***    ***
Job options:
ID = 2410031413293844761
JOBID =
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
ATOM 1 N VAL A 31 14.803 29.611 60.496 1.00122.89 N
ANISOU 1 N VAL A 31 21367 13436 11891 -4519 -1805 -5164 N
ATOM 2 CA VAL A 31 15.613 28.402 60.562 1.00121.24 C
ANISOU 2 CA VAL A 31 20718 13779 11569 -4554 -2225 -5015 C
ATOM 3 C VAL A 31 15.789 27.878 59.130 1.00115.76 C
ANISOU 3 C VAL A 31 19647 13079 11259 -4518 -2184 -4728 C
ATOM 4 O VAL A 31 15.461 28.574 58.170 1.00114.23 O
ANISOU 4 O VAL A 31 19528 12473 11400 -4537 -1879 -4682 O
ATOM 5 CB VAL A 31 14.970 27.358 61.518 1.00119.33 C
ANISOU 5 CB VAL A 31 20604 13840 10895 -4217 -2287 -4923 C
ATOM 6 CG1 VAL A 31 13.712 26.756 60.907 1.00113.28 C
ANISOU 6 CG1 VAL A 31 19944 12887 10209 -3802 -1928 -4658 C
ATOM 7 CG2 VAL A 31 15.978 26.290 61.972 1.00120.17 C
ANISOU 7 CG2 VAL A 31 20322 14548 10790 -4284 -2794 -4830 C
ATOM 8 N TRP A 32 16.301 26.657 58.987 1.00120.55 N
ANISOU 8 N TRP A 32 19861 14137 11807 -4452 -2487 -4527 N
ATOM 9 CA TRP A 32 16.697 26.095 57.701 1.00116.34 C
ANISOU 9 CA TRP A 32 18915 13677 11612 -4470 -2516 -4280 C
ATOM 10 C TRP A 32 15.519 25.522 56.920 1.00110.38 C
ANISOU 10 C TRP A 32 18285 12702 10951 -4097 -2191 -4030 C
ATOM 11 O TRP A 32 15.727 24.892 55.878 1.00106.69 O
ANISOU 11 O TRP A 32 17508 12314 10716 -4066 -2211 -3810 O
ATOM 12 CB TRP A 32 17.749 25.007 57.931 1.00119.55 C
ANISOU 12 CB TRP A 32 18841 14674 11908 -4525 -2988 -4165 C
ATOM 13 CG TRP A 32 18.936 25.491 58.715 1.00125.92 C
ANISOU 13 CG TRP A 32 19471 15753 12620 -4872 -3349 -4398 C
ATOM 14 CD1 TRP A 32 19.252 26.787 59.016 1.00130.88 C
ANISOU 14 CD1 TRP A 32 20289 16129 13311 -5197 -3291 -4690 C
ATOM 15 CD2 TRP A 32 19.930 24.681 59.353 1.00128.60 C
ANISOU 15 CD2 TRP A 32 19426 16669 12767 -4907 -3834 -4356 C
ATOM 16 NE1 TRP A 32 20.394 26.833 59.776 1.00136.46 N
ANISOU 16 NE1 TRP A 32 20743 17224 13881 -5462 -3718 -4848 N
ATOM 17 CE2 TRP A 32 20.830 25.553 59.998 1.00135.21 C
ANISOU 17 CE2 TRP A 32 20217 17590 13568 -5275 -4061 -4641 C
ATOM 18 CE3 TRP A 32 20.154 23.303 59.429 1.00126.43 C
ANISOU 18 CE3 TRP A 32 18841 16842 12354 -4646 -4104 -4088 C
ATOM 19 CZ2 TRP A 32 21.935 25.092 60.709 1.00139.71 C
ANISOU 19 CZ2 TRP A 32 20418 18694 13972 -5381 -4557 -4670 C
ATOM 20 CZ3 TRP A 32 21.252 22.848 60.135 1.00130.86 C
ANISOU 20 CZ3 TRP A 32 19042 17923 12756 -4721 -4583 -4096 C
ATOM 21 CH2 TRP A 32 22.128 23.739 60.766 1.00137.44 C
ANISOU 21 CH2 TRP A 32 19813 18848 13558 -5082 -4811 -4388 C
ATOM 22 N VAL A 33 14.296 25.732 57.408 1.00110.70 N
ANISOU 22 N VAL A 33 18760 12482 10820 -3815 -1888 -4065 N
ATOM 23 CA VAL A 33 13.101 25.170 56.784 1.00105.66 C
ANISOU 23 CA VAL A 33 18240 11659 10247 -3437 -1583 -3836 C
ATOM 24 C VAL A 33 12.735 25.913 55.502 1.00103.88 C
ANISOU 24 C VAL A 33 18039 10996 10435 -3441 -1258 -3761 C
ATOM 25 O VAL A 33 12.148 25.323 54.586 1.00102.15 O
ANISOU 25 O VAL A 33 17675 10730 10408 -3174 -1096 -3491 O
ATOM 26 CB VAL A 33 11.948 25.178 57.806 1.00108.73 C
ANISOU 26 CB VAL A 33 19039 11955 10319 -3137 -1356 -3900 C
ATOM 27 CG1 VAL A 33 10.626 24.847 57.155 1.00105.08 C
ANISOU 27 CG1 VAL A 33 18705 11247 9972 -2756 -981 -3696 C
ATOM 28 CG2 VAL A 33 12.235 24.186 58.925 1.00110.02 C
ANISOU 28 CG2 VAL A 33 19158 12581 10064 -3074 -1665 -3878 C
ATOM 29 N VAL A 34 13.083 27.200 55.406 1.00103.89 N
ANISOU 29 N VAL A 34 18161 10704 10610 -3689 -1154 -3940 N
ATOM 30 CA VAL A 34 12.740 27.995 54.227 1.00102.66 C
ANISOU 30 CA VAL A 34 18065 10112 10829 -3676 -837 -3841 C
ATOM 31 C VAL A 34 13.296 27.364 52.957 1.00 99.37 C
ANISOU 31 C VAL A 34 17250 9822 10682 -3762 -925 -3610 C
ATOM 32 O VAL A 34 12.696 27.480 51.881 1.00 97.65 O
ANISOU 32 O VAL A 34 17060 9330 10711 -3595 -660 -3417 O
ATOM 33 CB VAL A 34 13.241 29.443 54.408 1.00 99.67 C
ANISOU 33 CB VAL A 34 17867 9435 10568 -3983 -766 -4069 C
ATOM 34 CG1 VAL A 34 12.959 30.279 53.167 1.00 98.89 C
ANISOU 34 CG1 VAL A 34 17836 8892 10846 -3966 -451 -3927 C
ATOM 35 CG2 VAL A 34 12.608 30.072 55.639 1.00103.54 C
ANISOU 35 CG2 VAL A 34 18784 9771 10784 -3876 -645 -4305 C
ATOM 36 N GLY A 35 14.436 26.677 53.058 1.00 98.21 N
ANISOU 36 N GLY A 35 16716 10108 10490 -4005 -1295 -3613 N
ATOM 37 CA GLY A 35 14.994 26.017 51.888 1.00 97.81 C
ANISOU 37 CA GLY A 35 16176 10256 10729 -3996 -1348 -3339 C
ATOM 38 C GLY A 35 14.101 24.909 51.364 1.00 96.48 C
ANISOU 38 C GLY A 35 15841 10207 10610 -3484 -1215 -2994 C
ATOM 39 O GLY A 35 13.775 24.866 50.176 1.00 95.31 O
ANISOU 39 O GLY A 35 15562 9916 10736 -3334 -1001 -2762 O
ATOM 40 N MET A 36 13.685 24.000 52.251 1.00 97.37 N
ANISOU 40 N MET A 36 15978 10581 10439 -3227 -1339 -2957 N
ATOM 41 CA MET A 36 12.822 22.898 51.834 1.00 96.22 C
ANISOU 41 CA MET A 36 15689 10544 10328 -2782 -1216 -2646 C
ATOM 42 C MET A 36 11.457 23.389 51.373 1.00 94.66 C
ANISOU 42 C MET A 36 15777 9958 10230 -2517 -828 -2566 C
ATOM 43 O MET A 36 10.842 22.765 50.500 1.00 93.51 O
ANISOU 43 O MET A 36 15450 9827 10253 -2240 -686 -2294 O
ATOM 44 CB MET A 36 12.662 21.893 52.974 1.00105.77 C
ANISOU 44 CB MET A 36 16920 12077 11192 -2598 -1410 -2627 C
ATOM 45 CG MET A 36 13.928 21.127 53.308 1.00107.46 C
ANISOU 45 CG MET A 36 16769 12734 11325 -2735 -1811 -2604 C
ATOM 46 SD MET A 36 13.677 19.917 54.620 1.00108.24 S
ANISOU 46 SD MET A 36 16946 13182 10998 -2473 -2023 -2523 S
ATOM 47 CE MET A 36 13.587 20.989 56.054 1.00109.05 C
ANISOU 47 CE MET A 36 17565 13181 10689 -2730 -2092 -2920 C
ATOM 48 N GLY A 37 10.964 24.489 51.945 1.00 91.59 N
ANISOU 48 N GLY A 37 15830 9230 9740 -2589 -657 -2802 N
ATOM 49 CA GLY A 37 9.696 25.038 51.492 1.00 90.48 C
ANISOU 49 CA GLY A 37 15936 8720 9723 -2308 -284 -2717 C
ATOM 50 C GLY A 37 9.726 25.426 50.027 1.00 89.52 C
ANISOU 50 C GLY A 37 15656 8395 9964 -2308 -135 -2518 C
ATOM 51 O GLY A 37 8.811 25.103 49.264 1.00 88.47 O
ANISOU 51 O GLY A 37 15435 8212 9969 -1986 51 -2265 O
ATOM 52 N ILE A 38 10.784 26.127 49.613 1.00 89.61 N
ANISOU 52 N ILE A 38 15626 8301 10119 -2688 -219 -2625 N
ATOM 53 CA ILE A 38 10.936 26.479 48.204 1.00 88.82 C
ANISOU 53 CA ILE A 38 15382 8029 10335 -2723 -78 -2421 C
ATOM 54 C ILE A 38 11.131 25.224 47.365 1.00 88.21 C
ANISOU 54 C ILE A 38 14836 8323 10356 -2564 -185 -2131 C
ATOM 55 O ILE A 38 10.525 25.073 46.296 1.00 87.07 O
ANISOU 55 O ILE A 38 14609 8098 10376 -2340 -16 -1879 O
ATOM 56 CB ILE A 38 12.102 27.468 48.023 1.00 89.37 C
ANISOU 56 CB ILE A 38 15504 7925 10527 -3217 -133 -2608 C
ATOM 57 CG1 ILE A 38 11.822 28.758 48.791 1.00 89.93 C
ANISOU 57 CG1 ILE A 38 16112 7550 10509 -3373 13 -2911 C
ATOM 58 CG2 ILE A 38 12.324 27.769 46.551 1.00 88.66 C
ANISOU 58 CG2 ILE A 38 15264 7685 10738 -3266 24 -2371 C
ATOM 59 CD1 ILE A 38 13.021 29.668 48.899 1.00 92.10 C
ANISOU 59 CD1 ILE A 38 16359 7761 10874 -3855 -89 -3104 C
ATOM 60 N VAL A 39 11.977 24.304 47.836 1.00 86.13 N
ANISOU 60 N VAL A 39 14274 8468 9983 -2667 -471 -2163 N
ATOM 61 CA VAL A 39 12.215 23.058 47.108 1.00 85.84 C
ANISOU 61 CA VAL A 39 13820 8762 10032 -2503 -561 -1911 C
ATOM 62 C VAL A 39 10.909 22.301 46.903 1.00 84.53 C
ANISOU 62 C VAL A 39 13687 8605 9826 -2082 -416 -1703 C
ATOM 63 O VAL A 39 10.585 21.878 45.788 1.00 83.51 O
ANISOU 63 O VAL A 39 13389 8488 9854 -1925 -310 -1475 O
ATOM 64 CB VAL A 39 13.259 22.196 47.842 1.00 85.55 C
ANISOU 64 CB VAL A 39 13499 9146 9862 -2621 -893 -1980 C
ATOM 65 CG1 VAL A 39 13.361 20.823 47.197 1.00 85.48 C
ANISOU 65 CG1 VAL A 39 13122 9431 9924 -2379 -950 -1723 C
ATOM 66 CG2 VAL A 39 14.611 22.886 47.831 1.00 87.02 C
ANISOU 66 CG2 VAL A 39 13539 9383 10142 -3064 -1046 -2155 C
ATOM 67 N MET A 40 10.131 22.132 47.974 1.00 85.53 N
ANISOU 67 N MET A 40 14035 8734 9730 -1913 -403 -1786 N
ATOM 68 CA MET A 40 8.881 21.389 47.857 1.00 84.60 C
ANISOU 68 CA MET A 40 13915 8650 9578 -1548 -260 -1595 C
ATOM 69 C MET A 40 7.851 22.156 47.034 1.00 83.58 C
ANISOU 69 C MET A 40 13933 8206 9617 -1381 22 -1488 C
ATOM 70 O MET A 40 7.087 21.553 46.272 1.00 82.72 O
ANISOU 70 O MET A 40 13675 8158 9598 -1149 112 -1262 O
ATOM 71 CB MET A 40 8.336 21.057 49.245 1.00 87.44 C
ANISOU 71 CB MET A 40 14477 9098 9647 -1430 -285 -1708 C
ATOM 72 CG MET A 40 9.199 20.064 50.007 1.00 88.47 C
ANISOU 72 CG MET A 40 14444 9583 9587 -1507 -579 -1731 C
ATOM 73 SD MET A 40 8.574 19.694 51.655 1.00 89.23 S
ANISOU 73 SD MET A 40 14830 9787 9287 -1378 -596 -1842 S
ATOM 74 CE MET A 40 9.872 18.626 52.274 1.00 90.60 C
ANISOU 74 CE MET A 40 14765 10376 9284 -1487 -999 -1820 C
ATOM 75 N SER A 41 7.817 23.485 47.168 1.00 83.25 N
ANISOU 75 N SER A 41 14192 7824 9617 -1496 156 -1645 N
ATOM 76 CA SER A 41 6.888 24.281 46.370 1.00 82.63 C
ANISOU 76 CA SER A 41 14263 7426 9707 -1305 418 -1517 C
ATOM 77 C SER A 41 7.195 24.160 44.883 1.00 81.77 C
ANISOU 77 C SER A 41 13921 7335 9814 -1334 423 -1282 C
ATOM 78 O SER A 41 6.279 24.129 44.053 1.00 81.15 O
ANISOU 78 O SER A 41 13803 7195 9835 -1079 560 -1063 O
ATOM 79 CB SER A 41 6.933 25.744 46.809 1.00 83.63 C
ANISOU 79 CB SER A 41 14798 7134 9844 -1439 567 -1738 C
ATOM 80 OG SER A 41 6.489 25.890 48.146 1.00 84.40 O
ANISOU 80 OG SER A 41 15159 7195 9714 -1371 610 -1960 O
ATOM 81 N LEU A 42 8.480 24.095 44.526 1.00 80.08 N
ANISOU 81 N LEU A 42 13539 7227 9661 -1644 275 -1323 N
ATOM 82 CA LEU A 42 8.848 23.897 43.128 1.00 79.40 C
ANISOU 82 CA LEU A 42 13230 7192 9745 -1681 298 -1108 C
ATOM 83 C LEU A 42 8.493 22.495 42.652 1.00 78.66 C
ANISOU 83 C LEU A 42 12835 7429 9623 -1462 221 -915 C
ATOM 84 O LEU A 42 8.129 22.309 41.484 1.00 77.82 O
ANISOU 84 O LEU A 42 12631 7326 9610 -1345 303 -702 O
ATOM 85 CB LEU A 42 10.340 24.164 42.932 1.00 80.35 C
ANISOU 85 CB LEU A 42 13216 7367 9945 -2076 188 -1213 C
ATOM 86 CG LEU A 42 10.815 25.600 43.169 1.00 81.09 C
ANISOU 86 CG LEU A 42 13604 7100 10105 -2380 278 -1397 C
ATOM 87 CD1 LEU A 42 12.330 25.689 43.063 1.00 82.21 C
ANISOU 87 CD1 LEU A 42 13523 7388 10325 -2805 140 -1508 C
ATOM 88 CD2 LEU A 42 10.144 26.562 42.201 1.00 80.40 C
ANISOU 88 CD2 LEU A 42 13766 6622 10160 -2270 540 -1228 C
ATOM 89 N ILE A 43 8.595 21.499 43.534 1.00 77.60 N
ANISOU 89 N ILE A 43 12579 7561 9345 -1413 64 -984 N
ATOM 90 CA ILE A 43 8.207 20.143 43.163 1.00 77.00 C
ANISOU 90 CA ILE A 43 12269 7748 9242 -1214 11 -814 C
ATOM 91 C ILE A 43 6.705 20.068 42.922 1.00 76.24 C
ANISOU 91 C ILE A 43 12256 7571 9140 -926 164 -673 C
ATOM 92 O ILE A 43 6.245 19.377 42.006 1.00 75.43 O
ANISOU 92 O ILE A 43 11994 7579 9089 -801 184 -491 O
ATOM 93 CB ILE A 43 8.664 19.139 44.238 1.00 75.42 C
ANISOU 93 CB ILE A 43 11964 7811 8883 -1220 -181 -903 C
ATOM 94 CG1 ILE A 43 10.191 19.099 44.312 1.00 76.72 C
ANISOU 94 CG1 ILE A 43 11946 8125 9079 -1479 -362 -1003 C
ATOM 95 CG2 ILE A 43 8.113 17.749 43.950 1.00 74.90 C
ANISOU 95 CG2 ILE A 43 11728 7945 8786 -1006 -198 -732 C
ATOM 96 CD1 ILE A 43 10.723 18.350 45.514 1.00 78.18 C
ANISOU 96 CD1 ILE A 43 12065 8554 9085 -1488 -583 -1099 C
ATOM 97 N VAL A 44 5.918 20.788 43.724 1.00 75.70 N
ANISOU 97 N VAL A 44 12432 7321 9010 -822 279 -764 N
ATOM 98 CA VAL A 44 4.472 20.809 43.513 1.00 75.66 C
ANISOU 98 CA VAL A 44 12460 7258 9027 -533 438 -625 C
ATOM 99 C VAL A 44 4.141 21.446 42.169 1.00 75.11 C
ANISOU 99 C VAL A 44 12381 7036 9121 -464 538 -443 C
ATOM 100 O VAL A 44 3.244 20.988 41.452 1.00 74.95 O
ANISOU 100 O VAL A 44 12219 7119 9138 -273 570 -251 O
ATOM 101 CB VAL A 44 3.768 21.533 44.676 1.00 75.31 C
ANISOU 101 CB VAL A 44 12686 7039 8889 -418 579 -775 C
ATOM 102 CG1 VAL A 44 2.279 21.660 44.400 1.00 75.84 C
ANISOU 102 CG1 VAL A 44 12739 7058 9019 -99 766 -618 C
ATOM 103 CG2 VAL A 44 4.001 20.791 45.980 1.00 75.95 C
ANISOU 103 CG2 VAL A 44 12789 7311 8756 -468 477 -921 C
ATOM 104 N LEU A 45 4.865 22.506 41.801 1.00 74.15 N
ANISOU 104 N LEU A 45 12414 6674 9087 -635 581 -493 N
ATOM 105 CA LEU A 45 4.636 23.142 40.507 1.00 73.81 C
ANISOU 105 CA LEU A 45 12400 6471 9174 -577 678 -293 C
ATOM 106 C LEU A 45 5.054 22.230 39.361 1.00 72.95 C
ANISOU 106 C LEU A 45 12027 6612 9080 -641 577 -133 C
ATOM 107 O LEU A 45 4.293 22.026 38.409 1.00 72.74 O
ANISOU 107 O LEU A 45 11920 6645 9072 -467 604 76 O
ATOM 108 CB LEU A 45 5.381 24.474 40.432 1.00 73.36 C
ANISOU 108 CB LEU A 45 12605 6067 9203 -786 771 -385 C
ATOM 109 CG LEU A 45 4.867 25.598 41.329 1.00 74.22 C
ANISOU 109 CG LEU A 45 13059 5826 9314 -698 926 -532 C
ATOM 110 CD1 LEU A 45 5.789 26.802 41.240 1.00 74.57 C
ANISOU 110 CD1 LEU A 45 13369 5519 9445 -992 1002 -649 C
ATOM 111 CD2 LEU A 45 3.445 25.974 40.941 1.00 74.62 C
ANISOU 111 CD2 LEU A 45 13181 5748 9423 -301 1086 -332 C
ATOM 112 N ALA A 46 6.270 21.677 39.433 1.00 72.24 N
ANISOU 112 N ALA A 46 11796 6680 8973 -884 459 -234 N
ATOM 113 CA ALA A 46 6.754 20.798 38.372 1.00 71.61 C
ANISOU 113 CA ALA A 46 11485 6822 8903 -937 398 -110 C
ATOM 114 C ALA A 46 5.833 19.604 38.164 1.00 71.05 C
ANISOU 114 C ALA A 46 11256 6979 8760 -727 344 -1 C
ATOM 115 O ALA A 46 5.739 19.077 37.049 1.00 70.53 O
ANISOU 115 O ALA A 46 11077 7031 8689 -699 338 140 O
ATOM 116 CB ALA A 46 8.172 20.326 38.689 1.00 68.74 C
ANISOU 116 CB ALA A 46 10960 6615 8544 -1182 286 -250 C
ATOM 117 N ILE A 47 5.147 19.166 39.217 1.00 69.63 N
ANISOU 117 N ILE A 47 11084 6861 8511 -600 314 -72 N
ATOM 118 CA ILE A 47 4.177 18.086 39.084 1.00 69.40 C
ANISOU 118 CA ILE A 47 10917 7023 8428 -434 285 29 C
ATOM 119 C ILE A 47 2.892 18.589 38.440 1.00 69.90 C
ANISOU 119 C ILE A 47 11005 7023 8529 -235 373 195 C
ATOM 120 O ILE A 47 2.406 18.014 37.460 1.00 69.72 O
ANISOU 120 O ILE A 47 10853 7142 8496 -183 336 338 O
ATOM 121 CB ILE A 47 3.905 17.444 40.455 1.00 70.37 C
ANISOU 121 CB ILE A 47 11044 7235 8457 -384 249 -85 C
ATOM 122 CG1 ILE A 47 5.133 16.671 40.942 1.00 70.32 C
ANISOU 122 CG1 ILE A 47 10959 7360 8398 -536 116 -193 C
ATOM 123 CG2 ILE A 47 2.683 16.559 40.388 1.00 70.65 C
ANISOU 123 CG2 ILE A 47 10968 7417 8460 -226 269 26 C
ATOM 124 CD1 ILE A 47 5.047 16.238 42.391 1.00 71.33 C
ANISOU 124 CD1 ILE A 47 11153 7552 8396 -504 68 -303 C
ATOM 125 N VAL A 48 2.320 19.665 38.980 1.00 71.01 N
ANISOU 125 N VAL A 48 11315 6958 8709 -114 486 174 N
ATOM 126 CA VAL A 48 1.037 20.156 38.480 1.00 72.11 C
ANISOU 126 CA VAL A 48 11445 7053 8899 134 568 347 C
ATOM 127 C VAL A 48 1.193 20.725 37.075 1.00 71.85 C
ANISOU 127 C VAL A 48 11442 6945 8912 130 565 529 C
ATOM 128 O VAL A 48 0.536 20.275 36.128 1.00 72.29 O
ANISOU 128 O VAL A 48 11349 7174 8943 223 502 704 O
ATOM 129 CB VAL A 48 0.441 21.195 39.446 1.00 69.01 C
ANISOU 129 CB VAL A 48 11249 6427 8544 302 725 271 C
ATOM 130 CG1 VAL A 48 -0.813 21.814 38.846 1.00 70.40 C
ANISOU 130 CG1 VAL A 48 11395 6549 8804 601 816 478 C
ATOM 131 CG2 VAL A 48 0.122 20.547 40.786 1.00 69.70 C
ANISOU 131 CG2 VAL A 48 11308 6632 8542 326 745 118 C
ATOM 132 N PHE A 49 2.065 21.726 36.921 1.00 74.20 N
ANISOU 132 N PHE A 49 11945 6986 9261 2 633 491 N
ATOM 133 CA PHE A 49 2.224 22.385 35.628 1.00 74.24 C
ANISOU 133 CA PHE A 49 12032 6880 9295 -2 666 686 C
ATOM 134 C PHE A 49 2.662 21.404 34.547 1.00 73.55 C
ANISOU 134 C PHE A 49 11764 7057 9123 -129 557 771 C
ATOM 135 O PHE A 49 2.265 21.542 33.384 1.00 74.05 O
ANISOU 135 O PHE A 49 11826 7165 9143 -47 543 980 O
ATOM 136 CB PHE A 49 3.224 23.536 35.748 1.00 76.84 C
ANISOU 136 CB PHE A 49 12619 6878 9698 -191 777 604 C
ATOM 137 CG PHE A 49 3.368 24.350 34.494 1.00 77.12 C
ANISOU 137 CG PHE A 49 12799 6742 9760 -195 854 827 C
ATOM 138 CD1 PHE A 49 2.403 25.281 34.143 1.00 78.13 C
ANISOU 138 CD1 PHE A 49 13096 6656 9935 84 946 1026 C
ATOM 139 CD2 PHE A 49 4.468 24.189 33.668 1.00 76.60 C
ANISOU 139 CD2 PHE A 49 12704 6732 9668 -458 851 853 C
ATOM 140 CE1 PHE A 49 2.532 26.035 32.989 1.00 78.53 C
ANISOU 140 CE1 PHE A 49 13314 6537 9985 96 1015 1265 C
ATOM 141 CE2 PHE A 49 4.603 24.940 32.511 1.00 77.04 C
ANISOU 141 CE2 PHE A 49 12923 6629 9719 -472 945 1077 C
ATOM 142 CZ PHE A 49 3.633 25.864 32.172 1.00 77.96 C
ANISOU 142 CZ PHE A 49 13239 6519 9863 -196 1018 1291 C
ATOM 143 N GLY A 50 3.467 20.405 34.908 1.00 70.48 N
ANISOU 143 N GLY A 50 11239 6844 8696 -312 481 614 N
ATOM 144 CA GLY A 50 3.921 19.444 33.917 1.00 69.93 C
ANISOU 144 CA GLY A 50 11024 6996 8548 -416 413 666 C
ATOM 145 C GLY A 50 2.835 18.471 33.498 1.00 70.27 C
ANISOU 145 C GLY A 50 10916 7277 8507 -275 317 758 C
ATOM 146 O GLY A 50 2.701 18.148 32.314 1.00 70.55 O
ANISOU 146 O GLY A 50 10917 7436 8454 -285 279 883 O
ATOM 147 N ASN A 51 2.043 17.992 34.459 1.00 69.07 N
ANISOU 147 N ASN A 51 10678 7196 8367 -166 283 693 N
ATOM 148 CA ASN A 51 1.031 16.985 34.158 1.00 69.84 C
ANISOU 148 CA ASN A 51 10607 7528 8402 -89 195 758 C
ATOM 149 C ASN A 51 -0.246 17.595 33.594 1.00 71.86 C
ANISOU 149 C ASN A 51 10827 7815 8664 115 182 953 C
ATOM 150 O ASN A 51 -0.965 16.923 32.847 1.00 73.12 O
ANISOU 150 O ASN A 51 10842 8191 8747 130 77 1047 O
ATOM 151 CB ASN A 51 0.726 16.163 35.408 1.00 71.08 C
ANISOU 151 CB ASN A 51 10680 7759 8567 -81 187 626 C
ATOM 152 CG ASN A 51 1.854 15.221 35.764 1.00 69.44 C
ANISOU 152 CG ASN A 51 10460 7597 8327 -247 150 481 C
ATOM 153 OD1 ASN A 51 2.381 14.513 34.906 1.00 68.77 O
ANISOU 153 OD1 ASN A 51 10331 7605 8194 -347 108 487 O
ATOM 154 ND2 ASN A 51 2.260 15.236 37.027 1.00 69.18 N
ANISOU 154 ND2 ASN A 51 10478 7500 8310 -261 170 351 N
ATOM 155 N VAL A 52 -0.550 18.849 33.937 1.00 71.63 N
ANISOU 155 N VAL A 52 10923 7572 8721 276 280 1014 N
ATOM 156 CA VAL A 52 -1.606 19.554 33.219 1.00 73.49 C
ANISOU 156 CA VAL A 52 11134 7820 8970 507 265 1243 C
ATOM 157 C VAL A 52 -1.163 19.831 31.790 1.00 73.32 C
ANISOU 157 C VAL A 52 11203 7804 8851 442 211 1405 C
ATOM 158 O VAL A 52 -1.977 19.803 30.859 1.00 74.93 O
ANISOU 158 O VAL A 52 11315 8178 8977 563 103 1601 O
ATOM 159 CB VAL A 52 -1.996 20.851 33.956 1.00 70.65 C
ANISOU 159 CB VAL A 52 10928 7176 8738 729 418 1266 C
ATOM 160 CG1 VAL A 52 -2.995 21.651 33.136 1.00 72.39 C
ANISOU 160 CG1 VAL A 52 11133 7388 8984 1016 404 1540 C
ATOM 161 CG2 VAL A 52 -2.580 20.532 35.317 1.00 71.36 C
ANISOU 161 CG2 VAL A 52 10928 7302 8883 814 489 1116 C
ATOM 162 N LEU A 53 0.131 20.089 31.588 1.00 72.71 N
ANISOU 162 N LEU A 53 11295 7568 8762 241 283 1330 N
ATOM 163 CA LEU A 53 0.657 20.266 30.239 1.00 72.68 C
ANISOU 163 CA LEU A 53 11390 7584 8642 147 270 1474 C
ATOM 164 C LEU A 53 0.494 18.992 29.420 1.00 73.01 C
ANISOU 164 C LEU A 53 11271 7951 8518 51 129 1472 C
ATOM 165 O LEU A 53 0.064 19.034 28.261 1.00 74.24 O
ANISOU 165 O LEU A 53 11444 8239 8526 99 45 1655 O
ATOM 166 CB LEU A 53 2.127 20.678 30.310 1.00 73.57 C
ANISOU 166 CB LEU A 53 11661 7493 8797 -86 402 1364 C
ATOM 167 CG LEU A 53 2.837 21.021 29.002 1.00 73.66 C
ANISOU 167 CG LEU A 53 11809 7478 8699 -211 461 1509 C
ATOM 168 CD1 LEU A 53 2.233 22.266 28.370 1.00 74.87 C
ANISOU 168 CD1 LEU A 53 12167 7437 8842 -24 508 1782 C
ATOM 169 CD2 LEU A 53 4.325 21.201 29.246 1.00 72.66 C
ANISOU 169 CD2 LEU A 53 11742 7217 8647 -481 595 1356 C
ATOM 170 N VAL A 54 0.845 17.846 30.008 1.00 70.99 N
ANISOU 170 N VAL A 54 10887 7817 8268 -86 100 1265 N
ATOM 171 CA VAL A 54 0.667 16.563 29.331 1.00 71.25 C
ANISOU 171 CA VAL A 54 10803 8113 8156 -187 -13 1226 C
ATOM 172 C VAL A 54 -0.807 16.322 29.038 1.00 73.57 C
ANISOU 172 C VAL A 54 10945 8613 8394 -52 -163 1350 C
ATOM 173 O VAL A 54 -1.183 15.902 27.937 1.00 74.58 O
ANISOU 173 O VAL A 54 11048 8939 8349 -95 -283 1435 O
ATOM 174 CB VAL A 54 1.255 15.423 30.182 1.00 70.94 C
ANISOU 174 CB VAL A 54 10679 8109 8165 -318 3 996 C
ATOM 175 CG1 VAL A 54 0.935 14.077 29.557 1.00 71.35 C
ANISOU 175 CG1 VAL A 54 10646 8381 8083 -415 -97 944 C
ATOM 176 CG2 VAL A 54 2.753 15.600 30.348 1.00 69.35 C
ANISOU 176 CG2 VAL A 54 10566 7771 8014 -452 120 886 C
ATOM 177 N ILE A 55 -1.660 16.579 30.028 1.00 70.54 N
ANISOU 177 N ILE A 55 10448 8207 8148 104 -156 1354 N
ATOM 178 CA ILE A 55 -3.092 16.345 29.874 1.00 73.33 C
ANISOU 178 CA ILE A 55 10586 8789 8488 233 -286 1469 C
ATOM 179 C ILE A 55 -3.678 17.241 28.790 1.00 74.89 C
ANISOU 179 C ILE A 55 10808 9044 8603 405 -377 1732 C
ATOM 180 O ILE A 55 -4.440 16.783 27.931 1.00 76.22 O
ANISOU 180 O ILE A 55 10834 9489 8635 395 -560 1834 O
ATOM 181 CB ILE A 55 -3.802 16.538 31.224 1.00 70.23 C
ANISOU 181 CB ILE A 55 10069 8343 8270 384 -201 1420 C
ATOM 182 CG1 ILE A 55 -3.586 15.317 32.126 1.00 69.66 C
ANISOU 182 CG1 ILE A 55 9924 8328 8218 207 -175 1208 C
ATOM 183 CG2 ILE A 55 -5.255 16.891 31.022 1.00 72.77 C
ANISOU 183 CG2 ILE A 55 10169 8850 8632 610 -286 1608 C
ATOM 184 CD1 ILE A 55 -4.052 15.511 33.548 1.00 70.16 C
ANISOU 184 CD1 ILE A 55 9931 8313 8414 326 -50 1139 C
ATOM 185 N THR A 56 -3.332 18.529 28.810 1.00 74.99 N
ANISOU 185 N THR A 56 11016 8791 8687 559 -258 1851 N
ATOM 186 CA THR A 56 -3.908 19.454 27.839 1.00 76.32 C
ANISOU 186 CA THR A 56 11240 8977 8783 770 -332 2142 C
ATOM 187 C THR A 56 -3.414 19.163 26.426 1.00 76.55 C
ANISOU 187 C THR A 56 11390 9140 8555 610 -434 2230 C
ATOM 188 O THR A 56 -4.167 19.330 25.459 1.00 78.27 O
ANISOU 188 O THR A 56 11557 9562 8620 729 -607 2453 O
ATOM 189 CB THR A 56 -3.584 20.894 28.236 1.00 74.62 C
ANISOU 189 CB THR A 56 11265 8375 8713 956 -144 2238 C
ATOM 190 OG1 THR A 56 -4.103 21.157 29.547 1.00 74.68 O
ANISOU 190 OG1 THR A 56 11184 8266 8927 1117 -36 2137 O
ATOM 191 CG2 THR A 56 -4.204 21.875 27.252 1.00 76.05 C
ANISOU 191 CG2 THR A 56 11532 8538 8823 1220 -212 2579 C
ATOM 192 N ALA A 57 -2.162 18.720 26.289 1.00 77.26 N
ANISOU 192 N ALA A 57 11631 9140 8584 350 -331 2061 N
ATOM 193 CA ALA A 57 -1.638 18.381 24.970 1.00 77.07 C
ANISOU 193 CA ALA A 57 11738 9245 8299 191 -381 2116 C
ATOM 194 C ALA A 57 -2.429 17.246 24.335 1.00 78.20 C
ANISOU 194 C ALA A 57 11704 9759 8249 109 -609 2083 C
ATOM 195 O ALA A 57 -2.688 17.259 23.126 1.00 79.19 O
ANISOU 195 O ALA A 57 11902 10069 8117 99 -742 2236 O
ATOM 196 CB ALA A 57 -0.160 18.011 25.072 1.00 74.64 C
ANISOU 196 CB ALA A 57 11564 8796 8000 -56 -199 1912 C
ATOM 197 N ILE A 58 -2.820 16.251 25.133 1.00 76.61 N
ANISOU 197 N ILE A 58 11290 9667 8150 27 -656 1883 N
ATOM 198 CA ILE A 58 -3.623 15.156 24.604 1.00 77.60 C
ANISOU 198 CA ILE A 58 11249 10121 8116 -96 -868 1830 C
ATOM 199 C ILE A 58 -5.059 15.609 24.369 1.00 79.96 C
ANISOU 199 C ILE A 58 11325 10651 8407 110 -1078 2055 C
ATOM 200 O ILE A 58 -5.730 15.121 23.452 1.00 81.07 O
ANISOU 200 O ILE A 58 11372 11100 8331 31 -1308 2112 O
ATOM 201 CB ILE A 58 -3.547 13.945 25.554 1.00 76.65 C
ANISOU 201 CB ILE A 58 11000 10004 8120 -265 -823 1559 C
ATOM 202 CG1 ILE A 58 -2.103 13.448 25.654 1.00 74.30 C
ANISOU 202 CG1 ILE A 58 10900 9517 7814 -433 -641 1362 C
ATOM 203 CG2 ILE A 58 -4.455 12.820 25.084 1.00 78.01 C
ANISOU 203 CG2 ILE A 58 11005 10482 8155 -430 -1029 1490 C
ATOM 204 CD1 ILE A 58 -1.878 12.434 26.750 1.00 73.38 C
ANISOU 204 CD1 ILE A 58 10700 9334 7846 -536 -568 1136 C
ATOM 205 N ALA A 59 -5.547 16.562 25.165 1.00 79.97 N
ANISOU 205 N ALA A 59 11234 10517 8634 381 -1005 2184 N
ATOM 206 CA ALA A 59 -6.939 16.988 25.051 1.00 82.03 C
ANISOU 206 CA ALA A 59 11227 11008 8934 627 -1183 2404 C
ATOM 207 C ALA A 59 -7.190 17.741 23.749 1.00 83.01 C
ANISOU 207 C ALA A 59 11456 11248 8835 779 -1348 2703 C
ATOM 208 O ALA A 59 -8.128 17.424 23.008 1.00 84.41 O
ANISOU 208 O ALA A 59 11426 11795 8851 791 -1624 2825 O
ATOM 209 CB ALA A 59 -7.322 17.850 26.255 1.00 78.49 C
ANISOU 209 CB ALA A 59 10692 10344 8785 913 -1010 2453 C
ATOM 210 N LYS A 60 -6.360 18.743 23.449 1.00 85.56 N
ANISOU 210 N LYS A 60 12108 11268 9133 880 -1191 2834 N
ATOM 211 CA LYS A 60 -6.623 19.598 22.296 1.00 86.77 C
ANISOU 211 CA LYS A 60 12402 11485 9080 1072 -1319 3170 C
ATOM 212 C LYS A 60 -6.136 18.977 20.989 1.00 86.80 C
ANISOU 212 C LYS A 60 12584 11695 8702 813 -1448 3158 C
ATOM 213 O LYS A 60 -6.828 19.060 19.969 1.00 88.23 O
ANISOU 213 O LYS A 60 12724 12174 8626 895 -1708 3379 O
ATOM 214 CB LYS A 60 -5.981 20.972 22.498 1.00 90.63 C
ANISOU 214 CB LYS A 60 13204 11529 9700 1276 -1073 3335 C
ATOM 215 CG LYS A 60 -6.652 21.834 23.559 1.00 90.64 C
ANISOU 215 CG LYS A 60 13088 11324 10027 1618 -963 3416 C
ATOM 216 CD LYS A 60 -6.025 23.220 23.605 1.00 89.84 C
ANISOU 216 CD LYS A 60 13361 10751 10024 1794 -726 3585 C
ATOM 217 CE LYS A 60 -6.702 24.114 24.631 1.00 89.95 C
ANISOU 217 CE LYS A 60 13310 10522 10347 2157 -591 3650 C
ATOM 218 NZ LYS A 60 -6.100 25.478 24.651 1.00 89.20 N
ANISOU 218 NZ LYS A 60 13629 9917 10347 2305 -350 3803 N
ATOM 219 N PHE A 61 -4.957 18.360 20.991 1.00 88.30 N
ANISOU 219 N PHE A 61 12968 11747 8835 514 -1271 2905 N
ATOM 220 CA PHE A 61 -4.354 17.887 19.751 1.00 87.93 C
ANISOU 220 CA PHE A 61 13150 11840 8421 290 -1315 2887 C
ATOM 221 C PHE A 61 -4.903 16.516 19.377 1.00 88.04 C
ANISOU 221 C PHE A 61 12984 12223 8244 56 -1547 2686 C
ATOM 222 O PHE A 61 -4.993 15.619 20.221 1.00 87.24 O
ANISOU 222 O PHE A 61 12693 12130 8326 -83 -1519 2422 O
ATOM 223 CB PHE A 61 -2.832 17.844 19.881 1.00 87.44 C
ANISOU 223 CB PHE A 61 13351 11477 8395 94 -997 2710 C
ATOM 224 CG PHE A 61 -2.200 19.202 19.982 1.00 87.23 C
ANISOU 224 CG PHE A 61 13558 11095 8488 242 -775 2913 C
ATOM 225 CD1 PHE A 61 -1.972 19.960 18.844 1.00 88.07 C
ANISOU 225 CD1 PHE A 61 13947 11181 8334 296 -758 3192 C
ATOM 226 CD2 PHE A 61 -1.850 19.728 21.213 1.00 86.11 C
ANISOU 226 CD2 PHE A 61 13382 10633 8703 311 -580 2824 C
ATOM 227 CE1 PHE A 61 -1.397 21.212 18.934 1.00 87.66 C
ANISOU 227 CE1 PHE A 61 14139 10764 8404 402 -532 3384 C
ATOM 228 CE2 PHE A 61 -1.275 20.981 21.309 1.00 85.56 C
ANISOU 228 CE2 PHE A 61 13553 10208 8747 405 -372 2987 C
ATOM 229 CZ PHE A 61 -1.049 21.723 20.167 1.00 86.32 C
ANISOU 229 CZ PHE A 61 13930 10257 8610 445 -340 3271 C
ATOM 230 N GLU A 62 -5.271 16.360 18.102 1.00 89.95 N
ANISOU 230 N GLU A 62 13314 12763 8101 0 -1776 2812 N
ATOM 231 CA GLU A 62 -5.942 15.142 17.656 1.00 90.39 C
ANISOU 231 CA GLU A 62 13208 13190 7946 -238 -2040 2631 C
ATOM 232 C GLU A 62 -4.970 13.973 17.568 1.00 88.73 C
ANISOU 232 C GLU A 62 13181 12893 7638 -576 -1867 2268 C
ATOM 233 O GLU A 62 -5.250 12.881 18.073 1.00 88.36 O
ANISOU 233 O GLU A 62 12967 12916 7689 -770 -1911 2002 O
ATOM 234 CB GLU A 62 -6.608 15.374 16.300 1.00100.56 C
ANISOU 234 CB GLU A 62 14559 14839 8810 -202 -2360 2872 C
ATOM 235 CG GLU A 62 -7.704 16.415 16.311 1.00102.45 C
ANISOU 235 CG GLU A 62 14571 15223 9131 167 -2581 3253 C
ATOM 236 CD GLU A 62 -7.155 17.816 16.163 1.00102.80 C
ANISOU 236 CD GLU A 62 14895 14951 9214 465 -2384 3572 C
ATOM 237 OE1 GLU A 62 -5.925 17.955 15.996 1.00101.58 O
ANISOU 237 OE1 GLU A 62 15090 14504 9002 340 -2089 3492 O
ATOM 238 OE2 GLU A 62 -7.945 18.779 16.212 1.00104.30 O
ANISOU 238 OE2 GLU A 62 14953 15175 9500 824 -2510 3905 O
ATOM 239 N ARG A 63 -3.821 14.181 16.921 1.00 90.42 N
ANISOU 239 N ARG A 63 13744 12946 7666 -642 -1650 2261 N
ATOM 240 CA ARG A 63 -2.903 13.079 16.661 1.00 89.13 C
ANISOU 240 CA ARG A 63 13765 12729 7372 -923 -1479 1934 C
ATOM 241 C ARG A 63 -2.241 12.539 17.922 1.00 87.47 C
ANISOU 241 C ARG A 63 13448 12242 7543 -974 -1237 1679 C
ATOM 242 O ARG A 63 -1.574 11.501 17.851 1.00 86.61 O
ANISOU 242 O ARG A 63 13447 12081 7378 -1173 -1105 1399 O
ATOM 243 CB ARG A 63 -1.844 13.511 15.645 1.00 96.98 C
ANISOU 243 CB ARG A 63 15129 13642 8077 -957 -1273 2015 C
ATOM 244 CG ARG A 63 -0.933 14.631 16.105 1.00 96.13 C
ANISOU 244 CG ARG A 63 15115 13200 8209 -802 -977 2175 C
ATOM 245 CD ARG A 63 -0.030 15.070 14.965 1.00 96.28 C
ANISOU 245 CD ARG A 63 15490 13191 7903 -861 -784 2292 C
ATOM 246 NE ARG A 63 0.871 16.151 15.349 1.00 95.50 N
ANISOU 246 NE ARG A 63 15486 12767 8033 -769 -489 2443 N
ATOM 247 CZ ARG A 63 1.737 16.726 14.521 1.00 95.62 C
ANISOU 247 CZ ARG A 63 15791 12698 7841 -819 -256 2582 C
ATOM 248 NH1 ARG A 63 1.815 16.327 13.258 1.00 96.51 N
ANISOU 248 NH1 ARG A 63 16145 13037 7487 -935 -279 2594 N
ATOM 249 NH2 ARG A 63 2.521 17.704 14.953 1.00 94.90 N
ANISOU 249 NH2 ARG A 63 15763 12298 7996 -777 9 2704 N
ATOM 250 N LEU A 64 -2.407 13.198 19.066 1.00 83.13 N
ANISOU 250 N LEU A 64 12709 11515 7362 -787 -1176 1768 N
ATOM 251 CA LEU A 64 -2.004 12.621 20.340 1.00 81.81 C
ANISOU 251 CA LEU A 64 12412 11147 7526 -832 -1015 1539 C
ATOM 252 C LEU A 64 -3.152 11.938 21.067 1.00 82.66 C
ANISOU 252 C LEU A 64 12227 11400 7778 -862 -1202 1455 C
ATOM 253 O LEU A 64 -2.942 11.404 22.158 1.00 81.84 O
ANISOU 253 O LEU A 64 12023 11147 7925 -897 -1084 1285 O
ATOM 254 CB LEU A 64 -1.387 13.687 21.248 1.00 79.84 C
ANISOU 254 CB LEU A 64 12163 10599 7573 -652 -807 1639 C
ATOM 255 CG LEU A 64 -0.014 14.207 20.830 1.00 78.71 C
ANISOU 255 CG LEU A 64 12270 10258 7381 -691 -551 1655 C
ATOM 256 CD1 LEU A 64 0.422 15.309 21.770 1.00 77.88 C
ANISOU 256 CD1 LEU A 64 12150 9868 7574 -549 -390 1747 C
ATOM 257 CD2 LEU A 64 1.002 13.078 20.817 1.00 77.62 C
ANISOU 257 CD2 LEU A 64 12197 10080 7215 -887 -386 1369 C
ATOM 258 N GLN A 65 -4.356 11.944 20.496 1.00 81.16 N
ANISOU 258 N GLN A 65 11888 11517 7433 -855 -1490 1582 N
ATOM 259 CA GLN A 65 -5.497 11.252 21.093 1.00 82.25 C
ANISOU 259 CA GLN A 65 11712 11838 7701 -929 -1665 1504 C
ATOM 260 C GLN A 65 -5.495 9.779 20.680 1.00 82.09 C
ANISOU 260 C GLN A 65 11762 11925 7504 -1272 -1730 1217 C
ATOM 261 O GLN A 65 -6.398 9.281 20.010 1.00 83.30 O
ANISOU 261 O GLN A 65 11811 12383 7455 -1436 -1996 1199 O
ATOM 262 CB GLN A 65 -6.798 11.940 20.703 1.00 83.53 C
ANISOU 262 CB GLN A 65 11624 12308 7806 -763 -1951 1775 C
ATOM 263 CG GLN A 65 -6.947 13.332 21.282 1.00 83.93 C
ANISOU 263 CG GLN A 65 11596 12208 8087 -393 -1864 2044 C
ATOM 264 CD GLN A 65 -8.231 14.013 20.860 1.00 86.00 C
ANISOU 264 CD GLN A 65 11597 12778 8303 -170 -2143 2338 C
ATOM 265 OE1 GLN A 65 -9.004 13.472 20.071 1.00 87.10 O
ANISOU 265 OE1 GLN A 65 11594 13288 8212 -312 -2438 2351 O
ATOM 266 NE2 GLN A 65 -8.466 15.211 21.385 1.00 86.54 N
ANISOU 266 NE2 GLN A 65 11598 12694 8587 187 -2054 2574 N
ATOM 267 N THR A 66 -4.442 9.082 21.091 1.00 80.77 N
ANISOU 267 N THR A 66 11779 11493 7416 -1380 -1482 986 N
ATOM 268 CA THR A 66 -4.288 7.662 20.820 1.00 80.49 C
ANISOU 268 CA THR A 66 11871 11457 7255 -1675 -1473 695 C
ATOM 269 C THR A 66 -4.752 6.847 22.022 1.00 80.62 C
ANISOU 269 C THR A 66 11692 11385 7555 -1764 -1438 558 C
ATOM 270 O THR A 66 -5.069 7.383 23.086 1.00 80.93 O
ANISOU 270 O THR A 66 11515 11362 7872 -1592 -1391 674 O
ATOM 271 CB THR A 66 -2.831 7.327 20.482 1.00 78.39 C
ANISOU 271 CB THR A 66 11931 10954 6901 -1706 -1203 536 C
ATOM 272 OG1 THR A 66 -2.002 7.594 21.618 1.00 77.21 O
ANISOU 272 OG1 THR A 66 11743 10523 7069 -1547 -963 530 O
ATOM 273 CG2 THR A 66 -2.351 8.167 19.309 1.00 78.49 C
ANISOU 273 CG2 THR A 66 12148 11049 6625 -1631 -1195 689 C
ATOM 274 N VAL A 67 -4.790 5.526 21.837 1.00 78.92 N
ANISOU 274 N VAL A 67 11589 11145 7250 -2044 -1440 305 N
ATOM 275 CA VAL A 67 -5.189 4.642 22.927 1.00 78.96 C
ANISOU 275 CA VAL A 67 11464 11035 7501 -2163 -1381 179 C
ATOM 276 C VAL A 67 -4.148 4.663 24.040 1.00 77.70 C
ANISOU 276 C VAL A 67 11384 10541 7597 -1984 -1097 149 C
ATOM 277 O VAL A 67 -4.490 4.706 25.228 1.00 78.03 O
ANISOU 277 O VAL A 67 11245 10511 7893 -1909 -1041 199 O
ATOM 278 CB VAL A 67 -5.428 3.216 22.398 1.00 78.58 C
ANISOU 278 CB VAL A 67 11579 10989 7287 -2524 -1434 -90 C
ATOM 279 CG1 VAL A 67 -5.738 2.273 23.546 1.00 78.30 C
ANISOU 279 CG1 VAL A 67 11464 10775 7509 -2652 -1328 -203 C
ATOM 280 CG2 VAL A 67 -6.557 3.213 21.383 1.00 79.97 C
ANISOU 280 CG2 VAL A 67 11631 11547 7206 -2735 -1765 -65 C
ATOM 281 N THR A 68 -2.864 4.636 23.674 1.00 76.51 N
ANISOU 281 N THR A 68 11493 10206 7370 -1914 -916 70 N
ATOM 282 CA THR A 68 -1.800 4.692 24.671 1.00 75.36 C
ANISOU 282 CA THR A 68 11392 9787 7453 -1742 -680 48 C
ATOM 283 C THR A 68 -1.829 6.000 25.449 1.00 75.37 C
ANISOU 283 C THR A 68 11209 9787 7641 -1502 -668 259 C
ATOM 284 O THR A 68 -1.528 6.017 26.648 1.00 74.87 O
ANISOU 284 O THR A 68 11081 9565 7802 -1398 -556 257 O
ATOM 285 CB THR A 68 -0.440 4.509 23.995 1.00 73.79 C
ANISOU 285 CB THR A 68 11450 9452 7135 -1709 -494 -60 C
ATOM 286 OG1 THR A 68 -0.403 3.240 23.331 1.00 73.76 O
ANISOU 286 OG1 THR A 68 11659 9405 6962 -1915 -469 -285 O
ATOM 287 CG2 THR A 68 0.688 4.575 25.013 1.00 72.80 C
ANISOU 287 CG2 THR A 68 11320 9092 7250 -1532 -284 -74 C
ATOM 288 N ASN A 69 -2.200 7.102 24.798 1.00 75.69 N
ANISOU 288 N ASN A 69 11189 9988 7580 -1407 -781 443 N
ATOM 289 CA ASN A 69 -2.187 8.391 25.473 1.00 75.32 C
ANISOU 289 CA ASN A 69 11024 9886 7707 -1173 -743 632 C
ATOM 290 C ASN A 69 -3.430 8.629 26.322 1.00 76.87 C
ANISOU 290 C ASN A 69 10952 10186 8067 -1103 -845 730 C
ATOM 291 O ASN A 69 -3.418 9.534 27.162 1.00 76.54 O
ANISOU 291 O ASN A 69 10832 10046 8205 -907 -768 836 O
ATOM 292 CB ASN A 69 -2.022 9.517 24.455 1.00 79.98 C
ANISOU 292 CB ASN A 69 11700 10553 8135 -1070 -785 815 C
ATOM 293 CG ASN A 69 -0.703 9.440 23.715 1.00 78.79 C
ANISOU 293 CG ASN A 69 11798 10292 7845 -1121 -622 737 C
ATOM 294 OD1 ASN A 69 -0.671 9.256 22.499 1.00 79.41 O
ANISOU 294 OD1 ASN A 69 12025 10502 7646 -1219 -677 733 O
ATOM 295 ND2 ASN A 69 0.396 9.562 24.449 1.00 77.24 N
ANISOU 295 ND2 ASN A 69 11640 9878 7829 -1060 -419 669 N
ATOM 296 N TYR A 70 -4.499 7.853 26.128 1.00 76.20 N
ANISOU 296 N TYR A 70 10725 10300 7929 -1271 -1001 687 N
ATOM 297 CA TYR A 70 -5.549 7.828 27.142 1.00 77.96 C
ANISOU 297 CA TYR A 70 10674 10598 8348 -1236 -1027 740 C
ATOM 298 C TYR A 70 -5.033 7.201 28.427 1.00 77.42 C
ANISOU 298 C TYR A 70 10663 10291 8462 -1252 -830 611 C
ATOM 299 O TYR A 70 -5.374 7.650 29.527 1.00 78.33 O
ANISOU 299 O TYR A 70 10643 10362 8759 -1110 -747 680 O
ATOM 300 CB TYR A 70 -6.774 7.067 26.641 1.00 84.52 C
ANISOU 300 CB TYR A 70 11312 11712 9091 -1466 -1233 711 C
ATOM 301 CG TYR A 70 -7.584 7.791 25.596 1.00 85.57 C
ANISOU 301 CG TYR A 70 11290 12156 9066 -1406 -1480 890 C
ATOM 302 CD1 TYR A 70 -7.370 9.136 25.322 1.00 85.40 C
ANISOU 302 CD1 TYR A 70 11292 12122 9034 -1111 -1482 1104 C
ATOM 303 CD2 TYR A 70 -8.583 7.130 24.896 1.00 86.64 C
ANISOU 303 CD2 TYR A 70 11258 12598 9061 -1651 -1722 855 C
ATOM 304 CE1 TYR A 70 -8.119 9.796 24.364 1.00 86.46 C
ANISOU 304 CE1 TYR A 70 11299 12539 9012 -1020 -1719 1305 C
ATOM 305 CE2 TYR A 70 -9.335 7.780 23.942 1.00 87.68 C
ANISOU 305 CE2 TYR A 70 11229 13056 9029 -1581 -1987 1037 C
ATOM 306 CZ TYR A 70 -9.102 9.111 23.679 1.00 87.66 C
ANISOU 306 CZ TYR A 70 11261 13033 9010 -1244 -1985 1276 C
ATOM 307 OH TYR A 70 -9.857 9.753 22.725 1.00 88.77 O
ANISOU 307 OH TYR A 70 11257 13497 8976 -1141 -2259 1493 O
ATOM 308 N PHE A 71 -4.213 6.154 28.306 1.00 78.10 N
ANISOU 308 N PHE A 71 10965 10222 8488 -1408 -746 430 N
ATOM 309 CA PHE A 71 -3.563 5.584 29.479 1.00 77.12 C
ANISOU 309 CA PHE A 71 10928 9862 8514 -1382 -570 338 C
ATOM 310 C PHE A 71 -2.635 6.603 30.127 1.00 75.03 C
ANISOU 310 C PHE A 71 10708 9449 8350 -1143 -454 404 C
ATOM 311 O PHE A 71 -2.576 6.710 31.357 1.00 73.86 O
ANISOU 311 O PHE A 71 10520 9198 8343 -1049 -362 413 O
ATOM 312 CB PHE A 71 -2.788 4.327 29.084 1.00 76.62 C
ANISOU 312 CB PHE A 71 11103 9645 8363 -1542 -500 150 C
ATOM 313 CG PHE A 71 -3.654 3.205 28.577 1.00 76.88 C
ANISOU 313 CG PHE A 71 11144 9762 8303 -1827 -592 42 C
ATOM 314 CD1 PHE A 71 -5.014 3.181 28.835 1.00 78.61 C
ANISOU 314 CD1 PHE A 71 11115 10178 8576 -1945 -708 110 C
ATOM 315 CD2 PHE A 71 -3.106 2.185 27.818 1.00 75.60 C
ANISOU 315 CD2 PHE A 71 11235 9485 8005 -1988 -552 -140 C
ATOM 316 CE1 PHE A 71 -5.807 2.152 28.361 1.00 78.75 C
ANISOU 316 CE1 PHE A 71 11125 10283 8514 -2262 -804 -4 C
ATOM 317 CE2 PHE A 71 -3.893 1.156 27.339 1.00 75.88 C
ANISOU 317 CE2 PHE A 71 11315 9571 7946 -2291 -637 -269 C
ATOM 318 CZ PHE A 71 -5.245 1.140 27.610 1.00 77.34 C
ANISOU 318 CZ PHE A 71 11239 9961 8187 -2450 -775 -202 C
ATOM 319 N ILE A 72 -1.913 7.372 29.309 1.00 75.12 N
ANISOU 319 N ILE A 72 10814 9453 8276 -1065 -454 447 N
ATOM 320 CA ILE A 72 -1.041 8.417 29.835 1.00 72.76 C
ANISOU 320 CA ILE A 72 10555 9014 8075 -889 -351 503 C
ATOM 321 C ILE A 72 -1.856 9.543 30.462 1.00 73.54 C
ANISOU 321 C ILE A 72 10511 9149 8283 -726 -374 648 C
ATOM 322 O ILE A 72 -1.408 10.181 31.424 1.00 72.00 O
ANISOU 322 O ILE A 72 10337 8812 8209 -607 -277 650 O
ATOM 323 CB ILE A 72 -0.107 8.922 28.718 1.00 75.64 C
ANISOU 323 CB ILE A 72 11060 9362 8317 -887 -319 522 C
ATOM 324 CG1 ILE A 72 0.917 7.840 28.360 1.00 75.09 C
ANISOU 324 CG1 ILE A 72 11133 9214 8184 -992 -225 354 C
ATOM 325 CG2 ILE A 72 0.571 10.223 29.106 1.00 74.09 C
ANISOU 325 CG2 ILE A 72 10885 9041 8222 -746 -233 609 C
ATOM 326 CD1 ILE A 72 1.742 8.153 27.136 1.00 75.09 C
ANISOU 326 CD1 ILE A 72 11267 9233 8030 -1019 -164 358 C
ATOM 327 N THR A 73 -3.065 9.794 29.953 1.00 71.91 N
ANISOU 327 N THR A 73 10154 9136 8033 -712 -502 764 N
ATOM 328 CA THR A 73 -3.931 10.801 30.559 1.00 73.43 C
ANISOU 328 CA THR A 73 10189 9363 8346 -516 -500 907 C
ATOM 329 C THR A 73 -4.246 10.452 32.008 1.00 73.94 C
ANISOU 329 C THR A 73 10172 9364 8559 -491 -390 839 C
ATOM 330 O THR A 73 -4.069 11.277 32.911 1.00 73.30 O
ANISOU 330 O THR A 73 10122 9146 8583 -326 -279 859 O
ATOM 331 CB THR A 73 -5.221 10.946 29.750 1.00 74.33 C
ANISOU 331 CB THR A 73 10098 9750 8395 -500 -677 1049 C
ATOM 332 OG1 THR A 73 -4.908 11.382 28.422 1.00 73.61 O
ANISOU 332 OG1 THR A 73 10122 9720 8126 -500 -781 1138 O
ATOM 333 CG2 THR A 73 -6.153 11.953 30.408 1.00 76.24 C
ANISOU 333 CG2 THR A 73 10150 10030 8789 -248 -648 1202 C
ATOM 334 N SER A 74 -4.711 9.224 32.252 1.00 74.29 N
ANISOU 334 N SER A 74 10141 9490 8595 -669 -409 752 N
ATOM 335 CA SER A 74 -4.972 8.799 33.623 1.00 74.42 C
ANISOU 335 CA SER A 74 10116 9441 8721 -664 -284 702 C
ATOM 336 C SER A 74 -3.685 8.695 34.430 1.00 70.30 C
ANISOU 336 C SER A 74 9812 8684 8213 -631 -170 600 C
ATOM 337 O SER A 74 -3.692 8.952 35.639 1.00 69.87 O
ANISOU 337 O SER A 74 9773 8550 8226 -534 -62 590 O
ATOM 338 CB SER A 74 -5.711 7.463 33.633 1.00 74.45 C
ANISOU 338 CB SER A 74 10022 9555 8709 -898 -315 645 C
ATOM 339 OG SER A 74 -4.887 6.421 33.144 1.00 72.07 O
ANISOU 339 OG SER A 74 9922 9145 8317 -1075 -331 516 O
ATOM 340 N LEU A 75 -2.578 8.312 33.786 1.00 71.92 N
ANISOU 340 N LEU A 75 10178 8801 8346 -705 -192 522 N
ATOM 341 CA LEU A 75 -1.289 8.322 34.469 1.00 68.63 C
ANISOU 341 CA LEU A 75 9915 8206 7955 -654 -111 443 C
ATOM 342 C LEU A 75 -0.917 9.732 34.906 1.00 68.07 C
ANISOU 342 C LEU A 75 9866 8057 7941 -497 -69 486 C
ATOM 343 O LEU A 75 -0.423 9.935 36.021 1.00 66.89 O
ANISOU 343 O LEU A 75 9778 7805 7832 -438 -7 435 O
ATOM 344 CB LEU A 75 -0.205 7.739 33.562 1.00 69.73 C
ANISOU 344 CB LEU A 75 10175 8296 8023 -738 -122 363 C
ATOM 345 CG LEU A 75 1.190 7.613 34.181 1.00 67.42 C
ANISOU 345 CG LEU A 75 9981 7864 7770 -684 -56 286 C
ATOM 346 CD1 LEU A 75 1.180 6.623 35.336 1.00 66.72 C
ANISOU 346 CD1 LEU A 75 9932 7707 7712 -683 -21 244 C
ATOM 347 CD2 LEU A 75 2.218 7.215 33.135 1.00 67.30 C
ANISOU 347 CD2 LEU A 75 10044 7828 7701 -733 -35 223 C
ATOM 348 N ALA A 76 -1.149 10.722 34.041 1.00 69.44 N
ANISOU 348 N ALA A 76 10014 8266 8103 -436 -106 581 N
ATOM 349 CA ALA A 76 -0.885 12.104 34.424 1.00 69.17 C
ANISOU 349 CA ALA A 76 10038 8108 8134 -297 -47 624 C
ATOM 350 C ALA A 76 -1.868 12.588 35.482 1.00 71.19 C
ANISOU 350 C ALA A 76 10223 8361 8467 -157 18 657 C
ATOM 351 O ALA A 76 -1.497 13.390 36.345 1.00 70.46 O
ANISOU 351 O ALA A 76 10231 8118 8421 -72 103 612 O
ATOM 352 CB ALA A 76 -0.930 13.011 33.195 1.00 69.03 C
ANISOU 352 CB ALA A 76 10047 8102 8078 -252 -86 751 C
ATOM 353 N CYS A 77 -3.117 12.114 35.436 1.00 68.63 N
ANISOU 353 N CYS A 77 9722 8205 8150 -146 -9 723 N
ATOM 354 CA CYS A 77 -4.074 12.453 36.485 1.00 71.12 C
ANISOU 354 CA CYS A 77 9940 8541 8540 -10 94 748 C
ATOM 355 C CYS A 77 -3.629 11.901 37.831 1.00 69.57 C
ANISOU 355 C CYS A 77 9850 8255 8328 -57 192 624 C
ATOM 356 O CYS A 77 -3.709 12.594 38.853 1.00 69.96 O
ANISOU 356 O CYS A 77 9971 8210 8402 69 310 590 O
ATOM 357 CB CYS A 77 -5.462 11.924 36.128 1.00 70.65 C
ANISOU 357 CB CYS A 77 9617 8725 8504 -30 44 843 C
ATOM 358 SG CYS A 77 -6.229 12.738 34.718 1.00 72.56 S
ANISOU 358 SG CYS A 77 9696 9125 8747 93 -99 1032 S
ATOM 359 N ALA A 78 -3.170 10.649 37.855 1.00 72.40 N
ANISOU 359 N ALA A 78 10244 8635 8630 -228 150 558 N
ATOM 360 CA ALA A 78 -2.652 10.081 39.095 1.00 70.67 C
ANISOU 360 CA ALA A 78 10150 8331 8371 -255 220 471 C
ATOM 361 C ALA A 78 -1.475 10.895 39.615 1.00 68.63 C
ANISOU 361 C ALA A 78 10062 7921 8094 -192 225 389 C
ATOM 362 O ALA A 78 -1.315 11.067 40.829 1.00 68.96 O
ANISOU 362 O ALA A 78 10206 7905 8092 -142 293 330 O
ATOM 363 CB ALA A 78 -2.250 8.624 38.880 1.00 68.17 C
ANISOU 363 CB ALA A 78 9873 8022 8008 -418 171 435 C
ATOM 364 N ASP A 79 -0.645 11.413 38.708 1.00 68.25 N
ANISOU 364 N ASP A 79 10049 7818 8063 -214 155 382 N
ATOM 365 CA ASP A 79 0.442 12.293 39.115 1.00 67.15 C
ANISOU 365 CA ASP A 79 10042 7545 7929 -198 158 302 C
ATOM 366 C ASP A 79 -0.048 13.708 39.400 1.00 68.58 C
ANISOU 366 C ASP A 79 10279 7621 8156 -72 242 317 C
ATOM 367 O ASP A 79 0.512 14.385 40.268 1.00 68.61 O
ANISOU 367 O ASP A 79 10421 7502 8143 -62 278 216 O
ATOM 368 CB ASP A 79 1.533 12.314 38.042 1.00 72.65 C
ANISOU 368 CB ASP A 79 10746 8220 8638 -291 91 293 C
ATOM 369 CG ASP A 79 2.296 11.003 37.953 1.00 71.53 C
ANISOU 369 CG ASP A 79 10587 8132 8459 -376 38 244 C
ATOM 370 OD1 ASP A 79 2.376 10.283 38.970 1.00 71.65 O
ANISOU 370 OD1 ASP A 79 10633 8154 8437 -365 35 203 O
ATOM 371 OD2 ASP A 79 2.831 10.702 36.865 1.00 70.92 O
ANISOU 371 OD2 ASP A 79 10485 8081 8382 -439 15 253 O
ATOM 372 N LEU A 80 -1.087 14.168 38.698 1.00 67.65 N
ANISOU 372 N LEU A 80 10066 7547 8092 31 268 440 N
ATOM 373 CA LEU A 80 -1.614 15.507 38.950 1.00 69.11 C
ANISOU 373 CA LEU A 80 10317 7602 8340 203 372 473 C
ATOM 374 C LEU A 80 -2.286 15.592 40.314 1.00 71.06 C
ANISOU 374 C LEU A 80 10594 7836 8570 312 505 406 C
ATOM 375 O LEU A 80 -2.069 16.551 41.064 1.00 71.22 O
ANISOU 375 O LEU A 80 10793 7676 8590 387 604 315 O
ATOM 376 CB LEU A 80 -2.596 15.908 37.850 1.00 69.50 C
ANISOU 376 CB LEU A 80 10228 7732 8447 329 349 654 C
ATOM 377 CG LEU A 80 -3.217 17.290 38.042 1.00 70.91 C
ANISOU 377 CG LEU A 80 10476 7755 8712 568 471 722 C
ATOM 378 CD1 LEU A 80 -2.126 18.339 38.082 1.00 68.92 C
ANISOU 378 CD1 LEU A 80 10490 7222 8476 526 515 647 C
ATOM 379 CD2 LEU A 80 -4.214 17.589 36.935 1.00 72.77 C
ANISOU 379 CD2 LEU A 80 10539 8117 8996 725 413 937 C
ATOM 380 N VAL A 81 -3.118 14.603 40.648 1.00 68.40 N
ANISOU 380 N VAL A 81 10101 7677 8210 304 527 442 N
ATOM 381 CA VAL A 81 -3.737 14.575 41.968 1.00 70.80 C
ANISOU 381 CA VAL A 81 10440 7991 8472 390 685 385 C
ATOM 382 C VAL A 81 -2.677 14.370 43.042 1.00 69.34 C
ANISOU 382 C VAL A 81 10479 7710 8156 290 675 229 C
ATOM 383 O VAL A 81 -2.824 14.849 44.173 1.00 70.80 O
ANISOU 383 O VAL A 81 10812 7822 8266 370 805 136 O
ATOM 384 CB VAL A 81 -4.827 13.488 42.019 1.00 68.74 C
ANISOU 384 CB VAL A 81 9948 7949 8220 355 721 474 C
ATOM 385 CG1 VAL A 81 -5.439 13.404 43.407 1.00 71.49 C
ANISOU 385 CG1 VAL A 81 10340 8318 8506 429 922 426 C
ATOM 386 CG2 VAL A 81 -5.899 13.765 40.980 1.00 71.27 C
ANISOU 386 CG2 VAL A 81 10007 8410 8662 453 695 627 C
ATOM 387 N MET A 82 -1.592 13.667 42.706 1.00 69.64 N
ANISOU 387 N MET A 82 10546 7761 8154 127 520 197 N
ATOM 388 CA MET A 82 -0.468 13.545 43.627 1.00 68.84 C
ANISOU 388 CA MET A 82 10622 7600 7935 46 462 67 C
ATOM 389 C MET A 82 0.072 14.917 44.012 1.00 68.63 C
ANISOU 389 C MET A 82 10776 7398 7903 70 491 -56 C
ATOM 390 O MET A 82 0.500 15.128 45.152 1.00 69.11 O
ANISOU 390 O MET A 82 11009 7416 7834 48 500 -187 O
ATOM 391 CB MET A 82 0.637 12.700 42.992 1.00 71.68 C
ANISOU 391 CB MET A 82 10933 8003 8297 -91 297 71 C
ATOM 392 CG MET A 82 1.759 12.298 43.938 1.00 71.89 C
ANISOU 392 CG MET A 82 11075 8036 8206 -155 201 -26 C
ATOM 393 SD MET A 82 1.285 11.004 45.103 1.00 73.65 S
ANISOU 393 SD MET A 82 11358 8352 8275 -129 241 18 S
ATOM 394 CE MET A 82 1.321 9.577 44.022 1.00 70.68 C
ANISOU 394 CE MET A 82 10839 8032 7985 -194 182 131 C
ATOM 395 N GLY A 83 0.052 15.864 43.077 1.00 68.96 N
ANISOU 395 N GLY A 83 10805 7327 8069 105 505 -15 N
ATOM 396 CA GLY A 83 0.618 17.179 43.308 1.00 68.53 C
ANISOU 396 CA GLY A 83 10949 7055 8033 91 543 -129 C
ATOM 397 C GLY A 83 -0.366 18.209 43.820 1.00 70.09 C
ANISOU 397 C GLY A 83 11274 7102 8254 287 741 -152 C
ATOM 398 O GLY A 83 0.039 19.241 44.360 1.00 69.94 O
ANISOU 398 O GLY A 83 11491 6869 8214 271 805 -295 O
ATOM 399 N LEU A 84 -1.662 17.949 43.654 1.00 68.67 N
ANISOU 399 N LEU A 84 10935 7030 8126 471 847 -19 N
ATOM 400 CA LEU A 84 -2.680 18.869 44.148 1.00 70.39 C
ANISOU 400 CA LEU A 84 11231 7128 8385 711 1067 -25 C
ATOM 401 C LEU A 84 -3.183 18.501 45.541 1.00 71.90 C
ANISOU 401 C LEU A 84 11493 7391 8432 765 1214 -131 C
ATOM 402 O LEU A 84 -3.430 19.393 46.360 1.00 72.26 O
ANISOU 402 O LEU A 84 11757 7264 8433 890 1396 -258 O
ATOM 403 CB LEU A 84 -3.858 18.935 43.171 1.00 71.86 C
ANISOU 403 CB LEU A 84 11163 7417 8725 911 1109 195 C
ATOM 404 CG LEU A 84 -3.628 19.630 41.827 1.00 70.68 C
ANISOU 404 CG LEU A 84 11001 7159 8696 943 1020 331 C
ATOM 405 CD1 LEU A 84 -4.849 19.479 40.934 1.00 72.62 C
ANISOU 405 CD1 LEU A 84 10952 7592 9046 1134 1010 561 C
ATOM 406 CD2 LEU A 84 -3.300 21.101 42.035 1.00 70.01 C
ANISOU 406 CD2 LEU A 84 11219 6718 8662 1041 1149 253 C
ATOM 407 N ALA A 85 -3.337 17.205 45.833 1.00 75.30 N
ANISOU 407 N ALA A 85 11778 8055 8777 670 1158 -84 N
ATOM 408 CA ALA A 85 -3.927 16.762 47.090 1.00 76.69 C
ANISOU 408 CA ALA A 85 12011 8322 8804 719 1324 -140 C
ATOM 409 C ALA A 85 -2.950 16.110 48.055 1.00 75.53 C
ANISOU 409 C ALA A 85 12059 8209 8429 539 1215 -264 C
ATOM 410 O ALA A 85 -3.232 16.072 49.255 1.00 75.92 O
ANISOU 410 O ALA A 85 12274 8276 8295 581 1361 -351 O
ATOM 411 CB ALA A 85 -5.061 15.761 46.825 1.00 75.51 C
ANISOU 411 CB ALA A 85 11555 8414 8723 755 1391 35 C
ATOM 412 N VAL A 86 -1.826 15.593 47.575 1.00 76.44 N
ANISOU 412 N VAL A 86 12155 8349 8539 360 971 -263 N
ATOM 413 CA VAL A 86 -0.945 14.746 48.374 1.00 75.61 C
ANISOU 413 CA VAL A 86 12163 8329 8237 222 833 -321 C
ATOM 414 C VAL A 86 0.326 15.493 48.774 1.00 74.26 C
ANISOU 414 C VAL A 86 12196 8046 7971 108 687 -504 C
ATOM 415 O VAL A 86 0.583 15.710 49.959 1.00 74.42 O
ANISOU 415 O VAL A 86 12447 8059 7772 87 701 -645 O
ATOM 416 CB VAL A 86 -0.619 13.430 47.631 1.00 72.96 C
ANISOU 416 CB VAL A 86 11631 8127 7965 122 676 -179 C
ATOM 417 CG1 VAL A 86 0.378 12.594 48.415 1.00 71.96 C
ANISOU 417 CG1 VAL A 86 11619 8069 7652 28 520 -212 C
ATOM 418 CG2 VAL A 86 -1.901 12.641 47.363 1.00 74.47 C
ANISOU 418 CG2 VAL A 86 11636 8433 8227 175 816 -24 C
ATOM 419 N VAL A 87 1.125 15.913 47.788 1.00 76.16 N
ANISOU 419 N VAL A 87 12359 8213 8366 15 549 -509 N
ATOM 420 CA VAL A 87 2.437 16.501 48.087 1.00 75.33 C
ANISOU 420 CA VAL A 87 12387 8039 8198 -152 386 -676 C
ATOM 421 C VAL A 87 2.335 17.799 48.877 1.00 75.78 C
ANISOU 421 C VAL A 87 12728 7898 8165 -148 505 -877 C
ATOM 422 O VAL A 87 3.176 18.022 49.763 1.00 75.95 O
ANISOU 422 O VAL A 87 12922 7929 8005 -290 382 -1054 O
ATOM 423 CB VAL A 87 3.253 16.654 46.797 1.00 74.66 C
ANISOU 423 CB VAL A 87 12136 7922 8310 -264 262 -622 C
ATOM 424 CG1 VAL A 87 4.581 17.352 47.081 1.00 74.49 C
ANISOU 424 CG1 VAL A 87 12210 7838 8254 -470 113 -797 C
ATOM 425 CG2 VAL A 87 3.489 15.304 46.155 1.00 74.21 C
ANISOU 425 CG2 VAL A 87 11849 8049 8297 -274 149 -469 C
ATOM 426 N PRO A 88 1.393 18.711 48.603 1.00 78.03 N
ANISOU 426 N PRO A 88 13086 7997 8564 7 729 -870 N
ATOM 427 CA PRO A 88 1.318 19.918 49.447 1.00 78.51 C
ANISOU 427 CA PRO A 88 13475 7829 8525 21 870 -1090 C
ATOM 428 C PRO A 88 1.026 19.611 50.906 1.00 79.41 C
ANISOU 428 C PRO A 88 13791 8037 8344 57 945 -1218 C
ATOM 429 O PRO A 88 1.727 20.111 51.795 1.00 79.52 O
ANISOU 429 O PRO A 88 14072 7986 8157 -91 873 -1448 O
ATOM 430 CB PRO A 88 0.193 20.731 48.790 1.00 77.11 C
ANISOU 430 CB PRO A 88 13287 7459 8551 263 1120 -992 C
ATOM 431 CG PRO A 88 0.166 20.268 47.383 1.00 76.45 C
ANISOU 431 CG PRO A 88 12897 7468 8682 271 1017 -759 C
ATOM 432 CD PRO A 88 0.477 18.806 47.452 1.00 76.28 C
ANISOU 432 CD PRO A 88 12668 7744 8570 171 844 -674 C
ATOM 433 N PHE A 89 0.008 18.792 51.181 1.00 80.94 N
ANISOU 433 N PHE A 89 13869 8394 8489 226 1089 -1077 N
ATOM 434 CA PHE A 89 -0.327 18.471 52.563 1.00 81.69 C
ANISOU 434 CA PHE A 89 14172 8584 8280 264 1199 -1173 C
ATOM 435 C PHE A 89 0.753 17.638 53.243 1.00 81.28 C
ANISOU 435 C PHE A 89 14181 8722 7980 71 921 -1213 C
ATOM 436 O PHE A 89 0.838 17.648 54.475 1.00 81.76 O
ANISOU 436 O PHE A 89 14509 8832 7723 47 945 -1351 O
ATOM 437 CB PHE A 89 -1.673 17.754 52.617 1.00 81.51 C
ANISOU 437 CB PHE A 89 13975 8701 8293 462 1438 -987 C
ATOM 438 CG PHE A 89 -2.833 18.623 52.224 1.00 82.45 C
ANISOU 438 CG PHE A 89 14039 8675 8612 703 1733 -959 C
ATOM 439 CD1 PHE A 89 -3.421 19.480 53.141 1.00 83.12 C
ANISOU 439 CD1 PHE A 89 14395 8619 8568 857 2020 -1128 C
ATOM 440 CD2 PHE A 89 -3.320 18.600 50.929 1.00 82.74 C
ANISOU 440 CD2 PHE A 89 13763 8720 8956 792 1720 -763 C
ATOM 441 CE1 PHE A 89 -4.488 20.283 52.774 1.00 84.06 C
ANISOU 441 CE1 PHE A 89 14444 8601 8892 1130 2303 -1085 C
ATOM 442 CE2 PHE A 89 -4.381 19.399 50.556 1.00 83.79 C
ANISOU 442 CE2 PHE A 89 13818 8743 9275 1049 1964 -707 C
ATOM 443 CZ PHE A 89 -4.966 20.242 51.478 1.00 84.41 C
ANISOU 443 CZ PHE A 89 14141 8674 9256 1235 2261 -861 C
ATOM 444 N GLY A 90 1.574 16.918 52.475 1.00 81.97 N
ANISOU 444 N GLY A 90 14031 8922 8191 -45 662 -1090 N
ATOM 445 CA GLY A 90 2.751 16.295 53.051 1.00 81.83 C
ANISOU 445 CA GLY A 90 14050 9070 7973 -202 371 -1130 C
ATOM 446 C GLY A 90 3.871 17.279 53.299 1.00 81.86 C
ANISOU 446 C GLY A 90 14202 8988 7913 -403 187 -1369 C
ATOM 447 O GLY A 90 4.699 17.068 54.191 1.00 82.39 O
ANISOU 447 O GLY A 90 14387 9197 7720 -526 -29 -1473 O
ATOM 448 N ALA A 91 3.915 18.365 52.522 1.00 84.26 N
ANISOU 448 N ALA A 91 14506 9063 8446 -452 262 -1451 N
ATOM 449 CA ALA A 91 4.896 19.414 52.775 1.00 84.47 C
ANISOU 449 CA ALA A 91 14706 8962 8426 -687 129 -1701 C
ATOM 450 C ALA A 91 4.543 20.201 54.029 1.00 85.29 C
ANISOU 450 C ALA A 91 15220 8942 8245 -693 264 -1957 C
ATOM 451 O ALA A 91 5.424 20.528 54.831 1.00 85.94 O
ANISOU 451 O ALA A 91 15483 9073 8099 -913 65 -2177 O
ATOM 452 CB ALA A 91 4.997 20.343 51.567 1.00 83.67 C
ANISOU 452 CB ALA A 91 14530 8610 8650 -740 209 -1690 C
ATOM 453 N ALA A 92 3.257 20.510 54.219 1.00 88.37 N
ANISOU 453 N ALA A 92 15753 9188 8637 -453 602 -1940 N
ATOM 454 CA ALA A 92 2.828 21.153 55.455 1.00 89.22 C
ANISOU 454 CA ALA A 92 16267 9186 8445 -418 783 -2183 C
ATOM 455 C ALA A 92 3.039 20.242 56.656 1.00 89.80 C
ANISOU 455 C ALA A 92 16449 9554 8118 -454 650 -2200 C
ATOM 456 O ALA A 92 3.279 20.724 57.769 1.00 90.54 O
ANISOU 456 O ALA A 92 16902 9628 7872 -556 637 -2457 O
ATOM 457 CB ALA A 92 1.361 21.566 55.355 1.00 85.84 C
ANISOU 457 CB ALA A 92 15903 8580 8132 -105 1203 -2124 C
ATOM 458 N HIS A 93 2.951 18.926 56.451 1.00 91.61 N
ANISOU 458 N HIS A 93 16402 10041 8363 -373 553 -1929 N
ATOM 459 CA HIS A 93 3.207 17.982 57.532 1.00 92.12 C
ANISOU 459 CA HIS A 93 16574 10375 8051 -392 411 -1891 C
ATOM 460 C HIS A 93 4.669 18.006 57.959 1.00 92.57 C
ANISOU 460 C HIS A 93 16674 10581 7918 -647 -6 -2030 C
ATOM 461 O HIS A 93 4.973 17.965 59.157 1.00 93.42 O
ANISOU 461 O HIS A 93 17060 10823 7611 -720 -118 -2167 O
ATOM 462 CB HIS A 93 2.798 16.575 57.101 1.00 93.53 C
ANISOU 462 CB HIS A 93 16461 10738 8339 -254 416 -1555 C
ATOM 463 CG HIS A 93 2.996 15.539 58.162 1.00 93.96 C
ANISOU 463 CG HIS A 93 16645 11036 8021 -244 299 -1461 C
ATOM 464 ND1 HIS A 93 4.181 14.853 58.317 1.00 94.14 N
ANISOU 464 ND1 HIS A 93 16581 11258 7932 -350 -85 -1396 N
ATOM 465 CD2 HIS A 93 2.165 15.079 59.127 1.00 94.38 C
ANISOU 465 CD2 HIS A 93 16913 11165 7781 -127 525 -1402 C
ATOM 466 CE1 HIS A 93 4.070 14.010 59.328 1.00 94.60 C
ANISOU 466 CE1 HIS A 93 16816 11491 7636 -285 -108 -1287 C
ATOM 467 NE2 HIS A 93 2.856 14.128 59.837 1.00 94.66 N
ANISOU 467 NE2 HIS A 93 17021 11426 7520 -167 268 -1290 N
ATOM 468 N ILE A 94 5.588 18.065 56.995 1.00 91.79 N
ANISOU 468 N ILE A 94 16288 10486 8104 -787 -241 -1992 N
ATOM 469 CA ILE A 94 7.010 18.044 57.323 1.00 92.57 C
ANISOU 469 CA ILE A 94 16332 10772 8068 -1031 -649 -2103 C
ATOM 470 C ILE A 94 7.438 19.368 57.939 1.00 93.31 C
ANISOU 470 C ILE A 94 16745 10715 7994 -1277 -692 -2472 C
ATOM 471 O ILE A 94 8.115 19.400 58.973 1.00 94.45 O
ANISOU 471 O ILE A 94 17070 11042 7775 -1440 -944 -2641 O
ATOM 472 CB ILE A 94 7.846 17.714 56.075 1.00 88.47 C
ANISOU 472 CB ILE A 94 15384 10309 7921 -1105 -838 -1952 C
ATOM 473 CG1 ILE A 94 7.553 16.294 55.599 1.00 87.95 C
ANISOU 473 CG1 ILE A 94 15054 10400 7962 -885 -833 -1620 C
ATOM 474 CG2 ILE A 94 9.329 17.894 56.359 1.00 89.64 C
ANISOU 474 CG2 ILE A 94 15427 10651 7982 -1377 -1237 -2094 C
ATOM 475 CD1 ILE A 94 8.188 15.978 54.283 1.00 87.51 C
ANISOU 475 CD1 ILE A 94 14613 10362 8273 -917 -935 -1479 C
ATOM 476 N LEU A 95 7.057 20.480 57.310 1.00 95.34 N
ANISOU 476 N LEU A 95 17093 10631 8503 -1314 -455 -2601 N
ATOM 477 CA LEU A 95 7.553 21.778 57.752 1.00 96.04 C
ANISOU 477 CA LEU A 95 17493 10512 8485 -1589 -490 -2963 C
ATOM 478 C LEU A 95 7.009 22.131 59.132 1.00 96.84 C
ANISOU 478 C LEU A 95 18079 10578 8139 -1557 -353 -3203 C
ATOM 479 O LEU A 95 7.755 22.589 60.006 1.00 97.95 O
ANISOU 479 O LEU A 95 18410 10801 8005 -1810 -573 -3459 O
ATOM 480 CB LEU A 95 7.186 22.854 56.731 1.00 98.09 C
ANISOU 480 CB LEU A 95 17779 10363 9126 -1592 -225 -3005 C
ATOM 481 CG LEU A 95 7.686 22.624 55.299 1.00 97.23 C
ANISOU 481 CG LEU A 95 17238 10264 9439 -1634 -317 -2778 C
ATOM 482 CD1 LEU A 95 7.269 23.775 54.390 1.00 96.56 C
ANISOU 482 CD1 LEU A 95 17260 9754 9674 -1625 -43 -2812 C
ATOM 483 CD2 LEU A 95 9.184 22.357 55.218 1.00 97.93 C
ANISOU 483 CD2 LEU A 95 17064 10612 9532 -1952 -727 -2818 C
ATOM 484 N MET A 96 5.712 21.914 59.351 1.00 97.74 N
ANISOU 484 N MET A 96 18327 10607 8203 -1238 17 -3098 N
ATOM 485 CA MET A 96 5.092 22.225 60.634 1.00 98.53 C
ANISOU 485 CA MET A 96 18849 10683 7905 -1161 220 -3292 C
ATOM 486 C MET A 96 5.307 21.136 61.679 1.00 99.19 C
ANISOU 486 C MET A 96 18955 11165 7567 -1139 15 -3187 C
ATOM 487 O MET A 96 4.958 21.347 62.846 1.00101.93 O
ANISOU 487 O MET A 96 19548 11572 7607 -1097 131 -3302 O
ATOM 488 CB MET A 96 3.592 22.468 60.443 1.00105.04 C
ANISOU 488 CB MET A 96 19785 11266 8858 -819 736 -3221 C
ATOM 489 CG MET A 96 3.262 23.694 59.600 1.00104.68 C
ANISOU 489 CG MET A 96 19775 10799 9199 -779 976 -3316 C
ATOM 490 SD MET A 96 1.487 23.925 59.368 1.00104.61 S
ANISOU 490 SD MET A 96 19819 10566 9363 -318 1559 -3195 S
ATOM 491 CE MET A 96 1.460 25.319 58.242 1.00104.25 C
ANISOU 491 CE MET A 96 19779 10046 9785 -304 1703 -3255 C
ATOM 492 N LYS A 97 5.862 19.987 61.289 1.00 98.97 N
ANISOU 492 N LYS A 97 18617 11414 7572 -1138 -275 -2929 N
ATOM 493 CA LYS A 97 6.140 18.854 62.175 1.00 99.59 C
ANISOU 493 CA LYS A 97 18721 11856 7262 -1094 -497 -2774 C
ATOM 494 C LYS A 97 4.883 18.302 62.849 1.00 99.47 C
ANISOU 494 C LYS A 97 18922 11861 7011 -826 -124 -2641 C
ATOM 495 O LYS A 97 4.982 17.541 63.818 1.00100.08 O
ANISOU 495 O LYS A 97 19095 12202 6728 -784 -236 -2530 O
ATOM 496 CB LYS A 97 7.189 19.209 63.239 1.00101.54 C
ANISOU 496 CB LYS A 97 19085 12318 7178 -1339 -857 -2990 C
ATOM 497 CG LYS A 97 8.636 19.047 62.782 1.00101.74 C
ANISOU 497 CG LYS A 97 18803 12543 7309 -1583 -1357 -2992 C
ATOM 498 CD LYS A 97 9.108 20.215 61.928 1.00101.53 C
ANISOU 498 CD LYS A 97 18680 12250 7647 -1829 -1360 -3216 C
ATOM 499 CE LYS A 97 9.277 21.470 62.774 1.00106.01 C
ANISOU 499 CE LYS A 97 19492 12697 8088 -2026 -1318 -3563 C
ATOM 500 NZ LYS A 97 9.833 22.614 61.999 1.00106.50 N
ANISOU 500 NZ LYS A 97 19469 12491 8505 -2294 -1330 -3765 N
ATOM 501 N MET A 98 3.702 18.660 62.353 1.00 99.24 N
ANISOU 501 N MET A 98 18879 11583 7243 -630 322 -2605 N
ATOM 502 CA MET A 98 2.449 18.121 62.870 1.00 99.27 C
ANISOU 502 CA MET A 98 19001 11621 7095 -382 715 -2456 C
ATOM 503 C MET A 98 1.384 18.268 61.789 1.00 98.55 C
ANISOU 503 C MET A 98 18627 11325 7492 -177 1070 -2304 C
ATOM 504 O MET A 98 1.649 18.769 60.693 1.00 98.00 O
ANISOU 504 O MET A 98 18318 11089 7828 -219 997 -2308 O
ATOM 505 CB MET A 98 2.052 18.802 64.187 1.00103.11 C
ANISOU 505 CB MET A 98 19844 12090 7244 -374 916 -2682 C
ATOM 506 CG MET A 98 1.810 20.306 64.112 1.00105.20 C
ANISOU 506 CG MET A 98 20256 12030 7685 -398 1127 -2988 C
ATOM 507 SD MET A 98 0.129 20.781 63.663 1.00104.57 S
ANISOU 507 SD MET A 98 20170 11672 7889 -56 1761 -2939 S
ATOM 508 CE MET A 98 0.417 22.421 63.007 1.00105.67 C
ANISOU 508 CE MET A 98 20384 11395 8369 -138 1794 -3220 C
ATOM 509 N TRP A 99 0.171 17.819 62.105 1.00 94.28 N
ANISOU 509 N TRP A 99 18104 10819 6899 39 1455 -2158 N
ATOM 510 CA TRP A 99 -0.917 17.737 61.138 1.00 93.96 C
ANISOU 510 CA TRP A 99 17732 10674 7294 241 1763 -1963 C
ATOM 511 C TRP A 99 -1.965 18.790 61.475 1.00 94.66 C
ANISOU 511 C TRP A 99 18036 10549 7380 429 2225 -2153 C
ATOM 512 O TRP A 99 -2.574 18.749 62.550 1.00 95.38 O
ANISOU 512 O TRP A 99 18414 10704 7123 518 2510 -2228 O
ATOM 513 CB TRP A 99 -1.532 16.339 61.125 1.00 89.14 C
ANISOU 513 CB TRP A 99 16893 10283 6692 328 1851 -1622 C
ATOM 514 CG TRP A 99 -2.505 16.122 60.010 1.00 88.98 C
ANISOU 514 CG TRP A 99 16464 10211 7134 474 2066 -1410 C
ATOM 515 CD1 TRP A 99 -3.865 16.084 60.099 1.00 89.67 C
ANISOU 515 CD1 TRP A 99 16457 10307 7308 662 2497 -1319 C
ATOM 516 CD2 TRP A 99 -2.187 15.917 58.629 1.00 88.31 C
ANISOU 516 CD2 TRP A 99 15994 10086 7472 434 1852 -1265 C
ATOM 517 NE1 TRP A 99 -4.414 15.862 58.858 1.00 89.60 N
ANISOU 517 NE1 TRP A 99 16013 10282 7749 731 2526 -1125 N
ATOM 518 CE2 TRP A 99 -3.404 15.757 57.939 1.00 88.73 C
ANISOU 518 CE2 TRP A 99 15745 10134 7834 594 2137 -1092 C
ATOM 519 CE3 TRP A 99 -0.989 15.848 57.909 1.00 87.52 C
ANISOU 519 CE3 TRP A 99 15765 9976 7511 276 1453 -1264 C
ATOM 520 CZ2 TRP A 99 -3.459 15.535 56.564 1.00 88.43 C
ANISOU 520 CZ2 TRP A 99 15324 10076 8200 592 2015 -929 C
ATOM 521 CZ3 TRP A 99 -1.045 15.629 56.546 1.00 87.04 C
ANISOU 521 CZ3 TRP A 99 15334 9879 7857 287 1375 -1102 C
ATOM 522 CH2 TRP A 99 -2.271 15.476 55.887 1.00 87.51 C
ANISOU 522 CH2 TRP A 99 15139 9930 8183 440 1643 -941 C
ATOM 523 N THR A 100 -2.176 19.721 60.547 1.00 91.23 N
ANISOU 523 N THR A 100 17473 9858 7332 508 2316 -2217 N
ATOM 524 CA THR A 100 -3.055 20.866 60.743 1.00 91.90 C
ANISOU 524 CA THR A 100 17764 9680 7473 721 2737 -2407 C
ATOM 525 C THR A 100 -4.509 20.569 60.393 1.00 92.47 C
ANISOU 525 C THR A 100 17533 9807 7793 1026 3142 -2176 C
ATOM 526 O THR A 100 -5.409 21.276 60.864 1.00 93.32 O
ANISOU 526 O THR A 100 17813 9780 7863 1259 3566 -2303 O
ATOM 527 CB THR A 100 -2.541 22.036 59.887 1.00 90.42 C
ANISOU 527 CB THR A 100 17603 9163 7590 668 2631 -2558 C
ATOM 528 OG1 THR A 100 -1.191 22.345 60.257 1.00 90.14 O
ANISOU 528 OG1 THR A 100 17825 9096 7328 343 2262 -2793 O
ATOM 529 CG2 THR A 100 -3.396 23.286 60.046 1.00 91.21 C
ANISOU 529 CG2 THR A 100 17953 8928 7774 921 3067 -2752 C
ATOM 530 N PHE A 101 -4.764 19.510 59.629 1.00 89.72 N
ANISOU 530 N PHE A 101 16739 9668 7683 1024 3031 -1851 N
ATOM 531 CA PHE A 101 -5.972 19.414 58.826 1.00 90.35 C
ANISOU 531 CA PHE A 101 16414 9774 8142 1263 3297 -1629 C
ATOM 532 C PHE A 101 -7.000 18.425 59.363 1.00 91.08 C
ANISOU 532 C PHE A 101 16344 10130 8132 1348 3583 -1436 C
ATOM 533 O PHE A 101 -8.038 18.228 58.722 1.00 91.82 O
ANISOU 533 O PHE A 101 16043 10305 8538 1513 3786 -1238 O
ATOM 534 CB PHE A 101 -5.579 19.049 57.392 1.00 87.61 C
ANISOU 534 CB PHE A 101 15665 9446 8177 1176 2973 -1420 C
ATOM 535 CG PHE A 101 -4.550 19.975 56.807 1.00 86.80 C
ANISOU 535 CG PHE A 101 15698 9094 8189 1063 2713 -1580 C
ATOM 536 CD1 PHE A 101 -4.910 21.211 56.299 1.00 87.09 C
ANISOU 536 CD1 PHE A 101 15786 8842 8461 1243 2887 -1669 C
ATOM 537 CD2 PHE A 101 -3.210 19.619 56.800 1.00 85.81 C
ANISOU 537 CD2 PHE A 101 15652 9018 7933 778 2309 -1634 C
ATOM 538 CE1 PHE A 101 -3.956 22.064 55.777 1.00 86.28 C
ANISOU 538 CE1 PHE A 101 15836 8486 8461 1104 2673 -1807 C
ATOM 539 CE2 PHE A 101 -2.253 20.468 56.279 1.00 85.14 C
ANISOU 539 CE2 PHE A 101 15668 8720 7960 635 2091 -1781 C
ATOM 540 CZ PHE A 101 -2.627 21.692 55.767 1.00 85.32 C
ANISOU 540 CZ PHE A 101 15768 8436 8214 780 2280 -1869 C
ATOM 541 N GLY A 102 -6.750 17.802 60.509 1.00 90.04 N
ANISOU 541 N GLY A 102 16496 10146 7569 1230 3600 -1476 N
ATOM 542 CA GLY A 102 -7.729 16.934 61.132 1.00 90.71 C
ANISOU 542 CA GLY A 102 16490 10455 7522 1292 3927 -1301 C
ATOM 543 C GLY A 102 -7.577 15.477 60.727 1.00 90.16 C
ANISOU 543 C GLY A 102 16139 10595 7522 1112 3702 -997 C
ATOM 544 O GLY A 102 -6.922 15.134 59.745 1.00 89.40 O
ANISOU 544 O GLY A 102 15820 10481 7667 993 3335 -896 O
ATOM 545 N ASN A 103 -8.209 14.600 61.519 1.00 92.95 N
ANISOU 545 N ASN A 103 16532 11135 7650 1090 3958 -852 N
ATOM 546 CA ASN A 103 -8.162 13.172 61.215 1.00 92.43 C
ANISOU 546 CA ASN A 103 16250 11226 7643 917 3804 -559 C
ATOM 547 C ASN A 103 -8.955 12.826 59.963 1.00 92.80 C
ANISOU 547 C ASN A 103 15747 11321 8192 936 3843 -361 C
ATOM 548 O ASN A 103 -8.626 11.849 59.280 1.00 92.10 O
ANISOU 548 O ASN A 103 15459 11279 8256 772 3584 -174 O
ATOM 549 CB ASN A 103 -8.678 12.336 62.388 1.00 96.25 C
ANISOU 549 CB ASN A 103 16944 11871 7756 870 4103 -436 C
ATOM 550 CG ASN A 103 -7.738 12.342 63.575 1.00 95.95 C
ANISOU 550 CG ASN A 103 17452 11839 7164 801 3953 -566 C
ATOM 551 OD1 ASN A 103 -8.097 12.796 64.659 1.00 96.86 O
ANISOU 551 OD1 ASN A 103 17906 11982 6914 883 4266 -710 O
ATOM 552 ND2 ASN A 103 -6.528 11.826 63.378 1.00 94.98 N
ANISOU 552 ND2 ASN A 103 17413 11710 6964 656 3472 -515 N
ATOM 553 N PHE A 104 -10.008 13.586 59.653 1.00 89.54 N
ANISOU 553 N PHE A 104 15086 10904 8031 1140 4161 -396 N
ATOM 554 CA PHE A 104 -10.755 13.330 58.426 1.00 90.20 C
ANISOU 554 CA PHE A 104 14627 11067 8577 1159 4150 -212 C
ATOM 555 C PHE A 104 -9.859 13.481 57.205 1.00 89.40 C
ANISOU 555 C PHE A 104 14404 10846 8719 1085 3693 -214 C
ATOM 556 O PHE A 104 -9.727 12.557 56.394 1.00 89.01 O
ANISOU 556 O PHE A 104 14103 10871 8845 915 3467 -40 O
ATOM 557 CB PHE A 104 -11.961 14.262 58.316 1.00 91.32 C
ANISOU 557 CB PHE A 104 14521 11233 8943 1446 4540 -251 C
ATOM 558 CG PHE A 104 -12.720 14.104 57.025 1.00 92.28 C
ANISOU 558 CG PHE A 104 14066 11471 9526 1481 4480 -64 C
ATOM 559 CD1 PHE A 104 -13.554 13.016 56.822 1.00 92.97 C
ANISOU 559 CD1 PHE A 104 13776 11801 9747 1328 4591 160 C
ATOM 560 CD2 PHE A 104 -12.579 15.033 56.004 1.00 92.56 C
ANISOU 560 CD2 PHE A 104 13951 11373 9845 1645 4299 -108 C
ATOM 561 CE1 PHE A 104 -14.244 12.865 55.631 1.00 94.02 C
ANISOU 561 CE1 PHE A 104 13376 12072 10277 1330 4497 316 C
ATOM 562 CE2 PHE A 104 -13.266 14.887 54.812 1.00 93.63 C
ANISOU 562 CE2 PHE A 104 13569 11644 10360 1679 4211 73 C
ATOM 563 CZ PHE A 104 -14.100 13.803 54.627 1.00 94.41 C
ANISOU 563 CZ PHE A 104 13279 12015 10578 1517 4296 275 C
ATOM 564 N TRP A 105 -9.233 14.650 57.054 1.00 88.91 N
ANISOU 564 N TRP A 105 14537 10582 8662 1198 3574 -418 N
ATOM 565 CA TRP A 105 -8.342 14.841 55.918 1.00 88.17 C
ANISOU 565 CA TRP A 105 14345 10374 8782 1115 3173 -419 C
ATOM 566 C TRP A 105 -7.097 13.973 56.031 1.00 86.70 C
ANISOU 566 C TRP A 105 14333 10204 8407 869 2810 -398 C
ATOM 567 O TRP A 105 -6.508 13.609 55.008 1.00 86.09 O
ANISOU 567 O TRP A 105 14071 10112 8526 759 2506 -315 O
ATOM 568 CB TRP A 105 -7.959 16.312 55.769 1.00 86.14 C
ANISOU 568 CB TRP A 105 14282 9869 8576 1265 3160 -636 C
ATOM 569 CG TRP A 105 -7.093 16.534 54.574 1.00 85.42 C
ANISOU 569 CG TRP A 105 14080 9667 8710 1170 2791 -616 C
ATOM 570 CD1 TRP A 105 -5.766 16.846 54.567 1.00 84.17 C
ANISOU 570 CD1 TRP A 105 14172 9371 8438 1014 2493 -761 C
ATOM 571 CD2 TRP A 105 -7.480 16.388 53.203 1.00 86.01 C
ANISOU 571 CD2 TRP A 105 13750 9790 9139 1201 2680 -431 C
ATOM 572 NE1 TRP A 105 -5.310 16.937 53.274 1.00 83.79 N
ANISOU 572 NE1 TRP A 105 13905 9267 8664 957 2242 -676 N
ATOM 573 CE2 TRP A 105 -6.343 16.659 52.418 1.00 84.95 C
ANISOU 573 CE2 TRP A 105 13673 9523 9083 1074 2346 -474 C
ATOM 574 CE3 TRP A 105 -8.682 16.071 52.562 1.00 87.46 C
ANISOU 574 CE3 TRP A 105 13519 10138 9572 1313 2826 -235 C
ATOM 575 CZ2 TRP A 105 -6.371 16.622 51.025 1.00 85.28 C
ANISOU 575 CZ2 TRP A 105 13416 9575 9410 1067 2172 -328 C
ATOM 576 CZ3 TRP A 105 -8.708 16.035 51.181 1.00 87.96 C
ANISOU 576 CZ3 TRP A 105 13278 10226 9915 1298 2613 -96 C
ATOM 577 CH2 TRP A 105 -7.560 16.309 50.427 1.00 86.89 C
ANISOU 577 CH2 TRP A 105 13253 9941 9820 1182 2298 -142 C
ATOM 578 N CYS A 106 -6.686 13.628 57.254 1.00 86.82 N
ANISOU 578 N CYS A 106 14699 10258 8031 799 2841 -464 N
ATOM 579 CA CYS A 106 -5.594 12.674 57.423 1.00 85.61 C
ANISOU 579 CA CYS A 106 14677 10153 7696 609 2508 -395 C
ATOM 580 C CYS A 106 -5.915 11.346 56.750 1.00 85.25 C
ANISOU 580 C CYS A 106 14336 10214 7841 500 2454 -130 C
ATOM 581 O CYS A 106 -5.027 10.697 56.185 1.00 84.19 O
ANISOU 581 O CYS A 106 14153 10065 7769 383 2132 -57 O
ATOM 582 CB CYS A 106 -5.301 12.468 58.909 1.00 88.17 C
ANISOU 582 CB CYS A 106 15422 10539 7538 581 2581 -466 C
ATOM 583 SG CYS A 106 -3.987 11.274 59.265 1.00 87.01 S
ANISOU 583 SG CYS A 106 15450 10476 7135 410 2173 -342 S
ATOM 584 N GLU A 107 -7.181 10.927 56.798 1.00 85.91 N
ANISOU 584 N GLU A 107 14216 10402 8023 528 2778 6 N
ATOM 585 CA GLU A 107 -7.581 9.688 56.139 1.00 85.64 C
ANISOU 585 CA GLU A 107 13908 10450 8181 381 2747 234 C
ATOM 586 C GLU A 107 -7.548 9.837 54.621 1.00 85.67 C
ANISOU 586 C GLU A 107 13558 10423 8569 362 2535 261 C
ATOM 587 O GLU A 107 -6.883 9.060 53.927 1.00 84.51 O
ANISOU 587 O GLU A 107 13356 10245 8509 227 2265 341 O
ATOM 588 CB GLU A 107 -8.970 9.259 56.617 1.00 91.78 C
ANISOU 588 CB GLU A 107 14536 11369 8969 377 3163 359 C
ATOM 589 CG GLU A 107 -9.002 8.760 58.057 1.00 91.68 C
ANISOU 589 CG GLU A 107 14886 11400 8548 343 3381 398 C
ATOM 590 CD GLU A 107 -10.392 8.340 58.508 1.00 92.95 C
ANISOU 590 CD GLU A 107 14873 11711 8734 316 3835 531 C
ATOM 591 OE1 GLU A 107 -11.363 8.585 57.761 1.00 94.12 O
ANISOU 591 OE1 GLU A 107 14591 11947 9222 351 3980 566 O
ATOM 592 OE2 GLU A 107 -10.512 7.757 59.608 1.00 92.96 O
ANISOU 592 OE2 GLU A 107 15156 11755 8408 254 4046 612 O
ATOM 593 N PHE A 108 -8.265 10.831 54.086 1.00 83.21 N
ANISOU 593 N PHE A 108 13020 10118 8479 515 2662 204 N
ATOM 594 CA PHE A 108 -8.269 11.045 52.640 1.00 83.58 C
ANISOU 594 CA PHE A 108 12755 10151 8853 511 2458 245 C
ATOM 595 C PHE A 108 -6.868 11.302 52.099 1.00 82.27 C
ANISOU 595 C PHE A 108 12744 9839 8676 460 2100 154 C
ATOM 596 O PHE A 108 -6.476 10.717 51.083 1.00 81.60 O
ANISOU 596 O PHE A 108 12502 9758 8744 341 1871 232 O
ATOM 597 CB PHE A 108 -9.217 12.184 52.264 1.00 88.45 C
ANISOU 597 CB PHE A 108 13145 10785 9675 738 2650 215 C
ATOM 598 CG PHE A 108 -10.625 11.733 52.003 1.00 90.04 C
ANISOU 598 CG PHE A 108 12944 11200 10068 745 2875 373 C
ATOM 599 CD1 PHE A 108 -10.986 11.288 50.740 1.00 90.78 C
ANISOU 599 CD1 PHE A 108 12667 11402 10422 645 2698 502 C
ATOM 600 CD2 PHE A 108 -11.575 11.721 53.008 1.00 90.88 C
ANISOU 600 CD2 PHE A 108 13030 11419 10080 827 3261 389 C
ATOM 601 CE1 PHE A 108 -12.274 10.862 50.475 1.00 92.38 C
ANISOU 601 CE1 PHE A 108 12459 11837 10806 611 2869 640 C
ATOM 602 CE2 PHE A 108 -12.868 11.289 52.750 1.00 92.43 C
ANISOU 602 CE2 PHE A 108 12797 11846 10478 805 3468 539 C
ATOM 603 CZ PHE A 108 -13.216 10.861 51.482 1.00 93.20 C
ANISOU 603 CZ PHE A 108 12500 12064 10849 687 3255 663 C
ATOM 604 N TRP A 109 -6.100 12.180 52.752 1.00 82.07 N
ANISOU 604 N TRP A 109 13023 9689 8470 531 2059 -24 N
ATOM 605 CA TRP A 109 -4.723 12.413 52.319 1.00 80.88 C
ANISOU 605 CA TRP A 109 12994 9428 8309 450 1729 -113 C
ATOM 606 C TRP A 109 -3.968 11.099 52.179 1.00 79.44 C
ANISOU 606 C TRP A 109 12811 9304 8068 286 1504 -2 C
ATOM 607 O TRP A 109 -3.310 10.847 51.164 1.00 78.71 O
ANISOU 607 O TRP A 109 12586 9183 8136 212 1274 32 O
ATOM 608 CB TRP A 109 -3.993 13.330 53.298 1.00 81.12 C
ANISOU 608 CB TRP A 109 13380 9351 8092 483 1713 -329 C
ATOM 609 CG TRP A 109 -2.574 13.564 52.901 1.00 80.01 C
ANISOU 609 CG TRP A 109 13317 9130 7952 366 1378 -421 C
ATOM 610 CD1 TRP A 109 -2.129 14.302 51.844 1.00 79.79 C
ANISOU 610 CD1 TRP A 109 13176 8987 8154 354 1246 -464 C
ATOM 611 CD2 TRP A 109 -1.409 13.011 53.524 1.00 79.05 C
ANISOU 611 CD2 TRP A 109 13374 9064 7599 245 1134 -457 C
ATOM 612 NE1 TRP A 109 -0.756 14.267 51.788 1.00 78.66 N
ANISOU 612 NE1 TRP A 109 13114 8826 7946 212 959 -541 N
ATOM 613 CE2 TRP A 109 -0.290 13.478 52.807 1.00 78.37 C
ANISOU 613 CE2 TRP A 109 13237 8906 7635 154 871 -539 C
ATOM 614 CE3 TRP A 109 -1.203 12.177 54.627 1.00 78.85 C
ANISOU 614 CE3 TRP A 109 13543 9151 7265 213 1114 -413 C
ATOM 615 CZ2 TRP A 109 1.016 13.139 53.156 1.00 77.75 C
ANISOU 615 CZ2 TRP A 109 13244 8892 7407 39 582 -586 C
ATOM 616 CZ3 TRP A 109 0.093 11.840 54.972 1.00 78.27 C
ANISOU 616 CZ3 TRP A 109 13583 9130 7024 121 805 -445 C
ATOM 617 CH2 TRP A 109 1.186 12.321 54.239 1.00 77.84 C
ANISOU 617 CH2 TRP A 109 13425 9030 7122 38 539 -536 C
ATOM 618 N THR A 110 -4.057 10.248 53.200 1.00 82.71 N
ANISOU 618 N THR A 110 13395 9789 8245 243 1589 64 N
ATOM 619 CA THR A 110 -3.489 8.910 53.101 1.00 81.37 C
ANISOU 619 CA THR A 110 13240 9643 8033 124 1422 205 C
ATOM 620 C THR A 110 -4.213 8.085 52.043 1.00 81.15 C
ANISOU 620 C THR A 110 12919 9643 8271 37 1464 355 C
ATOM 621 O THR A 110 -3.575 7.400 51.234 1.00 79.87 O
ANISOU 621 O THR A 110 12684 9441 8222 -45 1258 409 O
ATOM 622 CB THR A 110 -3.559 8.217 54.461 1.00 84.06 C
ANISOU 622 CB THR A 110 13858 10036 8045 114 1541 276 C
ATOM 623 OG1 THR A 110 -2.784 8.954 55.417 1.00 84.26 O
ANISOU 623 OG1 THR A 110 14173 10058 7783 170 1447 117 O
ATOM 624 CG2 THR A 110 -3.032 6.804 54.362 1.00 82.84 C
ANISOU 624 CG2 THR A 110 13746 9867 7864 24 1394 451 C
ATOM 625 N SER A 111 -5.546 8.149 52.029 1.00 81.11 N
ANISOU 625 N SER A 111 12734 9718 8365 47 1732 413 N
ATOM 626 CA SER A 111 -6.324 7.342 51.095 1.00 81.25 C
ANISOU 626 CA SER A 111 12461 9796 8615 -80 1764 543 C
ATOM 627 C SER A 111 -6.074 7.759 49.651 1.00 81.20 C
ANISOU 627 C SER A 111 12227 9769 8854 -81 1553 508 C
ATOM 628 O SER A 111 -5.930 6.905 48.768 1.00 80.17 O
ANISOU 628 O SER A 111 11990 9630 8841 -221 1418 573 O
ATOM 629 CB SER A 111 -7.809 7.449 51.434 1.00 83.42 C
ANISOU 629 CB SER A 111 12537 10206 8951 -66 2093 606 C
ATOM 630 OG SER A 111 -8.090 6.890 52.703 1.00 83.36 O
ANISOU 630 OG SER A 111 12743 10224 8706 -101 2322 667 O
ATOM 631 N ILE A 112 -6.027 9.067 49.388 1.00 78.15 N
ANISOU 631 N ILE A 112 11798 9360 8534 71 1537 405 N
ATOM 632 CA ILE A 112 -5.763 9.546 48.035 1.00 78.33 C
ANISOU 632 CA ILE A 112 11644 9358 8758 80 1349 392 C
ATOM 633 C ILE A 112 -4.324 9.241 47.631 1.00 76.04 C
ANISOU 633 C ILE A 112 11500 8964 8427 4 1086 343 C
ATOM 634 O ILE A 112 -4.049 8.904 46.473 1.00 74.97 O
ANISOU 634 O ILE A 112 11234 8829 8424 -75 933 376 O
ATOM 635 CB ILE A 112 -6.081 11.049 47.934 1.00 76.96 C
ANISOU 635 CB ILE A 112 11435 9143 8661 280 1430 317 C
ATOM 636 CG1 ILE A 112 -7.572 11.293 48.176 1.00 79.16 C
ANISOU 636 CG1 ILE A 112 11493 9556 9029 394 1699 388 C
ATOM 637 CG2 ILE A 112 -5.666 11.602 46.583 1.00 77.31 C
ANISOU 637 CG2 ILE A 112 11362 9138 8875 292 1233 321 C
ATOM 638 CD1 ILE A 112 -7.926 12.750 48.384 1.00 80.74 C
ANISOU 638 CD1 ILE A 112 11725 9676 9275 648 1848 311 C
ATOM 639 N ASP A 113 -3.386 9.355 48.576 1.00 78.13 N
ANISOU 639 N ASP A 113 12026 9162 8499 27 1030 261 N
ATOM 640 CA ASP A 113 -1.994 9.017 48.293 1.00 76.42 C
ANISOU 640 CA ASP A 113 11901 8885 8249 -31 785 225 C
ATOM 641 C ASP A 113 -1.867 7.565 47.845 1.00 74.57 C
ANISOU 641 C ASP A 113 11620 8659 8054 -138 720 342 C
ATOM 642 O ASP A 113 -1.198 7.265 46.850 1.00 73.18 O
ANISOU 642 O ASP A 113 11365 8450 7990 -184 566 341 O
ATOM 643 CB ASP A 113 -1.134 9.283 49.532 1.00 74.86 C
ANISOU 643 CB ASP A 113 11965 8667 7811 5 725 133 C
ATOM 644 CG ASP A 113 0.357 9.201 49.247 1.00 74.01 C
ANISOU 644 CG ASP A 113 11890 8534 7696 -34 459 81 C
ATOM 645 OD1 ASP A 113 0.745 8.885 48.103 1.00 73.09 O
ANISOU 645 OD1 ASP A 113 11615 8400 7756 -78 355 117 O
ATOM 646 OD2 ASP A 113 1.148 9.471 50.174 1.00 74.27 O
ANISOU 646 OD2 ASP A 113 12099 8585 7537 -23 356 -2 O
ATOM 647 N VAL A 114 -2.509 6.648 48.571 1.00 75.62 N
ANISOU 647 N VAL A 114 11825 8817 8091 -182 862 441 N
ATOM 648 CA VAL A 114 -2.494 5.244 48.173 1.00 74.29 C
ANISOU 648 CA VAL A 114 11655 8604 7969 -298 837 550 C
ATOM 649 C VAL A 114 -3.208 5.063 46.839 1.00 74.26 C
ANISOU 649 C VAL A 114 11401 8631 8183 -409 840 567 C
ATOM 650 O VAL A 114 -2.777 4.274 45.988 1.00 72.91 O
ANISOU 650 O VAL A 114 11216 8394 8091 -494 732 580 O
ATOM 651 CB VAL A 114 -3.118 4.374 49.281 1.00 76.31 C
ANISOU 651 CB VAL A 114 12066 8857 8071 -345 1026 667 C
ATOM 652 CG1 VAL A 114 -3.217 2.925 48.836 1.00 75.36 C
ANISOU 652 CG1 VAL A 114 11974 8640 8021 -489 1034 780 C
ATOM 653 CG2 VAL A 114 -2.301 4.487 50.557 1.00 76.38 C
ANISOU 653 CG2 VAL A 114 12353 8854 7813 -232 977 661 C
ATOM 654 N LEU A 115 -4.302 5.799 46.630 1.00 73.44 N
ANISOU 654 N LEU A 115 11099 8636 8170 -396 960 564 N
ATOM 655 CA LEU A 115 -5.051 5.695 45.380 1.00 74.27 C
ANISOU 655 CA LEU A 115 10941 8821 8456 -498 929 589 C
ATOM 656 C LEU A 115 -4.202 6.085 44.176 1.00 72.96 C
ANISOU 656 C LEU A 115 10739 8614 8368 -478 720 526 C
ATOM 657 O LEU A 115 -4.245 5.418 43.136 1.00 72.38 O
ANISOU 657 O LEU A 115 10586 8547 8369 -609 632 536 O
ATOM 658 CB LEU A 115 -6.304 6.566 45.450 1.00 73.96 C
ANISOU 658 CB LEU A 115 10670 8932 8500 -423 1079 614 C
ATOM 659 CG LEU A 115 -7.150 6.625 44.179 1.00 75.93 C
ANISOU 659 CG LEU A 115 10606 9321 8922 -500 1011 656 C
ATOM 660 CD1 LEU A 115 -7.637 5.248 43.796 1.00 75.84 C
ANISOU 660 CD1 LEU A 115 10521 9346 8949 -766 1009 706 C
ATOM 661 CD2 LEU A 115 -8.322 7.568 44.373 1.00 79.20 C
ANISOU 661 CD2 LEU A 115 10774 9894 9425 -355 1162 700 C
ATOM 662 N CYS A 116 -3.428 7.165 44.293 1.00 73.64 N
ANISOU 662 N CYS A 116 10898 8654 8426 -336 652 453 N
ATOM 663 CA CYS A 116 -2.651 7.636 43.152 1.00 72.37 C
ANISOU 663 CA CYS A 116 10698 8460 8339 -328 492 408 C
ATOM 664 C CYS A 116 -1.497 6.699 42.824 1.00 69.85 C
ANISOU 664 C CYS A 116 10490 8058 7990 -396 373 383 C
ATOM 665 O CYS A 116 -1.108 6.585 41.657 1.00 68.77 O
ANISOU 665 O CYS A 116 10294 7916 7918 -447 280 366 O
ATOM 666 CB CYS A 116 -2.129 9.047 43.414 1.00 69.43 C
ANISOU 666 CB CYS A 116 10389 8034 7956 -193 477 335 C
ATOM 667 SG CYS A 116 -3.412 10.314 43.489 1.00 73.01 S
ANISOU 667 SG CYS A 116 10715 8538 8486 -48 626 365 S
ATOM 668 N VAL A 117 -0.937 6.026 43.826 1.00 70.81 N
ANISOU 668 N VAL A 117 10778 8119 8006 -377 381 390 N
ATOM 669 CA VAL A 117 0.163 5.105 43.561 1.00 69.36 C
ANISOU 669 CA VAL A 117 10688 7854 7812 -389 280 385 C
ATOM 670 C VAL A 117 -0.362 3.786 43.009 1.00 68.89 C
ANISOU 670 C VAL A 117 10638 7740 7796 -518 330 437 C
ATOM 671 O VAL A 117 0.237 3.196 42.104 1.00 68.00 O
ANISOU 671 O VAL A 117 10538 7562 7735 -551 267 407 O
ATOM 672 CB VAL A 117 0.999 4.901 44.836 1.00 70.87 C
ANISOU 672 CB VAL A 117 11052 8013 7864 -291 240 395 C
ATOM 673 CG1 VAL A 117 2.139 3.925 44.580 1.00 70.37 C
ANISOU 673 CG1 VAL A 117 11054 7873 7810 -249 138 414 C
ATOM 674 CG2 VAL A 117 1.529 6.232 45.334 1.00 72.02 C
ANISOU 674 CG2 VAL A 117 11200 8207 7956 -216 176 305 C
ATOM 675 N THR A 118 -1.494 3.309 43.534 1.00 71.69 N
ANISOU 675 N THR A 118 10994 8114 8131 -608 463 506 N
ATOM 676 CA THR A 118 -2.078 2.071 43.031 1.00 71.72 C
ANISOU 676 CA THR A 118 11017 8050 8184 -787 519 542 C
ATOM 677 C THR A 118 -2.562 2.233 41.594 1.00 72.05 C
ANISOU 677 C THR A 118 10877 8173 8327 -912 454 484 C
ATOM 678 O THR A 118 -2.331 1.358 40.752 1.00 71.45 O
ANISOU 678 O THR A 118 10865 8005 8277 -1026 418 443 O
ATOM 679 CB THR A 118 -3.225 1.623 43.939 1.00 72.66 C
ANISOU 679 CB THR A 118 11145 8194 8267 -891 696 633 C
ATOM 680 OG1 THR A 118 -2.729 1.392 45.263 1.00 72.40 O
ANISOU 680 OG1 THR A 118 11331 8086 8092 -775 753 700 O
ATOM 681 CG2 THR A 118 -3.860 0.345 43.413 1.00 72.94 C
ANISOU 681 CG2 THR A 118 11205 8142 8366 -1135 760 658 C
ATOM 682 N ALA A 119 -3.227 3.351 41.292 1.00 69.41 N
ANISOU 682 N ALA A 119 10335 8002 8034 -879 438 483 N
ATOM 683 CA ALA A 119 -3.706 3.588 39.936 1.00 70.38 C
ANISOU 683 CA ALA A 119 10285 8236 8221 -975 346 455 C
ATOM 684 C ALA A 119 -2.571 3.838 38.952 1.00 68.62 C
ANISOU 684 C ALA A 119 10130 7957 7984 -918 225 384 C
ATOM 685 O ALA A 119 -2.752 3.613 37.751 1.00 69.07 O
ANISOU 685 O ALA A 119 10135 8064 8044 -1033 149 349 O
ATOM 686 CB ALA A 119 -4.677 4.768 39.916 1.00 70.67 C
ANISOU 686 CB ALA A 119 10086 8456 8308 -896 362 506 C
ATOM 687 N SER A 120 -1.413 4.302 39.427 1.00 70.00 N
ANISOU 687 N SER A 120 10413 8049 8135 -760 206 360 N
ATOM 688 CA SER A 120 -0.290 4.556 38.530 1.00 68.69 C
ANISOU 688 CA SER A 120 10282 7846 7971 -715 124 298 C
ATOM 689 C SER A 120 0.328 3.254 38.036 1.00 67.99 C
ANISOU 689 C SER A 120 10326 7639 7870 -782 129 248 C
ATOM 690 O SER A 120 0.566 3.086 36.834 1.00 68.03 O
ANISOU 690 O SER A 120 10333 7651 7865 -847 95 191 O
ATOM 691 CB SER A 120 0.764 5.413 39.230 1.00 68.70 C
ANISOU 691 CB SER A 120 10322 7815 7965 -561 100 280 C
ATOM 692 OG SER A 120 0.269 6.709 39.510 1.00 69.53 O
ANISOU 692 OG SER A 120 10348 7984 8085 -498 112 300 O
ATOM 693 N ILE A 121 0.602 2.324 38.952 1.00 68.53 N
ANISOU 693 N ILE A 121 10533 7582 7922 -752 183 272 N
ATOM 694 CA ILE A 121 1.268 1.084 38.566 1.00 68.35 C
ANISOU 694 CA ILE A 121 10672 7396 7903 -764 211 231 C
ATOM 695 C ILE A 121 0.349 0.213 37.717 1.00 68.87 C
ANISOU 695 C ILE A 121 10781 7421 7968 -990 249 186 C
ATOM 696 O ILE A 121 0.802 -0.438 36.768 1.00 68.94 O
ANISOU 696 O ILE A 121 10892 7335 7968 -1036 259 96 O
ATOM 697 CB ILE A 121 1.787 0.339 39.811 1.00 69.35 C
ANISOU 697 CB ILE A 121 10957 7386 8006 -641 252 304 C
ATOM 698 CG1 ILE A 121 2.587 -0.900 39.396 1.00 69.70 C
ANISOU 698 CG1 ILE A 121 11179 7230 8076 -589 295 274 C
ATOM 699 CG2 ILE A 121 0.646 -0.015 40.759 1.00 69.70 C
ANISOU 699 CG2 ILE A 121 11050 7418 8015 -745 337 393 C
ATOM 700 CD1 ILE A 121 3.837 -0.596 38.603 1.00 70.15 C
ANISOU 700 CD1 ILE A 121 11172 7313 8170 -452 251 197 C
ATOM 701 N GLU A 122 -0.949 0.186 38.028 1.00 68.73 N
ANISOU 701 N GLU A 122 10679 7482 7955 -1148 277 233 N
ATOM 702 CA GLU A 122 -1.866 -0.577 37.187 1.00 69.73 C
ANISOU 702 CA GLU A 122 10806 7608 8079 -1414 281 175 C
ATOM 703 C GLU A 122 -1.991 0.050 35.807 1.00 70.42 C
ANISOU 703 C GLU A 122 10768 7860 8130 -1476 165 102 C
ATOM 704 O GLU A 122 -2.091 -0.665 34.804 1.00 70.87 O
ANISOU 704 O GLU A 122 10917 7872 8138 -1649 142 -3 O
ATOM 705 CB GLU A 122 -3.238 -0.701 37.844 1.00 76.83 C
ANISOU 705 CB GLU A 122 11581 8601 9010 -1583 340 252 C
ATOM 706 CG GLU A 122 -3.267 -1.645 39.027 1.00 76.51 C
ANISOU 706 CG GLU A 122 11730 8366 8974 -1603 485 328 C
ATOM 707 CD GLU A 122 -4.661 -1.815 39.591 1.00 78.15 C
ANISOU 707 CD GLU A 122 11797 8679 9217 -1811 582 402 C
ATOM 708 OE1 GLU A 122 -5.582 -1.121 39.111 1.00 79.77 O
ANISOU 708 OE1 GLU A 122 11716 9136 9458 -1900 520 397 O
ATOM 709 OE2 GLU A 122 -4.834 -2.637 40.516 1.00 78.12 O
ANISOU 709 OE2 GLU A 122 11960 8516 9205 -1876 727 480 O
ATOM 710 N THR A 123 -1.979 1.381 35.734 1.00 70.20 N
ANISOU 710 N THR A 123 10562 8006 8106 -1338 95 155 N
ATOM 711 CA THR A 123 -1.974 2.042 34.434 1.00 71.21 C
ANISOU 711 CA THR A 123 10607 8276 8175 -1361 -12 121 C
ATOM 712 C THR A 123 -0.720 1.678 33.649 1.00 70.10 C
ANISOU 712 C THR A 123 10646 8010 7978 -1312 8 20 C
ATOM 713 O THR A 123 -0.798 1.289 32.479 1.00 71.02 O
ANISOU 713 O THR A 123 10830 8155 8002 -1448 -30 -68 O
ATOM 714 CB THR A 123 -2.085 3.556 34.610 1.00 68.57 C
ANISOU 714 CB THR A 123 10101 8085 7869 -1191 -57 218 C
ATOM 715 OG1 THR A 123 -3.324 3.872 35.259 1.00 70.50 O
ANISOU 715 OG1 THR A 123 10160 8457 8169 -1213 -48 305 O
ATOM 716 CG2 THR A 123 -2.036 4.248 33.264 1.00 70.10 C
ANISOU 716 CG2 THR A 123 10246 8406 7985 -1199 -160 219 C
ATOM 717 N LEU A 124 0.449 1.784 34.287 1.00 70.39 N
ANISOU 717 N LEU A 124 10756 7927 8063 -1120 70 27 N
ATOM 718 CA LEU A 124 1.679 1.316 33.655 1.00 70.12 C
ANISOU 718 CA LEU A 124 10859 7777 8005 -1048 125 -63 C
ATOM 719 C LEU A 124 1.622 -0.176 33.363 1.00 70.40 C
ANISOU 719 C LEU A 124 11104 7628 8016 -1162 201 -162 C
ATOM 720 O LEU A 124 2.273 -0.652 32.426 1.00 70.93 O
ANISOU 720 O LEU A 124 11301 7621 8029 -1163 257 -272 O
ATOM 721 CB LEU A 124 2.879 1.631 34.542 1.00 68.78 C
ANISOU 721 CB LEU A 124 10676 7546 7912 -826 158 -25 C
ATOM 722 CG LEU A 124 3.231 3.107 34.688 1.00 68.46 C
ANISOU 722 CG LEU A 124 10478 7639 7895 -734 103 30 C
ATOM 723 CD1 LEU A 124 4.314 3.270 35.729 1.00 68.41 C
ANISOU 723 CD1 LEU A 124 10452 7587 7953 -567 106 51 C
ATOM 724 CD2 LEU A 124 3.684 3.667 33.353 1.00 69.26 C
ANISOU 724 CD2 LEU A 124 10556 7815 7944 -764 109 -10 C
ATOM 725 N CYS A 125 0.858 -0.929 34.153 1.00 69.36 N
ANISOU 725 N CYS A 125 11030 7401 7921 -1263 230 -127 N
ATOM 726 CA CYS A 125 0.681 -2.346 33.867 1.00 69.71 C
ANISOU 726 CA CYS A 125 11309 7227 7949 -1415 314 -223 C
ATOM 727 C CYS A 125 -0.242 -2.550 32.672 1.00 70.73 C
ANISOU 727 C CYS A 125 11440 7455 7977 -1707 247 -337 C
ATOM 728 O CYS A 125 0.001 -3.430 31.838 1.00 71.11 O
ANISOU 728 O CYS A 125 11708 7352 7957 -1815 304 -488 O
ATOM 729 CB CYS A 125 0.140 -3.062 35.103 1.00 72.16 C
ANISOU 729 CB CYS A 125 11698 7393 8326 -1460 383 -131 C
ATOM 730 SG CYS A 125 0.010 -4.847 34.936 1.00 72.60 S
ANISOU 730 SG CYS A 125 12108 7088 8389 -1639 524 -227 S
ATOM 731 N VAL A 126 -1.302 -1.744 32.567 1.00 70.33 N
ANISOU 731 N VAL A 126 11149 7666 7908 -1829 122 -271 N
ATOM 732 CA VAL A 126 -2.192 -1.839 31.413 1.00 71.82 C
ANISOU 732 CA VAL A 126 11292 8016 7979 -2099 6 -361 C
ATOM 733 C VAL A 126 -1.466 -1.415 30.141 1.00 72.16 C
ANISOU 733 C VAL A 126 11407 8132 7879 -2037 -36 -447 C
ATOM 734 O VAL A 126 -1.648 -2.019 29.078 1.00 72.83 O
ANISOU 734 O VAL A 126 11641 8212 7818 -2241 -67 -598 O
ATOM 735 CB VAL A 126 -3.469 -1.010 31.646 1.00 70.37 C
ANISOU 735 CB VAL A 126 10784 8126 7827 -2184 -124 -237 C
ATOM 736 CG1 VAL A 126 -4.305 -0.951 30.378 1.00 72.21 C
ANISOU 736 CG1 VAL A 126 10923 8593 7919 -2426 -299 -306 C
ATOM 737 CG2 VAL A 126 -4.287 -1.610 32.773 1.00 70.44 C
ANISOU 737 CG2 VAL A 126 10738 8071 7956 -2309 -44 -175 C
ATOM 738 N ILE A 127 -0.630 -0.376 30.230 1.00 71.53 N
ANISOU 738 N ILE A 127 11239 8115 7823 -1778 -25 -359 N
ATOM 739 CA ILE A 127 0.150 0.057 29.072 1.00 72.07 C
ANISOU 739 CA ILE A 127 11382 8244 7758 -1715 -20 -419 C
ATOM 740 C ILE A 127 1.028 -1.080 28.568 1.00 71.70 C
ANISOU 740 C ILE A 127 11621 7965 7657 -1722 133 -596 C
ATOM 741 O ILE A 127 1.044 -1.393 27.372 1.00 72.51 O
ANISOU 741 O ILE A 127 11877 8098 7577 -1854 133 -731 O
ATOM 742 CB ILE A 127 0.991 1.300 29.418 1.00 70.03 C
ANISOU 742 CB ILE A 127 10988 8046 7573 -1460 3 -294 C
ATOM 743 CG1 ILE A 127 0.088 2.493 29.722 1.00 71.09 C
ANISOU 743 CG1 ILE A 127 10886 8384 7739 -1439 -130 -135 C
ATOM 744 CG2 ILE A 127 1.944 1.635 28.282 1.00 70.77 C
ANISOU 744 CG2 ILE A 127 11177 8170 7541 -1404 65 -351 C
ATOM 745 CD1 ILE A 127 0.823 3.684 30.294 1.00 70.52 C
ANISOU 745 CD1 ILE A 127 10716 8314 7765 -1220 -95 -26 C
ATOM 746 N ALA A 128 1.773 -1.715 29.476 1.00 72.54 N
ANISOU 746 N ALA A 128 11817 7836 7909 -1561 270 -595 N
ATOM 747 CA ALA A 128 2.679 -2.788 29.079 1.00 72.79 C
ANISOU 747 CA ALA A 128 12114 7618 7923 -1495 444 -745 C
ATOM 748 C ALA A 128 1.924 -3.946 28.437 1.00 73.18 C
ANISOU 748 C ALA A 128 12417 7529 7861 -1782 460 -921 C
ATOM 749 O ALA A 128 2.367 -4.501 27.425 1.00 73.89 O
ANISOU 749 O ALA A 128 12737 7520 7817 -1824 561 -1100 O
ATOM 750 CB ALA A 128 3.479 -3.272 30.287 1.00 71.96 C
ANISOU 750 CB ALA A 128 12039 7301 8003 -1248 554 -669 C
ATOM 751 N VAL A 129 0.780 -4.325 29.011 1.00 75.34 N
ANISOU 751 N VAL A 129 12656 7790 8181 -2003 375 -886 N
ATOM 752 CA VAL A 129 -0.007 -5.412 28.437 1.00 75.90 C
ANISOU 752 CA VAL A 129 12952 7731 8155 -2342 376 -1064 C
ATOM 753 C VAL A 129 -0.657 -4.967 27.134 1.00 76.92 C
ANISOU 753 C VAL A 129 13030 8143 8055 -2584 206 -1166 C
ATOM 754 O VAL A 129 -0.760 -5.746 26.177 1.00 77.52 O
ANISOU 754 O VAL A 129 13370 8122 7960 -2804 231 -1385 O
ATOM 755 CB VAL A 129 -1.047 -5.911 29.457 1.00 73.81 C
ANISOU 755 CB VAL A 129 12630 7396 8020 -2538 349 -981 C
ATOM 756 CG1 VAL A 129 -1.939 -6.973 28.835 1.00 74.61 C
ANISOU 756 CG1 VAL A 129 12937 7384 8029 -2961 333 -1175 C
ATOM 757 CG2 VAL A 129 -0.350 -6.455 30.692 1.00 72.95 C
ANISOU 757 CG2 VAL A 129 12641 6988 8087 -2291 520 -874 C
ATOM 758 N ASP A 130 -1.106 -3.711 27.073 1.00 74.99 N
ANISOU 758 N ASP A 130 12467 8243 7785 -2540 31 -1007 N
ATOM 759 CA ASP A 130 -1.622 -3.173 25.818 1.00 76.20 C
ANISOU 759 CA ASP A 130 12566 8689 7696 -2706 -149 -1056 C
ATOM 760 C ASP A 130 -0.555 -3.188 24.732 1.00 76.36 C
ANISOU 760 C ASP A 130 12832 8656 7526 -2601 -33 -1189 C
ATOM 761 O ASP A 130 -0.837 -3.537 23.579 1.00 77.11 O
ANISOU 761 O ASP A 130 13108 8829 7363 -2825 -98 -1358 O
ATOM 762 CB ASP A 130 -2.149 -1.756 26.031 1.00 77.40 C
ANISOU 762 CB ASP A 130 12354 9170 7885 -2589 -323 -822 C
ATOM 763 CG ASP A 130 -2.736 -1.160 24.773 1.00 78.79 C
ANISOU 763 CG ASP A 130 12465 9666 7804 -2727 -535 -822 C
ATOM 764 OD1 ASP A 130 -3.844 -1.579 24.374 1.00 79.69 O
ANISOU 764 OD1 ASP A 130 12519 9941 7818 -3032 -715 -889 O
ATOM 765 OD2 ASP A 130 -2.087 -0.272 24.182 1.00 79.00 O
ANISOU 765 OD2 ASP A 130 12500 9794 7724 -2541 -527 -746 O
ATOM 766 N ARG A 131 0.679 -2.817 25.080 1.00 76.70 N
ANISOU 766 N ARG A 131 12877 8585 7680 -2275 142 -1121 N
ATOM 767 CA ARG A 131 1.753 -2.825 24.093 1.00 77.18 C
ANISOU 767 CA ARG A 131 13137 8605 7581 -2160 301 -1238 C
ATOM 768 C ARG A 131 2.174 -4.241 23.725 1.00 77.25 C
ANISOU 768 C ARG A 131 13518 8298 7534 -2229 499 -1494 C
ATOM 769 O ARG A 131 2.708 -4.459 22.632 1.00 77.95 O
ANISOU 769 O ARG A 131 13837 8374 7407 -2242 617 -1659 O
ATOM 770 CB ARG A 131 2.953 -2.029 24.607 1.00 73.30 C
ANISOU 770 CB ARG A 131 12492 8106 7255 -1817 435 -1092 C
ATOM 771 CG ARG A 131 2.701 -0.534 24.767 1.00 73.48 C
ANISOU 771 CG ARG A 131 12221 8398 7301 -1744 282 -867 C
ATOM 772 CD ARG A 131 2.451 0.140 23.427 1.00 74.47 C
ANISOU 772 CD ARG A 131 12391 8763 7139 -1854 193 -863 C
ATOM 773 NE ARG A 131 1.040 0.131 23.050 1.00 74.91 N
ANISOU 773 NE ARG A 131 12402 9011 7049 -2106 -60 -854 N
ATOM 774 CZ ARG A 131 0.594 0.390 21.825 1.00 75.74 C
ANISOU 774 CZ ARG A 131 12595 9333 6849 -2260 -189 -882 C
ATOM 775 NH1 ARG A 131 1.449 0.673 20.852 1.00 76.04 N
ANISOU 775 NH1 ARG A 131 12808 9401 6681 -2192 -56 -921 N
ATOM 776 NH2 ARG A 131 -0.706 0.362 21.571 1.00 76.38 N
ANISOU 776 NH2 ARG A 131 12578 9623 6819 -2484 -452 -863 N
ATOM 777 N TYR A 132 1.951 -5.215 24.611 1.00 80.07 N
ANISOU 777 N TYR A 132 13970 8379 8073 -2266 561 -1529 N
ATOM 778 CA TYR A 132 2.268 -6.595 24.262 1.00 80.34 C
ANISOU 778 CA TYR A 132 14404 8058 8063 -2337 760 -1773 C
ATOM 779 C TYR A 132 1.290 -7.142 23.231 1.00 80.96 C
ANISOU 779 C TYR A 132 14702 8185 7872 -2762 642 -2000 C
ATOM 780 O TYR A 132 1.700 -7.677 22.195 1.00 81.61 O
ANISOU 780 O TYR A 132 15110 8161 7737 -2823 772 -2239 O
ATOM 781 CB TYR A 132 2.281 -7.487 25.502 1.00 81.59 C
ANISOU 781 CB TYR A 132 14641 7878 8483 -2261 865 -1720 C
ATOM 782 CG TYR A 132 2.476 -8.939 25.133 1.00 82.06 C
ANISOU 782 CG TYR A 132 15157 7519 8503 -2354 1074 -1970 C
ATOM 783 CD1 TYR A 132 3.708 -9.402 24.695 1.00 82.70 C
ANISOU 783 CD1 TYR A 132 15472 7374 8576 -2065 1342 -2092 C
ATOM 784 CD2 TYR A 132 1.420 -9.839 25.193 1.00 82.07 C
ANISOU 784 CD2 TYR A 132 15357 7345 8481 -2741 1020 -2092 C
ATOM 785 CE1 TYR A 132 3.886 -10.724 24.336 1.00 83.24 C
ANISOU 785 CE1 TYR A 132 15997 7021 8611 -2123 1562 -2333 C
ATOM 786 CE2 TYR A 132 1.590 -11.164 24.839 1.00 82.57 C
ANISOU 786 CE2 TYR A 132 15890 6976 8509 -2847 1228 -2338 C
ATOM 787 CZ TYR A 132 2.825 -11.600 24.413 1.00 83.11 C
ANISOU 787 CZ TYR A 132 16219 6793 8565 -2520 1502 -2459 C
ATOM 788 OH TYR A 132 3.004 -12.916 24.056 1.00 83.90 O
ANISOU 788 OH TYR A 132 16683 6527 8668 -2540 1709 -2633 O
ATOM 789 N PHE A 133 -0.011 -7.027 23.502 1.00 84.00 N
ANISOU 789 N PHE A 133 14909 8747 8262 -3068 397 -1939 N
ATOM 790 CA PHE A 133 -1.006 -7.490 22.543 1.00 84.83 C
ANISOU 790 CA PHE A 133 15162 8961 8108 -3513 229 -2149 C
ATOM 791 C PHE A 133 -0.963 -6.697 21.244 1.00 85.61 C
ANISOU 791 C PHE A 133 15248 9408 7872 -3548 93 -2190 C
ATOM 792 O PHE A 133 -1.414 -7.198 20.209 1.00 86.38 O
ANISOU 792 O PHE A 133 15587 9559 7674 -3869 5 -2427 O
ATOM 793 CB PHE A 133 -2.403 -7.421 23.162 1.00 88.86 C
ANISOU 793 CB PHE A 133 15383 9653 8725 -3812 -12 -2038 C
ATOM 794 CG PHE A 133 -2.655 -8.474 24.206 1.00 88.35 C
ANISOU 794 CG PHE A 133 15441 9220 8906 -3921 129 -2057 C
ATOM 795 CD1 PHE A 133 -1.846 -9.595 24.286 1.00 88.03 C
ANISOU 795 CD1 PHE A 133 15831 8697 8919 -3838 413 -2226 C
ATOM 796 CD2 PHE A 133 -3.699 -8.342 25.109 1.00 88.40 C
ANISOU 796 CD2 PHE A 133 15142 9355 9091 -4089 2 -1892 C
ATOM 797 CE1 PHE A 133 -2.073 -10.566 25.242 1.00 87.70 C
ANISOU 797 CE1 PHE A 133 15943 8287 9093 -3927 553 -2213 C
ATOM 798 CE2 PHE A 133 -3.930 -9.311 26.069 1.00 88.03 C
ANISOU 798 CE2 PHE A 133 15234 8961 9250 -4204 156 -1889 C
ATOM 799 CZ PHE A 133 -3.116 -10.424 26.134 1.00 87.65 C
ANISOU 799 CZ PHE A 133 15646 8413 9243 -4126 425 -2041 C
ATOM 800 N ALA A 134 -0.428 -5.476 21.273 1.00 84.69 N
ANISOU 800 N ALA A 134 14880 9519 7778 -3241 75 -1966 N
ATOM 801 CA ALA A 134 -0.264 -4.711 20.042 1.00 85.45 C
ANISOU 801 CA ALA A 134 15010 9910 7547 -3241 -11 -1972 C
ATOM 802 C ALA A 134 0.910 -5.237 19.222 1.00 85.66 C
ANISOU 802 C ALA A 134 15423 9727 7398 -3121 289 -2191 C
ATOM 803 O ALA A 134 0.788 -5.450 18.010 1.00 86.39 O
ANISOU 803 O ALA A 134 15781 9922 7123 -3318 258 -2385 O
ATOM 804 CB ALA A 134 -0.078 -3.230 20.366 1.00 81.29 C
ANISOU 804 CB ALA A 134 14120 9648 7120 -2969 -97 -1653 C
ATOM 805 N ILE A 135 2.057 -5.463 19.870 1.00 83.47 N
ANISOU 805 N ILE A 135 15178 9169 7370 -2789 584 -2166 N
ATOM 806 CA ILE A 135 3.269 -5.854 19.156 1.00 84.01 C
ANISOU 806 CA ILE A 135 15540 9064 7317 -2603 909 -2340 C
ATOM 807 C ILE A 135 3.236 -7.302 18.687 1.00 84.34 C
ANISOU 807 C ILE A 135 16048 8766 7232 -2785 1075 -2687 C
ATOM 808 O ILE A 135 4.108 -7.717 17.914 1.00 84.99 O
ANISOU 808 O ILE A 135 16431 8708 7153 -2666 1356 -2884 O
ATOM 809 CB ILE A 135 4.499 -5.591 20.053 1.00 85.39 C
ANISOU 809 CB ILE A 135 15526 9092 7827 -2173 1145 -2178 C
ATOM 810 CG1 ILE A 135 5.787 -5.560 19.228 1.00 86.31 C
ANISOU 810 CG1 ILE A 135 15798 9175 7820 -1944 1466 -2282 C
ATOM 811 CG2 ILE A 135 4.602 -6.643 21.142 1.00 84.87 C
ANISOU 811 CG2 ILE A 135 15538 8648 8062 -2081 1255 -2214 C
ATOM 812 CD1 ILE A 135 6.960 -4.978 19.968 1.00 86.51 C
ANISOU 812 CD1 ILE A 135 15528 9198 8144 -1560 1633 -2084 C
ATOM 813 N THR A 136 2.246 -8.083 19.118 1.00 84.36 N
ANISOU 813 N THR A 136 16130 8621 7301 -3082 930 -2777 N
ATOM 814 CA THR A 136 2.099 -9.458 18.659 1.00 84.87 C
ANISOU 814 CA THR A 136 16553 8382 7313 -3257 1060 -3039 C
ATOM 815 C THR A 136 1.041 -9.620 17.577 1.00 88.02 C
ANISOU 815 C THR A 136 16993 9042 7409 -3661 804 -3159 C
ATOM 816 O THR A 136 1.043 -10.641 16.879 1.00 92.37 O
ANISOU 816 O THR A 136 17827 9407 7860 -3778 919 -3373 O
ATOM 817 CB THR A 136 1.752 -10.385 19.831 1.00 83.91 C
ANISOU 817 CB THR A 136 16455 7904 7524 -3296 1106 -3008 C
ATOM 818 OG1 THR A 136 0.527 -9.953 20.437 1.00 82.83 O
ANISOU 818 OG1 THR A 136 16043 7985 7445 -3591 787 -2875 O
ATOM 819 CG2 THR A 136 2.862 -10.377 20.867 1.00 82.69 C
ANISOU 819 CG2 THR A 136 16291 7463 7664 -2860 1362 -2890 C
ATOM 820 N SER A 137 0.144 -8.653 17.426 1.00 87.58 N
ANISOU 820 N SER A 137 16660 9410 7206 -3863 456 -3024 N
ATOM 821 CA SER A 137 -0.857 -8.697 16.378 1.00 91.26 C
ANISOU 821 CA SER A 137 17115 10183 7376 -4213 175 -3109 C
ATOM 822 C SER A 137 -0.248 -8.268 15.047 1.00 93.24 C
ANISOU 822 C SER A 137 17536 10626 7266 -4111 240 -3175 C
ATOM 823 O SER A 137 0.770 -7.571 15.015 1.00 90.90 O
ANISOU 823 O SER A 137 17249 10343 6946 -3795 434 -3084 O
ATOM 824 CB SER A 137 -2.030 -7.789 16.738 1.00 92.47 C
ANISOU 824 CB SER A 137 16865 10744 7525 -4413 -227 -2901 C
ATOM 825 OG SER A 137 -1.640 -6.426 16.729 1.00 90.19 O
ANISOU 825 OG SER A 137 16397 10734 7139 -4184 -299 -2687 O
ATOM 826 N PRO A 138 -0.846 -8.680 13.925 1.00 97.06 N
ANISOU 826 N PRO A 138 18159 11263 7457 -4382 92 -3334 N
ATOM 827 CA PRO A 138 -0.378 -8.172 12.626 1.00 99.31 C
ANISOU 827 CA PRO A 138 18593 11779 7360 -4303 121 -3369 C
ATOM 828 C PRO A 138 -0.562 -6.675 12.472 1.00 96.59 C
ANISOU 828 C PRO A 138 17968 11873 6858 -4211 -115 -3085 C
ATOM 829 O PRO A 138 0.093 -6.070 11.613 1.00 97.36 O
ANISOU 829 O PRO A 138 18179 12121 6693 -4051 -11 -3043 O
ATOM 830 CB PRO A 138 -1.224 -8.956 11.616 1.00105.36 C
ANISOU 830 CB PRO A 138 19534 12635 7863 -4666 -63 -3591 C
ATOM 831 CG PRO A 138 -2.440 -9.340 12.368 1.00105.42 C
ANISOU 831 CG PRO A 138 19308 12668 8079 -4971 -334 -3566 C
ATOM 832 CD PRO A 138 -1.991 -9.594 13.777 1.00101.11 C
ANISOU 832 CD PRO A 138 18693 11764 7959 -4784 -112 -3485 C
ATOM 833 N PHE A 139 -1.441 -6.059 13.268 1.00 96.85 N
ANISOU 833 N PHE A 139 17644 12112 7043 -4301 -416 -2877 N
ATOM 834 CA PHE A 139 -1.471 -4.605 13.423 1.00 93.68 C
ANISOU 834 CA PHE A 139 16971 12043 6579 -4134 -584 -2567 C
ATOM 835 C PHE A 139 -0.382 -4.207 14.418 1.00 90.37 C
ANISOU 835 C PHE A 139 16534 11378 6422 -3809 -283 -2466 C
ATOM 836 O PHE A 139 -0.637 -3.848 15.569 1.00 89.73 O
ANISOU 836 O PHE A 139 16153 11269 6672 -3720 -354 -2283 O
ATOM 837 CB PHE A 139 -2.840 -4.127 13.887 1.00 94.74 C
ANISOU 837 CB PHE A 139 16716 12497 6784 -4333 -1012 -2385 C
ATOM 838 CG PHE A 139 -3.913 -4.249 12.849 1.00 99.59 C
ANISOU 838 CG PHE A 139 17272 13453 7114 -4611 -1355 -2428 C
ATOM 839 CD1 PHE A 139 -4.009 -3.321 11.826 1.00101.34 C
ANISOU 839 CD1 PHE A 139 17471 14044 6990 -4529 -1538 -2267 C
ATOM 840 CD2 PHE A 139 -4.840 -5.275 12.907 1.00102.76 C
ANISOU 840 CD2 PHE A 139 17639 13810 7595 -4951 -1495 -2614 C
ATOM 841 CE1 PHE A 139 -4.999 -3.423 10.869 1.00106.22 C
ANISOU 841 CE1 PHE A 139 18029 14995 7336 -4763 -1875 -2302 C
ATOM 842 CE2 PHE A 139 -5.833 -5.382 11.953 1.00107.69 C
ANISOU 842 CE2 PHE A 139 18190 14773 7956 -5214 -1826 -2664 C
ATOM 843 CZ PHE A 139 -5.913 -4.454 10.932 1.00109.47 C
ANISOU 843 CZ PHE A 139 18387 15379 7827 -5110 -2028 -2510 C
ATOM 844 N LYS A 140 0.861 -4.294 13.952 1.00 87.96 N
ANISOU 844 N LYS A 140 16477 10901 6042 -3578 79 -2553 N
ATOM 845 CA LYS A 140 1.994 -4.019 14.821 1.00 87.25 C
ANISOU 845 CA LYS A 140 16320 10581 6253 -3233 394 -2458 C
ATOM 846 C LYS A 140 2.002 -2.552 15.238 1.00 87.03 C
ANISOU 846 C LYS A 140 15877 10812 6377 -3015 260 -2065 C
ATOM 847 O LYS A 140 1.750 -1.656 14.428 1.00 87.56 O
ANISOU 847 O LYS A 140 15922 11197 6150 -3049 103 -1918 O
ATOM 848 CB LYS A 140 3.308 -4.382 14.128 1.00 84.10 C
ANISOU 848 CB LYS A 140 16237 9997 5720 -3039 817 -2634 C
ATOM 849 CG LYS A 140 4.520 -4.282 15.042 1.00 80.94 C
ANISOU 849 CG LYS A 140 15674 9356 5725 -2649 1146 -2528 C
ATOM 850 CD LYS A 140 5.826 -4.539 14.306 1.00 83.24 C
ANISOU 850 CD LYS A 140 16224 9526 5878 -2443 1580 -2686 C
ATOM 851 CE LYS A 140 6.055 -6.006 14.025 1.00 86.93 C
ANISOU 851 CE LYS A 140 17010 9650 6368 -2459 1796 -2996 C
ATOM 852 NZ LYS A 140 7.409 -6.211 13.443 1.00 89.11 N
ANISOU 852 NZ LYS A 140 17416 9817 6622 -2171 2239 -3090 N
ATOM 853 N TYR A 141 2.271 -2.326 16.525 1.00 81.33 N
ANISOU 853 N TYR A 141 14857 9940 6107 -2796 320 -1894 N
ATOM 854 CA TYR A 141 2.395 -1.027 17.183 1.00 81.02 C
ANISOU 854 CA TYR A 141 14442 10046 6295 -2569 248 -1554 C
ATOM 855 C TYR A 141 1.059 -0.322 17.380 1.00 81.15 C
ANISOU 855 C TYR A 141 14185 10345 6303 -2701 -142 -1350 C
ATOM 856 O TYR A 141 1.046 0.856 17.756 1.00 81.03 O
ANISOU 856 O TYR A 141 13905 10464 6419 -2523 -217 -1069 O
ATOM 857 CB TYR A 141 3.331 -0.067 16.437 1.00 79.42 C
ANISOU 857 CB TYR A 141 14278 9970 5928 -2393 421 -1427 C
ATOM 858 CG TYR A 141 4.703 -0.615 16.127 1.00 79.69 C
ANISOU 858 CG TYR A 141 14528 9790 5960 -2235 834 -1604 C
ATOM 859 CD1 TYR A 141 5.615 -0.893 17.137 1.00 79.41 C
ANISOU 859 CD1 TYR A 141 14346 9508 6317 -1992 1063 -1599 C
ATOM 860 CD2 TYR A 141 5.109 -0.786 14.812 1.00 80.43 C
ANISOU 860 CD2 TYR A 141 14953 9960 5647 -2308 999 -1758 C
ATOM 861 CE1 TYR A 141 6.879 -1.379 16.840 1.00 80.00 C
ANISOU 861 CE1 TYR A 141 14567 9420 6411 -1813 1443 -1744 C
ATOM 862 CE2 TYR A 141 6.366 -1.257 14.507 1.00 80.90 C
ANISOU 862 CE2 TYR A 141 15184 9843 5712 -2138 1412 -1916 C
ATOM 863 CZ TYR A 141 7.246 -1.557 15.521 1.00 80.75 C
ANISOU 863 CZ TYR A 141 14978 9584 6119 -1882 1633 -1905 C
ATOM 864 OH TYR A 141 8.496 -2.033 15.202 1.00 81.52 O
ANISOU 864 OH TYR A 141 15201 9533 6240 -1683 2048 -2052 O
ATOM 865 N GLN A 142 -0.065 -0.994 17.145 1.00 84.17 N
ANISOU 865 N GLN A 142 14614 10822 6546 -3007 -386 -1483 N
ATOM 866 CA GLN A 142 -1.378 -0.375 17.275 1.00 84.71 C
ANISOU 866 CA GLN A 142 14377 11202 6607 -3127 -760 -1291 C
ATOM 867 C GLN A 142 -2.208 -1.152 18.288 1.00 84.45 C
ANISOU 867 C GLN A 142 14177 11057 6853 -3294 -853 -1359 C
ATOM 868 O GLN A 142 -2.320 -2.379 18.195 1.00 84.33 O
ANISOU 868 O GLN A 142 14400 10850 6793 -3537 -791 -1635 O
ATOM 869 CB GLN A 142 -2.096 -0.310 15.925 1.00 89.01 C
ANISOU 869 CB GLN A 142 15063 12080 6676 -3379 -1029 -1349 C
ATOM 870 CG GLN A 142 -3.394 0.478 15.959 1.00 89.88 C
ANISOU 870 CG GLN A 142 14810 12571 6771 -3437 -1430 -1101 C
ATOM 871 CD GLN A 142 -4.030 0.613 14.590 1.00 91.12 C
ANISOU 871 CD GLN A 142 15098 13100 6425 -3653 -1728 -1124 C
ATOM 872 OE1 GLN A 142 -3.521 0.082 13.603 1.00 91.30 O
ANISOU 872 OE1 GLN A 142 15521 13087 6082 -3790 -1626 -1353 O
ATOM 873 NE2 GLN A 142 -5.147 1.329 14.524 1.00 92.14 N
ANISOU 873 NE2 GLN A 142 14891 13599 6521 -3668 -2097 -885 N
ATOM 874 N SER A 143 -2.786 -0.433 19.249 1.00 84.87 N
ANISOU 874 N SER A 143 13846 11213 7189 -3169 -976 -1110 N
ATOM 875 CA SER A 143 -3.521 -1.069 20.333 1.00 84.67 C
ANISOU 875 CA SER A 143 13638 11082 7450 -3298 -1015 -1134 C
ATOM 876 C SER A 143 -4.766 -1.776 19.815 1.00 85.64 C
ANISOU 876 C SER A 143 13739 11402 7398 -3718 -1282 -1281 C
ATOM 877 O SER A 143 -5.506 -1.244 18.983 1.00 86.77 O
ANISOU 877 O SER A 143 13758 11919 7293 -3830 -1571 -1206 O
ATOM 878 CB SER A 143 -3.917 -0.036 21.385 1.00 83.74 C
ANISOU 878 CB SER A 143 13118 11072 7625 -3064 -1080 -836 C
ATOM 879 OG SER A 143 -4.678 -0.635 22.420 1.00 83.72 O
ANISOU 879 OG SER A 143 12938 10997 7874 -3198 -1098 -848 O
ATOM 880 N LEU A 144 -4.997 -2.989 20.323 1.00 87.52 N
ANISOU 880 N LEU A 144 14097 11387 7767 -3959 -1190 -1484 N
ATOM 881 CA LEU A 144 -6.189 -3.741 19.956 1.00 88.45 C
ANISOU 881 CA LEU A 144 14178 11664 7766 -4419 -1428 -1645 C
ATOM 882 C LEU A 144 -7.452 -3.145 20.559 1.00 89.46 C
ANISOU 882 C LEU A 144 13786 12131 8075 -4477 -1681 -1413 C
ATOM 883 O LEU A 144 -8.546 -3.377 20.034 1.00 90.69 O
ANISOU 883 O LEU A 144 13781 12592 8083 -4829 -1972 -1476 O
ATOM 884 CB LEU A 144 -6.045 -5.197 20.396 1.00 90.50 C
ANISOU 884 CB LEU A 144 14742 11497 8145 -4664 -1215 -1912 C
ATOM 885 CG LEU A 144 -4.925 -5.998 19.732 1.00 89.91 C
ANISOU 885 CG LEU A 144 15209 11065 7888 -4641 -952 -2191 C
ATOM 886 CD1 LEU A 144 -4.817 -7.377 20.362 1.00 89.31 C
ANISOU 886 CD1 LEU A 144 15421 10515 8000 -4819 -721 -2400 C
ATOM 887 CD2 LEU A 144 -5.151 -6.103 18.232 1.00 90.97 C
ANISOU 887 CD2 LEU A 144 15561 11431 7572 -4891 -1131 -2390 C
ATOM 888 N LEU A 145 -7.324 -2.388 21.644 1.00 87.50 N
ANISOU 888 N LEU A 145 13264 11847 8135 -4144 -1575 -1157 N
ATOM 889 CA LEU A 145 -8.475 -1.787 22.299 1.00 88.67 C
ANISOU 889 CA LEU A 145 12918 12294 8479 -4141 -1755 -934 C
ATOM 890 C LEU A 145 -8.956 -0.574 21.514 1.00 89.99 C
ANISOU 890 C LEU A 145 12828 12902 8464 -3992 -2041 -723 C
ATOM 891 O LEU A 145 -8.152 0.206 20.996 1.00 89.63 O
ANISOU 891 O LEU A 145 12934 12847 8274 -3713 -1998 -630 O
ATOM 892 CB LEU A 145 -8.112 -1.367 23.725 1.00 87.00 C
ANISOU 892 CB LEU A 145 12562 11872 8623 -3816 -1518 -752 C
ATOM 893 CG LEU A 145 -7.670 -2.445 24.719 1.00 85.63 C
ANISOU 893 CG LEU A 145 12603 11272 8659 -3888 -1237 -879 C
ATOM 894 CD1 LEU A 145 -7.211 -1.813 26.029 1.00 84.98 C
ANISOU 894 CD1 LEU A 145 12390 11045 8853 -3519 -1043 -676 C
ATOM 895 CD2 LEU A 145 -8.777 -3.452 24.969 1.00 86.27 C
ANISOU 895 CD2 LEU A 145 12585 11382 8811 -4330 -1303 -994 C
ATOM 896 N THR A 146 -10.273 -0.418 21.423 1.00 88.61 N
ANISOU 896 N THR A 146 12254 13116 8298 -4176 -2328 -632 N
ATOM 897 CA THR A 146 -10.807 0.832 20.911 1.00 89.95 C
ANISOU 897 CA THR A 146 12116 13696 8366 -3945 -2591 -360 C
ATOM 898 C THR A 146 -10.829 1.879 22.022 1.00 90.30 C
ANISOU 898 C THR A 146 11867 13700 8745 -3523 -2448 -75 C
ATOM 899 O THR A 146 -10.618 1.583 23.201 1.00 89.75 O
ANISOU 899 O THR A 146 11778 13358 8967 -3466 -2193 -94 O
ATOM 900 CB THR A 146 -12.203 0.636 20.321 1.00 92.67 C
ANISOU 900 CB THR A 146 12106 14521 8582 -4274 -2982 -358 C
ATOM 901 OG1 THR A 146 -12.659 1.873 19.757 1.00 93.93 O
ANISOU 901 OG1 THR A 146 11992 15075 8622 -3990 -3246 -64 O
ATOM 902 CG2 THR A 146 -13.183 0.181 21.381 1.00 93.35 C
ANISOU 902 CG2 THR A 146 11792 14666 9010 -4458 -2953 -345 C
ATOM 903 N LYS A 147 -11.084 3.128 21.629 1.00 89.74 N
ANISOU 903 N LYS A 147 11595 13891 8610 -3218 -2612 194 N
ATOM 904 CA LYS A 147 -11.030 4.223 22.592 1.00 90.16 C
ANISOU 904 CA LYS A 147 11437 13868 8951 -2795 -2461 449 C
ATOM 905 C LYS A 147 -12.153 4.115 23.616 1.00 91.52 C
ANISOU 905 C LYS A 147 11156 14190 9430 -2835 -2464 524 C
ATOM 906 O LYS A 147 -11.925 4.307 24.816 1.00 91.46 O
ANISOU 906 O LYS A 147 11103 13947 9700 -2649 -2202 570 O
ATOM 907 CB LYS A 147 -11.085 5.561 21.860 1.00 91.74 C
ANISOU 907 CB LYS A 147 11570 14282 9005 -2465 -2629 725 C
ATOM 908 CG LYS A 147 -9.880 5.809 20.968 1.00 90.40 C
ANISOU 908 CG LYS A 147 11855 13936 8556 -2389 -2552 687 C
ATOM 909 CD LYS A 147 -9.985 7.137 20.244 1.00 91.11 C
ANISOU 909 CD LYS A 147 11904 14219 8493 -2075 -2708 992 C
ATOM 910 CE LYS A 147 -8.763 7.376 19.379 1.00 89.84 C
ANISOU 910 CE LYS A 147 12200 13879 8055 -2027 -2586 962 C
ATOM 911 NZ LYS A 147 -8.678 6.396 18.260 1.00 89.70 N
ANISOU 911 NZ LYS A 147 12436 13994 7651 -2384 -2726 728 N
ATOM 912 N ASN A 148 -13.370 3.801 23.165 1.00 91.75 N
ANISOU 912 N ASN A 148 10835 14626 9399 -3090 -2755 533 N
ATOM 913 CA ASN A 148 -14.479 3.631 24.098 1.00 93.05 C
ANISOU 913 CA ASN A 148 10527 14968 9860 -3167 -2736 598 C
ATOM 914 C ASN A 148 -14.218 2.488 25.070 1.00 92.05 C
ANISOU 914 C ASN A 148 10562 14500 9912 -3439 -2450 382 C
ATOM 915 O ASN A 148 -14.609 2.565 26.240 1.00 92.65 O
ANISOU 915 O ASN A 148 10405 14521 10275 -3344 -2250 464 O
ATOM 916 CB ASN A 148 -15.777 3.393 23.327 1.00 94.17 C
ANISOU 916 CB ASN A 148 10250 15642 9889 -3455 -3126 622 C
ATOM 917 CG ASN A 148 -16.217 4.613 22.541 1.00 95.36 C
ANISOU 917 CG ASN A 148 10155 16172 9905 -3112 -3419 910 C
ATOM 918 OD1 ASN A 148 -16.128 5.743 23.023 1.00 95.84 O
ANISOU 918 OD1 ASN A 148 10106 16177 10132 -2633 -3298 1159 O
ATOM 919 ND2 ASN A 148 -16.696 4.390 21.323 1.00 95.90 N
ANISOU 919 ND2 ASN A 148 10161 16618 9657 -3357 -3809 878 N
ATOM 920 N LYS A 149 -13.550 1.430 24.607 1.00 92.68 N
ANISOU 920 N LYS A 149 11066 14333 9815 -3757 -2408 114 N
ATOM 921 CA LYS A 149 -13.209 0.309 25.476 1.00 91.46 C
ANISOU 921 CA LYS A 149 11135 13800 9814 -3987 -2128 -74 C
ATOM 922 C LYS A 149 -12.035 0.651 26.384 1.00 90.15 C
ANISOU 922 C LYS A 149 11251 13215 9786 -3618 -1799 -25 C
ATOM 923 O LYS A 149 -11.997 0.219 27.541 1.00 89.68 O
ANISOU 923 O LYS A 149 11201 12928 9944 -3627 -1555 -31 O
ATOM 924 CB LYS A 149 -12.887 -0.921 24.630 1.00 91.16 C
ANISOU 924 CB LYS A 149 11484 13612 9542 -4420 -2186 -380 C
ATOM 925 CG LYS A 149 -12.732 -2.222 25.389 1.00 90.03 C
ANISOU 925 CG LYS A 149 11576 13088 9546 -4722 -1932 -575 C
ATOM 926 CD LYS A 149 -12.309 -3.323 24.427 1.00 89.14 C
ANISOU 926 CD LYS A 149 11912 12782 9175 -5092 -1975 -889 C
ATOM 927 CE LYS A 149 -13.437 -3.689 23.474 1.00 90.63 C
ANISOU 927 CE LYS A 149 11880 13377 9178 -5560 -2329 -1006 C
ATOM 928 NZ LYS A 149 -13.067 -4.810 22.565 1.00 90.35 N
ANISOU 928 NZ LYS A 149 12329 13127 8875 -5960 -2354 -1353 N
ATOM 929 N ALA A 150 -11.066 1.416 25.875 1.00 87.58 N
ANISOU 929 N ALA A 150 11156 12796 9323 -3312 -1791 29 N
ATOM 930 CA ALA A 150 -9.968 1.866 26.723 1.00 86.52 C
ANISOU 930 CA ALA A 150 11229 12321 9323 -2969 -1515 85 C
ATOM 931 C ALA A 150 -10.464 2.791 27.826 1.00 87.98 C
ANISOU 931 C ALA A 150 11090 12582 9758 -2678 -1424 303 C
ATOM 932 O ALA A 150 -9.912 2.786 28.932 1.00 87.32 O
ANISOU 932 O ALA A 150 11114 12229 9836 -2524 -1179 311 O
ATOM 933 CB ALA A 150 -8.898 2.562 25.883 1.00 85.84 C
ANISOU 933 CB ALA A 150 11409 12160 9045 -2740 -1528 106 C
ATOM 934 N ARG A 151 -11.500 3.589 27.550 1.00 87.52 N
ANISOU 934 N ARG A 151 10641 12893 9722 -2583 -1616 481 N
ATOM 935 CA ARG A 151 -12.105 4.397 28.604 1.00 89.19 C
ANISOU 935 CA ARG A 151 10531 13181 10177 -2311 -1501 669 C
ATOM 936 C ARG A 151 -12.747 3.510 29.663 1.00 89.32 C
ANISOU 936 C ARG A 151 10391 13164 10382 -2541 -1337 604 C
ATOM 937 O ARG A 151 -12.719 3.833 30.857 1.00 89.78 O
ANISOU 937 O ARG A 151 10402 13088 10621 -2341 -1103 677 O
ATOM 938 CB ARG A 151 -13.141 5.358 28.015 1.00 90.82 C
ANISOU 938 CB ARG A 151 10328 13803 10376 -2144 -1743 882 C
ATOM 939 CG ARG A 151 -12.579 6.421 27.078 1.00 90.55 C
ANISOU 939 CG ARG A 151 10449 13788 10167 -1858 -1876 1013 C
ATOM 940 CD ARG A 151 -13.680 7.368 26.612 1.00 92.23 C
ANISOU 940 CD ARG A 151 10244 14403 10396 -1641 -2109 1265 C
ATOM 941 NE ARG A 151 -13.204 8.360 25.650 1.00 91.74 N
ANISOU 941 NE ARG A 151 10358 14356 10142 -1380 -2244 1421 N
ATOM 942 CZ ARG A 151 -13.292 8.223 24.329 1.00 91.40 C
ANISOU 942 CZ ARG A 151 10378 14548 9802 -1526 -2536 1431 C
ATOM 943 NH1 ARG A 151 -13.852 7.140 23.806 1.00 91.54 N
ANISOU 943 NH1 ARG A 151 10289 14807 9684 -1946 -2740 1267 N
ATOM 944 NH2 ARG A 151 -12.832 9.175 23.528 1.00 90.98 N
ANISOU 944 NH2 ARG A 151 10515 14482 9571 -1270 -2619 1603 N
ATOM 945 N VAL A 152 -13.332 2.386 29.242 1.00 88.48 N
ANISOU 945 N VAL A 152 10228 13172 10221 -2981 -1449 463 N
ATOM 946 CA VAL A 152 -13.898 1.434 30.193 1.00 88.33 C
ANISOU 946 CA VAL A 152 10109 13081 10370 -3259 -1269 399 C
ATOM 947 C VAL A 152 -12.803 0.826 31.059 1.00 86.22 C
ANISOU 947 C VAL A 152 10286 12335 10137 -3223 -979 300 C
ATOM 948 O VAL A 152 -13.026 0.530 32.240 1.00 86.10 O
ANISOU 948 O VAL A 152 10230 12200 10284 -3231 -745 340 O
ATOM 949 CB VAL A 152 -14.701 0.354 29.442 1.00 87.00 C
ANISOU 949 CB VAL A 152 9825 13110 10121 -3790 -1465 248 C
ATOM 950 CG1 VAL A 152 -15.194 -0.722 30.398 1.00 86.71 C
ANISOU 950 CG1 VAL A 152 9754 12935 10256 -4129 -1245 176 C
ATOM 951 CG2 VAL A 152 -15.872 0.986 28.707 1.00 89.05 C
ANISOU 951 CG2 VAL A 152 9564 13911 10361 -3809 -1779 377 C
ATOM 952 N ILE A 153 -11.603 0.645 30.504 1.00 86.94 N
ANISOU 952 N ILE A 153 10798 12163 10072 -3163 -983 184 N
ATOM 953 CA ILE A 153 -10.502 0.106 31.293 1.00 84.69 C
ANISOU 953 CA ILE A 153 10903 11450 9823 -3078 -733 111 C
ATOM 954 C ILE A 153 -10.032 1.126 32.323 1.00 84.85 C
ANISOU 954 C ILE A 153 10894 11389 9957 -2662 -575 263 C
ATOM 955 O ILE A 153 -9.731 0.774 33.470 1.00 83.65 O
ANISOU 955 O ILE A 153 10869 11014 9899 -2608 -359 276 O
ATOM 956 CB ILE A 153 -9.352 -0.343 30.371 1.00 84.57 C
ANISOU 956 CB ILE A 153 11299 11211 9624 -3105 -768 -54 C
ATOM 957 CG1 ILE A 153 -9.844 -1.395 29.374 1.00 84.61 C
ANISOU 957 CG1 ILE A 153 11385 11273 9491 -3544 -911 -243 C
ATOM 958 CG2 ILE A 153 -8.189 -0.885 31.190 1.00 82.12 C
ANISOU 958 CG2 ILE A 153 11346 10486 9369 -2970 -525 -106 C
ATOM 959 CD1 ILE A 153 -10.362 -2.664 30.019 1.00 84.17 C
ANISOU 959 CD1 ILE A 153 11395 11041 9546 -3899 -775 -337 C
ATOM 960 N ILE A 154 -9.980 2.407 31.942 1.00 83.10 N
ANISOU 960 N ILE A 154 10527 11335 9711 -2371 -680 381 N
ATOM 961 CA ILE A 154 -9.485 3.439 32.853 1.00 83.54 C
ANISOU 961 CA ILE A 154 10599 11284 9859 -1998 -534 495 C
ATOM 962 C ILE A 154 -10.358 3.524 34.099 1.00 84.66 C
ANISOU 962 C ILE A 154 10505 11497 10166 -1959 -368 587 C
ATOM 963 O ILE A 154 -9.850 3.626 35.223 1.00 83.54 O
ANISOU 963 O ILE A 154 10514 11151 10077 -1805 -170 599 O
ATOM 964 CB ILE A 154 -9.399 4.799 32.136 1.00 83.57 C
ANISOU 964 CB ILE A 154 10502 11435 9814 -1723 -670 613 C
ATOM 965 CG1 ILE A 154 -8.426 4.725 30.959 1.00 82.08 C
ANISOU 965 CG1 ILE A 154 10586 11162 9441 -1759 -784 528 C
ATOM 966 CG2 ILE A 154 -8.964 5.884 33.109 1.00 84.58 C
ANISOU 966 CG2 ILE A 154 10663 11428 10047 -1374 -509 706 C
ATOM 967 CD1 ILE A 154 -7.010 4.401 31.369 1.00 79.51 C
ANISOU 967 CD1 ILE A 154 10610 10499 9101 -1693 -622 422 C
ATOM 968 N LEU A 155 -11.680 3.484 33.924 1.00 84.72 N
ANISOU 968 N LEU A 155 10130 11815 10245 -2100 -445 653 N
ATOM 969 CA LEU A 155 -12.574 3.571 35.074 1.00 85.92 C
ANISOU 969 CA LEU A 155 10022 12066 10558 -2064 -251 745 C
ATOM 970 C LEU A 155 -12.379 2.385 36.010 1.00 83.95 C
ANISOU 970 C LEU A 155 9990 11576 10329 -2298 -37 666 C
ATOM 971 O LEU A 155 -12.255 2.557 37.228 1.00 83.72 O
ANISOU 971 O LEU A 155 10035 11422 10354 -2142 196 717 O
ATOM 972 CB LEU A 155 -14.027 3.665 34.609 1.00 84.74 C
ANISOU 972 CB LEU A 155 9366 12336 10494 -2198 -384 831 C
ATOM 973 CG LEU A 155 -14.390 4.942 33.849 1.00 86.70 C
ANISOU 973 CG LEU A 155 9353 12847 10740 -1892 -578 971 C
ATOM 974 CD1 LEU A 155 -15.827 4.884 33.354 1.00 88.21 C
ANISOU 974 CD1 LEU A 155 9006 13496 11014 -2045 -748 1060 C
ATOM 975 CD2 LEU A 155 -14.161 6.174 34.715 1.00 87.88 C
ANISOU 975 CD2 LEU A 155 9523 12887 10982 -1435 -384 1084 C
ATOM 976 N MET A 156 -12.333 1.170 35.456 1.00 84.86 N
ANISOU 976 N MET A 156 10251 11606 10386 -2670 -106 542 N
ATOM 977 CA MET A 156 -12.138 -0.013 36.290 1.00 83.14 C
ANISOU 977 CA MET A 156 10287 11114 10189 -2892 103 487 C
ATOM 978 C MET A 156 -10.825 0.057 37.059 1.00 80.84 C
ANISOU 978 C MET A 156 10399 10476 9841 -2621 245 482 C
ATOM 979 O MET A 156 -10.754 -0.378 38.213 1.00 80.13 O
ANISOU 979 O MET A 156 10447 10219 9778 -2616 464 530 O
ATOM 980 CB MET A 156 -12.183 -1.282 35.442 1.00 87.98 C
ANISOU 980 CB MET A 156 11060 11628 10740 -3318 2 331 C
ATOM 981 CG MET A 156 -13.543 -1.611 34.869 1.00 89.92 C
ANISOU 981 CG MET A 156 10912 12212 11043 -3692 -129 316 C
ATOM 982 SD MET A 156 -13.487 -3.138 33.913 1.00 88.72 S
ANISOU 982 SD MET A 156 11046 11874 10789 -4231 -233 83 S
ATOM 983 CE MET A 156 -13.285 -4.339 35.228 1.00 87.43 C
ANISOU 983 CE MET A 156 11218 11279 10720 -4404 125 91 C
ATOM 984 N VAL A 157 -9.773 0.592 36.436 1.00 81.01 N
ANISOU 984 N VAL A 157 10604 10405 9773 -2403 122 433 N
ATOM 985 CA VAL A 157 -8.505 0.748 37.144 1.00 78.66 C
ANISOU 985 CA VAL A 157 10623 9832 9432 -2145 226 431 C
ATOM 986 C VAL A 157 -8.686 1.656 38.354 1.00 79.57 C
ANISOU 986 C VAL A 157 10636 10001 9597 -1885 370 545 C
ATOM 987 O VAL A 157 -8.257 1.331 39.465 1.00 78.21 O
ANISOU 987 O VAL A 157 10665 9649 9401 -1815 530 572 O
ATOM 988 CB VAL A 157 -7.412 1.275 36.197 1.00 78.94 C
ANISOU 988 CB VAL A 157 10803 9809 9380 -1978 78 364 C
ATOM 989 CG1 VAL A 157 -6.153 1.603 36.980 1.00 76.51 C
ANISOU 989 CG1 VAL A 157 10733 9286 9053 -1708 167 373 C
ATOM 990 CG2 VAL A 157 -7.102 0.244 35.126 1.00 77.90 C
ANISOU 990 CG2 VAL A 157 10856 9573 9169 -2222 -9 225 C
ATOM 991 N TRP A 158 -9.347 2.800 38.160 1.00 77.59 N
ANISOU 991 N TRP A 158 10087 9994 9398 -1727 319 617 N
ATOM 992 CA TRP A 158 -9.597 3.704 39.279 1.00 78.91 C
ANISOU 992 CA TRP A 158 10173 10200 9608 -1474 482 701 C
ATOM 993 C TRP A 158 -10.637 3.141 40.242 1.00 80.14 C
ANISOU 993 C TRP A 158 10181 10442 9826 -1619 694 764 C
ATOM 994 O TRP A 158 -10.566 3.408 41.447 1.00 80.26 O
ANISOU 994 O TRP A 158 10294 10386 9816 -1469 893 803 O
ATOM 995 CB TRP A 158 -10.026 5.074 38.757 1.00 78.88 C
ANISOU 995 CB TRP A 158 9917 10395 9659 -1236 392 766 C
ATOM 996 CG TRP A 158 -8.904 5.849 38.126 1.00 77.84 C
ANISOU 996 CG TRP A 158 9979 10137 9461 -1049 259 729 C
ATOM 997 CD1 TRP A 158 -8.550 5.852 36.809 1.00 77.74 C
ANISOU 997 CD1 TRP A 158 9986 10159 9392 -1115 57 701 C
ATOM 998 CD2 TRP A 158 -8.008 6.755 38.783 1.00 76.75 C
ANISOU 998 CD2 TRP A 158 10041 9825 9294 -793 332 713 C
ATOM 999 NE1 TRP A 158 -7.481 6.690 36.606 1.00 76.44 N
ANISOU 999 NE1 TRP A 158 10011 9850 9182 -916 23 684 N
ATOM 1000 CE2 TRP A 158 -7.130 7.258 37.802 1.00 75.57 C
ANISOU 1000 CE2 TRP A 158 10005 9609 9099 -729 179 685 C
ATOM 1001 CE3 TRP A 158 -7.859 7.185 40.106 1.00 76.62 C
ANISOU 1001 CE3 TRP A 158 10133 9709 9270 -633 514 710 C
ATOM 1002 CZ2 TRP A 158 -6.118 8.169 38.101 1.00 73.81 C
ANISOU 1002 CZ2 TRP A 158 9971 9220 8852 -538 201 656 C
ATOM 1003 CZ3 TRP A 158 -6.854 8.089 40.401 1.00 75.04 C
ANISOU 1003 CZ3 TRP A 158 10138 9348 9026 -442 510 663 C
ATOM 1004 CH2 TRP A 158 -5.997 8.571 39.403 1.00 73.66 C
ANISOU 1004 CH2 TRP A 158 10045 9107 8836 -407 355 637 C
ATOM 1005 N ILE A 159 -11.608 2.374 39.738 1.00 80.83 N
ANISOU 1005 N ILE A 159 10038 10692 9982 -1931 661 770 N
ATOM 1006 CA ILE A 159 -12.569 1.711 40.619 1.00 81.79 C
ANISOU 1006 CA ILE A 159 10021 10885 10172 -2133 888 832 C
ATOM 1007 C ILE A 159 -11.860 0.693 41.505 1.00 79.47 C
ANISOU 1007 C ILE A 159 10142 10266 9788 -2237 1052 817 C
ATOM 1008 O ILE A 159 -11.974 0.727 42.736 1.00 79.77 O
ANISOU 1008 O ILE A 159 10263 10252 9793 -2146 1290 890 O
ATOM 1009 CB ILE A 159 -13.696 1.054 39.803 1.00 79.19 C
ANISOU 1009 CB ILE A 159 9349 10799 9939 -2506 789 823 C
ATOM 1010 CG1 ILE A 159 -14.592 2.114 39.159 1.00 81.72 C
ANISOU 1010 CG1 ILE A 159 9189 11504 10357 -2354 650 893 C
ATOM 1011 CG2 ILE A 159 -14.513 0.115 40.679 1.00 79.69 C
ANISOU 1011 CG2 ILE A 159 9340 10868 10071 -2806 1045 873 C
ATOM 1012 CD1 ILE A 159 -15.554 1.553 38.132 1.00 82.65 C
ANISOU 1012 CD1 ILE A 159 8958 11909 10537 -2717 451 870 C
ATOM 1013 N VAL A 160 -11.123 -0.235 40.887 1.00 82.04 N
ANISOU 1013 N VAL A 160 10748 10365 10057 -2411 936 728 N
ATOM 1014 CA VAL A 160 -10.403 -1.246 41.659 1.00 79.81 C
ANISOU 1014 CA VAL A 160 10877 9751 9697 -2470 1077 737 C
ATOM 1015 C VAL A 160 -9.376 -0.591 42.574 1.00 78.41 C
ANISOU 1015 C VAL A 160 10938 9444 9411 -2102 1126 774 C
ATOM 1016 O VAL A 160 -9.209 -0.993 43.732 1.00 77.76 O
ANISOU 1016 O VAL A 160 11072 9223 9252 -2065 1309 854 O
ATOM 1017 CB VAL A 160 -9.751 -2.280 40.721 1.00 78.35 C
ANISOU 1017 CB VAL A 160 10953 9331 9484 -2667 947 621 C
ATOM 1018 CG1 VAL A 160 -8.859 -3.225 41.510 1.00 76.30 C
ANISOU 1018 CG1 VAL A 160 11138 8703 9151 -2630 1081 655 C
ATOM 1019 CG2 VAL A 160 -10.821 -3.067 39.983 1.00 79.69 C
ANISOU 1019 CG2 VAL A 160 10936 9607 9737 -3104 916 565 C
ATOM 1020 N SER A 161 -8.676 0.430 42.074 1.00 79.44 N
ANISOU 1020 N SER A 161 11041 9623 9520 -1843 959 720 N
ATOM 1021 CA SER A 161 -7.755 1.173 42.927 1.00 78.20 C
ANISOU 1021 CA SER A 161 11069 9378 9265 -1531 986 733 C
ATOM 1022 C SER A 161 -8.501 1.877 44.053 1.00 80.14 C
ANISOU 1022 C SER A 161 11195 9762 9493 -1410 1184 809 C
ATOM 1023 O SER A 161 -8.066 1.846 45.209 1.00 79.08 O
ANISOU 1023 O SER A 161 11292 9523 9233 -1293 1305 847 O
ATOM 1024 CB SER A 161 -6.961 2.181 42.100 1.00 77.57 C
ANISOU 1024 CB SER A 161 10956 9328 9188 -1331 788 658 C
ATOM 1025 OG SER A 161 -6.146 1.534 41.143 1.00 75.56 O
ANISOU 1025 OG SER A 161 10847 8939 8923 -1414 645 582 O
ATOM 1026 N GLY A 162 -9.631 2.512 43.733 1.00 80.21 N
ANISOU 1026 N GLY A 162 10842 10020 9615 -1422 1221 834 N
ATOM 1027 CA GLY A 162 -10.399 3.211 44.747 1.00 82.17 C
ANISOU 1027 CA GLY A 162 10955 10405 9861 -1279 1448 896 C
ATOM 1028 C GLY A 162 -10.957 2.299 45.819 1.00 82.10 C
ANISOU 1028 C GLY A 162 11030 10367 9798 -1453 1712 979 C
ATOM 1029 O GLY A 162 -11.202 2.741 46.944 1.00 82.52 O
ANISOU 1029 O GLY A 162 11137 10454 9764 -1306 1934 1019 O
ATOM 1030 N LEU A 163 -11.166 1.022 45.491 1.00 83.36 N
ANISOU 1030 N LEU A 163 11232 10447 9996 -1776 1711 1004 N
ATOM 1031 CA LEU A 163 -11.649 0.077 46.489 1.00 83.30 C
ANISOU 1031 CA LEU A 163 11351 10367 9934 -1972 1980 1105 C
ATOM 1032 C LEU A 163 -10.506 -0.470 47.334 1.00 80.65 C
ANISOU 1032 C LEU A 163 11509 9737 9398 -1873 2005 1139 C
ATOM 1033 O LEU A 163 -10.633 -0.576 48.558 1.00 80.71 O
ANISOU 1033 O LEU A 163 11688 9715 9263 -1822 2235 1233 O
ATOM 1034 CB LEU A 163 -12.415 -1.058 45.809 1.00 79.67 C
ANISOU 1034 CB LEU A 163 10742 9920 9608 -2395 1987 1116 C
ATOM 1035 CG LEU A 163 -13.726 -0.667 45.127 1.00 82.63 C
ANISOU 1035 CG LEU A 163 10572 10648 10174 -2544 1974 1112 C
ATOM 1036 CD1 LEU A 163 -14.324 -1.864 44.409 1.00 82.69 C
ANISOU 1036 CD1 LEU A 163 10483 10646 10290 -3017 1933 1088 C
ATOM 1037 CD2 LEU A 163 -14.712 -0.087 46.132 1.00 84.98 C
ANISOU 1037 CD2 LEU A 163 10609 11179 10502 -2445 2279 1212 C
ATOM 1038 N THR A 164 -9.381 -0.810 46.705 1.00 83.45 N
ANISOU 1038 N THR A 164 12089 9891 9727 -1826 1774 1073 N
ATOM 1039 CA THR A 164 -8.234 -1.307 47.454 1.00 81.32 C
ANISOU 1039 CA THR A 164 12245 9371 9282 -1688 1760 1121 C
ATOM 1040 C THR A 164 -7.513 -0.212 48.227 1.00 80.79 C
ANISOU 1040 C THR A 164 12278 9361 9059 -1356 1715 1096 C
ATOM 1041 O THR A 164 -6.662 -0.531 49.065 1.00 79.61 O
ANISOU 1041 O THR A 164 12453 9068 8729 -1229 1706 1154 O
ATOM 1042 CB THR A 164 -7.247 -1.999 46.514 1.00 78.10 C
ANISOU 1042 CB THR A 164 12010 8747 8918 -1714 1546 1054 C
ATOM 1043 OG1 THR A 164 -6.759 -1.056 45.552 1.00 77.66 O
ANISOU 1043 OG1 THR A 164 11778 8803 8928 -1568 1322 926 O
ATOM 1044 CG2 THR A 164 -7.919 -3.157 45.793 1.00 78.59 C
ANISOU 1044 CG2 THR A 164 12049 8706 9107 -2074 1598 1050 C
ATOM 1045 N SER A 165 -7.822 1.059 47.971 1.00 83.06 N
ANISOU 1045 N SER A 165 12310 9845 9404 -1214 1678 1013 N
ATOM 1046 CA SER A 165 -7.162 2.170 48.646 1.00 82.72 C
ANISOU 1046 CA SER A 165 12377 9830 9221 -936 1638 954 C
ATOM 1047 C SER A 165 -8.031 2.811 49.722 1.00 84.49 C
ANISOU 1047 C SER A 165 12556 10196 9352 -854 1906 983 C
ATOM 1048 O SER A 165 -7.566 3.013 50.847 1.00 84.02 O
ANISOU 1048 O SER A 165 12767 10094 9064 -724 1975 990 O
ATOM 1049 CB SER A 165 -6.733 3.232 47.626 1.00 82.18 C
ANISOU 1049 CB SER A 165 12135 9819 9271 -805 1424 832 C
ATOM 1050 OG SER A 165 -5.773 2.710 46.723 1.00 80.27 O
ANISOU 1050 OG SER A 165 11972 9449 9077 -848 1202 793 O
ATOM 1051 N PHE A 166 -9.285 3.141 49.405 1.00 85.55 N
ANISOU 1051 N PHE A 166 12345 10513 9646 -919 2059 999 N
ATOM 1052 CA PHE A 166 -10.120 3.815 50.395 1.00 87.23 C
ANISOU 1052 CA PHE A 166 12492 10867 9786 -803 2352 1016 C
ATOM 1053 C PHE A 166 -10.644 2.851 51.453 1.00 87.38 C
ANISOU 1053 C PHE A 166 12662 10873 9663 -964 2639 1147 C
ATOM 1054 O PHE A 166 -10.643 3.183 52.643 1.00 87.48 O
ANISOU 1054 O PHE A 166 12888 10897 9452 -835 2840 1157 O
ATOM 1055 CB PHE A 166 -11.294 4.538 49.729 1.00 86.16 C
ANISOU 1055 CB PHE A 166 11894 10956 9885 -769 2433 1007 C
ATOM 1056 CG PHE A 166 -10.905 5.782 48.980 1.00 86.55 C
ANISOU 1056 CG PHE A 166 11843 11015 10026 -534 2234 903 C
ATOM 1057 CD1 PHE A 166 -9.593 6.217 48.958 1.00 84.69 C
ANISOU 1057 CD1 PHE A 166 11904 10602 9673 -407 2023 806 C
ATOM 1058 CD2 PHE A 166 -11.870 6.558 48.360 1.00 88.93 C
ANISOU 1058 CD2 PHE A 166 11752 11509 10530 -430 2276 916 C
ATOM 1059 CE1 PHE A 166 -9.239 7.372 48.287 1.00 85.20 C
ANISOU 1059 CE1 PHE A 166 11901 10649 9824 -222 1871 720 C
ATOM 1060 CE2 PHE A 166 -11.524 7.718 47.693 1.00 89.46 C
ANISOU 1060 CE2 PHE A 166 11769 11550 10674 -202 2114 848 C
ATOM 1061 CZ PHE A 166 -10.207 8.125 47.658 1.00 87.64 C
ANISOU 1061 CZ PHE A 166 11865 11109 10324 -114 1924 747 C
ATOM 1062 N LEU A 167 -11.098 1.664 51.043 1.00 89.50 N
ANISOU 1062 N LEU A 167 12851 11110 10044 -1261 2673 1245 N
ATOM 1063 CA LEU A 167 -11.712 0.738 51.996 1.00 89.93 C
ANISOU 1063 CA LEU A 167 13036 11143 9990 -1455 2985 1392 C
ATOM 1064 C LEU A 167 -10.780 0.342 53.134 1.00 88.30 C
ANISOU 1064 C LEU A 167 13344 10746 9461 -1350 3014 1462 C
ATOM 1065 O LEU A 167 -11.198 0.445 54.300 1.00 89.03 O
ANISOU 1065 O LEU A 167 13576 10903 9350 -1307 3306 1535 O
ATOM 1066 CB LEU A 167 -12.245 -0.497 51.261 1.00 86.64 C
ANISOU 1066 CB LEU A 167 12488 10670 9763 -1832 2987 1466 C
ATOM 1067 CG LEU A 167 -13.461 -0.307 50.357 1.00 88.98 C
ANISOU 1067 CG LEU A 167 12240 11223 10345 -2016 3015 1437 C
ATOM 1068 CD1 LEU A 167 -13.752 -1.585 49.588 1.00 88.92 C
ANISOU 1068 CD1 LEU A 167 12188 11111 10485 -2427 2953 1467 C
ATOM 1069 CD2 LEU A 167 -14.665 0.107 51.186 1.00 91.20 C
ANISOU 1069 CD2 LEU A 167 12256 11757 10640 -2010 3393 1509 C
ATOM 1070 N PRO A 168 -9.541 -0.110 52.897 1.00 90.46 N
ANISOU 1070 N PRO A 168 13907 10807 9658 -1293 2735 1455 N
ATOM 1071 CA PRO A 168 -8.681 -0.453 54.041 1.00 89.45 C
ANISOU 1071 CA PRO A 168 14239 10543 9205 -1164 2739 1547 C
ATOM 1072 C PRO A 168 -8.391 0.728 54.948 1.00 89.77 C
ANISOU 1072 C PRO A 168 14393 10711 9004 -901 2764 1453 C
ATOM 1073 O PRO A 168 -8.151 0.535 56.145 1.00 89.77 O
ANISOU 1073 O PRO A 168 14735 10690 8685 -832 2881 1543 O
ATOM 1074 CB PRO A 168 -7.401 -0.972 53.376 1.00 86.12 C
ANISOU 1074 CB PRO A 168 13985 9917 8819 -1106 2395 1529 C
ATOM 1075 CG PRO A 168 -7.816 -1.391 52.019 1.00 86.09 C
ANISOU 1075 CG PRO A 168 13700 9880 9130 -1313 2319 1477 C
ATOM 1076 CD PRO A 168 -8.874 -0.413 51.619 1.00 87.74 C
ANISOU 1076 CD PRO A 168 13491 10345 9502 -1340 2421 1380 C
ATOM 1077 N ILE A 169 -8.403 1.951 54.418 1.00 89.47 N
ANISOU 1077 N ILE A 169 14111 10793 9091 -756 2660 1275 N
ATOM 1078 CA ILE A 169 -8.115 3.112 55.251 1.00 89.86 C
ANISOU 1078 CA ILE A 169 14305 10922 8917 -526 2691 1152 C
ATOM 1079 C ILE A 169 -9.378 3.608 55.942 1.00 91.67 C
ANISOU 1079 C ILE A 169 14413 11314 9104 -507 3095 1155 C
ATOM 1080 O ILE A 169 -9.344 3.989 57.115 1.00 92.02 O
ANISOU 1080 O ILE A 169 14730 11396 8839 -393 3268 1131 O
ATOM 1081 CB ILE A 169 -7.456 4.217 54.411 1.00 90.69 C
ANISOU 1081 CB ILE A 169 14265 11026 9168 -375 2412 962 C
ATOM 1082 CG1 ILE A 169 -6.209 3.681 53.699 1.00 88.92 C
ANISOU 1082 CG1 ILE A 169 14125 10662 8998 -397 2050 964 C
ATOM 1083 CG2 ILE A 169 -7.082 5.391 55.300 1.00 91.14 C
ANISOU 1083 CG2 ILE A 169 14528 11118 8984 -173 2438 811 C
ATOM 1084 CD1 ILE A 169 -5.123 3.197 54.634 1.00 88.02 C
ANISOU 1084 CD1 ILE A 169 14397 10467 8578 -328 1916 1021 C
ATOM 1085 N GLN A 170 -10.512 3.604 55.235 1.00 90.86 N
ANISOU 1085 N GLN A 170 13893 11332 9299 -615 3254 1182 N
ATOM 1086 CA GLN A 170 -11.761 4.055 55.839 1.00 92.76 C
ANISOU 1086 CA GLN A 170 13946 11757 9542 -579 3663 1196 C
ATOM 1087 C GLN A 170 -12.311 3.038 56.831 1.00 93.10 C
ANISOU 1087 C GLN A 170 14166 11814 9395 -765 3996 1377 C
ATOM 1088 O GLN A 170 -12.950 3.424 57.816 1.00 94.16 O
ANISOU 1088 O GLN A 170 14359 12066 9352 -682 4359 1382 O
ATOM 1089 CB GLN A 170 -12.793 4.352 54.750 1.00 91.84 C
ANISOU 1089 CB GLN A 170 13275 11806 9815 -629 3697 1189 C
ATOM 1090 CG GLN A 170 -12.449 5.540 53.863 1.00 92.02 C
ANISOU 1090 CG GLN A 170 13125 11832 10007 -404 3446 1035 C
ATOM 1091 CD GLN A 170 -12.518 6.861 54.606 1.00 92.66 C
ANISOU 1091 CD GLN A 170 13317 11937 9954 -95 3626 900 C
ATOM 1092 OE1 GLN A 170 -13.400 7.070 55.439 1.00 93.85 O
ANISOU 1092 OE1 GLN A 170 13418 12211 10027 -26 4011 922 O
ATOM 1093 NE2 GLN A 170 -11.591 7.762 54.302 1.00 91.91 N
ANISOU 1093 NE2 GLN A 170 13381 11711 9830 83 3369 750 N
ATOM 1094 N MET A 171 -12.081 1.747 56.597 1.00 94.48 N
ANISOU 1094 N MET A 171 14451 11852 9596 -1013 3909 1528 N
ATOM 1095 CA MET A 171 -12.551 0.704 57.502 1.00 94.85 C
ANISOU 1095 CA MET A 171 14712 11862 9463 -1216 4228 1731 C
ATOM 1096 C MET A 171 -11.565 0.396 58.621 1.00 93.67 C
ANISOU 1096 C MET A 171 15143 11567 8880 -1100 4180 1807 C
ATOM 1097 O MET A 171 -11.802 -0.541 59.393 1.00 93.88 O
ANISOU 1097 O MET A 171 15433 11522 8715 -1254 4417 2009 O
ATOM 1098 CB MET A 171 -12.861 -0.578 56.722 1.00 94.34 C
ANISOU 1098 CB MET A 171 14518 11682 9645 -1563 4190 1864 C
ATOM 1099 CG MET A 171 -14.043 -0.465 55.768 1.00 96.05 C
ANISOU 1099 CG MET A 171 14148 12098 10249 -1754 4281 1825 C
ATOM 1100 SD MET A 171 -15.597 -0.119 56.619 1.00 98.59 S
ANISOU 1100 SD MET A 171 14156 12723 10579 -1812 4844 1896 S
ATOM 1101 CE MET A 171 -15.819 1.621 56.250 1.00 99.54 C
ANISOU 1101 CE MET A 171 13916 13077 10827 -1416 4776 1684 C
ATOM 1102 N HIS A 172 -10.467 1.149 58.714 1.00 95.24 N
ANISOU 1102 N HIS A 172 15542 11726 8918 -848 3872 1662 N
ATOM 1103 CA HIS A 172 -9.477 1.035 59.787 1.00 94.47 C
ANISOU 1103 CA HIS A 172 15958 11553 8384 -710 3765 1708 C
ATOM 1104 C HIS A 172 -8.818 -0.340 59.833 1.00 93.50 C
ANISOU 1104 C HIS A 172 16125 11218 8182 -822 3618 1932 C
ATOM 1105 O HIS A 172 -8.348 -0.772 60.888 1.00 93.46 O
ANISOU 1105 O HIS A 172 16553 11165 7793 -760 3644 2075 O
ATOM 1106 CB HIS A 172 -10.098 1.376 61.146 1.00 96.64 C
ANISOU 1106 CB HIS A 172 16460 11962 8295 -653 4164 1736 C
ATOM 1107 CG HIS A 172 -10.524 2.805 61.268 1.00 97.52 C
ANISOU 1107 CG HIS A 172 16399 12237 8416 -466 4298 1494 C
ATOM 1108 ND1 HIS A 172 -11.292 3.268 62.315 1.00 98.80 N
ANISOU 1108 ND1 HIS A 172 16678 12539 8324 -399 4727 1470 N
ATOM 1109 CD2 HIS A 172 -10.293 3.874 60.469 1.00 97.40 C
ANISOU 1109 CD2 HIS A 172 16130 12241 8635 -320 4085 1270 C
ATOM 1110 CE1 HIS A 172 -11.516 4.560 62.155 1.00 99.34 C
ANISOU 1110 CE1 HIS A 172 16573 12690 8482 -203 4772 1231 C
ATOM 1111 NE2 HIS A 172 -10.921 4.952 61.042 1.00 98.57 N
ANISOU 1111 NE2 HIS A 172 16256 12514 8683 -157 4381 1116 N
ATOM 1112 N TRP A 173 -8.768 -1.035 58.695 1.00 94.87 N
ANISOU 1112 N TRP A 173 16091 11255 8701 -974 3461 1966 N
ATOM 1113 CA TRP A 173 -8.099 -2.327 58.615 1.00 93.97 C
ANISOU 1113 CA TRP A 173 16258 10888 8557 -1050 3322 2160 C
ATOM 1114 C TRP A 173 -6.586 -2.203 58.702 1.00 92.82 C
ANISOU 1114 C TRP A 173 16359 10667 8242 -795 2909 2127 C
ATOM 1115 O TRP A 173 -5.909 -3.215 58.915 1.00 92.36 O
ANISOU 1115 O TRP A 173 16605 10411 8078 -768 2799 2316 O
ATOM 1116 CB TRP A 173 -8.494 -3.030 57.315 1.00 89.28 C
ANISOU 1116 CB TRP A 173 15377 10166 8380 -1291 3283 2156 C
ATOM 1117 CG TRP A 173 -9.942 -3.406 57.275 1.00 90.71 C
ANISOU 1117 CG TRP A 173 15322 10418 8724 -1599 3670 2229 C
ATOM 1118 CD1 TRP A 173 -10.815 -3.408 58.324 1.00 92.04 C
ANISOU 1118 CD1 TRP A 173 15565 10705 8702 -1678 4074 2345 C
ATOM 1119 CD2 TRP A 173 -10.699 -3.798 56.123 1.00 91.17 C
ANISOU 1119 CD2 TRP A 173 15004 10470 9167 -1883 3691 2179 C
ATOM 1120 NE1 TRP A 173 -12.062 -3.797 57.902 1.00 93.39 N
ANISOU 1120 NE1 TRP A 173 15394 10947 9142 -2000 4353 2382 N
ATOM 1121 CE2 TRP A 173 -12.018 -4.040 56.554 1.00 92.92 C
ANISOU 1121 CE2 TRP A 173 15052 10820 9433 -2139 4104 2277 C
ATOM 1122 CE3 TRP A 173 -10.387 -3.977 54.772 1.00 90.40 C
ANISOU 1122 CE3 TRP A 173 14701 10286 9360 -1958 3403 2058 C
ATOM 1123 CZ2 TRP A 173 -13.025 -4.450 55.683 1.00 94.04 C
ANISOU 1123 CZ2 TRP A 173 14795 11023 9914 -2482 4204 2255 C
ATOM 1124 CZ3 TRP A 173 -11.389 -4.385 53.908 1.00 91.44 C
ANISOU 1124 CZ3 TRP A 173 14483 10467 9794 -2292 3499 2029 C
ATOM 1125 CH2 TRP A 173 -12.692 -4.617 54.367 1.00 93.33 C
ANISOU 1125 CH2 TRP A 173 14526 10850 10083 -2558 3880 2126 C
ATOM 1126 N TYR A 174 -6.046 -0.995 58.536 1.00 93.69 N
ANISOU 1126 N TYR A 174 16336 10924 8338 -610 2686 1900 N
ATOM 1127 CA TYR A 174 -4.615 -0.763 58.667 1.00 92.97 C
ANISOU 1127 CA TYR A 174 16423 10815 8087 -392 2294 1850 C
ATOM 1128 C TYR A 174 -4.196 -0.521 60.109 1.00 93.67 C
ANISOU 1128 C TYR A 174 16899 11006 7686 -248 2295 1907 C
ATOM 1129 O TYR A 174 -3.029 -0.748 60.443 1.00 93.46 O
ANISOU 1129 O TYR A 174 17088 10958 7465 -92 1982 1965 O
ATOM 1130 CB TYR A 174 -4.203 0.441 57.816 1.00 94.98 C
ANISOU 1130 CB TYR A 174 16369 11169 8551 -305 2059 1576 C
ATOM 1131 CG TYR A 174 -4.763 1.755 58.322 1.00 95.92 C
ANISOU 1131 CG TYR A 174 16422 11468 8553 -247 2220 1390 C
ATOM 1132 CD1 TYR A 174 -6.035 2.177 57.959 1.00 96.71 C
ANISOU 1132 CD1 TYR A 174 16235 11644 8866 -341 2521 1332 C
ATOM 1133 CD2 TYR A 174 -4.014 2.580 59.154 1.00 96.23 C
ANISOU 1133 CD2 TYR A 174 16687 11602 8275 -94 2068 1265 C
ATOM 1134 CE1 TYR A 174 -6.551 3.374 58.420 1.00 97.73 C
ANISOU 1134 CE1 TYR A 174 16318 11908 8905 -243 2698 1166 C
ATOM 1135 CE2 TYR A 174 -4.522 3.781 59.618 1.00 97.12 C
ANISOU 1135 CE2 TYR A 174 16790 11833 8278 -37 2242 1071 C
ATOM 1136 CZ TYR A 174 -5.791 4.173 59.247 1.00 97.83 C
ANISOU 1136 CZ TYR A 174 16608 11966 8596 -91 2572 1027 C
ATOM 1137 OH TYR A 174 -6.303 5.367 59.703 1.00 98.83 O
ANISOU 1137 OH TYR A 174 16736 12183 8630 11 2773 838 O
ATOM 1138 N ARG A 175 -5.120 -0.071 60.959 1.00 94.61 N
ANISOU 1138 N ARG A 175 17100 11254 7594 -290 2637 1891 N
ATOM 1139 CA ARG A 175 -4.796 0.383 62.308 1.00 95.37 C
ANISOU 1139 CA ARG A 175 17567 11483 7187 -160 2652 1882 C
ATOM 1140 C ARG A 175 -3.977 -0.644 63.073 1.00 95.41 C
ANISOU 1140 C ARG A 175 17933 11415 6905 -81 2463 2129 C
ATOM 1141 O ARG A 175 -4.397 -1.793 63.240 1.00 96.14 O
ANISOU 1141 O ARG A 175 18078 11374 7076 -179 2620 2361 O
ATOM 1142 CB ARG A 175 -6.082 0.700 63.076 1.00 99.68 C
ANISOU 1142 CB ARG A 175 18161 12142 7570 -241 3148 1882 C
ATOM 1143 CG ARG A 175 -6.902 1.846 62.512 1.00100.09 C
ANISOU 1143 CG ARG A 175 17828 12302 7901 -245 3328 1626 C
ATOM 1144 CD ARG A 175 -6.179 3.170 62.669 1.00100.08 C
ANISOU 1144 CD ARG A 175 17876 12387 7763 -70 3089 1336 C
ATOM 1145 NE ARG A 175 -6.990 4.308 62.250 1.00100.72 N
ANISOU 1145 NE ARG A 175 17655 12536 8076 -30 3300 1111 N
ATOM 1146 CZ ARG A 175 -7.776 5.000 63.068 1.00101.84 C
ANISOU 1146 CZ ARG A 175 17898 12785 8010 33 3672 1010 C
ATOM 1147 NH1 ARG A 175 -7.855 4.668 64.350 1.00102.46 N
ANISOU 1147 NH1 ARG A 175 18386 12928 7615 36 3875 1106 N
ATOM 1148 NH2 ARG A 175 -8.481 6.024 62.608 1.00102.51 N
ANISOU 1148 NH2 ARG A 175 17691 12910 8350 114 3853 821 N
ATOM 1149 N ALA A 176 -2.804 -0.221 63.533 1.00 94.35 N
ANISOU 1149 N ALA A 176 17957 11380 6511 95 2085 2052 N
ATOM 1150 CA ALA A 176 -1.967 -1.054 64.376 1.00 96.22 C
ANISOU 1150 CA ALA A 176 18434 11616 6508 216 1841 2256 C
ATOM 1151 C ALA A 176 -2.528 -1.096 65.795 1.00100.72 C
ANISOU 1151 C ALA A 176 19229 12313 6725 198 2066 2318 C
ATOM 1152 O ALA A 176 -3.380 -0.291 66.182 1.00101.52 O
ANISOU 1152 O ALA A 176 19308 12531 6735 128 2358 2152 O
ATOM 1153 CB ALA A 176 -0.528 -0.536 64.381 1.00 97.36 C
ANISOU 1153 CB ALA A 176 18609 11880 6504 392 1343 2146 C
ATOM 1154 N THR A 177 -2.038 -2.054 66.580 1.00 98.59 N
ANISOU 1154 N THR A 177 19185 12021 6255 280 1938 2568 N
ATOM 1155 CA THR A 177 -2.512 -2.254 67.942 1.00103.57 C
ANISOU 1155 CA THR A 177 20064 12762 6526 262 2141 2675 C
ATOM 1156 C THR A 177 -1.467 -1.908 68.996 1.00106.60 C
ANISOU 1156 C THR A 177 20672 13365 6466 425 1781 2651 C
ATOM 1157 O THR A 177 -1.701 -2.152 70.184 1.00111.28 O
ANISOU 1157 O THR A 177 21510 14062 6711 428 1896 2767 O
ATOM 1158 CB THR A 177 -2.988 -3.696 68.136 1.00107.47 C
ANISOU 1158 CB THR A 177 20670 13055 7109 188 2352 3012 C
ATOM 1159 OG1 THR A 177 -1.912 -4.603 67.859 1.00107.49 O
ANISOU 1159 OG1 THR A 177 20742 12917 7183 339 2005 3214 O
ATOM 1160 CG2 THR A 177 -4.163 -4.001 67.219 1.00105.38 C
ANISOU 1160 CG2 THR A 177 20169 12615 7254 -36 2735 3012 C
ATOM 1161 N HIS A 178 -0.326 -1.351 68.603 1.00105.29 N
ANISOU 1161 N HIS A 178 20419 13290 6297 543 1347 2506 N
ATOM 1162 CA HIS A 178 0.666 -0.959 69.591 1.00108.54 C
ANISOU 1162 CA HIS A 178 20996 13952 6291 660 981 2459 C
ATOM 1163 C HIS A 178 0.404 0.467 70.066 1.00108.92 C
ANISOU 1163 C HIS A 178 21079 14194 6111 584 1048 2098 C
ATOM 1164 O HIS A 178 -0.267 1.259 69.400 1.00105.77 O
ANISOU 1164 O HIS A 178 20525 13729 5933 492 1279 1864 O
ATOM 1165 CB HIS A 178 2.089 -1.100 69.042 1.00112.80 C
ANISOU 1165 CB HIS A 178 21402 14532 6926 816 459 2490 C
ATOM 1166 CG HIS A 178 2.409 -0.168 67.916 1.00107.93 C
ANISOU 1166 CG HIS A 178 20522 13904 6582 780 314 2203 C
ATOM 1167 ND1 HIS A 178 2.046 -0.424 66.612 1.00103.54 N
ANISOU 1167 ND1 HIS A 178 19761 13115 6466 737 457 2215 N
ATOM 1168 CD2 HIS A 178 3.081 1.007 67.896 1.00107.12 C
ANISOU 1168 CD2 HIS A 178 20339 13991 6371 764 33 1899 C
ATOM 1169 CE1 HIS A 178 2.473 0.558 65.838 1.00100.33 C
ANISOU 1169 CE1 HIS A 178 19166 12759 6195 714 275 1946 C
ATOM 1170 NE2 HIS A 178 3.102 1.440 66.593 1.00102.36 N
ANISOU 1170 NE2 HIS A 178 19494 13260 6138 723 21 1746 N
ATOM 1171 N GLN A 179 0.955 0.782 71.243 1.00110.84 N
ANISOU 1171 N GLN A 179 21536 14677 5902 629 840 2054 N
ATOM 1172 CA GLN A 179 0.546 1.980 71.971 1.00112.83 C
ANISOU 1172 CA GLN A 179 21911 15088 5871 547 987 1736 C
ATOM 1173 C GLN A 179 0.847 3.252 71.187 1.00108.97 C
ANISOU 1173 C GLN A 179 21233 14602 5568 498 851 1355 C
ATOM 1174 O GLN A 179 0.006 4.156 71.114 1.00108.19 O
ANISOU 1174 O GLN A 179 21123 14457 5525 423 1177 1101 O
ATOM 1175 CB GLN A 179 1.235 2.017 73.334 1.00118.68 C
ANISOU 1175 CB GLN A 179 22918 16099 6077 593 724 1764 C
ATOM 1176 CG GLN A 179 0.756 3.130 74.249 1.00121.89 C
ANISOU 1176 CG GLN A 179 23517 16656 6140 507 916 1450 C
ATOM 1177 CD GLN A 179 -0.701 2.972 74.649 1.00123.55 C
ANISOU 1177 CD GLN A 179 23841 16767 6334 451 1517 1508 C
ATOM 1178 OE1 GLN A 179 -1.574 3.688 74.158 1.00121.12 O
ANISOU 1178 OE1 GLN A 179 23411 16348 6260 392 1863 1290 O
ATOM 1179 NE2 GLN A 179 -0.968 2.028 75.544 1.00128.07 N
ANISOU 1179 NE2 GLN A 179 24633 17389 6637 473 1646 1813 N
ATOM 1180 N GLU A 180 2.041 3.342 70.595 1.00111.04 N
ANISOU 1180 N GLU A 180 21338 14913 5939 547 381 1316 N
ATOM 1181 CA GLU A 180 2.430 4.563 69.892 1.00108.02 C
ANISOU 1181 CA GLU A 180 20792 14534 5715 477 222 953 C
ATOM 1182 C GLU A 180 1.480 4.877 68.741 1.00103.34 C
ANISOU 1182 C GLU A 180 20017 13704 5543 426 583 862 C
ATOM 1183 O GLU A 180 1.156 6.046 68.495 1.00102.15 O
ANISOU 1183 O GLU A 180 19833 13520 5460 356 710 540 O
ATOM 1184 CB GLU A 180 3.867 4.441 69.382 1.00113.87 C
ANISOU 1184 CB GLU A 180 21350 15376 6541 532 -333 975 C
ATOM 1185 CG GLU A 180 4.365 5.671 68.641 1.00111.12 C
ANISOU 1185 CG GLU A 180 20826 15029 6365 429 -524 608 C
ATOM 1186 CD GLU A 180 5.807 5.542 68.194 1.00110.62 C
ANISOU 1186 CD GLU A 180 20543 15104 6382 469 -1072 633 C
ATOM 1187 OE1 GLU A 180 6.433 4.505 68.498 1.00112.59 O
ANISOU 1187 OE1 GLU A 180 20776 15459 6546 612 -1307 940 O
ATOM 1188 OE2 GLU A 180 6.308 6.470 67.523 1.00108.58 O
ANISOU 1188 OE2 GLU A 180 20117 14845 6293 363 -1254 354 O
ATOM 1189 N ALA A 181 1.020 3.849 68.023 1.00107.60 N
ANISOU 1189 N ALA A 181 20438 14072 6374 459 755 1140 N
ATOM 1190 CA ALA A 181 0.083 4.084 66.929 1.00103.73 C
ANISOU 1190 CA ALA A 181 19750 13393 6270 398 1093 1075 C
ATOM 1191 C ALA A 181 -1.282 4.506 67.454 1.00105.42 C
ANISOU 1191 C ALA A 181 20035 13597 6422 341 1611 989 C
ATOM 1192 O ALA A 181 -1.937 5.375 66.867 1.00103.43 O
ANISOU 1192 O ALA A 181 19648 13280 6372 309 1849 775 O
ATOM 1193 CB ALA A 181 -0.040 2.833 66.060 1.00102.45 C
ANISOU 1193 CB ALA A 181 19445 13055 6426 415 1134 1386 C
ATOM 1194 N ILE A 182 -1.722 3.907 68.563 1.00102.70 N
ANISOU 1194 N ILE A 182 19894 13323 5803 342 1796 1160 N
ATOM 1195 CA ILE A 182 -3.033 4.227 69.122 1.00105.01 C
ANISOU 1195 CA ILE A 182 20236 13628 6033 296 2308 1100 C
ATOM 1196 C ILE A 182 -3.077 5.674 69.595 1.00106.39 C
ANISOU 1196 C ILE A 182 20507 13892 6024 312 2355 721 C
ATOM 1197 O ILE A 182 -4.089 6.366 69.429 1.00106.22 O
ANISOU 1197 O ILE A 182 20389 13824 6145 310 2751 562 O
ATOM 1198 CB ILE A 182 -3.380 3.244 70.256 1.00105.90 C
ANISOU 1198 CB ILE A 182 20574 13807 5858 286 2469 1375 C
ATOM 1199 CG1 ILE A 182 -3.500 1.820 69.708 1.00104.70 C
ANISOU 1199 CG1 ILE A 182 20328 13499 5956 252 2495 1738 C
ATOM 1200 CG2 ILE A 182 -4.666 3.660 70.962 1.00109.17 C
ANISOU 1200 CG2 ILE A 182 21043 14274 6160 244 2990 1292 C
ATOM 1201 CD1 ILE A 182 -3.605 0.760 70.781 1.00109.65 C
ANISOU 1201 CD1 ILE A 182 21205 14158 6298 250 2574 2039 C
ATOM 1202 N ASN A 183 -1.981 6.159 70.185 1.00108.14 N
ANISOU 1202 N ASN A 183 20905 14240 5942 327 1953 566 N
ATOM 1203 CA ASN A 183 -1.945 7.550 70.622 1.00109.78 C
ANISOU 1203 CA ASN A 183 21228 14497 5988 313 1975 178 C
ATOM 1204 C ASN A 183 -1.983 8.512 69.440 1.00105.53 C
ANISOU 1204 C ASN A 183 20468 13803 5824 305 1985 -73 C
ATOM 1205 O ASN A 183 -2.547 9.605 69.553 1.00106.45 O
ANISOU 1205 O ASN A 183 20621 13860 5964 318 2240 -353 O
ATOM 1206 CB ASN A 183 -0.703 7.808 71.477 1.00109.25 C
ANISOU 1206 CB ASN A 183 21368 14618 5523 287 1506 68 C
ATOM 1207 CG ASN A 183 -0.705 7.006 72.766 1.00114.50 C
ANISOU 1207 CG ASN A 183 22291 15458 5756 309 1515 293 C
ATOM 1208 OD1 ASN A 183 0.161 6.161 72.985 1.00115.47 O
ANISOU 1208 OD1 ASN A 183 22443 15692 5741 342 1155 529 O
ATOM 1209 ND2 ASN A 183 -1.686 7.266 73.624 1.00118.26 N
ANISOU 1209 ND2 ASN A 183 22951 15961 6019 308 1938 231 N
ATOM 1210 N CYS A 184 -1.394 8.131 68.304 1.00107.79 N
ANISOU 1210 N CYS A 184 20537 14012 6407 297 1722 28 N
ATOM 1211 CA CYS A 184 -1.465 8.984 67.122 1.00103.95 C
ANISOU 1211 CA CYS A 184 19845 13376 6276 289 1747 -180 C
ATOM 1212 C CYS A 184 -2.838 8.916 66.465 1.00102.24 C
ANISOU 1212 C CYS A 184 19433 13040 6374 332 2250 -103 C
ATOM 1213 O CYS A 184 -3.257 9.873 65.805 1.00101.34 O
ANISOU 1213 O CYS A 184 19197 12815 6492 366 2420 -315 O
ATOM 1214 CB CYS A 184 -0.375 8.591 66.121 1.00103.30 C
ANISOU 1214 CB CYS A 184 19592 13269 6388 265 1306 -96 C
ATOM 1215 SG CYS A 184 -0.323 9.614 64.626 1.00102.54 S
ANISOU 1215 SG CYS A 184 19142 12994 6823 235 1268 -333 S
ATOM 1216 N TYR A 185 -3.549 7.800 66.639 1.00105.53 N
ANISOU 1216 N TYR A 185 19802 13479 6813 327 2490 203 N
ATOM 1217 CA TYR A 185 -4.859 7.642 66.016 1.00104.36 C
ANISOU 1217 CA TYR A 185 19407 13263 6981 332 2953 297 C
ATOM 1218 C TYR A 185 -5.885 8.574 66.651 1.00107.30 C
ANISOU 1218 C TYR A 185 19812 13666 7293 404 3385 97 C
ATOM 1219 O TYR A 185 -6.597 9.300 65.948 1.00105.97 O
ANISOU 1219 O TYR A 185 19424 13427 7412 473 3644 -31 O
ATOM 1220 CB TYR A 185 -5.299 6.182 66.120 1.00104.31 C
ANISOU 1220 CB TYR A 185 19351 13267 7015 258 3081 666 C
ATOM 1221 CG TYR A 185 -4.470 5.243 65.273 1.00102.03 C
ANISOU 1221 CG TYR A 185 18982 12894 6892 215 2731 872 C
ATOM 1222 CD1 TYR A 185 -3.743 5.717 64.189 1.00101.27 C
ANISOU 1222 CD1 TYR A 185 18647 12728 7101 229 2399 732 C
ATOM 1223 CD2 TYR A 185 -4.377 3.892 65.583 1.00102.53 C
ANISOU 1223 CD2 TYR A 185 19119 12930 6907 167 2689 1189 C
ATOM 1224 CE1 TYR A 185 -2.974 4.868 63.416 1.00100.37 C
ANISOU 1224 CE1 TYR A 185 18375 12539 7222 206 2065 897 C
ATOM 1225 CE2 TYR A 185 -3.603 3.035 64.820 1.00100.97 C
ANISOU 1225 CE2 TYR A 185 18860 12624 6878 159 2382 1369 C
ATOM 1226 CZ TYR A 185 -2.907 3.529 63.737 1.00100.21 C
ANISOU 1226 CZ TYR A 185 18519 12480 7078 184 2074 1215 C
ATOM 1227 OH TYR A 185 -2.140 2.681 62.972 1.00 99.39 O
ANISOU 1227 OH TYR A 185 18281 12271 7212 193 1770 1368 O
ATOM 1228 N ALA A 186 -5.975 8.567 67.983 1.00103.80 N
ANISOU 1228 N ALA A 186 19636 13329 6475 408 3473 75 N
ATOM 1229 CA ALA A 186 -6.919 9.449 68.662 1.00107.32 C
ANISOU 1229 CA ALA A 186 20136 13800 6840 492 3891 -123 C
ATOM 1230 C ALA A 186 -6.489 10.908 68.578 1.00107.27 C
ANISOU 1230 C ALA A 186 20229 13700 6827 564 3779 -506 C
ATOM 1231 O ALA A 186 -7.342 11.803 68.558 1.00108.62 O
ANISOU 1231 O ALA A 186 20326 13808 7137 680 4141 -685 O
ATOM 1232 CB ALA A 186 -7.080 9.027 70.122 1.00107.76 C
ANISOU 1232 CB ALA A 186 20484 13999 6461 466 4008 -43 C
ATOM 1233 N GLU A 187 -5.184 11.167 68.529 1.00107.23 N
ANISOU 1233 N GLU A 187 20378 13681 6686 496 3288 -631 N
ATOM 1234 CA GLU A 187 -4.693 12.534 68.420 1.00107.40 C
ANISOU 1234 CA GLU A 187 20499 13586 6723 511 3154 -999 C
ATOM 1235 C GLU A 187 -4.988 13.089 67.033 1.00103.28 C
ANISOU 1235 C GLU A 187 19692 12883 6666 580 3242 -1068 C
ATOM 1236 O GLU A 187 -4.637 12.479 66.018 1.00 99.25 O
ANISOU 1236 O GLU A 187 18976 12354 6381 538 3047 -899 O
ATOM 1237 CB GLU A 187 -3.193 12.581 68.703 1.00101.41 C
ANISOU 1237 CB GLU A 187 19918 12896 5718 381 2585 -1095 C
ATOM 1238 CG GLU A 187 -2.582 13.971 68.628 1.00102.09 C
ANISOU 1238 CG GLU A 187 20111 12856 5821 331 2412 -1482 C
ATOM 1239 CD GLU A 187 -3.101 14.903 69.707 1.00107.37 C
ANISOU 1239 CD GLU A 187 21047 13500 6247 371 2694 -1744 C
ATOM 1240 OE1 GLU A 187 -3.525 14.409 70.772 1.00111.19 O
ANISOU 1240 OE1 GLU A 187 21700 14140 6407 395 2868 -1643 O
ATOM 1241 OE2 GLU A 187 -3.081 16.133 69.490 1.00108.00 O
ANISOU 1241 OE2 GLU A 187 21183 13390 6462 380 2750 -2049 O
ATOM 1242 N GLU A 188 -5.637 14.254 66.990 1.00103.74 N
ANISOU 1242 N GLU A 188 19748 12801 6866 702 3542 -1310 N
ATOM 1243 CA GLU A 188 -6.001 14.853 65.714 1.00100.50 C
ANISOU 1243 CA GLU A 188 19072 12215 6898 807 3659 -1365 C
ATOM 1244 C GLU A 188 -4.859 15.652 65.098 1.00 98.46 C
ANISOU 1244 C GLU A 188 18889 11794 6727 719 3258 -1590 C
ATOM 1245 O GLU A 188 -4.870 15.894 63.885 1.00 97.24 O
ANISOU 1245 O GLU A 188 18458 11514 6974 759 3203 -1563 O
ATOM 1246 CB GLU A 188 -7.246 15.731 65.890 1.00 98.14 C
ANISOU 1246 CB GLU A 188 18701 11825 6761 1021 4169 -1487 C
ATOM 1247 CG GLU A 188 -7.822 16.268 64.591 1.00 95.34 C
ANISOU 1247 CG GLU A 188 18020 11318 6885 1189 4343 -1483 C
ATOM 1248 CD GLU A 188 -9.136 16.995 64.784 1.00 98.75 C
ANISOU 1248 CD GLU A 188 18314 11702 7503 1445 4855 -1542 C
ATOM 1249 OE1 GLU A 188 -9.606 17.082 65.937 1.00103.28 O
ANISOU 1249 OE1 GLU A 188 19063 12356 7824 1478 5094 -1602 O
ATOM 1250 OE2 GLU A 188 -9.700 17.477 63.779 1.00 97.21 O
ANISOU 1250 OE2 GLU A 188 17825 11402 7710 1630 5016 -1518 O
ATOM 1251 N THR A 189 -3.867 16.044 65.893 1.00102.78 N
ANISOU 1251 N THR A 189 19722 12362 6967 576 2937 -1786 N
ATOM 1252 CA THR A 189 -2.691 16.731 65.378 1.00101.31 C
ANISOU 1252 CA THR A 189 19581 12054 6860 432 2527 -1992 C
ATOM 1253 C THR A 189 -1.622 15.771 64.872 1.00 98.79 C
ANISOU 1253 C THR A 189 19142 11875 6517 285 2062 -1810 C
ATOM 1254 O THR A 189 -0.599 16.226 64.351 1.00 98.39 O
ANISOU 1254 O THR A 189 19066 11757 6561 146 1702 -1951 O
ATOM 1255 CB THR A 189 -2.086 17.639 66.455 1.00101.01 C
ANISOU 1255 CB THR A 189 19863 11996 6519 313 2384 -2301 C
ATOM 1256 OG1 THR A 189 -1.652 16.845 67.565 1.00103.61 O
ANISOU 1256 OG1 THR A 189 20356 12595 6417 222 2193 -2204 O
ATOM 1257 CG2 THR A 189 -3.113 18.654 66.934 1.00104.59 C
ANISOU 1257 CG2 THR A 189 20457 12277 7006 477 2850 -2496 C
ATOM 1258 N CYS A 190 -1.831 14.464 65.010 1.00 99.87 N
ANISOU 1258 N CYS A 190 19198 12195 6552 310 2069 -1494 N
ATOM 1259 CA CYS A 190 -0.887 13.461 64.540 1.00 99.21 C
ANISOU 1259 CA CYS A 190 18930 12234 6531 216 1639 -1268 C
ATOM 1260 C CYS A 190 -1.485 12.717 63.356 1.00 98.42 C
ANISOU 1260 C CYS A 190 18367 12088 6940 281 1744 -985 C
ATOM 1261 O CYS A 190 -2.612 12.215 63.436 1.00 98.59 O
ANISOU 1261 O CYS A 190 18315 12129 7016 371 2121 -816 O
ATOM 1262 CB CYS A 190 -0.526 12.473 65.653 1.00106.64 C
ANISOU 1262 CB CYS A 190 20090 13400 7027 188 1492 -1089 C
ATOM 1263 SG CYS A 190 0.733 11.259 65.179 1.00106.09 S
ANISOU 1263 SG CYS A 190 19858 13469 6982 130 958 -813 S
ATOM 1264 N CYS A 191 -0.731 12.653 62.262 1.00 97.07 N
ANISOU 1264 N CYS A 191 17885 11868 7131 217 1419 -944 N
ATOM 1265 CA CYS A 191 -1.125 11.917 61.068 1.00 96.34 C
ANISOU 1265 CA CYS A 191 17376 11738 7490 248 1449 -700 C
ATOM 1266 C CYS A 191 -0.002 10.985 60.640 1.00 95.67 C
ANISOU 1266 C CYS A 191 17150 11733 7467 174 1033 -533 C
ATOM 1267 O CYS A 191 0.264 10.798 59.449 1.00 94.99 O
ANISOU 1267 O CYS A 191 16737 11585 7771 154 897 -459 O
ATOM 1268 CB CYS A 191 -1.509 12.872 59.939 1.00 90.00 C
ANISOU 1268 CB CYS A 191 16306 10765 7127 286 1549 -816 C
ATOM 1269 SG CYS A 191 -2.299 12.105 58.498 1.00 89.53 S
ANISOU 1269 SG CYS A 191 15755 10682 7579 325 1651 -546 S
ATOM 1270 N ASP A 192 0.693 10.402 61.612 1.00 96.00 N
ANISOU 1270 N ASP A 192 17446 11921 7109 153 825 -469 N
ATOM 1271 CA ASP A 192 1.697 9.398 61.300 1.00 95.62 C
ANISOU 1271 CA ASP A 192 17267 11955 7109 142 463 -270 C
ATOM 1272 C ASP A 192 1.020 8.154 60.742 1.00 94.88 C
ANISOU 1272 C ASP A 192 17000 11807 7244 195 640 37 C
ATOM 1273 O ASP A 192 -0.065 7.766 61.183 1.00 95.00 O
ANISOU 1273 O ASP A 192 17125 11809 7163 221 992 151 O
ATOM 1274 CB ASP A 192 2.515 9.046 62.541 1.00 98.91 C
ANISOU 1274 CB ASP A 192 18007 12558 7016 144 202 -239 C
ATOM 1275 CG ASP A 192 3.407 10.184 62.994 1.00 99.73 C
ANISOU 1275 CG ASP A 192 18245 12739 6908 36 -72 -555 C
ATOM 1276 OD1 ASP A 192 3.820 10.994 62.139 1.00 99.45 O
ANISOU 1276 OD1 ASP A 192 17981 12612 7195 -49 -182 -738 O
ATOM 1277 OD2 ASP A 192 3.697 10.268 64.206 1.00100.71 O
ANISOU 1277 OD2 ASP A 192 18721 13017 6529 16 -178 -621 O
ATOM 1278 N PHE A 193 1.663 7.530 59.763 1.00 96.99 N
ANISOU 1278 N PHE A 193 16998 12038 7815 194 413 159 N
ATOM 1279 CA PHE A 193 1.073 6.408 59.038 1.00 96.16 C
ANISOU 1279 CA PHE A 193 16719 11839 7977 208 564 403 C
ATOM 1280 C PHE A 193 1.656 5.113 59.593 1.00 96.19 C
ANISOU 1280 C PHE A 193 16896 11883 7771 274 407 663 C
ATOM 1281 O PHE A 193 2.650 4.589 59.089 1.00 95.99 O
ANISOU 1281 O PHE A 193 16743 11855 7874 323 117 742 O
ATOM 1282 CB PHE A 193 1.316 6.557 57.542 1.00 96.30 C
ANISOU 1282 CB PHE A 193 16369 11765 8457 174 462 359 C
ATOM 1283 CG PHE A 193 0.716 5.458 56.717 1.00 95.41 C
ANISOU 1283 CG PHE A 193 16089 11550 8613 154 601 564 C
ATOM 1284 CD1 PHE A 193 -0.656 5.352 56.575 1.00 95.38 C
ANISOU 1284 CD1 PHE A 193 16021 11503 8717 102 951 616 C
ATOM 1285 CD2 PHE A 193 1.525 4.550 56.055 1.00 94.78 C
ANISOU 1285 CD2 PHE A 193 15903 11418 8689 180 388 691 C
ATOM 1286 CE1 PHE A 193 -1.211 4.343 55.811 1.00 94.66 C
ANISOU 1286 CE1 PHE A 193 15778 11324 8866 32 1060 780 C
ATOM 1287 CE2 PHE A 193 0.974 3.543 55.284 1.00 93.88 C
ANISOU 1287 CE2 PHE A 193 15680 11181 8811 136 523 846 C
ATOM 1288 CZ PHE A 193 -0.396 3.444 55.159 1.00 93.78 C
ANISOU 1288 CZ PHE A 193 15615 11130 8889 39 846 884 C
ATOM 1289 N PHE A 194 1.027 4.598 60.647 1.00 97.29 N
ANISOU 1289 N PHE A 194 17334 12052 7580 293 622 808 N
ATOM 1290 CA PHE A 194 1.369 3.301 61.213 1.00 97.43 C
ANISOU 1290 CA PHE A 194 17567 12064 7389 368 545 1106 C
ATOM 1291 C PHE A 194 0.327 2.281 60.781 1.00 96.73 C
ANISOU 1291 C PHE A 194 17432 11805 7515 306 880 1323 C
ATOM 1292 O PHE A 194 -0.877 2.540 60.876 1.00 96.80 O
ANISOU 1292 O PHE A 194 17422 11799 7558 213 1249 1288 O
ATOM 1293 CB PHE A 194 1.436 3.349 62.740 1.00 99.46 C
ANISOU 1293 CB PHE A 194 18246 12469 7076 415 551 1152 C
ATOM 1294 CG PHE A 194 2.537 4.210 63.274 1.00100.37 C
ANISOU 1294 CG PHE A 194 18442 12772 6923 445 173 947 C
ATOM 1295 CD1 PHE A 194 3.851 3.776 63.244 1.00100.89 C
ANISOU 1295 CD1 PHE A 194 18453 12932 6949 542 -270 1042 C
ATOM 1296 CD2 PHE A 194 2.255 5.441 63.838 1.00100.90 C
ANISOU 1296 CD2 PHE A 194 18645 12923 6771 372 266 656 C
ATOM 1297 CE1 PHE A 194 4.867 4.568 63.742 1.00101.98 C
ANISOU 1297 CE1 PHE A 194 18626 13279 6843 528 -640 846 C
ATOM 1298 CE2 PHE A 194 3.264 6.233 64.343 1.00101.83 C
ANISOU 1298 CE2 PHE A 194 18855 13205 6629 347 -90 443 C
ATOM 1299 CZ PHE A 194 4.571 5.798 64.294 1.00102.40 C
ANISOU 1299 CZ PHE A 194 18833 13404 6670 407 -556 537 C
ATOM 1300 N THR A 195 0.791 1.128 60.306 1.00 91.64 N
ANISOU 1300 N THR A 195 16762 11032 7024 353 758 1540 N
ATOM 1301 CA THR A 195 -0.092 0.047 59.901 1.00 91.05 C
ANISOU 1301 CA THR A 195 16684 10765 7146 257 1047 1745 C
ATOM 1302 C THR A 195 0.348 -1.251 60.559 1.00 91.42 C
ANISOU 1302 C THR A 195 17061 10704 6971 359 995 2066 C
ATOM 1303 O THR A 195 1.526 -1.439 60.876 1.00 91.93 O
ANISOU 1303 O THR A 195 17228 10828 6875 542 654 2136 O
ATOM 1304 CB THR A 195 -0.113 -0.137 58.378 1.00 88.63 C
ANISOU 1304 CB THR A 195 16022 10322 7333 185 1007 1673 C
ATOM 1305 OG1 THR A 195 1.197 -0.492 57.917 1.00 88.46 O
ANISOU 1305 OG1 THR A 195 15946 10263 7401 330 654 1702 O
ATOM 1306 CG2 THR A 195 -0.554 1.144 57.698 1.00 88.44 C
ANISOU 1306 CG2 THR A 195 15687 10393 7521 108 1052 1395 C
ATOM 1307 N ASN A 196 -0.614 -2.146 60.767 1.00 88.83 N
ANISOU 1307 N ASN A 196 16891 10221 6641 239 1339 2273 N
ATOM 1308 CA ASN A 196 -0.278 -3.475 61.245 1.00 89.19 C
ANISOU 1308 CA ASN A 196 17258 10088 6541 326 1329 2603 C
ATOM 1309 C ASN A 196 0.466 -4.247 60.158 1.00 88.52 C
ANISOU 1309 C ASN A 196 17041 9789 6804 408 1126 2661 C
ATOM 1310 O ASN A 196 0.452 -3.883 58.979 1.00 87.64 O
ANISOU 1310 O ASN A 196 16579 9653 7069 330 1075 2455 O
ATOM 1311 CB ASN A 196 -1.536 -4.223 61.704 1.00 88.63 C
ANISOU 1311 CB ASN A 196 17268 9906 6502 125 1750 2748 C
ATOM 1312 CG ASN A 196 -2.572 -4.385 60.602 1.00 87.81 C
ANISOU 1312 CG ASN A 196 16941 9652 6772 -133 2039 2694 C
ATOM 1313 OD1 ASN A 196 -2.332 -4.046 59.450 1.00 86.97 O
ANISOU 1313 OD1 ASN A 196 16540 9521 6984 -151 1890 2520 O
ATOM 1314 ND2 ASN A 196 -3.739 -4.908 60.964 1.00 88.64 N
ANISOU 1314 ND2 ASN A 196 17051 9706 6921 -347 2409 2789 N
ATOM 1315 N GLN A 197 1.137 -5.322 60.573 1.00 88.14 N
ANISOU 1315 N GLN A 197 17207 9603 6678 580 1002 2910 N
ATOM 1316 CA GLN A 197 1.995 -6.046 59.641 1.00 87.83 C
ANISOU 1316 CA GLN A 197 17107 9353 6910 729 810 2979 C
ATOM 1317 C GLN A 197 1.197 -6.684 58.512 1.00 86.81 C
ANISOU 1317 C GLN A 197 16895 8926 7164 503 1081 2959 C
ATOM 1318 O GLN A 197 1.697 -6.790 57.388 1.00 86.22 O
ANISOU 1318 O GLN A 197 16587 8755 7416 541 947 2833 O
ATOM 1319 CB GLN A 197 2.811 -7.099 60.388 1.00 92.57 C
ANISOU 1319 CB GLN A 197 17903 9875 7393 980 649 3239 C
ATOM 1320 CG GLN A 197 3.837 -6.500 61.331 1.00 94.39 C
ANISOU 1320 CG GLN A 197 18156 10429 7277 1218 285 3251 C
ATOM 1321 CD GLN A 197 4.666 -7.549 62.037 1.00 98.71 C
ANISOU 1321 CD GLN A 197 18864 10923 7717 1485 108 3535 C
ATOM 1322 OE1 GLN A 197 4.437 -8.749 61.880 1.00100.53 O
ANISOU 1322 OE1 GLN A 197 19231 10841 8123 1500 287 3727 O
ATOM 1323 NE2 GLN A 197 5.641 -7.103 62.820 1.00100.79 N
ANISOU 1323 NE2 GLN A 197 19111 11494 7692 1690 -251 3559 N
ATOM 1324 N ALA A 198 -0.043 -7.100 58.784 1.00 84.53 N
ANISOU 1324 N ALA A 198 16667 8545 6906 239 1440 3011 N
ATOM 1325 CA ALA A 198 -0.857 -7.724 57.746 1.00 83.86 C
ANISOU 1325 CA ALA A 198 16484 8204 7173 -30 1680 2974 C
ATOM 1326 C ALA A 198 -1.146 -6.752 56.608 1.00 82.95 C
ANISOU 1326 C ALA A 198 15954 8234 7328 -167 1634 2668 C
ATOM 1327 O ALA A 198 -1.071 -7.124 55.431 1.00 82.28 O
ANISOU 1327 O ALA A 198 15709 7988 7566 -247 1597 2566 O
ATOM 1328 CB ALA A 198 -2.158 -8.251 58.347 1.00 83.44 C
ANISOU 1328 CB ALA A 198 16500 8101 7101 -308 2052 3068 C
ATOM 1329 N TYR A 199 -1.485 -5.504 56.938 1.00 83.53 N
ANISOU 1329 N TYR A 199 15827 8620 7290 -189 1629 2496 N
ATOM 1330 CA TYR A 199 -1.747 -4.512 55.900 1.00 82.85 C
ANISOU 1330 CA TYR A 199 15315 8688 7476 -285 1565 2207 C
ATOM 1331 C TYR A 199 -0.486 -4.208 55.102 1.00 82.25 C
ANISOU 1331 C TYR A 199 15079 8629 7544 -88 1212 2074 C
ATOM 1332 O TYR A 199 -0.512 -4.189 53.867 1.00 81.49 O
ANISOU 1332 O TYR A 199 14739 8472 7753 -176 1170 1933 O
ATOM 1333 CB TYR A 199 -2.305 -3.231 56.519 1.00 84.36 C
ANISOU 1333 CB TYR A 199 15384 9168 7502 -300 1650 2066 C
ATOM 1334 CG TYR A 199 -2.613 -2.150 55.511 1.00 83.93 C
ANISOU 1334 CG TYR A 199 14919 9256 7714 -366 1596 1799 C
ATOM 1335 CD1 TYR A 199 -3.767 -2.196 54.744 1.00 83.97 C
ANISOU 1335 CD1 TYR A 199 14668 9255 7981 -598 1808 1745 C
ATOM 1336 CD2 TYR A 199 -1.740 -1.089 55.317 1.00 83.72 C
ANISOU 1336 CD2 TYR A 199 14762 9374 7675 -204 1324 1615 C
ATOM 1337 CE1 TYR A 199 -4.047 -1.209 53.820 1.00 83.81 C
ANISOU 1337 CE1 TYR A 199 14289 9372 8185 -626 1742 1535 C
ATOM 1338 CE2 TYR A 199 -2.012 -0.098 54.396 1.00 83.44 C
ANISOU 1338 CE2 TYR A 199 14393 9437 7873 -253 1288 1401 C
ATOM 1339 CZ TYR A 199 -3.168 -0.163 53.650 1.00 83.48 C
ANISOU 1339 CZ TYR A 199 14164 9435 8119 -444 1493 1373 C
ATOM 1340 OH TYR A 199 -3.445 0.821 52.729 1.00 83.45 O
ANISOU 1340 OH TYR A 199 13842 9536 8330 -462 1441 1194 O
ATOM 1341 N ALA A 200 0.631 -3.970 55.795 1.00 81.87 N
ANISOU 1341 N ALA A 200 15156 8683 7266 168 956 2121 N
ATOM 1342 CA ALA A 200 1.874 -3.629 55.109 1.00 81.74 C
ANISOU 1342 CA ALA A 200 14945 8725 7387 349 632 1999 C
ATOM 1343 C ALA A 200 2.286 -4.706 54.114 1.00 81.33 C
ANISOU 1343 C ALA A 200 14890 8404 7606 389 616 2062 C
ATOM 1344 O ALA A 200 2.880 -4.394 53.075 1.00 80.93 O
ANISOU 1344 O ALA A 200 14586 8376 7786 429 470 1900 O
ATOM 1345 CB ALA A 200 2.987 -3.387 56.127 1.00 83.63 C
ANISOU 1345 CB ALA A 200 15323 9132 7319 601 353 2078 C
ATOM 1346 N ILE A 201 1.978 -5.970 54.402 1.00 80.12 N
ANISOU 1346 N ILE A 201 15042 7977 7422 374 788 2291 N
ATOM 1347 CA ILE A 201 2.267 -7.042 53.453 1.00 79.84 C
ANISOU 1347 CA ILE A 201 15061 7629 7645 394 823 2330 C
ATOM 1348 C ILE A 201 1.240 -7.050 52.327 1.00 78.83 C
ANISOU 1348 C ILE A 201 14749 7414 7790 63 1018 2152 C
ATOM 1349 O ILE A 201 1.585 -6.912 51.148 1.00 78.27 O
ANISOU 1349 O ILE A 201 14464 7323 7952 53 929 1973 O
ATOM 1350 CB ILE A 201 2.315 -8.404 54.169 1.00 79.90 C
ANISOU 1350 CB ILE A 201 15508 7324 7526 495 949 2646 C
ATOM 1351 CG1 ILE A 201 3.325 -8.386 55.320 1.00 81.11 C
ANISOU 1351 CG1 ILE A 201 15840 7609 7372 845 717 2850 C
ATOM 1352 CG2 ILE A 201 2.647 -9.512 53.178 1.00 79.79 C
ANISOU 1352 CG2 ILE A 201 15592 6938 7785 533 1005 2662 C
ATOM 1353 CD1 ILE A 201 4.742 -8.099 54.909 1.00 81.72 C
ANISOU 1353 CD1 ILE A 201 15697 7817 7536 1159 379 2778 C
ATOM 1354 N ALA A 202 -0.041 -7.201 52.680 1.00 79.24 N
ANISOU 1354 N ALA A 202 14869 7438 7800 -217 1286 2201 N
ATOM 1355 CA ALA A 202 -1.085 -7.369 51.672 1.00 78.74 C
ANISOU 1355 CA ALA A 202 14633 7300 7985 -557 1461 2063 C
ATOM 1356 C ALA A 202 -1.202 -6.147 50.768 1.00 78.07 C
ANISOU 1356 C ALA A 202 14128 7490 8046 -609 1329 1798 C
ATOM 1357 O ALA A 202 -1.469 -6.280 49.568 1.00 77.58 O
ANISOU 1357 O ALA A 202 13899 7369 8209 -773 1328 1651 O
ATOM 1358 CB ALA A 202 -2.423 -7.664 52.348 1.00 78.65 C
ANISOU 1358 CB ALA A 202 14715 7273 7895 -844 1771 2180 C
ATOM 1359 N SER A 203 -1.015 -4.948 51.323 1.00 77.61 N
ANISOU 1359 N SER A 203 13922 7719 7847 -478 1221 1734 N
ATOM 1360 CA SER A 203 -1.092 -3.743 50.502 1.00 77.11 C
ANISOU 1360 CA SER A 203 13499 7880 7918 -506 1108 1506 C
ATOM 1361 C SER A 203 0.065 -3.680 49.513 1.00 76.47 C
ANISOU 1361 C SER A 203 13316 7759 7979 -358 876 1393 C
ATOM 1362 O SER A 203 -0.135 -3.398 48.326 1.00 75.84 O
ANISOU 1362 O SER A 203 13017 7706 8093 -471 847 1241 O
ATOM 1363 CB SER A 203 -1.112 -2.498 51.388 1.00 79.44 C
ANISOU 1363 CB SER A 203 13724 8434 8023 -399 1069 1456 C
ATOM 1364 OG SER A 203 -1.146 -1.317 50.607 1.00 79.11 O
ANISOU 1364 OG SER A 203 13376 8564 8119 -408 970 1255 O
ATOM 1365 N SER A 204 1.288 -3.937 49.985 1.00 75.50 N
ANISOU 1365 N SER A 204 13338 7595 7753 -96 711 1476 N
ATOM 1366 CA SER A 204 2.449 -3.886 49.102 1.00 75.41 C
ANISOU 1366 CA SER A 204 13200 7570 7883 64 518 1379 C
ATOM 1367 C SER A 204 2.371 -4.954 48.020 1.00 75.00 C
ANISOU 1367 C SER A 204 13216 7251 8031 -22 615 1359 C
ATOM 1368 O SER A 204 2.703 -4.696 46.857 1.00 74.56 O
ANISOU 1368 O SER A 204 12975 7215 8137 -42 552 1199 O
ATOM 1369 CB SER A 204 3.735 -4.046 49.912 1.00 76.04 C
ANISOU 1369 CB SER A 204 13392 7685 7816 371 322 1499 C
ATOM 1370 OG SER A 204 3.915 -2.961 50.805 1.00 76.59 O
ANISOU 1370 OG SER A 204 13393 8018 7688 422 196 1464 O
ATOM 1371 N ILE A 205 1.936 -6.161 48.382 1.00 75.82 N
ANISOU 1371 N ILE A 205 13613 7086 8110 -86 783 1516 N
ATOM 1372 CA ILE A 205 1.871 -7.251 47.413 1.00 75.67 C
ANISOU 1372 CA ILE A 205 13725 6761 8266 -183 891 1480 C
ATOM 1373 C ILE A 205 0.784 -6.980 46.380 1.00 74.93 C
ANISOU 1373 C ILE A 205 13438 6722 8309 -534 982 1295 C
ATOM 1374 O ILE A 205 1.055 -6.885 45.179 1.00 74.52 O
ANISOU 1374 O ILE A 205 13256 6666 8390 -570 922 1123 O
ATOM 1375 CB ILE A 205 1.648 -8.596 48.126 1.00 75.22 C
ANISOU 1375 CB ILE A 205 14074 6361 8146 -186 1066 1704 C
ATOM 1376 CG1 ILE A 205 2.808 -8.899 49.078 1.00 76.22 C
ANISOU 1376 CG1 ILE A 205 14387 6446 8126 213 937 1913 C
ATOM 1377 CG2 ILE A 205 1.478 -9.714 47.112 1.00 75.18 C
ANISOU 1377 CG2 ILE A 205 14246 5996 8324 -335 1206 1632 C
ATOM 1378 CD1 ILE A 205 4.151 -9.009 48.395 1.00 76.77 C
ANISOU 1378 CD1 ILE A 205 14366 6485 8319 523 770 1848 C
ATOM 1379 N VAL A 206 -0.462 -6.838 46.837 1.00 74.96 N
ANISOU 1379 N VAL A 206 13406 6805 8268 -792 1125 1336 N
ATOM 1380 CA VAL A 206 -1.588 -6.746 45.912 1.00 74.84 C
ANISOU 1380 CA VAL A 206 13199 6853 8386 -1139 1205 1193 C
ATOM 1381 C VAL A 206 -1.511 -5.471 45.080 1.00 74.29 C
ANISOU 1381 C VAL A 206 12770 7081 8375 -1109 1040 1014 C
ATOM 1382 O VAL A 206 -1.715 -5.500 43.860 1.00 74.06 O
ANISOU 1382 O VAL A 206 12620 7057 8461 -1261 998 863 O
ATOM 1383 CB VAL A 206 -2.919 -6.840 46.680 1.00 72.45 C
ANISOU 1383 CB VAL A 206 12882 6610 8034 -1398 1408 1297 C
ATOM 1384 CG1 VAL A 206 -4.093 -6.613 45.741 1.00 72.89 C
ANISOU 1384 CG1 VAL A 206 12649 6813 8233 -1743 1448 1155 C
ATOM 1385 CG2 VAL A 206 -3.038 -8.192 47.364 1.00 73.00 C
ANISOU 1385 CG2 VAL A 206 13345 6336 8056 -1479 1601 1484 C
ATOM 1386 N SER A 207 -1.207 -4.339 45.711 1.00 73.98 N
ANISOU 1386 N SER A 207 12588 7279 8244 -921 946 1027 N
ATOM 1387 CA SER A 207 -1.322 -3.056 45.030 1.00 73.65 C
ANISOU 1387 CA SER A 207 12231 7496 8258 -917 830 883 C
ATOM 1388 C SER A 207 -0.046 -2.611 44.326 1.00 72.96 C
ANISOU 1388 C SER A 207 12082 7430 8210 -717 649 784 C
ATOM 1389 O SER A 207 -0.131 -1.818 43.382 1.00 72.58 O
ANISOU 1389 O SER A 207 11818 7523 8237 -763 572 662 O
ATOM 1390 CB SER A 207 -1.758 -1.969 46.019 1.00 75.09 C
ANISOU 1390 CB SER A 207 12301 7899 8333 -848 858 920 C
ATOM 1391 OG SER A 207 -3.059 -2.230 46.515 1.00 76.12 O
ANISOU 1391 OG SER A 207 12409 8064 8451 -1048 1057 996 O
ATOM 1392 N PHE A 208 1.128 -3.082 44.750 1.00 70.59 N
ANISOU 1392 N PHE A 208 11949 7010 7863 -492 582 846 N
ATOM 1393 CA PHE A 208 2.373 -2.660 44.113 1.00 70.59 C
ANISOU 1393 CA PHE A 208 11842 7060 7917 -308 431 756 C
ATOM 1394 C PHE A 208 3.135 -3.807 43.462 1.00 70.97 C
ANISOU 1394 C PHE A 208 12047 6872 8048 -217 456 750 C
ATOM 1395 O PHE A 208 3.442 -3.726 42.268 1.00 70.77 O
ANISOU 1395 O PHE A 208 11925 6845 8118 -250 440 616 O
ATOM 1396 CB PHE A 208 3.277 -1.940 45.120 1.00 67.43 C
ANISOU 1396 CB PHE A 208 11408 6806 7406 -84 291 807 C
ATOM 1397 CG PHE A 208 4.596 -1.518 44.542 1.00 68.17 C
ANISOU 1397 CG PHE A 208 11355 6976 7572 82 143 725 C
ATOM 1398 CD1 PHE A 208 4.678 -0.434 43.686 1.00 67.77 C
ANISOU 1398 CD1 PHE A 208 11077 7074 7598 9 91 585 C
ATOM 1399 CD2 PHE A 208 5.753 -2.219 44.841 1.00 69.64 C
ANISOU 1399 CD2 PHE A 208 11619 7085 7757 319 69 805 C
ATOM 1400 CE1 PHE A 208 5.890 -0.050 43.145 1.00 68.97 C
ANISOU 1400 CE1 PHE A 208 11083 7301 7823 130 -13 517 C
ATOM 1401 CE2 PHE A 208 6.968 -1.840 44.305 1.00 71.08 C
ANISOU 1401 CE2 PHE A 208 11613 7368 8025 464 -47 732 C
ATOM 1402 CZ PHE A 208 7.037 -0.754 43.456 1.00 70.86 C
ANISOU 1402 CZ PHE A 208 11359 7492 8073 350 -78 583 C
ATOM 1403 N TYR A 209 3.457 -4.873 44.199 1.00 69.66 N
ANISOU 1403 N TYR A 209 12138 6491 7837 -88 511 897 N
ATOM 1404 CA TYR A 209 4.400 -5.856 43.672 1.00 70.47 C
ANISOU 1404 CA TYR A 209 12386 6362 8026 93 533 899 C
ATOM 1405 C TYR A 209 3.793 -6.685 42.547 1.00 69.98 C
ANISOU 1405 C TYR A 209 12455 6068 8065 -131 684 779 C
ATOM 1406 O TYR A 209 4.473 -6.979 41.558 1.00 70.37 O
ANISOU 1406 O TYR A 209 12507 6028 8203 -47 698 661 O
ATOM 1407 CB TYR A 209 4.919 -6.759 44.792 1.00 70.99 C
ANISOU 1407 CB TYR A 209 12713 6246 8014 334 544 1119 C
ATOM 1408 CG TYR A 209 5.939 -6.098 45.696 1.00 72.15 C
ANISOU 1408 CG TYR A 209 12728 6624 8060 619 341 1212 C
ATOM 1409 CD1 TYR A 209 7.253 -5.925 45.275 1.00 73.58 C
ANISOU 1409 CD1 TYR A 209 12734 6895 8328 876 212 1167 C
ATOM 1410 CD2 TYR A 209 5.601 -5.671 46.974 1.00 72.18 C
ANISOU 1410 CD2 TYR A 209 12781 6771 7871 618 282 1339 C
ATOM 1411 CE1 TYR A 209 8.194 -5.329 46.091 1.00 75.09 C
ANISOU 1411 CE1 TYR A 209 12771 7328 8430 1097 -1 1242 C
ATOM 1412 CE2 TYR A 209 6.538 -5.074 47.800 1.00 73.46 C
ANISOU 1412 CE2 TYR A 209 12838 7160 7911 845 69 1401 C
ATOM 1413 CZ TYR A 209 7.832 -4.906 47.352 1.00 74.94 C
ANISOU 1413 CZ TYR A 209 12824 7448 8202 1072 -88 1352 C
ATOM 1414 OH TYR A 209 8.767 -4.316 48.168 1.00 76.58 O
ANISOU 1414 OH TYR A 209 12894 7912 8292 1260 -327 1404 O
ATOM 1415 N VAL A 210 2.523 -7.072 42.672 1.00 70.49 N
ANISOU 1415 N VAL A 210 12627 6045 8112 -433 805 795 N
ATOM 1416 CA VAL A 210 1.890 -7.869 41.618 1.00 70.36 C
ANISOU 1416 CA VAL A 210 12739 5821 8175 -706 925 659 C
ATOM 1417 C VAL A 210 1.846 -7.120 40.291 1.00 69.88 C
ANISOU 1417 C VAL A 210 12436 5963 8152 -822 840 447 C
ATOM 1418 O VAL A 210 2.324 -7.667 39.283 1.00 70.18 O
ANISOU 1418 O VAL A 210 12587 5841 8236 -810 883 311 O
ATOM 1419 CB VAL A 210 0.507 -8.366 42.079 1.00 71.40 C
ANISOU 1419 CB VAL A 210 12976 5865 8287 -1048 1060 725 C
ATOM 1420 CG1 VAL A 210 -0.221 -9.036 40.925 1.00 71.52 C
ANISOU 1420 CG1 VAL A 210 13071 5730 8374 -1399 1141 546 C
ATOM 1421 CG2 VAL A 210 0.662 -9.343 43.234 1.00 72.01 C
ANISOU 1421 CG2 VAL A 210 13389 5655 8316 -933 1185 945 C
ATOM 1422 N PRO A 211 1.330 -5.885 40.207 1.00 72.13 N
ANISOU 1422 N PRO A 211 12417 6581 8409 -913 734 415 N
ATOM 1423 CA PRO A 211 1.390 -5.181 38.916 1.00 71.83 C
ANISOU 1423 CA PRO A 211 12185 6720 8388 -987 650 247 C
ATOM 1424 C PRO A 211 2.806 -4.829 38.491 1.00 72.07 C
ANISOU 1424 C PRO A 211 12165 6780 8439 -701 593 199 C
ATOM 1425 O PRO A 211 3.070 -4.751 37.286 1.00 72.17 O
ANISOU 1425 O PRO A 211 12149 6816 8457 -748 592 55 O
ATOM 1426 CB PRO A 211 0.540 -3.927 39.155 1.00 71.04 C
ANISOU 1426 CB PRO A 211 11796 6935 8260 -1086 564 277 C
ATOM 1427 CG PRO A 211 0.619 -3.697 40.613 1.00 71.07 C
ANISOU 1427 CG PRO A 211 11817 6962 8222 -936 579 434 C
ATOM 1428 CD PRO A 211 0.678 -5.058 41.242 1.00 71.54 C
ANISOU 1428 CD PRO A 211 12184 6722 8276 -934 704 530 C
ATOM 1429 N LEU A 212 3.721 -4.609 39.440 1.00 69.33 N
ANISOU 1429 N LEU A 212 11794 6457 8091 -421 544 316 N
ATOM 1430 CA LEU A 212 5.113 -4.344 39.088 1.00 70.36 C
ANISOU 1430 CA LEU A 212 11831 6636 8266 -159 496 279 C
ATOM 1431 C LEU A 212 5.744 -5.550 38.404 1.00 71.37 C
ANISOU 1431 C LEU A 212 12175 6488 8453 -51 624 215 C
ATOM 1432 O LEU A 212 6.329 -5.431 37.321 1.00 71.98 O
ANISOU 1432 O LEU A 212 12193 6594 8561 -15 661 81 O
ATOM 1433 CB LEU A 212 5.911 -3.967 40.337 1.00 67.75 C
ANISOU 1433 CB LEU A 212 11424 6405 7913 95 389 422 C
ATOM 1434 CG LEU A 212 7.378 -3.594 40.104 1.00 69.69 C
ANISOU 1434 CG LEU A 212 11493 6764 8221 352 314 397 C
ATOM 1435 CD1 LEU A 212 7.482 -2.304 39.310 1.00 69.51 C
ANISOU 1435 CD1 LEU A 212 11214 6982 8215 238 256 278 C
ATOM 1436 CD2 LEU A 212 8.152 -3.492 41.410 1.00 71.23 C
ANISOU 1436 CD2 LEU A 212 11642 7045 8376 593 183 547 C
ATOM 1437 N VAL A 213 5.644 -6.724 39.034 1.00 72.11 N
ANISOU 1437 N VAL A 213 12549 6292 8558 12 719 313 N
ATOM 1438 CA VAL A 213 6.227 -7.933 38.458 1.00 73.12 C
ANISOU 1438 CA VAL A 213 12935 6094 8752 146 872 256 C
ATOM 1439 C VAL A 213 5.589 -8.241 37.110 1.00 72.56 C
ANISOU 1439 C VAL A 213 12975 5928 8666 -148 972 34 C
ATOM 1440 O VAL A 213 6.270 -8.662 36.166 1.00 73.43 O
ANISOU 1440 O VAL A 213 13177 5916 8808 -43 1077 -105 O
ATOM 1441 CB VAL A 213 6.093 -9.110 39.441 1.00 67.15 C
ANISOU 1441 CB VAL A 213 12505 5005 8004 244 965 429 C
ATOM 1442 CG1 VAL A 213 6.552 -10.405 38.793 1.00 68.06 C
ANISOU 1442 CG1 VAL A 213 12947 4714 8199 364 1157 354 C
ATOM 1443 CG2 VAL A 213 6.905 -8.836 40.695 1.00 68.09 C
ANISOU 1443 CG2 VAL A 213 12524 5247 8101 581 838 650 C
ATOM 1444 N ILE A 214 4.277 -8.025 36.990 1.00 72.86 N
ANISOU 1444 N ILE A 214 12996 6042 8644 -518 941 -8 N
ATOM 1445 CA ILE A 214 3.619 -8.193 35.697 1.00 72.63 C
ANISOU 1445 CA ILE A 214 13030 6000 8567 -828 978 -221 C
ATOM 1446 C ILE A 214 4.150 -7.171 34.699 1.00 72.72 C
ANISOU 1446 C ILE A 214 12800 6295 8535 -772 899 -334 C
ATOM 1447 O ILE A 214 4.507 -7.513 33.567 1.00 73.33 O
ANISOU 1447 O ILE A 214 12999 6292 8572 -795 983 -509 O
ATOM 1448 CB ILE A 214 2.091 -8.099 35.848 1.00 70.61 C
ANISOU 1448 CB ILE A 214 12726 5835 8268 -1228 929 -216 C
ATOM 1449 CG1 ILE A 214 1.569 -9.264 36.691 1.00 70.87 C
ANISOU 1449 CG1 ILE A 214 13049 5536 8342 -1338 1060 -118 C
ATOM 1450 CG2 ILE A 214 1.421 -8.095 34.484 1.00 70.76 C
ANISOU 1450 CG2 ILE A 214 12744 5934 8208 -1552 898 -431 C
ATOM 1451 CD1 ILE A 214 0.121 -9.118 37.103 1.00 70.67 C
ANISOU 1451 CD1 ILE A 214 12912 5640 8300 -1704 1034 -68 C
ATOM 1452 N MET A 215 4.216 -5.901 35.109 1.00 70.42 N
ANISOU 1452 N MET A 215 12196 6322 8239 -702 756 -237 N
ATOM 1453 CA MET A 215 4.723 -4.850 34.229 1.00 70.63 C
ANISOU 1453 CA MET A 215 12005 6603 8228 -659 694 -312 C
ATOM 1454 C MET A 215 6.122 -5.173 33.721 1.00 72.15 C
ANISOU 1454 C MET A 215 12244 6704 8466 -389 807 -377 C
ATOM 1455 O MET A 215 6.383 -5.138 32.514 1.00 72.74 O
ANISOU 1455 O MET A 215 12355 6807 8477 -440 878 -526 O
ATOM 1456 CB MET A 215 4.738 -3.509 34.962 1.00 70.59 C
ANISOU 1456 CB MET A 215 11708 6876 8239 -587 552 -184 C
ATOM 1457 CG MET A 215 5.209 -2.349 34.107 1.00 70.87 C
ANISOU 1457 CG MET A 215 11539 7146 8244 -569 500 -235 C
ATOM 1458 SD MET A 215 5.370 -0.825 35.052 1.00 70.32 S
ANISOU 1458 SD MET A 215 11189 7319 8210 -476 361 -105 S
ATOM 1459 CE MET A 215 6.883 -1.148 35.951 1.00 72.25 C
ANISOU 1459 CE MET A 215 11402 7501 8549 -162 373 -42 C
ATOM 1460 N VAL A 216 7.041 -5.482 34.638 1.00 73.02 N
ANISOU 1460 N VAL A 216 12341 6726 8676 -87 827 -260 N
ATOM 1461 CA VAL A 216 8.431 -5.697 34.253 1.00 75.07 C
ANISOU 1461 CA VAL A 216 12558 6955 9011 213 930 -296 C
ATOM 1462 C VAL A 216 8.575 -6.945 33.389 1.00 75.63 C
ANISOU 1462 C VAL A 216 12948 6711 9076 237 1142 -448 C
ATOM 1463 O VAL A 216 9.401 -6.976 32.470 1.00 76.98 O
ANISOU 1463 O VAL A 216 13099 6898 9253 364 1274 -567 O
ATOM 1464 CB VAL A 216 9.316 -5.761 35.512 1.00 73.79 C
ANISOU 1464 CB VAL A 216 12279 6805 8951 537 861 -114 C
ATOM 1465 CG1 VAL A 216 10.757 -6.078 35.145 1.00 76.38 C
ANISOU 1465 CG1 VAL A 216 12515 7118 9387 875 971 -137 C
ATOM 1466 CG2 VAL A 216 9.239 -4.445 36.274 1.00 73.52 C
ANISOU 1466 CG2 VAL A 216 11954 7085 8897 487 659 -13 C
ATOM 1467 N PHE A 217 7.771 -7.981 33.641 1.00 77.06 N
ANISOU 1467 N PHE A 217 13445 6593 9242 98 1203 -459 N
ATOM 1468 CA PHE A 217 7.879 -9.191 32.831 1.00 77.65 C
ANISOU 1468 CA PHE A 217 13880 6316 9306 97 1419 -630 C
ATOM 1469 C PHE A 217 7.179 -9.042 31.484 1.00 77.09 C
ANISOU 1469 C PHE A 217 13902 6313 9077 -255 1442 -865 C
ATOM 1470 O PHE A 217 7.702 -9.495 30.460 1.00 78.01 O
ANISOU 1470 O PHE A 217 14192 6306 9143 -198 1616 -1052 O
ATOM 1471 CB PHE A 217 7.317 -10.396 33.586 1.00 82.86 C
ANISOU 1471 CB PHE A 217 14886 6584 10013 53 1494 -558 C
ATOM 1472 CG PHE A 217 7.363 -11.672 32.795 1.00 83.46 C
ANISOU 1472 CG PHE A 217 15392 6235 10083 23 1731 -751 C
ATOM 1473 CD1 PHE A 217 8.561 -12.339 32.598 1.00 85.01 C
ANISOU 1473 CD1 PHE A 217 15720 6201 10377 434 1927 -775 C
ATOM 1474 CD2 PHE A 217 6.210 -12.198 32.234 1.00 82.68 C
ANISOU 1474 CD2 PHE A 217 15561 5970 9883 -419 1762 -922 C
ATOM 1475 CE1 PHE A 217 8.608 -13.510 31.862 1.00 85.55 C
ANISOU 1475 CE1 PHE A 217 16229 5839 10438 423 2177 -974 C
ATOM 1476 CE2 PHE A 217 6.251 -13.367 31.498 1.00 83.33 C
ANISOU 1476 CE2 PHE A 217 16083 5634 9945 -480 1985 -1134 C
ATOM 1477 CZ PHE A 217 7.450 -14.025 31.312 1.00 84.67 C
ANISOU 1477 CZ PHE A 217 16429 5534 10208 -50 2206 -1166 C
ATOM 1478 N VAL A 218 5.999 -8.417 31.462 1.00 75.79 N
ANISOU 1478 N VAL A 218 13624 6355 8818 -606 1270 -857 N
ATOM 1479 CA VAL A 218 5.258 -8.285 30.210 1.00 75.58 C
ANISOU 1479 CA VAL A 218 13673 6429 8615 -948 1243 -1058 C
ATOM 1480 C VAL A 218 5.919 -7.269 29.287 1.00 76.19 C
ANISOU 1480 C VAL A 218 13544 6804 8601 -858 1228 -1110 C
ATOM 1481 O VAL A 218 5.909 -7.440 28.062 1.00 76.74 O
ANISOU 1481 O VAL A 218 13774 6876 8509 -991 1304 -1307 O
ATOM 1482 CB VAL A 218 3.786 -7.923 30.492 1.00 73.82 C
ANISOU 1482 CB VAL A 218 13341 6371 8339 -1319 1053 -1006 C
ATOM 1483 CG1 VAL A 218 3.047 -7.599 29.204 1.00 74.05 C
ANISOU 1483 CG1 VAL A 218 13370 6597 8168 -1647 960 -1180 C
ATOM 1484 CG2 VAL A 218 3.090 -9.069 31.212 1.00 73.59 C
ANISOU 1484 CG2 VAL A 218 13566 6016 8380 -1481 1120 -987 C
ATOM 1485 N TYR A 219 6.511 -6.208 29.836 1.00 74.62 N
ANISOU 1485 N TYR A 219 13014 6852 8488 -653 1141 -943 N
ATOM 1486 CA TYR A 219 7.079 -5.181 28.971 1.00 75.38 C
ANISOU 1486 CA TYR A 219 12921 7220 8502 -613 1140 -973 C
ATOM 1487 C TYR A 219 8.505 -5.497 28.543 1.00 77.22 C
ANISOU 1487 C TYR A 219 13176 7372 8793 -311 1362 -1041 C
ATOM 1488 O TYR A 219 8.942 -5.014 27.490 1.00 78.12 O
ANISOU 1488 O TYR A 219 13255 7635 8791 -327 1449 -1131 O
ATOM 1489 CB TYR A 219 7.042 -3.808 29.649 1.00 71.35 C
ANISOU 1489 CB TYR A 219 12057 6999 8053 -580 960 -786 C
ATOM 1490 CG TYR A 219 7.178 -2.677 28.655 1.00 71.90 C
ANISOU 1490 CG TYR A 219 11984 7336 8001 -659 931 -804 C
ATOM 1491 CD1 TYR A 219 6.092 -2.293 27.878 1.00 71.28 C
ANISOU 1491 CD1 TYR A 219 11947 7394 7741 -937 815 -843 C
ATOM 1492 CD2 TYR A 219 8.384 -2.016 28.466 1.00 73.49 C
ANISOU 1492 CD2 TYR A 219 12006 7655 8261 -465 1022 -770 C
ATOM 1493 CE1 TYR A 219 6.194 -1.275 26.957 1.00 71.99 C
ANISOU 1493 CE1 TYR A 219 11946 7711 7696 -993 788 -828 C
ATOM 1494 CE2 TYR A 219 8.496 -0.993 27.540 1.00 74.14 C
ANISOU 1494 CE2 TYR A 219 11996 7952 8222 -557 1022 -767 C
ATOM 1495 CZ TYR A 219 7.395 -0.628 26.791 1.00 73.27 C
ANISOU 1495 CZ TYR A 219 11973 7952 7915 -809 906 -787 C
ATOM 1496 OH TYR A 219 7.488 0.386 25.869 1.00 74.01 O
ANISOU 1496 OH TYR A 219 12009 8246 7868 -881 904 -751 O
ATOM 1497 N SER A 220 9.242 -6.285 29.331 1.00 78.27 N
ANISOU 1497 N SER A 220 13355 7286 9098 -20 1464 -983 N
ATOM 1498 CA SER A 220 10.467 -6.894 28.824 1.00 80.16 C
ANISOU 1498 CA SER A 220 13665 7392 9398 280 1717 -1076 C
ATOM 1499 C SER A 220 10.171 -7.873 27.700 1.00 80.06 C
ANISOU 1499 C SER A 220 14061 7125 9233 149 1918 -1328 C
ATOM 1500 O SER A 220 11.033 -8.113 26.848 1.00 81.42 O
ANISOU 1500 O SER A 220 14301 7262 9372 316 2155 -1463 O
ATOM 1501 CB SER A 220 11.218 -7.601 29.951 1.00 79.15 C
ANISOU 1501 CB SER A 220 13513 7074 9485 645 1758 -935 C
ATOM 1502 OG SER A 220 10.500 -8.730 30.417 1.00 78.08 O
ANISOU 1502 OG SER A 220 13727 6581 9360 581 1781 -941 O
ATOM 1503 N ARG A 221 8.959 -8.426 27.680 1.00 82.81 N
ANISOU 1503 N ARG A 221 14678 7307 9480 -167 1835 -1404 N
ATOM 1504 CA ARG A 221 8.517 -9.275 26.583 1.00 82.82 C
ANISOU 1504 CA ARG A 221 15083 7090 9295 -388 1979 -1675 C
ATOM 1505 C ARG A 221 8.235 -8.458 25.330 1.00 82.86 C
ANISOU 1505 C ARG A 221 15041 7403 9041 -631 1927 -1801 C
ATOM 1506 O ARG A 221 8.289 -9.001 24.221 1.00 83.43 O
ANISOU 1506 O ARG A 221 15421 7360 8920 -730 2094 -2045 O
ATOM 1507 CB ARG A 221 7.264 -10.042 27.009 1.00 86.07 C
ANISOU 1507 CB ARG A 221 15747 7267 9689 -708 1876 -1706 C
ATOM 1508 CG ARG A 221 6.811 -11.143 26.081 1.00 86.32 C
ANISOU 1508 CG ARG A 221 16254 6985 9560 -957 2026 -2002 C
ATOM 1509 CD ARG A 221 7.750 -12.329 26.170 1.00 87.37 C
ANISOU 1509 CD ARG A 221 16714 6660 9823 -617 2342 -2087 C
ATOM 1510 NE ARG A 221 7.286 -13.450 25.364 1.00 87.64 N
ANISOU 1510 NE ARG A 221 17249 6338 9713 -872 2498 -2382 N
ATOM 1511 CZ ARG A 221 7.560 -13.595 24.074 1.00 88.57 C
ANISOU 1511 CZ ARG A 221 17499 6528 9625 -927 2625 -2610 C
ATOM 1512 NH1 ARG A 221 8.297 -12.687 23.451 1.00 88.94 N
ANISOU 1512 NH1 ARG A 221 17392 6839 9562 -760 2698 -2655 N
ATOM 1513 NH2 ARG A 221 7.099 -14.645 23.409 1.00 92.15 N
ANISOU 1513 NH2 ARG A 221 18247 6792 9973 -1159 2689 -2789 N
ATOM 1514 N VAL A 222 7.948 -7.163 25.487 1.00 79.89 N
ANISOU 1514 N VAL A 222 14313 7400 8642 -719 1708 -1635 N
ATOM 1515 CA VAL A 222 7.697 -6.296 24.339 1.00 80.09 C
ANISOU 1515 CA VAL A 222 14290 7724 8416 -917 1646 -1699 C
ATOM 1516 C VAL A 222 9.001 -5.927 23.645 1.00 81.58 C
ANISOU 1516 C VAL A 222 14408 8010 8580 -667 1884 -1735 C
ATOM 1517 O VAL A 222 9.131 -6.073 22.423 1.00 82.17 O
ANISOU 1517 O VAL A 222 14703 8110 8409 -759 2030 -1920 O
ATOM 1518 CB VAL A 222 6.917 -5.039 24.772 1.00 77.32 C
ANISOU 1518 CB VAL A 222 13613 7696 8068 -1068 1351 -1491 C
ATOM 1519 CG1 VAL A 222 6.768 -4.072 23.608 1.00 77.80 C
ANISOU 1519 CG1 VAL A 222 13626 8057 7876 -1214 1293 -1506 C
ATOM 1520 CG2 VAL A 222 5.558 -5.424 25.330 1.00 76.08 C
ANISOU 1520 CG2 VAL A 222 13507 7480 7920 -1338 1148 -1471 C
ATOM 1521 N PHE A 223 9.978 -5.425 24.409 1.00 79.61 N
ANISOU 1521 N PHE A 223 13841 7838 8568 -367 1926 -1561 N
ATOM 1522 CA PHE A 223 11.292 -5.131 23.842 1.00 81.37 C
ANISOU 1522 CA PHE A 223 13940 8162 8815 -125 2178 -1585 C
ATOM 1523 C PHE A 223 11.884 -6.334 23.123 1.00 82.23 C
ANISOU 1523 C PHE A 223 14378 7999 8867 31 2509 -1819 C
ATOM 1524 O PHE A 223 12.609 -6.174 22.134 1.00 83.32 O
ANISOU 1524 O PHE A 223 14547 8232 8879 103 2754 -1926 O
ATOM 1525 CB PHE A 223 12.264 -4.659 24.929 1.00 77.42 C
ANISOU 1525 CB PHE A 223 13045 7754 8617 172 2158 -1382 C
ATOM 1526 CG PHE A 223 12.075 -3.228 25.348 1.00 77.26 C
ANISOU 1526 CG PHE A 223 12690 8035 8629 50 1929 -1189 C
ATOM 1527 CD1 PHE A 223 11.310 -2.359 24.587 1.00 76.39 C
ANISOU 1527 CD1 PHE A 223 12616 8112 8296 -234 1816 -1184 C
ATOM 1528 CD2 PHE A 223 12.691 -2.745 26.491 1.00 78.22 C
ANISOU 1528 CD2 PHE A 223 12477 8247 8995 231 1827 -1015 C
ATOM 1529 CE1 PHE A 223 11.149 -1.039 24.970 1.00 76.29 C
ANISOU 1529 CE1 PHE A 223 12334 8326 8328 -319 1634 -1004 C
ATOM 1530 CE2 PHE A 223 12.534 -1.428 26.878 1.00 78.24 C
ANISOU 1530 CE2 PHE A 223 12217 8485 9025 108 1639 -866 C
ATOM 1531 CZ PHE A 223 11.762 -0.574 26.117 1.00 77.18 C
ANISOU 1531 CZ PHE A 223 12143 8490 8690 -158 1557 -860 C
ATOM 1532 N GLN A 224 11.591 -7.542 23.602 1.00 86.64 N
ANISOU 1532 N GLN A 224 15207 8202 9512 88 2548 -1899 N
ATOM 1533 CA GLN A 224 12.123 -8.744 22.978 1.00 87.49 C
ANISOU 1533 CA GLN A 224 15678 7981 9581 258 2883 -2132 C
ATOM 1534 C GLN A 224 11.398 -9.094 21.684 1.00 87.02 C
ANISOU 1534 C GLN A 224 16039 7863 9160 -83 2947 -2414 C
ATOM 1535 O GLN A 224 11.978 -9.768 20.825 1.00 87.94 O
ANISOU 1535 O GLN A 224 16447 7806 9162 38 3272 -2643 O
ATOM 1536 CB GLN A 224 12.056 -9.913 23.966 1.00 89.38 C
ANISOU 1536 CB GLN A 224 16104 7814 10043 438 2910 -2103 C
ATOM 1537 CG GLN A 224 12.770 -11.173 23.509 1.00 90.47 C
ANISOU 1537 CG GLN A 224 16605 7554 10216 719 3289 -2308 C
ATOM 1538 CD GLN A 224 12.794 -12.249 24.578 1.00 90.44 C
ANISOU 1538 CD GLN A 224 16772 7134 10457 952 3316 -2215 C
ATOM 1539 OE1 GLN A 224 12.243 -12.074 25.666 1.00 89.52 O
ANISOU 1539 OE1 GLN A 224 16512 7040 10461 875 3050 -2001 O
ATOM 1540 NE2 GLN A 224 13.440 -13.369 24.274 1.00 91.63 N
ANISOU 1540 NE2 GLN A 224 17252 6890 10675 1254 3658 -2368 N
ATOM 1541 N GLU A 225 10.156 -8.639 21.516 1.00 88.43 N
ANISOU 1541 N GLU A 225 16249 8204 9148 -496 2645 -2406 N
ATOM 1542 CA GLU A 225 9.453 -8.871 20.259 1.00 88.28 C
ANISOU 1542 CA GLU A 225 16591 8204 8747 -845 2648 -2663 C
ATOM 1543 C GLU A 225 9.803 -7.815 19.219 1.00 88.87 C
ANISOU 1543 C GLU A 225 16544 8655 8566 -889 2686 -2650 C
ATOM 1544 O GLU A 225 9.910 -8.129 18.029 1.00 89.45 O
ANISOU 1544 O GLU A 225 16946 8715 8325 -990 2870 -2890 O
ATOM 1545 CB GLU A 225 7.944 -8.909 20.494 1.00 92.13 C
ANISOU 1545 CB GLU A 225 17140 8726 9139 -1271 2297 -2657 C
ATOM 1546 CG GLU A 225 7.487 -10.111 21.290 1.00 91.65 C
ANISOU 1546 CG GLU A 225 17315 8248 9259 -1320 2309 -2721 C
ATOM 1547 CD GLU A 225 7.732 -11.414 20.554 1.00 92.48 C
ANISOU 1547 CD GLU A 225 17894 7985 9260 -1327 2583 -3016 C
ATOM 1548 OE1 GLU A 225 7.678 -11.411 19.306 1.00 93.72 O
ANISOU 1548 OE1 GLU A 225 18188 8294 9127 -1486 2621 -3183 O
ATOM 1549 OE2 GLU A 225 7.983 -12.440 21.220 1.00 93.01 O
ANISOU 1549 OE2 GLU A 225 18088 7682 9571 -1145 2718 -2994 O
ATOM 1550 N ALA A 226 9.978 -6.562 19.646 1.00 86.00 N
ANISOU 1550 N ALA A 226 15746 8612 8317 -827 2526 -2375 N
ATOM 1551 CA ALA A 226 10.402 -5.519 18.718 1.00 86.64 C
ANISOU 1551 CA ALA A 226 15716 9019 8183 -851 2595 -2323 C
ATOM 1552 C ALA A 226 11.747 -5.860 18.089 1.00 88.06 C
ANISOU 1552 C ALA A 226 15975 9129 8356 -566 3035 -2453 C
ATOM 1553 O ALA A 226 11.955 -5.643 16.889 1.00 88.58 O
ANISOU 1553 O ALA A 226 16230 9329 8095 -654 3208 -2575 O
ATOM 1554 CB ALA A 226 10.470 -4.173 19.438 1.00 81.67 C
ANISOU 1554 CB ALA A 226 14623 8667 7743 -806 2387 -2005 C
ATOM 1555 N LYS A 227 12.671 -6.406 18.883 1.00 87.80 N
ANISOU 1555 N LYS A 227 15795 8899 8667 -207 3227 -2420 N
ATOM 1556 CA LYS A 227 13.978 -6.778 18.353 1.00 89.34 C
ANISOU 1556 CA LYS A 227 16007 9035 8902 112 3667 -2534 C
ATOM 1557 C LYS A 227 13.893 -8.038 17.502 1.00 89.53 C
ANISOU 1557 C LYS A 227 16577 8740 8699 102 3941 -2879 C
ATOM 1558 O LYS A 227 14.563 -8.140 16.467 1.00 90.86 O
ANISOU 1558 O LYS A 227 16912 8948 8664 188 4293 -3048 O
ATOM 1559 CB LYS A 227 14.969 -6.967 19.500 1.00 92.01 C
ANISOU 1559 CB LYS A 227 15979 9292 9688 522 3749 -2371 C
ATOM 1560 CG LYS A 227 16.390 -7.263 19.057 1.00 93.83 C
ANISOU 1560 CG LYS A 227 16107 9518 10024 899 4199 -2447 C
ATOM 1561 CD LYS A 227 17.325 -7.335 20.251 1.00 95.03 C
ANISOU 1561 CD LYS A 227 15820 9667 10621 1294 4201 -2245 C
ATOM 1562 CE LYS A 227 18.749 -7.637 19.823 1.00 96.97 C
ANISOU 1562 CE LYS A 227 15894 9947 11005 1695 4650 -2307 C
ATOM 1563 NZ LYS A 227 19.668 -7.692 20.993 1.00 98.39 N
ANISOU 1563 NZ LYS A 227 15597 10175 11612 2085 4606 -2094 N
ATOM 1564 N ARG A 228 13.080 -9.013 17.921 1.00 89.72 N
ANISOU 1564 N ARG A 228 16907 8433 8750 -15 3809 -2997 N
ATOM 1565 CA ARG A 228 12.940 -10.235 17.137 1.00 92.59 C
ANISOU 1565 CA ARG A 228 17713 8509 8959 -73 3978 -3267 C
ATOM 1566 C ARG A 228 12.211 -9.964 15.828 1.00 94.31 C
ANISOU 1566 C ARG A 228 18147 8952 8733 -478 3853 -3401 C
ATOM 1567 O ARG A 228 12.529 -10.566 14.796 1.00 98.89 O
ANISOU 1567 O ARG A 228 18963 9473 9137 -469 4060 -3583 O
ATOM 1568 CB ARG A 228 12.184 -11.302 17.931 1.00 96.00 C
ANISOU 1568 CB ARG A 228 18336 8571 9569 -160 3807 -3287 C
ATOM 1569 CG ARG A 228 12.214 -12.678 17.274 1.00101.37 C
ANISOU 1569 CG ARG A 228 19385 8932 10198 -162 3983 -3501 C
ATOM 1570 CD ARG A 228 11.221 -13.641 17.904 1.00101.92 C
ANISOU 1570 CD ARG A 228 19673 8682 10369 -384 3783 -3520 C
ATOM 1571 NE ARG A 228 9.852 -13.245 17.587 1.00100.43 N
ANISOU 1571 NE ARG A 228 19541 8695 9923 -914 3424 -3559 N
ATOM 1572 CZ ARG A 228 9.249 -13.519 16.432 1.00103.71 C
ANISOU 1572 CZ ARG A 228 20201 9193 10011 -1252 3362 -3760 C
ATOM 1573 NH1 ARG A 228 8.003 -13.118 16.218 1.00102.50 N
ANISOU 1573 NH1 ARG A 228 20030 9265 9651 -1706 3005 -3764 N
ATOM 1574 NH2 ARG A 228 9.894 -14.190 15.485 1.00108.59 N
ANISOU 1574 NH2 ARG A 228 21071 9682 10508 -1128 3651 -3957 N
ATOM 1575 N GLN A 229 11.228 -9.069 15.854 1.00 92.25 N
ANISOU 1575 N GLN A 229 17809 8957 8285 -818 3505 -3306 N
ATOM 1576 CA GLN A 229 10.401 -8.774 14.686 1.00 93.90 C
ANISOU 1576 CA GLN A 229 18190 9413 8073 -1202 3307 -3389 C
ATOM 1577 C GLN A 229 10.949 -7.568 13.926 1.00 93.45 C
ANISOU 1577 C GLN A 229 17991 9733 7781 -1166 3410 -3283 C
ATOM 1578 O GLN A 229 10.298 -6.532 13.780 1.00 91.33 O
ANISOU 1578 O GLN A 229 17614 9774 7314 -1391 3140 -3136 O
ATOM 1579 CB GLN A 229 8.954 -8.549 15.113 1.00 91.66 C
ANISOU 1579 CB GLN A 229 17879 9222 7726 -1583 2850 -3323 C
ATOM 1580 CG GLN A 229 8.290 -9.782 15.694 1.00 92.96 C
ANISOU 1580 CG GLN A 229 18212 9034 8076 -1702 2754 -3429 C
ATOM 1581 CD GLN A 229 6.881 -9.513 16.176 1.00 90.72 C
ANISOU 1581 CD GLN A 229 17827 8877 7764 -2077 2324 -3345 C
ATOM 1582 OE1 GLN A 229 6.410 -8.378 16.148 1.00 88.24 O
ANISOU 1582 OE1 GLN A 229 17308 8911 7310 -2212 2081 -3195 O
ATOM 1583 NE2 GLN A 229 6.200 -10.561 16.626 1.00 92.25 N
ANISOU 1583 NE2 GLN A 229 18157 8793 8100 -2244 2240 -3426 N
ATOM 1584 N LEU A 230 12.179 -7.715 13.444 1.00 94.99 N
ANISOU 1584 N LEU A 230 18178 9901 8014 -869 3820 -3338 N
ATOM 1585 CA LEU A 230 12.801 -6.748 12.546 1.00 95.91 C
ANISOU 1585 CA LEU A 230 18202 10344 7894 -844 3996 -3256 C
ATOM 1586 C LEU A 230 13.054 -7.440 11.216 1.00101.66 C
ANISOU 1586 C LEU A 230 19246 11039 8343 -875 4206 -3476 C
ATOM 1587 O LEU A 230 13.926 -8.310 11.118 1.00104.95 O
ANISOU 1587 O LEU A 230 19734 11225 8918 -597 4552 -3619 O
ATOM 1588 CB LEU A 230 14.088 -6.176 13.137 1.00 94.37 C
ANISOU 1588 CB LEU A 230 17651 10209 7996 -482 4322 -3107 C
ATOM 1589 CG LEU A 230 13.858 -5.153 14.249 1.00 88.96 C
ANISOU 1589 CG LEU A 230 16556 9681 7566 -496 4042 -2810 C
ATOM 1590 CD1 LEU A 230 15.158 -4.749 14.898 1.00 88.12 C
ANISOU 1590 CD1 LEU A 230 15978 9640 7866 -143 4274 -2629 C
ATOM 1591 CD2 LEU A 230 13.178 -3.935 13.663 1.00 87.46 C
ANISOU 1591 CD2 LEU A 230 16328 9836 7068 -801 3780 -2635 C
ATOM 2861 N LYS A 263 18.848 -1.065 17.008 1.00 90.64 N
ANISOU 2861 N LYS A 263 14242 10808 9388 359 4498 -1702 N
ATOM 2862 CA LYS A 263 18.089 -0.942 18.247 1.00 89.81 C
ANISOU 2862 CA LYS A 263 14014 10619 9491 310 4044 -1575 C
ATOM 2863 C LYS A 263 17.516 0.459 18.393 1.00 88.90 C
ANISOU 2863 C LYS A 263 13770 10691 9318 18 3755 -1354 C
ATOM 2864 O LYS A 263 18.249 1.451 18.337 1.00 89.63 O
ANISOU 2864 O LYS A 263 13560 10982 9512 -30 3862 -1209 O
ATOM 2865 CB LYS A 263 18.963 -1.269 19.458 1.00 96.50 C
ANISOU 2865 CB LYS A 263 14440 11436 10788 620 4032 -1499 C
ATOM 2866 CG LYS A 263 19.237 -2.742 19.690 1.00 97.02 C
ANISOU 2866 CG LYS A 263 14661 11232 10970 950 4192 -1667 C
ATOM 2867 CD LYS A 263 19.968 -2.928 21.013 1.00 98.41 C
ANISOU 2867 CD LYS A 263 14402 11415 11572 1249 4080 -1528 C
ATOM 2868 CE LYS A 263 20.191 -4.393 21.335 1.00 98.78 C
ANISOU 2868 CE LYS A 263 14628 11154 11751 1612 4217 -1651 C
ATOM 2869 NZ LYS A 263 20.888 -4.572 22.639 1.00100.20 N
ANISOU 2869 NZ LYS A 263 14390 11365 12317 1925 4072 -1481 N
ATOM 2870 N PHE A 264 16.199 0.528 18.582 1.00 85.04 N
ANISOU 2870 N PHE A 264 13507 10126 8676 -177 3402 -1330 N
ATOM 2871 CA PHE A 264 15.501 1.771 18.902 1.00 84.00 C
ANISOU 2871 CA PHE A 264 13265 10121 8528 -400 3091 -1116 C
ATOM 2872 C PHE A 264 15.743 2.843 17.845 1.00 83.89 C
ANISOU 2872 C PHE A 264 13294 10303 8277 -573 3251 -1010 C
ATOM 2873 O PHE A 264 15.756 4.038 18.146 1.00 83.55 O
ANISOU 2873 O PHE A 264 13052 10366 8328 -688 3132 -804 O
ATOM 2874 CB PHE A 264 15.907 2.279 20.287 1.00 82.60 C
ANISOU 2874 CB PHE A 264 12669 9965 8749 -306 2916 -961 C
ATOM 2875 CG PHE A 264 15.692 1.274 21.375 1.00 82.76 C
ANISOU 2875 CG PHE A 264 12660 9802 8983 -127 2759 -1024 C
ATOM 2876 CD1 PHE A 264 14.422 1.015 21.856 1.00 81.19 C
ANISOU 2876 CD1 PHE A 264 12646 9485 8718 -236 2452 -1020 C
ATOM 2877 CD2 PHE A 264 16.764 0.584 21.915 1.00 84.47 C
ANISOU 2877 CD2 PHE A 264 12656 9972 9465 161 2928 -1070 C
ATOM 2878 CE1 PHE A 264 14.224 0.087 22.858 1.00 81.13 C
ANISOU 2878 CE1 PHE A 264 12639 9293 8892 -88 2335 -1058 C
ATOM 2879 CE2 PHE A 264 16.574 -0.344 22.917 1.00 84.53 C
ANISOU 2879 CE2 PHE A 264 12672 9795 9651 344 2788 -1095 C
ATOM 2880 CZ PHE A 264 15.302 -0.593 23.390 1.00 82.76 C
ANISOU 2880 CZ PHE A 264 12670 9431 9345 207 2501 -1088 C
ATOM 2881 N CYS A 265 15.953 2.418 16.602 1.00 85.52 N
ANISOU 2881 N CYS A 265 13791 10539 8164 -594 3540 -1151 N
ATOM 2882 CA CYS A 265 16.118 3.346 15.494 1.00 85.45 C
ANISOU 2882 CA CYS A 265 13899 10709 7859 -764 3712 -1044 C
ATOM 2883 C CYS A 265 14.813 3.629 14.766 1.00 84.13 C
ANISOU 2883 C CYS A 265 14106 10586 7273 -989 3451 -1005 C
ATOM 2884 O CYS A 265 14.698 4.671 14.109 1.00 83.83 O
ANISOU 2884 O CYS A 265 14140 10692 7020 -1141 3459 -819 O
ATOM 2885 CB CYS A 265 17.147 2.802 14.499 1.00 85.07 C
ANISOU 2885 CB CYS A 265 13960 10707 7657 -657 4212 -1208 C
ATOM 2886 SG CYS A 265 18.843 2.702 15.115 1.00 87.02 S
ANISOU 2886 SG CYS A 265 13682 11002 8377 -391 4578 -1205 S
ATOM 2887 N LEU A 266 13.835 2.734 14.865 1.00 81.44 N
ANISOU 2887 N LEU A 266 13998 10132 6814 -1019 3216 -1161 N
ATOM 2888 CA LEU A 266 12.543 2.949 14.234 1.00 80.46 C
ANISOU 2888 CA LEU A 266 14170 10090 6310 -1238 2917 -1126 C
ATOM 2889 C LEU A 266 11.671 3.824 15.127 1.00 79.35 C
ANISOU 2889 C LEU A 266 13809 9980 6363 -1303 2512 -887 C
ATOM 2890 O LEU A 266 11.755 3.757 16.356 1.00 79.14 O
ANISOU 2890 O LEU A 266 13501 9842 6728 -1195 2399 -853 O
ATOM 2891 CB LEU A 266 11.858 1.611 13.957 1.00 80.86 C
ANISOU 2891 CB LEU A 266 14545 10015 6162 -1289 2840 -1414 C
ATOM 2892 CG LEU A 266 10.556 1.644 13.158 1.00 80.28 C
ANISOU 2892 CG LEU A 266 14787 10069 5647 -1543 2535 -1432 C
ATOM 2893 CD1 LEU A 266 10.792 2.205 11.762 1.00 82.24 C
ANISOU 2893 CD1 LEU A 266 15303 10523 5423 -1645 2712 -1387 C
ATOM 2894 CD2 LEU A 266 9.951 0.255 13.083 1.00 80.19 C
ANISOU 2894 CD2 LEU A 266 15055 9893 5521 -1626 2461 -1744 C
ATOM 2895 N LYS A 267 10.841 4.658 14.492 1.00 79.88 N
ANISOU 2895 N LYS A 267 14014 10200 6135 -1459 2304 -714 N
ATOM 2896 CA LYS A 267 10.011 5.611 15.227 1.00 78.88 C
ANISOU 2896 CA LYS A 267 13694 10105 6173 -1491 1959 -468 C
ATOM 2897 C LYS A 267 9.151 4.922 16.279 1.00 78.23 C
ANISOU 2897 C LYS A 267 13495 9914 6314 -1474 1668 -556 C
ATOM 2898 O LYS A 267 9.027 5.410 17.409 1.00 77.64 O
ANISOU 2898 O LYS A 267 13148 9775 6575 -1402 1526 -429 O
ATOM 2899 CB LYS A 267 9.134 6.396 14.248 1.00 82.48 C
ANISOU 2899 CB LYS A 267 14365 10746 6228 -1627 1766 -284 C
ATOM 2900 CG LYS A 267 8.202 7.412 14.900 1.00 81.62 C
ANISOU 2900 CG LYS A 267 14077 10666 6267 -1621 1425 -18 C
ATOM 2901 CD LYS A 267 6.774 6.879 14.987 1.00 81.33 C
ANISOU 2901 CD LYS A 267 14085 10709 6110 -1700 1041 -73 C
ATOM 2902 CE LYS A 267 5.836 7.884 15.639 1.00 80.74 C
ANISOU 2902 CE LYS A 267 13807 10673 6197 -1651 734 193 C
ATOM 2903 NZ LYS A 267 5.682 9.120 14.825 1.00 81.11 N
ANISOU 2903 NZ LYS A 267 13970 10844 6005 -1645 700 486 N
ATOM 2904 N GLU A 268 8.550 3.786 15.927 1.00 77.47 N
ANISOU 2904 N GLU A 268 13622 9788 6025 -1559 1590 -781 N
ATOM 2905 CA GLU A 268 7.665 3.093 16.854 1.00 76.86 C
ANISOU 2905 CA GLU A 268 13461 9607 6137 -1587 1333 -858 C
ATOM 2906 C GLU A 268 8.430 2.376 17.960 1.00 77.00 C
ANISOU 2906 C GLU A 268 13313 9398 6543 -1412 1490 -963 C
ATOM 2907 O GLU A 268 7.862 2.132 19.030 1.00 76.41 O
ANISOU 2907 O GLU A 268 13089 9233 6711 -1394 1297 -937 O
ATOM 2908 CB GLU A 268 6.788 2.104 16.089 1.00 81.02 C
ANISOU 2908 CB GLU A 268 14294 10161 6328 -1785 1205 -1075 C
ATOM 2909 CG GLU A 268 5.793 2.754 15.135 1.00 81.13 C
ANISOU 2909 CG GLU A 268 14431 10443 5952 -1964 938 -952 C
ATOM 2910 CD GLU A 268 6.409 3.094 13.791 1.00 81.89 C
ANISOU 2910 CD GLU A 268 14795 10671 5646 -1993 1153 -954 C
ATOM 2911 OE1 GLU A 268 7.593 2.762 13.578 1.00 82.34 O
ANISOU 2911 OE1 GLU A 268 14935 10613 5739 -1884 1535 -1079 O
ATOM 2912 OE2 GLU A 268 5.712 3.694 12.945 1.00 82.17 O
ANISOU 2912 OE2 GLU A 268 14954 10941 5325 -2112 946 -820 O
ATOM 2913 N HIS A 269 9.697 2.027 17.726 1.00 75.61 N
ANISOU 2913 N HIS A 269 13156 9146 6427 -1269 1840 -1068 N
ATOM 2914 CA HIS A 269 10.528 1.474 18.790 1.00 76.13 C
ANISOU 2914 CA HIS A 269 13017 9035 6873 -1055 1974 -1117 C
ATOM 2915 C HIS A 269 10.985 2.549 19.761 1.00 76.22 C
ANISOU 2915 C HIS A 269 12658 9104 7197 -962 1909 -891 C
ATOM 2916 O HIS A 269 11.140 2.278 20.957 1.00 76.35 O
ANISOU 2916 O HIS A 269 12478 9013 7520 -837 1831 -871 O
ATOM 2917 CB HIS A 269 11.740 0.758 18.196 1.00 78.86 C
ANISOU 2917 CB HIS A 269 13465 9306 7193 -901 2376 -1296 C
ATOM 2918 CG HIS A 269 11.394 -0.507 17.479 1.00 78.82 C
ANISOU 2918 CG HIS A 269 13852 9157 6939 -958 2473 -1571 C
ATOM 2919 ND1 HIS A 269 12.301 -1.200 16.709 1.00 79.85 N
ANISOU 2919 ND1 HIS A 269 14172 9211 6955 -835 2857 -1771 N
ATOM 2920 CD2 HIS A 269 10.237 -1.207 17.421 1.00 77.94 C
ANISOU 2920 CD2 HIS A 269 13985 8956 6674 -1142 2246 -1696 C
ATOM 2921 CE1 HIS A 269 11.717 -2.272 16.203 1.00 79.55 C
ANISOU 2921 CE1 HIS A 269 14521 9015 6691 -941 2863 -2020 C
ATOM 2922 NE2 HIS A 269 10.463 -2.298 16.619 1.00 78.42 N
ANISOU 2922 NE2 HIS A 269 14410 8866 6521 -1149 2484 -1980 N
ATOM 2923 N LYS A 270 11.212 3.765 19.262 1.00 76.03 N
ANISOU 2923 N LYS A 270 12565 9237 7084 -1031 1944 -722 N
ATOM 2924 CA LYS A 270 11.515 4.885 20.142 1.00 75.86 C
ANISOU 2924 CA LYS A 270 12240 9250 7334 -999 1860 -521 C
ATOM 2925 C LYS A 270 10.320 5.224 21.020 1.00 74.52 C
ANISOU 2925 C LYS A 270 12009 9054 7253 -1048 1510 -415 C
ATOM 2926 O LYS A 270 10.492 5.634 22.173 1.00 74.41 O
ANISOU 2926 O LYS A 270 11760 8992 7520 -977 1416 -334 O
ATOM 2927 CB LYS A 270 11.933 6.094 19.311 1.00 78.44 C
ANISOU 2927 CB LYS A 270 12575 9707 7520 -1093 1996 -361 C
ATOM 2928 CG LYS A 270 13.165 5.847 18.454 1.00 79.81 C
ANISOU 2928 CG LYS A 270 12777 9934 7614 -1053 2390 -450 C
ATOM 2929 CD LYS A 270 13.561 7.086 17.670 1.00 79.74 C
ANISOU 2929 CD LYS A 270 12788 10042 7467 -1176 2543 -264 C
ATOM 2930 CE LYS A 270 14.673 6.773 16.681 1.00 81.06 C
ANISOU 2930 CE LYS A 270 13017 10287 7497 -1155 2971 -360 C
ATOM 2931 NZ LYS A 270 15.949 6.400 17.352 1.00 82.55 N
ANISOU 2931 NZ LYS A 270 12859 10459 8047 -1001 3198 -445 N
ATOM 2932 N ALA A 271 9.106 5.061 20.493 1.00 71.74 N
ANISOU 2932 N ALA A 271 11853 8751 6654 -1171 1315 -418 N
ATOM 2933 CA ALA A 271 7.913 5.276 21.304 1.00 70.66 C
ANISOU 2933 CA ALA A 271 11630 8610 6609 -1207 1008 -328 C
ATOM 2934 C ALA A 271 7.808 4.236 22.412 1.00 70.71 C
ANISOU 2934 C ALA A 271 11564 8465 6840 -1135 959 -449 C
ATOM 2935 O ALA A 271 7.385 4.553 23.530 1.00 70.05 O
ANISOU 2935 O ALA A 271 11309 8345 6962 -1093 804 -358 O
ATOM 2936 CB ALA A 271 6.665 5.251 20.425 1.00 70.70 C
ANISOU 2936 CB ALA A 271 11816 8747 6298 -1362 806 -309 C
ATOM 2937 N LEU A 272 8.185 2.990 22.121 1.00 72.15 N
ANISOU 2937 N LEU A 272 11903 8538 6973 -1111 1108 -651 N
ATOM 2938 CA LEU A 272 8.173 1.957 23.153 1.00 71.97 C
ANISOU 2938 CA LEU A 272 11853 8333 7161 -1022 1092 -743 C
ATOM 2939 C LEU A 272 9.253 2.213 24.196 1.00 72.78 C
ANISOU 2939 C LEU A 272 11705 8383 7566 -816 1180 -672 C
ATOM 2940 O LEU A 272 9.006 2.093 25.402 1.00 72.21 O
ANISOU 2940 O LEU A 272 11511 8238 7689 -752 1050 -615 O
ATOM 2941 CB LEU A 272 8.349 0.575 22.524 1.00 73.87 C
ANISOU 2941 CB LEU A 272 12370 8425 7275 -1032 1257 -977 C
ATOM 2942 CG LEU A 272 7.193 0.065 21.664 1.00 73.28 C
ANISOU 2942 CG LEU A 272 12560 8380 6903 -1280 1128 -1097 C
ATOM 2943 CD1 LEU A 272 7.567 -1.247 20.996 1.00 73.72 C
ANISOU 2943 CD1 LEU A 272 12934 8248 6827 -1287 1346 -1361 C
ATOM 2944 CD2 LEU A 272 5.940 -0.100 22.507 1.00 72.17 C
ANISOU 2944 CD2 LEU A 272 12343 8222 6857 -1406 857 -1038 C
ATOM 2945 N LYS A 273 10.463 2.560 23.747 1.00 71.49 N
ANISOU 2945 N LYS A 273 11455 8276 7432 -723 1401 -674 N
ATOM 2946 CA LYS A 273 11.534 2.897 24.681 1.00 72.92 C
ANISOU 2946 CA LYS A 273 11349 8463 7894 -558 1457 -604 C
ATOM 2947 C LYS A 273 11.138 4.054 25.589 1.00 72.27 C
ANISOU 2947 C LYS A 273 11078 8445 7935 -617 1240 -438 C
ATOM 2948 O LYS A 273 11.550 4.098 26.753 1.00 73.17 O
ANISOU 2948 O LYS A 273 11002 8532 8267 -510 1167 -398 O
ATOM 2949 CB LYS A 273 12.811 3.231 23.908 1.00 75.37 C
ANISOU 2949 CB LYS A 273 11561 8873 8204 -503 1736 -622 C
ATOM 2950 CG LYS A 273 14.034 3.496 24.773 1.00 77.42 C
ANISOU 2950 CG LYS A 273 11476 9181 8757 -349 1799 -570 C
ATOM 2951 CD LYS A 273 15.269 3.729 23.912 1.00 78.80 C
ANISOU 2951 CD LYS A 273 11529 9475 8936 -313 2114 -598 C
ATOM 2952 CE LYS A 273 16.477 4.101 24.756 1.00 80.98 C
ANISOU 2952 CE LYS A 273 11399 9855 9515 -201 2145 -538 C
ATOM 2953 NZ LYS A 273 17.671 4.391 23.912 1.00 82.16 N
ANISOU 2953 NZ LYS A 273 11377 10152 9689 -194 2473 -554 N
ATOM 2954 N THR A 274 10.335 4.991 25.081 1.00 71.83 N
ANISOU 2954 N THR A 274 11091 8470 7730 -771 1135 -339 N
ATOM 2955 CA THR A 274 9.819 6.061 25.928 1.00 70.51 C
ANISOU 2955 CA THR A 274 10795 8324 7672 -808 947 -195 C
ATOM 2956 C THR A 274 8.937 5.492 27.033 1.00 69.69 C
ANISOU 2956 C THR A 274 10684 8139 7656 -771 759 -206 C
ATOM 2957 O THR A 274 9.090 5.838 28.211 1.00 69.51 O
ANISOU 2957 O THR A 274 10514 8088 7808 -707 674 -156 O
ATOM 2958 CB THR A 274 9.044 7.071 25.080 1.00 70.27 C
ANISOU 2958 CB THR A 274 10869 8376 7455 -935 880 -72 C
ATOM 2959 OG1 THR A 274 9.888 7.560 24.031 1.00 71.01 O
ANISOU 2959 OG1 THR A 274 11003 8535 7442 -981 1085 -47 O
ATOM 2960 CG2 THR A 274 8.590 8.248 25.932 1.00 68.55 C
ANISOU 2960 CG2 THR A 274 10537 8140 7368 -939 732 73 C
ATOM 2961 N LEU A 275 8.015 4.598 26.668 1.00 70.96 N
ANISOU 2961 N LEU A 275 11014 8266 7680 -832 702 -277 N
ATOM 2962 CA LEU A 275 7.157 3.950 27.652 1.00 69.74 C
ANISOU 2962 CA LEU A 275 10865 8030 7602 -829 563 -286 C
ATOM 2963 C LEU A 275 7.935 3.031 28.582 1.00 69.79 C
ANISOU 2963 C LEU A 275 10839 7903 7776 -675 634 -346 C
ATOM 2964 O LEU A 275 7.479 2.769 29.699 1.00 68.15 O
ANISOU 2964 O LEU A 275 10597 7631 7666 -640 531 -305 O
ATOM 2965 CB LEU A 275 6.053 3.167 26.945 1.00 69.81 C
ANISOU 2965 CB LEU A 275 11056 8038 7429 -981 498 -363 C
ATOM 2966 CG LEU A 275 5.070 4.009 26.137 1.00 69.79 C
ANISOU 2966 CG LEU A 275 11062 8206 7250 -1116 361 -274 C
ATOM 2967 CD1 LEU A 275 4.108 3.116 25.371 1.00 69.91 C
ANISOU 2967 CD1 LEU A 275 11243 8255 7067 -1297 281 -382 C
ATOM 2968 CD2 LEU A 275 4.312 4.974 27.039 1.00 68.94 C
ANISOU 2968 CD2 LEU A 275 10777 8154 7263 -1085 208 -114 C
ATOM 2969 N GLY A 276 9.092 2.528 28.148 1.00 69.61 N
ANISOU 2969 N GLY A 276 10826 7843 7781 -564 816 -429 N
ATOM 2970 CA GLY A 276 9.942 1.757 29.036 1.00 70.52 C
ANISOU 2970 CA GLY A 276 10872 7853 8069 -363 872 -450 C
ATOM 2971 C GLY A 276 10.708 2.592 30.035 1.00 71.97 C
ANISOU 2971 C GLY A 276 10793 8130 8424 -266 801 -349 C
ATOM 2972 O GLY A 276 11.201 2.050 31.029 1.00 72.77 O
ANISOU 2972 O GLY A 276 10819 8175 8654 -103 766 -328 O
ATOM 2973 N ILE A 277 10.827 3.895 29.791 1.00 71.20 N
ANISOU 2973 N ILE A 277 10571 8165 8319 -371 773 -286 N
ATOM 2974 CA ILE A 277 11.542 4.771 30.713 1.00 72.86 C
ANISOU 2974 CA ILE A 277 10548 8456 8680 -336 698 -219 C
ATOM 2975 C ILE A 277 10.628 5.277 31.820 1.00 69.26 C
ANISOU 2975 C ILE A 277 10104 7976 8236 -381 501 -150 C
ATOM 2976 O ILE A 277 11.047 5.377 32.976 1.00 70.15 O
ANISOU 2976 O ILE A 277 10100 8105 8449 -305 403 -127 O
ATOM 2977 CB ILE A 277 12.201 5.929 29.939 1.00 69.75 C
ANISOU 2977 CB ILE A 277 10041 8174 8287 -447 799 -192 C
ATOM 2978 CG1 ILE A 277 13.308 5.382 29.042 1.00 71.85 C
ANISOU 2978 CG1 ILE A 277 10245 8489 8567 -370 1032 -263 C
ATOM 2979 CG2 ILE A 277 12.755 6.975 30.889 1.00 69.70 C
ANISOU 2979 CG2 ILE A 277 9827 8232 8423 -487 698 -141 C
ATOM 2980 CD1 ILE A 277 13.848 6.384 28.080 1.00 71.35 C
ANISOU 2980 CD1 ILE A 277 10120 8527 8465 -507 1184 -230 C
ATOM 2981 N ILE A 278 9.371 5.591 31.498 1.00 72.44 N
ANISOU 2981 N ILE A 278 10640 8359 8527 -496 441 -116 N
ATOM 2982 CA ILE A 278 8.428 5.977 32.543 1.00 69.46 C
ANISOU 2982 CA ILE A 278 10271 7958 8163 -514 295 -57 C
ATOM 2983 C ILE A 278 8.176 4.811 33.489 1.00 69.07 C
ANISOU 2983 C ILE A 278 10281 7824 8137 -422 252 -72 C
ATOM 2984 O ILE A 278 7.877 5.012 34.672 1.00 68.07 O
ANISOU 2984 O ILE A 278 10132 7689 8042 -388 159 -28 O
ATOM 2985 CB ILE A 278 7.111 6.502 31.933 1.00 69.78 C
ANISOU 2985 CB ILE A 278 10396 8023 8094 -626 249 -3 C
ATOM 2986 CG1 ILE A 278 6.414 5.415 31.115 1.00 70.24 C
ANISOU 2986 CG1 ILE A 278 10590 8064 8035 -687 270 -55 C
ATOM 2987 CG2 ILE A 278 7.365 7.726 31.074 1.00 70.10 C
ANISOU 2987 CG2 ILE A 278 10413 8120 8102 -693 291 52 C
ATOM 2988 CD1 ILE A 278 5.009 5.786 30.685 1.00 69.64 C
ANISOU 2988 CD1 ILE A 278 10545 8058 7857 -793 173 6 C
ATOM 2989 N MET A 279 8.300 3.578 32.991 1.00 68.72 N
ANISOU 2989 N MET A 279 10346 7698 8066 -381 338 -132 N
ATOM 2990 CA MET A 279 8.137 2.402 33.836 1.00 68.42 C
ANISOU 2990 CA MET A 279 10407 7533 8056 -288 325 -129 C
ATOM 2991 C MET A 279 9.386 2.145 34.670 1.00 71.27 C
ANISOU 2991 C MET A 279 10657 7897 8525 -86 315 -104 C
ATOM 2992 O MET A 279 9.297 1.911 35.880 1.00 71.14 O
ANISOU 2992 O MET A 279 10652 7852 8528 -6 223 -38 O
ATOM 2993 CB MET A 279 7.811 1.182 32.975 1.00 70.91 C
ANISOU 2993 CB MET A 279 10922 7714 8306 -328 433 -215 C
ATOM 2994 CG MET A 279 6.472 1.265 32.270 1.00 69.19 C
ANISOU 2994 CG MET A 279 10802 7522 7967 -549 395 -239 C
ATOM 2995 SD MET A 279 6.165 -0.171 31.228 1.00 69.72 S
ANISOU 2995 SD MET A 279 11133 7425 7932 -650 511 -387 S
ATOM 2996 CE MET A 279 4.627 0.311 30.451 1.00 69.01 C
ANISOU 2996 CE MET A 279 11050 7482 7688 -934 385 -391 C
ATOM 2997 N GLY A 280 10.560 2.181 34.034 1.00 65.93 N
ANISOU 2997 N GLY A 280 9863 7278 7911 1 410 -149 N
ATOM 2998 CA GLY A 280 11.799 1.997 34.769 1.00 69.79 C
ANISOU 2998 CA GLY A 280 10175 7825 8518 201 379 -117 C
ATOM 2999 C GLY A 280 12.047 3.088 35.791 1.00 71.27 C
ANISOU 2999 C GLY A 280 10187 8156 8736 159 208 -64 C
ATOM 3000 O GLY A 280 12.654 2.839 36.837 1.00 73.79 O
ANISOU 3000 O GLY A 280 10413 8523 9101 303 96 -13 O
ATOM 3001 N THR A 281 11.584 4.307 35.508 1.00 71.82 N
ANISOU 3001 N THR A 281 10230 8289 8769 -34 183 -75 N
ATOM 3002 CA THR A 281 11.681 5.381 36.490 1.00 72.44 C
ANISOU 3002 CA THR A 281 10208 8455 8861 -101 37 -53 C
ATOM 3003 C THR A 281 10.707 5.153 37.640 1.00 69.46 C
ANISOU 3003 C THR A 281 9982 8012 8399 -80 -72 -6 C
ATOM 3004 O THR A 281 11.062 5.327 38.812 1.00 71.63 O
ANISOU 3004 O THR A 281 10210 8347 8661 -27 -205 14 O
ATOM 3005 CB THR A 281 11.422 6.732 35.823 1.00 70.18 C
ANISOU 3005 CB THR A 281 9900 8198 8566 -292 75 -69 C
ATOM 3006 OG1 THR A 281 12.400 6.955 34.800 1.00 73.20 O
ANISOU 3006 OG1 THR A 281 10145 8651 9015 -327 202 -99 O
ATOM 3007 CG2 THR A 281 11.499 7.855 36.844 1.00 69.91 C
ANISOU 3007 CG2 THR A 281 9814 8205 8545 -375 -54 -76 C
ATOM 3008 N PHE A 282 9.468 4.765 37.318 1.00 70.29 N
ANISOU 3008 N PHE A 282 10263 8013 8432 -136 -17 11 N
ATOM 3009 CA PHE A 282 8.489 4.458 38.356 1.00 68.14 C
ANISOU 3009 CA PHE A 282 10123 7682 8085 -127 -73 64 C
ATOM 3010 C PHE A 282 9.008 3.382 39.298 1.00 70.20 C
ANISOU 3010 C PHE A 282 10435 7901 8338 42 -120 117 C
ATOM 3011 O PHE A 282 8.745 3.420 40.506 1.00 70.17 O
ANISOU 3011 O PHE A 282 10493 7910 8260 77 -205 170 O
ATOM 3012 CB PHE A 282 7.171 4.012 37.723 1.00 69.27 C
ANISOU 3012 CB PHE A 282 10398 7744 8179 -229 5 72 C
ATOM 3013 CG PHE A 282 6.063 3.795 38.716 1.00 67.72 C
ANISOU 3013 CG PHE A 282 10302 7509 7919 -254 -14 131 C
ATOM 3014 CD1 PHE A 282 5.314 4.862 39.183 1.00 66.71 C
ANISOU 3014 CD1 PHE A 282 10141 7443 7761 -312 -40 146 C
ATOM 3015 CD2 PHE A 282 5.785 2.528 39.198 1.00 67.73 C
ANISOU 3015 CD2 PHE A 282 10445 7396 7895 -213 23 176 C
ATOM 3016 CE1 PHE A 282 4.297 4.666 40.098 1.00 66.15 C
ANISOU 3016 CE1 PHE A 282 10146 7356 7631 -327 -18 199 C
ATOM 3017 CE2 PHE A 282 4.775 2.328 40.117 1.00 66.84 C
ANISOU 3017 CE2 PHE A 282 10421 7256 7719 -256 39 242 C
ATOM 3018 CZ PHE A 282 4.029 3.397 40.566 1.00 66.23 C
ANISOU 3018 CZ PHE A 282 10279 7276 7608 -312 23 250 C
ATOM 3019 N THR A 283 9.745 2.411 38.760 1.00 67.84 N
ANISOU 3019 N THR A 283 10131 7544 8101 166 -54 112 N
ATOM 3020 CA THR A 283 10.300 1.354 39.594 1.00 69.49 C
ANISOU 3020 CA THR A 283 10398 7692 8314 376 -95 192 C
ATOM 3021 C THR A 283 11.387 1.900 40.512 1.00 73.10 C
ANISOU 3021 C THR A 283 10661 8331 8784 486 -264 223 C
ATOM 3022 O THR A 283 11.353 1.682 41.727 1.00 72.98 O
ANISOU 3022 O THR A 283 10717 8335 8678 572 -385 308 O
ATOM 3023 CB THR A 283 10.850 0.229 38.717 1.00 70.29 C
ANISOU 3023 CB THR A 283 10547 7664 8495 514 45 169 C
ATOM 3024 OG1 THR A 283 9.800 -0.287 37.888 1.00 67.22 O
ANISOU 3024 OG1 THR A 283 10362 7112 8065 365 177 115 O
ATOM 3025 CG2 THR A 283 11.406 -0.893 39.581 1.00 71.50 C
ANISOU 3025 CG2 THR A 283 10785 7719 8664 777 11 282 C
ATOM 3026 N LEU A 284 12.344 2.643 39.954 1.00 69.51 N
ANISOU 3026 N LEU A 284 9960 8025 8424 458 -277 154 N
ATOM 3027 CA LEU A 284 13.453 3.143 40.756 1.00 73.19 C
ANISOU 3027 CA LEU A 284 10197 8694 8917 524 -455 166 C
ATOM 3028 C LEU A 284 13.017 4.182 41.782 1.00 72.30 C
ANISOU 3028 C LEU A 284 10125 8661 8683 372 -609 144 C
ATOM 3029 O LEU A 284 13.751 4.424 42.744 1.00 73.56 O
ANISOU 3029 O LEU A 284 10168 8980 8802 420 -800 158 O
ATOM 3030 CB LEU A 284 14.535 3.732 39.850 1.00 69.78 C
ANISOU 3030 CB LEU A 284 9475 8406 8633 477 -400 90 C
ATOM 3031 CG LEU A 284 15.247 2.726 38.940 1.00 71.01 C
ANISOU 3031 CG LEU A 284 9547 8523 8909 675 -237 99 C
ATOM 3032 CD1 LEU A 284 16.231 3.424 38.013 1.00 74.34 C
ANISOU 3032 CD1 LEU A 284 9678 9105 9464 591 -139 24 C
ATOM 3033 CD2 LEU A 284 15.944 1.655 39.765 1.00 71.27 C
ANISOU 3033 CD2 LEU A 284 9530 8578 8970 988 -337 209 C
ATOM 3034 N CYS A 285 11.848 4.803 41.609 1.00 74.36 N
ANISOU 3034 N CYS A 285 10547 8825 8880 199 -533 105 N
ATOM 3035 CA CYS A 285 11.394 5.787 42.586 1.00 73.10 C
ANISOU 3035 CA CYS A 285 10460 8711 8606 82 -636 69 C
ATOM 3036 C CYS A 285 10.628 5.147 43.737 1.00 70.68 C
ANISOU 3036 C CYS A 285 10374 8348 8134 169 -675 153 C
ATOM 3037 O CYS A 285 10.702 5.639 44.870 1.00 70.67 O
ANISOU 3037 O CYS A 285 10423 8432 7997 151 -806 136 O
ATOM 3038 CB CYS A 285 10.521 6.851 41.913 1.00 69.66 C
ANISOU 3038 CB CYS A 285 10079 8200 8190 -104 -523 3 C
ATOM 3039 SG CYS A 285 11.389 7.941 40.756 1.00 69.91 S
ANISOU 3039 SG CYS A 285 9904 8288 8370 -255 -473 -81 S
ATOM 3040 N TRP A 286 9.895 4.064 43.478 1.00 74.89 N
ANISOU 3040 N TRP A 286 11058 8735 8661 240 -553 236 N
ATOM 3041 CA TRP A 286 9.057 3.443 44.495 1.00 72.80 C
ANISOU 3041 CA TRP A 286 11019 8397 8245 287 -540 332 C
ATOM 3042 C TRP A 286 9.603 2.134 45.039 1.00 73.57 C
ANISOU 3042 C TRP A 286 11204 8446 8304 499 -589 468 C
ATOM 3043 O TRP A 286 9.313 1.796 46.187 1.00 73.07 O
ANISOU 3043 O TRP A 286 11311 8379 8073 561 -640 566 O
ATOM 3044 CB TRP A 286 7.647 3.198 43.946 1.00 72.74 C
ANISOU 3044 CB TRP A 286 11138 8248 8251 169 -357 341 C
ATOM 3045 CG TRP A 286 6.881 4.455 43.693 1.00 71.58 C
ANISOU 3045 CG TRP A 286 10945 8144 8109 14 -312 256 C
ATOM 3046 CD1 TRP A 286 6.688 5.071 42.493 1.00 70.55 C
ANISOU 3046 CD1 TRP A 286 10706 8010 8089 -86 -251 190 C
ATOM 3047 CD2 TRP A 286 6.224 5.268 44.672 1.00 71.45 C
ANISOU 3047 CD2 TRP A 286 11008 8169 7969 -30 -313 236 C
ATOM 3048 NE1 TRP A 286 5.938 6.210 42.660 1.00 69.73 N
ANISOU 3048 NE1 TRP A 286 10605 7930 7960 -170 -222 149 N
ATOM 3049 CE2 TRP A 286 5.641 6.354 43.990 1.00 70.62 C
ANISOU 3049 CE2 TRP A 286 10831 8064 7938 -135 -246 163 C
ATOM 3050 CE3 TRP A 286 6.067 5.180 46.058 1.00 72.00 C
ANISOU 3050 CE3 TRP A 286 11227 8273 7858 22 -351 277 C
ATOM 3051 CZ2 TRP A 286 4.912 7.342 44.646 1.00 70.85 C
ANISOU 3051 CZ2 TRP A 286 10923 8103 7893 -168 -199 121 C
ATOM 3052 CZ3 TRP A 286 5.346 6.163 46.708 1.00 72.01 C
ANISOU 3052 CZ3 TRP A 286 11299 8301 7762 -36 -298 216 C
ATOM 3053 CH2 TRP A 286 4.780 7.232 46.003 1.00 71.67 C
ANISOU 3053 CH2 TRP A 286 11173 8235 7823 -120 -215 134 C
ATOM 3054 N LEU A 287 10.374 1.387 44.249 1.00 74.30 N
ANISOU 3054 N LEU A 287 11204 8488 8537 628 -556 486 N
ATOM 3055 CA LEU A 287 10.909 0.122 44.743 1.00 75.08 C
ANISOU 3055 CA LEU A 287 11404 8505 8619 878 -588 634 C
ATOM 3056 C LEU A 287 11.765 0.282 45.997 1.00 77.02 C
ANISOU 3056 C LEU A 287 11584 8943 8736 1032 -830 720 C
ATOM 3057 O LEU A 287 11.624 -0.552 46.908 1.00 76.52 O
ANISOU 3057 O LEU A 287 11730 8805 8538 1184 -867 884 O
ATOM 3058 CB LEU A 287 11.689 -0.585 43.627 1.00 74.00 C
ANISOU 3058 CB LEU A 287 11159 8287 8671 1020 -491 612 C
ATOM 3059 CG LEU A 287 12.196 -2.002 43.882 1.00 74.63 C
ANISOU 3059 CG LEU A 287 11372 8205 8781 1318 -463 763 C
ATOM 3060 CD1 LEU A 287 11.038 -2.966 44.101 1.00 71.93 C
ANISOU 3060 CD1 LEU A 287 11398 7571 8361 1265 -311 848 C
ATOM 3061 CD2 LEU A 287 13.072 -2.461 42.730 1.00 76.41 C
ANISOU 3061 CD2 LEU A 287 11448 8384 9201 1468 -346 700 C
ATOM 3062 N PRO A 288 12.640 1.291 46.127 1.00 78.22 N
ANISOU 3062 N PRO A 288 11472 9344 8906 985 -1005 627 N
ATOM 3063 CA PRO A 288 13.317 1.478 47.424 1.00 79.49 C
ANISOU 3063 CA PRO A 288 11592 9716 8893 1084 -1271 695 C
ATOM 3064 C PRO A 288 12.352 1.676 48.579 1.00 77.53 C
ANISOU 3064 C PRO A 288 11639 9442 8376 997 -1293 734 C
ATOM 3065 O PRO A 288 12.551 1.099 49.655 1.00 77.81 O
ANISOU 3065 O PRO A 288 11818 9530 8218 1161 -1430 887 O
ATOM 3066 CB PRO A 288 14.186 2.721 47.190 1.00 76.69 C
ANISOU 3066 CB PRO A 288 10914 9606 8619 929 -1415 531 C
ATOM 3067 CG PRO A 288 14.420 2.743 45.734 1.00 77.70 C
ANISOU 3067 CG PRO A 288 10862 9659 9000 890 -1229 453 C
ATOM 3068 CD PRO A 288 13.155 2.232 45.114 1.00 75.05 C
ANISOU 3068 CD PRO A 288 10796 9047 8674 838 -978 467 C
ATOM 3069 N PHE A 289 11.312 2.488 48.384 1.00 81.58 N
ANISOU 3069 N PHE A 289 12249 9885 8865 760 -1152 611 N
ATOM 3070 CA PHE A 289 10.309 2.681 49.427 1.00 79.93 C
ANISOU 3070 CA PHE A 289 12313 9646 8411 685 -1111 638 C
ATOM 3071 C PHE A 289 9.633 1.364 49.794 1.00 78.63 C
ANISOU 3071 C PHE A 289 12416 9296 8165 810 -977 838 C
ATOM 3072 O PHE A 289 9.497 1.031 50.976 1.00 78.71 O
ANISOU 3072 O PHE A 289 12639 9341 7926 889 -1042 962 O
ATOM 3073 CB PHE A 289 9.279 3.715 48.968 1.00 80.41 C
ANISOU 3073 CB PHE A 289 12389 9644 8518 454 -941 484 C
ATOM 3074 CG PHE A 289 8.159 3.937 49.944 1.00 79.04 C
ANISOU 3074 CG PHE A 289 12470 9439 8124 389 -837 500 C
ATOM 3075 CD1 PHE A 289 8.364 4.653 51.113 1.00 79.85 C
ANISOU 3075 CD1 PHE A 289 12676 9685 7979 363 -973 436 C
ATOM 3076 CD2 PHE A 289 6.895 3.437 49.685 1.00 77.15 C
ANISOU 3076 CD2 PHE A 289 12359 9039 7917 339 -595 566 C
ATOM 3077 CE1 PHE A 289 7.326 4.856 52.007 1.00 79.00 C
ANISOU 3077 CE1 PHE A 289 12816 9549 7653 317 -834 442 C
ATOM 3078 CE2 PHE A 289 5.856 3.639 50.571 1.00 76.47 C
ANISOU 3078 CE2 PHE A 289 12470 8944 7641 283 -462 586 C
ATOM 3079 CZ PHE A 289 6.071 4.348 51.734 1.00 77.47 C
ANISOU 3079 CZ PHE A 289 12718 9202 7515 287 -565 525 C
ATOM 3080 N PHE A 290 9.210 0.595 48.789 1.00 80.15 N
ANISOU 3080 N PHE A 290 12624 9281 8548 810 -785 870 N
ATOM 3081 CA PHE A 290 8.469 -0.633 49.058 1.00 78.85 C
ANISOU 3081 CA PHE A 290 12736 8893 8330 866 -623 1041 C
ATOM 3082 C PHE A 290 9.360 -1.770 49.549 1.00 80.30 C
ANISOU 3082 C PHE A 290 13021 9019 8469 1155 -730 1242 C
ATOM 3083 O PHE A 290 8.884 -2.635 50.293 1.00 79.78 O
ANISOU 3083 O PHE A 290 13247 8808 8259 1223 -653 1426 O
ATOM 3084 CB PHE A 290 7.686 -1.056 47.814 1.00 75.22 C
ANISOU 3084 CB PHE A 290 12278 8228 8075 727 -396 980 C
ATOM 3085 CG PHE A 290 6.435 -0.252 47.588 1.00 73.43 C
ANISOU 3085 CG PHE A 290 12033 8024 7845 474 -260 871 C
ATOM 3086 CD1 PHE A 290 5.256 -0.598 48.228 1.00 72.32 C
ANISOU 3086 CD1 PHE A 290 12091 7800 7587 369 -102 957 C
ATOM 3087 CD2 PHE A 290 6.442 0.859 46.765 1.00 73.21 C
ANISOU 3087 CD2 PHE A 290 11781 8105 7931 355 -280 700 C
ATOM 3088 CE1 PHE A 290 4.104 0.136 48.033 1.00 71.21 C
ANISOU 3088 CE1 PHE A 290 11886 7707 7462 172 28 868 C
ATOM 3089 CE2 PHE A 290 5.293 1.600 46.569 1.00 71.77 C
ANISOU 3089 CE2 PHE A 290 11573 7945 7752 174 -162 626 C
ATOM 3090 CZ PHE A 290 4.122 1.237 47.205 1.00 70.89 C
ANISOU 3090 CZ PHE A 290 11620 7774 7541 94 -12 707 C
ATOM 3091 N ILE A 291 10.636 -1.802 49.155 1.00 79.61 N
ANISOU 3091 N ILE A 291 12698 9042 8509 1339 -890 1227 N
ATOM 3092 CA ILE A 291 11.528 -2.809 49.725 1.00 81.20 C
ANISOU 3092 CA ILE A 291 12966 9222 8663 1669 -1018 1442 C
ATOM 3093 C ILE A 291 11.793 -2.513 51.194 1.00 82.06 C
ANISOU 3093 C ILE A 291 13164 9552 8462 1746 -1258 1557 C
ATOM 3094 O ILE A 291 11.966 -3.432 52.002 1.00 82.54 O
ANISOU 3094 O ILE A 291 13450 9542 8370 1977 -1316 1799 O
ATOM 3095 CB ILE A 291 12.843 -2.908 48.926 1.00 77.84 C
ANISOU 3095 CB ILE A 291 12211 8895 8470 1871 -1115 1401 C
ATOM 3096 CG1 ILE A 291 12.590 -3.462 47.527 1.00 77.10 C
ANISOU 3096 CG1 ILE A 291 12122 8543 8632 1839 -850 1312 C
ATOM 3097 CG2 ILE A 291 13.856 -3.793 49.639 1.00 79.71 C
ANISOU 3097 CG2 ILE A 291 12455 9179 8653 2261 -1297 1637 C
ATOM 3098 CD1 ILE A 291 13.824 -3.438 46.655 1.00 79.48 C
ANISOU 3098 CD1 ILE A 291 12085 8955 9158 2012 -887 1242 C
ATOM 3099 N VAL A 292 11.814 -1.236 51.575 1.00 83.22 N
ANISOU 3099 N VAL A 292 13175 9954 8491 1554 -1398 1389 N
ATOM 3100 CA VAL A 292 12.047 -0.906 52.975 1.00 84.04 C
ANISOU 3100 CA VAL A 292 13395 10280 8257 1595 -1632 1462 C
ATOM 3101 C VAL A 292 10.816 -1.208 53.820 1.00 82.36 C
ANISOU 3101 C VAL A 292 13589 9921 7785 1510 -1451 1569 C
ATOM 3102 O VAL A 292 10.942 -1.618 54.980 1.00 83.03 O
ANISOU 3102 O VAL A 292 13904 10078 7567 1649 -1576 1755 O
ATOM 3103 CB VAL A 292 12.503 0.558 53.091 1.00 78.89 C
ANISOU 3103 CB VAL A 292 12496 9915 7562 1392 -1826 1217 C
ATOM 3104 CG1 VAL A 292 12.517 1.007 54.532 1.00 79.39 C
ANISOU 3104 CG1 VAL A 292 12747 10188 7229 1363 -2034 1235 C
ATOM 3105 CG2 VAL A 292 13.897 0.689 52.510 1.00 81.14 C
ANISOU 3105 CG2 VAL A 292 12373 10395 8063 1505 -2039 1172 C
ATOM 3106 N ASN A 293 9.614 -1.040 53.262 1.00 87.10 N
ANISOU 3106 N ASN A 293 14274 10330 8489 1287 -1153 1471 N
ATOM 3107 CA ASN A 293 8.410 -1.465 53.971 1.00 85.77 C
ANISOU 3107 CA ASN A 293 14453 10016 8122 1203 -930 1591 C
ATOM 3108 C ASN A 293 8.423 -2.966 54.226 1.00 85.89 C
ANISOU 3108 C ASN A 293 14731 9797 8107 1404 -850 1881 C
ATOM 3109 O ASN A 293 8.086 -3.421 55.325 1.00 86.10 O
ANISOU 3109 O ASN A 293 15071 9801 7842 1461 -822 2077 O
ATOM 3110 CB ASN A 293 7.161 -1.082 53.179 1.00 83.76 C
ANISOU 3110 CB ASN A 293 14161 9623 8041 940 -636 1442 C
ATOM 3111 CG ASN A 293 6.899 0.402 53.190 1.00 83.62 C
ANISOU 3111 CG ASN A 293 13992 9789 7992 761 -662 1200 C
ATOM 3112 OD1 ASN A 293 7.086 1.065 54.207 1.00 84.47 O
ANISOU 3112 OD1 ASN A 293 14189 10075 7832 760 -789 1159 O
ATOM 3113 ND2 ASN A 293 6.446 0.932 52.061 1.00 82.60 N
ANISOU 3113 ND2 ASN A 293 13661 9602 8120 609 -538 1040 N
ATOM 3114 N ILE A 294 8.813 -3.750 53.220 1.00 87.50 N
ANISOU 3114 N ILE A 294 14843 9804 8599 1516 -793 1915 N
ATOM 3115 CA ILE A 294 8.723 -5.200 53.333 1.00 87.51 C
ANISOU 3115 CA ILE A 294 15138 9497 8614 1688 -661 2172 C
ATOM 3116 C ILE A 294 9.802 -5.737 54.269 1.00 89.48 C
ANISOU 3116 C ILE A 294 15482 9845 8670 2048 -922 2421 C
ATOM 3117 O ILE A 294 9.636 -6.807 54.866 1.00 89.68 O
ANISOU 3117 O ILE A 294 15855 9650 8570 2205 -838 2698 O
ATOM 3118 CB ILE A 294 8.795 -5.840 51.931 1.00 86.96 C
ANISOU 3118 CB ILE A 294 14972 9166 8902 1692 -502 2093 C
ATOM 3119 CG1 ILE A 294 8.208 -7.251 51.943 1.00 86.38 C
ANISOU 3119 CG1 ILE A 294 15279 8683 8860 1723 -253 2296 C
ATOM 3120 CG2 ILE A 294 10.220 -5.879 51.412 1.00 88.77 C
ANISOU 3120 CG2 ILE A 294 14924 9506 9298 1977 -710 2071 C
ATOM 3121 CD1 ILE A 294 6.714 -7.272 52.127 1.00 84.76 C
ANISOU 3121 CD1 ILE A 294 15272 8351 8582 1376 14 2281 C
ATOM 3122 N VAL A 295 10.907 -5.012 54.428 1.00 90.88 N
ANISOU 3122 N VAL A 295 15357 10357 8815 2177 -1245 2342 N
ATOM 3123 CA VAL A 295 11.958 -5.427 55.354 1.00 92.93 C
ANISOU 3123 CA VAL A 295 15648 10789 8872 2520 -1550 2579 C
ATOM 3124 C VAL A 295 11.670 -4.937 56.767 1.00 93.19 C
ANISOU 3124 C VAL A 295 15904 11050 8454 2450 -1697 2651 C
ATOM 3125 O VAL A 295 11.891 -5.664 57.739 1.00 94.13 O
ANISOU 3125 O VAL A 295 16301 11163 8301 2685 -1805 2947 O
ATOM 3126 CB VAL A 295 13.331 -4.937 54.853 1.00 88.48 C
ANISOU 3126 CB VAL A 295 14609 10513 8496 2680 -1842 2464 C
ATOM 3127 CG1 VAL A 295 14.410 -5.222 55.886 1.00 90.73 C
ANISOU 3127 CG1 VAL A 295 14861 11066 8547 3017 -2216 2700 C
ATOM 3128 CG2 VAL A 295 13.677 -5.612 53.537 1.00 88.55 C
ANISOU 3128 CG2 VAL A 295 14459 10277 8909 2815 -1664 2434 C
ATOM 3129 N HIS A 296 11.187 -3.699 56.892 1.00 97.10 N
ANISOU 3129 N HIS A 296 16305 11738 8851 2140 -1694 2386 N
ATOM 3130 CA HIS A 296 10.660 -3.166 58.144 1.00 97.06 C
ANISOU 3130 CA HIS A 296 16565 11899 8414 2015 -1734 2395 C
ATOM 3131 C HIS A 296 9.767 -4.158 58.879 1.00 96.41 C
ANISOU 3131 C HIS A 296 16958 11572 8101 2058 -1487 2679 C
ATOM 3132 O HIS A 296 9.869 -4.307 60.101 1.00 97.39 O
ANISOU 3132 O HIS A 296 17361 11833 7808 2162 -1620 2863 O
ATOM 3133 CB HIS A 296 9.889 -1.876 57.863 1.00102.35 C
ANISOU 3133 CB HIS A 296 17125 12641 9120 1663 -1589 2061 C
ATOM 3134 CG HIS A 296 8.993 -1.452 58.981 1.00101.94 C
ANISOU 3134 CG HIS A 296 17404 12654 8674 1514 -1469 2053 C
ATOM 3135 ND1 HIS A 296 9.466 -0.968 60.181 1.00103.31 N
ANISOU 3135 ND1 HIS A 296 17716 13116 8420 1552 -1736 2055 N
ATOM 3136 CD2 HIS A 296 7.642 -1.433 59.074 1.00100.51 C
ANISOU 3136 CD2 HIS A 296 17433 12303 8454 1323 -1097 2035 C
ATOM 3137 CE1 HIS A 296 8.444 -0.678 60.968 1.00102.70 C
ANISOU 3137 CE1 HIS A 296 17955 13022 8044 1403 -1507 2034 C
ATOM 3138 NE2 HIS A 296 7.327 -0.949 60.319 1.00101.08 N
ANISOU 3138 NE2 HIS A 296 17776 12546 8082 1270 -1111 2028 N
ATOM 3139 N VAL A 297 8.891 -4.841 58.142 1.00 96.34 N
ANISOU 3139 N VAL A 297 17052 11206 8345 1956 -1128 2716 N
ATOM 3140 CA VAL A 297 7.976 -5.791 58.766 1.00 95.82 C
ANISOU 3140 CA VAL A 297 17429 10877 8100 1936 -847 2979 C
ATOM 3141 C VAL A 297 8.719 -7.055 59.180 1.00 97.13 C
ANISOU 3141 C VAL A 297 17819 10890 8195 2296 -963 3340 C
ATOM 3142 O VAL A 297 8.543 -7.562 60.294 1.00 98.87 O
ANISOU 3142 O VAL A 297 18253 11137 8175 2326 -931 3529 O
ATOM 3143 CB VAL A 297 6.809 -6.106 57.815 1.00 93.28 C
ANISOU 3143 CB VAL A 297 17112 10240 8090 1666 -445 2883 C
ATOM 3144 CG1 VAL A 297 5.914 -7.180 58.409 1.00 93.04 C
ANISOU 3144 CG1 VAL A 297 17524 9914 7912 1614 -138 3165 C
ATOM 3145 CG2 VAL A 297 6.015 -4.844 57.524 1.00 92.18 C
ANISOU 3145 CG2 VAL A 297 16753 10273 7997 1352 -332 2566 C
ATOM 3146 N ILE A 298 9.561 -7.583 58.290 1.00 97.07 N
ANISOU 3146 N ILE A 298 17616 10756 8509 2525 -1062 3365 N
ATOM 3147 CA ILE A 298 10.252 -8.838 58.572 1.00 98.84 C
ANISOU 3147 CA ILE A 298 17942 10815 8796 2855 -1118 3653 C
ATOM 3148 C ILE A 298 11.282 -8.648 59.679 1.00102.62 C
ANISOU 3148 C ILE A 298 18326 11679 8987 3102 -1518 3792 C
ATOM 3149 O ILE A 298 11.415 -9.493 60.573 1.00107.04 O
ANISOU 3149 O ILE A 298 19077 12190 9402 3247 -1530 4055 O
ATOM 3150 CB ILE A 298 10.893 -9.392 57.287 1.00 98.59 C
ANISOU 3150 CB ILE A 298 17740 10546 9175 3066 -1093 3626 C
ATOM 3151 CG1 ILE A 298 9.817 -9.698 56.244 1.00 96.60 C
ANISOU 3151 CG1 ILE A 298 17618 9900 9185 2779 -694 3491 C
ATOM 3152 CG2 ILE A 298 11.703 -10.644 57.586 1.00102.54 C
ANISOU 3152 CG2 ILE A 298 18296 10895 9771 3435 -1153 3898 C
ATOM 3153 CD1 ILE A 298 10.371 -10.000 54.872 1.00 96.59 C
ANISOU 3153 CD1 ILE A 298 17362 9733 9606 2879 -644 3335 C
ATOM 3154 N GLN A 299 12.019 -7.536 59.645 1.00103.09 N
ANISOU 3154 N GLN A 299 18085 12132 8951 3129 -1861 3615 N
ATOM 3155 CA GLN A 299 13.047 -7.294 60.650 1.00106.92 C
ANISOU 3155 CA GLN A 299 18426 13030 9170 3318 -2282 3715 C
ATOM 3156 C GLN A 299 12.445 -6.971 62.014 1.00109.10 C
ANISOU 3156 C GLN A 299 18973 13483 8997 3121 -2277 3752 C
ATOM 3157 O GLN A 299 13.148 -7.066 63.027 1.00113.65 O
ANISOU 3157 O GLN A 299 19531 14342 9309 3268 -2574 3905 O
ATOM 3158 CB GLN A 299 13.967 -6.162 60.179 1.00106.40 C
ANISOU 3158 CB GLN A 299 17938 13340 9149 3337 -2645 3472 C
ATOM 3159 CG GLN A 299 15.260 -5.996 60.969 1.00110.39 C
ANISOU 3159 CG GLN A 299 18166 14293 9483 3548 -3125 3563 C
ATOM 3160 CD GLN A 299 16.195 -7.186 60.819 1.00114.24 C
ANISOU 3160 CD GLN A 299 18508 14689 10210 3972 -3213 3858 C
ATOM 3161 OE1 GLN A 299 16.328 -8.005 61.728 1.00118.91 O
ANISOU 3161 OE1 GLN A 299 19287 15254 10638 4130 -3255 4144 O
ATOM 3162 NE2 GLN A 299 16.849 -7.283 59.665 1.00112.78 N
ANISOU 3162 NE2 GLN A 299 17989 14448 10415 4167 -3229 3789 N
ATOM 3163 N ASP A 300 11.163 -6.602 62.060 1.00108.79 N
ANISOU 3163 N ASP A 300 19170 13296 8867 2797 -1937 3618 N
ATOM 3164 CA ASP A 300 10.372 -6.317 63.258 1.00110.61 C
ANISOU 3164 CA ASP A 300 19682 13641 8703 2591 -1816 3628 C
ATOM 3165 C ASP A 300 10.826 -5.073 64.015 1.00111.53 C
ANISOU 3165 C ASP A 300 19693 14216 8466 2492 -2142 3423 C
ATOM 3166 O ASP A 300 10.248 -4.768 65.066 1.00113.58 O
ANISOU 3166 O ASP A 300 20188 14599 8367 2336 -2052 3409 O
ATOM 3167 CB ASP A 300 10.336 -7.497 64.243 1.00114.14 C
ANISOU 3167 CB ASP A 300 20405 13979 8984 2742 -1752 3984 C
ATOM 3168 CG ASP A 300 9.459 -8.640 63.761 1.00113.69 C
ANISOU 3168 CG ASP A 300 20571 13434 9192 2697 -1321 4139 C
ATOM 3169 OD1 ASP A 300 8.500 -8.378 63.005 1.00109.55 O
ANISOU 3169 OD1 ASP A 300 20058 12708 8858 2443 -1005 3957 O
ATOM 3170 OD2 ASP A 300 9.718 -9.799 64.153 1.00117.86 O
ANISOU 3170 OD2 ASP A 300 21263 13782 9735 2899 -1301 4440 O
ATOM 3171 N ASN A 301 11.828 -4.345 63.531 1.00112.78 N
ANISOU 3171 N ASN A 301 19508 14629 8712 2558 -2504 3249 N
ATOM 3172 CA ASN A 301 12.194 -3.069 64.129 1.00113.46 C
ANISOU 3172 CA ASN A 301 19491 15120 8499 2385 -2793 2984 C
ATOM 3173 C ASN A 301 11.434 -1.933 63.451 1.00108.88 C
ANISOU 3173 C ASN A 301 18900 14470 8000 2086 -2598 2625 C
ATOM 3174 O ASN A 301 11.292 -1.906 62.224 1.00107.56 O
ANISOU 3174 O ASN A 301 18528 14098 8244 2052 -2450 2522 O
ATOM 3175 CB ASN A 301 13.709 -2.843 64.059 1.00115.54 C
ANISOU 3175 CB ASN A 301 19358 15734 8807 2568 -3309 2974 C
ATOM 3176 CG ASN A 301 14.273 -2.984 62.651 1.00112.60 C
ANISOU 3176 CG ASN A 301 18647 15237 8899 2724 -3358 2932 C
ATOM 3177 OD1 ASN A 301 13.541 -3.192 61.684 1.00110.27 O
ANISOU 3177 OD1 ASN A 301 18405 14591 8901 2661 -3007 2882 O
ATOM 3178 ND2 ASN A 301 15.592 -2.874 62.536 1.00114.82 N
ANISOU 3178 ND2 ASN A 301 18525 15828 9273 2903 -3775 2941 N
ATOM 3179 N LEU A 302 10.913 -1.013 64.263 1.00109.86 N
ANISOU 3179 N LEU A 302 19192 14756 7793 1843 -2546 2415 N
ATOM 3180 CA LEU A 302 10.112 0.080 63.729 1.00107.76 C
ANISOU 3180 CA LEU A 302 18948 14405 7589 1569 -2323 2083 C
ATOM 3181 C LEU A 302 10.946 0.964 62.810 1.00108.08 C
ANISOU 3181 C LEU A 302 18502 14575 7990 1466 -2553 1787 C
ATOM 3182 O LEU A 302 12.160 1.109 62.978 1.00109.87 O
ANISOU 3182 O LEU A 302 18502 15080 8163 1560 -2983 1780 O
ATOM 3183 CB LEU A 302 9.497 0.909 64.857 1.00110.01 C
ANISOU 3183 CB LEU A 302 19476 14842 7479 1357 -2209 1894 C
ATOM 3184 CG LEU A 302 8.334 0.231 65.583 1.00111.32 C
ANISOU 3184 CG LEU A 302 19974 14839 7485 1339 -1789 2088 C
ATOM 3185 CD1 LEU A 302 7.876 1.046 66.783 1.00114.10 C
ANISOU 3185 CD1 LEU A 302 20552 15381 7418 1173 -1706 1903 C
ATOM 3186 CD2 LEU A 302 7.182 0.011 64.611 1.00107.40 C
ANISOU 3186 CD2 LEU A 302 19499 13996 7312 1248 -1339 2089 C
ATOM 3187 N ILE A 303 10.277 1.556 61.829 1.00102.04 N
ANISOU 3187 N ILE A 303 17562 13615 7592 1265 -2259 1556 N
ATOM 3188 CA ILE A 303 10.969 2.218 60.734 1.00102.18 C
ANISOU 3188 CA ILE A 303 17127 13676 8021 1175 -2390 1330 C
ATOM 3189 C ILE A 303 11.363 3.628 61.149 1.00103.03 C
ANISOU 3189 C ILE A 303 17171 14022 7952 942 -2600 995 C
ATOM 3190 O ILE A 303 10.681 4.289 61.941 1.00102.73 O
ANISOU 3190 O ILE A 303 17438 14004 7590 793 -2480 849 O
ATOM 3191 CB ILE A 303 10.100 2.214 59.460 1.00 98.48 C
ANISOU 3191 CB ILE A 303 16520 12898 8002 1071 -2003 1253 C
ATOM 3192 CG1 ILE A 303 10.968 2.510 58.238 1.00 98.90 C
ANISOU 3192 CG1 ILE A 303 16120 12974 8484 1057 -2137 1126 C
ATOM 3193 CG2 ILE A 303 8.948 3.203 59.577 1.00 97.25 C
ANISOU 3193 CG2 ILE A 303 16514 12658 7779 829 -1707 1021 C
ATOM 3194 CD1 ILE A 303 12.009 1.445 57.993 1.00100.20 C
ANISOU 3194 CD1 ILE A 303 16108 13186 8775 1340 -2352 1365 C
ATOM 3195 N ARG A 304 12.492 4.083 60.616 1.00 98.10 N
ANISOU 3195 N ARG A 304 16155 13573 7545 902 -2900 865 N
ATOM 3196 CA ARG A 304 13.031 5.401 60.928 1.00 99.08 C
ANISOU 3196 CA ARG A 304 16186 13914 7545 644 -3132 537 C
ATOM 3197 C ARG A 304 12.162 6.455 60.253 1.00 97.44 C
ANISOU 3197 C ARG A 304 15992 13469 7561 393 -2792 253 C
ATOM 3198 O ARG A 304 12.100 6.518 59.021 1.00 96.60 O
ANISOU 3198 O ARG A 304 15612 13194 7899 366 -2629 221 O
ATOM 3199 CB ARG A 304 14.479 5.487 60.455 1.00101.65 C
ANISOU 3199 CB ARG A 304 16039 14489 8095 662 -3517 510 C
ATOM 3200 CG ARG A 304 15.495 4.754 61.334 1.00103.86 C
ANISOU 3200 CG ARG A 304 16272 15105 8085 892 -3956 740 C
ATOM 3201 CD ARG A 304 15.425 3.244 61.114 1.00103.64 C
ANISOU 3201 CD ARG A 304 16276 14933 8169 1280 -3858 1142 C
ATOM 3202 NE ARG A 304 15.642 2.876 59.717 1.00103.18 N
ANISOU 3202 NE ARG A 304 15859 14687 8658 1366 -3682 1173 N
ATOM 3203 CZ ARG A 304 15.331 1.691 59.199 1.00102.36 C
ANISOU 3203 CZ ARG A 304 15813 14326 8755 1632 -3460 1439 C
ATOM 3204 NH1 ARG A 304 14.786 0.751 59.961 1.00101.87 N
ANISOU 3204 NH1 ARG A 304 16146 14146 8414 1831 -3377 1718 N
ATOM 3205 NH2 ARG A 304 15.558 1.445 57.916 1.00102.12 N
ANISOU 3205 NH2 ARG A 304 15473 14139 9190 1682 -3302 1421 N
ATOM 3206 N LYS A 305 11.484 7.280 61.059 1.00 96.78 N
ANISOU 3206 N LYS A 305 16246 13370 7156 228 -2676 53 N
ATOM 3207 CA LYS A 305 10.462 8.174 60.522 1.00 95.22 C
ANISOU 3207 CA LYS A 305 16119 12913 7146 64 -2298 -164 C
ATOM 3208 C LYS A 305 11.017 9.112 59.456 1.00 95.21 C
ANISOU 3208 C LYS A 305 15775 12861 7539 -121 -2354 -390 C
ATOM 3209 O LYS A 305 10.308 9.445 58.500 1.00 93.81 O
ANISOU 3209 O LYS A 305 15513 12442 7688 -162 -2050 -441 O
ATOM 3210 CB LYS A 305 9.812 8.974 61.654 1.00 98.80 C
ANISOU 3210 CB LYS A 305 16994 13379 7165 -59 -2186 -368 C
ATOM 3211 CG LYS A 305 8.690 9.894 61.195 1.00 97.42 C
ANISOU 3211 CG LYS A 305 16911 12933 7172 -170 -1771 -572 C
ATOM 3212 CD LYS A 305 7.975 10.539 62.370 1.00 97.69 C
ANISOU 3212 CD LYS A 305 17394 12964 6760 -234 -1598 -751 C
ATOM 3213 CE LYS A 305 6.992 11.595 61.895 1.00 96.72 C
ANISOU 3213 CE LYS A 305 17326 12574 6848 -316 -1211 -976 C
ATOM 3214 NZ LYS A 305 5.898 11.001 61.079 1.00 95.36 N
ANISOU 3214 NZ LYS A 305 17012 12214 7008 -173 -840 -767 N
ATOM 3215 N GLU A 306 12.274 9.543 59.585 1.00 96.44 N
ANISOU 3215 N GLU A 306 15720 13253 7668 -243 -2738 -513 N
ATOM 3216 CA GLU A 306 12.857 10.355 58.522 1.00 96.53 C
ANISOU 3216 CA GLU A 306 15391 13213 8073 -434 -2768 -694 C
ATOM 3217 C GLU A 306 13.366 9.508 57.365 1.00 96.66 C
ANISOU 3217 C GLU A 306 15008 13222 8497 -273 -2775 -481 C
ATOM 3218 O GLU A 306 13.304 9.948 56.213 1.00 95.97 O
ANISOU 3218 O GLU A 306 14713 12972 8780 -366 -2603 -557 O
ATOM 3219 CB GLU A 306 13.984 11.238 59.061 1.00105.35 C
ANISOU 3219 CB GLU A 306 16413 14582 9033 -691 -3149 -940 C
ATOM 3220 CG GLU A 306 13.505 12.399 59.915 1.00105.14 C
ANISOU 3220 CG GLU A 306 16783 14481 8686 -930 -3088 -1254 C
ATOM 3221 CD GLU A 306 14.637 13.314 60.336 1.00106.91 C
ANISOU 3221 CD GLU A 306 16904 14928 8788 -1251 -3465 -1533 C
ATOM 3222 OE1 GLU A 306 15.809 12.977 60.064 1.00108.46 O
ANISOU 3222 OE1 GLU A 306 16688 15396 9127 -1269 -3801 -1453 O
ATOM 3223 OE2 GLU A 306 14.355 14.375 60.930 1.00106.86 O
ANISOU 3223 OE2 GLU A 306 17224 14823 8553 -1491 -3416 -1841 O
ATOM 3224 N VAL A 307 13.868 8.301 57.638 1.00 93.15 N
ANISOU 3224 N VAL A 307 14474 12938 7980 -20 -2956 -213 N
ATOM 3225 CA VAL A 307 14.282 7.424 56.547 1.00 93.34 C
ANISOU 3225 CA VAL A 307 14168 12914 8382 168 -2910 -18 C
ATOM 3226 C VAL A 307 13.062 6.886 55.808 1.00 91.21 C
ANISOU 3226 C VAL A 307 14043 12313 8298 267 -2496 98 C
ATOM 3227 O VAL A 307 13.101 6.688 54.587 1.00 90.85 O
ANISOU 3227 O VAL A 307 13765 12135 8617 290 -2345 124 O
ATOM 3228 CB VAL A 307 15.178 6.291 57.084 1.00 94.98 C
ANISOU 3228 CB VAL A 307 14262 13363 8464 449 -3215 244 C
ATOM 3229 CG1 VAL A 307 15.552 5.318 55.974 1.00 95.24 C
ANISOU 3229 CG1 VAL A 307 14003 13301 8883 681 -3117 439 C
ATOM 3230 CG2 VAL A 307 16.429 6.871 57.734 1.00 97.32 C
ANISOU 3230 CG2 VAL A 307 14335 14043 8599 327 -3665 121 C
ATOM 3231 N TYR A 308 11.958 6.661 56.524 1.00 90.62 N
ANISOU 3231 N TYR A 308 14347 12117 7968 305 -2302 159 N
ATOM 3232 CA TYR A 308 10.715 6.246 55.882 1.00 88.65 C
ANISOU 3232 CA TYR A 308 14212 11584 7888 346 -1914 244 C
ATOM 3233 C TYR A 308 10.175 7.339 54.966 1.00 87.62 C
ANISOU 3233 C TYR A 308 13982 11297 8012 148 -1702 26 C
ATOM 3234 O TYR A 308 9.981 7.122 53.764 1.00 86.91 O
ANISOU 3234 O TYR A 308 13704 11066 8250 159 -1548 63 O
ATOM 3235 CB TYR A 308 9.676 5.878 56.943 1.00 90.36 C
ANISOU 3235 CB TYR A 308 14828 11744 7763 398 -1743 345 C
ATOM 3236 CG TYR A 308 8.334 5.482 56.372 1.00 88.54 C
ANISOU 3236 CG TYR A 308 14686 11258 7698 402 -1347 426 C
ATOM 3237 CD1 TYR A 308 8.123 4.213 55.851 1.00 87.87 C
ANISOU 3237 CD1 TYR A 308 14574 11037 7775 542 -1237 662 C
ATOM 3238 CD2 TYR A 308 7.280 6.387 56.339 1.00 87.64 C
ANISOU 3238 CD2 TYR A 308 14672 11040 7588 263 -1085 259 C
ATOM 3239 CE1 TYR A 308 6.897 3.854 55.327 1.00 86.30 C
ANISOU 3239 CE1 TYR A 308 14434 10632 7726 497 -900 719 C
ATOM 3240 CE2 TYR A 308 6.052 6.037 55.813 1.00 86.30 C
ANISOU 3240 CE2 TYR A 308 14522 10687 7580 260 -749 338 C
ATOM 3241 CZ TYR A 308 5.866 4.769 55.309 1.00 85.60 C
ANISOU 3241 CZ TYR A 308 14390 10493 7640 354 -670 562 C
ATOM 3242 OH TYR A 308 4.644 4.416 54.786 1.00 84.36 O
ANISOU 3242 OH TYR A 308 14234 10179 7641 304 -359 625 O
ATOM 3243 N ILE A 309 9.911 8.524 55.526 1.00 87.25 N
ANISOU 3243 N ILE A 309 14092 11260 7798 -26 -1687 -201 N
ATOM 3244 CA ILE A 309 9.317 9.610 54.748 1.00 86.24 C
ANISOU 3244 CA ILE A 309 13925 10951 7892 -179 -1467 -385 C
ATOM 3245 C ILE A 309 10.231 10.025 53.603 1.00 86.72 C
ANISOU 3245 C ILE A 309 13644 11021 8285 -279 -1575 -457 C
ATOM 3246 O ILE A 309 9.756 10.431 52.534 1.00 85.72 O
ANISOU 3246 O ILE A 309 13418 10723 8429 -329 -1371 -488 O
ATOM 3247 CB ILE A 309 8.974 10.798 55.671 1.00 87.95 C
ANISOU 3247 CB ILE A 309 14418 11153 7847 -325 -1432 -627 C
ATOM 3248 CG1 ILE A 309 7.890 10.392 56.672 1.00 87.55 C
ANISOU 3248 CG1 ILE A 309 14704 11073 7486 -215 -1230 -548 C
ATOM 3249 CG2 ILE A 309 8.522 12.008 54.866 1.00 87.10 C
ANISOU 3249 CG2 ILE A 309 14275 10836 7984 -461 -1231 -812 C
ATOM 3250 CD1 ILE A 309 7.671 11.396 57.786 1.00 88.09 C
ANISOU 3250 CD1 ILE A 309 15098 11160 7211 -326 -1210 -786 C
ATOM 3251 N LEU A 310 11.549 9.925 53.797 1.00 83.69 N
ANISOU 3251 N LEU A 310 13062 10855 7880 -308 -1892 -471 N
ATOM 3252 CA LEU A 310 12.494 10.192 52.716 1.00 84.54 C
ANISOU 3252 CA LEU A 310 12809 11004 8308 -397 -1972 -513 C
ATOM 3253 C LEU A 310 12.156 9.379 51.474 1.00 83.86 C
ANISOU 3253 C LEU A 310 12571 10779 8515 -252 -1765 -344 C
ATOM 3254 O LEU A 310 11.851 9.932 50.413 1.00 83.03 O
ANISOU 3254 O LEU A 310 12380 10522 8646 -349 -1582 -406 O
ATOM 3255 CB LEU A 310 13.920 9.884 53.175 1.00 83.38 C
ANISOU 3255 CB LEU A 310 12420 11165 8098 -385 -2342 -492 C
ATOM 3256 CG LEU A 310 15.011 10.042 52.112 1.00 84.80 C
ANISOU 3256 CG LEU A 310 12173 11438 8612 -461 -2416 -515 C
ATOM 3257 CD1 LEU A 310 15.104 11.482 51.637 1.00 84.36 C
ANISOU 3257 CD1 LEU A 310 12083 11281 8690 -787 -2343 -759 C
ATOM 3258 CD2 LEU A 310 16.359 9.547 52.627 1.00 87.35 C
ANISOU 3258 CD2 LEU A 310 12204 12107 8877 -385 -2782 -449 C
ATOM 3259 N LEU A 311 12.188 8.051 51.603 1.00 81.46 N
ANISOU 3259 N LEU A 311 12265 10510 8176 -18 -1790 -129 N
ATOM 3260 CA LEU A 311 11.977 7.174 50.458 1.00 81.11 C
ANISOU 3260 CA LEU A 311 12099 10331 8387 111 -1613 10 C
ATOM 3261 C LEU A 311 10.581 7.317 49.868 1.00 78.93 C
ANISOU 3261 C LEU A 311 11984 9819 8185 59 -1305 5 C
ATOM 3262 O LEU A 311 10.375 6.966 48.702 1.00 78.56 O
ANISOU 3262 O LEU A 311 11824 9661 8365 78 -1156 49 O
ATOM 3263 CB LEU A 311 12.239 5.730 50.873 1.00 78.20 C
ANISOU 3263 CB LEU A 311 11772 10000 7939 373 -1689 237 C
ATOM 3264 CG LEU A 311 13.669 5.525 51.376 1.00 80.62 C
ANISOU 3264 CG LEU A 311 11857 10577 8198 476 -2017 277 C
ATOM 3265 CD1 LEU A 311 13.867 4.117 51.883 1.00 81.07 C
ANISOU 3265 CD1 LEU A 311 12006 10643 8155 781 -2089 533 C
ATOM 3266 CD2 LEU A 311 14.686 5.863 50.297 1.00 82.34 C
ANISOU 3266 CD2 LEU A 311 11681 10884 8720 419 -2055 196 C
ATOM 3267 N ASN A 312 9.620 7.823 50.645 1.00 79.21 N
ANISOU 3267 N ASN A 312 12272 9797 8028 0 -1206 -51 N
ATOM 3268 CA ASN A 312 8.305 8.121 50.089 1.00 77.53 C
ANISOU 3268 CA ASN A 312 12148 9402 7907 -48 -928 -64 C
ATOM 3269 C ASN A 312 8.347 9.366 49.212 1.00 77.25 C
ANISOU 3269 C ASN A 312 11993 9299 8060 -198 -869 -218 C
ATOM 3270 O ASN A 312 7.524 9.509 48.300 1.00 76.19 O
ANISOU 3270 O ASN A 312 11826 9037 8084 -211 -679 -195 O
ATOM 3271 CB ASN A 312 7.287 8.294 51.218 1.00 77.55 C
ANISOU 3271 CB ASN A 312 12433 9379 7655 -38 -808 -72 C
ATOM 3272 CG ASN A 312 5.855 8.053 50.765 1.00 76.26 C
ANISOU 3272 CG ASN A 312 12319 9074 7582 -22 -520 2 C
ATOM 3273 OD1 ASN A 312 4.960 7.865 51.588 1.00 75.97 O
ANISOU 3273 OD1 ASN A 312 12474 9024 7368 9 -375 47 O
ATOM 3274 ND2 ASN A 312 5.635 8.050 49.455 1.00 75.69 N
ANISOU 3274 ND2 ASN A 312 12064 8919 7774 -53 -436 17 N
ATOM 3275 N TRP A 313 9.292 10.273 49.471 1.00 77.21 N
ANISOU 3275 N TRP A 313 11927 9376 8033 -324 -1036 -368 N
ATOM 3276 CA TRP A 313 9.438 11.471 48.650 1.00 76.69 C
ANISOU 3276 CA TRP A 313 11777 9214 8149 -485 -973 -501 C
ATOM 3277 C TRP A 313 10.211 11.217 47.364 1.00 77.21 C
ANISOU 3277 C TRP A 313 11564 9305 8468 -507 -988 -447 C
ATOM 3278 O TRP A 313 9.993 11.925 46.375 1.00 76.10 O
ANISOU 3278 O TRP A 313 11377 9044 8495 -596 -856 -479 O
ATOM 3279 CB TRP A 313 10.092 12.584 49.465 1.00 82.70 C
ANISOU 3279 CB TRP A 313 12618 10021 8783 -663 -1121 -704 C
ATOM 3280 CG TRP A 313 9.095 13.370 50.236 1.00 81.86 C
ANISOU 3280 CG TRP A 313 12817 9779 8506 -681 -979 -817 C
ATOM 3281 CD1 TRP A 313 8.579 13.071 51.459 1.00 82.13 C
ANISOU 3281 CD1 TRP A 313 13089 9865 8253 -600 -978 -822 C
ATOM 3282 CD2 TRP A 313 8.522 14.623 49.851 1.00 80.88 C
ANISOU 3282 CD2 TRP A 313 12813 9436 8482 -771 -796 -940 C
ATOM 3283 NE1 TRP A 313 7.691 14.044 51.846 1.00 81.58 N
ANISOU 3283 NE1 TRP A 313 13265 9628 8104 -627 -783 -956 N
ATOM 3284 CE2 TRP A 313 7.645 15.014 50.879 1.00 80.86 C
ANISOU 3284 CE2 TRP A 313 13106 9358 8258 -719 -675 -1028 C
ATOM 3285 CE3 TRP A 313 8.659 15.449 48.730 1.00 80.09 C
ANISOU 3285 CE3 TRP A 313 12616 9184 8631 -875 -705 -968 C
ATOM 3286 CZ2 TRP A 313 6.908 16.196 50.822 1.00 80.33 C
ANISOU 3286 CZ2 TRP A 313 13229 9058 8233 -740 -464 -1152 C
ATOM 3287 CZ3 TRP A 313 7.928 16.619 48.675 1.00 79.34 C
ANISOU 3287 CZ3 TRP A 313 12726 8851 8570 -902 -515 -1069 C
ATOM 3288 CH2 TRP A 313 7.063 16.982 49.714 1.00 79.58 C
ANISOU 3288 CH2 TRP A 313 13039 8800 8400 -822 -395 -1163 C
ATOM 3289 N ILE A 314 11.116 10.235 47.349 1.00 75.02 N
ANISOU 3289 N ILE A 314 11111 9179 8213 -411 -1132 -358 N
ATOM 3290 CA ILE A 314 11.635 9.763 46.069 1.00 75.92 C
ANISOU 3290 CA ILE A 314 10994 9297 8557 -377 -1071 -289 C
ATOM 3291 C ILE A 314 10.491 9.251 45.204 1.00 74.27 C
ANISOU 3291 C ILE A 314 10877 8923 8418 -302 -848 -195 C
ATOM 3292 O ILE A 314 10.505 9.397 43.975 1.00 73.87 O
ANISOU 3292 O ILE A 314 10723 8814 8529 -347 -733 -188 O
ATOM 3293 CB ILE A 314 12.724 8.693 46.277 1.00 73.85 C
ANISOU 3293 CB ILE A 314 10541 9211 8307 -223 -1237 -198 C
ATOM 3294 CG1 ILE A 314 13.996 9.315 46.861 1.00 75.68 C
ANISOU 3294 CG1 ILE A 314 10574 9661 8519 -338 -1482 -300 C
ATOM 3295 CG2 ILE A 314 13.057 7.996 44.971 1.00 75.24 C
ANISOU 3295 CG2 ILE A 314 10539 9353 8695 -136 -1109 -122 C
ATOM 3296 CD1 ILE A 314 14.082 9.292 48.360 1.00 75.76 C
ANISOU 3296 CD1 ILE A 314 10726 9802 8258 -314 -1704 -319 C
ATOM 3297 N GLY A 315 9.473 8.661 45.832 1.00 74.73 N
ANISOU 3297 N GLY A 315 11132 8920 8342 -207 -784 -121 N
ATOM 3298 CA GLY A 315 8.275 8.301 45.095 1.00 73.05 C
ANISOU 3298 CA GLY A 315 10990 8576 8191 -186 -589 -51 C
ATOM 3299 C GLY A 315 7.442 9.506 44.699 1.00 71.16 C
ANISOU 3299 C GLY A 315 10797 8246 7995 -288 -468 -120 C
ATOM 3300 O GLY A 315 6.810 9.510 43.640 1.00 69.55 O
ANISOU 3300 O GLY A 315 10551 7976 7900 -304 -350 -77 O
ATOM 3301 N TYR A 316 7.424 10.543 45.542 1.00 74.97 N
ANISOU 3301 N TYR A 316 11383 8720 8382 -348 -499 -226 N
ATOM 3302 CA TYR A 316 6.636 11.735 45.244 1.00 73.56 C
ANISOU 3302 CA TYR A 316 11280 8418 8252 -403 -366 -285 C
ATOM 3303 C TYR A 316 7.169 12.475 44.023 1.00 72.56 C
ANISOU 3303 C TYR A 316 11032 8235 8303 -503 -349 -307 C
ATOM 3304 O TYR A 316 6.387 13.019 43.233 1.00 71.10 O
ANISOU 3304 O TYR A 316 10864 7948 8203 -494 -220 -265 O
ATOM 3305 CB TYR A 316 6.595 12.655 46.468 1.00 75.58 C
ANISOU 3305 CB TYR A 316 11722 8643 8353 -444 -387 -422 C
ATOM 3306 CG TYR A 316 5.611 12.235 47.543 1.00 76.07 C
ANISOU 3306 CG TYR A 316 11957 8718 8228 -337 -300 -392 C
ATOM 3307 CD1 TYR A 316 4.606 11.317 47.269 1.00 75.97 C
ANISOU 3307 CD1 TYR A 316 11913 8712 8241 -240 -173 -247 C
ATOM 3308 CD2 TYR A 316 5.675 12.770 48.827 1.00 76.74 C
ANISOU 3308 CD2 TYR A 316 12245 8813 8099 -359 -331 -518 C
ATOM 3309 CE1 TYR A 316 3.695 10.936 48.240 1.00 76.51 C
ANISOU 3309 CE1 TYR A 316 12125 8799 8148 -167 -58 -207 C
ATOM 3310 CE2 TYR A 316 4.765 12.392 49.807 1.00 77.14 C
ANISOU 3310 CE2 TYR A 316 12468 8884 7957 -262 -213 -485 C
ATOM 3311 CZ TYR A 316 3.779 11.474 49.505 1.00 77.02 C
ANISOU 3311 CZ TYR A 316 12394 8877 7992 -166 -66 -319 C
ATOM 3312 OH TYR A 316 2.870 11.090 50.467 1.00 77.40 O
ANISOU 3312 OH TYR A 316 12597 8952 7859 -93 85 -273 O
ATOM 3313 N VAL A 317 8.488 12.505 43.845 1.00 72.60 N
ANISOU 3313 N VAL A 317 10902 8319 8362 -595 -472 -357 N
ATOM 3314 CA VAL A 317 9.087 13.284 42.766 1.00 72.10 C
ANISOU 3314 CA VAL A 317 10735 8205 8454 -723 -429 -379 C
ATOM 3315 C VAL A 317 8.922 12.542 41.444 1.00 71.19 C
ANISOU 3315 C VAL A 317 10506 8106 8435 -663 -341 -259 C
ATOM 3316 O VAL A 317 9.297 13.046 40.379 1.00 70.70 O
ANISOU 3316 O VAL A 317 10374 8009 8478 -750 -272 -243 O
ATOM 3317 CB VAL A 317 10.567 13.597 43.058 1.00 69.24 C
ANISOU 3317 CB VAL A 317 10228 7954 8127 -872 -576 -481 C
ATOM 3318 CG1 VAL A 317 10.676 14.440 44.305 1.00 69.72 C
ANISOU 3318 CG1 VAL A 317 10439 7989 8064 -976 -673 -631 C
ATOM 3319 CG2 VAL A 317 11.383 12.323 43.188 1.00 71.64 C
ANISOU 3319 CG2 VAL A 317 10340 8452 8426 -768 -699 -423 C
ATOM 3320 N ASN A 318 8.346 11.340 41.502 1.00 74.49 N
ANISOU 3320 N ASN A 318 10935 8567 8802 -530 -331 -177 N
ATOM 3321 CA ASN A 318 8.014 10.636 40.273 1.00 73.18 C
ANISOU 3321 CA ASN A 318 10715 8396 8695 -494 -243 -92 C
ATOM 3322 C ASN A 318 6.946 11.369 39.471 1.00 70.78 C
ANISOU 3322 C ASN A 318 10475 8004 8412 -518 -137 -42 C
ATOM 3323 O ASN A 318 6.941 11.295 38.237 1.00 69.93 O
ANISOU 3323 O ASN A 318 10322 7900 8346 -546 -79 7 O
ATOM 3324 CB ASN A 318 7.537 9.223 40.585 1.00 70.88 C
ANISOU 3324 CB ASN A 318 10461 8128 8342 -382 -248 -30 C
ATOM 3325 CG ASN A 318 7.602 8.324 39.383 1.00 70.13 C
ANISOU 3325 CG ASN A 318 10316 8032 8298 -367 -182 12 C
ATOM 3326 OD1 ASN A 318 7.457 7.116 39.501 1.00 70.30 O
ANISOU 3326 OD1 ASN A 318 10380 8038 8294 -295 -174 47 O
ATOM 3327 ND2 ASN A 318 7.845 8.906 38.216 1.00 69.47 N
ANISOU 3327 ND2 ASN A 318 10174 7948 8274 -442 -121 4 N
ATOM 3328 N SER A 319 6.040 12.074 40.147 1.00 71.56 N
ANISOU 3328 N SER A 319 10684 8036 8472 -488 -106 -48 N
ATOM 3329 CA SER A 319 4.939 12.735 39.459 1.00 70.52 C
ANISOU 3329 CA SER A 319 10588 7837 8368 -455 -15 26 C
ATOM 3330 C SER A 319 5.404 13.882 38.571 1.00 70.29 C
ANISOU 3330 C SER A 319 10573 7718 8414 -530 25 38 C
ATOM 3331 O SER A 319 4.633 14.344 37.723 1.00 69.89 O
ANISOU 3331 O SER A 319 10543 7629 8384 -487 83 139 O
ATOM 3332 CB SER A 319 3.920 13.235 40.480 1.00 68.98 C
ANISOU 3332 CB SER A 319 10493 7589 8128 -368 39 13 C
ATOM 3333 OG SER A 319 3.337 12.148 41.174 1.00 69.45 O
ANISOU 3333 OG SER A 319 10545 7732 8112 -313 38 35 O
ATOM 3334 N GLY A 320 6.635 14.351 38.743 1.00 69.94 N
ANISOU 3334 N GLY A 320 10515 7649 8410 -648 -7 -48 N
ATOM 3335 CA GLY A 320 7.205 15.365 37.885 1.00 69.96 C
ANISOU 3335 CA GLY A 320 10536 7556 8489 -761 56 -29 C
ATOM 3336 C GLY A 320 8.129 14.849 36.808 1.00 70.29 C
ANISOU 3336 C GLY A 320 10444 7697 8565 -842 75 4 C
ATOM 3337 O GLY A 320 8.621 15.645 36.003 1.00 70.51 O
ANISOU 3337 O GLY A 320 10489 7655 8646 -953 155 39 O
ATOM 3338 N PHE A 321 8.378 13.540 36.761 1.00 70.19 N
ANISOU 3338 N PHE A 321 10319 7827 8522 -785 29 -4 N
ATOM 3339 CA PHE A 321 9.309 12.969 35.794 1.00 71.33 C
ANISOU 3339 CA PHE A 321 10340 8066 8698 -831 78 6 C
ATOM 3340 C PHE A 321 8.655 12.609 34.467 1.00 70.25 C
ANISOU 3340 C PHE A 321 10255 7940 8495 -799 159 101 C
ATOM 3341 O PHE A 321 9.332 12.624 33.432 1.00 71.19 O
ANISOU 3341 O PHE A 321 10334 8098 8618 -865 253 121 O
ATOM 3342 CB PHE A 321 9.981 11.722 36.377 1.00 67.72 C
ANISOU 3342 CB PHE A 321 9758 7729 8245 -754 5 -51 C
ATOM 3343 CG PHE A 321 10.979 12.018 37.460 1.00 70.19 C
ANISOU 3343 CG PHE A 321 9963 8098 8607 -806 -102 -140 C
ATOM 3344 CD1 PHE A 321 11.473 13.300 37.637 1.00 70.32 C
ANISOU 3344 CD1 PHE A 321 9976 8062 8681 -975 -102 -194 C
ATOM 3345 CD2 PHE A 321 11.425 11.012 38.300 1.00 72.70 C
ANISOU 3345 CD2 PHE A 321 10197 8520 8905 -694 -212 -164 C
ATOM 3346 CE1 PHE A 321 12.394 13.572 38.632 1.00 72.57 C
ANISOU 3346 CE1 PHE A 321 10151 8427 8994 -1063 -231 -296 C
ATOM 3347 CE2 PHE A 321 12.345 11.276 39.295 1.00 75.31 C
ANISOU 3347 CE2 PHE A 321 10413 8948 9254 -741 -351 -237 C
ATOM 3348 CZ PHE A 321 12.829 12.558 39.462 1.00 75.02 C
ANISOU 3348 CZ PHE A 321 10350 8888 9266 -941 -371 -316 C
ATOM 3349 N ASN A 322 7.364 12.280 34.471 1.00 71.52 N
ANISOU 3349 N ASN A 322 10497 8092 8584 -711 126 156 N
ATOM 3350 CA ASN A 322 6.702 11.883 33.231 1.00 71.18 C
ANISOU 3350 CA ASN A 322 10495 8097 8451 -704 159 233 C
ATOM 3351 C ASN A 322 6.697 12.966 32.155 1.00 71.41 C
ANISOU 3351 C ASN A 322 10595 8086 8452 -760 229 336 C
ATOM 3352 O ASN A 322 6.928 12.622 30.983 1.00 72.06 O
ANISOU 3352 O ASN A 322 10699 8236 8446 -803 287 367 O
ATOM 3353 CB ASN A 322 5.272 11.417 33.532 1.00 72.44 C
ANISOU 3353 CB ASN A 322 10682 8283 8557 -629 91 274 C
ATOM 3354 CG ASN A 322 5.234 10.075 34.229 1.00 72.26 C
ANISOU 3354 CG ASN A 322 10633 8294 8528 -599 56 202 C
ATOM 3355 OD1 ASN A 322 5.980 9.160 33.880 1.00 72.92 O
ANISOU 3355 OD1 ASN A 322 10703 8400 8602 -612 84 145 O
ATOM 3356 ND2 ASN A 322 4.361 9.948 35.220 1.00 71.81 N
ANISOU 3356 ND2 ASN A 322 10582 8228 8476 -547 17 212 N
ATOM 3357 N PRO A 323 6.434 14.246 32.448 1.00 70.99 N
ANISOU 3357 N PRO A 323 10613 7910 8451 -757 243 395 N
ATOM 3358 CA PRO A 323 6.434 15.243 31.362 1.00 71.42 C
ANISOU 3358 CA PRO A 323 10772 7897 8468 -798 322 528 C
ATOM 3359 C PRO A 323 7.778 15.409 30.672 1.00 72.21 C
ANISOU 3359 C PRO A 323 10850 8002 8582 -948 444 508 C
ATOM 3360 O PRO A 323 7.808 15.722 29.476 1.00 72.68 O
ANISOU 3360 O PRO A 323 10997 8073 8545 -987 525 624 O
ATOM 3361 CB PRO A 323 6.001 16.533 32.073 1.00 72.15 C
ANISOU 3361 CB PRO A 323 10966 7799 8648 -750 333 568 C
ATOM 3362 CG PRO A 323 5.239 16.069 33.256 1.00 71.77 C
ANISOU 3362 CG PRO A 323 10868 7778 8624 -639 248 492 C
ATOM 3363 CD PRO A 323 5.931 14.825 33.708 1.00 71.47 C
ANISOU 3363 CD PRO A 323 10706 7870 8579 -692 201 360 C
ATOM 3364 N LEU A 324 8.893 15.216 31.380 1.00 70.57 N
ANISOU 3364 N LEU A 324 10518 7810 8485 -1034 460 376 N
ATOM 3365 CA LEU A 324 10.196 15.327 30.729 1.00 72.02 C
ANISOU 3365 CA LEU A 324 10620 8037 8707 -1180 594 357 C
ATOM 3366 C LEU A 324 10.466 14.135 29.819 1.00 72.98 C
ANISOU 3366 C LEU A 324 10683 8320 8728 -1138 656 339 C
ATOM 3367 O LEU A 324 11.055 14.290 28.743 1.00 73.95 O
ANISOU 3367 O LEU A 324 10823 8481 8793 -1223 812 388 O
ATOM 3368 CB LEU A 324 11.307 15.469 31.769 1.00 74.42 C
ANISOU 3368 CB LEU A 324 10756 8355 9167 -1282 567 222 C
ATOM 3369 CG LEU A 324 11.597 16.879 32.290 1.00 74.33 C
ANISOU 3369 CG LEU A 324 10817 8167 9257 -1443 587 210 C
ATOM 3370 CD1 LEU A 324 10.500 17.383 33.217 1.00 72.91 C
ANISOU 3370 CD1 LEU A 324 10801 7836 9064 -1339 481 203 C
ATOM 3371 CD2 LEU A 324 12.953 16.910 32.980 1.00 76.35 C
ANISOU 3371 CD2 LEU A 324 10851 8512 9648 -1608 563 72 C
ATOM 3372 N ILE A 325 10.047 12.937 30.235 1.00 71.97 N
ANISOU 3372 N ILE A 325 10511 8267 8567 -1015 559 265 N
ATOM 3373 CA ILE A 325 10.192 11.762 29.386 1.00 73.16 C
ANISOU 3373 CA ILE A 325 10663 8521 8613 -971 627 226 C
ATOM 3374 C ILE A 325 9.302 11.876 28.156 1.00 72.43 C
ANISOU 3374 C ILE A 325 10749 8448 8321 -985 647 327 C
ATOM 3375 O ILE A 325 9.575 11.249 27.125 1.00 73.61 O
ANISOU 3375 O ILE A 325 10954 8675 8339 -1003 753 301 O
ATOM 3376 CB ILE A 325 9.880 10.489 30.196 1.00 69.28 C
ANISOU 3376 CB ILE A 325 10129 8053 8143 -850 522 132 C
ATOM 3377 CG1 ILE A 325 10.779 10.418 31.432 1.00 70.71 C
ANISOU 3377 CG1 ILE A 325 10140 8242 8487 -818 470 59 C
ATOM 3378 CG2 ILE A 325 10.100 9.242 29.354 1.00 71.12 C
ANISOU 3378 CG2 ILE A 325 10401 8340 8281 -806 616 64 C
ATOM 3379 CD1 ILE A 325 10.369 9.357 32.427 1.00 70.65 C
ANISOU 3379 CD1 ILE A 325 10131 8224 8488 -690 353 11 C
ATOM 3380 N TYR A 326 8.244 12.684 28.236 1.00 72.55 N
ANISOU 3380 N TYR A 326 10861 8404 8302 -966 547 443 N
ATOM 3381 CA TYR A 326 7.385 12.924 27.085 1.00 72.61 C
ANISOU 3381 CA TYR A 326 11016 8460 8111 -965 527 573 C
ATOM 3382 C TYR A 326 7.980 13.970 26.153 1.00 73.15 C
ANISOU 3382 C TYR A 326 11188 8487 8119 -1052 675 701 C
ATOM 3383 O TYR A 326 7.751 13.914 24.941 1.00 73.80 O
ANISOU 3383 O TYR A 326 11404 8653 7986 -1076 713 786 O
ATOM 3384 CB TYR A 326 5.995 13.341 27.562 1.00 73.43 C
ANISOU 3384 CB TYR A 326 11141 8539 8220 -868 361 667 C
ATOM 3385 CG TYR A 326 5.281 12.242 28.316 1.00 73.07 C
ANISOU 3385 CG TYR A 326 11009 8554 8201 -815 241 563 C
ATOM 3386 CD1 TYR A 326 5.662 10.912 28.168 1.00 73.60 C
ANISOU 3386 CD1 TYR A 326 11058 8683 8222 -852 265 424 C
ATOM 3387 CD2 TYR A 326 4.260 12.533 29.208 1.00 72.56 C
ANISOU 3387 CD2 TYR A 326 10894 8462 8215 -725 135 604 C
ATOM 3388 CE1 TYR A 326 5.025 9.905 28.863 1.00 73.38 C
ANISOU 3388 CE1 TYR A 326 10985 8672 8223 -825 177 343 C
ATOM 3389 CE2 TYR A 326 3.620 11.533 29.912 1.00 72.38 C
ANISOU 3389 CE2 TYR A 326 10796 8491 8215 -703 56 522 C
ATOM 3390 CZ TYR A 326 4.005 10.220 29.734 1.00 72.63 C
ANISOU 3390 CZ TYR A 326 10832 8567 8199 -765 73 398 C
ATOM 3391 OH TYR A 326 3.370 9.217 30.430 1.00 72.54 O
ANISOU 3391 OH TYR A 326 10780 8571 8213 -764 14 332 O
ATOM 3392 N CYS A 327 8.757 14.915 26.691 1.00 73.68 N
ANISOU 3392 N CYS A 327 11214 8426 8355 -1122 762 713 N
ATOM 3393 CA CYS A 327 9.562 15.792 25.847 1.00 74.42 C
ANISOU 3393 CA CYS A 327 11392 8466 8418 -1253 954 817 C
ATOM 3394 C CYS A 327 10.632 15.030 25.084 1.00 75.79 C
ANISOU 3394 C CYS A 327 11494 8778 8525 -1334 1135 732 C
ATOM 3395 O CYS A 327 11.339 15.629 24.267 1.00 76.55 O
ANISOU 3395 O CYS A 327 11652 8863 8569 -1458 1334 818 O
ATOM 3396 CB CYS A 327 10.220 16.890 26.683 1.00 75.59 C
ANISOU 3396 CB CYS A 327 11497 8438 8786 -1362 1010 810 C
ATOM 3397 SG CYS A 327 9.074 18.098 27.370 1.00 74.51 S
ANISOU 3397 SG CYS A 327 11525 8069 8715 -1262 890 930 S
ATOM 3398 N ARG A 328 10.784 13.740 25.347 1.00 73.10 N
ANISOU 3398 N ARG A 328 11034 8551 8190 -1261 1097 569 N
ATOM 3399 CA ARG A 328 11.644 12.880 24.556 1.00 74.78 C
ANISOU 3399 CA ARG A 328 11208 8887 8320 -1280 1283 478 C
ATOM 3400 C ARG A 328 10.925 12.302 23.339 1.00 74.81 C
ANISOU 3400 C ARG A 328 11431 8978 8017 -1254 1290 505 C
ATOM 3401 O ARG A 328 11.584 11.786 22.429 1.00 76.07 O
ANISOU 3401 O ARG A 328 11637 9225 8043 -1284 1491 446 O
ATOM 3402 CB ARG A 328 12.229 11.796 25.477 1.00 71.93 C
ANISOU 3402 CB ARG A 328 10632 8568 8131 -1187 1252 296 C
ATOM 3403 CG ARG A 328 12.962 10.674 24.807 1.00 74.00 C
ANISOU 3403 CG ARG A 328 10859 8930 8327 -1131 1434 177 C
ATOM 3404 CD ARG A 328 12.160 9.403 24.943 1.00 73.98 C
ANISOU 3404 CD ARG A 328 10958 8916 8234 -1008 1309 73 C
ATOM 3405 NE ARG A 328 12.706 8.341 24.113 1.00 75.73 N
ANISOU 3405 NE ARG A 328 11239 9190 8346 -950 1506 -50 N
ATOM 3406 CZ ARG A 328 13.804 7.654 24.399 1.00 77.98 C
ANISOU 3406 CZ ARG A 328 11342 9498 8787 -840 1655 -155 C
ATOM 3407 NH1 ARG A 328 14.510 7.940 25.484 1.00 79.14 N
ANISOU 3407 NH1 ARG A 328 11215 9658 9196 -798 1597 -144 N
ATOM 3408 NH2 ARG A 328 14.217 6.706 23.574 1.00 79.12 N
ANISOU 3408 NH2 ARG A 328 11581 9663 8817 -764 1864 -273 N
ATOM 3409 N SER A 329 9.597 12.433 23.271 1.00 75.77 N
ANISOU 3409 N SER A 329 11685 9093 8012 -1207 1080 592 N
ATOM 3410 CA SER A 329 8.799 12.147 22.083 1.00 76.03 C
ANISOU 3410 CA SER A 329 11930 9234 7724 -1216 1030 651 C
ATOM 3411 C SER A 329 8.747 13.372 21.171 1.00 76.10 C
ANISOU 3411 C SER A 329 12110 9231 7572 -1272 1102 883 C
ATOM 3412 O SER A 329 8.655 14.504 21.657 1.00 75.47 O
ANISOU 3412 O SER A 329 12014 9019 7641 -1264 1077 1028 O
ATOM 3413 CB SER A 329 7.380 11.741 22.470 1.00 75.16 C
ANISOU 3413 CB SER A 329 11824 9160 7572 -1147 751 653 C
ATOM 3414 OG SER A 329 6.566 11.559 21.324 1.00 75.75 O
ANISOU 3414 OG SER A 329 12080 9375 7328 -1179 656 718 O
ATOM 3415 N PRO A 330 8.818 13.180 19.850 1.00 77.50 N
ANISOU 3415 N PRO A 330 12486 9529 7433 -1329 1205 924 N
ATOM 3416 CA PRO A 330 8.731 14.337 18.943 1.00 77.80 C
ANISOU 3416 CA PRO A 330 12727 9552 7280 -1371 1273 1183 C
ATOM 3417 C PRO A 330 7.348 14.961 18.892 1.00 77.59 C
ANISOU 3417 C PRO A 330 12792 9533 7154 -1268 992 1389 C
ATOM 3418 O PRO A 330 7.237 16.178 18.699 1.00 77.69 O
ANISOU 3418 O PRO A 330 12918 9433 7166 -1244 1018 1634 O
ATOM 3419 CB PRO A 330 9.126 13.748 17.581 1.00 75.67 C
ANISOU 3419 CB PRO A 330 12658 9443 6649 -1449 1447 1139 C
ATOM 3420 CG PRO A 330 9.886 12.505 17.905 1.00 76.03 C
ANISOU 3420 CG PRO A 330 12560 9521 6808 -1454 1583 846 C
ATOM 3421 CD PRO A 330 9.236 11.960 19.142 1.00 75.24 C
ANISOU 3421 CD PRO A 330 12268 9362 6957 -1362 1332 729 C
ATOM 3422 N ASP A 331 6.288 14.166 19.052 1.00 80.38 N
ANISOU 3422 N ASP A 331 13094 10013 7435 -1203 733 1306 N
ATOM 3423 CA ASP A 331 4.938 14.712 18.965 1.00 80.75 C
ANISOU 3423 CA ASP A 331 13167 10121 7394 -1087 458 1508 C
ATOM 3424 C ASP A 331 4.582 15.545 20.190 1.00 80.00 C
ANISOU 3424 C ASP A 331 12920 9837 7638 -962 391 1591 C
ATOM 3425 O ASP A 331 3.851 16.535 20.070 1.00 80.58 O
ANISOU 3425 O ASP A 331 13057 9865 7693 -834 286 1837 O
ATOM 3426 CB ASP A 331 3.926 13.582 18.771 1.00 80.83 C
ANISOU 3426 CB ASP A 331 13128 10348 7238 -1099 210 1378 C
ATOM 3427 CG ASP A 331 3.980 12.981 17.376 1.00 81.83 C
ANISOU 3427 CG ASP A 331 13480 10673 6939 -1216 221 1338 C
ATOM 3428 OD1 ASP A 331 4.316 13.716 16.423 1.00 82.44 O
ANISOU 3428 OD1 ASP A 331 13768 10774 6781 -1227 327 1528 O
ATOM 3429 OD2 ASP A 331 3.683 11.777 17.232 1.00 82.05 O
ANISOU 3429 OD2 ASP A 331 13503 10821 6853 -1306 133 1114 O
ATOM 3430 N PHE A 332 5.080 15.171 21.371 1.00 78.09 N
ANISOU 3430 N PHE A 332 12496 9482 7693 -979 453 1395 N
ATOM 3431 CA PHE A 332 4.799 15.970 22.560 1.00 77.35 C
ANISOU 3431 CA PHE A 332 12297 9204 7889 -876 411 1445 C
ATOM 3432 C PHE A 332 5.564 17.288 22.542 1.00 77.21 C
ANISOU 3432 C PHE A 332 12401 8960 7976 -910 600 1588 C
ATOM 3433 O PHE A 332 5.035 18.317 22.977 1.00 77.23 O
ANISOU 3433 O PHE A 332 12452 8797 8097 -795 559 1738 O
ATOM 3434 CB PHE A 332 5.115 15.178 23.827 1.00 74.94 C
ANISOU 3434 CB PHE A 332 11790 8861 7822 -893 407 1201 C
ATOM 3435 CG PHE A 332 4.093 14.126 24.157 1.00 75.09 C
ANISOU 3435 CG PHE A 332 11695 9027 7808 -844 211 1102 C
ATOM 3436 CD1 PHE A 332 2.921 14.467 24.814 1.00 75.28 C
ANISOU 3436 CD1 PHE A 332 11625 9053 7925 -712 50 1185 C
ATOM 3437 CD2 PHE A 332 4.300 12.801 23.814 1.00 75.37 C
ANISOU 3437 CD2 PHE A 332 11721 9185 7730 -935 213 923 C
ATOM 3438 CE1 PHE A 332 1.975 13.507 25.122 1.00 75.75 C
ANISOU 3438 CE1 PHE A 332 11556 9259 7967 -703 -110 1100 C
ATOM 3439 CE2 PHE A 332 3.357 11.836 24.118 1.00 75.69 C
ANISOU 3439 CE2 PHE A 332 11676 9332 7749 -934 47 830 C
ATOM 3440 CZ PHE A 332 2.193 12.190 24.773 1.00 75.87 C
ANISOU 3440 CZ PHE A 332 11578 9381 7870 -834 -116 923 C
ATOM 3441 N ARG A 333 6.810 17.281 22.057 1.00 77.17 N
ANISOU 3441 N ARG A 333 12447 8932 7941 -1074 830 1539 N
ATOM 3442 CA ARG A 333 7.558 18.530 21.932 1.00 77.29 C
ANISOU 3442 CA ARG A 333 12588 8732 8045 -1164 1031 1682 C
ATOM 3443 C ARG A 333 6.812 19.534 21.066 1.00 78.13 C
ANISOU 3443 C ARG A 333 12951 8771 7965 -1064 996 1999 C
ATOM 3444 O ARG A 333 6.656 20.701 21.441 1.00 78.13 O
ANISOU 3444 O ARG A 333 13059 8517 8110 -1011 1032 2151 O
ATOM 3445 CB ARG A 333 8.953 18.268 21.361 1.00 75.85 C
ANISOU 3445 CB ARG A 333 12393 8599 7828 -1367 1300 1597 C
ATOM 3446 CG ARG A 333 9.923 17.677 22.355 1.00 75.50 C
ANISOU 3446 CG ARG A 333 12082 8561 8045 -1454 1367 1338 C
ATOM 3447 CD ARG A 333 11.295 17.466 21.739 1.00 76.55 C
ANISOU 3447 CD ARG A 333 12154 8771 8161 -1629 1652 1275 C
ATOM 3448 NE ARG A 333 11.316 16.352 20.798 1.00 77.30 N
ANISOU 3448 NE ARG A 333 12289 9081 7999 -1593 1705 1201 N
ATOM 3449 CZ ARG A 333 12.363 16.034 20.045 1.00 78.44 C
ANISOU 3449 CZ ARG A 333 12413 9328 8063 -1700 1981 1151 C
ATOM 3450 NH1 ARG A 333 13.476 16.752 20.119 1.00 79.03 N
ANISOU 3450 NH1 ARG A 333 12386 9332 8308 -1869 2220 1184 N
ATOM 3451 NH2 ARG A 333 12.299 15.000 19.218 1.00 79.12 N
ANISOU 3451 NH2 ARG A 333 12580 9586 7897 -1652 2032 1057 N
ATOM 3452 N ILE A 334 6.337 19.094 19.899 1.00 80.24 N
ANISOU 3452 N ILE A 334 13338 9253 7895 -1030 922 2104 N
ATOM 3453 CA ILE A 334 5.565 19.977 19.033 1.00 81.38 C
ANISOU 3453 CA ILE A 334 13721 9378 7821 -900 844 2436 C
ATOM 3454 C ILE A 334 4.268 20.395 19.713 1.00 81.65 C
ANISOU 3454 C ILE A 334 13676 9363 7986 -650 595 2544 C
ATOM 3455 O ILE A 334 3.790 21.520 19.524 1.00 82.47 O
ANISOU 3455 O ILE A 334 13948 9296 8091 -495 583 2824 O
ATOM 3456 CB ILE A 334 5.317 19.287 17.678 1.00 83.01 C
ANISOU 3456 CB ILE A 334 14061 9882 7597 -931 777 2492 C
ATOM 3457 CG1 ILE A 334 6.650 19.025 16.973 1.00 82.99 C
ANISOU 3457 CG1 ILE A 334 14165 9902 7466 -1155 1094 2406 C
ATOM 3458 CG2 ILE A 334 4.410 20.126 16.794 1.00 84.49 C
ANISOU 3458 CG2 ILE A 334 14477 10102 7522 -764 632 2858 C
ATOM 3459 CD1 ILE A 334 6.532 18.158 15.742 1.00 83.90 C
ANISOU 3459 CD1 ILE A 334 14421 10309 7147 -1209 1065 2372 C
ATOM 3460 N ALA A 335 3.691 19.514 20.533 1.00 81.06 N
ANISOU 3460 N ALA A 335 13346 9418 8034 -596 418 2334 N
ATOM 3461 CA ALA A 335 2.464 19.854 21.243 1.00 81.61 C
ANISOU 3461 CA ALA A 335 13295 9466 8245 -359 217 2419 C
ATOM 3462 C ALA A 335 2.729 20.793 22.413 1.00 80.74 C
ANISOU 3462 C ALA A 335 13190 9017 8472 -301 349 2397 C
ATOM 3463 O ALA A 335 1.968 21.742 22.634 1.00 81.57 O
ANISOU 3463 O ALA A 335 13362 8967 8663 -78 304 2594 O
ATOM 3464 CB ALA A 335 1.771 18.585 21.732 1.00 77.62 C
ANISOU 3464 CB ALA A 335 12527 9212 7754 -357 19 2204 C
ATOM 3465 N PHE A 336 3.796 20.542 23.177 1.00 79.89 N
ANISOU 3465 N PHE A 336 13014 8792 8549 -491 507 2154 N
ATOM 3466 CA PHE A 336 4.103 21.394 24.321 1.00 79.13 C
ANISOU 3466 CA PHE A 336 12937 8386 8742 -483 616 2091 C
ATOM 3467 C PHE A 336 4.450 22.810 23.881 1.00 79.64 C
ANISOU 3467 C PHE A 336 13290 8139 8830 -490 789 2320 C
ATOM 3468 O PHE A 336 4.060 23.785 24.535 1.00 79.77 O
ANISOU 3468 O PHE A 336 13412 7875 9020 -355 822 2389 O
ATOM 3469 CB PHE A 336 5.254 20.798 25.132 1.00 73.59 C
ANISOU 3469 CB PHE A 336 12088 7675 8196 -706 716 1795 C
ATOM 3470 CG PHE A 336 4.895 19.540 25.870 1.00 72.95 C
ANISOU 3470 CG PHE A 336 11764 7805 8149 -671 566 1577 C
ATOM 3471 CD1 PHE A 336 3.572 19.172 26.046 1.00 73.52 C
ANISOU 3471 CD1 PHE A 336 11744 8010 8179 -475 378 1624 C
ATOM 3472 CD2 PHE A 336 5.884 18.728 26.394 1.00 72.10 C
ANISOU 3472 CD2 PHE A 336 11509 7762 8122 -832 620 1340 C
ATOM 3473 CE1 PHE A 336 3.245 18.015 26.729 1.00 73.03 C
ANISOU 3473 CE1 PHE A 336 11481 8116 8151 -475 268 1436 C
ATOM 3474 CE2 PHE A 336 5.565 17.570 27.078 1.00 71.55 C
ANISOU 3474 CE2 PHE A 336 11258 7849 8080 -791 498 1166 C
ATOM 3475 CZ PHE A 336 4.243 17.214 27.246 1.00 71.88 C
ANISOU 3475 CZ PHE A 336 11244 7994 8074 -629 332 1213 C
ATOM 3476 N GLN A 337 5.187 22.944 22.775 1.00 83.21 N
ANISOU 3476 N GLN A 337 13897 8613 9104 -649 927 2439 N
ATOM 3477 CA GLN A 337 5.623 24.263 22.327 1.00 83.75 C
ANISOU 3477 CA GLN A 337 14267 8360 9193 -704 1130 2668 C
ATOM 3478 C GLN A 337 4.440 25.128 21.906 1.00 84.99 C
ANISOU 3478 C GLN A 337 14627 8398 9268 -387 1028 3001 C
ATOM 3479 O GLN A 337 4.446 26.345 22.129 1.00 85.28 O
ANISOU 3479 O GLN A 337 14902 8054 9446 -326 1160 3153 O
ATOM 3480 CB GLN A 337 6.630 24.116 21.187 1.00 87.97 C
ANISOU 3480 CB GLN A 337 14913 8988 9524 -945 1321 2735 C
ATOM 3481 CG GLN A 337 7.951 23.487 21.618 1.00 87.17 C
ANISOU 3481 CG GLN A 337 14604 8957 9558 -1243 1477 2437 C
ATOM 3482 CD GLN A 337 8.909 23.276 20.460 1.00 87.82 C
ANISOU 3482 CD GLN A 337 14764 9167 9435 -1455 1700 2497 C
ATOM 3483 OE1 GLN A 337 8.587 23.573 19.310 1.00 88.72 O
ANISOU 3483 OE1 GLN A 337 15122 9320 9267 -1397 1735 2760 O
ATOM 3484 NE2 GLN A 337 10.090 22.742 20.758 1.00 87.60 N
ANISOU 3484 NE2 GLN A 337 14522 9225 9535 -1688 1854 2260 N
ATOM 3485 N GLU A 338 3.419 24.523 21.294 1.00 86.39 N
ANISOU 3485 N GLU A 338 14713 8891 9220 -182 789 3119 N
ATOM 3486 CA GLU A 338 2.196 25.262 20.988 1.00 87.89 C
ANISOU 3486 CA GLU A 338 15013 9030 9353 170 644 3438 C
ATOM 3487 C GLU A 338 1.510 25.752 22.257 1.00 87.69 C
ANISOU 3487 C GLU A 338 14891 8789 9639 395 614 3367 C
ATOM 3488 O GLU A 338 1.125 26.923 22.355 1.00 88.35 O
ANISOU 3488 O GLU A 338 15192 8545 9830 614 692 3590 O
ATOM 3489 CB GLU A 338 1.243 24.397 20.163 1.00 95.97 C
ANISOU 3489 CB GLU A 338 15884 10502 10078 304 352 3534 C
ATOM 3490 CG GLU A 338 1.556 24.361 18.682 1.00 96.88 C
ANISOU 3490 CG GLU A 338 16225 10777 9808 210 364 3748 C
ATOM 3491 CD GLU A 338 1.222 25.682 18.009 1.00 98.24 C
ANISOU 3491 CD GLU A 338 16728 10712 9886 432 409 4182 C
ATOM 3492 OE1 GLU A 338 0.272 26.353 18.469 1.00 99.06 O
ANISOU 3492 OE1 GLU A 338 16803 10684 10150 762 300 4351 O
ATOM 3493 OE2 GLU A 338 1.901 26.050 17.027 1.00 98.53 O
ANISOU 3493 OE2 GLU A 338 17060 10687 9689 293 571 4365 O
ATOM 3494 N LEU A 339 1.339 24.864 23.239 1.00 83.39 N
ANISOU 3494 N LEU A 339 14046 8408 9231 355 522 3063 N
ATOM 3495 CA LEU A 339 0.677 25.262 24.477 1.00 83.29 C
ANISOU 3495 CA LEU A 339 13944 8219 9482 563 517 2976 C
ATOM 3496 C LEU A 339 1.480 26.326 25.212 1.00 82.36 C
ANISOU 3496 C LEU A 339 14075 7626 9592 457 771 2897 C
ATOM 3497 O LEU A 339 0.909 27.262 25.782 1.00 82.84 O
ANISOU 3497 O LEU A 339 14268 7389 9818 698 838 2979 O
ATOM 3498 CB LEU A 339 0.453 24.043 25.368 1.00 78.53 C
ANISOU 3498 CB LEU A 339 13003 7886 8948 495 396 2668 C
ATOM 3499 CG LEU A 339 -0.508 22.995 24.805 1.00 79.82 C
ANISOU 3499 CG LEU A 339 12909 8492 8925 586 138 2715 C
ATOM 3500 CD1 LEU A 339 -0.569 21.785 25.720 1.00 79.06 C
ANISOU 3500 CD1 LEU A 339 12533 8596 8910 466 69 2405 C
ATOM 3501 CD2 LEU A 339 -1.894 23.587 24.591 1.00 81.81 C
ANISOU 3501 CD2 LEU A 339 13104 8804 9178 966 -3 2995 C
ATOM 3502 N LEU A 340 2.807 26.203 25.206 1.00 82.90 N
ANISOU 3502 N LEU A 340 14205 7616 9676 94 922 2729 N
ATOM 3503 CA LEU A 340 3.657 27.205 25.833 1.00 82.36 C
ANISOU 3503 CA LEU A 340 14365 7117 9812 -84 1150 2639 C
ATOM 3504 C LEU A 340 3.854 28.437 24.961 1.00 83.29 C
ANISOU 3504 C LEU A 340 14866 6891 9890 -70 1326 2954 C
ATOM 3505 O LEU A 340 4.421 29.426 25.440 1.00 83.19 O
ANISOU 3505 O LEU A 340 15099 6454 10057 -208 1528 2909 O
ATOM 3506 CB LEU A 340 5.017 26.598 26.181 1.00 82.18 C
ANISOU 3506 CB LEU A 340 14204 7182 9838 -489 1231 2346 C
ATOM 3507 CG LEU A 340 4.999 25.490 27.234 1.00 81.19 C
ANISOU 3507 CG LEU A 340 13755 7310 9782 -520 1089 2028 C
ATOM 3508 CD1 LEU A 340 6.390 24.909 27.410 1.00 80.40 C
ANISOU 3508 CD1 LEU A 340 13510 7320 9719 -879 1160 1795 C
ATOM 3509 CD2 LEU A 340 4.451 26.005 28.555 1.00 81.08 C
ANISOU 3509 CD2 LEU A 340 13779 7070 9957 -373 1085 1892 C
ATOM 3510 N CYS A 341 3.398 28.398 23.711 1.00 86.10 N
ANISOU 3510 N CYS A 341 15299 7413 10001 78 1253 3269 N
ATOM 3511 CA CYS A 341 3.498 29.516 22.775 1.00 87.15 C
ANISOU 3511 CA CYS A 341 15823 7243 10047 128 1408 3629 C
ATOM 3512 C CYS A 341 4.943 30.007 22.672 1.00 86.64 C
ANISOU 3512 C CYS A 341 15942 6918 10059 -308 1692 3541 C
ATOM 3513 O CYS A 341 5.267 31.163 22.952 1.00 88.04 O
ANISOU 3513 O CYS A 341 16290 6724 10437 -373 1846 3534 O
ATOM 3514 CB CYS A 341 2.547 30.646 23.176 1.00 91.99 C
ANISOU 3514 CB CYS A 341 16619 7508 10827 505 1417 3808 C
ATOM 3515 SG CYS A 341 2.434 31.999 21.982 1.00 97.06 S
ANISOU 3515 SG CYS A 341 17532 7946 11402 630 1488 4183 S
ATOM 3516 N LEU A 342 5.816 29.092 22.266 1.00 89.47 N
ANISOU 3516 N LEU A 342 16118 7586 10290 -611 1716 3394 N
ATOM 3517 CA LEU A 342 7.243 29.376 22.196 1.00 89.19 C
ANISOU 3517 CA LEU A 342 16154 7394 10338 -1049 1984 3284 C
ATOM 3518 C LEU A 342 7.659 29.755 20.777 1.00 91.05 C
ANISOU 3518 C LEU A 342 16531 7702 10361 -1136 2109 3543 C
ATOM 3519 O LEU A 342 7.588 28.937 19.859 1.00 90.88 O
ANISOU 3519 O LEU A 342 16461 8026 10043 -1116 2051 3639 O
ATOM 3520 CB LEU A 342 8.049 28.168 22.683 1.00 85.48 C
ANISOU 3520 CB LEU A 342 15286 7276 9915 -1299 1935 2914 C
ATOM 3521 CG LEU A 342 7.849 27.780 24.152 1.00 84.49 C
ANISOU 3521 CG LEU A 342 14915 7165 10021 -1255 1786 2583 C
ATOM 3522 CD1 LEU A 342 8.590 26.491 24.491 1.00 83.69 C
ANISOU 3522 CD1 LEU A 342 14434 7439 9926 -1444 1718 2279 C
ATOM 3523 CD2 LEU A 342 8.278 28.909 25.078 1.00 84.50 C
ANISOU 3523 CD2 LEU A 342 15105 6709 10291 -1415 1936 2479 C
TER 3524 LEU A 342
HETATM 3581 C1 JTZ A1203 0.374 8.005 53.099 1.00 76.39 C
ANISOU 3581 C1 JTZ A1203 12862 8978 7184 48 575 163 C
HETATM 3582 N1 JTZ A1203 2.550 6.923 52.508 1.00 75.90 N
ANISOU 3582 N1 JTZ A1203 12719 8940 7181 54 99 245 N
HETATM 3583 O1 JTZ A1203 2.874 7.493 49.346 1.00 74.46 O
ANISOU 3583 O1 JTZ A1203 12001 8638 7653 -46 26 164 O
HETATM 3584 C2 JTZ A1203 1.832 7.736 53.483 1.00 76.35 C
ANISOU 3584 C2 JTZ A1203 12954 9024 7032 57 266 148 C
HETATM 3585 O2 JTZ A1203 2.113 4.019 50.050 1.00 72.58 O
ANISOU 3585 O2 JTZ A1203 12008 8292 7278 -2 191 582 O
HETATM 3586 C3 JTZ A1203 2.608 9.029 53.711 1.00 76.71 C
ANISOU 3586 C3 JTZ A1203 13044 9091 7010 26 111 -75 C
HETATM 3587 C4 JTZ A1203 1.761 6.618 51.325 1.00 74.70 C
ANISOU 3587 C4 JTZ A1203 12367 8708 7308 9 243 303 C
HETATM 3588 C5 JTZ A1203 2.681 6.315 50.142 1.00 74.16 C
ANISOU 3588 C5 JTZ A1203 12112 8609 7458 -3 64 305 C
HETATM 3589 C6 JTZ A1203 2.087 5.194 49.293 1.00 72.75 C
ANISOU 3589 C6 JTZ A1203 11850 8349 7442 -42 168 434 C
HETATM 3590 C7 JTZ A1203 1.458 2.939 49.447 1.00 71.54 C
ANISOU 3590 C7 JTZ A1203 11860 8052 7271 -74 319 691 C
HETATM 3591 C8 JTZ A1203 0.694 3.123 48.303 1.00 70.78 C
ANISOU 3591 C8 JTZ A1203 11568 7940 7384 -188 408 642 C
HETATM 3592 C9 JTZ A1203 0.051 2.041 47.719 1.00 70.07 C
ANISOU 3592 C9 JTZ A1203 11472 7751 7401 -304 515 724 C
HETATM 3593 C10 JTZ A1203 0.164 0.775 48.274 1.00 70.08 C
ANISOU 3593 C10 JTZ A1203 11686 7623 7319 -300 566 863 C
HETATM 3594 C11 JTZ A1203 0.924 0.598 49.417 1.00 70.77 C
ANISOU 3594 C11 JTZ A1203 11978 7712 7200 -149 489 943 C
HETATM 3595 C12 JTZ A1203 1.569 1.677 50.003 1.00 71.52 C
ANISOU 3595 C12 JTZ A1203 12054 7952 7169 -39 351 853 C
HETATM 3596 C13 JTZ A1203 2.405 1.465 51.264 1.00 72.59 C
ANISOU 3596 C13 JTZ A1203 12408 8132 7041 111 223 939 C
HETATM 3597 C14 JTZ A1203 1.635 0.709 52.344 1.00 72.77 C
ANISOU 3597 C14 JTZ A1203 12693 8101 6854 90 410 1112 C
HETATM 3598 C15 JTZ A1203 2.532 -0.240 53.135 1.00 73.60 C
ANISOU 3598 C15 JTZ A1203 13042 8153 6770 257 277 1295 C
HETATM 3599 C10 M3J A1204 -2.465 -7.805 33.650 0.79 70.43 C
ANISOU 3599 C10 M3J A1204 12323 6380 8058 -2673 657 -558 C
HETATM 3600 N12 M3J A1204 -3.870 -7.049 37.562 0.79 70.38 N
ANISOU 3600 N12 M3J A1204 11936 6557 8249 -2531 816 41 N
HETATM 3601 C13 M3J A1204 -3.808 -7.632 38.789 0.79 70.30 C
ANISOU 3601 C13 M3J A1204 12113 6335 8262 -2463 971 200 C
HETATM 3602 C15 M3J A1204 -4.097 -9.582 40.217 0.79 70.89 C
ANISOU 3602 C15 M3J A1204 12724 5835 8375 -2637 1304 394 C
HETATM 3603 C02 M3J A1204 -3.057 -5.524 39.638 0.79 69.38 C
ANISOU 3603 C02 M3J A1204 11627 6643 8094 -1947 816 342 C
HETATM 3604 C04 M3J A1204 -3.541 -5.778 37.390 0.79 70.01 C
ANISOU 3604 C04 M3J A1204 11629 6797 8174 -2305 682 58 C
HETATM 3605 C06 M3J A1204 -3.503 -6.018 34.873 0.79 70.57 C
ANISOU 3605 C06 M3J A1204 11743 6929 8142 -2580 514 -274 C
HETATM 3606 C07 M3J A1204 -4.349 -5.779 33.804 0.79 71.68 C
ANISOU 3606 C07 M3J A1204 11713 7307 8216 -2858 371 -387 C
HETATM 3607 C08 M3J A1204 -4.254 -6.550 32.658 0.79 71.98 C
ANISOU 3607 C08 M3J A1204 11975 7215 8159 -3074 353 -596 C
HETATM 3608 C09 M3J A1204 -3.313 -7.563 32.582 0.79 71.31 C
ANISOU 3608 C09 M3J A1204 12290 6732 8074 -2987 511 -695 C
HETATM 3609 C11 M3J A1204 -2.561 -7.032 34.795 0.79 70.01 C
ANISOU 3609 C11 M3J A1204 12041 6488 8073 -2482 642 -347 C
HETATM 3610 C14 M3J A1204 -4.164 -9.003 38.958 0.79 70.82 C
ANISOU 3610 C14 M3J A1204 12495 6048 8363 -2718 1138 198 C
HETATM 3611 C16 M3J A1204 -3.682 -8.819 41.311 0.79 70.47 C
ANISOU 3611 C16 M3J A1204 12574 5935 8266 -2311 1288 572 C
HETATM 3612 C18 M3J A1204 -3.335 -7.483 41.149 0.79 69.93 C
ANISOU 3612 C18 M3J A1204 12196 6208 8166 -2084 1119 541 C
HETATM 3613 C19 M3J A1204 -3.402 -6.889 39.858 0.79 69.83 C
ANISOU 3613 C19 M3J A1204 11965 6392 8176 -2162 969 361 C
HETATM 3614 N01 M3J A1204 -2.619 -4.689 40.742 0.79 68.96 N
ANISOU 3614 N01 M3J A1204 11499 6707 7996 -1662 803 474 N
HETATM 3615 N03 M3J A1204 -3.139 -5.024 38.412 0.79 69.47 N
ANISOU 3615 N03 M3J A1204 11473 6819 8104 -2024 688 201 N
HETATM 3616 N05 M3J A1204 -3.618 -5.195 36.065 0.79 70.32 N
ANISOU 3616 N05 M3J A1204 11509 7045 8165 -2378 527 -81 N
HETATM 3617 BR1 M3J A1204 -3.587 -9.629 43.068 0.79 70.81 BR
ANISOU 3617 BR1 M3J A1204 12966 5697 8243 -2191 1505 867 BR
END
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