASP A 210 6.399 -44.351 31.917 1.00 62.24 O ANISOU 1621 OD1 ASP A 210 8807 5695 9148 -1436 -1340 563 O ATOM 1622 OD2 ASP A 210 5.667 -45.336 33.744 1.00 64.68 O1- ANISOU 1622 OD2 ASP A 210 9031 5852 9691 -1736 -1252 964 O1- ATOM 1623 N GLU A 211 9.832 -43.258 35.440 1.00 61.18 N ANISOU 1623 N GLU A 211 8754 5752 8739 -920 -976 1234 N ATOM 1624 CA GLU A 211 11.091 -42.851 36.072 1.00 59.91 C ANISOU 1624 CA GLU A 211 8623 5657 8482 -727 -937 1343 C ATOM 1625 C GLU A 211 11.000 -41.455 36.691 1.00 57.67 C ANISOU 1625 C GLU A 211 8216 5730 7965 -706 -842 1392 C ATOM 1626 O GLU A 211 11.855 -41.057 37.486 1.00 57.08 O ANISOU 1626 O GLU A 211 8149 5751 7788 -611 -819 1513 O ATOM 1627 CB GLU A 211 12.249 -42.885 35.075 1.00 59.45 C ANISOU 1627 CB GLU A 211 8641 5489 8460 -490 -963 1148 C ATOM 1628 CG GLU A 211 12.331 -44.155 34.243 1.00 62.00 C ANISOU 1628 CG GLU A 211 9101 5455 9002 -483 -1035 1011 C ATOM 1629 CD GLU A 211 11.607 -44.025 32.906 1.00 62.16 C ANISOU 1629 CD GLU A 211 9139 5495 8986 -540 -1066 725 C ATOM 1630 OE1 GLU A 211 12.137 -43.343 32.001 1.00 60.84 O ANISOU 1630 OE1 GLU A 211 8979 5450 8687 -382 -1028 534 O ATOM 1631 OE2 GLU A 211 10.507 -44.604 32.764 1.00 63.94 O1- ANISOU 1631 OE2 GLU A 211 9368 5619 9306 -757 -1135 703 O1- ATOM 1632 N GLY A 212 9.995 -40.695 36.279 1.00 32.67 N ANISOU 1632 N GLY A 212 4935 2750 4727 -784 -800 1281 N ATOM 1633 CA GLY A 212 9.745 -39.386 36.834 1.00 30.78 C ANISOU 1633 CA GLY A 212 4580 2810 4304 -768 -696 1304 C ATOM 1634 C GLY A 212 10.662 -38.356 36.203 1.00 28.84 C ANISOU 1634 C GLY A 212 4337 2672 3947 -560 -684 1160 C ATOM 1635 O GLY A 212 10.404 -37.157 36.262 1.00 27.80 O ANISOU 1635 O GLY A 212 4118 2752 3694 -526 -612 1112 O ATOM 1636 N ARG A 213 11.762 -38.818 35.629 1.00 36.85 N ANISOU 1636 N ARG A 213 5450 3529 5021 -420 -740 1097 N ATOM 1637 CA ARG A 213 12.706 -37.883 35.063 1.00 35.41 C ANISOU 1637 CA ARG A 213 5260 3448 4745 -241 -706 983 C ATOM 1638 C ARG A 213 13.733 -38.508 34.102 1.00 35.88 C ANISOU 1638 C ARG A 213 5409 3325 4898 -90 -739 863 C ATOM 1639 O ARG A 213 14.085 -39.674 34.222 1.00 37.17 O ANISOU 1639 O ARG A 213 5649 3263 5213 -79 -791 908 O ATOM 1640 CB ARG A 213 13.363 -37.141 36.218 1.00 34.37 C ANISOU 1640 CB ARG A 213 5087 3471 4500 -209 -659 1113 C ATOM 1641 CG ARG A 213 14.804 -36.837 36.074 1.00 33.88 C ANISOU 1641 CG ARG A 213 5032 3407 4434 -43 -664 1089 C ATOM 1642 CD ARG A 213 15.351 -36.098 37.309 1.00 33.36 C ANISOU 1642 CD ARG A 213 4924 3507 4245 -54 -653 1212 C ATOM 1643 NE ARG A 213 16.692 -35.595 37.021 1.00 32.93 N ANISOU 1643 NE ARG A 213 4829 3480 4202 91 -658 1162 N ATOM 1644 CZ ARG A 213 17.451 -34.919 37.872 1.00 32.86 C ANISOU 1644 CZ ARG A 213 4775 3602 4109 98 -679 1229 C ATOM 1645 NH1 ARG A 213 17.016 -34.651 39.099 1.00 33.12 N1+ ANISOU 1645 NH1 ARG A 213 4825 3761 3999 -23 -685 1331 N1+ ATOM 1646 NH2 ARG A 213 18.653 -34.510 37.482 1.00 32.79 N ANISOU 1646 NH2 ARG A 213 4698 3607 4151 216 -682 1177 N ATOM 1647 N ASN A 214 14.250 -37.709 33.178 1.00 31.73 N ANISOU 1647 N ASN A 214 4876 2892 4287 34 -690 718 N ATOM 1648 CA ASN A 214 15.279 -38.179 32.260 1.00 32.38 C ANISOU 1648 CA ASN A 214 5030 2841 4433 189 -670 589 C ATOM 1649 C ASN A 214 16.300 -37.086 31.977 1.00 31.39 C ANISOU 1649 C ASN A 214 4844 2871 4212 324 -577 553 C ATOM 1650 O ASN A 214 15.938 -35.942 31.613 1.00 30.62 O ANISOU 1650 O ASN A 214 4711 2953 3972 306 -533 513 O ATOM 1651 CB ASN A 214 14.649 -38.670 30.951 1.00 34.27 C ANISOU 1651 CB ASN A 214 5371 2984 4666 161 -701 388 C ATOM 1652 CG ASN A 214 13.749 -39.891 31.149 1.00 35.59 C ANISOU 1652 CG ASN A 214 5600 2948 4975 10 -802 403 C ATOM 1653 ND2 ASN A 214 14.356 -41.021 31.515 1.00 36.62 N ANISOU 1653 ND2 ASN A 214 5797 2827 5289 56 -822 451 N ATOM 1654 OD1 ASN A 214 12.523 -39.818 30.974 1.00 36.61 O ANISOU 1654 OD1 ASN A 214 5704 3133 5073 -147 -866 381 O ATOM 1655 N ASN A 215 17.569 -37.452 32.141 1.00 31.03 N ANISOU 1655 N ASN A 215 4774 2744 4273 459 -549 579 N ATOM 1656 CA ASN A 215 18.683 -36.529 31.986 1.00 30.85 C ANISOU 1656 CA ASN A 215 4659 2853 4207 572 -460 566 C ATOM 1657 C ASN A 215 19.262 -36.591 30.592 1.00 32.62 C ANISOU 1657 C ASN A 215 4931 3041 4422 696 -347 381 C ATOM 1658 O ASN A 215 19.551 -37.682 30.076 1.00 34.29 O ANISOU 1658 O ASN A 215 5214 3061 4752 780 -334 282 O ATOM 1659 CB ASN A 215 19.790 -36.846 32.989 1.00 31.14 C ANISOU 1659 CB ASN A 215 4598 2853 4379 647 -504 712 C ATOM 1660 CG ASN A 215 19.360 -36.600 34.421 1.00 30.38 C ANISOU 1660 CG ASN A 215 4472 2848 4224 518 -602 901 C ATOM 1661 ND2 ASN A 215 20.099 -37.167 35.367 1.00 31.31 N ANISOU 1661 ND2 ASN A 215 4543 2907 4446 558 -696 1061 N ATOM 1662 OD1 ASN A 215 18.371 -35.910 34.675 1.00 29.16 O ANISOU 1662 OD1 ASN A 215 4335 2819 3925 390 -592 906 O ATOM 1663 N PHE A 216 19.445 -35.429 29.975 1.00 31.45 N ANISOU 1663 N PHE A 216 4756 3064 4129 708 -251 331 N ATOM 1664 CA PHE A 216 20.028 -35.415 28.649 1.00 33.46 C ANISOU 1664 CA PHE A 216 5066 3317 4329 814 -114 170 C ATOM 1665 C PHE A 216 21.530 -35.698 28.689 1.00 34.93 C ANISOU 1665 C PHE A 216 5137 3459 4677 970 -5 168 C ATOM 1666 O PHE A 216 22.265 -35.134 29.498 1.00 34.41 O ANISOU 1666 O PHE A 216 4912 3476 4686 980 -10 296 O ATOM 1667 CB PHE A 216 19.755 -34.089 27.948 1.00 33.18 C ANISOU 1667 CB PHE A 216 5049 3470 4088 771 -42 154 C ATOM 1668 CG PHE A 216 20.375 -33.992 26.577 1.00 35.74 C ANISOU 1668 CG PHE A 216 5449 3827 4305 863 122 14 C ATOM 1669 CD1 PHE A 216 21.581 -33.340 26.394 1.00 36.85 C ANISOU 1669 CD1 PHE A 216 5479 4052 4469 939 287 41 C ATOM 1670 CD2 PHE A 216 19.751 -34.568 25.472 1.00 37.67 C ANISOU 1670 CD2 PHE A 216 5876 4026 4412 859 114 -149 C ATOM 1671 CE1 PHE A 216 22.159 -33.253 25.137 1.00 39.79 C ANISOU 1671 CE1 PHE A 216 5922 4472 4723 1015 476 -79 C ATOM 1672 CE2 PHE A 216 20.316 -34.480 24.196 1.00 40.47 C ANISOU 1672 CE2 PHE A 216 6330 4433 4614 936 283 -287 C ATOM 1673 CZ PHE A 216 21.518 -33.825 24.028 1.00 41.55 C ANISOU 1673 CZ PHE A 216 6357 4662 4768 1018 481 -245 C ATOM 1674 N GLU A 217 21.981 -36.566 27.792 1.00 66.50 N ANISOU 1674 N GLU A 217 9206 7326 8733 1093 95 6 N ATOM 1675 CA GLU A 217 23.407 -36.841 27.657 1.00 68.44 C ANISOU 1675 CA GLU A 217 9317 7534 9155 1269 236 -21 C ATOM 1676 C GLU A 217 23.942 -36.680 26.217 1.00 70.97 C ANISOU 1676 C GLU A 217 9699 7910 9358 1364 476 -218 C ATOM 1677 O GLU A 217 23.286 -37.059 25.242 1.00 71.88 O ANISOU 1677 O GLU A 217 10021 7980 9310 1344 507 -393 O ATOM 1678 CB GLU A 217 23.719 -38.212 28.253 1.00 68.86 C ANISOU 1678 CB GLU A 217 9349 7335 9479 1375 150 1 C ATOM 1679 CG GLU A 217 23.278 -38.265 29.710 1.00 67.18 C ANISOU 1679 CG GLU A 217 9081 7109 9337 1266 -69 232 C ATOM 1680 CD GLU A 217 23.727 -39.511 30.441 1.00 68.43 C ANISOU 1680 CD GLU A 217 9200 7027 9773 1373 -173 328 C ATOM 1681 OE1 GLU A 217 23.546 -40.619 29.878 1.00 70.00 O ANISOU 1681 OE1 GLU A 217 9530 6982 10086 1448 -149 192 O ATOM 1682 OE2 GLU A 217 24.254 -39.373 31.580 1.00 68.28 O1- ANISOU 1682 OE2 GLU A 217 9032 7056 9855 1379 -291 540 O1- ATOM 1683 N GLY A 218 25.141 -36.119 26.091 1.00 51.93 N ANISOU 1683 N GLY A 218 7105 5608 7018 1454 644 -188 N ATOM 1684 CA GLY A 218 25.718 -35.852 24.782 1.00 54.44 C ANISOU 1684 CA GLY A 218 7465 6015 7205 1530 913 -345 C ATOM 1685 C GLY A 218 25.743 -34.384 24.385 1.00 54.91 C ANISOU 1685 C GLY A 218 7505 6310 7049 1415 1008 -259 C ATOM 1686 O GLY A 218 25.364 -33.510 25.164 1.00 53.39 O ANISOU 1686 O GLY A 218 7250 6200 6836 1287 867 -92 O ATOM 1687 N GLU A 219 26.209 -34.113 23.171 1.00 55.18 N ANISOU 1687 N GLU A 219 7603 6441 6922 1461 1262 -375 N ATOM 1688 CA GLU A 219 26.325 -32.751 22.687 1.00 55.91 C ANISOU 1688 CA GLU A 219 7690 6733 6819 1356 1380 -274 C ATOM 1689 C GLU A 219 24.957 -32.110 22.610 1.00 54.64 C ANISOU 1689 C GLU A 219 7728 6622 6413 1203 1189 -207 C ATOM 1690 O GLU A 219 23.988 -32.755 22.223 1.00 54.24 O ANISOU 1690 O GLU A 219 7881 6504 6224 1187 1071 -319 O ATOM 1691 CB GLU A 219 26.976 -32.747 21.314 1.00 57.93 C ANISOU 1691 CB GLU A 219 8026 7082 6904 1430 1702 -413 C ATOM 1692 CG GLU A 219 27.443 -31.386 20.825 1.00 58.37 C ANISOU 1692 CG GLU A 219 8029 7331 6818 1333 1884 -275 C ATOM 1693 CD GLU A 219 28.175 -31.484 19.480 1.00 60.19 C ANISOU 1693 CD GLU A 219 8334 7667 6868 1409 2248 -409 C ATOM 1694 OE1 GLU A 219 29.387 -31.800 19.486 1.00 61.51 O ANISOU 1694 OE1 GLU A 219 8270 7840 7262 1527 2482 -457 O ATOM 1695 OE2 GLU A 219 27.537 -31.266 18.420 1.00 60.34 O1- ANISOU 1695 OE2 GLU A 219 8638 7772 6515 1353 2299 -465 O1- ATOM 1696 N VAL A 220 24.877 -30.833 22.951 1.00 55.78 N ANISOU 1696 N VAL A 220 7802 6872 6519 1089 1158 -31 N ATOM 1697 CA VAL A 220 23.590 -30.160 22.957 1.00 53.95 C ANISOU 1697 CA VAL A 220 7719 6676 6105 970 977 47 C ATOM 1698 C VAL A 220 23.340 -29.474 21.625 1.00 53.69 C ANISOU 1698 C VAL A 220 7874 6762 5763 936 1097 49 C ATOM 1699 O VAL A 220 23.946 -28.452 21.305 1.00 53.36 O ANISOU 1699 O VAL A 220 7784 6813 5677 896 1254 163 O ATOM 1700 CB VAL A 220 23.504 -29.124 24.107 1.00 51.25 C ANISOU 1700 CB VAL A 220 7226 6351 5894 873 861 225 C ATOM 1701 CG1 VAL A 220 22.236 -28.284 23.984 1.00 47.65 C ANISOU 1701 CG1 VAL A 220 6905 5930 5269 779 722 305 C ATOM 1702 CG2 VAL A 220 23.569 -29.829 25.448 1.00 49.77 C ANISOU 1702 CG2 VAL A 220 6901 6069 5942 888 705 238 C ATOM 1703 N THR A 221 22.410 -30.030 20.865 1.00 46.37 N ANISOU 1703 N THR A 221 7170 5832 4619 934 1003 -65 N ATOM 1704 CA THR A 221 22.059 -29.489 19.565 1.00 46.41 C ANISOU 1704 CA THR A 221 7389 5963 4280 898 1069 -59 C ATOM 1705 C THR A 221 20.563 -29.651 19.383 1.00 45.42 C ANISOU 1705 C THR A 221 7424 5831 4002 834 788 -76 C ATOM 1706 O THR A 221 19.933 -30.491 20.033 1.00 45.52 O ANISOU 1706 O THR A 221 7405 5731 4159 827 607 -157 O ATOM 1707 CB THR A 221 22.773 -30.236 18.409 1.00 49.03 C ANISOU 1707 CB THR A 221 7859 6339 4432 982 1312 -257 C ATOM 1708 CG2 THR A 221 24.260 -30.418 18.718 1.00 50.17 C ANISOU 1708 CG2 THR A 221 7781 6464 4817 1076 1585 -281 C ATOM 1709 OG1 THR A 221 22.153 -31.517 18.211 1.00 49.91 O ANISOU 1709 OG1 THR A 221 8110 6347 4506 1016 1182 -480 O ATOM 1710 N LYS A 222 19.989 -28.862 18.486 1.00 58.41 N ANISOU 1710 N LYS A 222 9232 7597 5365 782 746 16 N ATOM 1711 CA LYS A 222 18.567 -28.961 18.197 1.00 57.88 C ANISOU 1711 CA LYS A 222 9291 7549 5151 724 462 11 C ATOM 1712 C LYS A 222 18.182 -30.395 17.849 1.00 60.12 C ANISOU 1712 C LYS A 222 9698 7768 5377 729 370 -247 C ATOM 1713 O LYS A 222 17.167 -30.903 18.316 1.00 59.89 O ANISOU 1713 O LYS A 222 9640 7667 5448 676 126 -285 O ATOM 1714 CB LYS A 222 18.192 -28.023 17.049 1.00 58.08 C ANISOU 1714 CB LYS A 222 9503 7727 4836 688 443 143 C ATOM 1715 CG LYS A 222 16.707 -27.988 16.735 1.00 57.81 C ANISOU 1715 CG LYS A 222 9536 7733 4696 625 113 172 C ATOM 1716 CD LYS A 222 16.453 -27.436 15.344 1.00 59.44 C ANISOU 1716 CD LYS A 222 9848 8095 4642 560 79 241 C ATOM 1717 CE LYS A 222 15.014 -27.666 14.916 1.00 60.46 C ANISOU 1717 CE LYS A 222 10012 8281 4680 496 -255 225 C ATOM 1718 NZ LYS A 222 14.327 -26.394 14.566 1.00 60.63 N1+ ANISOU 1718 NZ LYS A 222 9961 8388 4689 465 -392 485 N1+ ATOM 1719 N GLU A 223 19.001 -31.042 17.027 1.00 50.56 N ANISOU 1719 N GLU A 223 8621 6574 4016 789 581 -432 N ATOM 1720 CA GLU A 223 18.729 -32.403 16.579 1.00 52.52 C ANISOU 1720 CA GLU A 223 9025 6733 4198 797 522 -715 C ATOM 1721 C GLU A 223 18.746 -33.411 17.722 1.00 52.42 C ANISOU 1721 C GLU A 223 8851 6499 4566 826 449 -796 C ATOM 1722 O GLU A 223 17.876 -34.273 17.813 1.00 52.93 O ANISOU 1722 O GLU A 223 8983 6455 4671 763 238 -921 O ATOM 1723 CB GLU A 223 19.734 -32.822 15.504 0.00 54.68 C ANISOU 1723 CB GLU A 223 9468 7062 4246 879 824 -913 C ATOM 1724 CG GLU A 223 19.905 -31.812 14.381 0.00 55.01 C ANISOU 1724 CG GLU A 223 9569 7333 3999 811 919 -776 C ATOM 1725 CD GLU A 223 21.091 -30.893 14.601 0.00 54.34 C ANISOU 1725 CD GLU A 223 9320 7309 4016 860 1210 -595 C ATOM 1726 OE1 GLU A 223 20.911 -29.831 15.233 0.81 52.64 O ANISOU 1726 OE1 GLU A 223 8996 7111 3892 827 1144 -340 O ATOM 1727 OE2 GLU A 223 22.202 -31.232 14.142 0.39 55.69 O1- ANISOU 1727 OE2 GLU A 223 9452 7508 4199 922 1503 -713 O1- ATOM 1728 N ASN A 224 19.747 -33.305 18.588 1.00 47.76 N ANISOU 1728 N ASN A 224 8047 5844 4256 909 614 -712 N ATOM 1729 CA ASN A 224 19.883 -34.223 19.712 1.00 47.55 C ANISOU 1729 CA ASN A 224 7871 5613 4581 946 548 -744 C ATOM 1730 C ASN A 224 18.744 -34.097 20.716 1.00 46.18 C ANISOU 1730 C ASN A 224 7603 5395 4547 833 271 -603 C ATOM 1731 O ASN A 224 18.268 -35.092 21.254 1.00 45.82 O ANISOU 1731 O ASN A 224 7553 5186 4671 803 134 -674 O ATOM 1732 CB ASN A 224 21.222 -34.010 20.414 1.00 47.29 C ANISOU 1732 CB ASN A 224 7613 5558 4797 1054 752 -653 C ATOM 1733 CG ASN A 224 22.401 -34.159 19.476 1.00 49.14 C ANISOU 1733 CG ASN A 224 7888 5842 4941 1175 1067 -791 C ATOM 1734 ND2 ASN A 224 23.387 -33.284 19.625 1.00 49.33 N ANISOU 1734 ND2 ASN A 224 7737 5976 5029 1207 1260 -649 N ATOM 1735 OD1 ASN A 224 22.427 -35.049 18.629 1.00 50.38 O ANISOU 1735 OD1 ASN A 224 8228 5938 4977 1231 1147 -1033 O ATOM 1736 N LEU A 225 18.313 -32.865 20.963 1.00 55.78 N ANISOU 1736 N LEU A 225 8746 6749 5701 771 207 -403 N ATOM 1737 CA LEU A 225 17.252 -32.606 21.928 1.00 53.15 C ANISOU 1737 CA LEU A 225 8301 6397 5497 678 -10 -270 C ATOM 1738 C LEU A 225 15.896 -33.079 21.422 1.00 54.24 C ANISOU 1738 C LEU A 225 8555 6534 5519 578 -239 -353 C ATOM 1739 O LEU A 225 15.104 -33.639 22.178 1.00 53.79 O ANISOU 1739 O LEU A 225 8422 6386 5630 501 -396 -343 O ATOM 1740 CB LEU A 225 17.199 -31.120 22.277 1.00 49.76 C ANISOU 1740 CB LEU A 225 7766 6090 5051 659 8 -60 C ATOM 1741 CG LEU A 225 18.412 -30.586 23.036 1.00 48.47 C ANISOU 1741 CG LEU A 225 7445 5921 5051 712 181 36 C ATOM 1742 CD1 LEU A 225 18.287 -29.090 23.267 1.00 46.14 C ANISOU 1742 CD1 LEU A 225 7084 5715 4733 676 192 216 C ATOM 1743 CD2 LEU A 225 18.586 -31.326 24.352 1.00 46.57 C ANISOU 1743 CD2 LEU A 225 7063 5559 5072 713 124 45 C ATOM 1744 N LEU A 226 15.631 -32.852 20.141 1.00 42.94 N ANISOU 1744 N LEU A 226 7306 5216 3794 566 -262 -427 N ATOM 1745 CA LEU A 226 14.378 -33.282 19.539 1.00 43.97 C ANISOU 1745 CA LEU A 226 7545 5369 3791 459 -511 -517 C ATOM 1746 C LEU A 226 14.268 -34.802 19.567 1.00 45.93 C ANISOU 1746 C LEU A 226 7874 5430 4149 419 -567 -746 C ATOM 1747 O LEU A 226 13.180 -35.351 19.717 1.00 46.31 O ANISOU 1747 O LEU A 226 7907 5423 4267 296 -794 -788 O ATOM 1748 CB LEU A 226 14.261 -32.762 18.106 1.00 44.69 C ANISOU 1748 CB LEU A 226 7848 5635 3499 457 -529 -550 C ATOM 1749 CG LEU A 226 13.826 -31.302 17.966 1.00 42.73 C ANISOU 1749 CG LEU A 226 7542 5549 3143 458 -594 -297 C ATOM 1750 CD1 LEU A 226 13.502 -30.962 16.521 1.00 44.25 C ANISOU 1750 CD1 LEU A 226 7970 5912 2931 433 -682 -313 C ATOM 1751 CD2 LEU A 226 12.642 -31.002 18.869 1.00 41.04 C ANISOU 1751 CD2 LEU A 226 7122 5317 3155 395 -818 -161 C ATOM 1752 N ASP A 227 15.404 -35.474 19.427 1.00 52.91 N ANISOU 1752 N ASP A 227 8827 6200 5076 523 -354 -890 N ATOM 1753 CA ASP A 227 15.449 -36.928 19.484 1.00 53.82 C ANISOU 1753 CA ASP A 227 9026 6083 5339 513 -378 -1110 C ATOM 1754 C ASP A 227 15.265 -37.404 20.918 1.00 52.21 C ANISOU 1754 C ASP A 227 8629 5707 5503 482 -449 -981 C ATOM 1755 O ASP A 227 14.527 -38.352 21.182 1.00 52.27 O ANISOU 1755 O ASP A 227 8663 5550 5649 375 -610 -1058 O ATOM 1756 CB ASP A 227 16.778 -37.444 18.934 1.00 54.78 C ANISOU 1756 CB ASP A 227 9254 6126 5432 671 -101 -1295 C ATOM 1757 CG ASP A 227 16.740 -37.671 17.439 1.00 56.90 C ANISOU 1757 CG ASP A 227 9806 6478 5336 663 -60 -1546 C ATOM 1758 OD1 ASP A 227 15.933 -37.009 16.755 1.00 57.27 O ANISOU 1758 OD1 ASP A 227 9949 6719 5090 560 -215 -1501 O ATOM 1759 OD2 ASP A 227 17.522 -38.511 16.948 1.00 58.16 O1- ANISOU 1759 OD2 ASP A 227 10094 6509 5496 767 129 -1791 O1- ATOM 1760 N PHE A 228 15.945 -36.732 21.837 1.00 46.91 N ANISOU 1760 N PHE A 228 7771 5078 4974 561 -331 -780 N ATOM 1761 CA PHE A 228 15.861 -37.042 23.257 1.00 44.50 C ANISOU 1761 CA PHE A 228 7293 4653 4962 533 -386 -626 C ATOM 1762 C PHE A 228 14.429 -36.913 23.761 1.00 44.13 C ANISOU 1762 C PHE A 228 7175 4643 4949 363 -603 -525 C ATOM 1763 O PHE A 228 13.922 -37.791 24.453 1.00 43.45 O ANISOU 1763 O PHE A 228 7056 4398 5056 274 -704 -510 O ATOM 1764 CB PHE A 228 16.792 -36.115 24.044 1.00 42.13 C ANISOU 1764 CB PHE A 228 6820 4450 4738 625 -246 -438 C ATOM 1765 CG PHE A 228 16.564 -36.134 25.528 1.00 38.97 C ANISOU 1765 CG PHE A 228 6256 4002 4551 571 -325 -251 C ATOM 1766 CD1 PHE A 228 16.917 -37.237 26.284 1.00 38.36 C ANISOU 1766 CD1 PHE A 228 6154 3720 4701 594 -344 -239 C ATOM 1767 CD2 PHE A 228 16.011 -35.040 26.169 1.00 36.79 C ANISOU 1767 CD2 PHE A 228 5862 3878 4237 502 -372 -85 C ATOM 1768 CE1 PHE A 228 16.713 -37.254 27.649 1.00 36.02 C ANISOU 1768 CE1 PHE A 228 5733 3402 4551 533 -416 -49 C ATOM 1769 CE2 PHE A 228 15.804 -35.049 27.534 1.00 34.41 C ANISOU 1769 CE2 PHE A 228 5434 3555 4086 446 -422 68 C ATOM 1770 CZ PHE A 228 16.156 -36.158 28.275 1.00 34.19 C ANISOU 1770 CZ PHE A 228 5396 3351 4243 453 -447 94 C ATOM 1771 N ILE A 229 13.779 -35.813 23.401 1.00 53.31 N ANISOU 1771 N ILE A 229 8305 6011 5940 322 -667 -443 N ATOM 1772 CA ILE A 229 12.424 -35.534 23.860 1.00 53.40 C ANISOU 1772 CA ILE A 229 8201 6087 6003 186 -850 -337 C ATOM 1773 C ILE A 229 11.394 -36.497 23.279 1.00 55.20 C ANISOU 1773 C ILE A 229 8513 6235 6224 43 -1049 -486 C ATOM 1774 O ILE A 229 10.739 -37.237 24.008 1.00 55.68 O ANISOU 1774 O ILE A 229 8493 6175 6486 -77 -1142 -459 O ATOM 1775 CB ILE A 229 12.007 -34.094 23.516 1.00 48.99 C ANISOU 1775 CB ILE A 229 7583 5745 5286 208 -874 -214 C ATOM 1776 CG1 ILE A 229 12.887 -33.095 24.266 1.00 45.75 C ANISOU 1776 CG1 ILE A 229 7069 5389 4926 308 -698 -62 C ATOM 1777 CG2 ILE A 229 10.541 -33.873 23.849 1.00 48.77 C ANISOU 1777 CG2 ILE A 229 7414 5784 5332 88 -1065 -131 C ATOM 1778 CD1 ILE A 229 12.845 -31.697 23.695 1.00 44.26 C ANISOU 1778 CD1 ILE A 229 6882 5361 4575 360 -672 37 C ATOM 1779 N LYS A 230 11.246 -36.473 21.961 1.00 79.37 N ANISOU 1779 N LYS A 230 11743 9372 9042 39 -1120 -639 N ATOM 1780 CA LYS A 230 10.260 -37.310 21.293 1.00 81.99 C ANISOU 1780 CA LYS A 230 12168 9650 9335 -117 -1344 -806 C ATOM 1781 C LYS A 230 10.378 -38.768 21.724 1.00 83.25 C ANISOU 1781 C LYS A 230 12384 9524 9725 -188 -1346 -940 C ATOM 1782 O LYS A 230 9.448 -39.553 21.548 1.00 85.27 O ANISOU 1782 O LYS A 230 12660 9684 10053 -362 -1541 -1044 O ATOM 1783 CB LYS A 230 10.404 -37.199 19.775 1.00 74.41 C ANISOU 1783 CB LYS A 230 11445 8800 8026 -93 -1386 -988 C ATOM 1784 CG LYS A 230 10.432 -38.538 19.056 1.00 77.59 C ANISOU 1784 CG LYS A 230 12075 9021 8387 -168 -1447 -1296 C ATOM 1785 CD LYS A 230 11.573 -38.601 18.056 1.00 79.16 C ANISOU 1785 CD LYS A 230 12521 9236 8321 -25 -1241 -1485 C ATOM 1786 CE LYS A 230 11.492 -37.463 17.050 1.00 79.73 C ANISOU 1786 CE LYS A 230 12684 9603 8009 8 -1266 -1420 C ATOM 1787 NZ LYS A 230 12.541 -37.580 16.000 1.00 81.90 N1+ ANISOU 1787 NZ LYS A 230 13217 9915 7987 121 -1043 -1617 N1+ ATOM 1788 N HIS A 231 11.525 -39.123 22.290 1.00 85.43 N ANISOU 1788 N HIS A 231 12674 9651 10134 -55 -1141 -927 N ATOM 1789 CA HIS A 231 11.780 -40.492 22.688 1.00 86.93 C ANISOU 1789 CA HIS A 231 12932 9534 10562 -84 -1129 -1031 C ATOM 1790 C HIS A 231 11.352 -40.771 24.099 1.00 85.61 C ANISOU 1790 C HIS A 231 12582 9268 10679 -176 -1167 -812 C ATOM 1791 O HIS A 231 10.764 -41.832 24.387 1.00 87.36 O ANISOU 1791 O HIS A 231 12828 9271 11094 -325 -1277 -853 O ATOM 1792 CB HIS A 231 13.254 -40.826 22.512 1.00 77.36 C ANISOU 1792 CB HIS A 231 11823 8200 9371 126 -900 -1131 C ATOM 1793 CG HIS A 231 13.715 -41.998 23.343 1.00 78.20 C ANISOU 1793 CG HIS A 231 11924 7985 9802 157 -860 -1120 C ATOM 1794 CD2 HIS A 231 14.912 -42.709 23.336 1.00 79.52 C ANISOU 1794 CD2 HIS A 231 12161 7939 10112 340 -694 -1217 C ATOM 1795 ND1 HIS A 231 12.945 -42.557 24.292 1.00 78.11 N ANISOU 1795 ND1 HIS A 231 11824 7835 10019 1 -992 -980 N ATOM 1796 CE1 HIS A 231 13.612 -43.576 24.866 1.00 79.31 C ANISOU 1796 CE1 HIS A 231 12012 7688 10434 75 -932 -969 C ATOM 1797 NE2 HIS A 231 14.815 -43.668 24.279 1.00 80.17 N ANISOU 1797 NE2 HIS A 231 12209 7747 10506 295 -757 -1119 N ATOM 1798 N ASN A 232 11.635 -39.837 25.001 1.00 54.18 N ANISOU 1798 N ASN A 232 8429 5439 6719 -105 -1072 -579 N ATOM 1799 CA ASN A 232 11.325 -40.017 26.415 1.00 53.08 C ANISOU 1799 CA ASN A 232 8131 5242 6795 -184 -1077 -358 C ATOM 1800 C ASN A 232 9.996 -39.393 26.825 1.00 52.37 C ANISOU 1800 C ASN A 232 7868 5329 6702 -342 -1185 -229 C ATOM 1801 O ASN A 232 9.620 -39.433 27.993 1.00 51.67 O ANISOU 1801 O ASN A 232 7644 5236 6752 -423 -1165 -46 O ATOM 1802 CB ASN A 232 12.450 -39.445 27.280 1.00 41.00 C ANISOU 1802 CB ASN A 232 6520 3764 5293 -25 -914 -197 C ATOM 1803 CG ASN A 232 13.698 -40.302 27.254 1.00 42.13 C ANISOU 1803 CG ASN A 232 6764 3688 5556 122 -818 -268 C ATOM 1804 ND2 ASN A 232 13.618 -41.479 27.857 1.00 43.66 N ANISOU 1804 ND2 ASN A 232 6992 3623 5974 63 -870 -228 N ATOM 1805 OD1 ASN A 232 14.722 -39.910 26.702 1.00 41.92 O ANISOU 1805 OD1 ASN A 232 6771 3717 5438 289 -690 -346 O ATOM 1806 N GLN A 233 9.290 -38.819 25.859 1.00 80.66 N ANISOU 1806 N GLN A 233 11452 9074 10120 -380 -1295 -319 N ATOM 1807 CA GLN A 233 8.050 -38.102 26.133 1.00 80.29 C ANISOU 1807 CA GLN A 233 11205 9213 10086 -490 -1395 -200 C ATOM 1808 C GLN A 233 6.860 -39.019 26.407 1.00 82.34 C ANISOU 1808 C GLN A 233 11376 9374 10538 -723 -1546 -203 C ATOM 1809 O GLN A 233 5.939 -38.647 27.131 1.00 82.07 O ANISOU 1809 O GLN A 233 11123 9449 10610 -821 -1561 -56 O ATOM 1810 CB GLN A 233 7.722 -37.159 24.975 1.00 70.58 C ANISOU 1810 CB GLN A 233 9999 8189 8629 -435 -1491 -264 C ATOM 1811 CG GLN A 233 6.661 -36.121 25.299 1.00 69.97 C ANISOU 1811 CG GLN A 233 9688 8317 8580 -466 -1558 -110 C ATOM 1812 CD GLN A 233 6.063 -35.492 24.056 1.00 71.38 C ANISOU 1812 CD GLN A 233 9889 8661 8571 -453 -1740 -165 C ATOM 1813 NE2 GLN A 233 4.886 -34.896 24.201 1.00 71.94 N ANISOU 1813 NE2 GLN A 233 9733 8875 8727 -508 -1865 -58 N ATOM 1814 OE1 GLN A 233 6.653 -35.542 22.978 1.00 72.27 O ANISOU 1814 OE1 GLN A 233 10218 8779 8461 -390 -1765 -295 O ATOM 1815 N LEU A 234 6.875 -40.212 25.823 1.00 58.82 N ANISOU 1815 N LEU A 234 8559 6177 7612 -819 -1643 -381 N ATOM 1816 CA LEU A 234 5.755 -41.137 25.958 1.00 61.30 C ANISOU 1816 CA LEU A 234 8799 6369 8122 -1074 -1803 -405 C ATOM 1817 C LEU A 234 5.933 -42.090 27.133 1.00 61.62 C ANISOU 1817 C LEU A 234 8829 6169 8416 -1162 -1707 -273 C ATOM 1818 O LEU A 234 7.049 -42.493 27.451 1.00 61.01 O ANISOU 1818 O LEU A 234 8893 5921 8365 -1025 -1579 -264 O ATOM 1819 CB LEU A 234 5.565 -41.935 24.666 1.00 54.33 C ANISOU 1819 CB LEU A 234 8116 5361 7168 -1167 -1989 -689 C ATOM 1820 CG LEU A 234 4.896 -41.208 23.499 1.00 55.33 C ANISOU 1820 CG LEU A 234 8226 5735 7061 -1186 -2183 -797 C ATOM 1821 CD1 LEU A 234 4.876 -42.088 22.258 1.00 58.68 C ANISOU 1821 CD1 LEU A 234 8906 6023 7367 -1280 -2355 -1110 C ATOM 1822 CD2 LEU A 234 3.488 -40.775 23.873 1.00 55.86 C ANISOU 1822 CD2 LEU A 234 7982 5981 7260 -1353 -2333 -646 C ATOM 1823 N PRO A 235 4.822 -42.448 27.770 1.00 50.82 N ANISOU 1823 N PRO A 235 7280 4789 7240 -1391 -1771 -154 N ATOM 1824 CA PRO A 235 4.845 -43.380 28.900 1.00 51.69 C ANISOU 1824 CA PRO A 235 7384 4674 7582 -1514 -1687 11 C ATOM 1825 C PRO A 235 4.985 -44.821 28.432 1.00 54.73 C ANISOU 1825 C PRO A 235 7977 4686 8132 -1634 -1790 -151 C ATOM 1826 O PRO A 235 4.745 -45.111 27.264 1.00 56.55 O ANISOU 1826 O PRO A 235 8317 4865 8305 -1685 -1950 -408 O ATOM 1827 CB PRO A 235 3.478 -43.170 29.559 1.00 42.56 C ANISOU 1827 CB PRO A 235 5941 3672 6556 -1738 -1710 174 C ATOM 1828 CG PRO A 235 2.623 -42.568 28.498 1.00 43.30 C ANISOU 1828 CG PRO A 235 5916 3973 6562 -1779 -1892 24 C ATOM 1829 CD PRO A 235 3.549 -41.717 27.684 1.00 41.17 C ANISOU 1829 CD PRO A 235 5797 3825 6019 -1507 -1873 -97 C ATOM 1830 N LEU A 236 5.389 -45.705 29.337 1.00 71.42 N ANISOU 1830 N LEU A 236 10162 6532 10440 -1674 -1705 -1 N ATOM 1831 CA LEU A 236 5.573 -47.115 29.013 1.00 74.61 C ANISOU 1831 CA LEU A 236 10755 6566 11029 -1746 -1754 -133 C ATOM 1832 C LEU A 236 4.336 -47.685 28.329 1.00 77.80 C ANISOU 1832 C LEU A 236 11085 6966 11508 -1997 -1903 -291 C ATOM 1833 O LEU A 236 4.440 -48.520 27.434 1.00 80.45 O ANISOU 1833 O LEU A 236 11586 7117 11864 -2008 -1965 -545 O ATOM 1834 CB LEU A 236 5.890 -47.916 30.277 1.00 65.47 C ANISOU 1834 CB LEU A 236 9591 5235 10048 -1751 -1606 132 C ATOM 1835 CG LEU A 236 6.681 -49.212 30.088 1.00 68.07 C ANISOU 1835 CG LEU A 236 10126 5217 10522 -1650 -1557 33 C ATOM 1836 CD1 LEU A 236 7.728 -49.056 28.996 1.00 67.48 C ANISOU 1836 CD1 LEU A 236 10237 5077 10328 -1405 -1559 -249 C ATOM 1837 CD2 LEU A 236 7.323 -49.641 31.397 1.00 68.07 C ANISOU 1837 CD2 LEU A 236 10125 5121 10618 -1563 -1416 336 C ATOM 1838 N VAL A 237 3.166 -47.234 28.766 1.00 80.18 N ANISOU 1838 N VAL A 237 11124 7483 11857 -2194 -1945 -144 N ATOM 1839 CA VAL A 237 1.907 -47.675 28.185 1.00 83.37 C ANISOU 1839 CA VAL A 237 11398 7931 12348 -2435 -2092 -266 C ATOM 1840 C VAL A 237 1.130 -46.481 27.653 1.00 82.22 C ANISOU 1840 C VAL A 237 11039 8142 12060 -2460 -2231 -301 C ATOM 1841 O VAL A 237 0.626 -45.666 28.424 1.00 80.63 O ANISOU 1841 O VAL A 237 10587 8163 11887 -2492 -2166 -83 O ATOM 1842 CB VAL A 237 1.039 -48.411 29.217 1.00 75.71 C ANISOU 1842 CB VAL A 237 10254 6890 11622 -2668 -1999 -47 C ATOM 1843 CG1 VAL A 237 1.729 -49.687 29.668 1.00 77.60 C ANISOU 1843 CG1 VAL A 237 10710 6765 12011 -2649 -1887 -8 C ATOM 1844 CG2 VAL A 237 0.751 -47.504 30.403 1.00 73.32 C ANISOU 1844 CG2 VAL A 237 9718 6833 11309 -2670 -1854 259 C ATOM 1845 N ILE A 238 1.039 -46.379 26.332 1.00 90.14 N ANISOU 1845 N ILE A 238 12140 9209 12899 -2431 -2411 -572 N ATOM 1846 CA ILE A 238 0.365 -45.254 25.699 1.00 89.46 C ANISOU 1846 CA ILE A 238 11872 9468 12650 -2414 -2568 -602 C ATOM 1847 C ILE A 238 -1.030 -45.627 25.218 1.00 93.20 C ANISOU 1847 C ILE A 238 12133 10049 13231 -2645 -2740 -671 C ATOM 1848 O ILE A 238 -1.263 -46.748 24.770 1.00 96.61 O ANISOU 1848 O ILE A 238 12676 10282 13751 -2792 -2803 -839 O ATOM 1849 CB ILE A 238 1.174 -44.714 24.506 1.00 78.44 C ANISOU 1849 CB ILE A 238 10723 8149 10931 -2205 -2653 -824 C ATOM 1850 CG1 ILE A 238 2.674 -44.800 24.798 1.00 76.05 C ANISOU 1850 CG1 ILE A 238 10693 7642 10560 -1992 -2473 -838 C ATOM 1851 CG2 ILE A 238 0.771 -43.283 24.195 1.00 76.67 C ANISOU 1851 CG2 ILE A 238 10317 8287 10526 -2109 -2753 -744 C ATOM 1852 CD1 ILE A 238 3.427 -45.716 23.860 1.00 78.18 C ANISOU 1852 CD1 ILE A 238 11281 7688 10738 -1914 -2459 -1126 C ATOM 1853 N GLU A 239 -1.953 -44.675 25.310 1.00 86.19 N ANISOU 1853 N GLU A 239 10926 9470 12350 -2668 -2811 -546 N ATOM 1854 CA GLU A 239 -3.321 -44.885 24.858 1.00 89.89 C ANISOU 1854 CA GLU A 239 11143 10080 12930 -2864 -2982 -595 C ATOM 1855 C GLU A 239 -3.398 -44.872 23.337 1.00 92.01 C ANISOU 1855 C GLU A 239 11564 10436 12958 -2833 -3228 -860 C ATOM 1856 O GLU A 239 -3.284 -43.819 22.710 1.00 90.60 O ANISOU 1856 O GLU A 239 11380 10498 12546 -2658 -3322 -865 O ATOM 1857 CB GLU A 239 -4.242 -43.811 25.435 1.00 79.09 C ANISOU 1857 CB GLU A 239 9368 9024 11660 -2849 -2957 -375 C ATOM 1858 CG GLU A 239 -5.498 -44.356 26.092 1.00 82.29 C ANISOU 1858 CG GLU A 239 9446 9451 12368 -3098 -2911 -267 C ATOM 1859 CD GLU A 239 -6.314 -43.272 26.765 1.00 81.55 C ANISOU 1859 CD GLU A 239 8947 9656 12383 -3043 -2820 -56 C ATOM 1860 OE1 GLU A 239 -5.887 -42.099 26.730 1.00 78.50 O ANISOU 1860 OE1 GLU A 239 8541 9441 11846 -2811 -2801 9 O ATOM 1861 OE2 GLU A 239 -7.381 -43.591 27.329 1.00 84.30 O1- ANISOU 1861 OE2 GLU A 239 8994 10063 12973 -3227 -2750 37 O1- TER 1862 GLU A 239 ATOM 1863 N ALA A 245 -0.846 -41.243 18.989 1.00 73.66 N ANISOU 1863 N ALA A 245 10051 8867 9070 -1920 -3519 -1216 N ATOM 1864 CA ALA A 245 -1.306 -41.718 17.696 1.00 77.95 C ANISOU 1864 CA ALA A 245 10706 9492 9421 -2021 -3717 -1435 C ATOM 1865 C ALA A 245 -0.255 -41.349 16.670 1.00 77.68 C ANISOU 1865 C ALA A 245 11013 9527 8974 -1833 -3649 -1565 C ATOM 1866 O ALA A 245 0.492 -42.204 16.196 1.00 78.92 O ANISOU 1866 O ALA A 245 11465 9506 9015 -1845 -3559 -1810 O ATOM 1867 CB ALA A 245 -2.640 -41.085 17.342 1.00 80.27 C ANISOU 1867 CB ALA A 245 10680 10069 9749 -2082 -3957 -1314 C ATOM 1868 N PRO A 246 -0.195 -40.068 16.327 1.00 93.96 N ANISOU 1868 N PRO A 246 13029 11846 10826 -1653 -3667 -1395 N ATOM 1869 CA PRO A 246 0.822 -39.581 15.392 1.00 93.70 C ANISOU 1869 CA PRO A 246 13300 11908 10395 -1472 -3561 -1468 C ATOM 1870 C PRO A 246 2.216 -39.877 15.928 1.00 90.80 C ANISOU 1870 C PRO A 246 13165 11310 10026 -1349 -3270 -1535 C ATOM 1871 O PRO A 246 3.135 -40.137 15.156 1.00 91.81 O ANISOU 1871 O PRO A 246 13586 11407 9891 -1267 -3139 -1719 O ATOM 1872 CB PRO A 246 0.572 -38.069 15.349 1.00 91.80 C ANISOU 1872 CB PRO A 246 12892 11931 10058 -1302 -3593 -1185 C ATOM 1873 CG PRO A 246 -0.204 -37.763 16.583 1.00 89.88 C ANISOU 1873 CG PRO A 246 12288 11667 10197 -1340 -3621 -973 C ATOM 1874 CD PRO A 246 -1.040 -38.979 16.840 1.00 92.54 C ANISOU 1874 CD PRO A 246 12500 11868 10794 -1597 -3750 -1111 C ATOM 1875 N LYS A 247 2.360 -39.844 17.248 1.00 92.98 N ANISOU 1875 N LYS A 247 13295 11435 10598 -1337 -3162 -1387 N ATOM 1876 CA LYS A 247 3.634 -40.139 17.888 1.00 90.74 C ANISOU 1876 CA LYS A 247 13197 10923 10356 -1221 -2908 -1429 C ATOM 1877 C LYS A 247 3.928 -41.632 17.829 1.00 92.75 C ANISOU 1877 C LYS A 247 13625 10876 10739 -1335 -2856 -1686 C ATOM 1878 O LYS A 247 5.085 -42.043 17.764 1.00 92.27 O ANISOU 1878 O LYS A 247 13799 10642 10617 -1209 -2647 -1821 O ATOM 1879 CB LYS A 247 3.633 -39.658 19.338 1.00 88.46 C ANISOU 1879 CB LYS A 247 12691 10580 10341 -1193 -2834 -1186 C ATOM 1880 CG LYS A 247 3.087 -38.254 19.522 1.00 87.55 C ANISOU 1880 CG LYS A 247 12335 10740 10189 -1102 -2898 -928 C ATOM 1881 CD LYS A 247 3.608 -37.623 20.803 1.00 85.55 C ANISOU 1881 CD LYS A 247 11915 10467 10121 -951 -2605 -698 C ATOM 1882 CE LYS A 247 3.342 -36.127 20.825 1.00 84.70 C ANISOU 1882 CE LYS A 247 11639 10604 9939 -800 -2601 -477 C ATOM 1883 NZ LYS A 247 2.537 -35.716 22.009 1.00 84.14 N1+ ANISOU 1883 NZ LYS A 247 11218 10578 10174 -830 -2555 -275 N1+ ATOM 1884 N ILE A 248 2.874 -42.442 17.850 1.00 87.73 N ANISOU 1884 N ILE A 248 12856 10172 10306 -1565 -3030 -1748 N ATOM 1885 CA ILE A 248 3.028 -43.887 17.744 1.00 90.71 C ANISOU 1885 CA ILE A 248 13386 10249 10829 -1691 -2992 -1988 C ATOM 1886 C ILE A 248 3.723 -44.261 16.435 1.00 93.49 C ANISOU 1886 C ILE A 248 14052 10609 10861 -1613 -2933 -2289 C ATOM 1887 O ILE A 248 4.687 -45.019 16.431 1.00 93.95 O ANISOU 1887 O ILE A 248 14321 10419 10958 -1530 -2734 -2461 O ATOM 1888 CB ILE A 248 1.675 -44.622 17.837 1.00 94.02 C ANISOU 1888 CB ILE A 248 13599 10632 11491 -1974 -3204 -2009 C ATOM 1889 CG1 ILE A 248 1.172 -44.660 19.284 1.00 91.88 C ANISOU 1889 CG1 ILE A 248 13047 10258 11604 -2073 -3168 -1748 C ATOM 1890 CG2 ILE A 248 1.818 -46.038 17.322 1.00 98.12 C ANISOU 1890 CG2 ILE A 248 14326 10883 12071 -2101 -3191 -2314 C ATOM 1891 CD1 ILE A 248 0.704 -43.333 19.821 1.00 88.85 C ANISOU 1891 CD1 ILE A 248 12387 10151 11221 -2000 -3209 -1463 C ATOM 1892 N PHE A 249 3.236 -43.722 15.325 1.00101.93 N ANISOU 1892 N PHE A 249 15138 11970 11620 -1632 -3092 -2343 N ATOM 1893 CA PHE A 249 3.835 -44.006 14.028 1.00105.07 C ANISOU 1893 CA PHE A 249 15823 12425 11672 -1575 -3031 -2622 C ATOM 1894 C PHE A 249 5.198 -43.343 13.900 1.00102.31 C ANISOU 1894 C PHE A 249 15652 12120 11099 -1309 -2749 -2590 C ATOM 1895 O PHE A 249 6.110 -43.890 13.264 1.00104.17 O ANISOU 1895 O PHE A 249 16132 12262 11186 -1223 -2558 -2837 O ATOM 1896 CB PHE A 249 2.920 -43.547 12.898 1.00108.37 C ANISOU 1896 CB PHE A 249 16201 13169 11803 -1671 -3291 -2652 C ATOM 1897 CG PHE A 249 1.662 -44.348 12.784 1.00112.27 C ANISOU 1897 CG PHE A 249 16551 13625 12482 -1943 -3561 -2760 C ATOM 1898 CD1 PHE A 249 0.620 -43.923 11.971 1.00115.36 C ANISOU 1898 CD1 PHE A 249 16823 14312 12696 -2049 -3849 -2740 C ATOM 1899 CD2 PHE A 249 1.519 -45.529 13.488 1.00113.19 C ANISOU 1899 CD2 PHE A 249 16641 13406 12960 -2094 -3526 -2869 C ATOM 1900 CE1 PHE A 249 -0.548 -44.667 11.863 1.00119.30 C ANISOU 1900 CE1 PHE A 249 17166 14785 13378 -2309 -4102 -2847 C ATOM 1901 CE2 PHE A 249 0.362 -46.277 13.389 1.00117.09 C ANISOU 1901 CE2 PHE A 249 16991 13859 13638 -2363 -3759 -2965 C ATOM 1902 CZ PHE A 249 -0.677 -45.848 12.574 1.00120.12 C ANISOU 1902 CZ PHE A 249 17244 14551 13845 -2475 -4050 -2964 C ATOM 1903 N GLY A 250 5.348 -42.172 14.510 1.00129.18 N ANISOU 1903 N GLY A 250 18919 15667 14496 -1178 -2706 -2294 N ATOM 1904 CA GLY A 250 6.634 -41.504 14.470 1.00126.49 C ANISOU 1904 CA GLY A 250 18719 15368 13973 -938 -2430 -2242 C ATOM 1905 C GLY A 250 7.757 -42.387 15.003 1.00125.73 C ANISOU 1905 C GLY A 250 18759 14947 14064 -836 -2165 -2393 C ATOM 1906 O GLY A 250 8.932 -42.185 14.666 1.00125.21 O ANISOU 1906 O GLY A 250 18846 14892 13835 -647 -1902 -2459 O ATOM 1907 N GLY A 251 7.393 -43.392 15.800 1.00 76.95 N ANISOU 1907 N GLY A 251 12509 8482 8248 -960 -2224 -2436 N ATOM 1908 CA GLY A 251 8.355 -44.184 16.553 1.00 75.93 C ANISOU 1908 CA GLY A 251 12448 8016 8386 -853 -1998 -2495 C ATOM 1909 C GLY A 251 9.343 -45.040 15.781 1.00 78.82 C ANISOU 1909 C GLY A 251 13044 8227 8678 -742 -1774 -2802 C ATOM 1910 O GLY A 251 9.123 -45.381 14.615 1.00 82.61 O ANISOU 1910 O GLY A 251 13660 8803 8926 -815 -1821 -3046 O ATOM 1911 N GLU A 252 10.439 -45.391 16.450 1.00112.93 N ANISOU 1911 N GLU A 252 17388 12310 13209 -558 -1527 -2789 N ATOM 1912 CA GLU A 252 11.500 -46.214 15.853 1.00115.69 C ANISOU 1912 CA GLU A 252 17904 12488 13566 -412 -1270 -3065 C ATOM 1913 C GLU A 252 11.241 -47.725 15.956 1.00119.24 C ANISOU 1913 C GLU A 252 18403 12574 14329 -532 -1301 -3268 C ATOM 1914 O GLU A 252 11.859 -48.523 15.247 1.00122.71 O ANISOU 1914 O GLU A 252 18988 12873 14763 -460 -1134 -3564 O ATOM 1915 CB GLU A 252 12.877 -45.866 16.465 1.00112.94 C ANISOU 1915 CB GLU A 252 17517 12070 13325 -131 -975 -2948 C ATOM 1916 CG GLU A 252 13.577 -44.658 15.831 1.00111.62 C ANISOU 1916 CG GLU A 252 17383 12236 12792 28 -808 -2897 C ATOM 1917 CD GLU A 252 14.088 -44.924 14.412 1.00115.80 C ANISOU 1917 CD GLU A 252 18084 12884 13030 76 -641 -3200 C ATOM 1918 OE1 GLU A 252 14.953 -45.814 14.226 1.00118.36 O ANISOU 1918 OE1 GLU A 252 18461 12998 13515 202 -418 -3419 O ATOM 1919 OE2 GLU A 252 13.625 -44.235 13.478 1.00116.83 O1- ANISOU 1919 OE2 GLU A 252 18287 13326 12779 -8 -733 -3213 O1- ATOM 1920 N ILE A 253 10.308 -48.105 16.824 1.00 89.17 N ANISOU 1920 N ILE A 253 14464 8616 10800 -723 -1503 -3110 N ATOM 1921 CA ILE A 253 9.992 -49.514 17.036 1.00 92.52 C ANISOU 1921 CA ILE A 253 14921 8680 11552 -861 -1532 -3249 C ATOM 1922 C ILE A 253 8.879 -49.983 16.110 1.00 96.60 C ANISOU 1922 C ILE A 253 15501 9265 11937 -1128 -1755 -3482 C ATOM 1923 O ILE A 253 7.796 -49.394 16.063 1.00 95.96 O ANISOU 1923 O ILE A 253 15297 9423 11741 -1308 -2003 -3358 O ATOM 1924 CB ILE A 253 9.616 -49.792 18.503 1.00 90.41 C ANISOU 1924 CB ILE A 253 14473 8201 11678 -942 -1597 -2935 C ATOM 1925 CG1 ILE A 253 8.493 -48.855 18.950 1.00 87.79 C ANISOU 1925 CG1 ILE A 253 13948 8138 11271 -1115 -1836 -2680 C ATOM 1926 CG2 ILE A 253 10.825 -49.599 19.402 1.00 87.32 C ANISOU 1926 CG2 ILE A 253 14034 7687 11457 -673 -1371 -2741 C ATOM 1927 CD1 ILE A 253 8.379 -48.753 20.453 1.00 84.83 C ANISOU 1927 CD1 ILE A 253 13381 7649 11202 -1133 -1833 -2327 C ATOM 1928 N LYS A 254 9.155 -51.045 15.365 1.00 86.74 N ANISOU 1928 N LYS A 254 14429 7808 10721 -1149 -1665 -3828 N ATOM 1929 CA LYS A 254 8.184 -51.538 14.404 1.00 91.22 C ANISOU 1929 CA LYS A 254 15074 8438 11146 -1401 -1872 -4095 C ATOM 1930 C LYS A 254 7.324 -52.685 14.938 1.00 93.82 C ANISOU 1930 C LYS A 254 15348 8442 11855 -1659 -2006 -4114 C ATOM 1931 O LYS A 254 6.495 -53.233 14.215 1.00 98.14 O ANISOU 1931 O LYS A 254 15950 8996 12342 -1893 -2182 -4350 O ATOM 1932 CB LYS A 254 8.874 -51.912 13.087 1.00 95.45 C ANISOU 1932 CB LYS A 254 15846 9004 11415 -1305 -1716 -4508 C ATOM 1933 CG LYS A 254 9.622 -50.729 12.457 1.00 93.32 C ANISOU 1933 CG LYS A 254 15624 9105 10728 -1086 -1583 -4471 C ATOM 1934 CD LYS A 254 8.754 -49.478 12.493 1.00 90.41 C ANISOU 1934 CD LYS A 254 15117 9124 10111 -1180 -1831 -4184 C ATOM 1935 CE LYS A 254 9.449 -48.256 11.916 1.00 88.34 C ANISOU 1935 CE LYS A 254 14900 9218 9446 -980 -1697 -4097 C ATOM 1936 NZ LYS A 254 8.613 -47.036 12.145 1.00 85.24 N1+ ANISOU 1936 NZ LYS A 254 14344 9144 8899 -1053 -1929 -3769 N1+ ATOM 1937 N THR A 255 7.514 -53.043 16.202 1.00 54.11 N ANISOU 1937 N THR A 255 6115 7385 7061 -103 945 1543 N ATOM 1938 CA THR A 255 6.737 -54.121 16.811 1.00 51.37 C ANISOU 1938 CA THR A 255 5811 7051 6658 29 736 1261 C ATOM 1939 C THR A 255 5.801 -53.580 17.879 1.00 50.66 C ANISOU 1939 C THR A 255 5849 6760 6637 -86 494 1140 C ATOM 1940 O THR A 255 6.234 -52.968 18.841 1.00 50.60 O ANISOU 1940 O THR A 255 5773 6617 6837 -303 400 1167 O ATOM 1941 CB THR A 255 7.649 -55.209 17.418 1.00 49.52 C ANISOU 1941 CB THR A 255 5323 6918 6576 35 712 1180 C ATOM 1942 CG2 THR A 255 6.821 -56.276 18.110 1.00 47.37 C ANISOU 1942 CG2 THR A 255 5158 6593 6248 117 495 934 C ATOM 1943 OG1 THR A 255 8.427 -55.821 16.378 1.00 50.60 O ANISOU 1943 OG1 THR A 255 5343 7269 6612 232 959 1245 O ATOM 1944 N HIS A 256 4.510 -53.822 17.699 1.00 54.63 N ANISOU 1944 N HIS A 256 6526 7275 6956 67 390 990 N ATOM 1945 CA HIS A 256 3.493 -53.276 18.592 1.00 54.43 C ANISOU 1945 CA HIS A 256 6602 7123 6957 23 211 869 C ATOM 1946 C HIS A 256 2.674 -54.374 19.267 1.00 50.80 C ANISOU 1946 C HIS A 256 6109 6749 6445 45 72 641 C ATOM 1947 O HIS A 256 2.294 -55.344 18.628 1.00 49.91 O ANISOU 1947 O HIS A 256 6006 6763 6196 159 75 554 O ATOM 1948 CB HIS A 256 2.523 -52.368 17.816 1.00 56.30 C ANISOU 1948 CB HIS A 256 7037 7321 7032 191 206 919 C ATOM 1949 CG HIS A 256 3.125 -51.075 17.351 1.00 59.08 C ANISOU 1949 CG HIS A 256 7513 7493 7441 131 316 1169 C ATOM 1950 CD2 HIS A 256 2.543 -49.944 16.880 1.00 60.46 C ANISOU 1950 CD2 HIS A 256 7925 7512 7536 248 299 1283 C ATOM 1951 ND1 HIS A 256 4.484 -50.840 17.339 1.00 60.33 N ANISOU 1951 ND1 HIS A 256 7555 7602 7767 -85 457 1354 N ATOM 1952 CE1 HIS A 256 4.714 -49.620 16.883 1.00 62.01 C ANISOU 1952 CE1 HIS A 256 7939 7618 8006 -156 537 1581 C ATOM 1953 NE2 HIS A 256 3.554 -49.053 16.602 1.00 62.37 N ANISOU 1953 NE2 HIS A 256 8235 7566 7895 62 437 1547 N ATOM 1954 N ILE A 257 2.395 -54.206 20.557 1.00 37.63 N ANISOU 1954 N ILE A 257 4429 5001 4868 -81 -46 545 N ATOM 1955 CA ILE A 257 1.413 -55.042 21.246 1.00 35.52 C ANISOU 1955 CA ILE A 257 4150 4818 4527 -94 -146 366 C ATOM 1956 C ILE A 257 0.209 -54.207 21.702 1.00 36.27 C ANISOU 1956 C ILE A 257 4299 4921 4563 -37 -199 268 C ATOM 1957 O ILE A 257 0.380 -53.151 22.338 1.00 37.79 O ANISOU 1957 O ILE A 257 4565 4969 4825 -67 -219 283 O ATOM 1958 CB ILE A 257 2.017 -55.842 22.431 1.00 34.09 C ANISOU 1958 CB ILE A 257 3916 4603 4435 -254 -217 333 C ATOM 1959 CG1 ILE A 257 0.946 -56.740 23.051 1.00 33.48 C ANISOU 1959 CG1 ILE A 257 3857 4607 4257 -306 -279 195 C ATOM 1960 CG2 ILE A 257 2.605 -54.924 23.497 1.00 34.58 C ANISOU 1960 CG2 ILE A 257 3990 4540 4609 -386 -282 362 C ATOM 1961 CD1 ILE A 257 1.468 -57.746 24.047 1.00 33.16 C ANISOU 1961 CD1 ILE A 257 3831 4518 4250 -436 -351 201 C ATOM 1962 N LEU A 258 -0.994 -54.681 21.356 1.00 32.63 N ANISOU 1962 N LEU A 258 3791 4629 3976 54 -231 155 N ATOM 1963 CA LEU A 258 -2.259 -53.999 21.665 1.00 33.22 C ANISOU 1963 CA LEU A 258 3838 4798 3988 174 -267 48 C ATOM 1964 C LEU A 258 -3.123 -54.757 22.680 1.00 32.50 C ANISOU 1964 C LEU A 258 3617 4871 3860 47 -282 -98 C ATOM 1965 O LEU A 258 -3.503 -55.924 22.476 1.00 31.59 O ANISOU 1965 O LEU A 258 3413 4883 3707 -67 -306 -147 O ATOM 1966 CB LEU A 258 -3.084 -53.745 20.392 1.00 33.57 C ANISOU 1966 CB LEU A 258 3867 4976 3912 403 -307 48 C ATOM 1967 CG LEU A 258 -2.900 -52.451 19.576 1.00 35.70 C ANISOU 1967 CG LEU A 258 4304 5106 4154 622 -295 191 C ATOM 1968 CD1 LEU A 258 -1.469 -52.291 19.085 1.00 36.89 C ANISOU 1968 CD1 LEU A 258 4580 5071 4366 523 -193 388 C ATOM 1969 CD2 LEU A 258 -3.877 -52.380 18.393 1.00 35.78 C ANISOU 1969 CD2 LEU A 258 4296 5308 3992 877 -385 177 C ATOM 1970 N LEU A 259 -3.430 -54.088 23.781 1.00 29.28 N ANISOU 1970 N LEU A 259 3226 4450 3451 55 -259 -166 N ATOM 1971 CA LEU A 259 -4.418 -54.609 24.700 1.00 29.66 C ANISOU 1971 CA LEU A 259 3135 4714 3420 -32 -218 -287 C ATOM 1972 C LEU A 259 -5.729 -53.952 24.347 1.00 30.73 C ANISOU 1972 C LEU A 259 3112 5066 3497 211 -209 -391 C ATOM 1973 O LEU A 259 -5.816 -52.731 24.351 1.00 32.22 O ANISOU 1973 O LEU A 259 3400 5155 3688 456 -212 -414 O ATOM 1974 CB LEU A 259 -4.055 -54.275 26.144 1.00 30.79 C ANISOU 1974 CB LEU A 259 3393 4774 3532 -120 -181 -325 C ATOM 1975 CG LEU A 259 -5.135 -54.618 27.178 1.00 32.12 C ANISOU 1975 CG LEU A 259 3433 5205 3566 -180 -76 -436 C ATOM 1976 CD1 LEU A 259 -5.489 -56.095 27.125 1.00 31.08 C ANISOU 1976 CD1 LEU A 259 3170 5221 3418 -441 -56 -387 C ATOM 1977 CD2 LEU A 259 -4.722 -54.203 28.598 1.00 33.19 C ANISOU 1977 CD2 LEU A 259 3751 5260 3600 -227 -45 -486 C ATOM 1978 N PHE A 260 -6.753 -54.742 24.040 1.00 43.37 N ANISOU 1978 N PHE A 260 4467 6956 5058 150 -218 -458 N ATOM 1979 CA PHE A 260 -8.048 -54.157 23.753 1.00 44.10 C ANISOU 1979 CA PHE A 260 4323 7328 5106 401 -229 -565 C ATOM 1980 C PHE A 260 -8.825 -54.091 25.050 1.00 45.64 C ANISOU 1980 C PHE A 260 4348 7749 5243 368 -78 -675 C ATOM 1981 O PHE A 260 -9.294 -55.110 25.564 1.00 45.56 O ANISOU 1981 O PHE A 260 4153 7948 5208 78 -3 -690 O ATOM 1982 CB PHE A 260 -8.791 -55.013 22.736 1.00 43.21 C ANISOU 1982 CB PHE A 260 3978 7458 4982 328 -345 -597 C ATOM 1983 CG PHE A 260 -8.174 -54.981 21.376 1.00 42.48 C ANISOU 1983 CG PHE A 260 4065 7203 4871 438 -479 -513 C ATOM 1984 CD1 PHE A 260 -8.393 -53.904 20.532 1.00 43.24 C ANISOU 1984 CD1 PHE A 260 4220 7292 4917 804 -563 -479 C ATOM 1985 CD2 PHE A 260 -7.361 -56.009 20.943 1.00 41.70 C ANISOU 1985 CD2 PHE A 260 4110 6952 4781 210 -509 -460 C ATOM 1986 CE1 PHE A 260 -7.821 -53.854 19.267 1.00 43.15 C ANISOU 1986 CE1 PHE A 260 4406 7157 4834 908 -654 -373 C ATOM 1987 CE2 PHE A 260 -6.779 -55.969 19.679 1.00 41.71 C ANISOU 1987 CE2 PHE A 260 4284 6845 4719 343 -589 -391 C ATOM 1988 CZ PHE A 260 -7.011 -54.887 18.842 1.00 42.50 C ANISOU 1988 CZ PHE A 260 4439 6970 4739 675 -650 -337 C ATOM 1989 N LEU A 261 -8.962 -52.875 25.575 1.00 45.98 N ANISOU 1989 N LEU A 261 4484 7735 5250 668 -21 -750 N ATOM 1990 CA LEU A 261 -9.578 -52.691 26.885 1.00 47.47 C ANISOU 1990 CA LEU A 261 4574 8130 5334 694 159 -876 C ATOM 1991 C LEU A 261 -10.827 -51.805 26.887 1.00 48.27 C ANISOU 1991 C LEU A 261 4423 8526 5390 1116 220 -1032 C ATOM 1992 O LEU A 261 -10.748 -50.574 26.770 1.00 49.12 O ANISOU 1992 O LEU A 261 4735 8427 5501 1504 171 -1092 O ATOM 1993 CB LEU A 261 -8.547 -52.195 27.908 1.00 48.62 C ANISOU 1993 CB LEU A 261 5098 7952 5425 647 194 -881 C ATOM 1994 CG LEU A 261 -8.868 -52.471 29.381 1.00 49.42 C ANISOU 1994 CG LEU A 261 5183 8250 5346 527 384 -969 C ATOM 1995 CD1 LEU A 261 -9.032 -53.969 29.593 1.00 48.71 C ANISOU 1995 CD1 LEU A 261 4913 8364 5231 108 453 -851 C ATOM 1996 CD2 LEU A 261 -7.787 -51.890 30.293 1.00 50.13 C ANISOU 1996 CD2 LEU A 261 5685 8000 5361 506 339 -1000 C ATOM 1997 N PRO A 262 -11.994 -52.436 27.057 1.00 60.08 N ANISOU 1997 N PRO A 262 5466 10506 6855 1039 328 -1096 N ATOM 1998 CA PRO A 262 -13.218 -51.633 27.158 1.00 61.63 C ANISOU 1998 CA PRO A 262 5339 11065 7013 1479 409 -1257 C ATOM 1999 C PRO A 262 -13.162 -50.791 28.437 1.00 63.34 C ANISOU 1999 C PRO A 262 5766 11217 7082 1716 613 -1399 C ATOM 2000 O PRO A 262 -12.900 -51.322 29.518 1.00 63.62 O ANISOU 2000 O PRO A 262 5884 11299 6991 1422 793 -1395 O ATOM 2001 CB PRO A 262 -14.337 -52.691 27.229 1.00 62.08 C ANISOU 2001 CB PRO A 262 4824 11684 7081 1200 515 -1272 C ATOM 2002 CG PRO A 262 -13.667 -53.948 27.733 1.00 61.15 C ANISOU 2002 CG PRO A 262 4855 11436 6944 605 583 -1136 C ATOM 2003 CD PRO A 262 -12.216 -53.875 27.308 1.00 59.59 C ANISOU 2003 CD PRO A 262 5180 10667 6793 541 402 -1022 C ATOM 2004 N LYS A 263 -13.420 -49.495 28.312 1.00 68.00 N ANISOU 2004 N LYS A 263 6484 11688 7664 2261 570 -1527 N ATOM 2005 CA LYS A 263 -13.472 -48.620 29.471 1.00 70.06 C ANISOU 2005 CA LYS A 263 6973 11879 7765 2558 745 -1721 C ATOM 2006 C LYS A 263 -14.543 -49.130 30.422 1.00 72.07 C ANISOU 2006 C LYS A 263 6838 12660 7887 2463 1025 -1789 C ATOM 2007 O LYS A 263 -14.553 -48.794 31.601 1.00 74.07 O ANISOU 2007 O LYS A 263 7280 12911 7953 2533 1217 -1908 O ATOM 2008 CB LYS A 263 -13.832 -47.195 29.044 1.00 71.77 C ANISOU 2008 CB LYS A 263 7371 11874 8026 3180 626 -1834 C ATOM 2009 CG LYS A 263 -12.720 -46.431 28.362 1.00 71.22 C ANISOU 2009 CG LYS A 263 7840 11155 8065 3257 381 -1741 C ATOM 2010 CD LYS A 263 -11.659 -46.030 29.355 1.00 71.91 C ANISOU 2010 CD LYS A 263 8452 10796 8072 3085 405 -1811 C ATOM 2011 CE LYS A 263 -10.692 -45.055 28.736 1.00 72.30 C ANISOU 2011 CE LYS A 263 9027 10186 8258 3162 171 -1720 C ATOM 2012 NZ LYS A 263 -11.416 -43.891 28.164 1.00 74.12 N1+ ANISOU 2012 NZ LYS A 263 9351 10283 8526 3785 88 -1799 N1+ ATOM 2013 N SER A 264 -15.451 -49.939 29.886 1.00 57.12 N ANISOU 2013 N SER A 264 4459 11147 6096 2247 1013 -1681 N ATOM 2014 CA SER A 264 -16.613 -50.419 30.627 1.00 61.59 C ANISOU 2014 CA SER A 264 4642 12166 6596 2108 1246 -1686 C ATOM 2015 C SER A 264 -16.374 -51.753 31.324 1.00 60.27 C ANISOU 2015 C SER A 264 4401 12151 6347 1500 1424 -1554 C ATOM 2016 O SER A 264 -17.289 -52.313 31.918 1.00 64.13 O ANISOU 2016 O SER A 264 4584 12990 6791 1299 1628 -1511 O ATOM 2017 CB SER A 264 -17.807 -50.564 29.683 1.00 64.77 C ANISOU 2017 CB SER A 264 4576 12879 7157 2179 1114 -1651 C ATOM 2018 OG SER A 264 -17.535 -51.527 28.671 1.00 61.56 O ANISOU 2018 OG SER A 264 4057 12449 6886 1796 907 -1515 O ATOM 2019 N VAL A 265 -15.153 -52.267 31.242 1.00 60.89 N ANISOU 2019 N VAL A 265 4771 11955 6409 1206 1348 -1472 N ATOM 2020 CA VAL A 265 -14.853 -53.570 31.820 1.00 60.15 C ANISOU 2020 CA VAL A 265 4681 11929 6242 620 1472 -1307 C ATOM 2021 C VAL A 265 -14.791 -53.500 33.345 1.00 62.35 C ANISOU 2021 C VAL A 265 5181 12272 6238 583 1753 -1333 C ATOM 2022 O VAL A 265 -14.592 -52.429 33.913 1.00 63.42 O ANISOU 2022 O VAL A 265 5581 12291 6224 988 1807 -1509 O ATOM 2023 CB VAL A 265 -13.522 -54.157 31.268 1.00 57.47 C ANISOU 2023 CB VAL A 265 4669 11180 5987 315 1255 -1175 C ATOM 2024 CG1 VAL A 265 -12.332 -53.274 31.647 1.00 57.08 C ANISOU 2024 CG1 VAL A 265 5191 10633 5865 532 1141 -1224 C ATOM 2025 CG2 VAL A 265 -13.316 -55.563 31.783 1.00 57.38 C ANISOU 2025 CG2 VAL A 265 4683 11197 5922 -275 1346 -979 C ATOM 2026 N SER A 266 -14.978 -54.651 33.990 1.00 62.68 N ANISOU 2026 N SER A 266 5162 12455 6199 98 1910 -1152 N ATOM 2027 CA SER A 266 -14.752 -54.806 35.426 1.00 64.59 C ANISOU 2027 CA SER A 266 5689 12721 6133 -16 2152 -1112 C ATOM 2028 C SER A 266 -13.258 -54.913 35.670 1.00 61.94 C ANISOU 2028 C SER A 266 5863 12019 5651 -153 2016 -1075 C ATOM 2029 O SER A 266 -12.562 -55.604 34.935 1.00 60.01 O ANISOU 2029 O SER A 266 5687 11541 5574 -444 1807 -934 O ATOM 2030 CB SER A 266 -15.415 -56.087 35.942 1.00 67.36 C ANISOU 2030 CB SER A 266 5846 13286 6461 -513 2336 -879 C ATOM 2031 OG SER A 266 -16.661 -56.332 35.307 1.00 70.76 O ANISOU 2031 OG SER A 266 5756 14012 7119 -552 2353 -871 O ATOM 2032 N ASP A 267 -12.775 -54.245 36.712 1.00 72.33 N ANISOU 2032 N ASP A 267 7577 13234 6673 56 2090 -1196 N ATOM 2033 CA ASP A 267 -11.355 -54.261 37.058 1.00 71.30 C ANISOU 2033 CA ASP A 267 7985 12680 6425 -61 1868 -1159 C ATOM 2034 C ASP A 267 -10.484 -53.725 35.926 1.00 69.01 C ANISOU 2034 C ASP A 267 7842 11905 6475 73 1487 -1188 C ATOM 2035 O ASP A 267 -9.477 -54.328 35.565 1.00 67.77 O ANISOU 2035 O ASP A 267 7881 11407 6461 -196 1246 -1015 O ATOM 2036 CB ASP A 267 -10.895 -55.664 37.454 1.00 71.22 C ANISOU 2036 CB ASP A 267 8106 12614 6342 -594 1863 -854 C ATOM 2037 CG ASP A 267 -9.443 -55.691 37.919 1.00 71.05 C ANISOU 2037 CG ASP A 267 8629 12135 6233 -670 1574 -791 C ATOM 2038 OD1 ASP A 267 -9.094 -54.895 38.825 1.00 72.35 O ANISOU 2038 OD1 ASP A 267 9120 12252 6116 -445 1571 -963 O ATOM 2039 OD2 ASP A 267 -8.649 -56.494 37.362 1.00 69.78 O1- ANISOU 2039 OD2 ASP A 267 8559 11668 6285 -935 1333 -590 O1- ATOM 2040 N TYR A 268 -10.891 -52.590 35.373 1.00 49.44 N ANISOU 2040 N TYR A 268 5267 9408 4110 512 1453 -1396 N ATOM 2041 CA TYR A 268 -10.143 -51.911 34.330 1.00 47.70 C ANISOU 2041 CA TYR A 268 5215 8739 4170 670 1138 -1412 C ATOM 2042 C TYR A 268 -8.681 -51.668 34.740 1.00 47.71 C ANISOU 2042 C TYR A 268 5722 8258 4148 542 897 -1387 C ATOM 2043 O TYR A 268 -7.755 -52.087 34.026 1.00 46.28 O ANISOU 2043 O TYR A 268 5614 7784 4187 319 671 -1216 O ATOM 2044 CB TYR A 268 -10.858 -50.600 33.975 1.00 48.77 C ANISOU 2044 CB TYR A 268 5275 8910 4347 1218 1166 -1646 C ATOM 2045 CG TYR A 268 -10.230 -49.770 32.878 1.00 47.44 C ANISOU 2045 CG TYR A 268 5301 8281 4441 1411 876 -1638 C ATOM 2046 CD1 TYR A 268 -10.465 -50.052 31.531 1.00 45.99 C ANISOU 2046 CD1 TYR A 268 4847 8123 4504 1400 754 -1501 C ATOM 2047 CD2 TYR A 268 -9.430 -48.679 33.189 1.00 48.43 C ANISOU 2047 CD2 TYR A 268 5905 7948 4549 1592 724 -1767 C ATOM 2048 CE1 TYR A 268 -9.907 -49.274 30.524 1.00 45.67 C ANISOU 2048 CE1 TYR A 268 5015 7681 4656 1579 523 -1458 C ATOM 2049 CE2 TYR A 268 -8.857 -47.896 32.186 1.00 48.12 C ANISOU 2049 CE2 TYR A 268 6062 7472 4749 1723 487 -1718 C ATOM 2050 CZ TYR A 268 -9.101 -48.199 30.860 1.00 46.84 C ANISOU 2050 CZ TYR A 268 5631 7365 4800 1725 407 -1547 C ATOM 2051 OH TYR A 268 -8.533 -47.422 29.878 1.00 46.94 O ANISOU 2051 OH TYR A 268 5869 6962 5002 1849 206 -1461 O ATOM 2052 N ASP A 269 -8.475 -51.021 35.891 1.00 77.40 N ANISOU 2052 N ASP A 269 9810 11968 7632 683 940 -1569 N ATOM 2053 CA ASP A 269 -7.122 -50.645 36.332 1.00 77.74 C ANISOU 2053 CA ASP A 269 10310 11575 7653 571 664 -1591 C ATOM 2054 C ASP A 269 -6.225 -51.804 36.781 1.00 77.18 C ANISOU 2054 C ASP A 269 10343 11463 7519 147 551 -1360 C ATOM 2055 O ASP A 269 -4.996 -51.694 36.718 1.00 76.65 O ANISOU 2055 O ASP A 269 10505 11047 7571 7 261 -1306 O ATOM 2056 CB ASP A 269 -7.155 -49.555 37.416 1.00 80.10 C ANISOU 2056 CB ASP A 269 10981 11798 7654 859 688 -1901 C ATOM 2057 CG ASP A 269 -7.391 -48.159 36.841 1.00 80.80 C ANISOU 2057 CG ASP A 269 11185 11611 7906 1276 611 -2123 C ATOM 2058 OD1 ASP A 269 -7.695 -47.229 37.625 1.00 82.87 O ANISOU 2058 OD1 ASP A 269 11729 11829 7928 1603 673 -2424 O ATOM 2059 OD2 ASP A 269 -7.279 -47.989 35.604 1.00 79.55 O1- ANISOU 2059 OD2 ASP A 269 10875 11261 8090 1297 489 -1997 O1- ATOM 2060 N GLY A 270 -6.827 -52.898 37.249 1.00 46.40 N ANISOU 2060 N GLY A 270 6275 7916 3438 -56 772 -1214 N ATOM 2061 CA GLY A 270 -6.061 -54.083 37.595 1.00 45.85 C ANISOU 2061 CA GLY A 270 6324 7777 3321 -424 660 -961 C ATOM 2062 C GLY A 270 -5.461 -54.762 36.371 1.00 43.62 C ANISOU 2062 C GLY A 270 5883 7267 3423 -604 468 -759 C ATOM 2063 O GLY A 270 -4.247 -54.995 36.304 1.00 42.76 O ANISOU 2063 O GLY A 270 5954 6871 3422 -725 203 -656 O ATOM 2064 N LYS A 271 -6.316 -55.064 35.395 1.00 55.07 N ANISOU 2064 N LYS A 271 6982 8874 5067 -600 596 -720 N ATOM 2065 CA LYS A 271 -5.894 -55.736 34.177 1.00 53.22 C ANISOU 2065 CA LYS A 271 6612 8462 5147 -739 444 -564 C ATOM 2066 C LYS A 271 -4.908 -54.831 33.458 1.00 52.17 C ANISOU 2066 C LYS A 271 6599 7990 5233 -572 209 -621 C ATOM 2067 O LYS A 271 -3.845 -55.279 32.972 1.00 50.70 O ANISOU 2067 O LYS A 271 6483 7563 5218 -697 20 -485 O ATOM 2068 CB LYS A 271 -7.112 -56.039 33.298 1.00 53.08 C ANISOU 2068 CB LYS A 271 6204 8712 5253 -734 596 -573 C ATOM 2069 CG LYS A 271 -8.195 -56.826 34.023 1.00 54.49 C ANISOU 2069 CG LYS A 271 6195 9273 5235 -944 867 -516 C ATOM 2070 CD LYS A 271 -9.479 -57.014 33.206 1.00 54.37 C ANISOU 2070 CD LYS A 271 5714 9587 5356 -950 994 -557 C ATOM 2071 CE LYS A 271 -10.590 -57.607 34.088 1.00 56.03 C ANISOU 2071 CE LYS A 271 5689 10241 5360 -1173 1319 -507 C ATOM 2072 NZ LYS A 271 -11.937 -57.614 33.447 1.00 56.25 N1+ ANISOU 2072 NZ LYS A 271 5171 10688 5511 -1153 1452 -584 N1+ ATOM 2073 N LEU A 272 -5.262 -53.550 33.410 1.00 55.46 N ANISOU 2073 N LEU A 272 7044 8387 5641 -282 236 -815 N ATOM 2074 CA LEU A 272 -4.361 -52.531 32.890 1.00 55.31 C ANISOU 2074 CA LEU A 272 7198 8012 5804 -159 33 -861 C ATOM 2075 C LEU A 272 -2.993 -52.592 33.577 1.00 55.46 C ANISOU 2075 C LEU A 272 7479 7789 5804 -347 -182 -812 C ATOM 2076 O LEU A 272 -1.941 -52.458 32.936 1.00 54.56 O ANISOU 2076 O LEU A 272 7388 7423 5919 -430 -363 -714 O ATOM 2077 CB LEU A 272 -4.966 -51.149 33.083 1.00 56.80 C ANISOU 2077 CB LEU A 272 7494 8163 5925 181 88 -1095 C ATOM 2078 CG LEU A 272 -4.165 -50.030 32.431 1.00 57.04 C ANISOU 2078 CG LEU A 272 7726 7777 6168 283 -108 -1117 C ATOM 2079 CD1 LEU A 272 -4.019 -50.308 30.957 1.00 55.84 C ANISOU 2079 CD1 LEU A 272 7377 7569 6272 258 -147 -927 C ATOM 2080 CD2 LEU A 272 -4.800 -48.669 32.668 1.00 58.93 C ANISOU 2080 CD2 LEU A 272 8151 7906 6335 652 -70 -1358 C ATOM 2081 N SER A 273 -3.002 -52.808 34.882 1.00 58.12 N ANISOU 2081 N SER A 273 7993 8239 5852 -414 -160 -872 N ATOM 2082 CA SER A 273 -1.750 -52.908 35.612 1.00 58.19 C ANISOU 2082 CA SER A 273 8234 8067 5808 -579 -412 -833 C ATOM 2083 C SER A 273 -0.961 -54.169 35.264 1.00 55.92 C ANISOU 2083 C SER A 273 7839 7748 5659 -798 -525 -574 C ATOM 2084 O SER A 273 0.267 -54.136 35.261 1.00 54.84 O ANISOU 2084 O SER A 273 7757 7422 5656 -890 -775 -511 O ATOM 2085 CB SER A 273 -1.983 -52.806 37.118 1.00 60.27 C ANISOU 2085 CB SER A 273 8765 8477 5657 -562 -379 -968 C ATOM 2086 OG SER A 273 -2.290 -51.471 37.481 1.00 61.79 O ANISOU 2086 OG SER A 273 9153 8579 5746 -332 -372 -1256 O ATOM 2087 N ASN A 274 -1.651 -55.274 34.991 1.00 47.29 N ANISOU 2087 N ASN A 274 6591 6836 4542 -878 -353 -433 N ATOM 2088 CA ASN A 274 -0.961 -56.486 34.563 1.00 45.60 C ANISOU 2088 CA ASN A 274 6321 6534 4472 -1034 -459 -210 C ATOM 2089 C ASN A 274 -0.194 -56.215 33.283 1.00 43.50 C ANISOU 2089 C ASN A 274 5903 6076 4548 -978 -573 -173 C ATOM 2090 O ASN A 274 0.987 -56.570 33.155 1.00 42.31 O ANISOU 2090 O ASN A 274 5757 5785 4534 -1028 -762 -63 O ATOM 2091 CB ASN A 274 -1.952 -57.628 34.357 1.00 46.07 C ANISOU 2091 CB ASN A 274 6266 6761 4477 -1156 -257 -95 C ATOM 2092 CG ASN A 274 -2.629 -58.045 35.645 1.00 48.20 C ANISOU 2092 CG ASN A 274 6682 7240 4392 -1268 -105 -63 C ATOM 2093 ND2 ASN A 274 -3.468 -59.084 35.582 1.00 48.83 N ANISOU 2093 ND2 ASN A 274 6673 7455 4426 -1456 75 69 N ATOM 2094 OD1 ASN A 274 -2.398 -57.438 36.691 1.00 49.37 O ANISOU 2094 OD1 ASN A 274 7038 7427 4292 -1205 -147 -155 O ATOM 2095 N PHE A 275 -0.870 -55.554 32.347 1.00 36.50 N ANISOU 2095 N PHE A 275 4873 5213 3780 -850 -451 -258 N ATOM 2096 CA PHE A 275 -0.218 -55.090 31.120 1.00 35.13 C ANISOU 2096 CA PHE A 275 4597 4875 3878 -781 -519 -216 C ATOM 2097 C PHE A 275 1.025 -54.243 31.430 1.00 35.08 C ANISOU 2097 C PHE A 275 4693 4662 3974 -819 -714 -228 C ATOM 2098 O PHE A 275 2.134 -54.499 30.920 1.00 33.67 O ANISOU 2098 O PHE A 275 4421 4385 3988 -885 -824 -103 O ATOM 2099 CB PHE A 275 -1.193 -54.257 30.309 1.00 36.02 C ANISOU 2099 CB PHE A 275 4621 5035 4028 -598 -389 -314 C ATOM 2100 CG PHE A 275 -0.885 -54.211 28.837 1.00 34.72 C ANISOU 2100 CG PHE A 275 4338 4787 4068 -533 -393 -217 C ATOM 2101 CD1 PHE A 275 -0.681 -55.385 28.116 1.00 32.91 C ANISOU 2101 CD1 PHE A 275 3999 4603 3902 -603 -385 -104 C ATOM 2102 CD2 PHE A 275 -0.857 -52.998 28.156 1.00 35.54 C ANISOU 2102 CD2 PHE A 275 4484 4753 4268 -384 -396 -241 C ATOM 2103 CE1 PHE A 275 -0.436 -55.352 26.738 1.00 31.98 C ANISOU 2103 CE1 PHE A 275 3801 4442 3906 -513 -367 -34 C ATOM 2104 CE2 PHE A 275 -0.599 -52.953 26.784 1.00 35.01 C ANISOU 2104 CE2 PHE A 275 4339 4634 4327 -318 -375 -124 C ATOM 2105 CZ PHE A 275 -0.389 -54.139 26.073 1.00 33.05 C ANISOU 2105 CZ PHE A 275 3967 4483 4107 -376 -353 -30 C ATOM 2106 N LYS A 276 0.827 -53.228 32.269 1.00 40.09 N ANISOU 2106 N LYS A 276 5508 5244 4481 -779 -755 -395 N ATOM 2107 CA LYS A 276 1.918 -52.351 32.685 1.00 40.56 C ANISOU 2107 CA LYS A 276 5694 5089 4629 -870 -979 -447 C ATOM 2108 C LYS A 276 3.121 -53.145 33.222 1.00 39.45 C ANISOU 2108 C LYS A 276 5511 4963 4516 -1040 -1196 -327 C ATOM 2109 O LYS A 276 4.287 -52.789 32.980 1.00 39.04 O ANISOU 2109 O LYS A 276 5369 4783 4683 -1155 -1376 -268 O ATOM 2110 CB LYS A 276 1.427 -51.349 33.740 1.00 42.92 C ANISOU 2110 CB LYS A 276 6271 5332 4703 -792 -1012 -694 C ATOM 2111 CG LYS A 276 2.483 -50.347 34.190 1.00 43.97 C ANISOU 2111 CG LYS A 276 6582 5196 4928 -926 -1285 -794 C ATOM 2112 CD LYS A 276 2.830 -49.365 33.065 1.00 44.53 C ANISOU 2112 CD LYS A 276 6613 4993 5314 -941 -1288 -745 C ATOM 2113 CE LYS A 276 4.153 -48.652 33.333 1.00 45.27 C ANISOU 2113 CE LYS A 276 6772 4832 5594 -1208 -1580 -758 C ATOM 2114 NZ LYS A 276 5.317 -49.591 33.308 1.00 43.55 N1+ ANISOU 2114 NZ LYS A 276 6269 4763 5514 -1410 -1724 -566 N1+ ATOM 2115 N THR A 277 2.845 -54.219 33.953 1.00 37.31 N ANISOU 2115 N THR A 277 5292 4857 4028 -1055 -1183 -272 N ATOM 2116 CA THR A 277 3.919 -54.988 34.567 1.00 37.01 C ANISOU 2116 CA THR A 277 5255 4831 3975 -1152 -1421 -152 C ATOM 2117 C THR A 277 4.689 -55.690 33.460 1.00 35.47 C ANISOU 2117 C THR A 277 4794 4604 4078 -1141 -1426 32 C ATOM 2118 O THR A 277 5.922 -55.735 33.480 1.00 35.42 O ANISOU 2118 O THR A 277 4655 4565 4238 -1190 -1640 106 O ATOM 2119 CB THR A 277 3.372 -55.994 35.599 1.00 37.92 C ANISOU 2119 CB THR A 277 5557 5095 3754 -1161 -1388 -96 C ATOM 2120 CG2 THR A 277 4.479 -56.751 36.297 1.00 38.15 C ANISOU 2120 CG2 THR A 277 5638 5121 3737 -1208 -1679 41 C ATOM 2121 OG1 THR A 277 2.623 -55.291 36.587 1.00 39.70 O ANISOU 2121 OG1 THR A 277 6020 5399 3665 -1138 -1327 -283 O ATOM 2122 N ALA A 278 3.962 -56.217 32.478 1.00 35.65 N ANISOU 2122 N ALA A 278 4722 4661 4163 -1063 -1195 88 N ATOM 2123 CA ALA A 278 4.638 -56.905 31.382 1.00 34.45 C ANISOU 2123 CA ALA A 278 4363 4483 4245 -1007 -1174 228 C ATOM 2124 C ALA A 278 5.455 -55.953 30.488 1.00 33.89 C ANISOU 2124 C ALA A 278 4099 4342 4434 -1016 -1179 245 C ATOM 2125 O ALA A 278 6.488 -56.335 29.948 1.00 33.73 O ANISOU 2125 O ALA A 278 3876 4337 4603 -991 -1225 360 O ATOM 2126 CB ALA A 278 3.659 -57.737 30.571 1.00 33.95 C ANISOU 2126 CB ALA A 278 4289 4461 4149 -941 -965 254 C ATOM 2127 N ALA A 279 5.006 -54.711 30.341 1.00 44.36 N ANISOU 2127 N ALA A 279 5496 5590 5771 -1044 -1120 142 N ATOM 2128 CA ALA A 279 5.755 -53.715 29.555 1.00 44.79 C ANISOU 2128 CA ALA A 279 5425 5531 6062 -1109 -1118 193 C ATOM 2129 C ALA A 279 7.209 -53.465 30.021 1.00 45.44 C ANISOU 2129 C ALA A 279 5354 5589 6322 -1285 -1352 248 C ATOM 2130 O ALA A 279 8.053 -53.065 29.216 1.00 45.74 O ANISOU 2130 O ALA A 279 5176 5606 6598 -1366 -1313 366 O ATOM 2131 CB ALA A 279 4.997 -52.410 29.498 1.00 46.48 C ANISOU 2131 CB ALA A 279 5830 5593 6238 -1097 -1058 72 C ATOM 2132 N GLU A 280 7.495 -53.705 31.304 1.00 52.58 N ANISOU 2132 N GLU A 280 6352 6527 7097 -1352 -1595 173 N ATOM 2133 CA GLU A 280 8.826 -53.460 31.881 1.00 53.71 C ANISOU 2133 CA GLU A 280 6333 6684 7391 -1526 -1891 196 C ATOM 2134 C GLU A 280 9.978 -54.250 31.239 1.00 53.38 C ANISOU 2134 C GLU A 280 5897 6799 7588 -1481 -1906 386 C ATOM 2135 O GLU A 280 11.108 -53.773 31.189 1.00 54.42 O ANISOU 2135 O GLU A 280 5770 6967 7942 -1626 -2025 432 O ATOM 2136 CB GLU A 280 8.814 -53.716 33.390 1.00 54.83 C ANISOU 2136 CB GLU A 280 6693 6870 7269 -1551 -2169 82 C ATOM 2137 CG GLU A 280 7.856 -52.816 34.170 1.00 56.17 C ANISOU 2137 CG GLU A 280 7243 6915 7182 -1580 -2170 -144 C ATOM 2138 CD GLU A 280 8.227 -52.671 35.656 1.00 58.09 C ANISOU 2138 CD GLU A 280 7694 7190 7188 -1637 -2465 -282 C ATOM 2139 OE1 GLU A 280 9.313 -52.097 35.966 1.00 59.35 O ANISOU 2139 OE1 GLU A 280 7731 7315 7505 -1753 -2650 -314 O ATOM 2140 OE2 GLU A 280 7.424 -53.121 36.519 1.00 58.72 O1- ANISOU 2140 OE2 GLU A 280 8055 7355 6900 -1547 -2457 -353 O1- ATOM 2141 N SER A 281 9.691 -55.449 30.752 1.00 46.69 N ANISOU 2141 N SER A 281 5016 6044 6682 -1255 -1751 475 N ATOM 2142 CA SER A 281 10.725 -56.330 30.218 1.00 47.16 C ANISOU 2142 CA SER A 281 4744 6248 6924 -1118 -1758 622 C ATOM 2143 C SER A 281 11.120 -55.956 28.800 1.00 47.03 C ANISOU 2143 C SER A 281 4460 6279 7132 -1108 -1491 721 C ATOM 2144 O SER A 281 12.113 -56.449 28.271 1.00 47.76 O ANISOU 2144 O SER A 281 4211 6532 7402 -1000 -1456 834 O ATOM 2145 CB SER A 281 10.255 -57.785 30.264 1.00 46.97 C ANISOU 2145 CB SER A 281 4873 6236 6737 -868 -1711 660 C ATOM 2146 OG SER A 281 9.595 -58.056 31.502 1.00 47.42 O ANISOU 2146 OG SER A 281 5259 6238 6522 -908 -1871 597 O ATOM 2147 N PHE A 282 10.304 -55.122 28.167 1.00 55.93 N ANISOU 2147 N PHE A 282 5750 7281 8218 -1180 -1286 686 N ATOM 2148 CA PHE A 282 10.576 -54.650 26.819 1.00 56.40 C ANISOU 2148 CA PHE A 282 5635 7369 8425 -1183 -1019 805 C ATOM 2149 C PHE A 282 10.351 -53.151 26.790 1.00 57.60 C ANISOU 2149 C PHE A 282 5920 7329 8638 -1433 -1013 789 C ATOM 2150 O PHE A 282 9.212 -52.681 26.881 1.00 57.45 O ANISOU 2150 O PHE A 282 6226 7151 8454 -1395 -972 682 O ATOM 2151 CB PHE A 282 9.645 -55.380 25.846 1.00 55.14 C ANISOU 2151 CB PHE A 282 5624 7227 8100 -928 -769 799 C ATOM 2152 CG PHE A 282 9.357 -56.796 26.264 1.00 54.36 C ANISOU 2152 CG PHE A 282 5615 7170 7868 -728 -845 742 C ATOM 2153 CD1 PHE A 282 10.089 -57.845 25.750 1.00 54.92 C ANISOU 2153 CD1 PHE A 282 5502 7358 8006 -512 -790 808 C ATOM 2154 CD2 PHE A 282 8.382 -57.068 27.227 1.00 53.75 C ANISOU 2154 CD2 PHE A 282 5824 7004 7594 -756 -966 630 C ATOM 2155 CE1 PHE A 282 9.834 -59.156 26.161 1.00 55.31 C ANISOU 2155 CE1 PHE A 282 5707 7366 7943 -332 -885 767 C ATOM 2156 CE2 PHE A 282 8.120 -58.361 27.644 1.00 53.91 C ANISOU 2156 CE2 PHE A 282 5969 7020 7496 -627 -1032 619 C ATOM 2157 CZ PHE A 282 8.848 -59.415 27.107 1.00 54.99 C ANISOU 2157 CZ PHE A 282 5974 7204 7716 -419 -1009 690 C ATOM 2158 N LYS A 283 11.434 -52.407 26.612 1.00 77.79 N ANISOU 2158 N LYS A 283 8217 9896 11445 -1680 -1046 902 N ATOM 2159 CA LYS A 283 11.380 -50.963 26.679 1.00 79.53 C ANISOU 2159 CA LYS A 283 8598 9859 11761 -1970 -1090 895 C ATOM 2160 C LYS A 283 11.519 -50.436 25.263 1.00 80.70 C ANISOU 2160 C LYS A 283 8669 9988 12005 -2003 -765 1110 C ATOM 2161 O LYS A 283 10.612 -49.790 24.735 1.00 81.36 O ANISOU 2161 O LYS A 283 9073 9866 11972 -1939 -630 1115 O ATOM 2162 CB LYS A 283 12.491 -50.418 27.579 1.00 81.24 C ANISOU 2162 CB LYS A 283 8703 10075 12091 -2192 -1321 815 C ATOM 2163 CG LYS A 283 12.154 -49.089 28.270 1.00 82.88 C ANISOU 2163 CG LYS A 283 9269 9951 12272 -2408 -1483 657 C ATOM 2164 CD LYS A 283 11.143 -49.269 29.416 1.00 82.05 C ANISOU 2164 CD LYS A 283 9520 9743 11911 -2288 -1693 422 C ATOM 2165 CE LYS A 283 10.825 -47.942 30.143 1.00 84.05 C ANISOU 2165 CE LYS A 283 10158 9663 12116 -2445 -1852 223 C ATOM 2166 NZ LYS A 283 10.310 -46.820 29.273 1.00 85.54 N1+ ANISOU 2166 NZ LYS A 283 10582 9518 12399 -2521 -1688 289 N1+ ATOM 2167 N GLY A 284 12.654 -50.714 24.635 1.00 77.35 N ANISOU 2167 N GLY A 284 7857 9802 11731 -2034 -615 1270 N ATOM 2168 CA GLY A 284 12.843 -50.286 23.262 1.00 78.66 C ANISOU 2168 CA GLY A 284 7954 10001 11934 -2057 -267 1498 C ATOM 2169 C GLY A 284 12.556 -51.402 22.284 1.00 77.48 C ANISOU 2169 C GLY A 284 7702 10101 11637 -1701 -3 1573 C ATOM 2170 O GLY A 284 12.681 -51.227 21.069 1.00 78.75 O ANISOU 2170 O GLY A 284 7823 10351 11750 -1647 317 1760 O ATOM 2171 N LYS A 285 12.224 -52.573 22.817 1.00 62.99 N ANISOU 2171 N LYS A 285 5886 8371 9677 -1429 -134 1400 N ATOM 2172 CA LYS A 285 11.944 -53.727 21.973 1.00 61.98 C ANISOU 2172 CA LYS A 285 5756 8426 9369 -1055 71 1386 C ATOM 2173 C LYS A 285 10.539 -53.741 21.373 1.00 61.07 C ANISOU 2173 C LYS A 285 6049 8176 8978 -870 169 1306 C ATOM 2174 O LYS A 285 10.376 -53.971 20.172 1.00 61.76 O ANISOU 2174 O LYS A 285 6175 8370 8923 -683 421 1380 O ATOM 2175 CB LYS A 285 12.215 -55.028 22.729 1.00 60.82 C ANISOU 2175 CB LYS A 285 5492 8398 9219 -849 -116 1259 C ATOM 2176 CG LYS A 285 13.690 -55.262 23.028 1.00 62.42 C ANISOU 2176 CG LYS A 285 5202 8838 9678 -898 -182 1353 C ATOM 2177 CD LYS A 285 13.900 -56.562 23.801 1.00 61.95 C ANISOU 2177 CD LYS A 285 5098 8850 9591 -633 -405 1243 C ATOM 2178 CE LYS A 285 13.205 -56.528 25.159 1.00 60.82 C ANISOU 2178 CE LYS A 285 5267 8496 9346 -755 -748 1103 C ATOM 2179 NZ LYS A 285 13.657 -55.396 26.035 1.00 61.57 N1+ ANISOU 2179 NZ LYS A 285 5264 8535 9595 -1132 -988 1106 N1+ ATOM 2180 N ILE A 286 9.536 -53.509 22.217 1.00 35.39 N ANISOU 2180 N ILE A 286 3082 4729 5636 -908 -35 1147 N ATOM 2181 CA ILE A 286 8.134 -53.639 21.835 1.00 34.69 C ANISOU 2181 CA ILE A 286 3305 4569 5307 -724 6 1039 C ATOM 2182 C ILE A 286 7.333 -52.501 22.447 1.00 35.70 C ANISOU 2182 C ILE A 286 3684 4465 5416 -849 -117 968 C ATOM 2183 O ILE A 286 7.487 -52.186 23.614 1.00 35.43 O ANISOU 2183 O ILE A 286 3674 4328 5461 -1009 -317 876 O ATOM 2184 CB ILE A 286 7.536 -54.983 22.326 1.00 32.46 C ANISOU 2184 CB ILE A 286 3087 4353 4893 -553 -101 867 C ATOM 2185 CG1 ILE A 286 8.353 -56.177 21.825 1.00 32.30 C ANISOU 2185 CG1 ILE A 286 2875 4499 4897 -375 -14 901 C ATOM 2186 CG2 ILE A 286 6.094 -55.129 21.877 1.00 31.85 C ANISOU 2186 CG2 ILE A 286 3251 4252 4598 -412 -65 757 C ATOM 2187 CD1 ILE A 286 7.771 -57.512 22.212 1.00 31.33 C ANISOU 2187 CD1 ILE A 286 2889 4361 4655 -226 -121 755 C ATOM 2188 N LEU A 287 6.475 -51.878 21.655 1.00 51.47 N ANISOU 2188 N LEU A 287 5890 6382 7286 -738 -12 1000 N ATOM 2189 CA LEU A 287 5.650 -50.775 22.150 1.00 53.38 C ANISOU 2189 CA LEU A 287 6391 6389 7501 -766 -117 920 C ATOM 2190 C LEU A 287 4.304 -51.267 22.689 1.00 52.41 C ANISOU 2190 C LEU A 287 6388 6330 7195 -581 -203 700 C ATOM 2191 O LEU A 287 3.515 -51.869 21.942 1.00 52.08 O ANISOU 2191 O LEU A 287 6353 6437 6997 -381 -128 673 O ATOM 2192 CB LEU A 287 5.406 -49.760 21.031 1.00 56.18 C ANISOU 2192 CB LEU A 287 6924 6606 7814 -703 22 1095 C ATOM 2193 CG LEU A 287 4.798 -48.410 21.428 1.00 57.64 C ANISOU 2193 CG LEU A 287 7415 6464 8020 -715 -83 1055 C ATOM 2194 CD1 LEU A 287 5.696 -47.711 22.438 1.00 57.97 C ANISOU 2194 CD1 LEU A 287 7462 6275 8288 -1046 -227 1033 C ATOM 2195 CD2 LEU A 287 4.566 -47.518 20.200 1.00 59.30 C ANISOU 2195 CD2 LEU A 287 7843 6526 8163 -609 51 1279 C ATOM 2196 N PHE A 288 4.036 -51.006 23.968 1.00 40.01 N ANISOU 2196 N PHE A 288 4904 4670 5629 -659 -357 540 N ATOM 2197 CA PHE A 288 2.779 -51.428 24.586 1.00 38.89 C ANISOU 2197 CA PHE A 288 4835 4632 5310 -516 -395 348 C ATOM 2198 C PHE A 288 1.707 -50.343 24.476 1.00 41.36 C ANISOU 2198 C PHE A 288 5343 4828 5543 -336 -385 266 C ATOM 2199 O PHE A 288 1.905 -49.209 24.924 1.00 43.66 O ANISOU 2199 O PHE A 288 5820 4866 5903 -385 -455 235 O ATOM 2200 CB PHE A 288 2.988 -51.815 26.054 1.00 37.25 C ANISOU 2200 CB PHE A 288 4633 4443 5077 -650 -534 220 C ATOM 2201 CG PHE A 288 3.558 -53.199 26.249 1.00 34.32 C ANISOU 2201 CG PHE A 288 4100 4230 4710 -712 -560 268 C ATOM 2202 CD1 PHE A 288 2.873 -54.153 26.995 1.00 33.06 C ANISOU 2202 CD1 PHE A 288 3969 4197 4396 -695 -584 175 C ATOM 2203 CD2 PHE A 288 4.779 -53.542 25.697 1.00 33.53 C ANISOU 2203 CD2 PHE A 288 3825 4148 4767 -774 -550 417 C ATOM 2204 CE1 PHE A 288 3.401 -55.427 27.177 1.00 31.65 C ANISOU 2204 CE1 PHE A 288 3712 4092 4223 -732 -628 237 C ATOM 2205 CE2 PHE A 288 5.310 -54.812 25.875 1.00 31.93 C ANISOU 2205 CE2 PHE A 288 3500 4061 4572 -758 -589 450 C ATOM 2206 CZ PHE A 288 4.622 -55.751 26.613 1.00 31.21 C ANISOU 2206 CZ PHE A 288 3503 4025 4328 -732 -644 363 C ATOM 2207 N ILE A 289 0.571 -50.716 23.891 1.00 32.30 N ANISOU 2207 N ILE A 289 4156 3859 4256 -119 -321 217 N ATOM 2208 CA ILE A 289 -0.519 -49.795 23.590 1.00 33.44 C ANISOU 2208 CA ILE A 289 4428 3956 4320 139 -318 155 C ATOM 2209 C ILE A 289 -1.838 -50.392 24.052 1.00 32.33 C ANISOU 2209 C ILE A 289 4154 4095 4035 279 -308 -31 C ATOM 2210 O ILE A 289 -2.139 -51.548 23.763 1.00 30.28 O ANISOU 2210 O ILE A 289 3712 4074 3720 228 -282 -38 O ATOM 2211 CB ILE A 289 -0.613 -49.535 22.064 1.00 33.55 C ANISOU 2211 CB ILE A 289 4477 3968 4302 299 -261 331 C ATOM 2212 CG1 ILE A 289 0.719 -49.003 21.533 1.00 35.05 C ANISOU 2212 CG1 ILE A 289 4760 3929 4627 117 -209 561 C ATOM 2213 CG2 ILE A 289 -1.738 -48.560 21.744 1.00 34.38 C ANISOU 2213 CG2 ILE A 289 4725 4018 4321 624 -299 284 C ATOM 2214 CD1 ILE A 289 0.840 -49.016 20.042 1.00 35.45 C ANISOU 2214 CD1 ILE A 289 4837 4040 4592 230 -105 768 C ATOM 2215 N PHE A 290 -2.625 -49.614 24.781 1.00 44.32 N ANISOU 2215 N PHE A 290 5761 5585 5495 449 -320 -189 N ATOM 2216 CA PHE A 290 -3.960 -50.060 25.106 1.00 44.12 C ANISOU 2216 CA PHE A 290 5543 5883 5337 602 -270 -346 C ATOM 2217 C PHE A 290 -4.951 -49.136 24.439 1.00 45.01 C ANISOU 2217 C PHE A 290 5674 6014 5411 983 -287 -384 C ATOM 2218 O PHE A 290 -4.630 -47.988 24.103 1.00 46.18 O ANISOU 2218 O PHE A 290 6086 5845 5617 1136 -337 -320 O ATOM 2219 CB PHE A 290 -4.210 -50.113 26.607 1.00 45.49 C ANISOU 2219 CB PHE A 290 5736 6131 5419 538 -228 -521 C ATOM 2220 CG PHE A 290 -4.302 -48.761 27.258 1.00 48.22 C ANISOU 2220 CG PHE A 290 6342 6238 5741 742 -253 -661 C ATOM 2221 CD1 PHE A 290 -3.331 -47.803 27.037 1.00 49.82 C ANISOU 2221 CD1 PHE A 290 6833 6024 6074 695 -358 -585 C ATOM 2222 CD2 PHE A 290 -5.354 -48.448 28.088 1.00 48.58 C ANISOU 2222 CD2 PHE A 290 6353 6470 5635 974 -164 -874 C ATOM 2223 CE1 PHE A 290 -3.409 -46.557 27.639 1.00 51.45 C ANISOU 2223 CE1 PHE A 290 7347 5935 6266 866 -412 -738 C ATOM 2224 CE2 PHE A 290 -5.435 -47.199 28.689 1.00 50.28 C ANISOU 2224 CE2 PHE A 290 6865 6429 5810 1211 -194 -1044 C ATOM 2225 CZ PHE A 290 -4.461 -46.258 28.463 1.00 51.54 C ANISOU 2225 CZ PHE A 290 7370 6106 6108 1151 -337 -984 C ATOM 2226 N ILE A 291 -6.153 -49.661 24.226 1.00 45.95 N ANISOU 2226 N ILE A 291 5511 6504 5443 1125 -262 -473 N ATOM 2227 CA ILE A 291 -7.176 -48.929 23.508 1.00 46.15 C ANISOU 2227 CA ILE A 291 5479 6631 5427 1530 -316 -505 C ATOM 2228 C ILE A 291 -8.571 -49.349 23.942 1.00 45.80 C ANISOU 2228 C ILE A 291 5054 7046 5301 1667 -260 -687 C ATOM 2229 O ILE A 291 -8.796 -50.504 24.313 1.00 44.70 O ANISOU 2229 O ILE A 291 4663 7182 5139 1377 -195 -722 O ATOM 2230 CB ILE A 291 -7.017 -49.128 21.987 1.00 45.03 C ANISOU 2230 CB ILE A 291 5343 6492 5274 1576 -414 -326 C ATOM 2231 CG1 ILE A 291 -8.119 -48.391 21.233 1.00 45.70 C ANISOU 2231 CG1 ILE A 291 5369 6708 5287 2033 -520 -346 C ATOM 2232 CG2 ILE A 291 -7.000 -50.615 21.646 1.00 43.05 C ANISOU 2232 CG2 ILE A 291 4849 6511 4998 1282 -413 -319 C ATOM 2233 CD1 ILE A 291 -8.147 -48.715 19.782 1.00 45.15 C ANISOU 2233 CD1 ILE A 291 5289 6735 5133 2093 -638 -198 C ATOM 2234 N ASP A 292 -9.505 -48.404 23.853 1.00 46.93 N ANISOU 2234 N ASP A 292 5153 7269 5411 2115 -286 -786 N ATOM 2235 CA ASP A 292 -10.864 -48.594 24.347 1.00 47.18 C ANISOU 2235 CA ASP A 292 4769 7779 5378 2308 -204 -971 C ATOM 2236 C ASP A 292 -11.761 -49.160 23.246 1.00 46.27 C ANISOU 2236 C ASP A 292 4267 8055 5260 2386 -335 -942 C ATOM 2237 O ASP A 292 -12.136 -48.467 22.301 1.00 46.86 O ANISOU 2237 O ASP A 292 4379 8104 5322 2768 -498 -894 O ATOM 2238 CB ASP A 292 -11.438 -47.276 24.899 1.00 49.08 C ANISOU 2238 CB ASP A 292 5133 7936 5581 2822 -163 -1133 C ATOM 2239 CG ASP A 292 -12.924 -47.369 25.208 1.00 50.14 C ANISOU 2239 CG ASP A 292 4757 8639 5655 3123 -69 -1315 C ATOM 2240 OD1 ASP A 292 -13.597 -46.316 25.265 1.00 53.56 O ANISOU 2240 OD1 ASP A 292 5232 9053 6064 3638 -85 -1424 O ATOM 2241 OD2 ASP A 292 -13.426 -48.495 25.395 1.00 49.29 O1- ANISOU 2241 OD2 ASP A 292 4216 8976 5534 2806 21 -1332 O1- ATOM 2242 N SER A 293 -12.146 -50.415 23.432 1.00 56.22 N ANISOU 2242 N SER A 293 5171 9672 6520 2018 -281 -975 N ATOM 2243 CA SER A 293 -12.829 -51.152 22.400 1.00 55.83 C ANISOU 2243 CA SER A 293 4787 9953 6475 1955 -447 -962 C ATOM 2244 C SER A 293 -14.329 -50.810 22.402 1.00 58.15 C ANISOU 2244 C SER A 293 4647 10691 6756 2258 -465 -1094 C ATOM 2245 O SER A 293 -15.092 -51.312 21.576 1.00 59.67 O ANISOU 2245 O SER A 293 4617 11105 6948 2165 -617 -1089 O ATOM 2246 CB SER A 293 -12.559 -52.666 22.543 1.00 54.40 C ANISOU 2246 CB SER A 293 4488 9861 6320 1376 -409 -935 C ATOM 2247 OG SER A 293 -12.689 -53.118 23.891 1.00 54.79 O ANISOU 2247 OG SER A 293 4420 10031 6365 1112 -174 -992 O ATOM 2248 N ASP A 294 -14.751 -49.973 23.349 1.00 74.15 N ANISOU 2248 N ASP A 294 6673 12742 8760 2540 -297 -1199 N ATOM 2249 CA ASP A 294 -16.127 -49.461 23.414 1.00 79.10 C ANISOU 2249 CA ASP A 294 7024 13661 9369 2824 -288 -1291 C ATOM 2250 C ASP A 294 -16.337 -48.259 22.497 1.00 81.61 C ANISOU 2250 C ASP A 294 7574 13767 9667 3343 -494 -1248 C ATOM 2251 O ASP A 294 -17.397 -48.105 21.894 1.00 85.75 O ANISOU 2251 O ASP A 294 7846 14548 10187 3525 -619 -1267 O ATOM 2252 CB ASP A 294 -16.517 -49.105 24.854 1.00 81.42 C ANISOU 2252 CB ASP A 294 7240 14082 9613 2915 -4 -1428 C ATOM 2253 CG ASP A 294 -16.559 -50.321 25.780 1.00 80.40 C ANISOU 2253 CG ASP A 294 6860 14223 9467 2385 222 -1436 C ATOM 2254 OD1 ASP A 294 -16.947 -51.423 25.321 1.00 80.33 O ANISOU 2254 OD1 ASP A 294 6566 14439 9516 1985 157 -1372 O ATOM 2255 OD2 ASP A 294 -16.221 -50.155 26.977 1.00 80.22 O1- ANISOU 2255 OD2 ASP A 294 6976 14151 9353 2365 459 -1505 O1- ATOM 2256 N HIS A 295 -15.334 -47.385 22.448 1.00 68.21 N ANISOU 2256 N HIS A 295 6374 11583 7962 3570 -525 -1181 N ATOM 2257 CA HIS A 295 -15.412 -46.147 21.683 1.00 70.95 C ANISOU 2257 CA HIS A 295 7056 11620 8283 4033 -695 -1101 C ATOM 2258 C HIS A 295 -15.397 -46.425 20.179 1.00 70.74 C ANISOU 2258 C HIS A 295 7058 11605 8214 4002 -942 -934 C ATOM 2259 O HIS A 295 -14.483 -47.064 19.651 1.00 66.83 O ANISOU 2259 O HIS A 295 6704 10978 7710 3720 -995 -811 O ATOM 2260 CB HIS A 295 -14.287 -45.194 22.097 1.00 69.56 C ANISOU 2260 CB HIS A 295 7455 10849 8127 4187 -650 -1056 C ATOM 2261 CG HIS A 295 -14.347 -43.854 21.431 1.00 73.21 C ANISOU 2261 CG HIS A 295 8333 10914 8570 4611 -801 -953 C ATOM 2262 CD2 HIS A 295 -13.376 -43.095 20.871 1.00 72.60 C ANISOU 2262 CD2 HIS A 295 8807 10268 8508 4675 -894 -761 C ATOM 2263 ND1 HIS A 295 -15.520 -43.143 21.288 1.00 78.74 N ANISOU 2263 ND1 HIS A 295 8902 11782 9233 5009 -863 -1028 N ATOM 2264 CE1 HIS A 295 -15.270 -42.005 20.667 1.00 81.24 C ANISOU 2264 CE1 HIS A 295 9690 11642 9536 5313 -997 -893 C ATOM 2265 NE2 HIS A 295 -13.975 -41.949 20.404 1.00 77.66 N ANISOU 2265 NE2 HIS A 295 9665 10729 9115 5088 -1009 -719 N ATOM 2266 N THR A 296 -16.430 -45.940 19.498 1.00 77.37 N ANISOU 2266 N THR A 296 7766 12620 9010 4314 -1093 -940 N ATOM 2267 CA THR A 296 -16.694 -46.314 18.112 1.00 78.32 C ANISOU 2267 CA THR A 296 7833 12871 9055 4286 -1332 -832 C ATOM 2268 C THR A 296 -15.575 -45.860 17.203 1.00 76.23 C ANISOU 2268 C THR A 296 8113 12142 8709 4339 -1433 -603 C ATOM 2269 O THR A 296 -15.378 -46.416 16.123 1.00 75.53 O ANISOU 2269 O THR A 296 8062 12113 8522 4197 -1580 -500 O ATOM 2270 CB THR A 296 -18.025 -45.731 17.609 1.00 84.67 C ANISOU 2270 CB THR A 296 8407 13939 9824 4679 -1489 -884 C ATOM 2271 CG2 THR A 296 -19.172 -46.226 18.475 1.00 87.48 C ANISOU 2271 CG2 THR A 296 8175 14797 10266 4599 -1368 -1086 C ATOM 2272 OG1 THR A 296 -17.972 -44.296 17.641 1.00 87.59 O ANISOU 2272 OG1 THR A 296 9170 13942 10169 5163 -1508 -824 O ATOM 2273 N ASP A 297 -14.836 -44.853 17.654 1.00 82.34 N ANISOU 2273 N ASP A 297 9329 12440 9516 4522 -1343 -524 N ATOM 2274 CA ASP A 297 -13.695 -44.349 16.904 1.00 80.88 C ANISOU 2274 CA ASP A 297 9687 11767 9276 4517 -1389 -266 C ATOM 2275 C ASP A 297 -12.671 -45.441 16.606 1.00 76.08 C ANISOU 2275 C ASP A 297 9091 11169 8647 4091 -1353 -169 C ATOM 2276 O ASP A 297 -11.845 -45.301 15.711 1.00 75.70 O ANISOU 2276 O ASP A 297 9398 10859 8505 4036 -1393 64 O ATOM 2277 CB ASP A 297 -13.024 -43.211 17.668 1.00 81.33 C ANISOU 2277 CB ASP A 297 10197 11281 9425 4666 -1279 -227 C ATOM 2278 CG ASP A 297 -13.733 -41.894 17.477 1.00 87.22 C ANISOU 2278 CG ASP A 297 11162 11831 10146 5126 -1369 -217 C ATOM 2279 OD1 ASP A 297 -13.104 -40.842 17.753 1.00 88.48 O ANISOU 2279 OD1 ASP A 297 11818 11437 10363 5228 -1332 -130 O ATOM 2280 OD2 ASP A 297 -14.916 -41.912 17.047 1.00 90.97 O1- ANISOU 2280 OD2 ASP A 297 11319 12691 10556 5373 -1490 -297 O1- ATOM 2281 N ASN A 298 -12.697 -46.504 17.396 1.00 72.47 N ANISOU 2281 N ASN A 298 8263 11005 8268 3784 -1254 -337 N ATOM 2282 CA ASN A 298 -11.742 -47.588 17.243 1.00 69.34 C ANISOU 2282 CA ASN A 298 7860 10624 7861 3390 -1222 -273 C ATOM 2283 C ASN A 298 -12.276 -48.797 16.481 1.00 68.72 C ANISOU 2283 C ASN A 298 7464 10950 7697 3145 -1345 -346 C ATOM 2284 O ASN A 298 -11.538 -49.759 16.250 1.00 67.33 O ANISOU 2284 O ASN A 298 7306 10787 7488 2825 -1339 -313 O ATOM 2285 CB ASN A 298 -11.254 -48.023 18.625 1.00 68.01 C ANISOU 2285 CB ASN A 298 7607 10395 7838 3053 -997 -395 C ATOM 2286 CG ASN A 298 -10.672 -46.867 19.438 1.00 69.10 C ANISOU 2286 CG ASN A 298 8126 10068 8061 3186 -874 -369 C ATOM 2287 ND2 ASN A 298 -11.168 -46.694 20.658 1.00 69.31 N ANISOU 2287 ND2 ASN A 298 7989 10201 8145 3254 -751 -578 N ATOM 2288 OD1 ASN A 298 -9.788 -46.144 18.972 1.00 70.02 O ANISOU 2288 OD1 ASN A 298 8688 9736 8179 3209 -885 -167 O ATOM 2289 N GLN A 299 -13.550 -48.749 16.090 1.00 68.82 N ANISOU 2289 N GLN A 299 7204 11269 7676 3295 -1470 -454 N ATOM 2290 CA GLN A 299 -14.232 -49.944 15.588 1.00 69.41 C ANISOU 2290 CA GLN A 299 6931 11722 7721 3015 -1593 -577 C ATOM 2291 C GLN A 299 -13.601 -50.480 14.306 1.00 68.81 C ANISOU 2291 C GLN A 299 7112 11561 7470 2903 -1734 -469 C ATOM 2292 O GLN A 299 -13.739 -51.662 13.974 1.00 68.42 O ANISOU 2292 O GLN A 299 6896 11699 7400 2577 -1814 -574 O ATOM 2293 CB GLN A 299 -15.729 -49.684 15.388 1.00 74.66 C ANISOU 2293 CB GLN A 299 7246 12726 8396 3227 -1721 -694 C ATOM 2294 CG GLN A 299 -16.050 -48.608 14.358 1.00 78.72 C ANISOU 2294 CG GLN A 299 8006 13132 8773 3685 -1902 -572 C ATOM 2295 CD GLN A 299 -17.529 -48.228 14.349 1.00 84.58 C ANISOU 2295 CD GLN A 299 8367 14218 9551 3957 -2022 -692 C ATOM 2296 NE2 GLN A 299 -17.844 -47.054 14.890 1.00 87.11 N ANISOU 2296 NE2 GLN A 299 8766 14419 9914 4357 -1950 -685 N ATOM 2297 OE1 GLN A 299 -18.375 -48.982 13.859 1.00 87.29 O ANISOU 2297 OE1 GLN A 299 8355 14920 9891 3809 -2187 -794 O ATOM 2298 N ARG A 300 -12.906 -49.604 13.589 1.00 59.02 N ANISOU 2298 N ARG A 300 6315 10014 6096 3162 -1750 -254 N ATOM 2299 CA ARG A 300 -12.155 -50.012 12.416 1.00 58.82 C ANISOU 2299 CA ARG A 300 6594 9893 5861 3081 -1814 -123 C ATOM 2300 C ARG A 300 -11.026 -50.949 12.832 1.00 56.05 C ANISOU 2300 C ARG A 300 6304 9450 5542 2722 -1672 -122 C ATOM 2301 O ARG A 300 -10.930 -52.090 12.354 1.00 55.76 O ANISOU 2301 O ARG A 300 6209 9557 5422 2466 -1740 -229 O ATOM 2302 CB ARG A 300 -11.574 -48.791 11.723 1.00 60.55 C ANISOU 2302 CB ARG A 300 7290 9772 5943 3388 -1785 155 C ATOM 2303 CG ARG A 300 -11.344 -49.015 10.262 1.00 62.72 C ANISOU 2303 CG ARG A 300 7818 10076 5937 3422 -1889 270 C ATOM 2304 CD ARG A 300 -12.486 -48.459 9.442 1.00 67.17 C ANISOU 2304 CD ARG A 300 8336 10804 6382 3740 -2122 255 C ATOM 2305 NE ARG A 300 -12.174 -47.124 8.939 1.00 69.77 N ANISOU 2305 NE ARG A 300 9092 10811 6608 4048 -2089 533 N ATOM 2306 CZ ARG A 300 -12.970 -46.419 8.140 1.00 74.86 C ANISOU 2306 CZ ARG A 300 9815 11511 7115 4381 -2284 597 C ATOM 2307 NH1 ARG A 300 -12.592 -45.218 7.722 1.00 77.42 N1+ ANISOU 2307 NH1 ARG A 300 10574 11488 7355 4617 -2237 874 N1+ ATOM 2308 NH2 ARG A 300 -14.139 -46.919 7.757 1.00 77.96 N ANISOU 2308 NH2 ARG A 300 9857 12299 7464 4455 -2535 395 N ATOM 2309 N ILE A 301 -10.195 -50.462 13.756 1.00 53.21 N ANISOU 2309 N ILE A 301 6074 8834 5310 2713 -1491 -17 N ATOM 2310 CA ILE A 301 -9.062 -51.226 14.269 1.00 51.51 C ANISOU 2310 CA ILE A 301 5952 8417 5203 2284 -1266 -8 C ATOM 2311 C ILE A 301 -9.506 -52.628 14.662 1.00 50.04 C ANISOU 2311 C ILE A 301 5428 8501 5086 1940 -1311 -245 C ATOM 2312 O ILE A 301 -8.902 -53.619 14.241 1.00 49.68 O ANISOU 2312 O ILE A 301 5480 8421 4976 1694 -1291 -271 O ATOM 2313 CB ILE A 301 -8.455 -50.578 15.522 1.00 50.84 C ANISOU 2313 CB ILE A 301 5953 8019 5346 2183 -1044 40 C ATOM 2314 CG1 ILE A 301 -8.222 -49.068 15.315 1.00 52.70 C ANISOU 2314 CG1 ILE A 301 6524 7934 5565 2513 -1029 245 C ATOM 2315 CG2 ILE A 301 -7.207 -51.349 15.944 1.00 49.46 C ANISOU 2315 CG2 ILE A 301 5873 7651 5269 1775 -851 75 C ATOM 2316 CD1 ILE A 301 -7.019 -48.725 14.460 1.00 54.13 C ANISOU 2316 CD1 ILE A 301 7101 7816 5648 2452 -922 528 C ATOM 2317 N LEU A 302 -10.573 -52.703 15.457 1.00 60.16 N ANISOU 2317 N LEU A 302 6324 10044 6491 1932 -1361 -414 N ATOM 2318 CA LEU A 302 -11.103 -53.987 15.905 1.00 59.47 C ANISOU 2318 CA LEU A 302 5903 10205 6487 1553 -1393 -610 C ATOM 2319 C LEU A 302 -11.291 -54.934 14.732 1.00 60.49 C ANISOU 2319 C LEU A 302 6059 10462 6462 1433 -1607 -692 C ATOM 2320 O LEU A 302 -10.779 -56.050 14.743 1.00 60.05 O ANISOU 2320 O LEU A 302 6076 10328 6413 1099 -1589 -761 O ATOM 2321 CB LEU A 302 -12.444 -53.804 16.597 1.00 60.07 C ANISOU 2321 CB LEU A 302 5547 10598 6679 1597 -1402 -747 C ATOM 2322 CG LEU A 302 -12.476 -53.462 18.077 1.00 59.33 C ANISOU 2322 CG LEU A 302 5290 10522 6732 1563 -1180 -782 C ATOM 2323 CD1 LEU A 302 -12.080 -52.013 18.314 1.00 59.72 C ANISOU 2323 CD1 LEU A 302 5621 10292 6778 1970 -1090 -671 C ATOM 2324 CD2 LEU A 302 -13.876 -53.719 18.526 1.00 60.98 C ANISOU 2324 CD2 LEU A 302 5082 11070 7018 1475 -1151 -918 C ATOM 2325 N GLU A 303 -12.026 -54.474 13.723 1.00 54.15 N ANISOU 2325 N GLU A 303 5269 9772 5535 1692 -1778 -685 N ATOM 2326 CA GLU A 303 -12.353 -55.291 12.562 1.00 55.88 C ANISOU 2326 CA GLU A 303 5543 10086 5604 1588 -1987 -781 C ATOM 2327 C GLU A 303 -11.093 -55.681 11.798 1.00 55.80 C ANISOU 2327 C GLU A 303 5956 9862 5383 1577 -1953 -707 C ATOM 2328 O GLU A 303 -11.029 -56.730 11.154 1.00 56.80 O ANISOU 2328 O GLU A 303 6178 9998 5408 1379 -2066 -840 O ATOM 2329 CB GLU A 303 -13.305 -54.520 11.648 1.00 59.49 C ANISOU 2329 CB GLU A 303 5957 10704 5942 1929 -2182 -755 C ATOM 2330 CG GLU A 303 -14.584 -54.065 12.340 1.00 61.65 C ANISOU 2330 CG GLU A 303 5799 11224 6400 2012 -2205 -831 C ATOM 2331 CD GLU A 303 -15.411 -53.160 11.464 1.00 66.11 C ANISOU 2331 CD GLU A 303 6357 11921 6842 2418 -2401 -782 C ATOM 2332 OE1 GLU A 303 -15.515 -53.483 10.265 1.00 68.68 O ANISOU 2332 OE1 GLU A 303 6828 12295 6971 2445 -2618 -792 O ATOM 2333 OE2 GLU A 303 -15.942 -52.132 11.956 1.00 67.69 O1- ANISOU 2333 OE2 GLU A 303 6434 12164 7122 2725 -2346 -740 O1- ATOM 2334 N PHE A 304 -10.091 -54.819 11.868 1.00 48.03 N ANISOU 2334 N PHE A 304 5245 8675 4330 1797 -1787 -492 N ATOM 2335 CA PHE A 304 -8.822 -55.111 11.242 1.00 48.55 C ANISOU 2335 CA PHE A 304 5688 8555 4203 1794 -1670 -383 C ATOM 2336 C PHE A 304 -8.098 -56.270 11.944 1.00 47.23 C ANISOU 2336 C PHE A 304 5516 8215 4216 1396 -1500 -489 C ATOM 2337 O PHE A 304 -7.263 -56.952 11.348 1.00 48.18 O ANISOU 2337 O PHE A 304 5884 8220 4201 1341 -1427 -502 O ATOM 2338 CB PHE A 304 -7.952 -53.863 11.212 1.00 48.88 C ANISOU 2338 CB PHE A 304 6012 8328 4233 2012 -1443 -75 C ATOM 2339 CG PHE A 304 -6.610 -54.089 10.600 1.00 49.98 C ANISOU 2339 CG PHE A 304 6484 8271 4234 1961 -1219 76 C ATOM 2340 CD1 PHE A 304 -5.506 -54.324 11.401 1.00 48.86 C ANISOU 2340 CD1 PHE A 304 6361 7885 4320 1712 -943 139 C ATOM 2341 CD2 PHE A 304 -6.451 -54.086 9.219 1.00 52.32 C ANISOU 2341 CD2 PHE A 304 7059 8669 4150 2180 -1283 151 C ATOM 2342 CE1 PHE A 304 -4.257 -54.530 10.847 1.00 50.16 C ANISOU 2342 CE1 PHE A 304 6753 7929 4378 1687 -715 277 C ATOM 2343 CE2 PHE A 304 -5.204 -54.296 8.652 1.00 53.46 C ANISOU 2343 CE2 PHE A 304 7475 8688 4149 2153 -1021 291 C ATOM 2344 CZ PHE A 304 -4.098 -54.516 9.475 1.00 52.36 C ANISOU 2344 CZ PHE A 304 7287 8324 4282 1907 -726 354 C ATOM 2345 N PHE A 305 -8.400 -56.474 13.220 1.00 40.68 N ANISOU 2345 N PHE A 305 4422 7366 3667 1157 -1426 -556 N ATOM 2346 CA PHE A 305 -7.866 -57.624 13.947 1.00 39.65 C ANISOU 2346 CA PHE A 305 4294 7076 3696 789 -1313 -644 C ATOM 2347 C PHE A 305 -8.846 -58.800 14.075 1.00 40.25 C ANISOU 2347 C PHE A 305 4144 7330 3822 485 -1518 -887 C ATOM 2348 O PHE A 305 -8.518 -59.830 14.685 1.00 39.98 O ANISOU 2348 O PHE A 305 4145 7128 3916 164 -1451 -952 O ATOM 2349 CB PHE A 305 -7.345 -57.197 15.311 1.00 37.65 C ANISOU 2349 CB PHE A 305 3986 6638 3683 675 -1077 -528 C ATOM 2350 CG PHE A 305 -6.162 -56.255 15.243 1.00 37.38 C ANISOU 2350 CG PHE A 305 4193 6361 3648 847 -881 -302 C ATOM 2351 CD1 PHE A 305 -4.855 -56.724 15.424 1.00 37.17 C ANISOU 2351 CD1 PHE A 305 4333 6105 3685 717 -709 -221 C ATOM 2352 CD2 PHE A 305 -6.360 -54.903 15.015 1.00 37.89 C ANISOU 2352 CD2 PHE A 305 4309 6421 3667 1130 -878 -164 C ATOM 2353 CE1 PHE A 305 -3.777 -55.861 15.374 1.00 37.43 C ANISOU 2353 CE1 PHE A 305 4518 5954 3748 813 -531 -8 C ATOM 2354 CE2 PHE A 305 -5.289 -54.019 14.951 1.00 38.45 C ANISOU 2354 CE2 PHE A 305 4611 6238 3761 1214 -703 60 C ATOM 2355 CZ PHE A 305 -3.987 -54.497 15.127 1.00 38.37 C ANISOU 2355 CZ PHE A 305 4706 6044 3828 1027 -524 140 C ATOM 2356 N GLY A 306 -10.043 -58.645 13.507 1.00 47.15 N ANISOU 2356 N GLY A 306 4783 8532 4600 576 -1782 -1007 N ATOM 2357 CA GLY A 306 -11.014 -59.720 13.498 1.00 48.45 C ANISOU 2357 CA GLY A 306 4759 8779 4870 228 -1938 -1187 C ATOM 2358 C GLY A 306 -11.708 -59.941 14.831 1.00 47.56 C ANISOU 2358 C GLY A 306 4293 8750 5029 -76 -1819 -1193 C ATOM 2359 O GLY A 306 -12.128 -61.059 15.153 1.00 48.31 O ANISOU 2359 O GLY A 306 4316 8789 5250 -478 -1862 -1285 O ATOM 2360 N LEU A 307 -11.830 -58.875 15.612 1.00 59.62 N ANISOU 2360 N LEU A 307 5638 10385 6630 123 -1658 -1085 N ATOM 2361 CA LEU A 307 -12.456 -58.967 16.922 1.00 59.07 C ANISOU 2361 CA LEU A 307 5258 10427 6759 -107 -1487 -1082 C ATOM 2362 C LEU A 307 -13.772 -58.211 16.960 1.00 60.91 C ANISOU 2362 C LEU A 307 5130 10979 7035 99 -1518 -1105 C ATOM 2363 O LEU A 307 -13.958 -57.233 16.238 1.00 61.78 O ANISOU 2363 O LEU A 307 5270 11168 7036 513 -1622 -1076 O ATOM 2364 CB LEU A 307 -11.521 -58.420 17.999 1.00 57.15 C ANISOU 2364 CB LEU A 307 5104 10053 6557 -56 -1252 -974 C ATOM 2365 CG LEU A 307 -10.323 -59.284 18.388 1.00 56.45 C ANISOU 2365 CG LEU A 307 5369 9569 6511 -324 -1122 -904 C ATOM 2366 CD1 LEU A 307 -9.435 -58.531 19.364 1.00 54.95 C ANISOU 2366 CD1 LEU A 307 5343 9158 6378 -212 -881 -753 C ATOM 2367 CD2 LEU A 307 -10.786 -60.603 18.985 1.00 57.32 C ANISOU 2367 CD2 LEU A 307 5356 9700 6723 -814 -1131 -981 C ATOM 2368 N LYS A 308 -14.680 -58.671 17.813 1.00 82.54 N ANISOU 2368 N LYS A 308 7545 13894 9920 -180 -1415 -1144 N ATOM 2369 CA LYS A 308 -15.945 -57.987 18.032 1.00 85.74 C ANISOU 2369 CA LYS A 308 7559 14645 10375 15 -1400 -1176 C ATOM 2370 C LYS A 308 -15.791 -57.025 19.199 1.00 84.38 C ANISOU 2370 C LYS A 308 7322 14523 10216 238 -1129 -1125 C ATOM 2371 O LYS A 308 -14.756 -56.379 19.344 1.00 81.25 O ANISOU 2371 O LYS A 308 7204 13910 9757 454 -1061 -1059 O ATOM 2372 CB LYS A 308 -17.055 -58.995 18.325 1.00 90.00 C ANISOU 2372 CB LYS A 308 7757 15384 11054 -406 -1419 -1237 C ATOM 2373 CG LYS A 308 -17.477 -59.821 17.120 1.00 93.09 C ANISOU 2373 CG LYS A 308 8159 15767 11445 -587 -1749 -1325 C ATOM 2374 CD LYS A 308 -17.662 -61.282 17.491 1.00 94.75 C ANISOU 2374 CD LYS A 308 8352 15849 11798 -1172 -1753 -1349 C ATOM 2375 CE LYS A 308 -18.236 -62.073 16.329 1.00 98.87 C ANISOU 2375 CE LYS A 308 8858 16373 12334 -1356 -2121 -1470 C ATOM 2376 NZ LYS A 308 -18.329 -61.247 15.094 1.00 99.57 N1+ ANISOU 2376 NZ LYS A 308 9001 16588 12244 -913 -2374 -1517 N1+ ATOM 2377 N LYS A 309 -16.816 -56.934 20.036 1.00 78.31 N ANISOU 2377 N LYS A 309 6191 14041 9523 189 -977 -1160 N ATOM 2378 CA LYS A 309 -16.751 -56.073 21.208 1.00 77.72 C ANISOU 2378 CA LYS A 309 6070 14030 9431 407 -711 -1147 C ATOM 2379 C LYS A 309 -16.851 -56.895 22.485 1.00 78.06 C ANISOU 2379 C LYS A 309 6003 14136 9520 -31 -448 -1118 C ATOM 2380 O LYS A 309 -16.334 -56.501 23.528 1.00 76.23 O ANISOU 2380 O LYS A 309 5881 13847 9237 23 -221 -1092 O ATOM 2381 CB LYS A 309 -17.854 -55.016 21.166 1.00 82.08 C ANISOU 2381 CB LYS A 309 6338 14875 9972 854 -720 -1212 C ATOM 2382 CG LYS A 309 -17.508 -53.798 20.325 1.00 81.53 C ANISOU 2382 CG LYS A 309 6517 14644 9818 1403 -888 -1192 C ATOM 2383 CD LYS A 309 -18.011 -52.516 20.967 1.00 84.15 C ANISOU 2383 CD LYS A 309 6777 15070 10126 1887 -758 -1237 C ATOM 2384 CE LYS A 309 -18.952 -51.768 20.039 1.00 88.87 C ANISOU 2384 CE LYS A 309 7239 15828 10701 2309 -977 -1261 C ATOM 2385 NZ LYS A 309 -19.865 -52.693 19.313 1.00 92.25 N1+ ANISOU 2385 NZ LYS A 309 7310 16556 11185 2032 -1163 -1299 N1+ ATOM 2386 N GLU A 310 -17.511 -58.043 22.395 1.00 86.31 N ANISOU 2386 N GLU A 310 6861 15279 10653 -468 -489 -1114 N ATOM 2387 CA GLU A 310 -17.684 -58.905 23.555 1.00 87.55 C ANISOU 2387 CA GLU A 310 6950 15472 10844 -912 -244 -1045 C ATOM 2388 C GLU A 310 -16.540 -59.900 23.712 1.00 83.84 C ANISOU 2388 C GLU A 310 6882 14601 10373 -1290 -246 -953 C ATOM 2389 O GLU A 310 -16.449 -60.596 24.721 1.00 84.34 O ANISOU 2389 O GLU A 310 7008 14606 10430 -1637 -46 -856 O ATOM 2390 CB GLU A 310 -19.017 -59.647 23.468 1.00 93.47 C ANISOU 2390 CB GLU A 310 7294 16506 11715 -1213 -275 -1062 C ATOM 2391 CG GLU A 310 -20.233 -58.747 23.610 1.00 98.42 C ANISOU 2391 CG GLU A 310 7461 17582 12353 -872 -210 -1137 C ATOM 2392 CD GLU A 310 -20.382 -58.186 25.010 1.00 99.46 C ANISOU 2392 CD GLU A 310 7503 17894 12395 -748 155 -1111 C ATOM 2393 OE1 GLU A 310 -20.858 -58.924 25.898 1.00102.56 O ANISOU 2393 OE1 GLU A 310 7731 18425 12812 -1132 379 -1034 O ATOM 2394 OE2 GLU A 310 -20.023 -57.009 25.222 1.00 97.61 O1- ANISOU 2394 OE2 GLU A 310 7390 17642 12054 -262 217 -1166 O1- ATOM 2395 N GLU A 311 -15.667 -59.963 22.711 1.00 93.17 N ANISOU 2395 N GLU A 311 8355 15502 11543 -1199 -471 -973 N ATOM 2396 CA GLU A 311 -14.525 -60.869 22.753 1.00 90.59 C ANISOU 2396 CA GLU A 311 8425 14776 11218 -1488 -497 -901 C ATOM 2397 C GLU A 311 -13.369 -60.260 23.542 1.00 87.86 C ANISOU 2397 C GLU A 311 8316 14274 10791 -1345 -335 -829 C ATOM 2398 O GLU A 311 -12.489 -60.970 24.021 1.00 87.46 O ANISOU 2398 O GLU A 311 8556 13936 10737 -1603 -284 -738 O ATOM 2399 CB GLU A 311 -14.071 -61.227 21.337 1.00 89.81 C ANISOU 2399 CB GLU A 311 8538 14468 11117 -1434 -796 -971 C ATOM 2400 CG GLU A 311 -14.485 -62.619 20.888 1.00 92.83 C ANISOU 2400 CG GLU A 311 8969 14710 11593 -1847 -953 -1009 C ATOM 2401 CD GLU A 311 -13.844 -63.025 19.576 1.00 92.04 C ANISOU 2401 CD GLU A 311 9170 14366 11437 -1777 -1232 -1104 C ATOM 2402 OE1 GLU A 311 -14.292 -62.537 18.518 1.00 92.98 O ANISOU 2402 OE1 GLU A 311 9182 14655 11491 -1525 -1438 -1197 O ATOM 2403 OE2 GLU A 311 -12.892 -63.831 19.602 1.00 90.82 O1- ANISOU 2403 OE2 GLU A 311 9379 13851 11277 -1950 -1246 -1087 O1- ATOM 2404 N CYS A 312 -13.384 -58.939 23.671 1.00 61.44 N ANISOU 2404 N CYS A 312 4858 11098 7388 -919 -275 -872 N ATOM 2405 CA CYS A 312 -12.380 -58.222 24.442 1.00 60.42 C ANISOU 2405 CA CYS A 312 4966 10794 7196 -747 -133 -819 C ATOM 2406 C CYS A 312 -12.785 -58.210 25.911 1.00 61.75 C ANISOU 2406 C CYS A 312 5005 11160 7297 -886 156 -796 C ATOM 2407 O CYS A 312 -13.948 -58.441 26.237 1.00 63.30 O ANISOU 2407 O CYS A 312 4895 11661 7496 -988 259 -823 O ATOM 2408 CB CYS A 312 -12.231 -56.793 23.923 1.00 59.99 C ANISOU 2408 CB CYS A 312 4983 10698 7110 -202 -199 -861 C ATOM 2409 SG CYS A 312 -12.432 -56.625 22.134 1.00 59.51 S ANISOU 2409 SG CYS A 312 4888 10669 7055 38 -518 -903 S ATOM 2410 N PRO A 313 -11.829 -57.955 26.798 1.00 54.26 N ANISOU 2410 N PRO A 313 4423 9925 6267 -856 275 -719 N ATOM 2411 CA PRO A 313 -10.459 -57.605 26.409 1.00 53.08 C ANISOU 2411 CA PRO A 313 4709 9320 6139 -698 142 -657 C ATOM 2412 C PRO A 313 -9.694 -58.738 25.729 1.00 51.81 C ANISOU 2412 C PRO A 313 4762 8870 6054 -965 -14 -569 C ATOM 2413 O PRO A 313 -10.005 -59.913 25.913 1.00 52.36 O ANISOU 2413 O PRO A 313 4782 8968 6143 -1341 -6 -529 O ATOM 2414 CB PRO A 313 -9.799 -57.267 27.746 1.00 54.22 C ANISOU 2414 CB PRO A 313 5111 9319 6171 -701 297 -611 C ATOM 2415 CG PRO A 313 -10.555 -58.072 28.743 1.00 55.37 C ANISOU 2415 CG PRO A 313 5081 9738 6219 -1027 496 -575 C ATOM 2416 CD PRO A 313 -11.975 -58.076 28.258 1.00 55.57 C ANISOU 2416 CD PRO A 313 4604 10214 6297 -1014 540 -675 C ATOM 2417 N ALA A 314 -8.688 -58.358 24.950 1.00 41.94 N ANISOU 2417 N ALA A 314 3763 7330 4840 -762 -141 -537 N ATOM 2418 CA ALA A 314 -7.856 -59.290 24.206 1.00 40.80 C ANISOU 2418 CA ALA A 314 3837 6917 4747 -898 -269 -480 C ATOM 2419 C ALA A 314 -6.525 -58.622 23.886 1.00 39.76 C ANISOU 2419 C ALA A 314 3972 6497 4636 -666 -296 -402 C ATOM 2420 O ALA A 314 -6.383 -57.392 23.975 1.00 39.73 O ANISOU 2420 O ALA A 314 3987 6486 4624 -416 -260 -401 O ATOM 2421 CB ALA A 314 -8.550 -59.729 22.934 1.00 40.61 C ANISOU 2421 CB ALA A 314 3663 7031 4736 -908 -431 -577 C ATOM 2422 N VAL A 315 -5.536 -59.433 23.530 1.00 44.36 N ANISOU 2422 N VAL A 315 4762 6835 5258 -753 -354 -337 N ATOM 2423 CA VAL A 315 -4.251 -58.872 23.149 1.00 43.73 C ANISOU 2423 CA VAL A 315 4858 6541 5217 -564 -357 -250 C ATOM 2424 C VAL A 315 -3.823 -59.353 21.765 1.00 43.81 C ANISOU 2424 C VAL A 315 4953 6479 5213 -465 -429 -258 C ATOM 2425 O VAL A 315 -3.962 -60.520 21.443 1.00 44.81 O ANISOU 2425 O VAL A 315 5135 6561 5329 -601 -496 -316 O ATOM 2426 CB VAL A 315 -3.144 -59.117 24.240 1.00 43.69 C ANISOU 2426 CB VAL A 315 5006 6336 5259 -671 -328 -147 C ATOM 2427 CG1 VAL A 315 -3.494 -58.378 25.513 1.00 44.08 C ANISOU 2427 CG1 VAL A 315 5024 6465 5258 -702 -261 -161 C ATOM 2428 CG2 VAL A 315 -2.981 -60.581 24.552 1.00 44.30 C ANISOU 2428 CG2 VAL A 315 5188 6301 5344 -885 -370 -118 C ATOM 2429 N ARG A 316 -3.333 -58.441 20.939 1.00 35.91 N ANISOU 2429 N ARG A 316 3996 5455 4192 -230 -409 -202 N ATOM 2430 CA ARG A 316 -2.785 -58.850 19.660 1.00 36.90 C ANISOU 2430 CA ARG A 316 4233 5534 4252 -107 -430 -195 C ATOM 2431 C ARG A 316 -1.426 -58.207 19.434 1.00 36.89 C ANISOU 2431 C ARG A 316 4318 5398 4302 18 -318 -38 C ATOM 2432 O ARG A 316 -1.175 -57.101 19.876 1.00 36.37 O ANISOU 2432 O ARG A 316 4233 5286 4300 49 -268 55 O ATOM 2433 CB ARG A 316 -3.723 -58.484 18.506 1.00 37.55 C ANISOU 2433 CB ARG A 316 4271 5806 4189 57 -519 -269 C ATOM 2434 CG ARG A 316 -5.033 -59.271 18.434 1.00 38.19 C ANISOU 2434 CG ARG A 316 4213 6070 4227 -93 -667 -444 C ATOM 2435 CD ARG A 316 -4.818 -60.771 18.223 1.00 39.75 C ANISOU 2435 CD ARG A 316 4542 6141 4422 -286 -738 -544 C ATOM 2436 NE ARG A 316 -6.087 -61.472 18.042 1.00 40.54 N ANISOU 2436 NE ARG A 316 4504 6404 4496 -490 -907 -711 N ATOM 2437 CZ ARG A 316 -6.860 -61.903 19.036 1.00 40.13 C ANISOU 2437 CZ ARG A 316 4277 6423 4549 -791 -904 -736 C ATOM 2438 NH1 ARG A 316 -6.509 -61.713 20.307 1.00 39.00 N1+ ANISOU 2438 NH1 ARG A 316 4120 6198 4498 -886 -746 -613 N1+ ATOM 2439 NH2 ARG A 316 -7.998 -62.525 18.759 1.00 41.25 N ANISOU 2439 NH2 ARG A 316 4250 6739 4685 -1016 -1061 -880 N ATOM 2440 N LEU A 317 -0.553 -58.908 18.726 1.00 45.88 N ANISOU 2440 N LEU A 317 5546 6472 5413 86 -276 -18 N ATOM 2441 CA LEU A 317 0.759 -58.387 18.357 1.00 46.06 C ANISOU 2441 CA LEU A 317 5582 6436 5484 194 -135 142 C ATOM 2442 C LEU A 317 0.783 -58.104 16.841 1.00 47.74 C ANISOU 2442 C LEU A 317 5885 6753 5502 407 -61 176 C ATOM 2443 O LEU A 317 0.178 -58.847 16.045 1.00 49.28 O ANISOU 2443 O LEU A 317 6173 7027 5524 487 -141 32 O ATOM 2444 CB LEU A 317 1.828 -59.423 18.709 1.00 46.68 C ANISOU 2444 CB LEU A 317 5663 6415 5660 173 -108 148 C ATOM 2445 CG LEU A 317 3.295 -59.072 18.971 1.00 46.19 C ANISOU 2445 CG LEU A 317 5487 6315 5749 196 4 309 C ATOM 2446 CD1 LEU A 317 3.910 -58.269 17.832 1.00 46.86 C ANISOU 2446 CD1 LEU A 317 5539 6495 5769 332 189 447 C ATOM 2447 CD2 LEU A 317 3.448 -58.355 20.289 1.00 44.62 C ANISOU 2447 CD2 LEU A 317 5202 6045 5707 10 -68 374 C ATOM 2448 N ILE A 318 1.504 -57.060 16.444 1.00 38.27 N ANISOU 2448 N ILE A 318 4682 5545 4313 475 84 372 N ATOM 2449 CA ILE A 318 1.645 -56.727 15.030 1.00 40.72 C ANISOU 2449 CA ILE A 318 5113 5962 4399 675 197 462 C ATOM 2450 C ILE A 318 3.006 -56.121 14.689 1.00 41.98 C ANISOU 2450 C ILE A 318 5226 6108 4619 680 443 704 C ATOM 2451 O ILE A 318 3.381 -55.079 15.219 1.00 42.58 O ANISOU 2451 O ILE A 318 5242 6071 4863 543 486 870 O ATOM 2452 CB ILE A 318 0.546 -55.753 14.567 1.00 42.10 C ANISOU 2452 CB ILE A 318 5382 6185 4430 777 98 495 C ATOM 2453 CG1 ILE A 318 0.596 -55.578 13.049 1.00 44.26 C ANISOU 2453 CG1 ILE A 318 5835 6588 4391 1006 179 584 C ATOM 2454 CG2 ILE A 318 0.696 -54.411 15.265 1.00 42.03 C ANISOU 2454 CG2 ILE A 318 5354 6018 4596 693 130 662 C ATOM 2455 CD1 ILE A 318 -0.672 -55.006 12.457 1.00 44.79 C ANISOU 2455 CD1 ILE A 318 6010 6754 4256 1174 -8 556 C ATOM 2456 N THR A 319 3.731 -56.769 13.784 1.00 40.59 N ANISOU 2456 N THR A 319 5074 6052 4297 832 610 715 N ATOM 2457 CA THR A 319 4.983 -56.219 13.280 1.00 42.03 C ANISOU 2457 CA THR A 319 5164 6305 4501 843 898 964 C ATOM 2458 C THR A 319 4.710 -55.393 12.029 1.00 44.69 C ANISOU 2458 C THR A 319 5707 6731 4541 977 1028 1141 C ATOM 2459 O THR A 319 4.083 -55.870 11.086 1.00 45.27 O ANISOU 2459 O THR A 319 5981 6928 4290 1195 983 1020 O ATOM 2460 CB THR A 319 6.010 -57.320 12.948 1.00 41.95 C ANISOU 2460 CB THR A 319 5043 6426 4470 994 1068 897 C ATOM 2461 CG2 THR A 319 6.077 -58.344 14.065 1.00 39.91 C ANISOU 2461 CG2 THR A 319 4682 6051 4433 935 881 702 C ATOM 2462 OG1 THR A 319 5.644 -57.973 11.728 1.00 43.21 O ANISOU 2462 OG1 THR A 319 5433 6721 4265 1266 1120 764 O ATOM 2463 N LEU A 320 5.176 -54.150 12.031 1.00 60.43 N ANISOU 2463 N LEU A 320 7683 8643 6634 833 1165 1431 N ATOM 2464 CA LEU A 320 4.981 -53.264 10.892 1.00 63.40 C ANISOU 2464 CA LEU A 320 8302 9059 6727 944 1299 1670 C ATOM 2465 C LEU A 320 6.092 -53.454 9.869 1.00 65.08 C ANISOU 2465 C LEU A 320 8477 9500 6752 1028 1676 1858 C ATOM 2466 O LEU A 320 6.861 -52.535 9.593 1.00 67.05 O ANISOU 2466 O LEU A 320 8692 9731 7053 871 1928 2192 O ATOM 2467 CB LEU A 320 4.922 -51.805 11.348 1.00 64.76 C ANISOU 2467 CB LEU A 320 8547 8969 7090 740 1269 1914 C ATOM 2468 CG LEU A 320 3.732 -51.429 12.233 1.00 63.95 C ANISOU 2468 CG LEU A 320 8523 8667 7109 738 937 1739 C ATOM 2469 CD1 LEU A 320 3.745 -49.945 12.554 1.00 65.23 C ANISOU 2469 CD1 LEU A 320 8838 8523 7425 596 924 1972 C ATOM 2470 CD2 LEU A 320 2.422 -51.829 11.575 1.00 63.66 C ANISOU 2470 CD2 LEU A 320 8659 8769 6759 1032 737 1563 C ATOM 2471 N GLU A 321 6.184 -54.660 9.319 1.00105.36 N ANISOU 2471 N GLU A 321 13587 14810 11634 1268 1727 1639 N ATOM 2472 CA GLU A 321 7.245 -54.992 8.376 1.00107.19 C ANISOU 2472 CA GLU A 321 13761 15310 11656 1419 2117 1760 C ATOM 2473 C GLU A 321 8.441 -55.575 9.116 1.00106.14 C ANISOU 2473 C GLU A 321 13219 15241 11869 1328 2261 1725 C ATOM 2474 O GLU A 321 8.494 -55.537 10.344 1.00104.12 O ANISOU 2474 O GLU A 321 12758 14801 12001 1106 2056 1665 O ATOM 2475 CB GLU A 321 7.675 -53.751 7.595 1.00106.10 C ANISOU 2475 CB GLU A 321 13723 15220 11368 1325 2412 2185 C ATOM 2476 CG GLU A 321 9.181 -53.596 7.465 1.00107.53 C ANISOU 2476 CG GLU A 321 13567 15527 11763 1153 2747 2357 C ATOM 2477 CD GLU A 321 9.819 -53.020 8.714 1.00106.46 C ANISOU 2477 CD GLU A 321 13080 15235 12135 773 2727 2505 C ATOM 2478 OE1 GLU A 321 9.863 -51.780 8.843 1.00107.72 O ANISOU 2478 OE1 GLU A 321 13311 15180 12438 476 2720 2763 O ATOM 2479 OE2 GLU A 321 10.278 -53.808 9.566 1.00104.56 O1- ANISOU 2479 OE2 GLU A 321 12516 15062 12152 774 2686 2344 O1- TER 2480 GLU A 321 ATOM 2481 N MET A 324 4.614 -57.665 7.278 1.00 80.67 N ANISOU 2481 N MET A 324 11058 12029 7564 2028 1408 804 N ATOM 2482 CA MET A 324 3.769 -57.427 8.441 1.00 78.57 C ANISOU 2482 CA MET A 324 10671 11545 7637 1783 1083 732 C ATOM 2483 C MET A 324 2.731 -58.516 8.695 1.00 77.65 C ANISOU 2483 C MET A 324 10640 11362 7502 1789 728 351 C ATOM 2484 O MET A 324 1.701 -58.580 8.028 1.00 78.51 O ANISOU 2484 O MET A 324 10946 11552 7331 1888 501 215 O ATOM 2485 CB MET A 324 3.090 -56.061 8.330 1.00 79.43 C ANISOU 2485 CB MET A 324 10869 11608 7703 1721 1001 972 C ATOM 2486 CG MET A 324 1.664 -56.023 8.846 1.00 78.70 C ANISOU 2486 CG MET A 324 10792 11432 7677 1670 605 783 C ATOM 2487 SD MET A 324 0.613 -54.988 7.815 1.00 81.12 S ANISOU 2487 SD MET A 324 11373 11838 7612 1887 446 929 S ATOM 2488 CE MET A 324 -0.797 -56.067 7.587 1.00 80.20 C ANISOU 2488 CE MET A 324 11286 11866 7322 1975 17 502 C ATOM 2489 N THR A 325 3.014 -59.364 9.678 1.00 69.55 N ANISOU 2489 N THR A 325 9460 10188 6779 1661 664 196 N ATOM 2490 CA THR A 325 2.057 -60.356 10.147 1.00 69.16 C ANISOU 2490 CA THR A 325 9469 10017 6792 1560 341 -113 C ATOM 2491 C THR A 325 1.453 -59.973 11.493 1.00 67.10 C ANISOU 2491 C THR A 325 9000 9621 6873 1270 170 -74 C ATOM 2492 O THR A 325 1.896 -59.027 12.141 1.00 65.72 O ANISOU 2492 O THR A 325 8658 9408 6905 1165 287 154 O ATOM 2493 CB THR A 325 2.702 -61.750 10.270 1.00 70.29 C ANISOU 2493 CB THR A 325 9682 10041 6984 1645 369 -329 C ATOM 2494 CG2 THR A 325 1.653 -62.837 10.118 1.00 72.03 C ANISOU 2494 CG2 THR A 325 10119 10151 7099 1588 46 -669 C ATOM 2495 OG1 THR A 325 3.695 -61.912 9.251 1.00 71.82 O ANISOU 2495 OG1 THR A 325 9978 10383 6926 1953 658 -300 O ATOM 2496 N LYS A 326 0.436 -60.722 11.904 1.00 63.90 N ANISOU 2496 N LYS A 326 8616 9148 6514 1126 -101 -305 N ATOM 2497 CA LYS A 326 -0.219 -60.502 13.184 1.00 62.30 C ANISOU 2497 CA LYS A 326 8224 8862 6587 862 -235 -293 C ATOM 2498 C LYS A 326 -0.208 -61.784 14.004 1.00 63.29 C ANISOU 2498 C LYS A 326 8367 8801 6881 684 -335 -455 C ATOM 2499 O LYS A 326 -0.211 -62.883 13.453 1.00 65.52 O ANISOU 2499 O LYS A 326 8844 9007 7045 741 -414 -652 O ATOM 2500 CB LYS A 326 -1.657 -60.029 12.972 1.00 61.97 C ANISOU 2500 CB LYS A 326 8134 8968 6444 823 -455 -369 C ATOM 2501 CG LYS A 326 -1.812 -58.520 12.902 1.00 61.11 C ANISOU 2501 CG LYS A 326 7956 8942 6320 928 -390 -149 C ATOM 2502 CD LYS A 326 -3.104 -58.132 12.206 1.00 61.76 C ANISOU 2502 CD LYS A 326 8041 9225 6200 1046 -618 -230 C ATOM 2503 CE LYS A 326 -2.926 -58.081 10.699 1.00 63.87 C ANISOU 2503 CE LYS A 326 8555 9620 6093 1310 -615 -211 C ATOM 2504 NZ LYS A 326 -4.234 -58.051 9.990 1.00 64.61 N1+ ANISOU 2504 NZ LYS A 326 8651 9936 5962 1416 -929 -359 N1+ ATOM 2505 N TYR A 327 -0.194 -61.641 15.324 1.00 43.97 N ANISOU 2505 N TYR A 327 5764 6256 4687 476 -340 -370 N ATOM 2506 CA TYR A 327 -0.187 -62.790 16.205 1.00 45.34 C ANISOU 2506 CA TYR A 327 5988 6233 5008 294 -431 -461 C ATOM 2507 C TYR A 327 -1.103 -62.551 17.393 1.00 42.78 C ANISOU 2507 C TYR A 327 5509 5924 4821 11 -521 -437 C ATOM 2508 O TYR A 327 -1.485 -61.414 17.688 1.00 39.82 O ANISOU 2508 O TYR A 327 4973 5689 4468 6 -485 -344 O ATOM 2509 CB TYR A 327 1.229 -63.051 16.724 1.00 45.41 C ANISOU 2509 CB TYR A 327 5990 6104 5161 391 -293 -340 C ATOM 2510 CG TYR A 327 2.298 -62.997 15.658 1.00 45.13 C ANISOU 2510 CG TYR A 327 6000 6140 5009 700 -112 -309 C ATOM 2511 CD1 TYR A 327 2.837 -61.786 15.258 1.00 42.75 C ANISOU 2511 CD1 TYR A 327 5555 6007 4681 795 72 -118 C ATOM 2512 CD2 TYR A 327 2.774 -64.157 15.057 1.00 47.59 C ANISOU 2512 CD2 TYR A 327 6515 6340 5227 899 -105 -466 C ATOM 2513 CE1 TYR A 327 3.819 -61.729 14.292 1.00 43.35 C ANISOU 2513 CE1 TYR A 327 5642 6196 4635 1050 292 -57 C ATOM 2514 CE2 TYR A 327 3.764 -64.112 14.100 1.00 47.58 C ANISOU 2514 CE2 TYR A 327 6530 6457 5091 1217 111 -444 C ATOM 2515 CZ TYR A 327 4.282 -62.897 13.720 1.00 45.52 C ANISOU 2515 CZ TYR A 327 6077 6420 4799 1277 326 -226 C ATOM 2516 OH TYR A 327 5.261 -62.832 12.746 1.00 46.37 O ANISOU 2516 OH TYR A 327 6172 6695 4751 1567 594 -172 O ATOM 2517 N LYS A 328 -1.459 -63.634 18.072 1.00 42.88 N ANISOU 2517 N LYS A 328 5600 5780 4913 -213 -625 -517 N ATOM 2518 CA LYS A 328 -2.165 -63.535 19.334 1.00 40.47 C ANISOU 2518 CA LYS A 328 5161 5499 4718 -490 -651 -462 C ATOM 2519 C LYS A 328 -1.613 -64.614 20.246 1.00 41.84 C ANISOU 2519 C LYS A 328 5502 5402 4994 -628 -671 -412 C ATOM 2520 O LYS A 328 -0.927 -65.529 19.793 1.00 44.80 O ANISOU 2520 O LYS A 328 6094 5563 5364 -510 -706 -466 O ATOM 2521 CB LYS A 328 -3.667 -63.713 19.139 1.00 39.73 C ANISOU 2521 CB LYS A 328 4951 5572 4573 -702 -777 -600 C ATOM 2522 CG LYS A 328 -4.062 -65.103 18.739 1.00 41.93 C ANISOU 2522 CG LYS A 328 5418 5681 4833 -894 -934 -761 C ATOM 2523 CD LYS A 328 -5.551 -65.199 18.528 1.00 41.39 C ANISOU 2523 CD LYS A 328 5151 5835 4741 -1149 -1079 -895 C ATOM 2524 CE LYS A 328 -5.950 -66.651 18.334 1.00 43.91 C ANISOU 2524 CE LYS A 328 5680 5918 5086 -1456 -1254 -1047 C ATOM 2525 NZ LYS A 328 -5.222 -67.570 19.277 1.00 44.60 N1+ ANISOU 2525 NZ LYS A 328 6033 5625 5286 -1594 -1190 -930 N1+ ATOM 2526 N PRO A 329 -1.902 -64.514 21.545 1.00 38.05 N ANISOU 2526 N PRO A 329 4950 4926 4582 -843 -649 -306 N ATOM 2527 CA PRO A 329 -1.307 -65.482 22.473 1.00 39.12 C ANISOU 2527 CA PRO A 329 5285 4796 4783 -944 -683 -210 C ATOM 2528 C PRO A 329 -1.914 -66.893 22.401 1.00 40.72 C ANISOU 2528 C PRO A 329 5722 4763 4987 -1188 -800 -289 C ATOM 2529 O PRO A 329 -3.070 -67.065 22.036 1.00 40.34 O ANISOU 2529 O PRO A 329 5598 4822 4909 -1418 -852 -404 O ATOM 2530 CB PRO A 329 -1.553 -64.836 23.833 1.00 36.87 C ANISOU 2530 CB PRO A 329 4876 4633 4501 -1101 -617 -78 C ATOM 2531 CG PRO A 329 -1.782 -63.363 23.511 1.00 34.70 C ANISOU 2531 CG PRO A 329 4356 4627 4203 -957 -536 -106 C ATOM 2532 CD PRO A 329 -2.546 -63.393 22.250 1.00 35.14 C ANISOU 2532 CD PRO A 329 4349 4795 4206 -916 -576 -252 C ATOM 2533 N GLU A 330 -1.111 -67.894 22.749 1.00 43.75 N ANISOU 2533 N GLU A 330 6391 4813 5419 -1135 -860 -225 N ATOM 2534 CA GLU A 330 -1.541 -69.285 22.740 1.00 45.34 C ANISOU 2534 CA GLU A 330 6911 4677 5640 -1365 -986 -279 C ATOM 2535 C GLU A 330 -2.657 -69.539 23.748 1.00 44.23 C ANISOU 2535 C GLU A 330 6734 4570 5500 -1843 -972 -171 C ATOM 2536 O GLU A 330 -3.466 -70.441 23.567 1.00 45.25 O ANISOU 2536 O GLU A 330 7014 4528 5653 -2173 -1063 -241 O ATOM 2537 CB GLU A 330 -0.370 -70.229 23.063 1.00 47.15 C ANISOU 2537 CB GLU A 330 7480 4511 5922 -1143 -1056 -194 C ATOM 2538 CG GLU A 330 0.930 -69.951 22.305 1.00 48.69 C ANISOU 2538 CG GLU A 330 7638 4734 6129 -636 -1014 -251 C ATOM 2539 CD GLU A 330 1.959 -69.154 23.138 1.00 47.98 C ANISOU 2539 CD GLU A 330 7330 4809 6092 -443 -943 -51 C ATOM 2540 OE1 GLU A 330 3.116 -69.639 23.282 1.00 48.78 O ANISOU 2540 OE1 GLU A 330 7534 4744 6256 -135 -988 11 O ATOM 2541 OE2 GLU A 330 1.617 -68.039 23.628 1.00 46.04 O1- ANISOU 2541 OE2 GLU A 330 6806 4859 5827 -583 -863 26 O1- ATOM 2542 N SER A 331 -2.694 -68.767 24.825 1.00 48.47 N ANISOU 2542 N SER A 331 7083 5329 6002 -1898 -851 -4 N ATOM 2543 CA SER A 331 -3.698 -68.991 25.852 1.00 48.11 C ANISOU 2543 CA SER A 331 6996 5368 5915 -2324 -777 120 C ATOM 2544 C SER A 331 -4.668 -67.809 25.976 1.00 46.41 C ANISOU 2544 C SER A 331 6348 5638 5649 -2398 -636 65 C ATOM 2545 O SER A 331 -4.445 -66.748 25.394 1.00 45.10 O ANISOU 2545 O SER A 331 5970 5688 5479 -2100 -613 -35 O ATOM 2546 CB SER A 331 -2.976 -69.245 27.174 1.00 48.45 C ANISOU 2546 CB SER A 331 7265 5246 5899 -2316 -755 367 C ATOM 2547 OG SER A 331 -3.883 -69.286 28.245 1.00 48.82 O ANISOU 2547 OG SER A 331 7260 5445 5844 -2692 -624 513 O ATOM 2548 N GLU A 332 -5.725 -67.971 26.764 1.00 50.11 N ANISOU 2548 N GLU A 332 6692 6278 6070 -2778 -525 145 N ATOM 2549 CA GLU A 332 -6.716 -66.903 26.884 1.00 49.18 C ANISOU 2549 CA GLU A 332 6138 6643 5904 -2798 -381 72 C ATOM 2550 C GLU A 332 -6.526 -66.058 28.133 1.00 49.03 C ANISOU 2550 C GLU A 332 6064 6816 5750 -2697 -204 196 C ATOM 2551 O GLU A 332 -7.232 -65.058 28.323 1.00 48.68 O ANISOU 2551 O GLU A 332 5696 7151 5649 -2619 -71 120 O ATOM 2552 CB GLU A 332 -8.143 -67.457 26.871 1.00 50.35 C ANISOU 2552 CB GLU A 332 6073 6972 6087 -3128 -323 41 C ATOM 2553 CG GLU A 332 -8.471 -68.339 25.675 1.00 51.39 C ANISOU 2553 CG GLU A 332 6274 6908 6343 -3214 -520 -110 C ATOM 2554 CD GLU A 332 -8.197 -67.660 24.334 1.00 50.52 C ANISOU 2554 CD GLU A 332 6053 6892 6248 -2922 -679 -328 C ATOM 2555 OE1 GLU A 332 -8.889 -66.651 24.027 1.00 49.49 O ANISOU 2555 OE1 GLU A 332 5542 7167 6095 -2783 -639 -421 O ATOM 2556 OE2 GLU A 332 -7.284 -68.144 23.600 1.00 51.06 O1- ANISOU 2556 OE2 GLU A 332 6443 6630 6328 -2806 -842 -403 O1- ATOM 2557 N GLU A 333 -5.567 -66.449 28.970 1.00 65.42 N ANISOU 2557 N GLU A 333 8470 8627 7758 -2662 -228 368 N ATOM 2558 CA GLU A 333 -5.374 -65.810 30.272 1.00 66.24 C ANISOU 2558 CA GLU A 333 8601 8887 7681 -2611 -98 483 C ATOM 2559 C GLU A 333 -4.492 -64.560 30.192 1.00 65.08 C ANISOU 2559 C GLU A 333 8393 8800 7535 -2205 -148 392 C ATOM 2560 O GLU A 333 -3.396 -64.582 29.633 1.00 64.11 O ANISOU 2560 O GLU A 333 8387 8450 7521 -1979 -303 382 O ATOM 2561 CB GLU A 333 -4.831 -66.821 31.302 1.00 68.04 C ANISOU 2561 CB GLU A 333 9230 8828 7795 -2783 -132 731 C ATOM 2562 CG GLU A 333 -3.527 -67.521 30.876 1.00 68.13 C ANISOU 2562 CG GLU A 333 9559 8404 7922 -2572 -371 782 C ATOM 2563 CD GLU A 333 -3.289 -68.871 31.568 1.00 69.97 C ANISOU 2563 CD GLU A 333 10224 8269 8092 -2786 -444 1027 C ATOM 2564 OE1 GLU A 333 -3.786 -69.894 31.048 1.00 70.53 O ANISOU 2564 OE1 GLU A 333 10433 8097 8268 -3043 -480 1035 O ATOM 2565 OE2 GLU A 333 -2.583 -68.919 32.611 1.00 70.94 O1- ANISOU 2565 OE2 GLU A 333 10582 8316 8056 -2691 -495 1210 O1- ATOM 2566 N LEU A 334 -4.977 -63.452 30.737 1.00 52.72 N ANISOU 2566 N LEU A 334 6638 7539 5853 -2116 -7 319 N ATOM 2567 CA LEU A 334 -4.140 -62.273 30.815 1.00 51.87 C ANISOU 2567 CA LEU A 334 6537 7426 5744 -1799 -69 244 C ATOM 2568 C LEU A 334 -3.654 -62.055 32.240 1.00 54.03 C ANISOU 2568 C LEU A 334 7021 7703 5804 -1805 -58 334 C ATOM 2569 O LEU A 334 -4.326 -61.479 33.074 1.00 54.81 O ANISOU 2569 O LEU A 334 7071 8046 5707 -1822 103 286 O ATOM 2570 CB LEU A 334 -4.938 -61.080 30.306 1.00 51.22 C ANISOU 2570 CB LEU A 334 6165 7610 5686 -1624 28 63 C ATOM 2571 CG LEU A 334 -5.667 -61.494 29.015 1.00 49.84 C ANISOU 2571 CG LEU A 334 5783 7498 5657 -1673 1 -11 C ATOM 2572 CD1 LEU A 334 -6.597 -60.414 28.521 1.00 49.70 C ANISOU 2572 CD1 LEU A 334 5462 7773 5648 -1479 73 -168 C ATOM 2573 CD2 LEU A 334 -4.683 -61.907 27.924 1.00 47.89 C ANISOU 2573 CD2 LEU A 334 5670 6966 5561 -1562 -175 0 C ATOM 2574 N THR A 335 -2.412 -62.456 32.442 1.00 51.17 N ANISOU 2574 N THR A 335 6885 7082 5475 -1739 -250 443 N ATOM 2575 CA THR A 335 -1.678 -62.218 33.653 1.00 51.53 C ANISOU 2575 CA THR A 335 7145 7103 5333 -1696 -341 517 C ATOM 2576 C THR A 335 -0.429 -61.534 33.142 1.00 49.44 C ANISOU 2576 C THR A 335 6828 6702 5255 -1463 -542 452 C ATOM 2577 O THR A 335 -0.103 -61.647 31.955 1.00 48.03 O ANISOU 2577 O THR A 335 6517 6420 5311 -1369 -580 422 O ATOM 2578 CB THR A 335 -1.274 -63.529 34.349 1.00 53.05 C ANISOU 2578 CB THR A 335 7641 7103 5413 -1842 -436 753 C ATOM 2579 CG2 THR A 335 -0.345 -63.247 35.525 1.00 53.35 C ANISOU 2579 CG2 THR A 335 7902 7123 5246 -1744 -610 826 C ATOM 2580 OG1 THR A 335 -2.433 -64.190 34.850 1.00 54.43 O ANISOU 2580 OG1 THR A 335 7873 7393 5413 -2131 -222 856 O ATOM 2581 N ALA A 336 0.256 -60.801 34.010 1.00 41.75 N ANISOU 2581 N ALA A 336 5949 5747 4166 -1387 -665 423 N ATOM 2582 CA ALA A 336 1.541 -60.242 33.630 1.00 40.09 C ANISOU 2582 CA ALA A 336 5662 5416 4154 -1239 -875 396 C ATOM 2583 C ALA A 336 2.421 -61.347 33.049 1.00 40.17 C ANISOU 2583 C ALA A 336 5671 5248 4345 -1180 -1007 543 C ATOM 2584 O ALA A 336 3.073 -61.153 32.017 1.00 38.75 O ANISOU 2584 O ALA A 336 5307 5008 4409 -1056 -1038 516 O ATOM 2585 CB ALA A 336 2.210 -59.568 34.833 1.00 40.47 C ANISOU 2585 CB ALA A 336 5856 5493 4029 -1228 -1060 359 C ATOM 2586 N GLU A 337 2.415 -62.506 33.702 1.00 46.58 N ANISOU 2586 N GLU A 337 6709 5970 5019 -1250 -1065 704 N ATOM 2587 CA GLU A 337 3.289 -63.605 33.300 1.00 47.41 C ANISOU 2587 CA GLU A 337 6876 5864 5271 -1130 -1218 837 C ATOM 2588 C GLU A 337 2.964 -64.192 31.908 1.00 47.56 C ANISOU 2588 C GLU A 337 6802 5772 5496 -1090 -1097 789 C ATOM 2589 O GLU A 337 3.865 -64.579 31.141 1.00 47.33 O ANISOU 2589 O GLU A 337 6699 5625 5659 -885 -1184 798 O ATOM 2590 CB GLU A 337 3.283 -64.716 34.345 1.00 49.30 C ANISOU 2590 CB GLU A 337 7461 5975 5296 -1204 -1319 1044 C ATOM 2591 CG GLU A 337 4.109 -65.928 33.925 1.00 50.25 C ANISOU 2591 CG GLU A 337 7702 5821 5570 -1025 -1484 1177 C ATOM 2592 CD GLU A 337 4.181 -67.005 34.992 1.00 52.04 C ANISOU 2592 CD GLU A 337 8333 5863 5575 -1068 -1621 1422 C ATOM 2593 OE1 GLU A 337 4.613 -66.698 36.125 1.00 52.63 O ANISOU 2593 OE1 GLU A 337 8522 6044 5431 -1044 -1785 1508 O ATOM 2594 OE2 GLU A 337 3.817 -68.167 34.694 1.00 53.09 O1- ANISOU 2594 OE2 GLU A 337 8711 5722 5740 -1128 -1584 1531 O1- ATOM 2595 N ARG A 338 1.680 -64.266 31.585 1.00 56.74 N ANISOU 2595 N ARG A 338 7956 6998 6603 -1273 -901 724 N ATOM 2596 CA ARG A 338 1.285 -64.798 30.287 1.00 56.07 C ANISOU 2596 CA ARG A 338 7809 6824 6672 -1259 -828 646 C ATOM 2597 C ARG A 338 1.618 -63.819 29.166 1.00 53.80 C ANISOU 2597 C ARG A 338 7253 6649 6540 -1071 -784 505 C ATOM 2598 O ARG A 338 2.113 -64.205 28.108 1.00 54.28 O ANISOU 2598 O ARG A 338 7278 6611 6734 -910 -800 469 O ATOM 2599 CB ARG A 338 -0.198 -65.171 30.277 1.00 55.86 C ANISOU 2599 CB ARG A 338 7801 6871 6554 -1544 -671 617 C ATOM 2600 CG ARG A 338 -0.445 -66.487 30.955 1.00 57.78 C ANISOU 2600 CG ARG A 338 8355 6896 6702 -1760 -705 790 C ATOM 2601 CD ARG A 338 0.471 -67.529 30.356 1.00 58.73 C ANISOU 2601 CD ARG A 338 8684 6665 6967 -1581 -874 833 C ATOM 2602 NE ARG A 338 0.490 -68.737 31.164 1.00 60.37 N ANISOU 2602 NE ARG A 338 9277 6582 7079 -1728 -957 1044 N ATOM 2603 CZ ARG A 338 -0.343 -69.756 30.987 1.00 61.20 C ANISOU 2603 CZ ARG A 338 9590 6472 7190 -2020 -917 1088 C ATOM 2604 NH1 ARG A 338 -1.244 -69.706 30.019 1.00 60.56 N1+ ANISOU 2604 NH1 ARG A 338 9325 6477 7206 -2182 -824 906 N1+ ATOM 2605 NH2 ARG A 338 -0.276 -70.823 31.776 1.00 62.73 N ANISOU 2605 NH2 ARG A 338 10191 6354 7291 -2164 -993 1323 N ATOM 2606 N ILE A 339 1.360 -62.546 29.413 1.00 37.86 N ANISOU 2606 N ILE A 339 5082 4821 4480 -1079 -719 432 N ATOM 2607 CA ILE A 339 1.750 -61.533 28.458 1.00 35.78 C ANISOU 2607 CA ILE A 339 4619 4625 4352 -922 -683 350 C ATOM 2608 C ILE A 339 3.258 -61.621 28.192 1.00 36.01 C ANISOU 2608 C ILE A 339 4585 4562 4533 -754 -797 426 C ATOM 2609 O ILE A 339 3.688 -61.790 27.044 1.00 36.11 O ANISOU 2609 O ILE A 339 4505 4552 4662 -605 -746 411 O ATOM 2610 CB ILE A 339 1.309 -60.138 28.923 1.00 34.35 C ANISOU 2610 CB ILE A 339 4360 4584 4105 -946 -629 268 C ATOM 2611 CG1 ILE A 339 -0.189 -60.181 29.246 1.00 35.00 C ANISOU 2611 CG1 ILE A 339 4447 4817 4034 -1069 -494 196 C ATOM 2612 CG2 ILE A 339 1.641 -59.100 27.861 1.00 32.66 C ANISOU 2612 CG2 ILE A 339 3996 4382 4030 -808 -586 223 C ATOM 2613 CD1 ILE A 339 -0.839 -58.819 29.524 1.00 35.20 C ANISOU 2613 CD1 ILE A 339 4395 4989 3988 -1005 -409 72 C ATOM 2614 N THR A 340 4.058 -61.553 29.249 1.00 35.52 N ANISOU 2614 N THR A 340 4562 4482 4454 -764 -951 503 N ATOM 2615 CA THR A 340 5.508 -61.664 29.095 1.00 35.67 C ANISOU 2615 CA THR A 340 4443 4472 4637 -606 -1082 579 C ATOM 2616 C THR A 340 5.883 -62.904 28.271 1.00 37.33 C ANISOU 2616 C THR A 340 4688 4565 4931 -415 -1065 615 C ATOM 2617 O THR A 340 6.704 -62.834 27.340 1.00 37.03 O ANISOU 2617 O THR A 340 4455 4571 5046 -230 -1011 613 O ATOM 2618 CB THR A 340 6.228 -61.688 30.475 1.00 36.20 C ANISOU 2618 CB THR A 340 4576 4543 4634 -639 -1322 659 C ATOM 2619 CG2 THR A 340 7.717 -61.886 30.310 1.00 36.38 C ANISOU 2619 CG2 THR A 340 4380 4589 4853 -458 -1482 738 C ATOM 2620 OG1 THR A 340 6.000 -60.442 31.142 1.00 35.21 O ANISOU 2620 OG1 THR A 340 4439 4510 4431 -788 -1350 577 O ATOM 2621 N GLU A 341 5.268 -64.032 28.600 1.00 45.54 N ANISOU 2621 N GLU A 341 5996 5447 5859 -463 -1094 645 N ATOM 2622 CA GLU A 341 5.635 -65.294 27.956 1.00 47.38 C ANISOU 2622 CA GLU A 341 6358 5485 6158 -266 -1120 659 C ATOM 2623 C GLU A 341 5.335 -65.256 26.451 1.00 47.54 C ANISOU 2623 C GLU A 341 6295 5532 6237 -170 -948 521 C ATOM 2624 O GLU A 341 6.147 -65.689 25.631 1.00 48.01 O ANISOU 2624 O GLU A 341 6297 5554 6390 104 -924 494 O ATOM 2625 CB GLU A 341 4.931 -66.482 28.637 1.00 49.18 C ANISOU 2625 CB GLU A 341 6958 5472 6255 -408 -1192 733 C ATOM 2626 CG GLU A 341 5.212 -67.826 27.983 1.00 51.13 C ANISOU 2626 CG GLU A 341 7435 5424 6570 -211 -1242 722 C ATOM 2627 CD GLU A 341 4.335 -68.950 28.541 1.00 52.48 C ANISOU 2627 CD GLU A 341 8014 5301 6626 -448 -1292 803 C ATOM 2628 OE1 GLU A 341 3.079 -68.866 28.425 1.00 52.23 O ANISOU 2628 OE1 GLU A 341 8013 5313 6517 -775 -1171 742 O ATOM 2629 OE2 GLU A 341 4.910 -69.925 29.090 1.00 53.50 O1- ANISOU 2629 OE2 GLU A 341 8425 5154 6749 -307 -1458 942 O1- ATOM 2630 N PHE A 342 4.164 -64.731 26.106 1.00 34.21 N ANISOU 2630 N PHE A 342 4596 3936 4467 -366 -831 429 N ATOM 2631 CA PHE A 342 3.804 -64.471 24.724 1.00 34.32 C ANISOU 2631 CA PHE A 342 4528 4027 4485 -283 -698 304 C ATOM 2632 C PHE A 342 4.874 -63.624 24.038 1.00 32.26 C ANISOU 2632 C PHE A 342 4016 3916 4324 -74 -610 333 C ATOM 2633 O PHE A 342 5.379 -63.983 22.971 1.00 33.13 O ANISOU 2633 O PHE A 342 4106 4030 4453 151 -527 287 O ATOM 2634 CB PHE A 342 2.452 -63.761 24.678 1.00 32.29 C ANISOU 2634 CB PHE A 342 4224 3911 4132 -500 -626 229 C ATOM 2635 CG PHE A 342 2.045 -63.277 23.302 1.00 31.81 C ANISOU 2635 CG PHE A 342 4073 3972 4042 -398 -527 120 C ATOM 2636 CD1 PHE A 342 1.947 -64.159 22.235 1.00 34.84 C ANISOU 2636 CD1 PHE A 342 4585 4268 4384 -288 -532 11 C ATOM 2637 CD2 PHE A 342 1.718 -61.946 23.092 1.00 29.02 C ANISOU 2637 CD2 PHE A 342 3557 3797 3672 -398 -450 121 C ATOM 2638 CE1 PHE A 342 1.555 -63.722 20.990 1.00 34.80 C ANISOU 2638 CE1 PHE A 342 4532 4397 4292 -182 -466 -86 C ATOM 2639 CE2 PHE A 342 1.323 -61.496 21.834 1.00 28.99 C ANISOU 2639 CE2 PHE A 342 3510 3902 3603 -281 -381 54 C ATOM 2640 CZ PHE A 342 1.243 -62.383 20.789 1.00 31.69 C ANISOU 2640 CZ PHE A 342 3966 4201 3874 -176 -391 -46 C ATOM 2641 N CYS A 343 5.235 -62.499 24.651 1.00 36.38 N ANISOU 2641 N CYS A 343 4361 4560 4902 -163 -620 408 N ATOM 2642 CA CYS A 343 6.224 -61.620 24.023 1.00 34.93 C ANISOU 2642 CA CYS A 343 3924 4511 4837 -53 -525 467 C ATOM 2643 C CYS A 343 7.512 -62.356 23.712 1.00 36.30 C ANISOU 2643 C CYS A 343 3973 4694 5124 196 -527 521 C ATOM 2644 O CYS A 343 8.011 -62.302 22.597 1.00 36.77 O ANISOU 2644 O CYS A 343 3910 4855 5206 377 -358 518 O ATOM 2645 CB CYS A 343 6.485 -60.393 24.890 1.00 33.10 C ANISOU 2645 CB CYS A 343 3565 4339 4671 -234 -593 528 C ATOM 2646 SG CYS A 343 5.083 -59.239 24.888 1.00 31.53 S ANISOU 2646 SG CYS A 343 3468 4160 4353 -400 -522 445 S ATOM 2647 N HIS A 344 8.037 -63.068 24.703 1.00 43.78 N ANISOU 2647 N HIS A 344 4962 5554 6119 239 -714 573 N ATOM 2648 CA HIS A 344 9.244 -63.877 24.494 1.00 45.40 C ANISOU 2648 CA HIS A 344 5042 5769 6439 550 -747 616 C ATOM 2649 C HIS A 344 9.112 -64.968 23.417 1.00 47.45 C ANISOU 2649 C HIS A 344 5488 5911 6632 829 -632 505 C ATOM 2650 O HIS A 344 10.021 -65.164 22.610 1.00 48.42 O ANISOU 2650 O HIS A 344 5424 6153 6822 1127 -501 496 O ATOM 2651 CB HIS A 344 9.703 -64.465 25.817 1.00 46.06 C ANISOU 2651 CB HIS A 344 5196 5754 6550 571 -1019 703 C ATOM 2652 CG HIS A 344 10.308 -63.443 26.727 1.00 44.88 C ANISOU 2652 CG HIS A 344 4793 5773 6488 394 -1163 788 C ATOM 2653 CD2 HIS A 344 11.113 -62.390 26.446 1.00 44.04 C ANISOU 2653 CD2 HIS A 344 4304 5887 6544 330 -1106 828 C ATOM 2654 ND1 HIS A 344 10.093 -63.426 28.082 1.00 44.91 N ANISOU 2654 ND1 HIS A 344 4959 5711 6393 231 -1399 835 N ATOM 2655 CE1 HIS A 344 10.757 -62.403 28.610 1.00 44.22 C ANISOU 2655 CE1 HIS A 344 4610 5791 6400 90 -1518 865 C ATOM 2656 NE2 HIS A 344 11.376 -61.764 27.643 1.00 43.65 N ANISOU 2656 NE2 HIS A 344 4198 5877 6509 121 -1348 868 N ATOM 2657 N ARG A 345 7.980 -65.666 23.410 1.00 42.88 N ANISOU 2657 N ARG A 345 5271 5107 5913 720 -677 410 N ATOM 2658 CA ARG A 345 7.755 -66.734 22.451 1.00 45.22 C ANISOU 2658 CA ARG A 345 5820 5230 6131 937 -623 263 C ATOM 2659 C ARG A 345 7.637 -66.140 21.050 1.00 45.12 C ANISOU 2659 C ARG A 345 5693 5416 6034 1026 -392 165 C ATOM 2660 O ARG A 345 7.876 -66.814 20.047 1.00 46.63 O ANISOU 2660 O ARG A 345 6004 5564 6148 1312 -298 34 O ATOM 2661 CB ARG A 345 6.510 -67.540 22.815 1.00 46.62 C ANISOU 2661 CB ARG A 345 6390 5123 6202 696 -748 193 C ATOM 2662 CG ARG A 345 6.736 -68.534 23.943 1.00 47.62 C ANISOU 2662 CG ARG A 345 6763 4965 6364 703 -955 300 C ATOM 2663 CD ARG A 345 6.051 -69.877 23.666 1.00 49.85 C ANISOU 2663 CD ARG A 345 7503 4855 6581 675 -1038 192 C ATOM 2664 NE ARG A 345 6.357 -70.382 22.329 1.00 51.52 N ANISOU 2664 NE ARG A 345 7806 4999 6771 999 -951 -11 N ATOM 2665 CZ ARG A 345 5.846 -71.493 21.797 1.00 53.41 C ANISOU 2665 CZ ARG A 345 8459 4885 6948 1017 -1026 -178 C ATOM 2666 NH1 ARG A 345 4.992 -72.244 22.486 1.00 53.86 N1+ ANISOU 2666 NH1 ARG A 345 8861 4610 6994 680 -1181 -133 N1+ ATOM 2667 NH2 ARG A 345 6.189 -71.855 20.566 1.00 54.73 N ANISOU 2667 NH2 ARG A 345 8717 5027 7052 1355 -939 -394 N ATOM 2668 N PHE A 346 7.265 -64.866 20.990 1.00 39.54 N ANISOU 2668 N PHE A 346 4795 4913 5315 804 -306 227 N ATOM 2669 CA PHE A 346 7.202 -64.185 19.724 1.00 39.14 C ANISOU 2669 CA PHE A 346 4654 5054 5162 885 -94 193 C ATOM 2670 C PHE A 346 8.616 -63.892 19.284 1.00 38.91 C ANISOU 2670 C PHE A 346 4317 5231 5234 1127 85 298 C ATOM 2671 O PHE A 346 8.974 -64.126 18.125 1.00 39.93 O ANISOU 2671 O PHE A 346 4450 5471 5248 1391 282 237 O ATOM 2672 CB PHE A 346 6.413 -62.883 19.829 1.00 36.60 C ANISOU 2672 CB PHE A 346 4254 4844 4808 608 -71 254 C ATOM 2673 CG PHE A 346 6.764 -61.885 18.762 1.00 35.52 C ANISOU 2673 CG PHE A 346 3966 4915 4616 687 150 332 C ATOM 2674 CD1 PHE A 346 6.398 -62.105 17.429 1.00 36.73 C ANISOU 2674 CD1 PHE A 346 4269 5137 4550 865 274 234 C ATOM 2675 CD2 PHE A 346 7.493 -60.745 19.074 1.00 33.75 C ANISOU 2675 CD2 PHE A 346 3479 4805 4540 570 226 513 C ATOM 2676 CE1 PHE A 346 6.744 -61.200 16.444 1.00 36.26 C ANISOU 2676 CE1 PHE A 346 4111 5271 4394 942 497 350 C ATOM 2677 CE2 PHE A 346 7.829 -59.827 18.079 1.00 33.86 C ANISOU 2677 CE2 PHE A 346 3388 4978 4500 602 451 633 C ATOM 2678 CZ PHE A 346 7.455 -60.054 16.776 1.00 35.00 C ANISOU 2678 CZ PHE A 346 3694 5203 4400 797 599 569 C ATOM 2679 N LEU A 347 9.425 -63.375 20.207 1.00 48.76 N ANISOU 2679 N LEU A 347 5283 6560 6684 1030 17 451 N ATOM 2680 CA LEU A 347 10.775 -62.956 19.851 1.00 49.08 C ANISOU 2680 CA LEU A 347 4926 6856 6865 1182 187 577 C ATOM 2681 C LEU A 347 11.644 -64.117 19.385 1.00 51.62 C ANISOU 2681 C LEU A 347 5203 7212 7196 1626 262 504 C ATOM 2682 O LEU A 347 12.615 -63.922 18.672 1.00 52.39 O ANISOU 2682 O LEU A 347 4988 7580 7339 1834 503 567 O ATOM 2683 CB LEU A 347 11.413 -62.200 21.001 1.00 47.74 C ANISOU 2683 CB LEU A 347 4461 6758 6918 945 30 725 C ATOM 2684 CG LEU A 347 10.641 -60.891 21.157 1.00 45.55 C ANISOU 2684 CG LEU A 347 4242 6456 6611 576 33 774 C ATOM 2685 CD1 LEU A 347 10.894 -60.199 22.495 1.00 44.34 C ANISOU 2685 CD1 LEU A 347 3966 6270 6611 295 -203 844 C ATOM 2686 CD2 LEU A 347 10.955 -59.987 19.967 1.00 45.56 C ANISOU 2686 CD2 LEU A 347 4078 6643 6590 563 333 879 C ATOM 2687 N GLU A 348 11.269 -65.332 19.756 1.00 75.04 N ANISOU 2687 N GLU A 348 10759 10500 7254 2732 -2201 -855 N ATOM 2688 CA GLU A 348 12.032 -66.505 19.354 1.00 75.73 C ANISOU 2688 CA GLU A 348 10866 10542 7365 2835 -2267 -821 C ATOM 2689 C GLU A 348 11.616 -67.040 17.984 1.00 72.21 C ANISOU 2689 C GLU A 348 10349 9997 7091 2669 -2096 -719 C ATOM 2690 O GLU A 348 12.269 -67.938 17.447 1.00 72.31 O ANISOU 2690 O GLU A 348 10346 9970 7160 2731 -2139 -706 O ATOM 2691 CB GLU A 348 11.902 -67.606 20.410 1.00 79.21 C ANISOU 2691 CB GLU A 348 11600 10957 7539 3032 -2320 -686 C ATOM 2692 CG GLU A 348 12.258 -67.135 21.799 1.00 83.27 C ANISOU 2692 CG GLU A 348 12216 11571 7852 3212 -2491 -777 C ATOM 2693 CD GLU A 348 12.236 -68.255 22.806 1.00 87.01 C ANISOU 2693 CD GLU A 348 12990 12015 8055 3424 -2551 -643 C ATOM 2694 OE1 GLU A 348 12.762 -69.338 22.478 1.00 87.66 O ANISOU 2694 OE1 GLU A 348 13124 12036 8149 3519 -2596 -585 O ATOM 2695 OE2 GLU A 348 11.692 -68.061 23.918 1.00 89.55 O1- ANISOU 2695 OE2 GLU A 348 13507 12371 8147 3499 -2550 -593 O1- ATOM 2696 N GLY A 349 10.542 -66.494 17.420 1.00 41.84 N ANISOU 2696 N GLY A 349 6460 6115 3323 2467 -1911 -654 N ATOM 2697 CA GLY A 349 9.971 -67.041 16.200 1.00 38.80 C ANISOU 2697 CA GLY A 349 6038 5634 3069 2313 -1745 -544 C ATOM 2698 C GLY A 349 9.092 -68.266 16.463 1.00 39.29 C ANISOU 2698 C GLY A 349 6343 5602 2984 2331 -1638 -332 C ATOM 2699 O GLY A 349 8.709 -68.982 15.532 1.00 37.44 O ANISOU 2699 O GLY A 349 6110 5277 2838 2234 -1525 -235 O ATOM 2700 N LYS A 350 8.773 -68.505 17.736 1.00 56.15 N ANISOU 2700 N LYS A 350 8691 7755 4890 2453 -1670 -262 N ATOM 2701 CA LYS A 350 7.982 -69.668 18.126 1.00 57.37 C ANISOU 2701 CA LYS A 350 9097 7815 4886 2477 -1564 -56 C ATOM 2702 C LYS A 350 6.473 -69.461 18.028 1.00 55.96 C ANISOU 2702 C LYS A 350 8972 7599 4692 2291 -1348 72 C ATOM 2703 O LYS A 350 5.704 -70.429 18.045 1.00 56.30 O ANISOU 2703 O LYS A 350 9181 7546 4663 2252 -1221 245 O ATOM 2704 CB LYS A 350 8.371 -70.119 19.527 1.00 61.61 C ANISOU 2704 CB LYS A 350 9859 8381 5169 2705 -1691 -27 C ATOM 2705 CG LYS A 350 9.692 -70.878 19.584 1.00 63.62 C ANISOU 2705 CG LYS A 350 10129 8632 5413 2909 -1882 -87 C ATOM 2706 CD LYS A 350 10.272 -70.904 21.015 1.00 68.02 C ANISOU 2706 CD LYS A 350 10853 9261 5729 3153 -2061 -126 C ATOM 2707 CE LYS A 350 9.194 -71.150 22.095 1.00 70.28 C ANISOU 2707 CE LYS A 350 11421 9521 5760 3174 -1947 43 C ATOM 2708 NZ LYS A 350 8.535 -72.498 22.002 1.00 70.66 N1+ ANISOU 2708 NZ LYS A 350 11696 9422 5728 3160 -1802 271 N1+ ATOM 2709 N ILE A 351 6.039 -68.206 17.918 1.00 47.22 N ANISOU 2709 N ILE A 351 7721 6563 3657 2173 -1305 -15 N ATOM 2710 CA ILE A 351 4.621 -67.930 17.703 1.00 45.66 C ANISOU 2710 CA ILE A 351 7537 6341 3470 1990 -1106 86 C ATOM 2711 C ILE A 351 4.326 -67.864 16.218 1.00 42.11 C ANISOU 2711 C ILE A 351 6907 5836 3256 1808 -1009 83 C ATOM 2712 O ILE A 351 5.010 -67.156 15.484 1.00 40.20 O ANISOU 2712 O ILE A 351 6465 5628 3181 1777 -1077 -54 O ATOM 2713 CB ILE A 351 4.174 -66.614 18.342 1.00 45.97 C ANISOU 2713 CB ILE A 351 7530 6480 3457 1958 -1097 2 C ATOM 2714 CG1 ILE A 351 4.345 -66.665 19.855 1.00 49.58 C ANISOU 2714 CG1 ILE A 351 8187 6997 3653 2137 -1182 9 C ATOM 2715 CG2 ILE A 351 2.697 -66.345 18.013 1.00 44.31 C ANISOU 2715 CG2 ILE A 351 7312 6249 3275 1765 -888 98 C ATOM 2716 CD1 ILE A 351 3.293 -67.521 20.507 1.00 51.22 C ANISOU 2716 CD1 ILE A 351 8635 7154 3671 2127 -1028 206 C ATOM 2717 N LYS A 352 3.325 -68.631 15.791 1.00 66.81 N ANISOU 2717 N LYS A 352 10113 8879 6393 1691 -850 233 N ATOM 2718 CA LYS A 352 2.892 -68.666 14.392 1.00 63.85 C ANISOU 2718 CA LYS A 352 9591 8447 6220 1518 -751 244 C ATOM 2719 C LYS A 352 1.786 -67.645 14.107 1.00 62.12 C ANISOU 2719 C LYS A 352 9267 8270 6066 1351 -629 232 C ATOM 2720 O LYS A 352 0.894 -67.420 14.927 1.00 63.36 O ANISOU 2720 O LYS A 352 9520 8459 6093 1327 -545 292 O ATOM 2721 CB LYS A 352 2.386 -70.065 14.017 1.00 64.08 C ANISOU 2721 CB LYS A 352 9751 8354 6240 1476 -653 401 C ATOM 2722 CG LYS A 352 0.945 -70.327 14.479 1.00 64.87 C ANISOU 2722 CG LYS A 352 9974 8427 6245 1366 -478 545 C ATOM 2723 CD LYS A 352 0.472 -71.727 14.111 1.00 65.13 C ANISOU 2723 CD LYS A 352 10135 8326 6286 1316 -380 696 C ATOM 2724 CE LYS A 352 1.410 -72.787 14.666 1.00 67.48 C ANISOU 2724 CE LYS A 352 10611 8558 6471 1502 -483 745 C ATOM 2725 NZ LYS A 352 0.805 -74.134 14.480 1.00 68.24 N1+ ANISOU 2725 NZ LYS A 352 10864 8509 6556 1447 -368 909 N1+ ATOM 2726 N PRO A 353 1.828 -67.042 12.939 1.00 45.91 N ANISOU 2726 N PRO A 353 7023 6217 4205 1239 -613 156 N ATOM 2727 CA PRO A 353 0.954 -65.923 12.603 1.00 44.20 C ANISOU 2727 CA PRO A 353 6688 6043 4063 1103 -527 118 C ATOM 2728 C PRO A 353 -0.522 -66.223 12.727 1.00 44.31 C ANISOU 2728 C PRO A 353 6778 6036 4020 983 -364 242 C ATOM 2729 O PRO A 353 -0.932 -67.350 12.583 1.00 44.61 O ANISOU 2729 O PRO A 353 6915 6001 4033 952 -293 360 O ATOM 2730 CB PRO A 353 1.314 -65.642 11.161 1.00 41.24 C ANISOU 2730 CB PRO A 353 6134 5638 3898 1015 -531 52 C ATOM 2731 CG PRO A 353 2.706 -66.098 11.047 1.00 41.71 C ANISOU 2731 CG PRO A 353 6179 5687 3983 1139 -660 -12 C ATOM 2732 CD PRO A 353 2.781 -67.329 11.871 1.00 44.22 C ANISOU 2732 CD PRO A 353 6695 5964 4142 1249 -681 92 C ATOM 2733 N HIS A 354 -1.311 -65.199 12.989 1.00 54.33 N ANISOU 2733 N HIS A 354 7996 7370 5278 914 -302 206 N ATOM 2734 CA HIS A 354 -2.723 -65.371 13.164 1.00 54.27 C ANISOU 2734 CA HIS A 354 8038 7364 5218 800 -142 302 C ATOM 2735 C HIS A 354 -3.505 -64.978 11.944 1.00 51.30 C ANISOU 2735 C HIS A 354 7508 6971 5013 639 -61 286 C ATOM 2736 O HIS A 354 -3.345 -63.869 11.425 1.00 49.33 O ANISOU 2736 O HIS A 354 7121 6752 4869 611 -100 180 O ATOM 2737 CB HIS A 354 -3.169 -64.566 14.360 1.00 55.66 C ANISOU 2737 CB HIS A 354 8277 7629 5243 843 -117 273 C ATOM 2738 CG HIS A 354 -4.626 -64.660 14.635 1.00 55.80 C ANISOU 2738 CG HIS A 354 8334 7666 5199 731 60 357 C ATOM 2739 CD2 HIS A 354 -5.572 -63.685 14.819 1.00 54.98 C ANISOU 2739 CD2 HIS A 354 8168 7632 5088 658 149 310 C ATOM 2740 ND1 HIS A 354 -5.257 -65.824 14.738 1.00 56.63 N ANISOU 2740 ND1 HIS A 354 8545 7721 5252 681 172 497 N ATOM 2741 CE1 HIS A 354 -6.540 -65.606 14.985 1.00 56.29 C ANISOU 2741 CE1 HIS A 354 8491 7723 5173 577 328 536 C ATOM 2742 NE2 HIS A 354 -6.731 -64.295 15.034 1.00 55.42 N ANISOU 2742 NE2 HIS A 354 8280 7690 5088 567 312 417 N ATOM 2743 N LEU A 355 -4.307 -65.908 11.443 1.00 60.51 N ANISOU 2743 N LEU A 355 8699 8080 6212 538 45 390 N ATOM 2744 CA LEU A 355 -5.026 -65.698 10.199 1.00 57.81 C ANISOU 2744 CA LEU A 355 8216 7719 6030 394 107 376 C ATOM 2745 C LEU A 355 -6.520 -65.605 10.441 1.00 57.66 C ANISOU 2745 C LEU A 355 8188 7741 5979 280 256 427 C ATOM 2746 O LEU A 355 -7.061 -66.271 11.320 1.00 59.45 O ANISOU 2746 O LEU A 355 8537 7971 6081 283 345 524 O ATOM 2747 CB LEU A 355 -4.720 -66.824 9.211 1.00 57.19 C ANISOU 2747 CB LEU A 355 8138 7545 6048 365 95 429 C ATOM 2748 CG LEU A 355 -3.239 -67.108 8.961 1.00 57.91 C ANISOU 2748 CG LEU A 355 8239 7596 6168 483 -39 382 C ATOM 2749 CD1 LEU A 355 -3.065 -68.199 7.917 1.00 57.25 C ANISOU 2749 CD1 LEU A 355 8157 7415 6180 447 -34 427 C ATOM 2750 CD2 LEU A 355 -2.506 -65.843 8.546 1.00 56.35 C ANISOU 2750 CD2 LEU A 355 7900 7450 6058 510 -127 246 C ATOM 2751 N MET A 356 -7.181 -64.770 9.651 1.00 58.62 N ANISOU 2751 N MET A 356 8166 7892 6214 183 288 360 N ATOM 2752 CA MET A 356 -8.616 -64.586 9.766 1.00 58.82 C ANISOU 2752 CA MET A 356 8146 7971 6231 77 423 383 C ATOM 2753 C MET A 356 -9.249 -64.552 8.385 1.00 56.65 C ANISOU 2753 C MET A 356 7723 7680 6123 -36 441 361 C ATOM 2754 O MET A 356 -8.605 -64.188 7.405 1.00 54.86 O ANISOU 2754 O MET A 356 7427 7412 6007 -34 352 295 O ATOM 2755 CB MET A 356 -8.933 -63.297 10.524 1.00 59.08 C ANISOU 2755 CB MET A 356 8168 8084 6197 105 444 297 C ATOM 2756 CG MET A 356 -8.835 -62.041 9.678 1.00 56.91 C ANISOU 2756 CG MET A 356 7770 7796 6056 87 388 175 C ATOM 2757 SD MET A 356 -8.819 -60.537 10.666 1.00 57.65 S ANISOU 2757 SD MET A 356 7878 7952 6073 175 375 73 S ATOM 2758 CE MET A 356 -7.923 -59.432 9.582 1.00 54.96 C ANISOU 2758 CE MET A 356 7418 7558 5909 212 242 -27 C ATOM 2759 N SER A 357 -10.523 -64.915 8.330 1.00 51.33 N ANISOU 2759 N SER A 357 6995 7045 5464 -123 558 419 N ATOM 2760 CA SER A 357 -11.277 -64.888 7.091 1.00 49.77 C ANISOU 2760 CA SER A 357 6638 6837 5438 -182 562 403 C ATOM 2761 C SER A 357 -12.757 -64.729 7.387 1.00 50.64 C ANISOU 2761 C SER A 357 6665 7020 5557 -226 686 433 C ATOM 2762 O SER A 357 -13.281 -65.347 8.310 1.00 52.85 O ANISOU 2762 O SER A 357 7024 7327 5731 -261 805 521 O ATOM 2763 CB SER A 357 -11.052 -66.179 6.305 1.00 47.96 C ANISOU 2763 CB SER A 357 6434 6507 5281 -201 558 491 C ATOM 2764 OG SER A 357 -12.283 -66.816 6.021 1.00 49.01 O ANISOU 2764 OG SER A 357 6517 6618 5486 -277 668 564 O ATOM 2765 N GLN A 358 -13.431 -63.900 6.601 1.00 50.87 N ANISOU 2765 N GLN A 358 6541 7071 5715 -185 670 385 N ATOM 2766 CA GLN A 358 -14.875 -63.808 6.689 1.00 51.99 C ANISOU 2766 CA GLN A 358 6604 7244 5907 -195 801 429 C ATOM 2767 C GLN A 358 -15.415 -65.158 6.253 1.00 52.93 C ANISOU 2767 C GLN A 358 6732 7288 6093 -311 879 520 C ATOM 2768 O GLN A 358 -14.643 -66.077 5.988 1.00 52.73 O ANISOU 2768 O GLN A 358 6791 7182 6061 -342 834 559 O ATOM 2769 CB GLN A 358 -15.402 -62.707 5.775 1.00 50.49 C ANISOU 2769 CB GLN A 358 6361 6937 5885 -115 819 357 C ATOM 2770 CG GLN A 358 -14.627 -61.405 5.860 1.00 48.99 C ANISOU 2770 CG GLN A 358 6278 6645 5690 -45 776 230 C ATOM 2771 CD GLN A 358 -14.955 -60.459 4.723 1.00 47.52 C ANISOU 2771 CD GLN A 358 5971 6473 5613 -92 705 140 C ATOM 2772 NE2 GLN A 358 -15.888 -59.549 4.962 1.00 48.17 N ANISOU 2772 NE2 GLN A 358 5984 6610 5709 -81 765 99 N ATOM 2773 OE1 GLN A 358 -14.375 -60.546 3.643 1.00 45.97 O ANISOU 2773 OE1 GLN A 358 5742 6244 5482 -124 584 109 O ATOM 2774 N GLU A 359 -16.732 -65.286 6.175 1.00 62.21 N ANISOU 2774 N GLU A 359 7815 8483 7340 -379 996 550 N ATOM 2775 CA GLU A 359 -17.326 -66.534 5.718 1.00 63.50 C ANISOU 2775 CA GLU A 359 7964 8573 7590 -515 1066 623 C ATOM 2776 C GLU A 359 -17.508 -66.499 4.209 1.00 61.79 C ANISOU 2776 C GLU A 359 7660 8264 7554 -542 981 548 C ATOM 2777 O GLU A 359 -17.884 -65.475 3.648 1.00 60.58 O ANISOU 2777 O GLU A 359 7415 8132 7472 -496 943 462 O ATOM 2778 CB GLU A 359 -18.664 -66.790 6.410 1.00 66.40 C ANISOU 2778 CB GLU A 359 8261 9017 7951 -607 1239 686 C ATOM 2779 CG GLU A 359 -19.361 -65.535 6.901 1.00 66.97 C ANISOU 2779 CG GLU A 359 8236 9216 7995 -529 1287 627 C ATOM 2780 CD GLU A 359 -20.770 -65.812 7.380 1.00 69.99 C ANISOU 2780 CD GLU A 359 8511 9678 8405 -629 1467 679 C ATOM 2781 OE1 GLU A 359 -21.064 -66.979 7.713 1.00 72.14 O ANISOU 2781 OE1 GLU A 359 8830 9912 8667 -756 1572 776 O ATOM 2782 OE2 GLU A 359 -21.583 -64.865 7.425 1.00 70.45 O1- ANISOU 2782 OE2 GLU A 359 8445 9820 8505 -577 1510 624 O1- ATOM 2783 N LEU A 360 -17.229 -67.621 3.556 1.00 66.63 N ANISOU 2783 N LEU A 360 8322 8768 8228 -617 945 569 N ATOM 2784 CA LEU A 360 -17.365 -67.714 2.110 1.00 65.37 C ANISOU 2784 CA LEU A 360 8095 8535 8206 -652 853 486 C ATOM 2785 C LEU A 360 -18.819 -67.561 1.687 1.00 66.54 C ANISOU 2785 C LEU A 360 8091 8723 8469 -738 907 454 C ATOM 2786 O LEU A 360 -19.636 -68.447 1.919 1.00 68.72 O ANISOU 2786 O LEU A 360 8332 8985 8792 -857 1004 514 O ATOM 2787 CB LEU A 360 -16.815 -69.050 1.608 1.00 54.11 C ANISOU 2787 CB LEU A 360 6760 6989 6811 -713 819 520 C ATOM 2788 CG LEU A 360 -16.142 -69.046 0.234 1.00 52.04 C ANISOU 2788 CG LEU A 360 6500 6662 6611 -681 683 428 C ATOM 2789 CD1 LEU A 360 -16.870 -69.972 -0.725 1.00 53.08 C ANISOU 2789 CD1 LEU A 360 6581 6725 6861 -795 678 413 C ATOM 2790 CD2 LEU A 360 -16.071 -67.636 -0.329 1.00 50.12 C ANISOU 2790 CD2 LEU A 360 6188 6483 6374 -597 602 323 C ATOM 2791 N PRO A 361 -19.137 -66.433 1.065 1.00 50.18 N ANISOU 2791 N PRO A 361 5929 6696 6441 -682 843 358 N ATOM 2792 CA PRO A 361 -20.495 -66.194 0.568 1.00 51.38 C ANISOU 2792 CA PRO A 361 5922 6899 6703 -748 871 314 C ATOM 2793 C PRO A 361 -20.864 -67.213 -0.502 1.00 51.97 C ANISOU 2793 C PRO A 361 5958 6904 6886 -857 825 295 C ATOM 2794 O PRO A 361 -19.987 -67.688 -1.221 1.00 50.54 O ANISOU 2794 O PRO A 361 5867 6640 6697 -841 731 276 O ATOM 2795 CB PRO A 361 -20.413 -64.786 -0.030 1.00 50.11 C ANISOU 2795 CB PRO A 361 5724 6776 6542 -645 773 210 C ATOM 2796 CG PRO A 361 -18.962 -64.527 -0.244 1.00 47.75 C ANISOU 2796 CG PRO A 361 5561 6418 6163 -560 670 186 C ATOM 2797 CD PRO A 361 -18.251 -65.282 0.833 1.00 48.28 C ANISOU 2797 CD PRO A 361 5733 6462 6148 -559 741 283 C ATOM 2798 N GLU A 362 -22.145 -67.550 -0.597 1.00 75.04 N ANISOU 2798 N GLU A 362 8740 9863 9910 -966 892 295 N ATOM 2799 CA GLU A 362 -22.601 -68.571 -1.534 1.00 76.15 C ANISOU 2799 CA GLU A 362 8832 9937 10164 -1087 853 275 C ATOM 2800 C GLU A 362 -22.544 -68.105 -2.985 1.00 74.63 C ANISOU 2800 C GLU A 362 8600 9740 10016 -1039 695 166 C ATOM 2801 O GLU A 362 -22.548 -68.921 -3.903 1.00 74.90 O ANISOU 2801 O GLU A 362 8637 9705 10114 -1107 627 141 O ATOM 2802 CB GLU A 362 -24.022 -69.024 -1.185 1.00 76.76 C ANISOU 2802 CB GLU A 362 8752 10065 10349 -1231 974 298 C ATOM 2803 CG GLU A 362 -24.335 -69.008 0.303 1.00 78.52 C ANISOU 2803 CG GLU A 362 8979 10348 10507 -1251 1153 396 C ATOM 2804 CD GLU A 362 -25.603 -69.767 0.644 1.00 82.10 C ANISOU 2804 CD GLU A 362 9298 10825 11071 -1425 1295 435 C ATOM 2805 OE1 GLU A 362 -26.656 -69.119 0.821 1.00 83.58 O ANISOU 2805 OE1 GLU A 362 9308 11131 11317 -1435 1359 398 O ATOM 2806 OE2 GLU A 362 -25.548 -71.011 0.737 1.00 83.63 O1- ANISOU 2806 OE2 GLU A 362 9561 10915 11300 -1554 1347 500 O1- ATOM 2807 N ASP A 363 -22.493 -66.794 -3.188 1.00 63.34 N ANISOU 2807 N ASP A 363 7143 8379 8544 -922 639 106 N ATOM 2808 CA ASP A 363 -22.455 -66.237 -4.535 1.00 62.08 C ANISOU 2808 CA ASP A 363 6962 8224 8403 -866 500 15 C ATOM 2809 C ASP A 363 -21.085 -65.662 -4.883 1.00 59.31 C ANISOU 2809 C ASP A 363 6762 7832 7942 -743 416 -3 C ATOM 2810 O ASP A 363 -20.976 -64.763 -5.713 1.00 58.17 O ANISOU 2810 O ASP A 363 6618 7712 7774 -665 329 -64 O ATOM 2811 CB ASP A 363 -23.531 -65.163 -4.699 1.00 62.88 C ANISOU 2811 CB ASP A 363 6912 8429 8550 -834 492 -46 C ATOM 2812 CG ASP A 363 -23.309 -63.974 -3.789 1.00 62.10 C ANISOU 2812 CG ASP A 363 6838 8384 8372 -730 540 -40 C ATOM 2813 OD1 ASP A 363 -24.044 -62.975 -3.922 1.00 62.63 O ANISOU 2813 OD1 ASP A 363 6802 8529 8466 -679 527 -93 O ATOM 2814 OD2 ASP A 363 -22.398 -64.037 -2.940 1.00 61.06 O1- ANISOU 2814 OD2 ASP A 363 6829 8217 8153 -696 585 14 O1- ATOM 2815 N TRP A 364 -20.043 -66.188 -4.250 1.00 41.63 N ANISOU 2815 N TRP A 364 4648 5534 5635 -730 445 53 N ATOM 2816 CA TRP A 364 -18.694 -65.699 -4.461 1.00 39.34 C ANISOU 2816 CA TRP A 364 4485 5215 5247 -625 375 33 C ATOM 2817 C TRP A 364 -18.271 -65.779 -5.898 1.00 38.23 C ANISOU 2817 C TRP A 364 4375 5041 5108 -597 271 -17 C ATOM 2818 O TRP A 364 -17.648 -64.841 -6.433 1.00 36.56 O ANISOU 2818 O TRP A 364 4212 4846 4832 -506 210 -56 O ATOM 2819 CB TRP A 364 -17.711 -66.462 -3.585 1.00 39.17 C ANISOU 2819 CB TRP A 364 4573 5138 5170 -626 419 101 C ATOM 2820 CG TRP A 364 -17.538 -67.904 -3.989 1.00 40.01 C ANISOU 2820 CG TRP A 364 4719 5160 5323 -704 420 136 C ATOM 2821 CD1 TRP A 364 -18.367 -68.976 -3.686 1.00 42.26 C ANISOU 2821 CD1 TRP A 364 4962 5409 5685 -828 497 191 C ATOM 2822 CD2 TRP A 364 -16.451 -68.480 -4.789 1.00 38.86 C ANISOU 2822 CD2 TRP A 364 4666 4946 5153 -671 346 118 C ATOM 2823 CE2 TRP A 364 -16.738 -69.910 -4.898 1.00 40.54 C ANISOU 2823 CE2 TRP A 364 4893 5073 5438 -777 378 162 C ATOM 2824 CE3 TRP A 364 -15.315 -67.974 -5.400 1.00 36.95 C ANISOU 2824 CE3 TRP A 364 4491 4707 4842 -574 267 73 C ATOM 2825 NE1 TRP A 364 -17.883 -70.137 -4.224 1.00 42.47 N ANISOU 2825 NE1 TRP A 364 5059 5338 5741 -873 466 205 N ATOM 2826 CZ2 TRP A 364 -15.912 -70.771 -5.593 1.00 40.12 C ANISOU 2826 CZ2 TRP A 364 4920 4936 5387 -772 327 155 C ATOM 2827 CZ3 TRP A 364 -14.490 -68.854 -6.098 1.00 36.67 C ANISOU 2827 CZ3 TRP A 364 4522 4604 4805 -570 227 71 C ATOM 2828 CH2 TRP A 364 -14.783 -70.218 -6.192 1.00 38.15 C ANISOU 2828 CH2 TRP A 364 4725 4706 5063 -662 253 108 C ATOM 2829 N ASP A 365 -18.593 -66.893 -6.544 1.00 60.77 N ANISOU 2829 N ASP A 365 7207 7847 8036 -678 257 -12 N ATOM 2830 CA ASP A 365 -18.254 -67.101 -7.957 1.00 60.10 C ANISOU 2830 CA ASP A 365 7148 7730 7958 -658 164 -55 C ATOM 2831 C ASP A 365 -19.323 -66.718 -8.998 1.00 60.92 C ANISOU 2831 C ASP A 365 7142 7878 8126 -680 100 -111 C ATOM 2832 O ASP A 365 -19.188 -67.030 -10.183 1.00 60.85 O ANISOU 2832 O ASP A 365 7148 7841 8130 -680 20 -142 O ATOM 2833 CB ASP A 365 -17.739 -68.521 -8.208 1.00 60.67 C ANISOU 2833 CB ASP A 365 7282 7709 8061 -718 158 -29 C ATOM 2834 CG ASP A 365 -18.773 -69.576 -7.944 1.00 63.21 C ANISOU 2834 CG ASP A 365 7531 7994 8493 -862 200 -5 C ATOM 2835 OD1 ASP A 365 -18.442 -70.771 -8.139 1.00 64.08 O ANISOU 2835 OD1 ASP A 365 7699 8008 8640 -925 195 16 O ATOM 2836 OD2 ASP A 365 -19.904 -69.235 -7.534 1.00 64.56 O1- ANISOU 2836 OD2 ASP A 365 7587 8227 8718 -918 243 -7 O1- ATOM 2837 N LYS A 366 -20.396 -66.083 -8.545 1.00 50.98 N ANISOU 2837 N LYS A 366 5769 6692 6909 -699 132 -125 N ATOM 2838 CA LYS A 366 -21.503 -65.696 -9.421 1.00 52.09 C ANISOU 2838 CA LYS A 366 5784 6891 7116 -718 68 -186 C ATOM 2839 C LYS A 366 -21.154 -64.592 -10.419 1.00 50.66 C ANISOU 2839 C LYS A 366 5643 6735 6871 -604 -15 -227 C ATOM 2840 O LYS A 366 -21.487 -64.694 -11.602 1.00 51.32 O ANISOU 2840 O LYS A 366 5695 6826 6979 -610 -104 -271 O ATOM 2841 CB LYS A 366 -22.699 -65.275 -8.574 1.00 53.88 C ANISOU 2841 CB LYS A 366 5866 7199 7408 -757 138 -192 C ATOM 2842 CG LYS A 366 -23.923 -64.846 -9.359 1.00 55.59 C ANISOU 2842 CG LYS A 366 5924 7495 7704 -770 71 -266 C ATOM 2843 CD LYS A 366 -25.155 -64.823 -8.446 1.00 57.97 C ANISOU 2843 CD LYS A 366 6054 7874 8098 -841 162 -268 C ATOM 2844 CE LYS A 366 -26.345 -64.166 -9.132 1.00 59.64 C ANISOU 2844 CE LYS A 366 6091 8184 8386 -821 91 -353 C ATOM 2845 NZ LYS A 366 -26.493 -64.636 -10.535 1.00 60.24 N1+ ANISOU 2845 NZ LYS A 366 6152 8243 8494 -847 -45 -415 N1+ ATOM 2846 N GLN A 367 -20.507 -63.531 -9.938 1.00 45.76 N ANISOU 2846 N GLN A 367 5093 6126 6166 -508 14 -214 N ATOM 2847 CA GLN A 367 -20.078 -62.428 -10.796 1.00 44.25 C ANISOU 2847 CA GLN A 367 4955 5945 5915 -408 -43 -239 C ATOM 2848 C GLN A 367 -18.820 -62.757 -11.584 1.00 42.65 C ANISOU 2848 C GLN A 367 4877 5677 5649 -373 -71 -218 C ATOM 2849 O GLN A 367 -18.113 -63.721 -11.285 1.00 41.91 O ANISOU 2849 O GLN A 367 4845 5533 5545 -405 -45 -187 O ATOM 2850 CB GLN A 367 -19.818 -61.186 -9.949 1.00 43.57 C ANISOU 2850 CB GLN A 367 4900 5885 5770 -336 0 -236 C ATOM 2851 CG GLN A 367 -21.065 -60.371 -9.631 1.00 45.26 C ANISOU 2851 CG GLN A 367 4982 6176 6037 -325 4 -273 C ATOM 2852 CD GLN A 367 -22.327 -61.205 -9.645 1.00 47.54 C ANISOU 2852 CD GLN A 367 5117 6510 6436 -415 5 -293 C ATOM 2853 NE2 GLN A 367 -23.180 -60.967 -10.637 1.00 48.66 N ANISOU 2853 NE2 GLN A 367 5160 6697 6630 -404 -76 -348 N ATOM 2854 OE1 GLN A 367 -22.531 -62.060 -8.774 1.00 48.46 O ANISOU 2854 OE1 GLN A 367 5201 6621 6592 -498 78 -260 O ATOM 2855 N PRO A 368 -18.543 -61.957 -12.616 1.00 36.21 N ANISOU 2855 N PRO A 368 4095 4864 4798 -305 -122 -234 N ATOM 2856 CA PRO A 368 -17.274 -62.126 -13.346 1.00 35.30 C ANISOU 2856 CA PRO A 368 4091 4696 4627 -268 -129 -208 C ATOM 2857 C PRO A 368 -16.036 -61.917 -12.449 1.00 33.86 C ANISOU 2857 C PRO A 368 4001 4488 4376 -229 -56 -171 C ATOM 2858 O PRO A 368 -15.057 -62.648 -12.594 1.00 33.32 O ANISOU 2858 O PRO A 368 3996 4382 4281 -229 -43 -146 O ATOM 2859 CB PRO A 368 -17.344 -61.068 -14.456 1.00 35.44 C ANISOU 2859 CB PRO A 368 4113 4730 4622 -205 -183 -227 C ATOM 2860 CG PRO A 368 -18.812 -60.848 -14.681 1.00 36.91 C ANISOU 2860 CG PRO A 368 4180 4978 4865 -221 -244 -279 C ATOM 2861 CD PRO A 368 -19.504 -61.103 -13.334 1.00 37.12 C ANISOU 2861 CD PRO A 368 4129 5034 4940 -272 -185 -280 C ATOM 2862 N VAL A 369 -16.067 -60.946 -11.547 1.00 27.48 N ANISOU 2862 N VAL A 369 3198 3706 3536 -198 -19 -174 N ATOM 2863 CA VAL A 369 -15.000 -60.866 -10.562 1.00 26.57 C ANISOU 2863 CA VAL A 369 3163 3578 3354 -177 25 -151 C ATOM 2864 C VAL A 369 -15.373 -61.794 -9.422 1.00 26.99 C ANISOU 2864 C VAL A 369 3188 3638 3428 -236 47 -141 C ATOM 2865 O VAL A 369 -16.386 -61.575 -8.765 1.00 27.71 O ANISOU 2865 O VAL A 369 3205 3765 3560 -267 62 -154 O ATOM 2866 CB VAL A 369 -14.808 -59.447 -9.958 1.00 25.98 C ANISOU 2866 CB VAL A 369 3114 3520 3238 -132 38 -167 C ATOM 2867 CG1 VAL A 369 -13.749 -59.499 -8.886 1.00 24.95 C ANISOU 2867 CG1 VAL A 369 3053 3363 3062 -118 48 -140 C ATOM 2868 CG2 VAL A 369 -14.441 -58.405 -11.026 1.00 25.63 C ANISOU 2868 CG2 VAL A 369 3093 3458 3189 -81 28 -171 C ATOM 2869 N LYS A 370 -14.559 -62.821 -9.193 1.00 35.05 N ANISOU 2869 N LYS A 370 4261 4627 4431 -253 55 -116 N ATOM 2870 CA LYS A 370 -14.760 -63.755 -8.084 1.00 35.69 C ANISOU 2870 CA LYS A 370 4326 4698 4537 -312 85 -94 C ATOM 2871 C LYS A 370 -14.370 -63.131 -6.740 1.00 35.31 C ANISOU 2871 C LYS A 370 4304 4672 4440 -291 103 -87 C ATOM 2872 O LYS A 370 -13.398 -62.357 -6.647 1.00 34.40 O ANISOU 2872 O LYS A 370 4249 4561 4259 -232 75 -99 O ATOM 2873 CB LYS A 370 -13.915 -65.020 -8.290 1.00 35.82 C ANISOU 2873 CB LYS A 370 4395 4664 4552 -331 81 -70 C ATOM 2874 CG LYS A 370 -14.042 -65.691 -9.648 1.00 36.32 C ANISOU 2874 CG LYS A 370 4446 4695 4660 -350 49 -80 C ATOM 2875 CD LYS A 370 -15.499 -65.913 -10.012 1.00 37.50 C ANISOU 2875 CD LYS A 370 4498 4849 4903 -422 36 -100 C ATOM 2876 CE LYS A 370 -15.656 -66.022 -11.525 1.00 37.96 C ANISOU 2876 CE LYS A 370 4541 4891 4991 -419 -32 -129 C ATOM 2877 NZ LYS A 370 -17.074 -66.124 -11.959 1.00 39.27 N1+ ANISOU 2877 NZ LYS A 370 4601 5077 5242 -489 -75 -160 N1+ ATOM 2878 N VAL A 371 -15.109 -63.476 -5.693 1.00 35.86 N ANISOU 2878 N VAL A 371 4322 4754 4550 -344 155 -64 N ATOM 2879 CA VAL A 371 -14.789 -62.978 -4.357 1.00 35.84 C ANISOU 2879 CA VAL A 371 4334 4773 4511 -328 180 -48 C ATOM 2880 C VAL A 371 -14.073 -64.045 -3.519 1.00 36.22 C ANISOU 2880 C VAL A 371 4431 4782 4550 -351 216 6 C ATOM 2881 O VAL A 371 -14.547 -65.182 -3.433 1.00 37.40 O ANISOU 2881 O VAL A 371 4568 4898 4745 -415 272 51 O ATOM 2882 CB VAL A 371 -16.056 -62.521 -3.623 1.00 37.09 C ANISOU 2882 CB VAL A 371 4402 4982 4710 -356 248 -42 C ATOM 2883 CG1 VAL A 371 -15.742 -62.160 -2.171 1.00 37.31 C ANISOU 2883 CG1 VAL A 371 4447 5033 4696 -336 300 -10 C ATOM 2884 CG2 VAL A 371 -16.710 -61.340 -4.351 1.00 36.81 C ANISOU 2884 CG2 VAL A 371 4316 4986 4684 -320 211 -96 C ATOM 2885 N LEU A 372 -12.940 -63.692 -2.911 1.00 30.15 N ANISOU 2885 N LEU A 372 3715 4011 3729 -305 184 7 N ATOM 2886 CA LEU A 372 -12.197 -64.632 -2.065 1.00 30.70 C ANISOU 2886 CA LEU A 372 3838 4043 3783 -309 224 69 C ATOM 2887 C LEU A 372 -12.199 -64.224 -0.587 1.00 31.43 C ANISOU 2887 C LEU A 372 3942 4171 3831 -280 293 117 C ATOM 2888 O LEU A 372 -12.277 -63.023 -0.256 1.00 30.97 O ANISOU 2888 O LEU A 372 3854 4160 3755 -247 273 77 O ATOM 2889 CB LEU A 372 -10.738 -64.735 -2.514 1.00 29.80 C ANISOU 2889 CB LEU A 372 3772 3902 3649 -267 145 45 C ATOM 2890 CG LEU A 372 -10.537 -65.092 -3.971 1.00 29.15 C ANISOU 2890 CG LEU A 372 3701 3800 3577 -266 93 6 C ATOM 2891 CD1 LEU A 372 -9.072 -65.349 -4.274 1.00 28.51 C ANISOU 2891 CD1 LEU A 372 3657 3695 3479 -227 43 -6 C ATOM 2892 CD2 LEU A 372 -11.403 -66.303 -4.308 1.00 30.05 C ANISOU 2892 CD2 LEU A 372 3809 3872 3736 -329 148 41 C ATOM 2893 N VAL A 373 -12.102 -65.216 0.295 1.00 27.72 N ANISOU 2893 N VAL A 373 3527 3683 3323 -283 373 210 N ATOM 2894 CA VAL A 373 -11.906 -64.938 1.703 1.00 28.76 C ANISOU 2894 CA VAL A 373 3701 3868 3359 -220 437 271 C ATOM 2895 C VAL A 373 -10.759 -65.825 2.135 1.00 29.59 C ANISOU 2895 C VAL A 373 3890 3964 3388 -185 406 334 C ATOM 2896 O VAL A 373 -10.233 -66.590 1.323 1.00 29.37 O ANISOU 2896 O VAL A 373 3888 3864 3408 -212 358 324 O ATOM 2897 CB VAL A 373 -13.187 -65.178 2.548 1.00 30.36 C ANISOU 2897 CB VAL A 373 3872 4127 3535 -262 561 345 C ATOM 2898 CG1 VAL A 373 -14.323 -64.290 2.084 1.00 29.99 C ANISOU 2898 CG1 VAL A 373 3724 4101 3567 -292 581 276 C ATOM 2899 CG2 VAL A 373 -13.608 -66.645 2.514 1.00 31.68 C ANISOU 2899 CG2 VAL A 373 4066 4251 3720 -361 613 428 C ATOM 2900 N GLY A 374 -10.349 -65.715 3.389 1.00 36.34 N ANISOU 2900 N GLY A 374 4790 4901 4118 -147 403 367 N ATOM 2901 CA GLY A 374 -9.183 -66.438 3.842 1.00 37.38 C ANISOU 2901 CA GLY A 374 5030 5015 4158 -139 349 398 C ATOM 2902 C GLY A 374 -9.263 -67.932 3.591 1.00 38.63 C ANISOU 2902 C GLY A 374 5278 5059 4342 -181 387 479 C ATOM 2903 O GLY A 374 -8.239 -68.575 3.349 1.00 38.78 O ANISOU 2903 O GLY A 374 5372 5005 4357 -141 325 482 O ATOM 2904 N LYS A 375 -10.472 -68.496 3.640 1.00 58.96 N ANISOU 2904 N LYS A 375 7843 7609 6951 -264 489 538 N ATOM 2905 CA LYS A 375 -10.619 -69.953 3.559 1.00 60.40 C ANISOU 2905 CA LYS A 375 8124 7672 7155 -322 534 617 C ATOM 2906 C LYS A 375 -10.514 -70.583 2.149 1.00 59.42 C ANISOU 2906 C LYS A 375 7968 7445 7162 -362 489 573 C ATOM 2907 O LYS A 375 -9.869 -71.622 1.995 1.00 60.18 O ANISOU 2907 O LYS A 375 8169 7440 7255 -351 466 609 O ATOM 2908 CB LYS A 375 -11.880 -70.435 4.296 1.00 62.28 C ANISOU 2908 CB LYS A 375 8377 7914 7372 -414 672 706 C ATOM 2909 CG LYS A 375 -13.156 -69.728 3.889 1.00 61.98 C ANISOU 2909 CG LYS A 375 8179 7945 7424 -479 728 663 C ATOM 2910 CD LYS A 375 -14.393 -70.357 4.532 1.00 64.55 C ANISOU 2910 CD LYS A 375 8507 8269 7750 -589 877 751 C ATOM 2911 CE LYS A 375 -14.476 -70.059 6.028 1.00 66.25 C ANISOU 2911 CE LYS A 375 8798 8576 7798 -556 962 816 C ATOM 2912 NZ LYS A 375 -13.505 -70.863 6.824 1.00 67.40 N1+ ANISOU 2912 NZ LYS A 375 9145 8648 7815 -503 951 895 N1+ ATOM 2913 N ASN A 376 -11.127 -69.988 1.126 1.00 42.51 N ANISOU 2913 N ASN A 376 5702 5327 5124 -398 472 492 N ATOM 2914 CA ASN A 376 -11.035 -70.586 -0.212 1.00 41.72 C ANISOU 2914 CA ASN A 376 5586 5145 5121 -435 423 438 C ATOM 2915 C ASN A 376 -9.925 -69.985 -1.061 1.00 40.08 C ANISOU 2915 C ASN A 376 5359 4951 4918 -358 319 347 C ATOM 2916 O ASN A 376 -9.683 -70.423 -2.191 1.00 39.42 O ANISOU 2916 O ASN A 376 5272 4819 4887 -372 274 298 O ATOM 2917 CB ASN A 376 -12.356 -70.516 -0.965 1.00 41.53 C ANISOU 2917 CB ASN A 376 5457 5128 5196 -526 453 398 C ATOM 2918 CG ASN A 376 -12.683 -69.120 -1.438 1.00 40.10 C ANISOU 2918 CG ASN A 376 5169 5035 5031 -488 410 306 C ATOM 2919 ND2 ASN A 376 -13.355 -69.021 -2.570 1.00 39.70 N ANISOU 2919 ND2 ASN A 376 5045 4985 5053 -529 376 241 N ATOM 2920 OD1 ASN A 376 -12.346 -68.144 -0.792 1.00 39.54 O ANISOU 2920 OD1 ASN A 376 5091 5028 4903 -422 403 296 O ATOM 2921 N PHE A 377 -9.242 -68.997 -0.490 1.00 35.52 N ANISOU 2921 N PHE A 377 4770 4445 4282 -279 287 329 N ATOM 2922 CA PHE A 377 -8.199 -68.289 -1.205 1.00 34.14 C ANISOU 2922 CA PHE A 377 4564 4288 4121 -220 202 247 C ATOM 2923 C PHE A 377 -7.125 -69.237 -1.722 1.00 34.38 C ANISOU 2923 C PHE A 377 4664 4248 4153 -193 158 251 C ATOM 2924 O PHE A 377 -6.809 -69.233 -2.902 1.00 33.46 O ANISOU 2924 O PHE A 377 4518 4115 4082 -200 115 186 O ATOM 2925 CB PHE A 377 -7.561 -67.223 -0.329 1.00 33.82 C ANISOU 2925 CB PHE A 377 4506 4325 4019 -145 181 241 C ATOM 2926 CG PHE A 377 -6.362 -66.595 -0.951 1.00 32.59 C ANISOU 2926 CG PHE A 377 4318 4178 3888 -94 105 173 C ATOM 2927 CD1 PHE A 377 -6.506 -65.641 -1.948 1.00 31.03 C ANISOU 2927 CD1 PHE A 377 4043 3985 3762 -129 65 87 C ATOM 2928 CD2 PHE A 377 -5.093 -66.973 -0.567 1.00 33.28 C ANISOU 2928 CD2 PHE A 377 4450 4269 3926 -35 58 190 C ATOM 2929 CE1 PHE A 377 -5.399 -65.057 -2.551 1.00 30.08 C ANISOU 2929 CE1 PHE A 377 3879 3867 3683 -106 14 43 C ATOM 2930 CE2 PHE A 377 -3.963 -66.403 -1.170 1.00 33.17 C ANISOU 2930 CE2 PHE A 377 4386 4269 3948 1 0 128 C ATOM 2931 CZ PHE A 377 -4.119 -65.437 -2.156 1.00 31.36 C ANISOU 2931 CZ PHE A 377 4077 4037 3799 -19 1 65 C ATOM 2932 N GLU A 378 -6.552 -70.033 -0.831 1.00 51.85 N ANISOU 2932 N GLU A 378 6979 6422 6301 -152 164 325 N ATOM 2933 CA GLU A 378 -5.529 -70.994 -1.216 1.00 52.18 C ANISOU 2933 CA GLU A 378 7101 6382 6341 -105 119 331 C ATOM 2934 C GLU A 378 -6.048 -71.865 -2.340 1.00 51.89 C ANISOU 2934 C GLU A 378 7070 6267 6381 -175 135 315 C ATOM 2935 O GLU A 378 -5.346 -72.133 -3.301 1.00 51.32 O ANISOU 2935 O GLU A 378 6998 6165 6338 -149 90 265 O ATOM 2936 CB GLU A 378 -5.160 -71.877 -0.017 1.00 54.08 C ANISOU 2936 CB GLU A 378 7480 6571 6496 -50 129 423 C ATOM 2937 CG GLU A 378 -3.760 -72.476 -0.056 1.00 54.57 C ANISOU 2937 CG GLU A 378 7620 6582 6530 62 53 413 C ATOM 2938 CD GLU A 378 -2.673 -71.438 0.185 1.00 54.22 C ANISOU 2938 CD GLU A 378 7515 6631 6458 154 -23 345 C ATOM 2939 OE1 GLU A 378 -2.337 -70.707 -0.767 1.00 53.41 O ANISOU 2939 OE1 GLU A 378 7305 6567 6419 141 -49 264 O ATOM 2940 OE2 GLU A 378 -2.153 -71.345 1.318 1.00 55.42 O1- ANISOU 2940 OE2 GLU A 378 7725 6812 6521 240 -56 367 O1- ATOM 2941 N ASP A 379 -7.291 -72.307 -2.201 1.00 57.36 N ANISOU 2941 N ASP A 379 7760 6930 7103 -264 202 356 N ATOM 2942 CA ASP A 379 -7.906 -73.220 -3.156 1.00 57.55 C ANISOU 2942 CA ASP A 379 7788 6874 7205 -341 216 344 C ATOM 2943 C ASP A 379 -7.983 -72.647 -4.560 1.00 56.06 C ANISOU 2943 C ASP A 379 7504 6734 7061 -350 166 243 C ATOM 2944 O ASP A 379 -7.712 -73.349 -5.530 1.00 55.96 O ANISOU 2944 O ASP A 379 7515 6663 7084 -355 138 214 O ATOM 2945 CB ASP A 379 -9.313 -73.580 -2.695 1.00 58.96 C ANISOU 2945 CB ASP A 379 7950 7029 7421 -446 299 401 C ATOM 2946 CG ASP A 379 -9.354 -73.990 -1.244 1.00 60.90 C ANISOU 2946 CG ASP A 379 8294 7249 7595 -440 364 514 C ATOM 2947 OD1 ASP A 379 -8.980 -73.166 -0.354 1.00 60.81 O ANISOU 2947 OD1 ASP A 379 8282 7324 7498 -373 360 528 O ATOM 2948 OD2 ASP A 379 -9.779 -75.141 -0.998 1.00 62.54 O1- ANISOU 2948 OD2 ASP A 379 8586 7347 7828 -505 419 589 O1- ATOM 2949 N VAL A 380 -8.444 -71.402 -4.673 1.00 33.67 N ANISOU 2949 N VAL A 380 4571 4002 4219 -349 159 193 N ATOM 2950 CA VAL A 380 -8.573 -70.777 -5.982 1.00 32.38 C ANISOU 2950 CA VAL A 380 4337 3895 4072 -342 112 114 C ATOM 2951 C VAL A 380 -7.298 -70.118 -6.564 1.00 31.23 C ANISOU 2951 C VAL A 380 4184 3796 3886 -263 56 67 C ATOM 2952 O VAL A 380 -6.991 -70.304 -7.745 1.00 30.77 O ANISOU 2952 O VAL A 380 4120 3736 3835 -249 32 39 O ATOM 2953 CB VAL A 380 -9.876 -69.895 -6.116 1.00 32.17 C ANISOU 2953 CB VAL A 380 4222 3936 4064 -378 127 88 C ATOM 2954 CG1 VAL A 380 -10.787 -70.018 -4.883 1.00 33.18 C ANISOU 2954 CG1 VAL A 380 4341 4056 4209 -433 199 147 C ATOM 2955 CG2 VAL A 380 -9.552 -68.472 -6.414 1.00 31.02 C ANISOU 2955 CG2 VAL A 380 4034 3881 3871 -312 85 36 C ATOM 2956 N ALA A 381 -6.553 -69.382 -5.741 1.00 30.46 N ANISOU 2956 N ALA A 381 4083 3734 3757 -217 43 65 N ATOM 2957 CA ALA A 381 -5.433 -68.572 -6.226 1.00 29.55 C ANISOU 2957 CA ALA A 381 3936 3666 3624 -160 -2 21 C ATOM 2958 C ALA A 381 -4.231 -69.424 -6.592 1.00 30.07 C ANISOU 2958 C ALA A 381 4054 3677 3695 -120 -19 30 C ATOM 2959 O ALA A 381 -3.433 -69.070 -7.484 1.00 29.77 O ANISOU 2959 O ALA A 381 3983 3672 3656 -85 -39 10 O ATOM 2960 CB ALA A 381 -5.032 -67.505 -5.207 1.00 29.11 C ANISOU 2960 CB ALA A 381 3846 3642 3572 -141 -15 10 C ATOM 2961 N PHE A 382 -4.076 -70.524 -5.870 1.00 33.78 N ANISOU 2961 N PHE A 382 4609 4062 4164 -109 -7 81 N ATOM 2962 CA PHE A 382 -2.951 -71.422 -6.100 1.00 34.44 C ANISOU 2962 CA PHE A 382 4758 4082 4248 -43 -35 88 C ATOM 2963 C PHE A 382 -3.230 -72.673 -6.924 1.00 34.46 C ANISOU 2963 C PHE A 382 4815 3996 4281 -69 -27 94 C ATOM 2964 O PHE A 382 -2.364 -73.551 -7.035 1.00 35.07 O ANISOU 2964 O PHE A 382 4959 4002 4362 -5 -50 100 O ATOM 2965 CB PHE A 382 -2.204 -71.712 -4.816 1.00 35.51 C ANISOU 2965 CB PHE A 382 4960 4190 4341 38 -54 133 C ATOM 2966 CG PHE A 382 -1.297 -70.592 -4.414 1.00 35.89 C ANISOU 2966 CG PHE A 382 4943 4319 4374 102 -92 94 C ATOM 2967 CD1 PHE A 382 -0.224 -70.249 -5.220 1.00 35.55 C ANISOU 2967 CD1 PHE A 382 4844 4306 4356 149 -128 29 C ATOM 2968 CD2 PHE A 382 -1.519 -69.870 -3.257 1.00 36.23 C ANISOU 2968 CD2 PHE A 382 4970 4414 4381 112 -87 117 C ATOM 2969 CE1 PHE A 382 0.622 -69.224 -4.867 1.00 35.89 C ANISOU 2969 CE1 PHE A 382 4814 4420 4403 197 -156 -23 C ATOM 2970 CE2 PHE A 382 -0.680 -68.852 -2.896 1.00 36.40 C ANISOU 2970 CE2 PHE A 382 4924 4506 4401 167 -123 68 C ATOM 2971 CZ PHE A 382 0.395 -68.523 -3.696 1.00 36.15 C ANISOU 2971 CZ PHE A 382 4832 4491 4412 208 -153 -7 C ATOM 2972 N ASP A 383 -4.443 -72.785 -7.462 1.00 39.12 N ANISOU 2972 N ASP A 383 5379 4586 4901 -153 0 89 N ATOM 2973 CA ASP A 383 -4.724 -73.839 -8.428 1.00 39.68 C ANISOU 2973 CA ASP A 383 5487 4573 5017 -184 -1 75 C ATOM 2974 C ASP A 383 -3.711 -73.754 -9.595 1.00 39.09 C ANISOU 2974 C ASP A 383 5394 4516 4943 -124 -34 23 C ATOM 2975 O ASP A 383 -3.602 -72.726 -10.256 1.00 38.02 O ANISOU 2975 O ASP A 383 5177 4475 4793 -116 -40 -5 O ATOM 2976 CB ASP A 383 -6.148 -73.705 -8.951 1.00 39.82 C ANISOU 2976 CB ASP A 383 5448 4610 5073 -274 19 59 C ATOM 2977 CG ASP A 383 -6.519 -74.822 -9.927 1.00 40.68 C ANISOU 2977 CG ASP A 383 5593 4617 5246 -318 9 33 C ATOM 2978 OD1 ASP A 383 -5.613 -75.385 -10.595 1.00 40.76 O ANISOU 2978 OD1 ASP A 383 5653 4577 5257 -266 -16 5 O ATOM 2979 OD2 ASP A 383 -7.728 -75.131 -10.041 1.00 41.37 O1- ANISOU 2979 OD2 ASP A 383 5655 4671 5392 -405 25 31 O1- ATOM 2980 N GLU A 384 -3.002 -74.854 -9.852 1.00 47.96 N ANISOU 2980 N GLU A 384 6596 5540 6085 -78 -48 18 N ATOM 2981 CA GLU A 384 -1.986 -74.930 -10.909 1.00 47.79 C ANISOU 2981 CA GLU A 384 6563 5524 6072 -13 -69 -34 C ATOM 2982 C GLU A 384 -2.533 -74.714 -12.314 1.00 47.41 C ANISOU 2982 C GLU A 384 6471 5503 6041 -57 -65 -83 C ATOM 2983 O GLU A 384 -1.805 -74.276 -13.199 1.00 46.94 O ANISOU 2983 O GLU A 384 6372 5489 5975 -14 -66 -121 O ATOM 2984 CB GLU A 384 -1.236 -76.273 -10.859 1.00 48.98 C ANISOU 2984 CB GLU A 384 6819 5550 6243 57 -84 -36 C ATOM 2985 CG GLU A 384 -0.185 -76.356 -9.748 1.00 49.74 C ANISOU 2985 CG GLU A 384 6949 5641 6311 159 -107 -2 C ATOM 2986 CD GLU A 384 0.492 -77.731 -9.639 1.00 51.87 C ANISOU 2986 CD GLU A 384 7331 5780 6596 247 -126 6 C ATOM 2987 OE1 GLU A 384 0.599 -78.446 -10.663 1.00 52.70 O ANISOU 2987 OE1 GLU A 384 7467 5818 6739 254 -124 -42 O ATOM 2988 OE2 GLU A 384 0.925 -78.092 -8.520 1.00 52.90 O1- ANISOU 2988 OE2 GLU A 384 7528 5875 6698 318 -148 59 O1- ATOM 2989 N LYS A 385 -3.814 -75.021 -12.505 1.00 49.53 N ANISOU 2989 N LYS A 385 6743 5741 6334 -141 -60 -84 N ATOM 2990 CA LYS A 385 -4.464 -74.950 -13.820 1.00 49.71 C ANISOU 2990 CA LYS A 385 6737 5775 6376 -179 -71 -138 C ATOM 2991 C LYS A 385 -5.004 -73.568 -14.192 1.00 48.80 C ANISOU 2991 C LYS A 385 6528 5783 6232 -192 -69 -133 C ATOM 2992 O LYS A 385 -5.488 -73.367 -15.314 1.00 48.89 O ANISOU 2992 O LYS A 385 6518 5809 6248 -207 -84 -175 O ATOM 2993 CB LYS A 385 -5.620 -75.955 -13.893 1.00 50.95 C ANISOU 2993 CB LYS A 385 6931 5831 6599 -265 -76 -156 C ATOM 2994 CG LYS A 385 -5.204 -77.415 -13.719 1.00 52.85 C ANISOU 2994 CG LYS A 385 7281 5917 6882 -256 -76 -161 C ATOM 2995 CD LYS A 385 -6.438 -78.328 -13.672 1.00 54.77 C ANISOU 2995 CD LYS A 385 7547 6046 7217 -364 -74 -174 C ATOM 2996 CE LYS A 385 -6.067 -79.769 -13.328 1.00 56.79 C ANISOU 2996 CE LYS A 385 7929 6125 7525 -359 -65 -159 C ATOM 2997 NZ LYS A 385 -5.076 -80.325 -14.296 1.00 57.37 N1+ ANISOU 2997 NZ LYS A 385 8065 6149 7583 -274 -90 -229 N1+ ATOM 2998 N LYS A 386 -4.931 -72.617 -13.261 1.00 39.61 N ANISOU 2998 N LYS A 386 5317 4695 5036 -179 -52 -87 N ATOM 2999 CA LYS A 386 -5.536 -71.307 -13.501 1.00 38.83 C ANISOU 2999 CA LYS A 386 5144 4693 4915 -183 -43 -77 C ATOM 3000 C LYS A 386 -4.568 -70.124 -13.425 1.00 37.89 C ANISOU 3000 C LYS A 386 4980 4650 4767 -127 -26 -56 C ATOM 3001 O LYS A 386 -3.623 -70.136 -12.650 1.00 37.75 O ANISOU 3001 O LYS A 386 4965 4630 4746 -96 -25 -44 O ATOM 3002 CB LYS A 386 -6.740 -71.100 -12.586 1.00 39.04 C ANISOU 3002 CB LYS A 386 5146 4738 4948 -233 -32 -56 C ATOM 3003 CG LYS A 386 -7.812 -72.159 -12.769 1.00 40.20 C ANISOU 3003 CG LYS A 386 5311 4804 5161 -310 -42 -80 C ATOM 3004 CD LYS A 386 -8.305 -72.222 -14.196 1.00 40.47 C ANISOU 3004 CD LYS A 386 5325 4827 5226 -324 -78 -137 C ATOM 3005 CE LYS A 386 -9.415 -73.267 -14.358 1.00 41.71 C ANISOU 3005 CE LYS A 386 5480 4893 5474 -414 -99 -179 C ATOM 3006 NZ LYS A 386 -9.874 -73.386 -15.787 1.00 42.19 N1+ ANISOU 3006 NZ LYS A 386 5522 4943 5566 -425 -150 -267 N1+ ATOM 3007 N ASN A 387 -4.817 -69.109 -14.248 1.00 26.42 N ANISOU 3007 N ASN A 387 3487 3247 3306 -119 -14 -55 N ATOM 3008 CA ASN A 387 -4.077 -67.858 -14.160 1.00 25.59 C ANISOU 3008 CA ASN A 387 3334 3197 3192 -86 18 -32 C ATOM 3009 C ASN A 387 -4.913 -66.832 -13.407 1.00 24.85 C ANISOU 3009 C ASN A 387 3195 3147 3101 -64 26 -13 C ATOM 3010 O ASN A 387 -5.844 -66.242 -13.964 1.00 24.62 O ANISOU 3010 O ASN A 387 3157 3128 3071 -68 26 -15 O ATOM 3011 CB ASN A 387 -3.737 -67.334 -15.562 1.00 25.40 C ANISOU 3011 CB ASN A 387 3302 3177 3172 -81 26 -45 C ATOM 3012 CG ASN A 387 -2.742 -68.214 -16.281 1.00 26.00 C ANISOU 3012 CG ASN A 387 3413 3208 3260 -60 7 -90 C ATOM 3013 ND2 ASN A 387 -3.203 -68.884 -17.338 1.00 26.64 N ANISOU 3013 ND2 ASN A 387 3540 3251 3329 -67 -15 -131 N ATOM 3014 OD1 ASN A 387 -1.562 -68.297 -15.887 1.00 25.78 O ANISOU 3014 OD1 ASN A 387 3368 3178 3251 -31 10 -102 O ATOM 3015 N VAL A 388 -4.517 -66.573 -12.158 1.00 26.35 N ANISOU 3015 N VAL A 388 3367 3333 3311 -49 16 -11 N ATOM 3016 CA VAL A 388 -5.381 -65.855 -11.230 1.00 26.16 C ANISOU 3016 CA VAL A 388 3336 3322 3280 -44 13 -12 C ATOM 3017 C VAL A 388 -4.858 -64.457 -10.937 1.00 25.88 C ANISOU 3017 C VAL A 388 3282 3285 3267 -16 7 -8 C ATOM 3018 O VAL A 388 -3.730 -64.293 -10.537 1.00 26.02 O ANISOU 3018 O VAL A 388 3296 3297 3295 -4 2 -2 O ATOM 3019 CB VAL A 388 -5.590 -66.680 -9.961 1.00 26.90 C ANISOU 3019 CB VAL A 388 3453 3414 3354 -65 10 -7 C ATOM 3020 CG1 VAL A 388 -6.641 -66.049 -9.085 1.00 27.04 C ANISOU 3020 CG1 VAL A 388 3457 3438 3378 -84 10 -9 C ATOM 3021 CG2 VAL A 388 -6.011 -68.111 -10.349 1.00 27.61 C ANISOU 3021 CG2 VAL A 388 3617 3479 3395 -135 10 -6 C ATOM 3022 N PHE A 389 -5.666 -63.441 -11.196 1.00 27.09 N ANISOU 3022 N PHE A 389 3432 3440 3420 -15 6 -8 N ATOM 3023 CA PHE A 389 -5.242 -62.064 -10.986 1.00 26.80 C ANISOU 3023 CA PHE A 389 3394 3396 3393 -2 1 -2 C ATOM 3024 C PHE A 389 -6.151 -61.482 -9.891 1.00 26.75 C ANISOU 3024 C PHE A 389 3385 3394 3384 -8 3 -5 C ATOM 3025 O PHE A 389 -7.369 -61.365 -10.082 1.00 26.89 O ANISOU 3025 O PHE A 389 3402 3424 3391 -19 7 -12 O ATOM 3026 CB PHE A 389 -5.351 -61.276 -12.296 1.00 26.58 C ANISOU 3026 CB PHE A 389 3367 3368 3366 -1 1 -1 C ATOM 3027 CG PHE A 389 -4.533 -59.992 -12.331 1.00 26.62 C ANISOU 3027 CG PHE A 389 3372 3372 3372 0 0 0 C ATOM 3028 CD1 PHE A 389 -3.610 -59.696 -11.328 1.00 26.26 C ANISOU 3028 CD1 PHE A 389 3326 3326 3326 0 0 0 C ATOM 3029 CD2 PHE A 389 -4.709 -59.064 -13.377 1.00 26.55 C ANISOU 3029 CD2 PHE A 389 3362 3362 3362 0 0 0 C ATOM 3030 CE1 PHE A 389 -2.871 -58.522 -11.362 1.00 26.30 C ANISOU 3030 CE1 PHE A 389 3327 3334 3331 -4 3 -6 C ATOM 3031 CE2 PHE A 389 -3.956 -57.861 -13.422 1.00 26.38 C ANISOU 3031 CE2 PHE A 389 3341 3342 3341 -2 2 -3 C ATOM 3032 CZ PHE A 389 -3.049 -57.595 -12.403 1.00 26.42 C ANISOU 3032 CZ PHE A 389 3343 3350 3346 -6 6 -10 C ATOM 3033 N VAL A 390 -5.551 -61.164 -8.740 1.00 23.92 N ANISOU 3033 N VAL A 390 3028 3035 3027 -6 2 -4 N ATOM 3034 CA VAL A 390 -6.275 -60.844 -7.510 1.00 24.02 C ANISOU 3034 CA VAL A 390 3037 3061 3029 -15 5 -11 C ATOM 3035 C VAL A 390 -6.030 -59.399 -7.039 1.00 23.82 C ANISOU 3035 C VAL A 390 3006 3036 3009 -14 5 -12 C ATOM 3036 O VAL A 390 -4.881 -58.920 -6.997 1.00 23.67 O ANISOU 3036 O VAL A 390 2987 3013 2992 -10 4 -12 O ATOM 3037 CB VAL A 390 -5.859 -61.815 -6.346 1.00 24.27 C ANISOU 3037 CB VAL A 390 3067 3101 3052 -24 6 -11 C ATOM 3038 CG1 VAL A 390 -6.584 -61.469 -5.059 1.00 24.33 C ANISOU 3038 CG1 VAL A 390 3061 3133 3051 -46 7 -15 C ATOM 3039 CG2 VAL A 390 -6.092 -63.280 -6.730 1.00 24.76 C ANISOU 3039 CG2 VAL A 390 3132 3162 3112 -41 6 -8 C ATOM 3040 N GLU A 391 -7.119 -58.716 -6.686 1.00 30.92 N ANISOU 3040 N GLU A 391 3902 3949 3896 -20 8 -22 N ATOM 3041 CA GLU A 391 -7.059 -57.374 -6.108 1.00 30.99 C ANISOU 3041 CA GLU A 391 3897 3967 3911 -23 9 -30 C ATOM 3042 C GLU A 391 -7.270 -57.390 -4.575 1.00 31.03 C ANISOU 3042 C GLU A 391 3884 4001 3904 -33 11 -43 C ATOM 3043 O GLU A 391 -8.321 -57.824 -4.091 1.00 31.09 O ANISOU 3043 O GLU A 391 3881 4033 3900 -47 14 -48 O ATOM 3044 CB GLU A 391 -8.137 -56.514 -6.741 1.00 31.16 C ANISOU 3044 CB GLU A 391 3914 3992 3933 -24 10 -36 C ATOM 3045 CG GLU A 391 -8.070 -55.062 -6.328 1.00 31.47 C ANISOU 3045 CG GLU A 391 3942 4037 3976 -22 12 -49 C ATOM 3046 CD GLU A 391 -9.439 -54.447 -6.124 1.00 31.58 C ANISOU 3046 CD GLU A 391 3938 4074 3986 -25 14 -69 C ATOM 3047 OE1 GLU A 391 -9.510 -53.227 -5.863 1.00 31.89 O ANISOU 3047 OE1 GLU A 391 3981 4114 4019 -19 12 -95 O ATOM 3048 OE2 GLU A 391 -10.443 -55.185 -6.195 1.00 31.98 O1- ANISOU 3048 OE2 GLU A 391 3980 4144 4027 -33 16 -74 O1- ATOM 3049 N PHE A 392 -6.281 -56.923 -3.821 1.00 26.13 N ANISOU 3049 N PHE A 392 3255 3391 3284 -28 12 -52 N ATOM 3050 CA PHE A 392 -6.405 -56.839 -2.372 1.00 26.37 C ANISOU 3050 CA PHE A 392 3278 3461 3281 -28 10 -74 C ATOM 3051 C PHE A 392 -6.750 -55.423 -1.947 1.00 26.55 C ANISOU 3051 C PHE A 392 3261 3506 3322 -25 11 -95 C ATOM 3052 O PHE A 392 -5.968 -54.501 -2.131 1.00 26.82 O ANISOU 3052 O PHE A 392 3314 3525 3350 -15 8 -121 O ATOM 3053 CB PHE A 392 -5.114 -57.305 -1.692 1.00 26.42 C ANISOU 3053 CB PHE A 392 3275 3483 3281 -16 6 -81 C ATOM 3054 CG PHE A 392 -4.759 -58.729 -2.009 1.00 26.53 C ANISOU 3054 CG PHE A 392 3284 3483 3315 -20 6 -52 C ATOM 3055 CD1 PHE A 392 -5.109 -59.751 -1.142 1.00 26.88 C ANISOU 3055 CD1 PHE A 392 3315 3557 3341 -24 4 -40 C ATOM 3056 CD2 PHE A 392 -4.098 -59.054 -3.195 1.00 26.62 C ANISOU 3056 CD2 PHE A 392 3317 3456 3342 -18 6 -43 C ATOM 3057 CE1 PHE A 392 -4.792 -61.081 -1.436 1.00 27.27 C ANISOU 3057 CE1 PHE A 392 3395 3592 3375 -28 3 -23 C ATOM 3058 CE2 PHE A 392 -3.780 -60.397 -3.502 1.00 26.94 C ANISOU 3058 CE2 PHE A 392 3369 3483 3384 -18 4 -29 C ATOM 3059 CZ PHE A 392 -4.131 -61.407 -2.615 1.00 27.18 C ANISOU 3059 CZ PHE A 392 3403 3537 3388 -24 4 -21 C ATOM 3060 N TYR A 393 -7.935 -55.241 -1.385 1.00 30.49 N ANISOU 3060 N TYR A 393 3769 4033 3782 -29 11 -114 N ATOM 3061 CA TYR A 393 -8.387 -53.876 -1.134 1.00 30.84 C ANISOU 3061 CA TYR A 393 3796 4093 3827 -20 9 -147 C ATOM 3062 C TYR A 393 -8.924 -53.654 0.303 1.00 31.08 C ANISOU 3062 C TYR A 393 3753 4197 3860 -9 4 -161 C ATOM 3063 O TYR A 393 -8.973 -54.597 1.108 1.00 31.38 O ANISOU 3063 O TYR A 393 3772 4306 3845 -14 -7 -169 O ATOM 3064 CB TYR A 393 -9.468 -53.508 -2.154 1.00 30.67 C ANISOU 3064 CB TYR A 393 3751 4059 3843 -28 13 -133 C ATOM 3065 CG TYR A 393 -10.752 -54.272 -1.932 1.00 31.12 C ANISOU 3065 CG TYR A 393 3829 4146 3849 -39 16 -146 C ATOM 3066 CD1 TYR A 393 -11.858 -53.674 -1.322 1.00 31.78 C ANISOU 3066 CD1 TYR A 393 3860 4294 3922 -46 0 -184 C ATOM 3067 CD2 TYR A 393 -10.848 -55.608 -2.288 1.00 31.09 C ANISOU 3067 CD2 TYR A 393 3839 4134 3840 -55 20 -120 C ATOM 3068 CE1 TYR A 393 -13.034 -54.383 -1.105 1.00 32.81 C ANISOU 3068 CE1 TYR A 393 3930 4534 4002 -75 23 -227 C ATOM 3069 CE2 TYR A 393 -12.016 -56.330 -2.075 1.00 31.83 C ANISOU 3069 CE2 TYR A 393 3902 4279 3913 -89 15 -135 C ATOM 3070 CZ TYR A 393 -13.105 -55.713 -1.488 1.00 32.93 C ANISOU 3070 CZ TYR A 393 3965 4540 4009 -110 34 -199 C ATOM 3071 OH TYR A 393 -14.260 -56.443 -1.281 1.00 34.04 O ANISOU 3071 OH TYR A 393 4059 4722 4153 -132 105 -186 O ATOM 3072 N ALA A 394 -9.323 -52.412 0.594 1.00 27.40 N ANISOU 3072 N ALA A 394 3269 3757 3385 1 -20 -207 N ATOM 3073 CA ALA A 394 -10.087 -52.070 1.802 1.00 28.90 C ANISOU 3073 CA ALA A 394 3377 4104 3500 37 -19 -297 C ATOM 3074 C ALA A 394 -11.355 -51.315 1.427 1.00 29.55 C ANISOU 3074 C ALA A 394 3439 4211 3579 41 -11 -338 C ATOM 3075 O ALA A 394 -11.338 -50.488 0.524 1.00 29.05 O ANISOU 3075 O ALA A 394 3401 4068 3569 35 -25 -333 O ATOM 3076 CB ALA A 394 -9.248 -51.202 2.773 1.00 29.54 C ANISOU 3076 CB ALA A 394 3435 4224 3563 100 -34 -361 C ATOM 3077 N PRO A 395 -12.445 -51.586 2.152 1.00 50.37 N ANISOU 3077 N PRO A 395 6086 6889 6163 70 69 -333 N ATOM 3078 CA PRO A 395 -13.772 -50.976 2.033 1.00 51.49 C ANISOU 3078 CA PRO A 395 6203 7051 6310 99 119 -360 C ATOM 3079 C PRO A 395 -13.798 -49.444 2.083 1.00 52.07 C ANISOU 3079 C PRO A 395 6270 7111 6403 157 100 -425 C ATOM 3080 O PRO A 395 -14.529 -48.838 1.295 1.00 52.34 O ANISOU 3080 O PRO A 395 6282 7129 6476 172 95 -443 O ATOM 3081 CB PRO A 395 -14.507 -51.536 3.242 1.00 52.89 C ANISOU 3081 CB PRO A 395 6389 7283 6425 128 235 -344 C ATOM 3082 CG PRO A 395 -13.896 -52.866 3.450 1.00 52.57 C ANISOU 3082 CG PRO A 395 6387 7231 6356 86 244 -283 C ATOM 3083 CD PRO A 395 -12.443 -52.705 3.110 1.00 51.35 C ANISOU 3083 CD PRO A 395 6247 7041 6225 75 138 -290 C ATOM 3084 N TRP A 396 -13.031 -48.823 2.971 1.00 52.68 N ANISOU 3084 N TRP A 396 6374 7190 6453 198 92 -466 N ATOM 3085 CA TRP A 396 -13.075 -47.368 3.096 1.00 53.43 C ANISOU 3085 CA TRP A 396 6478 7257 6567 258 82 -537 C ATOM 3086 C TRP A 396 -12.028 -46.635 2.257 1.00 52.33 C ANISOU 3086 C TRP A 396 6339 7043 6502 230 8 -550 C ATOM 3087 O TRP A 396 -11.897 -45.413 2.358 1.00 53.18 O ANISOU 3087 O TRP A 396 6469 7104 6633 275 2 -609 O ATOM 3088 CB TRP A 396 -12.912 -46.950 4.548 0.00 54.96 C ANISOU 3088 CB TRP A 396 6716 7482 6683 324 120 -597 C ATOM 3089 CG TRP A 396 -11.739 -47.589 5.156 0.00 54.80 C ANISOU 3089 CG TRP A 396 6726 7473 6622 306 87 -585 C ATOM 3090 CD1 TRP A 396 -10.448 -47.165 5.096 0.43 54.41 C ANISOU 3090 CD1 TRP A 396 6678 7385 6610 298 14 -617 C ATOM 3091 CD2 TRP A 396 -11.733 -48.799 5.906 0.00 55.34 C ANISOU 3091 CD2 TRP A 396 6829 7590 6608 301 133 -538 C ATOM 3092 CE2 TRP A 396 -10.402 -49.050 6.282 0.20 55.14 C ANISOU 3092 CE2 TRP A 396 6829 7557 6565 303 71 -547 C ATOM 3093 CE3 TRP A 396 -12.726 -49.694 6.301 1.00 56.02 C ANISOU 3093 CE3 TRP A 396 6930 7719 6637 296 233 -490 C ATOM 3094 NE1 TRP A 396 -9.633 -48.038 5.773 0.72 54.63 N ANISOU 3094 NE1 TRP A 396 6731 7444 6582 300 0 -599 N ATOM 3095 CZ2 TRP A 396 -10.039 -50.153 7.032 0.34 55.80 C ANISOU 3095 CZ2 TRP A 396 6970 7671 6561 309 94 -508 C ATOM 3096 CZ3 TRP A 396 -12.365 -50.789 7.045 0.28 56.49 C ANISOU 3096 CZ3 TRP A 396 7053 7800 6612 288 272 -445 C ATOM 3097 CH2 TRP A 396 -11.032 -51.010 7.404 1.00 56.45 C ANISOU 3097 CH2 TRP A 396 7089 7783 6575 299 196 -454 C ATOM 3098 N CYS A 397 -11.270 -47.365 1.447 1.00 41.46 N ANISOU 3098 N CYS A 397 4941 5647 5164 158 -35 -496 N ATOM 3099 CA CYS A 397 -10.199 -46.752 0.653 1.00 40.69 C ANISOU 3099 CA CYS A 397 4832 5483 5144 128 -73 -498 C ATOM 3100 C CYS A 397 -10.675 -46.037 -0.629 1.00 40.55 C ANISOU 3100 C CYS A 397 4832 5399 5176 123 -75 -488 C ATOM 3101 O CYS A 397 -11.336 -46.638 -1.492 1.00 40.21 O ANISOU 3101 O CYS A 397 4798 5355 5124 97 -76 -443 O ATOM 3102 CB CYS A 397 -9.123 -47.793 0.319 1.00 39.47 C ANISOU 3102 CB CYS A 397 4712 5284 5002 72 -61 -401 C ATOM 3103 SG CYS A 397 -7.730 -47.174 -0.636 1.00 39.00 S ANISOU 3103 SG CYS A 397 4674 5132 5010 45 -49 -366 S ATOM 3104 N GLY A 398 -10.300 -44.762 -0.753 1.00 33.20 N ANISOU 3104 N GLY A 398 3931 4396 4288 156 -68 -528 N ATOM 3105 CA GLY A 398 -10.600 -43.961 -1.927 1.00 33.49 C ANISOU 3105 CA GLY A 398 4008 4349 4367 173 -57 -511 C ATOM 3106 C GLY A 398 -9.966 -44.491 -3.207 1.00 32.48 C ANISOU 3106 C GLY A 398 3873 4193 4275 108 -61 -443 C ATOM 3107 O GLY A 398 -10.611 -44.486 -4.262 1.00 32.48 O ANISOU 3107 O GLY A 398 3903 4166 4273 124 -58 -406 O ATOM 3108 N HIS A 399 -8.709 -44.932 -3.130 1.00 23.45 N ANISOU 3108 N HIS A 399 2688 3059 3163 52 -59 -427 N ATOM 3109 CA HIS A 399 -8.008 -45.467 -4.318 1.00 22.51 C ANISOU 3109 CA HIS A 399 2620 2897 3037 12 -22 -323 C ATOM 3110 C HIS A 399 -8.607 -46.774 -4.798 1.00 21.66 C ANISOU 3110 C HIS A 399 2609 2782 2840 10 -11 -241 C ATOM 3111 O HIS A 399 -8.683 -47.034 -6.006 1.00 21.57 O ANISOU 3111 O HIS A 399 2582 2771 2842 5 -6 -187 O ATOM 3112 CB HIS A 399 -6.533 -45.665 -4.025 1.00 22.22 C ANISOU 3112 CB HIS A 399 2583 2855 3007 -6 3 -307 C ATOM 3113 CG HIS A 399 -5.843 -44.398 -3.629 1.00 23.76 C ANISOU 3113 CG HIS A 399 2703 3018 3307 -7 9 -433 C ATOM 3114 CD2 HIS A 399 -5.473 -43.933 -2.406 1.00 24.36 C ANISOU 3114 CD2 HIS A 399 2762 3103 3392 13 -17 -519 C ATOM 3115 ND1 HIS A 399 -5.516 -43.428 -4.540 1.00 24.98 N ANISOU 3115 ND1 HIS A 399 2919 3069 3502 -25 42 -436 N ATOM 3116 CE1 HIS A 399 -4.939 -42.410 -3.904 1.00 25.96 C ANISOU 3116 CE1 HIS A 399 3073 3127 3662 -29 37 -513 C ATOM 3117 NE2 HIS A 399 -4.898 -42.701 -2.622 1.00 26.19 N ANISOU 3117 NE2 HIS A 399 3052 3228 3673 -5 -2 -568 N ATOM 3118 N CYS A 400 -9.062 -47.585 -3.848 1.00 33.80 N ANISOU 3118 N CYS A 400 4144 4360 4338 15 -14 -248 N ATOM 3119 CA CYS A 400 -9.785 -48.800 -4.205 1.00 33.71 C ANISOU 3119 CA CYS A 400 4113 4380 4315 10 -9 -196 C ATOM 3120 C CYS A 400 -11.119 -48.458 -4.888 1.00 34.09 C ANISOU 3120 C CYS A 400 4154 4436 4363 27 -22 -206 C ATOM 3121 O CYS A 400 -11.483 -49.075 -5.891 1.00 34.15 O ANISOU 3121 O CYS A 400 4181 4433 4362 23 -19 -182 O ATOM 3122 CB CYS A 400 -9.976 -49.704 -2.986 1.00 33.59 C ANISOU 3122 CB CYS A 400 4125 4394 4245 7 -5 -221 C ATOM 3123 SG CYS A 400 -8.416 -50.217 -2.172 1.00 33.81 S ANISOU 3123 SG CYS A 400 4116 4436 4294 2 -1 -198 S ATOM 3124 N LYS A 401 -11.822 -47.450 -4.376 1.00 33.29 N ANISOU 3124 N LYS A 401 4020 4369 4260 50 -58 -300 N ATOM 3125 CA LYS A 401 -13.021 -46.956 -5.043 1.00 33.85 C ANISOU 3125 CA LYS A 401 4056 4474 4333 103 -87 -366 C ATOM 3126 C LYS A 401 -12.738 -46.440 -6.436 1.00 33.75 C ANISOU 3126 C LYS A 401 4073 4398 4353 121 -96 -335 C ATOM 3127 O LYS A 401 -13.558 -46.613 -7.320 1.00 33.97 O ANISOU 3127 O LYS A 401 4108 4433 4366 158 -103 -324 O ATOM 3128 CB LYS A 401 -13.674 -45.829 -4.261 1.00 34.84 C ANISOU 3128 CB LYS A 401 4156 4611 4471 189 -69 -415 C ATOM 3129 CG LYS A 401 -14.321 -46.257 -2.994 1.00 35.52 C ANISOU 3129 CG LYS A 401 4201 4776 4517 202 -43 -447 C ATOM 3130 CD LYS A 401 -15.465 -47.226 -3.259 1.00 35.93 C ANISOU 3130 CD LYS A 401 4217 4889 4545 197 -24 -435 C ATOM 3131 CE LYS A 401 -16.066 -47.653 -1.908 1.00 37.08 C ANISOU 3131 CE LYS A 401 4317 5112 4660 209 32 -452 C ATOM 3132 NZ LYS A 401 -15.992 -46.534 -0.900 1.00 38.14 N1+ ANISOU 3132 NZ LYS A 401 4453 5247 4793 279 56 -501 N1+ ATOM 3133 N GLN A 402 -11.610 -45.780 -6.644 1.00 25.34 N ANISOU 3133 N GLN A 402 3025 3270 3332 107 -81 -313 N ATOM 3134 CA GLN A 402 -11.314 -45.303 -7.985 1.00 25.52 C ANISOU 3134 CA GLN A 402 3105 3219 3371 136 -59 -264 C ATOM 3135 C GLN A 402 -11.040 -46.497 -8.914 1.00 24.94 C ANISOU 3135 C GLN A 402 3028 3172 3275 79 -74 -223 C ATOM 3136 O GLN A 402 -11.350 -46.440 -10.105 1.00 25.18 O ANISOU 3136 O GLN A 402 3103 3176 3288 124 -71 -189 O ATOM 3137 CB GLN A 402 -10.157 -44.291 -7.994 1.00 25.88 C ANISOU 3137 CB GLN A 402 3208 3171 3455 132 -10 -260 C ATOM 3138 CG GLN A 402 -9.520 -44.008 -9.377 1.00 26.04 C ANISOU 3138 CG GLN A 402 3328 3100 3466 136 31 -204 C ATOM 3139 CD GLN A 402 -10.289 -42.999 -10.273 1.00 26.94 C ANISOU 3139 CD GLN A 402 3543 3107 3587 229 71 -179 C ATOM 3140 NE2 GLN A 402 -9.656 -41.841 -10.556 1.00 27.60 N ANISOU 3140 NE2 GLN A 402 3733 3076 3679 225 119 -164 N ATOM 3141 OE1 GLN A 402 -11.407 -43.272 -10.726 1.00 26.93 O ANISOU 3141 OE1 GLN A 402 3494 3154 3584 283 20 -173 O ATOM 3142 N LEU A 403 -10.465 -47.577 -8.382 1.00 24.42 N ANISOU 3142 N LEU A 403 3005 3110 3164 25 -30 -162 N ATOM 3143 CA LEU A 403 -10.173 -48.751 -9.215 1.00 24.20 C ANISOU 3143 CA LEU A 403 2998 3082 3115 14 -16 -122 C ATOM 3144 C LEU A 403 -11.393 -49.658 -9.509 1.00 24.15 C ANISOU 3144 C LEU A 403 2991 3102 3083 25 -23 -129 C ATOM 3145 O LEU A 403 -11.395 -50.423 -10.491 1.00 24.23 O ANISOU 3145 O LEU A 403 2994 3117 3093 25 -22 -97 O ATOM 3146 CB LEU A 403 -9.072 -49.587 -8.558 1.00 23.71 C ANISOU 3146 CB LEU A 403 2945 3020 3042 -3 3 -103 C ATOM 3147 CG LEU A 403 -8.658 -50.905 -9.220 1.00 23.69 C ANISOU 3147 CG LEU A 403 2952 3023 3026 -8 8 -62 C ATOM 3148 CD1 LEU A 403 -8.148 -50.686 -10.644 1.00 23.69 C ANISOU 3148 CD1 LEU A 403 2975 3005 3023 -7 9 -48 C ATOM 3149 CD2 LEU A 403 -7.600 -51.664 -8.362 1.00 22.99 C ANISOU 3149 CD2 LEU A 403 2867 2936 2931 -13 13 -58 C ATOM 3150 N ALA A 404 -12.425 -49.599 -8.668 1.00 26.26 N ANISOU 3150 N ALA A 404 3237 3402 3339 37 -31 -167 N ATOM 3151 CA ALA A 404 -13.510 -50.580 -8.802 1.00 26.21 C ANISOU 3151 CA ALA A 404 3216 3433 3310 37 -33 -183 C ATOM 3152 C ALA A 404 -14.074 -50.773 -10.223 1.00 26.63 C ANISOU 3152 C ALA A 404 3253 3504 3363 68 -50 -206 C ATOM 3153 O ALA A 404 -14.147 -51.907 -10.699 1.00 26.50 O ANISOU 3153 O ALA A 404 3240 3491 3338 53 -34 -190 O ATOM 3154 CB ALA A 404 -14.623 -50.311 -7.794 1.00 26.57 C ANISOU 3154 CB ALA A 404 3189 3562 3346 62 -46 -269 C ATOM 3155 N PRO A 405 -14.490 -49.674 -10.896 1.00 27.30 N ANISOU 3155 N PRO A 405 3318 3603 3452 132 -99 -255 N ATOM 3156 CA PRO A 405 -15.061 -49.776 -12.263 1.00 28.07 C ANISOU 3156 CA PRO A 405 3409 3710 3547 188 -137 -260 C ATOM 3157 C PRO A 405 -14.137 -50.420 -13.309 1.00 27.85 C ANISOU 3157 C PRO A 405 3434 3640 3506 163 -121 -220 C ATOM 3158 O PRO A 405 -14.580 -51.221 -14.142 1.00 28.44 O ANISOU 3158 O PRO A 405 3491 3733 3581 176 -137 -219 O ATOM 3159 CB PRO A 405 -15.386 -48.319 -12.646 1.00 28.86 C ANISOU 3159 CB PRO A 405 3519 3791 3657 277 -187 -249 C ATOM 3160 CG PRO A 405 -14.853 -47.430 -11.494 1.00 28.52 C ANISOU 3160 CG PRO A 405 3477 3724 3635 264 -164 -250 C ATOM 3161 CD PRO A 405 -14.642 -48.325 -10.306 1.00 27.59 C ANISOU 3161 CD PRO A 405 3335 3641 3507 179 -128 -281 C ATOM 3162 N ILE A 406 -12.859 -50.071 -13.263 1.00 30.59 N ANISOU 3162 N ILE A 406 3824 3936 3863 112 -88 -152 N ATOM 3163 CA ILE A 406 -11.875 -50.722 -14.109 1.00 30.32 C ANISOU 3163 CA ILE A 406 3821 3871 3828 76 -57 -96 C ATOM 3164 C ILE A 406 -11.720 -52.213 -13.793 1.00 30.06 C ANISOU 3164 C ILE A 406 3772 3851 3800 40 -29 -81 C ATOM 3165 O ILE A 406 -11.721 -53.048 -14.718 1.00 30.19 O ANISOU 3165 O ILE A 406 3778 3872 3822 49 -30 -71 O ATOM 3166 CB ILE A 406 -10.490 -50.030 -14.033 1.00 29.97 C ANISOU 3166 CB ILE A 406 3791 3806 3791 48 -50 -59 C ATOM 3167 CG1 ILE A 406 -10.536 -48.651 -14.709 1.00 30.61 C ANISOU 3167 CG1 ILE A 406 3946 3838 3845 134 -77 -58 C ATOM 3168 CG2 ILE A 406 -9.419 -50.897 -14.700 1.00 29.52 C ANISOU 3168 CG2 ILE A 406 3740 3742 3735 23 -24 -25 C ATOM 3169 CD1 ILE A 406 -11.298 -47.610 -13.952 1.00 31.10 C ANISOU 3169 CD1 ILE A 406 3988 3887 3940 181 -90 -83 C ATOM 3170 N TRP A 407 -11.592 -52.563 -12.510 1.00 24.10 N ANISOU 3170 N TRP A 407 3010 3100 3047 19 -13 -77 N ATOM 3171 CA TRP A 407 -11.502 -53.991 -12.153 1.00 23.82 C ANISOU 3171 CA TRP A 407 2963 3073 3013 3 -2 -60 C ATOM 3172 C TRP A 407 -12.728 -54.783 -12.656 1.00 24.18 C ANISOU 3172 C TRP A 407 3000 3148 3038 9 -5 -98 C ATOM 3173 O TRP A 407 -12.593 -55.867 -13.231 1.00 24.25 O ANISOU 3173 O TRP A 407 2993 3163 3056 0 0 -83 O ATOM 3174 CB TRP A 407 -11.307 -54.178 -10.653 1.00 23.40 C ANISOU 3174 CB TRP A 407 2922 3020 2949 -6 4 -67 C ATOM 3175 CG TRP A 407 -10.636 -55.475 -10.300 1.00 23.10 C ANISOU 3175 CG TRP A 407 2895 2974 2908 -15 8 -48 C ATOM 3176 CD1 TRP A 407 -11.193 -56.538 -9.626 1.00 22.95 C ANISOU 3176 CD1 TRP A 407 2856 2978 2888 -28 13 -54 C ATOM 3177 CD2 TRP A 407 -9.268 -55.851 -10.582 1.00 22.72 C ANISOU 3177 CD2 TRP A 407 2864 2901 2869 -10 6 -24 C ATOM 3178 CE2 TRP A 407 -9.074 -57.154 -10.053 1.00 22.43 C ANISOU 3178 CE2 TRP A 407 2823 2868 2833 -16 7 -21 C ATOM 3179 CE3 TRP A 407 -8.199 -55.217 -11.227 1.00 22.85 C ANISOU 3179 CE3 TRP A 407 2888 2901 2891 -4 3 -10 C ATOM 3180 NE1 TRP A 407 -10.253 -57.548 -9.477 1.00 22.82 N ANISOU 3180 NE1 TRP A 407 2855 2943 2872 -30 11 -37 N ATOM 3181 CZ2 TRP A 407 -7.838 -57.835 -10.160 1.00 21.98 C ANISOU 3181 CZ2 TRP A 407 2777 2796 2780 -9 4 -10 C ATOM 3182 CZ3 TRP A 407 -6.971 -55.896 -11.332 1.00 22.38 C ANISOU 3182 CZ3 TRP A 407 2833 2835 2834 -1 0 -1 C ATOM 3183 CH2 TRP A 407 -6.810 -57.194 -10.807 1.00 22.15 C ANISOU 3183 CH2 TRP A 407 2804 2807 2805 -1 1 -1 C ATOM 3184 N ASP A 408 -13.920 -54.238 -12.462 1.00 29.45 N ANISOU 3184 N ASP A 408 3616 3869 3705 35 -18 -165 N ATOM 3185 CA ASP A 408 -15.114 -54.832 -13.038 1.00 30.51 C ANISOU 3185 CA ASP A 408 3677 4063 3854 45 -54 -216 C ATOM 3186 C ASP A 408 -15.065 -54.974 -14.581 1.00 31.18 C ANISOU 3186 C ASP A 408 3764 4132 3950 66 -107 -201 C ATOM 3187 O ASP A 408 -15.490 -55.992 -15.146 1.00 31.59 O ANISOU 3187 O ASP A 408 3787 4201 4015 42 -141 -203 O ATOM 3188 CB ASP A 408 -16.346 -54.040 -12.614 1.00 31.41 C ANISOU 3188 CB ASP A 408 3721 4224 3989 73 -91 -257 C ATOM 3189 CG ASP A 408 -16.751 -54.318 -11.173 1.00 31.46 C ANISOU 3189 CG ASP A 408 3695 4266 3993 38 -55 -273 C ATOM 3190 OD1 ASP A 408 -15.889 -54.273 -10.266 1.00 30.80 O ANISOU 3190 OD1 ASP A 408 3674 4160 3870 18 -18 -263 O ATOM 3191 OD2 ASP A 408 -17.941 -54.596 -10.941 1.00 32.55 O1- ANISOU 3191 OD2 ASP A 408 3736 4460 4172 30 -72 -296 O1- ATOM 3192 N LYS A 409 -14.553 -53.956 -15.261 1.00 32.57 N ANISOU 3192 N LYS A 409 3984 4277 4115 110 -127 -190 N ATOM 3193 CA LYS A 409 -14.456 -54.030 -16.709 1.00 33.49 C ANISOU 3193 CA LYS A 409 4133 4380 4213 139 -188 -176 C ATOM 3194 C LYS A 409 -13.556 -55.205 -17.108 1.00 33.05 C ANISOU 3194 C LYS A 409 4100 4303 4153 88 -159 -143 C ATOM 3195 O LYS A 409 -13.878 -55.975 -18.039 1.00 33.73 O ANISOU 3195 O LYS A 409 4192 4403 4223 83 -214 -152 O ATOM 3196 CB LYS A 409 -13.921 -52.711 -17.268 1.00 33.79 C ANISOU 3196 CB LYS A 409 4244 4376 4218 196 -207 -157 C ATOM 3197 CG LYS A 409 -14.132 -52.518 -18.761 1.00 35.44 C ANISOU 3197 CG LYS A 409 4522 4575 4367 261 -282 -149 C ATOM 3198 CD LYS A 409 -15.610 -52.551 -19.113 1.00 36.88 C ANISOU 3198 CD LYS A 409 4650 4814 4546 317 -374 -194 C ATOM 3199 CE LYS A 409 -15.852 -52.576 -20.625 1.00 38.35 C ANISOU 3199 CE LYS A 409 4915 4999 4659 389 -462 -194 C ATOM 3200 NZ LYS A 409 -17.320 -52.774 -20.836 1.00 39.78 N1+ ANISOU 3200 NZ LYS A 409 5009 5249 4856 435 -564 -252 N1+ ATOM 3201 N LEU A 410 -12.443 -55.343 -16.384 1.00 28.68 N ANISOU 3201 N LEU A 410 3563 3724 3611 56 -81 -112 N ATOM 3202 CA LEU A 410 -11.478 -56.419 -16.615 1.00 27.89 C ANISOU 3202 CA LEU A 410 3479 3609 3509 18 -52 -80 C ATOM 3203 C LEU A 410 -12.124 -57.811 -16.431 1.00 27.98 C ANISOU 3203 C LEU A 410 3468 3643 3522 -13 -64 -96 C ATOM 3204 O LEU A 410 -12.061 -58.695 -17.312 1.00 28.42 O ANISOU 3204 O LEU A 410 3541 3689 3567 -34 -108 -95 O ATOM 3205 CB LEU A 410 -10.270 -56.231 -15.676 1.00 26.75 C ANISOU 3205 CB LEU A 410 3356 3430 3377 -3 1 -30 C ATOM 3206 CG LEU A 410 -9.118 -57.231 -15.805 1.00 26.35 C ANISOU 3206 CG LEU A 410 3327 3361 3323 -12 4 -14 C ATOM 3207 CD1 LEU A 410 -8.408 -57.157 -17.171 1.00 26.35 C ANISOU 3207 CD1 LEU A 410 3335 3357 3321 -20 4 -7 C ATOM 3208 CD2 LEU A 410 -8.115 -57.058 -14.693 1.00 26.11 C ANISOU 3208 CD2 LEU A 410 3305 3313 3304 -4 2 -4 C ATOM 3209 N GLY A 411 -12.772 -57.991 -15.294 1.00 27.36 N ANISOU 3209 N GLY A 411 3360 3591 3446 -22 -37 -115 N ATOM 3210 CA GLY A 411 -13.525 -59.208 -15.079 1.00 28.15 C ANISOU 3210 CA GLY A 411 3429 3707 3560 -62 -62 -130 C ATOM 3211 C GLY A 411 -14.438 -59.475 -16.261 1.00 29.51 C ANISOU 3211 C GLY A 411 3568 3892 3752 -74 -155 -158 C ATOM 3212 O GLY A 411 -14.462 -60.583 -16.799 1.00 29.80 O ANISOU 3212 O GLY A 411 3612 3919 3793 -113 -193 -163 O ATOM 3213 N GLU A 412 -15.168 -58.441 -16.686 1.00 46.83 N ANISOU 3213 N GLU A 412 5735 6113 5946 -33 -201 -185 N ATOM 3214 CA GLU A 412 -16.139 -58.579 -17.758 1.00 48.36 C ANISOU 3214 CA GLU A 412 5893 6341 6139 -21 -302 -228 C ATOM 3215 C GLU A 412 -15.487 -59.134 -19.002 1.00 48.58 C ANISOU 3215 C GLU A 412 5990 6347 6121 -23 -341 -224 C ATOM 3216 O GLU A 412 -15.981 -60.106 -19.583 1.00 49.45 O ANISOU 3216 O GLU A 412 6084 6473 6232 -58 -402 -260 O ATOM 3217 CB GLU A 412 -16.827 -57.243 -18.075 1.00 49.41 C ANISOU 3217 CB GLU A 412 6006 6503 6263 58 -352 -255 C ATOM 3218 CG GLU A 412 -18.310 -57.369 -18.420 1.00 51.17 C ANISOU 3218 CG GLU A 412 6133 6791 6516 73 -449 -317 C ATOM 3219 CD GLU A 412 -19.141 -57.846 -17.223 1.00 51.51 C ANISOU 3219 CD GLU A 412 6069 6873 6629 11 -413 -336 C ATOM 3220 OE1 GLU A 412 -19.000 -57.256 -16.114 1.00 50.64 O ANISOU 3220 OE1 GLU A 412 5956 6760 6527 15 -337 -319 O ATOM 3221 OE2 GLU A 412 -19.928 -58.818 -17.380 1.00 52.53 O1- ANISOU 3221 OE2 GLU A 412 6121 7035 6803 -47 -460 -372 O1- ATOM 3222 N THR A 413 -14.384 -58.521 -19.416 1.00 37.62 N ANISOU 3222 N THR A 413 4679 4923 4694 12 -306 -188 N ATOM 3223 CA THR A 413 -13.743 -58.934 -20.658 1.00 38.07 C ANISOU 3223 CA THR A 413 4811 4963 4693 24 -336 -191 C ATOM 3224 C THR A 413 -13.148 -60.352 -20.586 1.00 37.45 C ANISOU 3224 C THR A 413 4742 4870 4618 -45 -306 -190 C ATOM 3225 O THR A 413 -12.925 -60.971 -21.633 1.00 38.09 O ANISOU 3225 O THR A 413 4874 4946 4653 -38 -346 -219 O ATOM 3226 CB THR A 413 -12.676 -57.916 -21.149 1.00 37.66 C ANISOU 3226 CB THR A 413 4841 4870 4597 76 -300 -153 C ATOM 3227 CG2 THR A 413 -13.032 -56.493 -20.688 1.00 37.88 C ANISOU 3227 CG2 THR A 413 4860 4895 4637 126 -297 -143 C ATOM 3228 OG1 THR A 413 -11.388 -58.269 -20.643 1.00 36.36 O ANISOU 3228 OG1 THR A 413 4684 4677 4452 29 -214 -116 O ATOM 3229 N TYR A 414 -12.856 -60.846 -19.377 1.00 37.64 N ANISOU 3229 N TYR A 414 4737 4878 4686 -95 -242 -157 N ATOM 3230 CA TYR A 414 -12.408 -62.244 -19.222 1.00 37.45 C ANISOU 3230 CA TYR A 414 4734 4830 4665 -147 -226 -154 C ATOM 3231 C TYR A 414 -13.372 -63.342 -18.736 1.00 38.06 C ANISOU 3231 C TYR A 414 4773 4904 4786 -204 -268 -178 C ATOM 3232 O TYR A 414 -12.919 -64.460 -18.447 1.00 37.75 O ANISOU 3232 O TYR A 414 4762 4817 4765 -226 -257 -167 O ATOM 3233 CB TYR A 414 -11.118 -62.316 -18.408 1.00 36.20 C ANISOU 3233 CB TYR A 414 4598 4611 4545 -101 -163 -108 C ATOM 3234 CG TYR A 414 -9.940 -61.736 -19.135 1.00 35.79 C ANISOU 3234 CG TYR A 414 4546 4582 4471 -52 -116 -125 C ATOM 3235 CD1 TYR A 414 -9.435 -60.484 -18.796 1.00 35.01 C ANISOU 3235 CD1 TYR A 414 4460 4468 4376 -37 -86 -80 C ATOM 3236 CD2 TYR A 414 -9.331 -62.439 -20.179 1.00 36.20 C ANISOU 3236 CD2 TYR A 414 4646 4635 4473 -75 -126 -145 C ATOM 3237 CE1 TYR A 414 -8.350 -59.952 -19.466 1.00 34.87 C ANISOU 3237 CE1 TYR A 414 4476 4439 4332 -39 -60 -60 C ATOM 3238 CE2 TYR A 414 -8.245 -61.911 -20.859 1.00 35.95 C ANISOU 3238 CE2 TYR A 414 4675 4574 4412 -51 -106 -117 C ATOM 3239 CZ TYR A 414 -7.761 -60.669 -20.500 1.00 35.37 C ANISOU 3239 CZ TYR A 414 4598 4487 4355 -40 -70 -74 C ATOM 3240 OH TYR A 414 -6.686 -60.146 -21.181 1.00 35.75 O ANISOU 3240 OH TYR A 414 4710 4497 4375 -32 -40 -53 O ATOM 3241 N LYS A 415 -14.656 -63.042 -18.561 1.00 46.98 N ANISOU 3241 N LYS A 415 5826 6074 5948 -217 -315 -212 N ATOM 3242 CA LYS A 415 -15.518 -64.004 -17.848 1.00 47.90 C ANISOU 3242 CA LYS A 415 5882 6188 6129 -287 -333 -230 C ATOM 3243 C LYS A 415 -15.637 -65.364 -18.552 1.00 48.82 C ANISOU 3243 C LYS A 415 6027 6282 6242 -364 -389 -269 C ATOM 3244 O LYS A 415 -15.904 -66.383 -17.895 1.00 49.24 O ANISOU 3244 O LYS A 415 6060 6294 6352 -427 -385 -267 O ATOM 3245 CB LYS A 415 -16.919 -63.451 -17.572 1.00 48.97 C ANISOU 3245 CB LYS A 415 5909 6384 6314 -293 -366 -269 C ATOM 3246 CG LYS A 415 -17.717 -63.165 -18.801 1.00 50.49 C ANISOU 3246 CG LYS A 415 6067 6625 6490 -274 -468 -334 C ATOM 3247 CD LYS A 415 -19.078 -62.652 -18.422 1.00 51.91 C ANISOU 3247 CD LYS A 415 6121 6869 6734 -272 -504 -376 C ATOM 3248 CE LYS A 415 -19.877 -62.365 -19.665 1.00 53.69 C ANISOU 3248 CE LYS A 415 6309 7145 6945 -228 -629 -450 C ATOM 3249 NZ LYS A 415 -21.232 -61.854 -19.280 1.00 54.97 N1+ ANISOU 3249 NZ LYS A 415 6327 7380 7179 -218 -670 -498 N1+ ATOM 3250 N ASP A 416 -15.455 -65.376 -19.867 1.00 44.91 N ANISOU 3250 N ASP A 416 5574 5807 5683 -348 -434 -320 N ATOM 3251 CA ASP A 416 -15.538 -66.626 -20.614 1.00 45.97 C ANISOU 3251 CA ASP A 416 5739 5922 5804 -413 -482 -388 C ATOM 3252 C ASP A 416 -14.184 -67.300 -20.893 1.00 45.19 C ANISOU 3252 C ASP A 416 5728 5780 5661 -394 -409 -386 C ATOM 3253 O ASP A 416 -14.097 -68.207 -21.717 1.00 46.07 O ANISOU 3253 O ASP A 416 5880 5869 5754 -421 -448 -462 O ATOM 3254 CB ASP A 416 -16.396 -66.480 -21.885 1.00 47.53 C ANISOU 3254 CB ASP A 416 5914 6162 5982 -388 -600 -476 C ATOM 3255 CG ASP A 416 -17.883 -66.338 -21.572 1.00 49.14 C ANISOU 3255 CG ASP A 416 5994 6412 6265 -428 -672 -513 C ATOM 3256 OD1 ASP A 416 -18.341 -66.895 -20.535 1.00 49.36 O ANISOU 3256 OD1 ASP A 416 5959 6422 6373 -516 -639 -492 O ATOM 3257 OD2 ASP A 416 -18.595 -65.665 -22.357 1.00 50.52 O1- ANISOU 3257 OD2 ASP A 416 6130 6642 6424 -364 -765 -564 O1- ATOM 3258 N HIS A 417 -13.112 -66.804 -20.290 1.00 37.72 N ANISOU 3258 N HIS A 417 4799 4827 4706 -336 -312 -320 N ATOM 3259 CA HIS A 417 -11.794 -67.368 -20.576 1.00 37.16 C ANISOU 3259 CA HIS A 417 4762 4725 4633 -287 -260 -345 C ATOM 3260 C HIS A 417 -11.667 -68.756 -19.981 1.00 37.46 C ANISOU 3260 C HIS A 417 4786 4707 4741 -319 -241 -385 C ATOM 3261 O HIS A 417 -12.076 -68.997 -18.851 1.00 37.27 O ANISOU 3261 O HIS A 417 4697 4648 4816 -310 -236 -373 O ATOM 3262 CB HIS A 417 -10.644 -66.464 -20.098 1.00 35.80 C ANISOU 3262 CB HIS A 417 4582 4550 4471 -199 -200 -282 C ATOM 3263 CG HIS A 417 -9.338 -66.730 -20.788 1.00 35.56 C ANISOU 3263 CG HIS A 417 4624 4485 4403 -164 -192 -279 C ATOM 3264 CD2 HIS A 417 -8.720 -66.082 -21.805 1.00 35.46 C ANISOU 3264 CD2 HIS A 417 4670 4474 4328 -122 -194 -267 C ATOM 3265 ND1 HIS A 417 -8.502 -67.776 -20.437 1.00 35.58 N ANISOU 3265 ND1 HIS A 417 4656 4437 4427 -163 -173 -275 N ATOM 3266 CE1 HIS A 417 -7.430 -67.758 -21.211 1.00 35.60 C ANISOU 3266 CE1 HIS A 417 4719 4426 4383 -127 -156 -271 C ATOM 3267 NE2 HIS A 417 -7.529 -66.730 -22.041 1.00 35.57 N ANISOU 3267 NE2 HIS A 417 4735 4452 4330 -101 -165 -265 N ATOM 3268 N GLU A 418 -11.076 -69.657 -20.756 1.00 49.93 N ANISOU 3268 N GLU A 418 6436 6236 6300 -325 -266 -431 N ATOM 3269 CA GLU A 418 -10.778 -71.015 -20.317 1.00 50.47 C ANISOU 3269 CA GLU A 418 6526 6220 6431 -355 -257 -461 C ATOM 3270 C GLU A 418 -10.022 -71.037 -18.986 1.00 49.49 C ANISOU 3270 C GLU A 418 6394 6060 6351 -318 -215 -376 C ATOM 3271 O GLU A 418 -10.525 -71.572 -18.006 1.00 49.81 O ANISOU 3271 O GLU A 418 6408 6057 6461 -360 -212 -358 O ATOM 3272 CB GLU A 418 -9.983 -71.749 -21.405 1.00 51.26 C ANISOU 3272 CB GLU A 418 6726 6271 6479 -339 -281 -518 C ATOM 3273 CG GLU A 418 -10.281 -73.255 -21.566 1.00 52.94 C ANISOU 3273 CG GLU A 418 6982 6393 6742 -409 -304 -604 C ATOM 3274 CD GLU A 418 -9.572 -74.126 -20.531 1.00 52.88 C ANISOU 3274 CD GLU A 418 6994 6292 6805 -402 -263 -564 C ATOM 3275 OE1 GLU A 418 -8.642 -73.623 -19.839 1.00 51.39 O ANISOU 3275 OE1 GLU A 418 6806 6125 6595 -335 -223 -470 O ATOM 3276 OE2 GLU A 418 -9.946 -75.322 -20.411 1.00 54.54 O1- ANISOU 3276 OE2 GLU A 418 7231 6406 7087 -468 -272 -621 O1- ATOM 3277 N ASN A 419 -8.795 -70.506 -18.979 1.00 44.04 N ANISOU 3277 N ASN A 419 5740 5387 5607 -252 -182 -317 N ATOM 3278 CA ASN A 419 -7.941 -70.497 -17.774 1.00 43.23 C ANISOU 3278 CA ASN A 419 5645 5278 5503 -229 -136 -235 C ATOM 3279 C ASN A 419 -7.713 -69.194 -16.947 1.00 42.21 C ANISOU 3279 C ASN A 419 5476 5216 5346 -195 -96 -157 C ATOM 3280 O ASN A 419 -7.074 -69.249 -15.890 1.00 41.86 O ANISOU 3280 O ASN A 419 5436 5178 5289 -184 -63 -113 O ATOM 3281 CB ASN A 419 -6.591 -71.099 -18.123 1.00 43.23 C ANISOU 3281 CB ASN A 419 5707 5242 5476 -191 -120 -241 C ATOM 3282 CG ASN A 419 -5.981 -70.429 -19.306 1.00 43.29 C ANISOU 3282 CG ASN A 419 5731 5283 5436 -147 -117 -259 C ATOM 3283 ND2 ASN A 419 -6.198 -70.992 -20.494 1.00 44.05 N ANISOU 3283 ND2 ASN A 419 5878 5352 5509 -153 -148 -333 N ATOM 3284 OD1 ASN A 419 -5.336 -69.393 -19.165 1.00 42.53 O ANISOU 3284 OD1 ASN A 419 5607 5233 5321 -114 -84 -210 O ATOM 3285 N ILE A 420 -8.197 -68.037 -17.394 1.00 34.86 N ANISOU 3285 N ILE A 420 4512 4330 4404 -178 -101 -152 N ATOM 3286 CA ILE A 420 -7.911 -66.809 -16.648 1.00 33.80 C ANISOU 3286 CA ILE A 420 4353 4245 4245 -151 -50 -89 C ATOM 3287 C ILE A 420 -9.039 -66.428 -15.707 1.00 33.66 C ANISOU 3287 C ILE A 420 4300 4252 4237 -170 -45 -81 C ATOM 3288 O ILE A 420 -10.193 -66.399 -16.108 1.00 34.19 O ANISOU 3288 O ILE A 420 4338 4312 4339 -194 -91 -118 O ATOM 3289 CB ILE A 420 -7.625 -65.625 -17.583 1.00 33.57 C ANISOU 3289 CB ILE A 420 4321 4235 4200 -122 -44 -82 C ATOM 3290 CG1 ILE A 420 -6.295 -65.829 -18.319 1.00 33.50 C ANISOU 3290 CG1 ILE A 420 4345 4209 4175 -105 -31 -84 C ATOM 3291 CG2 ILE A 420 -7.599 -64.327 -16.779 1.00 32.68 C ANISOU 3291 CG2 ILE A 420 4175 4164 4078 -108 11 -35 C ATOM 3292 CD1 ILE A 420 -5.945 -64.693 -19.202 1.00 33.57 C ANISOU 3292 CD1 ILE A 420 4364 4225 4167 -90 -22 -77 C ATOM 3293 N VAL A 421 -8.689 -66.118 -14.461 1.00 31.95 N ANISOU 3293 N VAL A 421 4084 4066 3990 -155 1 -48 N ATOM 3294 CA VAL A 421 -9.658 -65.793 -13.411 1.00 31.88 C ANISOU 3294 CA VAL A 421 4055 4081 3979 -171 9 -51 C ATOM 3295 C VAL A 421 -9.343 -64.448 -12.736 1.00 31.15 C ANISOU 3295 C VAL A 421 3955 4005 3874 -103 29 -33 C ATOM 3296 O VAL A 421 -8.239 -64.260 -12.209 1.00 30.69 O ANISOU 3296 O VAL A 421 3898 3924 3838 -65 19 -23 O ATOM 3297 CB VAL A 421 -9.626 -66.848 -12.294 1.00 32.33 C ANISOU 3297 CB VAL A 421 4129 4115 4042 -206 9 -47 C ATOM 3298 CG1 VAL A 421 -10.375 -66.337 -11.093 1.00 32.32 C ANISOU 3298 CG1 VAL A 421 4108 4143 4030 -219 24 -48 C ATOM 3299 CG2 VAL A 421 -10.191 -68.165 -12.763 1.00 33.33 C ANISOU 3299 CG2 VAL A 421 4252 4178 4234 -271 -22 -70 C ATOM 3300 N ILE A 422 -10.306 -63.526 -12.741 1.00 26.88 N ANISOU 3300 N ILE A 422 3395 3489 3330 -109 33 -47 N ATOM 3301 CA ILE A 422 -10.139 -62.235 -12.089 1.00 26.38 C ANISOU 3301 CA ILE A 422 3318 3402 3302 -71 20 -34 C ATOM 3302 C ILE A 422 -10.877 -62.305 -10.770 1.00 26.64 C ANISOU 3302 C ILE A 422 3357 3457 3307 -82 27 -48 C ATOM 3303 O ILE A 422 -11.987 -62.869 -10.700 1.00 27.24 O ANISOU 3303 O ILE A 422 3405 3594 3350 -156 47 -85 O ATOM 3304 CB ILE A 422 -10.744 -61.087 -12.906 1.00 26.44 C ANISOU 3304 CB ILE A 422 3314 3418 3314 -62 19 -41 C ATOM 3305 CG1 ILE A 422 -10.254 -61.099 -14.371 1.00 26.34 C ANISOU 3305 CG1 ILE A 422 3317 3400 3293 -50 18 -38 C ATOM 3306 CG2 ILE A 422 -10.465 -59.755 -12.238 1.00 26.28 C ANISOU 3306 CG2 ILE A 422 3307 3386 3294 -37 15 -38 C ATOM 3307 CD1 ILE A 422 -8.776 -61.393 -14.563 1.00 25.80 C ANISOU 3307 CD1 ILE A 422 3254 3302 3245 -42 12 -21 C ATOM 3308 N ALA A 423 -10.275 -61.750 -9.712 1.00 28.52 N ANISOU 3308 N ALA A 423 3585 3680 3570 -74 20 -36 N ATOM 3309 CA ALA A 423 -10.894 -61.854 -8.392 1.00 28.66 C ANISOU 3309 CA ALA A 423 3611 3725 3555 -89 27 -49 C ATOM 3310 C ALA A 423 -10.445 -60.756 -7.441 1.00 28.38 C ANISOU 3310 C ALA A 423 3556 3681 3547 -79 20 -41 C ATOM 3311 O ALA A 423 -9.572 -59.948 -7.776 1.00 27.76 O ANISOU 3311 O ALA A 423 3495 3579 3473 -46 16 -35 O ATOM 3312 CB ALA A 423 -10.599 -63.212 -7.798 1.00 28.85 C ANISOU 3312 CB ALA A 423 3649 3749 3562 -115 27 -45 C ATOM 3313 N LYS A 424 -11.029 -60.750 -6.246 1.00 26.97 N ANISOU 3313 N LYS A 424 3365 3530 3353 -102 25 -51 N ATOM 3314 CA LYS A 424 -10.700 -59.755 -5.246 1.00 26.74 C ANISOU 3314 CA LYS A 424 3346 3510 3305 -82 24 -58 C ATOM 3315 C LYS A 424 -10.874 -60.274 -3.809 1.00 27.16 C ANISOU 3315 C LYS A 424 3393 3595 3330 -109 27 -61 C ATOM 3316 O LYS A 424 -11.613 -61.225 -3.565 1.00 27.68 O ANISOU 3316 O LYS A 424 3436 3727 3354 -194 40 -84 O ATOM 3317 CB LYS A 424 -11.515 -58.475 -5.472 1.00 26.76 C ANISOU 3317 CB LYS A 424 3333 3527 3308 -75 27 -78 C ATOM 3318 CG LYS A 424 -13.004 -58.661 -5.435 1.00 27.38 C ANISOU 3318 CG LYS A 424 3379 3665 3358 -112 34 -117 C ATOM 3319 CD LYS A 424 -13.711 -57.297 -5.306 1.00 27.73 C ANISOU 3319 CD LYS A 424 3389 3746 3402 -103 36 -153 C ATOM 3320 CE LYS A 424 -15.221 -57.453 -5.086 1.00 28.83 C ANISOU 3320 CE LYS A 424 3430 3984 3541 -147 71 -204 C ATOM 3321 NZ LYS A 424 -15.949 -56.265 -5.641 1.00 29.06 N1+ ANISOU 3321 NZ LYS A 424 3417 4031 3595 -111 63 -239 N1+ ATOM 3322 N MET A 425 -10.176 -59.645 -2.864 1.00 32.14 N ANISOU 3322 N MET A 425 4015 4232 3963 -97 22 -58 N ATOM 3323 CA MET A 425 -10.318 -59.967 -1.442 1.00 33.15 C ANISOU 3323 CA MET A 425 4097 4449 4051 -154 21 -70 C ATOM 3324 C MET A 425 -10.203 -58.720 -0.561 1.00 33.00 C ANISOU 3324 C MET A 425 4041 4473 4023 -129 19 -87 C ATOM 3325 O MET A 425 -9.314 -57.868 -0.750 1.00 31.94 O ANISOU 3325 O MET A 425 3953 4262 3922 -70 17 -78 O ATOM 3326 CB MET A 425 -9.271 -61.010 -0.998 1.00 33.52 C ANISOU 3326 CB MET A 425 4155 4493 4088 -165 26 -39 C ATOM 3327 CG MET A 425 -9.473 -61.568 0.430 1.00 35.17 C ANISOU 3327 CG MET A 425 4419 4709 4234 -134 133 24 C ATOM 3328 SD MET A 425 -8.658 -63.175 0.703 1.00 36.51 S ANISOU 3328 SD MET A 425 4694 4819 4357 -103 176 96 S ATOM 3329 CE MET A 425 -6.939 -62.692 0.774 1.00 35.91 C ANISOU 3329 CE MET A 425 4632 4740 4272 -43 97 58 C ATOM 3330 N ASP A 426 -11.084 -58.648 0.429 1.00 37.31 N ANISOU 3330 N ASP A 426 4569 5084 4524 -131 92 -80 N ATOM 3331 CA ASP A 426 -11.055 -57.559 1.389 1.00 37.88 C ANISOU 3331 CA ASP A 426 4624 5203 4565 -85 110 -102 C ATOM 3332 C ASP A 426 -9.933 -57.861 2.395 1.00 38.26 C ANISOU 3332 C ASP A 426 4724 5254 4560 -35 125 -82 C ATOM 3333 O ASP A 426 -10.055 -58.759 3.238 1.00 39.33 O ANISOU 3333 O ASP A 426 4950 5377 4615 -20 207 -38 O ATOM 3334 CB ASP A 426 -12.422 -57.481 2.097 1.00 39.19 C ANISOU 3334 CB ASP A 426 4789 5405 4696 -77 220 -92 C ATOM 3335 CG ASP A 426 -12.507 -56.337 3.079 1.00 40.22 C ANISOU 3335 CG ASP A 426 4919 5584 4778 -19 247 -130 C ATOM 3336 OD1 ASP A 426 -11.448 -55.786 3.457 1.00 39.95 O ANISOU 3336 OD1 ASP A 426 4901 5555 4725 19 189 -157 O ATOM 3337 OD2 ASP A 426 -13.642 -55.987 3.484 1.00 41.44 O1- ANISOU 3337 OD2 ASP A 426 5052 5774 4920 -7 331 -139 O1- ATOM 3338 N SER A 427 -8.892 -57.034 2.364 1.00 43.06 N ANISOU 3338 N SER A 427 5291 5874 5198 -5 57 -120 N ATOM 3339 CA SER A 427 -7.646 -57.377 3.037 1.00 43.45 C ANISOU 3339 CA SER A 427 5388 5919 5202 50 46 -118 C ATOM 3340 C SER A 427 -7.612 -56.852 4.460 1.00 45.14 C ANISOU 3340 C SER A 427 5670 6175 5306 113 65 -150 C ATOM 3341 O SER A 427 -6.664 -57.090 5.205 1.00 46.01 O ANISOU 3341 O SER A 427 5838 6293 5349 165 33 -163 O ATOM 3342 CB SER A 427 -6.432 -56.873 2.241 1.00 42.13 C ANISOU 3342 CB SER A 427 5131 5742 5134 59 -10 -148 C ATOM 3343 OG SER A 427 -5.220 -57.169 2.924 1.00 42.91 O ANISOU 3343 OG SER A 427 5279 5841 5185 126 -30 -167 O ATOM 3344 N THR A 428 -8.648 -56.106 4.810 1.00 40.51 N ANISOU 3344 N THR A 428 5075 5620 4697 113 107 -172 N ATOM 3345 CA THR A 428 -8.891 -55.699 6.187 1.00 42.58 C ANISOU 3345 CA THR A 428 5416 5926 4837 166 149 -202 C ATOM 3346 C THR A 428 -9.539 -56.858 6.968 1.00 43.81 C ANISOU 3346 C THR A 428 5689 6082 4876 143 257 -141 C ATOM 3347 O THR A 428 -9.315 -56.995 8.177 1.00 45.45 O ANISOU 3347 O THR A 428 5993 6331 4947 180 278 -148 O ATOM 3348 CB THR A 428 -9.791 -54.429 6.243 1.00 42.81 C ANISOU 3348 CB THR A 428 5393 5986 4887 179 172 -256 C ATOM 3349 CG2 THR A 428 -9.142 -53.282 5.454 1.00 41.21 C ANISOU 3349 CG2 THR A 428 5095 5770 4793 182 76 -311 C ATOM 3350 OG1 THR A 428 -11.082 -54.714 5.682 1.00 42.49 O ANISOU 3350 OG1 THR A 428 5317 5941 4887 131 245 -220 O ATOM 3351 N ALA A 429 -10.342 -57.666 6.262 1.00 35.10 N ANISOU 3351 N ALA A 429 4572 4939 3825 80 325 -85 N ATOM 3352 CA ALA A 429 -11.119 -58.754 6.856 1.00 36.51 C ANISOU 3352 CA ALA A 429 4849 5103 3919 29 459 -26 C ATOM 3353 C ALA A 429 -10.525 -60.151 6.711 1.00 36.70 C ANISOU 3353 C ALA A 429 4945 5082 3916 -25 444 33 C ATOM 3354 O ALA A 429 -11.116 -61.122 7.174 1.00 38.08 O ANISOU 3354 O ALA A 429 5156 5278 4034 -106 518 83 O ATOM 3355 CB ALA A 429 -12.552 -58.745 6.314 1.00 36.58 C ANISOU 3355 CB ALA A 429 4782 5103 4015 3 562 -3 C ATOM 3356 N ASN A 430 -9.399 -60.255 6.019 1.00 33.29 N ANISOU 3356 N ASN A 430 4489 4620 3538 3 331 26 N ATOM 3357 CA ASN A 430 -8.826 -61.557 5.714 1.00 33.57 C ANISOU 3357 CA ASN A 430 4568 4621 3567 -41 301 79 C ATOM 3358 C ASN A 430 -7.312 -61.559 5.787 1.00 33.55 C ANISOU 3358 C ASN A 430 4567 4632 3547 35 183 65 C ATOM 3359 O ASN A 430 -6.650 -60.711 5.196 1.00 32.34 O ANISOU 3359 O ASN A 430 4332 4469 3489 82 112 8 O ATOM 3360 CB ASN A 430 -9.272 -62.029 4.328 1.00 32.05 C ANISOU 3360 CB ASN A 430 4329 4326 3522 -50 320 99 C ATOM 3361 CG ASN A 430 -10.772 -62.200 4.222 1.00 32.47 C ANISOU 3361 CG ASN A 430 4326 4390 3623 -39 434 153 C ATOM 3362 ND2 ASN A 430 -11.452 -61.167 3.746 1.00 31.58 N ANISOU 3362 ND2 ASN A 430 4099 4331 3567 -61 426 105 N ATOM 3363 OD1 ASN A 430 -11.313 -63.250 4.560 1.00 33.56 O ANISOU 3363 OD1 ASN A 430 4413 4603 3733 -8 484 273 O ATOM 3364 N GLU A 431 -6.772 -62.529 6.513 1.00 56.62 N ANISOU 3364 N GLU A 431 7568 7578 6367 72 163 124 N ATOM 3365 CA GLU A 431 -5.332 -62.686 6.635 1.00 57.18 C ANISOU 3365 CA GLU A 431 7657 7636 6434 178 56 105 C ATOM 3366 C GLU A 431 -4.919 -64.053 6.110 1.00 57.66 C ANISOU 3366 C GLU A 431 7757 7639 6511 174 43 174 C ATOM 3367 O GLU A 431 -5.363 -65.080 6.617 1.00 59.14 O ANISOU 3367 O GLU A 431 8038 7815 6619 165 96 265 O ATOM 3368 CB GLU A 431 -4.900 -62.522 8.092 1.00 59.40 C ANISOU 3368 CB GLU A 431 8030 7969 6569 285 23 100 C ATOM 3369 CG GLU A 431 -3.450 -62.883 8.354 1.00 60.60 C ANISOU 3369 CG GLU A 431 8215 8108 6701 407 -92 76 C ATOM 3370 CD GLU A 431 -2.570 -61.664 8.537 1.00 60.46 C ANISOU 3370 CD GLU A 431 8118 8130 6725 480 -183 -41 C ATOM 3371 OE1 GLU A 431 -2.677 -60.723 7.726 1.00 58.95 O ANISOU 3371 OE1 GLU A 431 7806 7934 6657 427 -175 -98 O ATOM 3372 OE2 GLU A 431 -1.770 -61.648 9.493 1.00 62.18 O1- ANISOU 3372 OE2 GLU A 431 8394 8381 6849 595 -264 -76 O1- ATOM 3373 N VAL A 432 -4.075 -64.062 5.085 1.00 39.54 N ANISOU 3373 N VAL A 432 5396 5304 4325 186 -19 133 N ATOM 3374 CA VAL A 432 -3.610 -65.314 4.504 1.00 40.16 C ANISOU 3374 CA VAL A 432 5513 5319 4426 197 -35 183 C ATOM 3375 C VAL A 432 -2.106 -65.484 4.669 1.00 41.01 C ANISOU 3375 C VAL A 432 5638 5413 4530 321 -132 138 C ATOM 3376 O VAL A 432 -1.360 -64.512 4.717 1.00 39.99 O ANISOU 3376 O VAL A 432 5434 5322 4439 371 -187 50 O ATOM 3377 CB VAL A 432 -3.983 -65.434 3.013 1.00 38.37 C ANISOU 3377 CB VAL A 432 5199 5056 4322 104 -10 174 C ATOM 3378 CG1 VAL A 432 -5.384 -66.002 2.865 1.00 38.22 C ANISOU 3378 CG1 VAL A 432 5180 5041 4302 13 78 244 C ATOM 3379 CG2 VAL A 432 -3.871 -64.085 2.324 1.00 36.30 C ANISOU 3379 CG2 VAL A 432 4830 4810 4153 78 -28 87 C ATOM 3380 N GLU A 433 -1.679 -66.737 4.756 1.00 55.39 N ANISOU 3380 N GLU A 433 7556 7179 6313 374 -151 194 N ATOM 3381 CA GLU A 433 -0.283 -67.081 4.952 1.00 55.98 C ANISOU 3381 CA GLU A 433 7654 7242 6373 502 -248 150 C ATOM 3382 C GLU A 433 0.618 -66.522 3.875 1.00 54.04 C ANISOU 3382 C GLU A 433 7278 7003 6254 504 -290 50 C ATOM 3383 O GLU A 433 1.604 -65.841 4.168 1.00 53.93 O ANISOU 3383 O GLU A 433 7203 7035 6252 580 -358 -41 O ATOM 3384 CB GLU A 433 -0.142 -68.603 4.996 1.00 57.14 C ANISOU 3384 CB GLU A 433 7932 7305 6473 545 -248 235 C ATOM 3385 CG GLU A 433 1.265 -69.092 5.270 1.00 58.13 C ANISOU 3385 CG GLU A 433 8096 7420 6570 694 -356 191 C ATOM 3386 CD GLU A 433 2.128 -69.084 4.023 1.00 56.61 C ANISOU 3386 CD GLU A 433 7795 7215 6500 694 -392 110 C ATOM 3387 OE1 GLU A 433 1.774 -69.794 3.050 1.00 55.79 O ANISOU 3387 OE1 GLU A 433 7700 7041 6455 629 -345 149 O ATOM 3388 OE2 GLU A 433 3.156 -68.368 4.016 1.00 56.44 O1- ANISOU 3388 OE2 GLU A 433 7678 7252 6513 755 -463 2 O1- ATOM 3389 N ALA A 434 0.256 -66.809 2.625 1.00 51.06 N ANISOU 3389 N ALA A 434 6855 6579 5964 418 -242 63 N ATOM 3390 CA ALA A 434 1.141 -66.610 1.474 1.00 49.96 C ANISOU 3390 CA ALA A 434 6623 6431 5928 423 -264 -14 C ATOM 3391 C ALA A 434 1.355 -65.159 1.047 1.00 48.35 C ANISOU 3391 C ALA A 434 6289 6275 5806 389 -249 -98 C ATOM 3392 O ALA A 434 2.349 -64.842 0.389 1.00 47.60 O ANISOU 3392 O ALA A 434 6125 6187 5775 412 -265 -177 O ATOM 3393 CB ALA A 434 0.654 -67.446 0.283 1.00 49.77 C ANISOU 3393 CB ALA A 434 6616 6340 5956 352 -220 30 C ATOM 3394 N VAL A 435 0.430 -64.279 1.401 1.00 51.18 N ANISOU 3394 N VAL A 435 6622 6664 6159 333 -209 -82 N ATOM 3395 CA VAL A 435 0.545 -62.900 0.946 1.00 48.95 C ANISOU 3395 CA VAL A 435 6229 6412 5958 305 -182 -148 C ATOM 3396 C VAL A 435 0.261 -61.886 2.054 1.00 48.81 C ANISOU 3396 C VAL A 435 6198 6448 5898 328 -195 -174 C ATOM 3397 O VAL A 435 -0.676 -62.054 2.822 1.00 50.07 O ANISOU 3397 O VAL A 435 6424 6622 5980 309 -183 -119 O ATOM 3398 CB VAL A 435 -0.357 -62.643 -0.302 1.00 47.42 C ANISOU 3398 CB VAL A 435 5988 6189 5839 206 -108 -116 C ATOM 3399 CG1 VAL A 435 -1.813 -62.869 0.036 1.00 47.64 C ANISOU 3399 CG1 VAL A 435 6062 6215 5824 135 -82 -46 C ATOM 3400 CG2 VAL A 435 -0.140 -61.238 -0.861 1.00 45.72 C ANISOU 3400 CG2 VAL A 435 5699 5978 5695 165 -66 -153 C ATOM 3401 N LYS A 436 1.083 -60.840 2.131 1.00 40.49 N ANISOU 3401 N LYS A 436 5071 5424 4891 365 -215 -265 N ATOM 3402 CA LYS A 436 0.914 -59.789 3.133 1.00 40.84 C ANISOU 3402 CA LYS A 436 5098 5518 4903 392 -239 -307 C ATOM 3403 C LYS A 436 0.717 -58.374 2.524 1.00 39.64 C ANISOU 3403 C LYS A 436 4851 5369 4841 345 -186 -353 C ATOM 3404 O LYS A 436 1.576 -57.870 1.802 1.00 39.22 O ANISOU 3404 O LYS A 436 4762 5282 4856 308 -176 -391 O ATOM 3405 CB LYS A 436 2.105 -59.807 4.097 1.00 43.06 C ANISOU 3405 CB LYS A 436 5392 5833 5135 494 -338 -387 C ATOM 3406 CG LYS A 436 2.281 -61.125 4.849 1.00 45.65 C ANISOU 3406 CG LYS A 436 5833 6160 5350 567 -394 -335 C ATOM 3407 CD LYS A 436 0.980 -61.539 5.572 1.00 46.30 C ANISOU 3407 CD LYS A 436 6023 6247 5322 540 -353 -233 C ATOM 3408 CE LYS A 436 1.185 -62.827 6.368 1.00 48.38 C ANISOU 3408 CE LYS A 436 6422 6500 5459 620 -395 -171 C ATOM 3409 NZ LYS A 436 -0.025 -63.215 7.146 1.00 49.45 N1+ ANISOU 3409 NZ LYS A 436 6673 6641 5473 589 -334 -73 N1+ ATOM 3410 N VAL A 437 -0.413 -57.734 2.796 1.00 37.06 N ANISOU 3410 N VAL A 437 4517 5062 4501 308 -155 -322 N ATOM 3411 CA VAL A 437 -0.660 -56.427 2.188 1.00 36.52 C ANISOU 3411 CA VAL A 437 4409 4959 4505 232 -114 -325 C ATOM 3412 C VAL A 437 -0.768 -55.280 3.191 1.00 37.54 C ANISOU 3412 C VAL A 437 4499 5148 4615 287 -152 -407 C ATOM 3413 O VAL A 437 -1.561 -55.329 4.128 1.00 38.01 O ANISOU 3413 O VAL A 437 4595 5253 4593 313 -172 -396 O ATOM 3414 CB VAL A 437 -1.888 -56.445 1.258 1.00 35.38 C ANISOU 3414 CB VAL A 437 4298 4752 4394 133 -51 -224 C ATOM 3415 CG1 VAL A 437 -2.528 -57.822 1.245 1.00 35.06 C ANISOU 3415 CG1 VAL A 437 4273 4731 4318 133 -44 -178 C ATOM 3416 CG2 VAL A 437 -2.886 -55.376 1.668 1.00 35.60 C ANISOU 3416 CG2 VAL A 437 4307 4800 4418 120 -46 -232 C ATOM 3417 N HIS A 438 0.041 -54.247 2.974 1.00 69.36 N ANISOU 3417 N HIS A 438 8496 9154 8704 274 -165 -472 N ATOM 3418 CA HIS A 438 0.093 -53.097 3.857 1.00 70.70 C ANISOU 3418 CA HIS A 438 8617 9372 8874 329 -215 -576 C ATOM 3419 C HIS A 438 -0.515 -51.874 3.234 1.00 70.58 C ANISOU 3419 C HIS A 438 8592 9312 8915 251 -170 -555 C ATOM 3420 O HIS A 438 -0.930 -50.939 3.947 1.00 71.57 O ANISOU 3420 O HIS A 438 8681 9479 9034 289 -204 -630 O ATOM 3421 CB HIS A 438 1.535 -52.803 4.253 0.51 71.96 C ANISOU 3421 CB HIS A 438 8743 9538 9063 377 -289 -692 C ATOM 3422 CG HIS A 438 2.415 -52.404 3.091 0.48 71.73 C ANISOU 3422 CG HIS A 438 8671 9447 9136 315 -248 -711 C ATOM 3423 CD2 HIS A 438 3.165 -53.174 2.205 0.00 71.12 C ANISOU 3423 CD2 HIS A 438 8610 9331 9083 282 -222 -675 C ATOM 3424 ND1 HIS A 438 2.596 -51.123 2.726 0.30 72.13 N ANISOU 3424 ND1 HIS A 438 8675 9466 9265 273 -233 -764 N ATOM 3425 CE1 HIS A 438 3.419 -51.070 1.663 1.00 71.76 C ANISOU 3425 CE1 HIS A 438 8615 9366 9283 218 -194 -760 C ATOM 3426 NE2 HIS A 438 3.767 -52.326 1.344 1.00 71.31 N ANISOU 3426 NE2 HIS A 438 8598 9308 9189 225 -190 -707 N ATOM 3427 N SER A 439 -0.571 -51.845 1.907 1.00 55.16 N ANISOU 3427 N SER A 439 6676 7276 7006 166 -106 -463 N ATOM 3428 CA SER A 439 -1.140 -50.710 1.190 1.00 55.08 C ANISOU 3428 CA SER A 439 6672 7219 7035 118 -73 -436 C ATOM 3429 C SER A 439 -2.297 -51.161 0.311 1.00 53.98 C ANISOU 3429 C SER A 439 6591 7040 6877 59 -46 -307 C ATOM 3430 O SER A 439 -2.393 -52.334 -0.041 1.00 53.21 O ANISOU 3430 O SER A 439 6575 6920 6722 46 -33 -286 O ATOM 3431 CB SER A 439 -0.073 -50.018 0.342 1.00 55.18 C ANISOU 3431 CB SER A 439 6663 7188 7115 95 -59 -475 C ATOM 3432 OG SER A 439 0.770 -50.964 -0.286 1.00 54.73 O ANISOU 3432 OG SER A 439 6631 7111 7054 87 -45 -442 O ATOM 3433 N PHE A 440 -3.179 -50.233 -0.045 1.00 44.84 N ANISOU 3433 N PHE A 440 5437 5867 5733 43 -35 -303 N ATOM 3434 CA PHE A 440 -4.351 -50.603 -0.842 1.00 44.09 C ANISOU 3434 CA PHE A 440 5383 5750 5619 19 -15 -248 C ATOM 3435 C PHE A 440 -4.637 -49.626 -1.970 1.00 44.07 C ANISOU 3435 C PHE A 440 5434 5688 5622 2 -2 -263 C ATOM 3436 O PHE A 440 -4.506 -48.415 -1.789 1.00 44.42 O ANISOU 3436 O PHE A 440 5455 5723 5700 6 -6 -307 O ATOM 3437 CB PHE A 440 -5.598 -50.715 0.042 1.00 43.81 C ANISOU 3437 CB PHE A 440 5339 5754 5553 32 -21 -249 C ATOM 3438 CG PHE A 440 -5.328 -51.289 1.397 1.00 44.13 C ANISOU 3438 CG PHE A 440 5352 5856 5560 68 -38 -277 C ATOM 3439 CD1 PHE A 440 -5.458 -52.652 1.623 1.00 43.71 C ANISOU 3439 CD1 PHE A 440 5313 5821 5474 66 -33 -240 C ATOM 3440 CD2 PHE A 440 -4.947 -50.467 2.457 1.00 45.39 C ANISOU 3440 CD2 PHE A 440 5451 6093 5701 126 -77 -396 C ATOM 3441 CE1 PHE A 440 -5.208 -53.198 2.882 1.00 44.41 C ANISOU 3441 CE1 PHE A 440 5361 6025 5490 134 -60 -305 C ATOM 3442 CE2 PHE A 440 -4.695 -51.001 3.720 1.00 46.09 C ANISOU 3442 CE2 PHE A 440 5507 6285 5720 207 -116 -464 C ATOM 3443 CZ PHE A 440 -4.822 -52.372 3.926 1.00 45.67 C ANISOU 3443 CZ PHE A 440 5485 6256 5609 213 -103 -406 C ATOM 3444 N PRO A 441 -5.032 -50.153 -3.142 1.00 34.00 N ANISOU 3444 N PRO A 441 4154 4404 4362 -11 10 -193 N ATOM 3445 CA PRO A 441 -5.141 -51.586 -3.437 1.00 33.27 C ANISOU 3445 CA PRO A 441 4091 4309 4240 -15 12 -152 C ATOM 3446 C PRO A 441 -3.778 -52.255 -3.727 1.00 33.17 C ANISOU 3446 C PRO A 441 4109 4278 4215 -15 12 -163 C ATOM 3447 O PRO A 441 -2.818 -51.581 -4.101 1.00 33.58 O ANISOU 3447 O PRO A 441 4148 4316 4293 -18 17 -190 O ATOM 3448 CB PRO A 441 -5.994 -51.597 -4.696 1.00 32.81 C ANISOU 3448 CB PRO A 441 4061 4226 4181 -19 16 -120 C ATOM 3449 CG PRO A 441 -5.594 -50.379 -5.389 1.00 33.43 C ANISOU 3449 CG PRO A 441 4131 4286 4286 -22 22 -134 C ATOM 3450 CD PRO A 441 -5.336 -49.340 -4.328 1.00 33.93 C ANISOU 3450 CD PRO A 441 4188 4346 4357 -17 17 -198 C ATOM 3451 N THR A 442 -3.685 -53.567 -3.541 1.00 30.25 N ANISOU 3451 N THR A 442 3751 3916 3827 -13 9 -139 N ATOM 3452 CA THR A 442 -2.502 -54.298 -3.972 1.00 30.03 C ANISOU 3452 CA THR A 442 3725 3882 3805 -12 9 -137 C ATOM 3453 C THR A 442 -2.948 -55.343 -5.007 1.00 29.40 C ANISOU 3453 C THR A 442 3657 3786 3729 -17 12 -82 C ATOM 3454 O THR A 442 -3.978 -55.993 -4.853 1.00 29.26 O ANISOU 3454 O THR A 442 3665 3761 3691 -16 10 -68 O ATOM 3455 CB THR A 442 -1.692 -54.891 -2.770 1.00 30.24 C ANISOU 3455 CB THR A 442 3700 3949 3840 6 -4 -155 C ATOM 3456 CG2 THR A 442 -0.563 -55.774 -3.249 1.00 30.13 C ANISOU 3456 CG2 THR A 442 3685 3929 3833 11 -8 -159 C ATOM 3457 OG1 THR A 442 -1.110 -53.819 -2.007 1.00 30.99 O ANISOU 3457 OG1 THR A 442 3794 4052 3930 18 -14 -230 O ATOM 3458 N LEU A 443 -2.200 -55.457 -6.094 1.00 26.08 N ANISOU 3458 N LEU A 443 3242 3351 3316 -18 15 -78 N ATOM 3459 CA LEU A 443 -2.587 -56.333 -7.190 1.00 25.68 C ANISOU 3459 CA LEU A 443 3225 3279 3252 -15 11 -52 C ATOM 3460 C LEU A 443 -1.498 -57.363 -7.481 1.00 25.73 C ANISOU 3460 C LEU A 443 3229 3286 3261 -13 11 -56 C ATOM 3461 O LEU A 443 -0.294 -57.020 -7.670 1.00 25.74 O ANISOU 3461 O LEU A 443 3213 3291 3275 -17 15 -88 O ATOM 3462 CB LEU A 443 -2.871 -55.543 -8.460 1.00 25.85 C ANISOU 3462 CB LEU A 443 3245 3294 3283 -17 15 -41 C ATOM 3463 CG LEU A 443 -3.782 -54.310 -8.420 1.00 26.30 C ANISOU 3463 CG LEU A 443 3308 3347 3338 -16 15 -48 C ATOM 3464 CD1 LEU A 443 -4.039 -53.903 -9.852 1.00 26.38 C ANISOU 3464 CD1 LEU A 443 3325 3349 3349 -15 15 -37 C ATOM 3465 CD2 LEU A 443 -5.108 -54.579 -7.703 1.00 25.98 C ANISOU 3465 CD2 LEU A 443 3270 3310 3290 -14 11 -40 C ATOM 3466 N LYS A 444 -1.940 -58.623 -7.538 1.00 33.89 N ANISOU 3466 N LYS A 444 4275 4313 4290 -9 7 -33 N ATOM 3467 CA LYS A 444 -1.011 -59.727 -7.601 1.00 34.10 C ANISOU 3467 CA LYS A 444 4297 4341 4317 -7 6 -39 C ATOM 3468 C LYS A 444 -1.487 -60.844 -8.498 1.00 34.11 C ANISOU 3468 C LYS A 444 4309 4330 4321 -5 4 -14 C ATOM 3469 O LYS A 444 -2.647 -61.259 -8.439 1.00 34.27 O ANISOU 3469 O LYS A 444 4339 4341 4340 -1 1 -1 O ATOM 3470 CB LYS A 444 -0.708 -60.231 -6.181 1.00 34.29 C ANISOU 3470 CB LYS A 444 4310 4382 4337 -2 1 -54 C ATOM 3471 CG LYS A 444 0.560 -59.627 -5.610 1.00 34.64 C ANISOU 3471 CG LYS A 444 4327 4448 4387 9 -7 -105 C ATOM 3472 CD LYS A 444 0.549 -59.518 -4.096 1.00 35.10 C ANISOU 3472 CD LYS A 444 4372 4535 4431 29 -20 -130 C ATOM 3473 CE LYS A 444 1.721 -58.684 -3.619 1.00 35.36 C ANISOU 3473 CE LYS A 444 4338 4598 4498 53 -40 -179 C ATOM 3474 NZ LYS A 444 1.826 -58.717 -2.140 1.00 36.22 N1+ ANISOU 3474 NZ LYS A 444 4470 4730 4562 90 -63 -231 N1+ ATOM 3475 N PHE A 445 -0.560 -61.354 -9.296 1.00 25.88 N ANISOU 3475 N PHE A 445 3263 3289 3280 -6 5 -27 N ATOM 3476 CA PHE A 445 -0.860 -62.359 -10.304 1.00 26.03 C ANISOU 3476 CA PHE A 445 3289 3302 3298 -4 4 -15 C ATOM 3477 C PHE A 445 -0.259 -63.694 -9.919 1.00 26.34 C ANISOU 3477 C PHE A 445 3320 3344 3344 -3 3 -21 C ATOM 3478 O PHE A 445 0.871 -63.738 -9.427 1.00 26.46 O ANISOU 3478 O PHE A 445 3313 3369 3372 4 -4 -49 O ATOM 3479 CB PHE A 445 -0.277 -61.899 -11.630 1.00 25.86 C ANISOU 3479 CB PHE A 445 3262 3283 3282 -10 10 -30 C ATOM 3480 CG PHE A 445 -0.621 -62.777 -12.793 1.00 26.20 C ANISOU 3480 CG PHE A 445 3303 3325 3326 -13 13 -24 C ATOM 3481 CD1 PHE A 445 0.343 -63.113 -13.727 1.00 26.37 C ANISOU 3481 CD1 PHE A 445 3311 3349 3360 -23 26 -45 C ATOM 3482 CD2 PHE A 445 -1.896 -63.255 -12.969 1.00 26.36 C ANISOU 3482 CD2 PHE A 445 3333 3342 3340 -9 7 -11 C ATOM 3483 CE1 PHE A 445 0.034 -63.911 -14.828 1.00 26.64 C ANISOU 3483 CE1 PHE A 445 3351 3380 3391 -28 36 -47 C ATOM 3484 CE2 PHE A 445 -2.213 -64.056 -14.083 1.00 26.74 C ANISOU 3484 CE2 PHE A 445 3385 3392 3385 -15 15 -19 C ATOM 3485 CZ PHE A 445 -1.248 -64.380 -15.000 1.00 26.80 C ANISOU 3485 CZ PHE A 445 3385 3396 3401 -30 27 -32 C ATOM 3486 N PHE A 446 -1.012 -64.772 -10.163 1.00 25.24 N ANISOU 3486 N PHE A 446 3191 3199 3200 -2 2 -7 N ATOM 3487 CA PHE A 446 -0.607 -66.146 -9.861 1.00 26.46 C ANISOU 3487 CA PHE A 446 3341 3349 3362 4 -5 -18 C ATOM 3488 C PHE A 446 -0.773 -67.024 -11.099 1.00 26.45 C ANISOU 3488 C PHE A 446 3354 3333 3364 -3 -7 -30 C ATOM 3489 O PHE A 446 -1.851 -67.610 -11.307 1.00 26.67 O ANISOU 3489 O PHE A 446 3427 3343 3363 -26 -1 -18 O ATOM 3490 CB PHE A 446 -1.467 -66.735 -8.752 1.00 26.87 C ANISOU 3490 CB PHE A 446 3426 3391 3394 -2 -17 1 C ATOM 3491 CG PHE A 446 -1.491 -65.916 -7.496 1.00 26.87 C ANISOU 3491 CG PHE A 446 3412 3397 3401 1 -10 0 C ATOM 3492 CD1 PHE A 446 -2.376 -64.858 -7.354 1.00 25.44 C ANISOU 3492 CD1 PHE A 446 3222 3222 3222 0 0 0 C ATOM 3493 CD2 PHE A 446 -0.629 -66.208 -6.445 1.00 28.55 C ANISOU 3493 CD2 PHE A 446 3645 3593 3609 36 -40 -20 C ATOM 3494 CE1 PHE A 446 -2.395 -64.096 -6.177 1.00 25.36 C ANISOU 3494 CE1 PHE A 446 3209 3219 3209 -5 1 -2 C ATOM 3495 CE2 PHE A 446 -0.660 -65.457 -5.262 1.00 28.54 C ANISOU 3495 CE2 PHE A 446 3637 3613 3593 63 -46 -39 C ATOM 3496 CZ PHE A 446 -1.544 -64.399 -5.130 1.00 26.45 C ANISOU 3496 CZ PHE A 446 3333 3381 3337 17 -6 -21 C ATOM 3497 N PRO A 447 0.294 -67.125 -11.925 1.00 32.42 N ANISOU 3497 N PRO A 447 4080 4093 4146 11 -14 -63 N ATOM 3498 CA PRO A 447 0.253 -67.807 -13.226 1.00 32.68 C ANISOU 3498 CA PRO A 447 4180 4082 4156 8 3 -81 C ATOM 3499 C PRO A 447 -0.078 -69.291 -13.081 1.00 33.43 C ANISOU 3499 C PRO A 447 4335 4113 4256 15 -7 -103 C ATOM 3500 O PRO A 447 0.102 -69.845 -11.987 1.00 34.01 O ANISOU 3500 O PRO A 447 4444 4159 4317 41 -38 -88 O ATOM 3501 CB PRO A 447 1.692 -67.666 -13.756 1.00 32.67 C ANISOU 3501 CB PRO A 447 4138 4092 4181 36 10 -125 C ATOM 3502 CG PRO A 447 2.317 -66.587 -12.956 1.00 32.39 C ANISOU 3502 CG PRO A 447 4011 4113 4183 10 -15 -132 C ATOM 3503 CD PRO A 447 1.649 -66.628 -11.611 1.00 32.34 C ANISOU 3503 CD PRO A 447 4038 4104 4145 19 -29 -80 C ATOM 3504 N ALA A 448 -0.525 -69.919 -14.163 1.00 29.79 N ANISOU 3504 N ALA A 448 3911 3618 3789 7 -8 -124 N ATOM 3505 CA ALA A 448 -0.791 -71.350 -14.165 1.00 30.63 C ANISOU 3505 CA ALA A 448 4107 3642 3890 13 -29 -135 C ATOM 3506 C ALA A 448 0.486 -72.129 -14.461 1.00 31.28 C ANISOU 3506 C ALA A 448 4221 3675 3989 82 -24 -178 C ATOM 3507 O ALA A 448 1.317 -71.695 -15.254 1.00 30.93 O ANISOU 3507 O ALA A 448 4138 3661 3954 107 10 -215 O ATOM 3508 CB ALA A 448 -1.866 -71.686 -15.184 1.00 30.91 C ANISOU 3508 CB ALA A 448 4173 3655 3916 -30 -36 -151 C ATOM 3509 N SER A 449 0.616 -73.299 -13.847 1.00 41.68 N ANISOU 3509 N SER A 449 5615 4911 5310 116 -48 -173 N ATOM 3510 CA SER A 449 1.738 -74.191 -14.117 1.00 42.91 C ANISOU 3510 CA SER A 449 5811 5009 5485 204 -48 -213 C ATOM 3511 C SER A 449 3.075 -73.536 -13.810 1.00 42.70 C ANISOU 3511 C SER A 449 5706 5046 5471 274 -37 -228 C ATOM 3512 O SER A 449 4.049 -73.726 -14.535 1.00 43.50 O ANISOU 3512 O SER A 449 5789 5147 5594 334 -8 -279 O ATOM 3513 CB SER A 449 1.715 -74.661 -15.573 1.00 40.45 C ANISOU 3513 CB SER A 449 5530 4665 5176 205 -26 -273 C ATOM 3514 OG SER A 449 0.596 -75.490 -15.825 1.00 41.16 O ANISOU 3514 OG SER A 449 5697 4678 5265 150 -48 -275 O ATOM 3515 N ALA A 450 3.113 -72.765 -12.731 1.00 52.72 N ANISOU 3515 N ALA A 450 6929 6372 6730 266 -61 -193 N ATOM 3516 CA ALA A 450 4.338 -72.108 -12.301 1.00 52.84 C ANISOU 3516 CA ALA A 450 6861 6454 6760 324 -71 -215 C ATOM 3517 C ALA A 450 4.546 -72.346 -10.814 1.00 53.18 C ANISOU 3517 C ALA A 450 6928 6497 6782 378 -137 -189 C ATOM 3518 O ALA A 450 5.130 -71.518 -10.117 1.00 52.96 O ANISOU 3518 O ALA A 450 6827 6545 6751 393 -167 -205 O ATOM 3519 CB ALA A 450 4.276 -70.620 -12.599 1.00 51.66 C ANISOU 3519 CB ALA A 450 6622 6393 6615 255 -43 -214 C ATOM 3520 N ASP A 451 4.058 -73.485 -10.335 1.00 70.47 N ANISOU 3520 N ASP A 451 9230 8594 8951 402 -158 -154 N ATOM 3521 CA ASP A 451 4.132 -73.810 -8.919 1.00 71.12 C ANISOU 3521 CA ASP A 451 9370 8658 8995 456 -209 -115 C ATOM 3522 C ASP A 451 3.349 -72.786 -8.112 1.00 70.69 C ANISOU 3522 C ASP A 451 9290 8662 8905 382 -207 -85 C ATOM 3523 O ASP A 451 2.133 -72.668 -8.253 1.00 70.03 O ANISOU 3523 O ASP A 451 9235 8559 8815 288 -170 -52 O ATOM 3524 CB ASP A 451 5.584 -73.846 -8.453 1.00 72.40 C ANISOU 3524 CB ASP A 451 9481 8864 9165 580 -262 -157 C ATOM 3525 CG ASP A 451 6.197 -75.222 -8.570 1.00 74.21 C ANISOU 3525 CG ASP A 451 9789 9000 9406 691 -286 -160 C ATOM 3526 OD1 ASP A 451 6.713 -75.551 -9.658 1.00 74.74 O ANISOU 3526 OD1 ASP A 451 9825 9052 9521 718 -254 -208 O ATOM 3527 OD2 ASP A 451 6.162 -75.977 -7.577 1.00 75.38 O1- ANISOU 3527 OD2 ASP A 451 10041 9086 9514 758 -330 -112 O1- ATOM 3528 N ARG A 452 4.051 -72.039 -7.271 1.00 57.83 N ANISOU 3528 N ARG A 452 7604 7112 7259 427 -247 -110 N ATOM 3529 CA ARG A 452 3.408 -71.028 -6.449 1.00 57.61 C ANISOU 3529 CA ARG A 452 7555 7136 7197 371 -243 -98 C ATOM 3530 C ARG A 452 4.010 -69.651 -6.690 1.00 56.58 C ANISOU 3530 C ARG A 452 7300 7105 7092 340 -247 -166 C ATOM 3531 O ARG A 452 3.988 -68.794 -5.810 1.00 56.75 O ANISOU 3531 O ARG A 452 7301 7169 7093 333 -254 -191 O ATOM 3532 CB ARG A 452 3.499 -71.407 -4.972 1.00 58.51 C ANISOU 3532 CB ARG A 452 7746 7232 7254 443 -280 -64 C ATOM 3533 CG ARG A 452 2.765 -72.691 -4.632 1.00 59.43 C ANISOU 3533 CG ARG A 452 8001 7236 7342 447 -263 20 C ATOM 3534 CD ARG A 452 3.153 -73.207 -3.259 1.00 60.59 C ANISOU 3534 CD ARG A 452 8238 7364 7421 548 -309 62 C ATOM 3535 NE ARG A 452 2.673 -72.331 -2.197 1.00 61.01 N ANISOU 3535 NE ARG A 452 8280 7477 7426 524 -302 80 N ATOM 3536 CZ ARG A 452 1.426 -72.321 -1.745 1.00 61.14 C ANISOU 3536 CZ ARG A 452 8348 7466 7418 439 -242 152 C ATOM 3537 NH1 ARG A 452 0.526 -73.144 -2.264 1.00 60.93 N1+ ANISOU 3537 NH1 ARG A 452 8383 7352 7417 361 -186 205 N1+ ATOM 3538 NH2 ARG A 452 1.079 -71.490 -0.775 1.00 61.43 N ANISOU 3538 NH2 ARG A 452 8365 7567 7408 430 -236 163 N ATOM 3539 N THR A 453 4.544 -69.444 -7.888 1.00 33.09 N ANISOU 3539 N THR A 453 4252 4151 4168 318 -229 -199 N ATOM 3540 CA THR A 453 5.084 -68.151 -8.258 1.00 31.82 C ANISOU 3540 CA THR A 453 3990 4060 4040 262 -219 -257 C ATOM 3541 C THR A 453 4.002 -67.083 -8.146 1.00 31.03 C ANISOU 3541 C THR A 453 3888 3963 3940 154 -156 -196 C ATOM 3542 O THR A 453 2.832 -67.303 -8.498 1.00 30.96 O ANISOU 3542 O THR A 453 3906 3930 3926 111 -124 -131 O ATOM 3543 CB THR A 453 5.586 -68.136 -9.736 1.00 31.64 C ANISOU 3543 CB THR A 453 3911 4037 4075 242 -172 -273 C ATOM 3544 CG2 THR A 453 6.174 -66.784 -10.101 1.00 31.31 C ANISOU 3544 CG2 THR A 453 3788 4038 4071 174 -152 -329 C ATOM 3545 OG1 THR A 453 6.587 -69.140 -9.946 1.00 32.75 O ANISOU 3545 OG1 THR A 453 4050 4157 4238 343 -179 -299 O ATOM 3546 N VAL A 454 4.417 -65.925 -7.636 1.00 38.87 N ANISOU 3546 N VAL A 454 4852 4974 4941 128 -132 -212 N ATOM 3547 CA VAL A 454 3.599 -64.729 -7.605 1.00 37.78 C ANISOU 3547 CA VAL A 454 4720 4826 4809 77 -73 -166 C ATOM 3548 C VAL A 454 4.360 -63.564 -8.242 1.00 37.37 C ANISOU 3548 C VAL A 454 4634 4783 4784 55 -55 -200 C ATOM 3549 O VAL A 454 5.517 -63.309 -7.892 1.00 37.89 O ANISOU 3549 O VAL A 454 4666 4865 4865 72 -80 -266 O ATOM 3550 CB VAL A 454 3.305 -64.315 -6.171 1.00 37.89 C ANISOU 3550 CB VAL A 454 4739 4857 4798 92 -91 -166 C ATOM 3551 CG1 VAL A 454 2.123 -63.325 -6.142 1.00 37.04 C ANISOU 3551 CG1 VAL A 454 4637 4742 4693 57 -47 -124 C ATOM 3552 CG2 VAL A 454 3.046 -65.559 -5.283 1.00 39.91 C ANISOU 3552 CG2 VAL A 454 5040 5099 5024 160 -121 -169 C ATOM 3553 N ILE A 455 3.692 -62.854 -9.152 1.00 29.14 N ANISOU 3553 N ILE A 455 3574 3741 3756 23 -24 -150 N ATOM 3554 CA ILE A 455 4.221 -61.664 -9.808 1.00 28.99 C ANISOU 3554 CA ILE A 455 3533 3723 3759 2 -2 -175 C ATOM 3555 C ILE A 455 3.398 -60.434 -9.436 1.00 28.91 C ANISOU 3555 C ILE A 455 3569 3693 3721 -8 9 -165 C ATOM 3556 O ILE A 455 2.194 -60.453 -9.604 1.00 28.74 O ANISOU 3556 O ILE A 455 3559 3676 3686 -13 13 -105 O ATOM 3557 CB ILE A 455 4.112 -61.839 -11.331 1.00 28.90 C ANISOU 3557 CB ILE A 455 3533 3697 3751 -18 22 -161 C ATOM 3558 CG1 ILE A 455 4.721 -63.178 -11.756 1.00 29.28 C ANISOU 3558 CG1 ILE A 455 3597 3728 3800 -7 8 -198 C ATOM 3559 CG2 ILE A 455 4.726 -60.646 -12.080 1.00 28.93 C ANISOU 3559 CG2 ILE A 455 3552 3671 3770 -39 50 -209 C ATOM 3560 CD1 ILE A 455 4.267 -63.664 -13.111 1.00 29.23 C ANISOU 3560 CD1 ILE A 455 3575 3729 3802 -24 30 -160 C ATOM 3561 N ASP A 456 4.030 -59.362 -8.956 1.00 45.97 N ANISOU 3561 N ASP A 456 5706 5858 5903 -12 13 -210 N ATOM 3562 CA ASP A 456 3.293 -58.151 -8.566 1.00 45.98 C ANISOU 3562 CA ASP A 456 5684 5876 5911 -20 22 -178 C ATOM 3563 C ASP A 456 3.010 -57.252 -9.747 1.00 45.91 C ANISOU 3563 C ASP A 456 5719 5831 5896 -37 45 -183 C ATOM 3564 O ASP A 456 3.854 -57.096 -10.636 1.00 46.09 O ANISOU 3564 O ASP A 456 5727 5838 5947 -52 67 -215 O ATOM 3565 CB ASP A 456 4.057 -57.306 -7.528 1.00 46.58 C ANISOU 3565 CB ASP A 456 5755 5944 5998 -13 14 -258 C ATOM 3566 CG ASP A 456 4.110 -57.946 -6.154 1.00 46.87 C ANISOU 3566 CG ASP A 456 5785 6006 6017 17 -17 -274 C ATOM 3567 OD1 ASP A 456 3.334 -58.893 -5.905 1.00 46.97 O ANISOU 3567 OD1 ASP A 456 5826 6023 5997 25 -24 -224 O ATOM 3568 OD2 ASP A 456 4.953 -57.529 -5.332 1.00 47.44 O1- ANISOU 3568 OD2 ASP A 456 5820 6093 6110 35 -36 -343 O1- ATOM 3569 N TYR A 457 1.845 -56.610 -9.745 1.00 31.24 N ANISOU 3569 N TYR A 457 3883 3971 4016 -36 43 -145 N ATOM 3570 CA TYR A 457 1.545 -55.691 -10.827 1.00 31.39 C ANISOU 3570 CA TYR A 457 3888 3989 4050 -52 67 -127 C ATOM 3571 C TYR A 457 1.816 -54.293 -10.352 1.00 31.92 C ANISOU 3571 C TYR A 457 3962 4030 4137 -58 79 -175 C ATOM 3572 O TYR A 457 1.141 -53.792 -9.466 1.00 32.12 O ANISOU 3572 O TYR A 457 3958 4083 4163 -56 72 -152 O ATOM 3573 CB TYR A 457 0.109 -55.825 -11.322 1.00 31.04 C ANISOU 3573 CB TYR A 457 3879 3942 3972 -41 49 -81 C ATOM 3574 CG TYR A 457 -0.161 -54.937 -12.512 1.00 30.94 C ANISOU 3574 CG TYR A 457 3877 3918 3961 -46 70 -82 C ATOM 3575 CD1 TYR A 457 0.256 -55.308 -13.773 1.00 31.00 C ANISOU 3575 CD1 TYR A 457 3893 3917 3971 -56 89 -86 C ATOM 3576 CD2 TYR A 457 -0.808 -53.708 -12.363 1.00 31.17 C ANISOU 3576 CD2 TYR A 457 3921 3927 3994 -52 65 -89 C ATOM 3577 CE1 TYR A 457 0.056 -54.483 -14.862 1.00 31.31 C ANISOU 3577 CE1 TYR A 457 3949 3936 4010 -67 119 -87 C ATOM 3578 CE2 TYR A 457 -1.022 -52.875 -13.454 1.00 31.65 C ANISOU 3578 CE2 TYR A 457 3982 3984 4057 -57 102 -82 C ATOM 3579 CZ TYR A 457 -0.586 -53.278 -14.701 1.00 31.75 C ANISOU 3579 CZ TYR A 457 4026 3964 4075 -73 112 -91 C ATOM 3580 OH TYR A 457 -0.801 -52.476 -15.803 1.00 32.36 O ANISOU 3580 OH TYR A 457 4137 4007 4154 -82 150 -86 O ATOM 3581 N ASN A 458 2.893 -53.737 -10.891 1.00 40.50 N ANISOU 3581 N ASN A 458 5028 5092 5267 -78 114 -222 N ATOM 3582 CA ASN A 458 3.337 -52.382 -10.657 1.00 41.30 C ANISOU 3582 CA ASN A 458 5106 5167 5419 -102 142 -265 C ATOM 3583 C ASN A 458 3.093 -51.352 -11.783 1.00 42.04 C ANISOU 3583 C ASN A 458 5221 5220 5531 -121 190 -256 C ATOM 3584 O ASN A 458 3.599 -50.228 -11.706 1.00 43.13 O ANISOU 3584 O ASN A 458 5319 5339 5729 -123 271 -315 O ATOM 3585 CB ASN A 458 4.805 -52.395 -10.226 1.00 41.99 C ANISOU 3585 CB ASN A 458 5134 5258 5563 -90 179 -347 C ATOM 3586 CG ASN A 458 5.047 -53.259 -8.985 1.00 41.70 C ANISOU 3586 CG ASN A 458 5025 5292 5528 -88 125 -329 C ATOM 3587 ND2 ASN A 458 6.144 -54.012 -8.990 1.00 42.20 N ANISOU 3587 ND2 ASN A 458 5093 5325 5614 -71 128 -427 N ATOM 3588 OD1 ASN A 458 4.260 -53.246 -8.040 1.00 41.38 O ANISOU 3588 OD1 ASN A 458 5000 5270 5454 -68 92 -307 O ATOM 3589 N GLY A 459 2.412 -51.732 -12.860 1.00 35.63 N ANISOU 3589 N GLY A 459 4411 4448 4679 -107 215 -192 N ATOM 3590 CA GLY A 459 2.214 -50.814 -13.981 1.00 36.34 C ANISOU 3590 CA GLY A 459 4532 4501 4773 -120 273 -184 C ATOM 3591 C GLY A 459 0.998 -49.895 -13.889 1.00 36.19 C ANISOU 3591 C GLY A 459 4571 4433 4746 -119 235 -171 C ATOM 3592 O GLY A 459 0.545 -49.577 -12.792 1.00 36.09 O ANISOU 3592 O GLY A 459 4535 4443 4734 -109 204 -175 O ATOM 3593 N GLU A 460 0.483 -49.466 -15.044 1.00 47.51 N ANISOU 3593 N GLU A 460 6044 5855 6151 -100 297 -158 N ATOM 3594 CA GLU A 460 -0.692 -48.602 -15.123 1.00 47.65 C ANISOU 3594 CA GLU A 460 6088 5866 6150 -91 305 -131 C ATOM 3595 C GLU A 460 -1.953 -49.324 -14.662 1.00 46.95 C ANISOU 3595 C GLU A 460 5989 5817 6032 -79 189 -89 C ATOM 3596 O GLU A 460 -2.165 -50.488 -15.037 1.00 46.73 O ANISOU 3596 O GLU A 460 5946 5845 5965 -65 169 -69 O ATOM 3597 CB GLU A 460 -0.958 -48.195 -16.577 1.00 48.41 C ANISOU 3597 CB GLU A 460 6280 5890 6223 -100 396 -110 C ATOM 3598 CG GLU A 460 0.198 -47.579 -17.313 1.00 49.86 C ANISOU 3598 CG GLU A 460 6522 5971 6453 -139 552 -137 C ATOM 3599 CD GLU A 460 0.394 -46.136 -16.932 1.00 50.89 C ANISOU 3599 CD GLU A 460 6665 6031 6641 -176 643 -141 C ATOM 3600 OE1 GLU A 460 0.602 -45.867 -15.718 1.00 50.72 O ANISOU 3600 OE1 GLU A 460 6553 6039 6679 -189 616 -187 O ATOM 3601 OE2 GLU A 460 0.331 -45.271 -17.839 1.00 52.17 O1- ANISOU 3601 OE2 GLU A 460 6929 6107 6786 -195 713 -80 O1- ATOM 3602 N ARG A 461 -2.852 -48.647 -13.947 1.00 40.15 N ANISOU 3602 N ARG A 461 5116 4966 5172 -69 172 -82 N ATOM 3603 CA ARG A 461 -4.098 -49.324 -13.668 1.00 39.73 C ANISOU 3603 CA ARG A 461 5037 4977 5083 -45 125 -54 C ATOM 3604 C ARG A 461 -5.090 -48.845 -14.699 1.00 39.69 C ANISOU 3604 C ARG A 461 5086 4933 5061 -37 125 -33 C ATOM 3605 O ARG A 461 -5.824 -47.875 -14.520 1.00 40.26 O ANISOU 3605 O ARG A 461 5183 4985 5129 -31 181 -27 O ATOM 3606 CB ARG A 461 -4.561 -48.981 -12.256 1.00 39.68 C ANISOU 3606 CB ARG A 461 4998 4985 5094 -40 100 -64 C ATOM 3607 CG ARG A 461 -3.449 -49.092 -11.241 1.00 40.15 C ANISOU 3607 CG ARG A 461 5052 5028 5177 -54 94 -100 C ATOM 3608 CD ARG A 461 -3.862 -49.678 -9.898 1.00 39.96 C ANISOU 3608 CD ARG A 461 5015 5032 5136 -42 61 -102 C ATOM 3609 NE ARG A 461 -4.140 -48.641 -8.903 1.00 40.09 N ANISOU 3609 NE ARG A 461 5011 5042 5177 -41 67 -131 N ATOM 3610 CZ ARG A 461 -3.412 -48.448 -7.813 1.00 39.88 C ANISOU 3610 CZ ARG A 461 4962 5020 5169 -45 69 -169 C ATOM 3611 NH1 ARG A 461 -3.740 -47.495 -6.956 1.00 40.21 N1+ ANISOU 3611 NH1 ARG A 461 4982 5059 5238 -44 68 -202 N1+ ATOM 3612 NH2 ARG A 461 -2.357 -49.214 -7.583 1.00 39.69 N ANISOU 3612 NH2 ARG A 461 4934 5006 5142 -48 69 -181 N ATOM 3613 N THR A 462 -5.167 -49.636 -15.752 1.00 28.56 N ANISOU 3613 N THR A 462 3704 3524 3624 -31 116 -22 N ATOM 3614 CA THR A 462 -6.032 -49.356 -16.878 1.00 29.72 C ANISOU 3614 CA THR A 462 3930 3659 3703 1 134 -5 C ATOM 3615 C THR A 462 -6.286 -50.672 -17.547 1.00 29.55 C ANISOU 3615 C THR A 462 3894 3642 3692 1 79 0 C ATOM 3616 O THR A 462 -5.404 -51.552 -17.556 1.00 28.98 O ANISOU 3616 O THR A 462 3792 3582 3637 -23 83 -10 O ATOM 3617 CB THR A 462 -5.397 -48.388 -17.918 1.00 30.97 C ANISOU 3617 CB THR A 462 4229 3717 3820 18 239 4 C ATOM 3618 CG2 THR A 462 -4.855 -47.141 -17.229 1.00 30.72 C ANISOU 3618 CG2 THR A 462 4208 3634 3832 -5 321 3 C ATOM 3619 OG1 THR A 462 -4.336 -49.068 -18.602 1.00 30.82 O ANISOU 3619 OG1 THR A 462 4207 3688 3816 -2 266 -11 O ATOM 3620 N LEU A 463 -7.476 -50.800 -18.119 1.00 26.42 N ANISOU 3620 N LEU A 463 3533 3251 3255 43 42 -5 N ATOM 3621 CA LEU A 463 -7.817 -52.008 -18.839 1.00 26.38 C ANISOU 3621 CA LEU A 463 3543 3238 3242 55 10 -1 C ATOM 3622 C LEU A 463 -6.638 -52.402 -19.752 1.00 27.15 C ANISOU 3622 C LEU A 463 3696 3300 3319 39 58 1 C ATOM 3623 O LEU A 463 -6.236 -53.558 -19.789 1.00 26.38 O ANISOU 3623 O LEU A 463 3555 3222 3246 8 49 -1 O ATOM 3624 CB LEU A 463 -9.091 -51.764 -19.638 1.00 27.25 C ANISOU 3624 CB LEU A 463 3749 3325 3280 154 -49 -16 C ATOM 3625 CG LEU A 463 -9.769 -52.982 -20.239 1.00 27.26 C ANISOU 3625 CG LEU A 463 3715 3374 3267 162 -108 -27 C ATOM 3626 CD1 LEU A 463 -9.796 -54.151 -19.247 1.00 25.69 C ANISOU 3626 CD1 LEU A 463 3395 3225 3141 93 -99 -36 C ATOM 3627 CD2 LEU A 463 -11.171 -52.581 -20.675 1.00 28.14 C ANISOU 3627 CD2 LEU A 463 3836 3519 3337 238 -190 -51 C ATOM 3628 N ASP A 464 -6.050 -51.430 -20.441 1.00 39.51 N ANISOU 3628 N ASP A 464 5372 4806 4835 64 125 8 N ATOM 3629 CA ASP A 464 -4.927 -51.689 -21.338 1.00 39.56 C ANISOU 3629 CA ASP A 464 5454 4760 4819 56 199 12 C ATOM 3630 C ASP A 464 -3.690 -52.359 -20.704 1.00 38.27 C ANISOU 3630 C ASP A 464 5177 4632 4732 -8 211 -12 C ATOM 3631 O ASP A 464 -3.182 -53.380 -21.202 1.00 37.99 O ANISOU 3631 O ASP A 464 5151 4590 4693 -19 219 -13 O ATOM 3632 CB ASP A 464 -4.499 -50.374 -21.993 1.00 40.43 C ANISOU 3632 CB ASP A 464 5708 4783 4873 91 306 31 C ATOM 3633 CG ASP A 464 -5.314 -50.047 -23.210 1.00 41.87 C ANISOU 3633 CG ASP A 464 6018 4946 4944 170 279 83 C ATOM 3634 OD1 ASP A 464 -6.561 -49.957 -23.102 1.00 42.35 O ANISOU 3634 OD1 ASP A 464 6073 5042 4976 222 181 84 O ATOM 3635 OD2 ASP A 464 -4.707 -49.896 -24.293 1.00 42.68 O1- ANISOU 3635 OD2 ASP A 464 6230 5001 4986 188 352 119 O1- ATOM 3636 N GLY A 465 -3.186 -51.739 -19.638 1.00 28.04 N ANISOU 3636 N GLY A 465 3801 3368 3487 -29 211 -30 N ATOM 3637 CA GLY A 465 -2.058 -52.273 -18.898 1.00 27.10 C ANISOU 3637 CA GLY A 465 3604 3270 3424 -64 196 -41 C ATOM 3638 C GLY A 465 -2.336 -53.687 -18.410 1.00 26.52 C ANISOU 3638 C GLY A 465 3467 3280 3330 -60 149 -39 C ATOM 3639 O GLY A 465 -1.454 -54.563 -18.493 1.00 26.51 O ANISOU 3639 O GLY A 465 3452 3281 3339 -70 159 -50 O ATOM 3640 N PHE A 466 -3.560 -53.931 -17.931 1.00 29.63 N ANISOU 3640 N PHE A 466 3837 3685 3735 -54 85 -27 N ATOM 3641 CA PHE A 466 -3.915 -55.276 -17.460 1.00 28.49 C ANISOU 3641 CA PHE A 466 3651 3590 3586 -40 50 -25 C ATOM 3642 C PHE A 466 -3.913 -56.289 -18.602 1.00 28.53 C ANISOU 3642 C PHE A 466 3682 3571 3586 -55 52 -21 C ATOM 3643 O PHE A 466 -3.365 -57.383 -18.450 1.00 28.40 O ANISOU 3643 O PHE A 466 3649 3577 3564 -51 54 -28 O ATOM 3644 CB PHE A 466 -5.266 -55.309 -16.734 1.00 28.05 C ANISOU 3644 CB PHE A 466 3565 3547 3543 -24 16 -11 C ATOM 3645 CG PHE A 466 -5.340 -54.410 -15.512 1.00 28.50 C ANISOU 3645 CG PHE A 466 3613 3609 3607 -14 11 -9 C ATOM 3646 CD1 PHE A 466 -4.308 -54.381 -14.572 1.00 28.06 C ANISOU 3646 CD1 PHE A 466 3555 3553 3552 -16 19 -18 C ATOM 3647 CD2 PHE A 466 -6.440 -53.586 -15.314 1.00 28.62 C ANISOU 3647 CD2 PHE A 466 3626 3625 3624 -6 4 -3 C ATOM 3648 CE1 PHE A 466 -4.373 -53.568 -13.454 1.00 28.33 C ANISOU 3648 CE1 PHE A 466 3583 3586 3594 -19 19 -20 C ATOM 3649 CE2 PHE A 466 -6.518 -52.749 -14.183 1.00 28.69 C ANISOU 3649 CE2 PHE A 466 3632 3633 3634 -5 5 -5 C ATOM 3650 CZ PHE A 466 -5.469 -52.742 -13.259 1.00 28.66 C ANISOU 3650 CZ PHE A 466 3626 3629 3634 -10 14 -17 C ATOM 3651 N LYS A 467 -4.522 -55.941 -19.736 1.00 30.72 N ANISOU 3651 N LYS A 467 4023 3831 3820 -43 64 -14 N ATOM 3652 CA LYS A 467 -4.536 -56.862 -20.871 1.00 31.77 C ANISOU 3652 CA LYS A 467 4246 3902 3923 -46 74 -9 C ATOM 3653 C LYS A 467 -3.124 -57.179 -21.369 1.00 32.18 C ANISOU 3653 C LYS A 467 4334 3923 3970 -59 134 -18 C ATOM 3654 O LYS A 467 -2.780 -58.350 -21.556 1.00 31.99 O ANISOU 3654 O LYS A 467 4317 3900 3939 -72 140 -23 O ATOM 3655 CB LYS A 467 -5.387 -56.327 -22.003 1.00 32.81 C ANISOU 3655 CB LYS A 467 4506 3996 3965 16 63 -1 C ATOM 3656 CG LYS A 467 -6.894 -56.416 -21.778 1.00 32.66 C ANISOU 3656 CG LYS A 467 4443 4032 3935 44 -17 -11 C ATOM 3657 CD LYS A 467 -7.645 -55.908 -23.020 1.00 34.05 C ANISOU 3657 CD LYS A 467 4721 4203 4013 122 -58 -15 C ATOM 3658 CE LYS A 467 -9.142 -55.857 -22.814 1.00 34.37 C ANISOU 3658 CE LYS A 467 4712 4295 4054 153 -145 -42 C ATOM 3659 NZ LYS A 467 -9.876 -55.433 -24.065 1.00 36.06 N1+ ANISOU 3659 NZ LYS A 467 5027 4508 4167 241 -210 -50 N1+ ATOM 3660 N LYS A 468 -2.291 -56.157 -21.567 1.00 47.84 N ANISOU 3660 N LYS A 468 6353 5867 5955 -58 197 -24 N ATOM 3661 CA LYS A 468 -0.900 -56.416 -21.942 1.00 48.35 C ANISOU 3661 CA LYS A 468 6450 5890 6030 -77 282 -39 C ATOM 3662 C LYS A 468 -0.278 -57.420 -20.973 1.00 47.63 C ANISOU 3662 C LYS A 468 6241 5861 5993 -100 230 -59 C ATOM 3663 O LYS A 468 0.287 -58.463 -21.359 1.00 48.29 O ANISOU 3663 O LYS A 468 6349 5928 6072 -113 269 -68 O ATOM 3664 CB LYS A 468 -0.091 -55.118 -21.958 1.00 50.23 C ANISOU 3664 CB LYS A 468 6717 6079 6291 -85 371 -51 C ATOM 3665 CG LYS A 468 -0.495 -54.147 -23.057 1.00 51.35 C ANISOU 3665 CG LYS A 468 6996 6157 6357 -44 445 -16 C ATOM 3666 CD LYS A 468 0.330 -52.873 -23.000 1.00 52.14 C ANISOU 3666 CD LYS A 468 7115 6208 6488 -63 554 -20 C ATOM 3667 CE LYS A 468 -0.057 -51.913 -24.112 1.00 53.49 C ANISOU 3667 CE LYS A 468 7421 6338 6565 -21 622 40 C ATOM 3668 NZ LYS A 468 0.727 -50.649 -24.053 1.00 54.50 N1+ ANISOU 3668 NZ LYS A 468 7569 6409 6729 -55 743 50 N1+ ATOM 3669 N PHE A 469 -0.410 -57.096 -19.696 1.00 29.22 N ANISOU 3669 N PHE A 469 3810 3618 3673 -82 174 -56 N ATOM 3670 CA PHE A 469 0.180 -57.879 -18.626 1.00 28.45 C ANISOU 3670 CA PHE A 469 3663 3528 3619 -94 134 -69 C ATOM 3671 C PHE A 469 -0.271 -59.347 -18.683 1.00 28.02 C ANISOU 3671 C PHE A 469 3598 3512 3536 -73 114 -65 C ATOM 3672 O PHE A 469 0.563 -60.244 -18.731 1.00 28.36 O ANISOU 3672 O PHE A 469 3634 3534 3608 -94 119 -72 O ATOM 3673 CB PHE A 469 -0.175 -57.215 -17.279 1.00 27.90 C ANISOU 3673 CB PHE A 469 3558 3487 3554 -80 101 -66 C ATOM 3674 CG PHE A 469 0.467 -57.848 -16.082 1.00 27.64 C ANISOU 3674 CG PHE A 469 3498 3483 3522 -58 92 -81 C ATOM 3675 CD1 PHE A 469 -0.269 -58.664 -15.237 1.00 27.38 C ANISOU 3675 CD1 PHE A 469 3459 3466 3478 -39 53 -58 C ATOM 3676 CD2 PHE A 469 1.800 -57.609 -15.782 1.00 27.78 C ANISOU 3676 CD2 PHE A 469 3504 3474 3578 -83 110 -115 C ATOM 3677 CE1 PHE A 469 0.330 -59.248 -14.103 1.00 27.44 C ANISOU 3677 CE1 PHE A 469 3448 3482 3496 -36 47 -58 C ATOM 3678 CE2 PHE A 469 2.402 -58.182 -14.649 1.00 27.59 C ANISOU 3678 CE2 PHE A 469 3436 3486 3562 -68 108 -119 C ATOM 3679 CZ PHE A 469 1.671 -58.999 -13.812 1.00 27.41 C ANISOU 3679 CZ PHE A 469 3419 3477 3516 -48 68 -92 C ATOM 3680 N LEU A 470 -1.582 -59.565 -18.682 1.00 22.16 N ANISOU 3680 N LEU A 470 2855 2772 2795 -73 73 -43 N ATOM 3681 CA LEU A 470 -2.156 -60.906 -18.675 1.00 22.30 C ANISOU 3681 CA LEU A 470 2867 2811 2794 -60 62 -40 C ATOM 3682 C LEU A 470 -1.836 -61.705 -19.934 1.00 23.29 C ANISOU 3682 C LEU A 470 3051 2892 2906 -94 96 -40 C ATOM 3683 O LEU A 470 -1.501 -62.883 -19.859 1.00 23.62 O ANISOU 3683 O LEU A 470 3107 2928 2940 -107 117 -53 O ATOM 3684 CB LEU A 470 -3.672 -60.830 -18.489 1.00 21.88 C ANISOU 3684 CB LEU A 470 2804 2762 2748 -58 34 -24 C ATOM 3685 CG LEU A 470 -4.177 -60.459 -17.095 1.00 21.52 C ANISOU 3685 CG LEU A 470 2734 2733 2709 -29 19 -18 C ATOM 3686 CD1 LEU A 470 -5.619 -59.982 -17.148 1.00 21.17 C ANISOU 3686 CD1 LEU A 470 2686 2690 2668 -30 11 -12 C ATOM 3687 CD2 LEU A 470 -4.032 -61.634 -16.144 1.00 21.73 C ANISOU 3687 CD2 LEU A 470 2754 2759 2745 -25 14 -15 C ATOM 3688 N GLU A 471 -1.956 -61.062 -21.090 1.00 44.19 N ANISOU 3688 N GLU A 471 5802 5486 5503 -100 137 -43 N ATOM 3689 CA GLU A 471 -1.718 -61.728 -22.364 1.00 45.89 C ANISOU 3689 CA GLU A 471 6095 5705 5636 -49 155 -69 C ATOM 3690 C GLU A 471 -0.268 -62.161 -22.512 1.00 46.28 C ANISOU 3690 C GLU A 471 6139 5753 5693 -44 222 -92 C ATOM 3691 O GLU A 471 0.053 -63.000 -23.347 1.00 47.37 O ANISOU 3691 O GLU A 471 6323 5904 5770 -2 241 -126 O ATOM 3692 CB GLU A 471 -2.105 -60.819 -23.529 1.00 46.95 C ANISOU 3692 CB GLU A 471 6323 5821 5695 -11 171 -61 C ATOM 3693 CG GLU A 471 -3.464 -60.162 -23.384 1.00 46.71 C ANISOU 3693 CG GLU A 471 6292 5798 5659 -2 105 -48 C ATOM 3694 CD GLU A 471 -4.591 -61.041 -23.882 1.00 47.28 C ANISOU 3694 CD GLU A 471 6380 5903 5681 25 28 -82 C ATOM 3695 OE1 GLU A 471 -4.487 -62.277 -23.743 1.00 47.35 O ANISOU 3695 OE1 GLU A 471 6365 5925 5699 13 12 -113 O ATOM 3696 OE2 GLU A 471 -5.581 -60.495 -24.409 1.00 47.86 O1- ANISOU 3696 OE2 GLU A 471 6493 5986 5707 58 -21 -87 O1- ATOM 3697 N SER A 472 0.607 -61.583 -21.701 1.00 30.59 N ANISOU 3697 N SER A 472 4093 3752 3780 -84 253 -89 N ATOM 3698 CA SER A 472 2.021 -61.910 -21.768 1.00 31.19 C ANISOU 3698 CA SER A 472 4140 3837 3873 -73 318 -121 C ATOM 3699 C SER A 472 2.420 -62.882 -20.666 1.00 30.65 C ANISOU 3699 C SER A 472 3995 3796 3854 -75 277 -142 C ATOM 3700 O SER A 472 3.579 -63.275 -20.568 1.00 31.05 O ANISOU 3700 O SER A 472 4007 3866 3925 -50 316 -178 O ATOM 3701 CB SER A 472 2.872 -60.641 -21.700 1.00 31.31 C ANISOU 3701 CB SER A 472 4141 3818 3937 -105 385 -127 C ATOM 3702 OG SER A 472 3.132 -60.267 -20.362 1.00 30.64 O ANISOU 3702 OG SER A 472 3984 3721 3935 -149 339 -150 O ATOM 3703 N GLY A 473 1.454 -63.274 -19.841 1.00 33.55 N ANISOU 3703 N GLY A 473 4339 4173 4237 -95 206 -119 N ATOM 3704 CA GLY A 473 1.728 -64.204 -18.764 1.00 33.08 C ANISOU 3704 CA GLY A 473 4224 4137 4208 -85 172 -130 C ATOM 3705 C GLY A 473 2.521 -63.545 -17.645 1.00 32.33 C ANISOU 3705 C GLY A 473 4065 4054 4166 -103 145 -138 C ATOM 3706 O GLY A 473 3.241 -64.226 -16.921 1.00 32.51 O ANISOU 3706 O GLY A 473 4043 4089 4222 -95 139 -177 O ATOM 3707 N GLY A 474 2.381 -62.230 -17.510 1.00 46.92 N ANISOU 3707 N GLY A 474 5916 5920 5991 -80 129 -106 N ATOM 3708 CA GLY A 474 3.042 -61.488 -16.452 1.00 46.66 C ANISOU 3708 CA GLY A 474 5853 5895 5979 -75 121 -124 C ATOM 3709 C GLY A 474 4.505 -61.192 -16.715 1.00 47.86 C ANISOU 3709 C GLY A 474 5986 6004 6195 -119 166 -200 C ATOM 3710 O GLY A 474 5.187 -60.619 -15.869 1.00 47.91 O ANISOU 3710 O GLY A 474 5963 6014 6226 -117 159 -233 O ATOM 3711 N GLN A 475 4.991 -61.582 -17.888 1.00 69.99 N ANISOU 3711 N GLN A 475 8787 8774 9032 -151 264 -245 N ATOM 3712 CA GLN A 475 6.395 -61.388 -18.235 1.00 71.11 C ANISOU 3712 CA GLN A 475 8875 8933 9211 -134 348 -288 C ATOM 3713 C GLN A 475 6.660 -59.994 -18.793 1.00 71.75 C ANISOU 3713 C GLN A 475 8978 8970 9316 -171 428 -292 C ATOM 3714 O GLN A 475 7.809 -59.594 -18.961 1.00 72.77 O ANISOU 3714 O GLN A 475 9044 9109 9495 -178 509 -330 O ATOM 3715 CB GLN A 475 6.851 -62.451 -19.234 1.00 72.09 C ANISOU 3715 CB GLN A 475 9001 9097 9292 -67 410 -284 C ATOM 3716 CG GLN A 475 6.800 -63.869 -18.693 1.00 71.79 C ANISOU 3716 CG GLN A 475 8950 9093 9236 -1 348 -293 C ATOM 3717 CD GLN A 475 7.839 -64.123 -17.617 1.00 72.04 C ANISOU 3717 CD GLN A 475 8887 9154 9331 24 320 -343 C ATOM 3718 NE2 GLN A 475 8.753 -63.178 -17.442 1.00 72.86 N ANISOU 3718 NE2 GLN A 475 8919 9264 9500 -13 360 -384 N ATOM 3719 OE1 GLN A 475 7.820 -65.158 -16.953 1.00 71.90 O ANISOU 3719 OE1 GLN A 475 8867 9148 9304 83 263 -348 O ATOM 3720 N ASP A 476 5.593 -59.258 -19.076 1.00 57.32 N ANISOU 3720 N ASP A 476 7230 7095 7454 -188 411 -255 N ATOM 3721 CA ASP A 476 5.718 -57.901 -19.589 1.00 57.98 C ANISOU 3721 CA ASP A 476 7349 7130 7550 -206 491 -253 C ATOM 3722 C ASP A 476 4.657 -56.992 -18.983 1.00 57.13 C ANISOU 3722 C ASP A 476 7273 7021 7412 -190 408 -227 C ATOM 3723 O ASP A 476 3.539 -56.913 -19.482 1.00 56.80 O ANISOU 3723 O ASP A 476 7284 6988 7310 -166 368 -174 O ATOM 3724 CB ASP A 476 5.606 -57.895 -21.113 1.00 59.31 C ANISOU 3724 CB ASP A 476 7590 7293 7652 -187 584 -201 C ATOM 3725 CG ASP A 476 6.543 -56.898 -21.762 1.00 60.80 C ANISOU 3725 CG ASP A 476 7777 7455 7868 -210 725 -205 C ATOM 3726 OD1 ASP A 476 6.055 -56.027 -22.511 1.00 61.36 O ANISOU 3726 OD1 ASP A 476 7939 7481 7893 -208 780 -162 O ATOM 3727 OD2 ASP A 476 7.766 -56.987 -21.525 1.00 61.62 O1- ANISOU 3727 OD2 ASP A 476 7786 7586 8040 -231 786 -249 O1- ATOM 3728 N GLY A 477 5.013 -56.308 -17.901 1.00 59.19 N ANISOU 3728 N GLY A 477 7484 7304 7703 -186 375 -253 N ATOM 3729 CA GLY A 477 4.085 -55.420 -17.228 1.00 58.42 C ANISOU 3729 CA GLY A 477 7399 7237 7562 -151 301 -214 C ATOM 3730 C GLY A 477 4.550 -55.027 -15.841 1.00 58.15 C ANISOU 3730 C GLY A 477 7316 7228 7552 -142 268 -244 C ATOM 3731 O GLY A 477 5.176 -55.815 -15.135 1.00 57.83 O ANISOU 3731 O GLY A 477 7236 7210 7525 -138 239 -269 O ATOM 3732 N ALA A 478 4.234 -53.799 -15.450 1.00 68.89 N ANISOU 3732 N ALA A 478 8678 8579 8919 -140 282 -246 N ATOM 3733 CA ALA A 478 4.658 -53.263 -14.153 1.00 68.89 C ANISOU 3733 CA ALA A 478 8631 8593 8951 -137 271 -285 C ATOM 3734 C ALA A 478 5.999 -52.536 -14.283 1.00 70.58 C ANISOU 3734 C ALA A 478 8781 8749 9287 -196 389 -391 C ATOM 3735 O ALA A 478 6.943 -52.809 -13.530 1.00 71.17 O ANISOU 3735 O ALA A 478 8782 8835 9423 -206 387 -466 O ATOM 3736 CB ALA A 478 4.735 -54.366 -13.109 1.00 67.68 C ANISOU 3736 CB ALA A 478 8417 8526 8773 -114 211 -246 C CONECT 1 6 CONECT 2 3 8 9 CONECT 3 2 4 CONECT 4 3 5 CONECT 5 4 6 7 CONECT 6 1 5 CONECT 7 5 8 CONECT 8 2 7 CONECT 9 2 10 CONECT 10 9 11 CONECT 11 10 12 18 CONECT 12 11 13 17 CONECT 13 12 14 CONECT 14 13 15 20 CONECT 15 14 16 19 CONECT 16 15 17 CONECT 17 12 16 CONECT 18 11 CONECT 19 15 21 CONECT 20 14 CONECT 21 19 ENDMDL END