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*** ***elNémo ID: 2511261720261317523Job options:ID = 2511261720261317523 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -50 DQMAX = 50 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:ATOM 1 N HIS A 0 -14.219 34.302 47.176 1.00 98.76 N ANISOU 1 N HIS A 0 17049 9783 10692 -475 5776 -1340 N ATOM 2 CA HIS A 0 -15.042 33.152 46.819 1.00130.71 C ANISOU 2 CA HIS A 0 20601 13995 15067 -308 5781 -1109 C ATOM 3 C HIS A 0 -14.232 31.869 46.969 1.00126.00 C ANISOU 3 C HIS A 0 19642 13698 14532 -557 5674 -1126 C ATOM 4 O HIS A 0 -13.083 31.804 46.528 1.00115.21 O ANISOU 4 O HIS A 0 18335 12394 13043 -905 5529 -1358 O ATOM 5 CB HIS A 0 -15.576 33.299 45.391 1.00127.25 C ANISOU 5 CB HIS A 0 20177 13342 14830 -323 5593 -997 C ATOM 6 CG HIS A 0 -15.922 32.001 44.728 1.00138.98 C ANISOU 6 CG HIS A 0 21138 15023 16644 -346 5467 -799 C ATOM 7 CD2 HIS A 0 -15.519 31.471 43.550 1.00135.75 C ANISOU 7 CD2 HIS A 0 20573 14654 16353 -629 5260 -811 C ATOM 8 ND1 HIS A 0 -16.791 31.085 45.282 1.00146.92 N ANISOU 8 ND1 HIS A 0 21713 16235 17874 -88 5534 -571 N ATOM 9 CE1 HIS A 0 -16.907 30.047 44.472 1.00139.81 C ANISOU 9 CE1 HIS A 0 20451 15432 17240 -185 5345 -426 C ATOM 10 NE2 HIS A 0 -16.143 30.255 43.415 1.00133.68 N ANISOU 10 NE2 HIS A 0 19809 14563 16420 -483 5183 -589 N ATOM 11 N MET A 1 -14.829 30.857 47.600 1.00142.19 N ANISOU 11 N MET A 1 21316 15950 16758 -397 5685 -908 N ATOM 12 CA MET A 1 -14.103 29.624 47.878 1.00147.37 C ANISOU 12 CA MET A 1 21702 16807 17484 -586 5472 -923 C ATOM 13 C MET A 1 -13.670 28.955 46.579 1.00150.43 C ANISOU 13 C MET A 1 21857 17208 18093 -763 5179 -1006 C ATOM 14 O MET A 1 -14.481 28.727 45.676 1.00155.70 O ANISOU 14 O MET A 1 22341 17812 19006 -669 5121 -812 O ATOM 15 CB MET A 1 -14.952 28.666 48.727 1.00148.64 C ANISOU 15 CB MET A 1 21580 17138 17758 -460 5469 -606 C ATOM 16 CG MET A 1 -16.199 28.083 48.068 1.00139.72 C ANISOU 16 CG MET A 1 20121 16037 16928 -310 5422 -291 C ATOM 17 SD MET A 1 -17.443 29.293 47.587 1.00128.60 S ANISOU 17 SD MET A 1 18802 14504 15556 25 5702 -255 S ATOM 18 CE MET A 1 -18.741 28.214 46.983 1.00118.20 C ANISOU 18 CE MET A 1 16994 13328 14587 131 5594 110 C ATOM 19 N SER A 2 -12.376 28.660 46.483 1.00134.66 N ANISOU 19 N SER A 2 19837 15331 15995 -1016 4990 -1347 N ATOM 20 CA SER A 2 -11.818 28.081 45.270 1.00121.53 C ANISOU 20 CA SER A 2 17906 13781 14490 -1210 4713 -1565 C ATOM 21 C SER A 2 -10.416 27.574 45.557 1.00113.63 C ANISOU 21 C SER A 2 16785 13006 13385 -1401 4473 -2019 C ATOM 22 O SER A 2 -9.630 28.248 46.228 1.00111.24 O ANISOU 22 O SER A 2 16749 12753 12765 -1528 4609 -2262 O ATOM 23 CB SER A 2 -11.774 29.103 44.131 1.00113.39 C ANISOU 23 CB SER A 2 17094 12674 13313 -1426 4828 -1673 C ATOM 24 OG SER A 2 -10.517 29.753 44.103 1.00111.96 O ANISOU 24 OG SER A 2 17132 12639 12769 -1786 4857 -2101 O ATOM 25 N THR A 3 -10.106 26.404 45.008 1.00117.26 N ANISOU 25 N THR A 3 16833 13604 14118 -1399 4083 -2177 N ATOM 26 CA THR A 3 -8.850 25.717 45.256 1.00103.55 C ANISOU 26 CA THR A 3 14889 12086 12369 -1478 3729 -2677 C ATOM 27 C THR A 3 -8.574 24.778 44.091 1.00106.39 C ANISOU 27 C THR A 3 14775 12634 13015 -1507 3337 -2972 C ATOM 28 O THR A 3 -9.430 24.555 43.231 1.00 78.81 O ANISOU 28 O THR A 3 11137 9062 9744 -1458 3344 -2694 O ATOM 29 CB THR A 3 -8.897 24.962 46.585 1.00109.64 C ANISOU 29 CB THR A 3 15716 12723 13221 -1276 3504 -2493 C ATOM 30 CG2 THR A 3 -8.517 25.868 47.754 1.00102.02 C ANISOU 30 CG2 THR A 3 15146 11732 11884 -1335 3815 -2516 C ATOM 31 OG1 THR A 3 -10.215 24.427 46.772 1.00114.54 O ANISOU 31 OG1 THR A 3 16310 13139 14070 -1095 3499 -1903 O ATOM 32 N THR A 4 -7.356 24.238 44.057 1.00115.61 N ANISOU 32 N THR A 4 15672 14079 14175 -1570 2979 -3595 N ATOM 33 CA THR A 4 -6.973 23.311 42.997 1.00103.78 C ANISOU 33 CA THR A 4 13658 12829 12945 -1563 2554 -4023 C ATOM 34 C THR A 4 -7.143 21.861 43.429 1.00107.91 C ANISOU 34 C THR A 4 13967 13142 13890 -1209 1938 -3949 C ATOM 35 O THR A 4 -7.975 21.133 42.878 1.00114.09 O ANISOU 35 O THR A 4 14577 13766 15006 -1067 1738 -3632 O ATOM 36 CB THR A 4 -5.522 23.539 42.568 1.00102.66 C ANISOU 36 CB THR A 4 13250 13211 12544 -1838 2463 -4890 C ATOM 37 CG2 THR A 4 -5.392 24.812 41.756 1.00105.74 C ANISOU 37 CG2 THR A 4 13759 13842 12573 -2270 2862 -4768 C ATOM 38 OG1 THR A 4 -4.683 23.610 43.728 1.00 95.82 O ANISOU 38 OG1 THR A 4 12518 12364 11527 -1753 2329 -5069 O ATOM 39 N GLY A 5 -6.358 21.440 44.418 1.00 95.89 N ANISOU 39 N GLY A 5 12498 11590 12347 -1087 1588 -4231 N ATOM 40 CA GLY A 5 -6.307 20.051 44.830 1.00 91.55 C ANISOU 40 CA GLY A 5 11811 10806 12167 -791 844 -4260 C ATOM 41 C GLY A 5 -7.587 19.474 45.400 1.00 93.27 C ANISOU 41 C GLY A 5 12292 10572 12575 -674 753 -3424 C ATOM 42 O GLY A 5 -7.595 18.332 45.865 1.00 97.69 O ANISOU 42 O GLY A 5 12865 10864 13389 -502 82 -3351 O ATOM 43 N GLN A 6 -8.672 20.236 45.372 1.00 88.65 N ANISOU 43 N GLN A 6 11921 9909 11852 -784 1369 -2819 N ATOM 44 CA GLN A 6 -9.944 19.767 45.886 1.00 90.99 C ANISOU 44 CA GLN A 6 12401 9909 12262 -735 1363 -2070 C ATOM 45 C GLN A 6 -10.849 19.345 44.736 1.00 86.54 C ANISOU 45 C GLN A 6 11563 9323 11995 -684 1339 -1823 C ATOM 46 O GLN A 6 -10.438 19.288 43.573 1.00 73.24 O ANISOU 46 O GLN A 6 9546 7828 10454 -676 1249 -2244 O ATOM 47 CB GLN A 6 -10.610 20.852 46.729 1.00 84.06 C ANISOU 47 CB GLN A 6 11889 9010 11038 -838 2029 -1628 C ATOM 48 CG GLN A 6 -9.647 21.697 47.548 1.00 94.31 C ANISOU 48 CG GLN A 6 13438 10412 11985 -922 2253 -1963 C ATOM 49 CD GLN A 6 -8.796 20.896 48.495 1.00108.94 C ANISOU 49 CD GLN A 6 15382 12165 13847 -886 1681 -2181 C ATOM 50 NE2 GLN A 6 -7.477 21.045 48.392 1.00107.69 N ANISOU 50 NE2 GLN A 6 15115 12185 13618 -881 1495 -2863 N ATOM 51 OE1 GLN A 6 -9.320 20.157 49.323 1.00109.22 O ANISOU 51 OE1 GLN A 6 15596 11979 13924 -898 1385 -1752 O ATOM 52 N ILE A 7 -12.107 19.068 45.064 1.00 77.89 N ANISOU 52 N ILE A 7 10587 8049 10958 -687 1443 -1153 N ATOM 53 CA ILE A 7 -13.098 18.728 44.055 1.00 80.92 C ANISOU 53 CA ILE A 7 10735 8409 11603 -644 1473 -854 C ATOM 54 C ILE A 7 -13.654 20.005 43.432 1.00 68.31 C ANISOU 54 C ILE A 7 9159 6947 9848 -682 2174 -757 C ATOM 55 O ILE A 7 -13.531 21.105 43.978 1.00 80.52 O ANISOU 55 O ILE A 7 10966 8548 11078 -737 2635 -780 O ATOM 56 CB ILE A 7 -14.213 17.865 44.670 1.00 70.87 C ANISOU 56 CB ILE A 7 9564 6942 10420 -683 1262 -206 C ATOM 57 CG1 ILE A 7 -13.639 16.997 45.793 1.00 80.88 C ANISOU 57 CG1 ILE A 7 11069 8016 11645 -745 658 -207 C ATOM 58 CG2 ILE A 7 -14.869 16.991 43.614 1.00 80.53 C ANISOU 58 CG2 ILE A 7 10492 8093 12014 -617 950 -39 C ATOM 59 CD1 ILE A 7 -14.652 16.090 46.448 1.00 76.05 C ANISOU 59 CD1 ILE A 7 10627 7232 11038 -924 370 442 C ATOM 60 N ILE A 8 -14.267 19.858 42.260 1.00 76.93 N ANISOU 60 N ILE A 8 10003 8058 11168 -647 2198 -657 N ATOM 61 CA ILE A 8 -14.861 20.979 41.541 1.00 76.32 C ANISOU 61 CA ILE A 8 9978 8035 10986 -676 2731 -547 C ATOM 62 C ILE A 8 -16.318 20.651 41.256 1.00 76.32 C ANISOU 62 C ILE A 8 9870 7939 11190 -569 2819 1 C ATOM 63 O ILE A 8 -16.621 19.591 40.705 1.00 88.15 O ANISOU 63 O ILE A 8 11104 9396 12993 -533 2441 111 O ATOM 64 CB ILE A 8 -14.110 21.284 40.231 1.00 70.74 C ANISOU 64 CB ILE A 8 9081 7504 10295 -811 2697 -1030 C ATOM 65 CG1 ILE A 8 -12.863 22.121 40.518 1.00 64.32 C ANISOU 65 CG1 ILE A 8 8445 6863 9130 -998 2842 -1537 C ATOM 66 CG2 ILE A 8 -15.019 22.007 39.246 1.00 76.25 C ANISOU 66 CG2 ILE A 8 9802 8156 11012 -841 3030 -775 C ATOM 67 CD1 ILE A 8 -12.121 22.548 39.273 1.00 64.03 C ANISOU 67 CD1 ILE A 8 8243 7103 8980 -1271 2867 -2025 C ATOM 68 N ARG A 9 -17.217 21.551 41.625 1.00 82.04 N ANISOU 68 N ARG A 9 10778 8645 11750 -504 3288 300 N ATOM 69 CA ARG A 9 -18.641 21.358 41.388 1.00 89.15 C ANISOU 69 CA ARG A 9 11534 9530 12808 -391 3417 754 C ATOM 70 C ARG A 9 -19.030 22.197 40.176 1.00 82.79 C ANISOU 70 C ARG A 9 10709 8675 12072 -325 3639 702 C ATOM 71 O ARG A 9 -18.820 23.415 40.175 1.00 92.21 O ANISOU 71 O ARG A 9 12178 9818 13041 -321 3932 538 O ATOM 72 CB ARG A 9 -19.447 21.753 42.625 1.00 94.22 C ANISOU 72 CB ARG A 9 12324 10258 13219 -339 3745 1039 C ATOM 73 CG ARG A 9 -20.736 20.985 42.799 1.00108.23 C ANISOU 73 CG ARG A 9 13872 12141 15111 -336 3714 1489 C ATOM 74 CD ARG A 9 -21.024 20.626 44.244 1.00119.07 C ANISOU 74 CD ARG A 9 15341 13682 16218 -498 3751 1716 C ATOM 75 NE ARG A 9 -22.460 20.674 44.495 1.00118.23 N ANISOU 75 NE ARG A 9 15040 13835 16047 -479 4039 2033 N ATOM 76 CZ ARG A 9 -23.020 20.987 45.656 1.00133.69 C ANISOU 76 CZ ARG A 9 17032 16090 17674 -568 4343 2131 C ATOM 77 NH1 ARG A 9 -22.292 21.246 46.730 1.00133.93 N1+ ANISOU 77 NH1 ARG A 9 17328 16148 17410 -694 4390 2004 N1+ ATOM 78 NH2 ARG A 9 -24.347 21.052 45.738 1.00135.36 N ANISOU 78 NH2 ARG A 9 16970 16628 17831 -538 4611 2320 N ATOM 79 N CYS A 10 -19.577 21.554 39.142 1.00 79.62 N ANISOU 79 N CYS A 10 11952 8319 9982 -295 4774 -768 N ATOM 80 CA CYS A 10 -19.781 22.257 37.879 1.00 77.94 C ANISOU 80 CA CYS A 10 11601 7979 10032 -155 4629 -814 C ATOM 81 C CYS A 10 -20.849 21.564 37.043 1.00 86.58 C ANISOU 81 C CYS A 10 12433 9057 11407 -92 4651 -770 C ATOM 82 O CYS A 10 -21.247 20.430 37.314 1.00102.06 O ANISOU 82 O CYS A 10 14324 11088 13367 -175 4731 -675 O ATOM 83 CB CYS A 10 -18.469 22.358 37.094 1.00 76.92 C ANISOU 83 CB CYS A 10 11562 7820 9846 -165 4345 -706 C ATOM 84 SG CYS A 10 -18.077 20.892 36.110 1.00 79.14 S ANISOU 84 SG CYS A 10 11729 8151 10189 -185 4153 -499 S ATOM 85 N LYS A 11 -21.289 22.262 35.997 1.00 70.12 N ANISOU 85 N LYS A 11 10205 6869 9568 49 4558 -832 N ATOM 86 CA LYS A 11 -22.306 21.746 35.090 1.00 78.86 C ANISOU 86 CA LYS A 11 11052 7954 10959 127 4546 -810 C ATOM 87 C LYS A 11 -21.705 20.767 34.087 1.00 80.29 C ANISOU 87 C LYS A 11 11188 8146 11173 107 4310 -647 C ATOM 88 O LYS A 11 -20.562 20.917 33.646 1.00 88.58 O ANISOU 88 O LYS A 11 12358 9196 12104 103 4115 -576 O ATOM 89 CB LYS A 11 -22.986 22.890 34.333 1.00 76.91 C ANISOU 89 CB LYS A 11 10675 7594 10953 299 4514 -934 C ATOM 90 CG LYS A 11 -23.915 23.746 35.176 1.00 78.32 C ANISOU 90 CG LYS A 11 10824 7755 11178 367 4757 -1127 C ATOM 91 CD LYS A 11 -24.267 25.041 34.456 1.00 96.74 C ANISOU 91 CD LYS A 11 13098 9940 13719 545 4668 -1244 C ATOM 92 CE LYS A 11 -25.689 25.484 34.764 1.00 94.31 C ANISOU 92 CE LYS A 11 12598 9624 13610 672 4882 -1421 C ATOM 93 NZ LYS A 11 -26.545 25.515 33.545 1.00 89.69 N1+ ANISOU 93 NZ LYS A 11 11755 8976 13347 812 4772 -1408 N1+ ATOM 94 N ALA A 12 -22.498 19.763 33.720 1.00 73.68 N ANISOU 94 N ALA A 12 10166 7324 10504 98 4328 -598 N ATOM 95 CA ALA A 12 -22.090 18.784 32.722 1.00 76.09 C ANISOU 95 CA ALA A 12 10408 7631 10872 104 4102 -479 C ATOM 96 C ALA A 12 -23.328 18.231 32.032 1.00 77.78 C ANISOU 96 C ALA A 12 10359 7815 11379 156 4109 -498 C ATOM 97 O ALA A 12 -24.355 18.009 32.675 1.00 66.47 O ANISOU 97 O ALA A 12 8815 6397 10042 105 4318 -538 O ATOM 98 CB ALA A 12 -21.278 17.646 33.348 1.00 71.84 C ANISOU 98 CB ALA A 12 10018 7149 10128 -36 4069 -350 C ATOM 99 N ALA A 13 -23.223 18.006 30.725 1.00 62.58 N ANISOU 99 N ALA A 13 8325 5863 9588 256 3880 -471 N ATOM 100 CA ALA A 13 -24.322 17.446 29.941 1.00 77.35 C ANISOU 100 CA ALA A 13 9944 7705 11740 310 3837 -494 C ATOM 101 C ALA A 13 -24.274 15.928 30.068 1.00 78.65 C ANISOU 101 C ALA A 13 10099 7874 11911 192 3784 -398 C ATOM 102 O ALA A 13 -23.522 15.257 29.357 1.00 75.74 O ANISOU 102 O ALA A 13 9775 7507 11498 218 3559 -338 O ATOM 103 CB ALA A 13 -24.230 17.896 28.487 1.00 74.93 C ANISOU 103 CB ALA A 13 9538 7379 11553 474 3604 -514 C ATOM 104 N VAL A 14 -25.080 15.381 30.975 1.00 68.34 N ANISOU 104 N VAL A 14 8731 6571 10661 64 3989 -382 N ATOM 105 CA VAL A 14 -25.066 13.954 31.271 1.00 70.82 C ANISOU 105 CA VAL A 14 9057 6864 10985 -79 3953 -268 C ATOM 106 C VAL A 14 -26.048 13.241 30.352 1.00 68.62 C ANISOU 106 C VAL A 14 8528 6527 11019 -53 3842 -288 C ATOM 107 O VAL A 14 -27.180 13.704 30.150 1.00 81.24 O ANISOU 107 O VAL A 14 9909 8129 12829 -6 3947 -372 O ATOM 108 CB VAL A 14 -25.409 13.698 32.749 1.00 76.28 C ANISOU 108 CB VAL A 14 9818 7604 11563 -257 4230 -209 C ATOM 109 CG1 VAL A 14 -25.659 12.215 32.999 1.00 72.65 C ANISOU 109 CG1 VAL A 14 9328 7096 11179 -420 4198 -73 C ATOM 110 CG2 VAL A 14 -24.299 14.217 33.649 1.00 75.25 C ANISOU 110 CG2 VAL A 14 9961 7532 11097 -293 4293 -184 C ATOM 111 N ALA A 15 -25.604 12.123 29.778 1.00 69.00 N ANISOU 111 N ALA A 15 8600 6516 11101 -71 3614 -223 N ATOM 112 CA ALA A 15 -26.477 11.194 29.070 1.00 72.94 C ANISOU 112 CA ALA A 15 8889 6938 11885 -88 3491 -232 C ATOM 113 C ALA A 15 -26.895 10.107 30.052 1.00 73.34 C ANISOU 113 C ALA A 15 8950 6940 11978 -312 3614 -111 C ATOM 114 O ALA A 15 -26.064 9.302 30.486 1.00 91.99 O ANISOU 114 O ALA A 15 11503 9259 14191 -399 3536 -1 O ATOM 115 CB ALA A 15 -25.770 10.593 27.859 1.00 65.01 C ANISOU 115 CB ALA A 15 7911 5893 10898 32 3157 -252 C ATOM 116 N TRP A 16 -28.176 10.085 30.411 1.00 74.06 N ANISOU 116 N TRP A 16 8827 7041 12271 -407 3804 -118 N ATOM 117 CA TRP A 16 -28.666 9.101 31.367 1.00 77.65 C ANISOU 117 CA TRP A 16 9267 7465 12770 -644 3945 23 C ATOM 118 C TRP A 16 -29.121 7.813 30.693 1.00 85.40 C ANISOU 118 C TRP A 16 10120 8303 14024 -722 3724 68 C ATOM 119 O TRP A 16 -28.923 6.725 31.244 1.00 87.82 O ANISOU 119 O TRP A 16 10529 8522 14318 -898 3692 217 O ATOM 120 CB TRP A 16 -29.814 9.691 32.191 1.00 75.47 C ANISOU 120 CB TRP A 16 8813 7302 12559 -727 4286 3 C ATOM 121 CG TRP A 16 -29.364 10.648 33.254 1.00 85.61 C ANISOU 121 CG TRP A 16 10271 8714 13544 -719 4535 -10 C ATOM 122 CD1 TRP A 16 -29.397 12.010 33.196 1.00 86.03 C ANISOU 122 CD1 TRP A 16 10311 8844 13530 -552 4639 -161 C ATOM 123 CD2 TRP A 16 -28.814 10.314 34.534 1.00 82.15 C ANISOU 123 CD2 TRP A 16 10053 8330 12831 -884 4693 126 C ATOM 124 CE2 TRP A 16 -28.537 11.525 35.199 1.00 81.38 C ANISOU 124 CE2 TRP A 16 10064 8353 12502 -804 4890 31 C ATOM 125 CE3 TRP A 16 -28.529 9.108 35.183 1.00 77.26 C ANISOU 125 CE3 TRP A 16 9556 7661 12140 -1090 4674 324 C ATOM 126 NE1 TRP A 16 -28.902 12.546 34.361 1.00 84.07 N ANISOU 126 NE1 TRP A 16 10263 8693 12988 -602 4850 -146 N ATOM 127 CZ2 TRP A 16 -27.989 11.566 36.479 1.00 76.80 C ANISOU 127 CZ2 TRP A 16 9707 7866 11607 -920 5070 113 C ATOM 128 CZ3 TRP A 16 -27.984 9.151 36.455 1.00 80.19 C ANISOU 128 CZ3 TRP A 16 10148 8126 12196 -1206 4855 429 C ATOM 129 CH2 TRP A 16 -27.721 10.372 37.089 1.00 77.76 C ANISOU 129 CH2 TRP A 16 9940 7959 11646 -1120 5052 317 C ATOM 130 N GLU A 17 -29.730 7.912 29.513 1.00 85.43 N ANISOU 130 N GLU A 17 9909 8273 14277 -595 3558 -57 N ATOM 131 CA GLU A 17 -30.237 6.747 28.806 1.00 86.36 C ANISOU 131 CA GLU A 17 9889 8250 14676 -659 3329 -48 C ATOM 132 C GLU A 17 -29.876 6.853 27.332 1.00 76.78 C ANISOU 132 C GLU A 17 8642 7003 13526 -429 3009 -196 C ATOM 133 O GLU A 17 -29.689 7.950 26.798 1.00 87.69 O ANISOU 133 O GLU A 17 10007 8487 14824 -237 3011 -302 O ATOM 134 CB GLU A 17 -31.756 6.606 28.976 1.00 85.75 C ANISOU 134 CB GLU A 17 9497 8185 14900 -796 3485 -43 C ATOM 135 CG GLU A 17 -32.189 6.338 30.410 1.00108.01 C ANISOU 135 CG GLU A 17 12322 11057 17661 -1049 3801 122 C ATOM 136 CD GLU A 17 -33.692 6.392 30.589 1.00132.13 C ANISOU 136 CD GLU A 17 15032 14180 20991 -1165 3995 116 C ATOM 137 OE1 GLU A 17 -34.148 6.504 31.746 1.00139.88 O ANISOU 137 OE1 GLU A 17 15975 15278 21895 -1331 4316 219 O ATOM 138 OE2 GLU A 17 -34.416 6.324 29.574 1.00136.22 O1- ANISOU 138 OE2 GLU A 17 15308 14654 21796 -1089 3828 4 O1- ATOM 139 N ALA A 18 -29.779 5.695 26.682 1.00 86.32 N ANISOU 139 N ALA A 18 9848 8067 14882 -449 2728 -199 N ATOM 140 CA ALA A 18 -29.395 5.651 25.279 1.00 86.27 C ANISOU 140 CA ALA A 18 9821 8046 14912 -229 2410 -346 C ATOM 141 C ALA A 18 -30.431 6.352 24.408 1.00 77.78 C ANISOU 141 C ALA A 18 8466 7039 14048 -113 2391 -479 C ATOM 142 O ALA A 18 -31.637 6.268 24.655 1.00 83.09 O ANISOU 142 O ALA A 18 8908 7696 14968 -237 2513 -471 O ATOM 143 CB ALA A 18 -29.224 4.201 24.828 1.00 73.18 C ANISOU 143 CB ALA A 18 8202 6204 13399 -280 2115 -345 C ATOM 144 N GLY A 19 -29.947 7.063 23.391 1.00 79.41 N ANISOU 144 N GLY A 19 8689 7336 14149 124 2237 -593 N ATOM 145 CA GLY A 19 -30.808 7.693 22.408 1.00 95.55 C ANISOU 145 CA GLY A 19 10491 9442 16373 266 2158 -717 C ATOM 146 C GLY A 19 -31.722 8.779 22.940 1.00 92.33 C ANISOU 146 C GLY A 19 9917 9119 16047 249 2442 -716 C ATOM 147 O GLY A 19 -32.548 9.318 22.197 1.00 92.61 O ANISOU 147 O GLY A 19 9730 9198 16260 363 2386 -812 O ATOM 148 N LYS A 20 -31.584 9.118 24.219 1.00 88.82 N ANISOU 148 N LYS A 20 9577 8702 15467 121 2739 -618 N ATOM 149 CA LYS A 20 -32.434 10.131 24.819 1.00 88.20 C ANISOU 149 CA LYS A 20 9349 8710 15453 117 3024 -637 C ATOM 150 C LYS A 20 -31.659 11.432 25.010 1.00 92.85 C ANISOU 150 C LYS A 20 10114 9385 15780 262 3130 -656 C ATOM 151 O LYS A 20 -30.430 11.414 25.127 1.00 89.41 O ANISOU 151 O LYS A 20 9939 8951 15081 281 3067 -605 O ATOM 152 CB LYS A 20 -32.986 9.650 26.166 1.00 93.37 C ANISOU 152 CB LYS A 20 9966 9361 16148 -130 3309 -529 C ATOM 153 CG LYS A 20 -34.045 8.560 26.043 1.00104.63 C ANISOU 153 CG LYS A 20 11150 10710 17895 -299 3250 -502 C ATOM 154 CD LYS A 20 -35.011 8.843 24.900 1.00109.46 C ANISOU 154 CD LYS A 20 11464 11335 18791 -161 3090 -640 C ATOM 155 CE LYS A 20 -35.790 7.596 24.510 1.00 97.71 C ANISOU 155 CE LYS A 20 9777 9735 17613 -316 2916 -627 C ATOM 156 NZ LYS A 20 -36.302 7.670 23.113 1.00 97.60 N1+ ANISOU 156 NZ LYS A 20 9564 9711 17811 -146 2628 -776 N1+ ATOM 157 N PRO A 21 -32.347 12.577 25.036 1.00 76.13 N ANISOU 157 N PRO A 21 7855 7331 13738 366 3277 -730 N ATOM 158 CA PRO A 21 -31.640 13.862 25.105 1.00 98.85 C ANISOU 158 CA PRO A 21 10900 10258 16402 510 3337 -756 C ATOM 159 C PRO A 21 -30.756 13.972 26.339 1.00 91.93 C ANISOU 159 C PRO A 21 10289 9400 15241 393 3534 -677 C ATOM 160 O PRO A 21 -31.022 13.369 27.381 1.00 79.78 O ANISOU 160 O PRO A 21 8760 7866 13688 210 3726 -612 O ATOM 161 CB PRO A 21 -32.775 14.892 25.148 1.00 77.83 C ANISOU 161 CB PRO A 21 8010 7632 13929 611 3492 -853 C ATOM 162 CG PRO A 21 -33.942 14.202 24.542 1.00 87.00 C ANISOU 162 CG PRO A 21 8864 8780 15410 590 3396 -894 C ATOM 163 CD PRO A 21 -33.804 12.755 24.903 1.00 82.61 C ANISOU 163 CD PRO A 21 8346 8175 14868 374 3362 -803 C ATOM 164 N LEU A 22 -29.687 14.754 26.203 1.00 74.14 N ANISOU 164 N LEU A 22 8250 7166 12754 494 3476 -672 N ATOM 165 CA LEU A 22 -28.823 15.042 27.334 1.00 76.25 C ANISOU 165 CA LEU A 22 8769 7459 12744 404 3646 -616 C ATOM 166 C LEU A 22 -29.552 15.925 28.341 1.00 79.48 C ANISOU 166 C LEU A 22 9123 7903 13170 387 3952 -680 C ATOM 167 O LEU A 22 -30.498 16.645 28.009 1.00 88.16 O ANISOU 167 O LEU A 22 10023 9006 14469 503 4004 -779 O ATOM 168 CB LEU A 22 -27.539 15.738 26.877 1.00 77.56 C ANISOU 168 CB LEU A 22 9149 7640 12680 512 3496 -599 C ATOM 169 CG LEU A 22 -26.677 15.064 25.809 1.00 77.07 C ANISOU 169 CG LEU A 22 9145 7584 12553 571 3196 -555 C ATOM 170 CD1 LEU A 22 -25.330 15.762 25.699 1.00 61.60 C ANISOU 170 CD1 LEU A 22 7407 5674 10324 629 3119 -514 C ATOM 171 CD2 LEU A 22 -26.494 13.589 26.107 1.00 67.66 C ANISOU 171 CD2 LEU A 22 7991 6357 11359 434 3141 -489 C ATOM 172 N VAL A 23 -29.099 15.866 29.590 1.00 78.56 N ANISOU 172 N VAL A 23 9189 7825 12837 254 4152 -630 N ATOM 173 CA VAL A 23 -29.661 16.687 30.655 1.00 85.03 C ANISOU 173 CA VAL A 23 9990 8701 13615 243 4453 -707 C ATOM 174 C VAL A 23 -28.517 17.415 31.346 1.00 88.65 C ANISOU 174 C VAL A 23 10748 9173 13762 243 4502 -706 C ATOM 175 O VAL A 23 -27.506 16.798 31.698 1.00 85.84 O ANISOU 175 O VAL A 23 10601 8824 13189 134 4437 -598 O ATOM 176 CB VAL A 23 -30.473 15.847 31.661 1.00 87.40 C ANISOU 176 CB VAL A 23 10179 9070 13960 54 4695 -652 C ATOM 177 CG1 VAL A 23 -30.547 16.542 33.009 1.00 87.70 C ANISOU 177 CG1 VAL A 23 10315 9204 13802 13 5007 -705 C ATOM 178 CG2 VAL A 23 -31.870 15.585 31.118 1.00 85.29 C ANISOU 178 CG2 VAL A 23 9560 8809 14038 78 4714 -703 C ATOM 179 N ILE A 24 -28.665 18.727 31.512 1.00 83.27 N ANISOU 179 N ILE A 24 10085 8483 13069 370 4595 -831 N ATOM 180 CA ILE A 24 -27.647 19.530 32.182 1.00 87.13 C ANISOU 180 CA ILE A 24 10850 8970 13285 369 4634 -852 C ATOM 181 C ILE A 24 -27.725 19.240 33.677 1.00 80.60 C ANISOU 181 C ILE A 24 10122 8240 12263 217 4910 -847 C ATOM 182 O ILE A 24 -28.657 19.676 34.357 1.00 79.71 O ANISOU 182 O ILE A 24 9893 8185 12208 239 5157 -958 O ATOM 183 CB ILE A 24 -27.825 21.025 31.895 1.00 90.32 C ANISOU 183 CB ILE A 24 11249 9305 13763 551 4629 -993 C ATOM 184 CG1 ILE A 24 -28.055 21.253 30.400 1.00 99.05 C ANISOU 184 CG1 ILE A 24 12201 10336 15097 702 4381 -985 C ATOM 185 CG2 ILE A 24 -26.616 21.807 32.386 1.00 78.74 C ANISOU 185 CG2 ILE A 24 10078 7808 12030 536 4597 -1000 C ATOM 186 CD1 ILE A 24 -26.821 21.032 29.552 1.00 83.77 C ANISOU 186 CD1 ILE A 24 10416 8380 13032 696 4106 -864 C ATOM 187 N GLU A 25 -26.750 18.499 34.188 1.00 87.96 N ANISOU 187 N GLU A 25 11262 9203 12956 71 4869 -719 N ATOM 188 CA GLU A 25 -26.694 18.118 35.586 1.00 85.65 C ANISOU 188 CA GLU A 25 11091 9012 12439 -88 5101 -679 C ATOM 189 C GLU A 25 -25.538 18.823 36.280 1.00 88.92 C ANISOU 189 C GLU A 25 11802 9440 12542 -98 5097 -707 C ATOM 190 O GLU A 25 -24.651 19.406 35.649 1.00 88.39 O ANISOU 190 O GLU A 25 11851 9300 12432 -17 4891 -719 O ATOM 191 CB GLU A 25 -26.555 16.600 35.726 1.00 89.48 C ANISOU 191 CB GLU A 25 11581 9516 12901 -264 5051 -491 C ATOM 192 CG GLU A 25 -27.810 15.827 35.370 1.00 85.37 C ANISOU 192 CG GLU A 25 10769 8995 12671 -309 5108 -459 C ATOM 193 CD GLU A 25 -28.851 15.876 36.471 1.00 99.50 C ANISOU 193 CD GLU A 25 12439 10916 14452 -400 5451 -490 C ATOM 194 OE1 GLU A 25 -28.463 15.875 37.659 1.00112.76 O ANISOU 194 OE1 GLU A 25 14300 12692 15849 -509 5626 -451 O ATOM 195 OE2 GLU A 25 -30.057 15.920 36.152 1.00113.56 O1- ANISOU 195 OE2 GLU A 25 13932 12718 16498 -360 5547 -554 O1- ATOM 196 N GLU A 26 -25.564 18.747 37.603 1.00 90.65 N ANISOU 196 N GLU A 26 12137 9770 12538 -211 5327 -711 N ATOM 197 CA GLU A 26 -24.593 19.406 38.467 1.00 80.21 C ANISOU 197 CA GLU A 26 11092 8481 10903 -236 5355 -758 C ATOM 198 C GLU A 26 -23.712 18.312 39.063 1.00 89.42 C ANISOU 198 C GLU A 26 12442 9708 11826 -414 5301 -568 C ATOM 199 O GLU A 26 -24.123 17.613 39.994 1.00 92.63 O ANISOU 199 O GLU A 26 12852 10222 12122 -550 5493 -489 O ATOM 200 CB GLU A 26 -25.323 20.213 39.533 1.00 93.84 C ANISOU 200 CB GLU A 26 12813 10302 12541 -205 5655 -933 C ATOM 201 CG GLU A 26 -24.631 21.484 39.954 1.00105.94 C ANISOU 201 CG GLU A 26 14559 11796 13896 -124 5637 -1095 C ATOM 202 CD GLU A 26 -23.633 21.269 41.062 1.00117.10 C ANISOU 202 CD GLU A 26 16255 13304 14935 -264 5666 -1038 C ATOM 203 OE1 GLU A 26 -23.475 20.118 41.523 1.00119.42 O ANISOU 203 OE1 GLU A 26 16583 13694 15098 -421 5703 -860 O ATOM 204 OE2 GLU A 26 -23.035 22.273 41.495 1.00116.64 O1- ANISOU 204 OE2 GLU A 26 16383 13217 14717 -218 5644 -1176 O1- ATOM 205 N VAL A 27 -22.507 18.160 38.523 1.00 92.97 N ANISOU 205 N VAL A 27 13036 10096 12193 -411 5038 -484 N ATOM 206 CA VAL A 27 -21.656 17.022 38.827 1.00 86.36 C ANISOU 206 CA VAL A 27 12341 9289 11184 -544 4926 -296 C ATOM 207 C VAL A 27 -20.407 17.490 39.572 1.00 87.35 C ANISOU 207 C VAL A 27 12743 9463 10981 -587 4874 -299 C ATOM 208 O VAL A 27 -20.084 18.681 39.626 1.00 85.36 O ANISOU 208 O VAL A 27 12572 9195 10667 -511 4870 -440 O ATOM 209 CB VAL A 27 -21.274 16.237 37.556 1.00 75.24 C ANISOU 209 CB VAL A 27 10846 7790 9953 -500 4646 -192 C ATOM 210 CG1 VAL A 27 -22.487 16.054 36.657 1.00 79.42 C ANISOU 210 CG1 VAL A 27 11095 8259 10823 -427 4661 -234 C ATOM 211 CG2 VAL A 27 -20.151 16.943 36.809 1.00 69.07 C ANISOU 211 CG2 VAL A 27 10161 6972 9110 -397 4415 -226 C ATOM 212 N GLU A 28 -19.704 16.522 40.156 1.00 84.00 N ANISOU 212 N GLU A 28 12467 9091 10359 -714 4817 -137 N ATOM 213 CA GLU A 28 -18.444 16.737 40.851 1.00 85.61 C ANISOU 213 CA GLU A 28 12925 9353 10248 -768 4732 -108 C ATOM 214 C GLU A 28 -17.302 16.172 40.017 1.00 78.63 C ANISOU 214 C GLU A 28 12084 8421 9371 -741 4425 8 C ATOM 215 O GLU A 28 -17.426 15.097 39.423 1.00 82.75 O ANISOU 215 O GLU A 28 12510 8894 10038 -745 4314 127 O ATOM 216 CB GLU A 28 -18.457 16.076 42.233 1.00 74.33 C ANISOU 216 CB GLU A 28 11644 8042 8556 -926 4896 -4 C ATOM 217 CG GLU A 28 -18.963 16.970 43.355 1.00 88.61 C ANISOU 217 CG GLU A 28 13525 9960 10182 -946 5168 -155 C ATOM 218 CD GLU A 28 -19.667 16.190 44.449 1.00101.86 C ANISOU 218 CD GLU A 28 15213 11769 11720 -1090 5412 -47 C ATOM 219 OE1 GLU A 28 -18.986 15.445 45.186 1.00109.02 O ANISOU 219 OE1 GLU A 28 16298 12743 12380 -1214 5365 118 O ATOM 220 OE2 GLU A 28 -20.903 16.319 44.572 1.00118.45 O1- ANISOU 220 OE2 GLU A 28 17134 13914 13957 -1080 5649 -116 O1- ATOM 221 N VAL A 29 -16.190 16.900 39.986 1.00 78.19 N ANISOU 221 N VAL A 29 12166 8385 9159 -713 4285 -34 N ATOM 222 CA VAL A 29 -15.015 16.557 39.196 1.00 79.80 C ANISOU 222 CA VAL A 29 12395 8581 9345 -672 4004 54 C ATOM 223 C VAL A 29 -13.833 16.467 40.147 1.00 77.64 C ANISOU 223 C VAL A 29 12350 8398 8750 -765 3935 118 C ATOM 224 O VAL A 29 -13.459 17.466 40.778 1.00 69.11 O ANISOU 224 O VAL A 29 11399 7357 7502 -793 3986 19 O ATOM 225 CB VAL A 29 -14.752 17.591 38.089 1.00 69.40 C ANISOU 225 CB VAL A 29 10989 7216 8165 -552 3876 -41 C ATOM 226 CG1 VAL A 29 -13.512 17.218 37.293 1.00 77.06 C ANISOU 226 CG1 VAL A 29 11967 8223 9089 -512 3604 55 C ATOM 227 CG2 VAL A 29 -15.964 17.714 37.178 1.00 63.78 C ANISOU 227 CG2 VAL A 29 10052 6419 7763 -453 3937 -106 C ATOM 228 N ALA A 30 -13.250 15.276 40.249 1.00 76.75 N ANISOU 228 N ALA A 30 12291 8310 8561 -806 3805 277 N ATOM 229 CA ALA A 30 -12.147 15.042 41.161 1.00 75.29 C ANISOU 229 CA ALA A 30 12314 8216 8077 -888 3721 358 C ATOM 230 C ALA A 30 -10.874 15.720 40.656 1.00 67.05 C ANISOU 230 C ALA A 30 11306 7218 6953 -836 3508 324 C ATOM 231 O ALA A 30 -10.759 16.047 39.472 1.00 68.54 O ANISOU 231 O ALA A 30 11350 7371 7321 -734 3392 286 O ATOM 232 CB ALA A 30 -11.914 13.541 41.328 1.00 74.10 C ANISOU 232 CB ALA A 30 12197 8055 7903 -928 3618 545 C ATOM 233 N PRO A 31 -9.912 15.960 41.543 1.00 65.96 N ANISOU 233 N PRO A 31 11351 7172 6538 -913 3454 341 N ATOM 234 CA PRO A 31 -8.608 16.474 41.107 1.00 67.68 C ANISOU 234 CA PRO A 31 11589 7452 6673 -886 3234 337 C ATOM 235 C PRO A 31 -7.863 15.435 40.288 1.00 70.46 C ANISOU 235 C PRO A 31 11853 7833 7085 -807 3006 464 C ATOM 236 O PRO A 31 -8.130 14.230 40.406 1.00 80.63 O ANISOU 236 O PRO A 31 13141 9089 8407 -800 2992 571 O ATOM 237 CB PRO A 31 -7.883 16.773 42.430 1.00 74.66 C ANISOU 237 CB PRO A 31 12696 8434 7238 -1002 3239 333 C ATOM 238 CG PRO A 31 -8.609 15.978 43.462 1.00 71.39 C ANISOU 238 CG PRO A 31 12380 8028 6715 -1076 3411 400 C ATOM 239 CD PRO A 31 -10.031 15.934 43.010 1.00 65.81 C ANISOU 239 CD PRO A 31 11523 7222 6260 -1034 3606 349 C ATOM 240 N PRO A 32 -6.920 15.859 39.449 1.00 70.69 N ANISOU 240 N PRO A 32 11804 7924 7129 -746 2821 457 N ATOM 241 CA PRO A 32 -6.243 14.906 38.563 1.00 68.25 C ANISOU 241 CA PRO A 32 11385 7663 6882 -638 2611 549 C ATOM 242 C PRO A 32 -5.228 14.053 39.308 1.00 75.75 C ANISOU 242 C PRO A 32 12461 8700 7620 -668 2469 661 C ATOM 243 O PRO A 32 -4.572 14.500 40.252 1.00 80.19 O ANISOU 243 O PRO A 32 13172 9341 7957 -767 2460 665 O ATOM 244 CB PRO A 32 -5.560 15.810 37.532 1.00 68.12 C ANISOU 244 CB PRO A 32 11244 7723 6915 -581 2490 506 C ATOM 245 CG PRO A 32 -5.313 17.081 38.265 1.00 67.81 C ANISOU 245 CG PRO A 32 11325 7697 6743 -701 2560 435 C ATOM 246 CD PRO A 32 -6.455 17.242 39.236 1.00 73.13 C ANISOU 246 CD PRO A 32 12114 8263 7411 -772 2795 365 C ATOM 247 N GLN A 33 -5.106 12.806 38.863 1.00 76.91 N ANISOU 247 N GLN A 33 12549 8825 7847 -573 2341 745 N ATOM 248 CA GLN A 33 -4.173 11.854 39.447 1.00 78.53 C ANISOU 248 CA GLN A 33 12859 9090 7889 -567 2176 859 C ATOM 249 C GLN A 33 -2.835 11.942 38.710 1.00 83.23 C ANISOU 249 C GLN A 33 13350 9842 8431 -463 1946 860 C ATOM 250 O GLN A 33 -2.565 12.918 38.005 1.00 73.49 O ANISOU 250 O GLN A 33 12004 8687 7231 -447 1939 787 O ATOM 251 CB GLN A 33 -4.772 10.445 39.407 1.00 84.48 C ANISOU 251 CB GLN A 33 13615 9710 8774 -518 2148 948 C ATOM 252 CG GLN A 33 -5.946 10.232 40.348 1.00 87.50 C ANISOU 252 CG GLN A 33 14110 9976 9161 -654 2371 992 C ATOM 253 CD GLN A 33 -5.578 10.457 41.802 1.00 86.78 C ANISOU 253 CD GLN A 33 14235 9960 8776 -797 2439 1055 C ATOM 254 NE2 GLN A 33 -6.527 10.965 42.580 1.00 86.56 N ANISOU 254 NE2 GLN A 33 14282 9910 8698 -921 2690 1023 N ATOM 255 OE1 GLN A 33 -4.457 10.172 42.223 1.00 95.79 O ANISOU 255 OE1 GLN A 33 15470 11194 9731 -789 2264 1126 O ATOM 256 N LYS A 34 -1.988 10.924 38.863 1.00 89.24 N ANISOU 256 N LYS A 34 14141 10654 9111 -390 1754 949 N ATOM 257 CA LYS A 34 -0.693 10.914 38.195 1.00 74.63 C ANISOU 257 CA LYS A 34 12170 8982 7203 -276 1537 948 C ATOM 258 C LYS A 34 -0.868 10.981 36.683 1.00 77.61 C ANISOU 258 C LYS A 34 12321 9389 7778 -127 1498 874 C ATOM 259 O LYS A 34 -1.657 10.229 36.102 1.00 74.47 O ANISOU 259 O LYS A 34 11865 8863 7568 -32 1507 855 O ATOM 260 CB LYS A 34 0.092 9.658 38.580 1.00 86.34 C ANISOU 260 CB LYS A 34 13716 10489 8603 -188 1335 1046 C ATOM 261 CG LYS A 34 1.566 9.907 38.880 1.00 96.39 C ANISOU 261 CG LYS A 34 14981 11975 9665 -180 1159 1077 C ATOM 262 CD LYS A 34 2.411 8.665 38.619 1.00 94.29 C ANISOU 262 CD LYS A 34 14666 11759 9401 5 913 1132 C ATOM 263 CE LYS A 34 3.882 8.919 38.923 1.00 91.34 C ANISOU 263 CE LYS A 34 14259 11622 8824 17 736 1161 C ATOM 264 NZ LYS A 34 4.792 7.979 38.211 1.00 99.58 N1+ ANISOU 264 NZ LYS A 34 15153 12777 9906 251 499 1161 N1+ ATOM 265 N HIS A 35 -0.138 11.904 36.054 1.00 72.89 N ANISOU 265 N HIS A 35 11597 8965 7133 -118 1449 837 N ATOM 266 CA HIS A 35 -0.098 12.119 34.610 1.00 67.63 C ANISOU 266 CA HIS A 35 10710 8391 6597 15 1400 783 C ATOM 267 C HIS A 35 -1.420 12.616 34.039 1.00 69.89 C ANISOU 267 C HIS A 35 10948 8528 7079 0 1569 717 C ATOM 268 O HIS A 35 -1.619 12.552 32.819 1.00 73.70 O ANISOU 268 O HIS A 35 11260 9054 7689 130 1528 674 O ATOM 269 CB HIS A 35 0.336 10.855 33.860 1.00 64.93 C ANISOU 269 CB HIS A 35 10255 8107 6311 232 1216 780 C ATOM 270 CG HIS A 35 1.714 10.388 34.212 1.00 83.83 C ANISOU 270 CG HIS A 35 12646 10676 8529 290 1026 833 C ATOM 271 CD2 HIS A 35 2.395 9.272 33.858 1.00 89.25 C ANISOU 271 CD2 HIS A 35 13262 11435 9212 484 832 832 C ATOM 272 ND1 HIS A 35 2.553 11.101 35.041 1.00 95.38 N ANISOU 272 ND1 HIS A 35 14181 12261 9799 148 1012 884 N ATOM 273 CE1 HIS A 35 3.693 10.449 35.177 1.00 88.55 C ANISOU 273 CE1 HIS A 35 13278 11549 8818 249 819 923 C ATOM 274 NE2 HIS A 35 3.623 9.336 34.470 1.00 96.14 N ANISOU 274 NE2 HIS A 35 14153 12482 9892 461 709 890 N ATOM 275 N GLU A 36 -2.326 13.114 34.875 1.00 67.18 N ANISOU 275 N GLU A 36 10742 8027 6755 -143 1755 701 N ATOM 276 CA GLU A 36 -3.592 13.676 34.431 1.00 81.83 C ANISOU 276 CA GLU A 36 12547 9747 8797 -158 1920 632 C ATOM 277 C GLU A 36 -3.588 15.188 34.619 1.00 76.26 C ANISOU 277 C GLU A 36 11870 9057 8048 -281 2022 594 C ATOM 278 O GLU A 36 -2.832 15.735 35.428 1.00 63.53 O ANISOU 278 O GLU A 36 10369 7512 6257 -395 2003 613 O ATOM 279 CB GLU A 36 -4.769 13.060 35.199 1.00 70.14 C ANISOU 279 CB GLU A 36 11177 8072 7400 -214 2070 632 C ATOM 280 CG GLU A 36 -4.946 11.565 34.988 1.00 68.32 C ANISOU 280 CG GLU A 36 10927 7770 7262 -110 1966 675 C ATOM 281 CD GLU A 36 -6.028 10.971 35.871 1.00 78.69 C ANISOU 281 CD GLU A 36 12355 8905 8640 -208 2115 712 C ATOM 282 OE1 GLU A 36 -6.569 11.701 36.730 1.00 73.04 O ANISOU 282 OE1 GLU A 36 11737 8153 7860 -346 2308 698 O ATOM 283 OE2 GLU A 36 -6.339 9.774 35.705 1.00 80.62 O1- ANISOU 283 OE2 GLU A 36 12587 9046 9000 -147 2037 753 O1- ATOM 284 N VAL A 37 -4.438 15.867 33.847 1.00 67.20 N ANISOU 284 N VAL A 37 10622 7835 7074 -252 2111 536 N ATOM 285 CA VAL A 37 -4.644 17.304 33.981 1.00 74.35 C ANISOU 285 CA VAL A 37 11562 8698 7990 -354 2208 489 C ATOM 286 C VAL A 37 -6.141 17.585 33.949 1.00 67.14 C ANISOU 286 C VAL A 37 10640 7600 7270 -344 2392 408 C ATOM 287 O VAL A 37 -6.915 16.885 33.287 1.00 64.41 O ANISOU 287 O VAL A 37 10185 7200 7089 -240 2404 397 O ATOM 288 CB VAL A 37 -3.911 18.123 32.884 1.00 72.48 C ANISOU 288 CB VAL A 37 11181 8593 7764 -327 2089 523 C ATOM 289 CG1 VAL A 37 -2.495 17.606 32.663 1.00 70.85 C ANISOU 289 CG1 VAL A 37 10914 8609 7395 -294 1902 604 C ATOM 290 CG2 VAL A 37 -4.693 18.120 31.576 1.00 73.34 C ANISOU 290 CG2 VAL A 37 11118 8673 8075 -196 2095 504 C ATOM 291 N ARG A 38 -6.551 18.613 34.686 1.00 75.65 N ANISOU 291 N ARG A 38 11828 8584 8331 -449 2527 340 N ATOM 292 CA ARG A 38 -7.930 19.081 34.675 1.00 62.51 C ANISOU 292 CA ARG A 38 10141 6761 6850 -432 2706 247 C ATOM 293 C ARG A 38 -8.031 20.310 33.781 1.00 66.63 C ANISOU 293 C ARG A 38 10573 7245 7498 -403 2675 216 C ATOM 294 O ARG A 38 -7.238 21.248 33.913 1.00 62.31 O ANISOU 294 O ARG A 38 10089 6728 6858 -484 2608 226 O ATOM 295 CB ARG A 38 -8.418 19.403 36.088 1.00 61.32 C ANISOU 295 CB ARG A 38 10167 6532 6599 -540 2888 170 C ATOM 296 CG ARG A 38 -9.933 19.491 36.204 1.00 65.66 C ANISOU 296 CG ARG A 38 10670 6949 7330 -505 3094 79 C ATOM 297 CD ARG A 38 -10.410 19.180 37.614 1.00 62.04 C ANISOU 297 CD ARG A 38 10360 6476 6736 -596 3277 42 C ATOM 298 NE ARG A 38 -9.784 20.041 38.610 1.00 60.38 N ANISOU 298 NE ARG A 38 10335 6293 6312 -697 3298 -21 N ATOM 299 CZ ARG A 38 -9.959 19.922 39.919 1.00 76.38 C ANISOU 299 CZ ARG A 38 12522 8348 8153 -785 3437 -58 C ATOM 300 NH1 ARG A 38 -10.743 18.986 40.429 1.00 70.28 N1+ ANISOU 300 NH1 ARG A 38 11745 7581 7377 -800 3582 -17 N1+ ATOM 301 NH2 ARG A 38 -9.335 20.765 40.737 1.00 76.87 N ANISOU 301 NH2 ARG A 38 12751 8437 8020 -867 3426 -135 N ATOM 302 N ILE A 39 -9.004 20.295 32.876 1.00 65.92 N ANISOU 302 N ILE A 39 10338 7083 7626 -296 2712 189 N ATOM 303 CA ILE A 39 -9.175 21.322 31.859 1.00 67.39 C ANISOU 303 CA ILE A 39 10422 7233 7951 -246 2661 188 C ATOM 304 C ILE A 39 -10.538 21.971 32.043 1.00 73.55 C ANISOU 304 C ILE A 39 11195 7831 8920 -217 2828 73 C ATOM 305 O ILE A 39 -11.543 21.283 32.265 1.00 66.39 O ANISOU 305 O ILE A 39 10243 6867 8114 -171 2950 21 O ATOM 306 CB ILE A 39 -9.045 20.737 30.437 1.00 66.49 C ANISOU 306 CB ILE A 39 10117 7228 7917 -117 2520 262 C ATOM 307 CG1 ILE A 39 -7.759 19.919 30.303 1.00 61.62 C ANISOU 307 CG1 ILE A 39 9489 6808 7114 -115 2367 352 C ATOM 308 CG2 ILE A 39 -9.090 21.843 29.394 1.00 57.18 C ANISOU 308 CG2 ILE A 39 8844 6038 6844 -82 2453 295 C ATOM 309 CD1 ILE A 39 -7.665 19.142 29.006 1.00 51.70 C ANISOU 309 CD1 ILE A 39 8053 5676 5914 37 2238 391 C ATOM 310 N LYS A 40 -10.558 23.301 31.961 1.00 69.38 N ANISOU 310 N LYS A 40 10706 7209 8447 -244 2827 36 N ATOM 311 CA LYS A 40 -11.792 24.074 31.885 1.00 69.20 C ANISOU 311 CA LYS A 40 10648 7012 8633 -179 2947 -73 C ATOM 312 C LYS A 40 -12.170 24.201 30.414 1.00 68.69 C ANISOU 312 C LYS A 40 10397 6949 8755 -57 2842 -9 C ATOM 313 O LYS A 40 -11.496 24.901 29.651 1.00 69.59 O ANISOU 313 O LYS A 40 10487 7094 8861 -68 2697 83 O ATOM 314 CB LYS A 40 -11.610 25.446 32.530 1.00 84.11 C ANISOU 314 CB LYS A 40 12686 8773 10500 -256 2972 -154 C ATOM 315 CG LYS A 40 -12.805 26.384 32.393 1.00 68.25 C ANISOU 315 CG LYS A 40 10642 6570 8721 -165 3069 -276 C ATOM 316 CD LYS A 40 -12.484 27.757 32.975 1.00 85.71 C ANISOU 316 CD LYS A 40 13018 8634 10914 -236 3052 -361 C ATOM 317 CE LYS A 40 -13.564 28.784 32.655 1.00 66.09 C ANISOU 317 CE LYS A 40 10490 5940 8682 -121 3100 -472 C ATOM 318 NZ LYS A 40 -14.814 28.563 33.436 1.00 70.24 N1+ ANISOU 318 NZ LYS A 40 10998 6411 9279 -36 3331 -653 N1+ ATOM 319 N ILE A 41 -13.238 23.514 30.012 1.00 72.26 N ANISOU 319 N ILE A 41 10712 7377 9366 50 2907 -49 N ATOM 320 CA ILE A 41 -13.668 23.550 28.620 1.00 68.92 C ANISOU 320 CA ILE A 41 10110 6967 9109 176 2800 0 C ATOM 321 C ILE A 41 -14.301 24.901 28.320 1.00 72.32 C ANISOU 321 C ILE A 41 10529 7237 9712 222 2814 -44 C ATOM 322 O ILE A 41 -15.127 25.405 29.092 1.00 74.56 O ANISOU 322 O ILE A 41 10863 7373 10091 227 2967 -173 O ATOM 323 CB ILE A 41 -14.640 22.398 28.325 1.00 70.70 C ANISOU 323 CB ILE A 41 10193 7204 9465 267 2849 -41 C ATOM 324 CG1 ILE A 41 -13.964 21.054 28.600 1.00 58.91 C ANISOU 324 CG1 ILE A 41 8727 5839 7816 227 2805 9 C ATOM 325 CG2 ILE A 41 -15.127 22.461 26.885 1.00 66.01 C ANISOU 325 CG2 ILE A 41 9415 6630 9036 405 2726 -7 C ATOM 326 CD1 ILE A 41 -12.741 20.804 27.746 1.00 53.80 C ANISOU 326 CD1 ILE A 41 8049 5364 7027 251 2605 121 C ATOM 327 N LEU A 42 -13.904 25.501 27.201 1.00 63.66 N ANISOU 327 N LEU A 42 9366 6172 8649 260 2653 67 N ATOM 328 CA LEU A 42 -14.506 26.732 26.702 1.00 57.22 C ANISOU 328 CA LEU A 42 8527 5196 8020 321 2624 59 C ATOM 329 C LEU A 42 -15.416 26.507 25.507 1.00 61.57 C ANISOU 329 C LEU A 42 8881 5756 8755 478 2564 79 C ATOM 330 O LEU A 42 -16.480 27.124 25.424 1.00 65.28 O ANISOU 330 O LEU A 42 9301 6065 9435 569 2616 -2 O ATOM 331 CB LEU A 42 -13.417 27.742 26.321 1.00 66.42 C ANISOU 331 CB LEU A 42 9771 6368 9097 228 2474 196 C ATOM 332 CG LEU A 42 -12.607 28.372 27.454 1.00 65.56 C ANISOU 332 CG LEU A 42 9864 6190 8854 68 2503 162 C ATOM 333 CD1 LEU A 42 -11.876 29.612 26.959 1.00 63.72 C ANISOU 333 CD1 LEU A 42 9687 5891 8632 -17 2349 293 C ATOM 334 CD2 LEU A 42 -13.498 28.709 28.640 1.00 59.58 C ANISOU 334 CD2 LEU A 42 9213 5243 8184 82 2685 -43 C ATOM 335 N PHE A 43 -15.020 25.641 24.578 1.00 63.64 N ANISOU 335 N PHE A 43 9028 6211 8941 524 2446 175 N ATOM 336 CA PHE A 43 -15.827 25.320 23.411 1.00 63.68 C ANISOU 336 CA PHE A 43 8848 6253 9094 675 2367 186 C ATOM 337 C PHE A 43 -15.672 23.845 23.085 1.00 74.76 C ANISOU 337 C PHE A 43 10159 7831 10415 716 2328 178 C ATOM 338 O PHE A 43 -14.586 23.280 23.231 1.00 71.52 O ANISOU 338 O PHE A 43 9805 7570 9800 651 2280 236 O ATOM 339 CB PHE A 43 -15.428 26.162 22.190 1.00 63.38 C ANISOU 339 CB PHE A 43 8760 6271 9051 715 2192 342 C ATOM 340 CG PHE A 43 -15.464 27.641 22.434 1.00 77.41 C ANISOU 340 CG PHE A 43 10643 7852 10918 666 2191 374 C ATOM 341 CD1 PHE A 43 -14.348 28.306 22.913 1.00 75.51 C ANISOU 341 CD1 PHE A 43 10553 7606 10531 512 2161 457 C ATOM 342 CD2 PHE A 43 -16.617 28.366 22.189 1.00 76.69 C ANISOU 342 CD2 PHE A 43 10498 7569 11071 777 2204 316 C ATOM 343 CE1 PHE A 43 -14.381 29.668 23.141 1.00 65.62 C ANISOU 343 CE1 PHE A 43 9410 6141 9381 461 2138 479 C ATOM 344 CE2 PHE A 43 -16.655 29.727 22.414 1.00 80.10 C ANISOU 344 CE2 PHE A 43 11039 7790 11605 746 2183 335 C ATOM 345 CZ PHE A 43 -15.536 30.379 22.891 1.00 70.29 C ANISOU 345 CZ PHE A 43 9961 6524 10221 584 2146 415 C ATOM 346 N THR A 44 -16.766 23.228 22.646 1.00 70.76 N ANISOU 346 N THR A 44 9507 7297 10082 828 2337 98 N ATOM 347 CA THR A 44 -16.754 21.849 22.186 1.00 64.35 C ANISOU 347 CA THR A 44 8597 6617 9237 886 2266 76 C ATOM 348 C THR A 44 -17.686 21.728 20.989 1.00 75.45 C ANISOU 348 C THR A 44 9816 8036 10815 1038 2160 52 C ATOM 349 O THR A 44 -18.472 22.632 20.692 1.00 69.66 O ANISOU 349 O THR A 44 9028 7193 10247 1095 2170 45 O ATOM 350 CB THR A 44 -17.168 20.870 23.294 1.00 67.81 C ANISOU 350 CB THR A 44 9075 6983 9708 817 2411 -23 C ATOM 351 CG2 THR A 44 -18.582 21.167 23.769 1.00 66.44 C ANISOU 351 CG2 THR A 44 8834 6637 9773 835 2565 -131 C ATOM 352 OG1 THR A 44 -17.108 19.528 22.798 1.00 68.64 O ANISOU 352 OG1 THR A 44 9096 7187 9798 872 2310 -40 O ATOM 353 N SER A 45 -17.587 20.600 20.293 1.00 81.14 N ANISOU 353 N SER A 45 10442 8890 11499 1112 2043 33 N ATOM 354 CA SER A 45 -18.425 20.318 19.138 1.00 74.13 C ANISOU 354 CA SER A 45 9377 8037 10753 1259 1918 -7 C ATOM 355 C SER A 45 -18.990 18.909 19.271 1.00 66.96 C ANISOU 355 C SER A 45 8391 7106 9944 1279 1912 -124 C ATOM 356 O SER A 45 -18.785 18.226 20.278 1.00 73.47 O ANISOU 356 O SER A 45 9304 7875 10735 1176 2015 -156 O ATOM 357 CB SER A 45 -17.642 20.480 17.828 1.00 75.43 C ANISOU 357 CB SER A 45 9491 8422 10748 1353 1723 94 C ATOM 358 OG SER A 45 -18.506 20.400 16.707 1.00 81.55 O ANISOU 358 OG SER A 45 10103 9230 11651 1498 1597 59 O ATOM 359 N LEU A 46 -19.710 18.473 18.242 1.00 72.25 N ANISOU 359 N LEU A 46 10169 5586 11697 1140 1667 -2251 N ATOM 360 CA LEU A 46 -20.317 17.151 18.212 1.00 75.74 C ANISOU 360 CA LEU A 46 10478 6368 11934 1112 1533 -2046 C ATOM 361 C LEU A 46 -19.833 16.395 16.983 1.00 89.46 C ANISOU 361 C LEU A 46 12598 7992 13401 1033 1293 -1653 C ATOM 362 O LEU A 46 -19.689 16.974 15.901 1.00 90.98 O ANISOU 362 O LEU A 46 13067 7816 13685 1120 1104 -1455 O ATOM 363 CB LEU A 46 -21.846 17.247 18.214 1.00 83.67 C ANISOU 363 CB LEU A 46 11144 7354 13294 1322 1372 -2066 C ATOM 364 CG LEU A 46 -22.609 15.924 18.145 1.00 84.56 C ANISOU 364 CG LEU A 46 11080 7776 13275 1232 1237 -1882 C ATOM 365 CD1 LEU A 46 -23.063 15.490 19.530 1.00 80.09 C ANISOU 365 CD1 LEU A 46 10078 7681 12672 1163 1510 -2104 C ATOM 366 CD2 LEU A 46 -23.790 16.045 17.200 1.00 87.67 C ANISOU 366 CD2 LEU A 46 11369 8000 13943 1417 888 -1727 C ATOM 367 N CYS A 47 -19.576 15.100 17.158 1.00 89.01 N ANISOU 367 N CYS A 47 12562 8253 13004 886 1320 -1534 N ATOM 368 CA CYS A 47 -19.067 14.242 16.099 1.00 82.83 C ANISOU 368 CA CYS A 47 12132 7407 11934 814 1129 -1237 C ATOM 369 C CYS A 47 -19.949 13.007 15.980 1.00 81.87 C ANISOU 369 C CYS A 47 11890 7412 11806 758 989 -1123 C ATOM 370 O CYS A 47 -20.789 12.729 16.840 1.00 90.68 O ANISOU 370 O CYS A 47 12648 8724 13082 736 1095 -1236 O ATOM 371 CB CYS A 47 -17.610 13.837 16.365 1.00 77.78 C ANISOU 371 CB CYS A 47 11711 6975 10866 685 1342 -1222 C ATOM 372 SG CYS A 47 -16.963 12.541 15.284 1.00 99.11 S ANISOU 372 SG CYS A 47 14804 9682 13171 632 1171 -919 S ATOM 373 N HIS A 48 -19.746 12.258 14.893 1.00100.12 N ANISOU 373 N HIS A 48 14493 9618 13928 713 763 -919 N ATOM 374 CA HIS A 48 -20.528 11.044 14.681 1.00 89.66 C ANISOU 374 CA HIS A 48 13090 8352 12626 600 631 -859 C ATOM 375 C HIS A 48 -20.217 9.983 15.728 1.00 83.02 C ANISOU 375 C HIS A 48 12188 7727 11630 458 934 -851 C ATOM 376 O HIS A 48 -21.081 9.159 16.041 1.00 82.39 O ANISOU 376 O HIS A 48 11905 7704 11696 329 947 -840 O ATOM 377 CB HIS A 48 -20.280 10.486 13.280 1.00 90.01 C ANISOU 377 CB HIS A 48 13476 8250 12473 583 336 -717 C ATOM 378 CG HIS A 48 -21.135 9.304 12.946 1.00124.46 C ANISOU 378 CG HIS A 48 17757 12621 16909 425 175 -735 C ATOM 379 CD2 HIS A 48 -22.423 9.223 12.534 1.00130.05 C ANISOU 379 CD2 HIS A 48 18188 13353 17871 387 -83 -807 C ATOM 380 ND1 HIS A 48 -20.679 8.006 13.031 1.00108.33 N ANISOU 380 ND1 HIS A 48 15917 10558 14685 267 293 -700 N ATOM 381 CE1 HIS A 48 -21.647 7.177 12.683 1.00110.91 C ANISOU 381 CE1 HIS A 48 16119 10837 15187 92 129 -771 C ATOM 382 NE2 HIS A 48 -22.716 7.890 12.377 1.00121.34 N ANISOU 382 NE2 HIS A 48 17121 12230 16752 145 -111 -849 N ATOM 383 N THR A 49 -18.999 9.982 16.273 1.00 82.77 N ANISOU 383 N THR A 49 12313 7841 11296 479 1188 -834 N ATOM 384 CA THR A 49 -18.651 9.023 17.318 1.00 81.96 C ANISOU 384 CA THR A 49 12143 7999 11000 419 1493 -764 C ATOM 385 C THR A 49 -19.488 9.255 18.572 1.00 76.46 C ANISOU 385 C THR A 49 10985 7566 10499 399 1702 -880 C ATOM 386 O THR A 49 -20.003 8.305 19.181 1.00 85.16 O ANISOU 386 O THR A 49 11937 8792 11630 299 1851 -761 O ATOM 387 CB THR A 49 -17.158 9.127 17.640 1.00 72.67 C ANISOU 387 CB THR A 49 11158 7037 9417 497 1700 -744 C ATOM 388 CG2 THR A 49 -16.730 8.002 18.568 1.00 56.12 C ANISOU 388 CG2 THR A 49 9041 5223 7059 511 1989 -582 C ATOM 389 OG1 THR A 49 -16.398 9.054 16.427 1.00 68.97 O ANISOU 389 OG1 THR A 49 11080 6364 8761 527 1508 -654 O ATOM 390 N ASP A 50 -19.626 10.523 18.972 1.00 69.47 N ANISOU 390 N ASP A 50 9876 6763 9758 491 1738 -1116 N ATOM 391 CA ASP A 50 -20.448 10.864 20.128 1.00 68.88 C ANISOU 391 CA ASP A 50 9334 6980 9859 509 1930 -1293 C ATOM 392 C ASP A 50 -21.870 10.347 19.960 1.00 76.30 C ANISOU 392 C ASP A 50 10023 7855 11112 425 1795 -1229 C ATOM 393 O ASP A 50 -22.412 9.691 20.854 1.00 74.26 O ANISOU 393 O ASP A 50 9477 7881 10857 331 2007 -1172 O ATOM 394 CB ASP A 50 -20.458 12.379 20.342 1.00 80.47 C ANISOU 394 CB ASP A 50 10648 8411 11517 642 1941 -1614 C ATOM 395 CG ASP A 50 -19.097 12.927 20.713 1.00 77.83 C ANISOU 395 CG ASP A 50 10460 8219 10891 649 2130 -1759 C ATOM 396 OD1 ASP A 50 -18.493 12.417 21.681 1.00 76.16 O ANISOU 396 OD1 ASP A 50 10137 8462 10339 619 2396 -1768 O ATOM 397 OD2 ASP A 50 -18.636 13.878 20.046 1.00 90.50 O1- ANISOU 397 OD2 ASP A 50 12271 9511 12602 681 2020 -1854 O1- ATOM 398 N VAL A 51 -22.487 10.629 18.811 1.00 67.37 N ANISOU 398 N VAL A 51 8971 6401 10224 451 1447 -1224 N ATOM 399 CA VAL A 51 -23.871 10.221 18.589 1.00 77.15 C ANISOU 399 CA VAL A 51 9906 7649 11758 360 1284 -1218 C ATOM 400 C VAL A 51 -23.978 8.705 18.488 1.00 81.18 C ANISOU 400 C VAL A 51 10526 8134 12186 92 1325 -1016 C ATOM 401 O VAL A 51 -24.957 8.107 18.951 1.00 80.41 O ANISOU 401 O VAL A 51 10092 8187 12273 -83 1406 -999 O ATOM 402 CB VAL A 51 -24.434 10.911 17.333 1.00 68.69 C ANISOU 402 CB VAL A 51 8880 6319 10900 497 879 -1253 C ATOM 403 CG1 VAL A 51 -25.893 10.539 17.134 1.00 70.18 C ANISOU 403 CG1 VAL A 51 8667 6628 11370 409 697 -1294 C ATOM 404 CG2 VAL A 51 -24.276 12.418 17.441 1.00 80.65 C ANISOU 404 CG2 VAL A 51 10349 7742 12551 778 885 -1410 C ATOM 405 N TYR A 52 -22.980 8.059 17.883 1.00 76.19 N ANISOU 405 N TYR A 52 10360 7293 11297 52 1290 -867 N ATOM 406 CA TYR A 52 -23.009 6.607 17.739 1.00 81.27 C ANISOU 406 CA TYR A 52 11175 7803 11902 -179 1347 -696 C ATOM 407 C TYR A 52 -23.003 5.926 19.100 1.00 76.39 C ANISOU 407 C TYR A 52 10371 7432 11221 -267 1767 -539 C ATOM 408 O TYR A 52 -23.776 4.993 19.343 1.00 92.17 O ANISOU 408 O TYR A 52 12220 9389 13409 -513 1864 -433 O ATOM 409 CB TYR A 52 -21.818 6.142 16.895 1.00 85.38 C ANISOU 409 CB TYR A 52 12234 8079 12127 -123 1263 -597 C ATOM 410 CG TYR A 52 -21.806 4.660 16.575 1.00 76.02 C ANISOU 410 CG TYR A 52 11298 6642 10945 -325 1300 -471 C ATOM 411 CD1 TYR A 52 -21.198 3.747 17.428 1.00 89.94 C ANISOU 411 CD1 TYR A 52 13196 8425 12553 -334 1662 -244 C ATOM 412 CD2 TYR A 52 -22.394 4.176 15.411 1.00 93.18 C ANISOU 412 CD2 TYR A 52 13574 8556 13272 -492 979 -589 C ATOM 413 CE1 TYR A 52 -21.180 2.393 17.134 1.00 94.34 C ANISOU 413 CE1 TYR A 52 14026 8646 13175 -500 1729 -121 C ATOM 414 CE2 TYR A 52 -22.380 2.825 15.110 1.00 93.83 C ANISOU 414 CE2 TYR A 52 13904 8341 13406 -703 1030 -546 C ATOM 415 CZ TYR A 52 -21.773 1.938 15.975 1.00 99.88 C ANISOU 415 CZ TYR A 52 14844 9026 14082 -705 1417 -304 C ATOM 416 OH TYR A 52 -21.759 0.594 15.676 1.00 90.29 O ANISOU 416 OH TYR A 52 13915 7414 12978 -897 1499 -253 O ATOM 417 N PHE A 53 -22.142 6.384 20.009 1.00 75.39 N ANISOU 417 N PHE A 53 10229 7597 10818 -84 2031 -517 N ATOM 418 CA PHE A 53 -22.104 5.749 21.320 1.00 77.55 C ANISOU 418 CA PHE A 53 10307 8206 10953 -118 2434 -323 C ATOM 419 C PHE A 53 -23.119 6.332 22.294 1.00 80.17 C ANISOU 419 C PHE A 53 10072 8933 11456 -137 2580 -464 C ATOM 420 O PHE A 53 -23.303 5.772 23.380 1.00 81.73 O ANISOU 420 O PHE A 53 10039 9464 11550 -192 2918 -276 O ATOM 421 CB PHE A 53 -20.691 5.824 21.894 1.00 66.44 C ANISOU 421 CB PHE A 53 9097 7058 9089 98 2659 -233 C ATOM 422 CG PHE A 53 -19.737 4.888 21.219 1.00 86.97 C ANISOU 422 CG PHE A 53 12201 9360 11483 132 2630 -9 C ATOM 423 CD1 PHE A 53 -18.999 5.304 20.125 1.00 79.29 C ANISOU 423 CD1 PHE A 53 11567 8150 10411 219 2366 -133 C ATOM 424 CD2 PHE A 53 -19.615 3.577 21.648 1.00 81.71 C ANISOU 424 CD2 PHE A 53 11674 8631 10741 89 2882 342 C ATOM 425 CE1 PHE A 53 -18.135 4.438 19.487 1.00 87.58 C ANISOU 425 CE1 PHE A 53 13056 8964 11256 280 2345 37 C ATOM 426 CE2 PHE A 53 -18.753 2.705 21.014 1.00 85.03 C ANISOU 426 CE2 PHE A 53 12568 8738 11002 170 2866 521 C ATOM 427 CZ PHE A 53 -18.015 3.135 19.928 1.00 94.02 C ANISOU 427 CZ PHE A 53 14013 9696 12014 271 2590 341 C ATOM 428 N TRP A 54 -23.787 7.425 21.927 1.00 76.67 N ANISOU 428 N TRP A 54 9395 8474 11262 -63 2347 -766 N ATOM 429 CA TRP A 54 -24.921 7.916 22.699 1.00 77.29 C ANISOU 429 CA TRP A 54 8910 8899 11558 -65 2450 -932 C ATOM 430 C TRP A 54 -26.185 7.134 22.370 1.00 77.16 C ANISOU 430 C TRP A 54 8663 8791 11865 -342 2355 -837 C ATOM 431 O TRP A 54 -26.990 6.843 23.262 1.00 77.16 O ANISOU 431 O TRP A 54 8226 9143 11947 -465 2596 -789 O ATOM 432 CB TRP A 54 -25.111 9.409 22.426 1.00 71.17 C ANISOU 432 CB TRP A 54 7994 8098 10948 180 2252 -1291 C ATOM 433 CG TRP A 54 -26.461 9.952 22.764 1.00 73.99 C ANISOU 433 CG TRP A 54 7803 8681 11626 226 2226 -1498 C ATOM 434 CD1 TRP A 54 -26.952 10.216 24.008 1.00 76.52 C ANISOU 434 CD1 TRP A 54 7642 9509 11924 281 2525 -1639 C ATOM 435 CD2 TRP A 54 -27.491 10.321 21.838 1.00 80.32 C ANISOU 435 CD2 TRP A 54 8447 9286 12783 264 1877 -1598 C ATOM 436 CE2 TRP A 54 -28.582 10.793 22.594 1.00 79.64 C ANISOU 436 CE2 TRP A 54 7771 9590 12899 352 1991 -1799 C ATOM 437 CE3 TRP A 54 -27.598 10.293 20.444 1.00 75.43 C ANISOU 437 CE3 TRP A 54 8100 8272 12290 258 1477 -1538 C ATOM 438 NE1 TRP A 54 -28.228 10.719 23.915 1.00 80.24 N ANISOU 438 NE1 TRP A 54 7664 10086 12738 352 2395 -1831 N ATOM 439 CZ2 TRP A 54 -29.763 11.235 22.003 1.00 84.40 C ANISOU 439 CZ2 TRP A 54 8039 10190 13840 454 1714 -1930 C ATOM 440 CZ3 TRP A 54 -28.773 10.731 19.859 1.00 80.84 C ANISOU 440 CZ3 TRP A 54 8452 8981 13282 352 1193 -1657 C ATOM 441 CH2 TRP A 54 -29.840 11.194 20.638 1.00 82.27 C ANISOU 441 CH2 TRP A 54 8036 9546 13676 457 1310 -1846 C ATOM 442 N GLU A 55 -26.370 6.783 21.096 1.00 73.75 N ANISOU 442 N GLU A 55 8487 7938 11595 -463 2012 -828 N ATOM 443 CA GLU A 55 -27.459 5.889 20.719 1.00 82.86 C ANISOU 443 CA GLU A 55 9447 9000 13036 -801 1920 -775 C ATOM 444 C GLU A 55 -27.223 4.490 21.272 1.00 94.79 C ANISOU 444 C GLU A 55 11115 10423 14480 -1086 2255 -450 C ATOM 445 O GLU A 55 -28.133 3.873 21.840 1.00 89.02 O ANISOU 445 O GLU A 55 10027 9852 13945 -1369 2454 -348 O ATOM 446 CB GLU A 55 -27.603 5.849 19.198 1.00 82.02 C ANISOU 446 CB GLU A 55 9590 8526 13050 -848 1462 -891 C ATOM 447 CG GLU A 55 -28.251 7.084 18.595 1.00 88.63 C ANISOU 447 CG GLU A 55 10164 9467 14045 -598 1119 -1138 C ATOM 448 CD GLU A 55 -28.369 7.001 17.084 1.00 94.83 C ANISOU 448 CD GLU A 55 11177 9989 14864 -617 665 -1208 C ATOM 449 OE1 GLU A 55 -27.340 7.163 16.394 1.00 96.25 O ANISOU 449 OE1 GLU A 55 11845 9909 14814 -469 544 -1150 O ATOM 450 OE2 GLU A 55 -29.490 6.770 16.586 1.00102.57 O1- ANISOU 450 OE2 GLU A 55 11815 11087 16069 -783 432 -1332 O1- ATOM 451 N ALA A 56 -26.004 3.977 21.110 1.00 90.03 N ANISOU 451 N ALA A 56 11039 9562 13608 -1003 2338 -262 N ATOM 452 CA ALA A 56 -25.593 2.679 21.644 1.00 94.15 C ANISOU 452 CA ALA A 56 11793 9939 14041 -1166 2684 105 C ATOM 453 C ALA A 56 -26.564 1.577 21.220 1.00107.09 C ANISOU 453 C ALA A 56 13379 11247 16065 -1619 2663 162 C ATOM 454 O ALA A 56 -27.148 0.870 22.040 1.00108.11 O ANISOU 454 O ALA A 56 13270 11475 16334 -1872 2997 401 O ATOM 455 CB ALA A 56 -25.451 2.738 23.167 1.00 83.76 C ANISOU 455 CB ALA A 56 10188 9139 12497 -1050 3132 330 C ATOM 456 N LYS A 57 -26.721 1.441 19.902 1.00115.95 N ANISOU 456 N LYS A 57 14717 11992 17345 -1739 2271 -73 N ATOM 457 CA LYS A 57 -27.662 0.479 19.341 1.00132.00 C ANISOU 457 CA LYS A 57 16674 13722 19757 -2212 2186 -151 C ATOM 458 C LYS A 57 -27.129 -0.949 19.318 1.00131.63 C ANISOU 458 C LYS A 57 17106 13140 19768 -2426 2442 105 C ATOM 459 O LYS A 57 -27.892 -1.869 19.007 1.00124.39 O ANISOU 459 O LYS A 57 16137 11910 19214 -2888 2459 47 O ATOM 460 CB LYS A 57 -28.058 0.894 17.921 1.00130.90 C ANISOU 460 CB LYS A 57 16542 13478 19715 -2239 1649 -545 C ATOM 461 CG LYS A 57 -29.198 1.899 17.857 1.00117.14 C ANISOU 461 CG LYS A 57 14189 12188 18133 -2208 1404 -794 C ATOM 462 CD LYS A 57 -30.311 1.540 18.826 1.00127.97 C ANISOU 462 CD LYS A 57 14997 13847 19779 -2538 1694 -716 C ATOM 463 CE LYS A 57 -31.671 1.946 18.281 1.00133.01 C ANISOU 463 CE LYS A 57 15055 14797 20685 -2703 1361 -1041 C ATOM 464 NZ LYS A 57 -32.756 1.048 18.766 1.00130.20 N1+ ANISOU 464 NZ LYS A 57 14262 14541 20666 -3256 1592 -1011 N1+ ATOM 465 N GLY A 58 -25.855 -1.159 19.635 1.00125.19 N ANISOU 465 N GLY A 58 16737 12205 18623 -2104 2646 370 N ATOM 466 CA GLY A 58 -25.291 -2.494 19.634 1.00112.94 C ANISOU 466 CA GLY A 58 15669 10116 17129 -2211 2909 645 C ATOM 467 C GLY A 58 -24.035 -2.594 20.473 1.00122.97 C ANISOU 467 C GLY A 58 17221 11515 17985 -1783 3244 1048 C ATOM 468 O GLY A 58 -23.159 -3.422 20.206 1.00131.57 O ANISOU 468 O GLY A 58 18824 12185 18982 -1648 3356 1223 O ATOM 469 N GLN A 59 -23.943 -1.748 21.491 1.00119.19 N ANISOU 469 N GLN A 59 16677 16886 11724 -2915 394 -1213 N ATOM 470 CA GLN A 59 -22.772 -1.636 22.346 1.00110.23 C ANISOU 470 CA GLN A 59 15745 15352 10785 -2472 682 -1495 C ATOM 471 C GLN A 59 -23.155 -2.044 23.766 1.00104.56 C ANISOU 471 C GLN A 59 15182 14069 10478 -2348 782 -1568 C ATOM 472 O GLN A 59 -24.280 -2.475 24.030 1.00 96.26 O ANISOU 472 O GLN A 59 14082 12948 9544 -2584 661 -1442 O ATOM 473 CB GLN A 59 -22.201 -0.210 22.339 1.00100.95 C ANISOU 473 CB GLN A 59 14236 14312 9807 -2206 818 -1111 C ATOM 474 CG GLN A 59 -21.862 0.459 20.984 1.00102.61 C ANISOU 474 CG GLN A 59 14193 15139 9656 -2347 710 -870 C ATOM 475 CD GLN A 59 -22.923 0.283 19.909 1.00120.61 C ANISOU 475 CD GLN A 59 16294 17916 11615 -2848 394 -607 C ATOM 476 NE2 GLN A 59 -22.495 -0.056 18.703 1.00123.04 N ANISOU 476 NE2 GLN A 59 16736 18715 11299 -3115 301 -802 N ATOM 477 OE1 GLN A 59 -24.107 0.479 20.157 1.00125.03 O ANISOU 477 OE1 GLN A 59 16587 18433 12487 -3018 241 -210 O ATOM 478 N THR A 60 -22.201 -1.919 24.685 1.00101.06 N ANISOU 478 N THR A 60 14923 13241 10234 -2018 988 -1742 N ATOM 479 CA THR A 60 -22.535 -2.042 26.098 1.00 89.62 C ANISOU 479 CA THR A 60 13598 11318 9135 -1941 1103 -1721 C ATOM 480 C THR A 60 -23.122 -0.714 26.559 1.00 86.97 C ANISOU 480 C THR A 60 12902 11000 9144 -1847 1268 -1261 C ATOM 481 O THR A 60 -22.402 0.291 26.617 1.00 90.62 O ANISOU 481 O THR A 60 13249 11469 9713 -1614 1397 -1130 O ATOM 482 CB THR A 60 -21.310 -2.401 26.940 1.00 88.45 C ANISOU 482 CB THR A 60 13792 10754 9061 -1702 1207 -2022 C ATOM 483 CG2 THR A 60 -21.694 -2.506 28.411 1.00 68.22 C ANISOU 483 CG2 THR A 60 11390 7762 6767 -1720 1305 -1966 C ATOM 484 OG1 THR A 60 -20.774 -3.656 26.508 1.00 95.19 O ANISOU 484 OG1 THR A 60 14930 11515 9723 -1756 1089 -2452 O ATOM 485 N PRO A 61 -24.416 -0.659 26.880 1.00 85.36 N ANISOU 485 N PRO A 61 12487 10775 9169 -2018 1285 -1002 N ATOM 486 CA PRO A 61 -25.002 0.610 27.334 1.00 73.78 C ANISOU 486 CA PRO A 61 10642 9254 8137 -1896 1519 -595 C ATOM 487 C PRO A 61 -24.387 1.077 28.644 1.00 82.82 C ANISOU 487 C PRO A 61 12031 9966 9471 -1662 1827 -743 C ATOM 488 O PRO A 61 -24.805 0.660 29.728 1.00 77.04 O ANISOU 488 O PRO A 61 11507 8928 8837 -1731 1990 -858 O ATOM 489 CB PRO A 61 -26.494 0.285 27.484 1.00 76.76 C ANISOU 489 CB PRO A 61 10775 9648 8741 -2142 1500 -345 C ATOM 490 CG PRO A 61 -26.558 -1.188 27.634 1.00 80.32 C ANISOU 490 CG PRO A 61 11619 10003 8898 -2359 1311 -692 C ATOM 491 CD PRO A 61 -25.384 -1.770 26.909 1.00 83.65 C ANISOU 491 CD PRO A 61 12360 10533 8891 -2322 1118 -1070 C ATOM 492 N LEU A 62 -23.382 1.945 28.539 1.00 82.77 N ANISOU 492 N LEU A 62 12013 9954 9482 -1433 1888 -721 N ATOM 493 CA LEU A 62 -22.602 2.413 29.682 1.00 75.86 C ANISOU 493 CA LEU A 62 11423 8689 8710 -1262 2107 -866 C ATOM 494 C LEU A 62 -23.150 3.788 30.052 1.00 78.94 C ANISOU 494 C LEU A 62 11494 8958 9540 -1145 2399 -577 C ATOM 495 O LEU A 62 -22.778 4.795 29.446 1.00 75.35 O ANISOU 495 O LEU A 62 10752 8635 9241 -997 2374 -341 O ATOM 496 CB LEU A 62 -21.119 2.477 29.323 1.00 76.23 C ANISOU 496 CB LEU A 62 11641 8777 8547 -1101 1968 -1001 C ATOM 497 CG LEU A 62 -20.084 1.553 29.974 1.00 88.18 C ANISOU 497 CG LEU A 62 13623 10014 9868 -1092 1879 -1334 C ATOM 498 CD1 LEU A 62 -18.680 1.918 29.494 1.00 69.57 C ANISOU 498 CD1 LEU A 62 11265 7731 7436 -893 1789 -1339 C ATOM 499 CD2 LEU A 62 -20.150 1.528 31.488 1.00 81.63 C ANISOU 499 CD2 LEU A 62 13126 8754 9134 -1172 2037 -1419 C ATOM 500 N PHE A 63 -24.051 3.831 31.029 1.00 71.69 N ANISOU 500 N PHE A 63 10606 7779 8855 -1218 2697 -592 N ATOM 501 CA PHE A 63 -24.716 5.063 31.426 1.00 73.34 C ANISOU 501 CA PHE A 63 10494 7802 9571 -1100 3067 -373 C ATOM 502 C PHE A 63 -24.824 5.115 32.942 1.00 71.84 C ANISOU 502 C PHE A 63 10696 7191 9408 -1148 3472 -651 C ATOM 503 O PHE A 63 -24.912 4.068 33.593 1.00 78.10 O ANISOU 503 O PHE A 63 11857 7918 9901 -1344 3446 -876 O ATOM 504 CB PHE A 63 -26.116 5.174 30.798 1.00 70.22 C ANISOU 504 CB PHE A 63 9520 7605 9555 -1176 3092 10 C ATOM 505 CG PHE A 63 -26.098 5.371 29.309 1.00 74.64 C ANISOU 505 CG PHE A 63 9656 8605 10100 -1198 2702 369 C ATOM 506 CD1 PHE A 63 -25.775 6.602 28.766 1.00 74.64 C ANISOU 506 CD1 PHE A 63 9293 8653 10413 -1025 2692 681 C ATOM 507 CD2 PHE A 63 -26.401 4.324 28.453 1.00 68.59 C ANISOU 507 CD2 PHE A 63 8874 8204 8981 -1440 2330 399 C ATOM 508 CE1 PHE A 63 -25.754 6.789 27.397 1.00 72.21 C ANISOU 508 CE1 PHE A 63 8601 8803 10031 -1115 2313 1059 C ATOM 509 CE2 PHE A 63 -26.383 4.504 27.082 1.00 68.18 C ANISOU 509 CE2 PHE A 63 8488 8605 8815 -1543 1973 716 C ATOM 510 CZ PHE A 63 -26.059 5.739 26.554 1.00 76.87 C ANISOU 510 CZ PHE A 63 9215 9801 10191 -1392 1962 1067 C ATOM 511 N PRO A 64 -24.824 6.321 33.538 1.00 79.86 N ANISOU 511 N PRO A 64 11662 7910 10772 -1009 3851 -647 N ATOM 512 CA PRO A 64 -24.763 7.658 32.919 1.00 75.33 C ANISOU 512 CA PRO A 64 10640 7312 10670 -780 3912 -358 C ATOM 513 C PRO A 64 -23.372 8.022 32.410 1.00 74.87 C ANISOU 513 C PRO A 64 10719 7343 10386 -670 3577 -347 C ATOM 514 O PRO A 64 -22.366 7.630 32.995 1.00 75.47 O ANISOU 514 O PRO A 64 11310 7299 10064 -730 3474 -628 O ATOM 515 CB PRO A 64 -25.209 8.580 34.062 1.00 70.99 C ANISOU 515 CB PRO A 64 10166 6291 10515 -719 4509 -517 C ATOM 516 CG PRO A 64 -24.744 7.873 35.298 1.00 82.33 C ANISOU 516 CG PRO A 64 12317 7538 11427 -935 4626 -958 C ATOM 517 CD PRO A 64 -24.934 6.407 35.006 1.00 65.31 C ANISOU 517 CD PRO A 64 10258 5688 8868 -1122 4286 -963 C ATOM 518 N ARG A 65 -23.288 8.787 31.323 1.00 67.70 N ANISOU 518 N ARG A 65 9319 6652 9752 -533 3389 31 N ATOM 519 CA ARG A 65 -22.019 9.054 30.665 1.00 65.97 C ANISOU 519 CA ARG A 65 9149 6616 9301 -449 3055 107 C ATOM 520 C ARG A 65 -21.973 10.485 30.151 1.00 74.67 C ANISOU 520 C ARG A 65 9780 7666 10927 -281 3074 497 C ATOM 521 O ARG A 65 -22.990 11.033 29.716 1.00 71.88 O ANISOU 521 O ARG A 65 8888 7341 11081 -248 3167 848 O ATOM 522 CB ARG A 65 -21.795 8.080 29.503 1.00 60.80 C ANISOU 522 CB ARG A 65 8405 6482 8212 -549 2649 181 C ATOM 523 CG ARG A 65 -20.340 7.835 29.162 1.00 64.61 C ANISOU 523 CG ARG A 65 9147 7108 8296 -494 2393 58 C ATOM 524 CD ARG A 65 -20.214 6.757 28.103 1.00 69.47 C ANISOU 524 CD ARG A 65 9737 8187 8471 -609 2107 8 C ATOM 525 NE ARG A 65 -18.897 6.134 28.111 1.00 61.74 N ANISOU 525 NE ARG A 65 9109 7217 7133 -556 1974 -259 N ATOM 526 CZ ARG A 65 -18.461 5.299 27.179 1.00 66.21 C ANISOU 526 CZ ARG A 65 9693 8136 7328 -606 1790 -376 C ATOM 527 NH1 ARG A 65 -19.219 4.956 26.150 1.00 65.18 N1+ ANISOU 527 NH1 ARG A 65 9318 8417 7031 -769 1670 -269 N1+ ATOM 528 NH2 ARG A 65 -17.235 4.795 27.281 1.00 70.61 N ANISOU 528 NH2 ARG A 65 10518 8618 7691 -512 1732 -602 N ATOM 529 N ILE A 66 -20.785 11.079 30.204 1.00 56.81 N ANISOU 529 N ILE A 66 7688 5308 8591 -188 2955 483 N ATOM 530 CA ILE A 66 -20.519 12.389 29.621 1.00 63.52 C ANISOU 530 CA ILE A 66 8108 6134 9894 -48 2876 887 C ATOM 531 C ILE A 66 -19.728 12.170 28.339 1.00 62.00 C ANISOU 531 C ILE A 66 7708 6502 9348 -73 2436 1166 C ATOM 532 O ILE A 66 -18.617 11.627 28.372 1.00 76.61 O ANISOU 532 O ILE A 66 9917 8462 10728 -84 2273 954 O ATOM 533 CB ILE A 66 -19.753 13.298 30.595 1.00 65.10 C ANISOU 533 CB ILE A 66 8639 5813 10282 34 3051 702 C ATOM 534 CG1 ILE A 66 -20.612 13.621 31.820 1.00 67.07 C ANISOU 534 CG1 ILE A 66 9089 5518 10875 28 3575 393 C ATOM 535 CG2 ILE A 66 -19.310 14.574 29.896 1.00 64.81 C ANISOU 535 CG2 ILE A 66 8164 5772 10691 163 2878 1152 C ATOM 536 CD1 ILE A 66 -19.835 14.243 32.962 1.00 61.36 C ANISOU 536 CD1 ILE A 66 8903 4284 10124 -6 3757 60 C ATOM 537 N PHE A 67 -20.296 12.585 27.211 1.00 71.80 N ANISOU 537 N PHE A 67 11293 6165 9823 89 567 1069 N ATOM 538 CA PHE A 67 -19.669 12.379 25.914 1.00 62.38 C ANISOU 538 CA PHE A 67 10050 5102 8550 439 411 814 C ATOM 539 C PHE A 67 -18.850 13.611 25.529 1.00 69.65 C ANISOU 539 C PHE A 67 10930 6302 9233 530 806 775 C ATOM 540 O PHE A 67 -18.581 14.491 26.351 1.00 68.59 O ANISOU 540 O PHE A 67 10830 6190 9041 332 1128 899 O ATOM 541 CB PHE A 67 -20.731 12.047 24.868 1.00 65.53 C ANISOU 541 CB PHE A 67 10378 5465 9054 616 234 784 C ATOM 542 CG PHE A 67 -21.392 10.712 25.075 1.00 69.13 C ANISOU 542 CG PHE A 67 10851 5627 9788 565 -258 802 C ATOM 543 CD1 PHE A 67 -20.673 9.538 24.927 1.00 64.59 C ANISOU 543 CD1 PHE A 67 10286 4930 9326 717 -751 578 C ATOM 544 CD2 PHE A 67 -22.734 10.633 25.415 1.00 63.24 C ANISOU 544 CD2 PHE A 67 10089 4724 9215 363 -260 1048 C ATOM 545 CE1 PHE A 67 -21.277 8.309 25.114 1.00 66.64 C ANISOU 545 CE1 PHE A 67 10547 4865 9909 656 -1273 619 C ATOM 546 CE2 PHE A 67 -23.343 9.406 25.604 1.00 73.66 C ANISOU 546 CE2 PHE A 67 11400 5763 10823 284 -748 1121 C ATOM 547 CZ PHE A 67 -22.614 8.243 25.454 1.00 67.28 C ANISOU 547 CZ PHE A 67 10610 4785 10169 424 -1273 918 C ATOM 548 N GLY A 68 -18.441 13.682 24.264 1.00 65.20 N ANISOU 548 N GLY A 68 10266 5975 8531 831 758 609 N ATOM 549 CA GLY A 68 -17.673 14.808 23.769 1.00 65.88 C ANISOU 549 CA GLY A 68 10269 6365 8398 905 1086 634 C ATOM 550 C GLY A 68 -16.180 14.548 23.752 1.00 72.91 C ANISOU 550 C GLY A 68 11130 7448 9124 1021 1003 451 C ATOM 551 O GLY A 68 -15.642 13.947 24.687 1.00 65.26 O ANISOU 551 O GLY A 68 10262 6306 8229 906 856 388 O ATOM 552 N HIS A 69 -15.496 14.999 22.698 1.00 76.90 N ANISOU 552 N HIS A 69 11478 8345 9395 1241 1092 384 N ATOM 553 CA HIS A 69 -14.056 14.794 22.589 1.00 73.82 C ANISOU 553 CA HIS A 69 11015 8218 8815 1373 1028 205 C ATOM 554 C HIS A 69 -13.382 15.890 21.770 1.00 72.26 C ANISOU 554 C HIS A 69 10627 8472 8356 1445 1317 333 C ATOM 555 O HIS A 69 -12.182 16.134 21.929 1.00 82.26 O ANISOU 555 O HIS A 69 11831 9947 9477 1444 1395 306 O ATOM 556 CB HIS A 69 -13.754 13.420 21.985 1.00 63.45 C ANISOU 556 CB HIS A 69 9641 6991 7475 1691 564 -171 C ATOM 557 CG HIS A 69 -14.390 13.189 20.650 1.00 65.02 C ANISOU 557 CG HIS A 69 9688 7439 7577 1986 426 -294 C ATOM 558 CD2 HIS A 69 -13.909 13.343 19.393 1.00 66.88 C ANISOU 558 CD2 HIS A 69 9688 8219 7504 2293 429 -438 C ATOM 559 ND1 HIS A 69 -15.682 12.729 20.511 1.00 68.13 N ANISOU 559 ND1 HIS A 69 10147 7551 8187 1985 250 -274 N ATOM 560 CE1 HIS A 69 -15.971 12.615 19.227 1.00 71.09 C ANISOU 560 CE1 HIS A 69 10353 8251 8407 2289 145 -421 C ATOM 561 NE2 HIS A 69 -14.913 12.981 18.528 1.00 67.93 N ANISOU 561 NE2 HIS A 69 9761 8380 7669 2484 255 -523 N ATOM 562 N GLU A 70 -14.131 16.545 20.885 1.00 71.53 N ANISOU 562 N GLU A 70 10426 8543 8210 1496 1458 501 N ATOM 563 CA GLU A 70 -13.626 17.699 20.146 1.00 73.66 C ANISOU 563 CA GLU A 70 10498 9218 8274 1496 1726 735 C ATOM 564 C GLU A 70 -13.863 18.942 20.992 1.00 82.29 C ANISOU 564 C GLU A 70 11682 10017 9568 1163 2034 1059 C ATOM 565 O GLU A 70 -15.012 19.342 21.204 1.00 72.80 O ANISOU 565 O GLU A 70 10563 8528 8570 1040 2119 1195 O ATOM 566 CB GLU A 70 -14.312 17.838 18.789 1.00 76.63 C ANISOU 566 CB GLU A 70 10695 9918 8503 1698 1702 789 C ATOM 567 CG GLU A 70 -14.675 16.540 18.097 1.00 79.96 C ANISOU 567 CG GLU A 70 11082 10445 8855 2024 1341 425 C ATOM 568 CD GLU A 70 -14.843 16.722 16.599 1.00 84.48 C ANISOU 568 CD GLU A 70 11393 11571 9136 2288 1327 433 C ATOM 569 OE1 GLU A 70 -14.720 17.870 16.121 1.00 86.06 O ANISOU 569 OE1 GLU A 70 11442 12057 9202 2178 1601 782 O ATOM 570 OE2 GLU A 70 -15.112 15.725 15.900 1.00103.67 O1- ANISOU 570 OE2 GLU A 70 13754 14153 11484 2603 1015 99 O1- ATOM 571 N ALA A 71 -12.786 19.558 21.470 1.00 78.92 N ANISOU 571 N ALA A 71 11223 9665 9097 1033 2180 1158 N ATOM 572 CA ALA A 71 -12.933 20.720 22.333 1.00 76.73 C ANISOU 572 CA ALA A 71 11023 9086 9044 744 2418 1404 C ATOM 573 C ALA A 71 -11.632 21.507 22.370 1.00 76.65 C ANISOU 573 C ALA A 71 10884 9298 8942 659 2546 1558 C ATOM 574 O ALA A 71 -10.593 21.066 21.874 1.00 80.17 O ANISOU 574 O ALA A 71 11194 10132 9133 807 2467 1461 O ATOM 575 CB ALA A 71 -13.347 20.316 23.750 1.00 66.02 C ANISOU 575 CB ALA A 71 9909 7272 7905 577 2394 1274 C ATOM 576 N GLY A 72 -11.720 22.693 22.964 1.00 76.36 N ANISOU 576 N GLY A 72 10869 9012 9132 426 2722 1789 N ATOM 577 CA GLY A 72 -10.573 23.517 23.281 1.00 69.76 C ANISOU 577 CA GLY A 72 9944 8247 8315 287 2820 1951 C ATOM 578 C GLY A 72 -10.779 24.179 24.627 1.00 71.10 C ANISOU 578 C GLY A 72 10281 7939 8795 64 2912 1945 C ATOM 579 O GLY A 72 -11.880 24.656 24.920 1.00 73.14 O ANISOU 579 O GLY A 72 10609 7903 9277 -11 2963 1983 O ATOM 580 N GLY A 73 -9.746 24.208 25.460 1.00 69.28 N ANISOU 580 N GLY A 73 10103 7651 8571 -26 2924 1868 N ATOM 581 CA GLY A 73 -9.916 24.722 26.799 1.00 67.83 C ANISOU 581 CA GLY A 73 10070 7062 8639 -204 2989 1795 C ATOM 582 C GLY A 73 -8.619 25.229 27.387 1.00 70.51 C ANISOU 582 C GLY A 73 10377 7396 9016 -316 3016 1831 C ATOM 583 O GLY A 73 -7.611 25.378 26.692 1.00 74.10 O ANISOU 583 O GLY A 73 10661 8162 9330 -286 3003 1982 O ATOM 584 N ILE A 74 -8.663 25.494 28.691 1.00 62.16 N ANISOU 584 N ILE A 74 9465 6016 8135 -442 3049 1687 N ATOM 585 CA ILE A 74 -7.540 26.054 29.432 1.00 70.48 C ANISOU 585 CA ILE A 74 10511 6989 9279 -559 3062 1688 C ATOM 586 C ILE A 74 -7.288 25.186 30.657 1.00 64.96 C ANISOU 586 C ILE A 74 10012 6179 8492 -585 3030 1398 C ATOM 587 O ILE A 74 -8.228 24.788 31.352 1.00 78.56 O ANISOU 587 O ILE A 74 11869 7741 10239 -604 3036 1243 O ATOM 588 CB ILE A 74 -7.806 27.520 29.837 1.00 69.99 C ANISOU 588 CB ILE A 74 10385 6630 9580 -692 3100 1810 C ATOM 589 CG1 ILE A 74 -8.022 28.384 28.591 1.00 62.15 C ANISOU 589 CG1 ILE A 74 9174 5736 8703 -698 3087 2165 C ATOM 590 CG2 ILE A 74 -6.655 28.066 30.665 1.00 72.68 C ANISOU 590 CG2 ILE A 74 10721 6854 10041 -805 3079 1781 C ATOM 591 CD1 ILE A 74 -8.503 29.789 28.885 1.00 85.88 C ANISOU 591 CD1 ILE A 74 12108 8384 12137 -809 3053 2279 C ATOM 592 N VAL A 75 -6.013 24.895 30.919 1.00 65.31 N ANISOU 592 N VAL A 75 10054 6333 8426 -597 2986 1349 N ATOM 593 CA VAL A 75 -5.646 23.988 32.001 1.00 70.79 C ANISOU 593 CA VAL A 75 10926 6950 9022 -625 2921 1104 C ATOM 594 C VAL A 75 -5.900 24.657 33.345 1.00 69.04 C ANISOU 594 C VAL A 75 10800 6446 8985 -771 2986 1001 C ATOM 595 O VAL A 75 -5.550 25.826 33.555 1.00 77.99 O ANISOU 595 O VAL A 75 11852 7455 10325 -846 3036 1076 O ATOM 596 CB VAL A 75 -4.179 23.555 31.862 1.00 68.63 C ANISOU 596 CB VAL A 75 10603 6879 8593 -585 2846 1072 C ATOM 597 CG1 VAL A 75 -3.752 22.708 33.051 1.00 68.16 C ANISOU 597 CG1 VAL A 75 10727 6700 8472 -637 2754 842 C ATOM 598 CG2 VAL A 75 -3.977 22.791 30.565 1.00 63.31 C ANISOU 598 CG2 VAL A 75 9806 6556 7693 -393 2760 1092 C ATOM 599 N GLU A 76 -6.511 23.912 34.266 1.00 69.70 N ANISOU 599 N GLU A 76 11034 6451 8998 -810 2959 830 N ATOM 600 CA GLU A 76 -6.768 24.375 35.624 1.00 67.56 C ANISOU 600 CA GLU A 76 10832 6020 8816 -926 3015 687 C ATOM 601 C GLU A 76 -5.709 23.899 36.610 1.00 73.59 C ANISOU 601 C GLU A 76 11693 6791 9476 -999 2950 559 C ATOM 602 O GLU A 76 -5.186 24.698 37.394 1.00 74.55 O ANISOU 602 O GLU A 76 11804 6814 9707 -1066 2989 477 O ATOM 603 CB GLU A 76 -8.160 23.914 36.076 1.00 77.60 C ANISOU 603 CB GLU A 76 12162 7282 10042 -949 3037 622 C ATOM 604 CG GLU A 76 -8.529 24.314 37.494 1.00 72.27 C ANISOU 604 CG GLU A 76 11515 6561 9385 -1048 3101 450 C ATOM 605 CD GLU A 76 -8.335 23.188 38.487 1.00 75.08 C ANISOU 605 CD GLU A 76 11984 7018 9524 -1149 3018 382 C ATOM 606 OE1 GLU A 76 -8.040 22.055 38.051 1.00 88.06 O ANISOU 606 OE1 GLU A 76 13697 8708 11054 -1137 2879 459 O ATOM 607 OE2 GLU A 76 -8.481 23.433 39.702 1.00 85.16 O1- ANISOU 607 OE2 GLU A 76 13264 8342 10749 -1235 3065 246 O1- ATOM 608 N SER A 77 -5.385 22.608 36.590 1.00 73.44 N ANISOU 608 N SER A 77 11762 6870 9273 -980 2818 527 N ATOM 609 CA SER A 77 -4.291 22.070 37.387 1.00 75.03 C ANISOU 609 CA SER A 77 12049 7078 9382 -1040 2720 425 C ATOM 610 C SER A 77 -3.786 20.804 36.713 1.00 76.80 C ANISOU 610 C SER A 77 12300 7410 9472 -940 2528 417 C ATOM 611 O SER A 77 -4.444 20.236 35.838 1.00 81.98 O ANISOU 611 O SER A 77 12928 8127 10093 -835 2457 460 O ATOM 612 CB SER A 77 -4.717 21.779 38.831 1.00 78.56 C ANISOU 612 CB SER A 77 12600 7483 9767 -1183 2712 321 C ATOM 613 OG SER A 77 -6.056 21.323 38.898 1.00 95.39 O ANISOU 613 OG SER A 77 14744 9644 11855 -1211 2713 366 O ATOM 614 N VAL A 78 -2.602 20.366 37.128 1.00 64.68 N ANISOU 614 N VAL A 78 10808 5893 7875 -954 2417 330 N ATOM 615 CA VAL A 78 -1.999 19.149 36.604 1.00 67.74 C ANISOU 615 CA VAL A 78 11207 6370 8160 -835 2183 253 C ATOM 616 C VAL A 78 -1.677 18.220 37.765 1.00 75.84 C ANISOU 616 C VAL A 78 12379 7285 9149 -954 1992 163 C ATOM 617 O VAL A 78 -1.365 18.661 38.877 1.00 71.01 O ANISOU 617 O VAL A 78 11830 6605 8545 -1104 2069 146 O ATOM 618 CB VAL A 78 -0.736 19.437 35.757 1.00 77.77 C ANISOU 618 CB VAL A 78 12337 7830 9382 -702 2189 236 C ATOM 619 CG1 VAL A 78 -1.006 20.545 34.749 1.00 77.49 C ANISOU 619 CG1 VAL A 78 12131 7922 9392 -648 2386 407 C ATOM 620 CG2 VAL A 78 0.452 19.793 36.642 1.00 76.09 C ANISOU 620 CG2 VAL A 78 12157 7567 9188 -804 2206 180 C ATOM 621 N GLY A 79 -1.777 16.920 37.503 1.00 84.14 N ANISOU 621 N GLY A 79 13474 8318 10177 -883 1707 108 N ATOM 622 CA GLY A 79 -1.454 15.922 38.496 1.00 71.47 C ANISOU 622 CA GLY A 79 11991 6593 8572 -1004 1452 67 C ATOM 623 C GLY A 79 0.041 15.735 38.651 1.00 87.97 C ANISOU 623 C GLY A 79 14081 8708 10635 -949 1340 -75 C ATOM 624 O GLY A 79 0.860 16.412 38.029 1.00 89.16 O ANISOU 624 O GLY A 79 14124 8999 10754 -829 1479 -130 O ATOM 625 N GLU A 80 0.397 14.782 39.507 1.00 85.62 N ANISOU 625 N GLU A 80 13890 8285 10358 -1053 1066 -108 N ATOM 626 CA GLU A 80 1.800 14.501 39.778 1.00 85.00 C ANISOU 626 CA GLU A 80 13822 8204 10269 -1012 922 -254 C ATOM 627 C GLU A 80 2.467 13.901 38.545 1.00 84.64 C ANISOU 627 C GLU A 80 13660 8274 10225 -723 719 -450 C ATOM 628 O GLU A 80 1.926 12.989 37.913 1.00 77.30 O ANISOU 628 O GLU A 80 12711 7305 9354 -593 456 -511 O ATOM 629 CB GLU A 80 1.919 13.558 40.975 1.00 84.84 C ANISOU 629 CB GLU A 80 13936 8011 10287 -1205 632 -214 C ATOM 630 CG GLU A 80 3.140 12.655 40.969 1.00 94.76 C ANISOU 630 CG GLU A 80 15205 9199 11599 -1103 285 -396 C ATOM 631 CD GLU A 80 3.036 11.542 41.994 1.00102.76 C ANISOU 631 CD GLU A 80 16337 10004 12702 -1301 -94 -299 C ATOM 632 OE1 GLU A 80 2.708 11.841 43.161 1.00105.87 O ANISOU 632 OE1 GLU A 80 16808 10394 13026 -1567 26 -115 O ATOM 633 OE2 GLU A 80 3.285 10.372 41.639 1.00101.23 O1- ANISOU 633 OE2 GLU A 80 16140 9668 12654 -1190 -536 -407 O1- ATOM 634 N GLY A 81 3.639 14.430 38.194 1.00 81.01 N ANISOU 634 N GLY A 81 13096 7987 9698 -611 830 -558 N ATOM 635 CA GLY A 81 4.409 13.950 37.071 1.00 85.83 C ANISOU 635 CA GLY A 81 13542 8819 10249 -320 666 -772 C ATOM 636 C GLY A 81 4.220 14.730 35.787 1.00 84.58 C ANISOU 636 C GLY A 81 13183 8978 9977 -154 915 -723 C ATOM 637 O GLY A 81 5.046 14.601 34.876 1.00 84.23 O ANISOU 637 O GLY A 81 12944 9247 9815 79 860 -879 O ATOM 638 N VAL A 82 3.160 15.529 35.685 1.00 76.28 N ANISOU 638 N VAL A 82 12149 7889 8946 -263 1175 -507 N ATOM 639 CA VAL A 82 2.912 16.304 34.473 1.00 67.92 C ANISOU 639 CA VAL A 82 10894 7118 7795 -135 1395 -406 C ATOM 640 C VAL A 82 3.930 17.439 34.418 1.00 88.79 C ANISOU 640 C VAL A 82 13398 9947 10392 -192 1636 -292 C ATOM 641 O VAL A 82 3.889 18.362 35.236 1.00 87.21 O ANISOU 641 O VAL A 82 13276 9559 10300 -408 1827 -141 O ATOM 642 CB VAL A 82 1.478 16.843 34.427 1.00 85.84 C ANISOU 642 CB VAL A 82 13223 9255 10137 -243 1573 -209 C ATOM 643 CG1 VAL A 82 1.314 17.802 33.256 1.00 77.66 C ANISOU 643 CG1 VAL A 82 11979 8501 9028 -150 1804 -53 C ATOM 644 CG2 VAL A 82 0.483 15.701 34.330 1.00 74.09 C ANISOU 644 CG2 VAL A 82 11831 7620 8700 -180 1313 -292 C ATOM 645 N THR A 83 4.848 17.371 33.454 1.00 90.56 N ANISOU 645 N THR A 83 13389 10562 10459 6 1605 -370 N ATOM 646 CA THR A 83 5.860 18.398 33.270 1.00 90.18 C ANISOU 646 CA THR A 83 13155 10747 10364 -55 1803 -212 C ATOM 647 C THR A 83 5.756 19.122 31.936 1.00 91.04 C ANISOU 647 C THR A 83 12976 11280 10336 39 1974 -2 C ATOM 648 O THR A 83 6.383 20.176 31.776 1.00 85.54 O ANISOU 648 O THR A 83 12109 10740 9652 -77 2150 245 O ATOM 649 CB THR A 83 7.269 17.795 33.401 1.00 81.05 C ANISOU 649 CB THR A 83 11914 9770 9109 57 1633 -436 C ATOM 650 CG2 THR A 83 7.554 16.847 32.243 1.00 77.62 C ANISOU 650 CG2 THR A 83 11270 9764 8459 395 1430 -690 C ATOM 651 OG1 THR A 83 8.243 18.845 33.406 1.00108.32 O ANISOU 651 OG1 THR A 83 15201 13400 12556 -57 1822 -239 O ATOM 652 N ASP A 84 4.989 18.599 30.983 1.00 89.23 N ANISOU 652 N ASP A 84 12673 11243 9989 233 1905 -69 N ATOM 653 CA ASP A 84 4.822 19.224 29.680 1.00 82.74 C ANISOU 653 CA ASP A 84 11563 10872 9001 326 2053 145 C ATOM 654 C ASP A 84 3.606 20.141 29.617 1.00 75.11 C ANISOU 654 C ASP A 84 10666 9673 8199 157 2242 445 C ATOM 655 O ASP A 84 3.292 20.660 28.541 1.00 76.45 O ANISOU 655 O ASP A 84 10615 10175 8257 213 2347 659 O ATOM 656 CB ASP A 84 4.724 18.150 28.594 1.00 90.84 C ANISOU 656 CB ASP A 84 12431 12304 9780 673 1852 -137 C ATOM 657 CG ASP A 84 3.593 17.172 28.842 1.00 88.47 C ANISOU 657 CG ASP A 84 12375 11634 9604 752 1643 -355 C ATOM 658 OD1 ASP A 84 3.444 16.712 29.994 1.00 92.57 O ANISOU 658 OD1 ASP A 84 13170 11677 10326 616 1522 -455 O ATOM 659 OD2 ASP A 84 2.855 16.859 27.885 1.00 78.67 O1- ANISOU 659 OD2 ASP A 84 11035 10599 8257 940 1586 -406 O1- ATOM 660 N LEU A 85 2.919 20.349 30.739 1.00 70.60 N ANISOU 660 N LEU A 85 10373 8576 7875 -40 2276 460 N ATOM 661 CA LEU A 85 1.751 21.217 30.781 1.00 75.54 C ANISOU 661 CA LEU A 85 11062 8962 8677 -184 2435 689 C ATOM 662 C LEU A 85 1.712 21.923 32.128 1.00 83.90 C ANISOU 662 C LEU A 85 12305 9586 9985 -427 2518 733 C ATOM 663 O LEU A 85 2.300 21.463 33.110 1.00 69.40 O ANISOU 663 O LEU A 85 10614 7588 8168 -480 2431 555 O ATOM 664 CB LEU A 85 0.455 20.433 30.547 1.00 70.74 C ANISOU 664 CB LEU A 85 10580 8237 8059 -78 2344 568 C ATOM 665 CG LEU A 85 0.193 19.965 29.114 1.00 73.06 C ANISOU 665 CG LEU A 85 10675 8944 8139 172 2276 542 C ATOM 666 CD1 LEU A 85 -0.665 18.712 29.111 1.00 67.46 C ANISOU 666 CD1 LEU A 85 10119 8086 7428 317 2053 286 C ATOM 667 CD2 LEU A 85 -0.454 21.072 28.299 1.00 73.52 C ANISOU 667 CD2 LEU A 85 10575 9131 8228 112 2471 874 C ATOM 668 N GLN A 86 1.006 23.049 32.164 1.00 71.69 N ANISOU 668 N GLN A 86 10326 6826 10086 -1141 -92 -160 N ATOM 669 CA GLN A 86 0.910 23.864 33.366 1.00 78.04 C ANISOU 669 CA GLN A 86 11399 7408 10844 -1172 -415 -445 C ATOM 670 C GLN A 86 -0.356 24.705 33.275 1.00 74.25 C ANISOU 670 C GLN A 86 10994 6966 10251 -1177 -158 -596 C ATOM 671 O GLN A 86 -0.865 24.944 32.173 1.00 77.84 O ANISOU 671 O GLN A 86 11186 7542 10846 -1163 162 -442 O ATOM 672 CB GLN A 86 2.153 24.754 33.535 1.00 77.83 C ANISOU 672 CB GLN A 86 11079 7085 11408 -1215 -860 -418 C ATOM 673 CG GLN A 86 2.562 25.505 32.283 1.00 81.83 C ANISOU 673 CG GLN A 86 11043 7551 12498 -1269 -690 -135 C ATOM 674 CD GLN A 86 3.601 26.570 32.566 1.00 94.47 C ANISOU 674 CD GLN A 86 12361 8803 14729 -1359 -1111 -147 C ATOM 675 NE2 GLN A 86 4.848 26.146 32.737 1.00104.38 N ANISOU 675 NE2 GLN A 86 13395 9963 16304 -1372 -1412 -79 N ATOM 676 OE1 GLN A 86 3.289 27.757 32.635 1.00108.54 O ANISOU 676 OE1 GLN A 86 14111 10386 16743 -1412 -1186 -233 O ATOM 677 N PRO A 87 -0.894 25.155 34.411 1.00 75.80 N ANISOU 677 N PRO A 87 11566 7058 10175 -1164 -299 -910 N ATOM 678 CA PRO A 87 -2.150 25.917 34.382 1.00 77.17 C ANISOU 678 CA PRO A 87 11805 7281 10235 -1139 -47 -1096 C ATOM 679 C PRO A 87 -2.042 27.165 33.518 1.00 80.11 C ANISOU 679 C PRO A 87 11788 7508 11142 -1144 -81 -990 C ATOM 680 O PRO A 87 -1.049 27.894 33.563 1.00 71.68 O ANISOU 680 O PRO A 87 10535 6179 10522 -1189 -431 -923 O ATOM 681 CB PRO A 87 -2.383 26.270 35.855 1.00 72.40 C ANISOU 681 CB PRO A 87 11671 6533 9306 -1097 -286 -1450 C ATOM 682 CG PRO A 87 -1.656 25.216 36.613 1.00 78.48 C ANISOU 682 CG PRO A 87 12751 7289 9780 -1095 -501 -1432 C ATOM 683 CD PRO A 87 -0.446 24.887 35.790 1.00 79.48 C ANISOU 683 CD PRO A 87 12466 7375 10357 -1135 -677 -1126 C ATOM 684 N GLY A 88 -3.089 27.407 32.731 1.00 86.65 N ANISOU 684 N GLY A 88 12499 8485 11937 -1097 273 -979 N ATOM 685 CA GLY A 88 -3.132 28.512 31.800 1.00 67.87 C ANISOU 685 CA GLY A 88 9816 5977 9996 -1075 289 -849 C ATOM 686 C GLY A 88 -2.893 28.125 30.358 1.00 80.26 C ANISOU 686 C GLY A 88 11066 7680 11747 -1056 544 -479 C ATOM 687 O GLY A 88 -3.170 28.934 29.461 1.00 79.37 O ANISOU 687 O GLY A 88 10772 7498 11889 -1004 644 -355 O ATOM 688 N ASP A 89 -2.397 26.915 30.110 1.00 64.22 N ANISOU 688 N ASP A 89 9004 5828 9567 -1071 645 -305 N ATOM 689 CA ASP A 89 -2.106 26.480 28.753 1.00 63.59 C ANISOU 689 CA ASP A 89 8658 5886 9617 -1016 888 34 C ATOM 690 C ASP A 89 -3.393 26.294 27.959 1.00 67.98 C ANISOU 690 C ASP A 89 9245 6649 9935 -893 1211 -10 C ATOM 691 O ASP A 89 -4.353 25.687 28.443 1.00 77.55 O ANISOU 691 O ASP A 89 10662 8021 10783 -881 1331 -253 O ATOM 692 CB ASP A 89 -1.314 25.173 28.777 1.00 74.53 C ANISOU 692 CB ASP A 89 10038 7410 10872 -1028 886 173 C ATOM 693 CG ASP A 89 0.146 25.379 29.130 1.00 83.59 C ANISOU 693 CG ASP A 89 11004 8353 12403 -1111 573 296 C ATOM 694 OD1 ASP A 89 0.597 26.543 29.150 1.00 77.07 O ANISOU 694 OD1 ASP A 89 10002 7274 12006 -1178 399 333 O ATOM 695 OD2 ASP A 89 0.842 24.374 29.386 1.00 88.83 O1- ANISOU 695 OD2 ASP A 89 11689 9088 12972 -1106 480 344 O1- ATOM 696 N HIS A 90 -3.413 26.830 26.741 1.00 67.08 N ANISOU 696 N HIS A 90 8933 6514 10040 -798 1350 223 N ATOM 697 CA HIS A 90 -4.482 26.540 25.797 1.00 67.04 C ANISOU 697 CA HIS A 90 8939 6700 9832 -636 1604 211 C ATOM 698 C HIS A 90 -4.259 25.150 25.219 1.00 65.30 C ANISOU 698 C HIS A 90 8705 6720 9386 -579 1773 362 C ATOM 699 O HIS A 90 -3.190 24.863 24.674 1.00 71.63 O ANISOU 699 O HIS A 90 9365 7519 10333 -567 1797 659 O ATOM 700 CB HIS A 90 -4.513 27.579 24.678 1.00 64.81 C ANISOU 700 CB HIS A 90 8529 6284 9814 -516 1661 428 C ATOM 701 CG HIS A 90 -4.917 28.948 25.128 1.00 76.17 C ANISOU 701 CG HIS A 90 10005 7470 11464 -535 1487 257 C ATOM 702 CD2 HIS A 90 -5.634 29.913 24.506 1.00 79.76 C ANISOU 702 CD2 HIS A 90 10474 7809 12024 -395 1495 237 C ATOM 703 ND1 HIS A 90 -4.576 29.460 26.361 1.00 83.41 N ANISOU 703 ND1 HIS A 90 10986 8202 12504 -685 1235 59 N ATOM 704 CE1 HIS A 90 -5.065 30.681 26.479 1.00 72.05 C ANISOU 704 CE1 HIS A 90 9585 6545 11245 -642 1106 -80 C ATOM 705 NE2 HIS A 90 -5.712 30.980 25.367 1.00 64.71 N ANISOU 705 NE2 HIS A 90 8622 5650 10316 -470 1261 29 N ATOM 706 N VAL A 91 -5.260 24.282 25.347 1.00 61.28 N ANISOU 706 N VAL A 91 8329 6405 8550 -544 1896 147 N ATOM 707 CA VAL A 91 -5.082 22.870 25.035 1.00 72.24 C ANISOU 707 CA VAL A 91 9755 7983 9709 -514 2002 231 C ATOM 708 C VAL A 91 -6.279 22.331 24.268 1.00 66.44 C ANISOU 708 C VAL A 91 9039 7421 8784 -375 2173 111 C ATOM 709 O VAL A 91 -7.418 22.771 24.451 1.00 63.78 O ANISOU 709 O VAL A 91 8721 7091 8423 -361 2210 -149 O ATOM 710 CB VAL A 91 -4.852 22.034 26.312 1.00 71.74 C ANISOU 710 CB VAL A 91 9890 7932 9437 -680 1911 83 C ATOM 711 CG1 VAL A 91 -3.553 22.440 26.991 1.00 57.54 C ANISOU 711 CG1 VAL A 91 8063 5954 7847 -778 1665 193 C ATOM 712 CG2 VAL A 91 -6.028 22.179 27.265 1.00 60.69 C ANISOU 712 CG2 VAL A 91 8673 6542 7845 -769 1964 -266 C ATOM 713 N LEU A 92 -6.001 21.358 23.402 1.00 64.53 N ANISOU 713 N LEU A 92 8777 7312 8429 -254 2257 278 N ATOM 714 CA LEU A 92 -7.023 20.589 22.712 1.00 72.12 C ANISOU 714 CA LEU A 92 9770 8424 9209 -124 2359 145 C ATOM 715 C LEU A 92 -7.012 19.166 23.244 1.00 70.57 C ANISOU 715 C LEU A 92 9702 8318 8792 -236 2382 68 C ATOM 716 O LEU A 92 -5.955 18.515 23.227 1.00 75.12 O ANISOU 716 O LEU A 92 10309 8905 9329 -234 2339 268 O ATOM 717 CB LEU A 92 -6.787 20.590 21.200 1.00 60.49 C ANISOU 717 CB LEU A 92 8234 7007 7744 155 2411 380 C ATOM 718 CG LEU A 92 -6.745 21.939 20.481 1.00 68.51 C ANISOU 718 CG LEU A 92 9180 7904 8945 298 2411 528 C ATOM 719 CD1 LEU A 92 -6.532 21.739 18.988 1.00 63.28 C ANISOU 719 CD1 LEU A 92 8545 7312 8185 603 2501 770 C ATOM 720 CD2 LEU A 92 -8.014 22.729 20.744 1.00 70.46 C ANISOU 720 CD2 LEU A 92 9427 8094 9250 306 2350 223 C ATOM 721 N PRO A 93 -8.129 18.659 23.759 1.00 68.44 N ANISOU 721 N PRO A 93 9506 8097 8400 -343 2454 -214 N ATOM 722 CA PRO A 93 -8.202 17.228 24.072 1.00 56.91 C ANISOU 722 CA PRO A 93 8190 6694 6738 -440 2494 -256 C ATOM 723 C PRO A 93 -8.371 16.413 22.801 1.00 68.04 C ANISOU 723 C PRO A 93 9551 8198 8102 -227 2494 -194 C ATOM 724 O PRO A 93 -9.158 16.760 21.918 1.00 78.68 O ANISOU 724 O PRO A 93 10783 9588 9522 -54 2500 -291 O ATOM 725 CB PRO A 93 -9.437 17.118 24.978 1.00 68.34 C ANISOU 725 CB PRO A 93 9696 8143 8127 -636 2630 -572 C ATOM 726 CG PRO A 93 -9.726 18.522 25.426 1.00 53.21 C ANISOU 726 CG PRO A 93 7701 6166 6351 -650 2625 -692 C ATOM 727 CD PRO A 93 -9.274 19.402 24.307 1.00 65.27 C ANISOU 727 CD PRO A 93 9067 7672 8062 -419 2514 -509 C ATOM 728 N ILE A 94 -7.613 15.325 22.711 1.00 72.12 N ANISOU 728 N ILE A 94 10180 8734 8489 -207 2450 -49 N ATOM 729 CA ILE A 94 -7.659 14.423 21.568 1.00 66.95 C ANISOU 729 CA ILE A 94 9529 8156 7753 18 2421 -1 C ATOM 730 C ILE A 94 -8.294 13.114 22.011 1.00 66.24 C ANISOU 730 C ILE A 94 9583 8045 7539 -136 2429 -176 C ATOM 731 O ILE A 94 -8.076 12.656 23.139 1.00 69.63 O ANISOU 731 O ILE A 94 10177 8403 7878 -376 2449 -187 O ATOM 732 CB ILE A 94 -6.256 14.182 20.975 1.00 57.99 C ANISOU 732 CB ILE A 94 8393 7052 6588 208 2373 301 C ATOM 733 CG1 ILE A 94 -5.384 15.434 21.110 1.00 65.05 C ANISOU 733 CG1 ILE A 94 9151 7901 7665 202 2389 500 C ATOM 734 CG2 ILE A 94 -6.363 13.765 19.516 1.00 54.67 C ANISOU 734 CG2 ILE A 94 7961 6724 6085 546 2370 357 C ATOM 735 CD1 ILE A 94 -5.827 16.597 20.250 1.00 59.71 C ANISOU 735 CD1 ILE A 94 8353 7229 7105 365 2451 536 C ATOM 736 N PHE A 95 -9.089 12.515 21.120 1.00 66.27 N ANISOU 736 N PHE A 95 9550 8086 7542 7 2397 -312 N ATOM 737 CA PHE A 95 -9.732 11.243 21.434 1.00 72.00 C ANISOU 737 CA PHE A 95 10389 8754 8213 -151 2398 -476 C ATOM 738 C PHE A 95 -8.718 10.114 21.550 1.00 76.68 C ANISOU 738 C PHE A 95 11196 9302 8635 -130 2307 -299 C ATOM 739 O PHE A 95 -8.954 9.141 22.275 1.00 70.37 O ANISOU 739 O PHE A 95 10576 8399 7763 -352 2324 -364 O ATOM 740 CB PHE A 95 -10.777 10.907 20.370 1.00 58.31 C ANISOU 740 CB PHE A 95 8537 7043 6576 26 2315 -689 C ATOM 741 CG PHE A 95 -10.188 10.533 19.039 1.00 64.88 C ANISOU 741 CG PHE A 95 9422 7931 7299 416 2152 -561 C ATOM 742 CD1 PHE A 95 -9.731 11.508 18.168 1.00 61.97 C ANISOU 742 CD1 PHE A 95 8989 7647 6908 716 2138 -407 C ATOM 743 CD2 PHE A 95 -10.086 9.203 18.662 1.00 70.49 C ANISOU 743 CD2 PHE A 95 10277 8593 7912 492 2027 -590 C ATOM 744 CE1 PHE A 95 -9.186 11.164 16.944 1.00 67.86 C ANISOU 744 CE1 PHE A 95 9826 8454 7504 1098 2043 -278 C ATOM 745 CE2 PHE A 95 -9.542 8.853 17.441 1.00 73.58 C ANISOU 745 CE2 PHE A 95 10748 9044 8164 891 1889 -494 C ATOM 746 CZ PHE A 95 -9.092 9.834 16.581 1.00 72.83 C ANISOU 746 CZ PHE A 95 10599 9059 8014 1201 1917 -335 C ATOM 747 N THR A 96 -7.600 10.217 20.836 1.00 72.12 N ANISOU 747 N THR A 96 10609 8791 8004 142 2224 -74 N ATOM 748 CA THR A 96 -6.503 9.266 20.923 1.00 71.82 C ANISOU 748 CA THR A 96 10731 8722 7836 214 2122 89 C ATOM 749 C THR A 96 -5.245 10.009 21.352 1.00 66.80 C ANISOU 749 C THR A 96 10030 8105 7248 222 2123 314 C ATOM 750 O THR A 96 -5.075 11.194 21.051 1.00 77.41 O ANISOU 750 O THR A 96 11185 9505 8721 288 2196 398 O ATOM 751 CB THR A 96 -6.275 8.548 19.586 1.00 71.49 C ANISOU 751 CB THR A 96 10706 8745 7712 578 2025 122 C ATOM 752 CG2 THR A 96 -6.064 9.554 18.464 1.00 58.89 C ANISOU 752 CG2 THR A 96 8939 7281 6154 885 2090 236 C ATOM 753 OG1 THR A 96 -5.127 7.696 19.684 1.00 72.13 O ANISOU 753 OG1 THR A 96 10915 8803 7687 680 1928 274 O ATOM 754 N GLY A 97 -4.361 9.310 22.064 1.00 67.67 N ANISOU 754 N GLY A 97 10294 8138 7279 154 2014 403 N ATOM 755 CA GLY A 97 -3.256 9.939 22.749 1.00 62.17 C ANISOU 755 CA GLY A 97 9536 7410 6673 100 1954 553 C ATOM 756 C GLY A 97 -1.888 9.543 22.220 1.00 66.55 C ANISOU 756 C GLY A 97 10000 8010 7274 354 1858 745 C ATOM 757 O GLY A 97 -1.750 8.775 21.263 1.00 70.00 O ANISOU 757 O GLY A 97 10447 8519 7630 609 1857 775 O ATOM 758 N GLU A 98 -0.870 10.099 22.877 1.00 64.71 N ANISOU 758 N GLU A 98 9664 7727 7195 293 1766 854 N ATOM 759 CA GLU A 98 0.534 9.863 22.540 1.00 54.94 C ANISOU 759 CA GLU A 98 8256 6523 6096 504 1678 1024 C ATOM 760 C GLU A 98 1.289 9.740 23.859 1.00 61.71 C ANISOU 760 C GLU A 98 9224 7224 7000 345 1414 999 C ATOM 761 O GLU A 98 1.544 10.745 24.530 1.00 66.75 O ANISOU 761 O GLU A 98 9753 7791 7817 188 1358 1004 O ATOM 762 CB GLU A 98 1.089 10.990 21.675 1.00 58.77 C ANISOU 762 CB GLU A 98 8371 7112 6846 639 1862 1210 C ATOM 763 CG GLU A 98 2.568 10.872 21.340 1.00 57.26 C ANISOU 763 CG GLU A 98 7914 6961 6880 831 1839 1391 C ATOM 764 CD GLU A 98 3.030 11.951 20.378 1.00 70.99 C ANISOU 764 CD GLU A 98 9305 8794 8876 950 2111 1612 C ATOM 765 OE1 GLU A 98 2.164 12.650 19.810 1.00 67.92 O ANISOU 765 OE1 GLU A 98 8942 8443 8419 946 2293 1627 O ATOM 766 OE2 GLU A 98 4.255 12.103 20.189 1.00 75.34 O1- ANISOU 766 OE2 GLU A 98 9552 9363 9710 1048 2147 1773 O1- ATOM 767 N CYS A 99 1.634 8.505 24.233 1.00 59.88 N ANISOU 767 N CYS A 99 9240 6911 6599 406 1215 957 N ATOM 768 CA CYS A 99 2.280 8.275 25.522 1.00 66.95 C ANISOU 768 CA CYS A 99 10337 7629 7472 291 910 914 C ATOM 769 C CYS A 99 3.699 8.825 25.551 1.00 78.43 C ANISOU 769 C CYS A 99 11436 9080 9284 412 746 1016 C ATOM 770 O CYS A 99 4.181 9.242 26.611 1.00 68.13 O ANISOU 770 O CYS A 99 10189 7627 8070 287 490 964 O ATOM 771 CB CYS A 99 2.289 6.782 25.849 1.00 61.03 C ANISOU 771 CB CYS A 99 9979 6763 6446 351 721 858 C ATOM 772 SG CYS A 99 3.715 5.877 25.192 1.00 74.56 S ANISOU 772 SG CYS A 99 11516 8513 8301 732 515 942 S ATOM 773 N GLY A 100 4.382 8.830 24.409 1.00 70.16 N ANISOU 773 N GLY A 100 10022 8185 8452 663 889 1151 N ATOM 774 CA GLY A 100 5.727 9.357 24.337 1.00 72.77 C ANISOU 774 CA GLY A 100 9928 8520 9201 765 799 1257 C ATOM 775 C GLY A 100 6.821 8.420 24.791 1.00 83.12 C ANISOU 775 C GLY A 100 11259 9742 10581 933 452 1212 C ATOM 776 O GLY A 100 7.980 8.843 24.867 1.00 91.45 O ANISOU 776 O GLY A 100 11922 10776 12051 1003 327 1263 O ATOM 777 N GLU A 101 6.500 7.163 25.103 1.00 79.90 N ANISOU 777 N GLU A 101 11284 9257 9815 1001 276 1112 N ATOM 778 CA GLU A 101 7.533 6.204 25.478 1.00 96.07 C ANISOU 778 CA GLU A 101 13387 11204 11913 1209 -87 1060 C ATOM 779 C GLU A 101 7.100 4.766 25.219 1.00 80.80 C ANISOU 779 C GLU A 101 11861 9237 9601 1364 -141 1003 C ATOM 780 O GLU A 101 7.502 3.852 25.946 1.00 88.56 O ANISOU 780 O GLU A 101 13163 10035 10450 1437 -512 920 O ATOM 781 CB GLU A 101 7.931 6.381 26.945 1.00 93.16 C ANISOU 781 CB GLU A 101 13242 10591 11565 1054 -528 950 C ATOM 782 CG GLU A 101 6.771 6.522 27.912 1.00 80.87 C ANISOU 782 CG GLU A 101 12214 8895 9617 752 -539 867 C ATOM 783 CD GLU A 101 7.065 7.518 29.017 1.00108.12 C ANISOU 783 CD GLU A 101 15673 12197 13211 573 -789 793 C ATOM 784 OE1 GLU A 101 7.605 8.602 28.712 1.00114.21 O ANISOU 784 OE1 GLU A 101 15942 13034 14419 553 -731 842 O ATOM 785 OE2 GLU A 101 6.763 7.213 30.190 1.00103.18 O1- ANISOU 785 OE2 GLU A 101 15580 11370 12254 460 -1045 689 O1- ATOM 786 N CYS A 102 6.287 4.553 24.191 1.00 84.60 N ANISOU 786 N CYS A 102 12359 9869 9917 1426 188 1037 N ATOM 787 CA CYS A 102 5.980 3.222 23.691 1.00 70.00 C ANISOU 787 CA CYS A 102 10807 7997 7794 1624 142 978 C ATOM 788 C CYS A 102 6.659 3.035 22.337 1.00 79.94 C ANISOU 788 C CYS A 102 11695 9475 9203 2017 331 1046 C ATOM 789 O CYS A 102 7.354 3.924 21.837 1.00 87.17 O ANISOU 789 O CYS A 102 12134 10553 10434 2104 533 1163 O ATOM 790 CB CYS A 102 4.466 3.004 23.615 1.00 67.15 C ANISOU 790 CB CYS A 102 10792 7598 7124 1407 315 916 C ATOM 791 SG CYS A 102 3.665 3.597 22.106 1.00 78.03 S ANISOU 791 SG CYS A 102 11897 9234 8515 1516 745 959 S ATOM 792 N ARG A 103 6.461 1.857 21.741 1.00 92.47 N ANISOU 792 N ARG A 103 13521 11051 10561 2260 277 974 N ATOM 793 CA ARG A 103 7.170 1.540 20.504 1.00 83.62 C ANISOU 793 CA ARG A 103 12116 10132 9523 2696 436 1013 C ATOM 794 C ARG A 103 6.687 2.403 19.344 1.00 84.12 C ANISOU 794 C ARG A 103 11936 10436 9591 2759 884 1121 C ATOM 795 O ARG A 103 7.495 2.862 18.528 1.00 77.02 O ANISOU 795 O ARG A 103 10637 9736 8890 3011 1142 1245 O ATOM 796 CB ARG A 103 7.018 0.056 20.171 1.00 79.85 C ANISOU 796 CB ARG A 103 12009 9552 8776 2959 224 878 C ATOM 797 CG ARG A 103 8.094 -0.469 19.232 1.00 89.98 C ANISOU 797 CG ARG A 103 13032 10995 10160 3466 266 875 C ATOM 798 CD ARG A 103 8.412 -1.932 19.501 1.00 98.08 C ANISOU 798 CD ARG A 103 14412 11818 11038 3697 -142 720 C ATOM 799 NE ARG A 103 8.762 -2.652 18.282 1.00 92.71 N ANISOU 799 NE ARG A 103 13678 11285 10264 4198 -44 654 N ATOM 800 CZ ARG A 103 9.955 -2.612 17.703 1.00 99.66 C ANISOU 800 CZ ARG A 103 14141 12360 11365 4589 80 682 C ATOM 801 NH1 ARG A 103 10.946 -1.896 18.208 1.00110.95 N1+ ANISOU 801 NH1 ARG A 103 15122 13849 13185 4523 99 771 N1+ ATOM 802 NH2 ARG A 103 10.158 -3.310 16.589 1.00 97.16 N ANISOU 802 NH2 ARG A 103 13849 12175 10892 5066 188 604 N ATOM 803 N HIS A 104 5.376 2.638 19.253 1.00 86.67 N ANISOU 803 N HIS A 104 12495 10732 9703 2542 989 1077 N ATOM 804 CA HIS A 104 4.854 3.460 18.166 1.00 88.73 C ANISOU 804 CA HIS A 104 12585 11190 9937 2628 1356 1164 C ATOM 805 C HIS A 104 5.177 4.935 18.368 1.00 87.50 C ANISOU 805 C HIS A 104 12061 11108 10076 2428 1575 1334 C ATOM 806 O HIS A 104 5.384 5.661 17.389 1.00 86.04 O ANISOU 806 O HIS A 104 11623 11099 9967 2601 1905 1486 O ATOM 807 CB HIS A 104 3.345 3.266 18.033 1.00 69.11 C ANISOU 807 CB HIS A 104 10426 8634 7197 2470 1347 1027 C ATOM 808 CG HIS A 104 2.943 1.868 17.682 1.00 79.08 C ANISOU 808 CG HIS A 104 12033 9799 8213 2662 1141 858 C ATOM 809 CD2 HIS A 104 2.874 0.744 18.435 1.00 64.51 C ANISOU 809 CD2 HIS A 104 10511 7728 6274 2569 828 738 C ATOM 810 ND1 HIS A 104 2.539 1.505 16.415 1.00 71.09 N ANISOU 810 ND1 HIS A 104 11097 8895 7018 3002 1229 793 N ATOM 811 CE1 HIS A 104 2.244 0.218 16.401 1.00 69.62 C ANISOU 811 CE1 HIS A 104 11234 8549 6670 3101 961 621 C ATOM 812 NE2 HIS A 104 2.438 -0.267 17.614 1.00 73.56 N ANISOU 812 NE2 HIS A 104 11887 8837 7225 2830 729 600 N ATOM 813 N CYS A 105 5.217 5.397 19.621 1.00 82.57 N ANISOU 813 N CYS A 105 11440 10331 9604 2076 1392 1312 N ATOM 814 CA CYS A 105 5.542 6.797 19.877 1.00 81.26 C ANISOU 814 CA CYS A 105 10934 10189 9751 1878 1542 1447 C ATOM 815 C CYS A 105 6.991 7.100 19.518 1.00 80.84 C ANISOU 815 C CYS A 105 10419 10230 10068 2078 1640 1601 C ATOM 816 O CYS A 105 7.290 8.164 18.965 1.00 89.41 O ANISOU 816 O CYS A 105 11162 11410 11397 2070 1944 1782 O ATOM 817 CB CYS A 105 5.263 7.143 21.339 1.00 77.17 C ANISOU 817 CB CYS A 105 10577 9470 9276 1497 1278 1348 C ATOM 818 SG CYS A 105 3.510 7.352 21.724 1.00 73.62 S ANISOU 818 SG CYS A 105 10501 8948 8524 1191 1337 1211 S ATOM 819 N HIS A 106 7.905 6.177 19.825 1.00 88.27 N ANISOU 819 N HIS A 106 11332 11126 11080 2258 1391 1533 N ATOM 820 CA HIS A 106 9.285 6.331 19.385 1.00 94.42 C ANISOU 820 CA HIS A 106 11617 12014 12246 2491 1510 1651 C ATOM 821 C HIS A 106 9.423 6.172 17.877 1.00 96.80 C ANISOU 821 C HIS A 106 11784 12557 12438 2867 1941 1778 C ATOM 822 O HIS A 106 10.425 6.616 17.308 1.00 98.37 O ANISOU 822 O HIS A 106 11519 12885 12972 3027 2224 1940 O ATOM 823 CB HIS A 106 10.185 5.327 20.105 1.00 83.47 C ANISOU 823 CB HIS A 106 10249 10508 10959 2630 1087 1505 C ATOM 824 CG HIS A 106 10.245 5.527 21.586 1.00 96.59 C ANISOU 824 CG HIS A 106 12051 11922 12728 2318 646 1392 C ATOM 825 CD2 HIS A 106 10.288 4.638 22.607 1.00102.36 C ANISOU 825 CD2 HIS A 106 13163 12441 13287 2295 172 1223 C ATOM 826 ND1 HIS A 106 10.270 6.777 22.167 1.00 99.12 N ANISOU 826 ND1 HIS A 106 12158 12169 13334 2006 655 1451 N ATOM 827 CE1 HIS A 106 10.325 6.649 23.481 1.00 89.16 C ANISOU 827 CE1 HIS A 106 11145 10679 12054 1822 199 1306 C ATOM 828 NE2 HIS A 106 10.336 5.361 23.774 1.00 93.33 N ANISOU 828 NE2 HIS A 106 12050 11118 12292 1991 -89 1179 N ATOM 829 N SER A 107 8.444 5.551 17.225 1.00101.05 N ANISOU 829 N SER A 107 9491 12266 16638 1020 1839 -1549 N ATOM 830 CA SER A 107 8.437 5.455 15.774 1.00102.01 C ANISOU 830 CA SER A 107 10145 12179 16437 473 2368 -1832 C ATOM 831 C SER A 107 7.996 6.776 15.157 1.00 96.43 C ANISOU 831 C SER A 107 9970 11533 15137 -148 2432 -1714 C ATOM 832 O SER A 107 7.140 7.479 15.702 1.00 99.52 O ANISOU 832 O SER A 107 10587 11992 15235 -156 1955 -1256 O ATOM 833 CB SER A 107 7.508 4.330 15.318 1.00 90.34 C ANISOU 833 CB SER A 107 9144 10343 14840 570 2282 -1652 C ATOM 834 OG SER A 107 6.867 4.664 14.098 1.00 89.46 O ANISOU 834 OG SER A 107 9773 10059 14158 -12 2507 -1653 O ATOM 835 N GLU A 108 8.590 7.112 14.013 1.00 99.50 N ANISOU 835 N GLU A 108 10569 11893 15344 -656 3038 -2127 N ATOM 836 CA GLU A 108 8.217 8.328 13.302 1.00 98.24 C ANISOU 836 CA GLU A 108 10968 11760 14599 -1255 3184 -2046 C ATOM 837 C GLU A 108 7.005 8.128 12.401 1.00 99.26 C ANISOU 837 C GLU A 108 11940 11621 14153 -1535 3122 -1791 C ATOM 838 O GLU A 108 6.360 9.111 12.021 1.00 94.77 O ANISOU 838 O GLU A 108 11904 11072 13032 -1923 3057 -1561 O ATOM 839 CB GLU A 108 9.406 8.834 12.476 1.00110.89 C ANISOU 839 CB GLU A 108 12433 13452 16248 -1679 3889 -2599 C ATOM 840 CG GLU A 108 9.224 10.226 11.886 1.00132.51 C ANISOU 840 CG GLU A 108 15649 16253 18446 -2269 4084 -2543 C ATOM 841 CD GLU A 108 10.535 10.855 11.460 1.00139.26 C ANISOU 841 CD GLU A 108 16172 17260 19481 -2601 4713 -3067 C ATOM 842 OE1 GLU A 108 11.242 10.252 10.626 1.00136.47 O ANISOU 842 OE1 GLU A 108 15768 16807 19278 -2724 5259 -3512 O ATOM 843 OE2 GLU A 108 10.858 11.955 11.958 1.00157.60 O1- ANISOU 843 OE2 GLU A 108 18284 19798 21799 -2746 4670 -3042 O1- ATOM 844 N GLU A 109 6.667 6.882 12.070 1.00 96.02 N ANISOU 844 N GLU A 109 11662 10967 13856 -1334 3134 -1829 N ATOM 845 CA GLU A 109 5.604 6.615 11.109 1.00 87.32 C ANISOU 845 CA GLU A 109 11331 9618 12230 -1618 3134 -1678 C ATOM 846 C GLU A 109 4.248 6.394 11.767 1.00 79.84 C ANISOU 846 C GLU A 109 10648 8589 11098 -1364 2460 -1112 C ATOM 847 O GLU A 109 3.222 6.813 11.220 1.00 93.16 O ANISOU 847 O GLU A 109 12988 10202 12205 -1666 2310 -853 O ATOM 848 CB GLU A 109 5.965 5.394 10.260 1.00 89.53 C ANISOU 848 CB GLU A 109 11658 9659 12700 -1601 3564 -2072 C ATOM 849 CG GLU A 109 5.876 5.634 8.766 1.00 98.33 C ANISOU 849 CG GLU A 109 13408 10647 13307 -2160 4062 -2325 C ATOM 850 CD GLU A 109 7.015 6.489 8.249 1.00122.71 C ANISOU 850 CD GLU A 109 16339 13897 16388 -2520 4633 -2724 C ATOM 851 OE1 GLU A 109 6.742 7.562 7.673 1.00132.62 O ANISOU 851 OE1 GLU A 109 18064 15209 17115 -2967 4762 -2648 O ATOM 852 OE2 GLU A 109 8.186 6.091 8.425 1.00127.36 O1- ANISOU 852 OE2 GLU A 109 16335 14556 17500 -2351 4962 -3117 O1- ATOM 853 N SER A 110 4.216 5.743 12.924 1.00 77.93 N ANISOU 853 N SER A 110 9918 8364 11329 -804 2058 -915 N ATOM 854 CA SER A 110 2.969 5.317 13.541 1.00 75.59 C ANISOU 854 CA SER A 110 9837 7949 10934 -520 1463 -410 C ATOM 855 C SER A 110 2.505 6.322 14.586 1.00 77.96 C ANISOU 855 C SER A 110 10038 8477 11105 -396 928 48 C ATOM 856 O SER A 110 3.316 6.897 15.318 1.00 81.16 O ANISOU 856 O SER A 110 9919 9125 11794 -246 912 -24 O ATOM 857 CB SER A 110 3.126 3.940 14.188 1.00 81.88 C ANISOU 857 CB SER A 110 10210 8589 12311 49 1346 -432 C ATOM 858 OG SER A 110 1.902 3.500 14.753 1.00 73.45 O ANISOU 858 OG SER A 110 9369 7383 11157 305 805 50 O ATOM 859 N ASN A 111 1.188 6.525 14.648 1.00 70.16 N ANISOU 859 N ASN A 111 9553 7420 9685 -458 487 509 N ATOM 860 CA ASN A 111 0.551 7.301 15.704 1.00 88.30 C ANISOU 860 CA ASN A 111 11796 9895 11860 -273 -96 1011 C ATOM 861 C ASN A 111 -0.337 6.431 16.586 1.00 82.50 C ANISOU 861 C ASN A 111 10986 9030 11331 218 -630 1420 C ATOM 862 O ASN A 111 -1.218 6.946 17.281 1.00 80.08 O ANISOU 862 O ASN A 111 10815 8808 10803 330 -1153 1903 O ATOM 863 CB ASN A 111 -0.257 8.458 15.111 1.00 65.75 C ANISOU 863 CB ASN A 111 9594 7108 8282 -759 -182 1245 C ATOM 864 CG ASN A 111 -1.493 7.992 14.350 1.00 64.71 C ANISOU 864 CG ASN A 111 10132 6759 7694 -942 -307 1428 C ATOM 865 ND2 ASN A 111 -2.332 8.942 13.954 1.00 65.41 N ANISOU 865 ND2 ASN A 111 10791 6921 7141 -1281 -469 1694 N ATOM 866 OD1 ASN A 111 -1.693 6.799 14.128 1.00 63.31 O ANISOU 866 OD1 ASN A 111 9960 6357 7737 -774 -257 1324 O ATOM 867 N MET A 112 -0.128 5.115 16.559 1.00 75.99 N ANISOU 867 N MET A 112 9962 7988 10923 513 -492 1238 N ATOM 868 CA MET A 112 -1.005 4.174 17.248 1.00 84.64 C ANISOU 868 CA MET A 112 11055 8897 12207 942 -920 1597 C ATOM 869 C MET A 112 -0.352 3.792 18.573 1.00 70.37 C ANISOU 869 C MET A 112 8530 7193 11015 1575 -1128 1671 C ATOM 870 O MET A 112 0.261 2.735 18.725 1.00 68.60 O ANISOU 870 O MET A 112 7949 6834 11282 1920 -920 1432 O ATOM 871 CB MET A 112 -1.287 2.967 16.363 1.00 72.86 C ANISOU 871 CB MET A 112 9859 7073 10752 858 -639 1370 C ATOM 872 CG MET A 112 -2.493 3.194 15.480 1.00 75.42 C ANISOU 872 CG MET A 112 10922 7285 10449 417 -739 1535 C ATOM 873 SD MET A 112 -2.871 1.864 14.338 1.00103.63 S ANISOU 873 SD MET A 112 14885 10484 14005 251 -403 1230 S ATOM 874 CE MET A 112 -4.657 1.931 14.425 1.00 98.38 C ANISOU 874 CE MET A 112 14785 9736 12858 165 -972 1754 C ATOM 875 N CYS A 113 -0.501 4.688 19.546 1.00 75.38 N ANISOU 875 N CYS A 113 11370 8195 9075 1340 1388 -91 N ATOM 876 CA CYS A 113 0.108 4.503 20.856 1.00 72.12 C ANISOU 876 CA CYS A 113 10876 7778 8749 1125 1382 470 C ATOM 877 C CYS A 113 -0.430 3.249 21.531 1.00 80.53 C ANISOU 877 C CYS A 113 11739 8522 10336 998 1380 619 C ATOM 878 O CYS A 113 -1.644 3.027 21.581 1.00 83.18 O ANISOU 878 O CYS A 113 12048 8783 10772 914 1362 421 O ATOM 879 CB CYS A 113 -0.157 5.731 21.726 1.00 57.28 C ANISOU 879 CB CYS A 113 9190 6222 6351 928 1355 685 C ATOM 880 SG CYS A 113 0.544 5.639 23.379 1.00 68.24 S ANISOU 880 SG CYS A 113 10515 7662 7750 663 1319 1357 S ATOM 881 N ASP A 114 0.484 2.426 22.051 1.00 73.58 N ANISOU 881 N ASP A 114 10703 7461 9794 987 1405 994 N ATOM 882 CA ASP A 114 0.079 1.199 22.728 1.00 85.92 C ANISOU 882 CA ASP A 114 12081 8690 11876 875 1423 1189 C ATOM 883 C ASP A 114 -0.795 1.486 23.941 1.00 83.19 C ANISOU 883 C ASP A 114 11734 8468 11405 610 1407 1458 C ATOM 884 O ASP A 114 -1.648 0.666 24.300 1.00 81.21 O ANISOU 884 O ASP A 114 11353 7978 11524 500 1421 1476 O ATOM 885 CB ASP A 114 1.311 0.399 23.153 1.00 80.60 C ANISOU 885 CB ASP A 114 11259 7854 11512 938 1470 1609 C ATOM 886 CG ASP A 114 1.939 -0.360 22.004 1.00 83.16 C ANISOU 886 CG ASP A 114 11542 7915 12139 1234 1518 1346 C ATOM 887 OD1 ASP A 114 1.187 -0.908 21.172 1.00 91.50 O ANISOU 887 OD1 ASP A 114 12622 8708 13436 1325 1509 893 O ATOM 888 OD2 ASP A 114 3.186 -0.418 21.939 1.00 84.84 O1- ANISOU 888 OD2 ASP A 114 11698 8193 12343 1384 1562 1600 O1- ATOM 889 N LEU A 115 -0.607 2.640 24.577 1.00 75.94 N ANISOU 889 N LEU A 115 10971 7913 9969 508 1379 1672 N ATOM 890 CA LEU A 115 -1.279 2.958 25.831 1.00 75.99 C ANISOU 890 CA LEU A 115 11009 8065 9799 296 1374 1987 C ATOM 891 C LEU A 115 -2.499 3.854 25.656 1.00 75.07 C ANISOU 891 C LEU A 115 11061 8165 9299 270 1369 1695 C ATOM 892 O LEU A 115 -3.497 3.668 26.359 1.00 69.11 O ANISOU 892 O LEU A 115 10247 7410 8600 150 1395 1814 O ATOM 893 CB LEU A 115 -0.291 3.622 26.798 1.00 73.69 C ANISOU 893 CB LEU A 115 10810 8027 9161 194 1334 2448 C ATOM 894 CG LEU A 115 -0.866 4.443 27.956 1.00 76.56 C ANISOU 894 CG LEU A 115 11341 8652 9094 22 1310 2700 C ATOM 895 CD1 LEU A 115 -1.266 3.533 29.103 1.00 65.51 C ANISOU 895 CD1 LEU A 115 9756 7110 8024 -94 1354 3101 C ATOM 896 CD2 LEU A 115 0.123 5.498 28.429 1.00 75.46 C ANISOU 896 CD2 LEU A 115 11406 8807 8456 -55 1225 2939 C ATOM 897 N LEU A 116 -2.458 4.811 24.727 1.00 73.64 N ANISOU 897 N LEU A 116 11075 8176 8727 399 1350 1334 N ATOM 898 CA LEU A 116 -3.467 5.864 24.668 1.00 67.90 C ANISOU 898 CA LEU A 116 10554 7716 7529 401 1357 1125 C ATOM 899 C LEU A 116 -4.211 5.912 23.337 1.00 64.18 C ANISOU 899 C LEU A 116 10084 7229 7072 575 1362 565 C ATOM 900 O LEU A 116 -4.868 6.916 23.043 1.00 77.06 O ANISOU 900 O LEU A 116 11911 9116 8253 643 1376 348 O ATOM 901 CB LEU A 116 -2.826 7.221 24.956 1.00 66.55 C ANISOU 901 CB LEU A 116 10689 7848 6750 383 1334 1255 C ATOM 902 CG LEU A 116 -2.237 7.407 26.354 1.00 59.23 C ANISOU 902 CG LEU A 116 9819 7011 5674 194 1299 1786 C ATOM 903 CD1 LEU A 116 -1.664 8.800 26.511 1.00 66.33 C ANISOU 903 CD1 LEU A 116 11058 8183 5961 154 1249 1841 C ATOM 904 CD2 LEU A 116 -3.291 7.136 27.414 1.00 65.81 C ANISOU 904 CD2 LEU A 116 10605 7858 6543 85 1337 2007 C ATOM 905 N ARG A 117 -4.136 4.860 22.526 1.00 67.12 N ANISOU 905 N ARG A 117 10262 7309 7932 664 1347 321 N ATOM 906 CA ARG A 117 -4.912 4.854 21.296 1.00 71.20 C ANISOU 906 CA ARG A 117 10776 7820 8458 820 1325 -224 C ATOM 907 C ARG A 117 -6.403 4.752 21.619 1.00 69.60 C ANISOU 907 C ARG A 117 10476 7677 8294 703 1318 -302 C ATOM 908 O ARG A 117 -6.805 4.486 22.756 1.00 69.28 O ANISOU 908 O ARG A 117 10340 7620 8364 512 1344 71 O ATOM 909 CB ARG A 117 -4.469 3.717 20.375 1.00 71.14 C ANISOU 909 CB ARG A 117 10618 7461 8952 948 1297 -479 C ATOM 910 CG ARG A 117 -5.063 2.359 20.697 1.00 97.46 C ANISOU 910 CG ARG A 117 13708 10427 12896 799 1270 -437 C ATOM 911 CD ARG A 117 -4.793 1.378 19.566 1.00103.65 C ANISOU 911 CD ARG A 117 14426 10865 14092 966 1229 -820 C ATOM 912 NE ARG A 117 -3.376 1.307 19.230 1.00105.54 N ANISOU 912 NE ARG A 117 14730 11037 14331 1162 1276 -719 N ATOM 913 CZ ARG A 117 -2.609 0.246 19.436 1.00107.70 C ANISOU 913 CZ ARG A 117 14896 10967 15056 1188 1308 -508 C ATOM 914 NH1 ARG A 117 -3.093 -0.863 19.973 1.00 97.62 N1+ ANISOU 914 NH1 ARG A 117 13461 9340 14288 1018 1297 -382 N1+ ATOM 915 NH2 ARG A 117 -1.324 0.297 19.094 1.00 91.33 N ANISOU 915 NH2 ARG A 117 12870 8908 12924 1397 1362 -399 N ATOM 916 N ILE A 118 -7.226 4.968 20.588 1.00 75.49 N ANISOU 916 N ILE A 118 11230 8516 8936 833 1285 -778 N ATOM 917 CA ILE A 118 -8.661 5.139 20.786 1.00 74.69 C ANISOU 917 CA ILE A 118 11043 8585 8748 756 1280 -864 C ATOM 918 C ILE A 118 -9.248 3.946 21.531 1.00 70.85 C ANISOU 918 C ILE A 118 10264 7832 8824 515 1262 -631 C ATOM 919 O ILE A 118 -8.877 2.791 21.295 1.00 78.09 O ANISOU 919 O ILE A 118 11022 8365 10286 459 1215 -675 O ATOM 920 CB ILE A 118 -9.361 5.365 19.432 1.00 77.00 C ANISOU 920 CB ILE A 118 11342 8997 8918 944 1222 -1437 C ATOM 921 CG1 ILE A 118 -10.841 5.698 19.634 1.00 63.94 C ANISOU 921 CG1 ILE A 118 9591 7607 7097 887 1224 -1496 C ATOM 922 CG2 ILE A 118 -9.186 4.161 18.516 1.00 63.37 C ANISOU 922 CG2 ILE A 118 9447 6900 7730 974 1124 -1775 C ATOM 923 CD1 ILE A 118 -11.602 5.893 18.338 1.00 61.58 C ANISOU 923 CD1 ILE A 118 9264 7464 6671 1067 1150 -2045 C ATOM 924 N ASN A 119 -10.157 4.237 22.461 1.00 75.67 N ANISOU 924 N ASN A 119 10816 8640 9294 386 1313 -357 N ATOM 925 CA ASN A 119 -10.822 3.201 23.248 1.00 66.71 C ANISOU 925 CA ASN A 119 9390 7299 8659 150 1319 -80 C ATOM 926 C ASN A 119 -12.177 3.746 23.675 1.00 69.68 C ANISOU 926 C ASN A 119 9692 8014 8768 108 1366 -6 C ATOM 927 O ASN A 119 -12.250 4.634 24.531 1.00 73.43 O ANISOU 927 O ASN A 119 10340 8781 8780 146 1461 304 O ATOM 928 CB ASN A 119 -9.983 2.800 24.458 1.00 70.52 C ANISOU 928 CB ASN A 119 9866 7618 9310 28 1384 468 C ATOM 929 CG ASN A 119 -10.488 1.534 25.128 1.00 82.69 C ANISOU 929 CG ASN A 119 11096 8852 11470 -200 1398 744 C ATOM 930 ND2 ASN A 119 -9.605 0.857 25.853 1.00 79.28 N ANISOU 930 ND2 ASN A 119 10624 8162 11337 -272 1436 1127 N ATOM 931 OD1 ASN A 119 -11.656 1.167 24.996 1.00 83.23 O ANISOU 931 OD1 ASN A 119 10952 8921 11749 -311 1376 632 O ATOM 932 N THR A 120 -13.244 3.213 23.084 1.00 69.27 N ANISOU 932 N THR A 120 9390 7931 8998 36 1294 -284 N ATOM 933 CA THR A 120 -14.597 3.636 23.411 1.00 79.07 C ANISOU 933 CA THR A 120 10495 9517 10031 4 1338 -207 C ATOM 934 C THR A 120 -15.235 2.794 24.506 1.00 88.55 C ANISOU 934 C THR A 120 11392 10595 11658 -254 1393 251 C ATOM 935 O THR A 120 -16.315 3.149 24.990 1.00 80.85 O ANISOU 935 O THR A 120 10288 9935 10498 -274 1464 433 O ATOM 936 CB THR A 120 -15.483 3.582 22.164 1.00 85.23 C ANISOU 936 CB THR A 120 11132 10402 10851 58 1217 -743 C ATOM 937 CG2 THR A 120 -14.826 4.322 21.009 1.00 74.38 C ANISOU 937 CG2 THR A 120 10044 9126 9091 335 1172 -1199 C ATOM 938 OG1 THR A 120 -15.688 2.216 21.787 1.00 95.03 O ANISOU 938 OG1 THR A 120 12081 11231 12797 -166 1087 -896 O ATOM 939 N GLU A 121 -14.600 1.689 24.901 1.00 88.91 N ANISOU 939 N GLU A 121 11318 10201 12263 -429 1377 461 N ATOM 940 CA GLU A 121 -15.152 0.838 25.948 1.00 92.02 C ANISOU 940 CA GLU A 121 11423 10447 13094 -672 1445 928 C ATOM 941 C GLU A 121 -14.878 1.389 27.339 1.00 88.82 C ANISOU 941 C GLU A 121 11151 10254 12344 -631 1605 1506 C ATOM 942 O GLU A 121 -15.670 1.160 28.260 1.00 95.60 O ANISOU 942 O GLU A 121 11804 11216 13303 -748 1704 1911 O ATOM 943 CB GLU A 121 -14.576 -0.575 25.833 1.00 85.47 C ANISOU 943 CB GLU A 121 10440 9037 12997 -854 1381 940 C ATOM 944 CG GLU A 121 -15.069 -1.349 24.627 1.00101.98 C ANISOU 944 CG GLU A 121 12360 10859 15530 -957 1211 418 C ATOM 945 CD GLU A 121 -16.568 -1.543 24.641 1.00118.47 C ANISOU 945 CD GLU A 121 14119 13116 17779 -1153 1173 408 C ATOM 946 OE1 GLU A 121 -17.108 -1.903 25.708 1.00111.32 O ANISOU 946 OE1 GLU A 121 12993 12222 17083 -1334 1281 908 O ATOM 947 OE2 GLU A 121 -17.206 -1.342 23.588 1.00124.46 O1- ANISOU 947 OE2 GLU A 121 14822 14014 18452 -1121 1036 -83 O1- ATOM 948 N ARG A 122 -13.777 2.113 27.509 1.00 79.68 N ANISOU 948 N ARG A 122 10331 9172 10773 -470 1628 1558 N ATOM 949 CA ARG A 122 -13.353 2.541 28.834 1.00 74.74 C ANISOU 949 CA ARG A 122 9858 8695 9844 -449 1743 2091 C ATOM 950 C ARG A 122 -14.256 3.646 29.368 1.00 76.03 C ANISOU 950 C ARG A 122 10148 9338 9400 -325 1845 2230 C ATOM 951 O ARG A 122 -14.589 4.599 28.657 1.00 73.69 O ANISOU 951 O ARG A 122 10034 9317 8646 -156 1827 1883 O ATOM 952 CB ARG A 122 -11.901 3.014 28.782 1.00 75.43 C ANISOU 952 CB ARG A 122 10259 8733 9666 -340 1705 2077 C ATOM 953 CG ARG A 122 -11.478 3.898 29.938 1.00 93.29 C ANISOU 953 CG ARG A 122 12793 11266 11386 -277 1779 2491 C ATOM 954 CD ARG A 122 -9.960 3.943 30.096 1.00 89.76 C ANISOU 954 CD ARG A 122 12529 10684 10891 -266 1722 2608 C ATOM 955 NE ARG A 122 -9.322 2.648 29.879 1.00 86.68 N ANISOU 955 NE ARG A 122 11894 9872 11167 -366 1686 2651 N ATOM 956 CZ ARG A 122 -8.710 2.286 28.758 1.00 93.25 C ANISOU 956 CZ ARG A 122 12710 10476 12247 -313 1606 2274 C ATOM 957 NH1 ARG A 122 -8.645 3.097 27.714 1.00 84.36 N1+ ANISOU 957 NH1 ARG A 122 11770 9505 10778 -170 1550 1823 N1+ ATOM 958 NH2 ARG A 122 -8.147 1.083 28.685 1.00 89.86 N ANISOU 958 NH2 ARG A 122 12086 9649 12409 -378 1596 2364 N ATOM 959 N GLY A 123 -14.659 3.505 30.630 1.00 72.50 N ANISOU 959 N GLY A 123 11068 6336 10142 -486 4924 -599 N ATOM 960 CA GLY A 123 -15.462 4.509 31.298 1.00 58.17 C ANISOU 960 CA GLY A 123 9469 4580 8055 -617 4946 -469 C ATOM 961 C GLY A 123 -14.733 5.127 32.472 1.00 77.74 C ANISOU 961 C GLY A 123 12145 7132 10261 -491 4706 -237 C ATOM 962 O GLY A 123 -15.263 6.005 33.155 1.00 80.75 O ANISOU 962 O GLY A 123 12701 7577 10405 -579 4694 -142 O ATOM 963 N GLY A 124 -13.510 4.658 32.721 1.00 75.60 N ANISOU 963 N GLY A 124 11832 6868 10026 -278 4514 -168 N ATOM 964 CA GLY A 124 -12.666 5.186 33.752 1.00 73.04 C ANISOU 964 CA GLY A 124 11638 6669 9445 -140 4264 15 C ATOM 965 C GLY A 124 -11.443 5.886 33.198 1.00 78.91 C ANISOU 965 C GLY A 124 12108 7736 10137 -123 4004 -123 C ATOM 966 O GLY A 124 -11.369 6.234 32.010 1.00 90.15 O ANISOU 966 O GLY A 124 13247 9335 11669 -264 4017 -343 O ATOM 967 N MET A 125 -10.460 6.094 34.069 1.00 85.61 N ANISOU 967 N MET A 125 13028 8694 10804 48 3766 10 N ATOM 968 CA MET A 125 -9.202 6.718 33.687 1.00 70.76 C ANISOU 968 CA MET A 125 10898 7120 8866 78 3507 -112 C ATOM 969 C MET A 125 -8.125 5.659 33.489 1.00 72.89 C ANISOU 969 C MET A 125 11034 7347 9313 320 3398 -126 C ATOM 970 O MET A 125 -8.216 4.546 34.011 1.00 85.69 O ANISOU 970 O MET A 125 12817 8693 11048 511 3470 32 O ATOM 971 CB MET A 125 -8.765 7.736 34.740 1.00 78.25 C ANISOU 971 CB MET A 125 11966 8265 9501 98 3302 -13 C ATOM 972 CG MET A 125 -9.568 9.025 34.737 1.00 69.36 C ANISOU 972 CG MET A 125 10874 7241 8240 -154 3357 -74 C ATOM 973 SD MET A 125 -8.998 10.204 33.499 1.00 85.71 S ANISOU 973 SD MET A 125 12578 9616 10372 -365 3242 -305 S ATOM 974 CE MET A 125 -10.369 10.181 32.350 1.00 69.78 C ANISOU 974 CE MET A 125 10486 7489 8536 -592 3532 -398 C ATOM 975 N ILE A 126 -7.103 6.019 32.710 1.00 84.37 N ANISOU 975 N ILE A 126 12179 9074 10805 308 3227 -316 N ATOM 976 CA ILE A 126 -5.986 5.107 32.481 1.00 64.64 C ANISOU 976 CA ILE A 126 9511 6578 8471 541 3098 -371 C ATOM 977 C ILE A 126 -5.283 4.788 33.793 1.00 78.62 C ANISOU 977 C ILE A 126 11483 8306 10083 819 2914 -133 C ATOM 978 O ILE A 126 -4.833 3.656 34.018 1.00 82.77 O ANISOU 978 O ILE A 126 12031 8642 10777 1072 2891 -44 O ATOM 979 CB ILE A 126 -5.014 5.714 31.453 1.00 69.84 C ANISOU 979 CB ILE A 126 9790 7600 9147 449 2940 -624 C ATOM 980 CG1 ILE A 126 -5.642 5.746 30.061 1.00 84.55 C ANISOU 980 CG1 ILE A 126 11412 9524 11190 220 3131 -849 C ATOM 981 CG2 ILE A 126 -3.713 4.930 31.418 1.00 79.78 C ANISOU 981 CG2 ILE A 126 10878 8915 10522 711 2755 -684 C ATOM 982 CD1 ILE A 126 -6.333 4.467 29.679 1.00 81.97 C ANISOU 982 CD1 ILE A 126 11106 8886 11154 281 3363 -902 C ATOM 983 N HIS A 127 -5.198 5.774 34.688 1.00 76.56 N ANISOU 983 N HIS A 127 11361 8226 9504 781 2782 -28 N ATOM 984 CA HIS A 127 -4.395 5.637 35.898 1.00 83.50 C ANISOU 984 CA HIS A 127 12370 9184 10170 1037 2569 164 C ATOM 985 C HIS A 127 -4.911 4.511 36.788 1.00 83.46 C ANISOU 985 C HIS A 127 12660 8848 10201 1247 2687 468 C ATOM 986 O HIS A 127 -4.188 3.553 37.083 1.00 81.63 O ANISOU 986 O HIS A 127 12424 8522 10072 1531 2590 594 O ATOM 987 CB HIS A 127 -4.378 6.964 36.658 1.00 73.18 C ANISOU 987 CB HIS A 127 11141 8144 8522 916 2442 171 C ATOM 988 CG HIS A 127 -3.747 6.876 38.012 1.00 78.80 C ANISOU 988 CG HIS A 127 12002 8978 8958 1159 2247 368 C ATOM 989 CD2 HIS A 127 -4.273 7.012 39.252 1.00 80.97 C ANISOU 989 CD2 HIS A 127 12553 9245 8965 1210 2265 583 C ATOM 990 ND1 HIS A 127 -2.405 6.616 38.191 1.00 74.35 N ANISOU 990 ND1 HIS A 127 11279 8615 8354 1392 1996 347 N ATOM 991 CE1 HIS A 127 -2.132 6.598 39.484 1.00 89.09 C ANISOU 991 CE1 HIS A 127 13317 10599 9933 1583 1863 551 C ATOM 992 NE2 HIS A 127 -3.248 6.835 40.149 1.00 94.24 N ANISOU 992 NE2 HIS A 127 14233 11139 10436 1473 2024 698 N ATOM 993 N ASP A 128 -6.167 4.608 37.228 1.00 76.44 N ANISOU 993 N ASP A 128 12026 7778 9238 1112 2899 601 N ATOM 994 CA ASP A 128 -6.707 3.669 38.204 1.00 74.49 C ANISOU 994 CA ASP A 128 12080 7248 8975 1282 3017 930 C ATOM 995 C ASP A 128 -7.984 2.980 37.739 1.00 80.72 C ANISOU 995 C ASP A 128 12981 7662 10027 1147 3350 947 C ATOM 996 O ASP A 128 -8.589 2.238 38.522 1.00 81.00 O ANISOU 996 O ASP A 128 13278 7437 10064 1241 3491 1229 O ATOM 997 CB ASP A 128 -6.964 4.382 39.537 1.00 89.03 C ANISOU 997 CB ASP A 128 14157 9270 10399 1283 2943 1124 C ATOM 998 CG ASP A 128 -7.869 5.591 39.387 1.00 82.05 C ANISOU 998 CG ASP A 128 13298 8505 9371 966 3044 956 C ATOM 999 OD1 ASP A 128 -8.189 5.960 38.238 1.00 78.29 O ANISOU 999 OD1 ASP A 128 12643 8009 9093 755 3140 710 O ATOM 1000 OD2 ASP A 128 -8.260 6.173 40.421 1.00 79.52 O1- ANISOU 1000 OD2 ASP A 128 13163 8312 8740 934 3024 1070 O1- ATOM 1001 N GLY A 129 -8.410 3.196 36.496 1.00 78.58 N ANISOU 1001 N GLY A 129 12509 7376 9970 925 3483 659 N ATOM 1002 CA GLY A 129 -9.659 2.620 36.041 1.00 81.21 C ANISOU 1002 CA GLY A 129 12924 7399 10534 778 3801 632 C ATOM 1003 C GLY A 129 -10.897 3.180 36.701 1.00 80.62 C ANISOU 1003 C GLY A 129 13106 7284 10240 598 3966 748 C ATOM 1004 O GLY A 129 -11.979 2.605 36.546 1.00 71.40 O ANISOU 1004 O GLY A 129 12050 5840 9240 497 4240 770 O ATOM 1005 N GLU A 130 -10.775 4.284 37.431 1.00 71.19 N ANISOU 1005 N GLU A 130 11993 6364 8690 549 3812 794 N ATOM 1006 CA GLU A 130 -11.882 4.891 38.150 1.00 70.70 C ANISOU 1006 CA GLU A 130 12162 6305 8398 391 3944 881 C ATOM 1007 C GLU A 130 -12.300 6.190 37.474 1.00 81.48 C ANISOU 1007 C GLU A 130 13378 7881 9700 124 3945 619 C ATOM 1008 O GLU A 130 -11.554 6.776 36.685 1.00 84.39 O ANISOU 1008 O GLU A 130 13487 8456 10120 78 3792 423 O ATOM 1009 CB GLU A 130 -11.501 5.151 39.613 1.00 73.65 C ANISOU 1009 CB GLU A 130 12740 6835 8408 545 3780 1128 C ATOM 1010 CG GLU A 130 -11.542 3.906 40.487 1.00103.92 C ANISOU 1010 CG GLU A 130 16802 10428 12256 773 3854 1481 C ATOM 1011 CD GLU A 130 -10.670 4.025 41.722 1.00107.19 C ANISOU 1011 CD GLU A 130 17312 11085 12332 1005 3608 1713 C ATOM 1012 OE1 GLU A 130 -10.711 5.085 42.381 1.00110.85 O ANISOU 1012 OE1 GLU A 130 17811 11853 12453 922 3498 1660 O ATOM 1013 OE2 GLU A 130 -9.945 3.056 42.034 1.00104.53 O1- ANISOU 1013 OE2 GLU A 130 16999 10641 12077 1276 3525 1938 O1- ATOM 1014 N SER A 131 -13.511 6.634 37.793 1.00 80.34 N ANISOU 1014 N SER A 131 13393 7682 9449 -52 4123 628 N ATOM 1015 CA SER A 131 -14.076 7.835 37.198 1.00 81.02 C ANISOU 1015 CA SER A 131 13359 7922 9503 -298 4150 412 C ATOM 1016 C SER A 131 -13.833 9.048 38.087 1.00 78.80 C ANISOU 1016 C SER A 131 13138 7886 8915 -328 3969 413 C ATOM 1017 O SER A 131 -13.677 8.933 39.306 1.00 78.14 O ANISOU 1017 O SER A 131 13249 7846 8595 -200 3899 587 O ATOM 1018 CB SER A 131 -15.577 7.663 36.956 1.00 80.07 C ANISOU 1018 CB SER A 131 13345 7609 9470 -475 4452 378 C ATOM 1019 OG SER A 131 -16.151 8.847 36.431 1.00 84.23 O ANISOU 1019 OG SER A 131 13713 8296 9994 -666 4378 169 O ATOM 1020 N ARG A 132 -13.801 10.222 37.457 1.00 81.91 N ANISOU 1020 N ARG A 132 13346 8453 9324 -500 3896 214 N ATOM 1021 CA ARG A 132 -13.662 11.486 38.165 1.00 83.20 C ANISOU 1021 CA ARG A 132 13527 8820 9266 -567 3747 154 C ATOM 1022 C ARG A 132 -14.979 12.240 38.299 1.00 82.30 C ANISOU 1022 C ARG A 132 13506 8653 9110 -765 3915 81 C ATOM 1023 O ARG A 132 -15.058 13.175 39.103 1.00 81.23 O ANISOU 1023 O ARG A 132 13428 8647 8788 -811 3828 30 O ATOM 1024 CB ARG A 132 -12.634 12.380 37.459 1.00 76.08 C ANISOU 1024 CB ARG A 132 12344 8132 8432 -622 3535 -8 C ATOM 1025 CG ARG A 132 -11.329 11.680 37.114 1.00 79.96 C ANISOU 1025 CG ARG A 132 12686 8698 8995 -446 3373 13 C ATOM 1026 CD ARG A 132 -10.322 11.789 38.249 1.00 71.39 C ANISOU 1026 CD ARG A 132 11662 7793 7672 -265 3139 82 C ATOM 1027 NE ARG A 132 -9.168 10.923 38.041 1.00 84.86 N ANISOU 1027 NE ARG A 132 13257 9541 9445 -55 3000 131 N ATOM 1028 CZ ARG A 132 -9.160 9.615 38.262 1.00 84.63 C ANISOU 1028 CZ ARG A 132 13351 9330 9474 141 3070 308 C ATOM 1029 NH1 ARG A 132 -10.230 8.984 38.718 1.00 76.15 N1+ ANISOU 1029 NH1 ARG A 132 12521 8021 8391 145 3286 468 N1+ ATOM 1030 NH2 ARG A 132 -8.051 8.923 38.019 1.00 75.84 N ANISOU 1030 NH2 ARG A 132 12104 8263 8450 337 2925 324 N ATOM 1031 N PHE A 133 -16.003 11.863 37.539 1.00 76.64 N ANISOU 1031 N PHE A 133 12730 7772 8616 -852 4041 28 N ATOM 1032 CA PHE A 133 -17.308 12.508 37.596 1.00 82.09 C ANISOU 1032 CA PHE A 133 13372 8427 9390 -961 3970 -92 C ATOM 1033 C PHE A 133 -18.236 11.737 38.524 1.00 85.14 C ANISOU 1033 C PHE A 133 13966 8677 9707 -894 4055 6 C ATOM 1034 O PHE A 133 -18.246 10.504 38.522 1.00 87.03 O ANISOU 1034 O PHE A 133 14298 8764 10006 -795 4179 123 O ATOM 1035 CB PHE A 133 -17.941 12.594 36.207 1.00 74.17 C ANISOU 1035 CB PHE A 133 12115 7388 8678 -1044 3917 -245 C ATOM 1036 CG PHE A 133 -17.065 13.237 35.174 1.00 78.15 C ANISOU 1036 CG PHE A 133 12380 8044 9267 -1111 3833 -316 C ATOM 1037 CD1 PHE A 133 -16.568 14.515 35.363 1.00 71.65 C ANISOU 1037 CD1 PHE A 133 11502 7366 8356 -1198 3745 -358 C ATOM 1038 CD2 PHE A 133 -16.749 12.564 34.006 1.00 70.95 C ANISOU 1038 CD2 PHE A 133 11285 7142 8531 -1099 3856 -356 C ATOM 1039 CE1 PHE A 133 -15.765 15.108 34.406 1.00 67.34 C ANISOU 1039 CE1 PHE A 133 10722 6966 7898 -1273 3676 -411 C ATOM 1040 CE2 PHE A 133 -15.949 13.150 33.048 1.00 76.64 C ANISOU 1040 CE2 PHE A 133 11760 8044 9317 -1167 3771 -417 C ATOM 1041 CZ PHE A 133 -15.455 14.424 33.247 1.00 71.61 C ANISOU 1041 CZ PHE A 133 11070 7545 8593 -1254 3678 -431 C ATOM 1042 N SER A 134 -19.047 12.467 39.288 1.00 81.65 N ANISOU 1042 N SER A 134 13581 8280 9160 -959 4005 -50 N ATOM 1043 CA SER A 134 -20.017 11.829 40.164 1.00 88.86 C ANISOU 1043 CA SER A 134 14658 9101 10003 -921 4081 26 C ATOM 1044 C SER A 134 -21.198 12.760 40.402 1.00 89.13 C ANISOU 1044 C SER A 134 14638 9164 10061 -1040 4019 -132 C ATOM 1045 O SER A 134 -21.068 13.986 40.344 1.00 88.44 O ANISOU 1045 O SER A 134 14462 9186 9955 -1130 3928 -250 O ATOM 1046 CB SER A 134 -19.389 11.426 41.504 1.00 90.21 C ANISOU 1046 CB SER A 134 15067 9359 9851 -805 4126 248 C ATOM 1047 OG SER A 134 -18.930 12.561 42.216 1.00 71.76 O ANISOU 1047 OG SER A 134 12752 7248 7265 -844 4034 190 O ATOM 1048 N ILE A 135 -22.353 12.152 40.662 1.00 96.59 N ANISOU 1048 N ILE A 135 15642 9998 11061 -1042 4088 -136 N ATOM 1049 CA ILE A 135 -23.567 12.849 41.073 1.00 90.95 C ANISOU 1049 CA ILE A 135 14913 9300 10343 -1139 4058 -260 C ATOM 1050 C ILE A 135 -24.084 12.136 42.315 1.00100.84 C ANISOU 1050 C ILE A 135 16354 10554 11405 -1097 4158 -125 C ATOM 1051 O ILE A 135 -24.501 10.973 42.237 1.00 97.24 O ANISOU 1051 O ILE A 135 15960 9959 11027 -1043 4267 -47 O ATOM 1052 CB ILE A 135 -24.639 12.863 39.975 1.00 93.05 C ANISOU 1052 CB ILE A 135 15024 9452 10881 -1198 4032 -426 C ATOM 1053 CG1 ILE A 135 -24.300 13.895 38.904 1.00102.63 C ANISOU 1053 CG1 ILE A 135 16036 10723 12235 -1258 3908 -547 C ATOM 1054 CG2 ILE A 135 -26.010 13.164 40.573 1.00101.42 C ANISOU 1054 CG2 ILE A 135 16122 10492 11922 -1272 4048 -506 C ATOM 1055 CD1 ILE A 135 -25.484 14.287 38.063 1.00105.84 C ANISOU 1055 CD1 ILE A 135 16301 11081 12832 -1321 3851 -698 C ATOM 1056 N ASN A 136 -24.055 12.826 43.456 1.00 96.45 N ANISOU 1056 N ASN A 136 15880 10174 10594 -1125 4133 -104 N ATOM 1057 CA ASN A 136 -24.521 12.269 44.728 1.00105.71 C ANISOU 1057 CA ASN A 136 17211 11422 11532 -1091 4214 37 C ATOM 1058 C ASN A 136 -23.835 10.940 45.037 1.00103.11 C ANISOU 1058 C ASN A 136 17030 11038 11111 -948 4306 311 C ATOM 1059 O ASN A 136 -24.445 10.007 45.564 1.00 97.89 O ANISOU 1059 O ASN A 136 16469 10308 10415 -918 4413 451 O ATOM 1060 CB ASN A 136 -26.043 12.109 44.738 1.00106.78 C ANISOU 1060 CB ASN A 136 17318 11459 11795 -1176 4268 -66 C ATOM 1061 CG ASN A 136 -26.761 13.304 44.142 1.00122.06 C ANISOU 1061 CG ASN A 136 19095 13382 13900 -1300 4179 -315 C ATOM 1062 ND2 ASN A 136 -26.341 14.502 44.531 1.00100.96 N ANISOU 1062 ND2 ASN A 136 16385 10869 11107 -1352 4104 -400 N ATOM 1063 OD1 ASN A 136 -27.685 13.152 43.344 1.00127.50 O ANISOU 1063 OD1 ASN A 136 19697 13924 14822 -1346 4184 -429 O ATOM 1064 N GLY A 137 -22.550 10.850 44.698 1.00105.56 N ANISOU 1064 N GLY A 137 17353 11367 11388 -859 4270 401 N ATOM 1065 CA GLY A 137 -21.776 9.650 44.915 1.00 84.37 C ANISOU 1065 CA GLY A 137 14809 8607 8639 -704 4350 680 C ATOM 1066 C GLY A 137 -21.839 8.633 43.794 1.00 97.79 C ANISOU 1066 C GLY A 137 16455 10028 10673 -669 4447 679 C ATOM 1067 O GLY A 137 -20.951 7.779 43.703 1.00102.82 O ANISOU 1067 O GLY A 137 17175 10571 11321 -535 4505 883 O ATOM 1068 N LYS A 138 -22.859 8.694 42.944 1.00 97.36 N ANISOU 1068 N LYS A 138 16260 9849 10882 -772 4468 451 N ATOM 1069 CA LYS A 138 -22.964 7.775 41.816 1.00 93.95 C ANISOU 1069 CA LYS A 138 15747 9200 10752 -746 4566 389 C ATOM 1070 C LYS A 138 -21.977 8.181 40.729 1.00101.13 C ANISOU 1070 C LYS A 138 16508 10135 11782 -741 4492 294 C ATOM 1071 O LYS A 138 -22.036 9.319 40.252 1.00 94.55 O ANISOU 1071 O LYS A 138 15529 9425 10973 -838 4356 114 O ATOM 1072 CB LYS A 138 -24.382 7.769 41.262 1.00 89.26 C ANISOU 1072 CB LYS A 138 15045 8519 10349 -849 4596 160 C ATOM 1073 CG LYS A 138 -24.499 7.193 39.858 1.00 90.13 C ANISOU 1073 CG LYS A 138 15004 8485 10755 -849 4655 -3 C ATOM 1074 CD LYS A 138 -25.947 6.911 39.494 1.00 97.22 C ANISOU 1074 CD LYS A 138 15848 9293 11799 -923 4717 -188 C ATOM 1075 CE LYS A 138 -26.096 5.541 38.853 1.00 97.77 C ANISOU 1075 CE LYS A 138 15906 9163 12079 -870 4918 -213 C ATOM 1076 NZ LYS A 138 -27.440 5.358 38.240 1.00 98.95 N1+ ANISOU 1076 NZ LYS A 138 15971 9240 12384 -952 4964 -445 N1+ ATOM 1077 N PRO A 139 -21.064 7.304 40.318 1.00 86.61 N ANISOU 1077 N PRO A 139 10966 10298 11643 -410 5213 2456 N ATOM 1078 CA PRO A 139 -20.076 7.694 39.307 1.00 80.84 C ANISOU 1078 CA PRO A 139 10537 9300 10878 -374 4978 2080 C ATOM 1079 C PRO A 139 -20.704 7.880 37.934 1.00 81.88 C ANISOU 1079 C PRO A 139 10607 9145 11358 -363 4779 1933 C ATOM 1080 O PRO A 139 -21.677 7.217 37.568 1.00 81.97 O ANISOU 1080 O PRO A 139 10361 9043 11739 -464 4683 2159 O ATOM 1081 CB PRO A 139 -19.083 6.524 39.304 1.00 73.74 C ANISOU 1081 CB PRO A 139 9740 8249 10031 -511 4753 2214 C ATOM 1082 CG PRO A 139 -19.352 5.766 40.571 1.00 84.13 C ANISOU 1082 CG PRO A 139 10865 9813 11289 -604 4919 2626 C ATOM 1083 CD PRO A 139 -20.805 5.961 40.858 1.00 88.90 C ANISOU 1083 CD PRO A 139 11152 10580 12046 -590 5120 2832 C ATOM 1084 N ILE A 140 -20.129 8.809 37.174 1.00 86.66 N ANISOU 1084 N ILE A 140 11443 9645 11840 -251 4704 1567 N ATOM 1085 CA ILE A 140 -20.494 9.055 35.784 1.00 76.74 C ANISOU 1085 CA ILE A 140 10176 8134 10848 -228 4489 1395 C ATOM 1086 C ILE A 140 -19.327 8.609 34.917 1.00 75.96 C ANISOU 1086 C ILE A 140 10313 7808 10741 -261 4198 1225 C ATOM 1087 O ILE A 140 -18.167 8.909 35.225 1.00 67.35 O ANISOU 1087 O ILE A 140 9448 6792 9351 -219 4223 1093 O ATOM 1088 CB ILE A 140 -20.830 10.536 35.531 1.00 70.97 C ANISOU 1088 CB ILE A 140 9495 7476 9996 -52 4640 1144 C ATOM 1089 CG1 ILE A 140 -21.696 11.098 36.661 1.00 86.62 C ANISOU 1089 CG1 ILE A 140 11314 9746 11853 49 4996 1265 C ATOM 1090 CG2 ILE A 140 -21.510 10.707 34.176 1.00 76.86 C ANISOU 1090 CG2 ILE A 140 10140 8008 11056 -40 4438 1063 C ATOM 1091 CD1 ILE A 140 -23.179 10.862 36.486 1.00 88.54 C ANISOU 1091 CD1 ILE A 140 11194 10016 12431 39 5054 1510 C ATOM 1092 N TYR A 141 -19.632 7.898 33.839 1.00 76.05 N ANISOU 1092 N TYR A 141 10267 7558 11070 -328 3919 1230 N ATOM 1093 CA TYR A 141 -18.603 7.275 33.022 1.00 75.87 C ANISOU 1093 CA TYR A 141 10449 7325 11054 -333 3645 1092 C ATOM 1094 C TYR A 141 -17.985 8.278 32.054 1.00 76.00 C ANISOU 1094 C TYR A 141 10652 7321 10905 -197 3575 772 C ATOM 1095 O TYR A 141 -18.644 9.210 31.583 1.00 64.53 O ANISOU 1095 O TYR A 141 9135 5894 9492 -131 3624 665 O ATOM 1096 CB TYR A 141 -19.197 6.093 32.256 1.00 66.48 C ANISOU 1096 CB TYR A 141 9151 5851 10256 -449 3354 1196 C ATOM 1097 CG TYR A 141 -19.708 4.995 33.158 1.00 74.97 C ANISOU 1097 CG TYR A 141 10038 6907 11539 -613 3377 1557 C ATOM 1098 CD1 TYR A 141 -21.017 4.541 33.055 1.00 80.58 C ANISOU 1098 CD1 TYR A 141 10474 7535 12610 -749 3307 1780 C ATOM 1099 CD2 TYR A 141 -18.880 4.397 34.100 1.00 78.78 C ANISOU 1099 CD2 TYR A 141 10599 7463 11872 -644 3452 1711 C ATOM 1100 CE1 TYR A 141 -21.492 3.536 33.882 1.00 83.64 C ANISOU 1100 CE1 TYR A 141 10661 7909 13208 -919 3318 2162 C ATOM 1101 CE2 TYR A 141 -19.343 3.388 34.923 1.00 80.26 C ANISOU 1101 CE2 TYR A 141 10599 7637 12259 -800 3467 2085 C ATOM 1102 CZ TYR A 141 -20.648 2.959 34.807 1.00 98.56 C ANISOU 1102 CZ TYR A 141 12639 9867 14943 -942 3400 2315 C ATOM 1103 OH TYR A 141 -21.112 1.955 35.625 1.00 84.00 O ANISOU 1103 OH TYR A 141 10583 8015 13318 -1117 3406 2734 O ATOM 1104 N HIS A 142 -16.700 8.081 31.770 1.00 69.77 N ANISOU 1104 N HIS A 142 10076 6497 9934 -150 3464 653 N ATOM 1105 CA HIS A 142 -15.988 8.900 30.803 1.00 61.68 C ANISOU 1105 CA HIS A 142 9212 5468 8754 -31 3375 401 C ATOM 1106 C HIS A 142 -16.213 8.373 29.386 1.00 58.01 C ANISOU 1106 C HIS A 142 8753 4791 8499 0 3089 292 C ATOM 1107 O HIS A 142 -16.701 7.260 29.174 1.00 63.39 O ANISOU 1107 O HIS A 142 9363 5288 9435 -76 2924 383 O ATOM 1108 CB HIS A 142 -14.490 8.924 31.108 1.00 67.14 C ANISOU 1108 CB HIS A 142 10099 6262 9150 12 3384 357 C ATOM 1109 CG HIS A 142 -14.140 9.591 32.401 1.00 64.28 C ANISOU 1109 CG HIS A 142 9774 6124 8524 -18 3625 413 C ATOM 1110 CD2 HIS A 142 -14.233 9.160 33.681 1.00 70.70 C ANISOU 1110 CD2 HIS A 142 10533 7063 9267 -98 3781 604 C ATOM 1111 ND1 HIS A 142 -13.601 10.858 32.463 1.00 68.75 N ANISOU 1111 ND1 HIS A 142 10458 6815 8849 33 3711 261 N ATOM 1112 CE1 HIS A 142 -13.385 11.182 33.726 1.00 76.63 C ANISOU 1112 CE1 HIS A 142 11493 7993 9629 -12 3897 321 C ATOM 1113 NE2 HIS A 142 -13.761 10.169 34.485 1.00 78.02 N ANISOU 1113 NE2 HIS A 142 11561 8197 9884 -83 3955 532 N ATOM 1114 N PHE A 143 -15.838 9.190 28.404 1.00 63.72 N ANISOU 1114 N PHE A 143 9566 5538 9106 110 3016 97 N ATOM 1115 CA PHE A 143 -15.883 8.803 26.998 1.00 67.06 C ANISOU 1115 CA PHE A 143 10027 5817 9636 174 2747 -40 C ATOM 1116 C PHE A 143 -14.565 9.191 26.345 1.00 71.06 C ANISOU 1116 C PHE A 143 10713 6420 9868 313 2692 -185 C ATOM 1117 O PHE A 143 -14.189 10.368 26.355 1.00 63.31 O ANISOU 1117 O PHE A 143 9761 5591 8704 358 2810 -230 O ATOM 1118 CB PHE A 143 -17.057 9.462 26.270 1.00 72.71 C ANISOU 1118 CB PHE A 143 10596 6505 10523 170 2699 -83 C ATOM 1119 CG PHE A 143 -17.237 8.983 24.855 1.00 65.92 C ANISOU 1119 CG PHE A 143 9767 5512 9767 217 2398 -218 C ATOM 1120 CD1 PHE A 143 -17.305 7.629 24.575 1.00 63.48 C ANISOU 1120 CD1 PHE A 143 9498 4998 9623 169 2171 -223 C ATOM 1121 CD2 PHE A 143 -17.339 9.884 23.808 1.00 72.22 C ANISOU 1121 CD2 PHE A 143 10563 6384 10493 312 2328 -340 C ATOM 1122 CE1 PHE A 143 -17.470 7.181 23.278 1.00 71.90 C ANISOU 1122 CE1 PHE A 143 10625 5940 10755 223 1875 -388 C ATOM 1123 CE2 PHE A 143 -17.506 9.440 22.506 1.00 68.06 C ANISOU 1123 CE2 PHE A 143 10072 5772 10016 364 2045 -471 C ATOM 1124 CZ PHE A 143 -17.572 8.087 22.242 1.00 62.09 C ANISOU 1124 CZ PHE A 143 9377 4815 9397 323 1816 -516 C ATOM 1125 N LEU A 144 -13.865 8.200 25.790 1.00 61.26 N ANISOU 1125 N LEU A 144 9585 5087 8606 389 2512 -244 N ATOM 1126 CA LEU A 144 -12.605 8.392 25.075 1.00 68.68 C ANISOU 1126 CA LEU A 144 10666 6142 9286 552 2452 -354 C ATOM 1127 C LEU A 144 -11.541 9.067 25.933 1.00 70.28 C ANISOU 1127 C LEU A 144 10918 6555 9231 547 2644 -268 C ATOM 1128 O LEU A 144 -10.568 9.614 25.404 1.00 65.84 O ANISOU 1128 O LEU A 144 10423 6148 8447 653 2632 -313 O ATOM 1129 CB LEU A 144 -12.818 9.190 23.783 1.00 68.77 C ANISOU 1129 CB LEU A 144 10669 6219 9242 649 2348 -494 C ATOM 1130 CG LEU A 144 -13.709 8.536 22.728 1.00 65.32 C ANISOU 1130 CG LEU A 144 10209 5608 9002 671 2103 -611 C ATOM 1131 CD1 LEU A 144 -14.021 9.517 21.610 1.00 54.48 C ANISOU 1131 CD1 LEU A 144 8791 4351 7557 744 2034 -701 C ATOM 1132 CD2 LEU A 144 -13.048 7.284 22.180 1.00 59.72 C ANISOU 1132 CD2 LEU A 144 9650 4782 8260 798 1910 -722 C ATOM 1133 N GLY A 145 -11.703 9.038 27.255 1.00 62.67 N ANISOU 1133 N GLY A 145 9913 5616 8281 419 2812 -129 N ATOM 1134 CA GLY A 145 -10.789 9.729 28.141 1.00 63.13 C ANISOU 1134 CA GLY A 145 10025 5874 8088 386 2973 -60 C ATOM 1135 C GLY A 145 -10.851 11.237 28.074 1.00 70.51 C ANISOU 1135 C GLY A 145 10960 6923 8906 372 3068 -129 C ATOM 1136 O GLY A 145 -9.978 11.902 28.638 1.00 74.23 O ANISOU 1136 O GLY A 145 11499 7545 9160 339 3149 -98 O ATOM 1137 N THR A 146 -11.858 11.798 27.405 1.00 59.30 N ANISOU 1137 N THR A 146 9466 5425 7640 388 3042 -211 N ATOM 1138 CA THR A 146 -11.975 13.243 27.239 1.00 68.73 C ANISOU 1138 CA THR A 146 10661 6682 8769 393 3112 -272 C ATOM 1139 C THR A 146 -13.198 13.799 27.954 1.00 71.97 C ANISOU 1139 C THR A 146 10983 7042 9318 338 3275 -267 C ATOM 1140 O THR A 146 -13.047 14.598 28.884 1.00 69.58 O ANISOU 1140 O THR A 146 10737 6811 8890 299 3433 -275 O ATOM 1141 CB THR A 146 -12.011 13.594 25.745 1.00 62.63 C ANISOU 1141 CB THR A 146 9867 5898 8031 498 2949 -351 C ATOM 1142 CG2 THR A 146 -10.648 13.359 25.112 1.00 66.88 C ANISOU 1142 CG2 THR A 146 10490 6562 8359 585 2841 -343 C ATOM 1143 OG1 THR A 146 -12.984 12.776 25.084 1.00 66.59 O ANISOU 1143 OG1 THR A 146 10285 6265 8752 522 2825 -384 O ATOM 1144 N SER A 147 -14.404 13.401 27.548 1.00 73.72 N ANISOU 1144 N SER A 147 11068 7153 9791 342 3233 -256 N ATOM 1145 CA SER A 147 -15.654 13.826 28.181 1.00 66.37 C ANISOU 1145 CA SER A 147 10004 6200 9012 317 3399 -214 C ATOM 1146 C SER A 147 -15.738 15.351 28.262 1.00 69.46 C ANISOU 1146 C SER A 147 10434 6626 9331 376 3519 -300 C ATOM 1147 O SER A 147 -15.784 15.947 29.340 1.00 66.89 O ANISOU 1147 O SER A 147 10156 6360 8898 369 3716 -314 O ATOM 1148 CB SER A 147 -15.804 13.190 29.565 1.00 54.67 C ANISOU 1148 CB SER A 147 8495 4779 7499 236 3566 -91 C ATOM 1149 OG SER A 147 -16.375 11.897 29.476 1.00 67.87 O ANISOU 1149 OG SER A 147 10046 6357 9386 171 3467 32 O ATOM 1150 N THR A 148 -15.761 15.978 27.088 1.00 65.86 N ANISOU 1150 N THR A 148 9966 6126 8930 442 3386 -361 N ATOM 1151 CA THR A 148 -15.709 17.429 26.983 1.00 67.47 C ANISOU 1151 CA THR A 148 10220 6320 9094 497 3450 -427 C ATOM 1152 C THR A 148 -17.084 18.083 27.040 1.00 65.61 C ANISOU 1152 C THR A 148 9837 6016 9077 566 3567 -422 C ATOM 1153 O THR A 148 -17.186 19.297 26.839 1.00 76.51 O ANISOU 1153 O THR A 148 11247 7343 10480 636 3604 -474 O ATOM 1154 CB THR A 148 -14.991 17.840 25.697 1.00 65.97 C ANISOU 1154 CB THR A 148 10071 6144 8849 537 3255 -445 C ATOM 1155 CG2 THR A 148 -13.591 17.244 25.664 1.00 67.82 C ANISOU 1155 CG2 THR A 148 10429 6482 8857 501 3165 -430 C ATOM 1156 OG1 THR A 148 -15.729 17.376 24.560 1.00 65.23 O ANISOU 1156 OG1 THR A 148 9840 6016 8927 584 3100 -426 O ATOM 1157 N PHE A 149 -18.141 17.313 27.305 1.00 73.37 N ANISOU 1157 N PHE A 149 10647 6993 10238 550 3619 -336 N ATOM 1158 CA PHE A 149 -19.454 17.877 27.594 1.00 57.39 C ANISOU 1158 CA PHE A 149 8450 4949 8406 629 3779 -293 C ATOM 1159 C PHE A 149 -19.606 18.246 29.063 1.00 71.42 C ANISOU 1159 C PHE A 149 10276 6798 10061 665 4065 -312 C ATOM 1160 O PHE A 149 -20.720 18.217 29.603 1.00 74.68 O ANISOU 1160 O PHE A 149 10510 7258 10608 723 4241 -225 O ATOM 1161 CB PHE A 149 -20.557 16.910 27.159 1.00 73.41 C ANISOU 1161 CB PHE A 149 10234 6963 10697 582 3688 -153 C ATOM 1162 CG PHE A 149 -20.693 16.779 25.667 1.00 79.09 C ANISOU 1162 CG PHE A 149 10890 7617 11542 580 3412 -160 C ATOM 1163 CD1 PHE A 149 -20.004 17.628 24.814 1.00 71.95 C ANISOU 1163 CD1 PHE A 149 10105 6701 10531 647 3306 -253 C ATOM 1164 CD2 PHE A 149 -21.516 15.809 25.117 1.00 61.15 C ANISOU 1164 CD2 PHE A 149 8437 5307 9489 504 3243 -62 C ATOM 1165 CE1 PHE A 149 -20.128 17.510 23.442 1.00 74.46 C ANISOU 1165 CE1 PHE A 149 10363 7007 10921 660 3059 -251 C ATOM 1166 CE2 PHE A 149 -21.644 15.687 23.745 1.00 67.03 C ANISOU 1166 CE2 PHE A 149 9144 6013 10312 507 2971 -92 C ATOM 1167 CZ PHE A 149 -20.950 16.538 22.907 1.00 61.96 C ANISOU 1167 CZ PHE A 149 8621 5395 9523 597 2890 -189 C ATOM 1168 N SER A 150 -18.499 18.574 29.722 1.00 73.41 N ANISOU 1168 N SER A 150 10760 7086 10046 635 4111 -415 N ATOM 1169 CA SER A 150 -18.481 19.060 31.089 1.00 71.25 C ANISOU 1169 CA SER A 150 10591 6891 9588 677 4356 -483 C ATOM 1170 C SER A 150 -17.679 20.351 31.131 1.00 78.34 C ANISOU 1170 C SER A 150 11726 7707 10333 714 4338 -663 C ATOM 1171 O SER A 150 -16.723 20.527 30.372 1.00 76.61 O ANISOU 1171 O SER A 150 11609 7434 10066 644 4136 -684 O ATOM 1172 CB SER A 150 -17.870 18.027 32.048 1.00 65.03 C ANISOU 1172 CB SER A 150 9860 6247 8603 560 4401 -409 C ATOM 1173 OG SER A 150 -17.710 18.566 33.348 1.00 71.01 O ANISOU 1173 OG SER A 150 10753 7111 9117 600 4615 -497 O ATOM 1174 N GLU A 151 -18.081 21.261 32.020 1.00 79.40 N ANISOU 1174 N GLU A 151 11945 7831 10394 830 4545 -786 N ATOM 1175 CA GLU A 151 -17.364 22.526 32.131 1.00 82.57 C ANISOU 1175 CA GLU A 151 12593 8102 10676 852 4505 -971 C ATOM 1176 C GLU A 151 -15.933 22.311 32.608 1.00 79.63 C ANISOU 1176 C GLU A 151 12436 7803 10018 681 4393 -1011 C ATOM 1177 O GLU A 151 -15.034 23.078 32.245 1.00 85.39 O ANISOU 1177 O GLU A 151 13325 8424 10693 614 4233 -1081 O ATOM 1178 CB GLU A 151 -18.122 23.475 33.058 1.00 69.57 C ANISOU 1178 CB GLU A 151 11011 6426 8997 1029 4724 -1120 C ATOM 1179 CG GLU A 151 -19.398 24.027 32.433 1.00 75.30 C ANISOU 1179 CG GLU A 151 11538 7044 10028 1220 4798 -1082 C ATOM 1180 CD GLU A 151 -20.170 24.942 33.363 1.00 73.97 C ANISOU 1180 CD GLU A 151 11395 6894 9817 1407 4944 -1197 C ATOM 1181 OE1 GLU A 151 -20.047 24.785 34.596 1.00 77.11 O ANISOU 1181 OE1 GLU A 151 11885 7460 9952 1408 5047 -1266 O ATOM 1182 OE2 GLU A 151 -20.903 25.818 32.859 1.00 82.27 O1- ANISOU 1182 OE2 GLU A 151 12372 7799 11089 1570 4954 -1216 O1- ATOM 1183 N TYR A 152 -15.704 21.274 33.411 1.00 80.56 N ANISOU 1183 N TYR A 152 12535 8109 9964 601 4465 -932 N ATOM 1184 CA TYR A 152 -14.369 20.847 33.804 1.00 73.85 C ANISOU 1184 CA TYR A 152 11833 7363 8862 437 4349 -910 C ATOM 1185 C TYR A 152 -14.259 19.346 33.592 1.00 79.34 C ANISOU 1185 C TYR A 152 12370 8178 9597 359 4294 -707 C ATOM 1186 O TYR A 152 -15.190 18.600 33.908 1.00 74.51 O ANISOU 1186 O TYR A 152 11590 7632 9088 400 4425 -603 O ATOM 1187 CB TYR A 152 -14.065 21.192 35.268 1.00 73.73 C ANISOU 1187 CB TYR A 152 12011 7463 8539 421 4493 -1034 C ATOM 1188 CG TYR A 152 -13.997 22.672 35.552 1.00 89.31 C ANISOU 1188 CG TYR A 152 14196 9283 10455 482 4487 -1269 C ATOM 1189 CD1 TYR A 152 -15.144 23.455 35.550 1.00 86.58 C ANISOU 1189 CD1 TYR A 152 13784 8834 10281 668 4583 -1358 C ATOM 1190 CD2 TYR A 152 -12.781 23.290 35.813 1.00 85.87 C ANISOU 1190 CD2 TYR A 152 14007 8803 9816 344 4338 -1377 C ATOM 1191 CE1 TYR A 152 -15.084 24.807 35.802 1.00 95.90 C ANISOU 1191 CE1 TYR A 152 15158 9844 11437 733 4537 -1570 C ATOM 1192 CE2 TYR A 152 -12.712 24.643 36.068 1.00 90.24 C ANISOU 1192 CE2 TYR A 152 14784 9161 10341 385 4308 -1606 C ATOM 1193 CZ TYR A 152 -13.867 25.395 36.061 1.00 95.05 C ANISOU 1193 CZ TYR A 152 15328 9650 11137 586 4392 -1702 C ATOM 1194 OH TYR A 152 -13.805 26.741 36.312 1.00108.92 O ANISOU 1194 OH TYR A 152 17299 11190 12895 638 4323 -1924 O ATOM 1195 N THR A 153 -13.125 18.905 33.051 1.00 65.59 N ANISOU 1195 N THR A 153 10675 6459 7787 254 4096 -639 N ATOM 1196 CA THR A 153 -12.925 17.488 32.776 1.00 58.39 C ANISOU 1196 CA THR A 153 9646 5616 6925 204 4019 -471 C ATOM 1197 C THR A 153 -11.477 17.106 33.038 1.00 71.71 C ANISOU 1197 C THR A 153 11448 7417 8381 97 3905 -411 C ATOM 1198 O THR A 153 -10.578 17.941 32.954 1.00 65.71 O ANISOU 1198 O THR A 153 10821 6663 7484 48 3816 -475 O ATOM 1199 CB THR A 153 -13.303 17.131 31.330 1.00 67.65 C ANISOU 1199 CB THR A 153 10682 6673 8350 258 3863 -430 C ATOM 1200 CG2 THR A 153 -12.721 18.147 30.364 1.00 65.04 C ANISOU 1200 CG2 THR A 153 10425 6273 8016 280 3722 -505 C ATOM 1201 OG1 THR A 153 -12.795 15.833 31.007 1.00 70.59 O ANISOU 1201 OG1 THR A 153 11010 7080 8731 218 3741 -313 O ATOM 1202 N VAL A 154 -11.250 15.832 33.348 1.00 67.82 N ANISOU 1202 N VAL A 154 10891 7008 7869 57 3896 -262 N ATOM 1203 CA VAL A 154 -9.915 15.319 33.637 1.00 63.65 C ANISOU 1203 CA VAL A 154 10439 6606 7140 -23 3800 -165 C ATOM 1204 C VAL A 154 -9.475 14.429 32.484 1.00 61.79 C ANISOU 1204 C VAL A 154 10129 6315 7033 29 3628 -83 C ATOM 1205 O VAL A 154 -10.193 13.497 32.102 1.00 76.78 O ANISOU 1205 O VAL A 154 11917 8119 9137 75 3610 -31 O ATOM 1206 CB VAL A 154 -9.878 14.556 34.972 1.00 70.13 C ANISOU 1206 CB VAL A 154 11256 7578 7813 -90 3923 -41 C ATOM 1207 CG1 VAL A 154 -8.493 13.983 35.215 1.00 67.44 C ANISOU 1207 CG1 VAL A 154 10968 7370 7285 -163 3810 90 C ATOM 1208 CG2 VAL A 154 -10.283 15.478 36.113 1.00 57.28 C ANISOU 1208 CG2 VAL A 154 9726 6041 5997 -110 4099 -156 C ATOM 1209 N VAL A 155 -8.299 14.719 31.928 1.00 71.37 N ANISOU 1209 N VAL A 155 11401 7593 8124 25 3493 -68 N ATOM 1210 CA VAL A 155 -7.776 14.010 30.766 1.00 67.98 C ANISOU 1210 CA VAL A 155 10919 7148 7764 120 3341 -15 C ATOM 1211 C VAL A 155 -6.324 13.636 31.032 1.00 72.22 C ANISOU 1211 C VAL A 155 11493 7857 8092 94 3274 119 C ATOM 1212 O VAL A 155 -5.569 14.418 31.619 1.00 73.18 O ANISOU 1212 O VAL A 155 11683 8102 8021 -12 3276 145 O ATOM 1213 CB VAL A 155 -7.887 14.862 29.481 1.00 67.52 C ANISOU 1213 CB VAL A 155 10841 7032 7782 194 3245 -103 C ATOM 1214 CG1 VAL A 155 -7.385 14.083 28.274 1.00 54.24 C ANISOU 1214 CG1 VAL A 155 9111 5373 6126 327 3100 -67 C ATOM 1215 CG2 VAL A 155 -9.319 15.324 29.259 1.00 49.48 C ANISOU 1215 CG2 VAL A 155 8501 4591 5707 221 3310 -213 C ATOM 1216 N HIS A 156 -5.938 12.434 30.608 1.00 72.66 N ANISOU 1216 N HIS A 156 11503 7910 8193 194 3202 205 N ATOM 1217 CA HIS A 156 -4.537 12.037 30.649 1.00 65.65 C ANISOU 1217 CA HIS A 156 10619 7196 7129 221 3135 351 C ATOM 1218 C HIS A 156 -3.701 13.000 29.814 1.00 66.39 C ANISOU 1218 C HIS A 156 10705 7415 7104 245 3048 357 C ATOM 1219 O HIS A 156 -4.123 13.444 28.742 1.00 65.73 O ANISOU 1219 O HIS A 156 10597 7263 7113 328 2999 260 O ATOM 1220 CB HIS A 156 -4.383 10.604 30.136 1.00 57.75 C ANISOU 1220 CB HIS A 156 9582 6123 6237 383 3068 405 C ATOM 1221 CG HIS A 156 -3.013 10.030 30.325 1.00 66.55 C ANISOU 1221 CG HIS A 156 10682 7414 7191 444 3027 582 C ATOM 1222 CD2 HIS A 156 -2.534 9.146 31.232 1.00 73.60 C ANISOU 1222 CD2 HIS A 156 11564 8356 8044 422 3052 750 C ATOM 1223 ND1 HIS A 156 -1.952 10.350 29.506 1.00 69.35 N ANISOU 1223 ND1 HIS A 156 11002 7940 7406 553 2953 635 N ATOM 1224 CE1 HIS A 156 -0.877 9.693 29.903 1.00 75.98 C ANISOU 1224 CE1 HIS A 156 11808 8931 8132 605 2941 821 C ATOM 1225 NE2 HIS A 156 -1.203 8.955 30.949 1.00 79.84 N ANISOU 1225 NE2 HIS A 156 12316 9338 8682 526 2994 891 N ATOM 1226 N SER A 157 -2.508 13.331 30.316 1.00 71.27 N ANISOU 1226 N SER A 157 11327 8235 7518 157 3019 501 N ATOM 1227 CA SER A 157 -1.696 14.365 29.681 1.00 70.16 C ANISOU 1227 CA SER A 157 11157 8227 7273 125 2930 559 C ATOM 1228 C SER A 157 -1.244 13.977 28.280 1.00 67.85 C ANISOU 1228 C SER A 157 10771 8016 6993 340 2856 610 C ATOM 1229 O SER A 157 -0.941 14.862 27.472 1.00 67.86 O ANISOU 1229 O SER A 157 10724 8096 6963 344 2793 643 O ATOM 1230 CB SER A 157 -0.477 14.687 30.547 1.00 63.84 C ANISOU 1230 CB SER A 157 10357 7639 6261 -34 2887 739 C ATOM 1231 OG SER A 157 0.472 13.638 30.499 1.00 74.15 O ANISOU 1231 OG SER A 157 11577 9115 7483 81 2865 927 O ATOM 1232 N GLY A 158 -1.188 12.682 27.972 1.00 58.97 N ANISOU 1232 N GLY A 158 9623 6874 5908 529 2859 619 N ATOM 1233 CA GLY A 158 -0.867 12.253 26.623 1.00 57.01 C ANISOU 1233 CA GLY A 158 9318 6698 5647 777 2796 612 C ATOM 1234 C GLY A 158 -1.953 12.525 25.603 1.00 62.58 C ANISOU 1234 C GLY A 158 10040 7247 6493 856 2762 420 C ATOM 1235 O GLY A 158 -1.692 12.410 24.401 1.00 65.13 O ANISOU 1235 O GLY A 158 10318 7670 6758 1054 2701 405 O ATOM 1236 N GLN A 159 -3.158 12.878 26.052 1.00 67.90 N ANISOU 1236 N GLN A 159 10764 7704 7331 720 2804 285 N ATOM 1237 CA GLN A 159 -4.266 13.222 25.172 1.00 74.40 C ANISOU 1237 CA GLN A 159 11581 8384 8305 769 2767 127 C ATOM 1238 C GLN A 159 -4.539 14.719 25.145 1.00 72.54 C ANISOU 1238 C GLN A 159 11331 8149 8081 631 2782 128 C ATOM 1239 O GLN A 159 -5.592 15.141 24.654 1.00 72.54 O ANISOU 1239 O GLN A 159 11317 8012 8232 639 2772 15 O ATOM 1240 CB GLN A 159 -5.532 12.475 25.600 1.00 73.57 C ANISOU 1240 CB GLN A 159 11509 8027 8418 740 2798 1 C ATOM 1241 CG GLN A 159 -5.585 11.022 25.172 1.00 69.08 C ANISOU 1241 CG GLN A 159 10963 7363 7923 902 2719 -49 C ATOM 1242 CD GLN A 159 -6.697 10.257 25.861 1.00 75.56 C ANISOU 1242 CD GLN A 159 11794 7942 8975 811 2743 -96 C ATOM 1243 NE2 GLN A 159 -6.392 9.690 27.023 1.00 76.22 N ANISOU 1243 NE2 GLN A 159 11891 8021 9048 727 2820 24 N ATOM 1244 OE1 GLN A 159 -7.816 10.176 25.357 1.00 80.83 O ANISOU 1244 OE1 GLN A 159 12437 8446 9829 810 2687 -209 O ATOM 1245 N VAL A 160 -3.622 15.529 25.662 1.00 63.83 N ANISOU 1245 N VAL A 160 10229 7184 6840 501 2788 260 N ATOM 1246 CA VAL A 160 -3.828 16.962 25.833 1.00 68.07 C ANISOU 1246 CA VAL A 160 10787 7666 7412 346 2785 255 C ATOM 1247 C VAL A 160 -2.746 17.666 25.026 1.00 69.82 C ANISOU 1247 C VAL A 160 10922 8097 7511 352 2685 441 C ATOM 1248 O VAL A 160 -1.587 17.739 25.454 1.00 70.19 O ANISOU 1248 O VAL A 160 10945 8321 7404 269 2654 611 O ATOM 1249 CB VAL A 160 -3.784 17.376 27.308 1.00 69.66 C ANISOU 1249 CB VAL A 160 11090 7807 7571 146 2855 234 C ATOM 1250 CG1 VAL A 160 -3.840 18.878 27.438 1.00 74.47 C ANISOU 1250 CG1 VAL A 160 11751 8334 8211 2 2820 213 C ATOM 1251 CG2 VAL A 160 -4.928 16.733 28.071 1.00 59.45 C ANISOU 1251 CG2 VAL A 160 9846 6348 6393 153 2975 90 C ATOM 1252 N ALA A 161 -3.111 18.189 23.857 1.00 59.96 N ANISOU 1252 N ALA A 161 9605 6852 6327 441 2628 443 N ATOM 1253 CA ALA A 161 -2.156 18.846 22.974 1.00 63.17 C ANISOU 1253 CA ALA A 161 9894 7488 6621 460 2538 662 C ATOM 1254 C ALA A 161 -2.117 20.337 23.286 1.00 72.32 C ANISOU 1254 C ALA A 161 11073 8542 7865 239 2484 737 C ATOM 1255 O ALA A 161 -3.144 21.018 23.213 1.00 74.18 O ANISOU 1255 O ALA A 161 11356 8550 8279 207 2494 610 O ATOM 1256 CB ALA A 161 -2.526 18.610 21.511 1.00 52.09 C ANISOU 1256 CB ALA A 161 8400 6180 5213 683 2495 650 C ATOM 1257 N LYS A 162 -0.935 20.838 23.638 1.00 60.08 N ANISOU 1257 N LYS A 162 9483 7143 6202 86 2415 950 N ATOM 1258 CA LYS A 162 -0.748 22.265 23.865 1.00 69.06 C ANISOU 1258 CA LYS A 162 10645 8164 7430 -141 2316 1043 C ATOM 1259 C LYS A 162 -0.645 22.984 22.526 1.00 63.80 C ANISOU 1259 C LYS A 162 9825 7602 6815 -82 2229 1241 C ATOM 1260 O LYS A 162 0.144 22.591 21.661 1.00 70.06 O ANISOU 1260 O LYS A 162 10448 8716 7455 45 2205 1461 O ATOM 1261 CB LYS A 162 0.507 22.510 24.701 1.00 59.56 C ANISOU 1261 CB LYS A 162 9442 7092 6096 -356 2233 1225 C ATOM 1262 CG LYS A 162 0.814 23.975 24.961 1.00 62.22 C ANISOU 1262 CG LYS A 162 9823 7281 6539 -623 2081 1326 C ATOM 1263 CD LYS A 162 1.977 24.128 25.928 1.00 69.52 C ANISOU 1263 CD LYS A 162 10767 8317 7330 -866 1973 1472 C ATOM 1264 CE LYS A 162 2.332 25.590 26.142 1.00 84.73 C ANISOU 1264 CE LYS A 162 12748 10064 9380 -1156 1774 1576 C ATOM 1265 NZ LYS A 162 3.479 25.749 27.079 1.00 84.34 N1+ ANISOU 1265 NZ LYS A 162 12717 10129 9199 -1424 1628 1723 N1+ ATOM 1266 N ILE A 163 -1.444 24.037 22.351 1.00 54.06 N ANISOU 1266 N ILE A 163 8640 6113 5787 -153 2189 1178 N ATOM 1267 CA ILE A 163 -1.487 24.746 21.075 1.00 62.39 C ANISOU 1267 CA ILE A 163 9542 7252 6911 -96 2105 1381 C ATOM 1268 C ILE A 163 -1.126 26.214 21.258 1.00 73.93 C ANISOU 1268 C ILE A 163 11014 8548 8528 -347 1961 1557 C ATOM 1269 O ILE A 163 -0.846 26.667 22.375 1.00 65.27 O ANISOU 1269 O ILE A 163 10066 7263 7471 -560 1915 1483 O ATOM 1270 CB ILE A 163 -2.867 24.607 20.405 1.00 62.32 C ANISOU 1270 CB ILE A 163 9542 7098 7039 88 2166 1191 C ATOM 1271 CG1 ILE A 163 -3.936 25.350 21.210 1.00 64.59 C ANISOU 1271 CG1 ILE A 163 9993 6979 7571 -11 2201 964 C ATOM 1272 CG2 ILE A 163 -3.237 23.142 20.230 1.00 64.90 C ANISOU 1272 CG2 ILE A 163 9875 7544 7241 306 2267 1010 C ATOM 1273 CD1 ILE A 163 -5.248 25.511 20.472 1.00 59.63 C ANISOU 1273 CD1 ILE A 163 9323 6213 7120 139 2231 861 C ATOM 1274 N ASN A 164 -1.129 26.956 20.155 1.00 78.56 N ANISOU 1274 N ASN A 164 11448 9199 9201 -324 1872 1794 N ATOM 1275 CA ASN A 164 -0.807 28.375 20.179 1.00 70.24 C ANISOU 1275 CA ASN A 164 10387 7961 8341 -562 1706 2004 C ATOM 1276 C ASN A 164 -1.814 29.123 21.049 1.00 82.55 C ANISOU 1276 C ASN A 164 12188 9026 10150 -651 1712 1700 C ATOM 1277 O ASN A 164 -3.027 28.997 20.829 1.00 70.93 O ANISOU 1277 O ASN A 164 10762 7394 8794 -478 1817 1484 O ATOM 1278 CB ASN A 164 -0.820 28.921 18.750 1.00 77.68 C ANISOU 1278 CB ASN A 164 11103 9074 9336 -478 1633 2321 C ATOM 1279 CG ASN A 164 -0.191 30.297 18.631 1.00 90.82 C ANISOU 1279 CG ASN A 164 12698 10622 11189 -743 1430 2660 C ATOM 1280 ND2 ASN A 164 -0.414 30.947 17.495 1.00 83.32 N ANISOU 1280 ND2 ASN A 164 11573 9738 10347 -690 1362 2931 N ATOM 1281 OD1 ASN A 164 0.493 30.766 19.538 1.00101.52 O ANISOU 1281 OD1 ASN A 164 14149 11831 12592 -1002 1318 2694 O ATOM 1282 N PRO A 165 -1.364 29.895 22.043 1.00 90.96 N ANISOU 1282 N PRO A 165 13413 9851 11299 -906 1599 1668 N ATOM 1283 CA PRO A 165 -2.326 30.603 22.907 1.00 80.00 C ANISOU 1283 CA PRO A 165 12281 7998 10119 -945 1621 1340 C ATOM 1284 C PRO A 165 -3.190 31.607 22.164 1.00 80.97 C ANISOU 1284 C PRO A 165 12376 7850 10537 -878 1576 1385 C ATOM 1285 O PRO A 165 -4.307 31.897 22.611 1.00 82.21 O ANISOU 1285 O PRO A 165 12692 7689 10856 -775 1673 1091 O ATOM 1286 CB PRO A 165 -1.429 31.294 23.947 1.00 72.42 C ANISOU 1286 CB PRO A 165 11484 6877 9156 -1250 1450 1348 C ATOM 1287 CG PRO A 165 -0.119 30.584 23.880 1.00 76.45 C ANISOU 1287 CG PRO A 165 11828 7806 9412 -1347 1396 1618 C ATOM 1288 CD PRO A 165 0.029 30.086 22.481 1.00 72.74 C ANISOU 1288 CD PRO A 165 11065 7696 8876 -1158 1445 1908 C ATOM 1289 N ASP A 166 -2.714 32.144 21.044 1.00 71.00 N ANISOU 1289 N ASP A 166 10899 6727 9351 -920 1439 1770 N ATOM 1290 CA ASP A 166 -3.460 33.125 20.270 1.00 77.63 C ANISOU 1290 CA ASP A 166 11683 7330 10481 -865 1375 1880 C ATOM 1291 C ASP A 166 -4.411 32.489 19.262 1.00 76.52 C ANISOU 1291 C ASP A 166 11384 7381 10309 -576 1515 1862 C ATOM 1292 O ASP A 166 -5.003 33.206 18.449 1.00 81.32 O ANISOU 1292 O ASP A 166 11893 7876 11129 -509 1460 2013 O ATOM 1293 CB ASP A 166 -2.494 34.069 19.549 1.00 78.72 C ANISOU 1293 CB ASP A 166 11649 7531 10729 -1073 1141 2354 C ATOM 1294 CG ASP A 166 -1.711 34.942 20.510 1.00 79.61 C ANISOU 1294 CG ASP A 166 11939 7346 10964 -1397 939 2371 C ATOM 1295 OD1 ASP A 166 -2.050 34.952 21.712 1.00 81.07 O ANISOU 1295 OD1 ASP A 166 12410 7236 11157 -1434 985 1976 O ATOM 1296 OD2 ASP A 166 -0.758 35.617 20.066 1.00 99.90 O1- ANISOU 1296 OD2 ASP A 166 14357 9988 13612 -1621 725 2787 O1- ATOM 1297 N ALA A 167 -4.576 31.168 19.299 1.00 70.86 N ANISOU 1297 N ALA A 167 10643 6936 9346 -411 1673 1690 N ATOM 1298 CA ALA A 167 -5.495 30.554 18.350 1.00 70.09 C ANISOU 1298 CA ALA A 167 10412 6997 9222 -159 1767 1653 C ATOM 1299 C ALA A 167 -6.915 30.550 18.911 1.00 76.48 C ANISOU 1299 C ALA A 167 11359 7478 10220 -41 1895 1309 C ATOM 1300 O ALA A 167 -7.112 30.274 20.098 1.00 72.49 O ANISOU 1300 O ALA A 167 11043 6800 9701 -77 1996 1025 O ATOM 1301 CB ALA A 167 -5.069 29.125 18.029 1.00 77.64 C ANISOU 1301 CB ALA A 167 11282 8365 9853 -24 1851 1626 C ATOM 1302 N PRO A 168 -7.914 30.853 18.080 1.00 67.45 N ANISOU 1302 N PRO A 168 10104 6277 9246 106 1896 1353 N ATOM 1303 CA PRO A 168 -9.300 30.859 18.567 1.00 73.65 C ANISOU 1303 CA PRO A 168 10973 6784 10224 234 2025 1070 C ATOM 1304 C PRO A 168 -9.802 29.456 18.866 1.00 74.37 C ANISOU 1304 C PRO A 168 11073 7037 10146 355 2171 828 C ATOM 1305 O PRO A 168 -9.976 28.643 17.953 1.00 73.59 O ANISOU 1305 O PRO A 168 10830 7211 9921 473 2154 886 O ATOM 1306 CB PRO A 168 -10.073 31.509 17.413 1.00 71.43 C ANISOU 1306 CB PRO A 168 10516 6476 10148 349 1953 1268 C ATOM 1307 CG PRO A 168 -9.257 31.210 16.201 1.00 71.25 C ANISOU 1307 CG PRO A 168 10297 6863 9912 350 1835 1580 C ATOM 1308 CD PRO A 168 -7.823 31.184 16.648 1.00 71.23 C ANISOU 1308 CD PRO A 168 10352 6982 9728 169 1781 1690 C ATOM 1309 N LEU A 169 -10.030 29.166 20.149 1.00 61.32 N ANISOU 1309 N LEU A 169 9597 5216 8485 324 2303 558 N ATOM 1310 CA LEU A 169 -10.451 27.826 20.545 1.00 69.64 C ANISOU 1310 CA LEU A 169 10657 6404 9401 408 2433 363 C ATOM 1311 C LEU A 169 -11.771 27.444 19.887 1.00 78.46 C ANISOU 1311 C LEU A 169 11633 7523 10656 578 2475 318 C ATOM 1312 O LEU A 169 -11.948 26.299 19.449 1.00 80.53 O ANISOU 1312 O LEU A 169 11814 7989 10796 650 2474 285 O ATOM 1313 CB LEU A 169 -10.556 27.745 22.069 1.00 67.90 C ANISOU 1313 CB LEU A 169 10634 6004 9161 347 2573 120 C ATOM 1314 CG LEU A 169 -9.267 28.060 22.834 1.00 67.61 C ANISOU 1314 CG LEU A 169 10749 5971 8970 156 2510 144 C ATOM 1315 CD1 LEU A 169 -9.539 28.221 24.322 1.00 63.74 C ANISOU 1315 CD1 LEU A 169 10471 5278 8468 113 2638 -115 C ATOM 1316 CD2 LEU A 169 -8.220 26.984 22.589 1.00 65.12 C ANISOU 1316 CD2 LEU A 169 10367 5990 8385 115 2467 257 C ATOM 1317 N ASP A 170 -12.697 28.402 19.780 1.00 78.53 N ANISOU 1317 N ASP A 170 11608 7298 10931 643 2492 327 N ATOM 1318 CA ASP A 170 -13.993 28.177 19.152 1.00 74.42 C ANISOU 1318 CA ASP A 170 10924 6780 10574 793 2515 323 C ATOM 1319 C ASP A 170 -13.887 27.809 17.678 1.00 75.81 C ANISOU 1319 C ASP A 170 10918 7230 10658 845 2355 517 C ATOM 1320 O ASP A 170 -14.891 27.392 17.090 1.00 78.08 O ANISOU 1320 O ASP A 170 11065 7572 11029 949 2337 509 O ATOM 1321 CB ASP A 170 -14.873 29.420 19.304 1.00 73.64 C ANISOU 1321 CB ASP A 170 10816 6377 10787 868 2560 335 C ATOM 1322 CG ASP A 170 -14.267 30.651 18.654 1.00 83.33 C ANISOU 1322 CG ASP A 170 12034 7511 12118 812 2406 566 C ATOM 1323 OD1 ASP A 170 -13.133 31.025 19.023 1.00 84.89 O ANISOU 1323 OD1 ASP A 170 12365 7677 12213 662 2343 605 O ATOM 1324 OD2 ASP A 170 -14.924 31.246 17.775 1.00 92.27 O1- ANISOU 1324 OD2 ASP A 170 13010 8604 13446 904 2335 736 O1- ATOM 1325 N LYS A 171 -12.713 27.961 17.067 1.00 59.73 N ANISOU 1325 N LYS A 171 8870 5386 8439 779 2234 700 N ATOM 1326 CA LYS A 171 -12.485 27.541 15.691 1.00 67.56 C ANISOU 1326 CA LYS A 171 9703 6702 9264 854 2097 872 C ATOM 1327 C LYS A 171 -11.647 26.272 15.602 1.00 73.31 C ANISOU 1327 C LYS A 171 10471 7711 9671 868 2090 798 C ATOM 1328 O LYS A 171 -12.008 25.341 14.878 1.00 79.64 O ANISOU 1328 O LYS A 171 11207 8701 10353 979 2035 735 O ATOM 1329 CB LYS A 171 -11.806 28.666 14.899 1.00 74.82 C ANISOU 1329 CB LYS A 171 10532 7692 10204 808 1971 1195 C ATOM 1330 CG LYS A 171 -12.491 30.016 15.013 1.00 84.13 C ANISOU 1330 CG LYS A 171 11692 8543 11730 794 1961 1291 C ATOM 1331 CD LYS A 171 -13.931 29.952 14.535 1.00 85.95 C ANISOU 1331 CD LYS A 171 11793 8718 12146 940 1971 1249 C ATOM 1332 CE LYS A 171 -14.564 31.333 14.518 1.00 93.51 C ANISOU 1332 CE LYS A 171 12708 9364 13456 963 1955 1387 C ATOM 1333 NZ LYS A 171 -16.026 31.271 14.237 1.00 86.51 N1+ ANISOU 1333 NZ LYS A 171 11684 8409 12776 1112 1990 1343 N1+ ATOM 1334 N VAL A 172 -10.532 26.213 16.339 1.00 63.49 N ANISOU 1334 N VAL A 172 9342 6489 8292 761 2131 799 N ATOM 1335 CA VAL A 172 -9.602 25.095 16.223 1.00 75.70 C ANISOU 1335 CA VAL A 172 10911 8312 9538 796 2126 772 C ATOM 1336 C VAL A 172 -9.990 23.908 17.094 1.00 78.63 C ANISOU 1336 C VAL A 172 11394 8596 9887 814 2228 500 C ATOM 1337 O VAL A 172 -9.275 22.896 17.094 1.00 64.77 O ANISOU 1337 O VAL A 172 9674 7023 7911 858 2229 457 O ATOM 1338 CB VAL A 172 -8.165 25.537 16.568 1.00 59.66 C ANISOU 1338 CB VAL A 172 8911 6386 7369 670 2108 953 C ATOM 1339 CG1 VAL A 172 -7.724 26.667 15.650 1.00 60.13 C ANISOU 1339 CG1 VAL A 172 8832 6555 7461 636 1990 1281 C ATOM 1340 CG2 VAL A 172 -8.071 25.953 18.028 1.00 60.96 C ANISOU 1340 CG2 VAL A 172 9243 6261 7657 505 2192 826 C ATOM 1341 N CYS A 173 -11.099 23.990 17.835 1.00 75.70 N ANISOU 1341 N CYS A 173 11064 7957 9740 792 2319 338 N ATOM 1342 CA CYS A 173 -11.531 22.841 18.623 1.00 73.01 C ANISOU 1342 CA CYS A 173 10795 7552 9393 798 2411 131 C ATOM 1343 C CYS A 173 -11.940 21.657 17.752 1.00 67.16 C ANISOU 1343 C CYS A 173 9987 6951 8579 916 2317 61 C ATOM 1344 O CYS A 173 -12.008 20.530 18.254 1.00 66.24 O ANISOU 1344 O CYS A 173 9931 6812 8423 919 2351 -74 O ATOM 1345 CB CYS A 173 -12.689 23.240 19.537 1.00 68.32 C ANISOU 1345 CB CYS A 173 10220 6688 9050 769 2541 13 C ATOM 1346 SG CYS A 173 -14.148 23.838 18.659 1.00 74.00 S ANISOU 1346 SG CYS A 173 10765 7313 10038 869 2490 64 S ATOM 1347 N ILE A 174 -12.205 21.879 16.465 1.00 68.08 N ANISOU 1347 N ILE A 174 9988 7206 8675 1010 2183 153 N ATOM 1348 CA ILE A 174 -12.660 20.816 15.574 1.00 67.08 C ANISOU 1348 CA ILE A 174 9820 7199 8469 1123 2056 56 C ATOM 1349 C ILE A 174 -11.474 20.193 14.850 1.00 73.11 C ANISOU 1349 C ILE A 174 10622 8251 8905 1233 1979 84 C ATOM 1350 O ILE A 174 -11.647 19.382 13.934 1.00 81.13 O ANISOU 1350 O ILE A 174 11631 9405 9791 1361 1849 -6 O ATOM 1351 CB ILE A 174 -13.697 21.340 14.566 1.00 71.69 C ANISOU 1351 CB ILE A 174 10254 7799 9185 1177 1939 127 C ATOM 1352 CG1 ILE A 174 -13.153 22.570 13.838 1.00 70.27 C ANISOU 1352 CG1 ILE A 174 9990 7764 8946 1196 1897 372 C ATOM 1353 CG2 ILE A 174 -15.009 21.653 15.268 1.00 66.19 C ANISOU 1353 CG2 ILE A 174 9498 6833 8816 1111 2021 77 C ATOM 1354 CD1 ILE A 174 -13.904 22.919 12.574 1.00 70.96 C ANISOU 1354 CD1 ILE A 174 9921 7978 9063 1282 1745 480 C ATOM 1355 N VAL A 175 -10.259 20.571 15.253 1.00 76.79 N ANISOU 1355 N VAL A 175 11128 8818 9231 1192 2052 207 N ATOM 1356 CA VAL A 175 -9.050 20.030 14.637 1.00 78.36 C ANISOU 1356 CA VAL A 175 11335 9326 9113 1318 2011 272 C ATOM 1357 C VAL A 175 -8.619 18.720 15.288 1.00 77.60 C ANISOU 1357 C VAL A 175 11365 9198 8923 1361 2058 100 C ATOM 1358 O VAL A 175 -7.827 17.969 14.697 1.00 79.81 O ANISOU 1358 O VAL A 175 11664 9709 8949 1528 2017 87 O ATOM 1359 CB VAL A 175 -7.969 21.136 14.667 1.00 69.96 C ANISOU 1359 CB VAL A 175 10205 8409 7968 1240 2043 551 C ATOM 1360 CG1 VAL A 175 -6.549 20.578 14.713 1.00 77.19 C ANISOU 1360 CG1 VAL A 175 11136 9589 8605 1309 2076 638 C ATOM 1361 CG2 VAL A 175 -8.139 22.058 13.467 1.00 69.29 C ANISOU 1361 CG2 VAL A 175 9967 8495 7863 1292 1944 763 C ATOM 1362 N SER A 176 -9.168 18.383 16.453 1.00 74.13 N ANISOU 1362 N SER A 176 11005 8484 8678 1236 2142 -29 N ATOM 1363 CA SER A 176 -8.773 17.189 17.186 1.00 65.77 C ANISOU 1363 CA SER A 176 10054 7370 7564 1253 2188 -149 C ATOM 1364 C SER A 176 -9.544 15.938 16.766 1.00 75.16 C ANISOU 1364 C SER A 176 11290 8458 8808 1353 2082 -354 C ATOM 1365 O SER A 176 -9.602 14.977 17.543 1.00 72.60 O ANISOU 1365 O SER A 176 11049 7983 8553 1322 2115 -454 O ATOM 1366 CB SER A 176 -8.940 17.423 18.688 1.00 69.50 C ANISOU 1366 CB SER A 176 10582 7630 8195 1066 2331 -157 C ATOM 1367 OG SER A 176 -10.263 17.828 18.992 1.00 66.43 O ANISOU 1367 OG SER A 176 10157 7020 8062 982 2360 -224 O ATOM 1368 N CYS A 177 -10.129 15.920 15.565 1.00 76.08 N ANISOU 1368 N CYS A 177 11357 8651 8900 1460 1935 -408 N ATOM 1369 CA CYS A 177 -10.848 14.731 15.112 1.00 69.57 C ANISOU 1369 CA CYS A 177 10593 7712 8127 1537 1785 -619 C ATOM 1370 C CYS A 177 -11.054 14.698 13.599 1.00 77.94 C ANISOU 1370 C CYS A 177 11625 8969 9020 1705 1599 -676 C ATOM 1371 O CYS A 177 -10.169 15.102 12.838 1.00 83.44 O ANISOU 1371 O CYS A 177 12293 9970 9441 1850 1600 -574 O ATOM 1372 CB CYS A 177 -12.200 14.625 15.821 1.00 77.87 C ANISOU 1372 CB CYS A 177 11604 8466 9520 1361 1790 -674 C ATOM 1373 SG CYS A 177 -12.849 12.939 15.938 1.00 77.95 S ANISOU 1373 SG CYS A 177 11711 8234 9674 1359 1638 -888 S ATOM 1374 N GLY A 178 -12.227 14.221 13.170 1.00 92.44 N ANISOU 1374 N GLY A 178 13454 10655 11013 1678 1432 -820 N ATOM 1375 CA GLY A 178 -12.540 13.880 11.789 1.00 97.71 C ANISOU 1375 CA GLY A 178 14135 11474 11515 1831 1206 -943 C ATOM 1376 C GLY A 178 -11.978 14.756 10.685 1.00 94.32 C ANISOU 1376 C GLY A 178 13621 11421 10795 1979 1190 -797 C ATOM 1377 O GLY A 178 -11.484 14.246 9.669 1.00 98.27 O ANISOU 1377 O GLY A 178 14194 12162 10982 2202 1074 -904 O ATOM 1378 N LEU A 179 -12.067 16.076 10.865 1.00 86.82 N ANISOU 1378 N LEU A 179 10891 9625 12470 2027 3509 2009 N ATOM 1379 CA LEU A 179 -11.501 16.997 9.885 1.00 81.82 C ANISOU 1379 CA LEU A 179 10425 8963 11698 1916 3252 1779 C ATOM 1380 C LEU A 179 -10.023 16.705 9.668 1.00 78.40 C ANISOU 1380 C LEU A 179 10199 8748 10841 1731 2993 1542 C ATOM 1381 O LEU A 179 -9.577 16.498 8.533 1.00 78.83 O ANISOU 1381 O LEU A 179 10199 8823 10930 1583 2647 1447 O ATOM 1382 CB LEU A 179 -11.717 18.444 10.340 1.00 77.06 C ANISOU 1382 CB LEU A 179 10092 8266 10922 2040 3517 1677 C ATOM 1383 CG LEU A 179 -10.946 19.611 9.708 1.00 91.84 C ANISOU 1383 CG LEU A 179 12304 10117 12473 1900 3326 1408 C ATOM 1384 CD1 LEU A 179 -11.784 20.852 9.868 1.00 94.02 C ANISOU 1384 CD1 LEU A 179 12728 10168 12828 2096 3548 1421 C ATOM 1385 CD2 LEU A 179 -9.567 19.854 10.327 1.00 84.66 C ANISOU 1385 CD2 LEU A 179 11764 9427 10975 1745 3317 1180 C ATOM 1386 N SER A 180 -9.251 16.669 10.757 1.00 74.86 N ANISOU 1386 N SER A 180 9984 8474 9985 1744 3157 1451 N ATOM 1387 CA SER A 180 -7.831 16.364 10.646 1.00 79.98 C ANISOU 1387 CA SER A 180 10772 9378 10239 1591 2918 1242 C ATOM 1388 C SER A 180 -7.604 14.927 10.205 1.00 78.14 C ANISOU 1388 C SER A 180 10314 9220 10155 1581 2669 1317 C ATOM 1389 O SER A 180 -6.594 14.636 9.559 1.00 73.24 O ANISOU 1389 O SER A 180 9703 8780 9343 1474 2391 1149 O ATOM 1390 CB SER A 180 -7.130 16.630 11.975 1.00 64.69 C ANISOU 1390 CB SER A 180 9134 7593 7852 1613 3125 1154 C ATOM 1391 OG SER A 180 -7.286 17.984 12.364 1.00 84.49 O ANISOU 1391 OG SER A 180 11932 10001 10169 1618 3331 1070 O ATOM 1392 N THR A 181 -8.530 14.025 10.530 1.00 69.64 N ANISOU 1392 N THR A 181 9047 8007 9405 1690 2767 1570 N ATOM 1393 CA THR A 181 -8.434 12.654 10.041 1.00 69.56 C ANISOU 1393 CA THR A 181 8881 7999 9551 1676 2498 1661 C ATOM 1394 C THR A 181 -8.377 12.624 8.517 1.00 74.23 C ANISOU 1394 C THR A 181 9359 8521 10324 1568 2151 1591 C ATOM 1395 O THR A 181 -7.440 12.070 7.929 1.00 77.34 O ANISOU 1395 O THR A 181 9796 9054 10536 1525 1880 1444 O ATOM 1396 CB THR A 181 -9.613 11.833 10.565 1.00 75.57 C ANISOU 1396 CB THR A 181 9465 8585 10665 1750 2660 1979 C ATOM 1397 CG2 THR A 181 -9.518 10.402 10.095 1.00 53.63 C ANISOU 1397 CG2 THR A 181 6605 5762 8008 1717 2354 2080 C ATOM 1398 OG1 THR A 181 -9.612 11.855 11.999 1.00 64.71 O ANISOU 1398 OG1 THR A 181 8243 7275 9069 1843 3002 2034 O ATOM 1399 N GLY A 182 -9.355 13.249 7.857 1.00 69.12 N ANISOU 1399 N GLY A 182 8583 7661 10020 1540 2157 1688 N ATOM 1400 CA GLY A 182 -9.331 13.297 6.400 1.00 66.13 C ANISOU 1400 CA GLY A 182 8153 7182 9792 1422 1818 1622 C ATOM 1401 C GLY A 182 -8.182 14.128 5.854 1.00 73.11 C ANISOU 1401 C GLY A 182 9243 8243 10292 1302 1704 1318 C ATOM 1402 O GLY A 182 -7.553 13.760 4.851 1.00 74.98 O ANISOU 1402 O GLY A 182 9502 8538 10448 1208 1418 1196 O ATOM 1403 N LEU A 183 -7.890 15.258 6.508 1.00 73.19 N ANISOU 1403 N LEU A 183 9430 8341 10039 1291 1929 1196 N ATOM 1404 CA LEU A 183 -6.807 16.125 6.058 1.00 68.03 C ANISOU 1404 CA LEU A 183 8984 7866 8998 1119 1828 926 C ATOM 1405 C LEU A 183 -5.477 15.384 6.036 1.00 73.45 C ANISOU 1405 C LEU A 183 9676 8880 9351 1069 1678 767 C ATOM 1406 O LEU A 183 -4.702 15.516 5.084 1.00 70.94 O ANISOU 1406 O LEU A 183 9386 8701 8866 921 1470 596 O ATOM 1407 CB LEU A 183 -6.723 17.360 6.955 1.00 68.39 C ANISOU 1407 CB LEU A 183 9272 7930 8782 1112 2093 847 C ATOM 1408 CG LEU A 183 -5.710 18.433 6.559 1.00 64.56 C ANISOU 1408 CG LEU A 183 9045 7598 7886 876 1995 594 C ATOM 1409 CD1 LEU A 183 -6.327 19.401 5.565 1.00 69.95 C ANISOU 1409 CD1 LEU A 183 9828 8018 8731 786 1895 577 C ATOM 1410 CD2 LEU A 183 -5.205 19.171 7.789 1.00 68.61 C ANISOU 1410 CD2 LEU A 183 9831 8232 8006 860 2220 509 C ATOM 1411 N GLY A 184 -5.202 14.587 7.071 1.00 67.94 N ANISOU 1411 N GLY A 184 8950 8315 8547 1203 1782 824 N ATOM 1412 CA GLY A 184 -3.986 13.796 7.092 1.00 71.93 C ANISOU 1412 CA GLY A 184 9435 9129 8767 1218 1622 688 C ATOM 1413 C GLY A 184 -4.040 12.586 6.189 1.00 66.87 C ANISOU 1413 C GLY A 184 8658 8425 8326 1295 1366 739 C ATOM 1414 O GLY A 184 -3.014 12.191 5.628 1.00 64.66 O ANISOU 1414 O GLY A 184 8358 8386 7825 1288 1182 572 O ATOM 1415 N ALA A 185 -5.222 11.980 6.035 1.00 70.88 N ANISOU 1415 N ALA A 185 9075 8616 9240 1369 1349 975 N ATOM 1416 CA ALA A 185 -5.371 10.892 5.077 1.00 69.82 C ANISOU 1416 CA ALA A 185 8879 8351 9298 1408 1066 1036 C ATOM 1417 C ALA A 185 -4.946 11.333 3.685 1.00 72.87 C ANISOU 1417 C ALA A 185 9300 8761 9626 1272 857 863 C ATOM 1418 O ALA A 185 -4.345 10.557 2.933 1.00 77.43 O ANISOU 1418 O ALA A 185 9902 9409 10108 1318 634 772 O ATOM 1419 CB ALA A 185 -6.817 10.394 5.064 1.00 63.87 C ANISOU 1419 CB ALA A 185 8017 7238 9012 1428 1065 1338 C ATOM 1420 N THR A 186 -5.241 12.583 3.326 1.00 62.47 N ANISOU 1420 N THR A 186 8022 7374 8339 1115 929 813 N ATOM 1421 CA THR A 186 -4.781 13.074 2.029 1.00 70.58 C ANISOU 1421 CA THR A 186 9130 8427 9260 949 741 642 C ATOM 1422 C THR A 186 -3.331 13.552 2.082 1.00 71.02 C ANISOU 1422 C THR A 186 9246 8903 8835 853 781 373 C ATOM 1423 O THR A 186 -2.500 13.123 1.275 1.00 62.98 O ANISOU 1423 O THR A 186 8226 8069 7633 834 625 226 O ATOM 1424 CB THR A 186 -5.687 14.197 1.524 1.00 69.81 C ANISOU 1424 CB THR A 186 9090 8052 9381 811 751 701 C ATOM 1425 CG2 THR A 186 -5.175 14.718 0.190 1.00 56.40 C ANISOU 1425 CG2 THR A 186 7532 6367 7528 609 552 523 C ATOM 1426 OG1 THR A 186 -7.019 13.698 1.355 1.00 81.38 O ANISOU 1426 OG1 THR A 186 10435 9163 11324 889 675 963 O ATOM 1427 N LEU A 187 -3.009 14.431 3.033 1.00 73.74 N ANISOU 1427 N LEU A 187 9647 9411 8959 789 991 313 N ATOM 1428 CA LEU A 187 -1.711 15.102 3.031 1.00 65.74 C ANISOU 1428 CA LEU A 187 8689 8788 7500 612 1008 78 C ATOM 1429 C LEU A 187 -0.586 14.160 3.442 1.00 69.29 C ANISOU 1429 C LEU A 187 9004 9623 7700 751 964 -18 C ATOM 1430 O LEU A 187 0.472 14.126 2.802 1.00 67.06 O ANISOU 1430 O LEU A 187 8657 9666 7157 666 867 -198 O ATOM 1431 CB LEU A 187 -1.760 16.318 3.958 1.00 71.29 C ANISOU 1431 CB LEU A 187 9553 9501 8033 488 1211 59 C ATOM 1432 CG LEU A 187 -1.725 17.691 3.288 1.00 62.37 C ANISOU 1432 CG LEU A 187 8629 8301 6769 201 1192 -50 C ATOM 1433 CD1 LEU A 187 -2.790 17.771 2.223 1.00 63.56 C ANISOU 1433 CD1 LEU A 187 8806 8059 7286 204 1071 50 C ATOM 1434 CD2 LEU A 187 -1.937 18.781 4.318 1.00 80.92 C ANISOU 1434 CD2 LEU A 187 11203 10576 8968 141 1391 -40 C ATOM 1435 N ASN A 188 -0.787 13.394 4.515 1.00 73.29 N ANISOU 1435 N ASN A 188 9466 10108 8271 973 1038 103 N ATOM 1436 CA ASN A 188 0.283 12.571 5.067 1.00 65.40 C ANISOU 1436 CA ASN A 188 8369 9464 7016 1132 983 16 C ATOM 1437 C ASN A 188 0.404 11.211 4.398 1.00 69.81 C ANISOU 1437 C ASN A 188 8844 9996 7683 1363 787 29 C ATOM 1438 O ASN A 188 1.520 10.695 4.259 1.00 67.37 O ANISOU 1438 O ASN A 188 8434 10042 7123 1476 688 -122 O ATOM 1439 CB ASN A 188 0.070 12.367 6.571 1.00 64.09 C ANISOU 1439 CB ASN A 188 8265 9270 6817 1261 1134 135 C ATOM 1440 CG ASN A 188 0.044 13.674 7.340 1.00 64.75 C ANISOU 1440 CG ASN A 188 8499 9377 6725 1065 1330 109 C ATOM 1441 ND2 ASN A 188 -0.891 13.790 8.276 1.00 69.18 N ANISOU 1441 ND2 ASN A 188 9181 9670 7436 1145 1526 280 N ATOM 1442 OD1 ASN A 188 0.856 14.566 7.099 1.00 70.01 O ANISOU 1442 OD1 ASN A 188 9193 10298 7108 838 1308 -59 O ATOM 1443 N VAL A 189 -0.712 10.624 3.973 1.00 63.76 N ANISOU 1443 N VAL A 189 8126 8822 7279 1439 716 208 N ATOM 1444 CA VAL A 189 -0.751 9.241 3.496 1.00 68.03 C ANISOU 1444 CA VAL A 189 8677 9247 7926 1666 512 259 C ATOM 1445 C VAL A 189 -0.871 9.181 1.973 1.00 62.87 C ANISOU 1445 C VAL A 189 8068 8455 7364 1590 333 198 C ATOM 1446 O VAL A 189 0.004 8.643 1.295 1.00 72.02 O ANISOU 1446 O VAL A 189 9222 9820 8320 1706 207 39 O ATOM 1447 CB VAL A 189 -1.889 8.449 4.179 1.00 65.37 C ANISOU 1447 CB VAL A 189 8395 8543 7901 1781 523 533 C ATOM 1448 CG1 VAL A 189 -1.672 6.948 4.029 1.00 61.03 C ANISOU 1448 CG1 VAL A 189 7922 7923 7342 2033 304 570 C ATOM 1449 CG2 VAL A 189 -1.999 8.839 5.647 1.00 61.60 C ANISOU 1449 CG2 VAL A 189 7918 8139 7347 1785 764 609 C ATOM 1450 N ALA A 190 -1.959 9.721 1.418 1.00 69.22 N ANISOU 1450 N ALA A 190 8927 8906 8469 1414 317 326 N ATOM 1451 CA ALA A 190 -2.131 9.695 -0.035 1.00 59.03 C ANISOU 1451 CA ALA A 190 7732 7438 7260 1319 121 280 C ATOM 1452 C ALA A 190 -1.011 10.452 -0.733 1.00 67.26 C ANISOU 1452 C ALA A 190 8773 8834 7949 1175 151 15 C ATOM 1453 O ALA A 190 -0.470 9.981 -1.740 1.00 63.77 O ANISOU 1453 O ALA A 190 8396 8461 7372 1223 14 -109 O ATOM 1454 CB ALA A 190 -3.493 10.278 -0.422 1.00 50.87 C ANISOU 1454 CB ALA A 190 6738 5980 6612 1146 85 470 C ATOM 1455 N LYS A 191 -0.643 11.614 -0.199 1.00 68.37 N ANISOU 1455 N LYS A 191 8863 9201 7915 988 335 -70 N ATOM 1456 CA LYS A 191 0.423 12.447 -0.746 1.00 61.36 C ANISOU 1456 CA LYS A 191 7964 8677 6671 776 380 -300 C ATOM 1457 C LYS A 191 0.273 12.675 -2.251 1.00 67.95 C ANISOU 1457 C LYS A 191 8947 9343 7528 614 238 -364 C ATOM 1458 O LYS A 191 1.145 12.272 -3.036 1.00 68.89 O ANISOU 1458 O LYS A 191 9053 9709 7413 649 183 -523 O ATOM 1459 CB LYS A 191 1.784 11.847 -0.424 1.00 54.28 C ANISOU 1459 CB LYS A 191 6896 8289 5438 940 405 -464 C ATOM 1460 CG LYS A 191 2.100 11.802 1.063 1.00 63.85 C ANISOU 1460 CG LYS A 191 7997 9709 6555 1046 526 -427 C ATOM 1461 CD LYS A 191 3.526 11.346 1.316 1.00 64.60 C ANISOU 1461 CD LYS A 191 7890 10348 6306 1187 518 -600 C ATOM 1462 CE LYS A 191 3.694 9.869 1.003 1.00 73.74 C ANISOU 1462 CE LYS A 191 9025 11478 7517 1575 370 -598 C ATOM 1463 NZ LYS A 191 5.123 9.454 1.055 1.00 62.62 N1+ ANISOU 1463 NZ LYS A 191 7388 10627 5776 1755 356 -787 N1+ ATOM 1464 N PRO A 192 -0.813 13.307 -2.694 1.00 70.87 N ANISOU 1464 N PRO A 192 9468 9296 8165 451 176 -243 N ATOM 1465 CA PRO A 192 -0.978 13.554 -4.128 1.00 69.69 C ANISOU 1465 CA PRO A 192 9510 8949 8021 279 10 -297 C ATOM 1466 C PRO A 192 -0.085 14.692 -4.592 1.00 67.80 C ANISOU 1466 C PRO A 192 9344 9009 7407 -35 99 -501 C ATOM 1467 O PRO A 192 0.018 15.736 -3.943 1.00 76.31 O ANISOU 1467 O PRO A 192 10428 10192 8374 -218 235 -523 O ATOM 1468 CB PRO A 192 -2.461 13.923 -4.255 1.00 63.07 C ANISOU 1468 CB PRO A 192 8775 7582 7607 222 -96 -80 C ATOM 1469 CG PRO A 192 -2.796 14.537 -2.947 1.00 62.70 C ANISOU 1469 CG PRO A 192 8616 7572 7633 244 113 5 C ATOM 1470 CD PRO A 192 -1.939 13.850 -1.911 1.00 54.28 C ANISOU 1470 CD PRO A 192 7374 6889 6363 434 256 -52 C ATOM 1471 N LYS A 193 0.576 14.475 -5.724 1.00 74.14 N ANISOU 1471 N LYS A 193 9815 10469 7886 732 343 1842 N ATOM 1472 CA LYS A 193 1.399 15.519 -6.303 1.00 73.44 C ANISOU 1472 CA LYS A 193 9760 10408 7734 608 420 1954 C ATOM 1473 C LYS A 193 0.519 16.562 -6.986 1.00 79.82 C ANISOU 1473 C LYS A 193 10740 11085 8502 731 554 2057 C ATOM 1474 O LYS A 193 -0.665 16.337 -7.251 1.00 86.27 O ANISOU 1474 O LYS A 193 11549 11876 9354 960 550 2024 O ATOM 1475 CB LYS A 193 2.405 14.924 -7.289 1.00 63.85 C ANISOU 1475 CB LYS A 193 8278 9481 6499 629 380 1951 C ATOM 1476 CG LYS A 193 3.421 13.998 -6.632 1.00 87.34 C ANISOU 1476 CG LYS A 193 11062 12575 9550 543 222 1853 C ATOM 1477 CD LYS A 193 4.288 13.289 -7.658 1.00 86.33 C ANISOU 1477 CD LYS A 193 10626 12735 9440 627 209 1802 C ATOM 1478 CE LYS A 193 5.270 12.336 -6.989 1.00 86.18 C ANISOU 1478 CE LYS A 193 10392 12813 9538 609 17 1697 C ATOM 1479 NZ LYS A 193 6.268 13.051 -6.147 1.00 99.35 N1+ ANISOU 1479 NZ LYS A 193 12053 14463 11235 338 -45 1718 N1+ ATOM 1480 N LYS A 194 1.111 17.725 -7.253 1.00 76.70 N ANISOU 1480 N LYS A 194 10502 10595 8046 574 661 2182 N ATOM 1481 CA LYS A 194 0.360 18.820 -7.852 1.00 71.29 C ANISOU 1481 CA LYS A 194 10049 9720 7317 701 770 2316 C ATOM 1482 C LYS A 194 -0.169 18.420 -9.224 1.00 71.86 C ANISOU 1482 C LYS A 194 10009 9990 7303 979 725 2376 C ATOM 1483 O LYS A 194 0.529 17.785 -10.018 1.00 67.60 O ANISOU 1483 O LYS A 194 9287 9720 6678 962 703 2374 O ATOM 1484 CB LYS A 194 1.236 20.070 -7.966 1.00 69.92 C ANISOU 1484 CB LYS A 194 10096 9388 7081 437 907 2453 C ATOM 1485 CG LYS A 194 0.449 21.363 -8.133 1.00 81.75 C ANISOU 1485 CG LYS A 194 11946 10544 8570 542 1017 2587 C ATOM 1486 CD LYS A 194 1.308 22.486 -8.701 1.00 83.51 C ANISOU 1486 CD LYS A 194 12405 10630 8696 302 1169 2772 C ATOM 1487 CE LYS A 194 0.557 23.812 -8.697 1.00 93.07 C ANISOU 1487 CE LYS A 194 14030 11410 9923 409 1268 2904 C ATOM 1488 NZ LYS A 194 1.402 24.935 -8.201 1.00 95.86 N1+ ANISOU 1488 NZ LYS A 194 14668 11467 10288 20 1427 2948 N1+ ATOM 1489 N GLY A 195 -1.422 18.781 -9.491 1.00 77.59 N ANISOU 1489 N GLY A 195 10834 10592 8054 1247 703 2407 N ATOM 1490 CA GLY A 195 -2.058 18.480 -10.755 1.00 73.79 C ANISOU 1490 CA GLY A 195 10273 10294 7472 1529 607 2456 C ATOM 1491 C GLY A 195 -2.658 17.096 -10.870 1.00 76.95 C ANISOU 1491 C GLY A 195 10368 10930 7938 1685 467 2260 C ATOM 1492 O GLY A 195 -3.287 16.798 -11.893 1.00 75.94 O ANISOU 1492 O GLY A 195 10160 10967 7726 1918 354 2260 O ATOM 1493 N GLN A 196 -2.490 16.242 -9.864 1.00 72.39 N ANISOU 1493 N GLN A 196 9649 10362 7494 1555 459 2096 N ATOM 1494 CA GLN A 196 -3.029 14.893 -9.922 1.00 72.27 C ANISOU 1494 CA GLN A 196 9387 10517 7556 1663 348 1911 C ATOM 1495 C GLN A 196 -4.527 14.900 -9.623 1.00 82.70 C ANISOU 1495 C GLN A 196 10657 11743 9023 1844 326 1810 C ATOM 1496 O GLN A 196 -5.110 15.916 -9.237 1.00 87.55 O ANISOU 1496 O GLN A 196 11417 12149 9699 1905 400 1868 O ATOM 1497 CB GLN A 196 -2.288 13.979 -8.947 1.00 70.91 C ANISOU 1497 CB GLN A 196 9135 10347 7459 1465 341 1804 C ATOM 1498 CG GLN A 196 -0.818 13.778 -9.285 1.00 71.49 C ANISOU 1498 CG GLN A 196 9145 10572 7446 1326 336 1849 C ATOM 1499 CD GLN A 196 -0.218 12.562 -8.605 1.00 73.47 C ANISOU 1499 CD GLN A 196 9255 10873 7785 1250 246 1722 C ATOM 1500 NE2 GLN A 196 0.456 11.723 -9.382 1.00 85.71 N ANISOU 1500 NE2 GLN A 196 10613 12640 9312 1315 194 1654 N ATOM 1501 OE1 GLN A 196 -0.359 12.380 -7.395 1.00 73.98 O ANISOU 1501 OE1 GLN A 196 9409 10773 7927 1146 226 1686 O ATOM 1502 N SER A 197 -5.153 13.741 -9.811 1.00 78.82 N ANISOU 1502 N SER A 197 9939 11400 8610 1926 234 1634 N ATOM 1503 CA SER A 197 -6.581 13.573 -9.585 1.00 75.65 C ANISOU 1503 CA SER A 197 9396 10965 8381 2067 219 1489 C ATOM 1504 C SER A 197 -6.815 12.733 -8.337 1.00 70.51 C ANISOU 1504 C SER A 197 8701 10207 7882 1881 320 1332 C ATOM 1505 O SER A 197 -6.100 11.756 -8.090 1.00 69.24 O ANISOU 1505 O SER A 197 8528 10088 7691 1735 292 1290 O ATOM 1506 CB SER A 197 -7.257 12.920 -10.794 1.00 69.30 C ANISOU 1506 CB SER A 197 8366 10411 7553 2270 36 1384 C ATOM 1507 OG SER A 197 -6.830 11.579 -10.953 1.00 68.21 O ANISOU 1507 OG SER A 197 8100 10412 7404 2165 -16 1245 O ATOM 1508 N VAL A 198 -7.819 13.120 -7.552 1.00 70.75 N ANISOU 1508 N VAL A 198 8725 10088 8068 1896 447 1247 N ATOM 1509 CA VAL A 198 -8.118 12.480 -6.277 1.00 69.95 C ANISOU 1509 CA VAL A 198 8652 9856 8069 1688 601 1117 C ATOM 1510 C VAL A 198 -9.604 12.157 -6.233 1.00 69.96 C ANISOU 1510 C VAL A 198 8397 9896 8287 1778 669 910 C ATOM 1511 O VAL A 198 -10.443 13.049 -6.405 1.00 72.68 O ANISOU 1511 O VAL A 198 8655 10217 8745 1974 707 883 O ATOM 1512 CB VAL A 198 -7.728 13.364 -5.080 1.00 63.18 C ANISOU 1512 CB VAL A 198 8088 8756 7161 1530 775 1191 C ATOM 1513 CG1 VAL A 198 -8.074 12.666 -3.774 1.00 54.03 C ANISOU 1513 CG1 VAL A 198 7012 7473 6043 1305 943 1065 C ATOM 1514 CG2 VAL A 198 -6.248 13.710 -5.129 1.00 64.69 C ANISOU 1514 CG2 VAL A 198 8476 8933 7168 1410 692 1368 C ATOM 1515 N ALA A 199 -9.925 10.888 -6.006 1.00 71.86 N ANISOU 1515 N ALA A 199 8510 10187 8607 1638 687 756 N ATOM 1516 CA ALA A 199 -11.289 10.451 -5.748 1.00 65.88 C ANISOU 1516 CA ALA A 199 7497 9455 8081 1620 810 526 C ATOM 1517 C ALA A 199 -11.498 10.329 -4.244 1.00 59.90 C ANISOU 1517 C ALA A 199 6927 8481 7353 1356 1111 472 C ATOM 1518 O ALA A 199 -10.604 9.886 -3.518 1.00 78.11 O ANISOU 1518 O ALA A 199 9524 10658 9496 1146 1140 574 O ATOM 1519 CB ALA A 199 -11.581 9.115 -6.432 1.00 64.95 C ANISOU 1519 CB ALA A 199 7148 9497 8034 1576 675 370 C ATOM 1520 N ILE A 200 -12.674 10.737 -3.775 1.00 69.46 N ANISOU 1520 N ILE A 200 7972 9659 8758 1378 1331 304 N ATOM 1521 CA ILE A 200 -12.978 10.756 -2.349 1.00 71.02 C ANISOU 1521 CA ILE A 200 8368 9662 8955 1127 1677 231 C ATOM 1522 C ILE A 200 -14.346 10.128 -2.138 1.00 69.71 C ANISOU 1522 C ILE A 200 7866 9566 9055 1030 1896 -44 C ATOM 1523 O ILE A 200 -15.341 10.588 -2.713 1.00 77.49 O ANISOU 1523 O ILE A 200 8461 10694 10287 1258 1883 -203 O ATOM 1524 CB ILE A 200 -12.937 12.179 -1.773 1.00 68.89 C ANISOU 1524 CB ILE A 200 8292 9239 8645 1226 1829 283 C ATOM 1525 CG1 ILE A 200 -11.511 12.720 -1.843 1.00 72.63 C ANISOU 1525 CG1 ILE A 200 9114 9627 8856 1223 1644 538 C ATOM 1526 CG2 ILE A 200 -13.450 12.191 -0.340 1.00 62.54 C ANISOU 1526 CG2 ILE A 200 7664 8263 7834 973 2228 146 C ATOM 1527 CD1 ILE A 200 -11.375 14.114 -1.350 1.00 71.95 C ANISOU 1527 CD1 ILE A 200 9258 9358 8723 1291 1771 586 C ATOM 1528 N PHE A 201 -14.396 9.085 -1.315 1.00 64.91 N ANISOU 1528 N PHE A 201 7409 8854 8401 688 2092 -100 N ATOM 1529 CA PHE A 201 -15.632 8.375 -1.017 1.00 66.28 C ANISOU 1529 CA PHE A 201 7294 9071 8818 496 2361 -365 C ATOM 1530 C PHE A 201 -16.168 8.870 0.320 1.00 74.16 C ANISOU 1530 C PHE A 201 8457 9915 9806 307 2817 -461 C ATOM 1531 O PHE A 201 -15.496 8.742 1.348 1.00 72.62 O ANISOU 1531 O PHE A 201 8748 9515 9329 68 2960 -323 O ATOM 1532 CB PHE A 201 -15.397 6.865 -0.988 1.00 70.72 C ANISOU 1532 CB PHE A 201 7962 9575 9334 208 2325 -366 C ATOM 1533 CG PHE A 201 -15.146 6.266 -2.344 1.00 73.69 C ANISOU 1533 CG PHE A 201 8100 10125 9774 377 1941 -376 C ATOM 1534 CD1 PHE A 201 -13.958 6.507 -3.015 1.00 72.43 C ANISOU 1534 CD1 PHE A 201 8112 9997 9411 587 1608 -157 C ATOM 1535 CD2 PHE A 201 -16.101 5.468 -2.951 1.00 72.39 C ANISOU 1535 CD2 PHE A 201 7534 10103 9869 302 1929 -630 C ATOM 1536 CE1 PHE A 201 -13.725 5.963 -4.263 1.00 71.25 C ANISOU 1536 CE1 PHE A 201 7770 10016 9286 736 1293 -188 C ATOM 1537 CE2 PHE A 201 -15.874 4.919 -4.200 1.00 78.09 C ANISOU 1537 CE2 PHE A 201 8070 10986 10613 447 1574 -669 C ATOM 1538 CZ PHE A 201 -14.684 5.168 -4.857 1.00 73.45 C ANISOU 1538 CZ PHE A 201 7689 10427 9791 672 1267 -446 C ATOM 1539 N GLY A 202 -17.371 9.439 0.300 1.00 80.58 N ANISOU 1539 N GLY A 202 8864 10836 10917 428 3035 -711 N ATOM 1540 CA GLY A 202 -17.950 10.028 1.491 1.00 82.05 C ANISOU 1540 CA GLY A 202 9161 10896 11116 294 3507 -851 C ATOM 1541 C GLY A 202 -17.705 11.519 1.571 1.00 86.28 C ANISOU 1541 C GLY A 202 9816 11353 11612 608 3486 -789 C ATOM 1542 O GLY A 202 -16.558 11.969 1.497 1.00 81.11 O ANISOU 1542 O GLY A 202 9543 10588 10688 681 3244 -532 O ATOM 1543 N LEU A 203 -18.772 12.297 1.720 1.00 94.21 N ANISOU 1543 N LEU A 203 10486 12403 12907 793 3743 -1038 N ATOM 1544 CA LEU A 203 -18.686 13.751 1.752 1.00 92.00 C ANISOU 1544 CA LEU A 203 10301 12004 12650 1130 3741 -1013 C ATOM 1545 C LEU A 203 -19.160 14.300 3.092 1.00 93.19 C ANISOU 1545 C LEU A 203 10646 11982 12777 972 4285 -1215 C ATOM 1546 O LEU A 203 -19.826 15.336 3.163 1.00 96.34 O ANISOU 1546 O LEU A 203 10854 12337 13413 1266 4453 -1393 O ATOM 1547 CB LEU A 203 -19.468 14.366 0.594 1.00 91.03 C ANISOU 1547 CB LEU A 203 9628 12059 12901 1616 3489 -1115 C ATOM 1548 CG LEU A 203 -18.806 14.164 -0.771 1.00 86.69 C ANISOU 1548 CG LEU A 203 9025 11644 12270 1829 2926 -871 C ATOM 1549 CD1 LEU A 203 -19.564 14.902 -1.863 1.00 93.24 C ANISOU 1549 CD1 LEU A 203 9399 12623 13403 2338 2649 -940 C ATOM 1550 CD2 LEU A 203 -17.347 14.602 -0.733 1.00 80.62 C ANISOU 1550 CD2 LEU A 203 8834 10683 11116 1791 2737 -535 C ATOM 1551 N GLY A 204 -18.823 13.601 4.170 1.00 97.46 N ANISOU 1551 N GLY A 204 11597 12415 13020 515 4568 -1191 N ATOM 1552 CA GLY A 204 -18.988 14.112 5.513 1.00 73.61 C ANISOU 1552 CA GLY A 204 8936 9208 9826 309 5061 -1332 C ATOM 1553 C GLY A 204 -17.791 14.945 5.920 1.00 78.26 C ANISOU 1553 C GLY A 204 10123 9568 10043 327 4900 -1110 C ATOM 1554 O GLY A 204 -16.978 15.358 5.090 1.00 76.47 O ANISOU 1554 O GLY A 204 9946 9331 9780 563 4450 -880 O ATOM 1555 N ALA A 205 -17.677 15.183 7.229 1.00 80.19 N ANISOU 1555 N ALA A 205 10841 9638 9991 40 5286 -1194 N ATOM 1556 CA ALA A 205 -16.572 15.994 7.734 1.00 77.99 C ANISOU 1556 CA ALA A 205 11139 9143 9349 6 5150 -1034 C ATOM 1557 C ALA A 205 -15.222 15.371 7.395 1.00 84.00 C ANISOU 1557 C ALA A 205 12185 9917 9813 -121 4650 -677 C ATOM 1558 O ALA A 205 -14.264 16.084 7.078 1.00 85.95 O ANISOU 1558 O ALA A 205 12634 10078 9944 8 4329 -503 O ATOM 1559 CB ALA A 205 -16.711 16.194 9.243 1.00 75.43 C ANISOU 1559 CB ALA A 205 11302 8658 8699 -331 5645 -1207 C ATOM 1560 N VAL A 206 -15.132 14.040 7.436 1.00 87.30 N ANISOU 1560 N VAL A 206 12607 10432 10130 -369 4589 -576 N ATOM 1561 CA VAL A 206 -13.874 13.367 7.121 1.00 75.78 C ANISOU 1561 CA VAL A 206 11381 8985 8428 -453 4122 -262 C ATOM 1562 C VAL A 206 -13.571 13.473 5.630 1.00 75.44 C ANISOU 1562 C VAL A 206 10928 9087 8648 -105 3687 -137 C ATOM 1563 O VAL A 206 -12.447 13.802 5.226 1.00 80.17 O ANISOU 1563 O VAL A 206 11686 9667 9107 -20 3322 74 O ATOM 1564 CB VAL A 206 -13.920 11.900 7.584 1.00 72.72 C ANISOU 1564 CB VAL A 206 11143 8606 7881 -787 4193 -195 C ATOM 1565 CG1 VAL A 206 -12.660 11.167 7.154 1.00 66.95 C ANISOU 1565 CG1 VAL A 206 10583 7886 6970 -796 3688 106 C ATOM 1566 CG2 VAL A 206 -14.104 11.823 9.093 1.00 67.49 C ANISOU 1566 CG2 VAL A 206 10996 7787 6860 -1158 4612 -274 C ATOM 1567 N GLY A 207 -14.567 13.188 4.789 1.00 78.03 N ANISOU 1567 N GLY A 207 10720 9579 9350 83 3724 -279 N ATOM 1568 CA GLY A 207 -14.365 13.315 3.356 1.00 73.39 C ANISOU 1568 CA GLY A 207 9773 9144 8968 418 3319 -174 C ATOM 1569 C GLY A 207 -14.100 14.746 2.931 1.00 77.45 C ANISOU 1569 C GLY A 207 10314 9579 9534 730 3200 -123 C ATOM 1570 O GLY A 207 -13.300 14.998 2.027 1.00 73.19 O ANISOU 1570 O GLY A 207 9774 9084 8952 900 2835 81 O ATOM 1571 N LEU A 208 -14.754 15.706 3.588 1.00 82.62 N ANISOU 1571 N LEU A 208 11021 10095 10276 798 3534 -311 N ATOM 1572 CA LEU A 208 -14.499 17.106 3.269 1.00 78.06 C ANISOU 1572 CA LEU A 208 10547 9365 9749 1084 3446 -262 C ATOM 1573 C LEU A 208 -13.125 17.550 3.753 1.00 77.83 C ANISOU 1573 C LEU A 208 11053 9161 9357 884 3306 -63 C ATOM 1574 O LEU A 208 -12.492 18.397 3.117 1.00 72.45 O ANISOU 1574 O LEU A 208 10460 8396 8672 1061 3074 91 O ATOM 1575 CB LEU A 208 -15.594 17.991 3.861 1.00 80.00 C ANISOU 1575 CB LEU A 208 10700 9480 10216 1236 3856 -553 C ATOM 1576 CG LEU A 208 -16.947 17.841 3.163 1.00 68.12 C ANISOU 1576 CG LEU A 208 8561 8166 9156 1544 3916 -759 C ATOM 1577 CD1 LEU A 208 -18.033 18.593 3.910 1.00 72.98 C ANISOU 1577 CD1 LEU A 208 9054 8666 10009 1669 4384 -1095 C ATOM 1578 CD2 LEU A 208 -16.864 18.295 1.714 1.00 69.71 C ANISOU 1578 CD2 LEU A 208 8501 8449 9537 1970 3469 -589 C ATOM 1579 N GLY A 209 -12.639 16.987 4.862 1.00 71.29 N ANISOU 1579 N GLY A 209 10593 8278 8217 504 3431 -60 N ATOM 1580 CA GLY A 209 -11.261 17.238 5.253 1.00 75.18 C ANISOU 1580 CA GLY A 209 11527 8667 8373 304 3210 127 C ATOM 1581 C GLY A 209 -10.273 16.670 4.254 1.00 74.31 C ANISOU 1581 C GLY A 209 11288 8714 8232 353 2763 386 C ATOM 1582 O GLY A 209 -9.256 17.295 3.944 1.00 80.70 O ANISOU 1582 O GLY A 209 12251 9473 8940 362 2529 538 O ATOM 1583 N ALA A 210 -10.567 15.479 3.726 1.00 76.86 N ANISOU 1583 N ALA A 210 11322 9229 8654 370 2664 415 N ATOM 1584 CA ALA A 210 -9.736 14.913 2.668 1.00 77.53 C ANISOU 1584 CA ALA A 210 11243 9475 8742 460 2274 616 C ATOM 1585 C ALA A 210 -9.766 15.785 1.417 1.00 63.83 C ANISOU 1585 C ALA A 210 9270 7790 7191 787 2114 683 C ATOM 1586 O ALA A 210 -8.749 15.937 0.728 1.00 70.99 O ANISOU 1586 O ALA A 210 10206 8753 8013 823 1843 866 O ATOM 1587 CB ALA A 210 -10.195 13.491 2.345 1.00 70.46 C ANISOU 1587 CB ALA A 210 10096 8735 7939 421 2238 584 C ATOM 1588 N ALA A 211 -10.927 16.369 1.110 1.00 74.59 N ANISOU 1588 N ALA A 211 10400 9134 8806 1031 2281 536 N ATOM 1589 CA ALA A 211 -11.031 17.264 -0.039 1.00 70.57 C ANISOU 1589 CA ALA A 211 9731 8635 8447 1372 2114 624 C ATOM 1590 C ALA A 211 -10.232 18.541 0.180 1.00 65.60 C ANISOU 1590 C ALA A 211 9469 7766 7690 1352 2112 738 C ATOM 1591 O ALA A 211 -9.557 19.024 -0.736 1.00 65.96 O ANISOU 1591 O ALA A 211 9544 7820 7697 1465 1890 932 O ATOM 1592 CB ALA A 211 -12.497 17.589 -0.322 1.00 81.50 C ANISOU 1592 CB ALA A 211 10772 10045 10150 1672 2265 426 C ATOM 1593 N GLU A 212 -10.310 19.109 1.384 1.00 64.47 N ANISOU 1593 N GLU A 212 9626 7399 7469 1185 2379 606 N ATOM 1594 CA GLU A 212 -9.488 20.267 1.716 1.00 78.67 C ANISOU 1594 CA GLU A 212 11813 8946 9132 1092 2383 679 C ATOM 1595 C GLU A 212 -8.007 19.931 1.606 1.00 77.69 C ANISOU 1595 C GLU A 212 11849 8908 8763 832 2115 881 C ATOM 1596 O GLU A 212 -7.206 20.752 1.143 1.00 71.86 O ANISOU 1596 O GLU A 212 11258 8067 7980 823 1991 1023 O ATOM 1597 CB GLU A 212 -9.831 20.760 3.121 1.00 77.41 C ANISOU 1597 CB GLU A 212 11966 8557 8889 913 2722 456 C ATOM 1598 CG GLU A 212 -8.998 21.937 3.596 1.00 82.01 C ANISOU 1598 CG GLU A 212 12986 8855 9319 761 2740 479 C ATOM 1599 CD GLU A 212 -9.430 23.251 2.976 1.00 91.91 C ANISOU 1599 CD GLU A 212 14268 9850 10802 1083 2801 481 C ATOM 1600 OE1 GLU A 212 -10.453 23.271 2.257 1.00 93.99 O ANISOU 1600 OE1 GLU A 212 14202 10169 11342 1459 2826 451 O ATOM 1601 OE2 GLU A 212 -8.746 24.268 3.212 1.00 97.77 O1- ANISOU 1601 OE2 GLU A 212 15373 10321 11452 961 2810 511 O1- ATOM 1602 N GLY A 213 -7.628 18.720 2.017 1.00 76.59 N ANISOU 1602 N GLY A 213 11673 8946 8480 622 2026 892 N ATOM 1603 CA GLY A 213 -6.249 18.293 1.851 1.00 70.07 C ANISOU 1603 CA GLY A 213 10912 8237 7473 434 1744 1063 C ATOM 1604 C GLY A 213 -5.837 18.223 0.394 1.00 69.79 C ANISOU 1604 C GLY A 213 10610 8372 7536 629 1518 1233 C ATOM 1605 O GLY A 213 -4.775 18.717 0.009 1.00 67.03 O ANISOU 1605 O GLY A 213 10340 8020 7106 541 1376 1367 O ATOM 1606 N ALA A 214 -6.677 17.605 -0.440 1.00 64.62 N ANISOU 1606 N ALA A 214 9632 7876 7043 872 1493 1213 N ATOM 1607 CA ALA A 214 -6.375 17.525 -1.866 1.00 64.44 C ANISOU 1607 CA ALA A 214 9387 8030 7068 1066 1287 1358 C ATOM 1608 C ALA A 214 -6.290 18.908 -2.498 1.00 72.12 C ANISOU 1608 C ALA A 214 10489 8844 8069 1210 1302 1473 C ATOM 1609 O ALA A 214 -5.486 19.126 -3.412 1.00 77.65 O ANISOU 1609 O ALA A 214 11182 9627 8693 1221 1159 1643 O ATOM 1610 CB ALA A 214 -7.424 16.673 -2.581 1.00 66.96 C ANISOU 1610 CB ALA A 214 9357 8538 7546 1293 1249 1274 C ATOM 1611 N ARG A 215 -7.105 19.852 -2.024 1.00 71.95 N ANISOU 1611 N ARG A 215 10606 8576 8157 1321 1495 1379 N ATOM 1612 CA ARG A 215 -7.021 21.226 -2.509 1.00 72.12 C ANISOU 1612 CA ARG A 215 10832 8359 8211 1457 1520 1497 C ATOM 1613 C ARG A 215 -5.699 21.869 -2.107 1.00 70.37 C ANISOU 1613 C ARG A 215 10933 7987 7818 1128 1519 1593 C ATOM 1614 O ARG A 215 -5.036 22.517 -2.926 1.00 74.70 O ANISOU 1614 O ARG A 215 11584 8485 8316 1125 1442 1780 O ATOM 1615 CB ARG A 215 -8.201 22.041 -1.975 1.00 73.67 C ANISOU 1615 CB ARG A 215 11102 8295 8595 1670 1742 1334 C ATOM 1616 CG ARG A 215 -8.254 23.478 -2.474 1.00 83.98 C ANISOU 1616 CG ARG A 215 12655 9285 9969 1873 1765 1455 C ATOM 1617 CD ARG A 215 -9.338 24.267 -1.753 1.00 83.02 C ANISOU 1617 CD ARG A 215 12620 8871 10054 2079 2012 1246 C ATOM 1618 NE ARG A 215 -9.014 24.503 -0.351 1.00 84.39 N ANISOU 1618 NE ARG A 215 13084 8853 10128 1750 2249 1061 N ATOM 1619 CZ ARG A 215 -8.233 25.483 0.082 1.00 92.11 C ANISOU 1619 CZ ARG A 215 14480 9520 10996 1535 2320 1093 C ATOM 1620 NH1 ARG A 215 -7.683 26.349 -0.753 1.00 86.69 N1+ ANISOU 1620 NH1 ARG A 215 13987 8649 10304 1594 2209 1318 N1+ ATOM 1621 NH2 ARG A 215 -8.000 25.599 1.387 1.00 93.53 N ANISOU 1621 NH2 ARG A 215 14917 9567 11052 1229 2513 891 N ATOM 1622 N ILE A 216 -5.304 21.701 -0.843 1.00 78.33 N ANISOU 1622 N ILE A 216 11364 9922 8476 972 11 1113 N ATOM 1623 CA ILE A 216 -4.045 22.270 -0.365 1.00 73.85 C ANISOU 1623 CA ILE A 216 10829 9354 7878 810 -66 1239 C ATOM 1624 C ILE A 216 -2.866 21.677 -1.128 1.00 73.01 C ANISOU 1624 C ILE A 216 10547 9217 7976 727 20 1337 C ATOM 1625 O ILE A 216 -1.890 22.373 -1.435 1.00 76.60 O ANISOU 1625 O ILE A 216 11043 9633 8430 595 9 1386 O ATOM 1626 CB ILE A 216 -3.911 22.054 1.155 1.00 74.61 C ANISOU 1626 CB ILE A 216 10853 9577 7917 774 -156 1350 C ATOM 1627 CG1 ILE A 216 -4.934 22.909 1.906 1.00 72.38 C ANISOU 1627 CG1 ILE A 216 10771 9357 7374 865 -231 1217 C ATOM 1628 CG2 ILE A 216 -2.503 22.371 1.632 1.00 67.16 C ANISOU 1628 CG2 ILE A 216 9855 8655 7007 615 -274 1459 C ATOM 1629 CD1 ILE A 216 -5.194 22.446 3.322 1.00 59.28 C ANISOU 1629 CD1 ILE A 216 9038 7889 5598 904 -249 1322 C ATOM 1630 N ALA A 217 -2.946 20.389 -1.466 1.00 72.45 N ANISOU 1630 N ALA A 217 10262 9153 8113 802 118 1354 N ATOM 1631 CA ALA A 217 -1.866 19.720 -2.181 1.00 76.46 C ANISOU 1631 CA ALA A 217 10577 9649 8824 773 210 1407 C ATOM 1632 C ALA A 217 -1.787 20.118 -3.648 1.00 65.30 C ANISOU 1632 C ALA A 217 9269 8210 7332 824 324 1288 C ATOM 1633 O ALA A 217 -0.843 19.708 -4.332 1.00 83.36 O ANISOU 1633 O ALA A 217 11406 10526 9742 811 437 1315 O ATOM 1634 CB ALA A 217 -2.023 18.202 -2.067 1.00 65.73 C ANISOU 1634 CB ALA A 217 8975 8258 7740 865 260 1435 C ATOM 1635 N GLY A 218 -2.743 20.898 -4.146 1.00 72.34 N ANISOU 1635 N GLY A 218 10412 9070 8004 908 303 1162 N ATOM 1636 CA GLY A 218 -2.707 21.338 -5.525 1.00 74.86 C ANISOU 1636 CA GLY A 218 10882 9387 8175 989 401 1087 C ATOM 1637 C GLY A 218 -3.284 20.366 -6.526 1.00 79.54 C ANISOU 1637 C GLY A 218 11392 10018 8813 1196 460 890 C ATOM 1638 O GLY A 218 -2.930 20.432 -7.707 1.00 77.89 O ANISOU 1638 O GLY A 218 11244 9866 8485 1282 573 841 O ATOM 1639 N ALA A 219 -4.161 19.462 -6.095 1.00 78.21 N ANISOU 1639 N ALA A 219 11078 9822 8815 1276 393 769 N ATOM 1640 CA ALA A 219 -4.774 18.525 -7.025 1.00 68.47 C ANISOU 1640 CA ALA A 219 9744 8590 7680 1461 405 520 C ATOM 1641 C ALA A 219 -5.657 19.269 -8.018 1.00 73.99 C ANISOU 1641 C ALA A 219 10692 9342 8081 1643 342 331 C ATOM 1642 O ALA A 219 -6.363 20.216 -7.662 1.00 88.05 O ANISOU 1642 O ALA A 219 12663 11109 9684 1654 247 347 O ATOM 1643 CB ALA A 219 -5.590 17.477 -6.268 1.00 63.57 C ANISOU 1643 CB ALA A 219 8904 7882 7367 1461 347 455 C ATOM 1644 N SER A 220 -5.606 18.837 -9.279 1.00 73.76 N ANISOU 1644 N SER A 220 10665 9383 7978 1820 382 138 N ATOM 1645 CA SER A 220 -6.389 19.489 -10.322 1.00 80.36 C ANISOU 1645 CA SER A 220 11750 10302 8480 2043 298 -37 C ATOM 1646 C SER A 220 -7.825 18.986 -10.358 1.00 83.46 C ANISOU 1646 C SER A 220 12040 10678 8991 2198 110 -349 C ATOM 1647 O SER A 220 -8.741 19.762 -10.651 1.00 83.29 O ANISOU 1647 O SER A 220 12209 10697 8739 2349 -28 -449 O ATOM 1648 CB SER A 220 -5.735 19.273 -11.688 1.00 85.83 C ANISOU 1648 CB SER A 220 12508 11137 8967 2204 418 -125 C ATOM 1649 OG SER A 220 -5.466 17.899 -11.914 1.00 94.86 O ANISOU 1649 OG SER A 220 13363 12280 10400 2256 453 -333 O ATOM 1650 N ARG A 221 -8.038 17.706 -10.064 1.00 76.56 N ANISOU 1650 N ARG A 221 10854 9726 8510 2163 97 -503 N ATOM 1651 CA ARG A 221 -9.352 17.083 -10.157 1.00 75.46 C ANISOU 1651 CA ARG A 221 10542 9549 8581 2272 -65 -823 C ATOM 1652 C ARG A 221 -9.653 16.377 -8.844 1.00 79.87 C ANISOU 1652 C ARG A 221 10829 9956 9562 2059 -25 -699 C ATOM 1653 O ARG A 221 -8.894 15.501 -8.420 1.00 74.56 O ANISOU 1653 O ARG A 221 9982 9169 9177 1931 81 -567 O ATOM 1654 CB ARG A 221 -9.402 16.096 -11.327 1.00 78.35 C ANISOU 1654 CB ARG A 221 10787 9939 9045 2461 -128 -1193 C ATOM 1655 CG ARG A 221 -10.740 16.019 -12.038 1.00 79.76 C ANISOU 1655 CG ARG A 221 10930 10180 9195 2683 -368 -1606 C ATOM 1656 CD ARG A 221 -10.617 15.218 -13.323 1.00 74.42 C ANISOU 1656 CD ARG A 221 10205 9572 8498 2913 -453 -2002 C ATOM 1657 NE ARG A 221 -11.913 14.807 -13.847 1.00 86.16 N ANISOU 1657 NE ARG A 221 11537 11074 10124 3086 -728 -2469 N ATOM 1658 CZ ARG A 221 -12.083 13.863 -14.763 1.00 79.90 C ANISOU 1658 CZ ARG A 221 10602 10285 9470 3262 -872 -2925 C ATOM 1659 NH1 ARG A 221 -11.055 13.214 -15.285 1.00 89.35 N1+ ANISOU 1659 NH1 ARG A 221 11802 11479 10667 3316 -750 -2985 N1+ ATOM 1660 NH2 ARG A 221 -13.315 13.562 -15.164 1.00 87.04 N ANISOU 1660 NH2 ARG A 221 11335 11202 10535 3398 -1160 -3368 N ATOM 1661 N ILE A 222 -10.753 16.761 -8.203 1.00 83.21 N ANISOU 1661 N ILE A 222 11217 10388 10012 2043 -99 -725 N ATOM 1662 CA ILE A 222 -11.190 16.159 -6.948 1.00 74.35 C ANISOU 1662 CA ILE A 222 9849 9165 9234 1856 -25 -581 C ATOM 1663 C ILE A 222 -12.612 15.662 -7.172 1.00 74.54 C ANISOU 1663 C ILE A 222 9633 9168 9522 1928 -134 -905 C ATOM 1664 O ILE A 222 -13.561 16.455 -7.206 1.00 74.55 O ANISOU 1664 O ILE A 222 9692 9290 9343 2043 -235 -1038 O ATOM 1665 CB ILE A 222 -11.117 17.139 -5.773 1.00 71.81 C ANISOU 1665 CB ILE A 222 9677 8918 8690 1751 38 -285 C ATOM 1666 CG1 ILE A 222 -9.723 17.766 -5.689 1.00 70.05 C ANISOU 1666 CG1 ILE A 222 9681 8717 8220 1679 97 -27 C ATOM 1667 CG2 ILE A 222 -11.460 16.430 -4.471 1.00 65.42 C ANISOU 1667 CG2 ILE A 222 8630 8050 8178 1577 154 -90 C ATOM 1668 CD1 ILE A 222 -9.585 18.810 -4.604 1.00 66.65 C ANISOU 1668 CD1 ILE A 222 9420 8347 7558 1589 108 197 C ATOM 1669 N ILE A 223 -12.766 14.351 -7.330 1.00 65.97 N ANISOU 1669 N ILE A 223 8256 7909 8900 1863 -128 -1049 N ATOM 1670 CA ILE A 223 -14.058 13.730 -7.596 1.00 64.42 C ANISOU 1670 CA ILE A 223 7763 7651 9065 1889 -242 -1392 C ATOM 1671 C ILE A 223 -14.642 13.251 -6.274 1.00 80.38 C ANISOU 1671 C ILE A 223 9522 9570 11451 1651 -73 -1145 C ATOM 1672 O ILE A 223 -14.033 12.426 -5.581 1.00 78.63 O ANISOU 1672 O ILE A 223 9200 9163 11512 1469 84 -858 O ATOM 1673 CB ILE A 223 -13.930 12.571 -8.596 1.00 79.49 C ANISOU 1673 CB ILE A 223 9498 9390 11315 1953 -352 -1743 C ATOM 1674 CG1 ILE A 223 -13.648 13.104 -10.001 1.00 76.55 C ANISOU 1674 CG1 ILE A 223 9375 9203 10506 2248 -527 -2051 C ATOM 1675 CG2 ILE A 223 -15.195 11.727 -8.596 1.00 77.89 C ANISOU 1675 CG2 ILE A 223 8902 9039 11652 1882 -448 -2052 C ATOM 1676 CD1 ILE A 223 -12.276 12.744 -10.529 1.00 74.07 C ANISOU 1676 CD1 ILE A 223 9201 8858 10085 2295 -439 -1982 C ATOM 1677 N GLY A 224 -15.816 13.765 -5.926 1.00 78.15 N ANISOU 1677 N GLY A 224 9125 9420 11149 1673 -94 -1241 N ATOM 1678 CA GLY A 224 -16.511 13.362 -4.715 1.00 74.11 C ANISOU 1678 CA GLY A 224 8341 8870 10947 1464 107 -1018 C ATOM 1679 C GLY A 224 -17.571 12.335 -5.022 1.00 80.67 C ANISOU 1679 C GLY A 224 8735 9536 12379 1374 64 -1315 C ATOM 1680 O GLY A 224 -18.427 12.537 -5.890 1.00 91.41 O ANISOU 1680 O GLY A 224 9973 10981 13778 1533 -157 -1762 O ATOM 1681 N VAL A 225 -17.515 11.213 -4.305 1.00 71.15 N ANISOU 1681 N VAL A 225 7286 8078 11671 1119 262 -1063 N ATOM 1682 CA VAL A 225 -18.457 10.114 -4.464 1.00 83.03 C ANISOU 1682 CA VAL A 225 8339 9341 13869 956 261 -1286 C ATOM 1683 C VAL A 225 -19.312 10.035 -3.208 1.00 90.12 C ANISOU 1683 C VAL A 225 8973 10297 14972 740 558 -967 C ATOM 1684 O VAL A 225 -18.788 9.852 -2.102 1.00 96.36 O ANISOU 1684 O VAL A 225 9857 11057 15698 594 825 -443 O ATOM 1685 CB VAL A 225 -17.739 8.782 -4.725 1.00 73.80 C ANISOU 1685 CB VAL A 225 7085 7757 13198 829 262 -1252 C ATOM 1686 CG1 VAL A 225 -18.753 7.663 -4.904 1.00 82.18 C ANISOU 1686 CG1 VAL A 225 7667 8508 15049 633 240 -1512 C ATOM 1687 CG2 VAL A 225 -16.838 8.896 -5.945 1.00 82.65 C ANISOU 1687 CG2 VAL A 225 8469 8884 14050 1073 13 -1567 C ATOM 1688 N ASP A 226 -20.625 10.172 -3.377 1.00 78.27 N ANISOU 1688 N ASP A 226 7130 8909 13699 738 513 -1283 N ATOM 1689 CA ASP A 226 -21.550 10.080 -2.259 1.00106.66 C ANISOU 1689 CA ASP A 226 10409 12600 17518 538 831 -1020 C ATOM 1690 C ASP A 226 -22.917 9.660 -2.774 1.00101.58 C ANISOU 1690 C ASP A 226 9232 11910 17453 463 732 -1475 C ATOM 1691 O ASP A 226 -23.235 9.817 -3.956 1.00 92.27 O ANISOU 1691 O ASP A 226 8001 10750 16308 655 365 -2030 O ATOM 1692 CB ASP A 226 -21.651 11.406 -1.497 1.00 87.11 C ANISOU 1692 CB ASP A 226 8172 10549 14376 703 951 -831 C ATOM 1693 CG ASP A 226 -22.106 11.218 -0.065 1.00 95.48 C ANISOU 1693 CG ASP A 226 9043 11721 15514 497 1378 -367 C ATOM 1694 OD1 ASP A 226 -23.272 10.820 0.141 1.00103.70 O ANISOU 1694 OD1 ASP A 226 9610 12781 17012 349 1534 -465 O ATOM 1695 OD2 ASP A 226 -21.298 11.465 0.853 1.00 94.74 O1- ANISOU 1695 OD2 ASP A 226 9261 11718 15019 487 1561 92 O1- ATOM 1696 N PHE A 227 -23.725 9.117 -1.865 1.00 91.37 N ANISOU 1696 N PHE A 227 7530 10571 16613 182 1067 -1226 N ATOM 1697 CA PHE A 227 -25.096 8.738 -2.183 1.00102.89 C ANISOU 1697 CA PHE A 227 8398 12010 18686 60 1026 -1621 C ATOM 1698 C PHE A 227 -26.071 9.885 -1.950 1.00104.73 C ANISOU 1698 C PHE A 227 8496 12727 18569 262 1046 -1804 C ATOM 1699 O PHE A 227 -27.018 10.061 -2.724 1.00110.11 O ANISOU 1699 O PHE A 227 8842 13511 19484 380 774 -2355 O ATOM 1700 CB PHE A 227 -25.507 7.519 -1.354 1.00108.69 C ANISOU 1700 CB PHE A 227 8707 12420 20170 -379 1415 -1242 C ATOM 1701 CG PHE A 227 -24.870 6.237 -1.808 1.00115.75 C ANISOU 1701 CG PHE A 227 9587 12744 21649 -575 1314 -1234 C ATOM 1702 CD1 PHE A 227 -24.966 5.831 -3.129 1.00119.53 C ANISOU 1702 CD1 PHE A 227 9943 12997 22476 -486 873 -1881 C ATOM 1703 CD2 PHE A 227 -24.170 5.441 -0.918 1.00114.88 C ANISOU 1703 CD2 PHE A 227 9601 12327 21720 -813 1642 -594 C ATOM 1704 CE1 PHE A 227 -24.381 4.652 -3.552 1.00112.25 C ANISOU 1704 CE1 PHE A 227 9009 11538 22102 -636 769 -1927 C ATOM 1705 CE2 PHE A 227 -23.581 4.261 -1.335 1.00109.97 C ANISOU 1705 CE2 PHE A 227 8970 11143 21669 -962 1535 -600 C ATOM 1706 CZ PHE A 227 -23.686 3.866 -2.654 1.00101.15 C ANISOU 1706 CZ PHE A 227 7720 9790 20923 -874 1102 -1285 C ATOM 1707 N ASN A 228 -25.855 10.671 -0.898 1.00110.33 N ANISOU 1707 N ASN A 228 9458 13741 18722 333 1336 -1382 N ATOM 1708 CA ASN A 228 -26.678 11.844 -0.615 1.00109.42 C ANISOU 1708 CA ASN A 228 9275 14085 18217 578 1358 -1555 C ATOM 1709 C ASN A 228 -26.195 12.987 -1.499 1.00105.34 C ANISOU 1709 C ASN A 228 9232 13724 17070 992 933 -1882 C ATOM 1710 O ASN A 228 -25.219 13.669 -1.176 1.00 96.04 O ANISOU 1710 O ASN A 228 8581 12622 15289 1124 949 -1610 O ATOM 1711 CB ASN A 228 -26.603 12.210 0.863 1.00105.21 C ANISOU 1711 CB ASN A 228 8847 13810 17319 513 1827 -1008 C ATOM 1712 CG ASN A 228 -27.549 13.335 1.235 1.00103.56 C ANISOU 1712 CG ASN A 228 8503 14067 16778 768 1892 -1214 C ATOM 1713 ND2 ASN A 228 -27.392 13.864 2.444 1.00101.96 N ANISOU 1713 ND2 ASN A 228 8488 14149 16104 809 2238 -822 N ATOM 1714 OD1 ASN A 228 -28.412 13.724 0.448 1.00116.70 O ANISOU 1714 OD1 ASN A 228 9895 15845 18599 955 1615 -1740 O ATOM 1715 N SER A 229 -26.881 13.198 -2.626 1.00114.53 N ANISOU 1715 N SER A 229 10203 14930 18382 1196 543 -2464 N ATOM 1716 CA SER A 229 -26.477 14.239 -3.564 1.00 99.91 C ANISOU 1716 CA SER A 229 8805 13205 15950 1599 136 -2752 C ATOM 1717 C SER A 229 -26.658 15.640 -2.997 1.00 98.27 C ANISOU 1717 C SER A 229 8857 13343 15139 1883 190 -2670 C ATOM 1718 O SER A 229 -26.085 16.591 -3.540 1.00 98.38 O ANISOU 1718 O SER A 229 9360 13413 14607 2180 -65 -2741 O ATOM 1719 CB SER A 229 -27.258 14.102 -4.872 1.00 85.49 C ANISOU 1719 CB SER A 229 6697 11378 14408 1786 -310 -3391 C ATOM 1720 OG SER A 229 -26.862 12.942 -5.583 1.00 95.00 O ANISOU 1720 OG SER A 229 7801 12243 16053 1601 -450 -3539 O ATOM 1721 N LYS A 230 -27.435 15.788 -1.920 1.00 99.95 N ANISOU 1721 N LYS A 230 8755 13777 15446 1802 530 -2522 N ATOM 1722 CA LYS A 230 -27.582 17.089 -1.276 1.00103.21 C ANISOU 1722 CA LYS A 230 9416 14504 15294 2083 601 -2463 C ATOM 1723 C LYS A 230 -26.251 17.641 -0.786 1.00107.63 C ANISOU 1723 C LYS A 230 10619 15013 15264 2107 671 -2065 C ATOM 1724 O LYS A 230 -26.124 18.856 -0.600 1.00100.02 O ANISOU 1724 O LYS A 230 10004 14215 13782 2394 579 -2102 O ATOM 1725 CB LYS A 230 -28.567 16.991 -0.109 1.00105.49 C ANISOU 1725 CB LYS A 230 9233 15059 15788 1964 1030 -2338 C ATOM 1726 CG LYS A 230 -30.025 17.155 -0.506 1.00103.15 C ANISOU 1726 CG LYS A 230 8356 14977 15861 2122 910 -2828 C ATOM 1727 CD LYS A 230 -30.854 17.693 0.651 1.00124.68 C ANISOU 1727 CD LYS A 230 10808 18092 18474 2199 1297 -2743 C ATOM 1728 CE LYS A 230 -31.745 16.614 1.246 1.00125.07 C ANISOU 1728 CE LYS A 230 10132 18191 19197 1821 1722 -2629 C ATOM 1729 NZ LYS A 230 -32.914 17.194 1.965 1.00104.54 N1+ ANISOU 1729 NZ LYS A 230 7088 16036 16597 1987 1998 -2772 N1+ ATOM 1730 N ARG A 231 -25.259 16.778 -0.577 1.00 98.80 N ANISOU 1730 N ARG A 231 9644 13647 14248 1821 809 -1705 N ATOM 1731 CA ARG A 231 -23.928 17.191 -0.154 1.00 99.82 C ANISOU 1731 CA ARG A 231 10325 13717 13884 1821 845 -1346 C ATOM 1732 C ARG A 231 -23.070 17.701 -1.304 1.00100.08 C ANISOU 1732 C ARG A 231 10796 13600 13631 2008 468 -1514 C ATOM 1733 O ARG A 231 -21.937 18.131 -1.063 1.00 98.81 O ANISOU 1733 O ARG A 231 11075 13386 13084 2009 468 -1254 O ATOM 1734 CB ARG A 231 -23.211 16.021 0.523 1.00101.69 C ANISOU 1734 CB ARG A 231 10513 13757 14369 1468 1130 -888 C ATOM 1735 CG ARG A 231 -23.571 15.821 1.979 1.00109.60 C ANISOU 1735 CG ARG A 231 11337 14956 15350 1315 1569 -508 C ATOM 1736 CD ARG A 231 -23.200 14.416 2.448 1.00 96.22 C ANISOU 1736 CD ARG A 231 9460 13007 14091 959 1834 -90 C ATOM 1737 NE ARG A 231 -23.558 14.138 3.837 1.00117.98 N ANISOU 1737 NE ARG A 231 12054 15964 16811 810 2291 340 N ATOM 1738 CZ ARG A 231 -23.238 14.886 4.887 1.00125.33 C ANISOU 1738 CZ ARG A 231 13271 17200 17146 937 2455 590 C ATOM 1739 NH1 ARG A 231 -22.464 15.955 4.774 1.00112.58 N1+ ANISOU 1739 NH1 ARG A 231 12130 15677 14968 1178 2197 478 N1+ ATOM 1740 NH2 ARG A 231 -23.693 14.542 6.089 1.00122.62 N ANISOU 1740 NH2 ARG A 231 12737 17076 16778 816 2896 966 N ATOM 1741 N PHE A 232 -23.579 17.674 -2.535 1.00 96.76 N ANISOU 1741 N PHE A 232 10255 13131 13377 2170 152 -1937 N ATOM 1742 CA PHE A 232 -22.742 17.882 -3.712 1.00 93.01 C ANISOU 1742 CA PHE A 232 10155 12510 12676 2314 -156 -2059 C ATOM 1743 C PHE A 232 -22.265 19.323 -3.857 1.00 94.01 C ANISOU 1743 C PHE A 232 10799 12729 12193 2592 -309 -2026 C ATOM 1744 O PHE A 232 -21.075 19.599 -3.667 1.00100.21 O ANISOU 1744 O PHE A 232 11974 13418 12683 2521 -254 -1732 O ATOM 1745 CB PHE A 232 -23.490 17.441 -4.971 1.00 98.16 C ANISOU 1745 CB PHE A 232 10535 13130 13633 2446 -469 -2545 C ATOM 1746 CG PHE A 232 -23.394 15.966 -5.237 1.00 93.13 C ANISOU 1746 CG PHE A 232 9568 12254 13565 2166 -419 -2592 C ATOM 1747 CD1 PHE A 232 -22.805 15.120 -4.309 1.00 95.58 C ANISOU 1747 CD1 PHE A 232 9807 12391 14118 1826 -84 -2175 C ATOM 1748 CD2 PHE A 232 -23.881 15.424 -6.414 1.00 88.66 C ANISOU 1748 CD2 PHE A 232 8778 11621 13289 2265 -732 -3062 C ATOM 1749 CE1 PHE A 232 -22.709 13.764 -4.547 1.00 87.61 C ANISOU 1749 CE1 PHE A 232 8512 11097 13677 1579 -49 -2209 C ATOM 1750 CE2 PHE A 232 -23.788 14.067 -6.659 1.00 87.53 C ANISOU 1750 CE2 PHE A 232 8336 11209 13712 2011 -709 -3150 C ATOM 1751 CZ PHE A 232 -23.201 13.236 -5.723 1.00 93.82 C ANISOU 1751 CZ PHE A 232 9069 11785 14794 1662 -360 -2713 C ATOM 1752 N ASP A 233 -23.169 20.246 -4.201 1.00117.35 N ANISOU 1752 N ASP A 233 13750 15848 14992 2910 -512 -2326 N ATOM 1753 CA ASP A 233 -22.763 21.633 -4.406 1.00124.27 C ANISOU 1753 CA ASP A 233 15132 16742 15341 3185 -679 -2295 C ATOM 1754 C ASP A 233 -22.242 22.279 -3.132 1.00108.26 C ANISOU 1754 C ASP A 233 13336 14752 13047 3098 -443 -1978 C ATOM 1755 O ASP A 233 -21.657 23.365 -3.203 1.00111.32 O ANISOU 1755 O ASP A 233 14178 15077 13043 3248 -557 -1898 O ATOM 1756 CB ASP A 233 -23.916 22.463 -4.980 1.00110.71 C ANISOU 1756 CB ASP A 233 13346 15173 13547 3582 -961 -2679 C ATOM 1757 CG ASP A 233 -25.242 22.174 -4.308 1.00117.78 C ANISOU 1757 CG ASP A 233 13678 16278 14794 3585 -833 -2887 C ATOM 1758 OD1 ASP A 233 -25.249 21.811 -3.112 1.00120.70 O ANISOU 1758 OD1 ASP A 233 13855 16717 15287 3340 -476 -2656 O ATOM 1759 OD2 ASP A 233 -26.281 22.309 -4.985 1.00116.14 O1- ANISOU 1759 OD2 ASP A 233 13208 16188 14732 3844 -1088 -3278 O1- ATOM 1760 N GLN A 234 -22.438 21.644 -1.977 1.00101.16 N ANISOU 1760 N GLN A 234 12143 13948 12344 2863 -123 -1795 N ATOM 1761 CA GLN A 234 -21.711 22.064 -0.787 1.00104.12 C ANISOU 1761 CA GLN A 234 12768 14364 12428 2756 87 -1471 C ATOM 1762 C GLN A 234 -20.237 21.695 -0.917 1.00104.95 C ANISOU 1762 C GLN A 234 13169 14263 12443 2539 95 -1164 C ATOM 1763 O GLN A 234 -19.370 22.575 -0.908 1.00105.98 O ANISOU 1763 O GLN A 234 13721 14318 12228 2597 -7 -1061 O ATOM 1764 CB GLN A 234 -22.337 21.446 0.465 1.00 96.88 C ANISOU 1764 CB GLN A 234 11468 13648 11694 2592 444 -1327 C ATOM 1765 CG GLN A 234 -21.518 21.644 1.744 1.00 94.48 C ANISOU 1765 CG GLN A 234 11403 13421 11074 2470 663 -969 C ATOM 1766 CD GLN A 234 -22.195 21.037 2.964 1.00 97.78 C ANISOU 1766 CD GLN A 234 11461 14084 11608 2342 1048 -792 C ATOM 1767 NE2 GLN A 234 -22.657 21.890 3.873 1.00 95.85 N ANISOU 1767 NE2 GLN A 234 11270 14112 11036 2532 1162 -858 N ATOM 1768 OE1 GLN A 234 -22.307 19.817 3.082 1.00103.49 O ANISOU 1768 OE1 GLN A 234 11865 14743 12714 2083 1251 -596 O ATOM 1769 N ALA A 235 -19.935 20.399 -1.117 1.00 99.31 N ANISOU 1769 N ALA A 235 12537 11850 13347 3365 1483 -346 N ATOM 1770 CA ALA A 235 -18.548 19.942 -1.262 1.00 95.10 C ANISOU 1770 CA ALA A 235 12353 11367 12415 3140 1438 -74 C ATOM 1771 C ALA A 235 -17.731 20.831 -2.203 1.00 93.66 C ANISOU 1771 C ALA A 235 12315 11050 12221 3278 1160 357 C ATOM 1772 O ALA A 235 -16.499 20.839 -2.117 1.00 95.18 O ANISOU 1772 O ALA A 235 12783 11208 12174 3104 1165 574 O ATOM 1773 CB ALA A 235 -18.500 18.483 -1.744 1.00 90.92 C ANISOU 1773 CB ALA A 235 11789 11192 11566 2992 1396 -63 C ATOM 1774 N LYS A 236 -18.392 21.633 -3.050 1.00103.25 N ANISOU 1774 N LYS A 236 13340 12180 13711 3569 909 507 N ATOM 1775 CA LYS A 236 -17.684 22.501 -3.989 1.00 99.92 C ANISOU 1775 CA LYS A 236 13060 11642 13264 3659 617 973 C ATOM 1776 C LYS A 236 -16.763 23.494 -3.290 1.00 97.09 C ANISOU 1776 C LYS A 236 12991 10898 13000 3553 677 1080 C ATOM 1777 O LYS A 236 -15.704 23.828 -3.829 1.00 96.63 O ANISOU 1777 O LYS A 236 13132 10838 12747 3445 534 1482 O ATOM 1778 CB LYS A 236 -18.683 23.256 -4.869 1.00 96.79 C ANISOU 1778 CB LYS A 236 12411 11156 13209 3983 302 1111 C ATOM 1779 CG LYS A 236 -18.523 23.011 -6.366 1.00116.34 C ANISOU 1779 CG LYS A 236 14861 13942 15400 4023 -30 1521 C ATOM 1780 CD LYS A 236 -17.287 23.695 -6.915 1.00130.11 C ANISOU 1780 CD LYS A 236 16895 15609 16933 3910 -176 2008 C ATOM 1781 CE LYS A 236 -17.144 23.449 -8.407 1.00124.00 C ANISOU 1781 CE LYS A 236 16102 15209 15803 3921 -469 2400 C ATOM 1782 NZ LYS A 236 -15.738 23.595 -8.875 1.00103.45 N1+ ANISOU 1782 NZ LYS A 236 13759 12744 12804 3703 -464 2799 N1+ ATOM 1783 N GLU A 237 -17.142 23.999 -2.113 1.00 91.53 N ANISOU 1783 N GLU A 237 12312 9884 12582 3565 884 724 N ATOM 1784 CA GLU A 237 -16.273 24.963 -1.446 1.00 81.00 C ANISOU 1784 CA GLU A 237 11286 8157 11335 3443 904 800 C ATOM 1785 C GLU A 237 -15.114 24.297 -0.710 1.00 93.76 C ANISOU 1785 C GLU A 237 13167 9895 12563 3070 1100 798 C ATOM 1786 O GLU A 237 -14.340 24.996 -0.048 1.00 92.51 O ANISOU 1786 O GLU A 237 13273 9438 12438 2908 1118 840 O ATOM 1787 CB GLU A 237 -17.070 25.865 -0.480 1.00107.27 C ANISOU 1787 CB GLU A 237 14576 11072 15111 3612 1038 384 C ATOM 1788 CG GLU A 237 -18.487 26.209 -0.944 1.00116.65 C ANISOU 1788 CG GLU A 237 15382 12208 16734 4010 929 223 C ATOM 1789 CD GLU A 237 -19.562 25.596 -0.085 1.00122.43 C ANISOU 1789 CD GLU A 237 15840 13121 17558 4051 1280 -337 C ATOM 1790 OE1 GLU A 237 -20.612 26.250 0.083 1.00128.15 O ANISOU 1790 OE1 GLU A 237 16294 13643 18756 4372 1298 -620 O ATOM 1791 OE2 GLU A 237 -19.340 24.518 0.489 1.00118.57 O1- ANISOU 1791 OE2 GLU A 237 15406 12950 16696 3756 1544 -500 O1- ATOM 1792 N PHE A 238 -14.955 22.976 -0.827 1.00 86.17 N ANISOU 1792 N PHE A 238 12146 9339 11257 2930 1205 763 N ATOM 1793 CA PHE A 238 -13.837 22.271 -0.211 1.00 79.92 C ANISOU 1793 CA PHE A 238 11574 8660 10131 2607 1333 802 C ATOM 1794 C PHE A 238 -12.846 21.740 -1.242 1.00 82.06 C ANISOU 1794 C PHE A 238 11860 9219 10099 2555 1181 1199 C ATOM 1795 O PHE A 238 -12.021 20.877 -0.921 1.00 72.98 O ANISOU 1795 O PHE A 238 10806 8239 8685 2349 1265 1217 O ATOM 1796 CB PHE A 238 -14.350 21.134 0.674 1.00 73.72 C ANISOU 1796 CB PHE A 238 10743 8056 9211 2455 1584 419 C ATOM 1797 CG PHE A 238 -15.217 21.596 1.809 1.00 78.54 C ANISOU 1797 CG PHE A 238 11342 8461 10039 2448 1812 -4 C ATOM 1798 CD1 PHE A 238 -16.574 21.809 1.622 1.00 90.54 C ANISOU 1798 CD1 PHE A 238 12560 9992 11849 2708 1860 -255 C ATOM 1799 CD2 PHE A 238 -14.675 21.822 3.063 1.00 78.62 C ANISOU 1799 CD2 PHE A 238 11624 8292 9954 2179 1979 -165 C ATOM 1800 CE1 PHE A 238 -17.373 22.237 2.666 1.00 82.23 C ANISOU 1800 CE1 PHE A 238 11452 8794 10997 2722 2120 -688 C ATOM 1801 CE2 PHE A 238 -15.469 22.248 4.111 1.00 74.99 C ANISOU 1801 CE2 PHE A 238 11163 7687 9641 2166 2229 -600 C ATOM 1802 CZ PHE A 238 -16.820 22.457 3.912 1.00 73.29 C ANISOU 1802 CZ PHE A 238 10620 7503 9724 2449 2324 -877 C ATOM 1803 N GLY A 239 -12.904 22.246 -2.473 1.00 77.88 N ANISOU 1803 N GLY A 239 11234 8757 9602 2738 954 1517 N ATOM 1804 CA GLY A 239 -12.008 21.846 -3.531 1.00 72.07 C ANISOU 1804 CA GLY A 239 10494 8342 8547 2698 843 1877 C ATOM 1805 C GLY A 239 -12.594 20.861 -4.522 1.00 76.37 C ANISOU 1805 C GLY A 239 10848 9277 8892 2846 788 1821 C ATOM 1806 O GLY A 239 -12.028 20.689 -5.608 1.00 72.30 O ANISOU 1806 O GLY A 239 10312 9053 8106 2865 679 2109 O ATOM 1807 N VAL A 240 -13.712 20.217 -4.178 1.00 78.48 N ANISOU 1807 N VAL A 240 10974 9576 9267 2927 864 1452 N ATOM 1808 CA VAL A 240 -14.305 19.205 -5.048 1.00 84.39 C ANISOU 1808 CA VAL A 240 11558 10672 9833 3028 787 1359 C ATOM 1809 C VAL A 240 -14.670 19.837 -6.383 1.00 78.04 C ANISOU 1809 C VAL A 240 10649 9989 9015 3222 509 1657 C ATOM 1810 O VAL A 240 -15.433 20.809 -6.441 1.00 83.86 O ANISOU 1810 O VAL A 240 11292 10495 10076 3378 368 1715 O ATOM 1811 CB VAL A 240 -15.525 18.567 -4.375 1.00 68.89 C ANISOU 1811 CB VAL A 240 9436 8688 8051 3039 898 942 C ATOM 1812 CG1 VAL A 240 -16.132 17.501 -5.275 1.00 74.93 C ANISOU 1812 CG1 VAL A 240 10045 9785 8639 3105 777 844 C ATOM 1813 CG2 VAL A 240 -15.133 17.974 -3.031 1.00 63.22 C ANISOU 1813 CG2 VAL A 240 8862 7861 7297 2793 1154 702 C ATOM 1814 N THR A 241 -14.122 19.286 -7.466 1.00 68.48 N ANISOU 1814 N THR A 241 9455 9141 7422 3217 419 1842 N ATOM 1815 CA THR A 241 -14.365 19.816 -8.801 1.00 81.82 C ANISOU 1815 CA THR A 241 11086 11017 8985 3343 142 2169 C ATOM 1816 C THR A 241 -15.562 19.171 -9.484 1.00 90.05 C ANISOU 1816 C THR A 241 11940 12278 9997 3482 -30 1980 C ATOM 1817 O THR A 241 -16.174 19.794 -10.360 1.00 91.78 O ANISOU 1817 O THR A 241 12068 12544 10260 3612 -319 2213 O ATOM 1818 CB THR A 241 -13.119 19.639 -9.673 1.00 82.96 C ANISOU 1818 CB THR A 241 11346 11504 8671 3240 156 2473 C ATOM 1819 CG2 THR A 241 -11.860 19.820 -8.840 1.00 78.37 C ANISOU 1819 CG2 THR A 241 10903 10779 8096 3059 373 2554 C ATOM 1820 OG1 THR A 241 -13.123 18.332 -10.261 1.00 94.13 O ANISOU 1820 OG1 THR A 241 12723 13309 9734 3259 200 2241 O ATOM 1821 N GLU A 242 -15.908 17.941 -9.111 1.00 79.21 N ANISOU 1821 N GLU A 242 10511 11026 8560 3434 102 1591 N ATOM 1822 CA GLU A 242 -17.105 17.296 -9.630 1.00 78.01 C ANISOU 1822 CA GLU A 242 10164 11050 8425 3520 -71 1381 C ATOM 1823 C GLU A 242 -17.507 16.177 -8.684 1.00 89.21 C ANISOU 1823 C GLU A 242 11534 12421 9941 3402 130 948 C ATOM 1824 O GLU A 242 -16.670 15.620 -7.968 1.00 80.39 O ANISOU 1824 O GLU A 242 10580 11244 8721 3255 356 841 O ATOM 1825 CB GLU A 242 -16.897 16.752 -11.050 1.00 69.39 C ANISOU 1825 CB GLU A 242 9118 10379 6866 3542 -270 1502 C ATOM 1826 CG GLU A 242 -15.776 15.738 -11.181 1.00 82.57 C ANISOU 1826 CG GLU A 242 10967 12272 8133 3435 -79 1387 C ATOM 1827 CD GLU A 242 -15.187 15.704 -12.579 1.00 91.38 C ANISOU 1827 CD GLU A 242 12172 13802 8747 3462 -205 1615 C ATOM 1828 OE1 GLU A 242 -15.889 15.258 -13.511 1.00 97.31 O ANISOU 1828 OE1 GLU A 242 12872 14813 9287 3511 -433 1532 O ATOM 1829 OE2 GLU A 242 -14.023 16.124 -12.747 1.00 82.48 O1- ANISOU 1829 OE2 GLU A 242 11159 12766 7416 3411 -75 1875 O1- ATOM 1830 N CYS A 243 -18.798 15.860 -8.687 1.00 98.40 N ANISOU 1830 N CYS A 243 12457 13615 11314 3446 21 731 N ATOM 1831 CA CYS A 243 -19.358 14.836 -7.821 1.00 78.99 C ANISOU 1831 CA CYS A 243 9918 11127 8967 3289 185 356 C ATOM 1832 C CYS A 243 -20.032 13.759 -8.660 1.00 83.06 C ANISOU 1832 C CYS A 243 10332 11916 9310 3259 -32 195 C ATOM 1833 O CYS A 243 -20.514 14.022 -9.766 1.00 79.58 O ANISOU 1833 O CYS A 243 9782 11664 8790 3392 -327 332 O ATOM 1834 CB CYS A 243 -20.366 15.434 -6.835 1.00 88.19 C ANISOU 1834 CB CYS A 243 10839 12077 10591 3313 311 192 C ATOM 1835 SG CYS A 243 -19.671 16.667 -5.711 1.00 95.12 S ANISOU 1835 SG CYS A 243 11872 12587 11685 3325 567 281 S ATOM 1836 N VAL A 244 -20.053 12.538 -8.128 1.00 88.99 N ANISOU 1836 N VAL A 244 11143 12670 9998 3060 82 -84 N ATOM 1837 CA VAL A 244 -20.653 11.393 -8.805 1.00 81.28 C ANISOU 1837 CA VAL A 244 10113 11893 8876 2982 -127 -284 C ATOM 1838 C VAL A 244 -21.490 10.613 -7.800 1.00 91.83 C ANISOU 1838 C VAL A 244 11305 13125 10461 2746 -10 -565 C ATOM 1839 O VAL A 244 -21.090 10.440 -6.644 1.00 83.95 O ANISOU 1839 O VAL A 244 10417 11935 9544 2585 260 -633 O ATOM 1840 CB VAL A 244 -19.587 10.478 -9.446 1.00 89.40 C ANISOU 1840 CB VAL A 244 11441 13042 9485 2963 -161 -330 C ATOM 1841 CG1 VAL A 244 -20.249 9.335 -10.202 1.00 89.89 C ANISOU 1841 CG1 VAL A 244 11479 13275 9399 2888 -415 -576 C ATOM 1842 CG2 VAL A 244 -18.680 11.269 -10.377 1.00 83.81 C ANISOU 1842 CG2 VAL A 244 10859 12497 8487 3148 -211 -35 C ATOM 1843 N ASN A 245 -22.656 10.143 -8.243 1.00 98.84 N ANISOU 1843 N ASN A 245 11942 14160 11452 2691 -229 -704 N ATOM 1844 CA ASN A 245 -23.494 9.265 -7.446 1.00 90.53 C ANISOU 1844 CA ASN A 245 10735 13067 10597 2408 -153 -951 C ATOM 1845 C ASN A 245 -23.510 7.878 -8.069 1.00 99.59 C ANISOU 1845 C ASN A 245 12034 14290 11514 2242 -388 -1125 C ATOM 1846 O ASN A 245 -23.809 7.748 -9.264 1.00101.08 O ANISOU 1846 O ASN A 245 12188 14676 11543 2349 -707 -1124 O ATOM 1847 CB ASN A 245 -24.922 9.810 -7.349 1.00101.25 C ANISOU 1847 CB ASN A 245 11612 14527 12332 2441 -212 -994 C ATOM 1848 CG ASN A 245 -25.755 9.076 -6.316 1.00111.51 C ANISOU 1848 CG ASN A 245 12705 15814 13851 2108 -33 -1220 C ATOM 1849 ND2 ASN A 245 -26.443 9.828 -5.468 1.00117.02 N ANISOU 1849 ND2 ASN A 245 13077 16500 14885 2128 217 -1270 N ATOM 1850 OD1 ASN A 245 -25.784 7.849 -6.285 1.00111.51 O ANISOU 1850 OD1 ASN A 245 12835 15813 13720 1828 -116 -1352 O ATOM 1851 N PRO A 246 -23.195 6.827 -7.305 1.00103.43 N ANISOU 1851 N PRO A 246 12716 14609 11975 1972 -271 -1276 N ATOM 1852 CA PRO A 246 -23.179 5.476 -7.895 1.00106.38 C ANISOU 1852 CA PRO A 246 13271 14977 12170 1826 -526 -1470 C ATOM 1853 C PRO A 246 -24.518 5.023 -8.455 1.00108.17 C ANISOU 1853 C PRO A 246 13214 15371 12517 1683 -823 -1605 C ATOM 1854 O PRO A 246 -24.553 4.466 -9.560 1.00101.10 O ANISOU 1854 O PRO A 246 12426 14587 11399 1732 -1141 -1714 O ATOM 1855 CB PRO A 246 -22.723 4.597 -6.722 1.00102.52 C ANISOU 1855 CB PRO A 246 13002 14212 11741 1536 -345 -1547 C ATOM 1856 CG PRO A 246 -21.911 5.510 -5.868 1.00 94.21 C ANISOU 1856 CG PRO A 246 12029 13055 10713 1632 -17 -1364 C ATOM 1857 CD PRO A 246 -22.575 6.858 -5.969 1.00 89.71 C ANISOU 1857 CD PRO A 246 11130 12646 10309 1819 64 -1246 C ATOM 1858 N LYS A 247 -25.625 5.234 -7.736 1.00112.74 N ANISOU 1858 N LYS A 247 13415 15992 13428 1496 -729 -1617 N ATOM 1859 CA LYS A 247 -26.913 4.772 -8.246 1.00116.28 C ANISOU 1859 CA LYS A 247 13538 16618 14025 1328 -1029 -1732 C ATOM 1860 C LYS A 247 -27.381 5.565 -9.460 1.00104.99 C ANISOU 1860 C LYS A 247 11888 15444 12562 1626 -1329 -1630 C ATOM 1861 O LYS A 247 -28.357 5.161 -10.101 1.00116.92 O ANISOU 1861 O LYS A 247 13158 17124 14142 1509 -1666 -1713 O ATOM 1862 CB LYS A 247 -27.986 4.819 -7.151 1.00116.51 C ANISOU 1862 CB LYS A 247 13151 16686 14431 1047 -813 -1771 C ATOM 1863 CG LYS A 247 -28.270 6.197 -6.579 1.00117.42 C ANISOU 1863 CG LYS A 247 12939 16873 14802 1277 -515 -1659 C ATOM 1864 CD LYS A 247 -28.581 6.127 -5.088 1.00111.09 C ANISOU 1864 CD LYS A 247 11996 16016 14196 980 -92 -1730 C ATOM 1865 CE LYS A 247 -29.242 7.405 -4.586 1.00111.30 C ANISOU 1865 CE LYS A 247 11575 16160 14552 1196 174 -1724 C ATOM 1866 NZ LYS A 247 -28.590 7.910 -3.344 1.00106.60 N1+ ANISOU 1866 NZ LYS A 247 11168 15409 13928 1163 634 -1727 N1+ ATOM 1867 N ASP A 248 -26.714 6.670 -9.790 1.00 97.91 N ANISOU 1867 N ASP A 248 6626 13132 17445 1548 -855 -1673 N ATOM 1868 CA ASP A 248 -26.996 7.418 -11.007 1.00106.88 C ANISOU 1868 CA ASP A 248 7627 14443 18539 1713 -1282 -1585 C ATOM 1869 C ASP A 248 -26.286 6.851 -12.229 1.00101.14 C ANISOU 1869 C ASP A 248 7242 13764 17423 1553 -1698 -1717 C ATOM 1870 O ASP A 248 -26.419 7.418 -13.319 1.00 94.48 O ANISOU 1870 O ASP A 248 6341 13094 16464 1652 -2081 -1637 O ATOM 1871 CB ASP A 248 -26.599 8.887 -10.828 1.00 98.06 C ANISOU 1871 CB ASP A 248 6638 13273 17347 2120 -1144 -1447 C ATOM 1872 CG ASP A 248 -27.617 9.675 -10.033 1.00120.76 C ANISOU 1872 CG ASP A 248 9066 16171 20646 2373 -879 -1319 C ATOM 1873 OD1 ASP A 248 -28.567 9.059 -9.505 1.00133.36 O ANISOU 1873 OD1 ASP A 248 10237 17861 22571 2221 -731 -1321 O ATOM 1874 OD2 ASP A 248 -27.467 10.911 -9.936 1.00120.94 O1- ANISOU 1874 OD2 ASP A 248 9162 16117 20674 2728 -821 -1214 O1- ATOM 1875 N HIS A 249 -25.544 5.755 -12.081 1.00 94.86 N ANISOU 1875 N HIS A 249 6801 12825 16415 1325 -1633 -1915 N ATOM 1876 CA HIS A 249 -24.740 5.202 -13.160 1.00105.85 C ANISOU 1876 CA HIS A 249 8570 14255 17391 1233 -1954 -2089 C ATOM 1877 C HIS A 249 -24.980 3.704 -13.275 1.00108.94 C ANISOU 1877 C HIS A 249 9001 14544 17847 874 -2111 -2311 C ATOM 1878 O HIS A 249 -25.080 3.000 -12.265 1.00 91.36 O ANISOU 1878 O HIS A 249 6757 12120 15837 706 -1836 -2343 O ATOM 1879 CB HIS A 249 -23.249 5.480 -12.933 1.00 88.96 C ANISOU 1879 CB HIS A 249 6943 12009 14849 1403 -1716 -2122 C ATOM 1880 CG HIS A 249 -22.865 6.913 -13.138 1.00 92.07 C ANISOU 1880 CG HIS A 249 7388 12500 15093 1706 -1701 -1908 C ATOM 1881 CD2 HIS A 249 -22.817 7.955 -12.275 1.00 86.77 C ANISOU 1881 CD2 HIS A 249 6683 11726 14559 1927 -1405 -1730 C ATOM 1882 ND1 HIS A 249 -22.476 7.411 -14.363 1.00 86.38 N ANISOU 1882 ND1 HIS A 249 6790 11994 14036 1795 -2043 -1854 N ATOM 1883 CE1 HIS A 249 -22.202 8.698 -14.245 1.00101.11 C ANISOU 1883 CE1 HIS A 249 8685 13867 15863 2039 -1976 -1620 C ATOM 1884 NE2 HIS A 249 -22.401 9.053 -12.989 1.00107.53 N ANISOU 1884 NE2 HIS A 249 9421 14468 16967 2133 -1598 -1560 N ATOM 1885 N ASP A 250 -25.069 3.225 -14.518 1.00103.68 N ANISOU 1885 N ASP A 250 8414 14003 16976 745 -2574 -2462 N ATOM 1886 CA ASP A 250 -25.263 1.799 -14.762 1.00101.33 C ANISOU 1886 CA ASP A 250 8225 13562 16712 404 -2801 -2711 C ATOM 1887 C ASP A 250 -24.055 0.995 -14.298 1.00113.18 C ANISOU 1887 C ASP A 250 10233 14792 17980 403 -2555 -2921 C ATOM 1888 O ASP A 250 -24.192 -0.019 -13.603 1.00106.59 O ANISOU 1888 O ASP A 250 9435 13696 17369 161 -2457 -3008 O ATOM 1889 CB ASP A 250 -25.522 1.558 -16.250 1.00101.07 C ANISOU 1889 CB ASP A 250 8244 13729 16431 302 -3363 -2859 C ATOM 1890 CG ASP A 250 -26.979 1.279 -16.555 1.00127.11 C ANISOU 1890 CG ASP A 250 11051 17131 20112 12 -3732 -2774 C ATOM 1891 OD1 ASP A 250 -27.655 0.650 -15.713 1.00107.62 O ANISOU 1891 OD1 ASP A 250 8325 14504 18061 -233 -3609 -2724 O ATOM 1892 OD2 ASP A 250 -27.446 1.687 -17.638 1.00126.40 O1- ANISOU 1892 OD2 ASP A 250 10821 17304 19903 10 -4157 -2728 O1- ATOM 1893 N LYS A 251 -22.863 1.439 -14.676 1.00116.97 N ANISOU 1893 N LYS A 251 11084 15337 18021 665 -2466 -2973 N ATOM 1894 CA LYS A 251 -21.638 0.701 -14.439 1.00108.38 C ANISOU 1894 CA LYS A 251 10462 14044 16672 712 -2283 -3172 C ATOM 1895 C LYS A 251 -21.148 0.921 -13.010 1.00 98.14 C ANISOU 1895 C LYS A 251 9208 12546 15536 782 -1789 -3005 C ATOM 1896 O LYS A 251 -21.491 1.922 -12.376 1.00 97.42 O ANISOU 1896 O LYS A 251 8874 12528 15612 892 -1567 -2753 O ATOM 1897 CB LYS A 251 -20.590 1.143 -15.455 1.00105.72 C ANISOU 1897 CB LYS A 251 10438 13940 15791 962 -2382 -3252 C ATOM 1898 CG LYS A 251 -21.036 0.896 -16.893 1.00104.85 C ANISOU 1898 CG LYS A 251 10333 14058 15447 881 -2876 -3435 C ATOM 1899 CD LYS A 251 -19.973 1.271 -17.910 1.00101.07 C ANISOU 1899 CD LYS A 251 10164 13864 14372 1116 -2945 -3513 C ATOM 1900 CE LYS A 251 -19.811 2.782 -18.029 1.00101.33 C ANISOU 1900 CE LYS A 251 10039 14174 14286 1321 -2870 -3150 C ATOM 1901 NZ LYS A 251 -21.035 3.453 -18.545 1.00117.79 N1+ ANISOU 1901 NZ LYS A 251 11740 16444 16570 1238 -3201 -2966 N1+ ATOM 1902 N PRO A 252 -20.369 -0.017 -12.468 1.00107.65 N ANISOU 1902 N PRO A 252 10727 13480 16696 723 -1623 -3147 N ATOM 1903 CA PRO A 252 -19.841 0.160 -11.108 1.00104.77 C ANISOU 1903 CA PRO A 252 10434 12934 16440 764 -1179 -2976 C ATOM 1904 C PRO A 252 -19.021 1.437 -10.996 1.00 89.53 C ANISOU 1904 C PRO A 252 8600 11173 14245 1063 -963 -2785 C ATOM 1905 O PRO A 252 -18.475 1.946 -11.977 1.00 94.57 O ANISOU 1905 O PRO A 252 9360 12033 14540 1246 -1126 -2809 O ATOM 1906 CB PRO A 252 -18.966 -1.081 -10.878 1.00 84.65 C ANISOU 1906 CB PRO A 252 8261 10094 13809 693 -1143 -3175 C ATOM 1907 CG PRO A 252 -19.127 -1.955 -12.065 1.00101.63 C ANISOU 1907 CG PRO A 252 10539 12233 15842 615 -1556 -3489 C ATOM 1908 CD PRO A 252 -20.034 -1.323 -13.059 1.00106.43 C ANISOU 1908 CD PRO A 252 10871 13147 16420 603 -1868 -3475 C ATOM 1909 N ILE A 253 -18.944 1.959 -9.769 1.00 76.51 N ANISOU 1909 N ILE A 253 6906 9421 12744 1089 -600 -2582 N ATOM 1910 CA ILE A 253 -18.298 3.254 -9.565 1.00 91.18 C ANISOU 1910 CA ILE A 253 8849 11393 14401 1335 -423 -2381 C ATOM 1911 C ILE A 253 -16.829 3.198 -9.959 1.00 86.89 C ANISOU 1911 C ILE A 253 8680 10887 13446 1476 -414 -2411 C ATOM 1912 O ILE A 253 -16.274 4.191 -10.443 1.00 83.78 O ANISOU 1912 O ILE A 253 8356 10687 12792 1660 -455 -2275 O ATOM 1913 CB ILE A 253 -18.483 3.731 -8.111 1.00 78.10 C ANISOU 1913 CB ILE A 253 7130 9591 12955 1320 -37 -2203 C ATOM 1914 CG1 ILE A 253 -17.911 5.141 -7.940 1.00 87.52 C ANISOU 1914 CG1 ILE A 253 8433 10859 13962 1561 86 -2009 C ATOM 1915 CG2 ILE A 253 -17.808 2.784 -7.152 1.00 84.41 C ANISOU 1915 CG2 ILE A 253 8170 10144 13758 1169 191 -2233 C ATOM 1916 CD1 ILE A 253 -18.910 6.240 -8.222 1.00 81.23 C ANISOU 1916 CD1 ILE A 253 7326 10199 13341 1703 -4 -1903 C ATOM 1917 N GLN A 254 -16.179 2.046 -9.784 1.00 78.80 N ANISOU 1917 N GLN A 254 7884 9688 12367 1396 -375 -2570 N ATOM 1918 CA GLN A 254 -14.792 1.921 -10.222 1.00 86.49 C ANISOU 1918 CA GLN A 254 9162 10740 12962 1564 -361 -2607 C ATOM 1919 C GLN A 254 -14.682 2.112 -11.729 1.00 89.48 C ANISOU 1919 C GLN A 254 9550 11430 13020 1695 -661 -2730 C ATOM 1920 O GLN A 254 -13.831 2.869 -12.210 1.00 81.06 O ANISOU 1920 O GLN A 254 8579 10607 11611 1871 -650 -2596 O ATOM 1921 CB GLN A 254 -14.221 0.564 -9.805 1.00 86.17 C ANISOU 1921 CB GLN A 254 9340 10426 12974 1486 -294 -2779 C ATOM 1922 CG GLN A 254 -15.201 -0.591 -9.900 1.00 89.81 C ANISOU 1922 CG GLN A 254 9718 10672 13732 1258 -482 -3007 C ATOM 1923 CD GLN A 254 -15.774 -0.979 -8.554 1.00 92.24 C ANISOU 1923 CD GLN A 254 9925 10700 14423 1013 -278 -2878 C ATOM 1924 NE2 GLN A 254 -15.242 -2.047 -7.973 1.00 81.98 N ANISOU 1924 NE2 GLN A 254 8840 9100 13211 920 -211 -2940 N ATOM 1925 OE1 GLN A 254 -16.681 -0.325 -8.039 1.00 94.04 O ANISOU 1925 OE1 GLN A 254 9880 10991 14860 920 -177 -2716 O ATOM 1926 N GLN A 255 -15.555 1.447 -12.489 1.00 92.70 N ANISOU 1926 N GLN A 255 9856 11850 13517 1582 -949 -2964 N ATOM 1927 CA GLN A 255 -15.536 1.589 -13.941 1.00 93.01 C ANISOU 1927 CA GLN A 255 9918 12204 13217 1679 -1259 -3096 C ATOM 1928 C GLN A 255 -15.878 3.014 -14.357 1.00 93.36 C ANISOU 1928 C GLN A 255 9762 12537 13174 1765 -1347 -2822 C ATOM 1929 O GLN A 255 -15.272 3.556 -15.291 1.00 83.44 O ANISOU 1929 O GLN A 255 8594 11596 11515 1908 -1464 -2766 O ATOM 1930 CB GLN A 255 -16.505 0.590 -14.575 1.00 93.48 C ANISOU 1930 CB GLN A 255 9918 12180 13419 1490 -1587 -3395 C ATOM 1931 CG GLN A 255 -16.044 0.048 -15.915 1.00104.69 C ANISOU 1931 CG GLN A 255 11568 13800 14409 1590 -1850 -3697 C ATOM 1932 CD GLN A 255 -17.195 -0.371 -16.807 1.00101.45 C ANISOU 1932 CD GLN A 255 11039 13444 14065 1396 -2277 -3900 C ATOM 1933 NE2 GLN A 255 -17.061 -0.113 -18.103 1.00103.90 N ANISOU 1933 NE2 GLN A 255 11427 14108 13940 1491 -2539 -4008 N ATOM 1934 OE1 GLN A 255 -18.187 -0.932 -16.341 1.00 95.33 O ANISOU 1934 OE1 GLN A 255 10097 12415 13710 1140 -2382 -3941 O ATOM 1935 N VAL A 256 -16.832 3.640 -13.662 1.00 92.72 N ANISOU 1935 N VAL A 256 9407 12354 13467 1690 -1286 -2636 N ATOM 1936 CA VAL A 256 -17.152 5.042 -13.922 1.00 88.06 C ANISOU 1936 CA VAL A 256 8640 11959 12858 1807 -1361 -2361 C ATOM 1937 C VAL A 256 -15.904 5.902 -13.764 1.00 68.07 C ANISOU 1937 C VAL A 256 6330 9515 10017 1975 -1184 -2138 C ATOM 1938 O VAL A 256 -15.416 6.497 -14.731 1.00 85.27 O ANISOU 1938 O VAL A 256 8572 11985 11841 2074 -1361 -2032 O ATOM 1939 CB VAL A 256 -18.286 5.522 -12.999 1.00 94.58 C ANISOU 1939 CB VAL A 256 9152 12620 14163 1755 -1241 -2223 C ATOM 1940 CG1 VAL A 256 -18.523 7.014 -13.184 1.00 84.35 C ANISOU 1940 CG1 VAL A 256 7719 11457 12875 1931 -1307 -1944 C ATOM 1941 CG2 VAL A 256 -19.561 4.740 -13.272 1.00 74.95 C ANISOU 1941 CG2 VAL A 256 6379 10116 11982 1559 -1463 -2383 C ATOM 1942 N ILE A 257 -15.354 5.948 -12.544 1.00 74.34 N ANISOU 1942 N ILE A 257 7247 10076 10924 1977 -848 -2046 N ATOM 1943 CA ILE A 257 -14.199 6.800 -12.254 1.00 84.80 C ANISOU 1943 CA ILE A 257 8771 11452 11998 2090 -695 -1799 C ATOM 1944 C ILE A 257 -13.046 6.507 -13.207 1.00 83.90 C ANISOU 1944 C ILE A 257 8846 11617 11416 2170 -782 -1832 C ATOM 1945 O ILE A 257 -12.310 7.416 -13.611 1.00 92.02 O ANISOU 1945 O ILE A 257 9944 12864 12155 2253 -824 -1583 O ATOM 1946 CB ILE A 257 -13.767 6.636 -10.783 1.00 81.37 C ANISOU 1946 CB ILE A 257 8467 10715 11733 2037 -345 -1740 C ATOM 1947 CG1 ILE A 257 -14.951 6.858 -9.836 1.00 71.99 C ANISOU 1947 CG1 ILE A 257 7077 9304 10970 1969 -215 -1734 C ATOM 1948 CG2 ILE A 257 -12.626 7.588 -10.452 1.00 83.39 C ANISOU 1948 CG2 ILE A 257 8924 11012 11747 2114 -233 -1458 C ATOM 1949 CD1 ILE A 257 -14.547 7.128 -8.397 1.00 71.59 C ANISOU 1949 CD1 ILE A 257 7176 9012 11014 1937 120 -1610 C ATOM 1950 N ALA A 258 -12.871 5.239 -13.588 1.00 76.34 N ANISOU 1950 N ALA A 258 7972 10660 10373 2149 -813 -2135 N ATOM 1951 CA ALA A 258 -11.812 4.898 -14.532 1.00 79.02 C ANISOU 1951 CA ALA A 258 8476 11297 10250 2273 -865 -2215 C ATOM 1952 C ALA A 258 -12.071 5.527 -15.895 1.00 84.50 C ANISOU 1952 C ALA A 258 9086 12390 10630 2320 -1166 -2163 C ATOM 1953 O ALA A 258 -11.172 6.129 -16.492 1.00 95.82 O ANISOU 1953 O ALA A 258 10586 14156 11663 2417 -1174 -1966 O ATOM 1954 CB ALA A 258 -11.681 3.380 -14.648 1.00 66.09 C ANISOU 1954 CB ALA A 258 6972 9518 8624 2273 -855 -2603 C ATOM 1955 N GLU A 259 -13.301 5.406 -16.400 1.00 83.20 N ANISOU 1955 N GLU A 259 8757 12219 10636 2228 -1430 -2301 N ATOM 1956 CA GLU A 259 -13.630 6.008 -17.686 1.00 77.54 C ANISOU 1956 CA GLU A 259 7955 11879 9628 2246 -1757 -2225 C ATOM 1957 C GLU A 259 -13.607 7.532 -17.641 1.00 92.39 C ANISOU 1957 C GLU A 259 9730 13871 11503 2282 -1803 -1786 C ATOM 1958 O GLU A 259 -13.439 8.165 -18.689 1.00 96.61 O ANISOU 1958 O GLU A 259 10252 14769 11686 2312 -2032 -1621 O ATOM 1959 CB GLU A 259 -14.995 5.512 -18.162 1.00 81.57 C ANISOU 1959 CB GLU A 259 8291 12335 10366 2111 -2061 -2447 C ATOM 1960 CG GLU A 259 -14.960 4.117 -18.767 1.00 95.81 C ANISOU 1960 CG GLU A 259 10263 14142 12000 2069 -2176 -2890 C ATOM 1961 CD GLU A 259 -16.323 3.457 -18.794 1.00104.93 C ANISOU 1961 CD GLU A 259 11247 15095 13528 1863 -2428 -3098 C ATOM 1962 OE1 GLU A 259 -17.214 3.965 -19.506 1.00115.07 O ANISOU 1962 OE1 GLU A 259 12326 16569 14826 1785 -2754 -3006 O ATOM 1963 OE2 GLU A 259 -16.503 2.431 -18.105 1.00 98.17 O1- ANISOU 1963 OE2 GLU A 259 10449 13892 12958 1761 -2321 -3323 O1- ATOM 1964 N MET A 260 -13.772 8.134 -16.460 1.00 92.37 N ANISOU 1964 N MET A 260 9674 13555 11868 2277 -1604 -1595 N ATOM 1965 CA MET A 260 -13.653 9.583 -16.333 1.00 85.35 C ANISOU 1965 CA MET A 260 8750 12692 10987 2328 -1650 -1197 C ATOM 1966 C MET A 260 -12.210 10.066 -16.382 1.00 88.32 C ANISOU 1966 C MET A 260 9332 13249 10975 2368 -1529 -947 C ATOM 1967 O MET A 260 -11.973 11.231 -16.716 1.00 83.88 O ANISOU 1967 O MET A 260 8772 12819 10281 2380 -1675 -596 O ATOM 1968 CB MET A 260 -14.282 10.075 -15.024 1.00 82.37 C ANISOU 1968 CB MET A 260 8288 11909 11101 2332 -1463 -1116 C ATOM 1969 CG MET A 260 -15.607 9.439 -14.652 1.00 92.09 C ANISOU 1969 CG MET A 260 9283 12943 12764 2274 -1469 -1352 C ATOM 1970 SD MET A 260 -16.404 10.207 -13.225 1.00 88.76 S ANISOU 1970 SD MET A 260 8720 12146 12859 2330 -1231 -1233 S ATOM 1971 CE MET A 260 -15.614 11.815 -13.204 1.00 77.13 C ANISOU 1971 CE MET A 260 7434 10669 11204 2459 -1275 -846 C ATOM 1972 N THR A 261 -11.247 9.203 -16.060 1.00 87.68 N ANISOU 1972 N THR A 261 9409 13177 10729 2383 -1287 -1092 N ATOM 1973 CA THR A 261 -9.869 9.623 -15.838 1.00 90.35 C ANISOU 1973 CA THR A 261 9897 13649 10783 2407 -1126 -824 C ATOM 1974 C THR A 261 -8.862 8.882 -16.709 1.00 91.17 C ANISOU 1974 C THR A 261 10075 14157 10410 2488 -1085 -939 C ATOM 1975 O THR A 261 -7.656 8.968 -16.446 1.00 94.85 O ANISOU 1975 O THR A 261 10626 14748 10664 2518 -905 -751 O ATOM 1976 CB THR A 261 -9.502 9.443 -14.363 1.00 85.44 C ANISOU 1976 CB THR A 261 9382 12637 10445 2371 -824 -808 C ATOM 1977 CG2 THR A 261 -10.256 10.441 -13.499 1.00 81.43 C ANISOU 1977 CG2 THR A 261 8839 11795 10307 2326 -829 -636 C ATOM 1978 OG1 THR A 261 -9.848 8.115 -13.954 1.00 78.70 O ANISOU 1978 OG1 THR A 261 8535 11577 9792 2368 -687 -1185 O ATOM 1979 N ASP A 262 -9.321 8.158 -17.733 1.00 97.78 N ANISOU 1979 N ASP A 262 10879 15210 11063 2531 -1249 -1244 N ATOM 1980 CA ASP A 262 -8.447 7.423 -18.649 1.00 97.80 C ANISOU 1980 CA ASP A 262 10968 15617 10576 2654 -1204 -1422 C ATOM 1981 C ASP A 262 -7.566 6.431 -17.883 1.00 89.69 C ANISOU 1981 C ASP A 262 10060 14410 9609 2756 -887 -1605 C ATOM 1982 O ASP A 262 -6.338 6.532 -17.853 1.00103.61 O ANISOU 1982 O ASP A 262 11856 16411 11100 2846 -704 -1417 O ATOM 1983 CB ASP A 262 -7.609 8.394 -19.495 1.00105.80 C ANISOU 1983 CB ASP A 262 11950 17153 11095 2667 -1278 -1028 C ATOM 1984 CG ASP A 262 -6.675 7.683 -20.459 1.00121.78 C ANISOU 1984 CG ASP A 262 14034 19675 12562 2826 -1184 -1203 C ATOM 1985 OD1 ASP A 262 -7.029 6.586 -20.941 1.00122.82 O ANISOU 1985 OD1 ASP A 262 14244 19804 12618 2922 -1216 -1678 O ATOM 1986 OD2 ASP A 262 -5.583 8.225 -20.732 1.00129.76 O1- ANISOU 1986 OD2 ASP A 262 15014 21082 13208 2856 -1080 -866 O1- ATOM 1987 N GLY A 263 -8.227 5.467 -17.237 1.00 81.67 N ANISOU 1987 N GLY A 263 9087 12965 8980 2727 -839 -1942 N ATOM 1988 CA GLY A 263 -7.563 4.384 -16.531 1.00 72.47 C ANISOU 1988 CA GLY A 263 8046 11561 7929 2817 -594 -2148 C ATOM 1989 C GLY A 263 -7.804 4.381 -15.034 1.00 79.29 C ANISOU 1989 C GLY A 263 8915 11932 9278 2686 -428 -2039 C ATOM 1990 O GLY A 263 -7.760 3.316 -14.408 1.00 74.91 O ANISOU 1990 O GLY A 263 8452 11061 8950 2695 -309 -2272 O ATOM 1991 N GLY A 264 -8.047 5.548 -14.446 1.00 79.08 N ANISOU 1991 N GLY A 264 8815 11829 9403 2568 -425 -1692 N ATOM 1992 CA GLY A 264 -8.220 5.627 -13.006 1.00 78.04 C ANISOU 1992 CA GLY A 264 8714 11276 9661 2452 -244 -1586 C ATOM 1993 C GLY A 264 -7.626 6.880 -12.402 1.00 77.32 C ANISOU 1993 C GLY A 264 8651 11203 9523 2398 -169 -1158 C ATOM 1994 O GLY A 264 -6.821 7.566 -13.036 1.00 76.35 O ANISOU 1994 O GLY A 264 8527 11424 9057 2444 -231 -905 O ATOM 1995 N VAL A 265 -8.018 7.196 -11.164 1.00 69.99 N ANISOU 1995 N VAL A 265 7759 9910 8924 2283 -44 -1068 N ATOM 1996 CA VAL A 265 -7.510 8.390 -10.504 1.00 74.36 C ANISOU 1996 CA VAL A 265 8397 10409 9449 2215 1 -698 C ATOM 1997 C VAL A 265 -6.081 8.149 -10.026 1.00 77.38 C ANISOU 1997 C VAL A 265 8905 10855 9643 2204 157 -513 C ATOM 1998 O VAL A 265 -5.619 7.013 -9.888 1.00 68.66 O ANISOU 1998 O VAL A 265 7825 9727 8535 2259 281 -688 O ATOM 1999 CB VAL A 265 -8.424 8.811 -9.342 1.00 63.69 C ANISOU 1999 CB VAL A 265 7065 8663 8470 2121 98 -703 C ATOM 2000 CG1 VAL A 265 -9.607 9.615 -9.857 1.00 83.56 C ANISOU 2000 CG1 VAL A 265 9430 11187 11131 2162 -91 -714 C ATOM 2001 CG2 VAL A 265 -8.897 7.592 -8.565 1.00 73.07 C ANISOU 2001 CG2 VAL A 265 8249 9586 9929 2062 276 -978 C ATOM 2002 N ASP A 266 -5.369 9.249 -9.772 1.00 76.37 N ANISOU 2002 N ASP A 266 8852 10792 9372 2128 125 -135 N ATOM 2003 CA ASP A 266 -4.022 9.135 -9.223 1.00 68.21 C ANISOU 2003 CA ASP A 266 7910 9822 8186 2079 247 105 C ATOM 2004 C ASP A 266 -4.062 8.727 -7.756 1.00 71.91 C ANISOU 2004 C ASP A 266 8520 9879 8922 1966 433 62 C ATOM 2005 O ASP A 266 -3.268 7.888 -7.317 1.00 72.71 O ANISOU 2005 O ASP A 266 8654 9967 9005 1975 564 64 O ATOM 2006 CB ASP A 266 -3.268 10.453 -9.393 1.00 64.49 C ANISOU 2006 CB ASP A 266 7480 9537 7487 1975 110 555 C ATOM 2007 CG ASP A 266 -3.075 10.829 -10.848 1.00 68.09 C ANISOU 2007 CG ASP A 266 7789 10464 7620 2057 -67 667 C ATOM 2008 OD1 ASP A 266 -2.554 9.994 -11.616 1.00 82.91 O ANISOU 2008 OD1 ASP A 266 9551 12685 9266 2199 -3 542 O ATOM 2009 OD2 ASP A 266 -3.450 11.958 -11.226 1.00 75.70 O1- ANISOU 2009 OD2 ASP A 266 8761 11451 8550 1987 -273 876 O1- ATOM 2010 N ARG A 267 -4.980 9.307 -6.985 1.00 65.27 N ANISOU 2010 N ARG A 267 7761 8716 8323 1872 449 28 N ATOM 2011 CA ARG A 267 -5.126 8.986 -5.574 1.00 63.35 C ANISOU 2011 CA ARG A 267 7662 8113 8293 1747 637 -14 C ATOM 2012 C ARG A 267 -6.599 8.795 -5.250 1.00 70.26 C ANISOU 2012 C ARG A 267 8469 8751 9476 1754 704 -299 C ATOM 2013 O ARG A 267 -7.474 9.365 -5.905 1.00 67.49 O ANISOU 2013 O ARG A 267 7996 8455 9191 1835 579 -373 O ATOM 2014 CB ARG A 267 -4.548 10.087 -4.674 1.00 57.09 C ANISOU 2014 CB ARG A 267 7088 7178 7426 1591 629 304 C ATOM 2015 CG ARG A 267 -3.090 10.413 -4.931 1.00 72.62 C ANISOU 2015 CG ARG A 267 9092 9397 9103 1531 535 662 C ATOM 2016 CD ARG A 267 -2.187 9.251 -4.575 1.00 64.17 C ANISOU 2016 CD ARG A 267 7997 8386 7998 1532 669 670 C ATOM 2017 NE ARG A 267 -0.784 9.641 -4.607 1.00 67.34 N ANISOU 2017 NE ARG A 267 8409 9023 8155 1450 595 1065 N ATOM 2018 CZ ARG A 267 0.025 9.439 -5.637 1.00 74.19 C ANISOU 2018 CZ ARG A 267 9083 10312 8795 1575 545 1186 C ATOM 2019 NH1 ARG A 267 -0.394 8.831 -6.736 1.00 75.70 N1+ ANISOU 2019 NH1 ARG A 267 9101 10720 8941 1795 554 913 N1+ ATOM 2020 NH2 ARG A 267 1.285 9.857 -5.565 1.00 69.89 N ANISOU 2020 NH2 ARG A 267 8513 9997 8045 1469 484 1596 N ATOM 2021 N SER A 268 -6.866 7.985 -4.229 1.00 65.61 N ANISOU 2021 N SER A 268 7936 7916 9078 1659 895 -426 N ATOM 2022 CA SER A 268 -8.224 7.861 -3.716 1.00 64.21 C ANISOU 2022 CA SER A 268 7674 7534 9190 1627 1001 -636 C ATOM 2023 C SER A 268 -8.188 7.784 -2.198 1.00 62.99 C ANISOU 2023 C SER A 268 7700 7117 9119 1463 1227 -576 C ATOM 2024 O SER A 268 -7.196 7.355 -1.609 1.00 68.33 O ANISOU 2024 O SER A 268 8534 7746 9683 1361 1286 -435 O ATOM 2025 CB SER A 268 -8.954 6.639 -4.289 1.00 60.43 C ANISOU 2025 CB SER A 268 6997 7077 8886 1657 975 -924 C ATOM 2026 OG SER A 268 -8.525 5.444 -3.665 1.00 78.67 O ANISOU 2026 OG SER A 268 9386 9242 11262 1557 1094 -976 O ATOM 2027 N VAL A 269 -9.280 8.222 -1.571 1.00 63.45 N ANISOU 2027 N VAL A 269 7721 7027 9359 1447 1354 -675 N ATOM 2028 CA VAL A 269 -9.417 8.216 -0.116 1.00 67.02 C ANISOU 2028 CA VAL A 269 8344 7267 9856 1295 1598 -647 C ATOM 2029 C VAL A 269 -10.825 7.751 0.232 1.00 76.28 C ANISOU 2029 C VAL A 269 9294 8379 11309 1278 1768 -860 C ATOM 2030 O VAL A 269 -11.808 8.389 -0.164 1.00 77.13 O ANISOU 2030 O VAL A 269 9217 8532 11557 1419 1745 -963 O ATOM 2031 CB VAL A 269 -9.146 9.596 0.512 1.00 80.54 C ANISOU 2031 CB VAL A 269 10310 8871 11422 1300 1616 -500 C ATOM 2032 CG1 VAL A 269 -9.298 9.521 2.023 1.00 61.42 C ANISOU 2032 CG1 VAL A 269 8090 6257 8989 1140 1880 -506 C ATOM 2033 CG2 VAL A 269 -7.758 10.101 0.146 1.00 67.59 C ANISOU 2033 CG2 VAL A 269 8857 7312 9513 1268 1414 -235 C ATOM 2034 N GLU A 270 -10.922 6.659 0.988 1.00 68.64 N ANISOU 2034 N GLU A 270 8329 7317 10435 1097 1927 -893 N ATOM 2035 CA GLU A 270 -12.196 6.085 1.404 1.00 70.72 C ANISOU 2035 CA GLU A 270 8359 7549 10960 1015 2097 -1041 C ATOM 2036 C GLU A 270 -12.522 6.560 2.816 1.00 61.46 C ANISOU 2036 C GLU A 270 7326 6283 9743 918 2399 -993 C ATOM 2037 O GLU A 270 -11.778 6.269 3.758 1.00 68.34 O ANISOU 2037 O GLU A 270 8458 7052 10456 741 2504 -859 O ATOM 2038 CB GLU A 270 -12.140 4.557 1.349 1.00 71.28 C ANISOU 2038 CB GLU A 270 8355 7561 11166 845 2059 -1086 C ATOM 2039 CG GLU A 270 -13.483 3.888 1.118 1.00 72.38 C ANISOU 2039 CG GLU A 270 8160 7728 11612 773 2076 -1246 C ATOM 2040 CD GLU A 270 -14.444 4.090 2.273 1.00 73.36 C ANISOU 2040 CD GLU A 270 8179 7845 11848 652 2386 -1223 C ATOM 2041 OE1 GLU A 270 -14.148 3.607 3.386 1.00 85.66 O ANISOU 2041 OE1 GLU A 270 9904 9298 13345 441 2574 -1107 O ATOM 2042 OE2 GLU A 270 -15.489 4.742 2.070 1.00 70.02 O1- ANISOU 2042 OE2 GLU A 270 7497 7542 11565 778 2447 -1310 O1- ATOM 2043 N CYS A 271 -13.644 7.269 2.964 1.00 73.06 N ANISOU 2043 N CYS A 271 8616 7800 11344 1044 2540 -1105 N ATOM 2044 CA CYS A 271 -14.006 7.881 4.236 1.00 77.71 C ANISOU 2044 CA CYS A 271 9347 8330 11850 1021 2852 -1108 C ATOM 2045 C CYS A 271 -15.343 7.419 4.800 1.00 72.64 C ANISOU 2045 C CYS A 271 8384 7783 11432 960 3133 -1211 C ATOM 2046 O CYS A 271 -15.717 7.862 5.893 1.00 73.32 O ANISOU 2046 O CYS A 271 8566 7868 11426 953 3443 -1235 O ATOM 2047 CB CYS A 271 -14.025 9.411 4.103 1.00 66.58 C ANISOU 2047 CB CYS A 271 8078 6871 10348 1283 2812 -1142 C ATOM 2048 SG CYS A 271 -12.474 10.136 3.531 1.00 72.85 S ANISOU 2048 SG CYS A 271 9241 7577 10861 1309 2482 -956 S ATOM 2049 N THR A 272 -16.080 6.551 4.103 1.00 74.10 N ANISOU 2049 N THR A 272 8194 8069 11893 904 3036 -1268 N ATOM 2050 CA THR A 272 -17.346 6.078 4.654 1.00 78.56 C ANISOU 2050 CA THR A 272 8408 8759 12682 799 3294 -1313 C ATOM 2051 C THR A 272 -17.139 4.935 5.638 1.00 77.67 C ANISOU 2051 C THR A 272 8391 8596 12525 437 3458 -1188 C ATOM 2052 O THR A 272 -17.793 4.888 6.686 1.00 75.56 O ANISOU 2052 O THR A 272 8037 8424 12247 322 3798 -1158 O ATOM 2053 CB THR A 272 -18.289 5.633 3.536 1.00 74.68 C ANISOU 2053 CB THR A 272 7461 8393 12520 838 3085 -1396 C ATOM 2054 CG2 THR A 272 -18.321 6.658 2.424 1.00 68.28 C ANISOU 2054 CG2 THR A 272 6590 7623 11730 1164 2839 -1473 C ATOM 2055 OG1 THR A 272 -17.848 4.375 3.009 1.00 73.57 O ANISOU 2055 OG1 THR A 272 7342 8171 12442 610 2839 -1368 O ATOM 2056 N GLY A 273 -16.241 4.007 5.320 1.00 87.58 N ANISOU 2056 N GLY A 273 9819 9711 13748 266 3225 -1107 N ATOM 2057 CA GLY A 273 -16.046 2.817 6.116 1.00 80.39 C ANISOU 2057 CA GLY A 273 8986 8708 12851 -80 3304 -964 C ATOM 2058 C GLY A 273 -16.684 1.570 5.546 1.00 84.06 C ANISOU 2058 C GLY A 273 9152 9149 13637 -273 3132 -984 C ATOM 2059 O GLY A 273 -16.458 0.479 6.081 1.00 90.65 O ANISOU 2059 O GLY A 273 10071 9850 14522 -571 3122 -849 O ATOM 2060 N SER A 274 -17.475 1.697 4.485 1.00 87.63 N ANISOU 2060 N SER A 274 9274 9708 14312 -130 2964 -1133 N ATOM 2061 CA SER A 274 -18.043 0.526 3.835 1.00 87.62 C ANISOU 2061 CA SER A 274 9027 9656 14607 -329 2729 -1171 C ATOM 2062 C SER A 274 -16.928 -0.308 3.215 1.00 90.14 C ANISOU 2062 C SER A 274 9640 9735 14875 -353 2414 -1202 C ATOM 2063 O SER A 274 -16.096 0.209 2.464 1.00 80.69 O ANISOU 2063 O SER A 274 8624 8534 13502 -94 2251 -1285 O ATOM 2064 CB SER A 274 -19.057 0.949 2.772 1.00 82.55 C ANISOU 2064 CB SER A 274 7992 9195 14176 -159 2575 -1321 C ATOM 2065 OG SER A 274 -19.384 -0.127 1.911 1.00 86.27 O ANISOU 2065 OG SER A 274 8317 9581 14881 -330 2244 -1396 O ATOM 2066 N VAL A 275 -16.896 -1.600 3.554 1.00 82.22 N ANISOU 2066 N VAL A 275 8681 8534 14024 -659 2333 -1119 N ATOM 2067 CA VAL A 275 -15.875 -2.487 3.002 1.00 86.56 C ANISOU 2067 CA VAL A 275 9504 8823 14562 -647 2041 -1169 C ATOM 2068 C VAL A 275 -15.986 -2.542 1.486 1.00 82.02 C ANISOU 2068 C VAL A 275 8832 8277 14055 -440 1713 -1425 C ATOM 2069 O VAL A 275 -14.975 -2.561 0.767 1.00 86.50 O ANISOU 2069 O VAL A 275 9624 8784 14459 -218 1536 -1526 O ATOM 2070 CB VAL A 275 -15.989 -3.888 3.630 1.00 95.22 C ANISOU 2070 CB VAL A 275 10652 9656 15872 -1021 1980 -1034 C ATOM 2071 CG1 VAL A 275 -14.885 -4.793 3.107 1.00 82.30 C ANISOU 2071 CG1 VAL A 275 9320 7713 14239 -947 1689 -1103 C ATOM 2072 CG2 VAL A 275 -15.936 -3.787 5.144 1.00102.71 C ANISOU 2072 CG2 VAL A 275 11687 10632 16705 -1250 2314 -756 C ATOM 2073 N GLN A 276 -17.217 -2.566 0.972 1.00 83.95 N ANISOU 2073 N GLN A 276 8726 8649 14524 -516 1625 -1521 N ATOM 2074 CA GLN A 276 -17.399 -2.410 -0.462 1.00 84.35 C ANISOU 2074 CA GLN A 276 8676 8788 14584 -316 1317 -1753 C ATOM 2075 C GLN A 276 -16.765 -1.110 -0.939 1.00 82.19 C ANISOU 2075 C GLN A 276 8497 8715 14017 50 1363 -1785 C ATOM 2076 O GLN A 276 -16.067 -1.095 -1.959 1.00 81.56 O ANISOU 2076 O GLN A 276 8566 8649 13775 254 1136 -1925 O ATOM 2077 CB GLN A 276 -18.886 -2.456 -0.821 1.00 87.99 C ANISOU 2077 CB GLN A 276 8699 9402 15330 -467 1229 -1794 C ATOM 2078 CG GLN A 276 -19.400 -3.842 -1.234 1.00106.24 C ANISOU 2078 CG GLN A 276 10951 11499 17919 -779 914 -1879 C ATOM 2079 CD GLN A 276 -18.580 -4.507 -2.337 1.00117.86 C ANISOU 2079 CD GLN A 276 12732 12766 19283 -645 552 -2132 C ATOM 2080 NE2 GLN A 276 -18.041 -3.705 -3.250 1.00110.17 N ANISOU 2080 NE2 GLN A 276 11842 11973 18044 -295 473 -2274 N ATOM 2081 OE1 GLN A 276 -18.461 -5.733 -2.380 1.00122.40 O ANISOU 2081 OE1 GLN A 276 13469 13026 20012 -854 340 -2198 O ATOM 2082 N ALA A 277 -16.974 -0.015 -0.199 1.00 84.24 N ANISOU 2082 N ALA A 277 8688 9126 14192 135 1654 -1654 N ATOM 2083 CA ALA A 277 -16.379 1.262 -0.587 1.00 76.48 C ANISOU 2083 CA ALA A 277 7821 8285 12952 449 1669 -1652 C ATOM 2084 C ALA A 277 -14.862 1.184 -0.615 1.00 73.88 C ANISOU 2084 C ALA A 277 7873 7853 12346 543 1621 -1601 C ATOM 2085 O ALA A 277 -14.219 1.798 -1.471 1.00 74.38 O ANISOU 2085 O ALA A 277 8026 8029 12206 773 1473 -1636 O ATOM 2086 CB ALA A 277 -16.847 2.375 0.353 1.00 61.00 C ANISOU 2086 CB ALA A 277 5783 6431 10962 514 1991 -1540 C ATOM 2087 N MET A 278 -14.275 0.424 0.306 1.00 77.62 N ANISOU 2087 N MET A 278 8555 8949 11989 801 2133 -488 N ATOM 2088 CA MET A 278 -12.828 0.246 0.310 1.00 79.20 C ANISOU 2088 CA MET A 278 9114 9199 11780 730 1912 -657 C ATOM 2089 C MET A 278 -12.368 -0.497 -0.937 1.00 73.53 C ANISOU 2089 C MET A 278 8110 8807 11022 588 1493 -896 C ATOM 2090 O MET A 278 -11.380 -0.111 -1.579 1.00 73.54 O ANISOU 2090 O MET A 278 8212 9021 10708 582 1244 -971 O ATOM 2091 CB MET A 278 -12.407 -0.509 1.567 1.00 71.04 C ANISOU 2091 CB MET A 278 8468 7837 10686 697 2134 -685 C ATOM 2092 CG MET A 278 -12.762 0.228 2.829 1.00 66.22 C ANISOU 2092 CG MET A 278 8239 6916 10006 828 2559 -487 C ATOM 2093 SD MET A 278 -12.754 -0.859 4.255 1.00 79.53 S ANISOU 2093 SD MET A 278 10276 8238 11703 807 2882 -451 S ATOM 2094 CE MET A 278 -12.226 0.302 5.497 1.00 88.43 C ANISOU 2094 CE MET A 278 12086 9158 12354 915 3125 -345 C ATOM 2095 N ILE A 279 -13.078 -1.570 -1.296 1.00 69.02 N ANISOU 2095 N ILE A 279 7186 8261 10779 462 1440 -1031 N ATOM 2096 CA ILE A 279 -12.732 -2.317 -2.505 1.00 71.49 C ANISOU 2096 CA ILE A 279 7251 8866 11044 307 1069 -1313 C ATOM 2097 C ILE A 279 -12.812 -1.411 -3.730 1.00 75.19 C ANISOU 2097 C ILE A 279 7501 9759 11310 357 776 -1270 C ATOM 2098 O ILE A 279 -11.903 -1.388 -4.573 1.00 82.68 O ANISOU 2098 O ILE A 279 8517 10957 11939 322 521 -1419 O ATOM 2099 CB ILE A 279 -13.639 -3.552 -2.654 1.00 79.68 C ANISOU 2099 CB ILE A 279 7932 9822 12519 130 1080 -1486 C ATOM 2100 CG1 ILE A 279 -13.387 -4.541 -1.514 1.00 76.85 C ANISOU 2100 CG1 ILE A 279 7827 9036 12337 92 1380 -1510 C ATOM 2101 CG2 ILE A 279 -13.416 -4.220 -4.002 1.00 64.33 C ANISOU 2101 CG2 ILE A 279 5738 8202 10500 -48 692 -1823 C ATOM 2102 CD1 ILE A 279 -14.423 -5.639 -1.423 1.00 66.32 C ANISOU 2102 CD1 ILE A 279 6154 7513 11532 -72 1513 -1608 C ATOM 2103 N GLN A 280 -13.898 -0.636 -3.838 1.00 78.40 N ANISOU 2103 N GLN A 280 7639 10244 11907 461 838 -1028 N ATOM 2104 CA GLN A 280 -14.069 0.244 -4.994 1.00 77.33 C ANISOU 2104 CA GLN A 280 7273 10518 11589 541 562 -911 C ATOM 2105 C GLN A 280 -13.009 1.341 -5.026 1.00 77.89 C ANISOU 2105 C GLN A 280 7709 10619 11265 683 586 -776 C ATOM 2106 O GLN A 280 -12.497 1.682 -6.099 1.00 65.60 O ANISOU 2106 O GLN A 280 6108 9407 9411 690 316 -803 O ATOM 2107 CB GLN A 280 -15.479 0.850 -5.022 1.00 80.23 C ANISOU 2107 CB GLN A 280 7237 10933 12313 659 647 -616 C ATOM 2108 CG GLN A 280 -16.613 -0.142 -4.743 1.00 84.82 C ANISOU 2108 CG GLN A 280 7433 11394 13399 517 713 -697 C ATOM 2109 CD GLN A 280 -17.885 0.511 -4.187 1.00 90.04 C ANISOU 2109 CD GLN A 280 7804 11897 14509 685 1017 -336 C ATOM 2110 NE2 GLN A 280 -18.840 0.777 -5.062 1.00 82.79 N ANISOU 2110 NE2 GLN A 280 6340 11317 13800 705 752 -191 N ATOM 2111 OE1 GLN A 280 -18.023 0.717 -2.999 1.00 86.32 O ANISOU 2111 OE1 GLN A 280 7585 11016 14197 794 1482 -191 O ATOM 2112 N ALA A 281 -12.655 1.896 -3.864 1.00 75.21 N ANISOU 2112 N ALA A 281 7747 9920 10910 780 914 -642 N ATOM 2113 CA ALA A 281 -11.657 2.959 -3.826 1.00 71.29 C ANISOU 2113 CA ALA A 281 7588 9406 10094 872 943 -537 C ATOM 2114 C ALA A 281 -10.268 2.438 -4.162 1.00 75.64 C ANISOU 2114 C ALA A 281 8338 10060 10342 750 732 -775 C ATOM 2115 O ALA A 281 -9.459 3.172 -4.743 1.00 68.11 O ANISOU 2115 O ALA A 281 7485 9263 9132 788 626 -722 O ATOM 2116 CB ALA A 281 -11.656 3.631 -2.454 1.00 71.50 C ANISOU 2116 CB ALA A 281 7993 9011 10164 965 1331 -393 C ATOM 2117 N PHE A 282 -9.965 1.187 -3.807 1.00 79.45 N ANISOU 2117 N PHE A 282 8865 10433 10890 616 703 -1012 N ATOM 2118 CA PHE A 282 -8.697 0.614 -4.243 1.00 69.42 C ANISOU 2118 CA PHE A 282 7709 9269 9397 524 517 -1226 C ATOM 2119 C PHE A 282 -8.706 0.341 -5.741 1.00 67.51 C ANISOU 2119 C PHE A 282 7185 9433 9031 471 241 -1375 C ATOM 2120 O PHE A 282 -7.716 0.608 -6.432 1.00 71.30 O ANISOU 2120 O PHE A 282 7748 10101 9243 477 122 -1420 O ATOM 2121 CB PHE A 282 -8.385 -0.674 -3.485 1.00 66.04 C ANISOU 2121 CB PHE A 282 7391 8590 9109 426 587 -1404 C ATOM 2122 CG PHE A 282 -7.252 -1.456 -4.089 1.00 71.81 C ANISOU 2122 CG PHE A 282 8140 9433 9713 347 416 -1634 C ATOM 2123 CD1 PHE A 282 -5.976 -0.919 -4.142 1.00 68.09 C ANISOU 2123 CD1 PHE A 282 7864 9009 8999 381 352 -1593 C ATOM 2124 CD2 PHE A 282 -7.468 -2.712 -4.632 1.00 66.56 C ANISOU 2124 CD2 PHE A 282 7279 8805 9207 233 343 -1899 C ATOM 2125 CE1 PHE A 282 -4.933 -1.627 -4.708 1.00 78.89 C ANISOU 2125 CE1 PHE A 282 9213 10464 10296 334 244 -1779 C ATOM 2126 CE2 PHE A 282 -6.427 -3.426 -5.200 1.00 69.65 C ANISOU 2126 CE2 PHE A 282 7698 9260 9505 183 248 -2117 C ATOM 2127 CZ PHE A 282 -5.159 -2.881 -5.239 1.00 74.98 C ANISOU 2127 CZ PHE A 282 8550 9990 9949 250 211 -2041 C ATOM 2128 N GLU A 283 -9.816 -0.186 -6.263 1.00 69.34 N ANISOU 2128 N GLU A 283 7085 9814 9447 409 138 -1456 N ATOM 2129 CA GLU A 283 -9.848 -0.585 -7.665 1.00 72.13 C ANISOU 2129 CA GLU A 283 7210 10571 9626 323 -158 -1659 C ATOM 2130 C GLU A 283 -9.959 0.600 -8.617 1.00 72.59 C ANISOU 2130 C GLU A 283 7175 10995 9411 453 -305 -1424 C ATOM 2131 O GLU A 283 -9.654 0.449 -9.805 1.00 63.82 O ANISOU 2131 O GLU A 283 5992 10250 8006 410 -534 -1562 O ATOM 2132 CB GLU A 283 -11.003 -1.558 -7.905 1.00 69.54 C ANISOU 2132 CB GLU A 283 6542 10290 9591 169 -268 -1852 C ATOM 2133 CG GLU A 283 -10.686 -2.991 -7.506 1.00 75.45 C ANISOU 2133 CG GLU A 283 7359 10769 10541 -1 -188 -2185 C ATOM 2134 CD GLU A 283 -11.889 -3.908 -7.606 1.00 88.20 C ANISOU 2134 CD GLU A 283 8628 12350 12535 -182 -250 -2365 C ATOM 2135 OE1 GLU A 283 -12.751 -3.673 -8.478 1.00 91.75 O ANISOU 2135 OE1 GLU A 283 8746 13146 12969 -237 -509 -2373 O ATOM 2136 OE2 GLU A 283 -11.967 -4.871 -6.813 1.00 92.03 O1- ANISOU 2136 OE2 GLU A 283 9158 12462 13348 -275 -46 -2482 O1- ATOM 2137 N CYS A 284 -10.373 1.771 -8.135 1.00 62.26 N ANISOU 2137 N CYS A 284 5890 9583 8182 622 -149 -1065 N ATOM 2138 CA CYS A 284 -10.615 2.904 -9.020 1.00 72.78 C ANISOU 2138 CA CYS A 284 7101 11230 9322 776 -259 -775 C ATOM 2139 C CYS A 284 -9.370 3.739 -9.298 1.00 68.63 C ANISOU 2139 C CYS A 284 6864 10731 8483 856 -195 -665 C ATOM 2140 O CYS A 284 -9.426 4.627 -10.155 1.00 78.66 O ANISOU 2140 O CYS A 284 8060 12274 9555 985 -273 -417 O ATOM 2141 CB CYS A 284 -11.716 3.802 -8.444 1.00 78.96 C ANISOU 2141 CB CYS A 284 7737 11858 10407 945 -76 -413 C ATOM 2142 SG CYS A 284 -11.179 4.931 -7.140 1.00 72.32 S ANISOU 2142 SG CYS A 284 7312 10520 9645 1084 353 -182 S ATOM 2143 N VAL A 285 -8.256 3.486 -8.613 1.00 68.76 N ANISOU 2143 N VAL A 285 7180 10479 8468 784 -58 -813 N ATOM 2144 CA VAL A 285 -7.027 4.221 -8.893 1.00 74.58 C ANISOU 2144 CA VAL A 285 8135 11235 8967 825 -5 -724 C ATOM 2145 C VAL A 285 -6.343 3.621 -10.115 1.00 72.92 C ANISOU 2145 C VAL A 285 7868 11379 8460 760 -190 -927 C ATOM 2146 O VAL A 285 -6.505 2.436 -10.432 1.00 63.53 O ANISOU 2146 O VAL A 285 6575 10297 7266 641 -323 -1238 O ATOM 2147 CB VAL A 285 -6.089 4.234 -7.668 1.00 66.89 C ANISOU 2147 CB VAL A 285 7467 9860 8089 763 172 -783 C ATOM 2148 CG1 VAL A 285 -6.854 4.622 -6.414 1.00 66.72 C ANISOU 2148 CG1 VAL A 285 7552 9487 8311 808 376 -654 C ATOM 2149 CG2 VAL A 285 -5.410 2.885 -7.489 1.00 60.80 C ANISOU 2149 CG2 VAL A 285 6730 9040 7330 626 96 -1107 C ATOM 2150 N HIS A 286 -5.581 4.455 -10.816 1.00 68.02 N ANISOU 2150 N HIS A 286 7331 10917 7598 838 -158 -755 N ATOM 2151 CA HIS A 286 -4.869 4.020 -12.009 1.00 67.13 C ANISOU 2151 CA HIS A 286 7209 11139 7160 805 -259 -913 C ATOM 2152 C HIS A 286 -3.813 2.979 -11.654 1.00 73.50 C ANISOU 2152 C HIS A 286 8129 11767 8030 677 -202 -1242 C ATOM 2153 O HIS A 286 -3.203 3.021 -10.584 1.00 72.35 O ANISOU 2153 O HIS A 286 8116 11271 8102 644 -78 -1228 O ATOM 2154 CB HIS A 286 -4.209 5.221 -12.691 1.00 63.99 C ANISOU 2154 CB HIS A 286 6895 10879 6541 930 -154 -598 C ATOM 2155 CG HIS A 286 -3.970 5.037 -14.158 1.00 65.40 C ANISOU 2155 CG HIS A 286 7034 11518 6299 961 -259 -643 C ATOM 2156 CD2 HIS A 286 -4.520 5.651 -15.232 1.00 80.31 C ANISOU 2156 CD2 HIS A 286 8838 13801 7874 1089 -370 -392 C ATOM 2157 ND1 HIS A 286 -3.057 4.135 -14.660 1.00 70.89 N ANISOU 2157 ND1 HIS A 286 7804 12306 6826 868 -236 -962 N ATOM 2158 CE1 HIS A 286 -3.058 4.198 -15.980 1.00 76.15 C ANISOU 2158 CE1 HIS A 286 8467 13405 7060 924 -309 -942 C ATOM 2159 NE2 HIS A 286 -3.938 5.110 -16.352 1.00 80.79 N ANISOU 2159 NE2 HIS A 286 8962 14205 7531 1057 -416 -587 N ATOM 2160 N ASP A 287 -3.603 2.031 -12.563 1.00 70.87 N ANISOU 2160 N ASP A 287 7749 11679 7501 609 -295 -1537 N ATOM 2161 CA ASP A 287 -2.517 1.086 -12.370 1.00 67.17 C ANISOU 2161 CA ASP A 287 7369 11040 7113 530 -193 -1811 C ATOM 2162 C ASP A 287 -1.175 1.766 -12.637 1.00 78.81 C ANISOU 2162 C ASP A 287 8947 12514 8482 594 -29 -1648 C ATOM 2163 O ASP A 287 -1.096 2.822 -13.273 1.00 83.06 O ANISOU 2163 O ASP A 287 9501 13248 8809 686 9 -1380 O ATOM 2164 CB ASP A 287 -2.690 -0.144 -13.267 1.00 63.57 C ANISOU 2164 CB ASP A 287 6857 10792 6505 435 -283 -2213 C ATOM 2165 CG ASP A 287 -2.809 0.204 -14.743 1.00 77.59 C ANISOU 2165 CG ASP A 287 8626 13047 7807 478 -375 -2212 C ATOM 2166 OD1 ASP A 287 -2.625 1.380 -15.112 1.00 82.05 O ANISOU 2166 OD1 ASP A 287 9224 13774 8179 605 -335 -1861 O ATOM 2167 OD2 ASP A 287 -3.087 -0.716 -15.542 1.00 77.19 O1- ANISOU 2167 OD2 ASP A 287 8560 13206 7564 378 -480 -2570 O1- ATOM 2168 N GLY A 288 -0.113 1.152 -12.130 1.00 72.15 N ANISOU 2168 N GLY A 288 8151 11435 7830 550 81 -1782 N ATOM 2169 CA GLY A 288 1.238 1.662 -12.286 1.00 70.23 C ANISOU 2169 CA GLY A 288 7942 11155 7588 585 240 -1644 C ATOM 2170 C GLY A 288 1.694 2.703 -11.280 1.00 71.45 C ANISOU 2170 C GLY A 288 8153 11048 7948 575 276 -1359 C ATOM 2171 O GLY A 288 2.874 2.739 -10.925 1.00 74.14 O ANISOU 2171 O GLY A 288 8481 11235 8453 543 353 -1321 O ATOM 2172 N TRP A 289 0.781 3.554 -10.808 1.00 71.55 N ANISOU 2172 N TRP A 289 8217 10997 7970 595 224 -1166 N ATOM 2173 CA TRP A 289 1.179 4.637 -9.916 1.00 72.90 C ANISOU 2173 CA TRP A 289 8491 10905 8301 567 283 -935 C ATOM 2174 C TRP A 289 0.090 5.023 -8.921 1.00 72.24 C ANISOU 2174 C TRP A 289 8507 10616 8326 570 249 -858 C ATOM 2175 O TRP A 289 0.346 5.799 -7.994 1.00 75.67 O ANISOU 2175 O TRP A 289 9084 10779 8886 522 302 -739 O ATOM 2176 CB TRP A 289 1.593 5.866 -10.733 1.00 78.14 C ANISOU 2176 CB TRP A 289 9152 11695 8842 626 416 -663 C ATOM 2177 CG TRP A 289 0.479 6.469 -11.544 1.00 82.33 C ANISOU 2177 CG TRP A 289 9656 12468 9158 756 413 -480 C ATOM 2178 CD1 TRP A 289 -0.550 7.237 -11.080 1.00 76.27 C ANISOU 2178 CD1 TRP A 289 8927 11586 8465 819 415 -288 C ATOM 2179 CD2 TRP A 289 0.291 6.360 -12.960 1.00 78.17 C ANISOU 2179 CD2 TRP A 289 9052 12351 8299 853 406 -447 C ATOM 2180 CE2 TRP A 289 -0.876 7.082 -13.282 1.00 72.94 C ANISOU 2180 CE2 TRP A 289 8355 11831 7528 974 352 -201 C ATOM 2181 CE3 TRP A 289 0.993 5.721 -13.987 1.00 79.23 C ANISOU 2181 CE3 TRP A 289 9157 12748 8200 858 454 -598 C ATOM 2182 NE1 TRP A 289 -1.370 7.607 -12.117 1.00 69.49 N ANISOU 2182 NE1 TRP A 289 7973 11048 7381 960 382 -104 N ATOM 2183 CZ2 TRP A 289 -1.355 7.184 -14.586 1.00 79.00 C ANISOU 2183 CZ2 TRP A 289 9054 13033 7929 1091 282 -86 C ATOM 2184 CZ3 TRP A 289 0.515 5.822 -15.281 1.00 85.36 C ANISOU 2184 CZ3 TRP A 289 9918 13942 8574 963 422 -525 C ATOM 2185 CH2 TRP A 289 -0.648 6.549 -15.569 1.00 76.82 C ANISOU 2185 CH2 TRP A 289 8797 13034 7357 1073 306 -262 C ATOM 2186 N GLY A 290 -1.121 4.500 -9.098 1.00 71.40 N ANISOU 2186 N GLY A 290 8325 10624 8182 614 178 -938 N ATOM 2187 CA GLY A 290 -2.227 4.910 -8.251 1.00 59.06 C ANISOU 2187 CA GLY A 290 6818 8871 6750 646 208 -830 C ATOM 2188 C GLY A 290 -2.086 4.414 -6.823 1.00 59.83 C ANISOU 2188 C GLY A 290 7076 8626 7032 561 228 -939 C ATOM 2189 O GLY A 290 -1.584 3.322 -6.561 1.00 69.26 O ANISOU 2189 O GLY A 290 8258 9775 8281 494 162 -1137 O ATOM 2190 N VAL A 291 -2.537 5.245 -5.884 1.00 63.06 N ANISOU 2190 N VAL A 291 7656 8778 7526 578 344 -794 N ATOM 2191 CA VAL A 291 -2.485 4.935 -4.459 1.00 60.09 C ANISOU 2191 CA VAL A 291 7501 8085 7246 508 383 -865 C ATOM 2192 C VAL A 291 -3.864 5.174 -3.855 1.00 66.35 C ANISOU 2192 C VAL A 291 8344 8722 8143 587 541 -778 C ATOM 2193 O VAL A 291 -4.493 6.211 -4.105 1.00 71.47 O ANISOU 2193 O VAL A 291 8979 9359 8817 684 670 -589 O ATOM 2194 CB VAL A 291 -1.416 5.771 -3.725 1.00 63.32 C ANISOU 2194 CB VAL A 291 8151 8285 7625 413 396 -814 C ATOM 2195 CG1 VAL A 291 -1.353 5.384 -2.256 1.00 48.27 C ANISOU 2195 CG1 VAL A 291 6509 6105 5728 338 392 -892 C ATOM 2196 CG2 VAL A 291 -0.053 5.592 -4.380 1.00 49.06 C ANISOU 2196 CG2 VAL A 291 6220 6632 5787 344 268 -858 C ATOM 2197 N ALA A 292 -4.331 4.214 -3.060 1.00 56.58 N ANISOU 2197 N ALA A 292 7152 7346 7001 561 567 -887 N ATOM 2198 CA ALA A 292 -5.622 4.287 -2.394 1.00 60.06 C ANISOU 2198 CA ALA A 292 7624 7610 7585 633 767 -806 C ATOM 2199 C ALA A 292 -5.408 4.245 -0.890 1.00 54.49 C ANISOU 2199 C ALA A 292 7292 6569 6843 587 903 -825 C ATOM 2200 O ALA A 292 -4.691 3.375 -0.387 1.00 63.70 O ANISOU 2200 O ALA A 292 8559 7689 7957 507 789 -937 O ATOM 2201 CB ALA A 292 -6.531 3.136 -2.829 1.00 67.85 C ANISOU 2201 CB ALA A 292 8313 8726 8739 636 719 -904 C ATOM 2202 N VAL A 293 -6.037 5.176 -0.180 1.00 55.36 N ANISOU 2202 N VAL A 293 7618 6448 6971 651 1157 -704 N ATOM 2203 CA VAL A 293 -5.953 5.278 1.269 1.00 58.37 C ANISOU 2203 CA VAL A 293 8423 6514 7243 612 1325 -727 C ATOM 2204 C VAL A 293 -7.313 4.926 1.851 1.00 63.75 C ANISOU 2204 C VAL A 293 9093 7025 8104 717 1630 -653 C ATOM 2205 O VAL A 293 -8.346 5.401 1.365 1.00 64.68 O ANISOU 2205 O VAL A 293 8982 7163 8433 839 1802 -522 O ATOM 2206 CB VAL A 293 -5.512 6.686 1.705 1.00 60.39 C ANISOU 2206 CB VAL A 293 9009 6579 7359 580 1436 -692 C ATOM 2207 CG1 VAL A 293 -5.604 6.834 3.214 1.00 63.84 C ANISOU 2207 CG1 VAL A 293 9935 6697 7626 539 1638 -745 C ATOM 2208 CG2 VAL A 293 -4.102 6.966 1.225 1.00 56.68 C ANISOU 2208 CG2 VAL A 293 8524 6250 6761 445 1143 -760 C ATOM 2209 N LEU A 294 -7.310 4.069 2.865 1.00 72.99 N ANISOU 2209 N LEU A 294 10480 8037 9217 681 1702 -703 N ATOM 2210 CA LEU A 294 -8.491 3.759 3.653 1.00 61.04 C ANISOU 2210 CA LEU A 294 9037 6299 7857 771 2064 -617 C ATOM 2211 C LEU A 294 -8.377 4.467 4.994 1.00 69.73 C ANISOU 2211 C LEU A 294 10706 7097 8692 775 2328 -604 C ATOM 2212 O LEU A 294 -7.296 4.512 5.590 1.00 68.49 O ANISOU 2212 O LEU A 294 10893 6919 8210 662 2137 -696 O ATOM 2213 CB LEU A 294 -8.636 2.250 3.870 1.00 67.91 C ANISOU 2213 CB LEU A 294 9779 7171 8852 734 2024 -658 C ATOM 2214 CG LEU A 294 -8.496 1.339 2.650 1.00 60.53 C ANISOU 2214 CG LEU A 294 8374 6508 8116 677 1730 -763 C ATOM 2215 CD1 LEU A 294 -8.729 -0.111 3.044 1.00 58.37 C ANISOU 2215 CD1 LEU A 294 8032 6125 8021 640 1786 -802 C ATOM 2216 CD2 LEU A 294 -9.449 1.758 1.542 1.00 67.12 C ANISOU 2216 CD2 LEU A 294 8777 7528 9197 733 1731 -718 C ATOM 2217 N VAL A 295 -9.488 5.029 5.466 1.00 77.63 N ANISOU 2217 N VAL A 295 11801 7867 9828 903 2765 -494 N ATOM 2218 CA VAL A 295 -9.474 5.745 6.735 1.00 66.61 C ANISOU 2218 CA VAL A 295 10998 6158 8152 911 3083 -517 C ATOM 2219 C VAL A 295 -10.834 5.621 7.410 1.00 72.54 C ANISOU 2219 C VAL A 295 11796 6651 9116 1070 3628 -380 C ATOM 2220 O VAL A 295 -10.938 5.693 8.640 1.00 66.43 O ANISOU 2220 O VAL A 295 11539 5619 8081 1083 3943 -397 O ATOM 2221 CB VAL A 295 -9.068 7.219 6.537 1.00 69.76 C ANISOU 2221 CB VAL A 295 11588 6472 8444 892 3106 -563 C ATOM 2222 CG1 VAL A 295 -10.151 7.998 5.805 1.00 71.89 C ANISOU 2222 CG1 VAL A 295 11520 6689 9106 1078 3399 -388 C ATOM 2223 CG2 VAL A 295 -8.742 7.858 7.867 1.00 78.74 C ANISOU 2223 CG2 VAL A 295 13416 7309 9194 822 3328 -687 C ATOM 2224 N GLY A 296 -11.882 5.423 6.615 1.00 75.90 N ANISOU 2224 N GLY A 296 11677 7154 10008 1187 3744 -237 N ATOM 2225 CA GLY A 296 -13.192 5.153 7.184 1.00 77.64 C ANISOU 2225 CA GLY A 296 11823 7144 10532 1329 4254 -81 C ATOM 2226 C GLY A 296 -13.202 3.795 7.860 1.00 84.33 C ANISOU 2226 C GLY A 296 12756 7946 11340 1265 4287 -88 C ATOM 2227 O GLY A 296 -12.786 2.790 7.272 1.00 89.55 O ANISOU 2227 O GLY A 296 13118 8828 12079 1156 3906 -152 O ATOM 2228 N VAL A 297 -13.668 3.759 9.103 1.00 86.57 N ANISOU 2228 N VAL A 297 13473 7920 11499 1341 4779 -17 N ATOM 2229 CA VAL A 297 -13.680 2.530 9.893 1.00 97.40 C ANISOU 2229 CA VAL A 297 15009 9200 12797 1306 4886 32 C ATOM 2230 C VAL A 297 -14.963 1.763 9.598 1.00 98.55 C ANISOU 2230 C VAL A 297 14609 9273 13561 1376 5184 197 C ATOM 2231 O VAL A 297 -16.050 2.358 9.587 1.00103.13 O ANISOU 2231 O VAL A 297 14995 9702 14487 1516 5610 332 O ATOM 2232 CB VAL A 297 -13.540 2.838 11.393 1.00 91.13 C ANISOU 2232 CB VAL A 297 14990 8129 11506 1352 5279 45 C ATOM 2233 CG1 VAL A 297 -13.888 1.617 12.233 1.00112.55 C ANISOU 2233 CG1 VAL A 297 17836 10698 14229 1380 5551 196 C ATOM 2234 CG2 VAL A 297 -12.131 3.318 11.702 1.00 96.55 C ANISOU 2234 CG2 VAL A 297 16171 8934 11578 1215 4851 -145 C ATOM 2235 N PRO A 298 -14.893 0.459 9.348 1.00 95.47 N ANISOU 2235 N PRO A 298 13934 8966 13374 1278 4990 196 N ATOM 2236 CA PRO A 298 -16.110 -0.308 9.076 1.00 94.28 C ANISOU 2236 CA PRO A 298 13241 8725 13857 1293 5259 324 C ATOM 2237 C PRO A 298 -16.890 -0.605 10.348 1.00 97.13 C ANISOU 2237 C PRO A 298 13910 8714 14282 1406 5938 529 C ATOM 2238 O PRO A 298 -16.383 -0.498 11.465 1.00 98.35 O ANISOU 2238 O PRO A 298 14739 8710 13920 1454 6142 559 O ATOM 2239 CB PRO A 298 -15.574 -1.598 8.446 1.00 86.67 C ANISOU 2239 CB PRO A 298 11978 7928 13027 1123 4823 202 C ATOM 2240 CG PRO A 298 -14.237 -1.774 9.082 1.00 74.76 C ANISOU 2240 CG PRO A 298 11041 6438 10925 1089 4592 135 C ATOM 2241 CD PRO A 298 -13.684 -0.381 9.275 1.00 97.12 C ANISOU 2241 CD PRO A 298 14273 9334 13295 1143 4520 75 C ATOM 2242 N SER A 299 -18.155 -0.970 10.153 1.00 85.37 N ANISOU 2242 N SER A 299 11903 7098 13437 1443 6288 679 N ATOM 2243 CA SER A 299 -19.014 -1.446 11.229 1.00104.84 C ANISOU 2243 CA SER A 299 14529 9200 16106 1538 6980 905 C ATOM 2244 C SER A 299 -19.323 -2.929 11.100 1.00123.27 C ANISOU 2244 C SER A 299 16483 11461 18894 1402 6976 955 C ATOM 2245 O SER A 299 -19.184 -3.678 12.072 1.00121.88 O ANISOU 2245 O SER A 299 16702 11050 18556 1421 7290 1083 O ATOM 2246 CB SER A 299 -20.320 -0.638 11.268 1.00102.12 C ANISOU 2246 CB SER A 299 13884 8684 16232 1709 7526 1088 C ATOM 2247 OG SER A 299 -20.752 -0.296 9.963 1.00107.13 O ANISOU 2247 OG SER A 299 13790 9583 17330 1669 7153 1046 O ATOM 2248 N LYS A 300 -19.736 -3.375 9.917 1.00123.73 N ANISOU 2248 N LYS A 300 15797 11706 19508 1256 6627 854 N ATOM 2249 CA LYS A 300 -19.892 -4.800 9.672 1.00119.27 C ANISOU 2249 CA LYS A 300 14878 11065 19373 1075 6549 819 C ATOM 2250 C LYS A 300 -18.524 -5.450 9.490 1.00104.63 C ANISOU 2250 C LYS A 300 13321 9355 17079 965 6042 627 C ATOM 2251 O LYS A 300 -17.559 -4.811 9.063 1.00118.88 O ANISOU 2251 O LYS A 300 15331 11433 18406 969 5582 463 O ATOM 2252 CB LYS A 300 -20.766 -5.041 8.441 1.00124.33 C ANISOU 2252 CB LYS A 300 14646 11880 20714 920 6297 721 C ATOM 2253 CG LYS A 300 -22.244 -5.205 8.759 1.00138.65 C ANISOU 2253 CG LYS A 300 15998 13430 23252 950 6874 960 C ATOM 2254 CD LYS A 300 -23.024 -5.697 7.551 1.00143.68 C ANISOU 2254 CD LYS A 300 15743 14257 24590 727 6524 831 C ATOM 2255 CE LYS A 300 -23.104 -7.214 7.523 1.00139.47 C ANISOU 2255 CE LYS A 300 14990 13525 24478 476 6531 724 C ATOM 2256 NZ LYS A 300 -23.588 -7.721 6.208 1.00140.25 N1+ ANISOU 2256 NZ LYS A 300 14307 13873 25107 192 6022 472 N1+ ATOM 2257 N ASP A 301 -18.449 -6.737 9.819 1.00124.60 N ANISOU 2257 N ASP A 301 15850 11670 19822 875 6162 672 N ATOM 2258 CA ASP A 301 -17.181 -7.460 9.900 1.00116.49 C ANISOU 2258 CA ASP A 301 15155 10688 18420 826 5815 579 C ATOM 2259 C ASP A 301 -16.851 -8.211 8.615 1.00115.05 C ANISOU 2259 C ASP A 301 14465 10691 18557 614 5297 281 C ATOM 2260 O ASP A 301 -16.370 -9.346 8.660 1.00110.84 O ANISOU 2260 O ASP A 301 13958 10010 18144 537 5244 248 O ATOM 2261 CB ASP A 301 -17.204 -8.418 11.088 1.00122.74 C ANISOU 2261 CB ASP A 301 16316 11104 19214 895 6289 850 C ATOM 2262 CG ASP A 301 -15.841 -8.590 11.723 1.00119.87 C ANISOU 2262 CG ASP A 301 16574 10795 18178 981 6052 906 C ATOM 2263 OD1 ASP A 301 -14.869 -7.995 11.214 1.00120.35 O ANISOU 2263 OD1 ASP A 301 16735 11169 17824 964 5523 709 O ATOM 2264 OD2 ASP A 301 -15.742 -9.319 12.732 1.00103.18 O1- ANISOU 2264 OD2 ASP A 301 14828 8414 15962 1070 6395 1174 O1- ATOM 2265 N ASP A 302 -17.089 -7.604 7.456 1.00113.84 N ANISOU 2265 N ASP A 302 13870 10852 18530 528 4928 67 N ATOM 2266 CA ASP A 302 -16.741 -8.244 6.198 1.00 95.00 C ANISOU 2266 CA ASP A 302 11070 8680 16347 324 4430 -253 C ATOM 2267 C ASP A 302 -15.254 -8.059 5.899 1.00102.78 C ANISOU 2267 C ASP A 302 12396 9898 16758 356 3979 -403 C ATOM 2268 O ASP A 302 -14.541 -7.320 6.581 1.00106.30 O ANISOU 2268 O ASP A 302 13337 10383 16669 511 3984 -274 O ATOM 2269 CB ASP A 302 -17.595 -7.691 5.059 1.00100.57 C ANISOU 2269 CB ASP A 302 11176 9670 17366 224 4190 -396 C ATOM 2270 CG ASP A 302 -19.041 -8.132 5.153 1.00117.27 C ANISOU 2270 CG ASP A 302 12790 11572 20196 129 4549 -290 C ATOM 2271 OD1 ASP A 302 -19.377 -8.867 6.105 1.00106.71 O ANISOU 2271 OD1 ASP A 302 11591 9835 19117 142 5034 -108 O ATOM 2272 OD2 ASP A 302 -19.841 -7.749 4.273 1.00113.93 O1- ANISOU 2272 OD2 ASP A 302 11816 11384 20088 43 4345 -366 O1- ATOM 2273 N ALA A 303 -14.787 -8.745 4.860 1.00 99.79 N ANISOU 2273 N ALA A 303 11740 9667 16509 195 3595 -695 N ATOM 2274 CA ALA A 303 -13.379 -8.759 4.495 1.00 97.53 C ANISOU 2274 CA ALA A 303 11695 9569 15794 216 3209 -839 C ATOM 2275 C ALA A 303 -13.145 -7.993 3.199 1.00 91.41 C ANISOU 2275 C ALA A 303 10665 9224 14843 155 2760 -1078 C ATOM 2276 O ALA A 303 -14.038 -7.871 2.355 1.00 94.99 O ANISOU 2276 O ALA A 303 10671 9835 15585 42 2662 -1206 O ATOM 2277 CB ALA A 303 -12.866 -10.195 4.342 1.00 89.99 C ANISOU 2277 CB ALA A 303 10691 8407 15096 116 3187 -974 C ATOM 2278 N PHE A 304 -11.926 -7.479 3.054 1.00 84.30 N ANISOU 2278 N PHE A 304 10043 8521 13467 232 2483 -1114 N ATOM 2279 CA PHE A 304 -11.512 -6.791 1.838 1.00 71.26 C ANISOU 2279 CA PHE A 304 8210 7265 11601 192 2086 -1311 C ATOM 2280 C PHE A 304 -11.130 -7.824 0.784 1.00 82.74 C ANISOU 2280 C PHE A 304 9405 8805 13227 35 1847 -1636 C ATOM 2281 O PHE A 304 -10.265 -8.673 1.025 1.00 75.51 O ANISOU 2281 O PHE A 304 8656 7724 12310 40 1857 -1685 O ATOM 2282 CB PHE A 304 -10.348 -5.847 2.141 1.00 70.32 C ANISOU 2282 CB PHE A 304 8477 7280 10962 317 1932 -1214 C ATOM 2283 CG PHE A 304 -9.796 -5.144 0.932 1.00 68.48 C ANISOU 2283 CG PHE A 304 8094 7425 10502 291 1573 -1374 C ATOM 2284 CD1 PHE A 304 -10.271 -3.895 0.567 1.00 80.11 C ANISOU 2284 CD1 PHE A 304 9490 9097 11852 347 1532 -1287 C ATOM 2285 CD2 PHE A 304 -8.783 -5.716 0.177 1.00 73.08 C ANISOU 2285 CD2 PHE A 304 8626 8141 11001 232 1322 -1581 C ATOM 2286 CE1 PHE A 304 -9.763 -3.240 -0.541 1.00 83.95 C ANISOU 2286 CE1 PHE A 304 9856 9923 12118 339 1234 -1385 C ATOM 2287 CE2 PHE A 304 -8.272 -5.067 -0.930 1.00 75.11 C ANISOU 2287 CE2 PHE A 304 8769 8742 11028 219 1046 -1704 C ATOM 2288 CZ PHE A 304 -8.763 -3.828 -1.290 1.00 76.53 C ANISOU 2288 CZ PHE A 304 8882 9132 11066 270 995 -1596 C ATOM 2289 N LYS A 305 -11.771 -7.752 -0.383 1.00 83.64 N ANISOU 2289 N LYS A 305 9121 9177 13481 -98 1637 -1853 N ATOM 2290 CA LYS A 305 -11.580 -8.720 -1.456 1.00 76.66 C ANISOU 2290 CA LYS A 305 7999 8380 12748 -282 1429 -2226 C ATOM 2291 C LYS A 305 -11.197 -7.998 -2.738 1.00 80.05 C ANISOU 2291 C LYS A 305 8316 9278 12823 -300 1052 -2399 C ATOM 2292 O LYS A 305 -11.869 -7.040 -3.134 1.00 75.06 O ANISOU 2292 O LYS A 305 7506 8913 12100 -270 933 -2294 O ATOM 2293 CB LYS A 305 -12.855 -9.535 -1.699 1.00 83.92 C ANISOU 2293 CB LYS A 305 8519 9165 14200 -492 1518 -2379 C ATOM 2294 CG LYS A 305 -13.170 -10.606 -0.672 1.00 95.05 C ANISOU 2294 CG LYS A 305 9995 10069 16050 -527 1912 -2282 C ATOM 2295 CD LYS A 305 -14.254 -11.520 -1.225 1.00 91.46 C ANISOU 2295 CD LYS A 305 9089 9506 16155 -806 1925 -2546 C ATOM 2296 CE LYS A 305 -15.056 -12.193 -0.129 1.00 98.05 C ANISOU 2296 CE LYS A 305 9882 9862 17512 -830 2391 -2326 C ATOM 2297 NZ LYS A 305 -15.471 -13.566 -0.528 1.00 95.60 N1+ ANISOU 2297 NZ LYS A 305 9294 9267 17761 -1115 2460 -2648 N1+ ATOM 2298 N THR A 306 -10.139 -8.468 -3.397 1.00 86.90 N ANISOU 2298 N THR A 306 9278 10232 13507 -330 898 -2638 N ATOM 2299 CA THR A 306 -9.780 -7.927 -4.701 1.00 76.05 C ANISOU 2299 CA THR A 306 7808 9298 11791 -358 582 -2823 C ATOM 2300 C THR A 306 -8.909 -8.925 -5.450 1.00 79.96 C ANISOU 2300 C THR A 306 8342 9780 12259 -451 519 -3184 C ATOM 2301 O THR A 306 -8.236 -9.771 -4.853 1.00 85.82 O ANISOU 2301 O THR A 306 9249 10183 13176 -417 711 -3199 O ATOM 2302 CB THR A 306 -9.060 -6.577 -4.584 1.00 83.56 C ANISOU 2302 CB THR A 306 8974 10455 12321 -165 511 -2554 C ATOM 2303 CG2 THR A 306 -7.682 -6.756 -3.971 1.00 80.12 C ANISOU 2303 CG2 THR A 306 8857 9838 11748 -57 597 -2480 C ATOM 2304 OG1 THR A 306 -8.920 -5.999 -5.888 1.00 78.42 O ANISOU 2304 OG1 THR A 306 8197 10239 11361 -186 239 -2680 O ATOM 2305 N HIS A 307 -8.954 -8.814 -6.774 1.00 93.55 N ANISOU 2305 N HIS A 307 9917 11874 13754 -554 264 -3461 N ATOM 2306 CA HIS A 307 -8.064 -9.570 -7.643 1.00 90.52 C ANISOU 2306 CA HIS A 307 9611 11532 13249 -620 226 -3824 C ATOM 2307 C HIS A 307 -6.615 -9.247 -7.288 1.00 93.34 C ANISOU 2307 C HIS A 307 10242 11829 13394 -411 327 -3637 C ATOM 2308 O HIS A 307 -6.249 -8.065 -7.235 1.00 88.94 O ANISOU 2308 O HIS A 307 9770 11498 12527 -271 240 -3366 O ATOM 2309 CB HIS A 307 -8.359 -9.203 -9.101 1.00 90.35 C ANISOU 2309 CB HIS A 307 9447 12007 12873 -730 -80 -4081 C ATOM 2310 CG HIS A 307 -7.878 -10.205 -10.106 1.00110.39 C ANISOU 2310 CG HIS A 307 12030 14572 15342 -880 -98 -4579 C ATOM 2311 CD2 HIS A 307 -7.923 -10.193 -11.460 1.00115.14 C ANISOU 2311 CD2 HIS A 307 12598 15576 15576 -1000 -326 -4913 C ATOM 2312 ND1 HIS A 307 -7.270 -11.390 -9.756 1.00109.91 N ANISOU 2312 ND1 HIS A 307 12087 14075 15597 -910 167 -4786 N ATOM 2313 CE1 HIS A 307 -6.956 -12.063 -10.849 1.00105.07 C ANISOU 2313 CE1 HIS A 307 11516 13562 14843 -1045 134 -5255 C ATOM 2314 NE2 HIS A 307 -7.344 -11.359 -11.897 1.00121.65 N ANISOU 2314 NE2 HIS A 307 13543 16183 16494 -1112 -172 -5355 N ATOM 2315 N PRO A 308 -5.773 -10.248 -7.008 1.00 97.15 N ANISOU 2315 N PRO A 308 10842 11991 14078 -383 517 -3751 N ATOM 2316 CA PRO A 308 -4.362 -9.936 -6.710 1.00 85.91 C ANISOU 2316 CA PRO A 308 9609 10542 12491 -188 575 -3553 C ATOM 2317 C PRO A 308 -3.686 -9.135 -7.807 1.00 88.24 C ANISOU 2317 C PRO A 308 9918 11250 12361 -143 426 -3622 C ATOM 2318 O PRO A 308 -2.872 -8.248 -7.515 1.00 75.09 O ANISOU 2318 O PRO A 308 8352 9683 10496 0 396 -3341 O ATOM 2319 CB PRO A 308 -3.713 -11.318 -6.529 1.00 83.19 C ANISOU 2319 CB PRO A 308 9309 9807 12492 -178 801 -3725 C ATOM 2320 CG PRO A 308 -4.818 -12.295 -6.414 1.00 84.63 C ANISOU 2320 CG PRO A 308 9375 9724 13058 -362 906 -3943 C ATOM 2321 CD PRO A 308 -6.093 -11.679 -6.875 1.00 94.64 C ANISOU 2321 CD PRO A 308 10466 11288 14206 -522 701 -4022 C ATOM 2322 N MET A 309 -4.021 -9.405 -9.071 1.00 78.51 N ANISOU 2322 N MET A 309 8595 10267 10968 -277 331 -3989 N ATOM 2323 CA MET A 309 -3.419 -8.653 -10.164 1.00 81.23 C ANISOU 2323 CA MET A 309 8979 11021 10865 -223 224 -4032 C ATOM 2324 C MET A 309 -3.742 -7.166 -10.091 1.00 77.93 C ANISOU 2324 C MET A 309 8543 10904 10163 -139 54 -3671 C ATOM 2325 O MET A 309 -3.001 -6.357 -10.658 1.00 77.72 O ANISOU 2325 O MET A 309 8583 11130 9816 -39 29 -3552 O ATOM 2326 CB MET A 309 -3.857 -9.236 -11.506 1.00 87.98 C ANISOU 2326 CB MET A 309 9781 12114 11533 -399 134 -4505 C ATOM 2327 CG MET A 309 -3.376 -10.660 -11.733 1.00 96.53 C ANISOU 2327 CG MET A 309 10927 12875 12875 -476 361 -4914 C ATOM 2328 SD MET A 309 -1.580 -10.767 -11.886 1.00 90.48 S ANISOU 2328 SD MET A 309 10317 12001 12062 -251 640 -4851 S ATOM 2329 CE MET A 309 -1.262 -9.489 -13.099 1.00 78.15 C ANISOU 2329 CE MET A 309 8808 11037 9847 -191 486 -4783 C ATOM 2330 N ASN A 310 -4.815 -6.779 -9.396 1.00 72.14 N ANISOU 2330 N ASN A 310 7720 10115 9574 -167 -15 -3477 N ATOM 2331 CA ASN A 310 -5.029 -5.359 -9.137 1.00 73.11 C ANISOU 2331 CA ASN A 310 7858 10417 9504 -52 -98 -3100 C ATOM 2332 C ASN A 310 -3.854 -4.759 -8.377 1.00 79.30 C ANISOU 2332 C ASN A 310 8834 11048 10249 93 15 -2826 C ATOM 2333 O ASN A 310 -3.517 -3.587 -8.580 1.00 74.02 O ANISOU 2333 O ASN A 310 8216 10568 9339 180 -32 -2598 O ATOM 2334 CB ASN A 310 -6.332 -5.145 -8.365 1.00 71.85 C ANISOU 2334 CB ASN A 310 7578 10136 9584 -82 -104 -2933 C ATOM 2335 CG ASN A 310 -7.556 -5.509 -9.180 1.00 74.80 C ANISOU 2335 CG ASN A 310 7684 10732 10003 -237 -283 -3151 C ATOM 2336 ND2 ASN A 310 -8.670 -5.758 -8.500 1.00 74.32 N ANISOU 2336 ND2 ASN A 310 7459 10482 10295 -303 -235 -3086 N ATOM 2337 OD1 ASN A 310 -7.502 -5.565 -10.408 1.00 69.79 O ANISOU 2337 OD1 ASN A 310 6986 10445 9084 -304 -466 -3373 O ATOM 2338 N PHE A 311 -3.215 -5.548 -7.511 1.00 70.79 N ANISOU 2338 N PHE A 311 7852 9626 9419 112 153 -2832 N ATOM 2339 CA PHE A 311 -1.979 -5.116 -6.870 1.00 70.31 C ANISOU 2339 CA PHE A 311 7935 9455 9324 223 199 -2608 C ATOM 2340 C PHE A 311 -0.783 -5.314 -7.793 1.00 75.98 C ANISOU 2340 C PHE A 311 8627 10313 9929 261 231 -2741 C ATOM 2341 O PHE A 311 0.016 -4.392 -7.990 1.00 69.91 O ANISOU 2341 O PHE A 311 7890 9691 8981 324 205 -2567 O ATOM 2342 CB PHE A 311 -1.761 -5.879 -5.562 1.00 73.97 C ANISOU 2342 CB PHE A 311 8498 9531 10076 252 304 -2506 C ATOM 2343 CG PHE A 311 -2.592 -5.376 -4.422 1.00 75.08 C ANISOU 2343 CG PHE A 311 8750 9520 10256 260 327 -2273 C ATOM 2344 CD1 PHE A 311 -2.253 -4.205 -3.764 1.00 71.75 C ANISOU 2344 CD1 PHE A 311 8490 9122 9649 316 279 -2009 C ATOM 2345 CD2 PHE A 311 -3.707 -6.079 -3.999 1.00 65.81 C ANISOU 2345 CD2 PHE A 311 7528 8155 9323 200 432 -2330 C ATOM 2346 CE1 PHE A 311 -3.013 -3.741 -2.709 1.00 73.23 C ANISOU 2346 CE1 PHE A 311 8829 9148 9845 330 354 -1823 C ATOM 2347 CE2 PHE A 311 -4.473 -5.621 -2.945 1.00 81.00 C ANISOU 2347 CE2 PHE A 311 9567 9925 11285 226 522 -2105 C ATOM 2348 CZ PHE A 311 -4.127 -4.449 -2.300 1.00 80.37 C ANISOU 2348 CZ PHE A 311 9688 9874 10974 299 492 -1860 C ATOM 2349 N LEU A 312 -0.649 -6.513 -8.370 1.00 72.44 N ANISOU 2349 N LEU A 312 8122 9791 9610 218 326 -3058 N ATOM 2350 CA LEU A 312 0.532 -6.816 -9.178 1.00 70.46 C ANISOU 2350 CA LEU A 312 7859 9614 9299 279 439 -3192 C ATOM 2351 C LEU A 312 0.645 -5.928 -10.409 1.00 79.66 C ANISOU 2351 C LEU A 312 9018 11193 10057 282 386 -3222 C ATOM 2352 O LEU A 312 1.728 -5.843 -10.998 1.00 72.97 O ANISOU 2352 O LEU A 312 8171 10429 9124 359 511 -3230 O ATOM 2353 CB LEU A 312 0.548 -8.283 -9.612 1.00 75.77 C ANISOU 2353 CB LEU A 312 8507 10092 10193 228 604 -3572 C ATOM 2354 CG LEU A 312 0.948 -9.321 -8.561 1.00 75.92 C ANISOU 2354 CG LEU A 312 8529 9659 10659 291 752 -3506 C ATOM 2355 CD1 LEU A 312 2.216 -8.909 -7.825 1.00 74.05 C ANISOU 2355 CD1 LEU A 312 8291 9339 10506 453 760 -3148 C ATOM 2356 CD2 LEU A 312 -0.177 -9.555 -7.589 1.00 94.60 C ANISOU 2356 CD2 LEU A 312 10911 11818 13214 214 698 -3418 C ATOM 2357 N ASN A 313 -0.440 -5.273 -10.818 1.00 82.01 N ANISOU 2357 N ASN A 313 9294 11748 10116 219 222 -3207 N ATOM 2358 CA ASN A 313 -0.359 -4.234 -11.834 1.00 77.52 C ANISOU 2358 CA ASN A 313 8735 11575 9144 259 159 -3108 C ATOM 2359 C ASN A 313 0.062 -2.886 -11.258 1.00 76.13 C ANISOU 2359 C ASN A 313 8594 11400 8932 351 143 -2688 C ATOM 2360 O ASN A 313 -0.238 -1.841 -11.849 1.00 75.77 O ANISOU 2360 O ASN A 313 8549 11628 8612 389 77 -2511 O ATOM 2361 CB ASN A 313 -1.688 -4.114 -12.583 1.00 73.10 C ANISOU 2361 CB ASN A 313 8107 11318 8349 168 -38 -3236 C ATOM 2362 CG ASN A 313 -1.924 -5.273 -13.538 1.00 95.16 C ANISOU 2362 CG ASN A 313 10898 14215 11045 43 -42 -3715 C ATOM 2363 ND2 ASN A 313 -1.924 -4.977 -14.831 1.00108.61 N ANISOU 2363 ND2 ASN A 313 12646 16330 12289 38 -109 -3832 N ATOM 2364 OD1 ASN A 313 -2.097 -6.416 -13.123 1.00 98.13 O ANISOU 2364 OD1 ASN A 313 11253 14293 11739 -53 29 -3978 O ATOM 2365 N GLU A 314 0.742 -2.917 -10.110 1.00 70.83 N ANISOU 2365 N GLU A 314 7959 10418 8536 381 196 -2528 N ATOM 2366 CA GLU A 314 1.358 -1.761 -9.470 1.00 72.82 C ANISOU 2366 CA GLU A 314 8263 10612 8792 426 183 -2195 C ATOM 2367 C GLU A 314 0.324 -0.762 -8.968 1.00 63.68 C ANISOU 2367 C GLU A 314 7165 9463 7568 418 92 -1988 C ATOM 2368 O GLU A 314 0.224 0.361 -9.472 1.00 65.29 O ANISOU 2368 O GLU A 314 7377 9850 7580 456 87 -1803 O ATOM 2369 CB GLU A 314 2.359 -1.102 -10.420 1.00 64.54 C ANISOU 2369 CB GLU A 314 7182 9777 7564 477 279 -2110 C ATOM 2370 CG GLU A 314 3.618 -1.934 -10.585 1.00 66.74 C ANISOU 2370 CG GLU A 314 7388 9955 8017 513 426 -2226 C ATOM 2371 CD GLU A 314 4.612 -1.335 -11.551 1.00 76.77 C ANISOU 2371 CD GLU A 314 8605 11421 9144 569 585 -2135 C ATOM 2372 OE1 GLU A 314 4.300 -0.296 -12.170 1.00 76.93 O ANISOU 2372 OE1 GLU A 314 8667 11670 8892 580 580 -1982 O ATOM 2373 OE2 GLU A 314 5.710 -1.912 -11.686 1.00 75.28 O1- ANISOU 2373 OE2 GLU A 314 8320 11141 9143 617 746 -2188 O1- ATOM 2374 N ARG A 315 -0.447 -1.180 -7.969 1.00 70.50 N ANISOU 2374 N ARG A 315 8072 10102 8615 385 63 -1997 N ATOM 2375 CA ARG A 315 -1.279 -0.305 -7.162 1.00 55.47 C ANISOU 2375 CA ARG A 315 6255 8094 6726 395 51 -1786 C ATOM 2376 C ARG A 315 -0.837 -0.420 -5.710 1.00 67.38 C ANISOU 2376 C ARG A 315 7932 9274 8394 380 76 -1687 C ATOM 2377 O ARG A 315 -0.261 -1.428 -5.294 1.00 69.58 O ANISOU 2377 O ARG A 315 8214 9404 8820 369 79 -1783 O ATOM 2378 CB ARG A 315 -2.767 -0.660 -7.288 1.00 57.91 C ANISOU 2378 CB ARG A 315 6460 8450 7095 375 25 -1865 C ATOM 2379 CG ARG A 315 -3.412 -0.221 -8.589 1.00 63.99 C ANISOU 2379 CG ARG A 315 7073 9590 7651 395 -69 -1877 C ATOM 2380 CD ARG A 315 -4.887 -0.592 -8.615 1.00 62.30 C ANISOU 2380 CD ARG A 315 6691 9418 7561 354 -137 -1939 C ATOM 2381 NE ARG A 315 -5.524 -0.209 -9.869 1.00 64.13 N ANISOU 2381 NE ARG A 315 6749 10055 7563 371 -297 -1933 N ATOM 2382 CZ ARG A 315 -5.605 -0.990 -10.938 1.00 70.21 C ANISOU 2382 CZ ARG A 315 7413 11091 8174 283 -435 -2223 C ATOM 2383 NH1 ARG A 315 -5.105 -2.215 -10.939 1.00 80.47 N1+ ANISOU 2383 NH1 ARG A 315 8752 12251 9570 176 -388 -2559 N1+ ATOM 2384 NH2 ARG A 315 -6.205 -0.530 -12.033 1.00 61.94 N ANISOU 2384 NH2 ARG A 315 6230 10454 6852 306 -621 -2172 N ATOM 2385 N THR A 316 -1.106 0.627 -4.936 1.00 57.05 N ANISOU 2385 N THR A 316 6782 7849 7045 387 101 -1487 N ATOM 2386 CA THR A 316 -0.753 0.663 -3.524 1.00 54.71 C ANISOU 2386 CA THR A 316 6709 7275 6803 359 104 -1397 C ATOM 2387 C THR A 316 -2.004 0.913 -2.694 1.00 61.87 C ANISOU 2387 C THR A 316 7755 8010 7741 381 225 -1321 C ATOM 2388 O THR A 316 -2.853 1.728 -3.068 1.00 57.42 O ANISOU 2388 O THR A 316 7151 7518 7146 423 301 -1238 O ATOM 2389 CB THR A 316 0.296 1.748 -3.237 1.00 52.28 C ANISOU 2389 CB THR A 316 6523 6942 6401 313 45 -1265 C ATOM 2390 CG2 THR A 316 0.667 1.767 -1.759 1.00 49.58 C ANISOU 2390 CG2 THR A 316 6439 6351 6047 257 -11 -1201 C ATOM 2391 OG1 THR A 316 1.474 1.490 -4.011 1.00 63.37 O ANISOU 2391 OG1 THR A 316 7753 8494 7832 302 -25 -1310 O ATOM 2392 N LEU A 317 -2.121 0.198 -1.577 1.00 60.62 N ANISOU 2392 N LEU A 317 7751 7621 7659 372 270 -1318 N ATOM 2393 CA LEU A 317 -3.224 0.380 -0.639 1.00 63.03 C ANISOU 2393 CA LEU A 317 8230 7723 7997 401 450 -1230 C ATOM 2394 C LEU A 317 -2.640 0.652 0.740 1.00 57.55 C ANISOU 2394 C LEU A 317 7899 6813 7154 375 450 -1134 C ATOM 2395 O LEU A 317 -1.999 -0.222 1.332 1.00 67.99 O ANISOU 2395 O LEU A 317 9294 8054 8485 363 365 -1134 O ATOM 2396 CB LEU A 317 -4.145 -0.839 -0.612 1.00 69.33 C ANISOU 2396 CB LEU A 317 8879 8442 9021 412 555 -1312 C ATOM 2397 CG LEU A 317 -5.384 -0.693 0.273 1.00 66.65 C ANISOU 2397 CG LEU A 317 8660 7889 8774 453 804 -1200 C ATOM 2398 CD1 LEU A 317 -6.221 0.488 -0.182 1.00 59.15 C ANISOU 2398 CD1 LEU A 317 7625 7034 7816 505 891 -1109 C ATOM 2399 CD2 LEU A 317 -6.210 -1.964 0.254 1.00 69.45 C ANISOU 2399 CD2 LEU A 317 8821 8146 9420 433 913 -1282 C ATOM 2400 N LYS A 318 -2.853 1.864 1.240 1.00 58.06 N ANISOU 2400 N LYS A 318 8201 6784 7076 367 543 -1051 N ATOM 2401 CA LYS A 318 -2.432 2.258 2.574 1.00 61.50 C ANISOU 2401 CA LYS A 318 9044 7020 7301 314 546 -1001 C ATOM 2402 C LYS A 318 -3.656 2.400 3.464 1.00 65.24 C ANISOU 2402 C LYS A 318 9762 7266 7759 383 863 -936 C ATOM 2403 O LYS A 318 -4.723 2.817 3.005 1.00 66.53 O ANISOU 2403 O LYS A 318 9785 7419 8074 460 1078 -900 O ATOM 2404 CB LYS A 318 -1.656 3.578 2.542 1.00 49.84 C ANISOU 2404 CB LYS A 318 7710 5555 5673 219 447 -1002 C ATOM 2405 CG LYS A 318 -0.460 3.583 1.605 1.00 59.32 C ANISOU 2405 CG LYS A 318 8640 6969 6930 155 196 -1035 C ATOM 2406 CD LYS A 318 0.121 4.981 1.456 1.00 49.70 C ANISOU 2406 CD LYS A 318 7518 5727 5640 53 167 -1020 C ATOM 2407 CE LYS A 318 1.364 4.971 0.580 1.00 56.06 C ANISOU 2407 CE LYS A 318 8041 6726 6532 -14 -40 -1024 C ATOM 2408 NZ LYS A 318 1.928 6.337 0.394 1.00 70.31 N1+ ANISOU 2408 NZ LYS A 318 9911 8475 8328 -132 -36 -994 N1+ ATOM 2409 N GLY A 319 -3.503 2.035 4.731 1.00 65.42 N ANISOU 2409 N GLY A 319 10138 7118 7600 368 901 -897 N ATOM 2410 CA GLY A 319 -4.508 2.290 5.744 1.00 63.94 C ANISOU 2410 CA GLY A 319 10281 6687 7325 429 1249 -831 C ATOM 2411 C GLY A 319 -3.954 3.286 6.742 1.00 61.95 C ANISOU 2411 C GLY A 319 10529 6308 6700 339 1229 -865 C ATOM 2412 O GLY A 319 -2.754 3.298 7.021 1.00 72.94 O ANISOU 2412 O GLY A 319 12039 7790 7886 220 894 -907 O ATOM 2413 N THR A 320 -4.828 4.136 7.272 1.00 67.41 N ANISOU 2413 N THR A 320 11583 5955 8075 527 1002 351 N ATOM 2414 CA THR A 320 -4.394 5.164 8.203 1.00 77.29 C ANISOU 2414 CA THR A 320 12707 7346 9314 559 1124 425 C ATOM 2415 C THR A 320 -5.427 5.345 9.303 1.00 69.69 C ANISOU 2415 C THR A 320 11524 6400 8553 418 1212 380 C ATOM 2416 O THR A 320 -6.623 5.111 9.109 1.00 63.59 O ANISOU 2416 O THR A 320 10637 5569 7956 309 1128 281 O ATOM 2417 CB THR A 320 -4.143 6.504 7.497 1.00 69.20 C ANISOU 2417 CB THR A 320 11638 6410 8243 663 1008 428 C ATOM 2418 CG2 THR A 320 -5.409 7.007 6.836 1.00 61.48 C ANISOU 2418 CG2 THR A 320 10522 5401 7437 622 829 315 C ATOM 2419 OG1 THR A 320 -3.689 7.471 8.452 1.00 78.64 O ANISOU 2419 OG1 THR A 320 12731 7723 9424 676 1134 489 O ATOM 2420 N PHE A 321 -4.938 5.758 10.468 1.00 65.35 N ANISOU 2420 N PHE A 321 10912 5949 7967 421 1383 453 N ATOM 2421 CA PHE A 321 -5.761 6.076 11.624 1.00 64.48 C ANISOU 2421 CA PHE A 321 10598 5888 8015 311 1497 422 C ATOM 2422 C PHE A 321 -5.460 7.506 12.045 1.00 75.17 C ANISOU 2422 C PHE A 321 11844 7367 9350 377 1527 433 C ATOM 2423 O PHE A 321 -4.292 7.862 12.237 1.00 74.57 O ANISOU 2423 O PHE A 321 11864 7369 9102 457 1588 518 O ATOM 2424 CB PHE A 321 -5.486 5.108 12.778 1.00 65.79 C ANISOU 2424 CB PHE A 321 10812 6045 8142 239 1696 497 C ATOM 2425 CG PHE A 321 -5.958 5.606 14.115 1.00 70.60 C ANISOU 2425 CG PHE A 321 11234 6751 8839 162 1851 495 C ATOM 2426 CD1 PHE A 321 -7.311 5.720 14.389 1.00 63.55 C ANISOU 2426 CD1 PHE A 321 10139 5848 8160 43 1846 402 C ATOM 2427 CD2 PHE A 321 -5.049 5.959 15.100 1.00 70.88 C ANISOU 2427 CD2 PHE A 321 11289 6906 8736 209 2002 583 C ATOM 2428 CE1 PHE A 321 -7.749 6.177 15.619 1.00 68.19 C ANISOU 2428 CE1 PHE A 321 10557 6534 8817 -16 2001 395 C ATOM 2429 CE2 PHE A 321 -5.480 6.417 16.332 1.00 70.10 C ANISOU 2429 CE2 PHE A 321 11032 6901 8700 141 2146 570 C ATOM 2430 CZ PHE A 321 -6.832 6.526 16.592 1.00 75.20 C ANISOU 2430 CZ PHE A 321 11488 7528 9556 34 2152 476 C ATOM 2431 N PHE A 322 -6.509 8.321 12.175 1.00 71.53 N ANISOU 2431 N PHE A 322 11188 6928 9064 343 1482 344 N ATOM 2432 CA PHE A 322 -6.373 9.726 12.557 1.00 64.83 C ANISOU 2432 CA PHE A 322 10247 6165 8219 404 1506 334 C ATOM 2433 C PHE A 322 -5.451 10.479 11.599 1.00 65.53 C ANISOU 2433 C PHE A 322 10470 6262 8168 526 1392 379 C ATOM 2434 O PHE A 322 -4.734 11.401 11.998 1.00 70.50 O ANISOU 2434 O PHE A 322 11116 6960 8711 567 1452 418 O ATOM 2435 CB PHE A 322 -5.885 9.853 14.006 1.00 64.87 C ANISOU 2435 CB PHE A 322 10221 6266 8162 364 1719 382 C ATOM 2436 CG PHE A 322 -6.035 11.232 14.587 1.00 64.46 C ANISOU 2436 CG PHE A 322 10055 6284 8155 394 1761 336 C ATOM 2437 CD1 PHE A 322 -7.088 12.050 14.215 1.00 66.19 C ANISOU 2437 CD1 PHE A 322 10131 6471 8545 425 1663 239 C ATOM 2438 CD2 PHE A 322 -5.123 11.703 15.517 1.00 64.92 C ANISOU 2438 CD2 PHE A 322 10151 6438 8076 398 1897 387 C ATOM 2439 CE1 PHE A 322 -7.224 13.316 14.754 1.00 72.41 C ANISOU 2439 CE1 PHE A 322 10840 7300 9373 469 1709 192 C ATOM 2440 CE2 PHE A 322 -5.254 12.966 16.060 1.00 58.69 C ANISOU 2440 CE2 PHE A 322 9283 5693 7323 417 1938 330 C ATOM 2441 CZ PHE A 322 -6.305 13.774 15.678 1.00 69.16 C ANISOU 2441 CZ PHE A 322 10488 6963 8825 458 1848 232 C ATOM 2442 N GLY A 323 -5.462 10.085 10.326 1.00 59.45 N ANISOU 2442 N GLY A 323 9801 5422 7366 573 1229 372 N ATOM 2443 CA GLY A 323 -4.610 10.713 9.333 1.00 72.84 C ANISOU 2443 CA GLY A 323 11630 7127 8917 685 1124 424 C ATOM 2444 C GLY A 323 -3.130 10.576 9.598 1.00 71.10 C ANISOU 2444 C GLY A 323 11554 6982 8480 725 1233 538 C ATOM 2445 O GLY A 323 -2.345 11.396 9.114 1.00 69.09 O ANISOU 2445 O GLY A 323 11370 6774 8109 795 1195 592 O ATOM 2446 N ASN A 324 -2.725 9.556 10.357 1.00 77.46 N ANISOU 2446 N ASN A 324 12402 7807 9224 682 1370 583 N ATOM 2447 CA ASN A 324 -1.342 9.355 10.786 1.00 79.83 C ANISOU 2447 CA ASN A 324 12806 8208 9318 726 1489 697 C ATOM 2448 C ASN A 324 -0.788 10.563 11.536 1.00 72.51 C ANISOU 2448 C ASN A 324 11806 7402 8344 714 1569 726 C ATOM 2449 O ASN A 324 0.431 10.757 11.595 1.00 83.71 O ANISOU 2449 O ASN A 324 13296 8929 9581 756 1619 817 O ATOM 2450 CB ASN A 324 -0.432 9.002 9.603 1.00 70.54 C ANISOU 2450 CB ASN A 324 11804 7031 7966 836 1404 759 C ATOM 2451 CG ASN A 324 -0.321 7.506 9.383 1.00 85.80 C ANISOU 2451 CG ASN A 324 13869 8887 9845 860 1424 776 C ATOM 2452 ND2 ASN A 324 0.900 6.988 9.451 1.00 99.21 N ANISOU 2452 ND2 ASN A 324 15688 10664 11346 948 1509 881 N ATOM 2453 OD1 ASN A 324 -1.320 6.824 9.160 1.00 81.07 O ANISOU 2453 OD1 ASN A 324 13264 8160 9380 799 1366 695 O ATOM 2454 N TYR A 325 -1.667 11.379 12.113 1.00 62.23 N ANISOU 2454 N TYR A 325 10359 6084 7200 656 1582 645 N ATOM 2455 CA TYR A 325 -1.248 12.524 12.908 1.00 71.12 C ANISOU 2455 CA TYR A 325 11429 7300 8293 631 1663 648 C ATOM 2456 C TYR A 325 -0.918 12.078 14.326 1.00 70.80 C ANISOU 2456 C TYR A 325 11344 7361 8195 566 1845 678 C ATOM 2457 O TYR A 325 -1.725 11.407 14.977 1.00 69.23 O ANISOU 2457 O TYR A 325 11069 7132 8102 512 1916 639 O ATOM 2458 CB TYR A 325 -2.349 13.584 12.947 1.00 64.57 C ANISOU 2458 CB TYR A 325 10479 6403 7653 621 1608 541 C ATOM 2459 CG TYR A 325 -2.345 14.563 11.795 1.00 66.50 C ANISOU 2459 CG TYR A 325 10776 6583 7907 694 1452 536 C ATOM 2460 CD1 TYR A 325 -1.219 15.321 11.500 1.00 63.23 C ANISOU 2460 CD1 TYR A 325 10467 6218 7339 715 1447 610 C ATOM 2461 CD2 TYR A 325 -3.480 14.747 11.016 1.00 72.45 C ANISOU 2461 CD2 TYR A 325 11471 7236 8821 739 1311 463 C ATOM 2462 CE1 TYR A 325 -1.220 16.224 10.452 1.00 58.15 C ANISOU 2462 CE1 TYR A 325 9888 5507 6700 777 1314 620 C ATOM 2463 CE2 TYR A 325 -3.490 15.647 9.969 1.00 67.56 C ANISOU 2463 CE2 TYR A 325 10911 6557 8200 820 1167 472 C ATOM 2464 CZ TYR A 325 -2.359 16.381 9.690 1.00 66.43 C ANISOU 2464 CZ TYR A 325 10893 6447 7903 839 1174 555 C ATOM 2465 OH TYR A 325 -2.372 17.276 8.645 1.00 69.13 O ANISOU 2465 OH TYR A 325 11308 6720 8237 914 1039 579 O ATOM 2466 N LYS A 326 0.261 12.453 14.806 1.00 63.63 N ANISOU 2466 N LYS A 326 10478 6586 7112 566 1920 750 N ATOM 2467 CA LYS A 326 0.600 12.223 16.204 1.00 64.52 C ANISOU 2467 CA LYS A 326 10542 6821 7152 508 2084 775 C ATOM 2468 C LYS A 326 -0.132 13.243 17.067 1.00 71.85 C ANISOU 2468 C LYS A 326 11352 7750 8199 441 2139 669 C ATOM 2469 O LYS A 326 0.012 14.449 16.835 1.00 71.48 O ANISOU 2469 O LYS A 326 11305 7693 8161 439 2087 626 O ATOM 2470 CB LYS A 326 2.105 12.313 16.418 1.00 75.91 C ANISOU 2470 CB LYS A 326 12049 8433 8360 527 2131 881 C ATOM 2471 CG LYS A 326 2.873 11.143 15.819 1.00 71.58 C ANISOU 2471 CG LYS A 326 11611 7910 7675 617 2119 994 C ATOM 2472 CD LYS A 326 4.365 11.248 16.082 1.00 73.83 C ANISOU 2472 CD LYS A 326 11926 8401 7727 645 2171 1104 C ATOM 2473 CE LYS A 326 5.123 10.142 15.365 1.00 81.51 C ANISOU 2473 CE LYS A 326 13011 9397 8564 769 2156 1212 C ATOM 2474 NZ LYS A 326 4.750 8.794 15.876 1.00 82.68 N1+ ANISOU 2474 NZ LYS A 326 13201 9484 8731 804 2236 1243 N1+ ATOM 2475 N PRO A 327 -0.925 12.811 18.053 1.00 70.15 N ANISOU 2475 N PRO A 327 11042 7539 8071 388 2250 624 N ATOM 2476 CA PRO A 327 -1.813 13.762 18.751 1.00 61.24 C ANISOU 2476 CA PRO A 327 9795 6397 7079 347 2298 505 C ATOM 2477 C PRO A 327 -1.096 14.944 19.383 1.00 68.99 C ANISOU 2477 C PRO A 327 10790 7470 7953 319 2346 478 C ATOM 2478 O PRO A 327 -1.535 16.089 19.216 1.00 77.41 O ANISOU 2478 O PRO A 327 11831 8465 9117 330 2300 386 O ATOM 2479 CB PRO A 327 -2.500 12.876 19.799 1.00 64.42 C ANISOU 2479 CB PRO A 327 10110 6833 7532 289 2442 498 C ATOM 2480 CG PRO A 327 -2.481 11.509 19.199 1.00 64.50 C ANISOU 2480 CG PRO A 327 10189 6782 7536 302 2406 580 C ATOM 2481 CD PRO A 327 -1.188 11.414 18.441 1.00 65.08 C ANISOU 2481 CD PRO A 327 10406 6890 7431 369 2329 677 C ATOM 2482 N LYS A 328 -0.003 14.707 20.106 1.00 70.59 N ANISOU 2482 N LYS A 328 11037 7829 7956 284 2434 554 N ATOM 2483 CA LYS A 328 0.704 15.791 20.775 1.00 68.66 C ANISOU 2483 CA LYS A 328 10803 7686 7597 229 2478 518 C ATOM 2484 C LYS A 328 1.793 16.419 19.918 1.00 82.05 C ANISOU 2484 C LYS A 328 12592 9403 9179 233 2375 575 C ATOM 2485 O LYS A 328 2.143 17.583 20.144 1.00 86.76 O ANISOU 2485 O LYS A 328 13209 10012 9742 176 2371 518 O ATOM 2486 CB LYS A 328 1.318 15.289 22.085 1.00 57.44 C ANISOU 2486 CB LYS A 328 9362 6457 6004 177 2622 565 C ATOM 2487 CG LYS A 328 0.305 15.077 23.194 1.00 53.92 C ANISOU 2487 CG LYS A 328 8823 6018 5646 145 2753 489 C ATOM 2488 CD LYS A 328 0.969 14.566 24.458 1.00 75.35 C ANISOU 2488 CD LYS A 328 11533 8933 8163 102 2890 552 C ATOM 2489 CE LYS A 328 1.713 15.680 25.173 1.00 57.05 C ANISOU 2489 CE LYS A 328 9227 6746 5702 34 2916 488 C ATOM 2490 NZ LYS A 328 0.800 16.514 26.004 1.00 63.08 N1+ ANISOU 2490 NZ LYS A 328 9930 7475 6562 -6 3000 330 N1+ ATOM 2491 N THR A 329 2.324 15.687 18.942 1.00 69.73 N ANISOU 2491 N THR A 329 11096 7840 7557 295 2298 683 N ATOM 2492 CA THR A 329 3.434 16.169 18.130 1.00 70.63 C ANISOU 2492 CA THR A 329 11289 8006 7542 299 2217 756 C ATOM 2493 C THR A 329 2.964 16.952 16.907 1.00 76.39 C ANISOU 2493 C THR A 329 12068 8561 8396 336 2082 719 C ATOM 2494 O THR A 329 3.580 17.960 16.543 1.00 80.95 O ANISOU 2494 O THR A 329 12698 9142 8916 295 2037 728 O ATOM 2495 CB THR A 329 4.313 14.983 17.703 1.00 74.99 C ANISOU 2495 CB THR A 329 11890 8663 7940 368 2216 896 C ATOM 2496 CG2 THR A 329 5.152 15.320 16.479 1.00 54.52 C ANISOU 2496 CG2 THR A 329 9375 6082 5258 406 2113 970 C ATOM 2497 OG1 THR A 329 5.188 14.623 18.779 1.00 71.11 O ANISOU 2497 OG1 THR A 329 11365 8382 7270 333 2326 957 O ATOM 2498 N ASP A 330 1.860 16.535 16.287 1.00 73.26 N ANISOU 2498 N ASP A 330 11655 8013 8168 406 2014 677 N ATOM 2499 CA ASP A 330 1.451 17.060 14.989 1.00 72.50 C ANISOU 2499 CA ASP A 330 11611 7770 8165 468 1867 665 C ATOM 2500 C ASP A 330 0.250 17.997 15.030 1.00 74.89 C ANISOU 2500 C ASP A 330 11858 7925 8670 482 1829 544 C ATOM 2501 O ASP A 330 0.188 18.922 14.220 1.00 75.93 O ANISOU 2501 O ASP A 330 12051 7956 8841 517 1728 538 O ATOM 2502 CB ASP A 330 1.135 15.903 14.033 1.00 74.21 C ANISOU 2502 CB ASP A 330 11860 7932 8407 551 1785 710 C ATOM 2503 CG ASP A 330 2.364 15.091 13.674 1.00 77.25 C ANISOU 2503 CG ASP A 330 12329 8436 8586 581 1800 835 C ATOM 2504 OD1 ASP A 330 3.485 15.635 13.764 1.00 82.81 O ANISOU 2504 OD1 ASP A 330 13068 9262 9136 549 1829 900 O ATOM 2505 OD2 ASP A 330 2.210 13.906 13.312 1.00 76.77 O1- ANISOU 2505 OD2 ASP A 330 12300 8351 8518 637 1785 866 O1- ATOM 2506 N ILE A 331 -0.704 17.777 15.943 1.00 66.53 N ANISOU 2506 N ILE A 331 10687 6856 7737 466 1911 455 N ATOM 2507 CA ILE A 331 -1.937 18.577 15.930 1.00 73.41 C ANISOU 2507 CA ILE A 331 11484 7600 8810 510 1875 339 C ATOM 2508 C ILE A 331 -1.672 20.062 16.122 1.00 76.17 C ANISOU 2508 C ILE A 331 11893 7894 9153 496 1879 289 C ATOM 2509 O ILE A 331 -2.322 20.879 15.441 1.00 75.00 O ANISOU 2509 O ILE A 331 11761 7605 9130 574 1781 246 O ATOM 2510 CB ILE A 331 -2.943 18.003 16.944 1.00 68.39 C ANISOU 2510 CB ILE A 331 10700 6995 8292 488 1987 260 C ATOM 2511 CG1 ILE A 331 -3.423 16.623 16.487 1.00 57.85 C ANISOU 2511 CG1 ILE A 331 9321 5654 7006 498 1950 301 C ATOM 2512 CG2 ILE A 331 -4.123 18.943 17.130 1.00 67.00 C ANISOU 2512 CG2 ILE A 331 10429 6724 8306 543 1980 135 C ATOM 2513 CD1 ILE A 331 -4.044 16.617 15.106 1.00 60.15 C ANISOU 2513 CD1 ILE A 331 9620 5826 7407 579 1768 295 C ATOM 2514 N PRO A 332 -0.770 20.501 17.011 1.00 72.33 N ANISOU 2514 N PRO A 332 11449 7505 8528 400 1983 289 N ATOM 2515 CA PRO A 332 -0.399 21.926 17.017 1.00 68.31 C ANISOU 2515 CA PRO A 332 11036 6917 8003 367 1969 247 C ATOM 2516 C PRO A 332 0.049 22.434 15.659 1.00 68.27 C ANISOU 2516 C PRO A 332 11152 6815 7973 404 1828 331 C ATOM 2517 O PRO A 332 -0.211 23.596 15.320 1.00 76.56 O ANISOU 2517 O PRO A 332 12278 7713 9098 431 1777 290 O ATOM 2518 CB PRO A 332 0.736 21.983 18.047 1.00 56.39 C ANISOU 2518 CB PRO A 332 9551 5576 6301 232 2083 261 C ATOM 2519 CG PRO A 332 0.436 20.874 18.980 1.00 58.99 C ANISOU 2519 CG PRO A 332 9766 6036 6613 225 2192 253 C ATOM 2520 CD PRO A 332 -0.160 19.779 18.146 1.00 68.48 C ANISOU 2520 CD PRO A 332 10921 7196 7902 316 2120 313 C ATOM 2521 N GLY A 333 0.705 21.590 14.858 1.00 69.39 N ANISOU 2521 N GLY A 333 11325 7034 8006 415 1769 453 N ATOM 2522 CA GLY A 333 1.053 21.983 13.504 1.00 61.63 C ANISOU 2522 CA GLY A 333 10454 5970 6992 462 1638 538 C ATOM 2523 C GLY A 333 -0.158 22.215 12.623 1.00 64.89 C ANISOU 2523 C GLY A 333 10858 6212 7585 595 1512 499 C ATOM 2524 O GLY A 333 -0.136 23.088 11.752 1.00 67.58 O ANISOU 2524 O GLY A 333 11302 6433 7942 639 1416 533 O ATOM 2525 N VAL A 334 -1.233 21.455 12.840 1.00 67.68 N ANISOU 2525 N VAL A 334 11085 6559 8073 656 1510 432 N ATOM 2526 CA VAL A 334 -2.470 21.699 12.103 1.00 75.86 C ANISOU 2526 CA VAL A 334 12075 7461 9288 781 1387 382 C ATOM 2527 C VAL A 334 -3.096 23.018 12.543 1.00 70.93 C ANISOU 2527 C VAL A 334 11448 6711 8790 823 1408 288 C ATOM 2528 O VAL A 334 -3.610 23.792 11.719 1.00 77.11 O ANISOU 2528 O VAL A 334 12281 7358 9659 932 1291 290 O ATOM 2529 CB VAL A 334 -3.437 20.516 12.290 1.00 67.07 C ANISOU 2529 CB VAL A 334 10808 6392 8284 806 1389 331 C ATOM 2530 CG1 VAL A 334 -4.686 20.709 11.446 1.00 67.87 C ANISOU 2530 CG1 VAL A 334 10840 6389 8559 929 1241 283 C ATOM 2531 CG2 VAL A 334 -2.744 19.208 11.942 1.00 63.82 C ANISOU 2531 CG2 VAL A 334 10433 6078 7736 766 1385 418 C ATOM 2532 N VAL A 335 -3.058 23.299 13.848 1.00 71.66 N ANISOU 2532 N VAL A 335 11494 6847 8887 750 1559 206 N ATOM 2533 CA VAL A 335 -3.530 24.596 14.328 1.00 70.39 C ANISOU 2533 CA VAL A 335 11361 6558 8825 791 1595 108 C ATOM 2534 C VAL A 335 -2.733 25.723 13.678 1.00 72.16 C ANISOU 2534 C VAL A 335 11786 6661 8972 772 1534 170 C ATOM 2535 O VAL A 335 -3.290 26.758 13.289 1.00 76.97 O ANISOU 2535 O VAL A 335 12463 7095 9688 875 1473 138 O ATOM 2536 CB VAL A 335 -3.458 24.658 15.865 1.00 79.56 C ANISOU 2536 CB VAL A 335 12463 7806 9962 699 1776 7 C ATOM 2537 CG1 VAL A 335 -3.582 26.095 16.349 1.00 66.29 C ANISOU 2537 CG1 VAL A 335 10876 5983 8328 716 1823 -92 C ATOM 2538 CG2 VAL A 335 -4.547 23.792 16.477 1.00 59.72 C ANISOU 2538 CG2 VAL A 335 9749 5372 7571 742 1840 -65 C ATOM 2539 N GLU A 336 -1.421 25.530 13.531 1.00 73.89 N ANISOU 2539 N GLU A 336 12100 6974 9001 644 1550 270 N ATOM 2540 CA GLU A 336 -0.594 26.538 12.873 1.00 83.50 C ANISOU 2540 CA GLU A 336 13501 8092 10133 596 1499 347 C ATOM 2541 C GLU A 336 -0.941 26.661 11.394 1.00 75.64 C ANISOU 2541 C GLU A 336 12575 6985 9181 727 1335 439 C ATOM 2542 O GLU A 336 -0.942 27.767 10.841 1.00 69.90 O ANISOU 2542 O GLU A 336 11990 6086 8481 763 1276 466 O ATOM 2543 CB GLU A 336 0.888 26.208 13.050 1.00 73.20 C ANISOU 2543 CB GLU A 336 12245 6958 8611 426 1558 439 C ATOM 2544 CG GLU A 336 1.362 26.230 14.494 1.00 68.83 C ANISOU 2544 CG GLU A 336 11642 6526 7985 285 1706 356 C ATOM 2545 CD GLU A 336 1.165 27.578 15.166 1.00 89.30 C ANISOU 2545 CD GLU A 336 14327 8964 10640 237 1760 240 C ATOM 2546 OE1 GLU A 336 1.120 28.607 14.457 1.00 81.32 O ANISOU 2546 OE1 GLU A 336 13460 7759 9677 265 1689 262 O ATOM 2547 OE2 GLU A 336 1.052 27.607 16.409 1.00 89.41 O1- ANISOU 2547 OE2 GLU A 336 14280 9043 10648 177 1876 125 O1- ATOM 2548 N LYS A 337 -1.224 25.534 10.735 1.00 72.91 N ANISOU 2548 N LYS A 337 12301 7388 8014 -189 2087 969 N ATOM 2549 CA LYS A 337 -1.694 25.579 9.354 1.00 77.05 C ANISOU 2549 CA LYS A 337 12802 8109 8364 72 1966 1112 C ATOM 2550 C LYS A 337 -2.947 26.434 9.234 1.00 89.67 C ANISOU 2550 C LYS A 337 14507 9437 10127 246 1959 1250 C ATOM 2551 O LYS A 337 -3.135 27.138 8.235 1.00 91.41 O ANISOU 2551 O LYS A 337 14811 9703 10217 388 1957 1488 O ATOM 2552 CB LYS A 337 -1.960 24.166 8.838 1.00 83.28 C ANISOU 2552 CB LYS A 337 13382 9203 9056 266 1734 891 C ATOM 2553 CG LYS A 337 -1.035 23.733 7.717 1.00 96.83 C ANISOU 2553 CG LYS A 337 15023 11339 10428 332 1672 927 C ATOM 2554 CD LYS A 337 -1.256 22.276 7.359 1.00 88.78 C ANISOU 2554 CD LYS A 337 13799 10581 9350 516 1421 651 C ATOM 2555 CE LYS A 337 -0.304 21.834 6.266 1.00 94.51 C ANISOU 2555 CE LYS A 337 14445 11753 9710 610 1354 659 C ATOM 2556 NZ LYS A 337 -0.009 20.380 6.344 1.00 98.78 N1+ ANISOU 2556 NZ LYS A 337 14806 12506 10218 667 1159 339 N1+ ATOM 2557 N TYR A 338 -3.819 26.383 10.243 1.00 84.50 N ANISOU 2557 N TYR A 338 13845 8515 9748 251 1957 1111 N ATOM 2558 CA TYR A 338 -4.948 27.311 10.249 1.00 80.80 C ANISOU 2558 CA TYR A 338 13487 7770 9443 406 1972 1239 C ATOM 2559 C TYR A 338 -4.480 28.746 10.468 1.00 84.44 C ANISOU 2559 C TYR A 338 14183 7956 9945 251 2165 1465 C ATOM 2560 O TYR A 338 -4.961 29.670 9.801 1.00 74.81 O ANISOU 2560 O TYR A 338 13091 6619 8715 394 2173 1692 O ATOM 2561 CB TYR A 338 -5.980 26.928 11.309 1.00 78.81 C ANISOU 2561 CB TYR A 338 13151 7327 9467 454 1937 1041 C ATOM 2562 CG TYR A 338 -7.043 27.997 11.498 1.00 78.83 C ANISOU 2562 CG TYR A 338 13279 7026 9647 595 1983 1158 C ATOM 2563 CD1 TYR A 338 -8.090 28.128 10.595 1.00 90.21 C ANISOU 2563 CD1 TYR A 338 14688 8513 11076 887 1847 1245 C ATOM 2564 CD2 TYR A 338 -7.004 28.870 12.579 1.00 73.48 C ANISOU 2564 CD2 TYR A 338 12749 6026 9144 456 2147 1162 C ATOM 2565 CE1 TYR A 338 -9.065 29.096 10.758 1.00 87.30 C ANISOU 2565 CE1 TYR A 338 14430 7876 10865 1037 1880 1346 C ATOM 2566 CE2 TYR A 338 -7.976 29.845 12.749 1.00 70.95 C ANISOU 2566 CE2 TYR A 338 12545 5430 8984 611 2176 1250 C ATOM 2567 CZ TYR A 338 -9.002 29.952 11.835 1.00 90.08 C ANISOU 2567 CZ TYR A 338 14931 7903 11391 901 2045 1348 C ATOM 2568 OH TYR A 338 -9.967 30.920 12.005 1.00 91.68 O ANISOU 2568 OH TYR A 338 15248 7838 11749 1072 2069 1430 O ATOM 2569 N MET A 339 -3.548 28.952 11.402 1.00 82.34 N ANISOU 2569 N MET A 339 13977 7572 9737 -37 2310 1404 N ATOM 2570 CA MET A 339 -3.109 30.306 11.735 1.00 85.68 C ANISOU 2570 CA MET A 339 14618 7686 10252 -207 2476 1584 C ATOM 2571 C MET A 339 -2.402 30.981 10.568 1.00 80.14 C ANISOU 2571 C MET A 339 14008 7092 9350 -239 2524 1895 C ATOM 2572 O MET A 339 -2.508 32.202 10.400 1.00 86.24 O ANISOU 2572 O MET A 339 14969 7589 10209 -256 2606 2128 O ATOM 2573 CB MET A 339 -2.198 30.272 12.964 1.00 76.76 C ANISOU 2573 CB MET A 339 13504 6450 9212 -507 2596 1418 C ATOM 2574 CG MET A 339 -2.899 29.894 14.268 1.00 75.31 C ANISOU 2574 CG MET A 339 13270 6103 9241 -484 2592 1159 C ATOM 2575 SD MET A 339 -3.703 31.283 15.101 1.00 90.01 S ANISOU 2575 SD MET A 339 15341 7482 11377 -441 2683 1195 S ATOM 2576 CE MET A 339 -5.269 31.391 14.247 1.00 92.83 C ANISOU 2576 CE MET A 339 15677 7821 11774 -65 2553 1308 C ATOM 2577 N ASN A 340 -1.673 30.216 9.757 1.00 87.47 N ANISOU 2577 N ASN A 340 14805 8419 10012 -242 2475 1912 N ATOM 2578 CA ASN A 340 -1.008 30.757 8.581 1.00 82.00 C ANISOU 2578 CA ASN A 340 14165 7905 9087 -247 2526 2224 C ATOM 2579 C ASN A 340 -1.945 30.890 7.383 1.00 83.32 C ANISOU 2579 C ASN A 340 14340 8189 9130 94 2406 2400 C ATOM 2580 O ASN A 340 -1.467 31.054 6.253 1.00 77.47 O ANISOU 2580 O ASN A 340 13594 7714 8127 158 2416 2640 O ATOM 2581 CB ASN A 340 0.203 29.893 8.218 1.00 91.53 C ANISOU 2581 CB ASN A 340 15215 9531 10031 -371 2529 2160 C ATOM 2582 CG ASN A 340 1.277 29.916 9.291 1.00 87.34 C ANISOU 2582 CG ASN A 340 14687 8903 9595 -719 2660 2034 C ATOM 2583 ND2 ASN A 340 1.982 31.037 9.397 1.00104.77 N ANISOU 2583 ND2 ASN A 340 17035 10909 11864 -956 2822 2260 N ATOM 2584 OD1 ASN A 340 1.467 28.942 10.020 1.00 84.95 O ANISOU 2584 OD1 ASN A 340 14259 8698 9318 -774 2608 1739 O ATOM 2585 N LYS A 341 -3.258 30.817 7.617 1.00 93.32 N ANISOU 2585 N LYS A 341 15604 9285 10567 320 2296 2287 N ATOM 2586 CA LYS A 341 -4.276 31.008 6.582 1.00105.07 C ANISOU 2586 CA LYS A 341 17102 10849 11972 662 2170 2432 C ATOM 2587 C LYS A 341 -4.130 30.006 5.441 1.00 96.61 C ANISOU 2587 C LYS A 341 15851 10271 10587 861 2015 2392 C ATOM 2588 O LYS A 341 -4.454 30.306 4.289 1.00 92.50 O ANISOU 2588 O LYS A 341 15354 9919 9873 1101 1949 2603 O ATOM 2589 CB LYS A 341 -4.259 32.443 6.048 1.00 92.00 C ANISOU 2589 CB LYS A 341 15672 8968 10317 673 2281 2818 C ATOM 2590 CG LYS A 341 -4.646 33.483 7.089 1.00 96.01 C ANISOU 2590 CG LYS A 341 16369 8955 11157 556 2386 2834 C ATOM 2591 CD LYS A 341 -3.824 34.753 6.942 1.00117.56 C ANISOU 2591 CD LYS A 341 19308 11447 13912 342 2555 3166 C ATOM 2592 CE LYS A 341 -3.861 35.583 8.216 1.00117.53 C ANISOU 2592 CE LYS A 341 19464 10947 14246 145 2656 3080 C ATOM 2593 NZ LYS A 341 -2.530 35.645 8.881 1.00117.87 N1+ ANISOU 2593 NZ LYS A 341 19513 10953 14321 -242 2792 3032 N1+ ATOM 2594 N GLU A 342 -3.643 28.807 5.756 1.00 88.54 N ANISOU 2594 N GLU A 342 14650 9485 9507 780 1945 2113 N ATOM 2595 CA GLU A 342 -3.555 27.710 4.801 1.00 88.97 C ANISOU 2595 CA GLU A 342 14517 9991 9295 985 1762 1992 C ATOM 2596 C GLU A 342 -4.721 26.740 4.922 1.00 89.53 C ANISOU 2596 C GLU A 342 14429 10083 9506 1212 1533 1704 C ATOM 2597 O GLU A 342 -5.280 26.318 3.906 1.00 90.90 O ANISOU 2597 O GLU A 342 14506 10508 9522 1509 1344 1683 O ATOM 2598 CB GLU A 342 -2.237 26.952 4.991 1.00 89.37 C ANISOU 2598 CB GLU A 342 14463 10304 9189 772 1806 1861 C ATOM 2599 CG GLU A 342 -1.897 25.989 3.867 1.00 95.21 C ANISOU 2599 CG GLU A 342 15035 11545 9596 985 1638 1777 C ATOM 2600 CD GLU A 342 -0.673 25.150 4.176 1.00101.73 C ANISOU 2600 CD GLU A 342 15744 12613 10295 794 1663 1598 C ATOM 2601 OE1 GLU A 342 0.328 25.714 4.666 1.00101.76 O ANISOU 2601 OE1 GLU A 342 15826 12539 10299 501 1870 1724 O ATOM 2602 OE2 GLU A 342 -0.708 23.928 3.924 1.00 96.44 O1- ANISOU 2602 OE2 GLU A 342 14900 12206 9536 942 1463 1324 O1- ATOM 2603 N LEU A 343 -5.100 26.384 6.146 1.00 90.45 N ANISOU 2603 N LEU A 343 14504 9945 9916 1078 1544 1486 N ATOM 2604 CA LEU A 343 -6.240 25.516 6.407 1.00 88.40 C ANISOU 2604 CA LEU A 343 14083 9660 9847 1249 1350 1237 C ATOM 2605 C LEU A 343 -7.429 26.379 6.810 1.00 89.21 C ANISOU 2605 C LEU A 343 14278 9424 10192 1350 1388 1328 C ATOM 2606 O LEU A 343 -7.376 27.077 7.828 1.00 90.07 O ANISOU 2606 O LEU A 343 14512 9218 10492 1166 1562 1368 O ATOM 2607 CB LEU A 343 -5.908 24.505 7.504 1.00 81.89 C ANISOU 2607 CB LEU A 343 13133 8801 9181 1049 1343 960 C ATOM 2608 CG LEU A 343 -7.054 23.622 7.996 1.00 76.18 C ANISOU 2608 CG LEU A 343 12232 7998 8714 1162 1174 726 C ATOM 2609 CD1 LEU A 343 -7.414 22.579 6.952 1.00 65.58 C ANISOU 2609 CD1 LEU A 343 10702 6961 7253 1409 894 578 C ATOM 2610 CD2 LEU A 343 -6.688 22.961 9.316 1.00 69.91 C ANISOU 2610 CD2 LEU A 343 11374 7085 8105 918 1245 539 C ATOM 2611 N GLU A 344 -8.495 26.332 6.014 1.00 89.53 N ANISOU 2611 N GLU A 344 14253 9543 10221 1658 1214 1343 N ATOM 2612 CA GLU A 344 -9.682 27.150 6.240 1.00 86.39 C ANISOU 2612 CA GLU A 344 13929 8869 10026 1807 1227 1433 C ATOM 2613 C GLU A 344 -10.701 26.328 7.025 1.00 81.27 C ANISOU 2613 C GLU A 344 13086 8134 9661 1850 1112 1170 C ATOM 2614 O GLU A 344 -11.215 25.322 6.525 1.00 97.84 O ANISOU 2614 O GLU A 344 14977 10446 11753 2013 887 996 O ATOM 2615 CB GLU A 344 -10.260 27.636 4.912 1.00 91.52 C ANISOU 2615 CB GLU A 344 14617 9665 10491 2129 1108 1620 C ATOM 2616 CG GLU A 344 -9.406 28.688 4.217 1.00102.78 C ANISOU 2616 CG GLU A 344 16260 11115 11678 2089 1259 1958 C ATOM 2617 CD GLU A 344 -9.558 28.663 2.707 1.00114.46 C ANISOU 2617 CD GLU A 344 17710 12933 12845 2396 1110 2101 C ATOM 2618 OE1 GLU A 344 -10.506 28.017 2.215 1.00108.79 O ANISOU 2618 OE1 GLU A 344 16830 12375 12132 2671 881 1937 O ATOM 2619 OE2 GLU A 344 -8.729 29.290 2.013 1.00109.96 O1- ANISOU 2619 OE2 GLU A 344 17271 12483 12026 2364 1222 2380 O1- ATOM 2620 N LEU A 345 -10.997 26.765 8.252 1.00 86.22 N ANISOU 2620 N LEU A 345 13771 8452 10538 1709 1261 1142 N ATOM 2621 CA LEU A 345 -11.858 26.015 9.158 1.00 89.10 C ANISOU 2621 CA LEU A 345 13944 8736 11173 1707 1199 924 C ATOM 2622 C LEU A 345 -13.283 26.546 9.243 1.00 86.77 C ANISOU 2622 C LEU A 345 13619 8283 11069 1937 1156 956 C ATOM 2623 O LEU A 345 -14.171 25.809 9.684 1.00 81.04 O ANISOU 2623 O LEU A 345 12677 7567 10547 1996 1054 791 O ATOM 2624 CB LEU A 345 -11.267 26.004 10.574 1.00 77.41 C ANISOU 2624 CB LEU A 345 12509 7072 9831 1415 1393 842 C ATOM 2625 CG LEU A 345 -9.939 25.285 10.809 1.00 70.72 C ANISOU 2625 CG LEU A 345 11644 6372 8855 1166 1434 751 C ATOM 2626 CD1 LEU A 345 -9.524 25.397 12.271 1.00 71.63 C ANISOU 2626 CD1 LEU A 345 11808 6288 9119 917 1622 674 C ATOM 2627 CD2 LEU A 345 -10.025 23.840 10.385 1.00 73.68 C ANISOU 2627 CD2 LEU A 345 11779 7006 9208 1229 1214 559 C ATOM 2628 N GLU A 346 -13.523 27.799 8.846 1.00 81.64 N ANISOU 2628 N GLU A 346 13169 7483 10366 2066 1229 1171 N ATOM 2629 CA GLU A 346 -14.844 28.391 9.040 1.00 88.96 C ANISOU 2629 CA GLU A 346 14081 8240 11480 2288 1205 1196 C ATOM 2630 C GLU A 346 -15.909 27.660 8.232 1.00 87.18 C ANISOU 2630 C GLU A 346 13619 8232 11275 2564 950 1099 C ATOM 2631 O GLU A 346 -17.033 27.463 8.708 1.00 93.11 O ANISOU 2631 O GLU A 346 14206 8920 12252 2677 893 994 O ATOM 2632 CB GLU A 346 -14.819 29.874 8.673 1.00 91.29 C ANISOU 2632 CB GLU A 346 14656 8325 11705 2386 1312 1457 C ATOM 2633 CG GLU A 346 -16.009 30.664 9.199 1.00 89.28 C ANISOU 2633 CG GLU A 346 14434 7821 11666 2572 1342 1472 C ATOM 2634 CD GLU A 346 -16.133 30.602 10.709 1.00105.45 C ANISOU 2634 CD GLU A 346 16442 9679 13944 2402 1486 1312 C ATOM 2635 OE1 GLU A 346 -17.075 29.948 11.205 1.00103.60 O ANISOU 2635 OE1 GLU A 346 15974 9506 13883 2487 1418 1148 O ATOM 2636 OE2 GLU A 346 -15.288 31.208 11.400 1.00115.07 O1- ANISOU 2636 OE2 GLU A 346 17854 10698 15170 2186 1665 1352 O1- ATOM 2637 N LYS A 347 -15.574 27.243 7.008 1.00 81.29 N ANISOU 2637 N LYS A 347 12837 7758 10293 2680 789 1125 N ATOM 2638 CA LYS A 347 -16.543 26.544 6.170 1.00 78.13 C ANISOU 2638 CA LYS A 347 12209 7575 9900 2955 517 1008 C ATOM 2639 C LYS A 347 -16.967 25.209 6.767 1.00 86.95 C ANISOU 2639 C LYS A 347 13031 8761 11246 2866 387 732 C ATOM 2640 O LYS A 347 -18.025 24.687 6.399 1.00 85.42 O ANISOU 2640 O LYS A 347 12615 8665 11176 3068 175 612 O ATOM 2641 CB LYS A 347 -15.973 26.332 4.767 1.00 77.66 C ANISOU 2641 CB LYS A 347 12175 7823 9507 3101 371 1071 C ATOM 2642 CG LYS A 347 -14.480 26.061 4.735 1.00 83.87 C ANISOU 2642 CG LYS A 347 13059 8724 10085 2857 477 1097 C ATOM 2643 CD LYS A 347 -14.071 25.426 3.417 1.00 81.18 C ANISOU 2643 CD LYS A 347 12638 8767 9438 3030 276 1059 C ATOM 2644 CE LYS A 347 -12.596 25.640 3.133 1.00 86.07 C ANISOU 2644 CE LYS A 347 13415 9514 9773 2854 426 1202 C ATOM 2645 NZ LYS A 347 -12.169 24.985 1.868 1.00 87.14 N1+ ANISOU 2645 NZ LYS A 347 13459 10066 9583 3044 234 1151 N1+ ATOM 2646 N PHE A 348 -16.168 24.642 7.673 1.00 86.63 N ANISOU 2646 N PHE A 348 12975 8669 11272 2570 503 636 N ATOM 2647 CA PHE A 348 -16.571 23.437 8.386 1.00 86.00 C ANISOU 2647 CA PHE A 348 12629 8606 11441 2462 409 414 C ATOM 2648 C PHE A 348 -17.587 23.720 9.484 1.00 77.62 C ANISOU 2648 C PHE A 348 11480 7332 10678 2451 516 406 C ATOM 2649 O PHE A 348 -18.312 22.806 9.891 1.00 75.62 O ANISOU 2649 O PHE A 348 10960 7107 10664 2439 404 259 O ATOM 2650 CB PHE A 348 -15.350 22.746 8.999 1.00 82.06 C ANISOU 2650 CB PHE A 348 12151 8131 10896 2164 499 329 C ATOM 2651 CG PHE A 348 -14.443 22.100 7.992 1.00 85.48 C ANISOU 2651 CG PHE A 348 12581 8827 11072 2182 349 267 C ATOM 2652 CD1 PHE A 348 -13.409 22.817 7.411 1.00 79.54 C ANISOU 2652 CD1 PHE A 348 12055 8151 10015 2157 461 429 C ATOM 2653 CD2 PHE A 348 -14.613 20.771 7.637 1.00 78.90 C ANISOU 2653 CD2 PHE A 348 11508 8164 10307 2225 93 46 C ATOM 2654 CE1 PHE A 348 -12.566 22.223 6.489 1.00 85.57 C ANISOU 2654 CE1 PHE A 348 12799 9197 10516 2192 333 373 C ATOM 2655 CE2 PHE A 348 -13.773 20.171 6.715 1.00 80.71 C ANISOU 2655 CE2 PHE A 348 11732 8652 10284 2271 -56 -37 C ATOM 2656 CZ PHE A 348 -12.748 20.898 6.140 1.00 78.24 C ANISOU 2656 CZ PHE A 348 11638 8452 9637 2263 71 127 C ATOM 2657 N ILE A 349 -17.654 24.956 9.970 1.00 75.61 N ANISOU 2657 N ILE A 349 11436 6870 10422 2460 727 561 N ATOM 2658 CA ILE A 349 -18.536 25.319 11.073 1.00 87.44 C ANISOU 2658 CA ILE A 349 12870 8183 12169 2467 853 550 C ATOM 2659 C ILE A 349 -19.846 25.833 10.486 1.00 73.56 C ANISOU 2659 C ILE A 349 11035 6430 10485 2788 733 596 C ATOM 2660 O ILE A 349 -19.907 26.942 9.950 1.00 83.62 O ANISOU 2660 O ILE A 349 12524 7620 11630 2954 772 753 O ATOM 2661 CB ILE A 349 -17.887 26.364 11.987 1.00 87.84 C ANISOU 2661 CB ILE A 349 13189 7998 12189 2316 1130 651 C ATOM 2662 CG1 ILE A 349 -16.586 25.817 12.578 1.00 78.73 C ANISOU 2662 CG1 ILE A 349 12091 6863 10961 2003 1237 590 C ATOM 2663 CG2 ILE A 349 -18.852 26.785 13.085 1.00 76.44 C ANISOU 2663 CG2 ILE A 349 11676 6394 10974 2375 1251 626 C ATOM 2664 CD1 ILE A 349 -15.909 26.762 13.546 1.00 80.74 C ANISOU 2664 CD1 ILE A 349 12585 6892 11201 1838 1490 653 C ATOM 2665 N THR A 350 -20.902 25.025 10.595 1.00 76.91 N ANISOU 2665 N THR A 350 11145 6947 11128 2875 582 468 N ATOM 2666 CA THR A 350 -22.204 25.385 10.053 1.00 87.54 C ANISOU 2666 CA THR A 350 12368 8331 12563 3183 444 484 C ATOM 2667 C THR A 350 -23.177 25.905 11.102 1.00 85.06 C ANISOU 2667 C THR A 350 11973 7872 12474 3242 590 497 C ATOM 2668 O THR A 350 -24.105 26.640 10.748 1.00 79.43 O ANISOU 2668 O THR A 350 11258 7134 11787 3514 545 555 O ATOM 2669 CB THR A 350 -22.838 24.182 9.344 1.00 83.27 C ANISOU 2669 CB THR A 350 11500 8010 12128 3274 144 323 C ATOM 2670 CG2 THR A 350 -22.000 23.766 8.144 1.00 83.19 C ANISOU 2670 CG2 THR A 350 11569 8181 11857 3303 -32 296 C ATOM 2671 OG1 THR A 350 -22.933 23.082 10.258 1.00 87.74 O ANISOU 2671 OG1 THR A 350 11817 8579 12940 3048 150 191 O ATOM 2672 N HIS A 351 -22.996 25.545 12.371 1.00 88.72 N ANISOU 2672 N HIS A 351 12364 8259 13085 3016 762 444 N ATOM 2673 CA HIS A 351 -23.911 25.965 13.421 1.00 83.24 C ANISOU 2673 CA HIS A 351 11567 7474 12588 3082 908 446 C ATOM 2674 C HIS A 351 -23.130 26.384 14.657 1.00 84.70 C ANISOU 2674 C HIS A 351 11938 7497 12745 2870 1183 466 C ATOM 2675 O HIS A 351 -21.955 26.048 14.825 1.00 81.87 O ANISOU 2675 O HIS A 351 11709 7123 12273 2629 1245 453 O ATOM 2676 CB HIS A 351 -24.906 24.856 13.796 1.00 84.87 C ANISOU 2676 CB HIS A 351 11355 7823 13070 3066 801 341 C ATOM 2677 CG HIS A 351 -25.756 24.388 12.657 1.00 88.95 C ANISOU 2677 CG HIS A 351 11647 8498 13651 3272 509 286 C ATOM 2678 CD2 HIS A 351 -27.078 24.544 12.411 1.00 85.79 C ANISOU 2678 CD2 HIS A 351 11023 8170 13404 3519 397 272 C ATOM 2679 ND1 HIS A 351 -25.252 23.666 11.598 1.00 85.28 N ANISOU 2679 ND1 HIS A 351 11165 8157 13081 3250 281 219 N ATOM 2680 CE1 HIS A 351 -26.226 23.394 10.748 1.00 96.91 C ANISOU 2680 CE1 HIS A 351 12417 9764 14641 3474 32 157 C ATOM 2681 NE2 HIS A 351 -27.345 23.915 11.219 1.00 87.47 N ANISOU 2681 NE2 HIS A 351 11088 8538 13608 3634 97 192 N ATOM 2682 N THR A 352 -23.811 27.131 15.525 1.00 88.64 N ANISOU 2682 N THR A 352 12442 7892 13344 2983 1340 483 N ATOM 2683 CA THR A 352 -23.274 27.509 16.827 1.00 86.41 C ANISOU 2683 CA THR A 352 12291 7481 13059 2826 1590 468 C ATOM 2684 C THR A 352 -24.437 27.610 17.800 1.00 80.74 C ANISOU 2684 C THR A 352 11349 6798 12528 2962 1690 433 C ATOM 2685 O THR A 352 -25.392 28.352 17.549 1.00 99.53 O ANISOU 2685 O THR A 352 13713 9149 14954 3241 1658 461 O ATOM 2686 CB THR A 352 -22.514 28.836 16.765 1.00 95.29 C ANISOU 2686 CB THR A 352 13818 8374 14014 2849 1708 543 C ATOM 2687 CG2 THR A 352 -21.644 29.005 18.003 1.00 73.77 C ANISOU 2687 CG2 THR A 352 11231 5537 11260 2624 1928 492 C ATOM 2688 OG1 THR A 352 -21.686 28.869 15.597 1.00 93.35 O ANISOU 2688 OG1 THR A 352 13747 8131 13589 2799 1592 619 O ATOM 2689 N VAL A 353 -24.360 26.864 18.897 1.00 81.17 N ANISOU 2689 N VAL A 353 11227 6933 12682 2779 1812 383 N ATOM 2690 CA VAL A 353 -25.401 26.879 19.921 1.00 77.84 C ANISOU 2690 CA VAL A 353 10566 6590 12420 2890 1936 366 C ATOM 2691 C VAL A 353 -24.739 27.069 21.281 1.00 76.88 C ANISOU 2691 C VAL A 353 10559 6415 12238 2740 2183 332 C ATOM 2692 O VAL A 353 -23.562 26.718 21.448 1.00 78.32 O ANISOU 2692 O VAL A 353 10891 6553 12314 2492 2223 314 O ATOM 2693 CB VAL A 353 -26.239 25.590 19.892 1.00 85.98 C ANISOU 2693 CB VAL A 353 11161 7835 13672 2842 1818 361 C ATOM 2694 CG1 VAL A 353 -26.982 25.460 18.569 1.00 77.83 C ANISOU 2694 CG1 VAL A 353 9999 6867 12705 3025 1556 364 C ATOM 2695 CG2 VAL A 353 -25.355 24.377 20.137 1.00 73.89 C ANISOU 2695 CG2 VAL A 353 9558 6358 12159 2520 1802 343 C ATOM 2696 N PRO A 354 -25.437 27.622 22.269 1.00 78.42 N ANISOU 2696 N PRO A 354 10688 6629 12480 2897 2346 311 N ATOM 2697 CA PRO A 354 -24.892 27.650 23.629 1.00 79.39 C ANISOU 2697 CA PRO A 354 10866 6756 12542 2771 2571 263 C ATOM 2698 C PRO A 354 -24.871 26.252 24.231 1.00 86.29 C ANISOU 2698 C PRO A 354 11432 7832 13520 2548 2603 292 C ATOM 2699 O PRO A 354 -25.416 25.293 23.680 1.00 89.07 O ANISOU 2699 O PRO A 354 11502 8310 14031 2503 2455 342 O ATOM 2700 CB PRO A 354 -25.849 28.575 24.387 1.00 78.34 C ANISOU 2700 CB PRO A 354 10697 6635 12436 3062 2705 228 C ATOM 2701 CG PRO A 354 -27.116 28.540 23.600 1.00 80.34 C ANISOU 2701 CG PRO A 354 10713 6981 12831 3291 2557 276 C ATOM 2702 CD PRO A 354 -26.720 28.339 22.167 1.00 81.86 C ANISOU 2702 CD PRO A 354 11014 7089 12999 3229 2330 317 C ATOM 2703 N PHE A 355 -24.216 26.144 25.389 1.00 85.60 N ANISOU 2703 N PHE A 355 11404 7769 13349 2409 2792 260 N ATOM 2704 CA PHE A 355 -24.136 24.854 26.066 1.00 83.03 C ANISOU 2704 CA PHE A 355 10810 7624 13113 2199 2842 311 C ATOM 2705 C PHE A 355 -25.513 24.383 26.515 1.00 80.80 C ANISOU 2705 C PHE A 355 10119 7551 13028 2325 2884 392 C ATOM 2706 O PHE A 355 -25.862 23.208 26.347 1.00 96.43 O ANISOU 2706 O PHE A 355 11797 9651 15190 2188 2791 473 O ATOM 2707 CB PHE A 355 -23.177 24.942 27.253 1.00 79.35 C ANISOU 2707 CB PHE A 355 10504 7157 12490 2064 3043 261 C ATOM 2708 CG PHE A 355 -23.076 23.672 28.046 1.00 83.25 C ANISOU 2708 CG PHE A 355 10739 7835 13058 1866 3114 336 C ATOM 2709 CD1 PHE A 355 -23.648 23.576 29.304 1.00 81.99 C ANISOU 2709 CD1 PHE A 355 10381 7859 12911 1942 3318 381 C ATOM 2710 CD2 PHE A 355 -22.414 22.570 27.531 1.00 81.41 C ANISOU 2710 CD2 PHE A 355 10458 7596 12878 1618 2975 369 C ATOM 2711 CE1 PHE A 355 -23.557 22.406 30.035 1.00101.19 C ANISOU 2711 CE1 PHE A 355 12576 10458 15413 1760 3390 487 C ATOM 2712 CE2 PHE A 355 -22.319 21.397 28.257 1.00 85.36 C ANISOU 2712 CE2 PHE A 355 10731 8237 13465 1438 3030 453 C ATOM 2713 CZ PHE A 355 -22.892 21.314 29.510 1.00 82.39 C ANISOU 2713 CZ PHE A 355 10161 8035 13107 1502 3242 527 C ATOM 2714 N SER A 356 -26.319 25.295 27.065 1.00 76.63 N ANISOU 2714 N SER A 356 9568 7068 12479 2591 3013 369 N ATOM 2715 CA SER A 356 -27.666 24.966 27.519 1.00 87.84 C ANISOU 2715 CA SER A 356 10586 8716 14071 2738 3073 450 C ATOM 2716 C SER A 356 -28.562 24.449 26.402 1.00 87.80 C ANISOU 2716 C SER A 356 10322 8755 14285 2781 2845 506 C ATOM 2717 O SER A 356 -29.634 23.906 26.694 1.00 91.41 O ANISOU 2717 O SER A 356 10385 9414 14933 2833 2866 594 O ATOM 2718 CB SER A 356 -28.309 26.195 28.169 1.00 81.41 C ANISOU 2718 CB SER A 356 9840 7930 13162 3062 3229 383 C ATOM 2719 OG SER A 356 -28.522 27.224 27.218 1.00 82.32 O ANISOU 2719 OG SER A 356 10177 7858 13245 3277 3095 313 O ATOM 2720 N GLU A 357 -28.160 24.604 25.141 1.00 87.48 N ANISOU 2720 N GLU A 357 10509 8212 14518 663 3272 -1826 N ATOM 2721 CA GLU A 357 -28.916 24.102 24.001 1.00 83.49 C ANISOU 2721 CA GLU A 357 9900 7910 13911 917 3016 -1525 C ATOM 2722 C GLU A 357 -28.134 23.020 23.262 1.00 82.74 C ANISOU 2722 C GLU A 357 9805 7778 13854 626 2692 -1514 C ATOM 2723 O GLU A 357 -28.268 22.863 22.045 1.00 87.01 O ANISOU 2723 O GLU A 357 10477 8255 14327 841 2582 -1337 O ATOM 2724 CB GLU A 357 -29.289 25.245 23.058 1.00 98.81 C ANISOU 2724 CB GLU A 357 12169 9558 15818 1411 3320 -1390 C ATOM 2725 CG GLU A 357 -30.041 26.384 23.732 1.00101.50 C ANISOU 2725 CG GLU A 357 12563 9884 16118 1765 3649 -1418 C ATOM 2726 CD GLU A 357 -31.540 26.176 23.738 1.00116.81 C ANISOU 2726 CD GLU A 357 14157 12319 17907 2103 3488 -1136 C ATOM 2727 OE1 GLU A 357 -32.205 26.647 24.682 1.00117.68 O ANISOU 2727 OE1 GLU A 357 14127 12634 17950 2287 3651 -1174 O ATOM 2728 OE2 GLU A 357 -32.053 25.534 22.797 1.00116.08 O1- ANISOU 2728 OE2 GLU A 357 13933 12421 17753 2193 3188 -862 O1- ATOM 2729 N ILE A 358 -27.320 22.259 24.002 1.00 88.68 N ANISOU 2729 N ILE A 358 10417 8576 14699 153 2531 -1706 N ATOM 2730 CA ILE A 358 -26.434 21.267 23.396 1.00 90.03 C ANISOU 2730 CA ILE A 358 10615 8677 14915 -116 2255 -1741 C ATOM 2731 C ILE A 358 -27.215 20.255 22.568 1.00 87.51 C ANISOU 2731 C ILE A 358 10126 8660 14463 7 1775 -1499 C ATOM 2732 O ILE A 358 -26.728 19.781 21.531 1.00 80.18 O ANISOU 2732 O ILE A 358 9374 7594 13496 50 1623 -1464 O ATOM 2733 CB ILE A 358 -25.592 20.581 24.493 1.00 82.84 C ANISOU 2733 CB ILE A 358 9520 7822 14133 -645 2124 -1969 C ATOM 2734 CG1 ILE A 358 -24.511 19.689 23.878 1.00 73.30 C ANISOU 2734 CG1 ILE A 358 8384 6478 12988 -889 1909 -2035 C ATOM 2735 CG2 ILE A 358 -26.476 19.795 25.458 1.00 86.27 C ANISOU 2735 CG2 ILE A 358 9512 8753 14515 -822 1774 -1904 C ATOM 2736 CD1 ILE A 358 -23.253 19.595 24.721 1.00 83.07 C ANISOU 2736 CD1 ILE A 358 9623 7570 14368 -1321 2008 -2260 C ATOM 2737 N ASN A 359 -28.442 19.927 22.985 1.00 84.40 N ANISOU 2737 N ASN A 359 9401 8683 13986 84 1521 -1311 N ATOM 2738 CA ASN A 359 -29.220 18.928 22.261 1.00 77.98 C ANISOU 2738 CA ASN A 359 8416 8152 13062 152 992 -1050 C ATOM 2739 C ASN A 359 -29.540 19.380 20.844 1.00 83.99 C ANISOU 2739 C ASN A 359 9478 8726 13710 589 1060 -871 C ATOM 2740 O ASN A 359 -29.702 18.538 19.951 1.00 78.27 O ANISOU 2740 O ASN A 359 8786 8059 12892 625 638 -735 O ATOM 2741 CB ASN A 359 -30.502 18.601 23.024 1.00 75.88 C ANISOU 2741 CB ASN A 359 7698 8391 12741 146 735 -821 C ATOM 2742 CG ASN A 359 -30.280 17.571 24.110 1.00 94.98 C ANISOU 2742 CG ASN A 359 9759 11094 15233 -349 389 -901 C ATOM 2743 ND2 ASN A 359 -30.404 17.996 25.363 1.00 81.93 N ANISOU 2743 ND2 ASN A 359 7904 9615 13610 -464 635 -997 N ATOM 2744 OD1 ASN A 359 -29.999 16.407 23.829 1.00100.96 O ANISOU 2744 OD1 ASN A 359 10441 11909 16011 -615 -105 -880 O ATOM 2745 N LYS A 360 -29.625 20.695 20.612 1.00 83.15 N ANISOU 2745 N LYS A 360 9614 8376 13602 924 1562 -869 N ATOM 2746 CA LYS A 360 -29.808 21.183 19.249 1.00 83.36 C ANISOU 2746 CA LYS A 360 9952 8192 13528 1321 1658 -702 C ATOM 2747 C LYS A 360 -28.703 20.674 18.333 1.00 84.81 C ANISOU 2747 C LYS A 360 10416 8122 13688 1225 1573 -807 C ATOM 2748 O LYS A 360 -28.966 20.298 17.184 1.00 78.02 O ANISOU 2748 O LYS A 360 9698 7263 12682 1442 1333 -641 O ATOM 2749 CB LYS A 360 -29.863 22.711 19.225 1.00 80.24 C ANISOU 2749 CB LYS A 360 9804 7511 13172 1642 2226 -718 C ATOM 2750 CG LYS A 360 -31.277 23.266 19.158 1.00 80.62 C ANISOU 2750 CG LYS A 360 9715 7780 13137 2040 2252 -452 C ATOM 2751 CD LYS A 360 -31.385 24.618 19.840 1.00 99.98 C ANISOU 2751 CD LYS A 360 12283 10044 15660 2247 2764 -558 C ATOM 2752 CE LYS A 360 -32.814 25.142 19.797 1.00102.99 C ANISOU 2752 CE LYS A 360 12499 10679 15953 2683 2796 -284 C ATOM 2753 NZ LYS A 360 -33.035 26.103 18.679 1.00 98.21 N1+ ANISOU 2753 NZ LYS A 360 12230 9768 15317 3113 3032 -128 N1+ ATOM 2754 N ALA A 361 -27.462 20.634 18.831 1.00 89.20 N ANISOU 2754 N ALA A 361 11047 8472 14372 912 1758 -1071 N ATOM 2755 CA ALA A 361 -26.375 20.044 18.057 1.00 82.53 C ANISOU 2755 CA ALA A 361 10412 7448 13499 820 1671 -1163 C ATOM 2756 C ALA A 361 -26.717 18.618 17.647 1.00 84.53 C ANISOU 2756 C ALA A 361 10531 7957 13630 744 1043 -1093 C ATOM 2757 O ALA A 361 -26.563 18.243 16.478 1.00 90.88 O ANISOU 2757 O ALA A 361 11567 8686 14277 956 878 -1020 O ATOM 2758 CB ALA A 361 -25.074 20.082 18.860 1.00 61.21 C ANISOU 2758 CB ALA A 361 7715 4561 10981 437 1899 -1429 C ATOM 2759 N PHE A 362 -27.208 17.815 18.597 1.00 82.91 N ANISOU 2759 N PHE A 362 9964 8055 13483 449 664 -1101 N ATOM 2760 CA PHE A 362 -27.645 16.461 18.274 1.00 79.51 C ANISOU 2760 CA PHE A 362 9397 7857 12957 352 -7 -1001 C ATOM 2761 C PHE A 362 -28.687 16.476 17.165 1.00 87.12 C ANISOU 2761 C PHE A 362 10475 8897 13730 742 -245 -713 C ATOM 2762 O PHE A 362 -28.669 15.623 16.271 1.00 83.96 O ANISOU 2762 O PHE A 362 10232 8483 13188 818 -680 -664 O ATOM 2763 CB PHE A 362 -28.206 15.777 19.521 1.00 75.00 C ANISOU 2763 CB PHE A 362 8375 7635 12488 -12 -354 -974 C ATOM 2764 CG PHE A 362 -27.156 15.321 20.493 1.00 86.16 C ANISOU 2764 CG PHE A 362 9670 9003 14065 -458 -333 -1248 C ATOM 2765 CD1 PHE A 362 -26.482 16.237 21.285 1.00 62.63 C ANISOU 2765 CD1 PHE A 362 6719 5857 11219 -574 212 -1441 C ATOM 2766 CD2 PHE A 362 -26.848 13.977 20.620 1.00 81.43 C ANISOU 2766 CD2 PHE A 362 8943 8508 13491 -767 -891 -1306 C ATOM 2767 CE1 PHE A 362 -25.518 15.821 22.182 1.00 63.77 C ANISOU 2767 CE1 PHE A 362 6753 5958 11519 -1001 213 -1675 C ATOM 2768 CE2 PHE A 362 -25.884 13.553 21.517 1.00 64.90 C ANISOU 2768 CE2 PHE A 362 6728 6373 11558 -1180 -881 -1544 C ATOM 2769 CZ PHE A 362 -25.218 14.477 22.299 1.00 75.15 C ANISOU 2769 CZ PHE A 362 8041 7525 12990 -1304 -323 -1723 C ATOM 2770 N ASP A 363 -29.596 17.452 17.197 1.00 84.81 N ANISOU 2770 N ASP A 363 10128 8671 13423 1009 28 -522 N ATOM 2771 CA ASP A 363 -30.616 17.551 16.162 1.00 84.30 C ANISOU 2771 CA ASP A 363 10159 8678 13192 1379 -178 -219 C ATOM 2772 C ASP A 363 -30.055 18.105 14.859 1.00100.03 C ANISOU 2772 C ASP A 363 12616 10339 15054 1717 95 -235 C ATOM 2773 O ASP A 363 -30.613 17.837 13.789 1.00100.67 O ANISOU 2773 O ASP A 363 12858 10438 14953 1977 -201 -35 O ATOM 2774 CB ASP A 363 -31.773 18.422 16.648 1.00 95.12 C ANISOU 2774 CB ASP A 363 11295 10248 14597 1576 38 6 C ATOM 2775 CG ASP A 363 -32.485 17.827 17.844 1.00 89.64 C ANISOU 2775 CG ASP A 363 10105 9969 13986 1290 -266 100 C ATOM 2776 OD1 ASP A 363 -31.984 16.824 18.394 1.00 96.82 O ANISOU 2776 OD1 ASP A 363 10862 10970 14957 895 -602 -39 O ATOM 2777 OD2 ASP A 363 -33.540 18.365 18.238 1.00 90.12 O1- ANISOU 2777 OD2 ASP A 363 9917 10279 14045 1471 -165 329 O1- ATOM 2778 N TYR A 364 -28.965 18.878 14.921 1.00101.36 N ANISOU 2778 N TYR A 364 12999 10211 15303 1711 640 -445 N ATOM 2779 CA TYR A 364 -28.379 19.389 13.686 1.00 95.52 C ANISOU 2779 CA TYR A 364 12670 9191 14431 2017 907 -423 C ATOM 2780 C TYR A 364 -27.604 18.304 12.953 1.00 99.22 C ANISOU 2780 C TYR A 364 13325 9622 14753 1970 574 -534 C ATOM 2781 O TYR A 364 -27.576 18.291 11.716 1.00 97.65 O ANISOU 2781 O TYR A 364 13432 9333 14338 2286 525 -431 O ATOM 2782 CB TYR A 364 -27.498 20.601 13.978 1.00 85.75 C ANISOU 2782 CB TYR A 364 11585 7656 13340 2014 1570 -551 C ATOM 2783 CG TYR A 364 -28.294 21.851 14.273 1.00 94.44 C ANISOU 2783 CG TYR A 364 12659 8706 14517 2232 1922 -416 C ATOM 2784 CD1 TYR A 364 -29.281 22.289 13.399 1.00 95.04 C ANISOU 2784 CD1 TYR A 364 12838 8815 14457 2627 1882 -142 C ATOM 2785 CD2 TYR A 364 -28.055 22.598 15.418 1.00 91.68 C ANISOU 2785 CD2 TYR A 364 12205 8262 14366 2062 2279 -566 C ATOM 2786 CE1 TYR A 364 -30.012 23.433 13.661 1.00 86.01 C ANISOU 2786 CE1 TYR A 364 11676 7619 13386 2862 2200 -20 C ATOM 2787 CE2 TYR A 364 -28.780 23.742 15.688 1.00 89.37 C ANISOU 2787 CE2 TYR A 364 11926 7904 14127 2308 2588 -466 C ATOM 2788 CZ TYR A 364 -29.756 24.156 14.807 1.00 97.28 C ANISOU 2788 CZ TYR A 364 13013 8945 15002 2716 2554 -192 C ATOM 2789 OH TYR A 364 -30.478 25.296 15.075 1.00112.59 O ANISOU 2789 OH TYR A 364 14968 10814 16998 2993 2860 -94 O ATOM 2790 N MET A 365 -26.989 17.380 13.690 1.00 96.83 N ANISOU 2790 N MET A 365 12852 9393 14548 1600 333 -743 N ATOM 2791 CA MET A 365 -26.601 16.099 13.116 1.00 97.59 C ANISOU 2791 CA MET A 365 13064 9523 14493 1564 -171 -827 C ATOM 2792 C MET A 365 -27.874 15.277 12.950 1.00100.03 C ANISOU 2792 C MET A 365 13237 10071 14697 1589 -843 -624 C ATOM 2793 O MET A 365 -28.969 15.848 12.908 1.00112.94 O ANISOU 2793 O MET A 365 14767 11820 16324 1750 -823 -377 O ATOM 2794 CB MET A 365 -25.572 15.388 13.999 1.00 91.72 C ANISOU 2794 CB MET A 365 12165 8772 13912 1156 -235 -1099 C ATOM 2795 CG MET A 365 -24.658 14.419 13.253 1.00105.94 C ANISOU 2795 CG MET A 365 14208 10487 15558 1216 -491 -1252 C ATOM 2796 SD MET A 365 -22.954 14.446 13.841 1.00107.59 S ANISOU 2796 SD MET A 365 14393 10536 15948 941 -76 -1530 S ATOM 2797 CE MET A 365 -22.168 15.420 12.559 1.00103.37 C ANISOU 2797 CE MET A 365 14256 9784 15236 1378 517 -1453 C ATOM 2798 N LEU A 366 -27.762 13.951 12.849 1.00 87.71 N ANISOU 2798 N LEU A 366 11095 10079 12153 2360 918 129 N ATOM 2799 CA LEU A 366 -28.933 13.090 12.686 1.00103.77 C ANISOU 2799 CA LEU A 366 12858 12218 14353 2405 697 48 C ATOM 2800 C LEU A 366 -29.724 13.453 11.431 1.00100.96 C ANISOU 2800 C LEU A 366 12780 11712 13871 2573 363 -27 C ATOM 2801 O LEU A 366 -29.938 12.606 10.559 1.00101.96 O ANISOU 2801 O LEU A 366 12989 11782 13969 2524 230 -63 O ATOM 2802 CB LEU A 366 -29.835 13.165 13.923 1.00 80.51 C ANISOU 2802 CB LEU A 366 9449 9506 11635 2467 677 9 C ATOM 2803 CG LEU A 366 -29.245 12.648 15.235 1.00 85.87 C ANISOU 2803 CG LEU A 366 9789 10391 12447 2282 967 92 C ATOM 2804 CD1 LEU A 366 -30.268 12.732 16.357 1.00 69.41 C ANISOU 2804 CD1 LEU A 366 7270 8547 10557 2359 934 41 C ATOM 2805 CD2 LEU A 366 -28.755 11.223 15.063 1.00 57.40 C ANISOU 2805 CD2 LEU A 366 6048 6809 8953 2080 1073 171 C ATOM 2806 N LYS A 367 -30.175 14.705 11.340 1.00 92.77 N ANISOU 2806 N LYS A 367 11880 10605 12764 2762 218 -50 N ATOM 2807 CA LYS A 367 -30.842 15.221 10.152 1.00 96.25 C ANISOU 2807 CA LYS A 367 12607 10893 13071 2918 -107 -78 C ATOM 2808 C LYS A 367 -29.873 15.563 9.027 1.00107.24 C ANISOU 2808 C LYS A 367 14523 12075 14149 2877 -65 -17 C ATOM 2809 O LYS A 367 -30.318 16.027 7.971 1.00104.21 O ANISOU 2809 O LYS A 367 14422 11565 13607 2987 -332 -15 O ATOM 2810 CB LYS A 367 -31.665 16.462 10.509 1.00 95.61 C ANISOU 2810 CB LYS A 367 12450 10799 13080 3140 -260 -101 C ATOM 2811 CG LYS A 367 -33.144 16.190 10.723 1.00 90.34 C ANISOU 2811 CG LYS A 367 11414 10245 12666 3265 -525 -164 C ATOM 2812 CD LYS A 367 -33.740 17.150 11.739 1.00 89.54 C ANISOU 2812 CD LYS A 367 11057 10206 12758 3426 -482 -201 C ATOM 2813 CE LYS A 367 -34.963 17.855 11.179 1.00 87.88 C ANISOU 2813 CE LYS A 367 10834 9897 12659 3655 -831 -207 C ATOM 2814 NZ LYS A 367 -35.749 18.533 12.246 1.00 97.57 N1+ ANISOU 2814 NZ LYS A 367 11712 11204 14156 3813 -775 -265 N1+ ATOM 2815 N GLY A 368 -28.573 15.355 9.225 1.00105.37 N ANISOU 2815 N GLY A 368 14413 11798 13826 2718 260 52 N ATOM 2816 CA GLY A 368 -27.599 15.639 8.185 1.00104.02 C ANISOU 2816 CA GLY A 368 14726 11426 13371 2674 343 123 C ATOM 2817 C GLY A 368 -27.523 17.095 7.787 1.00110.51 C ANISOU 2817 C GLY A 368 15857 12098 14035 2833 247 182 C ATOM 2818 O GLY A 368 -27.148 17.402 6.651 1.00118.12 O ANISOU 2818 O GLY A 368 17238 12900 14741 2851 185 237 O ATOM 2819 N GLU A 369 -27.871 18.005 8.696 1.00 96.04 N ANISOU 2819 N GLU A 369 13830 10311 12351 2948 241 172 N ATOM 2820 CA GLU A 369 -27.874 19.428 8.385 1.00110.54 C ANISOU 2820 CA GLU A 369 15917 11987 14095 3111 143 224 C ATOM 2821 C GLU A 369 -26.554 20.112 8.710 1.00 94.60 C ANISOU 2821 C GLU A 369 14096 9856 11993 3037 436 322 C ATOM 2822 O GLU A 369 -26.211 21.112 8.069 1.00 89.84 O ANISOU 2822 O GLU A 369 13825 9066 11245 3126 387 406 O ATOM 2823 CB GLU A 369 -29.003 20.132 9.142 1.00105.82 C ANISOU 2823 CB GLU A 369 15016 11461 13731 3291 -19 144 C ATOM 2824 CG GLU A 369 -30.226 20.442 8.297 1.00107.19 C ANISOU 2824 CG GLU A 369 15232 11578 13919 3472 -411 133 C ATOM 2825 CD GLU A 369 -31.475 20.646 9.133 1.00108.53 C ANISOU 2825 CD GLU A 369 14978 11863 14394 3617 -544 41 C ATOM 2826 OE1 GLU A 369 -31.425 20.384 10.352 1.00107.58 O ANISOU 2826 OE1 GLU A 369 14531 11899 14444 3561 -325 -32 O ATOM 2827 OE2 GLU A 369 -32.506 21.071 8.570 1.00101.63 O1- ANISOU 2827 OE2 GLU A 369 14096 10926 13594 3784 -862 54 O1- ATOM 2828 N SER A 370 -25.806 19.602 9.683 1.00 86.20 N ANISOU 2828 N SER A 370 12827 8897 11027 2869 725 332 N ATOM 2829 CA SER A 370 -24.605 20.259 10.174 1.00 85.48 C ANISOU 2829 CA SER A 370 12861 8716 10902 2784 988 429 C ATOM 2830 C SER A 370 -23.360 19.476 9.783 1.00 97.53 C ANISOU 2830 C SER A 370 14552 10181 12325 2583 1239 550 C ATOM 2831 O SER A 370 -23.375 18.242 9.745 1.00 95.55 O ANISOU 2831 O SER A 370 14147 10033 12126 2461 1299 530 O ATOM 2832 CB SER A 370 -24.648 20.412 11.697 1.00 87.24 C ANISOU 2832 CB SER A 370 12719 9108 11320 2730 1128 369 C ATOM 2833 OG SER A 370 -24.470 19.160 12.338 1.00 80.07 O ANISOU 2833 OG SER A 370 11506 8395 10521 2547 1278 372 O ATOM 2834 N ILE A 371 -22.286 20.206 9.491 1.00 92.17 N ANISOU 2834 N ILE A 371 14174 9317 11528 2553 1392 682 N ATOM 2835 CA ILE A 371 -20.959 19.616 9.362 1.00 79.12 C ANISOU 2835 CA ILE A 371 12632 7592 9837 2357 1689 824 C ATOM 2836 C ILE A 371 -20.374 19.529 10.765 1.00 76.74 C ANISOU 2836 C ILE A 371 12018 7413 9726 2201 1901 866 C ATOM 2837 O ILE A 371 -20.134 18.435 11.287 1.00 84.12 O ANISOU 2837 O ILE A 371 12688 8485 10790 2035 2046 887 O ATOM 2838 CB ILE A 371 -20.057 20.440 8.425 1.00 78.68 C ANISOU 2838 CB ILE A 371 13025 7282 9587 2390 1765 973 C ATOM 2839 CG1 ILE A 371 -20.589 20.393 6.992 1.00 79.67 C ANISOU 2839 CG1 ILE A 371 13473 7315 9482 2509 1562 948 C ATOM 2840 CG2 ILE A 371 -18.623 19.923 8.477 1.00 76.24 C ANISOU 2840 CG2 ILE A 371 12779 6890 9299 2186 2109 1139 C ATOM 2841 CD1 ILE A 371 -19.676 21.052 5.981 1.00 69.41 C ANISOU 2841 CD1 ILE A 371 12624 5784 7966 2527 1661 1113 C ATOM 2842 N ARG A 372 -20.155 20.687 11.386 1.00 85.70 N ANISOU 2842 N ARG A 372 13180 8498 10884 2247 1909 880 N ATOM 2843 CA ARG A 372 -19.737 20.773 12.777 1.00 81.05 C ANISOU 2843 CA ARG A 372 12310 8043 10441 2104 2061 893 C ATOM 2844 C ARG A 372 -20.506 21.899 13.450 1.00 85.52 C ANISOU 2844 C ARG A 372 12800 8645 11049 2255 1915 747 C ATOM 2845 O ARG A 372 -20.733 22.952 12.848 1.00 75.88 O ANISOU 2845 O ARG A 372 11835 7241 9755 2430 1781 727 O ATOM 2846 CB ARG A 372 -18.227 21.016 12.902 1.00 68.62 C ANISOU 2846 CB ARG A 372 10887 6325 8860 1931 2309 1098 C ATOM 2847 CG ARG A 372 -17.391 19.753 12.800 1.00 73.42 C ANISOU 2847 CG ARG A 372 11403 6960 9534 1721 2531 1246 C ATOM 2848 CD ARG A 372 -17.658 18.826 13.976 1.00 71.55 C ANISOU 2848 CD ARG A 372 10713 6999 9473 1567 2586 1215 C ATOM 2849 NE ARG A 372 -16.837 17.623 13.930 1.00 74.93 N ANISOU 2849 NE ARG A 372 11018 7434 10017 1361 2804 1378 N ATOM 2850 CZ ARG A 372 -17.070 16.587 13.136 1.00 76.00 C ANISOU 2850 CZ ARG A 372 11161 7550 10166 1367 2817 1355 C ATOM 2851 NH1 ARG A 372 -18.098 16.572 12.303 1.00 80.11 N1+ ANISOU 2851 NH1 ARG A 372 11813 8056 10567 1553 2604 1184 N1+ ATOM 2852 NH2 ARG A 372 -16.252 15.539 13.179 1.00 79.11 N ANISOU 2852 NH2 ARG A 372 11422 7927 10710 1173 3046 1509 N ATOM 2853 N CYS A 373 -20.909 21.671 14.698 1.00 71.75 N ANISOU 2853 N CYS A 373 10698 7133 9430 2185 1951 649 N ATOM 2854 CA CYS A 373 -21.674 22.645 15.471 1.00 68.71 C ANISOU 2854 CA CYS A 373 10202 6802 9103 2316 1856 480 C ATOM 2855 C CYS A 373 -20.890 22.995 16.729 1.00 71.70 C ANISOU 2855 C CYS A 373 10463 7266 9515 2128 2042 499 C ATOM 2856 O CYS A 373 -20.710 22.146 17.610 1.00 73.71 O ANISOU 2856 O CYS A 373 10426 7753 9826 1938 2163 529 O ATOM 2857 CB CYS A 373 -23.060 22.104 15.824 1.00 63.09 C ANISOU 2857 CB CYS A 373 9166 6309 8495 2423 1716 316 C ATOM 2858 SG CYS A 373 -23.985 23.148 16.974 1.00 84.38 S ANISOU 2858 SG CYS A 373 11660 9103 11297 2559 1675 94 S ATOM 2859 N ILE A 374 -20.434 24.246 16.813 1.00 74.80 N ANISOU 2859 N ILE A 374 11078 7469 9874 2173 2053 490 N ATOM 2860 CA ILE A 374 -19.672 24.691 17.972 1.00 76.71 C ANISOU 2860 CA ILE A 374 11247 7770 10129 1986 2204 496 C ATOM 2861 C ILE A 374 -20.612 24.909 19.149 1.00 73.46 C ANISOU 2861 C ILE A 374 10550 7587 9773 2021 2185 264 C ATOM 2862 O ILE A 374 -21.659 25.556 19.018 1.00 78.41 O ANISOU 2862 O ILE A 374 11178 8166 10448 2255 2054 81 O ATOM 2863 CB ILE A 374 -18.889 25.969 17.641 1.00 71.03 C ANISOU 2863 CB ILE A 374 10862 6750 9375 2021 2212 555 C ATOM 2864 CG1 ILE A 374 -17.961 25.732 16.447 1.00 69.00 C ANISOU 2864 CG1 ILE A 374 10886 6273 9057 1991 2257 799 C ATOM 2865 CG2 ILE A 374 -18.100 26.444 18.852 1.00 63.90 C ANISOU 2865 CG2 ILE A 374 9894 5903 8483 1808 2344 550 C ATOM 2866 CD1 ILE A 374 -17.058 24.526 16.605 1.00 65.73 C ANISOU 2866 CD1 ILE A 374 10347 5972 8655 1737 2435 995 C ATOM 2867 N ILE A 375 -20.244 24.363 20.306 1.00 72.35 N ANISOU 2867 N ILE A 375 10159 7697 9633 1784 2323 283 N ATOM 2868 CA ILE A 375 -20.991 24.535 21.547 1.00 71.86 C ANISOU 2868 CA ILE A 375 9831 7883 9588 1773 2351 75 C ATOM 2869 C ILE A 375 -20.181 25.441 22.463 1.00 76.35 C ANISOU 2869 C ILE A 375 10497 8423 10091 1609 2453 36 C ATOM 2870 O ILE A 375 -18.989 25.200 22.688 1.00 75.96 O ANISOU 2870 O ILE A 375 10496 8367 10000 1360 2550 235 O ATOM 2871 CB ILE A 375 -21.285 23.183 22.221 1.00 70.92 C ANISOU 2871 CB ILE A 375 9331 8112 9503 1615 2417 127 C ATOM 2872 CG1 ILE A 375 -22.093 22.284 21.282 1.00 67.30 C ANISOU 2872 CG1 ILE A 375 8784 7662 9127 1770 2299 152 C ATOM 2873 CG2 ILE A 375 -22.022 23.387 23.531 1.00 64.23 C ANISOU 2873 CG2 ILE A 375 8220 7537 8646 1593 2470 -79 C ATOM 2874 CD1 ILE A 375 -21.704 20.823 21.351 1.00 68.75 C ANISOU 2874 CD1 ILE A 375 8737 8023 9362 1566 2378 344 C ATOM 2875 N THR A 376 -20.826 26.479 22.988 1.00 79.83 N ANISOU 2875 N THR A 376 10961 8833 10538 1744 2432 -219 N ATOM 2876 CA THR A 376 -20.161 27.492 23.799 1.00 79.80 C ANISOU 2876 CA THR A 376 11088 8761 10473 1614 2509 -309 C ATOM 2877 C THR A 376 -20.487 27.264 25.270 1.00 72.76 C ANISOU 2877 C THR A 376 9923 8219 9506 1447 2619 -469 C ATOM 2878 O THR A 376 -21.660 27.273 25.658 1.00 67.43 O ANISOU 2878 O THR A 376 9060 7692 8868 1604 2619 -688 O ATOM 2879 CB THR A 376 -20.590 28.896 23.371 1.00 73.75 C ANISOU 2879 CB THR A 376 10560 7683 9777 1872 2428 -498 C ATOM 2880 CG2 THR A 376 -19.768 29.950 24.099 1.00 63.88 C ANISOU 2880 CG2 THR A 376 9481 6313 8479 1721 2500 -580 C ATOM 2881 OG1 THR A 376 -20.412 29.043 21.957 1.00 65.81 O ANISOU 2881 OG1 THR A 376 9794 6386 8825 2037 2311 -332 O ATOM 2882 N MET A 377 -19.452 27.067 26.082 1.00 60.41 N ANISOU 2882 N MET A 377 8332 6787 7836 1124 2713 -348 N ATOM 2883 CA MET A 377 -19.644 26.947 27.517 1.00 67.33 C ANISOU 2883 CA MET A 377 8988 8001 8592 929 2815 -489 C ATOM 2884 C MET A 377 -19.980 28.310 28.122 1.00 72.88 C ANISOU 2884 C MET A 377 9843 8599 9250 1015 2844 -821 C ATOM 2885 O MET A 377 -19.834 29.360 27.488 1.00 87.93 O ANISOU 2885 O MET A 377 12027 10152 11232 1178 2783 -896 O ATOM 2886 CB MET A 377 -18.395 26.368 28.180 1.00 63.59 C ANISOU 2886 CB MET A 377 8450 7692 8020 538 2879 -232 C ATOM 2887 CG MET A 377 -17.861 25.107 27.520 1.00 75.44 C ANISOU 2887 CG MET A 377 9830 9224 9611 441 2874 116 C ATOM 2888 SD MET A 377 -19.149 23.927 27.088 1.00 82.75 S ANISOU 2888 SD MET A 377 10453 10343 10645 644 2846 95 S ATOM 2889 CE MET A 377 -19.049 22.821 28.492 1.00 78.60 C ANISOU 2889 CE MET A 377 9516 10303 10045 310 2951 216 C ATOM 2890 N GLY A 378 -20.437 28.284 29.370 1.00 76.98 N ANISOU 2890 N GLY A 378 10175 9427 9647 899 2949 -1022 N ATOM 2891 CA GLY A 378 -20.774 29.502 30.077 1.00 78.29 C ANISOU 2891 CA GLY A 378 10466 9521 9758 955 3014 -1372 C ATOM 2892 C GLY A 378 -22.093 30.132 29.695 1.00 87.42 C ANISOU 2892 C GLY A 378 11613 10527 11076 1337 3007 -1651 C ATOM 2893 O GLY A 378 -22.346 31.278 30.081 1.00 95.96 O ANISOU 2893 O GLY A 378 12836 11451 12172 1427 3062 -1946 O ATOM 2894 N ALA A 379 -22.942 29.428 28.953 1.00 91.36 N ANISOU 2894 N ALA A 379 11942 11055 11717 1558 2938 -1567 N ATOM 2895 CA ALA A 379 -24.241 29.962 28.563 1.00 87.73 C ANISOU 2895 CA ALA A 379 11434 10455 11445 1919 2910 -1793 C ATOM 2896 C ALA A 379 -25.218 28.833 28.258 1.00 98.19 C ANISOU 2896 C ALA A 379 12447 11994 12865 2047 2866 -1701 C ATOM 2897 O ALA A 379 -26.329 29.063 27.780 1.00 90.36 O ANISOU 2897 O ALA A 379 11375 10895 12063 2348 2806 -1817 O ATOM 2898 CB ALA A 379 -24.100 30.885 27.362 1.00 86.41 C ANISOU 2898 CB ALA A 379 11561 9831 11440 2151 2768 -1760 C ATOM 2899 OXT ALA A 379 -24.914 27.662 28.481 1.00 89.50 O1- ANISOU 2899 OXT ALA A 379 11157 11168 11679 1847 2882 -1497 O1- TER HETATM 2900 ZN ZN A 400 2.848 5.564 23.056 0.93 70.81 Zn2+ HETATM 2901 ZN ZN A 401 -15.077 13.411 16.277 0.89 74.86 Zn2+ HETATM 2902 O1 SO4 B 1 -17.900 13.242 9.851 0.93102.64 O HETATM 2903 O2 SO4 B 1 -19.952 12.148 10.377 0.93127.06 O HETATM 2904 O3 SO4 B 1 -18.763 13.326 12.073 0.93 95.00 O1- HETATM 2905 O4 SO4 B 1 -19.846 14.531 10.324 0.93 98.53 O HETATM 2906 S SO4 B 1 -19.115 13.312 10.656 0.93133.13 S HETATM 2907 O1 SO4 B 2 6.995 5.124 -0.301 0.41 76.04 O HETATM 2908 O2 SO4 B 2 5.619 7.023 -0.729 0.41 73.33 O HETATM 2909 O3 SO4 B 2 4.624 4.885 -0.374 0.41 77.02 O1- HETATM 2910 O4 SO4 B 2 5.651 6.039 1.442 0.41 66.59 O HETATM 2911 S SO4 B 2 5.722 5.768 0.009 0.41 74.13 S HETATM 2912 O1 SO4 B 3 -14.775 -12.748 3.070 0.81123.33 O HETATM 2913 O2 SO4 B 3 -16.551 -13.977 4.079 0.81127.21 O HETATM 2914 O3 SO4 B 3 -15.317 -12.385 5.360 0.81 97.97 O1- HETATM 2915 O4 SO4 B 3 -16.810 -11.647 3.654 0.81108.77 O HETATM 2916 S SO4 B 3 -15.863 -12.689 4.040 0.81134.84 S HETATM 2917 O1 SO4 B 4 -9.587 30.483 7.638 0.84 99.50 O HETATM 2918 O2 SO4 B 4 -11.571 30.166 6.355 0.84 90.11 O HETATM 2919 O3 SO4 B 4 -11.556 29.641 8.682 0.84100.87 O1- HETATM 2920 O4 SO4 B 4 -11.469 31.915 7.964 0.84115.05 O HETATM 2921 S SO4 B 4 -11.046 30.551 7.661 0.84109.90 S HETATM 2922 O1 SO4 B 5 10.240 3.103 7.921 0.75 87.12 O HETATM 2923 O2 SO4 B 5 7.932 3.302 8.443 0.75101.63 O HETATM 2924 O3 SO4 B 5 9.262 1.666 9.546 0.75102.78 O1- HETATM 2925 O4 SO4 B 5 9.573 3.979 10.040 0.75 85.73 O HETATM 2926 S SO4 B 5 9.253 3.015 8.991 0.75108.75 S HETATM 2927 O1 SO4 B 6 -19.863 -2.966 4.133 0.82104.80 O HETATM 2928 O2 SO4 B 6 -20.720 -2.274 2.018 0.82111.44 O HETATM 2929 O3 SO4 B 6 -22.081 -3.561 3.495 0.82114.53 O1- HETATM 2930 O4 SO4 B 6 -21.562 -1.296 4.023 0.82102.74 O HETATM 2931 S SO4 B 6 -21.056 -2.525 3.417 0.82124.42 S HETATM 2932 O1 SO4 B 7 2.003 10.033 -14.714 0.66 90.86 O HETATM 2933 O2 SO4 B 7 0.083 9.971 -13.301 0.66 96.83 O HETATM 2934 O3 SO4 B 7 2.181 9.195 -12.485 0.66 92.11 O1- HETATM 2935 O4 SO4 B 7 1.840 11.525 -12.866 0.66108.46 O HETATM 2936 S SO4 B 7 1.527 10.181 -13.341 0.66115.92 S HETATM 2937 O1 SO4 B 8 -7.755 4.843 25.537 0.80118.92 O HETATM 2938 O2 SO4 B 8 -8.881 6.721 24.594 0.80 66.79 O HETATM 2939 O3 SO4 B 8 -9.358 6.041 26.830 0.80 73.73 O1- HETATM 2940 O4 SO4 B 8 -7.261 7.047 26.307 0.80 82.86 O HETATM 2941 S SO4 B 8 -8.314 6.162 25.818 0.80107.50 S HETATM 2942 O1 SO4 B 9 -22.779 5.675 -17.583 0.88125.87 O HETATM 2943 O2 SO4 B 9 -23.916 3.656 -18.139 0.88111.03 O HETATM 2944 O3 SO4 B 9 -22.896 3.898 -15.997 0.88133.28 O1- HETATM 2945 O4 SO4 B 9 -24.855 5.149 -16.534 0.88129.62 O HETATM 2946 S SO4 B 9 -23.612 4.595 -17.063 0.88149.33 S HETATM 2947 O HOH C 5 -17.297 11.787 7.572 1.00 68.41 O HETATM 2948 O HOH C 8 -1.951 9.512 41.658 1.00 63.30 O HETATM 2949 O1 SO4 D 1 13.242 -17.900 -9.851 0.93102.64 A O HETATM 2950 O2 SO4 D 1 12.148 -19.952 -10.377 0.93127.06 A O HETATM 2951 O3 SO4 D 1 13.326 -18.763 -12.073 0.93 95.00 A O1- HETATM 2952 O4 SO4 D 1 14.531 -19.846 -10.324 0.93 98.53 A O HETATM 2953 S SO4 D 1 13.312 -19.115 -10.656 0.93133.13 A S HETATM 2954 O1 SO4 D 2 5.124 6.995 0.301 0.41 76.04 A O HETATM 2955 O2 SO4 D 2 7.023 5.619 0.729 0.41 73.33 A O HETATM 2956 O3 SO4 D 2 4.885 4.624 0.374 0.41 77.02 A O1- HETATM 2957 O4 SO4 D 2 6.039 5.651 -1.442 0.41 66.59 A O HETATM 2958 S SO4 D 2 5.768 5.722 -0.009 0.41 74.13 A S HETATM 2959 O1 SO4 D 3 -12.748 -14.775 -3.070 0.81123.33 A O HETATM 2960 O2 SO4 D 3 -13.977 -16.551 -4.079 0.81127.21 A O HETATM 2961 O3 SO4 D 3 -12.385 -15.317 -5.360 0.81 97.97 A O1- HETATM 2962 O4 SO4 D 3 -11.647 -16.810 -3.654 0.81108.77 A O HETATM 2963 S SO4 D 3 -12.689 -15.863 -4.040 0.81134.84 A S HETATM 2964 O1 SO4 D 4 30.483 -9.587 -7.638 0.84 99.50 A O HETATM 2965 O2 SO4 D 4 30.166 -11.571 -6.355 0.84 90.11 A O HETATM 2966 O3 SO4 D 4 29.641 -11.556 -8.682 0.84100.87 A O1- HETATM 2967 O4 SO4 D 4 31.915 -11.469 -7.964 0.84115.05 A O HETATM 2968 S SO4 D 4 30.551 -11.046 -7.661 0.84109.90 A S HETATM 2969 O1 SO4 D 5 3.103 10.240 -7.921 0.75 87.12 A O HETATM 2970 O2 SO4 D 5 3.302 7.932 -8.443 0.75101.63 A O HETATM 2971 O3 SO4 D 5 1.666 9.262 -9.546 0.75102.78 A O1- HETATM 2972 O4 SO4 D 5 3.979 9.573 -10.040 0.75 85.73 A O HETATM 2973 S SO4 D 5 3.015 9.253 -8.991 0.75108.75 A S HETATM 2974 O1 SO4 D 6 -2.966 -19.863 -4.133 0.82104.80 A O HETATM 2975 O2 SO4 D 6 -2.274 -20.720 -2.018 0.82111.44 A O HETATM 2976 O3 SO4 D 6 -3.561 -22.081 -3.495 0.82114.53 A O1- HETATM 2977 O4 SO4 D 6 -1.296 -21.562 -4.023 0.82102.74 A O HETATM 2978 S SO4 D 6 -2.525 -21.056 -3.417 0.82124.42 A S HETATM 2979 O1 SO4 D 7 10.033 2.003 14.714 0.66 90.86 A O HETATM 2980 O2 SO4 D 7 9.971 0.083 13.301 0.66 96.83 A O HETATM 2981 O3 SO4 D 7 9.195 2.181 12.485 0.66 92.11 A O1- HETATM 2982 O4 SO4 D 7 11.525 1.840 12.866 0.66108.46 A O HETATM 2983 S SO4 D 7 10.181 1.527 13.341 0.66115.92 A S HETATM 2984 O1 SO4 D 8 4.843 -7.755 -25.537 0.80118.92 A O HETATM 2985 O2 SO4 D 8 6.721 -8.881 -24.594 0.80 66.79 A O HETATM 2986 O3 SO4 D 8 6.041 -9.358 -26.830 0.80 73.73 A O1- HETATM 2987 O4 SO4 D 8 7.047 -7.261 -26.307 0.80 82.86 A O HETATM 2988 S SO4 D 8 6.162 -8.314 -25.818 0.80107.50 A S HETATM 2989 O1 SO4 D 9 5.675 -22.779 17.583 0.88125.87 A O HETATM 2990 O2 SO4 D 9 3.656 -23.916 18.139 0.88111.03 A O HETATM 2991 O3 SO4 D 9 3.898 -22.896 15.997 0.88133.28 A O1- HETATM 2992 O4 SO4 D 9 5.149 -24.855 16.534 0.88129.62 A O HETATM 2993 S SO4 D 9 4.595 -23.612 17.063 0.88149.33 A S ATOM 2994 N HIS E 0 34.302 -14.219 -47.176 1.00 98.76 A N ANISOU 2994 N HIS E 0 17049 9783 10692 -475 5776 -1340 A N ATOM 2995 CA HIS E 0 33.152 -15.042 -46.819 1.00130.71 A C ANISOU 2995 CA HIS E 0 20601 13995 15067 -308 5781 -1109 A C ATOM 2996 C HIS E 0 31.869 -14.232 -46.969 1.00126.00 A C ANISOU 2996 C HIS E 0 19642 13698 14532 -557 5674 -1126 A C ATOM 2997 O HIS E 0 31.804 -13.083 -46.528 1.00115.21 A O ANISOU 2997 O HIS E 0 18335 12394 13043 -905 5529 -1358 A O ATOM 2998 CB HIS E 0 33.299 -15.576 -45.391 1.00127.25 A C ANISOU 2998 CB HIS E 0 20177 13342 14830 -323 5593 -997 A C ATOM 2999 CG HIS E 0 32.001 -15.922 -44.728 1.00138.98 A C ANISOU 2999 CG HIS E 0 21138 15023 16644 -346 5467 -799 A C ATOM 3000 CD2 HIS E 0 31.471 -15.519 -43.550 1.00135.75 A C ANISOU 3000 CD2 HIS E 0 20573 14654 16353 -629 5260 -811 A C ATOM 3001 ND1 HIS E 0 31.085 -16.791 -45.282 1.00146.92 A N ANISOU 3001 ND1 HIS E 0 21713 16235 17874 -88 5534 -571 A N ATOM 3002 CE1 HIS E 0 30.047 -16.907 -44.472 1.00139.81 A C ANISOU 3002 CE1 HIS E 0 20451 15432 17240 -185 5345 -426 A C ATOM 3003 NE2 HIS E 0 30.255 -16.143 -43.415 1.00133.68 A N ANISOU 3003 NE2 HIS E 0 19809 14563 16420 -483 5183 -589 A N ATOM 3004 N MET E 1 30.857 -14.829 -47.600 1.00142.19 A N ANISOU 3004 N MET E 1 21316 15950 16758 -397 5685 -908 A N ATOM 3005 CA MET E 1 29.624 -14.103 -47.878 1.00147.37 A C ANISOU 3005 CA MET E 1 21702 16807 17484 -586 5472 -923 A C ATOM 3006 C MET E 1 28.955 -13.670 -46.579 1.00150.43 A C ANISOU 3006 C MET E 1 21857 17208 18093 -763 5179 -1006 A C ATOM 3007 O MET E 1 28.727 -14.481 -45.676 1.00155.70 A O ANISOU 3007 O MET E 1 22341 17812 19006 -669 5121 -812 A O ATOM 3008 CB MET E 1 28.666 -14.952 -48.727 1.00148.64 A C ANISOU 3008 CB MET E 1 21580 17138 17758 -460 5469 -606 A C ATOM 3009 CG MET E 1 28.083 -16.199 -48.068 1.00139.72 A C ANISOU 3009 CG MET E 1 20121 16037 16928 -310 5422 -291 A C ATOM 3010 SD MET E 1 29.293 -17.443 -47.587 1.00128.60 A S ANISOU 3010 SD MET E 1 18802 14504 15556 25 5702 -255 A S ATOM 3011 CE MET E 1 28.214 -18.741 -46.983 1.00118.20 A C ANISOU 3011 CE MET E 1 16994 13328 14587 131 5594 110 A C ATOM 3012 N SER E 2 28.660 -12.376 -46.483 1.00134.66 A N ANISOU 3012 N SER E 2 19837 15331 15995 -1016 4990 -1347 A N ATOM 3013 CA SER E 2 28.081 -11.818 -45.270 1.00121.53 A C ANISOU 3013 CA SER E 2 17906 13781 14490 -1210 4713 -1565 A C ATOM 3014 C SER E 2 27.574 -10.416 -45.557 1.00113.63 A C ANISOU 3014 C SER E 2 16785 13006 13385 -1401 4473 -2019 A C ATOM 3015 O SER E 2 28.248 -9.630 -46.228 1.00111.24 A O ANISOU 3015 O SER E 2 16749 12753 12765 -1528 4609 -2262 A O ATOM 3016 CB SER E 2 29.103 -11.774 -44.131 1.00113.39 A C ANISOU 3016 CB SER E 2 17094 12674 13313 -1426 4828 -1673 A C ATOM 3017 OG SER E 2 29.753 -10.517 -44.103 1.00111.96 A O ANISOU 3017 OG SER E 2 17132 12639 12769 -1786 4857 -2101 A O ATOM 3018 N THR E 3 26.404 -10.106 -45.008 1.00117.26 A N ANISOU 3018 N THR E 3 16833 13604 14118 -1399 4083 -2177 A N ATOM 3019 CA THR E 3 25.717 -8.850 -45.256 1.00103.55 A C ANISOU 3019 CA THR E 3 14889 12086 12369 -1478 3729 -2677 A C ATOM 3020 C THR E 3 24.778 -8.574 -44.091 1.00106.39 A C ANISOU 3020 C THR E 3 14775 12634 13015 -1507 3337 -2972 A C ATOM 3021 O THR E 3 24.555 -9.430 -43.231 1.00 78.81 A O ANISOU 3021 O THR E 3 11137 9062 9744 -1458 3344 -2694 A O ATOM 3022 CB THR E 3 24.962 -8.897 -46.585 1.00109.64 A C ANISOU 3022 CB THR E 3 15716 12723 13221 -1276 3504 -2493 A C ATOM 3023 CG2 THR E 3 25.868 -8.517 -47.754 1.00102.02 A C ANISOU 3023 CG2 THR E 3 15146 11732 11884 -1335 3815 -2516 A C ATOM 3024 OG1 THR E 3 24.427 -10.215 -46.772 1.00114.54 A O ANISOU 3024 OG1 THR E 3 16310 13139 14070 -1095 3499 -1903 A O ATOM 3025 N THR E 4 24.238 -7.356 -44.057 1.00115.61 A N ANISOU 3025 N THR E 4 15672 14079 14175 -1570 2979 -3595 A N ATOM 3026 CA THR E 4 23.311 -6.973 -42.997 1.00103.78 A C ANISOU 3026 CA THR E 4 13658 12829 12945 -1563 2554 -4023 A C ATOM 3027 C THR E 4 21.861 -7.143 -43.429 1.00107.91 A C ANISOU 3027 C THR E 4 13967 13142 13890 -1209 1938 -3949 A C ATOM 3028 O THR E 4 21.133 -7.975 -42.878 1.00114.09 A O ANISOU 3028 O THR E 4 14577 13766 15006 -1067 1738 -3632 A O ATOM 3029 CB THR E 4 23.539 -5.522 -42.568 1.00102.66 A C ANISOU 3029 CB THR E 4 13250 13211 12544 -1838 2463 -4890 A C ATOM 3030 CG2 THR E 4 24.812 -5.392 -41.756 1.00105.74 A C ANISOU 3030 CG2 THR E 4 13759 13842 12573 -2270 2862 -4768 A C ATOM 3031 OG1 THR E 4 23.610 -4.683 -43.728 1.00 95.82 A O ANISOU 3031 OG1 THR E 4 12518 12364 11527 -1753 2329 -5069 A O ATOM 3032 N GLY E 5 21.440 -6.358 -44.418 1.00 95.89 A N ANISOU 3032 N GLY E 5 12498 11590 12347 -1087 1588 -4231 A N ATOM 3033 CA GLY E 5 20.051 -6.307 -44.830 1.00 91.55 A C ANISOU 3033 CA GLY E 5 11811 10806 12167 -791 844 -4260 A C ATOM 3034 C GLY E 5 19.474 -7.587 -45.400 1.00 93.27 A C ANISOU 3034 C GLY E 5 12292 10572 12575 -674 753 -3424 A C ATOM 3035 O GLY E 5 18.332 -7.595 -45.865 1.00 97.69 A O ANISOU 3035 O GLY E 5 12865 10864 13389 -502 82 -3351 A O ATOM 3036 N GLN E 6 20.236 -8.672 -45.372 1.00 88.65 A N ANISOU 3036 N GLN E 6 11921 9909 11852 -784 1369 -2819 A N ATOM 3037 CA GLN E 6 19.767 -9.944 -45.886 1.00 90.99 A C ANISOU 3037 CA GLN E 6 12401 9909 12262 -735 1363 -2070 A C ATOM 3038 C GLN E 6 19.345 -10.849 -44.736 1.00 86.54 A C ANISOU 3038 C GLN E 6 11563 9323 11995 -684 1339 -1823 A C ATOM 3039 O GLN E 6 19.288 -10.438 -43.573 1.00 73.24 A O ANISOU 3039 O GLN E 6 9546 7828 10454 -676 1249 -2244 A O ATOM 3040 CB GLN E 6 20.852 -10.610 -46.729 1.00 84.06 A C ANISOU 3040 CB GLN E 6 11889 9010 11038 -838 2029 -1628 A C ATOM 3041 CG GLN E 6 21.697 -9.647 -47.548 1.00 94.31 A C ANISOU 3041 CG GLN E 6 13438 10412 11985 -922 2253 -1963 A C ATOM 3042 CD GLN E 6 20.896 -8.796 -48.495 1.00108.94 A C ANISOU 3042 CD GLN E 6 15382 12165 13847 -886 1681 -2181 A C ATOM 3043 NE2 GLN E 6 21.045 -7.477 -48.392 1.00107.69 A N ANISOU 3043 NE2 GLN E 6 15115 12185 13618 -881 1495 -2863 A N ATOM 3044 OE1 GLN E 6 20.157 -9.320 -49.323 1.00109.22 A O ANISOU 3044 OE1 GLN E 6 15596 11979 13924 -898 1385 -1752 A O ATOM 3045 N ILE E 7 19.068 -12.107 -45.064 1.00 77.89 A N ANISOU 3045 N ILE E 7 10587 8049 10958 -687 1443 -1153 A N ATOM 3046 CA ILE E 7 18.728 -13.098 -44.055 1.00 80.92 A C ANISOU 3046 CA ILE E 7 10735 8409 11603 -644 1473 -854 A C ATOM 3047 C ILE E 7 20.005 -13.654 -43.432 1.00 68.31 A C ANISOU 3047 C ILE E 7 9159 6947 9848 -682 2174 -757 A C ATOM 3048 O ILE E 7 21.105 -13.531 -43.978 1.00 80.52 A O ANISOU 3048 O ILE E 7 10966 8548 11078 -737 2635 -780 A O ATOM 3049 CB ILE E 7 17.865 -14.213 -44.670 1.00 70.87 A C ANISOU 3049 CB ILE E 7 9564 6942 10420 -683 1262 -206 A C ATOM 3050 CG1 ILE E 7 16.997 -13.639 -45.793 1.00 80.88 A C ANISOU 3050 CG1 ILE E 7 11069 8016 11645 -745 658 -207 A C ATOM 3051 CG2 ILE E 7 16.991 -14.869 -43.614 1.00 80.53 A C ANISOU 3051 CG2 ILE E 7 10492 8093 12014 -617 950 -39 A C ATOM 3052 CD1 ILE E 7 16.090 -14.652 -46.448 1.00 76.05 A C ANISOU 3052 CD1 ILE E 7 10627 7232 11038 -924 370 442 A C ATOM 3053 N ILE E 8 19.858 -14.267 -42.260 1.00 76.93 A N ANISOU 3053 N ILE E 8 10003 8058 11168 -647 2198 -657 A N ATOM 3054 CA ILE E 8 20.979 -14.861 -41.541 1.00 76.32 A C ANISOU 3054 CA ILE E 8 9978 8035 10986 -676 2731 -547 A C ATOM 3055 C ILE E 8 20.651 -16.318 -41.256 1.00 76.32 A C ANISOU 3055 C ILE E 8 9870 7939 11190 -569 2819 1 A C ATOM 3056 O ILE E 8 19.591 -16.621 -40.705 1.00 88.15 A O ANISOU 3056 O ILE E 8 11104 9396 12993 -533 2441 111 A O ATOM 3057 CB ILE E 8 21.284 -14.110 -40.231 1.00 70.74 A C ANISOU 3057 CB ILE E 8 9081 7504 10295 -811 2697 -1030 A C ATOM 3058 CG1 ILE E 8 22.121 -12.863 -40.518 1.00 64.32 A C ANISOU 3058 CG1 ILE E 8 8445 6863 9130 -998 2842 -1537 A C ATOM 3059 CG2 ILE E 8 22.007 -15.019 -39.246 1.00 76.25 A C ANISOU 3059 CG2 ILE E 8 9802 8156 11012 -841 3030 -775 A C ATOM 3060 CD1 ILE E 8 22.548 -12.121 -39.273 1.00 64.03 A C ANISOU 3060 CD1 ILE E 8 8243 7103 8980 -1271 2867 -2025 A C ATOM 3061 N ARG E 9 21.551 -17.217 -41.625 1.00 82.04 A N ANISOU 3061 N ARG E 9 10778 8645 11750 -504 3288 300 A N ATOM 3062 CA ARG E 9 21.358 -18.641 -41.388 1.00 89.15 A C ANISOU 3062 CA ARG E 9 11534 9530 12808 -391 3417 754 A C ATOM 3063 C ARG E 9 22.197 -19.030 -40.176 1.00 82.79 A C ANISOU 3063 C ARG E 9 10709 8675 12072 -325 3639 702 A C ATOM 3064 O ARG E 9 23.415 -18.820 -40.175 1.00 92.21 A O ANISOU 3064 O ARG E 9 12178 9818 13041 -321 3932 538 A O ATOM 3065 CB ARG E 9 21.753 -19.447 -42.625 1.00 94.22 A C ANISOU 3065 CB ARG E 9 12324 10258 13219 -339 3745 1039 A C ATOM 3066 CG ARG E 9 20.985 -20.736 -42.799 1.00108.23 A C ANISOU 3066 CG ARG E 9 13872 12141 15111 -336 3714 1489 A C ATOM 3067 CD ARG E 9 20.626 -21.024 -44.244 1.00119.07 A C ANISOU 3067 CD ARG E 9 15341 13682 16218 -498 3751 1716 A C ATOM 3068 NE ARG E 9 20.674 -22.460 -44.495 1.00118.23 A N ANISOU 3068 NE ARG E 9 15040 13835 16047 -479 4039 2033 A N ATOM 3069 CZ ARG E 9 20.987 -23.020 -45.656 1.00133.69 A C ANISOU 3069 CZ ARG E 9 17032 16090 17674 -568 4343 2131 A C ATOM 3070 NH1 ARG E 9 21.246 -22.292 -46.730 1.00133.93 A N1+ ANISOU 3070 NH1 ARG E 9 17328 16148 17410 -694 4390 2004 A N1+ ATOM 3071 NH2 ARG E 9 21.052 -24.347 -45.738 1.00135.36 A N ANISOU 3071 NH2 ARG E 9 16970 16628 17831 -538 4611 2320 A N ATOM 3072 N CYS E 10 21.554 -19.577 -39.142 1.00 79.62 A N ANISOU 3072 N CYS E 10 11952 8319 9982 -295 4774 -768 A N ATOM 3073 CA CYS E 10 22.257 -19.781 -37.879 1.00 77.94 A C ANISOU 3073 CA CYS E 10 11601 7979 10032 -155 4629 -814 A C ATOM 3074 C CYS E 10 21.564 -20.849 -37.043 1.00 86.58 A C ANISOU 3074 C CYS E 10 12433 9057 11407 -92 4651 -770 A C ATOM 3075 O CYS E 10 20.430 -21.247 -37.314 1.00102.06 A O ANISOU 3075 O CYS E 10 14324 11088 13367 -175 4731 -675 A O ATOM 3076 CB CYS E 10 22.358 -18.469 -37.094 1.00 76.92 A C ANISOU 3076 CB CYS E 10 11562 7820 9846 -165 4345 -706 A C ATOM 3077 SG CYS E 10 20.892 -18.077 -36.110 1.00 79.14 A S ANISOU 3077 SG CYS E 10 11729 8151 10189 -185 4153 -499 A S ATOM 3078 N LYS E 11 22.262 -21.289 -35.997 1.00 70.12 A N ANISOU 3078 N LYS E 11 10205 6869 9568 49 4558 -832 A N ATOM 3079 CA LYS E 11 21.746 -22.306 -35.090 1.00 78.86 A C ANISOU 3079 CA LYS E 11 11052 7954 10959 127 4546 -810 A C ATOM 3080 C LYS E 11 20.767 -21.705 -34.087 1.00 80.29 A C ANISOU 3080 C LYS E 11 11188 8146 11173 107 4310 -647 A C ATOM 3081 O LYS E 11 20.917 -20.562 -33.646 1.00 88.58 A O ANISOU 3081 O LYS E 11 12358 9196 12104 103 4115 -576 A O ATOM 3082 CB LYS E 11 22.890 -22.986 -34.333 1.00 76.91 A C ANISOU 3082 CB LYS E 11 10675 7594 10953 299 4514 -934 A C ATOM 3083 CG LYS E 11 23.746 -23.915 -35.176 1.00 78.32 A C ANISOU 3083 CG LYS E 11 10824 7755 11178 367 4757 -1127 A C ATOM 3084 CD LYS E 11 25.041 -24.267 -34.456 1.00 96.74 A C ANISOU 3084 CD LYS E 11 13098 9940 13719 545 4668 -1244 A C ATOM 3085 CE LYS E 11 25.484 -25.689 -34.764 1.00 94.31 A C ANISOU 3085 CE LYS E 11 12598 9624 13610 672 4882 -1421 A C ATOM 3086 NZ LYS E 11 25.515 -26.545 -33.545 1.00 89.69 A N1+ ANISOU 3086 NZ LYS E 11 11755 8976 13347 812 4772 -1408 A N1+ ATOM 3087 N ALA E 12 19.763 -22.498 -33.720 1.00 73.68 A N ANISOU 3087 N ALA E 12 10166 7324 10504 98 4328 -598 A N ATOM 3088 CA ALA E 12 18.784 -22.090 -32.722 1.00 76.09 A C ANISOU 3088 CA ALA E 12 10408 7631 10872 104 4102 -479 A C ATOM 3089 C ALA E 12 18.231 -23.328 -32.032 1.00 77.78 A C ANISOU 3089 C ALA E 12 10359 7815 11379 156 4109 -498 A C ATOM 3090 O ALA E 12 18.009 -24.355 -32.675 1.00 66.47 A O ANISOU 3090 O ALA E 12 8815 6397 10042 105 4318 -538 A O ATOM 3091 CB ALA E 12 17.646 -21.278 -33.348 1.00 71.84 A C ANISOU 3091 CB ALA E 12 10018 7149 10128 -36 4069 -350 A C ATOM 3092 N ALA E 13 18.006 -23.223 -30.725 1.00 62.58 A N ANISOU 3092 N ALA E 13 8325 5863 9588 256 3880 -471 A N ATOM 3093 CA ALA E 13 17.446 -24.322 -29.941 1.00 77.35 A C ANISOU 3093 CA ALA E 13 9944 7705 11740 310 3837 -494 A C ATOM 3094 C ALA E 13 15.928 -24.274 -30.068 1.00 78.65 A C ANISOU 3094 C ALA E 13 10099 7874 11911 192 3784 -398 A C ATOM 3095 O ALA E 13 15.257 -23.522 -29.357 1.00 75.74 A O ANISOU 3095 O ALA E 13 9775 7507 11498 218 3559 -338 A O ATOM 3096 CB ALA E 13 17.896 -24.230 -28.487 1.00 74.93 A C ANISOU 3096 CB ALA E 13 9538 7379 11553 474 3604 -514 A C ATOM 3097 N VAL E 14 15.381 -25.080 -30.975 1.00 68.34 A N ANISOU 3097 N VAL E 14 8731 6571 10661 64 3989 -382 A N ATOM 3098 CA VAL E 14 13.954 -25.066 -31.271 1.00 70.82 A C ANISOU 3098 CA VAL E 14 9057 6864 10985 -79 3953 -268 A C ATOM 3099 C VAL E 14 13.241 -26.048 -30.352 1.00 68.62 A C ANISOU 3099 C VAL E 14 8528 6527 11019 -53 3842 -288 A C ATOM 3100 O VAL E 14 13.704 -27.180 -30.150 1.00 81.24 A O ANISOU 3100 O VAL E 14 9909 8129 12829 -6 3947 -372 A O ATOM 3101 CB VAL E 14 13.698 -25.409 -32.749 1.00 76.28 A C ANISOU 3101 CB VAL E 14 9818 7604 11563 -257 4230 -209 A C ATOM 3102 CG1 VAL E 14 12.215 -25.659 -32.999 1.00 72.65 A C ANISOU 3102 CG1 VAL E 14 9328 7096 11179 -420 4198 -73 A C ATOM 3103 CG2 VAL E 14 14.217 -24.299 -33.649 1.00 75.25 A C ANISOU 3103 CG2 VAL E 14 9961 7532 11097 -293 4293 -184 A C ATOM 3104 N ALA E 15 12.123 -25.604 -29.778 1.00 69.00 A N ANISOU 3104 N ALA E 15 8600 6516 11101 -71 3614 -223 A N ATOM 3105 CA ALA E 15 11.194 -26.477 -29.070 1.00 72.94 A C ANISOU 3105 CA ALA E 15 8889 6938 11885 -88 3491 -232 A C ATOM 3106 C ALA E 15 10.107 -26.895 -30.052 1.00 73.34 A C ANISOU 3106 C ALA E 15 8950 6940 11978 -312 3614 -111 A C ATOM 3107 O ALA E 15 9.302 -26.064 -30.486 1.00 91.99 A O ANISOU 3107 O ALA E 15 11503 9259 14191 -399 3536 -1 A O ATOM 3108 CB ALA E 15 10.593 -25.770 -27.859 1.00 65.01 A C ANISOU 3108 CB ALA E 15 7911 5893 10898 32 3157 -252 A C ATOM 3109 N TRP E 16 10.085 -28.176 -30.411 1.00 74.06 A N ANISOU 3109 N TRP E 16 8827 7041 12271 -407 3804 -118 A N ATOM 3110 CA TRP E 16 9.101 -28.666 -31.367 1.00 77.65 A C ANISOU 3110 CA TRP E 16 9267 7465 12770 -644 3945 23 A C ATOM 3111 C TRP E 16 7.813 -29.121 -30.693 1.00 85.40 A C ANISOU 3111 C TRP E 16 10120 8303 14024 -722 3724 68 A C ATOM 3112 O TRP E 16 6.725 -28.923 -31.244 1.00 87.82 A O ANISOU 3112 O TRP E 16 10529 8522 14318 -898 3692 217 A O ATOM 3113 CB TRP E 16 9.691 -29.814 -32.191 1.00 75.47 A C ANISOU 3113 CB TRP E 16 8813 7302 12559 -727 4286 3 A C ATOM 3114 CG TRP E 16 10.648 -29.364 -33.254 1.00 85.61 A C ANISOU 3114 CG TRP E 16 10271 8714 13544 -719 4535 -10 A C ATOM 3115 CD1 TRP E 16 12.010 -29.397 -33.196 1.00 86.03 A C ANISOU 3115 CD1 TRP E 16 10311 8844 13530 -552 4639 -161 A C ATOM 3116 CD2 TRP E 16 10.314 -28.814 -34.534 1.00 82.15 A C ANISOU 3116 CD2 TRP E 16 10053 8330 12831 -884 4693 126 A C ATOM 3117 CE2 TRP E 16 11.525 -28.537 -35.199 1.00 81.38 A C ANISOU 3117 CE2 TRP E 16 10064 8353 12502 -804 4890 31 A C ATOM 3118 CE3 TRP E 16 9.108 -28.529 -35.183 1.00 77.26 A C ANISOU 3118 CE3 TRP E 16 9556 7661 12140 -1090 4674 324 A C ATOM 3119 NE1 TRP E 16 12.546 -28.902 -34.361 1.00 84.07 A N ANISOU 3119 NE1 TRP E 16 10263 8693 12988 -602 4850 -146 A N ATOM 3120 CZ2 TRP E 16 11.566 -27.989 -36.479 1.00 76.80 A C ANISOU 3120 CZ2 TRP E 16 9707 7866 11607 -920 5070 113 A C ATOM 3121 CZ3 TRP E 16 9.151 -27.984 -36.455 1.00 80.19 A C ANISOU 3121 CZ3 TRP E 16 10148 8126 12196 -1206 4855 429 A C ATOM 3122 CH2 TRP E 16 10.372 -27.721 -37.089 1.00 77.76 A C ANISOU 3122 CH2 TRP E 16 9940 7959 11646 -1120 5052 317 A C ATOM 3123 N GLU E 17 7.912 -29.730 -29.513 1.00 85.43 A N ANISOU 3123 N GLU E 17 9909 8273 14277 -595 3558 -57 A N ATOM 3124 CA GLU E 17 6.747 -30.237 -28.806 1.00 86.36 A C ANISOU 3124 CA GLU E 17 9889 8250 14676 -659 3329 -48 A C ATOM 3125 C GLU E 17 6.853 -29.876 -27.332 1.00 76.78 A C ANISOU 3125 C GLU E 17 8642 7003 13526 -429 3009 -196 A C ATOM 3126 O GLU E 17 7.950 -29.689 -26.798 1.00 87.69 A O ANISOU 3126 O GLU E 17 10007 8487 14824 -237 3011 -302 A O ATOM 3127 CB GLU E 17 6.606 -31.756 -28.976 1.00 85.75 A C ANISOU 3127 CB GLU E 17 9497 8185 14900 -796 3485 -43 A C ATOM 3128 CG GLU E 17 6.338 -32.189 -30.410 1.00108.01 A C ANISOU 3128 CG GLU E 17 12322 11057 17661 -1049 3801 122 A C ATOM 3129 CD GLU E 17 6.392 -33.692 -30.589 1.00132.13 A C ANISOU 3129 CD GLU E 17 15032 14180 20991 -1165 3995 116 A C ATOM 3130 OE1 GLU E 17 6.504 -34.148 -31.746 1.00139.88 A O ANISOU 3130 OE1 GLU E 17 15975 15278 21895 -1331 4316 219 A O ATOM 3131 OE2 GLU E 17 6.324 -34.416 -29.574 1.00136.22 A O1- ANISOU 3131 OE2 GLU E 17 15308 14654 21796 -1089 3828 4 A O1- ATOM 3132 N ALA E 18 5.695 -29.779 -26.682 1.00 86.32 A N ANISOU 3132 N ALA E 18 9848 8067 14882 -449 2728 -199 A N ATOM 3133 CA ALA E 18 5.651 -29.395 -25.279 1.00 86.27 A C ANISOU 3133 CA ALA E 18 9821 8046 14912 -229 2410 -346 A C ATOM 3134 C ALA E 18 6.352 -30.431 -24.408 1.00 77.78 A C ANISOU 3134 C ALA E 18 8466 7039 14048 -113 2391 -479 A C ATOM 3135 O ALA E 18 6.268 -31.637 -24.655 1.00 83.09 A O ANISOU 3135 O ALA E 18 8908 7696 14968 -237 2513 -471 A O ATOM 3136 CB ALA E 18 4.201 -29.224 -24.828 1.00 73.18 A C ANISOU 3136 CB ALA E 18 8202 6204 13399 -280 2115 -345 A C ATOM 3137 N GLY E 19 7.063 -29.947 -23.391 1.00 79.41 A N ANISOU 3137 N GLY E 19 8689 7336 14149 124 2237 -593 A N ATOM 3138 CA GLY E 19 7.693 -30.808 -22.408 1.00 95.55 A C ANISOU 3138 CA GLY E 19 10491 9442 16373 266 2158 -717 A C ATOM 3139 C GLY E 19 8.779 -31.722 -22.940 1.00 92.33 A C ANISOU 3139 C GLY E 19 9917 9119 16047 249 2442 -716 A C ATOM 3140 O GLY E 19 9.318 -32.548 -22.197 1.00 92.61 A O ANISOU 3140 O GLY E 19 9730 9198 16260 363 2386 -812 A O ATOM 3141 N LYS E 20 9.118 -31.584 -24.219 1.00 88.82 A N ANISOU 3141 N LYS E 20 9577 8702 15467 121 2739 -618 A N ATOM 3142 CA LYS E 20 10.131 -32.434 -24.819 1.00 88.20 A C ANISOU 3142 CA LYS E 20 9349 8710 15453 117 3024 -637 A C ATOM 3143 C LYS E 20 11.432 -31.659 -25.010 1.00 92.85 A C ANISOU 3143 C LYS E 20 10114 9385 15780 262 3130 -656 A C ATOM 3144 O LYS E 20 11.414 -30.430 -25.127 1.00 89.41 A O ANISOU 3144 O LYS E 20 9939 8951 15081 281 3067 -605 A O ATOM 3145 CB LYS E 20 9.650 -32.986 -26.166 1.00 93.37 A C ANISOU 3145 CB LYS E 20 9966 9361 16148 -130 3309 -529 A C ATOM 3146 CG LYS E 20 8.560 -34.045 -26.043 1.00104.63 A C ANISOU 3146 CG LYS E 20 11150 10710 17895 -299 3250 -502 A C ATOM 3147 CD LYS E 20 8.843 -35.011 -24.900 1.00109.46 A C ANISOU 3147 CD LYS E 20 11464 11335 18791 -161 3090 -640 A C ATOM 3148 CE LYS E 20 7.596 -35.790 -24.510 1.00 97.71 A C ANISOU 3148 CE LYS E 20 9777 9735 17613 -316 2916 -627 A C ATOM 3149 NZ LYS E 20 7.670 -36.302 -23.113 1.00 97.60 A N1+ ANISOU 3149 NZ LYS E 20 9564 9711 17811 -146 2628 -776 A N1+ ATOM 3150 N PRO E 21 12.577 -32.347 -25.036 1.00 76.13 A N ANISOU 3150 N PRO E 21 7855 7331 13738 366 3277 -730 A N ATOM 3151 CA PRO E 21 13.862 -31.640 -25.105 1.00 98.85 A C ANISOU 3151 CA PRO E 21 10900 10258 16402 510 3337 -756 A C ATOM 3152 C PRO E 21 13.972 -30.756 -26.339 1.00 91.93 A C ANISOU 3152 C PRO E 21 10289 9400 15241 393 3534 -677 A C ATOM 3153 O PRO E 21 13.369 -31.022 -27.381 1.00 79.78 A O ANISOU 3153 O PRO E 21 8760 7866 13688 210 3726 -612 A O ATOM 3154 CB PRO E 21 14.892 -32.775 -25.148 1.00 77.83 A C ANISOU 3154 CB PRO E 21 8010 7632 13929 611 3492 -853 A C ATOM 3155 CG PRO E 21 14.202 -33.942 -24.542 1.00 87.00 A C ANISOU 3155 CG PRO E 21 8864 8780 15410 590 3396 -894 A C ATOM 3156 CD PRO E 21 12.755 -33.804 -24.903 1.00 82.61 A C ANISOU 3156 CD PRO E 21 8346 8175 14868 374 3362 -803 A C ATOM 3157 N LEU E 22 14.754 -29.687 -26.203 1.00 74.14 A N ANISOU 3157 N LEU E 22 8250 7166 12754 494 3476 -672 A N ATOM 3158 CA LEU E 22 15.042 -28.823 -27.334 1.00 76.25 A C ANISOU 3158 CA LEU E 22 8769 7459 12744 404 3646 -616 A C ATOM 3159 C LEU E 22 15.925 -29.552 -28.341 1.00 79.48 A C ANISOU 3159 C LEU E 22 9123 7903 13170 387 3952 -680 A C ATOM 3160 O LEU E 22 16.645 -30.498 -28.009 1.00 88.16 A O ANISOU 3160 O LEU E 22 10023 9006 14469 503 4004 -779 A O ATOM 3161 CB LEU E 22 15.738 -27.539 -26.877 1.00 77.56 A C ANISOU 3161 CB LEU E 22 9149 7640 12680 512 3496 -599 A C ATOM 3162 CG LEU E 22 15.064 -26.677 -25.809 1.00 77.07 A C ANISOU 3162 CG LEU E 22 9145 7584 12553 571 3196 -555 A C ATOM 3163 CD1 LEU E 22 15.762 -25.330 -25.699 1.00 61.60 A C ANISOU 3163 CD1 LEU E 22 7407 5674 10324 629 3119 -514 A C ATOM 3164 CD2 LEU E 22 13.589 -26.494 -26.107 1.00 67.66 A C ANISOU 3164 CD2 LEU E 22 7991 6357 11359 434 3141 -489 A C ATOM 3165 N VAL E 23 15.866 -29.099 -29.590 1.00 78.56 A N ANISOU 3165 N VAL E 23 9189 7825 12837 254 4152 -630 A N ATOM 3166 CA VAL E 23 16.687 -29.661 -30.655 1.00 85.03 A C ANISOU 3166 CA VAL E 23 9990 8701 13615 243 4453 -707 A C ATOM 3167 C VAL E 23 17.415 -28.517 -31.346 1.00 88.65 A C ANISOU 3167 C VAL E 23 10748 9173 13762 243 4502 -706 A C ATOM 3168 O VAL E 23 16.798 -27.506 -31.698 1.00 85.84 A O ANISOU 3168 O VAL E 23 10601 8824 13189 134 4437 -598 A O ATOM 3169 CB VAL E 23 15.847 -30.473 -31.661 1.00 87.40 A C ANISOU 3169 CB VAL E 23 10179 9070 13960 54 4695 -652 A C ATOM 3170 CG1 VAL E 23 16.542 -30.547 -33.009 1.00 87.70 A C ANISOU 3170 CG1 VAL E 23 10315 9204 13802 13 5007 -705 A C ATOM 3171 CG2 VAL E 23 15.585 -31.870 -31.118 1.00 85.29 A C ANISOU 3171 CG2 VAL E 23 9560 8809 14038 78 4714 -703 A C ATOM 3172 N ILE E 24 18.727 -28.665 -31.512 1.00 83.27 A N ANISOU 3172 N ILE E 24 10085 8483 13069 370 4595 -831 A N ATOM 3173 CA ILE E 24 19.530 -27.647 -32.182 1.00 87.13 A C ANISOU 3173 CA ILE E 24 10850 8970 13285 369 4634 -852 A C ATOM 3174 C ILE E 24 19.240 -27.725 -33.677 1.00 80.60 A C ANISOU 3174 C ILE E 24 10122 8240 12263 217 4910 -847 A C ATOM 3175 O ILE E 24 19.676 -28.657 -34.357 1.00 79.71 A O ANISOU 3175 O ILE E 24 9893 8185 12208 239 5157 -958 A O ATOM 3176 CB ILE E 24 21.025 -27.825 -31.895 1.00 90.32 A C ANISOU 3176 CB ILE E 24 11249 9305 13763 551 4629 -993 A C ATOM 3177 CG1 ILE E 24 21.253 -28.055 -30.400 1.00 99.05 A C ANISOU 3177 CG1 ILE E 24 12201 10336 15097 702 4381 -985 A C ATOM 3178 CG2 ILE E 24 21.807 -26.616 -32.386 1.00 78.74 A C ANISOU 3178 CG2 ILE E 24 10078 7808 12030 536 4597 -1000 A C ATOM 3179 CD1 ILE E 24 21.032 -26.821 -29.552 1.00 83.77 A C ANISOU 3179 CD1 ILE E 24 10416 8380 13032 696 4106 -864 A C ATOM 3180 N GLU E 25 18.499 -26.750 -34.188 1.00 87.96 A N ANISOU 3180 N GLU E 25 11262 9203 12956 71 4869 -719 A N ATOM 3181 CA GLU E 25 18.118 -26.694 -35.586 1.00 85.65 A C ANISOU 3181 CA GLU E 25 11091 9012 12439 -88 5101 -679 A C ATOM 3182 C GLU E 25 18.823 -25.538 -36.280 1.00 88.92 A C ANISOU 3182 C GLU E 25 11802 9440 12542 -98 5097 -707 A C ATOM 3183 O GLU E 25 19.406 -24.651 -35.649 1.00 88.39 A O ANISOU 3183 O GLU E 25 11851 9300 12432 -17 4891 -719 A O ATOM 3184 CB GLU E 25 16.600 -26.555 -35.726 1.00 89.48 A C ANISOU 3184 CB GLU E 25 11581 9516 12901 -264 5051 -491 A C ATOM 3185 CG GLU E 25 15.827 -27.810 -35.370 1.00 85.37 A C ANISOU 3185 CG GLU E 25 10769 8995 12671 -309 5108 -459 A C ATOM 3186 CD GLU E 25 15.876 -28.851 -36.471 1.00 99.50 A C ANISOU 3186 CD GLU E 25 12439 10916 14452 -400 5451 -490 A C ATOM 3187 OE1 GLU E 25 15.875 -28.463 -37.659 1.00112.76 A O ANISOU 3187 OE1 GLU E 25 14300 12692 15849 -509 5626 -451 A O ATOM 3188 OE2 GLU E 25 15.920 -30.057 -36.152 1.00113.56 A O1- ANISOU 3188 OE2 GLU E 25 13932 12718 16498 -360 5547 -554 A O1- ATOM 3189 N GLU E 26 18.747 -25.564 -37.603 1.00 90.65 A N ANISOU 3189 N GLU E 26 12137 9770 12538 -211 5327 -711 A N ATOM 3190 CA GLU E 26 19.406 -24.593 -38.467 1.00 80.21 A C ANISOU 3190 CA GLU E 26 11092 8481 10903 -236 5355 -758 A C ATOM 3191 C GLU E 26 18.312 -23.712 -39.063 1.00 89.42 A C ANISOU 3191 C GLU E 26 12442 9708 11826 -414 5301 -568 A C ATOM 3192 O GLU E 26 17.613 -24.123 -39.994 1.00 92.63 A O ANISOU 3192 O GLU E 26 12852 10222 12122 -550 5493 -489 A O ATOM 3193 CB GLU E 26 20.213 -25.323 -39.533 1.00 93.84 A C ANISOU 3193 CB GLU E 26 12813 10302 12541 -205 5655 -933 A C ATOM 3194 CG GLU E 26 21.484 -24.631 -39.954 1.00105.94 A C ANISOU 3194 CG GLU E 26 14559 11796 13896 -124 5637 -1095 A C ATOM 3195 CD GLU E 26 21.269 -23.633 -41.062 1.00117.10 A C ANISOU 3195 CD GLU E 26 16255 13304 14935 -264 5666 -1038 A C ATOM 3196 OE1 GLU E 26 20.118 -23.475 -41.523 1.00119.42 A O ANISOU 3196 OE1 GLU E 26 16583 13694 15098 -421 5703 -860 A O ATOM 3197 OE2 GLU E 26 22.273 -23.035 -41.495 1.00116.64 A O1- ANISOU 3197 OE2 GLU E 26 16383 13217 14717 -218 5644 -1176 A O1- ATOM 3198 N VAL E 27 18.160 -22.507 -38.523 1.00 92.97 A N ANISOU 3198 N VAL E 27 13036 10096 12193 -411 5038 -484 A N ATOM 3199 CA VAL E 27 17.022 -21.656 -38.827 1.00 86.36 A C ANISOU 3199 CA VAL E 27 12341 9289 11184 -544 4926 -296 A C ATOM 3200 C VAL E 27 17.490 -20.407 -39.572 1.00 87.35 A C ANISOU 3200 C VAL E 27 12743 9463 10981 -587 4874 -299 A C ATOM 3201 O VAL E 27 18.681 -20.084 -39.626 1.00 85.36 A O ANISOU 3201 O VAL E 27 12572 9195 10667 -511 4870 -440 A O ATOM 3202 CB VAL E 27 16.237 -21.274 -37.556 1.00 75.24 A C ANISOU 3202 CB VAL E 27 10846 7790 9953 -500 4646 -192 A C ATOM 3203 CG1 VAL E 27 16.054 -22.487 -36.657 1.00 79.42 A C ANISOU 3203 CG1 VAL E 27 11095 8259 10823 -427 4661 -234 A C ATOM 3204 CG2 VAL E 27 16.943 -20.151 -36.809 1.00 69.07 A C ANISOU 3204 CG2 VAL E 27 10161 6972 9110 -397 4415 -226 A C ATOM 3205 N GLU E 28 16.522 -19.704 -40.156 1.00 84.00 A N ANISOU 3205 N GLU E 28 12467 9091 10359 -714 4817 -137 A N ATOM 3206 CA GLU E 28 16.737 -18.444 -40.851 1.00 85.61 A C ANISOU 3206 CA GLU E 28 12925 9353 10248 -768 4732 -108 A C ATOM 3207 C GLU E 28 16.172 -17.302 -40.017 1.00 78.63 A C ANISOU 3207 C GLU E 28 12084 8421 9371 -741 4425 8 A C ATOM 3208 O GLU E 28 15.097 -17.426 -39.423 1.00 82.75 A O ANISOU 3208 O GLU E 28 12510 8894 10038 -745 4314 127 A O ATOM 3209 CB GLU E 28 16.076 -18.457 -42.233 1.00 74.33 A C ANISOU 3209 CB GLU E 28 11644 8042 8556 -926 4896 -4 A C ATOM 3210 CG GLU E 28 16.970 -18.963 -43.355 1.00 88.61 A C ANISOU 3210 CG GLU E 28 13525 9960 10182 -946 5168 -155 A C ATOM 3211 CD GLU E 28 16.190 -19.667 -44.449 1.00101.86 A C ANISOU 3211 CD GLU E 28 15213 11769 11720 -1090 5412 -47 A C ATOM 3212 OE1 GLU E 28 15.445 -18.986 -45.186 1.00109.02 A O ANISOU 3212 OE1 GLU E 28 16298 12743 12380 -1214 5365 118 A O ATOM 3213 OE2 GLU E 28 16.319 -20.903 -44.572 1.00118.45 A O1- ANISOU 3213 OE2 GLU E 28 17134 13914 13957 -1080 5649 -116 A O1- ATOM 3214 N VAL E 29 16.900 -16.190 -39.986 1.00 78.19 A N ANISOU 3214 N VAL E 29 12166 8385 9159 -713 4285 -34 A N ATOM 3215 CA VAL E 29 16.557 -15.015 -39.196 1.00 79.80 A C ANISOU 3215 CA VAL E 29 12395 8581 9345 -672 4004 54 A C ATOM 3216 C VAL E 29 16.467 -13.833 -40.147 1.00 77.64 A C ANISOU 3216 C VAL E 29 12350 8398 8750 -765 3935 118 A C ATOM 3217 O VAL E 29 17.466 -13.459 -40.778 1.00 69.11 A O ANISOU 3217 O VAL E 29 11399 7357 7502 -793 3986 19 A O ATOM 3218 CB VAL E 29 17.591 -14.752 -38.089 1.00 69.40 A C ANISOU 3218 CB VAL E 29 10989 7216 8165 -552 3876 -41 A C ATOM 3219 CG1 VAL E 29 17.218 -13.512 -37.293 1.00 77.06 A C ANISOU 3219 CG1 VAL E 29 11967 8223 9089 -512 3604 55 A C ATOM 3220 CG2 VAL E 29 17.714 -15.964 -37.178 1.00 63.78 A C ANISOU 3220 CG2 VAL E 29 10052 6419 7763 -453 3937 -106 A C ATOM 3221 N ALA E 30 15.276 -13.250 -40.249 1.00 76.75 A N ANISOU 3221 N ALA E 30 12291 8310 8561 -806 3805 277 A N ATOM 3222 CA ALA E 30 15.042 -12.147 -41.161 1.00 75.29 A C ANISOU 3222 CA ALA E 30 12314 8216 8077 -888 3721 358 A C ATOM 3223 C ALA E 30 15.720 -10.874 -40.656 1.00 67.05 A C ANISOU 3223 C ALA E 30 11306 7218 6953 -836 3508 324 A C ATOM 3224 O ALA E 30 16.047 -10.759 -39.472 1.00 68.54 A O ANISOU 3224 O ALA E 30 11350 7371 7321 -734 3392 286 A O ATOM 3225 CB ALA E 30 13.541 -11.914 -41.328 1.00 74.10 A C ANISOU 3225 CB ALA E 30 12197 8055 7903 -928 3618 545 A C ATOM 3226 N PRO E 31 15.960 -9.912 -41.543 1.00 65.96 A N ANISOU 3226 N PRO E 31 11351 7172 6538 -913 3454 341 A N ATOM 3227 CA PRO E 31 16.474 -8.608 -41.107 1.00 67.68 A C ANISOU 3227 CA PRO E 31 11589 7452 6673 -886 3234 337 A C ATOM 3228 C PRO E 31 15.435 -7.863 -40.288 1.00 70.46 A C ANISOU 3228 C PRO E 31 11853 7833 7085 -807 3006 464 A C ATOM 3229 O PRO E 31 14.230 -8.130 -40.406 1.00 80.63 A O ANISOU 3229 O PRO E 31 13141 9089 8407 -800 2992 571 A O ATOM 3230 CB PRO E 31 16.773 -7.883 -42.430 1.00 74.66 A C ANISOU 3230 CB PRO E 31 12696 8434 7238 -1002 3239 333 A C ATOM 3231 CG PRO E 31 15.978 -8.609 -43.462 1.00 71.39 A C ANISOU 3231 CG PRO E 31 12380 8028 6715 -1076 3411 400 A C ATOM 3232 CD PRO E 31 15.934 -10.031 -43.010 1.00 65.81 A C ANISOU 3232 CD PRO E 31 11523 7222 6260 -1034 3606 349 A C ATOM 3233 N PRO E 32 15.859 -6.920 -39.449 1.00 70.69 A N ANISOU 3233 N PRO E 32 11804 7924 7129 -746 2821 457 A N ATOM 3234 CA PRO E 32 14.906 -6.243 -38.563 1.00 68.25 A C ANISOU 3234 CA PRO E 32 11385 7663 6882 -638 2611 549 A C ATOM 3235 C PRO E 32 14.053 -5.228 -39.308 1.00 75.75 A C ANISOU 3235 C PRO E 32 12461 8700 7620 -668 2469 661 A C ATOM 3236 O PRO E 32 14.500 -4.572 -40.252 1.00 80.19 A O ANISOU 3236 O PRO E 32 13172 9341 7957 -767 2460 665 A O ATOM 3237 CB PRO E 32 15.810 -5.560 -37.532 1.00 68.12 A C ANISOU 3237 CB PRO E 32 11244 7723 6915 -581 2490 506 A C ATOM 3238 CG PRO E 32 17.081 -5.313 -38.265 1.00 67.81 A C ANISOU 3238 CG PRO E 32 11325 7697 6743 -701 2560 435 A C ATOM 3239 CD PRO E 32 17.242 -6.455 -39.236 1.00 73.13 A C ANISOU 3239 CD PRO E 32 12114 8263 7411 -772 2795 365 A C ATOM 3240 N GLN E 33 12.806 -5.106 -38.863 1.00 76.91 A N ANISOU 3240 N GLN E 33 12549 8825 7847 -573 2341 745 A N ATOM 3241 CA GLN E 33 11.854 -4.173 -39.447 1.00 78.53 A C ANISOU 3241 CA GLN E 33 12859 9090 7889 -567 2176 859 A C ATOM 3242 C GLN E 33 11.942 -2.835 -38.710 1.00 83.23 A C ANISOU 3242 C GLN E 33 13350 9842 8431 -463 1946 860 A C ATOM 3243 O GLN E 33 12.918 -2.565 -38.005 1.00 73.49 A O ANISOU 3243 O GLN E 33 12004 8687 7231 -447 1939 787 A O ATOM 3244 CB GLN E 33 10.445 -4.772 -39.407 1.00 84.48 A C ANISOU 3244 CB GLN E 33 13615 9710 8774 -518 2148 948 A C ATOM 3245 CG GLN E 33 10.232 -5.946 -40.348 1.00 87.50 A C ANISOU 3245 CG GLN E 33 14110 9976 9161 -654 2371 992 A C ATOM 3246 CD GLN E 33 10.457 -5.578 -41.802 1.00 86.78 A C ANISOU 3246 CD GLN E 33 14235 9960 8776 -797 2439 1055 A C ATOM 3247 NE2 GLN E 33 10.965 -6.527 -42.580 1.00 86.56 A N ANISOU 3247 NE2 GLN E 33 14282 9910 8698 -921 2690 1023 A N ATOM 3248 OE1 GLN E 33 10.172 -4.457 -42.223 1.00 95.79 A O ANISOU 3248 OE1 GLN E 33 15470 11194 9731 -789 2264 1126 A O ATOM 3249 N LYS E 34 10.924 -1.988 -38.863 1.00 89.24 A N ANISOU 3249 N LYS E 34 14141 10654 9111 -390 1754 949 A N ATOM 3250 CA LYS E 34 10.914 -0.693 -38.195 1.00 74.63 A C ANISOU 3250 CA LYS E 34 12170 8982 7203 -276 1537 948 A C ATOM 3251 C LYS E 34 10.981 -0.868 -36.683 1.00 77.61 A C ANISOU 3251 C LYS E 34 12321 9389 7778 -127 1498 874 A C ATOM 3252 O LYS E 34 10.229 -1.657 -36.102 1.00 74.47 A O ANISOU 3252 O LYS E 34 11865 8863 7568 -32 1507 855 A O ATOM 3253 CB LYS E 34 9.658 0.092 -38.580 1.00 86.34 A C ANISOU 3253 CB LYS E 34 13716 10489 8603 -188 1335 1046 A C ATOM 3254 CG LYS E 34 9.907 1.566 -38.880 1.00 96.39 A C ANISOU 3254 CG LYS E 34 14981 11975 9665 -180 1159 1077 A C ATOM 3255 CD LYS E 34 8.665 2.411 -38.619 1.00 94.29 A C ANISOU 3255 CD LYS E 34 14666 11759 9401 5 913 1132 A C ATOM 3256 CE LYS E 34 8.919 3.882 -38.923 1.00 91.34 A C ANISOU 3256 CE LYS E 34 14259 11622 8824 17 736 1161 A C ATOM 3257 NZ LYS E 34 7.979 4.792 -38.211 1.00 99.58 A N1+ ANISOU 3257 NZ LYS E 34 15153 12777 9906 251 499 1161 A N1+ ATOM 3258 N HIS E 35 11.904 -0.138 -36.054 1.00 72.89 A N ANISOU 3258 N HIS E 35 11597 8965 7133 -118 1449 837 A N ATOM 3259 CA HIS E 35 12.119 -0.098 -34.610 1.00 67.63 A C ANISOU 3259 CA HIS E 35 10710 8391 6597 15 1400 783 A C ATOM 3260 C HIS E 35 12.616 -1.420 -34.039 1.00 69.89 A C ANISOU 3260 C HIS E 35 10948 8528 7079 0 1569 717 A C ATOM 3261 O HIS E 35 12.552 -1.619 -32.819 1.00 73.70 A O ANISOU 3261 O HIS E 35 11260 9054 7689 130 1528 674 A O ATOM 3262 CB HIS E 35 10.855 0.336 -33.860 1.00 64.93 A C ANISOU 3262 CB HIS E 35 10255 8107 6311 232 1216 780 A C ATOM 3263 CG HIS E 35 10.388 1.714 -34.212 1.00 83.83 A C ANISOU 3263 CG HIS E 35 12646 10676 8529 290 1026 833 A C ATOM 3264 CD2 HIS E 35 9.272 2.395 -33.858 1.00 89.25 A C ANISOU 3264 CD2 HIS E 35 13262 11435 9212 484 832 832 A C ATOM 3265 ND1 HIS E 35 11.101 2.553 -35.041 1.00 95.38 A N ANISOU 3265 ND1 HIS E 35 14181 12261 9799 148 1012 884 A N ATOM 3266 CE1 HIS E 35 10.449 3.693 -35.177 1.00 88.55 A C ANISOU 3266 CE1 HIS E 35 13278 11549 8818 249 819 923 A C ATOM 3267 NE2 HIS E 35 9.336 3.623 -34.470 1.00 96.14 A N ANISOU 3267 NE2 HIS E 35 14153 12482 9892 461 709 890 A N ATOM 3268 N GLU E 36 13.114 -2.326 -34.875 1.00 67.18 A N ANISOU 3268 N GLU E 36 10742 8027 6755 -143 1755 701 A N ATOM 3269 CA GLU E 36 13.676 -3.592 -34.431 1.00 81.83 A C ANISOU 3269 CA GLU E 36 12547 9747 8797 -158 1920 632 A C ATOM 3270 C GLU E 36 15.188 -3.588 -34.619 1.00 76.26 A C ANISOU 3270 C GLU E 36 11870 9057 8048 -281 2022 594 A C ATOM 3271 O GLU E 36 15.735 -2.832 -35.428 1.00 63.53 A O ANISOU 3271 O GLU E 36 10369 7512 6257 -395 2003 613 A O ATOM 3272 CB GLU E 36 13.060 -4.769 -35.199 1.00 70.14 A C ANISOU 3272 CB GLU E 36 11177 8072 7400 -214 2070 632 A C ATOM 3273 CG GLU E 36 11.565 -4.946 -34.988 1.00 68.32 A C ANISOU 3273 CG GLU E 36 10927 7770 7262 -110 1966 675 A C ATOM 3274 CD GLU E 36 10.971 -6.028 -35.871 1.00 78.69 A C ANISOU 3274 CD GLU E 36 12355 8905 8640 -208 2115 712 A C ATOM 3275 OE1 GLU E 36 11.701 -6.569 -36.730 1.00 73.04 A O ANISOU 3275 OE1 GLU E 36 11737 8153 7860 -346 2308 698 A O ATOM 3276 OE2 GLU E 36 9.774 -6.339 -35.705 1.00 80.62 A O1- ANISOU 3276 OE2 GLU E 36 12587 9046 9000 -147 2037 753 A O1- ATOM 3277 N VAL E 37 15.867 -4.438 -33.847 1.00 67.20 A N ANISOU 3277 N VAL E 37 10622 7835 7074 -252 2111 536 A N ATOM 3278 CA VAL E 37 17.304 -4.644 -33.981 1.00 74.35 A C ANISOU 3278 CA VAL E 37 11562 8698 7990 -354 2208 489 A C ATOM 3279 C VAL E 37 17.585 -6.141 -33.949 1.00 67.14 A C ANISOU 3279 C VAL E 37 10640 7600 7270 -344 2392 408 A C ATOM 3280 O VAL E 37 16.885 -6.915 -33.287 1.00 64.41 A O ANISOU 3280 O VAL E 37 10185 7200 7089 -240 2404 397 A O ATOM 3281 CB VAL E 37 18.123 -3.911 -32.884 1.00 72.48 A C ANISOU 3281 CB VAL E 37 11181 8593 7764 -327 2089 523 A C ATOM 3282 CG1 VAL E 37 17.606 -2.495 -32.663 1.00 70.85 A C ANISOU 3282 CG1 VAL E 37 10914 8609 7395 -294 1902 604 A C ATOM 3283 CG2 VAL E 37 18.120 -4.693 -31.576 1.00 73.34 A C ANISOU 3283 CG2 VAL E 37 11118 8673 8075 -196 2095 504 A C ATOM 3284 N ARG E 38 18.613 -6.551 -34.686 1.00 75.65 A N ANISOU 3284 N ARG E 38 11828 8584 8331 -449 2527 340 A N ATOM 3285 CA ARG E 38 19.081 -7.930 -34.675 1.00 62.51 A C ANISOU 3285 CA ARG E 38 10141 6761 6850 -432 2706 247 A C ATOM 3286 C ARG E 38 20.310 -8.031 -33.781 1.00 66.63 A C ANISOU 3286 C ARG E 38 10573 7245 7498 -403 2675 216 A C ATOM 3287 O ARG E 38 21.248 -7.238 -33.913 1.00 62.31 A O ANISOU 3287 O ARG E 38 10089 6728 6858 -484 2608 226 A O ATOM 3288 CB ARG E 38 19.403 -8.418 -36.088 1.00 61.32 A C ANISOU 3288 CB ARG E 38 10167 6532 6599 -540 2888 170 A C ATOM 3289 CG ARG E 38 19.491 -9.933 -36.204 1.00 65.66 A C ANISOU 3289 CG ARG E 38 10670 6949 7330 -505 3094 79 A C ATOM 3290 CD ARG E 38 19.180 -10.410 -37.614 1.00 62.04 A C ANISOU 3290 CD ARG E 38 10360 6476 6736 -596 3277 42 A C ATOM 3291 NE ARG E 38 20.041 -9.784 -38.610 1.00 60.38 A N ANISOU 3291 NE ARG E 38 10335 6293 6312 -697 3298 -21 A N ATOM 3292 CZ ARG E 38 19.922 -9.959 -39.919 1.00 76.38 A C ANISOU 3292 CZ ARG E 38 12522 8348 8153 -785 3437 -58 A C ATOM 3293 NH1 ARG E 38 18.986 -10.743 -40.429 1.00 70.28 A N1+ ANISOU 3293 NH1 ARG E 38 11745 7581 7377 -800 3582 -17 A N1+ ATOM 3294 NH2 ARG E 38 20.765 -9.335 -40.737 1.00 76.87 A N ANISOU 3294 NH2 ARG E 38 12751 8437 8020 -867 3426 -135 A N ATOM 3295 N ILE E 39 20.295 -9.004 -32.876 1.00 65.92 A N ANISOU 3295 N ILE E 39 10338 7083 7626 -296 2712 189 A N ATOM 3296 CA ILE E 39 21.322 -9.175 -31.859 1.00 67.39 A C ANISOU 3296 CA ILE E 39 10422 7233 7951 -246 2661 188 A C ATOM 3297 C ILE E 39 21.971 -10.538 -32.043 1.00 73.55 A C ANISOU 3297 C ILE E 39 11195 7831 8920 -217 2828 73 A C ATOM 3298 O ILE E 39 21.283 -11.543 -32.265 1.00 66.39 A O ANISOU 3298 O ILE E 39 10243 6867 8114 -171 2950 21 A O ATOM 3299 CB ILE E 39 20.737 -9.045 -30.437 1.00 66.49 A C ANISOU 3299 CB ILE E 39 10117 7228 7917 -117 2520 262 A C ATOM 3300 CG1 ILE E 39 19.919 -7.759 -30.303 1.00 61.62 A C ANISOU 3300 CG1 ILE E 39 9489 6808 7114 -115 2367 352 A C ATOM 3301 CG2 ILE E 39 21.843 -9.090 -29.394 1.00 57.18 A C ANISOU 3301 CG2 ILE E 39 8844 6038 6844 -82 2453 295 A C ATOM 3302 CD1 ILE E 39 19.142 -7.665 -29.006 1.00 51.70 A C ANISOU 3302 CD1 ILE E 39 8053 5676 5914 37 2238 391 A C ATOM 3303 N LYS E 40 23.301 -10.558 -31.961 1.00 69.38 A N ANISOU 3303 N LYS E 40 10706 7209 8447 -244 2827 36 A N ATOM 3304 CA LYS E 40 24.074 -11.792 -31.885 1.00 69.20 A C ANISOU 3304 CA LYS E 40 10648 7012 8633 -179 2947 -73 A C ATOM 3305 C LYS E 40 24.201 -12.170 -30.414 1.00 68.69 A C ANISOU 3305 C LYS E 40 10397 6949 8755 -57 2842 -9 A C ATOM 3306 O LYS E 40 24.901 -11.496 -29.651 1.00 69.59 A O ANISOU 3306 O LYS E 40 10487 7094 8861 -68 2697 83 A O ATOM 3307 CB LYS E 40 25.446 -11.610 -32.530 1.00 84.11 A C ANISOU 3307 CB LYS E 40 12686 8773 10500 -256 2972 -154 A C ATOM 3308 CG LYS E 40 26.384 -12.805 -32.393 1.00 68.25 A C ANISOU 3308 CG LYS E 40 10642 6570 8721 -165 3069 -276 A C ATOM 3309 CD LYS E 40 27.757 -12.484 -32.975 1.00 85.71 A C ANISOU 3309 CD LYS E 40 13018 8634 10914 -236 3052 -361 A C ATOM 3310 CE LYS E 40 28.784 -13.564 -32.655 1.00 66.09 A C ANISOU 3310 CE LYS E 40 10490 5940 8682 -121 3100 -472 A C ATOM 3311 NZ LYS E 40 28.563 -14.814 -33.436 1.00 70.24 A N1+ ANISOU 3311 NZ LYS E 40 10998 6411 9279 -36 3331 -653 A N1+ ATOM 3312 N ILE E 41 23.514 -13.238 -30.012 1.00 72.26 A N ANISOU 3312 N ILE E 41 10712 7377 9366 50 2907 -49 A N ATOM 3313 CA ILE E 41 23.550 -13.668 -28.620 1.00 68.92 A C ANISOU 3313 CA ILE E 41 10110 6967 9109 176 2800 0 A C ATOM 3314 C ILE E 41 24.901 -14.301 -28.320 1.00 72.32 A C ANISOU 3314 C ILE E 41 10529 7237 9712 222 2814 -44 A C ATOM 3315 O ILE E 41 25.405 -15.127 -29.092 1.00 74.56 A O ANISOU 3315 O ILE E 41 10863 7373 10091 227 2967 -173 A O ATOM 3316 CB ILE E 41 22.398 -14.640 -28.325 1.00 70.70 A C ANISOU 3316 CB ILE E 41 10193 7204 9465 267 2849 -41 A C ATOM 3317 CG1 ILE E 41 21.054 -13.964 -28.600 1.00 58.91 A C ANISOU 3317 CG1 ILE E 41 8727 5839 7816 227 2805 9 A C ATOM 3318 CG2 ILE E 41 22.461 -15.127 -26.885 1.00 66.01 A C ANISOU 3318 CG2 ILE E 41 9415 6630 9036 405 2726 -7 A C ATOM 3319 CD1 ILE E 41 20.804 -12.741 -27.746 1.00 53.80 A C ANISOU 3319 CD1 ILE E 41 8049 5364 7027 251 2605 121 A C ATOM 3320 N LEU E 42 25.501 -13.904 -27.201 1.00 63.66 A N ANISOU 3320 N LEU E 42 9366 6172 8649 260 2653 67 A N ATOM 3321 CA LEU E 42 26.732 -14.506 -26.702 1.00 57.22 A C ANISOU 3321 CA LEU E 42 8527 5196 8020 321 2624 59 A C ATOM 3322 C LEU E 42 26.507 -15.416 -25.507 1.00 61.57 A C ANISOU 3322 C LEU E 42 8881 5756 8755 478 2564 79 A C ATOM 3323 O LEU E 42 27.124 -16.480 -25.424 1.00 65.28 A O ANISOU 3323 O LEU E 42 9301 6065 9435 569 2616 -2 A O ATOM 3324 CB LEU E 42 27.742 -13.417 -26.321 1.00 66.42 A C ANISOU 3324 CB LEU E 42 9771 6368 9097 228 2474 196 A C ATOM 3325 CG LEU E 42 28.372 -12.607 -27.454 1.00 65.56 A C ANISOU 3325 CG LEU E 42 9864 6190 8854 68 2503 162 A C ATOM 3326 CD1 LEU E 42 29.612 -11.876 -26.959 1.00 63.72 A C ANISOU 3326 CD1 LEU E 42 9687 5891 8632 -17 2349 293 A C ATOM 3327 CD2 LEU E 42 28.709 -13.498 -28.640 1.00 59.58 A C ANISOU 3327 CD2 LEU E 42 9213 5243 8184 82 2685 -43 A C ATOM 3328 N PHE E 43 25.641 -15.020 -24.578 1.00 63.64 A N ANISOU 3328 N PHE E 43 9028 6211 8941 524 2446 175 A N ATOM 3329 CA PHE E 43 25.320 -15.827 -23.411 1.00 63.68 A C ANISOU 3329 CA PHE E 43 8848 6253 9094 675 2367 186 A C ATOM 3330 C PHE E 43 23.845 -15.672 -23.085 1.00 74.76 A C ANISOU 3330 C PHE E 43 10159 7831 10415 716 2328 178 A C ATOM 3331 O PHE E 43 23.280 -14.586 -23.231 1.00 71.52 A O ANISOU 3331 O PHE E 43 9805 7570 9800 651 2280 236 A O ATOM 3332 CB PHE E 43 26.162 -15.428 -22.190 1.00 63.38 A C ANISOU 3332 CB PHE E 43 8760 6271 9051 715 2192 342 A C ATOM 3333 CG PHE E 43 27.641 -15.464 -22.434 1.00 77.41 A C ANISOU 3333 CG PHE E 43 10643 7852 10918 666 2191 374 A C ATOM 3334 CD1 PHE E 43 28.306 -14.348 -22.913 1.00 75.51 A C ANISOU 3334 CD1 PHE E 43 10553 7606 10531 512 2161 457 A C ATOM 3335 CD2 PHE E 43 28.366 -16.617 -22.189 1.00 76.69 A C ANISOU 3335 CD2 PHE E 43 10498 7569 11071 777 2204 316 A C ATOM 3336 CE1 PHE E 43 29.668 -14.381 -23.141 1.00 65.62 A C ANISOU 3336 CE1 PHE E 43 9410 6141 9381 461 2138 479 A C ATOM 3337 CE2 PHE E 43 29.727 -16.655 -22.414 1.00 80.10 A C ANISOU 3337 CE2 PHE E 43 11039 7790 11605 746 2183 335 A C ATOM 3338 CZ PHE E 43 30.379 -15.536 -22.891 1.00 70.29 A C ANISOU 3338 CZ PHE E 43 9961 6524 10221 584 2146 415 A C ATOM 3339 N THR E 44 23.228 -16.766 -22.646 1.00 70.76 A N ANISOU 3339 N THR E 44 9507 7297 10082 828 2337 98 A N ATOM 3340 CA THR E 44 21.849 -16.754 -22.186 1.00 64.35 A C ANISOU 3340 CA THR E 44 8597 6617 9237 886 2266 76 A C ATOM 3341 C THR E 44 21.728 -17.686 -20.989 1.00 75.45 A C ANISOU 3341 C THR E 44 9816 8036 10815 1038 2160 52 A C ATOM 3342 O THR E 44 22.632 -18.472 -20.692 1.00 69.66 A O ANISOU 3342 O THR E 44 9028 7193 10247 1095 2170 45 A O ATOM 3343 CB THR E 44 20.870 -17.168 -23.294 1.00 67.81 A C ANISOU 3343 CB THR E 44 9075 6983 9708 817 2411 -23 A C ATOM 3344 CG2 THR E 44 21.167 -18.582 -23.769 1.00 66.44 A C ANISOU 3344 CG2 THR E 44 8834 6637 9773 835 2565 -131 A C ATOM 3345 OG1 THR E 44 19.528 -17.108 -22.798 1.00 68.64 A O ANISOU 3345 OG1 THR E 44 9096 7187 9798 872 2310 -40 A O ATOM 3346 N SER E 45 20.600 -17.587 -20.293 1.00 81.14 A N ANISOU 3346 N SER E 45 10442 8890 11499 1112 2043 33 A N ATOM 3347 CA SER E 45 20.318 -18.425 -19.138 1.00 74.13 A C ANISOU 3347 CA SER E 45 9377 8037 10753 1259 1918 -7 A C ATOM 3348 C SER E 45 18.909 -18.990 -19.271 1.00 66.96 A C ANISOU 3348 C SER E 45 8391 7106 9944 1279 1912 -124 A C ATOM 3349 O SER E 45 18.226 -18.785 -20.278 1.00 73.47 A O ANISOU 3349 O SER E 45 9304 7875 10735 1176 2015 -156 A O ATOM 3350 CB SER E 45 20.480 -17.642 -17.828 1.00 75.43 A C ANISOU 3350 CB SER E 45 9491 8422 10748 1353 1723 94 A C ATOM 3351 OG SER E 45 20.400 -18.506 -16.707 1.00 81.55 A O ANISOU 3351 OG SER E 45 10103 9230 11651 1498 1597 59 A O ATOM 3352 N LEU E 46 18.473 -19.710 -18.242 1.00 72.25 A N ANISOU 3352 N LEU E 46 10169 5586 11697 1140 1667 -2251 A N ATOM 3353 CA LEU E 46 17.151 -20.317 -18.212 1.00 75.74 A C ANISOU 3353 CA LEU E 46 10478 6368 11934 1112 1533 -2046 A C ATOM 3354 C LEU E 46 16.395 -19.833 -16.983 1.00 89.46 A C ANISOU 3354 C LEU E 46 12598 7992 13401 1033 1293 -1653 A C ATOM 3355 O LEU E 46 16.974 -19.689 -15.901 1.00 90.98 A O ANISOU 3355 O LEU E 46 13067 7816 13685 1120 1104 -1455 A O ATOM 3356 CB LEU E 46 17.247 -21.846 -18.214 1.00 83.67 A C ANISOU 3356 CB LEU E 46 11144 7354 13294 1322 1372 -2066 A C ATOM 3357 CG LEU E 46 15.924 -22.609 -18.145 1.00 84.56 A C ANISOU 3357 CG LEU E 46 11080 7776 13275 1232 1237 -1882 A C ATOM 3358 CD1 LEU E 46 15.490 -23.063 -19.530 1.00 80.09 A C ANISOU 3358 CD1 LEU E 46 10078 7681 12672 1163 1510 -2104 A C ATOM 3359 CD2 LEU E 46 16.045 -23.790 -17.200 1.00 87.67 A C ANISOU 3359 CD2 LEU E 46 11369 8000 13943 1417 888 -1727 A C ATOM 3360 N CYS E 47 15.100 -19.576 -17.158 1.00 89.01 A N ANISOU 3360 N CYS E 47 12562 8253 13004 886 1320 -1534 A N ATOM 3361 CA CYS E 47 14.242 -19.067 -16.099 1.00 82.83 A C ANISOU 3361 CA CYS E 47 12132 7407 11934 814 1129 -1237 A C ATOM 3362 C CYS E 47 13.007 -19.949 -15.980 1.00 81.87 A C ANISOU 3362 C CYS E 47 11890 7412 11806 758 989 -1123 A C ATOM 3363 O CYS E 47 12.729 -20.789 -16.840 1.00 90.68 A O ANISOU 3363 O CYS E 47 12648 8724 13082 736 1095 -1236 A O ATOM 3364 CB CYS E 47 13.837 -17.610 -16.365 1.00 77.78 A C ANISOU 3364 CB CYS E 47 11711 6975 10866 685 1342 -1222 A C ATOM 3365 SG CYS E 47 12.541 -16.963 -15.284 1.00 99.11 A S ANISOU 3365 SG CYS E 47 14804 9682 13171 632 1171 -919 A S ATOM 3366 N HIS E 48 12.258 -19.746 -14.893 1.00100.12 A N ANISOU 3366 N HIS E 48 14493 9618 13928 713 763 -919 A N ATOM 3367 CA HIS E 48 11.044 -20.528 -14.681 1.00 89.66 A C ANISOU 3367 CA HIS E 48 13090 8352 12626 600 631 -859 A C ATOM 3368 C HIS E 48 9.983 -20.217 -15.728 1.00 83.02 A C ANISOU 3368 C HIS E 48 12188 7727 11630 458 934 -851 A C ATOM 3369 O HIS E 48 9.159 -21.081 -16.041 1.00 82.39 A O ANISOU 3369 O HIS E 48 11905 7704 11696 329 947 -840 A O ATOM 3370 CB HIS E 48 10.486 -20.280 -13.280 1.00 90.01 A C ANISOU 3370 CB HIS E 48 13476 8250 12473 583 336 -717 A C ATOM 3371 CG HIS E 48 9.304 -21.135 -12.946 1.00124.46 A C ANISOU 3371 CG HIS E 48 17757 12621 16909 425 175 -735 A C ATOM 3372 CD2 HIS E 48 9.223 -22.423 -12.534 1.00130.05 A C ANISOU 3372 CD2 HIS E 48 18188 13353 17871 387 -83 -807 A C ATOM 3373 ND1 HIS E 48 8.006 -20.679 -13.031 1.00108.33 A N ANISOU 3373 ND1 HIS E 48 15917 10558 14685 267 293 -700 A N ATOM 3374 CE1 HIS E 48 7.177 -21.647 -12.683 1.00110.91 A C ANISOU 3374 CE1 HIS E 48 16119 10837 15187 92 129 -771 A C ATOM 3375 NE2 HIS E 48 7.890 -22.716 -12.377 1.00121.34 A N ANISOU 3375 NE2 HIS E 48 17121 12230 16752 145 -111 -849 A N ATOM 3376 N THR E 49 9.982 -18.999 -16.273 1.00 82.77 A N ANISOU 3376 N THR E 49 12313 7841 11296 479 1188 -834 A N ATOM 3377 CA THR E 49 9.023 -18.651 -17.318 1.00 81.96 A C ANISOU 3377 CA THR E 49 12143 7999 11000 419 1493 -764 A C ATOM 3378 C THR E 49 9.255 -19.488 -18.572 1.00 76.46 A C ANISOU 3378 C THR E 49 10985 7566 10499 399 1702 -880 A C ATOM 3379 O THR E 49 8.305 -20.003 -19.181 1.00 85.16 A O ANISOU 3379 O THR E 49 11937 8792 11630 299 1851 -761 A O ATOM 3380 CB THR E 49 9.127 -17.158 -17.640 1.00 72.67 A C ANISOU 3380 CB THR E 49 11158 7037 9417 497 1700 -744 A C ATOM 3381 CG2 THR E 49 8.002 -16.730 -18.568 1.00 56.12 A C ANISOU 3381 CG2 THR E 49 9041 5223 7059 511 1989 -582 A C ATOM 3382 OG1 THR E 49 9.054 -16.398 -16.427 1.00 68.97 A O ANISOU 3382 OG1 THR E 49 11080 6364 8761 527 1508 -654 A O ATOM 3383 N ASP E 50 10.523 -19.626 -18.972 1.00 69.47 A N ANISOU 3383 N ASP E 50 9876 6763 9758 491 1738 -1116 A N ATOM 3384 CA ASP E 50 10.864 -20.448 -20.128 1.00 68.88 A C ANISOU 3384 CA ASP E 50 9334 6980 9859 509 1930 -1293 A C ATOM 3385 C ASP E 50 10.347 -21.870 -19.960 1.00 76.30 A C ANISOU 3385 C ASP E 50 10023 7855 11112 425 1795 -1229 A C ATOM 3386 O ASP E 50 9.691 -22.412 -20.854 1.00 74.26 A O ANISOU 3386 O ASP E 50 9477 7881 10857 331 2007 -1172 A O ATOM 3387 CB ASP E 50 12.379 -20.458 -20.342 1.00 80.47 A C ANISOU 3387 CB ASP E 50 10648 8411 11517 642 1941 -1614 A C ATOM 3388 CG ASP E 50 12.927 -19.097 -20.713 1.00 77.83 A C ANISOU 3388 CG ASP E 50 10460 8219 10891 649 2130 -1759 A C ATOM 3389 OD1 ASP E 50 12.417 -18.493 -21.681 1.00 76.16 A O ANISOU 3389 OD1 ASP E 50 10137 8462 10339 619 2396 -1768 A O ATOM 3390 OD2 ASP E 50 13.878 -18.636 -20.046 1.00 90.50 A O1- ANISOU 3390 OD2 ASP E 50 12271 9511 12602 681 2020 -1854 A O1- ATOM 3391 N VAL E 51 10.629 -22.487 -18.811 1.00 67.37 A N ANISOU 3391 N VAL E 51 8971 6401 10224 451 1447 -1224 A N ATOM 3392 CA VAL E 51 10.221 -23.871 -18.589 1.00 77.15 A C ANISOU 3392 CA VAL E 51 9906 7649 11758 360 1284 -1218 A C ATOM 3393 C VAL E 51 8.705 -23.978 -18.488 1.00 81.18 A C ANISOU 3393 C VAL E 51 10526 8134 12186 92 1325 -1016 A C ATOM 3394 O VAL E 51 8.107 -24.957 -18.951 1.00 80.41 A O ANISOU 3394 O VAL E 51 10092 8187 12273 -83 1406 -999 A O ATOM 3395 CB VAL E 51 10.911 -24.434 -17.333 1.00 68.69 A C ANISOU 3395 CB VAL E 51 8880 6319 10900 497 879 -1253 A C ATOM 3396 CG1 VAL E 51 10.539 -25.893 -17.134 1.00 70.18 A C ANISOU 3396 CG1 VAL E 51 8667 6628 11370 409 697 -1294 A C ATOM 3397 CG2 VAL E 51 12.418 -24.276 -17.441 1.00 80.65 A C ANISOU 3397 CG2 VAL E 51 10349 7742 12551 778 885 -1410 A C ATOM 3398 N TYR E 52 8.059 -22.980 -17.883 1.00 76.19 A N ANISOU 3398 N TYR E 52 10360 7293 11297 52 1290 -867 A N ATOM 3399 CA TYR E 52 6.607 -23.009 -17.739 1.00 81.27 A C ANISOU 3399 CA TYR E 52 11175 7803 11902 -179 1347 -696 A C ATOM 3400 C TYR E 52 5.926 -23.003 -19.100 1.00 76.39 A C ANISOU 3400 C TYR E 52 10371 7432 11221 -267 1767 -539 A C ATOM 3401 O TYR E 52 4.993 -23.776 -19.343 1.00 92.17 A O ANISOU 3401 O TYR E 52 12220 9389 13409 -513 1864 -433 A O ATOM 3402 CB TYR E 52 6.142 -21.818 -16.895 1.00 85.38 A C ANISOU 3402 CB TYR E 52 12234 8079 12127 -123 1263 -597 A C ATOM 3403 CG TYR E 52 4.660 -21.806 -16.575 1.00 76.02 A C ANISOU 3403 CG TYR E 52 11298 6642 10945 -325 1300 -471 A C ATOM 3404 CD1 TYR E 52 3.747 -21.198 -17.428 1.00 89.94 A C ANISOU 3404 CD1 TYR E 52 13196 8425 12553 -334 1662 -244 A C ATOM 3405 CD2 TYR E 52 4.176 -22.394 -15.411 1.00 93.18 A C ANISOU 3405 CD2 TYR E 52 13574 8556 13272 -492 979 -589 A C ATOM 3406 CE1 TYR E 52 2.393 -21.180 -17.134 1.00 94.34 A C ANISOU 3406 CE1 TYR E 52 14026 8646 13175 -500 1729 -121 A C ATOM 3407 CE2 TYR E 52 2.825 -22.380 -15.110 1.00 93.83 A C ANISOU 3407 CE2 TYR E 52 13904 8341 13406 -703 1030 -546 A C ATOM 3408 CZ TYR E 52 1.938 -21.773 -15.975 1.00 99.88 A C ANISOU 3408 CZ TYR E 52 14844 9026 14082 -705 1417 -304 A C ATOM 3409 OH TYR E 52 0.594 -21.759 -15.676 1.00 90.29 A O ANISOU 3409 OH TYR E 52 13915 7414 12978 -897 1499 -253 A O ATOM 3410 N PHE E 53 6.384 -22.142 -20.009 1.00 75.39 A N ANISOU 3410 N PHE E 53 10229 7597 10818 -84 2031 -517 A N ATOM 3411 CA PHE E 53 5.749 -22.104 -21.320 1.00 77.55 A C ANISOU 3411 CA PHE E 53 10307 8206 10953 -118 2434 -323 A C ATOM 3412 C PHE E 53 6.332 -23.119 -22.294 1.00 80.17 A C ANISOU 3412 C PHE E 53 10072 8933 11456 -137 2580 -464 A C ATOM 3413 O PHE E 53 5.772 -23.303 -23.380 1.00 81.73 A O ANISOU 3413 O PHE E 53 10039 9464 11550 -192 2918 -276 A O ATOM 3414 CB PHE E 53 5.824 -20.691 -21.894 1.00 66.44 A C ANISOU 3414 CB PHE E 53 9097 7058 9089 98 2659 -233 A C ATOM 3415 CG PHE E 53 4.888 -19.737 -21.219 1.00 86.97 A C ANISOU 3415 CG PHE E 53 12201 9360 11483 132 2630 -9 A C ATOM 3416 CD1 PHE E 53 3.577 -19.615 -21.648 1.00 81.71 A C ANISOU 3416 CD1 PHE E 53 11674 8631 10741 89 2882 342 A C ATOM 3417 CD2 PHE E 53 5.304 -18.999 -20.125 1.00 79.29 A C ANISOU 3417 CD2 PHE E 53 11567 8150 10411 219 2366 -133 A C ATOM 3418 CE1 PHE E 53 2.705 -18.753 -21.014 1.00 85.03 A C ANISOU 3418 CE1 PHE E 53 12568 8738 11002 170 2866 521 A C ATOM 3419 CE2 PHE E 53 4.438 -18.135 -19.487 1.00 87.58 A C ANISOU 3419 CE2 PHE E 53 13056 8964 11256 280 2345 37 A C ATOM 3420 CZ PHE E 53 3.135 -18.015 -19.928 1.00 94.02 A C ANISOU 3420 CZ PHE E 53 14013 9696 12014 271 2590 341 A C ATOM 3421 N TRP E 54 7.425 -23.787 -21.927 1.00 76.67 A N ANISOU 3421 N TRP E 54 9395 8474 11262 -63 2347 -766 A N ATOM 3422 CA TRP E 54 7.916 -24.921 -22.699 1.00 77.29 A C ANISOU 3422 CA TRP E 54 8910 8899 11558 -65 2450 -932 A C ATOM 3423 C TRP E 54 7.134 -26.185 -22.370 1.00 77.16 A C ANISOU 3423 C TRP E 54 8663 8791 11865 -342 2355 -837 A C ATOM 3424 O TRP E 54 6.843 -26.990 -23.262 1.00 77.16 A O ANISOU 3424 O TRP E 54 8226 9143 11947 -465 2596 -789 A O ATOM 3425 CB TRP E 54 9.409 -25.111 -22.426 1.00 71.17 A C ANISOU 3425 CB TRP E 54 7994 8098 10948 180 2252 -1291 A C ATOM 3426 CG TRP E 54 9.952 -26.461 -22.764 1.00 73.99 A C ANISOU 3426 CG TRP E 54 7803 8681 11626 226 2226 -1498 A C ATOM 3427 CD1 TRP E 54 10.216 -26.952 -24.008 1.00 76.52 A C ANISOU 3427 CD1 TRP E 54 7642 9509 11924 281 2525 -1639 A C ATOM 3428 CD2 TRP E 54 10.321 -27.491 -21.838 1.00 80.32 A C ANISOU 3428 CD2 TRP E 54 8447 9286 12783 264 1877 -1598 A C ATOM 3429 CE2 TRP E 54 10.793 -28.582 -22.594 1.00 79.64 A C ANISOU 3429 CE2 TRP E 54 7771 9590 12899 352 1991 -1799 A C ATOM 3430 CE3 TRP E 54 10.293 -27.598 -20.444 1.00 75.43 A C ANISOU 3430 CE3 TRP E 54 8100 8272 12290 258 1477 -1538 A C ATOM 3431 NE1 TRP E 54 10.719 -28.228 -23.915 1.00 80.24 A N ANISOU 3431 NE1 TRP E 54 7664 10086 12738 352 2395 -1831 A N ATOM 3432 CZ2 TRP E 54 11.235 -29.763 -22.003 1.00 84.40 A C ANISOU 3432 CZ2 TRP E 54 8039 10190 13840 454 1714 -1930 A C ATOM 3433 CZ3 TRP E 54 10.731 -28.773 -19.859 1.00 80.84 A C ANISOU 3433 CZ3 TRP E 54 8452 8981 13282 352 1193 -1657 A C ATOM 3434 CH2 TRP E 54 11.194 -29.840 -20.638 1.00 82.27 A C ANISOU 3434 CH2 TRP E 54 8036 9546 13676 457 1310 -1846 A C ATOM 3435 N GLU E 55 6.783 -26.370 -21.096 1.00 73.75 A N ANISOU 3435 N GLU E 55 8487 7938 11595 -463 2012 -828 A N ATOM 3436 CA GLU E 55 5.889 -27.459 -20.719 1.00 82.86 A C ANISOU 3436 CA GLU E 55 9447 9000 13036 -801 1920 -775 A C ATOM 3437 C GLU E 55 4.490 -27.223 -21.272 1.00 94.79 A C ANISOU 3437 C GLU E 55 11115 10423 14480 -1086 2255 -450 A C ATOM 3438 O GLU E 55 3.873 -28.133 -21.840 1.00 89.02 A O ANISOU 3438 O GLU E 55 10027 9852 13945 -1369 2454 -348 A O ATOM 3439 CB GLU E 55 5.849 -27.603 -19.198 1.00 82.02 A C ANISOU 3439 CB GLU E 55 9590 8526 13050 -848 1462 -891 A C ATOM 3440 CG GLU E 55 7.084 -28.251 -18.595 1.00 88.63 A C ANISOU 3440 CG GLU E 55 10164 9467 14045 -598 1119 -1138 A C ATOM 3441 CD GLU E 55 7.001 -28.369 -17.084 1.00 94.83 A C ANISOU 3441 CD GLU E 55 11177 9989 14864 -617 665 -1208 A C ATOM 3442 OE1 GLU E 55 7.163 -27.340 -16.394 1.00 96.25 A O ANISOU 3442 OE1 GLU E 55 11845 9909 14814 -469 544 -1150 A O ATOM 3443 OE2 GLU E 55 6.770 -29.490 -16.586 1.00102.57 A O1- ANISOU 3443 OE2 GLU E 55 11815 11087 16069 -783 432 -1332 A O1- ATOM 3444 N ALA E 56 3.977 -26.004 -21.110 1.00 90.03 A N ANISOU 3444 N ALA E 56 11039 9562 13608 -1003 2338 -262 A N ATOM 3445 CA ALA E 56 2.679 -25.593 -21.644 1.00 94.15 A C ANISOU 3445 CA ALA E 56 11793 9939 14041 -1166 2684 105 A C ATOM 3446 C ALA E 56 1.577 -26.564 -21.220 1.00107.09 A C ANISOU 3446 C ALA E 56 13379 11247 16065 -1619 2663 162 A C ATOM 3447 O ALA E 56 0.870 -27.148 -22.040 1.00108.11 A O ANISOU 3447 O ALA E 56 13270 11475 16334 -1872 2997 401 A O ATOM 3448 CB ALA E 56 2.738 -25.451 -23.167 1.00 83.76 A C ANISOU 3448 CB ALA E 56 10188 9139 12497 -1050 3132 330 A C ATOM 3449 N LYS E 57 1.441 -26.721 -19.902 1.00115.95 A N ANISOU 3449 N LYS E 57 14717 11992 17345 -1739 2271 -73 A N ATOM 3450 CA LYS E 57 0.479 -27.662 -19.341 1.00132.00 A C ANISOU 3450 CA LYS E 57 16674 13722 19757 -2212 2186 -151 A C ATOM 3451 C LYS E 57 -0.949 -27.129 -19.318 1.00131.63 A C ANISOU 3451 C LYS E 57 17106 13140 19768 -2426 2442 105 A C ATOM 3452 O LYS E 57 -1.869 -27.892 -19.007 1.00124.39 A O ANISOU 3452 O LYS E 57 16137 11910 19214 -2888 2459 47 A O ATOM 3453 CB LYS E 57 0.894 -28.058 -17.921 1.00130.90 A C ANISOU 3453 CB LYS E 57 16542 13478 19715 -2239 1649 -545 A C ATOM 3454 CG LYS E 57 1.899 -29.198 -17.857 1.00117.14 A C ANISOU 3454 CG LYS E 57 14189 12188 18133 -2208 1404 -794 A C ATOM 3455 CD LYS E 57 1.540 -30.311 -18.826 1.00127.97 A C ANISOU 3455 CD LYS E 57 14997 13847 19779 -2538 1694 -716 A C ATOM 3456 CE LYS E 57 1.946 -31.671 -18.281 1.00133.01 A C ANISOU 3456 CE LYS E 57 15055 14797 20685 -2703 1361 -1041 A C ATOM 3457 NZ LYS E 57 1.048 -32.756 -18.766 1.00130.20 A N1+ ANISOU 3457 NZ LYS E 57 14262 14541 20666 -3256 1592 -1011 A N1+ ATOM 3458 N GLY E 58 -1.159 -25.855 -19.635 1.00125.19 A N ANISOU 3458 N GLY E 58 16737 12205 18623 -2104 2646 370 A N ATOM 3459 CA GLY E 58 -2.494 -25.291 -19.634 1.00112.94 A C ANISOU 3459 CA GLY E 58 15669 10116 17129 -2211 2909 645 A C ATOM 3460 C GLY E 58 -2.594 -24.035 -20.473 1.00122.97 A C ANISOU 3460 C GLY E 58 17221 11515 17985 -1783 3244 1048 A C ATOM 3461 O GLY E 58 -3.422 -23.159 -20.206 1.00131.57 A O ANISOU 3461 O GLY E 58 18824 12185 18982 -1648 3356 1223 A O ATOM 3462 N GLN E 59 -1.748 -23.943 -21.491 1.00119.19 A N ANISOU 3462 N GLN E 59 16677 16886 11724 -2915 394 -1213 A N ATOM 3463 CA GLN E 59 -1.636 -22.772 -22.346 1.00110.23 A C ANISOU 3463 CA GLN E 59 15745 15352 10785 -2472 682 -1495 A C ATOM 3464 C GLN E 59 -2.044 -23.155 -23.766 1.00104.56 A C ANISOU 3464 C GLN E 59 15182 14069 10478 -2348 782 -1568 A C ATOM 3465 O GLN E 59 -2.475 -24.280 -24.030 1.00 96.26 A O ANISOU 3465 O GLN E 59 14082 12948 9544 -2584 661 -1442 A O ATOM 3466 CB GLN E 59 -0.210 -22.201 -22.339 1.00100.95 A C ANISOU 3466 CB GLN E 59 14236 14312 9807 -2206 818 -1111 A C ATOM 3467 CG GLN E 59 0.459 -21.862 -20.984 1.00102.61 A C ANISOU 3467 CG GLN E 59 14193 15139 9656 -2347 710 -870 A C ATOM 3468 CD GLN E 59 0.283 -22.923 -19.909 1.00120.61 A C ANISOU 3468 CD GLN E 59 16294 17916 11615 -2848 394 -607 A C ATOM 3469 NE2 GLN E 59 -0.056 -22.495 -18.703 1.00123.04 A N ANISOU 3469 NE2 GLN E 59 16736 18715 11299 -3115 301 -802 A N ATOM 3470 OE1 GLN E 59 0.479 -24.107 -20.157 1.00125.03 A O ANISOU 3470 OE1 GLN E 59 16587 18433 12487 -3018 241 -210 A O ATOM 3471 N THR E 60 -1.919 -22.201 -24.685 1.00101.06 A N ANISOU 3471 N THR E 60 14923 13241 10234 -2018 988 -1742 A N ATOM 3472 CA THR E 60 -2.042 -22.535 -26.098 1.00 89.62 A C ANISOU 3472 CA THR E 60 13598 11318 9135 -1941 1103 -1721 A C ATOM 3473 C THR E 60 -0.714 -23.122 -26.559 1.00 86.97 A C ANISOU 3473 C THR E 60 12902 11000 9144 -1847 1268 -1261 A C ATOM 3474 O THR E 60 0.291 -22.402 -26.617 1.00 90.62 A O ANISOU 3474 O THR E 60 13249 11469 9713 -1614 1397 -1130 A O ATOM 3475 CB THR E 60 -2.401 -21.310 -26.940 1.00 88.45 A C ANISOU 3475 CB THR E 60 13792 10754 9061 -1702 1207 -2022 A C ATOM 3476 CG2 THR E 60 -2.506 -21.694 -28.411 1.00 68.22 A C ANISOU 3476 CG2 THR E 60 11390 7762 6767 -1720 1305 -1966 A C ATOM 3477 OG1 THR E 60 -3.656 -20.774 -26.508 1.00 95.19 A O ANISOU 3477 OG1 THR E 60 14930 11515 9723 -1756 1089 -2452 A O ATOM 3478 N PRO E 61 -0.659 -24.416 -26.880 1.00 85.36 A N ANISOU 3478 N PRO E 61 12487 10775 9169 -2018 1285 -1002 A N ATOM 3479 CA PRO E 61 0.610 -25.002 -27.334 1.00 73.78 A C ANISOU 3479 CA PRO E 61 10642 9254 8137 -1896 1519 -595 A C ATOM 3480 C PRO E 61 1.077 -24.387 -28.644 1.00 82.82 A C ANISOU 3480 C PRO E 61 12031 9966 9471 -1662 1827 -743 A C ATOM 3481 O PRO E 61 0.660 -24.805 -29.728 1.00 77.04 A O ANISOU 3481 O PRO E 61 11507 8928 8837 -1731 1990 -858 A O ATOM 3482 CB PRO E 61 0.285 -26.494 -27.484 1.00 76.76 A C ANISOU 3482 CB PRO E 61 10775 9648 8741 -2142 1500 -345 A C ATOM 3483 CG PRO E 61 -1.188 -26.558 -27.634 1.00 80.32 A C ANISOU 3483 CG PRO E 61 11619 10003 8898 -2359 1311 -692 A C ATOM 3484 CD PRO E 61 -1.770 -25.384 -26.909 1.00 83.65 A C ANISOU 3484 CD PRO E 61 12360 10533 8891 -2322 1118 -1070 A C ATOM 3485 N LEU E 62 1.945 -23.382 -28.539 1.00 82.77 A N ANISOU 3485 N LEU E 62 12013 9954 9482 -1433 1888 -721 A N ATOM 3486 CA LEU E 62 2.413 -22.602 -29.682 1.00 75.86 A C ANISOU 3486 CA LEU E 62 11423 8689 8710 -1262 2107 -866 A C ATOM 3487 C LEU E 62 3.788 -23.150 -30.052 1.00 78.94 A C ANISOU 3487 C LEU E 62 11494 8958 9540 -1145 2399 -577 A C ATOM 3488 O LEU E 62 4.795 -22.778 -29.446 1.00 75.35 A O ANISOU 3488 O LEU E 62 10752 8635 9241 -997 2374 -341 A O ATOM 3489 CB LEU E 62 2.477 -21.119 -29.323 1.00 76.23 A C ANISOU 3489 CB LEU E 62 11641 8777 8547 -1101 1968 -1001 A C ATOM 3490 CG LEU E 62 1.553 -20.084 -29.974 1.00 88.18 A C ANISOU 3490 CG LEU E 62 13623 10014 9868 -1092 1879 -1334 A C ATOM 3491 CD1 LEU E 62 1.918 -18.680 -29.494 1.00 69.57 A C ANISOU 3491 CD1 LEU E 62 11265 7731 7436 -893 1789 -1339 A C ATOM 3492 CD2 LEU E 62 1.528 -20.150 -31.488 1.00 81.63 A C ANISOU 3492 CD2 LEU E 62 13126 8754 9134 -1172 2037 -1419 A C ATOM 3493 N PHE E 63 3.831 -24.051 -31.029 1.00 71.69 A N ANISOU 3493 N PHE E 63 10606 7779 8855 -1218 2697 -592 A N ATOM 3494 CA PHE E 63 5.063 -24.716 -31.426 1.00 73.34 A C ANISOU 3494 CA PHE E 63 10494 7802 9571 -1100 3067 -373 A C ATOM 3495 C PHE E 63 5.115 -24.824 -32.942 1.00 71.84 A C ANISOU 3495 C PHE E 63 10696 7191 9408 -1148 3472 -651 A C ATOM 3496 O PHE E 63 4.068 -24.912 -33.593 1.00 78.10 A O ANISOU 3496 O PHE E 63 11857 7918 9901 -1344 3446 -876 A O ATOM 3497 CB PHE E 63 5.174 -26.116 -30.798 1.00 70.22 A C ANISOU 3497 CB PHE E 63 9520 7605 9555 -1176 3092 10 A C ATOM 3498 CG PHE E 63 5.371 -26.098 -29.309 1.00 74.64 A C ANISOU 3498 CG PHE E 63 9656 8605 10100 -1198 2702 369 A C ATOM 3499 CD1 PHE E 63 6.602 -25.775 -28.766 1.00 74.64 A C ANISOU 3499 CD1 PHE E 63 9293 8653 10413 -1025 2692 681 A C ATOM 3500 CD2 PHE E 63 4.324 -26.401 -28.453 1.00 68.59 A C ANISOU 3500 CD2 PHE E 63 8874 8204 8981 -1440 2330 399 A C ATOM 3501 CE1 PHE E 63 6.789 -25.754 -27.397 1.00 72.21 A C ANISOU 3501 CE1 PHE E 63 8601 8803 10031 -1115 2313 1059 A C ATOM 3502 CE2 PHE E 63 4.504 -26.383 -27.082 1.00 68.18 A C ANISOU 3502 CE2 PHE E 63 8488 8605 8815 -1543 1973 716 A C ATOM 3503 CZ PHE E 63 5.739 -26.059 -26.554 1.00 76.87 A C ANISOU 3503 CZ PHE E 63 9215 9801 10191 -1392 1962 1067 A C ATOM 3504 N PRO E 64 6.321 -24.824 -33.538 1.00 79.86 A N ANISOU 3504 N PRO E 64 11662 7910 10772 -1009 3851 -647 A N ATOM 3505 CA PRO E 64 7.658 -24.763 -32.919 1.00 75.33 A C ANISOU 3505 CA PRO E 64 10640 7312 10670 -780 3912 -358 A C ATOM 3506 C PRO E 64 8.022 -23.372 -32.410 1.00 74.87 A C ANISOU 3506 C PRO E 64 10719 7343 10386 -670 3577 -347 A C ATOM 3507 O PRO E 64 7.630 -22.366 -32.995 1.00 75.47 A O ANISOU 3507 O PRO E 64 11310 7299 10064 -730 3474 -628 A O ATOM 3508 CB PRO E 64 8.580 -25.209 -34.062 1.00 70.99 A C ANISOU 3508 CB PRO E 64 10166 6291 10515 -719 4509 -517 A C ATOM 3509 CG PRO E 64 7.873 -24.744 -35.298 1.00 82.33 A C ANISOU 3509 CG PRO E 64 12317 7538 11427 -935 4626 -958 A C ATOM 3510 CD PRO E 64 6.407 -24.934 -35.006 1.00 65.31 A C ANISOU 3510 CD PRO E 64 10258 5688 8868 -1122 4286 -963 A C ATOM 3511 N ARG E 65 8.787 -23.288 -31.323 1.00 67.70 A N ANISOU 3511 N ARG E 65 9319 6652 9752 -533 3389 31 A N ATOM 3512 CA ARG E 65 9.054 -22.019 -30.665 1.00 65.97 A C ANISOU 3512 CA ARG E 65 9149 6616 9301 -449 3055 107 A C ATOM 3513 C ARG E 65 10.485 -21.973 -30.151 1.00 74.67 A C ANISOU 3513 C ARG E 65 9780 7666 10927 -281 3074 497 A C ATOM 3514 O ARG E 65 11.033 -22.990 -29.716 1.00 71.88 A O ANISOU 3514 O ARG E 65 8888 7341 11081 -248 3167 848 A O ATOM 3515 CB ARG E 65 8.080 -21.795 -29.503 1.00 60.80 A C ANISOU 3515 CB ARG E 65 8405 6482 8212 -549 2649 181 A C ATOM 3516 CG ARG E 65 7.835 -20.340 -29.162 1.00 64.61 A C ANISOU 3516 CG ARG E 65 9147 7108 8296 -494 2393 58 A C ATOM 3517 CD ARG E 65 6.757 -20.214 -28.103 1.00 69.47 A C ANISOU 3517 CD ARG E 65 9737 8187 8471 -609 2107 8 A C ATOM 3518 NE ARG E 65 6.134 -18.897 -28.111 1.00 61.74 A N ANISOU 3518 NE ARG E 65 9109 7217 7133 -556 1974 -259 A N ATOM 3519 CZ ARG E 65 5.299 -18.461 -27.179 1.00 66.21 A C ANISOU 3519 CZ ARG E 65 9693 8136 7328 -606 1790 -376 A C ATOM 3520 NH1 ARG E 65 4.956 -19.219 -26.150 1.00 65.18 A N1+ ANISOU 3520 NH1 ARG E 65 9318 8417 7031 -769 1670 -269 A N1+ ATOM 3521 NH2 ARG E 65 4.795 -17.235 -27.281 1.00 70.61 A N ANISOU 3521 NH2 ARG E 65 10518 8618 7691 -512 1732 -602 A N ATOM 3522 N ILE E 66 11.079 -20.785 -30.204 1.00 56.81 A N ANISOU 3522 N ILE E 66 7688 5308 8591 -188 2955 483 A N ATOM 3523 CA ILE E 66 12.389 -20.519 -29.621 1.00 63.52 A C ANISOU 3523 CA ILE E 66 8108 6134 9894 -48 2876 887 A C ATOM 3524 C ILE E 66 12.170 -19.728 -28.339 1.00 62.00 A C ANISOU 3524 C ILE E 66 7708 6502 9348 -73 2436 1166 A C ATOM 3525 O ILE E 66 11.627 -18.617 -28.372 1.00 76.61 A O ANISOU 3525 O ILE E 66 9917 8462 10728 -84 2273 954 A O ATOM 3526 CB ILE E 66 13.298 -19.753 -30.595 1.00 65.10 A C ANISOU 3526 CB ILE E 66 8639 5813 10282 34 3051 702 A C ATOM 3527 CG1 ILE E 66 13.621 -20.612 -31.820 1.00 67.07 A C ANISOU 3527 CG1 ILE E 66 9089 5518 10875 28 3575 393 A C ATOM 3528 CG2 ILE E 66 14.574 -19.310 -29.896 1.00 64.81 A C ANISOU 3528 CG2 ILE E 66 8164 5772 10691 163 2878 1152 A C ATOM 3529 CD1 ILE E 66 14.243 -19.835 -32.962 1.00 61.36 A C ANISOU 3529 CD1 ILE E 66 8903 4284 10124 -6 3757 60 A C ATOM 3530 N PHE E 67 12.585 -20.296 -27.211 1.00 71.80 A N ANISOU 3530 N PHE E 67 11293 6165 9823 89 567 1069 A N ATOM 3531 CA PHE E 67 12.379 -19.669 -25.914 1.00 62.38 A C ANISOU 3531 CA PHE E 67 10050 5102 8550 439 411 814 A C ATOM 3532 C PHE E 67 13.611 -18.850 -25.529 1.00 69.65 A C ANISOU 3532 C PHE E 67 10930 6302 9233 530 806 775 A C ATOM 3533 O PHE E 67 14.491 -18.581 -26.351 1.00 68.59 A O ANISOU 3533 O PHE E 67 10830 6190 9041 332 1128 899 A O ATOM 3534 CB PHE E 67 12.047 -20.731 -24.868 1.00 65.53 A C ANISOU 3534 CB PHE E 67 10378 5465 9054 616 234 784 A C ATOM 3535 CG PHE E 67 10.712 -21.392 -25.075 1.00 69.13 A C ANISOU 3535 CG PHE E 67 10851 5627 9788 565 -258 802 A C ATOM 3536 CD1 PHE E 67 9.538 -20.673 -24.927 1.00 64.59 A C ANISOU 3536 CD1 PHE E 67 10286 4930 9326 717 -751 578 A C ATOM 3537 CD2 PHE E 67 10.633 -22.734 -25.415 1.00 63.24 A C ANISOU 3537 CD2 PHE E 67 10089 4724 9215 363 -260 1048 A C ATOM 3538 CE1 PHE E 67 8.309 -21.277 -25.114 1.00 66.64 A C ANISOU 3538 CE1 PHE E 67 10547 4865 9909 656 -1273 619 A C ATOM 3539 CE2 PHE E 67 9.406 -23.343 -25.604 1.00 73.66 A C ANISOU 3539 CE2 PHE E 67 11400 5763 10823 284 -748 1121 A C ATOM 3540 CZ PHE E 67 8.243 -22.614 -25.454 1.00 67.28 A C ANISOU 3540 CZ PHE E 67 10610 4785 10169 424 -1273 918 A C ATOM 3541 N GLY E 68 13.682 -18.441 -24.264 1.00 65.20 A N ANISOU 3541 N GLY E 68 10266 5975 8531 831 758 609 A N ATOM 3542 CA GLY E 68 14.808 -17.673 -23.769 1.00 65.88 A C ANISOU 3542 CA GLY E 68 10269 6365 8398 905 1086 634 A C ATOM 3543 C GLY E 68 14.548 -16.180 -23.752 1.00 72.91 A C ANISOU 3543 C GLY E 68 11130 7448 9124 1021 1003 451 A C ATOM 3544 O GLY E 68 13.947 -15.642 -24.687 1.00 65.26 A O ANISOU 3544 O GLY E 68 10262 6306 8229 906 856 388 A O ATOM 3545 N HIS E 69 14.999 -15.496 -22.698 1.00 76.90 A N ANISOU 3545 N HIS E 69 11478 8345 9395 1241 1092 384 A N ATOM 3546 CA HIS E 69 14.794 -14.056 -22.589 1.00 73.82 A C ANISOU 3546 CA HIS E 69 11015 8218 8815 1373 1028 205 A C ATOM 3547 C HIS E 69 15.890 -13.382 -21.770 1.00 72.26 A C ANISOU 3547 C HIS E 69 10627 8472 8356 1445 1317 333 A C ATOM 3548 O HIS E 69 16.134 -12.182 -21.929 1.00 82.26 A O ANISOU 3548 O HIS E 69 11831 9947 9477 1444 1395 306 A O ATOM 3549 CB HIS E 69 13.420 -13.754 -21.985 1.00 63.45 A C ANISOU 3549 CB HIS E 69 9641 6991 7475 1691 564 -171 A C ATOM 3550 CG HIS E 69 13.189 -14.390 -20.650 1.00 65.02 A C ANISOU 3550 CG HIS E 69 9688 7439 7577 1986 426 -294 A C ATOM 3551 CD2 HIS E 69 13.343 -13.909 -19.393 1.00 66.88 A C ANISOU 3551 CD2 HIS E 69 9688 8219 7504 2293 429 -438 A C ATOM 3552 ND1 HIS E 69 12.729 -15.682 -20.511 1.00 68.13 A N ANISOU 3552 ND1 HIS E 69 10147 7551 8187 1985 250 -274 A N ATOM 3553 CE1 HIS E 69 12.615 -15.971 -19.227 1.00 71.09 A C ANISOU 3553 CE1 HIS E 69 10353 8251 8407 2289 145 -421 A C ATOM 3554 NE2 HIS E 69 12.981 -14.913 -18.528 1.00 67.93 A N ANISOU 3554 NE2 HIS E 69 9761 8380 7669 2484 255 -523 A N ATOM 3555 N GLU E 70 16.545 -14.131 -20.885 1.00 71.53 A N ANISOU 3555 N GLU E 70 10426 8543 8210 1496 1458 501 A N ATOM 3556 CA GLU E 70 17.699 -13.626 -20.146 1.00 73.66 A C ANISOU 3556 CA GLU E 70 10498 9218 8274 1496 1726 735 A C ATOM 3557 C GLU E 70 18.942 -13.863 -20.992 1.00 82.29 A C ANISOU 3557 C GLU E 70 11682 10017 9568 1163 2034 1059 A C ATOM 3558 O GLU E 70 19.342 -15.012 -21.204 1.00 72.80 A O ANISOU 3558 O GLU E 70 10563 8528 8570 1040 2119 1195 A O ATOM 3559 CB GLU E 70 17.838 -14.312 -18.789 1.00 76.63 A C ANISOU 3559 CB GLU E 70 10695 9918 8503 1698 1702 789 A C ATOM 3560 CG GLU E 70 16.540 -14.675 -18.097 1.00 79.96 A C ANISOU 3560 CG GLU E 70 11082 10445 8855 2024 1341 425 A C ATOM 3561 CD GLU E 70 16.722 -14.843 -16.599 1.00 84.48 A C ANISOU 3561 CD GLU E 70 11393 11571 9136 2288 1327 433 A C ATOM 3562 OE1 GLU E 70 17.870 -14.720 -16.121 1.00 86.06 A O ANISOU 3562 OE1 GLU E 70 11442 12057 9202 2178 1601 782 A O ATOM 3563 OE2 GLU E 70 15.725 -15.112 -15.900 1.00103.67 A O1- ANISOU 3563 OE2 GLU E 70 13754 14153 11484 2603 1015 99 A O1- ATOM 3564 N ALA E 71 19.558 -12.786 -21.470 1.00 78.92 A N ANISOU 3564 N ALA E 71 11223 9665 9097 1033 2180 1158 A N ATOM 3565 CA ALA E 71 20.720 -12.933 -22.333 1.00 76.73 A C ANISOU 3565 CA ALA E 71 11023 9086 9044 744 2418 1404 A C ATOM 3566 C ALA E 71 21.507 -11.632 -22.370 1.00 76.65 A C ANISOU 3566 C ALA E 71 10884 9298 8942 659 2546 1558 A C ATOM 3567 O ALA E 71 21.066 -10.593 -21.874 1.00 80.17 A O ANISOU 3567 O ALA E 71 11194 10132 9133 807 2467 1461 A O ATOM 3568 CB ALA E 71 20.316 -13.347 -23.750 1.00 66.02 A C ANISOU 3568 CB ALA E 71 9909 7272 7905 577 2394 1274 A C ATOM 3569 N GLY E 72 22.693 -11.720 -22.964 1.00 76.36 A N ANISOU 3569 N GLY E 72 10869 9012 9132 426 2722 1789 A N ATOM 3570 CA GLY E 72 23.517 -10.573 -23.281 1.00 69.76 A C ANISOU 3570 CA GLY E 72 9944 8247 8315 287 2820 1951 A C ATOM 3571 C GLY E 72 24.179 -10.779 -24.627 1.00 71.10 A C ANISOU 3571 C GLY E 72 10281 7939 8795 64 2912 1945 A C ATOM 3572 O GLY E 72 24.656 -11.880 -24.920 1.00 73.14 A O ANISOU 3572 O GLY E 72 10609 7903 9277 -11 2963 1983 A O ATOM 3573 N GLY E 73 24.208 -9.746 -25.460 1.00 69.28 A N ANISOU 3573 N GLY E 73 10103 7651 8571 -26 2924 1868 A N ATOM 3574 CA GLY E 73 24.722 -9.916 -26.799 1.00 67.83 A C ANISOU 3574 CA GLY E 73 10070 7062 8639 -204 2989 1795 A C ATOM 3575 C GLY E 73 25.229 -8.619 -27.387 1.00 70.51 A C ANISOU 3575 C GLY E 73 10377 7396 9016 -316 3016 1831 A C ATOM 3576 O GLY E 73 25.378 -7.611 -26.692 1.00 74.10 A O ANISOU 3576 O GLY E 73 10661 8162 9330 -286 3003 1982 A O ATOM 3577 N ILE E 74 25.494 -8.663 -28.691 1.00 62.16 A N ANISOU 3577 N ILE E 74 9465 6016 8135 -442 3049 1687 A N ATOM 3578 CA ILE E 74 26.054 -7.540 -29.432 1.00 70.48 A C ANISOU 3578 CA ILE E 74 10511 6989 9279 -559 3062 1688 A C ATOM 3579 C ILE E 74 25.186 -7.288 -30.657 1.00 64.96 A C ANISOU 3579 C ILE E 74 10012 6179 8492 -585 3030 1398 A C ATOM 3580 O ILE E 74 24.788 -8.228 -31.352 1.00 78.56 A O ANISOU 3580 O ILE E 74 11869 7741 10239 -604 3036 1243 A O ATOM 3581 CB ILE E 74 27.520 -7.806 -29.837 1.00 69.99 A C ANISOU 3581 CB ILE E 74 10385 6630 9580 -692 3100 1810 A C ATOM 3582 CG1 ILE E 74 28.384 -8.022 -28.591 1.00 62.15 A C ANISOU 3582 CG1 ILE E 74 9174 5736 8703 -698 3087 2165 A C ATOM 3583 CG2 ILE E 74 28.066 -6.655 -30.665 1.00 72.68 A C ANISOU 3583 CG2 ILE E 74 10721 6854 10041 -805 3079 1781 A C ATOM 3584 CD1 ILE E 74 29.789 -8.503 -28.885 1.00 85.88 A C ANISOU 3584 CD1 ILE E 74 12108 8384 12137 -809 3053 2279 A C ATOM 3585 N VAL E 75 24.895 -6.013 -30.919 1.00 65.31 A N ANISOU 3585 N VAL E 75 10054 6333 8426 -597 2986 1349 A N ATOM 3586 CA VAL E 75 23.988 -5.646 -32.001 1.00 70.79 A C ANISOU 3586 CA VAL E 75 10926 6950 9022 -625 2921 1104 A C ATOM 3587 C VAL E 75 24.657 -5.900 -33.345 1.00 69.04 A C ANISOU 3587 C VAL E 75 10800 6446 8985 -771 2986 1001 A C ATOM 3588 O VAL E 75 25.826 -5.550 -33.555 1.00 77.99 A O ANISOU 3588 O VAL E 75 11852 7455 10325 -846 3036 1076 A O ATOM 3589 CB VAL E 75 23.555 -4.179 -31.862 1.00 68.63 A C ANISOU 3589 CB VAL E 75 10603 6879 8593 -585 2846 1072 A C ATOM 3590 CG1 VAL E 75 22.708 -3.752 -33.051 1.00 68.16 A C ANISOU 3590 CG1 VAL E 75 10727 6700 8472 -637 2754 842 A C ATOM 3591 CG2 VAL E 75 22.791 -3.977 -30.565 1.00 63.31 A C ANISOU 3591 CG2 VAL E 75 9806 6556 7693 -393 2760 1092 A C ATOM 3592 N GLU E 76 23.912 -6.511 -34.266 1.00 69.70 A N ANISOU 3592 N GLU E 76 11034 6451 8998 -810 2959 830 A N ATOM 3593 CA GLU E 76 24.375 -6.768 -35.624 1.00 67.56 A C ANISOU 3593 CA GLU E 76 10832 6020 8816 -926 3015 687 A C ATOM 3594 C GLU E 76 23.899 -5.709 -36.610 1.00 73.59 A C ANISOU 3594 C GLU E 76 11693 6791 9476 -999 2950 559 A C ATOM 3595 O GLU E 76 24.698 -5.186 -37.394 1.00 74.55 A O ANISOU 3595 O GLU E 76 11804 6814 9707 -1066 2989 477 A O ATOM 3596 CB GLU E 76 23.914 -8.160 -36.076 1.00 77.60 A C ANISOU 3596 CB GLU E 76 12162 7282 10042 -949 3037 622 A C ATOM 3597 CG GLU E 76 24.314 -8.529 -37.494 1.00 72.27 A C ANISOU 3597 CG GLU E 76 11515 6561 9385 -1048 3101 450 A C ATOM 3598 CD GLU E 76 23.188 -8.335 -38.487 1.00 75.08 A C ANISOU 3598 CD GLU E 76 11984 7018 9524 -1149 3018 382 A C ATOM 3599 OE1 GLU E 76 22.055 -8.040 -38.051 1.00 88.06 A O ANISOU 3599 OE1 GLU E 76 13697 8708 11054 -1137 2879 459 A O ATOM 3600 OE2 GLU E 76 23.433 -8.481 -39.702 1.00 85.16 A O1- ANISOU 3600 OE2 GLU E 76 13264 8342 10749 -1235 3065 246 A O1- ATOM 3601 N SER E 77 22.608 -5.385 -36.590 1.00 73.44 A N ANISOU 3601 N SER E 77 11762 6870 9273 -980 2818 527 A N ATOM 3602 CA SER E 77 22.070 -4.291 -37.387 1.00 75.03 A C ANISOU 3602 CA SER E 77 12049 7078 9382 -1040 2720 425 A C ATOM 3603 C SER E 77 20.804 -3.786 -36.713 1.00 76.80 A C ANISOU 3603 C SER E 77 12300 7410 9472 -940 2528 417 A C ATOM 3604 O SER E 77 20.236 -4.444 -35.838 1.00 81.98 A O ANISOU 3604 O SER E 77 12928 8127 10093 -835 2457 460 A O ATOM 3605 CB SER E 77 21.779 -4.717 -38.831 1.00 78.56 A C ANISOU 3605 CB SER E 77 12600 7483 9767 -1183 2712 321 A C ATOM 3606 OG SER E 77 21.323 -6.056 -38.898 1.00 95.39 A O ANISOU 3606 OG SER E 77 14744 9644 11855 -1211 2713 366 A O ATOM 3607 N VAL E 78 20.366 -2.602 -37.128 1.00 64.68 A N ANISOU 3607 N VAL E 78 10808 5893 7875 -954 2417 330 A N ATOM 3608 CA VAL E 78 19.149 -1.999 -36.604 1.00 67.74 A C ANISOU 3608 CA VAL E 78 11207 6370 8160 -835 2183 253 A C ATOM 3609 C VAL E 78 18.220 -1.677 -37.765 1.00 75.84 A C ANISOU 3609 C VAL E 78 12379 7285 9149 -954 1992 163 A C ATOM 3610 O VAL E 78 18.661 -1.365 -38.877 1.00 71.01 A O ANISOU 3610 O VAL E 78 11830 6605 8545 -1104 2069 146 A O ATOM 3611 CB VAL E 78 19.437 -0.736 -35.757 1.00 77.77 A C ANISOU 3611 CB VAL E 78 12337 7830 9382 -702 2189 236 A C ATOM 3612 CG1 VAL E 78 20.545 -1.006 -34.749 1.00 77.49 A C ANISOU 3612 CG1 VAL E 78 12131 7922 9392 -648 2386 407 A C ATOM 3613 CG2 VAL E 78 19.793 0.452 -36.642 1.00 76.09 A C ANISOU 3613 CG2 VAL E 78 12157 7567 9188 -804 2206 180 A C ATOM 3614 N GLY E 79 16.920 -1.777 -37.503 1.00 84.14 A N ANISOU 3614 N GLY E 79 13474 8318 10177 -883 1707 108 A N ATOM 3615 CA GLY E 79 15.922 -1.454 -38.496 1.00 71.47 A C ANISOU 3615 CA GLY E 79 11991 6593 8572 -1004 1452 67 A C ATOM 3616 C GLY E 79 15.735 0.041 -38.651 1.00 87.97 A C ANISOU 3616 C GLY E 79 14081 8708 10635 -949 1340 -75 A C ATOM 3617 O GLY E 79 16.412 0.860 -38.029 1.00 89.16 A O ANISOU 3617 O GLY E 79 14124 8999 10754 -829 1479 -130 A O ATOM 3618 N GLU E 80 14.782 0.397 -39.507 1.00 85.62 A N ANISOU 3618 N GLU E 80 13890 8285 10358 -1053 1066 -108 A N ATOM 3619 CA GLU E 80 14.501 1.800 -39.778 1.00 85.00 A C ANISOU 3619 CA GLU E 80 13822 8204 10269 -1012 922 -254 A C ATOM 3620 C GLU E 80 13.901 2.467 -38.545 1.00 84.64 A C ANISOU 3620 C GLU E 80 13660 8274 10225 -723 719 -450 A C ATOM 3621 O GLU E 80 12.989 1.926 -37.913 1.00 77.30 A O ANISOU 3621 O GLU E 80 12711 7305 9354 -593 456 -511 A O ATOM 3622 CB GLU E 80 13.558 1.919 -40.975 1.00 84.84 A C ANISOU 3622 CB GLU E 80 13936 8011 10287 -1205 632 -214 A C ATOM 3623 CG GLU E 80 12.655 3.140 -40.969 1.00 94.76 A C ANISOU 3623 CG GLU E 80 15205 9199 11599 -1103 285 -396 A C ATOM 3624 CD GLU E 80 11.542 3.036 -41.994 1.00102.76 A C ANISOU 3624 CD GLU E 80 16337 10004 12702 -1301 -94 -299 A C ATOM 3625 OE1 GLU E 80 11.841 2.708 -43.161 1.00105.87 A O ANISOU 3625 OE1 GLU E 80 16808 10394 13026 -1567 26 -115 A O ATOM 3626 OE2 GLU E 80 10.372 3.285 -41.639 1.00101.23 A O1- ANISOU 3626 OE2 GLU E 80 16140 9668 12654 -1190 -536 -407 A O1- ATOM 3627 N GLY E 81 14.430 3.639 -38.194 1.00 81.01 A N ANISOU 3627 N GLY E 81 13096 7987 9698 -611 830 -558 A N ATOM 3628 CA GLY E 81 13.950 4.409 -37.071 1.00 85.83 A C ANISOU 3628 CA GLY E 81 13542 8819 10249 -320 666 -772 A C ATOM 3629 C GLY E 81 14.730 4.220 -35.787 1.00 84.58 A C ANISOU 3629 C GLY E 81 13183 8978 9977 -154 915 -723 A C ATOM 3630 O GLY E 81 14.601 5.046 -34.876 1.00 84.23 A O ANISOU 3630 O GLY E 81 12944 9247 9815 79 860 -879 A O ATOM 3631 N VAL E 82 15.529 3.160 -35.685 1.00 76.28 A N ANISOU 3631 N VAL E 82 12149 7889 8946 -263 1175 -507 A N ATOM 3632 CA VAL E 82 16.304 2.912 -34.473 1.00 67.92 A C ANISOU 3632 CA VAL E 82 10894 7118 7795 -135 1395 -406 A C ATOM 3633 C VAL E 82 17.439 3.930 -34.418 1.00 88.79 A C ANISOU 3633 C VAL E 82 13398 9947 10392 -192 1636 -292 A C ATOM 3634 O VAL E 82 18.362 3.889 -35.236 1.00 87.21 A O ANISOU 3634 O VAL E 82 13276 9559 10300 -408 1827 -141 A O ATOM 3635 CB VAL E 82 16.843 1.478 -34.427 1.00 85.84 A C ANISOU 3635 CB VAL E 82 13223 9255 10137 -243 1573 -209 A C ATOM 3636 CG1 VAL E 82 17.802 1.314 -33.256 1.00 77.66 A C ANISOU 3636 CG1 VAL E 82 11979 8501 9028 -150 1804 -53 A C ATOM 3637 CG2 VAL E 82 15.701 0.483 -34.330 1.00 74.09 A C ANISOU 3637 CG2 VAL E 82 11831 7620 8700 -180 1313 -292 A C ATOM 3638 N THR E 83 17.371 4.848 -33.454 1.00 90.56 A N ANISOU 3638 N THR E 83 13389 10562 10459 6 1605 -370 A N ATOM 3639 CA THR E 83 18.398 5.860 -33.270 1.00 90.18 A C ANISOU 3639 CA THR E 83 13155 10747 10364 -55 1803 -212 A C ATOM 3640 C THR E 83 19.122 5.756 -31.936 1.00 91.04 A C ANISOU 3640 C THR E 83 12976 11280 10336 39 1974 -2 A C ATOM 3641 O THR E 83 20.176 6.383 -31.776 1.00 85.54 A O ANISOU 3641 O THR E 83 12109 10740 9652 -77 2150 245 A O ATOM 3642 CB THR E 83 17.795 7.269 -33.401 1.00 81.05 A C ANISOU 3642 CB THR E 83 11914 9770 9109 57 1633 -436 A C ATOM 3643 CG2 THR E 83 16.847 7.554 -32.243 1.00 77.62 A C ANISOU 3643 CG2 THR E 83 11270 9764 8459 395 1430 -690 A C ATOM 3644 OG1 THR E 83 18.845 8.243 -33.406 1.00108.32 A O ANISOU 3644 OG1 THR E 83 15201 13400 12556 -57 1822 -239 A O ATOM 3645 N ASP E 84 18.599 4.989 -30.983 1.00 89.23 A N ANISOU 3645 N ASP E 84 12673 11243 9989 233 1905 -69 A N ATOM 3646 CA ASP E 84 19.224 4.822 -29.680 1.00 82.74 A C ANISOU 3646 CA ASP E 84 11563 10872 9001 326 2053 145 A C ATOM 3647 C ASP E 84 20.141 3.606 -29.617 1.00 75.11 A C ANISOU 3647 C ASP E 84 10666 9673 8199 157 2242 445 A C ATOM 3648 O ASP E 84 20.660 3.292 -28.541 1.00 76.45 A O ANISOU 3648 O ASP E 84 10615 10175 8257 213 2347 659 A O ATOM 3649 CB ASP E 84 18.150 4.724 -28.594 1.00 90.84 A C ANISOU 3649 CB ASP E 84 12431 12304 9780 673 1852 -137 A C ATOM 3650 CG ASP E 84 17.172 3.593 -28.842 1.00 88.47 A C ANISOU 3650 CG ASP E 84 12375 11634 9604 752 1643 -355 A C ATOM 3651 OD1 ASP E 84 16.712 3.444 -29.994 1.00 92.57 A O ANISOU 3651 OD1 ASP E 84 13170 11677 10326 616 1522 -455 A O ATOM 3652 OD2 ASP E 84 16.859 2.855 -27.885 1.00 78.67 A O1- ANISOU 3652 OD2 ASP E 84 11035 10599 8257 940 1586 -406 A O1- ATOM 3653 N LEU E 85 20.349 2.919 -30.739 1.00 70.60 A N ANISOU 3653 N LEU E 85 10373 8576 7875 -40 2276 460 A N ATOM 3654 CA LEU E 85 21.217 1.751 -30.781 1.00 75.54 A C ANISOU 3654 CA LEU E 85 11062 8962 8677 -184 2435 689 A C ATOM 3655 C LEU E 85 21.923 1.712 -32.128 1.00 83.90 A C ANISOU 3655 C LEU E 85 12305 9586 9985 -427 2518 733 A C ATOM 3656 O LEU E 85 21.463 2.300 -33.110 1.00 69.40 A O ANISOU 3656 O LEU E 85 10614 7588 8168 -480 2431 555 A O ATOM 3657 CB LEU E 85 20.433 0.455 -30.547 1.00 70.74 A C ANISOU 3657 CB LEU E 85 10580 8237 8059 -78 2344 568 A C ATOM 3658 CG LEU E 85 19.965 0.193 -29.114 1.00 73.06 A C ANISOU 3658 CG LEU E 85 10675 8944 8139 172 2276 542 A C ATOM 3659 CD1 LEU E 85 18.712 -0.665 -29.111 1.00 67.46 A C ANISOU 3659 CD1 LEU E 85 10119 8086 7428 317 2053 286 A C ATOM 3660 CD2 LEU E 85 21.072 -0.454 -28.299 1.00 73.52 A C ANISOU 3660 CD2 LEU E 85 10575 9131 8228 112 2471 874 A C ATOM 3661 N GLN E 86 23.049 1.006 -32.164 1.00 71.69 A N ANISOU 3661 N GLN E 86 10326 6826 10086 -1141 -92 -160 A N ATOM 3662 CA GLN E 86 23.864 0.910 -33.366 1.00 78.04 A C ANISOU 3662 CA GLN E 86 11399 7408 10844 -1172 -415 -445 A C ATOM 3663 C GLN E 86 24.705 -0.356 -33.275 1.00 74.25 A C ANISOU 3663 C GLN E 86 10994 6966 10251 -1177 -158 -596 A C ATOM 3664 O GLN E 86 24.944 -0.865 -32.173 1.00 77.84 A O ANISOU 3664 O GLN E 86 11186 7542 10846 -1163 162 -442 A O ATOM 3665 CB GLN E 86 24.754 2.153 -33.535 1.00 77.83 A C ANISOU 3665 CB GLN E 86 11079 7085 11408 -1215 -860 -418 A C ATOM 3666 CG GLN E 86 25.505 2.562 -32.283 1.00 81.83 A C ANISOU 3666 CG GLN E 86 11043 7551 12498 -1269 -690 -135 A C ATOM 3667 CD GLN E 86 26.570 3.601 -32.566 1.00 94.47 A C ANISOU 3667 CD GLN E 86 12361 8803 14729 -1359 -1111 -147 A C ATOM 3668 NE2 GLN E 86 26.146 4.848 -32.737 1.00104.38 A N ANISOU 3668 NE2 GLN E 86 13395 9963 16304 -1372 -1412 -79 A N ATOM 3669 OE1 GLN E 86 27.757 3.289 -32.635 1.00108.54 A O ANISOU 3669 OE1 GLN E 86 14111 10386 16743 -1412 -1186 -233 A O ATOM 3670 N PRO E 87 25.155 -0.894 -34.411 1.00 75.80 A N ANISOU 3670 N PRO E 87 11566 7058 10175 -1164 -299 -910 A N ATOM 3671 CA PRO E 87 25.917 -2.150 -34.382 1.00 77.17 A C ANISOU 3671 CA PRO E 87 11805 7281 10235 -1139 -47 -1096 A C ATOM 3672 C PRO E 87 27.165 -2.042 -33.518 1.00 80.11 A C ANISOU 3672 C PRO E 87 11788 7508 11142 -1144 -81 -990 A C ATOM 3673 O PRO E 87 27.894 -1.049 -33.563 1.00 71.68 A O ANISOU 3673 O PRO E 87 10535 6179 10522 -1189 -431 -923 A O ATOM 3674 CB PRO E 87 26.270 -2.383 -35.855 1.00 72.40 A C ANISOU 3674 CB PRO E 87 11671 6533 9306 -1097 -286 -1450 A C ATOM 3675 CG PRO E 87 25.216 -1.656 -36.613 1.00 78.48 A C ANISOU 3675 CG PRO E 87 12751 7289 9780 -1095 -501 -1432 A C ATOM 3676 CD PRO E 87 24.887 -0.446 -35.790 1.00 79.48 A C ANISOU 3676 CD PRO E 87 12466 7375 10357 -1135 -677 -1126 A C ATOM 3677 N GLY E 88 27.407 -3.089 -32.731 1.00 86.65 A N ANISOU 3677 N GLY E 88 12499 8485 11937 -1097 273 -979 A N ATOM 3678 CA GLY E 88 28.512 -3.132 -31.800 1.00 67.87 A C ANISOU 3678 CA GLY E 88 9816 5977 9996 -1075 289 -849 A C ATOM 3679 C GLY E 88 28.125 -2.893 -30.358 1.00 80.26 A C ANISOU 3679 C GLY E 88 11066 7680 11747 -1056 544 -479 A C ATOM 3680 O GLY E 88 28.934 -3.170 -29.461 1.00 79.37 A O ANISOU 3680 O GLY E 88 10772 7498 11889 -1004 644 -355 A O ATOM 3681 N ASP E 89 26.915 -2.397 -30.110 1.00 64.22 A N ANISOU 3681 N ASP E 89 9004 5828 9567 -1071 645 -305 A N ATOM 3682 CA ASP E 89 26.480 -2.106 -28.753 1.00 63.59 A C ANISOU 3682 CA ASP E 89 8658 5886 9617 -1016 888 34 A C ATOM 3683 C ASP E 89 26.294 -3.393 -27.959 1.00 67.98 A C ANISOU 3683 C ASP E 89 9245 6649 9935 -893 1211 -10 A C ATOM 3684 O ASP E 89 25.687 -4.353 -28.443 1.00 77.55 A O ANISOU 3684 O ASP E 89 10662 8021 10783 -881 1331 -253 A O ATOM 3685 CB ASP E 89 25.173 -1.314 -28.777 1.00 74.53 A C ANISOU 3685 CB ASP E 89 10038 7410 10872 -1028 886 173 A C ATOM 3686 CG ASP E 89 25.379 0.146 -29.130 1.00 83.59 A C ANISOU 3686 CG ASP E 89 11004 8353 12403 -1111 573 296 A C ATOM 3687 OD1 ASP E 89 26.543 0.597 -29.150 1.00 77.07 A O ANISOU 3687 OD1 ASP E 89 10002 7274 12006 -1178 399 333 A O ATOM 3688 OD2 ASP E 89 24.374 0.842 -29.386 1.00 88.83 A O1- ANISOU 3688 OD2 ASP E 89 11689 9088 12972 -1106 480 344 A O1- ATOM 3689 N HIS E 90 26.830 -3.413 -26.741 1.00 67.08 A N ANISOU 3689 N HIS E 90 8933 6514 10040 -798 1350 223 A N ATOM 3690 CA HIS E 90 26.540 -4.482 -25.797 1.00 67.04 A C ANISOU 3690 CA HIS E 90 8939 6700 9832 -636 1604 211 A C ATOM 3691 C HIS E 90 25.150 -4.259 -25.219 1.00 65.30 A C ANISOU 3691 C HIS E 90 8705 6720 9386 -579 1773 362 A C ATOM 3692 O HIS E 90 24.863 -3.190 -24.674 1.00 71.63 A O ANISOU 3692 O HIS E 90 9365 7519 10333 -567 1797 659 A O ATOM 3693 CB HIS E 90 27.579 -4.513 -24.678 1.00 64.81 A C ANISOU 3693 CB HIS E 90 8529 6284 9814 -516 1661 428 A C ATOM 3694 CG HIS E 90 28.948 -4.917 -25.128 1.00 76.17 A C ANISOU 3694 CG HIS E 90 10005 7470 11464 -535 1487 257 A C ATOM 3695 CD2 HIS E 90 29.913 -5.634 -24.506 1.00 79.76 A C ANISOU 3695 CD2 HIS E 90 10474 7809 12024 -395 1495 237 A C ATOM 3696 ND1 HIS E 90 29.460 -4.576 -26.361 1.00 83.41 A N ANISOU 3696 ND1 HIS E 90 10986 8202 12504 -685 1235 59 A N ATOM 3697 CE1 HIS E 90 30.681 -5.065 -26.479 1.00 72.05 A C ANISOU 3697 CE1 HIS E 90 9585 6545 11245 -642 1106 -80 A C ATOM 3698 NE2 HIS E 90 30.980 -5.712 -25.367 1.00 64.71 A N ANISOU 3698 NE2 HIS E 90 8622 5650 10316 -470 1261 29 A N ATOM 3699 N VAL E 91 24.282 -5.260 -25.347 1.00 61.28 A N ANISOU 3699 N VAL E 91 8329 6405 8550 -544 1896 147 A N ATOM 3700 CA VAL E 91 22.870 -5.082 -25.035 1.00 72.24 A C ANISOU 3700 CA VAL E 91 9755 7983 9709 -514 2002 231 A C ATOM 3701 C VAL E 91 22.331 -6.279 -24.268 1.00 66.44 A C ANISOU 3701 C VAL E 91 9039 7421 8784 -375 2173 111 A C ATOM 3702 O VAL E 91 22.771 -7.418 -24.451 1.00 63.78 A O ANISOU 3702 O VAL E 91 8721 7091 8423 -361 2210 -149 A O ATOM 3703 CB VAL E 91 22.034 -4.852 -26.312 1.00 71.74 A C ANISOU 3703 CB VAL E 91 9890 7932 9437 -680 1911 83 A C ATOM 3704 CG1 VAL E 91 22.440 -3.553 -26.991 1.00 57.54 A C ANISOU 3704 CG1 VAL E 91 8063 5954 7847 -778 1665 193 A C ATOM 3705 CG2 VAL E 91 22.179 -6.028 -27.265 1.00 60.69 A C ANISOU 3705 CG2 VAL E 91 8673 6542 7845 -769 1964 -266 A C ATOM 3706 N LEU E 92 21.358 -6.001 -23.402 1.00 64.53 A N ANISOU 3706 N LEU E 92 8777 7312 8429 -254 2257 278 A N ATOM 3707 CA LEU E 92 20.589 -7.023 -22.712 1.00 72.12 A C ANISOU 3707 CA LEU E 92 9770 8424 9209 -124 2359 145 A C ATOM 3708 C LEU E 92 19.166 -7.012 -23.244 1.00 70.57 A C ANISOU 3708 C LEU E 92 9702 8318 8792 -236 2382 68 A C ATOM 3709 O LEU E 92 18.515 -5.955 -23.227 1.00 75.12 A O ANISOU 3709 O LEU E 92 10309 8905 9329 -234 2339 268 A O ATOM 3710 CB LEU E 92 20.590 -6.787 -21.200 1.00 60.49 A C ANISOU 3710 CB LEU E 92 8234 7007 7744 155 2411 380 A C ATOM 3711 CG LEU E 92 21.939 -6.745 -20.481 1.00 68.51 A C ANISOU 3711 CG LEU E 92 9180 7904 8945 298 2411 528 A C ATOM 3712 CD1 LEU E 92 21.739 -6.532 -18.988 1.00 63.28 A C ANISOU 3712 CD1 LEU E 92 8545 7312 8185 603 2501 770 A C ATOM 3713 CD2 LEU E 92 22.729 -8.014 -20.744 1.00 70.46 A C ANISOU 3713 CD2 LEU E 92 9427 8094 9250 306 2350 223 A C ATOM 3714 N PRO E 93 18.659 -8.129 -23.759 1.00 68.44 A N ANISOU 3714 N PRO E 93 9506 8097 8400 -343 2454 -214 A N ATOM 3715 CA PRO E 93 17.228 -8.202 -24.072 1.00 56.91 A C ANISOU 3715 CA PRO E 93 8190 6694 6738 -440 2494 -256 A C ATOM 3716 C PRO E 93 16.413 -8.371 -22.801 1.00 68.04 A C ANISOU 3716 C PRO E 93 9551 8198 8102 -227 2494 -194 A C ATOM 3717 O PRO E 93 16.760 -9.158 -21.918 1.00 78.68 A O ANISOU 3717 O PRO E 93 10783 9588 9522 -54 2500 -291 A O ATOM 3718 CB PRO E 93 17.118 -9.437 -24.978 1.00 68.34 A C ANISOU 3718 CB PRO E 93 9696 8143 8127 -636 2630 -572 A C ATOM 3719 CG PRO E 93 18.522 -9.726 -25.426 1.00 53.21 A C ANISOU 3719 CG PRO E 93 7701 6166 6351 -650 2625 -692 A C ATOM 3720 CD PRO E 93 19.402 -9.274 -24.307 1.00 65.27 A C ANISOU 3720 CD PRO E 93 9067 7672 8062 -419 2514 -509 A C ATOM 3721 N ILE E 94 15.325 -7.613 -22.711 1.00 72.12 A N ANISOU 3721 N ILE E 94 10180 8734 8489 -207 2450 -49 A N ATOM 3722 CA ILE E 94 14.423 -7.659 -21.568 1.00 66.95 A C ANISOU 3722 CA ILE E 94 9529 8156 7753 18 2421 -1 A C ATOM 3723 C ILE E 94 13.114 -8.294 -22.011 1.00 66.24 A C ANISOU 3723 C ILE E 94 9583 8045 7539 -136 2429 -176 A C ATOM 3724 O ILE E 94 12.656 -8.076 -23.139 1.00 69.63 A O ANISOU 3724 O ILE E 94 10177 8403 7878 -376 2449 -187 A O ATOM 3725 CB ILE E 94 14.182 -6.256 -20.975 1.00 57.99 A C ANISOU 3725 CB ILE E 94 8393 7052 6588 208 2373 301 A C ATOM 3726 CG1 ILE E 94 15.434 -5.384 -21.110 1.00 65.05 A C ANISOU 3726 CG1 ILE E 94 9151 7901 7665 202 2389 500 A C ATOM 3727 CG2 ILE E 94 13.765 -6.363 -19.516 1.00 54.67 A C ANISOU 3727 CG2 ILE E 94 7961 6724 6085 546 2370 357 A C ATOM 3728 CD1 ILE E 94 16.597 -5.827 -20.250 1.00 59.71 A C ANISOU 3728 CD1 ILE E 94 8353 7229 7105 365 2451 536 A C ATOM 3729 N PHE E 95 12.515 -9.089 -21.120 1.00 66.27 A N ANISOU 3729 N PHE E 95 9550 8086 7542 7 2397 -312 A N ATOM 3730 CA PHE E 95 11.243 -9.732 -21.434 1.00 72.00 A C ANISOU 3730 CA PHE E 95 10389 8754 8213 -151 2398 -476 A C ATOM 3731 C PHE E 95 10.114 -8.718 -21.550 1.00 76.68 A C ANISOU 3731 C PHE E 95 11196 9302 8635 -130 2307 -299 A C ATOM 3732 O PHE E 95 9.141 -8.954 -22.275 1.00 70.37 A O ANISOU 3732 O PHE E 95 10576 8399 7763 -352 2324 -364 A O ATOM 3733 CB PHE E 95 10.907 -10.777 -20.370 1.00 58.31 A C ANISOU 3733 CB PHE E 95 8537 7043 6576 26 2315 -689 A C ATOM 3734 CG PHE E 95 10.533 -10.188 -19.039 1.00 64.88 A C ANISOU 3734 CG PHE E 95 9422 7931 7299 416 2152 -561 A C ATOM 3735 CD1 PHE E 95 11.508 -9.731 -18.168 1.00 61.97 A C ANISOU 3735 CD1 PHE E 95 8989 7647 6908 716 2138 -407 A C ATOM 3736 CD2 PHE E 95 9.203 -10.086 -18.662 1.00 70.49 A C ANISOU 3736 CD2 PHE E 95 10277 8593 7912 492 2027 -590 A C ATOM 3737 CE1 PHE E 95 11.164 -9.186 -16.944 1.00 67.86 A C ANISOU 3737 CE1 PHE E 95 9826 8454 7504 1098 2043 -278 A C ATOM 3738 CE2 PHE E 95 8.853 -9.542 -17.441 1.00 73.58 A C ANISOU 3738 CE2 PHE E 95 10748 9044 8164 891 1889 -494 A C ATOM 3739 CZ PHE E 95 9.834 -9.092 -16.581 1.00 72.83 A C ANISOU 3739 CZ PHE E 95 10599 9059 8014 1201 1917 -335 A C ATOM 3740 N THR E 96 10.217 -7.600 -20.836 1.00 72.12 A N ANISOU 3740 N THR E 96 10609 8791 8004 142 2224 -74 A N ATOM 3741 CA THR E 96 9.266 -6.503 -20.923 1.00 71.82 A C ANISOU 3741 CA THR E 96 10731 8722 7836 214 2122 89 A C ATOM 3742 C THR E 96 10.009 -5.245 -21.352 1.00 66.80 A C ANISOU 3742 C THR E 96 10030 8105 7248 222 2123 314 A C ATOM 3743 O THR E 96 11.194 -5.075 -21.051 1.00 77.41 A O ANISOU 3743 O THR E 96 11185 9505 8721 288 2196 398 A O ATOM 3744 CB THR E 96 8.548 -6.275 -19.586 1.00 71.49 A C ANISOU 3744 CB THR E 96 10706 8745 7712 578 2025 122 A C ATOM 3745 CG2 THR E 96 9.554 -6.064 -18.464 1.00 58.89 A C ANISOU 3745 CG2 THR E 96 8939 7281 6154 885 2090 236 A C ATOM 3746 OG1 THR E 96 7.696 -5.127 -19.684 1.00 72.13 A O ANISOU 3746 OG1 THR E 96 10915 8803 7687 680 1928 274 A O ATOM 3747 N GLY E 97 9.310 -4.361 -22.064 1.00 67.67 A N ANISOU 3747 N GLY E 97 10294 8138 7279 154 2014 403 A N ATOM 3748 CA GLY E 97 9.939 -3.256 -22.749 1.00 62.17 A C ANISOU 3748 CA GLY E 97 9536 7410 6673 100 1954 553 A C ATOM 3749 C GLY E 97 9.543 -1.888 -22.220 1.00 66.55 A C ANISOU 3749 C GLY E 97 10000 8010 7274 354 1858 745 A C ATOM 3750 O GLY E 97 8.775 -1.750 -21.263 1.00 70.00 A O ANISOU 3750 O GLY E 97 10447 8519 7630 609 1857 775 A O ATOM 3751 N GLU E 98 10.099 -0.870 -22.877 1.00 64.71 A N ANISOU 3751 N GLU E 98 9664 7727 7195 293 1766 854 A N ATOM 3752 CA GLU E 98 9.863 0.534 -22.540 1.00 54.94 A C ANISOU 3752 CA GLU E 98 8256 6523 6096 504 1678 1024 A C ATOM 3753 C GLU E 98 9.740 1.289 -23.859 1.00 61.71 A C ANISOU 3753 C GLU E 98 9224 7224 7000 345 1414 999 A C ATOM 3754 O GLU E 98 10.745 1.544 -24.530 1.00 66.75 A O ANISOU 3754 O GLU E 98 9753 7791 7817 188 1358 1004 A O ATOM 3755 CB GLU E 98 10.990 1.089 -21.675 1.00 58.77 A C ANISOU 3755 CB GLU E 98 8371 7112 6846 639 1862 1210 A C ATOM 3756 CG GLU E 98 10.872 2.568 -21.340 1.00 57.26 A C ANISOU 3756 CG GLU E 98 7914 6961 6880 831 1839 1391 A C ATOM 3757 CD GLU E 98 11.951 3.030 -20.378 1.00 70.99 A C ANISOU 3757 CD GLU E 98 9305 8794 8876 950 2111 1612 A C ATOM 3758 OE1 GLU E 98 12.650 2.164 -19.810 1.00 67.92 A O ANISOU 3758 OE1 GLU E 98 8942 8443 8419 946 2293 1627 A O ATOM 3759 OE2 GLU E 98 12.103 4.255 -20.189 1.00 75.34 A O1- ANISOU 3759 OE2 GLU E 98 9552 9363 9710 1048 2147 1773 A O1- ATOM 3760 N CYS E 99 8.505 1.634 -24.233 1.00 59.88 A N ANISOU 3760 N CYS E 99 9240 6911 6599 406 1215 957 A N ATOM 3761 CA CYS E 99 8.275 2.280 -25.522 1.00 66.95 A C ANISOU 3761 CA CYS E 99 10337 7629 7472 291 910 914 A C ATOM 3762 C CYS E 99 8.825 3.699 -25.551 1.00 78.43 A C ANISOU 3762 C CYS E 99 11436 9080 9284 412 746 1016 A C ATOM 3763 O CYS E 99 9.242 4.181 -26.611 1.00 68.13 A O ANISOU 3763 O CYS E 99 10189 7627 8070 287 490 964 A O ATOM 3764 CB CYS E 99 6.782 2.289 -25.849 1.00 61.03 A C ANISOU 3764 CB CYS E 99 9979 6763 6446 351 721 858 A C ATOM 3765 SG CYS E 99 5.877 3.715 -25.192 1.00 74.56 A S ANISOU 3765 SG CYS E 99 11516 8513 8301 732 515 942 A S ATOM 3766 N GLY E 100 8.830 4.382 -24.409 1.00 70.16 A N ANISOU 3766 N GLY E 100 10022 8185 8452 663 889 1151 A N ATOM 3767 CA GLY E 100 9.357 5.727 -24.337 1.00 72.77 A C ANISOU 3767 CA GLY E 100 9928 8520 9201 765 799 1257 A C ATOM 3768 C GLY E 100 8.420 6.821 -24.791 1.00 83.12 A C ANISOU 3768 C GLY E 100 11259 9742 10581 933 452 1212 A C ATOM 3769 O GLY E 100 8.843 7.980 -24.867 1.00 91.45 A O ANISOU 3769 O GLY E 100 11922 10776 12051 1003 327 1263 A O ATOM 3770 N GLU E 101 7.163 6.500 -25.103 1.00 79.90 A N ANISOU 3770 N GLU E 101 11284 9257 9815 1001 276 1112 A N ATOM 3771 CA GLU E 101 6.204 7.533 -25.478 1.00 96.07 A C ANISOU 3771 CA GLU E 101 13387 11204 11913 1209 -87 1060 A C ATOM 3772 C GLU E 101 4.766 7.100 -25.219 1.00 80.80 A C ANISOU 3772 C GLU E 101 11861 9237 9601 1364 -141 1003 A C ATOM 3773 O GLU E 101 3.852 7.502 -25.946 1.00 88.56 A O ANISOU 3773 O GLU E 101 13163 10035 10450 1437 -512 920 A O ATOM 3774 CB GLU E 101 6.381 7.931 -26.945 1.00 93.16 A C ANISOU 3774 CB GLU E 101 13242 10591 11565 1054 -528 950 A C ATOM 3775 CG GLU E 101 6.522 6.771 -27.912 1.00 80.87 A C ANISOU 3775 CG GLU E 101 12214 8895 9617 752 -539 867 A C ATOM 3776 CD GLU E 101 7.518 7.065 -29.017 1.00108.12 A C ANISOU 3776 CD GLU E 101 15673 12197 13211 573 -789 793 A C ATOM 3777 OE1 GLU E 101 8.602 7.605 -28.712 1.00114.21 A O ANISOU 3777 OE1 GLU E 101 15942 13034 14419 553 -731 842 A O ATOM 3778 OE2 GLU E 101 7.213 6.763 -30.190 1.00103.18 A O1- ANISOU 3778 OE2 GLU E 101 15580 11370 12254 460 -1045 689 A O1- ATOM 3779 N CYS E 102 4.553 6.287 -24.191 1.00 84.60 A N ANISOU 3779 N CYS E 102 12359 9869 9917 1426 188 1037 A N ATOM 3780 CA CYS E 102 3.222 5.980 -23.691 1.00 70.00 A C ANISOU 3780 CA CYS E 102 10807 7997 7794 1624 142 978 A C ATOM 3781 C CYS E 102 3.035 6.659 -22.337 1.00 79.94 A C ANISOU 3781 C CYS E 102 11695 9475 9203 2017 331 1046 A C ATOM 3782 O CYS E 102 3.924 7.354 -21.837 1.00 87.17 A O ANISOU 3782 O CYS E 102 12134 10553 10434 2104 533 1163 A O ATOM 3783 CB CYS E 102 3.004 4.466 -23.615 1.00 67.15 A C ANISOU 3783 CB CYS E 102 10792 7598 7124 1407 315 916 A C ATOM 3784 SG CYS E 102 3.597 3.665 -22.106 1.00 78.03 A S ANISOU 3784 SG CYS E 102 11897 9234 8515 1516 745 959 A S ATOM 3785 N ARG E 103 1.857 6.461 -21.741 1.00 92.47 A N ANISOU 3785 N ARG E 103 13521 11051 10561 2260 277 974 A N ATOM 3786 CA ARG E 103 1.540 7.170 -20.504 1.00 83.62 A C ANISOU 3786 CA ARG E 103 12116 10132 9523 2696 436 1013 A C ATOM 3787 C ARG E 103 2.403 6.687 -19.344 1.00 84.12 A C ANISOU 3787 C ARG E 103 11936 10436 9591 2759 884 1121 A C ATOM 3788 O ARG E 103 2.862 7.495 -18.528 1.00 77.02 A O ANISOU 3788 O ARG E 103 10637 9736 8890 3011 1142 1245 A O ATOM 3789 CB ARG E 103 0.056 7.018 -20.171 1.00 79.85 A C ANISOU 3789 CB ARG E 103 12009 9552 8776 2959 224 878 A C ATOM 3790 CG ARG E 103 -0.469 8.094 -19.232 1.00 89.98 A C ANISOU 3790 CG ARG E 103 13032 10995 10160 3466 266 875 A C ATOM 3791 CD ARG E 103 -1.932 8.412 -19.501 1.00 98.08 A C ANISOU 3791 CD ARG E 103 14412 11818 11038 3697 -142 720 A C ATOM 3792 NE ARG E 103 -2.652 8.762 -18.282 1.00 92.71 A N ANISOU 3792 NE ARG E 103 13678 11285 10264 4198 -44 654 A N ATOM 3793 CZ ARG E 103 -2.612 9.955 -17.703 1.00 99.66 A C ANISOU 3793 CZ ARG E 103 14141 12360 11365 4589 80 682 A C ATOM 3794 NH1 ARG E 103 -1.896 10.946 -18.208 1.00110.95 A N1+ ANISOU 3794 NH1 ARG E 103 15122 13849 13185 4523 99 771 A N1+ ATOM 3795 NH2 ARG E 103 -3.310 10.158 -16.589 1.00 97.16 A N ANISOU 3795 NH2 ARG E 103 13849 12175 10892 5066 188 604 A N ATOM 3796 N HIS E 104 2.638 5.376 -19.253 1.00 86.67 A N ANISOU 3796 N HIS E 104 12495 10732 9703 2542 989 1077 A N ATOM 3797 CA HIS E 104 3.460 4.854 -18.166 1.00 88.73 A C ANISOU 3797 CA HIS E 104 12585 11190 9937 2628 1356 1164 A C ATOM 3798 C HIS E 104 4.935 5.177 -18.368 1.00 87.50 A C ANISOU 3798 C HIS E 104 12061 11108 10076 2428 1575 1334 A C ATOM 3799 O HIS E 104 5.661 5.384 -17.389 1.00 86.04 A O ANISOU 3799 O HIS E 104 11623 11099 9967 2601 1905 1486 A O ATOM 3800 CB HIS E 104 3.266 3.345 -18.033 1.00 69.11 A C ANISOU 3800 CB HIS E 104 10426 8634 7197 2470 1347 1027 A C ATOM 3801 CG HIS E 104 1.868 2.943 -17.682 1.00 79.08 A C ANISOU 3801 CG HIS E 104 12033 9799 8213 2662 1141 858 A C ATOM 3802 CD2 HIS E 104 0.744 2.874 -18.435 1.00 64.51 A C ANISOU 3802 CD2 HIS E 104 10511 7728 6274 2569 828 738 A C ATOM 3803 ND1 HIS E 104 1.505 2.539 -16.415 1.00 71.09 A N ANISOU 3803 ND1 HIS E 104 11097 8895 7018 3002 1229 793 A N ATOM 3804 CE1 HIS E 104 0.218 2.244 -16.401 1.00 69.62 A C ANISOU 3804 CE1 HIS E 104 11234 8549 6670 3101 961 621 A C ATOM 3805 NE2 HIS E 104 -0.267 2.438 -17.614 1.00 73.56 A N ANISOU 3805 NE2 HIS E 104 11887 8837 7225 2830 729 600 A N ATOM 3806 N CYS E 105 5.397 5.217 -19.621 1.00 82.57 A N ANISOU 3806 N CYS E 105 11440 10331 9604 2076 1392 1312 A N ATOM 3807 CA CYS E 105 6.797 5.542 -19.877 1.00 81.26 A C ANISOU 3807 CA CYS E 105 10934 10189 9751 1878 1542 1447 A C ATOM 3808 C CYS E 105 7.100 6.991 -19.518 1.00 80.84 A C ANISOU 3808 C CYS E 105 10419 10230 10068 2078 1640 1601 A C ATOM 3809 O CYS E 105 8.164 7.290 -18.965 1.00 89.41 A O ANISOU 3809 O CYS E 105 11162 11410 11397 2070 1944 1782 A O ATOM 3810 CB CYS E 105 7.143 5.263 -21.339 1.00 77.17 A C ANISOU 3810 CB CYS E 105 10577 9470 9276 1497 1278 1348 A C ATOM 3811 SG CYS E 105 7.352 3.510 -21.724 1.00 73.62 A S ANISOU 3811 SG CYS E 105 10501 8948 8524 1191 1337 1211 A S ATOM 3812 N HIS E 106 6.177 7.905 -19.825 1.00 88.27 A N ANISOU 3812 N HIS E 106 11332 11126 11080 2258 1391 1533 A N ATOM 3813 CA HIS E 106 6.331 9.285 -19.385 1.00 94.42 A C ANISOU 3813 CA HIS E 106 11617 12014 12246 2491 1510 1651 A C ATOM 3814 C HIS E 106 6.172 9.423 -17.877 1.00 96.80 A C ANISOU 3814 C HIS E 106 11784 12557 12438 2867 1941 1778 A C ATOM 3815 O HIS E 106 6.616 10.425 -17.308 1.00 98.37 A O ANISOU 3815 O HIS E 106 11519 12885 12972 3027 2224 1940 A O ATOM 3816 CB HIS E 106 5.327 10.185 -20.105 1.00 83.47 A C ANISOU 3816 CB HIS E 106 10249 10508 10959 2630 1087 1505 A C ATOM 3817 CG HIS E 106 5.527 10.245 -21.586 1.00 96.59 A C ANISOU 3817 CG HIS E 106 12051 11922 12728 2318 646 1392 A C ATOM 3818 CD2 HIS E 106 4.638 10.288 -22.607 1.00102.36 A C ANISOU 3818 CD2 HIS E 106 13163 12441 13287 2295 172 1223 A C ATOM 3819 ND1 HIS E 106 6.777 10.270 -22.167 1.00 99.12 A N ANISOU 3819 ND1 HIS E 106 12158 12169 13334 2006 655 1451 A N ATOM 3820 CE1 HIS E 106 6.649 10.325 -23.481 1.00 89.16 A C ANISOU 3820 CE1 HIS E 106 11145 10679 12054 1822 199 1306 A C ATOM 3821 NE2 HIS E 106 5.361 10.336 -23.774 1.00 93.33 A N ANISOU 3821 NE2 HIS E 106 12050 11118 12292 1991 -89 1179 A N ATOM 3822 N SER E 107 5.551 8.444 -17.225 1.00101.05 A N ANISOU 3822 N SER E 107 9491 12266 16638 1020 1839 -1549 A N ATOM 3823 CA SER E 107 5.455 8.437 -15.774 1.00102.01 A C ANISOU 3823 CA SER E 107 10145 12179 16437 473 2368 -1832 A C ATOM 3824 C SER E 107 6.776 7.996 -15.157 1.00 96.43 A C ANISOU 3824 C SER E 107 9970 11533 15137 -148 2432 -1714 A C ATOM 3825 O SER E 107 7.479 7.140 -15.702 1.00 99.52 A O ANISOU 3825 O SER E 107 10587 11992 15235 -156 1955 -1256 A O ATOM 3826 CB SER E 107 4.330 7.508 -15.318 1.00 90.34 A C ANISOU 3826 CB SER E 107 9144 10343 14840 570 2282 -1652 A C ATOM 3827 OG SER E 107 4.664 6.867 -14.098 1.00 89.46 A O ANISOU 3827 OG SER E 107 9773 10059 14158 -12 2507 -1653 A O ATOM 3828 N GLU E 108 7.112 8.590 -14.013 1.00 99.50 A N ANISOU 3828 N GLU E 108 10569 11893 15344 -656 3038 -2127 A N ATOM 3829 CA GLU E 108 8.328 8.217 -13.302 1.00 98.24 A C ANISOU 3829 CA GLU E 108 10968 11760 14599 -1255 3184 -2046 A C ATOM 3830 C GLU E 108 8.128 7.005 -12.401 1.00 99.26 A C ANISOU 3830 C GLU E 108 11940 11621 14153 -1535 3122 -1791 A C ATOM 3831 O GLU E 108 9.111 6.360 -12.021 1.00 94.77 A O ANISOU 3831 O GLU E 108 11904 11072 13032 -1923 3057 -1561 A O ATOM 3832 CB GLU E 108 8.834 9.406 -12.476 1.00110.89 A C ANISOU 3832 CB GLU E 108 12433 13452 16248 -1679 3889 -2599 A C ATOM 3833 CG GLU E 108 10.226 9.224 -11.886 1.00132.51 A C ANISOU 3833 CG GLU E 108 15649 16253 18446 -2269 4084 -2543 A C ATOM 3834 CD GLU E 108 10.855 10.535 -11.460 1.00139.26 A C ANISOU 3834 CD GLU E 108 16172 17260 19481 -2601 4713 -3067 A C ATOM 3835 OE1 GLU E 108 10.252 11.242 -10.626 1.00136.47 A O ANISOU 3835 OE1 GLU E 108 15768 16807 19278 -2724 5259 -3512 A O ATOM 3836 OE2 GLU E 108 11.955 10.858 -11.958 1.00157.60 A O1- ANISOU 3836 OE2 GLU E 108 18284 19798 21799 -2746 4670 -3042 A O1- ATOM 3837 N GLU E 109 6.882 6.667 -12.070 1.00 96.02 A N ANISOU 3837 N GLU E 109 11662 10967 13856 -1334 3134 -1829 A N ATOM 3838 CA GLU E 109 6.615 5.604 -11.109 1.00 87.32 A C ANISOU 3838 CA GLU E 109 11331 9618 12230 -1618 3134 -1678 A C ATOM 3839 C GLU E 109 6.394 4.248 -11.767 1.00 79.84 A C ANISOU 3839 C GLU E 109 10648 8589 11098 -1364 2460 -1112 A C ATOM 3840 O GLU E 109 6.813 3.222 -11.220 1.00 93.16 A O ANISOU 3840 O GLU E 109 12988 10202 12205 -1666 2310 -853 A O ATOM 3841 CB GLU E 109 5.394 5.965 -10.260 1.00 89.53 A C ANISOU 3841 CB GLU E 109 11658 9659 12700 -1601 3564 -2072 A C ATOM 3842 CG GLU E 109 5.634 5.876 -8.766 1.00 98.33 A C ANISOU 3842 CG GLU E 109 13408 10647 13307 -2160 4062 -2325 A C ATOM 3843 CD GLU E 109 6.489 7.015 -8.249 1.00122.71 A C ANISOU 3843 CD GLU E 109 16339 13897 16388 -2520 4633 -2724 A C ATOM 3844 OE1 GLU E 109 7.562 6.742 -7.673 1.00132.62 A O ANISOU 3844 OE1 GLU E 109 18064 15209 17115 -2967 4762 -2648 A O ATOM 3845 OE2 GLU E 109 6.091 8.186 -8.425 1.00127.36 A O1- ANISOU 3845 OE2 GLU E 109 16335 14556 17500 -2351 4962 -3117 A O1- ATOM 3846 N SER E 110 5.743 4.216 -12.924 1.00 77.93 A N ANISOU 3846 N SER E 110 9918 8364 11329 -804 2058 -915 A N ATOM 3847 CA SER E 110 5.317 2.969 -13.541 1.00 75.59 A C ANISOU 3847 CA SER E 110 9837 7949 10934 -520 1463 -410 A C ATOM 3848 C SER E 110 6.322 2.505 -14.586 1.00 77.96 A C ANISOU 3848 C SER E 110 10038 8477 11105 -396 928 48 A C ATOM 3849 O SER E 110 6.897 3.316 -15.318 1.00 81.16 A O ANISOU 3849 O SER E 110 9919 9125 11794 -246 912 -24 A O ATOM 3850 CB SER E 110 3.940 3.126 -14.188 1.00 81.88 A C ANISOU 3850 CB SER E 110 10210 8589 12311 49 1346 -432 A C ATOM 3851 OG SER E 110 3.500 1.902 -14.753 1.00 73.45 A O ANISOU 3851 OG SER E 110 9369 7383 11157 305 805 50 A O ATOM 3852 N ASN E 111 6.525 1.188 -14.648 1.00 70.16 A N ANISOU 3852 N ASN E 111 9553 7420 9685 -458 487 509 A N ATOM 3853 CA ASN E 111 7.301 0.551 -15.704 1.00 88.30 A C ANISOU 3853 CA ASN E 111 11796 9895 11860 -273 -96 1011 A C ATOM 3854 C ASN E 111 6.431 -0.337 -16.586 1.00 82.50 A C ANISOU 3854 C ASN E 111 10986 9030 11331 218 -630 1420 A C ATOM 3855 O ASN E 111 6.946 -1.218 -17.281 1.00 80.08 A O ANISOU 3855 O ASN E 111 10815 8808 10803 330 -1153 1903 A O ATOM 3856 CB ASN E 111 8.458 -0.257 -15.111 1.00 65.75 A C ANISOU 3856 CB ASN E 111 9594 7108 8282 -759 -182 1245 A C ATOM 3857 CG ASN E 111 7.992 -1.493 -14.350 1.00 64.71 A C ANISOU 3857 CG ASN E 111 10132 6759 7694 -942 -307 1428 A C ATOM 3858 ND2 ASN E 111 8.942 -2.332 -13.954 1.00 65.41 A N ANISOU 3858 ND2 ASN E 111 10791 6921 7141 -1281 -469 1694 A N ATOM 3859 OD1 ASN E 111 6.799 -1.693 -14.128 1.00 63.31 A O ANISOU 3859 OD1 ASN E 111 9960 6357 7737 -774 -257 1324 A O ATOM 3860 N MET E 112 5.115 -0.128 -16.559 1.00 75.99 A N ANISOU 3860 N MET E 112 9962 7988 10923 513 -492 1238 A N ATOM 3861 CA MET E 112 4.174 -1.005 -17.248 1.00 84.64 A C ANISOU 3861 CA MET E 112 11055 8897 12207 942 -920 1597 A C ATOM 3862 C MET E 112 3.792 -0.352 -18.573 1.00 70.37 A C ANISOU 3862 C MET E 112 8530 7193 11015 1575 -1128 1671 A C ATOM 3863 O MET E 112 2.735 0.261 -18.725 1.00 68.60 A O ANISOU 3863 O MET E 112 7949 6834 11282 1920 -920 1432 A O ATOM 3864 CB MET E 112 2.967 -1.287 -16.363 1.00 72.86 A C ANISOU 3864 CB MET E 112 9859 7073 10752 858 -639 1370 A C ATOM 3865 CG MET E 112 3.194 -2.493 -15.480 1.00 75.42 A C ANISOU 3865 CG MET E 112 10922 7285 10449 417 -739 1535 A C ATOM 3866 SD MET E 112 1.864 -2.871 -14.338 1.00103.63 A S ANISOU 3866 SD MET E 112 14885 10484 14005 251 -403 1230 A S ATOM 3867 CE MET E 112 1.931 -4.657 -14.425 1.00 98.38 A C ANISOU 3867 CE MET E 112 14785 9736 12858 165 -972 1754 A C ATOM 3868 N CYS E 113 4.688 -0.501 -19.546 1.00 75.38 A N ANISOU 3868 N CYS E 113 11370 8195 9075 1340 1388 -91 A N ATOM 3869 CA CYS E 113 4.503 0.108 -20.856 1.00 72.12 A C ANISOU 3869 CA CYS E 113 10876 7778 8749 1125 1382 470 A C ATOM 3870 C CYS E 113 3.249 -0.430 -21.531 1.00 80.53 A C ANISOU 3870 C CYS E 113 11739 8522 10336 998 1380 619 A C ATOM 3871 O CYS E 113 3.027 -1.644 -21.581 1.00 83.18 A O ANISOU 3871 O CYS E 113 12048 8783 10772 914 1362 421 A O ATOM 3872 CB CYS E 113 5.731 -0.157 -21.726 1.00 57.28 A C ANISOU 3872 CB CYS E 113 9190 6222 6351 928 1355 685 A C ATOM 3873 SG CYS E 113 5.639 0.544 -23.379 1.00 68.24 A S ANISOU 3873 SG CYS E 113 10515 7662 7750 663 1319 1357 A S ATOM 3874 N ASP E 114 2.426 0.484 -22.051 1.00 73.58 A N ANISOU 3874 N ASP E 114 10703 7461 9794 987 1405 994 A N ATOM 3875 CA ASP E 114 1.199 0.079 -22.728 1.00 85.92 A C ANISOU 3875 CA ASP E 114 12081 8690 11876 875 1423 1189 A C ATOM 3876 C ASP E 114 1.486 -0.795 -23.941 1.00 83.19 A C ANISOU 3876 C ASP E 114 11734 8468 11405 610 1407 1458 A C ATOM 3877 O ASP E 114 0.666 -1.648 -24.300 1.00 81.21 A O ANISOU 3877 O ASP E 114 11353 7978 11524 500 1421 1476 A O ATOM 3878 CB ASP E 114 0.399 1.311 -23.153 1.00 80.60 A C ANISOU 3878 CB ASP E 114 11259 7854 11512 938 1470 1609 A C ATOM 3879 CG ASP E 114 -0.360 1.939 -22.004 1.00 83.16 A C ANISOU 3879 CG ASP E 114 11542 7915 12139 1234 1518 1346 A C ATOM 3880 OD1 ASP E 114 -0.908 1.187 -21.172 1.00 91.50 A O ANISOU 3880 OD1 ASP E 114 12622 8708 13436 1325 1509 893 A O ATOM 3881 OD2 ASP E 114 -0.418 3.186 -21.939 1.00 84.84 A O1- ANISOU 3881 OD2 ASP E 114 11698 8193 12343 1384 1562 1600 A O1- ATOM 3882 N LEU E 115 2.640 -0.607 -24.577 1.00 75.94 A N ANISOU 3882 N LEU E 115 10971 7913 9969 508 1379 1672 A N ATOM 3883 CA LEU E 115 2.958 -1.279 -25.831 1.00 75.99 A C ANISOU 3883 CA LEU E 115 11009 8065 9799 296 1374 1987 A C ATOM 3884 C LEU E 115 3.854 -2.499 -25.656 1.00 75.07 A C ANISOU 3884 C LEU E 115 11061 8165 9299 270 1369 1695 A C ATOM 3885 O LEU E 115 3.668 -3.497 -26.359 1.00 69.11 A O ANISOU 3885 O LEU E 115 10247 7410 8600 150 1395 1814 A O ATOM 3886 CB LEU E 115 3.622 -0.291 -26.798 1.00 73.69 A C ANISOU 3886 CB LEU E 115 10810 8027 9161 194 1334 2448 A C ATOM 3887 CG LEU E 115 4.443 -0.866 -27.956 1.00 76.56 A C ANISOU 3887 CG LEU E 115 11341 8652 9094 22 1310 2700 A C ATOM 3888 CD1 LEU E 115 3.533 -1.266 -29.103 1.00 65.51 A C ANISOU 3888 CD1 LEU E 115 9756 7110 8024 -94 1354 3101 A C ATOM 3889 CD2 LEU E 115 5.498 0.123 -28.429 1.00 75.46 A C ANISOU 3889 CD2 LEU E 115 11406 8807 8456 -55 1225 2939 A C ATOM 3890 N LEU E 116 4.811 -2.458 -24.727 1.00 73.64 A N ANISOU 3890 N LEU E 116 11075 8176 8727 399 1350 1334 A N ATOM 3891 CA LEU E 116 5.864 -3.467 -24.668 1.00 67.90 A C ANISOU 3891 CA LEU E 116 10554 7716 7529 401 1357 1125 A C ATOM 3892 C LEU E 116 5.912 -4.211 -23.337 1.00 64.18 A C ANISOU 3892 C LEU E 116 10084 7229 7072 575 1362 565 A C ATOM 3893 O LEU E 116 6.916 -4.868 -23.043 1.00 77.06 A O ANISOU 3893 O LEU E 116 11911 9116 8253 643 1376 348 A O ATOM 3894 CB LEU E 116 7.221 -2.826 -24.956 1.00 66.55 A C ANISOU 3894 CB LEU E 116 10689 7848 6750 383 1334 1255 A C ATOM 3895 CG LEU E 116 7.407 -2.237 -26.354 1.00 59.23 A C ANISOU 3895 CG LEU E 116 9819 7011 5674 194 1299 1786 A C ATOM 3896 CD1 LEU E 116 8.800 -1.664 -26.511 1.00 66.33 A C ANISOU 3896 CD1 LEU E 116 11058 8183 5961 154 1249 1841 A C ATOM 3897 CD2 LEU E 116 7.136 -3.291 -27.414 1.00 65.81 A C ANISOU 3897 CD2 LEU E 116 10605 7858 6543 85 1337 2007 A C ATOM 3898 N ARG E 117 4.860 -4.136 -22.526 1.00 67.12 A N ANISOU 3898 N ARG E 117 10262 7309 7932 664 1347 321 A N ATOM 3899 CA ARG E 117 4.854 -4.912 -21.296 1.00 71.20 A C ANISOU 3899 CA ARG E 117 10776 7820 8458 820 1325 -224 A C ATOM 3900 C ARG E 117 4.752 -6.403 -21.619 1.00 69.60 A C ANISOU 3900 C ARG E 117 10476 7677 8294 703 1318 -302 A C ATOM 3901 O ARG E 117 4.486 -6.805 -22.756 1.00 69.28 A O ANISOU 3901 O ARG E 117 10340 7620 8364 512 1344 71 A O ATOM 3902 CB ARG E 117 3.717 -4.469 -20.375 1.00 71.14 A C ANISOU 3902 CB ARG E 117 10618 7461 8952 948 1297 -479 A C ATOM 3903 CG ARG E 117 2.359 -5.063 -20.697 1.00 97.46 A C ANISOU 3903 CG ARG E 117 13708 10427 12896 799 1270 -437 A C ATOM 3904 CD ARG E 117 1.378 -4.793 -19.566 1.00103.65 A C ANISOU 3904 CD ARG E 117 14426 10865 14092 966 1229 -820 A C ATOM 3905 NE ARG E 117 1.307 -3.376 -19.230 1.00105.54 A N ANISOU 3905 NE ARG E 117 14730 11037 14331 1162 1276 -719 A N ATOM 3906 CZ ARG E 117 0.246 -2.609 -19.436 1.00107.70 A C ANISOU 3906 CZ ARG E 117 14896 10967 15056 1188 1308 -508 A C ATOM 3907 NH1 ARG E 117 -0.863 -3.093 -19.973 1.00 97.62 A N1+ ANISOU 3907 NH1 ARG E 117 13461 9340 14288 1018 1297 -382 A N1+ ATOM 3908 NH2 ARG E 117 0.297 -1.324 -19.094 1.00 91.33 A N ANISOU 3908 NH2 ARG E 117 12870 8908 12924 1397 1362 -399 A N ATOM 3909 N ILE E 118 4.968 -7.226 -20.588 1.00 75.49 A N ANISOU 3909 N ILE E 118 11230 8516 8936 833 1285 -778 A N ATOM 3910 CA ILE E 118 5.139 -8.661 -20.786 1.00 74.69 A C ANISOU 3910 CA ILE E 118 11043 8585 8748 756 1280 -864 A C ATOM 3911 C ILE E 118 3.946 -9.248 -21.531 1.00 70.85 A C ANISOU 3911 C ILE E 118 10264 7832 8824 515 1262 -631 A C ATOM 3912 O ILE E 118 2.791 -8.877 -21.295 1.00 78.09 A O ANISOU 3912 O ILE E 118 11022 8365 10286 459 1215 -675 A O ATOM 3913 CB ILE E 118 5.365 -9.361 -19.432 1.00 77.00 A C ANISOU 3913 CB ILE E 118 11342 8997 8918 944 1222 -1437 A C ATOM 3914 CG1 ILE E 118 5.698 -10.841 -19.634 1.00 63.94 A C ANISOU 3914 CG1 ILE E 118 9591 7607 7097 887 1224 -1496 A C ATOM 3915 CG2 ILE E 118 4.161 -9.186 -18.516 1.00 63.37 A C ANISOU 3915 CG2 ILE E 118 9447 6900 7730 974 1124 -1775 A C ATOM 3916 CD1 ILE E 118 5.893 -11.602 -18.338 1.00 61.58 A C ANISOU 3916 CD1 ILE E 118 9264 7464 6671 1067 1150 -2045 A C ATOM 3917 N ASN E 119 4.237 -10.157 -22.461 1.00 75.67 A N ANISOU 3917 N ASN E 119 10816 8640 9294 386 1313 -357 A N ATOM 3918 CA ASN E 119 3.201 -10.822 -23.248 1.00 66.71 A C ANISOU 3918 CA ASN E 119 9390 7299 8659 150 1319 -80 A C ATOM 3919 C ASN E 119 3.746 -12.177 -23.675 1.00 69.68 A C ANISOU 3919 C ASN E 119 9692 8014 8768 108 1366 -6 A C ATOM 3920 O ASN E 119 4.634 -12.250 -24.531 1.00 73.43 A O ANISOU 3920 O ASN E 119 10340 8781 8780 146 1461 304 A O ATOM 3921 CB ASN E 119 2.800 -9.983 -24.458 1.00 70.52 A C ANISOU 3921 CB ASN E 119 9866 7618 9310 28 1384 468 A C ATOM 3922 CG ASN E 119 1.534 -10.488 -25.128 1.00 82.69 A C ANISOU 3922 CG ASN E 119 11096 8852 11470 -200 1398 744 A C ATOM 3923 ND2 ASN E 119 0.857 -9.605 -25.853 1.00 79.28 A N ANISOU 3923 ND2 ASN E 119 10624 8162 11337 -272 1436 1127 A N ATOM 3924 OD1 ASN E 119 1.167 -11.656 -24.996 1.00 83.23 A O ANISOU 3924 OD1 ASN E 119 10952 8921 11749 -311 1376 632 A O ATOM 3925 N THR E 120 3.213 -13.244 -23.084 1.00 69.27 A N ANISOU 3925 N THR E 120 9390 7931 8998 36 1294 -284 A N ATOM 3926 CA THR E 120 3.636 -14.597 -23.411 1.00 79.07 A C ANISOU 3926 CA THR E 120 10495 9517 10031 4 1338 -207 A C ATOM 3927 C THR E 120 2.794 -15.235 -24.506 1.00 88.55 A C ANISOU 3927 C THR E 120 11392 10595 11658 -254 1393 251 A C ATOM 3928 O THR E 120 3.149 -16.315 -24.990 1.00 80.85 A O ANISOU 3928 O THR E 120 10288 9935 10498 -274 1464 433 A O ATOM 3929 CB THR E 120 3.582 -15.483 -22.164 1.00 85.23 A C ANISOU 3929 CB THR E 120 11132 10402 10851 58 1217 -743 A C ATOM 3930 CG2 THR E 120 4.322 -14.826 -21.009 1.00 74.38 A C ANISOU 3930 CG2 THR E 120 10044 9126 9091 335 1172 -1199 A C ATOM 3931 OG1 THR E 120 2.216 -15.688 -21.787 1.00 95.03 A O ANISOU 3931 OG1 THR E 120 12081 11231 12797 -166 1087 -896 A O ATOM 3932 N GLU E 121 1.689 -14.600 -24.901 1.00 88.91 A N ANISOU 3932 N GLU E 121 11318 10201 12263 -429 1377 461 A N ATOM 3933 CA GLU E 121 0.838 -15.152 -25.948 1.00 92.02 A C ANISOU 3933 CA GLU E 121 11423 10447 13094 -672 1445 928 A C ATOM 3934 C GLU E 121 1.389 -14.878 -27.339 1.00 88.82 A C ANISOU 3934 C GLU E 121 11151 10254 12344 -631 1605 1506 A C ATOM 3935 O GLU E 121 1.160 -15.670 -28.260 1.00 95.60 A O ANISOU 3935 O GLU E 121 11804 11216 13303 -748 1704 1911 A O ATOM 3936 CB GLU E 121 -0.575 -14.576 -25.833 1.00 85.47 A C ANISOU 3936 CB GLU E 121 10440 9037 12997 -854 1381 940 A C ATOM 3937 CG GLU E 121 -1.349 -15.069 -24.627 1.00101.98 A C ANISOU 3937 CG GLU E 121 12360 10859 15530 -957 1211 418 A C ATOM 3938 CD GLU E 121 -1.543 -16.568 -24.641 1.00118.47 A C ANISOU 3938 CD GLU E 121 14119 13116 17779 -1153 1173 408 A C ATOM 3939 OE1 GLU E 121 -1.903 -17.108 -25.708 1.00111.32 A O ANISOU 3939 OE1 GLU E 121 12993 12222 17083 -1334 1281 908 A O ATOM 3940 OE2 GLU E 121 -1.342 -17.206 -23.588 1.00124.46 A O1- ANISOU 3940 OE2 GLU E 121 14822 14014 18452 -1121 1036 -83 A O1- ATOM 3941 N ARG E 122 2.113 -13.777 -27.509 1.00 79.68 A N ANISOU 3941 N ARG E 122 10331 9172 10773 -470 1628 1558 A N ATOM 3942 CA ARG E 122 2.541 -13.353 -28.834 1.00 74.74 A C ANISOU 3942 CA ARG E 122 9858 8695 9844 -449 1743 2091 A C ATOM 3943 C ARG E 122 3.646 -14.256 -29.368 1.00 76.03 A C ANISOU 3943 C ARG E 122 10148 9338 9400 -325 1845 2230 A C ATOM 3944 O ARG E 122 4.599 -14.589 -28.657 1.00 73.69 A O ANISOU 3944 O ARG E 122 10034 9317 8646 -156 1827 1883 A O ATOM 3945 CB ARG E 122 3.014 -11.901 -28.782 1.00 75.43 A C ANISOU 3945 CB ARG E 122 10259 8733 9666 -340 1705 2077 A C ATOM 3946 CG ARG E 122 3.898 -11.478 -29.938 1.00 93.29 A C ANISOU 3946 CG ARG E 122 12793 11266 11386 -277 1779 2491 A C ATOM 3947 CD ARG E 122 3.943 -9.960 -30.096 1.00 89.76 A C ANISOU 3947 CD ARG E 122 12529 10684 10891 -266 1722 2608 A C ATOM 3948 NE ARG E 122 2.648 -9.322 -29.879 1.00 86.68 A N ANISOU 3948 NE ARG E 122 11894 9872 11167 -366 1686 2651 A N ATOM 3949 CZ ARG E 122 2.286 -8.710 -28.758 1.00 93.25 A C ANISOU 3949 CZ ARG E 122 12710 10476 12247 -313 1606 2274 A C ATOM 3950 NH1 ARG E 122 3.097 -8.645 -27.714 1.00 84.36 A N1+ ANISOU 3950 NH1 ARG E 122 11770 9505 10778 -170 1550 1823 A N1+ ATOM 3951 NH2 ARG E 122 1.083 -8.147 -28.685 1.00 89.86 A N ANISOU 3951 NH2 ARG E 122 12086 9649 12409 -378 1596 2364 A N ATOM 3952 N GLY E 123 3.505 -14.659 -30.630 1.00 72.50 A N ANISOU 3952 N GLY E 123 11068 6336 10142 -486 4924 -599 A N ATOM 3953 CA GLY E 123 4.509 -15.462 -31.298 1.00 58.17 A C ANISOU 3953 CA GLY E 123 9469 4580 8055 -617 4946 -469 A C ATOM 3954 C GLY E 123 5.127 -14.733 -32.472 1.00 77.74 A C ANISOU 3954 C GLY E 123 12145 7132 10261 -491 4706 -237 A C ATOM 3955 O GLY E 123 6.005 -15.263 -33.155 1.00 80.75 A O ANISOU 3955 O GLY E 123 12701 7577 10405 -579 4694 -142 A O ATOM 3956 N GLY E 124 4.658 -13.510 -32.721 1.00 75.60 A N ANISOU 3956 N GLY E 124 11832 6868 10026 -278 4514 -168 A N ATOM 3957 CA GLY E 124 5.186 -12.666 -33.752 1.00 73.04 A C ANISOU 3957 CA GLY E 124 11638 6669 9445 -140 4264 15 A C ATOM 3958 C GLY E 124 5.886 -11.443 -33.198 1.00 78.91 A C ANISOU 3958 C GLY E 124 12108 7736 10137 -123 4004 -123 A C ATOM 3959 O GLY E 124 6.234 -11.369 -32.010 1.00 90.15 A O ANISOU 3959 O GLY E 124 13247 9335 11669 -264 4017 -343 A O ATOM 3960 N MET E 125 6.094 -10.460 -34.069 1.00 85.61 A N ANISOU 3960 N MET E 125 13028 8694 10804 48 3766 10 A N ATOM 3961 CA MET E 125 6.718 -9.202 -33.687 1.00 70.76 A C ANISOU 3961 CA MET E 125 10898 7120 8866 78 3507 -112 A C ATOM 3962 C MET E 125 5.659 -8.125 -33.489 1.00 72.89 A C ANISOU 3962 C MET E 125 11034 7347 9313 320 3398 -126 A C ATOM 3963 O MET E 125 4.546 -8.216 -34.011 1.00 85.69 A O ANISOU 3963 O MET E 125 12817 8693 11048 511 3470 32 A O ATOM 3964 CB MET E 125 7.736 -8.765 -34.740 1.00 78.25 A C ANISOU 3964 CB MET E 125 11966 8265 9501 98 3302 -13 A C ATOM 3965 CG MET E 125 9.025 -9.568 -34.737 1.00 69.36 A C ANISOU 3965 CG MET E 125 10874 7241 8240 -154 3357 -74 A C ATOM 3966 SD MET E 125 10.204 -8.998 -33.499 1.00 85.71 A S ANISOU 3966 SD MET E 125 12578 9616 10372 -365 3242 -305 A S ATOM 3967 CE MET E 125 10.181 -10.369 -32.350 1.00 69.78 A C ANISOU 3967 CE MET E 125 10486 7489 8536 -592 3532 -398 A C ATOM 3968 N ILE E 126 6.019 -7.103 -32.710 1.00 84.37 A N ANISOU 3968 N ILE E 126 12179 9074 10805 308 3227 -316 A N ATOM 3969 CA ILE E 126 5.107 -5.986 -32.481 1.00 64.64 A C ANISOU 3969 CA ILE E 126 9511 6578 8471 541 3098 -371 A C ATOM 3970 C ILE E 126 4.788 -5.283 -33.793 1.00 78.62 A C ANISOU 3970 C ILE E 126 11483 8306 10083 819 2914 -133 A C ATOM 3971 O ILE E 126 3.656 -4.833 -34.018 1.00 82.77 A O ANISOU 3971 O ILE E 126 12031 8642 10777 1072 2891 -44 A O ATOM 3972 CB ILE E 126 5.714 -5.014 -31.453 1.00 69.84 A C ANISOU 3972 CB ILE E 126 9790 7600 9147 449 2940 -624 A C ATOM 3973 CG1 ILE E 126 5.746 -5.642 -30.061 1.00 84.55 A C ANISOU 3973 CG1 ILE E 126 11412 9524 11190 220 3131 -849 A C ATOM 3974 CG2 ILE E 126 4.930 -3.713 -31.418 1.00 79.78 A C ANISOU 3974 CG2 ILE E 126 10878 8915 10522 711 2755 -684 A C ATOM 3975 CD1 ILE E 126 4.467 -6.333 -29.679 1.00 81.97 A C ANISOU 3975 CD1 ILE E 126 11106 8886 11154 281 3363 -902 A C ATOM 3976 N HIS E 127 5.774 -5.198 -34.688 1.00 76.56 A N ANISOU 3976 N HIS E 127 11361 8226 9504 781 2782 -28 A N ATOM 3977 CA HIS E 127 5.637 -4.395 -35.898 1.00 83.50 A C ANISOU 3977 CA HIS E 127 12370 9184 10170 1037 2569 164 A C ATOM 3978 C HIS E 127 4.511 -4.911 -36.788 1.00 83.46 A C ANISOU 3978 C HIS E 127 12660 8848 10201 1247 2687 468 A C ATOM 3979 O HIS E 127 3.553 -4.188 -37.083 1.00 81.63 A O ANISOU 3979 O HIS E 127 12424 8522 10072 1531 2590 594 A O ATOM 3980 CB HIS E 127 6.964 -4.378 -36.658 1.00 73.18 A C ANISOU 3980 CB HIS E 127 11141 8144 8522 916 2442 171 A C ATOM 3981 CG HIS E 127 6.876 -3.747 -38.012 1.00 78.80 A C ANISOU 3981 CG HIS E 127 12002 8978 8958 1159 2247 368 A C ATOM 3982 CD2 HIS E 127 7.012 -4.273 -39.252 1.00 80.97 A C ANISOU 3982 CD2 HIS E 127 12553 9245 8965 1210 2265 583 A C ATOM 3983 ND1 HIS E 127 6.616 -2.405 -38.191 1.00 74.35 A N ANISOU 3983 ND1 HIS E 127 11279 8615 8354 1392 1996 347 A N ATOM 3984 CE1 HIS E 127 6.598 -2.132 -39.484 1.00 89.09 A C ANISOU 3984 CE1 HIS E 127 13317 10599 9933 1583 1863 551 A C ATOM 3985 NE2 HIS E 127 6.835 -3.248 -40.149 1.00 94.24 A N ANISOU 3985 NE2 HIS E 127 14233 11139 10436 1473 2024 698 A N ATOM 3986 N ASP E 128 4.608 -6.167 -37.228 1.00 76.44 A N ANISOU 3986 N ASP E 128 12026 7778 9238 1112 2899 601 A N ATOM 3987 CA ASP E 128 3.669 -6.707 -38.204 1.00 74.49 A C ANISOU 3987 CA ASP E 128 12080 7248 8975 1282 3017 930 A C ATOM 3988 C ASP E 128 2.980 -7.984 -37.739 1.00 80.72 A C ANISOU 3988 C ASP E 128 12981 7662 10027 1147 3350 947 A C ATOM 3989 O ASP E 128 2.238 -8.589 -38.522 1.00 81.00 A O ANISOU 3989 O ASP E 128 13278 7437 10064 1241 3491 1229 A O ATOM 3990 CB ASP E 128 4.382 -6.964 -39.537 1.00 89.03 A C ANISOU 3990 CB ASP E 128 14157 9270 10399 1283 2943 1124 A C ATOM 3991 CG ASP E 128 5.591 -7.869 -39.387 1.00 82.05 A C ANISOU 3991 CG ASP E 128 13298 8505 9371 966 3044 956 A C ATOM 3992 OD1 ASP E 128 5.960 -8.189 -38.238 1.00 78.29 A O ANISOU 3992 OD1 ASP E 128 12643 8009 9093 755 3140 710 A O ATOM 3993 OD2 ASP E 128 6.173 -8.260 -40.421 1.00 79.52 A O1- ANISOU 3993 OD2 ASP E 128 13163 8312 8740 934 3024 1070 A O1- ATOM 3994 N GLY E 129 3.196 -8.410 -36.496 1.00 78.58 A N ANISOU 3994 N GLY E 129 12509 7376 9970 925 3483 659 A N ATOM 3995 CA GLY E 129 2.620 -9.659 -36.041 1.00 81.21 A C ANISOU 3995 CA GLY E 129 12924 7399 10534 778 3801 632 A C ATOM 3996 C GLY E 129 3.180 -10.897 -36.701 1.00 80.62 A C ANISOU 3996 C GLY E 129 13106 7284 10240 598 3966 748 A C ATOM 3997 O GLY E 129 2.605 -11.979 -36.546 1.00 71.40 A O ANISOU 3997 O GLY E 129 12050 5840 9240 497 4240 770 A O ATOM 3998 N GLU E 130 4.284 -10.775 -37.431 1.00 71.19 A N ANISOU 3998 N GLU E 130 11993 6364 8690 549 3812 794 A N ATOM 3999 CA GLU E 130 4.891 -11.882 -38.150 1.00 70.70 A C ANISOU 3999 CA GLU E 130 12162 6305 8398 391 3944 881 A C ATOM 4000 C GLU E 130 6.190 -12.300 -37.474 1.00 81.48 A C ANISOU 4000 C GLU E 130 13378 7881 9700 124 3945 619 A C ATOM 4001 O GLU E 130 6.776 -11.554 -36.685 1.00 84.39 A O ANISOU 4001 O GLU E 130 13487 8456 10120 78 3792 423 A O ATOM 4002 CB GLU E 130 5.151 -11.501 -39.613 1.00 73.65 A C ANISOU 4002 CB GLU E 130 12740 6835 8408 545 3780 1128 A C ATOM 4003 CG GLU E 130 3.906 -11.542 -40.487 1.00103.92 A C ANISOU 4003 CG GLU E 130 16802 10428 12256 773 3854 1481 A C ATOM 4004 CD GLU E 130 4.025 -10.670 -41.722 1.00107.19 A C ANISOU 4004 CD GLU E 130 17312 11085 12332 1005 3608 1713 A C ATOM 4005 OE1 GLU E 130 5.085 -10.711 -42.381 1.00110.85 A O ANISOU 4005 OE1 GLU E 130 17811 11853 12453 922 3498 1660 A O ATOM 4006 OE2 GLU E 130 3.056 -9.945 -42.034 1.00104.53 A O1- ANISOU 4006 OE2 GLU E 130 16999 10641 12077 1276 3525 1938 A O1- ATOM 4007 N SER E 131 6.634 -13.511 -37.793 1.00 80.34 A N ANISOU 4007 N SER E 131 13393 7682 9449 -52 4123 628 A N ATOM 4008 CA SER E 131 7.835 -14.076 -37.198 1.00 81.02 A C ANISOU 4008 CA SER E 131 13359 7922 9503 -298 4150 412 A C ATOM 4009 C SER E 131 9.048 -13.833 -38.087 1.00 78.80 A C ANISOU 4009 C SER E 131 13138 7886 8915 -328 3969 413 A C ATOM 4010 O SER E 131 8.933 -13.677 -39.306 1.00 78.14 A O ANISOU 4010 O SER E 131 13249 7846 8595 -200 3899 587 A O ATOM 4011 CB SER E 131 7.663 -15.577 -36.956 1.00 80.07 A C ANISOU 4011 CB SER E 131 13345 7609 9470 -475 4452 378 A C ATOM 4012 OG SER E 131 8.847 -16.151 -36.431 1.00 84.23 A O ANISOU 4012 OG SER E 131 13713 8296 9994 -666 4378 169 A O ATOM 4013 N ARG E 132 10.222 -13.801 -37.457 1.00 81.91 A N ANISOU 4013 N ARG E 132 13346 8453 9324 -500 3896 214 A N ATOM 4014 CA ARG E 132 11.486 -13.662 -38.165 1.00 83.20 A C ANISOU 4014 CA ARG E 132 13527 8820 9266 -567 3747 154 A C ATOM 4015 C ARG E 132 12.240 -14.979 -38.299 1.00 82.30 A C ANISOU 4015 C ARG E 132 13506 8653 9110 -765 3915 81 A C ATOM 4016 O ARG E 132 13.175 -15.058 -39.103 1.00 81.23 A O ANISOU 4016 O ARG E 132 13428 8647 8788 -811 3828 30 A O ATOM 4017 CB ARG E 132 12.380 -12.634 -37.459 1.00 76.08 A C ANISOU 4017 CB ARG E 132 12344 8132 8432 -622 3535 -8 A C ATOM 4018 CG ARG E 132 11.680 -11.329 -37.114 1.00 79.96 A C ANISOU 4018 CG ARG E 132 12686 8698 8995 -446 3373 13 A C ATOM 4019 CD ARG E 132 11.789 -10.322 -38.249 1.00 71.39 A C ANISOU 4019 CD ARG E 132 11662 7793 7672 -265 3139 82 A C ATOM 4020 NE ARG E 132 10.923 -9.168 -38.041 1.00 84.86 A N ANISOU 4020 NE ARG E 132 13257 9541 9445 -55 3000 131 A N ATOM 4021 CZ ARG E 132 9.615 -9.160 -38.262 1.00 84.63 A C ANISOU 4021 CZ ARG E 132 13351 9330 9474 141 3070 308 A C ATOM 4022 NH1 ARG E 132 8.984 -10.230 -38.718 1.00 76.15 A N1+ ANISOU 4022 NH1 ARG E 132 12521 8021 8391 145 3286 468 A N1+ ATOM 4023 NH2 ARG E 132 8.923 -8.051 -38.019 1.00 75.84 A N ANISOU 4023 NH2 ARG E 132 12104 8263 8450 337 2925 324 A N ATOM 4024 N PHE E 133 11.863 -16.003 -37.539 1.00 76.64 A N ANISOU 4024 N PHE E 133 12730 7772 8616 -852 4041 28 A N ATOM 4025 CA PHE E 133 12.508 -17.308 -37.596 1.00 82.09 A C ANISOU 4025 CA PHE E 133 13372 8427 9390 -961 3970 -92 A C ATOM 4026 C PHE E 133 11.737 -18.236 -38.524 1.00 85.14 A C ANISOU 4026 C PHE E 133 13966 8677 9707 -894 4055 6 A C ATOM 4027 O PHE E 133 10.504 -18.246 -38.522 1.00 87.03 A O ANISOU 4027 O PHE E 133 14298 8764 10006 -795 4179 123 A O ATOM 4028 CB PHE E 133 12.594 -17.941 -36.207 1.00 74.17 A C ANISOU 4028 CB PHE E 133 12115 7388 8678 -1044 3917 -245 A C ATOM 4029 CG PHE E 133 13.237 -17.065 -35.174 1.00 78.15 A C ANISOU 4029 CG PHE E 133 12380 8044 9267 -1111 3833 -316 A C ATOM 4030 CD1 PHE E 133 14.515 -16.568 -35.363 1.00 71.65 A C ANISOU 4030 CD1 PHE E 133 11502 7366 8356 -1198 3745 -358 A C ATOM 4031 CD2 PHE E 133 12.564 -16.749 -34.006 1.00 70.95 A C ANISOU 4031 CD2 PHE E 133 11285 7142 8531 -1099 3856 -356 A C ATOM 4032 CE1 PHE E 133 15.108 -15.765 -34.406 1.00 67.34 A C ANISOU 4032 CE1 PHE E 133 10722 6966 7898 -1273 3676 -411 A C ATOM 4033 CE2 PHE E 133 13.150 -15.949 -33.048 1.00 76.64 A C ANISOU 4033 CE2 PHE E 133 11760 8044 9317 -1167 3771 -417 A C ATOM 4034 CZ PHE E 133 14.424 -15.455 -33.247 1.00 71.61 A C ANISOU 4034 CZ PHE E 133 11070 7545 8593 -1254 3678 -431 A C ATOM 4035 N SER E 134 12.467 -19.047 -39.288 1.00 81.65 A N ANISOU 4035 N SER E 134 13581 8280 9160 -959 4005 -50 A N ATOM 4036 CA SER E 134 11.829 -20.017 -40.164 1.00 88.86 A C ANISOU 4036 CA SER E 134 14658 9101 10003 -921 4081 26 A C ATOM 4037 C SER E 134 12.760 -21.198 -40.402 1.00 89.13 A C ANISOU 4037 C SER E 134 14638 9164 10061 -1040 4019 -132 A C ATOM 4038 O SER E 134 13.986 -21.068 -40.344 1.00 88.44 A O ANISOU 4038 O SER E 134 14462 9186 9955 -1130 3928 -250 A O ATOM 4039 CB SER E 134 11.426 -19.389 -41.504 1.00 90.21 A C ANISOU 4039 CB SER E 134 15067 9359 9851 -805 4126 248 A C ATOM 4040 OG SER E 134 12.561 -18.930 -42.216 1.00 71.76 A O ANISOU 4040 OG SER E 134 12752 7248 7265 -844 4034 190 A O ATOM 4041 N ILE E 135 12.152 -22.353 -40.662 1.00 96.59 A N ANISOU 4041 N ILE E 135 15642 9998 11061 -1042 4088 -136 A N ATOM 4042 CA ILE E 135 12.849 -23.567 -41.073 1.00 90.95 A C ANISOU 4042 CA ILE E 135 14913 9300 10343 -1139 4058 -260 A C ATOM 4043 C ILE E 135 12.136 -24.084 -42.315 1.00100.84 A C ANISOU 4043 C ILE E 135 16354 10554 11405 -1097 4158 -125 A C ATOM 4044 O ILE E 135 10.973 -24.501 -42.237 1.00 97.24 A O ANISOU 4044 O ILE E 135 15960 9959 11027 -1043 4267 -47 A O ATOM 4045 CB ILE E 135 12.863 -24.639 -39.975 1.00 93.05 A C ANISOU 4045 CB ILE E 135 15024 9452 10881 -1198 4032 -426 A C ATOM 4046 CG1 ILE E 135 13.895 -24.300 -38.904 1.00102.63 A C ANISOU 4046 CG1 ILE E 135 16036 10723 12235 -1258 3908 -547 A C ATOM 4047 CG2 ILE E 135 13.164 -26.010 -40.573 1.00101.42 A C ANISOU 4047 CG2 ILE E 135 16122 10492 11922 -1272 4048 -506 A C ATOM 4048 CD1 ILE E 135 14.287 -25.484 -38.063 1.00105.84 A C ANISOU 4048 CD1 ILE E 135 16301 11081 12832 -1321 3851 -698 A C ATOM 4049 N ASN E 136 12.826 -24.055 -43.456 1.00 96.45 A N ANISOU 4049 N ASN E 136 15880 10174 10594 -1125 4133 -104 A N ATOM 4050 CA ASN E 136 12.269 -24.521 -44.728 1.00105.71 A C ANISOU 4050 CA ASN E 136 17211 11422 11532 -1091 4214 37 A C ATOM 4051 C ASN E 136 10.940 -23.835 -45.037 1.00103.11 A C ANISOU 4051 C ASN E 136 17030 11038 11111 -948 4306 311 A C ATOM 4052 O ASN E 136 10.007 -24.445 -45.564 1.00 97.89 A O ANISOU 4052 O ASN E 136 16469 10308 10415 -918 4413 451 A O ATOM 4053 CB ASN E 136 12.109 -26.043 -44.738 1.00106.78 A C ANISOU 4053 CB ASN E 136 17318 11459 11795 -1176 4268 -66 A C ATOM 4054 CG ASN E 136 13.304 -26.761 -44.142 1.00122.06 A C ANISOU 4054 CG ASN E 136 19095 13382 13900 -1300 4179 -315 A C ATOM 4055 ND2 ASN E 136 14.502 -26.341 -44.531 1.00100.96 A N ANISOU 4055 ND2 ASN E 136 16385 10869 11107 -1352 4104 -400 A N ATOM 4056 OD1 ASN E 136 13.152 -27.685 -43.344 1.00127.50 A O ANISOU 4056 OD1 ASN E 136 19697 13924 14822 -1346 4184 -429 A O ATOM 4057 N GLY E 137 10.850 -22.550 -44.698 1.00105.56 A N ANISOU 4057 N GLY E 137 17353 11367 11388 -859 4270 401 A N ATOM 4058 CA GLY E 137 9.650 -21.776 -44.915 1.00 84.37 A C ANISOU 4058 CA GLY E 137 14809 8607 8639 -704 4350 680 A C ATOM 4059 C GLY E 137 8.633 -21.839 -43.794 1.00 97.79 A C ANISOU 4059 C GLY E 137 16455 10028 10673 -669 4447 679 A C ATOM 4060 O GLY E 137 7.779 -20.951 -43.703 1.00102.82 A O ANISOU 4060 O GLY E 137 17175 10571 11321 -535 4505 883 A O ATOM 4061 N LYS E 138 8.694 -22.859 -42.944 1.00 97.36 A N ANISOU 4061 N LYS E 138 16260 9849 10882 -772 4468 451 A N ATOM 4062 CA LYS E 138 7.775 -22.964 -41.816 1.00 93.95 A C ANISOU 4062 CA LYS E 138 15747 9200 10752 -746 4566 389 A C ATOM 4063 C LYS E 138 8.181 -21.977 -40.729 1.00101.13 A C ANISOU 4063 C LYS E 138 16508 10135 11782 -741 4492 294 A C ATOM 4064 O LYS E 138 9.319 -22.036 -40.252 1.00 94.55 A O ANISOU 4064 O LYS E 138 15529 9425 10973 -838 4356 114 A O ATOM 4065 CB LYS E 138 7.769 -24.382 -41.262 1.00 89.26 A C ANISOU 4065 CB LYS E 138 15045 8519 10349 -849 4596 160 A C ATOM 4066 CG LYS E 138 7.193 -24.499 -39.858 1.00 90.13 A C ANISOU 4066 CG LYS E 138 15004 8485 10755 -849 4655 -3 A C ATOM 4067 CD LYS E 138 6.911 -25.947 -39.494 1.00 97.22 A C ANISOU 4067 CD LYS E 138 15848 9293 11799 -923 4717 -188 A C ATOM 4068 CE LYS E 138 5.541 -26.096 -38.853 1.00 97.77 A C ANISOU 4068 CE LYS E 138 15906 9163 12079 -870 4918 -213 A C ATOM 4069 NZ LYS E 138 5.358 -27.440 -38.240 1.00 98.95 A N1+ ANISOU 4069 NZ LYS E 138 15971 9240 12384 -952 4964 -445 A N1+ ATOM 4070 N PRO E 139 7.304 -21.064 -40.318 1.00 86.61 A N ANISOU 4070 N PRO E 139 10966 10298 11643 -410 5213 2456 A N ATOM 4071 CA PRO E 139 7.694 -20.076 -39.307 1.00 80.84 A C ANISOU 4071 CA PRO E 139 10537 9300 10878 -374 4978 2080 A C ATOM 4072 C PRO E 139 7.880 -20.704 -37.934 1.00 81.88 A C ANISOU 4072 C PRO E 139 10607 9145 11358 -363 4779 1933 A C ATOM 4073 O PRO E 139 7.217 -21.677 -37.568 1.00 81.97 A O ANISOU 4073 O PRO E 139 10361 9043 11739 -464 4683 2159 A O ATOM 4074 CB PRO E 139 6.524 -19.083 -39.304 1.00 73.74 A C ANISOU 4074 CB PRO E 139 9740 8249 10031 -511 4753 2214 A C ATOM 4075 CG PRO E 139 5.766 -19.352 -40.571 1.00 84.13 A C ANISOU 4075 CG PRO E 139 10865 9813 11289 -604 4919 2626 A C ATOM 4076 CD PRO E 139 5.961 -20.805 -40.858 1.00 88.90 A C ANISOU 4076 CD PRO E 139 11152 10580 12046 -590 5120 2832 A C ATOM 4077 N ILE E 140 8.809 -20.129 -37.174 1.00 86.66 A N ANISOU 4077 N ILE E 140 11443 9645 11840 -251 4704 1567 A N ATOM 4078 CA ILE E 140 9.055 -20.494 -35.784 1.00 76.74 A C ANISOU 4078 CA ILE E 140 10176 8134 10848 -228 4489 1395 A C ATOM 4079 C ILE E 140 8.609 -19.327 -34.917 1.00 75.96 A C ANISOU 4079 C ILE E 140 10313 7808 10741 -261 4198 1225 A C ATOM 4080 O ILE E 140 8.909 -18.167 -35.225 1.00 67.35 A O ANISOU 4080 O ILE E 140 9448 6792 9351 -219 4223 1093 A O ATOM 4081 CB ILE E 140 10.536 -20.830 -35.531 1.00 70.97 A C ANISOU 4081 CB ILE E 140 9495 7476 9996 -52 4640 1144 A C ATOM 4082 CG1 ILE E 140 11.098 -21.696 -36.661 1.00 86.62 A C ANISOU 4082 CG1 ILE E 140 11314 9746 11853 49 4996 1265 A C ATOM 4083 CG2 ILE E 140 10.707 -21.510 -34.176 1.00 76.86 A C ANISOU 4083 CG2 ILE E 140 10140 8008 11056 -40 4438 1063 A C ATOM 4084 CD1 ILE E 140 10.862 -23.179 -36.486 1.00 88.54 A C ANISOU 4084 CD1 ILE E 140 11194 10016 12431 39 5054 1510 A C ATOM 4085 N TYR E 141 7.898 -19.632 -33.839 1.00 76.05 A N ANISOU 4085 N TYR E 141 10267 7558 11070 -328 3919 1230 A N ATOM 4086 CA TYR E 141 7.275 -18.603 -33.022 1.00 75.87 A C ANISOU 4086 CA TYR E 141 10449 7325 11054 -333 3645 1092 A C ATOM 4087 C TYR E 141 8.278 -17.985 -32.054 1.00 76.00 A C ANISOU 4087 C TYR E 141 10652 7321 10905 -197 3575 772 A C ATOM 4088 O TYR E 141 9.210 -18.644 -31.583 1.00 64.53 A O ANISOU 4088 O TYR E 141 9135 5894 9492 -131 3624 665 A O ATOM 4089 CB TYR E 141 6.093 -19.197 -32.256 1.00 66.48 A C ANISOU 4089 CB TYR E 141 9151 5851 10256 -449 3354 1196 A C ATOM 4090 CG TYR E 141 4.995 -19.708 -33.158 1.00 74.97 A C ANISOU 4090 CG TYR E 141 10038 6907 11539 -613 3377 1557 A C ATOM 4091 CD1 TYR E 141 4.397 -18.880 -34.100 1.00 78.78 A C ANISOU 4091 CD1 TYR E 141 10599 7463 11872 -644 3452 1711 A C ATOM 4092 CD2 TYR E 141 4.541 -21.017 -33.055 1.00 80.58 A C ANISOU 4092 CD2 TYR E 141 10474 7535 12610 -749 3307 1780 A C ATOM 4093 CE1 TYR E 141 3.388 -19.343 -34.923 1.00 80.26 A C ANISOU 4093 CE1 TYR E 141 10599 7637 12259 -800 3467 2085 A C ATOM 4094 CE2 TYR E 141 3.536 -21.492 -33.882 1.00 83.64 A C ANISOU 4094 CE2 TYR E 141 10661 7909 13208 -919 3318 2162 A C ATOM 4095 CZ TYR E 141 2.959 -20.648 -34.807 1.00 98.56 A C ANISOU 4095 CZ TYR E 141 12639 9867 14943 -942 3400 2315 A C ATOM 4096 OH TYR E 141 1.955 -21.112 -35.625 1.00 84.00 A O ANISOU 4096 OH TYR E 141 10583 8015 13318 -1117 3406 2734 A O ATOM 4097 N HIS E 142 8.081 -16.700 -31.770 1.00 69.77 A N ANISOU 4097 N HIS E 142 10076 6497 9934 -150 3464 653 A N ATOM 4098 CA HIS E 142 8.900 -15.988 -30.803 1.00 61.68 A C ANISOU 4098 CA HIS E 142 9212 5468 8754 -31 3375 401 A C ATOM 4099 C HIS E 142 8.373 -16.213 -29.386 1.00 58.01 A C ANISOU 4099 C HIS E 142 8753 4791 8499 0 3089 292 A C ATOM 4100 O HIS E 142 7.260 -16.701 -29.174 1.00 63.39 A O ANISOU 4100 O HIS E 142 9363 5288 9435 -76 2924 383 A O ATOM 4101 CB HIS E 142 8.924 -14.490 -31.108 1.00 67.14 A C ANISOU 4101 CB HIS E 142 10099 6262 9150 12 3384 357 A C ATOM 4102 CG HIS E 142 9.591 -14.140 -32.401 1.00 64.28 A C ANISOU 4102 CG HIS E 142 9774 6124 8524 -18 3625 413 A C ATOM 4103 CD2 HIS E 142 9.160 -14.233 -33.681 1.00 70.70 A C ANISOU 4103 CD2 HIS E 142 10533 7063 9267 -98 3781 604 A C ATOM 4104 ND1 HIS E 142 10.858 -13.601 -32.463 1.00 68.75 A N ANISOU 4104 ND1 HIS E 142 10458 6815 8849 33 3711 261 A N ATOM 4105 CE1 HIS E 142 11.182 -13.385 -33.726 1.00 76.63 A C ANISOU 4105 CE1 HIS E 142 11493 7993 9629 -12 3897 321 A C ATOM 4106 NE2 HIS E 142 10.169 -13.761 -34.485 1.00 78.02 A N ANISOU 4106 NE2 HIS E 142 11561 8197 9884 -83 3955 532 A N ATOM 4107 N PHE E 143 9.190 -15.838 -28.404 1.00 63.72 A N ANISOU 4107 N PHE E 143 9566 5538 9106 110 3016 97 A N ATOM 4108 CA PHE E 143 8.803 -15.883 -26.998 1.00 67.06 A C ANISOU 4108 CA PHE E 143 10027 5817 9636 174 2747 -40 A C ATOM 4109 C PHE E 143 9.191 -14.565 -26.345 1.00 71.06 A C ANISOU 4109 C PHE E 143 10713 6420 9868 313 2692 -185 A C ATOM 4110 O PHE E 143 10.368 -14.189 -26.355 1.00 63.31 A O ANISOU 4110 O PHE E 143 9761 5591 8704 358 2810 -230 A O ATOM 4111 CB PHE E 143 9.462 -17.057 -26.270 1.00 72.71 A C ANISOU 4111 CB PHE E 143 10596 6505 10523 170 2699 -83 A C ATOM 4112 CG PHE E 143 8.983 -17.237 -24.855 1.00 65.92 A C ANISOU 4112 CG PHE E 143 9767 5512 9767 217 2398 -218 A C ATOM 4113 CD1 PHE E 143 7.629 -17.305 -24.575 1.00 63.48 A C ANISOU 4113 CD1 PHE E 143 9498 4998 9623 169 2171 -223 A C ATOM 4114 CD2 PHE E 143 9.884 -17.339 -23.808 1.00 72.22 A C ANISOU 4114 CD2 PHE E 143 10563 6384 10493 312 2328 -340 A C ATOM 4115 CE1 PHE E 143 7.181 -17.470 -23.278 1.00 71.90 A C ANISOU 4115 CE1 PHE E 143 10625 5940 10755 223 1875 -388 A C ATOM 4116 CE2 PHE E 143 9.440 -17.506 -22.506 1.00 68.06 A C ANISOU 4116 CE2 PHE E 143 10072 5772 10016 364 2045 -471 A C ATOM 4117 CZ PHE E 143 8.087 -17.572 -22.242 1.00 62.09 A C ANISOU 4117 CZ PHE E 143 9377 4815 9397 323 1816 -516 A C ATOM 4118 N LEU E 144 8.200 -13.865 -25.790 1.00 61.26 A N ANISOU 4118 N LEU E 144 9585 5087 8606 389 2512 -244 A N ATOM 4119 CA LEU E 144 8.392 -12.605 -25.075 1.00 68.68 A C ANISOU 4119 CA LEU E 144 10666 6142 9286 552 2452 -354 A C ATOM 4120 C LEU E 144 9.067 -11.541 -25.933 1.00 70.28 A C ANISOU 4120 C LEU E 144 10918 6555 9231 547 2644 -268 A C ATOM 4121 O LEU E 144 9.614 -10.568 -25.404 1.00 65.84 A O ANISOU 4121 O LEU E 144 10423 6148 8447 653 2632 -313 A O ATOM 4122 CB LEU E 144 9.190 -12.818 -23.783 1.00 68.77 A C ANISOU 4122 CB LEU E 144 10669 6219 9242 649 2348 -494 A C ATOM 4123 CG LEU E 144 8.536 -13.709 -22.728 1.00 65.32 A C ANISOU 4123 CG LEU E 144 10209 5608 9002 671 2103 -611 A C ATOM 4124 CD1 LEU E 144 9.517 -14.021 -21.610 1.00 54.48 A C ANISOU 4124 CD1 LEU E 144 8791 4351 7557 744 2034 -701 A C ATOM 4125 CD2 LEU E 144 7.284 -13.048 -22.180 1.00 59.72 A C ANISOU 4125 CD2 LEU E 144 9650 4782 8260 798 1910 -722 A C ATOM 4126 N GLY E 145 9.038 -11.703 -27.255 1.00 62.67 A N ANISOU 4126 N GLY E 145 9913 5616 8281 419 2812 -129 A N ATOM 4127 CA GLY E 145 9.729 -10.789 -28.141 1.00 63.13 A C ANISOU 4127 CA GLY E 145 10025 5874 8088 386 2973 -60 A C ATOM 4128 C GLY E 145 11.237 -10.851 -28.074 1.00 70.51 A C ANISOU 4128 C GLY E 145 10960 6923 8906 372 3068 -129 A C ATOM 4129 O GLY E 145 11.902 -9.978 -28.638 1.00 74.23 A O ANISOU 4129 O GLY E 145 11499 7545 9160 339 3149 -98 A O ATOM 4130 N THR E 146 11.798 -11.858 -27.405 1.00 59.30 A N ANISOU 4130 N THR E 146 9466 5425 7640 388 3042 -211 A N ATOM 4131 CA THR E 146 13.243 -11.975 -27.239 1.00 68.73 A C ANISOU 4131 CA THR E 146 10661 6682 8769 393 3112 -272 A C ATOM 4132 C THR E 146 13.799 -13.198 -27.954 1.00 71.97 A C ANISOU 4132 C THR E 146 10983 7042 9318 338 3275 -267 A C ATOM 4133 O THR E 146 14.598 -13.047 -28.884 1.00 69.58 A O ANISOU 4133 O THR E 146 10737 6811 8890 299 3433 -275 A O ATOM 4134 CB THR E 146 13.594 -12.011 -25.745 1.00 62.63 A C ANISOU 4134 CB THR E 146 9867 5898 8031 498 2949 -351 A C ATOM 4135 CG2 THR E 146 13.359 -10.648 -25.112 1.00 66.88 A C ANISOU 4135 CG2 THR E 146 10490 6562 8359 585 2841 -343 A C ATOM 4136 OG1 THR E 146 12.776 -12.984 -25.084 1.00 66.59 A O ANISOU 4136 OG1 THR E 146 10285 6265 8752 522 2825 -384 A O ATOM 4137 N SER E 147 13.401 -14.404 -27.548 1.00 73.72 A N ANISOU 4137 N SER E 147 11068 7153 9791 342 3233 -256 A N ATOM 4138 CA SER E 147 13.826 -15.654 -28.181 1.00 66.37 A C ANISOU 4138 CA SER E 147 10004 6200 9012 317 3399 -214 A C ATOM 4139 C SER E 147 15.351 -15.738 -28.262 1.00 69.46 A C ANISOU 4139 C SER E 147 10434 6626 9331 376 3519 -300 A C ATOM 4140 O SER E 147 15.947 -15.784 -29.340 1.00 66.89 A O ANISOU 4140 O SER E 147 10156 6360 8898 369 3716 -314 A O ATOM 4141 CB SER E 147 13.190 -15.804 -29.565 1.00 54.67 A C ANISOU 4141 CB SER E 147 8495 4779 7499 236 3566 -91 A C ATOM 4142 OG SER E 147 11.897 -16.375 -29.476 1.00 67.87 A O ANISOU 4142 OG SER E 147 10046 6357 9386 171 3467 32 A O ATOM 4143 N THR E 148 15.978 -15.761 -27.088 1.00 65.86 A N ANISOU 4143 N THR E 148 9966 6126 8930 442 3386 -361 A N ATOM 4144 CA THR E 148 17.429 -15.709 -26.983 1.00 67.47 A C ANISOU 4144 CA THR E 148 10220 6320 9094 497 3450 -427 A C ATOM 4145 C THR E 148 18.083 -17.084 -27.040 1.00 65.61 A C ANISOU 4145 C THR E 148 9837 6016 9077 566 3567 -422 A C ATOM 4146 O THR E 148 19.297 -17.186 -26.839 1.00 76.51 A O ANISOU 4146 O THR E 148 11247 7343 10480 636 3604 -474 A O ATOM 4147 CB THR E 148 17.840 -14.991 -25.697 1.00 65.97 A C ANISOU 4147 CB THR E 148 10071 6144 8849 537 3255 -445 A C ATOM 4148 CG2 THR E 148 17.244 -13.591 -25.664 1.00 67.82 A C ANISOU 4148 CG2 THR E 148 10429 6482 8857 501 3165 -430 A C ATOM 4149 OG1 THR E 148 17.376 -15.729 -24.560 1.00 65.23 A O ANISOU 4149 OG1 THR E 148 9840 6016 8927 584 3100 -426 A O ATOM 4150 N PHE E 149 17.313 -18.141 -27.305 1.00 73.37 A N ANISOU 4150 N PHE E 149 10647 6993 10238 550 3619 -336 A N ATOM 4151 CA PHE E 149 17.877 -19.454 -27.594 1.00 57.39 A C ANISOU 4151 CA PHE E 149 8450 4949 8406 629 3779 -293 A C ATOM 4152 C PHE E 149 18.246 -19.606 -29.063 1.00 71.42 A C ANISOU 4152 C PHE E 149 10276 6798 10061 665 4065 -312 A C ATOM 4153 O PHE E 149 18.217 -20.720 -29.603 1.00 74.68 A O ANISOU 4153 O PHE E 149 10510 7258 10608 723 4241 -225 A O ATOM 4154 CB PHE E 149 16.910 -20.557 -27.159 1.00 73.41 A C ANISOU 4154 CB PHE E 149 10234 6963 10697 582 3688 -153 A C ATOM 4155 CG PHE E 149 16.779 -20.693 -25.667 1.00 79.09 A C ANISOU 4155 CG PHE E 149 10890 7617 11542 580 3412 -160 A C ATOM 4156 CD1 PHE E 149 17.628 -20.004 -24.814 1.00 71.95 A C ANISOU 4156 CD1 PHE E 149 10105 6701 10531 647 3306 -253 A C ATOM 4157 CD2 PHE E 149 15.809 -21.516 -25.117 1.00 61.15 A C ANISOU 4157 CD2 PHE E 149 8437 5307 9489 504 3243 -62 A C ATOM 4158 CE1 PHE E 149 17.510 -20.128 -23.442 1.00 74.46 A C ANISOU 4158 CE1 PHE E 149 10363 7007 10921 660 3059 -251 A C ATOM 4159 CE2 PHE E 149 15.687 -21.644 -23.745 1.00 67.03 A C ANISOU 4159 CE2 PHE E 149 9144 6013 10312 507 2971 -92 A C ATOM 4160 CZ PHE E 149 16.538 -20.950 -22.907 1.00 61.96 A C ANISOU 4160 CZ PHE E 149 8621 5395 9523 597 2890 -189 A C ATOM 4161 N SER E 150 18.574 -18.499 -29.722 1.00 73.41 A N ANISOU 4161 N SER E 150 10760 7086 10046 635 4111 -415 A N ATOM 4162 CA SER E 150 19.060 -18.481 -31.089 1.00 71.25 A C ANISOU 4162 CA SER E 150 10591 6891 9588 677 4356 -483 A C ATOM 4163 C SER E 150 20.351 -17.679 -31.131 1.00 78.34 A C ANISOU 4163 C SER E 150 11726 7707 10333 714 4338 -663 A C ATOM 4164 O SER E 150 20.527 -16.723 -30.372 1.00 76.61 A O ANISOU 4164 O SER E 150 11609 7434 10066 644 4136 -684 A O ATOM 4165 CB SER E 150 18.027 -17.870 -32.048 1.00 65.03 A C ANISOU 4165 CB SER E 150 9860 6247 8603 560 4401 -409 A C ATOM 4166 OG SER E 150 18.566 -17.710 -33.348 1.00 71.01 A O ANISOU 4166 OG SER E 150 10753 7111 9117 600 4615 -497 A O ATOM 4167 N GLU E 151 21.261 -18.081 -32.020 1.00 79.40 A N ANISOU 4167 N GLU E 151 11945 7831 10394 830 4545 -786 A N ATOM 4168 CA GLU E 151 22.526 -17.364 -32.131 1.00 82.57 A C ANISOU 4168 CA GLU E 151 12593 8102 10676 852 4505 -971 A C ATOM 4169 C GLU E 151 22.311 -15.933 -32.608 1.00 79.63 A C ANISOU 4169 C GLU E 151 12436 7803 10018 681 4393 -1011 A C ATOM 4170 O GLU E 151 23.078 -15.034 -32.245 1.00 85.39 A O ANISOU 4170 O GLU E 151 13325 8424 10693 614 4233 -1081 A O ATOM 4171 CB GLU E 151 23.475 -18.122 -33.058 1.00 69.57 A C ANISOU 4171 CB GLU E 151 11011 6426 8997 1029 4724 -1120 A C ATOM 4172 CG GLU E 151 24.027 -19.398 -32.433 1.00 75.30 A C ANISOU 4172 CG GLU E 151 11538 7044 10028 1220 4798 -1082 A C ATOM 4173 CD GLU E 151 24.942 -20.170 -33.363 1.00 73.97 A C ANISOU 4173 CD GLU E 151 11395 6894 9817 1407 4944 -1197 A C ATOM 4174 OE1 GLU E 151 24.785 -20.047 -34.596 1.00 77.11 A O ANISOU 4174 OE1 GLU E 151 11885 7460 9952 1408 5047 -1266 A O ATOM 4175 OE2 GLU E 151 25.818 -20.903 -32.859 1.00 82.27 A O1- ANISOU 4175 OE2 GLU E 151 12372 7799 11089 1570 4954 -1216 A O1- ATOM 4176 N TYR E 152 21.274 -15.704 -33.411 1.00 80.56 A N ANISOU 4176 N TYR E 152 12535 8109 9964 601 4465 -932 A N ATOM 4177 CA TYR E 152 20.847 -14.369 -33.804 1.00 73.85 A C ANISOU 4177 CA TYR E 152 11833 7363 8862 437 4349 -910 A C ATOM 4178 C TYR E 152 19.346 -14.259 -33.592 1.00 79.34 A C ANISOU 4178 C TYR E 152 12370 8178 9597 359 4294 -707 A C ATOM 4179 O TYR E 152 18.600 -15.190 -33.908 1.00 74.51 A O ANISOU 4179 O TYR E 152 11590 7632 9088 400 4425 -603 A O ATOM 4180 CB TYR E 152 21.192 -14.065 -35.268 1.00 73.73 A C ANISOU 4180 CB TYR E 152 12011 7463 8539 421 4493 -1034 A C ATOM 4181 CG TYR E 152 22.672 -13.997 -35.552 1.00 89.31 A C ANISOU 4181 CG TYR E 152 14196 9283 10455 482 4487 -1269 A C ATOM 4182 CD1 TYR E 152 23.455 -15.144 -35.550 1.00 86.58 A C ANISOU 4182 CD1 TYR E 152 13784 8834 10281 668 4583 -1358 A C ATOM 4183 CD2 TYR E 152 23.290 -12.781 -35.813 1.00 85.87 A C ANISOU 4183 CD2 TYR E 152 14007 8803 9816 344 4338 -1377 A C ATOM 4184 CE1 TYR E 152 24.807 -15.084 -35.802 1.00 95.90 A C ANISOU 4184 CE1 TYR E 152 15158 9844 11437 733 4537 -1570 A C ATOM 4185 CE2 TYR E 152 24.643 -12.712 -36.068 1.00 90.24 A C ANISOU 4185 CE2 TYR E 152 14784 9161 10341 385 4308 -1606 A C ATOM 4186 CZ TYR E 152 25.395 -13.867 -36.061 1.00 95.05 A C ANISOU 4186 CZ TYR E 152 15328 9650 11137 586 4392 -1702 A C ATOM 4187 OH TYR E 152 26.741 -13.805 -36.312 1.00108.92 A O ANISOU 4187 OH TYR E 152 17299 11190 12895 638 4323 -1924 A O ATOM 4188 N THR E 153 18.905 -13.125 -33.051 1.00 65.59 A N ANISOU 4188 N THR E 153 10675 6459 7787 254 4096 -639 A N ATOM 4189 CA THR E 153 17.488 -12.925 -32.776 1.00 58.39 A C ANISOU 4189 CA THR E 153 9646 5616 6925 204 4019 -471 A C ATOM 4190 C THR E 153 17.106 -11.477 -33.038 1.00 71.71 A C ANISOU 4190 C THR E 153 11448 7417 8381 97 3905 -411 A C ATOM 4191 O THR E 153 17.941 -10.578 -32.954 1.00 65.71 A O ANISOU 4191 O THR E 153 10821 6663 7484 48 3816 -475 A O ATOM 4192 CB THR E 153 17.131 -13.303 -31.330 1.00 67.65 A C ANISOU 4192 CB THR E 153 10682 6673 8350 258 3863 -430 A C ATOM 4193 CG2 THR E 153 18.147 -12.721 -30.364 1.00 65.04 A C ANISOU 4193 CG2 THR E 153 10425 6273 8016 280 3722 -505 A C ATOM 4194 OG1 THR E 153 15.833 -12.795 -31.007 1.00 70.59 A O ANISOU 4194 OG1 THR E 153 11010 7080 8731 218 3741 -313 A O ATOM 4195 N VAL E 154 15.832 -11.250 -33.348 1.00 67.82 A N ANISOU 4195 N VAL E 154 10891 7008 7869 57 3896 -262 A N ATOM 4196 CA VAL E 154 15.319 -9.915 -33.637 1.00 63.65 A C ANISOU 4196 CA VAL E 154 10439 6606 7140 -23 3800 -165 A C ATOM 4197 C VAL E 154 14.429 -9.475 -32.484 1.00 61.79 A C ANISOU 4197 C VAL E 154 10129 6315 7033 29 3628 -83 A C ATOM 4198 O VAL E 154 13.497 -10.193 -32.102 1.00 76.78 A O ANISOU 4198 O VAL E 154 11917 8119 9137 75 3610 -31 A O ATOM 4199 CB VAL E 154 14.556 -9.878 -34.972 1.00 70.13 A C ANISOU 4199 CB VAL E 154 11256 7578 7813 -90 3923 -41 A C ATOM 4200 CG1 VAL E 154 13.983 -8.493 -35.215 1.00 67.44 A C ANISOU 4200 CG1 VAL E 154 10968 7370 7285 -163 3810 90 A C ATOM 4201 CG2 VAL E 154 15.478 -10.283 -36.113 1.00 57.28 A C ANISOU 4201 CG2 VAL E 154 9726 6041 5997 -110 4099 -156 A C ATOM 4202 N VAL E 155 14.719 -8.299 -31.928 1.00 71.37 A N ANISOU 4202 N VAL E 155 11401 7593 8124 25 3493 -68 A N ATOM 4203 CA VAL E 155 14.010 -7.776 -30.766 1.00 67.98 A C ANISOU 4203 CA VAL E 155 10919 7148 7764 120 3341 -15 A C ATOM 4204 C VAL E 155 13.636 -6.324 -31.032 1.00 72.22 A C ANISOU 4204 C VAL E 155 11493 7857 8092 94 3274 119 A C ATOM 4205 O VAL E 155 14.418 -5.569 -31.619 1.00 73.18 A O ANISOU 4205 O VAL E 155 11683 8102 8021 -12 3276 145 A O ATOM 4206 CB VAL E 155 14.862 -7.887 -29.481 1.00 67.52 A C ANISOU 4206 CB VAL E 155 10841 7032 7782 194 3245 -103 A C ATOM 4207 CG1 VAL E 155 14.083 -7.385 -28.274 1.00 54.24 A C ANISOU 4207 CG1 VAL E 155 9111 5373 6126 327 3100 -67 A C ATOM 4208 CG2 VAL E 155 15.324 -9.319 -29.259 1.00 49.48 A C ANISOU 4208 CG2 VAL E 155 8501 4591 5707 221 3310 -213 A C ATOM 4209 N HIS E 156 12.434 -5.938 -30.608 1.00 72.66 A N ANISOU 4209 N HIS E 156 11503 7910 8193 194 3202 205 A N ATOM 4210 CA HIS E 156 12.037 -4.537 -30.649 1.00 65.65 A C ANISOU 4210 CA HIS E 156 10619 7196 7129 221 3135 351 A C ATOM 4211 C HIS E 156 13.000 -3.701 -29.814 1.00 66.39 A C ANISOU 4211 C HIS E 156 10705 7415 7104 245 3048 357 A C ATOM 4212 O HIS E 156 13.444 -4.123 -28.742 1.00 65.73 A O ANISOU 4212 O HIS E 156 10597 7263 7113 328 2999 260 A O ATOM 4213 CB HIS E 156 10.604 -4.383 -30.136 1.00 57.75 A C ANISOU 4213 CB HIS E 156 9582 6123 6237 383 3068 405 A C ATOM 4214 CG HIS E 156 10.030 -3.013 -30.325 1.00 66.55 A C ANISOU 4214 CG HIS E 156 10682 7414 7191 444 3027 582 A C ATOM 4215 CD2 HIS E 156 9.146 -2.534 -31.232 1.00 73.60 A C ANISOU 4215 CD2 HIS E 156 11564 8356 8044 422 3052 750 A C ATOM 4216 ND1 HIS E 156 10.350 -1.952 -29.506 1.00 69.35 A N ANISOU 4216 ND1 HIS E 156 11002 7940 7406 553 2953 635 A N ATOM 4217 CE1 HIS E 156 9.693 -0.877 -29.903 1.00 75.98 A C ANISOU 4217 CE1 HIS E 156 11808 8931 8132 605 2941 821 A C ATOM 4218 NE2 HIS E 156 8.955 -1.203 -30.949 1.00 79.84 A N ANISOU 4218 NE2 HIS E 156 12316 9338 8682 526 2994 891 A N ATOM 4219 N SER E 157 13.331 -2.508 -30.316 1.00 71.27 A N ANISOU 4219 N SER E 157 11327 8235 7518 157 3019 501 A N ATOM 4220 CA SER E 157 14.365 -1.696 -29.681 1.00 70.16 A C ANISOU 4220 CA SER E 157 11157 8227 7273 125 2930 559 A C ATOM 4221 C SER E 157 13.977 -1.244 -28.280 1.00 67.85 A C ANISOU 4221 C SER E 157 10771 8016 6993 340 2856 610 A C ATOM 4222 O SER E 157 14.862 -0.941 -27.472 1.00 67.86 A O ANISOU 4222 O SER E 157 10724 8096 6963 344 2793 643 A O ATOM 4223 CB SER E 157 14.687 -0.477 -30.547 1.00 63.84 A C ANISOU 4223 CB SER E 157 10357 7639 6261 -34 2887 739 A C ATOM 4224 OG SER E 157 13.638 0.472 -30.499 1.00 74.15 A O ANISOU 4224 OG SER E 157 11577 9115 7483 81 2865 927 A O ATOM 4225 N GLY E 158 12.682 -1.188 -27.972 1.00 58.97 A N ANISOU 4225 N GLY E 158 9623 6874 5908 529 2859 619 A N ATOM 4226 CA GLY E 158 12.253 -0.867 -26.623 1.00 57.01 A C ANISOU 4226 CA GLY E 158 9318 6698 5647 777 2796 612 A C ATOM 4227 C GLY E 158 12.525 -1.953 -25.603 1.00 62.58 A C ANISOU 4227 C GLY E 158 10040 7247 6493 856 2762 420 A C ATOM 4228 O GLY E 158 12.410 -1.692 -24.401 1.00 65.13 A O ANISOU 4228 O GLY E 158 10318 7670 6758 1054 2701 405 A O ATOM 4229 N GLN E 159 12.878 -3.158 -26.052 1.00 67.90 A N ANISOU 4229 N GLN E 159 10764 7704 7331 720 2804 285 A N ATOM 4230 CA GLN E 159 13.222 -4.266 -25.172 1.00 74.40 A C ANISOU 4230 CA GLN E 159 11581 8384 8305 769 2767 127 A C ATOM 4231 C GLN E 159 14.719 -4.539 -25.145 1.00 72.54 A C ANISOU 4231 C GLN E 159 11331 8149 8081 631 2782 128 A C ATOM 4232 O GLN E 159 15.141 -5.592 -24.654 1.00 72.54 A O ANISOU 4232 O GLN E 159 11317 8012 8232 639 2772 15 A O ATOM 4233 CB GLN E 159 12.475 -5.532 -25.600 1.00 73.57 A C ANISOU 4233 CB GLN E 159 11509 8027 8418 740 2798 1 A C ATOM 4234 CG GLN E 159 11.022 -5.585 -25.172 1.00 69.08 A C ANISOU 4234 CG GLN E 159 10963 7363 7923 902 2719 -49 A C ATOM 4235 CD GLN E 159 10.257 -6.697 -25.861 1.00 75.56 A C ANISOU 4235 CD GLN E 159 11794 7942 8975 811 2743 -96 A C ATOM 4236 NE2 GLN E 159 9.690 -6.392 -27.023 1.00 76.22 A N ANISOU 4236 NE2 GLN E 159 11891 8021 9048 727 2820 24 A N ATOM 4237 OE1 GLN E 159 10.176 -7.816 -25.357 1.00 80.83 A O ANISOU 4237 OE1 GLN E 159 12437 8446 9829 810 2687 -209 A O ATOM 4238 N VAL E 160 15.529 -3.622 -25.662 1.00 63.83 A N ANISOU 4238 N VAL E 160 10229 7184 6840 501 2788 260 A N ATOM 4239 CA VAL E 160 16.962 -3.828 -25.833 1.00 68.07 A C ANISOU 4239 CA VAL E 160 10787 7666 7412 346 2785 255 A C ATOM 4240 C VAL E 160 17.666 -2.746 -25.026 1.00 69.82 A C ANISOU 4240 C VAL E 160 10922 8097 7511 352 2685 441 A C ATOM 4241 O VAL E 160 17.739 -1.587 -25.454 1.00 70.19 A O ANISOU 4241 O VAL E 160 10945 8321 7404 269 2654 611 A O ATOM 4242 CB VAL E 160 17.376 -3.784 -27.308 1.00 69.66 A C ANISOU 4242 CB VAL E 160 11090 7807 7571 146 2855 234 A C ATOM 4243 CG1 VAL E 160 18.878 -3.840 -27.438 1.00 74.47 A C ANISOU 4243 CG1 VAL E 160 11751 8334 8211 2 2820 213 A C ATOM 4244 CG2 VAL E 160 16.733 -4.928 -28.071 1.00 59.45 A C ANISOU 4244 CG2 VAL E 160 9846 6348 6393 153 2975 90 A C ATOM 4245 N ALA E 161 18.189 -3.111 -23.857 1.00 59.96 A N ANISOU 4245 N ALA E 161 9605 6852 6327 441 2628 443 A N ATOM 4246 CA ALA E 161 18.846 -2.156 -22.974 1.00 63.17 A C ANISOU 4246 CA ALA E 161 9894 7488 6621 460 2538 662 A C ATOM 4247 C ALA E 161 20.337 -2.117 -23.286 1.00 72.32 A C ANISOU 4247 C ALA E 161 11073 8542 7865 239 2484 737 A C ATOM 4248 O ALA E 161 21.018 -3.144 -23.213 1.00 74.18 A O ANISOU 4248 O ALA E 161 11356 8550 8279 207 2494 610 A O ATOM 4249 CB ALA E 161 18.610 -2.526 -21.511 1.00 52.09 A C ANISOU 4249 CB ALA E 161 8400 6180 5213 683 2495 650 A C ATOM 4250 N LYS E 162 20.838 -0.935 -23.638 1.00 60.08 A N ANISOU 4250 N LYS E 162 9483 7143 6202 86 2415 950 A N ATOM 4251 CA LYS E 162 22.265 -0.748 -23.865 1.00 69.06 A C ANISOU 4251 CA LYS E 162 10645 8164 7430 -141 2316 1043 A C ATOM 4252 C LYS E 162 22.984 -0.645 -22.526 1.00 63.80 A C ANISOU 4252 C LYS E 162 9825 7602 6815 -82 2229 1241 A C ATOM 4253 O LYS E 162 22.591 0.144 -21.661 1.00 70.06 A O ANISOU 4253 O LYS E 162 10448 8716 7455 45 2205 1461 A O ATOM 4254 CB LYS E 162 22.510 0.507 -24.701 1.00 59.56 A C ANISOU 4254 CB LYS E 162 9442 7092 6096 -356 2233 1225 A C ATOM 4255 CG LYS E 162 23.975 0.814 -24.961 1.00 62.22 A C ANISOU 4255 CG LYS E 162 9823 7281 6539 -623 2081 1326 A C ATOM 4256 CD LYS E 162 24.128 1.977 -25.928 1.00 69.52 A C ANISOU 4256 CD LYS E 162 10767 8317 7330 -866 1973 1472 A C ATOM 4257 CE LYS E 162 25.590 2.332 -26.142 1.00 84.73 A C ANISOU 4257 CE LYS E 162 12748 10064 9380 -1156 1774 1576 A C ATOM 4258 NZ LYS E 162 25.749 3.479 -27.079 1.00 84.34 A N1+ ANISOU 4258 NZ LYS E 162 12717 10129 9199 -1424 1628 1723 A N1+ ATOM 4259 N ILE E 163 24.037 -1.444 -22.351 1.00 54.06 A N ANISOU 4259 N ILE E 163 8640 6113 5787 -153 2189 1178 A N ATOM 4260 CA ILE E 163 24.746 -1.487 -21.075 1.00 62.39 A C ANISOU 4260 CA ILE E 163 9542 7252 6911 -96 2105 1381 A C ATOM 4261 C ILE E 163 26.214 -1.126 -21.258 1.00 73.93 A C ANISOU 4261 C ILE E 163 11014 8548 8528 -347 1961 1557 A C ATOM 4262 O ILE E 163 26.667 -0.846 -22.375 1.00 65.27 A O ANISOU 4262 O ILE E 163 10066 7263 7471 -560 1915 1483 A O ATOM 4263 CB ILE E 163 24.607 -2.867 -20.405 1.00 62.32 A C ANISOU 4263 CB ILE E 163 9542 7098 7039 88 2166 1191 A C ATOM 4264 CG1 ILE E 163 25.350 -3.936 -21.210 1.00 64.59 A C ANISOU 4264 CG1 ILE E 163 9993 6979 7571 -11 2201 964 A C ATOM 4265 CG2 ILE E 163 23.142 -3.237 -20.230 1.00 64.90 A C ANISOU 4265 CG2 ILE E 163 9875 7544 7241 306 2267 1010 A C ATOM 4266 CD1 ILE E 163 25.511 -5.248 -20.472 1.00 59.63 A C ANISOU 4266 CD1 ILE E 163 9323 6213 7120 139 2231 861 A C ATOM 4267 N ASN E 164 26.956 -1.129 -20.155 1.00 78.56 A N ANISOU 4267 N ASN E 164 11448 9199 9201 -324 1872 1794 A N ATOM 4268 CA ASN E 164 28.375 -0.807 -20.179 1.00 70.24 A C ANISOU 4268 CA ASN E 164 10387 7961 8341 -562 1706 2004 A C ATOM 4269 C ASN E 164 29.123 -1.814 -21.049 1.00 82.55 A C ANISOU 4269 C ASN E 164 12188 9026 10150 -651 1712 1700 A C ATOM 4270 O ASN E 164 28.997 -3.027 -20.829 1.00 70.93 A O ANISOU 4270 O ASN E 164 10762 7394 8794 -478 1817 1484 A O ATOM 4271 CB ASN E 164 28.921 -0.820 -18.750 1.00 77.68 A C ANISOU 4271 CB ASN E 164 11103 9074 9336 -478 1633 2321 A C ATOM 4272 CG ASN E 164 30.297 -0.191 -18.631 1.00 90.82 A C ANISOU 4272 CG ASN E 164 12698 10622 11189 -743 1430 2660 A C ATOM 4273 ND2 ASN E 164 30.947 -0.414 -17.495 1.00 83.32 A N ANISOU 4273 ND2 ASN E 164 11573 9738 10347 -690 1362 2931 A N ATOM 4274 OD1 ASN E 164 30.766 0.493 -19.538 1.00101.52 A O ANISOU 4274 OD1 ASN E 164 14149 11831 12592 -1002 1318 2694 A O ATOM 4275 N PRO E 165 29.895 -1.364 -22.043 1.00 90.96 A N ANISOU 4275 N PRO E 165 13413 9851 11299 -906 1599 1668 A N ATOM 4276 CA PRO E 165 30.603 -2.326 -22.907 1.00 80.00 A C ANISOU 4276 CA PRO E 165 12281 7998 10119 -945 1621 1340 A C ATOM 4277 C PRO E 165 31.607 -3.190 -22.164 1.00 80.97 A C ANISOU 4277 C PRO E 165 12376 7850 10537 -878 1576 1385 A C ATOM 4278 O PRO E 165 31.897 -4.307 -22.611 1.00 82.21 A O ANISOU 4278 O PRO E 165 12692 7689 10856 -775 1673 1091 A O ATOM 4279 CB PRO E 165 31.294 -1.429 -23.947 1.00 72.42 A C ANISOU 4279 CB PRO E 165 11484 6877 9156 -1250 1450 1348 A C ATOM 4280 CG PRO E 165 30.584 -0.119 -23.880 1.00 76.45 A C ANISOU 4280 CG PRO E 165 11828 7806 9412 -1347 1396 1618 A C ATOM 4281 CD PRO E 165 30.086 0.029 -22.481 1.00 72.74 A C ANISOU 4281 CD PRO E 165 11065 7696 8876 -1158 1445 1908 A C ATOM 4282 N ASP E 166 32.144 -2.714 -21.044 1.00 71.00 A N ANISOU 4282 N ASP E 166 10899 6727 9351 -920 1439 1770 A N ATOM 4283 CA ASP E 166 33.125 -3.460 -20.270 1.00 77.63 A C ANISOU 4283 CA ASP E 166 11683 7330 10481 -865 1375 1880 A C ATOM 4284 C ASP E 166 32.489 -4.411 -19.262 1.00 76.52 A C ANISOU 4284 C ASP E 166 11384 7381 10309 -576 1515 1862 A C ATOM 4285 O ASP E 166 33.206 -5.003 -18.449 1.00 81.32 A O ANISOU 4285 O ASP E 166 11893 7876 11129 -509 1460 2013 A O ATOM 4286 CB ASP E 166 34.069 -2.494 -19.549 1.00 78.72 A C ANISOU 4286 CB ASP E 166 11649 7531 10729 -1073 1141 2354 A C ATOM 4287 CG ASP E 166 34.942 -1.711 -20.510 1.00 79.61 A C ANISOU 4287 CG ASP E 166 11939 7346 10964 -1397 939 2371 A C ATOM 4288 OD1 ASP E 166 34.952 -2.050 -21.712 1.00 81.07 A O ANISOU 4288 OD1 ASP E 166 12410 7236 11157 -1434 985 1976 A O ATOM 4289 OD2 ASP E 166 35.617 -0.758 -20.066 1.00 99.90 A O1- ANISOU 4289 OD2 ASP E 166 14357 9988 13612 -1621 725 2787 A O1- ATOM 4290 N ALA E 167 31.168 -4.576 -19.299 1.00 70.86 A N ANISOU 4290 N ALA E 167 10643 6936 9346 -411 1673 1690 A N ATOM 4291 CA ALA E 167 30.554 -5.495 -18.350 1.00 70.09 A C ANISOU 4291 CA ALA E 167 10412 6997 9222 -159 1767 1653 A C ATOM 4292 C ALA E 167 30.550 -6.915 -18.911 1.00 76.48 A C ANISOU 4292 C ALA E 167 11359 7478 10220 -41 1895 1309 A C ATOM 4293 O ALA E 167 30.274 -7.112 -20.098 1.00 72.49 A O ANISOU 4293 O ALA E 167 11043 6800 9701 -77 1996 1025 A O ATOM 4294 CB ALA E 167 29.125 -5.069 -18.029 1.00 77.64 A C ANISOU 4294 CB ALA E 167 11282 8365 9853 -24 1851 1626 A C ATOM 4295 N PRO E 168 30.853 -7.914 -18.080 1.00 67.45 A N ANISOU 4295 N PRO E 168 10104 6277 9246 106 1896 1353 A N ATOM 4296 CA PRO E 168 30.859 -9.300 -18.567 1.00 73.65 A C ANISOU 4296 CA PRO E 168 10973 6784 10224 234 2025 1070 A C ATOM 4297 C PRO E 168 29.456 -9.802 -18.866 1.00 74.37 A C ANISOU 4297 C PRO E 168 11073 7037 10146 355 2171 828 A C ATOM 4298 O PRO E 168 28.643 -9.976 -17.953 1.00 73.59 A O ANISOU 4298 O PRO E 168 10830 7211 9921 473 2154 886 A O ATOM 4299 CB PRO E 168 31.509 -10.073 -17.413 1.00 71.43 A C ANISOU 4299 CB PRO E 168 10516 6476 10148 349 1953 1268 A C ATOM 4300 CG PRO E 168 31.210 -9.257 -16.201 1.00 71.25 A C ANISOU 4300 CG PRO E 168 10297 6863 9912 350 1835 1580 A C ATOM 4301 CD PRO E 168 31.184 -7.823 -16.648 1.00 71.23 A C ANISOU 4301 CD PRO E 168 10352 6982 9728 169 1781 1690 A C ATOM 4302 N LEU E 169 29.166 -10.030 -20.149 1.00 61.32 A N ANISOU 4302 N LEU E 169 9597 5216 8485 324 2303 558 A N ATOM 4303 CA LEU E 169 27.826 -10.451 -20.545 1.00 69.64 A C ANISOU 4303 CA LEU E 169 10657 6404 9401 408 2433 363 A C ATOM 4304 C LEU E 169 27.444 -11.771 -19.887 1.00 78.46 A C ANISOU 4304 C LEU E 169 11633 7523 10656 578 2475 318 A C ATOM 4305 O LEU E 169 26.299 -11.948 -19.449 1.00 80.53 A O ANISOU 4305 O LEU E 169 11814 7989 10796 650 2474 285 A O ATOM 4306 CB LEU E 169 27.745 -10.556 -22.069 1.00 67.90 A C ANISOU 4306 CB LEU E 169 10634 6004 9161 347 2573 120 A C ATOM 4307 CG LEU E 169 28.060 -9.267 -22.834 1.00 67.61 A C ANISOU 4307 CG LEU E 169 10749 5971 8970 156 2510 144 A C ATOM 4308 CD1 LEU E 169 28.221 -9.539 -24.322 1.00 63.74 A C ANISOU 4308 CD1 LEU E 169 10471 5278 8468 113 2638 -115 A C ATOM 4309 CD2 LEU E 169 26.984 -8.220 -22.589 1.00 65.12 A C ANISOU 4309 CD2 LEU E 169 10367 5990 8385 115 2467 257 A C ATOM 4310 N ASP E 170 28.402 -12.697 -19.780 1.00 78.53 A N ANISOU 4310 N ASP E 170 11608 7298 10931 643 2492 327 A N ATOM 4311 CA ASP E 170 28.177 -13.993 -19.152 1.00 74.42 A C ANISOU 4311 CA ASP E 170 10924 6780 10574 793 2515 323 A C ATOM 4312 C ASP E 170 27.809 -13.887 -17.678 1.00 75.81 A C ANISOU 4312 C ASP E 170 10918 7230 10658 845 2355 517 A C ATOM 4313 O ASP E 170 27.392 -14.891 -17.090 1.00 78.08 A O ANISOU 4313 O ASP E 170 11065 7572 11029 949 2337 509 A O ATOM 4314 CB ASP E 170 29.420 -14.873 -19.304 1.00 73.64 A C ANISOU 4314 CB ASP E 170 10816 6377 10787 868 2560 335 A C ATOM 4315 CG ASP E 170 30.651 -14.267 -18.654 1.00 83.33 A C ANISOU 4315 CG ASP E 170 12034 7511 12118 812 2406 566 A C ATOM 4316 OD1 ASP E 170 31.025 -13.133 -19.023 1.00 84.89 A O ANISOU 4316 OD1 ASP E 170 12365 7677 12213 662 2343 605 A O ATOM 4317 OD2 ASP E 170 31.246 -14.924 -17.775 1.00 92.27 A O1- ANISOU 4317 OD2 ASP E 170 13010 8604 13446 904 2335 736 A O1- ATOM 4318 N LYS E 171 27.961 -12.713 -17.067 1.00 59.73 A N ANISOU 4318 N LYS E 171 8870 5386 8439 779 2234 700 A N ATOM 4319 CA LYS E 171 27.541 -12.485 -15.691 1.00 67.56 A C ANISOU 4319 CA LYS E 171 9703 6702 9264 854 2097 872 A C ATOM 4320 C LYS E 171 26.272 -11.647 -15.602 1.00 73.31 A C ANISOU 4320 C LYS E 171 10471 7711 9671 868 2090 798 A C ATOM 4321 O LYS E 171 25.341 -12.008 -14.878 1.00 79.64 A O ANISOU 4321 O LYS E 171 11207 8701 10353 979 2035 735 A O ATOM 4322 CB LYS E 171 28.666 -11.806 -14.899 1.00 74.82 A C ANISOU 4322 CB LYS E 171 10532 7692 10204 808 1971 1195 A C ATOM 4323 CG LYS E 171 30.016 -12.491 -15.013 1.00 84.13 A C ANISOU 4323 CG LYS E 171 11692 8543 11730 794 1961 1291 A C ATOM 4324 CD LYS E 171 29.952 -13.931 -14.535 1.00 85.95 A C ANISOU 4324 CD LYS E 171 11793 8718 12146 940 1971 1249 A C ATOM 4325 CE LYS E 171 31.333 -14.564 -14.518 1.00 93.51 A C ANISOU 4325 CE LYS E 171 12708 9364 13456 963 1955 1387 A C ATOM 4326 NZ LYS E 171 31.271 -16.026 -14.237 1.00 86.51 A N1+ ANISOU 4326 NZ LYS E 171 11684 8409 12776 1112 1990 1343 A N1+ ATOM 4327 N VAL E 172 26.213 -10.532 -16.339 1.00 63.49 A N ANISOU 4327 N VAL E 172 9342 6489 8292 761 2131 799 A N ATOM 4328 CA VAL E 172 25.095 -9.602 -16.223 1.00 75.70 A C ANISOU 4328 CA VAL E 172 10911 8312 9538 796 2126 772 A C ATOM 4329 C VAL E 172 23.908 -9.990 -17.094 1.00 78.63 A C ANISOU 4329 C VAL E 172 11394 8596 9887 814 2228 500 A C ATOM 4330 O VAL E 172 22.896 -9.275 -17.094 1.00 64.77 A O ANISOU 4330 O VAL E 172 9674 7023 7911 858 2229 457 A O ATOM 4331 CB VAL E 172 25.537 -8.165 -16.568 1.00 59.66 A C ANISOU 4331 CB VAL E 172 8911 6386 7369 670 2108 953 A C ATOM 4332 CG1 VAL E 172 26.667 -7.724 -15.650 1.00 60.13 A C ANISOU 4332 CG1 VAL E 172 8832 6555 7461 636 1990 1281 A C ATOM 4333 CG2 VAL E 172 25.953 -8.071 -18.028 1.00 60.96 A C ANISOU 4333 CG2 VAL E 172 9243 6261 7657 505 2192 826 A C ATOM 4334 N CYS E 173 23.990 -11.099 -17.835 1.00 75.70 A N ANISOU 4334 N CYS E 173 11064 7957 9740 792 2319 338 A N ATOM 4335 CA CYS E 173 22.841 -11.531 -18.623 1.00 73.01 A C ANISOU 4335 CA CYS E 173 10795 7552 9393 798 2411 131 A C ATOM 4336 C CYS E 173 21.657 -11.940 -17.752 1.00 67.16 A C ANISOU 4336 C CYS E 173 9987 6951 8579 916 2317 61 A C ATOM 4337 O CYS E 173 20.530 -12.008 -18.254 1.00 66.24 A O ANISOU 4337 O CYS E 173 9931 6812 8423 919 2351 -74 A O ATOM 4338 CB CYS E 173 23.240 -12.689 -19.537 1.00 68.32 A C ANISOU 4338 CB CYS E 173 10220 6688 9050 769 2541 13 A C ATOM 4339 SG CYS E 173 23.838 -14.148 -18.659 1.00 74.00 A S ANISOU 4339 SG CYS E 173 10765 7313 10038 869 2490 64 A S ATOM 4340 N ILE E 174 21.879 -12.205 -16.465 1.00 68.08 A N ANISOU 4340 N ILE E 174 9988 7206 8675 1010 2183 153 A N ATOM 4341 CA ILE E 174 20.816 -12.660 -15.574 1.00 67.08 A C ANISOU 4341 CA ILE E 174 9820 7199 8469 1123 2056 56 A C ATOM 4342 C ILE E 174 20.193 -11.474 -14.850 1.00 73.11 A C ANISOU 4342 C ILE E 174 10622 8251 8905 1233 1979 84 A C ATOM 4343 O ILE E 174 19.382 -11.647 -13.934 1.00 81.13 A O ANISOU 4343 O ILE E 174 11631 9405 9791 1361 1849 -6 A O ATOM 4344 CB ILE E 174 21.340 -13.697 -14.566 1.00 71.69 A C ANISOU 4344 CB ILE E 174 10254 7799 9185 1177 1939 127 A C ATOM 4345 CG1 ILE E 174 22.570 -13.153 -13.838 1.00 70.27 A C ANISOU 4345 CG1 ILE E 174 9990 7764 8946 1196 1897 372 A C ATOM 4346 CG2 ILE E 174 21.653 -15.009 -15.268 1.00 66.19 A C ANISOU 4346 CG2 ILE E 174 9498 6833 8816 1111 2021 77 A C ATOM 4347 CD1 ILE E 174 22.919 -13.904 -12.574 1.00 70.96 A C ANISOU 4347 CD1 ILE E 174 9921 7978 9063 1282 1745 480 A C ATOM 4348 N VAL E 175 20.571 -10.259 -15.253 1.00 76.79 A N ANISOU 4348 N VAL E 175 11128 8818 9231 1192 2052 207 A N ATOM 4349 CA VAL E 175 20.030 -9.050 -14.637 1.00 78.36 A C ANISOU 4349 CA VAL E 175 11335 9326 9113 1318 2011 272 A C ATOM 4350 C VAL E 175 18.720 -8.619 -15.288 1.00 77.60 A C ANISOU 4350 C VAL E 175 11365 9198 8923 1361 2058 100 A C ATOM 4351 O VAL E 175 17.969 -7.827 -14.697 1.00 79.81 A O ANISOU 4351 O VAL E 175 11664 9709 8949 1528 2017 87 A O ATOM 4352 CB VAL E 175 21.136 -7.969 -14.667 1.00 69.96 A C ANISOU 4352 CB VAL E 175 10205 8409 7968 1240 2043 551 A C ATOM 4353 CG1 VAL E 175 20.578 -6.549 -14.713 1.00 77.19 A C ANISOU 4353 CG1 VAL E 175 11136 9589 8605 1309 2076 638 A C ATOM 4354 CG2 VAL E 175 22.058 -8.139 -13.467 1.00 69.29 A C ANISOU 4354 CG2 VAL E 175 9967 8495 7863 1292 1944 763 A C ATOM 4355 N SER E 176 18.383 -9.168 -16.453 1.00 74.13 A N ANISOU 4355 N SER E 176 11005 8484 8678 1236 2142 -29 A N ATOM 4356 CA SER E 176 17.189 -8.773 -17.186 1.00 65.77 A C ANISOU 4356 CA SER E 176 10054 7370 7564 1253 2188 -149 A C ATOM 4357 C SER E 176 15.938 -9.544 -16.766 1.00 75.16 A C ANISOU 4357 C SER E 176 11290 8458 8808 1353 2082 -354 A C ATOM 4358 O SER E 176 14.977 -9.602 -17.543 1.00 72.60 A O ANISOU 4358 O SER E 176 11049 7983 8553 1322 2115 -454 A O ATOM 4359 CB SER E 176 17.423 -8.940 -18.688 1.00 69.50 A C ANISOU 4359 CB SER E 176 10582 7630 8195 1066 2331 -157 A C ATOM 4360 OG SER E 176 17.828 -10.263 -18.992 1.00 66.43 A O ANISOU 4360 OG SER E 176 10157 7020 8062 982 2360 -224 A O ATOM 4361 N CYS E 177 15.920 -10.129 -15.565 1.00 76.08 A N ANISOU 4361 N CYS E 177 11357 8651 8900 1460 1935 -408 A N ATOM 4362 CA CYS E 177 14.731 -10.848 -15.112 1.00 69.57 A C ANISOU 4362 CA CYS E 177 10593 7712 8127 1537 1785 -619 A C ATOM 4363 C CYS E 177 14.698 -11.054 -13.599 1.00 77.94 A C ANISOU 4363 C CYS E 177 11625 8969 9020 1705 1599 -676 A C ATOM 4364 O CYS E 177 15.102 -10.169 -12.838 1.00 83.44 A O ANISOU 4364 O CYS E 177 12293 9970 9441 1850 1600 -574 A O ATOM 4365 CB CYS E 177 14.625 -12.200 -15.821 1.00 77.87 A C ANISOU 4365 CB CYS E 177 11604 8466 9520 1361 1790 -674 A C ATOM 4366 SG CYS E 177 12.939 -12.849 -15.938 1.00 77.95 A S ANISOU 4366 SG CYS E 177 11711 8234 9674 1359 1638 -888 A S ATOM 4367 N GLY E 178 14.221 -12.227 -13.170 1.00 92.44 A N ANISOU 4367 N GLY E 178 13454 10655 11013 1678 1432 -820 A N ATOM 4368 CA GLY E 178 13.880 -12.540 -11.789 1.00 97.71 A C ANISOU 4368 CA GLY E 178 14135 11474 11515 1831 1206 -943 A C ATOM 4369 C GLY E 178 14.756 -11.978 -10.685 1.00 94.32 A C ANISOU 4369 C GLY E 178 13621 11421 10795 1979 1190 -797 A C ATOM 4370 O GLY E 178 14.246 -11.484 -9.669 1.00 98.27 A O ANISOU 4370 O GLY E 178 14194 12162 10982 2202 1074 -904 A O ATOM 4371 N LEU E 179 16.076 -12.067 -10.865 1.00 86.82 A N ANISOU 4371 N LEU E 179 10891 9625 12470 2027 3509 2009 A N ATOM 4372 CA LEU E 179 16.997 -11.501 -9.885 1.00 81.82 A C ANISOU 4372 CA LEU E 179 10425 8963 11698 1916 3252 1779 A C ATOM 4373 C LEU E 179 16.705 -10.023 -9.668 1.00 78.40 A C ANISOU 4373 C LEU E 179 10199 8748 10841 1731 2993 1542 A C ATOM 4374 O LEU E 179 16.498 -9.577 -8.533 1.00 78.83 A O ANISOU 4374 O LEU E 179 10199 8823 10930 1583 2647 1447 A O ATOM 4375 CB LEU E 179 18.444 -11.717 -10.340 1.00 77.06 A C ANISOU 4375 CB LEU E 179 10092 8266 10922 2040 3517 1677 A C ATOM 4376 CG LEU E 179 19.611 -10.946 -9.708 1.00 91.84 A C ANISOU 4376 CG LEU E 179 12304 10117 12473 1900 3326 1408 A C ATOM 4377 CD1 LEU E 179 20.852 -11.784 -9.868 1.00 94.02 A C ANISOU 4377 CD1 LEU E 179 12728 10168 12828 2096 3548 1421 A C ATOM 4378 CD2 LEU E 179 19.854 -9.567 -10.327 1.00 84.66 A C ANISOU 4378 CD2 LEU E 179 11764 9427 10975 1745 3317 1180 A C ATOM 4379 N SER E 180 16.669 -9.251 -10.757 1.00 74.86 A N ANISOU 4379 N SER E 180 9984 8474 9985 1744 3157 1451 A N ATOM 4380 CA SER E 180 16.364 -7.831 -10.646 1.00 79.98 A C ANISOU 4380 CA SER E 180 10772 9378 10239 1591 2918 1242 A C ATOM 4381 C SER E 180 14.927 -7.604 -10.205 1.00 78.14 A C ANISOU 4381 C SER E 180 10314 9220 10155 1581 2669 1317 A C ATOM 4382 O SER E 180 14.636 -6.594 -9.559 1.00 73.24 A O ANISOU 4382 O SER E 180 9703 8780 9343 1474 2391 1149 A O ATOM 4383 CB SER E 180 16.630 -7.130 -11.975 1.00 64.69 A C ANISOU 4383 CB SER E 180 9134 7593 7852 1613 3125 1154 A C ATOM 4384 OG SER E 180 17.984 -7.286 -12.364 1.00 84.49 A O ANISOU 4384 OG SER E 180 11932 10001 10169 1618 3331 1070 A O ATOM 4385 N THR E 181 14.025 -8.530 -10.530 1.00 69.64 A N ANISOU 4385 N THR E 181 9047 8007 9405 1690 2767 1570 A N ATOM 4386 CA THR E 181 12.654 -8.434 -10.041 1.00 69.56 A C ANISOU 4386 CA THR E 181 8881 7999 9551 1676 2498 1661 A C ATOM 4387 C THR E 181 12.624 -8.377 -8.517 1.00 74.23 A C ANISOU 4387 C THR E 181 9359 8521 10324 1568 2151 1591 A C ATOM 4388 O THR E 181 12.070 -7.440 -7.929 1.00 77.34 A O ANISOU 4388 O THR E 181 9796 9054 10536 1525 1880 1444 A O ATOM 4389 CB THR E 181 11.833 -9.613 -10.565 1.00 75.57 A C ANISOU 4389 CB THR E 181 9465 8585 10665 1750 2660 1979 A C ATOM 4390 CG2 THR E 181 10.402 -9.518 -10.095 1.00 53.63 A C ANISOU 4390 CG2 THR E 181 6605 5762 8008 1717 2354 2080 A C ATOM 4391 OG1 THR E 181 11.855 -9.612 -11.999 1.00 64.71 A O ANISOU 4391 OG1 THR E 181 8243 7275 9069 1843 3002 2034 A O ATOM 4392 N GLY E 182 13.249 -9.355 -7.857 1.00 69.12 A N ANISOU 4392 N GLY E 182 8583 7661 10020 1540 2157 1688 A N ATOM 4393 CA GLY E 182 13.297 -9.331 -6.400 1.00 66.13 A C ANISOU 4393 CA GLY E 182 8153 7182 9792 1422 1818 1622 A C ATOM 4394 C GLY E 182 14.128 -8.182 -5.854 1.00 73.11 A C ANISOU 4394 C GLY E 182 9243 8243 10292 1302 1704 1318 A C ATOM 4395 O GLY E 182 13.760 -7.553 -4.851 1.00 74.98 A O ANISOU 4395 O GLY E 182 9502 8538 10448 1208 1418 1196 A O ATOM 4396 N LEU E 183 15.258 -7.890 -6.508 1.00 73.19 A N ANISOU 4396 N LEU E 183 9430 8341 10039 1291 1929 1196 A N ATOM 4397 CA LEU E 183 16.125 -6.807 -6.058 1.00 68.03 A C ANISOU 4397 CA LEU E 183 8984 7866 8998 1119 1828 926 A C ATOM 4398 C LEU E 183 15.384 -5.477 -6.036 1.00 73.45 A C ANISOU 4398 C LEU E 183 9676 8880 9351 1069 1678 767 A C ATOM 4399 O LEU E 183 15.516 -4.702 -5.084 1.00 70.94 A O ANISOU 4399 O LEU E 183 9386 8701 8866 921 1470 596 A O ATOM 4400 CB LEU E 183 17.360 -6.723 -6.955 1.00 68.39 A C ANISOU 4400 CB LEU E 183 9272 7930 8782 1112 2093 847 A C ATOM 4401 CG LEU E 183 18.433 -5.710 -6.559 1.00 64.56 A C ANISOU 4401 CG LEU E 183 9045 7598 7886 876 1995 594 A C ATOM 4402 CD1 LEU E 183 19.401 -6.327 -5.565 1.00 69.95 A C ANISOU 4402 CD1 LEU E 183 9828 8018 8731 786 1895 577 A C ATOM 4403 CD2 LEU E 183 19.171 -5.205 -7.789 1.00 68.61 A C ANISOU 4403 CD2 LEU E 183 9831 8232 8006 860 2220 509 A C ATOM 4404 N GLY E 184 14.587 -5.202 -7.071 1.00 67.94 A N ANISOU 4404 N GLY E 184 8950 8315 8547 1203 1782 824 A N ATOM 4405 CA GLY E 184 13.796 -3.986 -7.092 1.00 71.93 A C ANISOU 4405 CA GLY E 184 9435 9129 8767 1218 1622 688 A C ATOM 4406 C GLY E 184 12.586 -4.040 -6.189 1.00 66.87 A C ANISOU 4406 C GLY E 184 8658 8425 8326 1295 1366 739 A C ATOM 4407 O GLY E 184 12.191 -3.014 -5.628 1.00 64.66 A O ANISOU 4407 O GLY E 184 8358 8386 7825 1288 1182 572 A O ATOM 4408 N ALA E 185 11.980 -5.222 -6.035 1.00 70.88 A N ANISOU 4408 N ALA E 185 9075 8616 9240 1369 1349 975 A N ATOM 4409 CA ALA E 185 10.892 -5.371 -5.077 1.00 69.82 A C ANISOU 4409 CA ALA E 185 8879 8351 9298 1408 1066 1036 A C ATOM 4410 C ALA E 185 11.333 -4.946 -3.685 1.00 72.87 A C ANISOU 4410 C ALA E 185 9300 8761 9626 1272 857 863 A C ATOM 4411 O ALA E 185 10.557 -4.345 -2.933 1.00 77.43 A O ANISOU 4411 O ALA E 185 9902 9409 10108 1318 634 772 A O ATOM 4412 CB ALA E 185 10.394 -6.817 -5.064 1.00 63.87 A C ANISOU 4412 CB ALA E 185 8017 7238 9012 1428 1065 1338 A C ATOM 4413 N THR E 186 12.583 -5.241 -3.326 1.00 62.47 A N ANISOU 4413 N THR E 186 8022 7374 8339 1115 929 813 A N ATOM 4414 CA THR E 186 13.074 -4.781 -2.029 1.00 70.58 A C ANISOU 4414 CA THR E 186 9130 8427 9260 949 741 642 A C ATOM 4415 C THR E 186 13.552 -3.331 -2.082 1.00 71.02 A C ANISOU 4415 C THR E 186 9246 8903 8835 853 781 373 A C ATOM 4416 O THR E 186 13.123 -2.500 -1.275 1.00 62.98 A O ANISOU 4416 O THR E 186 8226 8069 7633 834 625 226 A O ATOM 4417 CB THR E 186 14.197 -5.687 -1.524 1.00 69.81 A C ANISOU 4417 CB THR E 186 9090 8052 9381 811 751 701 A C ATOM 4418 CG2 THR E 186 14.718 -5.175 -0.190 1.00 56.40 A C ANISOU 4418 CG2 THR E 186 7532 6367 7528 609 552 523 A C ATOM 4419 OG1 THR E 186 13.698 -7.019 -1.355 1.00 81.38 A O ANISOU 4419 OG1 THR E 186 10435 9163 11324 889 675 963 A O ATOM 4420 N LEU E 187 14.431 -3.009 -3.033 1.00 73.74 A N ANISOU 4420 N LEU E 187 9647 9411 8959 789 991 313 A N ATOM 4421 CA LEU E 187 15.102 -1.711 -3.031 1.00 65.74 A C ANISOU 4421 CA LEU E 187 8689 8788 7500 612 1008 78 A C ATOM 4422 C LEU E 187 14.160 -0.586 -3.442 1.00 69.29 A C ANISOU 4422 C LEU E 187 9004 9623 7700 751 964 -18 A C ATOM 4423 O LEU E 187 14.126 0.472 -2.802 1.00 67.06 A O ANISOU 4423 O LEU E 187 8657 9666 7157 666 867 -198 A O ATOM 4424 CB LEU E 187 16.318 -1.760 -3.958 1.00 71.29 A C ANISOU 4424 CB LEU E 187 9553 9501 8033 488 1211 59 A C ATOM 4425 CG LEU E 187 17.691 -1.725 -3.288 1.00 62.37 A C ANISOU 4425 CG LEU E 187 8629 8301 6769 201 1192 -50 A C ATOM 4426 CD1 LEU E 187 17.771 -2.790 -2.223 1.00 63.56 A C ANISOU 4426 CD1 LEU E 187 8806 8059 7286 204 1071 50 A C ATOM 4427 CD2 LEU E 187 18.781 -1.937 -4.318 1.00 80.92 A C ANISOU 4427 CD2 LEU E 187 11203 10576 8968 141 1391 -40 A C ATOM 4428 N ASN E 188 13.394 -0.787 -4.515 1.00 73.29 A N ANISOU 4428 N ASN E 188 9466 10108 8271 973 1038 103 A N ATOM 4429 CA ASN E 188 12.571 0.283 -5.067 1.00 65.40 A C ANISOU 4429 CA ASN E 188 8369 9464 7016 1132 983 16 A C ATOM 4430 C ASN E 188 11.211 0.404 -4.398 1.00 69.81 A C ANISOU 4430 C ASN E 188 8844 9996 7683 1363 787 29 A C ATOM 4431 O ASN E 188 10.695 1.520 -4.259 1.00 67.37 A O ANISOU 4431 O ASN E 188 8434 10042 7123 1476 688 -122 A O ATOM 4432 CB ASN E 188 12.367 0.070 -6.571 1.00 64.09 A C ANISOU 4432 CB ASN E 188 8265 9270 6817 1261 1134 135 A C ATOM 4433 CG ASN E 188 13.674 0.044 -7.340 1.00 64.75 A C ANISOU 4433 CG ASN E 188 8499 9377 6725 1065 1330 109 A C ATOM 4434 ND2 ASN E 188 13.790 -0.891 -8.276 1.00 69.18 A N ANISOU 4434 ND2 ASN E 188 9181 9670 7436 1145 1526 280 A N ATOM 4435 OD1 ASN E 188 14.566 0.856 -7.099 1.00 70.01 A O ANISOU 4435 OD1 ASN E 188 9193 10298 7108 838 1308 -59 A O ATOM 4436 N VAL E 189 10.624 -0.712 -3.973 1.00 63.76 A N ANISOU 4436 N VAL E 189 8126 8822 7279 1439 716 208 A N ATOM 4437 CA VAL E 189 9.241 -0.751 -3.496 1.00 68.03 A C ANISOU 4437 CA VAL E 189 8677 9247 7926 1666 512 259 A C ATOM 4438 C VAL E 189 9.181 -0.871 -1.973 1.00 62.87 A C ANISOU 4438 C VAL E 189 8068 8455 7364 1590 333 198 A C ATOM 4439 O VAL E 189 8.643 0.004 -1.295 1.00 72.02 A O ANISOU 4439 O VAL E 189 9222 9820 8320 1706 207 39 A O ATOM 4440 CB VAL E 189 8.449 -1.889 -4.179 1.00 65.37 A C ANISOU 4440 CB VAL E 189 8395 8543 7901 1781 523 533 A C ATOM 4441 CG1 VAL E 189 6.948 -1.672 -4.029 1.00 61.03 A C ANISOU 4441 CG1 VAL E 189 7922 7923 7342 2033 304 570 A C ATOM 4442 CG2 VAL E 189 8.839 -1.999 -5.647 1.00 61.60 A C ANISOU 4442 CG2 VAL E 189 7918 8139 7347 1785 764 609 A C ATOM 4443 N ALA E 190 9.721 -1.959 -1.418 1.00 69.22 A N ANISOU 4443 N ALA E 190 8927 8906 8469 1414 317 326 A N ATOM 4444 CA ALA E 190 9.695 -2.131 0.035 1.00 59.03 A C ANISOU 4444 CA ALA E 190 7732 7438 7260 1319 121 280 A C ATOM 4445 C ALA E 190 10.452 -1.011 0.733 1.00 67.26 A C ANISOU 4445 C ALA E 190 8773 8834 7949 1175 151 15 A C ATOM 4446 O ALA E 190 9.981 -0.470 1.740 1.00 63.77 A O ANISOU 4446 O ALA E 190 8396 8461 7372 1223 14 -109 A O ATOM 4447 CB ALA E 190 10.278 -3.493 0.422 1.00 50.87 A C ANISOU 4447 CB ALA E 190 6738 5980 6612 1146 85 470 A C ATOM 4448 N LYS E 191 11.614 -0.643 0.199 1.00 68.37 A N ANISOU 4448 N LYS E 191 8863 9201 7915 988 335 -70 A N ATOM 4449 CA LYS E 191 12.447 0.423 0.746 1.00 61.36 A C ANISOU 4449 CA LYS E 191 7964 8677 6671 776 380 -300 A C ATOM 4450 C LYS E 191 12.675 0.273 2.251 1.00 67.95 A C ANISOU 4450 C LYS E 191 8947 9343 7528 614 238 -364 A C ATOM 4451 O LYS E 191 12.272 1.145 3.036 1.00 68.89 A O ANISOU 4451 O LYS E 191 9053 9709 7413 649 183 -523 A O ATOM 4452 CB LYS E 191 11.847 1.784 0.424 1.00 54.28 A C ANISOU 4452 CB LYS E 191 6896 8289 5438 940 405 -464 A C ATOM 4453 CG LYS E 191 11.802 2.100 -1.063 1.00 63.85 A C ANISOU 4453 CG LYS E 191 7997 9709 6555 1046 526 -427 A C ATOM 4454 CD LYS E 191 11.346 3.526 -1.316 1.00 64.60 A C ANISOU 4454 CD LYS E 191 7890 10348 6306 1187 518 -600 A C ATOM 4455 CE LYS E 191 9.869 3.694 -1.003 1.00 73.74 A C ANISOU 4455 CE LYS E 191 9025 11478 7517 1575 370 -598 A C ATOM 4456 NZ LYS E 191 9.454 5.123 -1.055 1.00 62.62 A N1+ ANISOU 4456 NZ LYS E 191 7388 10627 5776 1755 356 -787 A N1+ ATOM 4457 N PRO E 192 13.307 -0.813 2.694 1.00 70.87 A N ANISOU 4457 N PRO E 192 9468 9296 8165 451 176 -243 A N ATOM 4458 CA PRO E 192 13.554 -0.978 4.128 1.00 69.69 A C ANISOU 4458 CA PRO E 192 9510 8949 8021 279 10 -297 A C ATOM 4459 C PRO E 192 14.692 -0.085 4.592 1.00 67.80 A C ANISOU 4459 C PRO E 192 9344 9009 7407 -35 99 -501 A C ATOM 4460 O PRO E 192 15.736 0.018 3.943 1.00 76.31 A O ANISOU 4460 O PRO E 192 10428 10192 8374 -218 235 -523 A O ATOM 4461 CB PRO E 192 13.923 -2.461 4.255 1.00 63.07 A C ANISOU 4461 CB PRO E 192 8775 7582 7607 222 -96 -80 A C ATOM 4462 CG PRO E 192 14.537 -2.796 2.947 1.00 62.70 A C ANISOU 4462 CG PRO E 192 8616 7572 7633 244 113 5 A C ATOM 4463 CD PRO E 192 13.850 -1.939 1.911 1.00 54.28 A C ANISOU 4463 CD PRO E 192 7374 6889 6363 434 256 -52 A C ATOM 4464 N LYS E 193 14.475 0.576 5.724 1.00 74.14 A N ANISOU 4464 N LYS E 193 9815 10469 7886 732 343 1842 A N ATOM 4465 CA LYS E 193 15.519 1.399 6.303 1.00 73.44 A C ANISOU 4465 CA LYS E 193 9760 10408 7734 608 420 1954 A C ATOM 4466 C LYS E 193 16.562 0.519 6.986 1.00 79.82 A C ANISOU 4466 C LYS E 193 10740 11085 8502 731 554 2057 A C ATOM 4467 O LYS E 193 16.337 -0.665 7.251 1.00 86.27 A O ANISOU 4467 O LYS E 193 11549 11876 9354 960 550 2024 A O ATOM 4468 CB LYS E 193 14.924 2.405 7.289 1.00 63.85 A C ANISOU 4468 CB LYS E 193 8278 9481 6499 629 380 1951 A C ATOM 4469 CG LYS E 193 13.998 3.421 6.632 1.00 87.34 A C ANISOU 4469 CG LYS E 193 11062 12575 9550 543 222 1853 A C ATOM 4470 CD LYS E 193 13.289 4.288 7.658 1.00 86.33 A C ANISOU 4470 CD LYS E 193 10626 12735 9440 627 209 1802 A C ATOM 4471 CE LYS E 193 12.336 5.270 6.989 1.00 86.18 A C ANISOU 4471 CE LYS E 193 10392 12813 9538 609 17 1697 A C ATOM 4472 NZ LYS E 193 13.051 6.268 6.147 1.00 99.35 A N1+ ANISOU 4472 NZ LYS E 193 12053 14463 11235 338 -45 1718 A N1+ ATOM 4473 N LYS E 194 17.725 1.111 7.253 1.00 76.70 A N ANISOU 4473 N LYS E 194 10502 10595 8046 574 661 2182 A N ATOM 4474 CA LYS E 194 18.820 0.360 7.852 1.00 71.29 A C ANISOU 4474 CA LYS E 194 10049 9720 7317 701 770 2316 A C ATOM 4475 C LYS E 194 18.420 -0.169 9.224 1.00 71.86 A C ANISOU 4475 C LYS E 194 10009 9990 7303 979 725 2376 A C ATOM 4476 O LYS E 194 17.785 0.529 10.018 1.00 67.60 A O ANISOU 4476 O LYS E 194 9287 9720 6678 962 703 2374 A O ATOM 4477 CB LYS E 194 20.070 1.236 7.966 1.00 69.92 A C ANISOU 4477 CB LYS E 194 10096 9388 7081 437 907 2453 A C ATOM 4478 CG LYS E 194 21.363 0.449 8.133 1.00 81.75 A C ANISOU 4478 CG LYS E 194 11946 10544 8570 542 1017 2587 A C ATOM 4479 CD LYS E 194 22.486 1.308 8.701 1.00 83.51 A C ANISOU 4479 CD LYS E 194 12405 10630 8696 302 1169 2772 A C ATOM 4480 CE LYS E 194 23.812 0.557 8.697 1.00 93.07 A C ANISOU 4480 CE LYS E 194 14030 11410 9923 409 1268 2904 A C ATOM 4481 NZ LYS E 194 24.935 1.402 8.201 1.00 95.86 A N1+ ANISOU 4481 NZ LYS E 194 14668 11467 10288 20 1427 2948 A N1+ ATOM 4482 N GLY E 195 18.781 -1.422 9.491 1.00 77.59 A N ANISOU 4482 N GLY E 195 10834 10592 8054 1247 703 2407 A N ATOM 4483 CA GLY E 195 18.480 -2.058 10.755 1.00 73.79 A C ANISOU 4483 CA GLY E 195 10273 10294 7472 1529 607 2456 A C ATOM 4484 C GLY E 195 17.096 -2.658 10.870 1.00 76.95 A C ANISOU 4484 C GLY E 195 10368 10930 7938 1685 467 2260 A C ATOM 4485 O GLY E 195 16.798 -3.287 11.893 1.00 75.94 A O ANISOU 4485 O GLY E 195 10160 10967 7726 1918 354 2260 A O ATOM 4486 N GLN E 196 16.242 -2.490 9.864 1.00 72.39 A N ANISOU 4486 N GLN E 196 9649 10362 7494 1555 459 2096 A N ATOM 4487 CA GLN E 196 14.893 -3.029 9.922 1.00 72.27 A C ANISOU 4487 CA GLN E 196 9387 10517 7556 1663 348 1911 A C ATOM 4488 C GLN E 196 14.900 -4.527 9.623 1.00 82.70 A C ANISOU 4488 C GLN E 196 10657 11743 9023 1844 326 1810 A C ATOM 4489 O GLN E 196 15.916 -5.110 9.237 1.00 87.55 A O ANISOU 4489 O GLN E 196 11417 12149 9699 1905 400 1868 A O ATOM 4490 CB GLN E 196 13.979 -2.288 8.947 1.00 70.91 A C ANISOU 4490 CB GLN E 196 9135 10347 7459 1465 341 1804 A C ATOM 4491 CG GLN E 196 13.778 -0.818 9.285 1.00 71.49 A C ANISOU 4491 CG GLN E 196 9145 10572 7446 1326 336 1849 A C ATOM 4492 CD GLN E 196 12.562 -0.218 8.605 1.00 73.47 A C ANISOU 4492 CD GLN E 196 9255 10873 7785 1250 246 1722 A C ATOM 4493 NE2 GLN E 196 11.723 0.456 9.382 1.00 85.71 A N ANISOU 4493 NE2 GLN E 196 10613 12640 9312 1315 194 1654 A N ATOM 4494 OE1 GLN E 196 12.380 -0.359 7.395 1.00 73.98 A O ANISOU 4494 OE1 GLN E 196 9409 10773 7927 1146 226 1686 A O ATOM 4495 N SER E 197 13.741 -5.153 9.811 1.00 78.82 A N ANISOU 4495 N SER E 197 9939 11400 8610 1926 234 1634 A N ATOM 4496 CA SER E 197 13.573 -6.581 9.585 1.00 75.65 A C ANISOU 4496 CA SER E 197 9396 10965 8381 2067 219 1489 A C ATOM 4497 C SER E 197 12.733 -6.815 8.337 1.00 70.51 A C ANISOU 4497 C SER E 197 8701 10207 7882 1881 320 1332 A C ATOM 4498 O SER E 197 11.756 -6.100 8.090 1.00 69.24 A O ANISOU 4498 O SER E 197 8528 10088 7691 1735 292 1290 A O ATOM 4499 CB SER E 197 12.920 -7.257 10.794 1.00 69.30 A C ANISOU 4499 CB SER E 197 8366 10411 7553 2270 36 1384 A C ATOM 4500 OG SER E 197 11.579 -6.830 10.953 1.00 68.21 A O ANISOU 4500 OG SER E 197 8100 10412 7404 2165 -16 1245 A O ATOM 4501 N VAL E 198 13.120 -7.819 7.552 1.00 70.75 A N ANISOU 4501 N VAL E 198 8725 10088 8068 1896 447 1247 A N ATOM 4502 CA VAL E 198 12.480 -8.118 6.277 1.00 69.95 A C ANISOU 4502 CA VAL E 198 8652 9856 8069 1688 601 1117 A C ATOM 4503 C VAL E 198 12.157 -9.604 6.233 1.00 69.96 A C ANISOU 4503 C VAL E 198 8397 9896 8287 1778 669 910 A C ATOM 4504 O VAL E 198 13.049 -10.443 6.405 1.00 72.68 A O ANISOU 4504 O VAL E 198 8655 10217 8745 1974 707 883 A O ATOM 4505 CB VAL E 198 13.364 -7.728 5.080 1.00 63.18 A C ANISOU 4505 CB VAL E 198 8088 8756 7161 1530 775 1191 A C ATOM 4506 CG1 VAL E 198 12.666 -8.074 3.774 1.00 54.03 A C ANISOU 4506 CG1 VAL E 198 7012 7473 6043 1305 943 1065 A C ATOM 4507 CG2 VAL E 198 13.710 -6.248 5.129 1.00 64.69 A C ANISOU 4507 CG2 VAL E 198 8476 8933 7168 1410 692 1368 A C ATOM 4508 N ALA E 199 10.888 -9.925 6.006 1.00 71.86 A N ANISOU 4508 N ALA E 199 8510 10187 8607 1638 687 756 A N ATOM 4509 CA ALA E 199 10.451 -11.289 5.748 1.00 65.88 A C ANISOU 4509 CA ALA E 199 7497 9455 8081 1620 810 526 A C ATOM 4510 C ALA E 199 10.329 -11.498 4.244 1.00 59.90 A C ANISOU 4510 C ALA E 199 6927 8481 7353 1356 1111 472 A C ATOM 4511 O ALA E 199 9.886 -10.604 3.518 1.00 78.11 A O ANISOU 4511 O ALA E 199 9524 10658 9496 1146 1140 574 A O ATOM 4512 CB ALA E 199 9.115 -11.581 6.432 1.00 64.95 A C ANISOU 4512 CB ALA E 199 7148 9497 8034 1576 675 370 A C ATOM 4513 N ILE E 200 10.737 -12.674 3.775 1.00 69.46 A N ANISOU 4513 N ILE E 200 7972 9659 8758 1378 1331 304 A N ATOM 4514 CA ILE E 200 10.756 -12.978 2.349 1.00 71.02 A C ANISOU 4514 CA ILE E 200 8368 9662 8955 1127 1677 231 A C ATOM 4515 C ILE E 200 10.128 -14.346 2.138 1.00 69.71 A C ANISOU 4515 C ILE E 200 7866 9566 9055 1030 1896 -44 A C ATOM 4516 O ILE E 200 10.588 -15.341 2.713 1.00 77.49 A O ANISOU 4516 O ILE E 200 8461 10694 10287 1258 1883 -203 A O ATOM 4517 CB ILE E 200 12.179 -12.937 1.773 1.00 68.89 A C ANISOU 4517 CB ILE E 200 8292 9239 8645 1226 1829 283 A C ATOM 4518 CG1 ILE E 200 12.720 -11.511 1.843 1.00 72.63 A C ANISOU 4518 CG1 ILE E 200 9114 9627 8856 1223 1644 538 A C ATOM 4519 CG2 ILE E 200 12.191 -13.450 0.340 1.00 62.54 A C ANISOU 4519 CG2 ILE E 200 7664 8263 7834 973 2228 146 A C ATOM 4520 CD1 ILE E 200 14.114 -11.375 1.350 1.00 71.95 A C ANISOU 4520 CD1 ILE E 200 9258 9358 8723 1291 1771 586 A C ATOM 4521 N PHE E 201 9.085 -14.396 1.315 1.00 64.91 A N ANISOU 4521 N PHE E 201 7409 8854 8401 688 2092 -100 A N ATOM 4522 CA PHE E 201 8.375 -15.632 1.017 1.00 66.28 A C ANISOU 4522 CA PHE E 201 7294 9071 8818 496 2361 -365 A C ATOM 4523 C PHE E 201 8.870 -16.168 -0.320 1.00 74.16 A C ANISOU 4523 C PHE E 201 8457 9915 9806 307 2817 -461 A C ATOM 4524 O PHE E 201 8.742 -15.496 -1.348 1.00 72.62 A O ANISOU 4524 O PHE E 201 8748 9515 9329 68 2960 -323 A O ATOM 4525 CB PHE E 201 6.865 -15.397 0.988 1.00 70.72 A C ANISOU 4525 CB PHE E 201 7962 9575 9334 208 2325 -366 A C ATOM 4526 CG PHE E 201 6.266 -15.146 2.344 1.00 73.69 A C ANISOU 4526 CG PHE E 201 8100 10125 9774 377 1941 -376 A C ATOM 4527 CD1 PHE E 201 6.507 -13.958 3.015 1.00 72.43 A C ANISOU 4527 CD1 PHE E 201 8112 9997 9411 587 1608 -157 A C ATOM 4528 CD2 PHE E 201 5.468 -16.101 2.951 1.00 72.39 A C ANISOU 4528 CD2 PHE E 201 7534 10103 9869 302 1929 -630 A C ATOM 4529 CE1 PHE E 201 5.963 -13.725 4.263 1.00 71.25 A C ANISOU 4529 CE1 PHE E 201 7770 10016 9286 736 1293 -188 A C ATOM 4530 CE2 PHE E 201 4.919 -15.874 4.200 1.00 78.09 A C ANISOU 4530 CE2 PHE E 201 8070 10986 10613 447 1574 -669 A C ATOM 4531 CZ PHE E 201 5.168 -14.684 4.857 1.00 73.45 A C ANISOU 4531 CZ PHE E 201 7689 10427 9791 672 1267 -446 A C ATOM 4532 N GLY E 202 9.439 -17.371 -0.300 1.00 80.58 A N ANISOU 4532 N GLY E 202 8864 10836 10917 428 3035 -711 A N ATOM 4533 CA GLY E 202 10.028 -17.950 -1.491 1.00 82.05 A C ANISOU 4533 CA GLY E 202 9161 10896 11116 294 3507 -851 A C ATOM 4534 C GLY E 202 11.519 -17.705 -1.571 1.00 86.28 A C ANISOU 4534 C GLY E 202 9816 11353 11612 608 3486 -789 A C ATOM 4535 O GLY E 202 11.969 -16.558 -1.497 1.00 81.11 A O ANISOU 4535 O GLY E 202 9543 10588 10688 681 3244 -532 A O ATOM 4536 N LEU E 203 12.297 -18.772 -1.720 1.00 94.21 A N ANISOU 4536 N LEU E 203 10486 12403 12907 793 3743 -1038 A N ATOM 4537 CA LEU E 203 13.751 -18.686 -1.752 1.00 92.00 A C ANISOU 4537 CA LEU E 203 10301 12004 12650 1130 3741 -1013 A C ATOM 4538 C LEU E 203 14.300 -19.160 -3.092 1.00 93.19 A C ANISOU 4538 C LEU E 203 10646 11982 12777 972 4285 -1215 A C ATOM 4539 O LEU E 203 15.336 -19.826 -3.163 1.00 96.34 A O ANISOU 4539 O LEU E 203 10854 12337 13413 1266 4453 -1393 A O ATOM 4540 CB LEU E 203 14.366 -19.468 -0.594 1.00 91.03 A C ANISOU 4540 CB LEU E 203 9628 12059 12901 1616 3489 -1115 A C ATOM 4541 CG LEU E 203 14.164 -18.806 0.771 1.00 86.69 A C ANISOU 4541 CG LEU E 203 9025 11644 12270 1829 2926 -871 A C ATOM 4542 CD1 LEU E 203 14.902 -19.564 1.863 1.00 93.24 A C ANISOU 4542 CD1 LEU E 203 9399 12623 13403 2338 2649 -940 A C ATOM 4543 CD2 LEU E 203 14.602 -17.347 0.733 1.00 80.62 A C ANISOU 4543 CD2 LEU E 203 8834 10683 11116 1791 2737 -535 A C ATOM 4544 N GLY E 204 13.601 -18.823 -4.170 1.00 97.46 A N ANISOU 4544 N GLY E 204 11597 12415 13020 515 4568 -1191 A N ATOM 4545 CA GLY E 204 14.112 -18.988 -5.513 1.00 73.61 A C ANISOU 4545 CA GLY E 204 8936 9208 9826 309 5061 -1332 A C ATOM 4546 C GLY E 204 14.945 -17.791 -5.920 1.00 78.26 A C ANISOU 4546 C GLY E 204 10123 9568 10043 327 4900 -1110 A C ATOM 4547 O GLY E 204 15.358 -16.978 -5.090 1.00 76.47 A O ANISOU 4547 O GLY E 204 9946 9331 9780 563 4450 -880 A O ATOM 4548 N ALA E 205 15.183 -17.677 -7.229 1.00 80.19 A N ANISOU 4548 N ALA E 205 10841 9638 9991 40 5286 -1194 A N ATOM 4549 CA ALA E 205 15.994 -16.572 -7.734 1.00 77.99 A C ANISOU 4549 CA ALA E 205 11139 9143 9349 6 5150 -1034 A C ATOM 4550 C ALA E 205 15.371 -15.222 -7.395 1.00 84.00 A C ANISOU 4550 C ALA E 205 12185 9917 9813 -121 4650 -677 A C ATOM 4551 O ALA E 205 16.084 -14.264 -7.078 1.00 85.95 A O ANISOU 4551 O ALA E 205 12634 10078 9944 8 4329 -503 A O ATOM 4552 CB ALA E 205 16.194 -16.711 -9.243 1.00 75.43 A C ANISOU 4552 CB ALA E 205 11302 8658 8699 -331 5645 -1207 A C ATOM 4553 N VAL E 206 14.040 -15.132 -7.436 1.00 87.30 A N ANISOU 4553 N VAL E 206 12607 10432 10130 -369 4589 -576 A N ATOM 4554 CA VAL E 206 13.367 -13.874 -7.121 1.00 75.78 A C ANISOU 4554 CA VAL E 206 11381 8985 8428 -453 4122 -262 A C ATOM 4555 C VAL E 206 13.473 -13.571 -5.630 1.00 75.44 A C ANISOU 4555 C VAL E 206 10928 9087 8648 -105 3687 -137 A C ATOM 4556 O VAL E 206 13.802 -12.447 -5.226 1.00 80.17 A O ANISOU 4556 O VAL E 206 11686 9667 9107 -20 3322 74 A O ATOM 4557 CB VAL E 206 11.900 -13.920 -7.584 1.00 72.72 A C ANISOU 4557 CB VAL E 206 11143 8606 7881 -787 4193 -195 A C ATOM 4558 CG1 VAL E 206 11.167 -12.660 -7.154 1.00 66.95 A C ANISOU 4558 CG1 VAL E 206 10583 7886 6970 -796 3688 106 A C ATOM 4559 CG2 VAL E 206 11.823 -14.104 -9.093 1.00 67.49 A C ANISOU 4559 CG2 VAL E 206 10996 7787 6860 -1158 4612 -274 A C ATOM 4560 N GLY E 207 13.188 -14.567 -4.789 1.00 78.03 A N ANISOU 4560 N GLY E 207 10720 9579 9350 83 3724 -279 A N ATOM 4561 CA GLY E 207 13.315 -14.365 -3.356 1.00 73.39 A C ANISOU 4561 CA GLY E 207 9773 9144 8968 418 3319 -174 A C ATOM 4562 C GLY E 207 14.746 -14.100 -2.931 1.00 77.45 A C ANISOU 4562 C GLY E 207 10314 9579 9534 730 3200 -123 A C ATOM 4563 O GLY E 207 14.998 -13.300 -2.027 1.00 73.19 A O ANISOU 4563 O GLY E 207 9774 9084 8952 900 2835 81 A O ATOM 4564 N LEU E 208 15.706 -14.754 -3.588 1.00 82.62 A N ANISOU 4564 N LEU E 208 11021 10095 10276 798 3534 -311 A N ATOM 4565 CA LEU E 208 17.106 -14.499 -3.269 1.00 78.06 A C ANISOU 4565 CA LEU E 208 10547 9365 9749 1084 3446 -262 A C ATOM 4566 C LEU E 208 17.550 -13.125 -3.753 1.00 77.83 A C ANISOU 4566 C LEU E 208 11053 9161 9357 884 3306 -63 A C ATOM 4567 O LEU E 208 18.397 -12.492 -3.117 1.00 72.45 A O ANISOU 4567 O LEU E 208 10460 8396 8672 1061 3074 91 A O ATOM 4568 CB LEU E 208 17.991 -15.594 -3.861 1.00 80.00 A C ANISOU 4568 CB LEU E 208 10700 9480 10216 1236 3856 -553 A C ATOM 4569 CG LEU E 208 17.841 -16.947 -3.163 1.00 68.12 A C ANISOU 4569 CG LEU E 208 8561 8166 9156 1544 3916 -759 A C ATOM 4570 CD1 LEU E 208 18.593 -18.033 -3.910 1.00 72.98 A C ANISOU 4570 CD1 LEU E 208 9054 8666 10009 1669 4384 -1095 A C ATOM 4571 CD2 LEU E 208 18.295 -16.864 -1.714 1.00 69.71 A C ANISOU 4571 CD2 LEU E 208 8501 8449 9537 1970 3469 -589 A C ATOM 4572 N GLY E 209 16.987 -12.639 -4.862 1.00 71.29 A N ANISOU 4572 N GLY E 209 10593 8278 8217 504 3431 -60 A N ATOM 4573 CA GLY E 209 17.238 -11.261 -5.253 1.00 75.18 A C ANISOU 4573 CA GLY E 209 11527 8667 8373 304 3210 127 A C ATOM 4574 C GLY E 209 16.670 -10.273 -4.254 1.00 74.31 A C ANISOU 4574 C GLY E 209 11288 8714 8232 353 2763 386 A C ATOM 4575 O GLY E 209 17.295 -9.256 -3.944 1.00 80.70 A O ANISOU 4575 O GLY E 209 12251 9473 8940 362 2529 538 A O ATOM 4576 N ALA E 210 15.479 -10.567 -3.726 1.00 76.86 A N ANISOU 4576 N ALA E 210 11322 9229 8654 370 2664 415 A N ATOM 4577 CA ALA E 210 14.913 -9.736 -2.668 1.00 77.53 A C ANISOU 4577 CA ALA E 210 11243 9475 8742 460 2274 616 A C ATOM 4578 C ALA E 210 15.785 -9.766 -1.417 1.00 63.83 A C ANISOU 4578 C ALA E 210 9270 7790 7191 787 2114 683 A C ATOM 4579 O ALA E 210 15.937 -8.749 -0.728 1.00 70.99 A O ANISOU 4579 O ALA E 210 10206 8753 8013 823 1843 866 A O ATOM 4580 CB ALA E 210 13.491 -10.195 -2.345 1.00 70.46 A C ANISOU 4580 CB ALA E 210 10096 8735 7939 421 2238 584 A C ATOM 4581 N ALA E 211 16.369 -10.927 -1.110 1.00 74.59 A N ANISOU 4581 N ALA E 211 10400 9134 8806 1031 2281 536 A N ATOM 4582 CA ALA E 211 17.264 -11.031 0.039 1.00 70.57 A C ANISOU 4582 CA ALA E 211 9731 8635 8447 1372 2114 624 A C ATOM 4583 C ALA E 211 18.541 -10.232 -0.180 1.00 65.60 A C ANISOU 4583 C ALA E 211 9469 7766 7690 1352 2112 738 A C ATOM 4584 O ALA E 211 19.024 -9.557 0.736 1.00 65.96 A O ANISOU 4584 O ALA E 211 9544 7820 7697 1465 1890 932 A O ATOM 4585 CB ALA E 211 17.589 -12.497 0.322 1.00 81.50 A C ANISOU 4585 CB ALA E 211 10772 10045 10150 1672 2265 426 A C ATOM 4586 N GLU E 212 19.109 -10.310 -1.384 1.00 64.47 A N ANISOU 4586 N GLU E 212 9626 7399 7469 1185 2379 606 A N ATOM 4587 CA GLU E 212 20.267 -9.488 -1.716 1.00 78.67 A C ANISOU 4587 CA GLU E 212 11813 8946 9132 1092 2383 679 A C ATOM 4588 C GLU E 212 19.931 -8.007 -1.606 1.00 77.69 A C ANISOU 4588 C GLU E 212 11849 8908 8763 832 2115 881 A C ATOM 4589 O GLU E 212 20.752 -7.206 -1.143 1.00 71.86 A O ANISOU 4589 O GLU E 212 11258 8067 7980 823 1991 1023 A O ATOM 4590 CB GLU E 212 20.760 -9.831 -3.121 1.00 77.41 A C ANISOU 4590 CB GLU E 212 11966 8557 8889 913 2722 456 A C ATOM 4591 CG GLU E 212 21.937 -8.998 -3.596 1.00 82.01 A C ANISOU 4591 CG GLU E 212 12986 8855 9319 761 2740 479 A C ATOM 4592 CD GLU E 212 23.251 -9.430 -2.976 1.00 91.91 A C ANISOU 4592 CD GLU E 212 14268 9850 10802 1083 2801 481 A C ATOM 4593 OE1 GLU E 212 23.271 -10.453 -2.257 1.00 93.99 A O ANISOU 4593 OE1 GLU E 212 14202 10169 11342 1459 2826 451 A O ATOM 4594 OE2 GLU E 212 24.268 -8.746 -3.212 1.00 97.77 A O1- ANISOU 4594 OE2 GLU E 212 15373 10321 11452 961 2810 511 A O1- ATOM 4595 N GLY E 213 18.720 -7.628 -2.017 1.00 76.59 A N ANISOU 4595 N GLY E 213 11673 8946 8480 622 2026 892 A N ATOM 4596 CA GLY E 213 18.293 -6.249 -1.851 1.00 70.07 A C ANISOU 4596 CA GLY E 213 10912 8237 7473 434 1744 1063 A C ATOM 4597 C GLY E 213 18.223 -5.837 -0.394 1.00 69.79 A C ANISOU 4597 C GLY E 213 10610 8372 7536 629 1518 1233 A C ATOM 4598 O GLY E 213 18.717 -4.775 -0.009 1.00 67.03 A O ANISOU 4598 O GLY E 213 10340 8020 7106 541 1376 1367 A O ATOM 4599 N ALA E 214 17.605 -6.677 0.440 1.00 64.62 A N ANISOU 4599 N ALA E 214 9632 7876 7043 872 1493 1213 A N ATOM 4600 CA ALA E 214 17.525 -6.375 1.866 1.00 64.44 A C ANISOU 4600 CA ALA E 214 9387 8030 7068 1066 1287 1358 A C ATOM 4601 C ALA E 214 18.908 -6.290 2.498 1.00 72.12 A C ANISOU 4601 C ALA E 214 10489 8844 8069 1210 1302 1473 A C ATOM 4602 O ALA E 214 19.126 -5.486 3.412 1.00 77.65 A O ANISOU 4602 O ALA E 214 11182 9627 8693 1221 1159 1643 A O ATOM 4603 CB ALA E 214 16.673 -7.424 2.581 1.00 66.96 A C ANISOU 4603 CB ALA E 214 9357 8538 7546 1293 1249 1274 A C ATOM 4604 N ARG E 215 19.852 -7.105 2.024 1.00 71.95 A N ANISOU 4604 N ARG E 215 10606 8576 8157 1321 1495 1379 A N ATOM 4605 CA ARG E 215 21.226 -7.021 2.509 1.00 72.12 A C ANISOU 4605 CA ARG E 215 10832 8359 8211 1457 1520 1497 A C ATOM 4606 C ARG E 215 21.869 -5.699 2.107 1.00 70.37 A C ANISOU 4606 C ARG E 215 10933 7987 7818 1128 1519 1593 A C ATOM 4607 O ARG E 215 22.517 -5.036 2.926 1.00 74.70 A O ANISOU 4607 O ARG E 215 11584 8485 8316 1125 1442 1780 A O ATOM 4608 CB ARG E 215 22.041 -8.201 1.975 1.00 73.67 A C ANISOU 4608 CB ARG E 215 11102 8295 8595 1670 1742 1334 A C ATOM 4609 CG ARG E 215 23.478 -8.254 2.474 1.00 83.98 A C ANISOU 4609 CG ARG E 215 12655 9285 9969 1873 1765 1455 A C ATOM 4610 CD ARG E 215 24.267 -9.338 1.753 1.00 83.02 A C ANISOU 4610 CD ARG E 215 12620 8871 10054 2079 2012 1246 A C ATOM 4611 NE ARG E 215 24.503 -9.014 0.351 1.00 84.39 A N ANISOU 4611 NE ARG E 215 13084 8853 10128 1750 2249 1061 A N ATOM 4612 CZ ARG E 215 25.483 -8.233 -0.082 1.00 92.11 A C ANISOU 4612 CZ ARG E 215 14480 9520 10996 1535 2320 1093 A C ATOM 4613 NH1 ARG E 215 26.349 -7.683 0.753 1.00 86.69 A N1+ ANISOU 4613 NH1 ARG E 215 13987 8649 10304 1594 2209 1318 A N1+ ATOM 4614 NH2 ARG E 215 25.599 -8.000 -1.387 1.00 93.53 A N ANISOU 4614 NH2 ARG E 215 14917 9567 11052 1229 2513 891 A N ATOM 4615 N ILE E 216 21.701 -5.304 0.843 1.00 78.33 A N ANISOU 4615 N ILE E 216 11364 9922 8476 972 11 1113 A N ATOM 4616 CA ILE E 216 22.270 -4.045 0.365 1.00 73.85 A C ANISOU 4616 CA ILE E 216 10829 9354 7878 810 -66 1239 A C ATOM 4617 C ILE E 216 21.677 -2.866 1.128 1.00 73.01 A C ANISOU 4617 C ILE E 216 10547 9217 7976 727 20 1337 A C ATOM 4618 O ILE E 216 22.373 -1.890 1.435 1.00 76.60 A O ANISOU 4618 O ILE E 216 11043 9633 8430 595 9 1386 A O ATOM 4619 CB ILE E 216 22.054 -3.911 -1.155 1.00 74.61 A C ANISOU 4619 CB ILE E 216 10853 9577 7917 774 -156 1350 A C ATOM 4620 CG1 ILE E 216 22.909 -4.934 -1.906 1.00 72.38 A C ANISOU 4620 CG1 ILE E 216 10771 9357 7374 865 -231 1217 A C ATOM 4621 CG2 ILE E 216 22.371 -2.503 -1.632 1.00 67.16 A C ANISOU 4621 CG2 ILE E 216 9855 8655 7007 615 -274 1459 A C ATOM 4622 CD1 ILE E 216 22.446 -5.194 -3.322 1.00 59.28 A C ANISOU 4622 CD1 ILE E 216 9038 7889 5598 904 -249 1322 A C ATOM 4623 N ALA E 217 20.389 -2.946 1.466 1.00 72.45 A N ANISOU 4623 N ALA E 217 10262 9153 8113 802 118 1354 A N ATOM 4624 CA ALA E 217 19.720 -1.866 2.181 1.00 76.46 A C ANISOU 4624 CA ALA E 217 10577 9649 8824 773 210 1407 A C ATOM 4625 C ALA E 217 20.118 -1.787 3.648 1.00 65.30 A C ANISOU 4625 C ALA E 217 9269 8210 7332 824 324 1288 A C ATOM 4626 O ALA E 217 19.708 -0.843 4.332 1.00 83.36 A O ANISOU 4626 O ALA E 217 11406 10526 9742 811 437 1315 A O ATOM 4627 CB ALA E 217 18.202 -2.023 2.067 1.00 65.73 A C ANISOU 4627 CB ALA E 217 8975 8258 7740 865 260 1435 A C ATOM 4628 N GLY E 218 20.898 -2.743 4.146 1.00 72.34 A N ANISOU 4628 N GLY E 218 10412 9070 8004 908 303 1162 A N ATOM 4629 CA GLY E 218 21.338 -2.707 5.525 1.00 74.86 A C ANISOU 4629 CA GLY E 218 10882 9387 8175 989 401 1087 A C ATOM 4630 C GLY E 218 20.366 -3.284 6.526 1.00 79.54 A C ANISOU 4630 C GLY E 218 11392 10018 8813 1196 460 890 A C ATOM 4631 O GLY E 218 20.432 -2.930 7.707 1.00 77.89 A O ANISOU 4631 O GLY E 218 11244 9866 8485 1282 573 841 A O ATOM 4632 N ALA E 219 19.462 -4.161 6.095 1.00 78.21 A N ANISOU 4632 N ALA E 219 11078 9822 8815 1276 393 769 A N ATOM 4633 CA ALA E 219 18.525 -4.774 7.025 1.00 68.47 A C ANISOU 4633 CA ALA E 219 9744 8590 7680 1461 405 520 A C ATOM 4634 C ALA E 219 19.269 -5.657 8.018 1.00 73.99 A C ANISOU 4634 C ALA E 219 10692 9342 8081 1643 342 331 A C ATOM 4635 O ALA E 219 20.216 -6.363 7.662 1.00 88.05 A O ANISOU 4635 O ALA E 219 12663 11109 9684 1654 247 347 A O ATOM 4636 CB ALA E 219 17.477 -5.590 6.268 1.00 63.57 A C ANISOU 4636 CB ALA E 219 8904 7882 7367 1461 347 455 A C ATOM 4637 N SER E 220 18.837 -5.606 9.279 1.00 73.76 A N ANISOU 4637 N SER E 220 10665 9383 7978 1820 382 138 A N ATOM 4638 CA SER E 220 19.489 -6.389 10.322 1.00 80.36 A C ANISOU 4638 CA SER E 220 11750 10302 8480 2043 298 -37 A C ATOM 4639 C SER E 220 18.986 -7.825 10.358 1.00 83.46 A C ANISOU 4639 C SER E 220 12040 10678 8991 2198 110 -349 A C ATOM 4640 O SER E 220 19.762 -8.741 10.651 1.00 83.29 A O ANISOU 4640 O SER E 220 12209 10697 8739 2349 -28 -449 A O ATOM 4641 CB SER E 220 19.273 -5.735 11.688 1.00 85.83 A C ANISOU 4641 CB SER E 220 12508 11137 8967 2204 418 -125 A C ATOM 4642 OG SER E 220 17.899 -5.466 11.914 1.00 94.86 A O ANISOU 4642 OG SER E 220 13363 12280 10400 2256 453 -333 A O ATOM 4643 N ARG E 221 17.706 -8.038 10.064 1.00 76.56 A N ANISOU 4643 N ARG E 221 10854 9726 8510 2163 97 -503 A N ATOM 4644 CA ARG E 221 17.083 -9.352 10.157 1.00 75.46 A C ANISOU 4644 CA ARG E 221 10542 9549 8581 2272 -65 -823 A C ATOM 4645 C ARG E 221 16.377 -9.653 8.844 1.00 79.87 A C ANISOU 4645 C ARG E 221 10829 9956 9562 2059 -25 -699 A C ATOM 4646 O ARG E 221 15.501 -8.894 8.420 1.00 74.56 A O ANISOU 4646 O ARG E 221 9982 9169 9177 1931 81 -567 A O ATOM 4647 CB ARG E 221 16.096 -9.402 11.327 1.00 78.35 A C ANISOU 4647 CB ARG E 221 10787 9939 9045 2461 -128 -1193 A C ATOM 4648 CG ARG E 221 16.019 -10.740 12.038 1.00 79.76 A C ANISOU 4648 CG ARG E 221 10930 10180 9195 2683 -368 -1606 A C ATOM 4649 CD ARG E 221 15.218 -10.617 13.323 1.00 74.42 A C ANISOU 4649 CD ARG E 221 10205 9572 8498 2913 -453 -2002 A C ATOM 4650 NE ARG E 221 14.807 -11.913 13.847 1.00 86.16 A N ANISOU 4650 NE ARG E 221 11537 11074 10124 3086 -728 -2469 A N ATOM 4651 CZ ARG E 221 13.863 -12.083 14.763 1.00 79.90 A C ANISOU 4651 CZ ARG E 221 10602 10285 9470 3262 -872 -2925 A C ATOM 4652 NH1 ARG E 221 13.214 -11.055 15.285 1.00 89.35 A N1+ ANISOU 4652 NH1 ARG E 221 11802 11479 10667 3316 -750 -2985 A N1+ ATOM 4653 NH2 ARG E 221 13.562 -13.315 15.164 1.00 87.04 A N ANISOU 4653 NH2 ARG E 221 11335 11202 10535 3398 -1160 -3368 A N ATOM 4654 N ILE E 222 16.761 -10.753 8.203 1.00 83.21 A N ANISOU 4654 N ILE E 222 11217 10388 10012 2043 -99 -725 A N ATOM 4655 CA ILE E 222 16.159 -11.190 6.948 1.00 74.35 A C ANISOU 4655 CA ILE E 222 9849 9165 9234 1856 -25 -581 A C ATOM 4656 C ILE E 222 15.662 -12.612 7.172 1.00 74.54 A C ANISOU 4656 C ILE E 222 9633 9168 9522 1928 -134 -905 A C ATOM 4657 O ILE E 222 16.455 -13.561 7.206 1.00 74.55 A O ANISOU 4657 O ILE E 222 9692 9290 9343 2043 -235 -1038 A O ATOM 4658 CB ILE E 222 17.139 -11.117 5.773 1.00 71.81 A C ANISOU 4658 CB ILE E 222 9677 8918 8690 1751 38 -285 A C ATOM 4659 CG1 ILE E 222 17.766 -9.723 5.689 1.00 70.05 A C ANISOU 4659 CG1 ILE E 222 9681 8717 8220 1679 97 -27 A C ATOM 4660 CG2 ILE E 222 16.430 -11.460 4.471 1.00 65.42 A C ANISOU 4660 CG2 ILE E 222 8630 8050 8178 1577 154 -90 A C ATOM 4661 CD1 ILE E 222 18.810 -9.585 4.604 1.00 66.65 A C ANISOU 4661 CD1 ILE E 222 9420 8347 7558 1589 108 197 A C ATOM 4662 N ILE E 223 14.351 -12.766 7.330 1.00 65.97 A N ANISOU 4662 N ILE E 223 8256 7909 8900 1863 -128 -1049 A N ATOM 4663 CA ILE E 223 13.730 -14.058 7.596 1.00 64.42 A C ANISOU 4663 CA ILE E 223 7763 7651 9065 1889 -242 -1392 A C ATOM 4664 C ILE E 223 13.251 -14.642 6.274 1.00 80.38 A C ANISOU 4664 C ILE E 223 9522 9570 11451 1651 -73 -1145 A C ATOM 4665 O ILE E 223 12.426 -14.033 5.581 1.00 78.63 A O ANISOU 4665 O ILE E 223 9200 9163 11512 1469 84 -858 A O ATOM 4666 CB ILE E 223 12.571 -13.930 8.596 1.00 79.49 A C ANISOU 4666 CB ILE E 223 9498 9390 11315 1953 -352 -1743 A C ATOM 4667 CG1 ILE E 223 13.104 -13.648 10.001 1.00 76.55 A C ANISOU 4667 CG1 ILE E 223 9375 9203 10506 2248 -527 -2051 A C ATOM 4668 CG2 ILE E 223 11.727 -15.195 8.596 1.00 77.89 A C ANISOU 4668 CG2 ILE E 223 8902 9039 11652 1882 -448 -2052 A C ATOM 4669 CD1 ILE E 223 12.744 -12.276 10.529 1.00 74.07 A C ANISOU 4669 CD1 ILE E 223 9201 8858 10085 2295 -439 -1982 A C ATOM 4670 N GLY E 224 13.765 -15.816 5.926 1.00 78.15 A N ANISOU 4670 N GLY E 224 9125 9420 11149 1673 -94 -1241 A N ATOM 4671 CA GLY E 224 13.362 -16.511 4.715 1.00 74.11 A C ANISOU 4671 CA GLY E 224 8341 8870 10947 1464 107 -1018 A C ATOM 4672 C GLY E 224 12.335 -17.571 5.022 1.00 80.67 A C ANISOU 4672 C GLY E 224 8735 9536 12379 1374 64 -1315 A C ATOM 4673 O GLY E 224 12.537 -18.427 5.890 1.00 91.41 A O ANISOU 4673 O GLY E 224 9973 10981 13778 1533 -157 -1762 A O ATOM 4674 N VAL E 225 11.213 -17.515 4.305 1.00 71.15 A N ANISOU 4674 N VAL E 225 7286 8078 11671 1119 262 -1063 A N ATOM 4675 CA VAL E 225 10.114 -18.457 4.464 1.00 83.03 A C ANISOU 4675 CA VAL E 225 8339 9341 13869 956 261 -1286 A C ATOM 4676 C VAL E 225 10.035 -19.312 3.208 1.00 90.12 A C ANISOU 4676 C VAL E 225 8973 10297 14972 740 558 -967 A C ATOM 4677 O VAL E 225 9.852 -18.788 2.102 1.00 96.36 A O ANISOU 4677 O VAL E 225 9857 11057 15698 594 825 -443 A O ATOM 4678 CB VAL E 225 8.782 -17.739 4.725 1.00 73.80 A C ANISOU 4678 CB VAL E 225 7085 7757 13198 829 262 -1252 A C ATOM 4679 CG1 VAL E 225 7.663 -18.753 4.904 1.00 82.18 A C ANISOU 4679 CG1 VAL E 225 7667 8508 15049 633 240 -1512 A C ATOM 4680 CG2 VAL E 225 8.896 -16.838 5.945 1.00 82.65 A C ANISOU 4680 CG2 VAL E 225 8469 8884 14050 1073 13 -1567 A C ATOM 4681 N ASP E 226 10.172 -20.625 3.377 1.00 78.27 A N ANISOU 4681 N ASP E 226 7130 8909 13699 738 513 -1283 A N ATOM 4682 CA ASP E 226 10.080 -21.550 2.259 1.00106.66 A C ANISOU 4682 CA ASP E 226 10409 12600 17518 538 831 -1020 A C ATOM 4683 C ASP E 226 9.660 -22.917 2.774 1.00101.58 A C ANISOU 4683 C ASP E 226 9232 11910 17453 463 732 -1475 A C ATOM 4684 O ASP E 226 9.817 -23.235 3.956 1.00 92.27 A O ANISOU 4684 O ASP E 226 8001 10750 16308 655 365 -2030 A O ATOM 4685 CB ASP E 226 11.406 -21.651 1.497 1.00 87.11 A C ANISOU 4685 CB ASP E 226 8172 10549 14376 703 951 -831 A C ATOM 4686 CG ASP E 226 11.218 -22.106 0.065 1.00 95.48 A C ANISOU 4686 CG ASP E 226 9043 11721 15514 497 1378 -367 A C ATOM 4687 OD1 ASP E 226 10.820 -23.272 -0.141 1.00103.70 A O ANISOU 4687 OD1 ASP E 226 9610 12781 17012 349 1534 -465 A O ATOM 4688 OD2 ASP E 226 11.465 -21.298 -0.853 1.00 94.74 A O1- ANISOU 4688 OD2 ASP E 226 9261 11718 15019 487 1561 92 A O1- ATOM 4689 N PHE E 227 9.117 -23.725 1.865 1.00 91.37 A N ANISOU 4689 N PHE E 227 7530 10571 16613 182 1067 -1226 A N ATOM 4690 CA PHE E 227 8.738 -25.096 2.183 1.00102.89 A C ANISOU 4690 CA PHE E 227 8398 12010 18686 60 1026 -1621 A C ATOM 4691 C PHE E 227 9.885 -26.071 1.950 1.00104.73 A C ANISOU 4691 C PHE E 227 8496 12727 18569 262 1046 -1804 A C ATOM 4692 O PHE E 227 10.061 -27.018 2.724 1.00110.11 A O ANISOU 4692 O PHE E 227 8842 13511 19484 380 774 -2355 A O ATOM 4693 CB PHE E 227 7.519 -25.507 1.354 1.00108.69 A C ANISOU 4693 CB PHE E 227 8707 12420 20170 -379 1415 -1242 A C ATOM 4694 CG PHE E 227 6.237 -24.870 1.808 1.00115.75 A C ANISOU 4694 CG PHE E 227 9587 12744 21649 -575 1314 -1234 A C ATOM 4695 CD1 PHE E 227 5.831 -24.966 3.129 1.00119.53 A C ANISOU 4695 CD1 PHE E 227 9943 12997 22476 -486 873 -1881 A C ATOM 4696 CD2 PHE E 227 5.441 -24.170 0.918 1.00114.88 A C ANISOU 4696 CD2 PHE E 227 9601 12327 21720 -813 1642 -594 A C ATOM 4697 CE1 PHE E 227 4.652 -24.381 3.552 1.00112.25 A C ANISOU 4697 CE1 PHE E 227 9009 11538 22102 -636 769 -1927 A C ATOM 4698 CE2 PHE E 227 4.261 -23.581 1.335 1.00109.97 A C ANISOU 4698 CE2 PHE E 227 8970 11143 21669 -962 1535 -600 A C ATOM 4699 CZ PHE E 227 3.866 -23.686 2.654 1.00101.15 A C ANISOU 4699 CZ PHE E 227 7720 9790 20923 -874 1102 -1285 A C ATOM 4700 N ASN E 228 10.671 -25.855 0.898 1.00110.33 A N ANISOU 4700 N ASN E 228 9458 13741 18722 333 1336 -1382 A N ATOM 4701 CA ASN E 228 11.844 -26.678 0.615 1.00109.42 A C ANISOU 4701 CA ASN E 228 9275 14085 18217 578 1358 -1555 A C ATOM 4702 C ASN E 228 12.987 -26.195 1.499 1.00105.34 A C ANISOU 4702 C ASN E 228 9232 13724 17070 992 933 -1882 A C ATOM 4703 O ASN E 228 13.669 -25.219 1.176 1.00 96.04 A O ANISOU 4703 O ASN E 228 8581 12622 15289 1124 949 -1610 A O ATOM 4704 CB ASN E 228 12.210 -26.603 -0.863 1.00105.21 A C ANISOU 4704 CB ASN E 228 8847 13810 17319 513 1827 -1008 A C ATOM 4705 CG ASN E 228 13.335 -27.549 -1.235 1.00103.56 A C ANISOU 4705 CG ASN E 228 8503 14067 16778 768 1892 -1214 A C ATOM 4706 ND2 ASN E 228 13.864 -27.392 -2.444 1.00101.96 A N ANISOU 4706 ND2 ASN E 228 8488 14149 16104 809 2238 -822 A N ATOM 4707 OD1 ASN E 228 13.724 -28.412 -0.448 1.00116.70 A O ANISOU 4707 OD1 ASN E 228 9895 15845 18599 955 1615 -1740 A O ATOM 4708 N SER E 229 13.198 -26.881 2.626 1.00114.53 A N ANISOU 4708 N SER E 229 10203 14930 18382 1196 543 -2464 A N ATOM 4709 CA SER E 229 14.239 -26.477 3.564 1.00 99.91 A C ANISOU 4709 CA SER E 229 8805 13205 15950 1599 136 -2752 A C ATOM 4710 C SER E 229 15.640 -26.658 2.997 1.00 98.27 A C ANISOU 4710 C SER E 229 8857 13343 15139 1883 190 -2670 A C ATOM 4711 O SER E 229 16.591 -26.085 3.540 1.00 98.38 A O ANISOU 4711 O SER E 229 9360 13413 14607 2180 -65 -2741 A O ATOM 4712 CB SER E 229 14.102 -27.258 4.872 1.00 85.49 A C ANISOU 4712 CB SER E 229 6697 11378 14408 1786 -310 -3391 A C ATOM 4713 OG SER E 229 12.942 -26.862 5.583 1.00 95.00 A O ANISOU 4713 OG SER E 229 7801 12243 16053 1601 -450 -3539 A O ATOM 4714 N LYS E 230 15.788 -27.435 1.920 1.00 99.95 A N ANISOU 4714 N LYS E 230 8755 13777 15446 1802 530 -2522 A N ATOM 4715 CA LYS E 230 17.089 -27.582 1.276 1.00103.21 A C ANISOU 4715 CA LYS E 230 9416 14504 15294 2083 601 -2463 A C ATOM 4716 C LYS E 230 17.641 -26.251 0.786 1.00107.63 A C ANISOU 4716 C LYS E 230 10619 15013 15264 2107 671 -2065 A C ATOM 4717 O LYS E 230 18.856 -26.124 0.600 1.00100.02 A O ANISOU 4717 O LYS E 230 10004 14215 13782 2394 579 -2102 A O ATOM 4718 CB LYS E 230 16.991 -28.567 0.109 1.00105.49 A C ANISOU 4718 CB LYS E 230 9233 15059 15788 1964 1030 -2338 A C ATOM 4719 CG LYS E 230 17.155 -30.025 0.506 1.00103.15 A C ANISOU 4719 CG LYS E 230 8356 14977 15861 2122 910 -2828 A C ATOM 4720 CD LYS E 230 17.693 -30.854 -0.651 1.00124.68 A C ANISOU 4720 CD LYS E 230 10808 18092 18474 2199 1297 -2743 A C ATOM 4721 CE LYS E 230 16.614 -31.745 -1.246 1.00125.07 A C ANISOU 4721 CE LYS E 230 10132 18191 19197 1821 1722 -2629 A C ATOM 4722 NZ LYS E 230 17.194 -32.914 -1.965 1.00104.54 A N1+ ANISOU 4722 NZ LYS E 230 7088 16036 16597 1987 1998 -2772 A N1+ ATOM 4723 N ARG E 231 16.778 -25.259 0.577 1.00 98.80 A N ANISOU 4723 N ARG E 231 9644 13647 14248 1821 809 -1705 A N ATOM 4724 CA ARG E 231 17.191 -23.928 0.154 1.00 99.82 A C ANISOU 4724 CA ARG E 231 10325 13717 13884 1821 845 -1346 A C ATOM 4725 C ARG E 231 17.701 -23.070 1.304 1.00100.08 A C ANISOU 4725 C ARG E 231 10796 13600 13631 2008 468 -1514 A C ATOM 4726 O ARG E 231 18.131 -21.937 1.063 1.00 98.81 A O ANISOU 4726 O ARG E 231 11075 13386 13084 2009 468 -1254 A O ATOM 4727 CB ARG E 231 16.021 -23.211 -0.523 1.00101.69 A C ANISOU 4727 CB ARG E 231 10513 13757 14369 1468 1130 -888 A C ATOM 4728 CG ARG E 231 15.821 -23.571 -1.979 1.00109.60 A C ANISOU 4728 CG ARG E 231 11337 14956 15350 1315 1569 -508 A C ATOM 4729 CD ARG E 231 14.416 -23.200 -2.448 1.00 96.22 A C ANISOU 4729 CD ARG E 231 9460 13007 14091 959 1834 -90 A C ATOM 4730 NE ARG E 231 14.138 -23.558 -3.837 1.00117.98 A N ANISOU 4730 NE ARG E 231 12054 15964 16811 810 2291 340 A N ATOM 4731 CZ ARG E 231 14.886 -23.238 -4.887 1.00125.33 A C ANISOU 4731 CZ ARG E 231 13271 17200 17146 937 2455 590 A C ATOM 4732 NH1 ARG E 231 15.955 -22.464 -4.774 1.00112.58 A N1+ ANISOU 4732 NH1 ARG E 231 12130 15677 14968 1178 2197 478 A N1+ ATOM 4733 NH2 ARG E 231 14.542 -23.693 -6.089 1.00122.62 A N ANISOU 4733 NH2 ARG E 231 12737 17076 16778 816 2896 966 A N ATOM 4734 N PHE E 232 17.674 -23.579 2.535 1.00 96.76 A N ANISOU 4734 N PHE E 232 10255 13131 13377 2170 152 -1937 A N ATOM 4735 CA PHE E 232 17.882 -22.742 3.712 1.00 93.01 A C ANISOU 4735 CA PHE E 232 10155 12510 12676 2314 -156 -2059 A C ATOM 4736 C PHE E 232 19.323 -22.265 3.857 1.00 94.01 A C ANISOU 4736 C PHE E 232 10799 12729 12193 2592 -309 -2026 A C ATOM 4737 O PHE E 232 19.599 -21.075 3.667 1.00100.21 A O ANISOU 4737 O PHE E 232 11974 13418 12683 2521 -254 -1732 A O ATOM 4738 CB PHE E 232 17.441 -23.490 4.971 1.00 98.16 A C ANISOU 4738 CB PHE E 232 10535 13130 13633 2446 -469 -2545 A C ATOM 4739 CG PHE E 232 15.966 -23.394 5.237 1.00 93.13 A C ANISOU 4739 CG PHE E 232 9568 12254 13565 2166 -419 -2592 A C ATOM 4740 CD1 PHE E 232 15.120 -22.805 4.309 1.00 95.58 A C ANISOU 4740 CD1 PHE E 232 9807 12391 14118 1826 -84 -2175 A C ATOM 4741 CD2 PHE E 232 15.424 -23.881 6.414 1.00 88.66 A C ANISOU 4741 CD2 PHE E 232 8778 11621 13289 2265 -732 -3062 A C ATOM 4742 CE1 PHE E 232 13.764 -22.709 4.547 1.00 87.61 A C ANISOU 4742 CE1 PHE E 232 8512 11097 13677 1579 -49 -2209 A C ATOM 4743 CE2 PHE E 232 14.067 -23.788 6.659 1.00 87.53 A C ANISOU 4743 CE2 PHE E 232 8336 11209 13712 2011 -709 -3150 A C ATOM 4744 CZ PHE E 232 13.236 -23.201 5.723 1.00 93.82 A C ANISOU 4744 CZ PHE E 232 9069 11785 14794 1662 -360 -2713 A C ATOM 4745 N ASP E 233 20.246 -23.169 4.201 1.00117.35 A N ANISOU 4745 N ASP E 233 13750 15848 14992 2910 -512 -2326 A N ATOM 4746 CA ASP E 233 21.633 -22.763 4.406 1.00124.27 A C ANISOU 4746 CA ASP E 233 15132 16742 15341 3185 -679 -2295 A C ATOM 4747 C ASP E 233 22.279 -22.242 3.132 1.00108.26 A C ANISOU 4747 C ASP E 233 13336 14752 13047 3098 -443 -1978 A C ATOM 4748 O ASP E 233 23.365 -21.657 3.203 1.00111.32 A O ANISOU 4748 O ASP E 233 14178 15077 13043 3248 -557 -1898 A O ATOM 4749 CB ASP E 233 22.463 -23.916 4.980 1.00110.71 A C ANISOU 4749 CB ASP E 233 13346 15173 13547 3582 -961 -2679 A C ATOM 4750 CG ASP E 233 22.174 -25.242 4.308 1.00117.78 A C ANISOU 4750 CG ASP E 233 13678 16278 14794 3585 -833 -2887 A C ATOM 4751 OD1 ASP E 233 21.811 -25.249 3.112 1.00120.70 A O ANISOU 4751 OD1 ASP E 233 13855 16717 15287 3340 -476 -2656 A O ATOM 4752 OD2 ASP E 233 22.309 -26.281 4.985 1.00116.14 A O1- ANISOU 4752 OD2 ASP E 233 13208 16188 14732 3844 -1088 -3278 A O1- ATOM 4753 N GLN E 234 21.644 -22.438 1.977 1.00101.16 A N ANISOU 4753 N GLN E 234 12143 13948 12344 2863 -123 -1795 A N ATOM 4754 CA GLN E 234 22.064 -21.711 0.787 1.00104.12 A C ANISOU 4754 CA GLN E 234 12768 14364 12428 2756 87 -1471 A C ATOM 4755 C GLN E 234 21.695 -20.237 0.917 1.00104.95 A C ANISOU 4755 C GLN E 234 13169 14263 12443 2539 95 -1164 A C ATOM 4756 O GLN E 234 22.575 -19.370 0.908 1.00105.98 A O ANISOU 4756 O GLN E 234 13721 14318 12228 2597 -7 -1061 A O ATOM 4757 CB GLN E 234 21.446 -22.337 -0.465 1.00 96.88 A C ANISOU 4757 CB GLN E 234 11468 13648 11694 2592 444 -1327 A C ATOM 4758 CG GLN E 234 21.644 -21.518 -1.744 1.00 94.48 A C ANISOU 4758 CG GLN E 234 11403 13421 11074 2470 663 -969 A C ATOM 4759 CD GLN E 234 21.037 -22.195 -2.964 1.00 97.78 A C ANISOU 4759 CD GLN E 234 11461 14084 11608 2342 1048 -792 A C ATOM 4760 NE2 GLN E 234 21.890 -22.657 -3.873 1.00 95.85 A N ANISOU 4760 NE2 GLN E 234 11270 14112 11036 2532 1162 -858 A N ATOM 4761 OE1 GLN E 234 19.817 -22.307 -3.082 1.00103.49 A O ANISOU 4761 OE1 GLN E 234 11865 14743 12714 2083 1251 -596 A O ATOM 4762 N ALA E 235 20.399 -19.935 1.117 1.00 99.31 A N ANISOU 4762 N ALA E 235 12537 11850 13347 3365 1483 -346 A N ATOM 4763 CA ALA E 235 19.942 -18.548 1.262 1.00 95.10 A C ANISOU 4763 CA ALA E 235 12353 11367 12415 3140 1438 -74 A C ATOM 4764 C ALA E 235 20.831 -17.731 2.203 1.00 93.66 A C ANISOU 4764 C ALA E 235 12315 11050 12221 3278 1160 357 A C ATOM 4765 O ALA E 235 20.839 -16.499 2.117 1.00 95.18 A O ANISOU 4765 O ALA E 235 12783 11208 12174 3104 1165 574 A O ATOM 4766 CB ALA E 235 18.483 -18.500 1.744 1.00 90.92 A C ANISOU 4766 CB ALA E 235 11789 11192 11566 2992 1396 -63 A C ATOM 4767 N LYS E 236 21.633 -18.392 3.050 1.00103.25 A N ANISOU 4767 N LYS E 236 13340 12180 13711 3569 909 507 A N ATOM 4768 CA LYS E 236 22.501 -17.684 3.989 1.00 99.92 A C ANISOU 4768 CA LYS E 236 13060 11642 13264 3659 617 973 A C ATOM 4769 C LYS E 236 23.494 -16.763 3.290 1.00 97.09 A C ANISOU 4769 C LYS E 236 12991 10898 13000 3553 677 1080 A C ATOM 4770 O LYS E 236 23.828 -15.704 3.829 1.00 96.63 A O ANISOU 4770 O LYS E 236 13132 10838 12747 3445 534 1482 A O ATOM 4771 CB LYS E 236 23.256 -18.683 4.869 1.00 96.79 A C ANISOU 4771 CB LYS E 236 12411 11156 13209 3983 302 1111 A C ATOM 4772 CG LYS E 236 23.011 -18.523 6.366 1.00116.34 A C ANISOU 4772 CG LYS E 236 14861 13942 15400 4023 -30 1521 A C ATOM 4773 CD LYS E 236 23.695 -17.287 6.915 1.00130.11 A C ANISOU 4773 CD LYS E 236 16895 15609 16933 3910 -176 2008 A C ATOM 4774 CE LYS E 236 23.449 -17.144 8.407 1.00124.00 A C ANISOU 4774 CE LYS E 236 16102 15209 15803 3921 -469 2400 A C ATOM 4775 NZ LYS E 236 23.595 -15.738 8.875 1.00103.45 A N1+ ANISOU 4775 NZ LYS E 236 13759 12744 12804 3703 -464 2799 A N1+ ATOM 4776 N GLU E 237 23.999 -17.142 2.113 1.00 91.53 A N ANISOU 4776 N GLU E 237 12312 9884 12582 3565 884 724 A N ATOM 4777 CA GLU E 237 24.963 -16.273 1.446 1.00 81.00 A C ANISOU 4777 CA GLU E 237 11286 8157 11335 3443 904 800 A C ATOM 4778 C GLU E 237 24.297 -15.114 0.710 1.00 93.76 A C ANISOU 4778 C GLU E 237 13167 9895 12563 3070 1100 798 A C ATOM 4779 O GLU E 237 24.996 -14.340 0.048 1.00 92.51 A O ANISOU 4779 O GLU E 237 13273 9438 12438 2908 1118 840 A O ATOM 4780 CB GLU E 237 25.865 -17.070 0.480 1.00107.27 A C ANISOU 4780 CB GLU E 237 14576 11072 15111 3612 1038 384 A C ATOM 4781 CG GLU E 237 26.209 -18.487 0.944 1.00116.65 A C ANISOU 4781 CG GLU E 237 15382 12208 16734 4010 929 223 A C ATOM 4782 CD GLU E 237 25.596 -19.562 0.085 1.00122.43 A C ANISOU 4782 CD GLU E 237 15840 13121 17558 4051 1280 -337 A C ATOM 4783 OE1 GLU E 237 26.250 -20.612 -0.083 1.00128.15 A O ANISOU 4783 OE1 GLU E 237 16294 13643 18756 4372 1298 -620 A O ATOM 4784 OE2 GLU E 237 24.518 -19.340 -0.489 1.00118.57 A O1- ANISOU 4784 OE2 GLU E 237 15406 12950 16696 3756 1544 -500 A O1- ATOM 4785 N PHE E 238 22.976 -14.955 0.827 1.00 86.17 A N ANISOU 4785 N PHE E 238 12146 9339 11257 2930 1205 763 A N ATOM 4786 CA PHE E 238 22.271 -13.837 0.211 1.00 79.92 A C ANISOU 4786 CA PHE E 238 11574 8660 10131 2607 1333 802 A C ATOM 4787 C PHE E 238 21.740 -12.846 1.242 1.00 82.06 A C ANISOU 4787 C PHE E 238 11860 9219 10099 2555 1181 1199 A C ATOM 4788 O PHE E 238 20.877 -12.021 0.921 1.00 72.98 A O ANISOU 4788 O PHE E 238 10806 8239 8685 2349 1265 1217 A O ATOM 4789 CB PHE E 238 21.134 -14.350 -0.674 1.00 73.72 A C ANISOU 4789 CB PHE E 238 10743 8056 9211 2455 1584 419 A C ATOM 4790 CG PHE E 238 21.596 -15.217 -1.809 1.00 78.54 A C ANISOU 4790 CG PHE E 238 11342 8461 10039 2448 1812 -4 A C ATOM 4791 CD1 PHE E 238 21.809 -16.574 -1.622 1.00 90.54 A C ANISOU 4791 CD1 PHE E 238 12560 9992 11849 2708 1860 -255 A C ATOM 4792 CD2 PHE E 238 21.822 -14.675 -3.063 1.00 78.62 A C ANISOU 4792 CD2 PHE E 238 11624 8292 9954 2179 1979 -165 A C ATOM 4793 CE1 PHE E 238 22.237 -17.373 -2.666 1.00 82.23 A C ANISOU 4793 CE1 PHE E 238 11452 8794 10997 2722 2120 -688 A C ATOM 4794 CE2 PHE E 238 22.248 -15.469 -4.111 1.00 74.99 A C ANISOU 4794 CE2 PHE E 238 11163 7687 9641 2166 2229 -600 A C ATOM 4795 CZ PHE E 238 22.457 -16.820 -3.912 1.00 73.29 A C ANISOU 4795 CZ PHE E 238 10620 7503 9724 2449 2324 -877 A C ATOM 4796 N GLY E 239 22.246 -12.904 2.473 1.00 77.88 A N ANISOU 4796 N GLY E 239 11234 8757 9602 2738 954 1517 A N ATOM 4797 CA GLY E 239 21.846 -12.008 3.531 1.00 72.07 A C ANISOU 4797 CA GLY E 239 10494 8342 8547 2698 843 1877 A C ATOM 4798 C GLY E 239 20.861 -12.594 4.522 1.00 76.37 A C ANISOU 4798 C GLY E 239 10848 9277 8892 2846 788 1821 A C ATOM 4799 O GLY E 239 20.689 -12.028 5.608 1.00 72.30 A O ANISOU 4799 O GLY E 239 10312 9053 8106 2865 679 2109 A O ATOM 4800 N VAL E 240 20.217 -13.712 4.178 1.00 78.48 A N ANISOU 4800 N VAL E 240 10974 9576 9267 2927 864 1452 A N ATOM 4801 CA VAL E 240 19.205 -14.305 5.048 1.00 84.39 A C ANISOU 4801 CA VAL E 240 11558 10672 9833 3028 787 1359 A C ATOM 4802 C VAL E 240 19.837 -14.670 6.383 1.00 78.04 A C ANISOU 4802 C VAL E 240 10649 9989 9015 3222 509 1657 A C ATOM 4803 O VAL E 240 20.809 -15.433 6.441 1.00 83.86 A O ANISOU 4803 O VAL E 240 11292 10495 10076 3378 368 1715 A O ATOM 4804 CB VAL E 240 18.567 -15.525 4.375 1.00 68.89 A C ANISOU 4804 CB VAL E 240 9436 8688 8051 3039 898 942 A C ATOM 4805 CG1 VAL E 240 17.501 -16.132 5.275 1.00 74.93 A C ANISOU 4805 CG1 VAL E 240 10045 9785 8639 3105 777 844 A C ATOM 4806 CG2 VAL E 240 17.974 -15.133 3.031 1.00 63.22 A C ANISOU 4806 CG2 VAL E 240 8862 7861 7297 2793 1154 702 A C ATOM 4807 N THR E 241 19.286 -14.122 7.466 1.00 68.48 A N ANISOU 4807 N THR E 241 9455 9141 7422 3217 419 1842 A N ATOM 4808 CA THR E 241 19.816 -14.365 8.801 1.00 81.82 A C ANISOU 4808 CA THR E 241 11086 11017 8985 3343 142 2169 A C ATOM 4809 C THR E 241 19.171 -15.562 9.484 1.00 90.05 A C ANISOU 4809 C THR E 241 11940 12278 9997 3482 -30 1980 A C ATOM 4810 O THR E 241 19.794 -16.174 10.360 1.00 91.78 A O ANISOU 4810 O THR E 241 12068 12544 10260 3612 -319 2213 A O ATOM 4811 CB THR E 241 19.639 -13.119 9.673 1.00 82.96 A C ANISOU 4811 CB THR E 241 11346 11504 8671 3240 156 2473 A C ATOM 4812 CG2 THR E 241 19.820 -11.860 8.840 1.00 78.37 A C ANISOU 4812 CG2 THR E 241 10903 10779 8096 3059 373 2554 A C ATOM 4813 OG1 THR E 241 18.332 -13.123 10.261 1.00 94.13 A O ANISOU 4813 OG1 THR E 241 12723 13309 9734 3259 200 2241 A O ATOM 4814 N GLU E 242 17.941 -15.908 9.111 1.00 79.21 A N ANISOU 4814 N GLU E 242 10511 11026 8560 3434 102 1591 A N ATOM 4815 CA GLU E 242 17.296 -17.105 9.630 1.00 78.01 A C ANISOU 4815 CA GLU E 242 10164 11050 8425 3520 -71 1381 A C ATOM 4816 C GLU E 242 16.177 -17.507 8.684 1.00 89.21 A C ANISOU 4816 C GLU E 242 11534 12421 9941 3402 130 948 A C ATOM 4817 O GLU E 242 15.620 -16.670 7.968 1.00 80.39 A O ANISOU 4817 O GLU E 242 10580 11244 8721 3255 356 841 A O ATOM 4818 CB GLU E 242 16.752 -16.897 11.050 1.00 69.39 A C ANISOU 4818 CB GLU E 242 9118 10379 6866 3542 -270 1502 A C ATOM 4819 CG GLU E 242 15.738 -15.776 11.181 1.00 82.57 A C ANISOU 4819 CG GLU E 242 10967 12272 8133 3435 -79 1387 A C ATOM 4820 CD GLU E 242 15.704 -15.187 12.579 1.00 91.38 A C ANISOU 4820 CD GLU E 242 12172 13802 8747 3462 -205 1615 A C ATOM 4821 OE1 GLU E 242 15.258 -15.889 13.511 1.00 97.31 A O ANISOU 4821 OE1 GLU E 242 12872 14813 9287 3511 -433 1532 A O ATOM 4822 OE2 GLU E 242 16.124 -14.023 12.747 1.00 82.48 A O1- ANISOU 4822 OE2 GLU E 242 11159 12766 7416 3411 -75 1875 A O1- ATOM 4823 N CYS E 243 15.860 -18.798 8.687 1.00 98.40 A N ANISOU 4823 N CYS E 243 12457 13615 11314 3446 21 731 A N ATOM 4824 CA CYS E 243 14.836 -19.358 7.821 1.00 78.99 A C ANISOU 4824 CA CYS E 243 9918 11127 8967 3289 185 356 A C ATOM 4825 C CYS E 243 13.759 -20.032 8.660 1.00 83.06 A C ANISOU 4825 C CYS E 243 10332 11916 9310 3259 -32 195 A C ATOM 4826 O CYS E 243 14.022 -20.514 9.766 1.00 79.58 A O ANISOU 4826 O CYS E 243 9782 11664 8790 3392 -327 332 A O ATOM 4827 CB CYS E 243 15.434 -20.366 6.835 1.00 88.19 A C ANISOU 4827 CB CYS E 243 10839 12077 10591 3313 311 192 A C ATOM 4828 SG CYS E 243 16.667 -19.671 5.711 1.00 95.12 A S ANISOU 4828 SG CYS E 243 11872 12587 11685 3325 567 281 A S ATOM 4829 N VAL E 244 12.538 -20.053 8.128 1.00 88.99 A N ANISOU 4829 N VAL E 244 11143 12670 9998 3060 82 -84 A N ATOM 4830 CA VAL E 244 11.393 -20.653 8.805 1.00 81.28 A C ANISOU 4830 CA VAL E 244 10113 11893 8876 2982 -127 -284 A C ATOM 4831 C VAL E 244 10.613 -21.490 7.800 1.00 91.83 A C ANISOU 4831 C VAL E 244 11305 13125 10461 2746 -10 -565 A C ATOM 4832 O VAL E 244 10.440 -21.090 6.644 1.00 83.95 A O ANISOU 4832 O VAL E 244 10417 11935 9544 2585 260 -633 A O ATOM 4833 CB VAL E 244 10.478 -19.587 9.446 1.00 89.40 A C ANISOU 4833 CB VAL E 244 11441 13042 9485 2963 -161 -330 A C ATOM 4834 CG1 VAL E 244 9.335 -20.249 10.202 1.00 89.89 A C ANISOU 4834 CG1 VAL E 244 11479 13275 9399 2888 -415 -576 A C ATOM 4835 CG2 VAL E 244 11.269 -18.680 10.377 1.00 83.81 A C ANISOU 4835 CG2 VAL E 244 10859 12497 8487 3148 -211 -35 A C ATOM 4836 N ASN E 245 10.143 -22.656 8.243 1.00 98.84 A N ANISOU 4836 N ASN E 245 11942 14160 11452 2691 -229 -704 A N ATOM 4837 CA ASN E 245 9.265 -23.494 7.446 1.00 90.53 A C ANISOU 4837 CA ASN E 245 10735 13067 10597 2408 -153 -951 A C ATOM 4838 C ASN E 245 7.878 -23.510 8.069 1.00 99.59 A C ANISOU 4838 C ASN E 245 12034 14290 11514 2242 -388 -1125 A C ATOM 4839 O ASN E 245 7.748 -23.809 9.264 1.00101.08 A O ANISOU 4839 O ASN E 245 12188 14676 11543 2349 -707 -1124 A O ATOM 4840 CB ASN E 245 9.810 -24.922 7.349 1.00101.25 A C ANISOU 4840 CB ASN E 245 11612 14527 12332 2441 -212 -994 A C ATOM 4841 CG ASN E 245 9.076 -25.755 6.316 1.00111.51 A C ANISOU 4841 CG ASN E 245 12705 15814 13851 2108 -33 -1220 A C ATOM 4842 ND2 ASN E 245 9.828 -26.443 5.468 1.00117.02 A N ANISOU 4842 ND2 ASN E 245 13077 16500 14885 2128 217 -1270 A N ATOM 4843 OD1 ASN E 245 7.849 -25.784 6.285 1.00111.51 A O ANISOU 4843 OD1 ASN E 245 12835 15813 13720 1828 -116 -1352 A O ATOM 4844 N PRO E 246 6.827 -23.195 7.305 1.00103.43 A N ANISOU 4844 N PRO E 246 12716 14609 11975 1972 -271 -1276 A N ATOM 4845 CA PRO E 246 5.476 -23.179 7.895 1.00106.38 A C ANISOU 4845 CA PRO E 246 13271 14977 12170 1826 -526 -1470 A C ATOM 4846 C PRO E 246 5.023 -24.518 8.455 1.00108.17 A C ANISOU 4846 C PRO E 246 13214 15371 12517 1683 -823 -1605 A C ATOM 4847 O PRO E 246 4.466 -24.553 9.560 1.00101.10 A O ANISOU 4847 O PRO E 246 12426 14587 11399 1732 -1141 -1714 A O ATOM 4848 CB PRO E 246 4.597 -22.723 6.722 1.00102.52 A C ANISOU 4848 CB PRO E 246 13002 14212 11741 1536 -345 -1547 A C ATOM 4849 CG PRO E 246 5.510 -21.911 5.868 1.00 94.21 A C ANISOU 4849 CG PRO E 246 12029 13055 10713 1632 -17 -1364 A C ATOM 4850 CD PRO E 246 6.858 -22.575 5.969 1.00 89.71 A C ANISOU 4850 CD PRO E 246 11130 12646 10309 1819 64 -1246 A C ATOM 4851 N LYS E 247 5.234 -25.625 7.736 1.00112.74 A N ANISOU 4851 N LYS E 247 13415 15992 13428 1496 -729 -1617 A N ATOM 4852 CA LYS E 247 4.772 -26.913 8.246 1.00116.28 A C ANISOU 4852 CA LYS E 247 13538 16618 14025 1328 -1029 -1732 A C ATOM 4853 C LYS E 247 5.565 -27.381 9.460 1.00104.99 A C ANISOU 4853 C LYS E 247 11888 15444 12562 1626 -1329 -1630 A C ATOM 4854 O LYS E 247 5.161 -28.357 10.101 1.00116.92 A O ANISOU 4854 O LYS E 247 13158 17124 14142 1509 -1666 -1713 A O ATOM 4855 CB LYS E 247 4.819 -27.986 7.151 1.00116.51 A C ANISOU 4855 CB LYS E 247 13151 16686 14431 1047 -813 -1771 A C ATOM 4856 CG LYS E 247 6.197 -28.270 6.579 1.00117.42 A C ANISOU 4856 CG LYS E 247 12939 16873 14802 1277 -515 -1659 A C ATOM 4857 CD LYS E 247 6.127 -28.581 5.088 1.00111.09 A C ANISOU 4857 CD LYS E 247 11996 16016 14196 980 -92 -1730 A C ATOM 4858 CE LYS E 247 7.405 -29.242 4.586 1.00111.30 A C ANISOU 4858 CE LYS E 247 11575 16160 14552 1196 174 -1724 A C ATOM 4859 NZ LYS E 247 7.910 -28.590 3.344 1.00106.60 A N1+ ANISOU 4859 NZ LYS E 247 11168 15409 13928 1163 634 -1727 A N1+ ATOM 4860 N ASP E 248 6.670 -26.714 9.790 1.00 97.91 A N ANISOU 4860 N ASP E 248 6626 13132 17445 1548 -855 -1673 A N ATOM 4861 CA ASP E 248 7.418 -26.996 11.007 1.00106.88 A C ANISOU 4861 CA ASP E 248 7627 14443 18539 1713 -1282 -1585 A C ATOM 4862 C ASP E 248 6.851 -26.286 12.229 1.00101.14 A C ANISOU 4862 C ASP E 248 7242 13764 17423 1553 -1698 -1717 A C ATOM 4863 O ASP E 248 7.418 -26.419 13.319 1.00 94.48 A O ANISOU 4863 O ASP E 248 6341 13094 16464 1652 -2081 -1637 A O ATOM 4864 CB ASP E 248 8.887 -26.599 10.828 1.00 98.06 A C ANISOU 4864 CB ASP E 248 6638 13273 17347 2120 -1144 -1447 A C ATOM 4865 CG ASP E 248 9.675 -27.617 10.033 1.00120.76 A C ANISOU 4865 CG ASP E 248 9066 16171 20646 2373 -879 -1319 A C ATOM 4866 OD1 ASP E 248 9.059 -28.567 9.505 1.00133.36 A O ANISOU 4866 OD1 ASP E 248 10237 17861 22571 2221 -731 -1321 A O ATOM 4867 OD2 ASP E 248 10.911 -27.467 9.936 1.00120.94 A O1- ANISOU 4867 OD2 ASP E 248 9162 16117 20674 2728 -821 -1214 A O1- ATOM 4868 N HIS E 249 5.755 -25.544 12.081 1.00 94.86 A N ANISOU 4868 N HIS E 249 6801 12825 16415 1325 -1633 -1915 A N ATOM 4869 CA HIS E 249 5.202 -24.740 13.160 1.00105.85 A C ANISOU 4869 CA HIS E 249 8570 14255 17391 1233 -1954 -2089 A C ATOM 4870 C HIS E 249 3.704 -24.980 13.275 1.00108.94 A C ANISOU 4870 C HIS E 249 9001 14544 17847 874 -2111 -2311 A C ATOM 4871 O HIS E 249 3.000 -25.080 12.265 1.00 91.36 A O ANISOU 4871 O HIS E 249 6757 12120 15837 706 -1836 -2343 A O ATOM 4872 CB HIS E 249 5.480 -23.249 12.933 1.00 88.96 A C ANISOU 4872 CB HIS E 249 6943 12009 14849 1403 -1716 -2122 A C ATOM 4873 CG HIS E 249 6.913 -22.865 13.138 1.00 92.07 A C ANISOU 4873 CG HIS E 249 7388 12500 15093 1706 -1701 -1908 A C ATOM 4874 CD2 HIS E 249 7.955 -22.817 12.275 1.00 86.77 A C ANISOU 4874 CD2 HIS E 249 6683 11726 14559 1927 -1405 -1730 A C ATOM 4875 ND1 HIS E 249 7.411 -22.476 14.363 1.00 86.38 A N ANISOU 4875 ND1 HIS E 249 6790 11994 14036 1795 -2043 -1854 A N ATOM 4876 CE1 HIS E 249 8.698 -22.202 14.245 1.00101.11 A C ANISOU 4876 CE1 HIS E 249 8685 13867 15863 2039 -1976 -1620 A C ATOM 4877 NE2 HIS E 249 9.053 -22.401 12.989 1.00107.53 A N ANISOU 4877 NE2 HIS E 249 9421 14468 16967 2133 -1598 -1560 A N ATOM 4878 N ASP E 250 3.225 -25.069 14.518 1.00103.68 A N ANISOU 4878 N ASP E 250 8414 14003 16976 745 -2574 -2462 A N ATOM 4879 CA ASP E 250 1.799 -25.263 14.762 1.00101.33 A C ANISOU 4879 CA ASP E 250 8225 13562 16712 404 -2801 -2711 A C ATOM 4880 C ASP E 250 0.995 -24.055 14.298 1.00113.18 A C ANISOU 4880 C ASP E 250 10233 14792 17980 403 -2555 -2921 A C ATOM 4881 O ASP E 250 -0.019 -24.192 13.603 1.00106.59 A O ANISOU 4881 O ASP E 250 9435 13696 17369 161 -2457 -3008 A O ATOM 4882 CB ASP E 250 1.558 -25.522 16.250 1.00101.07 A C ANISOU 4882 CB ASP E 250 8244 13729 16431 302 -3363 -2859 A C ATOM 4883 CG ASP E 250 1.279 -26.979 16.555 1.00127.11 A C ANISOU 4883 CG ASP E 250 11051 17131 20112 12 -3732 -2774 A C ATOM 4884 OD1 ASP E 250 0.650 -27.655 15.713 1.00107.62 A O ANISOU 4884 OD1 ASP E 250 8325 14504 18061 -233 -3609 -2724 A O ATOM 4885 OD2 ASP E 250 1.687 -27.446 17.638 1.00126.40 A O1- ANISOU 4885 OD2 ASP E 250 10821 17304 19903 10 -4157 -2728 A O1- ATOM 4886 N LYS E 251 1.439 -22.863 14.676 1.00116.97 A N ANISOU 4886 N LYS E 251 11084 15337 18021 665 -2466 -2973 A N ATOM 4887 CA LYS E 251 0.701 -21.638 14.439 1.00108.38 A C ANISOU 4887 CA LYS E 251 10462 14044 16672 712 -2283 -3172 A C ATOM 4888 C LYS E 251 0.921 -21.148 13.010 1.00 98.14 A C ANISOU 4888 C LYS E 251 9208 12546 15536 782 -1789 -3005 A C ATOM 4889 O LYS E 251 1.922 -21.491 12.376 1.00 97.42 A O ANISOU 4889 O LYS E 251 8874 12528 15612 892 -1567 -2753 A O ATOM 4890 CB LYS E 251 1.143 -20.590 15.455 1.00105.72 A C ANISOU 4890 CB LYS E 251 10438 13940 15791 962 -2382 -3252 A C ATOM 4891 CG LYS E 251 0.896 -21.036 16.893 1.00104.85 A C ANISOU 4891 CG LYS E 251 10333 14058 15447 881 -2876 -3435 A C ATOM 4892 CD LYS E 251 1.271 -19.973 17.910 1.00101.07 A C ANISOU 4892 CD LYS E 251 10164 13864 14372 1116 -2945 -3513 A C ATOM 4893 CE LYS E 251 2.782 -19.811 18.029 1.00101.33 A C ANISOU 4893 CE LYS E 251 10039 14174 14286 1321 -2870 -3150 A C ATOM 4894 NZ LYS E 251 3.453 -21.035 18.545 1.00117.79 A N1+ ANISOU 4894 NZ LYS E 251 11740 16444 16570 1238 -3201 -2966 A N1+ ATOM 4895 N PRO E 252 -0.017 -20.369 12.468 1.00107.65 A N ANISOU 4895 N PRO E 252 10727 13480 16696 723 -1623 -3147 A N ATOM 4896 CA PRO E 252 0.160 -19.841 11.108 1.00104.77 A C ANISOU 4896 CA PRO E 252 10434 12934 16440 764 -1179 -2976 A C ATOM 4897 C PRO E 252 1.437 -19.021 10.996 1.00 89.53 A C ANISOU 4897 C PRO E 252 8600 11173 14245 1063 -963 -2785 A C ATOM 4898 O PRO E 252 1.946 -18.475 11.977 1.00 94.57 A O ANISOU 4898 O PRO E 252 9360 12033 14540 1246 -1126 -2809 A O ATOM 4899 CB PRO E 252 -1.081 -18.966 10.878 1.00 84.65 A C ANISOU 4899 CB PRO E 252 8261 10094 13809 693 -1143 -3175 A C ATOM 4900 CG PRO E 252 -1.955 -19.127 12.065 1.00101.63 A C ANISOU 4900 CG PRO E 252 10539 12233 15842 615 -1556 -3489 A C ATOM 4901 CD PRO E 252 -1.323 -20.034 13.059 1.00106.43 A C ANISOU 4901 CD PRO E 252 10871 13147 16420 603 -1868 -3475 A C ATOM 4902 N ILE E 253 1.959 -18.944 9.769 1.00 76.51 A N ANISOU 4902 N ILE E 253 6906 9421 12744 1089 -600 -2582 A N ATOM 4903 CA ILE E 253 3.254 -18.298 9.565 1.00 91.18 A C ANISOU 4903 CA ILE E 253 8849 11393 14401 1335 -423 -2381 A C ATOM 4904 C ILE E 253 3.198 -16.829 9.959 1.00 86.89 A C ANISOU 4904 C ILE E 253 8680 10887 13446 1476 -414 -2411 A C ATOM 4905 O ILE E 253 4.191 -16.274 10.443 1.00 83.78 A O ANISOU 4905 O ILE E 253 8356 10687 12792 1660 -455 -2275 A O ATOM 4906 CB ILE E 253 3.731 -18.483 8.111 1.00 78.10 A C ANISOU 4906 CB ILE E 253 7130 9591 12955 1320 -37 -2203 A C ATOM 4907 CG1 ILE E 253 5.141 -17.911 7.940 1.00 87.52 A C ANISOU 4907 CG1 ILE E 253 8433 10859 13962 1561 86 -2009 A C ATOM 4908 CG2 ILE E 253 2.784 -17.808 7.152 1.00 84.41 A C ANISOU 4908 CG2 ILE E 253 8170 10144 13758 1169 191 -2233 A C ATOM 4909 CD1 ILE E 253 6.240 -18.910 8.222 1.00 81.23 A C ANISOU 4909 CD1 ILE E 253 7326 10199 13341 1703 -4 -1903 A C ATOM 4910 N GLN E 254 2.046 -16.179 9.784 1.00 78.80 A N ANISOU 4910 N GLN E 254 7884 9688 12367 1396 -375 -2570 A N ATOM 4911 CA GLN E 254 1.921 -14.792 10.222 1.00 86.49 A C ANISOU 4911 CA GLN E 254 9162 10740 12962 1564 -361 -2607 A C ATOM 4912 C GLN E 254 2.112 -14.682 11.729 1.00 89.48 A C ANISOU 4912 C GLN E 254 9550 11430 13020 1695 -661 -2730 A C ATOM 4913 O GLN E 254 2.869 -13.831 12.210 1.00 81.06 A O ANISOU 4913 O GLN E 254 8579 10607 11611 1871 -650 -2596 A O ATOM 4914 CB GLN E 254 0.564 -14.221 9.805 1.00 86.17 A C ANISOU 4914 CB GLN E 254 9340 10426 12974 1486 -294 -2779 A C ATOM 4915 CG GLN E 254 -0.591 -15.201 9.900 1.00 89.81 A C ANISOU 4915 CG GLN E 254 9718 10672 13732 1258 -482 -3007 A C ATOM 4916 CD GLN E 254 -0.979 -15.774 8.554 1.00 92.24 A C ANISOU 4916 CD GLN E 254 9925 10700 14423 1013 -278 -2878 A C ATOM 4917 NE2 GLN E 254 -2.047 -15.242 7.973 1.00 81.98 A N ANISOU 4917 NE2 GLN E 254 8840 9100 13211 920 -211 -2940 A N ATOM 4918 OE1 GLN E 254 -0.325 -16.681 8.039 1.00 94.04 A O ANISOU 4918 OE1 GLN E 254 9880 10991 14860 920 -177 -2716 A O ATOM 4919 N GLN E 255 1.447 -15.555 12.489 1.00 92.70 A N ANISOU 4919 N GLN E 255 9856 11850 13517 1582 -949 -2964 A N ATOM 4920 CA GLN E 255 1.589 -15.536 13.941 1.00 93.01 A C ANISOU 4920 CA GLN E 255 9918 12204 13217 1679 -1259 -3096 A C ATOM 4921 C GLN E 255 3.014 -15.878 14.357 1.00 93.36 A C ANISOU 4921 C GLN E 255 9762 12537 13174 1765 -1347 -2822 A C ATOM 4922 O GLN E 255 3.556 -15.272 15.291 1.00 83.44 A O ANISOU 4922 O GLN E 255 8594 11596 11515 1908 -1464 -2766 A O ATOM 4923 CB GLN E 255 0.590 -16.505 14.575 1.00 93.48 A C ANISOU 4923 CB GLN E 255 9918 12180 13419 1490 -1587 -3395 A C ATOM 4924 CG GLN E 255 0.048 -16.044 15.915 1.00104.69 A C ANISOU 4924 CG GLN E 255 11568 13800 14409 1590 -1850 -3697 A C ATOM 4925 CD GLN E 255 -0.371 -17.195 16.807 1.00101.45 A C ANISOU 4925 CD GLN E 255 11039 13444 14065 1396 -2277 -3900 A C ATOM 4926 NE2 GLN E 255 -0.113 -17.061 18.103 1.00103.90 A N ANISOU 4926 NE2 GLN E 255 11427 14108 13940 1491 -2539 -4008 A N ATOM 4927 OE1 GLN E 255 -0.932 -18.187 16.341 1.00 95.33 A O ANISOU 4927 OE1 GLN E 255 10097 12415 13710 1140 -2382 -3941 A O ATOM 4928 N VAL E 256 3.640 -16.832 13.662 1.00 92.72 A N ANISOU 4928 N VAL E 256 9407 12354 13467 1690 -1286 -2636 A N ATOM 4929 CA VAL E 256 5.042 -17.152 13.922 1.00 88.06 A C ANISOU 4929 CA VAL E 256 8640 11959 12858 1807 -1361 -2361 A C ATOM 4930 C VAL E 256 5.902 -15.904 13.764 1.00 68.07 A C ANISOU 4930 C VAL E 256 6330 9515 10017 1975 -1184 -2138 A C ATOM 4931 O VAL E 256 6.497 -15.416 14.731 1.00 85.27 A O ANISOU 4931 O VAL E 256 8572 11985 11841 2074 -1361 -2032 A O ATOM 4932 CB VAL E 256 5.522 -18.286 12.999 1.00 94.58 A C ANISOU 4932 CB VAL E 256 9152 12620 14163 1755 -1241 -2223 A C ATOM 4933 CG1 VAL E 256 7.014 -18.523 13.184 1.00 84.35 A C ANISOU 4933 CG1 VAL E 256 7719 11457 12875 1931 -1307 -1944 A C ATOM 4934 CG2 VAL E 256 4.740 -19.561 13.272 1.00 74.95 A C ANISOU 4934 CG2 VAL E 256 6379 10116 11982 1559 -1463 -2383 A C ATOM 4935 N ILE E 257 5.948 -15.354 12.544 1.00 74.34 A N ANISOU 4935 N ILE E 257 7247 10076 10924 1977 -848 -2046 A N ATOM 4936 CA ILE E 257 6.800 -14.199 12.254 1.00 84.80 A C ANISOU 4936 CA ILE E 257 8771 11452 11998 2090 -695 -1799 A C ATOM 4937 C ILE E 257 6.507 -13.046 13.207 1.00 83.90 A C ANISOU 4937 C ILE E 257 8846 11617 11416 2170 -782 -1832 A C ATOM 4938 O ILE E 257 7.416 -12.310 13.611 1.00 92.02 A O ANISOU 4938 O ILE E 257 9944 12864 12155 2253 -824 -1583 A O ATOM 4939 CB ILE E 257 6.636 -13.767 10.783 1.00 81.37 A C ANISOU 4939 CB ILE E 257 8467 10715 11733 2037 -345 -1740 A C ATOM 4940 CG1 ILE E 257 6.858 -14.951 9.836 1.00 71.99 A C ANISOU 4940 CG1 ILE E 257 7077 9304 10970 1969 -215 -1734 A C ATOM 4941 CG2 ILE E 257 7.588 -12.626 10.452 1.00 83.39 A C ANISOU 4941 CG2 ILE E 257 8924 11012 11747 2114 -233 -1458 A C ATOM 4942 CD1 ILE E 257 7.128 -14.547 8.397 1.00 71.59 A C ANISOU 4942 CD1 ILE E 257 7176 9012 11014 1937 120 -1610 A C ATOM 4943 N ALA E 258 5.239 -12.871 13.588 1.00 76.34 A N ANISOU 4943 N ALA E 258 7972 10660 10373 2149 -813 -2135 A N ATOM 4944 CA ALA E 258 4.898 -11.812 14.532 1.00 79.02 A C ANISOU 4944 CA ALA E 258 8476 11297 10250 2273 -865 -2215 A C ATOM 4945 C ALA E 258 5.527 -12.071 15.895 1.00 84.50 A C ANISOU 4945 C ALA E 258 9086 12390 10630 2320 -1166 -2163 A C ATOM 4946 O ALA E 258 6.129 -11.172 16.492 1.00 95.82 A O ANISOU 4946 O ALA E 258 10586 14156 11663 2417 -1174 -1966 A O ATOM 4947 CB ALA E 258 3.380 -11.681 14.648 1.00 66.09 A C ANISOU 4947 CB ALA E 258 6972 9518 8624 2273 -855 -2603 A C ATOM 4948 N GLU E 259 5.406 -13.301 16.400 1.00 83.20 A N ANISOU 4948 N GLU E 259 8757 12219 10636 2228 -1430 -2301 A N ATOM 4949 CA GLU E 259 6.008 -13.630 17.686 1.00 77.54 A C ANISOU 4949 CA GLU E 259 7955 11879 9628 2246 -1757 -2225 A C ATOM 4950 C GLU E 259 7.532 -13.607 17.641 1.00 92.39 A C ANISOU 4950 C GLU E 259 9730 13871 11503 2282 -1803 -1786 A C ATOM 4951 O GLU E 259 8.165 -13.439 18.689 1.00 96.61 A O ANISOU 4951 O GLU E 259 10252 14769 11686 2312 -2032 -1621 A O ATOM 4952 CB GLU E 259 5.512 -14.995 18.162 1.00 81.57 A C ANISOU 4952 CB GLU E 259 8291 12335 10366 2111 -2061 -2447 A C ATOM 4953 CG GLU E 259 4.117 -14.960 18.767 1.00 95.81 A C ANISOU 4953 CG GLU E 259 10263 14142 12000 2069 -2176 -2890 A C ATOM 4954 CD GLU E 259 3.457 -16.323 18.794 1.00104.93 A C ANISOU 4954 CD GLU E 259 11247 15095 13528 1863 -2428 -3098 A C ATOM 4955 OE1 GLU E 259 3.965 -17.214 19.506 1.00115.07 A O ANISOU 4955 OE1 GLU E 259 12326 16569 14826 1785 -2754 -3006 A O ATOM 4956 OE2 GLU E 259 2.431 -16.503 18.105 1.00 98.17 A O1- ANISOU 4956 OE2 GLU E 259 10449 13892 12958 1761 -2321 -3323 A O1- ATOM 4957 N MET E 260 8.134 -13.772 16.460 1.00 92.37 A N ANISOU 4957 N MET E 260 9674 13555 11868 2277 -1604 -1595 A N ATOM 4958 CA MET E 260 9.583 -13.653 16.333 1.00 85.35 A C ANISOU 4958 CA MET E 260 8750 12692 10987 2328 -1650 -1197 A C ATOM 4959 C MET E 260 10.066 -12.210 16.382 1.00 88.32 A C ANISOU 4959 C MET E 260 9332 13249 10975 2368 -1529 -947 A C ATOM 4960 O MET E 260 11.231 -11.973 16.716 1.00 83.88 A O ANISOU 4960 O MET E 260 8772 12819 10281 2380 -1675 -596 A O ATOM 4961 CB MET E 260 10.075 -14.282 15.024 1.00 82.37 A C ANISOU 4961 CB MET E 260 8288 11909 11101 2332 -1463 -1116 A C ATOM 4962 CG MET E 260 9.439 -15.607 14.652 1.00 92.09 A C ANISOU 4962 CG MET E 260 9283 12943 12764 2274 -1469 -1352 A C ATOM 4963 SD MET E 260 10.207 -16.404 13.225 1.00 88.76 A S ANISOU 4963 SD MET E 260 8720 12146 12859 2330 -1231 -1233 A S ATOM 4964 CE MET E 260 11.815 -15.614 13.204 1.00 77.13 A C ANISOU 4964 CE MET E 260 7434 10669 11204 2459 -1275 -846 A C ATOM 4965 N THR E 261 9.203 -11.247 16.060 1.00 87.68 A N ANISOU 4965 N THR E 261 9409 13177 10729 2383 -1287 -1092 A N ATOM 4966 CA THR E 261 9.623 -9.869 15.838 1.00 90.35 A C ANISOU 4966 CA THR E 261 9897 13649 10783 2407 -1126 -824 A C ATOM 4967 C THR E 261 8.882 -8.862 16.709 1.00 91.17 A C ANISOU 4967 C THR E 261 10075 14157 10410 2488 -1085 -939 A C ATOM 4968 O THR E 261 8.968 -7.656 16.446 1.00 94.85 A O ANISOU 4968 O THR E 261 10626 14748 10664 2518 -905 -751 A O ATOM 4969 CB THR E 261 9.443 -9.502 14.363 1.00 85.44 A C ANISOU 4969 CB THR E 261 9382 12637 10445 2371 -824 -808 A C ATOM 4970 CG2 THR E 261 10.441 -10.256 13.499 1.00 81.43 A C ANISOU 4970 CG2 THR E 261 8839 11795 10307 2326 -829 -636 A C ATOM 4971 OG1 THR E 261 8.115 -9.848 13.954 1.00 78.70 A O ANISOU 4971 OG1 THR E 261 8535 11577 9792 2368 -687 -1185 A O ATOM 4972 N ASP E 262 8.158 -9.321 17.733 1.00 97.78 A N ANISOU 4972 N ASP E 262 10879 15210 11063 2531 -1249 -1244 A N ATOM 4973 CA ASP E 262 7.423 -8.447 18.649 1.00 97.80 A C ANISOU 4973 CA ASP E 262 10968 15617 10576 2654 -1204 -1422 A C ATOM 4974 C ASP E 262 6.431 -7.566 17.883 1.00 89.69 A C ANISOU 4974 C ASP E 262 10060 14410 9609 2756 -887 -1605 A C ATOM 4975 O ASP E 262 6.532 -6.338 17.853 1.00103.61 A O ANISOU 4975 O ASP E 262 11856 16411 11100 2846 -704 -1417 A O ATOM 4976 CB ASP E 262 8.394 -7.609 19.495 1.00105.80 A C ANISOU 4976 CB ASP E 262 11950 17153 11095 2667 -1278 -1028 A C ATOM 4977 CG ASP E 262 7.683 -6.675 20.459 1.00121.78 A C ANISOU 4977 CG ASP E 262 14034 19675 12562 2826 -1184 -1203 A C ATOM 4978 OD1 ASP E 262 6.586 -7.029 20.941 1.00122.82 A O ANISOU 4978 OD1 ASP E 262 14244 19804 12618 2922 -1216 -1678 A O ATOM 4979 OD2 ASP E 262 8.225 -5.583 20.732 1.00129.76 A O1- ANISOU 4979 OD2 ASP E 262 15014 21082 13208 2856 -1080 -866 A O1- ATOM 4980 N GLY E 263 5.467 -8.227 17.237 1.00 81.67 A N ANISOU 4980 N GLY E 263 9087 12965 8980 2727 -839 -1942 A N ATOM 4981 CA GLY E 263 4.384 -7.563 16.531 1.00 72.47 A C ANISOU 4981 CA GLY E 263 8046 11561 7929 2817 -594 -2148 A C ATOM 4982 C GLY E 263 4.381 -7.804 15.034 1.00 79.29 A C ANISOU 4982 C GLY E 263 8915 11932 9278 2686 -428 -2039 A C ATOM 4983 O GLY E 263 3.316 -7.760 14.408 1.00 74.91 A O ANISOU 4983 O GLY E 263 8452 11061 8950 2695 -309 -2272 A O ATOM 4984 N GLY E 264 5.548 -8.047 14.446 1.00 79.08 A N ANISOU 4984 N GLY E 264 8815 11829 9403 2568 -425 -1692 A N ATOM 4985 CA GLY E 264 5.627 -8.220 13.006 1.00 78.04 A C ANISOU 4985 CA GLY E 264 8714 11276 9661 2452 -244 -1586 A C ATOM 4986 C GLY E 264 6.880 -7.626 12.402 1.00 77.32 A C ANISOU 4986 C GLY E 264 8651 11203 9523 2398 -169 -1158 A C ATOM 4987 O GLY E 264 7.566 -6.821 13.036 1.00 76.35 A O ANISOU 4987 O GLY E 264 8527 11424 9057 2444 -231 -905 A O ATOM 4988 N VAL E 265 7.196 -8.018 11.164 1.00 69.99 A N ANISOU 4988 N VAL E 265 7759 9910 8924 2283 -44 -1068 A N ATOM 4989 CA VAL E 265 8.390 -7.510 10.504 1.00 74.36 A C ANISOU 4989 CA VAL E 265 8397 10409 9449 2215 1 -698 A C ATOM 4990 C VAL E 265 8.149 -6.081 10.026 1.00 77.38 A C ANISOU 4990 C VAL E 265 8905 10855 9643 2204 157 -513 A C ATOM 4991 O VAL E 265 7.013 -5.619 9.888 1.00 68.66 A O ANISOU 4991 O VAL E 265 7825 9727 8535 2259 281 -688 A O ATOM 4992 CB VAL E 265 8.811 -8.424 9.342 1.00 63.69 A C ANISOU 4992 CB VAL E 265 7065 8663 8470 2121 98 -703 A C ATOM 4993 CG1 VAL E 265 9.615 -9.607 9.857 1.00 83.56 A C ANISOU 4993 CG1 VAL E 265 9430 11187 11131 2162 -91 -714 A C ATOM 4994 CG2 VAL E 265 7.592 -8.897 8.565 1.00 73.07 A C ANISOU 4994 CG2 VAL E 265 8249 9586 9929 2062 276 -978 A C ATOM 4995 N ASP E 266 9.249 -5.369 9.772 1.00 76.37 A N ANISOU 4995 N ASP E 266 8852 10792 9372 2128 125 -135 A N ATOM 4996 CA ASP E 266 9.135 -4.022 9.223 1.00 68.21 A C ANISOU 4996 CA ASP E 266 7910 9822 8186 2079 247 105 A C ATOM 4997 C ASP E 266 8.727 -4.062 7.756 1.00 71.91 A C ANISOU 4997 C ASP E 266 8520 9879 8922 1966 433 62 A C ATOM 4998 O ASP E 266 7.888 -3.268 7.317 1.00 72.71 A O ANISOU 4998 O ASP E 266 8654 9967 9005 1975 564 64 A O ATOM 4999 CB ASP E 266 10.453 -3.268 9.393 1.00 64.49 A C ANISOU 4999 CB ASP E 266 7480 9537 7487 1975 110 555 A C ATOM 5000 CG ASP E 266 10.829 -3.075 10.848 1.00 68.09 A C ANISOU 5000 CG ASP E 266 7789 10464 7620 2057 -67 667 A C ATOM 5001 OD1 ASP E 266 9.994 -2.554 11.616 1.00 82.91 A O ANISOU 5001 OD1 ASP E 266 9551 12685 9266 2199 -3 542 A O ATOM 5002 OD2 ASP E 266 11.958 -3.450 11.226 1.00 75.70 A O1- ANISOU 5002 OD2 ASP E 266 8761 11451 8550 1987 -273 876 A O1- ATOM 5003 N ARG E 267 9.307 -4.980 6.985 1.00 65.27 A N ANISOU 5003 N ARG E 267 7761 8716 8323 1872 449 28 A N ATOM 5004 CA ARG E 267 8.986 -5.126 5.574 1.00 63.35 A C ANISOU 5004 CA ARG E 267 7662 8113 8293 1747 637 -14 A C ATOM 5005 C ARG E 267 8.795 -6.599 5.250 1.00 70.26 A C ANISOU 5005 C ARG E 267 8469 8751 9476 1754 704 -299 A C ATOM 5006 O ARG E 267 9.365 -7.474 5.905 1.00 67.49 A O ANISOU 5006 O ARG E 267 7996 8455 9191 1835 579 -373 A O ATOM 5007 CB ARG E 267 10.087 -4.548 4.674 1.00 57.09 A C ANISOU 5007 CB ARG E 267 7088 7178 7426 1591 629 304 A C ATOM 5008 CG ARG E 267 10.413 -3.090 4.931 1.00 72.62 A C ANISOU 5008 CG ARG E 267 9092 9397 9103 1531 535 662 A C ATOM 5009 CD ARG E 267 9.251 -2.187 4.575 1.00 64.17 A C ANISOU 5009 CD ARG E 267 7997 8386 7998 1532 669 670 A C ATOM 5010 NE ARG E 267 9.641 -0.784 4.607 1.00 67.34 A N ANISOU 5010 NE ARG E 267 8409 9023 8155 1450 595 1065 A N ATOM 5011 CZ ARG E 267 9.439 0.025 5.637 1.00 74.19 A C ANISOU 5011 CZ ARG E 267 9083 10312 8795 1575 545 1186 A C ATOM 5012 NH1 ARG E 267 8.831 -0.394 6.736 1.00 75.70 A N1+ ANISOU 5012 NH1 ARG E 267 9101 10720 8941 1795 554 913 A N1+ ATOM 5013 NH2 ARG E 267 9.857 1.285 5.565 1.00 69.89 A N ANISOU 5013 NH2 ARG E 267 8513 9997 8045 1469 484 1596 A N ATOM 5014 N SER E 268 7.985 -6.866 4.229 1.00 65.61 A N ANISOU 5014 N SER E 268 7936 7916 9078 1659 895 -426 A N ATOM 5015 CA SER E 268 7.861 -8.224 3.716 1.00 64.21 A C ANISOU 5015 CA SER E 268 7674 7534 9190 1627 1001 -636 A C ATOM 5016 C SER E 268 7.784 -8.188 2.198 1.00 62.99 A C ANISOU 5016 C SER E 268 7700 7117 9119 1463 1227 -576 A C ATOM 5017 O SER E 268 7.355 -7.196 1.609 1.00 68.33 A O ANISOU 5017 O SER E 268 8534 7746 9683 1361 1286 -435 A O ATOM 5018 CB SER E 268 6.639 -8.954 4.289 1.00 60.43 A C ANISOU 5018 CB SER E 268 6997 7077 8886 1657 975 -924 A C ATOM 5019 OG SER E 268 5.444 -8.525 3.665 1.00 78.67 A O ANISOU 5019 OG SER E 268 9386 9242 11262 1557 1094 -976 A O ATOM 5020 N VAL E 269 8.222 -9.280 1.571 1.00 63.45 A N ANISOU 5020 N VAL E 269 7721 7027 9359 1447 1354 -675 A N ATOM 5021 CA VAL E 269 8.216 -9.417 0.116 1.00 67.02 A C ANISOU 5021 CA VAL E 269 8344 7267 9856 1295 1598 -647 A C ATOM 5022 C VAL E 269 7.751 -10.825 -0.232 1.00 76.28 A C ANISOU 5022 C VAL E 269 9294 8379 11309 1278 1768 -860 A C ATOM 5023 O VAL E 269 8.389 -11.808 0.164 1.00 77.13 A O ANISOU 5023 O VAL E 269 9217 8532 11557 1419 1745 -963 A O ATOM 5024 CB VAL E 269 9.596 -9.146 -0.512 1.00 80.54 A C ANISOU 5024 CB VAL E 269 10310 8871 11422 1300 1616 -500 A C ATOM 5025 CG1 VAL E 269 9.521 -9.298 -2.023 1.00 61.42 A C ANISOU 5025 CG1 VAL E 269 8090 6257 8989 1140 1880 -506 A C ATOM 5026 CG2 VAL E 269 10.101 -7.758 -0.146 1.00 67.59 A C ANISOU 5026 CG2 VAL E 269 8857 7312 9513 1268 1414 -235 A C ATOM 5027 N GLU E 270 6.659 -10.922 -0.988 1.00 68.64 A N ANISOU 5027 N GLU E 270 8329 7317 10435 1097 1927 -893 A N ATOM 5028 CA GLU E 270 6.085 -12.196 -1.404 1.00 70.72 A C ANISOU 5028 CA GLU E 270 8359 7549 10960 1015 2097 -1041 A C ATOM 5029 C GLU E 270 6.560 -12.522 -2.816 1.00 61.46 A C ANISOU 5029 C GLU E 270 7326 6283 9743 918 2399 -993 A C ATOM 5030 O GLU E 270 6.269 -11.778 -3.758 1.00 68.34 A O ANISOU 5030 O GLU E 270 8458 7052 10456 741 2504 -859 A O ATOM 5031 CB GLU E 270 4.557 -12.140 -1.349 1.00 71.28 A C ANISOU 5031 CB GLU E 270 8355 7561 11166 845 2059 -1086 A C ATOM 5032 CG GLU E 270 3.888 -13.483 -1.118 1.00 72.38 A C ANISOU 5032 CG GLU E 270 8160 7728 11612 773 2076 -1246 A C ATOM 5033 CD GLU E 270 4.090 -14.444 -2.273 1.00 73.36 A C ANISOU 5033 CD GLU E 270 8179 7845 11848 652 2386 -1223 A C ATOM 5034 OE1 GLU E 270 3.607 -14.148 -3.386 1.00 85.66 A O ANISOU 5034 OE1 GLU E 270 9904 9298 13345 441 2574 -1107 A O ATOM 5035 OE2 GLU E 270 4.742 -15.489 -2.070 1.00 70.02 A O1- ANISOU 5035 OE2 GLU E 270 7497 7542 11565 778 2447 -1310 A O1- ATOM 5036 N CYS E 271 7.269 -13.644 -2.964 1.00 73.06 A N ANISOU 5036 N CYS E 271 8616 7800 11344 1044 2540 -1105 A N ATOM 5037 CA CYS E 271 7.881 -14.006 -4.236 1.00 77.71 A C ANISOU 5037 CA CYS E 271 9347 8330 11850 1021 2852 -1108 A C ATOM 5038 C CYS E 271 7.419 -15.343 -4.800 1.00 72.64 A C ANISOU 5038 C CYS E 271 8384 7783 11432 960 3133 -1211 A C ATOM 5039 O CYS E 271 7.862 -15.717 -5.893 1.00 73.32 A O ANISOU 5039 O CYS E 271 8566 7868 11426 953 3443 -1235 A O ATOM 5040 CB CYS E 271 9.411 -14.025 -4.103 1.00 66.58 A C ANISOU 5040 CB CYS E 271 8078 6871 10348 1283 2812 -1142 A C ATOM 5041 SG CYS E 271 10.136 -12.474 -3.531 1.00 72.85 A S ANISOU 5041 SG CYS E 271 9241 7577 10861 1309 2482 -956 A S ATOM 5042 N THR E 272 6.551 -16.080 -4.103 1.00 74.10 A N ANISOU 5042 N THR E 272 8194 8069 11893 904 3036 -1268 A N ATOM 5043 CA THR E 272 6.078 -17.346 -4.654 1.00 78.56 A C ANISOU 5043 CA THR E 272 8408 8759 12682 799 3294 -1313 A C ATOM 5044 C THR E 272 4.935 -17.139 -5.638 1.00 77.67 A C ANISOU 5044 C THR E 272 8391 8596 12525 437 3458 -1188 A C ATOM 5045 O THR E 272 4.888 -17.793 -6.686 1.00 75.56 A O ANISOU 5045 O THR E 272 8037 8424 12247 322 3798 -1158 A O ATOM 5046 CB THR E 272 5.633 -18.289 -3.536 1.00 74.68 A C ANISOU 5046 CB THR E 272 7461 8393 12520 838 3085 -1396 A C ATOM 5047 CG2 THR E 272 6.658 -18.321 -2.424 1.00 68.28 A C ANISOU 5047 CG2 THR E 272 6590 7623 11730 1164 2839 -1473 A C ATOM 5048 OG1 THR E 272 4.375 -17.848 -3.009 1.00 73.57 A O ANISOU 5048 OG1 THR E 272 7342 8171 12442 610 2839 -1368 A O ATOM 5049 N GLY E 273 4.007 -16.241 -5.320 1.00 87.58 A N ANISOU 5049 N GLY E 273 9819 9711 13748 266 3225 -1107 A N ATOM 5050 CA GLY E 273 2.817 -16.046 -6.116 1.00 80.39 A C ANISOU 5050 CA GLY E 273 8986 8708 12851 -80 3304 -964 A C ATOM 5051 C GLY E 273 1.570 -16.684 -5.546 1.00 84.06 A C ANISOU 5051 C GLY E 273 9152 9149 13637 -273 3132 -984 A C ATOM 5052 O GLY E 273 0.479 -16.458 -6.081 1.00 90.65 A O ANISOU 5052 O GLY E 273 10071 9850 14522 -571 3122 -849 A O ATOM 5053 N SER E 274 1.697 -17.475 -4.485 1.00 87.63 A N ANISOU 5053 N SER E 274 9274 9708 14312 -130 2964 -1133 A N ATOM 5054 CA SER E 274 0.526 -18.043 -3.835 1.00 87.62 A C ANISOU 5054 CA SER E 274 9027 9656 14607 -329 2729 -1171 A C ATOM 5055 C SER E 274 -0.308 -16.928 -3.215 1.00 90.14 A C ANISOU 5055 C SER E 274 9640 9735 14875 -353 2414 -1202 A C ATOM 5056 O SER E 274 0.209 -16.096 -2.464 1.00 80.69 A O ANISOU 5056 O SER E 274 8624 8534 13502 -94 2251 -1285 A O ATOM 5057 CB SER E 274 0.949 -19.057 -2.772 1.00 82.55 A C ANISOU 5057 CB SER E 274 7992 9195 14176 -159 2575 -1321 A C ATOM 5058 OG SER E 274 -0.127 -19.384 -1.911 1.00 86.27 A O ANISOU 5058 OG SER E 274 8317 9581 14881 -330 2244 -1396 A O ATOM 5059 N VAL E 275 -1.600 -16.896 -3.554 1.00 82.22 A N ANISOU 5059 N VAL E 275 8681 8534 14024 -659 2333 -1119 A N ATOM 5060 CA VAL E 275 -2.487 -15.875 -3.002 1.00 86.56 A C ANISOU 5060 CA VAL E 275 9504 8823 14562 -647 2041 -1169 A C ATOM 5061 C VAL E 275 -2.542 -15.986 -1.486 1.00 82.02 A C ANISOU 5061 C VAL E 275 8832 8277 14055 -440 1713 -1425 A C ATOM 5062 O VAL E 275 -2.561 -14.975 -0.767 1.00 86.50 A O ANISOU 5062 O VAL E 275 9624 8784 14459 -218 1536 -1526 A O ATOM 5063 CB VAL E 275 -3.888 -15.989 -3.630 1.00 95.22 A C ANISOU 5063 CB VAL E 275 10652 9656 15872 -1021 1980 -1034 A C ATOM 5064 CG1 VAL E 275 -4.793 -14.885 -3.107 1.00 82.30 A C ANISOU 5064 CG1 VAL E 275 9320 7713 14239 -947 1689 -1103 A C ATOM 5065 CG2 VAL E 275 -3.787 -15.936 -5.144 1.00102.71 A C ANISOU 5065 CG2 VAL E 275 11687 10632 16705 -1250 2314 -756 A C ATOM 5066 N GLN E 276 -2.566 -17.217 -0.972 1.00 83.95 A N ANISOU 5066 N GLN E 276 8726 8649 14524 -516 1625 -1521 A N ATOM 5067 CA GLN E 276 -2.410 -17.399 0.462 1.00 84.35 A C ANISOU 5067 CA GLN E 276 8676 8788 14584 -316 1317 -1753 A C ATOM 5068 C GLN E 276 -1.110 -16.765 0.939 1.00 82.19 A C ANISOU 5068 C GLN E 276 8497 8715 14017 50 1363 -1785 A C ATOM 5069 O GLN E 276 -1.095 -16.067 1.959 1.00 81.56 A O ANISOU 5069 O GLN E 276 8566 8649 13775 254 1136 -1925 A O ATOM 5070 CB GLN E 276 -2.456 -18.886 0.821 1.00 87.99 A C ANISOU 5070 CB GLN E 276 8699 9402 15330 -467 1229 -1794 A C ATOM 5071 CG GLN E 276 -3.842 -19.400 1.234 1.00106.24 A C ANISOU 5071 CG GLN E 276 10951 11499 17919 -779 914 -1879 A C ATOM 5072 CD GLN E 276 -4.507 -18.580 2.337 1.00117.86 A C ANISOU 5072 CD GLN E 276 12732 12766 19283 -645 552 -2132 A C ATOM 5073 NE2 GLN E 276 -3.705 -18.041 3.250 1.00110.17 A N ANISOU 5073 NE2 GLN E 276 11842 11973 18044 -295 473 -2274 A N ATOM 5074 OE1 GLN E 276 -5.733 -18.461 2.380 1.00122.40 A O ANISOU 5074 OE1 GLN E 276 13469 13026 20012 -854 340 -2198 A O ATOM 5075 N ALA E 277 -0.015 -16.974 0.199 1.00 84.24 A N ANISOU 5075 N ALA E 277 8688 9126 14192 135 1654 -1654 A N ATOM 5076 CA ALA E 277 1.262 -16.379 0.587 1.00 76.48 A C ANISOU 5076 CA ALA E 277 7821 8285 12952 449 1669 -1652 A C ATOM 5077 C ALA E 277 1.184 -14.862 0.615 1.00 73.88 A C ANISOU 5077 C ALA E 277 7873 7853 12346 543 1621 -1601 A C ATOM 5078 O ALA E 277 1.798 -14.219 1.471 1.00 74.38 A O ANISOU 5078 O ALA E 277 8026 8029 12206 773 1473 -1636 A O ATOM 5079 CB ALA E 277 2.375 -16.847 -0.353 1.00 61.00 A C ANISOU 5079 CB ALA E 277 5783 6431 10962 514 1991 -1540 A C ATOM 5080 N MET E 278 0.424 -14.275 -0.306 1.00 77.62 A N ANISOU 5080 N MET E 278 8555 8949 11989 801 2133 -488 A N ATOM 5081 CA MET E 278 0.246 -12.828 -0.310 1.00 79.20 A C ANISOU 5081 CA MET E 278 9114 9199 11780 730 1912 -657 A C ATOM 5082 C MET E 278 -0.497 -12.368 0.937 1.00 73.53 A C ANISOU 5082 C MET E 278 8110 8807 11022 588 1493 -896 A C ATOM 5083 O MET E 278 -0.111 -11.380 1.579 1.00 73.54 A O ANISOU 5083 O MET E 278 8212 9021 10708 582 1244 -971 A O ATOM 5084 CB MET E 278 -0.509 -12.407 -1.567 1.00 71.04 A C ANISOU 5084 CB MET E 278 8468 7837 10686 697 2134 -685 A C ATOM 5085 CG MET E 278 0.228 -12.762 -2.829 1.00 66.22 A C ANISOU 5085 CG MET E 278 8239 6916 10006 828 2559 -487 A C ATOM 5086 SD MET E 278 -0.859 -12.754 -4.255 1.00 79.53 A S ANISOU 5086 SD MET E 278 10276 8238 11703 807 2882 -451 A S ATOM 5087 CE MET E 278 0.302 -12.226 -5.497 1.00 88.43 A C ANISOU 5087 CE MET E 278 12086 9158 12354 915 3125 -345 A C ATOM 5088 N ILE E 279 -1.570 -13.078 1.296 1.00 69.02 A N ANISOU 5088 N ILE E 279 7186 8261 10779 462 1440 -1031 A N ATOM 5089 CA ILE E 279 -2.317 -12.732 2.505 1.00 71.49 A C ANISOU 5089 CA ILE E 279 7251 8866 11044 307 1069 -1313 A C ATOM 5090 C ILE E 279 -1.411 -12.812 3.730 1.00 75.19 A C ANISOU 5090 C ILE E 279 7501 9759 11310 357 776 -1270 A C ATOM 5091 O ILE E 279 -1.388 -11.903 4.573 1.00 82.68 A O ANISOU 5091 O ILE E 279 8517 10957 11939 322 521 -1419 A O ATOM 5092 CB ILE E 279 -3.552 -13.639 2.654 1.00 79.68 A C ANISOU 5092 CB ILE E 279 7932 9822 12519 130 1080 -1486 A C ATOM 5093 CG1 ILE E 279 -4.541 -13.387 1.514 1.00 76.85 A C ANISOU 5093 CG1 ILE E 279 7827 9036 12337 92 1380 -1510 A C ATOM 5094 CG2 ILE E 279 -4.220 -13.416 4.002 1.00 64.33 A C ANISOU 5094 CG2 ILE E 279 5738 8202 10500 -48 692 -1823 A C ATOM 5095 CD1 ILE E 279 -5.639 -14.423 1.423 1.00 66.32 A C ANISOU 5095 CD1 ILE E 279 6154 7513 11532 -72 1513 -1608 A C ATOM 5096 N GLN E 280 -0.636 -13.898 3.838 1.00 78.40 A N ANISOU 5096 N GLN E 280 7639 10244 11907 461 838 -1028 A N ATOM 5097 CA GLN E 280 0.244 -14.069 4.994 1.00 77.33 A C ANISOU 5097 CA GLN E 280 7273 10518 11589 541 562 -911 A C ATOM 5098 C GLN E 280 1.341 -13.009 5.026 1.00 77.89 A C ANISOU 5098 C GLN E 280 7709 10619 11265 683 586 -776 A C ATOM 5099 O GLN E 280 1.682 -12.497 6.099 1.00 65.60 A O ANISOU 5099 O GLN E 280 6108 9407 9411 690 316 -803 A O ATOM 5100 CB GLN E 280 0.850 -15.479 5.022 1.00 80.23 A C ANISOU 5100 CB GLN E 280 7237 10933 12313 659 647 -616 A C ATOM 5101 CG GLN E 280 -0.142 -16.613 4.743 1.00 84.82 A C ANISOU 5101 CG GLN E 280 7433 11394 13399 517 713 -697 A C ATOM 5102 CD GLN E 280 0.511 -17.885 4.187 1.00 90.04 A C ANISOU 5102 CD GLN E 280 7804 11897 14509 685 1017 -336 A C ATOM 5103 NE2 GLN E 280 0.777 -18.840 5.062 1.00 82.79 A N ANISOU 5103 NE2 GLN E 280 6340 11317 13800 705 752 -191 A N ATOM 5104 OE1 GLN E 280 0.717 -18.023 2.999 1.00 86.32 A O ANISOU 5104 OE1 GLN E 280 7585 11016 14197 794 1482 -191 A O ATOM 5105 N ALA E 281 1.896 -12.655 3.864 1.00 75.21 A N ANISOU 5105 N ALA E 281 7747 9920 10910 780 914 -642 A N ATOM 5106 CA ALA E 281 2.959 -11.657 3.826 1.00 71.29 A C ANISOU 5106 CA ALA E 281 7588 9406 10094 872 943 -537 A C ATOM 5107 C ALA E 281 2.438 -10.268 4.162 1.00 75.64 A C ANISOU 5107 C ALA E 281 8338 10060 10342 750 732 -775 A C ATOM 5108 O ALA E 281 3.172 -9.459 4.743 1.00 68.11 A O ANISOU 5108 O ALA E 281 7485 9263 9132 788 626 -722 A O ATOM 5109 CB ALA E 281 3.631 -11.656 2.454 1.00 71.50 A C ANISOU 5109 CB ALA E 281 7993 9011 10164 965 1331 -393 A C ATOM 5110 N PHE E 282 1.187 -9.965 3.807 1.00 79.45 A N ANISOU 5110 N PHE E 282 8865 10433 10890 616 703 -1012 A N ATOM 5111 CA PHE E 282 0.614 -8.697 4.243 1.00 69.42 A C ANISOU 5111 CA PHE E 282 7709 9269 9397 524 517 -1226 A C ATOM 5112 C PHE E 282 0.341 -8.706 5.741 1.00 67.51 A C ANISOU 5112 C PHE E 282 7185 9433 9031 471 241 -1375 A C ATOM 5113 O PHE E 282 0.608 -7.716 6.432 1.00 71.30 A O ANISOU 5113 O PHE E 282 7748 10101 9243 477 122 -1420 A O ATOM 5114 CB PHE E 282 -0.674 -8.385 3.485 1.00 66.04 A C ANISOU 5114 CB PHE E 282 7391 8590 9109 426 587 -1404 A C ATOM 5115 CG PHE E 282 -1.456 -7.252 4.089 1.00 71.81 A C ANISOU 5115 CG PHE E 282 8140 9433 9713 347 416 -1634 A C ATOM 5116 CD1 PHE E 282 -0.919 -5.976 4.142 1.00 68.09 A C ANISOU 5116 CD1 PHE E 282 7864 9009 8999 381 352 -1593 A C ATOM 5117 CD2 PHE E 282 -2.712 -7.468 4.632 1.00 66.56 A C ANISOU 5117 CD2 PHE E 282 7279 8805 9207 233 343 -1899 A C ATOM 5118 CE1 PHE E 282 -1.627 -4.933 4.708 1.00 78.89 A C ANISOU 5118 CE1 PHE E 282 9213 10464 10296 334 244 -1779 A C ATOM 5119 CE2 PHE E 282 -3.426 -6.427 5.200 1.00 69.65 A C ANISOU 5119 CE2 PHE E 282 7698 9260 9505 183 248 -2117 A C ATOM 5120 CZ PHE E 282 -2.881 -5.159 5.239 1.00 74.98 A C ANISOU 5120 CZ PHE E 282 8550 9990 9949 250 211 -2041 A C ATOM 5121 N GLU E 283 -0.186 -9.816 6.263 1.00 69.34 A N ANISOU 5121 N GLU E 283 7085 9814 9447 409 138 -1456 A N ATOM 5122 CA GLU E 283 -0.585 -9.848 7.665 1.00 72.13 A C ANISOU 5122 CA GLU E 283 7210 10571 9626 323 -158 -1659 A C ATOM 5123 C GLU E 283 0.600 -9.959 8.617 1.00 72.59 A C ANISOU 5123 C GLU E 283 7175 10995 9411 453 -305 -1424 A C ATOM 5124 O GLU E 283 0.449 -9.654 9.805 1.00 63.82 A O ANISOU 5124 O GLU E 283 5992 10250 8006 410 -534 -1562 A O ATOM 5125 CB GLU E 283 -1.558 -11.003 7.905 1.00 69.54 A C ANISOU 5125 CB GLU E 283 6542 10290 9591 169 -268 -1852 A C ATOM 5126 CG GLU E 283 -2.991 -10.686 7.506 1.00 75.45 A C ANISOU 5126 CG GLU E 283 7359 10769 10541 -1 -188 -2185 A C ATOM 5127 CD GLU E 283 -3.908 -11.889 7.606 1.00 88.20 A C ANISOU 5127 CD GLU E 283 8628 12350 12535 -182 -250 -2365 A C ATOM 5128 OE1 GLU E 283 -3.673 -12.751 8.478 1.00 91.75 A O ANISOU 5128 OE1 GLU E 283 8746 13146 12969 -237 -509 -2373 A O ATOM 5129 OE2 GLU E 283 -4.871 -11.967 6.813 1.00 92.03 A O1- ANISOU 5129 OE2 GLU E 283 9158 12462 13348 -275 -46 -2482 A O1- ATOM 5130 N CYS E 284 1.771 -10.373 8.135 1.00 62.26 A N ANISOU 5130 N CYS E 284 5890 9583 8182 622 -149 -1065 A N ATOM 5131 CA CYS E 284 2.904 -10.615 9.020 1.00 72.78 A C ANISOU 5131 CA CYS E 284 7101 11230 9322 776 -259 -775 A C ATOM 5132 C CYS E 284 3.739 -9.370 9.298 1.00 68.63 A C ANISOU 5132 C CYS E 284 6864 10731 8483 856 -195 -665 A C ATOM 5133 O CYS E 284 4.627 -9.426 10.155 1.00 78.66 A O ANISOU 5133 O CYS E 284 8060 12274 9555 985 -273 -417 A O ATOM 5134 CB CYS E 284 3.802 -11.716 8.444 1.00 78.96 A C ANISOU 5134 CB CYS E 284 7737 11858 10407 945 -76 -413 A C ATOM 5135 SG CYS E 284 4.931 -11.179 7.140 1.00 72.32 A S ANISOU 5135 SG CYS E 284 7312 10520 9645 1084 353 -182 A S ATOM 5136 N VAL E 285 3.486 -8.256 8.613 1.00 68.76 A N ANISOU 5136 N VAL E 285 7180 10479 8468 784 -58 -813 A N ATOM 5137 CA VAL E 285 4.221 -7.027 8.893 1.00 74.58 A C ANISOU 5137 CA VAL E 285 8135 11235 8967 825 -5 -724 A C ATOM 5138 C VAL E 285 3.621 -6.343 10.115 1.00 72.92 A C ANISOU 5138 C VAL E 285 7868 11379 8460 760 -190 -927 A C ATOM 5139 O VAL E 285 2.436 -6.505 10.432 1.00 63.53 A O ANISOU 5139 O VAL E 285 6575 10297 7266 641 -323 -1238 A O ATOM 5140 CB VAL E 285 4.234 -6.089 7.668 1.00 66.89 A C ANISOU 5140 CB VAL E 285 7467 9860 8089 763 172 -783 A C ATOM 5141 CG1 VAL E 285 4.622 -6.854 6.414 1.00 66.72 A C ANISOU 5141 CG1 VAL E 285 7552 9487 8311 808 376 -654 A C ATOM 5142 CG2 VAL E 285 2.885 -5.410 7.489 1.00 60.80 A C ANISOU 5142 CG2 VAL E 285 6730 9040 7330 626 96 -1107 A C ATOM 5143 N HIS E 286 4.455 -5.581 10.816 1.00 68.02 A N ANISOU 5143 N HIS E 286 7331 10917 7598 838 -158 -755 A N ATOM 5144 CA HIS E 286 4.020 -4.869 12.009 1.00 67.13 A C ANISOU 5144 CA HIS E 286 7209 11139 7160 805 -259 -913 A C ATOM 5145 C HIS E 286 2.979 -3.813 11.654 1.00 73.50 A C ANISOU 5145 C HIS E 286 8129 11767 8030 677 -202 -1242 A C ATOM 5146 O HIS E 286 3.021 -3.203 10.584 1.00 72.35 A O ANISOU 5146 O HIS E 286 8116 11271 8102 644 -78 -1228 A O ATOM 5147 CB HIS E 286 5.221 -4.209 12.691 1.00 63.99 A C ANISOU 5147 CB HIS E 286 6895 10879 6541 930 -154 -598 A C ATOM 5148 CG HIS E 286 5.037 -3.970 14.158 1.00 65.40 A C ANISOU 5148 CG HIS E 286 7034 11518 6299 961 -259 -643 A C ATOM 5149 CD2 HIS E 286 5.651 -4.520 15.232 1.00 80.31 A C ANISOU 5149 CD2 HIS E 286 8838 13801 7874 1089 -370 -392 A C ATOM 5150 ND1 HIS E 286 4.135 -3.057 14.660 1.00 70.89 A N ANISOU 5150 ND1 HIS E 286 7804 12306 6826 868 -236 -962 A N ATOM 5151 CE1 HIS E 286 4.198 -3.058 15.980 1.00 76.15 A C ANISOU 5151 CE1 HIS E 286 8467 13405 7060 924 -309 -942 A C ATOM 5152 NE2 HIS E 286 5.110 -3.938 16.352 1.00 80.79 A N ANISOU 5152 NE2 HIS E 286 8962 14205 7531 1057 -416 -587 A N ATOM 5153 N ASP E 287 2.031 -3.603 12.563 1.00 70.87 A N ANISOU 5153 N ASP E 287 7749 11679 7501 609 -295 -1537 A N ATOM 5154 CA ASP E 287 1.086 -2.517 12.370 1.00 67.17 A C ANISOU 5154 CA ASP E 287 7369 11040 7113 530 -193 -1811 A C ATOM 5155 C ASP E 287 1.766 -1.175 12.637 1.00 78.81 A C ANISOU 5155 C ASP E 287 8947 12514 8482 594 -29 -1648 A C ATOM 5156 O ASP E 287 2.822 -1.096 13.273 1.00 83.06 A O ANISOU 5156 O ASP E 287 9501 13248 8809 686 9 -1380 A O ATOM 5157 CB ASP E 287 -0.144 -2.690 13.267 1.00 63.57 A C ANISOU 5157 CB ASP E 287 6857 10792 6505 435 -283 -2213 A C ATOM 5158 CG ASP E 287 0.204 -2.809 14.743 1.00 77.59 A C ANISOU 5158 CG ASP E 287 8626 13047 7807 478 -375 -2212 A C ATOM 5159 OD1 ASP E 287 1.380 -2.625 15.112 1.00 82.05 A O ANISOU 5159 OD1 ASP E 287 9224 13774 8179 605 -335 -1861 A O ATOM 5160 OD2 ASP E 287 -0.716 -3.087 15.542 1.00 77.19 A O1- ANISOU 5160 OD2 ASP E 287 8560 13206 7564 378 -480 -2570 A O1- ATOM 5161 N GLY E 288 1.152 -0.113 12.130 1.00 72.15 A N ANISOU 5161 N GLY E 288 8151 11435 7830 550 81 -1782 A N ATOM 5162 CA GLY E 288 1.662 1.238 12.286 1.00 70.23 A C ANISOU 5162 CA GLY E 288 7942 11155 7588 585 240 -1644 A C ATOM 5163 C GLY E 288 2.703 1.694 11.280 1.00 71.45 A C ANISOU 5163 C GLY E 288 8153 11048 7948 575 276 -1359 A C ATOM 5164 O GLY E 288 2.739 2.874 10.925 1.00 74.14 A O ANISOU 5164 O GLY E 288 8481 11235 8453 543 353 -1321 A O ATOM 5165 N TRP E 289 3.554 0.781 10.808 1.00 71.55 A N ANISOU 5165 N TRP E 289 8217 10997 7970 595 224 -1166 A N ATOM 5166 CA TRP E 289 4.637 1.179 9.916 1.00 72.90 A C ANISOU 5166 CA TRP E 289 8491 10905 8301 567 283 -935 A C ATOM 5167 C TRP E 289 5.023 0.090 8.921 1.00 72.24 A C ANISOU 5167 C TRP E 289 8507 10616 8326 570 249 -858 A C ATOM 5168 O TRP E 289 5.799 0.346 7.994 1.00 75.67 A O ANISOU 5168 O TRP E 289 9084 10779 8886 522 302 -739 A O ATOM 5169 CB TRP E 289 5.866 1.593 10.733 1.00 78.14 A C ANISOU 5169 CB TRP E 289 9152 11695 8842 626 416 -663 A C ATOM 5170 CG TRP E 289 6.469 0.479 11.544 1.00 82.33 A C ANISOU 5170 CG TRP E 289 9656 12468 9158 756 413 -480 A C ATOM 5171 CD1 TRP E 289 7.237 -0.550 11.080 1.00 76.27 A C ANISOU 5171 CD1 TRP E 289 8927 11586 8465 819 415 -288 A C ATOM 5172 CD2 TRP E 289 6.360 0.291 12.960 1.00 78.17 A C ANISOU 5172 CD2 TRP E 289 9052 12351 8299 853 406 -447 A C ATOM 5173 CE2 TRP E 289 7.082 -0.876 13.282 1.00 72.94 A C ANISOU 5173 CE2 TRP E 289 8355 11831 7528 974 352 -201 A C ATOM 5174 CE3 TRP E 289 5.721 0.993 13.987 1.00 79.23 A C ANISOU 5174 CE3 TRP E 289 9157 12748 8200 858 454 -598 A C ATOM 5175 NE1 TRP E 289 7.607 -1.370 12.117 1.00 69.49 A N ANISOU 5175 NE1 TRP E 289 7973 11048 7381 960 382 -104 A N ATOM 5176 CZ2 TRP E 289 7.184 -1.355 14.586 1.00 79.00 A C ANISOU 5176 CZ2 TRP E 289 9054 13033 7929 1091 282 -86 A C ATOM 5177 CZ3 TRP E 289 5.822 0.515 15.281 1.00 85.36 A C ANISOU 5177 CZ3 TRP E 289 9918 13942 8574 963 422 -525 A C ATOM 5178 CH2 TRP E 289 6.549 -0.648 15.569 1.00 76.82 A C ANISOU 5178 CH2 TRP E 289 8797 13034 7357 1073 306 -262 A C ATOM 5179 N GLY E 290 4.500 -1.121 9.098 1.00 71.40 A N ANISOU 5179 N GLY E 290 8325 10624 8182 614 178 -938 A N ATOM 5180 CA GLY E 290 4.910 -2.227 8.251 1.00 59.06 A C ANISOU 5180 CA GLY E 290 6818 8871 6750 646 208 -830 A C ATOM 5181 C GLY E 290 4.414 -2.086 6.823 1.00 59.83 A C ANISOU 5181 C GLY E 290 7076 8626 7032 561 228 -939 A C ATOM 5182 O GLY E 290 3.322 -1.584 6.561 1.00 69.26 A O ANISOU 5182 O GLY E 290 8258 9775 8281 494 162 -1137 A O ATOM 5183 N VAL E 291 5.245 -2.537 5.884 1.00 63.06 A N ANISOU 5183 N VAL E 291 7656 8778 7526 578 344 -794 A N ATOM 5184 CA VAL E 291 4.935 -2.485 4.459 1.00 60.09 A C ANISOU 5184 CA VAL E 291 7501 8085 7246 508 383 -865 A C ATOM 5185 C VAL E 291 5.174 -3.864 3.855 1.00 66.35 A C ANISOU 5185 C VAL E 291 8344 8722 8143 587 541 -778 A C ATOM 5186 O VAL E 291 6.211 -4.493 4.105 1.00 71.47 A O ANISOU 5186 O VAL E 291 8979 9359 8817 684 670 -589 A O ATOM 5187 CB VAL E 291 5.771 -1.416 3.725 1.00 63.32 A C ANISOU 5187 CB VAL E 291 8151 8285 7625 413 396 -814 A C ATOM 5188 CG1 VAL E 291 5.384 -1.353 2.256 1.00 48.27 A C ANISOU 5188 CG1 VAL E 291 6509 6105 5728 338 392 -892 A C ATOM 5189 CG2 VAL E 291 5.592 -0.053 4.380 1.00 49.06 A C ANISOU 5189 CG2 VAL E 291 6220 6632 5787 344 268 -858 A C ATOM 5190 N ALA E 292 4.214 -4.331 3.060 1.00 56.58 A N ANISOU 5190 N ALA E 292 7152 7346 7001 561 567 -887 A N ATOM 5191 CA ALA E 292 4.287 -5.622 2.394 1.00 60.06 A C ANISOU 5191 CA ALA E 292 7624 7610 7585 633 767 -806 A C ATOM 5192 C ALA E 292 4.245 -5.408 0.890 1.00 54.49 A C ANISOU 5192 C ALA E 292 7292 6569 6843 587 903 -825 A C ATOM 5193 O ALA E 292 3.375 -4.691 0.387 1.00 63.70 A O ANISOU 5193 O ALA E 292 8559 7689 7957 507 789 -937 A O ATOM 5194 CB ALA E 292 3.136 -6.531 2.829 1.00 67.85 A C ANISOU 5194 CB ALA E 292 8313 8726 8739 636 719 -904 A C ATOM 5195 N VAL E 293 5.176 -6.037 0.180 1.00 55.36 A N ANISOU 5195 N VAL E 293 7618 6448 6971 651 1157 -704 A N ATOM 5196 CA VAL E 293 5.278 -5.953 -1.269 1.00 58.37 A C ANISOU 5196 CA VAL E 293 8423 6514 7243 612 1325 -727 A C ATOM 5197 C VAL E 293 4.926 -7.313 -1.851 1.00 63.75 A C ANISOU 5197 C VAL E 293 9093 7025 8104 717 1630 -653 A C ATOM 5198 O VAL E 293 5.401 -8.346 -1.365 1.00 64.68 A O ANISOU 5198 O VAL E 293 8982 7163 8433 839 1802 -522 A O ATOM 5199 CB VAL E 293 6.686 -5.512 -1.705 1.00 60.39 A C ANISOU 5199 CB VAL E 293 9009 6579 7359 580 1436 -692 A C ATOM 5200 CG1 VAL E 293 6.834 -5.604 -3.214 1.00 63.84 A C ANISOU 5200 CG1 VAL E 293 9935 6697 7626 539 1638 -745 A C ATOM 5201 CG2 VAL E 293 6.966 -4.102 -1.225 1.00 56.68 A C ANISOU 5201 CG2 VAL E 293 8524 6250 6761 445 1143 -760 A C ATOM 5202 N LEU E 294 4.069 -7.310 -2.865 1.00 72.99 A N ANISOU 5202 N LEU E 294 10480 8037 9217 681 1702 -703 A N ATOM 5203 CA LEU E 294 3.759 -8.491 -3.653 1.00 61.04 A C ANISOU 5203 CA LEU E 294 9037 6299 7857 771 2064 -617 A C ATOM 5204 C LEU E 294 4.467 -8.377 -4.994 1.00 69.73 A C ANISOU 5204 C LEU E 294 10706 7097 8692 775 2328 -604 A C ATOM 5205 O LEU E 294 4.512 -7.296 -5.590 1.00 68.49 A O ANISOU 5205 O LEU E 294 10893 6919 8210 662 2137 -696 A O ATOM 5206 CB LEU E 294 2.250 -8.636 -3.870 1.00 67.91 A C ANISOU 5206 CB LEU E 294 9779 7171 8852 734 2024 -658 A C ATOM 5207 CG LEU E 294 1.339 -8.496 -2.650 1.00 60.53 A C ANISOU 5207 CG LEU E 294 8374 6508 8116 677 1730 -763 A C ATOM 5208 CD1 LEU E 294 -0.111 -8.729 -3.044 1.00 58.37 A C ANISOU 5208 CD1 LEU E 294 8032 6125 8021 640 1786 -802 A C ATOM 5209 CD2 LEU E 294 1.758 -9.449 -1.542 1.00 67.12 A C ANISOU 5209 CD2 LEU E 294 8777 7528 9197 733 1731 -718 A C ATOM 5210 N VAL E 295 5.029 -9.488 -5.466 1.00 77.63 A N ANISOU 5210 N VAL E 295 11801 7867 9828 903 2765 -494 A N ATOM 5211 CA VAL E 295 5.745 -9.474 -6.735 1.00 66.61 A C ANISOU 5211 CA VAL E 295 10998 6158 8152 911 3083 -517 A C ATOM 5212 C VAL E 295 5.621 -10.834 -7.410 1.00 72.54 A C ANISOU 5212 C VAL E 295 11796 6651 9116 1070 3628 -380 A C ATOM 5213 O VAL E 295 5.693 -10.938 -8.640 1.00 66.43 A O ANISOU 5213 O VAL E 295 11539 5619 8081 1083 3943 -397 A O ATOM 5214 CB VAL E 295 7.219 -9.068 -6.537 1.00 69.76 A C ANISOU 5214 CB VAL E 295 11588 6472 8444 892 3106 -563 A C ATOM 5215 CG1 VAL E 295 7.998 -10.151 -5.805 1.00 71.89 A C ANISOU 5215 CG1 VAL E 295 11520 6689 9106 1078 3399 -388 A C ATOM 5216 CG2 VAL E 295 7.858 -8.742 -7.867 1.00 78.74 A C ANISOU 5216 CG2 VAL E 295 13416 7309 9194 822 3328 -687 A C ATOM 5217 N GLY E 296 5.423 -11.882 -6.615 1.00 75.90 A N ANISOU 5217 N GLY E 296 11677 7154 10008 1187 3744 -237 A N ATOM 5218 CA GLY E 296 5.153 -13.192 -7.184 1.00 77.64 A C ANISOU 5218 CA GLY E 296 11823 7144 10532 1329 4254 -81 A C ATOM 5219 C GLY E 296 3.795 -13.202 -7.860 1.00 84.33 A C ANISOU 5219 C GLY E 296 12756 7946 11340 1265 4287 -88 A C ATOM 5220 O GLY E 296 2.790 -12.786 -7.272 1.00 89.55 A O ANISOU 5220 O GLY E 296 13118 8828 12079 1156 3906 -152 A O ATOM 5221 N VAL E 297 3.759 -13.668 -9.103 1.00 86.57 A N ANISOU 5221 N VAL E 297 13473 7920 11499 1341 4779 -17 A N ATOM 5222 CA VAL E 297 2.530 -13.680 -9.893 1.00 97.40 A C ANISOU 5222 CA VAL E 297 15009 9200 12797 1306 4886 32 A C ATOM 5223 C VAL E 297 1.763 -14.963 -9.598 1.00 98.55 A C ANISOU 5223 C VAL E 297 14609 9273 13561 1376 5184 197 A C ATOM 5224 O VAL E 297 2.358 -16.050 -9.587 1.00103.13 A O ANISOU 5224 O VAL E 297 14995 9702 14487 1516 5610 332 A O ATOM 5225 CB VAL E 297 2.838 -13.540 -11.393 1.00 91.13 A C ANISOU 5225 CB VAL E 297 14990 8129 11506 1352 5279 45 A C ATOM 5226 CG1 VAL E 297 1.617 -13.888 -12.233 1.00112.55 A C ANISOU 5226 CG1 VAL E 297 17836 10698 14229 1380 5551 196 A C ATOM 5227 CG2 VAL E 297 3.318 -12.131 -11.702 1.00 96.55 A C ANISOU 5227 CG2 VAL E 297 16171 8934 11578 1215 4851 -145 A C ATOM 5228 N PRO E 298 0.459 -14.893 -9.348 1.00 95.47 A N ANISOU 5228 N PRO E 298 13934 8966 13374 1278 4990 196 A N ATOM 5229 CA PRO E 298 -0.308 -16.110 -9.076 1.00 94.28 A C ANISOU 5229 CA PRO E 298 13241 8725 13857 1293 5259 324 A C ATOM 5230 C PRO E 298 -0.605 -16.890 -10.348 1.00 97.13 A C ANISOU 5230 C PRO E 298 13910 8714 14282 1406 5938 529 A C ATOM 5231 O PRO E 298 -0.498 -16.383 -11.465 1.00 98.35 A O ANISOU 5231 O PRO E 298 14739 8710 13920 1454 6142 559 A O ATOM 5232 CB PRO E 298 -1.598 -15.574 -8.446 1.00 86.67 A C ANISOU 5232 CB PRO E 298 11978 7928 13027 1123 4823 202 A C ATOM 5233 CG PRO E 298 -1.774 -14.237 -9.082 1.00 74.76 A C ANISOU 5233 CG PRO E 298 11041 6438 10925 1089 4592 135 A C ATOM 5234 CD PRO E 298 -0.381 -13.684 -9.275 1.00 97.12 A C ANISOU 5234 CD PRO E 298 14273 9334 13295 1143 4520 75 A C ATOM 5235 N SER E 299 -0.970 -18.155 -10.153 1.00 85.37 A N ANISOU 5235 N SER E 299 11903 7098 13437 1443 6288 679 A N ATOM 5236 CA SER E 299 -1.446 -19.014 -11.229 1.00104.84 A C ANISOU 5236 CA SER E 299 14529 9200 16106 1538 6980 905 A C ATOM 5237 C SER E 299 -2.929 -19.323 -11.100 1.00123.27 A C ANISOU 5237 C SER E 299 16483 11461 18894 1402 6976 955 A C ATOM 5238 O SER E 299 -3.678 -19.184 -12.072 1.00121.88 A O ANISOU 5238 O SER E 299 16702 11050 18556 1421 7290 1083 A O ATOM 5239 CB SER E 299 -0.638 -20.320 -11.268 1.00102.12 A C ANISOU 5239 CB SER E 299 13884 8684 16232 1709 7526 1088 A C ATOM 5240 OG SER E 299 -0.296 -20.752 -9.963 1.00107.13 A O ANISOU 5240 OG SER E 299 13790 9583 17330 1669 7153 1046 A O ATOM 5241 N LYS E 300 -3.375 -19.736 -9.917 1.00123.73 A N ANISOU 5241 N LYS E 300 15797 11706 19508 1256 6627 854 A N ATOM 5242 CA LYS E 300 -4.800 -19.892 -9.672 1.00119.27 A C ANISOU 5242 CA LYS E 300 14878 11065 19373 1075 6549 819 A C ATOM 5243 C LYS E 300 -5.450 -18.524 -9.490 1.00104.63 A C ANISOU 5243 C LYS E 300 13321 9355 17079 965 6042 627 A C ATOM 5244 O LYS E 300 -4.811 -17.559 -9.063 1.00118.88 A O ANISOU 5244 O LYS E 300 15331 11433 18406 969 5582 463 A O ATOM 5245 CB LYS E 300 -5.041 -20.766 -8.441 1.00124.33 A C ANISOU 5245 CB LYS E 300 14646 11880 20714 920 6297 721 A C ATOM 5246 CG LYS E 300 -5.205 -22.244 -8.759 1.00138.65 A C ANISOU 5246 CG LYS E 300 15998 13430 23252 950 6874 960 A C ATOM 5247 CD LYS E 300 -5.697 -23.024 -7.551 1.00143.68 A C ANISOU 5247 CD LYS E 300 15743 14257 24590 727 6524 831 A C ATOM 5248 CE LYS E 300 -7.214 -23.104 -7.523 1.00139.47 A C ANISOU 5248 CE LYS E 300 14990 13525 24478 476 6531 724 A C ATOM 5249 NZ LYS E 300 -7.721 -23.588 -6.208 1.00140.25 A N1+ ANISOU 5249 NZ LYS E 300 14307 13873 25107 192 6022 472 A N1+ ATOM 5250 N ASP E 301 -6.737 -18.449 -9.819 1.00124.60 A N ANISOU 5250 N ASP E 301 15850 11670 19822 875 6162 672 A N ATOM 5251 CA ASP E 301 -7.460 -17.181 -9.900 1.00116.49 A C ANISOU 5251 CA ASP E 301 15155 10688 18420 826 5815 579 A C ATOM 5252 C ASP E 301 -8.211 -16.851 -8.615 1.00115.05 A C ANISOU 5252 C ASP E 301 14465 10691 18557 614 5297 281 A C ATOM 5253 O ASP E 301 -9.346 -16.370 -8.660 1.00110.84 A O ANISOU 5253 O ASP E 301 13958 10010 18144 537 5244 248 A O ATOM 5254 CB ASP E 301 -8.418 -17.204 -11.088 1.00122.74 A C ANISOU 5254 CB ASP E 301 16316 11104 19214 895 6289 850 A C ATOM 5255 CG ASP E 301 -8.590 -15.841 -11.723 1.00119.87 A C ANISOU 5255 CG ASP E 301 16574 10795 18178 981 6052 906 A C ATOM 5256 OD1 ASP E 301 -7.995 -14.869 -11.214 1.00120.35 A O ANISOU 5256 OD1 ASP E 301 16735 11169 17824 964 5523 709 A O ATOM 5257 OD2 ASP E 301 -9.319 -15.742 -12.732 1.00103.18 A O1- ANISOU 5257 OD2 ASP E 301 14828 8414 15962 1070 6395 1174 A O1- ATOM 5258 N ASP E 302 -7.604 -17.089 -7.456 1.00113.84 A N ANISOU 5258 N ASP E 302 13870 10852 18530 528 4928 67 A N ATOM 5259 CA ASP E 302 -8.244 -16.741 -6.198 1.00 95.00 A C ANISOU 5259 CA ASP E 302 11070 8680 16347 324 4430 -253 A C ATOM 5260 C ASP E 302 -8.059 -15.254 -5.899 1.00102.78 A C ANISOU 5260 C ASP E 302 12396 9898 16758 356 3979 -403 A C ATOM 5261 O ASP E 302 -7.320 -14.541 -6.581 1.00106.30 A O ANISOU 5261 O ASP E 302 13337 10383 16669 511 3984 -274 A O ATOM 5262 CB ASP E 302 -7.691 -17.595 -5.059 1.00100.57 A C ANISOU 5262 CB ASP E 302 11176 9670 17366 224 4190 -396 A C ATOM 5263 CG ASP E 302 -8.132 -19.041 -5.153 1.00117.27 A C ANISOU 5263 CG ASP E 302 12790 11572 20196 129 4549 -290 A C ATOM 5264 OD1 ASP E 302 -8.867 -19.377 -6.105 1.00106.71 A O ANISOU 5264 OD1 ASP E 302 11591 9835 19117 142 5034 -108 A O ATOM 5265 OD2 ASP E 302 -7.749 -19.841 -4.273 1.00113.93 A O1- ANISOU 5265 OD2 ASP E 302 11816 11384 20088 43 4345 -366 A O1- ATOM 5266 N ALA E 303 -8.745 -14.787 -4.860 1.00 99.79 A N ANISOU 5266 N ALA E 303 11740 9667 16509 195 3595 -695 A N ATOM 5267 CA ALA E 303 -8.759 -13.379 -4.495 1.00 97.53 A C ANISOU 5267 CA ALA E 303 11695 9569 15794 216 3209 -839 A C ATOM 5268 C ALA E 303 -7.993 -13.145 -3.199 1.00 91.41 A C ANISOU 5268 C ALA E 303 10665 9224 14843 155 2760 -1078 A C ATOM 5269 O ALA E 303 -7.871 -14.038 -2.355 1.00 94.99 A O ANISOU 5269 O ALA E 303 10671 9835 15585 42 2662 -1206 A O ATOM 5270 CB ALA E 303 -10.195 -12.866 -4.342 1.00 89.99 A C ANISOU 5270 CB ALA E 303 10691 8407 15096 116 3187 -974 A C ATOM 5271 N PHE E 304 -7.479 -11.926 -3.054 1.00 84.30 A N ANISOU 5271 N PHE E 304 10043 8521 13467 232 2483 -1114 A N ATOM 5272 CA PHE E 304 -6.791 -11.512 -1.838 1.00 71.26 A C ANISOU 5272 CA PHE E 304 8210 7265 11601 192 2086 -1311 A C ATOM 5273 C PHE E 304 -7.824 -11.130 -0.784 1.00 82.74 A C ANISOU 5273 C PHE E 304 9405 8805 13227 35 1847 -1636 A C ATOM 5274 O PHE E 304 -8.673 -10.265 -1.025 1.00 75.51 A O ANISOU 5274 O PHE E 304 8656 7724 12310 40 1857 -1685 A O ATOM 5275 CB PHE E 304 -5.847 -10.348 -2.141 1.00 70.32 A C ANISOU 5275 CB PHE E 304 8477 7280 10962 317 1932 -1214 A C ATOM 5276 CG PHE E 304 -5.144 -9.796 -0.932 1.00 68.48 A C ANISOU 5276 CG PHE E 304 8094 7425 10502 291 1573 -1374 A C ATOM 5277 CD1 PHE E 304 -5.716 -8.783 -0.177 1.00 73.08 A C ANISOU 5277 CD1 PHE E 304 8626 8141 11001 232 1322 -1581 A C ATOM 5278 CD2 PHE E 304 -3.895 -10.271 -0.567 1.00 80.11 A C ANISOU 5278 CD2 PHE E 304 9490 9097 11852 347 1532 -1287 A C ATOM 5279 CE1 PHE E 304 -5.067 -8.272 0.930 1.00 75.11 A C ANISOU 5279 CE1 PHE E 304 8769 8742 11028 219 1046 -1704 A C ATOM 5280 CE2 PHE E 304 -3.240 -9.763 0.541 1.00 83.95 A C ANISOU 5280 CE2 PHE E 304 9856 9923 12118 339 1234 -1385 A C ATOM 5281 CZ PHE E 304 -3.828 -8.763 1.290 1.00 76.53 A C ANISOU 5281 CZ PHE E 304 8882 9132 11066 270 995 -1596 A C ATOM 5282 N LYS E 305 -7.752 -11.771 0.383 1.00 83.64 A N ANISOU 5282 N LYS E 305 9121 9177 13481 -98 1637 -1853 A N ATOM 5283 CA LYS E 305 -8.720 -11.580 1.456 1.00 76.66 A C ANISOU 5283 CA LYS E 305 7999 8380 12748 -282 1429 -2226 A C ATOM 5284 C LYS E 305 -7.998 -11.197 2.738 1.00 80.05 A C ANISOU 5284 C LYS E 305 8316 9278 12823 -300 1052 -2399 A C ATOM 5285 O LYS E 305 -7.040 -11.869 3.134 1.00 75.06 A O ANISOU 5285 O LYS E 305 7506 8913 12100 -270 933 -2294 A O ATOM 5286 CB LYS E 305 -9.535 -12.855 1.699 1.00 83.92 A C ANISOU 5286 CB LYS E 305 8519 9165 14200 -492 1518 -2379 A C ATOM 5287 CG LYS E 305 -10.606 -13.170 0.672 1.00 95.05 A C ANISOU 5287 CG LYS E 305 9995 10069 16050 -527 1912 -2282 A C ATOM 5288 CD LYS E 305 -11.520 -14.254 1.225 1.00 91.46 A C ANISOU 5288 CD LYS E 305 9089 9506 16155 -806 1925 -2546 A C ATOM 5289 CE LYS E 305 -12.193 -15.056 0.129 1.00 98.05 A C ANISOU 5289 CE LYS E 305 9882 9862 17512 -830 2391 -2326 A C ATOM 5290 NZ LYS E 305 -13.566 -15.471 0.528 1.00 95.60 A N1+ ANISOU 5290 NZ LYS E 305 9294 9267 17761 -1115 2460 -2648 A N1+ ATOM 5291 N THR E 306 -8.468 -10.139 3.397 1.00 86.90 A N ANISOU 5291 N THR E 306 9278 10232 13507 -330 898 -2638 A N ATOM 5292 CA THR E 306 -7.927 -9.780 4.701 1.00 76.05 A C ANISOU 5292 CA THR E 306 7808 9298 11791 -358 582 -2823 A C ATOM 5293 C THR E 306 -8.925 -8.909 5.450 1.00 79.96 A C ANISOU 5293 C THR E 306 8342 9780 12259 -451 519 -3184 A C ATOM 5294 O THR E 306 -9.771 -8.236 4.853 1.00 85.82 A O ANISOU 5294 O THR E 306 9249 10183 13176 -417 711 -3199 A O ATOM 5295 CB THR E 306 -6.577 -9.060 4.584 1.00 83.56 A C ANISOU 5295 CB THR E 306 8974 10455 12321 -165 511 -2554 A C ATOM 5296 CG2 THR E 306 -6.756 -7.682 3.971 1.00 80.12 A C ANISOU 5296 CG2 THR E 306 8857 9838 11748 -57 597 -2480 A C ATOM 5297 OG1 THR E 306 -5.999 -8.920 5.888 1.00 78.42 A O ANISOU 5297 OG1 THR E 306 8197 10239 11361 -186 239 -2680 A O ATOM 5298 N HIS E 307 -8.814 -8.954 6.774 1.00 93.55 A N ANISOU 5298 N HIS E 307 9917 11874 13754 -554 264 -3461 A N ATOM 5299 CA HIS E 307 -9.570 -8.064 7.643 1.00 90.52 A C ANISOU 5299 CA HIS E 307 9611 11532 13249 -620 226 -3824 A C ATOM 5300 C HIS E 307 -9.247 -6.615 7.288 1.00 93.34 A C ANISOU 5300 C HIS E 307 10242 11829 13394 -411 327 -3637 A C ATOM 5301 O HIS E 307 -8.065 -6.249 7.235 1.00 88.94 A O ANISOU 5301 O HIS E 307 9770 11498 12527 -271 240 -3366 A O ATOM 5302 CB HIS E 307 -9.203 -8.359 9.101 1.00 90.35 A C ANISOU 5302 CB HIS E 307 9447 12007 12873 -730 -80 -4081 A C ATOM 5303 CG HIS E 307 -10.205 -7.878 10.106 1.00110.39 A C ANISOU 5303 CG HIS E 307 12030 14572 15342 -880 -98 -4579 A C ATOM 5304 CD2 HIS E 307 -10.193 -7.923 11.460 1.00115.14 A C ANISOU 5304 CD2 HIS E 307 12598 15576 15576 -1000 -326 -4913 A C ATOM 5305 ND1 HIS E 307 -11.390 -7.270 9.756 1.00109.91 A N ANISOU 5305 ND1 HIS E 307 12087 14075 15597 -910 167 -4786 A N ATOM 5306 CE1 HIS E 307 -12.063 -6.956 10.849 1.00105.07 A C ANISOU 5306 CE1 HIS E 307 11516 13562 14843 -1045 134 -5255 A C ATOM 5307 NE2 HIS E 307 -11.359 -7.344 11.897 1.00121.65 A N ANISOU 5307 NE2 HIS E 307 13543 16183 16494 -1112 -172 -5355 A N ATOM 5308 N PRO E 308 -10.248 -5.773 7.008 1.00 97.15 A N ANISOU 5308 N PRO E 308 10842 11991 14078 -383 517 -3751 A N ATOM 5309 CA PRO E 308 -9.936 -4.362 6.710 1.00 85.91 A C ANISOU 5309 CA PRO E 308 9609 10542 12491 -188 575 -3553 A C ATOM 5310 C PRO E 308 -9.135 -3.686 7.807 1.00 88.24 A C ANISOU 5310 C PRO E 308 9918 11250 12361 -143 426 -3622 A C ATOM 5311 O PRO E 308 -8.248 -2.872 7.515 1.00 75.09 A O ANISOU 5311 O PRO E 308 8352 9683 10496 0 396 -3341 A O ATOM 5312 CB PRO E 308 -11.318 -3.713 6.529 1.00 83.19 A C ANISOU 5312 CB PRO E 308 9309 9807 12492 -178 801 -3725 A C ATOM 5313 CG PRO E 308 -12.295 -4.818 6.414 1.00 84.63 A C ANISOU 5313 CG PRO E 308 9375 9724 13058 -362 906 -3943 A C ATOM 5314 CD PRO E 308 -11.679 -6.093 6.875 1.00 94.64 A C ANISOU 5314 CD PRO E 308 10466 11288 14206 -522 701 -4022 A C ATOM 5315 N MET E 309 -9.405 -4.021 9.071 1.00 78.51 A N ANISOU 5315 N MET E 309 8595 10267 10968 -277 331 -3989 A N ATOM 5316 CA MET E 309 -8.653 -3.419 10.164 1.00 81.23 A C ANISOU 5316 CA MET E 309 8979 11021 10865 -223 224 -4032 A C ATOM 5317 C MET E 309 -7.166 -3.742 10.091 1.00 77.93 A C ANISOU 5317 C MET E 309 8543 10904 10163 -139 54 -3671 A C ATOM 5318 O MET E 309 -6.357 -3.001 10.658 1.00 77.72 A O ANISOU 5318 O MET E 309 8583 11130 9816 -39 29 -3552 A O ATOM 5319 CB MET E 309 -9.236 -3.857 11.506 1.00 87.98 A C ANISOU 5319 CB MET E 309 9781 12114 11533 -399 134 -4505 A C ATOM 5320 CG MET E 309 -10.660 -3.376 11.733 1.00 96.53 A C ANISOU 5320 CG MET E 309 10927 12875 12875 -476 361 -4914 A C ATOM 5321 SD MET E 309 -10.767 -1.580 11.886 1.00 90.48 A S ANISOU 5321 SD MET E 309 10317 12001 12062 -251 640 -4851 A S ATOM 5322 CE MET E 309 -9.489 -1.262 13.099 1.00 78.15 A C ANISOU 5322 CE MET E 309 8808 11037 9847 -191 486 -4783 A C ATOM 5323 N ASN E 310 -6.779 -4.815 9.396 1.00 72.14 A N ANISOU 5323 N ASN E 310 7720 10115 9574 -167 -15 -3477 A N ATOM 5324 CA ASN E 310 -5.359 -5.029 9.137 1.00 73.11 A C ANISOU 5324 CA ASN E 310 7858 10417 9504 -52 -98 -3100 A C ATOM 5325 C ASN E 310 -4.759 -3.854 8.377 1.00 79.30 A C ANISOU 5325 C ASN E 310 8834 11048 10249 93 15 -2826 A C ATOM 5326 O ASN E 310 -3.587 -3.517 8.580 1.00 74.02 A O ANISOU 5326 O ASN E 310 8216 10568 9339 180 -32 -2598 A O ATOM 5327 CB ASN E 310 -5.145 -6.332 8.365 1.00 71.85 A C ANISOU 5327 CB ASN E 310 7578 10136 9584 -82 -104 -2933 A C ATOM 5328 CG ASN E 310 -5.509 -7.556 9.180 1.00 74.80 A C ANISOU 5328 CG ASN E 310 7684 10732 10003 -237 -283 -3151 A C ATOM 5329 ND2 ASN E 310 -5.758 -8.670 8.500 1.00 74.32 A N ANISOU 5329 ND2 ASN E 310 7459 10482 10295 -303 -235 -3086 A N ATOM 5330 OD1 ASN E 310 -5.565 -7.502 10.408 1.00 69.79 A O ANISOU 5330 OD1 ASN E 310 6986 10445 9084 -304 -466 -3373 A O ATOM 5331 N PHE E 311 -5.548 -3.215 7.511 1.00 70.79 A N ANISOU 5331 N PHE E 311 7852 9626 9419 112 153 -2832 A N ATOM 5332 CA PHE E 311 -5.116 -1.979 6.870 1.00 70.31 A C ANISOU 5332 CA PHE E 311 7935 9455 9324 223 199 -2608 A C ATOM 5333 C PHE E 311 -5.314 -0.783 7.793 1.00 75.98 A C ANISOU 5333 C PHE E 311 8627 10313 9929 261 231 -2741 A C ATOM 5334 O PHE E 311 -4.392 0.016 7.990 1.00 69.91 A O ANISOU 5334 O PHE E 311 7890 9691 8981 324 205 -2567 A O ATOM 5335 CB PHE E 311 -5.879 -1.761 5.562 1.00 73.97 A C ANISOU 5335 CB PHE E 311 8498 9531 10076 252 304 -2506 A C ATOM 5336 CG PHE E 311 -5.376 -2.592 4.422 1.00 75.08 A C ANISOU 5336 CG PHE E 311 8750 9520 10256 260 327 -2273 A C ATOM 5337 CD1 PHE E 311 -4.205 -2.253 3.764 1.00 71.75 A C ANISOU 5337 CD1 PHE E 311 8490 9122 9649 316 279 -2009 A C ATOM 5338 CD2 PHE E 311 -6.079 -3.707 3.999 1.00 65.81 A C ANISOU 5338 CD2 PHE E 311 7528 8155 9323 200 432 -2330 A C ATOM 5339 CE1 PHE E 311 -3.741 -3.013 2.709 1.00 73.23 A C ANISOU 5339 CE1 PHE E 311 8829 9148 9845 330 354 -1823 A C ATOM 5340 CE2 PHE E 311 -5.621 -4.473 2.945 1.00 81.00 A C ANISOU 5340 CE2 PHE E 311 9567 9925 11285 226 522 -2105 A C ATOM 5341 CZ PHE E 311 -4.449 -4.127 2.300 1.00 80.37 A C ANISOU 5341 CZ PHE E 311 9688 9874 10974 299 492 -1860 A C ATOM 5342 N LEU E 312 -6.513 -0.649 8.370 1.00 72.44 A N ANISOU 5342 N LEU E 312 8122 9791 9610 218 326 -3058 A N ATOM 5343 CA LEU E 312 -6.816 0.532 9.178 1.00 70.46 A C ANISOU 5343 CA LEU E 312 7859 9614 9299 279 439 -3192 A C ATOM 5344 C LEU E 312 -5.928 0.645 10.409 1.00 79.66 A C ANISOU 5344 C LEU E 312 9018 11193 10057 282 386 -3222 A C ATOM 5345 O LEU E 312 -5.843 1.728 10.998 1.00 72.97 A O ANISOU 5345 O LEU E 312 8171 10429 9124 359 511 -3230 A O ATOM 5346 CB LEU E 312 -8.283 0.548 9.612 1.00 75.77 A C ANISOU 5346 CB LEU E 312 8507 10092 10193 228 604 -3572 A C ATOM 5347 CG LEU E 312 -9.321 0.948 8.561 1.00 75.92 A C ANISOU 5347 CG LEU E 312 8529 9659 10659 291 752 -3506 A C ATOM 5348 CD1 LEU E 312 -8.909 2.216 7.825 1.00 74.05 A C ANISOU 5348 CD1 LEU E 312 8291 9339 10506 453 760 -3148 A C ATOM 5349 CD2 LEU E 312 -9.555 -0.177 7.589 1.00 94.60 A C ANISOU 5349 CD2 LEU E 312 10911 11818 13214 214 698 -3418 A C ATOM 5350 N ASN E 313 -5.273 -0.440 10.818 1.00 82.01 A N ANISOU 5350 N ASN E 313 9294 11748 10116 219 222 -3207 A N ATOM 5351 CA ASN E 313 -4.234 -0.359 11.834 1.00 77.52 A C ANISOU 5351 CA ASN E 313 8735 11575 9144 259 159 -3108 A C ATOM 5352 C ASN E 313 -2.886 0.062 11.258 1.00 76.13 A C ANISOU 5352 C ASN E 313 8594 11400 8932 351 143 -2688 A C ATOM 5353 O ASN E 313 -1.841 -0.238 11.849 1.00 75.77 A O ANISOU 5353 O ASN E 313 8549 11628 8612 389 77 -2511 A O ATOM 5354 CB ASN E 313 -4.114 -1.688 12.583 1.00 73.10 A C ANISOU 5354 CB ASN E 313 8107 11318 8349 168 -38 -3236 A C ATOM 5355 CG ASN E 313 -5.273 -1.924 13.538 1.00 95.16 A C ANISOU 5355 CG ASN E 313 10898 14215 11045 43 -42 -3715 A C ATOM 5356 ND2 ASN E 313 -4.977 -1.924 14.831 1.00108.61 A N ANISOU 5356 ND2 ASN E 313 12646 16330 12289 38 -109 -3832 A N ATOM 5357 OD1 ASN E 313 -6.416 -2.097 13.123 1.00 98.13 A O ANISOU 5357 OD1 ASN E 313 11253 14293 11739 -53 29 -3978 A O ATOM 5358 N GLU E 314 -2.917 0.742 10.110 1.00 70.83 A N ANISOU 5358 N GLU E 314 7959 10418 8536 381 196 -2528 A N ATOM 5359 CA GLU E 314 -1.761 1.358 9.470 1.00 72.82 A C ANISOU 5359 CA GLU E 314 8263 10612 8792 426 183 -2195 A C ATOM 5360 C GLU E 314 -0.762 0.324 8.968 1.00 63.68 A C ANISOU 5360 C GLU E 314 7165 9463 7568 418 92 -1988 A C ATOM 5361 O GLU E 314 0.361 0.224 9.472 1.00 65.29 A O ANISOU 5361 O GLU E 314 7377 9850 7580 456 87 -1803 A O ATOM 5362 CB GLU E 314 -1.102 2.359 10.420 1.00 64.54 A C ANISOU 5362 CB GLU E 314 7182 9777 7564 477 279 -2110 A C ATOM 5363 CG GLU E 314 -1.934 3.618 10.585 1.00 66.74 A C ANISOU 5363 CG GLU E 314 7388 9955 8017 513 426 -2226 A C ATOM 5364 CD GLU E 314 -1.335 4.612 11.551 1.00 76.77 A C ANISOU 5364 CD GLU E 314 8605 11421 9144 569 585 -2135 A C ATOM 5365 OE1 GLU E 314 -0.296 4.300 12.170 1.00 76.93 A O ANISOU 5365 OE1 GLU E 314 8667 11670 8892 580 580 -1982 A O ATOM 5366 OE2 GLU E 314 -1.912 5.710 11.686 1.00 75.28 A O1- ANISOU 5366 OE2 GLU E 314 8320 11141 9143 617 746 -2188 A O1- ATOM 5367 N ARG E 315 -1.180 -0.447 7.969 1.00 70.50 A N ANISOU 5367 N ARG E 315 8072 10102 8615 385 63 -1997 A N ATOM 5368 CA ARG E 315 -0.305 -1.279 7.162 1.00 55.47 A C ANISOU 5368 CA ARG E 315 6255 8094 6726 395 51 -1786 A C ATOM 5369 C ARG E 315 -0.420 -0.837 5.710 1.00 67.38 A C ANISOU 5369 C ARG E 315 7932 9274 8394 380 76 -1687 A C ATOM 5370 O ARG E 315 -1.428 -0.261 5.294 1.00 69.58 A O ANISOU 5370 O ARG E 315 8214 9404 8820 369 79 -1783 A O ATOM 5371 CB ARG E 315 -0.660 -2.767 7.288 1.00 57.91 A C ANISOU 5371 CB ARG E 315 6460 8450 7095 375 25 -1865 A C ATOM 5372 CG ARG E 315 -0.221 -3.412 8.589 1.00 63.99 A C ANISOU 5372 CG ARG E 315 7073 9590 7651 395 -69 -1877 A C ATOM 5373 CD ARG E 315 -0.592 -4.887 8.615 1.00 62.30 A C ANISOU 5373 CD ARG E 315 6691 9418 7561 354 -137 -1939 A C ATOM 5374 NE ARG E 315 -0.209 -5.524 9.869 1.00 64.13 A N ANISOU 5374 NE ARG E 315 6749 10055 7563 371 -297 -1933 A N ATOM 5375 CZ ARG E 315 -0.990 -5.605 10.938 1.00 70.21 A C ANISOU 5375 CZ ARG E 315 7413 11091 8174 283 -435 -2223 A C ATOM 5376 NH1 ARG E 315 -2.215 -5.105 10.939 1.00 80.47 A N1+ ANISOU 5376 NH1 ARG E 315 8752 12251 9570 176 -388 -2559 A N1+ ATOM 5377 NH2 ARG E 315 -0.530 -6.205 12.033 1.00 61.94 A N ANISOU 5377 NH2 ARG E 315 6230 10454 6852 306 -621 -2172 A N ATOM 5378 N THR E 316 0.627 -1.106 4.936 1.00 57.05 A N ANISOU 5378 N THR E 316 6782 7849 7045 387 101 -1487 A N ATOM 5379 CA THR E 316 0.663 -0.753 3.524 1.00 54.71 A C ANISOU 5379 CA THR E 316 6709 7275 6803 359 104 -1397 A C ATOM 5380 C THR E 316 0.913 -2.004 2.694 1.00 61.87 A C ANISOU 5380 C THR E 316 7755 8010 7741 381 225 -1321 A C ATOM 5381 O THR E 316 1.728 -2.853 3.068 1.00 57.42 A O ANISOU 5381 O THR E 316 7151 7518 7146 423 301 -1238 A O ATOM 5382 CB THR E 316 1.748 0.296 3.237 1.00 52.28 A C ANISOU 5382 CB THR E 316 6523 6942 6401 313 45 -1265 A C ATOM 5383 CG2 THR E 316 1.767 0.667 1.759 1.00 49.58 A C ANISOU 5383 CG2 THR E 316 6439 6351 6047 257 -11 -1201 A C ATOM 5384 OG1 THR E 316 1.490 1.474 4.011 1.00 63.37 A O ANISOU 5384 OG1 THR E 316 7753 8494 7832 302 -25 -1310 A O ATOM 5385 N LEU E 317 0.198 -2.121 1.577 1.00 60.62 A N ANISOU 5385 N LEU E 317 7751 7621 7659 372 270 -1318 A N ATOM 5386 CA LEU E 317 0.380 -3.224 0.639 1.00 63.03 A C ANISOU 5386 CA LEU E 317 8230 7723 7997 401 450 -1230 A C ATOM 5387 C LEU E 317 0.652 -2.640 -0.740 1.00 57.55 A C ANISOU 5387 C LEU E 317 7899 6813 7154 375 450 -1134 A C ATOM 5388 O LEU E 317 -0.222 -1.999 -1.332 1.00 67.99 A O ANISOU 5388 O LEU E 317 9294 8054 8485 363 365 -1134 A O ATOM 5389 CB LEU E 317 -0.839 -4.145 0.612 1.00 69.33 A C ANISOU 5389 CB LEU E 317 8879 8442 9021 412 555 -1312 A C ATOM 5390 CG LEU E 317 -0.693 -5.384 -0.273 1.00 66.65 A C ANISOU 5390 CG LEU E 317 8660 7889 8774 453 804 -1200 A C ATOM 5391 CD1 LEU E 317 0.488 -6.221 0.182 1.00 59.15 A C ANISOU 5391 CD1 LEU E 317 7625 7034 7816 505 891 -1109 A C ATOM 5392 CD2 LEU E 317 -1.964 -6.210 -0.254 1.00 69.45 A C ANISOU 5392 CD2 LEU E 317 8821 8146 9420 433 913 -1282 A C ATOM 5393 N LYS E 318 1.864 -2.853 -1.240 1.00 58.06 A N ANISOU 5393 N LYS E 318 8201 6784 7076 367 543 -1051 A N ATOM 5394 CA LYS E 318 2.258 -2.432 -2.574 1.00 61.50 A C ANISOU 5394 CA LYS E 318 9044 7020 7301 314 546 -1001 A C ATOM 5395 C LYS E 318 2.400 -3.656 -3.464 1.00 65.24 A C ANISOU 5395 C LYS E 318 9762 7266 7759 383 863 -936 A C ATOM 5396 O LYS E 318 2.817 -4.723 -3.005 1.00 66.53 A O ANISOU 5396 O LYS E 318 9785 7419 8074 460 1078 -900 A O ATOM 5397 CB LYS E 318 3.578 -1.656 -2.542 1.00 49.84 A C ANISOU 5397 CB LYS E 318 7710 5555 5673 219 447 -1002 A C ATOM 5398 CG LYS E 318 3.583 -0.460 -1.605 1.00 59.32 A C ANISOU 5398 CG LYS E 318 8640 6969 6930 155 196 -1035 A C ATOM 5399 CD LYS E 318 4.981 0.121 -1.456 1.00 49.70 A C ANISOU 5399 CD LYS E 318 7518 5727 5640 53 167 -1020 A C ATOM 5400 CE LYS E 318 4.971 1.364 -0.580 1.00 56.06 A C ANISOU 5400 CE LYS E 318 8041 6726 6532 -14 -40 -1024 A C ATOM 5401 NZ LYS E 318 6.337 1.928 -0.394 1.00 70.31 A N1+ ANISOU 5401 NZ LYS E 318 9911 8475 8328 -132 -36 -994 A N1+ ATOM 5402 N GLY E 319 2.035 -3.503 -4.731 1.00 65.42 A N ANISOU 5402 N GLY E 319 10138 7118 7600 368 901 -897 A N ATOM 5403 CA GLY E 319 2.290 -4.508 -5.744 1.00 63.94 A C ANISOU 5403 CA GLY E 319 10281 6687 7325 429 1249 -831 A C ATOM 5404 C GLY E 319 3.286 -3.954 -6.742 1.00 61.95 A C ANISOU 5404 C GLY E 319 10529 6308 6700 339 1229 -865 A C ATOM 5405 O GLY E 319 3.298 -2.754 -7.021 1.00 72.94 A O ANISOU 5405 O GLY E 319 12039 7790 7886 220 894 -907 A O ATOM 5406 N THR E 320 4.136 -4.828 -7.272 1.00 67.41 A N ANISOU 5406 N THR E 320 11583 5955 8075 527 1002 351 A N ATOM 5407 CA THR E 320 5.164 -4.394 -8.203 1.00 77.29 A C ANISOU 5407 CA THR E 320 12707 7346 9314 559 1124 425 A C ATOM 5408 C THR E 320 5.345 -5.427 -9.303 1.00 69.69 A C ANISOU 5408 C THR E 320 11524 6400 8553 418 1212 380 A C ATOM 5409 O THR E 320 5.111 -6.623 -9.109 1.00 63.59 A O ANISOU 5409 O THR E 320 10637 5569 7956 309 1128 281 A O ATOM 5410 CB THR E 320 6.504 -4.143 -7.497 1.00 69.20 A C ANISOU 5410 CB THR E 320 11638 6410 8243 663 1008 428 A C ATOM 5411 CG2 THR E 320 7.007 -5.409 -6.836 1.00 61.48 A C ANISOU 5411 CG2 THR E 320 10522 5401 7437 622 829 315 A C ATOM 5412 OG1 THR E 320 7.471 -3.689 -8.452 1.00 78.64 A O ANISOU 5412 OG1 THR E 320 12731 7723 9424 676 1134 489 A O ATOM 5413 N PHE E 321 5.758 -4.938 -10.468 1.00 65.35 A N ANISOU 5413 N PHE E 321 10912 5949 7967 421 1383 453 A N ATOM 5414 CA PHE E 321 6.076 -5.761 -11.624 1.00 64.48 A C ANISOU 5414 CA PHE E 321 10598 5888 8015 311 1497 422 A C ATOM 5415 C PHE E 321 7.506 -5.460 -12.045 1.00 75.17 A C ANISOU 5415 C PHE E 321 11844 7367 9350 377 1527 433 A C ATOM 5416 O PHE E 321 7.862 -4.292 -12.237 1.00 74.57 A O ANISOU 5416 O PHE E 321 11864 7369 9102 457 1588 518 A O ATOM 5417 CB PHE E 321 5.108 -5.486 -12.778 1.00 65.79 A C ANISOU 5417 CB PHE E 321 10812 6045 8142 239 1696 497 A C ATOM 5418 CG PHE E 321 5.606 -5.958 -14.115 1.00 70.60 A C ANISOU 5418 CG PHE E 321 11234 6751 8839 162 1851 495 A C ATOM 5419 CD1 PHE E 321 5.720 -7.311 -14.389 1.00 63.55 A C ANISOU 5419 CD1 PHE E 321 10139 5848 8160 43 1846 402 A C ATOM 5420 CD2 PHE E 321 5.959 -5.049 -15.100 1.00 70.88 A C ANISOU 5420 CD2 PHE E 321 11289 6906 8736 209 2002 583 A C ATOM 5421 CE1 PHE E 321 6.177 -7.749 -15.619 1.00 68.19 A C ANISOU 5421 CE1 PHE E 321 10557 6534 8817 -16 2001 395 A C ATOM 5422 CE2 PHE E 321 6.417 -5.480 -16.332 1.00 70.10 A C ANISOU 5422 CE2 PHE E 321 11032 6901 8700 141 2146 570 A C ATOM 5423 CZ PHE E 321 6.526 -6.832 -16.592 1.00 75.20 A C ANISOU 5423 CZ PHE E 321 11488 7528 9556 34 2152 476 A C ATOM 5424 N PHE E 322 8.321 -6.509 -12.175 1.00 71.53 A N ANISOU 5424 N PHE E 322 11188 6928 9064 343 1482 344 A N ATOM 5425 CA PHE E 322 9.726 -6.373 -12.557 1.00 64.83 A C ANISOU 5425 CA PHE E 322 10247 6165 8219 404 1506 334 A C ATOM 5426 C PHE E 322 10.479 -5.451 -11.599 1.00 65.53 A C ANISOU 5426 C PHE E 322 10470 6262 8168 526 1392 379 A C ATOM 5427 O PHE E 322 11.401 -4.734 -11.998 1.00 70.50 A O ANISOU 5427 O PHE E 322 11116 6960 8711 567 1452 418 A O ATOM 5428 CB PHE E 322 9.853 -5.885 -14.006 1.00 64.87 A C ANISOU 5428 CB PHE E 322 10221 6266 8162 364 1719 382 A C ATOM 5429 CG PHE E 322 11.232 -6.035 -14.587 1.00 64.46 A C ANISOU 5429 CG PHE E 322 10055 6284 8155 394 1761 336 A C ATOM 5430 CD1 PHE E 322 12.050 -7.088 -14.215 1.00 66.19 A C ANISOU 5430 CD1 PHE E 322 10131 6471 8545 425 1663 239 A C ATOM 5431 CD2 PHE E 322 11.703 -5.123 -15.517 1.00 64.92 A C ANISOU 5431 CD2 PHE E 322 10151 6438 8076 398 1897 387 A C ATOM 5432 CE1 PHE E 322 13.316 -7.224 -14.754 1.00 72.41 A C ANISOU 5432 CE1 PHE E 322 10840 7300 9373 469 1709 192 A C ATOM 5433 CE2 PHE E 322 12.966 -5.254 -16.060 1.00 58.69 A C ANISOU 5433 CE2 PHE E 322 9283 5693 7323 417 1938 330 A C ATOM 5434 CZ PHE E 322 13.774 -6.305 -15.678 1.00 69.16 A C ANISOU 5434 CZ PHE E 322 10488 6963 8825 458 1848 232 A C ATOM 5435 N GLY E 323 10.085 -5.462 -10.326 1.00 59.45 A N ANISOU 5435 N GLY E 323 9801 5422 7366 573 1229 372 A N ATOM 5436 CA GLY E 323 10.713 -4.610 -9.333 1.00 72.84 A C ANISOU 5436 CA GLY E 323 11630 7127 8917 685 1124 424 A C ATOM 5437 C GLY E 323 10.576 -3.130 -9.598 1.00 71.10 A C ANISOU 5437 C GLY E 323 11554 6982 8480 725 1233 538 A C ATOM 5438 O GLY E 323 11.396 -2.345 -9.114 1.00 69.09 A O ANISOU 5438 O GLY E 323 11370 6774 8109 795 1195 592 A O ATOM 5439 N ASN E 324 9.556 -2.725 -10.357 1.00 77.46 A N ANISOU 5439 N ASN E 324 12402 7807 9224 682 1370 583 A N ATOM 5440 CA ASN E 324 9.355 -1.342 -10.786 1.00 79.83 A C ANISOU 5440 CA ASN E 324 12806 8208 9318 726 1489 697 A C ATOM 5441 C ASN E 324 10.563 -0.788 -11.536 1.00 72.51 A C ANISOU 5441 C ASN E 324 11806 7402 8344 714 1569 726 A C ATOM 5442 O ASN E 324 10.757 0.431 -11.595 1.00 83.71 A O ANISOU 5442 O ASN E 324 13296 8929 9581 756 1619 817 A O ATOM 5443 CB ASN E 324 9.002 -0.432 -9.603 1.00 70.54 A C ANISOU 5443 CB ASN E 324 11804 7031 7966 836 1404 759 A C ATOM 5444 CG ASN E 324 7.506 -0.321 -9.383 1.00 85.80 A C ANISOU 5444 CG ASN E 324 13869 8887 9845 860 1424 776 A C ATOM 5445 ND2 ASN E 324 6.988 0.900 -9.451 1.00 99.21 A N ANISOU 5445 ND2 ASN E 324 15688 10664 11346 948 1509 881 A N ATOM 5446 OD1 ASN E 324 6.824 -1.320 -9.160 1.00 81.07 A O ANISOU 5446 OD1 ASN E 324 13264 8160 9380 799 1366 695 A O ATOM 5447 N TYR E 325 11.379 -1.667 -12.113 1.00 62.23 A N ANISOU 5447 N TYR E 325 10359 6084 7200 656 1582 645 A N ATOM 5448 CA TYR E 325 12.524 -1.248 -12.908 1.00 71.12 A C ANISOU 5448 CA TYR E 325 11429 7300 8293 631 1663 648 A C ATOM 5449 C TYR E 325 12.078 -0.918 -14.326 1.00 70.80 A C ANISOU 5449 C TYR E 325 11344 7361 8195 566 1845 678 A C ATOM 5450 O TYR E 325 11.407 -1.725 -14.977 1.00 69.23 A O ANISOU 5450 O TYR E 325 11069 7132 8102 512 1916 639 A O ATOM 5451 CB TYR E 325 13.584 -2.349 -12.947 1.00 64.57 A C ANISOU 5451 CB TYR E 325 10479 6403 7653 621 1608 541 A C ATOM 5452 CG TYR E 325 14.563 -2.345 -11.795 1.00 66.50 A C ANISOU 5452 CG TYR E 325 10776 6583 7907 694 1452 536 A C ATOM 5453 CD1 TYR E 325 15.321 -1.219 -11.500 1.00 63.23 A C ANISOU 5453 CD1 TYR E 325 10467 6218 7339 715 1447 610 A C ATOM 5454 CD2 TYR E 325 14.747 -3.480 -11.016 1.00 72.45 A C ANISOU 5454 CD2 TYR E 325 11471 7236 8821 739 1311 463 A C ATOM 5455 CE1 TYR E 325 16.224 -1.220 -10.452 1.00 58.15 A C ANISOU 5455 CE1 TYR E 325 9888 5507 6700 777 1314 620 A C ATOM 5456 CE2 TYR E 325 15.647 -3.490 -9.969 1.00 67.56 A C ANISOU 5456 CE2 TYR E 325 10911 6557 8200 820 1167 472 A C ATOM 5457 CZ TYR E 325 16.381 -2.359 -9.690 1.00 66.43 A C ANISOU 5457 CZ TYR E 325 10893 6447 7903 839 1174 555 A C ATOM 5458 OH TYR E 325 17.276 -2.372 -8.645 1.00 69.13 A O ANISOU 5458 OH TYR E 325 11308 6720 8237 914 1039 579 A O ATOM 5459 N LYS E 326 12.453 0.261 -14.806 1.00 63.63 A N ANISOU 5459 N LYS E 326 10478 6586 7112 566 1920 750 A N ATOM 5460 CA LYS E 326 12.223 0.600 -16.204 1.00 64.52 A C ANISOU 5460 CA LYS E 326 10542 6821 7152 508 2084 775 A C ATOM 5461 C LYS E 326 13.243 -0.132 -17.067 1.00 71.85 A C ANISOU 5461 C LYS E 326 11352 7750 8199 441 2139 669 A C ATOM 5462 O LYS E 326 14.449 0.012 -16.835 1.00 71.48 A O ANISOU 5462 O LYS E 326 11305 7693 8161 439 2087 626 A O ATOM 5463 CB LYS E 326 12.313 2.105 -16.418 1.00 75.91 A C ANISOU 5463 CB LYS E 326 12049 8433 8360 527 2131 881 A C ATOM 5464 CG LYS E 326 11.143 2.873 -15.819 1.00 71.58 A C ANISOU 5464 CG LYS E 326 11611 7910 7675 617 2119 994 A C ATOM 5465 CD LYS E 326 11.248 4.365 -16.082 1.00 73.83 A C ANISOU 5465 CD LYS E 326 11926 8401 7727 645 2171 1104 A C ATOM 5466 CE LYS E 326 10.142 5.123 -15.365 1.00 81.51 A C ANISOU 5466 CE LYS E 326 13011 9397 8564 769 2156 1212 A C ATOM 5467 NZ LYS E 326 8.794 4.750 -15.876 1.00 82.68 A N1+ ANISOU 5467 NZ LYS E 326 13201 9484 8731 804 2236 1243 A N1+ ATOM 5468 N PRO E 327 12.811 -0.925 -18.053 1.00 70.15 A N ANISOU 5468 N PRO E 327 11042 7539 8071 388 2250 624 A N ATOM 5469 CA PRO E 327 13.762 -1.813 -18.751 1.00 61.24 A C ANISOU 5469 CA PRO E 327 9795 6397 7079 347 2298 505 A C ATOM 5470 C PRO E 327 14.944 -1.096 -19.383 1.00 68.99 A C ANISOU 5470 C PRO E 327 10790 7470 7953 319 2346 478 A C ATOM 5471 O PRO E 327 16.089 -1.535 -19.216 1.00 77.41 A O ANISOU 5471 O PRO E 327 11831 8465 9117 330 2300 386 A O ATOM 5472 CB PRO E 327 12.876 -2.500 -19.799 1.00 64.42 A C ANISOU 5472 CB PRO E 327 10110 6833 7532 289 2442 498 A C ATOM 5473 CG PRO E 327 11.509 -2.481 -19.199 1.00 64.50 A C ANISOU 5473 CG PRO E 327 10189 6782 7536 302 2406 580 A C ATOM 5474 CD PRO E 327 11.414 -1.188 -18.441 1.00 65.08 A C ANISOU 5474 CD PRO E 327 10406 6890 7431 369 2329 677 A C ATOM 5475 N LYS E 328 14.707 -0.003 -20.106 1.00 70.59 A N ANISOU 5475 N LYS E 328 11037 7829 7956 284 2434 554 A N ATOM 5476 CA LYS E 328 15.791 0.704 -20.775 1.00 68.66 A C ANISOU 5476 CA LYS E 328 10803 7686 7597 229 2478 518 A C ATOM 5477 C LYS E 328 16.419 1.793 -19.918 1.00 82.05 A C ANISOU 5477 C LYS E 328 12592 9403 9179 233 2375 575 A C ATOM 5478 O LYS E 328 17.583 2.143 -20.144 1.00 86.76 A O ANISOU 5478 O LYS E 328 13209 10012 9742 176 2371 518 A O ATOM 5479 CB LYS E 328 15.289 1.318 -22.085 1.00 57.44 A C ANISOU 5479 CB LYS E 328 9362 6457 6004 177 2622 565 A C ATOM 5480 CG LYS E 328 15.077 0.305 -23.194 1.00 53.92 A C ANISOU 5480 CG LYS E 328 8823 6018 5646 145 2753 489 A C ATOM 5481 CD LYS E 328 14.566 0.969 -24.458 1.00 75.35 A C ANISOU 5481 CD LYS E 328 11533 8933 8163 102 2890 552 A C ATOM 5482 CE LYS E 328 15.680 1.713 -25.173 1.00 57.05 A C ANISOU 5482 CE LYS E 328 9227 6746 5702 34 2916 488 A C ATOM 5483 NZ LYS E 328 16.514 0.800 -26.004 1.00 63.08 A N1+ ANISOU 5483 NZ LYS E 328 9930 7475 6562 -6 3000 330 A N1+ ATOM 5484 N THR E 329 15.687 2.324 -18.942 1.00 69.73 A N ANISOU 5484 N THR E 329 11096 7840 7557 295 2298 683 A N ATOM 5485 CA THR E 329 16.169 3.434 -18.130 1.00 70.63 A C ANISOU 5485 CA THR E 329 11289 8006 7542 299 2217 756 A C ATOM 5486 C THR E 329 16.952 2.964 -16.907 1.00 76.39 A C ANISOU 5486 C THR E 329 12068 8561 8396 336 2082 719 A C ATOM 5487 O THR E 329 17.960 3.580 -16.543 1.00 80.95 A O ANISOU 5487 O THR E 329 12698 9142 8916 295 2037 728 A O ATOM 5488 CB THR E 329 14.983 4.313 -17.703 1.00 74.99 A C ANISOU 5488 CB THR E 329 11890 8663 7940 368 2216 896 A C ATOM 5489 CG2 THR E 329 15.320 5.152 -16.479 1.00 54.52 A C ANISOU 5489 CG2 THR E 329 9375 6082 5258 406 2113 970 A C ATOM 5490 OG1 THR E 329 14.623 5.188 -18.779 1.00 71.11 A O ANISOU 5490 OG1 THR E 329 11365 8382 7270 333 2326 957 A O ATOM 5491 N ASP E 330 16.535 1.860 -16.287 1.00 73.26 A N ANISOU 5491 N ASP E 330 11655 8013 8168 406 2014 677 A N ATOM 5492 CA ASP E 330 17.060 1.451 -14.989 1.00 72.50 A C ANISOU 5492 CA ASP E 330 11611 7770 8165 468 1867 665 A C ATOM 5493 C ASP E 330 17.997 0.250 -15.030 1.00 74.89 A C ANISOU 5493 C ASP E 330 11858 7925 8670 482 1829 544 A C ATOM 5494 O ASP E 330 18.922 0.188 -14.220 1.00 75.93 A O ANISOU 5494 O ASP E 330 12051 7956 8841 517 1728 538 A O ATOM 5495 CB ASP E 330 15.903 1.135 -14.033 1.00 74.21 A C ANISOU 5495 CB ASP E 330 11860 7932 8407 551 1785 710 A C ATOM 5496 CG ASP E 330 15.091 2.364 -13.674 1.00 77.25 A C ANISOU 5496 CG ASP E 330 12329 8436 8586 581 1800 835 A C ATOM 5497 OD1 ASP E 330 15.635 3.485 -13.764 1.00 82.81 A O ANISOU 5497 OD1 ASP E 330 13068 9262 9136 549 1829 900 A O ATOM 5498 OD2 ASP E 330 13.906 2.210 -13.312 1.00 76.77 A O1- ANISOU 5498 OD2 ASP E 330 12300 8351 8518 637 1785 866 A O1- ATOM 5499 N ILE E 331 17.777 -0.704 -15.943 1.00 66.53 A N ANISOU 5499 N ILE E 331 10687 6856 7737 466 1911 455 A N ATOM 5500 CA ILE E 331 18.577 -1.937 -15.930 1.00 73.41 A C ANISOU 5500 CA ILE E 331 11484 7600 8810 510 1875 339 A C ATOM 5501 C ILE E 331 20.062 -1.672 -16.122 1.00 76.17 A C ANISOU 5501 C ILE E 331 11893 7894 9153 496 1879 289 A C ATOM 5502 O ILE E 331 20.879 -2.322 -15.441 1.00 75.00 A O ANISOU 5502 O ILE E 331 11761 7605 9130 574 1781 246 A O ATOM 5503 CB ILE E 331 18.003 -2.943 -16.944 1.00 68.39 A C ANISOU 5503 CB ILE E 331 10700 6995 8292 488 1987 260 A C ATOM 5504 CG1 ILE E 331 16.623 -3.423 -16.487 1.00 57.85 A C ANISOU 5504 CG1 ILE E 331 9321 5654 7006 498 1950 301 A C ATOM 5505 CG2 ILE E 331 18.943 -4.123 -17.130 1.00 67.00 A C ANISOU 5505 CG2 ILE E 331 10429 6724 8306 543 1980 135 A C ATOM 5506 CD1 ILE E 331 16.617 -4.044 -15.106 1.00 60.15 A C ANISOU 5506 CD1 ILE E 331 9620 5826 7407 579 1768 295 A C ATOM 5507 N PRO E 332 20.501 -0.770 -17.011 1.00 72.33 A N ANISOU 5507 N PRO E 332 11449 7505 8528 400 1983 289 A N ATOM 5508 CA PRO E 332 21.926 -0.399 -17.017 1.00 68.31 A C ANISOU 5508 CA PRO E 332 11036 6917 8003 367 1969 247 A C ATOM 5509 C PRO E 332 22.434 0.049 -15.659 1.00 68.27 A C ANISOU 5509 C PRO E 332 11152 6815 7973 404 1828 331 A C ATOM 5510 O PRO E 332 23.596 -0.211 -15.320 1.00 76.56 A O ANISOU 5510 O PRO E 332 12278 7713 9098 431 1777 290 A O ATOM 5511 CB PRO E 332 21.983 0.736 -18.047 1.00 56.39 A C ANISOU 5511 CB PRO E 332 9551 5576 6301 232 2083 261 A C ATOM 5512 CG PRO E 332 20.874 0.436 -18.980 1.00 58.99 A C ANISOU 5512 CG PRO E 332 9766 6036 6613 225 2192 253 A C ATOM 5513 CD PRO E 332 19.779 -0.160 -18.146 1.00 68.48 A C ANISOU 5513 CD PRO E 332 10921 7196 7902 316 2120 313 A C ATOM 5514 N GLY E 333 21.590 0.705 -14.858 1.00 69.39 A N ANISOU 5514 N GLY E 333 11325 7034 8006 415 1769 453 A N ATOM 5515 CA GLY E 333 21.983 1.053 -13.504 1.00 61.63 A C ANISOU 5515 CA GLY E 333 10454 5970 6992 462 1638 538 A C ATOM 5516 C GLY E 333 22.215 -0.158 -12.623 1.00 64.89 A C ANISOU 5516 C GLY E 333 10858 6212 7585 595 1512 499 A C ATOM 5517 O GLY E 333 23.088 -0.136 -11.752 1.00 67.58 A O ANISOU 5517 O GLY E 333 11302 6433 7942 639 1416 533 A O ATOM 5518 N VAL E 334 21.455 -1.233 -12.840 1.00 67.68 A N ANISOU 5518 N VAL E 334 11085 6559 8073 656 1510 432 A N ATOM 5519 CA VAL E 334 21.699 -2.470 -12.103 1.00 75.86 A C ANISOU 5519 CA VAL E 334 12075 7461 9288 781 1387 382 A C ATOM 5520 C VAL E 334 23.018 -3.096 -12.543 1.00 70.93 A C ANISOU 5520 C VAL E 334 11448 6711 8790 823 1408 288 A C ATOM 5521 O VAL E 334 23.792 -3.610 -11.719 1.00 77.11 A O ANISOU 5521 O VAL E 334 12281 7358 9659 932 1291 290 A O ATOM 5522 CB VAL E 334 20.516 -3.437 -12.290 1.00 67.07 A C ANISOU 5522 CB VAL E 334 10808 6392 8284 806 1389 331 A C ATOM 5523 CG1 VAL E 334 20.709 -4.686 -11.446 1.00 67.87 A C ANISOU 5523 CG1 VAL E 334 10840 6389 8559 929 1241 283 A C ATOM 5524 CG2 VAL E 334 19.208 -2.744 -11.942 1.00 63.82 A C ANISOU 5524 CG2 VAL E 334 10433 6078 7736 766 1385 418 A C ATOM 5525 N VAL E 335 23.299 -3.058 -13.848 1.00 71.66 A N ANISOU 5525 N VAL E 335 11494 6847 8887 750 1559 206 A N ATOM 5526 CA VAL E 335 24.596 -3.530 -14.328 1.00 70.39 A C ANISOU 5526 CA VAL E 335 11361 6558 8825 791 1595 108 A C ATOM 5527 C VAL E 335 25.723 -2.733 -13.678 1.00 72.16 A C ANISOU 5527 C VAL E 335 11786 6661 8972 772 1534 170 A C ATOM 5528 O VAL E 335 26.758 -3.290 -13.289 1.00 76.97 A O ANISOU 5528 O VAL E 335 12463 7095 9688 875 1473 138 A O ATOM 5529 CB VAL E 335 24.658 -3.458 -15.865 1.00 79.56 A C ANISOU 5529 CB VAL E 335 12463 7806 9962 699 1776 7 A C ATOM 5530 CG1 VAL E 335 26.095 -3.582 -16.349 1.00 66.29 A C ANISOU 5530 CG1 VAL E 335 10876 5983 8328 716 1823 -92 A C ATOM 5531 CG2 VAL E 335 23.792 -4.547 -16.477 1.00 59.72 A C ANISOU 5531 CG2 VAL E 335 9749 5372 7571 742 1840 -65 A C ATOM 5532 N GLU E 336 25.530 -1.421 -13.531 1.00 73.89 A N ANISOU 5532 N GLU E 336 12100 6974 9001 644 1550 270 A N ATOM 5533 CA GLU E 336 26.538 -0.594 -12.873 1.00 83.50 A C ANISOU 5533 CA GLU E 336 13501 8092 10133 596 1499 347 A C ATOM 5534 C GLU E 336 26.661 -0.941 -11.394 1.00 75.64 A C ANISOU 5534 C GLU E 336 12575 6985 9181 727 1335 439 A C ATOM 5535 O GLU E 336 27.767 -0.942 -10.841 1.00 69.90 A O ANISOU 5535 O GLU E 336 11990 6086 8481 763 1276 466 A O ATOM 5536 CB GLU E 336 26.208 0.888 -13.050 1.00 73.20 A C ANISOU 5536 CB GLU E 336 12245 6958 8611 426 1558 439 A C ATOM 5537 CG GLU E 336 26.230 1.362 -14.494 1.00 68.83 A C ANISOU 5537 CG GLU E 336 11642 6526 7985 285 1706 356 A C ATOM 5538 CD GLU E 336 27.578 1.165 -15.166 1.00 89.30 A C ANISOU 5538 CD GLU E 336 14327 8964 10640 237 1760 240 A C ATOM 5539 OE1 GLU E 336 28.607 1.120 -14.457 1.00 81.32 A O ANISOU 5539 OE1 GLU E 336 13460 7759 9677 265 1689 262 A O ATOM 5540 OE2 GLU E 336 27.607 1.052 -16.409 1.00 89.41 A O1- ANISOU 5540 OE2 GLU E 336 14280 9043 10648 177 1876 125 A O1- ATOM 5541 N LYS E 337 25.534 -1.224 -10.735 1.00 72.91 A N ANISOU 5541 N LYS E 337 12301 7388 8014 -189 2087 969 A N ATOM 5542 CA LYS E 337 25.579 -1.694 -9.354 1.00 77.05 A C ANISOU 5542 CA LYS E 337 12802 8109 8364 72 1966 1112 A C ATOM 5543 C LYS E 337 26.434 -2.947 -9.234 1.00 89.67 A C ANISOU 5543 C LYS E 337 14507 9437 10127 246 1959 1250 A C ATOM 5544 O LYS E 337 27.138 -3.135 -8.235 1.00 91.41 A O ANISOU 5544 O LYS E 337 14811 9703 10217 388 1957 1488 A O ATOM 5545 CB LYS E 337 24.166 -1.960 -8.838 1.00 83.28 A C ANISOU 5545 CB LYS E 337 13382 9203 9056 266 1734 891 A C ATOM 5546 CG LYS E 337 23.733 -1.035 -7.717 1.00 96.83 A C ANISOU 5546 CG LYS E 337 15023 11339 10428 332 1672 927 A C ATOM 5547 CD LYS E 337 22.276 -1.256 -7.359 1.00 88.78 A C ANISOU 5547 CD LYS E 337 13799 10581 9350 516 1421 651 A C ATOM 5548 CE LYS E 337 21.834 -0.304 -6.266 1.00 94.51 A C ANISOU 5548 CE LYS E 337 14445 11753 9710 610 1354 659 A C ATOM 5549 NZ LYS E 337 20.380 -0.009 -6.344 1.00 98.78 A N1+ ANISOU 5549 NZ LYS E 337 14806 12506 10218 667 1159 339 A N1+ ATOM 5550 N TYR E 338 26.383 -3.819 -10.243 1.00 84.50 A N ANISOU 5550 N TYR E 338 13845 8515 9748 251 1957 1111 A N ATOM 5551 CA TYR E 338 27.311 -4.948 -10.249 1.00 80.80 A C ANISOU 5551 CA TYR E 338 13487 7770 9443 406 1972 1239 A C ATOM 5552 C TYR E 338 28.746 -4.480 -10.468 1.00 84.44 A C ANISOU 5552 C TYR E 338 14183 7956 9945 251 2165 1465 A C ATOM 5553 O TYR E 338 29.670 -4.961 -9.801 1.00 74.81 A O ANISOU 5553 O TYR E 338 13091 6619 8715 394 2173 1692 A O ATOM 5554 CB TYR E 338 26.928 -5.980 -11.309 1.00 78.81 A C ANISOU 5554 CB TYR E 338 13151 7327 9467 454 1937 1041 A C ATOM 5555 CG TYR E 338 27.997 -7.043 -11.498 1.00 78.83 A C ANISOU 5555 CG TYR E 338 13279 7026 9647 595 1983 1158 A C ATOM 5556 CD1 TYR E 338 28.128 -8.090 -10.595 1.00 90.21 A C ANISOU 5556 CD1 TYR E 338 14688 8513 11076 887 1847 1245 A C ATOM 5557 CD2 TYR E 338 28.870 -7.004 -12.579 1.00 73.48 A C ANISOU 5557 CD2 TYR E 338 12749 6026 9144 456 2147 1162 A C ATOM 5558 CE1 TYR E 338 29.096 -9.065 -10.758 1.00 87.30 A C ANISOU 5558 CE1 TYR E 338 14430 7876 10865 1037 1880 1346 A C ATOM 5559 CE2 TYR E 338 29.845 -7.976 -12.749 1.00 70.95 A C ANISOU 5559 CE2 TYR E 338 12545 5430 8984 611 2176 1250 A C ATOM 5560 CZ TYR E 338 29.952 -9.002 -11.835 1.00 90.08 A C ANISOU 5560 CZ TYR E 338 14931 7903 11391 901 2045 1348 A C ATOM 5561 OH TYR E 338 30.920 -9.967 -12.005 1.00 91.68 A O ANISOU 5561 OH TYR E 338 15248 7838 11749 1072 2069 1430 A O ATOM 5562 N MET E 339 28.952 -3.548 -11.402 1.00 82.34 A N ANISOU 5562 N MET E 339 13977 7572 9737 -37 2310 1404 A N ATOM 5563 CA MET E 339 30.306 -3.109 -11.735 1.00 85.68 A C ANISOU 5563 CA MET E 339 14618 7686 10252 -207 2476 1584 A C ATOM 5564 C MET E 339 30.981 -2.402 -10.568 1.00 80.14 A C ANISOU 5564 C MET E 339 14008 7092 9350 -239 2524 1895 A C ATOM 5565 O MET E 339 32.202 -2.508 -10.400 1.00 86.24 A O ANISOU 5565 O MET E 339 14969 7589 10209 -256 2606 2128 A O ATOM 5566 CB MET E 339 30.272 -2.198 -12.964 1.00 76.76 A C ANISOU 5566 CB MET E 339 13504 6450 9212 -507 2596 1418 A C ATOM 5567 CG MET E 339 29.894 -2.899 -14.268 1.00 75.31 A C ANISOU 5567 CG MET E 339 13270 6103 9241 -484 2592 1159 A C ATOM 5568 SD MET E 339 31.283 -3.703 -15.101 1.00 90.01 A S ANISOU 5568 SD MET E 339 15341 7482 11377 -441 2683 1195 A S ATOM 5569 CE MET E 339 31.391 -5.269 -14.247 1.00 92.83 A C ANISOU 5569 CE MET E 339 15677 7821 11774 -65 2553 1308 A C ATOM 5570 N ASN E 340 30.216 -1.673 -9.757 1.00 87.47 A N ANISOU 5570 N ASN E 340 14805 8419 10012 -242 2475 1912 A N ATOM 5571 CA ASN E 340 30.757 -1.008 -8.581 1.00 82.00 A C ANISOU 5571 CA ASN E 340 14165 7905 9087 -247 2526 2224 A C ATOM 5572 C ASN E 340 30.890 -1.945 -7.383 1.00 83.32 A C ANISOU 5572 C ASN E 340 14340 8189 9130 94 2406 2400 A C ATOM 5573 O ASN E 340 31.054 -1.467 -6.253 1.00 77.47 A O ANISOU 5573 O ASN E 340 13594 7714 8127 158 2416 2640 A O ATOM 5574 CB ASN E 340 29.893 0.203 -8.218 1.00 91.53 A C ANISOU 5574 CB ASN E 340 15215 9531 10031 -371 2529 2160 A C ATOM 5575 CG ASN E 340 29.916 1.277 -9.291 1.00 87.34 A C ANISOU 5575 CG ASN E 340 14687 8903 9595 -719 2660 2034 A C ATOM 5576 ND2 ASN E 340 31.037 1.982 -9.397 1.00104.77 A N ANISOU 5576 ND2 ASN E 340 17035 10909 11864 -956 2822 2260 A N ATOM 5577 OD1 ASN E 340 28.942 1.467 -10.020 1.00 84.95 A O ANISOU 5577 OD1 ASN E 340 14259 8698 9318 -774 2608 1739 A O ATOM 5578 N LYS E 341 30.817 -3.258 -7.617 1.00 93.32 A N ANISOU 5578 N LYS E 341 15604 9285 10567 320 2296 2287 A N ATOM 5579 CA LYS E 341 31.008 -4.276 -6.582 1.00105.07 A C ANISOU 5579 CA LYS E 341 17102 10849 11972 662 2170 2432 A C ATOM 5580 C LYS E 341 30.006 -4.130 -5.441 1.00 96.61 A C ANISOU 5580 C LYS E 341 15851 10271 10587 861 2015 2392 A C ATOM 5581 O LYS E 341 30.306 -4.454 -4.289 1.00 92.50 A O ANISOU 5581 O LYS E 341 15354 9919 9873 1101 1949 2603 A O ATOM 5582 CB LYS E 341 32.443 -4.259 -6.048 1.00 92.00 A C ANISOU 5582 CB LYS E 341 15672 8968 10317 673 2281 2818 A C ATOM 5583 CG LYS E 341 33.483 -4.646 -7.089 1.00 96.01 A C ANISOU 5583 CG LYS E 341 16369 8955 11157 556 2386 2834 A C ATOM 5584 CD LYS E 341 34.753 -3.824 -6.942 1.00117.56 A C ANISOU 5584 CD LYS E 341 19308 11447 13912 342 2555 3166 A C ATOM 5585 CE LYS E 341 35.583 -3.861 -8.216 1.00117.53 A C ANISOU 5585 CE LYS E 341 19464 10947 14246 145 2656 3080 A C ATOM 5586 NZ LYS E 341 35.645 -2.530 -8.881 1.00117.87 A N1+ ANISOU 5586 NZ LYS E 341 19513 10953 14321 -242 2792 3032 A N1+ ATOM 5587 N GLU E 342 28.807 -3.643 -5.756 1.00 88.54 A N ANISOU 5587 N GLU E 342 14650 9485 9507 780 1945 2113 A N ATOM 5588 CA GLU E 342 27.710 -3.555 -4.801 1.00 88.97 A C ANISOU 5588 CA GLU E 342 14517 9991 9295 985 1762 1992 A C ATOM 5589 C GLU E 342 26.740 -4.721 -4.922 1.00 89.53 A C ANISOU 5589 C GLU E 342 14429 10083 9506 1212 1533 1704 A C ATOM 5590 O GLU E 342 26.318 -5.280 -3.906 1.00 90.90 A O ANISOU 5590 O GLU E 342 14506 10508 9522 1509 1344 1683 A O ATOM 5591 CB GLU E 342 26.952 -2.237 -4.991 1.00 89.37 A C ANISOU 5591 CB GLU E 342 14463 10304 9189 772 1806 1861 A C ATOM 5592 CG GLU E 342 25.989 -1.897 -3.867 1.00 95.21 A C ANISOU 5592 CG GLU E 342 15035 11545 9596 985 1638 1777 A C ATOM 5593 CD GLU E 342 25.150 -0.673 -4.176 1.00101.73 A C ANISOU 5593 CD GLU E 342 15744 12613 10295 794 1663 1598 A C ATOM 5594 OE1 GLU E 342 25.714 0.328 -4.666 1.00101.76 A O ANISOU 5594 OE1 GLU E 342 15826 12539 10299 501 1870 1724 A O ATOM 5595 OE2 GLU E 342 23.928 -0.708 -3.924 1.00 96.44 A O1- ANISOU 5595 OE2 GLU E 342 14900 12206 9536 942 1463 1324 A O1- ATOM 5596 N LEU E 343 26.384 -5.100 -6.146 1.00 90.45 A N ANISOU 5596 N LEU E 343 14504 9945 9916 1078 1544 1486 A N ATOM 5597 CA LEU E 343 25.516 -6.240 -6.407 1.00 88.40 A C ANISOU 5597 CA LEU E 343 14083 9660 9847 1249 1350 1237 A C ATOM 5598 C LEU E 343 26.379 -7.429 -6.810 1.00 89.21 A C ANISOU 5598 C LEU E 343 14278 9424 10192 1350 1388 1328 A C ATOM 5599 O LEU E 343 27.077 -7.376 -7.828 1.00 90.07 A O ANISOU 5599 O LEU E 343 14512 9218 10492 1166 1562 1368 A O ATOM 5600 CB LEU E 343 24.505 -5.908 -7.504 1.00 81.89 A C ANISOU 5600 CB LEU E 343 13133 8801 9181 1049 1343 960 A C ATOM 5601 CG LEU E 343 23.622 -7.054 -7.996 1.00 76.18 A C ANISOU 5601 CG LEU E 343 12232 7998 8714 1162 1174 726 A C ATOM 5602 CD1 LEU E 343 22.579 -7.414 -6.952 1.00 65.58 A C ANISOU 5602 CD1 LEU E 343 10702 6961 7253 1409 894 578 A C ATOM 5603 CD2 LEU E 343 22.961 -6.688 -9.316 1.00 69.91 A C ANISOU 5603 CD2 LEU E 343 11374 7085 8105 918 1245 539 A C ATOM 5604 N GLU E 344 26.332 -8.495 -6.014 1.00 89.53 A N ANISOU 5604 N GLU E 344 14253 9543 10221 1658 1214 1343 A N ATOM 5605 CA GLU E 344 27.150 -9.682 -6.240 1.00 86.39 A C ANISOU 5605 CA GLU E 344 13929 8869 10026 1807 1227 1433 A C ATOM 5606 C GLU E 344 26.328 -10.701 -7.025 1.00 81.27 A C ANISOU 5606 C GLU E 344 13086 8134 9661 1850 1112 1170 A C ATOM 5607 O GLU E 344 25.322 -11.215 -6.525 1.00 97.84 A O ANISOU 5607 O GLU E 344 14977 10446 11753 2013 887 996 A O ATOM 5608 CB GLU E 344 27.636 -10.260 -4.912 1.00 91.52 A C ANISOU 5608 CB GLU E 344 14617 9665 10491 2129 1108 1620 A C ATOM 5609 CG GLU E 344 28.688 -9.406 -4.217 1.00102.78 A C ANISOU 5609 CG GLU E 344 16260 11115 11678 2089 1259 1958 A C ATOM 5610 CD GLU E 344 28.663 -9.558 -2.707 1.00114.46 A C ANISOU 5610 CD GLU E 344 17710 12933 12845 2396 1110 2101 A C ATOM 5611 OE1 GLU E 344 28.017 -10.506 -2.215 1.00108.79 A O ANISOU 5611 OE1 GLU E 344 16830 12375 12132 2671 881 1937 A O ATOM 5612 OE2 GLU E 344 29.290 -8.729 -2.013 1.00109.96 A O1- ANISOU 5612 OE2 GLU E 344 17271 12483 12026 2364 1222 2380 A O1- ATOM 5613 N LEU E 345 26.765 -10.997 -8.252 1.00 86.22 A N ANISOU 5613 N LEU E 345 13771 8452 10538 1709 1261 1142 A N ATOM 5614 CA LEU E 345 26.015 -11.858 -9.158 1.00 89.10 A C ANISOU 5614 CA LEU E 345 13944 8736 11173 1707 1199 924 A C ATOM 5615 C LEU E 345 26.546 -13.283 -9.243 1.00 86.77 A C ANISOU 5615 C LEU E 345 13619 8283 11069 1937 1156 956 A C ATOM 5616 O LEU E 345 25.809 -14.171 -9.684 1.00 81.04 A O ANISOU 5616 O LEU E 345 12677 7567 10547 1996 1054 791 A O ATOM 5617 CB LEU E 345 26.004 -11.267 -10.574 1.00 77.41 A C ANISOU 5617 CB LEU E 345 12509 7072 9831 1415 1393 842 A C ATOM 5618 CG LEU E 345 25.285 -9.939 -10.809 1.00 70.72 A C ANISOU 5618 CG LEU E 345 11644 6372 8855 1166 1434 751 A C ATOM 5619 CD1 LEU E 345 25.397 -9.524 -12.271 1.00 71.63 A C ANISOU 5619 CD1 LEU E 345 11808 6288 9119 917 1622 674 A C ATOM 5620 CD2 LEU E 345 23.840 -10.025 -10.385 1.00 73.68 A C ANISOU 5620 CD2 LEU E 345 11779 7006 9208 1229 1214 559 A C ATOM 5621 N GLU E 346 27.799 -13.523 -8.846 1.00 81.64 A N ANISOU 5621 N GLU E 346 13169 7483 10366 2066 1229 1171 A N ATOM 5622 CA GLU E 346 28.391 -14.844 -9.040 1.00 88.96 A C ANISOU 5622 CA GLU E 346 14081 8240 11480 2288 1205 1196 A C ATOM 5623 C GLU E 346 27.660 -15.909 -8.232 1.00 87.18 A C ANISOU 5623 C GLU E 346 13619 8232 11275 2564 950 1099 A C ATOM 5624 O GLU E 346 27.463 -17.033 -8.708 1.00 93.11 A O ANISOU 5624 O GLU E 346 14206 8920 12252 2677 893 994 A O ATOM 5625 CB GLU E 346 29.874 -14.819 -8.673 1.00 91.29 A C ANISOU 5625 CB GLU E 346 14656 8325 11705 2386 1312 1457 A C ATOM 5626 CG GLU E 346 30.664 -16.009 -9.199 1.00 89.28 A C ANISOU 5626 CG GLU E 346 14434 7821 11666 2572 1342 1472 A C ATOM 5627 CD GLU E 346 30.602 -16.133 -10.709 1.00105.45 A C ANISOU 5627 CD GLU E 346 16442 9679 13944 2402 1486 1312 A C ATOM 5628 OE1 GLU E 346 29.948 -17.075 -11.205 1.00103.60 A O ANISOU 5628 OE1 GLU E 346 15974 9506 13883 2487 1418 1148 A O ATOM 5629 OE2 GLU E 346 31.208 -15.288 -11.400 1.00115.07 A O1- ANISOU 5629 OE2 GLU E 346 17854 10698 15170 2186 1665 1352 A O1- ATOM 5630 N LYS E 347 27.243 -15.574 -7.008 1.00 81.29 A N ANISOU 5630 N LYS E 347 12837 7758 10293 2680 789 1125 A N ATOM 5631 CA LYS E 347 26.544 -16.543 -6.170 1.00 78.13 A C ANISOU 5631 CA LYS E 347 12209 7575 9900 2955 517 1008 A C ATOM 5632 C LYS E 347 25.209 -16.967 -6.767 1.00 86.95 A C ANISOU 5632 C LYS E 347 13031 8761 11246 2866 387 732 A C ATOM 5633 O LYS E 347 24.687 -18.025 -6.399 1.00 85.42 A O ANISOU 5633 O LYS E 347 12615 8665 11176 3068 175 612 A O ATOM 5634 CB LYS E 347 26.332 -15.973 -4.767 1.00 77.66 A C ANISOU 5634 CB LYS E 347 12175 7823 9507 3101 371 1071 A C ATOM 5635 CG LYS E 347 26.061 -14.480 -4.735 1.00 83.87 A C ANISOU 5635 CG LYS E 347 13059 8724 10085 2857 477 1097 A C ATOM 5636 CD LYS E 347 25.426 -14.071 -3.417 1.00 81.18 A C ANISOU 5636 CD LYS E 347 12638 8767 9438 3030 276 1059 A C ATOM 5637 CE LYS E 347 25.640 -12.596 -3.133 1.00 86.07 A C ANISOU 5637 CE LYS E 347 13415 9514 9773 2854 426 1202 A C ATOM 5638 NZ LYS E 347 24.985 -12.169 -1.868 1.00 87.14 A N1+ ANISOU 5638 NZ LYS E 347 13459 10066 9583 3044 234 1151 A N1+ ATOM 5639 N PHE E 348 24.642 -16.168 -7.673 1.00 86.63 A N ANISOU 5639 N PHE E 348 12975 8669 11272 2570 503 636 A N ATOM 5640 CA PHE E 348 23.437 -16.571 -8.386 1.00 86.00 A C ANISOU 5640 CA PHE E 348 12629 8606 11441 2462 409 414 A C ATOM 5641 C PHE E 348 23.720 -17.587 -9.484 1.00 77.62 A C ANISOU 5641 C PHE E 348 11480 7332 10678 2451 516 406 A C ATOM 5642 O PHE E 348 22.806 -18.312 -9.891 1.00 75.62 A O ANISOU 5642 O PHE E 348 10960 7107 10664 2439 404 259 A O ATOM 5643 CB PHE E 348 22.746 -15.350 -8.999 1.00 82.06 A C ANISOU 5643 CB PHE E 348 12151 8131 10896 2164 499 329 A C ATOM 5644 CG PHE E 348 22.100 -14.443 -7.992 1.00 85.48 A C ANISOU 5644 CG PHE E 348 12581 8827 11072 2182 349 267 A C ATOM 5645 CD1 PHE E 348 22.817 -13.409 -7.411 1.00 79.54 A C ANISOU 5645 CD1 PHE E 348 12055 8151 10015 2157 461 429 A C ATOM 5646 CD2 PHE E 348 20.771 -14.613 -7.637 1.00 78.90 A C ANISOU 5646 CD2 PHE E 348 11508 8164 10307 2225 93 46 A C ATOM 5647 CE1 PHE E 348 22.223 -12.566 -6.489 1.00 85.57 A C ANISOU 5647 CE1 PHE E 348 12799 9197 10516 2192 333 373 A C ATOM 5648 CE2 PHE E 348 20.171 -13.773 -6.715 1.00 80.71 A C ANISOU 5648 CE2 PHE E 348 11732 8652 10284 2271 -56 -37 A C ATOM 5649 CZ PHE E 348 20.898 -12.748 -6.140 1.00 78.24 A C ANISOU 5649 CZ PHE E 348 11638 8452 9637 2263 71 127 A C ATOM 5650 N ILE E 349 24.956 -17.654 -9.970 1.00 75.61 A N ANISOU 5650 N ILE E 349 11436 6870 10422 2460 727 561 A N ATOM 5651 CA ILE E 349 25.319 -18.536 -11.073 1.00 87.44 A C ANISOU 5651 CA ILE E 349 12870 8183 12169 2467 853 550 A C ATOM 5652 C ILE E 349 25.833 -19.846 -10.486 1.00 73.56 A C ANISOU 5652 C ILE E 349 11035 6430 10485 2788 733 596 A C ATOM 5653 O ILE E 349 26.942 -19.907 -9.950 1.00 83.62 A O ANISOU 5653 O ILE E 349 12524 7620 11630 2954 772 753 A O ATOM 5654 CB ILE E 349 26.364 -17.887 -11.987 1.00 87.84 A C ANISOU 5654 CB ILE E 349 13189 7998 12189 2316 1130 651 A C ATOM 5655 CG1 ILE E 349 25.817 -16.586 -12.578 1.00 78.73 A C ANISOU 5655 CG1 ILE E 349 12091 6863 10961 2003 1237 590 A C ATOM 5656 CG2 ILE E 349 26.785 -18.852 -13.085 1.00 76.44 A C ANISOU 5656 CG2 ILE E 349 11676 6394 10974 2375 1251 626 A C ATOM 5657 CD1 ILE E 349 26.762 -15.909 -13.546 1.00 80.74 A C ANISOU 5657 CD1 ILE E 349 12585 6892 11201 1838 1490 653 A C ATOM 5658 N THR E 350 25.025 -20.902 -10.595 1.00 76.91 A N ANISOU 5658 N THR E 350 11145 6947 11128 2875 582 468 A N ATOM 5659 CA THR E 350 25.385 -22.204 -10.053 1.00 87.54 A C ANISOU 5659 CA THR E 350 12368 8331 12563 3183 444 484 A C ATOM 5660 C THR E 350 25.905 -23.177 -11.102 1.00 85.06 A C ANISOU 5660 C THR E 350 11973 7872 12474 3242 590 497 A C ATOM 5661 O THR E 350 26.640 -24.105 -10.748 1.00 79.43 A O ANISOU 5661 O THR E 350 11258 7134 11787 3514 545 555 A O ATOM 5662 CB THR E 350 24.182 -22.838 -9.344 1.00 83.27 A C ANISOU 5662 CB THR E 350 11500 8010 12128 3274 144 323 A C ATOM 5663 CG2 THR E 350 23.766 -22.000 -8.144 1.00 83.19 A C ANISOU 5663 CG2 THR E 350 11569 8181 11857 3303 -32 296 A C ATOM 5664 OG1 THR E 350 23.082 -22.933 -10.258 1.00 87.74 A O ANISOU 5664 OG1 THR E 350 11817 8579 12940 3048 150 191 A O ATOM 5665 N HIS E 351 25.545 -22.996 -12.371 1.00 88.72 A N ANISOU 5665 N HIS E 351 12364 8259 13085 3016 762 444 A N ATOM 5666 CA HIS E 351 25.965 -23.911 -13.421 1.00 83.24 A C ANISOU 5666 CA HIS E 351 11567 7474 12588 3082 908 446 A C ATOM 5667 C HIS E 351 26.384 -23.130 -14.657 1.00 84.70 A C ANISOU 5667 C HIS E 351 11938 7497 12745 2870 1183 466 A C ATOM 5668 O HIS E 351 26.048 -21.955 -14.825 1.00 81.87 A O ANISOU 5668 O HIS E 351 11709 7123 12273 2629 1245 453 A O ATOM 5669 CB HIS E 351 24.856 -24.906 -13.796 1.00 84.87 A C ANISOU 5669 CB HIS E 351 11355 7823 13070 3066 801 341 A C ATOM 5670 CG HIS E 351 24.388 -25.756 -12.657 1.00 88.95 A C ANISOU 5670 CG HIS E 351 11647 8498 13651 3272 509 286 A C ATOM 5671 CD2 HIS E 351 24.544 -27.078 -12.411 1.00 85.79 A C ANISOU 5671 CD2 HIS E 351 11023 8170 13404 3519 397 272 A C ATOM 5672 ND1 HIS E 351 23.666 -25.252 -11.598 1.00 85.28 A N ANISOU 5672 ND1 HIS E 351 11165 8157 13081 3250 281 219 A N ATOM 5673 CE1 HIS E 351 23.394 -26.226 -10.748 1.00 96.91 A C ANISOU 5673 CE1 HIS E 351 12417 9764 14641 3474 32 157 A C ATOM 5674 NE2 HIS E 351 23.915 -27.345 -11.219 1.00 87.47 A N ANISOU 5674 NE2 HIS E 351 11088 8538 13608 3634 97 192 A N ATOM 5675 N THR E 352 27.131 -23.811 -15.525 1.00 88.64 A N ANISOU 5675 N THR E 352 12442 7892 13344 2983 1340 483 A N ATOM 5676 CA THR E 352 27.509 -23.274 -16.827 1.00 86.41 A C ANISOU 5676 CA THR E 352 12291 7481 13059 2826 1590 468 A C ATOM 5677 C THR E 352 27.610 -24.437 -17.800 1.00 80.74 A C ANISOU 5677 C THR E 352 11349 6798 12528 2962 1690 433 A C ATOM 5678 O THR E 352 28.352 -25.392 -17.549 1.00 99.53 A O ANISOU 5678 O THR E 352 13713 9149 14954 3241 1658 461 A O ATOM 5679 CB THR E 352 28.836 -22.514 -16.765 1.00 95.29 A C ANISOU 5679 CB THR E 352 13818 8374 14014 2849 1708 543 A C ATOM 5680 CG2 THR E 352 29.005 -21.644 -18.003 1.00 73.77 A C ANISOU 5680 CG2 THR E 352 11231 5537 11260 2624 1928 492 A C ATOM 5681 OG1 THR E 352 28.869 -21.686 -15.597 1.00 93.35 A O ANISOU 5681 OG1 THR E 352 13747 8131 13589 2799 1592 619 A O ATOM 5682 N VAL E 353 26.864 -24.360 -18.897 1.00 81.17 A N ANISOU 5682 N VAL E 353 11227 6933 12682 2779 1812 383 A N ATOM 5683 CA VAL E 353 26.879 -25.401 -19.921 1.00 77.84 A C ANISOU 5683 CA VAL E 353 10566 6590 12420 2890 1936 366 A C ATOM 5684 C VAL E 353 27.069 -24.739 -21.281 1.00 76.88 A C ANISOU 5684 C VAL E 353 10559 6415 12238 2740 2183 332 A C ATOM 5685 O VAL E 353 26.718 -23.562 -21.448 1.00 78.32 A O ANISOU 5685 O VAL E 353 10891 6553 12314 2492 2223 314 A O ATOM 5686 CB VAL E 353 25.590 -26.239 -19.892 1.00 85.98 A C ANISOU 5686 CB VAL E 353 11161 7835 13672 2842 1818 361 A C ATOM 5687 CG1 VAL E 353 25.460 -26.982 -18.569 1.00 77.83 A C ANISOU 5687 CG1 VAL E 353 9999 6867 12705 3025 1556 364 A C ATOM 5688 CG2 VAL E 353 24.377 -25.355 -20.137 1.00 73.89 A C ANISOU 5688 CG2 VAL E 353 9558 6358 12159 2520 1802 343 A C ATOM 5689 N PRO E 354 27.622 -25.437 -22.269 1.00 78.42 A N ANISOU 5689 N PRO E 354 10688 6629 12480 2897 2346 311 A N ATOM 5690 CA PRO E 354 27.650 -24.892 -23.629 1.00 79.39 A C ANISOU 5690 CA PRO E 354 10866 6756 12542 2771 2571 263 A C ATOM 5691 C PRO E 354 26.252 -24.871 -24.231 1.00 86.29 A C ANISOU 5691 C PRO E 354 11432 7832 13520 2548 2603 292 A C ATOM 5692 O PRO E 354 25.293 -25.416 -23.680 1.00 89.07 A O ANISOU 5692 O PRO E 354 11502 8310 14031 2503 2455 342 A O ATOM 5693 CB PRO E 354 28.575 -25.849 -24.387 1.00 78.34 A C ANISOU 5693 CB PRO E 354 10697 6635 12436 3062 2705 228 A C ATOM 5694 CG PRO E 354 28.540 -27.116 -23.600 1.00 80.34 A C ANISOU 5694 CG PRO E 354 10713 6981 12831 3291 2557 276 A C ATOM 5695 CD PRO E 354 28.339 -26.720 -22.167 1.00 81.86 A C ANISOU 5695 CD PRO E 354 11014 7089 12999 3229 2330 317 A C ATOM 5696 N PHE E 355 26.144 -24.216 -25.389 1.00 85.60 A N ANISOU 5696 N PHE E 355 11404 7769 13349 2409 2792 260 A N ATOM 5697 CA PHE E 355 24.854 -24.136 -26.066 1.00 83.03 A C ANISOU 5697 CA PHE E 355 10810 7624 13113 2199 2842 311 A C ATOM 5698 C PHE E 355 24.383 -25.513 -26.515 1.00 80.80 A C ANISOU 5698 C PHE E 355 10119 7551 13028 2325 2884 392 A C ATOM 5699 O PHE E 355 23.208 -25.862 -26.347 1.00 96.43 A O ANISOU 5699 O PHE E 355 11797 9651 15190 2188 2791 473 A O ATOM 5700 CB PHE E 355 24.942 -23.177 -27.253 1.00 79.35 A C ANISOU 5700 CB PHE E 355 10504 7157 12490 2064 3043 261 A C ATOM 5701 CG PHE E 355 23.672 -23.076 -28.046 1.00 83.25 A C ANISOU 5701 CG PHE E 355 10739 7835 13058 1866 3114 336 A C ATOM 5702 CD1 PHE E 355 22.570 -22.414 -27.531 1.00 81.41 A C ANISOU 5702 CD1 PHE E 355 10458 7596 12878 1618 2975 369 A C ATOM 5703 CD2 PHE E 355 23.576 -23.648 -29.304 1.00 81.99 A C ANISOU 5703 CD2 PHE E 355 10381 7859 12911 1942 3318 381 A C ATOM 5704 CE1 PHE E 355 21.397 -22.319 -28.257 1.00 85.36 A C ANISOU 5704 CE1 PHE E 355 10731 8237 13465 1438 3030 453 A C ATOM 5705 CE2 PHE E 355 22.406 -23.557 -30.035 1.00101.19 A C ANISOU 5705 CE2 PHE E 355 12576 10458 15413 1760 3390 487 A C ATOM 5706 CZ PHE E 355 21.314 -22.892 -29.510 1.00 82.39 A C ANISOU 5706 CZ PHE E 355 10161 8035 13107 1502 3242 527 A C ATOM 5707 N SER E 356 25.295 -26.319 -27.065 1.00 76.63 A N ANISOU 5707 N SER E 356 9568 7068 12479 2591 3013 369 A N ATOM 5708 CA SER E 356 24.966 -27.666 -27.519 1.00 87.84 A C ANISOU 5708 CA SER E 356 10586 8716 14071 2738 3073 450 A C ATOM 5709 C SER E 356 24.449 -28.562 -26.402 1.00 87.80 A C ANISOU 5709 C SER E 356 10322 8755 14285 2781 2845 506 A C ATOM 5710 O SER E 356 23.906 -29.634 -26.694 1.00 91.41 A O ANISOU 5710 O SER E 356 10385 9414 14933 2833 2866 594 A O ATOM 5711 CB SER E 356 26.195 -28.309 -28.169 1.00 81.41 A C ANISOU 5711 CB SER E 356 9840 7930 13162 3062 3229 383 A C ATOM 5712 OG SER E 356 27.224 -28.522 -27.218 1.00 82.32 A O ANISOU 5712 OG SER E 356 10177 7858 13245 3277 3095 313 A O ATOM 5713 N GLU E 357 24.604 -28.160 -25.141 1.00 87.48 A N ANISOU 5713 N GLU E 357 10509 8212 14518 663 3272 -1826 A N ATOM 5714 CA GLU E 357 24.102 -28.916 -24.001 1.00 83.49 A C ANISOU 5714 CA GLU E 357 9900 7910 13911 917 3016 -1525 A C ATOM 5715 C GLU E 357 23.020 -28.134 -23.262 1.00 82.74 A C ANISOU 5715 C GLU E 357 9805 7778 13854 626 2692 -1514 A C ATOM 5716 O GLU E 357 22.863 -28.268 -22.045 1.00 87.01 A O ANISOU 5716 O GLU E 357 10477 8255 14327 841 2582 -1337 A O ATOM 5717 CB GLU E 357 25.245 -29.289 -23.058 1.00 98.81 A C ANISOU 5717 CB GLU E 357 12169 9558 15818 1411 3320 -1390 A C ATOM 5718 CG GLU E 357 26.384 -30.041 -23.732 1.00101.50 A C ANISOU 5718 CG GLU E 357 12563 9884 16118 1765 3649 -1418 A C ATOM 5719 CD GLU E 357 26.176 -31.540 -23.738 1.00116.81 A C ANISOU 5719 CD GLU E 357 14157 12319 17907 2103 3488 -1136 A C ATOM 5720 OE1 GLU E 357 26.647 -32.205 -24.682 1.00117.68 A O ANISOU 5720 OE1 GLU E 357 14127 12634 17950 2287 3651 -1174 A O ATOM 5721 OE2 GLU E 357 25.534 -32.053 -22.797 1.00116.08 A O1- ANISOU 5721 OE2 GLU E 357 13933 12421 17753 2193 3188 -862 A O1- ATOM 5722 N ILE E 358 22.259 -27.320 -24.002 1.00 88.68 A N ANISOU 5722 N ILE E 358 10417 8576 14699 153 2531 -1706 A N ATOM 5723 CA ILE E 358 21.267 -26.434 -23.396 1.00 90.03 A C ANISOU 5723 CA ILE E 358 10615 8677 14915 -116 2255 -1741 A C ATOM 5724 C ILE E 358 20.255 -27.215 -22.568 1.00 87.51 A C ANISOU 5724 C ILE E 358 10126 8660 14463 7 1775 -1499 A C ATOM 5725 O ILE E 358 19.781 -26.728 -21.531 1.00 80.18 A O ANISOU 5725 O ILE E 358 9374 7594 13496 50 1623 -1464 A O ATOM 5726 CB ILE E 358 20.581 -25.592 -24.493 1.00 82.84 A C ANISOU 5726 CB ILE E 358 9520 7822 14133 -645 2124 -1969 A C ATOM 5727 CG1 ILE E 358 19.689 -24.511 -23.878 1.00 73.30 A C ANISOU 5727 CG1 ILE E 358 8384 6478 12988 -889 1909 -2035 A C ATOM 5728 CG2 ILE E 358 19.795 -26.476 -25.458 1.00 86.27 A C ANISOU 5728 CG2 ILE E 358 9512 8753 14515 -822 1774 -1904 A C ATOM 5729 CD1 ILE E 358 19.595 -23.253 -24.721 1.00 83.07 A C ANISOU 5729 CD1 ILE E 358 9623 7570 14368 -1321 2008 -2260 A C ATOM 5730 N ASN E 359 19.927 -28.442 -22.985 1.00 84.40 A N ANISOU 5730 N ASN E 359 9401 8683 13986 84 1521 -1311 A N ATOM 5731 CA ASN E 359 18.928 -29.220 -22.261 1.00 77.98 A C ANISOU 5731 CA ASN E 359 8416 8152 13062 152 992 -1050 A C ATOM 5732 C ASN E 359 19.380 -29.540 -20.844 1.00 83.99 A C ANISOU 5732 C ASN E 359 9478 8726 13710 589 1060 -871 A C ATOM 5733 O ASN E 359 18.538 -29.702 -19.951 1.00 78.27 A O ANISOU 5733 O ASN E 359 8786 8059 12892 625 638 -735 A O ATOM 5734 CB ASN E 359 18.601 -30.502 -23.024 1.00 75.88 A C ANISOU 5734 CB ASN E 359 7698 8391 12741 146 735 -821 A C ATOM 5735 CG ASN E 359 17.571 -30.280 -24.110 1.00 94.98 A C ANISOU 5735 CG ASN E 359 9759 11094 15233 -349 389 -901 A C ATOM 5736 ND2 ASN E 359 17.996 -30.404 -25.363 1.00 81.93 A N ANISOU 5736 ND2 ASN E 359 7904 9615 13610 -464 635 -997 A N ATOM 5737 OD1 ASN E 359 16.407 -29.999 -23.829 1.00100.96 A O ANISOU 5737 OD1 ASN E 359 10441 11909 16011 -615 -105 -880 A O ATOM 5738 N LYS E 360 20.695 -29.625 -20.612 1.00 83.15 A N ANISOU 5738 N LYS E 360 9614 8376 13602 924 1562 -869 A N ATOM 5739 CA LYS E 360 21.183 -29.808 -19.249 1.00 83.36 A C ANISOU 5739 CA LYS E 360 9952 8192 13528 1321 1658 -702 A C ATOM 5740 C LYS E 360 20.674 -28.703 -18.333 1.00 84.81 A C ANISOU 5740 C LYS E 360 10416 8122 13688 1225 1573 -807 A C ATOM 5741 O LYS E 360 20.298 -28.966 -17.184 1.00 78.02 A O ANISOU 5741 O LYS E 360 9698 7263 12682 1442 1333 -641 A O ATOM 5742 CB LYS E 360 22.711 -29.863 -19.225 1.00 80.24 A C ANISOU 5742 CB LYS E 360 9804 7511 13172 1642 2226 -718 A C ATOM 5743 CG LYS E 360 23.266 -31.277 -19.158 1.00 80.62 A C ANISOU 5743 CG LYS E 360 9715 7780 13137 2040 2252 -452 A C ATOM 5744 CD LYS E 360 24.618 -31.385 -19.840 1.00 99.98 A C ANISOU 5744 CD LYS E 360 12283 10044 15660 2247 2764 -558 A C ATOM 5745 CE LYS E 360 25.142 -32.814 -19.797 1.00102.99 A C ANISOU 5745 CE LYS E 360 12499 10679 15953 2683 2796 -284 A C ATOM 5746 NZ LYS E 360 26.103 -33.035 -18.679 1.00 98.21 A N1+ ANISOU 5746 NZ LYS E 360 12230 9768 15317 3113 3032 -128 A N1+ ATOM 5747 N ALA E 361 20.634 -27.462 -18.831 1.00 89.20 A N ANISOU 5747 N ALA E 361 11047 8472 14372 912 1758 -1071 A N ATOM 5748 CA ALA E 361 20.044 -26.375 -18.057 1.00 82.53 A C ANISOU 5748 CA ALA E 361 10412 7448 13499 820 1671 -1163 A C ATOM 5749 C ALA E 361 18.618 -26.717 -17.647 1.00 84.53 A C ANISOU 5749 C ALA E 361 10531 7957 13630 744 1043 -1093 A C ATOM 5750 O ALA E 361 18.243 -26.563 -16.478 1.00 90.88 A O ANISOU 5750 O ALA E 361 11567 8686 14277 956 878 -1020 A O ATOM 5751 CB ALA E 361 20.082 -25.074 -18.860 1.00 61.21 A C ANISOU 5751 CB ALA E 361 7715 4561 10981 437 1899 -1429 A C ATOM 5752 N PHE E 362 17.815 -27.208 -18.597 1.00 82.91 A N ANISOU 5752 N PHE E 362 9964 8055 13483 449 664 -1101 A N ATOM 5753 CA PHE E 362 16.461 -27.645 -18.274 1.00 79.51 A C ANISOU 5753 CA PHE E 362 9397 7857 12957 352 -7 -1001 A C ATOM 5754 C PHE E 362 16.476 -28.687 -17.165 1.00 87.12 A C ANISOU 5754 C PHE E 362 10475 8897 13730 742 -245 -713 A C ATOM 5755 O PHE E 362 15.623 -28.669 -16.271 1.00 83.96 A O ANISOU 5755 O PHE E 362 10232 8483 13188 818 -680 -664 A O ATOM 5756 CB PHE E 362 15.777 -28.206 -19.521 1.00 75.00 A C ANISOU 5756 CB PHE E 362 8375 7635 12488 -12 -354 -974 A C ATOM 5757 CG PHE E 362 15.321 -27.156 -20.493 1.00 86.16 A C ANISOU 5757 CG PHE E 362 9670 9003 14065 -458 -333 -1248 A C ATOM 5758 CD1 PHE E 362 16.237 -26.482 -21.285 1.00 62.63 A C ANISOU 5758 CD1 PHE E 362 6719 5857 11219 -574 212 -1441 A C ATOM 5759 CD2 PHE E 362 13.977 -26.848 -20.620 1.00 81.43 A C ANISOU 5759 CD2 PHE E 362 8943 8508 13491 -767 -891 -1306 A C ATOM 5760 CE1 PHE E 362 15.821 -25.518 -22.182 1.00 63.77 A C ANISOU 5760 CE1 PHE E 362 6753 5958 11519 -1001 213 -1675 A C ATOM 5761 CE2 PHE E 362 13.553 -25.884 -21.517 1.00 64.90 A C ANISOU 5761 CE2 PHE E 362 6728 6373 11558 -1180 -881 -1544 A C ATOM 5762 CZ PHE E 362 14.477 -25.218 -22.299 1.00 75.15 A C ANISOU 5762 CZ PHE E 362 8041 7525 12990 -1304 -323 -1723 A C ATOM 5763 N ASP E 363 17.452 -29.596 -17.197 1.00 84.81 A N ANISOU 5763 N ASP E 363 10128 8671 13423 1009 28 -522 A N ATOM 5764 CA ASP E 363 17.551 -30.616 -16.162 1.00 84.30 A C ANISOU 5764 CA ASP E 363 10159 8678 13192 1379 -178 -219 A C ATOM 5765 C ASP E 363 18.105 -30.055 -14.859 1.00100.03 A C ANISOU 5765 C ASP E 363 12616 10339 15054 1717 95 -235 A C ATOM 5766 O ASP E 363 17.837 -30.613 -13.789 1.00100.67 A O ANISOU 5766 O ASP E 363 12858 10438 14953 1977 -201 -35 A O ATOM 5767 CB ASP E 363 18.422 -31.773 -16.648 1.00 95.12 A C ANISOU 5767 CB ASP E 363 11295 10248 14597 1576 38 6 A C ATOM 5768 CG ASP E 363 17.827 -32.485 -17.844 1.00 89.64 A C ANISOU 5768 CG ASP E 363 10105 9969 13986 1290 -266 100 A C ATOM 5769 OD1 ASP E 363 16.824 -31.984 -18.394 1.00 96.82 A O ANISOU 5769 OD1 ASP E 363 10862 10970 14957 895 -602 -39 A O ATOM 5770 OD2 ASP E 363 18.365 -33.540 -18.238 1.00 90.12 A O1- ANISOU 5770 OD2 ASP E 363 9917 10279 14045 1471 -165 329 A O1- ATOM 5771 N TYR E 364 18.878 -28.965 -14.921 1.00101.36 A N ANISOU 5771 N TYR E 364 12999 10211 15303 1711 640 -445 A N ATOM 5772 CA TYR E 364 19.389 -28.379 -13.686 1.00 95.52 A C ANISOU 5772 CA TYR E 364 12670 9191 14431 2017 907 -423 A C ATOM 5773 C TYR E 364 18.304 -27.604 -12.953 1.00 99.22 A C ANISOU 5773 C TYR E 364 13325 9622 14753 1970 574 -534 A C ATOM 5774 O TYR E 364 18.291 -27.576 -11.716 1.00 97.65 A O ANISOU 5774 O TYR E 364 13432 9333 14338 2286 525 -431 A O ATOM 5775 CB TYR E 364 20.601 -27.498 -13.978 1.00 85.75 A C ANISOU 5775 CB TYR E 364 11585 7656 13340 2014 1570 -551 A C ATOM 5776 CG TYR E 364 21.851 -28.294 -14.273 1.00 94.44 A C ANISOU 5776 CG TYR E 364 12659 8706 14517 2232 1922 -416 A C ATOM 5777 CD1 TYR E 364 22.289 -29.281 -13.399 1.00 95.04 A C ANISOU 5777 CD1 TYR E 364 12838 8815 14457 2627 1882 -142 A C ATOM 5778 CD2 TYR E 364 22.598 -28.055 -15.418 1.00 91.68 A C ANISOU 5778 CD2 TYR E 364 12205 8262 14366 2062 2279 -566 A C ATOM 5779 CE1 TYR E 364 23.433 -30.012 -13.661 1.00 86.01 A C ANISOU 5779 CE1 TYR E 364 11676 7619 13386 2862 2200 -20 A C ATOM 5780 CE2 TYR E 364 23.742 -28.780 -15.688 1.00 89.37 A C ANISOU 5780 CE2 TYR E 364 11926 7904 14127 2308 2588 -466 A C ATOM 5781 CZ TYR E 364 24.156 -29.756 -14.807 1.00 97.28 A C ANISOU 5781 CZ TYR E 364 13013 8945 15002 2716 2554 -192 A C ATOM 5782 OH TYR E 364 25.296 -30.478 -15.075 1.00112.59 A O ANISOU 5782 OH TYR E 364 14968 10814 16998 2993 2860 -94 A O ATOM 5783 N MET E 365 17.380 -26.989 -13.690 1.00 96.83 A N ANISOU 5783 N MET E 365 12852 9393 14548 1600 333 -743 A N ATOM 5784 CA MET E 365 16.099 -26.601 -13.116 1.00 97.59 A C ANISOU 5784 CA MET E 365 13064 9523 14493 1564 -171 -827 A C ATOM 5785 C MET E 365 15.277 -27.874 -12.950 1.00100.03 A C ANISOU 5785 C MET E 365 13237 10071 14697 1589 -843 -624 A C ATOM 5786 O MET E 365 15.848 -28.969 -12.908 1.00112.94 A O ANISOU 5786 O MET E 365 14767 11820 16324 1750 -823 -377 A O ATOM 5787 CB MET E 365 15.388 -25.572 -13.999 1.00 91.72 A C ANISOU 5787 CB MET E 365 12165 8772 13912 1156 -235 -1099 A C ATOM 5788 CG MET E 365 14.419 -24.658 -13.253 1.00105.94 A C ANISOU 5788 CG MET E 365 14208 10487 15558 1216 -491 -1252 A C ATOM 5789 SD MET E 365 14.446 -22.954 -13.841 1.00107.59 A S ANISOU 5789 SD MET E 365 14393 10536 15948 941 -76 -1530 A S ATOM 5790 CE MET E 365 15.420 -22.168 -12.559 1.00103.37 A C ANISOU 5790 CE MET E 365 14256 9784 15236 1378 517 -1453 A C ATOM 5791 N LEU E 366 13.951 -27.762 -12.849 1.00 87.71 A N ANISOU 5791 N LEU E 366 11095 10079 12153 2360 918 129 A N ATOM 5792 CA LEU E 366 13.090 -28.933 -12.686 1.00103.77 A C ANISOU 5792 CA LEU E 366 12858 12218 14353 2405 697 48 A C ATOM 5793 C LEU E 366 13.453 -29.724 -11.431 1.00100.96 A C ANISOU 5793 C LEU E 366 12780 11712 13871 2573 363 -27 A C ATOM 5794 O LEU E 366 12.606 -29.938 -10.559 1.00101.96 A O ANISOU 5794 O LEU E 366 12989 11782 13969 2524 230 -63 A O ATOM 5795 CB LEU E 366 13.165 -29.835 -13.923 1.00 80.51 A C ANISOU 5795 CB LEU E 366 9449 9506 11635 2467 677 9 A C ATOM 5796 CG LEU E 366 12.648 -29.245 -15.235 1.00 85.87 A C ANISOU 5796 CG LEU E 366 9789 10391 12447 2282 967 92 A C ATOM 5797 CD1 LEU E 366 12.732 -30.268 -16.357 1.00 69.41 A C ANISOU 5797 CD1 LEU E 366 7270 8547 10557 2359 934 41 A C ATOM 5798 CD2 LEU E 366 11.223 -28.755 -15.063 1.00 57.40 A C ANISOU 5798 CD2 LEU E 366 6048 6809 8953 2080 1073 171 A C ATOM 5799 N LYS E 367 14.705 -30.175 -11.340 1.00 92.77 A N ANISOU 5799 N LYS E 367 11880 10605 12764 2762 218 -50 A N ATOM 5800 CA LYS E 367 15.221 -30.842 -10.152 1.00 96.25 A C ANISOU 5800 CA LYS E 367 12607 10893 13071 2918 -107 -78 A C ATOM 5801 C LYS E 367 15.563 -29.873 -9.027 1.00107.24 A C ANISOU 5801 C LYS E 367 14523 12075 14149 2877 -65 -17 A C ATOM 5802 O LYS E 367 16.027 -30.318 -7.971 1.00104.21 A O ANISOU 5802 O LYS E 367 14422 11565 13607 2987 -332 -15 A O ATOM 5803 CB LYS E 367 16.462 -31.665 -10.509 1.00 95.61 A C ANISOU 5803 CB LYS E 367 12450 10799 13080 3140 -260 -101 A C ATOM 5804 CG LYS E 367 16.190 -33.144 -10.723 1.00 90.34 A C ANISOU 5804 CG LYS E 367 11414 10245 12666 3265 -525 -164 A C ATOM 5805 CD LYS E 367 17.150 -33.740 -11.739 1.00 89.54 A C ANISOU 5805 CD LYS E 367 11057 10206 12758 3426 -482 -201 A C ATOM 5806 CE LYS E 367 17.855 -34.963 -11.179 1.00 87.88 A C ANISOU 5806 CE LYS E 367 10834 9897 12659 3655 -831 -207 A C ATOM 5807 NZ LYS E 367 18.533 -35.749 -12.246 1.00 97.57 A N1+ ANISOU 5807 NZ LYS E 367 11712 11204 14156 3813 -775 -265 A N1+ ATOM 5808 N GLY E 368 15.355 -28.573 -9.225 1.00105.37 A N ANISOU 5808 N GLY E 368 14413 11798 13826 2718 260 52 A N ATOM 5809 CA GLY E 368 15.639 -27.599 -8.185 1.00104.02 A C ANISOU 5809 CA GLY E 368 14726 11426 13371 2674 343 123 A C ATOM 5810 C GLY E 368 17.095 -27.523 -7.787 1.00110.51 A C ANISOU 5810 C GLY E 368 15857 12098 14035 2833 247 182 A C ATOM 5811 O GLY E 368 17.402 -27.148 -6.651 1.00118.12 A O ANISOU 5811 O GLY E 368 17238 12900 14741 2851 185 237 A O ATOM 5812 N GLU E 369 18.005 -27.871 -8.696 1.00 96.04 A N ANISOU 5812 N GLU E 369 13830 10311 12351 2948 241 172 A N ATOM 5813 CA GLU E 369 19.428 -27.874 -8.385 1.00110.54 A C ANISOU 5813 CA GLU E 369 15917 11987 14095 3111 143 224 A C ATOM 5814 C GLU E 369 20.112 -26.554 -8.710 1.00 94.60 A C ANISOU 5814 C GLU E 369 14096 9856 11993 3037 436 322 A C ATOM 5815 O GLU E 369 21.112 -26.211 -8.069 1.00 89.84 A O ANISOU 5815 O GLU E 369 13825 9066 11245 3126 387 406 A O ATOM 5816 CB GLU E 369 20.132 -29.003 -9.142 1.00105.82 A C ANISOU 5816 CB GLU E 369 15016 11461 13731 3291 -19 144 A C ATOM 5817 CG GLU E 369 20.442 -30.226 -8.297 1.00107.19 A C ANISOU 5817 CG GLU E 369 15232 11578 13919 3472 -411 133 A C ATOM 5818 CD GLU E 369 20.646 -31.475 -9.133 1.00108.53 A C ANISOU 5818 CD GLU E 369 14978 11863 14394 3617 -544 41 A C ATOM 5819 OE1 GLU E 369 20.384 -31.425 -10.352 1.00107.58 A O ANISOU 5819 OE1 GLU E 369 14531 11899 14444 3561 -325 -32 A O ATOM 5820 OE2 GLU E 369 21.071 -32.506 -8.570 1.00101.63 A O1- ANISOU 5820 OE2 GLU E 369 14096 10926 13594 3784 -862 54 A O1- ATOM 5821 N SER E 370 19.602 -25.806 -9.683 1.00 86.20 A N ANISOU 5821 N SER E 370 12827 8897 11027 2869 725 332 A N ATOM 5822 CA SER E 370 20.259 -24.605 -10.174 1.00 85.48 A C ANISOU 5822 CA SER E 370 12861 8716 10902 2784 988 429 A C ATOM 5823 C SER E 370 19.476 -23.360 -9.783 1.00 97.53 A C ANISOU 5823 C SER E 370 14552 10181 12325 2583 1239 550 A C ATOM 5824 O SER E 370 18.242 -23.375 -9.745 1.00 95.55 A O ANISOU 5824 O SER E 370 14147 10033 12126 2461 1299 530 A O ATOM 5825 CB SER E 370 20.412 -24.648 -11.697 1.00 87.24 A C ANISOU 5825 CB SER E 370 12719 9108 11320 2730 1128 369 A C ATOM 5826 OG SER E 370 19.160 -24.470 -12.338 1.00 80.07 A O ANISOU 5826 OG SER E 370 11506 8395 10521 2547 1278 372 A O ATOM 5827 N ILE E 371 20.206 -22.286 -9.491 1.00 92.17 A N ANISOU 5827 N ILE E 371 14174 9317 11528 2553 1392 682 A N ATOM 5828 CA ILE E 371 19.616 -20.959 -9.362 1.00 79.12 A C ANISOU 5828 CA ILE E 371 12632 7592 9837 2357 1689 824 A C ATOM 5829 C ILE E 371 19.529 -20.374 -10.765 1.00 76.74 A C ANISOU 5829 C ILE E 371 12018 7413 9726 2201 1901 866 A C ATOM 5830 O ILE E 371 18.435 -20.134 -11.287 1.00 84.12 A O ANISOU 5830 O ILE E 371 12688 8485 10790 2035 2046 887 A O ATOM 5831 CB ILE E 371 20.440 -20.057 -8.425 1.00 78.68 A C ANISOU 5831 CB ILE E 371 13025 7282 9587 2390 1765 973 A C ATOM 5832 CG1 ILE E 371 20.393 -20.589 -6.992 1.00 79.67 A C ANISOU 5832 CG1 ILE E 371 13473 7315 9482 2509 1562 948 A C ATOM 5833 CG2 ILE E 371 19.923 -18.623 -8.477 1.00 76.24 A C ANISOU 5833 CG2 ILE E 371 12779 6890 9299 2186 2109 1139 A C ATOM 5834 CD1 ILE E 371 21.052 -19.676 -5.981 1.00 69.41 A C ANISOU 5834 CD1 ILE E 371 12624 5784 7966 2527 1661 1113 A C ATOM 5835 N ARG E 372 20.687 -20.155 -11.386 1.00 85.70 A N ANISOU 5835 N ARG E 372 13180 8498 10884 2247 1909 880 A N ATOM 5836 CA ARG E 372 20.773 -19.737 -12.777 1.00 81.05 A C ANISOU 5836 CA ARG E 372 12310 8043 10441 2104 2061 893 A C ATOM 5837 C ARG E 372 21.899 -20.506 -13.450 1.00 85.52 A C ANISOU 5837 C ARG E 372 12800 8645 11049 2255 1915 747 A C ATOM 5838 O ARG E 372 22.952 -20.733 -12.848 1.00 75.88 A O ANISOU 5838 O ARG E 372 11835 7241 9755 2430 1781 727 A O ATOM 5839 CB ARG E 372 21.016 -18.227 -12.902 1.00 68.62 A C ANISOU 5839 CB ARG E 372 10887 6325 8860 1931 2309 1098 A C ATOM 5840 CG ARG E 372 19.753 -17.391 -12.800 1.00 73.42 A C ANISOU 5840 CG ARG E 372 11403 6960 9534 1721 2531 1246 A C ATOM 5841 CD ARG E 372 18.826 -17.658 -13.976 1.00 71.55 A C ANISOU 5841 CD ARG E 372 10713 6999 9473 1567 2586 1215 A C ATOM 5842 NE ARG E 372 17.623 -16.837 -13.930 1.00 74.93 A N ANISOU 5842 NE ARG E 372 11018 7434 10017 1361 2804 1378 A N ATOM 5843 CZ ARG E 372 16.587 -17.070 -13.136 1.00 76.00 A C ANISOU 5843 CZ ARG E 372 11161 7550 10166 1367 2817 1355 A C ATOM 5844 NH1 ARG E 372 16.572 -18.098 -12.303 1.00 80.11 A N1+ ANISOU 5844 NH1 ARG E 372 11813 8056 10567 1553 2604 1184 A N1+ ATOM 5845 NH2 ARG E 372 15.539 -16.252 -13.179 1.00 79.11 A N ANISOU 5845 NH2 ARG E 372 11422 7927 10710 1173 3046 1509 A N ATOM 5846 N CYS E 373 21.671 -20.909 -14.698 1.00 71.75 A N ANISOU 5846 N CYS E 373 10698 7133 9430 2185 1951 649 A N ATOM 5847 CA CYS E 373 22.645 -21.674 -15.471 1.00 68.71 A C ANISOU 5847 CA CYS E 373 10202 6802 9103 2316 1856 480 A C ATOM 5848 C CYS E 373 22.995 -20.890 -16.729 1.00 71.70 A C ANISOU 5848 C CYS E 373 10463 7266 9515 2128 2042 499 A C ATOM 5849 O CYS E 373 22.146 -20.710 -17.610 1.00 73.71 A O ANISOU 5849 O CYS E 373 10426 7753 9826 1938 2163 529 A O ATOM 5850 CB CYS E 373 22.104 -23.060 -15.824 1.00 63.09 A C ANISOU 5850 CB CYS E 373 9166 6309 8495 2423 1716 316 A C ATOM 5851 SG CYS E 373 23.148 -23.985 -16.974 1.00 84.38 A S ANISOU 5851 SG CYS E 373 11660 9103 11297 2559 1675 94 A S ATOM 5852 N ILE E 374 24.246 -20.434 -16.813 1.00 74.80 A N ANISOU 5852 N ILE E 374 11078 7469 9874 2173 2053 490 A N ATOM 5853 CA ILE E 374 24.691 -19.672 -17.972 1.00 76.71 A C ANISOU 5853 CA ILE E 374 11247 7770 10129 1986 2204 496 A C ATOM 5854 C ILE E 374 24.909 -20.612 -19.149 1.00 73.46 A C ANISOU 5854 C ILE E 374 10550 7587 9773 2021 2185 264 A C ATOM 5855 O ILE E 374 25.556 -21.659 -19.018 1.00 78.41 A O ANISOU 5855 O ILE E 374 11178 8166 10448 2255 2054 81 A O ATOM 5856 CB ILE E 374 25.969 -18.889 -17.641 1.00 71.03 A C ANISOU 5856 CB ILE E 374 10862 6750 9375 2021 2212 555 A C ATOM 5857 CG1 ILE E 374 25.732 -17.961 -16.447 1.00 69.00 A C ANISOU 5857 CG1 ILE E 374 10886 6273 9057 1991 2257 799 A C ATOM 5858 CG2 ILE E 374 26.444 -18.100 -18.852 1.00 63.90 A C ANISOU 5858 CG2 ILE E 374 9894 5903 8483 1808 2344 550 A C ATOM 5859 CD1 ILE E 374 24.526 -17.058 -16.605 1.00 65.73 A C ANISOU 5859 CD1 ILE E 374 10347 5972 8655 1737 2435 995 A C ATOM 5860 N ILE E 375 24.363 -20.244 -20.306 1.00 72.35 A N ANISOU 5860 N ILE E 375 10159 7697 9633 1784 2323 283 A N ATOM 5861 CA ILE E 375 24.535 -20.991 -21.547 1.00 71.86 A C ANISOU 5861 CA ILE E 375 9831 7883 9588 1773 2351 75 A C ATOM 5862 C ILE E 375 25.441 -20.181 -22.463 1.00 76.35 A C ANISOU 5862 C ILE E 375 10497 8423 10091 1609 2453 36 A C ATOM 5863 O ILE E 375 25.200 -18.989 -22.688 1.00 75.96 A O ANISOU 5863 O ILE E 375 10496 8367 10000 1360 2550 235 A O ATOM 5864 CB ILE E 375 23.183 -21.285 -22.221 1.00 70.92 A C ANISOU 5864 CB ILE E 375 9331 8112 9503 1615 2417 127 A C ATOM 5865 CG1 ILE E 375 22.284 -22.093 -21.282 1.00 67.30 A C ANISOU 5865 CG1 ILE E 375 8784 7662 9127 1770 2299 152 A C ATOM 5866 CG2 ILE E 375 23.387 -22.022 -23.531 1.00 64.23 A C ANISOU 5866 CG2 ILE E 375 8220 7537 8646 1593 2470 -79 A C ATOM 5867 CD1 ILE E 375 20.823 -21.704 -21.351 1.00 68.75 A C ANISOU 5867 CD1 ILE E 375 8737 8023 9362 1566 2378 344 A C ATOM 5868 N THR E 376 26.479 -20.826 -22.988 1.00 79.83 A N ANISOU 5868 N THR E 376 10961 8833 10538 1744 2432 -219 A N ATOM 5869 CA THR E 376 27.492 -20.161 -23.799 1.00 79.80 A C ANISOU 5869 CA THR E 376 11088 8761 10473 1614 2509 -309 A C ATOM 5870 C THR E 376 27.264 -20.487 -25.270 1.00 72.76 A C ANISOU 5870 C THR E 376 9923 8219 9506 1447 2619 -469 A C ATOM 5871 O THR E 376 27.273 -21.660 -25.658 1.00 67.43 A O ANISOU 5871 O THR E 376 9060 7692 8868 1604 2619 -688 A O ATOM 5872 CB THR E 376 28.896 -20.590 -23.371 1.00 73.75 A C ANISOU 5872 CB THR E 376 10560 7683 9777 1872 2428 -498 A C ATOM 5873 CG2 THR E 376 29.950 -19.768 -24.099 1.00 63.88 A C ANISOU 5873 CG2 THR E 376 9481 6313 8479 1721 2500 -580 A C ATOM 5874 OG1 THR E 376 29.043 -20.412 -21.957 1.00 65.81 A O ANISOU 5874 OG1 THR E 376 9794 6386 8825 2037 2311 -332 A O ATOM 5875 N MET E 377 27.067 -19.452 -26.082 1.00 60.41 A N ANISOU 5875 N MET E 377 8332 6787 7836 1124 2713 -348 A N ATOM 5876 CA MET E 377 26.947 -19.644 -27.517 1.00 67.33 A C ANISOU 5876 CA MET E 377 8988 8001 8592 929 2815 -489 A C ATOM 5877 C MET E 377 28.310 -19.980 -28.122 1.00 72.88 A C ANISOU 5877 C MET E 377 9843 8599 9250 1015 2844 -821 A C ATOM 5878 O MET E 377 29.360 -19.834 -27.488 1.00 87.93 A O ANISOU 5878 O MET E 377 12027 10152 11232 1178 2783 -896 A O ATOM 5879 CB MET E 377 26.368 -18.395 -28.180 1.00 63.59 A C ANISOU 5879 CB MET E 377 8450 7692 8020 538 2879 -232 A C ATOM 5880 CG MET E 377 25.107 -17.861 -27.520 1.00 75.44 A C ANISOU 5880 CG MET E 377 9830 9224 9611 441 2874 116 A C ATOM 5881 SD MET E 377 23.927 -19.149 -27.088 1.00 82.75 A S ANISOU 5881 SD MET E 377 10453 10343 10645 644 2846 95 A S ATOM 5882 CE MET E 377 22.821 -19.049 -28.492 1.00 78.60 A C ANISOU 5882 CE MET E 377 9516 10303 10045 310 2951 216 A C ATOM 5883 N GLY E 378 28.284 -20.437 -29.370 1.00 76.98 A N ANISOU 5883 N GLY E 378 10175 9427 9647 899 2949 -1022 A N ATOM 5884 CA GLY E 378 29.502 -20.774 -30.077 1.00 78.29 A C ANISOU 5884 CA GLY E 378 10466 9521 9758 955 3014 -1372 A C ATOM 5885 C GLY E 378 30.132 -22.093 -29.695 1.00 87.42 A C ANISOU 5885 C GLY E 378 11613 10527 11076 1337 3007 -1651 A C ATOM 5886 O GLY E 378 31.278 -22.346 -30.081 1.00 95.96 A O ANISOU 5886 O GLY E 378 12836 11451 12172 1427 3062 -1946 A O ATOM 5887 N ALA E 379 29.428 -22.942 -28.953 1.00 91.36 A N ANISOU 5887 N ALA E 379 11942 11055 11717 1558 2938 -1567 A N ATOM 5888 CA ALA E 379 29.962 -24.241 -28.563 1.00 87.73 A C ANISOU 5888 CA ALA E 379 11434 10455 11445 1919 2910 -1793 A C ATOM 5889 C ALA E 379 28.833 -25.218 -28.258 1.00 98.19 A C ANISOU 5889 C ALA E 379 12447 11994 12865 2047 2866 -1701 A C ATOM 5890 O ALA E 379 29.063 -26.329 -27.780 1.00 90.36 A O ANISOU 5890 O ALA E 379 11375 10895 12063 2348 2806 -1817 A O ATOM 5891 CB ALA E 379 30.885 -24.100 -27.362 1.00 86.41 A C ANISOU 5891 CB ALA E 379 11561 9831 11440 2151 2768 -1760 A C ATOM 5892 OXT ALA E 379 27.662 -24.914 -28.481 1.00 89.50 A O1- ANISOU 5892 OXT ALA E 379 11157 11168 11679 1847 2882 -1497 A O1- TER HETATM 5893 ZN ZN E 400 5.564 2.848 -23.056 0.93 70.81 A Zn2+ HETATM 5894 ZN ZN E 401 13.411 -15.077 -16.277 0.89 74.86 A Zn2+ HETATM 5895 O HOH F 5 11.787 -17.297 -7.572 1.00 68.41 A O HETATM 5896 O HOH F 8 9.512 -1.951 -41.658 1.00 63.30 A O CONECT 2902 2906 CONECT 2903 2906 CONECT 2904 2906 CONECT 2905 2906 CONECT 2906 2902 2903 2904 2905 CONECT 2907 2911 CONECT 2908 2911 CONECT 2909 2911 CONECT 2910 2911 CONECT 2911 2907 2908 2909 2910 CONECT 2912 2916 CONECT 2913 2916 CONECT 2914 2916 CONECT 2915 2916 CONECT 2916 2912 2913 2914 2915 CONECT 2917 2921 CONECT 2918 2921 CONECT 2919 2921 CONECT 2920 2921 CONECT 2921 2917 2918 2919 2920 CONECT 2922 2926 CONECT 2923 2926 CONECT 2924 2926 CONECT 2925 2926 CONECT 2926 2922 2923 2924 2925 CONECT 2927 2931 CONECT 2928 2931 CONECT 2929 2931 CONECT 2930 2931 CONECT 2931 2927 2928 2929 2930 CONECT 2932 2936 CONECT 2933 2936 CONECT 2934 2936 CONECT 2935 2936 CONECT 2936 2932 2933 2934 2935 CONECT 2937 2941 CONECT 2938 2941 CONECT 2939 2941 CONECT 2940 2941 CONECT 2941 2937 2938 2939 2940 CONECT 2942 2946 CONECT 2943 2946 CONECT 2944 2946 CONECT 2945 2946 CONECT 2946 2942 2943 2944 2945 CONECT 2949 2953 CONECT 2950 2953 CONECT 2951 2953 CONECT 2952 2953 CONECT 2953 2949 2950 2951 2952 CONECT 2954 2958 CONECT 2955 2958 CONECT 2956 2958 CONECT 2957 2958 CONECT 2958 2954 2955 2956 2957 CONECT 2959 2963 CONECT 2960 2963 CONECT 2961 2963 CONECT 2962 2963 CONECT 2963 2959 2960 2961 2962 CONECT 2964 2968 CONECT 2965 2968 CONECT 2966 2968 CONECT 2967 2968 CONECT 2968 2964 2965 2966 2967 CONECT 2969 2973 CONECT 2970 2973 CONECT 2971 2973 CONECT 2972 2973 CONECT 2973 2969 2970 2971 2972 CONECT 2974 2978 CONECT 2975 2978 CONECT 2976 2978 CONECT 2977 2978 CONECT 2978 2974 2975 2976 2977 CONECT 2979 2983 CONECT 2980 2983 CONECT 2981 2983 CONECT 2982 2983 CONECT 2983 2979 2980 2981 2982 CONECT 2984 2988 CONECT 2985 2988 CONECT 2986 2988 CONECT 2987 2988 CONECT 2988 2984 2985 2986 2987 CONECT 2989 2993 CONECT 2990 2993 CONECT 2991 2993 CONECT 2992 2993 CONECT 2993 2989 2990 2991 2992 END If you find results from this site helpful for your research, please cite one of our papers:
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